data_8YTP
# 
_entry.id   8YTP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.395 
_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   8YTP         pdb_00008ytp 10.2210/pdb8ytp/pdb 
WWPDB D_1300046352 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-07-03 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YTP 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              hanazono.str@tmd.ac.jp 
_pdbx_contact_author.name_first         Yuya 
_pdbx_contact_author.name_last          Hanazono 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3102-2945 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yoshida, M.'  1 ? 
'Hanazono, Y.' 2 ? 
'Numoto, N.'   3 ? 
'Ito, N.'      4 ? 
'Oda, M.'      5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                110068 
_citation.page_last                 110068 
_citation.title                     'Affinity-matured antibody with a disulfide bond in H-CDR3 loop.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2024.110068 
_citation.pdbx_database_id_PubMed   38909835 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yoshida, M.'   1  ? 
primary 'Hanazono, Y.'  2  ? 
primary 'Numoto, N.'    3  ? 
primary 'Nagao, S.'     4  ? 
primary 'Yabuno, S.'    5  ? 
primary 'Kitagawa, Y.'  6  ? 
primary 'Sekiguchi, H.' 7  ? 
primary 'Ito, N.'       8  ? 
primary 'Azuma, T.'     9  ? 
primary 'Oda, M.'       10 ? 
# 
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 'Single-chain Fv antibody of E11'                             26157.059 1   ? ? ? ? 
2 non-polymer syn '2-[2-(3-nitro-4-oxidanyl-phenyl)ethanoylamino]ethanoic acid' 254.196   1   ? ? ? ? 
3 water       nat water                                                         18.015    222 ? ? ? ? 
# 
_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       
;GSAQAVVTQESALTTSPGETVTLTCRSSTGAVISSNFVSWVQEKPDHLFTGLIGGNKNRAPGVPARFSGSLIGDKAVLTI
TGAQTEDEAIYFCALWYSNHWVFGGGTKLTVLGQGGGGSGGGGSGGGGSQVQLQQPGAELAKPGASVQLSCKGSGYTFPN
YWMHWVTQRPGRGLEWIGRIDPNSGFIRYDERFKTKATLTVDKPSSTAYMQLSSLTSDDSAVYFCARGCYGCIHFDYWGQ
GTTLTVSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSAQAVVTQESALTTSPGETVTLTCRSSTGAVISSNFVSWVQEKPDHLFTGLIGGNKNRAPGVPARFSGSLIGDKAVLTI
TGAQTEDEAIYFCALWYSNHWVFGGGTKLTVLGQGGGGSGGGGSGGGGSQVQLQQPGAELAKPGASVQLSCKGSGYTFPN
YWMHWVTQRPGRGLEWIGRIDPNSGFIRYDERFKTKATLTVDKPSSTAYMQLSSLTSDDSAVYFCARGCYGCIHFDYWGQ
GTTLTVSS
;
_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 '2-[2-(3-nitro-4-oxidanyl-phenyl)ethanoylamino]ethanoic acid' A1LZO 
3 water                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ALA n 
1 4   GLN n 
1 5   ALA n 
1 6   VAL n 
1 7   VAL n 
1 8   THR n 
1 9   GLN n 
1 10  GLU n 
1 11  SER n 
1 12  ALA n 
1 13  LEU n 
1 14  THR n 
1 15  THR n 
1 16  SER n 
1 17  PRO n 
1 18  GLY n 
1 19  GLU n 
1 20  THR n 
1 21  VAL n 
1 22  THR n 
1 23  LEU n 
1 24  THR n 
1 25  CYS n 
1 26  ARG n 
1 27  SER n 
1 28  SER n 
1 29  THR n 
1 30  GLY n 
1 31  ALA n 
1 32  VAL n 
1 33  ILE n 
1 34  SER n 
1 35  SER n 
1 36  ASN n 
1 37  PHE n 
1 38  VAL n 
1 39  SER n 
1 40  TRP n 
1 41  VAL n 
1 42  GLN n 
1 43  GLU n 
1 44  LYS n 
1 45  PRO n 
1 46  ASP n 
1 47  HIS n 
1 48  LEU n 
1 49  PHE n 
1 50  THR n 
1 51  GLY n 
1 52  LEU n 
1 53  ILE n 
1 54  GLY n 
1 55  GLY n 
1 56  ASN n 
1 57  LYS n 
1 58  ASN n 
1 59  ARG n 
1 60  ALA n 
1 61  PRO n 
1 62  GLY n 
1 63  VAL n 
1 64  PRO n 
1 65  ALA n 
1 66  ARG n 
1 67  PHE n 
1 68  SER n 
1 69  GLY n 
1 70  SER n 
1 71  LEU n 
1 72  ILE n 
1 73  GLY n 
1 74  ASP n 
1 75  LYS n 
1 76  ALA n 
1 77  VAL n 
1 78  LEU n 
1 79  THR n 
1 80  ILE n 
1 81  THR n 
1 82  GLY n 
1 83  ALA n 
1 84  GLN n 
1 85  THR n 
1 86  GLU n 
1 87  ASP n 
1 88  GLU n 
1 89  ALA n 
1 90  ILE n 
1 91  TYR n 
1 92  PHE n 
1 93  CYS n 
1 94  ALA n 
1 95  LEU n 
1 96  TRP n 
1 97  TYR n 
1 98  SER n 
1 99  ASN n 
1 100 HIS n 
1 101 TRP n 
1 102 VAL n 
1 103 PHE n 
1 104 GLY n 
1 105 GLY n 
1 106 GLY n 
1 107 THR n 
1 108 LYS n 
1 109 LEU n 
1 110 THR n 
1 111 VAL n 
1 112 LEU n 
1 113 GLY n 
1 114 GLN n 
1 115 GLY n 
1 116 GLY n 
1 117 GLY n 
1 118 GLY n 
1 119 SER n 
1 120 GLY n 
1 121 GLY n 
1 122 GLY n 
1 123 GLY n 
1 124 SER n 
1 125 GLY n 
1 126 GLY n 
1 127 GLY n 
1 128 GLY n 
1 129 SER n 
1 130 GLN n 
1 131 VAL n 
1 132 GLN n 
1 133 LEU n 
1 134 GLN n 
1 135 GLN n 
1 136 PRO n 
1 137 GLY n 
1 138 ALA n 
1 139 GLU n 
1 140 LEU n 
1 141 ALA n 
1 142 LYS n 
1 143 PRO n 
1 144 GLY n 
1 145 ALA n 
1 146 SER n 
1 147 VAL n 
1 148 GLN n 
1 149 LEU n 
1 150 SER n 
1 151 CYS n 
1 152 LYS n 
1 153 GLY n 
1 154 SER n 
1 155 GLY n 
1 156 TYR n 
1 157 THR n 
1 158 PHE n 
1 159 PRO n 
1 160 ASN n 
1 161 TYR n 
1 162 TRP n 
1 163 MET n 
1 164 HIS n 
1 165 TRP n 
1 166 VAL n 
1 167 THR n 
1 168 GLN n 
1 169 ARG n 
1 170 PRO n 
1 171 GLY n 
1 172 ARG n 
1 173 GLY n 
1 174 LEU n 
1 175 GLU n 
1 176 TRP n 
1 177 ILE n 
1 178 GLY n 
1 179 ARG n 
1 180 ILE n 
1 181 ASP n 
1 182 PRO n 
1 183 ASN n 
1 184 SER n 
1 185 GLY n 
1 186 PHE n 
1 187 ILE n 
1 188 ARG n 
1 189 TYR n 
1 190 ASP n 
1 191 GLU n 
1 192 ARG n 
1 193 PHE n 
1 194 LYS n 
1 195 THR n 
1 196 LYS n 
1 197 ALA n 
1 198 THR n 
1 199 LEU n 
1 200 THR n 
1 201 VAL n 
1 202 ASP n 
1 203 LYS n 
1 204 PRO n 
1 205 SER n 
1 206 SER n 
1 207 THR n 
1 208 ALA n 
1 209 TYR n 
1 210 MET n 
1 211 GLN n 
1 212 LEU n 
1 213 SER n 
1 214 SER n 
1 215 LEU n 
1 216 THR n 
1 217 SER n 
1 218 ASP n 
1 219 ASP n 
1 220 SER n 
1 221 ALA n 
1 222 VAL n 
1 223 TYR n 
1 224 PHE n 
1 225 CYS n 
1 226 ALA n 
1 227 ARG n 
1 228 GLY n 
1 229 CYS n 
1 230 TYR n 
1 231 GLY n 
1 232 CYS n 
1 233 ILE n 
1 234 HIS n 
1 235 PHE n 
1 236 ASP n 
1 237 TYR n 
1 238 TRP n 
1 239 GLY n 
1 240 GLN n 
1 241 GLY n 
1 242 THR n 
1 243 THR n 
1 244 LEU n 
1 245 THR n 
1 246 VAL n 
1 247 SER n 
1 248 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   248 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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 
A1LZO non-polymer         . '2-[2-(3-nitro-4-oxidanyl-phenyl)ethanoylamino]ethanoic acid' ? 'C10 H10 N2 O6'  254.196 
ALA   'L-peptide linking' y ALANINE                                                       ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                    ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                               ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                      ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                     ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                               ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                       ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                         ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                    ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                        ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                    ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                 ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                       ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                        ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                     ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                    ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                      ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   GLN 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  CYS 25  25  25  CYS CYS A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  HIS 47  47  47  HIS HIS A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  CYS 93  93  93  CYS CYS A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 GLY 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 GLY 123 123 ?   ?   ?   A . n 
A 1 124 SER 124 124 ?   ?   ?   A . n 
A 1 125 GLY 125 125 ?   ?   ?   A . n 
A 1 126 GLY 126 126 ?   ?   ?   A . n 
A 1 127 GLY 127 127 ?   ?   ?   A . n 
A 1 128 GLY 128 128 ?   ?   ?   A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLN 134 134 134 GLN GLN A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 CYS 151 151 151 CYS CYS A . n 
A 1 152 LYS 152 152 152 LYS LYS A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 MET 163 163 163 MET MET A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 TRP 165 165 165 TRP TRP A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ILE 180 180 180 ILE ILE A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 TYR 189 189 189 TYR TYR A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 THR 200 200 200 THR THR A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 TYR 223 223 223 TYR TYR A . n 
A 1 224 PHE 224 224 224 PHE PHE A . n 
A 1 225 CYS 225 225 225 CYS CYS A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 CYS 229 229 229 CYS CYS A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 CYS 232 232 232 CYS CYS A . n 
A 1 233 ILE 233 233 233 ILE ILE A . n 
A 1 234 HIS 234 234 234 HIS HIS A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 TRP 238 238 238 TRP TRP A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 GLN 240 240 240 GLN GLN A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 THR 243 243 243 THR THR 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 VAL 246 246 246 VAL VAL A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 SER 248 248 248 SER SER A . n 
# 
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 A1LZO 1   401 401 A1LZO LIG A . 
C 3 HOH   1   501 74  HOH   HOH A . 
C 3 HOH   2   502 16  HOH   HOH A . 
C 3 HOH   3   503 72  HOH   HOH A . 
C 3 HOH   4   504 198 HOH   HOH A . 
C 3 HOH   5   505 33  HOH   HOH A . 
C 3 HOH   6   506 54  HOH   HOH A . 
C 3 HOH   7   507 102 HOH   HOH A . 
C 3 HOH   8   508 61  HOH   HOH A . 
C 3 HOH   9   509 125 HOH   HOH A . 
C 3 HOH   10  510 156 HOH   HOH A . 
C 3 HOH   11  511 116 HOH   HOH A . 
C 3 HOH   12  512 161 HOH   HOH A . 
C 3 HOH   13  513 90  HOH   HOH A . 
C 3 HOH   14  514 210 HOH   HOH A . 
C 3 HOH   15  515 200 HOH   HOH A . 
C 3 HOH   16  516 179 HOH   HOH A . 
C 3 HOH   17  517 92  HOH   HOH A . 
C 3 HOH   18  518 190 HOH   HOH A . 
C 3 HOH   19  519 71  HOH   HOH A . 
C 3 HOH   20  520 8   HOH   HOH A . 
C 3 HOH   21  521 40  HOH   HOH A . 
C 3 HOH   22  522 124 HOH   HOH A . 
C 3 HOH   23  523 121 HOH   HOH A . 
C 3 HOH   24  524 182 HOH   HOH A . 
C 3 HOH   25  525 193 HOH   HOH A . 
C 3 HOH   26  526 171 HOH   HOH A . 
C 3 HOH   27  527 134 HOH   HOH A . 
C 3 HOH   28  528 56  HOH   HOH A . 
C 3 HOH   29  529 31  HOH   HOH A . 
C 3 HOH   30  530 95  HOH   HOH A . 
C 3 HOH   31  531 108 HOH   HOH A . 
C 3 HOH   32  532 89  HOH   HOH A . 
C 3 HOH   33  533 42  HOH   HOH A . 
C 3 HOH   34  534 150 HOH   HOH A . 
C 3 HOH   35  535 127 HOH   HOH A . 
C 3 HOH   36  536 37  HOH   HOH A . 
C 3 HOH   37  537 149 HOH   HOH A . 
C 3 HOH   38  538 94  HOH   HOH A . 
C 3 HOH   39  539 97  HOH   HOH A . 
C 3 HOH   40  540 48  HOH   HOH A . 
C 3 HOH   41  541 23  HOH   HOH A . 
C 3 HOH   42  542 55  HOH   HOH A . 
C 3 HOH   43  543 117 HOH   HOH A . 
C 3 HOH   44  544 187 HOH   HOH A . 
C 3 HOH   45  545 221 HOH   HOH A . 
C 3 HOH   46  546 46  HOH   HOH A . 
C 3 HOH   47  547 18  HOH   HOH A . 
C 3 HOH   48  548 3   HOH   HOH A . 
C 3 HOH   49  549 50  HOH   HOH A . 
C 3 HOH   50  550 169 HOH   HOH A . 
C 3 HOH   51  551 36  HOH   HOH A . 
C 3 HOH   52  552 19  HOH   HOH A . 
C 3 HOH   53  553 47  HOH   HOH A . 
C 3 HOH   54  554 154 HOH   HOH A . 
C 3 HOH   55  555 70  HOH   HOH A . 
C 3 HOH   56  556 81  HOH   HOH A . 
C 3 HOH   57  557 27  HOH   HOH A . 
C 3 HOH   58  558 5   HOH   HOH A . 
C 3 HOH   59  559 30  HOH   HOH A . 
C 3 HOH   60  560 211 HOH   HOH A . 
C 3 HOH   61  561 172 HOH   HOH A . 
C 3 HOH   62  562 82  HOH   HOH A . 
C 3 HOH   63  563 9   HOH   HOH A . 
C 3 HOH   64  564 213 HOH   HOH A . 
C 3 HOH   65  565 2   HOH   HOH A . 
C 3 HOH   66  566 26  HOH   HOH A . 
C 3 HOH   67  567 178 HOH   HOH A . 
C 3 HOH   68  568 75  HOH   HOH A . 
C 3 HOH   69  569 79  HOH   HOH A . 
C 3 HOH   70  570 166 HOH   HOH A . 
C 3 HOH   71  571 80  HOH   HOH A . 
C 3 HOH   72  572 34  HOH   HOH A . 
C 3 HOH   73  573 7   HOH   HOH A . 
C 3 HOH   74  574 222 HOH   HOH A . 
C 3 HOH   75  575 45  HOH   HOH A . 
C 3 HOH   76  576 28  HOH   HOH A . 
C 3 HOH   77  577 25  HOH   HOH A . 
C 3 HOH   78  578 11  HOH   HOH A . 
C 3 HOH   79  579 43  HOH   HOH A . 
C 3 HOH   80  580 21  HOH   HOH A . 
C 3 HOH   81  581 6   HOH   HOH A . 
C 3 HOH   82  582 88  HOH   HOH A . 
C 3 HOH   83  583 126 HOH   HOH A . 
C 3 HOH   84  584 32  HOH   HOH A . 
C 3 HOH   85  585 183 HOH   HOH A . 
C 3 HOH   86  586 64  HOH   HOH A . 
C 3 HOH   87  587 220 HOH   HOH A . 
C 3 HOH   88  588 112 HOH   HOH A . 
C 3 HOH   89  589 131 HOH   HOH A . 
C 3 HOH   90  590 1   HOH   HOH A . 
C 3 HOH   91  591 113 HOH   HOH A . 
C 3 HOH   92  592 164 HOH   HOH A . 
C 3 HOH   93  593 68  HOH   HOH A . 
C 3 HOH   94  594 135 HOH   HOH A . 
C 3 HOH   95  595 20  HOH   HOH A . 
C 3 HOH   96  596 38  HOH   HOH A . 
C 3 HOH   97  597 195 HOH   HOH A . 
C 3 HOH   98  598 10  HOH   HOH A . 
C 3 HOH   99  599 189 HOH   HOH A . 
C 3 HOH   100 600 13  HOH   HOH A . 
C 3 HOH   101 601 181 HOH   HOH A . 
C 3 HOH   102 602 84  HOH   HOH A . 
C 3 HOH   103 603 218 HOH   HOH A . 
C 3 HOH   104 604 173 HOH   HOH A . 
C 3 HOH   105 605 51  HOH   HOH A . 
C 3 HOH   106 606 62  HOH   HOH A . 
C 3 HOH   107 607 49  HOH   HOH A . 
C 3 HOH   108 608 103 HOH   HOH A . 
C 3 HOH   109 609 15  HOH   HOH A . 
C 3 HOH   110 610 107 HOH   HOH A . 
C 3 HOH   111 611 132 HOH   HOH A . 
C 3 HOH   112 612 141 HOH   HOH A . 
C 3 HOH   113 613 17  HOH   HOH A . 
C 3 HOH   114 614 99  HOH   HOH A . 
C 3 HOH   115 615 73  HOH   HOH A . 
C 3 HOH   116 616 65  HOH   HOH A . 
C 3 HOH   117 617 4   HOH   HOH A . 
C 3 HOH   118 618 63  HOH   HOH A . 
C 3 HOH   119 619 162 HOH   HOH A . 
C 3 HOH   120 620 167 HOH   HOH A . 
C 3 HOH   121 621 96  HOH   HOH A . 
C 3 HOH   122 622 87  HOH   HOH A . 
C 3 HOH   123 623 52  HOH   HOH A . 
C 3 HOH   124 624 85  HOH   HOH A . 
C 3 HOH   125 625 151 HOH   HOH A . 
C 3 HOH   126 626 69  HOH   HOH A . 
C 3 HOH   127 627 119 HOH   HOH A . 
C 3 HOH   128 628 59  HOH   HOH A . 
C 3 HOH   129 629 192 HOH   HOH A . 
C 3 HOH   130 630 14  HOH   HOH A . 
C 3 HOH   131 631 144 HOH   HOH A . 
C 3 HOH   132 632 163 HOH   HOH A . 
C 3 HOH   133 633 86  HOH   HOH A . 
C 3 HOH   134 634 67  HOH   HOH A . 
C 3 HOH   135 635 41  HOH   HOH A . 
C 3 HOH   136 636 180 HOH   HOH A . 
C 3 HOH   137 637 128 HOH   HOH A . 
C 3 HOH   138 638 136 HOH   HOH A . 
C 3 HOH   139 639 201 HOH   HOH A . 
C 3 HOH   140 640 186 HOH   HOH A . 
C 3 HOH   141 641 184 HOH   HOH A . 
C 3 HOH   142 642 115 HOH   HOH A . 
C 3 HOH   143 643 53  HOH   HOH A . 
C 3 HOH   144 644 120 HOH   HOH A . 
C 3 HOH   145 645 138 HOH   HOH A . 
C 3 HOH   146 646 109 HOH   HOH A . 
C 3 HOH   147 647 185 HOH   HOH A . 
C 3 HOH   148 648 66  HOH   HOH A . 
C 3 HOH   149 649 143 HOH   HOH A . 
C 3 HOH   150 650 214 HOH   HOH A . 
C 3 HOH   151 651 206 HOH   HOH A . 
C 3 HOH   152 652 57  HOH   HOH A . 
C 3 HOH   153 653 29  HOH   HOH A . 
C 3 HOH   154 654 168 HOH   HOH A . 
C 3 HOH   155 655 93  HOH   HOH A . 
C 3 HOH   156 656 160 HOH   HOH A . 
C 3 HOH   157 657 60  HOH   HOH A . 
C 3 HOH   158 658 12  HOH   HOH A . 
C 3 HOH   159 659 175 HOH   HOH A . 
C 3 HOH   160 660 123 HOH   HOH A . 
C 3 HOH   161 661 158 HOH   HOH A . 
C 3 HOH   162 662 24  HOH   HOH A . 
C 3 HOH   163 663 39  HOH   HOH A . 
C 3 HOH   164 664 196 HOH   HOH A . 
C 3 HOH   165 665 58  HOH   HOH A . 
C 3 HOH   166 666 202 HOH   HOH A . 
C 3 HOH   167 667 22  HOH   HOH A . 
C 3 HOH   168 668 170 HOH   HOH A . 
C 3 HOH   169 669 35  HOH   HOH A . 
C 3 HOH   170 670 139 HOH   HOH A . 
C 3 HOH   171 671 191 HOH   HOH A . 
C 3 HOH   172 672 77  HOH   HOH A . 
C 3 HOH   173 673 152 HOH   HOH A . 
C 3 HOH   174 674 188 HOH   HOH A . 
C 3 HOH   175 675 44  HOH   HOH A . 
C 3 HOH   176 676 122 HOH   HOH A . 
C 3 HOH   177 677 91  HOH   HOH A . 
C 3 HOH   178 678 106 HOH   HOH A . 
C 3 HOH   179 679 101 HOH   HOH A . 
C 3 HOH   180 680 148 HOH   HOH A . 
C 3 HOH   181 681 111 HOH   HOH A . 
C 3 HOH   182 682 76  HOH   HOH A . 
C 3 HOH   183 683 137 HOH   HOH A . 
C 3 HOH   184 684 133 HOH   HOH A . 
C 3 HOH   185 685 98  HOH   HOH A . 
C 3 HOH   186 686 157 HOH   HOH A . 
C 3 HOH   187 687 219 HOH   HOH A . 
C 3 HOH   188 688 203 HOH   HOH A . 
C 3 HOH   189 689 176 HOH   HOH A . 
C 3 HOH   190 690 159 HOH   HOH A . 
C 3 HOH   191 691 208 HOH   HOH A . 
C 3 HOH   192 692 153 HOH   HOH A . 
C 3 HOH   193 693 194 HOH   HOH A . 
C 3 HOH   194 694 140 HOH   HOH A . 
C 3 HOH   195 695 129 HOH   HOH A . 
C 3 HOH   196 696 209 HOH   HOH A . 
C 3 HOH   197 697 197 HOH   HOH A . 
C 3 HOH   198 698 118 HOH   HOH A . 
C 3 HOH   199 699 100 HOH   HOH A . 
C 3 HOH   200 700 83  HOH   HOH A . 
C 3 HOH   201 701 146 HOH   HOH A . 
C 3 HOH   202 702 174 HOH   HOH A . 
C 3 HOH   203 703 147 HOH   HOH A . 
C 3 HOH   204 704 105 HOH   HOH A . 
C 3 HOH   205 705 114 HOH   HOH A . 
C 3 HOH   206 706 204 HOH   HOH A . 
C 3 HOH   207 707 130 HOH   HOH A . 
C 3 HOH   208 708 142 HOH   HOH A . 
C 3 HOH   209 709 207 HOH   HOH A . 
C 3 HOH   210 710 217 HOH   HOH A . 
C 3 HOH   211 711 199 HOH   HOH A . 
C 3 HOH   212 712 212 HOH   HOH A . 
C 3 HOH   213 713 110 HOH   HOH A . 
C 3 HOH   214 714 205 HOH   HOH A . 
C 3 HOH   215 715 155 HOH   HOH A . 
C 3 HOH   216 716 215 HOH   HOH A . 
C 3 HOH   217 717 104 HOH   HOH A . 
C 3 HOH   218 718 78  HOH   HOH A . 
C 3 HOH   219 719 177 HOH   HOH A . 
C 3 HOH   220 720 165 HOH   HOH A . 
C 3 HOH   221 721 145 HOH   HOH A . 
C 3 HOH   222 722 216 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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    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                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YTP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.680 
_cell.length_a_esd                 ? 
_cell.length_b                     61.420 
_cell.length_b_esd                 ? 
_cell.length_c                     88.820 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YTP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YTP 
_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             1.86 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          33.88 
_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    '0.1 M HEPES sodium pH 7.5, 10% v/v 2-propanol, 20% w/v polyethylene glycol 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 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         2023-10-25 
_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   0.8 
_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                        'SPRING-8 BEAMLINE BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YTP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.36 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     42209 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.101 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.36 
_reflns_shell.d_res_low                                     1.44 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6460 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.550 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.004 
_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                                 8YTP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.36 
_refine.ls_d_res_low                             35.99 
_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                     42161 
_refine.ls_number_reflns_R_free                  2109 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.53 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1473 
_refine.ls_R_factor_R_free                       0.1748 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1458 
_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                          1.35 
_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                      6K4Z 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.64 
_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                            0.15 
_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        1784 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_refine_hist.number_atoms_solvent             222 
_refine_hist.number_atoms_total               2024 
_refine_hist.d_res_high                       1.36 
_refine_hist.d_res_low                        35.99 
# 
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' ? 0.012  ? 1944 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.256  ? 2668 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.299 ? 700  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.113  ? 292  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 345  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.36 1.39  . . 136 2571 96.00  . . . . 0.2380 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 1.39 1.43  . . 137 2615 98.00  . . . . 0.2219 . . . . . . . . . . . 0.2588 
'X-RAY DIFFRACTION' 1.43 1.46  . . 139 2632 100.00 . . . . 0.1982 . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 1.47 1.51  . . 137 2624 98.00  . . . . 0.1805 . . . . . . . . . . . 0.2423 
'X-RAY DIFFRACTION' 1.51 1.56  . . 140 2642 98.00  . . . . 0.1642 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 1.56 1.61  . . 140 2670 100.00 . . . . 0.1591 . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 1.61 1.68  . . 140 2663 99.00  . . . . 0.1525 . . . . . . . . . . . 0.1902 
'X-RAY DIFFRACTION' 1.68 1.75  . . 139 2638 99.00  . . . . 0.1380 . . . . . . . . . . . 0.2080 
'X-RAY DIFFRACTION' 1.75 1.85  . . 141 2672 99.00  . . . . 0.1303 . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 1.85 1.96  . . 142 2696 99.00  . . . . 0.1360 . . . . . . . . . . . 0.1742 
'X-RAY DIFFRACTION' 1.96 2.11  . . 141 2689 99.00  . . . . 0.1306 . . . . . . . . . . . 0.1764 
'X-RAY DIFFRACTION' 2.11 2.33  . . 143 2709 100.00 . . . . 0.1324 . . . . . . . . . . . 0.1665 
'X-RAY DIFFRACTION' 2.33 2.66  . . 141 2685 98.00  . . . . 0.1490 . . . . . . . . . . . 0.1545 
'X-RAY DIFFRACTION' 2.66 3.35  . . 145 2742 99.00  . . . . 0.1499 . . . . . . . . . . . 0.1720 
'X-RAY DIFFRACTION' 3.35 35.99 . . 148 2804 96.00  . . . . 0.1379 . . . . . . . . . . . 0.1479 
# 
_struct.entry_id                     8YTP 
_struct.title                        'Single-chain Fv antibody of E11 complex with NP-glycine under reducing conditions' 
_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        8YTP 
_struct_keywords.text            'ANTIGEN BINDING, AFFINITY MATURATION, SOMATIC HYPERMUTATION, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8YTP 
_struct_ref.pdbx_db_accession          8YTP 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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              8YTP 
_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                 248 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8YTP 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  248 
_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       248 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 ILE A 33  ? PHE A 37  ? ILE A 33  PHE A 37  5 ? 5 
HELX_P HELX_P2 AA2 GLN A 84  ? GLU A 88  ? GLN A 84  GLU A 88  5 ? 5 
HELX_P HELX_P3 AA3 THR A 157 ? TYR A 161 ? THR A 157 TYR A 161 5 ? 5 
HELX_P HELX_P4 AA4 GLU A 191 ? LYS A 194 ? GLU A 191 LYS A 194 5 ? 4 
HELX_P HELX_P5 AA5 THR A 216 ? SER A 220 ? THR A 216 SER A 220 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 25  SG ? ? ? 1_555 A CYS 93  SG A ? A CYS 25  A CYS 93  1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf2 disulf ? ? A CYS 25  SG ? ? ? 1_555 A CYS 93  SG B ? A CYS 25  A CYS 93  1_555 ? ? ? ? ? ? ? 1.939 ? ? 
disulf3 disulf ? ? A CYS 151 SG ? ? ? 1_555 A CYS 225 SG ? ? A CYS 151 A CYS 225 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 7   ? GLN A 9   ? VAL A 7   GLN A 9   
AA1 2 THR A 20  ? SER A 27  ? THR A 20  SER A 27  
AA1 3 LYS A 75  ? THR A 81  ? LYS A 75  THR A 81  
AA1 4 PHE A 67  ? ILE A 72  ? PHE A 67  ILE A 72  
AA2 1 ALA A 12  ? THR A 15  ? ALA A 12  THR A 15  
AA2 2 THR A 107 ? VAL A 111 ? THR A 107 VAL A 111 
AA2 3 ALA A 89  ? TRP A 96  ? ALA A 89  TRP A 96  
AA2 4 SER A 39  ? LYS A 44  ? SER A 39  LYS A 44  
AA2 5 LEU A 48  ? GLY A 54  ? LEU A 48  GLY A 54  
AA2 6 ASN A 58  ? ARG A 59  ? ASN A 58  ARG A 59  
AA3 1 ALA A 12  ? THR A 15  ? ALA A 12  THR A 15  
AA3 2 THR A 107 ? VAL A 111 ? THR A 107 VAL A 111 
AA3 3 ALA A 89  ? TRP A 96  ? ALA A 89  TRP A 96  
AA3 4 TRP A 101 ? PHE A 103 ? TRP A 101 PHE A 103 
AA4 1 GLN A 132 ? GLN A 134 ? GLN A 132 GLN A 134 
AA4 2 VAL A 147 ? SER A 154 ? VAL A 147 SER A 154 
AA4 3 THR A 207 ? LEU A 212 ? THR A 207 LEU A 212 
AA4 4 ALA A 197 ? ASP A 202 ? ALA A 197 ASP A 202 
AA5 1 ALA A 138 ? ALA A 141 ? ALA A 138 ALA A 141 
AA5 2 THR A 242 ? VAL A 246 ? THR A 242 VAL A 246 
AA5 3 ALA A 221 ? GLY A 228 ? ALA A 221 GLY A 228 
AA5 4 TRP A 162 ? ARG A 169 ? TRP A 162 ARG A 169 
AA5 5 GLY A 173 ? ILE A 180 ? GLY A 173 ILE A 180 
AA5 6 ILE A 187 ? TYR A 189 ? ILE A 187 TYR A 189 
# 
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 THR A 8   ? N THR A 8   O ARG A 26  ? O ARG A 26  
AA1 2 3 N VAL A 21  ? N VAL A 21  O ILE A 80  ? O ILE A 80  
AA1 3 4 O THR A 79  ? O THR A 79  N SER A 68  ? N SER A 68  
AA2 1 2 N THR A 15  ? N THR A 15  O THR A 110 ? O THR A 110 
AA2 2 3 O LEU A 109 ? O LEU A 109 N ALA A 89  ? N ALA A 89  
AA2 3 4 O ILE A 90  ? O ILE A 90  N GLU A 43  ? N GLU A 43  
AA2 4 5 N TRP A 40  ? N TRP A 40  O LEU A 52  ? O LEU A 52  
AA2 5 6 N GLY A 54  ? N GLY A 54  O ASN A 58  ? O ASN A 58  
AA3 1 2 N THR A 15  ? N THR A 15  O THR A 110 ? O THR A 110 
AA3 2 3 O LEU A 109 ? O LEU A 109 N ALA A 89  ? N ALA A 89  
AA3 3 4 N LEU A 95  ? N LEU A 95  O VAL A 102 ? O VAL A 102 
AA4 1 2 N GLN A 134 ? N GLN A 134 O LYS A 152 ? O LYS A 152 
AA4 2 3 N LEU A 149 ? N LEU A 149 O MET A 210 ? O MET A 210 
AA4 3 4 O THR A 207 ? O THR A 207 N ASP A 202 ? N ASP A 202 
AA5 1 2 N GLU A 139 ? N GLU A 139 O THR A 245 ? O THR A 245 
AA5 2 3 O LEU A 244 ? O LEU A 244 N ALA A 221 ? N ALA A 221 
AA5 3 4 O ALA A 226 ? O ALA A 226 N HIS A 164 ? N HIS A 164 
AA5 4 5 N TRP A 165 ? N TRP A 165 O ILE A 177 ? O ILE A 177 
AA5 5 6 N ARG A 179 ? N ARG A 179 O ARG A 188 ? O ARG A 188 
# 
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 ASP A 46  ? ? 70.06   42.81   
2  1 HIS A 47  ? ? 27.45   59.46   
3  1 HIS A 47  ? ? 27.64   59.14   
4  1 ASN A 56  ? ? 76.41   -46.63  
5  1 TYR A 97  ? ? -116.95 64.33   
6  1 SER A 98  ? ? 76.34   -41.51  
7  1 ASN A 99  ? ? -146.45 10.01   
8  1 CYS A 229 ? ? -171.12 133.70  
9  1 CYS A 232 ? ? -119.82 -150.94 
10 1 PHE A 235 ? ? 70.36   30.82   
# 
_pdbx_entry_details.entry_id                 8YTP 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A ALA 3   ? A ALA 3   
4  1 Y 1 A GLN 4   ? A GLN 4   
5  1 Y 1 A GLY 121 ? A GLY 121 
6  1 Y 1 A GLY 122 ? A GLY 122 
7  1 Y 1 A GLY 123 ? A GLY 123 
8  1 Y 1 A SER 124 ? A SER 124 
9  1 Y 1 A GLY 125 ? A GLY 125 
10 1 Y 1 A GLY 126 ? A GLY 126 
11 1 Y 1 A GLY 127 ? A GLY 127 
12 1 Y 1 A GLY 128 ? A GLY 128 
# 
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 
A1LZO C10  C N N 1   
A1LZO N12  N N N 2   
A1LZO C01  C Y N 3   
A1LZO C02  C Y N 4   
A1LZO C03  C Y N 5   
A1LZO C04  C Y N 6   
A1LZO C05  C Y N 7   
A1LZO C06  C Y N 8   
A1LZO C08  C N N 9   
A1LZO C09  C N N 10  
A1LZO C18  C N N 11  
A1LZO N11  N N N 12  
A1LZO O07  O N N 13  
A1LZO O13  O N N 14  
A1LZO O14  O N N 15  
A1LZO O15  O N N 16  
A1LZO O16  O N N 17  
A1LZO O17  O N N 18  
A1LZO H121 H N N 19  
A1LZO H011 H N N 20  
A1LZO H041 H N N 21  
A1LZO H061 H N N 22  
A1LZO H091 H N N 23  
A1LZO H092 H N N 24  
A1LZO H182 H N N 25  
A1LZO H181 H N N 26  
A1LZO H071 H N N 27  
A1LZO H1   H N N 28  
ALA   N    N N N 29  
ALA   CA   C N S 30  
ALA   C    C N N 31  
ALA   O    O N N 32  
ALA   CB   C N N 33  
ALA   OXT  O N N 34  
ALA   H    H N N 35  
ALA   H2   H N N 36  
ALA   HA   H N N 37  
ALA   HB1  H N N 38  
ALA   HB2  H N N 39  
ALA   HB3  H N N 40  
ALA   HXT  H N N 41  
ARG   N    N N N 42  
ARG   CA   C N S 43  
ARG   C    C N N 44  
ARG   O    O N N 45  
ARG   CB   C N N 46  
ARG   CG   C N N 47  
ARG   CD   C N N 48  
ARG   NE   N N N 49  
ARG   CZ   C N N 50  
ARG   NH1  N N N 51  
ARG   NH2  N N N 52  
ARG   OXT  O N N 53  
ARG   H    H N N 54  
ARG   H2   H N N 55  
ARG   HA   H N N 56  
ARG   HB2  H N N 57  
ARG   HB3  H N N 58  
ARG   HG2  H N N 59  
ARG   HG3  H N N 60  
ARG   HD2  H N N 61  
ARG   HD3  H N N 62  
ARG   HE   H N N 63  
ARG   HH11 H N N 64  
ARG   HH12 H N N 65  
ARG   HH21 H N N 66  
ARG   HH22 H N N 67  
ARG   HXT  H N N 68  
ASN   N    N N N 69  
ASN   CA   C N S 70  
ASN   C    C N N 71  
ASN   O    O N N 72  
ASN   CB   C N N 73  
ASN   CG   C N N 74  
ASN   OD1  O N N 75  
ASN   ND2  N N N 76  
ASN   OXT  O N N 77  
ASN   H    H N N 78  
ASN   H2   H N N 79  
ASN   HA   H N N 80  
ASN   HB2  H N N 81  
ASN   HB3  H N N 82  
ASN   HD21 H N N 83  
ASN   HD22 H N N 84  
ASN   HXT  H N N 85  
ASP   N    N N N 86  
ASP   CA   C N S 87  
ASP   C    C N N 88  
ASP   O    O N N 89  
ASP   CB   C N N 90  
ASP   CG   C N N 91  
ASP   OD1  O N N 92  
ASP   OD2  O N N 93  
ASP   OXT  O N N 94  
ASP   H    H N N 95  
ASP   H2   H N N 96  
ASP   HA   H N N 97  
ASP   HB2  H N N 98  
ASP   HB3  H N N 99  
ASP   HD2  H N N 100 
ASP   HXT  H N N 101 
CYS   N    N N N 102 
CYS   CA   C N R 103 
CYS   C    C N N 104 
CYS   O    O N N 105 
CYS   CB   C N N 106 
CYS   SG   S N N 107 
CYS   OXT  O N N 108 
CYS   H    H N N 109 
CYS   H2   H N N 110 
CYS   HA   H N N 111 
CYS   HB2  H N N 112 
CYS   HB3  H N N 113 
CYS   HG   H N N 114 
CYS   HXT  H N N 115 
GLN   N    N N N 116 
GLN   CA   C N S 117 
GLN   C    C N N 118 
GLN   O    O N N 119 
GLN   CB   C N N 120 
GLN   CG   C N N 121 
GLN   CD   C N N 122 
GLN   OE1  O N N 123 
GLN   NE2  N N N 124 
GLN   OXT  O N N 125 
GLN   H    H N N 126 
GLN   H2   H N N 127 
GLN   HA   H N N 128 
GLN   HB2  H N N 129 
GLN   HB3  H N N 130 
GLN   HG2  H N N 131 
GLN   HG3  H N N 132 
GLN   HE21 H N N 133 
GLN   HE22 H N N 134 
GLN   HXT  H N N 135 
GLU   N    N N N 136 
GLU   CA   C N S 137 
GLU   C    C N N 138 
GLU   O    O N N 139 
GLU   CB   C N N 140 
GLU   CG   C N N 141 
GLU   CD   C N N 142 
GLU   OE1  O N N 143 
GLU   OE2  O N N 144 
GLU   OXT  O N N 145 
GLU   H    H N N 146 
GLU   H2   H N N 147 
GLU   HA   H N N 148 
GLU   HB2  H N N 149 
GLU   HB3  H N N 150 
GLU   HG2  H N N 151 
GLU   HG3  H N N 152 
GLU   HE2  H N N 153 
GLU   HXT  H N N 154 
GLY   N    N N N 155 
GLY   CA   C N N 156 
GLY   C    C N N 157 
GLY   O    O N N 158 
GLY   OXT  O N N 159 
GLY   H    H N N 160 
GLY   H2   H N N 161 
GLY   HA2  H N N 162 
GLY   HA3  H N N 163 
GLY   HXT  H N N 164 
HIS   N    N N N 165 
HIS   CA   C N S 166 
HIS   C    C N N 167 
HIS   O    O N N 168 
HIS   CB   C N N 169 
HIS   CG   C Y N 170 
HIS   ND1  N Y N 171 
HIS   CD2  C Y N 172 
HIS   CE1  C Y N 173 
HIS   NE2  N Y N 174 
HIS   OXT  O N N 175 
HIS   H    H N N 176 
HIS   H2   H N N 177 
HIS   HA   H N N 178 
HIS   HB2  H N N 179 
HIS   HB3  H N N 180 
HIS   HD1  H N N 181 
HIS   HD2  H N N 182 
HIS   HE1  H N N 183 
HIS   HE2  H N N 184 
HIS   HXT  H N N 185 
HOH   O    O N N 186 
HOH   H1   H N N 187 
HOH   H2   H N N 188 
ILE   N    N N N 189 
ILE   CA   C N S 190 
ILE   C    C N N 191 
ILE   O    O N N 192 
ILE   CB   C N S 193 
ILE   CG1  C N N 194 
ILE   CG2  C N N 195 
ILE   CD1  C N N 196 
ILE   OXT  O N N 197 
ILE   H    H N N 198 
ILE   H2   H N N 199 
ILE   HA   H N N 200 
ILE   HB   H N N 201 
ILE   HG12 H N N 202 
ILE   HG13 H N N 203 
ILE   HG21 H N N 204 
ILE   HG22 H N N 205 
ILE   HG23 H N N 206 
ILE   HD11 H N N 207 
ILE   HD12 H N N 208 
ILE   HD13 H N N 209 
ILE   HXT  H N N 210 
LEU   N    N N N 211 
LEU   CA   C N S 212 
LEU   C    C N N 213 
LEU   O    O N N 214 
LEU   CB   C N N 215 
LEU   CG   C N N 216 
LEU   CD1  C N N 217 
LEU   CD2  C N N 218 
LEU   OXT  O N N 219 
LEU   H    H N N 220 
LEU   H2   H N N 221 
LEU   HA   H N N 222 
LEU   HB2  H N N 223 
LEU   HB3  H N N 224 
LEU   HG   H N N 225 
LEU   HD11 H N N 226 
LEU   HD12 H N N 227 
LEU   HD13 H N N 228 
LEU   HD21 H N N 229 
LEU   HD22 H N N 230 
LEU   HD23 H N N 231 
LEU   HXT  H N N 232 
LYS   N    N N N 233 
LYS   CA   C N S 234 
LYS   C    C N N 235 
LYS   O    O N N 236 
LYS   CB   C N N 237 
LYS   CG   C N N 238 
LYS   CD   C N N 239 
LYS   CE   C N N 240 
LYS   NZ   N N N 241 
LYS   OXT  O N N 242 
LYS   H    H N N 243 
LYS   H2   H N N 244 
LYS   HA   H N N 245 
LYS   HB2  H N N 246 
LYS   HB3  H N N 247 
LYS   HG2  H N N 248 
LYS   HG3  H N N 249 
LYS   HD2  H N N 250 
LYS   HD3  H N N 251 
LYS   HE2  H N N 252 
LYS   HE3  H N N 253 
LYS   HZ1  H N N 254 
LYS   HZ2  H N N 255 
LYS   HZ3  H N N 256 
LYS   HXT  H N N 257 
MET   N    N N N 258 
MET   CA   C N S 259 
MET   C    C N N 260 
MET   O    O N N 261 
MET   CB   C N N 262 
MET   CG   C N N 263 
MET   SD   S N N 264 
MET   CE   C N N 265 
MET   OXT  O N N 266 
MET   H    H N N 267 
MET   H2   H N N 268 
MET   HA   H N N 269 
MET   HB2  H N N 270 
MET   HB3  H N N 271 
MET   HG2  H N N 272 
MET   HG3  H N N 273 
MET   HE1  H N N 274 
MET   HE2  H N N 275 
MET   HE3  H N N 276 
MET   HXT  H N N 277 
PHE   N    N N N 278 
PHE   CA   C N S 279 
PHE   C    C N N 280 
PHE   O    O N N 281 
PHE   CB   C N N 282 
PHE   CG   C Y N 283 
PHE   CD1  C Y N 284 
PHE   CD2  C Y N 285 
PHE   CE1  C Y N 286 
PHE   CE2  C Y N 287 
PHE   CZ   C Y N 288 
PHE   OXT  O N N 289 
PHE   H    H N N 290 
PHE   H2   H N N 291 
PHE   HA   H N N 292 
PHE   HB2  H N N 293 
PHE   HB3  H N N 294 
PHE   HD1  H N N 295 
PHE   HD2  H N N 296 
PHE   HE1  H N N 297 
PHE   HE2  H N N 298 
PHE   HZ   H N N 299 
PHE   HXT  H N N 300 
PRO   N    N N N 301 
PRO   CA   C N S 302 
PRO   C    C N N 303 
PRO   O    O N N 304 
PRO   CB   C N N 305 
PRO   CG   C N N 306 
PRO   CD   C N N 307 
PRO   OXT  O N N 308 
PRO   H    H N N 309 
PRO   HA   H N N 310 
PRO   HB2  H N N 311 
PRO   HB3  H N N 312 
PRO   HG2  H N N 313 
PRO   HG3  H N N 314 
PRO   HD2  H N N 315 
PRO   HD3  H N N 316 
PRO   HXT  H N N 317 
SER   N    N N N 318 
SER   CA   C N S 319 
SER   C    C N N 320 
SER   O    O N N 321 
SER   CB   C N N 322 
SER   OG   O N N 323 
SER   OXT  O N N 324 
SER   H    H N N 325 
SER   H2   H N N 326 
SER   HA   H N N 327 
SER   HB2  H N N 328 
SER   HB3  H N N 329 
SER   HG   H N N 330 
SER   HXT  H N N 331 
THR   N    N N N 332 
THR   CA   C N S 333 
THR   C    C N N 334 
THR   O    O N N 335 
THR   CB   C N R 336 
THR   OG1  O N N 337 
THR   CG2  C N N 338 
THR   OXT  O N N 339 
THR   H    H N N 340 
THR   H2   H N N 341 
THR   HA   H N N 342 
THR   HB   H N N 343 
THR   HG1  H N N 344 
THR   HG21 H N N 345 
THR   HG22 H N N 346 
THR   HG23 H N N 347 
THR   HXT  H N N 348 
TRP   N    N N N 349 
TRP   CA   C N S 350 
TRP   C    C N N 351 
TRP   O    O N N 352 
TRP   CB   C N N 353 
TRP   CG   C Y N 354 
TRP   CD1  C Y N 355 
TRP   CD2  C Y N 356 
TRP   NE1  N Y N 357 
TRP   CE2  C Y N 358 
TRP   CE3  C Y N 359 
TRP   CZ2  C Y N 360 
TRP   CZ3  C Y N 361 
TRP   CH2  C Y N 362 
TRP   OXT  O N N 363 
TRP   H    H N N 364 
TRP   H2   H N N 365 
TRP   HA   H N N 366 
TRP   HB2  H N N 367 
TRP   HB3  H N N 368 
TRP   HD1  H N N 369 
TRP   HE1  H N N 370 
TRP   HE3  H N N 371 
TRP   HZ2  H N N 372 
TRP   HZ3  H N N 373 
TRP   HH2  H N N 374 
TRP   HXT  H N N 375 
TYR   N    N N N 376 
TYR   CA   C N S 377 
TYR   C    C N N 378 
TYR   O    O N N 379 
TYR   CB   C N N 380 
TYR   CG   C Y N 381 
TYR   CD1  C Y N 382 
TYR   CD2  C Y N 383 
TYR   CE1  C Y N 384 
TYR   CE2  C Y N 385 
TYR   CZ   C Y N 386 
TYR   OH   O N N 387 
TYR   OXT  O N N 388 
TYR   H    H N N 389 
TYR   H2   H N N 390 
TYR   HA   H N N 391 
TYR   HB2  H N N 392 
TYR   HB3  H N N 393 
TYR   HD1  H N N 394 
TYR   HD2  H N N 395 
TYR   HE1  H N N 396 
TYR   HE2  H N N 397 
TYR   HH   H N N 398 
TYR   HXT  H N N 399 
VAL   N    N N N 400 
VAL   CA   C N S 401 
VAL   C    C N N 402 
VAL   O    O N N 403 
VAL   CB   C N N 404 
VAL   CG1  C N N 405 
VAL   CG2  C N N 406 
VAL   OXT  O N N 407 
VAL   H    H N N 408 
VAL   H2   H N N 409 
VAL   HA   H N N 410 
VAL   HB   H N N 411 
VAL   HG11 H N N 412 
VAL   HG12 H N N 413 
VAL   HG13 H N N 414 
VAL   HG21 H N N 415 
VAL   HG22 H N N 416 
VAL   HG23 H N N 417 
VAL   HXT  H N N 418 
# 
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 
A1LZO O07 C02  sing N N 1   
A1LZO O16 N11  doub N N 2   
A1LZO C02 C01  doub Y N 3   
A1LZO C02 C03  sing Y N 4   
A1LZO C01 C06  sing Y N 5   
A1LZO N11 C03  sing N N 6   
A1LZO N11 O15  doub N N 7   
A1LZO C03 C04  doub Y N 8   
A1LZO C06 C05  doub Y N 9   
A1LZO C04 C05  sing Y N 10  
A1LZO C05 C09  sing N N 11  
A1LZO C09 C10  sing N N 12  
A1LZO C10 O17  doub N N 13  
A1LZO C10 N12  sing N N 14  
A1LZO N12 C18  sing N N 15  
A1LZO C18 C08  sing N N 16  
A1LZO O13 C08  doub N N 17  
A1LZO C08 O14  sing N N 18  
A1LZO N12 H121 sing N N 19  
A1LZO C01 H011 sing N N 20  
A1LZO C04 H041 sing N N 21  
A1LZO C06 H061 sing N N 22  
A1LZO C09 H091 sing N N 23  
A1LZO C09 H092 sing N N 24  
A1LZO C18 H182 sing N N 25  
A1LZO C18 H181 sing N N 26  
A1LZO O07 H071 sing N N 27  
A1LZO O14 H1   sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
GLN   N   CA   sing N N 111 
GLN   N   H    sing N N 112 
GLN   N   H2   sing N N 113 
GLN   CA  C    sing N N 114 
GLN   CA  CB   sing N N 115 
GLN   CA  HA   sing N N 116 
GLN   C   O    doub N N 117 
GLN   C   OXT  sing N N 118 
GLN   CB  CG   sing N N 119 
GLN   CB  HB2  sing N N 120 
GLN   CB  HB3  sing N N 121 
GLN   CG  CD   sing N N 122 
GLN   CG  HG2  sing N N 123 
GLN   CG  HG3  sing N N 124 
GLN   CD  OE1  doub N N 125 
GLN   CD  NE2  sing N N 126 
GLN   NE2 HE21 sing N N 127 
GLN   NE2 HE22 sing N N 128 
GLN   OXT HXT  sing N N 129 
GLU   N   CA   sing N N 130 
GLU   N   H    sing N N 131 
GLU   N   H2   sing N N 132 
GLU   CA  C    sing N N 133 
GLU   CA  CB   sing N N 134 
GLU   CA  HA   sing N N 135 
GLU   C   O    doub N N 136 
GLU   C   OXT  sing N N 137 
GLU   CB  CG   sing N N 138 
GLU   CB  HB2  sing N N 139 
GLU   CB  HB3  sing N N 140 
GLU   CG  CD   sing N N 141 
GLU   CG  HG2  sing N N 142 
GLU   CG  HG3  sing N N 143 
GLU   CD  OE1  doub N N 144 
GLU   CD  OE2  sing N N 145 
GLU   OE2 HE2  sing N N 146 
GLU   OXT HXT  sing N N 147 
GLY   N   CA   sing N N 148 
GLY   N   H    sing N N 149 
GLY   N   H2   sing N N 150 
GLY   CA  C    sing N N 151 
GLY   CA  HA2  sing N N 152 
GLY   CA  HA3  sing N N 153 
GLY   C   O    doub N N 154 
GLY   C   OXT  sing N N 155 
GLY   OXT HXT  sing N N 156 
HIS   N   CA   sing N N 157 
HIS   N   H    sing N N 158 
HIS   N   H2   sing N N 159 
HIS   CA  C    sing N N 160 
HIS   CA  CB   sing N N 161 
HIS   CA  HA   sing N N 162 
HIS   C   O    doub N N 163 
HIS   C   OXT  sing N N 164 
HIS   CB  CG   sing N N 165 
HIS   CB  HB2  sing N N 166 
HIS   CB  HB3  sing N N 167 
HIS   CG  ND1  sing Y N 168 
HIS   CG  CD2  doub Y N 169 
HIS   ND1 CE1  doub Y N 170 
HIS   ND1 HD1  sing N N 171 
HIS   CD2 NE2  sing Y N 172 
HIS   CD2 HD2  sing N N 173 
HIS   CE1 NE2  sing Y N 174 
HIS   CE1 HE1  sing N N 175 
HIS   NE2 HE2  sing N N 176 
HIS   OXT HXT  sing N N 177 
HOH   O   H1   sing N N 178 
HOH   O   H2   sing N N 179 
ILE   N   CA   sing N N 180 
ILE   N   H    sing N N 181 
ILE   N   H2   sing N N 182 
ILE   CA  C    sing N N 183 
ILE   CA  CB   sing N N 184 
ILE   CA  HA   sing N N 185 
ILE   C   O    doub N N 186 
ILE   C   OXT  sing N N 187 
ILE   CB  CG1  sing N N 188 
ILE   CB  CG2  sing N N 189 
ILE   CB  HB   sing N N 190 
ILE   CG1 CD1  sing N N 191 
ILE   CG1 HG12 sing N N 192 
ILE   CG1 HG13 sing N N 193 
ILE   CG2 HG21 sing N N 194 
ILE   CG2 HG22 sing N N 195 
ILE   CG2 HG23 sing N N 196 
ILE   CD1 HD11 sing N N 197 
ILE   CD1 HD12 sing N N 198 
ILE   CD1 HD13 sing N N 199 
ILE   OXT HXT  sing N N 200 
LEU   N   CA   sing N N 201 
LEU   N   H    sing N N 202 
LEU   N   H2   sing N N 203 
LEU   CA  C    sing N N 204 
LEU   CA  CB   sing N N 205 
LEU   CA  HA   sing N N 206 
LEU   C   O    doub N N 207 
LEU   C   OXT  sing N N 208 
LEU   CB  CG   sing N N 209 
LEU   CB  HB2  sing N N 210 
LEU   CB  HB3  sing N N 211 
LEU   CG  CD1  sing N N 212 
LEU   CG  CD2  sing N N 213 
LEU   CG  HG   sing N N 214 
LEU   CD1 HD11 sing N N 215 
LEU   CD1 HD12 sing N N 216 
LEU   CD1 HD13 sing N N 217 
LEU   CD2 HD21 sing N N 218 
LEU   CD2 HD22 sing N N 219 
LEU   CD2 HD23 sing N N 220 
LEU   OXT HXT  sing N N 221 
LYS   N   CA   sing N N 222 
LYS   N   H    sing N N 223 
LYS   N   H2   sing N N 224 
LYS   CA  C    sing N N 225 
LYS   CA  CB   sing N N 226 
LYS   CA  HA   sing N N 227 
LYS   C   O    doub N N 228 
LYS   C   OXT  sing N N 229 
LYS   CB  CG   sing N N 230 
LYS   CB  HB2  sing N N 231 
LYS   CB  HB3  sing N N 232 
LYS   CG  CD   sing N N 233 
LYS   CG  HG2  sing N N 234 
LYS   CG  HG3  sing N N 235 
LYS   CD  CE   sing N N 236 
LYS   CD  HD2  sing N N 237 
LYS   CD  HD3  sing N N 238 
LYS   CE  NZ   sing N N 239 
LYS   CE  HE2  sing N N 240 
LYS   CE  HE3  sing N N 241 
LYS   NZ  HZ1  sing N N 242 
LYS   NZ  HZ2  sing N N 243 
LYS   NZ  HZ3  sing N N 244 
LYS   OXT HXT  sing N N 245 
MET   N   CA   sing N N 246 
MET   N   H    sing N N 247 
MET   N   H2   sing N N 248 
MET   CA  C    sing N N 249 
MET   CA  CB   sing N N 250 
MET   CA  HA   sing N N 251 
MET   C   O    doub N N 252 
MET   C   OXT  sing N N 253 
MET   CB  CG   sing N N 254 
MET   CB  HB2  sing N N 255 
MET   CB  HB3  sing N N 256 
MET   CG  SD   sing N N 257 
MET   CG  HG2  sing N N 258 
MET   CG  HG3  sing N N 259 
MET   SD  CE   sing N N 260 
MET   CE  HE1  sing N N 261 
MET   CE  HE2  sing N N 262 
MET   CE  HE3  sing N N 263 
MET   OXT HXT  sing N N 264 
PHE   N   CA   sing N N 265 
PHE   N   H    sing N N 266 
PHE   N   H2   sing N N 267 
PHE   CA  C    sing N N 268 
PHE   CA  CB   sing N N 269 
PHE   CA  HA   sing N N 270 
PHE   C   O    doub N N 271 
PHE   C   OXT  sing N N 272 
PHE   CB  CG   sing N N 273 
PHE   CB  HB2  sing N N 274 
PHE   CB  HB3  sing N N 275 
PHE   CG  CD1  doub Y N 276 
PHE   CG  CD2  sing Y N 277 
PHE   CD1 CE1  sing Y N 278 
PHE   CD1 HD1  sing N N 279 
PHE   CD2 CE2  doub Y N 280 
PHE   CD2 HD2  sing N N 281 
PHE   CE1 CZ   doub Y N 282 
PHE   CE1 HE1  sing N N 283 
PHE   CE2 CZ   sing Y N 284 
PHE   CE2 HE2  sing N N 285 
PHE   CZ  HZ   sing N N 286 
PHE   OXT HXT  sing N N 287 
PRO   N   CA   sing N N 288 
PRO   N   CD   sing N N 289 
PRO   N   H    sing N N 290 
PRO   CA  C    sing N N 291 
PRO   CA  CB   sing N N 292 
PRO   CA  HA   sing N N 293 
PRO   C   O    doub N N 294 
PRO   C   OXT  sing N N 295 
PRO   CB  CG   sing N N 296 
PRO   CB  HB2  sing N N 297 
PRO   CB  HB3  sing N N 298 
PRO   CG  CD   sing N N 299 
PRO   CG  HG2  sing N N 300 
PRO   CG  HG3  sing N N 301 
PRO   CD  HD2  sing N N 302 
PRO   CD  HD3  sing N N 303 
PRO   OXT HXT  sing N N 304 
SER   N   CA   sing N N 305 
SER   N   H    sing N N 306 
SER   N   H2   sing N N 307 
SER   CA  C    sing N N 308 
SER   CA  CB   sing N N 309 
SER   CA  HA   sing N N 310 
SER   C   O    doub N N 311 
SER   C   OXT  sing N N 312 
SER   CB  OG   sing N N 313 
SER   CB  HB2  sing N N 314 
SER   CB  HB3  sing N N 315 
SER   OG  HG   sing N N 316 
SER   OXT HXT  sing N N 317 
THR   N   CA   sing N N 318 
THR   N   H    sing N N 319 
THR   N   H2   sing N N 320 
THR   CA  C    sing N N 321 
THR   CA  CB   sing N N 322 
THR   CA  HA   sing N N 323 
THR   C   O    doub N N 324 
THR   C   OXT  sing N N 325 
THR   CB  OG1  sing N N 326 
THR   CB  CG2  sing N N 327 
THR   CB  HB   sing N N 328 
THR   OG1 HG1  sing N N 329 
THR   CG2 HG21 sing N N 330 
THR   CG2 HG22 sing N N 331 
THR   CG2 HG23 sing N N 332 
THR   OXT HXT  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   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1LZO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1LZO 
_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        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6K4Z 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YTP 
_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]   0.028027 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016281 
_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]   0.011259 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA   A 1 5   ? 23.039  4.148   -16.848 1.00 42.70 ? 5   ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 5   ? 22.292  3.734   -15.657 1.00 40.13 ? 5   ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 5   ? 22.144  2.218   -15.589 1.00 38.56 ? 5   ALA   A C   1 
ATOM   4    O O   . ALA   A 1 5   ? 21.749  1.574   -16.571 1.00 40.08 ? 5   ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 5   ? 20.931  4.388   -15.638 1.00 40.02 ? 5   ALA   A CB  1 
ATOM   6    N N   . VAL   A 1 6   ? 22.468  1.641   -14.435 1.00 34.65 ? 6   VAL   A N   1 
ATOM   7    C CA  . VAL   A 1 6   ? 22.405  0.196   -14.214 1.00 31.26 ? 6   VAL   A CA  1 
ATOM   8    C C   . VAL   A 1 6   ? 21.405  -0.084  -13.092 1.00 25.32 ? 6   VAL   A C   1 
ATOM   9    O O   . VAL   A 1 6   ? 21.423  0.579   -12.049 1.00 26.80 ? 6   VAL   A O   1 
ATOM   10   C CB  . VAL   A 1 6   ? 23.801  -0.390  -13.901 1.00 34.61 ? 6   VAL   A CB  1 
ATOM   11   C CG1 . VAL   A 1 6   ? 23.715  -1.878  -13.548 1.00 33.64 ? 6   VAL   A CG1 1 
ATOM   12   C CG2 . VAL   A 1 6   ? 24.767  -0.189  -15.100 1.00 34.51 ? 6   VAL   A CG2 1 
ATOM   13   N N   . VAL   A 1 7   ? 20.518  -1.050  -13.299 1.00 20.98 ? 7   VAL   A N   1 
ATOM   14   C CA  . VAL   A 1 7   ? 19.461  -1.348  -12.333 1.00 17.55 ? 7   VAL   A CA  1 
ATOM   15   C C   . VAL   A 1 7   ? 19.782  -2.724  -11.756 1.00 17.38 ? 7   VAL   A C   1 
ATOM   16   O O   . VAL   A 1 7   ? 19.928  -3.688  -12.522 1.00 17.75 ? 7   VAL   A O   1 
ATOM   17   C CB  . VAL   A 1 7   ? 18.089  -1.380  -13.025 1.00 18.65 ? 7   VAL   A CB  1 
ATOM   18   C CG1 . VAL   A 1 7   ? 17.015  -1.778  -12.021 1.00 19.17 ? 7   VAL   A CG1 1 
ATOM   19   C CG2 . VAL   A 1 7   ? 17.729  -0.010  -13.699 1.00 22.30 ? 7   VAL   A CG2 1 
ATOM   20   N N   . THR   A 1 8   ? 19.889  -2.830  -10.417 1.00 17.38 ? 8   THR   A N   1 
ATOM   21   C CA  A THR   A 1 8   ? 20.313  -4.052  -9.740  0.57 17.71 ? 8   THR   A CA  1 
ATOM   22   C CA  B THR   A 1 8   ? 20.285  -4.081  -9.783  0.43 16.85 ? 8   THR   A CA  1 
ATOM   23   C C   . THR   A 1 8   ? 19.198  -4.634  -8.874  1.00 15.95 ? 8   THR   A C   1 
ATOM   24   O O   . THR   A 1 8   ? 18.551  -3.904  -8.109  1.00 16.30 ? 8   THR   A O   1 
ATOM   25   C CB  A THR   A 1 8   ? 21.578  -3.775  -8.892  0.57 20.57 ? 8   THR   A CB  1 
ATOM   26   C CB  B THR   A 1 8   ? 21.603  -3.968  -9.012  0.43 17.45 ? 8   THR   A CB  1 
ATOM   27   O OG1 A THR   A 1 8   ? 22.611  -3.219  -9.716  0.57 23.61 ? 8   THR   A OG1 1 
ATOM   28   O OG1 B THR   A 1 8   ? 21.450  -3.002  -7.975  0.43 18.07 ? 8   THR   A OG1 1 
ATOM   29   C CG2 A THR   A 1 8   ? 22.099  -5.042  -8.295  0.57 22.99 ? 8   THR   A CG2 1 
ATOM   30   C CG2 B THR   A 1 8   ? 22.744  -3.559  -9.942  0.43 18.22 ? 8   THR   A CG2 1 
ATOM   31   N N   . GLN   A 1 9   ? 19.033  -5.954  -8.968  1.00 14.43 ? 9   GLN   A N   1 
ATOM   32   C CA  . GLN   A 1 9   ? 18.096  -6.756  -8.179  1.00 14.69 ? 9   GLN   A CA  1 
ATOM   33   C C   . GLN   A 1 9   ? 18.863  -7.911  -7.570  1.00 14.81 ? 9   GLN   A C   1 
ATOM   34   O O   . GLN   A 1 9   ? 19.881  -8.343  -8.109  1.00 16.04 ? 9   GLN   A O   1 
ATOM   35   C CB  . GLN   A 1 9   ? 16.995  -7.338  -9.072  1.00 14.33 ? 9   GLN   A CB  1 
ATOM   36   C CG  . GLN   A 1 9   ? 16.156  -6.244  -9.756  1.00 14.78 ? 9   GLN   A CG  1 
ATOM   37   C CD  . GLN   A 1 9   ? 15.068  -6.872  -10.607 1.00 14.32 ? 9   GLN   A CD  1 
ATOM   38   O OE1 . GLN   A 1 9   ? 15.112  -6.797  -11.836 1.00 14.03 ? 9   GLN   A OE1 1 
ATOM   39   N NE2 . GLN   A 1 9   ? 14.083  -7.501  -9.954  1.00 16.03 ? 9   GLN   A NE2 1 
ATOM   40   N N   . GLU   A 1 10  ? 18.330  -8.476  -6.485  1.00 15.17 ? 10  GLU   A N   1 
ATOM   41   C CA  . GLU   A 1 10  ? 18.861  -9.731  -5.944  1.00 14.78 ? 10  GLU   A CA  1 
ATOM   42   C C   . GLU   A 1 10  ? 18.814  -10.806 -7.028  1.00 15.69 ? 10  GLU   A C   1 
ATOM   43   O O   . GLU   A 1 10  ? 17.801  -10.974 -7.708  1.00 16.99 ? 10  GLU   A O   1 
ATOM   44   C CB  . GLU   A 1 10  ? 17.990  -10.188 -4.758  1.00 15.78 ? 10  GLU   A CB  1 
ATOM   45   C CG  . GLU   A 1 10  ? 18.056  -9.288  -3.542  1.00 17.55 ? 10  GLU   A CG  1 
ATOM   46   C CD  . GLU   A 1 10  ? 17.012  -8.176  -3.547  1.00 18.13 ? 10  GLU   A CD  1 
ATOM   47   O OE1 . GLU   A 1 10  ? 16.227  -8.038  -4.540  1.00 16.83 ? 10  GLU   A OE1 1 
ATOM   48   O OE2 . GLU   A 1 10  ? 16.983  -7.444  -2.550  1.00 18.90 ? 10  GLU   A OE2 1 
ATOM   49   N N   . SER   A 1 11  ? 19.885  -11.586 -7.176  1.00 13.92 ? 11  SER   A N   1 
ATOM   50   C CA  A SER   A 1 11  ? 19.867  -12.616 -8.212  0.68 13.52 ? 11  SER   A CA  1 
ATOM   51   C CA  B SER   A 1 11  ? 19.875  -12.618 -8.209  0.32 14.17 ? 11  SER   A CA  1 
ATOM   52   C C   . SER   A 1 11  ? 18.822  -13.685 -7.913  1.00 14.47 ? 11  SER   A C   1 
ATOM   53   O O   . SER   A 1 11  ? 18.121  -14.158 -8.830  1.00 15.17 ? 11  SER   A O   1 
ATOM   54   C CB  A SER   A 1 11  ? 21.259  -13.242 -8.377  0.68 16.13 ? 11  SER   A CB  1 
ATOM   55   C CB  B SER   A 1 11  ? 21.271  -13.239 -8.345  0.32 15.97 ? 11  SER   A CB  1 
ATOM   56   O OG  A SER   A 1 11  ? 22.121  -12.286 -8.955  0.68 18.52 ? 11  SER   A OG  1 
ATOM   57   O OG  B SER   A 1 11  ? 21.288  -14.262 -9.320  0.32 18.08 ? 11  SER   A OG  1 
ATOM   58   N N   . ALA   A 1 12  ? 18.710  -14.106 -6.643  1.00 13.97 ? 12  ALA   A N   1 
ATOM   59   C CA  . ALA   A 1 12  ? 17.752  -15.145 -6.267  1.00 14.13 ? 12  ALA   A CA  1 
ATOM   60   C C   . ALA   A 1 12  ? 17.336  -14.911 -4.831  1.00 13.86 ? 12  ALA   A C   1 
ATOM   61   O O   . ALA   A 1 12  ? 18.104  -14.385 -4.021  1.00 15.76 ? 12  ALA   A O   1 
ATOM   62   C CB  . ALA   A 1 12  ? 18.402  -16.545 -6.361  1.00 16.49 ? 12  ALA   A CB  1 
ATOM   63   N N   . LEU   A 1 13  ? 16.111  -15.323 -4.513  1.00 13.76 ? 13  LEU   A N   1 
ATOM   64   C CA  . LEU   A 1 13  ? 15.642  -15.360 -3.133  1.00 14.01 ? 13  LEU   A CA  1 
ATOM   65   C C   . LEU   A 1 13  ? 14.840  -16.630 -2.974  1.00 14.17 ? 13  LEU   A C   1 
ATOM   66   O O   . LEU   A 1 13  ? 14.191  -17.073 -3.918  1.00 16.32 ? 13  LEU   A O   1 
ATOM   67   C CB  . LEU   A 1 13  ? 14.723  -14.151 -2.794  1.00 15.98 ? 13  LEU   A CB  1 
ATOM   68   C CG  . LEU   A 1 13  ? 15.421  -12.797 -2.782  1.00 17.14 ? 13  LEU   A CG  1 
ATOM   69   C CD1 . LEU   A 1 13  ? 14.378  -11.703 -2.592  1.00 17.12 ? 13  LEU   A CD1 1 
ATOM   70   C CD2 . LEU   A 1 13  ? 16.466  -12.670 -1.668  1.00 19.05 ? 13  LEU   A CD2 1 
ATOM   71   N N   . THR   A 1 14  ? 14.870  -17.216 -1.774  1.00 14.66 ? 14  THR   A N   1 
ATOM   72   C CA  . THR   A 1 14  ? 14.096  -18.412 -1.484  1.00 15.04 ? 14  THR   A CA  1 
ATOM   73   C C   . THR   A 1 14  ? 13.113  -18.129 -0.361  1.00 15.83 ? 14  THR   A C   1 
ATOM   74   O O   . THR   A 1 14  ? 13.455  -17.496 0.644   1.00 16.56 ? 14  THR   A O   1 
ATOM   75   C CB  . THR   A 1 14  ? 15.031  -19.560 -1.044  1.00 16.85 ? 14  THR   A CB  1 
ATOM   76   O OG1 . THR   A 1 14  ? 15.973  -19.863 -2.073  1.00 19.05 ? 14  THR   A OG1 1 
ATOM   77   C CG2 . THR   A 1 14  ? 14.234  -20.847 -0.748  1.00 17.55 ? 14  THR   A CG2 1 
ATOM   78   N N   . THR   A 1 15  ? 11.886  -18.601 -0.544  1.00 16.14 ? 15  THR   A N   1 
ATOM   79   C CA  . THR   A 1 15  ? 10.831  -18.401 0.432   1.00 16.36 ? 15  THR   A CA  1 
ATOM   80   C C   . THR   A 1 15  ? 10.041  -19.700 0.544   1.00 17.43 ? 15  THR   A C   1 
ATOM   81   O O   . THR   A 1 15  ? 10.386  -20.716 -0.070  1.00 17.80 ? 15  THR   A O   1 
ATOM   82   C CB  . THR   A 1 15  ? 9.973   -17.162 0.078   1.00 20.01 ? 15  THR   A CB  1 
ATOM   83   O OG1 . THR   A 1 15  ? 9.079   -16.880 1.167   1.00 22.00 ? 15  THR   A OG1 1 
ATOM   84   C CG2 . THR   A 1 15  ? 9.135   -17.370 -1.228  1.00 19.40 ? 15  THR   A CG2 1 
ATOM   85   N N   . SER   A 1 16  ? 8.993   -19.683 1.361   1.00 17.59 ? 16  SER   A N   1 
ATOM   86   C CA  A SER   A 1 16  ? 8.078   -20.804 1.462   0.43 17.59 ? 16  SER   A CA  1 
ATOM   87   C CA  B SER   A 1 16  ? 8.075   -20.797 1.529   0.57 17.08 ? 16  SER   A CA  1 
ATOM   88   C C   . SER   A 1 16  ? 6.662   -20.261 1.421   1.00 16.26 ? 16  SER   A C   1 
ATOM   89   O O   . SER   A 1 16  ? 6.432   -19.061 1.642   1.00 16.75 ? 16  SER   A O   1 
ATOM   90   C CB  A SER   A 1 16  ? 8.303   -21.636 2.739   0.43 21.28 ? 16  SER   A CB  1 
ATOM   91   C CB  B SER   A 1 16  ? 8.248   -21.417 2.922   0.57 19.55 ? 16  SER   A CB  1 
ATOM   92   O OG  A SER   A 1 16  ? 8.194   -20.878 3.927   0.43 23.93 ? 16  SER   A OG  1 
ATOM   93   O OG  B SER   A 1 16  ? 9.522   -21.990 3.072   0.57 21.06 ? 16  SER   A OG  1 
ATOM   94   N N   . PRO   A 1 17  ? 5.680   -21.127 1.132   1.00 16.08 ? 17  PRO   A N   1 
ATOM   95   C CA  . PRO   A 1 17  ? 4.294   -20.668 1.085   1.00 14.95 ? 17  PRO   A CA  1 
ATOM   96   C C   . PRO   A 1 17  ? 3.916   -20.055 2.421   1.00 14.70 ? 17  PRO   A C   1 
ATOM   97   O O   . PRO   A 1 17  ? 4.201   -20.622 3.485   1.00 15.87 ? 17  PRO   A O   1 
ATOM   98   C CB  . PRO   A 1 17  ? 3.502   -21.946 0.753   1.00 18.27 ? 17  PRO   A CB  1 
ATOM   99   C CG  . PRO   A 1 17  ? 4.445   -22.785 0.058   1.00 19.21 ? 17  PRO   A CG  1 
ATOM   100  C CD  . PRO   A 1 17  ? 5.797   -22.523 0.674   1.00 19.41 ? 17  PRO   A CD  1 
ATOM   101  N N   . GLY   A 1 18  ? 3.245   -18.900 2.349   1.00 15.26 ? 18  GLY   A N   1 
ATOM   102  C CA  . GLY   A 1 18  ? 2.798   -18.206 3.540   1.00 15.91 ? 18  GLY   A CA  1 
ATOM   103  C C   . GLY   A 1 18  ? 3.763   -17.180 4.103   1.00 15.01 ? 18  GLY   A C   1 
ATOM   104  O O   . GLY   A 1 18  ? 3.387   -16.469 5.054   1.00 16.46 ? 18  GLY   A O   1 
ATOM   105  N N   . GLU   A 1 19  ? 5.007   -17.109 3.608   1.00 14.58 ? 19  GLU   A N   1 
ATOM   106  C CA  . GLU   A 1 19  ? 5.929   -16.113 4.117   1.00 15.63 ? 19  GLU   A CA  1 
ATOM   107  C C   . GLU   A 1 19  ? 5.743   -14.775 3.385   1.00 15.42 ? 19  GLU   A C   1 
ATOM   108  O O   . GLU   A 1 19  ? 5.056   -14.678 2.365   1.00 17.06 ? 19  GLU   A O   1 
ATOM   109  C CB  . GLU   A 1 19  ? 7.366   -16.615 3.984   1.00 16.85 ? 19  GLU   A CB  1 
ATOM   110  C CG  . GLU   A 1 19  ? 7.688   -17.875 4.802   1.00 21.30 ? 19  GLU   A CG  1 
ATOM   111  C CD  . GLU   A 1 19  ? 7.423   -17.680 6.315   1.00 26.75 ? 19  GLU   A CD  1 
ATOM   112  O OE1 . GLU   A 1 19  ? 7.924   -16.686 6.889   1.00 33.01 ? 19  GLU   A OE1 1 
ATOM   113  O OE2 . GLU   A 1 19  ? 6.681   -18.504 6.931   1.00 29.32 ? 19  GLU   A OE2 1 
ATOM   114  N N   . THR   A 1 20  ? 6.337   -13.709 3.934   1.00 15.17 ? 20  THR   A N   1 
ATOM   115  C CA  . THR   A 1 20  ? 6.301   -12.402 3.302   1.00 16.30 ? 20  THR   A CA  1 
ATOM   116  C C   . THR   A 1 20  ? 7.674   -12.146 2.717   1.00 15.50 ? 20  THR   A C   1 
ATOM   117  O O   . THR   A 1 20  ? 8.684   -12.269 3.427   1.00 18.02 ? 20  THR   A O   1 
ATOM   118  C CB  . THR   A 1 20  ? 5.962   -11.345 4.353   1.00 18.94 ? 20  THR   A CB  1 
ATOM   119  O OG1 . THR   A 1 20  ? 4.626   -11.624 4.817   1.00 21.77 ? 20  THR   A OG1 1 
ATOM   120  C CG2 . THR   A 1 20  ? 6.010   -9.949  3.771   1.00 19.71 ? 20  THR   A CG2 1 
ATOM   121  N N   . VAL   A 1 21  ? 7.728   -11.824 1.423   1.00 15.09 ? 21  VAL   A N   1 
ATOM   122  C CA  A VAL   A 1 21  ? 8.984   -11.636 0.706   0.53 15.99 ? 21  VAL   A CA  1 
ATOM   123  C CA  B VAL   A 1 21  ? 8.999   -11.615 0.758   0.47 16.22 ? 21  VAL   A CA  1 
ATOM   124  C C   . VAL   A 1 21  ? 9.024   -10.240 0.119   1.00 14.51 ? 21  VAL   A C   1 
ATOM   125  O O   . VAL   A 1 21  ? 8.021   -9.774  -0.434  1.00 15.48 ? 21  VAL   A O   1 
ATOM   126  C CB  A VAL   A 1 21  ? 9.158   -12.638 -0.458  0.53 19.94 ? 21  VAL   A CB  1 
ATOM   127  C CB  B VAL   A 1 21  ? 9.342   -12.749 -0.237  0.47 20.27 ? 21  VAL   A CB  1 
ATOM   128  C CG1 A VAL   A 1 21  ? 10.651  -12.772 -0.827  0.53 18.59 ? 21  VAL   A CG1 1 
ATOM   129  C CG1 B VAL   A 1 21  ? 8.294   -12.866 -1.311  0.47 19.84 ? 21  VAL   A CG1 1 
ATOM   130  C CG2 A VAL   A 1 21  ? 8.506   -13.979 -0.174  0.53 23.15 ? 21  VAL   A CG2 1 
ATOM   131  C CG2 B VAL   A 1 21  ? 10.717  -12.524 -0.882  0.47 22.37 ? 21  VAL   A CG2 1 
ATOM   132  N N   . THR   A 1 22  ? 10.170  -9.587  0.245   1.00 14.10 ? 22  THR   A N   1 
ATOM   133  C CA  . THR   A 1 22  ? 10.404  -8.308  -0.404  1.00 14.34 ? 22  THR   A CA  1 
ATOM   134  C C   . THR   A 1 22  ? 11.515  -8.475  -1.442  1.00 13.47 ? 22  THR   A C   1 
ATOM   135  O O   . THR   A 1 22  ? 12.541  -9.088  -1.167  1.00 16.07 ? 22  THR   A O   1 
ATOM   136  C CB  . THR   A 1 22  ? 10.726  -7.216  0.618   1.00 18.11 ? 22  THR   A CB  1 
ATOM   137  O OG1 . THR   A 1 22  ? 11.805  -7.666  1.424   1.00 23.02 ? 22  THR   A OG1 1 
ATOM   138  C CG2 . THR   A 1 22  ? 9.520   -6.907  1.520   1.00 16.78 ? 22  THR   A CG2 1 
ATOM   139  N N   . LEU   A 1 23  ? 11.294  -7.942  -2.632  1.00 12.95 ? 23  LEU   A N   1 
ATOM   140  C CA  . LEU   A 1 23  ? 12.260  -7.943  -3.728  1.00 13.96 ? 23  LEU   A CA  1 
ATOM   141  C C   . LEU   A 1 23  ? 12.635  -6.492  -3.957  1.00 13.37 ? 23  LEU   A C   1 
ATOM   142  O O   . LEU   A 1 23  ? 11.754  -5.633  -3.936  1.00 15.01 ? 23  LEU   A O   1 
ATOM   143  C CB  . LEU   A 1 23  ? 11.601  -8.533  -4.990  1.00 16.38 ? 23  LEU   A CB  1 
ATOM   144  C CG  . LEU   A 1 23  ? 11.226  -10.015 -4.863  1.00 19.62 ? 23  LEU   A CG  1 
ATOM   145  C CD1 . LEU   A 1 23  ? 9.863   -10.198 -4.190  1.00 25.15 ? 23  LEU   A CD1 1 
ATOM   146  C CD2 . LEU   A 1 23  ? 11.223  -10.634 -6.262  1.00 24.01 ? 23  LEU   A CD2 1 
ATOM   147  N N   . THR   A 1 24  ? 13.933  -6.203  -4.092  1.00 14.11 ? 24  THR   A N   1 
ATOM   148  C CA  . THR   A 1 24  ? 14.377  -4.820  -4.201  1.00 14.33 ? 24  THR   A CA  1 
ATOM   149  C C   . THR   A 1 24  ? 15.006  -4.506  -5.548  1.00 14.32 ? 24  THR   A C   1 
ATOM   150  O O   . THR   A 1 24  ? 15.483  -5.380  -6.287  1.00 14.68 ? 24  THR   A O   1 
ATOM   151  C CB  . THR   A 1 24  ? 15.302  -4.369  -3.058  1.00 16.44 ? 24  THR   A CB  1 
ATOM   152  O OG1 . THR   A 1 24  ? 16.567  -5.020  -3.169  1.00 17.51 ? 24  THR   A OG1 1 
ATOM   153  C CG2 . THR   A 1 24  ? 14.692  -4.697  -1.716  1.00 18.25 ? 24  THR   A CG2 1 
ATOM   154  N N   . CYS   A 1 25  ? 15.060  -3.213  -5.851  1.00 14.22 ? 25  CYS   A N   1 
ATOM   155  C CA  . CYS   A 1 25  ? 15.474  -2.754  -7.169  1.00 16.67 ? 25  CYS   A CA  1 
ATOM   156  C C   . CYS   A 1 25  ? 16.173  -1.421  -6.939  1.00 16.53 ? 25  CYS   A C   1 
ATOM   157  O O   . CYS   A 1 25  ? 15.539  -0.481  -6.457  1.00 18.68 ? 25  CYS   A O   1 
ATOM   158  C CB  . CYS   A 1 25  ? 14.223  -2.612  -8.038  1.00 17.93 ? 25  CYS   A CB  1 
ATOM   159  S SG  . CYS   A 1 25  ? 14.417  -1.855  -9.644  1.00 18.32 ? 25  CYS   A SG  1 
ATOM   160  N N   . ARG   A 1 26  ? 17.477  -1.349  -7.227  1.00 16.69 ? 26  ARG   A N   1 
ATOM   161  C CA  A ARG   A 1 26  ? 18.248  -0.135  -7.011  0.51 18.78 ? 26  ARG   A CA  1 
ATOM   162  C CA  B ARG   A 1 26  ? 18.310  -0.179  -6.994  0.49 18.06 ? 26  ARG   A CA  1 
ATOM   163  C C   . ARG   A 1 26  ? 18.768  0.438   -8.312  1.00 19.84 ? 26  ARG   A C   1 
ATOM   164  O O   . ARG   A 1 26  ? 19.055  -0.279  -9.277  1.00 19.91 ? 26  ARG   A O   1 
ATOM   165  C CB  A ARG   A 1 26  ? 19.485  -0.278  -6.137  0.51 22.18 ? 26  ARG   A CB  1 
ATOM   166  C CB  B ARG   A 1 26  ? 19.512  -0.520  -6.096  0.49 20.00 ? 26  ARG   A CB  1 
ATOM   167  C CG  A ARG   A 1 26  ? 19.417  -1.041  -4.871  0.51 28.03 ? 26  ARG   A CG  1 
ATOM   168  C CG  B ARG   A 1 26  ? 20.844  0.052   -6.564  0.49 25.40 ? 26  ARG   A CG  1 
ATOM   169  C CD  A ARG   A 1 26  ? 20.761  -0.774  -4.203  0.51 32.99 ? 26  ARG   A CD  1 
ATOM   170  C CD  B ARG   A 1 26  ? 21.891  0.029   -5.458  0.49 30.93 ? 26  ARG   A CD  1 
ATOM   171  N NE  A ARG   A 1 26  ? 21.784  -1.716  -4.646  0.51 36.38 ? 26  ARG   A NE  1 
ATOM   172  N NE  B ARG   A 1 26  ? 23.202  0.456   -5.941  0.49 34.64 ? 26  ARG   A NE  1 
ATOM   173  C CZ  A ARG   A 1 26  ? 22.775  -1.433  -5.481  0.51 38.11 ? 26  ARG   A CZ  1 
ATOM   174  C CZ  B ARG   A 1 26  ? 23.608  1.717   -5.994  0.49 37.89 ? 26  ARG   A CZ  1 
ATOM   175  N NH1 A ARG   A 1 26  ? 22.919  -0.227  -6.005  0.51 38.62 ? 26  ARG   A NH1 1 
ATOM   176  N NH1 B ARG   A 1 26  ? 22.823  2.713   -5.620  0.49 37.60 ? 26  ARG   A NH1 1 
ATOM   177  N NH2 A ARG   A 1 26  ? 23.644  -2.388  -5.801  0.51 38.80 ? 26  ARG   A NH2 1 
ATOM   178  N NH2 B ARG   A 1 26  ? 24.833  1.986   -6.437  0.49 40.75 ? 26  ARG   A NH2 1 
ATOM   179  N N   . SER   A 1 27  ? 18.880  1.761   -8.313  1.00 20.71 ? 27  SER   A N   1 
ATOM   180  C CA  . SER   A 1 27  ? 19.433  2.507   -9.432  1.00 22.68 ? 27  SER   A CA  1 
ATOM   181  C C   . SER   A 1 27  ? 20.885  2.869   -9.140  1.00 24.64 ? 27  SER   A C   1 
ATOM   182  O O   . SER   A 1 27  ? 21.232  3.206   -8.004  1.00 25.57 ? 27  SER   A O   1 
ATOM   183  C CB  . SER   A 1 27  ? 18.611  3.788   -9.637  1.00 25.88 ? 27  SER   A CB  1 
ATOM   184  O OG  . SER   A 1 27  ? 19.193  4.625   -10.623 1.00 27.03 ? 27  SER   A OG  1 
ATOM   185  N N   . SER   A 1 28  ? 21.729  2.836   -10.178 1.00 26.67 ? 28  SER   A N   1 
ATOM   186  C CA  . SER   A 1 28  ? 23.110  3.263   -10.016 1.00 27.67 ? 28  SER   A CA  1 
ATOM   187  C C   . SER   A 1 28  ? 23.236  4.753   -9.683  1.00 29.31 ? 28  SER   A C   1 
ATOM   188  O O   . SER   A 1 28  ? 24.331  5.197   -9.290  1.00 29.89 ? 28  SER   A O   1 
ATOM   189  C CB  . SER   A 1 28  ? 23.874  2.918   -11.292 1.00 28.05 ? 28  SER   A CB  1 
ATOM   190  O OG  . SER   A 1 28  ? 23.199  3.432   -12.425 1.00 29.89 ? 28  SER   A OG  1 
ATOM   191  N N   . THR   A 1 29  ? 22.154  5.541   -9.816  1.00 30.52 ? 29  THR   A N   1 
ATOM   192  C CA  . THR   A 1 29  ? 22.165  6.926   -9.317  1.00 30.24 ? 29  THR   A CA  1 
ATOM   193  C C   . THR   A 1 29  ? 22.185  6.993   -7.804  1.00 29.98 ? 29  THR   A C   1 
ATOM   194  O O   . THR   A 1 29  ? 22.428  8.067   -7.240  1.00 32.87 ? 29  THR   A O   1 
ATOM   195  C CB  . THR   A 1 29  ? 20.895  7.665   -9.745  1.00 30.21 ? 29  THR   A CB  1 
ATOM   196  O OG1 . THR   A 1 29  ? 19.740  7.077   -9.086  1.00 29.95 ? 29  THR   A OG1 1 
ATOM   197  C CG2 . THR   A 1 29  ? 20.730  7.601   -11.229 1.00 33.52 ? 29  THR   A CG2 1 
ATOM   198  N N   . GLY   A 1 30  ? 21.912  5.890   -7.126  1.00 29.37 ? 30  GLY   A N   1 
ATOM   199  C CA  . GLY   A 1 30  ? 21.791  5.938   -5.696  1.00 29.84 ? 30  GLY   A CA  1 
ATOM   200  C C   . GLY   A 1 30  ? 20.384  6.145   -5.199  1.00 29.17 ? 30  GLY   A C   1 
ATOM   201  O O   . GLY   A 1 30  ? 20.153  6.022   -3.985  1.00 29.93 ? 30  GLY   A O   1 
ATOM   202  N N   . ALA   A 1 31  ? 19.430  6.430   -6.089  1.00 26.08 ? 31  ALA   A N   1 
ATOM   203  C CA  . ALA   A 1 31  ? 18.045  6.497   -5.647  1.00 23.67 ? 31  ALA   A CA  1 
ATOM   204  C C   . ALA   A 1 31  ? 17.095  6.259   -6.800  1.00 22.67 ? 31  ALA   A C   1 
ATOM   205  O O   . ALA   A 1 31  ? 17.254  6.838   -7.874  1.00 24.32 ? 31  ALA   A O   1 
ATOM   206  C CB  . ALA   A 1 31  ? 17.727  7.840   -5.024  1.00 23.74 ? 31  ALA   A CB  1 
ATOM   207  N N   . VAL   A 1 32  ? 16.131  5.381   -6.575  1.00 20.98 ? 32  VAL   A N   1 
ATOM   208  C CA  . VAL   A 1 32  ? 14.984  5.278   -7.459  1.00 19.29 ? 32  VAL   A CA  1 
ATOM   209  C C   . VAL   A 1 32  ? 14.022  6.389   -7.062  1.00 20.20 ? 32  VAL   A C   1 
ATOM   210  O O   . VAL   A 1 32  ? 13.690  6.552   -5.875  1.00 23.08 ? 32  VAL   A O   1 
ATOM   211  C CB  . VAL   A 1 32  ? 14.318  3.891   -7.342  1.00 18.70 ? 32  VAL   A CB  1 
ATOM   212  C CG1 . VAL   A 1 32  ? 13.152  3.861   -8.279  1.00 19.35 ? 32  VAL   A CG1 1 
ATOM   213  C CG2 . VAL   A 1 32  ? 15.320  2.759   -7.666  1.00 19.92 ? 32  VAL   A CG2 1 
ATOM   214  N N   . ILE   A 1 33  ? 13.599  7.180   -8.037  1.00 18.42 ? 33  ILE   A N   1 
ATOM   215  C CA  . ILE   A 1 33  ? 12.749  8.333   -7.778  1.00 18.26 ? 33  ILE   A CA  1 
ATOM   216  C C   . ILE   A 1 33  ? 11.393  8.156   -8.462  1.00 17.32 ? 33  ILE   A C   1 
ATOM   217  O O   . ILE   A 1 33  ? 11.225  7.331   -9.334  1.00 17.98 ? 33  ILE   A O   1 
ATOM   218  C CB  . ILE   A 1 33  ? 13.440  9.667   -8.160  1.00 19.05 ? 33  ILE   A CB  1 
ATOM   219  C CG1 . ILE   A 1 33  ? 13.733  9.776   -9.665  1.00 19.88 ? 33  ILE   A CG1 1 
ATOM   220  C CG2 . ILE   A 1 33  ? 14.706  9.848   -7.285  1.00 23.11 ? 33  ILE   A CG2 1 
ATOM   221  C CD1 . ILE   A 1 33  ? 14.503  11.053  -10.086 1.00 20.77 ? 33  ILE   A CD1 1 
ATOM   222  N N   . SER   A 1 34  ? 10.445  8.997   -8.092  1.00 17.67 ? 34  SER   A N   1 
ATOM   223  C CA  . SER   A 1 34  ? 9.084   8.828   -8.596  1.00 18.95 ? 34  SER   A CA  1 
ATOM   224  C C   . SER   A 1 34  ? 9.022   8.886   -10.122 1.00 19.27 ? 34  SER   A C   1 
ATOM   225  O O   . SER   A 1 34  ? 8.225   8.171   -10.735 1.00 16.88 ? 34  SER   A O   1 
ATOM   226  C CB  . SER   A 1 34  ? 8.142   9.863   -7.959  1.00 23.81 ? 34  SER   A CB  1 
ATOM   227  O OG  . SER   A 1 34  ? 7.960   9.578   -6.578  1.00 30.48 ? 34  SER   A OG  1 
ATOM   228  N N   . SER   A 1 35  ? 9.812   9.742   -10.757 1.00 19.91 ? 35  SER   A N   1 
ATOM   229  C CA  . SER   A 1 35  ? 9.801   9.837   -12.219 1.00 19.35 ? 35  SER   A CA  1 
ATOM   230  C C   . SER   A 1 35  ? 10.363  8.601   -12.913 1.00 18.44 ? 35  SER   A C   1 
ATOM   231  O O   . SER   A 1 35  ? 10.181  8.468   -14.124 1.00 20.25 ? 35  SER   A O   1 
ATOM   232  C CB  . SER   A 1 35  ? 10.520  11.097  -12.728 1.00 21.26 ? 35  SER   A CB  1 
ATOM   233  O OG  . SER   A 1 35  ? 11.862  11.101  -12.308 1.00 26.13 ? 35  SER   A OG  1 
ATOM   234  N N   . ASN   A 1 36  ? 11.053  7.710   -12.201 1.00 16.73 ? 36  ASN   A N   1 
ATOM   235  C CA  . ASN   A 1 36  ? 11.417  6.421   -12.814 1.00 15.94 ? 36  ASN   A CA  1 
ATOM   236  C C   . ASN   A 1 36  ? 10.189  5.539   -13.042 1.00 16.30 ? 36  ASN   A C   1 
ATOM   237  O O   . ASN   A 1 36  ? 10.294  4.544   -13.770 1.00 16.63 ? 36  ASN   A O   1 
ATOM   238  C CB  . ASN   A 1 36  ? 12.410  5.686   -11.900 1.00 16.51 ? 36  ASN   A CB  1 
ATOM   239  C CG  . ASN   A 1 36  ? 13.804  6.319   -11.868 1.00 18.08 ? 36  ASN   A CG  1 
ATOM   240  O OD1 . ASN   A 1 36  ? 14.407  6.424   -10.796 1.00 20.07 ? 36  ASN   A OD1 1 
ATOM   241  N ND2 . ASN   A 1 36  ? 14.316  6.734   -13.035 1.00 19.98 ? 36  ASN   A ND2 1 
ATOM   242  N N   . PHE   A 1 37  ? 9.044   5.876   -12.439 1.00 15.92 ? 37  PHE   A N   1 
ATOM   243  C CA  . PHE   A 1 37  ? 7.715   5.328   -12.808 1.00 15.53 ? 37  PHE   A CA  1 
ATOM   244  C C   . PHE   A 1 37  ? 7.783   3.808   -13.009 1.00 15.68 ? 37  PHE   A C   1 
ATOM   245  O O   . PHE   A 1 37  ? 7.472   3.284   -14.087 1.00 15.71 ? 37  PHE   A O   1 
ATOM   246  C CB  . PHE   A 1 37  ? 7.135   6.040   -14.042 1.00 16.76 ? 37  PHE   A CB  1 
ATOM   247  C CG  . PHE   A 1 37  ? 5.641   6.125   -14.007 1.00 16.26 ? 37  PHE   A CG  1 
ATOM   248  C CD1 . PHE   A 1 37  ? 5.012   6.980   -13.093 1.00 17.56 ? 37  PHE   A CD1 1 
ATOM   249  C CD2 . PHE   A 1 37  ? 4.864   5.324   -14.852 1.00 16.77 ? 37  PHE   A CD2 1 
ATOM   250  C CE1 . PHE   A 1 37  ? 3.620   7.046   -13.034 1.00 19.71 ? 37  PHE   A CE1 1 
ATOM   251  C CE2 . PHE   A 1 37  ? 3.482   5.406   -14.819 1.00 17.45 ? 37  PHE   A CE2 1 
ATOM   252  C CZ  . PHE   A 1 37  ? 2.865   6.272   -13.880 1.00 18.62 ? 37  PHE   A CZ  1 
ATOM   253  N N   . VAL   A 1 38  ? 8.151   3.114   -11.923 1.00 14.25 ? 38  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 38  ? 8.665   1.744   -12.014 1.00 14.09 ? 38  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 38  ? 7.534   0.767   -12.333 1.00 15.14 ? 38  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 38  ? 6.443   0.828   -11.736 1.00 16.26 ? 38  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 38  ? 9.314   1.370   -10.662 1.00 15.23 ? 38  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 38  ? 9.734   -0.125  -10.634 1.00 14.66 ? 38  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 38  ? 10.531  2.213   -10.358 1.00 17.08 ? 38  VAL   A CG2 1 
ATOM   260  N N   . SER   A 1 39  ? 7.785   -0.172  -13.244 1.00 13.09 ? 39  SER   A N   1 
ATOM   261  C CA  . SER   A 1 39  ? 6.943   -1.364  -13.386 1.00 14.53 ? 39  SER   A CA  1 
ATOM   262  C C   . SER   A 1 39  ? 7.666   -2.576  -12.823 1.00 14.71 ? 39  SER   A C   1 
ATOM   263  O O   . SER   A 1 39  ? 8.896   -2.692  -12.899 1.00 14.08 ? 39  SER   A O   1 
ATOM   264  C CB  . SER   A 1 39  ? 6.635   -1.610  -14.863 1.00 14.66 ? 39  SER   A CB  1 
ATOM   265  O OG  . SER   A 1 39  ? 5.638   -0.724  -15.349 1.00 15.42 ? 39  SER   A OG  1 
ATOM   266  N N   . TRP   A 1 40  ? 6.888   -3.522  -12.293 1.00 13.43 ? 40  TRP   A N   1 
ATOM   267  C CA  . TRP   A 1 40  ? 7.383   -4.840  -11.953 1.00 13.22 ? 40  TRP   A CA  1 
ATOM   268  C C   . TRP   A 1 40  ? 6.649   -5.845  -12.830 1.00 12.78 ? 40  TRP   A C   1 
ATOM   269  O O   . TRP   A 1 40  ? 5.408   -5.802  -12.916 1.00 13.88 ? 40  TRP   A O   1 
ATOM   270  C CB  . TRP   A 1 40  ? 7.081   -5.157  -10.492 1.00 13.46 ? 40  TRP   A CB  1 
ATOM   271  C CG  . TRP   A 1 40  ? 7.948   -4.430  -9.515  1.00 12.93 ? 40  TRP   A CG  1 
ATOM   272  C CD1 . TRP   A 1 40  ? 7.714   -3.192  -8.950  1.00 14.48 ? 40  TRP   A CD1 1 
ATOM   273  C CD2 . TRP   A 1 40  ? 9.195   -4.872  -9.006  1.00 13.38 ? 40  TRP   A CD2 1 
ATOM   274  N NE1 . TRP   A 1 40  ? 8.730   -2.877  -8.106  1.00 14.86 ? 40  TRP   A NE1 1 
ATOM   275  C CE2 . TRP   A 1 40  ? 9.641   -3.900  -8.101  1.00 14.03 ? 40  TRP   A CE2 1 
ATOM   276  C CE3 . TRP   A 1 40  ? 9.951   -6.037  -9.185  1.00 13.41 ? 40  TRP   A CE3 1 
ATOM   277  C CZ2 . TRP   A 1 40  ? 10.830  -4.024  -7.384  1.00 13.97 ? 40  TRP   A CZ2 1 
ATOM   278  C CZ3 . TRP   A 1 40  ? 11.143  -6.192  -8.455  1.00 13.32 ? 40  TRP   A CZ3 1 
ATOM   279  C CH2 . TRP   A 1 40  ? 11.565  -5.160  -7.549  1.00 14.42 ? 40  TRP   A CH2 1 
ATOM   280  N N   . VAL   A 1 41  ? 7.399   -6.766  -13.448 1.00 12.99 ? 41  VAL   A N   1 
ATOM   281  C CA  . VAL   A 1 41  ? 6.826   -7.817  -14.278 1.00 13.64 ? 41  VAL   A CA  1 
ATOM   282  C C   . VAL   A 1 41  ? 7.328   -9.180  -13.819 1.00 13.79 ? 41  VAL   A C   1 
ATOM   283  O O   . VAL   A 1 41  ? 8.390   -9.307  -13.203 1.00 15.26 ? 41  VAL   A O   1 
ATOM   284  C CB  . VAL   A 1 41  ? 7.098   -7.595  -15.789 1.00 16.28 ? 41  VAL   A CB  1 
ATOM   285  C CG1 . VAL   A 1 41  ? 6.669   -6.217  -16.255 1.00 17.20 ? 41  VAL   A CG1 1 
ATOM   286  C CG2 . VAL   A 1 41  ? 8.550   -7.752  -16.113 1.00 17.09 ? 41  VAL   A CG2 1 
ATOM   287  N N   . GLN   A 1 42  ? 6.552   -10.207 -14.124 1.00 13.31 ? 42  GLN   A N   1 
ATOM   288  C CA  . GLN   A 1 42  ? 6.823   -11.565 -13.680 1.00 13.92 ? 42  GLN   A CA  1 
ATOM   289  C C   . GLN   A 1 42  ? 6.967   -12.462 -14.890 1.00 14.61 ? 42  GLN   A C   1 
ATOM   290  O O   . GLN   A 1 42  ? 6.077   -12.474 -15.743 1.00 15.75 ? 42  GLN   A O   1 
ATOM   291  C CB  . GLN   A 1 42  ? 5.590   -12.004 -12.875 1.00 16.32 ? 42  GLN   A CB  1 
ATOM   292  C CG  . GLN   A 1 42  ? 5.685   -13.354 -12.232 1.00 17.01 ? 42  GLN   A CG  1 
ATOM   293  C CD  . GLN   A 1 42  ? 4.328   -13.805 -11.754 1.00 17.13 ? 42  GLN   A CD  1 
ATOM   294  O OE1 . GLN   A 1 42  ? 3.379   -13.905 -12.555 1.00 20.00 ? 42  GLN   A OE1 1 
ATOM   295  N NE2 . GLN   A 1 42  ? 4.200   -14.023 -10.448 1.00 16.56 ? 42  GLN   A NE2 1 
ATOM   296  N N   . GLU   A 1 43  ? 8.046   -13.240 -14.950 1.00 12.79 ? 43  GLU   A N   1 
ATOM   297  C CA  . GLU   A 1 43  ? 8.299   -14.203 -16.020 1.00 13.12 ? 43  GLU   A CA  1 
ATOM   298  C C   . GLU   A 1 43  ? 8.180   -15.627 -15.519 1.00 14.36 ? 43  GLU   A C   1 
ATOM   299  O O   . GLU   A 1 43  ? 8.907   -16.032 -14.607 1.00 16.03 ? 43  GLU   A O   1 
ATOM   300  C CB  . GLU   A 1 43  ? 9.716   -14.021 -16.619 1.00 15.23 ? 43  GLU   A CB  1 
ATOM   301  C CG  . GLU   A 1 43  ? 9.888   -14.848 -17.894 1.00 18.20 ? 43  GLU   A CG  1 
ATOM   302  C CD  . GLU   A 1 43  ? 11.262  -14.647 -18.503 1.00 25.12 ? 43  GLU   A CD  1 
ATOM   303  O OE1 . GLU   A 1 43  ? 12.205  -14.247 -17.772 1.00 25.53 ? 43  GLU   A OE1 1 
ATOM   304  O OE2 . GLU   A 1 43  ? 11.424  -15.031 -19.675 1.00 28.95 ? 43  GLU   A OE2 1 
ATOM   305  N N   . LYS   A 1 44  ? 7.348   -16.409 -16.174 1.00 15.30 ? 44  LYS   A N   1 
ATOM   306  C CA  . LYS   A 1 44  ? 7.199   -17.840 -15.906 1.00 16.68 ? 44  LYS   A CA  1 
ATOM   307  C C   . LYS   A 1 44  ? 7.676   -18.640 -17.099 1.00 18.65 ? 44  LYS   A C   1 
ATOM   308  O O   . LYS   A 1 44  ? 7.854   -18.087 -18.182 1.00 18.93 ? 44  LYS   A O   1 
ATOM   309  C CB  . LYS   A 1 44  ? 5.752   -18.159 -15.531 1.00 17.81 ? 44  LYS   A CB  1 
ATOM   310  C CG  . LYS   A 1 44  ? 5.503   -17.589 -14.123 1.00 21.03 ? 44  LYS   A CG  1 
ATOM   311  C CD  . LYS   A 1 44  ? 4.159   -17.871 -13.577 1.00 21.30 ? 44  LYS   A CD  1 
ATOM   312  C CE  . LYS   A 1 44  ? 4.037   -17.330 -12.152 1.00 20.08 ? 44  LYS   A CE  1 
ATOM   313  N NZ  . LYS   A 1 44  ? 2.600   -17.452 -11.733 1.00 18.06 ? 44  LYS   A NZ  1 
ATOM   314  N N   . PRO   A 1 45  ? 7.906   -19.950 -16.929 1.00 18.76 ? 45  PRO   A N   1 
ATOM   315  C CA  . PRO   A 1 45  ? 8.525   -20.751 -17.991 1.00 20.45 ? 45  PRO   A CA  1 
ATOM   316  C C   . PRO   A 1 45  ? 7.734   -20.706 -19.271 1.00 24.79 ? 45  PRO   A C   1 
ATOM   317  O O   . PRO   A 1 45  ? 6.509   -20.535 -19.268 1.00 27.28 ? 45  PRO   A O   1 
ATOM   318  C CB  . PRO   A 1 45  ? 8.537   -22.165 -17.402 1.00 20.92 ? 45  PRO   A CB  1 
ATOM   319  C CG  . PRO   A 1 45  ? 8.747   -21.929 -15.944 1.00 20.74 ? 45  PRO   A CG  1 
ATOM   320  C CD  . PRO   A 1 45  ? 7.898   -20.707 -15.660 1.00 20.02 ? 45  PRO   A CD  1 
ATOM   321  N N   . ASP   A 1 46  ? 8.495   -20.871 -20.358 1.00 31.03 ? 46  ASP   A N   1 
ATOM   322  C CA  . ASP   A 1 46  ? 8.106   -20.614 -21.723 1.00 37.33 ? 46  ASP   A CA  1 
ATOM   323  C C   . ASP   A 1 46  ? 7.956   -19.109 -21.965 1.00 32.55 ? 46  ASP   A C   1 
ATOM   324  O O   . ASP   A 1 46  ? 7.004   -18.696 -22.625 1.00 36.66 ? 46  ASP   A O   1 
ATOM   325  C CB  . ASP   A 1 46  ? 6.888   -21.442 -22.178 1.00 46.06 ? 46  ASP   A CB  1 
ATOM   326  C CG  . ASP   A 1 46  ? 7.105   -22.969 -21.994 1.00 55.65 ? 46  ASP   A CG  1 
ATOM   327  O OD1 . ASP   A 1 46  ? 8.212   -23.470 -22.318 1.00 55.83 ? 46  ASP   A OD1 1 
ATOM   328  O OD2 . ASP   A 1 46  ? 6.176   -23.670 -21.513 1.00 62.72 ? 46  ASP   A OD2 1 
ATOM   329  N N   . HIS   A 1 47  ? 8.929   -18.317 -21.422 1.00 26.48 ? 47  HIS   A N   1 
ATOM   330  C CA  A HIS   A 1 47  ? 8.957   -16.841 -21.408 0.62 24.15 ? 47  HIS   A CA  1 
ATOM   331  C CA  B HIS   A 1 47  ? 8.948   -16.841 -21.412 0.38 25.31 ? 47  HIS   A CA  1 
ATOM   332  C C   . HIS   A 1 47  ? 7.568   -16.191 -21.445 1.00 24.93 ? 47  HIS   A C   1 
ATOM   333  O O   . HIS   A 1 47  ? 7.257   -15.390 -22.346 1.00 27.85 ? 47  HIS   A O   1 
ATOM   334  C CB  A HIS   A 1 47  ? 9.961   -16.287 -22.431 0.62 23.02 ? 47  HIS   A CB  1 
ATOM   335  C CB  B HIS   A 1 47  ? 9.910   -16.227 -22.442 0.38 26.01 ? 47  HIS   A CB  1 
ATOM   336  C CG  A HIS   A 1 47  ? 9.831   -16.901 -23.785 0.62 20.35 ? 47  HIS   A CG  1 
ATOM   337  C CG  B HIS   A 1 47  ? 10.341  -17.173 -23.513 0.38 25.97 ? 47  HIS   A CG  1 
ATOM   338  N ND1 A HIS   A 1 47  ? 8.752   -16.639 -24.597 0.62 21.30 ? 47  HIS   A ND1 1 
ATOM   339  N ND1 B HIS   A 1 47  ? 9.452   -17.740 -24.399 0.38 26.64 ? 47  HIS   A ND1 1 
ATOM   340  C CD2 A HIS   A 1 47  ? 10.627  -17.754 -24.471 0.62 20.16 ? 47  HIS   A CD2 1 
ATOM   341  C CD2 B HIS   A 1 47  ? 11.563  -17.647 -23.847 0.38 27.26 ? 47  HIS   A CD2 1 
ATOM   342  C CE1 A HIS   A 1 47  ? 8.875   -17.325 -25.723 0.62 21.81 ? 47  HIS   A CE1 1 
ATOM   343  C CE1 B HIS   A 1 47  ? 10.107  -18.537 -25.224 0.38 27.25 ? 47  HIS   A CE1 1 
ATOM   344  N NE2 A HIS   A 1 47  ? 10.002  -18.010 -25.670 0.62 22.25 ? 47  HIS   A NE2 1 
ATOM   345  N NE2 B HIS   A 1 47  ? 11.390  -18.495 -24.914 0.38 27.74 ? 47  HIS   A NE2 1 
ATOM   346  N N   . LEU   A 1 48  ? 6.737   -16.513 -20.419 1.00 21.77 ? 48  LEU   A N   1 
ATOM   347  C CA  . LEU   A 1 48  ? 5.376   -15.999 -20.233 1.00 20.73 ? 48  LEU   A CA  1 
ATOM   348  C C   . LEU   A 1 48  ? 5.445   -14.845 -19.236 1.00 17.80 ? 48  LEU   A C   1 
ATOM   349  O O   . LEU   A 1 48  ? 5.672   -15.064 -18.035 1.00 16.15 ? 48  LEU   A O   1 
ATOM   350  C CB  . LEU   A 1 48  ? 4.455   -17.094 -19.685 1.00 24.69 ? 48  LEU   A CB  1 
ATOM   351  C CG  . LEU   A 1 48  ? 4.071   -18.198 -20.659 1.00 30.41 ? 48  LEU   A CG  1 
ATOM   352  C CD1 . LEU   A 1 48  ? 3.008   -19.159 -20.050 1.00 28.05 ? 48  LEU   A CD1 1 
ATOM   353  C CD2 . LEU   A 1 48  ? 3.591   -17.524 -21.947 1.00 37.39 ? 48  LEU   A CD2 1 
ATOM   354  N N   . PHE   A 1 49  ? 5.241   -13.612 -19.721 1.00 15.56 ? 49  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 49  ? 5.351   -12.431 -18.873 1.00 15.47 ? 49  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 49  ? 3.973   -11.875 -18.533 1.00 15.93 ? 49  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 49  ? 3.079   -11.849 -19.377 1.00 18.28 ? 49  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 49  ? 6.091   -11.327 -19.623 1.00 16.09 ? 49  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 49  ? 7.568   -11.451 -19.563 1.00 18.69 ? 49  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 49  ? 8.254   -12.185 -20.490 1.00 21.58 ? 49  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 49  ? 8.272   -10.780 -18.590 1.00 19.89 ? 49  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 49  ? 9.635   -12.298 -20.425 1.00 22.16 ? 49  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 49  ? 9.645   -10.847 -18.529 1.00 21.13 ? 49  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 49  ? 10.325  -11.617 -19.449 1.00 21.16 ? 49  PHE   A CZ  1 
ATOM   365  N N   . THR   A 1 50  ? 3.843   -11.341 -17.312 1.00 16.80 ? 50  THR   A N   1 
ATOM   366  C CA  . THR   A 1 50  ? 2.678   -10.601 -16.830 1.00 20.14 ? 50  THR   A CA  1 
ATOM   367  C C   . THR   A 1 50  ? 3.164   -9.390  -16.047 1.00 17.44 ? 50  THR   A C   1 
ATOM   368  O O   . THR   A 1 50  ? 4.092   -9.523  -15.248 1.00 18.10 ? 50  THR   A O   1 
ATOM   369  C CB  . THR   A 1 50  ? 1.825   -11.453 -15.850 1.00 27.29 ? 50  THR   A CB  1 
ATOM   370  O OG1 . THR   A 1 50  ? 1.644   -12.790 -16.345 1.00 34.05 ? 50  THR   A OG1 1 
ATOM   371  C CG2 . THR   A 1 50  ? 0.508   -10.791 -15.503 1.00 32.50 ? 50  THR   A CG2 1 
ATOM   372  N N   . GLY   A 1 51  ? 2.562   -8.218  -16.259 1.00 16.51 ? 51  GLY   A N   1 
ATOM   373  C CA  . GLY   A 1 51  ? 2.884   -7.072  -15.422 1.00 17.26 ? 51  GLY   A CA  1 
ATOM   374  C C   . GLY   A 1 51  ? 2.100   -7.137  -14.114 1.00 15.27 ? 51  GLY   A C   1 
ATOM   375  O O   . GLY   A 1 51  ? 0.924   -7.541  -14.073 1.00 20.74 ? 51  GLY   A O   1 
ATOM   376  N N   . LEU   A 1 52  ? 2.758   -6.749  -13.033 1.00 15.01 ? 52  LEU   A N   1 
ATOM   377  C CA  . LEU   A 1 52  ? 2.162   -6.766  -11.688 1.00 15.19 ? 52  LEU   A CA  1 
ATOM   378  C C   . LEU   A 1 52  ? 1.937   -5.374  -11.115 1.00 14.98 ? 52  LEU   A C   1 
ATOM   379  O O   . LEU   A 1 52  ? 0.870   -5.105  -10.553 1.00 15.24 ? 52  LEU   A O   1 
ATOM   380  C CB  . LEU   A 1 52  ? 3.059   -7.512  -10.697 1.00 16.38 ? 52  LEU   A CB  1 
ATOM   381  C CG  . LEU   A 1 52  ? 3.364   -8.970  -11.043 1.00 17.04 ? 52  LEU   A CG  1 
ATOM   382  C CD1 . LEU   A 1 52  ? 4.409   -9.542  -10.096 1.00 21.75 ? 52  LEU   A CD1 1 
ATOM   383  C CD2 . LEU   A 1 52  ? 2.095   -9.802  -10.964 1.00 19.61 ? 52  LEU   A CD2 1 
ATOM   384  N N   . ILE   A 1 53  ? 2.907   -4.471  -11.282 1.00 15.81 ? 53  ILE   A N   1 
ATOM   385  C CA  . ILE   A 1 53  ? 2.882   -3.127  -10.701 1.00 14.81 ? 53  ILE   A CA  1 
ATOM   386  C C   . ILE   A 1 53  ? 3.264   -2.157  -11.810 1.00 14.76 ? 53  ILE   A C   1 
ATOM   387  O O   . ILE   A 1 53  ? 4.125   -2.474  -12.643 1.00 15.84 ? 53  ILE   A O   1 
ATOM   388  C CB  . ILE   A 1 53  ? 3.899   -2.983  -9.557  1.00 16.20 ? 53  ILE   A CB  1 
ATOM   389  C CG1 . ILE   A 1 53  ? 3.671   -4.059  -8.478  1.00 17.40 ? 53  ILE   A CG1 1 
ATOM   390  C CG2 . ILE   A 1 53  ? 3.876   -1.535  -8.972  1.00 18.21 ? 53  ILE   A CG2 1 
ATOM   391  C CD1 . ILE   A 1 53  ? 2.382   -3.867  -7.607  1.00 21.04 ? 53  ILE   A CD1 1 
ATOM   392  N N   . GLY   A 1 54  ? 2.639   -0.979  -11.821 1.00 15.46 ? 54  GLY   A N   1 
ATOM   393  C CA  . GLY   A 1 54  ? 3.104   0.103   -12.658 1.00 16.28 ? 54  GLY   A CA  1 
ATOM   394  C C   . GLY   A 1 54  ? 3.064   1.406   -11.893 1.00 16.49 ? 54  GLY   A C   1 
ATOM   395  O O   . GLY   A 1 54  ? 2.449   1.489   -10.822 1.00 16.09 ? 54  GLY   A O   1 
ATOM   396  N N   . GLY   A 1 55  ? 3.758   2.415   -12.426 1.00 15.63 ? 55  GLY   A N   1 
ATOM   397  C CA  . GLY   A 1 55  ? 3.721   3.713   -11.748 1.00 16.75 ? 55  GLY   A CA  1 
ATOM   398  C C   . GLY   A 1 55  ? 4.213   3.648   -10.322 1.00 17.14 ? 55  GLY   A C   1 
ATOM   399  O O   . GLY   A 1 55  ? 3.670   4.358   -9.457  1.00 18.12 ? 55  GLY   A O   1 
ATOM   400  N N   . ASN   A 1 56  ? 5.240   2.811   -10.044 1.00 16.69 ? 56  ASN   A N   1 
ATOM   401  C CA  . ASN   A 1 56  ? 5.891   2.665   -8.722  1.00 16.79 ? 56  ASN   A CA  1 
ATOM   402  C C   . ASN   A 1 56  ? 5.059   1.852   -7.737  1.00 15.94 ? 56  ASN   A C   1 
ATOM   403  O O   . ASN   A 1 56  ? 5.594   1.015   -7.017  1.00 17.20 ? 56  ASN   A O   1 
ATOM   404  C CB  . ASN   A 1 56  ? 6.253   4.003   -8.025  1.00 18.19 ? 56  ASN   A CB  1 
ATOM   405  C CG  . ASN   A 1 56  ? 7.104   4.877   -8.887  1.00 18.37 ? 56  ASN   A CG  1 
ATOM   406  O OD1 . ASN   A 1 56  ? 8.165   4.434   -9.347  1.00 19.30 ? 56  ASN   A OD1 1 
ATOM   407  N ND2 . ASN   A 1 56  ? 6.649   6.120   -9.154  1.00 20.17 ? 56  ASN   A ND2 1 
ATOM   408  N N   . LYS   A 1 57  ? 3.765   2.155   -7.643  1.00 17.58 ? 57  LYS   A N   1 
ATOM   409  C CA  . LYS   A 1 57  ? 2.957   1.638   -6.550  1.00 19.42 ? 57  LYS   A CA  1 
ATOM   410  C C   . LYS   A 1 57  ? 1.578   1.120   -6.954  1.00 20.55 ? 57  LYS   A C   1 
ATOM   411  O O   . LYS   A 1 57  ? 0.804   0.726   -6.067  1.00 22.75 ? 57  LYS   A O   1 
ATOM   412  C CB  . LYS   A 1 57  ? 2.815   2.737   -5.494  1.00 23.55 ? 57  LYS   A CB  1 
ATOM   413  C CG  . LYS   A 1 57  ? 1.961   3.894   -6.013  1.00 27.47 ? 57  LYS   A CG  1 
ATOM   414  C CD  . LYS   A 1 57  ? 2.123   5.187   -5.237  1.00 36.47 ? 57  LYS   A CD  1 
ATOM   415  C CE  . LYS   A 1 57  ? 1.374   6.322   -5.965  1.00 40.31 ? 57  LYS   A CE  1 
ATOM   416  N NZ  . LYS   A 1 57  ? -0.074  6.017   -6.276  1.00 42.76 ? 57  LYS   A NZ  1 
ATOM   417  N N   . ASN   A 1 58  ? 1.221   1.131   -8.239  1.00 19.21 ? 58  ASN   A N   1 
ATOM   418  C CA  . ASN   A 1 58  ? -0.144  0.802   -8.637  1.00 20.38 ? 58  ASN   A CA  1 
ATOM   419  C C   . ASN   A 1 58  ? -0.225  -0.657  -9.029  1.00 18.28 ? 58  ASN   A C   1 
ATOM   420  O O   . ASN   A 1 58  ? 0.460   -1.098  -9.962  1.00 18.89 ? 58  ASN   A O   1 
ATOM   421  C CB  . ASN   A 1 58  ? -0.656  1.677   -9.777  1.00 21.78 ? 58  ASN   A CB  1 
ATOM   422  C CG  . ASN   A 1 58  ? -0.630  3.124   -9.421  1.00 24.57 ? 58  ASN   A CG  1 
ATOM   423  O OD1 . ASN   A 1 58  ? -1.172  3.516   -8.398  1.00 28.44 ? 58  ASN   A OD1 1 
ATOM   424  N ND2 . ASN   A 1 58  ? 0.030   3.924   -10.240 1.00 24.91 ? 58  ASN   A ND2 1 
ATOM   425  N N   . ARG   A 1 59  ? -1.038  -1.408  -8.298  1.00 19.77 ? 59  ARG   A N   1 
ATOM   426  C CA  . ARG   A 1 59  ? -1.266  -2.810  -8.635  1.00 23.86 ? 59  ARG   A CA  1 
ATOM   427  C C   . ARG   A 1 59  ? -2.158  -2.865  -9.865  1.00 26.24 ? 59  ARG   A C   1 
ATOM   428  O O   . ARG   A 1 59  ? -3.207  -2.207  -9.907  1.00 27.56 ? 59  ARG   A O   1 
ATOM   429  C CB  . ARG   A 1 59  ? -1.931  -3.508  -7.443  1.00 23.01 ? 59  ARG   A CB  1 
ATOM   430  C CG  . ARG   A 1 59  ? -2.223  -4.955  -7.584  1.00 24.20 ? 59  ARG   A CG  1 
ATOM   431  C CD  . ARG   A 1 59  ? -3.197  -5.437  -6.504  1.00 24.58 ? 59  ARG   A CD  1 
ATOM   432  N NE  . ARG   A 1 59  ? -2.594  -5.407  -5.185  1.00 25.25 ? 59  ARG   A NE  1 
ATOM   433  C CZ  . ARG   A 1 59  ? -2.919  -4.593  -4.186  1.00 24.74 ? 59  ARG   A CZ  1 
ATOM   434  N NH1 . ARG   A 1 59  ? -3.870  -3.662  -4.308  1.00 24.93 ? 59  ARG   A NH1 1 
ATOM   435  N NH2 . ARG   A 1 59  ? -2.269  -4.714  -3.032  1.00 24.21 ? 59  ARG   A NH2 1 
ATOM   436  N N   . ALA   A 1 60  ? -1.714  -3.577  -10.892 1.00 24.26 ? 60  ALA   A N   1 
ATOM   437  C CA  . ALA   A 1 60  ? -2.481  -3.630  -12.133 1.00 27.06 ? 60  ALA   A CA  1 
ATOM   438  C C   . ALA   A 1 60  ? -3.831  -4.297  -11.889 1.00 28.94 ? 60  ALA   A C   1 
ATOM   439  O O   . ALA   A 1 60  ? -3.932  -5.231  -11.098 1.00 25.05 ? 60  ALA   A O   1 
ATOM   440  C CB  . ALA   A 1 60  ? -1.707  -4.430  -13.180 1.00 26.51 ? 60  ALA   A CB  1 
ATOM   441  N N   . PRO   A 1 61  ? -4.903  -3.833  -12.523 1.00 32.16 ? 61  PRO   A N   1 
ATOM   442  C CA  . PRO   A 1 61  ? -6.182  -4.533  -12.340 1.00 31.86 ? 61  PRO   A CA  1 
ATOM   443  C C   . PRO   A 1 61  ? -6.044  -6.020  -12.669 1.00 30.59 ? 61  PRO   A C   1 
ATOM   444  O O   . PRO   A 1 61  ? -5.286  -6.418  -13.560 1.00 33.91 ? 61  PRO   A O   1 
ATOM   445  C CB  . PRO   A 1 61  ? -7.143  -3.801  -13.286 1.00 33.84 ? 61  PRO   A CB  1 
ATOM   446  C CG  . PRO   A 1 61  ? -6.401  -2.628  -13.841 1.00 36.75 ? 61  PRO   A CG  1 
ATOM   447  C CD  . PRO   A 1 61  ? -5.050  -2.529  -13.207 1.00 34.65 ? 61  PRO   A CD  1 
ATOM   448  N N   . GLY   A 1 62  ? -6.722  -6.856  -11.886 1.00 28.75 ? 62  GLY   A N   1 
ATOM   449  C CA  . GLY   A 1 62  ? -6.627  -8.289  -12.044 1.00 27.47 ? 62  GLY   A CA  1 
ATOM   450  C C   . GLY   A 1 62  ? -5.500  -8.935  -11.256 1.00 24.62 ? 62  GLY   A C   1 
ATOM   451  O O   . GLY   A 1 62  ? -5.547  -10.137 -11.005 1.00 28.12 ? 62  GLY   A O   1 
ATOM   452  N N   . VAL   A 1 63  ? -4.501  -8.171  -10.829 1.00 21.08 ? 63  VAL   A N   1 
ATOM   453  C CA  . VAL   A 1 63  ? -3.368  -8.749  -10.121 1.00 19.05 ? 63  VAL   A CA  1 
ATOM   454  C C   . VAL   A 1 63  ? -3.777  -9.069  -8.686  1.00 16.79 ? 63  VAL   A C   1 
ATOM   455  O O   . VAL   A 1 63  ? -4.435  -8.254  -8.038  1.00 19.30 ? 63  VAL   A O   1 
ATOM   456  C CB  . VAL   A 1 63  ? -2.155  -7.804  -10.210 1.00 19.55 ? 63  VAL   A CB  1 
ATOM   457  C CG1 . VAL   A 1 63  ? -1.044  -8.211  -9.216  1.00 19.73 ? 63  VAL   A CG1 1 
ATOM   458  C CG2 . VAL   A 1 63  ? -1.611  -7.795  -11.652 1.00 20.76 ? 63  VAL   A CG2 1 
ATOM   459  N N   . PRO   A 1 64  ? -3.373  -10.210 -8.134  1.00 15.69 ? 64  PRO   A N   1 
ATOM   460  C CA  . PRO   A 1 64  ? -3.816  -10.552 -6.774  1.00 16.01 ? 64  PRO   A CA  1 
ATOM   461  C C   . PRO   A 1 64  ? -3.344  -9.569  -5.705  1.00 15.41 ? 64  PRO   A C   1 
ATOM   462  O O   . PRO   A 1 64  ? -2.256  -8.974  -5.777  1.00 15.38 ? 64  PRO   A O   1 
ATOM   463  C CB  . PRO   A 1 64  ? -3.199  -11.931 -6.534  1.00 17.58 ? 64  PRO   A CB  1 
ATOM   464  C CG  . PRO   A 1 64  ? -3.030  -12.520 -7.880  1.00 18.04 ? 64  PRO   A CG  1 
ATOM   465  C CD  . PRO   A 1 64  ? -2.707  -11.347 -8.801  1.00 16.53 ? 64  PRO   A CD  1 
ATOM   466  N N   . ALA   A 1 65  ? -4.159  -9.454  -4.653  1.00 14.39 ? 65  ALA   A N   1 
ATOM   467  C CA  . ALA   A 1 65  ? -3.918  -8.519  -3.551  1.00 15.74 ? 65  ALA   A CA  1 
ATOM   468  C C   . ALA   A 1 65  ? -2.630  -8.782  -2.805  1.00 14.02 ? 65  ALA   A C   1 
ATOM   469  O O   . ALA   A 1 65  ? -2.117  -7.836  -2.182  1.00 14.69 ? 65  ALA   A O   1 
ATOM   470  C CB  . ALA   A 1 65  ? -5.066  -8.575  -2.534  1.00 17.97 ? 65  ALA   A CB  1 
ATOM   471  N N   . ARG   A 1 66  ? -2.093  -10.015 -2.837  1.00 13.98 ? 66  ARG   A N   1 
ATOM   472  C CA  . ARG   A 1 66  ? -0.842  -10.247 -2.107  1.00 13.52 ? 66  ARG   A CA  1 
ATOM   473  C C   . ARG   A 1 66  ? 0.353   -9.512  -2.688  1.00 12.92 ? 66  ARG   A C   1 
ATOM   474  O O   . ARG   A 1 66  ? 1.360   -9.397  -1.987  1.00 13.97 ? 66  ARG   A O   1 
ATOM   475  C CB  . ARG   A 1 66  ? -0.528  -11.743 -2.021  1.00 13.73 ? 66  ARG   A CB  1 
ATOM   476  C CG  . ARG   A 1 66  ? -0.213  -12.412 -3.364  1.00 13.79 ? 66  ARG   A CG  1 
ATOM   477  C CD  . ARG   A 1 66  ? -0.085  -13.925 -3.172  1.00 13.45 ? 66  ARG   A CD  1 
ATOM   478  N NE  . ARG   A 1 66  ? 0.146   -14.635 -4.429  1.00 14.18 ? 66  ARG   A NE  1 
ATOM   479  C CZ  . ARG   A 1 66  ? -0.802  -14.952 -5.300  1.00 14.50 ? 66  ARG   A CZ  1 
ATOM   480  N NH1 . ARG   A 1 66  ? -2.083  -14.600 -5.110  1.00 15.29 ? 66  ARG   A NH1 1 
ATOM   481  N NH2 . ARG   A 1 66  ? -0.456  -15.629 -6.400  1.00 15.87 ? 66  ARG   A NH2 1 
ATOM   482  N N   . PHE   A 1 67  ? 0.274   -8.984  -3.912  1.00 14.24 ? 67  PHE   A N   1 
ATOM   483  C CA  . PHE   A 1 67  ? 1.363   -8.187  -4.490  1.00 13.57 ? 67  PHE   A CA  1 
ATOM   484  C C   . PHE   A 1 67  ? 1.153   -6.703  -4.196  1.00 13.57 ? 67  PHE   A C   1 
ATOM   485  O O   . PHE   A 1 67  ? 0.066   -6.153  -4.414  1.00 16.16 ? 67  PHE   A O   1 
ATOM   486  C CB  . PHE   A 1 67  ? 1.389   -8.385  -6.020  1.00 14.36 ? 67  PHE   A CB  1 
ATOM   487  C CG  . PHE   A 1 67  ? 1.727   -9.773  -6.427  1.00 13.96 ? 67  PHE   A CG  1 
ATOM   488  C CD1 . PHE   A 1 67  ? 3.044   -10.214 -6.403  1.00 15.18 ? 67  PHE   A CD1 1 
ATOM   489  C CD2 . PHE   A 1 67  ? 0.707   -10.656 -6.814  1.00 15.48 ? 67  PHE   A CD2 1 
ATOM   490  C CE1 . PHE   A 1 67  ? 3.348   -11.568 -6.771  1.00 16.48 ? 67  PHE   A CE1 1 
ATOM   491  C CE2 . PHE   A 1 67  ? 0.978   -11.977 -7.168  1.00 16.16 ? 67  PHE   A CE2 1 
ATOM   492  C CZ  . PHE   A 1 67  ? 2.313   -12.448 -7.167  1.00 15.68 ? 67  PHE   A CZ  1 
ATOM   493  N N   . SER   A 1 68  ? 2.206   -6.026  -3.791  1.00 13.31 ? 68  SER   A N   1 
ATOM   494  C CA  . SER   A 1 68  ? 2.168   -4.573  -3.647  1.00 14.95 ? 68  SER   A CA  1 
ATOM   495  C C   . SER   A 1 68  ? 3.544   -4.017  -3.967  1.00 14.67 ? 68  SER   A C   1 
ATOM   496  O O   . SER   A 1 68  ? 4.537   -4.743  -3.911  1.00 15.35 ? 68  SER   A O   1 
ATOM   497  C CB  . SER   A 1 68  ? 1.733   -4.182  -2.224  1.00 17.75 ? 68  SER   A CB  1 
ATOM   498  O OG  . SER   A 1 68  ? 2.694   -4.577  -1.252  1.00 19.77 ? 68  SER   A OG  1 
ATOM   499  N N   . GLY   A 1 69  ? 3.605   -2.741  -4.319  1.00 16.00 ? 69  GLY   A N   1 
ATOM   500  C CA  . GLY   A 1 69  ? 4.861   -2.114  -4.669  1.00 16.41 ? 69  GLY   A CA  1 
ATOM   501  C C   . GLY   A 1 69  ? 4.930   -0.710  -4.111  1.00 15.55 ? 69  GLY   A C   1 
ATOM   502  O O   . GLY   A 1 69  ? 3.900   -0.043  -3.944  1.00 18.01 ? 69  GLY   A O   1 
ATOM   503  N N   . SER   A 1 70  ? 6.151   -0.262  -3.796  1.00 16.34 ? 70  SER   A N   1 
ATOM   504  C CA  . SER   A 1 70  ? 6.334   1.160   -3.493  1.00 19.12 ? 70  SER   A CA  1 
ATOM   505  C C   . SER   A 1 70  ? 7.800   1.532   -3.580  1.00 18.58 ? 70  SER   A C   1 
ATOM   506  O O   . SER   A 1 70  ? 8.656   0.688   -3.828  1.00 17.82 ? 70  SER   A O   1 
ATOM   507  C CB  . SER   A 1 70  ? 5.808   1.544   -2.121  1.00 25.92 ? 70  SER   A CB  1 
ATOM   508  O OG  . SER   A 1 70  ? 6.576   0.899   -1.130  1.00 31.37 ? 70  SER   A OG  1 
ATOM   509  N N   . LEU   A 1 71  ? 8.082   2.835   -3.392  1.00 18.12 ? 71  LEU   A N   1 
ATOM   510  C CA  . LEU   A 1 71  ? 9.454   3.322   -3.278  1.00 19.31 ? 71  LEU   A CA  1 
ATOM   511  C C   . LEU   A 1 71  ? 9.772   3.490   -1.806  1.00 19.55 ? 71  LEU   A C   1 
ATOM   512  O O   . LEU   A 1 71  ? 9.052   4.199   -1.092  1.00 21.44 ? 71  LEU   A O   1 
ATOM   513  C CB  . LEU   A 1 71  ? 9.644   4.642   -4.034  1.00 19.91 ? 71  LEU   A CB  1 
ATOM   514  C CG  . LEU   A 1 71  ? 9.311   4.593   -5.542  1.00 21.11 ? 71  LEU   A CG  1 
ATOM   515  C CD1 . LEU   A 1 71  ? 9.724   5.940   -6.174  1.00 23.68 ? 71  LEU   A CD1 1 
ATOM   516  C CD2 . LEU   A 1 71  ? 10.000  3.428   -6.296  1.00 18.96 ? 71  LEU   A CD2 1 
ATOM   517  N N   . ILE   A 1 72  ? 10.840  2.829   -1.346  1.00 20.08 ? 72  ILE   A N   1 
ATOM   518  C CA  . ILE   A 1 72  ? 11.190  2.843   0.077   1.00 22.44 ? 72  ILE   A CA  1 
ATOM   519  C C   . ILE   A 1 72  ? 12.707  2.955   0.199   1.00 20.44 ? 72  ILE   A C   1 
ATOM   520  O O   . ILE   A 1 72  ? 13.431  2.184   -0.428  1.00 22.17 ? 72  ILE   A O   1 
ATOM   521  C CB  . ILE   A 1 72  ? 10.767  1.507   0.736   1.00 25.96 ? 72  ILE   A CB  1 
ATOM   522  C CG1 . ILE   A 1 72  ? 9.288   1.457   0.993   1.00 29.14 ? 72  ILE   A CG1 1 
ATOM   523  C CG2 . ILE   A 1 72  ? 11.454  1.339   2.085   1.00 28.96 ? 72  ILE   A CG2 1 
ATOM   524  C CD1 . ILE   A 1 72  ? 8.818   0.003   1.330   1.00 30.21 ? 72  ILE   A CD1 1 
ATOM   525  N N   . GLY   A 1 73  ? 13.201  3.846   1.062   1.00 22.07 ? 73  GLY   A N   1 
ATOM   526  C CA  . GLY   A 1 73  ? 14.644  3.891   1.327   1.00 27.00 ? 73  GLY   A CA  1 
ATOM   527  C C   . GLY   A 1 73  ? 15.510  4.010   0.087   1.00 26.37 ? 73  GLY   A C   1 
ATOM   528  O O   . GLY   A 1 73  ? 16.591  3.400   0.008   1.00 24.75 ? 73  GLY   A O   1 
ATOM   529  N N   . ASP   A 1 74  ? 15.057  4.803   -0.889  1.00 27.43 ? 74  ASP   A N   1 
ATOM   530  C CA  . ASP   A 1 74  ? 15.733  5.121   -2.147  1.00 27.45 ? 74  ASP   A CA  1 
ATOM   531  C C   . ASP   A 1 74  ? 15.756  3.945   -3.135  1.00 22.30 ? 74  ASP   A C   1 
ATOM   532  O O   . ASP   A 1 74  ? 16.492  3.994   -4.124  1.00 20.74 ? 74  ASP   A O   1 
ATOM   533  C CB  . ASP   A 1 74  ? 17.128  5.725   -1.949  1.00 32.09 ? 74  ASP   A CB  1 
ATOM   534  C CG  . ASP   A 1 74  ? 17.068  7.258   -1.651  1.00 38.84 ? 74  ASP   A CG  1 
ATOM   535  O OD1 . ASP   A 1 74  ? 16.039  7.934   -1.961  1.00 41.35 ? 74  ASP   A OD1 1 
ATOM   536  O OD2 . ASP   A 1 74  ? 18.006  7.750   -0.987  1.00 42.01 ? 74  ASP   A OD2 1 
ATOM   537  N N   . LYS   A 1 75  ? 14.958  2.899   -2.905  1.00 20.92 ? 75  LYS   A N   1 
ATOM   538  C CA  . LYS   A 1 75  ? 14.858  1.759   -3.789  1.00 18.79 ? 75  LYS   A CA  1 
ATOM   539  C C   . LYS   A 1 75  ? 13.393  1.550   -4.165  1.00 17.96 ? 75  LYS   A C   1 
ATOM   540  O O   . LYS   A 1 75  ? 12.490  2.106   -3.552  1.00 19.66 ? 75  LYS   A O   1 
ATOM   541  C CB  . LYS   A 1 75  ? 15.313  0.503   -3.036  1.00 23.09 ? 75  LYS   A CB  1 
ATOM   542  C CG  . LYS   A 1 75  ? 16.761  0.522   -2.640  1.00 28.49 ? 75  LYS   A CG  1 
ATOM   543  C CD  . LYS   A 1 75  ? 17.191  -0.856  -2.132  1.00 33.74 ? 75  LYS   A CD  1 
ATOM   544  C CE  . LYS   A 1 75  ? 17.585  -0.777  -0.664  1.00 37.98 ? 75  LYS   A CE  1 
ATOM   545  N NZ  . LYS   A 1 75  ? 19.067  -0.644  -0.490  1.00 40.38 ? 75  LYS   A NZ  1 
ATOM   546  N N   . ALA   A 1 76  ? 13.163  0.749   -5.195  1.00 15.48 ? 76  ALA   A N   1 
ATOM   547  C CA  . ALA   A 1 76  ? 11.819  0.254   -5.486  1.00 15.97 ? 76  ALA   A CA  1 
ATOM   548  C C   . ALA   A 1 76  ? 11.698  -1.134  -4.859  1.00 14.46 ? 76  ALA   A C   1 
ATOM   549  O O   . ALA   A 1 76  ? 12.643  -1.929  -4.921  1.00 15.29 ? 76  ALA   A O   1 
ATOM   550  C CB  . ALA   A 1 76  ? 11.571  0.167   -7.008  1.00 17.12 ? 76  ALA   A CB  1 
ATOM   551  N N   . VAL   A 1 77  ? 10.532  -1.445  -4.290  1.00 14.78 ? 77  VAL   A N   1 
ATOM   552  C CA  . VAL   A 1 77  ? 10.322  -2.699  -3.560  1.00 14.37 ? 77  VAL   A CA  1 
ATOM   553  C C   . VAL   A 1 77  ? 9.006   -3.318  -4.000  1.00 15.13 ? 77  VAL   A C   1 
ATOM   554  O O   . VAL   A 1 77  ? 7.983   -2.629  -4.071  1.00 18.42 ? 77  VAL   A O   1 
ATOM   555  C CB  . VAL   A 1 77  ? 10.331  -2.481  -2.035  1.00 16.44 ? 77  VAL   A CB  1 
ATOM   556  C CG1 . VAL   A 1 77  ? 10.034  -3.796  -1.290  1.00 19.75 ? 77  VAL   A CG1 1 
ATOM   557  C CG2 . VAL   A 1 77  ? 11.693  -1.886  -1.564  1.00 17.48 ? 77  VAL   A CG2 1 
ATOM   558  N N   . LEU   A 1 78  ? 9.030   -4.610  -4.332  1.00 13.32 ? 78  LEU   A N   1 
ATOM   559  C CA  . LEU   A 1 78  ? 7.825   -5.400  -4.553  1.00 12.78 ? 78  LEU   A CA  1 
ATOM   560  C C   . LEU   A 1 78  ? 7.676   -6.337  -3.369  1.00 12.84 ? 78  LEU   A C   1 
ATOM   561  O O   . LEU   A 1 78  ? 8.664   -6.990  -2.970  1.00 14.97 ? 78  LEU   A O   1 
ATOM   562  C CB  . LEU   A 1 78  ? 7.990   -6.243  -5.833  1.00 14.04 ? 78  LEU   A CB  1 
ATOM   563  C CG  . LEU   A 1 78  ? 6.881   -7.261  -6.135  1.00 13.81 ? 78  LEU   A CG  1 
ATOM   564  C CD1 . LEU   A 1 78  ? 5.570   -6.528  -6.555  1.00 16.06 ? 78  LEU   A CD1 1 
ATOM   565  C CD2 . LEU   A 1 78  ? 7.313   -8.241  -7.227  1.00 16.37 ? 78  LEU   A CD2 1 
ATOM   566  N N   . THR   A 1 79  ? 6.510   -6.317  -2.740  1.00 12.75 ? 79  THR   A N   1 
ATOM   567  C CA  . THR   A 1 79  ? 6.235   -7.163  -1.586  1.00 13.38 ? 79  THR   A CA  1 
ATOM   568  C C   . THR   A 1 79  ? 5.191   -8.220  -1.927  1.00 13.48 ? 79  THR   A C   1 
ATOM   569  O O   . THR   A 1 79  ? 4.145   -7.886  -2.488  1.00 14.34 ? 79  THR   A O   1 
ATOM   570  C CB  . THR   A 1 79  ? 5.760   -6.311  -0.398  1.00 15.94 ? 79  THR   A CB  1 
ATOM   571  O OG1 . THR   A 1 79  ? 6.776   -5.331  -0.104  1.00 18.92 ? 79  THR   A OG1 1 
ATOM   572  C CG2 . THR   A 1 79  ? 5.587   -7.185  0.841   1.00 17.27 ? 79  THR   A CG2 1 
ATOM   573  N N   . ILE   A 1 80  ? 5.456   -9.474  -1.552  1.00 13.21 ? 80  ILE   A N   1 
ATOM   574  C CA  . ILE   A 1 80  ? 4.467   -10.549 -1.675  1.00 12.61 ? 80  ILE   A CA  1 
ATOM   575  C C   . ILE   A 1 80  ? 4.086   -10.931 -0.257  1.00 13.68 ? 80  ILE   A C   1 
ATOM   576  O O   . ILE   A 1 80  ? 4.901   -11.510 0.483   1.00 14.98 ? 80  ILE   A O   1 
ATOM   577  C CB  . ILE   A 1 80  ? 4.958   -11.762 -2.472  1.00 14.42 ? 80  ILE   A CB  1 
ATOM   578  C CG1 . ILE   A 1 80  ? 5.588   -11.306 -3.811  1.00 15.48 ? 80  ILE   A CG1 1 
ATOM   579  C CG2 . ILE   A 1 80  ? 3.773   -12.704 -2.714  1.00 15.99 ? 80  ILE   A CG2 1 
ATOM   580  C CD1 . ILE   A 1 80  ? 6.239   -12.463 -4.631  1.00 17.90 ? 80  ILE   A CD1 1 
ATOM   581  N N   . THR   A 1 81  ? 2.874   -10.595 0.153   1.00 14.62 ? 81  THR   A N   1 
ATOM   582  C CA  . THR   A 1 81  ? 2.466   -10.842 1.539   1.00 15.87 ? 81  THR   A CA  1 
ATOM   583  C C   . THR   A 1 81  ? 1.697   -12.159 1.587   1.00 16.52 ? 81  THR   A C   1 
ATOM   584  O O   . THR   A 1 81  ? 0.473   -12.209 1.386   1.00 17.68 ? 81  THR   A O   1 
ATOM   585  C CB  . THR   A 1 81  ? 1.672   -9.652  2.094   1.00 17.50 ? 81  THR   A CB  1 
ATOM   586  O OG1 . THR   A 1 81  ? 2.496   -8.461  2.007   1.00 17.60 ? 81  THR   A OG1 1 
ATOM   587  C CG2 . THR   A 1 81  ? 1.320   -9.911  3.575   1.00 20.56 ? 81  THR   A CG2 1 
ATOM   588  N N   . GLY   A 1 82  ? 2.420   -13.245 1.890   1.00 16.15 ? 82  GLY   A N   1 
ATOM   589  C CA  . GLY   A 1 82  ? 1.838   -14.579 1.855   1.00 15.38 ? 82  GLY   A CA  1 
ATOM   590  C C   . GLY   A 1 82  ? 2.141   -15.220 0.504   1.00 14.95 ? 82  GLY   A C   1 
ATOM   591  O O   . GLY   A 1 82  ? 1.273   -15.338 -0.372  1.00 15.69 ? 82  GLY   A O   1 
ATOM   592  N N   . ALA   A 1 83  ? 3.398   -15.591 0.290   1.00 13.68 ? 83  ALA   A N   1 
ATOM   593  C CA  . ALA   A 1 83  ? 3.779   -16.182 -0.979  1.00 14.68 ? 83  ALA   A CA  1 
ATOM   594  C C   . ALA   A 1 83  ? 3.009   -17.478 -1.225  1.00 14.73 ? 83  ALA   A C   1 
ATOM   595  O O   . ALA   A 1 83  ? 2.719   -18.256 -0.300  1.00 16.53 ? 83  ALA   A O   1 
ATOM   596  C CB  . ALA   A 1 83  ? 5.279   -16.491 -0.987  1.00 17.87 ? 83  ALA   A CB  1 
ATOM   597  N N   . GLN   A 1 84  ? 2.737   -17.743 -2.492  1.00 13.93 ? 84  GLN   A N   1 
ATOM   598  C CA  . GLN   A 1 84  ? 2.077   -18.962 -2.919  1.00 13.74 ? 84  GLN   A CA  1 
ATOM   599  C C   . GLN   A 1 84  ? 3.023   -19.748 -3.831  1.00 13.07 ? 84  GLN   A C   1 
ATOM   600  O O   . GLN   A 1 84  ? 3.923   -19.165 -4.476  1.00 14.10 ? 84  GLN   A O   1 
ATOM   601  C CB  . GLN   A 1 84  ? 0.728   -18.654 -3.575  1.00 15.00 ? 84  GLN   A CB  1 
ATOM   602  C CG  . GLN   A 1 84  ? -0.188  -17.941 -2.559  1.00 14.44 ? 84  GLN   A CG  1 
ATOM   603  C CD  . GLN   A 1 84  ? -1.533  -17.448 -3.073  1.00 15.26 ? 84  GLN   A CD  1 
ATOM   604  O OE1 . GLN   A 1 84  ? -2.199  -16.675 -2.381  1.00 15.52 ? 84  GLN   A OE1 1 
ATOM   605  N NE2 . GLN   A 1 84  ? -1.940  -17.890 -4.252  1.00 15.51 ? 84  GLN   A NE2 1 
ATOM   606  N N   . THR   A 1 85  ? 2.789   -21.069 -3.916  1.00 14.48 ? 85  THR   A N   1 
ATOM   607  C CA  A THR   A 1 85  ? 3.663   -21.948 -4.692  0.77 15.90 ? 85  THR   A CA  1 
ATOM   608  C CA  B THR   A 1 85  ? 3.670   -21.937 -4.686  0.23 15.85 ? 85  THR   A CA  1 
ATOM   609  C C   . THR   A 1 85  ? 3.825   -21.451 -6.122  1.00 15.72 ? 85  THR   A C   1 
ATOM   610  O O   . THR   A 1 85  ? 4.939   -21.473 -6.678  1.00 15.93 ? 85  THR   A O   1 
ATOM   611  C CB  A THR   A 1 85  ? 3.081   -23.361 -4.691  0.77 19.97 ? 85  THR   A CB  1 
ATOM   612  C CB  B THR   A 1 85  ? 3.160   -23.377 -4.606  0.23 17.49 ? 85  THR   A CB  1 
ATOM   613  O OG1 A THR   A 1 85  ? 3.068   -23.856 -3.365  0.77 23.97 ? 85  THR   A OG1 1 
ATOM   614  O OG1 B THR   A 1 85  ? 1.873   -23.505 -5.232  0.23 16.03 ? 85  THR   A OG1 1 
ATOM   615  C CG2 A THR   A 1 85  ? 3.896   -24.314 -5.570  0.77 19.27 ? 85  THR   A CG2 1 
ATOM   616  C CG2 B THR   A 1 85  ? 2.986   -23.710 -3.183  0.23 19.66 ? 85  THR   A CG2 1 
ATOM   617  N N   . GLU   A 1 86  ? 2.714   -20.959 -6.738  1.00 14.73 ? 86  GLU   A N   1 
ATOM   618  C CA  . GLU   A 1 86  ? 2.735   -20.486 -8.118  1.00 15.55 ? 86  GLU   A CA  1 
ATOM   619  C C   . GLU   A 1 86  ? 3.463   -19.172 -8.276  1.00 14.15 ? 86  GLU   A C   1 
ATOM   620  O O   . GLU   A 1 86  ? 3.608   -18.715 -9.418  1.00 15.45 ? 86  GLU   A O   1 
ATOM   621  C CB  . GLU   A 1 86  ? 1.316   -20.383 -8.692  1.00 17.31 ? 86  GLU   A CB  1 
ATOM   622  C CG  . GLU   A 1 86  ? 0.408   -19.364 -7.977  1.00 18.17 ? 86  GLU   A CG  1 
ATOM   623  C CD  . GLU   A 1 86  ? -0.392  -19.987 -6.862  1.00 19.30 ? 86  GLU   A CD  1 
ATOM   624  O OE1 . GLU   A 1 86  ? 0.063   -20.981 -6.240  1.00 20.88 ? 86  GLU   A OE1 1 
ATOM   625  O OE2 . GLU   A 1 86  ? -1.494  -19.457 -6.595  1.00 22.13 ? 86  GLU   A OE2 1 
ATOM   626  N N   . ASP   A 1 87  ? 3.917   -18.545 -7.192  1.00 13.99 ? 87  ASP   A N   1 
ATOM   627  C CA  . ASP   A 1 87  ? 4.684   -17.305 -7.328  1.00 13.22 ? 87  ASP   A CA  1 
ATOM   628  C C   . ASP   A 1 87  ? 6.156   -17.542 -7.650  1.00 14.47 ? 87  ASP   A C   1 
ATOM   629  O O   . ASP   A 1 87  ? 6.908   -16.572 -7.835  1.00 13.68 ? 87  ASP   A O   1 
ATOM   630  C CB  . ASP   A 1 87  ? 4.530   -16.497 -6.048  1.00 13.81 ? 87  ASP   A CB  1 
ATOM   631  C CG  . ASP   A 1 87  ? 3.092   -16.064 -5.812  1.00 14.16 ? 87  ASP   A CG  1 
ATOM   632  O OD1 . ASP   A 1 87  ? 2.309   -15.981 -6.794  1.00 15.89 ? 87  ASP   A OD1 1 
ATOM   633  O OD2 . ASP   A 1 87  ? 2.746   -15.787 -4.653  1.00 14.34 ? 87  ASP   A OD2 1 
ATOM   634  N N   . GLU   A 1 88  ? 6.591   -18.806 -7.734  1.00 13.32 ? 88  GLU   A N   1 
ATOM   635  C CA  . GLU   A 1 88  ? 7.921   -19.115 -8.217  1.00 13.72 ? 88  GLU   A CA  1 
ATOM   636  C C   . GLU   A 1 88  ? 8.044   -18.623 -9.660  1.00 14.84 ? 88  GLU   A C   1 
ATOM   637  O O   . GLU   A 1 88  ? 7.243   -18.989 -10.526 1.00 15.66 ? 88  GLU   A O   1 
ATOM   638  C CB  . GLU   A 1 88  ? 8.168   -20.618 -8.054  1.00 17.07 ? 88  GLU   A CB  1 
ATOM   639  C CG  . GLU   A 1 88  ? 9.445   -21.050 -8.697  1.00 19.28 ? 88  GLU   A CG  1 
ATOM   640  C CD  . GLU   A 1 88  ? 10.007  -22.367 -8.121  1.00 24.23 ? 88  GLU   A CD  1 
ATOM   641  O OE1 . GLU   A 1 88  ? 9.911   -22.615 -6.892  1.00 26.69 ? 88  GLU   A OE1 1 
ATOM   642  O OE2 . GLU   A 1 88  ? 10.572  -23.140 -8.923  1.00 28.77 ? 88  GLU   A OE2 1 
ATOM   643  N N   . ALA   A 1 89  ? 8.993   -17.725 -9.895  1.00 13.79 ? 89  ALA   A N   1 
ATOM   644  C CA  . ALA   A 1 89  ? 9.039   -16.962 -11.144 1.00 12.78 ? 89  ALA   A CA  1 
ATOM   645  C C   . ALA   A 1 89  ? 10.304  -16.109 -11.119 1.00 12.52 ? 89  ALA   A C   1 
ATOM   646  O O   . ALA   A 1 89  ? 10.956  -15.975 -10.074 1.00 14.47 ? 89  ALA   A O   1 
ATOM   647  C CB  . ALA   A 1 89  ? 7.800   -16.070 -11.319 1.00 14.72 ? 89  ALA   A CB  1 
ATOM   648  N N   . ILE   A 1 90  ? 10.583  -15.437 -12.249 1.00 12.59 ? 90  ILE   A N   1 
ATOM   649  C CA  . ILE   A 1 90  ? 11.616  -14.384 -12.281 1.00 13.44 ? 90  ILE   A CA  1 
ATOM   650  C C   . ILE   A 1 90  ? 10.906  -13.047 -12.287 1.00 13.43 ? 90  ILE   A C   1 
ATOM   651  O O   . ILE   A 1 90  ? 9.999   -12.817 -13.102 1.00 16.88 ? 90  ILE   A O   1 
ATOM   652  C CB  . ILE   A 1 90  ? 12.560  -14.526 -13.491 1.00 15.21 ? 90  ILE   A CB  1 
ATOM   653  C CG1 . ILE   A 1 90  ? 13.114  -15.970 -13.546 1.00 17.95 ? 90  ILE   A CG1 1 
ATOM   654  C CG2 . ILE   A 1 90  ? 13.684  -13.473 -13.388 1.00 15.87 ? 90  ILE   A CG2 1 
ATOM   655  C CD1 . ILE   A 1 90  ? 13.898  -16.222 -14.814 1.00 22.67 ? 90  ILE   A CD1 1 
ATOM   656  N N   . TYR   A 1 91  ? 11.295  -12.154 -11.392 1.00 13.39 ? 91  TYR   A N   1 
ATOM   657  C CA  . TYR   A 1 91  ? 10.647  -10.860 -11.265 1.00 13.07 ? 91  TYR   A CA  1 
ATOM   658  C C   . TYR   A 1 91  ? 11.622  -9.809  -11.756 1.00 12.98 ? 91  TYR   A C   1 
ATOM   659  O O   . TYR   A 1 91  ? 12.756  -9.744  -11.273 1.00 14.22 ? 91  TYR   A O   1 
ATOM   660  C CB  . TYR   A 1 91  ? 10.274  -10.597 -9.797  1.00 12.77 ? 91  TYR   A CB  1 
ATOM   661  C CG  . TYR   A 1 91  ? 9.182   -11.511 -9.327  1.00 12.87 ? 91  TYR   A CG  1 
ATOM   662  C CD1 . TYR   A 1 91  ? 9.466   -12.828 -8.902  1.00 13.42 ? 91  TYR   A CD1 1 
ATOM   663  C CD2 . TYR   A 1 91  ? 7.857   -11.103 -9.369  1.00 13.37 ? 91  TYR   A CD2 1 
ATOM   664  C CE1 . TYR   A 1 91  ? 8.449   -13.712 -8.531  1.00 12.66 ? 91  TYR   A CE1 1 
ATOM   665  C CE2 . TYR   A 1 91  ? 6.833   -11.964 -8.984  1.00 14.88 ? 91  TYR   A CE2 1 
ATOM   666  C CZ  . TYR   A 1 91  ? 7.144   -13.252 -8.545  1.00 13.00 ? 91  TYR   A CZ  1 
ATOM   667  O OH  . TYR   A 1 91  ? 6.104   -14.069 -8.204  1.00 13.49 ? 91  TYR   A OH  1 
ATOM   668  N N   . PHE   A 1 92  ? 11.163  -8.941  -12.654 1.00 11.49 ? 92  PHE   A N   1 
ATOM   669  C CA  . PHE   A 1 92  ? 11.993  -7.872  -13.192 1.00 13.11 ? 92  PHE   A CA  1 
ATOM   670  C C   . PHE   A 1 92  ? 11.394  -6.524  -12.848 1.00 13.67 ? 92  PHE   A C   1 
ATOM   671  O O   . PHE   A 1 92  ? 10.175  -6.344  -12.908 1.00 14.15 ? 92  PHE   A O   1 
ATOM   672  C CB  . PHE   A 1 92  ? 12.057  -7.917  -14.722 1.00 14.68 ? 92  PHE   A CB  1 
ATOM   673  C CG  . PHE   A 1 92  ? 12.793  -9.095  -15.274 1.00 13.52 ? 92  PHE   A CG  1 
ATOM   674  C CD1 . PHE   A 1 92  ? 12.127  -10.275 -15.562 1.00 14.44 ? 92  PHE   A CD1 1 
ATOM   675  C CD2 . PHE   A 1 92  ? 14.156  -9.016  -15.525 1.00 15.76 ? 92  PHE   A CD2 1 
ATOM   676  C CE1 . PHE   A 1 92  ? 12.811  -11.361 -16.088 1.00 15.75 ? 92  PHE   A CE1 1 
ATOM   677  C CE2 . PHE   A 1 92  ? 14.838  -10.097 -16.052 1.00 15.01 ? 92  PHE   A CE2 1 
ATOM   678  C CZ  . PHE   A 1 92  ? 14.166  -11.269 -16.337 1.00 15.96 ? 92  PHE   A CZ  1 
ATOM   679  N N   A CYS   A 1 93  ? 12.239  -5.564  -12.462 0.89 13.22 ? 93  CYS   A N   1 
ATOM   680  N N   B CYS   A 1 93  ? 12.278  -5.594  -12.552 0.11 13.22 ? 93  CYS   A N   1 
ATOM   681  C CA  A CYS   A 1 93  ? 11.794  -4.177  -12.389 0.89 13.70 ? 93  CYS   A CA  1 
ATOM   682  C CA  B CYS   A 1 93  ? 11.990  -4.182  -12.479 0.11 13.71 ? 93  CYS   A CA  1 
ATOM   683  C C   A CYS   A 1 93  ? 12.259  -3.427  -13.635 0.89 15.44 ? 93  CYS   A C   1 
ATOM   684  C C   B CYS   A 1 93  ? 12.053  -3.591  -13.873 0.11 15.44 ? 93  CYS   A C   1 
ATOM   685  O O   A CYS   A 1 93  ? 13.253  -3.794  -14.268 0.89 15.75 ? 93  CYS   A O   1 
ATOM   686  O O   B CYS   A 1 93  ? 12.613  -4.178  -14.802 0.11 15.75 ? 93  CYS   A O   1 
ATOM   687  C CB  A CYS   A 1 93  ? 12.305  -3.461  -11.134 0.89 14.74 ? 93  CYS   A CB  1 
ATOM   688  C CB  B CYS   A 1 93  ? 13.128  -3.549  -11.720 0.11 14.74 ? 93  CYS   A CB  1 
ATOM   689  S SG  A CYS   A 1 93  ? 14.086  -3.351  -11.000 0.89 15.44 ? 93  CYS   A SG  1 
ATOM   690  S SG  B CYS   A 1 93  ? 12.751  -2.384  -10.484 0.11 15.42 ? 93  CYS   A SG  1 
ATOM   691  N N   . ALA   A 1 94  ? 11.504  -2.393  -14.003 1.00 14.69 ? 94  ALA   A N   1 
ATOM   692  C CA  . ALA   A 1 94  ? 11.799  -1.566  -15.164 1.00 14.08 ? 94  ALA   A CA  1 
ATOM   693  C C   . ALA   A 1 94  ? 11.702  -0.112  -14.743 1.00 14.63 ? 94  ALA   A C   1 
ATOM   694  O O   . ALA   A 1 94  ? 10.688  0.297   -14.163 1.00 14.54 ? 94  ALA   A O   1 
ATOM   695  C CB  . ALA   A 1 94  ? 10.824  -1.842  -16.312 1.00 17.59 ? 94  ALA   A CB  1 
ATOM   696  N N   . LEU   A 1 95  ? 12.753  0.655   -15.035 1.00 14.48 ? 95  LEU   A N   1 
ATOM   697  C CA  . LEU   A 1 95  ? 12.822  2.081   -14.685 1.00 13.84 ? 95  LEU   A CA  1 
ATOM   698  C C   . LEU   A 1 95  ? 12.866  2.973   -15.918 1.00 14.82 ? 95  LEU   A C   1 
ATOM   699  O O   . LEU   A 1 95  ? 13.596  2.685   -16.896 1.00 15.37 ? 95  LEU   A O   1 
ATOM   700  C CB  . LEU   A 1 95  ? 14.086  2.386   -13.854 1.00 16.42 ? 95  LEU   A CB  1 
ATOM   701  C CG  . LEU   A 1 95  ? 13.975  2.129   -12.338 1.00 17.36 ? 95  LEU   A CG  1 
ATOM   702  C CD1 . LEU   A 1 95  ? 13.717  0.681   -11.987 1.00 18.81 ? 95  LEU   A CD1 1 
ATOM   703  C CD2 . LEU   A 1 95  ? 15.291  2.497   -11.663 1.00 18.51 ? 95  LEU   A CD2 1 
ATOM   704  N N   . TRP   A 1 96  ? 12.117  4.086   -15.845 1.00 15.16 ? 96  TRP   A N   1 
ATOM   705  C CA  . TRP   A 1 96  ? 12.128  5.070   -16.917 1.00 16.00 ? 96  TRP   A CA  1 
ATOM   706  C C   . TRP   A 1 96  ? 13.211  6.118   -16.645 1.00 16.31 ? 96  TRP   A C   1 
ATOM   707  O O   . TRP   A 1 96  ? 13.176  6.796   -15.621 1.00 16.95 ? 96  TRP   A O   1 
ATOM   708  C CB  . TRP   A 1 96  ? 10.756  5.734   -17.014 1.00 15.06 ? 96  TRP   A CB  1 
ATOM   709  C CG  . TRP   A 1 96  ? 10.716  6.826   -18.041 1.00 15.63 ? 96  TRP   A CG  1 
ATOM   710  C CD1 . TRP   A 1 96  ? 10.513  8.151   -17.797 1.00 17.12 ? 96  TRP   A CD1 1 
ATOM   711  C CD2 . TRP   A 1 96  ? 10.826  6.679   -19.459 1.00 16.09 ? 96  TRP   A CD2 1 
ATOM   712  N NE1 . TRP   A 1 96  ? 10.524  8.860   -18.981 1.00 17.77 ? 96  TRP   A NE1 1 
ATOM   713  C CE2 . TRP   A 1 96  ? 10.703  7.974   -20.028 1.00 16.18 ? 96  TRP   A CE2 1 
ATOM   714  C CE3 . TRP   A 1 96  ? 11.014  5.573   -20.310 1.00 15.93 ? 96  TRP   A CE3 1 
ATOM   715  C CZ2 . TRP   A 1 96  ? 10.752  8.206   -21.415 1.00 17.27 ? 96  TRP   A CZ2 1 
ATOM   716  C CZ3 . TRP   A 1 96  ? 11.074  5.799   -21.706 1.00 14.51 ? 96  TRP   A CZ3 1 
ATOM   717  C CH2 . TRP   A 1 96  ? 10.947  7.124   -22.250 1.00 16.50 ? 96  TRP   A CH2 1 
ATOM   718  N N   . TYR   A 1 97  ? 14.153  6.274   -17.576 1.00 17.11 ? 97  TYR   A N   1 
ATOM   719  C CA  . TYR   A 1 97  ? 15.236  7.245   -17.446 1.00 18.02 ? 97  TYR   A CA  1 
ATOM   720  C C   . TYR   A 1 97  ? 15.092  8.261   -18.578 1.00 19.84 ? 97  TYR   A C   1 
ATOM   721  O O   . TYR   A 1 97  ? 15.920  8.312   -19.497 1.00 21.38 ? 97  TYR   A O   1 
ATOM   722  C CB  . TYR   A 1 97  ? 16.598  6.550   -17.488 1.00 18.32 ? 97  TYR   A CB  1 
ATOM   723  C CG  . TYR   A 1 97  ? 17.018  5.805   -16.233 1.00 19.52 ? 97  TYR   A CG  1 
ATOM   724  C CD1 . TYR   A 1 97  ? 17.566  6.490   -15.138 1.00 22.64 ? 97  TYR   A CD1 1 
ATOM   725  C CD2 . TYR   A 1 97  ? 16.879  4.407   -16.146 1.00 21.85 ? 97  TYR   A CD2 1 
ATOM   726  C CE1 . TYR   A 1 97  ? 17.969  5.778   -13.999 1.00 22.57 ? 97  TYR   A CE1 1 
ATOM   727  C CE2 . TYR   A 1 97  ? 17.261  3.713   -15.025 1.00 23.37 ? 97  TYR   A CE2 1 
ATOM   728  C CZ  . TYR   A 1 97  ? 17.821  4.388   -13.956 1.00 25.25 ? 97  TYR   A CZ  1 
ATOM   729  O OH  . TYR   A 1 97  ? 18.246  3.649   -12.855 1.00 26.62 ? 97  TYR   A OH  1 
ATOM   730  N N   . SER   A 1 98  ? 13.984  9.016   -18.552 1.00 22.28 ? 98  SER   A N   1 
ATOM   731  C CA  . SER   A 1 98  ? 13.799  10.249  -19.303 1.00 25.09 ? 98  SER   A CA  1 
ATOM   732  C C   . SER   A 1 98  ? 13.516  10.030  -20.787 1.00 21.77 ? 98  SER   A C   1 
ATOM   733  O O   . SER   A 1 98  ? 12.698  10.751  -21.382 1.00 22.91 ? 98  SER   A O   1 
ATOM   734  C CB  . SER   A 1 98  ? 15.042  11.123  -19.101 1.00 29.96 ? 98  SER   A CB  1 
ATOM   735  O OG  . SER   A 1 98  ? 14.898  11.825  -17.886 1.00 33.55 ? 98  SER   A OG  1 
ATOM   736  N N   . ASN   A 1 99  ? 14.226  9.083   -21.421 1.00 21.73 ? 99  ASN   A N   1 
ATOM   737  C CA  . ASN   A 1 99  ? 13.965  8.779   -22.823 1.00 21.69 ? 99  ASN   A CA  1 
ATOM   738  C C   . ASN   A 1 99  ? 14.183  7.301   -23.144 1.00 18.97 ? 99  ASN   A C   1 
ATOM   739  O O   . ASN   A 1 99  ? 14.154  6.928   -24.336 1.00 20.49 ? 99  ASN   A O   1 
ATOM   740  C CB  . ASN   A 1 99  ? 14.748  9.662   -23.830 1.00 24.08 ? 99  ASN   A CB  1 
ATOM   741  C CG  . ASN   A 1 99  ? 16.253  9.577   -23.631 1.00 27.24 ? 99  ASN   A CG  1 
ATOM   742  O OD1 . ASN   A 1 99  ? 16.712  8.777   -22.822 1.00 26.89 ? 99  ASN   A OD1 1 
ATOM   743  N ND2 . ASN   A 1 99  ? 17.028  10.405  -24.357 1.00 28.39 ? 99  ASN   A ND2 1 
ATOM   744  N N   . HIS   A 1 100 ? 14.371  6.436   -22.146 1.00 16.74 ? 100 HIS   A N   1 
ATOM   745  C CA  . HIS   A 1 100 ? 14.463  4.996   -22.414 1.00 16.51 ? 100 HIS   A CA  1 
ATOM   746  C C   . HIS   A 1 100 ? 14.134  4.254   -21.134 1.00 16.41 ? 100 HIS   A C   1 
ATOM   747  O O   . HIS   A 1 100 ? 14.269  4.806   -20.035 1.00 17.73 ? 100 HIS   A O   1 
ATOM   748  C CB  . HIS   A 1 100 ? 15.844  4.588   -22.970 1.00 19.29 ? 100 HIS   A CB  1 
ATOM   749  C CG  . HIS   A 1 100 ? 16.981  4.802   -22.013 1.00 23.50 ? 100 HIS   A CG  1 
ATOM   750  N ND1 . HIS   A 1 100 ? 17.378  6.056   -21.594 1.00 27.55 ? 100 HIS   A ND1 1 
ATOM   751  C CD2 . HIS   A 1 100 ? 17.817  3.922   -21.414 1.00 26.54 ? 100 HIS   A CD2 1 
ATOM   752  C CE1 . HIS   A 1 100 ? 18.391  5.935   -20.750 1.00 27.94 ? 100 HIS   A CE1 1 
ATOM   753  N NE2 . HIS   A 1 100 ? 18.689  4.654   -20.640 1.00 26.93 ? 100 HIS   A NE2 1 
ATOM   754  N N   . TRP   A 1 101 ? 13.707  3.005   -21.289 1.00 15.23 ? 101 TRP   A N   1 
ATOM   755  C CA  . TRP   A 1 101 ? 13.514  2.114   -20.143 1.00 13.72 ? 101 TRP   A CA  1 
ATOM   756  C C   . TRP   A 1 101 ? 14.741  1.230   -19.936 1.00 14.54 ? 101 TRP   A C   1 
ATOM   757  O O   . TRP   A 1 101 ? 15.356  0.770   -20.907 1.00 16.23 ? 101 TRP   A O   1 
ATOM   758  C CB  . TRP   A 1 101 ? 12.323  1.160   -20.390 1.00 14.11 ? 101 TRP   A CB  1 
ATOM   759  C CG  . TRP   A 1 101 ? 10.980  1.846   -20.326 1.00 13.77 ? 101 TRP   A CG  1 
ATOM   760  C CD1 . TRP   A 1 101 ? 10.306  2.444   -21.369 1.00 14.42 ? 101 TRP   A CD1 1 
ATOM   761  C CD2 . TRP   A 1 101 ? 10.182  2.062   -19.156 1.00 14.17 ? 101 TRP   A CD2 1 
ATOM   762  N NE1 . TRP   A 1 101 ? 9.134   2.980   -20.921 1.00 16.03 ? 101 TRP   A NE1 1 
ATOM   763  C CE2 . TRP   A 1 101 ? 9.033   2.784   -19.570 1.00 14.53 ? 101 TRP   A CE2 1 
ATOM   764  C CE3 . TRP   A 1 101 ? 10.318  1.711   -17.801 1.00 15.20 ? 101 TRP   A CE3 1 
ATOM   765  C CZ2 . TRP   A 1 101 ? 7.990   3.143   -18.693 1.00 15.06 ? 101 TRP   A CZ2 1 
ATOM   766  C CZ3 . TRP   A 1 101 ? 9.289   2.074   -16.917 1.00 15.28 ? 101 TRP   A CZ3 1 
ATOM   767  C CH2 . TRP   A 1 101 ? 8.135   2.796   -17.373 1.00 15.52 ? 101 TRP   A CH2 1 
ATOM   768  N N   . VAL   A 1 102 ? 15.064  0.958   -18.669 1.00 15.94 ? 102 VAL   A N   1 
ATOM   769  C CA  . VAL   A 1 102 ? 16.131  0.024   -18.308 1.00 15.06 ? 102 VAL   A CA  1 
ATOM   770  C C   . VAL   A 1 102 ? 15.544  -1.026  -17.371 1.00 15.29 ? 102 VAL   A C   1 
ATOM   771  O O   . VAL   A 1 102 ? 14.897  -0.673  -16.372 1.00 15.29 ? 102 VAL   A O   1 
ATOM   772  C CB  . VAL   A 1 102 ? 17.308  0.745   -17.610 1.00 16.04 ? 102 VAL   A CB  1 
ATOM   773  C CG1 . VAL   A 1 102 ? 18.429  -0.291  -17.268 1.00 18.41 ? 102 VAL   A CG1 1 
ATOM   774  C CG2 . VAL   A 1 102 ? 17.876  1.836   -18.542 1.00 18.14 ? 102 VAL   A CG2 1 
ATOM   775  N N   . PHE   A 1 103 ? 15.808  -2.305  -17.663 1.00 14.12 ? 103 PHE   A N   1 
ATOM   776  C CA  . PHE   A 1 103 ? 15.359  -3.393  -16.811 1.00 14.80 ? 103 PHE   A CA  1 
ATOM   777  C C   . PHE   A 1 103 ? 16.474  -3.809  -15.849 1.00 15.16 ? 103 PHE   A C   1 
ATOM   778  O O   . PHE   A 1 103 ? 17.663  -3.814  -16.200 1.00 16.06 ? 103 PHE   A O   1 
ATOM   779  C CB  . PHE   A 1 103 ? 14.966  -4.605  -17.689 1.00 14.06 ? 103 PHE   A CB  1 
ATOM   780  C CG  . PHE   A 1 103 ? 13.654  -4.429  -18.420 1.00 15.54 ? 103 PHE   A CG  1 
ATOM   781  C CD1 . PHE   A 1 103 ? 13.630  -3.900  -19.713 1.00 17.53 ? 103 PHE   A CD1 1 
ATOM   782  C CD2 . PHE   A 1 103 ? 12.454  -4.840  -17.854 1.00 16.08 ? 103 PHE   A CD2 1 
ATOM   783  C CE1 . PHE   A 1 103 ? 12.451  -3.758  -20.426 1.00 19.67 ? 103 PHE   A CE1 1 
ATOM   784  C CE2 . PHE   A 1 103 ? 11.227  -4.702  -18.579 1.00 16.93 ? 103 PHE   A CE2 1 
ATOM   785  C CZ  . PHE   A 1 103 ? 11.231  -4.136  -19.866 1.00 19.97 ? 103 PHE   A CZ  1 
ATOM   786  N N   . GLY   A 1 104 ? 16.071  -4.235  -14.651 1.00 14.94 ? 104 GLY   A N   1 
ATOM   787  C CA  . GLY   A 1 104 ? 16.967  -4.929  -13.765 1.00 16.36 ? 104 GLY   A CA  1 
ATOM   788  C C   . GLY   A 1 104 ? 17.296  -6.298  -14.308 1.00 15.85 ? 104 GLY   A C   1 
ATOM   789  O O   . GLY   A 1 104 ? 16.735  -6.772  -15.310 1.00 16.29 ? 104 GLY   A O   1 
ATOM   790  N N   . GLY   A 1 105 ? 18.259  -6.947  -13.639 1.00 14.54 ? 105 GLY   A N   1 
ATOM   791  C CA  . GLY   A 1 105 ? 18.692  -8.285  -14.051 1.00 14.29 ? 105 GLY   A CA  1 
ATOM   792  C C   . GLY   A 1 105 ? 17.739  -9.401  -13.645 1.00 15.17 ? 105 GLY   A C   1 
ATOM   793  O O   . GLY   A 1 105 ? 17.949  -10.536 -14.086 1.00 18.10 ? 105 GLY   A O   1 
ATOM   794  N N   . GLY   A 1 106 ? 16.675  -9.108  -12.886 1.00 14.64 ? 106 GLY   A N   1 
ATOM   795  C CA  . GLY   A 1 106 ? 15.683  -10.115 -12.513 1.00 15.10 ? 106 GLY   A CA  1 
ATOM   796  C C   . GLY   A 1 106 ? 16.097  -10.836 -11.255 1.00 14.15 ? 106 GLY   A C   1 
ATOM   797  O O   . GLY   A 1 106 ? 17.278  -11.111 -11.019 1.00 16.32 ? 106 GLY   A O   1 
ATOM   798  N N   . THR   A 1 107 ? 15.096  -11.213 -10.454 1.00 13.10 ? 107 THR   A N   1 
ATOM   799  C CA  . THR   A 1 107 ? 15.260  -12.021 -9.246  1.00 12.70 ? 107 THR   A CA  1 
ATOM   800  C C   . THR   A 1 107 ? 14.514  -13.321 -9.448  1.00 13.19 ? 107 THR   A C   1 
ATOM   801  O O   . THR   A 1 107 ? 13.291  -13.318 -9.664  1.00 13.41 ? 107 THR   A O   1 
ATOM   802  C CB  . THR   A 1 107 ? 14.659  -11.293 -8.039  1.00 13.82 ? 107 THR   A CB  1 
ATOM   803  O OG1 . THR   A 1 107 ? 15.389  -10.090 -7.811  1.00 14.99 ? 107 THR   A OG1 1 
ATOM   804  C CG2 . THR   A 1 107 ? 14.783  -12.153 -6.751  1.00 16.29 ? 107 THR   A CG2 1 
ATOM   805  N N   . LYS   A 1 108 ? 15.246  -14.432 -9.364  1.00 14.12 ? 108 LYS   A N   1 
ATOM   806  C CA  A LYS   A 1 108 ? 14.627  -15.754 -9.383  0.49 14.27 ? 108 LYS   A CA  1 
ATOM   807  C CA  B LYS   A 1 108 ? 14.646  -15.759 -9.385  0.51 14.66 ? 108 LYS   A CA  1 
ATOM   808  C C   . LYS   A 1 108 ? 14.115  -16.081 -7.991  1.00 13.85 ? 108 LYS   A C   1 
ATOM   809  O O   . LYS   A 1 108 ? 14.904  -16.306 -7.056  1.00 16.26 ? 108 LYS   A O   1 
ATOM   810  C CB  A LYS   A 1 108 ? 15.621  -16.821 -9.827  0.49 15.50 ? 108 LYS   A CB  1 
ATOM   811  C CB  B LYS   A 1 108 ? 15.728  -16.758 -9.784  0.51 16.66 ? 108 LYS   A CB  1 
ATOM   812  C CG  A LYS   A 1 108 ? 14.997  -18.224 -9.941  0.49 18.58 ? 108 LYS   A CG  1 
ATOM   813  C CG  B LYS   A 1 108 ? 16.290  -16.538 -11.208 0.51 19.62 ? 108 LYS   A CG  1 
ATOM   814  C CD  A LYS   A 1 108 ? 13.572  -18.130 -10.572 0.49 23.65 ? 108 LYS   A CD  1 
ATOM   815  C CD  B LYS   A 1 108 ? 17.430  -17.494 -11.528 0.51 25.81 ? 108 LYS   A CD  1 
ATOM   816  C CE  A LYS   A 1 108 ? 12.646  -19.255 -10.182 0.49 24.86 ? 108 LYS   A CE  1 
ATOM   817  C CE  B LYS   A 1 108 ? 17.935  -17.279 -12.932 0.51 29.87 ? 108 LYS   A CE  1 
ATOM   818  N NZ  A LYS   A 1 108 ? 13.395  -20.536 -10.391 0.49 27.80 ? 108 LYS   A NZ  1 
ATOM   819  N NZ  B LYS   A 1 108 ? 19.079  -18.197 -13.197 0.51 33.81 ? 108 LYS   A NZ  1 
ATOM   820  N N   . LEU   A 1 109 ? 12.792  -16.092 -7.849  1.00 13.93 ? 109 LEU   A N   1 
ATOM   821  C CA  . LEU   A 1 109 ? 12.162  -16.421 -6.579  1.00 14.16 ? 109 LEU   A CA  1 
ATOM   822  C C   . LEU   A 1 109 ? 11.834  -17.908 -6.596  1.00 15.82 ? 109 LEU   A C   1 
ATOM   823  O O   . LEU   A 1 109 ? 11.043  -18.362 -7.445  1.00 15.35 ? 109 LEU   A O   1 
ATOM   824  C CB  . LEU   A 1 109 ? 10.858  -15.619 -6.411  1.00 14.55 ? 109 LEU   A CB  1 
ATOM   825  C CG  . LEU   A 1 109 ? 10.217  -15.880 -5.041  1.00 14.59 ? 109 LEU   A CG  1 
ATOM   826  C CD1 . LEU   A 1 109 ? 11.090  -15.431 -3.846  1.00 17.50 ? 109 LEU   A CD1 1 
ATOM   827  C CD2 . LEU   A 1 109 ? 8.837   -15.204 -4.978  1.00 15.74 ? 109 LEU   A CD2 1 
ATOM   828  N N   . THR   A 1 110 ? 12.412  -18.666 -5.655  1.00 14.64 ? 110 THR   A N   1 
ATOM   829  C CA  . THR   A 1 110 ? 12.019  -20.048 -5.428  1.00 16.66 ? 110 THR   A CA  1 
ATOM   830  C C   . THR   A 1 110 ? 11.038  -20.095 -4.249  1.00 16.26 ? 110 THR   A C   1 
ATOM   831  O O   . THR   A 1 110 ? 11.256  -19.441 -3.225  1.00 17.81 ? 110 THR   A O   1 
ATOM   832  C CB  . THR   A 1 110 ? 13.277  -20.888 -5.085  1.00 20.40 ? 110 THR   A CB  1 
ATOM   833  O OG1 . THR   A 1 110 ? 14.111  -20.926 -6.248  1.00 25.66 ? 110 THR   A OG1 1 
ATOM   834  C CG2 . THR   A 1 110 ? 12.901  -22.306 -4.745  1.00 22.46 ? 110 THR   A CG2 1 
ATOM   835  N N   . VAL   A 1 111 ? 9.959   -20.862 -4.377  1.00 17.38 ? 111 VAL   A N   1 
ATOM   836  C CA  . VAL   A 1 111 ? 9.004   -21.036 -3.275  1.00 18.16 ? 111 VAL   A CA  1 
ATOM   837  C C   . VAL   A 1 111 ? 9.025   -22.519 -2.911  1.00 19.75 ? 111 VAL   A C   1 
ATOM   838  O O   . VAL   A 1 111 ? 8.489   -23.342 -3.657  1.00 22.32 ? 111 VAL   A O   1 
ATOM   839  C CB  . VAL   A 1 111 ? 7.586   -20.555 -3.637  1.00 18.52 ? 111 VAL   A CB  1 
ATOM   840  C CG1 . VAL   A 1 111 ? 6.670   -20.673 -2.431  1.00 19.26 ? 111 VAL   A CG1 1 
ATOM   841  C CG2 . VAL   A 1 111 ? 7.618   -19.094 -4.155  1.00 18.41 ? 111 VAL   A CG2 1 
ATOM   842  N N   . LEU   A 1 112 ? 9.662   -22.830 -1.785  1.00 20.98 ? 112 LEU   A N   1 
ATOM   843  C CA  . LEU   A 1 112 ? 9.854   -24.231 -1.340  1.00 24.18 ? 112 LEU   A CA  1 
ATOM   844  C C   . LEU   A 1 112 ? 8.874   -24.588 -0.226  1.00 29.05 ? 112 LEU   A C   1 
ATOM   845  O O   . LEU   A 1 112 ? 8.865   -23.900 0.783   1.00 30.00 ? 112 LEU   A O   1 
ATOM   846  C CB  . LEU   A 1 112 ? 11.268  -24.325 -0.751  1.00 26.88 ? 112 LEU   A CB  1 
ATOM   847  C CG  . LEU   A 1 112 ? 12.450  -24.424 -1.707  1.00 33.76 ? 112 LEU   A CG  1 
ATOM   848  C CD1 . LEU   A 1 112 ? 13.718  -24.683 -0.907  1.00 30.85 ? 112 LEU   A CD1 1 
ATOM   849  C CD2 . LEU   A 1 112 ? 12.240  -25.529 -2.728  1.00 37.67 ? 112 LEU   A CD2 1 
ATOM   850  N N   . GLY   A 1 113 ? 8.141   -25.674 -0.398  1.00 32.84 ? 113 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 113 ? 7.311   -26.131 0.705   1.00 40.03 ? 113 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 113 ? 5.885   -26.417 0.276   1.00 42.85 ? 113 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 113 ? 5.572   -26.481 -0.924  1.00 46.02 ? 113 GLY   A O   1 
ATOM   854  N N   . GLN   A 1 114 ? 5.049   -26.619 1.307   1.00 42.20 ? 114 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 114 ? 3.663   -27.121 1.092   1.00 45.79 ? 114 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 114 ? 2.854   -26.381 0.037   1.00 38.59 ? 114 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 114 ? 2.540   -25.239 0.274   1.00 40.56 ? 114 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 114 ? 2.878   -27.183 2.420   1.00 49.87 ? 114 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 114 ? 2.912   -25.931 3.289   1.00 49.66 ? 114 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 114 ? 2.320   -26.175 4.659   1.00 45.23 ? 114 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 114 ? 1.106   -26.138 4.867   1.00 45.43 ? 114 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 114 ? 3.185   -26.438 5.622   1.00 34.57 ? 114 GLN   A NE2 1 
ATOM   863  N N   . GLY   A 1 115 ? 2.582   -27.026 -1.091  1.00 33.32 ? 115 GLY   A N   1 
ATOM   864  C CA  . GLY   A 1 115 ? 1.653   -26.478 -2.057  1.00 33.47 ? 115 GLY   A CA  1 
ATOM   865  C C   . GLY   A 1 115 ? 0.219   -26.597 -1.597  1.00 31.11 ? 115 GLY   A C   1 
ATOM   866  O O   . GLY   A 1 115 ? -0.083  -27.256 -0.602  1.00 27.28 ? 115 GLY   A O   1 
ATOM   867  N N   . GLY   A 1 116 ? -0.684  -25.926 -2.338  1.00 31.27 ? 116 GLY   A N   1 
ATOM   868  C CA  . GLY   A 1 116 ? -2.117  -26.086 -2.174  1.00 33.30 ? 116 GLY   A CA  1 
ATOM   869  C C   . GLY   A 1 116 ? -2.801  -24.942 -1.461  1.00 31.92 ? 116 GLY   A C   1 
ATOM   870  O O   . GLY   A 1 116 ? -4.049  -24.922 -1.392  1.00 31.76 ? 116 GLY   A O   1 
ATOM   871  N N   . GLY   A 1 117 ? -2.042  -24.006 -0.906  1.00 27.97 ? 117 GLY   A N   1 
ATOM   872  C CA  . GLY   A 1 117 ? -2.626  -22.886 -0.212  1.00 23.24 ? 117 GLY   A CA  1 
ATOM   873  C C   . GLY   A 1 117 ? -2.585  -21.623 -1.050  1.00 19.94 ? 117 GLY   A C   1 
ATOM   874  O O   . GLY   A 1 117 ? -1.633  -21.360 -1.788  1.00 25.00 ? 117 GLY   A O   1 
ATOM   875  N N   . GLY   A 1 118 ? -3.583  -20.798 -0.874  1.00 16.84 ? 118 GLY   A N   1 
ATOM   876  C CA  . GLY   A 1 118 ? -3.494  -19.466 -1.427  1.00 17.90 ? 118 GLY   A CA  1 
ATOM   877  C C   . GLY   A 1 118 ? -4.819  -18.972 -1.947  1.00 18.36 ? 118 GLY   A C   1 
ATOM   878  O O   . GLY   A 1 118 ? -5.811  -19.699 -1.987  1.00 20.21 ? 118 GLY   A O   1 
ATOM   879  N N   . SER   A 1 119 ? -4.821  -17.733 -2.407  1.00 19.45 ? 119 SER   A N   1 
ATOM   880  C CA  . SER   A 1 119 ? -5.995  -17.117 -2.995  1.00 20.84 ? 119 SER   A CA  1 
ATOM   881  C C   . SER   A 1 119 ? -5.887  -17.187 -4.511  1.00 25.39 ? 119 SER   A C   1 
ATOM   882  O O   . SER   A 1 119 ? -4.791  -17.049 -5.067  1.00 24.32 ? 119 SER   A O   1 
ATOM   883  C CB  . SER   A 1 119 ? -6.030  -15.655 -2.540  1.00 24.66 ? 119 SER   A CB  1 
ATOM   884  O OG  . SER   A 1 119 ? -7.194  -15.029 -2.996  1.00 25.77 ? 119 SER   A OG  1 
ATOM   885  N N   . GLY   A 1 120 ? -7.015  -17.397 -5.184  1.00 29.96 ? 120 GLY   A N   1 
ATOM   886  C CA  . GLY   A 1 120 ? -7.003  -17.435 -6.645  1.00 34.54 ? 120 GLY   A CA  1 
ATOM   887  C C   . GLY   A 1 120 ? -7.097  -16.064 -7.304  1.00 39.15 ? 120 GLY   A C   1 
ATOM   888  O O   . GLY   A 1 120 ? -7.049  -15.014 -6.615  1.00 41.38 ? 120 GLY   A O   1 
ATOM   889  N N   . SER   A 1 129 ? -8.738  -13.669 -19.128 1.00 63.74 ? 129 SER   A N   1 
ATOM   890  C CA  . SER   A 1 129 ? -8.023  -12.463 -19.558 1.00 62.65 ? 129 SER   A CA  1 
ATOM   891  C C   . SER   A 1 129 ? -8.790  -11.712 -20.652 1.00 59.01 ? 129 SER   A C   1 
ATOM   892  O O   . SER   A 1 129 ? -9.114  -12.296 -21.679 1.00 60.31 ? 129 SER   A O   1 
ATOM   893  C CB  . SER   A 1 129 ? -6.633  -12.841 -20.078 1.00 64.96 ? 129 SER   A CB  1 
ATOM   894  O OG  . SER   A 1 129 ? -5.825  -11.690 -20.261 1.00 66.54 ? 129 SER   A OG  1 
ATOM   895  N N   . GLN   A 1 130 ? -9.098  -10.425 -20.435 1.00 53.97 ? 130 GLN   A N   1 
ATOM   896  C CA  . GLN   A 1 130 ? -9.701  -9.633  -21.510 1.00 49.36 ? 130 GLN   A CA  1 
ATOM   897  C C   . GLN   A 1 130 ? -8.673  -9.308  -22.581 1.00 36.83 ? 130 GLN   A C   1 
ATOM   898  O O   . GLN   A 1 130 ? -8.925  -9.481  -23.778 1.00 36.33 ? 130 GLN   A O   1 
ATOM   899  C CB  . GLN   A 1 130 ? -10.312 -8.325  -20.984 1.00 57.91 ? 130 GLN   A CB  1 
ATOM   900  C CG  . GLN   A 1 130 ? -11.529 -8.454  -20.096 1.00 67.47 ? 130 GLN   A CG  1 
ATOM   901  C CD  . GLN   A 1 130 ? -12.038 -7.112  -19.589 1.00 78.53 ? 130 GLN   A CD  1 
ATOM   902  O OE1 . GLN   A 1 130 ? -11.282 -6.142  -19.495 1.00 80.64 ? 130 GLN   A OE1 1 
ATOM   903  N NE2 . GLN   A 1 130 ? -13.333 -7.048  -19.274 1.00 84.84 ? 130 GLN   A NE2 1 
ATOM   904  N N   . VAL   A 1 131 ? -7.506  -8.839  -22.171 1.00 27.44 ? 131 VAL   A N   1 
ATOM   905  C CA  . VAL   A 1 131 ? -6.524  -8.313  -23.100 1.00 23.84 ? 131 VAL   A CA  1 
ATOM   906  C C   . VAL   A 1 131 ? -5.617  -9.451  -23.568 1.00 22.48 ? 131 VAL   A C   1 
ATOM   907  O O   . VAL   A 1 131 ? -5.096  -10.220 -22.749 1.00 24.64 ? 131 VAL   A O   1 
ATOM   908  C CB  . VAL   A 1 131 ? -5.716  -7.193  -22.431 1.00 23.31 ? 131 VAL   A CB  1 
ATOM   909  C CG1 . VAL   A 1 131 ? -4.571  -6.761  -23.323 1.00 23.72 ? 131 VAL   A CG1 1 
ATOM   910  C CG2 . VAL   A 1 131 ? -6.650  -6.000  -22.053 1.00 23.35 ? 131 VAL   A CG2 1 
ATOM   911  N N   . GLN   A 1 132 ? -5.413  -9.556  -24.891 1.00 22.56 ? 132 GLN   A N   1 
ATOM   912  C CA  . GLN   A 1 132 ? -4.448  -10.500 -25.430 1.00 23.58 ? 132 GLN   A CA  1 
ATOM   913  C C   . GLN   A 1 132 ? -3.625  -9.845  -26.526 1.00 21.96 ? 132 GLN   A C   1 
ATOM   914  O O   . GLN   A 1 132 ? -4.166  -9.124  -27.372 1.00 21.94 ? 132 GLN   A O   1 
ATOM   915  C CB  . GLN   A 1 132 ? -5.162  -11.709 -26.052 1.00 30.75 ? 132 GLN   A CB  1 
ATOM   916  C CG  . GLN   A 1 132 ? -5.986  -12.455 -25.051 1.00 43.40 ? 132 GLN   A CG  1 
ATOM   917  C CD  . GLN   A 1 132 ? -6.240  -13.894 -25.446 1.00 55.72 ? 132 GLN   A CD  1 
ATOM   918  O OE1 . GLN   A 1 132 ? -5.899  -14.321 -26.553 1.00 58.94 ? 132 GLN   A OE1 1 
ATOM   919  N NE2 . GLN   A 1 132 ? -6.829  -14.660 -24.529 1.00 61.35 ? 132 GLN   A NE2 1 
ATOM   920  N N   . LEU   A 1 133 ? -2.322  -10.117 -26.516 1.00 19.92 ? 133 LEU   A N   1 
ATOM   921  C CA  A LEU   A 1 133 ? -1.408  -9.709  -27.578 0.59 18.53 ? 133 LEU   A CA  1 
ATOM   922  C CA  B LEU   A 1 133 ? -1.405  -9.711  -27.577 0.41 19.32 ? 133 LEU   A CA  1 
ATOM   923  C C   . LEU   A 1 133 ? -0.904  -10.983 -28.246 1.00 19.47 ? 133 LEU   A C   1 
ATOM   924  O O   . LEU   A 1 133 ? -0.316  -11.842 -27.580 1.00 21.78 ? 133 LEU   A O   1 
ATOM   925  C CB  A LEU   A 1 133 ? -0.244  -8.896  -27.006 0.59 17.28 ? 133 LEU   A CB  1 
ATOM   926  C CB  B LEU   A 1 133 ? -0.225  -8.928  -27.001 0.41 19.02 ? 133 LEU   A CB  1 
ATOM   927  C CG  A LEU   A 1 133 ? -0.506  -7.408  -26.718 0.59 15.74 ? 133 LEU   A CG  1 
ATOM   928  C CG  B LEU   A 1 133 ? -0.570  -7.598  -26.334 0.41 19.11 ? 133 LEU   A CG  1 
ATOM   929  C CD1 A LEU   A 1 133 ? -1.696  -7.155  -25.787 0.59 17.57 ? 133 LEU   A CD1 1 
ATOM   930  C CD1 B LEU   A 1 133 ? 0.696   -6.890  -25.862 0.41 20.31 ? 133 LEU   A CD1 1 
ATOM   931  C CD2 A LEU   A 1 133 ? 0.760   -6.750  -26.159 0.59 17.58 ? 133 LEU   A CD2 1 
ATOM   932  C CD2 B LEU   A 1 133 ? -1.347  -6.717  -27.294 0.41 20.16 ? 133 LEU   A CD2 1 
ATOM   933  N N   . GLN   A 1 134 ? -1.142  -11.115 -29.555 1.00 20.42 ? 134 GLN   A N   1 
ATOM   934  C CA  A GLN   A 1 134 ? -0.836  -12.342 -30.284 0.59 22.20 ? 134 GLN   A CA  1 
ATOM   935  C CA  B GLN   A 1 134 ? -0.849  -12.338 -30.298 0.41 22.20 ? 134 GLN   A CA  1 
ATOM   936  C C   . GLN   A 1 134 ? 0.357   -12.111 -31.204 1.00 19.45 ? 134 GLN   A C   1 
ATOM   937  O O   . GLN   A 1 134 ? 0.314   -11.247 -32.091 1.00 20.05 ? 134 GLN   A O   1 
ATOM   938  C CB  A GLN   A 1 134 ? -2.054  -12.826 -31.073 0.59 27.62 ? 134 GLN   A CB  1 
ATOM   939  C CB  B GLN   A 1 134 ? -2.069  -12.741 -31.130 0.41 27.62 ? 134 GLN   A CB  1 
ATOM   940  C CG  A GLN   A 1 134 ? -1.760  -13.948 -32.078 0.59 39.29 ? 134 GLN   A CG  1 
ATOM   941  C CG  B GLN   A 1 134 ? -1.894  -14.011 -31.957 0.41 39.29 ? 134 GLN   A CG  1 
ATOM   942  C CD  A GLN   A 1 134 ? -1.235  -15.227 -31.429 0.59 52.21 ? 134 GLN   A CD  1 
ATOM   943  C CD  B GLN   A 1 134 ? -1.943  -13.755 -33.456 0.41 52.21 ? 134 GLN   A CD  1 
ATOM   944  O OE1 A GLN   A 1 134 ? -1.516  -15.511 -30.264 0.59 54.30 ? 134 GLN   A OE1 1 
ATOM   945  O OE1 B GLN   A 1 134 ? -2.948  -13.274 -33.983 0.41 54.30 ? 134 GLN   A OE1 1 
ATOM   946  N NE2 A GLN   A 1 134 ? -0.476  -16.009 -32.192 0.59 58.20 ? 134 GLN   A NE2 1 
ATOM   947  N NE2 B GLN   A 1 134 ? -0.857  -14.083 -34.150 0.41 58.20 ? 134 GLN   A NE2 1 
ATOM   948  N N   . GLN   A 1 135 ? 1.421   -12.886 -30.986 1.00 17.70 ? 135 GLN   A N   1 
ATOM   949  C CA  . GLN   A 1 135 ? 2.622   -12.857 -31.797 1.00 17.87 ? 135 GLN   A CA  1 
ATOM   950  C C   . GLN   A 1 135 ? 2.865   -14.252 -32.366 1.00 18.27 ? 135 GLN   A C   1 
ATOM   951  O O   . GLN   A 1 135 ? 2.614   -15.247 -31.677 1.00 20.05 ? 135 GLN   A O   1 
ATOM   952  C CB  . GLN   A 1 135 ? 3.841   -12.500 -30.929 1.00 17.61 ? 135 GLN   A CB  1 
ATOM   953  C CG  . GLN   A 1 135 ? 3.880   -11.108 -30.349 1.00 16.86 ? 135 GLN   A CG  1 
ATOM   954  C CD  . GLN   A 1 135 ? 5.180   -10.882 -29.594 1.00 16.18 ? 135 GLN   A CD  1 
ATOM   955  O OE1 . GLN   A 1 135 ? 5.243   -11.075 -28.383 1.00 15.94 ? 135 GLN   A OE1 1 
ATOM   956  N NE2 . GLN   A 1 135 ? 6.224   -10.468 -30.307 1.00 18.36 ? 135 GLN   A NE2 1 
ATOM   957  N N   . PRO   A 1 136 ? 3.365   -14.366 -33.598 1.00 20.17 ? 136 PRO   A N   1 
ATOM   958  C CA  . PRO   A 1 136 ? 3.808   -15.679 -34.076 1.00 20.57 ? 136 PRO   A CA  1 
ATOM   959  C C   . PRO   A 1 136 ? 4.919   -16.237 -33.198 1.00 20.93 ? 136 PRO   A C   1 
ATOM   960  O O   . PRO   A 1 136 ? 5.768   -15.505 -32.674 1.00 21.77 ? 136 PRO   A O   1 
ATOM   961  C CB  . PRO   A 1 136 ? 4.309   -15.406 -35.501 1.00 23.67 ? 136 PRO   A CB  1 
ATOM   962  C CG  . PRO   A 1 136 ? 3.912   -14.027 -35.842 1.00 26.84 ? 136 PRO   A CG  1 
ATOM   963  C CD  . PRO   A 1 136 ? 3.565   -13.288 -34.591 1.00 20.95 ? 136 PRO   A CD  1 
ATOM   964  N N   . GLY   A 1 137 ? 4.939   -17.558 -33.066 1.00 21.11 ? 137 GLY   A N   1 
ATOM   965  C CA  . GLY   A 1 137 ? 5.918   -18.166 -32.189 1.00 19.98 ? 137 GLY   A CA  1 
ATOM   966  C C   . GLY   A 1 137 ? 7.342   -18.107 -32.704 1.00 19.62 ? 137 GLY   A C   1 
ATOM   967  O O   . GLY   A 1 137 ? 8.269   -18.021 -31.907 1.00 20.01 ? 137 GLY   A O   1 
ATOM   968  N N   . ALA   A 1 138 ? 7.540   -18.080 -34.023 1.00 20.59 ? 138 ALA   A N   1 
ATOM   969  C CA  . ALA   A 1 138 ? 8.897   -18.224 -34.534 1.00 20.42 ? 138 ALA   A CA  1 
ATOM   970  C C   . ALA   A 1 138 ? 9.009   -17.587 -35.914 1.00 21.60 ? 138 ALA   A C   1 
ATOM   971  O O   . ALA   A 1 138 ? 8.039   -17.549 -36.680 1.00 25.13 ? 138 ALA   A O   1 
ATOM   972  C CB  . ALA   A 1 138 ? 9.270   -19.702 -34.658 1.00 22.42 ? 138 ALA   A CB  1 
ATOM   973  N N   . GLU   A 1 139 ? 10.203  -17.106 -36.228 1.00 19.96 ? 139 GLU   A N   1 
ATOM   974  C CA  . GLU   A 1 139 ? 10.526  -16.642 -37.577 1.00 20.46 ? 139 GLU   A CA  1 
ATOM   975  C C   . GLU   A 1 139 ? 11.946  -17.071 -37.881 1.00 19.45 ? 139 GLU   A C   1 
ATOM   976  O O   . GLU   A 1 139 ? 12.819  -17.015 -37.006 1.00 20.07 ? 139 GLU   A O   1 
ATOM   977  C CB  . GLU   A 1 139 ? 10.458  -15.101 -37.708 1.00 23.05 ? 139 GLU   A CB  1 
ATOM   978  C CG  . GLU   A 1 139 ? 9.067   -14.530 -37.575 1.00 28.32 ? 139 GLU   A CG  1 
ATOM   979  C CD  . GLU   A 1 139 ? 8.181   -14.812 -38.786 1.00 31.84 ? 139 GLU   A CD  1 
ATOM   980  O OE1 . GLU   A 1 139 ? 8.703   -15.331 -39.803 1.00 32.26 ? 139 GLU   A OE1 1 
ATOM   981  O OE2 . GLU   A 1 139 ? 6.959   -14.510 -38.719 1.00 33.00 ? 139 GLU   A OE2 1 
ATOM   982  N N   . LEU   A 1 140 ? 12.180  -17.465 -39.127 1.00 21.95 ? 140 LEU   A N   1 
ATOM   983  C CA  . LEU   A 1 140 ? 13.503  -17.847 -39.597 1.00 23.36 ? 140 LEU   A CA  1 
ATOM   984  C C   . LEU   A 1 140 ? 13.888  -16.859 -40.689 1.00 23.46 ? 140 LEU   A C   1 
ATOM   985  O O   . LEU   A 1 140 ? 13.088  -16.619 -41.598 1.00 24.71 ? 140 LEU   A O   1 
ATOM   986  C CB  . LEU   A 1 140 ? 13.441  -19.279 -40.161 1.00 23.66 ? 140 LEU   A CB  1 
ATOM   987  C CG  . LEU   A 1 140 ? 14.709  -19.857 -40.760 1.00 25.11 ? 140 LEU   A CG  1 
ATOM   988  C CD1 . LEU   A 1 140 ? 15.849  -19.870 -39.766 1.00 25.44 ? 140 LEU   A CD1 1 
ATOM   989  C CD2 . LEU   A 1 140 ? 14.376  -21.275 -41.261 1.00 26.16 ? 140 LEU   A CD2 1 
ATOM   990  N N   . ALA   A 1 141 ? 15.102  -16.305 -40.632 1.00 23.55 ? 141 ALA   A N   1 
ATOM   991  C CA  . ALA   A 1 141 ? 15.506  -15.328 -41.654 1.00 24.15 ? 141 ALA   A CA  1 
ATOM   992  C C   . ALA   A 1 141 ? 17.005  -15.459 -41.944 1.00 24.64 ? 141 ALA   A C   1 
ATOM   993  O O   . ALA   A 1 141 ? 17.778  -15.966 -41.124 1.00 24.66 ? 141 ALA   A O   1 
ATOM   994  C CB  . ALA   A 1 141 ? 15.095  -13.890 -41.271 1.00 24.21 ? 141 ALA   A CB  1 
ATOM   995  N N   . LYS   A 1 142 ? 17.425  -14.978 -43.177 1.00 26.83 ? 142 LYS   A N   1 
ATOM   996  C CA  . LYS   A 1 142 ? 18.811  -15.135 -43.591 1.00 27.70 ? 142 LYS   A CA  1 
ATOM   997  C C   . LYS   A 1 142 ? 19.631  -13.896 -43.238 1.00 25.79 ? 142 LYS   A C   1 
ATOM   998  O O   . LYS   A 1 142 ? 19.089  -12.791 -43.138 1.00 26.73 ? 142 LYS   A O   1 
ATOM   999  C CB  . LYS   A 1 142 ? 18.874  -15.360 -45.112 1.00 32.26 ? 142 LYS   A CB  1 
ATOM   1000 C CG  . LYS   A 1 142 ? 18.531  -16.780 -45.513 1.00 39.31 ? 142 LYS   A CG  1 
ATOM   1001 C CD  . LYS   A 1 142 ? 17.574  -16.835 -46.684 1.00 44.66 ? 142 LYS   A CD  1 
ATOM   1002 C CE  . LYS   A 1 142 ? 17.997  -17.884 -47.705 1.00 49.65 ? 142 LYS   A CE  1 
ATOM   1003 N NZ  . LYS   A 1 142 ? 18.442  -19.160 -47.064 1.00 51.96 ? 142 LYS   A NZ  1 
ATOM   1004 N N   . PRO   A 1 143 ? 20.943  -14.005 -43.035 1.00 26.64 ? 143 PRO   A N   1 
ATOM   1005 C CA  . PRO   A 1 143 ? 21.733  -12.797 -42.756 1.00 27.99 ? 143 PRO   A CA  1 
ATOM   1006 C C   . PRO   A 1 143 ? 21.671  -11.815 -43.912 1.00 28.65 ? 143 PRO   A C   1 
ATOM   1007 O O   . PRO   A 1 143 ? 21.658  -12.196 -45.088 1.00 29.84 ? 143 PRO   A O   1 
ATOM   1008 C CB  . PRO   A 1 143 ? 23.156  -13.321 -42.556 1.00 29.04 ? 143 PRO   A CB  1 
ATOM   1009 C CG  . PRO   A 1 143 ? 22.991  -14.777 -42.264 1.00 29.20 ? 143 PRO   A CG  1 
ATOM   1010 C CD  . PRO   A 1 143 ? 21.751  -15.235 -42.965 1.00 27.49 ? 143 PRO   A CD  1 
ATOM   1011 N N   . GLY   A 1 144 ? 21.675  -10.529 -43.562 1.00 29.69 ? 144 GLY   A N   1 
ATOM   1012 C CA  . GLY   A 1 144 ? 21.576  -9.462  -44.529 1.00 28.29 ? 144 GLY   A CA  1 
ATOM   1013 C C   . GLY   A 1 144 ? 20.163  -9.116  -44.926 1.00 29.00 ? 144 GLY   A C   1 
ATOM   1014 O O   . GLY   A 1 144 ? 19.942  -8.046  -45.517 1.00 32.16 ? 144 GLY   A O   1 
ATOM   1015 N N   . ALA   A 1 145 ? 19.201  -9.992  -44.650 1.00 26.81 ? 145 ALA   A N   1 
ATOM   1016 C CA  . ALA   A 1 145 ? 17.819  -9.711  -44.978 1.00 26.79 ? 145 ALA   A CA  1 
ATOM   1017 C C   . ALA   A 1 145 ? 17.206  -8.861  -43.873 1.00 26.06 ? 145 ALA   A C   1 
ATOM   1018 O O   . ALA   A 1 145 ? 17.841  -8.543  -42.856 1.00 26.39 ? 145 ALA   A O   1 
ATOM   1019 C CB  . ALA   A 1 145 ? 17.034  -11.013 -45.103 1.00 28.13 ? 145 ALA   A CB  1 
ATOM   1020 N N   . SER   A 1 146 ? 15.952  -8.474  -44.078 1.00 26.22 ? 146 SER   A N   1 
ATOM   1021 C CA  A SER   A 1 146 ? 15.125  -7.876  -43.043 0.53 23.85 ? 146 SER   A CA  1 
ATOM   1022 C CA  B SER   A 1 146 ? 15.117  -7.876  -43.047 0.47 24.31 ? 146 SER   A CA  1 
ATOM   1023 C C   . SER   A 1 146 ? 14.024  -8.863  -42.682 1.00 24.05 ? 146 SER   A C   1 
ATOM   1024 O O   . SER   A 1 146 ? 13.711  -9.782  -43.448 1.00 27.81 ? 146 SER   A O   1 
ATOM   1025 C CB  A SER   A 1 146 ? 14.542  -6.543  -43.522 0.53 23.95 ? 146 SER   A CB  1 
ATOM   1026 C CB  B SER   A 1 146 ? 14.493  -6.555  -43.512 0.47 24.96 ? 146 SER   A CB  1 
ATOM   1027 O OG  A SER   A 1 146 ? 13.531  -6.769  -44.473 0.53 24.41 ? 146 SER   A OG  1 
ATOM   1028 O OG  B SER   A 1 146 ? 15.484  -5.559  -43.639 0.47 25.79 ? 146 SER   A OG  1 
ATOM   1029 N N   . VAL   A 1 147 ? 13.448  -8.680  -41.494 1.00 20.62 ? 147 VAL   A N   1 
ATOM   1030 C CA  . VAL   A 1 147 ? 12.344  -9.513  -41.048 1.00 20.53 ? 147 VAL   A CA  1 
ATOM   1031 C C   . VAL   A 1 147 ? 11.285  -8.632  -40.408 1.00 21.65 ? 147 VAL   A C   1 
ATOM   1032 O O   . VAL   A 1 147 ? 11.587  -7.608  -39.784 1.00 20.17 ? 147 VAL   A O   1 
ATOM   1033 C CB  . VAL   A 1 147 ? 12.825  -10.642 -40.097 1.00 22.92 ? 147 VAL   A CB  1 
ATOM   1034 C CG1 . VAL   A 1 147 ? 13.211  -10.075 -38.744 1.00 21.59 ? 147 VAL   A CG1 1 
ATOM   1035 C CG2 . VAL   A 1 147 ? 11.725  -11.679 -39.916 1.00 24.27 ? 147 VAL   A CG2 1 
ATOM   1036 N N   . GLN   A 1 148 ? 10.032  -9.018  -40.589 1.00 21.03 ? 148 GLN   A N   1 
ATOM   1037 C CA  . GLN   A 1 148 ? 8.913   -8.313  -39.982 1.00 20.10 ? 148 GLN   A CA  1 
ATOM   1038 C C   . GLN   A 1 148 ? 8.331   -9.131  -38.851 1.00 20.90 ? 148 GLN   A C   1 
ATOM   1039 O O   . GLN   A 1 148 ? 7.933   -10.282 -39.060 1.00 24.11 ? 148 GLN   A O   1 
ATOM   1040 C CB  . GLN   A 1 148 ? 7.822   -8.041  -41.006 1.00 20.52 ? 148 GLN   A CB  1 
ATOM   1041 C CG  . GLN   A 1 148 ? 6.572   -7.425  -40.383 1.00 23.68 ? 148 GLN   A CG  1 
ATOM   1042 C CD  . GLN   A 1 148 ? 5.683   -6.848  -41.451 1.00 27.69 ? 148 GLN   A CD  1 
ATOM   1043 O OE1 . GLN   A 1 148 ? 5.815   -5.674  -41.818 1.00 32.14 ? 148 GLN   A OE1 1 
ATOM   1044 N NE2 . GLN   A 1 148 ? 4.773   -7.671  -41.969 1.00 27.04 ? 148 GLN   A NE2 1 
ATOM   1045 N N   . LEU   A 1 149 ? 8.228   -8.522  -37.680 1.00 19.88 ? 149 LEU   A N   1 
ATOM   1046 C CA  . LEU   A 1 149 ? 7.566   -9.139  -36.539 1.00 18.27 ? 149 LEU   A CA  1 
ATOM   1047 C C   . LEU   A 1 149 ? 6.227   -8.459  -36.298 1.00 19.27 ? 149 LEU   A C   1 
ATOM   1048 O O   . LEU   A 1 149 ? 6.123   -7.248  -36.431 1.00 20.70 ? 149 LEU   A O   1 
ATOM   1049 C CB  . LEU   A 1 149 ? 8.420   -9.010  -35.281 1.00 19.48 ? 149 LEU   A CB  1 
ATOM   1050 C CG  . LEU   A 1 149 ? 9.833   -9.582  -35.481 1.00 24.85 ? 149 LEU   A CG  1 
ATOM   1051 C CD1 . LEU   A 1 149 ? 10.559  -9.507  -34.167 1.00 27.31 ? 149 LEU   A CD1 1 
ATOM   1052 C CD2 . LEU   A 1 149 ? 9.786   -11.012 -35.956 1.00 26.73 ? 149 LEU   A CD2 1 
ATOM   1053 N N   . SER   A 1 150 ? 5.201   -9.230  -35.936 1.00 20.32 ? 150 SER   A N   1 
ATOM   1054 C CA  . SER   A 1 150 ? 3.846   -8.706  -35.798 1.00 20.02 ? 150 SER   A CA  1 
ATOM   1055 C C   . SER   A 1 150 ? 3.270   -8.976  -34.415 1.00 18.48 ? 150 SER   A C   1 
ATOM   1056 O O   . SER   A 1 150 ? 3.635   -9.923  -33.714 1.00 19.04 ? 150 SER   A O   1 
ATOM   1057 C CB  . SER   A 1 150 ? 2.910   -9.287  -36.879 1.00 25.01 ? 150 SER   A CB  1 
ATOM   1058 O OG  . SER   A 1 150 ? 2.768   -10.694 -36.710 1.00 27.37 ? 150 SER   A OG  1 
ATOM   1059 N N   . CYS   A 1 151 ? 2.326   -8.137  -34.038 1.00 17.87 ? 151 CYS   A N   1 
ATOM   1060 C CA  . CYS   A 1 151 ? 1.740   -8.231  -32.708 1.00 18.00 ? 151 CYS   A CA  1 
ATOM   1061 C C   . CYS   A 1 151 ? 0.313   -7.683  -32.766 1.00 20.05 ? 151 CYS   A C   1 
ATOM   1062 O O   . CYS   A 1 151 ? 0.104   -6.474  -32.875 1.00 22.23 ? 151 CYS   A O   1 
ATOM   1063 C CB  . CYS   A 1 151 ? 2.587   -7.407  -31.742 1.00 19.73 ? 151 CYS   A CB  1 
ATOM   1064 S SG  . CYS   A 1 151 ? 1.842   -7.272  -30.073 1.00 21.60 ? 151 CYS   A SG  1 
ATOM   1065 N N   . LYS   A 1 152 ? -0.672  -8.558  -32.714 1.00 19.96 ? 152 LYS   A N   1 
ATOM   1066 C CA  . LYS   A 1 152 ? -2.055  -8.131  -32.857 1.00 21.14 ? 152 LYS   A CA  1 
ATOM   1067 C C   . LYS   A 1 152 ? -2.686  -8.034  -31.475 1.00 21.36 ? 152 LYS   A C   1 
ATOM   1068 O O   . LYS   A 1 152 ? -2.624  -8.987  -30.697 1.00 21.05 ? 152 LYS   A O   1 
ATOM   1069 C CB  . LYS   A 1 152 ? -2.817  -9.139  -33.722 1.00 26.44 ? 152 LYS   A CB  1 
ATOM   1070 C CG  . LYS   A 1 152 ? -4.310  -8.809  -33.891 1.00 30.13 ? 152 LYS   A CG  1 
ATOM   1071 C CD  . LYS   A 1 152 ? -5.039  -9.983  -34.527 1.00 36.24 ? 152 LYS   A CD  1 
ATOM   1072 C CE  . LYS   A 1 152 ? -6.129  -10.507 -33.560 1.00 43.41 ? 152 LYS   A CE  1 
ATOM   1073 N NZ  . LYS   A 1 152 ? -5.638  -11.523 -32.556 1.00 45.04 ? 152 LYS   A NZ  1 
ATOM   1074 N N   . GLY   A 1 153 ? -3.265  -6.875  -31.165 1.00 20.80 ? 153 GLY   A N   1 
ATOM   1075 C CA  . GLY   A 1 153 ? -3.904  -6.650  -29.876 1.00 20.62 ? 153 GLY   A CA  1 
ATOM   1076 C C   . GLY   A 1 153 ? -5.404  -6.850  -29.998 1.00 24.09 ? 153 GLY   A C   1 
ATOM   1077 O O   . GLY   A 1 153 ? -6.016  -6.416  -30.978 1.00 27.61 ? 153 GLY   A O   1 
ATOM   1078 N N   . SER   A 1 154 ? -6.001  -7.500  -28.989 1.00 21.07 ? 154 SER   A N   1 
ATOM   1079 C CA  . SER   A 1 154 ? -7.441  -7.703  -28.961 1.00 22.21 ? 154 SER   A CA  1 
ATOM   1080 C C   . SER   A 1 154 ? -7.922  -7.520  -27.530 1.00 21.48 ? 154 SER   A C   1 
ATOM   1081 O O   . SER   A 1 154 ? -7.158  -7.666  -26.562 1.00 22.29 ? 154 SER   A O   1 
ATOM   1082 C CB  . SER   A 1 154 ? -7.811  -9.097  -29.502 1.00 23.26 ? 154 SER   A CB  1 
ATOM   1083 O OG  . SER   A 1 154 ? -7.344  -10.073 -28.595 1.00 25.92 ? 154 SER   A OG  1 
ATOM   1084 N N   . GLY   A 1 155 ? -9.202  -7.184  -27.404 1.00 21.03 ? 155 GLY   A N   1 
ATOM   1085 C CA  . GLY   A 1 155 ? -9.835  -7.048  -26.113 1.00 20.65 ? 155 GLY   A CA  1 
ATOM   1086 C C   . GLY   A 1 155 ? -9.702  -5.681  -25.479 1.00 22.38 ? 155 GLY   A C   1 
ATOM   1087 O O   . GLY   A 1 155 ? -10.017 -5.538  -24.286 1.00 23.41 ? 155 GLY   A O   1 
ATOM   1088 N N   . TYR   A 1 156 ? -9.207  -4.686  -26.224 1.00 20.74 ? 156 TYR   A N   1 
ATOM   1089 C CA  . TYR   A 1 156 ? -9.123  -3.297  -25.766 1.00 22.19 ? 156 TYR   A CA  1 
ATOM   1090 C C   . TYR   A 1 156 ? -9.161  -2.401  -26.987 1.00 20.94 ? 156 TYR   A C   1 
ATOM   1091 O O   . TYR   A 1 156 ? -9.106  -2.880  -28.128 1.00 20.63 ? 156 TYR   A O   1 
ATOM   1092 C CB  . TYR   A 1 156 ? -7.843  -3.042  -24.958 1.00 20.88 ? 156 TYR   A CB  1 
ATOM   1093 C CG  . TYR   A 1 156 ? -6.533  -3.245  -25.715 1.00 20.51 ? 156 TYR   A CG  1 
ATOM   1094 C CD1 . TYR   A 1 156 ? -6.006  -4.541  -25.914 1.00 19.93 ? 156 TYR   A CD1 1 
ATOM   1095 C CD2 . TYR   A 1 156 ? -5.767  -2.152  -26.118 1.00 20.46 ? 156 TYR   A CD2 1 
ATOM   1096 C CE1 . TYR   A 1 156 ? -4.769  -4.722  -26.536 1.00 20.53 ? 156 TYR   A CE1 1 
ATOM   1097 C CE2 . TYR   A 1 156 ? -4.540  -2.328  -26.753 1.00 20.38 ? 156 TYR   A CE2 1 
ATOM   1098 C CZ  . TYR   A 1 156 ? -4.042  -3.614  -26.962 1.00 21.61 ? 156 TYR   A CZ  1 
ATOM   1099 O OH  . TYR   A 1 156 ? -2.821  -3.774  -27.575 1.00 22.94 ? 156 TYR   A OH  1 
ATOM   1100 N N   . THR   A 1 157 ? -9.271  -1.098  -26.746 1.00 20.58 ? 157 THR   A N   1 
ATOM   1101 C CA  . THR   A 1 157 ? -9.282  -0.119  -27.833 1.00 21.05 ? 157 THR   A CA  1 
ATOM   1102 C C   . THR   A 1 157 ? -7.843  0.097   -28.261 1.00 19.90 ? 157 THR   A C   1 
ATOM   1103 O O   . THR   A 1 157 ? -7.092  0.886   -27.662 1.00 20.53 ? 157 THR   A O   1 
ATOM   1104 C CB  . THR   A 1 157 ? -9.969  1.167   -27.410 1.00 23.11 ? 157 THR   A CB  1 
ATOM   1105 O OG1 . THR   A 1 157 ? -11.280 0.826   -26.932 1.00 26.97 ? 157 THR   A OG1 1 
ATOM   1106 C CG2 . THR   A 1 157 ? -10.097 2.101   -28.596 1.00 25.07 ? 157 THR   A CG2 1 
ATOM   1107 N N   . PHE   A 1 158 ? -7.453  -0.631  -29.302 1.00 20.83 ? 158 PHE   A N   1 
ATOM   1108 C CA  . PHE   A 1 158 ? -6.044  -0.760  -29.669 1.00 20.10 ? 158 PHE   A CA  1 
ATOM   1109 C C   . PHE   A 1 158 ? -5.292  0.561   -29.826 1.00 20.45 ? 158 PHE   A C   1 
ATOM   1110 O O   . PHE   A 1 158 ? -4.180  0.692   -29.271 1.00 20.03 ? 158 PHE   A O   1 
ATOM   1111 C CB  . PHE   A 1 158 ? -5.952  -1.671  -30.905 1.00 22.08 ? 158 PHE   A CB  1 
ATOM   1112 C CG  . PHE   A 1 158 ? -4.558  -1.828  -31.410 1.00 25.10 ? 158 PHE   A CG  1 
ATOM   1113 C CD1 . PHE   A 1 158 ? -3.695  -2.742  -30.825 1.00 25.76 ? 158 PHE   A CD1 1 
ATOM   1114 C CD2 . PHE   A 1 158 ? -4.096  -1.024  -32.445 1.00 25.12 ? 158 PHE   A CD2 1 
ATOM   1115 C CE1 . PHE   A 1 158 ? -2.388  -2.877  -31.302 1.00 26.93 ? 158 PHE   A CE1 1 
ATOM   1116 C CE2 . PHE   A 1 158 ? -2.815  -1.154  -32.921 1.00 26.12 ? 158 PHE   A CE2 1 
ATOM   1117 C CZ  . PHE   A 1 158 ? -1.958  -2.077  -32.358 1.00 26.21 ? 158 PHE   A CZ  1 
ATOM   1118 N N   . PRO   A 1 159 ? -5.811  1.569   -30.526 1.00 21.21 ? 159 PRO   A N   1 
ATOM   1119 C CA  . PRO   A 1 159 ? -5.024  2.799   -30.727 1.00 22.41 ? 159 PRO   A CA  1 
ATOM   1120 C C   . PRO   A 1 159 ? -4.770  3.595   -29.473 1.00 19.34 ? 159 PRO   A C   1 
ATOM   1121 O O   . PRO   A 1 159 ? -3.815  4.400   -29.465 1.00 19.03 ? 159 PRO   A O   1 
ATOM   1122 C CB  . PRO   A 1 159 ? -5.866  3.616   -31.715 1.00 25.04 ? 159 PRO   A CB  1 
ATOM   1123 C CG  . PRO   A 1 159 ? -6.892  2.717   -32.228 1.00 25.49 ? 159 PRO   A CG  1 
ATOM   1124 C CD  . PRO   A 1 159 ? -7.088  1.612   -31.252 1.00 22.96 ? 159 PRO   A CD  1 
ATOM   1125 N N   . ASN   A 1 160 ? -5.540  3.364   -28.402 1.00 17.64 ? 160 ASN   A N   1 
ATOM   1126 C CA  . ASN   A 1 160 ? -5.464  4.148   -27.176 1.00 17.92 ? 160 ASN   A CA  1 
ATOM   1127 C C   . ASN   A 1 160 ? -4.366  3.699   -26.227 1.00 19.05 ? 160 ASN   A C   1 
ATOM   1128 O O   . ASN   A 1 160 ? -4.263  4.279   -25.139 1.00 19.31 ? 160 ASN   A O   1 
ATOM   1129 C CB  . ASN   A 1 160 ? -6.802  4.110   -26.439 1.00 18.55 ? 160 ASN   A CB  1 
ATOM   1130 C CG  . ASN   A 1 160 ? -7.904  4.900   -27.168 1.00 21.07 ? 160 ASN   A CG  1 
ATOM   1131 O OD1 . ASN   A 1 160 ? -7.723  5.389   -28.282 1.00 21.66 ? 160 ASN   A OD1 1 
ATOM   1132 N ND2 . ASN   A 1 160 ? -9.067  4.941   -26.565 1.00 21.45 ? 160 ASN   A ND2 1 
ATOM   1133 N N   . TYR   A 1 161 ? -3.549  2.711   -26.603 1.00 16.93 ? 161 TYR   A N   1 
ATOM   1134 C CA  . TYR   A 1 161 ? -2.421  2.292   -25.804 1.00 17.22 ? 161 TYR   A CA  1 
ATOM   1135 C C   . TYR   A 1 161 ? -1.193  2.300   -26.689 1.00 17.82 ? 161 TYR   A C   1 
ATOM   1136 O O   . TYR   A 1 161 ? -1.277  2.075   -27.903 1.00 20.24 ? 161 TYR   A O   1 
ATOM   1137 C CB  . TYR   A 1 161 ? -2.610  0.842   -25.268 1.00 18.55 ? 161 TYR   A CB  1 
ATOM   1138 C CG  . TYR   A 1 161 ? -3.616  0.818   -24.160 1.00 17.47 ? 161 TYR   A CG  1 
ATOM   1139 C CD1 . TYR   A 1 161 ? -4.977  0.871   -24.421 1.00 20.16 ? 161 TYR   A CD1 1 
ATOM   1140 C CD2 . TYR   A 1 161 ? -3.200  0.737   -22.826 1.00 20.96 ? 161 TYR   A CD2 1 
ATOM   1141 C CE1 . TYR   A 1 161 ? -5.915  0.846   -23.366 1.00 21.26 ? 161 TYR   A CE1 1 
ATOM   1142 C CE2 . TYR   A 1 161 ? -4.112  0.702   -21.774 1.00 22.36 ? 161 TYR   A CE2 1 
ATOM   1143 C CZ  . TYR   A 1 161 ? -5.468  0.758   -22.051 1.00 23.07 ? 161 TYR   A CZ  1 
ATOM   1144 O OH  . TYR   A 1 161 ? -6.383  0.743   -21.022 1.00 28.35 ? 161 TYR   A OH  1 
ATOM   1145 N N   . TRP   A 1 162 ? -0.039  2.543   -26.063 1.00 16.77 ? 162 TRP   A N   1 
ATOM   1146 C CA  . TRP   A 1 162 ? 1.217   2.426   -26.786 1.00 16.62 ? 162 TRP   A CA  1 
ATOM   1147 C C   . TRP   A 1 162 ? 1.578   0.950   -26.903 1.00 15.49 ? 162 TRP   A C   1 
ATOM   1148 O O   . TRP   A 1 162 ? 1.065   0.107   -26.156 1.00 15.54 ? 162 TRP   A O   1 
ATOM   1149 C CB  . TRP   A 1 162 ? 2.331   3.067   -25.965 1.00 16.58 ? 162 TRP   A CB  1 
ATOM   1150 C CG  . TRP   A 1 162 ? 2.133   4.530   -25.684 1.00 16.90 ? 162 TRP   A CG  1 
ATOM   1151 C CD1 . TRP   A 1 162 ? 1.170   5.369   -26.196 1.00 16.57 ? 162 TRP   A CD1 1 
ATOM   1152 C CD2 . TRP   A 1 162 ? 2.945   5.322   -24.812 1.00 18.06 ? 162 TRP   A CD2 1 
ATOM   1153 N NE1 . TRP   A 1 162 ? 1.364   6.649   -25.693 1.00 16.96 ? 162 TRP   A NE1 1 
ATOM   1154 C CE2 . TRP   A 1 162 ? 2.437   6.639   -24.844 1.00 17.64 ? 162 TRP   A CE2 1 
ATOM   1155 C CE3 . TRP   A 1 162 ? 4.042   5.041   -23.991 1.00 19.19 ? 162 TRP   A CE3 1 
ATOM   1156 C CZ2 . TRP   A 1 162 ? 2.992   7.679   -24.083 1.00 18.73 ? 162 TRP   A CZ2 1 
ATOM   1157 C CZ3 . TRP   A 1 162 ? 4.610   6.097   -23.238 1.00 19.38 ? 162 TRP   A CZ3 1 
ATOM   1158 C CH2 . TRP   A 1 162 ? 4.088   7.395   -23.310 1.00 20.43 ? 162 TRP   A CH2 1 
ATOM   1159 N N   . MET   A 1 163 ? 2.491   0.627   -27.829 1.00 15.59 ? 163 MET   A N   1 
ATOM   1160 C CA  . MET   A 1 163 ? 3.084   -0.700  -27.868 1.00 14.94 ? 163 MET   A CA  1 
ATOM   1161 C C   . MET   A 1 163 ? 4.584   -0.550  -27.666 1.00 14.45 ? 163 MET   A C   1 
ATOM   1162 O O   . MET   A 1 163 ? 5.260   0.142   -28.455 1.00 15.09 ? 163 MET   A O   1 
ATOM   1163 C CB  . MET   A 1 163 ? 2.813   -1.394  -29.196 1.00 15.59 ? 163 MET   A CB  1 
ATOM   1164 C CG  . MET   A 1 163 ? 3.096   -2.928  -29.215 1.00 17.67 ? 163 MET   A CG  1 
ATOM   1165 S SD  . MET   A 1 163 ? 1.976   -3.778  -28.041 1.00 18.83 ? 163 MET   A SD  1 
ATOM   1166 C CE  . MET   A 1 163 ? 0.577   -4.122  -29.134 1.00 20.77 ? 163 MET   A CE  1 
ATOM   1167 N N   . HIS   A 1 164 ? 5.095   -1.170  -26.599 1.00 14.03 ? 164 HIS   A N   1 
ATOM   1168 C CA  . HIS   A 1 164 ? 6.523   -1.312  -26.411 1.00 13.71 ? 164 HIS   A CA  1 
ATOM   1169 C C   . HIS   A 1 164 ? 7.011   -2.589  -27.095 1.00 14.02 ? 164 HIS   A C   1 
ATOM   1170 O O   . HIS   A 1 164 ? 6.259   -3.562  -27.245 1.00 14.28 ? 164 HIS   A O   1 
ATOM   1171 C CB  . HIS   A 1 164 ? 6.801   -1.498  -24.917 1.00 14.94 ? 164 HIS   A CB  1 
ATOM   1172 C CG  . HIS   A 1 164 ? 6.508   -0.297  -24.067 1.00 13.89 ? 164 HIS   A CG  1 
ATOM   1173 N ND1 . HIS   A 1 164 ? 7.295   0.838   -24.104 1.00 14.76 ? 164 HIS   A ND1 1 
ATOM   1174 C CD2 . HIS   A 1 164 ? 5.536   -0.051  -23.147 1.00 14.27 ? 164 HIS   A CD2 1 
ATOM   1175 C CE1 . HIS   A 1 164 ? 6.822   1.734   -23.243 1.00 15.45 ? 164 HIS   A CE1 1 
ATOM   1176 N NE2 . HIS   A 1 164 ? 5.760   1.216   -22.643 1.00 14.78 ? 164 HIS   A NE2 1 
ATOM   1177 N N   . TRP   A 1 165 ? 8.293   -2.617  -27.439 1.00 13.21 ? 165 TRP   A N   1 
ATOM   1178 C CA  . TRP   A 1 165 ? 8.953   -3.832  -27.889 1.00 14.40 ? 165 TRP   A CA  1 
ATOM   1179 C C   . TRP   A 1 165 ? 10.187  -4.056  -27.022 1.00 13.63 ? 165 TRP   A C   1 
ATOM   1180 O O   . TRP   A 1 165 ? 10.891  -3.107  -26.675 1.00 13.29 ? 165 TRP   A O   1 
ATOM   1181 C CB  . TRP   A 1 165 ? 9.332   -3.708  -29.371 1.00 16.15 ? 165 TRP   A CB  1 
ATOM   1182 C CG  . TRP   A 1 165 ? 8.129   -3.679  -30.257 1.00 16.37 ? 165 TRP   A CG  1 
ATOM   1183 C CD1 . TRP   A 1 165 ? 7.341   -2.583  -30.576 1.00 16.53 ? 165 TRP   A CD1 1 
ATOM   1184 C CD2 . TRP   A 1 165 ? 7.595   -4.791  -30.988 1.00 16.74 ? 165 TRP   A CD2 1 
ATOM   1185 N NE1 . TRP   A 1 165 ? 6.337   -2.989  -31.437 1.00 17.32 ? 165 TRP   A NE1 1 
ATOM   1186 C CE2 . TRP   A 1 165 ? 6.493   -4.322  -31.728 1.00 16.92 ? 165 TRP   A CE2 1 
ATOM   1187 C CE3 . TRP   A 1 165 ? 7.915   -6.158  -31.047 1.00 17.48 ? 165 TRP   A CE3 1 
ATOM   1188 C CZ2 . TRP   A 1 165 ? 5.737   -5.168  -32.556 1.00 17.68 ? 165 TRP   A CZ2 1 
ATOM   1189 C CZ3 . TRP   A 1 165 ? 7.173   -6.997  -31.856 1.00 17.38 ? 165 TRP   A CZ3 1 
ATOM   1190 C CH2 . TRP   A 1 165 ? 6.099   -6.489  -32.619 1.00 18.45 ? 165 TRP   A CH2 1 
ATOM   1191 N N   . VAL   A 1 166 ? 10.435  -5.314  -26.649 1.00 13.87 ? 166 VAL   A N   1 
ATOM   1192 C CA  . VAL   A 1 166 ? 11.512  -5.690  -25.741 1.00 13.28 ? 166 VAL   A CA  1 
ATOM   1193 C C   . VAL   A 1 166 ? 12.125  -6.973  -26.310 1.00 14.29 ? 166 VAL   A C   1 
ATOM   1194 O O   . VAL   A 1 166 ? 11.427  -7.817  -26.888 1.00 16.41 ? 166 VAL   A O   1 
ATOM   1195 C CB  . VAL   A 1 166 ? 10.874  -5.973  -24.343 1.00 15.08 ? 166 VAL   A CB  1 
ATOM   1196 C CG1 . VAL   A 1 166 ? 11.889  -6.456  -23.279 1.00 18.81 ? 166 VAL   A CG1 1 
ATOM   1197 C CG2 . VAL   A 1 166 ? 10.125  -4.736  -23.791 1.00 16.45 ? 166 VAL   A CG2 1 
ATOM   1198 N N   . THR   A 1 167 ? 13.414  -7.181  -26.075 1.00 14.93 ? 167 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 167 ? 14.085  -8.412  -26.489 1.00 14.35 ? 167 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 167 ? 14.719  -9.091  -25.277 1.00 14.35 ? 167 THR   A C   1 
ATOM   1201 O O   . THR   A 1 167 ? 15.121  -8.417  -24.303 1.00 15.21 ? 167 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 167 ? 15.094  -8.176  -27.627 1.00 16.90 ? 167 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 167 ? 15.655  -9.428  -28.031 1.00 17.42 ? 167 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 167 ? 16.222  -7.230  -27.169 1.00 17.29 ? 167 THR   A CG2 1 
ATOM   1205 N N   . GLN   A 1 168 ? 14.822  -10.412 -25.385 1.00 16.57 ? 168 GLN   A N   1 
ATOM   1206 C CA  . GLN   A 1 168 ? 15.475  -11.179 -24.318 1.00 15.80 ? 168 GLN   A CA  1 
ATOM   1207 C C   . GLN   A 1 168 ? 16.286  -12.348 -24.841 1.00 19.30 ? 168 GLN   A C   1 
ATOM   1208 O O   . GLN   A 1 168 ? 15.914  -12.926 -25.856 1.00 20.25 ? 168 GLN   A O   1 
ATOM   1209 C CB  . GLN   A 1 168 ? 14.445  -11.793 -23.371 1.00 21.69 ? 168 GLN   A CB  1 
ATOM   1210 C CG  . GLN   A 1 168 ? 15.053  -12.483 -22.157 1.00 25.59 ? 168 GLN   A CG  1 
ATOM   1211 C CD  . GLN   A 1 168 ? 14.041  -13.127 -21.242 1.00 29.84 ? 168 GLN   A CD  1 
ATOM   1212 O OE1 . GLN   A 1 168 ? 13.120  -13.800 -21.689 1.00 30.91 ? 168 GLN   A OE1 1 
ATOM   1213 N NE2 . GLN   A 1 168 ? 14.206  -12.921 -19.949 1.00 29.76 ? 168 GLN   A NE2 1 
ATOM   1214 N N   . ARG   A 1 169 ? 17.430  -12.558 -24.222 1.00 23.73 ? 169 ARG   A N   1 
ATOM   1215 C CA  . ARG   A 1 169 ? 18.186  -13.796 -24.356 1.00 30.45 ? 169 ARG   A CA  1 
ATOM   1216 C C   . ARG   A 1 169 ? 18.916  -14.035 -23.046 1.00 40.04 ? 169 ARG   A C   1 
ATOM   1217 O O   . ARG   A 1 169 ? 19.199  -13.083 -22.303 1.00 39.84 ? 169 ARG   A O   1 
ATOM   1218 C CB  . ARG   A 1 169 ? 19.165  -13.747 -25.535 1.00 32.78 ? 169 ARG   A CB  1 
ATOM   1219 C CG  . ARG   A 1 169 ? 20.317  -12.844 -25.336 1.00 36.52 ? 169 ARG   A CG  1 
ATOM   1220 C CD  . ARG   A 1 169 ? 21.102  -12.766 -26.627 1.00 38.08 ? 169 ARG   A CD  1 
ATOM   1221 N NE  . ARG   A 1 169 ? 20.473  -11.820 -27.539 1.00 35.08 ? 169 ARG   A NE  1 
ATOM   1222 C CZ  . ARG   A 1 169 ? 20.917  -11.566 -28.764 1.00 34.64 ? 169 ARG   A CZ  1 
ATOM   1223 N NH1 . ARG   A 1 169 ? 21.991  -12.181 -29.247 1.00 35.00 ? 169 ARG   A NH1 1 
ATOM   1224 N NH2 . ARG   A 1 169 ? 20.267  -10.679 -29.522 1.00 30.71 ? 169 ARG   A NH2 1 
ATOM   1225 N N   . PRO   A 1 170 ? 19.206  -15.285 -22.718 1.00 50.52 ? 170 PRO   A N   1 
ATOM   1226 C CA  . PRO   A 1 170 ? 19.981  -15.555 -21.506 1.00 52.56 ? 170 PRO   A CA  1 
ATOM   1227 C C   . PRO   A 1 170 ? 21.335  -14.869 -21.581 1.00 52.70 ? 170 PRO   A C   1 
ATOM   1228 O O   . PRO   A 1 170 ? 21.923  -14.713 -22.652 1.00 55.18 ? 170 PRO   A O   1 
ATOM   1229 C CB  . PRO   A 1 170 ? 20.112  -17.078 -21.532 1.00 51.71 ? 170 PRO   A CB  1 
ATOM   1230 C CG  . PRO   A 1 170 ? 20.053  -17.362 -22.978 1.00 50.78 ? 170 PRO   A CG  1 
ATOM   1231 C CD  . PRO   A 1 170 ? 18.908  -16.536 -23.425 1.00 51.48 ? 170 PRO   A CD  1 
ATOM   1232 N N   . GLY   A 1 171 ? 21.809  -14.418 -20.436 1.00 50.63 ? 171 GLY   A N   1 
ATOM   1233 C CA  . GLY   A 1 171 ? 23.062  -13.700 -20.372 1.00 50.46 ? 171 GLY   A CA  1 
ATOM   1234 C C   . GLY   A 1 171 ? 22.935  -12.227 -20.656 1.00 53.18 ? 171 GLY   A C   1 
ATOM   1235 O O   . GLY   A 1 171 ? 23.673  -11.428 -20.080 1.00 54.08 ? 171 GLY   A O   1 
ATOM   1236 N N   . ARG   A 1 172 ? 22.006  -11.837 -21.535 1.00 53.44 ? 172 ARG   A N   1 
ATOM   1237 C CA  . ARG   A 1 172 ? 21.849  -10.420 -21.834 1.00 51.75 ? 172 ARG   A CA  1 
ATOM   1238 C C   . ARG   A 1 172 ? 20.702  -9.780  -21.057 1.00 47.47 ? 172 ARG   A C   1 
ATOM   1239 O O   . ARG   A 1 172 ? 20.741  -8.563  -20.807 1.00 48.62 ? 172 ARG   A O   1 
ATOM   1240 C CB  . ARG   A 1 172 ? 21.685  -10.199 -23.345 1.00 51.21 ? 172 ARG   A CB  1 
ATOM   1241 C CG  . ARG   A 1 172 ? 22.287  -8.890  -23.846 1.00 50.06 ? 172 ARG   A CG  1 
ATOM   1242 C CD  . ARG   A 1 172 ? 22.231  -8.830  -25.371 1.00 46.86 ? 172 ARG   A CD  1 
ATOM   1243 N NE  . ARG   A 1 172 ? 23.332  -9.547  -26.011 1.00 43.10 ? 172 ARG   A NE  1 
ATOM   1244 C CZ  . ARG   A 1 172 ? 23.532  -9.566  -27.324 1.00 39.66 ? 172 ARG   A CZ  1 
ATOM   1245 N NH1 . ARG   A 1 172 ? 22.709  -8.943  -28.158 1.00 35.95 ? 172 ARG   A NH1 1 
ATOM   1246 N NH2 . ARG   A 1 172 ? 24.581  -10.230 -27.814 1.00 40.13 ? 172 ARG   A NH2 1 
ATOM   1247 N N   . GLY   A 1 173 ? 19.715  -10.582 -20.640 1.00 37.39 ? 173 GLY   A N   1 
ATOM   1248 C CA  . GLY   A 1 173 ? 18.591  -10.069 -19.885 1.00 31.58 ? 173 GLY   A CA  1 
ATOM   1249 C C   . GLY   A 1 173 ? 17.543  -9.492  -20.816 1.00 24.87 ? 173 GLY   A C   1 
ATOM   1250 O O   . GLY   A 1 173 ? 17.420  -9.903  -21.962 1.00 24.57 ? 173 GLY   A O   1 
ATOM   1251 N N   . LEU   A 1 174 ? 16.764  -8.554  -20.292 1.00 21.61 ? 174 LEU   A N   1 
ATOM   1252 C CA  . LEU   A 1 174 ? 15.721  -7.876  -21.053 1.00 17.71 ? 174 LEU   A CA  1 
ATOM   1253 C C   . LEU   A 1 174 ? 16.226  -6.513  -21.483 1.00 16.92 ? 174 LEU   A C   1 
ATOM   1254 O O   . LEU   A 1 174 ? 16.793  -5.766  -20.684 1.00 18.69 ? 174 LEU   A O   1 
ATOM   1255 C CB  . LEU   A 1 174 ? 14.448  -7.629  -20.222 1.00 20.63 ? 174 LEU   A CB  1 
ATOM   1256 C CG  . LEU   A 1 174 ? 13.545  -8.785  -19.886 1.00 22.67 ? 174 LEU   A CG  1 
ATOM   1257 C CD1 . LEU   A 1 174 ? 12.486  -8.275  -18.910 1.00 21.79 ? 174 LEU   A CD1 1 
ATOM   1258 C CD2 . LEU   A 1 174 ? 12.910  -9.397  -21.115 1.00 22.61 ? 174 LEU   A CD2 1 
ATOM   1259 N N   . GLU   A 1 175 ? 15.957  -6.170  -22.727 1.00 15.81 ? 175 GLU   A N   1 
ATOM   1260 C CA  . GLU   A 1 175 ? 16.374  -4.881  -23.293 1.00 15.94 ? 175 GLU   A CA  1 
ATOM   1261 C C   . GLU   A 1 175 ? 15.190  -4.239  -23.990 1.00 15.77 ? 175 GLU   A C   1 
ATOM   1262 O O   . GLU   A 1 175 ? 14.522  -4.886  -24.792 1.00 16.27 ? 175 GLU   A O   1 
ATOM   1263 C CB  . GLU   A 1 175 ? 17.546  -5.086  -24.263 1.00 18.32 ? 175 GLU   A CB  1 
ATOM   1264 C CG  . GLU   A 1 175 ? 18.824  -5.604  -23.530 1.00 24.62 ? 175 GLU   A CG  1 
ATOM   1265 C CD  . GLU   A 1 175 ? 20.009  -5.795  -24.450 1.00 39.47 ? 175 GLU   A CD  1 
ATOM   1266 O OE1 . GLU   A 1 175 ? 19.814  -6.424  -25.518 1.00 39.36 ? 175 GLU   A OE1 1 
ATOM   1267 O OE2 . GLU   A 1 175 ? 21.143  -5.398  -24.065 1.00 43.31 ? 175 GLU   A OE2 1 
ATOM   1268 N N   . TRP   A 1 176 ? 14.910  -2.997  -23.656 1.00 15.02 ? 176 TRP   A N   1 
ATOM   1269 C CA  . TRP   A 1 176 ? 13.827  -2.269  -24.305 1.00 13.98 ? 176 TRP   A CA  1 
ATOM   1270 C C   . TRP   A 1 176 ? 14.299  -1.786  -25.668 1.00 15.34 ? 176 TRP   A C   1 
ATOM   1271 O O   . TRP   A 1 176 ? 15.374  -1.170  -25.782 1.00 16.82 ? 176 TRP   A O   1 
ATOM   1272 C CB  . TRP   A 1 176 ? 13.430  -1.095  -23.408 1.00 15.18 ? 176 TRP   A CB  1 
ATOM   1273 C CG  . TRP   A 1 176 ? 12.332  -0.198  -23.914 1.00 15.81 ? 176 TRP   A CG  1 
ATOM   1274 C CD1 . TRP   A 1 176 ? 10.980  -0.455  -23.910 1.00 16.11 ? 176 TRP   A CD1 1 
ATOM   1275 C CD2 . TRP   A 1 176 ? 12.487  1.111   -24.466 1.00 14.61 ? 176 TRP   A CD2 1 
ATOM   1276 N NE1 . TRP   A 1 176 ? 10.295  0.631   -24.411 1.00 15.61 ? 176 TRP   A NE1 1 
ATOM   1277 C CE2 . TRP   A 1 176 ? 11.200  1.610   -24.737 1.00 15.02 ? 176 TRP   A CE2 1 
ATOM   1278 C CE3 . TRP   A 1 176 ? 13.601  1.929   -24.720 1.00 14.70 ? 176 TRP   A CE3 1 
ATOM   1279 C CZ2 . TRP   A 1 176 ? 10.987  2.899   -25.260 1.00 16.74 ? 176 TRP   A CZ2 1 
ATOM   1280 C CZ3 . TRP   A 1 176 ? 13.384  3.208   -25.251 1.00 16.19 ? 176 TRP   A CZ3 1 
ATOM   1281 C CH2 . TRP   A 1 176 ? 12.081  3.684   -25.491 1.00 16.83 ? 176 TRP   A CH2 1 
ATOM   1282 N N   . ILE   A 1 177 ? 13.474  -2.001  -26.690 1.00 12.74 ? 177 ILE   A N   1 
ATOM   1283 C CA  . ILE   A 1 177 ? 13.802  -1.582  -28.054 1.00 13.86 ? 177 ILE   A CA  1 
ATOM   1284 C C   . ILE   A 1 177 ? 13.237  -0.200  -28.368 1.00 13.57 ? 177 ILE   A C   1 
ATOM   1285 O O   . ILE   A 1 177 ? 13.883  0.643   -29.017 1.00 15.07 ? 177 ILE   A O   1 
ATOM   1286 C CB  . ILE   A 1 177 ? 13.282  -2.636  -29.076 1.00 14.29 ? 177 ILE   A CB  1 
ATOM   1287 C CG1 . ILE   A 1 177 ? 14.070  -3.942  -28.892 1.00 15.09 ? 177 ILE   A CG1 1 
ATOM   1288 C CG2 . ILE   A 1 177 ? 13.400  -2.114  -30.495 1.00 17.28 ? 177 ILE   A CG2 1 
ATOM   1289 C CD1 . ILE   A 1 177 ? 13.465  -5.137  -29.646 1.00 15.46 ? 177 ILE   A CD1 1 
ATOM   1290 N N   . GLY   A 1 178 ? 11.976  0.024   -28.017 1.00 14.43 ? 178 GLY   A N   1 
ATOM   1291 C CA  . GLY   A 1 178 ? 11.313  1.264   -28.392 1.00 15.36 ? 178 GLY   A CA  1 
ATOM   1292 C C   . GLY   A 1 178 ? 9.826   1.152   -28.139 1.00 13.19 ? 178 GLY   A C   1 
ATOM   1293 O O   . GLY   A 1 178 ? 9.347   0.132   -27.650 1.00 14.37 ? 178 GLY   A O   1 
ATOM   1294 N N   . ARG   A 1 179 ? 9.112   2.237   -28.441 1.00 12.99 ? 179 ARG   A N   1 
ATOM   1295 C CA  . ARG   A 1 179 ? 7.664   2.184   -28.360 1.00 15.16 ? 179 ARG   A CA  1 
ATOM   1296 C C   . ARG   A 1 179 ? 7.046   3.085   -29.417 1.00 15.30 ? 179 ARG   A C   1 
ATOM   1297 O O   . ARG   A 1 179 ? 7.695   4.028   -29.922 1.00 16.13 ? 179 ARG   A O   1 
ATOM   1298 C CB  . ARG   A 1 179 ? 7.151   2.588   -26.986 1.00 18.21 ? 179 ARG   A CB  1 
ATOM   1299 C CG  . ARG   A 1 179 ? 7.483   4.021   -26.576 1.00 17.14 ? 179 ARG   A CG  1 
ATOM   1300 C CD  . ARG   A 1 179 ? 6.390   5.063   -27.011 1.00 17.91 ? 179 ARG   A CD  1 
ATOM   1301 N NE  . ARG   A 1 179 ? 6.610   6.303   -26.300 1.00 17.88 ? 179 ARG   A NE  1 
ATOM   1302 C CZ  . ARG   A 1 179 ? 5.992   7.435   -26.567 1.00 17.85 ? 179 ARG   A CZ  1 
ATOM   1303 N NH1 . ARG   A 1 179 ? 5.155   7.538   -27.577 1.00 20.34 ? 179 ARG   A NH1 1 
ATOM   1304 N NH2 . ARG   A 1 179 ? 6.203   8.482   -25.776 1.00 19.42 ? 179 ARG   A NH2 1 
ATOM   1305 N N   . ILE   A 1 180 ? 5.772   2.791   -29.737 1.00 15.53 ? 180 ILE   A N   1 
ATOM   1306 C CA  . ILE   A 1 180 ? 5.010   3.599   -30.688 1.00 14.24 ? 180 ILE   A CA  1 
ATOM   1307 C C   . ILE   A 1 180 ? 3.657   3.941   -30.091 1.00 15.02 ? 180 ILE   A C   1 
ATOM   1308 O O   . ILE   A 1 180 ? 3.018   3.116   -29.430 1.00 16.19 ? 180 ILE   A O   1 
ATOM   1309 C CB  . ILE   A 1 180 ? 4.884   2.885   -32.050 1.00 15.61 ? 180 ILE   A CB  1 
ATOM   1310 C CG1 . ILE   A 1 180 ? 4.120   3.775   -33.041 1.00 17.73 ? 180 ILE   A CG1 1 
ATOM   1311 C CG2 . ILE   A 1 180 ? 4.255   1.499   -31.867 1.00 17.38 ? 180 ILE   A CG2 1 
ATOM   1312 C CD1 . ILE   A 1 180 ? 4.203   3.200   -34.461 1.00 20.04 ? 180 ILE   A CD1 1 
ATOM   1313 N N   . ASP   A 1 181 ? 3.245   5.208   -30.260 1.00 14.54 ? 181 ASP   A N   1 
ATOM   1314 C CA  . ASP   A 1 181 ? 1.904   5.674   -29.883 1.00 16.11 ? 181 ASP   A CA  1 
ATOM   1315 C C   . ASP   A 1 181 ? 1.025   5.796   -31.115 1.00 16.45 ? 181 ASP   A C   1 
ATOM   1316 O O   . ASP   A 1 181 ? 1.251   6.704   -31.931 1.00 17.71 ? 181 ASP   A O   1 
ATOM   1317 C CB  . ASP   A 1 181 ? 2.021   7.017   -29.169 1.00 16.33 ? 181 ASP   A CB  1 
ATOM   1318 C CG  . ASP   A 1 181 ? 0.681   7.592   -28.730 1.00 18.62 ? 181 ASP   A CG  1 
ATOM   1319 O OD1 . ASP   A 1 181 ? -0.380  7.096   -29.167 1.00 18.72 ? 181 ASP   A OD1 1 
ATOM   1320 O OD2 . ASP   A 1 181 ? 0.702   8.554   -27.904 1.00 20.83 ? 181 ASP   A OD2 1 
ATOM   1321 N N   . PRO   A 1 182 ? 0.037   4.899   -31.311 1.00 17.72 ? 182 PRO   A N   1 
ATOM   1322 C CA  . PRO   A 1 182 ? -0.817  4.965   -32.524 1.00 19.34 ? 182 PRO   A CA  1 
ATOM   1323 C C   . PRO   A 1 182 ? -1.601  6.250   -32.669 1.00 19.77 ? 182 PRO   A C   1 
ATOM   1324 O O   . PRO   A 1 182 ? -1.897  6.655   -33.791 1.00 23.53 ? 182 PRO   A O   1 
ATOM   1325 C CB  . PRO   A 1 182 ? -1.791  3.787   -32.350 1.00 19.73 ? 182 PRO   A CB  1 
ATOM   1326 C CG  . PRO   A 1 182 ? -1.113  2.880   -31.388 1.00 19.93 ? 182 PRO   A CG  1 
ATOM   1327 C CD  . PRO   A 1 182 ? -0.289  3.745   -30.450 1.00 18.33 ? 182 PRO   A CD  1 
ATOM   1328 N N   . ASN   A 1 183 ? -1.937  6.922   -31.579 1.00 17.21 ? 183 ASN   A N   1 
ATOM   1329 C CA  . ASN   A 1 183 ? -2.790  8.107   -31.684 1.00 18.00 ? 183 ASN   A CA  1 
ATOM   1330 C C   . ASN   A 1 183 ? -1.988  9.386   -31.913 1.00 18.62 ? 183 ASN   A C   1 
ATOM   1331 O O   . ASN   A 1 183 ? -2.523  10.334  -32.488 1.00 18.74 ? 183 ASN   A O   1 
ATOM   1332 C CB  . ASN   A 1 183 ? -3.591  8.287   -30.395 1.00 17.86 ? 183 ASN   A CB  1 
ATOM   1333 C CG  . ASN   A 1 183 ? -4.814  7.415   -30.340 1.00 19.80 ? 183 ASN   A CG  1 
ATOM   1334 O OD1 . ASN   A 1 183 ? -5.180  6.794   -31.363 1.00 20.96 ? 183 ASN   A OD1 1 
ATOM   1335 N ND2 . ASN   A 1 183 ? -5.437  7.309   -29.161 1.00 20.28 ? 183 ASN   A ND2 1 
ATOM   1336 N N   . SER   A 1 184 ? -0.730  9.467   -31.448 1.00 20.61 ? 184 SER   A N   1 
ATOM   1337 C CA  . SER   A 1 184 ? 0.110   10.626  -31.734 1.00 21.55 ? 184 SER   A CA  1 
ATOM   1338 C C   . SER   A 1 184 ? 1.043   10.416  -32.916 1.00 22.14 ? 184 SER   A C   1 
ATOM   1339 O O   . SER   A 1 184 ? 1.499   11.404  -33.516 1.00 22.88 ? 184 SER   A O   1 
ATOM   1340 C CB  . SER   A 1 184 ? 0.925   11.022  -30.496 1.00 21.85 ? 184 SER   A CB  1 
ATOM   1341 O OG  . SER   A 1 184 ? 1.971   10.089  -30.295 1.00 21.68 ? 184 SER   A OG  1 
ATOM   1342 N N   . GLY   A 1 185 ? 1.334   9.169   -33.271 1.00 21.81 ? 185 GLY   A N   1 
ATOM   1343 C CA  . GLY   A 1 185 ? 2.379   8.857   -34.214 1.00 22.24 ? 185 GLY   A CA  1 
ATOM   1344 C C   . GLY   A 1 185 ? 3.786   8.899   -33.653 1.00 21.62 ? 185 GLY   A C   1 
ATOM   1345 O O   . GLY   A 1 185 ? 4.741   8.549   -34.379 1.00 25.42 ? 185 GLY   A O   1 
ATOM   1346 N N   . PHE   A 1 186 ? 3.971   9.318   -32.401 1.00 19.36 ? 186 PHE   A N   1 
ATOM   1347 C CA  . PHE   A 1 186 ? 5.322   9.477   -31.877 1.00 17.90 ? 186 PHE   A CA  1 
ATOM   1348 C C   . PHE   A 1 186 ? 5.947   8.117   -31.603 1.00 18.06 ? 186 PHE   A C   1 
ATOM   1349 O O   . PHE   A 1 186 ? 5.323   7.247   -30.979 1.00 18.40 ? 186 PHE   A O   1 
ATOM   1350 C CB  . PHE   A 1 186 ? 5.285   10.290  -30.584 1.00 18.56 ? 186 PHE   A CB  1 
ATOM   1351 C CG  . PHE   A 1 186 ? 6.648   10.678  -30.067 1.00 23.61 ? 186 PHE   A CG  1 
ATOM   1352 C CD1 . PHE   A 1 186 ? 7.505   11.457  -30.834 1.00 28.84 ? 186 PHE   A CD1 1 
ATOM   1353 C CD2 . PHE   A 1 186 ? 7.066   10.265  -28.817 1.00 27.60 ? 186 PHE   A CD2 1 
ATOM   1354 C CE1 . PHE   A 1 186 ? 8.764   11.811  -30.342 1.00 30.51 ? 186 PHE   A CE1 1 
ATOM   1355 C CE2 . PHE   A 1 186 ? 8.320   10.631  -28.318 1.00 29.64 ? 186 PHE   A CE2 1 
ATOM   1356 C CZ  . PHE   A 1 186 ? 9.163   11.389  -29.087 1.00 29.98 ? 186 PHE   A CZ  1 
ATOM   1357 N N   . ILE   A 1 187 ? 7.201   7.955   -32.028 1.00 16.76 ? 187 ILE   A N   1 
ATOM   1358 C CA  . ILE   A 1 187 ? 7.958   6.727   -31.842 1.00 16.76 ? 187 ILE   A CA  1 
ATOM   1359 C C   . ILE   A 1 187 ? 9.246   7.066   -31.114 1.00 17.20 ? 187 ILE   A C   1 
ATOM   1360 O O   . ILE   A 1 187 ? 9.934   8.022   -31.491 1.00 19.00 ? 187 ILE   A O   1 
ATOM   1361 C CB  . ILE   A 1 187 ? 8.269   6.077   -33.212 1.00 17.57 ? 187 ILE   A CB  1 
ATOM   1362 C CG1 . ILE   A 1 187 ? 6.987   5.720   -33.972 1.00 20.62 ? 187 ILE   A CG1 1 
ATOM   1363 C CG2 . ILE   A 1 187 ? 9.133   4.830   -33.042 1.00 19.55 ? 187 ILE   A CG2 1 
ATOM   1364 C CD1 . ILE   A 1 187 ? 7.197   5.536   -35.488 1.00 24.26 ? 187 ILE   A CD1 1 
ATOM   1365 N N   . ARG   A 1 188 ? 9.602   6.257   -30.100 1.00 17.19 ? 188 ARG   A N   1 
ATOM   1366 C CA  . ARG   A 1 188 ? 10.898  6.336   -29.448 1.00 17.19 ? 188 ARG   A CA  1 
ATOM   1367 C C   . ARG   A 1 188 ? 11.674  5.061   -29.728 1.00 16.75 ? 188 ARG   A C   1 
ATOM   1368 O O   . ARG   A 1 188 ? 11.112  3.964   -29.685 1.00 17.75 ? 188 ARG   A O   1 
ATOM   1369 C CB  . ARG   A 1 188 ? 10.746  6.400   -27.938 1.00 19.40 ? 188 ARG   A CB  1 
ATOM   1370 C CG  . ARG   A 1 188 ? 10.090  7.651   -27.384 1.00 19.78 ? 188 ARG   A CG  1 
ATOM   1371 C CD  . ARG   A 1 188 ? 10.474  7.714   -25.904 1.00 22.92 ? 188 ARG   A CD  1 
ATOM   1372 N NE  . ARG   A 1 188 ? 9.760   8.749   -25.163 1.00 24.12 ? 188 ARG   A NE  1 
ATOM   1373 C CZ  . ARG   A 1 188 ? 10.203  9.983   -24.979 1.00 24.74 ? 188 ARG   A CZ  1 
ATOM   1374 N NH1 . ARG   A 1 188 ? 11.354  10.394  -25.498 1.00 25.81 ? 188 ARG   A NH1 1 
ATOM   1375 N NH2 . ARG   A 1 188 ? 9.480   10.823  -24.242 1.00 25.90 ? 188 ARG   A NH2 1 
ATOM   1376 N N   . TYR   A 1 189 ? 12.973  5.204   -29.996 1.00 17.43 ? 189 TYR   A N   1 
ATOM   1377 C CA  . TYR   A 1 189 ? 13.876  4.064   -30.103 1.00 16.93 ? 189 TYR   A CA  1 
ATOM   1378 C C   . TYR   A 1 189 ? 14.929  4.167   -29.014 1.00 17.23 ? 189 TYR   A C   1 
ATOM   1379 O O   . TYR   A 1 189 ? 15.495  5.243   -28.767 1.00 18.89 ? 189 TYR   A O   1 
ATOM   1380 C CB  . TYR   A 1 189 ? 14.590  4.049   -31.463 1.00 19.31 ? 189 TYR   A CB  1 
ATOM   1381 C CG  . TYR   A 1 189 ? 13.658  3.841   -32.618 1.00 18.89 ? 189 TYR   A CG  1 
ATOM   1382 C CD1 . TYR   A 1 189 ? 13.245  2.563   -32.979 1.00 20.33 ? 189 TYR   A CD1 1 
ATOM   1383 C CD2 . TYR   A 1 189 ? 13.123  4.917   -33.324 1.00 21.82 ? 189 TYR   A CD2 1 
ATOM   1384 C CE1 . TYR   A 1 189 ? 12.358  2.363   -34.035 1.00 21.94 ? 189 TYR   A CE1 1 
ATOM   1385 C CE2 . TYR   A 1 189 ? 12.265  4.715   -34.426 1.00 22.88 ? 189 TYR   A CE2 1 
ATOM   1386 C CZ  . TYR   A 1 189 ? 11.880  3.435   -34.762 1.00 22.14 ? 189 TYR   A CZ  1 
ATOM   1387 O OH  . TYR   A 1 189 ? 10.997  3.197   -35.817 1.00 21.45 ? 189 TYR   A OH  1 
ATOM   1388 N N   . ASP   A 1 190 ? 15.286  3.027   -28.447 1.00 17.11 ? 190 ASP   A N   1 
ATOM   1389 C CA  . ASP   A 1 190 ? 16.505  2.983   -27.668 1.00 17.90 ? 190 ASP   A CA  1 
ATOM   1390 C C   . ASP   A 1 190 ? 17.718  3.190   -28.572 1.00 18.14 ? 190 ASP   A C   1 
ATOM   1391 O O   . ASP   A 1 190 ? 17.737  2.764   -29.731 1.00 19.18 ? 190 ASP   A O   1 
ATOM   1392 C CB  . ASP   A 1 190 ? 16.626  1.625   -26.988 1.00 19.91 ? 190 ASP   A CB  1 
ATOM   1393 C CG  . ASP   A 1 190 ? 17.683  1.617   -25.919 1.00 22.39 ? 190 ASP   A CG  1 
ATOM   1394 O OD1 . ASP   A 1 190 ? 17.340  2.013   -24.784 1.00 22.99 ? 190 ASP   A OD1 1 
ATOM   1395 O OD2 . ASP   A 1 190 ? 18.864  1.255   -26.208 1.00 24.15 ? 190 ASP   A OD2 1 
ATOM   1396 N N   . GLU   A 1 191 ? 18.763  3.813   -28.004 1.00 19.86 ? 191 GLU   A N   1 
ATOM   1397 C CA  . GLU   A 1 191 ? 19.988  4.072   -28.751 1.00 21.63 ? 191 GLU   A CA  1 
ATOM   1398 C C   . GLU   A 1 191 ? 20.586  2.799   -29.350 1.00 22.82 ? 191 GLU   A C   1 
ATOM   1399 O O   . GLU   A 1 191 ? 21.161  2.834   -30.447 1.00 24.87 ? 191 GLU   A O   1 
ATOM   1400 C CB  . GLU   A 1 191 ? 20.989  4.775   -27.819 1.00 25.68 ? 191 GLU   A CB  1 
ATOM   1401 C CG  . GLU   A 1 191 ? 22.413  4.813   -28.340 1.00 34.51 ? 191 GLU   A CG  1 
ATOM   1402 C CD  . GLU   A 1 191 ? 23.365  5.553   -27.406 1.00 38.31 ? 191 GLU   A CD  1 
ATOM   1403 O OE1 . GLU   A 1 191 ? 23.408  5.237   -26.196 1.00 37.09 ? 191 GLU   A OE1 1 
ATOM   1404 O OE2 . GLU   A 1 191 ? 24.129  6.394   -27.904 1.00 38.33 ? 191 GLU   A OE2 1 
ATOM   1405 N N   . ARG   A 1 192 ? 20.440  1.672   -28.654 1.00 22.37 ? 192 ARG   A N   1 
ATOM   1406 C CA  . ARG   A 1 192 ? 20.994  0.410   -29.136 1.00 26.59 ? 192 ARG   A CA  1 
ATOM   1407 C C   . ARG   A 1 192 ? 20.305  -0.063  -30.419 1.00 23.73 ? 192 ARG   A C   1 
ATOM   1408 O O   . ARG   A 1 192 ? 20.913  -0.765  -31.222 1.00 25.90 ? 192 ARG   A O   1 
ATOM   1409 C CB  . ARG   A 1 192 ? 20.872  -0.641  -28.021 1.00 29.99 ? 192 ARG   A CB  1 
ATOM   1410 C CG  . ARG   A 1 192 ? 21.382  -2.010  -28.374 1.00 36.51 ? 192 ARG   A CG  1 
ATOM   1411 C CD  . ARG   A 1 192 ? 22.858  -2.115  -28.035 1.00 41.00 ? 192 ARG   A CD  1 
ATOM   1412 N NE  . ARG   A 1 192 ? 23.126  -1.797  -26.638 1.00 44.79 ? 192 ARG   A NE  1 
ATOM   1413 C CZ  . ARG   A 1 192 ? 22.962  -2.636  -25.623 1.00 51.80 ? 192 ARG   A CZ  1 
ATOM   1414 N NH1 . ARG   A 1 192 ? 22.561  -3.889  -25.814 1.00 51.57 ? 192 ARG   A NH1 1 
ATOM   1415 N NH2 . ARG   A 1 192 ? 23.232  -2.217  -24.386 1.00 55.03 ? 192 ARG   A NH2 1 
ATOM   1416 N N   . PHE   A 1 193 ? 19.043  0.301   -30.631 1.00 21.13 ? 193 PHE   A N   1 
ATOM   1417 C CA  . PHE   A 1 193 ? 18.236  -0.242  -31.716 1.00 21.70 ? 193 PHE   A CA  1 
ATOM   1418 C C   . PHE   A 1 193 ? 17.832  0.773   -32.762 1.00 24.68 ? 193 PHE   A C   1 
ATOM   1419 O O   . PHE   A 1 193 ? 17.088  0.422   -33.686 1.00 27.51 ? 193 PHE   A O   1 
ATOM   1420 C CB  . PHE   A 1 193 ? 17.004  -0.939  -31.136 1.00 20.48 ? 193 PHE   A CB  1 
ATOM   1421 C CG  . PHE   A 1 193 ? 17.354  -2.122  -30.305 1.00 22.26 ? 193 PHE   A CG  1 
ATOM   1422 C CD1 . PHE   A 1 193 ? 17.598  -3.359  -30.899 1.00 25.93 ? 193 PHE   A CD1 1 
ATOM   1423 C CD2 . PHE   A 1 193 ? 17.447  -2.009  -28.938 1.00 22.85 ? 193 PHE   A CD2 1 
ATOM   1424 C CE1 . PHE   A 1 193 ? 17.950  -4.462  -30.133 1.00 23.47 ? 193 PHE   A CE1 1 
ATOM   1425 C CE2 . PHE   A 1 193 ? 17.811  -3.118  -28.156 1.00 23.65 ? 193 PHE   A CE2 1 
ATOM   1426 C CZ  . PHE   A 1 193 ? 18.057  -4.344  -28.766 1.00 24.97 ? 193 PHE   A CZ  1 
ATOM   1427 N N   . LYS   A 1 194 ? 18.338  2.001   -32.678 1.00 23.86 ? 194 LYS   A N   1 
ATOM   1428 C CA  . LYS   A 1 194 ? 17.817  3.060   -33.538 1.00 31.10 ? 194 LYS   A CA  1 
ATOM   1429 C C   . LYS   A 1 194 ? 17.987  2.761   -35.028 1.00 33.20 ? 194 LYS   A C   1 
ATOM   1430 O O   . LYS   A 1 194 ? 17.160  3.187   -35.839 1.00 36.58 ? 194 LYS   A O   1 
ATOM   1431 C CB  . LYS   A 1 194 ? 18.443  4.410   -33.169 1.00 36.09 ? 194 LYS   A CB  1 
ATOM   1432 C CG  . LYS   A 1 194 ? 19.948  4.482   -33.371 1.00 45.50 ? 194 LYS   A CG  1 
ATOM   1433 C CD  . LYS   A 1 194 ? 20.526  5.831   -32.886 1.00 54.17 ? 194 LYS   A CD  1 
ATOM   1434 C CE  . LYS   A 1 194 ? 22.023  5.747   -32.577 1.00 59.98 ? 194 LYS   A CE  1 
ATOM   1435 N NZ  . LYS   A 1 194 ? 22.353  6.269   -31.208 1.00 64.30 ? 194 LYS   A NZ  1 
ATOM   1436 N N   . THR   A 1 195 ? 19.026  2.053   -35.428 1.00 35.81 ? 195 THR   A N   1 
ATOM   1437 C CA  . THR   A 1 195 ? 19.131  1.763   -36.858 1.00 40.29 ? 195 THR   A CA  1 
ATOM   1438 C C   . THR   A 1 195 ? 18.688  0.349   -37.209 1.00 37.77 ? 195 THR   A C   1 
ATOM   1439 O O   . THR   A 1 195 ? 18.503  0.032   -38.394 1.00 42.76 ? 195 THR   A O   1 
ATOM   1440 C CB  . THR   A 1 195 ? 20.539  2.056   -37.374 1.00 45.27 ? 195 THR   A CB  1 
ATOM   1441 O OG1 . THR   A 1 195 ? 21.477  1.141   -36.786 1.00 46.97 ? 195 THR   A OG1 1 
ATOM   1442 C CG2 . THR   A 1 195 ? 20.916  3.497   -37.026 1.00 48.29 ? 195 THR   A CG2 1 
ATOM   1443 N N   . LYS   A 1 196 ? 18.466  -0.483  -36.214 1.00 27.05 ? 196 LYS   A N   1 
ATOM   1444 C CA  . LYS   A 1 196 ? 18.108  -1.868  -36.493 1.00 24.85 ? 196 LYS   A CA  1 
ATOM   1445 C C   . LYS   A 1 196 ? 16.594  -2.038  -36.605 1.00 22.54 ? 196 LYS   A C   1 
ATOM   1446 O O   . LYS   A 1 196 ? 16.116  -2.810  -37.447 1.00 24.27 ? 196 LYS   A O   1 
ATOM   1447 C CB  . LYS   A 1 196 ? 18.699  -2.737  -35.379 1.00 25.07 ? 196 LYS   A CB  1 
ATOM   1448 C CG  . LYS   A 1 196 ? 18.193  -4.178  -35.277 1.00 26.29 ? 196 LYS   A CG  1 
ATOM   1449 C CD  . LYS   A 1 196 ? 18.794  -5.115  -36.304 1.00 26.29 ? 196 LYS   A CD  1 
ATOM   1450 C CE  . LYS   A 1 196 ? 20.317  -5.023  -36.393 1.00 25.36 ? 196 LYS   A CE  1 
ATOM   1451 N NZ  . LYS   A 1 196 ? 20.789  -5.913  -37.504 1.00 24.34 ? 196 LYS   A NZ  1 
ATOM   1452 N N   . ALA   A 1 197 ? 15.815  -1.313  -35.783 1.00 21.37 ? 197 ALA   A N   1 
ATOM   1453 C CA  . ALA   A 1 197 ? 14.371  -1.495  -35.711 1.00 19.27 ? 197 ALA   A CA  1 
ATOM   1454 C C   . ALA   A 1 197 ? 13.628  -0.363  -36.417 1.00 20.13 ? 197 ALA   A C   1 
ATOM   1455 O O   . ALA   A 1 197 ? 14.049  0.794   -36.378 1.00 21.68 ? 197 ALA   A O   1 
ATOM   1456 C CB  . ALA   A 1 197 ? 13.905  -1.558  -34.240 1.00 21.37 ? 197 ALA   A CB  1 
ATOM   1457 N N   . THR   A 1 198 ? 12.464  -0.694  -36.987 1.00 19.16 ? 198 THR   A N   1 
ATOM   1458 C CA  . THR   A 1 198 ? 11.479  0.298   -37.445 1.00 17.99 ? 198 THR   A CA  1 
ATOM   1459 C C   . THR   A 1 198 ? 10.108  -0.135  -36.938 1.00 18.36 ? 198 THR   A C   1 
ATOM   1460 O O   . THR   A 1 198 ? 9.677   -1.260  -37.216 1.00 18.32 ? 198 THR   A O   1 
ATOM   1461 C CB  . THR   A 1 198 ? 11.437  0.387   -38.981 1.00 18.64 ? 198 THR   A CB  1 
ATOM   1462 O OG1 . THR   A 1 198 ? 12.751  0.695   -39.474 1.00 20.17 ? 198 THR   A OG1 1 
ATOM   1463 C CG2 . THR   A 1 198 ? 10.443  1.489   -39.449 1.00 21.34 ? 198 THR   A CG2 1 
ATOM   1464 N N   . LEU   A 1 199 ? 9.423   0.743   -36.199 1.00 17.04 ? 199 LEU   A N   1 
ATOM   1465 C CA  . LEU   A 1 199 ? 8.124   0.427   -35.602 1.00 17.03 ? 199 LEU   A CA  1 
ATOM   1466 C C   . LEU   A 1 199 ? 7.012   1.076   -36.405 1.00 18.23 ? 199 LEU   A C   1 
ATOM   1467 O O   . LEU   A 1 199 ? 7.115   2.250   -36.769 1.00 19.45 ? 199 LEU   A O   1 
ATOM   1468 C CB  . LEU   A 1 199 ? 8.017   0.939   -34.165 1.00 18.91 ? 199 LEU   A CB  1 
ATOM   1469 C CG  . LEU   A 1 199 ? 9.046   0.394   -33.160 1.00 18.18 ? 199 LEU   A CG  1 
ATOM   1470 C CD1 . LEU   A 1 199 ? 8.662   0.848   -31.726 1.00 18.62 ? 199 LEU   A CD1 1 
ATOM   1471 C CD2 . LEU   A 1 199 ? 9.170   -1.156  -33.277 1.00 19.84 ? 199 LEU   A CD2 1 
ATOM   1472 N N   . THR   A 1 200 ? 5.955   0.313   -36.689 1.00 17.70 ? 200 THR   A N   1 
ATOM   1473 C CA  . THR   A 1 200 ? 4.779   0.857   -37.349 1.00 19.34 ? 200 THR   A CA  1 
ATOM   1474 C C   . THR   A 1 200 ? 3.546   0.242   -36.695 1.00 18.62 ? 200 THR   A C   1 
ATOM   1475 O O   . THR   A 1 200 ? 3.650   -0.744  -35.949 1.00 18.85 ? 200 THR   A O   1 
ATOM   1476 C CB  . THR   A 1 200 ? 4.784   0.592   -38.865 1.00 22.01 ? 200 THR   A CB  1 
ATOM   1477 O OG1 . THR   A 1 200 ? 4.738   -0.821  -39.113 1.00 22.91 ? 200 THR   A OG1 1 
ATOM   1478 C CG2 . THR   A 1 200 ? 6.010   1.210   -39.545 1.00 22.63 ? 200 THR   A CG2 1 
ATOM   1479 N N   . VAL   A 1 201 ? 2.366   0.802   -37.008 1.00 21.59 ? 201 VAL   A N   1 
ATOM   1480 C CA  A VAL   A 1 201 ? 1.098   0.208   -36.578 0.85 22.20 ? 201 VAL   A CA  1 
ATOM   1481 C CA  B VAL   A 1 201 ? 1.091   0.259   -36.548 0.15 22.57 ? 201 VAL   A CA  1 
ATOM   1482 C C   . VAL   A 1 201 ? 0.081   0.330   -37.687 1.00 24.04 ? 201 VAL   A C   1 
ATOM   1483 O O   . VAL   A 1 201 ? 0.116   1.254   -38.510 1.00 26.73 ? 201 VAL   A O   1 
ATOM   1484 C CB  A VAL   A 1 201 ? 0.478   0.785   -35.288 0.85 25.74 ? 201 VAL   A CB  1 
ATOM   1485 C CB  B VAL   A 1 201 ? 0.571   1.005   -35.293 0.15 25.97 ? 201 VAL   A CB  1 
ATOM   1486 C CG1 A VAL   A 1 201 ? 1.324   0.527   -34.116 0.85 27.91 ? 201 VAL   A CG1 1 
ATOM   1487 C CG1 B VAL   A 1 201 ? -0.810  0.540   -34.922 0.15 27.96 ? 201 VAL   A CG1 1 
ATOM   1488 C CG2 A VAL   A 1 201 ? 0.283   2.275   -35.465 0.85 27.18 ? 201 VAL   A CG2 1 
ATOM   1489 C CG2 B VAL   A 1 201 ? 1.500   0.800   -34.121 0.15 27.75 ? 201 VAL   A CG2 1 
ATOM   1490 N N   . ASP   A 1 202 ? -0.812  -0.638  -37.718 1.00 23.27 ? 202 ASP   A N   1 
ATOM   1491 C CA  . ASP   A 1 202 ? -1.980  -0.608  -38.585 1.00 23.29 ? 202 ASP   A CA  1 
ATOM   1492 C C   . ASP   A 1 202 ? -3.235  -0.645  -37.716 1.00 23.72 ? 202 ASP   A C   1 
ATOM   1493 O O   . ASP   A 1 202 ? -3.564  -1.689  -37.152 1.00 26.13 ? 202 ASP   A O   1 
ATOM   1494 C CB  . ASP   A 1 202 ? -1.935  -1.760  -39.591 1.00 26.89 ? 202 ASP   A CB  1 
ATOM   1495 C CG  . ASP   A 1 202 ? -3.002  -1.631  -40.649 1.00 33.31 ? 202 ASP   A CG  1 
ATOM   1496 O OD1 . ASP   A 1 202 ? -2.775  -0.902  -41.654 1.00 37.29 ? 202 ASP   A OD1 1 
ATOM   1497 O OD2 . ASP   A 1 202 ? -4.060  -2.269  -40.475 1.00 33.63 ? 202 ASP   A OD2 1 
ATOM   1498 N N   . LYS   A 1 203 ? -3.923  0.498   -37.585 1.00 27.61 ? 203 LYS   A N   1 
ATOM   1499 C CA  . LYS   A 1 203 ? -5.123  0.540   -36.746 1.00 29.06 ? 203 LYS   A CA  1 
ATOM   1500 C C   . LYS   A 1 203 ? -6.235  -0.380  -37.225 1.00 29.20 ? 203 LYS   A C   1 
ATOM   1501 O O   . LYS   A 1 203 ? -6.858  -1.038  -36.374 1.00 27.91 ? 203 LYS   A O   1 
ATOM   1502 C CB  . LYS   A 1 203 ? -5.626  1.986   -36.629 1.00 30.50 ? 203 LYS   A CB  1 
ATOM   1503 C CG  . LYS   A 1 203 ? -4.674  2.881   -35.924 1.00 31.78 ? 203 LYS   A CG  1 
ATOM   1504 C CD  . LYS   A 1 203 ? -5.420  4.027   -35.281 1.00 33.43 ? 203 LYS   A CD  1 
ATOM   1505 C CE  . LYS   A 1 203 ? -5.918  4.960   -36.355 1.00 37.89 ? 203 LYS   A CE  1 
ATOM   1506 N NZ  . LYS   A 1 203 ? -6.820  6.040   -35.799 1.00 41.48 ? 203 LYS   A NZ  1 
ATOM   1507 N N   . PRO   A 1 204 ? -6.550  -0.460  -38.525 1.00 31.97 ? 204 PRO   A N   1 
ATOM   1508 C CA  . PRO   A 1 204 ? -7.685  -1.300  -38.936 1.00 32.62 ? 204 PRO   A CA  1 
ATOM   1509 C C   . PRO   A 1 204 ? -7.515  -2.758  -38.553 1.00 32.83 ? 204 PRO   A C   1 
ATOM   1510 O O   . PRO   A 1 204 ? -8.481  -3.407  -38.139 1.00 33.44 ? 204 PRO   A O   1 
ATOM   1511 C CB  . PRO   A 1 204 ? -7.772  -1.070  -40.455 1.00 33.28 ? 204 PRO   A CB  1 
ATOM   1512 C CG  . PRO   A 1 204 ? -7.200  0.250   -40.673 1.00 29.68 ? 204 PRO   A CG  1 
ATOM   1513 C CD  . PRO   A 1 204 ? -6.052  0.354   -39.647 1.00 31.67 ? 204 PRO   A CD  1 
ATOM   1514 N N   . SER   A 1 205 ? -6.293  -3.283  -38.605 1.00 30.59 ? 205 SER   A N   1 
ATOM   1515 C CA  . SER   A 1 205 ? -6.077  -4.668  -38.234 1.00 27.90 ? 205 SER   A CA  1 
ATOM   1516 C C   . SER   A 1 205 ? -5.606  -4.814  -36.794 1.00 26.51 ? 205 SER   A C   1 
ATOM   1517 O O   . SER   A 1 205 ? -5.239  -5.916  -36.396 1.00 28.50 ? 205 SER   A O   1 
ATOM   1518 C CB  . SER   A 1 205 ? -5.083  -5.337  -39.195 1.00 30.07 ? 205 SER   A CB  1 
ATOM   1519 O OG  . SER   A 1 205 ? -3.759  -4.842  -38.997 1.00 29.62 ? 205 SER   A OG  1 
ATOM   1520 N N   . SER   A 1 206 ? -5.583  -3.724  -36.015 1.00 25.02 ? 206 SER   A N   1 
ATOM   1521 C CA  . SER   A 1 206 ? -5.086  -3.737  -34.629 1.00 24.75 ? 206 SER   A CA  1 
ATOM   1522 C C   . SER   A 1 206 ? -3.748  -4.439  -34.476 1.00 21.52 ? 206 SER   A C   1 
ATOM   1523 O O   . SER   A 1 206 ? -3.541  -5.230  -33.557 1.00 23.76 ? 206 SER   A O   1 
ATOM   1524 C CB  . SER   A 1 206 ? -6.098  -4.259  -33.611 1.00 27.29 ? 206 SER   A CB  1 
ATOM   1525 O OG  . SER   A 1 206 ? -7.379  -3.724  -33.873 1.00 29.57 ? 206 SER   A OG  1 
ATOM   1526 N N   . THR   A 1 207 ? -2.827  -4.153  -35.388 1.00 21.48 ? 207 THR   A N   1 
ATOM   1527 C CA  . THR   A 1 207 ? -1.555  -4.838  -35.384 1.00 21.12 ? 207 THR   A CA  1 
ATOM   1528 C C   . THR   A 1 207 ? -0.408  -3.843  -35.335 1.00 20.70 ? 207 THR   A C   1 
ATOM   1529 O O   . THR   A 1 207 ? -0.402  -2.857  -36.085 1.00 23.97 ? 207 THR   A O   1 
ATOM   1530 C CB  . THR   A 1 207 ? -1.448  -5.750  -36.627 1.00 22.18 ? 207 THR   A CB  1 
ATOM   1531 O OG1 . THR   A 1 207 ? -2.541  -6.682  -36.615 1.00 24.10 ? 207 THR   A OG1 1 
ATOM   1532 C CG2 . THR   A 1 207 ? -0.123  -6.532  -36.635 1.00 23.10 ? 207 THR   A CG2 1 
ATOM   1533 N N   . ALA   A 1 208 ? 0.561   -4.129  -34.462 1.00 19.35 ? 208 ALA   A N   1 
ATOM   1534 C CA  . ALA   A 1 208 ? 1.823   -3.407  -34.388 1.00 18.82 ? 208 ALA   A CA  1 
ATOM   1535 C C   . ALA   A 1 208 ? 2.900   -4.255  -35.063 1.00 17.36 ? 208 ALA   A C   1 
ATOM   1536 O O   . ALA   A 1 208 ? 2.869   -5.488  -34.975 1.00 19.39 ? 208 ALA   A O   1 
ATOM   1537 C CB  . ALA   A 1 208 ? 2.216   -3.146  -32.911 1.00 22.06 ? 208 ALA   A CB  1 
ATOM   1538 N N   . TYR   A 1 209 ? 3.814   -3.588  -35.769 1.00 17.26 ? 209 TYR   A N   1 
ATOM   1539 C CA  . TYR   A 1 209 ? 4.879   -4.252  -36.500 1.00 17.16 ? 209 TYR   A CA  1 
ATOM   1540 C C   . TYR   A 1 209 ? 6.232   -3.704  -36.086 1.00 17.68 ? 209 TYR   A C   1 
ATOM   1541 O O   . TYR   A 1 209 ? 6.390   -2.506  -35.812 1.00 18.74 ? 209 TYR   A O   1 
ATOM   1542 C CB  . TYR   A 1 209 ? 4.756   -4.000  -38.004 1.00 20.13 ? 209 TYR   A CB  1 
ATOM   1543 C CG  . TYR   A 1 209 ? 3.551   -4.657  -38.659 1.00 21.03 ? 209 TYR   A CG  1 
ATOM   1544 C CD1 . TYR   A 1 209 ? 3.520   -6.042  -38.896 1.00 23.22 ? 209 TYR   A CD1 1 
ATOM   1545 C CD2 . TYR   A 1 209 ? 2.423   -3.892  -39.043 1.00 21.61 ? 209 TYR   A CD2 1 
ATOM   1546 C CE1 . TYR   A 1 209 ? 2.448   -6.645  -39.507 1.00 25.23 ? 209 TYR   A CE1 1 
ATOM   1547 C CE2 . TYR   A 1 209 ? 1.320   -4.524  -39.650 1.00 24.34 ? 209 TYR   A CE2 1 
ATOM   1548 C CZ  . TYR   A 1 209 ? 1.355   -5.885  -39.876 1.00 26.86 ? 209 TYR   A CZ  1 
ATOM   1549 O OH  . TYR   A 1 209 ? 0.288   -6.487  -40.486 1.00 29.64 ? 209 TYR   A OH  1 
ATOM   1550 N N   . MET   A 1 210 ? 7.223   -4.591  -36.111 1.00 16.28 ? 210 MET   A N   1 
ATOM   1551 C CA  . MET   A 1 210 ? 8.624   -4.248  -35.943 1.00 17.22 ? 210 MET   A CA  1 
ATOM   1552 C C   . MET   A 1 210 ? 9.428   -4.876  -37.060 1.00 17.89 ? 210 MET   A C   1 
ATOM   1553 O O   . MET   A 1 210 ? 9.443   -6.102  -37.207 1.00 19.53 ? 210 MET   A O   1 
ATOM   1554 C CB  . MET   A 1 210 ? 9.148   -4.712  -34.586 1.00 15.57 ? 210 MET   A CB  1 
ATOM   1555 C CG  . MET   A 1 210 ? 10.577  -4.216  -34.404 1.00 16.73 ? 210 MET   A CG  1 
ATOM   1556 S SD  . MET   A 1 210 ? 11.244  -4.471  -32.756 1.00 18.73 ? 210 MET   A SD  1 
ATOM   1557 C CE  . MET   A 1 210 ? 11.116  -6.264  -32.574 1.00 19.67 ? 210 MET   A CE  1 
ATOM   1558 N N   . GLN   A 1 211 ? 10.083  -4.046  -37.859 1.00 17.69 ? 211 GLN   A N   1 
ATOM   1559 C CA  . GLN   A 1 211 ? 11.023  -4.554  -38.845 1.00 18.95 ? 211 GLN   A CA  1 
ATOM   1560 C C   . GLN   A 1 211 ? 12.418  -4.509  -38.252 1.00 19.83 ? 211 GLN   A C   1 
ATOM   1561 O O   . GLN   A 1 211 ? 12.802  -3.487  -37.677 1.00 19.46 ? 211 GLN   A O   1 
ATOM   1562 C CB  . GLN   A 1 211 ? 10.977  -3.664  -40.099 1.00 21.56 ? 211 GLN   A CB  1 
ATOM   1563 C CG  . GLN   A 1 211 ? 11.944  -4.148  -41.172 1.00 26.11 ? 211 GLN   A CG  1 
ATOM   1564 C CD  . GLN   A 1 211 ? 12.201  -3.130  -42.264 1.00 30.55 ? 211 GLN   A CD  1 
ATOM   1565 O OE1 . GLN   A 1 211 ? 11.550  -3.213  -43.292 1.00 33.59 ? 211 GLN   A OE1 1 
ATOM   1566 N NE2 . GLN   A 1 211 ? 13.165  -2.209  -42.076 1.00 30.49 ? 211 GLN   A NE2 1 
ATOM   1567 N N   . LEU   A 1 212 ? 13.158  -5.615  -38.367 1.00 19.22 ? 212 LEU   A N   1 
ATOM   1568 C CA  . LEU   A 1 212 ? 14.585  -5.662  -38.019 1.00 19.25 ? 212 LEU   A CA  1 
ATOM   1569 C C   . LEU   A 1 212 ? 15.342  -5.811  -39.325 1.00 20.96 ? 212 LEU   A C   1 
ATOM   1570 O O   . LEU   A 1 212 ? 15.087  -6.757  -40.085 1.00 22.91 ? 212 LEU   A O   1 
ATOM   1571 C CB  . LEU   A 1 212 ? 14.924  -6.832  -37.079 1.00 19.27 ? 212 LEU   A CB  1 
ATOM   1572 C CG  . LEU   A 1 212 ? 14.147  -6.806  -35.752 1.00 20.45 ? 212 LEU   A CG  1 
ATOM   1573 C CD1 . LEU   A 1 212 ? 14.226  -8.126  -35.018 1.00 22.52 ? 212 LEU   A CD1 1 
ATOM   1574 C CD2 . LEU   A 1 212 ? 14.559  -5.641  -34.834 1.00 19.90 ? 212 LEU   A CD2 1 
ATOM   1575 N N   . SER   A 1 213 ? 16.259  -4.890  -39.580 1.00 22.52 ? 213 SER   A N   1 
ATOM   1576 C CA  . SER   A 1 213 ? 16.959  -4.840  -40.848 1.00 23.59 ? 213 SER   A CA  1 
ATOM   1577 C C   . SER   A 1 213 ? 18.388  -5.330  -40.715 1.00 23.54 ? 213 SER   A C   1 
ATOM   1578 O O   . SER   A 1 213 ? 18.927  -5.481  -39.613 1.00 25.17 ? 213 SER   A O   1 
ATOM   1579 C CB  . SER   A 1 213 ? 16.964  -3.410  -41.395 1.00 27.93 ? 213 SER   A CB  1 
ATOM   1580 O OG  . SER   A 1 213 ? 17.590  -2.544  -40.456 1.00 32.49 ? 213 SER   A OG  1 
ATOM   1581 N N   . SER   A 1 214 ? 18.974  -5.611  -41.881 1.00 24.87 ? 214 SER   A N   1 
ATOM   1582 C CA  . SER   A 1 214 ? 20.383  -5.994  -42.004 1.00 27.50 ? 214 SER   A CA  1 
ATOM   1583 C C   . SER   A 1 214 ? 20.751  -7.058  -40.979 1.00 25.67 ? 214 SER   A C   1 
ATOM   1584 O O   . SER   A 1 214 ? 21.669  -6.896  -40.172 1.00 26.74 ? 214 SER   A O   1 
ATOM   1585 C CB  . SER   A 1 214 ? 21.276  -4.773  -41.804 1.00 33.56 ? 214 SER   A CB  1 
ATOM   1586 O OG  . SER   A 1 214 ? 21.001  -3.781  -42.768 1.00 36.46 ? 214 SER   A OG  1 
ATOM   1587 N N   . LEU   A 1 215 ? 20.009  -8.158  -41.003 1.00 24.16 ? 215 LEU   A N   1 
ATOM   1588 C CA  . LEU   A 1 215 ? 20.124  -9.163  -39.951 1.00 23.26 ? 215 LEU   A CA  1 
ATOM   1589 C C   . LEU   A 1 215 ? 21.512  -9.777  -39.878 1.00 25.13 ? 215 LEU   A C   1 
ATOM   1590 O O   . LEU   A 1 215 ? 22.159  -10.032 -40.895 1.00 26.85 ? 215 LEU   A O   1 
ATOM   1591 C CB  . LEU   A 1 215 ? 19.096  -10.259 -40.194 1.00 22.68 ? 215 LEU   A CB  1 
ATOM   1592 C CG  . LEU   A 1 215 ? 17.704  -9.763  -39.882 1.00 22.09 ? 215 LEU   A CG  1 
ATOM   1593 C CD1 . LEU   A 1 215 ? 16.741  -10.839 -40.365 1.00 24.38 ? 215 LEU   A CD1 1 
ATOM   1594 C CD2 . LEU   A 1 215 ? 17.533  -9.462  -38.359 1.00 23.13 ? 215 LEU   A CD2 1 
ATOM   1595 N N   . THR   A 1 216 ? 21.969  -10.001 -38.651 1.00 24.19 ? 216 THR   A N   1 
ATOM   1596 C CA  . THR   A 1 216 ? 23.186  -10.769 -38.408 1.00 24.37 ? 216 THR   A CA  1 
ATOM   1597 C C   . THR   A 1 216 ? 22.900  -11.848 -37.369 1.00 22.95 ? 216 THR   A C   1 
ATOM   1598 O O   . THR   A 1 216 ? 21.830  -11.872 -36.749 1.00 23.40 ? 216 THR   A O   1 
ATOM   1599 C CB  . THR   A 1 216 ? 24.316  -9.891  -37.854 1.00 29.74 ? 216 THR   A CB  1 
ATOM   1600 O OG1 . THR   A 1 216 ? 24.036  -9.601  -36.483 1.00 30.70 ? 216 THR   A OG1 1 
ATOM   1601 C CG2 . THR   A 1 216 ? 24.451  -8.594  -38.623 1.00 33.00 ? 216 THR   A CG2 1 
ATOM   1602 N N   . SER   A 1 217 ? 23.889  -12.728 -37.164 1.00 24.37 ? 217 SER   A N   1 
ATOM   1603 C CA  A SER   A 1 217 ? 23.731  -13.799 -36.189 0.49 24.47 ? 217 SER   A CA  1 
ATOM   1604 C CA  B SER   A 1 217 ? 23.764  -13.796 -36.177 0.51 24.16 ? 217 SER   A CA  1 
ATOM   1605 C C   . SER   A 1 217 ? 23.446  -13.248 -34.789 1.00 24.12 ? 217 SER   A C   1 
ATOM   1606 O O   . SER   A 1 217 ? 22.745  -13.895 -34.002 1.00 27.51 ? 217 SER   A O   1 
ATOM   1607 C CB  A SER   A 1 217 ? 24.964  -14.709 -36.214 0.49 25.72 ? 217 SER   A CB  1 
ATOM   1608 C CB  B SER   A 1 217 ? 25.068  -14.591 -36.147 0.51 24.75 ? 217 SER   A CB  1 
ATOM   1609 O OG  A SER   A 1 217 ? 24.997  -15.480 -37.413 0.49 25.24 ? 217 SER   A OG  1 
ATOM   1610 O OG  B SER   A 1 217 ? 26.144  -13.742 -35.790 0.51 24.20 ? 217 SER   A OG  1 
ATOM   1611 N N   . ASP   A 1 218 ? 23.936  -12.047 -34.477 1.00 24.62 ? 218 ASP   A N   1 
ATOM   1612 C CA  . ASP   A 1 218 ? 23.683  -11.460 -33.175 1.00 25.04 ? 218 ASP   A CA  1 
ATOM   1613 C C   . ASP   A 1 218 ? 22.213  -11.143 -32.932 1.00 23.57 ? 218 ASP   A C   1 
ATOM   1614 O O   . ASP   A 1 218 ? 21.832  -10.894 -31.784 1.00 25.06 ? 218 ASP   A O   1 
ATOM   1615 C CB  . ASP   A 1 218 ? 24.501  -10.176 -33.012 1.00 30.72 ? 218 ASP   A CB  1 
ATOM   1616 C CG  . ASP   A 1 218 ? 24.559  -9.721  -31.558 1.00 35.39 ? 218 ASP   A CG  1 
ATOM   1617 O OD1 . ASP   A 1 218 ? 24.995  -10.539 -30.709 1.00 36.07 ? 218 ASP   A OD1 1 
ATOM   1618 O OD2 . ASP   A 1 218 ? 24.112  -8.573  -31.256 1.00 38.10 ? 218 ASP   A OD2 1 
ATOM   1619 N N   . ASP   A 1 219 ? 21.389  -11.107 -33.976 1.00 19.65 ? 219 ASP   A N   1 
ATOM   1620 C CA  . ASP   A 1 219 ? 19.988  -10.750 -33.819 1.00 18.31 ? 219 ASP   A CA  1 
ATOM   1621 C C   . ASP   A 1 219 ? 19.094  -11.904 -33.388 1.00 18.28 ? 219 ASP   A C   1 
ATOM   1622 O O   . ASP   A 1 219 ? 17.923  -11.645 -33.060 1.00 18.59 ? 219 ASP   A O   1 
ATOM   1623 C CB  . ASP   A 1 219 ? 19.469  -10.117 -35.112 1.00 18.81 ? 219 ASP   A CB  1 
ATOM   1624 C CG  . ASP   A 1 219 ? 20.185  -8.816  -35.439 1.00 21.02 ? 219 ASP   A CG  1 
ATOM   1625 O OD1 . ASP   A 1 219 ? 20.396  -7.990  -34.516 1.00 23.06 ? 219 ASP   A OD1 1 
ATOM   1626 O OD2 . ASP   A 1 219 ? 20.521  -8.584  -36.626 1.00 22.24 ? 219 ASP   A OD2 1 
ATOM   1627 N N   . SER   A 1 220 ? 19.572  -13.159 -33.429 1.00 17.74 ? 220 SER   A N   1 
ATOM   1628 C CA  . SER   A 1 220 ? 18.739  -14.261 -32.973 1.00 17.23 ? 220 SER   A CA  1 
ATOM   1629 C C   . SER   A 1 220 ? 18.448  -14.087 -31.477 1.00 17.08 ? 220 SER   A C   1 
ATOM   1630 O O   . SER   A 1 220 ? 19.375  -13.982 -30.659 1.00 18.78 ? 220 SER   A O   1 
ATOM   1631 C CB  . SER   A 1 220 ? 19.515  -15.571 -33.190 1.00 17.67 ? 220 SER   A CB  1 
ATOM   1632 O OG  . SER   A 1 220 ? 19.815  -15.815 -34.560 1.00 19.67 ? 220 SER   A OG  1 
ATOM   1633 N N   . ALA   A 1 221 ? 17.160  -14.072 -31.110 1.00 15.41 ? 221 ALA   A N   1 
ATOM   1634 C CA  . ALA   A 1 221 ? 16.692  -13.732 -29.756 1.00 14.91 ? 221 ALA   A CA  1 
ATOM   1635 C C   . ALA   A 1 221 ? 15.191  -13.890 -29.741 1.00 14.74 ? 221 ALA   A C   1 
ATOM   1636 O O   . ALA   A 1 221 ? 14.590  -14.184 -30.783 1.00 16.09 ? 221 ALA   A O   1 
ATOM   1637 C CB  . ALA   A 1 221 ? 17.095  -12.312 -29.292 1.00 17.44 ? 221 ALA   A CB  1 
ATOM   1638 N N   . VAL   A 1 222 ? 14.580  -13.691 -28.586 1.00 14.66 ? 222 VAL   A N   1 
ATOM   1639 C CA  . VAL   A 1 222 ? 13.117  -13.588 -28.475 1.00 14.81 ? 222 VAL   A CA  1 
ATOM   1640 C C   . VAL   A 1 222 ? 12.725  -12.121 -28.428 1.00 15.31 ? 222 VAL   A C   1 
ATOM   1641 O O   . VAL   A 1 222 ? 13.383  -11.309 -27.764 1.00 15.22 ? 222 VAL   A O   1 
ATOM   1642 C CB  . VAL   A 1 222 ? 12.608  -14.330 -27.222 1.00 16.47 ? 222 VAL   A CB  1 
ATOM   1643 C CG1 . VAL   A 1 222 ? 11.067  -14.349 -27.203 1.00 16.92 ? 222 VAL   A CG1 1 
ATOM   1644 C CG2 . VAL   A 1 222 ? 13.165  -15.794 -27.230 1.00 17.61 ? 222 VAL   A CG2 1 
ATOM   1645 N N   . TYR   A 1 223 ? 11.684  -11.769 -29.172 1.00 14.83 ? 223 TYR   A N   1 
ATOM   1646 C CA  . TYR   A 1 223 ? 11.218  -10.378 -29.279 1.00 12.97 ? 223 TYR   A CA  1 
ATOM   1647 C C   . TYR   A 1 223 ? 9.766   -10.323 -28.845 1.00 12.67 ? 223 TYR   A C   1 
ATOM   1648 O O   . TYR   A 1 223 ? 8.925   -11.071 -29.391 1.00 15.50 ? 223 TYR   A O   1 
ATOM   1649 C CB  . TYR   A 1 223 ? 11.343  -9.882  -30.721 1.00 14.46 ? 223 TYR   A CB  1 
ATOM   1650 C CG  . TYR   A 1 223 ? 12.782  -9.771  -31.155 1.00 14.71 ? 223 TYR   A CG  1 
ATOM   1651 C CD1 . TYR   A 1 223 ? 13.485  -10.879 -31.701 1.00 14.21 ? 223 TYR   A CD1 1 
ATOM   1652 C CD2 . TYR   A 1 223 ? 13.488  -8.590  -30.944 1.00 15.11 ? 223 TYR   A CD2 1 
ATOM   1653 C CE1 . TYR   A 1 223 ? 14.819  -10.777 -32.050 1.00 15.35 ? 223 TYR   A CE1 1 
ATOM   1654 C CE2 . TYR   A 1 223 ? 14.819  -8.463  -31.309 1.00 15.62 ? 223 TYR   A CE2 1 
ATOM   1655 C CZ  . TYR   A 1 223 ? 15.484  -9.571  -31.865 1.00 15.02 ? 223 TYR   A CZ  1 
ATOM   1656 O OH  . TYR   A 1 223 ? 16.802  -9.443  -32.198 1.00 17.02 ? 223 TYR   A OH  1 
ATOM   1657 N N   . PHE   A 1 224 ? 9.460   -9.454  -27.880 1.00 14.08 ? 224 PHE   A N   1 
ATOM   1658 C CA  . PHE   A 1 224 ? 8.130   -9.344  -27.300 1.00 14.57 ? 224 PHE   A CA  1 
ATOM   1659 C C   . PHE   A 1 224 ? 7.536   -7.990  -27.637 1.00 14.29 ? 224 PHE   A C   1 
ATOM   1660 O O   . PHE   A 1 224 ? 8.246   -6.993  -27.716 1.00 15.28 ? 224 PHE   A O   1 
ATOM   1661 C CB  . PHE   A 1 224 ? 8.194   -9.356  -25.769 1.00 16.09 ? 224 PHE   A CB  1 
ATOM   1662 C CG  . PHE   A 1 224 ? 8.794   -10.599 -25.190 1.00 15.35 ? 224 PHE   A CG  1 
ATOM   1663 C CD1 . PHE   A 1 224 ? 8.004   -11.696 -24.872 1.00 17.06 ? 224 PHE   A CD1 1 
ATOM   1664 C CD2 . PHE   A 1 224 ? 10.149  -10.670 -24.928 1.00 18.65 ? 224 PHE   A CD2 1 
ATOM   1665 C CE1 . PHE   A 1 224 ? 8.551   -12.822 -24.329 1.00 19.83 ? 224 PHE   A CE1 1 
ATOM   1666 C CE2 . PHE   A 1 224 ? 10.715  -11.819 -24.372 1.00 21.49 ? 224 PHE   A CE2 1 
ATOM   1667 C CZ  . PHE   A 1 224 ? 9.912   -12.884 -24.085 1.00 22.65 ? 224 PHE   A CZ  1 
ATOM   1668 N N   . CYS   A 1 225 ? 6.225   -7.953  -27.742 1.00 14.82 ? 225 CYS   A N   1 
ATOM   1669 C CA  . CYS   A 1 225 ? 5.499   -6.703  -27.640 1.00 14.99 ? 225 CYS   A CA  1 
ATOM   1670 C C   . CYS   A 1 225 ? 4.828   -6.668  -26.277 1.00 15.34 ? 225 CYS   A C   1 
ATOM   1671 O O   . CYS   A 1 225 ? 4.481   -7.712  -25.722 1.00 14.88 ? 225 CYS   A O   1 
ATOM   1672 C CB  . CYS   A 1 225 ? 4.447   -6.585  -28.744 1.00 16.54 ? 225 CYS   A CB  1 
ATOM   1673 S SG  . CYS   A 1 225 ? 3.285   -7.958  -28.802 1.00 18.88 ? 225 CYS   A SG  1 
ATOM   1674 N N   . ALA   A 1 226 ? 4.595   -5.463  -25.766 1.00 15.35 ? 226 ALA   A N   1 
ATOM   1675 C CA  . ALA   A 1 226 ? 3.957   -5.265  -24.470 1.00 15.61 ? 226 ALA   A CA  1 
ATOM   1676 C C   . ALA   A 1 226 ? 3.258   -3.922  -24.489 1.00 14.58 ? 226 ALA   A C   1 
ATOM   1677 O O   . ALA   A 1 226 ? 3.785   -2.949  -25.016 1.00 16.20 ? 226 ALA   A O   1 
ATOM   1678 C CB  . ALA   A 1 226 ? 4.939   -5.370  -23.283 1.00 16.11 ? 226 ALA   A CB  1 
ATOM   1679 N N   . ARG   A 1 227 ? 2.090   -3.877  -23.885 1.00 14.74 ? 227 ARG   A N   1 
ATOM   1680 C CA  A ARG   A 1 227 ? 1.316   -2.650  -23.882 0.67 15.45 ? 227 ARG   A CA  1 
ATOM   1681 C CA  B ARG   A 1 227 ? 1.293   -2.660  -23.850 0.33 16.13 ? 227 ARG   A CA  1 
ATOM   1682 C C   . ARG   A 1 227 ? 1.908   -1.616  -22.911 1.00 15.83 ? 227 ARG   A C   1 
ATOM   1683 O O   . ARG   A 1 227 ? 2.546   -1.950  -21.914 1.00 18.64 ? 227 ARG   A O   1 
ATOM   1684 C CB  A ARG   A 1 227 ? -0.129  -3.002  -23.493 0.67 17.44 ? 227 ARG   A CB  1 
ATOM   1685 C CB  B ARG   A 1 227 ? -0.081  -3.028  -23.298 0.33 18.19 ? 227 ARG   A CB  1 
ATOM   1686 C CG  A ARG   A 1 227 ? -1.173  -1.967  -23.811 0.67 16.95 ? 227 ARG   A CG  1 
ATOM   1687 C CG  B ARG   A 1 227 ? -1.028  -3.551  -24.326 0.33 17.86 ? 227 ARG   A CG  1 
ATOM   1688 C CD  A ARG   A 1 227 ? -2.582  -2.536  -23.663 0.67 18.41 ? 227 ARG   A CD  1 
ATOM   1689 C CD  B ARG   A 1 227 ? -2.461  -3.165  -24.006 0.33 16.33 ? 227 ARG   A CD  1 
ATOM   1690 N NE  A ARG   A 1 227 ? -2.927  -2.681  -22.248 0.67 17.79 ? 227 ARG   A NE  1 
ATOM   1691 N NE  B ARG   A 1 227 ? -2.717  -3.069  -22.571 0.33 16.06 ? 227 ARG   A NE  1 
ATOM   1692 C CZ  A ARG   A 1 227 ? -4.165  -2.651  -21.766 0.67 18.68 ? 227 ARG   A CZ  1 
ATOM   1693 C CZ  B ARG   A 1 227 ? -3.924  -3.006  -22.028 0.33 17.68 ? 227 ARG   A CZ  1 
ATOM   1694 N NH1 A ARG   A 1 227 ? -5.218  -2.625  -22.573 0.67 19.23 ? 227 ARG   A NH1 1 
ATOM   1695 N NH1 B ARG   A 1 227 ? -5.016  -2.975  -22.778 0.33 16.16 ? 227 ARG   A NH1 1 
ATOM   1696 N NH2 A ARG   A 1 227 ? -4.349  -2.637  -20.440 0.67 17.26 ? 227 ARG   A NH2 1 
ATOM   1697 N NH2 B ARG   A 1 227 ? -4.036  -2.929  -20.701 0.33 19.57 ? 227 ARG   A NH2 1 
ATOM   1698 N N   . GLY   A 1 228 ? 1.673   -0.343  -23.210 1.00 16.77 ? 228 GLY   A N   1 
ATOM   1699 C CA  . GLY   A 1 228 ? 2.028   0.716   -22.280 1.00 19.16 ? 228 GLY   A CA  1 
ATOM   1700 C C   . GLY   A 1 228 ? 1.113   1.898   -22.469 1.00 20.27 ? 228 GLY   A C   1 
ATOM   1701 O O   . GLY   A 1 228 ? 0.277   1.918   -23.371 1.00 18.72 ? 228 GLY   A O   1 
ATOM   1702 N N   . CYS   A 1 229 ? 1.249   2.881   -21.571 1.00 23.28 ? 229 CYS   A N   1 
ATOM   1703 C CA  . CYS   A 1 229 ? 0.440   4.087   -21.670 1.00 33.00 ? 229 CYS   A CA  1 
ATOM   1704 C C   . CYS   A 1 229 ? 0.963   5.103   -20.662 1.00 25.54 ? 229 CYS   A C   1 
ATOM   1705 O O   . CYS   A 1 229 ? 1.282   4.742   -19.524 1.00 24.00 ? 229 CYS   A O   1 
ATOM   1706 C CB  . CYS   A 1 229 ? -1.036  3.718   -21.443 1.00 54.32 ? 229 CYS   A CB  1 
ATOM   1707 S SG  . CYS   A 1 229 ? -2.152  4.991   -20.822 1.00 77.19 ? 229 CYS   A SG  1 
ATOM   1708 N N   . TYR   A 1 230 ? 1.131   6.346   -21.097 1.00 23.53 ? 230 TYR   A N   1 
ATOM   1709 C CA  . TYR   A 1 230 ? 1.598   7.402   -20.208 1.00 22.77 ? 230 TYR   A CA  1 
ATOM   1710 C C   . TYR   A 1 230 ? 0.816   7.452   -18.894 1.00 21.00 ? 230 TYR   A C   1 
ATOM   1711 O O   . TYR   A 1 230 ? -0.417  7.517   -18.882 1.00 21.24 ? 230 TYR   A O   1 
ATOM   1712 C CB  . TYR   A 1 230 ? 1.622   8.787   -20.903 1.00 22.36 ? 230 TYR   A CB  1 
ATOM   1713 C CG  . TYR   A 1 230 ? 2.240   9.838   -19.998 1.00 23.51 ? 230 TYR   A CG  1 
ATOM   1714 C CD1 . TYR   A 1 230 ? 3.601   10.051  -19.979 1.00 25.30 ? 230 TYR   A CD1 1 
ATOM   1715 C CD2 . TYR   A 1 230 ? 1.441   10.625  -19.179 1.00 25.39 ? 230 TYR   A CD2 1 
ATOM   1716 C CE1 . TYR   A 1 230 ? 4.166   10.989  -19.153 1.00 26.44 ? 230 TYR   A CE1 1 
ATOM   1717 C CE2 . TYR   A 1 230 ? 1.991   11.583  -18.352 1.00 26.46 ? 230 TYR   A CE2 1 
ATOM   1718 C CZ  . TYR   A 1 230 ? 3.352   11.771  -18.352 1.00 28.47 ? 230 TYR   A CZ  1 
ATOM   1719 O OH  . TYR   A 1 230 ? 3.913   12.730  -17.524 1.00 32.21 ? 230 TYR   A OH  1 
ATOM   1720 N N   . GLY   A 1 231 ? 1.551   7.385   -17.780 1.00 19.55 ? 231 GLY   A N   1 
ATOM   1721 C CA  . GLY   A 1 231 ? 0.926   7.458   -16.480 1.00 21.80 ? 231 GLY   A CA  1 
ATOM   1722 C C   . GLY   A 1 231 ? 0.150   6.229   -16.082 1.00 24.06 ? 231 GLY   A C   1 
ATOM   1723 O O   . GLY   A 1 231 ? -0.532  6.256   -15.051 1.00 25.28 ? 231 GLY   A O   1 
ATOM   1724 N N   . CYS   A 1 232 ? 0.229   5.146   -16.861 1.00 23.88 ? 232 CYS   A N   1 
ATOM   1725 C CA  . CYS   A 1 232 ? -0.553  3.969   -16.502 1.00 30.63 ? 232 CYS   A CA  1 
ATOM   1726 C C   . CYS   A 1 232 ? 0.367   2.786   -16.260 1.00 24.45 ? 232 CYS   A C   1 
ATOM   1727 O O   . CYS   A 1 232 ? 1.517   2.969   -15.846 1.00 24.36 ? 232 CYS   A O   1 
ATOM   1728 C CB  . CYS   A 1 232 ? -1.658  3.705   -17.515 1.00 44.44 ? 232 CYS   A CB  1 
ATOM   1729 S SG  . CYS   A 1 232 ? -2.963  4.980   -17.342 1.00 57.65 ? 232 CYS   A SG  1 
ATOM   1730 N N   . ILE   A 1 233 ? -0.095  1.569   -16.498 1.00 20.48 ? 233 ILE   A N   1 
ATOM   1731 C CA  . ILE   A 1 233 ? 0.665   0.382   -16.101 1.00 18.56 ? 233 ILE   A CA  1 
ATOM   1732 C C   . ILE   A 1 233 ? 1.492   -0.054  -17.303 1.00 20.20 ? 233 ILE   A C   1 
ATOM   1733 O O   . ILE   A 1 233 ? 1.067   -0.902  -18.094 1.00 21.07 ? 233 ILE   A O   1 
ATOM   1734 C CB  . ILE   A 1 233 ? -0.224  -0.758  -15.602 1.00 19.36 ? 233 ILE   A CB  1 
ATOM   1735 C CG1 . ILE   A 1 233 ? -1.288  -0.287  -14.608 1.00 20.30 ? 233 ILE   A CG1 1 
ATOM   1736 C CG2 . ILE   A 1 233 ? 0.659   -1.898  -15.018 1.00 20.95 ? 233 ILE   A CG2 1 
ATOM   1737 C CD1 . ILE   A 1 233 ? -0.763  0.147   -13.243 1.00 21.81 ? 233 ILE   A CD1 1 
ATOM   1738 N N   . HIS   A 1 234 ? 2.717   0.461   -17.414 1.00 16.73 ? 234 HIS   A N   1 
ATOM   1739 C CA  . HIS   A 1 234 ? 3.556   0.015   -18.520 1.00 14.67 ? 234 HIS   A CA  1 
ATOM   1740 C C   . HIS   A 1 234 ? 3.877   -1.462  -18.373 1.00 13.98 ? 234 HIS   A C   1 
ATOM   1741 O O   . HIS   A 1 234 ? 4.160   -1.950  -17.273 1.00 14.65 ? 234 HIS   A O   1 
ATOM   1742 C CB  . HIS   A 1 234 ? 4.857   0.803   -18.551 1.00 13.63 ? 234 HIS   A CB  1 
ATOM   1743 C CG  . HIS   A 1 234 ? 4.663   2.237   -18.929 1.00 13.39 ? 234 HIS   A CG  1 
ATOM   1744 N ND1 . HIS   A 1 234 ? 4.506   2.635   -20.239 1.00 15.50 ? 234 HIS   A ND1 1 
ATOM   1745 C CD2 . HIS   A 1 234 ? 4.590   3.358   -18.169 1.00 14.98 ? 234 HIS   A CD2 1 
ATOM   1746 C CE1 . HIS   A 1 234 ? 4.349   3.946   -20.277 1.00 16.37 ? 234 HIS   A CE1 1 
ATOM   1747 N NE2 . HIS   A 1 234 ? 4.413   4.412   -19.034 1.00 16.02 ? 234 HIS   A NE2 1 
ATOM   1748 N N   . PHE   A 1 235 ? 3.831   -2.172  -19.498 1.00 13.85 ? 235 PHE   A N   1 
ATOM   1749 C CA  . PHE   A 1 235 ? 4.199   -3.596  -19.533 1.00 13.98 ? 235 PHE   A CA  1 
ATOM   1750 C C   . PHE   A 1 235 ? 3.163   -4.458  -18.815 1.00 14.92 ? 235 PHE   A C   1 
ATOM   1751 O O   . PHE   A 1 235 ? 3.509   -5.497  -18.249 1.00 14.71 ? 235 PHE   A O   1 
ATOM   1752 C CB  . PHE   A 1 235 ? 5.649   -3.882  -19.002 1.00 13.30 ? 235 PHE   A CB  1 
ATOM   1753 C CG  . PHE   A 1 235 ? 6.690   -2.937  -19.578 1.00 12.71 ? 235 PHE   A CG  1 
ATOM   1754 C CD1 . PHE   A 1 235 ? 7.125   -3.076  -20.872 1.00 14.50 ? 235 PHE   A CD1 1 
ATOM   1755 C CD2 . PHE   A 1 235 ? 7.198   -1.903  -18.812 1.00 13.39 ? 235 PHE   A CD2 1 
ATOM   1756 C CE1 . PHE   A 1 235 ? 8.057   -2.185  -21.440 1.00 15.52 ? 235 PHE   A CE1 1 
ATOM   1757 C CE2 . PHE   A 1 235 ? 8.157   -0.993  -19.359 1.00 14.39 ? 235 PHE   A CE2 1 
ATOM   1758 C CZ  . PHE   A 1 235 ? 8.565   -1.121  -20.672 1.00 14.81 ? 235 PHE   A CZ  1 
ATOM   1759 N N   . ASP   A 1 236 ? 1.894   -4.062  -18.818 1.00 15.12 ? 236 ASP   A N   1 
ATOM   1760 C CA  . ASP   A 1 236 ? 0.853   -4.844  -18.085 1.00 15.95 ? 236 ASP   A CA  1 
ATOM   1761 C C   . ASP   A 1 236 ? 0.552   -6.169  -18.798 1.00 16.19 ? 236 ASP   A C   1 
ATOM   1762 O O   . ASP   A 1 236 ? 0.473   -7.168  -18.121 1.00 18.18 ? 236 ASP   A O   1 
ATOM   1763 C CB  . ASP   A 1 236 ? -0.408  -4.009  -17.833 1.00 15.57 ? 236 ASP   A CB  1 
ATOM   1764 C CG  . ASP   A 1 236 ? -1.049  -3.294  -19.015 1.00 16.67 ? 236 ASP   A CG  1 
ATOM   1765 O OD1 . ASP   A 1 236 ? -0.539  -3.385  -20.140 1.00 17.16 ? 236 ASP   A OD1 1 
ATOM   1766 O OD2 . ASP   A 1 236 ? -2.073  -2.640  -18.786 1.00 18.75 ? 236 ASP   A OD2 1 
ATOM   1767 N N   . TYR   A 1 237 ? 0.422   -6.141  -20.113 1.00 15.41 ? 237 TYR   A N   1 
ATOM   1768 C CA  . TYR   A 1 237 ? 0.128   -7.309  -20.939 1.00 15.13 ? 237 TYR   A CA  1 
ATOM   1769 C C   . TYR   A 1 237 ? 1.216   -7.473  -21.985 1.00 14.36 ? 237 TYR   A C   1 
ATOM   1770 O O   . TYR   A 1 237 ? 1.635   -6.491  -22.600 1.00 15.60 ? 237 TYR   A O   1 
ATOM   1771 C CB  . TYR   A 1 237 ? -1.261  -7.184  -21.591 1.00 17.31 ? 237 TYR   A CB  1 
ATOM   1772 C CG  . TYR   A 1 237 ? -2.340  -7.226  -20.559 1.00 18.58 ? 237 TYR   A CG  1 
ATOM   1773 C CD1 . TYR   A 1 237 ? -2.761  -8.438  -20.025 1.00 20.76 ? 237 TYR   A CD1 1 
ATOM   1774 C CD2 . TYR   A 1 237 ? -2.934  -6.061  -20.110 1.00 20.13 ? 237 TYR   A CD2 1 
ATOM   1775 C CE1 . TYR   A 1 237 ? -3.734  -8.500  -19.065 1.00 23.66 ? 237 TYR   A CE1 1 
ATOM   1776 C CE2 . TYR   A 1 237 ? -3.956  -6.117  -19.142 1.00 23.57 ? 237 TYR   A CE2 1 
ATOM   1777 C CZ  . TYR   A 1 237 ? -4.328  -7.349  -18.632 1.00 26.02 ? 237 TYR   A CZ  1 
ATOM   1778 O OH  . TYR   A 1 237 ? -5.308  -7.463  -17.671 1.00 30.70 ? 237 TYR   A OH  1 
ATOM   1779 N N   . TRP   A 1 238 ? 1.621   -8.727  -22.241 1.00 15.11 ? 238 TRP   A N   1 
ATOM   1780 C CA  . TRP   A 1 238 ? 2.710   -9.048  -23.142 1.00 13.88 ? 238 TRP   A CA  1 
ATOM   1781 C C   . TRP   A 1 238 ? 2.260   -10.091 -24.160 1.00 15.14 ? 238 TRP   A C   1 
ATOM   1782 O O   . TRP   A 1 238 ? 1.475   -10.980 -23.846 1.00 16.82 ? 238 TRP   A O   1 
ATOM   1783 C CB  . TRP   A 1 238 ? 3.865   -9.720  -22.359 1.00 15.08 ? 238 TRP   A CB  1 
ATOM   1784 C CG  . TRP   A 1 238 ? 4.604   -8.801  -21.391 1.00 13.29 ? 238 TRP   A CG  1 
ATOM   1785 C CD1 . TRP   A 1 238 ? 4.086   -8.141  -20.308 1.00 13.37 ? 238 TRP   A CD1 1 
ATOM   1786 C CD2 . TRP   A 1 238 ? 6.008   -8.464  -21.431 1.00 12.98 ? 238 TRP   A CD2 1 
ATOM   1787 N NE1 . TRP   A 1 238 ? 5.078   -7.391  -19.682 1.00 13.66 ? 238 TRP   A NE1 1 
ATOM   1788 C CE2 . TRP   A 1 238 ? 6.269   -7.594  -20.343 1.00 12.51 ? 238 TRP   A CE2 1 
ATOM   1789 C CE3 . TRP   A 1 238 ? 7.071   -8.860  -22.255 1.00 15.02 ? 238 TRP   A CE3 1 
ATOM   1790 C CZ2 . TRP   A 1 238 ? 7.546   -7.076  -20.089 1.00 14.08 ? 238 TRP   A CZ2 1 
ATOM   1791 C CZ3 . TRP   A 1 238 ? 8.341   -8.352  -22.004 1.00 14.71 ? 238 TRP   A CZ3 1 
ATOM   1792 C CH2 . TRP   A 1 238 ? 8.566   -7.485  -20.928 1.00 15.07 ? 238 TRP   A CH2 1 
ATOM   1793 N N   . GLY   A 1 239 ? 2.813   -10.018 -25.370 1.00 15.75 ? 239 GLY   A N   1 
ATOM   1794 C CA  . GLY   A 1 239 ? 2.749   -11.145 -26.276 1.00 16.51 ? 239 GLY   A CA  1 
ATOM   1795 C C   . GLY   A 1 239 ? 3.603   -12.287 -25.754 1.00 16.48 ? 239 GLY   A C   1 
ATOM   1796 O O   . GLY   A 1 239 ? 4.417   -12.113 -24.855 1.00 15.31 ? 239 GLY   A O   1 
ATOM   1797 N N   . GLN   A 1 240 ? 3.404   -13.465 -26.345 1.00 18.68 ? 240 GLN   A N   1 
ATOM   1798 C CA  A GLN   A 1 240 ? 4.164   -14.657 -25.968 0.52 18.64 ? 240 GLN   A CA  1 
ATOM   1799 C CA  B GLN   A 1 240 ? 4.186   -14.619 -25.900 0.48 19.16 ? 240 GLN   A CA  1 
ATOM   1800 C C   . GLN   A 1 240 ? 5.618   -14.611 -26.411 1.00 18.62 ? 240 GLN   A C   1 
ATOM   1801 O O   . GLN   A 1 240 ? 6.411   -15.458 -25.975 1.00 21.51 ? 240 GLN   A O   1 
ATOM   1802 C CB  A GLN   A 1 240 ? 3.513   -15.887 -26.612 0.52 21.07 ? 240 GLN   A CB  1 
ATOM   1803 C CB  B GLN   A 1 240 ? 3.518   -15.971 -26.232 0.48 23.32 ? 240 GLN   A CB  1 
ATOM   1804 C CG  A GLN   A 1 240 ? 3.109   -15.669 -28.062 0.52 28.27 ? 240 GLN   A CG  1 
ATOM   1805 C CG  B GLN   A 1 240 ? 2.921   -16.121 -27.616 0.48 28.80 ? 240 GLN   A CG  1 
ATOM   1806 C CD  A GLN   A 1 240 ? 1.647   -15.212 -28.190 0.52 26.69 ? 240 GLN   A CD  1 
ATOM   1807 C CD  B GLN   A 1 240 ? 3.817   -16.844 -28.628 0.48 27.57 ? 240 GLN   A CD  1 
ATOM   1808 O OE1 A GLN   A 1 240 ? 1.376   -14.020 -28.332 0.52 18.17 ? 240 GLN   A OE1 1 
ATOM   1809 O OE1 B GLN   A 1 240 ? 4.281   -16.235 -29.590 0.48 24.31 ? 240 GLN   A OE1 1 
ATOM   1810 N NE2 A GLN   A 1 240 ? 0.693   -16.180 -28.095 0.52 29.05 ? 240 GLN   A NE2 1 
ATOM   1811 N NE2 B GLN   A 1 240 ? 4.044   -18.146 -28.417 0.48 29.65 ? 240 GLN   A NE2 1 
ATOM   1812 N N   . GLY   A 1 241 ? 5.979   -13.681 -27.292 1.00 15.81 ? 241 GLY   A N   1 
ATOM   1813 C CA  . GLY   A 1 241 ? 7.341   -13.605 -27.807 1.00 17.94 ? 241 GLY   A CA  1 
ATOM   1814 C C   . GLY   A 1 241 ? 7.513   -14.351 -29.119 1.00 19.50 ? 241 GLY   A C   1 
ATOM   1815 O O   . GLY   A 1 241 ? 7.018   -15.474 -29.300 1.00 22.84 ? 241 GLY   A O   1 
ATOM   1816 N N   . THR   A 1 242 ? 8.209   -13.747 -30.065 1.00 18.35 ? 242 THR   A N   1 
ATOM   1817 C CA  . THR   A 1 242 ? 8.583   -14.441 -31.286 1.00 17.51 ? 242 THR   A CA  1 
ATOM   1818 C C   . THR   A 1 242 ? 10.058  -14.780 -31.203 1.00 17.56 ? 242 THR   A C   1 
ATOM   1819 O O   . THR   A 1 242 ? 10.888  -13.895 -30.965 1.00 17.21 ? 242 THR   A O   1 
ATOM   1820 C CB  . THR   A 1 242 ? 8.343   -13.563 -32.510 1.00 17.40 ? 242 THR   A CB  1 
ATOM   1821 O OG1 . THR   A 1 242 ? 6.949   -13.218 -32.572 1.00 18.60 ? 242 THR   A OG1 1 
ATOM   1822 C CG2 . THR   A 1 242 ? 8.782   -14.303 -33.803 1.00 18.62 ? 242 THR   A CG2 1 
ATOM   1823 N N   . THR   A 1 243 ? 10.389  -16.053 -31.379 1.00 16.56 ? 243 THR   A N   1 
ATOM   1824 C CA  . THR   A 1 243 ? 11.782  -16.471 -31.387 1.00 16.61 ? 243 THR   A CA  1 
ATOM   1825 C C   . THR   A 1 243 ? 12.284  -16.283 -32.803 1.00 16.14 ? 243 THR   A C   1 
ATOM   1826 O O   . THR   A 1 243 ? 11.827  -16.968 -33.721 1.00 17.79 ? 243 THR   A O   1 
ATOM   1827 C CB  . THR   A 1 243 ? 11.904  -17.912 -30.935 1.00 17.74 ? 243 THR   A CB  1 
ATOM   1828 O OG1 . THR   A 1 243 ? 11.510  -17.994 -29.564 1.00 19.38 ? 243 THR   A OG1 1 
ATOM   1829 C CG2 . THR   A 1 243 ? 13.361  -18.375 -31.075 1.00 19.90 ? 243 THR   A CG2 1 
ATOM   1830 N N   . LEU   A 1 244 ? 13.233  -15.362 -32.997 1.00 16.11 ? 244 LEU   A N   1 
ATOM   1831 C CA  . LEU   A 1 244 ? 13.849  -15.149 -34.311 1.00 16.29 ? 244 LEU   A CA  1 
ATOM   1832 C C   . LEU   A 1 244 ? 15.144  -15.954 -34.392 1.00 17.80 ? 244 LEU   A C   1 
ATOM   1833 O O   . LEU   A 1 244 ? 16.027  -15.811 -33.540 1.00 18.06 ? 244 LEU   A O   1 
ATOM   1834 C CB  . LEU   A 1 244 ? 14.218  -13.663 -34.465 1.00 15.45 ? 244 LEU   A CB  1 
ATOM   1835 C CG  . LEU   A 1 244 ? 14.985  -13.323 -35.730 1.00 17.62 ? 244 LEU   A CG  1 
ATOM   1836 C CD1 . LEU   A 1 244 ? 14.120  -13.668 -36.939 1.00 18.86 ? 244 LEU   A CD1 1 
ATOM   1837 C CD2 . LEU   A 1 244 ? 15.376  -11.825 -35.746 1.00 18.85 ? 244 LEU   A CD2 1 
ATOM   1838 N N   . THR   A 1 245 ? 15.272  -16.776 -35.422 1.00 17.36 ? 245 THR   A N   1 
ATOM   1839 C CA  . THR   A 1 245 ? 16.511  -17.491 -35.704 1.00 17.98 ? 245 THR   A CA  1 
ATOM   1840 C C   . THR   A 1 245 ? 17.063  -16.923 -36.995 1.00 18.82 ? 245 THR   A C   1 
ATOM   1841 O O   . THR   A 1 245 ? 16.357  -16.907 -38.008 1.00 19.67 ? 245 THR   A O   1 
ATOM   1842 C CB  . THR   A 1 245 ? 16.247  -18.991 -35.867 1.00 20.41 ? 245 THR   A CB  1 
ATOM   1843 O OG1 . THR   A 1 245 ? 15.662  -19.498 -34.660 1.00 22.06 ? 245 THR   A OG1 1 
ATOM   1844 C CG2 . THR   A 1 245 ? 17.555  -19.736 -36.157 1.00 21.54 ? 245 THR   A CG2 1 
ATOM   1845 N N   . VAL   A 1 246 ? 18.277  -16.417 -36.948 1.00 19.78 ? 246 VAL   A N   1 
ATOM   1846 C CA  . VAL   A 1 246 ? 18.981  -15.972 -38.146 1.00 20.85 ? 246 VAL   A CA  1 
ATOM   1847 C C   . VAL   A 1 246 ? 19.907  -17.112 -38.567 1.00 22.18 ? 246 VAL   A C   1 
ATOM   1848 O O   . VAL   A 1 246 ? 20.718  -17.593 -37.759 1.00 22.48 ? 246 VAL   A O   1 
ATOM   1849 C CB  . VAL   A 1 246 ? 19.746  -14.656 -37.912 1.00 20.99 ? 246 VAL   A CB  1 
ATOM   1850 C CG1 . VAL   A 1 246 ? 20.411  -14.227 -39.219 1.00 22.39 ? 246 VAL   A CG1 1 
ATOM   1851 C CG2 . VAL   A 1 246 ? 18.794  -13.559 -37.417 1.00 20.74 ? 246 VAL   A CG2 1 
ATOM   1852 N N   . SER   A 1 247 ? 19.728  -17.612 -39.794 1.00 23.94 ? 247 SER   A N   1 
ATOM   1853 C CA  . SER   A 1 247 ? 20.473  -18.782 -40.239 1.00 24.04 ? 247 SER   A CA  1 
ATOM   1854 C C   . SER   A 1 247 ? 21.930  -18.415 -40.497 1.00 26.88 ? 247 SER   A C   1 
ATOM   1855 O O   . SER   A 1 247 ? 22.314  -17.246 -40.553 1.00 27.15 ? 247 SER   A O   1 
ATOM   1856 C CB  . SER   A 1 247 ? 19.790  -19.436 -41.432 1.00 26.97 ? 247 SER   A CB  1 
ATOM   1857 O OG  . SER   A 1 247 ? 19.758  -18.544 -42.528 1.00 30.49 ? 247 SER   A OG  1 
ATOM   1858 N N   . SER   A 1 248 ? 22.757  -19.437 -40.633 1.00 30.16 ? 248 SER   A N   1 
ATOM   1859 C CA  . SER   A 1 248 ? 24.180  -19.185 -40.766 1.00 38.55 ? 248 SER   A CA  1 
ATOM   1860 C C   . SER   A 1 248 ? 24.545  -19.130 -42.244 1.00 51.30 ? 248 SER   A C   1 
ATOM   1861 O O   . SER   A 1 248 ? 24.953  -18.070 -42.733 1.00 53.60 ? 248 SER   A O   1 
ATOM   1862 C CB  . SER   A 1 248 ? 24.988  -20.222 -39.969 1.00 37.51 ? 248 SER   A CB  1 
ATOM   1863 O OG  . SER   A 1 248 ? 24.684  -20.103 -38.582 1.00 34.91 ? 248 SER   A OG  1 
ATOM   1864 O OXT . SER   A 1 248 ? 24.391  -20.109 -42.987 1.00 59.03 ? 248 SER   A OXT 1 
HETATM 1865 C C10 . A1LZO B 2 .   ? 5.510   7.550   -17.501 1.00 19.00 ? 401 A1LZO A C10 1 
HETATM 1866 N N12 . A1LZO B 2 .   ? 5.496   8.528   -16.590 1.00 20.34 ? 401 A1LZO A N12 1 
HETATM 1867 C C01 . A1LZO B 2 .   ? 7.283   9.377   -20.988 1.00 20.05 ? 401 A1LZO A C01 1 
HETATM 1868 C C02 . A1LZO B 2 .   ? 7.509   8.497   -22.078 1.00 18.85 ? 401 A1LZO A C02 1 
HETATM 1869 C C03 . A1LZO B 2 .   ? 7.541   7.086   -21.770 1.00 17.50 ? 401 A1LZO A C03 1 
HETATM 1870 C C04 . A1LZO B 2 .   ? 7.309   6.612   -20.474 1.00 18.78 ? 401 A1LZO A C04 1 
HETATM 1871 C C05 . A1LZO B 2 .   ? 7.104   7.487   -19.411 1.00 19.20 ? 401 A1LZO A C05 1 
HETATM 1872 C C06 . A1LZO B 2 .   ? 7.088   8.884   -19.694 1.00 19.66 ? 401 A1LZO A C06 1 
HETATM 1873 C C08 . A1LZO B 2 .   ? 4.568   10.073  -14.876 1.00 25.71 ? 401 A1LZO A C08 1 
HETATM 1874 C C09 . A1LZO B 2 .   ? 6.852   6.975   -17.993 1.00 18.42 ? 401 A1LZO A C09 1 
HETATM 1875 C C18 . A1LZO B 2 .   ? 4.257   9.082   -16.068 1.00 21.67 ? 401 A1LZO A C18 1 
HETATM 1876 N N11 . A1LZO B 2 .   ? 7.825   6.050   -22.914 1.00 18.71 ? 401 A1LZO A N11 1 
HETATM 1877 O O07 . A1LZO B 2 .   ? 7.686   8.941   -23.352 1.00 20.95 ? 401 A1LZO A O07 1 
HETATM 1878 O O13 . A1LZO B 2 .   ? 5.761   10.323  -14.646 1.00 29.39 ? 401 A1LZO A O13 1 
HETATM 1879 O O14 . A1LZO B 2 .   ? 3.580   10.512  -14.307 1.00 28.29 ? 401 A1LZO A O14 1 
HETATM 1880 O O15 . A1LZO B 2 .   ? 7.722   4.867   -22.531 1.00 19.51 ? 401 A1LZO A O15 1 
HETATM 1881 O O16 . A1LZO B 2 .   ? 8.164   6.421   -24.046 1.00 23.64 ? 401 A1LZO A O16 1 
HETATM 1882 O O17 . A1LZO B 2 .   ? 4.475   7.044   -17.943 1.00 18.82 ? 401 A1LZO A O17 1 
HETATM 1883 O O   . HOH   C 3 .   ? 14.995  3.334   -36.278 1.00 35.36 ? 501 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 0.599   -23.844 0.121   1.00 25.30 ? 502 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 23.153  2.906   -25.544 1.00 30.41 ? 503 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 22.373  -15.706 -24.856 1.00 42.46 ? 504 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 0.740   -22.026 -2.061  1.00 24.71 ? 505 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -5.071  7.443   -34.737 1.00 30.34 ? 506 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 24.882  -6.789  -29.703 1.00 32.83 ? 507 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 23.780  10.166  -7.531  1.00 29.68 ? 508 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 11.349  -22.717 -11.276 1.00 45.76 ? 509 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 1.092   10.087  -14.194 1.00 43.64 ? 510 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 17.866  1.109   -22.473 1.00 37.31 ? 511 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -7.456  -0.425  -33.986 1.00 39.81 ? 512 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 5.691   -24.585 -2.614  1.00 29.17 ? 513 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 22.359  -16.407 -34.184 1.00 32.57 ? 514 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -0.330  -9.586  -17.912 1.00 42.34 ? 515 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 17.903  -5.065  -44.386 1.00 40.49 ? 516 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -4.105  -15.497 -7.024  1.00 32.90 ? 517 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 14.052  14.236  -17.437 1.00 37.56 ? 518 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 6.194   -12.153 -37.933 1.00 34.56 ? 519 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 4.644   -19.896 6.096   1.00 18.23 ? 520 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -1.133  -1.791  -27.409 1.00 26.23 ? 521 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 22.452  -8.462  -7.609  1.00 37.19 ? 522 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -3.913  0.249   -10.530 1.00 35.62 ? 523 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -1.028  -22.847 -4.736  1.00 47.72 ? 524 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -5.552  -3.303  -42.384 1.00 44.36 ? 525 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -7.296  -8.793  -19.399 1.00 42.50 ? 526 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 11.128  -7.397  -43.562 1.00 37.81 ? 527 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -4.956  -10.677 -30.135 1.00 28.42 ? 528 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 8.170   9.684   -15.564 1.00 21.57 ? 529 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 23.325  -17.559 -37.219 1.00 31.62 ? 530 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -3.616  -2.980  -16.638 1.00 31.68 ? 531 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 20.868  1.934   -24.580 1.00 35.52 ? 532 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 17.268  7.066   -10.537 1.00 27.24 ? 533 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -2.883  -11.642 -22.265 1.00 41.79 ? 534 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -7.717  6.855   -32.209 1.00 33.82 ? 535 HOH   A O   1 
HETATM 1918 O O   A HOH   C 3 .   ? 15.827  -18.874 -6.273  0.82 24.96 ? 536 HOH   A O   1 
HETATM 1919 O O   B HOH   C 3 .   ? 15.721  -19.017 -5.001  0.18 24.98 ? 536 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 12.630  -19.443 -27.613 1.00 33.68 ? 537 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -9.461  5.604   -30.307 1.00 34.36 ? 538 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 11.775  -8.392  4.007   1.00 35.51 ? 539 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -1.486  -0.087  -29.480 1.00 28.75 ? 540 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 12.978  -19.383 -34.625 1.00 25.01 ? 541 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 0.867   -16.743 -13.660 1.00 25.84 ? 542 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 10.428  -25.033 -5.834  1.00 40.04 ? 543 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 3.356   -10.050 6.592   1.00 36.95 ? 544 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 20.445  7.653   -29.886 1.00 33.85 ? 545 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? 0.943   -1.583  -4.668  1.00 25.69 ? 546 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 14.213  -1.623  -39.649 1.00 25.39 ? 547 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 5.217   2.039   -14.922 1.00 15.74 ? 548 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -7.684  -2.442  -21.467 1.00 28.88 ? 549 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -2.040  8.623   -20.753 1.00 35.90 ? 550 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 17.610  -7.934  -17.602 1.00 25.71 ? 551 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 4.989   -13.480 -22.580 1.00 22.07 ? 552 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 8.716   -18.309 -29.244 1.00 31.37 ? 553 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -0.934  5.981   -36.240 1.00 41.74 ? 554 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 10.600  5.172   -37.643 1.00 28.88 ? 555 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 2.043   6.534   -9.347  1.00 28.40 ? 556 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -0.662  -6.896  -0.081  1.00 23.21 ? 557 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 2.013   -15.767 -9.496  1.00 15.88 ? 558 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 3.149   9.733   -27.658 1.00 22.99 ? 559 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 14.518  7.209   -27.027 1.00 35.45 ? 560 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 14.867  -14.858 -17.643 1.00 37.08 ? 561 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? 22.341  -0.352  -9.646  1.00 32.75 ? 562 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? 14.174  -7.737  -7.118  1.00 16.80 ? 563 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 23.404  -5.145  -37.769 1.00 43.83 ? 564 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 14.294  -17.990 3.207   1.00 15.15 ? 565 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -2.186  5.732   -27.617 1.00 21.69 ? 566 HOH   A O   1 
HETATM 1950 O O   A HOH   C 3 .   ? -1.501  9.980   -27.101 0.67 35.44 ? 567 HOH   A O   1 
HETATM 1951 O O   B HOH   C 3 .   ? -2.461  10.987  -28.211 0.33 35.87 ? 567 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? 7.045   -4.073  2.322   1.00 24.13 ? 568 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 7.880   -4.341  -40.585 1.00 36.72 ? 569 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? -3.621  -5.577  -15.583 1.00 41.92 ? 570 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -3.320  2.628   -39.222 1.00 31.01 ? 571 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? 18.860  -13.986 -11.477 1.00 26.03 ? 572 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 2.102   -7.133  -0.409  1.00 17.10 ? 573 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? 5.552   -26.995 -3.632  1.00 34.12 ? 574 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? 7.978   -14.010 6.230   1.00 29.10 ? 575 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 6.297   -10.610 -33.184 1.00 22.79 ? 576 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? 6.339   -3.017  -1.538  1.00 23.87 ? 577 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? 17.524  -3.211  -19.945 1.00 17.48 ? 578 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? 13.893  8.458   -3.889  1.00 26.24 ? 579 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? 19.737  -9.878  -10.786 1.00 20.66 ? 580 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 5.223   -1.368  -33.583 1.00 17.08 ? 581 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? 3.550   -7.070  4.148   1.00 31.13 ? 582 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? 2.278   -0.318  -1.723  1.00 45.53 ? 583 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? -1.191  -11.487 -24.379 1.00 26.37 ? 584 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? -2.705  -9.214  -37.722 1.00 36.88 ? 585 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? -6.914  7.268   -38.279 1.00 26.33 ? 586 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? -2.271  -17.295 -8.149  1.00 32.01 ? 587 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? 18.869  -10.588 -16.707 1.00 33.59 ? 588 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? -9.897  -3.854  -22.076 1.00 42.02 ? 589 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? -1.472  -14.940 -0.168  1.00 15.92 ? 590 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? 17.451  1.506   1.857   1.00 42.18 ? 591 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? 10.874  -18.352 -19.431 1.00 40.43 ? 592 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? 13.316  -12.406 -44.294 1.00 33.48 ? 593 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? 13.602  13.148  -13.048 1.00 35.96 ? 594 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? 0.697   -10.644 -20.181 1.00 20.04 ? 595 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? 10.839  -20.315 4.871   1.00 26.36 ? 596 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? -1.242  -7.321  -15.820 1.00 29.34 ? 597 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? 5.193   -20.857 -10.845 1.00 18.06 ? 598 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? 13.983  -4.809  -46.410 1.00 40.24 ? 599 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? 16.628  -1.504  -21.913 1.00 18.99 ? 600 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? 20.141  -7.628  -28.024 1.00 41.15 ? 601 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? 10.424  -18.368 -14.902 1.00 27.09 ? 602 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? 26.844  -10.917 -26.307 1.00 37.16 ? 603 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? 12.578  -24.746 -7.790  1.00 43.33 ? 604 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? -6.092  -12.777 -4.263  1.00 28.17 ? 605 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? 18.469  4.785   -25.384 1.00 28.50 ? 606 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? 7.975   4.146   -38.658 1.00 25.58 ? 607 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? 6.028   4.702   -3.872  1.00 32.09 ? 608 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? 18.601  2.919   -5.653  1.00 20.24 ? 609 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? 13.010  5.034   -3.599  1.00 31.06 ? 610 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? 0.623   -11.305 -34.985 1.00 35.31 ? 611 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? 2.453   -0.668  -40.769 1.00 39.22 ? 612 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? 4.121   -14.014 6.247   1.00 22.12 ? 613 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? 16.389  -22.634 -2.446  1.00 29.14 ? 614 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? 16.726  -19.987 -32.087 1.00 31.72 ? 615 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? 12.850  9.606   -15.535 1.00 30.93 ? 616 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? 8.047   -0.363  -6.702  1.00 16.23 ? 617 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? 17.351  -13.279 -13.709 1.00 26.37 ? 618 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? -1.880  -2.835  -0.946  1.00 37.55 ? 619 HOH   A O   1 
HETATM 2004 O O   . HOH   C 3 .   ? 16.927  -12.629 -19.211 1.00 40.15 ? 620 HOH   A O   1 
HETATM 2005 O O   . HOH   C 3 .   ? 1.607   1.631   -40.894 1.00 38.17 ? 621 HOH   A O   1 
HETATM 2006 O O   . HOH   C 3 .   ? 18.020  -1.411  -24.759 1.00 29.30 ? 622 HOH   A O   1 
HETATM 2007 O O   . HOH   C 3 .   ? 18.125  -10.235 -26.861 1.00 27.64 ? 623 HOH   A O   1 
HETATM 2008 O O   . HOH   C 3 .   ? 8.065   9.811   -34.013 1.00 31.46 ? 624 HOH   A O   1 
HETATM 2009 O O   . HOH   C 3 .   ? 4.892   11.024  -25.768 1.00 40.90 ? 625 HOH   A O   1 
HETATM 2010 O O   . HOH   C 3 .   ? 15.445  -14.185 -45.095 1.00 29.40 ? 626 HOH   A O   1 
HETATM 2011 O O   . HOH   C 3 .   ? 25.924  -12.757 -39.187 1.00 35.87 ? 627 HOH   A O   1 
HETATM 2012 O O   . HOH   C 3 .   ? 7.353   -2.003  -39.103 1.00 25.62 ? 628 HOH   A O   1 
HETATM 2013 O O   . HOH   C 3 .   ? 5.952   11.192  -23.767 1.00 42.03 ? 629 HOH   A O   1 
HETATM 2014 O O   . HOH   C 3 .   ? 20.312  -2.781  -15.770 1.00 22.02 ? 630 HOH   A O   1 
HETATM 2015 O O   . HOH   C 3 .   ? -5.287  -2.066  -6.236  1.00 39.87 ? 631 HOH   A O   1 
HETATM 2016 O O   . HOH   C 3 .   ? 9.323   -11.091 -42.458 1.00 31.63 ? 632 HOH   A O   1 
HETATM 2017 O O   . HOH   C 3 .   ? 11.869  9.806   -30.318 1.00 34.93 ? 633 HOH   A O   1 
HETATM 2018 O O   . HOH   C 3 .   ? -5.469  -27.322 -2.136  1.00 33.40 ? 634 HOH   A O   1 
HETATM 2019 O O   . HOH   C 3 .   ? 8.269   -20.973 -12.360 1.00 29.29 ? 635 HOH   A O   1 
HETATM 2020 O O   . HOH   C 3 .   ? 24.657  -19.339 -45.762 1.00 44.71 ? 636 HOH   A O   1 
HETATM 2021 O O   . HOH   C 3 .   ? -1.260  3.800   -38.587 1.00 42.71 ? 637 HOH   A O   1 
HETATM 2022 O O   . HOH   C 3 .   ? 20.618  0.006   -33.998 1.00 38.50 ? 638 HOH   A O   1 
HETATM 2023 O O   . HOH   C 3 .   ? 14.845  0.013   0.890   1.00 41.65 ? 639 HOH   A O   1 
HETATM 2024 O O   . HOH   C 3 .   ? -9.636  3.076   -24.409 1.00 39.56 ? 640 HOH   A O   1 
HETATM 2025 O O   . HOH   C 3 .   ? 3.672   7.206   -36.729 1.00 48.99 ? 641 HOH   A O   1 
HETATM 2026 O O   . HOH   C 3 .   ? 12.455  13.076  -25.202 1.00 39.12 ? 642 HOH   A O   1 
HETATM 2027 O O   . HOH   C 3 .   ? -9.581  0.016   -24.069 1.00 29.85 ? 643 HOH   A O   1 
HETATM 2028 O O   . HOH   C 3 .   ? 9.802   -18.238 -40.630 1.00 35.85 ? 644 HOH   A O   1 
HETATM 2029 O O   . HOH   C 3 .   ? 0.460   14.091  -33.989 1.00 36.89 ? 645 HOH   A O   1 
HETATM 2030 O O   . HOH   C 3 .   ? 21.788  -3.780  -21.721 1.00 44.29 ? 646 HOH   A O   1 
HETATM 2031 O O   . HOH   C 3 .   ? 23.006  -7.020  -35.401 1.00 49.39 ? 647 HOH   A O   1 
HETATM 2032 O O   . HOH   C 3 .   ? 0.516   3.507   -13.151 1.00 30.25 ? 648 HOH   A O   1 
HETATM 2033 O O   . HOH   C 3 .   ? -5.696  -3.313  -8.810  1.00 37.82 ? 649 HOH   A O   1 
HETATM 2034 O O   . HOH   C 3 .   ? 22.429  -14.507 -46.728 1.00 46.11 ? 650 HOH   A O   1 
HETATM 2035 O O   . HOH   C 3 .   ? 17.569  -20.009 -43.829 1.00 45.11 ? 651 HOH   A O   1 
HETATM 2036 O O   . HOH   C 3 .   ? 2.652   3.378   -38.392 1.00 24.97 ? 652 HOH   A O   1 
HETATM 2037 O O   . HOH   C 3 .   ? 14.022  7.811   -30.857 1.00 25.78 ? 653 HOH   A O   1 
HETATM 2038 O O   . HOH   C 3 .   ? 18.207  -8.588  -29.691 1.00 35.55 ? 654 HOH   A O   1 
HETATM 2039 O O   . HOH   C 3 .   ? 12.492  6.181   -1.303  1.00 32.06 ? 655 HOH   A O   1 
HETATM 2040 O O   . HOH   C 3 .   ? 16.220  -21.197 -9.905  1.00 51.34 ? 656 HOH   A O   1 
HETATM 2041 O O   . HOH   C 3 .   ? -2.893  -0.214  -6.347  1.00 28.11 ? 657 HOH   A O   1 
HETATM 2042 O O   . HOH   C 3 .   ? 20.197  -7.220  -11.366 1.00 19.40 ? 658 HOH   A O   1 
HETATM 2043 O O   . HOH   C 3 .   ? 0.462   -13.594 -12.188 1.00 41.77 ? 659 HOH   A O   1 
HETATM 2044 O O   . HOH   C 3 .   ? 16.802  -15.640 -26.638 1.00 34.76 ? 660 HOH   A O   1 
HETATM 2045 O O   . HOH   C 3 .   ? 21.014  -16.147 -11.589 1.00 47.35 ? 661 HOH   A O   1 
HETATM 2046 O O   . HOH   C 3 .   ? 3.857   -14.608 -15.552 1.00 25.11 ? 662 HOH   A O   1 
HETATM 2047 O O   . HOH   C 3 .   ? -4.424  9.302   -27.197 1.00 27.43 ? 663 HOH   A O   1 
HETATM 2048 O O   . HOH   C 3 .   ? 2.730   -19.365 -33.923 1.00 35.98 ? 664 HOH   A O   1 
HETATM 2049 O O   . HOH   C 3 .   ? 18.613  -9.007  -24.638 1.00 28.05 ? 665 HOH   A O   1 
HETATM 2050 O O   . HOH   C 3 .   ? 1.787   -13.631 -22.518 1.00 35.47 ? 666 HOH   A O   1 
HETATM 2051 O O   . HOH   C 3 .   ? 3.478   -3.963  -15.177 1.00 20.73 ? 667 HOH   A O   1 
HETATM 2052 O O   . HOH   C 3 .   ? 0.189   6.892   -10.551 1.00 42.38 ? 668 HOH   A O   1 
HETATM 2053 O O   . HOH   C 3 .   ? 16.915  -17.523 -31.256 1.00 25.74 ? 669 HOH   A O   1 
HETATM 2054 O O   . HOH   C 3 .   ? -6.854  -2.988  -18.839 1.00 38.11 ? 670 HOH   A O   1 
HETATM 2055 O O   A HOH   C 3 .   ? 10.059  11.816  -19.135 0.73 40.70 ? 671 HOH   A O   1 
HETATM 2056 O O   B HOH   C 3 .   ? 9.337   11.317  -17.824 0.27 40.70 ? 671 HOH   A O   1 
HETATM 2057 O O   . HOH   C 3 .   ? -2.101  0.467   -18.436 1.00 30.22 ? 672 HOH   A O   1 
HETATM 2058 O O   . HOH   C 3 .   ? 11.578  8.600   -33.932 1.00 40.22 ? 673 HOH   A O   1 
HETATM 2059 O O   . HOH   C 3 .   ? 21.300  -12.422 -11.838 1.00 47.87 ? 674 HOH   A O   1 
HETATM 2060 O O   . HOH   C 3 .   ? 10.827  12.226  -9.409  1.00 23.51 ? 675 HOH   A O   1 
HETATM 2061 O O   . HOH   C 3 .   ? 8.487   5.295   1.659   1.00 31.78 ? 676 HOH   A O   1 
HETATM 2062 O O   . HOH   C 3 .   ? 12.702  2.077   -42.164 1.00 30.28 ? 677 HOH   A O   1 
HETATM 2063 O O   . HOH   C 3 .   ? 13.304  9.384   -27.590 1.00 34.66 ? 678 HOH   A O   1 
HETATM 2064 O O   . HOH   C 3 .   ? -0.848  -0.230  -20.349 1.00 29.15 ? 679 HOH   A O   1 
HETATM 2065 O O   . HOH   C 3 .   ? 23.756  -7.841  -42.293 1.00 47.47 ? 680 HOH   A O   1 
HETATM 2066 O O   . HOH   C 3 .   ? 13.981  3.282   -38.410 1.00 36.74 ? 681 HOH   A O   1 
HETATM 2067 O O   . HOH   C 3 .   ? -9.407  -1.913  -31.288 1.00 30.90 ? 682 HOH   A O   1 
HETATM 2068 O O   . HOH   C 3 .   ? 16.908  10.101  -16.293 1.00 36.29 ? 683 HOH   A O   1 
HETATM 2069 O O   . HOH   C 3 .   ? 5.412   -19.508 -35.766 1.00 31.71 ? 684 HOH   A O   1 
HETATM 2070 O O   . HOH   C 3 .   ? 14.566  -9.212  -46.773 1.00 36.51 ? 685 HOH   A O   1 
HETATM 2071 O O   . HOH   C 3 .   ? -0.710  7.564   -23.311 1.00 29.75 ? 686 HOH   A O   1 
HETATM 2072 O O   . HOH   C 3 .   ? 8.339   -26.494 -21.496 1.00 49.40 ? 687 HOH   A O   1 
HETATM 2073 O O   . HOH   C 3 .   ? -3.849  -20.997 -5.140  1.00 44.61 ? 688 HOH   A O   1 
HETATM 2074 O O   . HOH   C 3 .   ? 21.074  -3.672  -32.482 1.00 49.73 ? 689 HOH   A O   1 
HETATM 2075 O O   . HOH   C 3 .   ? 24.055  -0.340  -31.330 1.00 47.58 ? 690 HOH   A O   1 
HETATM 2076 O O   . HOH   C 3 .   ? 23.597  9.170   -26.447 1.00 46.10 ? 691 HOH   A O   1 
HETATM 2077 O O   . HOH   C 3 .   ? 4.135   7.642   -7.928  1.00 50.23 ? 692 HOH   A O   1 
HETATM 2078 O O   . HOH   C 3 .   ? 25.498  7.698   -10.925 1.00 43.41 ? 693 HOH   A O   1 
HETATM 2079 O O   . HOH   C 3 .   ? 25.137  -23.228 -43.727 1.00 43.94 ? 694 HOH   A O   1 
HETATM 2080 O O   . HOH   C 3 .   ? 0.099   9.567   -24.790 1.00 40.47 ? 695 HOH   A O   1 
HETATM 2081 O O   . HOH   C 3 .   ? 15.034  11.707  -26.786 1.00 47.29 ? 696 HOH   A O   1 
HETATM 2082 O O   . HOH   C 3 .   ? 14.107  -17.131 -19.241 1.00 46.73 ? 697 HOH   A O   1 
HETATM 2083 O O   . HOH   C 3 .   ? 10.967  -19.822 -12.732 1.00 36.90 ? 698 HOH   A O   1 
HETATM 2084 O O   . HOH   C 3 .   ? 21.686  -1.621  -17.892 1.00 31.13 ? 699 HOH   A O   1 
HETATM 2085 O O   . HOH   C 3 .   ? 16.838  9.079   -12.536 1.00 34.35 ? 700 HOH   A O   1 
HETATM 2086 O O   . HOH   C 3 .   ? 9.739   -20.202 -38.325 1.00 38.69 ? 701 HOH   A O   1 
HETATM 2087 O O   . HOH   C 3 .   ? 11.598  11.693  -16.430 1.00 40.17 ? 702 HOH   A O   1 
HETATM 2088 O O   . HOH   C 3 .   ? 8.832   13.186  -9.854  1.00 43.36 ? 703 HOH   A O   1 
HETATM 2089 O O   . HOH   C 3 .   ? -1.065  -1.169  -2.851  1.00 39.29 ? 704 HOH   A O   1 
HETATM 2090 O O   . HOH   C 3 .   ? 16.505  -17.015 -28.832 1.00 33.51 ? 705 HOH   A O   1 
HETATM 2091 O O   . HOH   C 3 .   ? -7.761  -10.092 -7.723  1.00 47.10 ? 706 HOH   A O   1 
HETATM 2092 O O   . HOH   C 3 .   ? -5.133  -25.856 -5.054  1.00 43.94 ? 707 HOH   A O   1 
HETATM 2093 O O   . HOH   C 3 .   ? -0.762  -4.320  0.722   1.00 35.64 ? 708 HOH   A O   1 
HETATM 2094 O O   . HOH   C 3 .   ? 25.257  3.528   -31.775 1.00 45.64 ? 709 HOH   A O   1 
HETATM 2095 O O   . HOH   C 3 .   ? -7.429  -4.912  -42.131 1.00 50.37 ? 710 HOH   A O   1 
HETATM 2096 O O   . HOH   C 3 .   ? 22.984  -7.297  -10.568 1.00 45.45 ? 711 HOH   A O   1 
HETATM 2097 O O   . HOH   C 3 .   ? 11.877  -18.930 -17.030 1.00 47.22 ? 712 HOH   A O   1 
HETATM 2098 O O   . HOH   C 3 .   ? 17.081  -14.324 -15.958 1.00 40.55 ? 713 HOH   A O   1 
HETATM 2099 O O   . HOH   C 3 .   ? -1.529  -12.099 -20.313 1.00 40.65 ? 714 HOH   A O   1 
HETATM 2100 O O   . HOH   C 3 .   ? 11.854  -21.222 -32.731 1.00 36.85 ? 715 HOH   A O   1 
HETATM 2101 O O   . HOH   C 3 .   ? 23.497  -18.513 -12.552 1.00 55.03 ? 716 HOH   A O   1 
HETATM 2102 O O   . HOH   C 3 .   ? 10.916  7.757   -36.638 1.00 41.10 ? 717 HOH   A O   1 
HETATM 2103 O O   . HOH   C 3 .   ? 9.651   -3.493  3.079   1.00 26.14 ? 718 HOH   A O   1 
HETATM 2104 O O   . HOH   C 3 .   ? 20.158  -2.556  -20.039 1.00 36.64 ? 719 HOH   A O   1 
HETATM 2105 O O   . HOH   C 3 .   ? 12.100  5.357   -39.901 1.00 39.89 ? 720 HOH   A O   1 
HETATM 2106 O O   . HOH   C 3 .   ? 15.684  -21.367 -30.072 1.00 43.72 ? 721 HOH   A O   1 
HETATM 2107 O O   . HOH   C 3 .   ? 16.481  -13.551 -47.831 1.00 45.02 ? 722 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   . ALA   A 5   ? 0.6010 0.5326 0.4888 -0.0202 -0.0158 0.0698  5   ALA   A N   
2    C CA  . ALA   A 5   ? 0.5036 0.5350 0.4861 -0.0123 0.0163  0.0491  5   ALA   A CA  
3    C C   . ALA   A 5   ? 0.4790 0.5178 0.4684 -0.0702 0.0507  0.0473  5   ALA   A C   
4    O O   . ALA   A 5   ? 0.4730 0.5627 0.4870 -0.0953 0.0654  0.0627  5   ALA   A O   
5    C CB  . ALA   A 5   ? 0.4836 0.5433 0.4938 0.0090  0.0259  0.0333  5   ALA   A CB  
6    N N   . VAL   A 6   ? 0.4388 0.4538 0.4241 -0.1205 0.0992  0.0413  6   VAL   A N   
7    C CA  . VAL   A 6   ? 0.4106 0.3862 0.3909 -0.0840 0.1094  0.0136  6   VAL   A CA  
8    C C   . VAL   A 6   ? 0.3141 0.3019 0.3462 -0.1057 0.0808  -0.0089 6   VAL   A C   
9    O O   . VAL   A 6   ? 0.3361 0.3127 0.3696 -0.1494 0.0618  -0.0173 6   VAL   A O   
10   C CB  . VAL   A 6   ? 0.4635 0.4487 0.4028 -0.0679 0.1576  0.0134  6   VAL   A CB  
11   C CG1 . VAL   A 6   ? 0.4205 0.4508 0.4070 -0.0558 0.1471  0.0086  6   VAL   A CG1 
12   C CG2 . VAL   A 6   ? 0.4374 0.4657 0.4080 -0.0733 0.1780  0.0094  6   VAL   A CG2 
13   N N   . VAL   A 7   ? 0.2536 0.2646 0.2790 -0.1009 0.0556  -0.0013 7   VAL   A N   
14   C CA  . VAL   A 7   ? 0.1956 0.2213 0.2499 -0.0455 0.0354  0.0049  7   VAL   A CA  
15   C C   . VAL   A 7   ? 0.1786 0.2360 0.2459 -0.0334 -0.0010 -0.0002 7   VAL   A C   
16   O O   . VAL   A 7   ? 0.2111 0.2098 0.2533 -0.0021 -0.0056 -0.0236 7   VAL   A O   
17   C CB  . VAL   A 7   ? 0.2556 0.1972 0.2556 0.0005  0.0195  0.0290  7   VAL   A CB  
18   C CG1 . VAL   A 7   ? 0.2884 0.1957 0.2444 -0.0075 0.0734  0.0386  7   VAL   A CG1 
19   C CG2 . VAL   A 7   ? 0.3601 0.2088 0.2782 0.0144  0.0279  0.0298  7   VAL   A CG2 
20   N N   . THR   A 8   ? 0.2142 0.2207 0.2255 -0.0424 -0.0147 0.0046  8   THR   A N   
21   C CA  A THR   A 8   ? 0.1950 0.2392 0.2386 -0.0316 0.0059  0.0056  8   THR   A CA  
22   C CA  B THR   A 8   ? 0.1967 0.2242 0.2194 -0.0274 0.0076  -0.0103 8   THR   A CA  
23   C C   . THR   A 8   ? 0.1957 0.1987 0.2116 0.0108  0.0089  -0.0204 8   THR   A C   
24   O O   . THR   A 8   ? 0.2075 0.1961 0.2158 -0.0144 0.0194  -0.0199 8   THR   A O   
25   C CB  A THR   A 8   ? 0.2084 0.2898 0.2832 -0.0650 0.0335  0.0331  8   THR   A CB  
26   C CB  B THR   A 8   ? 0.1930 0.2451 0.2249 -0.0531 0.0368  -0.0169 8   THR   A CB  
27   O OG1 A THR   A 8   ? 0.2611 0.3244 0.3115 -0.0495 0.0500  0.0347  8   THR   A OG1 
28   O OG1 B THR   A 8   ? 0.2220 0.2432 0.2212 -0.0651 0.0232  -0.0319 8   THR   A OG1 
29   C CG2 A THR   A 8   ? 0.2611 0.3165 0.2958 -0.0474 0.0154  0.0405  8   THR   A CG2 
30   C CG2 B THR   A 8   ? 0.1960 0.2619 0.2345 -0.0411 0.0553  -0.0184 8   THR   A CG2 
31   N N   . GLN   A 9   ? 0.1708 0.1877 0.1897 -0.0074 0.0122  -0.0086 9   GLN   A N   
32   C CA  . GLN   A 9   ? 0.1868 0.1800 0.1914 -0.0361 0.0004  0.0043  9   GLN   A CA  
33   C C   . GLN   A 9   ? 0.1654 0.1997 0.1977 -0.0221 -0.0027 0.0077  9   GLN   A C   
34   O O   . GLN   A 9   ? 0.1945 0.2322 0.1827 0.0209  0.0171  0.0056  9   GLN   A O   
35   C CB  . GLN   A 9   ? 0.1665 0.1884 0.1894 -0.0118 -0.0250 0.0005  9   GLN   A CB  
36   C CG  . GLN   A 9   ? 0.1657 0.1965 0.1994 0.0091  -0.0273 -0.0188 9   GLN   A CG  
37   C CD  . GLN   A 9   ? 0.1772 0.1966 0.1703 -0.0156 -0.0073 0.0017  9   GLN   A CD  
38   O OE1 . GLN   A 9   ? 0.1603 0.2140 0.1587 -0.0253 0.0121  0.0144  9   GLN   A OE1 
39   N NE2 . GLN   A 9   ? 0.1977 0.2198 0.1916 -0.0100 0.0098  -0.0032 9   GLN   A NE2 
40   N N   . GLU   A 10  ? 0.1951 0.2018 0.1794 0.0192  -0.0055 0.0106  10  GLU   A N   
41   C CA  . GLU   A 10  ? 0.1806 0.2095 0.1715 0.0259  0.0196  -0.0066 10  GLU   A CA  
42   C C   . GLU   A 10  ? 0.2129 0.1916 0.1917 0.0490  0.0110  -0.0067 10  GLU   A C   
43   O O   . GLU   A 10  ? 0.2142 0.2075 0.2240 0.0232  -0.0199 -0.0016 10  GLU   A O   
44   C CB  . GLU   A 10  ? 0.2094 0.2139 0.1762 0.0321  0.0085  -0.0178 10  GLU   A CB  
45   C CG  . GLU   A 10  ? 0.2385 0.2334 0.1949 0.0416  0.0105  -0.0359 10  GLU   A CG  
46   C CD  . GLU   A 10  ? 0.2386 0.2371 0.2132 0.0098  0.0095  -0.0242 10  GLU   A CD  
47   O OE1 . GLU   A 10  ? 0.1983 0.2117 0.2294 0.0137  0.0222  -0.0072 10  GLU   A OE1 
48   O OE2 . GLU   A 10  ? 0.2095 0.2730 0.2354 0.0327  0.0183  -0.0259 10  GLU   A OE2 
49   N N   . SER   A 11  ? 0.1667 0.1842 0.1780 0.0133  0.0140  -0.0148 11  SER   A N   
50   C CA  A SER   A 11  ? 0.1190 0.2035 0.1912 0.0202  0.0099  -0.0178 11  SER   A CA  
51   C CA  B SER   A 11  ? 0.1503 0.2082 0.1800 0.0092  0.0048  -0.0076 11  SER   A CA  
52   C C   . SER   A 11  ? 0.1603 0.2048 0.1846 -0.0020 -0.0023 0.0186  11  SER   A C   
53   O O   . SER   A 11  ? 0.1620 0.2203 0.1940 0.0255  -0.0078 0.0116  11  SER   A O   
54   C CB  A SER   A 11  ? 0.1549 0.2409 0.2170 0.0256  0.0497  -0.0318 11  SER   A CB  
55   C CB  B SER   A 11  ? 0.1798 0.2450 0.1819 0.0097  0.0151  -0.0132 11  SER   A CB  
56   O OG  A SER   A 11  ? 0.1966 0.2694 0.2378 -0.0311 0.0839  -0.0267 11  SER   A OG  
57   O OG  B SER   A 11  ? 0.2260 0.2779 0.1832 -0.0263 0.0158  -0.0061 11  SER   A OG  
58   N N   . ALA   A 12  ? 0.1551 0.1989 0.1769 -0.0071 0.0212  0.0252  12  ALA   A N   
59   C CA  . ALA   A 12  ? 0.1620 0.1975 0.1775 0.0174  0.0412  0.0186  12  ALA   A CA  
60   C C   . ALA   A 12  ? 0.1437 0.2211 0.1619 0.0022  0.0092  0.0110  12  ALA   A C   
61   O O   . ALA   A 12  ? 0.1533 0.2530 0.1926 -0.0193 -0.0284 0.0061  12  ALA   A O   
62   C CB  . ALA   A 12  ? 0.1972 0.2045 0.2249 0.0143  0.0590  0.0114  12  ALA   A CB  
63   N N   . LEU   A 13  ? 0.1586 0.2009 0.1632 0.0097  0.0291  0.0126  13  LEU   A N   
64   C CA  . LEU   A 13  ? 0.1579 0.1936 0.1807 0.0232  0.0186  0.0026  13  LEU   A CA  
65   C C   . LEU   A 13  ? 0.1237 0.2224 0.1924 0.0001  -0.0105 0.0187  13  LEU   A C   
66   O O   . LEU   A 13  ? 0.1738 0.2417 0.2045 -0.0212 -0.0602 0.0210  13  LEU   A O   
67   C CB  . LEU   A 13  ? 0.1993 0.2112 0.1966 -0.0024 0.0135  0.0133  13  LEU   A CB  
68   C CG  . LEU   A 13  ? 0.2444 0.2132 0.1935 0.0076  -0.0056 0.0191  13  LEU   A CG  
69   C CD1 . LEU   A 13  ? 0.2545 0.2153 0.1808 0.0602  -0.0057 0.0087  13  LEU   A CD1 
70   C CD2 . LEU   A 13  ? 0.2292 0.2881 0.2065 0.0027  -0.0013 0.0199  13  LEU   A CD2 
71   N N   . THR   A 14  ? 0.1390 0.2194 0.1984 -0.0283 0.0008  0.0372  14  THR   A N   
72   C CA  . THR   A 14  ? 0.1502 0.2152 0.2062 -0.0135 0.0305  0.0388  14  THR   A CA  
73   C C   . THR   A 14  ? 0.1292 0.2464 0.2260 -0.0336 -0.0105 0.0238  14  THR   A C   
74   O O   . THR   A 14  ? 0.1296 0.2701 0.2293 -0.0367 -0.0075 -0.0062 14  THR   A O   
75   C CB  . THR   A 14  ? 0.2020 0.2140 0.2242 -0.0065 0.0085  0.0352  14  THR   A CB  
76   O OG1 . THR   A 14  ? 0.2201 0.2461 0.2575 0.0418  0.0054  0.0127  14  THR   A OG1 
77   C CG2 . THR   A 14  ? 0.2191 0.2204 0.2274 -0.0338 -0.0410 0.0537  14  THR   A CG2 
78   N N   . THR   A 15  ? 0.0843 0.2737 0.2554 -0.0126 0.0059  0.0259  15  THR   A N   
79   C CA  . THR   A 15  ? 0.0955 0.2632 0.2627 -0.0571 0.0351  0.0120  15  THR   A CA  
80   C C   . THR   A 15  ? 0.1297 0.2912 0.2414 -0.0371 0.0153  0.0220  15  THR   A C   
81   O O   . THR   A 15  ? 0.1490 0.3065 0.2207 -0.0048 -0.0039 0.0446  15  THR   A O   
82   C CB  . THR   A 15  ? 0.1894 0.2897 0.2812 -0.0550 0.0419  -0.0095 15  THR   A CB  
83   O OG1 . THR   A 15  ? 0.2355 0.2811 0.3191 -0.0703 0.0664  0.0188  15  THR   A OG1 
84   C CG2 . THR   A 15  ? 0.1730 0.2923 0.2719 -0.0731 0.0165  -0.0085 15  THR   A CG2 
85   N N   . SER   A 16  ? 0.1528 0.2598 0.2558 -0.0467 0.0292  0.0234  16  SER   A N   
86   C CA  A SER   A 16  ? 0.1550 0.2546 0.2588 -0.0217 0.0009  0.0266  16  SER   A CA  
87   C CA  B SER   A 16  ? 0.1319 0.2541 0.2629 -0.0233 -0.0052 0.0430  16  SER   A CA  
88   C C   . SER   A 16  ? 0.1505 0.2195 0.2478 -0.0099 0.0118  0.0076  16  SER   A C   
89   O O   . SER   A 16  ? 0.1620 0.2244 0.2500 -0.0314 0.0101  0.0073  16  SER   A O   
90   C CB  A SER   A 16  ? 0.2520 0.2804 0.2760 -0.0188 -0.0077 0.0214  16  SER   A CB  
91   C CB  B SER   A 16  ? 0.1718 0.2838 0.2871 -0.0265 -0.0213 0.0553  16  SER   A CB  
92   O OG  A SER   A 16  ? 0.3298 0.2914 0.2881 -0.0192 -0.0117 0.0015  16  SER   A OG  
93   O OG  B SER   A 16  ? 0.1795 0.3129 0.3076 -0.0322 -0.0271 0.0469  16  SER   A OG  
94   N N   . PRO   A 17  ? 0.1400 0.2320 0.2389 -0.0454 0.0135  -0.0089 17  PRO   A N   
95   C CA  . PRO   A 17  ? 0.1071 0.2381 0.2227 -0.0249 0.0124  -0.0208 17  PRO   A CA  
96   C C   . PRO   A 17  ? 0.1204 0.2451 0.1930 0.0150  0.0005  0.0180  17  PRO   A C   
97   O O   . PRO   A 17  ? 0.1932 0.2427 0.1671 -0.0072 -0.0093 0.0354  17  PRO   A O   
98   C CB  . PRO   A 17  ? 0.1628 0.2882 0.2430 -0.0261 0.0127  -0.0163 17  PRO   A CB  
99   C CG  . PRO   A 17  ? 0.1707 0.3053 0.2537 -0.0503 -0.0124 -0.0167 17  PRO   A CG  
100  C CD  . PRO   A 17  ? 0.2143 0.2746 0.2485 -0.0670 -0.0242 -0.0259 17  PRO   A CD  
101  N N   . GLY   A 18  ? 0.1316 0.2519 0.1963 -0.0100 0.0103  0.0287  18  GLY   A N   
102  C CA  . GLY   A 18  ? 0.1178 0.2786 0.2080 -0.0046 0.0085  0.0295  18  GLY   A CA  
103  C C   . GLY   A 18  ? 0.1014 0.2521 0.2169 -0.0249 0.0149  0.0308  18  GLY   A C   
104  O O   . GLY   A 18  ? 0.1483 0.2544 0.2227 -0.0023 0.0230  0.0171  18  GLY   A O   
105  N N   . GLU   A 19  ? 0.1080 0.2218 0.2243 -0.0453 -0.0123 0.0264  19  GLU   A N   
106  C CA  . GLU   A 19  ? 0.1124 0.2467 0.2349 -0.0116 -0.0014 0.0219  19  GLU   A CA  
107  C C   . GLU   A 19  ? 0.1451 0.2284 0.2124 -0.0206 -0.0175 0.0251  19  GLU   A C   
108  O O   . GLU   A 19  ? 0.1715 0.2659 0.2106 -0.0070 -0.0330 0.0172  19  GLU   A O   
109  C CB  . GLU   A 19  ? 0.0930 0.2876 0.2595 -0.0220 -0.0119 0.0312  19  GLU   A CB  
110  C CG  . GLU   A 19  ? 0.2069 0.3215 0.2808 -0.0129 0.0000  0.0387  19  GLU   A CG  
111  C CD  . GLU   A 19  ? 0.3358 0.3661 0.3144 -0.0796 -0.0217 0.0531  19  GLU   A CD  
112  O OE1 . GLU   A 19  ? 0.5162 0.3962 0.3418 -0.0738 -0.0389 0.0536  19  GLU   A OE1 
113  O OE2 . GLU   A 19  ? 0.3527 0.4341 0.3271 -0.0876 0.0142  0.0334  19  GLU   A OE2 
114  N N   . THR   A 20  ? 0.1595 0.2167 0.2002 -0.0357 -0.0021 0.0407  20  THR   A N   
115  C CA  . THR   A 20  ? 0.1744 0.2383 0.2066 -0.0122 -0.0063 0.0368  20  THR   A CA  
116  C C   . THR   A 20  ? 0.1342 0.2562 0.1984 -0.0336 -0.0338 0.0136  20  THR   A C   
117  O O   . THR   A 20  ? 0.1608 0.3169 0.2071 -0.0233 -0.0401 0.0317  20  THR   A O   
118  C CB  . THR   A 20  ? 0.1842 0.2835 0.2519 -0.0179 -0.0168 0.0226  20  THR   A CB  
119  O OG1 . THR   A 20  ? 0.1961 0.3431 0.2880 0.0066  0.0060  0.0239  20  THR   A OG1 
120  C CG2 . THR   A 20  ? 0.2386 0.2654 0.2450 -0.0133 -0.0166 0.0268  20  THR   A CG2 
121  N N   . VAL   A 21  ? 0.1588 0.2166 0.1979 -0.0064 0.0164  0.0256  21  VAL   A N   
122  C CA  A VAL   A 21  ? 0.1963 0.1940 0.2173 0.0148  0.0498  0.0163  21  VAL   A CA  
123  C CA  B VAL   A 21  ? 0.1945 0.2149 0.2069 0.0071  0.0405  0.0163  21  VAL   A CA  
124  C C   . VAL   A 21  ? 0.1466 0.2043 0.2002 0.0030  0.0106  0.0212  21  VAL   A C   
125  O O   . VAL   A 21  ? 0.1391 0.2333 0.2159 -0.0081 -0.0221 0.0241  21  VAL   A O   
126  C CB  A VAL   A 21  ? 0.2643 0.2152 0.2780 0.0095  0.0908  -0.0193 21  VAL   A CB  
127  C CB  B VAL   A 21  ? 0.2499 0.2735 0.2468 -0.0066 0.0614  -0.0085 21  VAL   A CB  
128  C CG1 A VAL   A 21  ? 0.2119 0.1844 0.3100 -0.0027 0.0989  -0.0064 21  VAL   A CG1 
129  C CG1 B VAL   A 21  ? 0.1981 0.3089 0.2469 -0.0373 0.0490  0.0020  21  VAL   A CG1 
130  C CG2 A VAL   A 21  ? 0.3394 0.2532 0.2868 0.0095  0.1030  -0.0573 21  VAL   A CG2 
131  C CG2 B VAL   A 21  ? 0.3003 0.2780 0.2718 -0.0019 0.0621  -0.0252 21  VAL   A CG2 
132  N N   . THR   A 22  ? 0.1337 0.2119 0.1900 -0.0246 -0.0076 0.0137  22  THR   A N   
133  C CA  . THR   A 22  ? 0.1480 0.2199 0.1769 -0.0315 0.0150  0.0167  22  THR   A CA  
134  C C   . THR   A 22  ? 0.1223 0.2154 0.1741 0.0023  -0.0028 0.0243  22  THR   A C   
135  O O   . THR   A 22  ? 0.1562 0.2765 0.1778 0.0285  -0.0131 0.0455  22  THR   A O   
136  C CB  . THR   A 22  ? 0.2108 0.2727 0.2047 0.0074  -0.0163 -0.0317 22  THR   A CB  
137  O OG1 . THR   A 22  ? 0.3155 0.3275 0.2316 0.0307  -0.0347 -0.0398 22  THR   A OG1 
138  C CG2 . THR   A 22  ? 0.1722 0.2733 0.1922 -0.0203 0.0270  -0.0648 22  THR   A CG2 
139  N N   . LEU   A 23  ? 0.1617 0.1791 0.1511 0.0341  -0.0105 -0.0134 23  LEU   A N   
140  C CA  . LEU   A 23  ? 0.1673 0.1728 0.1904 0.0118  0.0200  -0.0051 23  LEU   A CA  
141  C C   . LEU   A 23  ? 0.1296 0.1907 0.1876 0.0078  0.0127  0.0124  23  LEU   A C   
142  O O   . LEU   A 23  ? 0.1537 0.2111 0.2053 0.0173  0.0090  0.0216  23  LEU   A O   
143  C CB  . LEU   A 23  ? 0.2169 0.1827 0.2228 -0.0330 -0.0048 -0.0461 23  LEU   A CB  
144  C CG  . LEU   A 23  ? 0.2270 0.2764 0.2421 -0.0371 -0.0208 -0.1026 23  LEU   A CG  
145  C CD1 . LEU   A 23  ? 0.3664 0.3307 0.2585 -0.0540 -0.0034 -0.0815 23  LEU   A CD1 
146  C CD2 . LEU   A 23  ? 0.3182 0.3351 0.2590 -0.0239 -0.0248 -0.1142 23  LEU   A CD2 
147  N N   . THR   A 24  ? 0.1586 0.1898 0.1877 -0.0042 0.0136  -0.0109 24  THR   A N   
148  C CA  . THR   A 24  ? 0.1664 0.2012 0.1770 -0.0132 -0.0061 0.0078  24  THR   A CA  
149  C C   . THR   A 24  ? 0.1839 0.1841 0.1761 0.0095  0.0010  0.0026  24  THR   A C   
150  O O   . THR   A 24  ? 0.2036 0.1746 0.1797 -0.0086 0.0396  -0.0142 24  THR   A O   
151  C CB  . THR   A 24  ? 0.2001 0.2359 0.1886 0.0016  -0.0490 0.0068  24  THR   A CB  
152  O OG1 . THR   A 24  ? 0.1801 0.2540 0.2312 0.0059  -0.0221 -0.0092 24  THR   A OG1 
153  C CG2 . THR   A 24  ? 0.2611 0.2612 0.1712 0.0183  -0.0425 0.0297  24  THR   A CG2 
154  N N   . CYS   A 25  ? 0.1767 0.1880 0.1755 -0.0102 0.0072  0.0197  25  CYS   A N   
155  C CA  . CYS   A 25  ? 0.2407 0.1967 0.1961 -0.0440 0.0035  -0.0068 25  CYS   A CA  
156  C C   . CYS   A 25  ? 0.1995 0.1993 0.2294 -0.0259 0.0052  -0.0181 25  CYS   A C   
157  O O   . CYS   A 25  ? 0.2344 0.2157 0.2597 -0.0198 0.0307  -0.0297 25  CYS   A O   
158  C CB  . CYS   A 25  ? 0.2556 0.2331 0.1924 -0.0512 -0.0077 0.0005  25  CYS   A CB  
159  S SG  . CYS   A 25  ? 0.2635 0.2189 0.2136 -0.0100 0.0014  0.0069  25  CYS   A SG  
160  N N   . ARG   A 26  ? 0.2052 0.1850 0.2438 -0.0506 0.0303  -0.0048 26  ARG   A N   
161  C CA  A ARG   A 26  ? 0.2505 0.2057 0.2573 -0.0669 0.0121  -0.0068 26  ARG   A CA  
162  C CA  B ARG   A 26  ? 0.2389 0.1925 0.2548 -0.0694 0.0146  -0.0094 26  ARG   A CA  
163  C C   . ARG   A 26  ? 0.2998 0.1959 0.2581 -0.0476 0.0196  -0.0139 26  ARG   A C   
164  O O   . ARG   A 26  ? 0.2817 0.2111 0.2638 -0.0642 0.0553  -0.0434 26  ARG   A O   
165  C CB  A ARG   A 26  ? 0.2708 0.2774 0.2946 -0.0663 -0.0039 -0.0103 26  ARG   A CB  
166  C CB  B ARG   A 26  ? 0.2309 0.2426 0.2865 -0.0699 0.0065  -0.0125 26  ARG   A CB  
167  C CG  A ARG   A 26  ? 0.3656 0.3571 0.3424 -0.0621 -0.0112 -0.0117 26  ARG   A CG  
168  C CG  B ARG   A 26  ? 0.3139 0.3197 0.3313 -0.0672 0.0040  -0.0075 26  ARG   A CG  
169  C CD  A ARG   A 26  ? 0.4358 0.4289 0.3887 -0.0477 -0.0159 -0.0098 26  ARG   A CD  
170  C CD  B ARG   A 26  ? 0.4015 0.3925 0.3812 -0.0588 -0.0053 -0.0009 26  ARG   A CD  
171  N NE  A ARG   A 26  ? 0.4771 0.4774 0.4279 -0.0323 0.0010  0.0062  26  ARG   A NE  
172  N NE  B ARG   A 26  ? 0.4475 0.4438 0.4247 -0.0691 0.0076  0.0008  26  ARG   A NE  
173  C CZ  A ARG   A 26  ? 0.4971 0.4999 0.4509 0.0062  0.0130  0.0210  26  ARG   A CZ  
174  C CZ  B ARG   A 26  ? 0.4949 0.4915 0.4533 -0.0445 0.0003  -0.0227 26  ARG   A CZ  
175  N NH1 A ARG   A 26  ? 0.5011 0.5099 0.4564 0.0377  0.0176  0.0277  26  ARG   A NH1 
176  N NH1 B ARG   A 26  ? 0.4658 0.5044 0.4584 -0.0233 -0.0110 -0.0415 26  ARG   A NH1 
177  N NH2 A ARG   A 26  ? 0.5085 0.5034 0.4622 0.0062  0.0115  0.0264  26  ARG   A NH2 
178  N NH2 B ARG   A 26  ? 0.5710 0.5069 0.4702 -0.0471 0.0025  -0.0206 26  ARG   A NH2 
179  N N   . SER   A 27  ? 0.3102 0.1998 0.2767 -0.0320 0.0020  0.0017  27  SER   A N   
180  C CA  . SER   A 27  ? 0.3101 0.2558 0.2957 -0.0873 0.0251  0.0131  27  SER   A CA  
181  C C   . SER   A 27  ? 0.3456 0.2815 0.3090 -0.1026 0.0593  -0.0005 27  SER   A C   
182  O O   . SER   A 27  ? 0.3816 0.2774 0.3127 -0.1103 0.0186  -0.0079 27  SER   A O   
183  C CB  . SER   A 27  ? 0.3897 0.2938 0.2998 -0.1109 0.0126  0.0412  27  SER   A CB  
184  O OG  . SER   A 27  ? 0.3951 0.3392 0.2927 -0.1378 0.0093  0.0276  27  SER   A OG  
185  N N   . SER   A 28  ? 0.3771 0.2995 0.3368 -0.1139 0.0681  -0.0157 28  SER   A N   
186  C CA  . SER   A 28  ? 0.3493 0.3160 0.3861 -0.0806 0.0592  -0.0153 28  SER   A CA  
187  C C   . SER   A 28  ? 0.3492 0.3327 0.4316 -0.0832 0.0221  0.0005  28  SER   A C   
188  O O   . SER   A 28  ? 0.3258 0.3600 0.4497 -0.0502 0.0041  -0.0104 28  SER   A O   
189  C CB  . SER   A 28  ? 0.3117 0.3502 0.4039 -0.1239 0.0344  0.0050  28  SER   A CB  
190  O OG  . SER   A 28  ? 0.3586 0.3656 0.4116 -0.0573 0.0335  0.0284  28  SER   A OG  
191  N N   . THR   A 29  ? 0.3987 0.3093 0.4515 -0.0930 -0.0023 0.0270  29  THR   A N   
192  C CA  . THR   A 29  ? 0.3752 0.3107 0.4630 -0.0847 0.0091  0.0173  29  THR   A CA  
193  C C   . THR   A 29  ? 0.3770 0.3079 0.4542 -0.1010 -0.0020 -0.0194 29  THR   A C   
194  O O   . THR   A 29  ? 0.4485 0.3237 0.4768 -0.0605 0.0069  -0.0751 29  THR   A O   
195  C CB  . THR   A 29  ? 0.3421 0.3247 0.4812 -0.0730 0.0197  0.0420  29  THR   A CB  
196  O OG1 . THR   A 29  ? 0.2843 0.3527 0.5010 -0.0774 0.0058  0.0399  29  THR   A OG1 
197  C CG2 . THR   A 29  ? 0.4448 0.3556 0.4731 -0.0216 -0.0001 0.0588  29  THR   A CG2 
198  N N   . GLY   A 30  ? 0.3976 0.2977 0.4206 -0.0615 0.0008  -0.0031 30  GLY   A N   
199  C CA  . GLY   A 30  ? 0.4120 0.3315 0.3902 -0.0634 -0.0270 -0.0199 30  GLY   A CA  
200  C C   . GLY   A 30  ? 0.4227 0.3286 0.3571 -0.0332 -0.0698 -0.0461 30  GLY   A C   
201  O O   . GLY   A 30  ? 0.4065 0.3712 0.3595 0.0015  -0.0730 -0.1025 30  GLY   A O   
202  N N   . ALA   A 31  ? 0.3692 0.2895 0.3321 -0.0360 -0.1164 -0.0364 31  ALA   A N   
203  C CA  . ALA   A 31  ? 0.3245 0.2722 0.3026 -0.0748 -0.0959 -0.0474 31  ALA   A CA  
204  C C   . ALA   A 31  ? 0.3164 0.2646 0.2803 -0.0631 -0.0543 -0.0106 31  ALA   A C   
205  O O   . ALA   A 31  ? 0.3198 0.3060 0.2983 -0.0947 -0.0203 0.0045  31  ALA   A O   
206  C CB  . ALA   A 31  ? 0.3866 0.2250 0.2903 -0.0756 -0.0980 -0.0849 31  ALA   A CB  
207  N N   . VAL   A 32  ? 0.3096 0.2403 0.2472 -0.0483 -0.0642 -0.0353 32  VAL   A N   
208  C CA  . VAL   A 32  ? 0.2751 0.2317 0.2262 -0.0636 -0.0676 -0.0415 32  VAL   A CA  
209  C C   . VAL   A 32  ? 0.3417 0.2130 0.2128 -0.0224 -0.0317 -0.0382 32  VAL   A C   
210  O O   . VAL   A 32  ? 0.4186 0.2643 0.1939 -0.0014 -0.0571 -0.0360 32  VAL   A O   
211  C CB  . VAL   A 32  ? 0.2583 0.2263 0.2259 -0.0500 -0.0213 -0.0291 32  VAL   A CB  
212  C CG1 . VAL   A 32  ? 0.3054 0.2322 0.1974 -0.0742 -0.0191 -0.0106 32  VAL   A CG1 
213  C CG2 . VAL   A 32  ? 0.2805 0.2276 0.2486 0.0191  -0.0112 -0.0329 32  VAL   A CG2 
214  N N   . ILE   A 33  ? 0.2893 0.1750 0.2355 -0.0102 -0.0201 -0.0245 33  ILE   A N   
215  C CA  . ILE   A 33  ? 0.2728 0.1896 0.2313 -0.0387 0.0188  -0.0490 33  ILE   A CA  
216  C C   . ILE   A 33  ? 0.2665 0.1597 0.2318 -0.0459 0.0324  -0.0212 33  ILE   A C   
217  O O   . ILE   A 33  ? 0.3117 0.1495 0.2218 -0.0383 0.0202  -0.0212 33  ILE   A O   
218  C CB  . ILE   A 33  ? 0.2862 0.2068 0.2307 -0.0856 0.0037  -0.0459 33  ILE   A CB  
219  C CG1 . ILE   A 33  ? 0.3120 0.1943 0.2492 -0.0386 0.0098  0.0310  33  ILE   A CG1 
220  C CG2 . ILE   A 33  ? 0.3878 0.2649 0.2253 -0.0928 -0.0226 -0.0643 33  ILE   A CG2 
221  C CD1 . ILE   A 33  ? 0.3051 0.2263 0.2576 -0.0286 0.0054  0.0563  33  ILE   A CD1 
222  N N   . SER   A 34  ? 0.2584 0.1801 0.2329 -0.0329 0.0296  -0.0320 34  SER   A N   
223  C CA  . SER   A 34  ? 0.2689 0.2265 0.2245 0.0132  0.0419  -0.0343 34  SER   A CA  
224  C C   . SER   A 34  ? 0.2916 0.2262 0.2143 0.0086  -0.0137 -0.0352 34  SER   A C   
225  O O   . SER   A 34  ? 0.2245 0.2167 0.2002 0.0055  -0.0300 -0.0357 34  SER   A O   
226  C CB  . SER   A 34  ? 0.3355 0.3330 0.2363 0.0439  0.0679  -0.0443 34  SER   A CB  
227  O OG  . SER   A 34  ? 0.4227 0.4501 0.2853 0.0597  0.0491  -0.0473 34  SER   A OG  
228  N N   . SER   A 35  ? 0.3106 0.2255 0.2203 -0.0192 -0.0129 -0.0151 35  SER   A N   
229  C CA  . SER   A 35  ? 0.3100 0.1911 0.2340 0.0079  -0.0285 0.0002  35  SER   A CA  
230  C C   . SER   A 35  ? 0.2660 0.1981 0.2366 0.0209  0.0052  -0.0066 35  SER   A C   
231  O O   . SER   A 35  ? 0.3244 0.2076 0.2374 -0.0129 0.0235  -0.0157 35  SER   A O   
232  C CB  . SER   A 35  ? 0.3121 0.2302 0.2654 -0.0354 -0.0219 0.0282  35  SER   A CB  
233  O OG  . SER   A 35  ? 0.3893 0.3128 0.2906 -0.0853 -0.0439 0.0667  35  SER   A OG  
234  N N   . ASN   A 36  ? 0.2336 0.1680 0.2340 0.0195  0.0028  -0.0220 36  ASN   A N   
235  C CA  . ASN   A 36  ? 0.1796 0.1976 0.2285 -0.0227 -0.0078 -0.0162 36  ASN   A CA  
236  C C   . ASN   A 36  ? 0.2183 0.1914 0.2095 0.0014  -0.0088 -0.0012 36  ASN   A C   
237  O O   . ASN   A 36  ? 0.2460 0.1781 0.2079 -0.0049 0.0041  -0.0355 36  ASN   A O   
238  C CB  . ASN   A 36  ? 0.1863 0.2002 0.2408 -0.0133 -0.0311 -0.0201 36  ASN   A CB  
239  C CG  . ASN   A 36  ? 0.2139 0.2448 0.2283 0.0164  -0.0258 -0.0485 36  ASN   A CG  
240  O OD1 . ASN   A 36  ? 0.2627 0.2439 0.2560 -0.0176 -0.0231 -0.0545 36  ASN   A OD1 
241  N ND2 . ASN   A 36  ? 0.2340 0.2865 0.2385 -0.0062 -0.0090 -0.0429 36  ASN   A ND2 
242  N N   . PHE   A 37  ? 0.2184 0.1904 0.1961 -0.0093 0.0040  0.0084  37  PHE   A N   
243  C CA  . PHE   A 37  ? 0.2399 0.1679 0.1824 0.0188  -0.0057 0.0261  37  PHE   A CA  
244  C C   . PHE   A 37  ? 0.2542 0.1672 0.1742 0.0262  0.0212  0.0011  37  PHE   A C   
245  O O   . PHE   A 37  ? 0.2506 0.1809 0.1652 -0.0100 0.0022  -0.0074 37  PHE   A O   
246  C CB  . PHE   A 37  ? 0.2371 0.1892 0.2103 0.0107  0.0059  0.0184  37  PHE   A CB  
247  C CG  . PHE   A 37  ? 0.2328 0.1807 0.2044 0.0155  -0.0155 0.0036  37  PHE   A CG  
248  C CD1 . PHE   A 37  ? 0.2937 0.1716 0.2017 0.0432  0.0393  0.0040  37  PHE   A CD1 
249  C CD2 . PHE   A 37  ? 0.2347 0.1986 0.2037 -0.0085 -0.0425 0.0113  37  PHE   A CD2 
250  C CE1 . PHE   A 37  ? 0.3513 0.1863 0.2114 0.0435  0.0287  0.0017  37  PHE   A CE1 
251  C CE2 . PHE   A 37  ? 0.2763 0.1819 0.2049 0.0362  -0.0444 0.0128  37  PHE   A CE2 
252  C CZ  . PHE   A 37  ? 0.2885 0.2030 0.2160 0.0528  0.0101  0.0161  37  PHE   A CZ  
253  N N   . VAL   A 38  ? 0.1998 0.1505 0.1912 0.0171  0.0058  0.0054  38  VAL   A N   
254  C CA  . VAL   A 38  ? 0.2099 0.1371 0.1883 0.0159  -0.0189 -0.0010 38  VAL   A CA  
255  C C   . VAL   A 38  ? 0.2312 0.1531 0.1910 -0.0019 -0.0441 -0.0234 38  VAL   A C   
256  O O   . VAL   A 38  ? 0.2223 0.1810 0.2143 0.0103  -0.0083 -0.0211 38  VAL   A O   
257  C CB  . VAL   A 38  ? 0.2334 0.1455 0.1998 -0.0003 -0.0139 -0.0182 38  VAL   A CB  
258  C CG1 . VAL   A 38  ? 0.2039 0.1531 0.1998 0.0039  -0.0421 -0.0139 38  VAL   A CG1 
259  C CG2 . VAL   A 38  ? 0.2461 0.1801 0.2228 -0.0568 0.0060  -0.0334 38  VAL   A CG2 
260  N N   . SER   A 39  ? 0.1903 0.1198 0.1874 0.0017  -0.0240 -0.0050 39  SER   A N   
261  C CA  . SER   A 39  ? 0.2295 0.1503 0.1724 0.0195  -0.0127 0.0152  39  SER   A CA  
262  C C   . SER   A 39  ? 0.1905 0.1906 0.1777 0.0060  -0.0014 0.0018  39  SER   A C   
263  O O   . SER   A 39  ? 0.1893 0.1598 0.1860 0.0081  -0.0011 -0.0183 39  SER   A O   
264  C CB  . SER   A 39  ? 0.2070 0.1657 0.1844 0.0297  -0.0198 -0.0012 39  SER   A CB  
265  O OG  . SER   A 39  ? 0.2153 0.1752 0.1952 0.0346  -0.0142 0.0000  39  SER   A OG  
266  N N   . TRP   A 40  ? 0.1743 0.1590 0.1769 -0.0048 0.0191  0.0083  40  TRP   A N   
267  C CA  . TRP   A 40  ? 0.1658 0.1671 0.1695 -0.0195 -0.0049 -0.0007 40  TRP   A CA  
268  C C   . TRP   A 40  ? 0.1512 0.1646 0.1696 0.0118  -0.0159 -0.0196 40  TRP   A C   
269  O O   . TRP   A 40  ? 0.1484 0.1826 0.1964 0.0074  -0.0050 -0.0203 40  TRP   A O   
270  C CB  . TRP   A 40  ? 0.1715 0.1686 0.1713 0.0009  -0.0071 -0.0055 40  TRP   A CB  
271  C CG  . TRP   A 40  ? 0.1553 0.1672 0.1689 0.0030  0.0020  -0.0312 40  TRP   A CG  
272  C CD1 . TRP   A 40  ? 0.1912 0.1985 0.1606 -0.0107 -0.0099 -0.0162 40  TRP   A CD1 
273  C CD2 . TRP   A 40  ? 0.1661 0.1772 0.1652 0.0057  0.0113  -0.0222 40  TRP   A CD2 
274  N NE1 . TRP   A 40  ? 0.2068 0.1942 0.1637 -0.0140 -0.0186 -0.0104 40  TRP   A NE1 
275  C CE2 . TRP   A 40  ? 0.1912 0.1729 0.1688 -0.0096 0.0149  -0.0046 40  TRP   A CE2 
276  C CE3 . TRP   A 40  ? 0.1612 0.1814 0.1669 0.0218  0.0109  -0.0107 40  TRP   A CE3 
277  C CZ2 . TRP   A 40  ? 0.1615 0.1981 0.1711 -0.0152 0.0050  0.0061  40  TRP   A CZ2 
278  C CZ3 . TRP   A 40  ? 0.1424 0.2026 0.1612 -0.0015 0.0039  -0.0074 40  TRP   A CZ3 
279  C CH2 . TRP   A 40  ? 0.1647 0.2022 0.1809 -0.0074 -0.0090 -0.0041 40  TRP   A CH2 
280  N N   . VAL   A 41  ? 0.1865 0.1417 0.1652 -0.0146 -0.0142 -0.0125 41  VAL   A N   
281  C CA  . VAL   A 41  ? 0.2115 0.1401 0.1668 0.0100  -0.0425 -0.0147 41  VAL   A CA  
282  C C   . VAL   A 41  ? 0.1709 0.1690 0.1840 -0.0299 -0.0255 -0.0183 41  VAL   A C   
283  O O   . VAL   A 41  ? 0.1923 0.1709 0.2165 -0.0235 -0.0320 -0.0102 41  VAL   A O   
284  C CB  . VAL   A 41  ? 0.2335 0.1934 0.1916 0.0622  -0.0206 0.0101  41  VAL   A CB  
285  C CG1 . VAL   A 41  ? 0.2539 0.1977 0.2018 0.0512  -0.0647 0.0154  41  VAL   A CG1 
286  C CG2 . VAL   A 41  ? 0.2027 0.2213 0.2253 0.0123  -0.0084 0.0085  41  VAL   A CG2 
287  N N   . GLN   A 42  ? 0.1821 0.1504 0.1730 -0.0132 -0.0326 0.0005  42  GLN   A N   
288  C CA  . GLN   A 42  ? 0.1869 0.1610 0.1811 0.0002  -0.0151 0.0079  42  GLN   A CA  
289  C C   . GLN   A 42  ? 0.2008 0.1697 0.1847 0.0209  -0.0215 -0.0097 42  GLN   A C   
290  O O   . GLN   A 42  ? 0.2123 0.1938 0.1923 0.0161  -0.0506 -0.0053 42  GLN   A O   
291  C CB  . GLN   A 42  ? 0.2068 0.2003 0.2130 -0.0207 -0.0010 0.0290  42  GLN   A CB  
292  C CG  . GLN   A 42  ? 0.1896 0.2245 0.2323 -0.0225 -0.0315 0.0265  42  GLN   A CG  
293  C CD  . GLN   A 42  ? 0.1690 0.2472 0.2345 -0.0344 -0.0365 0.0345  42  GLN   A CD  
294  O OE1 . GLN   A 42  ? 0.2347 0.2971 0.2280 -0.0343 -0.0349 0.0455  42  GLN   A OE1 
295  N NE2 . GLN   A 42  ? 0.1883 0.2050 0.2358 0.0036  -0.0350 0.0148  42  GLN   A NE2 
296  N N   . GLU   A 43  ? 0.1527 0.1615 0.1717 0.0068  -0.0061 -0.0182 43  GLU   A N   
297  C CA  . GLU   A 43  ? 0.1663 0.1713 0.1607 0.0023  0.0098  -0.0039 43  GLU   A CA  
298  C C   . GLU   A 43  ? 0.2051 0.1596 0.1810 -0.0139 -0.0134 -0.0117 43  GLU   A C   
299  O O   . GLU   A 43  ? 0.2375 0.1810 0.1904 0.0033  -0.0385 0.0045  43  GLU   A O   
300  C CB  . GLU   A 43  ? 0.2079 0.1896 0.1810 0.0008  0.0056  -0.0457 43  GLU   A CB  
301  C CG  . GLU   A 43  ? 0.2010 0.2550 0.2353 -0.0337 0.0271  -0.0687 43  GLU   A CG  
302  C CD  . GLU   A 43  ? 0.2927 0.3607 0.3009 -0.0693 0.0653  -0.1227 43  GLU   A CD  
303  O OE1 . GLU   A 43  ? 0.2580 0.3827 0.3294 -0.0482 0.0454  -0.1347 43  GLU   A OE1 
304  O OE2 . GLU   A 43  ? 0.3391 0.4268 0.3339 -0.1057 0.1083  -0.1484 43  GLU   A OE2 
305  N N   . LYS   A 44  ? 0.2464 0.1554 0.1794 -0.0123 -0.0385 0.0109  44  LYS   A N   
306  C CA  . LYS   A 44  ? 0.2425 0.1899 0.2013 -0.0023 0.0433  -0.0028 44  LYS   A CA  
307  C C   . LYS   A 44  ? 0.2758 0.2021 0.2306 0.0064  0.0181  0.0012  44  LYS   A C   
308  O O   . LYS   A 44  ? 0.2835 0.1993 0.2366 0.0147  0.0132  -0.0044 44  LYS   A O   
309  C CB  . LYS   A 44  ? 0.2464 0.2202 0.2102 -0.0417 0.0619  -0.0401 44  LYS   A CB  
310  C CG  . LYS   A 44  ? 0.3219 0.2505 0.2265 -0.0441 0.0518  -0.0600 44  LYS   A CG  
311  C CD  . LYS   A 44  ? 0.3473 0.2263 0.2357 -0.0801 0.0551  -0.0635 44  LYS   A CD  
312  C CE  . LYS   A 44  ? 0.2861 0.2477 0.2291 -0.0368 0.0167  -0.0583 44  LYS   A CE  
313  N NZ  . LYS   A 44  ? 0.2008 0.2405 0.2449 -0.0344 0.0127  -0.0475 44  LYS   A NZ  
314  N N   . PRO   A 45  ? 0.2923 0.1576 0.2629 0.0149  0.0125  0.0032  45  PRO   A N   
315  C CA  . PRO   A 45  ? 0.2867 0.1875 0.3026 0.0221  0.0466  0.0100  45  PRO   A CA  
316  C C   . PRO   A 45  ? 0.3411 0.2350 0.3658 0.0360  0.0040  -0.0023 45  PRO   A C   
317  O O   . PRO   A 45  ? 0.3902 0.2854 0.3608 0.0366  -0.0850 -0.0178 45  PRO   A O   
318  C CB  . PRO   A 45  ? 0.3109 0.1981 0.2859 0.0377  0.0436  -0.0029 45  PRO   A CB  
319  C CG  . PRO   A 45  ? 0.3173 0.2013 0.2695 0.0437  -0.0207 0.0307  45  PRO   A CG  
320  C CD  . PRO   A 45  ? 0.3094 0.1845 0.2666 0.0148  -0.0289 0.0456  45  PRO   A CD  
321  N N   . ASP   A 46  ? 0.5187 0.2444 0.4159 0.0727  0.0223  -0.0139 46  ASP   A N   
322  C CA  . ASP   A 46  ? 0.5806 0.3610 0.4768 0.0642  0.0250  0.0251  46  ASP   A CA  
323  C C   . ASP   A 46  ? 0.5172 0.3125 0.4072 0.0883  0.0865  0.0432  46  ASP   A C   
324  O O   . ASP   A 46  ? 0.6200 0.3615 0.4113 0.1714  0.0719  0.0634  46  ASP   A O   
325  C CB  . ASP   A 46  ? 0.6307 0.5268 0.5927 0.0322  0.0064  0.0102  46  ASP   A CB  
326  C CG  . ASP   A 46  ? 0.7303 0.6912 0.6930 0.0006  -0.0057 -0.0362 46  ASP   A CG  
327  O OD1 . ASP   A 46  ? 0.7314 0.6915 0.6985 0.0274  -0.0087 -0.0614 46  ASP   A OD1 
328  O OD2 . ASP   A 46  ? 0.8405 0.7859 0.7568 -0.0111 -0.0135 -0.0534 46  ASP   A OD2 
329  N N   . HIS   A 47  ? 0.4029 0.2687 0.3344 0.0291  0.0837  0.0277  47  HIS   A N   
330  C CA  A HIS   A 47  ? 0.3706 0.2507 0.2963 0.0151  0.0720  0.0230  47  HIS   A CA  
331  C CA  B HIS   A 47  ? 0.3783 0.2738 0.3097 0.0199  0.0574  0.0267  47  HIS   A CA  
332  C C   . HIS   A 47  ? 0.4444 0.2354 0.2674 0.0199  0.0299  0.0186  47  HIS   A C   
333  O O   . HIS   A 47  ? 0.6034 0.2186 0.2361 0.0705  0.0389  -0.0427 47  HIS   A O   
334  C CB  A HIS   A 47  ? 0.3438 0.2510 0.2798 0.0497  0.0293  0.0056  47  HIS   A CB  
335  C CB  B HIS   A 47  ? 0.3537 0.3123 0.3224 0.0472  0.0211  0.0226  47  HIS   A CB  
336  C CG  A HIS   A 47  ? 0.3152 0.2085 0.2493 0.0262  0.0222  -0.0043 47  HIS   A CG  
337  C CG  B HIS   A 47  ? 0.3383 0.3218 0.3265 0.0462  0.0130  0.0258  47  HIS   A CG  
338  N ND1 A HIS   A 47  ? 0.3407 0.2170 0.2516 0.0383  -0.0046 -0.0292 47  HIS   A ND1 
339  N ND1 B HIS   A 47  ? 0.3395 0.3415 0.3312 0.0514  0.0148  0.0325  47  HIS   A ND1 
340  C CD2 A HIS   A 47  ? 0.2665 0.2644 0.2350 0.0306  0.0048  0.0027  47  HIS   A CD2 
341  C CD2 B HIS   A 47  ? 0.3588 0.3453 0.3318 0.0050  0.0028  0.0259  47  HIS   A CD2 
342  C CE1 A HIS   A 47  ? 0.3199 0.2703 0.2386 0.0210  0.0101  -0.0130 47  HIS   A CE1 
343  C CE1 B HIS   A 47  ? 0.3641 0.3382 0.3332 0.0310  0.0145  0.0266  47  HIS   A CE1 
344  N NE2 A HIS   A 47  ? 0.3352 0.2788 0.2312 0.0171  0.0279  -0.0106 47  HIS   A NE2 
345  N NE2 B HIS   A 47  ? 0.3739 0.3474 0.3328 0.0241  0.0060  0.0295  47  HIS   A NE2 
346  N N   . LEU   A 48  ? 0.3883 0.2173 0.2217 -0.0205 0.0229  -0.0059 48  LEU   A N   
347  C CA  . LEU   A 48  ? 0.3530 0.2058 0.2287 -0.0512 -0.0518 0.0026  48  LEU   A CA  
348  C C   . LEU   A 48  ? 0.2662 0.2064 0.2036 -0.0198 -0.0573 0.0014  48  LEU   A C   
349  O O   . LEU   A 48  ? 0.2386 0.1823 0.1927 -0.0065 -0.0550 0.0016  48  LEU   A O   
350  C CB  . LEU   A 48  ? 0.4185 0.2365 0.2829 -0.0891 -0.0908 -0.0207 48  LEU   A CB  
351  C CG  . LEU   A 48  ? 0.4564 0.3367 0.3624 -0.0807 -0.0770 0.0171  48  LEU   A CG  
352  C CD1 . LEU   A 48  ? 0.3615 0.3165 0.3879 -0.0798 -0.0514 0.0295  48  LEU   A CD1 
353  C CD2 . LEU   A 48  ? 0.5634 0.4403 0.4171 -0.0600 -0.0668 0.0088  48  LEU   A CD2 
354  N N   . PHE   A 49  ? 0.2211 0.1542 0.2159 -0.0144 -0.0256 0.0067  49  PHE   A N   
355  C CA  . PHE   A 49  ? 0.1982 0.1721 0.2176 -0.0158 -0.0232 -0.0026 49  PHE   A CA  
356  C C   . PHE   A 49  ? 0.1762 0.1916 0.2376 -0.0019 -0.0227 -0.0236 49  PHE   A C   
357  O O   . PHE   A 49  ? 0.1901 0.2452 0.2594 -0.0018 -0.0725 -0.0059 49  PHE   A O   
358  C CB  . PHE   A 49  ? 0.2123 0.1691 0.2300 -0.0022 -0.0652 0.0126  49  PHE   A CB  
359  C CG  . PHE   A 49  ? 0.2228 0.2426 0.2446 0.0243  -0.0731 0.0272  49  PHE   A CG  
360  C CD1 . PHE   A 49  ? 0.2588 0.2834 0.2779 0.0056  -0.0385 0.0347  49  PHE   A CD1 
361  C CD2 . PHE   A 49  ? 0.2053 0.2862 0.2643 0.0185  -0.0969 0.0204  49  PHE   A CD2 
362  C CE1 . PHE   A 49  ? 0.2276 0.3203 0.2942 -0.0090 -0.0169 0.0216  49  PHE   A CE1 
363  C CE2 . PHE   A 49  ? 0.2235 0.2948 0.2846 0.0269  -0.0294 0.0478  49  PHE   A CE2 
364  C CZ  . PHE   A 49  ? 0.2223 0.2900 0.2918 0.0355  0.0078  0.0248  49  PHE   A CZ  
365  N N   . THR   A 50  ? 0.1742 0.2204 0.2438 0.0157  -0.0235 -0.0354 50  THR   A N   
366  C CA  . THR   A 50  ? 0.2142 0.2478 0.3031 0.0303  0.0549  -0.0556 50  THR   A CA  
367  C C   . THR   A 50  ? 0.2044 0.1955 0.2628 0.0535  0.0137  -0.0151 50  THR   A C   
368  O O   . THR   A 50  ? 0.1890 0.2226 0.2759 0.0147  -0.0522 0.0099  50  THR   A O   
369  C CB  . THR   A 50  ? 0.2829 0.3423 0.4116 -0.0694 0.1015  -0.0928 50  THR   A CB  
370  O OG1 . THR   A 50  ? 0.4294 0.4134 0.4511 -0.0204 0.1161  -0.0715 50  THR   A OG1 
371  C CG2 . THR   A 50  ? 0.3781 0.3971 0.4597 -0.1158 0.0842  -0.0926 50  THR   A CG2 
372  N N   . GLY   A 51  ? 0.2099 0.2102 0.2072 0.0257  -0.0065 -0.0007 51  GLY   A N   
373  C CA  . GLY   A 51  ? 0.2494 0.2229 0.1833 0.0286  0.0384  -0.0062 51  GLY   A CA  
374  C C   . GLY   A 51  ? 0.1381 0.2494 0.1925 0.0120  0.0047  0.0056  51  GLY   A C   
375  O O   . GLY   A 51  ? 0.1915 0.3723 0.2241 -0.0222 0.0186  -0.0048 51  GLY   A O   
376  N N   . LEU   A 52  ? 0.1971 0.1904 0.1829 0.0179  0.0065  0.0250  52  LEU   A N   
377  C CA  . LEU   A 52  ? 0.1983 0.1845 0.1944 0.0645  0.0084  0.0335  52  LEU   A CA  
378  C C   . LEU   A 52  ? 0.1719 0.1846 0.2125 0.0492  0.0160  0.0081  52  LEU   A C   
379  O O   . LEU   A 52  ? 0.1817 0.1923 0.2052 0.0211  0.0183  0.0029  52  LEU   A O   
380  C CB  . LEU   A 52  ? 0.2287 0.1810 0.2125 0.0480  -0.0575 -0.0029 52  LEU   A CB  
381  C CG  . LEU   A 52  ? 0.2631 0.1558 0.2286 0.0416  -0.0439 -0.0126 52  LEU   A CG  
382  C CD1 . LEU   A 52  ? 0.3675 0.2355 0.2234 0.1250  -0.0518 0.0209  52  LEU   A CD1 
383  C CD2 . LEU   A 52  ? 0.2948 0.1701 0.2802 0.0041  0.0148  -0.0340 52  LEU   A CD2 
384  N N   . ILE   A 53  ? 0.1996 0.1807 0.2204 0.0015  0.0090  -0.0007 53  ILE   A N   
385  C CA  . ILE   A 53  ? 0.1844 0.1688 0.2096 0.0112  0.0045  -0.0021 53  ILE   A CA  
386  C C   . ILE   A 53  ? 0.1778 0.1708 0.2123 0.0290  0.0008  -0.0014 53  ILE   A C   
387  O O   . ILE   A 53  ? 0.1862 0.1929 0.2227 0.0227  0.0098  0.0020  53  ILE   A O   
388  C CB  . ILE   A 53  ? 0.2174 0.1943 0.2038 -0.0054 -0.0279 0.0048  53  ILE   A CB  
389  C CG1 . ILE   A 53  ? 0.2098 0.2487 0.2027 0.0405  0.0193  0.0287  53  ILE   A CG1 
390  C CG2 . ILE   A 53  ? 0.2671 0.2130 0.2117 0.0050  -0.0497 -0.0253 53  ILE   A CG2 
391  C CD1 . ILE   A 53  ? 0.2673 0.3128 0.2193 0.0519  0.0274  0.0179  53  ILE   A CD1 
392  N N   . GLY   A 54  ? 0.1815 0.1790 0.2270 0.0161  0.0025  0.0129  54  GLY   A N   
393  C CA  . GLY   A 54  ? 0.2235 0.1587 0.2363 0.0159  0.0316  0.0046  54  GLY   A CA  
394  C C   . GLY   A 54  ? 0.2306 0.1539 0.2420 0.0244  0.0142  -0.0097 54  GLY   A C   
395  O O   . GLY   A 54  ? 0.1827 0.2034 0.2253 0.0152  0.0290  0.0012  54  GLY   A O   
396  N N   . GLY   A 55  ? 0.2054 0.1552 0.2331 0.0263  -0.0286 -0.0320 55  GLY   A N   
397  C CA  . GLY   A 55  ? 0.2072 0.1898 0.2395 0.0363  -0.0273 -0.0260 55  GLY   A CA  
398  C C   . GLY   A 55  ? 0.2180 0.2125 0.2208 0.0159  0.0130  0.0035  55  GLY   A C   
399  O O   . GLY   A 55  ? 0.2679 0.2050 0.2156 0.0609  0.0275  -0.0100 55  GLY   A O   
400  N N   . ASN   A 56  ? 0.2040 0.2038 0.2265 0.0199  -0.0114 -0.0085 56  ASN   A N   
401  C CA  . ASN   A 56  ? 0.2057 0.2007 0.2317 0.0059  0.0105  -0.0324 56  ASN   A CA  
402  C C   . ASN   A 56  ? 0.2091 0.1722 0.2244 0.0368  0.0274  -0.0285 56  ASN   A C   
403  O O   . ASN   A 56  ? 0.2130 0.2120 0.2285 0.0424  0.0120  0.0021  56  ASN   A O   
404  C CB  . ASN   A 56  ? 0.2410 0.2223 0.2277 0.0036  0.0276  -0.0558 56  ASN   A CB  
405  C CG  . ASN   A 56  ? 0.2356 0.2225 0.2397 -0.0305 -0.0020 -0.0541 56  ASN   A CG  
406  O OD1 . ASN   A 56  ? 0.2396 0.2649 0.2287 -0.0070 0.0181  -0.0686 56  ASN   A OD1 
407  N ND2 . ASN   A 56  ? 0.2871 0.2249 0.2544 -0.0263 -0.0220 -0.0504 56  ASN   A ND2 
408  N N   . LYS   A 57  ? 0.1953 0.2309 0.2416 0.0320  0.0282  -0.0128 57  LYS   A N   
409  C CA  . LYS   A 57  ? 0.2200 0.2453 0.2727 0.0249  0.0553  0.0005  57  LYS   A CA  
410  C C   . LYS   A 57  ? 0.2410 0.2470 0.2928 0.0406  0.0764  0.0342  57  LYS   A C   
411  O O   . LYS   A 57  ? 0.2640 0.2839 0.3164 0.0495  0.0609  0.0525  57  LYS   A O   
412  C CB  . LYS   A 57  ? 0.3126 0.2651 0.3172 0.0753  0.0212  0.0105  57  LYS   A CB  
413  C CG  . LYS   A 57  ? 0.3655 0.3027 0.3756 0.1419  -0.0013 0.0075  57  LYS   A CG  
414  C CD  . LYS   A 57  ? 0.5297 0.4108 0.4450 0.1095  -0.0315 -0.0008 57  LYS   A CD  
415  C CE  . LYS   A 57  ? 0.5622 0.4735 0.4957 0.1138  -0.0247 -0.0279 57  LYS   A CE  
416  N NZ  . LYS   A 57  ? 0.6000 0.5031 0.5214 0.1145  0.0105  -0.0534 57  LYS   A NZ  
417  N N   . ASN   A 58  ? 0.2197 0.2109 0.2993 0.0312  0.0708  0.0195  58  ASN   A N   
418  C CA  . ASN   A 58  ? 0.2267 0.2277 0.3200 0.0069  0.0625  0.0217  58  ASN   A CA  
419  C C   . ASN   A 58  ? 0.1641 0.2226 0.3079 0.0272  0.0435  0.0233  58  ASN   A C   
420  O O   . ASN   A 58  ? 0.2015 0.2335 0.2826 0.0176  0.0544  0.0162  58  ASN   A O   
421  C CB  . ASN   A 58  ? 0.2500 0.2361 0.3414 0.0664  0.0275  0.0161  58  ASN   A CB  
422  C CG  . ASN   A 58  ? 0.2765 0.2796 0.3774 0.0507  0.0205  0.0269  58  ASN   A CG  
423  O OD1 . ASN   A 58  ? 0.3720 0.3138 0.3946 0.0537  0.0404  0.0119  58  ASN   A OD1 
424  N ND2 . ASN   A 58  ? 0.2845 0.2835 0.3784 0.0263  0.0305  0.0088  58  ASN   A ND2 
425  N N   . ARG   A 59  ? 0.1909 0.2271 0.3331 -0.0110 0.0317  0.0369  59  ARG   A N   
426  C CA  . ARG   A 59  ? 0.2862 0.2548 0.3655 -0.0047 0.0298  0.0188  59  ARG   A CA  
427  C C   . ARG   A 59  ? 0.2892 0.3020 0.4058 -0.0114 0.0034  0.0156  59  ARG   A C   
428  O O   . ARG   A 59  ? 0.2478 0.3462 0.4531 0.0493  0.0101  0.0041  59  ARG   A O   
429  C CB  . ARG   A 59  ? 0.2351 0.2738 0.3653 -0.0374 0.0886  0.0179  59  ARG   A CB  
430  C CG  . ARG   A 59  ? 0.2691 0.3009 0.3494 -0.0093 0.0606  0.0321  59  ARG   A CG  
431  C CD  . ARG   A 59  ? 0.2840 0.3208 0.3292 -0.0276 -0.0011 0.0716  59  ARG   A CD  
432  N NE  . ARG   A 59  ? 0.3253 0.2971 0.3369 -0.0076 0.0342  0.0738  59  ARG   A NE  
433  C CZ  . ARG   A 59  ? 0.3194 0.2735 0.3470 0.0608  0.0028  0.0439  59  ARG   A CZ  
434  N NH1 . ARG   A 59  ? 0.2868 0.2956 0.3649 0.0939  -0.0258 0.0464  59  ARG   A NH1 
435  N NH2 . ARG   A 59  ? 0.3081 0.2699 0.3418 -0.0058 -0.0004 0.0051  59  ARG   A NH2 
436  N N   . ALA   A 60  ? 0.2421 0.2974 0.3824 -0.0442 0.0143  0.0538  60  ALA   A N   
437  C CA  . ALA   A 60  ? 0.3017 0.3412 0.3853 -0.0419 0.0027  0.0687  60  ALA   A CA  
438  C C   . ALA   A 60  ? 0.3390 0.3649 0.3956 0.0160  -0.0658 0.0976  60  ALA   A C   
439  O O   . ALA   A 60  ? 0.2310 0.3218 0.3989 -0.0114 -0.0724 0.1047  60  ALA   A O   
440  C CB  . ALA   A 60  ? 0.2974 0.3380 0.3718 -0.0449 0.0727  0.0798  60  ALA   A CB  
441  N N   . PRO   A 61  ? 0.4037 0.4161 0.4021 0.0460  -0.0943 0.1371  61  PRO   A N   
442  C CA  . PRO   A 61  ? 0.3403 0.4637 0.4066 0.0271  -0.0951 0.1384  61  PRO   A CA  
443  C C   . PRO   A 61  ? 0.3096 0.4585 0.3942 -0.0169 -0.1067 0.1505  61  PRO   A C   
444  O O   . PRO   A 61  ? 0.4084 0.4883 0.3918 -0.0742 -0.1303 0.1350  61  PRO   A O   
445  C CB  . PRO   A 61  ? 0.3798 0.4914 0.4145 0.0529  -0.0617 0.1291  61  PRO   A CB  
446  C CG  . PRO   A 61  ? 0.4821 0.4911 0.4230 0.0384  -0.0537 0.1279  61  PRO   A CG  
447  C CD  . PRO   A 61  ? 0.4568 0.4528 0.4068 0.0322  -0.0814 0.1440  61  PRO   A CD  
448  N N   . GLY   A 62  ? 0.2731 0.4317 0.3877 0.0155  -0.1072 0.1724  62  GLY   A N   
449  C CA  . GLY   A 62  ? 0.2614 0.4018 0.3806 -0.0114 -0.0900 0.1312  62  GLY   A CA  
450  C C   . GLY   A 62  ? 0.2303 0.3577 0.3476 -0.0395 -0.0946 0.1196  62  GLY   A C   
451  O O   . GLY   A 62  ? 0.3077 0.3749 0.3859 -0.0695 -0.1276 0.1042  62  GLY   A O   
452  N N   . VAL   A 63  ? 0.1935 0.3248 0.2825 -0.0014 -0.0547 0.1025  63  VAL   A N   
453  C CA  . VAL   A 63  ? 0.1860 0.2979 0.2399 0.0115  -0.0248 0.0821  63  VAL   A CA  
454  C C   . VAL   A 63  ? 0.1249 0.2795 0.2337 -0.0143 0.0014  0.0619  63  VAL   A C   
455  O O   . VAL   A 63  ? 0.1562 0.3364 0.2408 0.0259  0.0046  0.0397  63  VAL   A O   
456  C CB  . VAL   A 63  ? 0.1906 0.3253 0.2267 -0.0477 -0.0214 0.0643  63  VAL   A CB  
457  C CG1 . VAL   A 63  ? 0.2059 0.3073 0.2365 -0.0074 -0.0177 0.0300  63  VAL   A CG1 
458  C CG2 . VAL   A 63  ? 0.2169 0.3514 0.2206 -0.0048 0.0032  0.0819  63  VAL   A CG2 
459  N N   . PRO   A 64  ? 0.1531 0.2331 0.2099 0.0164  0.0132  0.0426  64  PRO   A N   
460  C CA  . PRO   A 64  ? 0.1788 0.2399 0.1897 -0.0081 -0.0039 0.0286  64  PRO   A CA  
461  C C   . PRO   A 64  ? 0.1682 0.2380 0.1794 0.0186  0.0095  0.0135  64  PRO   A C   
462  O O   . PRO   A 64  ? 0.1431 0.2636 0.1778 -0.0207 0.0050  0.0155  64  PRO   A O   
463  C CB  . PRO   A 64  ? 0.2417 0.2325 0.1936 -0.0071 -0.0361 0.0007  64  PRO   A CB  
464  C CG  . PRO   A 64  ? 0.2504 0.2460 0.1889 -0.0021 -0.0092 0.0053  64  PRO   A CG  
465  C CD  . PRO   A 64  ? 0.2237 0.2159 0.1886 0.0334  0.0121  0.0386  64  PRO   A CD  
466  N N   . ALA   A 65  ? 0.1423 0.2301 0.1744 0.0155  0.0251  0.0330  65  ALA   A N   
467  C CA  . ALA   A 65  ? 0.1504 0.2395 0.2083 0.0164  0.0066  -0.0022 65  ALA   A CA  
468  C C   . ALA   A 65  ? 0.1336 0.1960 0.2031 0.0153  0.0008  0.0144  65  ALA   A C   
469  O O   . ALA   A 65  ? 0.1489 0.1958 0.2133 -0.0051 0.0240  -0.0039 65  ALA   A O   
470  C CB  . ALA   A 65  ? 0.1711 0.2853 0.2264 0.0097  -0.0171 -0.0265 65  ALA   A CB  
471  N N   . ARG   A 66  ? 0.1000 0.2300 0.2013 0.0177  0.0337  0.0195  66  ARG   A N   
472  C CA  . ARG   A 66  ? 0.1181 0.2012 0.1945 0.0091  0.0274  0.0401  66  ARG   A CA  
473  C C   . ARG   A 66  ? 0.1160 0.1832 0.1918 0.0104  0.0070  -0.0053 66  ARG   A C   
474  O O   . ARG   A 66  ? 0.1238 0.2240 0.1831 0.0034  -0.0044 0.0279  66  ARG   A O   
475  C CB  . ARG   A 66  ? 0.1511 0.1958 0.1747 0.0025  0.0319  0.0371  66  ARG   A CB  
476  C CG  . ARG   A 66  ? 0.1465 0.2070 0.1704 -0.0090 0.0008  0.0189  66  ARG   A CG  
477  C CD  . ARG   A 66  ? 0.1638 0.1843 0.1630 0.0082  -0.0115 0.0220  66  ARG   A CD  
478  N NE  . ARG   A 66  ? 0.1642 0.1847 0.1899 -0.0465 -0.0274 0.0104  66  ARG   A NE  
479  C CZ  . ARG   A 66  ? 0.1342 0.2084 0.2084 -0.0452 0.0017  0.0216  66  ARG   A CZ  
480  N NH1 . ARG   A 66  ? 0.1341 0.2150 0.2317 -0.0102 0.0177  0.0629  66  ARG   A NH1 
481  N NH2 . ARG   A 66  ? 0.1922 0.2166 0.1940 -0.0463 0.0118  0.0159  66  ARG   A NH2 
482  N N   . PHE   A 67  ? 0.1840 0.1708 0.1863 -0.0016 0.0024  0.0092  67  PHE   A N   
483  C CA  . PHE   A 67  ? 0.1583 0.1809 0.1764 -0.0229 -0.0115 0.0317  67  PHE   A CA  
484  C C   . PHE   A 67  ? 0.1306 0.1864 0.1985 -0.0304 -0.0173 0.0162  67  PHE   A C   
485  O O   . PHE   A 67  ? 0.1392 0.2474 0.2273 0.0228  -0.0012 0.0184  67  PHE   A O   
486  C CB  . PHE   A 67  ? 0.1949 0.1808 0.1700 0.0175  0.0011  0.0157  67  PHE   A CB  
487  C CG  . PHE   A 67  ? 0.1877 0.1700 0.1727 0.0079  0.0027  0.0171  67  PHE   A CG  
488  C CD1 . PHE   A 67  ? 0.1958 0.1992 0.1819 0.0597  -0.0104 0.0283  67  PHE   A CD1 
489  C CD2 . PHE   A 67  ? 0.2311 0.1962 0.1608 0.0027  -0.0040 -0.0028 67  PHE   A CD2 
490  C CE1 . PHE   A 67  ? 0.2268 0.2293 0.1700 -0.0064 -0.0121 0.0050  67  PHE   A CE1 
491  C CE2 . PHE   A 67  ? 0.2456 0.2020 0.1665 0.0142  0.0051  -0.0023 67  PHE   A CE2 
492  C CZ  . PHE   A 67  ? 0.2047 0.2287 0.1624 -0.0042 -0.0054 0.0027  67  PHE   A CZ  
493  N N   . SER   A 68  ? 0.1309 0.1761 0.1988 -0.0135 -0.0038 -0.0064 68  SER   A N   
494  C CA  . SER   A 68  ? 0.1720 0.1798 0.2161 0.0164  0.0002  -0.0230 68  SER   A CA  
495  C C   . SER   A 68  ? 0.1681 0.1641 0.2250 0.0048  0.0182  -0.0003 68  SER   A C   
496  O O   . SER   A 68  ? 0.1466 0.1749 0.2618 0.0080  0.0069  0.0021  68  SER   A O   
497  C CB  . SER   A 68  ? 0.1921 0.2612 0.2210 0.0306  -0.0223 -0.0045 68  SER   A CB  
498  O OG  . SER   A 68  ? 0.2351 0.2774 0.2387 0.0443  -0.0014 -0.0095 68  SER   A OG  
499  N N   . GLY   A 69  ? 0.1701 0.2075 0.2304 -0.0257 0.0559  0.0118  69  GLY   A N   
500  C CA  . GLY   A 69  ? 0.1825 0.1967 0.2442 -0.0218 0.0502  0.0063  69  GLY   A CA  
501  C C   . GLY   A 69  ? 0.1803 0.1795 0.2310 -0.0150 0.0000  0.0153  69  GLY   A C   
502  O O   . GLY   A 69  ? 0.2053 0.2193 0.2598 0.0413  0.0047  -0.0086 69  GLY   A O   
503  N N   . SER   A 70  ? 0.2142 0.1934 0.2134 0.0001  0.0507  0.0128  70  SER   A N   
504  C CA  . SER   A 70  ? 0.2208 0.2469 0.2586 0.0215  0.0422  -0.0192 70  SER   A CA  
505  C C   . SER   A 70  ? 0.2433 0.2002 0.2624 0.0218  0.0092  -0.0398 70  SER   A C   
506  O O   . SER   A 70  ? 0.2146 0.1770 0.2855 0.0304  0.0213  -0.0131 70  SER   A O   
507  C CB  . SER   A 70  ? 0.2961 0.3904 0.2983 0.0398  0.0745  0.0042  70  SER   A CB  
508  O OG  . SER   A 70  ? 0.3741 0.4970 0.3206 0.0380  0.0729  0.0183  70  SER   A OG  
509  N N   . LEU   A 71  ? 0.2606 0.1884 0.2396 -0.0035 -0.0105 -0.0449 71  LEU   A N   
510  C CA  . LEU   A 71  ? 0.3348 0.1913 0.2074 0.0026  -0.0110 -0.0143 71  LEU   A CA  
511  C C   . LEU   A 71  ? 0.3155 0.2256 0.2018 0.0547  -0.0073 -0.0249 71  LEU   A C   
512  O O   . LEU   A 71  ? 0.3506 0.2455 0.2184 0.0557  0.0057  -0.0290 71  LEU   A O   
513  C CB  . LEU   A 71  ? 0.3768 0.1850 0.1946 0.0303  -0.0180 -0.0173 71  LEU   A CB  
514  C CG  . LEU   A 71  ? 0.4019 0.2034 0.1969 0.0047  -0.0423 -0.0042 71  LEU   A CG  
515  C CD1 . LEU   A 71  ? 0.4649 0.2220 0.2127 -0.0124 -0.0400 0.0230  71  LEU   A CD1 
516  C CD2 . LEU   A 71  ? 0.3021 0.2250 0.1931 0.0293  -0.0099 -0.0109 71  LEU   A CD2 
517  N N   . ILE   A 72  ? 0.3186 0.2426 0.2018 0.0272  -0.0490 -0.0170 72  ILE   A N   
518  C CA  . ILE   A 72  ? 0.3326 0.2948 0.2250 0.0286  -0.0338 -0.0265 72  ILE   A CA  
519  C C   . ILE   A 72  ? 0.2481 0.2937 0.2349 -0.0015 -0.0636 -0.0757 72  ILE   A C   
520  O O   . ILE   A 72  ? 0.2801 0.3192 0.2431 0.0347  -0.0084 -0.0922 72  ILE   A O   
521  C CB  . ILE   A 72  ? 0.3415 0.3756 0.2692 0.0189  -0.0117 0.0560  72  ILE   A CB  
522  C CG1 . ILE   A 72  ? 0.4061 0.3877 0.3135 0.0161  0.0053  0.0832  72  ILE   A CG1 
523  C CG2 . ILE   A 72  ? 0.3842 0.4267 0.2895 0.0608  0.0120  0.0788  72  ILE   A CG2 
524  C CD1 . ILE   A 72  ? 0.4261 0.3906 0.3310 0.0072  0.0239  0.1065  72  ILE   A CD1 
525  N N   . GLY   A 73  ? 0.2079 0.3673 0.2632 0.0362  -0.0863 -0.0628 73  GLY   A N   
526  C CA  . GLY   A 73  ? 0.3547 0.3809 0.2904 0.0061  -0.0420 -0.0451 73  GLY   A CA  
527  C C   . GLY   A 73  ? 0.3620 0.3393 0.3005 -0.0390 -0.0243 -0.0474 73  GLY   A C   
528  O O   . GLY   A 73  ? 0.2964 0.3324 0.3115 -0.0254 -0.0345 -0.0334 73  GLY   A O   
529  N N   . ASP   A 74  ? 0.4316 0.3123 0.2981 -0.1048 -0.0432 -0.0595 74  ASP   A N   
530  C CA  . ASP   A 74  ? 0.4055 0.3245 0.3129 -0.0924 -0.0098 -0.0796 74  ASP   A CA  
531  C C   . ASP   A 74  ? 0.2928 0.2783 0.2760 -0.0300 -0.0156 -0.0756 74  ASP   A C   
532  O O   . ASP   A 74  ? 0.2768 0.2619 0.2494 -0.0066 -0.0305 -0.0394 74  ASP   A O   
533  C CB  . ASP   A 74  ? 0.4658 0.3833 0.3701 -0.0752 0.0093  -0.0819 74  ASP   A CB  
534  C CG  . ASP   A 74  ? 0.5583 0.4714 0.4460 -0.0835 -0.0018 -0.0501 74  ASP   A CG  
535  O OD1 . ASP   A 74  ? 0.6103 0.4872 0.4737 -0.1057 0.0006  -0.0396 74  ASP   A OD1 
536  O OD2 . ASP   A 74  ? 0.6106 0.5136 0.4720 -0.0975 -0.0047 -0.0491 74  ASP   A OD2 
537  N N   . LYS   A 75  ? 0.2851 0.2494 0.2605 -0.0117 -0.0271 -0.0885 75  LYS   A N   
538  C CA  . LYS   A 75  ? 0.2224 0.2303 0.2612 -0.0090 -0.0379 -0.0814 75  LYS   A CA  
539  C C   . LYS   A 75  ? 0.2310 0.2245 0.2269 0.0086  -0.0396 -0.0416 75  LYS   A C   
540  O O   . LYS   A 75  ? 0.2740 0.2624 0.2106 0.0095  -0.0251 -0.0491 75  LYS   A O   
541  C CB  . LYS   A 75  ? 0.3040 0.2559 0.3172 0.0232  -0.0780 -0.0899 75  LYS   A CB  
542  C CG  . LYS   A 75  ? 0.3893 0.3201 0.3731 0.0338  -0.0962 -0.0417 75  LYS   A CG  
543  C CD  . LYS   A 75  ? 0.4611 0.4007 0.4203 0.0213  -0.1136 0.0018  75  LYS   A CD  
544  C CE  . LYS   A 75  ? 0.5263 0.4606 0.4562 0.0147  -0.0746 0.0405  75  LYS   A CE  
545  N NZ  . LYS   A 75  ? 0.5584 0.4955 0.4802 0.0324  -0.0453 0.0542  75  LYS   A NZ  
546  N N   . ALA   A 76  ? 0.2260 0.1669 0.1954 -0.0299 -0.0008 -0.0163 76  ALA   A N   
547  C CA  . ALA   A 76  ? 0.2076 0.2125 0.1867 -0.0158 0.0053  -0.0002 76  ALA   A CA  
548  C C   . ALA   A 76  ? 0.1684 0.1936 0.1872 -0.0182 0.0100  -0.0168 76  ALA   A C   
549  O O   . ALA   A 76  ? 0.1852 0.1952 0.2004 0.0063  0.0183  -0.0120 76  ALA   A O   
550  C CB  . ALA   A 76  ? 0.2449 0.2223 0.1831 -0.0075 0.0146  0.0185  76  ALA   A CB  
551  N N   . VAL   A 77  ? 0.2106 0.1808 0.1702 -0.0104 0.0093  -0.0127 77  VAL   A N   
552  C CA  . VAL   A 77  ? 0.1784 0.2061 0.1616 -0.0143 -0.0157 -0.0017 77  VAL   A CA  
553  C C   . VAL   A 77  ? 0.1706 0.1905 0.2138 -0.0056 -0.0127 -0.0155 77  VAL   A C   
554  O O   . VAL   A 77  ? 0.1961 0.2108 0.2930 0.0362  -0.0205 -0.0158 77  VAL   A O   
555  C CB  . VAL   A 77  ? 0.2370 0.2259 0.1618 -0.0006 -0.0129 0.0036  77  VAL   A CB  
556  C CG1 . VAL   A 77  ? 0.2916 0.2465 0.2124 0.0064  0.0615  -0.0078 77  VAL   A CG1 
557  C CG2 . VAL   A 77  ? 0.2301 0.2582 0.1758 -0.0223 -0.0313 0.0017  77  VAL   A CG2 
558  N N   . LEU   A 78  ? 0.1609 0.1640 0.1812 -0.0271 0.0139  -0.0313 78  LEU   A N   
559  C CA  . LEU   A 78  ? 0.1517 0.1675 0.1662 -0.0325 0.0151  -0.0073 78  LEU   A CA  
560  C C   . LEU   A 78  ? 0.1126 0.1888 0.1863 0.0138  0.0268  0.0053  78  LEU   A C   
561  O O   . LEU   A 78  ? 0.1386 0.2029 0.2274 0.0303  0.0089  0.0087  78  LEU   A O   
562  C CB  . LEU   A 78  ? 0.1906 0.1732 0.1695 -0.0278 -0.0089 -0.0322 78  LEU   A CB  
563  C CG  . LEU   A 78  ? 0.1708 0.1781 0.1759 0.0109  -0.0067 -0.0331 78  LEU   A CG  
564  C CD1 . LEU   A 78  ? 0.1924 0.2156 0.2022 0.0320  -0.0480 -0.0314 78  LEU   A CD1 
565  C CD2 . LEU   A 78  ? 0.2487 0.2041 0.1690 0.0173  0.0257  -0.0376 78  LEU   A CD2 
566  N N   . THR   A 79  ? 0.1101 0.1792 0.1952 0.0003  0.0287  0.0035  79  THR   A N   
567  C CA  . THR   A 79  ? 0.1459 0.1742 0.1884 -0.0363 0.0235  0.0059  79  THR   A CA  
568  C C   . THR   A 79  ? 0.1740 0.1625 0.1757 -0.0060 0.0096  0.0156  79  THR   A C   
569  O O   . THR   A 79  ? 0.1472 0.2037 0.1938 0.0194  -0.0336 0.0138  79  THR   A O   
570  C CB  . THR   A 79  ? 0.1978 0.2111 0.1967 -0.0142 0.0170  -0.0136 79  THR   A CB  
571  O OG1 . THR   A 79  ? 0.2599 0.2326 0.2264 -0.0006 0.0098  -0.0344 79  THR   A OG1 
572  C CG2 . THR   A 79  ? 0.2171 0.2527 0.1862 -0.0272 0.0118  -0.0037 79  THR   A CG2 
573  N N   . ILE   A 80  ? 0.1673 0.1582 0.1765 -0.0386 0.0204  -0.0092 80  ILE   A N   
574  C CA  . ILE   A 80  ? 0.1424 0.1605 0.1762 -0.0124 -0.0193 -0.0219 80  ILE   A CA  
575  C C   . ILE   A 80  ? 0.1518 0.2026 0.1652 -0.0132 -0.0101 0.0070  80  ILE   A C   
576  O O   . ILE   A 80  ? 0.1537 0.2237 0.1918 0.0076  -0.0122 0.0344  80  ILE   A O   
577  C CB  . ILE   A 80  ? 0.1866 0.1678 0.1933 -0.0170 -0.0037 -0.0187 80  ILE   A CB  
578  C CG1 . ILE   A 80  ? 0.2030 0.1880 0.1971 0.0332  0.0247  -0.0079 80  ILE   A CG1 
579  C CG2 . ILE   A 80  ? 0.2450 0.1673 0.1951 -0.0216 -0.0260 -0.0354 80  ILE   A CG2 
580  C CD1 . ILE   A 80  ? 0.2278 0.2349 0.2174 0.0609  0.0065  0.0085  80  ILE   A CD1 
581  N N   . THR   A 81  ? 0.1544 0.2255 0.1757 -0.0052 0.0203  0.0174  81  THR   A N   
582  C CA  . THR   A 81  ? 0.2017 0.2104 0.1910 0.0190  0.0328  0.0210  81  THR   A CA  
583  C C   . THR   A 81  ? 0.1955 0.2327 0.1996 -0.0300 0.0261  0.0181  81  THR   A C   
584  O O   . THR   A 81  ? 0.1640 0.2866 0.2210 -0.0121 -0.0017 0.0137  81  THR   A O   
585  C CB  . THR   A 81  ? 0.2570 0.2031 0.2049 0.0155  0.0469  -0.0041 81  THR   A CB  
586  O OG1 . THR   A 81  ? 0.2439 0.2045 0.2201 0.0049  0.0187  -0.0025 81  THR   A OG1 
587  C CG2 . THR   A 81  ? 0.3196 0.2493 0.2121 0.0589  0.0535  -0.0034 81  THR   A CG2 
588  N N   . GLY   A 82  ? 0.1993 0.2213 0.1930 -0.0082 -0.0015 0.0035  82  GLY   A N   
589  C CA  . GLY   A 82  ? 0.1818 0.2070 0.1955 -0.0312 0.0013  0.0065  82  GLY   A CA  
590  C C   . GLY   A 82  ? 0.1623 0.2155 0.1901 -0.0041 0.0314  -0.0010 82  GLY   A C   
591  O O   . GLY   A 82  ? 0.1747 0.2234 0.1979 -0.0131 -0.0001 0.0002  82  GLY   A O   
592  N N   . ALA   A 83  ? 0.1236 0.2105 0.1857 0.0149  0.0391  0.0060  83  ALA   A N   
593  C CA  . ALA   A 83  ? 0.1117 0.2309 0.2153 -0.0115 0.0452  -0.0273 83  ALA   A CA  
594  C C   . ALA   A 83  ? 0.1355 0.2187 0.2056 -0.0030 0.0220  0.0076  83  ALA   A C   
595  O O   . ALA   A 83  ? 0.1694 0.2526 0.2060 0.0133  0.0014  0.0335  83  ALA   A O   
596  C CB  . ALA   A 83  ? 0.1242 0.3072 0.2476 -0.0026 0.0227  -0.0099 83  ALA   A CB  
597  N N   . GLN   A 84  ? 0.1299 0.2063 0.1932 0.0101  -0.0058 0.0051  84  GLN   A N   
598  C CA  . GLN   A 84  ? 0.1384 0.1901 0.1934 0.0087  -0.0193 -0.0043 84  GLN   A CA  
599  C C   . GLN   A 84  ? 0.1466 0.1710 0.1790 -0.0062 -0.0039 -0.0064 84  GLN   A C   
600  O O   . GLN   A 84  ? 0.1479 0.2083 0.1796 -0.0204 -0.0025 0.0147  84  GLN   A O   
601  C CB  . GLN   A 84  ? 0.1834 0.1897 0.1968 -0.0179 -0.0122 -0.0181 84  GLN   A CB  
602  C CG  . GLN   A 84  ? 0.1440 0.2015 0.2032 0.0141  0.0024  -0.0072 84  GLN   A CG  
603  C CD  . GLN   A 84  ? 0.1747 0.1968 0.2081 0.0163  0.0266  0.0101  84  GLN   A CD  
604  O OE1 . GLN   A 84  ? 0.1587 0.2095 0.2214 0.0070  0.0089  0.0180  84  GLN   A OE1 
605  N NE2 . GLN   A 84  ? 0.1618 0.2200 0.2075 -0.0354 0.0180  0.0250  84  GLN   A NE2 
606  N N   . THR   A 85  ? 0.1755 0.1766 0.1982 -0.0124 -0.0069 -0.0057 85  THR   A N   
607  C CA  A THR   A 85  ? 0.2066 0.1781 0.2193 -0.0145 -0.0097 0.0003  85  THR   A CA  
608  C CA  B THR   A 85  ? 0.2030 0.1892 0.2099 -0.0084 -0.0104 0.0027  85  THR   A CA  
609  C C   . THR   A 85  ? 0.1945 0.1974 0.2055 -0.0181 0.0097  0.0003  85  THR   A C   
610  O O   . THR   A 85  ? 0.2021 0.2115 0.1918 -0.0027 0.0220  0.0063  85  THR   A O   
611  C CB  A THR   A 85  ? 0.3180 0.1816 0.2590 -0.0102 -0.0029 0.0061  85  THR   A CB  
612  C CB  B THR   A 85  ? 0.2434 0.1958 0.2254 0.0035  -0.0326 0.0170  85  THR   A CB  
613  O OG1 A THR   A 85  ? 0.4233 0.1994 0.2880 -0.0332 -0.0502 0.0298  85  THR   A OG1 
614  O OG1 B THR   A 85  ? 0.2046 0.1782 0.2264 -0.0093 -0.0609 0.0354  85  THR   A OG1 
615  C CG2 A THR   A 85  ? 0.2711 0.1956 0.2655 -0.0473 0.0724  -0.0063 85  THR   A CG2 
616  C CG2 B THR   A 85  ? 0.2926 0.2173 0.2369 0.0082  -0.0255 0.0172  85  THR   A CG2 
617  N N   . GLU   A 86  ? 0.1890 0.1743 0.1963 -0.0012 -0.0142 -0.0042 86  GLU   A N   
618  C CA  . GLU   A 86  ? 0.1725 0.2150 0.2034 -0.0251 -0.0208 -0.0274 86  GLU   A CA  
619  C C   . GLU   A 86  ? 0.1567 0.1942 0.1868 -0.0331 -0.0011 -0.0376 86  GLU   A C   
620  O O   . GLU   A 86  ? 0.1827 0.2241 0.1801 -0.0158 -0.0140 -0.0006 86  GLU   A O   
621  C CB  . GLU   A 86  ? 0.1688 0.2740 0.2150 -0.0031 -0.0199 -0.0096 86  GLU   A CB  
622  C CG  . GLU   A 86  ? 0.1800 0.2922 0.2183 -0.0174 0.0085  -0.0027 86  GLU   A CG  
623  C CD  . GLU   A 86  ? 0.1626 0.3123 0.2584 0.0198  0.0062  0.0029  86  GLU   A CD  
624  O OE1 . GLU   A 86  ? 0.1619 0.3473 0.2843 0.0029  -0.0118 0.0181  86  GLU   A OE1 
625  O OE2 . GLU   A 86  ? 0.2177 0.3378 0.2852 -0.0214 0.0313  -0.0050 86  GLU   A OE2 
626  N N   . ASP   A 87  ? 0.1594 0.1851 0.1869 -0.0298 -0.0015 -0.0111 87  ASP   A N   
627  C CA  . ASP   A 87  ? 0.1290 0.1789 0.1943 -0.0122 -0.0082 -0.0057 87  ASP   A CA  
628  C C   . ASP   A 87  ? 0.1746 0.1801 0.1951 0.0158  0.0044  -0.0089 87  ASP   A C   
629  O O   . ASP   A 87  ? 0.1496 0.1763 0.1939 -0.0113 0.0039  -0.0014 87  ASP   A O   
630  C CB  . ASP   A 87  ? 0.1334 0.1977 0.1935 -0.0176 0.0086  -0.0228 87  ASP   A CB  
631  C CG  . ASP   A 87  ? 0.1684 0.1967 0.1727 -0.0174 0.0101  0.0098  87  ASP   A CG  
632  O OD1 . ASP   A 87  ? 0.1970 0.2232 0.1835 -0.0050 -0.0048 0.0049  87  ASP   A OD1 
633  O OD2 . ASP   A 87  ? 0.1637 0.2240 0.1571 0.0103  0.0103  0.0129  87  ASP   A OD2 
634  N N   . GLU   A 88  ? 0.1645 0.1526 0.1891 0.0018  0.0082  0.0011  88  GLU   A N   
635  C CA  . GLU   A 88  ? 0.1338 0.1776 0.2097 0.0205  0.0285  -0.0252 88  GLU   A CA  
636  C C   . GLU   A 88  ? 0.1645 0.2058 0.1936 0.0060  0.0199  -0.0138 88  GLU   A C   
637  O O   . GLU   A 88  ? 0.1685 0.2385 0.1881 -0.0379 0.0028  -0.0211 88  GLU   A O   
638  C CB  . GLU   A 88  ? 0.1856 0.1972 0.2658 0.0024  0.0186  -0.0302 88  GLU   A CB  
639  C CG  . GLU   A 88  ? 0.2011 0.2205 0.3108 0.0077  0.0186  -0.0257 88  GLU   A CG  
640  C CD  . GLU   A 88  ? 0.3151 0.2550 0.3505 0.0002  -0.0013 -0.0720 88  GLU   A CD  
641  O OE1 . GLU   A 88  ? 0.3266 0.3116 0.3757 0.0262  -0.0180 -0.0443 88  GLU   A OE1 
642  O OE2 . GLU   A 88  ? 0.4313 0.2871 0.3748 0.0313  -0.0041 -0.0559 88  GLU   A OE2 
643  N N   . ALA   A 89  ? 0.1533 0.1863 0.1844 -0.0025 0.0180  0.0109  89  ALA   A N   
644  C CA  . ALA   A 89  ? 0.1408 0.1659 0.1790 0.0135  -0.0006 -0.0003 89  ALA   A CA  
645  C C   . ALA   A 89  ? 0.1351 0.1672 0.1733 -0.0138 -0.0019 0.0012  89  ALA   A C   
646  O O   . ALA   A 89  ? 0.1737 0.2025 0.1736 0.0022  -0.0272 0.0084  89  ALA   A O   
647  C CB  . ALA   A 89  ? 0.1374 0.2381 0.1838 0.0208  -0.0455 -0.0234 89  ALA   A CB  
648  N N   . ILE   A 90  ? 0.1583 0.1396 0.1805 -0.0064 -0.0175 -0.0040 90  ILE   A N   
649  C CA  . ILE   A 90  ? 0.1590 0.1565 0.1952 0.0063  0.0082  -0.0254 90  ILE   A CA  
650  C C   . ILE   A 90  ? 0.1363 0.1620 0.2118 -0.0057 0.0016  -0.0356 90  ILE   A C   
651  O O   . ILE   A 90  ? 0.2031 0.1976 0.2405 0.0037  -0.0717 -0.0179 90  ILE   A O   
652  C CB  . ILE   A 90  ? 0.1614 0.1991 0.2175 0.0076  0.0238  -0.0228 90  ILE   A CB  
653  C CG1 . ILE   A 90  ? 0.2174 0.2274 0.2372 -0.0155 0.0660  -0.0664 90  ILE   A CG1 
654  C CG2 . ILE   A 90  ? 0.1676 0.2126 0.2228 -0.0115 0.0125  0.0059  90  ILE   A CG2 
655  C CD1 . ILE   A 90  ? 0.3184 0.2852 0.2577 -0.0079 0.0521  -0.0697 90  ILE   A CD1 
656  N N   . TYR   A 91  ? 0.1540 0.1615 0.1934 -0.0215 -0.0073 -0.0163 91  TYR   A N   
657  C CA  . TYR   A 91  ? 0.1694 0.1584 0.1688 0.0171  0.0000  -0.0031 91  TYR   A CA  
658  C C   . TYR   A 91  ? 0.1721 0.1545 0.1666 -0.0052 -0.0272 0.0091  91  TYR   A C   
659  O O   . TYR   A 91  ? 0.1584 0.1835 0.1982 -0.0078 -0.0205 0.0066  91  TYR   A O   
660  C CB  . TYR   A 91  ? 0.1583 0.1695 0.1574 -0.0062 0.0057  0.0029  91  TYR   A CB  
661  C CG  . TYR   A 91  ? 0.1698 0.1504 0.1689 -0.0044 -0.0216 -0.0018 91  TYR   A CG  
662  C CD1 . TYR   A 91  ? 0.1978 0.1429 0.1693 -0.0072 0.0053  0.0025  91  TYR   A CD1 
663  C CD2 . TYR   A 91  ? 0.1691 0.1750 0.1639 -0.0012 -0.0100 0.0043  91  TYR   A CD2 
664  C CE1 . TYR   A 91  ? 0.1565 0.1572 0.1672 -0.0169 -0.0117 0.0037  91  TYR   A CE1 
665  C CE2 . TYR   A 91  ? 0.2199 0.1858 0.1598 -0.0135 -0.0052 0.0168  91  TYR   A CE2 
666  C CZ  . TYR   A 91  ? 0.1502 0.1833 0.1603 -0.0048 0.0088  0.0055  91  TYR   A CZ  
667  O OH  . TYR   A 91  ? 0.1514 0.1936 0.1674 -0.0091 0.0034  0.0034  91  TYR   A OH  
668  N N   . PHE   A 92  ? 0.1491 0.1486 0.1389 -0.0060 0.0095  0.0197  92  PHE   A N   
669  C CA  . PHE   A 92  ? 0.1710 0.1610 0.1659 0.0043  0.0196  -0.0128 92  PHE   A CA  
670  C C   . PHE   A 92  ? 0.1697 0.1690 0.1808 0.0003  -0.0304 -0.0283 92  PHE   A C   
671  O O   . PHE   A 92  ? 0.1704 0.1626 0.2046 0.0011  -0.0167 -0.0091 92  PHE   A O   
672  C CB  . PHE   A 92  ? 0.1996 0.1908 0.1672 0.0083  0.0214  -0.0208 92  PHE   A CB  
673  C CG  . PHE   A 92  ? 0.1750 0.1801 0.1586 0.0278  -0.0136 -0.0295 92  PHE   A CG  
674  C CD1 . PHE   A 92  ? 0.1770 0.2082 0.1634 0.0492  -0.0068 -0.0154 92  PHE   A CD1 
675  C CD2 . PHE   A 92  ? 0.2714 0.1730 0.1543 0.0193  -0.0281 -0.0404 92  PHE   A CD2 
676  C CE1 . PHE   A 92  ? 0.1904 0.2228 0.1852 0.0338  -0.0212 0.0025  92  PHE   A CE1 
677  C CE2 . PHE   A 92  ? 0.2292 0.1804 0.1608 -0.0086 -0.0369 -0.0142 92  PHE   A CE2 
678  C CZ  . PHE   A 92  ? 0.2301 0.2012 0.1751 0.0171  0.0035  -0.0272 92  PHE   A CZ  
679  N N   A CYS   A 93  ? 0.1601 0.1565 0.1858 0.0001  -0.0136 -0.0170 93  CYS   A N   
680  N N   B CYS   A 93  ? 0.1601 0.1565 0.1858 0.0001  -0.0136 -0.0171 93  CYS   A N   
681  C CA  A CYS   A 93  ? 0.1677 0.1629 0.1900 -0.0254 -0.0013 -0.0143 93  CYS   A CA  
682  C CA  B CYS   A 93  ? 0.1677 0.1629 0.1901 -0.0254 -0.0013 -0.0143 93  CYS   A CA  
683  C C   A CYS   A 93  ? 0.2086 0.1763 0.2018 -0.0024 0.0227  -0.0075 93  CYS   A C   
684  C C   B CYS   A 93  ? 0.2086 0.1763 0.2018 -0.0024 0.0226  -0.0075 93  CYS   A C   
685  O O   A CYS   A 93  ? 0.2025 0.1729 0.2231 0.0074  0.0445  -0.0065 93  CYS   A O   
686  O O   B CYS   A 93  ? 0.2025 0.1729 0.2231 0.0074  0.0445  -0.0065 93  CYS   A O   
687  C CB  A CYS   A 93  ? 0.1723 0.1909 0.1968 -0.0302 -0.0147 -0.0107 93  CYS   A CB  
688  C CB  B CYS   A 93  ? 0.1723 0.1909 0.1968 -0.0302 -0.0146 -0.0107 93  CYS   A CB  
689  S SG  A CYS   A 93  ? 0.1772 0.2045 0.2051 -0.0247 -0.0142 -0.0119 93  CYS   A SG  
690  S SG  B CYS   A 93  ? 0.1768 0.2042 0.2049 -0.0246 -0.0143 -0.0118 93  CYS   A SG  
691  N N   . ALA   A 94  ? 0.2075 0.1599 0.1907 -0.0170 0.0139  0.0079  94  ALA   A N   
692  C CA  . ALA   A 94  ? 0.1762 0.1625 0.1964 -0.0212 -0.0043 -0.0046 94  ALA   A CA  
693  C C   . ALA   A 94  ? 0.2018 0.1606 0.1933 0.0100  0.0085  -0.0213 94  ALA   A C   
694  O O   . ALA   A 94  ? 0.1822 0.1655 0.2048 -0.0008 0.0240  -0.0014 94  ALA   A O   
695  C CB  . ALA   A 94  ? 0.2900 0.1842 0.1942 -0.0367 -0.0062 -0.0003 94  ALA   A CB  
696  N N   . LEU   A 95  ? 0.2299 0.1424 0.1778 -0.0390 -0.0044 0.0004  95  LEU   A N   
697  C CA  . LEU   A 95  ? 0.2022 0.1462 0.1775 -0.0147 -0.0289 0.0080  95  LEU   A CA  
698  C C   . LEU   A 95  ? 0.2077 0.1647 0.1906 -0.0130 -0.0214 -0.0060 95  LEU   A C   
699  O O   . LEU   A 95  ? 0.2219 0.1744 0.1876 -0.0115 -0.0072 -0.0001 95  LEU   A O   
700  C CB  . LEU   A 95  ? 0.2345 0.2136 0.1758 -0.0558 -0.0417 0.0160  95  LEU   A CB  
701  C CG  . LEU   A 95  ? 0.2296 0.2344 0.1955 -0.0475 -0.0249 0.0142  95  LEU   A CG  
702  C CD1 . LEU   A 95  ? 0.2399 0.2651 0.2096 -0.0249 -0.0360 0.0055  95  LEU   A CD1 
703  C CD2 . LEU   A 95  ? 0.2199 0.2728 0.2105 -0.0477 -0.0491 0.0157  95  LEU   A CD2 
704  N N   . TRP   A 96  ? 0.2125 0.1637 0.1999 -0.0235 -0.0208 0.0103  96  TRP   A N   
705  C CA  . TRP   A 96  ? 0.2538 0.1598 0.1942 -0.0247 -0.0185 0.0219  96  TRP   A CA  
706  C C   . TRP   A 96  ? 0.2459 0.1711 0.2025 -0.0594 0.0154  0.0103  96  TRP   A C   
707  O O   . TRP   A 96  ? 0.2325 0.2108 0.2007 -0.0261 0.0092  -0.0068 96  TRP   A O   
708  C CB  . TRP   A 96  ? 0.2236 0.1668 0.1817 0.0070  -0.0314 0.0165  96  TRP   A CB  
709  C CG  . TRP   A 96  ? 0.2155 0.1866 0.1916 0.0146  -0.0220 0.0008  96  TRP   A CG  
710  C CD1 . TRP   A 96  ? 0.2721 0.1833 0.1952 0.0205  -0.0101 0.0257  96  TRP   A CD1 
711  C CD2 . TRP   A 96  ? 0.2193 0.1917 0.2004 -0.0068 -0.0166 -0.0138 96  TRP   A CD2 
712  N NE1 . TRP   A 96  ? 0.3085 0.1871 0.1796 0.0170  -0.0149 0.0262  96  TRP   A NE1 
713  C CE2 . TRP   A 96  ? 0.2373 0.1819 0.1957 0.0023  -0.0100 0.0066  96  TRP   A CE2 
714  C CE3 . TRP   A 96  ? 0.1994 0.2206 0.1851 0.0006  -0.0093 -0.0201 96  TRP   A CE3 
715  C CZ2 . TRP   A 96  ? 0.2454 0.2003 0.2103 -0.0036 0.0104  0.0049  96  TRP   A CZ2 
716  C CZ3 . TRP   A 96  ? 0.1326 0.2341 0.1846 0.0243  -0.0272 0.0234  96  TRP   A CZ3 
717  C CH2 . TRP   A 96  ? 0.2166 0.2114 0.1988 0.0287  0.0025  0.0253  96  TRP   A CH2 
718  N N   . TYR   A 97  ? 0.2288 0.2089 0.2122 -0.0607 -0.0078 0.0280  97  TYR   A N   
719  C CA  . TYR   A 97  ? 0.2057 0.2468 0.2320 -0.0652 0.0158  0.0456  97  TYR   A CA  
720  C C   . TYR   A 97  ? 0.2431 0.2530 0.2576 -0.0663 0.0219  0.0307  97  TYR   A C   
721  O O   . TYR   A 97  ? 0.2942 0.2588 0.2593 -0.0520 0.0180  0.0340  97  TYR   A O   
722  C CB  . TYR   A 97  ? 0.2106 0.2657 0.2199 -0.0325 -0.0015 0.0554  97  TYR   A CB  
723  C CG  . TYR   A 97  ? 0.2398 0.2648 0.2372 -0.0502 0.0099  0.0383  97  TYR   A CG  
724  C CD1 . TYR   A 97  ? 0.2964 0.3113 0.2526 -0.0348 -0.0175 0.0311  97  TYR   A CD1 
725  C CD2 . TYR   A 97  ? 0.3014 0.2758 0.2528 -0.0690 0.0210  0.0456  97  TYR   A CD2 
726  C CE1 . TYR   A 97  ? 0.2668 0.3346 0.2560 -0.0551 -0.0013 0.0399  97  TYR   A CE1 
727  C CE2 . TYR   A 97  ? 0.3101 0.3121 0.2659 -0.1032 0.0337  0.0387  97  TYR   A CE2 
728  C CZ  . TYR   A 97  ? 0.3396 0.3488 0.2709 -0.0539 0.0107  0.0491  97  TYR   A CZ  
729  O OH  . TYR   A 97  ? 0.3598 0.3664 0.2852 -0.0611 0.0222  0.0679  97  TYR   A OH  
730  N N   . SER   A 98  ? 0.3279 0.2379 0.2807 -0.0557 -0.0001 0.0270  98  SER   A N   
731  C CA  . SER   A 98  ? 0.3964 0.2509 0.3058 -0.0946 -0.0537 0.0178  98  SER   A CA  
732  C C   . SER   A 98  ? 0.3068 0.2176 0.3028 -0.0154 -0.0518 0.0257  98  SER   A C   
733  O O   . SER   A 98  ? 0.3482 0.2176 0.3047 0.0219  -0.0128 0.0252  98  SER   A O   
734  C CB  . SER   A 98  ? 0.4928 0.3004 0.3450 -0.1043 -0.0618 0.0233  98  SER   A CB  
735  O OG  . SER   A 98  ? 0.5844 0.3058 0.3844 -0.0775 -0.0777 0.0049  98  SER   A OG  
736  N N   . ASN   A 99  ? 0.3589 0.1670 0.2998 -0.0265 -0.0198 0.0311  99  ASN   A N   
737  C CA  . ASN   A 99  ? 0.3491 0.1885 0.2864 -0.0429 -0.0403 0.0359  99  ASN   A CA  
738  C C   . ASN   A 99  ? 0.2661 0.2046 0.2499 0.0067  -0.0239 0.0267  99  ASN   A C   
739  O O   . ASN   A 99  ? 0.3180 0.2393 0.2213 -0.0619 0.0093  0.0165  99  ASN   A O   
740  C CB  . ASN   A 99  ? 0.3720 0.2347 0.3082 -0.0384 -0.0229 0.0575  99  ASN   A CB  
741  C CG  . ASN   A 99  ? 0.4044 0.2934 0.3373 -0.0736 0.0557  0.0338  99  ASN   A CG  
742  O OD1 . ASN   A 99  ? 0.3426 0.3165 0.3624 -0.0783 0.0706  0.0249  99  ASN   A OD1 
743  N ND2 . ASN   A 99  ? 0.4329 0.2973 0.3486 -0.0852 0.0971  0.0108  99  ASN   A ND2 
744  N N   . HIS   A 100 ? 0.2254 0.1690 0.2417 -0.0263 -0.0055 0.0253  100 HIS   A N   
745  C CA  . HIS   A 100 ? 0.2118 0.1754 0.2402 -0.0113 -0.0044 0.0136  100 HIS   A CA  
746  C C   . HIS   A 100 ? 0.2429 0.1702 0.2105 -0.0087 -0.0146 0.0174  100 HIS   A C   
747  O O   . HIS   A 100 ? 0.2414 0.2035 0.2289 -0.0519 0.0049  0.0090  100 HIS   A O   
748  C CB  . HIS   A 100 ? 0.1909 0.2579 0.2841 -0.0160 0.0095  0.0181  100 HIS   A CB  
749  C CG  . HIS   A 100 ? 0.2362 0.3217 0.3350 -0.0387 0.0489  0.0291  100 HIS   A CG  
750  N ND1 . HIS   A 100 ? 0.2985 0.3885 0.3598 -0.0314 0.0320  0.0036  100 HIS   A ND1 
751  C CD2 . HIS   A 100 ? 0.2907 0.3612 0.3563 -0.0353 0.0047  0.0594  100 HIS   A CD2 
752  C CE1 . HIS   A 100 ? 0.2983 0.3942 0.3692 -0.0534 0.0024  0.0265  100 HIS   A CE1 
753  N NE2 . HIS   A 100 ? 0.2908 0.3648 0.3675 -0.0373 -0.0166 0.0596  100 HIS   A NE2 
754  N N   . TRP   A 101 ? 0.2237 0.1675 0.1876 0.0128  0.0048  0.0172  101 TRP   A N   
755  C CA  . TRP   A 101 ? 0.1653 0.1591 0.1967 -0.0072 0.0003  0.0241  101 TRP   A CA  
756  C C   . TRP   A 101 ? 0.1842 0.1625 0.2058 -0.0264 -0.0035 0.0135  101 TRP   A C   
757  O O   . TRP   A 101 ? 0.2112 0.1921 0.2133 -0.0166 0.0026  0.0058  101 TRP   A O   
758  C CB  . TRP   A 101 ? 0.1705 0.1703 0.1953 -0.0082 0.0160  -0.0088 101 TRP   A CB  
759  C CG  . TRP   A 101 ? 0.1445 0.1858 0.1929 0.0127  0.0043  -0.0159 101 TRP   A CG  
760  C CD1 . TRP   A 101 ? 0.1413 0.2077 0.1987 -0.0200 0.0026  -0.0225 101 TRP   A CD1 
761  C CD2 . TRP   A 101 ? 0.1752 0.1738 0.1895 -0.0021 0.0071  0.0148  101 TRP   A CD2 
762  N NE1 . TRP   A 101 ? 0.1758 0.2327 0.2006 -0.0278 0.0289  0.0075  101 TRP   A NE1 
763  C CE2 . TRP   A 101 ? 0.1527 0.1983 0.2012 0.0051  0.0145  0.0106  101 TRP   A CE2 
764  C CE3 . TRP   A 101 ? 0.2405 0.1568 0.1802 -0.0028 0.0099  0.0138  101 TRP   A CE3 
765  C CZ2 . TRP   A 101 ? 0.1794 0.1937 0.1990 -0.0084 -0.0051 0.0120  101 TRP   A CZ2 
766  C CZ3 . TRP   A 101 ? 0.2358 0.1546 0.1901 0.0000  0.0059  0.0188  101 TRP   A CZ3 
767  C CH2 . TRP   A 101 ? 0.2581 0.1494 0.1823 -0.0143 -0.0249 0.0168  101 TRP   A CH2 
768  N N   . VAL   A 102 ? 0.2176 0.1897 0.1984 -0.0029 -0.0133 0.0297  102 VAL   A N   
769  C CA  . VAL   A 102 ? 0.2121 0.1709 0.1890 -0.0180 -0.0231 0.0295  102 VAL   A CA  
770  C C   . VAL   A 102 ? 0.2256 0.1602 0.1952 -0.0101 0.0039  0.0242  102 VAL   A C   
771  O O   . VAL   A 102 ? 0.2084 0.1825 0.1902 -0.0119 -0.0034 0.0031  102 VAL   A O   
772  C CB  . VAL   A 102 ? 0.1887 0.2151 0.2058 -0.0178 -0.0359 0.0508  102 VAL   A CB  
773  C CG1 . VAL   A 102 ? 0.2140 0.2656 0.2197 -0.0116 -0.0239 0.0415  102 VAL   A CG1 
774  C CG2 . VAL   A 102 ? 0.2468 0.2364 0.2061 -0.0669 -0.0316 0.0311  102 VAL   A CG2 
775  N N   . PHE   A 103 ? 0.1718 0.1726 0.1921 -0.0029 -0.0197 0.0077  103 PHE   A N   
776  C CA  . PHE   A 103 ? 0.2203 0.1654 0.1765 -0.0180 -0.0201 0.0131  103 PHE   A CA  
777  C C   . PHE   A 103 ? 0.1941 0.1982 0.1837 -0.0439 0.0206  0.0270  103 PHE   A C   
778  O O   . PHE   A 103 ? 0.1997 0.2192 0.1913 -0.0105 0.0034  0.0291  103 PHE   A O   
779  C CB  . PHE   A 103 ? 0.2117 0.1618 0.1607 -0.0145 -0.0061 0.0141  103 PHE   A CB  
780  C CG  . PHE   A 103 ? 0.2233 0.1940 0.1731 -0.0196 -0.0303 -0.0008 103 PHE   A CG  
781  C CD1 . PHE   A 103 ? 0.2866 0.2087 0.1708 -0.0387 -0.0486 0.0065  103 PHE   A CD1 
782  C CD2 . PHE   A 103 ? 0.1949 0.2394 0.1767 -0.0272 -0.0235 -0.0039 103 PHE   A CD2 
783  C CE1 . PHE   A 103 ? 0.3329 0.2410 0.1735 -0.0207 -0.0471 -0.0003 103 PHE   A CE1 
784  C CE2 . PHE   A 103 ? 0.2158 0.2627 0.1647 0.0010  -0.0361 -0.0262 103 PHE   A CE2 
785  C CZ  . PHE   A 103 ? 0.3163 0.2527 0.1896 0.0149  -0.0214 -0.0104 103 PHE   A CZ  
786  N N   . GLY   A 104 ? 0.2072 0.1842 0.1764 -0.0349 -0.0076 0.0282  104 GLY   A N   
787  C CA  . GLY   A 104 ? 0.2179 0.2047 0.1990 -0.0348 -0.0468 0.0265  104 GLY   A CA  
788  C C   . GLY   A 104 ? 0.1812 0.2087 0.2123 -0.0238 0.0037  0.0420  104 GLY   A C   
789  O O   . GLY   A 104 ? 0.1670 0.2369 0.2151 -0.0149 -0.0097 0.0166  104 GLY   A O   
790  N N   . GLY   A 105 ? 0.1628 0.1737 0.2161 0.0203  0.0219  0.0272  105 GLY   A N   
791  C CA  . GLY   A 105 ? 0.1666 0.1686 0.2078 0.0084  0.0335  0.0325  105 GLY   A CA  
792  C C   . GLY   A 105 ? 0.1670 0.2043 0.2049 0.0047  0.0179  0.0212  105 GLY   A C   
793  O O   . GLY   A 105 ? 0.2185 0.2257 0.2433 0.0413  0.0086  -0.0051 105 GLY   A O   
794  N N   . GLY   A 106 ? 0.1880 0.1852 0.1830 0.0004  0.0270  0.0239  106 GLY   A N   
795  C CA  . GLY   A 106 ? 0.2059 0.1916 0.1761 -0.0153 0.0152  0.0377  106 GLY   A CA  
796  C C   . GLY   A 106 ? 0.1634 0.1920 0.1821 -0.0098 0.0059  0.0213  106 GLY   A C   
797  O O   . GLY   A 106 ? 0.1797 0.2198 0.2204 0.0119  -0.0145 0.0173  106 GLY   A O   
798  N N   . THR   A 107 ? 0.1639 0.1567 0.1771 -0.0068 0.0076  0.0194  107 THR   A N   
799  C CA  . THR   A 107 ? 0.1484 0.1622 0.1719 -0.0123 0.0013  0.0006  107 THR   A CA  
800  C C   . THR   A 107 ? 0.1490 0.1718 0.1804 -0.0197 -0.0067 0.0094  107 THR   A C   
801  O O   . THR   A 107 ? 0.1523 0.1718 0.1854 -0.0235 -0.0192 0.0161  107 THR   A O   
802  C CB  . THR   A 107 ? 0.1625 0.1880 0.1746 0.0005  0.0036  0.0092  107 THR   A CB  
803  O OG1 . THR   A 107 ? 0.1708 0.1888 0.2100 -0.0110 0.0045  -0.0101 107 THR   A OG1 
804  C CG2 . THR   A 107 ? 0.2067 0.2367 0.1757 0.0025  -0.0473 0.0290  107 THR   A CG2 
805  N N   . LYS   A 108 ? 0.1829 0.1690 0.1847 0.0122  0.0041  -0.0148 108 LYS   A N   
806  C CA  A LYS   A 108 ? 0.1801 0.1762 0.1859 0.0008  0.0149  -0.0158 108 LYS   A CA  
807  C CA  B LYS   A 108 ? 0.1748 0.1807 0.2016 0.0177  0.0208  -0.0104 108 LYS   A CA  
808  C C   . LYS   A 108 ? 0.1602 0.1791 0.1869 -0.0004 0.0247  -0.0162 108 LYS   A C   
809  O O   . LYS   A 108 ? 0.1857 0.2247 0.2075 -0.0102 -0.0212 0.0142  108 LYS   A O   
810  C CB  A LYS   A 108 ? 0.1994 0.1859 0.2035 -0.0329 0.0211  -0.0231 108 LYS   A CB  
811  C CB  B LYS   A 108 ? 0.1860 0.1980 0.2491 0.0299  0.0553  -0.0108 108 LYS   A CB  
812  C CG  A LYS   A 108 ? 0.2394 0.2401 0.2263 -0.0249 0.0101  -0.0355 108 LYS   A CG  
813  C CG  B LYS   A 108 ? 0.1810 0.2645 0.3000 0.0536  0.0673  -0.0177 108 LYS   A CG  
814  C CD  A LYS   A 108 ? 0.3486 0.2978 0.2522 0.0093  0.0045  -0.0289 108 LYS   A CD  
815  C CD  B LYS   A 108 ? 0.3103 0.3220 0.3485 0.0318  0.0589  -0.0212 108 LYS   A CD  
816  C CE  A LYS   A 108 ? 0.3467 0.3207 0.2773 -0.0136 0.0072  -0.0284 108 LYS   A CE  
817  C CE  B LYS   A 108 ? 0.3762 0.3687 0.3901 0.0149  0.0645  -0.0120 108 LYS   A CE  
818  N NZ  A LYS   A 108 ? 0.3989 0.3447 0.3128 -0.0175 0.0147  -0.0134 108 LYS   A NZ  
819  N NZ  B LYS   A 108 ? 0.4515 0.4160 0.4172 -0.0037 0.0562  -0.0007 108 LYS   A NZ  
820  N N   . LEU   A 109 ? 0.1492 0.1892 0.1908 -0.0010 0.0221  -0.0148 109 LEU   A N   
821  C CA  . LEU   A 109 ? 0.1609 0.1915 0.1854 0.0021  0.0119  0.0165  109 LEU   A CA  
822  C C   . LEU   A 109 ? 0.2268 0.1865 0.1879 0.0105  0.0167  0.0277  109 LEU   A C   
823  O O   . LEU   A 109 ? 0.1834 0.2092 0.1905 -0.0024 0.0057  0.0117  109 LEU   A O   
824  C CB  . LEU   A 109 ? 0.1546 0.2222 0.1759 0.0353  0.0369  0.0268  109 LEU   A CB  
825  C CG  . LEU   A 109 ? 0.1399 0.2350 0.1794 0.0330  0.0132  0.0015  109 LEU   A CG  
826  C CD1 . LEU   A 109 ? 0.2388 0.2629 0.1631 0.0246  -0.0328 0.0027  109 LEU   A CD1 
827  C CD2 . LEU   A 109 ? 0.1664 0.2260 0.2055 0.0270  -0.0066 -0.0095 109 LEU   A CD2 
828  N N   . THR   A 110 ? 0.1743 0.1836 0.1985 -0.0211 -0.0074 0.0270  110 THR   A N   
829  C CA  . THR   A 110 ? 0.1728 0.2061 0.2540 -0.0029 0.0190  0.0360  110 THR   A CA  
830  C C   . THR   A 110 ? 0.1298 0.2420 0.2459 -0.0154 -0.0216 0.0314  110 THR   A C   
831  O O   . THR   A 110 ? 0.1962 0.2621 0.2183 -0.0424 -0.0210 0.0067  110 THR   A O   
832  C CB  . THR   A 110 ? 0.2258 0.2210 0.3283 0.0642  0.0814  0.0607  110 THR   A CB  
833  O OG1 . THR   A 110 ? 0.3026 0.3020 0.3703 0.0911  0.0912  0.0399  110 THR   A OG1 
834  C CG2 . THR   A 110 ? 0.2643 0.2230 0.3662 0.0164  0.0313  0.0731  110 THR   A CG2 
835  N N   . VAL   A 111 ? 0.1539 0.2375 0.2689 -0.0090 -0.0224 0.0373  111 VAL   A N   
836  C CA  . VAL   A 111 ? 0.1513 0.2528 0.2858 -0.0056 -0.0385 0.0590  111 VAL   A CA  
837  C C   . VAL   A 111 ? 0.1969 0.2336 0.3198 0.0164  -0.0585 0.0625  111 VAL   A C   
838  O O   . VAL   A 111 ? 0.2829 0.2387 0.3265 -0.0538 -0.0757 0.0342  111 VAL   A O   
839  C CB  . VAL   A 111 ? 0.1575 0.2746 0.2715 -0.0193 0.0113  0.0428  111 VAL   A CB  
840  C CG1 . VAL   A 111 ? 0.1940 0.2659 0.2719 -0.0307 0.0220  0.0530  111 VAL   A CG1 
841  C CG2 . VAL   A 111 ? 0.1672 0.2741 0.2583 -0.0540 -0.0052 0.0122  111 VAL   A CG2 
842  N N   . LEU   A 112 ? 0.2078 0.2489 0.3406 0.0357  -0.0656 0.0902  112 LEU   A N   
843  C CA  . LEU   A 112 ? 0.2016 0.3270 0.3901 0.0445  -0.0470 0.0839  112 LEU   A CA  
844  C C   . LEU   A 112 ? 0.2712 0.4093 0.4231 0.1129  0.0099  0.1150  112 LEU   A C   
845  O O   . LEU   A 112 ? 0.3062 0.4342 0.3996 0.1369  0.0867  0.1337  112 LEU   A O   
846  C CB  . LEU   A 112 ? 0.2461 0.3608 0.4145 0.0695  -0.0231 0.0122  112 LEU   A CB  
847  C CG  . LEU   A 112 ? 0.4018 0.4458 0.4352 0.0024  -0.0471 -0.0148 112 LEU   A CG  
848  C CD1 . LEU   A 112 ? 0.2846 0.4546 0.4328 0.0314  -0.0752 -0.0246 112 LEU   A CD1 
849  C CD2 . LEU   A 112 ? 0.4900 0.4951 0.4461 -0.0467 -0.0224 -0.0176 112 LEU   A CD2 
850  N N   . GLY   A 113 ? 0.2981 0.4652 0.4845 0.0941  -0.0335 0.1104  113 GLY   A N   
851  C CA  . GLY   A 113 ? 0.4776 0.5165 0.5267 0.0522  -0.0587 0.0890  113 GLY   A CA  
852  C C   . GLY   A 113 ? 0.5227 0.5532 0.5523 0.0209  -0.0721 0.0519  113 GLY   A C   
853  O O   . GLY   A 113 ? 0.6591 0.5331 0.5563 0.0046  -0.0682 0.0180  113 GLY   A O   
854  N N   . GLN   A 114 ? 0.4734 0.5694 0.5604 0.0452  -0.0449 0.0553  114 GLN   A N   
855  C CA  . GLN   A 114 ? 0.5808 0.5957 0.5633 0.0316  0.0101  0.0528  114 GLN   A CA  
856  C C   . GLN   A 114 ? 0.3935 0.5300 0.5429 -0.0109 0.0224  0.0614  114 GLN   A C   
857  O O   . GLN   A 114 ? 0.4265 0.5562 0.5585 -0.1060 0.0660  0.0659  114 GLN   A O   
858  C CB  . GLN   A 114 ? 0.6735 0.6460 0.5752 0.0418  0.0274  0.0453  114 GLN   A CB  
859  C CG  . GLN   A 114 ? 0.6639 0.6480 0.5751 0.0465  0.0295  0.0323  114 GLN   A CG  
860  C CD  . GLN   A 114 ? 0.5401 0.6132 0.5653 0.0366  0.0163  0.0128  114 GLN   A CD  
861  O OE1 . GLN   A 114 ? 0.5212 0.6264 0.5785 -0.0259 0.0021  -0.0127 114 GLN   A OE1 
862  N NE2 . GLN   A 114 ? 0.2323 0.5425 0.5388 0.0601  0.0410  0.0249  114 GLN   A NE2 
863  N N   . GLY   A 115 ? 0.2940 0.4622 0.5096 0.0077  0.0177  0.0501  115 GLY   A N   
864  C CA  . GLY   A 115 ? 0.3660 0.4393 0.4664 -0.0227 0.0536  0.0143  115 GLY   A CA  
865  C C   . GLY   A 115 ? 0.3576 0.3959 0.4285 0.0105  0.0471  -0.0205 115 GLY   A C   
866  O O   . GLY   A 115 ? 0.2596 0.3588 0.4182 -0.0487 0.0157  -0.0223 115 GLY   A O   
867  N N   . GLY   A 116 ? 0.3532 0.4140 0.4208 0.0105  0.0605  -0.0089 116 GLY   A N   
868  C CA  . GLY   A 116 ? 0.4391 0.4044 0.4217 0.0386  0.0541  -0.0082 116 GLY   A CA  
869  C C   . GLY   A 116 ? 0.4080 0.3846 0.4203 0.0163  0.0222  0.0260  116 GLY   A C   
870  O O   . GLY   A 116 ? 0.3475 0.4253 0.4338 -0.0048 0.0109  0.0192  116 GLY   A O   
871  N N   . GLY   A 117 ? 0.3903 0.2799 0.3924 -0.0265 0.0391  0.0669  117 GLY   A N   
872  C CA  . GLY   A 117 ? 0.2380 0.2776 0.3672 -0.0117 0.0026  0.0602  117 GLY   A CA  
873  C C   . GLY   A 117 ? 0.1274 0.2835 0.3467 0.0197  0.0376  0.0597  117 GLY   A C   
874  O O   . GLY   A 117 ? 0.2048 0.3428 0.4024 0.0041  0.1114  0.0543  117 GLY   A O   
875  N N   . GLY   A 118 ? 0.1237 0.2214 0.2948 0.0326  0.0100  0.0596  118 GLY   A N   
876  C CA  . GLY   A 118 ? 0.1722 0.2282 0.2795 0.0321  -0.0195 0.0660  118 GLY   A CA  
877  C C   . GLY   A 118 ? 0.1617 0.2499 0.2861 -0.0022 0.0011  0.0918  118 GLY   A C   
878  O O   . GLY   A 118 ? 0.1701 0.2951 0.3027 0.0012  0.0101  0.0898  118 GLY   A O   
879  N N   . SER   A 119 ? 0.1768 0.2706 0.2917 0.0450  0.0438  0.0936  119 SER   A N   
880  C CA  . SER   A 119 ? 0.1529 0.3359 0.3029 0.0366  0.0332  0.0709  119 SER   A CA  
881  C C   . SER   A 119 ? 0.2281 0.4329 0.3036 0.0080  0.0110  0.0617  119 SER   A C   
882  O O   . SER   A 119 ? 0.1978 0.4498 0.2764 0.0446  -0.0004 0.0700  119 SER   A O   
883  C CB  . SER   A 119 ? 0.2422 0.3644 0.3302 0.0241  0.0382  0.0325  119 SER   A CB  
884  O OG  . SER   A 119 ? 0.2311 0.4159 0.3321 -0.0008 0.0275  0.0202  119 SER   A OG  
885  N N   . GLY   A 120 ? 0.3086 0.4825 0.3471 -0.0140 -0.0052 0.0544  120 GLY   A N   
886  C CA  . GLY   A 120 ? 0.4054 0.5003 0.4067 -0.0104 -0.0301 0.0448  120 GLY   A CA  
887  C C   . GLY   A 120 ? 0.4885 0.5323 0.4666 0.0093  -0.0361 0.0482  120 GLY   A C   
888  O O   . GLY   A 120 ? 0.5160 0.5476 0.5087 0.0651  -0.0400 0.0728  120 GLY   A O   
889  N N   . SER   A 129 ? 0.8279 0.8049 0.7891 0.0072  0.0146  0.0435  129 SER   A N   
890  C CA  . SER   A 129 ? 0.7998 0.8002 0.7802 -0.0047 0.0087  0.0333  129 SER   A CA  
891  C C   . SER   A 129 ? 0.7566 0.7447 0.7406 -0.0216 0.0243  0.0212  129 SER   A C   
892  O O   . SER   A 129 ? 0.7880 0.7672 0.7364 -0.0231 0.0097  0.0062  129 SER   A O   
893  C CB  . SER   A 129 ? 0.8284 0.8366 0.8030 -0.0076 -0.0091 0.0382  129 SER   A CB  
894  O OG  . SER   A 129 ? 0.8656 0.8481 0.8146 0.0021  -0.0233 0.0421  129 SER   A OG  
895  N N   . GLN   A 130 ? 0.6637 0.6806 0.7064 -0.0414 0.0356  0.0232  130 GLN   A N   
896  C CA  . GLN   A 130 ? 0.5905 0.6169 0.6681 -0.0282 0.0170  0.0260  130 GLN   A CA  
897  C C   . GLN   A 130 ? 0.4146 0.4577 0.5271 -0.0366 -0.0136 0.0278  130 GLN   A C   
898  O O   . GLN   A 130 ? 0.4450 0.4220 0.5133 -0.0849 -0.0084 0.0600  130 GLN   A O   
899  C CB  . GLN   A 130 ? 0.6919 0.7310 0.7775 -0.0153 0.0267  0.0295  130 GLN   A CB  
900  C CG  . GLN   A 130 ? 0.8252 0.8518 0.8867 -0.0069 0.0232  0.0348  130 GLN   A CG  
901  C CD  . GLN   A 130 ? 1.0087 0.9877 0.9873 0.0009  0.0200  0.0474  130 GLN   A CD  
902  O OE1 . GLN   A 130 ? 1.0502 1.0060 1.0078 -0.0072 0.0183  0.0567  130 GLN   A OE1 
903  N NE2 . GLN   A 130 ? 1.1192 1.0644 1.0399 0.0123  0.0204  0.0474  130 GLN   A NE2 
904  N N   . VAL   A 131 ? 0.2576 0.3636 0.4212 -0.0069 -0.0452 0.0074  131 VAL   A N   
905  C CA  . VAL   A 131 ? 0.2362 0.3083 0.3612 0.0236  -0.0195 -0.0080 131 VAL   A CA  
906  C C   . VAL   A 131 ? 0.2004 0.2920 0.3618 0.0167  -0.0118 0.0036  131 VAL   A C   
907  O O   . VAL   A 131 ? 0.2539 0.3221 0.3602 0.0291  -0.0220 0.0223  131 VAL   A O   
908  C CB  . VAL   A 131 ? 0.2507 0.3051 0.3299 0.0241  -0.0286 -0.0010 131 VAL   A CB  
909  C CG1 . VAL   A 131 ? 0.2353 0.3296 0.3362 0.0019  -0.0219 0.0307  131 VAL   A CG1 
910  C CG2 . VAL   A 131 ? 0.2741 0.3039 0.3093 0.0636  -0.0236 -0.0064 131 VAL   A CG2 
911  N N   . GLN   A 132 ? 0.1824 0.2921 0.3826 -0.0049 -0.0140 -0.0041 132 GLN   A N   
912  C CA  . GLN   A 132 ? 0.1925 0.2993 0.4042 -0.0326 0.0084  -0.0409 132 GLN   A CA  
913  C C   . GLN   A 132 ? 0.1985 0.2772 0.3587 -0.0067 -0.0170 -0.0311 132 GLN   A C   
914  O O   . GLN   A 132 ? 0.1861 0.3130 0.3345 0.0375  -0.0128 -0.0037 132 GLN   A O   
915  C CB  . GLN   A 132 ? 0.2835 0.3898 0.4949 -0.0412 -0.0071 -0.0526 132 GLN   A CB  
916  C CG  . GLN   A 132 ? 0.5217 0.5306 0.5965 -0.0421 0.0054  -0.0487 132 GLN   A CG  
917  C CD  . GLN   A 132 ? 0.7381 0.6852 0.6936 -0.0550 0.0049  -0.0312 132 GLN   A CD  
918  O OE1 . GLN   A 132 ? 0.8011 0.7199 0.7184 -0.0770 0.0195  -0.0351 132 GLN   A OE1 
919  N NE2 . GLN   A 132 ? 0.8337 0.7577 0.7394 -0.0360 -0.0128 -0.0133 132 GLN   A NE2 
920  N N   . LEU   A 133 ? 0.1753 0.2429 0.3387 -0.0167 -0.0211 -0.0304 133 LEU   A N   
921  C CA  A LEU   A 133 ? 0.1828 0.2041 0.3171 -0.0441 -0.0333 -0.0369 133 LEU   A CA  
922  C CA  B LEU   A 133 ? 0.1889 0.2187 0.3263 -0.0372 -0.0336 -0.0383 133 LEU   A CA  
923  C C   . LEU   A 133 ? 0.1869 0.2197 0.3331 -0.0109 -0.0501 -0.0502 133 LEU   A C   
924  O O   . LEU   A 133 ? 0.2365 0.2282 0.3627 0.0237  -0.0787 -0.0261 133 LEU   A O   
925  C CB  A LEU   A 133 ? 0.1846 0.1850 0.2869 -0.0045 -0.0231 -0.0292 133 LEU   A CB  
926  C CB  B LEU   A 133 ? 0.1991 0.2108 0.3127 -0.0240 -0.0279 -0.0327 133 LEU   A CB  
927  C CG  A LEU   A 133 ? 0.1390 0.2047 0.2542 0.0432  -0.0247 -0.0412 133 LEU   A CG  
928  C CG  B LEU   A 133 ? 0.2058 0.2210 0.2991 -0.0214 -0.0275 -0.0366 133 LEU   A CG  
929  C CD1 A LEU   A 133 ? 0.1763 0.2475 0.2436 0.0257  -0.0566 -0.0592 133 LEU   A CD1 
930  C CD1 B LEU   A 133 ? 0.2303 0.2454 0.2958 -0.0432 -0.0400 -0.0399 133 LEU   A CD1 
931  C CD2 A LEU   A 133 ? 0.1829 0.2332 0.2517 -0.0056 -0.0591 -0.0040 133 LEU   A CD2 
932  C CD2 B LEU   A 133 ? 0.2387 0.2326 0.2948 -0.0262 -0.0302 -0.0255 133 LEU   A CD2 
933  N N   . GLN   A 134 ? 0.1847 0.2531 0.3381 -0.0157 -0.0410 -0.0735 134 GLN   A N   
934  C CA  A GLN   A 134 ? 0.2191 0.2571 0.3671 -0.0381 -0.0196 -0.0714 134 GLN   A CA  
935  C CA  B GLN   A 134 ? 0.2191 0.2571 0.3671 -0.0381 -0.0196 -0.0714 134 GLN   A CA  
936  C C   . GLN   A 134 ? 0.1958 0.2334 0.3096 -0.0057 -0.0359 -0.0678 134 GLN   A C   
937  O O   . GLN   A 134 ? 0.2254 0.2148 0.3216 0.0195  -0.0347 -0.0634 134 GLN   A O   
938  C CB  A GLN   A 134 ? 0.2622 0.3351 0.4520 -0.0407 -0.0282 -0.0868 134 GLN   A CB  
939  C CB  B GLN   A 134 ? 0.2622 0.3351 0.4520 -0.0407 -0.0282 -0.0868 134 GLN   A CB  
940  C CG  A GLN   A 134 ? 0.4562 0.4853 0.5515 -0.0254 -0.0197 -0.0659 134 GLN   A CG  
941  C CG  B GLN   A 134 ? 0.4562 0.4853 0.5515 -0.0254 -0.0197 -0.0659 134 GLN   A CG  
942  C CD  A GLN   A 134 ? 0.6830 0.6543 0.6466 -0.0200 -0.0033 -0.0405 134 GLN   A CD  
943  C CD  B GLN   A 134 ? 0.6830 0.6543 0.6466 -0.0200 -0.0033 -0.0405 134 GLN   A CD  
944  O OE1 A GLN   A 134 ? 0.6875 0.7004 0.6754 0.0093  0.0024  -0.0311 134 GLN   A OE1 
945  O OE1 B GLN   A 134 ? 0.6875 0.7004 0.6754 0.0093  0.0024  -0.0311 134 GLN   A OE1 
946  N NE2 A GLN   A 134 ? 0.7969 0.7274 0.6870 -0.0318 -0.0011 -0.0325 134 GLN   A NE2 
947  N NE2 B GLN   A 134 ? 0.7969 0.7274 0.6870 -0.0318 -0.0011 -0.0325 134 GLN   A NE2 
948  N N   . GLN   A 135 ? 0.1610 0.2382 0.2733 -0.0217 -0.0319 -0.0524 135 GLN   A N   
949  C CA  . GLN   A 135 ? 0.1903 0.2268 0.2618 -0.0017 -0.0437 -0.0565 135 GLN   A CA  
950  C C   . GLN   A 135 ? 0.2057 0.2114 0.2772 -0.0013 -0.0327 -0.0557 135 GLN   A C   
951  O O   . GLN   A 135 ? 0.2603 0.2127 0.2888 0.0175  -0.0406 -0.0568 135 GLN   A O   
952  C CB  . GLN   A 135 ? 0.2090 0.2094 0.2505 -0.0174 -0.0303 -0.0565 135 GLN   A CB  
953  C CG  . GLN   A 135 ? 0.2052 0.1979 0.2376 -0.0096 -0.0529 -0.0488 135 GLN   A CG  
954  C CD  . GLN   A 135 ? 0.1868 0.2045 0.2235 -0.0271 -0.0220 -0.0126 135 GLN   A CD  
955  O OE1 . GLN   A 135 ? 0.2100 0.2029 0.1927 -0.0162 -0.0429 -0.0080 135 GLN   A OE1 
956  N NE2 . GLN   A 135 ? 0.2395 0.2179 0.2403 -0.0231 0.0151  0.0061  135 GLN   A NE2 
957  N N   . PRO   A 136 ? 0.2620 0.2287 0.2755 -0.0110 -0.0303 -0.0405 136 PRO   A N   
958  C CA  . PRO   A 136 ? 0.2736 0.2233 0.2848 0.0274  -0.0484 -0.0568 136 PRO   A CA  
959  C C   . PRO   A 136 ? 0.2802 0.2204 0.2945 0.0336  -0.0587 -0.0400 136 PRO   A C   
960  O O   . PRO   A 136 ? 0.2629 0.2593 0.3048 0.0086  -0.0673 -0.0544 136 PRO   A O   
961  C CB  . PRO   A 136 ? 0.3362 0.2672 0.2961 0.0591  -0.0070 -0.0702 136 PRO   A CB  
962  C CG  . PRO   A 136 ? 0.4341 0.2943 0.2913 0.0046  0.0432  -0.0504 136 PRO   A CG  
963  C CD  . PRO   A 136 ? 0.2598 0.2665 0.2697 0.0130  0.0369  -0.0409 136 PRO   A CD  
964  N N   . GLY   A 137 ? 0.2621 0.2370 0.3031 0.0157  -0.0277 -0.0311 137 GLY   A N   
965  C CA  . GLY   A 137 ? 0.2375 0.2150 0.3068 0.0083  -0.0357 -0.0301 137 GLY   A CA  
966  C C   . GLY   A 137 ? 0.2203 0.2152 0.3101 0.0199  -0.0369 -0.0319 137 GLY   A C   
967  O O   . GLY   A 137 ? 0.2290 0.2187 0.3127 -0.0265 -0.0381 -0.0195 137 GLY   A O   
968  N N   . ALA   A 138 ? 0.2285 0.2359 0.3178 0.0365  -0.0280 -0.0462 138 ALA   A N   
969  C CA  . ALA   A 138 ? 0.2094 0.2660 0.3006 0.0568  -0.0317 -0.0516 138 ALA   A CA  
970  C C   . ALA   A 138 ? 0.2747 0.2670 0.2788 0.0316  -0.0506 -0.0295 138 ALA   A C   
971  O O   . ALA   A 138 ? 0.3393 0.3237 0.2919 0.0324  -0.0597 -0.0253 138 ALA   A O   
972  C CB  . ALA   A 138 ? 0.2468 0.2834 0.3217 0.0826  -0.0287 -0.0643 138 ALA   A CB  
973  N N   . GLU   A 139 ? 0.2861 0.2251 0.2471 0.0307  -0.0330 -0.0498 139 GLU   A N   
974  C CA  . GLU   A 139 ? 0.2597 0.2487 0.2688 0.0289  -0.0314 -0.0620 139 GLU   A CA  
975  C C   . GLU   A 139 ? 0.2497 0.2265 0.2626 0.0144  -0.0372 -0.0737 139 GLU   A C   
976  O O   . GLU   A 139 ? 0.2630 0.2388 0.2608 0.0024  -0.0709 -0.0535 139 GLU   A O   
977  C CB  . GLU   A 139 ? 0.2760 0.2857 0.3140 0.0627  -0.0510 -0.0401 139 GLU   A CB  
978  C CG  . GLU   A 139 ? 0.3938 0.3348 0.3475 0.0378  -0.0805 -0.0464 139 GLU   A CG  
979  C CD  . GLU   A 139 ? 0.4629 0.3690 0.3780 0.0285  -0.0624 -0.0523 139 GLU   A CD  
980  O OE1 . GLU   A 139 ? 0.4939 0.3595 0.3723 0.0481  -0.0510 -0.0679 139 GLU   A OE1 
981  O OE2 . GLU   A 139 ? 0.4755 0.3751 0.4031 -0.0069 -0.0708 -0.0522 139 GLU   A OE2 
982  N N   . LEU   A 140 ? 0.3144 0.2586 0.2610 0.0687  -0.0490 -0.0760 140 LEU   A N   
983  C CA  . LEU   A 140 ? 0.3551 0.2641 0.2684 0.0712  -0.0444 -0.0781 140 LEU   A CA  
984  C C   . LEU   A 140 ? 0.3742 0.2561 0.2610 0.0693  -0.0434 -0.0561 140 LEU   A C   
985  O O   . LEU   A 140 ? 0.3781 0.3059 0.2547 0.0921  -0.0823 -0.0458 140 LEU   A O   
986  C CB  . LEU   A 140 ? 0.3521 0.2781 0.2689 0.0914  -0.0423 -0.0872 140 LEU   A CB  
987  C CG  . LEU   A 140 ? 0.3817 0.2882 0.2840 0.0440  -0.0420 -0.0976 140 LEU   A CG  
988  C CD1 . LEU   A 140 ? 0.3573 0.3095 0.2998 0.0690  -0.0613 -0.0997 140 LEU   A CD1 
989  C CD2 . LEU   A 140 ? 0.4266 0.2754 0.2921 0.0207  -0.0031 -0.0976 140 LEU   A CD2 
990  N N   . ALA   A 141 ? 0.4114 0.2334 0.2501 0.0813  -0.0350 -0.0196 141 ALA   A N   
991  C CA  . ALA   A 141 ? 0.4094 0.2500 0.2582 0.1159  -0.0024 -0.0059 141 ALA   A CA  
992  C C   . ALA   A 141 ? 0.3776 0.3043 0.2542 0.1240  0.0246  0.0092  141 ALA   A C   
993  O O   . ALA   A 141 ? 0.3667 0.3277 0.2426 0.1098  -0.0117 0.0257  141 ALA   A O   
994  C CB  . ALA   A 141 ? 0.4119 0.2451 0.2627 0.1254  0.0117  -0.0016 141 ALA   A CB  
995  N N   . LYS   A 142 ? 0.4074 0.3357 0.2762 0.0915  0.0667  0.0150  142 LYS   A N   
996  C CA  . LYS   A 142 ? 0.3737 0.3767 0.3019 0.0910  0.0475  0.0256  142 LYS   A CA  
997  C C   . LYS   A 142 ? 0.3486 0.3636 0.2675 0.1329  0.0378  0.0644  142 LYS   A C   
998  O O   . LYS   A 142 ? 0.3925 0.3770 0.2459 0.1796  0.0256  0.0740  142 LYS   A O   
999  C CB  . LYS   A 142 ? 0.4221 0.4235 0.3802 0.0738  0.0132  -0.0003 142 LYS   A CB  
1000 C CG  . LYS   A 142 ? 0.5376 0.4963 0.4596 0.0325  -0.0054 -0.0042 142 LYS   A CG  
1001 C CD  . LYS   A 142 ? 0.6014 0.5618 0.5338 0.0349  -0.0054 -0.0004 142 LYS   A CD  
1002 C CE  . LYS   A 142 ? 0.6709 0.6256 0.5901 0.0117  -0.0021 0.0067  142 LYS   A CE  
1003 N NZ  . LYS   A 142 ? 0.7104 0.6481 0.6157 -0.0332 -0.0031 0.0146  142 LYS   A NZ  
1004 N N   . PRO   A 143 ? 0.3818 0.3398 0.2904 0.1216  0.0569  0.0818  143 PRO   A N   
1005 C CA  . PRO   A 143 ? 0.4077 0.3489 0.3068 0.1248  0.0445  0.0642  143 PRO   A CA  
1006 C C   . PRO   A 143 ? 0.4255 0.3639 0.2992 0.0680  0.0856  0.0404  143 PRO   A C   
1007 O O   . PRO   A 143 ? 0.4508 0.3827 0.3003 0.0618  0.0680  0.0355  143 PRO   A O   
1008 C CB  . PRO   A 143 ? 0.4114 0.3705 0.3214 0.1452  0.0065  0.0743  143 PRO   A CB  
1009 C CG  . PRO   A 143 ? 0.4161 0.3599 0.3336 0.1313  -0.0026 0.0874  143 PRO   A CG  
1010 C CD  . PRO   A 143 ? 0.3726 0.3535 0.3182 0.1330  0.0157  0.0860  143 PRO   A CD  
1011 N N   . GLY   A 144 ? 0.4751 0.3588 0.2940 0.0641  0.0924  0.0280  144 GLY   A N   
1012 C CA  . GLY   A 144 ? 0.4170 0.3756 0.2822 0.1116  0.0679  0.0345  144 GLY   A CA  
1013 C C   . GLY   A 144 ? 0.4513 0.3744 0.2763 0.1000  0.0532  0.0511  144 GLY   A C   
1014 O O   . GLY   A 144 ? 0.5603 0.3807 0.2809 0.1112  0.0660  0.1056  144 GLY   A O   
1015 N N   . ALA   A 145 ? 0.3953 0.3755 0.2477 0.1247  0.0554  0.0170  145 ALA   A N   
1016 C CA  . ALA   A 145 ? 0.3876 0.3757 0.2545 0.0762  0.0455  -0.0042 145 ALA   A CA  
1017 C C   . ALA   A 145 ? 0.3776 0.3342 0.2782 0.1148  0.0482  0.0211  145 ALA   A C   
1018 O O   . ALA   A 145 ? 0.3402 0.3679 0.2945 0.1369  0.0700  0.0510  145 ALA   A O   
1019 C CB  . ALA   A 145 ? 0.4409 0.3826 0.2451 0.0838  -0.0004 -0.0301 145 ALA   A CB  
1020 N N   . SER   A 146 ? 0.3818 0.3482 0.2663 0.1030  0.0530  0.0103  146 SER   A N   
1021 C CA  A SER   A 146 ? 0.3217 0.3350 0.2495 0.1143  0.0500  0.0008  146 SER   A CA  
1022 C CA  B SER   A 146 ? 0.3266 0.3351 0.2621 0.1038  0.0395  0.0022  146 SER   A CA  
1023 C C   . SER   A 146 ? 0.3524 0.3144 0.2468 0.0841  0.0155  -0.0076 146 SER   A C   
1024 O O   . SER   A 146 ? 0.4638 0.3298 0.2631 0.1040  0.0196  -0.0169 146 SER   A O   
1025 C CB  A SER   A 146 ? 0.3255 0.3519 0.2327 0.1015  0.0027  0.0163  146 SER   A CB  
1026 C CB  B SER   A 146 ? 0.3258 0.3529 0.2696 0.0679  -0.0174 0.0130  146 SER   A CB  
1027 O OG  A SER   A 146 ? 0.3481 0.3618 0.2175 0.1185  -0.0467 0.0314  146 SER   A OG  
1028 O OG  B SER   A 146 ? 0.3385 0.3673 0.2741 0.0330  -0.0767 0.0185  146 SER   A OG  
1029 N N   . VAL   A 147 ? 0.3084 0.2594 0.2156 0.0818  -0.0076 0.0246  147 VAL   A N   
1030 C CA  . VAL   A 147 ? 0.3218 0.2522 0.2062 0.0830  0.0069  0.0260  147 VAL   A CA  
1031 C C   . VAL   A 147 ? 0.3807 0.2419 0.1999 0.0499  -0.0077 0.0190  147 VAL   A C   
1032 O O   . VAL   A 147 ? 0.3439 0.2284 0.1939 0.0672  -0.0449 -0.0051 147 VAL   A O   
1033 C CB  . VAL   A 147 ? 0.3856 0.2639 0.2213 0.0659  -0.0026 0.0334  147 VAL   A CB  
1034 C CG1 . VAL   A 147 ? 0.3519 0.2560 0.2123 0.0936  0.0184  -0.0022 147 VAL   A CG1 
1035 C CG2 . VAL   A 147 ? 0.4054 0.2729 0.2439 0.0305  -0.0441 0.0594  147 VAL   A CG2 
1036 N N   . GLN   A 148 ? 0.3557 0.2362 0.2071 0.0426  -0.0064 0.0394  148 GLN   A N   
1037 C CA  . GLN   A 148 ? 0.3160 0.2235 0.2241 -0.0008 -0.0115 0.0029  148 GLN   A CA  
1038 C C   . GLN   A 148 ? 0.3644 0.2050 0.2247 -0.0110 -0.0316 -0.0104 148 GLN   A C   
1039 O O   . GLN   A 148 ? 0.4344 0.2483 0.2332 -0.0931 -0.0311 -0.0226 148 GLN   A O   
1040 C CB  . GLN   A 148 ? 0.2799 0.2285 0.2714 0.0327  -0.0102 -0.0064 148 GLN   A CB  
1041 C CG  . GLN   A 148 ? 0.3049 0.2945 0.3004 0.0303  -0.0119 0.0257  148 GLN   A CG  
1042 C CD  . GLN   A 148 ? 0.3757 0.3438 0.3324 0.0141  -0.0221 0.0423  148 GLN   A CD  
1043 O OE1 . GLN   A 148 ? 0.4562 0.4124 0.3527 0.0575  0.0008  0.0424  148 GLN   A OE1 
1044 N NE2 . GLN   A 148 ? 0.3548 0.3470 0.3257 -0.0062 -0.0185 0.0669  148 GLN   A NE2 
1045 N N   . LEU   A 149 ? 0.3265 0.2130 0.2158 0.0484  -0.0418 -0.0069 149 LEU   A N   
1046 C CA  . LEU   A 149 ? 0.2457 0.2182 0.2302 0.0363  -0.0393 0.0068  149 LEU   A CA  
1047 C C   . LEU   A 149 ? 0.2451 0.2438 0.2434 0.0316  -0.0356 0.0027  149 LEU   A C   
1048 O O   . LEU   A 149 ? 0.2866 0.2306 0.2694 0.0263  -0.0287 0.0198  149 LEU   A O   
1049 C CB  . LEU   A 149 ? 0.2412 0.2482 0.2506 0.0350  -0.0388 0.0116  149 LEU   A CB  
1050 C CG  . LEU   A 149 ? 0.3485 0.2994 0.2964 0.1035  -0.0678 0.0105  149 LEU   A CG  
1051 C CD1 . LEU   A 149 ? 0.3525 0.3756 0.3094 0.1201  -0.1022 -0.0194 149 LEU   A CD1 
1052 C CD2 . LEU   A 149 ? 0.3708 0.3045 0.3403 0.0803  -0.0506 0.0239  149 LEU   A CD2 
1053 N N   . SER   A 150 ? 0.2491 0.2669 0.2561 0.0539  -0.0182 0.0078  150 SER   A N   
1054 C CA  . SER   A 150 ? 0.2198 0.2729 0.2679 0.0476  0.0040  0.0029  150 SER   A CA  
1055 C C   . SER   A 150 ? 0.2055 0.2442 0.2523 0.0508  -0.0107 0.0284  150 SER   A C   
1056 O O   . SER   A 150 ? 0.2646 0.2245 0.2344 0.0447  -0.0352 0.0092  150 SER   A O   
1057 C CB  . SER   A 150 ? 0.3298 0.3176 0.3028 0.0700  -0.0238 -0.0237 150 SER   A CB  
1058 O OG  . SER   A 150 ? 0.3653 0.3498 0.3249 0.0450  -0.0300 -0.0329 150 SER   A OG  
1059 N N   . CYS   A 151 ? 0.1652 0.2529 0.2607 0.0558  -0.0063 -0.0025 151 CYS   A N   
1060 C CA  . CYS   A 151 ? 0.1627 0.2569 0.2642 0.0169  -0.0319 -0.0025 151 CYS   A CA  
1061 C C   . CYS   A 151 ? 0.2089 0.2476 0.3053 0.0177  -0.0481 -0.0472 151 CYS   A C   
1062 O O   . CYS   A 151 ? 0.2441 0.2678 0.3327 0.0585  -0.0809 -0.0577 151 CYS   A O   
1063 C CB  . CYS   A 151 ? 0.2329 0.2712 0.2454 0.0170  -0.0334 0.0120  151 CYS   A CB  
1064 S SG  . CYS   A 151 ? 0.2322 0.3199 0.2686 0.0373  -0.0239 -0.0149 151 CYS   A SG  
1065 N N   . LYS   A 152 ? 0.2151 0.2317 0.3117 0.0144  -0.0383 -0.0503 152 LYS   A N   
1066 C CA  . LYS   A 152 ? 0.1825 0.2889 0.3317 0.0083  -0.0555 -0.0811 152 LYS   A CA  
1067 C C   . LYS   A 152 ? 0.2142 0.2881 0.3093 -0.0089 -0.0240 -0.0344 152 LYS   A C   
1068 O O   . LYS   A 152 ? 0.2172 0.2785 0.3042 -0.0127 -0.0136 -0.0065 152 LYS   A O   
1069 C CB  . LYS   A 152 ? 0.2598 0.3570 0.3877 -0.0175 -0.0813 -0.1192 152 LYS   A CB  
1070 C CG  . LYS   A 152 ? 0.2893 0.4172 0.4382 -0.0458 -0.1075 -0.1207 152 LYS   A CG  
1071 C CD  . LYS   A 152 ? 0.4089 0.4809 0.4872 -0.0481 -0.0954 -0.0966 152 LYS   A CD  
1072 C CE  . LYS   A 152 ? 0.5795 0.5413 0.5285 -0.0350 -0.0530 -0.0790 152 LYS   A CE  
1073 N NZ  . LYS   A 152 ? 0.5862 0.5746 0.5506 -0.0547 -0.0126 -0.0756 152 LYS   A NZ  
1074 N N   . GLY   A 153 ? 0.2049 0.2832 0.3023 -0.0041 -0.0144 -0.0119 153 GLY   A N   
1075 C CA  . GLY   A 153 ? 0.1841 0.3073 0.2922 0.0295  -0.0235 0.0300  153 GLY   A CA  
1076 C C   . GLY   A 153 ? 0.2359 0.3717 0.3076 0.0250  -0.0187 0.0393  153 GLY   A C   
1077 O O   . GLY   A 153 ? 0.2725 0.4617 0.3147 0.0402  -0.0003 0.0964  153 GLY   A O   
1078 N N   . SER   A 154 ? 0.1623 0.3264 0.3119 0.0046  -0.0179 -0.0280 154 SER   A N   
1079 C CA  . SER   A 154 ? 0.2106 0.3028 0.3305 -0.0265 -0.0055 -0.0465 154 SER   A CA  
1080 C C   . SER   A 154 ? 0.2089 0.2873 0.3201 -0.0247 0.0162  -0.0224 154 SER   A C   
1081 O O   . SER   A 154 ? 0.2601 0.2839 0.3030 -0.0119 0.0032  -0.0536 154 SER   A O   
1082 C CB  . SER   A 154 ? 0.2253 0.3102 0.3481 -0.0243 -0.0436 -0.0433 154 SER   A CB  
1083 O OG  . SER   A 154 ? 0.3106 0.3158 0.3584 -0.0161 -0.0623 -0.0450 154 SER   A OG  
1084 N N   . GLY   A 155 ? 0.1911 0.2867 0.3213 -0.0212 0.0333  -0.0083 155 GLY   A N   
1085 C CA  . GLY   A 155 ? 0.2146 0.2523 0.3177 -0.0147 0.0381  -0.0168 155 GLY   A CA  
1086 C C   . GLY   A 155 ? 0.2630 0.2626 0.3247 -0.0027 0.0056  -0.0222 155 GLY   A C   
1087 O O   . GLY   A 155 ? 0.2520 0.3066 0.3308 -0.0532 0.0245  -0.0261 155 GLY   A O   
1088 N N   . TYR   A 156 ? 0.2112 0.2543 0.3225 -0.0283 -0.0385 -0.0168 156 TYR   A N   
1089 C CA  . TYR   A 156 ? 0.2596 0.2610 0.3225 -0.0108 -0.0355 -0.0021 156 TYR   A CA  
1090 C C   . TYR   A 156 ? 0.2171 0.2530 0.3256 -0.0090 -0.0324 0.0065  156 TYR   A C   
1091 O O   . TYR   A 156 ? 0.2207 0.2400 0.3233 -0.0121 -0.0533 0.0190  156 TYR   A O   
1092 C CB  . TYR   A 156 ? 0.2189 0.2714 0.3031 0.0076  -0.0245 -0.0128 156 TYR   A CB  
1093 C CG  . TYR   A 156 ? 0.2014 0.2835 0.2943 0.0129  -0.0308 -0.0168 156 TYR   A CG  
1094 C CD1 . TYR   A 156 ? 0.1718 0.3103 0.2752 0.0641  -0.0081 -0.0280 156 TYR   A CD1 
1095 C CD2 . TYR   A 156 ? 0.2206 0.2650 0.2917 0.0101  -0.0135 -0.0204 156 TYR   A CD2 
1096 C CE1 . TYR   A 156 ? 0.2312 0.2827 0.2661 0.0259  -0.0340 -0.0210 156 TYR   A CE1 
1097 C CE2 . TYR   A 156 ? 0.2347 0.2589 0.2807 -0.0373 -0.0206 -0.0337 156 TYR   A CE2 
1098 C CZ  . TYR   A 156 ? 0.2437 0.3054 0.2719 0.0069  -0.0044 -0.0062 156 TYR   A CZ  
1099 O OH  . TYR   A 156 ? 0.2282 0.3642 0.2790 0.0138  -0.0041 0.0033  156 TYR   A OH  
1100 N N   . THR   A 157 ? 0.1897 0.2581 0.3340 -0.0278 -0.0220 0.0195  157 THR   A N   
1101 C CA  . THR   A 157 ? 0.2063 0.2477 0.3458 0.0183  -0.0061 0.0098  157 THR   A CA  
1102 C C   . THR   A 157 ? 0.1950 0.2390 0.3222 0.0478  -0.0464 -0.0022 157 THR   A C   
1103 O O   . THR   A 157 ? 0.2094 0.2511 0.3194 -0.0052 -0.0725 -0.0237 157 THR   A O   
1104 C CB  . THR   A 157 ? 0.2112 0.2794 0.3875 -0.0057 -0.0004 -0.0048 157 THR   A CB  
1105 O OG1 . THR   A 157 ? 0.2986 0.3051 0.4210 -0.0036 -0.0271 -0.0089 157 THR   A OG1 
1106 C CG2 . THR   A 157 ? 0.2741 0.2832 0.3951 -0.0113 -0.0019 0.0055  157 THR   A CG2 
1107 N N   . PHE   A 158 ? 0.2360 0.2521 0.3034 0.0204  -0.0159 -0.0045 158 PHE   A N   
1108 C CA  . PHE   A 158 ? 0.2222 0.2519 0.2896 0.0026  -0.0119 -0.0229 158 PHE   A CA  
1109 C C   . PHE   A 158 ? 0.2634 0.2409 0.2725 -0.0041 -0.0674 -0.0127 158 PHE   A C   
1110 O O   . PHE   A 158 ? 0.2445 0.2312 0.2854 0.0090  -0.0497 0.0068  158 PHE   A O   
1111 C CB  . PHE   A 158 ? 0.2738 0.2709 0.2942 -0.0129 -0.0366 -0.0564 158 PHE   A CB  
1112 C CG  . PHE   A 158 ? 0.3275 0.3227 0.3033 -0.0213 -0.0433 -0.0890 158 PHE   A CG  
1113 C CD1 . PHE   A 158 ? 0.3239 0.3350 0.3199 -0.0196 -0.0608 -0.1143 158 PHE   A CD1 
1114 C CD2 . PHE   A 158 ? 0.2920 0.3598 0.3027 -0.0310 -0.0689 -0.0800 158 PHE   A CD2 
1115 C CE1 . PHE   A 158 ? 0.3371 0.3559 0.3301 -0.0286 -0.0615 -0.1036 158 PHE   A CE1 
1116 C CE2 . PHE   A 158 ? 0.2866 0.3932 0.3128 -0.0250 -0.0733 -0.0782 158 PHE   A CE2 
1117 C CZ  . PHE   A 158 ? 0.3093 0.3704 0.3162 -0.0117 -0.0774 -0.0956 158 PHE   A CZ  
1118 N N   . PRO   A 159 ? 0.2805 0.2492 0.2761 0.0402  -0.0733 -0.0157 159 PRO   A N   
1119 C CA  . PRO   A 159 ? 0.3095 0.2677 0.2742 -0.0033 -0.0832 -0.0012 159 PRO   A CA  
1120 C C   . PRO   A 159 ? 0.2288 0.2398 0.2661 0.0225  -0.0619 -0.0039 159 PRO   A C   
1121 O O   . PRO   A 159 ? 0.2310 0.2310 0.2612 0.0156  -0.0465 0.0013  159 PRO   A O   
1122 C CB  . PRO   A 159 ? 0.3975 0.2800 0.2740 0.0124  -0.1177 -0.0042 159 PRO   A CB  
1123 C CG  . PRO   A 159 ? 0.3696 0.3076 0.2911 -0.0056 -0.0572 0.0117  159 PRO   A CG  
1124 C CD  . PRO   A 159 ? 0.3020 0.2933 0.2770 0.0158  -0.0846 -0.0037 159 PRO   A CD  
1125 N N   . ASN   A 160 ? 0.1857 0.2260 0.2585 0.0118  -0.0720 -0.0142 160 ASN   A N   
1126 C CA  . ASN   A 160 ? 0.1637 0.2411 0.2759 0.0181  -0.0609 -0.0288 160 ASN   A CA  
1127 C C   . ASN   A 160 ? 0.2290 0.2313 0.2634 0.0215  -0.0323 -0.0235 160 ASN   A C   
1128 O O   . ASN   A 160 ? 0.2079 0.2634 0.2622 0.0282  -0.0476 -0.0198 160 ASN   A O   
1129 C CB  . ASN   A 160 ? 0.1359 0.2584 0.3106 0.0168  -0.0359 -0.0260 160 ASN   A CB  
1130 C CG  . ASN   A 160 ? 0.2032 0.2513 0.3459 -0.0070 -0.0376 -0.0179 160 ASN   A CG  
1131 O OD1 . ASN   A 160 ? 0.2139 0.2243 0.3849 0.0109  -0.0809 -0.0144 160 ASN   A OD1 
1132 N ND2 . ASN   A 160 ? 0.1629 0.2982 0.3537 0.0080  0.0122  -0.0373 160 ASN   A ND2 
1133 N N   . TYR   A 161 ? 0.1634 0.2241 0.2559 0.0322  -0.0251 0.0047  161 TYR   A N   
1134 C CA  . TYR   A 161 ? 0.2083 0.1963 0.2496 0.0156  -0.0167 0.0144  161 TYR   A CA  
1135 C C   . TYR   A 161 ? 0.2087 0.2263 0.2419 0.0218  0.0036  0.0059  161 TYR   A C   
1136 O O   . TYR   A 161 ? 0.2228 0.2937 0.2526 0.0291  -0.0032 0.0243  161 TYR   A O   
1137 C CB  . TYR   A 161 ? 0.2350 0.2190 0.2508 0.0016  -0.0190 0.0097  161 TYR   A CB  
1138 C CG  . TYR   A 161 ? 0.1746 0.2370 0.2520 0.0234  0.0084  0.0184  161 TYR   A CG  
1139 C CD1 . TYR   A 161 ? 0.2326 0.2702 0.2631 0.0047  0.0112  0.0105  161 TYR   A CD1 
1140 C CD2 . TYR   A 161 ? 0.2280 0.3004 0.2680 0.0032  0.0141  0.0233  161 TYR   A CD2 
1141 C CE1 . TYR   A 161 ? 0.2361 0.3085 0.2633 -0.0006 0.0406  -0.0053 161 TYR   A CE1 
1142 C CE2 . TYR   A 161 ? 0.2591 0.3165 0.2739 -0.0109 0.0265  0.0147  161 TYR   A CE2 
1143 C CZ  . TYR   A 161 ? 0.2472 0.3469 0.2825 -0.0136 0.0561  0.0155  161 TYR   A CZ  
1144 O OH  . TYR   A 161 ? 0.3790 0.4010 0.2970 -0.0235 0.0819  0.0052  161 TYR   A OH  
1145 N N   . TRP   A 162 ? 0.1919 0.2042 0.2411 0.0271  -0.0089 -0.0119 162 TRP   A N   
1146 C CA  . TRP   A 162 ? 0.1979 0.2058 0.2276 0.0403  0.0038  -0.0206 162 TRP   A CA  
1147 C C   . TRP   A 162 ? 0.1863 0.1805 0.2219 0.0359  -0.0162 -0.0033 162 TRP   A C   
1148 O O   . TRP   A 162 ? 0.1781 0.1938 0.2185 0.0290  0.0026  0.0072  162 TRP   A O   
1149 C CB  . TRP   A 162 ? 0.1701 0.2293 0.2307 0.0002  -0.0147 -0.0203 162 TRP   A CB  
1150 C CG  . TRP   A 162 ? 0.2260 0.2175 0.1985 0.0352  -0.0250 -0.0072 162 TRP   A CG  
1151 C CD1 . TRP   A 162 ? 0.2342 0.1900 0.2053 0.0460  0.0082  0.0061  162 TRP   A CD1 
1152 C CD2 . TRP   A 162 ? 0.2256 0.2515 0.2092 -0.0383 -0.0069 0.0030  162 TRP   A CD2 
1153 N NE1 . TRP   A 162 ? 0.2271 0.2000 0.2172 0.0079  -0.0365 -0.0091 162 TRP   A NE1 
1154 C CE2 . TRP   A 162 ? 0.2437 0.2154 0.2112 0.0101  -0.0105 -0.0044 162 TRP   A CE2 
1155 C CE3 . TRP   A 162 ? 0.2076 0.3025 0.2191 -0.0261 -0.0557 0.0174  162 TRP   A CE3 
1156 C CZ2 . TRP   A 162 ? 0.2636 0.2450 0.2031 -0.0408 -0.0015 -0.0229 162 TRP   A CZ2 
1157 C CZ3 . TRP   A 162 ? 0.2078 0.2986 0.2298 -0.0372 -0.0538 0.0258  162 TRP   A CZ3 
1158 C CH2 . TRP   A 162 ? 0.2720 0.2797 0.2247 -0.0411 -0.0051 -0.0023 162 TRP   A CH2 
1159 N N   . MET   A 163 ? 0.1891 0.1706 0.2326 0.0319  -0.0350 -0.0082 163 MET   A N   
1160 C CA  . MET   A 163 ? 0.1799 0.1698 0.2178 0.0276  -0.0451 -0.0194 163 MET   A CA  
1161 C C   . MET   A 163 ? 0.1744 0.1732 0.2015 0.0187  -0.0061 0.0159  163 MET   A C   
1162 O O   . MET   A 163 ? 0.1797 0.1862 0.2074 0.0049  -0.0179 0.0254  163 MET   A O   
1163 C CB  . MET   A 163 ? 0.1779 0.1828 0.2316 0.0081  -0.0406 -0.0012 163 MET   A CB  
1164 C CG  . MET   A 163 ? 0.2044 0.2076 0.2595 0.0179  -0.0303 0.0185  163 MET   A CG  
1165 S SD  . MET   A 163 ? 0.2224 0.2188 0.2744 0.0066  -0.0335 0.0066  163 MET   A SD  
1166 C CE  . MET   A 163 ? 0.2156 0.2685 0.3052 0.0309  -0.0514 -0.0271 163 MET   A CE  
1167 N N   . HIS   A 164 ? 0.1721 0.1824 0.1787 0.0339  -0.0282 -0.0118 164 HIS   A N   
1168 C CA  . HIS   A 164 ? 0.1630 0.1796 0.1781 0.0474  -0.0332 0.0031  164 HIS   A CA  
1169 C C   . HIS   A 164 ? 0.1569 0.2050 0.1708 0.0188  -0.0168 -0.0031 164 HIS   A C   
1170 O O   . HIS   A 164 ? 0.1772 0.1796 0.1858 -0.0006 -0.0126 -0.0081 164 HIS   A O   
1171 C CB  . HIS   A 164 ? 0.2236 0.1704 0.1737 0.0402  -0.0203 0.0061  164 HIS   A CB  
1172 C CG  . HIS   A 164 ? 0.1936 0.1544 0.1799 0.0172  -0.0162 -0.0098 164 HIS   A CG  
1173 N ND1 . HIS   A 164 ? 0.2211 0.1614 0.1783 0.0233  0.0074  0.0032  164 HIS   A ND1 
1174 C CD2 . HIS   A 164 ? 0.1793 0.1731 0.1896 0.0343  -0.0136 -0.0169 164 HIS   A CD2 
1175 C CE1 . HIS   A 164 ? 0.1984 0.2066 0.1821 0.0249  0.0212  -0.0158 164 HIS   A CE1 
1176 N NE2 . HIS   A 164 ? 0.2051 0.1906 0.1658 0.0302  0.0110  -0.0095 164 HIS   A NE2 
1177 N N   . TRP   A 165 ? 0.1381 0.1770 0.1866 0.0349  -0.0129 0.0045  165 TRP   A N   
1178 C CA  . TRP   A 165 ? 0.2032 0.1738 0.1702 0.0167  -0.0348 0.0082  165 TRP   A CA  
1179 C C   . TRP   A 165 ? 0.1764 0.1670 0.1746 0.0008  -0.0126 0.0041  165 TRP   A C   
1180 O O   . TRP   A 165 ? 0.1662 0.1581 0.1807 -0.0168 -0.0261 -0.0071 165 TRP   A O   
1181 C CB  . TRP   A 165 ? 0.1949 0.2352 0.1834 -0.0314 -0.0549 0.0215  165 TRP   A CB  
1182 C CG  . TRP   A 165 ? 0.2057 0.2275 0.1889 -0.0295 -0.0232 0.0151  165 TRP   A CG  
1183 C CD1 . TRP   A 165 ? 0.2324 0.1929 0.2026 0.0219  -0.0339 -0.0042 165 TRP   A CD1 
1184 C CD2 . TRP   A 165 ? 0.2231 0.2251 0.1877 0.0090  -0.0480 -0.0035 165 TRP   A CD2 
1185 N NE1 . TRP   A 165 ? 0.2472 0.2067 0.2042 0.0127  -0.0460 0.0076  165 TRP   A NE1 
1186 C CE2 . TRP   A 165 ? 0.2191 0.2218 0.2019 0.0120  -0.0689 0.0188  165 TRP   A CE2 
1187 C CE3 . TRP   A 165 ? 0.2394 0.2191 0.2057 -0.0128 -0.0244 -0.0179 165 TRP   A CE3 
1188 C CZ2 . TRP   A 165 ? 0.2285 0.2259 0.2175 -0.0298 -0.0317 0.0102  165 TRP   A CZ2 
1189 C CZ3 . TRP   A 165 ? 0.2362 0.2225 0.2016 0.0169  -0.0507 -0.0088 165 TRP   A CZ3 
1190 C CH2 . TRP   A 165 ? 0.2491 0.2412 0.2108 -0.0063 -0.0443 -0.0014 165 TRP   A CH2 
1191 N N   . VAL   A 166 ? 0.1620 0.1827 0.1823 0.0143  -0.0079 0.0119  166 VAL   A N   
1192 C CA  . VAL   A 166 ? 0.1598 0.1682 0.1764 0.0079  -0.0078 -0.0028 166 VAL   A CA  
1193 C C   . VAL   A 166 ? 0.1863 0.1603 0.1965 0.0141  -0.0092 -0.0032 166 VAL   A C   
1194 O O   . VAL   A 166 ? 0.1966 0.1815 0.2453 0.0118  -0.0434 -0.0124 166 VAL   A O   
1195 C CB  . VAL   A 166 ? 0.1877 0.2072 0.1782 0.0353  -0.0199 -0.0090 166 VAL   A CB  
1196 C CG1 . VAL   A 166 ? 0.2821 0.2374 0.1953 0.0693  -0.0613 -0.0253 166 VAL   A CG1 
1197 C CG2 . VAL   A 166 ? 0.2300 0.2101 0.1849 0.0467  -0.0171 -0.0173 166 VAL   A CG2 
1198 N N   . THR   A 167 ? 0.1892 0.1822 0.1959 0.0202  -0.0133 -0.0116 167 THR   A N   
1199 C CA  . THR   A 167 ? 0.1728 0.1777 0.1946 0.0439  -0.0210 -0.0171 167 THR   A CA  
1200 C C   . THR   A 167 ? 0.2146 0.1382 0.1924 0.0016  -0.0344 -0.0367 167 THR   A C   
1201 O O   . THR   A 167 ? 0.2382 0.1433 0.1965 0.0143  -0.0318 -0.0146 167 THR   A O   
1202 C CB  . THR   A 167 ? 0.2246 0.1958 0.2217 0.0230  -0.0167 -0.0341 167 THR   A CB  
1203 O OG1 . THR   A 167 ? 0.2427 0.1968 0.2224 0.0425  0.0000  -0.0270 167 THR   A OG1 
1204 C CG2 . THR   A 167 ? 0.2226 0.1950 0.2392 -0.0312 -0.0338 -0.0091 167 THR   A CG2 
1205 N N   . GLN   A 168 ? 0.2446 0.1790 0.2061 0.0232  -0.0591 -0.0139 168 GLN   A N   
1206 C CA  . GLN   A 168 ? 0.1294 0.2051 0.2659 0.0388  -0.0266 0.0171  168 GLN   A CA  
1207 C C   . GLN   A 168 ? 0.1968 0.2278 0.3085 0.0731  -0.0260 0.0201  168 GLN   A C   
1208 O O   . GLN   A 168 ? 0.2560 0.2361 0.2773 0.0030  -0.0630 -0.0243 168 GLN   A O   
1209 C CB  . GLN   A 168 ? 0.2358 0.2876 0.3008 0.0312  -0.0160 0.0571  168 GLN   A CB  
1210 C CG  . GLN   A 168 ? 0.2924 0.3497 0.3303 0.0089  0.0094  0.0723  168 GLN   A CG  
1211 C CD  . GLN   A 168 ? 0.3771 0.3985 0.3582 0.0493  0.0688  0.0458  168 GLN   A CD  
1212 O OE1 . GLN   A 168 ? 0.3784 0.4055 0.3905 0.0040  0.1166  0.0217  168 GLN   A OE1 
1213 N NE2 . GLN   A 168 ? 0.3595 0.4224 0.3490 0.0559  0.0694  0.0713  168 GLN   A NE2 
1214 N N   . ARG   A 169 ? 0.2432 0.2734 0.3849 0.0961  0.0685  0.0335  169 ARG   A N   
1215 C CA  . ARG   A 169 ? 0.3427 0.3543 0.4599 0.1223  0.1041  0.0104  169 ARG   A CA  
1216 C C   . ARG   A 169 ? 0.4810 0.4926 0.5476 0.0912  0.0866  0.0159  169 ARG   A C   
1217 O O   . ARG   A 169 ? 0.4460 0.5252 0.5425 0.0864  0.0935  0.0307  169 ARG   A O   
1218 C CB  . ARG   A 169 ? 0.4238 0.3704 0.4512 0.0940  0.0909  0.0572  169 ARG   A CB  
1219 C CG  . ARG   A 169 ? 0.4760 0.4524 0.4593 0.1114  0.0363  0.0629  169 ARG   A CG  
1220 C CD  . ARG   A 169 ? 0.4951 0.4838 0.4680 0.0948  0.0093  0.0558  169 ARG   A CD  
1221 N NE  . ARG   A 169 ? 0.3952 0.4743 0.4632 0.0879  0.0105  0.0356  169 ARG   A NE  
1222 C CZ  . ARG   A 169 ? 0.3920 0.4645 0.4597 0.0046  0.0278  0.0160  169 ARG   A CZ  
1223 N NH1 . ARG   A 169 ? 0.4229 0.4424 0.4645 -0.0022 0.0274  -0.0082 169 ARG   A NH1 
1224 N NH2 . ARG   A 169 ? 0.2775 0.4470 0.4422 -0.0275 0.0319  0.0247  169 ARG   A NH2 
1225 N N   . PRO   A 170 ? 0.6657 0.6217 0.6321 0.0373  0.0242  0.0084  170 PRO   A N   
1226 C CA  . PRO   A 170 ? 0.6686 0.6488 0.6795 0.0526  -0.0083 0.0179  170 PRO   A CA  
1227 C C   . PRO   A 170 ? 0.6436 0.6624 0.6963 0.0829  -0.0323 0.0402  170 PRO   A C   
1228 O O   . PRO   A 170 ? 0.6970 0.6904 0.7090 0.0743  -0.0303 0.0599  170 PRO   A O   
1229 C CB  . PRO   A 170 ? 0.6462 0.6275 0.6910 0.0773  -0.0192 -0.0078 170 PRO   A CB  
1230 C CG  . PRO   A 170 ? 0.6188 0.6321 0.6784 0.0859  -0.0360 -0.0238 170 PRO   A CG  
1231 C CD  . PRO   A 170 ? 0.6758 0.6241 0.6560 0.0485  -0.0104 -0.0246 170 PRO   A CD  
1232 N N   . GLY   A 171 ? 0.6046 0.6277 0.6912 0.0963  -0.0287 0.0405  171 GLY   A N   
1233 C CA  . GLY   A 171 ? 0.5987 0.6363 0.6823 0.0716  -0.0077 0.0331  171 GLY   A CA  
1234 C C   . GLY   A 171 ? 0.6796 0.6692 0.6719 0.0260  -0.0126 0.0227  171 GLY   A C   
1235 O O   . GLY   A 171 ? 0.6938 0.6848 0.6761 -0.0194 -0.0360 0.0202  171 GLY   A O   
1236 N N   . ARG   A 172 ? 0.7151 0.6649 0.6505 0.0636  0.0026  0.0193  172 ARG   A N   
1237 C CA  . ARG   A 172 ? 0.6879 0.6660 0.6123 0.0877  0.0009  0.0136  172 ARG   A CA  
1238 C C   . ARG   A 172 ? 0.6307 0.6136 0.5593 0.1170  -0.0275 -0.0008 172 ARG   A C   
1239 O O   . ARG   A 172 ? 0.6606 0.6173 0.5695 0.0894  0.0131  -0.0359 172 ARG   A O   
1240 C CB  . ARG   A 172 ? 0.6668 0.6698 0.6093 0.0628  0.0098  0.0211  172 ARG   A CB  
1241 C CG  . ARG   A 172 ? 0.6360 0.6630 0.6030 0.0328  0.0144  0.0190  172 ARG   A CG  
1242 C CD  . ARG   A 172 ? 0.5820 0.6145 0.5841 -0.0116 0.0275  0.0161  172 ARG   A CD  
1243 N NE  . ARG   A 172 ? 0.5246 0.5508 0.5623 -0.0711 0.0138  0.0048  172 ARG   A NE  
1244 C CZ  . ARG   A 172 ? 0.4681 0.4878 0.5508 -0.0604 -0.0057 -0.0027 172 ARG   A CZ  
1245 N NH1 . ARG   A 172 ? 0.4151 0.4188 0.5321 -0.0568 -0.0439 0.0259  172 ARG   A NH1 
1246 N NH2 . ARG   A 172 ? 0.4874 0.4801 0.5572 -0.0472 -0.0017 -0.0334 172 ARG   A NH2 
1247 N N   . GLY   A 173 ? 0.4227 0.5209 0.4771 0.1605  -0.0967 0.0066  173 GLY   A N   
1248 C CA  . GLY   A 173 ? 0.3762 0.4268 0.3970 0.1128  -0.1239 0.0005  173 GLY   A CA  
1249 C C   . GLY   A 173 ? 0.3051 0.3170 0.3227 0.0653  -0.1066 0.0053  173 GLY   A C   
1250 O O   . GLY   A 173 ? 0.3268 0.2901 0.3166 0.0736  -0.1164 -0.0308 173 GLY   A O   
1251 N N   . LEU   A 174 ? 0.3041 0.2416 0.2752 0.0202  -0.0281 0.0086  174 LEU   A N   
1252 C CA  . LEU   A 174 ? 0.1924 0.2505 0.2300 0.0078  0.0096  0.0002  174 LEU   A CA  
1253 C C   . LEU   A 174 ? 0.1883 0.2170 0.2376 -0.0006 -0.0086 -0.0022 174 LEU   A C   
1254 O O   . LEU   A 174 ? 0.2471 0.2427 0.2202 0.0267  -0.0576 0.0055  174 LEU   A O   
1255 C CB  . LEU   A 174 ? 0.2876 0.2745 0.2219 -0.0242 0.0414  -0.0450 174 LEU   A CB  
1256 C CG  . LEU   A 174 ? 0.3355 0.3084 0.2173 -0.0694 0.0231  -0.0582 174 LEU   A CG  
1257 C CD1 . LEU   A 174 ? 0.2973 0.3065 0.2242 -0.0236 0.0516  -0.0230 174 LEU   A CD1 
1258 C CD2 . LEU   A 174 ? 0.3157 0.3479 0.1955 -0.0674 -0.0065 -0.0808 174 LEU   A CD2 
1259 N N   . GLU   A 175 ? 0.1603 0.1762 0.2640 -0.0034 -0.0253 0.0091  175 GLU   A N   
1260 C CA  . GLU   A 175 ? 0.1706 0.1688 0.2661 -0.0064 -0.0143 0.0055  175 GLU   A CA  
1261 C C   . GLU   A 175 ? 0.1906 0.1698 0.2387 0.0346  -0.0052 -0.0123 175 GLU   A C   
1262 O O   . GLU   A 175 ? 0.2097 0.1677 0.2408 0.0165  -0.0495 -0.0129 175 GLU   A O   
1263 C CB  . GLU   A 175 ? 0.1555 0.2287 0.3117 -0.0107 -0.0335 0.0081  175 GLU   A CB  
1264 C CG  . GLU   A 175 ? 0.2054 0.3324 0.3978 0.0090  0.0178  -0.0244 175 GLU   A CG  
1265 C CD  . GLU   A 175 ? 0.5141 0.5028 0.4829 0.0156  0.0393  -0.0438 175 GLU   A CD  
1266 O OE1 . GLU   A 175 ? 0.4518 0.5482 0.4954 0.0491  0.0827  -0.0683 175 GLU   A OE1 
1267 O OE2 . GLU   A 175 ? 0.5618 0.5565 0.5271 -0.0225 0.0307  -0.0375 175 GLU   A OE2 
1268 N N   . TRP   A 176 ? 0.1853 0.1684 0.2168 0.0316  -0.0180 -0.0205 176 TRP   A N   
1269 C CA  . TRP   A 176 ? 0.1911 0.1482 0.1919 0.0505  -0.0232 -0.0195 176 TRP   A CA  
1270 C C   . TRP   A 176 ? 0.2178 0.1696 0.1953 0.0035  -0.0108 0.0140  176 TRP   A C   
1271 O O   . TRP   A 176 ? 0.2016 0.2256 0.2120 -0.0037 -0.0111 0.0323  176 TRP   A O   
1272 C CB  . TRP   A 176 ? 0.1990 0.1722 0.2054 0.0596  -0.0410 -0.0366 176 TRP   A CB  
1273 C CG  . TRP   A 176 ? 0.2274 0.1685 0.2049 0.0502  -0.0274 -0.0162 176 TRP   A CG  
1274 C CD1 . TRP   A 176 ? 0.2511 0.1630 0.1981 0.0092  -0.0202 -0.0138 176 TRP   A CD1 
1275 C CD2 . TRP   A 176 ? 0.2094 0.1563 0.1892 0.0435  -0.0361 -0.0060 176 TRP   A CD2 
1276 N NE1 . TRP   A 176 ? 0.2398 0.1680 0.1854 0.0161  0.0051  0.0007  176 TRP   A NE1 
1277 C CE2 . TRP   A 176 ? 0.2329 0.1547 0.1831 0.0126  -0.0272 0.0155  176 TRP   A CE2 
1278 C CE3 . TRP   A 176 ? 0.2092 0.1661 0.1831 -0.0106 0.0001  -0.0035 176 TRP   A CE3 
1279 C CZ2 . TRP   A 176 ? 0.2881 0.1691 0.1789 0.0157  -0.0187 0.0240  176 TRP   A CZ2 
1280 C CZ3 . TRP   A 176 ? 0.2467 0.1841 0.1842 0.0115  -0.0204 0.0358  176 TRP   A CZ3 
1281 C CH2 . TRP   A 176 ? 0.2859 0.1765 0.1772 0.0110  -0.0543 0.0275  176 TRP   A CH2 
1282 N N   . ILE   A 177 ? 0.1817 0.1463 0.1562 0.0109  -0.0082 0.0108  177 ILE   A N   
1283 C CA  . ILE   A 177 ? 0.2086 0.1591 0.1589 0.0458  -0.0431 0.0038  177 ILE   A CA  
1284 C C   . ILE   A 177 ? 0.1619 0.1624 0.1912 0.0241  -0.0268 0.0156  177 ILE   A C   
1285 O O   . ILE   A 177 ? 0.1865 0.1880 0.1979 0.0128  -0.0237 -0.0071 177 ILE   A O   
1286 C CB  . ILE   A 177 ? 0.2134 0.1750 0.1544 0.0447  -0.0415 0.0033  177 ILE   A CB  
1287 C CG1 . ILE   A 177 ? 0.2103 0.1792 0.1839 0.0225  -0.0216 -0.0084 177 ILE   A CG1 
1288 C CG2 . ILE   A 177 ? 0.2908 0.2040 0.1618 0.0298  -0.0283 0.0393  177 ILE   A CG2 
1289 C CD1 . ILE   A 177 ? 0.2368 0.1708 0.1796 -0.0019 -0.0259 -0.0209 177 ILE   A CD1 
1290 N N   . GLY   A 178 ? 0.1548 0.1980 0.1954 0.0429  -0.0126 0.0037  178 GLY   A N   
1291 C CA  . GLY   A 178 ? 0.1825 0.1911 0.2100 0.0566  0.0027  -0.0079 178 GLY   A CA  
1292 C C   . GLY   A 178 ? 0.1569 0.1446 0.1998 0.0459  0.0079  0.0009  178 GLY   A C   
1293 O O   . GLY   A 178 ? 0.1864 0.1708 0.1889 0.0192  -0.0146 -0.0009 178 GLY   A O   
1294 N N   . ARG   A 179 ? 0.1543 0.1567 0.1827 0.0163  -0.0118 -0.0114 179 ARG   A N   
1295 C CA  . ARG   A 179 ? 0.1657 0.2165 0.1936 0.0388  -0.0313 0.0004  179 ARG   A CA  
1296 C C   . ARG   A 179 ? 0.1847 0.1960 0.2006 0.0600  -0.0148 0.0102  179 ARG   A C   
1297 O O   . ARG   A 179 ? 0.2130 0.1934 0.2064 0.0138  -0.0262 0.0264  179 ARG   A O   
1298 C CB  . ARG   A 179 ? 0.2673 0.2283 0.1964 0.0548  0.0171  -0.0078 179 ARG   A CB  
1299 C CG  . ARG   A 179 ? 0.2423 0.1983 0.2106 0.0515  -0.0259 0.0086  179 ARG   A CG  
1300 C CD  . ARG   A 179 ? 0.2786 0.1820 0.2200 0.0359  -0.0133 -0.0272 179 ARG   A CD  
1301 N NE  . ARG   A 179 ? 0.2618 0.1916 0.2258 0.0471  -0.0147 -0.0130 179 ARG   A NE  
1302 C CZ  . ARG   A 179 ? 0.2461 0.2126 0.2196 0.0390  0.0000  0.0103  179 ARG   A CZ  
1303 N NH1 . ARG   A 179 ? 0.3020 0.2512 0.2195 0.0187  -0.0354 0.0352  179 ARG   A NH1 
1304 N NH2 . ARG   A 179 ? 0.2719 0.2354 0.2306 0.0062  0.0147  0.0056  179 ARG   A NH2 
1305 N N   . ILE   A 180 ? 0.1965 0.2026 0.1908 0.0520  -0.0369 0.0214  180 ILE   A N   
1306 C CA  . ILE   A 180 ? 0.1997 0.1842 0.1571 0.0315  -0.0380 0.0128  180 ILE   A CA  
1307 C C   . ILE   A 180 ? 0.1822 0.1969 0.1916 0.0225  -0.0161 0.0177  180 ILE   A C   
1308 O O   . ILE   A 180 ? 0.2249 0.1750 0.2153 0.0467  -0.0084 0.0198  180 ILE   A O   
1309 C CB  . ILE   A 180 ? 0.2712 0.1713 0.1504 0.0296  -0.0568 -0.0025 180 ILE   A CB  
1310 C CG1 . ILE   A 180 ? 0.2808 0.2320 0.1610 0.0261  -0.0508 0.0140  180 ILE   A CG1 
1311 C CG2 . ILE   A 180 ? 0.2933 0.2020 0.1651 0.0369  -0.0414 -0.0172 180 ILE   A CG2 
1312 C CD1 . ILE   A 180 ? 0.3377 0.2560 0.1676 0.0344  -0.0742 0.0195  180 ILE   A CD1 
1313 N N   . ASP   A 181 ? 0.1732 0.1776 0.2018 0.0285  -0.0139 0.0186  181 ASP   A N   
1314 C CA  . ASP   A 181 ? 0.1919 0.2103 0.2098 0.0189  -0.0211 0.0038  181 ASP   A CA  
1315 C C   . ASP   A 181 ? 0.2015 0.2141 0.2093 0.0298  0.0043  0.0215  181 ASP   A C   
1316 O O   . ASP   A 181 ? 0.2125 0.2298 0.2305 0.0246  -0.0061 0.0338  181 ASP   A O   
1317 C CB  . ASP   A 181 ? 0.1853 0.2061 0.2291 0.0229  0.0028  -0.0248 181 ASP   A CB  
1318 C CG  . ASP   A 181 ? 0.2290 0.2237 0.2549 0.0221  -0.0104 -0.0137 181 ASP   A CG  
1319 O OD1 . ASP   A 181 ? 0.2199 0.2480 0.2433 0.0263  -0.0132 0.0000  181 ASP   A OD1 
1320 O OD2 . ASP   A 181 ? 0.2582 0.2468 0.2863 0.0448  -0.0145 -0.0242 181 ASP   A OD2 
1321 N N   . PRO   A 182 ? 0.2472 0.2180 0.2081 0.0497  -0.0409 -0.0003 182 PRO   A N   
1322 C CA  . PRO   A 182 ? 0.2735 0.2248 0.2366 0.0565  -0.0769 -0.0264 182 PRO   A CA  
1323 C C   . PRO   A 182 ? 0.2691 0.2386 0.2434 0.0799  -0.0484 0.0010  182 PRO   A C   
1324 O O   . PRO   A 182 ? 0.3735 0.2828 0.2376 0.1133  -0.0523 0.0094  182 PRO   A O   
1325 C CB  . PRO   A 182 ? 0.2955 0.2136 0.2405 0.0463  -0.0712 -0.0286 182 PRO   A CB  
1326 C CG  . PRO   A 182 ? 0.2986 0.2394 0.2192 0.0503  -0.0836 -0.0034 182 PRO   A CG  
1327 C CD  . PRO   A 182 ? 0.2710 0.2225 0.2028 0.0282  -0.0540 -0.0052 182 PRO   A CD  
1328 N N   . ASN   A 183 ? 0.2028 0.2153 0.2358 0.0294  -0.0396 -0.0055 183 ASN   A N   
1329 C CA  . ASN   A 183 ? 0.2186 0.2122 0.2529 0.0367  -0.0417 0.0239  183 ASN   A CA  
1330 C C   . ASN   A 183 ? 0.2119 0.2195 0.2760 0.0386  -0.0535 0.0428  183 ASN   A C   
1331 O O   . ASN   A 183 ? 0.2523 0.2160 0.2437 0.0370  -0.0102 0.0462  183 ASN   A O   
1332 C CB  . ASN   A 183 ? 0.2097 0.2030 0.2657 0.0451  -0.0221 0.0164  183 ASN   A CB  
1333 C CG  . ASN   A 183 ? 0.2480 0.2093 0.2950 0.0251  -0.0109 -0.0028 183 ASN   A CG  
1334 O OD1 . ASN   A 183 ? 0.2577 0.2368 0.3018 0.0313  -0.0386 -0.0220 183 ASN   A OD1 
1335 N ND2 . ASN   A 183 ? 0.2371 0.2130 0.3205 0.0258  -0.0204 0.0173  183 ASN   A ND2 
1336 N N   . SER   A 184 ? 0.2339 0.2224 0.3269 0.0250  -0.0697 0.0600  184 SER   A N   
1337 C CA  . SER   A 184 ? 0.2268 0.2470 0.3451 0.0248  -0.0858 0.0609  184 SER   A CA  
1338 C C   . SER   A 184 ? 0.2297 0.2611 0.3502 0.0065  -0.0579 0.0622  184 SER   A C   
1339 O O   . SER   A 184 ? 0.2629 0.2573 0.3490 0.0124  -0.0830 0.0757  184 SER   A O   
1340 C CB  . SER   A 184 ? 0.2174 0.2677 0.3452 0.0104  -0.0895 0.0226  184 SER   A CB  
1341 O OG  . SER   A 184 ? 0.2230 0.2706 0.3300 0.0628  -0.0575 0.0152  184 SER   A OG  
1342 N N   . GLY   A 185 ? 0.2367 0.2602 0.3318 0.0333  -0.0702 0.0321  185 GLY   A N   
1343 C CA  . GLY   A 185 ? 0.2717 0.2674 0.3059 0.0247  -0.0270 0.0270  185 GLY   A CA  
1344 C C   . GLY   A 185 ? 0.2867 0.2568 0.2778 0.0338  -0.0073 0.0208  185 GLY   A C   
1345 O O   . GLY   A 185 ? 0.3973 0.2901 0.2784 0.0676  0.0092  0.0080  185 GLY   A O   
1346 N N   . PHE   A 186 ? 0.2445 0.2274 0.2635 0.0334  -0.0174 0.0237  186 PHE   A N   
1347 C CA  . PHE   A 186 ? 0.2074 0.2183 0.2545 0.0303  -0.0217 0.0248  186 PHE   A CA  
1348 C C   . PHE   A 186 ? 0.2235 0.2057 0.2569 0.0176  -0.0036 0.0235  186 PHE   A C   
1349 O O   . PHE   A 186 ? 0.2137 0.2225 0.2630 0.0526  0.0123  0.0168  186 PHE   A O   
1350 C CB  . PHE   A 186 ? 0.2125 0.2317 0.2609 0.0050  -0.0405 0.0253  186 PHE   A CB  
1351 C CG  . PHE   A 186 ? 0.2825 0.3121 0.3026 -0.0116 0.0089  0.0393  186 PHE   A CG  
1352 C CD1 . PHE   A 186 ? 0.3843 0.3887 0.3226 -0.0822 -0.0005 0.0444  186 PHE   A CD1 
1353 C CD2 . PHE   A 186 ? 0.3507 0.3722 0.3256 -0.0089 -0.0022 0.0455  186 PHE   A CD2 
1354 C CE1 . PHE   A 186 ? 0.3976 0.4230 0.3386 -0.0967 -0.0179 0.0527  186 PHE   A CE1 
1355 C CE2 . PHE   A 186 ? 0.3848 0.4006 0.3406 -0.0692 -0.0226 0.0555  186 PHE   A CE2 
1356 C CZ  . PHE   A 186 ? 0.3728 0.4191 0.3471 -0.0890 -0.0291 0.0527  186 PHE   A CZ  
1357 N N   . ILE   A 187 ? 0.1724 0.2123 0.2519 0.0509  -0.0092 0.0083  187 ILE   A N   
1358 C CA  . ILE   A 187 ? 0.1825 0.2094 0.2448 0.0274  -0.0390 -0.0007 187 ILE   A CA  
1359 C C   . ILE   A 187 ? 0.2015 0.2002 0.2518 0.0388  0.0005  0.0156  187 ILE   A C   
1360 O O   . ILE   A 187 ? 0.2304 0.2198 0.2718 0.0189  0.0263  0.0397  187 ILE   A O   
1361 C CB  . ILE   A 187 ? 0.2196 0.2115 0.2365 0.0316  -0.0174 0.0030  187 ILE   A CB  
1362 C CG1 . ILE   A 187 ? 0.2539 0.2933 0.2362 0.0431  -0.0103 -0.0017 187 ILE   A CG1 
1363 C CG2 . ILE   A 187 ? 0.3214 0.1748 0.2464 0.0722  0.0008  0.0087  187 ILE   A CG2 
1364 C CD1 . ILE   A 187 ? 0.3912 0.2891 0.2413 0.0844  0.0303  0.0176  187 ILE   A CD1 
1365 N N   . ARG   A 188 ? 0.2111 0.1992 0.2427 0.0421  -0.0086 0.0194  188 ARG   A N   
1366 C CA  . ARG   A 188 ? 0.2033 0.2118 0.2382 0.0349  0.0100  0.0171  188 ARG   A CA  
1367 C C   . ARG   A 188 ? 0.2021 0.1921 0.2423 0.0222  -0.0231 0.0411  188 ARG   A C   
1368 O O   . ARG   A 188 ? 0.1966 0.2164 0.2615 -0.0074 -0.0191 0.0602  188 ARG   A O   
1369 C CB  . ARG   A 188 ? 0.2635 0.2466 0.2269 0.0268  0.0234  -0.0047 188 ARG   A CB  
1370 C CG  . ARG   A 188 ? 0.2440 0.2825 0.2252 0.0072  0.0133  0.0240  188 ARG   A CG  
1371 C CD  . ARG   A 188 ? 0.3433 0.2966 0.2309 0.0125  -0.0046 0.0113  188 ARG   A CD  
1372 N NE  . ARG   A 188 ? 0.3740 0.2810 0.2614 -0.0020 -0.0215 0.0073  188 ARG   A NE  
1373 C CZ  . ARG   A 188 ? 0.3583 0.2822 0.2996 -0.0020 0.0038  0.0153  188 ARG   A CZ  
1374 N NH1 . ARG   A 188 ? 0.3724 0.2939 0.3145 0.0410  -0.0018 0.0311  188 ARG   A NH1 
1375 N NH2 . ARG   A 188 ? 0.3593 0.3103 0.3146 -0.0033 0.0220  0.0059  188 ARG   A NH2 
1376 N N   . TYR   A 189 ? 0.2135 0.2161 0.2328 0.0381  -0.0063 0.0149  189 TYR   A N   
1377 C CA  . TYR   A 189 ? 0.1623 0.2366 0.2442 0.0299  0.0040  -0.0037 189 TYR   A CA  
1378 C C   . TYR   A 189 ? 0.1935 0.2075 0.2537 0.0273  -0.0177 -0.0066 189 TYR   A C   
1379 O O   . TYR   A 189 ? 0.2377 0.1975 0.2825 -0.0128 -0.0344 0.0105  189 TYR   A O   
1380 C CB  . TYR   A 189 ? 0.2071 0.2662 0.2602 -0.0019 0.0059  -0.0473 189 TYR   A CB  
1381 C CG  . TYR   A 189 ? 0.1958 0.2591 0.2628 -0.0058 -0.0082 -0.0546 189 TYR   A CG  
1382 C CD1 . TYR   A 189 ? 0.2138 0.2737 0.2849 0.0759  -0.0235 -0.0431 189 TYR   A CD1 
1383 C CD2 . TYR   A 189 ? 0.2870 0.2709 0.2712 0.0051  0.0152  -0.0467 189 TYR   A CD2 
1384 C CE1 . TYR   A 189 ? 0.2479 0.3045 0.2811 0.0878  -0.0200 -0.0459 189 TYR   A CE1 
1385 C CE2 . TYR   A 189 ? 0.2763 0.3029 0.2901 0.0211  -0.0070 -0.0324 189 TYR   A CE2 
1386 C CZ  . TYR   A 189 ? 0.2612 0.2923 0.2876 0.0680  -0.0217 -0.0470 189 TYR   A CZ  
1387 O OH  . TYR   A 189 ? 0.2630 0.2562 0.2958 0.0487  -0.0110 -0.0520 189 TYR   A OH  
1388 N N   . ASP   A 190 ? 0.2257 0.1933 0.2310 0.0246  -0.0129 0.0008  190 ASP   A N   
1389 C CA  . ASP   A 190 ? 0.2003 0.2211 0.2587 -0.0168 -0.0161 0.0041  190 ASP   A CA  
1390 C C   . ASP   A 190 ? 0.1889 0.2196 0.2806 -0.0368 -0.0214 0.0020  190 ASP   A C   
1391 O O   . ASP   A 190 ? 0.2134 0.2303 0.2851 0.0003  -0.0043 0.0217  190 ASP   A O   
1392 C CB  . ASP   A 190 ? 0.2345 0.2424 0.2797 -0.0176 -0.0292 0.0190  190 ASP   A CB  
1393 C CG  . ASP   A 190 ? 0.2320 0.3145 0.3040 0.0497  -0.0238 0.0236  190 ASP   A CG  
1394 O OD1 . ASP   A 190 ? 0.2460 0.3392 0.2884 0.0267  -0.0207 0.0152  190 ASP   A OD1 
1395 O OD2 . ASP   A 190 ? 0.1981 0.3708 0.3485 0.0572  0.0095  0.0273  190 ASP   A OD2 
1396 N N   . GLU   A 191 ? 0.1707 0.2571 0.3269 -0.0272 -0.0205 0.0124  191 GLU   A N   
1397 C CA  . GLU   A 191 ? 0.1552 0.3035 0.3630 -0.0241 0.0421  -0.0253 191 GLU   A CA  
1398 C C   . GLU   A 191 ? 0.2129 0.2903 0.3640 -0.0304 0.0395  -0.0250 191 GLU   A C   
1399 O O   . GLU   A 191 ? 0.2756 0.2908 0.3786 -0.0518 0.0727  -0.0204 191 GLU   A O   
1400 C CB  . GLU   A 191 ? 0.1824 0.3942 0.3992 -0.0936 0.0424  -0.0494 191 GLU   A CB  
1401 C CG  . GLU   A 191 ? 0.4036 0.4573 0.4503 -0.0822 -0.0143 -0.0568 191 GLU   A CG  
1402 C CD  . GLU   A 191 ? 0.4757 0.4826 0.4971 -0.0360 -0.0123 -0.0411 191 GLU   A CD  
1403 O OE1 . GLU   A 191 ? 0.4082 0.4970 0.5041 0.0369  -0.0485 -0.0521 191 GLU   A OE1 
1404 O OE2 . GLU   A 191 ? 0.4403 0.4905 0.5256 -0.1132 0.0228  -0.0212 191 GLU   A OE2 
1405 N N   . ARG   A 192 ? 0.2181 0.2692 0.3627 0.0129  -0.0250 -0.0241 192 ARG   A N   
1406 C CA  . ARG   A 192 ? 0.3214 0.3123 0.3767 0.0210  0.0097  -0.0261 192 ARG   A CA  
1407 C C   . ARG   A 192 ? 0.2485 0.3088 0.3443 0.0123  0.0322  -0.0132 192 ARG   A C   
1408 O O   . ARG   A 192 ? 0.2941 0.3273 0.3627 0.0169  0.0643  -0.0230 192 ARG   A O   
1409 C CB  . ARG   A 192 ? 0.3676 0.3423 0.4295 0.0649  0.0066  -0.0175 192 ARG   A CB  
1410 C CG  . ARG   A 192 ? 0.4482 0.4495 0.4895 0.0662  -0.0245 -0.0005 192 ARG   A CG  
1411 C CD  . ARG   A 192 ? 0.4761 0.5365 0.5452 0.0452  -0.0298 0.0069  192 ARG   A CD  
1412 N NE  . ARG   A 192 ? 0.5173 0.5933 0.5913 0.0442  -0.0196 0.0158  192 ARG   A NE  
1413 C CZ  . ARG   A 192 ? 0.6411 0.6820 0.6450 0.0326  -0.0019 0.0057  192 ARG   A CZ  
1414 N NH1 . ARG   A 192 ? 0.6200 0.6696 0.6698 -0.0207 -0.0115 0.0079  192 ARG   A NH1 
1415 N NH2 . ARG   A 192 ? 0.7032 0.7331 0.6547 0.0704  0.0084  0.0014  192 ARG   A NH2 
1416 N N   . PHE   A 193 ? 0.2074 0.2804 0.3149 0.0070  0.0226  0.0019  193 PHE   A N   
1417 C CA  . PHE   A 193 ? 0.2580 0.2653 0.3013 -0.0015 0.0011  -0.0077 193 PHE   A CA  
1418 C C   . PHE   A 193 ? 0.3109 0.3114 0.3154 -0.0387 -0.0142 0.0018  193 PHE   A C   
1419 O O   . PHE   A 193 ? 0.3913 0.3399 0.3142 -0.1030 -0.0002 0.0048  193 PHE   A O   
1420 C CB  . PHE   A 193 ? 0.2250 0.2474 0.3059 -0.0113 -0.0151 -0.0228 193 PHE   A CB  
1421 C CG  . PHE   A 193 ? 0.2623 0.2475 0.3358 0.0208  0.0322  -0.0063 193 PHE   A CG  
1422 C CD1 . PHE   A 193 ? 0.3530 0.2762 0.3559 0.0036  0.0832  -0.0030 193 PHE   A CD1 
1423 C CD2 . PHE   A 193 ? 0.2385 0.2771 0.3525 -0.0260 0.0043  0.0470  193 PHE   A CD2 
1424 C CE1 . PHE   A 193 ? 0.2799 0.2556 0.3562 0.0335  0.1052  0.0247  193 PHE   A CE1 
1425 C CE2 . PHE   A 193 ? 0.2570 0.2774 0.3643 -0.0392 0.0516  0.0629  193 PHE   A CE2 
1426 C CZ  . PHE   A 193 ? 0.2972 0.2817 0.3700 -0.0053 0.0889  0.0590  193 PHE   A CZ  
1427 N N   . LYS   A 194 ? 0.2730 0.3001 0.3333 -0.0381 -0.0181 0.0028  194 LYS   A N   
1428 C CA  . LYS   A 194 ? 0.4010 0.3744 0.4061 -0.0089 -0.0139 0.0193  194 LYS   A CA  
1429 C C   . LYS   A 194 ? 0.4101 0.4225 0.4290 -0.0353 0.0027  0.0367  194 LYS   A C   
1430 O O   . LYS   A 194 ? 0.4632 0.5040 0.4226 -0.0790 -0.0517 0.0509  194 LYS   A O   
1431 C CB  . LYS   A 194 ? 0.4572 0.4269 0.4871 -0.0543 -0.0347 0.0058  194 LYS   A CB  
1432 C CG  . LYS   A 194 ? 0.5941 0.5554 0.5794 -0.0325 -0.0400 -0.0034 194 LYS   A CG  
1433 C CD  . LYS   A 194 ? 0.7277 0.6674 0.6629 -0.0183 -0.0356 -0.0135 194 LYS   A CD  
1434 C CE  . LYS   A 194 ? 0.7862 0.7642 0.7287 -0.0205 -0.0125 -0.0169 194 LYS   A CE  
1435 N NZ  . LYS   A 194 ? 0.8469 0.8283 0.7678 -0.0060 0.0087  -0.0093 194 LYS   A NZ  
1436 N N   . THR   A 195 ? 0.5031 0.4063 0.4512 -0.0961 0.0450  0.0084  195 THR   A N   
1437 C CA  . THR   A 195 ? 0.5911 0.4583 0.4813 -0.0593 0.0308  -0.0148 195 THR   A CA  
1438 C C   . THR   A 195 ? 0.5726 0.4177 0.4449 -0.0062 -0.0133 -0.0157 195 THR   A C   
1439 O O   . THR   A 195 ? 0.6968 0.4650 0.4629 0.0010  -0.0286 0.0029  195 THR   A O   
1440 C CB  . THR   A 195 ? 0.6358 0.5509 0.5332 -0.0548 0.0563  -0.0290 195 THR   A CB  
1441 O OG1 . THR   A 195 ? 0.6601 0.5793 0.5453 -0.0726 0.0883  -0.0495 195 THR   A OG1 
1442 C CG2 . THR   A 195 ? 0.6809 0.5982 0.5556 -0.0315 0.0547  -0.0208 195 THR   A CG2 
1443 N N   . LYS   A 196 ? 0.3233 0.3215 0.3831 0.0129  -0.0385 -0.0145 196 LYS   A N   
1444 C CA  . LYS   A 196 ? 0.3004 0.2999 0.3440 0.0071  -0.0182 -0.0100 196 LYS   A CA  
1445 C C   . LYS   A 196 ? 0.2673 0.2914 0.2976 0.0260  -0.0201 -0.0167 196 LYS   A C   
1446 O O   . LYS   A 196 ? 0.3108 0.3115 0.2997 0.0168  -0.0256 -0.0426 196 LYS   A O   
1447 C CB  . LYS   A 196 ? 0.3026 0.3010 0.3490 -0.0199 -0.0170 0.0143  196 LYS   A CB  
1448 C CG  . LYS   A 196 ? 0.3319 0.3158 0.3513 -0.0188 0.0228  0.0072  196 LYS   A CG  
1449 C CD  . LYS   A 196 ? 0.3097 0.3405 0.3487 0.0159  0.0808  0.0001  196 LYS   A CD  
1450 C CE  . LYS   A 196 ? 0.2952 0.3286 0.3397 -0.0129 0.0901  -0.0053 196 LYS   A CE  
1451 N NZ  . LYS   A 196 ? 0.2973 0.3067 0.3209 0.0276  0.0871  -0.0119 196 LYS   A NZ  
1452 N N   . ALA   A 197 ? 0.2654 0.2856 0.2609 0.0662  -0.0250 -0.0202 197 ALA   A N   
1453 C CA  . ALA   A 197 ? 0.2163 0.2828 0.2330 0.0636  -0.0271 -0.0207 197 ALA   A CA  
1454 C C   . ALA   A 197 ? 0.2744 0.2502 0.2404 0.0268  -0.0257 -0.0064 197 ALA   A C   
1455 O O   . ALA   A 197 ? 0.2960 0.2586 0.2691 0.0283  -0.0246 0.0069  197 ALA   A O   
1456 C CB  . ALA   A 197 ? 0.2971 0.2908 0.2240 0.0731  -0.0650 -0.0124 197 ALA   A CB  
1457 N N   . THR   A 198 ? 0.2621 0.2525 0.2132 0.0563  -0.0434 -0.0028 198 THR   A N   
1458 C CA  . THR   A 198 ? 0.2347 0.2581 0.1908 0.0617  -0.0210 0.0132  198 THR   A CA  
1459 C C   . THR   A 198 ? 0.2758 0.2347 0.1871 0.0514  0.0201  -0.0003 198 THR   A C   
1460 O O   . THR   A 198 ? 0.2861 0.2197 0.1904 0.0305  0.0147  -0.0022 198 THR   A O   
1461 C CB  . THR   A 198 ? 0.2143 0.3072 0.1866 0.1159  0.0095  0.0231  198 THR   A CB  
1462 O OG1 . THR   A 198 ? 0.2564 0.3295 0.1803 0.0642  0.0501  0.0069  198 THR   A OG1 
1463 C CG2 . THR   A 198 ? 0.2721 0.3424 0.1962 0.0898  0.0074  0.0134  198 THR   A CG2 
1464 N N   . LEU   A 199 ? 0.2575 0.2173 0.1726 0.0635  -0.0043 0.0053  199 LEU   A N   
1465 C CA  . LEU   A 199 ? 0.2700 0.2042 0.1730 0.0784  -0.0287 0.0219  199 LEU   A CA  
1466 C C   . LEU   A 199 ? 0.2872 0.2111 0.1943 0.0720  -0.0315 0.0147  199 LEU   A C   
1467 O O   . LEU   A 199 ? 0.2707 0.2299 0.2385 0.0741  0.0042  0.0198  199 LEU   A O   
1468 C CB  . LEU   A 199 ? 0.3376 0.1996 0.1812 0.0546  -0.0481 -0.0046 199 LEU   A CB  
1469 C CG  . LEU   A 199 ? 0.2800 0.2261 0.1845 0.0799  -0.0825 -0.0141 199 LEU   A CG  
1470 C CD1 . LEU   A 199 ? 0.3314 0.2147 0.1613 0.0535  -0.0579 -0.0352 199 LEU   A CD1 
1471 C CD2 . LEU   A 199 ? 0.3267 0.2257 0.2013 0.1068  -0.0594 -0.0114 199 LEU   A CD2 
1472 N N   . THR   A 200 ? 0.2618 0.2212 0.1896 0.0866  -0.0474 -0.0179 200 THR   A N   
1473 C CA  . THR   A 200 ? 0.2948 0.2201 0.2200 0.0875  -0.0471 -0.0242 200 THR   A CA  
1474 C C   . THR   A 200 ? 0.2597 0.2120 0.2358 0.0834  -0.0331 -0.0360 200 THR   A C   
1475 O O   . THR   A 200 ? 0.2525 0.2399 0.2237 0.0765  -0.0241 -0.0064 200 THR   A O   
1476 C CB  . THR   A 200 ? 0.3122 0.2724 0.2518 0.0572  -0.0422 -0.0071 200 THR   A CB  
1477 O OG1 . THR   A 200 ? 0.3405 0.2474 0.2824 0.0688  -0.0325 -0.0154 200 THR   A OG1 
1478 C CG2 . THR   A 200 ? 0.3034 0.3156 0.2407 0.0278  -0.0507 0.0343  200 THR   A CG2 
1479 N N   . VAL   A 201 ? 0.3074 0.2614 0.2516 0.1083  -0.0543 -0.0332 201 VAL   A N   
1480 C CA  A VAL   A 201 ? 0.2995 0.2773 0.2665 0.1213  -0.0613 0.0067  201 VAL   A CA  
1481 C CA  B VAL   A 201 ? 0.3035 0.2833 0.2707 0.1189  -0.0576 0.0054  201 VAL   A CA  
1482 C C   . VAL   A 201 ? 0.3108 0.3246 0.2778 0.0773  -0.0629 0.0156  201 VAL   A C   
1483 O O   . VAL   A 201 ? 0.3918 0.3589 0.2647 0.0473  -0.1272 0.0540  201 VAL   A O   
1484 C CB  A VAL   A 201 ? 0.3782 0.3076 0.2920 0.1584  -0.0301 0.0350  201 VAL   A CB  
1485 C CB  B VAL   A 201 ? 0.3817 0.3109 0.2943 0.1522  -0.0285 0.0322  201 VAL   A CB  
1486 C CG1 A VAL   A 201 ? 0.4218 0.3360 0.3027 0.1443  -0.0211 0.0412  201 VAL   A CG1 
1487 C CG1 B VAL   A 201 ? 0.4217 0.3374 0.3033 0.1369  -0.0197 0.0393  201 VAL   A CG1 
1488 C CG2 A VAL   A 201 ? 0.4386 0.2883 0.3059 0.1858  -0.0047 0.0348  201 VAL   A CG2 
1489 C CG2 B VAL   A 201 ? 0.4447 0.3021 0.3076 0.1724  -0.0058 0.0342  201 VAL   A CG2 
1490 N N   . ASP   A 202 ? 0.2363 0.3418 0.3061 0.0825  -0.0510 -0.0006 202 ASP   A N   
1491 C CA  . ASP   A 202 ? 0.1817 0.3648 0.3383 0.1000  -0.0829 -0.0293 202 ASP   A CA  
1492 C C   . ASP   A 202 ? 0.2016 0.3365 0.3630 0.0991  -0.1073 -0.0328 202 ASP   A C   
1493 O O   . ASP   A 202 ? 0.3050 0.3104 0.3775 0.0993  -0.0990 -0.0240 202 ASP   A O   
1494 C CB  . ASP   A 202 ? 0.2531 0.4148 0.3538 0.0768  -0.1189 -0.0423 202 ASP   A CB  
1495 C CG  . ASP   A 202 ? 0.4147 0.4656 0.3854 0.0322  -0.0966 -0.0246 202 ASP   A CG  
1496 O OD1 . ASP   A 202 ? 0.5008 0.5074 0.4087 -0.0326 -0.1271 -0.0259 202 ASP   A OD1 
1497 O OD2 . ASP   A 202 ? 0.4168 0.4718 0.3890 0.0161  -0.0603 -0.0282 202 ASP   A OD2 
1498 N N   . LYS   A 203 ? 0.3009 0.3620 0.3862 0.1127  -0.1008 -0.0226 203 LYS   A N   
1499 C CA  . LYS   A 203 ? 0.3390 0.3603 0.4050 0.0731  -0.0396 -0.0285 203 LYS   A CA  
1500 C C   . LYS   A 203 ? 0.3497 0.3566 0.4032 0.0654  -0.0710 -0.0286 203 LYS   A C   
1501 O O   . LYS   A 203 ? 0.2775 0.3791 0.4037 0.0916  -0.0773 -0.0591 203 LYS   A O   
1502 C CB  . LYS   A 203 ? 0.3738 0.3591 0.4260 0.0641  0.0119  -0.0275 203 LYS   A CB  
1503 C CG  . LYS   A 203 ? 0.3943 0.3685 0.4445 0.0608  0.0440  -0.0154 203 LYS   A CG  
1504 C CD  . LYS   A 203 ? 0.4234 0.3860 0.4607 0.0574  0.0217  -0.0123 203 LYS   A CD  
1505 C CE  . LYS   A 203 ? 0.5030 0.4536 0.4830 0.0316  -0.0120 -0.0316 203 LYS   A CE  
1506 N NZ  . LYS   A 203 ? 0.5970 0.4784 0.5008 0.0264  -0.0184 -0.0399 203 LYS   A NZ  
1507 N N   . PRO   A 204 ? 0.4102 0.3977 0.4069 0.0248  -0.0873 -0.0192 204 PRO   A N   
1508 C CA  . PRO   A 204 ? 0.3903 0.4416 0.4073 -0.0171 -0.0954 -0.0261 204 PRO   A CA  
1509 C C   . PRO   A 204 ? 0.3793 0.4721 0.3961 0.0148  -0.0877 -0.0575 204 PRO   A C   
1510 O O   . PRO   A 204 ? 0.3359 0.5275 0.4071 0.0467  -0.0526 -0.0612 204 PRO   A O   
1511 C CB  . PRO   A 204 ? 0.4072 0.4449 0.4122 -0.0248 -0.0840 -0.0025 204 PRO   A CB  
1512 C CG  . PRO   A 204 ? 0.2934 0.4318 0.4023 -0.0160 -0.1296 0.0051  204 PRO   A CG  
1513 C CD  . PRO   A 204 ? 0.3810 0.4236 0.3987 0.0205  -0.0983 0.0029  204 PRO   A CD  
1514 N N   . SER   A 205 ? 0.3471 0.4513 0.3637 0.0576  -0.1317 -0.0803 205 SER   A N   
1515 C CA  . SER   A 205 ? 0.3120 0.4077 0.3404 0.0412  -0.1243 -0.0848 205 SER   A CA  
1516 C C   . SER   A 205 ? 0.2916 0.3833 0.3324 0.0003  -0.1204 -0.0930 205 SER   A C   
1517 O O   . SER   A 205 ? 0.3269 0.4184 0.3377 0.0182  -0.1127 -0.0992 205 SER   A O   
1518 C CB  . SER   A 205 ? 0.3859 0.4249 0.3316 0.0208  -0.0822 -0.0924 205 SER   A CB  
1519 O OG  . SER   A 205 ? 0.3916 0.4243 0.3094 0.0538  -0.0713 -0.1190 205 SER   A OG  
1520 N N   . SER   A 206 ? 0.2594 0.3589 0.3323 0.0779  -0.1365 -0.0814 206 SER   A N   
1521 C CA  . SER   A 206 ? 0.2535 0.3490 0.3380 0.1151  -0.0955 -0.0612 206 SER   A CA  
1522 C C   . SER   A 206 ? 0.2052 0.2899 0.3224 0.0493  -0.0624 -0.0538 206 SER   A C   
1523 O O   . SER   A 206 ? 0.2847 0.2933 0.3247 0.0154  -0.0773 -0.0413 206 SER   A O   
1524 C CB  . SER   A 206 ? 0.2631 0.4039 0.3699 0.1041  -0.0862 -0.0424 206 SER   A CB  
1525 O OG  . SER   A 206 ? 0.2574 0.4690 0.3970 0.0924  -0.0491 -0.0494 206 SER   A OG  
1526 N N   . THR   A 207 ? 0.2061 0.2929 0.3171 0.0460  -0.0640 -0.0732 207 THR   A N   
1527 C CA  . THR   A 207 ? 0.2074 0.2884 0.3068 0.0611  -0.0586 -0.0408 207 THR   A CA  
1528 C C   . THR   A 207 ? 0.2350 0.2725 0.2788 0.0438  -0.0774 -0.0143 207 THR   A C   
1529 O O   . THR   A 207 ? 0.3051 0.3165 0.2891 0.0421  -0.1221 0.0041  207 THR   A O   
1530 C CB  . THR   A 207 ? 0.2204 0.3010 0.3212 0.0523  -0.0737 -0.0384 207 THR   A CB  
1531 O OG1 . THR   A 207 ? 0.2942 0.3030 0.3184 0.0333  -0.0889 -0.0211 207 THR   A OG1 
1532 C CG2 . THR   A 207 ? 0.2595 0.2902 0.3278 0.0843  -0.0938 -0.0359 207 THR   A CG2 
1533 N N   . ALA   A 208 ? 0.2059 0.2630 0.2661 0.0616  -0.0999 -0.0338 208 ALA   A N   
1534 C CA  . ALA   A 208 ? 0.2026 0.2670 0.2454 0.0233  -0.0891 -0.0435 208 ALA   A CA  
1535 C C   . ALA   A 208 ? 0.1938 0.2290 0.2369 0.0359  -0.0547 -0.0218 208 ALA   A C   
1536 O O   . ALA   A 208 ? 0.2702 0.2239 0.2426 0.0067  -0.0698 -0.0206 208 ALA   A O   
1537 C CB  . ALA   A 208 ? 0.2884 0.3104 0.2393 0.0359  -0.0944 -0.0583 208 ALA   A CB  
1538 N N   . TYR   A 209 ? 0.1994 0.2364 0.2201 0.0542  -0.0342 -0.0278 209 TYR   A N   
1539 C CA  . TYR   A 209 ? 0.1936 0.2252 0.2331 0.0479  -0.0545 0.0010  209 TYR   A CA  
1540 C C   . TYR   A 209 ? 0.2174 0.2132 0.2411 0.0601  -0.0771 0.0052  209 TYR   A C   
1541 O O   . TYR   A 209 ? 0.2338 0.2104 0.2679 0.0622  -0.0460 0.0046  209 TYR   A O   
1542 C CB  . TYR   A 209 ? 0.2492 0.2761 0.2394 0.0318  -0.0517 -0.0038 209 TYR   A CB  
1543 C CG  . TYR   A 209 ? 0.2543 0.2920 0.2529 0.0273  -0.0773 -0.0166 209 TYR   A CG  
1544 C CD1 . TYR   A 209 ? 0.3138 0.2959 0.2727 0.0007  -0.0968 -0.0336 209 TYR   A CD1 
1545 C CD2 . TYR   A 209 ? 0.2451 0.3054 0.2707 -0.0045 -0.0955 -0.0108 209 TYR   A CD2 
1546 C CE1 . TYR   A 209 ? 0.3314 0.3352 0.2921 0.0264  -0.0990 -0.0380 209 TYR   A CE1 
1547 C CE2 . TYR   A 209 ? 0.2938 0.3373 0.2936 -0.0183 -0.0955 -0.0382 209 TYR   A CE2 
1548 C CZ  . TYR   A 209 ? 0.3388 0.3788 0.3028 -0.0083 -0.1078 -0.0431 209 TYR   A CZ  
1549 O OH  . TYR   A 209 ? 0.3706 0.4329 0.3228 -0.0270 -0.0910 -0.0418 209 TYR   A OH  
1550 N N   . MET   A 210 ? 0.1973 0.2013 0.2201 0.0348  -0.0536 0.0066  210 MET   A N   
1551 C CA  . MET   A 210 ? 0.2170 0.2343 0.2031 0.0488  -0.0299 0.0009  210 MET   A CA  
1552 C C   . MET   A 210 ? 0.2492 0.2214 0.2092 0.0412  -0.0128 0.0055  210 MET   A C   
1553 O O   . MET   A 210 ? 0.3144 0.2018 0.2259 0.0339  -0.0281 0.0205  210 MET   A O   
1554 C CB  . MET   A 210 ? 0.1542 0.2510 0.1863 -0.0112 -0.0237 0.0139  210 MET   A CB  
1555 C CG  . MET   A 210 ? 0.1740 0.2689 0.1928 -0.0068 -0.0393 -0.0010 210 MET   A CG  
1556 S SD  . MET   A 210 ? 0.2411 0.2498 0.2206 0.0265  -0.0173 0.0010  210 MET   A SD  
1557 C CE  . MET   A 210 ? 0.2949 0.2170 0.2356 0.0388  -0.0034 0.0064  210 MET   A CE  
1558 N N   . GLN   A 211 ? 0.2401 0.2324 0.1995 0.0448  -0.0133 0.0096  211 GLN   A N   
1559 C CA  . GLN   A 211 ? 0.3027 0.2183 0.1990 0.0649  0.0229  0.0228  211 GLN   A CA  
1560 C C   . GLN   A 211 ? 0.3112 0.2162 0.2261 0.0571  -0.0093 0.0202  211 GLN   A C   
1561 O O   . GLN   A 211 ? 0.2846 0.2155 0.2393 0.0412  -0.0077 -0.0009 211 GLN   A O   
1562 C CB  . GLN   A 211 ? 0.3575 0.2671 0.1946 0.0768  0.0853  0.0444  211 GLN   A CB  
1563 C CG  . GLN   A 211 ? 0.4197 0.3358 0.2367 0.0573  0.0688  0.0574  211 GLN   A CG  
1564 C CD  . GLN   A 211 ? 0.4394 0.4138 0.3077 0.0075  0.0016  0.0697  211 GLN   A CD  
1565 O OE1 . GLN   A 211 ? 0.4573 0.4948 0.3243 0.0156  -0.0492 0.0744  211 GLN   A OE1 
1566 N NE2 . GLN   A 211 ? 0.4242 0.3985 0.3357 0.0296  -0.0467 0.0682  211 GLN   A NE2 
1567 N N   . LEU   A 212 ? 0.2872 0.2234 0.2195 0.0694  -0.0174 0.0309  212 LEU   A N   
1568 C CA  . LEU   A 212 ? 0.2787 0.2388 0.2137 0.0892  0.0234  0.0377  212 LEU   A CA  
1569 C C   . LEU   A 212 ? 0.3041 0.2607 0.2316 0.1071  0.0395  0.0208  212 LEU   A C   
1570 O O   . LEU   A 212 ? 0.3709 0.2647 0.2349 0.0920  0.0334  0.0162  212 LEU   A O   
1571 C CB  . LEU   A 212 ? 0.3166 0.2129 0.2026 0.0957  0.0029  0.0137  212 LEU   A CB  
1572 C CG  . LEU   A 212 ? 0.3649 0.2140 0.1980 0.0844  -0.0206 0.0090  212 LEU   A CG  
1573 C CD1 . LEU   A 212 ? 0.4210 0.2335 0.2013 0.0887  -0.0294 0.0258  212 LEU   A CD1 
1574 C CD2 . LEU   A 212 ? 0.3098 0.2287 0.2175 0.0290  -0.0192 -0.0281 212 LEU   A CD2 
1575 N N   . SER   A 213 ? 0.3306 0.2802 0.2447 0.0990  0.0339  0.0494  213 SER   A N   
1576 C CA  . SER   A 213 ? 0.3565 0.2800 0.2598 0.0826  0.0351  0.0784  213 SER   A CA  
1577 C C   . SER   A 213 ? 0.3419 0.2940 0.2585 0.0614  0.0486  0.0707  213 SER   A C   
1578 O O   . SER   A 213 ? 0.3788 0.3135 0.2640 0.0516  0.0107  0.0514  213 SER   A O   
1579 C CB  . SER   A 213 ? 0.4607 0.3111 0.2893 0.0109  0.0056  0.0984  213 SER   A CB  
1580 O OG  . SER   A 213 ? 0.5692 0.3364 0.3287 -0.0142 0.0248  0.0779  213 SER   A OG  
1581 N N   . SER   A 214 ? 0.3638 0.3112 0.2699 0.0933  0.0860  0.0818  214 SER   A N   
1582 C CA  . SER   A 214 ? 0.3736 0.3609 0.3103 0.0614  0.0614  0.0867  214 SER   A CA  
1583 C C   . SER   A 214 ? 0.3341 0.3652 0.2759 0.0662  0.0469  0.0711  214 SER   A C   
1584 O O   . SER   A 214 ? 0.3410 0.3787 0.2964 0.0573  0.0568  0.0632  214 SER   A O   
1585 C CB  . SER   A 214 ? 0.4635 0.4281 0.3834 0.0312  0.0171  0.1318  214 SER   A CB  
1586 O OG  . SER   A 214 ? 0.4893 0.4715 0.4244 0.0426  0.0128  0.1636  214 SER   A OG  
1587 N N   . LEU   A 215 ? 0.3062 0.3706 0.2411 0.0940  0.0568  0.0753  215 LEU   A N   
1588 C CA  . LEU   A 215 ? 0.3076 0.3479 0.2283 0.1003  0.0472  0.0688  215 LEU   A CA  
1589 C C   . LEU   A 215 ? 0.3568 0.3475 0.2505 0.0915  0.0734  0.0657  215 LEU   A C   
1590 O O   . LEU   A 215 ? 0.3977 0.3734 0.2490 0.1089  0.0985  0.0781  215 LEU   A O   
1591 C CB  . LEU   A 215 ? 0.3074 0.3367 0.2176 0.0508  0.0599  0.0538  215 LEU   A CB  
1592 C CG  . LEU   A 215 ? 0.2764 0.3447 0.2183 0.0532  0.0464  0.0388  215 LEU   A CG  
1593 C CD1 . LEU   A 215 ? 0.3686 0.3310 0.2268 0.0206  -0.0147 0.0209  215 LEU   A CD1 
1594 C CD2 . LEU   A 215 ? 0.3142 0.3546 0.2100 0.0021  0.0707  0.0392  215 LEU   A CD2 
1595 N N   . THR   A 216 ? 0.3243 0.3223 0.2725 0.0865  0.0732  0.0490  216 THR   A N   
1596 C CA  . THR   A 216 ? 0.2643 0.3624 0.2991 0.0851  0.0561  0.0571  216 THR   A CA  
1597 C C   . THR   A 216 ? 0.2400 0.3344 0.2976 0.1013  0.0368  0.0564  216 THR   A C   
1598 O O   . THR   A 216 ? 0.2609 0.3297 0.2983 0.0964  0.0129  0.0178  216 THR   A O   
1599 C CB  . THR   A 216 ? 0.3935 0.4019 0.3344 -0.0057 0.0609  0.0587  216 THR   A CB  
1600 O OG1 . THR   A 216 ? 0.3982 0.4211 0.3470 0.0312  0.0206  0.0366  216 THR   A OG1 
1601 C CG2 . THR   A 216 ? 0.4831 0.4141 0.3566 -0.0323 0.0823  0.0798  216 THR   A CG2 
1602 N N   . SER   A 217 ? 0.2730 0.3386 0.3143 0.0794  0.0315  0.0636  217 SER   A N   
1603 C CA  A SER   A 217 ? 0.2682 0.3346 0.3271 0.0866  0.0302  0.0494  217 SER   A CA  
1604 C CA  B SER   A 217 ? 0.2608 0.3279 0.3294 0.0820  0.0144  0.0376  217 SER   A CA  
1605 C C   . SER   A 217 ? 0.2588 0.3344 0.3231 0.0634  0.0325  0.0477  217 SER   A C   
1606 O O   . SER   A 217 ? 0.3601 0.3684 0.3166 0.1185  0.0519  0.0758  217 SER   A O   
1607 C CB  A SER   A 217 ? 0.2989 0.3382 0.3400 0.0789  0.0295  0.0216  217 SER   A CB  
1608 C CB  B SER   A 217 ? 0.2765 0.3184 0.3456 0.0592  -0.0311 -0.0125 217 SER   A CB  
1609 O OG  A SER   A 217 ? 0.3008 0.3199 0.3381 0.0702  0.0588  0.0151  217 SER   A OG  
1610 O OG  B SER   A 217 ? 0.2871 0.2863 0.3459 0.0382  -0.0437 -0.0383 217 SER   A OG  
1611 N N   . ASP   A 218 ? 0.2836 0.3315 0.3204 0.0238  0.0306  0.0101  218 ASP   A N   
1612 C CA  . ASP   A 218 ? 0.2895 0.3356 0.3264 0.0119  0.0413  -0.0164 218 ASP   A CA  
1613 C C   . ASP   A 218 ? 0.2657 0.3395 0.2904 0.0211  0.0284  0.0011  218 ASP   A C   
1614 O O   . ASP   A 218 ? 0.2743 0.3819 0.2961 0.0396  0.0216  -0.0059 218 ASP   A O   
1615 C CB  . ASP   A 218 ? 0.3743 0.4175 0.3752 -0.0017 0.0150  -0.0316 218 ASP   A CB  
1616 C CG  . ASP   A 218 ? 0.4531 0.4699 0.4218 0.0020  -0.0154 -0.0421 218 ASP   A CG  
1617 O OD1 . ASP   A 218 ? 0.4230 0.5116 0.4357 -0.0201 -0.0338 -0.0515 218 ASP   A OD1 
1618 O OD2 . ASP   A 218 ? 0.5125 0.4923 0.4427 0.0133  -0.0137 -0.0329 218 ASP   A OD2 
1619 N N   . ASP   A 219 ? 0.2083 0.2962 0.2420 0.0198  0.0439  0.0409  219 ASP   A N   
1620 C CA  . ASP   A 219 ? 0.2284 0.2413 0.2259 0.0172  0.0430  0.0127  219 ASP   A CA  
1621 C C   . ASP   A 219 ? 0.2447 0.2235 0.2262 0.0258  0.0258  -0.0010 219 ASP   A C   
1622 O O   . ASP   A 219 ? 0.2352 0.2328 0.2382 0.0138  0.0207  -0.0112 219 ASP   A O   
1623 C CB  . ASP   A 219 ? 0.2688 0.2274 0.2185 0.0088  0.0226  0.0068  219 ASP   A CB  
1624 C CG  . ASP   A 219 ? 0.3088 0.2709 0.2188 0.0092  0.0428  -0.0035 219 ASP   A CG  
1625 O OD1 . ASP   A 219 ? 0.3546 0.2875 0.2341 0.0147  0.0133  -0.0247 219 ASP   A OD1 
1626 O OD2 . ASP   A 219 ? 0.3411 0.2846 0.2191 0.0316  0.0669  0.0171  219 ASP   A OD2 
1627 N N   . SER   A 220 ? 0.2291 0.2246 0.2204 0.0099  -0.0029 0.0150  220 SER   A N   
1628 C CA  . SER   A 220 ? 0.2239 0.2076 0.2231 0.0455  0.0255  -0.0108 220 SER   A CA  
1629 C C   . SER   A 220 ? 0.1861 0.2478 0.2149 0.0257  0.0204  -0.0099 220 SER   A C   
1630 O O   . SER   A 220 ? 0.1974 0.3095 0.2066 0.0133  -0.0047 0.0013  220 SER   A O   
1631 C CB  . SER   A 220 ? 0.2104 0.2238 0.2370 0.0548  0.0131  -0.0168 220 SER   A CB  
1632 O OG  . SER   A 220 ? 0.2625 0.2425 0.2424 0.0314  0.0171  -0.0244 220 SER   A OG  
1633 N N   . ALA   A 221 ? 0.1946 0.1890 0.2020 -0.0017 0.0290  -0.0046 221 ALA   A N   
1634 C CA  . ALA   A 221 ? 0.1595 0.2054 0.2016 0.0048  -0.0019 -0.0020 221 ALA   A CA  
1635 C C   . ALA   A 221 ? 0.1821 0.1872 0.1906 0.0376  0.0047  0.0042  221 ALA   A C   
1636 O O   . ALA   A 221 ? 0.2284 0.2023 0.1805 0.0174  -0.0265 -0.0127 221 ALA   A O   
1637 C CB  . ALA   A 221 ? 0.2202 0.2294 0.2130 -0.0364 -0.0325 0.0147  221 ALA   A CB  
1638 N N   . VAL   A 222 ? 0.1787 0.1841 0.1941 0.0356  -0.0171 0.0035  222 VAL   A N   
1639 C CA  . VAL   A 222 ? 0.1890 0.1688 0.2050 0.0316  -0.0207 0.0146  222 VAL   A CA  
1640 C C   . VAL   A 222 ? 0.2118 0.1640 0.2060 -0.0147 -0.0406 -0.0026 222 VAL   A C   
1641 O O   . VAL   A 222 ? 0.1909 0.1802 0.2070 -0.0093 -0.0415 -0.0183 222 VAL   A O   
1642 C CB  . VAL   A 222 ? 0.2223 0.1877 0.2159 0.0129  -0.0114 0.0353  222 VAL   A CB  
1643 C CG1 . VAL   A 222 ? 0.1801 0.2251 0.2376 -0.0029 -0.0374 0.0329  222 VAL   A CG1 
1644 C CG2 . VAL   A 222 ? 0.2744 0.1708 0.2238 0.0323  -0.0490 0.0308  222 VAL   A CG2 
1645 N N   . TYR   A 223 ? 0.1845 0.1851 0.1939 0.0357  -0.0402 0.0062  223 TYR   A N   
1646 C CA  . TYR   A 223 ? 0.1607 0.1468 0.1852 0.0258  -0.0285 0.0104  223 TYR   A CA  
1647 C C   . TYR   A 223 ? 0.1532 0.1456 0.1827 0.0095  -0.0360 -0.0152 223 TYR   A C   
1648 O O   . TYR   A 223 ? 0.1846 0.1839 0.2204 -0.0040 -0.0271 -0.0159 223 TYR   A O   
1649 C CB  . TYR   A 223 ? 0.1973 0.1705 0.1815 0.0545  -0.0066 0.0070  223 TYR   A CB  
1650 C CG  . TYR   A 223 ? 0.1828 0.1937 0.1825 0.0519  0.0004  -0.0034 223 TYR   A CG  
1651 C CD1 . TYR   A 223 ? 0.1705 0.1929 0.1766 0.0263  0.0080  -0.0034 223 TYR   A CD1 
1652 C CD2 . TYR   A 223 ? 0.1912 0.1898 0.1930 0.0067  0.0137  -0.0020 223 TYR   A CD2 
1653 C CE1 . TYR   A 223 ? 0.2087 0.1954 0.1792 0.0076  -0.0108 0.0129  223 TYR   A CE1 
1654 C CE2 . TYR   A 223 ? 0.1948 0.2044 0.1942 0.0315  0.0016  -0.0126 223 TYR   A CE2 
1655 C CZ  . TYR   A 223 ? 0.1601 0.2115 0.1992 0.0266  -0.0018 0.0049  223 TYR   A CZ  
1656 O OH  . TYR   A 223 ? 0.1735 0.2532 0.2201 0.0335  -0.0017 0.0199  223 TYR   A OH  
1657 N N   . PHE   A 224 ? 0.1720 0.1829 0.1799 0.0175  -0.0152 -0.0264 224 PHE   A N   
1658 C CA  . PHE   A 224 ? 0.1598 0.1948 0.1991 0.0221  -0.0104 -0.0094 224 PHE   A CA  
1659 C C   . PHE   A 224 ? 0.1394 0.2010 0.2027 0.0174  -0.0191 -0.0233 224 PHE   A C   
1660 O O   . PHE   A 224 ? 0.1550 0.2113 0.2142 -0.0120 -0.0056 -0.0285 224 PHE   A O   
1661 C CB  . PHE   A 224 ? 0.2185 0.2060 0.1867 0.0094  -0.0182 -0.0148 224 PHE   A CB  
1662 C CG  . PHE   A 224 ? 0.1879 0.2133 0.1820 0.0061  -0.0120 -0.0150 224 PHE   A CG  
1663 C CD1 . PHE   A 224 ? 0.2673 0.1976 0.1831 0.0004  -0.0100 0.0112  224 PHE   A CD1 
1664 C CD2 . PHE   A 224 ? 0.2182 0.2739 0.2163 0.0618  -0.0287 0.0012  224 PHE   A CD2 
1665 C CE1 . PHE   A 224 ? 0.3405 0.2214 0.1915 0.0579  -0.0144 0.0154  224 PHE   A CE1 
1666 C CE2 . PHE   A 224 ? 0.2961 0.2994 0.2210 0.1070  -0.0311 0.0140  224 PHE   A CE2 
1667 C CZ  . PHE   A 224 ? 0.3805 0.2683 0.2119 0.1053  -0.0409 0.0265  224 PHE   A CZ  
1668 N N   . CYS   A 225 ? 0.1588 0.1905 0.2137 0.0271  -0.0238 -0.0159 225 CYS   A N   
1669 C CA  . CYS   A 225 ? 0.1430 0.1965 0.2302 0.0342  -0.0408 -0.0068 225 CYS   A CA  
1670 C C   . CYS   A 225 ? 0.1732 0.1887 0.2209 -0.0019 -0.0309 -0.0109 225 CYS   A C   
1671 O O   . CYS   A 225 ? 0.1920 0.1621 0.2111 -0.0275 -0.0348 0.0005  225 CYS   A O   
1672 C CB  . CYS   A 225 ? 0.1729 0.2103 0.2454 -0.0336 -0.0514 -0.0135 225 CYS   A CB  
1673 S SG  . CYS   A 225 ? 0.2233 0.2483 0.2458 0.0085  -0.0401 -0.0123 225 CYS   A SG  
1674 N N   . ALA   A 226 ? 0.1717 0.1969 0.2145 0.0050  -0.0030 -0.0031 226 ALA   A N   
1675 C CA  . ALA   A 226 ? 0.1740 0.2143 0.2048 0.0294  -0.0179 0.0050  226 ALA   A CA  
1676 C C   . ALA   A 226 ? 0.1519 0.1970 0.2050 0.0456  -0.0142 0.0058  226 ALA   A C   
1677 O O   . ALA   A 226 ? 0.2058 0.1904 0.2193 0.0019  0.0187  0.0195  226 ALA   A O   
1678 C CB  . ALA   A 226 ? 0.2113 0.2047 0.1959 0.0271  -0.0494 0.0028  226 ALA   A CB  
1679 N N   . ARG   A 227 ? 0.1446 0.2026 0.2127 0.0328  -0.0185 0.0044  227 ARG   A N   
1680 C CA  A ARG   A 227 ? 0.1715 0.2018 0.2138 0.0477  -0.0087 0.0048  227 ARG   A CA  
1681 C CA  B ARG   A 227 ? 0.1864 0.2153 0.2111 0.0303  -0.0140 -0.0045 227 ARG   A CA  
1682 C C   . ARG   A 227 ? 0.1820 0.2053 0.2140 0.0576  -0.0327 -0.0194 227 ARG   A C   
1683 O O   . ARG   A 227 ? 0.2445 0.2440 0.2198 0.0594  -0.0874 -0.0098 227 ARG   A O   
1684 C CB  A ARG   A 227 ? 0.1992 0.2247 0.2386 0.0432  0.0292  0.0396  227 ARG   A CB  
1685 C CB  B ARG   A 227 ? 0.2276 0.2463 0.2173 0.0017  0.0081  0.0115  227 ARG   A CB  
1686 C CG  A ARG   A 227 ? 0.2159 0.1859 0.2423 0.0302  0.0366  0.0308  227 ARG   A CG  
1687 C CG  B ARG   A 227 ? 0.2353 0.2366 0.2066 -0.0203 0.0036  0.0100  227 ARG   A CG  
1688 C CD  A ARG   A 227 ? 0.2094 0.2496 0.2403 -0.0187 0.0213  0.0141  227 ARG   A CD  
1689 C CD  B ARG   A 227 ? 0.1560 0.2553 0.2090 0.0023  -0.0222 0.0047  227 ARG   A CD  
1690 N NE  A ARG   A 227 ? 0.1772 0.2679 0.2307 -0.0083 0.0230  -0.0019 227 ARG   A NE  
1691 N NE  B ARG   A 227 ? 0.1472 0.2483 0.2147 0.0165  -0.0053 0.0211  227 ARG   A NE  
1692 C CZ  A ARG   A 227 ? 0.2164 0.2537 0.2395 0.0005  -0.0159 -0.0080 227 ARG   A CZ  
1693 C CZ  B ARG   A 227 ? 0.2263 0.2204 0.2251 0.0008  0.0052  0.0145  227 ARG   A CZ  
1694 N NH1 A ARG   A 227 ? 0.2486 0.2219 0.2600 -0.0311 -0.0521 -0.0135 227 ARG   A NH1 
1695 N NH1 B ARG   A 227 ? 0.1934 0.1856 0.2351 0.0238  0.0156  -0.0196 227 ARG   A NH1 
1696 N NH2 A ARG   A 227 ? 0.1767 0.2477 0.2312 0.0468  -0.0048 -0.0256 227 ARG   A NH2 
1697 N NH2 B ARG   A 227 ? 0.2903 0.2208 0.2323 -0.0104 -0.0015 0.0479  227 ARG   A NH2 
1698 N N   . GLY   A 228 ? 0.2136 0.1926 0.2311 0.0269  -0.0404 -0.0359 228 GLY   A N   
1699 C CA  . GLY   A 228 ? 0.2653 0.1906 0.2721 0.0697  -0.0344 -0.0322 228 GLY   A CA  
1700 C C   . GLY   A 228 ? 0.2540 0.2190 0.2972 0.0312  -0.0105 -0.0397 228 GLY   A C   
1701 O O   . GLY   A 228 ? 0.2275 0.2298 0.2538 0.0469  -0.0166 -0.0260 228 GLY   A O   
1702 N N   . CYS   A 229 ? 0.2478 0.2515 0.3853 0.0819  -0.0661 -0.0513 229 CYS   A N   
1703 C CA  . CYS   A 229 ? 0.3550 0.3801 0.5188 0.0637  -0.0740 -0.0594 229 CYS   A CA  
1704 C C   . CYS   A 229 ? 0.2818 0.2802 0.4082 0.0620  -0.0348 -0.0532 229 CYS   A C   
1705 O O   . CYS   A 229 ? 0.3391 0.2070 0.3659 0.0797  -0.0412 -0.0663 229 CYS   A O   
1706 C CB  . CYS   A 229 ? 0.6009 0.6943 0.7688 0.0603  -0.0468 -0.0635 229 CYS   A CB  
1707 S SG  . CYS   A 229 ? 1.0319 0.9697 0.9313 0.0740  -0.0167 -0.0535 229 CYS   A SG  
1708 N N   . TYR   A 230 ? 0.3096 0.2325 0.3519 0.0534  0.0191  -0.0262 230 TYR   A N   
1709 C CA  . TYR   A 230 ? 0.3579 0.2010 0.3061 0.0491  0.0269  -0.0048 230 TYR   A CA  
1710 C C   . TYR   A 230 ? 0.3008 0.2143 0.2826 0.0857  0.0138  -0.0048 230 TYR   A C   
1711 O O   . TYR   A 230 ? 0.2808 0.2515 0.2748 0.0886  -0.0190 -0.0206 230 TYR   A O   
1712 C CB  . TYR   A 230 ? 0.3752 0.1700 0.3043 0.0427  0.0150  0.0057  230 TYR   A CB  
1713 C CG  . TYR   A 230 ? 0.3419 0.2187 0.3327 0.0638  0.0231  0.0045  230 TYR   A CG  
1714 C CD1 . TYR   A 230 ? 0.3236 0.2754 0.3624 0.0251  0.0017  -0.0284 230 TYR   A CD1 
1715 C CD2 . TYR   A 230 ? 0.3603 0.2537 0.3508 0.0201  0.0119  0.0000  230 TYR   A CD2 
1716 C CE1 . TYR   A 230 ? 0.3257 0.2858 0.3932 0.0004  -0.0182 -0.0444 230 TYR   A CE1 
1717 C CE2 . TYR   A 230 ? 0.3693 0.2532 0.3830 0.0010  -0.0113 -0.0189 230 TYR   A CE2 
1718 C CZ  . TYR   A 230 ? 0.3727 0.2938 0.4152 0.0124  -0.0463 -0.0545 230 TYR   A CZ  
1719 O OH  . TYR   A 230 ? 0.4613 0.2961 0.4663 0.0284  -0.0455 -0.0712 230 TYR   A OH  
1720 N N   . GLY   A 231 ? 0.2801 0.1902 0.2726 0.0388  0.0091  0.0271  231 GLY   A N   
1721 C CA  . GLY   A 231 ? 0.3027 0.2261 0.2996 0.0429  0.0003  0.0131  231 GLY   A CA  
1722 C C   . GLY   A 231 ? 0.2826 0.2906 0.3411 0.0472  0.0141  -0.0034 231 GLY   A C   
1723 O O   . GLY   A 231 ? 0.2624 0.3542 0.3440 0.0391  0.0482  0.0200  231 GLY   A O   
1724 N N   . CYS   A 232 ? 0.2297 0.2931 0.3845 0.0136  -0.0178 -0.0121 232 CYS   A N   
1725 C CA  . CYS   A 232 ? 0.3650 0.3567 0.4421 -0.0109 -0.0133 0.0242  232 CYS   A CA  
1726 C C   . CYS   A 232 ? 0.2798 0.2927 0.3563 0.0015  0.0112  0.0163  232 CYS   A C   
1727 O O   . CYS   A 232 ? 0.3119 0.2601 0.3535 0.0215  0.0126  -0.0143 232 CYS   A O   
1728 C CB  . CYS   A 232 ? 0.5618 0.5377 0.5889 0.0229  -0.0410 0.0558  232 CYS   A CB  
1729 S SG  . CYS   A 232 ? 0.7719 0.7203 0.6982 0.0705  -0.0653 0.0707  232 CYS   A SG  
1730 N N   . ILE   A 233 ? 0.1879 0.3065 0.2837 0.0131  0.0356  0.0148  233 ILE   A N   
1731 C CA  . ILE   A 233 ? 0.1772 0.2759 0.2522 0.0567  -0.0211 -0.0003 233 ILE   A CA  
1732 C C   . ILE   A 233 ? 0.2142 0.3006 0.2526 0.0391  -0.0216 -0.0194 233 ILE   A C   
1733 O O   . ILE   A 233 ? 0.2232 0.3017 0.2758 -0.0040 -0.0135 0.0000  233 ILE   A O   
1734 C CB  . ILE   A 233 ? 0.2092 0.2812 0.2453 0.0144  0.0219  -0.0076 233 ILE   A CB  
1735 C CG1 . ILE   A 233 ? 0.2097 0.3015 0.2600 0.0329  0.0075  -0.0413 233 ILE   A CG1 
1736 C CG2 . ILE   A 233 ? 0.2476 0.2923 0.2559 0.0458  0.0148  -0.0312 233 ILE   A CG2 
1737 C CD1 . ILE   A 233 ? 0.2619 0.3084 0.2584 0.0313  -0.0185 -0.0523 233 ILE   A CD1 
1738 N N   . HIS   A 234 ? 0.2037 0.2120 0.2201 0.0393  -0.0052 -0.0190 234 HIS   A N   
1739 C CA  . HIS   A 234 ? 0.2005 0.1551 0.2019 0.0201  0.0211  0.0000  234 HIS   A CA  
1740 C C   . HIS   A 234 ? 0.1725 0.1583 0.2003 0.0277  0.0186  0.0030  234 HIS   A C   
1741 O O   . HIS   A 234 ? 0.1689 0.1913 0.1963 0.0143  0.0136  0.0084  234 HIS   A O   
1742 C CB  . HIS   A 234 ? 0.1547 0.1536 0.2095 -0.0014 -0.0018 0.0129  234 HIS   A CB  
1743 C CG  . HIS   A 234 ? 0.1660 0.1510 0.1918 0.0018  0.0135  0.0200  234 HIS   A CG  
1744 N ND1 . HIS   A 234 ? 0.2111 0.1703 0.2074 0.0340  -0.0058 0.0075  234 HIS   A ND1 
1745 C CD2 . HIS   A 234 ? 0.1964 0.1803 0.1923 0.0107  0.0092  0.0228  234 HIS   A CD2 
1746 C CE1 . HIS   A 234 ? 0.2330 0.1752 0.2139 0.0043  0.0061  -0.0102 234 HIS   A CE1 
1747 N NE2 . HIS   A 234 ? 0.2351 0.1825 0.1910 0.0062  -0.0006 0.0140  234 HIS   A NE2 
1748 N N   . PHE   A 235 ? 0.1875 0.1446 0.1940 -0.0022 0.0001  -0.0153 235 PHE   A N   
1749 C CA  . PHE   A 235 ? 0.1512 0.1715 0.2084 -0.0116 -0.0177 -0.0148 235 PHE   A CA  
1750 C C   . PHE   A 235 ? 0.1658 0.1848 0.2163 -0.0024 0.0115  -0.0091 235 PHE   A C   
1751 O O   . PHE   A 235 ? 0.1679 0.1863 0.2045 0.0110  -0.0091 0.0099  235 PHE   A O   
1752 C CB  . PHE   A 235 ? 0.1322 0.1731 0.1999 0.0039  0.0088  0.0113  235 PHE   A CB  
1753 C CG  . PHE   A 235 ? 0.1490 0.1407 0.1932 -0.0190 -0.0156 -0.0179 235 PHE   A CG  
1754 C CD1 . PHE   A 235 ? 0.1472 0.2115 0.1923 -0.0234 -0.0113 0.0108  235 PHE   A CD1 
1755 C CD2 . PHE   A 235 ? 0.1514 0.1438 0.2137 -0.0074 -0.0109 0.0025  235 PHE   A CD2 
1756 C CE1 . PHE   A 235 ? 0.1725 0.2273 0.1900 -0.0170 -0.0340 0.0185  235 PHE   A CE1 
1757 C CE2 . PHE   A 235 ? 0.1519 0.1902 0.2046 0.0020  0.0083  -0.0042 235 PHE   A CE2 
1758 C CZ  . PHE   A 235 ? 0.1754 0.1995 0.1878 -0.0028 -0.0065 0.0089  235 PHE   A CZ  
1759 N N   . ASP   A 236 ? 0.1627 0.1938 0.2180 0.0025  0.0150  -0.0092 236 ASP   A N   
1760 C CA  . ASP   A 236 ? 0.1635 0.2096 0.2329 -0.0059 0.0013  0.0109  236 ASP   A CA  
1761 C C   . ASP   A 236 ? 0.1800 0.1998 0.2353 -0.0078 0.0009  0.0110  236 ASP   A C   
1762 O O   . ASP   A 236 ? 0.2384 0.2263 0.2260 -0.0481 -0.0475 0.0188  236 ASP   A O   
1763 C CB  . ASP   A 236 ? 0.1315 0.2218 0.2384 -0.0004 -0.0014 0.0193  236 ASP   A CB  
1764 C CG  . ASP   A 236 ? 0.1517 0.2368 0.2447 0.0244  0.0103  -0.0009 236 ASP   A CG  
1765 O OD1 . ASP   A 236 ? 0.1918 0.2140 0.2462 0.0190  0.0137  0.0118  236 ASP   A OD1 
1766 O OD2 . ASP   A 236 ? 0.1921 0.2701 0.2502 0.0095  -0.0086 -0.0034 236 ASP   A OD2 
1767 N N   . TYR   A 237 ? 0.1837 0.1751 0.2268 -0.0209 -0.0010 0.0025  237 TYR   A N   
1768 C CA  . TYR   A 237 ? 0.1622 0.1895 0.2231 0.0081  -0.0196 -0.0062 237 TYR   A CA  
1769 C C   . TYR   A 237 ? 0.1727 0.1635 0.2093 0.0008  -0.0039 0.0052  237 TYR   A C   
1770 O O   . TYR   A 237 ? 0.1979 0.1771 0.2178 -0.0138 -0.0120 0.0068  237 TYR   A O   
1771 C CB  . TYR   A 237 ? 0.1660 0.2460 0.2458 -0.0104 -0.0190 -0.0130 237 TYR   A CB  
1772 C CG  . TYR   A 237 ? 0.1797 0.2442 0.2819 -0.0065 -0.0277 0.0107  237 TYR   A CG  
1773 C CD1 . TYR   A 237 ? 0.1970 0.2797 0.3120 0.0143  0.0215  0.0557  237 TYR   A CD1 
1774 C CD2 . TYR   A 237 ? 0.1973 0.2845 0.2830 0.0071  -0.0129 0.0033  237 TYR   A CD2 
1775 C CE1 . TYR   A 237 ? 0.2494 0.3183 0.3312 -0.0211 0.0520  0.0543  237 TYR   A CE1 
1776 C CE2 . TYR   A 237 ? 0.2328 0.3574 0.3052 -0.0002 0.0365  0.0180  237 TYR   A CE2 
1777 C CZ  . TYR   A 237 ? 0.2630 0.3848 0.3409 -0.0107 0.0611  0.0255  237 TYR   A CZ  
1778 O OH  . TYR   A 237 ? 0.3381 0.4464 0.3820 -0.0111 0.0956  0.0313  237 TYR   A OH  
1779 N N   . TRP   A 238 ? 0.1848 0.1918 0.1975 0.0157  -0.0242 -0.0039 238 TRP   A N   
1780 C CA  . TRP   A 238 ? 0.1450 0.1901 0.1922 0.0215  -0.0420 -0.0122 238 TRP   A CA  
1781 C C   . TRP   A 238 ? 0.1519 0.2106 0.2129 -0.0064 -0.0395 -0.0273 238 TRP   A C   
1782 O O   . TRP   A 238 ? 0.1930 0.2174 0.2287 -0.0007 -0.0277 -0.0139 238 TRP   A O   
1783 C CB  . TRP   A 238 ? 0.1787 0.2136 0.1808 0.0180  -0.0433 -0.0051 238 TRP   A CB  
1784 C CG  . TRP   A 238 ? 0.1732 0.1595 0.1723 0.0132  -0.0328 -0.0197 238 TRP   A CG  
1785 C CD1 . TRP   A 238 ? 0.1853 0.1538 0.1687 -0.0053 -0.0418 -0.0113 238 TRP   A CD1 
1786 C CD2 . TRP   A 238 ? 0.1650 0.1642 0.1640 -0.0022 -0.0315 -0.0222 238 TRP   A CD2 
1787 N NE1 . TRP   A 238 ? 0.1299 0.1875 0.2015 0.0008  -0.0198 0.0028  238 TRP   A NE1 
1788 C CE2 . TRP   A 238 ? 0.1147 0.1779 0.1826 0.0149  -0.0254 0.0031  238 TRP   A CE2 
1789 C CE3 . TRP   A 238 ? 0.1994 0.1800 0.1912 0.0320  -0.0253 0.0076  238 TRP   A CE3 
1790 C CZ2 . TRP   A 238 ? 0.1481 0.1979 0.1890 0.0243  -0.0088 0.0116  238 TRP   A CZ2 
1791 C CZ3 . TRP   A 238 ? 0.1962 0.1725 0.1901 -0.0069 -0.0232 0.0103  238 TRP   A CZ3 
1792 C CH2 . TRP   A 238 ? 0.2127 0.1756 0.1842 0.0299  -0.0097 -0.0163 238 TRP   A CH2 
1793 N N   . GLY   A 239 ? 0.1795 0.2041 0.2148 0.0042  -0.0276 -0.0336 239 GLY   A N   
1794 C CA  . GLY   A 239 ? 0.2184 0.1837 0.2250 0.0035  -0.0323 -0.0221 239 GLY   A CA  
1795 C C   . GLY   A 239 ? 0.1823 0.2114 0.2325 -0.0161 -0.0216 -0.0133 239 GLY   A C   
1796 O O   . GLY   A 239 ? 0.1980 0.1784 0.2053 -0.0110 -0.0280 -0.0266 239 GLY   A O   
1797 N N   . GLN   A 240 ? 0.2200 0.2188 0.2709 0.0103  0.0018  0.0024  240 GLN   A N   
1798 C CA  A GLN   A 240 ? 0.2088 0.2186 0.2809 -0.0190 -0.0210 -0.0029 240 GLN   A CA  
1799 C CA  B GLN   A 240 ? 0.2175 0.2229 0.2876 0.0004  -0.0171 0.0032  240 GLN   A CA  
1800 C C   . GLN   A 240 ? 0.2066 0.2263 0.2744 0.0116  -0.0063 0.0162  240 GLN   A C   
1801 O O   . GLN   A 240 ? 0.2318 0.2802 0.3053 -0.0024 -0.0373 0.0535  240 GLN   A O   
1802 C CB  A GLN   A 240 ? 0.2493 0.2490 0.3021 -0.0773 -0.0732 -0.0141 240 GLN   A CB  
1803 C CB  B GLN   A 240 ? 0.2968 0.2638 0.3253 -0.0079 -0.0432 0.0048  240 GLN   A CB  
1804 C CG  A GLN   A 240 ? 0.4224 0.3237 0.3280 -0.0657 -0.0553 -0.0187 240 GLN   A CG  
1805 C CG  B GLN   A 240 ? 0.4161 0.3219 0.3561 0.0087  -0.0266 0.0118  240 GLN   A CG  
1806 C CD  A GLN   A 240 ? 0.3737 0.3172 0.3233 -0.0549 -0.0629 -0.0178 240 GLN   A CD  
1807 C CD  B GLN   A 240 ? 0.3440 0.3394 0.3641 0.0010  -0.0115 0.0142  240 GLN   A CD  
1808 O OE1 A GLN   A 240 ? 0.2307 0.1858 0.2737 -0.0802 -0.0765 0.0041  240 GLN   A OE1 
1809 O OE1 B GLN   A 240 ? 0.2688 0.2903 0.3645 -0.0471 -0.0067 0.0280  240 GLN   A OE1 
1810 N NE2 A GLN   A 240 ? 0.4111 0.3359 0.3567 -0.0742 -0.0740 -0.0452 240 GLN   A NE2 
1811 N NE2 B GLN   A 240 ? 0.3978 0.3644 0.3643 -0.0427 -0.0106 -0.0132 240 GLN   A NE2 
1812 N N   . GLY   A 241 ? 0.1737 0.1901 0.2367 0.0037  0.0238  -0.0019 241 GLY   A N   
1813 C CA  . GLY   A 241 ? 0.2159 0.2165 0.2493 0.0236  0.0312  -0.0243 241 GLY   A CA  
1814 C C   . GLY   A 241 ? 0.2780 0.1960 0.2668 -0.0071 0.0007  -0.0243 241 GLY   A C   
1815 O O   . GLY   A 241 ? 0.3399 0.2197 0.3080 -0.0331 0.0392  -0.0473 241 GLY   A O   
1816 N N   . THR   A 242 ? 0.2157 0.2249 0.2564 0.0087  -0.0288 -0.0442 242 THR   A N   
1817 C CA  . THR   A 242 ? 0.2279 0.2040 0.2332 0.0287  -0.0306 -0.0380 242 THR   A CA  
1818 C C   . THR   A 242 ? 0.2348 0.2040 0.2283 0.0328  -0.0232 -0.0209 242 THR   A C   
1819 O O   . THR   A 242 ? 0.2207 0.1917 0.2414 -0.0045 -0.0297 -0.0442 242 THR   A O   
1820 C CB  . THR   A 242 ? 0.2049 0.2328 0.2234 0.0585  -0.0148 -0.0364 242 THR   A CB  
1821 O OG1 . THR   A 242 ? 0.2088 0.2418 0.2559 0.0402  -0.0084 -0.0366 242 THR   A OG1 
1822 C CG2 . THR   A 242 ? 0.2717 0.2191 0.2166 0.0436  0.0053  -0.0621 242 THR   A CG2 
1823 N N   . THR   A 243 ? 0.1972 0.2016 0.2304 0.0165  -0.0242 -0.0118 243 THR   A N   
1824 C CA  . THR   A 243 ? 0.2022 0.2004 0.2286 0.0279  -0.0133 0.0154  243 THR   A CA  
1825 C C   . THR   A 243 ? 0.2015 0.2020 0.2097 0.0412  -0.0251 -0.0032 243 THR   A C   
1826 O O   . THR   A 243 ? 0.2077 0.2351 0.2331 -0.0039 -0.0202 -0.0313 243 THR   A O   
1827 C CB  . THR   A 243 ? 0.2176 0.2181 0.2382 0.0483  0.0009  0.0141  243 THR   A CB  
1828 O OG1 . THR   A 243 ? 0.2547 0.2477 0.2340 0.0402  -0.0052 0.0086  243 THR   A OG1 
1829 C CG2 . THR   A 243 ? 0.2596 0.2363 0.2603 0.0646  -0.0333 0.0327  243 THR   A CG2 
1830 N N   . LEU   A 244 ? 0.2243 0.1926 0.1952 0.0231  -0.0254 -0.0043 244 LEU   A N   
1831 C CA  . LEU   A 244 ? 0.2393 0.1884 0.1912 0.0283  -0.0002 -0.0014 244 LEU   A CA  
1832 C C   . LEU   A 244 ? 0.2611 0.2159 0.1992 0.0265  -0.0064 -0.0084 244 LEU   A C   
1833 O O   . LEU   A 244 ? 0.2447 0.2390 0.2023 0.0269  0.0079  0.0010  244 LEU   A O   
1834 C CB  . LEU   A 244 ? 0.2326 0.1646 0.1897 0.0060  0.0257  0.0166  244 LEU   A CB  
1835 C CG  . LEU   A 244 ? 0.2813 0.2017 0.1866 0.0161  -0.0148 0.0198  244 LEU   A CG  
1836 C CD1 . LEU   A 244 ? 0.2717 0.2462 0.1988 0.0001  -0.0317 0.0178  244 LEU   A CD1 
1837 C CD2 . LEU   A 244 ? 0.3205 0.1972 0.1983 0.0086  0.0043  0.0241  244 LEU   A CD2 
1838 N N   . THR   A 245 ? 0.2419 0.2002 0.2173 0.0624  -0.0202 -0.0209 245 THR   A N   
1839 C CA  . THR   A 245 ? 0.2688 0.1897 0.2248 0.0557  0.0049  -0.0130 245 THR   A CA  
1840 C C   . THR   A 245 ? 0.2845 0.2202 0.2104 0.0363  -0.0001 0.0018  245 THR   A C   
1841 O O   . THR   A 245 ? 0.2944 0.2519 0.2009 0.0532  -0.0125 -0.0015 245 THR   A O   
1842 C CB  . THR   A 245 ? 0.3141 0.2023 0.2590 0.0812  0.0111  -0.0071 245 THR   A CB  
1843 O OG1 . THR   A 245 ? 0.3493 0.2323 0.2566 0.0380  -0.0376 -0.0015 245 THR   A OG1 
1844 C CG2 . THR   A 245 ? 0.3134 0.2309 0.2740 0.1009  0.0378  -0.0203 245 THR   A CG2 
1845 N N   . VAL   A 246 ? 0.2978 0.2346 0.2191 0.0582  0.0032  0.0104  246 VAL   A N   
1846 C CA  . VAL   A 246 ? 0.3127 0.2437 0.2357 0.0531  0.0269  0.0032  246 VAL   A CA  
1847 C C   . VAL   A 246 ? 0.3411 0.2478 0.2539 0.0782  0.0006  0.0095  246 VAL   A C   
1848 O O   . VAL   A 246 ? 0.3608 0.2300 0.2634 0.0743  -0.0274 0.0191  246 VAL   A O   
1849 C CB  . VAL   A 246 ? 0.2995 0.2639 0.2341 0.0785  0.0515  -0.0030 246 VAL   A CB  
1850 C CG1 . VAL   A 246 ? 0.3407 0.2995 0.2103 0.0150  0.0536  -0.0009 246 VAL   A CG1 
1851 C CG2 . VAL   A 246 ? 0.2963 0.2436 0.2481 0.0995  0.0344  -0.0006 246 VAL   A CG2 
1852 N N   . SER   A 247 ? 0.3783 0.2657 0.2655 0.1212  0.0525  0.0064  247 SER   A N   
1853 C CA  . SER   A 247 ? 0.3172 0.3042 0.2919 0.1085  0.0316  0.0104  247 SER   A CA  
1854 C C   . SER   A 247 ? 0.3599 0.3140 0.3472 0.1194  0.0546  0.0066  247 SER   A C   
1855 O O   . SER   A 247 ? 0.3946 0.2927 0.3444 0.0437  0.0809  0.0034  247 SER   A O   
1856 C CB  . SER   A 247 ? 0.3931 0.3240 0.3076 0.0870  -0.0106 -0.0114 247 SER   A CB  
1857 O OG  . SER   A 247 ? 0.4459 0.3878 0.3247 0.0726  -0.0108 -0.0186 247 SER   A OG  
1858 N N   . SER   A 248 ? 0.3715 0.3564 0.4182 0.1319  0.0805  -0.0014 248 SER   A N   
1859 C CA  . SER   A 248 ? 0.4767 0.4780 0.5101 0.0683  0.0469  0.0240  248 SER   A CA  
1860 C C   . SER   A 248 ? 0.6688 0.6401 0.6401 0.0100  0.0471  0.0124  248 SER   A C   
1861 O O   . SER   A 248 ? 0.7051 0.6623 0.6692 0.0071  0.0590  0.0027  248 SER   A O   
1862 C CB  . SER   A 248 ? 0.4748 0.4697 0.4807 0.0420  0.0304  0.0677  248 SER   A CB  
1863 O OG  . SER   A 248 ? 0.4411 0.4285 0.4568 0.0686  0.0270  0.1078  248 SER   A OG  
1864 O OXT . SER   A 248 ? 0.7956 0.7386 0.7088 -0.0356 0.0364  0.0160  248 SER   A OXT 
1865 C C10 . A1LZO B .   ? 0.3179 0.1758 0.2283 0.0546  -0.0080 -0.0041 401 A1LZO A C10 
1866 N N12 . A1LZO B .   ? 0.3527 0.1841 0.2360 0.0213  0.0171  -0.0239 401 A1LZO A N12 
1867 C C01 . A1LZO B .   ? 0.3218 0.2049 0.2349 0.0128  -0.0363 -0.0090 401 A1LZO A C01 
1868 C C02 . A1LZO B .   ? 0.2953 0.1910 0.2297 -0.0021 -0.0510 0.0091  401 A1LZO A C02 
1869 C C03 . A1LZO B .   ? 0.2421 0.1896 0.2332 -0.0179 -0.0393 0.0336  401 A1LZO A C03 
1870 C C04 . A1LZO B .   ? 0.2589 0.2125 0.2421 0.0080  -0.0330 0.0115  401 A1LZO A C04 
1871 C C05 . A1LZO B .   ? 0.2760 0.2077 0.2456 0.0265  -0.0224 0.0110  401 A1LZO A C05 
1872 C C06 . A1LZO B .   ? 0.3153 0.1934 0.2383 0.0210  -0.0294 -0.0032 401 A1LZO A C06 
1873 C C08 . A1LZO B .   ? 0.3479 0.2889 0.3399 0.0162  0.0068  -0.0818 401 A1LZO A C08 
1874 C C09 . A1LZO B .   ? 0.2720 0.1947 0.2331 0.0672  -0.0112 -0.0012 401 A1LZO A C09 
1875 C C18 . A1LZO B .   ? 0.2885 0.2569 0.2778 0.0418  0.0265  -0.0636 401 A1LZO A C18 
1876 N N11 . A1LZO B .   ? 0.2829 0.2013 0.2268 -0.0066 -0.0540 0.0374  401 A1LZO A N11 
1877 O O07 . A1LZO B .   ? 0.3443 0.2257 0.2258 0.0189  -0.0490 0.0076  401 A1LZO A O07 
1878 O O13 . A1LZO B .   ? 0.4175 0.3281 0.3709 0.0344  0.0104  -0.1096 401 A1LZO A O13 
1879 O O14 . A1LZO B .   ? 0.3986 0.3094 0.3669 0.0957  0.0537  -0.0590 401 A1LZO A O14 
1880 O O15 . A1LZO B .   ? 0.2897 0.2114 0.2401 0.0191  -0.0441 0.0341  401 A1LZO A O15 
1881 O O16 . A1LZO B .   ? 0.3888 0.2785 0.2310 0.0040  -0.0552 0.0354  401 A1LZO A O16 
1882 O O17 . A1LZO B .   ? 0.3076 0.1858 0.2217 0.0268  0.0047  0.0171  401 A1LZO A O17 
# 
