data_9H8L
# 
_entry.id   9H8L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H8L         pdb_00009h8l 10.2210/pdb9h8l/pdb 
WWPDB D_1292142458 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-05 ? 
2 'Structure model' 1 1 2025-02-12 ? 
3 'Structure model' 1 2 2025-03-12 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.title'                   
2 2 'Structure model' '_citation_author.identifier_ORCID' 
3 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H8L 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_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                 3 
_pdbx_contact_author.email              jennifer.andexer@pharmazie.uni-freiburg.de 
_pdbx_contact_author.name_first         Jennifer 
_pdbx_contact_author.name_last          Andexer 
_pdbx_contact_author.name_mi            N. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8238-5749 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Friedrich, F.' 1 0000-0001-5420-6184 
'Kuge, M.'      2 0000-0002-9052-2819 
'Keppler, M.'   3 0000-0002-6579-6885 
'Gerhardt, S.'  4 0000-0002-9098-8475 
'Einsle, O.'    5 0000-0001-8722-2893 
'Andexer, J.N.' 6 0000-0001-8238-5749 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chembiochem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1439-7633 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            26 
_citation.language                  ? 
_citation.page_first                e202400970 
_citation.page_last                 e202400970 
_citation.title                     
'Structural Insights into Broad-Range Polyphosphate Kinase 2-II Enzymes Applicable for Pyrimidine Nucleoside Diphosphate Synthesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cbic.202400970 
_citation.pdbx_database_id_PubMed   39846220 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kuge, M.'          1  0000-0002-9052-2819 
primary 'Keppler, M.'       2  0000-0002-6579-6885 
primary 'Friedrich, F.'     3  0000-0001-5420-6184 
primary 'Saleem-Batcha, R.' 4  0000-0003-3361-823X 
primary 'Winter, J.'        5  ?                   
primary 'Prucker, I.'       6  0000-0002-5794-6759 
primary 'Germer, P.'        7  0000-0001-9733-3773 
primary 'Gerhardt, S.'      8  0000-0002-9098-8475 
primary 'Einsle, O.'        9  0000-0001-8722-2893 
primary 'Jung, M.'          10 0000-0002-6361-7716 
primary 'Jessen, H.J.'      11 0000-0002-1025-9484 
primary 'Andexer, J.N.'     12 0000-0001-8238-5749 
# 
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 'Polyphosphate kinase'   31870.594 1  ? ? ? ? 
2 non-polymer syn "THYMIDINE-5'-PHOSPHATE" 322.208   1  ? ? ? ? 
3 non-polymer syn 'PHOSPHATE ION'          94.971    3  ? ? ? ? 
4 water       nat water                    18.015    88 ? ? ? ? 
# 
_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       
;MTQNIKNLDLSIELDKKMYKKKLKVLQYEMLNAQQFLLKNKIGLILVFEGMDAAGKGGAIKRLIERVDPRGYVVHPISAP
QPHELRYNYLQRFWRKLPQHGQIAVFDRSWYGRVLVERIEGFATKDEWSRAYEEINNFEKILTAGDYIIIKFWLHVSDEE
QLKRFKEREQNPYKSWKLTDEDWRNREKSPQYIEAANEMFEKTDKKNAPWVLVAGNDKKYARVQVLQETLAHIEREALKR
GLHLTNVLDKAHLEDAESSSLDILNEKKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTQNIKNLDLSIELDKKMYKKKLKVLQYEMLNAQQFLLKNKIGLILVFEGMDAAGKGGAIKRLIERVDPRGYVVHPISAP
QPHELRYNYLQRFWRKLPQHGQIAVFDRSWYGRVLVERIEGFATKDEWSRAYEEINNFEKILTAGDYIIIKFWLHVSDEE
QLKRFKEREQNPYKSWKLTDEDWRNREKSPQYIEAANEMFEKTDKKNAPWVLVAGNDKKYARVQVLQETLAHIEREALKR
GLHLTNVLDKAHLEDAESSSLDILNEKKK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "THYMIDINE-5'-PHOSPHATE" TMP 
3 'PHOSPHATE ION'          PO4 
4 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   THR n 
1 3   GLN n 
1 4   ASN n 
1 5   ILE n 
1 6   LYS n 
1 7   ASN n 
1 8   LEU n 
1 9   ASP n 
1 10  LEU n 
1 11  SER n 
1 12  ILE n 
1 13  GLU n 
1 14  LEU n 
1 15  ASP n 
1 16  LYS n 
1 17  LYS n 
1 18  MET n 
1 19  TYR n 
1 20  LYS n 
1 21  LYS n 
1 22  LYS n 
1 23  LEU n 
1 24  LYS n 
1 25  VAL n 
1 26  LEU n 
1 27  GLN n 
1 28  TYR n 
1 29  GLU n 
1 30  MET n 
1 31  LEU n 
1 32  ASN n 
1 33  ALA n 
1 34  GLN n 
1 35  GLN n 
1 36  PHE n 
1 37  LEU n 
1 38  LEU n 
1 39  LYS n 
1 40  ASN n 
1 41  LYS n 
1 42  ILE n 
1 43  GLY n 
1 44  LEU n 
1 45  ILE n 
1 46  LEU n 
1 47  VAL n 
1 48  PHE n 
1 49  GLU n 
1 50  GLY n 
1 51  MET n 
1 52  ASP n 
1 53  ALA n 
1 54  ALA n 
1 55  GLY n 
1 56  LYS n 
1 57  GLY n 
1 58  GLY n 
1 59  ALA n 
1 60  ILE n 
1 61  LYS n 
1 62  ARG n 
1 63  LEU n 
1 64  ILE n 
1 65  GLU n 
1 66  ARG n 
1 67  VAL n 
1 68  ASP n 
1 69  PRO n 
1 70  ARG n 
1 71  GLY n 
1 72  TYR n 
1 73  VAL n 
1 74  VAL n 
1 75  HIS n 
1 76  PRO n 
1 77  ILE n 
1 78  SER n 
1 79  ALA n 
1 80  PRO n 
1 81  GLN n 
1 82  PRO n 
1 83  HIS n 
1 84  GLU n 
1 85  LEU n 
1 86  ARG n 
1 87  TYR n 
1 88  ASN n 
1 89  TYR n 
1 90  LEU n 
1 91  GLN n 
1 92  ARG n 
1 93  PHE n 
1 94  TRP n 
1 95  ARG n 
1 96  LYS n 
1 97  LEU n 
1 98  PRO n 
1 99  GLN n 
1 100 HIS n 
1 101 GLY n 
1 102 GLN n 
1 103 ILE n 
1 104 ALA n 
1 105 VAL n 
1 106 PHE n 
1 107 ASP n 
1 108 ARG n 
1 109 SER n 
1 110 TRP n 
1 111 TYR n 
1 112 GLY n 
1 113 ARG n 
1 114 VAL n 
1 115 LEU n 
1 116 VAL n 
1 117 GLU n 
1 118 ARG n 
1 119 ILE n 
1 120 GLU n 
1 121 GLY n 
1 122 PHE n 
1 123 ALA n 
1 124 THR n 
1 125 LYS n 
1 126 ASP n 
1 127 GLU n 
1 128 TRP n 
1 129 SER n 
1 130 ARG n 
1 131 ALA n 
1 132 TYR n 
1 133 GLU n 
1 134 GLU n 
1 135 ILE n 
1 136 ASN n 
1 137 ASN n 
1 138 PHE n 
1 139 GLU n 
1 140 LYS n 
1 141 ILE n 
1 142 LEU n 
1 143 THR n 
1 144 ALA n 
1 145 GLY n 
1 146 ASP n 
1 147 TYR n 
1 148 ILE n 
1 149 ILE n 
1 150 ILE n 
1 151 LYS n 
1 152 PHE n 
1 153 TRP n 
1 154 LEU n 
1 155 HIS n 
1 156 VAL n 
1 157 SER n 
1 158 ASP n 
1 159 GLU n 
1 160 GLU n 
1 161 GLN n 
1 162 LEU n 
1 163 LYS n 
1 164 ARG n 
1 165 PHE n 
1 166 LYS n 
1 167 GLU n 
1 168 ARG n 
1 169 GLU n 
1 170 GLN n 
1 171 ASN n 
1 172 PRO n 
1 173 TYR n 
1 174 LYS n 
1 175 SER n 
1 176 TRP n 
1 177 LYS n 
1 178 LEU n 
1 179 THR n 
1 180 ASP n 
1 181 GLU n 
1 182 ASP n 
1 183 TRP n 
1 184 ARG n 
1 185 ASN n 
1 186 ARG n 
1 187 GLU n 
1 188 LYS n 
1 189 SER n 
1 190 PRO n 
1 191 GLN n 
1 192 TYR n 
1 193 ILE n 
1 194 GLU n 
1 195 ALA n 
1 196 ALA n 
1 197 ASN n 
1 198 GLU n 
1 199 MET n 
1 200 PHE n 
1 201 GLU n 
1 202 LYS n 
1 203 THR n 
1 204 ASP n 
1 205 LYS n 
1 206 LYS n 
1 207 ASN n 
1 208 ALA n 
1 209 PRO n 
1 210 TRP n 
1 211 VAL n 
1 212 LEU n 
1 213 VAL n 
1 214 ALA n 
1 215 GLY n 
1 216 ASN n 
1 217 ASP n 
1 218 LYS n 
1 219 LYS n 
1 220 TYR n 
1 221 ALA n 
1 222 ARG n 
1 223 VAL n 
1 224 GLN n 
1 225 VAL n 
1 226 LEU n 
1 227 GLN n 
1 228 GLU n 
1 229 THR n 
1 230 LEU n 
1 231 ALA n 
1 232 HIS n 
1 233 ILE n 
1 234 GLU n 
1 235 ARG n 
1 236 GLU n 
1 237 ALA n 
1 238 LEU n 
1 239 LYS n 
1 240 ARG n 
1 241 GLY n 
1 242 LEU n 
1 243 HIS n 
1 244 LEU n 
1 245 THR n 
1 246 ASN n 
1 247 VAL n 
1 248 LEU n 
1 249 ASP n 
1 250 LYS n 
1 251 ALA n 
1 252 HIS n 
1 253 LEU n 
1 254 GLU n 
1 255 ASP n 
1 256 ALA n 
1 257 GLU n 
1 258 SER n 
1 259 SER n 
1 260 SER n 
1 261 LEU n 
1 262 ASP n 
1 263 ILE n 
1 264 LEU n 
1 265 ASN n 
1 266 GLU n 
1 267 LYS n 
1 268 LYS n 
1 269 LYS 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                   269 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BG258_19905 
_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      'Lysinibacillus fusiformis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     28031 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                  ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                 ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE               ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'          ? 'C4 H7 N O4'      133.103 
GLN 'L-peptide linking' y GLUTAMINE                ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'          ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                  ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                    ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE               ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                  ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                   ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE               ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE            ? 'C9 H11 N O2'     165.189 
PO4 non-polymer         . 'PHOSPHATE ION'          ? 'O4 P -3'         94.971  
PRO 'L-peptide linking' y PROLINE                  ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                   ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                ? 'C4 H9 N O3'      119.119 
TMP non-polymer         . "THYMIDINE-5'-PHOSPHATE" ? 'C10 H15 N2 O8 P' 322.208 
TRP 'L-peptide linking' y TRYPTOPHAN               ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                 ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                   ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   ILE 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   ASP 9   9   ?   ?   ?   A . n 
A 1 10  LEU 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  MET 30  30  30  MET MET A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  MET 51  51  51  MET MET A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  HIS 75  75  75  HIS HIS A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  HIS 83  83  83  HIS HIS A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 SER 109 109 109 SER SER A . n 
A 1 110 TRP 110 110 110 TRP TRP A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 TRP 128 128 128 TRP TRP A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 TYR 132 132 132 TYR TYR A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 TYR 147 147 147 TYR TYR A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 TRP 183 183 183 TRP TRP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ILE 193 193 193 ILE ILE A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 TRP 210 210 210 TRP TRP A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 ILE 233 233 233 ILE ILE A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 LYS 239 239 239 LYS LYS A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 HIS 243 243 243 HIS HIS A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 LYS 250 250 ?   ?   ?   A . n 
A 1 251 ALA 251 251 ?   ?   ?   A . n 
A 1 252 HIS 252 252 ?   ?   ?   A . n 
A 1 253 LEU 253 253 ?   ?   ?   A . n 
A 1 254 GLU 254 254 ?   ?   ?   A . n 
A 1 255 ASP 255 255 ?   ?   ?   A . n 
A 1 256 ALA 256 256 ?   ?   ?   A . n 
A 1 257 GLU 257 257 ?   ?   ?   A . n 
A 1 258 SER 258 258 ?   ?   ?   A . n 
A 1 259 SER 259 259 ?   ?   ?   A . n 
A 1 260 SER 260 260 ?   ?   ?   A . n 
A 1 261 LEU 261 261 ?   ?   ?   A . n 
A 1 262 ASP 262 262 ?   ?   ?   A . n 
A 1 263 ILE 263 263 ?   ?   ?   A . n 
A 1 264 LEU 264 264 ?   ?   ?   A . n 
A 1 265 ASN 265 265 ?   ?   ?   A . n 
A 1 266 GLU 266 266 ?   ?   ?   A . n 
A 1 267 LYS 267 267 ?   ?   ?   A . n 
A 1 268 LYS 268 268 ?   ?   ?   A . n 
A 1 269 LYS 269 269 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TMP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TMP 
_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 
B 2 TMP 1  301 301 TMP TMP A . 
C 3 PO4 1  302 302 PO4 PO4 A . 
D 3 PO4 1  303 303 PO4 PO4 A . 
E 3 PO4 1  304 304 PO4 PO4 A . 
F 4 HOH 1  401 69  HOH HOH A . 
F 4 HOH 2  402 92  HOH HOH A . 
F 4 HOH 3  403 11  HOH HOH A . 
F 4 HOH 4  404 34  HOH HOH A . 
F 4 HOH 5  405 70  HOH HOH A . 
F 4 HOH 6  406 22  HOH HOH A . 
F 4 HOH 7  407 15  HOH HOH A . 
F 4 HOH 8  408 23  HOH HOH A . 
F 4 HOH 9  409 64  HOH HOH A . 
F 4 HOH 10 410 74  HOH HOH A . 
F 4 HOH 11 411 62  HOH HOH A . 
F 4 HOH 12 412 29  HOH HOH A . 
F 4 HOH 13 413 14  HOH HOH A . 
F 4 HOH 14 414 20  HOH HOH A . 
F 4 HOH 15 415 39  HOH HOH A . 
F 4 HOH 16 416 24  HOH HOH A . 
F 4 HOH 17 417 17  HOH HOH A . 
F 4 HOH 18 418 8   HOH HOH A . 
F 4 HOH 19 419 47  HOH HOH A . 
F 4 HOH 20 420 4   HOH HOH A . 
F 4 HOH 21 421 27  HOH HOH A . 
F 4 HOH 22 422 6   HOH HOH A . 
F 4 HOH 23 423 46  HOH HOH A . 
F 4 HOH 24 424 26  HOH HOH A . 
F 4 HOH 25 425 76  HOH HOH A . 
F 4 HOH 26 426 45  HOH HOH A . 
F 4 HOH 27 427 63  HOH HOH A . 
F 4 HOH 28 428 68  HOH HOH A . 
F 4 HOH 29 429 9   HOH HOH A . 
F 4 HOH 30 430 33  HOH HOH A . 
F 4 HOH 31 431 13  HOH HOH A . 
F 4 HOH 32 432 5   HOH HOH A . 
F 4 HOH 33 433 30  HOH HOH A . 
F 4 HOH 34 434 71  HOH HOH A . 
F 4 HOH 35 435 7   HOH HOH A . 
F 4 HOH 36 436 10  HOH HOH A . 
F 4 HOH 37 437 44  HOH HOH A . 
F 4 HOH 38 438 53  HOH HOH A . 
F 4 HOH 39 439 21  HOH HOH A . 
F 4 HOH 40 440 65  HOH HOH A . 
F 4 HOH 41 441 72  HOH HOH A . 
F 4 HOH 42 442 50  HOH HOH A . 
F 4 HOH 43 443 77  HOH HOH A . 
F 4 HOH 44 444 48  HOH HOH A . 
F 4 HOH 45 445 19  HOH HOH A . 
F 4 HOH 46 446 88  HOH HOH A . 
F 4 HOH 47 447 12  HOH HOH A . 
F 4 HOH 48 448 41  HOH HOH A . 
F 4 HOH 49 449 49  HOH HOH A . 
F 4 HOH 50 450 58  HOH HOH A . 
F 4 HOH 51 451 66  HOH HOH A . 
F 4 HOH 52 452 90  HOH HOH A . 
F 4 HOH 53 453 36  HOH HOH A . 
F 4 HOH 54 454 16  HOH HOH A . 
F 4 HOH 55 455 18  HOH HOH A . 
F 4 HOH 56 456 31  HOH HOH A . 
F 4 HOH 57 457 42  HOH HOH A . 
F 4 HOH 58 458 51  HOH HOH A . 
F 4 HOH 59 459 28  HOH HOH A . 
F 4 HOH 60 460 32  HOH HOH A . 
F 4 HOH 61 461 59  HOH HOH A . 
F 4 HOH 62 462 52  HOH HOH A . 
F 4 HOH 63 463 61  HOH HOH A . 
F 4 HOH 64 464 38  HOH HOH A . 
F 4 HOH 65 465 73  HOH HOH A . 
F 4 HOH 66 466 60  HOH HOH A . 
F 4 HOH 67 467 43  HOH HOH A . 
F 4 HOH 68 468 2   HOH HOH A . 
F 4 HOH 69 469 1   HOH HOH A . 
F 4 HOH 70 470 87  HOH HOH A . 
F 4 HOH 71 471 67  HOH HOH A . 
F 4 HOH 72 472 75  HOH HOH A . 
F 4 HOH 73 473 89  HOH HOH A . 
F 4 HOH 74 474 3   HOH HOH A . 
F 4 HOH 75 475 35  HOH HOH A . 
F 4 HOH 76 476 91  HOH HOH A . 
F 4 HOH 77 477 84  HOH HOH A . 
F 4 HOH 78 478 83  HOH HOH A . 
F 4 HOH 79 479 37  HOH HOH A . 
F 4 HOH 80 480 82  HOH HOH A . 
F 4 HOH 81 481 56  HOH HOH A . 
F 4 HOH 82 482 85  HOH HOH A . 
F 4 HOH 83 483 79  HOH HOH A . 
F 4 HOH 84 484 78  HOH HOH A . 
F 4 HOH 85 485 54  HOH HOH A . 
F 4 HOH 86 486 57  HOH HOH A . 
F 4 HOH 87 487 86  HOH HOH A . 
F 4 HOH 88 488 80  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H8L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     159.596 
_cell.length_a_esd                 ? 
_cell.length_b                     159.596 
_cell.length_b_esd                 ? 
_cell.length_c                     67.433 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9H8L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                180 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 62 2 2' 
_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                   9H8L 
_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             3.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          68.38 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'1.5 M ammonium sulfate, 0.1 M sodium acetate pH 4.6; Crystals have been soaked with TMP (final conc. of 0.75 M) for 24h.' 
_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 EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-10-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8731 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8731 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H8L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               138.21 
_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                                     29017 
_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                           96.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                39.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_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                                0.125 
_reflns.pdbx_Rpim_I_all                                0.020 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1138655 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.123 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           101646 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2424 
_reflns_shell.percent_possible_obs                          100.0 
_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                               41.9 
_reflns_shell.pdbx_chi_squared                              1.09 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.4 
_reflns_shell.pdbx_Rrim_I_all                               2.501 
_reflns_shell.pdbx_Rpim_I_all                               0.385 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.763 
_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                                  2.471 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9H8L 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             69.11 
_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                     28804 
_refine.ls_number_reflns_R_free                  1454 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.97 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1931 
_refine.ls_R_factor_R_free                       0.2082 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1923 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.52 
_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                            0.26 
_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        2010 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             88 
_refine_hist.number_atoms_total               2134 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        69.11 
# 
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' ? 0.006  ? 2118 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.704  ? 2861 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.707 ? 822  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 292  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 365  ? 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' 2.10 2.18  . . 147 2772 99.00  . . . . 0.2680 . . . . . . . . . . . 0.3244 
'X-RAY DIFFRACTION' 2.18 2.26  . . 135 2366 85.00  . . . . 0.2839 . . . . . . . . . . . 0.3883 
'X-RAY DIFFRACTION' 2.26 2.37  . . 149 2786 100.00 . . . . 0.2093 . . . . . . . . . . . 0.2608 
'X-RAY DIFFRACTION' 2.37 2.49  . . 119 2850 100.00 . . . . 0.2051 . . . . . . . . . . . 0.2150 
'X-RAY DIFFRACTION' 2.49 2.65  . . 154 2799 100.00 . . . . 0.2080 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 2.65 2.85  . . 137 2464 87.00  . . . . 0.2193 . . . . . . . . . . . 0.2701 
'X-RAY DIFFRACTION' 2.85 3.14  . . 147 2825 100.00 . . . . 0.2103 . . . . . . . . . . . 0.2312 
'X-RAY DIFFRACTION' 3.14 3.59  . . 140 2732 95.00  . . . . 0.1948 . . . . . . . . . . . 0.2231 
'X-RAY DIFFRACTION' 3.59 4.52  . . 154 2708 93.00  . . . . 0.1545 . . . . . . . . . . . 0.1750 
'X-RAY DIFFRACTION' 4.52 69.11 . . 172 3048 100.00 . . . . 0.1861 . . . . . . . . . . . 0.1721 
# 
_struct.entry_id                     9H8L 
_struct.title                        
'Crystal Structure of Polyphosphate kinase 2-II (PPK2-II) from Lysinibacillus fusiformis bound to TMP' 
_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        9H8L 
_struct_keywords.text            'Transferase, Polyphosphate, Nucleotide, Phosphorylation' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1E4R1F9_9BACI 
_struct_ref.pdbx_db_accession          A0A1E4R1F9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTQNIKNLDLSIELDKKMYKKKLKVLQYEMLNAQQFLLKNKIGLILVFEGMDAAGKGGAIKRLIERVDPRGYVVHPISAP
QPHELRYNYLQRFWRKLPQHGQIAVFDRSWYGRVLVERIEGFATKDEWSRAYEEINNFEKILTAGDYIIIKFWLHVSDEE
QLKRFKEREQNPYKSWKLTDEDWRNREKSPQYIEAANEMFEKTDKKNAPWVLVAGNDKKYARVQVLQETLAHIEREALKR
GLHLTNVLDKAHLEDAESSSLDILNEKKK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H8L 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 269 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A1E4R1F9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  269 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       269 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1190  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  13120 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 15  ? ASN A 40  ? ASP A 15  ASN A 40  1 ? 26 
HELX_P HELX_P2  AA2 GLY A 55  ? GLU A 65  ? GLY A 55  GLU A 65  1 ? 11 
HELX_P HELX_P3  AA3 ASP A 68  ? ARG A 70  ? ASP A 68  ARG A 70  5 ? 3  
HELX_P HELX_P4  AA4 HIS A 83  ? TYR A 87  ? HIS A 83  TYR A 87  5 ? 5  
HELX_P HELX_P5  AA5 LEU A 90  ? ARG A 95  ? LEU A 90  ARG A 95  1 ? 6  
HELX_P HELX_P6  AA6 SER A 109 ? VAL A 114 ? SER A 109 VAL A 114 5 ? 6  
HELX_P HELX_P7  AA7 LEU A 115 ? GLU A 120 ? LEU A 115 GLU A 120 1 ? 6  
HELX_P HELX_P8  AA8 THR A 124 ? GLY A 145 ? THR A 124 GLY A 145 1 ? 22 
HELX_P HELX_P9  AA9 SER A 157 ? GLN A 170 ? SER A 157 GLN A 170 1 ? 14 
HELX_P HELX_P10 AB1 LYS A 174 ? LEU A 178 ? LYS A 174 LEU A 178 5 ? 5  
HELX_P HELX_P11 AB2 THR A 179 ? ARG A 186 ? THR A 179 ARG A 186 1 ? 8  
HELX_P HELX_P12 AB3 LYS A 188 ? ASP A 204 ? LYS A 188 ASP A 204 1 ? 17 
HELX_P HELX_P13 AB4 ASP A 217 ? ARG A 240 ? ASP A 217 ARG A 240 1 ? 24 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
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 
# 
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 TYR A 72  ? PRO A 76  ? TYR A 72  PRO A 76  
AA1 2 ILE A 103 ? ASP A 107 ? ILE A 103 ASP A 107 
AA1 3 GLY A 43  ? GLU A 49  ? GLY A 43  GLU A 49  
AA1 4 TYR A 147 ? HIS A 155 ? TYR A 147 HIS A 155 
AA1 5 TRP A 210 ? ALA A 214 ? TRP A 210 ALA A 214 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 75  ? N HIS A 75  O VAL A 105 ? O VAL A 105 
AA1 2 3 O PHE A 106 ? O PHE A 106 N LEU A 46  ? N LEU A 46  
AA1 3 4 N ILE A 45  ? N ILE A 45  O ILE A 148 ? O ILE A 148 
AA1 4 5 N TRP A 153 ? N TRP A 153 O VAL A 213 ? O VAL A 213 
# 
_pdbx_entry_details.entry_id                   9H8L 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 78  ? ? -123.72 -166.79 
2 1 ARG A 108 ? ? 71.42   159.73  
3 1 SER A 109 ? ? -162.94 -164.20 
4 1 LEU A 115 ? ? -118.72 -99.84  
5 1 ALA A 208 ? ? -155.12 74.63   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         65.3003 
_pdbx_refine_tls.origin_y         18.9995 
_pdbx_refine_tls.origin_z         -3.3725 
_pdbx_refine_tls.T[1][1]          0.3148 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0548 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0188 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3690 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0513 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3785 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.2301 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.3302 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0469 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.9005 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0851 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.9418 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0888 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0538 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1764 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.1130 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.1384 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.3480 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1736 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1782 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0518 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A GLN 3   ? A GLN 3   
4  1 Y 1 A ASN 4   ? A ASN 4   
5  1 Y 1 A ILE 5   ? A ILE 5   
6  1 Y 1 A LYS 6   ? A LYS 6   
7  1 Y 1 A ASN 7   ? A ASN 7   
8  1 Y 1 A LEU 8   ? A LEU 8   
9  1 Y 1 A ASP 9   ? A ASP 9   
10 1 Y 1 A LEU 10  ? A LEU 10  
11 1 Y 1 A LYS 250 ? A LYS 250 
12 1 Y 1 A ALA 251 ? A ALA 251 
13 1 Y 1 A HIS 252 ? A HIS 252 
14 1 Y 1 A LEU 253 ? A LEU 253 
15 1 Y 1 A GLU 254 ? A GLU 254 
16 1 Y 1 A ASP 255 ? A ASP 255 
17 1 Y 1 A ALA 256 ? A ALA 256 
18 1 Y 1 A GLU 257 ? A GLU 257 
19 1 Y 1 A SER 258 ? A SER 258 
20 1 Y 1 A SER 259 ? A SER 259 
21 1 Y 1 A SER 260 ? A SER 260 
22 1 Y 1 A LEU 261 ? A LEU 261 
23 1 Y 1 A ASP 262 ? A ASP 262 
24 1 Y 1 A ILE 263 ? A ILE 263 
25 1 Y 1 A LEU 264 ? A LEU 264 
26 1 Y 1 A ASN 265 ? A ASN 265 
27 1 Y 1 A GLU 266 ? A GLU 266 
28 1 Y 1 A LYS 267 ? A LYS 267 
29 1 Y 1 A LYS 268 ? A LYS 268 
30 1 Y 1 A LYS 269 ? A LYS 269 
# 
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  
GLN N      N N N 74  
GLN CA     C N S 75  
GLN C      C N N 76  
GLN O      O N N 77  
GLN CB     C N N 78  
GLN CG     C N N 79  
GLN CD     C N N 80  
GLN OE1    O N N 81  
GLN NE2    N N N 82  
GLN OXT    O N N 83  
GLN H      H N N 84  
GLN H2     H N N 85  
GLN HA     H N N 86  
GLN HB2    H N N 87  
GLN HB3    H N N 88  
GLN HG2    H N N 89  
GLN HG3    H N N 90  
GLN HE21   H N N 91  
GLN HE22   H N N 92  
GLN HXT    H N N 93  
GLU N      N N N 94  
GLU CA     C N S 95  
GLU C      C N N 96  
GLU O      O N N 97  
GLU CB     C N N 98  
GLU CG     C N N 99  
GLU CD     C N N 100 
GLU OE1    O N N 101 
GLU OE2    O N N 102 
GLU OXT    O N N 103 
GLU H      H N N 104 
GLU H2     H N N 105 
GLU HA     H N N 106 
GLU HB2    H N N 107 
GLU HB3    H N N 108 
GLU HG2    H N N 109 
GLU HG3    H N N 110 
GLU HE2    H N N 111 
GLU HXT    H N N 112 
GLY N      N N N 113 
GLY CA     C N N 114 
GLY C      C N N 115 
GLY O      O N N 116 
GLY OXT    O N N 117 
GLY H      H N N 118 
GLY H2     H N N 119 
GLY HA2    H N N 120 
GLY HA3    H N N 121 
GLY HXT    H N N 122 
HIS N      N N N 123 
HIS CA     C N S 124 
HIS C      C N N 125 
HIS O      O N N 126 
HIS CB     C N N 127 
HIS CG     C Y N 128 
HIS ND1    N Y N 129 
HIS CD2    C Y N 130 
HIS CE1    C Y N 131 
HIS NE2    N Y N 132 
HIS OXT    O N N 133 
HIS H      H N N 134 
HIS H2     H N N 135 
HIS HA     H N N 136 
HIS HB2    H N N 137 
HIS HB3    H N N 138 
HIS HD1    H N N 139 
HIS HD2    H N N 140 
HIS HE1    H N N 141 
HIS HE2    H N N 142 
HIS HXT    H N N 143 
HOH O      O N N 144 
HOH H1     H N N 145 
HOH H2     H N N 146 
ILE N      N N N 147 
ILE CA     C N S 148 
ILE C      C N N 149 
ILE O      O N N 150 
ILE CB     C N S 151 
ILE CG1    C N N 152 
ILE CG2    C N N 153 
ILE CD1    C N N 154 
ILE OXT    O N N 155 
ILE H      H N N 156 
ILE H2     H N N 157 
ILE HA     H N N 158 
ILE HB     H N N 159 
ILE HG12   H N N 160 
ILE HG13   H N N 161 
ILE HG21   H N N 162 
ILE HG22   H N N 163 
ILE HG23   H N N 164 
ILE HD11   H N N 165 
ILE HD12   H N N 166 
ILE HD13   H N N 167 
ILE HXT    H N N 168 
LEU N      N N N 169 
LEU CA     C N S 170 
LEU C      C N N 171 
LEU O      O N N 172 
LEU CB     C N N 173 
LEU CG     C N N 174 
LEU CD1    C N N 175 
LEU CD2    C N N 176 
LEU OXT    O N N 177 
LEU H      H N N 178 
LEU H2     H N N 179 
LEU HA     H N N 180 
LEU HB2    H N N 181 
LEU HB3    H N N 182 
LEU HG     H N N 183 
LEU HD11   H N N 184 
LEU HD12   H N N 185 
LEU HD13   H N N 186 
LEU HD21   H N N 187 
LEU HD22   H N N 188 
LEU HD23   H N N 189 
LEU HXT    H N N 190 
LYS N      N N N 191 
LYS CA     C N S 192 
LYS C      C N N 193 
LYS O      O N N 194 
LYS CB     C N N 195 
LYS CG     C N N 196 
LYS CD     C N N 197 
LYS CE     C N N 198 
LYS NZ     N N N 199 
LYS OXT    O N N 200 
LYS H      H N N 201 
LYS H2     H N N 202 
LYS HA     H N N 203 
LYS HB2    H N N 204 
LYS HB3    H N N 205 
LYS HG2    H N N 206 
LYS HG3    H N N 207 
LYS HD2    H N N 208 
LYS HD3    H N N 209 
LYS HE2    H N N 210 
LYS HE3    H N N 211 
LYS HZ1    H N N 212 
LYS HZ2    H N N 213 
LYS HZ3    H N N 214 
LYS HXT    H N N 215 
MET N      N N N 216 
MET CA     C N S 217 
MET C      C N N 218 
MET O      O N N 219 
MET CB     C N N 220 
MET CG     C N N 221 
MET SD     S N N 222 
MET CE     C N N 223 
MET OXT    O N N 224 
MET H      H N N 225 
MET H2     H N N 226 
MET HA     H N N 227 
MET HB2    H N N 228 
MET HB3    H N N 229 
MET HG2    H N N 230 
MET HG3    H N N 231 
MET HE1    H N N 232 
MET HE2    H N N 233 
MET HE3    H N N 234 
MET HXT    H N N 235 
PHE N      N N N 236 
PHE CA     C N S 237 
PHE C      C N N 238 
PHE O      O N N 239 
PHE CB     C N N 240 
PHE CG     C Y N 241 
PHE CD1    C Y N 242 
PHE CD2    C Y N 243 
PHE CE1    C Y N 244 
PHE CE2    C Y N 245 
PHE CZ     C Y N 246 
PHE OXT    O N N 247 
PHE H      H N N 248 
PHE H2     H N N 249 
PHE HA     H N N 250 
PHE HB2    H N N 251 
PHE HB3    H N N 252 
PHE HD1    H N N 253 
PHE HD2    H N N 254 
PHE HE1    H N N 255 
PHE HE2    H N N 256 
PHE HZ     H N N 257 
PHE HXT    H N N 258 
PO4 P      P N N 259 
PO4 O1     O N N 260 
PO4 O2     O N N 261 
PO4 O3     O N N 262 
PO4 O4     O N N 263 
PRO N      N N N 264 
PRO CA     C N S 265 
PRO C      C N N 266 
PRO O      O N N 267 
PRO CB     C N N 268 
PRO CG     C N N 269 
PRO CD     C N N 270 
PRO OXT    O N N 271 
PRO H      H N N 272 
PRO HA     H N N 273 
PRO HB2    H N N 274 
PRO HB3    H N N 275 
PRO HG2    H N N 276 
PRO HG3    H N N 277 
PRO HD2    H N N 278 
PRO HD3    H N N 279 
PRO HXT    H N N 280 
SER N      N N N 281 
SER CA     C N S 282 
SER C      C N N 283 
SER O      O N N 284 
SER CB     C N N 285 
SER OG     O N N 286 
SER OXT    O N N 287 
SER H      H N N 288 
SER H2     H N N 289 
SER HA     H N N 290 
SER HB2    H N N 291 
SER HB3    H N N 292 
SER HG     H N N 293 
SER HXT    H N N 294 
THR N      N N N 295 
THR CA     C N S 296 
THR C      C N N 297 
THR O      O N N 298 
THR CB     C N R 299 
THR OG1    O N N 300 
THR CG2    C N N 301 
THR OXT    O N N 302 
THR H      H N N 303 
THR H2     H N N 304 
THR HA     H N N 305 
THR HB     H N N 306 
THR HG1    H N N 307 
THR HG21   H N N 308 
THR HG22   H N N 309 
THR HG23   H N N 310 
THR HXT    H N N 311 
TMP P      P N N 312 
TMP O1P    O N N 313 
TMP O2P    O N N 314 
TMP O3P    O N N 315 
TMP "O5'"  O N N 316 
TMP "C5'"  C N N 317 
TMP "C4'"  C N R 318 
TMP "O4'"  O N N 319 
TMP "C3'"  C N S 320 
TMP "O3'"  O N N 321 
TMP "C2'"  C N N 322 
TMP "C1'"  C N R 323 
TMP N1     N N N 324 
TMP C2     C N N 325 
TMP O2     O N N 326 
TMP N3     N N N 327 
TMP C4     C N N 328 
TMP O4     O N N 329 
TMP C5     C N N 330 
TMP C5M    C N N 331 
TMP C6     C N N 332 
TMP HOP2   H N N 333 
TMP HOP3   H N N 334 
TMP "H5'1" H N N 335 
TMP "H5'2" H N N 336 
TMP "H4'"  H N N 337 
TMP "H3'"  H N N 338 
TMP "HO3'" H N N 339 
TMP "H2'1" H N N 340 
TMP "H2'2" H N N 341 
TMP "H1'"  H N N 342 
TMP HN3    H N N 343 
TMP H51    H N N 344 
TMP H52    H N N 345 
TMP H53    H N N 346 
TMP H6     H N N 347 
TRP N      N N N 348 
TRP CA     C N S 349 
TRP C      C N N 350 
TRP O      O N N 351 
TRP CB     C N N 352 
TRP CG     C Y N 353 
TRP CD1    C Y N 354 
TRP CD2    C Y N 355 
TRP NE1    N Y N 356 
TRP CE2    C Y N 357 
TRP CE3    C Y N 358 
TRP CZ2    C Y N 359 
TRP CZ3    C Y N 360 
TRP CH2    C Y N 361 
TRP OXT    O N N 362 
TRP H      H N N 363 
TRP H2     H N N 364 
TRP HA     H N N 365 
TRP HB2    H N N 366 
TRP HB3    H N N 367 
TRP HD1    H N N 368 
TRP HE1    H N N 369 
TRP HE3    H N N 370 
TRP HZ2    H N N 371 
TRP HZ3    H N N 372 
TRP HH2    H N N 373 
TRP HXT    H N N 374 
TYR N      N N N 375 
TYR CA     C N S 376 
TYR C      C N N 377 
TYR O      O N N 378 
TYR CB     C N N 379 
TYR CG     C Y N 380 
TYR CD1    C Y N 381 
TYR CD2    C Y N 382 
TYR CE1    C Y N 383 
TYR CE2    C Y N 384 
TYR CZ     C Y N 385 
TYR OH     O N N 386 
TYR OXT    O N N 387 
TYR H      H N N 388 
TYR H2     H N N 389 
TYR HA     H N N 390 
TYR HB2    H N N 391 
TYR HB3    H N N 392 
TYR HD1    H N N 393 
TYR HD2    H N N 394 
TYR HE1    H N N 395 
TYR HE2    H N N 396 
TYR HH     H N N 397 
TYR HXT    H N N 398 
VAL N      N N N 399 
VAL CA     C N S 400 
VAL C      C N N 401 
VAL O      O N N 402 
VAL CB     C N N 403 
VAL CG1    C N N 404 
VAL CG2    C N N 405 
VAL OXT    O N N 406 
VAL H      H N N 407 
VAL H2     H N N 408 
VAL HA     H N N 409 
VAL HB     H N N 410 
VAL HG11   H N N 411 
VAL HG12   H N N 412 
VAL HG13   H N N 413 
VAL HG21   H N N 414 
VAL HG22   H N N 415 
VAL HG23   H N N 416 
VAL HXT    H N N 417 
# 
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  
GLN N     CA     sing N N 70  
GLN N     H      sing N N 71  
GLN N     H2     sing N N 72  
GLN CA    C      sing N N 73  
GLN CA    CB     sing N N 74  
GLN CA    HA     sing N N 75  
GLN C     O      doub N N 76  
GLN C     OXT    sing N N 77  
GLN CB    CG     sing N N 78  
GLN CB    HB2    sing N N 79  
GLN CB    HB3    sing N N 80  
GLN CG    CD     sing N N 81  
GLN CG    HG2    sing N N 82  
GLN CG    HG3    sing N N 83  
GLN CD    OE1    doub N N 84  
GLN CD    NE2    sing N N 85  
GLN NE2   HE21   sing N N 86  
GLN NE2   HE22   sing N N 87  
GLN OXT   HXT    sing N N 88  
GLU N     CA     sing N N 89  
GLU N     H      sing N N 90  
GLU N     H2     sing N N 91  
GLU CA    C      sing N N 92  
GLU CA    CB     sing N N 93  
GLU CA    HA     sing N N 94  
GLU C     O      doub N N 95  
GLU C     OXT    sing N N 96  
GLU CB    CG     sing N N 97  
GLU CB    HB2    sing N N 98  
GLU CB    HB3    sing N N 99  
GLU CG    CD     sing N N 100 
GLU CG    HG2    sing N N 101 
GLU CG    HG3    sing N N 102 
GLU CD    OE1    doub N N 103 
GLU CD    OE2    sing N N 104 
GLU OE2   HE2    sing N N 105 
GLU OXT   HXT    sing N N 106 
GLY N     CA     sing N N 107 
GLY N     H      sing N N 108 
GLY N     H2     sing N N 109 
GLY CA    C      sing N N 110 
GLY CA    HA2    sing N N 111 
GLY CA    HA3    sing N N 112 
GLY C     O      doub N N 113 
GLY C     OXT    sing N N 114 
GLY OXT   HXT    sing N N 115 
HIS N     CA     sing N N 116 
HIS N     H      sing N N 117 
HIS N     H2     sing N N 118 
HIS CA    C      sing N N 119 
HIS CA    CB     sing N N 120 
HIS CA    HA     sing N N 121 
HIS C     O      doub N N 122 
HIS C     OXT    sing N N 123 
HIS CB    CG     sing N N 124 
HIS CB    HB2    sing N N 125 
HIS CB    HB3    sing N N 126 
HIS CG    ND1    sing Y N 127 
HIS CG    CD2    doub Y N 128 
HIS ND1   CE1    doub Y N 129 
HIS ND1   HD1    sing N N 130 
HIS CD2   NE2    sing Y N 131 
HIS CD2   HD2    sing N N 132 
HIS CE1   NE2    sing Y N 133 
HIS CE1   HE1    sing N N 134 
HIS NE2   HE2    sing N N 135 
HIS OXT   HXT    sing N N 136 
HOH O     H1     sing N N 137 
HOH O     H2     sing N N 138 
ILE N     CA     sing N N 139 
ILE N     H      sing N N 140 
ILE N     H2     sing N N 141 
ILE CA    C      sing N N 142 
ILE CA    CB     sing N N 143 
ILE CA    HA     sing N N 144 
ILE C     O      doub N N 145 
ILE C     OXT    sing N N 146 
ILE CB    CG1    sing N N 147 
ILE CB    CG2    sing N N 148 
ILE CB    HB     sing N N 149 
ILE CG1   CD1    sing N N 150 
ILE CG1   HG12   sing N N 151 
ILE CG1   HG13   sing N N 152 
ILE CG2   HG21   sing N N 153 
ILE CG2   HG22   sing N N 154 
ILE CG2   HG23   sing N N 155 
ILE CD1   HD11   sing N N 156 
ILE CD1   HD12   sing N N 157 
ILE CD1   HD13   sing N N 158 
ILE OXT   HXT    sing N N 159 
LEU N     CA     sing N N 160 
LEU N     H      sing N N 161 
LEU N     H2     sing N N 162 
LEU CA    C      sing N N 163 
LEU CA    CB     sing N N 164 
LEU CA    HA     sing N N 165 
LEU C     O      doub N N 166 
LEU C     OXT    sing N N 167 
LEU CB    CG     sing N N 168 
LEU CB    HB2    sing N N 169 
LEU CB    HB3    sing N N 170 
LEU CG    CD1    sing N N 171 
LEU CG    CD2    sing N N 172 
LEU CG    HG     sing N N 173 
LEU CD1   HD11   sing N N 174 
LEU CD1   HD12   sing N N 175 
LEU CD1   HD13   sing N N 176 
LEU CD2   HD21   sing N N 177 
LEU CD2   HD22   sing N N 178 
LEU CD2   HD23   sing N N 179 
LEU OXT   HXT    sing N N 180 
LYS N     CA     sing N N 181 
LYS N     H      sing N N 182 
LYS N     H2     sing N N 183 
LYS CA    C      sing N N 184 
LYS CA    CB     sing N N 185 
LYS CA    HA     sing N N 186 
LYS C     O      doub N N 187 
LYS C     OXT    sing N N 188 
LYS CB    CG     sing N N 189 
LYS CB    HB2    sing N N 190 
LYS CB    HB3    sing N N 191 
LYS CG    CD     sing N N 192 
LYS CG    HG2    sing N N 193 
LYS CG    HG3    sing N N 194 
LYS CD    CE     sing N N 195 
LYS CD    HD2    sing N N 196 
LYS CD    HD3    sing N N 197 
LYS CE    NZ     sing N N 198 
LYS CE    HE2    sing N N 199 
LYS CE    HE3    sing N N 200 
LYS NZ    HZ1    sing N N 201 
LYS NZ    HZ2    sing N N 202 
LYS NZ    HZ3    sing N N 203 
LYS OXT   HXT    sing N N 204 
MET N     CA     sing N N 205 
MET N     H      sing N N 206 
MET N     H2     sing N N 207 
MET CA    C      sing N N 208 
MET CA    CB     sing N N 209 
MET CA    HA     sing N N 210 
MET C     O      doub N N 211 
MET C     OXT    sing N N 212 
MET CB    CG     sing N N 213 
MET CB    HB2    sing N N 214 
MET CB    HB3    sing N N 215 
MET CG    SD     sing N N 216 
MET CG    HG2    sing N N 217 
MET CG    HG3    sing N N 218 
MET SD    CE     sing N N 219 
MET CE    HE1    sing N N 220 
MET CE    HE2    sing N N 221 
MET CE    HE3    sing N N 222 
MET OXT   HXT    sing N N 223 
PHE N     CA     sing N N 224 
PHE N     H      sing N N 225 
PHE N     H2     sing N N 226 
PHE CA    C      sing N N 227 
PHE CA    CB     sing N N 228 
PHE CA    HA     sing N N 229 
PHE C     O      doub N N 230 
PHE C     OXT    sing N N 231 
PHE CB    CG     sing N N 232 
PHE CB    HB2    sing N N 233 
PHE CB    HB3    sing N N 234 
PHE CG    CD1    doub Y N 235 
PHE CG    CD2    sing Y N 236 
PHE CD1   CE1    sing Y N 237 
PHE CD1   HD1    sing N N 238 
PHE CD2   CE2    doub Y N 239 
PHE CD2   HD2    sing N N 240 
PHE CE1   CZ     doub Y N 241 
PHE CE1   HE1    sing N N 242 
PHE CE2   CZ     sing Y N 243 
PHE CE2   HE2    sing N N 244 
PHE CZ    HZ     sing N N 245 
PHE OXT   HXT    sing N N 246 
PO4 P     O1     doub N N 247 
PO4 P     O2     sing N N 248 
PO4 P     O3     sing N N 249 
PO4 P     O4     sing N N 250 
PRO N     CA     sing N N 251 
PRO N     CD     sing N N 252 
PRO N     H      sing N N 253 
PRO CA    C      sing N N 254 
PRO CA    CB     sing N N 255 
PRO CA    HA     sing N N 256 
PRO C     O      doub N N 257 
PRO C     OXT    sing N N 258 
PRO CB    CG     sing N N 259 
PRO CB    HB2    sing N N 260 
PRO CB    HB3    sing N N 261 
PRO CG    CD     sing N N 262 
PRO CG    HG2    sing N N 263 
PRO CG    HG3    sing N N 264 
PRO CD    HD2    sing N N 265 
PRO CD    HD3    sing N N 266 
PRO OXT   HXT    sing N N 267 
SER N     CA     sing N N 268 
SER N     H      sing N N 269 
SER N     H2     sing N N 270 
SER CA    C      sing N N 271 
SER CA    CB     sing N N 272 
SER CA    HA     sing N N 273 
SER C     O      doub N N 274 
SER C     OXT    sing N N 275 
SER CB    OG     sing N N 276 
SER CB    HB2    sing N N 277 
SER CB    HB3    sing N N 278 
SER OG    HG     sing N N 279 
SER OXT   HXT    sing N N 280 
THR N     CA     sing N N 281 
THR N     H      sing N N 282 
THR N     H2     sing N N 283 
THR CA    C      sing N N 284 
THR CA    CB     sing N N 285 
THR CA    HA     sing N N 286 
THR C     O      doub N N 287 
THR C     OXT    sing N N 288 
THR CB    OG1    sing N N 289 
THR CB    CG2    sing N N 290 
THR CB    HB     sing N N 291 
THR OG1   HG1    sing N N 292 
THR CG2   HG21   sing N N 293 
THR CG2   HG22   sing N N 294 
THR CG2   HG23   sing N N 295 
THR OXT   HXT    sing N N 296 
TMP P     O1P    doub N N 297 
TMP P     O2P    sing N N 298 
TMP P     O3P    sing N N 299 
TMP P     "O5'"  sing N N 300 
TMP O2P   HOP2   sing N N 301 
TMP O3P   HOP3   sing N N 302 
TMP "O5'" "C5'"  sing N N 303 
TMP "C5'" "C4'"  sing N N 304 
TMP "C5'" "H5'1" sing N N 305 
TMP "C5'" "H5'2" sing N N 306 
TMP "C4'" "O4'"  sing N N 307 
TMP "C4'" "C3'"  sing N N 308 
TMP "C4'" "H4'"  sing N N 309 
TMP "O4'" "C1'"  sing N N 310 
TMP "C3'" "O3'"  sing N N 311 
TMP "C3'" "C2'"  sing N N 312 
TMP "C3'" "H3'"  sing N N 313 
TMP "O3'" "HO3'" sing N N 314 
TMP "C2'" "C1'"  sing N N 315 
TMP "C2'" "H2'1" sing N N 316 
TMP "C2'" "H2'2" sing N N 317 
TMP "C1'" N1     sing N N 318 
TMP "C1'" "H1'"  sing N N 319 
TMP N1    C2     sing N N 320 
TMP N1    C6     sing N N 321 
TMP C2    O2     doub N N 322 
TMP C2    N3     sing N N 323 
TMP N3    C4     sing N N 324 
TMP N3    HN3    sing N N 325 
TMP C4    O4     doub N N 326 
TMP C4    C5     sing N N 327 
TMP C5    C5M    sing N N 328 
TMP C5    C6     doub N N 329 
TMP C5M   H51    sing N N 330 
TMP C5M   H52    sing N N 331 
TMP C5M   H53    sing N N 332 
TMP C6    H6     sing N N 333 
TRP N     CA     sing N N 334 
TRP N     H      sing N N 335 
TRP N     H2     sing N N 336 
TRP CA    C      sing N N 337 
TRP CA    CB     sing N N 338 
TRP CA    HA     sing N N 339 
TRP C     O      doub N N 340 
TRP C     OXT    sing N N 341 
TRP CB    CG     sing N N 342 
TRP CB    HB2    sing N N 343 
TRP CB    HB3    sing N N 344 
TRP CG    CD1    doub Y N 345 
TRP CG    CD2    sing Y N 346 
TRP CD1   NE1    sing Y N 347 
TRP CD1   HD1    sing N N 348 
TRP CD2   CE2    doub Y N 349 
TRP CD2   CE3    sing Y N 350 
TRP NE1   CE2    sing Y N 351 
TRP NE1   HE1    sing N N 352 
TRP CE2   CZ2    sing Y N 353 
TRP CE3   CZ3    doub Y N 354 
TRP CE3   HE3    sing N N 355 
TRP CZ2   CH2    doub Y N 356 
TRP CZ2   HZ2    sing N N 357 
TRP CZ3   CH2    sing Y N 358 
TRP CZ3   HZ3    sing N N 359 
TRP CH2   HH2    sing N N 360 
TRP OXT   HXT    sing N N 361 
TYR N     CA     sing N N 362 
TYR N     H      sing N N 363 
TYR N     H2     sing N N 364 
TYR CA    C      sing N N 365 
TYR CA    CB     sing N N 366 
TYR CA    HA     sing N N 367 
TYR C     O      doub N N 368 
TYR C     OXT    sing N N 369 
TYR CB    CG     sing N N 370 
TYR CB    HB2    sing N N 371 
TYR CB    HB3    sing N N 372 
TYR CG    CD1    doub Y N 373 
TYR CG    CD2    sing Y N 374 
TYR CD1   CE1    sing Y N 375 
TYR CD1   HD1    sing N N 376 
TYR CD2   CE2    doub Y N 377 
TYR CD2   HD2    sing N N 378 
TYR CE1   CZ     doub Y N 379 
TYR CE1   HE1    sing N N 380 
TYR CE2   CZ     sing Y N 381 
TYR CE2   HE2    sing N N 382 
TYR CZ    OH     sing N N 383 
TYR OH    HH     sing N N 384 
TYR OXT   HXT    sing N N 385 
VAL N     CA     sing N N 386 
VAL N     H      sing N N 387 
VAL N     H2     sing N N 388 
VAL CA    C      sing N N 389 
VAL CA    CB     sing N N 390 
VAL CA    HA     sing N N 391 
VAL C     O      doub N N 392 
VAL C     OXT    sing N N 393 
VAL CB    CG1    sing N N 394 
VAL CB    CG2    sing N N 395 
VAL CB    HB     sing N N 396 
VAL CG1   HG11   sing N N 397 
VAL CG1   HG12   sing N N 398 
VAL CG1   HG13   sing N N 399 
VAL CG2   HG21   sing N N 400 
VAL CG2   HG22   sing N N 401 
VAL CG2   HG23   sing N N 402 
VAL OXT   HXT    sing N N 403 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           527572100 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H8L 
_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]   0.006266 
_atom_sites.fract_transf_matrix[1][2]   0.003618 
_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]   0.007235 
_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]   0.014830 
_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 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . SER A 1 11  ? 53.841 37.608 5.051   1.00 86.72  ? 11  SER A N     1 
ATOM   2    C CA    . SER A 1 11  ? 55.200 38.136 4.945   1.00 93.74  ? 11  SER A CA    1 
ATOM   3    C C     . SER A 1 11  ? 55.354 39.040 3.723   1.00 99.36  ? 11  SER A C     1 
ATOM   4    O O     . SER A 1 11  ? 54.620 38.910 2.743   1.00 102.11 ? 11  SER A O     1 
ATOM   5    C CB    . SER A 1 11  ? 56.223 36.996 4.886   1.00 91.53  ? 11  SER A CB    1 
ATOM   6    O OG    . SER A 1 11  ? 56.294 36.307 6.122   1.00 90.35  ? 11  SER A OG    1 
ATOM   7    N N     . ILE A 1 12  ? 56.317 39.956 3.795   1.00 97.75  ? 12  ILE A N     1 
ATOM   8    C CA    . ILE A 1 12  ? 56.582 40.909 2.727   1.00 88.29  ? 12  ILE A CA    1 
ATOM   9    C C     . ILE A 1 12  ? 57.959 40.620 2.144   1.00 82.25  ? 12  ILE A C     1 
ATOM   10   O O     . ILE A 1 12  ? 58.798 39.950 2.755   1.00 85.54  ? 12  ILE A O     1 
ATOM   11   C CB    . ILE A 1 12  ? 56.503 42.370 3.218   1.00 74.44  ? 12  ILE A CB    1 
ATOM   12   C CG1   . ILE A 1 12  ? 57.539 42.611 4.320   1.00 72.25  ? 12  ILE A CG1   1 
ATOM   13   C CG2   . ILE A 1 12  ? 55.100 42.709 3.692   1.00 70.24  ? 12  ILE A CG2   1 
ATOM   14   C CD1   . ILE A 1 12  ? 57.770 44.071 4.649   1.00 62.71  ? 12  ILE A CD1   1 
ATOM   15   N N     . GLU A 1 13  ? 58.184 41.135 0.937   1.00 76.84  ? 13  GLU A N     1 
ATOM   16   C CA    . GLU A 1 13  ? 59.521 41.143 0.362   1.00 84.87  ? 13  GLU A CA    1 
ATOM   17   C C     . GLU A 1 13  ? 60.399 42.142 1.109   1.00 82.24  ? 13  GLU A C     1 
ATOM   18   O O     . GLU A 1 13  ? 59.924 43.160 1.621   1.00 81.91  ? 13  GLU A O     1 
ATOM   19   C CB    . GLU A 1 13  ? 59.468 41.498 -1.126  1.00 93.00  ? 13  GLU A CB    1 
ATOM   20   C CG    . GLU A 1 13  ? 60.804 41.368 -1.862  1.00 94.77  ? 13  GLU A CG    1 
ATOM   21   C CD    . GLU A 1 13  ? 60.822 42.121 -3.184  1.00 102.20 ? 13  GLU A CD    1 
ATOM   22   O OE1   . GLU A 1 13  ? 59.785 42.717 -3.552  1.00 104.40 ? 13  GLU A OE1   1 
ATOM   23   O OE2   . GLU A 1 13  ? 61.878 42.122 -3.853  1.00 94.03  ? 13  GLU A OE2   1 
ATOM   24   N N     . LEU A 1 14  ? 61.691 41.842 1.175   1.00 83.02  ? 14  LEU A N     1 
ATOM   25   C CA    . LEU A 1 14  ? 62.642 42.653 1.919   1.00 76.11  ? 14  LEU A CA    1 
ATOM   26   C C     . LEU A 1 14  ? 63.727 43.179 0.987   1.00 74.63  ? 14  LEU A C     1 
ATOM   27   O O     . LEU A 1 14  ? 64.035 42.568 -0.043  1.00 72.60  ? 14  LEU A O     1 
ATOM   28   C CB    . LEU A 1 14  ? 63.277 41.838 3.064   1.00 69.32  ? 14  LEU A CB    1 
ATOM   29   C CG    . LEU A 1 14  ? 62.658 41.772 4.473   1.00 72.36  ? 14  LEU A CG    1 
ATOM   30   C CD1   . LEU A 1 14  ? 61.143 41.957 4.512   1.00 65.80  ? 14  LEU A CD1   1 
ATOM   31   C CD2   . LEU A 1 14  ? 63.040 40.447 5.117   1.00 62.63  ? 14  LEU A CD2   1 
ATOM   32   N N     . ASP A 1 15  ? 64.306 44.322 1.355   1.00 71.04  ? 15  ASP A N     1 
ATOM   33   C CA    . ASP A 1 15  ? 65.494 44.796 0.660   1.00 68.38  ? 15  ASP A CA    1 
ATOM   34   C C     . ASP A 1 15  ? 66.694 43.921 1.032   1.00 61.83  ? 15  ASP A C     1 
ATOM   35   O O     . ASP A 1 15  ? 66.606 43.028 1.876   1.00 67.89  ? 15  ASP A O     1 
ATOM   36   C CB    . ASP A 1 15  ? 65.738 46.278 0.973   1.00 76.94  ? 15  ASP A CB    1 
ATOM   37   C CG    . ASP A 1 15  ? 66.215 46.528 2.399   1.00 67.03  ? 15  ASP A CG    1 
ATOM   38   O OD1   . ASP A 1 15  ? 66.337 45.582 3.207   1.00 70.66  ? 15  ASP A OD1   1 
ATOM   39   O OD2   . ASP A 1 15  ? 66.474 47.705 2.713   1.00 67.19  ? 15  ASP A OD2   1 
ATOM   40   N N     . LYS A 1 16  ? 67.841 44.195 0.409   1.00 63.08  ? 16  LYS A N     1 
ATOM   41   C CA    . LYS A 1 16  ? 68.967 43.273 0.521   1.00 65.34  ? 16  LYS A CA    1 
ATOM   42   C C     . LYS A 1 16  ? 69.500 43.189 1.952   1.00 61.40  ? 16  LYS A C     1 
ATOM   43   O O     . LYS A 1 16  ? 69.852 42.103 2.422   1.00 53.95  ? 16  LYS A O     1 
ATOM   44   C CB    . LYS A 1 16  ? 70.080 43.674 -0.448  1.00 73.29  ? 16  LYS A CB    1 
ATOM   45   C CG    . LYS A 1 16  ? 71.146 42.594 -0.647  1.00 79.78  ? 16  LYS A CG    1 
ATOM   46   C CD    . LYS A 1 16  ? 72.239 43.058 -1.604  1.00 91.81  ? 16  LYS A CD    1 
ATOM   47   C CE    . LYS A 1 16  ? 73.388 42.056 -1.664  1.00 95.04  ? 16  LYS A CE    1 
ATOM   48   N NZ    . LYS A 1 16  ? 74.513 42.529 -2.522  1.00 96.27  ? 16  LYS A NZ    1 
ATOM   49   N N     . LYS A 1 17  ? 69.570 44.317 2.665   1.00 62.83  ? 17  LYS A N     1 
ATOM   50   C CA    . LYS A 1 17  ? 70.113 44.284 4.024   1.00 60.13  ? 17  LYS A CA    1 
ATOM   51   C C     . LYS A 1 17  ? 69.205 43.494 4.963   1.00 55.71  ? 17  LYS A C     1 
ATOM   52   O O     . LYS A 1 17  ? 69.679 42.688 5.781   1.00 50.30  ? 17  LYS A O     1 
ATOM   53   C CB    . LYS A 1 17  ? 70.321 45.707 4.543   1.00 58.49  ? 17  LYS A CB    1 
ATOM   54   C CG    . LYS A 1 17  ? 71.409 46.494 3.822   1.00 64.58  ? 17  LYS A CG    1 
ATOM   55   C CD    . LYS A 1 17  ? 71.643 47.837 4.493   1.00 65.39  ? 17  LYS A CD    1 
ATOM   56   C CE    . LYS A 1 17  ? 72.839 48.565 3.887   1.00 66.00  ? 17  LYS A CE    1 
ATOM   57   N NZ    . LYS A 1 17  ? 73.039 49.928 4.468   1.00 73.86  ? 17  LYS A NZ    1 
ATOM   58   N N     . MET A 1 18  ? 67.893 43.688 4.840   1.00 56.32  ? 18  MET A N     1 
ATOM   59   C CA    . MET A 1 18  ? 66.975 42.954 5.698   1.00 56.25  ? 18  MET A CA    1 
ATOM   60   C C     . MET A 1 18  ? 66.888 41.494 5.280   1.00 50.75  ? 18  MET A C     1 
ATOM   61   O O     . MET A 1 18  ? 66.777 40.608 6.136   1.00 52.91  ? 18  MET A O     1 
ATOM   62   C CB    . MET A 1 18  ? 65.601 43.615 5.683   1.00 54.10  ? 18  MET A CB    1 
ATOM   63   C CG    . MET A 1 18  ? 65.006 43.819 7.075   1.00 62.93  ? 18  MET A CG    1 
ATOM   64   S SD    . MET A 1 18  ? 66.044 44.781 8.211   1.00 60.50  ? 18  MET A SD    1 
ATOM   65   C CE    . MET A 1 18  ? 66.359 46.187 7.190   1.00 62.01  ? 18  MET A CE    1 
ATOM   66   N N     . TYR A 1 19  ? 66.934 41.224 3.970   1.00 51.54  ? 19  TYR A N     1 
ATOM   67   C CA    . TYR A 1 19  ? 67.058 39.846 3.511   1.00 47.61  ? 19  TYR A CA    1 
ATOM   68   C C     . TYR A 1 19  ? 68.270 39.174 4.141   1.00 48.39  ? 19  TYR A C     1 
ATOM   69   O O     . TYR A 1 19  ? 68.186 38.037 4.608   1.00 41.79  ? 19  TYR A O     1 
ATOM   70   C CB    . TYR A 1 19  ? 67.159 39.779 1.985   1.00 49.22  ? 19  TYR A CB    1 
ATOM   71   C CG    . TYR A 1 19  ? 67.809 38.493 1.495   1.00 50.23  ? 19  TYR A CG    1 
ATOM   72   C CD1   . TYR A 1 19  ? 67.078 37.311 1.380   1.00 48.79  ? 19  TYR A CD1   1 
ATOM   73   C CD2   . TYR A 1 19  ? 69.160 38.457 1.161   1.00 49.81  ? 19  TYR A CD2   1 
ATOM   74   C CE1   . TYR A 1 19  ? 67.676 36.134 0.938   1.00 45.06  ? 19  TYR A CE1   1 
ATOM   75   C CE2   . TYR A 1 19  ? 69.760 37.287 0.722   1.00 53.60  ? 19  TYR A CE2   1 
ATOM   76   C CZ    . TYR A 1 19  ? 69.015 36.129 0.613   1.00 50.72  ? 19  TYR A CZ    1 
ATOM   77   O OH    . TYR A 1 19  ? 69.625 34.970 0.174   1.00 58.14  ? 19  TYR A OH    1 
ATOM   78   N N     . LYS A 1 20  ? 69.414 39.862 4.150   1.00 47.50  ? 20  LYS A N     1 
ATOM   79   C CA    . LYS A 1 20  ? 70.621 39.257 4.698   1.00 47.24  ? 20  LYS A CA    1 
ATOM   80   C C     . LYS A 1 20  ? 70.444 38.937 6.178   1.00 44.51  ? 20  LYS A C     1 
ATOM   81   O O     . LYS A 1 20  ? 70.812 37.846 6.633   1.00 43.21  ? 20  LYS A O     1 
ATOM   82   C CB    . LYS A 1 20  ? 71.815 40.184 4.471   1.00 52.67  ? 20  LYS A CB    1 
ATOM   83   C CG    . LYS A 1 20  ? 73.171 39.535 4.708   1.00 69.90  ? 20  LYS A CG    1 
ATOM   84   C CD    . LYS A 1 20  ? 74.313 40.478 4.325   1.00 84.52  ? 20  LYS A CD    1 
ATOM   85   C CE    . LYS A 1 20  ? 75.681 39.856 4.616   1.00 87.91  ? 20  LYS A CE    1 
ATOM   86   N NZ    . LYS A 1 20  ? 76.813 40.770 4.277   1.00 98.84  ? 20  LYS A NZ    1 
ATOM   87   N N     . LYS A 1 21  ? 69.850 39.866 6.942   1.00 45.32  ? 21  LYS A N     1 
ATOM   88   C CA    . LYS A 1 21  ? 69.648 39.608 8.371   1.00 44.85  ? 21  LYS A CA    1 
ATOM   89   C C     . LYS A 1 21  ? 68.691 38.435 8.605   1.00 44.14  ? 21  LYS A C     1 
ATOM   90   O O     . LYS A 1 21  ? 68.944 37.562 9.452   1.00 45.33  ? 21  LYS A O     1 
ATOM   91   C CB    . LYS A 1 21  ? 69.140 40.874 9.063   1.00 46.82  ? 21  LYS A CB    1 
ATOM   92   C CG    . LYS A 1 21  ? 70.211 41.919 9.247   1.00 49.98  ? 21  LYS A CG    1 
ATOM   93   C CD    . LYS A 1 21  ? 69.601 43.299 9.257   1.00 62.32  ? 21  LYS A CD    1 
ATOM   94   C CE    . LYS A 1 21  ? 69.928 44.052 10.519  1.00 60.15  ? 21  LYS A CE    1 
ATOM   95   N NZ    . LYS A 1 21  ? 71.381 44.298 10.686  1.00 61.35  ? 21  LYS A NZ    1 
ATOM   96   N N     . LYS A 1 22  ? 67.580 38.398 7.862   1.00 44.07  ? 22  LYS A N     1 
ATOM   97   C CA    . LYS A 1 22  ? 66.614 37.315 8.027   1.00 43.56  ? 22  LYS A CA    1 
ATOM   98   C C     . LYS A 1 22  ? 67.220 35.975 7.634   1.00 41.77  ? 22  LYS A C     1 
ATOM   99   O O     . LYS A 1 22  ? 66.991 34.956 8.302   1.00 44.59  ? 22  LYS A O     1 
ATOM   100  C CB    . LYS A 1 22  ? 65.363 37.601 7.198   1.00 47.65  ? 22  LYS A CB    1 
ATOM   101  C CG    . LYS A 1 22  ? 64.218 36.614 7.411   1.00 47.28  ? 22  LYS A CG    1 
ATOM   102  C CD    . LYS A 1 22  ? 62.918 37.214 6.862   1.00 64.33  ? 22  LYS A CD    1 
ATOM   103  C CE    . LYS A 1 22  ? 61.687 36.400 7.245   1.00 70.62  ? 22  LYS A CE    1 
ATOM   104  N NZ    . LYS A 1 22  ? 60.440 36.997 6.669   1.00 77.39  ? 22  LYS A NZ    1 
ATOM   105  N N     . LEU A 1 23  ? 67.996 35.963 6.547   1.00 40.81  ? 23  LEU A N     1 
ATOM   106  C CA    . LEU A 1 23  ? 68.702 34.757 6.131   1.00 40.64  ? 23  LEU A CA    1 
ATOM   107  C C     . LEU A 1 23  ? 69.653 34.276 7.218   1.00 40.76  ? 23  LEU A C     1 
ATOM   108  O O     . LEU A 1 23  ? 69.726 33.075 7.498   1.00 40.55  ? 23  LEU A O     1 
ATOM   109  C CB    . LEU A 1 23  ? 69.465 35.024 4.832   1.00 41.02  ? 23  LEU A CB    1 
ATOM   110  C CG    . LEU A 1 23  ? 70.309 33.871 4.275   1.00 49.06  ? 23  LEU A CG    1 
ATOM   111  C CD1   . LEU A 1 23  ? 69.390 32.788 3.760   1.00 42.87  ? 23  LEU A CD1   1 
ATOM   112  C CD2   . LEU A 1 23  ? 71.275 34.338 3.173   1.00 39.97  ? 23  LEU A CD2   1 
ATOM   113  N N     . LYS A 1 24  ? 70.399 35.199 7.834   1.00 41.81  ? 24  LYS A N     1 
ATOM   114  C CA    . LYS A 1 24  ? 71.345 34.806 8.881   1.00 45.84  ? 24  LYS A CA    1 
ATOM   115  C C     . LYS A 1 24  ? 70.632 34.180 10.075  1.00 42.16  ? 24  LYS A C     1 
ATOM   116  O O     . LYS A 1 24  ? 71.087 33.164 10.626  1.00 42.21  ? 24  LYS A O     1 
ATOM   117  C CB    . LYS A 1 24  ? 72.167 36.015 9.327   1.00 45.99  ? 24  LYS A CB    1 
ATOM   118  C CG    . LYS A 1 24  ? 73.232 36.426 8.330   1.00 55.00  ? 24  LYS A CG    1 
ATOM   119  C CD    . LYS A 1 24  ? 73.768 37.814 8.656   1.00 56.71  ? 24  LYS A CD    1 
ATOM   120  C CE    . LYS A 1 24  ? 74.877 38.170 7.694   1.00 62.38  ? 24  LYS A CE    1 
ATOM   121  N NZ    . LYS A 1 24  ? 75.680 39.321 8.187   1.00 91.03  ? 24  LYS A NZ    1 
ATOM   122  N N     . VAL A 1 25  ? 69.508 34.761 10.490  1.00 43.98  ? 25  VAL A N     1 
ATOM   123  C CA    . VAL A 1 25  ? 68.770 34.150 11.595  1.00 42.44  ? 25  VAL A CA    1 
ATOM   124  C C     . VAL A 1 25  ? 68.268 32.764 11.198  1.00 41.13  ? 25  VAL A C     1 
ATOM   125  O O     . VAL A 1 25  ? 68.383 31.801 11.966  1.00 41.72  ? 25  VAL A O     1 
ATOM   126  C CB    . VAL A 1 25  ? 67.619 35.055 12.064  1.00 47.33  ? 25  VAL A CB    1 
ATOM   127  C CG1   . VAL A 1 25  ? 66.813 34.343 13.158  1.00 44.81  ? 25  VAL A CG1   1 
ATOM   128  C CG2   . VAL A 1 25  ? 68.166 36.385 12.574  1.00 45.53  ? 25  VAL A CG2   1 
ATOM   129  N N     . LEU A 1 26  ? 67.692 32.638 9.997   1.00 42.69  ? 26  LEU A N     1 
ATOM   130  C CA    . LEU A 1 26  ? 67.157 31.334 9.615   1.00 39.89  ? 26  LEU A CA    1 
ATOM   131  C C     . LEU A 1 26  ? 68.262 30.291 9.514   1.00 39.90  ? 26  LEU A C     1 
ATOM   132  O O     . LEU A 1 26  ? 68.051 29.126 9.874   1.00 41.15  ? 26  LEU A O     1 
ATOM   133  C CB    . LEU A 1 26  ? 66.376 31.437 8.302   1.00 42.65  ? 26  LEU A CB    1 
ATOM   134  C CG    . LEU A 1 26  ? 65.044 32.194 8.400   1.00 45.65  ? 26  LEU A CG    1 
ATOM   135  C CD1   . LEU A 1 26  ? 64.455 32.487 7.026   1.00 41.30  ? 26  LEU A CD1   1 
ATOM   136  C CD2   . LEU A 1 26  ? 64.036 31.428 9.251   1.00 42.39  ? 26  LEU A CD2   1 
ATOM   137  N N     . GLN A 1 27  ? 69.457 30.687 9.070   1.00 37.54  ? 27  GLN A N     1 
ATOM   138  C CA    . GLN A 1 27  ? 70.540 29.712 8.957   1.00 39.16  ? 27  GLN A CA    1 
ATOM   139  C C     . GLN A 1 27  ? 71.054 29.302 10.331  1.00 42.57  ? 27  GLN A C     1 
ATOM   140  O O     . GLN A 1 27  ? 71.444 28.144 10.528  1.00 37.11  ? 27  GLN A O     1 
ATOM   141  C CB    . GLN A 1 27  ? 71.680 30.272 8.107   1.00 36.14  ? 27  GLN A CB    1 
ATOM   142  C CG    . GLN A 1 27  ? 71.346 30.458 6.642   1.00 39.53  ? 27  GLN A CG    1 
ATOM   143  C CD    . GLN A 1 27  ? 72.423 31.242 5.915   1.00 44.41  ? 27  GLN A CD    1 
ATOM   144  O OE1   . GLN A 1 27  ? 73.013 32.165 6.478   1.00 43.07  ? 27  GLN A OE1   1 
ATOM   145  N NE2   . GLN A 1 27  ? 72.693 30.873 4.664   1.00 34.98  ? 27  GLN A NE2   1 
ATOM   146  N N     . TYR A 1 28  ? 71.064 30.236 11.295  1.00 38.77  ? 28  TYR A N     1 
ATOM   147  C CA    . TYR A 1 28  ? 71.370 29.851 12.674  1.00 39.45  ? 28  TYR A CA    1 
ATOM   148  C C     . TYR A 1 28  ? 70.354 28.844 13.189  1.00 43.77  ? 28  TYR A C     1 
ATOM   149  O O     . TYR A 1 28  ? 70.719 27.841 13.821  1.00 40.91  ? 28  TYR A O     1 
ATOM   150  C CB    . TYR A 1 28  ? 71.406 31.086 13.573  1.00 41.23  ? 28  TYR A CB    1 
ATOM   151  C CG    . TYR A 1 28  ? 71.559 30.826 15.065  1.00 47.68  ? 28  TYR A CG    1 
ATOM   152  C CD1   . TYR A 1 28  ? 72.804 30.568 15.628  1.00 44.33  ? 28  TYR A CD1   1 
ATOM   153  C CD2   . TYR A 1 28  ? 70.461 30.892 15.919  1.00 54.23  ? 28  TYR A CD2   1 
ATOM   154  C CE1   . TYR A 1 28  ? 72.950 30.368 17.008  1.00 48.86  ? 28  TYR A CE1   1 
ATOM   155  C CE2   . TYR A 1 28  ? 70.594 30.692 17.295  1.00 52.55  ? 28  TYR A CE2   1 
ATOM   156  C CZ    . TYR A 1 28  ? 71.840 30.428 17.834  1.00 53.83  ? 28  TYR A CZ    1 
ATOM   157  O OH    . TYR A 1 28  ? 71.973 30.230 19.197  1.00 57.67  ? 28  TYR A OH    1 
ATOM   158  N N     . GLU A 1 29  ? 69.069 29.091 12.920  1.00 42.26  ? 29  GLU A N     1 
ATOM   159  C CA    . GLU A 1 29  ? 68.037 28.154 13.351  1.00 40.09  ? 29  GLU A CA    1 
ATOM   160  C C     . GLU A 1 29  ? 68.196 26.799 12.672  1.00 42.11  ? 29  GLU A C     1 
ATOM   161  O O     . GLU A 1 29  ? 67.911 25.760 13.278  1.00 41.41  ? 29  GLU A O     1 
ATOM   162  C CB    . GLU A 1 29  ? 66.651 28.736 13.080  1.00 42.71  ? 29  GLU A CB    1 
ATOM   163  C CG    . GLU A 1 29  ? 66.274 29.881 14.028  1.00 48.12  ? 29  GLU A CG    1 
ATOM   164  C CD    . GLU A 1 29  ? 64.933 30.508 13.688  1.00 51.52  ? 29  GLU A CD    1 
ATOM   165  O OE1   . GLU A 1 29  ? 63.982 29.760 13.372  1.00 61.85  ? 29  GLU A OE1   1 
ATOM   166  O OE2   . GLU A 1 29  ? 64.832 31.752 13.728  1.00 65.83  ? 29  GLU A OE2   1 
ATOM   167  N N     . MET A 1 30  ? 68.665 26.785 11.426  1.00 39.26  ? 30  MET A N     1 
ATOM   168  C CA    . MET A 1 30  ? 68.898 25.512 10.750  1.00 36.39  ? 30  MET A CA    1 
ATOM   169  C C     . MET A 1 30  ? 70.061 24.757 11.387  1.00 39.89  ? 30  MET A C     1 
ATOM   170  O O     . MET A 1 30  ? 70.002 23.533 11.545  1.00 35.30  ? 30  MET A O     1 
ATOM   171  C CB    . MET A 1 30  ? 69.162 25.740 9.259   1.00 35.40  ? 30  MET A CB    1 
ATOM   172  C CG    . MET A 1 30  ? 69.223 24.443 8.479   1.00 43.48  ? 30  MET A CG    1 
ATOM   173  S SD    . MET A 1 30  ? 67.639 23.569 8.530   1.00 42.82  ? 30  MET A SD    1 
ATOM   174  C CE    . MET A 1 30  ? 68.162 21.861 8.387   1.00 45.09  ? 30  MET A CE    1 
ATOM   175  N N     . LEU A 1 31  ? 71.136 25.469 11.737  1.00 40.04  ? 31  LEU A N     1 
ATOM   176  C CA    . LEU A 1 31  ? 72.235 24.832 12.463  1.00 38.56  ? 31  LEU A CA    1 
ATOM   177  C C     . LEU A 1 31  ? 71.738 24.229 13.775  1.00 41.93  ? 31  LEU A C     1 
ATOM   178  O O     . LEU A 1 31  ? 72.081 23.088 14.126  1.00 41.65  ? 31  LEU A O     1 
ATOM   179  C CB    . LEU A 1 31  ? 73.342 25.849 12.721  1.00 38.79  ? 31  LEU A CB    1 
ATOM   180  C CG    . LEU A 1 31  ? 74.391 25.493 13.772  1.00 44.40  ? 31  LEU A CG    1 
ATOM   181  C CD1   . LEU A 1 31  ? 75.158 24.244 13.346  1.00 42.34  ? 31  LEU A CD1   1 
ATOM   182  C CD2   . LEU A 1 31  ? 75.335 26.665 14.001  1.00 43.74  ? 31  LEU A CD2   1 
ATOM   183  N N     . ASN A 1 32  ? 70.910 24.980 14.505  1.00 42.96  ? 32  ASN A N     1 
ATOM   184  C CA    . ASN A 1 32  ? 70.356 24.453 15.749  1.00 44.17  ? 32  ASN A CA    1 
ATOM   185  C C     . ASN A 1 32  ? 69.499 23.221 15.501  1.00 41.19  ? 32  ASN A C     1 
ATOM   186  O O     . ASN A 1 32  ? 69.574 22.246 16.254  1.00 43.35  ? 32  ASN A O     1 
ATOM   187  C CB    . ASN A 1 32  ? 69.524 25.500 16.468  1.00 44.67  ? 32  ASN A CB    1 
ATOM   188  C CG    . ASN A 1 32  ? 68.942 24.955 17.753  1.00 57.31  ? 32  ASN A CG    1 
ATOM   189  O OD1   . ASN A 1 32  ? 69.651 24.809 18.745  1.00 52.42  ? 32  ASN A OD1   1 
ATOM   190  N ND2   . ASN A 1 32  ? 67.661 24.602 17.727  1.00 53.37  ? 32  ASN A ND2   1 
ATOM   191  N N     . ALA A 1 33  ? 68.662 23.261 14.463  1.00 41.73  ? 33  ALA A N     1 
ATOM   192  C CA    . ALA A 1 33  ? 67.804 22.128 14.137  1.00 42.95  ? 33  ALA A CA    1 
ATOM   193  C C     . ALA A 1 33  ? 68.628 20.902 13.777  1.00 41.22  ? 33  ALA A C     1 
ATOM   194  O O     . ALA A 1 33  ? 68.269 19.776 14.136  1.00 46.32  ? 33  ALA A O     1 
ATOM   195  C CB    . ALA A 1 33  ? 66.867 22.505 12.987  1.00 42.37  ? 33  ALA A CB    1 
ATOM   196  N N     . GLN A 1 34  ? 69.746 21.103 13.081  1.00 35.39  ? 34  GLN A N     1 
ATOM   197  C CA    . GLN A 1 34  ? 70.639 19.985 12.788  1.00 37.18  ? 34  GLN A CA    1 
ATOM   198  C C     . GLN A 1 34  ? 71.202 19.379 14.069  1.00 41.70  ? 34  GLN A C     1 
ATOM   199  O O     . GLN A 1 34  ? 71.233 18.150 14.231  1.00 38.02  ? 34  GLN A O     1 
ATOM   200  C CB    . GLN A 1 34  ? 71.782 20.435 11.882  1.00 37.70  ? 34  GLN A CB    1 
ATOM   201  C CG    . GLN A 1 34  ? 72.762 19.302 11.576  1.00 46.17  ? 34  GLN A CG    1 
ATOM   202  C CD    . GLN A 1 34  ? 74.210 19.718 11.725  1.00 54.10  ? 34  GLN A CD    1 
ATOM   203  O OE1   . GLN A 1 34  ? 74.551 20.518 12.592  1.00 51.99  ? 34  GLN A OE1   1 
ATOM   204  N NE2   . GLN A 1 34  ? 75.069 19.190 10.858  1.00 62.28  ? 34  GLN A NE2   1 
ATOM   205  N N     . GLN A 1 35  ? 71.676 20.227 14.990  1.00 40.20  ? 35  GLN A N     1 
ATOM   206  C CA    . GLN A 1 35  ? 72.189 19.686 16.252  1.00 37.88  ? 35  GLN A CA    1 
ATOM   207  C C     . GLN A 1 35  ? 71.090 18.967 17.031  1.00 41.29  ? 35  GLN A C     1 
ATOM   208  O O     . GLN A 1 35  ? 71.332 17.917 17.639  1.00 46.28  ? 35  GLN A O     1 
ATOM   209  C CB    . GLN A 1 35  ? 72.825 20.798 17.089  1.00 39.25  ? 35  GLN A CB    1 
ATOM   210  C CG    . GLN A 1 35  ? 74.092 21.343 16.460  1.00 46.75  ? 35  GLN A CG    1 
ATOM   211  C CD    . GLN A 1 35  ? 75.153 20.268 16.274  1.00 55.35  ? 35  GLN A CD    1 
ATOM   212  O OE1   . GLN A 1 35  ? 75.561 19.612 17.234  1.00 53.04  ? 35  GLN A OE1   1 
ATOM   213  N NE2   . GLN A 1 35  ? 75.599 20.078 15.036  1.00 42.51  ? 35  GLN A NE2   1 
ATOM   214  N N     . PHE A 1 36  ? 69.867 19.497 16.991  1.00 42.17  ? 36  PHE A N     1 
ATOM   215  C CA    . PHE A 1 36  ? 68.728 18.841 17.630  1.00 40.66  ? 36  PHE A CA    1 
ATOM   216  C C     . PHE A 1 36  ? 68.448 17.468 17.028  1.00 42.62  ? 36  PHE A C     1 
ATOM   217  O O     . PHE A 1 36  ? 68.200 16.499 17.756  1.00 45.21  ? 36  PHE A O     1 
ATOM   218  C CB    . PHE A 1 36  ? 67.493 19.724 17.498  1.00 45.18  ? 36  PHE A CB    1 
ATOM   219  C CG    . PHE A 1 36  ? 66.243 19.098 18.037  1.00 55.49  ? 36  PHE A CG    1 
ATOM   220  C CD1   . PHE A 1 36  ? 65.982 19.117 19.396  1.00 52.18  ? 36  PHE A CD1   1 
ATOM   221  C CD2   . PHE A 1 36  ? 65.321 18.504 17.189  1.00 56.01  ? 36  PHE A CD2   1 
ATOM   222  C CE1   . PHE A 1 36  ? 64.827 18.556 19.899  1.00 59.53  ? 36  PHE A CE1   1 
ATOM   223  C CE2   . PHE A 1 36  ? 64.164 17.934 17.693  1.00 53.23  ? 36  PHE A CE2   1 
ATOM   224  C CZ    . PHE A 1 36  ? 63.919 17.963 19.043  1.00 53.47  ? 36  PHE A CZ    1 
ATOM   225  N N     . LEU A 1 37  ? 68.428 17.376 15.690  1.00 41.93  ? 37  LEU A N     1 
ATOM   226  C CA    . LEU A 1 37  ? 68.138 16.096 15.045  1.00 43.71  ? 37  LEU A CA    1 
ATOM   227  C C     . LEU A 1 37  ? 69.242 15.085 15.321  1.00 45.16  ? 37  LEU A C     1 
ATOM   228  O O     . LEU A 1 37  ? 68.974 13.886 15.480  1.00 43.98  ? 37  LEU A O     1 
ATOM   229  C CB    . LEU A 1 37  ? 67.954 16.287 13.532  1.00 38.22  ? 37  LEU A CB    1 
ATOM   230  C CG    . LEU A 1 37  ? 66.731 17.107 13.093  1.00 40.90  ? 37  LEU A CG    1 
ATOM   231  C CD1   . LEU A 1 37  ? 66.759 17.380 11.605  1.00 44.48  ? 37  LEU A CD1   1 
ATOM   232  C CD2   . LEU A 1 37  ? 65.430 16.412 13.480  1.00 46.80  ? 37  LEU A CD2   1 
ATOM   233  N N     . LEU A 1 38  ? 70.489 15.554 15.373  1.00 40.09  ? 38  LEU A N     1 
ATOM   234  C CA    . LEU A 1 38  ? 71.603 14.677 15.710  1.00 40.29  ? 38  LEU A CA    1 
ATOM   235  C C     . LEU A 1 38  ? 71.481 14.165 17.143  1.00 44.39  ? 38  LEU A C     1 
ATOM   236  O O     . LEU A 1 38  ? 71.613 12.963 17.400  1.00 40.53  ? 38  LEU A O     1 
ATOM   237  C CB    . LEU A 1 38  ? 72.918 15.430 15.517  1.00 40.00  ? 38  LEU A CB    1 
ATOM   238  C CG    . LEU A 1 38  ? 74.187 14.637 15.816  1.00 50.74  ? 38  LEU A CG    1 
ATOM   239  C CD1   . LEU A 1 38  ? 74.337 13.508 14.802  1.00 46.19  ? 38  LEU A CD1   1 
ATOM   240  C CD2   . LEU A 1 38  ? 75.408 15.553 15.804  1.00 46.60  ? 38  LEU A CD2   1 
ATOM   241  N N     . LYS A 1 39  ? 71.212 15.069 18.086  1.00 44.37  ? 39  LYS A N     1 
ATOM   242  C CA    . LYS A 1 39  ? 71.080 14.685 19.487  1.00 47.35  ? 39  LYS A CA    1 
ATOM   243  C C     . LYS A 1 39  ? 69.966 13.666 19.673  1.00 46.02  ? 39  LYS A C     1 
ATOM   244  O O     . LYS A 1 39  ? 70.099 12.728 20.465  1.00 51.89  ? 39  LYS A O     1 
ATOM   245  C CB    . LYS A 1 39  ? 70.825 15.936 20.332  1.00 48.76  ? 39  LYS A CB    1 
ATOM   246  C CG    . LYS A 1 39  ? 70.603 15.709 21.806  1.00 57.37  ? 39  LYS A CG    1 
ATOM   247  C CD    . LYS A 1 39  ? 70.265 17.048 22.478  1.00 74.01  ? 39  LYS A CD    1 
ATOM   248  C CE    . LYS A 1 39  ? 70.270 16.965 23.997  1.00 77.79  ? 39  LYS A CE    1 
ATOM   249  N NZ    . LYS A 1 39  ? 70.164 18.326 24.619  1.00 78.89  ? 39  LYS A NZ    1 
ATOM   250  N N     . ASN A 1 40  ? 68.868 13.821 18.943  1.00 43.50  ? 40  ASN A N     1 
ATOM   251  C CA    . ASN A 1 40  ? 67.749 12.902 19.059  1.00 45.66  ? 40  ASN A CA    1 
ATOM   252  C C     . ASN A 1 40  ? 67.791 11.778 18.028  1.00 46.83  ? 40  ASN A C     1 
ATOM   253  O O     . ASN A 1 40  ? 66.829 11.010 17.931  1.00 48.25  ? 40  ASN A O     1 
ATOM   254  C CB    . ASN A 1 40  ? 66.439 13.681 18.972  1.00 40.95  ? 40  ASN A CB    1 
ATOM   255  C CG    . ASN A 1 40  ? 66.179 14.484 20.231  1.00 48.60  ? 40  ASN A CG    1 
ATOM   256  O OD1   . ASN A 1 40  ? 65.732 13.937 21.243  1.00 50.94  ? 40  ASN A OD1   1 
ATOM   257  N ND2   . ASN A 1 40  ? 66.487 15.778 20.189  1.00 43.29  ? 40  ASN A ND2   1 
ATOM   258  N N     . LYS A 1 41  ? 68.886 11.656 17.278  1.00 38.94  ? 41  LYS A N     1 
ATOM   259  C CA    . LYS A 1 41  ? 69.086 10.565 16.323  1.00 39.33  ? 41  LYS A CA    1 
ATOM   260  C C     . LYS A 1 41  ? 67.879 10.399 15.399  1.00 45.94  ? 41  LYS A C     1 
ATOM   261  O O     . LYS A 1 41  ? 67.356 9.300  15.196  1.00 41.32  ? 41  LYS A O     1 
ATOM   262  C CB    . LYS A 1 41  ? 69.412 9.260  17.050  1.00 40.07  ? 41  LYS A CB    1 
ATOM   263  C CG    . LYS A 1 41  ? 70.594 9.383  17.997  1.00 47.56  ? 41  LYS A CG    1 
ATOM   264  C CD    . LYS A 1 41  ? 70.875 8.081  18.732  1.00 60.89  ? 41  LYS A CD    1 
ATOM   265  C CE    . LYS A 1 41  ? 72.141 8.192  19.573  1.00 73.33  ? 41  LYS A CE    1 
ATOM   266  N NZ    . LYS A 1 41  ? 72.508 6.885  20.193  1.00 92.00  ? 41  LYS A NZ    1 
ATOM   267  N N     . ILE A 1 42  ? 67.431 11.517 14.835  1.00 40.41  ? 42  ILE A N     1 
ATOM   268  C CA    . ILE A 1 42  ? 66.388 11.534 13.817  1.00 39.70  ? 42  ILE A CA    1 
ATOM   269  C C     . ILE A 1 42  ? 67.019 12.022 12.524  1.00 37.78  ? 42  ILE A C     1 
ATOM   270  O O     . ILE A 1 42  ? 67.492 13.162 12.460  1.00 37.77  ? 42  ILE A O     1 
ATOM   271  C CB    . ILE A 1 42  ? 65.220 12.450 14.209  1.00 37.20  ? 42  ILE A CB    1 
ATOM   272  C CG1   . ILE A 1 42  ? 64.511 11.928 15.454  1.00 43.02  ? 42  ILE A CG1   1 
ATOM   273  C CG2   . ILE A 1 42  ? 64.267 12.631 13.016  1.00 39.37  ? 42  ILE A CG2   1 
ATOM   274  C CD1   . ILE A 1 42  ? 63.608 12.943 16.057  1.00 47.49  ? 42  ILE A CD1   1 
ATOM   275  N N     . GLY A 1 43  ? 67.005 11.179 11.490  1.00 36.19  ? 43  GLY A N     1 
ATOM   276  C CA    . GLY A 1 43  ? 67.564 11.576 10.216  1.00 32.41  ? 43  GLY A CA    1 
ATOM   277  C C     . GLY A 1 43  ? 66.653 12.522 9.441   1.00 36.55  ? 43  GLY A C     1 
ATOM   278  O O     . GLY A 1 43  ? 65.442 12.570 9.640   1.00 36.12  ? 43  GLY A O     1 
ATOM   279  N N     . LEU A 1 44  ? 67.255 13.291 8.538   1.00 33.42  ? 44  LEU A N     1 
ATOM   280  C CA    . LEU A 1 44  ? 66.525 14.270 7.737   1.00 32.01  ? 44  LEU A CA    1 
ATOM   281  C C     . LEU A 1 44  ? 66.871 14.082 6.264   1.00 32.86  ? 44  LEU A C     1 
ATOM   282  O O     . LEU A 1 44  ? 68.051 14.083 5.900   1.00 32.42  ? 44  LEU A O     1 
ATOM   283  C CB    . LEU A 1 44  ? 66.853 15.699 8.181   1.00 33.50  ? 44  LEU A CB    1 
ATOM   284  C CG    . LEU A 1 44  ? 66.231 16.825 7.349   1.00 39.87  ? 44  LEU A CG    1 
ATOM   285  C CD1   . LEU A 1 44  ? 64.713 16.844 7.520   1.00 38.71  ? 44  LEU A CD1   1 
ATOM   286  C CD2   . LEU A 1 44  ? 66.851 18.175 7.700   1.00 35.68  ? 44  LEU A CD2   1 
ATOM   287  N N     . ILE A 1 45  ? 65.841 13.932 5.429   1.00 33.10  ? 45  ILE A N     1 
ATOM   288  C CA    . ILE A 1 45  ? 65.975 13.704 3.991   1.00 39.08  ? 45  ILE A CA    1 
ATOM   289  C C     . ILE A 1 45  ? 65.241 14.819 3.248   1.00 37.92  ? 45  ILE A C     1 
ATOM   290  O O     . ILE A 1 45  ? 64.010 14.951 3.350   1.00 36.49  ? 45  ILE A O     1 
ATOM   291  C CB    . ILE A 1 45  ? 65.415 12.333 3.584   1.00 36.71  ? 45  ILE A CB    1 
ATOM   292  C CG1   . ILE A 1 45  ? 66.218 11.207 4.235   1.00 33.86  ? 45  ILE A CG1   1 
ATOM   293  C CG2   . ILE A 1 45  ? 65.385 12.189 2.074   1.00 31.85  ? 45  ILE A CG2   1 
ATOM   294  C CD1   . ILE A 1 45  ? 65.454 9.900  4.251   1.00 34.71  ? 45  ILE A CD1   1 
ATOM   295  N N     . LEU A 1 46  ? 65.990 15.602 2.486   1.00 35.44  ? 46  LEU A N     1 
ATOM   296  C CA    . LEU A 1 46  ? 65.436 16.727 1.752   1.00 34.93  ? 46  LEU A CA    1 
ATOM   297  C C     . LEU A 1 46  ? 65.567 16.450 0.265   1.00 39.20  ? 46  LEU A C     1 
ATOM   298  O O     . LEU A 1 46  ? 66.665 16.148 -0.221  1.00 38.47  ? 46  LEU A O     1 
ATOM   299  C CB    . LEU A 1 46  ? 66.141 18.030 2.122   1.00 38.53  ? 46  LEU A CB    1 
ATOM   300  C CG    . LEU A 1 46  ? 66.197 18.329 3.624   1.00 41.06  ? 46  LEU A CG    1 
ATOM   301  C CD1   . LEU A 1 46  ? 67.058 19.554 3.900   1.00 38.00  ? 46  LEU A CD1   1 
ATOM   302  C CD2   . LEU A 1 46  ? 64.785 18.519 4.199   1.00 36.19  ? 46  LEU A CD2   1 
ATOM   303  N N     . VAL A 1 47  ? 64.447 16.543 -0.445  1.00 34.95  ? 47  VAL A N     1 
ATOM   304  C CA    . VAL A 1 47  ? 64.407 16.349 -1.889  1.00 32.27  ? 47  VAL A CA    1 
ATOM   305  C C     . VAL A 1 47  ? 64.203 17.706 -2.547  1.00 35.82  ? 47  VAL A C     1 
ATOM   306  O O     . VAL A 1 47  ? 63.400 18.517 -2.077  1.00 37.20  ? 47  VAL A O     1 
ATOM   307  C CB    . VAL A 1 47  ? 63.285 15.360 -2.273  1.00 35.82  ? 47  VAL A CB    1 
ATOM   308  C CG1   . VAL A 1 47  ? 62.965 15.433 -3.758  1.00 33.41  ? 47  VAL A CG1   1 
ATOM   309  C CG2   . VAL A 1 47  ? 63.679 13.950 -1.886  1.00 33.59  ? 47  VAL A CG2   1 
ATOM   310  N N     . PHE A 1 48  ? 64.933 17.964 -3.624  1.00 30.52  ? 48  PHE A N     1 
ATOM   311  C CA    . PHE A 1 48  ? 64.717 19.169 -4.405  1.00 35.15  ? 48  PHE A CA    1 
ATOM   312  C C     . PHE A 1 48  ? 64.494 18.765 -5.853  1.00 35.03  ? 48  PHE A C     1 
ATOM   313  O O     . PHE A 1 48  ? 65.294 18.019 -6.425  1.00 39.31  ? 48  PHE A O     1 
ATOM   314  C CB    . PHE A 1 48  ? 65.896 20.147 -4.277  1.00 34.21  ? 48  PHE A CB    1 
ATOM   315  C CG    . PHE A 1 48  ? 65.977 20.836 -2.929  1.00 37.62  ? 48  PHE A CG    1 
ATOM   316  C CD1   . PHE A 1 48  ? 66.529 20.188 -1.832  1.00 31.98  ? 48  PHE A CD1   1 
ATOM   317  C CD2   . PHE A 1 48  ? 65.499 22.129 -2.764  1.00 38.44  ? 48  PHE A CD2   1 
ATOM   318  C CE1   . PHE A 1 48  ? 66.599 20.819 -0.595  1.00 37.40  ? 48  PHE A CE1   1 
ATOM   319  C CE2   . PHE A 1 48  ? 65.569 22.762 -1.532  1.00 36.67  ? 48  PHE A CE2   1 
ATOM   320  C CZ    . PHE A 1 48  ? 66.121 22.108 -0.447  1.00 37.42  ? 48  PHE A CZ    1 
ATOM   321  N N     . GLU A 1 49  ? 63.394 19.235 -6.427  1.00 38.06  ? 49  GLU A N     1 
ATOM   322  C CA    . GLU A 1 49  ? 63.089 19.027 -7.830  1.00 40.48  ? 49  GLU A CA    1 
ATOM   323  C C     . GLU A 1 49  ? 62.654 20.359 -8.427  1.00 39.98  ? 49  GLU A C     1 
ATOM   324  O O     . GLU A 1 49  ? 62.330 21.309 -7.709  1.00 40.28  ? 49  GLU A O     1 
ATOM   325  C CB    . GLU A 1 49  ? 62.001 17.950 -8.020  1.00 38.15  ? 49  GLU A CB    1 
ATOM   326  C CG    . GLU A 1 49  ? 62.372 16.557 -7.465  1.00 37.52  ? 49  GLU A CG    1 
ATOM   327  C CD    . GLU A 1 49  ? 63.385 15.817 -8.324  1.00 42.21  ? 49  GLU A CD    1 
ATOM   328  O OE1   . GLU A 1 49  ? 63.755 16.331 -9.409  1.00 40.41  ? 49  GLU A OE1   1 
ATOM   329  O OE2   . GLU A 1 49  ? 63.819 14.721 -7.912  1.00 39.97  ? 49  GLU A OE2   1 
ATOM   330  N N     . GLY A 1 50  ? 62.661 20.418 -9.746  1.00 40.27  ? 50  GLY A N     1 
ATOM   331  C CA    . GLY A 1 50  ? 62.311 21.614 -10.492 1.00 39.05  ? 50  GLY A CA    1 
ATOM   332  C C     . GLY A 1 50  ? 63.146 21.693 -11.751 1.00 44.97  ? 50  GLY A C     1 
ATOM   333  O O     . GLY A 1 50  ? 64.172 21.033 -11.896 1.00 44.61  ? 50  GLY A O     1 
ATOM   334  N N     . MET A 1 51  ? 62.697 22.526 -12.690 1.00 43.59  ? 51  MET A N     1 
ATOM   335  C CA    . MET A 1 51  ? 63.371 22.579 -13.976 1.00 43.75  ? 51  MET A CA    1 
ATOM   336  C C     . MET A 1 51  ? 64.775 23.169 -13.842 1.00 42.82  ? 51  MET A C     1 
ATOM   337  O O     . MET A 1 51  ? 65.137 23.783 -12.834 1.00 42.61  ? 51  MET A O     1 
ATOM   338  C CB    . MET A 1 51  ? 62.545 23.384 -14.985 1.00 46.53  ? 51  MET A CB    1 
ATOM   339  C CG    . MET A 1 51  ? 61.203 22.735 -15.279 1.00 49.27  ? 51  MET A CG    1 
ATOM   340  S SD    . MET A 1 51  ? 60.406 23.488 -16.703 1.00 72.69  ? 51  MET A SD    1 
ATOM   341  C CE    . MET A 1 51  ? 60.443 25.224 -16.250 1.00 60.66  ? 51  MET A CE    1 
ATOM   342  N N     . ASP A 1 52  ? 65.578 22.944 -14.875 1.00 44.84  ? 52  ASP A N     1 
ATOM   343  C CA    . ASP A 1 52  ? 66.896 23.552 -14.956 1.00 44.17  ? 52  ASP A CA    1 
ATOM   344  C C     . ASP A 1 52  ? 66.802 25.058 -14.703 1.00 42.28  ? 52  ASP A C     1 
ATOM   345  O O     . ASP A 1 52  ? 65.909 25.732 -15.223 1.00 43.61  ? 52  ASP A O     1 
ATOM   346  C CB    . ASP A 1 52  ? 67.506 23.264 -16.331 1.00 56.05  ? 52  ASP A CB    1 
ATOM   347  C CG    . ASP A 1 52  ? 69.020 23.404 -16.345 1.00 68.88  ? 52  ASP A CG    1 
ATOM   348  O OD1   . ASP A 1 52  ? 69.604 23.710 -15.278 1.00 65.88  ? 52  ASP A OD1   1 
ATOM   349  O OD2   . ASP A 1 52  ? 69.630 23.204 -17.420 1.00 70.64  ? 52  ASP A OD2   1 
ATOM   350  N N     . ALA A 1 53  ? 67.706 25.563 -13.858 1.00 41.35  ? 53  ALA A N     1 
ATOM   351  C CA    . ALA A 1 53  ? 67.808 26.969 -13.480 1.00 43.00  ? 53  ALA A CA    1 
ATOM   352  C C     . ALA A 1 53  ? 66.616 27.453 -12.663 1.00 46.43  ? 53  ALA A C     1 
ATOM   353  O O     . ALA A 1 53  ? 66.365 28.658 -12.592 1.00 46.29  ? 53  ALA A O     1 
ATOM   354  C CB    . ALA A 1 53  ? 68.004 27.875 -14.706 1.00 43.13  ? 53  ALA A CB    1 
ATOM   355  N N     . ALA A 1 54  ? 65.867 26.543 -12.040 1.00 43.15  ? 54  ALA A N     1 
ATOM   356  C CA    . ALA A 1 54  ? 64.838 26.949 -11.089 1.00 43.73  ? 54  ALA A CA    1 
ATOM   357  C C     . ALA A 1 54  ? 65.412 27.449 -9.765  1.00 43.00  ? 54  ALA A C     1 
ATOM   358  O O     . ALA A 1 54  ? 64.657 28.013 -8.965  1.00 44.74  ? 54  ALA A O     1 
ATOM   359  C CB    . ALA A 1 54  ? 63.873 25.790 -10.816 1.00 46.90  ? 54  ALA A CB    1 
ATOM   360  N N     . GLY A 1 55  ? 66.706 27.254 -9.508  1.00 40.06  ? 55  GLY A N     1 
ATOM   361  C CA    . GLY A 1 55  ? 67.328 27.715 -8.279  1.00 35.61  ? 55  GLY A CA    1 
ATOM   362  C C     . GLY A 1 55  ? 67.497 26.664 -7.191  1.00 42.69  ? 55  GLY A C     1 
ATOM   363  O O     . GLY A 1 55  ? 67.664 27.036 -6.020  1.00 37.24  ? 55  GLY A O     1 
ATOM   364  N N     . LYS A 1 56  ? 67.447 25.372 -7.544  1.00 36.35  ? 56  LYS A N     1 
ATOM   365  C CA    . LYS A 1 56  ? 67.663 24.291 -6.576  1.00 40.22  ? 56  LYS A CA    1 
ATOM   366  C C     . LYS A 1 56  ? 69.032 24.397 -5.915  1.00 36.62  ? 56  LYS A C     1 
ATOM   367  O O     . LYS A 1 56  ? 69.151 24.347 -4.684  1.00 37.17  ? 56  LYS A O     1 
ATOM   368  C CB    . LYS A 1 56  ? 67.529 22.930 -7.270  1.00 33.56  ? 56  LYS A CB    1 
ATOM   369  C CG    . LYS A 1 56  ? 66.166 22.668 -7.923  1.00 33.43  ? 56  LYS A CG    1 
ATOM   370  C CD    . LYS A 1 56  ? 66.089 21.276 -8.549  1.00 33.02  ? 56  LYS A CD    1 
ATOM   371  C CE    . LYS A 1 56  ? 67.122 21.074 -9.671  1.00 42.35  ? 56  LYS A CE    1 
ATOM   372  N NZ    . LYS A 1 56  ? 66.854 21.908 -10.895 1.00 37.84  ? 56  LYS A NZ    1 
ATOM   373  N N     . GLY A 1 57  ? 70.083 24.530 -6.724  1.00 35.49  ? 57  GLY A N     1 
ATOM   374  C CA    . GLY A 1 57  ? 71.427 24.549 -6.173  1.00 36.22  ? 57  GLY A CA    1 
ATOM   375  C C     . GLY A 1 57  ? 71.651 25.693 -5.202  1.00 36.66  ? 57  GLY A C     1 
ATOM   376  O O     . GLY A 1 57  ? 72.214 25.500 -4.119  1.00 35.45  ? 57  GLY A O     1 
ATOM   377  N N     . GLY A 1 58  ? 71.209 26.901 -5.574  1.00 37.45  ? 58  GLY A N     1 
ATOM   378  C CA    . GLY A 1 58  ? 71.430 28.057 -4.716  1.00 38.33  ? 58  GLY A CA    1 
ATOM   379  C C     . GLY A 1 58  ? 70.633 27.991 -3.423  1.00 39.31  ? 58  GLY A C     1 
ATOM   380  O O     . GLY A 1 58  ? 71.127 28.374 -2.352  1.00 42.05  ? 58  GLY A O     1 
ATOM   381  N N     . ALA A 1 59  ? 69.394 27.497 -3.500  1.00 37.35  ? 59  ALA A N     1 
ATOM   382  C CA    . ALA A 1 59  ? 68.603 27.336 -2.288  1.00 37.41  ? 59  ALA A CA    1 
ATOM   383  C C     . ALA A 1 59  ? 69.246 26.317 -1.361  1.00 40.00  ? 59  ALA A C     1 
ATOM   384  O O     . ALA A 1 59  ? 69.316 26.537 -0.144  1.00 39.07  ? 59  ALA A O     1 
ATOM   385  C CB    . ALA A 1 59  ? 67.169 26.936 -2.632  1.00 36.36  ? 59  ALA A CB    1 
ATOM   386  N N     . ILE A 1 60  ? 69.752 25.208 -1.918  1.00 34.90  ? 60  ILE A N     1 
ATOM   387  C CA    . ILE A 1 60  ? 70.470 24.239 -1.088  1.00 32.01  ? 60  ILE A CA    1 
ATOM   388  C C     . ILE A 1 60  ? 71.681 24.893 -0.431  1.00 39.23  ? 60  ILE A C     1 
ATOM   389  O O     . ILE A 1 60  ? 71.907 24.742 0.777   1.00 33.83  ? 60  ILE A O     1 
ATOM   390  C CB    . ILE A 1 60  ? 70.878 22.999 -1.905  1.00 36.12  ? 60  ILE A CB    1 
ATOM   391  C CG1   . ILE A 1 60  ? 69.639 22.197 -2.327  1.00 34.97  ? 60  ILE A CG1   1 
ATOM   392  C CG2   . ILE A 1 60  ? 71.822 22.112 -1.081  1.00 28.75  ? 60  ILE A CG2   1 
ATOM   393  C CD1   . ILE A 1 60  ? 69.930 21.133 -3.385  1.00 34.58  ? 60  ILE A CD1   1 
ATOM   394  N N     . LYS A 1 61  ? 72.479 25.632 -1.214  1.00 33.97  ? 61  LYS A N     1 
ATOM   395  C CA    . LYS A 1 61  ? 73.655 26.291 -0.645  1.00 39.45  ? 61  LYS A CA    1 
ATOM   396  C C     . LYS A 1 61  ? 73.289 27.160 0.552   1.00 37.59  ? 61  LYS A C     1 
ATOM   397  O O     . LYS A 1 61  ? 73.983 27.139 1.574   1.00 39.20  ? 61  LYS A O     1 
ATOM   398  C CB    . LYS A 1 61  ? 74.382 27.136 -1.697  1.00 36.26  ? 61  LYS A CB    1 
ATOM   399  C CG    . LYS A 1 61  ? 75.169 26.309 -2.695  1.00 49.16  ? 61  LYS A CG    1 
ATOM   400  C CD    . LYS A 1 61  ? 76.153 27.170 -3.501  1.00 64.03  ? 61  LYS A CD    1 
ATOM   401  C CE    . LYS A 1 61  ? 75.461 27.988 -4.579  1.00 73.70  ? 61  LYS A CE    1 
ATOM   402  N NZ    . LYS A 1 61  ? 76.430 28.578 -5.563  1.00 73.52  ? 61  LYS A NZ    1 
ATOM   403  N N     . ARG A 1 62  ? 72.204 27.933 0.451   1.00 36.70  ? 62  ARG A N     1 
ATOM   404  C CA    . ARG A 1 62  ? 71.856 28.769 1.603   1.00 42.99  ? 62  ARG A CA    1 
ATOM   405  C C     . ARG A 1 62  ? 71.333 27.930 2.762   1.00 40.24  ? 62  ARG A C     1 
ATOM   406  O O     . ARG A 1 62  ? 71.585 28.257 3.930   1.00 40.90  ? 62  ARG A O     1 
ATOM   407  C CB    . ARG A 1 62  ? 70.834 29.839 1.234   1.00 41.53  ? 62  ARG A CB    1 
ATOM   408  C CG    . ARG A 1 62  ? 71.451 31.109 0.685   1.00 44.89  ? 62  ARG A CG    1 
ATOM   409  C CD    . ARG A 1 62  ? 71.967 30.838 -0.693  1.00 41.53  ? 62  ARG A CD    1 
ATOM   410  N NE    . ARG A 1 62  ? 72.681 31.951 -1.302  1.00 45.40  ? 62  ARG A NE    1 
ATOM   411  C CZ    . ARG A 1 62  ? 73.096 31.944 -2.561  1.00 55.74  ? 62  ARG A CZ    1 
ATOM   412  N NH1   . ARG A 1 62  ? 72.863 30.909 -3.360  1.00 45.45  ? 62  ARG A NH1   1 
ATOM   413  N NH2   . ARG A 1 62  ? 73.765 32.994 -3.031  1.00 44.11  ? 62  ARG A NH2   1 
ATOM   414  N N     . LEU A 1 63  ? 70.622 26.846 2.461   1.00 37.95  ? 63  LEU A N     1 
ATOM   415  C CA    . LEU A 1 63  ? 70.033 26.029 3.517   1.00 40.87  ? 63  LEU A CA    1 
ATOM   416  C C     . LEU A 1 63  ? 71.101 25.446 4.438   1.00 38.72  ? 63  LEU A C     1 
ATOM   417  O O     . LEU A 1 63  ? 70.975 25.522 5.663   1.00 39.31  ? 63  LEU A O     1 
ATOM   418  C CB    . LEU A 1 63  ? 69.183 24.918 2.899   1.00 39.78  ? 63  LEU A CB    1 
ATOM   419  C CG    . LEU A 1 63  ? 68.555 23.849 3.802   1.00 41.45  ? 63  LEU A CG    1 
ATOM   420  C CD1   . LEU A 1 63  ? 67.575 24.462 4.781   1.00 41.45  ? 63  LEU A CD1   1 
ATOM   421  C CD2   . LEU A 1 63  ? 67.824 22.858 2.933   1.00 43.27  ? 63  LEU A CD2   1 
ATOM   422  N N     . ILE A 1 64  ? 72.166 24.866 3.877   1.00 34.55  ? 64  ILE A N     1 
ATOM   423  C CA    . ILE A 1 64  ? 73.152 24.176 4.712   1.00 35.81  ? 64  ILE A CA    1 
ATOM   424  C C     . ILE A 1 64  ? 74.428 24.987 4.909   1.00 39.02  ? 64  ILE A C     1 
ATOM   425  O O     . ILE A 1 64  ? 75.423 24.451 5.409   1.00 40.58  ? 64  ILE A O     1 
ATOM   426  C CB    . ILE A 1 64  ? 73.476 22.770 4.175   1.00 39.02  ? 64  ILE A CB    1 
ATOM   427  C CG1   . ILE A 1 64  ? 73.713 22.766 2.660   1.00 35.78  ? 64  ILE A CG1   1 
ATOM   428  C CG2   . ILE A 1 64  ? 72.357 21.824 4.553   1.00 39.53  ? 64  ILE A CG2   1 
ATOM   429  C CD1   . ILE A 1 64  ? 75.000 23.435 2.208   1.00 35.98  ? 64  ILE A CD1   1 
ATOM   430  N N     . GLU A 1 65  ? 74.417 26.269 4.549   1.00 36.36  ? 65  GLU A N     1 
ATOM   431  C CA    . GLU A 1 65  ? 75.640 27.061 4.560   1.00 39.15  ? 65  GLU A CA    1 
ATOM   432  C C     . GLU A 1 65  ? 76.285 27.106 5.944   1.00 42.46  ? 65  GLU A C     1 
ATOM   433  O O     . GLU A 1 65  ? 77.506 26.974 6.066   1.00 40.70  ? 65  GLU A O     1 
ATOM   434  C CB    . GLU A 1 65  ? 75.339 28.479 4.065   1.00 38.72  ? 65  GLU A CB    1 
ATOM   435  C CG    . GLU A 1 65  ? 76.529 29.414 4.110   1.00 43.82  ? 65  GLU A CG    1 
ATOM   436  C CD    . GLU A 1 65  ? 76.185 30.836 3.666   1.00 59.00  ? 65  GLU A CD    1 
ATOM   437  O OE1   . GLU A 1 65  ? 75.021 31.099 3.281   1.00 53.92  ? 65  GLU A OE1   1 
ATOM   438  O OE2   . GLU A 1 65  ? 77.088 31.697 3.710   1.00 66.61  ? 65  GLU A OE2   1 
ATOM   439  N N     . ARG A 1 66  ? 75.494 27.305 6.998   1.00 39.07  ? 66  ARG A N     1 
ATOM   440  C CA    A ARG A 1 66  ? 76.026 27.408 8.355   0.47 39.89  ? 66  ARG A CA    1 
ATOM   441  C CA    B ARG A 1 66  ? 76.026 27.411 8.354   0.53 39.48  ? 66  ARG A CA    1 
ATOM   442  C C     . ARG A 1 66  ? 75.881 26.122 9.153   1.00 40.50  ? 66  ARG A C     1 
ATOM   443  O O     . ARG A 1 66  ? 76.197 26.107 10.345  1.00 42.18  ? 66  ARG A O     1 
ATOM   444  C CB    A ARG A 1 66  ? 75.350 28.555 9.112   0.47 44.29  ? 66  ARG A CB    1 
ATOM   445  C CB    B ARG A 1 66  ? 75.346 28.561 9.104   0.53 44.22  ? 66  ARG A CB    1 
ATOM   446  C CG    A ARG A 1 66  ? 75.377 29.891 8.384   0.47 45.04  ? 66  ARG A CG    1 
ATOM   447  C CG    B ARG A 1 66  ? 75.138 29.831 8.274   0.53 44.96  ? 66  ARG A CG    1 
ATOM   448  C CD    A ARG A 1 66  ? 76.742 30.168 7.787   0.47 46.70  ? 66  ARG A CD    1 
ATOM   449  C CD    B ARG A 1 66  ? 76.345 30.753 8.287   0.53 48.18  ? 66  ARG A CD    1 
ATOM   450  N NE    A ARG A 1 66  ? 77.773 30.399 8.792   0.47 47.66  ? 66  ARG A NE    1 
ATOM   451  N NE    B ARG A 1 66  ? 76.092 31.980 7.536   0.53 49.67  ? 66  ARG A NE    1 
ATOM   452  C CZ    A ARG A 1 66  ? 78.284 31.589 9.078   0.47 48.86  ? 66  ARG A CZ    1 
ATOM   453  C CZ    B ARG A 1 66  ? 76.995 32.927 7.327   0.53 52.98  ? 66  ARG A CZ    1 
ATOM   454  N NH1   A ARG A 1 66  ? 77.842 32.691 8.493   0.47 50.52  ? 66  ARG A NH1   1 
ATOM   455  N NH1   B ARG A 1 66  ? 78.223 32.830 7.812   0.53 52.99  ? 66  ARG A NH1   1 
ATOM   456  N NH2   A ARG A 1 66  ? 79.271 31.675 9.965   0.47 50.45  ? 66  ARG A NH2   1 
ATOM   457  N NH2   B ARG A 1 66  ? 76.659 33.998 6.614   0.53 49.23  ? 66  ARG A NH2   1 
ATOM   458  N N     . VAL A 1 67  ? 75.411 25.056 8.538   1.00 42.35  ? 67  VAL A N     1 
ATOM   459  C CA    . VAL A 1 67  ? 75.269 23.770 9.212   1.00 41.00  ? 67  VAL A CA    1 
ATOM   460  C C     . VAL A 1 67  ? 76.638 23.089 9.290   1.00 46.34  ? 67  VAL A C     1 
ATOM   461  O O     . VAL A 1 67  ? 77.482 23.256 8.401   1.00 46.17  ? 67  VAL A O     1 
ATOM   462  C CB    . VAL A 1 67  ? 74.220 22.931 8.446   1.00 39.37  ? 67  VAL A CB    1 
ATOM   463  C CG1   . VAL A 1 67  ? 74.190 21.510 8.910   1.00 47.49  ? 67  VAL A CG1   1 
ATOM   464  C CG2   . VAL A 1 67  ? 72.821 23.566 8.583   1.00 35.65  ? 67  VAL A CG2   1 
ATOM   465  N N     . ASP A 1 68  ? 76.882 22.346 10.373  1.00 40.19  ? 68  ASP A N     1 
ATOM   466  C CA    . ASP A 1 68  ? 78.125 21.576 10.545  1.00 42.62  ? 68  ASP A CA    1 
ATOM   467  C C     . ASP A 1 68  ? 78.342 20.626 9.367   1.00 44.83  ? 68  ASP A C     1 
ATOM   468  O O     . ASP A 1 68  ? 77.478 19.777 9.104   1.00 40.83  ? 68  ASP A O     1 
ATOM   469  C CB    . ASP A 1 68  ? 78.065 20.782 11.857  1.00 50.07  ? 68  ASP A CB    1 
ATOM   470  C CG    . ASP A 1 68  ? 79.404 20.131 12.243  1.00 51.85  ? 68  ASP A CG    1 
ATOM   471  O OD1   . ASP A 1 68  ? 80.299 19.960 11.389  1.00 55.36  ? 68  ASP A OD1   1 
ATOM   472  O OD2   . ASP A 1 68  ? 79.545 19.771 13.427  1.00 60.59  ? 68  ASP A OD2   1 
ATOM   473  N N     . PRO A 1 69  ? 79.470 20.722 8.648   1.00 43.22  ? 69  PRO A N     1 
ATOM   474  C CA    . PRO A 1 69  ? 79.667 19.866 7.458   1.00 40.03  ? 69  PRO A CA    1 
ATOM   475  C C     . PRO A 1 69  ? 79.765 18.385 7.776   1.00 46.62  ? 69  PRO A C     1 
ATOM   476  O O     . PRO A 1 69  ? 79.547 17.555 6.881   1.00 41.76  ? 69  PRO A O     1 
ATOM   477  C CB    . PRO A 1 69  ? 80.984 20.380 6.856   1.00 44.57  ? 69  PRO A CB    1 
ATOM   478  C CG    . PRO A 1 69  ? 81.197 21.739 7.466   1.00 55.11  ? 69  PRO A CG    1 
ATOM   479  C CD    . PRO A 1 69  ? 80.570 21.681 8.836   1.00 46.24  ? 69  PRO A CD    1 
ATOM   480  N N     . ARG A 1 70  ? 80.097 18.027 9.014   1.00 40.29  ? 70  ARG A N     1 
ATOM   481  C CA    . ARG A 1 70  ? 80.085 16.631 9.421   1.00 40.17  ? 70  ARG A CA    1 
ATOM   482  C C     . ARG A 1 70  ? 78.679 16.051 9.475   1.00 38.07  ? 70  ARG A C     1 
ATOM   483  O O     . ARG A 1 70  ? 78.533 14.829 9.527   1.00 45.57  ? 70  ARG A O     1 
ATOM   484  C CB    . ARG A 1 70  ? 80.748 16.484 10.792  1.00 39.46  ? 70  ARG A CB    1 
ATOM   485  C CG    . ARG A 1 70  ? 82.218 16.898 10.809  1.00 54.48  ? 70  ARG A CG    1 
ATOM   486  C CD    . ARG A 1 70  ? 82.764 16.929 12.225  1.00 54.67  ? 70  ARG A CD    1 
ATOM   487  N NE    . ARG A 1 70  ? 81.963 17.811 13.068  1.00 64.42  ? 70  ARG A NE    1 
ATOM   488  C CZ    . ARG A 1 70  ? 82.142 17.983 14.371  1.00 77.05  ? 70  ARG A CZ    1 
ATOM   489  N NH1   . ARG A 1 70  ? 83.079 17.320 15.036  1.00 68.05  ? 70  ARG A NH1   1 
ATOM   490  N NH2   . ARG A 1 70  ? 81.362 18.841 15.025  1.00 64.04  ? 70  ARG A NH2   1 
ATOM   491  N N     . GLY A 1 71  ? 77.649 16.890 9.484   1.00 36.50  ? 71  GLY A N     1 
ATOM   492  C CA    . GLY A 1 71  ? 76.293 16.431 9.683   1.00 45.46  ? 71  GLY A CA    1 
ATOM   493  C C     . GLY A 1 71  ? 75.407 16.360 8.456   1.00 42.99  ? 71  GLY A C     1 
ATOM   494  O O     . GLY A 1 71  ? 74.211 16.086 8.605   1.00 40.87  ? 71  GLY A O     1 
ATOM   495  N N     . TYR A 1 72  ? 75.939 16.587 7.253   1.00 36.61  ? 72  TYR A N     1 
ATOM   496  C CA    . TYR A 1 72  ? 75.101 16.535 6.060   1.00 35.29  ? 72  TYR A CA    1 
ATOM   497  C C     . TYR A 1 72  ? 75.924 16.126 4.847   1.00 38.87  ? 72  TYR A C     1 
ATOM   498  O O     . TYR A 1 72  ? 77.142 16.314 4.809   1.00 34.44  ? 72  TYR A O     1 
ATOM   499  C CB    . TYR A 1 72  ? 74.417 17.881 5.789   1.00 37.15  ? 72  TYR A CB    1 
ATOM   500  C CG    . TYR A 1 72  ? 75.339 18.987 5.281   1.00 39.53  ? 72  TYR A CG    1 
ATOM   501  C CD1   . TYR A 1 72  ? 75.564 19.168 3.919   1.00 39.06  ? 72  TYR A CD1   1 
ATOM   502  C CD2   . TYR A 1 72  ? 75.951 19.869 6.163   1.00 41.33  ? 72  TYR A CD2   1 
ATOM   503  C CE1   . TYR A 1 72  ? 76.397 20.180 3.451   1.00 41.95  ? 72  TYR A CE1   1 
ATOM   504  C CE2   . TYR A 1 72  ? 76.781 20.885 5.704   1.00 39.74  ? 72  TYR A CE2   1 
ATOM   505  C CZ    . TYR A 1 72  ? 76.996 21.035 4.349   1.00 40.59  ? 72  TYR A CZ    1 
ATOM   506  O OH    . TYR A 1 72  ? 77.812 22.039 3.897   1.00 43.18  ? 72  TYR A OH    1 
ATOM   507  N N     . VAL A 1 73  ? 75.227 15.588 3.840   1.00 34.61  ? 73  VAL A N     1 
ATOM   508  C CA    . VAL A 1 73  ? 75.777 15.343 2.513   1.00 30.75  ? 73  VAL A CA    1 
ATOM   509  C C     . VAL A 1 73  ? 74.763 15.824 1.483   1.00 34.39  ? 73  VAL A C     1 
ATOM   510  O O     . VAL A 1 73  ? 73.574 15.496 1.575   1.00 34.26  ? 73  VAL A O     1 
ATOM   511  C CB    . VAL A 1 73  ? 76.104 13.856 2.273   1.00 37.21  ? 73  VAL A CB    1 
ATOM   512  C CG1   . VAL A 1 73  ? 76.759 13.683 0.887   1.00 32.00  ? 73  VAL A CG1   1 
ATOM   513  C CG2   . VAL A 1 73  ? 77.041 13.311 3.385   1.00 35.12  ? 73  VAL A CG2   1 
ATOM   514  N N     . VAL A 1 74  ? 75.227 16.606 0.518   1.00 32.52  ? 74  VAL A N     1 
ATOM   515  C CA    . VAL A 1 74  ? 74.424 17.019 -0.627  1.00 32.56  ? 74  VAL A CA    1 
ATOM   516  C C     . VAL A 1 74  ? 74.755 16.078 -1.784  1.00 35.56  ? 74  VAL A C     1 
ATOM   517  O O     . VAL A 1 74  ? 75.923 15.957 -2.174  1.00 34.70  ? 74  VAL A O     1 
ATOM   518  C CB    . VAL A 1 74  ? 74.705 18.480 -1.017  1.00 34.98  ? 74  VAL A CB    1 
ATOM   519  C CG1   . VAL A 1 74  ? 73.989 18.830 -2.344  1.00 30.64  ? 74  VAL A CG1   1 
ATOM   520  C CG2   . VAL A 1 74  ? 74.309 19.440 0.112   1.00 36.46  ? 74  VAL A CG2   1 
ATOM   521  N N     . HIS A 1 75  ? 73.735 15.401 -2.326  1.00 34.35  ? 75  HIS A N     1 
ATOM   522  C CA    . HIS A 1 75  ? 73.926 14.482 -3.441  1.00 33.61  ? 75  HIS A CA    1 
ATOM   523  C C     . HIS A 1 75  ? 73.433 15.140 -4.719  1.00 36.78  ? 75  HIS A C     1 
ATOM   524  O O     . HIS A 1 75  ? 72.217 15.321 -4.881  1.00 35.28  ? 75  HIS A O     1 
ATOM   525  C CB    . HIS A 1 75  ? 73.182 13.164 -3.208  1.00 31.10  ? 75  HIS A CB    1 
ATOM   526  C CG    . HIS A 1 75  ? 73.606 12.430 -1.976  1.00 35.16  ? 75  HIS A CG    1 
ATOM   527  N ND1   . HIS A 1 75  ? 74.753 11.663 -1.921  1.00 36.51  ? 75  HIS A ND1   1 
ATOM   528  C CD2   . HIS A 1 75  ? 73.034 12.342 -0.752  1.00 34.32  ? 75  HIS A CD2   1 
ATOM   529  C CE1   . HIS A 1 75  ? 74.863 11.129 -0.715  1.00 35.61  ? 75  HIS A CE1   1 
ATOM   530  N NE2   . HIS A 1 75  ? 73.835 11.528 0.014   1.00 35.53  ? 75  HIS A NE2   1 
ATOM   531  N N     . PRO A 1 76  ? 74.306 15.516 -5.637  1.00 37.18  ? 76  PRO A N     1 
ATOM   532  C CA    . PRO A 1 76  ? 73.848 16.000 -6.945  1.00 37.43  ? 76  PRO A CA    1 
ATOM   533  C C     . PRO A 1 76  ? 73.557 14.818 -7.862  1.00 39.14  ? 76  PRO A C     1 
ATOM   534  O O     . PRO A 1 76  ? 74.469 14.134 -8.324  1.00 44.08  ? 76  PRO A O     1 
ATOM   535  C CB    . PRO A 1 76  ? 75.035 16.839 -7.440  1.00 36.72  ? 76  PRO A CB    1 
ATOM   536  C CG    . PRO A 1 76  ? 76.233 16.234 -6.777  1.00 42.57  ? 76  PRO A CG    1 
ATOM   537  C CD    . PRO A 1 76  ? 75.766 15.631 -5.464  1.00 34.05  ? 76  PRO A CD    1 
ATOM   538  N N     . ILE A 1 77  ? 72.287 14.573 -8.107  1.00 35.71  ? 77  ILE A N     1 
ATOM   539  C CA    . ILE A 1 77  ? 71.863 13.348 -8.770  1.00 38.11  ? 77  ILE A CA    1 
ATOM   540  C C     . ILE A 1 77  ? 71.800 13.579 -10.274 1.00 42.03  ? 77  ILE A C     1 
ATOM   541  O O     . ILE A 1 77  ? 71.210 14.559 -10.738 1.00 36.15  ? 77  ILE A O     1 
ATOM   542  C CB    . ILE A 1 77  ? 70.510 12.876 -8.219  1.00 38.43  ? 77  ILE A CB    1 
ATOM   543  C CG1   . ILE A 1 77  ? 70.642 12.504 -6.733  1.00 36.47  ? 77  ILE A CG1   1 
ATOM   544  C CG2   . ILE A 1 77  ? 69.953 11.740 -9.061  1.00 37.49  ? 77  ILE A CG2   1 
ATOM   545  C CD1   . ILE A 1 77  ? 71.664 11.398 -6.445  1.00 34.97  ? 77  ILE A CD1   1 
ATOM   546  N N     . SER A 1 78  ? 72.415 12.679 -11.032 1.00 39.49  ? 78  SER A N     1 
ATOM   547  C CA    . SER A 1 78  ? 72.336 12.695 -12.489 1.00 48.43  ? 78  SER A CA    1 
ATOM   548  C C     . SER A 1 78  ? 71.804 11.349 -12.982 1.00 47.49  ? 78  SER A C     1 
ATOM   549  O O     . SER A 1 78  ? 71.296 10.536 -12.200 1.00 40.68  ? 78  SER A O     1 
ATOM   550  C CB    . SER A 1 78  ? 73.707 13.033 -13.088 1.00 41.91  ? 78  SER A CB    1 
ATOM   551  O OG    . SER A 1 78  ? 74.738 12.286 -12.461 1.00 55.04  ? 78  SER A OG    1 
ATOM   552  N N     . ALA A 1 79  ? 71.935 11.119 -14.287 1.00 40.82  ? 79  ALA A N     1 
ATOM   553  C CA    . ALA A 1 79  ? 71.429 9.903  -14.895 1.00 47.04  ? 79  ALA A CA    1 
ATOM   554  C C     . ALA A 1 79  ? 72.072 8.667  -14.266 1.00 36.45  ? 79  ALA A C     1 
ATOM   555  O O     . ALA A 1 79  ? 73.255 8.682  -13.916 1.00 40.46  ? 79  ALA A O     1 
ATOM   556  C CB    . ALA A 1 79  ? 71.711 9.903  -16.399 1.00 42.70  ? 79  ALA A CB    1 
ATOM   557  N N     . PRO A 1 80  ? 71.319 7.578  -14.140 1.00 39.84  ? 80  PRO A N     1 
ATOM   558  C CA    . PRO A 1 80  ? 71.911 6.319  -13.668 1.00 42.83  ? 80  PRO A CA    1 
ATOM   559  C C     . PRO A 1 80  ? 73.066 5.876  -14.560 1.00 46.44  ? 80  PRO A C     1 
ATOM   560  O O     . PRO A 1 80  ? 72.990 5.952  -15.788 1.00 43.79  ? 80  PRO A O     1 
ATOM   561  C CB    . PRO A 1 80  ? 70.744 5.327  -13.740 1.00 42.95  ? 80  PRO A CB    1 
ATOM   562  C CG    . PRO A 1 80  ? 69.501 6.173  -13.829 1.00 48.29  ? 80  PRO A CG    1 
ATOM   563  C CD    . PRO A 1 80  ? 69.905 7.430  -14.523 1.00 41.21  ? 80  PRO A CD    1 
ATOM   564  N N     . GLN A 1 81  ? 74.149 5.434  -13.925 1.00 41.67  ? 81  GLN A N     1 
ATOM   565  C CA    . GLN A 1 81  ? 75.279 4.825  -14.611 1.00 40.97  ? 81  GLN A CA    1 
ATOM   566  C C     . GLN A 1 81  ? 74.964 3.370  -14.958 1.00 47.44  ? 81  GLN A C     1 
ATOM   567  O O     . GLN A 1 81  ? 74.069 2.762  -14.362 1.00 40.14  ? 81  GLN A O     1 
ATOM   568  C CB    . GLN A 1 81  ? 76.518 4.891  -13.727 1.00 42.41  ? 81  GLN A CB    1 
ATOM   569  C CG    . GLN A 1 81  ? 77.042 6.297  -13.467 1.00 51.43  ? 81  GLN A CG    1 
ATOM   570  C CD    . GLN A 1 81  ? 77.680 6.886  -14.706 1.00 70.72  ? 81  GLN A CD    1 
ATOM   571  O OE1   . GLN A 1 81  ? 77.142 7.814  -15.310 1.00 81.57  ? 81  GLN A OE1   1 
ATOM   572  N NE2   . GLN A 1 81  ? 78.826 6.331  -15.110 1.00 70.25  ? 81  GLN A NE2   1 
ATOM   573  N N     . PRO A 1 82  ? 75.692 2.781  -15.921 1.00 47.68  ? 82  PRO A N     1 
ATOM   574  C CA    . PRO A 1 82  ? 75.428 1.370  -16.259 1.00 47.05  ? 82  PRO A CA    1 
ATOM   575  C C     . PRO A 1 82  ? 75.498 0.427  -15.062 1.00 45.24  ? 82  PRO A C     1 
ATOM   576  O O     . PRO A 1 82  ? 74.668 -0.484 -14.970 1.00 45.10  ? 82  PRO A O     1 
ATOM   577  C CB    . PRO A 1 82  ? 76.499 1.059  -17.318 1.00 50.97  ? 82  PRO A CB    1 
ATOM   578  C CG    . PRO A 1 82  ? 76.757 2.392  -17.970 1.00 46.82  ? 82  PRO A CG    1 
ATOM   579  C CD    . PRO A 1 82  ? 76.668 3.395  -16.842 1.00 47.96  ? 82  PRO A CD    1 
ATOM   580  N N     . HIS A 1 83  ? 76.429 0.627  -14.124 1.00 45.95  ? 83  HIS A N     1 
ATOM   581  C CA    A HIS A 1 83  ? 76.474 -0.243 -12.955 0.55 41.24  ? 83  HIS A CA    1 
ATOM   582  C CA    B HIS A 1 83  ? 76.471 -0.249 -12.954 0.45 42.10  ? 83  HIS A CA    1 
ATOM   583  C C     . HIS A 1 83  ? 75.240 -0.068 -12.074 1.00 41.39  ? 83  HIS A C     1 
ATOM   584  O O     . HIS A 1 83  ? 74.777 -1.035 -11.460 1.00 43.07  ? 83  HIS A O     1 
ATOM   585  C CB    A HIS A 1 83  ? 77.762 0.007  -12.162 0.55 43.95  ? 83  HIS A CB    1 
ATOM   586  C CB    B HIS A 1 83  ? 77.750 -0.010 -12.140 0.45 44.92  ? 83  HIS A CB    1 
ATOM   587  C CG    A HIS A 1 83  ? 77.828 1.343  -11.483 0.55 43.35  ? 83  HIS A CG    1 
ATOM   588  C CG    B HIS A 1 83  ? 77.910 -0.927 -10.958 0.45 45.32  ? 83  HIS A CG    1 
ATOM   589  N ND1   A HIS A 1 83  ? 78.268 2.485  -12.119 0.55 47.98  ? 83  HIS A ND1   1 
ATOM   590  N ND1   B HIS A 1 83  ? 78.358 -2.227 -11.072 0.45 47.78  ? 83  HIS A ND1   1 
ATOM   591  C CD2   A HIS A 1 83  ? 77.543 1.710  -10.211 0.55 41.27  ? 83  HIS A CD2   1 
ATOM   592  C CD2   B HIS A 1 83  ? 77.693 -0.723 -9.636  0.45 44.56  ? 83  HIS A CD2   1 
ATOM   593  C CE1   A HIS A 1 83  ? 78.235 3.500  -11.273 0.55 34.07  ? 83  HIS A CE1   1 
ATOM   594  C CE1   B HIS A 1 83  ? 78.404 -2.784 -9.875  0.45 44.58  ? 83  HIS A CE1   1 
ATOM   595  N NE2   A HIS A 1 83  ? 77.798 3.058  -10.109 0.55 40.90  ? 83  HIS A NE2   1 
ATOM   596  N NE2   B HIS A 1 83  ? 78.005 -1.893 -8.985  0.45 42.94  ? 83  HIS A NE2   1 
ATOM   597  N N     . GLU A 1 84  ? 74.685 1.147  -12.005 1.00 38.52  ? 84  GLU A N     1 
ATOM   598  C CA    . GLU A 1 84  ? 73.494 1.366  -11.188 1.00 35.13  ? 84  GLU A CA    1 
ATOM   599  C C     . GLU A 1 84  ? 72.248 0.752  -11.822 1.00 37.93  ? 84  GLU A C     1 
ATOM   600  O O     . GLU A 1 84  ? 71.315 0.371  -11.103 1.00 39.59  ? 84  GLU A O     1 
ATOM   601  C CB    . GLU A 1 84  ? 73.288 2.868  -10.932 1.00 35.78  ? 84  GLU A CB    1 
ATOM   602  C CG    . GLU A 1 84  ? 74.428 3.518  -10.128 1.00 40.28  ? 84  GLU A CG    1 
ATOM   603  C CD    . GLU A 1 84  ? 74.346 5.042  -10.060 1.00 42.46  ? 84  GLU A CD    1 
ATOM   604  O OE1   . GLU A 1 84  ? 74.014 5.690  -11.080 1.00 40.51  ? 84  GLU A OE1   1 
ATOM   605  O OE2   . GLU A 1 84  ? 74.626 5.595  -8.974  1.00 40.97  ? 84  GLU A OE2   1 
ATOM   606  N N     . LEU A 1 85  ? 72.214 0.629  -13.154 1.00 35.02  ? 85  LEU A N     1 
ATOM   607  C CA    . LEU A 1 85  ? 71.068 0.007  -13.816 1.00 36.47  ? 85  LEU A CA    1 
ATOM   608  C C     . LEU A 1 85  ? 71.007 -1.507 -13.612 1.00 38.99  ? 85  LEU A C     1 
ATOM   609  O O     . LEU A 1 85  ? 70.000 -2.124 -13.974 1.00 38.00  ? 85  LEU A O     1 
ATOM   610  C CB    . LEU A 1 85  ? 71.085 0.339  -15.312 1.00 39.99  ? 85  LEU A CB    1 
ATOM   611  C CG    . LEU A 1 85  ? 70.883 1.830  -15.604 1.00 41.87  ? 85  LEU A CG    1 
ATOM   612  C CD1   . LEU A 1 85  ? 71.254 2.177  -17.059 1.00 46.40  ? 85  LEU A CD1   1 
ATOM   613  C CD2   . LEU A 1 85  ? 69.444 2.252  -15.288 1.00 39.91  ? 85  LEU A CD2   1 
ATOM   614  N N     . ARG A 1 86  ? 72.038 -2.120 -13.036 1.00 39.65  ? 86  ARG A N     1 
ATOM   615  C CA    . ARG A 1 86  ? 71.968 -3.542 -12.706 1.00 36.25  ? 86  ARG A CA    1 
ATOM   616  C C     . ARG A 1 86  ? 71.127 -3.811 -11.456 1.00 34.78  ? 86  ARG A C     1 
ATOM   617  O O     . ARG A 1 86  ? 71.002 -4.968 -11.053 1.00 38.31  ? 86  ARG A O     1 
ATOM   618  C CB    . ARG A 1 86  ? 73.388 -4.109 -12.540 1.00 35.07  ? 86  ARG A CB    1 
ATOM   619  C CG    . ARG A 1 86  ? 74.241 -4.007 -13.836 1.00 47.69  ? 86  ARG A CG    1 
ATOM   620  C CD    . ARG A 1 86  ? 75.680 -4.567 -13.716 1.00 55.32  ? 86  ARG A CD    1 
ATOM   621  N NE    . ARG A 1 86  ? 76.487 -4.236 -14.894 1.00 70.80  ? 86  ARG A NE    1 
ATOM   622  C CZ    . ARG A 1 86  ? 77.665 -3.617 -14.869 1.00 80.31  ? 86  ARG A CZ    1 
ATOM   623  N NH1   . ARG A 1 86  ? 78.273 -3.326 -13.728 1.00 72.43  ? 86  ARG A NH1   1 
ATOM   624  N NH2   . ARG A 1 86  ? 78.254 -3.288 -16.019 1.00 78.69  ? 86  ARG A NH2   1 
ATOM   625  N N     . TYR A 1 87  ? 70.543 -2.774 -10.852 1.00 35.73  ? 87  TYR A N     1 
ATOM   626  C CA    . TYR A 1 87  ? 69.697 -2.893 -9.670  1.00 36.43  ? 87  TYR A CA    1 
ATOM   627  C C     . TYR A 1 87  ? 68.370 -2.180 -9.910  1.00 40.12  ? 87  TYR A C     1 
ATOM   628  O O     . TYR A 1 87  ? 68.196 -1.448 -10.892 1.00 39.15  ? 87  TYR A O     1 
ATOM   629  C CB    . TYR A 1 87  ? 70.383 -2.300 -8.433  1.00 35.70  ? 87  TYR A CB    1 
ATOM   630  C CG    . TYR A 1 87  ? 71.705 -2.943 -8.068  1.00 37.78  ? 87  TYR A CG    1 
ATOM   631  C CD1   . TYR A 1 87  ? 72.906 -2.472 -8.597  1.00 37.18  ? 87  TYR A CD1   1 
ATOM   632  C CD2   . TYR A 1 87  ? 71.752 -4.011 -7.183  1.00 33.98  ? 87  TYR A CD2   1 
ATOM   633  C CE1   . TYR A 1 87  ? 74.125 -3.061 -8.259  1.00 39.24  ? 87  TYR A CE1   1 
ATOM   634  C CE2   . TYR A 1 87  ? 72.960 -4.599 -6.832  1.00 36.89  ? 87  TYR A CE2   1 
ATOM   635  C CZ    . TYR A 1 87  ? 74.140 -4.124 -7.367  1.00 38.57  ? 87  TYR A CZ    1 
ATOM   636  O OH    . TYR A 1 87  ? 75.330 -4.732 -7.014  1.00 41.93  ? 87  TYR A OH    1 
ATOM   637  N N     . ASN A 1 88  ? 67.429 -2.394 -8.991  1.00 33.37  ? 88  ASN A N     1 
ATOM   638  C CA    . ASN A 1 88  ? 66.194 -1.618 -8.986  1.00 33.94  ? 88  ASN A CA    1 
ATOM   639  C C     . ASN A 1 88  ? 66.498 -0.121 -8.929  1.00 36.71  ? 88  ASN A C     1 
ATOM   640  O O     . ASN A 1 88  ? 67.489 0.313  -8.336  1.00 34.17  ? 88  ASN A O     1 
ATOM   641  C CB    . ASN A 1 88  ? 65.321 -2.026 -7.797  1.00 32.98  ? 88  ASN A CB    1 
ATOM   642  C CG    . ASN A 1 88  ? 64.036 -1.252 -7.739  1.00 40.22  ? 88  ASN A CG    1 
ATOM   643  O OD1   . ASN A 1 88  ? 63.950 -0.214 -7.066  1.00 36.63  ? 88  ASN A OD1   1 
ATOM   644  N ND2   . ASN A 1 88  ? 63.020 -1.740 -8.454  1.00 34.00  ? 88  ASN A ND2   1 
ATOM   645  N N     . TYR A 1 89  ? 65.632 0.677  -9.563  1.00 36.27  ? 89  TYR A N     1 
ATOM   646  C CA    . TYR A 1 89  ? 65.896 2.111  -9.684  1.00 34.44  ? 89  TYR A CA    1 
ATOM   647  C C     . TYR A 1 89  ? 66.034 2.812  -8.339  1.00 33.55  ? 89  TYR A C     1 
ATOM   648  O O     . TYR A 1 89  ? 66.631 3.890  -8.282  1.00 33.83  ? 89  TYR A O     1 
ATOM   649  C CB    . TYR A 1 89  ? 64.791 2.802  -10.486 1.00 34.75  ? 89  TYR A CB    1 
ATOM   650  C CG    . TYR A 1 89  ? 63.460 2.990  -9.761  1.00 37.85  ? 89  TYR A CG    1 
ATOM   651  C CD1   . TYR A 1 89  ? 62.543 1.938  -9.641  1.00 39.08  ? 89  TYR A CD1   1 
ATOM   652  C CD2   . TYR A 1 89  ? 63.099 4.234  -9.251  1.00 38.99  ? 89  TYR A CD2   1 
ATOM   653  C CE1   . TYR A 1 89  ? 61.312 2.118  -9.007  1.00 39.72  ? 89  TYR A CE1   1 
ATOM   654  C CE2   . TYR A 1 89  ? 61.873 4.430  -8.621  1.00 40.28  ? 89  TYR A CE2   1 
ATOM   655  C CZ    . TYR A 1 89  ? 60.986 3.370  -8.498  1.00 44.13  ? 89  TYR A CZ    1 
ATOM   656  O OH    . TYR A 1 89  ? 59.776 3.574  -7.866  1.00 40.45  ? 89  TYR A OH    1 
ATOM   657  N N     . LEU A 1 90  ? 65.487 2.253  -7.266  1.00 34.38  ? 90  LEU A N     1 
ATOM   658  C CA    . LEU A 1 90  ? 65.645 2.886  -5.960  1.00 35.19  ? 90  LEU A CA    1 
ATOM   659  C C     . LEU A 1 90  ? 66.966 2.540  -5.273  1.00 34.45  ? 90  LEU A C     1 
ATOM   660  O O     . LEU A 1 90  ? 67.328 3.206  -4.294  1.00 37.00  ? 90  LEU A O     1 
ATOM   661  C CB    . LEU A 1 90  ? 64.482 2.497  -5.045  1.00 30.39  ? 90  LEU A CB    1 
ATOM   662  C CG    . LEU A 1 90  ? 63.094 3.047  -5.384  1.00 36.83  ? 90  LEU A CG    1 
ATOM   663  C CD1   . LEU A 1 90  ? 62.085 2.441  -4.416  1.00 33.59  ? 90  LEU A CD1   1 
ATOM   664  C CD2   . LEU A 1 90  ? 63.065 4.578  -5.319  1.00 32.12  ? 90  LEU A CD2   1 
ATOM   665  N N     . GLN A 1 91  ? 67.691 1.531  -5.762  1.00 36.84  ? 91  GLN A N     1 
ATOM   666  C CA    . GLN A 1 91  ? 68.896 1.050  -5.082  1.00 36.92  ? 91  GLN A CA    1 
ATOM   667  C C     . GLN A 1 91  ? 69.941 2.152  -4.919  1.00 39.53  ? 91  GLN A C     1 
ATOM   668  O O     . GLN A 1 91  ? 70.539 2.305  -3.843  1.00 33.63  ? 91  GLN A O     1 
ATOM   669  C CB    . GLN A 1 91  ? 69.497 -0.113 -5.860  1.00 35.19  ? 91  GLN A CB    1 
ATOM   670  C CG    . GLN A 1 91  ? 70.685 -0.778 -5.169  1.00 34.03  ? 91  GLN A CG    1 
ATOM   671  C CD    . GLN A 1 91  ? 70.230 -1.852 -4.192  1.00 41.55  ? 91  GLN A CD    1 
ATOM   672  O OE1   . GLN A 1 91  ? 69.294 -2.607 -4.476  1.00 36.49  ? 91  GLN A OE1   1 
ATOM   673  N NE2   . GLN A 1 91  ? 70.882 -1.922 -3.036  1.00 35.08  ? 91  GLN A NE2   1 
ATOM   674  N N     . ARG A 1 92  ? 70.213 2.898  -5.995  1.00 32.31  ? 92  ARG A N     1 
ATOM   675  C CA    . ARG A 1 92  ? 71.209 3.963  -5.920  1.00 36.28  ? 92  ARG A CA    1 
ATOM   676  C C     . ARG A 1 92  ? 70.826 5.018  -4.893  1.00 33.86  ? 92  ARG A C     1 
ATOM   677  O O     . ARG A 1 92  ? 71.695 5.746  -4.412  1.00 34.85  ? 92  ARG A O     1 
ATOM   678  C CB    . ARG A 1 92  ? 71.402 4.625  -7.292  1.00 36.74  ? 92  ARG A CB    1 
ATOM   679  C CG    . ARG A 1 92  ? 70.179 5.420  -7.741  1.00 35.51  ? 92  ARG A CG    1 
ATOM   680  C CD    . ARG A 1 92  ? 70.145 5.655  -9.258  1.00 39.51  ? 92  ARG A CD    1 
ATOM   681  N NE    . ARG A 1 92  ? 71.014 6.747  -9.632  1.00 54.92  ? 92  ARG A NE    1 
ATOM   682  C CZ    . ARG A 1 92  ? 70.630 7.888  -10.185 1.00 46.15  ? 92  ARG A CZ    1 
ATOM   683  N NH1   . ARG A 1 92  ? 69.384 8.089  -10.586 1.00 39.60  ? 92  ARG A NH1   1 
ATOM   684  N NH2   . ARG A 1 92  ? 71.530 8.849  -10.351 1.00 39.49  ? 92  ARG A NH2   1 
ATOM   685  N N     . PHE A 1 93  ? 69.546 5.110  -4.544  1.00 31.67  ? 93  PHE A N     1 
ATOM   686  C CA    . PHE A 1 93  ? 69.114 6.056  -3.527  1.00 33.35  ? 93  PHE A CA    1 
ATOM   687  C C     . PHE A 1 93  ? 69.142 5.440  -2.127  1.00 33.37  ? 93  PHE A C     1 
ATOM   688  O O     . PHE A 1 93  ? 69.594 6.096  -1.178  1.00 32.18  ? 93  PHE A O     1 
ATOM   689  C CB    . PHE A 1 93  ? 67.729 6.593  -3.904  1.00 28.00  ? 93  PHE A CB    1 
ATOM   690  C CG    . PHE A 1 93  ? 67.737 7.356  -5.208  1.00 35.45  ? 93  PHE A CG    1 
ATOM   691  C CD1   . PHE A 1 93  ? 68.360 8.600  -5.286  1.00 32.18  ? 93  PHE A CD1   1 
ATOM   692  C CD2   . PHE A 1 93  ? 67.184 6.811  -6.359  1.00 29.32  ? 93  PHE A CD2   1 
ATOM   693  C CE1   . PHE A 1 93  ? 68.410 9.301  -6.495  1.00 36.12  ? 93  PHE A CE1   1 
ATOM   694  C CE2   . PHE A 1 93  ? 67.228 7.509  -7.584  1.00 35.59  ? 93  PHE A CE2   1 
ATOM   695  C CZ    . PHE A 1 93  ? 67.834 8.751  -7.648  1.00 35.48  ? 93  PHE A CZ    1 
ATOM   696  N N     . TRP A 1 94  ? 68.699 4.183  -1.991  1.00 31.53  ? 94  TRP A N     1 
ATOM   697  C CA    . TRP A 1 94  ? 68.901 3.437  -0.744  1.00 38.35  ? 94  TRP A CA    1 
ATOM   698  C C     . TRP A 1 94  ? 70.340 3.558  -0.255  1.00 35.48  ? 94  TRP A C     1 
ATOM   699  O O     . TRP A 1 94  ? 70.589 3.835  0.923   1.00 37.66  ? 94  TRP A O     1 
ATOM   700  C CB    . TRP A 1 94  ? 68.550 1.959  -0.943  1.00 31.93  ? 94  TRP A CB    1 
ATOM   701  C CG    . TRP A 1 94  ? 67.078 1.703  -1.156  1.00 35.91  ? 94  TRP A CG    1 
ATOM   702  C CD1   . TRP A 1 94  ? 66.043 2.500  -0.755  1.00 38.54  ? 94  TRP A CD1   1 
ATOM   703  C CD2   . TRP A 1 94  ? 66.479 0.570  -1.815  1.00 38.02  ? 94  TRP A CD2   1 
ATOM   704  N NE1   . TRP A 1 94  ? 64.842 1.938  -1.119  1.00 37.56  ? 94  TRP A NE1   1 
ATOM   705  C CE2   . TRP A 1 94  ? 65.079 0.759  -1.780  1.00 41.59  ? 94  TRP A CE2   1 
ATOM   706  C CE3   . TRP A 1 94  ? 66.990 -0.580 -2.437  1.00 45.52  ? 94  TRP A CE3   1 
ATOM   707  C CZ2   . TRP A 1 94  ? 64.180 -0.164 -2.340  1.00 35.70  ? 94  TRP A CZ2   1 
ATOM   708  C CZ3   . TRP A 1 94  ? 66.091 -1.497 -3.005  1.00 39.03  ? 94  TRP A CZ3   1 
ATOM   709  C CH2   . TRP A 1 94  ? 64.707 -1.284 -2.942  1.00 38.56  ? 94  TRP A CH2   1 
ATOM   710  N N     . ARG A 1 95  ? 71.299 3.340  -1.162  1.00 31.35  ? 95  ARG A N     1 
ATOM   711  C CA    . ARG A 1 95  ? 72.724 3.432  -0.855  1.00 38.92  ? 95  ARG A CA    1 
ATOM   712  C C     . ARG A 1 95  ? 73.144 4.800  -0.299  1.00 36.46  ? 95  ARG A C     1 
ATOM   713  O O     . ARG A 1 95  ? 74.195 4.901  0.344   1.00 31.67  ? 95  ARG A O     1 
ATOM   714  C CB    . ARG A 1 95  ? 73.510 3.103  -2.136  1.00 39.01  ? 95  ARG A CB    1 
ATOM   715  C CG    . ARG A 1 95  ? 75.018 3.108  -2.006  1.00 69.60  ? 95  ARG A CG    1 
ATOM   716  C CD    . ARG A 1 95  ? 75.718 2.604  -3.280  1.00 64.92  ? 95  ARG A CD    1 
ATOM   717  N NE    . ARG A 1 95  ? 77.022 3.243  -3.453  1.00 85.79  ? 95  ARG A NE    1 
ATOM   718  C CZ    . ARG A 1 95  ? 78.115 2.940  -2.761  1.00 87.33  ? 95  ARG A CZ    1 
ATOM   719  N NH1   . ARG A 1 95  ? 78.113 1.978  -1.848  1.00 76.31  ? 95  ARG A NH1   1 
ATOM   720  N NH2   . ARG A 1 95  ? 79.236 3.625  -2.983  1.00 80.02  ? 95  ARG A NH2   1 
ATOM   721  N N     . LYS A 1 96  ? 72.370 5.856  -0.543  1.00 33.56  ? 96  LYS A N     1 
ATOM   722  C CA    . LYS A 1 96  ? 72.757 7.213  -0.171  1.00 33.89  ? 96  LYS A CA    1 
ATOM   723  C C     . LYS A 1 96  ? 72.000 7.737  1.045   1.00 36.06  ? 96  LYS A C     1 
ATOM   724  O O     . LYS A 1 96  ? 72.094 8.931  1.347   1.00 37.64  ? 96  LYS A O     1 
ATOM   725  C CB    . LYS A 1 96  ? 72.542 8.175  -1.355  1.00 32.80  ? 96  LYS A CB    1 
ATOM   726  C CG    . LYS A 1 96  ? 73.503 7.981  -2.545  1.00 34.49  ? 96  LYS A CG    1 
ATOM   727  C CD    . LYS A 1 96  ? 73.094 8.874  -3.740  1.00 30.08  ? 96  LYS A CD    1 
ATOM   728  C CE    . LYS A 1 96  ? 74.079 8.739  -4.909  1.00 41.72  ? 96  LYS A CE    1 
ATOM   729  N NZ    . LYS A 1 96  ? 74.171 7.318  -5.359  1.00 47.22  ? 96  LYS A NZ    1 
ATOM   730  N N     . LEU A 1 97  ? 71.234 6.895  1.735   1.00 32.45  ? 97  LEU A N     1 
ATOM   731  C CA    . LEU A 1 97  ? 70.407 7.409  2.814   1.00 36.14  ? 97  LEU A CA    1 
ATOM   732  C C     . LEU A 1 97  ? 71.274 7.775  4.022   1.00 35.86  ? 97  LEU A C     1 
ATOM   733  O O     . LEU A 1 97  ? 72.265 7.103  4.300   1.00 35.23  ? 97  LEU A O     1 
ATOM   734  C CB    . LEU A 1 97  ? 69.345 6.380  3.210   1.00 30.92  ? 97  LEU A CB    1 
ATOM   735  C CG    . LEU A 1 97  ? 68.220 6.099  2.203   1.00 34.05  ? 97  LEU A CG    1 
ATOM   736  C CD1   . LEU A 1 97  ? 67.381 4.903  2.668   1.00 34.77  ? 97  LEU A CD1   1 
ATOM   737  C CD2   . LEU A 1 97  ? 67.321 7.323  2.009   1.00 32.70  ? 97  LEU A CD2   1 
ATOM   738  N N     . PRO A 1 98  ? 70.926 8.829  4.751   1.00 34.40  ? 98  PRO A N     1 
ATOM   739  C CA    . PRO A 1 98  ? 71.690 9.201  5.942   1.00 29.40  ? 98  PRO A CA    1 
ATOM   740  C C     . PRO A 1 98  ? 71.405 8.247  7.087   1.00 32.51  ? 98  PRO A C     1 
ATOM   741  O O     . PRO A 1 98  ? 70.356 7.609  7.149   1.00 36.69  ? 98  PRO A O     1 
ATOM   742  C CB    . PRO A 1 98  ? 71.156 10.597 6.272   1.00 33.51  ? 98  PRO A CB    1 
ATOM   743  C CG    . PRO A 1 98  ? 69.704 10.504 5.855   1.00 33.85  ? 98  PRO A CG    1 
ATOM   744  C CD    . PRO A 1 98  ? 69.719 9.659  4.590   1.00 34.03  ? 98  PRO A CD    1 
ATOM   745  N N     . GLN A 1 99  ? 72.369 8.162  8.000   1.00 31.77  ? 99  GLN A N     1 
ATOM   746  C CA    . GLN A 1 99  ? 72.129 7.537  9.287   1.00 37.23  ? 99  GLN A CA    1 
ATOM   747  C C     . GLN A 1 99  ? 71.104 8.341  10.079  1.00 35.82  ? 99  GLN A C     1 
ATOM   748  O O     . GLN A 1 99  ? 70.885 9.530  9.829   1.00 34.48  ? 99  GLN A O     1 
ATOM   749  C CB    . GLN A 1 99  ? 73.422 7.457  10.097  1.00 34.66  ? 99  GLN A CB    1 
ATOM   750  C CG    . GLN A 1 99  ? 74.535 6.695  9.423   1.00 46.18  ? 99  GLN A CG    1 
ATOM   751  C CD    . GLN A 1 99  ? 75.775 6.582  10.294  1.00 58.28  ? 99  GLN A CD    1 
ATOM   752  O OE1   . GLN A 1 99  ? 75.790 7.046  11.435  1.00 53.94  ? 99  GLN A OE1   1 
ATOM   753  N NE2   . GLN A 1 99  ? 76.821 5.949  9.761   1.00 57.75  ? 99  GLN A NE2   1 
ATOM   754  N N     . HIS A 1 100 ? 70.478 7.673  11.049  1.00 39.83  ? 100 HIS A N     1 
ATOM   755  C CA    . HIS A 1 100 ? 69.690 8.367  12.056  1.00 37.67  ? 100 HIS A CA    1 
ATOM   756  C C     . HIS A 1 100 ? 70.500 9.523  12.630  1.00 35.33  ? 100 HIS A C     1 
ATOM   757  O O     . HIS A 1 100 ? 71.654 9.350  13.021  1.00 37.60  ? 100 HIS A O     1 
ATOM   758  C CB    . HIS A 1 100 ? 69.287 7.395  13.171  1.00 38.33  ? 100 HIS A CB    1 
ATOM   759  C CG    . HIS A 1 100 ? 68.425 6.252  12.712  1.00 39.46  ? 100 HIS A CG    1 
ATOM   760  N ND1   . HIS A 1 100 ? 68.407 5.029  13.351  1.00 37.73  ? 100 HIS A ND1   1 
ATOM   761  C CD2   . HIS A 1 100 ? 67.554 6.147  11.678  1.00 37.27  ? 100 HIS A CD2   1 
ATOM   762  C CE1   . HIS A 1 100 ? 67.562 4.221  12.733  1.00 37.82  ? 100 HIS A CE1   1 
ATOM   763  N NE2   . HIS A 1 100 ? 67.034 4.875  11.712  1.00 40.28  ? 100 HIS A NE2   1 
ATOM   764  N N     . GLY A 1 101 ? 69.900 10.711 12.654  1.00 37.35  ? 101 GLY A N     1 
ATOM   765  C CA    . GLY A 1 101 ? 70.572 11.892 13.153  1.00 37.24  ? 101 GLY A CA    1 
ATOM   766  C C     . GLY A 1 101 ? 71.350 12.697 12.126  1.00 42.45  ? 101 GLY A C     1 
ATOM   767  O O     . GLY A 1 101 ? 71.843 13.778 12.471  1.00 39.30  ? 101 GLY A O     1 
ATOM   768  N N     . GLN A 1 102 ? 71.475 12.216 10.884  1.00 35.58  ? 102 GLN A N     1 
ATOM   769  C CA    . GLN A 1 102 ? 72.224 12.881 9.823   1.00 35.25  ? 102 GLN A CA    1 
ATOM   770  C C     . GLN A 1 102 ? 71.279 13.416 8.752   1.00 37.27  ? 102 GLN A C     1 
ATOM   771  O O     . GLN A 1 102 ? 70.115 13.020 8.657   1.00 31.92  ? 102 GLN A O     1 
ATOM   772  C CB    . GLN A 1 102 ? 73.236 11.925 9.172   1.00 33.89  ? 102 GLN A CB    1 
ATOM   773  C CG    . GLN A 1 102 ? 74.312 11.387 10.106  1.00 42.89  ? 102 GLN A CG    1 
ATOM   774  C CD    . GLN A 1 102 ? 75.346 12.442 10.448  1.00 55.05  ? 102 GLN A CD    1 
ATOM   775  O OE1   . GLN A 1 102 ? 75.958 13.031 9.555   1.00 62.70  ? 102 GLN A OE1   1 
ATOM   776  N NE2   . GLN A 1 102 ? 75.537 12.699 11.742  1.00 60.88  ? 102 GLN A NE2   1 
ATOM   777  N N     . ILE A 1 103 ? 71.814 14.300 7.907   1.00 33.29  ? 103 ILE A N     1 
ATOM   778  C CA    . ILE A 1 103 ? 71.044 14.992 6.879   1.00 33.73  ? 103 ILE A CA    1 
ATOM   779  C C     . ILE A 1 103 ? 71.537 14.565 5.504   1.00 31.30  ? 103 ILE A C     1 
ATOM   780  O O     . ILE A 1 103 ? 72.744 14.585 5.243   1.00 36.80  ? 103 ILE A O     1 
ATOM   781  C CB    . ILE A 1 103 ? 71.163 16.518 7.018   1.00 36.70  ? 103 ILE A CB    1 
ATOM   782  C CG1   . ILE A 1 103 ? 70.654 16.974 8.390   1.00 32.44  ? 103 ILE A CG1   1 
ATOM   783  C CG2   . ILE A 1 103 ? 70.426 17.195 5.875   1.00 34.49  ? 103 ILE A CG2   1 
ATOM   784  C CD1   . ILE A 1 103 ? 70.918 18.437 8.685   1.00 36.07  ? 103 ILE A CD1   1 
ATOM   785  N N     . ALA A 1 104 ? 70.607 14.220 4.619   1.00 29.55  ? 104 ALA A N     1 
ATOM   786  C CA    . ALA A 1 104 ? 70.912 13.988 3.211   1.00 33.73  ? 104 ALA A CA    1 
ATOM   787  C C     . ALA A 1 104 ? 70.064 14.915 2.360   1.00 35.87  ? 104 ALA A C     1 
ATOM   788  O O     . ALA A 1 104 ? 68.845 14.985 2.543   1.00 37.06  ? 104 ALA A O     1 
ATOM   789  C CB    . ALA A 1 104 ? 70.656 12.533 2.800   1.00 28.96  ? 104 ALA A CB    1 
ATOM   790  N N     . VAL A 1 105 ? 70.704 15.619 1.432   1.00 31.37  ? 105 VAL A N     1 
ATOM   791  C CA    . VAL A 1 105 ? 70.016 16.484 0.487   1.00 28.53  ? 105 VAL A CA    1 
ATOM   792  C C     . VAL A 1 105 ? 70.152 15.883 -0.904  1.00 35.42  ? 105 VAL A C     1 
ATOM   793  O O     . VAL A 1 105 ? 71.264 15.575 -1.353  1.00 35.34  ? 105 VAL A O     1 
ATOM   794  C CB    . VAL A 1 105 ? 70.573 17.915 0.526   1.00 39.01  ? 105 VAL A CB    1 
ATOM   795  C CG1   . VAL A 1 105 ? 69.809 18.783 -0.443  1.00 32.70  ? 105 VAL A CG1   1 
ATOM   796  C CG2   . VAL A 1 105 ? 70.483 18.476 1.953   1.00 35.70  ? 105 VAL A CG2   1 
ATOM   797  N N     . PHE A 1 106 ? 69.028 15.715 -1.582  1.00 33.68  ? 106 PHE A N     1 
ATOM   798  C CA    . PHE A 1 106 ? 69.009 15.164 -2.931  1.00 35.69  ? 106 PHE A CA    1 
ATOM   799  C C     . PHE A 1 106 ? 68.624 16.281 -3.890  1.00 36.34  ? 106 PHE A C     1 
ATOM   800  O O     . PHE A 1 106 ? 67.465 16.717 -3.924  1.00 35.43  ? 106 PHE A O     1 
ATOM   801  C CB    . PHE A 1 106 ? 68.060 13.975 -3.016  1.00 31.35  ? 106 PHE A CB    1 
ATOM   802  C CG    . PHE A 1 106 ? 68.530 12.788 -2.238  1.00 33.19  ? 106 PHE A CG    1 
ATOM   803  C CD1   . PHE A 1 106 ? 69.393 11.865 -2.817  1.00 34.51  ? 106 PHE A CD1   1 
ATOM   804  C CD2   . PHE A 1 106 ? 68.140 12.605 -0.923  1.00 32.30  ? 106 PHE A CD2   1 
ATOM   805  C CE1   . PHE A 1 106 ? 69.844 10.768 -2.109  1.00 31.75  ? 106 PHE A CE1   1 
ATOM   806  C CE2   . PHE A 1 106 ? 68.587 11.507 -0.200  1.00 32.25  ? 106 PHE A CE2   1 
ATOM   807  C CZ    . PHE A 1 106 ? 69.441 10.586 -0.794  1.00 32.09  ? 106 PHE A CZ    1 
ATOM   808  N N     . ASP A 1 107 ? 69.611 16.771 -4.630  1.00 34.01  ? 107 ASP A N     1 
ATOM   809  C CA    . ASP A 1 107 ? 69.369 17.717 -5.718  1.00 34.73  ? 107 ASP A CA    1 
ATOM   810  C C     . ASP A 1 107 ? 68.938 16.877 -6.915  1.00 34.40  ? 107 ASP A C     1 
ATOM   811  O O     . ASP A 1 107 ? 69.776 16.356 -7.660  1.00 38.54  ? 107 ASP A O     1 
ATOM   812  C CB    . ASP A 1 107 ? 70.624 18.546 -5.981  1.00 35.07  ? 107 ASP A CB    1 
ATOM   813  C CG    . ASP A 1 107 ? 70.400 19.672 -6.983  1.00 37.58  ? 107 ASP A CG    1 
ATOM   814  O OD1   . ASP A 1 107 ? 69.356 19.688 -7.658  1.00 37.17  ? 107 ASP A OD1   1 
ATOM   815  O OD2   . ASP A 1 107 ? 71.281 20.549 -7.098  1.00 42.17  ? 107 ASP A OD2   1 
ATOM   816  N N     . ARG A 1 108 ? 67.618 16.728 -7.075  1.00 33.38  ? 108 ARG A N     1 
ATOM   817  C CA    . ARG A 1 108 ? 66.971 15.692 -7.884  1.00 35.32  ? 108 ARG A CA    1 
ATOM   818  C C     . ARG A 1 108 ? 67.127 14.347 -7.180  1.00 40.82  ? 108 ARG A C     1 
ATOM   819  O O     . ARG A 1 108 ? 67.987 14.195 -6.305  1.00 37.13  ? 108 ARG A O     1 
ATOM   820  C CB    . ARG A 1 108 ? 67.507 15.661 -9.319  1.00 32.49  ? 108 ARG A CB    1 
ATOM   821  C CG    . ARG A 1 108 ? 67.385 17.015 -9.998  1.00 40.16  ? 108 ARG A CG    1 
ATOM   822  C CD    . ARG A 1 108 ? 67.945 17.023 -11.419 1.00 49.23  ? 108 ARG A CD    1 
ATOM   823  N NE    . ARG A 1 108 ? 67.011 16.476 -12.398 1.00 54.48  ? 108 ARG A NE    1 
ATOM   824  C CZ    . ARG A 1 108 ? 67.202 16.536 -13.712 1.00 72.76  ? 108 ARG A CZ    1 
ATOM   825  N NH1   . ARG A 1 108 ? 68.267 17.136 -14.225 1.00 63.65  ? 108 ARG A NH1   1 
ATOM   826  N NH2   . ARG A 1 108 ? 66.298 15.991 -14.532 1.00 47.88  ? 108 ARG A NH2   1 
ATOM   827  N N     . SER A 1 109 ? 66.281 13.381 -7.522  1.00 36.57  ? 109 SER A N     1 
ATOM   828  C CA    . SER A 1 109 ? 66.026 12.307 -6.578  1.00 33.29  ? 109 SER A CA    1 
ATOM   829  C C     . SER A 1 109 ? 65.389 11.125 -7.304  1.00 39.97  ? 109 SER A C     1 
ATOM   830  O O     . SER A 1 109 ? 65.413 11.054 -8.540  1.00 32.51  ? 109 SER A O     1 
ATOM   831  C CB    . SER A 1 109 ? 65.133 12.831 -5.443  1.00 34.20  ? 109 SER A CB    1 
ATOM   832  O OG    . SER A 1 109 ? 63.821 13.080 -5.925  1.00 34.30  ? 109 SER A OG    1 
ATOM   833  N N     . TRP A 1 110 ? 64.804 10.206 -6.529  1.00 32.86  ? 110 TRP A N     1 
ATOM   834  C CA    . TRP A 1 110 ? 64.075 9.084  -7.112  1.00 34.23  ? 110 TRP A CA    1 
ATOM   835  C C     . TRP A 1 110 ? 62.875 9.544  -7.938  1.00 41.07  ? 110 TRP A C     1 
ATOM   836  O O     . TRP A 1 110 ? 62.405 8.793  -8.802  1.00 40.15  ? 110 TRP A O     1 
ATOM   837  C CB    . TRP A 1 110 ? 63.630 8.104  -6.007  1.00 32.74  ? 110 TRP A CB    1 
ATOM   838  C CG    . TRP A 1 110 ? 63.085 8.742  -4.756  1.00 37.32  ? 110 TRP A CG    1 
ATOM   839  C CD1   . TRP A 1 110 ? 61.767 8.943  -4.444  1.00 37.17  ? 110 TRP A CD1   1 
ATOM   840  C CD2   . TRP A 1 110 ? 63.840 9.254  -3.645  1.00 38.95  ? 110 TRP A CD2   1 
ATOM   841  N NE1   . TRP A 1 110 ? 61.656 9.544  -3.208  1.00 36.12  ? 110 TRP A NE1   1 
ATOM   842  C CE2   . TRP A 1 110 ? 62.912 9.745  -2.697  1.00 37.01  ? 110 TRP A CE2   1 
ATOM   843  C CE3   . TRP A 1 110 ? 65.212 9.334  -3.354  1.00 36.69  ? 110 TRP A CE3   1 
ATOM   844  C CZ2   . TRP A 1 110 ? 63.312 10.329 -1.489  1.00 34.89  ? 110 TRP A CZ2   1 
ATOM   845  C CZ3   . TRP A 1 110 ? 65.609 9.912  -2.146  1.00 35.38  ? 110 TRP A CZ3   1 
ATOM   846  C CH2   . TRP A 1 110 ? 64.662 10.401 -1.232  1.00 33.82  ? 110 TRP A CH2   1 
ATOM   847  N N     . TYR A 1 111 ? 62.393 10.774 -7.724  1.00 38.19  ? 111 TYR A N     1 
ATOM   848  C CA    . TYR A 1 111 ? 61.278 11.287 -8.513  1.00 37.94  ? 111 TYR A CA    1 
ATOM   849  C C     . TYR A 1 111 ? 61.637 11.483 -9.981  1.00 37.61  ? 111 TYR A C     1 
ATOM   850  O O     . TYR A 1 111 ? 60.732 11.714 -10.794 1.00 40.69  ? 111 TYR A O     1 
ATOM   851  C CB    . TYR A 1 111 ? 60.752 12.596 -7.903  1.00 39.34  ? 111 TYR A CB    1 
ATOM   852  C CG    . TYR A 1 111 ? 59.955 12.349 -6.648  1.00 38.47  ? 111 TYR A CG    1 
ATOM   853  C CD1   . TYR A 1 111 ? 58.611 11.992 -6.711  1.00 42.09  ? 111 TYR A CD1   1 
ATOM   854  C CD2   . TYR A 1 111 ? 60.554 12.429 -5.399  1.00 39.07  ? 111 TYR A CD2   1 
ATOM   855  C CE1   . TYR A 1 111 ? 57.884 11.740 -5.552  1.00 39.36  ? 111 TYR A CE1   1 
ATOM   856  C CE2   . TYR A 1 111 ? 59.841 12.187 -4.245  1.00 39.07  ? 111 TYR A CE2   1 
ATOM   857  C CZ    . TYR A 1 111 ? 58.509 11.839 -4.325  1.00 40.14  ? 111 TYR A CZ    1 
ATOM   858  O OH    . TYR A 1 111 ? 57.810 11.592 -3.169  1.00 39.35  ? 111 TYR A OH    1 
ATOM   859  N N     . GLY A 1 112 ? 62.921 11.372 -10.346 1.00 36.36  ? 112 GLY A N     1 
ATOM   860  C CA    . GLY A 1 112 ? 63.268 11.297 -11.755 1.00 39.94  ? 112 GLY A CA    1 
ATOM   861  C C     . GLY A 1 112 ? 62.515 10.194 -12.471 1.00 46.84  ? 112 GLY A C     1 
ATOM   862  O O     . GLY A 1 112 ? 62.233 10.303 -13.671 1.00 43.28  ? 112 GLY A O     1 
ATOM   863  N N     . ARG A 1 113 ? 62.147 9.135  -11.739 1.00 41.66  ? 113 ARG A N     1 
ATOM   864  C CA    . ARG A 1 113 ? 61.367 8.049  -12.323 1.00 41.67  ? 113 ARG A CA    1 
ATOM   865  C C     . ARG A 1 113 ? 60.052 8.539  -12.921 1.00 42.62  ? 113 ARG A C     1 
ATOM   866  O O     . ARG A 1 113 ? 59.562 7.950  -13.891 1.00 46.83  ? 113 ARG A O     1 
ATOM   867  C CB    . ARG A 1 113 ? 61.097 6.974  -11.264 1.00 40.12  ? 113 ARG A CB    1 
ATOM   868  C CG    . ARG A 1 113 ? 60.409 5.710  -11.786 1.00 39.92  ? 113 ARG A CG    1 
ATOM   869  C CD    . ARG A 1 113 ? 61.393 4.769  -12.472 1.00 45.36  ? 113 ARG A CD    1 
ATOM   870  N NE    . ARG A 1 113 ? 60.968 3.374  -12.393 1.00 38.14  ? 113 ARG A NE    1 
ATOM   871  C CZ    . ARG A 1 113 ? 61.628 2.363  -12.943 1.00 45.04  ? 113 ARG A CZ    1 
ATOM   872  N NH1   . ARG A 1 113 ? 62.740 2.559  -13.639 1.00 39.71  ? 113 ARG A NH1   1 
ATOM   873  N NH2   . ARG A 1 113 ? 61.160 1.124  -12.796 1.00 41.09  ? 113 ARG A NH2   1 
ATOM   874  N N     . VAL A 1 114 ? 59.459 9.597  -12.366 1.00 41.67  ? 114 VAL A N     1 
ATOM   875  C CA    . VAL A 1 114 ? 58.174 10.097 -12.851 1.00 46.22  ? 114 VAL A CA    1 
ATOM   876  C C     . VAL A 1 114 ? 58.301 11.474 -13.488 1.00 43.49  ? 114 VAL A C     1 
ATOM   877  O O     . VAL A 1 114 ? 57.283 12.112 -13.776 1.00 46.62  ? 114 VAL A O     1 
ATOM   878  C CB    . VAL A 1 114 ? 57.109 10.116 -11.739 1.00 48.05  ? 114 VAL A CB    1 
ATOM   879  C CG1   . VAL A 1 114 ? 56.899 8.720  -11.171 1.00 42.51  ? 114 VAL A CG1   1 
ATOM   880  C CG2   . VAL A 1 114 ? 57.487 11.113 -10.644 1.00 39.23  ? 114 VAL A CG2   1 
ATOM   881  N N     . LEU A 1 115 ? 59.527 11.956 -13.710 1.00 42.21  ? 115 LEU A N     1 
ATOM   882  C CA    . LEU A 1 115 ? 59.741 13.255 -14.329 1.00 44.99  ? 115 LEU A CA    1 
ATOM   883  C C     . LEU A 1 115 ? 60.502 13.022 -15.617 1.00 45.55  ? 115 LEU A C     1 
ATOM   884  O O     . LEU A 1 115 ? 59.906 12.616 -16.628 1.00 49.94  ? 115 LEU A O     1 
ATOM   885  C CB    . LEU A 1 115 ? 60.450 14.214 -13.361 1.00 42.30  ? 115 LEU A CB    1 
ATOM   886  C CG    . LEU A 1 115 ? 59.692 14.583 -12.078 1.00 45.71  ? 115 LEU A CG    1 
ATOM   887  C CD1   . LEU A 1 115 ? 60.561 15.411 -11.109 1.00 34.88  ? 115 LEU A CD1   1 
ATOM   888  C CD2   . LEU A 1 115 ? 58.397 15.315 -12.415 1.00 39.84  ? 115 LEU A CD2   1 
ATOM   889  N N     . VAL A 1 116 ? 61.827 13.228 -15.630 1.00 45.83  ? 116 VAL A N     1 
ATOM   890  C CA    . VAL A 1 116 ? 62.589 13.163 -16.877 1.00 46.29  ? 116 VAL A CA    1 
ATOM   891  C C     . VAL A 1 116 ? 62.519 11.768 -17.488 1.00 47.44  ? 116 VAL A C     1 
ATOM   892  O O     . VAL A 1 116 ? 62.442 11.616 -18.714 1.00 46.12  ? 116 VAL A O     1 
ATOM   893  C CB    . VAL A 1 116 ? 64.047 13.606 -16.646 1.00 45.39  ? 116 VAL A CB    1 
ATOM   894  C CG1   . VAL A 1 116 ? 64.750 12.692 -15.640 1.00 47.61  ? 116 VAL A CG1   1 
ATOM   895  C CG2   . VAL A 1 116 ? 64.802 13.623 -17.960 1.00 56.37  ? 116 VAL A CG2   1 
ATOM   896  N N     . GLU A 1 117 ? 62.525 10.727 -16.652 1.00 37.88  ? 117 GLU A N     1 
ATOM   897  C CA    . GLU A 1 117 ? 62.492 9.369  -17.189 1.00 46.47  ? 117 GLU A CA    1 
ATOM   898  C C     . GLU A 1 117 ? 61.129 9.040  -17.783 1.00 46.23  ? 117 GLU A C     1 
ATOM   899  O O     . GLU A 1 117 ? 61.041 8.261  -18.738 1.00 49.03  ? 117 GLU A O     1 
ATOM   900  C CB    . GLU A 1 117 ? 62.892 8.359  -16.101 1.00 48.04  ? 117 GLU A CB    1 
ATOM   901  C CG    . GLU A 1 117 ? 64.337 8.571  -15.634 1.00 43.47  ? 117 GLU A CG    1 
ATOM   902  C CD    . GLU A 1 117 ? 64.783 7.668  -14.488 1.00 55.77  ? 117 GLU A CD    1 
ATOM   903  O OE1   . GLU A 1 117 ? 64.120 6.639  -14.210 1.00 57.49  ? 117 GLU A OE1   1 
ATOM   904  O OE2   . GLU A 1 117 ? 65.821 8.002  -13.872 1.00 56.73  ? 117 GLU A OE2   1 
ATOM   905  N N     . ARG A 1 118 ? 60.060 9.626  -17.255 1.00 44.16  ? 118 ARG A N     1 
ATOM   906  C CA    . ARG A 1 118 ? 58.769 9.462  -17.906 1.00 47.88  ? 118 ARG A CA    1 
ATOM   907  C C     . ARG A 1 118 ? 58.720 10.247 -19.214 1.00 50.82  ? 118 ARG A C     1 
ATOM   908  O O     . ARG A 1 118 ? 58.370 9.698  -20.263 1.00 50.04  ? 118 ARG A O     1 
ATOM   909  C CB    . ARG A 1 118 ? 57.647 9.895  -16.969 1.00 43.38  ? 118 ARG A CB    1 
ATOM   910  C CG    . ARG A 1 118 ? 56.315 10.061 -17.678 1.00 51.84  ? 118 ARG A CG    1 
ATOM   911  C CD    . ARG A 1 118 ? 55.285 10.718 -16.781 1.00 55.35  ? 118 ARG A CD    1 
ATOM   912  N NE    . ARG A 1 118 ? 54.070 11.036 -17.521 1.00 60.01  ? 118 ARG A NE    1 
ATOM   913  C CZ    . ARG A 1 118 ? 52.965 11.533 -16.982 1.00 59.65  ? 118 ARG A CZ    1 
ATOM   914  N NH1   . ARG A 1 118 ? 52.881 11.791 -15.686 1.00 56.32  ? 118 ARG A NH1   1 
ATOM   915  N NH2   . ARG A 1 118 ? 51.917 11.774 -17.763 1.00 62.47  ? 118 ARG A NH2   1 
ATOM   916  N N     . ILE A 1 119 ? 59.114 11.526 -19.172 1.00 47.43  ? 119 ILE A N     1 
ATOM   917  C CA    . ILE A 1 119 ? 59.026 12.400 -20.345 1.00 52.77  ? 119 ILE A CA    1 
ATOM   918  C C     . ILE A 1 119 ? 59.897 11.881 -21.483 1.00 49.61  ? 119 ILE A C     1 
ATOM   919  O O     . ILE A 1 119 ? 59.515 11.943 -22.656 1.00 53.03  ? 119 ILE A O     1 
ATOM   920  C CB    . ILE A 1 119 ? 59.404 13.847 -19.962 1.00 60.92  ? 119 ILE A CB    1 
ATOM   921  C CG1   . ILE A 1 119 ? 58.165 14.640 -19.576 1.00 64.45  ? 119 ILE A CG1   1 
ATOM   922  C CG2   . ILE A 1 119 ? 60.083 14.570 -21.112 1.00 63.29  ? 119 ILE A CG2   1 
ATOM   923  C CD1   . ILE A 1 119 ? 57.585 14.243 -18.278 1.00 59.03  ? 119 ILE A CD1   1 
ATOM   924  N N     . GLU A 1 120 ? 61.087 11.385 -21.167 1.00 53.74  ? 120 GLU A N     1 
ATOM   925  C CA    . GLU A 1 120 ? 61.988 10.937 -22.218 1.00 54.08  ? 120 GLU A CA    1 
ATOM   926  C C     . GLU A 1 120 ? 61.700 9.511  -22.669 1.00 53.59  ? 120 GLU A C     1 
ATOM   927  O O     . GLU A 1 120 ? 62.354 9.032  -23.599 1.00 54.99  ? 120 GLU A O     1 
ATOM   928  C CB    . GLU A 1 120 ? 63.443 11.069 -21.755 1.00 48.23  ? 120 GLU A CB    1 
ATOM   929  C CG    . GLU A 1 120 ? 63.900 12.518 -21.584 1.00 54.73  ? 120 GLU A CG    1 
ATOM   930  C CD    . GLU A 1 120 ? 63.844 13.310 -22.886 1.00 68.07  ? 120 GLU A CD    1 
ATOM   931  O OE1   . GLU A 1 120 ? 64.407 12.846 -23.900 1.00 75.90  ? 120 GLU A OE1   1 
ATOM   932  O OE2   . GLU A 1 120 ? 63.227 14.396 -22.904 1.00 64.63  ? 120 GLU A OE2   1 
ATOM   933  N N     . GLY A 1 121 ? 60.742 8.827  -22.047 1.00 51.72  ? 121 GLY A N     1 
ATOM   934  C CA    . GLY A 1 121 ? 60.498 7.437  -22.371 1.00 51.02  ? 121 GLY A CA    1 
ATOM   935  C C     . GLY A 1 121 ? 61.544 6.461  -21.877 1.00 53.63  ? 121 GLY A C     1 
ATOM   936  O O     . GLY A 1 121 ? 61.545 5.311  -22.326 1.00 57.50  ? 121 GLY A O     1 
ATOM   937  N N     . PHE A 1 122 ? 62.445 6.878  -20.976 1.00 49.80  ? 122 PHE A N     1 
ATOM   938  C CA    . PHE A 1 122 ? 63.414 5.935  -20.410 1.00 54.80  ? 122 PHE A CA    1 
ATOM   939  C C     . PHE A 1 122 ? 62.716 4.898  -19.534 1.00 53.07  ? 122 PHE A C     1 
ATOM   940  O O     . PHE A 1 122 ? 63.091 3.720  -19.539 1.00 60.63  ? 122 PHE A O     1 
ATOM   941  C CB    . PHE A 1 122 ? 64.493 6.670  -19.599 1.00 50.05  ? 122 PHE A CB    1 
ATOM   942  C CG    . PHE A 1 122 ? 65.302 7.668  -20.394 1.00 53.11  ? 122 PHE A CG    1 
ATOM   943  C CD1   . PHE A 1 122 ? 65.430 7.552  -21.773 1.00 53.04  ? 122 PHE A CD1   1 
ATOM   944  C CD2   . PHE A 1 122 ? 65.928 8.728  -19.758 1.00 52.28  ? 122 PHE A CD2   1 
ATOM   945  C CE1   . PHE A 1 122 ? 66.169 8.475  -22.496 1.00 56.15  ? 122 PHE A CE1   1 
ATOM   946  C CE2   . PHE A 1 122 ? 66.667 9.655  -20.476 1.00 62.30  ? 122 PHE A CE2   1 
ATOM   947  C CZ    . PHE A 1 122 ? 66.789 9.527  -21.846 1.00 56.03  ? 122 PHE A CZ    1 
ATOM   948  N N     . ALA A 1 123 ? 61.716 5.321  -18.763 1.00 47.67  ? 123 ALA A N     1 
ATOM   949  C CA    . ALA A 1 123 ? 60.842 4.412  -18.031 1.00 49.80  ? 123 ALA A CA    1 
ATOM   950  C C     . ALA A 1 123 ? 59.612 4.118  -18.881 1.00 56.52  ? 123 ALA A C     1 
ATOM   951  O O     . ALA A 1 123 ? 59.017 5.041  -19.448 1.00 53.75  ? 123 ALA A O     1 
ATOM   952  C CB    . ALA A 1 123 ? 60.422 5.020  -16.694 1.00 44.54  ? 123 ALA A CB    1 
ATOM   953  N N     . THR A 1 124 ? 59.242 2.837  -18.983 1.00 49.80  ? 124 THR A N     1 
ATOM   954  C CA    . THR A 1 124 ? 58.018 2.464  -19.677 1.00 50.29  ? 124 THR A CA    1 
ATOM   955  C C     . THR A 1 124 ? 56.805 3.001  -18.926 1.00 52.92  ? 124 THR A C     1 
ATOM   956  O O     . THR A 1 124 ? 56.895 3.453  -17.780 1.00 47.03  ? 124 THR A O     1 
ATOM   957  C CB    . THR A 1 124 ? 57.889 0.944  -19.801 1.00 58.54  ? 124 THR A CB    1 
ATOM   958  O OG1   . THR A 1 124 ? 57.718 0.381  -18.493 1.00 55.83  ? 124 THR A OG1   1 
ATOM   959  C CG2   . THR A 1 124 ? 59.125 0.340  -20.452 1.00 49.75  ? 124 THR A CG2   1 
ATOM   960  N N     . LYS A 1 125 ? 55.648 2.931  -19.588 1.00 49.52  ? 125 LYS A N     1 
ATOM   961  C CA    . LYS A 1 125 ? 54.415 3.410  -18.972 1.00 54.22  ? 125 LYS A CA    1 
ATOM   962  C C     . LYS A 1 125 ? 54.127 2.682  -17.664 1.00 55.23  ? 125 LYS A C     1 
ATOM   963  O O     . LYS A 1 125 ? 53.756 3.312  -16.667 1.00 54.18  ? 125 LYS A O     1 
ATOM   964  C CB    . LYS A 1 125 ? 53.236 3.253  -19.931 1.00 52.96  ? 125 LYS A CB    1 
ATOM   965  C CG    . LYS A 1 125 ? 51.943 3.884  -19.406 1.00 59.70  ? 125 LYS A CG    1 
ATOM   966  C CD    . LYS A 1 125 ? 50.814 3.832  -20.436 1.00 73.32  ? 125 LYS A CD    1 
ATOM   967  C CE    . LYS A 1 125 ? 49.590 4.611  -19.960 1.00 79.21  ? 125 LYS A CE    1 
ATOM   968  N NZ    . LYS A 1 125 ? 48.425 4.467  -20.882 1.00 86.41  ? 125 LYS A NZ    1 
ATOM   969  N N     . ASP A 1 126 ? 54.283 1.356  -17.643 1.00 48.27  ? 126 ASP A N     1 
ATOM   970  C CA    . ASP A 1 126 ? 54.025 0.615  -16.411 1.00 55.74  ? 126 ASP A CA    1 
ATOM   971  C C     . ASP A 1 126 ? 54.967 1.056  -15.293 1.00 48.27  ? 126 ASP A C     1 
ATOM   972  O O     . ASP A 1 126 ? 54.543 1.227  -14.142 1.00 50.64  ? 126 ASP A O     1 
ATOM   973  C CB    . ASP A 1 126 ? 54.160 -0.886 -16.653 1.00 57.30  ? 126 ASP A CB    1 
ATOM   974  C CG    . ASP A 1 126 ? 54.047 -1.692 -15.360 1.00 78.29  ? 126 ASP A CG    1 
ATOM   975  O OD1   . ASP A 1 126 ? 52.938 -1.722 -14.775 1.00 76.91  ? 126 ASP A OD1   1 
ATOM   976  O OD2   . ASP A 1 126 ? 55.065 -2.283 -14.919 1.00 67.77  ? 126 ASP A OD2   1 
ATOM   977  N N     . GLU A 1 127 ? 56.238 1.279  -15.631 1.00 46.69  ? 127 GLU A N     1 
ATOM   978  C CA    . GLU A 1 127 ? 57.246 1.661  -14.645 1.00 49.27  ? 127 GLU A CA    1 
ATOM   979  C C     . GLU A 1 127 ? 56.899 2.981  -13.969 1.00 50.01  ? 127 GLU A C     1 
ATOM   980  O O     . GLU A 1 127 ? 56.755 3.047  -12.736 1.00 47.90  ? 127 GLU A O     1 
ATOM   981  C CB    . GLU A 1 127 ? 58.615 1.720  -15.321 1.00 45.29  ? 127 GLU A CB    1 
ATOM   982  C CG    . GLU A 1 127 ? 59.214 0.324  -15.502 1.00 50.57  ? 127 GLU A CG    1 
ATOM   983  C CD    . GLU A 1 127 ? 60.489 0.306  -16.322 1.00 52.11  ? 127 GLU A CD    1 
ATOM   984  O OE1   . GLU A 1 127 ? 60.732 1.262  -17.088 1.00 59.79  ? 127 GLU A OE1   1 
ATOM   985  O OE2   . GLU A 1 127 ? 61.252 -0.674 -16.207 1.00 56.37  ? 127 GLU A OE2   1 
ATOM   986  N N     . TRP A 1 128 ? 56.732 4.051  -14.757 1.00 46.27  ? 128 TRP A N     1 
ATOM   987  C CA    . TRP A 1 128 ? 56.452 5.323  -14.104 1.00 47.33  ? 128 TRP A CA    1 
ATOM   988  C C     . TRP A 1 128 ? 55.046 5.350  -13.522 1.00 49.01  ? 128 TRP A C     1 
ATOM   989  O O     . TRP A 1 128 ? 54.824 6.002  -12.497 1.00 47.26  ? 128 TRP A O     1 
ATOM   990  C CB    . TRP A 1 128 ? 56.706 6.512  -15.043 1.00 49.58  ? 128 TRP A CB    1 
ATOM   991  C CG    . TRP A 1 128 ? 55.821 6.675  -16.247 1.00 52.12  ? 128 TRP A CG    1 
ATOM   992  C CD1   . TRP A 1 128 ? 56.136 6.364  -17.541 1.00 53.46  ? 128 TRP A CD1   1 
ATOM   993  C CD2   . TRP A 1 128 ? 54.505 7.247  -16.282 1.00 53.63  ? 128 TRP A CD2   1 
ATOM   994  N NE1   . TRP A 1 128 ? 55.087 6.682  -18.377 1.00 55.77  ? 128 TRP A NE1   1 
ATOM   995  C CE2   . TRP A 1 128 ? 54.074 7.227  -17.630 1.00 54.94  ? 128 TRP A CE2   1 
ATOM   996  C CE3   . TRP A 1 128 ? 53.643 7.763  -15.306 1.00 51.60  ? 128 TRP A CE3   1 
ATOM   997  C CZ2   . TRP A 1 128 ? 52.815 7.696  -18.025 1.00 52.68  ? 128 TRP A CZ2   1 
ATOM   998  C CZ3   . TRP A 1 128 ? 52.390 8.235  -15.705 1.00 56.09  ? 128 TRP A CZ3   1 
ATOM   999  C CH2   . TRP A 1 128 ? 51.994 8.198  -17.053 1.00 53.10  ? 128 TRP A CH2   1 
ATOM   1000 N N     . SER A 1 129 ? 54.102 4.610  -14.114 1.00 47.34  ? 129 SER A N     1 
ATOM   1001 C CA    . SER A 1 129 ? 52.740 4.591  -13.586 1.00 46.66  ? 129 SER A CA    1 
ATOM   1002 C C     . SER A 1 129 ? 52.684 3.991  -12.185 1.00 46.97  ? 129 SER A C     1 
ATOM   1003 O O     . SER A 1 129 ? 51.971 4.507  -11.318 1.00 48.31  ? 129 SER A O     1 
ATOM   1004 C CB    . SER A 1 129 ? 51.815 3.818  -14.529 1.00 46.02  ? 129 SER A CB    1 
ATOM   1005 O OG    . SER A 1 129 ? 51.599 4.559  -15.711 1.00 61.97  ? 129 SER A OG    1 
ATOM   1006 N N     . ARG A 1 130 ? 53.403 2.886  -11.948 1.00 42.13  ? 130 ARG A N     1 
ATOM   1007 C CA    . ARG A 1 130 ? 53.405 2.261  -10.625 1.00 47.44  ? 130 ARG A CA    1 
ATOM   1008 C C     . ARG A 1 130 ? 54.371 2.942  -9.658  1.00 44.47  ? 130 ARG A C     1 
ATOM   1009 O O     . ARG A 1 130 ? 54.320 2.679  -8.436  1.00 45.75  ? 130 ARG A O     1 
ATOM   1010 C CB    . ARG A 1 130 ? 53.768 0.779  -10.754 1.00 41.74  ? 130 ARG A CB    1 
ATOM   1011 C CG    . ARG A 1 130 ? 55.245 0.551  -11.124 1.00 45.98  ? 130 ARG A CG    1 
ATOM   1012 C CD    . ARG A 1 130 ? 55.632 -0.940 -11.124 1.00 44.65  ? 130 ARG A CD    1 
ATOM   1013 N NE    . ARG A 1 130 ? 57.080 -1.122 -11.119 1.00 42.58  ? 130 ARG A NE    1 
ATOM   1014 C CZ    . ARG A 1 130 ? 57.790 -1.557 -12.153 1.00 51.73  ? 130 ARG A CZ    1 
ATOM   1015 N NH1   . ARG A 1 130 ? 57.216 -1.883 -13.301 1.00 46.77  ? 130 ARG A NH1   1 
ATOM   1016 N NH2   . ARG A 1 130 ? 59.110 -1.684 -12.028 1.00 44.50  ? 130 ARG A NH2   1 
ATOM   1017 N N     . ALA A 1 131 ? 55.255 3.804  -10.181 1.00 43.60  ? 131 ALA A N     1 
ATOM   1018 C CA    . ALA A 1 131 ? 56.283 4.388  -9.327  1.00 41.91  ? 131 ALA A CA    1 
ATOM   1019 C C     . ALA A 1 131 ? 55.709 5.283  -8.233  1.00 42.84  ? 131 ALA A C     1 
ATOM   1020 O O     . ALA A 1 131 ? 56.324 5.405  -7.175  1.00 42.50  ? 131 ALA A O     1 
ATOM   1021 C CB    . ALA A 1 131 ? 57.290 5.173  -10.163 1.00 41.22  ? 131 ALA A CB    1 
ATOM   1022 N N     . TYR A 1 132 ? 54.566 5.940  -8.459  1.00 41.27  ? 132 TYR A N     1 
ATOM   1023 C CA    . TYR A 1 132 ? 54.040 6.843  -7.432  1.00 43.05  ? 132 TYR A CA    1 
ATOM   1024 C C     . TYR A 1 132 ? 53.799 6.107  -6.119  1.00 45.79  ? 132 TYR A C     1 
ATOM   1025 O O     . TYR A 1 132 ? 54.225 6.558  -5.048  1.00 45.57  ? 132 TYR A O     1 
ATOM   1026 C CB    . TYR A 1 132 ? 52.742 7.507  -7.899  1.00 47.33  ? 132 TYR A CB    1 
ATOM   1027 C CG    . TYR A 1 132 ? 52.832 8.247  -9.212  1.00 47.68  ? 132 TYR A CG    1 
ATOM   1028 C CD1   . TYR A 1 132 ? 53.428 9.503  -9.293  1.00 45.38  ? 132 TYR A CD1   1 
ATOM   1029 C CD2   . TYR A 1 132 ? 52.297 7.693  -10.372 1.00 49.00  ? 132 TYR A CD2   1 
ATOM   1030 C CE1   . TYR A 1 132 ? 53.499 10.186 -10.504 1.00 47.44  ? 132 TYR A CE1   1 
ATOM   1031 C CE2   . TYR A 1 132 ? 52.359 8.364  -11.580 1.00 46.99  ? 132 TYR A CE2   1 
ATOM   1032 C CZ    . TYR A 1 132 ? 52.960 9.605  -11.643 1.00 48.36  ? 132 TYR A CZ    1 
ATOM   1033 O OH    . TYR A 1 132 ? 53.016 10.252 -12.855 1.00 51.50  ? 132 TYR A OH    1 
ATOM   1034 N N     . GLU A 1 133 ? 53.112 4.966  -6.179  1.00 43.99  ? 133 GLU A N     1 
ATOM   1035 C CA    . GLU A 1 133 ? 52.855 4.234  -4.949  1.00 45.01  ? 133 GLU A CA    1 
ATOM   1036 C C     . GLU A 1 133 ? 54.104 3.530  -4.444  1.00 43.71  ? 133 GLU A C     1 
ATOM   1037 O O     . GLU A 1 133 ? 54.288 3.435  -3.224  1.00 43.71  ? 133 GLU A O     1 
ATOM   1038 C CB    . GLU A 1 133 ? 51.703 3.245  -5.138  1.00 43.55  ? 133 GLU A CB    1 
ATOM   1039 C CG    . GLU A 1 133 ? 50.358 3.934  -5.427  1.00 60.82  ? 133 GLU A CG    1 
ATOM   1040 C CD    . GLU A 1 133 ? 50.004 5.067  -4.441  1.00 64.33  ? 133 GLU A CD    1 
ATOM   1041 O OE1   . GLU A 1 133 ? 50.341 4.979  -3.236  1.00 62.01  ? 133 GLU A OE1   1 
ATOM   1042 O OE2   . GLU A 1 133 ? 49.367 6.052  -4.881  1.00 76.57  ? 133 GLU A OE2   1 
ATOM   1043 N N     . GLU A 1 134 ? 54.973 3.038  -5.343  1.00 39.31  ? 134 GLU A N     1 
ATOM   1044 C CA    . GLU A 1 134 ? 56.254 2.509  -4.861  1.00 40.03  ? 134 GLU A CA    1 
ATOM   1045 C C     . GLU A 1 134 ? 56.998 3.549  -4.028  1.00 43.04  ? 134 GLU A C     1 
ATOM   1046 O O     . GLU A 1 134 ? 57.523 3.246  -2.947  1.00 40.55  ? 134 GLU A O     1 
ATOM   1047 C CB    . GLU A 1 134 ? 57.126 2.061  -6.029  1.00 39.03  ? 134 GLU A CB    1 
ATOM   1048 C CG    . GLU A 1 134 ? 56.581 0.859  -6.804  1.00 41.35  ? 134 GLU A CG    1 
ATOM   1049 C CD    . GLU A 1 134 ? 57.456 0.506  -7.999  1.00 44.52  ? 134 GLU A CD    1 
ATOM   1050 O OE1   . GLU A 1 134 ? 58.190 1.398  -8.495  1.00 39.52  ? 134 GLU A OE1   1 
ATOM   1051 O OE2   . GLU A 1 134 ? 57.411 -0.656 -8.444  1.00 42.02  ? 134 GLU A OE2   1 
ATOM   1052 N N     . ILE A 1 135 ? 57.031 4.791  -4.509  1.00 43.37  ? 135 ILE A N     1 
ATOM   1053 C CA    . ILE A 1 135 ? 57.751 5.849  -3.815  1.00 43.60  ? 135 ILE A CA    1 
ATOM   1054 C C     . ILE A 1 135 ? 57.058 6.200  -2.507  1.00 38.43  ? 135 ILE A C     1 
ATOM   1055 O O     . ILE A 1 135 ? 57.718 6.377  -1.476  1.00 40.59  ? 135 ILE A O     1 
ATOM   1056 C CB    . ILE A 1 135 ? 57.904 7.076  -4.733  1.00 40.93  ? 135 ILE A CB    1 
ATOM   1057 C CG1   . ILE A 1 135 ? 58.933 6.771  -5.824  1.00 37.40  ? 135 ILE A CG1   1 
ATOM   1058 C CG2   . ILE A 1 135 ? 58.329 8.303  -3.920  1.00 37.31  ? 135 ILE A CG2   1 
ATOM   1059 C CD1   . ILE A 1 135 ? 58.900 7.723  -6.998  1.00 40.70  ? 135 ILE A CD1   1 
ATOM   1060 N N     . ASN A 1 136 ? 55.722 6.312  -2.526  1.00 37.03  ? 136 ASN A N     1 
ATOM   1061 C CA    . ASN A 1 136 ? 54.998 6.548  -1.278  1.00 42.11  ? 136 ASN A CA    1 
ATOM   1062 C C     . ASN A 1 136 ? 55.334 5.479  -0.243  1.00 43.65  ? 136 ASN A C     1 
ATOM   1063 O O     . ASN A 1 136 ? 55.584 5.796  0.928   1.00 39.90  ? 136 ASN A O     1 
ATOM   1064 C CB    . ASN A 1 136 ? 53.489 6.582  -1.520  1.00 44.57  ? 136 ASN A CB    1 
ATOM   1065 C CG    . ASN A 1 136 ? 53.018 7.860  -2.203  1.00 49.08  ? 136 ASN A CG    1 
ATOM   1066 O OD1   . ASN A 1 136 ? 53.636 8.918  -2.086  1.00 42.38  ? 136 ASN A OD1   1 
ATOM   1067 N ND2   . ASN A 1 136 ? 51.890 7.763  -2.904  1.00 46.81  ? 136 ASN A ND2   1 
ATOM   1068 N N     . ASN A 1 137 ? 55.359 4.205  -0.659  1.00 42.35  ? 137 ASN A N     1 
ATOM   1069 C CA    . ASN A 1 137 ? 55.596 3.123  0.295   1.00 45.12  ? 137 ASN A CA    1 
ATOM   1070 C C     . ASN A 1 137 ? 57.023 3.171  0.837   1.00 37.00  ? 137 ASN A C     1 
ATOM   1071 O O     . ASN A 1 137 ? 57.245 2.959  2.036   1.00 43.05  ? 137 ASN A O     1 
ATOM   1072 C CB    . ASN A 1 137 ? 55.310 1.762  -0.354  1.00 39.84  ? 137 ASN A CB    1 
ATOM   1073 C CG    . ASN A 1 137 ? 53.855 1.591  -0.778  1.00 39.19  ? 137 ASN A CG    1 
ATOM   1074 O OD1   . ASN A 1 137 ? 52.958 2.279  -0.293  1.00 44.02  ? 137 ASN A OD1   1 
ATOM   1075 N ND2   . ASN A 1 137 ? 53.619 0.654  -1.681  1.00 41.81  ? 137 ASN A ND2   1 
ATOM   1076 N N     . PHE A 1 138 ? 57.999 3.462  -0.033  1.00 39.54  ? 138 PHE A N     1 
ATOM   1077 C CA    . PHE A 1 138 ? 59.388 3.620  0.403   1.00 40.93  ? 138 PHE A CA    1 
ATOM   1078 C C     . PHE A 1 138 ? 59.518 4.738  1.442   1.00 43.27  ? 138 PHE A C     1 
ATOM   1079 O O     . PHE A 1 138 ? 60.065 4.540  2.555   1.00 36.91  ? 138 PHE A O     1 
ATOM   1080 C CB    . PHE A 1 138 ? 60.254 3.884  -0.838  1.00 38.70  ? 138 PHE A CB    1 
ATOM   1081 C CG    . PHE A 1 138 ? 61.602 4.484  -0.557  1.00 36.63  ? 138 PHE A CG    1 
ATOM   1082 C CD1   . PHE A 1 138 ? 62.477 3.888  0.340   1.00 37.20  ? 138 PHE A CD1   1 
ATOM   1083 C CD2   . PHE A 1 138 ? 62.018 5.617  -1.246  1.00 37.48  ? 138 PHE A CD2   1 
ATOM   1084 C CE1   . PHE A 1 138 ? 63.719 4.437  0.586   1.00 35.48  ? 138 PHE A CE1   1 
ATOM   1085 C CE2   . PHE A 1 138 ? 63.276 6.172  -1.021  1.00 36.11  ? 138 PHE A CE2   1 
ATOM   1086 C CZ    . PHE A 1 138 ? 64.128 5.578  -0.101  1.00 42.36  ? 138 PHE A CZ    1 
ATOM   1087 N N     . GLU A 1 139 ? 58.976 5.917  1.108   1.00 35.76  ? 139 GLU A N     1 
ATOM   1088 C CA    . GLU A 1 139 ? 59.062 7.054  2.017   1.00 41.25  ? 139 GLU A CA    1 
ATOM   1089 C C     . GLU A 1 139 ? 58.348 6.766  3.333   1.00 41.09  ? 139 GLU A C     1 
ATOM   1090 O O     . GLU A 1 139 ? 58.820 7.174  4.395   1.00 41.23  ? 139 GLU A O     1 
ATOM   1091 C CB    . GLU A 1 139 ? 58.498 8.309  1.337   1.00 36.31  ? 139 GLU A CB    1 
ATOM   1092 C CG    . GLU A 1 139 ? 59.399 8.818  0.202   1.00 38.61  ? 139 GLU A CG    1 
ATOM   1093 C CD    . GLU A 1 139 ? 58.841 10.026 -0.524  1.00 39.75  ? 139 GLU A CD    1 
ATOM   1094 O OE1   . GLU A 1 139 ? 57.772 10.535 -0.126  1.00 41.97  ? 139 GLU A OE1   1 
ATOM   1095 O OE2   . GLU A 1 139 ? 59.487 10.467 -1.500  1.00 41.89  ? 139 GLU A OE2   1 
ATOM   1096 N N     . LYS A 1 140 ? 57.235 6.033  3.285   1.00 37.16  ? 140 LYS A N     1 
ATOM   1097 C CA    . LYS A 1 140 ? 56.491 5.720  4.504   1.00 41.24  ? 140 LYS A CA    1 
ATOM   1098 C C     . LYS A 1 140 ? 57.262 4.744  5.394   1.00 41.18  ? 140 LYS A C     1 
ATOM   1099 O O     . LYS A 1 140 ? 57.218 4.850  6.629   1.00 42.96  ? 140 LYS A O     1 
ATOM   1100 C CB    . LYS A 1 140 ? 55.121 5.151  4.137   1.00 39.35  ? 140 LYS A CB    1 
ATOM   1101 C CG    . LYS A 1 140 ? 54.192 4.879  5.331   1.00 51.40  ? 140 LYS A CG    1 
ATOM   1102 C CD    . LYS A 1 140 ? 53.456 6.138  5.752   1.00 57.99  ? 140 LYS A CD    1 
ATOM   1103 C CE    . LYS A 1 140 ? 52.406 5.848  6.826   1.00 60.75  ? 140 LYS A CE    1 
ATOM   1104 N NZ    . LYS A 1 140 ? 51.702 7.100  7.233   1.00 70.09  ? 140 LYS A NZ    1 
ATOM   1105 N N     . ILE A 1 141 ? 57.966 3.783  4.787   1.00 39.11  ? 141 ILE A N     1 
ATOM   1106 C CA    . ILE A 1 141 ? 58.876 2.942  5.569   1.00 40.65  ? 141 ILE A CA    1 
ATOM   1107 C C     . ILE A 1 141 ? 59.809 3.818  6.392   1.00 39.14  ? 141 ILE A C     1 
ATOM   1108 O O     . ILE A 1 141 ? 59.984 3.618  7.601   1.00 40.47  ? 141 ILE A O     1 
ATOM   1109 C CB    . ILE A 1 141 ? 59.672 1.995  4.653   1.00 37.84  ? 141 ILE A CB    1 
ATOM   1110 C CG1   . ILE A 1 141 ? 58.777 0.874  4.125   1.00 39.79  ? 141 ILE A CG1   1 
ATOM   1111 C CG2   . ILE A 1 141 ? 60.864 1.398  5.411   1.00 35.23  ? 141 ILE A CG2   1 
ATOM   1112 C CD1   . ILE A 1 141 ? 59.464 -0.008 3.111   1.00 40.00  ? 141 ILE A CD1   1 
ATOM   1113 N N     . LEU A 1 142 ? 60.406 4.818  5.746   1.00 39.28  ? 142 LEU A N     1 
ATOM   1114 C CA    . LEU A 1 142 ? 61.373 5.655  6.465   1.00 36.69  ? 142 LEU A CA    1 
ATOM   1115 C C     . LEU A 1 142 ? 60.701 6.573  7.498   1.00 46.39  ? 142 LEU A C     1 
ATOM   1116 O O     . LEU A 1 142 ? 61.201 6.719  8.624   1.00 37.35  ? 142 LEU A O     1 
ATOM   1117 C CB    . LEU A 1 142 ? 62.195 6.474  5.468   1.00 31.04  ? 142 LEU A CB    1 
ATOM   1118 C CG    . LEU A 1 142 ? 63.053 5.661  4.491   1.00 36.40  ? 142 LEU A CG    1 
ATOM   1119 C CD1   . LEU A 1 142 ? 63.835 6.605  3.564   1.00 31.02  ? 142 LEU A CD1   1 
ATOM   1120 C CD2   . LEU A 1 142 ? 64.021 4.727  5.252   1.00 30.18  ? 142 LEU A CD2   1 
ATOM   1121 N N     . THR A 1 143 ? 59.579 7.212  7.138   1.00 38.83  ? 143 THR A N     1 
ATOM   1122 C CA    . THR A 1 143 ? 59.014 8.233  8.021   1.00 40.35  ? 143 THR A CA    1 
ATOM   1123 C C     . THR A 1 143 ? 58.300 7.619  9.213   1.00 42.61  ? 143 THR A C     1 
ATOM   1124 O O     . THR A 1 143 ? 58.172 8.278  10.249  1.00 42.77  ? 143 THR A O     1 
ATOM   1125 C CB    . THR A 1 143 ? 58.045 9.162  7.278   1.00 42.00  ? 143 THR A CB    1 
ATOM   1126 O OG1   . THR A 1 143 ? 56.950 8.410  6.740   1.00 43.28  ? 143 THR A OG1   1 
ATOM   1127 C CG2   . THR A 1 143 ? 58.755 9.925  6.164   1.00 38.62  ? 143 THR A CG2   1 
ATOM   1128 N N     . ALA A 1 144 ? 57.816 6.377  9.093   1.00 39.47  ? 144 ALA A N     1 
ATOM   1129 C CA    . ALA A 1 144 ? 57.267 5.714  10.275  1.00 42.29  ? 144 ALA A CA    1 
ATOM   1130 C C     . ALA A 1 144 ? 58.354 5.352  11.277  1.00 40.48  ? 144 ALA A C     1 
ATOM   1131 O O     . ALA A 1 144 ? 58.044 5.095  12.441  1.00 43.02  ? 144 ALA A O     1 
ATOM   1132 C CB    . ALA A 1 144 ? 56.490 4.454  9.886   1.00 41.46  ? 144 ALA A CB    1 
ATOM   1133 N N     . GLY A 1 145 ? 59.613 5.314  10.848  1.00 44.78  ? 145 GLY A N     1 
ATOM   1134 C CA    . GLY A 1 145 ? 60.732 5.111  11.747  1.00 38.53  ? 145 GLY A CA    1 
ATOM   1135 C C     . GLY A 1 145 ? 61.331 6.435  12.173  1.00 48.43  ? 145 GLY A C     1 
ATOM   1136 O O     . GLY A 1 145 ? 60.599 7.337  12.589  1.00 39.44  ? 145 GLY A O     1 
ATOM   1137 N N     . ASP A 1 146 ? 62.650 6.588  12.034  1.00 39.60  ? 146 ASP A N     1 
ATOM   1138 C CA    . ASP A 1 146 ? 63.322 7.750  12.606  1.00 43.40  ? 146 ASP A CA    1 
ATOM   1139 C C     . ASP A 1 146 ? 63.873 8.683  11.535  1.00 40.13  ? 146 ASP A C     1 
ATOM   1140 O O     . ASP A 1 146 ? 65.025 9.121  11.615  1.00 39.25  ? 146 ASP A O     1 
ATOM   1141 C CB    . ASP A 1 146 ? 64.443 7.301  13.544  1.00 39.08  ? 146 ASP A CB    1 
ATOM   1142 C CG    . ASP A 1 146 ? 63.910 6.659  14.812  1.00 44.55  ? 146 ASP A CG    1 
ATOM   1143 O OD1   . ASP A 1 146 ? 62.800 7.036  15.250  1.00 47.10  ? 146 ASP A OD1   1 
ATOM   1144 O OD2   . ASP A 1 146 ? 64.603 5.781  15.364  1.00 48.13  ? 146 ASP A OD2   1 
ATOM   1145 N N     . TYR A 1 147 ? 63.045 9.009  10.547  1.00 37.93  ? 147 TYR A N     1 
ATOM   1146 C CA    . TYR A 1 147 ? 63.416 9.897  9.460   1.00 39.81  ? 147 TYR A CA    1 
ATOM   1147 C C     . TYR A 1 147 ? 62.296 10.894 9.224   1.00 44.34  ? 147 TYR A C     1 
ATOM   1148 O O     . TYR A 1 147 ? 61.115 10.539 9.279   1.00 39.19  ? 147 TYR A O     1 
ATOM   1149 C CB    . TYR A 1 147 ? 63.683 9.126  8.159   1.00 34.62  ? 147 TYR A CB    1 
ATOM   1150 C CG    . TYR A 1 147 ? 64.957 8.312  8.152   1.00 33.24  ? 147 TYR A CG    1 
ATOM   1151 C CD1   . TYR A 1 147 ? 66.183 8.906  7.865   1.00 37.52  ? 147 TYR A CD1   1 
ATOM   1152 C CD2   . TYR A 1 147 ? 64.937 6.947  8.418   1.00 37.45  ? 147 TYR A CD2   1 
ATOM   1153 C CE1   . TYR A 1 147 ? 67.359 8.159  7.845   1.00 33.45  ? 147 TYR A CE1   1 
ATOM   1154 C CE2   . TYR A 1 147 ? 66.107 6.192  8.410   1.00 36.15  ? 147 TYR A CE2   1 
ATOM   1155 C CZ    . TYR A 1 147 ? 67.312 6.807  8.108   1.00 36.01  ? 147 TYR A CZ    1 
ATOM   1156 O OH    . TYR A 1 147 ? 68.473 6.078  8.090   1.00 36.14  ? 147 TYR A OH    1 
ATOM   1157 N N     . ILE A 1 148 ? 62.686 12.135 8.965   1.00 39.98  ? 148 ILE A N     1 
ATOM   1158 C CA    . ILE A 1 148 ? 61.804 13.191 8.489   1.00 39.29  ? 148 ILE A CA    1 
ATOM   1159 C C     . ILE A 1 148 ? 62.099 13.410 7.013   1.00 38.33  ? 148 ILE A C     1 
ATOM   1160 O O     . ILE A 1 148 ? 63.267 13.458 6.613   1.00 38.16  ? 148 ILE A O     1 
ATOM   1161 C CB    . ILE A 1 148 ? 62.024 14.481 9.298   1.00 37.10  ? 148 ILE A CB    1 
ATOM   1162 C CG1   . ILE A 1 148 ? 61.508 14.283 10.731  1.00 39.81  ? 148 ILE A CG1   1 
ATOM   1163 C CG2   . ILE A 1 148 ? 61.396 15.697 8.572   1.00 34.22  ? 148 ILE A CG2   1 
ATOM   1164 C CD1   . ILE A 1 148 ? 62.022 15.302 11.738  1.00 42.49  ? 148 ILE A CD1   1 
ATOM   1165 N N     . ILE A 1 149 ? 61.053 13.520 6.195   1.00 37.91  ? 149 ILE A N     1 
ATOM   1166 C CA    . ILE A 1 149 ? 61.224 13.737 4.762   1.00 41.05  ? 149 ILE A CA    1 
ATOM   1167 C C     . ILE A 1 149 ? 60.467 14.998 4.367   1.00 44.39  ? 149 ILE A C     1 
ATOM   1168 O O     . ILE A 1 149 ? 59.301 15.170 4.743   1.00 40.69  ? 149 ILE A O     1 
ATOM   1169 C CB    . ILE A 1 149 ? 60.747 12.529 3.937   1.00 39.39  ? 149 ILE A CB    1 
ATOM   1170 C CG1   . ILE A 1 149 ? 61.660 11.317 4.177   1.00 37.87  ? 149 ILE A CG1   1 
ATOM   1171 C CG2   . ILE A 1 149 ? 60.724 12.874 2.451   1.00 37.91  ? 149 ILE A CG2   1 
ATOM   1172 C CD1   . ILE A 1 149 ? 61.205 10.047 3.464   1.00 33.14  ? 149 ILE A CD1   1 
ATOM   1173 N N     . ILE A 1 150 ? 61.129 15.884 3.618   1.00 39.71  ? 150 ILE A N     1 
ATOM   1174 C CA    . ILE A 1 150 ? 60.443 17.016 2.989   1.00 40.00  ? 150 ILE A CA    1 
ATOM   1175 C C     . ILE A 1 150 ? 60.870 17.084 1.530   1.00 37.21  ? 150 ILE A C     1 
ATOM   1176 O O     . ILE A 1 150 ? 62.056 16.913 1.217   1.00 36.99  ? 150 ILE A O     1 
ATOM   1177 C CB    . ILE A 1 150 ? 60.744 18.364 3.676   1.00 40.87  ? 150 ILE A CB    1 
ATOM   1178 C CG1   . ILE A 1 150 ? 60.808 18.214 5.189   1.00 44.81  ? 150 ILE A CG1   1 
ATOM   1179 C CG2   . ILE A 1 150 ? 59.697 19.427 3.277   1.00 44.85  ? 150 ILE A CG2   1 
ATOM   1180 C CD1   . ILE A 1 150 ? 61.395 19.424 5.884   1.00 50.39  ? 150 ILE A CD1   1 
ATOM   1181 N N     . LYS A 1 151 ? 59.915 17.355 0.638   1.00 36.09  ? 151 LYS A N     1 
ATOM   1182 C CA    . LYS A 1 151 ? 60.202 17.476 -0.784  1.00 38.21  ? 151 LYS A CA    1 
ATOM   1183 C C     . LYS A 1 151 ? 59.842 18.884 -1.246  1.00 40.36  ? 151 LYS A C     1 
ATOM   1184 O O     . LYS A 1 151 ? 58.762 19.380 -0.925  1.00 41.27  ? 151 LYS A O     1 
ATOM   1185 C CB    . LYS A 1 151 ? 59.430 16.415 -1.568  1.00 39.05  ? 151 LYS A CB    1 
ATOM   1186 C CG    . LYS A 1 151 ? 59.838 14.970 -1.216  1.00 40.43  ? 151 LYS A CG    1 
ATOM   1187 C CD    . LYS A 1 151 ? 58.723 14.183 -0.535  1.00 40.59  ? 151 LYS A CD    1 
ATOM   1188 C CE    . LYS A 1 151 ? 57.485 14.080 -1.411  1.00 38.32  ? 151 LYS A CE    1 
ATOM   1189 N NZ    . LYS A 1 151 ? 56.568 12.985 -0.956  1.00 38.35  ? 151 LYS A NZ    1 
ATOM   1190 N N     . PHE A 1 152 ? 60.754 19.529 -1.973  1.00 39.94  ? 152 PHE A N     1 
ATOM   1191 C CA    . PHE A 1 152 ? 60.592 20.889 -2.474  1.00 42.65  ? 152 PHE A CA    1 
ATOM   1192 C C     . PHE A 1 152 ? 60.541 20.874 -3.992  1.00 39.69  ? 152 PHE A C     1 
ATOM   1193 O O     . PHE A 1 152 ? 61.408 20.276 -4.633  1.00 39.93  ? 152 PHE A O     1 
ATOM   1194 C CB    . PHE A 1 152 ? 61.753 21.790 -2.045  1.00 40.80  ? 152 PHE A CB    1 
ATOM   1195 C CG    . PHE A 1 152 ? 61.820 22.036 -0.578  1.00 40.68  ? 152 PHE A CG    1 
ATOM   1196 C CD1   . PHE A 1 152 ? 61.001 22.985 0.012   1.00 40.40  ? 152 PHE A CD1   1 
ATOM   1197 C CD2   . PHE A 1 152 ? 62.702 21.323 0.214   1.00 42.77  ? 152 PHE A CD2   1 
ATOM   1198 C CE1   . PHE A 1 152 ? 61.063 23.219 1.369   1.00 45.88  ? 152 PHE A CE1   1 
ATOM   1199 C CE2   . PHE A 1 152 ? 62.764 21.551 1.575   1.00 42.59  ? 152 PHE A CE2   1 
ATOM   1200 C CZ    . PHE A 1 152 ? 61.944 22.501 2.150   1.00 37.77  ? 152 PHE A CZ    1 
ATOM   1201 N N     . TRP A 1 153 ? 59.546 21.542 -4.562  1.00 40.73  ? 153 TRP A N     1 
ATOM   1202 C CA    . TRP A 1 153 ? 59.505 21.804 -5.995  1.00 42.63  ? 153 TRP A CA    1 
ATOM   1203 C C     . TRP A 1 153 ? 59.704 23.293 -6.210  1.00 46.10  ? 153 TRP A C     1 
ATOM   1204 O O     . TRP A 1 153 ? 58.845 24.090 -5.826  1.00 43.13  ? 153 TRP A O     1 
ATOM   1205 C CB    . TRP A 1 153 ? 58.182 21.373 -6.620  1.00 40.92  ? 153 TRP A CB    1 
ATOM   1206 C CG    . TRP A 1 153 ? 58.070 21.809 -8.068  1.00 45.93  ? 153 TRP A CG    1 
ATOM   1207 C CD1   . TRP A 1 153 ? 57.519 22.972 -8.544  1.00 47.46  ? 153 TRP A CD1   1 
ATOM   1208 C CD2   . TRP A 1 153 ? 58.538 21.091 -9.218  1.00 43.91  ? 153 TRP A CD2   1 
ATOM   1209 N NE1   . TRP A 1 153 ? 57.610 23.015 -9.918  1.00 45.51  ? 153 TRP A NE1   1 
ATOM   1210 C CE2   . TRP A 1 153 ? 58.227 21.872 -10.358 1.00 46.36  ? 153 TRP A CE2   1 
ATOM   1211 C CE3   . TRP A 1 153 ? 59.174 19.856 -9.397  1.00 42.73  ? 153 TRP A CE3   1 
ATOM   1212 C CZ2   . TRP A 1 153 ? 58.538 21.460 -11.656 1.00 39.99  ? 153 TRP A CZ2   1 
ATOM   1213 C CZ3   . TRP A 1 153 ? 59.486 19.446 -10.695 1.00 47.71  ? 153 TRP A CZ3   1 
ATOM   1214 C CH2   . TRP A 1 153 ? 59.165 20.252 -11.806 1.00 42.54  ? 153 TRP A CH2   1 
ATOM   1215 N N     . LEU A 1 154 ? 60.815 23.667 -6.840  1.00 40.04  ? 154 LEU A N     1 
ATOM   1216 C CA    . LEU A 1 154 ? 61.080 25.072 -7.137  1.00 43.19  ? 154 LEU A CA    1 
ATOM   1217 C C     . LEU A 1 154 ? 60.463 25.416 -8.488  1.00 46.88  ? 154 LEU A C     1 
ATOM   1218 O O     . LEU A 1 154 ? 60.926 24.932 -9.528  1.00 43.48  ? 154 LEU A O     1 
ATOM   1219 C CB    . LEU A 1 154 ? 62.578 25.361 -7.124  1.00 45.66  ? 154 LEU A CB    1 
ATOM   1220 C CG    . LEU A 1 154 ? 63.084 25.704 -5.721  1.00 55.09  ? 154 LEU A CG    1 
ATOM   1221 C CD1   . LEU A 1 154 ? 63.070 24.466 -4.830  1.00 43.56  ? 154 LEU A CD1   1 
ATOM   1222 C CD2   . LEU A 1 154 ? 64.456 26.328 -5.773  1.00 46.36  ? 154 LEU A CD2   1 
ATOM   1223 N N     . HIS A 1 155 ? 59.424 26.254 -8.474  1.00 43.86  ? 155 HIS A N     1 
ATOM   1224 C CA    . HIS A 1 155 ? 58.762 26.696 -9.699  1.00 47.67  ? 155 HIS A CA    1 
ATOM   1225 C C     . HIS A 1 155 ? 59.444 27.932 -10.265 1.00 49.59  ? 155 HIS A C     1 
ATOM   1226 O O     . HIS A 1 155 ? 59.823 28.842 -9.524  1.00 50.93  ? 155 HIS A O     1 
ATOM   1227 C CB    . HIS A 1 155 ? 57.289 27.020 -9.444  1.00 45.01  ? 155 HIS A CB    1 
ATOM   1228 C CG    . HIS A 1 155 ? 56.630 27.742 -10.579 1.00 48.88  ? 155 HIS A CG    1 
ATOM   1229 N ND1   . HIS A 1 155 ? 56.216 27.102 -11.727 1.00 55.76  ? 155 HIS A ND1   1 
ATOM   1230 C CD2   . HIS A 1 155 ? 56.335 29.054 -10.752 1.00 53.29  ? 155 HIS A CD2   1 
ATOM   1231 C CE1   . HIS A 1 155 ? 55.677 27.984 -12.552 1.00 54.62  ? 155 HIS A CE1   1 
ATOM   1232 N NE2   . HIS A 1 155 ? 55.739 29.177 -11.985 1.00 61.02  ? 155 HIS A NE2   1 
ATOM   1233 N N     . VAL A 1 156 ? 59.571 27.976 -11.587 1.00 49.85  ? 156 VAL A N     1 
ATOM   1234 C CA    . VAL A 1 156 ? 60.119 29.143 -12.269 1.00 48.74  ? 156 VAL A CA    1 
ATOM   1235 C C     . VAL A 1 156 ? 59.368 29.329 -13.582 1.00 53.92  ? 156 VAL A C     1 
ATOM   1236 O O     . VAL A 1 156 ? 58.995 28.352 -14.242 1.00 57.46  ? 156 VAL A O     1 
ATOM   1237 C CB    . VAL A 1 156 ? 61.643 28.997 -12.485 1.00 55.05  ? 156 VAL A CB    1 
ATOM   1238 C CG1   . VAL A 1 156 ? 61.964 27.923 -13.521 1.00 53.01  ? 156 VAL A CG1   1 
ATOM   1239 C CG2   . VAL A 1 156 ? 62.259 30.308 -12.856 1.00 52.32  ? 156 VAL A CG2   1 
ATOM   1240 N N     . SER A 1 157 ? 59.122 30.585 -13.948 1.00 53.96  ? 157 SER A N     1 
ATOM   1241 C CA    . SER A 1 157 ? 58.461 30.875 -15.213 1.00 53.13  ? 157 SER A CA    1 
ATOM   1242 C C     . SER A 1 157 ? 59.421 30.652 -16.378 1.00 56.43  ? 157 SER A C     1 
ATOM   1243 O O     . SER A 1 157 ? 60.645 30.706 -16.226 1.00 55.34  ? 157 SER A O     1 
ATOM   1244 C CB    . SER A 1 157 ? 57.946 32.314 -15.238 1.00 59.82  ? 157 SER A CB    1 
ATOM   1245 O OG    . SER A 1 157 ? 59.021 33.239 -15.215 1.00 55.79  ? 157 SER A OG    1 
ATOM   1246 N N     . ASP A 1 158 ? 58.844 30.408 -17.560 1.00 56.24  ? 158 ASP A N     1 
ATOM   1247 C CA    . ASP A 1 158 ? 59.654 30.262 -18.768 1.00 56.97  ? 158 ASP A CA    1 
ATOM   1248 C C     . ASP A 1 158 ? 60.524 31.486 -19.012 1.00 52.12  ? 158 ASP A C     1 
ATOM   1249 O O     . ASP A 1 158 ? 61.696 31.351 -19.379 1.00 53.68  ? 158 ASP A O     1 
ATOM   1250 C CB    . ASP A 1 158 ? 58.763 30.006 -19.983 1.00 60.83  ? 158 ASP A CB    1 
ATOM   1251 C CG    . ASP A 1 158 ? 58.041 28.686 -19.899 1.00 72.87  ? 158 ASP A CG    1 
ATOM   1252 O OD1   . ASP A 1 158 ? 58.645 27.710 -19.396 1.00 75.40  ? 158 ASP A OD1   1 
ATOM   1253 O OD2   . ASP A 1 158 ? 56.866 28.631 -20.321 1.00 76.72  ? 158 ASP A OD2   1 
ATOM   1254 N N     . GLU A 1 159 ? 59.970 32.689 -18.826 1.00 55.53  ? 159 GLU A N     1 
ATOM   1255 C CA    . GLU A 1 159 ? 60.753 33.897 -19.084 1.00 52.41  ? 159 GLU A CA    1 
ATOM   1256 C C     . GLU A 1 159 ? 61.876 34.058 -18.058 1.00 54.78  ? 159 GLU A C     1 
ATOM   1257 O O     . GLU A 1 159 ? 62.995 34.449 -18.412 1.00 52.56  ? 159 GLU A O     1 
ATOM   1258 C CB    . GLU A 1 159 ? 59.837 35.130 -19.125 1.00 53.77  ? 159 GLU A CB    1 
ATOM   1259 C CG    . GLU A 1 159 ? 58.872 35.131 -20.333 1.00 74.99  ? 159 GLU A CG    1 
ATOM   1260 C CD    . GLU A 1 159 ? 58.244 36.499 -20.659 1.00 81.05  ? 159 GLU A CD    1 
ATOM   1261 O OE1   . GLU A 1 159 ? 58.295 37.425 -19.814 1.00 74.99  ? 159 GLU A OE1   1 
ATOM   1262 O OE2   . GLU A 1 159 ? 57.693 36.640 -21.776 1.00 66.55  ? 159 GLU A OE2   1 
ATOM   1263 N N     . GLU A 1 160 ? 61.618 33.719 -16.790 1.00 53.34  ? 160 GLU A N     1 
ATOM   1264 C CA    . GLU A 1 160 ? 62.680 33.812 -15.789 1.00 50.36  ? 160 GLU A CA    1 
ATOM   1265 C C     . GLU A 1 160 ? 63.764 32.768 -16.042 1.00 49.23  ? 160 GLU A C     1 
ATOM   1266 O O     . GLU A 1 160 ? 64.962 33.060 -15.918 1.00 48.42  ? 160 GLU A O     1 
ATOM   1267 C CB    . GLU A 1 160 ? 62.096 33.669 -14.380 1.00 54.95  ? 160 GLU A CB    1 
ATOM   1268 C CG    . GLU A 1 160 ? 63.145 33.647 -13.250 1.00 49.20  ? 160 GLU A CG    1 
ATOM   1269 C CD    . GLU A 1 160 ? 63.842 34.989 -13.042 1.00 59.71  ? 160 GLU A CD    1 
ATOM   1270 O OE1   . GLU A 1 160 ? 63.285 36.038 -13.458 1.00 55.26  ? 160 GLU A OE1   1 
ATOM   1271 O OE2   . GLU A 1 160 ? 64.953 34.994 -12.460 1.00 54.54  ? 160 GLU A OE2   1 
ATOM   1272 N N     . GLN A 1 161 ? 63.362 31.553 -16.417 1.00 47.24  ? 161 GLN A N     1 
ATOM   1273 C CA    . GLN A 1 161 ? 64.340 30.541 -16.797 1.00 49.47  ? 161 GLN A CA    1 
ATOM   1274 C C     . GLN A 1 161 ? 65.186 31.011 -17.972 1.00 53.40  ? 161 GLN A C     1 
ATOM   1275 O O     . GLN A 1 161 ? 66.403 30.796 -17.986 1.00 46.40  ? 161 GLN A O     1 
ATOM   1276 C CB    . GLN A 1 161 ? 63.640 29.224 -17.141 1.00 49.31  ? 161 GLN A CB    1 
ATOM   1277 C CG    . GLN A 1 161 ? 64.593 28.064 -17.404 1.00 46.80  ? 161 GLN A CG    1 
ATOM   1278 C CD    . GLN A 1 161 ? 63.906 26.869 -18.064 1.00 54.68  ? 161 GLN A CD    1 
ATOM   1279 O OE1   . GLN A 1 161 ? 63.216 27.014 -19.070 1.00 51.52  ? 161 GLN A OE1   1 
ATOM   1280 N NE2   . GLN A 1 161 ? 64.100 25.683 -17.497 1.00 48.42  ? 161 GLN A NE2   1 
ATOM   1281 N N     . LEU A 1 162 ? 64.557 31.640 -18.973 1.00 48.26  ? 162 LEU A N     1 
ATOM   1282 C CA    . LEU A 1 162 ? 65.300 32.139 -20.129 1.00 51.47  ? 162 LEU A CA    1 
ATOM   1283 C C     . LEU A 1 162 ? 66.315 33.198 -19.715 1.00 50.89  ? 162 LEU A C     1 
ATOM   1284 O O     . LEU A 1 162 ? 67.468 33.195 -20.174 1.00 50.49  ? 162 LEU A O     1 
ATOM   1285 C CB    . LEU A 1 162 ? 64.328 32.708 -21.164 1.00 51.97  ? 162 LEU A CB    1 
ATOM   1286 C CG    . LEU A 1 162 ? 64.965 33.383 -22.380 1.00 59.42  ? 162 LEU A CG    1 
ATOM   1287 C CD1   . LEU A 1 162 ? 65.829 32.397 -23.145 1.00 61.25  ? 162 LEU A CD1   1 
ATOM   1288 C CD2   . LEU A 1 162 ? 63.894 33.971 -23.291 1.00 63.19  ? 162 LEU A CD2   1 
ATOM   1289 N N     . LYS A 1 163 ? 65.888 34.132 -18.862 1.00 48.21  ? 163 LYS A N     1 
ATOM   1290 C CA    . LYS A 1 163 ? 66.805 35.131 -18.322 1.00 55.29  ? 163 LYS A CA    1 
ATOM   1291 C C     . LYS A 1 163 ? 68.011 34.463 -17.657 1.00 46.46  ? 163 LYS A C     1 
ATOM   1292 O O     . LYS A 1 163 ? 69.167 34.847 -17.893 1.00 46.27  ? 163 LYS A O     1 
ATOM   1293 C CB    . LYS A 1 163 ? 66.048 36.023 -17.335 1.00 56.72  ? 163 LYS A CB    1 
ATOM   1294 C CG    . LYS A 1 163 ? 66.863 37.129 -16.702 1.00 64.15  ? 163 LYS A CG    1 
ATOM   1295 C CD    . LYS A 1 163 ? 66.024 37.889 -15.684 1.00 56.82  ? 163 LYS A CD    1 
ATOM   1296 C CE    . LYS A 1 163 ? 66.862 38.926 -14.963 1.00 70.49  ? 163 LYS A CE    1 
ATOM   1297 N NZ    . LYS A 1 163 ? 66.468 39.046 -13.531 1.00 83.69  ? 163 LYS A NZ    1 
ATOM   1298 N N     . ARG A 1 164 ? 67.757 33.428 -16.848 1.00 44.55  ? 164 ARG A N     1 
ATOM   1299 C CA    . ARG A 1 164 ? 68.853 32.747 -16.159 1.00 45.00  ? 164 ARG A CA    1 
ATOM   1300 C C     . ARG A 1 164 ? 69.743 31.963 -17.124 1.00 47.47  ? 164 ARG A C     1 
ATOM   1301 O O     . ARG A 1 164 ? 70.959 31.891 -16.915 1.00 49.00  ? 164 ARG A O     1 
ATOM   1302 C CB    . ARG A 1 164 ? 68.299 31.835 -15.061 1.00 45.54  ? 164 ARG A CB    1 
ATOM   1303 C CG    . ARG A 1 164 ? 67.520 32.600 -13.986 1.00 49.04  ? 164 ARG A CG    1 
ATOM   1304 C CD    . ARG A 1 164 ? 66.936 31.692 -12.884 1.00 43.98  ? 164 ARG A CD    1 
ATOM   1305 N NE    . ARG A 1 164 ? 66.084 32.475 -11.998 1.00 49.07  ? 164 ARG A NE    1 
ATOM   1306 C CZ    . ARG A 1 164 ? 65.524 32.035 -10.879 1.00 48.29  ? 164 ARG A CZ    1 
ATOM   1307 N NH1   . ARG A 1 164 ? 65.704 30.794 -10.450 1.00 45.15  ? 164 ARG A NH1   1 
ATOM   1308 N NH2   . ARG A 1 164 ? 64.769 32.866 -10.168 1.00 48.98  ? 164 ARG A NH2   1 
ATOM   1309 N N     . PHE A 1 165 ? 69.169 31.383 -18.182 1.00 46.88  ? 165 PHE A N     1 
ATOM   1310 C CA    . PHE A 1 165 ? 69.984 30.723 -19.200 1.00 46.76  ? 165 PHE A CA    1 
ATOM   1311 C C     . PHE A 1 165 ? 70.927 31.719 -19.870 1.00 49.57  ? 165 PHE A C     1 
ATOM   1312 O O     . PHE A 1 165 ? 72.094 31.403 -20.129 1.00 47.82  ? 165 PHE A O     1 
ATOM   1313 C CB    . PHE A 1 165 ? 69.101 30.058 -20.261 1.00 47.44  ? 165 PHE A CB    1 
ATOM   1314 C CG    . PHE A 1 165 ? 68.671 28.638 -19.937 1.00 48.62  ? 165 PHE A CG    1 
ATOM   1315 C CD1   . PHE A 1 165 ? 68.478 28.217 -18.625 1.00 46.13  ? 165 PHE A CD1   1 
ATOM   1316 C CD2   . PHE A 1 165 ? 68.447 27.726 -20.968 1.00 48.87  ? 165 PHE A CD2   1 
ATOM   1317 C CE1   . PHE A 1 165 ? 68.065 26.918 -18.357 1.00 46.24  ? 165 PHE A CE1   1 
ATOM   1318 C CE2   . PHE A 1 165 ? 68.042 26.427 -20.709 1.00 51.57  ? 165 PHE A CE2   1 
ATOM   1319 C CZ    . PHE A 1 165 ? 67.849 26.019 -19.399 1.00 46.62  ? 165 PHE A CZ    1 
ATOM   1320 N N     . LYS A 1 166 ? 70.434 32.924 -20.169 1.00 50.12  ? 166 LYS A N     1 
ATOM   1321 C CA    . LYS A 1 166 ? 71.284 33.915 -20.827 1.00 48.42  ? 166 LYS A CA    1 
ATOM   1322 C C     . LYS A 1 166 ? 72.378 34.416 -19.887 1.00 52.60  ? 166 LYS A C     1 
ATOM   1323 O O     . LYS A 1 166 ? 73.535 34.603 -20.306 1.00 52.79  ? 166 LYS A O     1 
ATOM   1324 C CB    . LYS A 1 166 ? 70.429 35.065 -21.369 1.00 53.62  ? 166 LYS A CB    1 
ATOM   1325 C CG    . LYS A 1 166 ? 69.606 34.647 -22.597 1.00 55.40  ? 166 LYS A CG    1 
ATOM   1326 C CD    . LYS A 1 166 ? 69.158 35.824 -23.452 1.00 71.26  ? 166 LYS A CD    1 
ATOM   1327 C CE    . LYS A 1 166 ? 68.469 35.342 -24.733 1.00 71.07  ? 166 LYS A CE    1 
ATOM   1328 N NZ    . LYS A 1 166 ? 68.153 36.466 -25.677 1.00 93.79  ? 166 LYS A NZ    1 
ATOM   1329 N N     . GLU A 1 167 ? 72.042 34.603 -18.605 1.00 46.73  ? 167 GLU A N     1 
ATOM   1330 C CA    . GLU A 1 167 ? 73.068 34.914 -17.611 1.00 51.80  ? 167 GLU A CA    1 
ATOM   1331 C C     . GLU A 1 167 ? 74.134 33.826 -17.557 1.00 49.40  ? 167 GLU A C     1 
ATOM   1332 O O     . GLU A 1 167 ? 75.333 34.121 -17.589 1.00 54.19  ? 167 GLU A O     1 
ATOM   1333 C CB    . GLU A 1 167 ? 72.435 35.109 -16.234 1.00 51.73  ? 167 GLU A CB    1 
ATOM   1334 C CG    . GLU A 1 167 ? 71.698 36.427 -16.122 1.00 60.43  ? 167 GLU A CG    1 
ATOM   1335 C CD    . GLU A 1 167 ? 70.769 36.494 -14.925 1.00 75.88  ? 167 GLU A CD    1 
ATOM   1336 O OE1   . GLU A 1 167 ? 70.690 35.503 -14.162 1.00 68.32  ? 167 GLU A OE1   1 
ATOM   1337 O OE2   . GLU A 1 167 ? 70.115 37.549 -14.756 1.00 80.02  ? 167 GLU A OE2   1 
ATOM   1338 N N     . ARG A 1 168 ? 73.712 32.558 -17.484 1.00 51.54  ? 168 ARG A N     1 
ATOM   1339 C CA    . ARG A 1 168 ? 74.658 31.444 -17.476 1.00 48.35  ? 168 ARG A CA    1 
ATOM   1340 C C     . ARG A 1 168 ? 75.557 31.468 -18.702 1.00 51.82  ? 168 ARG A C     1 
ATOM   1341 O O     . ARG A 1 168 ? 76.780 31.325 -18.592 1.00 51.07  ? 168 ARG A O     1 
ATOM   1342 C CB    . ARG A 1 168 ? 73.914 30.110 -17.404 1.00 48.97  ? 168 ARG A CB    1 
ATOM   1343 C CG    . ARG A 1 168 ? 73.409 29.787 -16.024 1.00 44.81  ? 168 ARG A CG    1 
ATOM   1344 C CD    . ARG A 1 168 ? 72.711 28.442 -15.973 1.00 43.25  ? 168 ARG A CD    1 
ATOM   1345 N NE    . ARG A 1 168 ? 72.173 28.204 -14.640 1.00 55.14  ? 168 ARG A NE    1 
ATOM   1346 C CZ    . ARG A 1 168 ? 71.631 27.061 -14.244 1.00 61.67  ? 168 ARG A CZ    1 
ATOM   1347 N NH1   . ARG A 1 168 ? 71.501 26.034 -15.071 1.00 53.50  ? 168 ARG A NH1   1 
ATOM   1348 N NH2   . ARG A 1 168 ? 71.215 26.945 -12.985 1.00 52.31  ? 168 ARG A NH2   1 
ATOM   1349 N N     . GLU A 1 169 ? 74.968 31.638 -19.886 1.00 50.20  ? 169 GLU A N     1 
ATOM   1350 C CA    . GLU A 1 169 ? 75.783 31.629 -21.091 1.00 50.44  ? 169 GLU A CA    1 
ATOM   1351 C C     . GLU A 1 169 ? 76.768 32.790 -21.102 1.00 54.13  ? 169 GLU A C     1 
ATOM   1352 O O     . GLU A 1 169 ? 77.792 32.707 -21.786 1.00 54.88  ? 169 GLU A O     1 
ATOM   1353 C CB    . GLU A 1 169 ? 74.896 31.631 -22.347 1.00 52.43  ? 169 GLU A CB    1 
ATOM   1354 C CG    . GLU A 1 169 ? 74.453 32.995 -22.800 1.00 68.45  ? 169 GLU A CG    1 
ATOM   1355 C CD    . GLU A 1 169 ? 73.748 32.976 -24.147 1.00 70.12  ? 169 GLU A CD    1 
ATOM   1356 O OE1   . GLU A 1 169 ? 73.623 31.886 -24.750 1.00 66.17  ? 169 GLU A OE1   1 
ATOM   1357 O OE2   . GLU A 1 169 ? 73.321 34.063 -24.594 1.00 67.94  ? 169 GLU A OE2   1 
ATOM   1358 N N     . GLN A 1 170 ? 76.507 33.855 -20.335 1.00 54.28  ? 170 GLN A N     1 
ATOM   1359 C CA    . GLN A 1 170 ? 77.491 34.926 -20.199 1.00 55.40  ? 170 GLN A CA    1 
ATOM   1360 C C     . GLN A 1 170 ? 78.404 34.763 -18.989 1.00 59.01  ? 170 GLN A C     1 
ATOM   1361 O O     . GLN A 1 170 ? 79.278 35.609 -18.777 1.00 60.23  ? 170 GLN A O     1 
ATOM   1362 C CB    . GLN A 1 170 ? 76.795 36.289 -20.121 1.00 57.35  ? 170 GLN A CB    1 
ATOM   1363 C CG    . GLN A 1 170 ? 76.070 36.662 -21.399 1.00 62.02  ? 170 GLN A CG    1 
ATOM   1364 C CD    . GLN A 1 170 ? 76.999 36.704 -22.601 1.00 76.90  ? 170 GLN A CD    1 
ATOM   1365 O OE1   . GLN A 1 170 ? 76.744 36.058 -23.622 1.00 82.78  ? 170 GLN A OE1   1 
ATOM   1366 N NE2   . GLN A 1 170 ? 78.082 37.472 -22.488 1.00 80.44  ? 170 GLN A NE2   1 
ATOM   1367 N N     . ASN A 1 171 ? 78.224 33.708 -18.194 1.00 52.83  ? 171 ASN A N     1 
ATOM   1368 C CA    . ASN A 1 171 ? 78.957 33.551 -16.946 1.00 47.35  ? 171 ASN A CA    1 
ATOM   1369 C C     . ASN A 1 171 ? 80.121 32.593 -17.145 1.00 47.52  ? 171 ASN A C     1 
ATOM   1370 O O     . ASN A 1 171 ? 79.900 31.396 -17.383 1.00 48.81  ? 171 ASN A O     1 
ATOM   1371 C CB    . ASN A 1 171 ? 78.034 33.043 -15.845 1.00 48.05  ? 171 ASN A CB    1 
ATOM   1372 C CG    . ASN A 1 171 ? 78.713 32.990 -14.480 1.00 56.89  ? 171 ASN A CG    1 
ATOM   1373 O OD1   . ASN A 1 171 ? 79.911 32.733 -14.375 1.00 55.77  ? 171 ASN A OD1   1 
ATOM   1374 N ND2   . ASN A 1 171 ? 77.939 33.228 -13.425 1.00 52.50  ? 171 ASN A ND2   1 
ATOM   1375 N N     . PRO A 1 172 ? 81.362 33.063 -17.023 1.00 50.39  ? 172 PRO A N     1 
ATOM   1376 C CA    . PRO A 1 172 ? 82.521 32.184 -17.266 1.00 46.70  ? 172 PRO A CA    1 
ATOM   1377 C C     . PRO A 1 172 ? 82.594 30.965 -16.360 1.00 49.68  ? 172 PRO A C     1 
ATOM   1378 O O     . PRO A 1 172 ? 83.255 29.985 -16.725 1.00 49.22  ? 172 PRO A O     1 
ATOM   1379 C CB    . PRO A 1 172 ? 83.718 33.115 -17.039 1.00 48.10  ? 172 PRO A CB    1 
ATOM   1380 C CG    . PRO A 1 172 ? 83.152 34.330 -16.347 1.00 57.54  ? 172 PRO A CG    1 
ATOM   1381 C CD    . PRO A 1 172 ? 81.751 34.460 -16.788 1.00 54.65  ? 172 PRO A CD    1 
ATOM   1382 N N     . TYR A 1 173 ? 81.954 30.981 -15.192 1.00 42.71  ? 173 TYR A N     1 
ATOM   1383 C CA    . TYR A 1 173 ? 81.949 29.780 -14.363 1.00 50.91  ? 173 TYR A CA    1 
ATOM   1384 C C     . TYR A 1 173 ? 80.868 28.778 -14.757 1.00 52.85  ? 173 TYR A C     1 
ATOM   1385 O O     . TYR A 1 173 ? 80.885 27.653 -14.251 1.00 43.27  ? 173 TYR A O     1 
ATOM   1386 C CB    . TYR A 1 173 ? 81.770 30.141 -12.888 1.00 44.45  ? 173 TYR A CB    1 
ATOM   1387 C CG    . TYR A 1 173 ? 82.853 31.045 -12.339 1.00 49.81  ? 173 TYR A CG    1 
ATOM   1388 C CD1   . TYR A 1 173 ? 84.150 30.575 -12.137 1.00 46.04  ? 173 TYR A CD1   1 
ATOM   1389 C CD2   . TYR A 1 173 ? 82.577 32.367 -12.016 1.00 52.28  ? 173 TYR A CD2   1 
ATOM   1390 C CE1   . TYR A 1 173 ? 85.141 31.406 -11.631 1.00 48.91  ? 173 TYR A CE1   1 
ATOM   1391 C CE2   . TYR A 1 173 ? 83.561 33.206 -11.509 1.00 48.85  ? 173 TYR A CE2   1 
ATOM   1392 C CZ    . TYR A 1 173 ? 84.838 32.720 -11.317 1.00 47.99  ? 173 TYR A CZ    1 
ATOM   1393 O OH    . TYR A 1 173 ? 85.810 33.557 -10.817 1.00 50.94  ? 173 TYR A OH    1 
ATOM   1394 N N     . LYS A 1 174 ? 79.942 29.147 -15.643 1.00 46.43  ? 174 LYS A N     1 
ATOM   1395 C CA    . LYS A 1 174 ? 78.775 28.318 -15.924 1.00 55.41  ? 174 LYS A CA    1 
ATOM   1396 C C     . LYS A 1 174 ? 78.526 28.056 -17.400 1.00 54.11  ? 174 LYS A C     1 
ATOM   1397 O O     . LYS A 1 174 ? 77.814 27.093 -17.718 1.00 51.51  ? 174 LYS A O     1 
ATOM   1398 C CB    . LYS A 1 174 ? 77.511 28.957 -15.331 1.00 48.86  ? 174 LYS A CB    1 
ATOM   1399 C CG    . LYS A 1 174 ? 77.563 29.162 -13.827 1.00 53.28  ? 174 LYS A CG    1 
ATOM   1400 C CD    . LYS A 1 174 ? 76.568 30.225 -13.380 1.00 67.94  ? 174 LYS A CD    1 
ATOM   1401 C CE    . LYS A 1 174 ? 76.468 30.290 -11.858 1.00 74.65  ? 174 LYS A CE    1 
ATOM   1402 N NZ    . LYS A 1 174 ? 75.472 31.307 -11.407 1.00 73.88  ? 174 LYS A NZ    1 
ATOM   1403 N N     . SER A 1 175 ? 79.088 28.863 -18.306 1.00 46.12  ? 175 SER A N     1 
ATOM   1404 C CA    . SER A 1 175 ? 78.756 28.773 -19.725 1.00 58.64  ? 175 SER A CA    1 
ATOM   1405 C C     . SER A 1 175 ? 79.212 27.456 -20.339 1.00 60.92  ? 175 SER A C     1 
ATOM   1406 O O     . SER A 1 175 ? 78.562 26.951 -21.262 1.00 58.10  ? 175 SER A O     1 
ATOM   1407 C CB    . SER A 1 175 ? 79.388 29.940 -20.477 1.00 50.58  ? 175 SER A CB    1 
ATOM   1408 O OG    . SER A 1 175 ? 80.796 29.814 -20.470 1.00 56.81  ? 175 SER A OG    1 
ATOM   1409 N N     . TRP A 1 176 ? 80.318 26.894 -19.844 1.00 56.80  ? 176 TRP A N     1 
ATOM   1410 C CA    . TRP A 1 176 ? 80.820 25.612 -20.328 1.00 58.38  ? 176 TRP A CA    1 
ATOM   1411 C C     . TRP A 1 176 ? 79.792 24.490 -20.186 1.00 54.91  ? 176 TRP A C     1 
ATOM   1412 O O     . TRP A 1 176 ? 79.862 23.505 -20.926 1.00 59.80  ? 176 TRP A O     1 
ATOM   1413 C CB    . TRP A 1 176 ? 82.090 25.240 -19.560 1.00 52.16  ? 176 TRP A CB    1 
ATOM   1414 C CG    . TRP A 1 176 ? 81.783 24.977 -18.123 1.00 51.43  ? 176 TRP A CG    1 
ATOM   1415 C CD1   . TRP A 1 176 ? 81.641 25.905 -17.131 1.00 52.04  ? 176 TRP A CD1   1 
ATOM   1416 C CD2   . TRP A 1 176 ? 81.537 23.703 -17.519 1.00 50.24  ? 176 TRP A CD2   1 
ATOM   1417 N NE1   . TRP A 1 176 ? 81.331 25.284 -15.940 1.00 51.83  ? 176 TRP A NE1   1 
ATOM   1418 C CE2   . TRP A 1 176 ? 81.263 23.932 -16.154 1.00 53.32  ? 176 TRP A CE2   1 
ATOM   1419 C CE3   . TRP A 1 176 ? 81.524 22.389 -18.000 1.00 54.87  ? 176 TRP A CE3   1 
ATOM   1420 C CZ2   . TRP A 1 176 ? 80.980 22.897 -15.265 1.00 52.83  ? 176 TRP A CZ2   1 
ATOM   1421 C CZ3   . TRP A 1 176 ? 81.246 21.362 -17.114 1.00 53.95  ? 176 TRP A CZ3   1 
ATOM   1422 C CH2   . TRP A 1 176 ? 80.975 21.623 -15.762 1.00 56.30  ? 176 TRP A CH2   1 
ATOM   1423 N N     . LYS A 1 177 ? 78.847 24.613 -19.252 1.00 56.36  ? 177 LYS A N     1 
ATOM   1424 C CA    . LYS A 1 177 ? 77.882 23.557 -18.958 1.00 58.15  ? 177 LYS A CA    1 
ATOM   1425 C C     . LYS A 1 177 ? 76.564 23.707 -19.714 1.00 60.96  ? 177 LYS A C     1 
ATOM   1426 O O     . LYS A 1 177 ? 75.820 22.729 -19.834 1.00 70.27  ? 177 LYS A O     1 
ATOM   1427 C CB    . LYS A 1 177 ? 77.597 23.518 -17.449 1.00 53.38  ? 177 LYS A CB    1 
ATOM   1428 C CG    . LYS A 1 177 ? 76.873 22.274 -16.959 1.00 63.52  ? 177 LYS A CG    1 
ATOM   1429 C CD    . LYS A 1 177 ? 76.690 22.272 -15.438 1.00 69.12  ? 177 LYS A CD    1 
ATOM   1430 C CE    . LYS A 1 177 ? 75.804 21.103 -15.007 1.00 79.14  ? 177 LYS A CE    1 
ATOM   1431 N NZ    . LYS A 1 177 ? 75.519 21.064 -13.544 1.00 70.47  ? 177 LYS A NZ    1 
ATOM   1432 N N     . LEU A 1 178 ? 76.257 24.895 -20.222 1.00 62.97  ? 178 LEU A N     1 
ATOM   1433 C CA    . LEU A 1 178 ? 75.001 25.127 -20.921 1.00 61.90  ? 178 LEU A CA    1 
ATOM   1434 C C     . LEU A 1 178 ? 75.150 24.704 -22.378 1.00 62.83  ? 178 LEU A C     1 
ATOM   1435 O O     . LEU A 1 178 ? 75.954 25.282 -23.115 1.00 62.74  ? 178 LEU A O     1 
ATOM   1436 C CB    . LEU A 1 178 ? 74.611 26.597 -20.813 1.00 60.62  ? 178 LEU A CB    1 
ATOM   1437 C CG    . LEU A 1 178 ? 73.304 27.007 -21.479 1.00 65.50  ? 178 LEU A CG    1 
ATOM   1438 C CD1   . LEU A 1 178 ? 72.147 26.244 -20.864 1.00 55.90  ? 178 LEU A CD1   1 
ATOM   1439 C CD2   . LEU A 1 178 ? 73.112 28.503 -21.332 1.00 62.01  ? 178 LEU A CD2   1 
ATOM   1440 N N     . THR A 1 179 ? 74.382 23.701 -22.791 1.00 62.82  ? 179 THR A N     1 
ATOM   1441 C CA    . THR A 1 179 ? 74.498 23.113 -24.119 1.00 71.61  ? 179 THR A CA    1 
ATOM   1442 C C     . THR A 1 179 ? 73.270 23.434 -24.962 1.00 71.34  ? 179 THR A C     1 
ATOM   1443 O O     . THR A 1 179 ? 72.221 23.828 -24.448 1.00 70.49  ? 179 THR A O     1 
ATOM   1444 C CB    . THR A 1 179 ? 74.656 21.594 -24.032 1.00 69.12  ? 179 THR A CB    1 
ATOM   1445 O OG1   . THR A 1 179 ? 73.406 21.016 -23.635 1.00 69.77  ? 179 THR A OG1   1 
ATOM   1446 C CG2   . THR A 1 179 ? 75.717 21.227 -23.009 1.00 72.69  ? 179 THR A CG2   1 
ATOM   1447 N N     . ASP A 1 180 ? 73.406 23.233 -26.277 1.00 75.31  ? 180 ASP A N     1 
ATOM   1448 C CA    . ASP A 1 180 ? 72.256 23.395 -27.162 1.00 73.65  ? 180 ASP A CA    1 
ATOM   1449 C C     . ASP A 1 180 ? 71.106 22.485 -26.752 1.00 76.38  ? 180 ASP A C     1 
ATOM   1450 O O     . ASP A 1 180 ? 69.932 22.852 -26.907 1.00 78.35  ? 180 ASP A O     1 
ATOM   1451 C CB    . ASP A 1 180 ? 72.659 23.116 -28.608 1.00 86.85  ? 180 ASP A CB    1 
ATOM   1452 C CG    . ASP A 1 180 ? 73.618 24.152 -29.150 1.00 94.64  ? 180 ASP A CG    1 
ATOM   1453 O OD1   . ASP A 1 180 ? 73.347 25.362 -28.981 1.00 91.96  ? 180 ASP A OD1   1 
ATOM   1454 O OD2   . ASP A 1 180 ? 74.647 23.755 -29.739 1.00 100.69 ? 180 ASP A OD2   1 
ATOM   1455 N N     . GLU A 1 181 ? 71.425 21.311 -26.202 1.00 74.72  ? 181 GLU A N     1 
ATOM   1456 C CA    . GLU A 1 181 ? 70.381 20.385 -25.787 1.00 76.63  ? 181 GLU A CA    1 
ATOM   1457 C C     . GLU A 1 181 ? 69.521 20.973 -24.672 1.00 75.31  ? 181 GLU A C     1 
ATOM   1458 O O     . GLU A 1 181 ? 68.313 20.733 -24.634 1.00 75.03  ? 181 GLU A O     1 
ATOM   1459 C CB    . GLU A 1 181 ? 71.002 19.057 -25.355 1.00 78.36  ? 181 GLU A CB    1 
ATOM   1460 C CG    . GLU A 1 181 ? 69.976 17.981 -25.026 1.00 93.80  ? 181 GLU A CG    1 
ATOM   1461 C CD    . GLU A 1 181 ? 70.612 16.672 -24.593 1.00 103.88 ? 181 GLU A CD    1 
ATOM   1462 O OE1   . GLU A 1 181 ? 71.811 16.468 -24.884 1.00 108.22 ? 181 GLU A OE1   1 
ATOM   1463 O OE2   . GLU A 1 181 ? 69.915 15.849 -23.958 1.00 98.25  ? 181 GLU A OE2   1 
ATOM   1464 N N     . ASP A 1 182 ? 70.116 21.753 -23.761 1.00 70.59  ? 182 ASP A N     1 
ATOM   1465 C CA    . ASP A 1 182 ? 69.336 22.359 -22.678 1.00 61.68  ? 182 ASP A CA    1 
ATOM   1466 C C     . ASP A 1 182 ? 68.334 23.372 -23.226 1.00 65.18  ? 182 ASP A C     1 
ATOM   1467 O O     . ASP A 1 182 ? 67.152 23.391 -22.834 1.00 67.56  ? 182 ASP A O     1 
ATOM   1468 C CB    . ASP A 1 182 ? 70.279 23.021 -21.671 1.00 61.16  ? 182 ASP A CB    1 
ATOM   1469 C CG    . ASP A 1 182 ? 71.324 22.058 -21.129 1.00 65.10  ? 182 ASP A CG    1 
ATOM   1470 O OD1   . ASP A 1 182 ? 70.948 20.941 -20.715 1.00 64.04  ? 182 ASP A OD1   1 
ATOM   1471 O OD2   . ASP A 1 182 ? 72.523 22.408 -21.132 1.00 67.81  ? 182 ASP A OD2   1 
ATOM   1472 N N     . TRP A 1 183 ? 68.800 24.225 -24.145 1.00 67.18  ? 183 TRP A N     1 
ATOM   1473 C CA    . TRP A 1 183 ? 67.912 25.141 -24.851 1.00 69.67  ? 183 TRP A CA    1 
ATOM   1474 C C     . TRP A 1 183 ? 66.762 24.390 -25.506 1.00 69.72  ? 183 TRP A C     1 
ATOM   1475 O O     . TRP A 1 183 ? 65.597 24.782 -25.378 1.00 67.83  ? 183 TRP A O     1 
ATOM   1476 C CB    . TRP A 1 183 ? 68.692 25.924 -25.905 1.00 65.56  ? 183 TRP A CB    1 
ATOM   1477 C CG    . TRP A 1 183 ? 69.676 26.901 -25.363 1.00 67.08  ? 183 TRP A CG    1 
ATOM   1478 C CD1   . TRP A 1 183 ? 71.027 26.738 -25.264 1.00 70.20  ? 183 TRP A CD1   1 
ATOM   1479 C CD2   . TRP A 1 183 ? 69.392 28.211 -24.865 1.00 64.16  ? 183 TRP A CD2   1 
ATOM   1480 N NE1   . TRP A 1 183 ? 71.604 27.866 -24.731 1.00 72.41  ? 183 TRP A NE1   1 
ATOM   1481 C CE2   . TRP A 1 183 ? 70.620 28.785 -24.475 1.00 68.13  ? 183 TRP A CE2   1 
ATOM   1482 C CE3   . TRP A 1 183 ? 68.219 28.953 -24.706 1.00 63.18  ? 183 TRP A CE3   1 
ATOM   1483 C CZ2   . TRP A 1 183 ? 70.707 30.067 -23.934 1.00 62.79  ? 183 TRP A CZ2   1 
ATOM   1484 C CZ3   . TRP A 1 183 ? 68.307 30.229 -24.172 1.00 62.72  ? 183 TRP A CZ3   1 
ATOM   1485 C CH2   . TRP A 1 183 ? 69.541 30.773 -23.793 1.00 58.02  ? 183 TRP A CH2   1 
ATOM   1486 N N     . ARG A 1 184 ? 67.072 23.299 -26.215 1.00 72.44  ? 184 ARG A N     1 
ATOM   1487 C CA    . ARG A 1 184 ? 66.018 22.554 -26.901 1.00 74.81  ? 184 ARG A CA    1 
ATOM   1488 C C     . ARG A 1 184 ? 65.052 21.914 -25.909 1.00 71.64  ? 184 ARG A C     1 
ATOM   1489 O O     . ARG A 1 184 ? 63.839 21.877 -26.154 1.00 71.73  ? 184 ARG A O     1 
ATOM   1490 C CB    . ARG A 1 184 ? 66.623 21.490 -27.818 1.00 80.21  ? 184 ARG A CB    1 
ATOM   1491 C CG    . ARG A 1 184 ? 67.428 22.031 -28.991 1.00 90.22  ? 184 ARG A CG    1 
ATOM   1492 C CD    . ARG A 1 184 ? 67.744 20.923 -29.996 1.00 96.42  ? 184 ARG A CD    1 
ATOM   1493 N NE    . ARG A 1 184 ? 68.211 19.708 -29.334 1.00 106.44 ? 184 ARG A NE    1 
ATOM   1494 C CZ    . ARG A 1 184 ? 69.478 19.318 -29.278 1.00 103.04 ? 184 ARG A CZ    1 
ATOM   1495 N NH1   . ARG A 1 184 ? 70.440 20.006 -29.873 1.00 94.79  ? 184 ARG A NH1   1 
ATOM   1496 N NH2   . ARG A 1 184 ? 69.787 18.211 -28.605 1.00 96.29  ? 184 ARG A NH2   1 
ATOM   1497 N N     . ASN A 1 185 ? 65.572 21.410 -24.784 1.00 70.23  ? 185 ASN A N     1 
ATOM   1498 C CA    . ASN A 1 185 ? 64.743 20.817 -23.738 1.00 70.88  ? 185 ASN A CA    1 
ATOM   1499 C C     . ASN A 1 185 ? 63.778 21.817 -23.134 1.00 72.05  ? 185 ASN A C     1 
ATOM   1500 O O     . ASN A 1 185 ? 62.777 21.410 -22.532 1.00 65.40  ? 185 ASN A O     1 
ATOM   1501 C CB    . ASN A 1 185 ? 65.614 20.238 -22.624 1.00 64.06  ? 185 ASN A CB    1 
ATOM   1502 C CG    . ASN A 1 185 ? 66.138 18.863 -22.953 1.00 76.92  ? 185 ASN A CG    1 
ATOM   1503 O OD1   . ASN A 1 185 ? 65.898 18.337 -24.042 1.00 83.14  ? 185 ASN A OD1   1 
ATOM   1504 N ND2   . ASN A 1 185 ? 66.869 18.270 -22.015 1.00 73.96  ? 185 ASN A ND2   1 
ATOM   1505 N N     . ARG A 1 186 ? 64.075 23.113 -23.239 1.00 68.08  ? 186 ARG A N     1 
ATOM   1506 C CA    . ARG A 1 186 ? 63.073 24.096 -22.825 1.00 62.56  ? 186 ARG A CA    1 
ATOM   1507 C C     . ARG A 1 186 ? 61.725 23.878 -23.520 1.00 65.49  ? 186 ARG A C     1 
ATOM   1508 O O     . ARG A 1 186 ? 60.674 24.190 -22.947 1.00 58.43  ? 186 ARG A O     1 
ATOM   1509 C CB    . ARG A 1 186 ? 63.575 25.514 -23.080 1.00 58.60  ? 186 ARG A CB    1 
ATOM   1510 C CG    . ARG A 1 186 ? 64.515 26.020 -22.015 1.00 59.72  ? 186 ARG A CG    1 
ATOM   1511 C CD    . ARG A 1 186 ? 65.017 27.403 -22.361 1.00 56.73  ? 186 ARG A CD    1 
ATOM   1512 N NE    . ARG A 1 186 ? 63.940 28.284 -22.804 1.00 74.58  ? 186 ARG A NE    1 
ATOM   1513 C CZ    . ARG A 1 186 ? 63.107 28.907 -21.983 1.00 65.26  ? 186 ARG A CZ    1 
ATOM   1514 N NH1   . ARG A 1 186 ? 63.181 28.745 -20.675 1.00 67.37  ? 186 ARG A NH1   1 
ATOM   1515 N NH2   . ARG A 1 186 ? 62.181 29.711 -22.487 1.00 57.32  ? 186 ARG A NH2   1 
ATOM   1516 N N     . GLU A 1 187 ? 61.729 23.328 -24.739 1.00 61.67  ? 187 GLU A N     1 
ATOM   1517 C CA    . GLU A 1 187 ? 60.483 23.069 -25.457 1.00 65.60  ? 187 GLU A CA    1 
ATOM   1518 C C     . GLU A 1 187 ? 59.633 21.987 -24.802 1.00 68.67  ? 187 GLU A C     1 
ATOM   1519 O O     . GLU A 1 187 ? 58.436 21.898 -25.094 1.00 64.65  ? 187 GLU A O     1 
ATOM   1520 C CB    . GLU A 1 187 ? 60.778 22.661 -26.896 1.00 58.43  ? 187 GLU A CB    1 
ATOM   1521 C CG    . GLU A 1 187 ? 59.576 22.785 -27.818 1.00 90.76  ? 187 GLU A CG    1 
ATOM   1522 C CD    . GLU A 1 187 ? 59.773 22.070 -29.139 1.00 103.99 ? 187 GLU A CD    1 
ATOM   1523 O OE1   . GLU A 1 187 ? 60.900 21.585 -29.384 1.00 107.05 ? 187 GLU A OE1   1 
ATOM   1524 O OE2   . GLU A 1 187 ? 58.801 21.989 -29.927 1.00 102.83 ? 187 GLU A OE2   1 
ATOM   1525 N N     . LYS A 1 188 ? 60.219 21.163 -23.939 1.00 62.45  ? 188 LYS A N     1 
ATOM   1526 C CA    . LYS A 1 188 ? 59.504 20.092 -23.264 1.00 64.36  ? 188 LYS A CA    1 
ATOM   1527 C C     . LYS A 1 188 ? 58.867 20.535 -21.954 1.00 63.45  ? 188 LYS A C     1 
ATOM   1528 O O     . LYS A 1 188 ? 58.285 19.700 -21.253 1.00 59.56  ? 188 LYS A O     1 
ATOM   1529 C CB    . LYS A 1 188 ? 60.456 18.915 -23.000 1.00 63.61  ? 188 LYS A CB    1 
ATOM   1530 C CG    . LYS A 1 188 ? 60.943 18.220 -24.266 1.00 72.10  ? 188 LYS A CG    1 
ATOM   1531 C CD    . LYS A 1 188 ? 62.172 17.354 -24.014 1.00 68.94  ? 188 LYS A CD    1 
ATOM   1532 C CE    . LYS A 1 188 ? 62.622 16.640 -25.288 1.00 77.38  ? 188 LYS A CE    1 
ATOM   1533 N NZ    . LYS A 1 188 ? 63.945 15.967 -25.117 1.00 80.96  ? 188 LYS A NZ    1 
ATOM   1534 N N     . SER A 1 189 ? 58.962 21.818 -21.606 1.00 62.12  ? 189 SER A N     1 
ATOM   1535 C CA    . SER A 1 189 ? 58.462 22.276 -20.311 1.00 57.31  ? 189 SER A CA    1 
ATOM   1536 C C     . SER A 1 189 ? 56.987 21.968 -20.058 1.00 60.61  ? 189 SER A C     1 
ATOM   1537 O O     . SER A 1 189 ? 56.662 21.581 -18.922 1.00 55.27  ? 189 SER A O     1 
ATOM   1538 C CB    . SER A 1 189 ? 58.733 23.778 -20.158 1.00 61.43  ? 189 SER A CB    1 
ATOM   1539 O OG    . SER A 1 189 ? 60.124 24.037 -20.071 1.00 61.49  ? 189 SER A OG    1 
ATOM   1540 N N     . PRO A 1 190 ? 56.056 22.126 -21.017 1.00 61.15  ? 190 PRO A N     1 
ATOM   1541 C CA    . PRO A 1 190 ? 54.655 21.749 -20.733 1.00 56.18  ? 190 PRO A CA    1 
ATOM   1542 C C     . PRO A 1 190 ? 54.497 20.317 -20.239 1.00 55.18  ? 190 PRO A C     1 
ATOM   1543 O O     . PRO A 1 190 ? 53.743 20.063 -19.286 1.00 61.32  ? 190 PRO A O     1 
ATOM   1544 C CB    . PRO A 1 190 ? 53.957 21.964 -22.085 1.00 62.47  ? 190 PRO A CB    1 
ATOM   1545 C CG    . PRO A 1 190 ? 54.784 23.008 -22.777 1.00 62.66  ? 190 PRO A CG    1 
ATOM   1546 C CD    . PRO A 1 190 ? 56.201 22.750 -22.349 1.00 53.13  ? 190 PRO A CD    1 
ATOM   1547 N N     . GLN A 1 191 ? 55.206 19.374 -20.861 1.00 56.04  ? 191 GLN A N     1 
ATOM   1548 C CA    . GLN A 1 191 ? 55.147 17.984 -20.421 1.00 59.33  ? 191 GLN A CA    1 
ATOM   1549 C C     . GLN A 1 191 ? 55.693 17.816 -19.008 1.00 52.75  ? 191 GLN A C     1 
ATOM   1550 O O     . GLN A 1 191 ? 55.130 17.057 -18.210 1.00 52.07  ? 191 GLN A O     1 
ATOM   1551 C CB    . GLN A 1 191 ? 55.915 17.107 -21.397 1.00 55.76  ? 191 GLN A CB    1 
ATOM   1552 C CG    . GLN A 1 191 ? 55.486 17.305 -22.818 1.00 70.36  ? 191 GLN A CG    1 
ATOM   1553 C CD    . GLN A 1 191 ? 56.575 16.936 -23.783 1.00 80.67  ? 191 GLN A CD    1 
ATOM   1554 O OE1   . GLN A 1 191 ? 57.118 15.829 -23.732 1.00 77.10  ? 191 GLN A OE1   1 
ATOM   1555 N NE2   . GLN A 1 191 ? 56.922 17.868 -24.663 1.00 74.11  ? 191 GLN A NE2   1 
ATOM   1556 N N     . TYR A 1 192 ? 56.796 18.504 -18.684 1.00 57.89  ? 192 TYR A N     1 
ATOM   1557 C CA    . TYR A 1 192 ? 57.336 18.437 -17.326 1.00 52.51  ? 192 TYR A CA    1 
ATOM   1558 C C     . TYR A 1 192 ? 56.350 18.989 -16.315 1.00 53.63  ? 192 TYR A C     1 
ATOM   1559 O O     . TYR A 1 192 ? 56.225 18.457 -15.211 1.00 50.13  ? 192 TYR A O     1 
ATOM   1560 C CB    . TYR A 1 192 ? 58.647 19.212 -17.211 1.00 52.98  ? 192 TYR A CB    1 
ATOM   1561 C CG    . TYR A 1 192 ? 59.856 18.410 -17.571 1.00 60.67  ? 192 TYR A CG    1 
ATOM   1562 C CD1   . TYR A 1 192 ? 60.496 17.615 -16.630 1.00 48.08  ? 192 TYR A CD1   1 
ATOM   1563 C CD2   . TYR A 1 192 ? 60.358 18.441 -18.864 1.00 63.07  ? 192 TYR A CD2   1 
ATOM   1564 C CE1   . TYR A 1 192 ? 61.610 16.869 -16.972 1.00 57.79  ? 192 TYR A CE1   1 
ATOM   1565 C CE2   . TYR A 1 192 ? 61.469 17.710 -19.216 1.00 69.15  ? 192 TYR A CE2   1 
ATOM   1566 C CZ    . TYR A 1 192 ? 62.093 16.924 -18.273 1.00 65.35  ? 192 TYR A CZ    1 
ATOM   1567 O OH    . TYR A 1 192 ? 63.199 16.203 -18.654 1.00 72.01  ? 192 TYR A OH    1 
ATOM   1568 N N     . ILE A 1 193 ? 55.668 20.080 -16.659 1.00 57.89  ? 193 ILE A N     1 
ATOM   1569 C CA    . ILE A 1 193 ? 54.700 20.661 -15.736 1.00 59.91  ? 193 ILE A CA    1 
ATOM   1570 C C     . ILE A 1 193 ? 53.554 19.688 -15.490 1.00 55.80  ? 193 ILE A C     1 
ATOM   1571 O O     . ILE A 1 193 ? 53.110 19.505 -14.351 1.00 54.03  ? 193 ILE A O     1 
ATOM   1572 C CB    . ILE A 1 193 ? 54.202 22.013 -16.276 1.00 62.18  ? 193 ILE A CB    1 
ATOM   1573 C CG1   . ILE A 1 193 ? 55.375 22.984 -16.407 1.00 61.18  ? 193 ILE A CG1   1 
ATOM   1574 C CG2   . ILE A 1 193 ? 53.110 22.589 -15.390 1.00 60.50  ? 193 ILE A CG2   1 
ATOM   1575 C CD1   . ILE A 1 193 ? 56.208 23.113 -15.154 1.00 66.43  ? 193 ILE A CD1   1 
ATOM   1576 N N     . GLU A 1 194 ? 53.062 19.045 -16.550 1.00 52.21  ? 194 GLU A N     1 
ATOM   1577 C CA    . GLU A 1 194 ? 52.016 18.035 -16.379 1.00 52.50  ? 194 GLU A CA    1 
ATOM   1578 C C     . GLU A 1 194 ? 52.488 16.877 -15.499 1.00 53.56  ? 194 GLU A C     1 
ATOM   1579 O O     . GLU A 1 194 ? 51.757 16.416 -14.607 1.00 53.77  ? 194 GLU A O     1 
ATOM   1580 C CB    . GLU A 1 194 ? 51.576 17.518 -17.746 1.00 61.11  ? 194 GLU A CB    1 
ATOM   1581 C CG    . GLU A 1 194 ? 50.663 16.305 -17.683 1.00 75.75  ? 194 GLU A CG    1 
ATOM   1582 C CD    . GLU A 1 194 ? 50.275 15.797 -19.061 1.00 80.82  ? 194 GLU A CD    1 
ATOM   1583 O OE1   . GLU A 1 194 ? 51.075 15.048 -19.669 1.00 72.89  ? 194 GLU A OE1   1 
ATOM   1584 O OE2   . GLU A 1 194 ? 49.175 16.157 -19.536 1.00 75.54  ? 194 GLU A OE2   1 
ATOM   1585 N N     . ALA A 1 195 ? 53.708 16.388 -15.738 1.00 51.05  ? 195 ALA A N     1 
ATOM   1586 C CA    . ALA A 1 195 ? 54.219 15.277 -14.939 1.00 54.31  ? 195 ALA A CA    1 
ATOM   1587 C C     . ALA A 1 195 ? 54.403 15.688 -13.485 1.00 52.18  ? 195 ALA A C     1 
ATOM   1588 O O     . ALA A 1 195 ? 54.106 14.913 -12.568 1.00 51.66  ? 195 ALA A O     1 
ATOM   1589 C CB    . ALA A 1 195 ? 55.532 14.765 -15.522 1.00 45.21  ? 195 ALA A CB    1 
ATOM   1590 N N     . ALA A 1 196 ? 54.874 16.913 -13.255 1.00 49.70  ? 196 ALA A N     1 
ATOM   1591 C CA    . ALA A 1 196 ? 55.039 17.392 -11.891 1.00 46.22  ? 196 ALA A CA    1 
ATOM   1592 C C     . ALA A 1 196 ? 53.695 17.516 -11.193 1.00 51.86  ? 196 ALA A C     1 
ATOM   1593 O O     . ALA A 1 196 ? 53.580 17.200 -10.006 1.00 50.88  ? 196 ALA A O     1 
ATOM   1594 C CB    . ALA A 1 196 ? 55.779 18.731 -11.886 1.00 50.46  ? 196 ALA A CB    1 
ATOM   1595 N N     . ASN A 1 197 ? 52.658 17.959 -11.915 1.00 49.20  ? 197 ASN A N     1 
ATOM   1596 C CA    . ASN A 1 197 ? 51.354 18.096 -11.273 1.00 50.18  ? 197 ASN A CA    1 
ATOM   1597 C C     . ASN A 1 197 ? 50.780 16.735 -10.899 1.00 53.44  ? 197 ASN A C     1 
ATOM   1598 O O     . ASN A 1 197 ? 50.227 16.571 -9.802  1.00 56.52  ? 197 ASN A O     1 
ATOM   1599 C CB    . ASN A 1 197 ? 50.394 18.880 -12.169 1.00 57.11  ? 197 ASN A CB    1 
ATOM   1600 C CG    . ASN A 1 197 ? 50.655 20.376 -12.123 1.00 61.09  ? 197 ASN A CG    1 
ATOM   1601 O OD1   . ASN A 1 197 ? 50.930 20.999 -13.145 1.00 73.12  ? 197 ASN A OD1   1 
ATOM   1602 N ND2   . ASN A 1 197 ? 50.580 20.957 -10.931 1.00 60.38  ? 197 ASN A ND2   1 
ATOM   1603 N N     . GLU A 1 198 ? 50.928 15.736 -11.773 1.00 51.54  ? 198 GLU A N     1 
ATOM   1604 C CA    . GLU A 1 198 ? 50.498 14.389 -11.393 1.00 53.95  ? 198 GLU A CA    1 
ATOM   1605 C C     . GLU A 1 198 ? 51.301 13.865 -10.198 1.00 49.43  ? 198 GLU A C     1 
ATOM   1606 O O     . GLU A 1 198 ? 50.744 13.228 -9.289  1.00 49.30  ? 198 GLU A O     1 
ATOM   1607 C CB    . GLU A 1 198 ? 50.614 13.436 -12.581 1.00 52.14  ? 198 GLU A CB    1 
ATOM   1608 C CG    . GLU A 1 198 ? 50.073 12.049 -12.271 1.00 58.13  ? 198 GLU A CG    1 
ATOM   1609 C CD    . GLU A 1 198 ? 49.974 11.162 -13.493 1.00 61.28  ? 198 GLU A CD    1 
ATOM   1610 O OE1   . GLU A 1 198 ? 50.213 11.654 -14.618 1.00 59.52  ? 198 GLU A OE1   1 
ATOM   1611 O OE2   . GLU A 1 198 ? 49.650 9.967  -13.321 1.00 61.81  ? 198 GLU A OE2   1 
ATOM   1612 N N     . MET A 1 199 ? 52.608 14.141 -10.181 1.00 48.20  ? 199 MET A N     1 
ATOM   1613 C CA    . MET A 1 199 ? 53.449 13.775 -9.044  1.00 47.19  ? 199 MET A CA    1 
ATOM   1614 C C     . MET A 1 199 ? 52.915 14.376 -7.744  1.00 49.97  ? 199 MET A C     1 
ATOM   1615 O O     . MET A 1 199 ? 52.774 13.678 -6.733  1.00 49.12  ? 199 MET A O     1 
ATOM   1616 C CB    . MET A 1 199 ? 54.883 14.235 -9.318  1.00 45.50  ? 199 MET A CB    1 
ATOM   1617 C CG    . MET A 1 199 ? 55.868 14.073 -8.153  1.00 42.95  ? 199 MET A CG    1 
ATOM   1618 S SD    . MET A 1 199 ? 57.519 14.666 -8.616  1.00 43.48  ? 199 MET A SD    1 
ATOM   1619 C CE    . MET A 1 199 ? 57.219 16.430 -8.567  1.00 39.98  ? 199 MET A CE    1 
ATOM   1620 N N     . PHE A 1 200 ? 52.621 15.677 -7.759  1.00 48.77  ? 200 PHE A N     1 
ATOM   1621 C CA    . PHE A 1 200 ? 52.033 16.341 -6.596  1.00 50.90  ? 200 PHE A CA    1 
ATOM   1622 C C     . PHE A 1 200 ? 50.748 15.652 -6.162  1.00 55.61  ? 200 PHE A C     1 
ATOM   1623 O O     . PHE A 1 200 ? 50.554 15.365 -4.974  1.00 50.27  ? 200 PHE A O     1 
ATOM   1624 C CB    . PHE A 1 200 ? 51.742 17.809 -6.905  1.00 49.30  ? 200 PHE A CB    1 
ATOM   1625 C CG    . PHE A 1 200 ? 52.947 18.595 -7.325  1.00 50.23  ? 200 PHE A CG    1 
ATOM   1626 C CD1   . PHE A 1 200 ? 54.206 18.274 -6.841  1.00 47.48  ? 200 PHE A CD1   1 
ATOM   1627 C CD2   . PHE A 1 200 ? 52.817 19.659 -8.210  1.00 49.53  ? 200 PHE A CD2   1 
ATOM   1628 C CE1   . PHE A 1 200 ? 55.321 19.003 -7.226  1.00 50.57  ? 200 PHE A CE1   1 
ATOM   1629 C CE2   . PHE A 1 200 ? 53.927 20.390 -8.604  1.00 51.19  ? 200 PHE A CE2   1 
ATOM   1630 C CZ    . PHE A 1 200 ? 55.183 20.058 -8.112  1.00 48.39  ? 200 PHE A CZ    1 
ATOM   1631 N N     . GLU A 1 201 ? 49.848 15.393 -7.116  1.00 54.27  ? 201 GLU A N     1 
ATOM   1632 C CA    . GLU A 1 201 ? 48.573 14.766 -6.768  1.00 55.27  ? 201 GLU A CA    1 
ATOM   1633 C C     . GLU A 1 201 ? 48.776 13.421 -6.082  1.00 49.81  ? 201 GLU A C     1 
ATOM   1634 O O     . GLU A 1 201 ? 48.015 13.062 -5.179  1.00 55.84  ? 201 GLU A O     1 
ATOM   1635 C CB    . GLU A 1 201 ? 47.705 14.576 -8.008  1.00 56.51  ? 201 GLU A CB    1 
ATOM   1636 C CG    . GLU A 1 201 ? 47.320 15.851 -8.713  1.00 73.14  ? 201 GLU A CG    1 
ATOM   1637 C CD    . GLU A 1 201 ? 46.529 15.577 -9.976  1.00 90.33  ? 201 GLU A CD    1 
ATOM   1638 O OE1   . GLU A 1 201 ? 45.582 14.762 -9.915  1.00 102.09 ? 201 GLU A OE1   1 
ATOM   1639 O OE2   . GLU A 1 201 ? 46.867 16.160 -11.030 1.00 90.32  ? 201 GLU A OE2   1 
ATOM   1640 N N     . LYS A 1 202 ? 49.791 12.661 -6.491  1.00 48.26  ? 202 LYS A N     1 
ATOM   1641 C CA    . LYS A 1 202 ? 49.860 11.285 -6.016  1.00 51.51  ? 202 LYS A CA    1 
ATOM   1642 C C     . LYS A 1 202 ? 50.831 11.055 -4.863  1.00 48.15  ? 202 LYS A C     1 
ATOM   1643 O O     . LYS A 1 202 ? 50.668 10.066 -4.142  1.00 49.81  ? 202 LYS A O     1 
ATOM   1644 C CB    . LYS A 1 202 ? 50.196 10.344 -7.179  1.00 47.43  ? 202 LYS A CB    1 
ATOM   1645 C CG    . LYS A 1 202 ? 49.082 10.336 -8.236  1.00 51.85  ? 202 LYS A CG    1 
ATOM   1646 C CD    . LYS A 1 202 ? 49.281 9.284  -9.310  1.00 51.27  ? 202 LYS A CD    1 
ATOM   1647 C CE    . LYS A 1 202 ? 48.107 9.290  -10.287 1.00 53.86  ? 202 LYS A CE    1 
ATOM   1648 N NZ    . LYS A 1 202 ? 48.378 8.426  -11.468 1.00 61.91  ? 202 LYS A NZ    1 
ATOM   1649 N N     . THR A 1 203 ? 51.813 11.938 -4.641  1.00 45.01  ? 203 THR A N     1 
ATOM   1650 C CA    . THR A 1 203 ? 52.849 11.674 -3.643  1.00 44.94  ? 203 THR A CA    1 
ATOM   1651 C C     . THR A 1 203 ? 53.003 12.800 -2.623  1.00 50.19  ? 203 THR A C     1 
ATOM   1652 O O     . THR A 1 203 ? 54.012 12.840 -1.907  1.00 45.43  ? 203 THR A O     1 
ATOM   1653 C CB    . THR A 1 203 ? 54.194 11.408 -4.326  1.00 44.36  ? 203 THR A CB    1 
ATOM   1654 O OG1   . THR A 1 203 ? 54.624 12.589 -5.020  1.00 42.47  ? 203 THR A OG1   1 
ATOM   1655 C CG2   . THR A 1 203 ? 54.061 10.246 -5.308  1.00 43.89  ? 203 THR A CG2   1 
ATOM   1656 N N     . ASP A 1 204 ? 52.035 13.711 -2.539  1.00 48.78  ? 204 ASP A N     1 
ATOM   1657 C CA    . ASP A 1 204 ? 51.992 14.737 -1.497  1.00 49.25  ? 204 ASP A CA    1 
ATOM   1658 C C     . ASP A 1 204 ? 51.315 14.116 -0.277  1.00 53.71  ? 204 ASP A C     1 
ATOM   1659 O O     . ASP A 1 204 ? 50.089 13.998 -0.225  1.00 49.04  ? 204 ASP A O     1 
ATOM   1660 C CB    . ASP A 1 204 ? 51.246 15.969 -2.007  1.00 50.80  ? 204 ASP A CB    1 
ATOM   1661 C CG    . ASP A 1 204 ? 51.211 17.106 -1.008  1.00 50.61  ? 204 ASP A CG    1 
ATOM   1662 O OD1   . ASP A 1 204 ? 51.998 17.100 -0.044  1.00 49.33  ? 204 ASP A OD1   1 
ATOM   1663 O OD2   . ASP A 1 204 ? 50.387 18.024 -1.196  1.00 63.08  ? 204 ASP A OD2   1 
ATOM   1664 N N     . LYS A 1 205 ? 52.113 13.706 0.706   1.00 51.62  ? 205 LYS A N     1 
ATOM   1665 C CA    . LYS A 1 205 ? 51.615 12.981 1.865   1.00 52.56  ? 205 LYS A CA    1 
ATOM   1666 C C     . LYS A 1 205 ? 51.925 13.739 3.151   1.00 49.25  ? 205 LYS A C     1 
ATOM   1667 O O     . LYS A 1 205 ? 52.891 14.505 3.228   1.00 52.28  ? 205 LYS A O     1 
ATOM   1668 C CB    . LYS A 1 205 ? 52.220 11.571 1.939   1.00 47.52  ? 205 LYS A CB    1 
ATOM   1669 C CG    . LYS A 1 205 ? 51.889 10.693 0.745   1.00 50.79  ? 205 LYS A CG    1 
ATOM   1670 C CD    . LYS A 1 205 ? 50.380 10.501 0.599   1.00 52.63  ? 205 LYS A CD    1 
ATOM   1671 C CE    . LYS A 1 205 ? 50.074 9.607  -0.592  1.00 49.94  ? 205 LYS A CE    1 
ATOM   1672 N NZ    . LYS A 1 205 ? 48.616 9.444  -0.827  1.00 56.25  ? 205 LYS A NZ    1 
ATOM   1673 N N     . LYS A 1 206 ? 51.102 13.489 4.171   1.00 51.85  ? 206 LYS A N     1 
ATOM   1674 C CA    . LYS A 1 206 ? 51.241 14.189 5.446   1.00 53.64  ? 206 LYS A CA    1 
ATOM   1675 C C     . LYS A 1 206 ? 52.611 13.945 6.069   1.00 53.22  ? 206 LYS A C     1 
ATOM   1676 O O     . LYS A 1 206 ? 53.207 14.855 6.659   1.00 47.76  ? 206 LYS A O     1 
ATOM   1677 C CB    . LYS A 1 206 ? 50.124 13.753 6.395   1.00 60.56  ? 206 LYS A CB    1 
ATOM   1678 C CG    . LYS A 1 206 ? 50.184 14.379 7.779   1.00 78.98  ? 206 LYS A CG    1 
ATOM   1679 C CD    . LYS A 1 206 ? 48.996 13.953 8.642   1.00 90.54  ? 206 LYS A CD    1 
ATOM   1680 C CE    . LYS A 1 206 ? 48.960 14.697 9.975   1.00 98.21  ? 206 LYS A CE    1 
ATOM   1681 N NZ    . LYS A 1 206 ? 47.762 14.327 10.794  1.00 95.70  ? 206 LYS A NZ    1 
ATOM   1682 N N     . ASN A 1 207 ? 53.127 12.723 5.940   1.00 45.73  ? 207 ASN A N     1 
ATOM   1683 C CA    . ASN A 1 207 ? 54.431 12.340 6.462   1.00 47.72  ? 207 ASN A CA    1 
ATOM   1684 C C     . ASN A 1 207 ? 55.583 12.717 5.536   1.00 50.01  ? 207 ASN A C     1 
ATOM   1685 O O     . ASN A 1 207 ? 56.750 12.568 5.923   1.00 46.50  ? 207 ASN A O     1 
ATOM   1686 C CB    . ASN A 1 207 ? 54.453 10.826 6.698   1.00 51.66  ? 207 ASN A CB    1 
ATOM   1687 C CG    . ASN A 1 207 ? 54.043 10.037 5.448   1.00 61.04  ? 207 ASN A CG    1 
ATOM   1688 O OD1   . ASN A 1 207 ? 52.863 10.028 5.078   1.00 53.88  ? 207 ASN A OD1   1 
ATOM   1689 N ND2   . ASN A 1 207 ? 55.019 9.383  4.785   1.00 40.89  ? 207 ASN A ND2   1 
ATOM   1690 N N     . ALA A 1 208 ? 55.291 13.159 4.312   1.00 44.93  ? 208 ALA A N     1 
ATOM   1691 C CA    . ALA A 1 208 ? 56.329 13.464 3.325   1.00 42.96  ? 208 ALA A CA    1 
ATOM   1692 C C     . ALA A 1 208 ? 55.759 14.478 2.344   1.00 45.39  ? 208 ALA A C     1 
ATOM   1693 O O     . ALA A 1 208 ? 55.396 14.144 1.208   1.00 43.94  ? 208 ALA A O     1 
ATOM   1694 C CB    . ALA A 1 208 ? 56.791 12.194 2.612   1.00 40.57  ? 208 ALA A CB    1 
ATOM   1695 N N     . PRO A 1 209 ? 55.636 15.732 2.765   1.00 39.47  ? 209 PRO A N     1 
ATOM   1696 C CA    . PRO A 1 209 ? 54.908 16.711 1.957   1.00 46.30  ? 209 PRO A CA    1 
ATOM   1697 C C     . PRO A 1 209 ? 55.735 17.244 0.799   1.00 45.65  ? 209 PRO A C     1 
ATOM   1698 O O     . PRO A 1 209 ? 56.971 17.274 0.839   1.00 41.95  ? 209 PRO A O     1 
ATOM   1699 C CB    . PRO A 1 209 ? 54.598 17.828 2.962   1.00 43.38  ? 209 PRO A CB    1 
ATOM   1700 C CG    . PRO A 1 209 ? 55.745 17.756 3.934   1.00 47.77  ? 209 PRO A CG    1 
ATOM   1701 C CD    . PRO A 1 209 ? 56.101 16.295 4.045   1.00 43.54  ? 209 PRO A CD    1 
ATOM   1702 N N     . TRP A 1 210 ? 55.009 17.646 -0.246  1.00 47.65  ? 210 TRP A N     1 
ATOM   1703 C CA    . TRP A 1 210 ? 55.528 18.497 -1.308  1.00 44.70  ? 210 TRP A CA    1 
ATOM   1704 C C     . TRP A 1 210 ? 55.270 19.951 -0.938  1.00 45.20  ? 210 TRP A C     1 
ATOM   1705 O O     . TRP A 1 210 ? 54.139 20.326 -0.619  1.00 49.95  ? 210 TRP A O     1 
ATOM   1706 C CB    . TRP A 1 210 ? 54.869 18.178 -2.654  1.00 43.58  ? 210 TRP A CB    1 
ATOM   1707 C CG    . TRP A 1 210 ? 55.523 17.038 -3.392  1.00 45.58  ? 210 TRP A CG    1 
ATOM   1708 C CD1   . TRP A 1 210 ? 55.027 15.775 -3.562  1.00 44.55  ? 210 TRP A CD1   1 
ATOM   1709 C CD2   . TRP A 1 210 ? 56.799 17.059 -4.049  1.00 43.20  ? 210 TRP A CD2   1 
ATOM   1710 N NE1   . TRP A 1 210 ? 55.914 15.010 -4.287  1.00 45.76  ? 210 TRP A NE1   1 
ATOM   1711 C CE2   . TRP A 1 210 ? 57.009 15.774 -4.600  1.00 42.59  ? 210 TRP A CE2   1 
ATOM   1712 C CE3   . TRP A 1 210 ? 57.783 18.041 -4.230  1.00 40.84  ? 210 TRP A CE3   1 
ATOM   1713 C CZ2   . TRP A 1 210 ? 58.165 15.444 -5.311  1.00 38.03  ? 210 TRP A CZ2   1 
ATOM   1714 C CZ3   . TRP A 1 210 ? 58.933 17.709 -4.936  1.00 40.47  ? 210 TRP A CZ3   1 
ATOM   1715 C CH2   . TRP A 1 210 ? 59.111 16.422 -5.470  1.00 40.44  ? 210 TRP A CH2   1 
ATOM   1716 N N     . VAL A 1 211 ? 56.323 20.754 -0.962  1.00 45.14  ? 211 VAL A N     1 
ATOM   1717 C CA    . VAL A 1 211 ? 56.254 22.187 -0.738  1.00 48.38  ? 211 VAL A CA    1 
ATOM   1718 C C     . VAL A 1 211 ? 56.573 22.842 -2.072  1.00 47.04  ? 211 VAL A C     1 
ATOM   1719 O O     . VAL A 1 211 ? 57.671 22.660 -2.612  1.00 44.83  ? 211 VAL A O     1 
ATOM   1720 C CB    . VAL A 1 211 ? 57.234 22.641 0.358   1.00 48.79  ? 211 VAL A CB    1 
ATOM   1721 C CG1   . VAL A 1 211 ? 57.177 24.151 0.533   1.00 46.12  ? 211 VAL A CG1   1 
ATOM   1722 C CG2   . VAL A 1 211 ? 56.940 21.929 1.686   1.00 45.18  ? 211 VAL A CG2   1 
ATOM   1723 N N     . LEU A 1 212 ? 55.607 23.568 -2.622  1.00 44.46  ? 212 LEU A N     1 
ATOM   1724 C CA    . LEU A 1 212 ? 55.819 24.304 -3.860  1.00 49.32  ? 212 LEU A CA    1 
ATOM   1725 C C     . LEU A 1 212 ? 56.419 25.662 -3.520  1.00 50.43  ? 212 LEU A C     1 
ATOM   1726 O O     . LEU A 1 212 ? 55.835 26.429 -2.751  1.00 51.65  ? 212 LEU A O     1 
ATOM   1727 C CB    . LEU A 1 212 ? 54.514 24.463 -4.636  1.00 50.49  ? 212 LEU A CB    1 
ATOM   1728 C CG    . LEU A 1 212 ? 54.137 23.341 -5.604  1.00 57.15  ? 212 LEU A CG    1 
ATOM   1729 C CD1   . LEU A 1 212 ? 53.992 22.010 -4.893  1.00 53.36  ? 212 LEU A CD1   1 
ATOM   1730 C CD2   . LEU A 1 212 ? 52.851 23.689 -6.340  1.00 58.66  ? 212 LEU A CD2   1 
ATOM   1731 N N     . VAL A 1 213 ? 57.584 25.952 -4.089  1.00 48.91  ? 213 VAL A N     1 
ATOM   1732 C CA    . VAL A 1 213 ? 58.354 27.146 -3.777  1.00 48.69  ? 213 VAL A CA    1 
ATOM   1733 C C     . VAL A 1 213 ? 58.283 28.098 -4.964  1.00 52.44  ? 213 VAL A C     1 
ATOM   1734 O O     . VAL A 1 213 ? 58.592 27.712 -6.099  1.00 47.41  ? 213 VAL A O     1 
ATOM   1735 C CB    . VAL A 1 213 ? 59.808 26.785 -3.439  1.00 50.80  ? 213 VAL A CB    1 
ATOM   1736 C CG1   . VAL A 1 213 ? 60.640 28.042 -3.260  1.00 56.15  ? 213 VAL A CG1   1 
ATOM   1737 C CG2   . VAL A 1 213 ? 59.853 25.902 -2.188  1.00 47.26  ? 213 VAL A CG2   1 
ATOM   1738 N N     . ALA A 1 214 ? 57.863 29.336 -4.702  1.00 51.21  ? 214 ALA A N     1 
ATOM   1739 C CA    . ALA A 1 214 ? 57.851 30.400 -5.704  1.00 46.60  ? 214 ALA A CA    1 
ATOM   1740 C C     . ALA A 1 214 ? 59.284 30.856 -5.930  1.00 52.88  ? 214 ALA A C     1 
ATOM   1741 O O     . ALA A 1 214 ? 59.858 31.566 -5.104  1.00 57.72  ? 214 ALA A O     1 
ATOM   1742 C CB    . ALA A 1 214 ? 56.968 31.554 -5.245  1.00 56.69  ? 214 ALA A CB    1 
ATOM   1743 N N     . GLY A 1 215 ? 59.875 30.439 -7.048  1.00 49.43  ? 215 GLY A N     1 
ATOM   1744 C CA    . GLY A 1 215 ? 61.302 30.558 -7.262  1.00 48.42  ? 215 GLY A CA    1 
ATOM   1745 C C     . GLY A 1 215 ? 61.760 31.680 -8.166  1.00 54.56  ? 215 GLY A C     1 
ATOM   1746 O O     . GLY A 1 215 ? 62.971 31.833 -8.368  1.00 51.53  ? 215 GLY A O     1 
ATOM   1747 N N     . ASN A 1 216 ? 60.835 32.475 -8.712  1.00 49.87  ? 216 ASN A N     1 
ATOM   1748 C CA    . ASN A 1 216 ? 61.225 33.542 -9.630  1.00 49.87  ? 216 ASN A CA    1 
ATOM   1749 C C     . ASN A 1 216 ? 62.160 34.545 -8.960  1.00 50.94  ? 216 ASN A C     1 
ATOM   1750 O O     . ASN A 1 216 ? 63.103 35.036 -9.592  1.00 52.05  ? 216 ASN A O     1 
ATOM   1751 C CB    . ASN A 1 216 ? 59.978 34.229 -10.189 1.00 49.42  ? 216 ASN A CB    1 
ATOM   1752 C CG    . ASN A 1 216 ? 59.261 33.370 -11.227 1.00 63.62  ? 216 ASN A CG    1 
ATOM   1753 O OD1   . ASN A 1 216 ? 59.895 32.606 -11.956 1.00 55.97  ? 216 ASN A OD1   1 
ATOM   1754 N ND2   . ASN A 1 216 ? 57.936 33.486 -11.291 1.00 70.10  ? 216 ASN A ND2   1 
ATOM   1755 N N     . ASP A 1 217 ? 61.929 34.846 -7.680  1.00 47.50  ? 217 ASP A N     1 
ATOM   1756 C CA    . ASP A 1 217 ? 62.848 35.642 -6.868  1.00 53.78  ? 217 ASP A CA    1 
ATOM   1757 C C     . ASP A 1 217 ? 63.707 34.692 -6.033  1.00 50.45  ? 217 ASP A C     1 
ATOM   1758 O O     . ASP A 1 217 ? 63.198 34.000 -5.145  1.00 50.81  ? 217 ASP A O     1 
ATOM   1759 C CB    . ASP A 1 217 ? 62.083 36.623 -5.978  1.00 56.27  ? 217 ASP A CB    1 
ATOM   1760 C CG    . ASP A 1 217 ? 63.002 37.404 -5.044  1.00 66.70  ? 217 ASP A CG    1 
ATOM   1761 O OD1   . ASP A 1 217 ? 63.971 38.022 -5.536  1.00 76.76  ? 217 ASP A OD1   1 
ATOM   1762 O OD2   . ASP A 1 217 ? 62.761 37.406 -3.819  1.00 74.29  ? 217 ASP A OD2   1 
ATOM   1763 N N     . LYS A 1 218 ? 65.012 34.661 -6.317  1.00 49.48  ? 218 LYS A N     1 
ATOM   1764 C CA    . LYS A 1 218 ? 65.896 33.718 -5.635  1.00 48.54  ? 218 LYS A CA    1 
ATOM   1765 C C     . LYS A 1 218 ? 65.951 33.972 -4.131  1.00 51.07  ? 218 LYS A C     1 
ATOM   1766 O O     . LYS A 1 218 ? 65.997 33.025 -3.335  1.00 48.49  ? 218 LYS A O     1 
ATOM   1767 C CB    . LYS A 1 218 ? 67.297 33.786 -6.240  1.00 51.33  ? 218 LYS A CB    1 
ATOM   1768 C CG    . LYS A 1 218 ? 67.399 33.180 -7.633  1.00 51.42  ? 218 LYS A CG    1 
ATOM   1769 C CD    . LYS A 1 218 ? 68.832 33.203 -8.150  1.00 59.64  ? 218 LYS A CD    1 
ATOM   1770 C CE    . LYS A 1 218 ? 68.938 32.591 -9.547  1.00 61.44  ? 218 LYS A CE    1 
ATOM   1771 N NZ    . LYS A 1 218 ? 70.354 32.471 -10.003 1.00 63.54  ? 218 LYS A NZ    1 
ATOM   1772 N N     . LYS A 1 219 ? 65.968 35.242 -3.721  1.00 46.89  ? 219 LYS A N     1 
ATOM   1773 C CA    . LYS A 1 219 ? 66.071 35.557 -2.298  1.00 51.58  ? 219 LYS A CA    1 
ATOM   1774 C C     . LYS A 1 219 ? 64.858 35.039 -1.532  1.00 48.44  ? 219 LYS A C     1 
ATOM   1775 O O     . LYS A 1 219 ? 64.993 34.401 -0.472  1.00 51.43  ? 219 LYS A O     1 
ATOM   1776 C CB    . LYS A 1 219 ? 66.236 37.067 -2.117  1.00 53.26  ? 219 LYS A CB    1 
ATOM   1777 C CG    . LYS A 1 219 ? 67.543 37.616 -2.705  1.00 56.37  ? 219 LYS A CG    1 
ATOM   1778 C CD    . LYS A 1 219 ? 67.692 39.119 -2.450  1.00 69.80  ? 219 LYS A CD    1 
ATOM   1779 C CE    . LYS A 1 219 ? 68.835 39.738 -3.260  1.00 73.13  ? 219 LYS A CE    1 
ATOM   1780 N NZ    . LYS A 1 219 ? 70.151 39.056 -3.062  1.00 80.31  ? 219 LYS A NZ    1 
ATOM   1781 N N     . TYR A 1 220 ? 63.660 35.292 -2.068  1.00 44.22  ? 220 TYR A N     1 
ATOM   1782 C CA    . TYR A 1 220 ? 62.446 34.755 -1.463  1.00 53.87  ? 220 TYR A CA    1 
ATOM   1783 C C     . TYR A 1 220 ? 62.471 33.231 -1.441  1.00 48.50  ? 220 TYR A C     1 
ATOM   1784 O O     . TYR A 1 220 ? 62.032 32.615 -0.466  1.00 49.38  ? 220 TYR A O     1 
ATOM   1785 C CB    . TYR A 1 220 ? 61.218 35.276 -2.215  1.00 52.54  ? 220 TYR A CB    1 
ATOM   1786 C CG    . TYR A 1 220 ? 59.892 34.689 -1.784  1.00 58.28  ? 220 TYR A CG    1 
ATOM   1787 C CD1   . TYR A 1 220 ? 59.060 35.371 -0.900  1.00 59.42  ? 220 TYR A CD1   1 
ATOM   1788 C CD2   . TYR A 1 220 ? 59.456 33.465 -2.284  1.00 55.30  ? 220 TYR A CD2   1 
ATOM   1789 C CE1   . TYR A 1 220 ? 57.840 34.840 -0.515  1.00 57.61  ? 220 TYR A CE1   1 
ATOM   1790 C CE2   . TYR A 1 220 ? 58.244 32.930 -1.906  1.00 60.11  ? 220 TYR A CE2   1 
ATOM   1791 C CZ    . TYR A 1 220 ? 57.439 33.619 -1.022  1.00 62.70  ? 220 TYR A CZ    1 
ATOM   1792 O OH    . TYR A 1 220 ? 56.228 33.080 -0.649  1.00 81.98  ? 220 TYR A OH    1 
ATOM   1793 N N     . ALA A 1 221 ? 62.988 32.606 -2.506  1.00 48.38  ? 221 ALA A N     1 
ATOM   1794 C CA    . ALA A 1 221 ? 63.030 31.145 -2.563  1.00 46.97  ? 221 ALA A CA    1 
ATOM   1795 C C     . ALA A 1 221 ? 63.914 30.575 -1.465  1.00 42.79  ? 221 ALA A C     1 
ATOM   1796 O O     . ALA A 1 221 ? 63.537 29.612 -0.787  1.00 42.88  ? 221 ALA A O     1 
ATOM   1797 C CB    . ALA A 1 221 ? 63.532 30.679 -3.931  1.00 42.63  ? 221 ALA A CB    1 
ATOM   1798 N N     . ARG A 1 222 ? 65.119 31.128 -1.314  1.00 40.70  ? 222 ARG A N     1 
ATOM   1799 C CA    . ARG A 1 222 ? 66.029 30.669 -0.272  1.00 44.30  ? 222 ARG A CA    1 
ATOM   1800 C C     . ARG A 1 222 ? 65.387 30.799 1.105   1.00 44.71  ? 222 ARG A C     1 
ATOM   1801 O O     . ARG A 1 222 ? 65.401 29.850 1.913   1.00 46.65  ? 222 ARG A O     1 
ATOM   1802 C CB    . ARG A 1 222 ? 67.328 31.465 -0.342  1.00 41.37  ? 222 ARG A CB    1 
ATOM   1803 C CG    . ARG A 1 222 ? 68.061 31.321 -1.662  1.00 37.75  ? 222 ARG A CG    1 
ATOM   1804 C CD    . ARG A 1 222 ? 68.969 32.500 -1.867  1.00 45.49  ? 222 ARG A CD    1 
ATOM   1805 N NE    . ARG A 1 222 ? 69.638 32.473 -3.162  1.00 52.42  ? 222 ARG A NE    1 
ATOM   1806 C CZ    . ARG A 1 222 ? 70.340 33.484 -3.659  1.00 55.62  ? 222 ARG A CZ    1 
ATOM   1807 N NH1   . ARG A 1 222 ? 70.484 34.623 -2.996  1.00 51.12  ? 222 ARG A NH1   1 
ATOM   1808 N NH2   . ARG A 1 222 ? 70.907 33.353 -4.852  1.00 49.58  ? 222 ARG A NH2   1 
ATOM   1809 N N     . VAL A 1 223 ? 64.802 31.972 1.380   1.00 41.00  ? 223 VAL A N     1 
ATOM   1810 C CA    . VAL A 1 223 ? 64.161 32.189 2.675   1.00 41.63  ? 223 VAL A CA    1 
ATOM   1811 C C     . VAL A 1 223 ? 63.031 31.189 2.887   1.00 43.43  ? 223 VAL A C     1 
ATOM   1812 O O     . VAL A 1 223 ? 62.892 30.607 3.971   1.00 46.14  ? 223 VAL A O     1 
ATOM   1813 C CB    . VAL A 1 223 ? 63.675 33.647 2.793   1.00 47.85  ? 223 VAL A CB    1 
ATOM   1814 C CG1   . VAL A 1 223 ? 62.638 33.778 3.910   1.00 48.77  ? 223 VAL A CG1   1 
ATOM   1815 C CG2   . VAL A 1 223 ? 64.867 34.581 3.053   1.00 45.54  ? 223 VAL A CG2   1 
ATOM   1816 N N     . GLN A 1 224 ? 62.218 30.955 1.854   1.00 43.80  ? 224 GLN A N     1 
ATOM   1817 C CA    . GLN A 1 224 ? 61.079 30.059 2.015   1.00 40.51  ? 224 GLN A CA    1 
ATOM   1818 C C     . GLN A 1 224 ? 61.538 28.634 2.258   1.00 44.38  ? 224 GLN A C     1 
ATOM   1819 O O     . GLN A 1 224 ? 60.947 27.923 3.075   1.00 44.36  ? 224 GLN A O     1 
ATOM   1820 C CB    . GLN A 1 224 ? 60.166 30.117 0.789   1.00 47.12  ? 224 GLN A CB    1 
ATOM   1821 C CG    . GLN A 1 224 ? 58.942 29.204 0.900   1.00 59.06  ? 224 GLN A CG    1 
ATOM   1822 C CD    . GLN A 1 224 ? 58.094 29.168 -0.369  1.00 69.75  ? 224 GLN A CD    1 
ATOM   1823 O OE1   . GLN A 1 224 ? 58.439 29.788 -1.380  1.00 67.09  ? 224 GLN A OE1   1 
ATOM   1824 N NE2   . GLN A 1 224 ? 56.977 28.435 -0.320  1.00 59.88  ? 224 GLN A NE2   1 
ATOM   1825 N N     . VAL A 1 225 ? 62.573 28.188 1.541   1.00 36.47  ? 225 VAL A N     1 
ATOM   1826 C CA    . VAL A 1 225 ? 63.087 26.841 1.763   1.00 39.41  ? 225 VAL A CA    1 
ATOM   1827 C C     . VAL A 1 225 ? 63.527 26.681 3.212   1.00 40.61  ? 225 VAL A C     1 
ATOM   1828 O O     . VAL A 1 225 ? 63.211 25.675 3.867   1.00 43.21  ? 225 VAL A O     1 
ATOM   1829 C CB    . VAL A 1 225 ? 64.228 26.528 0.779   1.00 44.07  ? 225 VAL A CB    1 
ATOM   1830 C CG1   . VAL A 1 225 ? 64.987 25.293 1.227   1.00 37.13  ? 225 VAL A CG1   1 
ATOM   1831 C CG2   . VAL A 1 225 ? 63.670 26.329 -0.623  1.00 38.28  ? 225 VAL A CG2   1 
ATOM   1832 N N     . LEU A 1 226 ? 64.225 27.686 3.752   1.00 40.64  ? 226 LEU A N     1 
ATOM   1833 C CA    . LEU A 1 226 ? 64.651 27.602 5.151   1.00 42.09  ? 226 LEU A CA    1 
ATOM   1834 C C     . LEU A 1 226 ? 63.450 27.565 6.101   1.00 41.46  ? 226 LEU A C     1 
ATOM   1835 O O     . LEU A 1 226 ? 63.384 26.716 7.008   1.00 41.13  ? 226 LEU A O     1 
ATOM   1836 C CB    . LEU A 1 226 ? 65.580 28.768 5.488   1.00 42.35  ? 226 LEU A CB    1 
ATOM   1837 C CG    . LEU A 1 226 ? 67.065 28.521 5.207   1.00 42.42  ? 226 LEU A CG    1 
ATOM   1838 C CD1   . LEU A 1 226 ? 67.784 29.835 5.024   1.00 42.56  ? 226 LEU A CD1   1 
ATOM   1839 C CD2   . LEU A 1 226 ? 67.695 27.739 6.346   1.00 36.83  ? 226 LEU A CD2   1 
ATOM   1840 N N     . GLN A 1 227 ? 62.486 28.474 5.901   1.00 38.80  ? 227 GLN A N     1 
ATOM   1841 C CA    . GLN A 1 227 ? 61.316 28.527 6.780   1.00 45.11  ? 227 GLN A CA    1 
ATOM   1842 C C     . GLN A 1 227 ? 60.535 27.222 6.749   1.00 41.59  ? 227 GLN A C     1 
ATOM   1843 O O     . GLN A 1 227 ? 60.121 26.710 7.792   1.00 45.02  ? 227 GLN A O     1 
ATOM   1844 C CB    . GLN A 1 227 ? 60.393 29.687 6.392   1.00 42.46  ? 227 GLN A CB    1 
ATOM   1845 C CG    . GLN A 1 227 ? 60.919 31.057 6.754   1.00 45.89  ? 227 GLN A CG    1 
ATOM   1846 C CD    . GLN A 1 227 ? 60.005 32.176 6.270   1.00 60.53  ? 227 GLN A CD    1 
ATOM   1847 O OE1   . GLN A 1 227 ? 59.165 31.975 5.390   1.00 60.88  ? 227 GLN A OE1   1 
ATOM   1848 N NE2   . GLN A 1 227 ? 60.169 33.361 6.843   1.00 57.00  ? 227 GLN A NE2   1 
ATOM   1849 N N     . GLU A 1 228 ? 60.311 26.673 5.556   1.00 42.27  ? 228 GLU A N     1 
ATOM   1850 C CA    . GLU A 1 228 ? 59.501 25.467 5.444   1.00 44.60  ? 228 GLU A CA    1 
ATOM   1851 C C     . GLU A 1 228 ? 60.226 24.261 6.031   1.00 45.28  ? 228 GLU A C     1 
ATOM   1852 O O     . GLU A 1 228 ? 59.605 23.430 6.712   1.00 45.79  ? 228 GLU A O     1 
ATOM   1853 C CB    . GLU A 1 228 ? 59.118 25.226 3.984   1.00 41.37  ? 228 GLU A CB    1 
ATOM   1854 C CG    . GLU A 1 228 ? 58.061 26.198 3.451   1.00 48.82  ? 228 GLU A CG    1 
ATOM   1855 C CD    . GLU A 1 228 ? 56.640 25.854 3.897   1.00 58.75  ? 228 GLU A CD    1 
ATOM   1856 O OE1   . GLU A 1 228 ? 56.438 24.839 4.604   1.00 67.42  ? 228 GLU A OE1   1 
ATOM   1857 O OE2   . GLU A 1 228 ? 55.714 26.607 3.532   1.00 68.28  ? 228 GLU A OE2   1 
ATOM   1858 N N     . THR A 1 229 ? 61.541 24.149 5.792   1.00 42.99  ? 229 THR A N     1 
ATOM   1859 C CA    . THR A 1 229 ? 62.306 23.086 6.438   1.00 41.38  ? 229 THR A CA    1 
ATOM   1860 C C     . THR A 1 229 ? 62.178 23.168 7.960   1.00 43.72  ? 229 THR A C     1 
ATOM   1861 O O     . THR A 1 229 ? 61.880 22.165 8.627   1.00 41.35  ? 229 THR A O     1 
ATOM   1862 C CB    . THR A 1 229 ? 63.776 23.154 6.011   1.00 39.79  ? 229 THR A CB    1 
ATOM   1863 O OG1   . THR A 1 229 ? 63.868 23.034 4.582   1.00 40.54  ? 229 THR A OG1   1 
ATOM   1864 C CG2   . THR A 1 229 ? 64.573 22.021 6.666   1.00 39.45  ? 229 THR A CG2   1 
ATOM   1865 N N     . LEU A 1 230 ? 62.376 24.364 8.526   1.00 42.04  ? 230 LEU A N     1 
ATOM   1866 C CA    . LEU A 1 230 ? 62.300 24.511 9.979   1.00 42.72  ? 230 LEU A CA    1 
ATOM   1867 C C     . LEU A 1 230 ? 60.898 24.204 10.506  1.00 48.33  ? 230 LEU A C     1 
ATOM   1868 O O     . LEU A 1 230 ? 60.743 23.570 11.562  1.00 43.31  ? 230 LEU A O     1 
ATOM   1869 C CB    . LEU A 1 230 ? 62.727 25.921 10.377  1.00 42.06  ? 230 LEU A CB    1 
ATOM   1870 C CG    . LEU A 1 230 ? 64.212 26.204 10.170  1.00 48.57  ? 230 LEU A CG    1 
ATOM   1871 C CD1   . LEU A 1 230 ? 64.468 27.696 10.256  1.00 45.43  ? 230 LEU A CD1   1 
ATOM   1872 C CD2   . LEU A 1 230 ? 65.036 25.452 11.208  1.00 38.76  ? 230 LEU A CD2   1 
ATOM   1873 N N     . ALA A 1 231 ? 59.864 24.631 9.776   1.00 49.42  ? 231 ALA A N     1 
ATOM   1874 C CA    . ALA A 1 231 ? 58.492 24.422 10.236  1.00 50.81  ? 231 ALA A CA    1 
ATOM   1875 C C     . ALA A 1 231 ? 58.138 22.942 10.262  1.00 50.59  ? 231 ALA A C     1 
ATOM   1876 O O     . ALA A 1 231 ? 57.530 22.455 11.228  1.00 50.30  ? 231 ALA A O     1 
ATOM   1877 C CB    . ALA A 1 231 ? 57.512 25.194 9.348   1.00 43.38  ? 231 ALA A CB    1 
ATOM   1878 N N     . HIS A 1 232 ? 58.497 22.202 9.205   1.00 46.56  ? 232 HIS A N     1 
ATOM   1879 C CA    A HIS A 1 232 ? 58.163 20.788 9.198   0.50 47.49  ? 232 HIS A CA    1 
ATOM   1880 C CA    B HIS A 1 232 ? 58.181 20.773 9.184   0.50 47.42  ? 232 HIS A CA    1 
ATOM   1881 C C     . HIS A 1 232 ? 59.009 20.014 10.206  1.00 50.56  ? 232 HIS A C     1 
ATOM   1882 O O     . HIS A 1 232 ? 58.517 19.050 10.809  1.00 53.01  ? 232 HIS A O     1 
ATOM   1883 C CB    A HIS A 1 232 ? 58.285 20.241 7.775   0.50 47.85  ? 232 HIS A CB    1 
ATOM   1884 C CB    B HIS A 1 232 ? 58.389 20.170 7.790   0.50 47.80  ? 232 HIS A CB    1 
ATOM   1885 C CG    A HIS A 1 232 ? 57.191 20.716 6.860   0.50 52.32  ? 232 HIS A CG    1 
ATOM   1886 C CG    B HIS A 1 232 ? 57.855 18.771 7.644   0.50 48.45  ? 232 HIS A CG    1 
ATOM   1887 N ND1   A HIS A 1 232 ? 57.220 21.943 6.229   0.50 47.02  ? 232 HIS A ND1   1 
ATOM   1888 N ND1   B HIS A 1 232 ? 58.672 17.666 7.517   0.50 47.35  ? 232 HIS A ND1   1 
ATOM   1889 C CD2   A HIS A 1 232 ? 56.019 20.138 6.500   0.50 52.73  ? 232 HIS A CD2   1 
ATOM   1890 C CD2   B HIS A 1 232 ? 56.584 18.298 7.609   0.50 48.94  ? 232 HIS A CD2   1 
ATOM   1891 C CE1   A HIS A 1 232 ? 56.124 22.090 5.505   0.50 55.16  ? 232 HIS A CE1   1 
ATOM   1892 C CE1   B HIS A 1 232 ? 57.932 16.578 7.402   0.50 39.95  ? 232 HIS A CE1   1 
ATOM   1893 N NE2   A HIS A 1 232 ? 55.379 21.009 5.651   0.50 51.55  ? 232 HIS A NE2   1 
ATOM   1894 N NE2   B HIS A 1 232 ? 56.661 16.933 7.461   0.50 50.68  ? 232 HIS A NE2   1 
ATOM   1895 N N     . ILE A 1 233 ? 60.258 20.433 10.434  1.00 47.92  ? 233 ILE A N     1 
ATOM   1896 C CA    . ILE A 1 233 ? 61.040 19.799 11.492  1.00 47.60  ? 233 ILE A CA    1 
ATOM   1897 C C     . ILE A 1 233 ? 60.352 19.983 12.843  1.00 51.30  ? 233 ILE A C     1 
ATOM   1898 O O     . ILE A 1 233 ? 60.237 19.037 13.630  1.00 48.32  ? 233 ILE A O     1 
ATOM   1899 C CB    . ILE A 1 233 ? 62.478 20.347 11.509  1.00 43.09  ? 233 ILE A CB    1 
ATOM   1900 C CG1   . ILE A 1 233 ? 63.263 19.809 10.309  1.00 41.20  ? 233 ILE A CG1   1 
ATOM   1901 C CG2   . ILE A 1 233 ? 63.177 19.975 12.816  1.00 41.77  ? 233 ILE A CG2   1 
ATOM   1902 C CD1   . ILE A 1 233 ? 64.645 20.386 10.183  1.00 39.16  ? 233 ILE A CD1   1 
ATOM   1903 N N     . GLU A 1 234 ? 59.865 21.193 13.124  1.00 46.82  ? 234 GLU A N     1 
ATOM   1904 C CA    . GLU A 1 234 ? 59.201 21.429 14.406  1.00 53.82  ? 234 GLU A CA    1 
ATOM   1905 C C     . GLU A 1 234 ? 57.924 20.608 14.540  1.00 54.67  ? 234 GLU A C     1 
ATOM   1906 O O     . GLU A 1 234 ? 57.654 20.034 15.607  1.00 57.63  ? 234 GLU A O     1 
ATOM   1907 C CB    . GLU A 1 234 ? 58.893 22.912 14.577  1.00 58.16  ? 234 GLU A CB    1 
ATOM   1908 C CG    . GLU A 1 234 ? 60.129 23.754 14.733  1.00 65.65  ? 234 GLU A CG    1 
ATOM   1909 C CD    . GLU A 1 234 ? 59.834 25.239 14.844  1.00 86.38  ? 234 GLU A CD    1 
ATOM   1910 O OE1   . GLU A 1 234 ? 58.935 25.625 15.633  1.00 83.24  ? 234 GLU A OE1   1 
ATOM   1911 O OE2   . GLU A 1 234 ? 60.517 26.015 14.135  1.00 74.10  ? 234 GLU A OE2   1 
ATOM   1912 N N     . ARG A 1 235 ? 57.118 20.549 13.471  1.00 52.40  ? 235 ARG A N     1 
ATOM   1913 C CA    . ARG A 1 235 ? 55.891 19.752 13.513  1.00 56.29  ? 235 ARG A CA    1 
ATOM   1914 C C     . ARG A 1 235 ? 56.198 18.283 13.777  1.00 56.11  ? 235 ARG A C     1 
ATOM   1915 O O     . ARG A 1 235 ? 55.574 17.654 14.643  1.00 55.50  ? 235 ARG A O     1 
ATOM   1916 C CB    . ARG A 1 235 ? 55.108 19.889 12.207  1.00 60.73  ? 235 ARG A CB    1 
ATOM   1917 C CG    . ARG A 1 235 ? 54.506 21.257 11.944  1.00 69.64  ? 235 ARG A CG    1 
ATOM   1918 C CD    . ARG A 1 235 ? 53.602 21.212 10.710  1.00 82.42  ? 235 ARG A CD    1 
ATOM   1919 N NE    . ARG A 1 235 ? 53.330 22.528 10.136  1.00 99.63  ? 235 ARG A NE    1 
ATOM   1920 C CZ    . ARG A 1 235 ? 53.870 22.986 9.011   1.00 87.92  ? 235 ARG A CZ    1 
ATOM   1921 N NH1   . ARG A 1 235 ? 54.733 22.265 8.314   1.00 80.36  ? 235 ARG A NH1   1 
ATOM   1922 N NH2   . ARG A 1 235 ? 53.527 24.195 8.569   1.00 96.07  ? 235 ARG A NH2   1 
ATOM   1923 N N     . GLU A 1 236 ? 57.150 17.712 13.027  1.00 53.08  ? 236 GLU A N     1 
ATOM   1924 C CA    . GLU A 1 236 ? 57.476 16.299 13.196  1.00 57.47  ? 236 GLU A CA    1 
ATOM   1925 C C     . GLU A 1 236 ? 58.080 16.026 14.571  1.00 57.53  ? 236 GLU A C     1 
ATOM   1926 O O     . GLU A 1 236 ? 57.826 14.968 15.172  1.00 52.75  ? 236 GLU A O     1 
ATOM   1927 C CB    . GLU A 1 236 ? 58.424 15.845 12.079  1.00 48.45  ? 236 GLU A CB    1 
ATOM   1928 C CG    . GLU A 1 236 ? 57.775 15.824 10.700  1.00 50.19  ? 236 GLU A CG    1 
ATOM   1929 C CD    . GLU A 1 236 ? 56.626 14.827 10.598  1.00 66.22  ? 236 GLU A CD    1 
ATOM   1930 O OE1   . GLU A 1 236 ? 56.656 13.806 11.326  1.00 66.06  ? 236 GLU A OE1   1 
ATOM   1931 O OE2   . GLU A 1 236 ? 55.694 15.065 9.794   1.00 67.34  ? 236 GLU A OE2   1 
ATOM   1932 N N     . ALA A 1 237 ? 58.870 16.975 15.089  1.00 50.39  ? 237 ALA A N     1 
ATOM   1933 C CA    . ALA A 1 237 ? 59.380 16.860 16.450  1.00 57.46  ? 237 ALA A CA    1 
ATOM   1934 C C     . ALA A 1 237 ? 58.235 16.748 17.442  1.00 58.37  ? 237 ALA A C     1 
ATOM   1935 O O     . ALA A 1 237 ? 58.234 15.866 18.308  1.00 58.28  ? 237 ALA A O     1 
ATOM   1936 C CB    . ALA A 1 237 ? 60.262 18.067 16.788  1.00 55.17  ? 237 ALA A CB    1 
ATOM   1937 N N     . LEU A 1 238 ? 57.241 17.634 17.314  1.00 63.48  ? 238 LEU A N     1 
ATOM   1938 C CA    . LEU A 1 238 ? 56.071 17.586 18.190  1.00 62.02  ? 238 LEU A CA    1 
ATOM   1939 C C     . LEU A 1 238 ? 55.342 16.254 18.072  1.00 58.40  ? 238 LEU A C     1 
ATOM   1940 O O     . LEU A 1 238 ? 55.023 15.622 19.083  1.00 61.34  ? 238 LEU A O     1 
ATOM   1941 C CB    . LEU A 1 238 ? 55.127 18.739 17.864  1.00 63.82  ? 238 LEU A CB    1 
ATOM   1942 C CG    . LEU A 1 238 ? 55.190 19.943 18.801  1.00 75.89  ? 238 LEU A CG    1 
ATOM   1943 C CD1   . LEU A 1 238 ? 56.619 20.454 18.949  1.00 85.14  ? 238 LEU A CD1   1 
ATOM   1944 C CD2   . LEU A 1 238 ? 54.284 21.031 18.273  1.00 73.63  ? 238 LEU A CD2   1 
ATOM   1945 N N     . LYS A 1 239 ? 55.071 15.812 16.836  1.00 56.84  ? 239 LYS A N     1 
ATOM   1946 C CA    . LYS A 1 239 ? 54.446 14.505 16.624  1.00 61.22  ? 239 LYS A CA    1 
ATOM   1947 C C     . LYS A 1 239 ? 55.201 13.392 17.331  1.00 62.04  ? 239 LYS A C     1 
ATOM   1948 O O     . LYS A 1 239 ? 54.600 12.384 17.714  1.00 62.59  ? 239 LYS A O     1 
ATOM   1949 C CB    . LYS A 1 239 ? 54.361 14.159 15.133  1.00 61.01  ? 239 LYS A CB    1 
ATOM   1950 C CG    . LYS A 1 239 ? 53.264 14.865 14.355  1.00 72.18  ? 239 LYS A CG    1 
ATOM   1951 C CD    . LYS A 1 239 ? 53.270 14.401 12.898  1.00 76.97  ? 239 LYS A CD    1 
ATOM   1952 C CE    . LYS A 1 239 ? 52.567 15.396 11.975  1.00 88.01  ? 239 LYS A CE    1 
ATOM   1953 N NZ    . LYS A 1 239 ? 52.720 15.024 10.534  1.00 80.23  ? 239 LYS A NZ    1 
ATOM   1954 N N     . ARG A 1 240 ? 56.517 13.533 17.487  1.00 64.56  ? 240 ARG A N     1 
ATOM   1955 C CA    . ARG A 1 240 ? 57.298 12.514 18.178  1.00 59.34  ? 240 ARG A CA    1 
ATOM   1956 C C     . ARG A 1 240 ? 57.429 12.762 19.683  1.00 62.62  ? 240 ARG A C     1 
ATOM   1957 O O     . ARG A 1 240 ? 58.187 12.048 20.349  1.00 61.31  ? 240 ARG A O     1 
ATOM   1958 C CB    . ARG A 1 240 ? 58.685 12.394 17.542  1.00 56.86  ? 240 ARG A CB    1 
ATOM   1959 C CG    . ARG A 1 240 ? 58.695 11.626 16.224  1.00 51.31  ? 240 ARG A CG    1 
ATOM   1960 C CD    . ARG A 1 240 ? 60.054 11.697 15.557  1.00 55.78  ? 240 ARG A CD    1 
ATOM   1961 N NE    . ARG A 1 240 ? 60.194 10.731 14.468  1.00 58.36  ? 240 ARG A NE    1 
ATOM   1962 C CZ    . ARG A 1 240 ? 59.698 10.909 13.253  1.00 53.58  ? 240 ARG A CZ    1 
ATOM   1963 N NH1   . ARG A 1 240 ? 59.023 12.004 12.938  1.00 59.58  ? 240 ARG A NH1   1 
ATOM   1964 N NH2   . ARG A 1 240 ? 59.877 9.965  12.335  1.00 50.02  ? 240 ARG A NH2   1 
ATOM   1965 N N     . GLY A 1 241 ? 56.708 13.736 20.237  1.00 57.82  ? 241 GLY A N     1 
ATOM   1966 C CA    . GLY A 1 241 ? 56.783 14.007 21.660  1.00 64.31  ? 241 GLY A CA    1 
ATOM   1967 C C     . GLY A 1 241 ? 57.977 14.828 22.093  1.00 72.23  ? 241 GLY A C     1 
ATOM   1968 O O     . GLY A 1 241 ? 58.207 14.977 23.298  1.00 71.53  ? 241 GLY A O     1 
ATOM   1969 N N     . LEU A 1 242 ? 58.739 15.365 21.150  1.00 61.77  ? 242 LEU A N     1 
ATOM   1970 C CA    . LEU A 1 242 ? 59.907 16.186 21.422  1.00 70.50  ? 242 LEU A CA    1 
ATOM   1971 C C     . LEU A 1 242 ? 59.568 17.646 21.166  1.00 69.48  ? 242 LEU A C     1 
ATOM   1972 O O     . LEU A 1 242 ? 58.627 17.968 20.436  1.00 75.76  ? 242 LEU A O     1 
ATOM   1973 C CB    . LEU A 1 242 ? 61.091 15.769 20.537  1.00 55.89  ? 242 LEU A CB    1 
ATOM   1974 C CG    . LEU A 1 242 ? 61.472 14.285 20.526  1.00 64.73  ? 242 LEU A CG    1 
ATOM   1975 C CD1   . LEU A 1 242 ? 62.490 14.019 19.435  1.00 57.46  ? 242 LEU A CD1   1 
ATOM   1976 C CD2   . LEU A 1 242 ? 61.999 13.820 21.887  1.00 59.47  ? 242 LEU A CD2   1 
ATOM   1977 N N     . HIS A 1 243 ? 60.358 18.531 21.766  1.00 74.00  ? 243 HIS A N     1 
ATOM   1978 C CA    . HIS A 1 243 ? 60.232 19.969 21.552  1.00 74.64  ? 243 HIS A CA    1 
ATOM   1979 C C     . HIS A 1 243 ? 61.572 20.508 21.075  1.00 67.40  ? 243 HIS A C     1 
ATOM   1980 O O     . HIS A 1 243 ? 62.591 20.330 21.752  1.00 62.87  ? 243 HIS A O     1 
ATOM   1981 C CB    . HIS A 1 243 ? 59.784 20.688 22.827  1.00 74.07  ? 243 HIS A CB    1 
ATOM   1982 C CG    . HIS A 1 243 ? 58.413 20.299 23.288  1.00 89.26  ? 243 HIS A CG    1 
ATOM   1983 N ND1   . HIS A 1 243 ? 58.148 19.095 23.908  1.00 92.49  ? 243 HIS A ND1   1 
ATOM   1984 C CD2   . HIS A 1 243 ? 57.228 20.952 23.216  1.00 92.92  ? 243 HIS A CD2   1 
ATOM   1985 C CE1   . HIS A 1 243 ? 56.861 19.026 24.201  1.00 93.11  ? 243 HIS A CE1   1 
ATOM   1986 N NE2   . HIS A 1 243 ? 56.281 20.140 23.792  1.00 93.25  ? 243 HIS A NE2   1 
ATOM   1987 N N     . LEU A 1 244 ? 61.566 21.153 19.910  1.00 66.67  ? 244 LEU A N     1 
ATOM   1988 C CA    . LEU A 1 244 ? 62.768 21.799 19.391  1.00 69.16  ? 244 LEU A CA    1 
ATOM   1989 C C     . LEU A 1 244 ? 63.137 22.989 20.275  1.00 67.81  ? 244 LEU A C     1 
ATOM   1990 O O     . LEU A 1 244 ? 62.339 23.916 20.446  1.00 72.75  ? 244 LEU A O     1 
ATOM   1991 C CB    . LEU A 1 244 ? 62.545 22.243 17.944  1.00 54.52  ? 244 LEU A CB    1 
ATOM   1992 C CG    . LEU A 1 244 ? 63.703 22.975 17.257  1.00 61.87  ? 244 LEU A CG    1 
ATOM   1993 C CD1   . LEU A 1 244 ? 64.930 22.100 17.219  1.00 63.46  ? 244 LEU A CD1   1 
ATOM   1994 C CD2   . LEU A 1 244 ? 63.340 23.387 15.851  1.00 64.25  ? 244 LEU A CD2   1 
ATOM   1995 N N     . THR A 1 245 ? 64.335 22.953 20.854  1.00 64.82  ? 245 THR A N     1 
ATOM   1996 C CA    . THR A 1 245 ? 64.850 24.035 21.678  1.00 67.62  ? 245 THR A CA    1 
ATOM   1997 C C     . THR A 1 245 ? 66.248 24.398 21.198  1.00 66.12  ? 245 THR A C     1 
ATOM   1998 O O     . THR A 1 245 ? 66.820 23.738 20.324  1.00 59.52  ? 245 THR A O     1 
ATOM   1999 C CB    . THR A 1 245 ? 64.884 23.649 23.164  1.00 68.34  ? 245 THR A CB    1 
ATOM   2000 O OG1   . THR A 1 245 ? 65.934 22.699 23.389  1.00 71.15  ? 245 THR A OG1   1 
ATOM   2001 C CG2   . THR A 1 245 ? 63.559 23.031 23.583  1.00 71.20  ? 245 THR A CG2   1 
ATOM   2002 N N     . ASN A 1 246 ? 66.801 25.463 21.776  1.00 61.28  ? 246 ASN A N     1 
ATOM   2003 C CA    . ASN A 1 246 ? 68.175 25.851 21.473  1.00 66.13  ? 246 ASN A CA    1 
ATOM   2004 C C     . ASN A 1 246 ? 69.122 24.899 22.193  1.00 67.23  ? 246 ASN A C     1 
ATOM   2005 O O     . ASN A 1 246 ? 69.267 24.964 23.418  1.00 60.69  ? 246 ASN A O     1 
ATOM   2006 C CB    . ASN A 1 246 ? 68.435 27.298 21.885  1.00 66.14  ? 246 ASN A CB    1 
ATOM   2007 C CG    . ASN A 1 246 ? 69.768 27.831 21.361  1.00 71.90  ? 246 ASN A CG    1 
ATOM   2008 O OD1   . ASN A 1 246 ? 70.808 27.182 21.490  1.00 66.75  ? 246 ASN A OD1   1 
ATOM   2009 N ND2   . ASN A 1 246 ? 69.736 29.017 20.757  1.00 66.65  ? 246 ASN A ND2   1 
ATOM   2010 N N     . VAL A 1 247 ? 69.759 24.007 21.434  1.00 64.31  ? 247 VAL A N     1 
ATOM   2011 C CA    . VAL A 1 247 ? 70.747 23.085 21.980  1.00 61.69  ? 247 VAL A CA    1 
ATOM   2012 C C     . VAL A 1 247 ? 72.174 23.551 21.699  1.00 62.60  ? 247 VAL A C     1 
ATOM   2013 O O     . VAL A 1 247 ? 73.123 22.793 21.914  1.00 65.47  ? 247 VAL A O     1 
ATOM   2014 C CB    . VAL A 1 247 ? 70.515 21.656 21.456  1.00 59.61  ? 247 VAL A CB    1 
ATOM   2015 C CG1   . VAL A 1 247 ? 69.135 21.157 21.868  1.00 61.39  ? 247 VAL A CG1   1 
ATOM   2016 C CG2   . VAL A 1 247 ? 70.643 21.609 19.958  1.00 50.10  ? 247 VAL A CG2   1 
ATOM   2017 N N     . LEU A 1 248 ? 72.350 24.789 21.233  1.00 62.41  ? 248 LEU A N     1 
ATOM   2018 C CA    . LEU A 1 248 ? 73.676 25.310 20.917  1.00 69.40  ? 248 LEU A CA    1 
ATOM   2019 C C     . LEU A 1 248 ? 74.327 26.017 22.105  1.00 76.88  ? 248 LEU A C     1 
ATOM   2020 O O     . LEU A 1 248 ? 75.464 25.700 22.465  1.00 79.55  ? 248 LEU A O     1 
ATOM   2021 C CB    . LEU A 1 248 ? 73.597 26.260 19.721  1.00 57.51  ? 248 LEU A CB    1 
ATOM   2022 C CG    . LEU A 1 248 ? 73.082 25.644 18.424  1.00 54.74  ? 248 LEU A CG    1 
ATOM   2023 C CD1   . LEU A 1 248 ? 72.970 26.711 17.349  1.00 50.13  ? 248 LEU A CD1   1 
ATOM   2024 C CD2   . LEU A 1 248 ? 73.996 24.512 17.977  1.00 48.08  ? 248 LEU A CD2   1 
ATOM   2025 N N     . ASP A 1 249 ? 73.636 26.973 22.721  1.00 78.22  ? 249 ASP A N     1 
ATOM   2026 C CA    . ASP A 1 249 ? 74.227 27.735 23.825  1.00 92.09  ? 249 ASP A CA    1 
ATOM   2027 C C     . ASP A 1 249 ? 73.829 27.197 25.207  1.00 87.86  ? 249 ASP A C     1 
ATOM   2028 O O     . ASP A 1 249 ? 73.978 26.008 25.493  1.00 84.07  ? 249 ASP A O     1 
ATOM   2029 C CB    . ASP A 1 249 ? 73.851 29.218 23.711  1.00 88.03  ? 249 ASP A CB    1 
ATOM   2030 C CG    . ASP A 1 249 ? 72.363 29.474 23.916  1.00 100.77 ? 249 ASP A CG    1 
ATOM   2031 O OD1   . ASP A 1 249 ? 71.596 28.517 24.161  1.00 109.01 ? 249 ASP A OD1   1 
ATOM   2032 O OD2   . ASP A 1 249 ? 71.957 30.652 23.828  1.00 103.08 ? 249 ASP A OD2   1 
HETATM 2033 P P     . TMP B 2 .   ? 71.054 16.164 -17.000 1.00 108.36 ? 301 TMP A P     1 
HETATM 2034 O O1P   . TMP B 2 .   ? 69.831 16.983 -16.649 1.00 76.99  ? 301 TMP A O1P   1 
HETATM 2035 O O2P   . TMP B 2 .   ? 71.778 15.617 -15.785 1.00 70.55  ? 301 TMP A O2P   1 
HETATM 2036 O O3P   . TMP B 2 .   ? 71.981 16.871 -17.968 1.00 91.31  ? 301 TMP A O3P   1 
HETATM 2037 O "O5'" . TMP B 2 .   ? 70.471 14.869 -17.788 1.00 93.81  ? 301 TMP A "O5'" 1 
HETATM 2038 C "C5'" . TMP B 2 .   ? 71.367 14.041 -18.565 1.00 72.96  ? 301 TMP A "C5'" 1 
HETATM 2039 C "C4'" . TMP B 2 .   ? 70.603 12.859 -19.109 1.00 75.31  ? 301 TMP A "C4'" 1 
HETATM 2040 O "O4'" . TMP B 2 .   ? 70.258 11.965 -18.026 1.00 73.19  ? 301 TMP A "O4'" 1 
HETATM 2041 C "C3'" . TMP B 2 .   ? 69.290 13.192 -19.820 1.00 69.97  ? 301 TMP A "C3'" 1 
HETATM 2042 O "O3'" . TMP B 2 .   ? 69.121 12.325 -20.941 1.00 72.04  ? 301 TMP A "O3'" 1 
HETATM 2043 C "C2'" . TMP B 2 .   ? 68.241 12.896 -18.756 1.00 65.68  ? 301 TMP A "C2'" 1 
HETATM 2044 C "C1'" . TMP B 2 .   ? 68.862 11.719 -18.026 1.00 61.22  ? 301 TMP A "C1'" 1 
HETATM 2045 N N1    . TMP B 2 .   ? 68.422 11.563 -16.615 1.00 65.68  ? 301 TMP A N1    1 
HETATM 2046 C C2    . TMP B 2 .   ? 67.778 10.392 -16.272 1.00 50.27  ? 301 TMP A C2    1 
HETATM 2047 O O2    . TMP B 2 .   ? 67.487 9.526  -17.087 1.00 57.23  ? 301 TMP A O2    1 
HETATM 2048 N N3    . TMP B 2 .   ? 67.471 10.276 -14.935 1.00 51.94  ? 301 TMP A N3    1 
HETATM 2049 C C4    . TMP B 2 .   ? 67.729 11.199 -13.937 1.00 46.84  ? 301 TMP A C4    1 
HETATM 2050 O O4    . TMP B 2 .   ? 67.403 10.957 -12.772 1.00 44.57  ? 301 TMP A O4    1 
HETATM 2051 C C5    . TMP B 2 .   ? 68.395 12.410 -14.368 1.00 53.72  ? 301 TMP A C5    1 
HETATM 2052 C C5M   . TMP B 2 .   ? 68.712 13.466 -13.348 1.00 50.59  ? 301 TMP A C5M   1 
HETATM 2053 C C6    . TMP B 2 .   ? 68.702 12.532 -15.674 1.00 56.87  ? 301 TMP A C6    1 
HETATM 2054 P P     . PO4 C 3 .   ? 69.174 24.789 -10.662 1.00 40.09  ? 302 PO4 A P     1 
HETATM 2055 O O1    . PO4 C 3 .   ? 70.152 24.176 -9.688  1.00 40.44  ? 302 PO4 A O1    1 
HETATM 2056 O O2    . PO4 C 3 .   ? 69.556 24.387 -12.064 1.00 47.14  ? 302 PO4 A O2    1 
HETATM 2057 O O3    . PO4 C 3 .   ? 67.778 24.319 -10.365 1.00 38.75  ? 302 PO4 A O3    1 
HETATM 2058 O O4    . PO4 C 3 .   ? 69.181 26.290 -10.507 1.00 39.69  ? 302 PO4 A O4    1 
HETATM 2059 P P     . PO4 D 3 .   ? 72.725 31.354 -7.081  1.00 112.20 ? 303 PO4 A P     1 
HETATM 2060 O O1    . PO4 D 3 .   ? 73.957 30.690 -6.484  1.00 61.72  ? 303 PO4 A O1    1 
HETATM 2061 O O2    . PO4 D 3 .   ? 71.702 31.561 -5.992  1.00 83.66  ? 303 PO4 A O2    1 
HETATM 2062 O O3    . PO4 D 3 .   ? 73.100 32.696 -7.668  1.00 75.74  ? 303 PO4 A O3    1 
HETATM 2063 O O4    . PO4 D 3 .   ? 72.063 30.504 -8.146  1.00 64.50  ? 303 PO4 A O4    1 
HETATM 2064 P P     . PO4 E 3 .   ? 73.622 35.578 -0.350  1.00 92.17  ? 304 PO4 A P     1 
HETATM 2065 O O1    . PO4 E 3 .   ? 74.141 36.150 0.948   1.00 82.77  ? 304 PO4 A O1    1 
HETATM 2066 O O2    . PO4 E 3 .   ? 74.781 35.026 -1.147  1.00 78.21  ? 304 PO4 A O2    1 
HETATM 2067 O O3    . PO4 E 3 .   ? 72.642 34.474 -0.031  1.00 58.50  ? 304 PO4 A O3    1 
HETATM 2068 O O4    . PO4 E 3 .   ? 72.932 36.654 -1.158  1.00 84.36  ? 304 PO4 A O4    1 
HETATM 2069 O O     . HOH F 4 .   ? 78.436 22.268 1.457   1.00 49.18  ? 401 HOH A O     1 
HETATM 2070 O O     . HOH F 4 .   ? 80.082 -1.788 -15.102 1.00 53.97  ? 402 HOH A O     1 
HETATM 2071 O O     . HOH F 4 .   ? 73.389 7.698  -8.256  1.00 36.55  ? 403 HOH A O     1 
HETATM 2072 O O     . HOH F 4 .   ? 55.771 -2.299 -7.386  1.00 42.40  ? 404 HOH A O     1 
HETATM 2073 O O     . HOH F 4 .   ? 74.607 33.442 2.317   1.00 54.59  ? 405 HOH A O     1 
HETATM 2074 O O     . HOH F 4 .   ? 71.172 21.825 -9.381  1.00 44.46  ? 406 HOH A O     1 
HETATM 2075 O O     . HOH F 4 .   ? 51.467 4.277  -8.787  1.00 49.23  ? 407 HOH A O     1 
HETATM 2076 O O     . HOH F 4 .   ? 54.789 12.359 -13.066 1.00 44.61  ? 408 HOH A O     1 
HETATM 2077 O O     . HOH F 4 .   ? 57.855 25.330 -12.723 1.00 56.08  ? 409 HOH A O     1 
HETATM 2078 O O     . HOH F 4 .   ? 58.524 13.527 7.604   1.00 42.26  ? 410 HOH A O     1 
HETATM 2079 O O     . HOH F 4 .   ? 70.644 16.412 -13.334 1.00 57.52  ? 411 HOH A O     1 
HETATM 2080 O O     . HOH F 4 .   ? 75.123 4.060  -6.878  1.00 44.63  ? 412 HOH A O     1 
HETATM 2081 O O     . HOH F 4 .   ? 55.203 9.975  0.177   1.00 43.66  ? 413 HOH A O     1 
HETATM 2082 O O     . HOH F 4 .   ? 60.610 24.289 -12.088 1.00 44.37  ? 414 HOH A O     1 
HETATM 2083 O O     . HOH F 4 .   ? 73.842 -1.899 -17.069 1.00 49.09  ? 415 HOH A O     1 
HETATM 2084 O O     . HOH F 4 .   ? 71.113 17.371 -9.750  1.00 44.10  ? 416 HOH A O     1 
HETATM 2085 O O     . HOH F 4 .   ? 76.561 26.486 1.229   1.00 41.42  ? 417 HOH A O     1 
HETATM 2086 O O     . HOH F 4 .   ? 69.570 1.985  -8.634  1.00 38.02  ? 418 HOH A O     1 
HETATM 2087 O O     . HOH F 4 .   ? 66.688 29.423 -5.256  1.00 44.63  ? 419 HOH A O     1 
HETATM 2088 O O     . HOH F 4 .   ? 73.768 10.742 2.595   1.00 38.81  ? 420 HOH A O     1 
HETATM 2089 O O     . HOH F 4 .   ? 67.973 0.978  -12.093 1.00 38.84  ? 421 HOH A O     1 
HETATM 2090 O O     . HOH F 4 .   ? 75.235 32.961 -5.716  1.00 64.87  ? 422 HOH A O     1 
HETATM 2091 O O     . HOH F 4 .   ? 74.515 8.398  -11.524 1.00 42.70  ? 423 HOH A O     1 
HETATM 2092 O O     . HOH F 4 .   ? 66.383 12.401 -10.705 1.00 38.99  ? 424 HOH A O     1 
HETATM 2093 O O     . HOH F 4 .   ? 62.861 0.927  -18.748 1.00 50.58  ? 425 HOH A O     1 
HETATM 2094 O O     . HOH F 4 .   ? 61.936 22.018 -19.825 1.00 62.55  ? 426 HOH A O     1 
HETATM 2095 O O     . HOH F 4 .   ? 73.522 16.020 11.241  1.00 40.50  ? 427 HOH A O     1 
HETATM 2096 O O     . HOH F 4 .   ? 64.931 30.231 -7.345  1.00 46.38  ? 428 HOH A O     1 
HETATM 2097 O O     . HOH F 4 .   ? 67.413 5.292  -10.501 1.00 36.85  ? 429 HOH A O     1 
HETATM 2098 O O     . HOH F 4 .   ? 74.838 9.243  7.503   1.00 43.71  ? 430 HOH A O     1 
HETATM 2099 O O     . HOH F 4 .   ? 59.958 1.405  9.242   1.00 36.90  ? 431 HOH A O     1 
HETATM 2100 O O     . HOH F 4 .   ? 63.556 18.223 -11.404 1.00 42.27  ? 432 HOH A O     1 
HETATM 2101 O O     . HOH F 4 .   ? 67.868 -3.778 -6.530  1.00 34.26  ? 433 HOH A O     1 
HETATM 2102 O O     . HOH F 4 .   ? 77.687 17.741 13.874  1.00 59.89  ? 434 HOH A O     1 
HETATM 2103 O O     . HOH F 4 .   ? 76.472 11.623 -4.136  1.00 45.63  ? 435 HOH A O     1 
HETATM 2104 O O     . HOH F 4 .   ? 58.784 1.792  -11.212 1.00 37.37  ? 436 HOH A O     1 
HETATM 2105 O O     . HOH F 4 .   ? 66.096 25.472 15.416  1.00 48.77  ? 437 HOH A O     1 
HETATM 2106 O O     . HOH F 4 .   ? 68.503 21.054 -13.020 1.00 53.06  ? 438 HOH A O     1 
HETATM 2107 O O     . HOH F 4 .   ? 70.875 27.278 -8.466  1.00 41.41  ? 439 HOH A O     1 
HETATM 2108 O O     . HOH F 4 .   ? 72.575 27.162 7.348   1.00 40.48  ? 440 HOH A O     1 
HETATM 2109 O O     . HOH F 4 .   ? 69.191 30.465 -5.202  1.00 49.86  ? 441 HOH A O     1 
HETATM 2110 O O     . HOH F 4 .   ? 78.482 14.697 -2.254  1.00 43.81  ? 442 HOH A O     1 
HETATM 2111 O O     . HOH F 4 .   ? 67.695 27.950 1.732   1.00 42.97  ? 443 HOH A O     1 
HETATM 2112 O O     . HOH F 4 .   ? 64.901 21.015 -16.868 1.00 54.58  ? 444 HOH A O     1 
HETATM 2113 O O     . HOH F 4 .   ? 64.565 14.532 -11.481 1.00 41.27  ? 445 HOH A O     1 
HETATM 2114 O O     . HOH F 4 .   ? 79.226 17.852 3.590   1.00 50.67  ? 446 HOH A O     1 
HETATM 2115 O O     . HOH F 4 .   ? 54.704 8.230  2.157   1.00 43.99  ? 447 HOH A O     1 
HETATM 2116 O O     . HOH F 4 .   ? 78.316 24.195 5.723   1.00 42.94  ? 448 HOH A O     1 
HETATM 2117 O O     . HOH F 4 .   ? 53.130 23.931 -1.197  1.00 57.31  ? 449 HOH A O     1 
HETATM 2118 O O     . HOH F 4 .   ? 70.184 5.183  15.614  1.00 44.86  ? 450 HOH A O     1 
HETATM 2119 O O     . HOH F 4 .   ? 55.952 30.371 -17.483 1.00 64.50  ? 451 HOH A O     1 
HETATM 2120 O O     . HOH F 4 .   ? 65.942 19.149 -13.214 1.00 50.36  ? 452 HOH A O     1 
HETATM 2121 O O     . HOH F 4 .   ? 63.579 15.243 -13.825 1.00 42.22  ? 453 HOH A O     1 
HETATM 2122 O O     . HOH F 4 .   ? 55.453 0.861  2.954   1.00 41.56  ? 454 HOH A O     1 
HETATM 2123 O O     . HOH F 4 .   ? 54.959 8.131  8.842   1.00 45.66  ? 455 HOH A O     1 
HETATM 2124 O O     . HOH F 4 .   ? 73.913 10.411 -9.753  1.00 40.14  ? 456 HOH A O     1 
HETATM 2125 O O     . HOH F 4 .   ? 64.151 23.230 -19.065 1.00 57.96  ? 457 HOH A O     1 
HETATM 2126 O O     . HOH F 4 .   ? 73.984 23.182 -3.947  1.00 45.22  ? 458 HOH A O     1 
HETATM 2127 O O     . HOH F 4 .   ? 64.913 6.311  -11.396 1.00 52.09  ? 459 HOH A O     1 
HETATM 2128 O O     . HOH F 4 .   ? 76.501 6.247  -3.897  1.00 54.11  ? 460 HOH A O     1 
HETATM 2129 O O     . HOH F 4 .   ? 66.179 36.491 -8.327  1.00 47.64  ? 461 HOH A O     1 
HETATM 2130 O O     . HOH F 4 .   ? 54.700 6.612  -21.329 1.00 68.30  ? 462 HOH A O     1 
HETATM 2131 O O     . HOH F 4 .   ? 74.166 11.995 4.824   1.00 46.32  ? 463 HOH A O     1 
HETATM 2132 O O     . HOH F 4 .   ? 75.406 11.979 -6.454  1.00 48.82  ? 464 HOH A O     1 
HETATM 2133 O O     . HOH F 4 .   ? 55.127 24.264 -11.720 1.00 61.73  ? 465 HOH A O     1 
HETATM 2134 O O     . HOH F 4 .   ? 70.573 30.577 -12.376 1.00 54.43  ? 466 HOH A O     1 
HETATM 2135 O O     . HOH F 4 .   ? 78.070 17.647 0.925   1.00 38.34  ? 467 HOH A O     1 
HETATM 2136 O O     . HOH F 4 .   ? 64.080 -0.623 -11.891 1.00 39.91  ? 468 HOH A O     1 
HETATM 2137 O O     . HOH F 4 .   ? 64.208 4.068  10.598  1.00 33.27  ? 469 HOH A O     1 
HETATM 2138 O O     . HOH F 4 .   ? 65.471 4.130  -15.680 1.00 70.07  ? 470 HOH A O     1 
HETATM 2139 O O     . HOH F 4 .   ? 56.784 33.083 -18.592 1.00 60.74  ? 471 HOH A O     1 
HETATM 2140 O O     . HOH F 4 .   ? 62.816 38.865 0.358   1.00 67.56  ? 472 HOH A O     1 
HETATM 2141 O O     . HOH F 4 .   ? 48.400 11.701 3.580   1.00 61.45  ? 473 HOH A O     1 
HETATM 2142 O O     . HOH F 4 .   ? 73.449 28.646 -11.029 1.00 59.78  ? 474 HOH A O     1 
HETATM 2143 O O     . HOH F 4 .   ? 69.181 3.296  -11.326 1.00 43.00  ? 475 HOH A O     1 
HETATM 2144 O O     . HOH F 4 .   ? 71.789 36.814 -5.747  1.00 65.26  ? 476 HOH A O     1 
HETATM 2145 O O     . HOH F 4 .   ? 51.235 21.609 -2.671  1.00 66.45  ? 477 HOH A O     1 
HETATM 2146 O O     . HOH F 4 .   ? 54.589 32.689 -12.910 1.00 69.54  ? 478 HOH A O     1 
HETATM 2147 O O     . HOH F 4 .   ? 52.018 7.298  2.240   1.00 53.54  ? 479 HOH A O     1 
HETATM 2148 O O     . HOH F 4 .   ? 74.543 -0.972 -1.494  1.00 55.17  ? 480 HOH A O     1 
HETATM 2149 O O     . HOH F 4 .   ? 74.106 1.485  -6.754  1.00 48.39  ? 481 HOH A O     1 
HETATM 2150 O O     . HOH F 4 .   ? 54.166 -1.223 -5.501  1.00 47.44  ? 482 HOH A O     1 
HETATM 2151 O O     . HOH F 4 .   ? 75.571 22.667 -1.705  1.00 47.78  ? 483 HOH A O     1 
HETATM 2152 O O     . HOH F 4 .   ? 62.155 17.667 -13.904 1.00 50.13  ? 484 HOH A O     1 
HETATM 2153 O O     . HOH F 4 .   ? 49.982 1.805  -8.054  1.00 56.71  ? 485 HOH A O     1 
HETATM 2154 O O     . HOH F 4 .   ? 78.294 20.004 -0.054  1.00 45.99  ? 486 HOH A O     1 
HETATM 2155 O O     . HOH F 4 .   ? 77.157 24.328 -0.133  1.00 44.62  ? 487 HOH A O     1 
HETATM 2156 O O     . HOH F 4 .   ? 53.362 -2.996 -8.558  1.00 48.72  ? 488 HOH A 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     . SER A 11  ? 1.0057 0.9271 1.3620 0.2351  0.1085  0.0185  11  SER A N     
2    C CA    . SER A 11  ? 1.1175 1.0140 1.4302 0.2263  0.0991  0.0142  11  SER A CA    
3    C C     . SER A 11  ? 1.1875 1.0750 1.5128 0.2273  0.0785  0.0260  11  SER A C     
4    O O     . SER A 11  ? 1.2057 1.1101 1.5641 0.2305  0.0647  0.0401  11  SER A O     
5    C CB    . SER A 11  ? 1.0996 1.0044 1.3739 0.2108  0.0911  0.0138  11  SER A CB    
6    O OG    . SER A 11  ? 1.0913 0.9968 1.3446 0.2091  0.1096  0.0021  11  SER A OG    
7    N N     . ILE A 12  ? 1.1858 1.0450 1.4834 0.2240  0.0758  0.0205  12  ILE A N     
8    C CA    . ILE A 12  ? 1.0686 0.9136 1.3723 0.2241  0.0583  0.0310  12  ILE A CA    
9    C C     . ILE A 12  ? 1.0074 0.8462 1.2716 0.2080  0.0440  0.0337  12  ILE A C     
10   O O     . ILE A 12  ? 1.0594 0.8990 1.2917 0.1985  0.0491  0.0244  12  ILE A O     
11   C CB    . ILE A 12  ? 0.9012 0.7158 1.2113 0.2342  0.0677  0.0233  12  ILE A CB    
12   C CG1   . ILE A 12  ? 0.8953 0.6867 1.1632 0.2278  0.0801  0.0054  12  ILE A CG1   
13   C CG2   . ILE A 12  ? 0.8310 0.6520 1.1859 0.2513  0.0826  0.0215  12  ILE A CG2   
14   C CD1   . ILE A 12  ? 0.7869 0.5436 1.0521 0.2338  0.0853  -0.0024 12  ILE A CD1   
15   N N     . GLU A 13  ? 0.9402 0.7721 1.2075 0.2050  0.0259  0.0469  13  GLU A N     
16   C CA    . GLU A 13  ? 1.0572 0.8778 1.2896 0.1907  0.0150  0.0491  13  GLU A CA    
17   C C     . GLU A 13  ? 1.0410 0.8317 1.2521 0.1890  0.0233  0.0365  13  GLU A C     
18   O O     . GLU A 13  ? 1.0380 0.8106 1.2636 0.1998  0.0319  0.0310  13  GLU A O     
19   C CB    . GLU A 13  ? 1.1589 0.9766 1.3982 0.1881  -0.0048 0.0672  13  GLU A CB    
20   C CG    . GLU A 13  ? 1.1958 1.0047 1.4005 0.1723  -0.0147 0.0711  13  GLU A CG    
21   C CD    . GLU A 13  ? 1.2942 1.0886 1.5005 0.1707  -0.0308 0.0875  13  GLU A CD    
22   O OE1   . GLU A 13  ? 1.3132 1.1052 1.5482 0.1821  -0.0369 0.0966  13  GLU A OE1   
23   O OE2   . GLU A 13  ? 1.2029 0.9877 1.3820 0.1580  -0.0372 0.0915  13  GLU A OE2   
24   N N     . LEU A 14  ? 1.0637 0.8490 1.2416 0.1753  0.0206  0.0316  14  LEU A N     
25   C CA    . LEU A 14  ? 0.9924 0.7511 1.1483 0.1712  0.0265  0.0188  14  LEU A CA    
26   C C     . LEU A 14  ? 0.9835 0.7276 1.1247 0.1597  0.0140  0.0262  14  LEU A C     
27   O O     . LEU A 14  ? 0.9548 0.7122 1.0916 0.1515  0.0031  0.0380  14  LEU A O     
28   C CB    . LEU A 14  ? 0.9131 0.6773 1.0434 0.1648  0.0356  0.0040  14  LEU A CB    
29   C CG    . LEU A 14  ? 0.9531 0.7140 1.0822 0.1738  0.0533  -0.0107 14  LEU A CG    
30   C CD1   . LEU A 14  ? 0.8558 0.6248 1.0197 0.1894  0.0623  -0.0070 14  LEU A CD1   
31   C CD2   . LEU A 14  ? 0.8310 0.6096 0.9392 0.1666  0.0567  -0.0166 14  LEU A CD2   
32   N N     . ASP A 15  ? 0.9502 0.6655 1.0833 0.1587  0.0166  0.0189  15  ASP A N     
33   C CA    . ASP A 15  ? 0.9268 0.6272 1.0442 0.1458  0.0075  0.0235  15  ASP A CA    
34   C C     . ASP A 15  ? 0.8485 0.5591 0.9415 0.1319  0.0072  0.0156  15  ASP A C     
35   O O     . ASP A 15  ? 0.9226 0.6484 1.0084 0.1326  0.0132  0.0065  15  ASP A O     
36   C CB    . ASP A 15  ? 1.0464 0.7124 1.1648 0.1485  0.0103  0.0177  15  ASP A CB    
37   C CG    . ASP A 15  ? 0.9310 0.5824 1.0335 0.1475  0.0207  -0.0029 15  ASP A CG    
38   O OD1   . ASP A 15  ? 0.9760 0.6429 1.0657 0.1455  0.0259  -0.0126 15  ASP A OD1   
39   O OD2   . ASP A 15  ? 0.9433 0.5651 1.0445 0.1486  0.0230  -0.0095 15  ASP A OD2   
40   N N     . LYS A 16  ? 0.8714 0.5727 0.9526 0.1190  0.0004  0.0195  16  LYS A N     
41   C CA    . LYS A 16  ? 0.9011 0.6161 0.9653 0.1058  -0.0016 0.0152  16  LYS A CA    
42   C C     . LYS A 16  ? 0.8576 0.5668 0.9084 0.1040  0.0042  -0.0031 16  LYS A C     
43   O O     . LYS A 16  ? 0.7606 0.4880 0.8014 0.0997  0.0046  -0.0082 16  LYS A O     
44   C CB    . LYS A 16  ? 1.0072 0.7124 1.0653 0.0926  -0.0080 0.0231  16  LYS A CB    
45   C CG    . LYS A 16  ? 1.0868 0.8107 1.1339 0.0796  -0.0101 0.0223  16  LYS A CG    
46   C CD    . LYS A 16  ? 1.2439 0.9571 1.2874 0.0665  -0.0135 0.0299  16  LYS A CD    
47   C CE    . LYS A 16  ? 1.2812 1.0121 1.3179 0.0541  -0.0138 0.0268  16  LYS A CE    
48   N NZ    . LYS A 16  ? 1.3006 1.0209 1.3362 0.0407  -0.0142 0.0330  16  LYS A NZ    
49   N N     . LYS A 17  ? 0.8854 0.5677 0.9340 0.1070  0.0079  -0.0132 17  LYS A N     
50   C CA    . LYS A 17  ? 0.8602 0.5333 0.8911 0.1042  0.0116  -0.0311 17  LYS A CA    
51   C C     . LYS A 17  ? 0.8015 0.4874 0.8279 0.1140  0.0206  -0.0383 17  LYS A C     
52   O O     . LYS A 17  ? 0.7361 0.4302 0.7450 0.1092  0.0209  -0.0472 17  LYS A O     
53   C CB    . LYS A 17  ? 0.8520 0.4903 0.8800 0.1052  0.0137  -0.0409 17  LYS A CB    
54   C CG    . LYS A 17  ? 0.9336 0.5565 0.9636 0.0930  0.0056  -0.0362 17  LYS A CG    
55   C CD    . LYS A 17  ? 0.9571 0.5445 0.9829 0.0932  0.0076  -0.0482 17  LYS A CD    
56   C CE    . LYS A 17  ? 0.9692 0.5415 0.9972 0.0790  -0.0002 -0.0446 17  LYS A CE    
57   N NZ    . LYS A 17  ? 1.0818 0.6172 1.1072 0.0787  0.0011  -0.0558 17  LYS A NZ    
58   N N     . MET A 18  ? 0.8028 0.4910 0.8462 0.1277  0.0279  -0.0338 18  MET A N     
59   C CA    . MET A 18  ? 0.7981 0.4989 0.8403 0.1369  0.0388  -0.0400 18  MET A CA    
60   C C     . MET A 18  ? 0.7169 0.4505 0.7608 0.1333  0.0352  -0.0314 18  MET A C     
61   O O     . MET A 18  ? 0.7450 0.4892 0.7763 0.1337  0.0411  -0.0385 18  MET A O     
62   C CB    . MET A 18  ? 0.7650 0.4598 0.8309 0.1527  0.0484  -0.0378 18  MET A CB    
63   C CG    . MET A 18  ? 0.8844 0.5658 0.9410 0.1618  0.0648  -0.0539 18  MET A CG    
64   S SD    . MET A 18  ? 0.8772 0.5204 0.9010 0.1552  0.0668  -0.0738 18  MET A SD    
65   C CE    . MET A 18  ? 0.8975 0.5192 0.9393 0.1542  0.0576  -0.0660 18  MET A CE    
66   N N     . TYR A 19  ? 0.7176 0.4657 0.7749 0.1296  0.0257  -0.0162 19  TYR A N     
67   C CA    . TYR A 19  ? 0.6590 0.4352 0.7147 0.1240  0.0212  -0.0090 19  TYR A CA    
68   C C     . TYR A 19  ? 0.6756 0.4544 0.7085 0.1127  0.0186  -0.0178 19  TYR A C     
69   O O     . TYR A 19  ? 0.5887 0.3848 0.6145 0.1120  0.0210  -0.0200 19  TYR A O     
70   C CB    . TYR A 19  ? 0.6730 0.4578 0.7393 0.1192  0.0107  0.0071  19  TYR A CB    
71   C CG    . TYR A 19  ? 0.6814 0.4881 0.7389 0.1090  0.0053  0.0116  19  TYR A CG    
72   C CD1   . TYR A 19  ? 0.6530 0.4839 0.7168 0.1121  0.0062  0.0159  19  TYR A CD1   
73   C CD2   . TYR A 19  ? 0.6816 0.4844 0.7267 0.0963  -0.0001 0.0110  19  TYR A CD2   
74   C CE1   . TYR A 19  ? 0.6025 0.4513 0.6582 0.1031  0.0018  0.0193  19  TYR A CE1   
75   C CE2   . TYR A 19  ? 0.7251 0.5470 0.7643 0.0878  -0.0036 0.0144  19  TYR A CE2   
76   C CZ    . TYR A 19  ? 0.6798 0.5239 0.7233 0.0914  -0.0027 0.0183  19  TYR A CZ    
77   O OH    . TYR A 19  ? 0.7701 0.6312 0.8077 0.0831  -0.0057 0.0210  19  TYR A OH    
78   N N     . LYS A 20  ? 0.6734 0.4351 0.6965 0.1037  0.0131  -0.0222 20  LYS A N     
79   C CA    . LYS A 20  ? 0.6745 0.4396 0.6807 0.0928  0.0084  -0.0297 20  LYS A CA    
80   C C     . LYS A 20  ? 0.6479 0.4076 0.6358 0.0965  0.0144  -0.0434 20  LYS A C     
81   O O     . LYS A 20  ? 0.6303 0.4044 0.6072 0.0924  0.0125  -0.0457 20  LYS A O     
82   C CB    . LYS A 20  ? 0.7504 0.4969 0.7541 0.0826  0.0015  -0.0323 20  LYS A CB    
83   C CG    . LYS A 20  ? 0.9689 0.7232 0.9637 0.0699  -0.0060 -0.0366 20  LYS A CG    
84   C CD    . LYS A 20  ? 1.1581 0.8962 1.1571 0.0592  -0.0121 -0.0374 20  LYS A CD    
85   C CE    . LYS A 20  ? 1.1990 0.9461 1.1949 0.0468  -0.0200 -0.0421 20  LYS A CE    
86   N NZ    . LYS A 20  ? 1.3396 1.0722 1.3436 0.0355  -0.0254 -0.0432 20  LYS A NZ    
87   N N     . LYS A 21  ? 0.6669 0.4047 0.6502 0.1046  0.0224  -0.0525 21  LYS A N     
88   C CA    . LYS A 21  ? 0.6714 0.4003 0.6322 0.1079  0.0299  -0.0661 21  LYS A CA    
89   C C     . LYS A 21  ? 0.6544 0.4055 0.6172 0.1148  0.0385  -0.0622 21  LYS A C     
90   O O     . LYS A 21  ? 0.6747 0.4305 0.6172 0.1118  0.0394  -0.0678 21  LYS A O     
91   C CB    . LYS A 21  ? 0.7082 0.4071 0.6637 0.1157  0.0391  -0.0769 21  LYS A CB    
92   C CG    . LYS A 21  ? 0.7603 0.4331 0.7054 0.1072  0.0307  -0.0852 21  LYS A CG    
93   C CD    . LYS A 21  ? 0.9225 0.5691 0.8764 0.1156  0.0383  -0.0894 21  LYS A CD    
94   C CE    . LYS A 21  ? 0.9149 0.5289 0.8417 0.1145  0.0417  -0.1081 21  LYS A CE    
95   N NZ    . LYS A 21  ? 0.9387 0.5412 0.8512 0.0995  0.0266  -0.1141 21  LYS A NZ    
96   N N     . LYS A 22  ? 0.6407 0.4051 0.6287 0.1236  0.0441  -0.0521 22  LYS A N     
97   C CA    . LYS A 22  ? 0.6246 0.4109 0.6195 0.1296  0.0524  -0.0479 22  LYS A CA    
98   C C     . LYS A 22  ? 0.5955 0.4053 0.5862 0.1207  0.0436  -0.0412 22  LYS A C     
99   O O     . LYS A 22  ? 0.6313 0.4517 0.6113 0.1210  0.0487  -0.0433 22  LYS A O     
100  C CB    . LYS A 22  ? 0.6621 0.4587 0.6897 0.1400  0.0569  -0.0376 22  LYS A CB    
101  C CG    . LYS A 22  ? 0.6458 0.4642 0.6863 0.1470  0.0668  -0.0338 22  LYS A CG    
102  C CD    . LYS A 22  ? 0.8487 0.6713 0.9241 0.1591  0.0723  -0.0268 22  LYS A CD    
103  C CE    . LYS A 22  ? 0.9161 0.7581 1.0088 0.1670  0.0851  -0.0250 22  LYS A CE    
104  N NZ    . LYS A 22  ? 0.9867 0.8345 1.1191 0.1790  0.0884  -0.0175 22  LYS A NZ    
105  N N     . LEU A 23  ? 0.5785 0.3952 0.5770 0.1126  0.0313  -0.0329 23  LEU A N     
106  C CA    . LEU A 23  ? 0.5709 0.4074 0.5659 0.1037  0.0235  -0.0276 23  LEU A CA    
107  C C     . LEU A 23  ? 0.5826 0.4133 0.5529 0.0972  0.0208  -0.0376 23  LEU A C     
108  O O     . LEU A 23  ? 0.5769 0.4228 0.5408 0.0951  0.0204  -0.0363 23  LEU A O     
109  C CB    . LEU A 23  ? 0.5713 0.4107 0.5765 0.0959  0.0132  -0.0189 23  LEU A CB    
110  C CG    . LEU A 23  ? 0.6676 0.5255 0.6711 0.0863  0.0061  -0.0139 23  LEU A CG    
111  C CD1   . LEU A 23  ? 0.5784 0.4584 0.5919 0.0901  0.0085  -0.0054 23  LEU A CD1   
112  C CD2   . LEU A 23  ? 0.5517 0.4062 0.5608 0.0773  -0.0013 -0.0081 23  LEU A CD2   
113  N N     . LYS A 24  ? 0.6081 0.4160 0.5645 0.0938  0.0176  -0.0475 24  LYS A N     
114  C CA    . LYS A 24  ? 0.6695 0.4701 0.6019 0.0870  0.0118  -0.0569 24  LYS A CA    
115  C C     . LYS A 24  ? 0.6305 0.4288 0.5426 0.0930  0.0213  -0.0630 24  LYS A C     
116  O O     . LYS A 24  ? 0.6336 0.4392 0.5308 0.0887  0.0170  -0.0639 24  LYS A O     
117  C CB    . LYS A 24  ? 0.6837 0.4580 0.6056 0.0822  0.0060  -0.0670 24  LYS A CB    
118  C CG    . LYS A 24  ? 0.7917 0.5684 0.7297 0.0726  -0.0048 -0.0618 24  LYS A CG    
119  C CD    . LYS A 24  ? 0.8243 0.5733 0.7572 0.0692  -0.0083 -0.0708 24  LYS A CD    
120  C CE    . LYS A 24  ? 0.8894 0.6413 0.8394 0.0585  -0.0177 -0.0652 24  LYS A CE    
121  N NZ    . LYS A 24  ? 1.2629 0.9889 1.2068 0.0520  -0.0240 -0.0754 24  LYS A NZ    
122  N N     . VAL A 25  ? 0.6573 0.4448 0.5690 0.1030  0.0351  -0.0668 25  VAL A N     
123  C CA    . VAL A 25  ? 0.6450 0.4300 0.5375 0.1086  0.0474  -0.0721 25  VAL A CA    
124  C C     . VAL A 25  ? 0.6149 0.4283 0.5195 0.1093  0.0497  -0.0615 25  VAL A C     
125  O O     . VAL A 25  ? 0.6281 0.4444 0.5128 0.1071  0.0509  -0.0631 25  VAL A O     
126  C CB    . VAL A 25  ? 0.7117 0.4805 0.6061 0.1198  0.0645  -0.0784 25  VAL A CB    
127  C CG1   . VAL A 25  ? 0.6866 0.4541 0.5619 0.1251  0.0802  -0.0829 25  VAL A CG1   
128  C CG2   . VAL A 25  ? 0.7049 0.4420 0.5830 0.1184  0.0623  -0.0906 25  VAL A CG2   
129  N N     . LEU A 26  ? 0.6176 0.4507 0.5537 0.1122  0.0496  -0.0503 26  LEU A N     
130  C CA    . LEU A 26  ? 0.5697 0.4284 0.5177 0.1126  0.0516  -0.0410 26  LEU A CA    
131  C C     . LEU A 26  ? 0.5699 0.4388 0.5074 0.1027  0.0394  -0.0384 26  LEU A C     
132  O O     . LEU A 26  ? 0.5837 0.4644 0.5153 0.1020  0.0422  -0.0358 26  LEU A O     
133  C CB    . LEU A 26  ? 0.5876 0.4633 0.5694 0.1166  0.0510  -0.0298 26  LEU A CB    
134  C CG    . LEU A 26  ? 0.6210 0.4926 0.6210 0.1282  0.0640  -0.0301 26  LEU A CG    
135  C CD1   . LEU A 26  ? 0.5507 0.4354 0.5830 0.1312  0.0582  -0.0185 26  LEU A CD1   
136  C CD2   . LEU A 26  ? 0.5774 0.4567 0.5766 0.1340  0.0793  -0.0318 26  LEU A CD2   
137  N N     . GLN A 27  ? 0.5419 0.4061 0.4784 0.0950  0.0266  -0.0392 27  GLN A N     
138  C CA    . GLN A 27  ? 0.5605 0.4353 0.4921 0.0862  0.0154  -0.0368 27  GLN A CA    
139  C C     . GLN A 27  ? 0.6175 0.4802 0.5197 0.0838  0.0132  -0.0450 27  GLN A C     
140  O O     . GLN A 27  ? 0.5465 0.4202 0.4433 0.0802  0.0085  -0.0419 27  GLN A O     
141  C CB    . GLN A 27  ? 0.5193 0.3927 0.4613 0.0784  0.0040  -0.0354 27  GLN A CB    
142  C CG    . GLN A 27  ? 0.5502 0.4356 0.5163 0.0787  0.0042  -0.0255 27  GLN A CG    
143  C CD    . GLN A 27  ? 0.6119 0.4904 0.5851 0.0711  -0.0039 -0.0250 27  GLN A CD    
144  O OE1   . GLN A 27  ? 0.6037 0.4639 0.5687 0.0687  -0.0070 -0.0328 27  GLN A OE1   
145  N NE2   . GLN A 27  ? 0.4832 0.3752 0.4709 0.0666  -0.0067 -0.0161 27  GLN A NE2   
146  N N     . TYR A 28  ? 0.5845 0.4228 0.4659 0.0857  0.0159  -0.0555 28  TYR A N     
147  C CA    . TYR A 28  ? 0.6094 0.4328 0.4568 0.0840  0.0146  -0.0632 28  TYR A CA    
148  C C     . TYR A 28  ? 0.6644 0.4956 0.5031 0.0894  0.0275  -0.0597 28  TYR A C     
149  O O     . TYR A 28  ? 0.6337 0.4665 0.4543 0.0860  0.0231  -0.0586 28  TYR A O     
150  C CB    . TYR A 28  ? 0.6499 0.4429 0.4740 0.0854  0.0172  -0.0759 28  TYR A CB    
151  C CG    . TYR A 28  ? 0.7526 0.5244 0.5344 0.0842  0.0175  -0.0850 28  TYR A CG    
152  C CD1   . TYR A 28  ? 0.7196 0.4830 0.4818 0.0753  -0.0007 -0.0887 28  TYR A CD1   
153  C CD2   . TYR A 28  ? 0.8470 0.6055 0.6080 0.0918  0.0359  -0.0900 28  TYR A CD2   
154  C CE1   . TYR A 28  ? 0.7990 0.5396 0.5177 0.0737  -0.0026 -0.0967 28  TYR A CE1   
155  C CE2   . TYR A 28  ? 0.8483 0.5835 0.5647 0.0901  0.0371  -0.0984 28  TYR A CE2   
156  C CZ    . TYR A 28  ? 0.8755 0.6010 0.5688 0.0809  0.0168  -0.1015 28  TYR A CZ    
157  O OH    . TYR A 28  ? 0.9489 0.6487 0.5937 0.0788  0.0160  -0.1092 28  TYR A OH    
158  N N     . GLU A 29  ? 0.6385 0.4748 0.4924 0.0978  0.0434  -0.0573 29  GLU A N     
159  C CA    . GLU A 29  ? 0.6089 0.4543 0.4600 0.1026  0.0574  -0.0535 29  GLU A CA    
160  C C     . GLU A 29  ? 0.6208 0.4917 0.4875 0.0985  0.0508  -0.0426 29  GLU A C     
161  O O     . GLU A 29  ? 0.6150 0.4895 0.4689 0.0983  0.0559  -0.0400 29  GLU A O     
162  C CB    . GLU A 29  ? 0.6337 0.4824 0.5066 0.1124  0.0746  -0.0525 29  GLU A CB    
163  C CG    . GLU A 29  ? 0.7181 0.5391 0.5713 0.1181  0.0868  -0.0646 29  GLU A CG    
164  C CD    . GLU A 29  ? 0.7501 0.5757 0.6319 0.1287  0.1035  -0.0633 29  GLU A CD    
165  O OE1   . GLU A 29  ? 0.8664 0.7128 0.7706 0.1325  0.1125  -0.0553 29  GLU A OE1   
166  O OE2   . GLU A 29  ? 0.9364 0.7446 0.8204 0.1331  0.1069  -0.0702 29  GLU A OE2   
167  N N     . MET A 30  ? 0.5709 0.4574 0.4634 0.0950  0.0401  -0.0362 30  MET A N     
168  C CA    . MET A 30  ? 0.5229 0.4311 0.4286 0.0907  0.0339  -0.0272 30  MET A CA    
169  C C     . MET A 30  ? 0.5755 0.4794 0.4606 0.0840  0.0225  -0.0289 30  MET A C     
170  O O     . MET A 30  ? 0.5149 0.4289 0.3976 0.0825  0.0225  -0.0238 30  MET A O     
171  C CB    . MET A 30  ? 0.4963 0.4187 0.4300 0.0882  0.0263  -0.0209 30  MET A CB    
172  C CG    . MET A 30  ? 0.5869 0.5306 0.5346 0.0845  0.0224  -0.0123 30  MET A CG    
173  S SD    . MET A 30  ? 0.5700 0.5280 0.5291 0.0903  0.0358  -0.0063 30  MET A SD    
174  C CE    . MET A 30  ? 0.5943 0.5665 0.5522 0.0840  0.0298  -0.0007 30  MET A CE    
175  N N     . LEU A 31  ? 0.5867 0.4756 0.4590 0.0797  0.0116  -0.0357 31  LEU A N     
176  C CA    . LEU A 31  ? 0.5761 0.4593 0.4295 0.0737  -0.0013 -0.0376 31  LEU A CA    
177  C C     . LEU A 31  ? 0.6336 0.5044 0.4550 0.0762  0.0054  -0.0396 31  LEU A C     
178  O O     . LEU A 31  ? 0.6313 0.5070 0.4443 0.0735  -0.0001 -0.0350 31  LEU A O     
179  C CB    . LEU A 31  ? 0.5870 0.4542 0.4327 0.0688  -0.0139 -0.0456 31  LEU A CB    
180  C CG    . LEU A 31  ? 0.6705 0.5250 0.4914 0.0633  -0.0287 -0.0499 31  LEU A CG    
181  C CD1   . LEU A 31  ? 0.6328 0.5064 0.4695 0.0591  -0.0392 -0.0421 31  LEU A CD1   
182  C CD2   . LEU A 31  ? 0.6693 0.5071 0.4854 0.0583  -0.0406 -0.0587 31  LEU A CD2   
183  N N     . ASN A 32  ? 0.6587 0.5121 0.4615 0.0814  0.0185  -0.0461 32  ASN A N     
184  C CA    . ASN A 32  ? 0.6898 0.5291 0.4592 0.0836  0.0283  -0.0481 32  ASN A CA    
185  C C     . ASN A 32  ? 0.6415 0.4998 0.4237 0.0859  0.0390  -0.0383 32  ASN A C     
186  O O     . ASN A 32  ? 0.6778 0.5316 0.4379 0.0840  0.0387  -0.0352 32  ASN A O     
187  C CB    . ASN A 32  ? 0.7096 0.5275 0.4603 0.0894  0.0444  -0.0573 32  ASN A CB    
188  C CG    . ASN A 32  ? 0.8878 0.6891 0.6007 0.0912  0.0572  -0.0594 32  ASN A CG    
189  O OD1   . ASN A 32  ? 0.8456 0.6261 0.5199 0.0866  0.0478  -0.0639 32  ASN A OD1   
190  N ND2   . ASN A 32  ? 0.8310 0.6415 0.5552 0.0972  0.0781  -0.0554 32  ASN A ND2   
191  N N     . ALA A 33  ? 0.6300 0.5082 0.4472 0.0898  0.0478  -0.0330 33  ALA A N     
192  C CA    . ALA A 33  ? 0.6336 0.5309 0.4673 0.0914  0.0570  -0.0239 33  ALA A CA    
193  C C     . ALA A 33  ? 0.6060 0.5158 0.4443 0.0853  0.0433  -0.0169 33  ALA A C     
194  O O     . ALA A 33  ? 0.6710 0.5853 0.5035 0.0846  0.0482  -0.0112 33  ALA A O     
195  C CB    . ALA A 33  ? 0.6073 0.5230 0.4794 0.0958  0.0644  -0.0198 33  ALA A CB    
196  N N     . GLN A 34  ? 0.5267 0.4415 0.3765 0.0808  0.0271  -0.0172 34  GLN A N     
197  C CA    . GLN A 34  ? 0.5441 0.4691 0.3994 0.0755  0.0144  -0.0116 34  GLN A CA    
198  C C     . GLN A 34  ? 0.6178 0.5268 0.4398 0.0733  0.0081  -0.0126 34  GLN A C     
199  O O     . GLN A 34  ? 0.5699 0.4847 0.3900 0.0718  0.0067  -0.0060 34  GLN A O     
200  C CB    . GLN A 34  ? 0.5424 0.4738 0.4163 0.0712  0.0003  -0.0128 34  GLN A CB    
201  C CG    . GLN A 34  ? 0.6431 0.5851 0.5261 0.0663  -0.0117 -0.0079 34  GLN A CG    
202  C CD    . GLN A 34  ? 0.7460 0.6815 0.6280 0.0615  -0.0280 -0.0123 34  GLN A CD    
203  O OE1   . GLN A 34  ? 0.7322 0.6498 0.5932 0.0610  -0.0330 -0.0190 34  GLN A OE1   
204  N NE2   . GLN A 34  ? 0.8369 0.7867 0.7429 0.0577  -0.0359 -0.0089 34  GLN A NE2   
205  N N     . GLN A 35  ? 0.6154 0.5023 0.4095 0.0726  0.0031  -0.0207 35  GLN A N     
206  C CA    . GLN A 35  ? 0.6045 0.4729 0.3620 0.0701  -0.0047 -0.0213 35  GLN A CA    
207  C C     . GLN A 35  ? 0.6571 0.5188 0.3927 0.0732  0.0121  -0.0175 35  GLN A C     
208  O O     . GLN A 35  ? 0.7279 0.5848 0.4457 0.0710  0.0073  -0.0119 35  GLN A O     
209  C CB    . GLN A 35  ? 0.6396 0.4831 0.3685 0.0682  -0.0136 -0.0317 35  GLN A CB    
210  C CG    . GLN A 35  ? 0.7257 0.5750 0.4757 0.0634  -0.0325 -0.0345 35  GLN A CG    
211  C CD    . GLN A 35  ? 0.8265 0.6875 0.5891 0.0590  -0.0498 -0.0278 35  GLN A CD    
212  O OE1   . GLN A 35  ? 0.8100 0.6587 0.5463 0.0572  -0.0596 -0.0260 35  GLN A OE1   
213  N NE2   . GLN A 35  ? 0.6431 0.5268 0.4455 0.0575  -0.0532 -0.0239 35  GLN A NE2   
214  N N     . PHE A 36  ? 0.6669 0.5288 0.4065 0.0783  0.0323  -0.0198 36  PHE A N     
215  C CA    . PHE A 36  ? 0.6536 0.5119 0.3793 0.0812  0.0517  -0.0159 36  PHE A CA    
216  C C     . PHE A 36  ? 0.6633 0.5432 0.4129 0.0797  0.0526  -0.0047 36  PHE A C     
217  O O     . PHE A 36  ? 0.7052 0.5781 0.4344 0.0784  0.0578  0.0007  36  PHE A O     
218  C CB    . PHE A 36  ? 0.7065 0.5659 0.4442 0.0875  0.0728  -0.0204 36  PHE A CB    
219  C CG    . PHE A 36  ? 0.8389 0.6984 0.5712 0.0905  0.0954  -0.0163 36  PHE A CG    
220  C CD1   . PHE A 36  ? 0.8208 0.6537 0.5081 0.0908  0.1073  -0.0203 36  PHE A CD1   
221  C CD2   . PHE A 36  ? 0.8239 0.7088 0.5953 0.0924  0.1050  -0.0086 36  PHE A CD2   
222  C CE1   . PHE A 36  ? 0.9154 0.7479 0.5987 0.0930  0.1306  -0.0164 36  PHE A CE1   
223  C CE2   . PHE A 36  ? 0.7886 0.6746 0.5591 0.0944  0.1265  -0.0048 36  PHE A CE2   
224  C CZ    . PHE A 36  ? 0.8146 0.6748 0.5420 0.0948  0.1403  -0.0085 36  PHE A CZ    
225  N N     . LEU A 37  ? 0.6325 0.5369 0.4236 0.0797  0.0486  -0.0012 37  LEU A N     
226  C CA    . LEU A 37  ? 0.6410 0.5647 0.4551 0.0779  0.0494  0.0082  37  LEU A CA    
227  C C     . LEU A 37  ? 0.6645 0.5847 0.4668 0.0732  0.0333  0.0126  37  LEU A C     
228  O O     . LEU A 37  ? 0.6485 0.5723 0.4503 0.0717  0.0364  0.0202  37  LEU A O     
229  C CB    . LEU A 37  ? 0.5496 0.4969 0.4057 0.0782  0.0470  0.0100  37  LEU A CB    
230  C CG    . LEU A 37  ? 0.5745 0.5292 0.4503 0.0832  0.0615  0.0083  37  LEU A CG    
231  C CD1   . LEU A 37  ? 0.6021 0.5755 0.5125 0.0826  0.0545  0.0103  37  LEU A CD1   
232  C CD2   . LEU A 37  ? 0.6461 0.6059 0.5264 0.0853  0.0793  0.0132  37  LEU A CD2   
233  N N     . LEU A 38  ? 0.6048 0.5180 0.4003 0.0709  0.0158  0.0083  38  LEU A N     
234  C CA    . LEU A 38  ? 0.6117 0.5208 0.3984 0.0672  -0.0011 0.0123  38  LEU A CA    
235  C C     . LEU A 38  ? 0.6854 0.5717 0.4295 0.0668  0.0004  0.0147  38  LEU A C     
236  O O     . LEU A 38  ? 0.6381 0.5242 0.3777 0.0652  -0.0031 0.0228  38  LEU A O     
237  C CB    . LEU A 38  ? 0.6073 0.5139 0.3987 0.0647  -0.0197 0.0065  38  LEU A CB    
238  C CG    . LEU A 38  ? 0.7449 0.6490 0.5341 0.0613  -0.0396 0.0101  38  LEU A CG    
239  C CD1   . LEU A 38  ? 0.6689 0.5943 0.4920 0.0606  -0.0403 0.0173  38  LEU A CD1   
240  C CD2   . LEU A 38  ? 0.6927 0.5923 0.4857 0.0584  -0.0569 0.0033  38  LEU A CD2   
241  N N     . LYS A 39  ? 0.7035 0.5684 0.4140 0.0680  0.0061  0.0078  39  LYS A N     
242  C CA    . LYS A 39  ? 0.7658 0.6046 0.4285 0.0671  0.0086  0.0094  39  LYS A CA    
243  C C     . LYS A 39  ? 0.7483 0.5907 0.4095 0.0682  0.0277  0.0179  39  LYS A C     
244  O O     . LYS A 39  ? 0.8362 0.6650 0.4705 0.0659  0.0249  0.0249  39  LYS A O     
245  C CB    . LYS A 39  ? 0.8031 0.6181 0.4313 0.0685  0.0157  -0.0012 39  LYS A CB    
246  C CG    . LYS A 39  ? 0.9415 0.7251 0.5131 0.0673  0.0211  -0.0012 39  LYS A CG    
247  C CD    . LYS A 39  ? 1.1700 0.9308 0.7114 0.0692  0.0311  -0.0138 39  LYS A CD    
248  C CE    . LYS A 39  ? 1.2519 0.9756 0.7282 0.0668  0.0331  -0.0158 39  LYS A CE    
249  N NZ    . LYS A 39  ? 1.2845 0.9832 0.7297 0.0678  0.0391  -0.0300 39  LYS A NZ    
250  N N     . ASN A 40  ? 0.7005 0.5608 0.3916 0.0712  0.0462  0.0180  40  ASN A N     
251  C CA    . ASN A 40  ? 0.7243 0.5902 0.4202 0.0716  0.0650  0.0257  40  ASN A CA    
252  C C     . ASN A 40  ? 0.7183 0.6084 0.4525 0.0696  0.0596  0.0342  40  ASN A C     
253  O O     . ASN A 40  ? 0.7296 0.6279 0.4759 0.0692  0.0744  0.0405  40  ASN A O     
254  C CB    . ASN A 40  ? 0.6594 0.5300 0.3667 0.0760  0.0889  0.0210  40  ASN A CB    
255  C CG    . ASN A 40  ? 0.7809 0.6227 0.4430 0.0778  0.1007  0.0136  40  ASN A CG    
256  O OD1   . ASN A 40  ? 0.8274 0.6516 0.4564 0.0766  0.1135  0.0172  40  ASN A OD1   
257  N ND2   . ASN A 40  ? 0.7174 0.5521 0.3755 0.0802  0.0967  0.0032  40  ASN A ND2   
258  N N     . LYS A 41  ? 0.6087 0.5090 0.3620 0.0679  0.0395  0.0341  41  LYS A N     
259  C CA    . LYS A 41  ? 0.5963 0.5158 0.3820 0.0658  0.0333  0.0409  41  LYS A CA    
260  C C     . LYS A 41  ? 0.6620 0.6022 0.4814 0.0667  0.0488  0.0429  41  LYS A C     
261  O O     . LYS A 41  ? 0.5969 0.5446 0.4285 0.0647  0.0547  0.0500  41  LYS A O     
262  C CB    . LYS A 41  ? 0.6160 0.5240 0.3824 0.0632  0.0282  0.0498  41  LYS A CB    
263  C CG    . LYS A 41  ? 0.7291 0.6158 0.4621 0.0623  0.0100  0.0490  41  LYS A CG    
264  C CD    . LYS A 41  ? 0.9090 0.7824 0.6220 0.0602  0.0040  0.0592  41  LYS A CD    
265  C CE    . LYS A 41  ? 1.0828 0.9367 0.7669 0.0592  -0.0186 0.0591  41  LYS A CE    
266  N NZ    . LYS A 41  ? 1.3287 1.1700 0.9970 0.0576  -0.0276 0.0704  41  LYS A NZ    
267  N N     . ILE A 42  ? 0.5839 0.5325 0.4190 0.0694  0.0543  0.0366  42  ILE A N     
268  C CA    . ILE A 42  ? 0.5561 0.5255 0.4267 0.0704  0.0644  0.0380  42  ILE A CA    
269  C C     . ILE A 42  ? 0.5185 0.5020 0.4151 0.0698  0.0516  0.0348  42  ILE A C     
270  O O     . ILE A 42  ? 0.5215 0.5000 0.4135 0.0717  0.0465  0.0284  42  ILE A O     
271  C CB    . ILE A 42  ? 0.5256 0.4926 0.3954 0.0748  0.0825  0.0343  42  ILE A CB    
272  C CG1   . ILE A 42  ? 0.6125 0.5653 0.4568 0.0749  0.0991  0.0377  42  ILE A CG1   
273  C CG2   . ILE A 42  ? 0.5315 0.5215 0.4430 0.0761  0.0879  0.0356  42  ILE A CG2   
274  C CD1   . ILE A 42  ? 0.6743 0.6193 0.5108 0.0798  0.1175  0.0321  42  ILE A CD1   
275  N N     . GLY A 43  ? 0.4845 0.4838 0.4068 0.0669  0.0473  0.0390  43  GLY A N     
276  C CA    . GLY A 43  ? 0.4255 0.4365 0.3694 0.0656  0.0371  0.0364  43  GLY A CA    
277  C C     . GLY A 43  ? 0.4680 0.4893 0.4314 0.0681  0.0433  0.0344  43  GLY A C     
278  O O     . GLY A 43  ? 0.4586 0.4841 0.4297 0.0704  0.0555  0.0363  43  GLY A O     
279  N N     . LEU A 44  ? 0.4240 0.4490 0.3970 0.0677  0.0346  0.0310  44  LEU A N     
280  C CA    . LEU A 44  ? 0.3979 0.4304 0.3881 0.0701  0.0375  0.0299  44  LEU A CA    
281  C C     . LEU A 44  ? 0.3988 0.4424 0.4072 0.0661  0.0286  0.0314  44  LEU A C     
282  O O     . LEU A 44  ? 0.3956 0.4362 0.3998 0.0632  0.0199  0.0292  44  LEU A O     
283  C CB    . LEU A 44  ? 0.4247 0.4453 0.4029 0.0738  0.0373  0.0238  44  LEU A CB    
284  C CG    . LEU A 44  ? 0.4979 0.5236 0.4936 0.0768  0.0386  0.0230  44  LEU A CG    
285  C CD1   . LEU A 44  ? 0.4758 0.5087 0.4862 0.0813  0.0510  0.0259  44  LEU A CD1   
286  C CD2   . LEU A 44  ? 0.4538 0.4653 0.4368 0.0792  0.0360  0.0166  44  LEU A CD2   
287  N N     . ILE A 45  ? 0.3914 0.4468 0.4196 0.0658  0.0309  0.0349  45  ILE A N     
288  C CA    . ILE A 45  ? 0.4598 0.5237 0.5014 0.0615  0.0230  0.0367  45  ILE A CA    
289  C C     . ILE A 45  ? 0.4396 0.5073 0.4938 0.0642  0.0219  0.0376  45  ILE A C     
290  O O     . ILE A 45  ? 0.4144 0.4889 0.4831 0.0673  0.0273  0.0404  45  ILE A O     
291  C CB    . ILE A 45  ? 0.4229 0.4962 0.4757 0.0573  0.0235  0.0408  45  ILE A CB    
292  C CG1   . ILE A 45  ? 0.3924 0.4605 0.4336 0.0548  0.0234  0.0406  45  ILE A CG1   
293  C CG2   . ILE A 45  ? 0.3557 0.4354 0.4190 0.0527  0.0156  0.0419  45  ILE A CG2   
294  C CD1   . ILE A 45  ? 0.3979 0.4724 0.4487 0.0518  0.0272  0.0450  45  ILE A CD1   
295  N N     . LEU A 46  ? 0.4110 0.4741 0.4616 0.0628  0.0151  0.0358  46  LEU A N     
296  C CA    . LEU A 46  ? 0.4013 0.4648 0.4612 0.0652  0.0124  0.0374  46  LEU A CA    
297  C C     . LEU A 46  ? 0.4526 0.5200 0.5167 0.0595  0.0039  0.0405  46  LEU A C     
298  O O     . LEU A 46  ? 0.4482 0.5114 0.5022 0.0544  0.0005  0.0384  46  LEU A O     
299  C CB    . LEU A 46  ? 0.4544 0.5056 0.5039 0.0682  0.0123  0.0332  46  LEU A CB    
300  C CG    . LEU A 46  ? 0.4931 0.5358 0.5312 0.0729  0.0199  0.0286  46  LEU A CG    
301  C CD1   . LEU A 46  ? 0.4628 0.4917 0.4894 0.0740  0.0175  0.0235  46  LEU A CD1   
302  C CD2   . LEU A 46  ? 0.4262 0.4731 0.4757 0.0792  0.0295  0.0302  46  LEU A CD2   
303  N N     . VAL A 47  ? 0.3914 0.4662 0.4702 0.0600  0.0005  0.0453  47  VAL A N     
304  C CA    . VAL A 47  ? 0.3569 0.4331 0.4361 0.0543  -0.0089 0.0485  47  VAL A CA    
305  C C     . VAL A 47  ? 0.4035 0.4736 0.4840 0.0569  -0.0144 0.0515  47  VAL A C     
306  O O     . VAL A 47  ? 0.4161 0.4878 0.5094 0.0638  -0.0123 0.0532  47  VAL A O     
307  C CB    . VAL A 47  ? 0.3929 0.4808 0.4874 0.0518  -0.0121 0.0524  47  VAL A CB    
308  C CG1   . VAL A 47  ? 0.3626 0.4500 0.4568 0.0468  -0.0240 0.0564  47  VAL A CG1   
309  C CG2   . VAL A 47  ? 0.3652 0.4558 0.4553 0.0475  -0.0080 0.0499  47  VAL A CG2   
310  N N     . PHE A 48  ? 0.3436 0.4055 0.4106 0.0516  -0.0204 0.0523  48  PHE A N     
311  C CA    . PHE A 48  ? 0.4050 0.4593 0.4711 0.0529  -0.0269 0.0567  48  PHE A CA    
312  C C     . PHE A 48  ? 0.4066 0.4591 0.4653 0.0459  -0.0370 0.0614  48  PHE A C     
313  O O     . PHE A 48  ? 0.4672 0.5159 0.5105 0.0387  -0.0364 0.0587  48  PHE A O     
314  C CB    . PHE A 48  ? 0.4021 0.4431 0.4547 0.0527  -0.0236 0.0536  48  PHE A CB    
315  C CG    . PHE A 48  ? 0.4443 0.4831 0.5019 0.0598  -0.0162 0.0492  48  PHE A CG    
316  C CD1   . PHE A 48  ? 0.3733 0.4146 0.4272 0.0601  -0.0094 0.0432  48  PHE A CD1   
317  C CD2   . PHE A 48  ? 0.4547 0.4869 0.5190 0.0661  -0.0167 0.0510  48  PHE A CD2   
318  C CE1   . PHE A 48  ? 0.4438 0.4801 0.4970 0.0659  -0.0033 0.0387  48  PHE A CE1   
319  C CE2   . PHE A 48  ? 0.4333 0.4607 0.4991 0.0722  -0.0093 0.0458  48  PHE A CE2   
320  C CZ    . PHE A 48  ? 0.4449 0.4738 0.5033 0.0718  -0.0027 0.0394  48  PHE A CZ    
321  N N     . GLU A 49  ? 0.4405 0.4953 0.5104 0.0482  -0.0465 0.0682  49  GLU A N     
322  C CA    . GLU A 49  ? 0.4761 0.5262 0.5358 0.0417  -0.0590 0.0735  49  GLU A CA    
323  C C     . GLU A 49  ? 0.4723 0.5135 0.5331 0.0452  -0.0681 0.0810  49  GLU A C     
324  O O     . GLU A 49  ? 0.4707 0.5128 0.5471 0.0537  -0.0647 0.0820  49  GLU A O     
325  C CB    . GLU A 49  ? 0.4370 0.5004 0.5119 0.0394  -0.0660 0.0754  49  GLU A CB    
326  C CG    . GLU A 49  ? 0.4269 0.4977 0.5011 0.0356  -0.0575 0.0688  49  GLU A CG    
327  C CD    . GLU A 49  ? 0.4986 0.5589 0.5461 0.0264  -0.0573 0.0649  49  GLU A CD    
328  O OE1   . GLU A 49  ? 0.4871 0.5341 0.5143 0.0219  -0.0633 0.0674  49  GLU A OE1   
329  O OE2   . GLU A 49  ? 0.4694 0.5335 0.5158 0.0236  -0.0503 0.0595  49  GLU A OE2   
330  N N     . GLY A 50  ? 0.4857 0.5163 0.5281 0.0386  -0.0794 0.0863  50  GLY A N     
331  C CA    . GLY A 50  ? 0.4756 0.4942 0.5140 0.0406  -0.0901 0.0950  50  GLY A CA    
332  C C     . GLY A 50  ? 0.5692 0.5683 0.5712 0.0309  -0.0938 0.0972  50  GLY A C     
333  O O     . GLY A 50  ? 0.5726 0.5673 0.5552 0.0241  -0.0843 0.0907  50  GLY A O     
334  N N     . MET A 51  ? 0.5591 0.5454 0.5518 0.0304  -0.1073 0.1069  51  MET A N     
335  C CA    . MET A 51  ? 0.5810 0.5463 0.5350 0.0204  -0.1110 0.1102  51  MET A CA    
336  C C     . MET A 51  ? 0.5793 0.5316 0.5161 0.0179  -0.0953 0.1062  51  MET A C     
337  O O     . MET A 51  ? 0.5693 0.5263 0.5235 0.0245  -0.0855 0.1026  51  MET A O     
338  C CB    . MET A 51  ? 0.6232 0.5756 0.5692 0.0205  -0.1306 0.1229  51  MET A CB    
339  C CG    . MET A 51  ? 0.6481 0.6130 0.6111 0.0211  -0.1488 0.1272  51  MET A CG    
340  S SD    . MET A 51  ? 0.9573 0.9028 0.9017 0.0183  -0.1753 0.1426  51  MET A SD    
341  C CE    . MET A 51  ? 0.8023 0.7396 0.7627 0.0293  -0.1729 0.1501  51  MET A CE    
342  N N     . ASP A 52  ? 0.6222 0.5575 0.5241 0.0077  -0.0924 0.1062  52  ASP A N     
343  C CA    . ASP A 52  ? 0.6236 0.5451 0.5094 0.0038  -0.0780 0.1039  52  ASP A CA    
344  C C     . ASP A 52  ? 0.5997 0.5123 0.4945 0.0100  -0.0804 0.1109  52  ASP A C     
345  O O     . ASP A 52  ? 0.6195 0.5242 0.5132 0.0129  -0.0953 0.1213  52  ASP A O     
346  C CB    . ASP A 52  ? 0.7948 0.6954 0.6394 -0.0081 -0.0764 0.1058  52  ASP A CB    
347  C CG    . ASP A 52  ? 0.9642 0.8561 0.7968 -0.0138 -0.0565 0.0999  52  ASP A CG    
348  O OD1   . ASP A 52  ? 0.9146 0.8171 0.7713 -0.0088 -0.0464 0.0943  52  ASP A OD1   
349  O OD2   . ASP A 52  ? 1.0037 0.8776 0.8028 -0.0236 -0.0509 0.1006  52  ASP A OD2   
350  N N     . ALA A 53  ? 0.5838 0.4977 0.4896 0.0124  -0.0667 0.1051  53  ALA A N     
351  C CA    . ALA A 53  ? 0.6048 0.5093 0.5199 0.0177  -0.0660 0.1092  53  ALA A CA    
352  C C     . ALA A 53  ? 0.6345 0.5498 0.5797 0.0298  -0.0748 0.1116  53  ALA A C     
353  O O     . ALA A 53  ? 0.6341 0.5388 0.5860 0.0351  -0.0786 0.1176  53  ALA A O     
354  C CB    . ALA A 53  ? 0.6243 0.5029 0.5115 0.0117  -0.0709 0.1202  53  ALA A CB    
355  N N     . ALA A 54  ? 0.5797 0.5155 0.5444 0.0344  -0.0771 0.1072  54  ALA A N     
356  C CA    . ALA A 54  ? 0.5723 0.5202 0.5689 0.0461  -0.0804 0.1075  54  ALA A CA    
357  C C     . ALA A 54  ? 0.5575 0.5081 0.5681 0.0518  -0.0670 0.0987  54  ALA A C     
358  O O     . ALA A 54  ? 0.5702 0.5258 0.6041 0.0617  -0.0672 0.0985  54  ALA A O     
359  C CB    . ALA A 54  ? 0.5999 0.5685 0.6136 0.0484  -0.0851 0.1055  54  ALA A CB    
360  N N     . GLY A 55  ? 0.5258 0.4728 0.5237 0.0457  -0.0558 0.0914  55  GLY A N     
361  C CA    . GLY A 55  ? 0.4658 0.4134 0.4739 0.0497  -0.0455 0.0829  55  GLY A CA    
362  C C     . GLY A 55  ? 0.5468 0.5114 0.5641 0.0512  -0.0381 0.0731  55  GLY A C     
363  O O     . GLY A 55  ? 0.4741 0.4398 0.5010 0.0564  -0.0319 0.0665  55  GLY A O     
364  N N     . LYS A 56  ? 0.4644 0.4399 0.4770 0.0465  -0.0388 0.0721  56  LYS A N     
365  C CA    . LYS A 56  ? 0.5063 0.4961 0.5258 0.0472  -0.0322 0.0640  56  LYS A CA    
366  C C     . LYS A 56  ? 0.4637 0.4495 0.4783 0.0442  -0.0237 0.0562  56  LYS A C     
367  O O     . LYS A 56  ? 0.4664 0.4569 0.4890 0.0487  -0.0192 0.0500  56  LYS A O     
368  C CB    . LYS A 56  ? 0.4213 0.4196 0.4342 0.0412  -0.0347 0.0646  56  LYS A CB    
369  C CG    . LYS A 56  ? 0.4157 0.4194 0.4350 0.0429  -0.0454 0.0718  56  LYS A CG    
370  C CD    . LYS A 56  ? 0.4109 0.4212 0.4223 0.0360  -0.0478 0.0708  56  LYS A CD    
371  C CE    . LYS A 56  ? 0.5423 0.5394 0.5273 0.0261  -0.0461 0.0705  56  LYS A CE    
372  N NZ    . LYS A 56  ? 0.4959 0.4775 0.4643 0.0229  -0.0553 0.0792  56  LYS A NZ    
373  N N     . GLY A 57  ? 0.4568 0.4333 0.4582 0.0362  -0.0215 0.0567  57  GLY A N     
374  C CA    . GLY A 57  ? 0.4666 0.4415 0.4682 0.0325  -0.0144 0.0497  57  GLY A CA    
375  C C     . GLY A 57  ? 0.4722 0.4399 0.4808 0.0370  -0.0134 0.0463  57  GLY A C     
376  O O     . GLY A 57  ? 0.4538 0.4255 0.4678 0.0383  -0.0107 0.0389  57  GLY A O     
377  N N     . GLY A 58  ? 0.4867 0.4419 0.4942 0.0394  -0.0165 0.0516  58  GLY A N     
378  C CA    . GLY A 58  ? 0.4994 0.4446 0.5125 0.0433  -0.0153 0.0478  58  GLY A CA    
379  C C     . GLY A 58  ? 0.5067 0.4581 0.5289 0.0526  -0.0147 0.0426  58  GLY A C     
380  O O     . GLY A 58  ? 0.5425 0.4894 0.5656 0.0543  -0.0120 0.0350  58  GLY A O     
381  N N     . ALA A 59  ? 0.4765 0.4376 0.5049 0.0584  -0.0169 0.0466  59  ALA A N     
382  C CA    . ALA A 59  ? 0.4722 0.4398 0.5095 0.0668  -0.0134 0.0419  59  ALA A CA    
383  C C     . ALA A 59  ? 0.5037 0.4797 0.5364 0.0645  -0.0094 0.0343  59  ALA A C     
384  O O     . ALA A 59  ? 0.4937 0.4660 0.5247 0.0684  -0.0054 0.0275  59  ALA A O     
385  C CB    . ALA A 59  ? 0.4512 0.4296 0.5007 0.0723  -0.0162 0.0482  59  ALA A CB    
386  N N     . ILE A 60  ? 0.4373 0.4224 0.4662 0.0579  -0.0104 0.0355  60  ILE A N     
387  C CA    . ILE A 60  ? 0.3996 0.3915 0.4253 0.0557  -0.0079 0.0293  60  ILE A CA    
388  C C     . ILE A 60  ? 0.4958 0.4776 0.5170 0.0531  -0.0077 0.0228  60  ILE A C     
389  O O     . ILE A 60  ? 0.4290 0.4097 0.4467 0.0554  -0.0069 0.0167  60  ILE A O     
390  C CB    . ILE A 60  ? 0.4488 0.4503 0.4731 0.0492  -0.0086 0.0314  60  ILE A CB    
391  C CG1   . ILE A 60  ? 0.4293 0.4412 0.4583 0.0515  -0.0100 0.0364  60  ILE A CG1   
392  C CG2   . ILE A 60  ? 0.3543 0.3606 0.3774 0.0469  -0.0071 0.0254  60  ILE A CG2   
393  C CD1   . ILE A 60  ? 0.4239 0.4411 0.4488 0.0445  -0.0114 0.0386  60  ILE A CD1   
394  N N     . LYS A 61  ? 0.4323 0.4056 0.4529 0.0475  -0.0090 0.0242  61  LYS A N     
395  C CA    . LYS A 61  ? 0.5049 0.4692 0.5250 0.0439  -0.0097 0.0181  61  LYS A CA    
396  C C     . LYS A 61  ? 0.4860 0.4397 0.5027 0.0500  -0.0100 0.0126  61  LYS A C     
397  O O     . LYS A 61  ? 0.5087 0.4591 0.5217 0.0490  -0.0120 0.0054  61  LYS A O     
398  C CB    . LYS A 61  ? 0.4672 0.4221 0.4886 0.0371  -0.0094 0.0215  61  LYS A CB    
399  C CG    . LYS A 61  ? 0.6277 0.5899 0.6504 0.0293  -0.0068 0.0240  61  LYS A CG    
400  C CD    . LYS A 61  ? 0.8191 0.7706 0.8433 0.0214  -0.0040 0.0258  61  LYS A CD    
401  C CE    . LYS A 61  ? 0.9483 0.8882 0.9638 0.0213  -0.0037 0.0343  61  LYS A CE    
402  N NZ    . LYS A 61  ? 0.9501 0.8796 0.9637 0.0120  0.0012  0.0376  61  LYS A NZ    
403  N N     . ARG A 62  ? 0.4765 0.4238 0.4942 0.0565  -0.0085 0.0155  62  ARG A N     
404  C CA    . ARG A 62  ? 0.5616 0.4968 0.5752 0.0626  -0.0066 0.0089  62  ARG A CA    
405  C C     . ARG A 62  ? 0.5265 0.4683 0.5341 0.0676  -0.0032 0.0044  62  ARG A C     
406  O O     . ARG A 62  ? 0.5418 0.4733 0.5389 0.0693  -0.0025 -0.0036 62  ARG A O     
407  C CB    . ARG A 62  ? 0.5441 0.4701 0.5637 0.0693  -0.0047 0.0130  62  ARG A CB    
408  C CG    . ARG A 62  ? 0.5919 0.5014 0.6122 0.0655  -0.0073 0.0140  62  ARG A CG    
409  C CD    . ARG A 62  ? 0.5472 0.4614 0.5692 0.0578  -0.0101 0.0223  62  ARG A CD    
410  N NE    . ARG A 62  ? 0.6016 0.5001 0.6235 0.0523  -0.0115 0.0244  62  ARG A NE    
411  C CZ    . ARG A 62  ? 0.7333 0.6309 0.7537 0.0453  -0.0121 0.0322  62  ARG A CZ    
412  N NH1   . ARG A 62  ? 0.5994 0.5101 0.6173 0.0431  -0.0124 0.0378  62  ARG A NH1   
413  N NH2   . ARG A 62  ? 0.5915 0.4731 0.6113 0.0399  -0.0120 0.0343  62  ARG A NH2   
414  N N     . LEU A 63  ? 0.4908 0.4480 0.5031 0.0693  -0.0013 0.0094  63  LEU A N     
415  C CA    . LEU A 63  ? 0.5276 0.4905 0.5346 0.0738  0.0034  0.0064  63  LEU A CA    
416  C C     . LEU A 63  ? 0.5056 0.4661 0.4995 0.0695  0.0003  0.0003  63  LEU A C     
417  O O     . LEU A 63  ? 0.5204 0.4723 0.5009 0.0727  0.0030  -0.0056 63  LEU A O     
418  C CB    . LEU A 63  ? 0.5049 0.4850 0.5217 0.0746  0.0050  0.0135  63  LEU A CB    
419  C CG    . LEU A 63  ? 0.5243 0.5126 0.5381 0.0777  0.0106  0.0125  63  LEU A CG    
420  C CD1   . LEU A 63  ? 0.5271 0.5082 0.5394 0.0859  0.0196  0.0090  63  LEU A CD1   
421  C CD2   . LEU A 63  ? 0.5375 0.5422 0.5643 0.0766  0.0101  0.0198  63  LEU A CD2   
422  N N     . ILE A 64  ? 0.4495 0.4166 0.4468 0.0622  -0.0055 0.0017  64  ILE A N     
423  C CA    . ILE A 64  ? 0.4681 0.4351 0.4574 0.0587  -0.0103 -0.0027 64  ILE A CA    
424  C C     . ILE A 64  ? 0.5124 0.4690 0.5010 0.0534  -0.0173 -0.0081 64  ILE A C     
425  O O     . ILE A 64  ? 0.5322 0.4902 0.5194 0.0493  -0.0240 -0.0109 64  ILE A O     
426  C CB    . ILE A 64  ? 0.5011 0.4836 0.4979 0.0551  -0.0117 0.0016  64  ILE A CB    
427  C CG1   . ILE A 64  ? 0.4535 0.4430 0.4632 0.0505  -0.0114 0.0067  64  ILE A CG1   
428  C CG2   . ILE A 64  ? 0.5061 0.4961 0.4996 0.0598  -0.0063 0.0047  64  ILE A CG2   
429  C CD1   . ILE A 64  ? 0.4558 0.4400 0.4714 0.0441  -0.0150 0.0045  64  ILE A CD1   
430  N N     . GLU A 65  ? 0.4815 0.4272 0.4727 0.0532  -0.0167 -0.0092 65  GLU A N     
431  C CA    . GLU A 65  ? 0.5188 0.4552 0.5134 0.0467  -0.0231 -0.0136 65  GLU A CA    
432  C C     . GLU A 65  ? 0.5684 0.4950 0.5500 0.0457  -0.0303 -0.0219 65  GLU A C     
433  O O     . GLU A 65  ? 0.5434 0.4714 0.5318 0.0391  -0.0387 -0.0244 65  GLU A O     
434  C CB    . GLU A 65  ? 0.5170 0.4401 0.5142 0.0475  -0.0204 -0.0133 65  GLU A CB    
435  C CG    . GLU A 65  ? 0.5839 0.4955 0.5856 0.0404  -0.0263 -0.0179 65  GLU A CG    
436  C CD    . GLU A 65  ? 0.7809 0.6766 0.7841 0.0414  -0.0234 -0.0172 65  GLU A CD    
437  O OE1   . GLU A 65  ? 0.7173 0.6117 0.7197 0.0483  -0.0175 -0.0126 65  GLU A OE1   
438  O OE2   . GLU A 65  ? 0.8797 0.7640 0.8871 0.0352  -0.0276 -0.0211 65  GLU A OE2   
439  N N     . ARG A 66  ? 0.5352 0.4510 0.4981 0.0518  -0.0274 -0.0264 66  ARG A N     
440  C CA    A ARG A 66  ? 0.5568 0.4587 0.5003 0.0506  -0.0348 -0.0347 66  ARG A CA    
441  C CA    B ARG A 66  ? 0.5515 0.4534 0.4950 0.0506  -0.0347 -0.0347 66  ARG A CA    
442  C C     . ARG A 66  ? 0.5669 0.4749 0.4971 0.0525  -0.0361 -0.0335 66  ARG A C     
443  O O     . ARG A 66  ? 0.5999 0.4946 0.5084 0.0519  -0.0424 -0.0395 66  ARG A O     
444  C CB    A ARG A 66  ? 0.6256 0.5060 0.5514 0.0554  -0.0298 -0.0419 66  ARG A CB    
445  C CB    B ARG A 66  ? 0.6246 0.5051 0.5505 0.0554  -0.0297 -0.0419 66  ARG A CB    
446  C CG    A ARG A 66  ? 0.6341 0.5054 0.5720 0.0545  -0.0280 -0.0427 66  ARG A CG    
447  C CG    B ARG A 66  ? 0.6320 0.5052 0.5711 0.0559  -0.0257 -0.0414 66  ARG A CG    
448  C CD    A ARG A 66  ? 0.6487 0.5227 0.6029 0.0448  -0.0379 -0.0424 66  ARG A CD    
449  C CD    B ARG A 66  ? 0.6754 0.5366 0.6186 0.0479  -0.0357 -0.0469 66  ARG A CD    
450  N NE    A ARG A 66  ? 0.6685 0.5304 0.6121 0.0391  -0.0501 -0.0510 66  ARG A NE    
451  N NE    B ARG A 66  ? 0.6939 0.5454 0.6478 0.0485  -0.0312 -0.0457 66  ARG A NE    
452  C CZ    A ARG A 66  ? 0.6907 0.5341 0.6318 0.0351  -0.0553 -0.0582 66  ARG A CZ    
453  C CZ    B ARG A 66  ? 0.7371 0.5775 0.6985 0.0415  -0.0373 -0.0489 66  ARG A CZ    
454  N NH1   A ARG A 66  ? 0.7129 0.5461 0.6604 0.0368  -0.0483 -0.0578 66  ARG A NH1   
455  N NH1   B ARG A 66  ? 0.7376 0.5762 0.6996 0.0332  -0.0489 -0.0542 66  ARG A NH1   
456  N NH2   A ARG A 66  ? 0.7167 0.5506 0.6494 0.0288  -0.0689 -0.0657 66  ARG A NH2   
457  N NH2   B ARG A 66  ? 0.6900 0.5205 0.6601 0.0426  -0.0324 -0.0464 66  ARG A NH2   
458  N N     . VAL A 67  ? 0.5811 0.5066 0.5216 0.0542  -0.0309 -0.0260 67  VAL A N     
459  C CA    . VAL A 67  ? 0.5656 0.4968 0.4955 0.0557  -0.0317 -0.0236 67  VAL A CA    
460  C C     . VAL A 67  ? 0.6287 0.5657 0.5663 0.0495  -0.0450 -0.0233 67  VAL A C     
461  O O     . VAL A 67  ? 0.6164 0.5617 0.5762 0.0446  -0.0490 -0.0221 67  VAL A O     
462  C CB    . VAL A 67  ? 0.5358 0.4830 0.4769 0.0594  -0.0213 -0.0159 67  VAL A CB    
463  C CG1   . VAL A 67  ? 0.6381 0.5928 0.5735 0.0595  -0.0223 -0.0121 67  VAL A CG1   
464  C CG2   . VAL A 67  ? 0.4924 0.4341 0.4280 0.0663  -0.0091 -0.0163 67  VAL A CG2   
465  N N     . ASP A 68  ? 0.5585 0.4901 0.4784 0.0497  -0.0517 -0.0241 68  ASP A N     
466  C CA    . ASP A 68  ? 0.5842 0.5217 0.5134 0.0450  -0.0656 -0.0229 68  ASP A CA    
467  C C     . ASP A 68  ? 0.5957 0.5544 0.5531 0.0438  -0.0621 -0.0161 68  ASP A C     
468  O O     . ASP A 68  ? 0.5428 0.5094 0.4990 0.0473  -0.0531 -0.0109 68  ASP A O     
469  C CB    . ASP A 68  ? 0.6910 0.6184 0.5931 0.0468  -0.0720 -0.0225 68  ASP A CB    
470  C CG    . ASP A 68  ? 0.7099 0.6398 0.6202 0.0424  -0.0902 -0.0215 68  ASP A CG    
471  O OD1   . ASP A 68  ? 0.7389 0.6834 0.6813 0.0389  -0.0948 -0.0198 68  ASP A OD1   
472  O OD2   . ASP A 68  ? 0.8339 0.7502 0.7180 0.0427  -0.0996 -0.0221 68  ASP A OD2   
473  N N     . PRO A 69  ? 0.5638 0.5313 0.5469 0.0386  -0.0681 -0.0163 69  PRO A N     
474  C CA    . PRO A 69  ? 0.5093 0.4946 0.5171 0.0374  -0.0622 -0.0110 69  PRO A CA    
475  C C     . PRO A 69  ? 0.5899 0.5825 0.5989 0.0392  -0.0651 -0.0067 69  PRO A C     
476  O O     . PRO A 69  ? 0.5199 0.5245 0.5423 0.0395  -0.0575 -0.0025 69  PRO A O     
477  C CB    . PRO A 69  ? 0.5567 0.5467 0.5902 0.0310  -0.0676 -0.0134 69  PRO A CB    
478  C CG    . PRO A 69  ? 0.6985 0.6736 0.7219 0.0289  -0.0738 -0.0195 69  PRO A CG    
479  C CD    . PRO A 69  ? 0.6015 0.5623 0.5931 0.0332  -0.0788 -0.0219 69  PRO A CD    
480  N N     . ARG A 70  ? 0.5176 0.5016 0.5118 0.0402  -0.0765 -0.0074 70  ARG A N     
481  C CA    . ARG A 70  ? 0.5155 0.5033 0.5074 0.0425  -0.0795 -0.0022 70  ARG A CA    
482  C C     . ARG A 70  ? 0.4949 0.4820 0.4694 0.0468  -0.0669 0.0018  70  ARG A C     
483  O O     . ARG A 70  ? 0.5876 0.5796 0.5641 0.0483  -0.0661 0.0069  70  ARG A O     
484  C CB    . ARG A 70  ? 0.5163 0.4915 0.4917 0.0421  -0.0964 -0.0032 70  ARG A CB    
485  C CG    . ARG A 70  ? 0.6980 0.6759 0.6961 0.0374  -0.1119 -0.0066 70  ARG A CG    
486  C CD    . ARG A 70  ? 0.7128 0.6750 0.6894 0.0366  -0.1312 -0.0080 70  ARG A CD    
487  N NE    . ARG A 70  ? 0.8560 0.7982 0.7935 0.0375  -0.1288 -0.0127 70  ARG A NE    
488  C CZ    . ARG A 70  ? 1.0331 0.9557 0.9389 0.0367  -0.1425 -0.0151 70  ARG A CZ    
489  N NH1   . ARG A 70  ? 0.9192 0.8394 0.8270 0.0351  -0.1623 -0.0121 70  ARG A NH1   
490  N NH2   . ARG A 70  ? 0.8863 0.7899 0.7569 0.0377  -0.1366 -0.0206 70  ARG A NH2   
491  N N     . GLY A 71  ? 0.4820 0.4631 0.4419 0.0489  -0.0572 -0.0003 71  GLY A N     
492  C CA    . GLY A 71  ? 0.6005 0.5808 0.5461 0.0530  -0.0454 0.0032  71  GLY A CA    
493  C C     . GLY A 71  ? 0.5597 0.5526 0.5212 0.0538  -0.0332 0.0060  71  GLY A C     
494  O O     . GLY A 71  ? 0.5354 0.5287 0.4889 0.0570  -0.0235 0.0087  71  GLY A O     
495  N N     . TYR A 72  ? 0.4684 0.4709 0.4518 0.0506  -0.0334 0.0057  72  TYR A N     
496  C CA    . TYR A 72  ? 0.4448 0.4569 0.4392 0.0508  -0.0238 0.0087  72  TYR A CA    
497  C C     . TYR A 72  ? 0.4800 0.5019 0.4949 0.0463  -0.0246 0.0095  72  TYR A C     
498  O O     . TYR A 72  ? 0.4207 0.4424 0.4454 0.0432  -0.0308 0.0068  72  TYR A O     
499  C CB    . TYR A 72  ? 0.4712 0.4781 0.4621 0.0525  -0.0190 0.0067  72  TYR A CB    
500  C CG    . TYR A 72  ? 0.5000 0.5030 0.4988 0.0489  -0.0232 0.0031  72  TYR A CG    
501  C CD1   . TYR A 72  ? 0.4870 0.4967 0.5005 0.0453  -0.0205 0.0051  72  TYR A CD1   
502  C CD2   . TYR A 72  ? 0.5299 0.5209 0.5196 0.0485  -0.0296 -0.0022 72  TYR A CD2   
503  C CE1   . TYR A 72  ? 0.5227 0.5278 0.5433 0.0414  -0.0227 0.0026  72  TYR A CE1   
504  C CE2   . TYR A 72  ? 0.5080 0.4951 0.5069 0.0444  -0.0332 -0.0053 72  TYR A CE2   
505  C CZ    . TYR A 72  ? 0.5109 0.5054 0.5260 0.0409  -0.0290 -0.0025 72  TYR A CZ    
506  O OH    . TYR A 72  ? 0.5421 0.5319 0.5664 0.0363  -0.0311 -0.0049 72  TYR A OH    
507  N N     . VAL A 73  ? 0.4213 0.4511 0.4427 0.0457  -0.0178 0.0128  73  VAL A N     
508  C CA    . VAL A 73  ? 0.3655 0.4017 0.4011 0.0412  -0.0154 0.0131  73  VAL A CA    
509  C C     . VAL A 73  ? 0.4118 0.4494 0.4454 0.0408  -0.0097 0.0155  73  VAL A C     
510  O O     . VAL A 73  ? 0.4109 0.4508 0.4399 0.0435  -0.0070 0.0185  73  VAL A O     
511  C CB    . VAL A 73  ? 0.4423 0.4851 0.4865 0.0400  -0.0147 0.0145  73  VAL A CB    
512  C CG1   . VAL A 73  ? 0.3708 0.4177 0.4275 0.0351  -0.0101 0.0133  73  VAL A CG1   
513  C CG2   . VAL A 73  ? 0.4156 0.4565 0.4624 0.0414  -0.0225 0.0136  73  VAL A CG2   
514  N N     . VAL A 74  ? 0.3875 0.4230 0.4251 0.0371  -0.0083 0.0148  74  VAL A N     
515  C CA    . VAL A 74  ? 0.3892 0.4242 0.4238 0.0357  -0.0050 0.0181  74  VAL A CA    
516  C C     . VAL A 74  ? 0.4247 0.4636 0.4627 0.0307  -0.0014 0.0186  74  VAL A C     
517  O O     . VAL A 74  ? 0.4116 0.4502 0.4566 0.0267  0.0008  0.0160  74  VAL A O     
518  C CB    . VAL A 74  ? 0.4231 0.4500 0.4561 0.0343  -0.0052 0.0178  74  VAL A CB    
519  C CG1   . VAL A 74  ? 0.3704 0.3951 0.3986 0.0321  -0.0032 0.0224  74  VAL A CG1   
520  C CG2   . VAL A 74  ? 0.4456 0.4662 0.4737 0.0395  -0.0079 0.0161  74  VAL A CG2   
521  N N     . HIS A 75  ? 0.4095 0.4517 0.4438 0.0306  -0.0006 0.0216  75  HIS A N     
522  C CA    . HIS A 75  ? 0.4001 0.4433 0.4336 0.0255  0.0027  0.0213  75  HIS A CA    
523  C C     . HIS A 75  ? 0.4456 0.4830 0.4689 0.0218  0.0029  0.0243  75  HIS A C     
524  O O     . HIS A 75  ? 0.4275 0.4659 0.4471 0.0237  -0.0012 0.0283  75  HIS A O     
525  C CB    . HIS A 75  ? 0.3658 0.4148 0.4010 0.0266  0.0022  0.0222  75  HIS A CB    
526  C CG    . HIS A 75  ? 0.4138 0.4662 0.4559 0.0300  0.0014  0.0208  75  HIS A CG    
527  N ND1   . HIS A 75  ? 0.4281 0.4810 0.4782 0.0286  0.0030  0.0176  75  HIS A ND1   
528  C CD2   . HIS A 75  ? 0.4028 0.4571 0.4441 0.0348  -0.0008 0.0225  75  HIS A CD2   
529  C CE1   . HIS A 75  ? 0.4150 0.4696 0.4684 0.0324  -0.0002 0.0182  75  HIS A CE1   
530  N NE2   . HIS A 75  ? 0.4166 0.4711 0.4624 0.0359  -0.0019 0.0211  75  HIS A NE2   
531  N N     . PRO A 76  ? 0.4542 0.4850 0.4733 0.0166  0.0074  0.0230  76  PRO A N     
532  C CA    . PRO A 76  ? 0.4653 0.4876 0.4694 0.0121  0.0072  0.0266  76  PRO A CA    
533  C C     . PRO A 76  ? 0.4903 0.5114 0.4854 0.0075  0.0088  0.0256  76  PRO A C     
534  O O     . PRO A 76  ? 0.5538 0.5725 0.5485 0.0034  0.0165  0.0212  76  PRO A O     
535  C CB    . PRO A 76  ? 0.4596 0.4737 0.4620 0.0077  0.0136  0.0254  76  PRO A CB    
536  C CG    . PRO A 76  ? 0.5260 0.5466 0.5448 0.0079  0.0187  0.0196  76  PRO A CG    
537  C CD    . PRO A 76  ? 0.4117 0.4418 0.4403 0.0144  0.0125  0.0188  76  PRO A CD    
538  N N     . ILE A 77  ? 0.4481 0.4708 0.4379 0.0082  0.0016  0.0294  77  ILE A N     
539  C CA    . ILE A 77  ? 0.4809 0.5031 0.4640 0.0041  0.0010  0.0278  77  ILE A CA    
540  C C     . ILE A 77  ? 0.5429 0.5514 0.5028 -0.0032 0.0005  0.0292  77  ILE A C     
541  O O     . ILE A 77  ? 0.4733 0.4763 0.4239 -0.0034 -0.0061 0.0351  77  ILE A O     
542  C CB    . ILE A 77  ? 0.4789 0.5106 0.4709 0.0077  -0.0071 0.0309  77  ILE A CB    
543  C CG1   . ILE A 77  ? 0.4446 0.4867 0.4543 0.0140  -0.0047 0.0293  77  ILE A CG1   
544  C CG2   . ILE A 77  ? 0.4705 0.4997 0.4543 0.0021  -0.0101 0.0297  77  ILE A CG2   
545  C CD1   . ILE A 77  ? 0.4238 0.4666 0.4383 0.0128  0.0020  0.0238  77  ILE A CD1   
546  N N     . SER A 78  ? 0.5165 0.5180 0.4658 -0.0091 0.0078  0.0240  78  SER A N     
547  C CA    . SER A 78  ? 0.6444 0.6299 0.5657 -0.0171 0.0082  0.0243  78  SER A CA    
548  C C     . SER A 78  ? 0.6361 0.6191 0.5492 -0.0213 0.0056  0.0204  78  SER A C     
549  O O     . SER A 78  ? 0.5400 0.5347 0.4707 -0.0177 0.0018  0.0192  78  SER A O     
550  C CB    . SER A 78  ? 0.5686 0.5432 0.4804 -0.0216 0.0226  0.0207  78  SER A CB    
551  O OG    . SER A 78  ? 0.7258 0.7081 0.6575 -0.0195 0.0334  0.0138  78  SER A OG    
552  N N     . ALA A 79  ? 0.5670 0.5327 0.4513 -0.0295 0.0083  0.0181  79  ALA A N     
553  C CA    . ALA A 79  ? 0.6520 0.6114 0.5238 -0.0348 0.0051  0.0136  79  ALA A CA    
554  C C     . ALA A 79  ? 0.5093 0.4757 0.4000 -0.0326 0.0153  0.0055  79  ALA A C     
555  O O     . ALA A 79  ? 0.5555 0.5239 0.4578 -0.0302 0.0286  0.0016  79  ALA A O     
556  C CB    . ALA A 79  ? 0.6180 0.5537 0.4508 -0.0445 0.0093  0.0110  79  ALA A CB    
557  N N     . PRO A 80  ? 0.5497 0.5191 0.4451 -0.0337 0.0087  0.0033  80  PRO A N     
558  C CA    . PRO A 80  ? 0.5814 0.5538 0.4921 -0.0322 0.0181  -0.0040 80  PRO A CA    
559  C C     . PRO A 80  ? 0.6378 0.5942 0.5324 -0.0371 0.0342  -0.0128 80  PRO A C     
560  O O     . PRO A 80  ? 0.6209 0.5592 0.4837 -0.0449 0.0356  -0.0153 80  PRO A O     
561  C CB    . PRO A 80  ? 0.5827 0.5557 0.4933 -0.0354 0.0070  -0.0044 80  PRO A CB    
562  C CG    . PRO A 80  ? 0.6498 0.6279 0.5572 -0.0356 -0.0092 0.0043  80  PRO A CG    
563  C CD    . PRO A 80  ? 0.5699 0.5388 0.4572 -0.0371 -0.0079 0.0075  80  PRO A CD    
564  N N     . GLN A 81  ? 0.5680 0.5305 0.4849 -0.0325 0.0465  -0.0172 81  GLN A N     
565  C CA    . GLN A 81  ? 0.5652 0.5152 0.4761 -0.0356 0.0640  -0.0265 81  GLN A CA    
566  C C     . GLN A 81  ? 0.6521 0.5928 0.5575 -0.0389 0.0651  -0.0339 81  GLN A C     
567  O O     . GLN A 81  ? 0.5537 0.5020 0.4696 -0.0372 0.0534  -0.0314 81  GLN A O     
568  C CB    . GLN A 81  ? 0.5686 0.5307 0.5120 -0.0286 0.0744  -0.0277 81  GLN A CB    
569  C CG    . GLN A 81  ? 0.6787 0.6473 0.6280 -0.0266 0.0755  -0.0223 81  GLN A CG    
570  C CD    . GLN A 81  ? 0.9364 0.8889 0.8616 -0.0336 0.0888  -0.0252 81  GLN A CD    
571  O OE1   . GLN A 81  ? 1.0848 1.0293 0.9851 -0.0378 0.0832  -0.0200 81  GLN A OE1   
572  N NE2   . GLN A 81  ? 0.9299 0.8766 0.8625 -0.0349 0.1072  -0.0333 81  GLN A NE2   
573  N N     . PRO A 82  ? 0.6666 0.5896 0.5556 -0.0439 0.0804  -0.0435 82  PRO A N     
574  C CA    . PRO A 82  ? 0.6642 0.5758 0.5476 -0.0472 0.0822  -0.0518 82  PRO A CA    
575  C C     . PRO A 82  ? 0.6243 0.5501 0.5444 -0.0397 0.0800  -0.0515 82  PRO A C     
576  O O     . PRO A 82  ? 0.6238 0.5468 0.5430 -0.0418 0.0714  -0.0527 82  PRO A O     
577  C CB    . PRO A 82  ? 0.7265 0.6182 0.5920 -0.0517 0.1038  -0.0627 82  PRO A CB    
578  C CG    . PRO A 82  ? 0.6833 0.5695 0.5262 -0.0555 0.1075  -0.0584 82  PRO A CG    
579  C CD    . PRO A 82  ? 0.6805 0.5904 0.5515 -0.0480 0.0970  -0.0474 82  PRO A CD    
580  N N     . HIS A 83  ? 0.6179 0.5582 0.5700 -0.0314 0.0861  -0.0492 83  HIS A N     
581  C CA    A HIS A 83  ? 0.5438 0.4956 0.5274 -0.0243 0.0822  -0.0474 83  HIS A CA    
582  C CA    B HIS A 83  ? 0.5547 0.5064 0.5384 -0.0243 0.0822  -0.0475 83  HIS A CA    
583  C C     . HIS A 83  ? 0.5398 0.5042 0.5284 -0.0225 0.0642  -0.0380 83  HIS A C     
584  O O     . HIS A 83  ? 0.5561 0.5228 0.5574 -0.0208 0.0591  -0.0370 83  HIS A O     
585  C CB    A HIS A 83  ? 0.5637 0.5273 0.5790 -0.0163 0.0903  -0.0465 83  HIS A CB    
586  C CB    B HIS A 83  ? 0.5757 0.5395 0.5915 -0.0162 0.0900  -0.0464 83  HIS A CB    
587  C CG    A HIS A 83  ? 0.5487 0.5270 0.5715 -0.0128 0.0831  -0.0380 83  HIS A CG    
588  C CG    B HIS A 83  ? 0.5678 0.5405 0.6136 -0.0089 0.0855  -0.0439 83  HIS A CG    
589  N ND1   A HIS A 83  ? 0.6122 0.5880 0.6227 -0.0160 0.0891  -0.0379 83  HIS A ND1   
590  N ND1   B HIS A 83  ? 0.5980 0.5618 0.6557 -0.0075 0.0936  -0.0507 83  HIS A ND1   
591  C CD2   A HIS A 83  ? 0.5115 0.5051 0.5516 -0.0067 0.0713  -0.0298 83  HIS A CD2   
592  C CD2   B HIS A 83  ? 0.5470 0.5346 0.6115 -0.0025 0.0740  -0.0352 83  HIS A CD2   
593  C CE1   A HIS A 83  ? 0.4278 0.4172 0.4494 -0.0118 0.0806  -0.0303 83  HIS A CE1   
594  C CE1   B HIS A 83  ? 0.5460 0.5191 0.6288 -0.0006 0.0862  -0.0452 83  HIS A CE1   
595  N NE2   A HIS A 83  ? 0.5051 0.5051 0.5436 -0.0061 0.0698  -0.0257 83  HIS A NE2   
596  N NE2   B HIS A 83  ? 0.5196 0.5067 0.6051 0.0022  0.0744  -0.0358 83  HIS A NE2   
597  N N     . GLU A 84  ? 0.5041 0.4759 0.4836 -0.0230 0.0555  -0.0309 84  GLU A N     
598  C CA    . GLU A 84  ? 0.4549 0.4388 0.4410 -0.0209 0.0406  -0.0223 84  GLU A CA    
599  C C     . GLU A 84  ? 0.4981 0.4745 0.4686 -0.0280 0.0315  -0.0232 84  GLU A C     
600  O O     . GLU A 84  ? 0.5120 0.4974 0.4950 -0.0268 0.0223  -0.0182 84  GLU A O     
601  C CB    . GLU A 84  ? 0.4610 0.4541 0.4445 -0.0185 0.0347  -0.0150 84  GLU A CB    
602  C CG    . GLU A 84  ? 0.5088 0.5108 0.5108 -0.0118 0.0409  -0.0136 84  GLU A CG    
603  C CD    . GLU A 84  ? 0.5367 0.5436 0.5331 -0.0106 0.0369  -0.0080 84  GLU A CD    
604  O OE1   . GLU A 84  ? 0.5223 0.5205 0.4965 -0.0160 0.0359  -0.0076 84  GLU A OE1   
605  O OE2   . GLU A 84  ? 0.5086 0.5264 0.5217 -0.0044 0.0342  -0.0040 84  GLU A OE2   
606  N N     . LEU A 85  ? 0.4762 0.4354 0.4190 -0.0361 0.0339  -0.0296 85  LEU A N     
607  C CA    . LEU A 85  ? 0.5028 0.4531 0.4298 -0.0440 0.0233  -0.0312 85  LEU A CA    
608  C C     . LEU A 85  ? 0.5330 0.4776 0.4707 -0.0454 0.0261  -0.0372 85  LEU A C     
609  O O     . LEU A 85  ? 0.5248 0.4640 0.4552 -0.0519 0.0160  -0.0382 85  LEU A O     
610  C CB    . LEU A 85  ? 0.5668 0.4970 0.4556 -0.0529 0.0241  -0.0364 85  LEU A CB    
611  C CG    . LEU A 85  ? 0.5939 0.5275 0.4694 -0.0528 0.0178  -0.0288 85  LEU A CG    
612  C CD1   . LEU A 85  ? 0.6728 0.5830 0.5073 -0.0612 0.0231  -0.0340 85  LEU A CD1   
613  C CD2   . LEU A 85  ? 0.5627 0.5084 0.4453 -0.0531 -0.0020 -0.0196 85  LEU A CD2   
614  N N     . ARG A 86  ? 0.5349 0.4803 0.4913 -0.0394 0.0384  -0.0407 86  ARG A N     
615  C CA    . ARG A 86  ? 0.4891 0.4291 0.4590 -0.0396 0.0404  -0.0448 86  ARG A CA    
616  C C     . ARG A 86  ? 0.4572 0.4130 0.4511 -0.0357 0.0302  -0.0354 86  ARG A C     
617  O O     . ARG A 86  ? 0.4990 0.4508 0.5058 -0.0357 0.0312  -0.0368 86  ARG A O     
618  C CB    . ARG A 86  ? 0.4712 0.4059 0.4552 -0.0339 0.0566  -0.0511 86  ARG A CB    
619  C CG    . ARG A 86  ? 0.6449 0.5615 0.6057 -0.0384 0.0708  -0.0620 86  ARG A CG    
620  C CD    . ARG A 86  ? 0.7363 0.6488 0.7168 -0.0323 0.0886  -0.0689 86  ARG A CD    
621  N NE    . ARG A 86  ? 0.9445 0.8420 0.9036 -0.0364 0.1045  -0.0780 86  ARG A NE    
622  C CZ    . ARG A 86  ? 1.0588 0.9617 1.0308 -0.0317 0.1175  -0.0788 86  ARG A CZ    
623  N NH1   . ARG A 86  ? 0.9409 0.8631 0.9479 -0.0226 0.1157  -0.0719 86  ARG A NH1   
624  N NH2   . ARG A 86  ? 1.0514 0.9389 0.9997 -0.0370 0.1329  -0.0868 86  ARG A NH2   
625  N N     . TYR A 87  ? 0.4621 0.4340 0.4614 -0.0327 0.0218  -0.0259 87  TYR A N     
626  C CA    . TYR A 87  ? 0.4594 0.4458 0.4790 -0.0292 0.0143  -0.0168 87  TYR A CA    
627  C C     . TYR A 87  ? 0.5052 0.4996 0.5195 -0.0334 0.0018  -0.0112 87  TYR A C     
628  O O     . TYR A 87  ? 0.5010 0.4907 0.4960 -0.0377 -0.0026 -0.0129 87  TYR A O     
629  C CB    . TYR A 87  ? 0.4404 0.4395 0.4765 -0.0193 0.0179  -0.0105 87  TYR A CB    
630  C CG    . TYR A 87  ? 0.4648 0.4586 0.5120 -0.0141 0.0278  -0.0144 87  TYR A CG    
631  C CD1   . TYR A 87  ? 0.4600 0.4497 0.5031 -0.0122 0.0364  -0.0199 87  TYR A CD1   
632  C CD2   . TYR A 87  ? 0.4115 0.4045 0.4752 -0.0109 0.0285  -0.0118 87  TYR A CD2   
633  C CE1   . TYR A 87  ? 0.4817 0.4684 0.5408 -0.0069 0.0450  -0.0232 87  TYR A CE1   
634  C CE2   . TYR A 87  ? 0.4454 0.4338 0.5224 -0.0054 0.0357  -0.0145 87  TYR A CE2   
635  C CZ    . TYR A 87  ? 0.4676 0.4538 0.5441 -0.0031 0.0436  -0.0203 87  TYR A CZ    
636  O OH    . TYR A 87  ? 0.5049 0.4880 0.6001 0.0028  0.0503  -0.0227 87  TYR A OH    
637  N N     . ASN A 88  ? 0.4096 0.4159 0.4424 -0.0320 -0.0037 -0.0039 88  ASN A N     
638  C CA    . ASN A 88  ? 0.4117 0.4298 0.4482 -0.0337 -0.0144 0.0027  88  ASN A CA    
639  C C     . ASN A 88  ? 0.4464 0.4716 0.4769 -0.0282 -0.0147 0.0064  88  ASN A C     
640  O O     . ASN A 88  ? 0.4130 0.4401 0.4452 -0.0214 -0.0069 0.0068  88  ASN A O     
641  C CB    . ASN A 88  ? 0.3873 0.4180 0.4479 -0.0314 -0.0155 0.0103  88  ASN A CB    
642  C CG    . ASN A 88  ? 0.4711 0.5155 0.5417 -0.0324 -0.0247 0.0170  88  ASN A CG    
643  O OD1   . ASN A 88  ? 0.4199 0.4754 0.4966 -0.0255 -0.0234 0.0227  88  ASN A OD1   
644  N ND2   . ASN A 88  ? 0.3915 0.4349 0.4654 -0.0409 -0.0347 0.0161  88  ASN A ND2   
645  N N     . TYR A 89  ? 0.4417 0.4704 0.4662 -0.0314 -0.0250 0.0095  89  TYR A N     
646  C CA    . TYR A 89  ? 0.4199 0.4521 0.4364 -0.0271 -0.0260 0.0128  89  TYR A CA    
647  C C     . TYR A 89  ? 0.3985 0.4442 0.4320 -0.0176 -0.0211 0.0187  89  TYR A C     
648  O O     . TYR A 89  ? 0.4041 0.4502 0.4313 -0.0133 -0.0186 0.0198  89  TYR A O     
649  C CB    . TYR A 89  ? 0.4251 0.4591 0.4362 -0.0315 -0.0400 0.0168  89  TYR A CB    
650  C CG    . TYR A 89  ? 0.4499 0.5010 0.4873 -0.0291 -0.0475 0.0245  89  TYR A CG    
651  C CD1   . TYR A 89  ? 0.4587 0.5141 0.5120 -0.0342 -0.0522 0.0249  89  TYR A CD1   
652  C CD2   . TYR A 89  ? 0.4572 0.5195 0.5048 -0.0222 -0.0492 0.0312  89  TYR A CD2   
653  C CE1   . TYR A 89  ? 0.4522 0.5242 0.5329 -0.0324 -0.0573 0.0320  89  TYR A CE1   
654  C CE2   . TYR A 89  ? 0.4596 0.5376 0.5334 -0.0196 -0.0539 0.0378  89  TYR A CE2   
655  C CZ    . TYR A 89  ? 0.5006 0.5842 0.5919 -0.0248 -0.0575 0.0383  89  TYR A CZ    
656  O OH    . TYR A 89  ? 0.4387 0.5387 0.5594 -0.0224 -0.0602 0.0449  89  TYR A OH    
657  N N     . LEU A 90  ? 0.3995 0.4544 0.4524 -0.0149 -0.0193 0.0225  90  LEU A N     
658  C CA    . LEU A 90  ? 0.4031 0.4674 0.4667 -0.0063 -0.0140 0.0274  90  LEU A CA    
659  C C     . LEU A 90  ? 0.3962 0.4554 0.4575 -0.0019 -0.0053 0.0247  90  LEU A C     
660  O O     . LEU A 90  ? 0.4259 0.4896 0.4902 0.0048  -0.0021 0.0276  90  LEU A O     
661  C CB    . LEU A 90  ? 0.3322 0.4073 0.4154 -0.0053 -0.0142 0.0333  90  LEU A CB    
662  C CG    . LEU A 90  ? 0.4063 0.4915 0.5015 -0.0072 -0.0224 0.0378  90  LEU A CG    
663  C CD1   . LEU A 90  ? 0.3545 0.4498 0.4721 -0.0068 -0.0188 0.0429  90  LEU A CD1   
664  C CD2   . LEU A 90  ? 0.3458 0.4358 0.4389 -0.0012 -0.0241 0.0407  90  LEU A CD2   
665  N N     . GLN A 91  ? 0.4314 0.4805 0.4879 -0.0053 -0.0020 0.0190  91  GLN A N     
666  C CA    . GLN A 91  ? 0.4326 0.4777 0.4926 -0.0008 0.0050  0.0171  91  GLN A CA    
667  C C     . GLN A 91  ? 0.4666 0.5128 0.5224 0.0042  0.0075  0.0162  91  GLN A C     
668  O O     . GLN A 91  ? 0.3888 0.4379 0.4510 0.0101  0.0093  0.0187  91  GLN A O     
669  C CB    . GLN A 91  ? 0.4158 0.4489 0.4726 -0.0053 0.0087  0.0100  91  GLN A CB    
670  C CG    . GLN A 91  ? 0.3993 0.4285 0.4652 -0.0002 0.0149  0.0086  91  GLN A CG    
671  C CD    . GLN A 91  ? 0.4908 0.5199 0.5681 0.0010  0.0144  0.0134  91  GLN A CD    
672  O OE1   . GLN A 91  ? 0.4270 0.4536 0.5058 -0.0045 0.0124  0.0136  91  GLN A OE1   
673  N NE2   . GLN A 91  ? 0.4058 0.4365 0.4906 0.0077  0.0155  0.0176  91  GLN A NE2   
674  N N     . ARG A 92  ? 0.3805 0.4228 0.4243 0.0012  0.0074  0.0128  92  ARG A N     
675  C CA    . ARG A 92  ? 0.4315 0.4742 0.4727 0.0047  0.0103  0.0120  92  ARG A CA    
676  C C     . ARG A 92  ? 0.3964 0.4480 0.4421 0.0104  0.0068  0.0178  92  ARG A C     
677  O O     . ARG A 92  ? 0.4081 0.4605 0.4556 0.0142  0.0085  0.0175  92  ARG A O     
678  C CB    . ARG A 92  ? 0.4453 0.4805 0.4701 -0.0005 0.0113  0.0086  92  ARG A CB    
679  C CG    . ARG A 92  ? 0.4318 0.4694 0.4482 -0.0028 0.0027  0.0132  92  ARG A CG    
680  C CD    . ARG A 92  ? 0.4935 0.5194 0.4885 -0.0101 0.0014  0.0103  92  ARG A CD    
681  N NE    . ARG A 92  ? 0.6932 0.7145 0.6791 -0.0095 0.0061  0.0099  92  ARG A NE    
682  C CZ    . ARG A 92  ? 0.5871 0.6056 0.5610 -0.0108 0.0009  0.0140  92  ARG A CZ    
683  N NH1   . ARG A 92  ? 0.5056 0.5249 0.4743 -0.0129 -0.0103 0.0185  92  ARG A NH1   
684  N NH2   . ARG A 92  ? 0.5057 0.5201 0.4745 -0.0100 0.0067  0.0138  92  ARG A NH2   
685  N N     . PHE A 93  ? 0.3656 0.4233 0.4143 0.0108  0.0023  0.0227  93  PHE A N     
686  C CA    . PHE A 93  ? 0.3833 0.4478 0.4361 0.0165  0.0010  0.0274  93  PHE A CA    
687  C C     . PHE A 93  ? 0.3805 0.4472 0.4402 0.0208  0.0037  0.0301  93  PHE A C     
688  O O     . PHE A 93  ? 0.3658 0.4329 0.4240 0.0259  0.0045  0.0312  93  PHE A O     
689  C CB    . PHE A 93  ? 0.3128 0.3830 0.3678 0.0153  -0.0040 0.0313  93  PHE A CB    
690  C CG    . PHE A 93  ? 0.4122 0.4779 0.4567 0.0115  -0.0084 0.0302  93  PHE A CG    
691  C CD1   . PHE A 93  ? 0.3740 0.4368 0.4118 0.0142  -0.0077 0.0301  93  PHE A CD1   
692  C CD2   . PHE A 93  ? 0.3377 0.3997 0.3765 0.0046  -0.0135 0.0291  93  PHE A CD2   
693  C CE1   . PHE A 93  ? 0.4303 0.4864 0.4555 0.0103  -0.0113 0.0300  93  PHE A CE1   
694  C CE2   . PHE A 93  ? 0.4246 0.4792 0.4483 0.0006  -0.0182 0.0287  93  PHE A CE2   
695  C CZ    . PHE A 93  ? 0.4267 0.4782 0.4434 0.0035  -0.0166 0.0296  93  PHE A CZ    
696  N N     . TRP A 94  ? 0.3555 0.4217 0.4208 0.0183  0.0047  0.0312  94  TRP A N     
697  C CA    . TRP A 94  ? 0.4413 0.5059 0.5100 0.0216  0.0073  0.0342  94  TRP A CA    
698  C C     . TRP A 94  ? 0.4074 0.4671 0.4735 0.0255  0.0073  0.0321  94  TRP A C     
699  O O     . TRP A 94  ? 0.4364 0.4951 0.4993 0.0301  0.0068  0.0351  94  TRP A O     
700  C CB    . TRP A 94  ? 0.3590 0.4203 0.4339 0.0173  0.0085  0.0346  94  TRP A CB    
701  C CG    . TRP A 94  ? 0.4051 0.4723 0.4870 0.0132  0.0077  0.0377  94  TRP A CG    
702  C CD1   . TRP A 94  ? 0.4340 0.5098 0.5204 0.0150  0.0080  0.0419  94  TRP A CD1   
703  C CD2   . TRP A 94  ? 0.4303 0.4954 0.5188 0.0064  0.0065  0.0367  94  TRP A CD2   
704  N NE1   . TRP A 94  ? 0.4160 0.4970 0.5141 0.0099  0.0067  0.0441  94  TRP A NE1   
705  C CE2   . TRP A 94  ? 0.4692 0.5434 0.5677 0.0041  0.0050  0.0408  94  TRP A CE2   
706  C CE3   . TRP A 94  ? 0.5287 0.5844 0.6166 0.0021  0.0067  0.0321  94  TRP A CE3   
707  C CZ2   . TRP A 94  ? 0.3910 0.4659 0.4996 -0.0033 0.0021  0.0409  94  TRP A CZ2   
708  C CZ3   . TRP A 94  ? 0.4448 0.4990 0.5392 -0.0052 0.0044  0.0315  94  TRP A CZ3   
709  C CH2   . TRP A 94  ? 0.4320 0.4961 0.5369 -0.0081 0.0014  0.0360  94  TRP A CH2   
710  N N     . ARG A 95  ? 0.3558 0.4118 0.4235 0.0233  0.0079  0.0267  95  ARG A N     
711  C CA    . ARG A 95  ? 0.4513 0.5045 0.5228 0.0265  0.0078  0.0243  95  ARG A CA    
712  C C     . ARG A 95  ? 0.4207 0.4765 0.4882 0.0300  0.0051  0.0248  95  ARG A C     
713  O O     . ARG A 95  ? 0.3590 0.4133 0.4310 0.0332  0.0026  0.0243  95  ARG A O     
714  C CB    . ARG A 95  ? 0.4526 0.5020 0.5276 0.0227  0.0118  0.0177  95  ARG A CB    
715  C CG    . ARG A 95  ? 0.8369 0.8850 0.9225 0.0254  0.0132  0.0145  95  ARG A CG    
716  C CD    . ARG A 95  ? 0.7780 0.8210 0.8678 0.0216  0.0208  0.0074  95  ARG A CD    
717  N NE    . ARG A 95  ? 1.0384 1.0830 1.1380 0.0229  0.0239  0.0040  95  ARG A NE    
718  C CZ    . ARG A 95  ? 1.0511 1.0979 1.1693 0.0274  0.0223  0.0040  95  ARG A CZ    
719  N NH1   . ARG A 95  ? 0.9093 0.9547 1.0353 0.0313  0.0173  0.0077  95  ARG A NH1   
720  N NH2   . ARG A 95  ? 0.9535 1.0033 1.0836 0.0277  0.0251  0.0009  95  ARG A NH2   
721  N N     . LYS A 96  ? 0.3852 0.4441 0.4457 0.0296  0.0048  0.0257  96  LYS A N     
722  C CA    . LYS A 96  ? 0.3906 0.4500 0.4471 0.0323  0.0028  0.0252  96  LYS A CA    
723  C C     . LYS A 96  ? 0.4201 0.4800 0.4700 0.0366  0.0015  0.0290  96  LYS A C     
724  O O     . LYS A 96  ? 0.4420 0.5009 0.4870 0.0388  0.0002  0.0283  96  LYS A O     
725  C CB    . LYS A 96  ? 0.3780 0.4378 0.4305 0.0292  0.0037  0.0233  96  LYS A CB    
726  C CG    . LYS A 96  ? 0.3999 0.4563 0.4542 0.0248  0.0071  0.0187  96  LYS A CG    
727  C CD    . LYS A 96  ? 0.3480 0.4020 0.3928 0.0209  0.0077  0.0184  96  LYS A CD    
728  C CE    . LYS A 96  ? 0.4981 0.5462 0.5406 0.0159  0.0135  0.0136  96  LYS A CE    
729  N NZ    . LYS A 96  ? 0.5680 0.6134 0.6126 0.0132  0.0171  0.0104  96  LYS A NZ    
730  N N     . LEU A 97  ? 0.3746 0.4347 0.4238 0.0375  0.0031  0.0329  97  LEU A N     
731  C CA    . LEU A 97  ? 0.4241 0.4836 0.4656 0.0411  0.0051  0.0362  97  LEU A CA    
732  C C     . LEU A 97  ? 0.4264 0.4786 0.4576 0.0449  0.0017  0.0359  97  LEU A C     
733  O O     . LEU A 97  ? 0.4192 0.4676 0.4520 0.0449  -0.0026 0.0357  97  LEU A O     
734  C CB    . LEU A 97  ? 0.3566 0.4177 0.4006 0.0402  0.0095  0.0409  97  LEU A CB    
735  C CG    . LEU A 97  ? 0.3900 0.4588 0.4449 0.0362  0.0114  0.0418  97  LEU A CG    
736  C CD1   . LEU A 97  ? 0.3971 0.4667 0.4573 0.0342  0.0156  0.0464  97  LEU A CD1   
737  C CD2   . LEU A 97  ? 0.3703 0.4447 0.4275 0.0382  0.0125  0.0423  97  LEU A CD2   
738  N N     . PRO A 98  ? 0.4124 0.4614 0.4333 0.0481  0.0028  0.0355  98  PRO A N     
739  C CA    . PRO A 98  ? 0.3569 0.3964 0.3639 0.0509  -0.0017 0.0346  98  PRO A CA    
740  C C     . PRO A 98  ? 0.4025 0.4350 0.3977 0.0521  -0.0003 0.0395  98  PRO A C     
741  O O     . PRO A 98  ? 0.4541 0.4892 0.4507 0.0515  0.0071  0.0434  98  PRO A O     
742  C CB    . PRO A 98  ? 0.4127 0.4494 0.4109 0.0536  0.0013  0.0322  98  PRO A CB    
743  C CG    . PRO A 98  ? 0.4121 0.4563 0.4177 0.0539  0.0099  0.0350  98  PRO A CG    
744  C CD    . PRO A 98  ? 0.4062 0.4591 0.4277 0.0495  0.0084  0.0361  98  PRO A CD    
745  N N     . GLN A 99  ? 0.4002 0.4231 0.3837 0.0534  -0.0082 0.0396  99  GLN A N     
746  C CA    . GLN A 99  ? 0.4797 0.4912 0.4436 0.0548  -0.0077 0.0446  99  GLN A CA    
747  C C     . GLN A 99  ? 0.4704 0.4755 0.4153 0.0570  0.0014  0.0442  99  GLN A C     
748  O O     . GLN A 99  ? 0.4524 0.4597 0.3979 0.0583  0.0038  0.0393  99  GLN A O     
749  C CB    . GLN A 99  ? 0.4541 0.4551 0.4077 0.0557  -0.0211 0.0447  99  GLN A CB    
750  C CG    . GLN A 99  ? 0.5906 0.5976 0.5663 0.0546  -0.0296 0.0448  99  GLN A CG    
751  C CD    . GLN A 99  ? 0.7491 0.7467 0.7186 0.0559  -0.0446 0.0459  99  GLN A CD    
752  O OE1   . GLN A 99  ? 0.7070 0.6916 0.6509 0.0570  -0.0498 0.0467  99  GLN A OE1   
753  N NE2   . GLN A 99  ? 0.7326 0.7360 0.7258 0.0557  -0.0520 0.0459  99  GLN A NE2   
754  N N     . HIS A 100 ? 0.5298 0.5259 0.4578 0.0574  0.0077  0.0496  100 HIS A N     
755  C CA    . HIS A 100 ? 0.5137 0.4993 0.4184 0.0596  0.0173  0.0489  100 HIS A CA    
756  C C     . HIS A 100 ? 0.4940 0.4683 0.3800 0.0614  0.0089  0.0427  100 HIS A C     
757  O O     . HIS A 100 ? 0.5284 0.4947 0.4055 0.0607  -0.0051 0.0426  100 HIS A O     
758  C CB    . HIS A 100 ? 0.5337 0.5061 0.4164 0.0590  0.0230  0.0561  100 HIS A CB    
759  C CG    . HIS A 100 ? 0.5389 0.5208 0.4398 0.0565  0.0321  0.0623  100 HIS A CG    
760  N ND1   . HIS A 100 ? 0.5238 0.4959 0.4137 0.0546  0.0329  0.0702  100 HIS A ND1   
761  C CD2   . HIS A 100 ? 0.4961 0.4950 0.4251 0.0551  0.0395  0.0620  100 HIS A CD2   
762  C CE1   . HIS A 100 ? 0.5140 0.4972 0.4259 0.0518  0.0414  0.0739  100 HIS A CE1   
763  N NE2   . HIS A 100 ? 0.5316 0.5314 0.4674 0.0519  0.0448  0.0688  100 HIS A NE2   
764  N N     . GLY A 101 ? 0.5210 0.4946 0.4035 0.0637  0.0167  0.0374  101 GLY A N     
765  C CA    . GLY A 101 ? 0.5293 0.4910 0.3947 0.0650  0.0097  0.0305  101 GLY A CA    
766  C C     . GLY A 101 ? 0.5849 0.5563 0.4719 0.0641  0.0004  0.0254  101 GLY A C     
767  O O     . GLY A 101 ? 0.5518 0.5137 0.4276 0.0646  -0.0048 0.0192  101 GLY A O     
768  N N     . GLN A 102 ? 0.4827 0.4709 0.3985 0.0622  -0.0012 0.0275  102 GLN A N     
769  C CA    . GLN A 102 ? 0.4690 0.4657 0.4045 0.0605  -0.0080 0.0235  102 GLN A CA    
770  C C     . GLN A 102 ? 0.4850 0.4930 0.4380 0.0613  0.0009  0.0232  102 GLN A C     
771  O O     . GLN A 102 ? 0.4140 0.4275 0.3713 0.0625  0.0107  0.0267  102 GLN A O     
772  C CB    . GLN A 102 ? 0.4433 0.4480 0.3963 0.0575  -0.0169 0.0257  102 GLN A CB    
773  C CG    . GLN A 102 ? 0.5641 0.5593 0.5062 0.0570  -0.0290 0.0269  102 GLN A CG    
774  C CD    . GLN A 102 ? 0.7220 0.7101 0.6596 0.0562  -0.0400 0.0212  102 GLN A CD    
775  O OE1   . GLN A 102 ? 0.8097 0.8057 0.7669 0.0542  -0.0425 0.0176  102 GLN A OE1   
776  N NE2   . GLN A 102 ? 0.8103 0.7820 0.7207 0.0570  -0.0466 0.0202  102 GLN A NE2   
777  N N     . ILE A 103 ? 0.4296 0.4410 0.3941 0.0600  -0.0034 0.0196  103 ILE A N     
778  C CA    . ILE A 103 ? 0.4280 0.4471 0.4064 0.0607  0.0022  0.0197  103 ILE A CA    
779  C C     . ILE A 103 ? 0.3877 0.4174 0.3843 0.0564  -0.0015 0.0211  103 ILE A C     
780  O O     . ILE A 103 ? 0.4563 0.4851 0.4567 0.0535  -0.0082 0.0189  103 ILE A O     
781  C CB    . ILE A 103 ? 0.4704 0.4808 0.4433 0.0626  0.0016  0.0147  103 ILE A CB    
782  C CG1   . ILE A 103 ? 0.4280 0.4251 0.3796 0.0668  0.0069  0.0118  103 ILE A CG1   
783  C CG2   . ILE A 103 ? 0.4348 0.4525 0.4231 0.0634  0.0054  0.0162  103 ILE A CG2   
784  C CD1   . ILE A 103 ? 0.4808 0.4656 0.4241 0.0685  0.0054  0.0055  103 ILE A CD1   
785  N N     . ALA A 104 ? 0.3587 0.3976 0.3665 0.0558  0.0031  0.0245  104 ALA A N     
786  C CA    . ALA A 104 ? 0.4053 0.4511 0.4253 0.0515  0.0008  0.0252  104 ALA A CA    
787  C C     . ALA A 104 ? 0.4297 0.4778 0.4553 0.0523  0.0024  0.0266  104 ALA A C     
788  O O     . ALA A 104 ? 0.4424 0.4941 0.4716 0.0554  0.0065  0.0293  104 ALA A O     
789  C CB    . ALA A 104 ? 0.3403 0.3930 0.3670 0.0487  0.0019  0.0282  104 ALA A CB    
790  N N     . VAL A 105 ? 0.3729 0.4188 0.4004 0.0494  -0.0006 0.0254  105 VAL A N     
791  C CA    . VAL A 105 ? 0.3356 0.3817 0.3669 0.0496  -0.0010 0.0278  105 VAL A CA    
792  C C     . VAL A 105 ? 0.4208 0.4704 0.4546 0.0437  -0.0030 0.0298  105 VAL A C     
793  O O     . VAL A 105 ? 0.4210 0.4685 0.4532 0.0393  -0.0031 0.0274  105 VAL A O     
794  C CB    . VAL A 105 ? 0.4726 0.5094 0.5001 0.0505  -0.0024 0.0255  105 VAL A CB    
795  C CG1   . VAL A 105 ? 0.3920 0.4274 0.4230 0.0512  -0.0037 0.0294  105 VAL A CG1   
796  C CG2   . VAL A 105 ? 0.4351 0.4654 0.4561 0.0558  -0.0005 0.0220  105 VAL A CG2   
797  N N     . PHE A 106 ? 0.3957 0.4501 0.4340 0.0435  -0.0044 0.0339  106 PHE A N     
798  C CA    . PHE A 106 ? 0.4217 0.4767 0.4578 0.0374  -0.0072 0.0356  106 PHE A CA    
799  C C     . PHE A 106 ? 0.4327 0.4824 0.4656 0.0368  -0.0115 0.0392  106 PHE A C     
800  O O     . PHE A 106 ? 0.4176 0.4706 0.4578 0.0403  -0.0150 0.0434  106 PHE A O     
801  C CB    . PHE A 106 ? 0.3617 0.4249 0.4044 0.0362  -0.0081 0.0376  106 PHE A CB    
802  C CG    . PHE A 106 ? 0.3837 0.4495 0.4278 0.0358  -0.0042 0.0350  106 PHE A CG    
803  C CD1   . PHE A 106 ? 0.4024 0.4658 0.4429 0.0307  -0.0034 0.0321  106 PHE A CD1   
804  C CD2   . PHE A 106 ? 0.3702 0.4390 0.4182 0.0407  -0.0006 0.0355  106 PHE A CD2   
805  C CE1   . PHE A 106 ? 0.3660 0.4308 0.4095 0.0310  -0.0007 0.0304  106 PHE A CE1   
806  C CE2   . PHE A 106 ? 0.3697 0.4388 0.4170 0.0402  0.0019  0.0343  106 PHE A CE2   
807  C CZ    . PHE A 106 ? 0.3685 0.4359 0.4148 0.0357  0.0011  0.0321  106 PHE A CZ    
808  N N     . ASP A 107 ? 0.4093 0.4504 0.4326 0.0325  -0.0110 0.0380  107 ASP A N     
809  C CA    . ASP A 107 ? 0.4237 0.4566 0.4394 0.0303  -0.0153 0.0424  107 ASP A CA    
810  C C     . ASP A 107 ? 0.4224 0.4549 0.4298 0.0243  -0.0193 0.0447  107 ASP A C     
811  O O     . ASP A 107 ? 0.4806 0.5073 0.4765 0.0179  -0.0157 0.0419  107 ASP A O     
812  C CB    . ASP A 107 ? 0.4339 0.4565 0.4420 0.0272  -0.0114 0.0404  107 ASP A CB    
813  C CG    . ASP A 107 ? 0.4727 0.4840 0.4712 0.0253  -0.0152 0.0460  107 ASP A CG    
814  O OD1   . ASP A 107 ? 0.4687 0.4795 0.4641 0.0255  -0.0223 0.0516  107 ASP A OD1   
815  O OD2   . ASP A 107 ? 0.5352 0.5373 0.5296 0.0233  -0.0118 0.0454  107 ASP A OD2   
816  N N     . ARG A 108 ? 0.4052 0.4435 0.4195 0.0262  -0.0265 0.0492  108 ARG A N     
817  C CA    . ARG A 108 ? 0.4300 0.4708 0.4410 0.0211  -0.0322 0.0504  108 ARG A CA    
818  C C     . ARG A 108 ? 0.4942 0.5436 0.5130 0.0206  -0.0267 0.0456  108 ARG A C     
819  O O     . ARG A 108 ? 0.4462 0.4968 0.4678 0.0229  -0.0190 0.0413  108 ARG A O     
820  C CB    . ARG A 108 ? 0.4065 0.4337 0.3941 0.0127  -0.0344 0.0507  108 ARG A CB    
821  C CG    . ARG A 108 ? 0.5106 0.5269 0.4882 0.0130  -0.0399 0.0569  108 ARG A CG    
822  C CD    . ARG A 108 ? 0.6406 0.6402 0.5897 0.0040  -0.0405 0.0577  108 ARG A CD    
823  N NE    . ARG A 108 ? 0.7120 0.7081 0.6498 -0.0009 -0.0524 0.0612  108 ARG A NE    
824  C CZ    . ARG A 108 ? 0.9590 0.9380 0.8674 -0.0089 -0.0560 0.0633  108 ARG A CZ    
825  N NH1   . ARG A 108 ? 0.8551 0.8194 0.7438 -0.0128 -0.0469 0.0628  108 ARG A NH1   
826  N NH2   . ARG A 108 ? 0.6487 0.6241 0.5464 -0.0137 -0.0692 0.0660  108 ARG A NH2   
827  N N     . SER A 109 ? 0.4373 0.4920 0.4604 0.0175  -0.0317 0.0466  109 SER A N     
828  C CA    . SER A 109 ? 0.3879 0.4524 0.4246 0.0192  -0.0273 0.0444  109 SER A CA    
829  C C     . SER A 109 ? 0.4721 0.5380 0.5087 0.0126  -0.0328 0.0441  109 SER A C     
830  O O     . SER A 109 ? 0.3856 0.4428 0.4068 0.0062  -0.0390 0.0440  109 SER A O     
831  C CB    . SER A 109 ? 0.3898 0.4644 0.4454 0.0270  -0.0260 0.0477  109 SER A CB    
832  O OG    . SER A 109 ? 0.3850 0.4655 0.4526 0.0272  -0.0347 0.0531  109 SER A OG    
833  N N     . TRP A 110 ? 0.3736 0.4491 0.4259 0.0137  -0.0306 0.0441  110 TRP A N     
834  C CA    . TRP A 110 ? 0.3890 0.4665 0.4451 0.0073  -0.0364 0.0440  110 TRP A CA    
835  C C     . TRP A 110 ? 0.4727 0.5533 0.5346 0.0050  -0.0496 0.0492  110 TRP A C     
836  O O     . TRP A 110 ? 0.4632 0.5411 0.5212 -0.0024 -0.0581 0.0486  110 TRP A O     
837  C CB    . TRP A 110 ? 0.3610 0.4480 0.4351 0.0091  -0.0304 0.0442  110 TRP A CB    
838  C CG    . TRP A 110 ? 0.4102 0.5071 0.5009 0.0171  -0.0249 0.0480  110 TRP A CG    
839  C CD1   . TRP A 110 ? 0.3971 0.5056 0.5097 0.0194  -0.0271 0.0529  110 TRP A CD1   
840  C CD2   . TRP A 110 ? 0.4329 0.5278 0.5194 0.0237  -0.0158 0.0467  110 TRP A CD2   
841  N NE1   . TRP A 110 ? 0.3797 0.4924 0.5001 0.0272  -0.0178 0.0543  110 TRP A NE1   
842  C CE2   . TRP A 110 ? 0.4001 0.5037 0.5025 0.0297  -0.0116 0.0504  110 TRP A CE2   
843  C CE3   . TRP A 110 ? 0.4119 0.4985 0.4838 0.0248  -0.0110 0.0426  110 TRP A CE3   
844  C CZ2   . TRP A 110 ? 0.3751 0.4766 0.4738 0.0363  -0.0031 0.0495  110 TRP A CZ2   
845  C CZ3   . TRP A 110 ? 0.3958 0.4818 0.4668 0.0313  -0.0047 0.0423  110 TRP A CZ3   
846  C CH2   . TRP A 110 ? 0.3704 0.4626 0.4520 0.0367  -0.0009 0.0455  110 TRP A CH2   
847  N N     . TYR A 111 ? 0.4316 0.5167 0.5026 0.0111  -0.0526 0.0543  111 TYR A N     
848  C CA    . TYR A 111 ? 0.4247 0.5127 0.5041 0.0099  -0.0669 0.0603  111 TYR A CA    
849  C C     . TYR A 111 ? 0.4350 0.5074 0.4864 0.0027  -0.0773 0.0604  111 TYR A C     
850  O O     . TYR A 111 ? 0.4732 0.5455 0.5273 -0.0002 -0.0925 0.0656  111 TYR A O     
851  C CB    . TYR A 111 ? 0.4344 0.5291 0.5312 0.0193  -0.0664 0.0655  111 TYR A CB    
852  C CG    . TYR A 111 ? 0.4083 0.5186 0.5346 0.0253  -0.0583 0.0666  111 TYR A CG    
853  C CD1   . TYR A 111 ? 0.4403 0.5642 0.5947 0.0245  -0.0654 0.0710  111 TYR A CD1   
854  C CD2   . TYR A 111 ? 0.4160 0.5269 0.5417 0.0309  -0.0433 0.0631  111 TYR A CD2   
855  C CE1   . TYR A 111 ? 0.3920 0.5297 0.5738 0.0295  -0.0551 0.0719  111 TYR A CE1   
856  C CE2   . TYR A 111 ? 0.4047 0.5270 0.5525 0.0357  -0.0341 0.0640  111 TYR A CE2   
857  C CZ    . TYR A 111 ? 0.4044 0.5402 0.5804 0.0350  -0.0387 0.0684  111 TYR A CZ    
858  O OH    . TYR A 111 ? 0.3836 0.5301 0.5816 0.0394  -0.0267 0.0694  111 TYR A OH    
859  N N     . GLY A 112 ? 0.4326 0.4913 0.4576 -0.0007 -0.0696 0.0551  112 GLY A N     
860  C CA    . GLY A 112 ? 0.4937 0.5355 0.4885 -0.0092 -0.0766 0.0540  112 GLY A CA    
861  C C     . GLY A 112 ? 0.5823 0.6228 0.5744 -0.0174 -0.0874 0.0526  112 GLY A C     
862  O O     . GLY A 112 ? 0.5487 0.5766 0.5193 -0.0242 -0.1000 0.0544  112 GLY A O     
863  N N     . ARG A 113 ? 0.5060 0.5581 0.5189 -0.0174 -0.0835 0.0497  113 ARG A N     
864  C CA    . ARG A 113 ? 0.5056 0.5573 0.5203 -0.0256 -0.0941 0.0481  113 ARG A CA    
865  C C     . ARG A 113 ? 0.5123 0.5691 0.5381 -0.0274 -0.1141 0.0557  113 ARG A C     
866  O O     . ARG A 113 ? 0.5721 0.6211 0.5862 -0.0365 -0.1280 0.0546  113 ARG A O     
867  C CB    . ARG A 113 ? 0.4730 0.5378 0.5136 -0.0242 -0.0858 0.0456  113 ARG A CB    
868  C CG    . ARG A 113 ? 0.4698 0.5331 0.5136 -0.0335 -0.0947 0.0427  113 ARG A CG    
869  C CD    . ARG A 113 ? 0.5551 0.5995 0.5691 -0.0408 -0.0890 0.0335  113 ARG A CD    
870  N NE    . ARG A 113 ? 0.4599 0.5049 0.4843 -0.0471 -0.0901 0.0293  113 ARG A NE    
871  C CZ    . ARG A 113 ? 0.5596 0.5883 0.5632 -0.0537 -0.0855 0.0206  113 ARG A CZ    
872  N NH1   . ARG A 113 ? 0.5086 0.5198 0.4804 -0.0551 -0.0784 0.0149  113 ARG A NH1   
873  N NH2   . ARG A 113 ? 0.5053 0.5345 0.5214 -0.0592 -0.0868 0.0173  113 ARG A NH2   
874  N N     . VAL A 114 ? 0.4883 0.5576 0.5375 -0.0189 -0.1166 0.0631  114 VAL A N     
875  C CA    . VAL A 114 ? 0.5375 0.6140 0.6047 -0.0191 -0.1361 0.0711  114 VAL A CA    
876  C C     . VAL A 114 ? 0.5117 0.5779 0.5630 -0.0159 -0.1444 0.0775  114 VAL A C     
877  O O     . VAL A 114 ? 0.5430 0.6157 0.6128 -0.0135 -0.1603 0.0856  114 VAL A O     
878  C CB    . VAL A 114 ? 0.5366 0.6374 0.6518 -0.0120 -0.1335 0.0754  114 VAL A CB    
879  C CG1   . VAL A 114 ? 0.4585 0.5678 0.5888 -0.0164 -0.1263 0.0704  114 VAL A CG1   
880  C CG2   . VAL A 114 ? 0.4191 0.5260 0.5455 -0.0002 -0.1181 0.0769  114 VAL A CG2   
881  N N     . LEU A 115 ? 0.5113 0.5616 0.5310 -0.0156 -0.1339 0.0745  115 LEU A N     
882  C CA    . LEU A 115 ? 0.5566 0.5944 0.5585 -0.0134 -0.1402 0.0808  115 LEU A CA    
883  C C     . LEU A 115 ? 0.5877 0.6006 0.5422 -0.0237 -0.1433 0.0778  115 LEU A C     
884  O O     . LEU A 115 ? 0.6515 0.6554 0.5905 -0.0319 -0.1606 0.0796  115 LEU A O     
885  C CB    . LEU A 115 ? 0.5186 0.5597 0.5288 -0.0037 -0.1240 0.0808  115 LEU A CB    
886  C CG    . LEU A 115 ? 0.5407 0.6028 0.5933 0.0070  -0.1194 0.0834  115 LEU A CG    
887  C CD1   . LEU A 115 ? 0.4034 0.4648 0.4570 0.0151  -0.1026 0.0810  115 LEU A CD1   
888  C CD2   . LEU A 115 ? 0.4563 0.5253 0.5320 0.0108  -0.1371 0.0930  115 LEU A CD2   
889  N N     . VAL A 116 ? 0.6037 0.6041 0.5337 -0.0242 -0.1267 0.0729  116 VAL A N     
890  C CA    . VAL A 116 ? 0.6333 0.6083 0.5171 -0.0337 -0.1265 0.0704  116 VAL A CA    
891  C C     . VAL A 116 ? 0.6559 0.6237 0.5230 -0.0436 -0.1293 0.0627  116 VAL A C     
892  O O     . VAL A 116 ? 0.6579 0.6053 0.4890 -0.0529 -0.1397 0.0629  116 VAL A O     
893  C CB    . VAL A 116 ? 0.6297 0.5961 0.4988 -0.0320 -0.1055 0.0660  116 VAL A CB    
894  C CG1   . VAL A 116 ? 0.6476 0.6263 0.5350 -0.0292 -0.0878 0.0566  116 VAL A CG1   
895  C CG2   . VAL A 116 ? 0.7936 0.7330 0.6153 -0.0418 -0.1029 0.0641  116 VAL A CG2   
896  N N     . GLU A 117 ? 0.5221 0.5044 0.4129 -0.0421 -0.1204 0.0560  117 GLU A N     
897  C CA    . GLU A 117 ? 0.6383 0.6125 0.5147 -0.0513 -0.1219 0.0479  117 GLU A CA    
898  C C     . GLU A 117 ? 0.6331 0.6090 0.5144 -0.0571 -0.1461 0.0522  117 GLU A C     
899  O O     . GLU A 117 ? 0.6833 0.6426 0.5368 -0.0676 -0.1539 0.0471  117 GLU A O     
900  C CB    . GLU A 117 ? 0.6453 0.6332 0.5467 -0.0479 -0.1061 0.0406  117 GLU A CB    
901  C CG    . GLU A 117 ? 0.5909 0.5752 0.4857 -0.0435 -0.0843 0.0356  117 GLU A CG    
902  C CD    . GLU A 117 ? 0.7341 0.7312 0.6537 -0.0390 -0.0703 0.0299  117 GLU A CD    
903  O OE1   . GLU A 117 ? 0.7484 0.7527 0.6834 -0.0413 -0.0745 0.0279  117 GLU A OE1   
904  O OE2   . GLU A 117 ? 0.7443 0.7434 0.6678 -0.0336 -0.0557 0.0279  117 GLU A OE2   
905  N N     . ARG A 118 ? 0.5888 0.5837 0.5055 -0.0508 -0.1583 0.0610  118 ARG A N     
906  C CA    . ARG A 118 ? 0.6328 0.6296 0.5569 -0.0563 -0.1837 0.0664  118 ARG A CA    
907  C C     . ARG A 118 ? 0.6908 0.6647 0.5755 -0.0618 -0.2006 0.0723  118 ARG A C     
908  O O     . ARG A 118 ? 0.6954 0.6532 0.5525 -0.0726 -0.2168 0.0706  118 ARG A O     
909  C CB    . ARG A 118 ? 0.5489 0.5732 0.5262 -0.0473 -0.1904 0.0744  118 ARG A CB    
910  C CG    . ARG A 118 ? 0.6505 0.6784 0.6408 -0.0513 -0.2190 0.0824  118 ARG A CG    
911  C CD    . ARG A 118 ? 0.6679 0.7225 0.7128 -0.0408 -0.2230 0.0910  118 ARG A CD    
912  N NE    . ARG A 118 ? 0.7208 0.7787 0.7805 -0.0436 -0.2519 0.1000  118 ARG A NE    
913  C CZ    . ARG A 118 ? 0.6916 0.7725 0.8025 -0.0359 -0.2604 0.1081  118 ARG A CZ    
914  N NH1   . ARG A 118 ? 0.6297 0.7313 0.7791 -0.0250 -0.2409 0.1081  118 ARG A NH1   
915  N NH2   . ARG A 118 ? 0.7224 0.8051 0.8462 -0.0393 -0.2891 0.1164  118 ARG A NH2   
916  N N     . ILE A 119 ? 0.6512 0.6211 0.5297 -0.0550 -0.1967 0.0792  119 ILE A N     
917  C CA    . ILE A 119 ? 0.7384 0.6860 0.5806 -0.0593 -0.2130 0.0872  119 ILE A CA    
918  C C     . ILE A 119 ? 0.7285 0.6450 0.5116 -0.0712 -0.2084 0.0799  119 ILE A C     
919  O O     . ILE A 119 ? 0.7907 0.6861 0.5380 -0.0801 -0.2277 0.0836  119 ILE A O     
920  C CB    . ILE A 119 ? 0.8392 0.7876 0.6878 -0.0493 -0.2059 0.0952  119 ILE A CB    
921  C CG1   . ILE A 119 ? 0.8638 0.8305 0.7545 -0.0408 -0.2239 0.1066  119 ILE A CG1   
922  C CG2   . ILE A 119 ? 0.8972 0.8147 0.6928 -0.0554 -0.2080 0.0992  119 ILE A CG2   
923  C CD1   . ILE A 119 ? 0.7668 0.7641 0.7121 -0.0326 -0.2164 0.1041  119 ILE A CD1   
924  N N     . GLU A 120 ? 0.7860 0.6983 0.5574 -0.0717 -0.1826 0.0696  120 GLU A N     
925  C CA    . GLU A 120 ? 0.8184 0.7008 0.5355 -0.0822 -0.1739 0.0619  120 GLU A CA    
926  C C     . GLU A 120 ? 0.8190 0.6941 0.5233 -0.0920 -0.1792 0.0519  120 GLU A C     
927  O O     . GLU A 120 ? 0.8613 0.7095 0.5185 -0.1015 -0.1724 0.0442  120 GLU A O     
928  C CB    . GLU A 120 ? 0.7467 0.6269 0.4591 -0.0784 -0.1437 0.0553  120 GLU A CB    
929  C CG    . GLU A 120 ? 0.8293 0.7082 0.5419 -0.0717 -0.1380 0.0642  120 GLU A CG    
930  C CD    . GLU A 120 ? 1.0238 0.8739 0.6885 -0.0789 -0.1500 0.0721  120 GLU A CD    
931  O OE1   . GLU A 120 ? 1.1478 0.9713 0.7648 -0.0893 -0.1441 0.0661  120 GLU A OE1   
932  O OE2   . GLU A 120 ? 0.9768 0.8289 0.6501 -0.0742 -0.1651 0.0843  120 GLU A OE2   
933  N N     . GLY A 121 ? 0.7745 0.6715 0.5190 -0.0904 -0.1901 0.0515  121 GLY A N     
934  C CA    . GLY A 121 ? 0.7705 0.6612 0.5070 -0.0997 -0.1938 0.0414  121 GLY A CA    
935  C C     . GLY A 121 ? 0.8035 0.6934 0.5407 -0.0993 -0.1671 0.0286  121 GLY A C     
936  O O     . GLY A 121 ? 0.8622 0.7396 0.5830 -0.1080 -0.1674 0.0187  121 GLY A O     
937  N N     . PHE A 122 ? 0.7447 0.6466 0.5007 -0.0895 -0.1448 0.0283  122 PHE A N     
938  C CA    . PHE A 122 ? 0.8052 0.7088 0.5684 -0.0880 -0.1213 0.0173  122 PHE A CA    
939  C C     . PHE A 122 ? 0.7631 0.6868 0.5665 -0.0864 -0.1245 0.0148  122 PHE A C     
940  O O     . PHE A 122 ? 0.8624 0.7792 0.6619 -0.0906 -0.1151 0.0047  122 PHE A O     
941  C CB    . PHE A 122 ? 0.7372 0.6502 0.5144 -0.0780 -0.1001 0.0186  122 PHE A CB    
942  C CG    . PHE A 122 ? 0.7946 0.6880 0.5352 -0.0799 -0.0932 0.0208  122 PHE A CG    
943  C CD1   . PHE A 122 ? 0.8205 0.6843 0.5106 -0.0908 -0.0973 0.0177  122 PHE A CD1   
944  C CD2   . PHE A 122 ? 0.7761 0.6790 0.5314 -0.0714 -0.0824 0.0261  122 PHE A CD2   
945  C CE1   . PHE A 122 ? 0.8779 0.7224 0.5332 -0.0931 -0.0893 0.0205  122 PHE A CE1   
946  C CE2   . PHE A 122 ? 0.9196 0.8042 0.6434 -0.0737 -0.0753 0.0287  122 PHE A CE2   
947  C CZ    . PHE A 122 ? 0.8665 0.7221 0.5404 -0.0845 -0.0780 0.0264  122 PHE A CZ    
948  N N     . ALA A 123 ? 0.6735 0.6213 0.5164 -0.0803 -0.1362 0.0239  123 ALA A N     
949  C CA    . ALA A 123 ? 0.6817 0.6479 0.5625 -0.0802 -0.1415 0.0234  123 ALA A CA    
950  C C     . ALA A 123 ? 0.7698 0.7314 0.6464 -0.0898 -0.1678 0.0258  123 ALA A C     
951  O O     . ALA A 123 ? 0.7376 0.6975 0.6072 -0.0903 -0.1854 0.0342  123 ALA A O     
952  C CB    . ALA A 123 ? 0.5903 0.5847 0.5173 -0.0685 -0.1374 0.0316  123 ALA A CB    
953  N N     . THR A 124 ? 0.6841 0.6428 0.5654 -0.0977 -0.1715 0.0186  124 THR A N     
954  C CA    . THR A 124 ? 0.6900 0.6469 0.5739 -0.1075 -0.1979 0.0205  124 THR A CA    
955  C C     . THR A 124 ? 0.6958 0.6827 0.6320 -0.1012 -0.2107 0.0321  124 THR A C     
956  O O     . THR A 124 ? 0.6031 0.6111 0.5728 -0.0900 -0.1966 0.0369  124 THR A O     
957  C CB    . THR A 124 ? 0.7974 0.7462 0.6809 -0.1170 -0.1974 0.0099  124 THR A CB    
958  O OG1   . THR A 124 ? 0.7395 0.7118 0.6700 -0.1106 -0.1845 0.0108  124 THR A OG1   
959  C CG2   . THR A 124 ? 0.7115 0.6310 0.5478 -0.1220 -0.1811 -0.0028 124 THR A CG2   
960  N N     . LYS A 125 ? 0.6501 0.6380 0.5934 -0.1090 -0.2378 0.0362  125 LYS A N     
961  C CA    . LYS A 125 ? 0.6821 0.6989 0.6792 -0.1036 -0.2508 0.0471  125 LYS A CA    
962  C C     . LYS A 125 ? 0.6705 0.7115 0.7164 -0.0991 -0.2350 0.0460  125 LYS A C     
963  O O     . LYS A 125 ? 0.6360 0.7009 0.7218 -0.0885 -0.2274 0.0536  125 LYS A O     
964  C CB    . LYS A 125 ? 0.6662 0.6800 0.6659 -0.1143 -0.2841 0.0506  125 LYS A CB    
965  C CG    . LYS A 125 ? 0.7219 0.7661 0.7805 -0.1082 -0.2990 0.0628  125 LYS A CG    
966  C CD    . LYS A 125 ? 0.8946 0.9352 0.9561 -0.1186 -0.3354 0.0674  125 LYS A CD    
967  C CE    . LYS A 125 ? 0.9385 1.0098 1.0614 -0.1109 -0.3498 0.0804  125 LYS A CE    
968  N NZ    . LYS A 125 ? 1.0257 1.0970 1.1605 -0.1212 -0.3873 0.0852  125 LYS A NZ    
969  N N     . ASP A 126 ? 0.5862 0.6197 0.6281 -0.1072 -0.2293 0.0367  126 ASP A N     
970  C CA    . ASP A 126 ? 0.6598 0.7134 0.7448 -0.1038 -0.2140 0.0365  126 ASP A CA    
971  C C     . ASP A 126 ? 0.5613 0.6223 0.6504 -0.0907 -0.1868 0.0375  126 ASP A C     
972  O O     . ASP A 126 ? 0.5705 0.6540 0.6997 -0.0829 -0.1768 0.0433  126 ASP A O     
973  C CB    . ASP A 126 ? 0.6876 0.7271 0.7625 -0.1149 -0.2121 0.0261  126 ASP A CB    
974  C CG    . ASP A 126 ? 0.9349 0.9911 1.0487 -0.1113 -0.1938 0.0263  126 ASP A CG    
975  O OD1   . ASP A 126 ? 0.8940 0.9733 1.0548 -0.1110 -0.1995 0.0335  126 ASP A OD1   
976  O OD2   . ASP A 126 ? 0.8103 0.8562 0.9086 -0.1087 -0.1734 0.0199  126 ASP A OD2   
977  N N     . GLU A 127 ? 0.5617 0.6032 0.6091 -0.0887 -0.1750 0.0318  127 GLU A N     
978  C CA    . GLU A 127 ? 0.5924 0.6386 0.6409 -0.0774 -0.1512 0.0318  127 GLU A CA    
979  C C     . GLU A 127 ? 0.5877 0.6525 0.6598 -0.0662 -0.1502 0.0418  127 GLU A C     
980  O O     . GLU A 127 ? 0.5448 0.6273 0.6479 -0.0582 -0.1372 0.0453  127 GLU A O     
981  C CB    . GLU A 127 ? 0.5658 0.5877 0.5674 -0.0786 -0.1413 0.0240  127 GLU A CB    
982  C CG    . GLU A 127 ? 0.6428 0.6490 0.6295 -0.0855 -0.1321 0.0130  127 GLU A CG    
983  C CD    . GLU A 127 ? 0.6858 0.6667 0.6273 -0.0879 -0.1222 0.0043  127 GLU A CD    
984  O OE1   . GLU A 127 ? 0.7955 0.7664 0.7097 -0.0882 -0.1275 0.0064  127 GLU A OE1   
985  O OE2   . GLU A 127 ? 0.7458 0.7161 0.6799 -0.0894 -0.1083 -0.0044 127 GLU A OE2   
986  N N     . TRP A 128 ? 0.5473 0.6068 0.6040 -0.0656 -0.1638 0.0466  128 TRP A N     
987  C CA    . TRP A 128 ? 0.5479 0.6231 0.6272 -0.0544 -0.1617 0.0554  128 TRP A CA    
988  C C     . TRP A 128 ? 0.5442 0.6440 0.6739 -0.0520 -0.1703 0.0627  128 TRP A C     
989  O O     . TRP A 128 ? 0.5069 0.6234 0.6652 -0.0417 -0.1596 0.0677  128 TRP A O     
990  C CB    . TRP A 128 ? 0.5907 0.6523 0.6409 -0.0535 -0.1726 0.0596  128 TRP A CB    
991  C CG    . TRP A 128 ? 0.6282 0.6826 0.6695 -0.0615 -0.2000 0.0640  128 TRP A CG    
992  C CD1   . TRP A 128 ? 0.6686 0.6977 0.6647 -0.0723 -0.2117 0.0597  128 TRP A CD1   
993  C CD2   . TRP A 128 ? 0.6299 0.7009 0.7070 -0.0592 -0.2197 0.0739  128 TRP A CD2   
994  N NE1   . TRP A 128 ? 0.6973 0.7253 0.6963 -0.0774 -0.2396 0.0666  128 TRP A NE1   
995  C CE2   . TRP A 128 ? 0.6605 0.7152 0.7117 -0.0693 -0.2455 0.0756  128 TRP A CE2   
996  C CE3   . TRP A 128 ? 0.5780 0.6754 0.7070 -0.0496 -0.2176 0.0812  128 TRP A CE3   
997  C CZ2   . TRP A 128 ? 0.6191 0.6846 0.6978 -0.0699 -0.2715 0.0852  128 TRP A CZ2   
998  C CZ3   . TRP A 128 ? 0.6210 0.7301 0.7799 -0.0497 -0.2411 0.0902  128 TRP A CZ3   
999  C CH2   . TRP A 128 ? 0.5962 0.6900 0.7312 -0.0596 -0.2688 0.0925  128 TRP A CH2   
1000 N N     . SER A 129 ? 0.5180 0.6202 0.6605 -0.0618 -0.1882 0.0628  129 SER A N     
1001 C CA    . SER A 129 ? 0.4833 0.6105 0.6792 -0.0603 -0.1960 0.0697  129 SER A CA    
1002 C C     . SER A 129 ? 0.4713 0.6146 0.6988 -0.0555 -0.1736 0.0688  129 SER A C     
1003 O O     . SER A 129 ? 0.4679 0.6321 0.7355 -0.0476 -0.1674 0.0753  129 SER A O     
1004 C CB    . SER A 129 ? 0.4735 0.5988 0.6764 -0.0734 -0.2207 0.0691  129 SER A CB    
1005 O OG    . SER A 129 ? 0.6869 0.8004 0.8675 -0.0766 -0.2445 0.0730  129 SER A OG    
1006 N N     . ARG A 130 ? 0.4195 0.5520 0.6294 -0.0603 -0.1608 0.0611  130 ARG A N     
1007 C CA    . ARG A 130 ? 0.4746 0.6188 0.7092 -0.0564 -0.1400 0.0610  130 ARG A CA    
1008 C C     . ARG A 130 ? 0.4412 0.5846 0.6639 -0.0445 -0.1190 0.0612  130 ARG A C     
1009 O O     . ARG A 130 ? 0.4476 0.6009 0.6899 -0.0394 -0.1017 0.0628  130 ARG A O     
1010 C CB    . ARG A 130 ? 0.4107 0.5424 0.6328 -0.0661 -0.1363 0.0534  130 ARG A CB    
1011 C CG    . ARG A 130 ? 0.4880 0.5961 0.6628 -0.0662 -0.1275 0.0451  130 ARG A CG    
1012 C CD    . ARG A 130 ? 0.4783 0.5738 0.6445 -0.0742 -0.1213 0.0375  130 ARG A CD    
1013 N NE    . ARG A 130 ? 0.4694 0.5471 0.6013 -0.0710 -0.1074 0.0307  130 ARG A NE    
1014 C CZ    . ARG A 130 ? 0.6044 0.6600 0.7010 -0.0776 -0.1109 0.0220  130 ARG A CZ    
1015 N NH1   . ARG A 130 ? 0.5488 0.5944 0.6337 -0.0884 -0.1290 0.0185  130 ARG A NH1   
1016 N NH2   . ARG A 130 ? 0.5251 0.5677 0.5980 -0.0733 -0.0960 0.0164  130 ARG A NH2   
1017 N N     . ALA A 131 ? 0.4454 0.5758 0.6352 -0.0407 -0.1203 0.0595  131 ALA A N     
1018 C CA    . ALA A 131 ? 0.4295 0.5570 0.6060 -0.0310 -0.1018 0.0586  131 ALA A CA    
1019 C C     . ALA A 131 ? 0.4253 0.5705 0.6319 -0.0204 -0.0931 0.0651  131 ALA A C     
1020 O O     . ALA A 131 ? 0.4219 0.5674 0.6256 -0.0135 -0.0758 0.0641  131 ALA A O     
1021 C CB    . ALA A 131 ? 0.4390 0.5496 0.5774 -0.0300 -0.1051 0.0559  131 ALA A CB    
1022 N N     . TYR A 132 ? 0.3915 0.5502 0.6264 -0.0187 -0.1047 0.0715  132 TYR A N     
1023 C CA    . TYR A 132 ? 0.3994 0.5733 0.6630 -0.0078 -0.0942 0.0768  132 TYR A CA    
1024 C C     . TYR A 132 ? 0.4239 0.6076 0.7083 -0.0060 -0.0752 0.0766  132 TYR A C     
1025 O O     . TYR A 132 ? 0.4222 0.6060 0.7033 0.0024  -0.0580 0.0764  132 TYR A O     
1026 C CB    . TYR A 132 ? 0.4372 0.6257 0.7355 -0.0065 -0.1101 0.0839  132 TYR A CB    
1027 C CG    . TYR A 132 ? 0.4519 0.6296 0.7300 -0.0087 -0.1314 0.0860  132 TYR A CG    
1028 C CD1   . TYR A 132 ? 0.4319 0.6011 0.6913 -0.0008 -0.1298 0.0877  132 TYR A CD1   
1029 C CD2   . TYR A 132 ? 0.4703 0.6448 0.7468 -0.0193 -0.1537 0.0867  132 TYR A CD2   
1030 C CE1   . TYR A 132 ? 0.4688 0.6260 0.7076 -0.0032 -0.1490 0.0908  132 TYR A CE1   
1031 C CE2   . TYR A 132 ? 0.4566 0.6186 0.7102 -0.0219 -0.1739 0.0894  132 TYR A CE2   
1032 C CZ    . TYR A 132 ? 0.4833 0.6365 0.7178 -0.0137 -0.1711 0.0919  132 TYR A CZ    
1033 O OH    . TYR A 132 ? 0.5363 0.6749 0.7456 -0.0169 -0.1909 0.0956  132 TYR A OH    
1034 N N     . GLU A 133 ? 0.3923 0.5826 0.6967 -0.0144 -0.0782 0.0769  133 GLU A N     
1035 C CA    . GLU A 133 ? 0.3965 0.5943 0.7193 -0.0135 -0.0595 0.0778  133 GLU A CA    
1036 C C     . GLU A 133 ? 0.3967 0.5783 0.6857 -0.0140 -0.0468 0.0726  133 GLU A C     
1037 O O     . GLU A 133 ? 0.3959 0.5786 0.6864 -0.0088 -0.0287 0.0738  133 GLU A O     
1038 C CB    . GLU A 133 ? 0.3621 0.5722 0.7203 -0.0228 -0.0660 0.0803  133 GLU A CB    
1039 C CG    . GLU A 133 ? 0.5595 0.7898 0.9617 -0.0212 -0.0771 0.0866  133 GLU A CG    
1040 C CD    . GLU A 133 ? 0.5930 0.8351 1.0160 -0.0083 -0.0616 0.0908  133 GLU A CD    
1041 O OE1   . GLU A 133 ? 0.5661 0.8064 0.9835 -0.0030 -0.0389 0.0902  133 GLU A OE1   
1042 O OE2   . GLU A 133 ? 0.7377 0.9896 1.1822 -0.0035 -0.0728 0.0948  133 GLU A OE2   
1043 N N     . GLU A 134 ? 0.3567 0.5222 0.6148 -0.0200 -0.0557 0.0670  134 GLU A N     
1044 C CA    . GLU A 134 ? 0.3804 0.5312 0.6094 -0.0187 -0.0438 0.0623  134 GLU A CA    
1045 C C     . GLU A 134 ? 0.4237 0.5725 0.6393 -0.0078 -0.0323 0.0628  134 GLU A C     
1046 O O     . GLU A 134 ? 0.3955 0.5407 0.6045 -0.0039 -0.0182 0.0628  134 GLU A O     
1047 C CB    . GLU A 134 ? 0.3835 0.5173 0.5821 -0.0253 -0.0536 0.0555  134 GLU A CB    
1048 C CG    . GLU A 134 ? 0.4120 0.5423 0.6168 -0.0371 -0.0640 0.0529  134 GLU A CG    
1049 C CD    . GLU A 134 ? 0.4701 0.5808 0.6408 -0.0432 -0.0721 0.0451  134 GLU A CD    
1050 O OE1   . GLU A 134 ? 0.4171 0.5203 0.5640 -0.0395 -0.0738 0.0433  134 GLU A OE1   
1051 O OE2   . GLU A 134 ? 0.4424 0.5442 0.6098 -0.0521 -0.0755 0.0405  134 GLU A OE2   
1052 N N     . ILE A 135 ? 0.4291 0.5790 0.6399 -0.0032 -0.0391 0.0636  135 ILE A N     
1053 C CA    . ILE A 135 ? 0.4376 0.5839 0.6350 0.0063  -0.0299 0.0633  135 ILE A CA    
1054 C C     . ILE A 135 ? 0.3613 0.5186 0.5803 0.0134  -0.0163 0.0674  135 ILE A C     
1055 O O     . ILE A 135 ? 0.3951 0.5466 0.6006 0.0189  -0.0035 0.0662  135 ILE A O     
1056 C CB    . ILE A 135 ? 0.4082 0.5512 0.5957 0.0087  -0.0410 0.0637  135 ILE A CB    
1057 C CG1   . ILE A 135 ? 0.3791 0.5065 0.5356 0.0025  -0.0485 0.0586  135 ILE A CG1   
1058 C CG2   . ILE A 135 ? 0.3644 0.5064 0.5469 0.0189  -0.0317 0.0642  135 ILE A CG2   
1059 C CD1   . ILE A 135 ? 0.4265 0.5484 0.5715 0.0015  -0.0622 0.0600  135 ILE A CD1   
1060 N N     . ASN A 136 ? 0.3272 0.4997 0.5800 0.0131  -0.0187 0.0721  136 ASN A N     
1061 C CA    . ASN A 136 ? 0.3809 0.5634 0.6558 0.0193  -0.0026 0.0755  136 ASN A CA    
1062 C C     . ASN A 136 ? 0.4052 0.5821 0.6711 0.0171  0.0122  0.0751  136 ASN A C     
1063 O O     . ASN A 136 ? 0.3620 0.5350 0.6189 0.0234  0.0275  0.0753  136 ASN A O     
1064 C CB    . ASN A 136 ? 0.3912 0.5925 0.7098 0.0178  -0.0069 0.0807  136 ASN A CB    
1065 C CG    . ASN A 136 ? 0.4415 0.6493 0.7740 0.0232  -0.0187 0.0830  136 ASN A CG    
1066 O OD1   . ASN A 136 ? 0.3654 0.5652 0.6795 0.0306  -0.0167 0.0814  136 ASN A OD1   
1067 N ND2   . ASN A 136 ? 0.3965 0.6185 0.7635 0.0193  -0.0318 0.0872  136 ASN A ND2   
1068 N N     . ASN A 137 ? 0.3895 0.5639 0.6557 0.0080  0.0073  0.0745  137 ASN A N     
1069 C CA    . ASN A 137 ? 0.4287 0.5969 0.6886 0.0056  0.0204  0.0755  137 ASN A CA    
1070 C C     . ASN A 137 ? 0.3438 0.4953 0.5670 0.0098  0.0255  0.0720  137 ASN A C     
1071 O O     . ASN A 137 ? 0.4253 0.5712 0.6391 0.0131  0.0392  0.0740  137 ASN A O     
1072 C CB    . ASN A 137 ? 0.3589 0.5265 0.6283 -0.0054 0.0128  0.0752  137 ASN A CB    
1073 C CG    . ASN A 137 ? 0.3314 0.5163 0.6413 -0.0108 0.0071  0.0790  137 ASN A CG    
1074 O OD1   . ASN A 137 ? 0.3792 0.5782 0.7152 -0.0060 0.0140  0.0831  137 ASN A OD1   
1075 N ND2   . ASN A 137 ? 0.3628 0.5465 0.6793 -0.0210 -0.0054 0.0773  137 ASN A ND2   
1076 N N     . PHE A 138 ? 0.3856 0.5286 0.5879 0.0095  0.0145  0.0672  138 PHE A N     
1077 C CA    . PHE A 138 ? 0.4178 0.5470 0.5904 0.0137  0.0179  0.0638  138 PHE A CA    
1078 C C     . PHE A 138 ? 0.4500 0.5788 0.6154 0.0228  0.0272  0.0647  138 PHE A C     
1079 O O     . PHE A 138 ? 0.3774 0.4976 0.5274 0.0260  0.0366  0.0653  138 PHE A O     
1080 C CB    . PHE A 138 ? 0.3970 0.5195 0.5540 0.0115  0.0057  0.0585  138 PHE A CB    
1081 C CG    . PHE A 138 ? 0.3821 0.4943 0.5153 0.0167  0.0076  0.0550  138 PHE A CG    
1082 C CD1   . PHE A 138 ? 0.3966 0.5000 0.5169 0.0185  0.0143  0.0545  138 PHE A CD1   
1083 C CD2   . PHE A 138 ? 0.3963 0.5071 0.5208 0.0191  0.0015  0.0526  138 PHE A CD2   
1084 C CE1   . PHE A 138 ? 0.3835 0.4787 0.4859 0.0228  0.0142  0.0514  138 PHE A CE1   
1085 C CE2   . PHE A 138 ? 0.3880 0.4900 0.4938 0.0229  0.0031  0.0493  138 PHE A CE2   
1086 C CZ    . PHE A 138 ? 0.4727 0.5677 0.5689 0.0247  0.0091  0.0484  138 PHE A CZ    
1087 N N     . GLU A 139 ? 0.3488 0.4852 0.5246 0.0269  0.0243  0.0650  139 GLU A N     
1088 C CA    . GLU A 139 ? 0.4213 0.5556 0.5904 0.0354  0.0331  0.0647  139 GLU A CA    
1089 C C     . GLU A 139 ? 0.4161 0.5525 0.5927 0.0379  0.0494  0.0681  139 GLU A C     
1090 O O     . GLU A 139 ? 0.4275 0.5543 0.5848 0.0430  0.0589  0.0669  139 GLU A O     
1091 C CB    . GLU A 139 ? 0.3516 0.4935 0.5347 0.0393  0.0267  0.0649  139 GLU A CB    
1092 C CG    . GLU A 139 ? 0.3885 0.5235 0.5553 0.0377  0.0131  0.0617  139 GLU A CG    
1093 C CD    . GLU A 139 ? 0.3971 0.5373 0.5760 0.0411  0.0052  0.0633  139 GLU A CD    
1094 O OE1   . GLU A 139 ? 0.4140 0.5641 0.6167 0.0458  0.0101  0.0665  139 GLU A OE1   
1095 O OE2   . GLU A 139 ? 0.4311 0.5646 0.5959 0.0392  -0.0053 0.0617  139 GLU A OE2   
1096 N N     . LYS A 140 ? 0.3538 0.5013 0.5569 0.0335  0.0530  0.0723  140 LYS A N     
1097 C CA    . LYS A 140 ? 0.4020 0.5513 0.6136 0.0349  0.0710  0.0761  140 LYS A CA    
1098 C C     . LYS A 140 ? 0.4152 0.5495 0.6001 0.0326  0.0780  0.0771  140 LYS A C     
1099 O O     . LYS A 140 ? 0.4450 0.5713 0.6161 0.0362  0.0928  0.0787  140 LYS A O     
1100 C CB    . LYS A 140 ? 0.3593 0.5255 0.6105 0.0297  0.0724  0.0806  140 LYS A CB    
1101 C CG    . LYS A 140 ? 0.5057 0.6758 0.7716 0.0307  0.0936  0.0850  140 LYS A CG    
1102 C CD    . LYS A 140 ? 0.5809 0.7590 0.8635 0.0393  0.1041  0.0846  140 LYS A CD    
1103 C CE    . LYS A 140 ? 0.6075 0.7910 0.9097 0.0396  0.1275  0.0888  140 LYS A CE    
1104 N NZ    . LYS A 140 ? 0.7176 0.9080 1.0375 0.0489  0.1395  0.0874  140 LYS A NZ    
1105 N N     . ILE A 141 ? 0.3936 0.5223 0.5700 0.0267  0.0675  0.0763  141 ILE A N     
1106 C CA    . ILE A 141 ? 0.4270 0.5399 0.5775 0.0257  0.0711  0.0774  141 ILE A CA    
1107 C C     . ILE A 141 ? 0.4218 0.5225 0.5427 0.0329  0.0736  0.0748  141 ILE A C     
1108 O O     . ILE A 141 ? 0.4490 0.5381 0.5506 0.0349  0.0837  0.0775  141 ILE A O     
1109 C CB    . ILE A 141 ? 0.3945 0.5025 0.5408 0.0200  0.0583  0.0752  141 ILE A CB    
1110 C CG1   . ILE A 141 ? 0.4087 0.5238 0.5794 0.0116  0.0574  0.0781  141 ILE A CG1   
1111 C CG2   . ILE A 141 ? 0.3761 0.4671 0.4953 0.0214  0.0591  0.0757  141 ILE A CG2   
1112 C CD1   . ILE A 141 ? 0.4146 0.5237 0.5816 0.0058  0.0454  0.0744  141 ILE A CD1   
1113 N N     . LEU A 142 ? 0.4250 0.5268 0.5408 0.0364  0.0641  0.0696  142 LEU A N     
1114 C CA    . LEU A 142 ? 0.4052 0.4948 0.4940 0.0423  0.0644  0.0664  142 LEU A CA    
1115 C C     . LEU A 142 ? 0.5301 0.6179 0.6146 0.0481  0.0779  0.0666  142 LEU A C     
1116 O O     . LEU A 142 ? 0.4292 0.5026 0.4871 0.0511  0.0838  0.0663  142 LEU A O     
1117 C CB    . LEU A 142 ? 0.3342 0.4248 0.4204 0.0436  0.0517  0.0610  142 LEU A CB    
1118 C CG    . LEU A 142 ? 0.4027 0.4919 0.4882 0.0384  0.0405  0.0592  142 LEU A CG    
1119 C CD1   . LEU A 142 ? 0.3361 0.4251 0.4174 0.0396  0.0310  0.0541  142 LEU A CD1   
1120 C CD2   . LEU A 142 ? 0.3339 0.4106 0.4020 0.0378  0.0406  0.0604  142 LEU A CD2   
1121 N N     . THR A 143 ? 0.4216 0.5225 0.5314 0.0500  0.0827  0.0669  143 THR A N     
1122 C CA    . THR A 143 ? 0.4426 0.5410 0.5496 0.0567  0.0962  0.0656  143 THR A CA    
1123 C C     . THR A 143 ? 0.4739 0.5678 0.5772 0.0561  0.1148  0.0698  143 THR A C     
1124 O O     . THR A 143 ? 0.4851 0.5688 0.5713 0.0611  0.1279  0.0679  143 THR A O     
1125 C CB    . THR A 143 ? 0.4478 0.5616 0.5864 0.0600  0.0956  0.0650  143 THR A CB    
1126 O OG1   . THR A 143 ? 0.4472 0.5773 0.6200 0.0553  0.0965  0.0698  143 THR A OG1   
1127 C CG2   . THR A 143 ? 0.4052 0.5199 0.5423 0.0609  0.0785  0.0613  143 THR A CG2   
1128 N N     . ALA A 144 ? 0.4273 0.5271 0.5452 0.0496  0.1172  0.0753  144 ALA A N     
1129 C CA    . ALA A 144 ? 0.4684 0.5606 0.5780 0.0480  0.1357  0.0803  144 ALA A CA    
1130 C C     . ALA A 144 ? 0.4680 0.5370 0.5331 0.0482  0.1358  0.0808  144 ALA A C     
1131 O O     . ALA A 144 ? 0.5105 0.5673 0.5569 0.0483  0.1518  0.0842  144 ALA A O     
1132 C CB    . ALA A 144 ? 0.4448 0.5481 0.5824 0.0402  0.1378  0.0865  144 ALA A CB    
1133 N N     . GLY A 145 ? 0.5303 0.5926 0.5785 0.0481  0.1182  0.0779  145 GLY A N     
1134 C CA    . GLY A 145 ? 0.4713 0.5126 0.4803 0.0490  0.1145  0.0781  145 GLY A CA    
1135 C C     . GLY A 145 ? 0.6074 0.6392 0.5937 0.0552  0.1122  0.0714  145 GLY A C     
1136 O O     . GLY A 145 ? 0.4929 0.5251 0.4804 0.0593  0.1249  0.0687  145 GLY A O     
1137 N N     . ASP A 146 ? 0.5041 0.5276 0.4728 0.0558  0.0962  0.0682  146 ASP A N     
1138 C CA    . ASP A 146 ? 0.5648 0.5758 0.5083 0.0605  0.0931  0.0620  146 ASP A CA    
1139 C C     . ASP A 146 ? 0.5152 0.5359 0.4737 0.0623  0.0804  0.0558  146 ASP A C     
1140 O O     . ASP A 146 ? 0.5123 0.5243 0.4547 0.0632  0.0685  0.0519  146 ASP A O     
1141 C CB    . ASP A 146 ? 0.5289 0.5194 0.4366 0.0596  0.0848  0.0637  146 ASP A CB    
1142 C CG    . ASP A 146 ? 0.6120 0.5867 0.4941 0.0584  0.0988  0.0697  146 ASP A CG    
1143 O OD1   . ASP A 146 ? 0.6436 0.6188 0.5271 0.0599  0.1175  0.0695  146 ASP A OD1   
1144 O OD2   . ASP A 146 ? 0.6688 0.6300 0.5301 0.0560  0.0915  0.0749  146 ASP A OD2   
1145 N N     . TYR A 147 ? 0.4711 0.5091 0.4608 0.0626  0.0827  0.0553  147 TYR A N     
1146 C CA    . TYR A 147 ? 0.4875 0.5339 0.4912 0.0639  0.0720  0.0507  147 TYR A CA    
1147 C C     . TYR A 147 ? 0.5355 0.5907 0.5584 0.0681  0.0808  0.0491  147 TYR A C     
1148 O O     . TYR A 147 ? 0.4607 0.5254 0.5030 0.0680  0.0917  0.0529  147 TYR A O     
1149 C CB    . TYR A 147 ? 0.4110 0.4694 0.4349 0.0589  0.0608  0.0525  147 TYR A CB    
1150 C CG    . TYR A 147 ? 0.4005 0.4513 0.4111 0.0558  0.0505  0.0527  147 TYR A CG    
1151 C CD1   . TYR A 147 ? 0.4593 0.5052 0.4612 0.0565  0.0396  0.0480  147 TYR A CD1   
1152 C CD2   . TYR A 147 ? 0.4548 0.5035 0.4647 0.0521  0.0518  0.0577  147 TYR A CD2   
1153 C CE1   . TYR A 147 ? 0.4116 0.4523 0.4071 0.0542  0.0304  0.0482  147 TYR A CE1   
1154 C CE2   . TYR A 147 ? 0.4435 0.4852 0.4448 0.0502  0.0421  0.0581  147 TYR A CE2   
1155 C CZ    . TYR A 147 ? 0.4447 0.4833 0.4403 0.0515  0.0315  0.0532  147 TYR A CZ    
1156 O OH    . TYR A 147 ? 0.4492 0.4825 0.4416 0.0502  0.0223  0.0535  147 TYR A OH    
1157 N N     . ILE A 148 ? 0.4824 0.5344 0.5022 0.0719  0.0758  0.0439  148 ILE A N     
1158 C CA    . ILE A 148 ? 0.4638 0.5241 0.5051 0.0764  0.0800  0.0425  148 ILE A CA    
1159 C C     . ILE A 148 ? 0.4424 0.5130 0.5012 0.0740  0.0653  0.0430  148 ILE A C     
1160 O O     . ILE A 148 ? 0.4464 0.5113 0.4924 0.0714  0.0541  0.0407  148 ILE A O     
1161 C CB    . ILE A 148 ? 0.4472 0.4927 0.4696 0.0824  0.0856  0.0362  148 ILE A CB    
1162 C CG1   . ILE A 148 ? 0.4916 0.5256 0.4953 0.0847  0.1030  0.0356  148 ILE A CG1   
1163 C CG2   . ILE A 148 ? 0.4007 0.4532 0.4464 0.0874  0.0853  0.0346  148 ILE A CG2   
1164 C CD1   . ILE A 148 ? 0.5432 0.5559 0.5154 0.0888  0.1070  0.0282  148 ILE A CD1   
1165 N N     . ILE A 149 ? 0.4223 0.5074 0.5105 0.0745  0.0651  0.0464  149 ILE A N     
1166 C CA    . ILE A 149 ? 0.4552 0.5479 0.5565 0.0717  0.0510  0.0476  149 ILE A CA    
1167 C C     . ILE A 149 ? 0.4902 0.5869 0.6095 0.0775  0.0511  0.0478  149 ILE A C     
1168 O O     . ILE A 149 ? 0.4339 0.5383 0.5740 0.0817  0.0608  0.0498  149 ILE A O     
1169 C CB    . ILE A 149 ? 0.4243 0.5294 0.5428 0.0652  0.0455  0.0522  149 ILE A CB    
1170 C CG1   . ILE A 149 ? 0.4130 0.5121 0.5138 0.0597  0.0437  0.0517  149 ILE A CG1   
1171 C CG2   . ILE A 149 ? 0.3999 0.5108 0.5295 0.0624  0.0315  0.0535  149 ILE A CG2   
1172 C CD1   . ILE A 149 ? 0.3449 0.4534 0.4608 0.0529  0.0395  0.0554  149 ILE A CD1   
1173 N N     . ILE A 150 ? 0.4348 0.5259 0.5480 0.0779  0.0409  0.0461  150 ILE A N     
1174 C CA    . ILE A 150 ? 0.4313 0.5257 0.5630 0.0827  0.0374  0.0479  150 ILE A CA    
1175 C C     . ILE A 150 ? 0.3954 0.4911 0.5272 0.0775  0.0216  0.0507  150 ILE A C     
1176 O O     . ILE A 150 ? 0.4022 0.4899 0.5134 0.0728  0.0162  0.0482  150 ILE A O     
1177 C CB    . ILE A 150 ? 0.4504 0.5313 0.5713 0.0896  0.0433  0.0429  150 ILE A CB    
1178 C CG1   . ILE A 150 ? 0.5086 0.5807 0.6132 0.0926  0.0581  0.0381  150 ILE A CG1   
1179 C CG2   . ILE A 150 ? 0.4906 0.5760 0.6375 0.0966  0.0435  0.0457  150 ILE A CG2   
1180 C CD1   . ILE A 150 ? 0.5915 0.6460 0.6770 0.0974  0.0618  0.0314  150 ILE A CD1   
1181 N N     . LYS A 151 ? 0.3704 0.4754 0.5253 0.0784  0.0143  0.0560  151 LYS A N     
1182 C CA    . LYS A 151 ? 0.3988 0.5025 0.5503 0.0733  -0.0010 0.0594  151 LYS A CA    
1183 C C     . LYS A 151 ? 0.4246 0.5238 0.5851 0.0791  -0.0064 0.0623  151 LYS A C     
1184 O O     . LYS A 151 ? 0.4254 0.5316 0.6110 0.0860  -0.0028 0.0648  151 LYS A O     
1185 C CB    . LYS A 151 ? 0.4001 0.5165 0.5673 0.0674  -0.0091 0.0640  151 LYS A CB    
1186 C CG    . LYS A 151 ? 0.4199 0.5385 0.5776 0.0610  -0.0045 0.0614  151 LYS A CG    
1187 C CD    . LYS A 151 ? 0.4095 0.5415 0.5913 0.0618  0.0034  0.0636  151 LYS A CD    
1188 C CE    . LYS A 151 ? 0.3665 0.5118 0.5777 0.0601  -0.0070 0.0694  151 LYS A CE    
1189 N NZ    . LYS A 151 ? 0.3548 0.5134 0.5890 0.0572  -0.0009 0.0715  151 LYS A NZ    
1190 N N     . PHE A 152 ? 0.4298 0.5166 0.5713 0.0764  -0.0139 0.0621  152 PHE A N     
1191 C CA    . PHE A 152 ? 0.4655 0.5441 0.6110 0.0810  -0.0198 0.0654  152 PHE A CA    
1192 C C     . PHE A 152 ? 0.4301 0.5067 0.5711 0.0750  -0.0357 0.0721  152 PHE A C     
1193 O O     . PHE A 152 ? 0.4422 0.5135 0.5614 0.0667  -0.0394 0.0708  152 PHE A O     
1194 C CB    . PHE A 152 ? 0.4545 0.5168 0.5788 0.0822  -0.0148 0.0601  152 PHE A CB    
1195 C CG    . PHE A 152 ? 0.4542 0.5136 0.5778 0.0882  -0.0009 0.0533  152 PHE A CG    
1196 C CD1   . PHE A 152 ? 0.4458 0.5034 0.5858 0.0976  0.0054  0.0530  152 PHE A CD1   
1197 C CD2   . PHE A 152 ? 0.4876 0.5444 0.5930 0.0847  0.0055  0.0472  152 PHE A CD2   
1198 C CE1   . PHE A 152 ? 0.5190 0.5707 0.6533 0.1027  0.0192  0.0458  152 PHE A CE1   
1199 C CE2   . PHE A 152 ? 0.4892 0.5405 0.5887 0.0896  0.0171  0.0411  152 PHE A CE2   
1200 C CZ    . PHE A 152 ? 0.4251 0.4730 0.5370 0.0983  0.0245  0.0400  152 PHE A CZ    
1201 N N     . TRP A 153 ? 0.4357 0.5151 0.5965 0.0793  -0.0450 0.0792  153 TRP A N     
1202 C CA    . TRP A 153 ? 0.4652 0.5377 0.6171 0.0743  -0.0617 0.0865  153 TRP A CA    
1203 C C     . TRP A 153 ? 0.5152 0.5730 0.6636 0.0797  -0.0644 0.0898  153 TRP A C     
1204 O O     . TRP A 153 ? 0.4680 0.5290 0.6419 0.0890  -0.0640 0.0927  153 TRP A O     
1205 C CB    . TRP A 153 ? 0.4305 0.5165 0.6078 0.0742  -0.0749 0.0937  153 TRP A CB    
1206 C CG    . TRP A 153 ? 0.5014 0.5770 0.6668 0.0697  -0.0942 0.1022  153 TRP A CG    
1207 C CD1   . TRP A 153 ? 0.5191 0.5883 0.6957 0.0756  -0.1049 0.1103  153 TRP A CD1   
1208 C CD2   . TRP A 153 ? 0.4879 0.5557 0.6249 0.0584  -0.1048 0.1034  153 TRP A CD2   
1209 N NE1   . TRP A 153 ? 0.5055 0.5631 0.6606 0.0682  -0.1226 0.1174  153 TRP A NE1   
1210 C CE2   . TRP A 153 ? 0.5255 0.5814 0.6547 0.0574  -0.1222 0.1128  153 TRP A CE2   
1211 C CE3   . TRP A 153 ? 0.4796 0.5476 0.5964 0.0491  -0.1011 0.0975  153 TRP A CE3   
1212 C CZ2   . TRP A 153 ? 0.4594 0.5027 0.5574 0.0468  -0.1352 0.1160  153 TRP A CZ2   
1213 C CZ3   . TRP A 153 ? 0.5560 0.6123 0.6446 0.0390  -0.1130 0.0998  153 TRP A CZ3   
1214 C CH2   . TRP A 153 ? 0.4984 0.5419 0.5760 0.0377  -0.1296 0.1089  153 TRP A CH2   
1215 N N     . LEU A 154 ? 0.4536 0.4950 0.5726 0.0738  -0.0664 0.0896  154 LEU A N     
1216 C CA    . LEU A 154 ? 0.5009 0.5257 0.6143 0.0774  -0.0693 0.0935  154 LEU A CA    
1217 C C     . LEU A 154 ? 0.5502 0.5690 0.6621 0.0752  -0.0876 0.1048  154 LEU A C     
1218 O O     . LEU A 154 ? 0.5179 0.5294 0.6046 0.0655  -0.0952 0.1075  154 LEU A O     
1219 C CB    . LEU A 154 ? 0.5467 0.5564 0.6316 0.0716  -0.0617 0.0882  154 LEU A CB    
1220 C CG    . LEU A 154 ? 0.6649 0.6741 0.7541 0.0768  -0.0472 0.0789  154 LEU A CG    
1221 C CD1   . LEU A 154 ? 0.5125 0.5367 0.6060 0.0761  -0.0387 0.0719  154 LEU A CD1   
1222 C CD2   . LEU A 154 ? 0.5670 0.5599 0.6346 0.0720  -0.0427 0.0753  154 LEU A CD2   
1223 N N     . HIS A 155 ? 0.5025 0.5231 0.6407 0.0843  -0.0947 0.1115  155 HIS A N     
1224 C CA    . HIS A 155 ? 0.5528 0.5666 0.6919 0.0835  -0.1147 0.1237  155 HIS A CA    
1225 C C     . HIS A 155 ? 0.5924 0.5818 0.7099 0.0830  -0.1177 0.1289  155 HIS A C     
1226 O O     . HIS A 155 ? 0.6104 0.5919 0.7328 0.0892  -0.1068 0.1251  155 HIS A O     
1227 C CB    . HIS A 155 ? 0.4997 0.5277 0.6827 0.0941  -0.1223 0.1296  155 HIS A CB    
1228 C CG    . HIS A 155 ? 0.5505 0.5690 0.7376 0.0955  -0.1442 0.1431  155 HIS A CG    
1229 N ND1   . HIS A 155 ? 0.6407 0.6601 0.8179 0.0875  -0.1641 0.1507  155 HIS A ND1   
1230 C CD2   . HIS A 155 ? 0.6070 0.6128 0.8051 0.1037  -0.1504 0.1508  155 HIS A CD2   
1231 C CE1   . HIS A 155 ? 0.6287 0.6367 0.8100 0.0907  -0.1827 0.1630  155 HIS A CE1   
1232 N NE2   . HIS A 155 ? 0.7077 0.7076 0.9030 0.1008  -0.1745 0.1637  155 HIS A NE2   
1233 N N     . VAL A 156 ? 0.6087 0.5843 0.7010 0.0753  -0.1327 0.1378  156 VAL A N     
1234 C CA    . VAL A 156 ? 0.6103 0.5607 0.6808 0.0740  -0.1370 0.1452  156 VAL A CA    
1235 C C     . VAL A 156 ? 0.6817 0.6227 0.7443 0.0714  -0.1606 0.1593  156 VAL A C     
1236 O O     . VAL A 156 ? 0.7272 0.6749 0.7811 0.0646  -0.1717 0.1611  156 VAL A O     
1237 C CB    . VAL A 156 ? 0.7078 0.6439 0.7402 0.0634  -0.1245 0.1391  156 VAL A CB    
1238 C CG1   . VAL A 156 ? 0.6931 0.6266 0.6946 0.0510  -0.1303 0.1400  156 VAL A CG1   
1239 C CG2   . VAL A 156 ? 0.6866 0.5981 0.7033 0.0632  -0.1237 0.1450  156 VAL A CG2   
1240 N N     . SER A 157 ? 0.6868 0.6111 0.7523 0.0769  -0.1695 0.1695  157 SER A N     
1241 C CA    . SER A 157 ? 0.6841 0.5956 0.7387 0.0746  -0.1939 0.1846  157 SER A CA    
1242 C C     . SER A 157 ? 0.7521 0.6403 0.7516 0.0601  -0.1965 0.1880  157 SER A C     
1243 O O     . SER A 157 ? 0.7500 0.6280 0.7246 0.0539  -0.1787 0.1809  157 SER A O     
1244 C CB    . SER A 157 ? 0.7667 0.6651 0.8410 0.0853  -0.2024 0.1953  157 SER A CB    
1245 O OG    . SER A 157 ? 0.7315 0.6066 0.7815 0.0831  -0.1903 0.1947  157 SER A OG    
1246 N N     . ASP A 158 ? 0.7590 0.6381 0.7398 0.0544  -0.2190 0.1989  158 ASP A N     
1247 C CA    . ASP A 158 ? 0.7958 0.6487 0.7200 0.0405  -0.2220 0.2033  158 ASP A CA    
1248 C C     . ASP A 158 ? 0.7513 0.5768 0.6523 0.0394  -0.2137 0.2090  158 ASP A C     
1249 O O     . ASP A 158 ? 0.7888 0.5990 0.6520 0.0290  -0.1991 0.2049  158 ASP A O     
1250 C CB    . ASP A 158 ? 0.8535 0.6970 0.7606 0.0356  -0.2509 0.2158  158 ASP A CB    
1251 C CG    . ASP A 158 ? 0.9927 0.8601 0.9161 0.0332  -0.2591 0.2096  158 ASP A CG    
1252 O OD1   . ASP A 158 ? 1.0216 0.9019 0.9415 0.0285  -0.2409 0.1957  158 ASP A OD1   
1253 O OD2   . ASP A 158 ? 1.0332 0.9066 0.9753 0.0361  -0.2843 0.2188  158 ASP A OD2   
1254 N N     . GLU A 159 ? 0.7887 0.6074 0.7137 0.0500  -0.2221 0.2186  159 GLU A N     
1255 C CA    . GLU A 159 ? 0.7657 0.5563 0.6695 0.0487  -0.2152 0.2250  159 GLU A CA    
1256 C C     . GLU A 159 ? 0.7918 0.5872 0.7022 0.0487  -0.1872 0.2109  159 GLU A C     
1257 O O     . GLU A 159 ? 0.7811 0.5559 0.6599 0.0400  -0.1750 0.2109  159 GLU A O     
1258 C CB    . GLU A 159 ? 0.7773 0.5584 0.7075 0.0607  -0.2319 0.2388  159 GLU A CB    
1259 C CG    . GLU A 159 ? 1.0543 0.8238 0.9709 0.0591  -0.2630 0.2558  159 GLU A CG    
1260 C CD    . GLU A 159 ? 1.1331 0.8830 1.0633 0.0685  -0.2803 0.2728  159 GLU A CD    
1261 O OE1   . GLU A 159 ? 1.0458 0.7960 1.0074 0.0793  -0.2692 0.2705  159 GLU A OE1   
1262 O OE2   . GLU A 159 ? 0.9600 0.6986 0.8698 0.0643  -0.2988 0.2823  159 GLU A OE2   
1263 N N     . GLU A 160 ? 0.7516 0.5735 0.7015 0.0575  -0.1767 0.1987  160 GLU A N     
1264 C CA    . GLU A 160 ? 0.7110 0.5371 0.6654 0.0570  -0.1527 0.1850  160 GLU A CA    
1265 C C     . GLU A 160 ? 0.7061 0.5344 0.6299 0.0439  -0.1397 0.1760  160 GLU A C     
1266 O O     . GLU A 160 ? 0.7046 0.5223 0.6127 0.0377  -0.1239 0.1709  160 GLU A O     
1267 C CB    . GLU A 160 ? 0.7457 0.5971 0.7450 0.0691  -0.1452 0.1745  160 GLU A CB    
1268 C CG    . GLU A 160 ? 0.6700 0.5266 0.6728 0.0684  -0.1226 0.1595  160 GLU A CG    
1269 C CD    . GLU A 160 ? 0.8117 0.6462 0.8109 0.0697  -0.1151 0.1606  160 GLU A CD    
1270 O OE1   . GLU A 160 ? 0.7588 0.5770 0.7638 0.0754  -0.1259 0.1720  160 GLU A OE1   
1271 O OE2   . GLU A 160 ? 0.7491 0.5820 0.7410 0.0648  -0.0993 0.1503  160 GLU A OE2   
1272 N N     . GLN A 161 ? 0.6787 0.5204 0.5959 0.0395  -0.1464 0.1740  161 GLN A N     
1273 C CA    . GLN A 161 ? 0.7172 0.5584 0.6042 0.0273  -0.1349 0.1662  161 GLN A CA    
1274 C C     . GLN A 161 ? 0.7918 0.6030 0.6341 0.0160  -0.1330 0.1738  161 GLN A C     
1275 O O     . GLN A 161 ? 0.7108 0.5167 0.5355 0.0078  -0.1149 0.1666  161 GLN A O     
1276 C CB    . GLN A 161 ? 0.7107 0.5670 0.5960 0.0242  -0.1452 0.1641  161 GLN A CB    
1277 C CG    . GLN A 161 ? 0.6870 0.5449 0.5463 0.0131  -0.1319 0.1541  161 GLN A CG    
1278 C CD    . GLN A 161 ? 0.7884 0.6528 0.6364 0.0078  -0.1447 0.1541  161 GLN A CD    
1279 O OE1   . GLN A 161 ? 0.7591 0.6101 0.5885 0.0047  -0.1640 0.1648  161 GLN A OE1   
1280 N NE2   . GLN A 161 ? 0.6993 0.5827 0.5579 0.0063  -0.1352 0.1423  161 GLN A NE2   
1281 N N     . LEU A 162 ? 0.7395 0.5305 0.5635 0.0152  -0.1513 0.1889  162 LEU A N     
1282 C CA    . LEU A 162 ? 0.8064 0.5653 0.5837 0.0041  -0.1493 0.1978  162 LEU A CA    
1283 C C     . LEU A 162 ? 0.8025 0.5487 0.5825 0.0038  -0.1320 0.1968  162 LEU A C     
1284 O O     . LEU A 162 ? 0.8120 0.5432 0.5630 -0.0072 -0.1161 0.1947  162 LEU A O     
1285 C CB    . LEU A 162 ? 0.8254 0.5642 0.5850 0.0048  -0.1750 0.2155  162 LEU A CB    
1286 C CG    . LEU A 162 ? 0.9495 0.6505 0.6578 -0.0061 -0.1748 0.2276  162 LEU A CG    
1287 C CD1   . LEU A 162 ? 0.9906 0.6826 0.6540 -0.0209 -0.1621 0.2212  162 LEU A CD1   
1288 C CD2   . LEU A 162 ? 1.0083 0.6900 0.7025 -0.0037 -0.2038 0.2462  162 LEU A CD2   
1289 N N     . LYS A 163 ? 0.7550 0.5060 0.5706 0.0155  -0.1346 0.1981  163 LYS A N     
1290 C CA    . LYS A 163 ? 0.8459 0.5862 0.6688 0.0157  -0.1190 0.1954  163 LYS A CA    
1291 C C     . LYS A 163 ? 0.7284 0.4825 0.5545 0.0096  -0.0965 0.1794  163 LYS A C     
1292 O O     . LYS A 163 ? 0.7364 0.4757 0.5459 0.0007  -0.0818 0.1783  163 LYS A O     
1293 C CB    . LYS A 163 ? 0.8477 0.5950 0.7122 0.0305  -0.1247 0.1957  163 LYS A CB    
1294 C CG    . LYS A 163 ? 0.9425 0.6775 0.8172 0.0316  -0.1111 0.1924  163 LYS A CG    
1295 C CD    . LYS A 163 ? 0.8338 0.5760 0.7491 0.0469  -0.1159 0.1907  163 LYS A CD    
1296 C CE    . LYS A 163 ? 1.0079 0.7376 0.9328 0.0474  -0.1022 0.1849  163 LYS A CE    
1297 N NZ    . LYS A 163 ? 1.1567 0.9040 1.1192 0.0594  -0.0968 0.1724  163 LYS A NZ    
1298 N N     . ARG A 164 ? 0.6873 0.4697 0.5355 0.0140  -0.0940 0.1675  164 ARG A N     
1299 C CA    . ARG A 164 ? 0.6865 0.4828 0.5404 0.0093  -0.0750 0.1529  164 ARG A CA    
1300 C C     . ARG A 164 ? 0.7319 0.5202 0.5514 -0.0043 -0.0655 0.1516  164 ARG A C     
1301 O O     . ARG A 164 ? 0.7520 0.5399 0.5699 -0.0109 -0.0481 0.1441  164 ARG A O     
1302 C CB    . ARG A 164 ? 0.6734 0.4995 0.5575 0.0175  -0.0755 0.1419  164 ARG A CB    
1303 C CG    . ARG A 164 ? 0.7036 0.5375 0.6222 0.0309  -0.0801 0.1409  164 ARG A CG    
1304 C CD    . ARG A 164 ? 0.6211 0.4829 0.5672 0.0386  -0.0787 0.1306  164 ARG A CD    
1305 N NE    . ARG A 164 ? 0.6742 0.5401 0.6502 0.0514  -0.0823 0.1307  164 ARG A NE    
1306 C CZ    . ARG A 164 ? 0.6489 0.5348 0.6511 0.0598  -0.0789 0.1224  164 ARG A CZ    
1307 N NH1   . ARG A 164 ? 0.6026 0.5071 0.6060 0.0570  -0.0731 0.1138  164 ARG A NH1   
1308 N NH2   . ARG A 164 ? 0.6494 0.5352 0.6767 0.0713  -0.0804 0.1228  164 ARG A NH2   
1309 N N     . PHE A 165 ? 0.7360 0.5170 0.5282 -0.0089 -0.0765 0.1585  165 PHE A N     
1310 C CA    . PHE A 165 ? 0.7515 0.5197 0.5056 -0.0221 -0.0664 0.1576  165 PHE A CA    
1311 C C     . PHE A 165 ? 0.8045 0.5449 0.5341 -0.0307 -0.0553 0.1647  165 PHE A C     
1312 O O     . PHE A 165 ? 0.7882 0.5241 0.5045 -0.0402 -0.0360 0.1587  165 PHE A O     
1313 C CB    . PHE A 165 ? 0.7725 0.5329 0.4972 -0.0257 -0.0829 0.1645  165 PHE A CB    
1314 C CG    . PHE A 165 ? 0.7758 0.5600 0.5115 -0.0244 -0.0856 0.1544  165 PHE A CG    
1315 C CD1   . PHE A 165 ? 0.7206 0.5337 0.4986 -0.0152 -0.0824 0.1442  165 PHE A CD1   
1316 C CD2   . PHE A 165 ? 0.7934 0.5686 0.4946 -0.0328 -0.0916 0.1552  165 PHE A CD2   
1317 C CE1   . PHE A 165 ? 0.7122 0.5452 0.4996 -0.0145 -0.0848 0.1360  165 PHE A CE1   
1318 C CE2   . PHE A 165 ? 0.8177 0.6127 0.5289 -0.0322 -0.0945 0.1461  165 PHE A CE2   
1319 C CZ    . PHE A 165 ? 0.7306 0.5549 0.4860 -0.0230 -0.0909 0.1369  165 PHE A CZ    
1320 N N     . LYS A 166 ? 0.8193 0.5405 0.5445 -0.0274 -0.0667 0.1779  166 LYS A N     
1321 C CA    . LYS A 166 ? 0.8154 0.5078 0.5165 -0.0360 -0.0563 0.1861  166 LYS A CA    
1322 C C     . LYS A 166 ? 0.8564 0.5562 0.5858 -0.0363 -0.0375 0.1768  166 LYS A C     
1323 O O     . LYS A 166 ? 0.8682 0.5551 0.5823 -0.0471 -0.0193 0.1760  166 LYS A O     
1324 C CB    . LYS A 166 ? 0.8929 0.5617 0.5829 -0.0319 -0.0750 0.2035  166 LYS A CB    
1325 C CG    . LYS A 166 ? 0.9339 0.5870 0.5843 -0.0359 -0.0932 0.2150  166 LYS A CG    
1326 C CD    . LYS A 166 ? 1.1540 0.7739 0.7794 -0.0366 -0.1079 0.2345  166 LYS A CD    
1327 C CE    . LYS A 166 ? 1.1732 0.7747 0.7525 -0.0427 -0.1263 0.2456  166 LYS A CE    
1328 N NZ    . LYS A 166 ? 1.4838 1.0484 1.0311 -0.0451 -0.1405 0.2661  166 LYS A NZ    
1329 N N     . GLU A 167 ? 0.7613 0.4821 0.5322 -0.0250 -0.0412 0.1692  167 GLU A N     
1330 C CA    . GLU A 167 ? 0.8133 0.5434 0.6113 -0.0255 -0.0255 0.1582  167 GLU A CA    
1331 C C     . GLU A 167 ? 0.7786 0.5229 0.5754 -0.0337 -0.0084 0.1463  167 GLU A C     
1332 O O     . GLU A 167 ? 0.8408 0.5790 0.6390 -0.0421 0.0080  0.1430  167 GLU A O     
1333 C CB    . GLU A 167 ? 0.7929 0.5426 0.6300 -0.0120 -0.0329 0.1507  167 GLU A CB    
1334 C CG    . GLU A 167 ? 0.9057 0.6392 0.7513 -0.0040 -0.0444 0.1605  167 GLU A CG    
1335 C CD    . GLU A 167 ? 1.0838 0.8356 0.9637 0.0105  -0.0528 0.1542  167 GLU A CD    
1336 O OE1   . GLU A 167 ? 0.9745 0.7514 0.8698 0.0138  -0.0500 0.1427  167 GLU A OE1   
1337 O OE2   . GLU A 167 ? 1.1365 0.8762 1.0277 0.0185  -0.0614 0.1609  167 GLU A OE2   
1338 N N     . ARG A 168 ? 0.7994 0.5627 0.5962 -0.0315 -0.0119 0.1399  168 ARG A N     
1339 C CA    . ARG A 168 ? 0.7549 0.5311 0.5513 -0.0383 0.0036  0.1288  168 ARG A CA    
1340 C C     . ARG A 168 ? 0.8171 0.5717 0.5800 -0.0518 0.0184  0.1333  168 ARG A C     
1341 O O     . ARG A 168 ? 0.8037 0.5614 0.5754 -0.0587 0.0369  0.1262  168 ARG A O     
1342 C CB    . ARG A 168 ? 0.7566 0.5512 0.5526 -0.0343 -0.0043 0.1235  168 ARG A CB    
1343 C CG    . ARG A 168 ? 0.6832 0.5036 0.5159 -0.0230 -0.0108 0.1151  168 ARG A CG    
1344 C CD    . ARG A 168 ? 0.6575 0.4952 0.4905 -0.0202 -0.0172 0.1103  168 ARG A CD    
1345 N NE    . ARG A 168 ? 0.7895 0.6497 0.6558 -0.0095 -0.0225 0.1035  168 ARG A NE    
1346 C CZ    . ARG A 168 ? 0.8629 0.7417 0.7385 -0.0059 -0.0263 0.0978  168 ARG A CZ    
1347 N NH1   . ARG A 168 ? 0.7662 0.6444 0.6220 -0.0118 -0.0271 0.0975  168 ARG A NH1   
1348 N NH2   . ARG A 168 ? 0.7290 0.6257 0.6330 0.0032  -0.0288 0.0921  168 ARG A NH2   
1349 N N     . GLU A 169 ? 0.8171 0.5489 0.5413 -0.0561 0.0105  0.1451  169 GLU A N     
1350 C CA    . GLU A 169 ? 0.8407 0.5488 0.5270 -0.0695 0.0260  0.1495  169 GLU A CA    
1351 C C     . GLU A 169 ? 0.8907 0.5834 0.5824 -0.0756 0.0403  0.1535  169 GLU A C     
1352 O O     . GLU A 169 ? 0.9103 0.5905 0.5843 -0.0871 0.0607  0.1529  169 GLU A O     
1353 C CB    . GLU A 169 ? 0.8900 0.5734 0.5288 -0.0731 0.0121  0.1623  169 GLU A CB    
1354 C CG    . GLU A 169 ? 1.1069 0.7639 0.7301 -0.0727 0.0009  0.1786  169 GLU A CG    
1355 C CD    . GLU A 169 ? 1.1550 0.7838 0.7256 -0.0783 -0.0123 0.1920  169 GLU A CD    
1356 O OE1   . GLU A 169 ? 1.1137 0.7427 0.6579 -0.0833 -0.0120 0.1875  169 GLU A OE1   
1357 O OE2   . GLU A 169 ? 1.1404 0.7454 0.6955 -0.0778 -0.0239 0.2071  169 GLU A OE2   
1358 N N     . GLN A 170 ? 0.8838 0.5772 0.6016 -0.0684 0.0315  0.1569  170 GLN A N     
1359 C CA    . GLN A 170 ? 0.8984 0.5793 0.6273 -0.0744 0.0450  0.1589  170 GLN A CA    
1360 C C     . GLN A 170 ? 0.9209 0.6266 0.6946 -0.0728 0.0556  0.1444  170 GLN A C     
1361 O O     . GLN A 170 ? 0.9339 0.6320 0.7224 -0.0783 0.0662  0.1444  170 GLN A O     
1362 C CB    . GLN A 170 ? 0.9291 0.5913 0.6589 -0.0688 0.0304  0.1711  170 GLN A CB    
1363 C CG    . GLN A 170 ? 1.0132 0.6455 0.6976 -0.0721 0.0199  0.1881  170 GLN A CG    
1364 C CD    . GLN A 170 ? 1.2233 0.8301 0.8684 -0.0878 0.0390  0.1943  170 GLN A CD    
1365 O OE1   . GLN A 170 ? 1.3156 0.9101 0.9196 -0.0935 0.0382  0.1989  170 GLN A OE1   
1366 N NE2   . GLN A 170 ? 1.2672 0.8648 0.9242 -0.0954 0.0568  0.1942  170 GLN A NE2   
1367 N N     . ASN A 171 ? 0.8261 0.5600 0.6212 -0.0660 0.0520  0.1324  171 ASN A N     
1368 C CA    . ASN A 171 ? 0.7352 0.4922 0.5717 -0.0631 0.0575  0.1193  171 ASN A CA    
1369 C C     . ASN A 171 ? 0.7315 0.5000 0.5740 -0.0714 0.0764  0.1103  171 ASN A C     
1370 O O     . ASN A 171 ? 0.7472 0.5269 0.5805 -0.0704 0.0771  0.1056  171 ASN A O     
1371 C CB    . ASN A 171 ? 0.7297 0.5091 0.5870 -0.0499 0.0418  0.1124  171 ASN A CB    
1372 C CG    . ASN A 171 ? 0.8221 0.6216 0.7178 -0.0466 0.0445  0.0999  171 ASN A CG    
1373 O OD1   . ASN A 171 ? 0.8010 0.6071 0.7108 -0.0538 0.0581  0.0933  171 ASN A OD1   
1374 N ND2   . ASN A 171 ? 0.7578 0.5665 0.6705 -0.0355 0.0314  0.0966  171 ASN A ND2   
1375 N N     . PRO A 172 ? 0.7622 0.5292 0.6234 -0.0794 0.0917  0.1072  172 PRO A N     
1376 C CA    . PRO A 172 ? 0.7083 0.4863 0.5797 -0.0872 0.1113  0.0990  172 PRO A CA    
1377 C C     . PRO A 172 ? 0.7274 0.5352 0.6251 -0.0802 0.1077  0.0862  172 PRO A C     
1378 O O     . PRO A 172 ? 0.7181 0.5343 0.6178 -0.0846 0.1216  0.0802  172 PRO A O     
1379 C CB    . PRO A 172 ? 0.7188 0.4926 0.6161 -0.0954 0.1239  0.0983  172 PRO A CB    
1380 C CG    . PRO A 172 ? 0.8383 0.6037 0.7441 -0.0897 0.1080  0.1027  172 PRO A CG    
1381 C CD    . PRO A 172 ? 0.8170 0.5693 0.6900 -0.0826 0.0925  0.1121  172 PRO A CD    
1382 N N     . TYR A 173 ? 0.6276 0.4502 0.5449 -0.0695 0.0906  0.0819  173 TYR A N     
1383 C CA    . TYR A 173 ? 0.7162 0.5644 0.6537 -0.0629 0.0866  0.0713  173 TYR A CA    
1384 C C     . TYR A 173 ? 0.7476 0.5990 0.6613 -0.0577 0.0789  0.0725  173 TYR A C     
1385 O O     . TYR A 173 ? 0.6157 0.4860 0.5423 -0.0535 0.0778  0.0644  173 TYR A O     
1386 C CB    . TYR A 173 ? 0.6203 0.4820 0.5865 -0.0544 0.0731  0.0654  173 TYR A CB    
1387 C CG    . TYR A 173 ? 0.6797 0.5401 0.6729 -0.0596 0.0779  0.0623  173 TYR A CG    
1388 C CD1   . TYR A 173 ? 0.6185 0.4921 0.6389 -0.0657 0.0892  0.0548  173 TYR A CD1   
1389 C CD2   . TYR A 173 ? 0.7155 0.5614 0.7094 -0.0585 0.0705  0.0665  173 TYR A CD2   
1390 C CE1   . TYR A 173 ? 0.6457 0.5189 0.6938 -0.0713 0.0919  0.0519  173 TYR A CE1   
1391 C CE2   . TYR A 173 ? 0.6645 0.5081 0.6833 -0.0642 0.0738  0.0631  173 TYR A CE2   
1392 C CZ    . TYR A 173 ? 0.6398 0.4975 0.6859 -0.0709 0.0840  0.0559  173 TYR A CZ    
1393 O OH    . TYR A 173 ? 0.6687 0.5247 0.7421 -0.0773 0.0857  0.0525  173 TYR A OH    
1394 N N     . LYS A 174 ? 0.6837 0.5166 0.5640 -0.0580 0.0724  0.0826  174 LYS A N     
1395 C CA    . LYS A 174 ? 0.8028 0.6390 0.6638 -0.0527 0.0608  0.0842  174 LYS A CA    
1396 C C     . LYS A 174 ? 0.8071 0.6229 0.6260 -0.0603 0.0651  0.0914  174 LYS A C     
1397 O O     . LYS A 174 ? 0.7778 0.5978 0.5816 -0.0583 0.0584  0.0901  174 LYS A O     
1398 C CB    . LYS A 174 ? 0.7182 0.5550 0.5831 -0.0425 0.0411  0.0895  174 LYS A CB    
1399 C CG    . LYS A 174 ? 0.7565 0.6110 0.6568 -0.0341 0.0357  0.0819  174 LYS A CG    
1400 C CD    . LYS A 174 ? 0.9436 0.7908 0.8471 -0.0260 0.0218  0.0879  174 LYS A CD    
1401 C CE    . LYS A 174 ? 1.0133 0.8769 0.9463 -0.0172 0.0166  0.0792  174 LYS A CE    
1402 N NZ    . LYS A 174 ? 1.0046 0.8605 0.9418 -0.0085 0.0052  0.0840  174 LYS A NZ    
1403 N N     . SER A 175 ? 0.7205 0.5132 0.5185 -0.0696 0.0759  0.0988  175 SER A N     
1404 C CA    . SER A 175 ? 0.9032 0.6711 0.6538 -0.0771 0.0780  0.1073  175 SER A CA    
1405 C C     . SER A 175 ? 0.9363 0.7069 0.6715 -0.0829 0.0919  0.0992  175 SER A C     
1406 O O     . SER A 175 ? 0.9179 0.6745 0.6150 -0.0859 0.0867  0.1028  175 SER A O     
1407 C CB    . SER A 175 ? 0.8161 0.5575 0.5482 -0.0865 0.0894  0.1169  175 SER A CB    
1408 O OG    . SER A 175 ? 0.8880 0.6335 0.6370 -0.0943 0.1133  0.1097  175 SER A OG    
1409 N N     . TRP A 176 ? 0.8686 0.6559 0.6335 -0.0845 0.1086  0.0882  176 TRP A N     
1410 C CA    . TRP A 176 ? 0.8901 0.6812 0.6468 -0.0889 0.1235  0.0791  176 TRP A CA    
1411 C C     . TRP A 176 ? 0.8453 0.6469 0.5943 -0.0824 0.1082  0.0751  176 TRP A C     
1412 O O     . TRP A 176 ? 0.9172 0.7122 0.6429 -0.0870 0.1167  0.0703  176 TRP A O     
1413 C CB    . TRP A 176 ? 0.7893 0.6016 0.5908 -0.0888 0.1395  0.0683  176 TRP A CB    
1414 C CG    . TRP A 176 ? 0.7576 0.5972 0.5991 -0.0777 0.1239  0.0625  176 TRP A CG    
1415 C CD1   . TRP A 176 ? 0.7545 0.6018 0.6211 -0.0721 0.1119  0.0648  176 TRP A CD1   
1416 C CD2   . TRP A 176 ? 0.7306 0.5904 0.5878 -0.0710 0.1186  0.0536  176 TRP A CD2   
1417 N NE1   . TRP A 176 ? 0.7347 0.6054 0.6294 -0.0625 0.1002  0.0579  176 TRP A NE1   
1418 C CE2   . TRP A 176 ? 0.7522 0.6313 0.6424 -0.0618 0.1039  0.0515  176 TRP A CE2   
1419 C CE3   . TRP A 176 ? 0.7927 0.6543 0.6379 -0.0723 0.1254  0.0471  176 TRP A CE3   
1420 C CZ2   . TRP A 176 ? 0.7324 0.6321 0.6427 -0.0540 0.0959  0.0443  176 TRP A CZ2   
1421 C CZ3   . TRP A 176 ? 0.7661 0.6491 0.6345 -0.0644 0.1170  0.0397  176 TRP A CZ3   
1422 C CH2   . TRP A 176 ? 0.7791 0.6808 0.6792 -0.0554 0.1024  0.0389  176 TRP A CH2   
1423 N N     . LYS A 177 ? 0.8521 0.6690 0.6205 -0.0721 0.0872  0.0765  177 LYS A N     
1424 C CA    . LYS A 177 ? 0.8701 0.7001 0.6391 -0.0658 0.0731  0.0725  177 LYS A CA    
1425 C C     . LYS A 177 ? 0.9224 0.7371 0.6566 -0.0657 0.0548  0.0819  177 LYS A C     
1426 O O     . LYS A 177 ? 1.0412 0.8614 0.7673 -0.0639 0.0454  0.0789  177 LYS A O     
1427 C CB    . LYS A 177 ? 0.7868 0.6431 0.5984 -0.0547 0.0622  0.0681  177 LYS A CB    
1428 C CG    . LYS A 177 ? 0.9065 0.7800 0.7271 -0.0487 0.0529  0.0620  177 LYS A CG    
1429 C CD    . LYS A 177 ? 0.9567 0.8535 0.8162 -0.0386 0.0447  0.0580  177 LYS A CD    
1430 C CE    . LYS A 177 ? 1.0768 0.9881 0.9422 -0.0331 0.0348  0.0541  177 LYS A CE    
1431 N NZ    . LYS A 177 ? 0.9495 0.8808 0.8472 -0.0236 0.0274  0.0509  177 LYS A NZ    
1432 N N     . LEU A 178 ? 0.9607 0.7560 0.6757 -0.0678 0.0484  0.0936  178 LEU A N     
1433 C CA    . LEU A 178 ? 0.9621 0.7427 0.6472 -0.0672 0.0281  0.1040  178 LEU A CA    
1434 C C     . LEU A 178 ? 1.0000 0.7540 0.6333 -0.0788 0.0348  0.1064  178 LEU A C     
1435 O O     . LEU A 178 ? 1.0141 0.7465 0.6234 -0.0875 0.0502  0.1104  178 LEU A O     
1436 C CB    . LEU A 178 ? 0.9484 0.7184 0.6364 -0.0638 0.0175  0.1162  178 LEU A CB    
1437 C CG    . LEU A 178 ? 1.0236 0.7786 0.6866 -0.0619 -0.0058 0.1288  178 LEU A CG    
1438 C CD1   . LEU A 178 ? 0.8873 0.6647 0.5718 -0.0529 -0.0240 0.1255  178 LEU A CD1   
1439 C CD2   . LEU A 178 ? 0.9810 0.7242 0.6506 -0.0582 -0.0128 0.1403  178 LEU A CD2   
1440 N N     . THR A 179 ? 1.0059 0.7601 0.6208 -0.0794 0.0238  0.1037  179 THR A N     
1441 C CA    . THR A 179 ? 1.1430 0.8716 0.7062 -0.0906 0.0298  0.1033  179 THR A CA    
1442 C C     . THR A 179 ? 1.1587 0.8673 0.6847 -0.0924 0.0045  0.1155  179 THR A C     
1443 O O     . THR A 179 ? 1.1368 0.8573 0.6842 -0.0838 -0.0184 0.1223  179 THR A O     
1444 C CB    . THR A 179 ? 1.1060 0.8468 0.6735 -0.0916 0.0372  0.0892  179 THR A CB    
1445 O OG1   . THR A 179 ? 1.1050 0.8609 0.6849 -0.0850 0.0134  0.0893  179 THR A OG1   
1446 C CG2   . THR A 179 ? 1.1279 0.8931 0.7409 -0.0873 0.0567  0.0780  179 THR A CG2   
1447 N N     . ASP A 180 ? 1.2382 0.9155 0.7077 -0.1039 0.0088  0.1181  180 ASP A N     
1448 C CA    . ASP A 180 ? 1.2376 0.8937 0.6670 -0.1069 -0.0174 0.1292  180 ASP A CA    
1449 C C     . ASP A 180 ? 1.2586 0.9356 0.7079 -0.1008 -0.0404 0.1250  180 ASP A C     
1450 O O     . ASP A 180 ? 1.2850 0.9600 0.7319 -0.0973 -0.0683 0.1355  180 ASP A O     
1451 C CB    . ASP A 180 ? 1.4403 1.0583 0.8013 -0.1213 -0.0073 0.1300  180 ASP A CB    
1452 C CG    . ASP A 180 ? 1.5557 1.1485 0.8917 -0.1283 0.0128  0.1376  180 ASP A CG    
1453 O OD1   . ASP A 180 ? 1.5202 1.1087 0.8652 -0.1244 0.0021  0.1510  180 ASP A OD1   
1454 O OD2   . ASP A 180 ? 1.6466 1.2236 0.9556 -0.1378 0.0405  0.1301  180 ASP A OD2   
1455 N N     . GLU A 181 ? 1.2230 0.9207 0.6954 -0.0993 -0.0290 0.1102  181 GLU A N     
1456 C CA    . GLU A 181 ? 1.2337 0.9511 0.7266 -0.0944 -0.0485 0.1057  181 GLU A CA    
1457 C C     . GLU A 181 ? 1.1908 0.9355 0.7350 -0.0814 -0.0662 0.1120  181 GLU A C     
1458 O O     . GLU A 181 ? 1.1816 0.9344 0.7347 -0.0781 -0.0904 0.1161  181 GLU A O     
1459 C CB    . GLU A 181 ? 1.2450 0.9779 0.7544 -0.0950 -0.0305 0.0891  181 GLU A CB    
1460 C CG    . GLU A 181 ? 1.4293 1.1792 0.9556 -0.0919 -0.0486 0.0839  181 GLU A CG    
1461 C CD    . GLU A 181 ? 1.5471 1.3101 1.0897 -0.0923 -0.0307 0.0681  181 GLU A CD    
1462 O OE1   . GLU A 181 ? 1.6101 1.3627 1.1392 -0.0971 -0.0052 0.0607  181 GLU A OE1   
1463 O OE2   . GLU A 181 ? 1.4595 1.2431 1.0304 -0.0876 -0.0416 0.0635  181 GLU A OE2   
1464 N N     . ASP A 182 ? 1.1148 0.8733 0.6939 -0.0744 -0.0542 0.1125  182 ASP A N     
1465 C CA    . ASP A 182 ? 0.9788 0.7605 0.6043 -0.0620 -0.0683 0.1174  182 ASP A CA    
1466 C C     . ASP A 182 ? 1.0324 0.7995 0.6446 -0.0602 -0.0920 0.1331  182 ASP A C     
1467 O O     . ASP A 182 ? 1.0491 0.8310 0.6867 -0.0526 -0.1131 0.1377  182 ASP A O     
1468 C CB    . ASP A 182 ? 0.9569 0.7513 0.6155 -0.0564 -0.0501 0.1139  182 ASP A CB    
1469 C CG    . ASP A 182 ? 0.9970 0.8055 0.6711 -0.0578 -0.0282 0.0994  182 ASP A CG    
1470 O OD1   . ASP A 182 ? 0.9730 0.7984 0.6621 -0.0555 -0.0314 0.0914  182 ASP A OD1   
1471 O OD2   . ASP A 182 ? 1.0337 0.8362 0.7065 -0.0616 -0.0080 0.0963  182 ASP A OD2   
1472 N N     . TRP A 183 ? 1.0804 0.8179 0.6540 -0.0672 -0.0884 0.1421  183 TRP A N     
1473 C CA    . TRP A 183 ? 1.1253 0.8433 0.6785 -0.0669 -0.1119 0.1584  183 TRP A CA    
1474 C C     . TRP A 183 ? 1.1329 0.8478 0.6682 -0.0697 -0.1373 0.1611  183 TRP A C     
1475 O O     . TRP A 183 ? 1.1000 0.8222 0.6551 -0.0626 -0.1624 0.1705  183 TRP A O     
1476 C CB    . TRP A 183 ? 1.1020 0.7837 0.6054 -0.0769 -0.1018 0.1668  183 TRP A CB    
1477 C CG    . TRP A 183 ? 1.1152 0.7966 0.6369 -0.0747 -0.0816 0.1675  183 TRP A CG    
1478 C CD1   . TRP A 183 ? 1.1560 0.8360 0.6751 -0.0806 -0.0524 0.1583  183 TRP A CD1   
1479 C CD2   . TRP A 183 ? 1.0698 0.7515 0.6166 -0.0664 -0.0896 0.1780  183 TRP A CD2   
1480 N NE1   . TRP A 183 ? 1.1767 0.8565 0.7179 -0.0772 -0.0426 0.1624  183 TRP A NE1   
1481 C CE2   . TRP A 183 ? 1.1174 0.7971 0.6743 -0.0685 -0.0648 0.1741  183 TRP A CE2   
1482 C CE3   . TRP A 183 ? 1.0511 0.7343 0.6153 -0.0572 -0.1151 0.1899  183 TRP A CE3   
1483 C CZ2   . TRP A 183 ? 1.0425 0.7202 0.6232 -0.0623 -0.0651 0.1813  183 TRP A CZ2   
1484 C CZ3   . TRP A 183 ? 1.0379 0.7189 0.6262 -0.0502 -0.1142 0.1970  183 TRP A CZ3   
1485 C CH2   . TRP A 183 ? 0.9775 0.6549 0.5722 -0.0530 -0.0895 0.1925  183 TRP A CH2   
1486 N N     . ARG A 184 ? 1.1830 0.8869 0.6824 -0.0800 -0.1311 0.1526  184 ARG A N     
1487 C CA    . ARG A 184 ? 1.2219 0.9201 0.7005 -0.0845 -0.1561 0.1544  184 ARG A CA    
1488 C C     . ARG A 184 ? 1.1514 0.8856 0.6850 -0.0749 -0.1696 0.1495  184 ARG A C     
1489 O O     . ARG A 184 ? 1.1494 0.8867 0.6895 -0.0731 -0.1978 0.1570  184 ARG A O     
1490 C CB    . ARG A 184 ? 1.3141 0.9914 0.7421 -0.0978 -0.1439 0.1441  184 ARG A CB    
1491 C CG    . ARG A 184 ? 1.4755 1.1123 0.8401 -0.1092 -0.1320 0.1497  184 ARG A CG    
1492 C CD    . ARG A 184 ? 1.5801 1.1932 0.8903 -0.1225 -0.1248 0.1398  184 ARG A CD    
1493 N NE    . ARG A 184 ? 1.6899 1.3261 1.0284 -0.1210 -0.1064 0.1219  184 ARG A NE    
1494 C CZ    . ARG A 184 ? 1.6493 1.2829 0.9827 -0.1246 -0.0734 0.1103  184 ARG A CZ    
1495 N NH1   . ARG A 184 ? 1.5643 1.1731 0.8643 -0.1310 -0.0528 0.1139  184 ARG A NH1   
1496 N NH2   . ARG A 184 ? 1.5460 1.2023 0.9105 -0.1217 -0.0606 0.0953  184 ARG A NH2   
1497 N N     . ASN A 185 ? 1.1110 0.8722 0.6851 -0.0689 -0.1500 0.1374  185 ASN A N     
1498 C CA    . ASN A 185 ? 1.0906 0.8855 0.7171 -0.0599 -0.1585 0.1326  185 ASN A CA    
1499 C C     . ASN A 185 ? 1.0876 0.8967 0.7535 -0.0483 -0.1757 0.1438  185 ASN A C     
1500 O O     . ASN A 185 ? 0.9826 0.8154 0.6870 -0.0418 -0.1889 0.1433  185 ASN A O     
1501 C CB    . ASN A 185 ? 0.9863 0.8033 0.6442 -0.0556 -0.1330 0.1191  185 ASN A CB    
1502 C CG    . ASN A 185 ? 1.1569 0.9707 0.7949 -0.0640 -0.1212 0.1061  185 ASN A CG    
1503 O OD1   . ASN A 185 ? 1.2562 1.0495 0.8533 -0.0738 -0.1304 0.1060  185 ASN A OD1   
1504 N ND2   . ASN A 185 ? 1.1041 0.9365 0.7697 -0.0603 -0.1012 0.0949  185 ASN A ND2   
1505 N N     . ARG A 186 ? 1.0437 0.8392 0.7036 -0.0452 -0.1741 0.1536  186 ARG A N     
1506 C CA    . ARG A 186 ? 0.9594 0.7642 0.6536 -0.0343 -0.1924 0.1651  186 ARG A CA    
1507 C C     . ARG A 186 ? 0.9981 0.8008 0.6895 -0.0354 -0.2243 0.1743  186 ARG A C     
1508 O O     . ARG A 186 ? 0.8873 0.7096 0.6232 -0.0253 -0.2396 0.1797  186 ARG A O     
1509 C CB    . ARG A 186 ? 0.9213 0.7046 0.6008 -0.0328 -0.1884 0.1756  186 ARG A CB    
1510 C CG    . ARG A 186 ? 0.9229 0.7173 0.6289 -0.0268 -0.1637 0.1685  186 ARG A CG    
1511 C CD    . ARG A 186 ? 0.8985 0.6690 0.5880 -0.0270 -0.1602 0.1790  186 ARG A CD    
1512 N NE    . ARG A 186 ? 1.1272 0.8872 0.8191 -0.0218 -0.1858 0.1948  186 ARG A NE    
1513 C CZ    . ARG A 186 ? 0.9880 0.7650 0.7266 -0.0086 -0.1956 0.1988  186 ARG A CZ    
1514 N NH1   . ARG A 186 ? 0.9910 0.7951 0.7738 0.0002  -0.1822 0.1880  186 ARG A NH1   
1515 N NH2   . ARG A 186 ? 0.8908 0.6562 0.6311 -0.0041 -0.2192 0.2139  186 ARG A NH2   
1516 N N     . GLU A 187 ? 0.9746 0.7535 0.6152 -0.0478 -0.2346 0.1758  187 GLU A N     
1517 C CA    . GLU A 187 ? 1.0274 0.8026 0.6624 -0.0505 -0.2675 0.1842  187 GLU A CA    
1518 C C     . GLU A 187 ? 1.0413 0.8481 0.7197 -0.0473 -0.2754 0.1760  187 GLU A C     
1519 O O     . GLU A 187 ? 0.9830 0.7960 0.6774 -0.0463 -0.3037 0.1836  187 GLU A O     
1520 C CB    . GLU A 187 ? 0.9722 0.7116 0.5364 -0.0659 -0.2752 0.1858  187 GLU A CB    
1521 C CG    . GLU A 187 ? 1.3907 1.1176 0.9401 -0.0692 -0.3128 0.1984  187 GLU A CG    
1522 C CD    . GLU A 187 ? 1.5877 1.2866 1.0770 -0.0842 -0.3148 0.1924  187 GLU A CD    
1523 O OE1   . GLU A 187 ? 1.6467 1.3279 1.0928 -0.0931 -0.2918 0.1837  187 GLU A OE1   
1524 O OE2   . GLU A 187 ? 1.5755 1.2698 1.0618 -0.0871 -0.3387 0.1959  187 GLU A OE2   
1525 N N     . LYS A 188 ? 0.9494 0.7756 0.6478 -0.0461 -0.2517 0.1614  188 LYS A N     
1526 C CA    . LYS A 188 ? 0.9508 0.8057 0.6891 -0.0438 -0.2557 0.1533  188 LYS A CA    
1527 C C     . LYS A 188 ? 0.9068 0.7937 0.7106 -0.0292 -0.2536 0.1550  188 LYS A C     
1528 O O     . LYS A 188 ? 0.8367 0.7488 0.6777 -0.0265 -0.2537 0.1487  188 LYS A O     
1529 C CB    . LYS A 188 ? 0.9446 0.8022 0.6699 -0.0500 -0.2314 0.1371  188 LYS A CB    
1530 C CG    . LYS A 188 ? 1.0828 0.9105 0.7464 -0.0648 -0.2327 0.1327  188 LYS A CG    
1531 C CD    . LYS A 188 ? 1.0478 0.8741 0.6975 -0.0692 -0.2030 0.1176  188 LYS A CD    
1532 C CE    . LYS A 188 ? 1.1857 0.9806 0.7737 -0.0838 -0.2023 0.1120  188 LYS A CE    
1533 N NZ    . LYS A 188 ? 1.2370 1.0277 0.8114 -0.0872 -0.1709 0.0981  188 LYS A NZ    
1534 N N     . SER A 189 ? 0.8859 0.7708 0.7036 -0.0202 -0.2507 0.1631  189 SER A N     
1535 C CA    . SER A 189 ? 0.7963 0.7087 0.6726 -0.0061 -0.2446 0.1630  189 SER A CA    
1536 C C     . SER A 189 ? 0.8150 0.7506 0.7375 -0.0008 -0.2654 0.1674  189 SER A C     
1537 O O     . SER A 189 ? 0.7235 0.6860 0.6904 0.0065  -0.2541 0.1608  189 SER A O     
1538 C CB    . SER A 189 ? 0.8512 0.7524 0.7305 0.0019  -0.2413 0.1718  189 SER A CB    
1539 O OG    . SER A 189 ? 0.8664 0.7531 0.7167 -0.0017 -0.2177 0.1657  189 SER A OG    
1540 N N     . PRO A 190 ? 0.8265 0.7536 0.7431 -0.0039 -0.2951 0.1786  190 PRO A N     
1541 C CA    . PRO A 190 ? 0.7381 0.6907 0.7057 0.0007  -0.3144 0.1821  190 PRO A CA    
1542 C C     . PRO A 190 ? 0.7131 0.6862 0.6975 -0.0042 -0.3063 0.1698  190 PRO A C     
1543 O O     . PRO A 190 ? 0.7630 0.7650 0.8020 0.0035  -0.3028 0.1677  190 PRO A O     
1544 C CB    . PRO A 190 ? 0.8326 0.7659 0.7752 -0.0061 -0.3490 0.1949  190 PRO A CB    
1545 C CG    . PRO A 190 ? 0.8620 0.7626 0.7562 -0.0078 -0.3470 0.2025  190 PRO A CG    
1546 C CD    . PRO A 190 ? 0.7528 0.6467 0.6192 -0.0111 -0.3132 0.1898  190 PRO A CD    
1547 N N     . GLN A 191 ? 0.7445 0.7020 0.6827 -0.0170 -0.3017 0.1616  191 GLN A N     
1548 C CA    . GLN A 191 ? 0.7765 0.7502 0.7275 -0.0222 -0.2932 0.1496  191 GLN A CA    
1549 C C     . GLN A 191 ? 0.6765 0.6704 0.6575 -0.0138 -0.2631 0.1403  191 GLN A C     
1550 O O     . GLN A 191 ? 0.6468 0.6647 0.6670 -0.0114 -0.2586 0.1353  191 GLN A O     
1551 C CB    . GLN A 191 ? 0.7592 0.7080 0.6513 -0.0368 -0.2919 0.1421  191 GLN A CB    
1552 C CG    . GLN A 191 ? 0.9660 0.8894 0.8181 -0.0461 -0.3208 0.1509  191 GLN A CG    
1553 C CD    . GLN A 191 ? 1.1307 1.0210 0.9133 -0.0585 -0.3121 0.1447  191 GLN A CD    
1554 O OE1   . GLN A 191 ? 1.0909 0.9799 0.8585 -0.0654 -0.2977 0.1318  191 GLN A OE1   
1555 N NE2   . GLN A 191 ? 1.0713 0.9334 0.8111 -0.0611 -0.3193 0.1539  191 GLN A NE2   
1556 N N     . TYR A 192 ? 0.7514 0.7346 0.7134 -0.0100 -0.2427 0.1380  192 TYR A N     
1557 C CA    . TYR A 192 ? 0.6690 0.6691 0.6570 -0.0020 -0.2164 0.1297  192 TYR A CA    
1558 C C     . TYR A 192 ? 0.6565 0.6807 0.7006 0.0106  -0.2174 0.1342  192 TYR A C     
1559 O O     . TYR A 192 ? 0.5952 0.6396 0.6699 0.0152  -0.2027 0.1275  192 TYR A O     
1560 C CB    . TYR A 192 ? 0.6897 0.6734 0.6499 -0.0005 -0.1977 0.1275  192 TYR A CB    
1561 C CG    . TYR A 192 ? 0.8049 0.7748 0.7256 -0.0102 -0.1829 0.1177  192 TYR A CG    
1562 C CD1   . TYR A 192 ? 0.6372 0.6198 0.5698 -0.0091 -0.1624 0.1067  192 TYR A CD1   
1563 C CD2   . TYR A 192 ? 0.8609 0.8037 0.7319 -0.0205 -0.1891 0.1198  192 TYR A CD2   
1564 C CE1   . TYR A 192 ? 0.7749 0.7453 0.6755 -0.0172 -0.1488 0.0977  192 TYR A CE1   
1565 C CE2   . TYR A 192 ? 0.9536 0.8834 0.7904 -0.0290 -0.1734 0.1102  192 TYR A CE2   
1566 C CZ    . TYR A 192 ? 0.8949 0.8393 0.7489 -0.0270 -0.1535 0.0992  192 TYR A CZ    
1567 O OH    . TYR A 192 ? 0.9937 0.9252 0.8171 -0.0348 -0.1380 0.0899  192 TYR A OH    
1568 N N     . ILE A 193 ? 0.7071 0.7281 0.7644 0.0167  -0.2335 0.1457  193 ILE A N     
1569 C CA    . ILE A 193 ? 0.7068 0.7498 0.8197 0.0296  -0.2333 0.1498  193 ILE A CA    
1570 C C     . ILE A 193 ? 0.6334 0.7007 0.7863 0.0284  -0.2424 0.1490  193 ILE A C     
1571 O O     . ILE A 193 ? 0.5894 0.6790 0.7842 0.0360  -0.2285 0.1451  193 ILE A O     
1572 C CB    . ILE A 193 ? 0.7370 0.7694 0.8561 0.0363  -0.2506 0.1630  193 ILE A CB    
1573 C CG1   . ILE A 193 ? 0.7446 0.7531 0.8268 0.0372  -0.2386 0.1634  193 ILE A CG1   
1574 C CG2   . ILE A 193 ? 0.6877 0.7430 0.8682 0.0501  -0.2508 0.1671  193 ILE A CG2   
1575 C CD1   . ILE A 193 ? 0.8064 0.8216 0.8962 0.0431  -0.2094 0.1529  193 ILE A CD1   
1576 N N     . GLU A 194 ? 0.5942 0.6562 0.7335 0.0183  -0.2656 0.1524  194 GLU A N     
1577 C CA    . GLU A 194 ? 0.5778 0.6622 0.7547 0.0151  -0.2751 0.1511  194 GLU A CA    
1578 C C     . GLU A 194 ? 0.5864 0.6822 0.7664 0.0119  -0.2516 0.1386  194 GLU A C     
1579 O O     . GLU A 194 ? 0.5656 0.6858 0.7918 0.0161  -0.2443 0.1366  194 GLU A O     
1580 C CB    . GLU A 194 ? 0.6994 0.7710 0.8517 0.0027  -0.3048 0.1557  194 GLU A CB    
1581 C CG    . GLU A 194 ? 0.8677 0.9589 1.0515 -0.0039 -0.3149 0.1525  194 GLU A CG    
1582 C CD    . GLU A 194 ? 0.9470 1.0223 1.1015 -0.0173 -0.3459 0.1560  194 GLU A CD    
1583 O OE1   . GLU A 194 ? 0.8708 0.9255 0.9734 -0.0288 -0.3427 0.1481  194 GLU A OE1   
1584 O OE2   . GLU A 194 ? 0.8680 0.9507 1.0515 -0.0162 -0.3736 0.1664  194 GLU A OE2   
1585 N N     . ALA A 195 ? 0.5767 0.6545 0.7086 0.0045  -0.2391 0.1304  195 ALA A N     
1586 C CA    . ALA A 195 ? 0.6146 0.7010 0.7478 0.0017  -0.2182 0.1192  195 ALA A CA    
1587 C C     . ALA A 195 ? 0.5730 0.6744 0.7353 0.0134  -0.1942 0.1162  195 ALA A C     
1588 O O     . ALA A 195 ? 0.5516 0.6704 0.7409 0.0147  -0.1821 0.1114  195 ALA A O     
1589 C CB    . ALA A 195 ? 0.5254 0.5887 0.6038 -0.0075 -0.2095 0.1114  195 ALA A CB    
1590 N N     . ALA A 196 ? 0.5463 0.6397 0.7021 0.0217  -0.1874 0.1192  196 ALA A N     
1591 C CA    . ALA A 196 ? 0.4907 0.5952 0.6703 0.0326  -0.1659 0.1159  196 ALA A CA    
1592 C C     . ALA A 196 ? 0.5359 0.6640 0.7706 0.0407  -0.1676 0.1201  196 ALA A C     
1593 O O     . ALA A 196 ? 0.5112 0.6532 0.7687 0.0457  -0.1490 0.1151  196 ALA A O     
1594 C CB    . ALA A 196 ? 0.5558 0.6446 0.7169 0.0389  -0.1606 0.1182  196 ALA A CB    
1595 N N     . ASN A 197 ? 0.4932 0.6257 0.7503 0.0419  -0.1898 0.1296  197 ASN A N     
1596 C CA    . ASN A 197 ? 0.4781 0.6348 0.7937 0.0500  -0.1907 0.1339  197 ASN A CA    
1597 C C     . ASN A 197 ? 0.5054 0.6805 0.8447 0.0437  -0.1872 0.1296  197 ASN A C     
1598 O O     . ASN A 197 ? 0.5253 0.7191 0.9030 0.0500  -0.1709 0.1276  197 ASN A O     
1599 C CB    . ASN A 197 ? 0.5583 0.7158 0.8958 0.0530  -0.2174 0.1458  197 ASN A CB    
1600 C CG    . ASN A 197 ? 0.6140 0.7592 0.9479 0.0637  -0.2157 0.1509  197 ASN A CG    
1601 O OD1   . ASN A 197 ? 0.7825 0.9083 1.0875 0.0611  -0.2331 0.1577  197 ASN A OD1   
1602 N ND2   . ASN A 197 ? 0.5931 0.7473 0.9538 0.0753  -0.1941 0.1475  197 ASN A ND2   
1603 N N     . GLU A 198 ? 0.4917 0.6600 0.8067 0.0308  -0.2009 0.1279  198 GLU A N     
1604 C CA    . GLU A 198 ? 0.5109 0.6940 0.8452 0.0238  -0.1962 0.1231  198 GLU A CA    
1605 C C     . GLU A 198 ? 0.4565 0.6407 0.7808 0.0259  -0.1668 0.1140  198 GLU A C     
1606 O O     . GLU A 198 ? 0.4382 0.6398 0.7953 0.0271  -0.1539 0.1121  198 GLU A O     
1607 C CB    . GLU A 198 ? 0.5018 0.6731 0.8063 0.0093  -0.2159 0.1215  198 GLU A CB    
1608 C CG    . GLU A 198 ? 0.5652 0.7509 0.8926 0.0013  -0.2137 0.1171  198 GLU A CG    
1609 C CD    . GLU A 198 ? 0.6170 0.7911 0.9203 -0.0132 -0.2365 0.1157  198 GLU A CD    
1610 O OE1   . GLU A 198 ? 0.6123 0.7677 0.8817 -0.0171 -0.2556 0.1190  198 GLU A OE1   
1611 O OE2   . GLU A 198 ? 0.6166 0.7986 0.9332 -0.0212 -0.2349 0.1112  198 GLU A OE2   
1612 N N     . MET A 199 ? 0.4621 0.6272 0.7419 0.0261  -0.1562 0.1090  199 MET A N     
1613 C CA    . MET A 199 ? 0.4532 0.6176 0.7220 0.0288  -0.1307 0.1012  199 MET A CA    
1614 C C     . MET A 199 ? 0.4718 0.6507 0.7761 0.0405  -0.1136 0.1021  199 MET A C     
1615 O O     . MET A 199 ? 0.4529 0.6418 0.7718 0.0413  -0.0970 0.0984  199 MET A O     
1616 C CB    . MET A 199 ? 0.4549 0.5974 0.6764 0.0281  -0.1250 0.0971  199 MET A CB    
1617 C CG    . MET A 199 ? 0.4277 0.5675 0.6365 0.0319  -0.1014 0.0897  199 MET A CG    
1618 S SD    . MET A 199 ? 0.4587 0.5747 0.6186 0.0303  -0.0974 0.0856  199 MET A SD    
1619 C CE    . MET A 199 ? 0.4119 0.5248 0.5825 0.0407  -0.1007 0.0921  199 MET A CE    
1620 N N     . PHE A 200 ? 0.4527 0.6308 0.7695 0.0498  -0.1168 0.1070  200 PHE A N     
1621 C CA    . PHE A 200 ? 0.4642 0.6544 0.8155 0.0615  -0.1005 0.1075  200 PHE A CA    
1622 C C     . PHE A 200 ? 0.4998 0.7133 0.8998 0.0615  -0.0982 0.1099  200 PHE A C     
1623 O O     . PHE A 200 ? 0.4239 0.6462 0.8399 0.0655  -0.0766 0.1063  200 PHE A O     
1624 C CB    . PHE A 200 ? 0.4418 0.6274 0.8041 0.0710  -0.1085 0.1134  200 PHE A CB    
1625 C CG    . PHE A 200 ? 0.4760 0.6384 0.7940 0.0710  -0.1100 0.1119  200 PHE A CG    
1626 C CD1   . PHE A 200 ? 0.4576 0.6080 0.7386 0.0678  -0.0952 0.1037  200 PHE A CD1   
1627 C CD2   . PHE A 200 ? 0.4714 0.6238 0.7865 0.0740  -0.1267 0.1192  200 PHE A CD2   
1628 C CE1   . PHE A 200 ? 0.5155 0.6459 0.7600 0.0673  -0.0959 0.1024  200 PHE A CE1   
1629 C CE2   . PHE A 200 ? 0.5132 0.6436 0.7883 0.0732  -0.1268 0.1184  200 PHE A CE2   
1630 C CZ    . PHE A 200 ? 0.4925 0.6126 0.7335 0.0696  -0.1109 0.1096  200 PHE A CZ    
1631 N N     . GLU A 201 ? 0.4717 0.6947 0.8957 0.0565  -0.1206 0.1163  201 GLU A N     
1632 C CA    . GLU A 201 ? 0.4588 0.7059 0.9354 0.0557  -0.1199 0.1193  201 GLU A CA    
1633 C C     . GLU A 201 ? 0.3900 0.6413 0.8612 0.0482  -0.1040 0.1133  201 GLU A C     
1634 O O     . GLU A 201 ? 0.4482 0.7164 0.9571 0.0508  -0.0885 0.1134  201 GLU A O     
1635 C CB    . GLU A 201 ? 0.4648 0.7192 0.9630 0.0491  -0.1504 0.1266  201 GLU A CB    
1636 C CG    . GLU A 201 ? 0.6726 0.9239 1.1823 0.0565  -0.1690 0.1348  201 GLU A CG    
1637 C CD    . GLU A 201 ? 0.8838 1.1397 1.4088 0.0485  -0.2023 0.1423  201 GLU A CD    
1638 O OE1   . GLU A 201 ? 1.0124 1.2882 1.5783 0.0434  -0.2076 0.1437  201 GLU A OE1   
1639 O OE2   . GLU A 201 ? 0.8996 1.1381 1.3941 0.0466  -0.2235 0.1469  201 GLU A OE2   
1640 N N     . LYS A 202 ? 0.3908 0.6263 0.8165 0.0390  -0.1067 0.1082  202 LYS A N     
1641 C CA    . LYS A 202 ? 0.4311 0.6705 0.8557 0.0309  -0.0963 0.1038  202 LYS A CA    
1642 C C     . LYS A 202 ? 0.4007 0.6307 0.7982 0.0341  -0.0709 0.0975  202 LYS A C     
1643 O O     . LYS A 202 ? 0.4167 0.6527 0.8232 0.0303  -0.0577 0.0956  202 LYS A O     
1644 C CB    . LYS A 202 ? 0.3914 0.6206 0.7900 0.0176  -0.1156 0.1020  202 LYS A CB    
1645 C CG    . LYS A 202 ? 0.4341 0.6736 0.8624 0.0124  -0.1424 0.1084  202 LYS A CG    
1646 C CD    . LYS A 202 ? 0.4387 0.6674 0.8421 -0.0019 -0.1607 0.1054  202 LYS A CD    
1647 C CE    . LYS A 202 ? 0.4576 0.6967 0.8920 -0.0075 -0.1893 0.1120  202 LYS A CE    
1648 N NZ    . LYS A 202 ? 0.5762 0.7992 0.9769 -0.0216 -0.2096 0.1084  202 LYS A NZ    
1649 N N     . THR A 203 ? 0.3763 0.5917 0.7422 0.0406  -0.0643 0.0946  203 THR A N     
1650 C CA    . THR A 203 ? 0.3889 0.5934 0.7252 0.0424  -0.0444 0.0885  203 THR A CA    
1651 C C     . THR A 203 ? 0.4561 0.6580 0.7929 0.0541  -0.0280 0.0872  203 THR A C     
1652 O O     . THR A 203 ? 0.4102 0.5995 0.7166 0.0560  -0.0155 0.0821  203 THR A O     
1653 C CB    . THR A 203 ? 0.4033 0.5890 0.6933 0.0364  -0.0513 0.0839  203 THR A CB    
1654 O OG1   . THR A 203 ? 0.3881 0.5636 0.6619 0.0401  -0.0612 0.0852  203 THR A OG1   
1655 C CG2   . THR A 203 ? 0.3988 0.5840 0.6848 0.0245  -0.0657 0.0837  203 THR A CG2   
1656 N N     . ASP A 204 ? 0.4233 0.6358 0.7943 0.0620  -0.0284 0.0914  204 ASP A N     
1657 C CA    . ASP A 204 ? 0.4283 0.6385 0.8046 0.0734  -0.0107 0.0895  204 ASP A CA    
1658 C C     . ASP A 204 ? 0.4736 0.6947 0.8723 0.0750  0.0110  0.0885  204 ASP A C     
1659 O O     . ASP A 204 ? 0.3935 0.6327 0.8372 0.0764  0.0128  0.0929  204 ASP A O     
1660 C CB    . ASP A 204 ? 0.4366 0.6521 0.8413 0.0815  -0.0206 0.0945  204 ASP A CB    
1661 C CG    . ASP A 204 ? 0.4342 0.6448 0.8438 0.0937  -0.0026 0.0916  204 ASP A CG    
1662 O OD1   . ASP A 204 ? 0.4319 0.6304 0.8122 0.0953  0.0143  0.0851  204 ASP A OD1   
1663 O OD2   . ASP A 204 ? 0.5787 0.7964 1.0216 0.1018  -0.0062 0.0957  204 ASP A OD2   
1664 N N     . LYS A 205 ? 0.4612 0.6709 0.8291 0.0745  0.0275  0.0833  205 LYS A N     
1665 C CA    . LYS A 205 ? 0.4674 0.6829 0.8468 0.0742  0.0487  0.0827  205 LYS A CA    
1666 C C     . LYS A 205 ? 0.4352 0.6389 0.7970 0.0831  0.0702  0.0779  205 LYS A C     
1667 O O     . LYS A 205 ? 0.4898 0.6774 0.8194 0.0868  0.0681  0.0736  205 LYS A O     
1668 C CB    . LYS A 205 ? 0.4129 0.6234 0.7692 0.0640  0.0484  0.0818  205 LYS A CB    
1669 C CG    . LYS A 205 ? 0.4462 0.6660 0.8175 0.0542  0.0289  0.0852  205 LYS A CG    
1670 C CD    . LYS A 205 ? 0.4442 0.6861 0.8693 0.0534  0.0284  0.0907  205 LYS A CD    
1671 C CE    . LYS A 205 ? 0.4038 0.6528 0.8408 0.0424  0.0068  0.0934  205 LYS A CE    
1672 N NZ    . LYS A 205 ? 0.4576 0.7292 0.9505 0.0408  0.0025  0.0991  205 LYS A NZ    
1673 N N     . LYS A 206 ? 0.4590 0.6698 0.8413 0.0858  0.0916  0.0784  206 LYS A N     
1674 C CA    . LYS A 206 ? 0.4916 0.6898 0.8569 0.0940  0.1141  0.0734  206 LYS A CA    
1675 C C     . LYS A 206 ? 0.5122 0.6880 0.8220 0.0914  0.1167  0.0683  206 LYS A C     
1676 O O     . LYS A 206 ? 0.4572 0.6169 0.7407 0.0976  0.1230  0.0627  206 LYS A O     
1677 C CB    . LYS A 206 ? 0.5660 0.7747 0.9603 0.0953  0.1383  0.0753  206 LYS A CB    
1678 C CG    . LYS A 206 ? 0.8115 1.0047 1.1848 0.1030  0.1645  0.0695  206 LYS A CG    
1679 C CD    . LYS A 206 ? 0.9437 1.1478 1.3484 0.1040  0.1906  0.0718  206 LYS A CD    
1680 C CE    . LYS A 206 ? 1.0538 1.2406 1.4371 0.1122  0.2183  0.0653  206 LYS A CE    
1681 N NZ    . LYS A 206 ? 1.0080 1.2050 1.4234 0.1133  0.2469  0.0675  206 LYS A NZ    
1682 N N     . ASN A 207 ? 0.4235 0.5976 0.7166 0.0822  0.1109  0.0700  207 ASN A N     
1683 C CA    . ASN A 207 ? 0.4710 0.6257 0.7164 0.0792  0.1106  0.0663  207 ASN A CA    
1684 C C     . ASN A 207 ? 0.5099 0.6568 0.7335 0.0776  0.0903  0.0637  207 ASN A C     
1685 O O     . ASN A 207 ? 0.4827 0.6142 0.6701 0.0760  0.0885  0.0603  207 ASN A O     
1686 C CB    . ASN A 207 ? 0.5219 0.6781 0.7629 0.0706  0.1134  0.0699  207 ASN A CB    
1687 C CG    . ASN A 207 ? 0.6264 0.7981 0.8948 0.0629  0.0970  0.0742  207 ASN A CG    
1688 O OD1   . ASN A 207 ? 0.5162 0.7054 0.8254 0.0627  0.0976  0.0780  207 ASN A OD1   
1689 N ND2   . ASN A 207 ? 0.3807 0.5456 0.6274 0.0566  0.0820  0.0732  207 ASN A ND2   
1690 N N     . ALA A 208 ? 0.4352 0.5920 0.6801 0.0774  0.0745  0.0659  208 ALA A N     
1691 C CA    . ALA A 208 ? 0.4196 0.5686 0.6441 0.0747  0.0565  0.0642  208 ALA A CA    
1692 C C     . ALA A 208 ? 0.4402 0.5964 0.6879 0.0784  0.0449  0.0667  208 ALA A C     
1693 O O     . ALA A 208 ? 0.4137 0.5789 0.6769 0.0735  0.0297  0.0708  208 ALA A O     
1694 C CB    . ALA A 208 ? 0.3913 0.5420 0.6081 0.0648  0.0455  0.0656  208 ALA A CB    
1695 N N     . PRO A 209 ? 0.3664 0.5171 0.6162 0.0872  0.0513  0.0646  209 PRO A N     
1696 C CA    . PRO A 209 ? 0.4414 0.5992 0.7187 0.0922  0.0418  0.0683  209 PRO A CA    
1697 C C     . PRO A 209 ? 0.4423 0.5910 0.7012 0.0894  0.0230  0.0691  209 PRO A C     
1698 O O     . PRO A 209 ? 0.4116 0.5461 0.6362 0.0865  0.0214  0.0649  209 PRO A O     
1699 C CB    . PRO A 209 ? 0.4049 0.5564 0.6871 0.1029  0.0582  0.0646  209 PRO A CB    
1700 C CG    . PRO A 209 ? 0.4805 0.6139 0.7206 0.1020  0.0680  0.0576  209 PRO A CG    
1701 C CD    . PRO A 209 ? 0.4302 0.5666 0.6574 0.0931  0.0677  0.0586  209 PRO A CD    
1702 N N     . TRP A 210 ? 0.4567 0.6137 0.7400 0.0901  0.0085  0.0751  210 TRP A N     
1703 C CA    . TRP A 210 ? 0.4271 0.5740 0.6972 0.0897  -0.0076 0.0773  210 TRP A CA    
1704 C C     . TRP A 210 ? 0.4320 0.5726 0.7127 0.1005  -0.0024 0.0771  210 TRP A C     
1705 O O     . TRP A 210 ? 0.4766 0.6282 0.7931 0.1079  0.0029  0.0797  210 TRP A O     
1706 C CB    . TRP A 210 ? 0.4042 0.5603 0.6913 0.0844  -0.0281 0.0848  210 TRP A CB    
1707 C CG    . TRP A 210 ? 0.4386 0.5917 0.7016 0.0727  -0.0375 0.0839  210 TRP A CG    
1708 C CD1   . TRP A 210 ? 0.4178 0.5824 0.6926 0.0656  -0.0404 0.0848  210 TRP A CD1   
1709 C CD2   . TRP A 210 ? 0.4267 0.5636 0.6511 0.0669  -0.0437 0.0812  210 TRP A CD2   
1710 N NE1   . TRP A 210 ? 0.4464 0.6016 0.6908 0.0561  -0.0481 0.0825  210 TRP A NE1   
1711 C CE2   . TRP A 210 ? 0.4218 0.5606 0.6357 0.0569  -0.0496 0.0802  210 TRP A CE2   
1712 C CE3   . TRP A 210 ? 0.4105 0.5312 0.6098 0.0689  -0.0440 0.0794  210 TRP A CE3   
1713 C CZ2   . TRP A 210 ? 0.3800 0.5052 0.5597 0.0495  -0.0542 0.0772  210 TRP A CZ2   
1714 C CZ3   . TRP A 210 ? 0.4209 0.5293 0.5876 0.0610  -0.0488 0.0770  210 TRP A CZ3   
1715 C CH2   . TRP A 210 ? 0.4228 0.5337 0.5801 0.0518  -0.0533 0.0757  210 TRP A CH2   
1716 N N     . VAL A 211 ? 0.4468 0.5697 0.6985 0.1014  -0.0031 0.0736  211 VAL A N     
1717 C CA    . VAL A 211 ? 0.4896 0.6021 0.7463 0.1106  -0.0001 0.0729  211 VAL A CA    
1718 C C     . VAL A 211 ? 0.4781 0.5822 0.7269 0.1080  -0.0192 0.0790  211 VAL A C     
1719 O O     . VAL A 211 ? 0.4643 0.5576 0.6815 0.1004  -0.0254 0.0778  211 VAL A O     
1720 C CB    . VAL A 211 ? 0.5098 0.6060 0.7380 0.1130  0.0143  0.0637  211 VAL A CB    
1721 C CG1   . VAL A 211 ? 0.4788 0.5619 0.7115 0.1219  0.0169  0.0624  211 VAL A CG1   
1722 C CG2   . VAL A 211 ? 0.4619 0.5633 0.6913 0.1146  0.0330  0.0583  211 VAL A CG2   
1723 N N     . LEU A 212 ? 0.4343 0.5429 0.7121 0.1141  -0.0283 0.0862  212 LEU A N     
1724 C CA    . LEU A 212 ? 0.5022 0.6001 0.7715 0.1124  -0.0468 0.0934  212 LEU A CA    
1725 C C     . LEU A 212 ? 0.5268 0.6055 0.7839 0.1188  -0.0409 0.0906  212 LEU A C     
1726 O O     . LEU A 212 ? 0.5348 0.6134 0.8141 0.1293  -0.0305 0.0885  212 LEU A O     
1727 C CB    . LEU A 212 ? 0.5006 0.6109 0.8070 0.1159  -0.0623 0.1036  212 LEU A CB    
1728 C CG    . LEU A 212 ? 0.5805 0.7022 0.8889 0.1062  -0.0788 0.1090  212 LEU A CG    
1729 C CD1   . LEU A 212 ? 0.5255 0.6623 0.8396 0.1015  -0.0671 0.1032  212 LEU A CD1   
1730 C CD2   . LEU A 212 ? 0.5831 0.7156 0.9302 0.1104  -0.0968 0.1195  212 LEU A CD2   
1731 N N     . VAL A 213 ? 0.5246 0.5866 0.7473 0.1122  -0.0465 0.0901  213 VAL A N     
1732 C CA    . VAL A 213 ? 0.5336 0.5758 0.7407 0.1158  -0.0410 0.0866  213 VAL A CA    
1733 C C     . VAL A 213 ? 0.5858 0.6154 0.7914 0.1160  -0.0571 0.0965  213 VAL A C     
1734 O O     . VAL A 213 ? 0.5290 0.5555 0.7170 0.1073  -0.0705 0.1027  213 VAL A O     
1735 C CB    . VAL A 213 ? 0.5755 0.6078 0.7469 0.1076  -0.0338 0.0785  213 VAL A CB    
1736 C CG1   . VAL A 213 ? 0.6553 0.6666 0.8116 0.1096  -0.0307 0.0755  213 VAL A CG1   
1737 C CG2   . VAL A 213 ? 0.5274 0.5696 0.6988 0.1081  -0.0189 0.0696  213 VAL A CG2   
1738 N N     . ALA A 214 ? 0.5675 0.5879 0.7901 0.1260  -0.0552 0.0982  214 ALA A N     
1739 C CA    . ALA A 214 ? 0.5154 0.5197 0.7355 0.1273  -0.0695 0.1080  214 ALA A CA    
1740 C C     . ALA A 214 ? 0.6145 0.5977 0.7968 0.1196  -0.0671 0.1050  214 ALA A C     
1741 O O     . ALA A 214 ? 0.6817 0.6531 0.8581 0.1229  -0.0552 0.0972  214 ALA A O     
1742 C CB    . ALA A 214 ? 0.6335 0.6341 0.8865 0.1412  -0.0664 0.1099  214 ALA A CB    
1743 N N     . GLY A 215 ? 0.5813 0.5591 0.7376 0.1088  -0.0781 0.1106  215 GLY A N     
1744 C CA    . GLY A 215 ? 0.5851 0.5474 0.7072 0.0994  -0.0734 0.1068  215 GLY A CA    
1745 C C     . GLY A 215 ? 0.6760 0.6149 0.7820 0.0969  -0.0813 0.1151  215 GLY A C     
1746 O O     . GLY A 215 ? 0.6507 0.5765 0.7307 0.0886  -0.0762 0.1122  215 GLY A O     
1747 N N     . ASN A 216 ? 0.6132 0.5460 0.7356 0.1039  -0.0934 0.1258  216 ASN A N     
1748 C CA    . ASN A 216 ? 0.6272 0.5352 0.7323 0.1012  -0.1020 0.1356  216 ASN A CA    
1749 C C     . ASN A 216 ? 0.6490 0.5396 0.7469 0.1021  -0.0891 0.1287  216 ASN A C     
1750 O O     . ASN A 216 ? 0.6781 0.5494 0.7503 0.0939  -0.0894 0.1321  216 ASN A O     
1751 C CB    . ASN A 216 ? 0.6145 0.5198 0.7434 0.1104  -0.1182 0.1485  216 ASN A CB    
1752 C CG    . ASN A 216 ? 0.7918 0.7072 0.9183 0.1057  -0.1363 0.1581  216 ASN A CG    
1753 O OD1   . ASN A 216 ? 0.7064 0.6192 0.8010 0.0936  -0.1391 0.1585  216 ASN A OD1   
1754 N ND2   . ASN A 216 ? 0.8584 0.7853 1.0200 0.1152  -0.1487 0.1653  216 ASN A ND2   
1755 N N     . ASP A 217 ? 0.5966 0.4925 0.7157 0.1113  -0.0772 0.1186  217 ASP A N     
1756 C CA    . ASP A 217 ? 0.6838 0.5644 0.7951 0.1112  -0.0647 0.1092  217 ASP A CA    
1757 C C     . ASP A 217 ? 0.6420 0.5342 0.7408 0.1048  -0.0527 0.0960  217 ASP A C     
1758 O O     . ASP A 217 ? 0.6363 0.5456 0.7486 0.1098  -0.0459 0.0887  217 ASP A O     
1759 C CB    . ASP A 217 ? 0.7082 0.5833 0.8465 0.1250  -0.0592 0.1056  217 ASP A CB    
1760 C CG    . ASP A 217 ? 0.8491 0.7072 0.9779 0.1245  -0.0467 0.0940  217 ASP A CG    
1761 O OD1   . ASP A 217 ? 0.9893 0.8286 1.0988 0.1167  -0.0485 0.0963  217 ASP A OD1   
1762 O OD2   . ASP A 217 ? 0.9402 0.8028 1.0798 0.1314  -0.0349 0.0824  217 ASP A OD2   
1763 N N     . LYS A 218 ? 0.6411 0.5237 0.7154 0.0937  -0.0498 0.0935  218 LYS A N     
1764 C CA    . LYS A 218 ? 0.6290 0.5227 0.6927 0.0873  -0.0408 0.0824  218 LYS A CA    
1765 C C     . LYS A 218 ? 0.6581 0.5520 0.7304 0.0937  -0.0302 0.0697  218 LYS A C     
1766 O O     . LYS A 218 ? 0.6205 0.5291 0.6929 0.0936  -0.0242 0.0618  218 LYS A O     
1767 C CB    . LYS A 218 ? 0.6755 0.5580 0.7167 0.0748  -0.0393 0.0825  218 LYS A CB    
1768 C CG    . LYS A 218 ? 0.6816 0.5652 0.7069 0.0664  -0.0464 0.0923  218 LYS A CG    
1769 C CD    . LYS A 218 ? 0.7958 0.6692 0.8010 0.0540  -0.0409 0.0911  218 LYS A CD    
1770 C CE    . LYS A 218 ? 0.8260 0.6975 0.8110 0.0453  -0.0457 0.1000  218 LYS A CE    
1771 N NZ    . LYS A 218 ? 0.8608 0.7248 0.8288 0.0333  -0.0369 0.0976  218 LYS A NZ    
1772 N N     . LYS A 219 ? 0.6096 0.4851 0.6869 0.0989  -0.0276 0.0674  219 LYS A N     
1773 C CA    . LYS A 219 ? 0.6695 0.5408 0.7497 0.1042  -0.0175 0.0543  219 LYS A CA    
1774 C C     . LYS A 219 ? 0.6188 0.5053 0.7163 0.1146  -0.0120 0.0511  219 LYS A C     
1775 O O     . LYS A 219 ? 0.6559 0.5500 0.7483 0.1150  -0.0036 0.0411  219 LYS A O     
1776 C CB    . LYS A 219 ? 0.6984 0.5445 0.7808 0.1078  -0.0163 0.0528  219 LYS A CB    
1777 C CG    . LYS A 219 ? 0.7486 0.5786 0.8148 0.0963  -0.0193 0.0544  219 LYS A CG    
1778 C CD    . LYS A 219 ? 0.9264 0.7299 0.9958 0.0996  -0.0178 0.0523  219 LYS A CD    
1779 C CE    . LYS A 219 ? 0.9783 0.7651 1.0354 0.0879  -0.0212 0.0573  219 LYS A CE    
1780 N NZ    . LYS A 219 ? 1.0711 0.8652 1.1151 0.0756  -0.0186 0.0503  219 LYS A NZ    
1781 N N     . TYR A 220 ? 0.5568 0.4477 0.6755 0.1228  -0.0168 0.0603  220 TYR A N     
1782 C CA    . TYR A 220 ? 0.6661 0.5741 0.8068 0.1323  -0.0111 0.0587  220 TYR A CA    
1783 C C     . TYR A 220 ? 0.5924 0.5227 0.7276 0.1262  -0.0109 0.0580  220 TYR A C     
1784 O O     . TYR A 220 ? 0.5979 0.5391 0.7391 0.1302  -0.0008 0.0510  220 TYR A O     
1785 C CB    . TYR A 220 ? 0.6391 0.5494 0.8077 0.1411  -0.0194 0.0703  220 TYR A CB    
1786 C CG    . TYR A 220 ? 0.6951 0.6261 0.8932 0.1502  -0.0148 0.0707  220 TYR A CG    
1787 C CD1   . TYR A 220 ? 0.7029 0.6304 0.9246 0.1629  -0.0031 0.0653  220 TYR A CD1   
1788 C CD2   . TYR A 220 ? 0.6480 0.6013 0.8520 0.1459  -0.0213 0.0763  220 TYR A CD2   
1789 C CE1   . TYR A 220 ? 0.6630 0.6104 0.9155 0.1710  0.0030  0.0659  220 TYR A CE1   
1790 C CE2   . TYR A 220 ? 0.6922 0.6650 0.9265 0.1533  -0.0169 0.0771  220 TYR A CE2   
1791 C CZ    . TYR A 220 ? 0.7174 0.6880 0.9770 0.1658  -0.0042 0.0721  220 TYR A CZ    
1792 O OH    . TYR A 220 ? 0.9435 0.9347 1.2367 0.1729  0.0020  0.0730  220 TYR A OH    
1793 N N     . ALA A 221 ? 0.5935 0.5287 0.7159 0.1164  -0.0210 0.0650  221 ALA A N     
1794 C CA    . ALA A 221 ? 0.5708 0.5254 0.6883 0.1104  -0.0213 0.0644  221 ALA A CA    
1795 C C     . ALA A 221 ? 0.5229 0.4786 0.6244 0.1065  -0.0110 0.0526  221 ALA A C     
1796 O O     . ALA A 221 ? 0.5181 0.4879 0.6234 0.1078  -0.0050 0.0487  221 ALA A O     
1797 C CB    . ALA A 221 ? 0.5205 0.4757 0.6235 0.1002  -0.0328 0.0727  221 ALA A CB    
1798 N N     . ARG A 222 ? 0.5074 0.4479 0.5909 0.1011  -0.0100 0.0476  222 ARG A N     
1799 C CA    . ARG A 222 ? 0.5583 0.4980 0.6268 0.0972  -0.0032 0.0369  222 ARG A CA    
1800 C C     . ARG A 222 ? 0.5624 0.5009 0.6354 0.1059  0.0074  0.0286  222 ARG A C     
1801 O O     . ARG A 222 ? 0.5860 0.5338 0.6528 0.1052  0.0130  0.0235  222 ARG A O     
1802 C CB    . ARG A 222 ? 0.5317 0.4542 0.5860 0.0906  -0.0050 0.0333  222 ARG A CB    
1803 C CG    . ARG A 222 ? 0.4883 0.4103 0.5359 0.0810  -0.0122 0.0409  222 ARG A CG    
1804 C CD    . ARG A 222 ? 0.5950 0.4972 0.6362 0.0768  -0.0132 0.0399  222 ARG A CD    
1805 N NE    . ARG A 222 ? 0.6863 0.5855 0.7200 0.0675  -0.0177 0.0478  222 ARG A NE    
1806 C CZ    . ARG A 222 ? 0.7342 0.6158 0.7632 0.0626  -0.0186 0.0503  222 ARG A CZ    
1807 N NH1   . ARG A 222 ? 0.6816 0.5470 0.7137 0.0658  -0.0168 0.0454  222 ARG A NH1   
1808 N NH2   . ARG A 222 ? 0.6616 0.5406 0.6816 0.0538  -0.0205 0.0578  222 ARG A NH2   
1809 N N     . VAL A 223 ? 0.5165 0.4421 0.5994 0.1143  0.0110  0.0273  223 VAL A N     
1810 C CA    . VAL A 223 ? 0.5250 0.4464 0.6106 0.1229  0.0236  0.0185  223 VAL A CA    
1811 C C     . VAL A 223 ? 0.5355 0.4774 0.6372 0.1277  0.0294  0.0215  223 VAL A C     
1812 O O     . VAL A 223 ? 0.5717 0.5164 0.6652 0.1291  0.0399  0.0144  223 VAL A O     
1813 C CB    . VAL A 223 ? 0.6060 0.5092 0.7028 0.1317  0.0270  0.0170  223 VAL A CB    
1814 C CG1   . VAL A 223 ? 0.6144 0.5169 0.7215 0.1426  0.0421  0.0100  223 VAL A CG1   
1815 C CG2   . VAL A 223 ? 0.5912 0.4711 0.6681 0.1265  0.0248  0.0099  223 VAL A CG2   
1816 N N     . GLN A 224 ? 0.5282 0.4841 0.6521 0.1294  0.0222  0.0323  224 GLN A N     
1817 C CA    . GLN A 224 ? 0.4729 0.4490 0.6173 0.1336  0.0270  0.0355  224 GLN A CA    
1818 C C     . GLN A 224 ? 0.5226 0.5113 0.6522 0.1255  0.0278  0.0338  224 GLN A C     
1819 O O     . GLN A 224 ? 0.5176 0.5158 0.6522 0.1282  0.0384  0.0308  224 GLN A O     
1820 C CB    . GLN A 224 ? 0.5438 0.5314 0.7152 0.1359  0.0155  0.0478  224 GLN A CB    
1821 C CG    . GLN A 224 ? 0.6785 0.6886 0.8767 0.1396  0.0191  0.0515  224 GLN A CG    
1822 C CD    . GLN A 224 ? 0.8013 0.8233 1.0254 0.1404  0.0038  0.0641  224 GLN A CD    
1823 O OE1   . GLN A 224 ? 0.7730 0.7852 0.9910 0.1379  -0.0098 0.0707  224 GLN A OE1   
1824 N NE2   . GLN A 224 ? 0.6599 0.7024 0.9127 0.1433  0.0055  0.0677  224 GLN A NE2   
1825 N N     . VAL A 225 ? 0.4283 0.4168 0.5407 0.1156  0.0176  0.0361  225 VAL A N     
1826 C CA    . VAL A 225 ? 0.4664 0.4653 0.5657 0.1083  0.0181  0.0343  225 VAL A CA    
1827 C C     . VAL A 225 ? 0.4900 0.4813 0.5717 0.1093  0.0290  0.0242  225 VAL A C     
1828 O O     . VAL A 225 ? 0.5205 0.5210 0.6004 0.1090  0.0357  0.0229  225 VAL A O     
1829 C CB    . VAL A 225 ? 0.5308 0.5282 0.6153 0.0982  0.0072  0.0371  225 VAL A CB    
1830 C CG1   . VAL A 225 ? 0.4457 0.4495 0.5156 0.0916  0.0090  0.0332  225 VAL A CG1   
1831 C CG2   . VAL A 225 ? 0.4506 0.4565 0.5473 0.0959  -0.0033 0.0473  225 VAL A CG2   
1832 N N     . LEU A 226 ? 0.5016 0.4740 0.5687 0.1102  0.0307  0.0173  226 LEU A N     
1833 C CA    . LEU A 226 ? 0.5305 0.4922 0.5765 0.1107  0.0392  0.0074  226 LEU A CA    
1834 C C     . LEU A 226 ? 0.5197 0.4826 0.5731 0.1194  0.0543  0.0044  226 LEU A C     
1835 O O     . LEU A 226 ? 0.5190 0.4842 0.5597 0.1185  0.0620  0.0012  226 LEU A O     
1836 C CB    . LEU A 226 ? 0.5464 0.4862 0.5765 0.1095  0.0367  0.0001  226 LEU A CB    
1837 C CG    . LEU A 226 ? 0.5533 0.4901 0.5683 0.0993  0.0259  -0.0012 226 LEU A CG    
1838 C CD1   . LEU A 226 ? 0.5625 0.4810 0.5735 0.0976  0.0213  -0.0047 226 LEU A CD1   
1839 C CD2   . LEU A 226 ? 0.4906 0.4249 0.4840 0.0959  0.0275  -0.0079 226 LEU A CD2   
1840 N N     . GLN A 227 ? 0.4795 0.4404 0.5545 0.1280  0.0593  0.0060  227 GLN A N     
1841 C CA    . GLN A 227 ? 0.5550 0.5171 0.6416 0.1370  0.0762  0.0027  227 GLN A CA    
1842 C C     . GLN A 227 ? 0.4982 0.4824 0.5995 0.1359  0.0806  0.0087  227 GLN A C     
1843 O O     . GLN A 227 ? 0.5443 0.5282 0.6380 0.1379  0.0951  0.0044  227 GLN A O     
1844 C CB    . GLN A 227 ? 0.5132 0.4721 0.6282 0.1468  0.0793  0.0049  227 GLN A CB    
1845 C CG    . GLN A 227 ? 0.5696 0.5030 0.6710 0.1500  0.0807  -0.0031 227 GLN A CG    
1846 C CD    . GLN A 227 ? 0.7457 0.6758 0.8783 0.1602  0.0824  0.0004  227 GLN A CD    
1847 O OE1   . GLN A 227 ? 0.7337 0.6815 0.8980 0.1634  0.0768  0.0108  227 GLN A OE1   
1848 N NE2   . GLN A 227 ? 0.7118 0.6182 0.8359 0.1654  0.0892  -0.0083 227 GLN A NE2   
1849 N N     . GLU A 228 ? 0.4944 0.4964 0.6154 0.1323  0.0684  0.0185  228 GLU A N     
1850 C CA    . GLU A 228 ? 0.5110 0.5339 0.6497 0.1309  0.0713  0.0242  228 GLU A CA    
1851 C C     . GLU A 228 ? 0.5280 0.5518 0.6407 0.1231  0.0729  0.0217  228 GLU A C     
1852 O O     . GLU A 228 ? 0.5306 0.5622 0.6469 0.1237  0.0843  0.0218  228 GLU A O     
1853 C CB    . GLU A 228 ? 0.4567 0.4954 0.6197 0.1282  0.0557  0.0346  228 GLU A CB    
1854 C CG    . GLU A 228 ? 0.5386 0.5808 0.7354 0.1370  0.0541  0.0396  228 GLU A CG    
1855 C CD    . GLU A 228 ? 0.6475 0.7058 0.8788 0.1438  0.0664  0.0416  228 GLU A CD    
1856 O OE1   . GLU A 228 ? 0.7559 0.8222 0.9834 0.1411  0.0771  0.0396  228 GLU A OE1   
1857 O OE2   . GLU A 228 ? 0.7557 0.8186 1.0199 0.1520  0.0655  0.0458  228 GLU A OE2   
1858 N N     . THR A 229 ? 0.5099 0.5255 0.5979 0.1159  0.0620  0.0198  229 THR A N     
1859 C CA    . THR A 229 ? 0.4981 0.5123 0.5619 0.1095  0.0626  0.0172  229 THR A CA    
1860 C C     . THR A 229 ? 0.5390 0.5397 0.5825 0.1132  0.0776  0.0098  229 THR A C     
1861 O O     . THR A 229 ? 0.5097 0.5148 0.5467 0.1117  0.0856  0.0107  229 THR A O     
1862 C CB    . THR A 229 ? 0.4869 0.4933 0.5315 0.1023  0.0493  0.0155  229 THR A CB    
1863 O OG1   . THR A 229 ? 0.4879 0.5048 0.5476 0.0984  0.0376  0.0223  229 THR A OG1   
1864 C CG2   . THR A 229 ? 0.4899 0.4956 0.5134 0.0965  0.0483  0.0136  229 THR A CG2   
1865 N N     . LEU A 230 ? 0.5278 0.5101 0.5592 0.1178  0.0820  0.0024  230 LEU A N     
1866 C CA    . LEU A 230 ? 0.5506 0.5159 0.5565 0.1208  0.0962  -0.0059 230 LEU A CA    
1867 C C     . LEU A 230 ? 0.6136 0.5866 0.6361 0.1271  0.1154  -0.0044 230 LEU A C     
1868 O O     . LEU A 230 ? 0.5589 0.5256 0.5610 0.1264  0.1276  -0.0070 230 LEU A O     
1869 C CB    . LEU A 230 ? 0.5546 0.4973 0.5461 0.1243  0.0968  -0.0148 230 LEU A CB    
1870 C CG    . LEU A 230 ? 0.6475 0.5795 0.6186 0.1170  0.0801  -0.0179 230 LEU A CG    
1871 C CD1   . LEU A 230 ? 0.6157 0.5280 0.5825 0.1204  0.0796  -0.0252 230 LEU A CD1   
1872 C CD2   . LEU A 230 ? 0.5382 0.4599 0.4745 0.1113  0.0783  -0.0222 230 LEU A CD2   
1873 N N     . ALA A 231 ? 0.6101 0.5967 0.6707 0.1331  0.1183  0.0003  231 ALA A N     
1874 C CA    . ALA A 231 ? 0.6168 0.6128 0.7009 0.1396  0.1373  0.0016  231 ALA A CA    
1875 C C     . ALA A 231 ? 0.6063 0.6194 0.6964 0.1340  0.1398  0.0083  231 ALA A C     
1876 O O     . ALA A 231 ? 0.6050 0.6163 0.6898 0.1355  0.1583  0.0068  231 ALA A O     
1877 C CB    . ALA A 231 ? 0.5038 0.5123 0.6324 0.1471  0.1361  0.0063  231 ALA A CB    
1878 N N     . HIS A 232 ? 0.5468 0.5752 0.6473 0.1272  0.1223  0.0158  232 HIS A N     
1879 C CA    A HIS A 232 ? 0.5513 0.5946 0.6584 0.1216  0.1241  0.0218  232 HIS A CA    
1880 C CA    B HIS A 232 ? 0.5505 0.5939 0.6574 0.1214  0.1238  0.0219  232 HIS A CA    
1881 C C     . HIS A 232 ? 0.6084 0.6377 0.6748 0.1162  0.1276  0.0185  232 HIS A C     
1882 O O     . HIS A 232 ? 0.6386 0.6721 0.7036 0.1141  0.1390  0.0212  232 HIS A O     
1883 C CB    A HIS A 232 ? 0.5432 0.6040 0.6710 0.1159  0.1049  0.0296  232 HIS A CB    
1884 C CB    B HIS A 232 ? 0.5438 0.6039 0.6687 0.1152  0.1042  0.0294  232 HIS A CB    
1885 C CG    A HIS A 232 ? 0.5802 0.6570 0.7506 0.1206  0.1016  0.0350  232 HIS A CG    
1886 C CG    B HIS A 232 ? 0.5418 0.6183 0.6808 0.1098  0.1057  0.0357  232 HIS A CG    
1887 N ND1   A HIS A 232 ? 0.5114 0.5835 0.6917 0.1257  0.0937  0.0347  232 HIS A ND1   
1888 N ND1   B HIS A 232 ? 0.5341 0.6106 0.6543 0.1015  0.0973  0.0375  232 HIS A ND1   
1889 C CD2   A HIS A 232 ? 0.5665 0.6635 0.7736 0.1211  0.1044  0.0414  232 HIS A CD2   
1890 C CD2   B HIS A 232 ? 0.5312 0.6245 0.7038 0.1113  0.1148  0.0406  232 HIS A CD2   
1891 C CE1   A HIS A 232 ? 0.5957 0.6841 0.8160 0.1293  0.0905  0.0411  232 HIS A CE1   
1892 C CE1   B HIS A 232 ? 0.4293 0.5201 0.5683 0.0980  0.1009  0.0430  232 HIS A CE1   
1893 N NE2   A HIS A 232 ? 0.5386 0.6431 0.7770 0.1265  0.0965  0.0450  232 HIS A NE2   
1894 N NE2   B HIS A 232 ? 0.5508 0.6526 0.7221 0.1033  0.1114  0.0450  232 HIS A NE2   
1895 N N     . ILE A 233 ? 0.5915 0.6036 0.6256 0.1137  0.1178  0.0131  233 ILE A N     
1896 C CA    . ILE A 233 ? 0.6056 0.6023 0.6006 0.1094  0.1197  0.0100  233 ILE A CA    
1897 C C     . ILE A 233 ? 0.6632 0.6456 0.6406 0.1140  0.1419  0.0052  233 ILE A C     
1898 O O     . ILE A 233 ? 0.6327 0.6111 0.5922 0.1109  0.1506  0.0074  233 ILE A O     
1899 C CB    . ILE A 233 ? 0.5627 0.5438 0.5306 0.1062  0.1043  0.0046  233 ILE A CB    
1900 C CG1   . ILE A 233 ? 0.5301 0.5247 0.5106 0.1000  0.0855  0.0098  233 ILE A CG1   
1901 C CG2   . ILE A 233 ? 0.5670 0.5278 0.4925 0.1034  0.1067  0.0002  233 ILE A CG2   
1902 C CD1   . ILE A 233 ? 0.5142 0.4969 0.4768 0.0966  0.0711  0.0051  233 ILE A CD1   
1903 N N     . GLU A 234 ? 0.6081 0.5811 0.5897 0.1214  0.1524  -0.0012 234 GLU A N     
1904 C CA    . GLU A 234 ? 0.7083 0.6653 0.6713 0.1260  0.1761  -0.0070 234 GLU A CA    
1905 C C     . GLU A 234 ? 0.7047 0.6783 0.6944 0.1273  0.1943  -0.0006 234 GLU A C     
1906 O O     . GLU A 234 ? 0.7538 0.7165 0.7193 0.1260  0.2111  -0.0014 234 GLU A O     
1907 C CB    . GLU A 234 ? 0.7663 0.7103 0.7333 0.1343  0.1844  -0.0157 234 GLU A CB    
1908 C CG    . GLU A 234 ? 0.8791 0.8013 0.8139 0.1323  0.1700  -0.0236 234 GLU A CG    
1909 C CD    . GLU A 234 ? 1.1447 1.0526 1.0848 0.1404  0.1776  -0.0323 234 GLU A CD    
1910 O OE1   . GLU A 234 ? 1.1086 1.0067 1.0476 0.1472  0.2008  -0.0378 234 GLU A OE1   
1911 O OE2   . GLU A 234 ? 0.9882 0.8935 0.9338 0.1397  0.1612  -0.0336 234 GLU A OE2   
1912 N N     . ARG A 235 ? 0.6507 0.6500 0.6902 0.1295  0.1910  0.0061  235 ARG A N     
1913 C CA    . ARG A 235 ? 0.6830 0.7010 0.7547 0.1299  0.2065  0.0126  235 ARG A CA    
1914 C C     . ARG A 235 ? 0.6856 0.7063 0.7401 0.1209  0.2044  0.0187  235 ARG A C     
1915 O O     . ARG A 235 ? 0.6809 0.6987 0.7292 0.1200  0.2244  0.0203  235 ARG A O     
1916 C CB    . ARG A 235 ? 0.7116 0.7568 0.8390 0.1323  0.1970  0.0193  235 ARG A CB    
1917 C CG    . ARG A 235 ? 0.8153 0.8606 0.9699 0.1425  0.2016  0.0155  235 ARG A CG    
1918 C CD    . ARG A 235 ? 0.9490 1.0223 1.1602 0.1443  0.1915  0.0241  235 ARG A CD    
1919 N NE    . ARG A 235 ? 1.1592 1.2319 1.3943 0.1529  0.1861  0.0225  235 ARG A NE    
1920 C CZ    . ARG A 235 ? 1.0086 1.0836 1.2483 0.1515  0.1625  0.0258  235 ARG A CZ    
1921 N NH1   . ARG A 235 ? 0.9176 0.9958 1.1398 0.1421  0.1431  0.0298  235 ARG A NH1   
1922 N NH2   . ARG A 235 ? 1.1050 1.1778 1.3672 0.1599  0.1593  0.0252  235 ARG A NH2   
1923 N N     . GLU A 236 ? 0.6480 0.6735 0.6953 0.1142  0.1813  0.0224  236 GLU A N     
1924 C CA    . GLU A 236 ? 0.7072 0.7351 0.7412 0.1061  0.1778  0.0285  236 GLU A CA    
1925 C C     . GLU A 236 ? 0.7338 0.7356 0.7164 0.1042  0.1866  0.0250  236 GLU A C     
1926 O O     . GLU A 236 ? 0.6776 0.6773 0.6495 0.0999  0.1962  0.0301  236 GLU A O     
1927 C CB    . GLU A 236 ? 0.5888 0.6255 0.6264 0.1003  0.1522  0.0319  236 GLU A CB    
1928 C CG    . GLU A 236 ? 0.5874 0.6485 0.6710 0.1001  0.1426  0.0369  236 GLU A CG    
1929 C CD    . GLU A 236 ? 0.7739 0.8531 0.8889 0.0975  0.1523  0.0440  236 GLU A CD    
1930 O OE1   . GLU A 236 ? 0.7791 0.8530 0.8777 0.0929  0.1607  0.0467  236 GLU A OE1   
1931 O OE2   . GLU A 236 ? 0.7681 0.8659 0.9247 0.0996  0.1507  0.0472  236 GLU A OE2   
1932 N N     . ALA A 237 ? 0.6616 0.6420 0.6110 0.1068  0.1829  0.0167  237 ALA A N     
1933 C CA    . ALA A 237 ? 0.7777 0.7303 0.6751 0.1052  0.1905  0.0125  237 ALA A CA    
1934 C C     . ALA A 237 ? 0.7933 0.7387 0.6856 0.1081  0.2201  0.0122  237 ALA A C     
1935 O O     . ALA A 237 ? 0.8059 0.7393 0.6693 0.1038  0.2291  0.0159  237 ALA A O     
1936 C CB    . ALA A 237 ? 0.7657 0.6969 0.6334 0.1078  0.1821  0.0023  237 ALA A CB    
1937 N N     . LEU A 238 ? 0.8460 0.7983 0.7676 0.1155  0.2361  0.0082  238 LEU A N     
1938 C CA    . LEU A 238 ? 0.8281 0.7760 0.7524 0.1190  0.2673  0.0073  238 LEU A CA    
1939 C C     . LEU A 238 ? 0.7680 0.7343 0.7165 0.1138  0.2758  0.0182  238 LEU A C     
1940 O O     . LEU A 238 ? 0.8185 0.7713 0.7410 0.1109  0.2951  0.0202  238 LEU A O     
1941 C CB    . LEU A 238 ? 0.8347 0.7919 0.7983 0.1286  0.2805  0.0021  238 LEU A CB    
1942 C CG    . LEU A 238 ? 1.0080 0.9366 0.9388 0.1351  0.2957  -0.0105 238 LEU A CG    
1943 C CD1   . LEU A 238 ? 1.1481 1.0539 1.0328 0.1322  0.2735  -0.0171 238 LEU A CD1   
1944 C CD2   . LEU A 238 ? 0.9591 0.9004 0.9380 0.1452  0.3053  -0.0142 238 LEU A CD2   
1945 N N     . LYS A 239 ? 0.7225 0.7182 0.7191 0.1119  0.2614  0.0253  239 LYS A N     
1946 C CA    . LYS A 239 ? 0.7638 0.7771 0.7852 0.1057  0.2660  0.0354  239 LYS A CA    
1947 C C     . LYS A 239 ? 0.7951 0.7910 0.7713 0.0978  0.2629  0.0398  239 LYS A C     
1948 O O     . LYS A 239 ? 0.7992 0.7985 0.7805 0.0931  0.2768  0.0469  239 LYS A O     
1949 C CB    . LYS A 239 ? 0.7360 0.7780 0.8042 0.1032  0.2441  0.0413  239 LYS A CB    
1950 C CG    . LYS A 239 ? 0.8508 0.9159 0.9757 0.1094  0.2480  0.0414  239 LYS A CG    
1951 C CD    . LYS A 239 ? 0.8909 0.9805 1.0530 0.1051  0.2237  0.0477  239 LYS A CD    
1952 C CE    . LYS A 239 ? 1.0094 1.1166 1.2178 0.1120  0.2178  0.0471  239 LYS A CE    
1953 N NZ    . LYS A 239 ? 0.8962 1.0218 1.1303 0.1072  0.1915  0.0526  239 LYS A NZ    
1954 N N     . ARG A 240 ? 0.8469 0.8248 0.7815 0.0960  0.2439  0.0364  240 ARG A N     
1955 C CA    . ARG A 240 ? 0.8008 0.7609 0.6928 0.0892  0.2383  0.0411  240 ARG A CA    
1956 C C     . ARG A 240 ? 0.8722 0.7992 0.7079 0.0899  0.2551  0.0369  240 ARG A C     
1957 O O     . ARG A 240 ? 0.8762 0.7838 0.6695 0.0848  0.2479  0.0405  240 ARG A O     
1958 C CB    . ARG A 240 ? 0.7736 0.7329 0.6539 0.0863  0.2075  0.0408  240 ARG A CB    
1959 C CG    . ARG A 240 ? 0.6806 0.6664 0.6028 0.0824  0.1915  0.0473  240 ARG A CG    
1960 C CD    . ARG A 240 ? 0.7404 0.7252 0.6536 0.0806  0.1644  0.0454  240 ARG A CD    
1961 N NE    . ARG A 240 ? 0.7571 0.7610 0.6993 0.0757  0.1507  0.0516  240 ARG A NE    
1962 C CZ    . ARG A 240 ? 0.6753 0.7016 0.6589 0.0761  0.1452  0.0521  240 ARG A CZ    
1963 N NH1   . ARG A 240 ? 0.7416 0.7759 0.7463 0.0817  0.1512  0.0480  240 ARG A NH1   
1964 N NH2   . ARG A 240 ? 0.6192 0.6588 0.6225 0.0708  0.1329  0.0570  240 ARG A NH2   
1965 N N     . GLY A 241 ? 0.8151 0.7337 0.6482 0.0961  0.2772  0.0293  241 GLY A N     
1966 C CA    . GLY A 241 ? 0.9278 0.8121 0.7036 0.0964  0.2949  0.0242  241 GLY A CA    
1967 C C     . GLY A 241 ? 1.0527 0.9110 0.7807 0.0974  0.2778  0.0151  241 GLY A C     
1968 O O     . GLY A 241 ? 1.0734 0.8992 0.7452 0.0963  0.2878  0.0108  241 GLY A O     
1969 N N     . LEU A 242 ? 0.9098 0.7801 0.6572 0.0987  0.2524  0.0119  242 LEU A N     
1970 C CA    . LEU A 242 ? 1.0397 0.8888 0.7502 0.0990  0.2339  0.0033  242 LEU A CA    
1971 C C     . LEU A 242 ? 1.0212 0.8702 0.7485 0.1066  0.2406  -0.0076 242 LEU A C     
1972 O O     . LEU A 242 ? 1.0766 0.9485 0.8535 0.1117  0.2511  -0.0068 242 LEU A O     
1973 C CB    . LEU A 242 ? 0.8468 0.7085 0.5683 0.0946  0.2012  0.0076  242 LEU A CB    
1974 C CG    . LEU A 242 ? 0.9589 0.8253 0.6753 0.0879  0.1914  0.0190  242 LEU A CG    
1975 C CD1   . LEU A 242 ? 0.8532 0.7367 0.5931 0.0852  0.1628  0.0218  242 LEU A CD1   
1976 C CD2   . LEU A 242 ? 0.9239 0.7574 0.5783 0.0838  0.1921  0.0202  242 LEU A CD2   
1977 N N     . HIS A 243 ? 1.1011 0.9233 0.7873 0.1072  0.2330  -0.0178 243 HIS A N     
1978 C CA    . HIS A 243 ? 1.1071 0.9246 0.8043 0.1139  0.2361  -0.0289 243 HIS A CA    
1979 C C     . HIS A 243 ? 1.0195 0.8329 0.7086 0.1111  0.2057  -0.0328 243 HIS A C     
1980 O O     . HIS A 243 ? 0.9845 0.7761 0.6282 0.1056  0.1911  -0.0350 243 HIS A O     
1981 C CB    . HIS A 243 ? 1.1251 0.9097 0.7795 0.1174  0.2607  -0.0398 243 HIS A CB    
1982 C CG    . HIS A 243 ? 1.3121 1.1007 0.9787 0.1208  0.2946  -0.0370 243 HIS A CG    
1983 N ND1   . HIS A 243 ? 1.3613 1.1460 1.0070 0.1153  0.3054  -0.0284 243 HIS A ND1   
1984 C CD2   . HIS A 243 ? 1.3445 1.1411 1.0450 0.1290  0.3207  -0.0413 243 HIS A CD2   
1985 C CE1   . HIS A 243 ? 1.3604 1.1508 1.0265 0.1194  0.3377  -0.0277 243 HIS A CE1   
1986 N NE2   . HIS A 243 ? 1.3479 1.1463 1.0488 0.1280  0.3475  -0.0356 243 HIS A NE2   
1987 N N     . LEU A 244 ? 0.9884 0.8226 0.7222 0.1145  0.1959  -0.0331 244 LEU A N     
1988 C CA    . LEU A 244 ? 1.0219 0.8529 0.7530 0.1120  0.1701  -0.0372 244 LEU A CA    
1989 C C     . LEU A 244 ? 1.0288 0.8270 0.7207 0.1137  0.1729  -0.0509 244 LEU A C     
1990 O O     . LEU A 244 ? 1.0913 0.8821 0.7908 0.1208  0.1914  -0.0582 244 LEU A O     
1991 C CB    . LEU A 244 ? 0.8091 0.6675 0.5950 0.1152  0.1622  -0.0337 244 LEU A CB    
1992 C CG    . LEU A 244 ? 0.9014 0.7585 0.6908 0.1125  0.1383  -0.0371 244 LEU A CG    
1993 C CD1   . LEU A 244 ? 0.9267 0.7849 0.6996 0.1042  0.1167  -0.0326 244 LEU A CD1   
1994 C CD2   . LEU A 244 ? 0.9066 0.7882 0.7462 0.1157  0.1333  -0.0325 244 LEU A CD2   
1995 N N     . THR A 245 ? 1.0114 0.7892 0.6622 0.1074  0.1543  -0.0545 245 THR A N     
1996 C CA    . THR A 245 ? 1.0714 0.8162 0.6816 0.1072  0.1521  -0.0679 245 THR A CA    
1997 C C     . THR A 245 ? 1.0520 0.7968 0.6636 0.1015  0.1216  -0.0698 245 THR A C     
1998 O O     . THR A 245 ? 0.9510 0.7197 0.5907 0.0978  0.1045  -0.0606 245 THR A O     
1999 C CB    . THR A 245 ? 1.1123 0.8245 0.6600 0.1040  0.1609  -0.0719 245 THR A CB    
2000 O OG1   . THR A 245 ? 1.1561 0.8663 0.6811 0.0960  0.1375  -0.0651 245 THR A OG1   
2001 C CG2   . THR A 245 ? 1.1467 0.8625 0.6961 0.1081  0.1915  -0.0674 245 THR A CG2   
2002 N N     . ASN A 246 ? 1.0098 0.7270 0.5915 0.1004  0.1158  -0.0821 246 ASN A N     
2003 C CA    . ASN A 246 ? 1.0726 0.7867 0.6532 0.0939  0.0872  -0.0848 246 ASN A CA    
2004 C C     . ASN A 246 ? 1.1019 0.8060 0.6466 0.0861  0.0687  -0.0810 246 ASN A C     
2005 O O     . ASN A 246 ? 1.0473 0.7198 0.5388 0.0836  0.0697  -0.0877 246 ASN A O     
2006 C CB    . ASN A 246 ? 1.0886 0.7750 0.6495 0.0946  0.0865  -0.0996 246 ASN A CB    
2007 C CG    . ASN A 246 ? 1.1572 0.8451 0.7297 0.0880  0.0586  -0.1019 246 ASN A CG    
2008 O OD1   . ASN A 246 ? 1.0946 0.7846 0.6571 0.0806  0.0367  -0.0979 246 ASN A OD1   
2009 N ND2   . ASN A 246 ? 1.0831 0.7700 0.6793 0.0907  0.0596  -0.1080 246 ASN A ND2   
2010 N N     . VAL A 247 ? 1.0471 0.7765 0.6200 0.0823  0.0517  -0.0702 247 VAL A N     
2011 C CA    . VAL A 247 ? 1.0243 0.7475 0.5721 0.0754  0.0312  -0.0652 247 VAL A CA    
2012 C C     . VAL A 247 ? 1.0335 0.7559 0.5889 0.0693  0.0026  -0.0688 247 VAL A C     
2013 O O     . VAL A 247 ? 1.0720 0.7955 0.6202 0.0639  -0.0181 -0.0635 247 VAL A O     
2014 C CB    . VAL A 247 ? 0.9811 0.7305 0.5534 0.0754  0.0324  -0.0509 247 VAL A CB    
2015 C CG1   . VAL A 247 ? 1.0072 0.7552 0.5700 0.0802  0.0604  -0.0473 247 VAL A CG1   
2016 C CG2   . VAL A 247 ? 0.8302 0.6132 0.4601 0.0764  0.0273  -0.0453 247 VAL A CG2   
2017 N N     . LEU A 248 ? 1.0263 0.7466 0.5983 0.0699  0.0010  -0.0773 248 LEU A N     
2018 C CA    . LEU A 248 ? 1.1108 0.8312 0.6948 0.0634  -0.0242 -0.0809 248 LEU A CA    
2019 C C     . LEU A 248 ? 1.2335 0.9179 0.7695 0.0583  -0.0373 -0.0928 248 LEU A C     
2020 O O     . LEU A 248 ? 1.2725 0.9519 0.7980 0.0513  -0.0622 -0.0920 248 LEU A O     
2021 C CB    . LEU A 248 ? 0.9402 0.6765 0.5683 0.0655  -0.0204 -0.0828 248 LEU A CB    
2022 C CG    . LEU A 248 ? 0.8779 0.6488 0.5533 0.0692  -0.0117 -0.0714 248 LEU A CG    
2023 C CD1   . LEU A 248 ? 0.8047 0.5848 0.5153 0.0712  -0.0082 -0.0736 248 LEU A CD1   
2024 C CD2   . LEU A 248 ? 0.7807 0.5718 0.4745 0.0642  -0.0288 -0.0619 248 LEU A CD2   
2025 N N     . ASP A 249 ? 1.2686 0.9273 0.7760 0.0617  -0.0214 -0.1041 249 ASP A N     
2026 C CA    . ASP A 249 ? 1.4731 1.0942 0.9319 0.0563  -0.0336 -0.1171 249 ASP A CA    
2027 C C     . ASP A 249 ? 1.4504 1.0417 0.8462 0.0559  -0.0267 -0.1193 249 ASP A C     
2028 O O     . ASP A 249 ? 1.4040 1.0016 0.7887 0.0541  -0.0330 -0.1089 249 ASP A O     
2029 C CB    . ASP A 249 ? 1.4261 1.0311 0.8874 0.0593  -0.0220 -0.1303 249 ASP A CB    
2030 C CG    . ASP A 249 ? 1.5928 1.1906 1.0454 0.0690  0.0118  -0.1335 249 ASP A CG    
2031 O OD1   . ASP A 249 ? 1.6975 1.3027 1.1417 0.0728  0.0272  -0.1257 249 ASP A OD1   
2032 O OD2   . ASP A 249 ? 1.6253 1.2097 1.0818 0.0728  0.0233  -0.1438 249 ASP A OD2   
2033 P P     . TMP B .   ? 1.4648 1.3807 1.2717 -0.0380 -0.0146 0.0505  301 TMP A P     
2034 O O1P   . TMP B .   ? 1.0611 0.9838 0.8803 -0.0318 -0.0330 0.0600  301 TMP A O1P   
2035 O O2P   . TMP B .   ? 0.9688 0.9034 0.8086 -0.0323 -0.0031 0.0427  301 TMP A O2P   
2036 O O3P   . TMP B .   ? 1.2659 1.1599 1.0434 -0.0452 -0.0031 0.0523  301 TMP A O3P   
2037 O "O5'" . TMP B .   ? 1.2897 1.1987 1.0759 -0.0446 -0.0207 0.0461  301 TMP A "O5'" 
2038 C "C5'" . TMP B .   ? 1.0383 0.9329 0.8007 -0.0526 -0.0056 0.0374  301 TMP A "C5'" 
2039 C "C4'" . TMP B .   ? 1.0747 0.9644 0.8222 -0.0576 -0.0149 0.0332  301 TMP A "C4'" 
2040 O "O4'" . TMP B .   ? 1.0286 0.9405 0.8116 -0.0514 -0.0170 0.0288  301 TMP A "O4'" 
2041 C "C3'" . TMP B .   ? 1.0167 0.8976 0.7441 -0.0608 -0.0382 0.0418  301 TMP A "C3'" 
2042 O "O3'" . TMP B .   ? 1.0619 0.9228 0.7524 -0.0709 -0.0410 0.0367  301 TMP A "O3'" 
2043 C "C2'" . TMP B .   ? 0.9406 0.8470 0.7078 -0.0530 -0.0519 0.0441  301 TMP A "C2'" 
2044 C "C1'" . TMP B .   ? 0.8735 0.7915 0.6612 -0.0511 -0.0375 0.0334  301 TMP A "C1'" 
2045 N N1    . TMP B .   ? 0.9069 0.8508 0.7377 -0.0416 -0.0402 0.0344  301 TMP A N1    
2046 C C2    . TMP B .   ? 0.7038 0.6573 0.5491 -0.0420 -0.0454 0.0305  301 TMP A C2    
2047 O O2    . TMP B .   ? 0.8023 0.7443 0.6277 -0.0498 -0.0499 0.0262  301 TMP A O2    
2048 N N3    . TMP B .   ? 0.7054 0.6806 0.5875 -0.0336 -0.0449 0.0317  301 TMP A N3    
2049 C C4    . TMP B .   ? 0.6299 0.6168 0.5331 -0.0250 -0.0405 0.0355  301 TMP A C4    
2050 O O4    . TMP B .   ? 0.5862 0.5899 0.5174 -0.0185 -0.0398 0.0359  301 TMP A O4    
2051 C C5    . TMP B .   ? 0.7257 0.7019 0.6135 -0.0252 -0.0365 0.0388  301 TMP A C5    
2052 C C5M   . TMP B .   ? 0.6760 0.6620 0.5843 -0.0168 -0.0323 0.0421  301 TMP A C5M   
2053 C C6    . TMP B .   ? 0.7838 0.7396 0.6375 -0.0334 -0.0363 0.0386  301 TMP A C6    
2054 P P     . PO4 C .   ? 0.5397 0.4886 0.4950 0.0217  -0.0388 0.0795  302 PO4 A P     
2055 O O1    . PO4 C .   ? 0.5375 0.4966 0.5023 0.0212  -0.0276 0.0691  302 PO4 A O1    
2056 O O2    . PO4 C .   ? 0.6421 0.5790 0.5699 0.0116  -0.0391 0.0832  302 PO4 A O2    
2057 O O3    . PO4 C .   ? 0.5132 0.4755 0.4836 0.0284  -0.0484 0.0819  302 PO4 A O3    
2058 O O4    . PO4 C .   ? 0.5375 0.4737 0.4966 0.0256  -0.0402 0.0841  302 PO4 A O4    
2059 P P     . PO4 D .   ? 1.4591 1.3511 1.4529 0.0297  -0.0156 0.0645  303 PO4 A P     
2060 O O1    . PO4 D .   ? 0.8150 0.7166 0.8135 0.0238  -0.0092 0.0549  303 PO4 A O1    
2061 O O2    . PO4 D .   ? 1.0918 0.9889 1.0981 0.0412  -0.0190 0.0607  303 PO4 A O2    
2062 O O3    . PO4 D .   ? 1.0063 0.8765 0.9951 0.0259  -0.0153 0.0706  303 PO4 A O3    
2063 O O4    . PO4 D .   ? 0.8566 0.7546 0.8394 0.0281  -0.0195 0.0720  303 PO4 A O4    
2064 P P     . PO4 E .   ? 1.2121 1.0548 1.2351 0.0513  -0.0122 0.0139  304 PO4 A P     
2065 O O1    . PO4 E .   ? 1.0986 0.9286 1.1176 0.0510  -0.0129 0.0011  304 PO4 A O1    
2066 O O2    . PO4 E .   ? 1.0322 0.8832 1.0562 0.0396  -0.0129 0.0173  304 PO4 A O2    
2067 O O3    . PO4 E .   ? 0.7798 0.6406 0.8022 0.0588  -0.0106 0.0144  304 PO4 A O3    
2068 O O4    . PO4 E .   ? 1.1170 0.9446 1.1437 0.0552  -0.0125 0.0227  304 PO4 A O4    
2069 O O     . HOH F .   ? 0.6079 0.6061 0.6547 0.0278  -0.0212 0.0008  401 HOH A O     
2070 O O     . HOH F .   ? 0.7137 0.6288 0.7081 -0.0259 0.1452  -0.0793 402 HOH A O     
2071 O O     . HOH F .   ? 0.4506 0.4789 0.4592 -0.0002 0.0199  0.0076  403 HOH A O     
2072 O O     . HOH F .   ? 0.4234 0.5421 0.6455 -0.0606 -0.0714 0.0462  404 HOH A O     
2073 O O     . HOH F .   ? 0.7328 0.5992 0.7422 0.0497  -0.0148 -0.0083 405 HOH A O     
2074 O O     . HOH F .   ? 0.5821 0.5593 0.5478 0.0147  -0.0165 0.0567  406 HOH A O     
2075 O O     . HOH F .   ? 0.4502 0.6442 0.7761 -0.0350 -0.1292 0.0793  407 HOH A O     
2076 O O     . HOH F .   ? 0.4770 0.5876 0.6305 -0.0055 -0.1786 0.0974  408 HOH A O     
2077 O O     . HOH F .   ? 0.6725 0.6802 0.7780 0.0637  -0.1603 0.1418  409 HOH A O     
2078 O O     . HOH F .   ? 0.4628 0.5592 0.5839 0.0819  0.0974  0.0503  410 HOH A O     
2079 O O     . HOH F .   ? 0.7726 0.7415 0.6713 -0.0140 -0.0169 0.0480  411 HOH A O     
2080 O O     . HOH F .   ? 0.5386 0.5687 0.5885 0.0057  0.0322  -0.0026 412 HOH A O     
2081 O O     . HOH F .   ? 0.4037 0.5828 0.6725 0.0454  0.0162  0.0748  413 HOH A O     
2082 O O     . HOH F .   ? 0.5469 0.5433 0.5957 0.0499  -0.1243 0.1208  414 HOH A O     
2083 O O     . HOH F .   ? 0.7073 0.5887 0.5693 -0.0591 0.0722  -0.0687 415 HOH A O     
2084 O O     . HOH F .   ? 0.5703 0.5716 0.5335 0.0062  -0.0109 0.0438  416 HOH A O     
2085 O O     . HOH F .   ? 0.5304 0.4879 0.5556 0.0340  -0.0175 0.0016  417 HOH A O     
2086 O O     . HOH F .   ? 0.4685 0.4912 0.4849 -0.0146 0.0042  0.0033  418 HOH A O     
2087 O O     . HOH F .   ? 0.5674 0.5145 0.6140 0.0714  -0.0332 0.0693  419 HOH A O     
2088 O O     . HOH F .   ? 0.4619 0.5127 0.4999 0.0430  -0.0070 0.0238  420 HOH A O     
2089 O O     . HOH F .   ? 0.5071 0.4972 0.4713 -0.0394 -0.0119 -0.0079 421 HOH A O     
2090 O O     . HOH F .   ? 0.8610 0.7346 0.8693 0.0195  -0.0066 0.0496  422 HOH A O     
2091 O O     . HOH F .   ? 0.5555 0.5515 0.5154 -0.0164 0.0363  -0.0001 423 HOH A O     
2092 O O     . HOH F .   ? 0.4914 0.5214 0.4686 -0.0019 -0.0440 0.0454  424 HOH A O     
2093 O O     . HOH F .   ? 0.7225 0.6440 0.5551 -0.0964 -0.1063 -0.0111 425 HOH A O     
2094 O O     . HOH F .   ? 0.8902 0.7801 0.7063 -0.0159 -0.1810 0.1405  426 HOH A O     
2095 O O     . HOH F .   ? 0.5578 0.5230 0.4580 0.0616  -0.0216 0.0071  427 HOH A O     
2096 O O     . HOH F .   ? 0.5900 0.5284 0.6439 0.0753  -0.0553 0.0923  428 HOH A O     
2097 O O     . HOH F .   ? 0.4633 0.4887 0.4481 -0.0203 -0.0220 0.0159  429 HOH A O     
2098 O O     . HOH F .   ? 0.5463 0.5698 0.5445 0.0523  -0.0258 0.0313  430 HOH A O     
2099 O O     . HOH F .   ? 0.4176 0.4857 0.4986 0.0282  0.0985  0.0893  431 HOH A O     
2100 O O     . HOH F .   ? 0.5290 0.5501 0.5272 0.0185  -0.0823 0.0802  432 HOH A O     
2101 O O     . HOH F .   ? 0.4065 0.4202 0.4749 -0.0214 0.0060  0.0045  433 HOH A O     
2102 O O     . HOH F .   ? 0.8325 0.7523 0.6907 0.0511  -0.0793 -0.0098 434 HOH A O     
2103 O O     . HOH F .   ? 0.5438 0.5910 0.5989 0.0187  0.0146  0.0115  435 HOH A O     
2104 O O     . HOH F .   ? 0.4189 0.4921 0.5088 -0.0517 -0.0977 0.0348  436 HOH A O     
2105 O O     . HOH F .   ? 0.7293 0.5808 0.5430 0.1079  0.0919  -0.0472 437 HOH A O     
2106 O O     . HOH F .   ? 0.7153 0.6716 0.6290 0.0030  -0.0473 0.0769  438 HOH A O     
2107 O O     . HOH F .   ? 0.5524 0.4886 0.5324 0.0289  -0.0238 0.0696  439 HOH A O     
2108 O O     . HOH F .   ? 0.5561 0.4730 0.5090 0.0688  -0.0057 -0.0223 440 HOH A O     
2109 O O     . HOH F .   ? 0.6492 0.5718 0.6736 0.0588  -0.0252 0.0619  441 HOH A O     
2110 O O     . HOH F .   ? 0.5154 0.5606 0.5886 0.0217  0.0051  0.0092  442 HOH A O     
2111 O O     . HOH F .   ? 0.5453 0.5043 0.5832 0.0859  0.0052  0.0201  443 HOH A O     
2112 O O     . HOH F .   ? 0.7643 0.6886 0.6209 -0.0091 -0.1104 0.1068  444 HOH A O     
2113 O O     . HOH F .   ? 0.5193 0.5477 0.5011 0.0027  -0.0679 0.0615  445 HOH A O     
2114 O O     . HOH F .   ? 0.6161 0.6388 0.6702 0.0339  -0.0343 0.0011  446 HOH A O     
2115 O O     . HOH F .   ? 0.4048 0.5864 0.6804 0.0419  0.0457  0.0767  447 HOH A O     
2116 O O     . HOH F .   ? 0.5555 0.5157 0.5603 0.0361  -0.0427 -0.0169 448 HOH A O     
2117 O O     . HOH F .   ? 0.5601 0.6964 0.9210 0.1329  -0.0066 0.0872  449 HOH A O     
2118 O O     . HOH F .   ? 0.6495 0.5812 0.4739 0.0568  0.0117  0.0731  450 HOH A O     
2119 O O     . HOH F .   ? 0.8243 0.7373 0.8893 0.0719  -0.2588 0.2133  451 HOH A O     
2120 O O     . HOH F .   ? 0.6672 0.6469 0.5991 0.0047  -0.0720 0.0796  452 HOH A O     
2121 O O     . HOH F .   ? 0.5505 0.5563 0.4975 -0.0070 -0.0950 0.0727  453 HOH A O     
2122 O O     . HOH F .   ? 0.3893 0.5450 0.6450 0.0013  0.0562  0.0838  454 HOH A O     
2123 O O     . HOH F .   ? 0.4692 0.6029 0.6628 0.0587  0.1394  0.0757  455 HOH A O     
2124 O O     . HOH F .   ? 0.5098 0.5243 0.4909 -0.0056 0.0223  0.0116  456 HOH A O     
2125 O O     . HOH F .   ? 0.8398 0.7170 0.6455 -0.0137 -0.1415 0.1342  457 HOH A O     
2126 O O     . HOH F .   ? 0.5704 0.5605 0.5874 0.0289  -0.0046 0.0304  458 HOH A O     
2127 O O     . HOH F .   ? 0.6533 0.6861 0.6399 -0.0248 -0.0500 0.0275  459 HOH A O     
2128 O O     . HOH F .   ? 0.6429 0.6923 0.7205 0.0201  0.0207  0.0064  460 HOH A O     
2129 O O     . HOH F .   ? 0.6436 0.4804 0.6860 0.0813  -0.0601 0.1120  461 HOH A O     
2130 O O     . HOH F .   ? 0.9029 0.8790 0.8132 -0.1011 -0.2873 0.0666  462 HOH A O     
2131 O O     . HOH F .   ? 0.5683 0.6060 0.5857 0.0486  -0.0144 0.0222  463 HOH A O     
2132 O O     . HOH F .   ? 0.5973 0.6331 0.6246 0.0100  0.0194  0.0135  464 HOH A O     
2133 O O     . HOH F .   ? 0.6953 0.7546 0.8954 0.0757  -0.1709 0.1438  465 HOH A O     
2134 O O     . HOH F .   ? 0.7601 0.6250 0.6831 0.0162  -0.0392 0.1068  466 HOH A O     
2135 O O     . HOH F .   ? 0.4563 0.4869 0.5134 0.0307  -0.0152 0.0071  467 HOH A O     
2136 O O     . HOH F .   ? 0.5027 0.5105 0.5032 -0.0532 -0.0470 0.0013  468 HOH A O     
2137 O O     . HOH F .   ? 0.4167 0.4444 0.4029 0.0461  0.0694  0.0743  469 HOH A O     
2138 O O     . HOH F .   ? 0.9355 0.9033 0.8237 -0.0579 -0.0596 0.0060  470 HOH A O     
2139 O O     . HOH F .   ? 0.8120 0.6632 0.8325 0.0748  -0.2678 0.2363  471 HOH A O     
2140 O O     . HOH F .   ? 0.8628 0.6971 1.0071 0.1508  0.0079  0.0388  472 HOH A O     
2141 O O     . HOH F .   ? 0.5292 0.7885 1.0170 0.0744  0.0913  0.0914  473 HOH A O     
2142 O O     . HOH F .   ? 0.8130 0.7068 0.7515 0.0039  -0.0089 0.0792  474 HOH A O     
2143 O O     . HOH F .   ? 0.5542 0.5570 0.5227 -0.0272 -0.0038 -0.0003 475 HOH A O     
2144 O O     . HOH F .   ? 0.8808 0.7017 0.8970 0.0484  -0.0218 0.0678  476 HOH A O     
2145 O O     . HOH F .   ? 0.6411 0.8226 1.0609 0.1190  -0.0342 0.1018  477 HOH A O     
2146 O O     . HOH F .   ? 0.8168 0.7775 1.0480 0.1241  -0.2042 0.1930  478 HOH A O     
2147 O O     . HOH F .   ? 0.4868 0.7026 0.8449 0.0360  0.0543  0.0861  479 HOH A O     
2148 O O     . HOH F .   ? 0.6535 0.6859 0.7568 0.0248  0.0159  0.0171  480 HOH A O     
2149 O O     . HOH F .   ? 0.5869 0.6100 0.6418 0.0032  0.0307  -0.0046 481 HOH A O     
2150 O O     . HOH F .   ? 0.4547 0.6106 0.7371 -0.0491 -0.0565 0.0617  482 HOH A O     
2151 O O     . HOH F .   ? 0.5962 0.5929 0.6261 0.0301  -0.0063 0.0176  483 HOH A O     
2152 O O     . HOH F .   ? 0.6430 0.6491 0.6124 0.0050  -0.1160 0.0911  484 HOH A O     
2153 O O     . HOH F .   ? 0.5183 0.7316 0.9047 -0.0516 -0.1235 0.0792  485 HOH A O     
2154 O O     . HOH F .   ? 0.5580 0.5758 0.6137 0.0257  -0.0118 0.0067  486 HOH A O     
2155 O O     . HOH F .   ? 0.5589 0.5408 0.5957 0.0279  -0.0129 0.0076  487 HOH A O     
2156 O O     . HOH F .   ? 0.4813 0.6166 0.7533 -0.0793 -0.1019 0.0493  488 HOH A O     
# 
