data_8Z4N
# 
_entry.id   8Z4N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z4N         pdb_00008z4n 10.2210/pdb8z4n/pdb 
WWPDB D_1300047043 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z4N 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bailiping@caas.cn 
_pdbx_contact_author.name_first         Liping 
_pdbx_contact_author.name_last          Bai 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2146-6526 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guo, L.Z.'  1 0000-0002-9192-9418 
'Wang, S.X.' 2 0000-0003-1417-2041 
'Bai, L.p.'  3 0000-0002-2146-6526 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Pseudomurein Endoisopeptidase PeiR-C90A' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guo, L.Z.'  1 0000-0002-9192-9418 
primary 'Wang, S.X.' 2 0000-0003-1417-2041 
primary 'Bai, L.p.'  3 0000-0002-2146-6526 
# 
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 'Endoisopeptidase PeiR' 26239.225 4   ? ? ? ? 
2 water   nat water                   18.015    556 ? ? ? ? 
# 
_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       
;MVRFSRDMLQDGAKRMFKWLRKGEGLPNYLIMYDMDRNKEYKLVPKEYAGLYESRNIFWIKNGREPNYVTLTSVARNPLV
MDYQNTNYTACPTSLSLASQMLYHYKSESECAKALGTSKGSGTSPAQLIANAPKLGFKIIPIKRDSKEVKKYLKKGFPVI
CHWQVNQSRNCKGDYTGNFGHYGLIWDMTSTHYVVADPAKGVNRKYKFSCLDNANKGYRQNYYVVCPA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVRFSRDMLQDGAKRMFKWLRKGEGLPNYLIMYDMDRNKEYKLVPKEYAGLYESRNIFWIKNGREPNYVTLTSVARNPLV
MDYQNTNYTACPTSLSLASQMLYHYKSESECAKALGTSKGSGTSPAQLIANAPKLGFKIIPIKRDSKEVKKYLKKGFPVI
CHWQVNQSRNCKGDYTGNFGHYGLIWDMTSTHYVVADPAKGVNRKYKFSCLDNANKGYRQNYYVVCPA
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   ARG n 
1 4   PHE n 
1 5   SER n 
1 6   ARG n 
1 7   ASP n 
1 8   MET n 
1 9   LEU n 
1 10  GLN n 
1 11  ASP n 
1 12  GLY n 
1 13  ALA n 
1 14  LYS n 
1 15  ARG n 
1 16  MET n 
1 17  PHE n 
1 18  LYS n 
1 19  TRP n 
1 20  LEU n 
1 21  ARG n 
1 22  LYS n 
1 23  GLY n 
1 24  GLU n 
1 25  GLY n 
1 26  LEU n 
1 27  PRO n 
1 28  ASN n 
1 29  TYR n 
1 30  LEU n 
1 31  ILE n 
1 32  MET n 
1 33  TYR n 
1 34  ASP n 
1 35  MET n 
1 36  ASP n 
1 37  ARG n 
1 38  ASN n 
1 39  LYS n 
1 40  GLU n 
1 41  TYR n 
1 42  LYS n 
1 43  LEU n 
1 44  VAL n 
1 45  PRO n 
1 46  LYS n 
1 47  GLU n 
1 48  TYR n 
1 49  ALA n 
1 50  GLY n 
1 51  LEU n 
1 52  TYR n 
1 53  GLU n 
1 54  SER n 
1 55  ARG n 
1 56  ASN n 
1 57  ILE n 
1 58  PHE n 
1 59  TRP n 
1 60  ILE n 
1 61  LYS n 
1 62  ASN n 
1 63  GLY n 
1 64  ARG n 
1 65  GLU n 
1 66  PRO n 
1 67  ASN n 
1 68  TYR n 
1 69  VAL n 
1 70  THR n 
1 71  LEU n 
1 72  THR n 
1 73  SER n 
1 74  VAL n 
1 75  ALA n 
1 76  ARG n 
1 77  ASN n 
1 78  PRO n 
1 79  LEU n 
1 80  VAL n 
1 81  MET n 
1 82  ASP n 
1 83  TYR n 
1 84  GLN n 
1 85  ASN n 
1 86  THR n 
1 87  ASN n 
1 88  TYR n 
1 89  THR n 
1 90  ALA n 
1 91  CYS n 
1 92  PRO n 
1 93  THR n 
1 94  SER n 
1 95  LEU n 
1 96  SER n 
1 97  LEU n 
1 98  ALA n 
1 99  SER n 
1 100 GLN n 
1 101 MET n 
1 102 LEU n 
1 103 TYR n 
1 104 HIS n 
1 105 TYR n 
1 106 LYS n 
1 107 SER n 
1 108 GLU n 
1 109 SER n 
1 110 GLU n 
1 111 CYS n 
1 112 ALA n 
1 113 LYS n 
1 114 ALA n 
1 115 LEU n 
1 116 GLY n 
1 117 THR n 
1 118 SER n 
1 119 LYS n 
1 120 GLY n 
1 121 SER n 
1 122 GLY n 
1 123 THR n 
1 124 SER n 
1 125 PRO n 
1 126 ALA n 
1 127 GLN n 
1 128 LEU n 
1 129 ILE n 
1 130 ALA n 
1 131 ASN n 
1 132 ALA n 
1 133 PRO n 
1 134 LYS n 
1 135 LEU n 
1 136 GLY n 
1 137 PHE n 
1 138 LYS n 
1 139 ILE n 
1 140 ILE n 
1 141 PRO n 
1 142 ILE n 
1 143 LYS n 
1 144 ARG n 
1 145 ASP n 
1 146 SER n 
1 147 LYS n 
1 148 GLU n 
1 149 VAL n 
1 150 LYS n 
1 151 LYS n 
1 152 TYR n 
1 153 LEU n 
1 154 LYS n 
1 155 LYS n 
1 156 GLY n 
1 157 PHE n 
1 158 PRO n 
1 159 VAL n 
1 160 ILE n 
1 161 CYS n 
1 162 HIS n 
1 163 TRP n 
1 164 GLN n 
1 165 VAL n 
1 166 ASN n 
1 167 GLN n 
1 168 SER n 
1 169 ARG n 
1 170 ASN n 
1 171 CYS n 
1 172 LYS n 
1 173 GLY n 
1 174 ASP n 
1 175 TYR n 
1 176 THR n 
1 177 GLY n 
1 178 ASN n 
1 179 PHE n 
1 180 GLY n 
1 181 HIS n 
1 182 TYR n 
1 183 GLY n 
1 184 LEU n 
1 185 ILE n 
1 186 TRP n 
1 187 ASP n 
1 188 MET n 
1 189 THR n 
1 190 SER n 
1 191 THR n 
1 192 HIS n 
1 193 TYR n 
1 194 VAL n 
1 195 VAL n 
1 196 ALA n 
1 197 ASP n 
1 198 PRO n 
1 199 ALA n 
1 200 LYS n 
1 201 GLY n 
1 202 VAL n 
1 203 ASN n 
1 204 ARG n 
1 205 LYS n 
1 206 TYR n 
1 207 LYS n 
1 208 PHE n 
1 209 SER n 
1 210 CYS n 
1 211 LEU n 
1 212 ASP n 
1 213 ASN n 
1 214 ALA n 
1 215 ASN n 
1 216 LYS n 
1 217 GLY n 
1 218 TYR n 
1 219 ARG n 
1 220 GLN n 
1 221 ASN n 
1 222 TYR n 
1 223 TYR n 
1 224 VAL n 
1 225 VAL n 
1 226 CYS n 
1 227 PRO n 
1 228 ALA 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                   228 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'peiR, mru_0320' 
_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      'Methanobrevibacter ruminantium M1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     634498 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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   MET 1   1   1   MET MET A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   ASP 7   7   7   ASP ASP A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  GLN 10  10  10  GLN GLN A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TRP 19  19  19  TRP TRP A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  MET 35  35  35  MET MET A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  TYR 41  41  41  TYR TYR A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  MET 81  81  81  MET MET A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 MET 101 101 101 MET MET A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 SER 109 109 109 SER SER A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 LYS 150 150 150 LYS LYS A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 CYS 161 161 161 CYS CYS A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 TRP 163 163 163 TRP TRP A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 CYS 171 171 171 CYS CYS A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 HIS 181 181 181 HIS HIS A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 TRP 186 186 186 TRP TRP A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 MET 188 188 188 MET MET A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 CYS 210 210 210 CYS CYS A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 TYR 218 218 218 TYR TYR A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 TYR 222 222 222 TYR TYR A . n 
A 1 223 TYR 223 223 223 TYR TYR A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   VAL 2   2   2   VAL VAL B . n 
B 1 3   ARG 3   3   3   ARG ARG B . n 
B 1 4   PHE 4   4   4   PHE PHE B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   ARG 6   6   6   ARG ARG B . n 
B 1 7   ASP 7   7   7   ASP ASP B . n 
B 1 8   MET 8   8   8   MET MET B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  GLN 10  10  10  GLN GLN B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  LYS 14  14  14  LYS LYS B . n 
B 1 15  ARG 15  15  15  ARG ARG B . n 
B 1 16  MET 16  16  16  MET MET B . n 
B 1 17  PHE 17  17  17  PHE PHE B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TRP 19  19  19  TRP TRP B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  PRO 27  27  27  PRO PRO B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  TYR 29  29  29  TYR TYR B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  MET 32  32  32  MET MET B . n 
B 1 33  TYR 33  33  33  TYR TYR B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  MET 35  35  35  MET MET B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  ASN 38  38  38  ASN ASN B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  TYR 41  41  41  TYR TYR B . n 
B 1 42  LYS 42  42  42  LYS LYS B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  VAL 44  44  44  VAL VAL B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  TYR 48  48  48  TYR TYR B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ARG 55  55  55  ARG ARG B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  PHE 58  58  58  PHE PHE B . n 
B 1 59  TRP 59  59  59  TRP TRP B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  VAL 69  69  69  VAL VAL B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  THR 72  72  72  THR THR B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  VAL 74  74  74  VAL VAL B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  PRO 78  78  78  PRO PRO B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  MET 81  81  81  MET MET B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  TYR 83  83  83  TYR TYR B . n 
B 1 84  GLN 84  84  84  GLN GLN B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  THR 89  89  89  THR THR B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 GLN 100 100 100 GLN GLN B . n 
B 1 101 MET 101 101 101 MET MET B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 HIS 104 104 104 HIS HIS B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 LYS 106 106 106 LYS LYS B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 SER 109 109 109 SER SER B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 THR 117 117 117 THR THR B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 SER 124 124 124 SER SER B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 LYS 134 134 134 LYS LYS B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 SER 146 146 146 SER SER B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 LYS 150 150 150 LYS LYS B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 LYS 155 155 155 LYS LYS B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 PHE 157 157 157 PHE PHE B . n 
B 1 158 PRO 158 158 158 PRO PRO B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 ILE 160 160 160 ILE ILE B . n 
B 1 161 CYS 161 161 161 CYS CYS B . n 
B 1 162 HIS 162 162 162 HIS HIS B . n 
B 1 163 TRP 163 163 163 TRP TRP B . n 
B 1 164 GLN 164 164 164 GLN GLN B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 ASN 166 166 166 ASN ASN B . n 
B 1 167 GLN 167 167 167 GLN GLN B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 ARG 169 169 169 ARG ARG B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 CYS 171 171 171 CYS CYS B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 ASP 174 174 174 ASP ASP B . n 
B 1 175 TYR 175 175 175 TYR TYR B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 PHE 179 179 179 PHE PHE B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 HIS 181 181 181 HIS HIS B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 ILE 185 185 185 ILE ILE B . n 
B 1 186 TRP 186 186 186 TRP TRP B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 MET 188 188 188 MET MET B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 THR 191 191 191 THR THR B . n 
B 1 192 HIS 192 192 192 HIS HIS B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 LYS 200 200 200 LYS LYS B . n 
B 1 201 GLY 201 201 201 GLY GLY B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 TYR 206 206 206 TYR TYR B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 CYS 210 210 210 CYS CYS B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 ASP 212 212 212 ASP ASP B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 ASN 215 215 215 ASN ASN B . n 
B 1 216 LYS 216 216 216 LYS LYS B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 TYR 218 218 218 TYR TYR B . n 
B 1 219 ARG 219 219 219 ARG ARG B . n 
B 1 220 GLN 220 220 220 GLN GLN B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 TYR 222 222 222 TYR TYR B . n 
B 1 223 TYR 223 223 223 TYR TYR B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 CYS 226 226 226 CYS CYS B . n 
B 1 227 PRO 227 227 227 PRO PRO B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   VAL 2   2   2   VAL VAL C . n 
C 1 3   ARG 3   3   3   ARG ARG C . n 
C 1 4   PHE 4   4   4   PHE PHE C . n 
C 1 5   SER 5   5   5   SER SER C . n 
C 1 6   ARG 6   6   6   ARG ARG C . n 
C 1 7   ASP 7   7   7   ASP ASP C . n 
C 1 8   MET 8   8   8   MET MET C . n 
C 1 9   LEU 9   9   9   LEU LEU C . n 
C 1 10  GLN 10  10  10  GLN GLN C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  ALA 13  13  13  ALA ALA C . n 
C 1 14  LYS 14  14  14  LYS LYS C . n 
C 1 15  ARG 15  15  15  ARG ARG C . n 
C 1 16  MET 16  16  16  MET MET C . n 
C 1 17  PHE 17  17  17  PHE PHE C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TRP 19  19  19  TRP TRP C . n 
C 1 20  LEU 20  20  20  LEU LEU C . n 
C 1 21  ARG 21  21  21  ARG ARG C . n 
C 1 22  LYS 22  22  22  LYS LYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  GLY 25  25  25  GLY GLY C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  PRO 27  27  27  PRO PRO C . n 
C 1 28  ASN 28  28  28  ASN ASN C . n 
C 1 29  TYR 29  29  29  TYR TYR C . n 
C 1 30  LEU 30  30  30  LEU LEU C . n 
C 1 31  ILE 31  31  31  ILE ILE C . n 
C 1 32  MET 32  32  32  MET MET C . n 
C 1 33  TYR 33  33  33  TYR TYR C . n 
C 1 34  ASP 34  34  34  ASP ASP C . n 
C 1 35  MET 35  35  35  MET MET C . n 
C 1 36  ASP 36  36  36  ASP ASP C . n 
C 1 37  ARG 37  37  37  ARG ARG C . n 
C 1 38  ASN 38  38  38  ASN ASN C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  TYR 41  41  41  TYR TYR C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  VAL 44  44  44  VAL VAL C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  TYR 48  48  48  TYR TYR C . n 
C 1 49  ALA 49  49  49  ALA ALA C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  LEU 51  51  51  LEU LEU C . n 
C 1 52  TYR 52  52  52  TYR TYR C . n 
C 1 53  GLU 53  53  53  GLU GLU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ARG 55  55  55  ARG ARG C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  ILE 57  57  57  ILE ILE C . n 
C 1 58  PHE 58  58  58  PHE PHE C . n 
C 1 59  TRP 59  59  59  TRP TRP C . n 
C 1 60  ILE 60  60  60  ILE ILE C . n 
C 1 61  LYS 61  61  61  LYS LYS C . n 
C 1 62  ASN 62  62  62  ASN ASN C . n 
C 1 63  GLY 63  63  63  GLY GLY C . n 
C 1 64  ARG 64  64  64  ARG ARG C . n 
C 1 65  GLU 65  65  65  GLU GLU C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  ASN 67  67  67  ASN ASN C . n 
C 1 68  TYR 68  68  68  TYR TYR C . n 
C 1 69  VAL 69  69  69  VAL VAL C . n 
C 1 70  THR 70  70  70  THR THR C . n 
C 1 71  LEU 71  71  71  LEU LEU C . n 
C 1 72  THR 72  72  72  THR THR C . n 
C 1 73  SER 73  73  73  SER SER C . n 
C 1 74  VAL 74  74  74  VAL VAL C . n 
C 1 75  ALA 75  75  75  ALA ALA C . n 
C 1 76  ARG 76  76  76  ARG ARG C . n 
C 1 77  ASN 77  77  77  ASN ASN C . n 
C 1 78  PRO 78  78  78  PRO PRO C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  MET 81  81  81  MET MET C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  TYR 83  83  83  TYR TYR C . n 
C 1 84  GLN 84  84  84  GLN GLN C . n 
C 1 85  ASN 85  85  85  ASN ASN C . n 
C 1 86  THR 86  86  86  THR THR C . n 
C 1 87  ASN 87  87  87  ASN ASN C . n 
C 1 88  TYR 88  88  88  TYR TYR C . n 
C 1 89  THR 89  89  89  THR THR C . n 
C 1 90  ALA 90  90  90  ALA ALA C . n 
C 1 91  CYS 91  91  91  CYS CYS C . n 
C 1 92  PRO 92  92  92  PRO PRO C . n 
C 1 93  THR 93  93  93  THR THR C . n 
C 1 94  SER 94  94  94  SER SER C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  SER 96  96  96  SER SER C . n 
C 1 97  LEU 97  97  97  LEU LEU C . n 
C 1 98  ALA 98  98  98  ALA ALA C . n 
C 1 99  SER 99  99  99  SER SER C . n 
C 1 100 GLN 100 100 100 GLN GLN C . n 
C 1 101 MET 101 101 101 MET MET C . n 
C 1 102 LEU 102 102 102 LEU LEU C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 HIS 104 104 104 HIS HIS C . n 
C 1 105 TYR 105 105 105 TYR TYR C . n 
C 1 106 LYS 106 106 106 LYS LYS C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLU 108 108 108 GLU GLU C . n 
C 1 109 SER 109 109 109 SER SER C . n 
C 1 110 GLU 110 110 110 GLU GLU C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ALA 112 112 112 ALA ALA C . n 
C 1 113 LYS 113 113 113 LYS LYS C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 GLY 116 116 116 GLY GLY C . n 
C 1 117 THR 117 117 117 THR THR C . n 
C 1 118 SER 118 118 118 SER SER C . n 
C 1 119 LYS 119 119 119 LYS LYS C . n 
C 1 120 GLY 120 120 120 GLY GLY C . n 
C 1 121 SER 121 121 121 SER SER C . n 
C 1 122 GLY 122 122 122 GLY GLY C . n 
C 1 123 THR 123 123 123 THR THR C . n 
C 1 124 SER 124 124 124 SER SER C . n 
C 1 125 PRO 125 125 125 PRO PRO C . n 
C 1 126 ALA 126 126 126 ALA ALA C . n 
C 1 127 GLN 127 127 127 GLN GLN C . n 
C 1 128 LEU 128 128 128 LEU LEU C . n 
C 1 129 ILE 129 129 129 ILE ILE C . n 
C 1 130 ALA 130 130 130 ALA ALA C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 PRO 133 133 133 PRO PRO C . n 
C 1 134 LYS 134 134 134 LYS LYS C . n 
C 1 135 LEU 135 135 135 LEU LEU C . n 
C 1 136 GLY 136 136 136 GLY GLY C . n 
C 1 137 PHE 137 137 137 PHE PHE C . n 
C 1 138 LYS 138 138 138 LYS LYS C . n 
C 1 139 ILE 139 139 139 ILE ILE C . n 
C 1 140 ILE 140 140 140 ILE ILE C . n 
C 1 141 PRO 141 141 141 PRO PRO C . n 
C 1 142 ILE 142 142 142 ILE ILE C . n 
C 1 143 LYS 143 143 143 LYS LYS C . n 
C 1 144 ARG 144 144 144 ARG ARG C . n 
C 1 145 ASP 145 145 145 ASP ASP C . n 
C 1 146 SER 146 146 146 SER SER C . n 
C 1 147 LYS 147 147 147 LYS LYS C . n 
C 1 148 GLU 148 148 148 GLU GLU C . n 
C 1 149 VAL 149 149 149 VAL VAL C . n 
C 1 150 LYS 150 150 150 LYS LYS C . n 
C 1 151 LYS 151 151 151 LYS LYS C . n 
C 1 152 TYR 152 152 152 TYR TYR C . n 
C 1 153 LEU 153 153 153 LEU LEU C . n 
C 1 154 LYS 154 154 154 LYS LYS C . n 
C 1 155 LYS 155 155 155 LYS LYS C . n 
C 1 156 GLY 156 156 156 GLY GLY C . n 
C 1 157 PHE 157 157 157 PHE PHE C . n 
C 1 158 PRO 158 158 158 PRO PRO C . n 
C 1 159 VAL 159 159 159 VAL VAL C . n 
C 1 160 ILE 160 160 160 ILE ILE C . n 
C 1 161 CYS 161 161 161 CYS CYS C . n 
C 1 162 HIS 162 162 162 HIS HIS C . n 
C 1 163 TRP 163 163 163 TRP TRP C . n 
C 1 164 GLN 164 164 164 GLN GLN C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 ASN 166 166 166 ASN ASN C . n 
C 1 167 GLN 167 167 167 GLN GLN C . n 
C 1 168 SER 168 168 168 SER SER C . n 
C 1 169 ARG 169 169 169 ARG ARG C . n 
C 1 170 ASN 170 170 170 ASN ASN C . n 
C 1 171 CYS 171 171 171 CYS CYS C . n 
C 1 172 LYS 172 172 172 LYS LYS C . n 
C 1 173 GLY 173 173 173 GLY GLY C . n 
C 1 174 ASP 174 174 174 ASP ASP C . n 
C 1 175 TYR 175 175 175 TYR TYR C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 GLY 177 177 177 GLY GLY C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 PHE 179 179 179 PHE PHE C . n 
C 1 180 GLY 180 180 180 GLY GLY C . n 
C 1 181 HIS 181 181 181 HIS HIS C . n 
C 1 182 TYR 182 182 182 TYR TYR C . n 
C 1 183 GLY 183 183 183 GLY GLY C . n 
C 1 184 LEU 184 184 184 LEU LEU C . n 
C 1 185 ILE 185 185 185 ILE ILE C . n 
C 1 186 TRP 186 186 186 TRP TRP C . n 
C 1 187 ASP 187 187 187 ASP ASP C . n 
C 1 188 MET 188 188 188 MET MET C . n 
C 1 189 THR 189 189 189 THR THR C . n 
C 1 190 SER 190 190 190 SER SER C . n 
C 1 191 THR 191 191 191 THR THR C . n 
C 1 192 HIS 192 192 192 HIS HIS C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 VAL 194 194 194 VAL VAL C . n 
C 1 195 VAL 195 195 195 VAL VAL C . n 
C 1 196 ALA 196 196 196 ALA ALA C . n 
C 1 197 ASP 197 197 197 ASP ASP C . n 
C 1 198 PRO 198 198 198 PRO PRO C . n 
C 1 199 ALA 199 199 199 ALA ALA C . n 
C 1 200 LYS 200 200 200 LYS LYS C . n 
C 1 201 GLY 201 201 201 GLY GLY C . n 
C 1 202 VAL 202 202 202 VAL VAL C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 ARG 204 204 204 ARG ARG C . n 
C 1 205 LYS 205 205 205 LYS LYS C . n 
C 1 206 TYR 206 206 206 TYR TYR C . n 
C 1 207 LYS 207 207 207 LYS LYS C . n 
C 1 208 PHE 208 208 208 PHE PHE C . n 
C 1 209 SER 209 209 209 SER SER C . n 
C 1 210 CYS 210 210 210 CYS CYS C . n 
C 1 211 LEU 211 211 211 LEU LEU C . n 
C 1 212 ASP 212 212 212 ASP ASP C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 ALA 214 214 214 ALA ALA C . n 
C 1 215 ASN 215 215 215 ASN ASN C . n 
C 1 216 LYS 216 216 216 LYS LYS C . n 
C 1 217 GLY 217 217 217 GLY GLY C . n 
C 1 218 TYR 218 218 218 TYR TYR C . n 
C 1 219 ARG 219 219 219 ARG ARG C . n 
C 1 220 GLN 220 220 220 GLN GLN C . n 
C 1 221 ASN 221 221 221 ASN ASN C . n 
C 1 222 TYR 222 222 222 TYR TYR C . n 
C 1 223 TYR 223 223 223 TYR TYR C . n 
C 1 224 VAL 224 224 224 VAL VAL C . n 
C 1 225 VAL 225 225 225 VAL VAL C . n 
C 1 226 CYS 226 226 226 CYS CYS C . n 
C 1 227 PRO 227 227 227 PRO PRO C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   VAL 2   2   2   VAL VAL D . n 
D 1 3   ARG 3   3   3   ARG ARG D . n 
D 1 4   PHE 4   4   4   PHE PHE D . n 
D 1 5   SER 5   5   5   SER SER D . n 
D 1 6   ARG 6   6   6   ARG ARG D . n 
D 1 7   ASP 7   7   7   ASP ASP D . n 
D 1 8   MET 8   8   8   MET MET D . n 
D 1 9   LEU 9   9   9   LEU LEU D . n 
D 1 10  GLN 10  10  10  GLN GLN D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  ALA 13  13  13  ALA ALA D . n 
D 1 14  LYS 14  14  14  LYS LYS D . n 
D 1 15  ARG 15  15  15  ARG ARG D . n 
D 1 16  MET 16  16  16  MET MET D . n 
D 1 17  PHE 17  17  17  PHE PHE D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TRP 19  19  19  TRP TRP D . n 
D 1 20  LEU 20  20  20  LEU LEU D . n 
D 1 21  ARG 21  21  21  ARG ARG D . n 
D 1 22  LYS 22  22  22  LYS LYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  GLY 25  25  25  GLY GLY D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  PRO 27  27  27  PRO PRO D . n 
D 1 28  ASN 28  28  28  ASN ASN D . n 
D 1 29  TYR 29  29  29  TYR TYR D . n 
D 1 30  LEU 30  30  30  LEU LEU D . n 
D 1 31  ILE 31  31  31  ILE ILE D . n 
D 1 32  MET 32  32  32  MET MET D . n 
D 1 33  TYR 33  33  33  TYR TYR D . n 
D 1 34  ASP 34  34  34  ASP ASP D . n 
D 1 35  MET 35  35  35  MET MET D . n 
D 1 36  ASP 36  36  36  ASP ASP D . n 
D 1 37  ARG 37  37  37  ARG ARG D . n 
D 1 38  ASN 38  38  38  ASN ASN D . n 
D 1 39  LYS 39  39  39  LYS LYS D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  TYR 41  41  41  TYR TYR D . n 
D 1 42  LYS 42  42  42  LYS LYS D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  VAL 44  44  44  VAL VAL D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LYS 46  46  46  LYS LYS D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  TYR 48  48  48  TYR TYR D . n 
D 1 49  ALA 49  49  49  ALA ALA D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  LEU 51  51  51  LEU LEU D . n 
D 1 52  TYR 52  52  52  TYR TYR D . n 
D 1 53  GLU 53  53  53  GLU GLU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ARG 55  55  55  ARG ARG D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  ILE 57  57  57  ILE ILE D . n 
D 1 58  PHE 58  58  58  PHE PHE D . n 
D 1 59  TRP 59  59  59  TRP TRP D . n 
D 1 60  ILE 60  60  60  ILE ILE D . n 
D 1 61  LYS 61  61  61  LYS LYS D . n 
D 1 62  ASN 62  62  62  ASN ASN D . n 
D 1 63  GLY 63  63  63  GLY GLY D . n 
D 1 64  ARG 64  64  64  ARG ARG D . n 
D 1 65  GLU 65  65  65  GLU GLU D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  ASN 67  67  67  ASN ASN D . n 
D 1 68  TYR 68  68  68  TYR TYR D . n 
D 1 69  VAL 69  69  69  VAL VAL D . n 
D 1 70  THR 70  70  70  THR THR D . n 
D 1 71  LEU 71  71  71  LEU LEU D . n 
D 1 72  THR 72  72  72  THR THR D . n 
D 1 73  SER 73  73  73  SER SER D . n 
D 1 74  VAL 74  74  74  VAL VAL D . n 
D 1 75  ALA 75  75  75  ALA ALA D . n 
D 1 76  ARG 76  76  76  ARG ARG D . n 
D 1 77  ASN 77  77  77  ASN ASN D . n 
D 1 78  PRO 78  78  78  PRO PRO D . n 
D 1 79  LEU 79  79  79  LEU LEU D . n 
D 1 80  VAL 80  80  80  VAL VAL D . n 
D 1 81  MET 81  81  81  MET MET D . n 
D 1 82  ASP 82  82  82  ASP ASP D . n 
D 1 83  TYR 83  83  83  TYR TYR D . n 
D 1 84  GLN 84  84  84  GLN GLN D . n 
D 1 85  ASN 85  85  85  ASN ASN D . n 
D 1 86  THR 86  86  86  THR THR D . n 
D 1 87  ASN 87  87  87  ASN ASN D . n 
D 1 88  TYR 88  88  88  TYR TYR D . n 
D 1 89  THR 89  89  89  THR THR D . n 
D 1 90  ALA 90  90  90  ALA ALA D . n 
D 1 91  CYS 91  91  91  CYS CYS D . n 
D 1 92  PRO 92  92  92  PRO PRO D . n 
D 1 93  THR 93  93  93  THR THR D . n 
D 1 94  SER 94  94  94  SER SER D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  SER 96  96  96  SER SER D . n 
D 1 97  LEU 97  97  97  LEU LEU D . n 
D 1 98  ALA 98  98  98  ALA ALA D . n 
D 1 99  SER 99  99  99  SER SER D . n 
D 1 100 GLN 100 100 100 GLN GLN D . n 
D 1 101 MET 101 101 101 MET MET D . n 
D 1 102 LEU 102 102 102 LEU LEU D . n 
D 1 103 TYR 103 103 103 TYR TYR D . n 
D 1 104 HIS 104 104 104 HIS HIS D . n 
D 1 105 TYR 105 105 105 TYR TYR D . n 
D 1 106 LYS 106 106 106 LYS LYS D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLU 108 108 108 GLU GLU D . n 
D 1 109 SER 109 109 109 SER SER D . n 
D 1 110 GLU 110 110 110 GLU GLU D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 ALA 112 112 112 ALA ALA D . n 
D 1 113 LYS 113 113 113 LYS LYS D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 GLY 116 116 116 GLY GLY D . n 
D 1 117 THR 117 117 117 THR THR D . n 
D 1 118 SER 118 118 118 SER SER D . n 
D 1 119 LYS 119 119 119 LYS LYS D . n 
D 1 120 GLY 120 120 120 GLY GLY D . n 
D 1 121 SER 121 121 121 SER SER D . n 
D 1 122 GLY 122 122 122 GLY GLY D . n 
D 1 123 THR 123 123 123 THR THR D . n 
D 1 124 SER 124 124 124 SER SER D . n 
D 1 125 PRO 125 125 125 PRO PRO D . n 
D 1 126 ALA 126 126 126 ALA ALA D . n 
D 1 127 GLN 127 127 127 GLN GLN D . n 
D 1 128 LEU 128 128 128 LEU LEU D . n 
D 1 129 ILE 129 129 129 ILE ILE D . n 
D 1 130 ALA 130 130 130 ALA ALA D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 PRO 133 133 133 PRO PRO D . n 
D 1 134 LYS 134 134 134 LYS LYS D . n 
D 1 135 LEU 135 135 135 LEU LEU D . n 
D 1 136 GLY 136 136 136 GLY GLY D . n 
D 1 137 PHE 137 137 137 PHE PHE D . n 
D 1 138 LYS 138 138 138 LYS LYS D . n 
D 1 139 ILE 139 139 139 ILE ILE D . n 
D 1 140 ILE 140 140 140 ILE ILE D . n 
D 1 141 PRO 141 141 141 PRO PRO D . n 
D 1 142 ILE 142 142 142 ILE ILE D . n 
D 1 143 LYS 143 143 143 LYS LYS D . n 
D 1 144 ARG 144 144 144 ARG ARG D . n 
D 1 145 ASP 145 145 145 ASP ASP D . n 
D 1 146 SER 146 146 146 SER SER D . n 
D 1 147 LYS 147 147 147 LYS LYS D . n 
D 1 148 GLU 148 148 148 GLU GLU D . n 
D 1 149 VAL 149 149 149 VAL VAL D . n 
D 1 150 LYS 150 150 150 LYS LYS D . n 
D 1 151 LYS 151 151 151 LYS LYS D . n 
D 1 152 TYR 152 152 152 TYR TYR D . n 
D 1 153 LEU 153 153 153 LEU LEU D . n 
D 1 154 LYS 154 154 154 LYS LYS D . n 
D 1 155 LYS 155 155 155 LYS LYS D . n 
D 1 156 GLY 156 156 156 GLY GLY D . n 
D 1 157 PHE 157 157 157 PHE PHE D . n 
D 1 158 PRO 158 158 158 PRO PRO D . n 
D 1 159 VAL 159 159 159 VAL VAL D . n 
D 1 160 ILE 160 160 160 ILE ILE D . n 
D 1 161 CYS 161 161 161 CYS CYS D . n 
D 1 162 HIS 162 162 162 HIS HIS D . n 
D 1 163 TRP 163 163 163 TRP TRP D . n 
D 1 164 GLN 164 164 164 GLN GLN D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 ASN 166 166 166 ASN ASN D . n 
D 1 167 GLN 167 167 167 GLN GLN D . n 
D 1 168 SER 168 168 168 SER SER D . n 
D 1 169 ARG 169 169 169 ARG ARG D . n 
D 1 170 ASN 170 170 170 ASN ASN D . n 
D 1 171 CYS 171 171 171 CYS CYS D . n 
D 1 172 LYS 172 172 172 LYS LYS D . n 
D 1 173 GLY 173 173 173 GLY GLY D . n 
D 1 174 ASP 174 174 174 ASP ASP D . n 
D 1 175 TYR 175 175 175 TYR TYR D . n 
D 1 176 THR 176 176 176 THR THR D . n 
D 1 177 GLY 177 177 177 GLY GLY D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 PHE 179 179 179 PHE PHE D . n 
D 1 180 GLY 180 180 180 GLY GLY D . n 
D 1 181 HIS 181 181 181 HIS HIS D . n 
D 1 182 TYR 182 182 182 TYR TYR D . n 
D 1 183 GLY 183 183 183 GLY GLY D . n 
D 1 184 LEU 184 184 184 LEU LEU D . n 
D 1 185 ILE 185 185 185 ILE ILE D . n 
D 1 186 TRP 186 186 186 TRP TRP D . n 
D 1 187 ASP 187 187 187 ASP ASP D . n 
D 1 188 MET 188 188 188 MET MET D . n 
D 1 189 THR 189 189 189 THR THR D . n 
D 1 190 SER 190 190 190 SER SER D . n 
D 1 191 THR 191 191 191 THR THR D . n 
D 1 192 HIS 192 192 192 HIS HIS D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 VAL 194 194 194 VAL VAL D . n 
D 1 195 VAL 195 195 195 VAL VAL D . n 
D 1 196 ALA 196 196 196 ALA ALA D . n 
D 1 197 ASP 197 197 197 ASP ASP D . n 
D 1 198 PRO 198 198 198 PRO PRO D . n 
D 1 199 ALA 199 199 199 ALA ALA D . n 
D 1 200 LYS 200 200 200 LYS LYS D . n 
D 1 201 GLY 201 201 201 GLY GLY D . n 
D 1 202 VAL 202 202 202 VAL VAL D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 ARG 204 204 204 ARG ARG D . n 
D 1 205 LYS 205 205 205 LYS LYS D . n 
D 1 206 TYR 206 206 206 TYR TYR D . n 
D 1 207 LYS 207 207 207 LYS LYS D . n 
D 1 208 PHE 208 208 208 PHE PHE D . n 
D 1 209 SER 209 209 209 SER SER D . n 
D 1 210 CYS 210 210 210 CYS CYS D . n 
D 1 211 LEU 211 211 211 LEU LEU D . n 
D 1 212 ASP 212 212 212 ASP ASP D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 ALA 214 214 214 ALA ALA D . n 
D 1 215 ASN 215 215 215 ASN ASN D . n 
D 1 216 LYS 216 216 216 LYS LYS D . n 
D 1 217 GLY 217 217 217 GLY GLY D . n 
D 1 218 TYR 218 218 218 TYR TYR D . n 
D 1 219 ARG 219 219 219 ARG ARG D . n 
D 1 220 GLN 220 220 220 GLN GLN D . n 
D 1 221 ASN 221 221 221 ASN ASN D . n 
D 1 222 TYR 222 222 222 TYR TYR D . n 
D 1 223 TYR 223 223 223 TYR TYR D . n 
D 1 224 VAL 224 224 224 VAL VAL D . n 
D 1 225 VAL 225 225 225 VAL VAL D . n 
D 1 226 CYS 226 226 226 CYS CYS D . n 
D 1 227 PRO 227 227 227 PRO PRO D . n 
D 1 228 ALA 228 228 228 ALA ALA D . 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 
E 2 HOH 1   301 403 HOH HOH A . 
E 2 HOH 2   302 353 HOH HOH A . 
E 2 HOH 3   303 555 HOH HOH A . 
E 2 HOH 4   304 284 HOH HOH A . 
E 2 HOH 5   305 167 HOH HOH A . 
E 2 HOH 6   306 550 HOH HOH A . 
E 2 HOH 7   307 182 HOH HOH A . 
E 2 HOH 8   308 465 HOH HOH A . 
E 2 HOH 9   309 196 HOH HOH A . 
E 2 HOH 10  310 511 HOH HOH A . 
E 2 HOH 11  311 132 HOH HOH A . 
E 2 HOH 12  312 9   HOH HOH A . 
E 2 HOH 13  313 90  HOH HOH A . 
E 2 HOH 14  314 195 HOH HOH A . 
E 2 HOH 15  315 255 HOH HOH A . 
E 2 HOH 16  316 7   HOH HOH A . 
E 2 HOH 17  317 459 HOH HOH A . 
E 2 HOH 18  318 169 HOH HOH A . 
E 2 HOH 19  319 134 HOH HOH A . 
E 2 HOH 20  320 532 HOH HOH A . 
E 2 HOH 21  321 530 HOH HOH A . 
E 2 HOH 22  322 331 HOH HOH A . 
E 2 HOH 23  323 363 HOH HOH A . 
E 2 HOH 24  324 201 HOH HOH A . 
E 2 HOH 25  325 102 HOH HOH A . 
E 2 HOH 26  326 30  HOH HOH A . 
E 2 HOH 27  327 430 HOH HOH A . 
E 2 HOH 28  328 380 HOH HOH A . 
E 2 HOH 29  329 211 HOH HOH A . 
E 2 HOH 30  330 368 HOH HOH A . 
E 2 HOH 31  331 152 HOH HOH A . 
E 2 HOH 32  332 115 HOH HOH A . 
E 2 HOH 33  333 146 HOH HOH A . 
E 2 HOH 34  334 183 HOH HOH A . 
E 2 HOH 35  335 222 HOH HOH A . 
E 2 HOH 36  336 270 HOH HOH A . 
E 2 HOH 37  337 444 HOH HOH A . 
E 2 HOH 38  338 63  HOH HOH A . 
E 2 HOH 39  339 382 HOH HOH A . 
E 2 HOH 40  340 355 HOH HOH A . 
E 2 HOH 41  341 335 HOH HOH A . 
E 2 HOH 42  342 371 HOH HOH A . 
E 2 HOH 43  343 3   HOH HOH A . 
E 2 HOH 44  344 417 HOH HOH A . 
E 2 HOH 45  345 451 HOH HOH A . 
E 2 HOH 46  346 393 HOH HOH A . 
E 2 HOH 47  347 44  HOH HOH A . 
E 2 HOH 48  348 111 HOH HOH A . 
E 2 HOH 49  349 188 HOH HOH A . 
E 2 HOH 50  350 98  HOH HOH A . 
E 2 HOH 51  351 159 HOH HOH A . 
E 2 HOH 52  352 13  HOH HOH A . 
E 2 HOH 53  353 38  HOH HOH A . 
E 2 HOH 54  354 175 HOH HOH A . 
E 2 HOH 55  355 59  HOH HOH A . 
E 2 HOH 56  356 539 HOH HOH A . 
E 2 HOH 57  357 133 HOH HOH A . 
E 2 HOH 58  358 116 HOH HOH A . 
E 2 HOH 59  359 173 HOH HOH A . 
E 2 HOH 60  360 472 HOH HOH A . 
E 2 HOH 61  361 8   HOH HOH A . 
E 2 HOH 62  362 343 HOH HOH A . 
E 2 HOH 63  363 329 HOH HOH A . 
E 2 HOH 64  364 299 HOH HOH A . 
E 2 HOH 65  365 277 HOH HOH A . 
E 2 HOH 66  366 171 HOH HOH A . 
E 2 HOH 67  367 64  HOH HOH A . 
E 2 HOH 68  368 80  HOH HOH A . 
E 2 HOH 69  369 147 HOH HOH A . 
E 2 HOH 70  370 301 HOH HOH A . 
E 2 HOH 71  371 192 HOH HOH A . 
E 2 HOH 72  372 87  HOH HOH A . 
E 2 HOH 73  373 180 HOH HOH A . 
E 2 HOH 74  374 120 HOH HOH A . 
E 2 HOH 75  375 524 HOH HOH A . 
E 2 HOH 76  376 504 HOH HOH A . 
E 2 HOH 77  377 232 HOH HOH A . 
E 2 HOH 78  378 370 HOH HOH A . 
E 2 HOH 79  379 551 HOH HOH A . 
E 2 HOH 80  380 148 HOH HOH A . 
E 2 HOH 81  381 123 HOH HOH A . 
E 2 HOH 82  382 509 HOH HOH A . 
E 2 HOH 83  383 265 HOH HOH A . 
E 2 HOH 84  384 27  HOH HOH A . 
E 2 HOH 85  385 204 HOH HOH A . 
E 2 HOH 86  386 114 HOH HOH A . 
E 2 HOH 87  387 546 HOH HOH A . 
E 2 HOH 88  388 208 HOH HOH A . 
E 2 HOH 89  389 273 HOH HOH A . 
E 2 HOH 90  390 135 HOH HOH A . 
E 2 HOH 91  391 521 HOH HOH A . 
E 2 HOH 92  392 88  HOH HOH A . 
E 2 HOH 93  393 485 HOH HOH A . 
E 2 HOH 94  394 240 HOH HOH A . 
E 2 HOH 95  395 351 HOH HOH A . 
E 2 HOH 96  396 547 HOH HOH A . 
E 2 HOH 97  397 290 HOH HOH A . 
E 2 HOH 98  398 174 HOH HOH A . 
E 2 HOH 99  399 113 HOH HOH A . 
E 2 HOH 100 400 241 HOH HOH A . 
E 2 HOH 101 401 410 HOH HOH A . 
E 2 HOH 102 402 344 HOH HOH A . 
E 2 HOH 103 403 361 HOH HOH A . 
E 2 HOH 104 404 412 HOH HOH A . 
E 2 HOH 105 405 209 HOH HOH A . 
E 2 HOH 106 406 272 HOH HOH A . 
E 2 HOH 107 407 428 HOH HOH A . 
E 2 HOH 108 408 436 HOH HOH A . 
E 2 HOH 109 409 261 HOH HOH A . 
E 2 HOH 110 410 262 HOH HOH A . 
E 2 HOH 111 411 464 HOH HOH A . 
E 2 HOH 112 412 404 HOH HOH A . 
E 2 HOH 113 413 346 HOH HOH A . 
E 2 HOH 114 414 402 HOH HOH A . 
E 2 HOH 115 415 460 HOH HOH A . 
E 2 HOH 116 416 431 HOH HOH A . 
E 2 HOH 117 417 307 HOH HOH A . 
E 2 HOH 118 418 388 HOH HOH A . 
E 2 HOH 119 419 447 HOH HOH A . 
E 2 HOH 120 420 106 HOH HOH A . 
E 2 HOH 121 421 433 HOH HOH A . 
E 2 HOH 122 422 544 HOH HOH A . 
E 2 HOH 123 423 536 HOH HOH A . 
E 2 HOH 124 424 364 HOH HOH A . 
E 2 HOH 125 425 531 HOH HOH A . 
E 2 HOH 126 426 514 HOH HOH A . 
E 2 HOH 127 427 549 HOH HOH A . 
E 2 HOH 128 428 323 HOH HOH A . 
E 2 HOH 129 429 226 HOH HOH A . 
E 2 HOH 130 430 498 HOH HOH A . 
E 2 HOH 131 431 474 HOH HOH A . 
E 2 HOH 132 432 315 HOH HOH A . 
E 2 HOH 133 433 357 HOH HOH A . 
E 2 HOH 134 434 214 HOH HOH A . 
E 2 HOH 135 435 336 HOH HOH A . 
E 2 HOH 136 436 333 HOH HOH A . 
E 2 HOH 137 437 526 HOH HOH A . 
E 2 HOH 138 438 479 HOH HOH A . 
E 2 HOH 139 439 244 HOH HOH A . 
E 2 HOH 140 440 267 HOH HOH A . 
E 2 HOH 141 441 424 HOH HOH A . 
E 2 HOH 142 442 291 HOH HOH A . 
E 2 HOH 143 443 224 HOH HOH A . 
E 2 HOH 144 444 497 HOH HOH A . 
E 2 HOH 145 445 328 HOH HOH A . 
E 2 HOH 146 446 397 HOH HOH A . 
E 2 HOH 147 447 342 HOH HOH A . 
E 2 HOH 148 448 489 HOH HOH A . 
E 2 HOH 149 449 476 HOH HOH A . 
E 2 HOH 150 450 442 HOH HOH A . 
E 2 HOH 151 451 250 HOH HOH A . 
F 2 HOH 1   301 419 HOH HOH B . 
F 2 HOH 2   302 502 HOH HOH B . 
F 2 HOH 3   303 488 HOH HOH B . 
F 2 HOH 4   304 392 HOH HOH B . 
F 2 HOH 5   305 413 HOH HOH B . 
F 2 HOH 6   306 505 HOH HOH B . 
F 2 HOH 7   307 421 HOH HOH B . 
F 2 HOH 8   308 463 HOH HOH B . 
F 2 HOH 9   309 184 HOH HOH B . 
F 2 HOH 10  310 534 HOH HOH B . 
F 2 HOH 11  311 26  HOH HOH B . 
F 2 HOH 12  312 243 HOH HOH B . 
F 2 HOH 13  313 126 HOH HOH B . 
F 2 HOH 14  314 53  HOH HOH B . 
F 2 HOH 15  315 12  HOH HOH B . 
F 2 HOH 16  316 275 HOH HOH B . 
F 2 HOH 17  317 177 HOH HOH B . 
F 2 HOH 18  318 358 HOH HOH B . 
F 2 HOH 19  319 185 HOH HOH B . 
F 2 HOH 20  320 486 HOH HOH B . 
F 2 HOH 21  321 542 HOH HOH B . 
F 2 HOH 22  322 6   HOH HOH B . 
F 2 HOH 23  323 187 HOH HOH B . 
F 2 HOH 24  324 39  HOH HOH B . 
F 2 HOH 25  325 181 HOH HOH B . 
F 2 HOH 26  326 58  HOH HOH B . 
F 2 HOH 27  327 137 HOH HOH B . 
F 2 HOH 28  328 4   HOH HOH B . 
F 2 HOH 29  329 395 HOH HOH B . 
F 2 HOH 30  330 65  HOH HOH B . 
F 2 HOH 31  331 418 HOH HOH B . 
F 2 HOH 32  332 494 HOH HOH B . 
F 2 HOH 33  333 238 HOH HOH B . 
F 2 HOH 34  334 11  HOH HOH B . 
F 2 HOH 35  335 161 HOH HOH B . 
F 2 HOH 36  336 252 HOH HOH B . 
F 2 HOH 37  337 298 HOH HOH B . 
F 2 HOH 38  338 503 HOH HOH B . 
F 2 HOH 39  339 23  HOH HOH B . 
F 2 HOH 40  340 89  HOH HOH B . 
F 2 HOH 41  341 263 HOH HOH B . 
F 2 HOH 42  342 105 HOH HOH B . 
F 2 HOH 43  343 31  HOH HOH B . 
F 2 HOH 44  344 314 HOH HOH B . 
F 2 HOH 45  345 206 HOH HOH B . 
F 2 HOH 46  346 462 HOH HOH B . 
F 2 HOH 47  347 527 HOH HOH B . 
F 2 HOH 48  348 375 HOH HOH B . 
F 2 HOH 49  349 131 HOH HOH B . 
F 2 HOH 50  350 179 HOH HOH B . 
F 2 HOH 51  351 216 HOH HOH B . 
F 2 HOH 52  352 66  HOH HOH B . 
F 2 HOH 53  353 149 HOH HOH B . 
F 2 HOH 54  354 480 HOH HOH B . 
F 2 HOH 55  355 51  HOH HOH B . 
F 2 HOH 56  356 103 HOH HOH B . 
F 2 HOH 57  357 319 HOH HOH B . 
F 2 HOH 58  358 108 HOH HOH B . 
F 2 HOH 59  359 29  HOH HOH B . 
F 2 HOH 60  360 294 HOH HOH B . 
F 2 HOH 61  361 28  HOH HOH B . 
F 2 HOH 62  362 40  HOH HOH B . 
F 2 HOH 63  363 202 HOH HOH B . 
F 2 HOH 64  364 379 HOH HOH B . 
F 2 HOH 65  365 260 HOH HOH B . 
F 2 HOH 66  366 41  HOH HOH B . 
F 2 HOH 67  367 286 HOH HOH B . 
F 2 HOH 68  368 541 HOH HOH B . 
F 2 HOH 69  369 499 HOH HOH B . 
F 2 HOH 70  370 518 HOH HOH B . 
F 2 HOH 71  371 118 HOH HOH B . 
F 2 HOH 72  372 432 HOH HOH B . 
F 2 HOH 73  373 155 HOH HOH B . 
F 2 HOH 74  374 467 HOH HOH B . 
F 2 HOH 75  375 324 HOH HOH B . 
F 2 HOH 76  376 79  HOH HOH B . 
F 2 HOH 77  377 213 HOH HOH B . 
F 2 HOH 78  378 242 HOH HOH B . 
F 2 HOH 79  379 316 HOH HOH B . 
F 2 HOH 80  380 227 HOH HOH B . 
F 2 HOH 81  381 215 HOH HOH B . 
F 2 HOH 82  382 57  HOH HOH B . 
F 2 HOH 83  383 306 HOH HOH B . 
F 2 HOH 84  384 399 HOH HOH B . 
F 2 HOH 85  385 163 HOH HOH B . 
F 2 HOH 86  386 508 HOH HOH B . 
F 2 HOH 87  387 347 HOH HOH B . 
F 2 HOH 88  388 254 HOH HOH B . 
F 2 HOH 89  389 128 HOH HOH B . 
F 2 HOH 90  390 268 HOH HOH B . 
F 2 HOH 91  391 121 HOH HOH B . 
F 2 HOH 92  392 374 HOH HOH B . 
F 2 HOH 93  393 68  HOH HOH B . 
F 2 HOH 94  394 248 HOH HOH B . 
F 2 HOH 95  395 130 HOH HOH B . 
F 2 HOH 96  396 282 HOH HOH B . 
F 2 HOH 97  397 311 HOH HOH B . 
F 2 HOH 98  398 367 HOH HOH B . 
F 2 HOH 99  399 429 HOH HOH B . 
F 2 HOH 100 400 540 HOH HOH B . 
F 2 HOH 101 401 507 HOH HOH B . 
F 2 HOH 102 402 117 HOH HOH B . 
F 2 HOH 103 403 320 HOH HOH B . 
F 2 HOH 104 404 422 HOH HOH B . 
F 2 HOH 105 405 523 HOH HOH B . 
F 2 HOH 106 406 441 HOH HOH B . 
F 2 HOH 107 407 338 HOH HOH B . 
F 2 HOH 108 408 525 HOH HOH B . 
F 2 HOH 109 409 529 HOH HOH B . 
F 2 HOH 110 410 198 HOH HOH B . 
F 2 HOH 111 411 552 HOH HOH B . 
F 2 HOH 112 412 151 HOH HOH B . 
F 2 HOH 113 413 394 HOH HOH B . 
F 2 HOH 114 414 283 HOH HOH B . 
F 2 HOH 115 415 325 HOH HOH B . 
F 2 HOH 116 416 510 HOH HOH B . 
F 2 HOH 117 417 545 HOH HOH B . 
F 2 HOH 118 418 423 HOH HOH B . 
F 2 HOH 119 419 136 HOH HOH B . 
F 2 HOH 120 420 362 HOH HOH B . 
F 2 HOH 121 421 150 HOH HOH B . 
F 2 HOH 122 422 548 HOH HOH B . 
F 2 HOH 123 423 453 HOH HOH B . 
F 2 HOH 124 424 452 HOH HOH B . 
F 2 HOH 125 425 109 HOH HOH B . 
F 2 HOH 126 426 406 HOH HOH B . 
F 2 HOH 127 427 535 HOH HOH B . 
F 2 HOH 128 428 454 HOH HOH B . 
F 2 HOH 129 429 373 HOH HOH B . 
F 2 HOH 130 430 400 HOH HOH B . 
F 2 HOH 131 431 376 HOH HOH B . 
F 2 HOH 132 432 234 HOH HOH B . 
F 2 HOH 133 433 522 HOH HOH B . 
G 2 HOH 1   301 491 HOH HOH C . 
G 2 HOH 2   302 493 HOH HOH C . 
G 2 HOH 3   303 304 HOH HOH C . 
G 2 HOH 4   304 492 HOH HOH C . 
G 2 HOH 5   305 92  HOH HOH C . 
G 2 HOH 6   306 302 HOH HOH C . 
G 2 HOH 7   307 387 HOH HOH C . 
G 2 HOH 8   308 556 HOH HOH C . 
G 2 HOH 9   309 36  HOH HOH C . 
G 2 HOH 10  310 437 HOH HOH C . 
G 2 HOH 11  311 100 HOH HOH C . 
G 2 HOH 12  312 217 HOH HOH C . 
G 2 HOH 13  313 264 HOH HOH C . 
G 2 HOH 14  314 83  HOH HOH C . 
G 2 HOH 15  315 142 HOH HOH C . 
G 2 HOH 16  316 15  HOH HOH C . 
G 2 HOH 17  317 312 HOH HOH C . 
G 2 HOH 18  318 46  HOH HOH C . 
G 2 HOH 19  319 17  HOH HOH C . 
G 2 HOH 20  320 95  HOH HOH C . 
G 2 HOH 21  321 278 HOH HOH C . 
G 2 HOH 22  322 49  HOH HOH C . 
G 2 HOH 23  323 48  HOH HOH C . 
G 2 HOH 24  324 82  HOH HOH C . 
G 2 HOH 25  325 75  HOH HOH C . 
G 2 HOH 26  326 56  HOH HOH C . 
G 2 HOH 27  327 326 HOH HOH C . 
G 2 HOH 28  328 327 HOH HOH C . 
G 2 HOH 29  329 194 HOH HOH C . 
G 2 HOH 30  330 71  HOH HOH C . 
G 2 HOH 31  331 2   HOH HOH C . 
G 2 HOH 32  332 483 HOH HOH C . 
G 2 HOH 33  333 225 HOH HOH C . 
G 2 HOH 34  334 448 HOH HOH C . 
G 2 HOH 35  335 104 HOH HOH C . 
G 2 HOH 36  336 236 HOH HOH C . 
G 2 HOH 37  337 365 HOH HOH C . 
G 2 HOH 38  338 339 HOH HOH C . 
G 2 HOH 39  339 164 HOH HOH C . 
G 2 HOH 40  340 317 HOH HOH C . 
G 2 HOH 41  341 10  HOH HOH C . 
G 2 HOH 42  342 496 HOH HOH C . 
G 2 HOH 43  343 99  HOH HOH C . 
G 2 HOH 44  344 189 HOH HOH C . 
G 2 HOH 45  345 218 HOH HOH C . 
G 2 HOH 46  346 14  HOH HOH C . 
G 2 HOH 47  347 86  HOH HOH C . 
G 2 HOH 48  348 220 HOH HOH C . 
G 2 HOH 49  349 43  HOH HOH C . 
G 2 HOH 50  350 162 HOH HOH C . 
G 2 HOH 51  351 212 HOH HOH C . 
G 2 HOH 52  352 229 HOH HOH C . 
G 2 HOH 53  353 484 HOH HOH C . 
G 2 HOH 54  354 487 HOH HOH C . 
G 2 HOH 55  355 32  HOH HOH C . 
G 2 HOH 56  356 313 HOH HOH C . 
G 2 HOH 57  357 125 HOH HOH C . 
G 2 HOH 58  358 91  HOH HOH C . 
G 2 HOH 59  359 190 HOH HOH C . 
G 2 HOH 60  360 139 HOH HOH C . 
G 2 HOH 61  361 199 HOH HOH C . 
G 2 HOH 62  362 60  HOH HOH C . 
G 2 HOH 63  363 138 HOH HOH C . 
G 2 HOH 64  364 321 HOH HOH C . 
G 2 HOH 65  365 85  HOH HOH C . 
G 2 HOH 66  366 158 HOH HOH C . 
G 2 HOH 67  367 537 HOH HOH C . 
G 2 HOH 68  368 348 HOH HOH C . 
G 2 HOH 69  369 19  HOH HOH C . 
G 2 HOH 70  370 289 HOH HOH C . 
G 2 HOH 71  371 166 HOH HOH C . 
G 2 HOH 72  372 42  HOH HOH C . 
G 2 HOH 73  373 144 HOH HOH C . 
G 2 HOH 74  374 303 HOH HOH C . 
G 2 HOH 75  375 407 HOH HOH C . 
G 2 HOH 76  376 269 HOH HOH C . 
G 2 HOH 77  377 276 HOH HOH C . 
G 2 HOH 78  378 279 HOH HOH C . 
G 2 HOH 79  379 349 HOH HOH C . 
G 2 HOH 80  380 141 HOH HOH C . 
G 2 HOH 81  381 193 HOH HOH C . 
G 2 HOH 82  382 143 HOH HOH C . 
G 2 HOH 83  383 386 HOH HOH C . 
G 2 HOH 84  384 450 HOH HOH C . 
G 2 HOH 85  385 251 HOH HOH C . 
G 2 HOH 86  386 110 HOH HOH C . 
G 2 HOH 87  387 354 HOH HOH C . 
G 2 HOH 88  388 281 HOH HOH C . 
G 2 HOH 89  389 310 HOH HOH C . 
G 2 HOH 90  390 288 HOH HOH C . 
G 2 HOH 91  391 340 HOH HOH C . 
G 2 HOH 92  392 337 HOH HOH C . 
G 2 HOH 93  393 334 HOH HOH C . 
G 2 HOH 94  394 112 HOH HOH C . 
G 2 HOH 95  395 223 HOH HOH C . 
G 2 HOH 96  396 457 HOH HOH C . 
G 2 HOH 97  397 191 HOH HOH C . 
G 2 HOH 98  398 235 HOH HOH C . 
G 2 HOH 99  399 396 HOH HOH C . 
G 2 HOH 100 400 466 HOH HOH C . 
G 2 HOH 101 401 308 HOH HOH C . 
G 2 HOH 102 402 543 HOH HOH C . 
G 2 HOH 103 403 205 HOH HOH C . 
G 2 HOH 104 404 74  HOH HOH C . 
G 2 HOH 105 405 470 HOH HOH C . 
G 2 HOH 106 406 461 HOH HOH C . 
G 2 HOH 107 407 528 HOH HOH C . 
G 2 HOH 108 408 468 HOH HOH C . 
G 2 HOH 109 409 475 HOH HOH C . 
G 2 HOH 110 410 153 HOH HOH C . 
G 2 HOH 111 411 62  HOH HOH C . 
G 2 HOH 112 412 221 HOH HOH C . 
G 2 HOH 113 413 482 HOH HOH C . 
G 2 HOH 114 414 305 HOH HOH C . 
G 2 HOH 115 415 426 HOH HOH C . 
G 2 HOH 116 416 554 HOH HOH C . 
G 2 HOH 117 417 350 HOH HOH C . 
G 2 HOH 118 418 352 HOH HOH C . 
G 2 HOH 119 419 469 HOH HOH C . 
G 2 HOH 120 420 434 HOH HOH C . 
G 2 HOH 121 421 237 HOH HOH C . 
G 2 HOH 122 422 266 HOH HOH C . 
G 2 HOH 123 423 513 HOH HOH C . 
G 2 HOH 124 424 415 HOH HOH C . 
G 2 HOH 125 425 533 HOH HOH C . 
G 2 HOH 126 426 256 HOH HOH C . 
G 2 HOH 127 427 385 HOH HOH C . 
G 2 HOH 128 428 34  HOH HOH C . 
G 2 HOH 129 429 160 HOH HOH C . 
G 2 HOH 130 430 101 HOH HOH C . 
G 2 HOH 131 431 247 HOH HOH C . 
G 2 HOH 132 432 330 HOH HOH C . 
G 2 HOH 133 433 287 HOH HOH C . 
G 2 HOH 134 434 186 HOH HOH C . 
G 2 HOH 135 435 515 HOH HOH C . 
G 2 HOH 136 436 369 HOH HOH C . 
G 2 HOH 137 437 438 HOH HOH C . 
G 2 HOH 138 438 165 HOH HOH C . 
G 2 HOH 139 439 389 HOH HOH C . 
G 2 HOH 140 440 512 HOH HOH C . 
H 2 HOH 1   301 127 HOH HOH D . 
H 2 HOH 2   302 210 HOH HOH D . 
H 2 HOH 3   303 55  HOH HOH D . 
H 2 HOH 4   304 168 HOH HOH D . 
H 2 HOH 5   305 76  HOH HOH D . 
H 2 HOH 6   306 378 HOH HOH D . 
H 2 HOH 7   307 197 HOH HOH D . 
H 2 HOH 8   308 5   HOH HOH D . 
H 2 HOH 9   309 22  HOH HOH D . 
H 2 HOH 10  310 47  HOH HOH D . 
H 2 HOH 11  311 274 HOH HOH D . 
H 2 HOH 12  312 52  HOH HOH D . 
H 2 HOH 13  313 24  HOH HOH D . 
H 2 HOH 14  314 154 HOH HOH D . 
H 2 HOH 15  315 231 HOH HOH D . 
H 2 HOH 16  316 383 HOH HOH D . 
H 2 HOH 17  317 25  HOH HOH D . 
H 2 HOH 18  318 359 HOH HOH D . 
H 2 HOH 19  319 18  HOH HOH D . 
H 2 HOH 20  320 203 HOH HOH D . 
H 2 HOH 21  321 296 HOH HOH D . 
H 2 HOH 22  322 78  HOH HOH D . 
H 2 HOH 23  323 107 HOH HOH D . 
H 2 HOH 24  324 37  HOH HOH D . 
H 2 HOH 25  325 1   HOH HOH D . 
H 2 HOH 26  326 84  HOH HOH D . 
H 2 HOH 27  327 140 HOH HOH D . 
H 2 HOH 28  328 16  HOH HOH D . 
H 2 HOH 29  329 21  HOH HOH D . 
H 2 HOH 30  330 67  HOH HOH D . 
H 2 HOH 31  331 69  HOH HOH D . 
H 2 HOH 32  332 239 HOH HOH D . 
H 2 HOH 33  333 61  HOH HOH D . 
H 2 HOH 34  334 129 HOH HOH D . 
H 2 HOH 35  335 473 HOH HOH D . 
H 2 HOH 36  336 73  HOH HOH D . 
H 2 HOH 37  337 124 HOH HOH D . 
H 2 HOH 38  338 300 HOH HOH D . 
H 2 HOH 39  339 435 HOH HOH D . 
H 2 HOH 40  340 381 HOH HOH D . 
H 2 HOH 41  341 170 HOH HOH D . 
H 2 HOH 42  342 292 HOH HOH D . 
H 2 HOH 43  343 257 HOH HOH D . 
H 2 HOH 44  344 45  HOH HOH D . 
H 2 HOH 45  345 345 HOH HOH D . 
H 2 HOH 46  346 356 HOH HOH D . 
H 2 HOH 47  347 259 HOH HOH D . 
H 2 HOH 48  348 50  HOH HOH D . 
H 2 HOH 49  349 70  HOH HOH D . 
H 2 HOH 50  350 207 HOH HOH D . 
H 2 HOH 51  351 318 HOH HOH D . 
H 2 HOH 52  352 156 HOH HOH D . 
H 2 HOH 53  353 176 HOH HOH D . 
H 2 HOH 54  354 271 HOH HOH D . 
H 2 HOH 55  355 285 HOH HOH D . 
H 2 HOH 56  356 372 HOH HOH D . 
H 2 HOH 57  357 93  HOH HOH D . 
H 2 HOH 58  358 33  HOH HOH D . 
H 2 HOH 59  359 360 HOH HOH D . 
H 2 HOH 60  360 414 HOH HOH D . 
H 2 HOH 61  361 253 HOH HOH D . 
H 2 HOH 62  362 72  HOH HOH D . 
H 2 HOH 63  363 249 HOH HOH D . 
H 2 HOH 64  364 94  HOH HOH D . 
H 2 HOH 65  365 377 HOH HOH D . 
H 2 HOH 66  366 178 HOH HOH D . 
H 2 HOH 67  367 35  HOH HOH D . 
H 2 HOH 68  368 96  HOH HOH D . 
H 2 HOH 69  369 478 HOH HOH D . 
H 2 HOH 70  370 538 HOH HOH D . 
H 2 HOH 71  371 200 HOH HOH D . 
H 2 HOH 72  372 77  HOH HOH D . 
H 2 HOH 73  373 408 HOH HOH D . 
H 2 HOH 74  374 230 HOH HOH D . 
H 2 HOH 75  375 172 HOH HOH D . 
H 2 HOH 76  376 122 HOH HOH D . 
H 2 HOH 77  377 405 HOH HOH D . 
H 2 HOH 78  378 246 HOH HOH D . 
H 2 HOH 79  379 157 HOH HOH D . 
H 2 HOH 80  380 411 HOH HOH D . 
H 2 HOH 81  381 557 HOH HOH D . 
H 2 HOH 82  382 54  HOH HOH D . 
H 2 HOH 83  383 280 HOH HOH D . 
H 2 HOH 84  384 519 HOH HOH D . 
H 2 HOH 85  385 449 HOH HOH D . 
H 2 HOH 86  386 553 HOH HOH D . 
H 2 HOH 87  387 145 HOH HOH D . 
H 2 HOH 88  388 97  HOH HOH D . 
H 2 HOH 89  389 446 HOH HOH D . 
H 2 HOH 90  390 456 HOH HOH D . 
H 2 HOH 91  391 500 HOH HOH D . 
H 2 HOH 92  392 520 HOH HOH D . 
H 2 HOH 93  393 420 HOH HOH D . 
H 2 HOH 94  394 409 HOH HOH D . 
H 2 HOH 95  395 258 HOH HOH D . 
H 2 HOH 96  396 427 HOH HOH D . 
H 2 HOH 97  397 506 HOH HOH D . 
H 2 HOH 98  398 228 HOH HOH D . 
H 2 HOH 99  399 425 HOH HOH D . 
H 2 HOH 100 400 219 HOH HOH D . 
H 2 HOH 101 401 322 HOH HOH D . 
H 2 HOH 102 402 341 HOH HOH D . 
H 2 HOH 103 403 297 HOH HOH D . 
H 2 HOH 104 404 391 HOH HOH D . 
H 2 HOH 105 405 458 HOH HOH D . 
H 2 HOH 106 406 293 HOH HOH D . 
H 2 HOH 107 407 477 HOH HOH D . 
H 2 HOH 108 408 445 HOH HOH D . 
H 2 HOH 109 409 309 HOH HOH D . 
H 2 HOH 110 410 439 HOH HOH D . 
H 2 HOH 111 411 398 HOH HOH D . 
H 2 HOH 112 412 384 HOH HOH D . 
H 2 HOH 113 413 245 HOH HOH D . 
H 2 HOH 114 414 516 HOH HOH D . 
H 2 HOH 115 415 501 HOH HOH D . 
H 2 HOH 116 416 401 HOH HOH D . 
H 2 HOH 117 417 481 HOH HOH D . 
H 2 HOH 118 418 517 HOH HOH D . 
H 2 HOH 119 419 332 HOH HOH D . 
H 2 HOH 120 420 233 HOH HOH D . 
H 2 HOH 121 421 455 HOH HOH D . 
H 2 HOH 122 422 81  HOH HOH D . 
H 2 HOH 123 423 443 HOH HOH D . 
H 2 HOH 124 424 119 HOH HOH D . 
H 2 HOH 125 425 390 HOH HOH D . 
H 2 HOH 126 426 295 HOH HOH D . 
H 2 HOH 127 427 490 HOH HOH D . 
H 2 HOH 128 428 416 HOH HOH D . 
H 2 HOH 129 429 440 HOH HOH D . 
H 2 HOH 130 430 471 HOH HOH D . 
H 2 HOH 131 431 495 HOH HOH D . 
H 2 HOH 132 432 366 HOH HOH D . 
# 
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' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.63 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z4N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.476 
_cell.length_a_esd                 ? 
_cell.length_b                     88.024 
_cell.length_b_esd                 ? 
_cell.length_c                     87.412 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z4N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z4N 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.93 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Salt:40.2 M Potassium phosphate dibasic;
Precipitant:20% w/v Polyethylene glycol 3,350, pH 9.2;
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-30 
_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   0.987 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          28.13 
_reflns.entry_id                                       8Z4N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.769 
_reflns.d_resolution_low                               74.45 
_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                                     109917 
_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                           92.39 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.72 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.132 
_reflns.pdbx_Rpim_I_all                                0.05176 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1211 
_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                                    1.769 
_reflns_shell.d_res_low                                     1.832 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.29 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9277 
_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                               6.4 
_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                               1.627 
_reflns_shell.pdbx_Rpim_I_all                               0.635 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.677 
_reflns_shell.pdbx_CC_star                                  0.899 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          84.77 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.494 
_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                                 8Z4N 
_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                            1.769 
_refine.ls_d_res_low                             74.45 
_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                     101628 
_refine.ls_number_reflns_R_free                  5164 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.39 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2601 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2271 
_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                    ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.769 
_refine_hist.d_res_low                        74.45 
_refine_hist.number_atoms_solvent             557 
_refine_hist.number_atoms_total               7923 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7366 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.R_factor_R_free                  0.4937 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.4809 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.d_res_high                       1.769 
_refine_ls_shell.d_res_low                        1.832 
_refine_ls_shell.number_reflns_R_free             482 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                9273 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
# 
_struct.entry_id                     8Z4N 
_struct.title                        'Pseudomurein Endoisopeptidase PeiR-C90A' 
_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        8Z4N 
_struct_keywords.text            'Methanogenic archaea, pseudomurein, endopeptidases, C39 peptidase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    D3DZZ6_METRM 
_struct_ref.pdbx_db_accession          D3DZZ6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVRFSRDMLQDGAKRMFKWLRKGEGLPNYLIMYDMDRNKEYKLVPKEYAGLYESRNIFWIKNGREPNYVTLTSVARNPLV
MDYQNTNYTCCPTSLSLASQMLYHYKSESECAKALGTSKGSGTSPAQLIANAPKLGFKIIPIKRDSKEVKKYLKKGFPVI
CHWQVNQSRNCKGDYTGNFGHYGLIWDMTSTHYVVADPAKGVNRKYKFSCLDNANKGYRQNYYVVCPA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Z4N A 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
2 1 8Z4N B 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
3 1 8Z4N C 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
4 1 8Z4N D 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Z4N ALA A 90 ? UNP D3DZZ6 CYS 90 'engineered mutation' 90 1 
2 8Z4N ALA B 90 ? UNP D3DZZ6 CYS 90 'engineered mutation' 90 2 
3 8Z4N ALA C 90 ? UNP D3DZZ6 CYS 90 'engineered mutation' 90 3 
4 8Z4N ALA D 90 ? UNP D3DZZ6 CYS 90 'engineered mutation' 90 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2170  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  19340 ? 
2 'ABSA (A^2)' 2120  ? 
2 MORE         -6    ? 
2 'SSA (A^2)'  19540 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,G 
2 1 B,D,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 ARG A 6   ? ARG A 21  ? ARG A 6   ARG A 21  1 ? 16 
HELX_P HELX_P2  AA2 VAL A 44  ? GLY A 63  ? VAL A 44  GLY A 63  1 ? 20 
HELX_P HELX_P3  AA3 THR A 89  ? LEU A 102 ? THR A 89  LEU A 102 1 ? 14 
HELX_P HELX_P4  AA4 SER A 107 ? GLY A 116 ? SER A 107 GLY A 116 1 ? 10 
HELX_P HELX_P5  AA5 SER A 124 ? ALA A 132 ? SER A 124 ALA A 132 1 ? 9  
HELX_P HELX_P6  AA6 PRO A 133 ? LEU A 135 ? PRO A 133 LEU A 135 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 145 ? LYS A 155 ? ASP A 145 LYS A 155 1 ? 11 
HELX_P HELX_P8  AA8 ASN A 166 ? ARG A 169 ? ASN A 166 ARG A 169 5 ? 4  
HELX_P HELX_P9  AA9 PHE A 208 ? ASN A 213 ? PHE A 208 ASN A 213 1 ? 6  
HELX_P HELX_P10 AB1 ARG B 6   ? ARG B 21  ? ARG B 6   ARG B 21  1 ? 16 
HELX_P HELX_P11 AB2 VAL B 44  ? GLY B 63  ? VAL B 44  GLY B 63  1 ? 20 
HELX_P HELX_P12 AB3 THR B 89  ? LEU B 102 ? THR B 89  LEU B 102 1 ? 14 
HELX_P HELX_P13 AB4 SER B 107 ? GLY B 116 ? SER B 107 GLY B 116 1 ? 10 
HELX_P HELX_P14 AB5 SER B 124 ? ALA B 132 ? SER B 124 ALA B 132 1 ? 9  
HELX_P HELX_P15 AB6 PRO B 133 ? LEU B 135 ? PRO B 133 LEU B 135 5 ? 3  
HELX_P HELX_P16 AB7 ASP B 145 ? LYS B 155 ? ASP B 145 LYS B 155 1 ? 11 
HELX_P HELX_P17 AB8 ASN B 166 ? ARG B 169 ? ASN B 166 ARG B 169 5 ? 4  
HELX_P HELX_P18 AB9 PHE B 208 ? ASN B 213 ? PHE B 208 ASN B 213 1 ? 6  
HELX_P HELX_P19 AC1 ARG C 6   ? ARG C 21  ? ARG C 6   ARG C 21  1 ? 16 
HELX_P HELX_P20 AC2 VAL C 44  ? GLY C 63  ? VAL C 44  GLY C 63  1 ? 20 
HELX_P HELX_P21 AC3 THR C 89  ? LEU C 102 ? THR C 89  LEU C 102 1 ? 14 
HELX_P HELX_P22 AC4 SER C 107 ? GLY C 116 ? SER C 107 GLY C 116 1 ? 10 
HELX_P HELX_P23 AC5 SER C 124 ? ALA C 132 ? SER C 124 ALA C 132 1 ? 9  
HELX_P HELX_P24 AC6 PRO C 133 ? LEU C 135 ? PRO C 133 LEU C 135 5 ? 3  
HELX_P HELX_P25 AC7 ASP C 145 ? LYS C 154 ? ASP C 145 LYS C 154 1 ? 10 
HELX_P HELX_P26 AC8 ASN C 166 ? ARG C 169 ? ASN C 166 ARG C 169 5 ? 4  
HELX_P HELX_P27 AC9 PHE C 208 ? ASN C 213 ? PHE C 208 ASN C 213 1 ? 6  
HELX_P HELX_P28 AD1 ARG D 6   ? ARG D 21  ? ARG D 6   ARG D 21  1 ? 16 
HELX_P HELX_P29 AD2 VAL D 44  ? GLY D 63  ? VAL D 44  GLY D 63  1 ? 20 
HELX_P HELX_P30 AD3 THR D 89  ? LEU D 102 ? THR D 89  LEU D 102 1 ? 14 
HELX_P HELX_P31 AD4 SER D 107 ? GLY D 116 ? SER D 107 GLY D 116 1 ? 10 
HELX_P HELX_P32 AD5 SER D 124 ? ALA D 132 ? SER D 124 ALA D 132 1 ? 9  
HELX_P HELX_P33 AD6 PRO D 133 ? LEU D 135 ? PRO D 133 LEU D 135 5 ? 3  
HELX_P HELX_P34 AD7 ASP D 145 ? LYS D 155 ? ASP D 145 LYS D 155 1 ? 11 
HELX_P HELX_P35 AD8 ASN D 166 ? ARG D 169 ? ASN D 166 ARG D 169 5 ? 4  
HELX_P HELX_P36 AD9 PHE D 208 ? ASN D 213 ? PHE D 208 ASN D 213 1 ? 6  
# 
_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 171 SG ? ? ? 1_555 A CYS 210 SG ? ? A CYS 171 A CYS 210 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
disulf2 disulf ? ? B CYS 171 SG ? ? ? 1_555 B CYS 210 SG ? ? B CYS 171 B CYS 210 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
disulf3 disulf ? ? C CYS 171 SG ? ? ? 1_555 C CYS 210 SG ? ? C CYS 171 C CYS 210 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf4 disulf ? ? D CYS 171 SG ? ? ? 1_555 D CYS 210 SG ? ? D CYS 171 D CYS 210 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 171 ? CYS A 210 ? CYS A 171 ? 1_555 CYS A 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 171 ? CYS B 210 ? CYS B 171 ? 1_555 CYS B 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 171 ? CYS C 210 ? CYS C 171 ? 1_555 CYS C 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 171 ? CYS D 210 ? CYS D 171 ? 1_555 CYS D 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 6 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 6 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB3 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 ARG A 3   ? SER A 5   ? ARG A 3   SER A 5   
AA1 2 TYR A 68  ? THR A 70  ? TYR A 68  THR A 70  
AA2 1 LEU A 30  ? TYR A 33  ? LEU A 30  TYR A 33  
AA2 2 GLU A 40  ? LEU A 43  ? GLU A 40  LEU A 43  
AA3 1 PHE A 137 ? ILE A 142 ? PHE A 137 ILE A 142 
AA3 2 TYR A 222 ? PRO A 227 ? TYR A 222 PRO A 227 
AA3 3 VAL A 159 ? GLN A 164 ? VAL A 159 GLN A 164 
AA3 4 GLY A 180 ? MET A 188 ? GLY A 180 MET A 188 
AA3 5 HIS A 192 ? ASP A 197 ? HIS A 192 ASP A 197 
AA3 6 GLY A 201 ? LYS A 207 ? GLY A 201 LYS A 207 
AA4 1 ARG B 3   ? SER B 5   ? ARG B 3   SER B 5   
AA4 2 TYR B 68  ? THR B 70  ? TYR B 68  THR B 70  
AA5 1 LEU B 30  ? TYR B 33  ? LEU B 30  TYR B 33  
AA5 2 GLU B 40  ? LEU B 43  ? GLU B 40  LEU B 43  
AA6 1 PHE B 137 ? LYS B 143 ? PHE B 137 LYS B 143 
AA6 2 ASN B 221 ? PRO B 227 ? ASN B 221 PRO B 227 
AA6 3 VAL B 159 ? GLN B 164 ? VAL B 159 GLN B 164 
AA6 4 GLY B 180 ? MET B 188 ? GLY B 180 MET B 188 
AA6 5 HIS B 192 ? ASP B 197 ? HIS B 192 ASP B 197 
AA6 6 GLY B 201 ? LYS B 207 ? GLY B 201 LYS B 207 
AA7 1 ARG C 3   ? SER C 5   ? ARG C 3   SER C 5   
AA7 2 TYR C 68  ? THR C 70  ? TYR C 68  THR C 70  
AA8 1 LEU C 30  ? TYR C 33  ? LEU C 30  TYR C 33  
AA8 2 GLU C 40  ? LEU C 43  ? GLU C 40  LEU C 43  
AA9 1 PHE C 137 ? ILE C 142 ? PHE C 137 ILE C 142 
AA9 2 TYR C 222 ? PRO C 227 ? TYR C 222 PRO C 227 
AA9 3 VAL C 159 ? GLN C 164 ? VAL C 159 GLN C 164 
AA9 4 GLY C 180 ? MET C 188 ? GLY C 180 MET C 188 
AA9 5 HIS C 192 ? ASP C 197 ? HIS C 192 ASP C 197 
AA9 6 GLY C 201 ? LYS C 207 ? GLY C 201 LYS C 207 
AB1 1 ARG D 3   ? SER D 5   ? ARG D 3   SER D 5   
AB1 2 TYR D 68  ? THR D 70  ? TYR D 68  THR D 70  
AB2 1 LEU D 30  ? TYR D 33  ? LEU D 30  TYR D 33  
AB2 2 GLU D 40  ? LEU D 43  ? GLU D 40  LEU D 43  
AB3 1 PHE D 137 ? ILE D 142 ? PHE D 137 ILE D 142 
AB3 2 TYR D 222 ? PRO D 227 ? TYR D 222 PRO D 227 
AB3 3 VAL D 159 ? GLN D 164 ? VAL D 159 GLN D 164 
AB3 4 GLY D 180 ? MET D 188 ? GLY D 180 MET D 188 
AB3 5 HIS D 192 ? ASP D 197 ? HIS D 192 ASP D 197 
AB3 6 GLY D 201 ? LYS D 207 ? GLY D 201 LYS D 207 
# 
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 PHE A 4   ? N PHE A 4   O VAL A 69  ? O VAL A 69  
AA2 1 2 N MET A 32  ? N MET A 32  O TYR A 41  ? O TYR A 41  
AA3 1 2 N LYS A 138 ? N LYS A 138 O CYS A 226 ? O CYS A 226 
AA3 2 3 O TYR A 223 ? O TYR A 223 N ILE A 160 ? N ILE A 160 
AA3 3 4 N VAL A 159 ? N VAL A 159 O ILE A 185 ? O ILE A 185 
AA3 4 5 N ASP A 187 ? N ASP A 187 O VAL A 194 ? O VAL A 194 
AA3 5 6 N TYR A 193 ? N TYR A 193 O TYR A 206 ? O TYR A 206 
AA4 1 2 N PHE B 4   ? N PHE B 4   O VAL B 69  ? O VAL B 69  
AA5 1 2 N MET B 32  ? N MET B 32  O TYR B 41  ? O TYR B 41  
AA6 1 2 N ILE B 142 ? N ILE B 142 O TYR B 222 ? O TYR B 222 
AA6 2 3 O TYR B 223 ? O TYR B 223 N ILE B 160 ? N ILE B 160 
AA6 3 4 N VAL B 159 ? N VAL B 159 O ILE B 185 ? O ILE B 185 
AA6 4 5 N LEU B 184 ? N LEU B 184 O ALA B 196 ? O ALA B 196 
AA6 5 6 N TYR B 193 ? N TYR B 193 O TYR B 206 ? O TYR B 206 
AA7 1 2 N PHE C 4   ? N PHE C 4   O VAL C 69  ? O VAL C 69  
AA8 1 2 N MET C 32  ? N MET C 32  O TYR C 41  ? O TYR C 41  
AA9 1 2 N LYS C 138 ? N LYS C 138 O CYS C 226 ? O CYS C 226 
AA9 2 3 O TYR C 223 ? O TYR C 223 N ILE C 160 ? N ILE C 160 
AA9 3 4 N VAL C 159 ? N VAL C 159 O ILE C 185 ? O ILE C 185 
AA9 4 5 N ASP C 187 ? N ASP C 187 O VAL C 194 ? O VAL C 194 
AA9 5 6 N VAL C 195 ? N VAL C 195 O ARG C 204 ? O ARG C 204 
AB1 1 2 N PHE D 4   ? N PHE D 4   O VAL D 69  ? O VAL D 69  
AB2 1 2 N MET D 32  ? N MET D 32  O TYR D 41  ? O TYR D 41  
AB3 1 2 N LYS D 138 ? N LYS D 138 O CYS D 226 ? O CYS D 226 
AB3 2 3 O TYR D 223 ? O TYR D 223 N ILE D 160 ? N ILE D 160 
AB3 3 4 N VAL D 159 ? N VAL D 159 O ILE D 185 ? O ILE D 185 
AB3 4 5 N LEU D 184 ? N LEU D 184 O ALA D 196 ? O ALA D 196 
AB3 5 6 N ASP D 197 ? N ASP D 197 O GLY D 201 ? O GLY D 201 
# 
_pdbx_entry_details.entry_id                   8Z4N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 NZ  C LYS 143 ? ? O C HOH 301 ? ? 1.87 
2  1 O   C HOH 334 ? ? O C HOH 422 ? ? 1.88 
3  1 OD1 A ASN 85  ? ? O A HOH 301 ? ? 1.96 
4  1 OD1 A ASN 170 ? ? O A HOH 302 ? ? 1.97 
5  1 O   A HOH 402 ? ? O A HOH 427 ? ? 1.99 
6  1 OD1 B ASP 11  ? ? O B HOH 301 ? ? 2.00 
7  1 O   D HOH 384 ? ? O D HOH 414 ? ? 2.00 
8  1 O   C HOH 411 ? ? O C HOH 437 ? ? 2.02 
9  1 OE2 C GLU 40  ? ? O C HOH 302 ? ? 2.05 
10 1 O   A HOH 305 ? ? O C HOH 428 ? ? 2.05 
11 1 O   A HOH 433 ? ? O C HOH 418 ? ? 2.05 
12 1 O   A HOH 421 ? ? O C HOH 333 ? ? 2.06 
13 1 O   B HOH 412 ? ? O B HOH 415 ? ? 2.06 
14 1 O   A HOH 432 ? ? O A HOH 433 ? ? 2.07 
15 1 O   A HOH 419 ? ? O A HOH 451 ? ? 2.07 
16 1 O   A HOH 397 ? ? O A HOH 449 ? ? 2.07 
17 1 O   D HOH 384 ? ? O D HOH 416 ? ? 2.07 
18 1 OD1 C ASN 203 ? ? O C HOH 303 ? ? 2.07 
19 1 O   C HOH 320 ? ? O C HOH 414 ? ? 2.07 
20 1 O   D HOH 301 ? ? O D HOH 396 ? ? 2.09 
21 1 O   B HOH 357 ? ? O B HOH 425 ? ? 2.10 
22 1 O   B HOH 382 ? ? O B HOH 426 ? ? 2.11 
23 1 O   A HOH 429 ? ? O A HOH 439 ? ? 2.12 
24 1 OE2 B GLU 110 ? ? O B HOH 302 ? ? 2.13 
25 1 O   A HOH 373 ? ? O A HOH 404 ? ? 2.13 
26 1 OG1 C THR 176 ? ? O C HOH 304 ? ? 2.15 
27 1 O   B HOH 367 ? ? O B HOH 432 ? ? 2.15 
28 1 O   A HOH 306 ? ? O A HOH 393 ? ? 2.16 
29 1 O   D HOH 360 ? ? O D HOH 406 ? ? 2.16 
30 1 O   C HOH 373 ? ? O C HOH 408 ? ? 2.17 
31 1 O   B HOH 316 ? ? O B HOH 422 ? ? 2.17 
32 1 ND2 C ASN 38  ? ? O C HOH 305 ? ? 2.19 
33 1 O   C HOH 333 ? ? O C HOH 428 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 429 ? ? 1_555 O C HOH 335 ? ? 2_545 2.10 
2 1 O B HOH 363 ? ? 1_555 O D HOH 381 ? ? 2_544 2.17 
3 1 O A HOH 389 ? ? 1_555 O C HOH 353 ? ? 2_645 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 36  ? ? -98.23  -60.36 
2 1 LYS A 172 ? ? -137.58 -59.96 
3 1 LYS A 200 ? ? -142.54 -45.78 
4 1 LYS B 200 ? ? -139.25 -48.59 
5 1 LYS C 172 ? ? -140.52 -56.60 
6 1 LYS C 200 ? ? -139.93 -50.56 
7 1 LYS D 172 ? ? -137.36 -58.70 
8 1 LYS D 200 ? ? -141.08 -49.30 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 42203080 1 
'National Natural Science Foundation of China (NSFC)' China 31970066 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z4N 
_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]   0.013427 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000382 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011361 
_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]   0.011445 
_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   . MET A 1 1   ? 40.882  13.525  3.675   1.00 55.07 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 42.241  13.104  3.246   1.00 55.85 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 42.165  12.145  2.042   1.00 51.54 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 42.330  12.619  0.930   1.00 54.05 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 43.004  12.454  4.407   1.00 66.25 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 44.500  12.697  4.339   1.00 67.61 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 44.813  13.388  2.724   1.00 89.11 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 46.520  12.918  2.457   1.00 67.00 ? 1   MET A CE  1 
ATOM   9    N N   . VAL A 1 2   ? 41.915  10.858  2.284   1.00 46.91 ? 2   VAL A N   1 
ATOM   10   C CA  . VAL A 1 2   ? 41.838  9.776   1.259   1.00 42.39 ? 2   VAL A CA  1 
ATOM   11   C C   . VAL A 1 2   ? 40.476  9.807   0.553   1.00 40.14 ? 2   VAL A C   1 
ATOM   12   O O   . VAL A 1 2   ? 39.482  10.039  1.199   1.00 35.97 ? 2   VAL A O   1 
ATOM   13   C CB  . VAL A 1 2   ? 42.101  8.415   1.930   1.00 43.08 ? 2   VAL A CB  1 
ATOM   14   C CG1 . VAL A 1 2   ? 42.040  7.258   0.960   1.00 42.56 ? 2   VAL A CG1 1 
ATOM   15   C CG2 . VAL A 1 2   ? 43.408  8.395   2.689   1.00 44.85 ? 2   VAL A CG2 1 
ATOM   16   N N   . ARG A 1 3   ? 40.472  9.519   -0.741  1.00 37.39 ? 3   ARG A N   1 
ATOM   17   C CA  . ARG A 1 3   ? 39.263  9.539   -1.589  1.00 34.18 ? 3   ARG A CA  1 
ATOM   18   C C   . ARG A 1 3   ? 39.045  8.191   -2.279  1.00 36.40 ? 3   ARG A C   1 
ATOM   19   O O   . ARG A 1 3   ? 40.007  7.529   -2.687  1.00 34.46 ? 3   ARG A O   1 
ATOM   20   C CB  . ARG A 1 3   ? 39.308  10.606  -2.722  1.00 35.50 ? 3   ARG A CB  1 
ATOM   21   C CG  . ARG A 1 3   ? 40.024  11.895  -2.401  1.00 43.78 ? 3   ARG A CG  1 
ATOM   22   C CD  . ARG A 1 3   ? 39.720  12.944  -3.466  1.00 45.03 ? 3   ARG A CD  1 
ATOM   23   N NE  . ARG A 1 3   ? 40.864  13.173  -4.349  1.00 51.58 ? 3   ARG A NE  1 
ATOM   24   C CZ  . ARG A 1 3   ? 40.792  13.167  -5.674  1.00 54.07 ? 3   ARG A CZ  1 
ATOM   25   N NH1 . ARG A 1 3   ? 39.677  12.820  -6.300  1.00 51.04 ? 3   ARG A NH1 1 
ATOM   26   N NH2 . ARG A 1 3   ? 41.867  13.500  -6.389  1.00 51.50 ? 3   ARG A NH2 1 
ATOM   27   N N   . PHE A 1 4   ? 37.770  7.802   -2.456  1.00 30.35 ? 4   PHE A N   1 
ATOM   28   C CA  . PHE A 1 4   ? 37.425  6.527   -3.070  1.00 26.95 ? 4   PHE A CA  1 
ATOM   29   C C   . PHE A 1 4   ? 36.456  6.762   -4.212  1.00 29.81 ? 4   PHE A C   1 
ATOM   30   O O   . PHE A 1 4   ? 35.452  7.460   -4.050  1.00 30.91 ? 4   PHE A O   1 
ATOM   31   C CB  . PHE A 1 4   ? 36.827  5.575   -2.034  1.00 29.71 ? 4   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 4   ? 37.777  5.236   -0.935  1.00 26.86 ? 4   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 4   ? 38.779  4.302   -1.140  1.00 30.69 ? 4   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 4   ? 37.687  5.864   0.298   1.00 28.75 ? 4   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 4   ? 39.672  3.988   -0.131  1.00 32.78 ? 4   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 4   ? 38.567  5.568   1.312   1.00 31.18 ? 4   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 4   ? 39.575  4.620   1.100   1.00 32.88 ? 4   PHE A CZ  1 
ATOM   38   N N   . SER A 1 5   ? 36.734  6.142   -5.351  1.00 29.98 ? 5   SER A N   1 
ATOM   39   C CA  . SER A 1 5   ? 35.962  6.371   -6.563  1.00 30.49 ? 5   SER A CA  1 
ATOM   40   C C   . SER A 1 5   ? 34.590  5.699   -6.485  1.00 31.68 ? 5   SER A C   1 
ATOM   41   O O   . SER A 1 5   ? 34.325  4.856   -5.631  1.00 27.76 ? 5   SER A O   1 
ATOM   42   C CB  . SER A 1 5   ? 36.717  5.808   -7.765  1.00 33.59 ? 5   SER A CB  1 
ATOM   43   O OG  . SER A 1 5   ? 36.704  4.393   -7.670  1.00 31.72 ? 5   SER A OG  1 
ATOM   44   N N   . ARG A 1 6   ? 33.726  6.051   -7.439  1.00 31.72 ? 6   ARG A N   1 
ATOM   45   C CA  . ARG A 1 6   ? 32.413  5.427   -7.519  1.00 31.48 ? 6   ARG A CA  1 
ATOM   46   C C   . ARG A 1 6   ? 32.533  3.917   -7.724  1.00 33.49 ? 6   ARG A C   1 
ATOM   47   O O   . ARG A 1 6   ? 31.832  3.132   -7.067  1.00 30.80 ? 6   ARG A O   1 
ATOM   48   C CB  . ARG A 1 6   ? 31.623  6.073   -8.655  1.00 33.29 ? 6   ARG A CB  1 
ATOM   49   C CG  . ARG A 1 6   ? 30.378  5.338   -9.110  1.00 37.51 ? 6   ARG A CG  1 
ATOM   50   C CD  . ARG A 1 6   ? 29.697  6.173   -10.198 1.00 36.35 ? 6   ARG A CD  1 
ATOM   51   N NE  . ARG A 1 6   ? 29.802  5.559   -11.515 1.00 45.43 ? 6   ARG A NE  1 
ATOM   52   C CZ  . ARG A 1 6   ? 30.231  6.181   -12.607 1.00 53.40 ? 6   ARG A CZ  1 
ATOM   53   N NH1 . ARG A 1 6   ? 30.691  7.422   -12.563 1.00 48.82 ? 6   ARG A NH1 1 
ATOM   54   N NH2 . ARG A 1 6   ? 30.236  5.528   -13.767 1.00 56.24 ? 6   ARG A NH2 1 
ATOM   55   N N   . ASP A 1 7   ? 33.435  3.493   -8.614  1.00 31.96 ? 7   ASP A N   1 
ATOM   56   C CA  . ASP A 1 7   ? 33.643  2.066   -8.844  1.00 32.86 ? 7   ASP A CA  1 
ATOM   57   C C   . ASP A 1 7   ? 34.063  1.359   -7.572  1.00 28.02 ? 7   ASP A C   1 
ATOM   58   O O   . ASP A 1 7   ? 33.560  0.267   -7.270  1.00 27.76 ? 7   ASP A O   1 
ATOM   59   C CB  . ASP A 1 7   ? 34.690  1.840   -9.939  1.00 37.52 ? 7   ASP A CB  1 
ATOM   60   C CG  . ASP A 1 7   ? 34.173  2.201   -11.315 1.00 46.84 ? 7   ASP A CG  1 
ATOM   61   O OD1 . ASP A 1 7   ? 32.998  2.625   -11.423 1.00 49.42 ? 7   ASP A OD1 1 
ATOM   62   O OD2 . ASP A 1 7   ? 34.934  2.043   -12.296 1.00 54.25 ? 7   ASP A OD2 1 
ATOM   63   N N   . MET A 1 8   ? 34.990  1.959   -6.820  1.00 25.80 ? 8   MET A N   1 
ATOM   64   C CA  . MET A 1 8   ? 35.412  1.365   -5.556  1.00 25.45 ? 8   MET A CA  1 
ATOM   65   C C   . MET A 1 8   ? 34.249  1.294   -4.566  1.00 28.79 ? 8   MET A C   1 
ATOM   66   O O   . MET A 1 8   ? 34.081  0.298   -3.862  1.00 27.89 ? 8   MET A O   1 
ATOM   67   C CB  . MET A 1 8   ? 36.536  2.186   -4.936  1.00 25.27 ? 8   MET A CB  1 
ATOM   68   C CG  . MET A 1 8   ? 37.289  1.511   -3.809  1.00 27.05 ? 8   MET A CG  1 
ATOM   69   S SD  . MET A 1 8   ? 38.207  0.011   -4.316  1.00 32.78 ? 8   MET A SD  1 
ATOM   70   C CE  . MET A 1 8   ? 37.293  -1.258  -3.511  1.00 29.13 ? 8   MET A CE  1 
ATOM   71   N N   . LEU A 1 9   ? 33.439  2.346   -4.492  1.00 28.30 ? 9   LEU A N   1 
ATOM   72   C CA  . LEU A 1 9   ? 32.333  2.323   -3.538  1.00 28.14 ? 9   LEU A CA  1 
ATOM   73   C C   . LEU A 1 9   ? 31.332  1.243   -3.900  1.00 26.31 ? 9   LEU A C   1 
ATOM   74   O O   . LEU A 1 9   ? 30.838  0.532   -3.016  1.00 27.66 ? 9   LEU A O   1 
ATOM   75   C CB  . LEU A 1 9   ? 31.664  3.683   -3.492  1.00 24.71 ? 9   LEU A CB  1 
ATOM   76   C CG  . LEU A 1 9   ? 32.636  4.782   -3.038  1.00 26.00 ? 9   LEU A CG  1 
ATOM   77   C CD1 . LEU A 1 9   ? 32.166  6.146   -3.487  1.00 26.93 ? 9   LEU A CD1 1 
ATOM   78   C CD2 . LEU A 1 9   ? 32.851  4.753   -1.567  1.00 24.94 ? 9   LEU A CD2 1 
ATOM   79   N N   . GLN A 1 10  ? 31.028  1.101   -5.192  1.00 27.53 ? 10  GLN A N   1 
ATOM   80   C CA  . GLN A 1 10  ? 30.120  0.043   -5.626  1.00 27.23 ? 10  GLN A CA  1 
ATOM   81   C C   . GLN A 1 10  ? 30.685  -1.322  -5.270  1.00 29.67 ? 10  GLN A C   1 
ATOM   82   O O   . GLN A 1 10  ? 29.971  -2.183  -4.737  1.00 28.47 ? 10  GLN A O   1 
ATOM   83   C CB  . GLN A 1 10  ? 29.870  0.150   -7.131  1.00 26.24 ? 10  GLN A CB  1 
ATOM   84   C CG  . GLN A 1 10  ? 28.999  1.325   -7.558  1.00 32.85 ? 10  GLN A CG  1 
ATOM   85   C CD  . GLN A 1 10  ? 28.911  1.431   -9.067  1.00 38.51 ? 10  GLN A CD  1 
ATOM   86   O OE1 . GLN A 1 10  ? 29.351  0.532   -9.775  1.00 40.11 ? 10  GLN A OE1 1 
ATOM   87   N NE2 . GLN A 1 10  ? 28.296  2.505   -9.566  1.00 34.23 ? 10  GLN A NE2 1 
ATOM   88   N N   . ASP A 1 11  ? 31.983  -1.516  -5.505  1.00 28.70 ? 11  ASP A N   1 
ATOM   89   C CA  . ASP A 1 11  ? 32.618  -2.795  -5.196  1.00 28.83 ? 11  ASP A CA  1 
ATOM   90   C C   . ASP A 1 11  ? 32.593  -3.078  -3.703  1.00 29.93 ? 11  ASP A C   1 
ATOM   91   O O   . ASP A 1 11  ? 32.288  -4.200  -3.277  1.00 29.91 ? 11  ASP A O   1 
ATOM   92   C CB  . ASP A 1 11  ? 34.066  -2.801  -5.690  1.00 27.66 ? 11  ASP A CB  1 
ATOM   93   C CG  . ASP A 1 11  ? 34.810  -4.037  -5.242  1.00 31.85 ? 11  ASP A CG  1 
ATOM   94   O OD1 . ASP A 1 11  ? 34.563  -5.063  -5.896  1.00 32.63 ? 11  ASP A OD1 1 
ATOM   95   O OD2 . ASP A 1 11  ? 35.565  -4.015  -4.232  1.00 31.25 ? 11  ASP A OD2 1 
ATOM   96   N N   . GLY A 1 12  ? 32.944  -2.078  -2.889  1.00 27.12 ? 12  GLY A N   1 
ATOM   97   C CA  . GLY A 1 12  ? 32.919  -2.282  -1.456  1.00 24.81 ? 12  GLY A CA  1 
ATOM   98   C C   . GLY A 1 12  ? 31.510  -2.563  -0.968  1.00 27.08 ? 12  GLY A C   1 
ATOM   99   O O   . GLY A 1 12  ? 31.305  -3.392  -0.080  1.00 25.27 ? 12  GLY A O   1 
ATOM   100  N N   . ALA A 1 13  ? 30.520  -1.872  -1.543  1.00 25.32 ? 13  ALA A N   1 
ATOM   101  C CA  . ALA A 1 13  ? 29.163  -2.168  -1.126  1.00 27.21 ? 13  ALA A CA  1 
ATOM   102  C C   . ALA A 1 13  ? 28.792  -3.587  -1.501  1.00 30.30 ? 13  ALA A C   1 
ATOM   103  O O   . ALA A 1 13  ? 28.066  -4.251  -0.747  1.00 30.28 ? 13  ALA A O   1 
ATOM   104  C CB  . ALA A 1 13  ? 28.157  -1.222  -1.781  1.00 27.97 ? 13  ALA A CB  1 
ATOM   105  N N   . LYS A 1 14  ? 29.120  -4.054  -2.697  1.00 28.26 ? 14  LYS A N   1 
ATOM   106  C CA  . LYS A 1 14  ? 28.730  -5.445  -3.046  1.00 32.73 ? 14  LYS A CA  1 
ATOM   107  C C   . LYS A 1 14  ? 29.296  -6.420  -2.020  1.00 31.57 ? 14  LYS A C   1 
ATOM   108  O O   . LYS A 1 14  ? 28.577  -7.261  -1.539  1.00 35.21 ? 14  LYS A O   1 
ATOM   109  C CB  . LYS A 1 14  ? 29.279  -5.852  -4.412  1.00 34.48 ? 14  LYS A CB  1 
ATOM   110  C CG  . LYS A 1 14  ? 28.696  -5.078  -5.581  1.00 44.69 ? 14  LYS A CG  1 
ATOM   111  C CD  . LYS A 1 14  ? 28.778  -5.788  -6.925  1.00 46.30 ? 14  LYS A CD  1 
ATOM   112  C CE  . LYS A 1 14  ? 28.255  -4.988  -8.099  1.00 48.92 ? 14  LYS A CE  1 
ATOM   113  N NZ  . LYS A 1 14  ? 29.316  -4.174  -8.742  1.00 51.47 ? 14  LYS A NZ  1 
ATOM   114  N N   . ARG A 1 15  ? 30.532  -6.193  -1.629  1.00 30.78 ? 15  ARG A N   1 
ATOM   115  C CA  . ARG A 1 15  ? 31.213  -7.092  -0.708  1.00 28.94 ? 15  ARG A CA  1 
ATOM   116  C C   . ARG A 1 15  ? 30.601  -7.005  0.678   1.00 29.66 ? 15  ARG A C   1 
ATOM   117  O O   . ARG A 1 15  ? 30.505  -8.023  1.378   1.00 28.68 ? 15  ARG A O   1 
ATOM   118  C CB  . ARG A 1 15  ? 32.724  -6.788  -0.648  1.00 30.89 ? 15  ARG A CB  1 
ATOM   119  C CG  . ARG A 1 15  ? 33.562  -7.326  -1.830  1.00 26.63 ? 15  ARG A CG  1 
ATOM   120  C CD  . ARG A 1 15  ? 35.062  -7.016  -1.626  1.00 28.91 ? 15  ARG A CD  1 
ATOM   121  N NE  . ARG A 1 15  ? 35.407  -5.659  -2.053  1.00 26.20 ? 15  ARG A NE  1 
ATOM   122  C CZ  . ARG A 1 15  ? 36.065  -4.797  -1.295  1.00 26.01 ? 15  ARG A CZ  1 
ATOM   123  N NH1 . ARG A 1 15  ? 36.484  -5.122  -0.085  1.00 24.96 ? 15  ARG A NH1 1 
ATOM   124  N NH2 . ARG A 1 15  ? 36.299  -3.574  -1.757  1.00 28.66 ? 15  ARG A NH2 1 
ATOM   125  N N   . MET A 1 16  ? 30.163  -5.808  1.098   1.00 29.87 ? 16  MET A N   1 
ATOM   126  C CA  . MET A 1 16  ? 29.481  -5.721  2.385   1.00 27.69 ? 16  MET A CA  1 
ATOM   127  C C   . MET A 1 16  ? 28.161  -6.476  2.346   1.00 28.29 ? 16  MET A C   1 
ATOM   128  O O   . MET A 1 16  ? 27.822  -7.181  3.295   1.00 31.17 ? 16  MET A O   1 
ATOM   129  C CB  . MET A 1 16  ? 29.229  -4.260  2.777   1.00 27.54 ? 16  MET A CB  1 
ATOM   130  C CG  . MET A 1 16  ? 30.502  -3.493  3.126   1.00 26.29 ? 16  MET A CG  1 
ATOM   131  S SD  . MET A 1 16  ? 31.165  -3.941  4.705   1.00 31.72 ? 16  MET A SD  1 
ATOM   132  C CE  . MET A 1 16  ? 29.807  -3.543  5.798   1.00 29.04 ? 16  MET A CE  1 
ATOM   133  N N   . PHE A 1 17  ? 27.405  -6.323  1.255   1.00 29.02 ? 17  PHE A N   1 
ATOM   134  C CA  . PHE A 1 17  ? 26.118  -6.998  1.091   1.00 28.04 ? 17  PHE A CA  1 
ATOM   135  C C   . PHE A 1 17  ? 26.309  -8.514  1.089   1.00 30.35 ? 17  PHE A C   1 
ATOM   136  O O   . PHE A 1 17  ? 25.613  -9.239  1.801   1.00 29.78 ? 17  PHE A O   1 
ATOM   137  C CB  . PHE A 1 17  ? 25.477  -6.488  -0.209  1.00 27.91 ? 17  PHE A CB  1 
ATOM   138  C CG  . PHE A 1 17  ? 24.092  -7.034  -0.517  1.00 30.70 ? 17  PHE A CG  1 
ATOM   139  C CD1 . PHE A 1 17  ? 22.997  -6.694  0.259   1.00 27.69 ? 17  PHE A CD1 1 
ATOM   140  C CD2 . PHE A 1 17  ? 23.895  -7.862  -1.626  1.00 32.63 ? 17  PHE A CD2 1 
ATOM   141  C CE1 . PHE A 1 17  ? 21.720  -7.163  -0.051  1.00 30.02 ? 17  PHE A CE1 1 
ATOM   142  C CE2 . PHE A 1 17  ? 22.624  -8.360  -1.932  1.00 34.97 ? 17  PHE A CE2 1 
ATOM   143  C CZ  . PHE A 1 17  ? 21.532  -7.991  -1.149  1.00 31.70 ? 17  PHE A CZ  1 
ATOM   144  N N   . LYS A 1 18  ? 27.294  -9.012  0.335   1.00 30.57 ? 18  LYS A N   1 
ATOM   145  C CA  . LYS A 1 18  ? 27.558  -10.457 0.364   1.00 30.68 ? 18  LYS A CA  1 
ATOM   146  C C   . LYS A 1 18  ? 27.988  -10.933 1.748   1.00 30.73 ? 18  LYS A C   1 
ATOM   147  O O   . LYS A 1 18  ? 27.578  -12.012 2.193   1.00 32.49 ? 18  LYS A O   1 
ATOM   148  C CB  . LYS A 1 18  ? 28.619  -10.870 -0.654  1.00 32.09 ? 18  LYS A CB  1 
ATOM   149  C CG  . LYS A 1 18  ? 28.188  -10.968 -2.112  1.00 40.29 ? 18  LYS A CG  1 
ATOM   150  C CD  . LYS A 1 18  ? 29.449  -11.287 -2.965  1.00 45.25 ? 18  LYS A CD  1 
ATOM   151  C CE  . LYS A 1 18  ? 29.346  -10.950 -4.451  1.00 47.95 ? 18  LYS A CE  1 
ATOM   152  N NZ  . LYS A 1 18  ? 27.965  -10.979 -5.017  1.00 51.15 ? 18  LYS A NZ  1 
ATOM   153  N N   . TRP A 1 19  ? 28.794  -10.147 2.459   1.00 27.57 ? 19  TRP A N   1 
ATOM   154  C CA  . TRP A 1 19  ? 29.179  -10.548 3.813   1.00 31.08 ? 19  TRP A CA  1 
ATOM   155  C C   . TRP A 1 19  ? 27.967  -10.635 4.733   1.00 33.44 ? 19  TRP A C   1 
ATOM   156  O O   . TRP A 1 19  ? 27.831  -11.584 5.524   1.00 32.81 ? 19  TRP A O   1 
ATOM   157  C CB  . TRP A 1 19  ? 30.209  -9.581  4.387   1.00 30.17 ? 19  TRP A CB  1 
ATOM   158  C CG  . TRP A 1 19  ? 30.735  -10.043 5.715   1.00 33.10 ? 19  TRP A CG  1 
ATOM   159  C CD1 . TRP A 1 19  ? 30.152  -9.874  6.943   1.00 33.22 ? 19  TRP A CD1 1 
ATOM   160  C CD2 . TRP A 1 19  ? 31.946  -10.777 5.944   1.00 36.83 ? 19  TRP A CD2 1 
ATOM   161  N NE1 . TRP A 1 19  ? 30.932  -10.442 7.920   1.00 34.81 ? 19  TRP A NE1 1 
ATOM   162  C CE2 . TRP A 1 19  ? 32.040  -11.003 7.334   1.00 37.17 ? 19  TRP A CE2 1 
ATOM   163  C CE3 . TRP A 1 19  ? 32.968  -11.250 5.110   1.00 36.94 ? 19  TRP A CE3 1 
ATOM   164  C CZ2 . TRP A 1 19  ? 33.112  -11.697 7.910   1.00 39.97 ? 19  TRP A CZ2 1 
ATOM   165  C CZ3 . TRP A 1 19  ? 34.040  -11.941 5.688   1.00 39.29 ? 19  TRP A CZ3 1 
ATOM   166  C CH2 . TRP A 1 19  ? 34.098  -12.154 7.072   1.00 40.83 ? 19  TRP A CH2 1 
ATOM   167  N N   . LEU A 1 20  ? 27.102  -9.613  4.679   1.00 30.27 ? 20  LEU A N   1 
ATOM   168  C CA  . LEU A 1 20  ? 25.907  -9.588  5.520   1.00 34.32 ? 20  LEU A CA  1 
ATOM   169  C C   . LEU A 1 20  ? 25.000  -10.778 5.252   1.00 32.14 ? 20  LEU A C   1 
ATOM   170  O O   . LEU A 1 20  ? 24.242  -11.195 6.133   1.00 33.47 ? 20  LEU A O   1 
ATOM   171  C CB  . LEU A 1 20  ? 25.144  -8.291  5.277   1.00 27.90 ? 20  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 20  ? 25.730  -7.112  6.041   1.00 30.08 ? 20  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 20  ? 25.080  -5.818  5.561   1.00 27.26 ? 20  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 20  ? 25.609  -7.311  7.536   1.00 30.44 ? 20  LEU A CD2 1 
ATOM   175  N N   . ARG A 1 21  ? 25.054  -11.329 4.041   1.00 32.09 ? 21  ARG A N   1 
ATOM   176  C CA  . ARG A 1 21  ? 24.220  -12.483 3.720   1.00 37.09 ? 21  ARG A CA  1 
ATOM   177  C C   . ARG A 1 21  ? 24.488  -13.677 4.625   1.00 38.03 ? 21  ARG A C   1 
ATOM   178  O O   . ARG A 1 21  ? 23.597  -14.514 4.788   1.00 37.47 ? 21  ARG A O   1 
ATOM   179  C CB  . ARG A 1 21  ? 24.430  -12.883 2.259   1.00 35.40 ? 21  ARG A CB  1 
ATOM   180  C CG  . ARG A 1 21  ? 23.238  -13.595 1.660   1.00 38.39 ? 21  ARG A CG  1 
ATOM   181  C CD  . ARG A 1 21  ? 23.140  -13.349 0.162   1.00 39.53 ? 21  ARG A CD  1 
ATOM   182  N NE  . ARG A 1 21  ? 24.367  -13.684 -0.557  1.00 41.23 ? 21  ARG A NE  1 
ATOM   183  C CZ  . ARG A 1 21  ? 24.579  -13.372 -1.828  1.00 45.75 ? 21  ARG A CZ  1 
ATOM   184  N NH1 . ARG A 1 21  ? 23.660  -12.734 -2.542  1.00 45.03 ? 21  ARG A NH1 1 
ATOM   185  N NH2 . ARG A 1 21  ? 25.749  -13.682 -2.391  1.00 38.95 ? 21  ARG A NH2 1 
ATOM   186  N N   . LYS A 1 22  ? 25.673  -13.753 5.251   1.00 36.71 ? 22  LYS A N   1 
ATOM   187  C CA  . LYS A 1 22  ? 26.021  -14.864 6.141   1.00 36.47 ? 22  LYS A CA  1 
ATOM   188  C C   . LYS A 1 22  ? 25.236  -14.861 7.445   1.00 39.76 ? 22  LYS A C   1 
ATOM   189  O O   . LYS A 1 22  ? 25.294  -15.853 8.177   1.00 42.18 ? 22  LYS A O   1 
ATOM   190  C CB  . LYS A 1 22  ? 27.523  -14.829 6.445   1.00 36.97 ? 22  LYS A CB  1 
ATOM   191  C CG  . LYS A 1 22  ? 28.396  -15.067 5.201   1.00 35.19 ? 22  LYS A CG  1 
ATOM   192  C CD  . LYS A 1 22  ? 29.745  -14.363 5.261   1.00 43.09 ? 22  LYS A CD  1 
ATOM   193  C CE  . LYS A 1 22  ? 30.465  -14.533 6.588   1.00 43.51 ? 22  LYS A CE  1 
ATOM   194  N NZ  . LYS A 1 22  ? 31.223  -15.831 6.654   1.00 54.31 ? 22  LYS A NZ  1 
ATOM   195  N N   . GLY A 1 23  ? 24.519  -13.783 7.764   1.00 38.51 ? 23  GLY A N   1 
ATOM   196  C CA  . GLY A 1 23  ? 23.753  -13.745 8.995   1.00 38.16 ? 23  GLY A CA  1 
ATOM   197  C C   . GLY A 1 23  ? 24.598  -13.652 10.238  1.00 39.56 ? 23  GLY A C   1 
ATOM   198  O O   . GLY A 1 23  ? 24.087  -13.869 11.337  1.00 35.66 ? 23  GLY A O   1 
ATOM   199  N N   . GLU A 1 24  ? 25.880  -13.306 10.093  1.00 36.68 ? 24  GLU A N   1 
ATOM   200  C CA  . GLU A 1 24  ? 26.814  -13.230 11.210  1.00 38.14 ? 24  GLU A CA  1 
ATOM   201  C C   . GLU A 1 24  ? 27.271  -11.797 11.512  1.00 37.61 ? 24  GLU A C   1 
ATOM   202  O O   . GLU A 1 24  ? 28.355  -11.601 12.070  1.00 37.28 ? 24  GLU A O   1 
ATOM   203  C CB  . GLU A 1 24  ? 28.010  -14.132 10.932  1.00 38.40 ? 24  GLU A CB  1 
ATOM   204  C CG  . GLU A 1 24  ? 27.617  -15.493 10.357  1.00 41.48 ? 24  GLU A CG  1 
ATOM   205  C CD  . GLU A 1 24  ? 28.819  -16.399 10.122  1.00 46.81 ? 24  GLU A CD  1 
ATOM   206  O OE1 . GLU A 1 24  ? 29.524  -16.211 9.109   1.00 47.10 ? 24  GLU A OE1 1 
ATOM   207  O OE2 . GLU A 1 24  ? 29.034  -17.327 10.928  1.00 55.53 ? 24  GLU A OE2 1 
ATOM   208  N N   . GLY A 1 25  ? 26.482  -10.789 11.131  1.00 37.80 ? 25  GLY A N   1 
ATOM   209  C CA  . GLY A 1 25  ? 26.798  -9.418  11.473  1.00 30.92 ? 25  GLY A CA  1 
ATOM   210  C C   . GLY A 1 25  ? 27.777  -8.783  10.502  1.00 34.02 ? 25  GLY A C   1 
ATOM   211  O O   . GLY A 1 25  ? 28.147  -9.356  9.476   1.00 32.14 ? 25  GLY A O   1 
ATOM   212  N N   . LEU A 1 26  ? 28.202  -7.550  10.850  1.00 31.03 ? 26  LEU A N   1 
ATOM   213  C CA  . LEU A 1 26  ? 29.107  -6.754  10.026  1.00 33.68 ? 26  LEU A CA  1 
ATOM   214  C C   . LEU A 1 26  ? 30.558  -7.246  10.135  1.00 34.08 ? 26  LEU A C   1 
ATOM   215  O O   . LEU A 1 26  ? 30.977  -7.750  11.181  1.00 33.83 ? 26  LEU A O   1 
ATOM   216  C CB  . LEU A 1 26  ? 29.037  -5.290  10.445  1.00 32.44 ? 26  LEU A CB  1 
ATOM   217  C CG  . LEU A 1 26  ? 27.724  -4.527  10.181  1.00 34.40 ? 26  LEU A CG  1 
ATOM   218  C CD1 . LEU A 1 26  ? 27.691  -3.192  10.944  1.00 34.01 ? 26  LEU A CD1 1 
ATOM   219  C CD2 . LEU A 1 26  ? 27.536  -4.280  8.675   1.00 28.94 ? 26  LEU A CD2 1 
ATOM   220  N N   . PRO A 1 27  ? 31.349  -7.074  9.080   1.00 31.72 ? 27  PRO A N   1 
ATOM   221  C CA  . PRO A 1 27  ? 32.770  -7.462  9.140   1.00 34.50 ? 27  PRO A CA  1 
ATOM   222  C C   . PRO A 1 27  ? 33.561  -6.521  10.039  1.00 37.92 ? 27  PRO A C   1 
ATOM   223  O O   . PRO A 1 27  ? 33.176  -5.370  10.278  1.00 33.17 ? 27  PRO A O   1 
ATOM   224  C CB  . PRO A 1 27  ? 33.251  -7.316  7.691   1.00 32.04 ? 27  PRO A CB  1 
ATOM   225  C CG  . PRO A 1 27  ? 32.028  -7.161  6.855   1.00 39.15 ? 27  PRO A CG  1 
ATOM   226  C CD  . PRO A 1 27  ? 30.965  -6.559  7.753   1.00 33.66 ? 27  PRO A CD  1 
ATOM   227  N N   . ASN A 1 28  ? 34.719  -7.012  10.496  1.00 34.74 ? 28  ASN A N   1 
ATOM   228  C CA  . ASN A 1 28  ? 35.571  -6.224  11.378  1.00 32.11 ? 28  ASN A CA  1 
ATOM   229  C C   . ASN A 1 28  ? 36.248  -5.085  10.627  1.00 32.28 ? 28  ASN A C   1 
ATOM   230  O O   . ASN A 1 28  ? 36.674  -4.104  11.246  1.00 31.59 ? 28  ASN A O   1 
ATOM   231  C CB  . ASN A 1 28  ? 36.616  -7.133  12.036  1.00 35.25 ? 28  ASN A CB  1 
ATOM   232  C CG  . ASN A 1 28  ? 36.015  -8.017  13.112  1.00 43.18 ? 28  ASN A CG  1 
ATOM   233  O OD1 . ASN A 1 28  ? 34.970  -7.697  13.678  1.00 44.88 ? 28  ASN A OD1 1 
ATOM   234  N ND2 . ASN A 1 28  ? 36.661  -9.138  13.389  1.00 40.19 ? 28  ASN A ND2 1 
ATOM   235  N N   . TYR A 1 29  ? 36.332  -5.187  9.310   1.00 28.40 ? 29  TYR A N   1 
ATOM   236  C CA  . TYR A 1 29  ? 36.893  -4.122  8.498   1.00 31.64 ? 29  TYR A CA  1 
ATOM   237  C C   . TYR A 1 29  ? 36.423  -4.350  7.075   1.00 31.39 ? 29  TYR A C   1 
ATOM   238  O O   . TYR A 1 29  ? 35.843  -5.390  6.755   1.00 32.66 ? 29  TYR A O   1 
ATOM   239  C CB  . TYR A 1 29  ? 38.429  -4.067  8.597   1.00 34.05 ? 29  TYR A CB  1 
ATOM   240  C CG  . TYR A 1 29  ? 39.089  -5.378  8.227   1.00 35.10 ? 29  TYR A CG  1 
ATOM   241  C CD1 . TYR A 1 29  ? 39.296  -5.725  6.901   1.00 34.03 ? 29  TYR A CD1 1 
ATOM   242  C CD2 . TYR A 1 29  ? 39.468  -6.286  9.213   1.00 36.72 ? 29  TYR A CD2 1 
ATOM   243  C CE1 . TYR A 1 29  ? 39.866  -6.956  6.560   1.00 41.57 ? 29  TYR A CE1 1 
ATOM   244  C CE2 . TYR A 1 29  ? 40.054  -7.512  8.881   1.00 43.89 ? 29  TYR A CE2 1 
ATOM   245  C CZ  . TYR A 1 29  ? 40.251  -7.837  7.558   1.00 43.41 ? 29  TYR A CZ  1 
ATOM   246  O OH  . TYR A 1 29  ? 40.827  -9.049  7.233   1.00 49.99 ? 29  TYR A OH  1 
ATOM   247  N N   . LEU A 1 30  ? 36.676  -3.353  6.231   1.00 27.58 ? 30  LEU A N   1 
ATOM   248  C CA  . LEU A 1 30  ? 36.400  -3.397  4.799   1.00 29.79 ? 30  LEU A CA  1 
ATOM   249  C C   . LEU A 1 30  ? 37.643  -2.906  4.073   1.00 30.78 ? 30  LEU A C   1 
ATOM   250  O O   . LEU A 1 30  ? 38.113  -1.796  4.351   1.00 27.35 ? 30  LEU A O   1 
ATOM   251  C CB  . LEU A 1 30  ? 35.199  -2.519  4.419   1.00 29.22 ? 30  LEU A CB  1 
ATOM   252  C CG  . LEU A 1 30  ? 34.811  -2.448  2.924   1.00 28.30 ? 30  LEU A CG  1 
ATOM   253  C CD1 . LEU A 1 30  ? 34.246  -3.795  2.422   1.00 27.64 ? 30  LEU A CD1 1 
ATOM   254  C CD2 . LEU A 1 30  ? 33.800  -1.288  2.644   1.00 28.85 ? 30  LEU A CD2 1 
ATOM   255  N N   . ILE A 1 31  ? 38.179  -3.737  3.159   1.00 29.74 ? 31  ILE A N   1 
ATOM   256  C CA  . ILE A 1 31  ? 39.338  -3.370  2.345   1.00 29.84 ? 31  ILE A CA  1 
ATOM   257  C C   . ILE A 1 31  ? 38.880  -2.472  1.212   1.00 30.14 ? 31  ILE A C   1 
ATOM   258  O O   . ILE A 1 31  ? 38.009  -2.857  0.418   1.00 30.51 ? 31  ILE A O   1 
ATOM   259  C CB  . ILE A 1 31  ? 40.034  -4.610  1.746   1.00 34.55 ? 31  ILE A CB  1 
ATOM   260  C CG1 . ILE A 1 31  ? 40.490  -5.632  2.775   1.00 36.99 ? 31  ILE A CG1 1 
ATOM   261  C CG2 . ILE A 1 31  ? 41.260  -4.170  0.970   1.00 33.07 ? 31  ILE A CG2 1 
ATOM   262  C CD1 . ILE A 1 31  ? 40.899  -5.028  4.049   1.00 38.35 ? 31  ILE A CD1 1 
ATOM   263  N N   . MET A 1 32  ? 39.546  -1.328  1.061   1.00 28.60 ? 32  MET A N   1 
ATOM   264  C CA  . MET A 1 32  ? 39.255  -0.390  -0.013  1.00 30.99 ? 32  MET A CA  1 
ATOM   265  C C   . MET A 1 32  ? 40.574  0.189   -0.540  1.00 28.65 ? 32  MET A C   1 
ATOM   266  O O   . MET A 1 32  ? 41.572  0.221   0.178   1.00 32.00 ? 32  MET A O   1 
ATOM   267  C CB  . MET A 1 32  ? 38.354  0.736   0.513   1.00 27.94 ? 32  MET A CB  1 
ATOM   268  C CG  . MET A 1 32  ? 36.971  0.272   1.001   1.00 25.79 ? 32  MET A CG  1 
ATOM   269  S SD  . MET A 1 32  ? 35.867  -0.052  -0.354  1.00 28.79 ? 32  MET A SD  1 
ATOM   270  C CE  . MET A 1 32  ? 35.214  1.611   -0.586  1.00 27.81 ? 32  MET A CE  1 
ATOM   271  N N   . TYR A 1 33  ? 40.572  0.633   -1.792  1.00 29.41 ? 33  TYR A N   1 
ATOM   272  C CA  . TYR A 1 33  ? 41.765  1.234   -2.449  1.00 33.43 ? 33  TYR A CA  1 
ATOM   273  C C   . TYR A 1 33  ? 41.442  2.656   -2.919  1.00 32.72 ? 33  TYR A C   1 
ATOM   274  O O   . TYR A 1 33  ? 40.486  2.833   -3.645  1.00 34.95 ? 33  TYR A O   1 
ATOM   275  C CB  . TYR A 1 33  ? 42.231  0.363   -3.617  1.00 31.81 ? 33  TYR A CB  1 
ATOM   276  C CG  . TYR A 1 33  ? 42.365  -1.076  -3.233  1.00 32.83 ? 33  TYR A CG  1 
ATOM   277  C CD1 . TYR A 1 33  ? 41.264  -1.903  -3.214  1.00 33.45 ? 33  TYR A CD1 1 
ATOM   278  C CD2 . TYR A 1 33  ? 43.573  -1.587  -2.811  1.00 33.30 ? 33  TYR A CD2 1 
ATOM   279  C CE1 . TYR A 1 33  ? 41.371  -3.216  -2.804  1.00 36.10 ? 33  TYR A CE1 1 
ATOM   280  C CE2 . TYR A 1 33  ? 43.702  -2.894  -2.398  1.00 31.93 ? 33  TYR A CE2 1 
ATOM   281  C CZ  . TYR A 1 33  ? 42.594  -3.710  -2.399  1.00 34.37 ? 33  TYR A CZ  1 
ATOM   282  O OH  . TYR A 1 33  ? 42.696  -4.991  -1.989  1.00 34.94 ? 33  TYR A OH  1 
ATOM   283  N N   . ASP A 1 34  ? 42.272  3.623   -2.538  1.00 31.83 ? 34  ASP A N   1 
ATOM   284  C CA  . ASP A 1 34  ? 42.036  5.042   -2.898  1.00 34.80 ? 34  ASP A CA  1 
ATOM   285  C C   . ASP A 1 34  ? 42.214  5.256   -4.394  1.00 34.97 ? 34  ASP A C   1 
ATOM   286  O O   . ASP A 1 34  ? 42.979  4.547   -5.005  1.00 36.40 ? 34  ASP A O   1 
ATOM   287  C CB  . ASP A 1 34  ? 42.865  5.988   -2.043  1.00 38.91 ? 34  ASP A CB  1 
ATOM   288  C CG  . ASP A 1 34  ? 44.278  6.153   -2.529  1.00 42.94 ? 34  ASP A CG  1 
ATOM   289  O OD1 . ASP A 1 34  ? 44.489  7.024   -3.327  1.00 41.46 ? 34  ASP A OD1 1 
ATOM   290  O OD2 . ASP A 1 34  ? 45.116  5.411   -2.094  1.00 39.65 ? 34  ASP A OD2 1 
ATOM   291  N N   . MET A 1 35  ? 41.506  6.231   -4.941  1.00 30.95 ? 35  MET A N   1 
ATOM   292  C CA  . MET A 1 35  ? 41.554  6.446   -6.400  1.00 37.64 ? 35  MET A CA  1 
ATOM   293  C C   . MET A 1 35  ? 42.816  7.221   -6.793  1.00 35.66 ? 35  MET A C   1 
ATOM   294  O O   . MET A 1 35  ? 43.031  7.320   -7.982  1.00 37.75 ? 35  MET A O   1 
ATOM   295  C CB  . MET A 1 35  ? 40.309  7.185   -6.906  1.00 32.90 ? 35  MET A CB  1 
ATOM   296  C CG  . MET A 1 35  ? 40.068  8.523   -6.260  1.00 36.73 ? 35  MET A CG  1 
ATOM   297  S SD  . MET A 1 35  ? 38.533  9.368   -6.743  1.00 42.24 ? 35  MET A SD  1 
ATOM   298  C CE  . MET A 1 35  ? 38.630  9.297   -8.523  1.00 42.74 ? 35  MET A CE  1 
ATOM   299  N N   . ASP A 1 36  ? 43.608  7.689   -5.825  1.00 40.60 ? 36  ASP A N   1 
ATOM   300  C CA  . ASP A 1 36  ? 44.785  8.528   -6.153  1.00 42.74 ? 36  ASP A CA  1 
ATOM   301  C C   . ASP A 1 36  ? 46.067  7.698   -6.171  1.00 45.85 ? 36  ASP A C   1 
ATOM   302  O O   . ASP A 1 36  ? 46.697  7.652   -7.215  1.00 51.64 ? 36  ASP A O   1 
ATOM   303  C CB  . ASP A 1 36  ? 44.862  9.737   -5.229  1.00 43.90 ? 36  ASP A CB  1 
ATOM   304  C CG  . ASP A 1 36  ? 43.668  10.645  -5.403  1.00 45.54 ? 36  ASP A CG  1 
ATOM   305  O OD1 . ASP A 1 36  ? 43.356  10.942  -6.540  1.00 45.30 ? 36  ASP A OD1 1 
ATOM   306  O OD2 . ASP A 1 36  ? 43.051  10.991  -4.402  1.00 41.85 ? 36  ASP A OD2 1 
ATOM   307  N N   . ARG A 1 37  ? 46.425  7.078   -5.055  1.00 50.64 ? 37  ARG A N   1 
ATOM   308  C CA  . ARG A 1 37  ? 47.666  6.275   -4.991  1.00 47.36 ? 37  ARG A CA  1 
ATOM   309  C C   . ARG A 1 37  ? 47.351  4.783   -5.077  1.00 44.55 ? 37  ARG A C   1 
ATOM   310  O O   . ARG A 1 37  ? 48.291  4.013   -4.931  1.00 35.62 ? 37  ARG A O   1 
ATOM   311  C CB  . ARG A 1 37  ? 48.360  6.476   -3.647  1.00 52.05 ? 37  ARG A CB  1 
ATOM   312  C CG  . ARG A 1 37  ? 48.411  7.920   -3.181  1.00 60.17 ? 37  ARG A CG  1 
ATOM   313  C CD  . ARG A 1 37  ? 49.602  8.203   -2.289  1.00 54.56 ? 37  ARG A CD  1 
ATOM   314  N NE  . ARG A 1 37  ? 50.839  8.406   -3.041  1.00 61.65 ? 37  ARG A NE  1 
ATOM   315  C CZ  . ARG A 1 37  ? 52.058  8.254   -2.543  1.00 61.01 ? 37  ARG A CZ  1 
ATOM   316  N NH1 . ARG A 1 37  ? 53.120  8.455   -3.308  1.00 59.57 ? 37  ARG A NH1 1 
ATOM   317  N NH2 . ARG A 1 37  ? 52.209  7.897   -1.284  1.00 65.17 ? 37  ARG A NH2 1 
ATOM   318  N N   . ASN A 1 38  ? 46.072  4.417   -5.196  1.00 39.63 ? 38  ASN A N   1 
ATOM   319  C CA  . ASN A 1 38  ? 45.681  3.056   -5.308  1.00 39.18 ? 38  ASN A CA  1 
ATOM   320  C C   . ASN A 1 38  ? 46.207  2.257   -4.134  1.00 37.82 ? 38  ASN A C   1 
ATOM   321  O O   . ASN A 1 38  ? 46.524  1.080   -4.299  1.00 38.43 ? 38  ASN A O   1 
ATOM   322  C CB  . ASN A 1 38  ? 46.091  2.460   -6.639  1.00 40.96 ? 38  ASN A CB  1 
ATOM   323  C CG  . ASN A 1 38  ? 45.610  3.287   -7.830  1.00 45.17 ? 38  ASN A CG  1 
ATOM   324  O OD1 . ASN A 1 38  ? 44.468  3.149   -8.262  1.00 46.38 ? 38  ASN A OD1 1 
ATOM   325  N ND2 . ASN A 1 38  ? 46.471  4.176   -8.342  1.00 46.74 ? 38  ASN A ND2 1 
ATOM   326  N N   . LYS A 1 39  ? 46.311  2.883   -2.959  1.00 35.96 ? 39  LYS A N   1 
ATOM   327  C CA  . LYS A 1 39  ? 46.837  2.244   -1.766  1.00 35.00 ? 39  LYS A CA  1 
ATOM   328  C C   . LYS A 1 39  ? 45.710  1.494   -1.046  1.00 37.53 ? 39  LYS A C   1 
ATOM   329  O O   . LYS A 1 39  ? 44.533  1.861   -1.135  1.00 38.05 ? 39  LYS A O   1 
ATOM   330  C CB  . LYS A 1 39  ? 47.455  3.304   -0.856  1.00 36.21 ? 39  LYS A CB  1 
ATOM   331  C CG  . LYS A 1 39  ? 48.009  2.760   0.441   1.00 45.20 ? 39  LYS A CG  1 
ATOM   332  C CD  . LYS A 1 39  ? 48.793  3.802   1.265   1.00 49.58 ? 39  LYS A CD  1 
ATOM   333  C CE  . LYS A 1 39  ? 48.768  3.422   2.767   1.00 47.51 ? 39  LYS A CE  1 
ATOM   334  N NZ  . LYS A 1 39  ? 48.318  4.542   3.658   1.00 53.89 ? 39  LYS A NZ  1 
ATOM   335  N N   . GLU A 1 40  ? 46.072  0.390   -0.409  1.00 33.97 ? 40  GLU A N   1 
ATOM   336  C CA  . GLU A 1 40  ? 45.115  -0.447  0.305   1.00 37.05 ? 40  GLU A CA  1 
ATOM   337  C C   . GLU A 1 40  ? 44.870  0.041   1.734   1.00 37.30 ? 40  GLU A C   1 
ATOM   338  O O   . GLU A 1 40  ? 45.818  0.253   2.488   1.00 34.16 ? 40  GLU A O   1 
ATOM   339  C CB  . GLU A 1 40  ? 45.615  -1.887  0.327   1.00 33.30 ? 40  GLU A CB  1 
ATOM   340  C CG  . GLU A 1 40  ? 44.671  -2.860  0.983   1.00 34.30 ? 40  GLU A CG  1 
ATOM   341  C CD  . GLU A 1 40  ? 45.199  -4.299  0.926   1.00 36.92 ? 40  GLU A CD  1 
ATOM   342  O OE1 . GLU A 1 40  ? 44.995  -4.981  -0.101  1.00 33.27 ? 40  GLU A OE1 1 
ATOM   343  O OE2 . GLU A 1 40  ? 45.824  -4.733  1.913   1.00 38.52 ? 40  GLU A OE2 1 
ATOM   344  N N   . TYR A 1 41  ? 43.592  0.181   2.114   1.00 35.46 ? 41  TYR A N   1 
ATOM   345  C CA  . TYR A 1 41  ? 43.178  0.536   3.462   1.00 32.45 ? 41  TYR A CA  1 
ATOM   346  C C   . TYR A 1 41  ? 42.192  -0.455  4.039   1.00 30.70 ? 41  TYR A C   1 
ATOM   347  O O   . TYR A 1 41  ? 41.246  -0.895  3.333   1.00 32.75 ? 41  TYR A O   1 
ATOM   348  C CB  . TYR A 1 41  ? 42.524  1.950   3.451   1.00 35.48 ? 41  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 41  ? 43.417  3.097   2.923   1.00 34.39 ? 41  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 41  ? 43.524  3.339   1.548   1.00 35.37 ? 41  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 41  ? 44.132  3.912   3.776   1.00 39.74 ? 41  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 41  ? 44.328  4.366   1.063   1.00 39.41 ? 41  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 41  ? 44.938  4.922   3.297   1.00 40.94 ? 41  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 41  ? 45.027  5.125   1.951   1.00 40.78 ? 41  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 41  ? 45.829  6.109   1.527   1.00 48.66 ? 41  TYR A OH  1 
ATOM   356  N N   . LYS A 1 42  ? 42.352  -0.703  5.326   1.00 28.17 ? 42  LYS A N   1 
ATOM   357  C CA  . LYS A 1 42  ? 41.437  -1.539  6.123   1.00 36.49 ? 42  LYS A CA  1 
ATOM   358  C C   . LYS A 1 42  ? 40.614  -0.588  6.995   1.00 30.68 ? 42  LYS A C   1 
ATOM   359  O O   . LYS A 1 42  ? 41.059  -0.272  8.078   1.00 34.12 ? 42  LYS A O   1 
ATOM   360  C CB  . LYS A 1 42  ? 42.234  -2.477  7.024   1.00 40.17 ? 42  LYS A CB  1 
ATOM   361  C CG  . LYS A 1 42  ? 42.739  -3.728  6.338   1.00 43.45 ? 42  LYS A CG  1 
ATOM   362  C CD  . LYS A 1 42  ? 43.212  -4.795  7.285   1.00 49.89 ? 42  LYS A CD  1 
ATOM   363  C CE  . LYS A 1 42  ? 43.336  -6.115  6.562   1.00 46.52 ? 42  LYS A CE  1 
ATOM   364  N NZ  . LYS A 1 42  ? 44.158  -7.095  7.303   1.00 55.25 ? 42  LYS A NZ  1 
ATOM   365  N N   . LEU A 1 43  ? 39.487  -0.120  6.473   1.00 33.83 ? 43  LEU A N   1 
ATOM   366  C CA  . LEU A 1 43  ? 38.601  0.781   7.171   1.00 30.30 ? 43  LEU A CA  1 
ATOM   367  C C   . LEU A 1 43  ? 37.901  -0.022  8.266   1.00 31.90 ? 43  LEU A C   1 
ATOM   368  O O   . LEU A 1 43  ? 37.296  -1.075  8.010   1.00 32.50 ? 43  LEU A O   1 
ATOM   369  C CB  . LEU A 1 43  ? 37.562  1.357   6.211   1.00 27.75 ? 43  LEU A CB  1 
ATOM   370  C CG  . LEU A 1 43  ? 38.154  1.981   4.958   1.00 30.06 ? 43  LEU A CG  1 
ATOM   371  C CD1 . LEU A 1 43  ? 37.045  2.449   4.033   1.00 31.20 ? 43  LEU A CD1 1 
ATOM   372  C CD2 . LEU A 1 43  ? 39.108  3.110   5.320   1.00 34.66 ? 43  LEU A CD2 1 
ATOM   373  N N   . VAL A 1 44  ? 37.999  0.463   9.502   1.00 30.33 ? 44  VAL A N   1 
ATOM   374  C CA  . VAL A 1 44  ? 37.267  -0.123  10.616  1.00 32.22 ? 44  VAL A CA  1 
ATOM   375  C C   . VAL A 1 44  ? 35.790  0.265   10.501  1.00 32.17 ? 44  VAL A C   1 
ATOM   376  O O   . VAL A 1 44  ? 35.447  1.130   9.681   1.00 27.95 ? 44  VAL A O   1 
ATOM   377  C CB  . VAL A 1 44  ? 37.890  0.308   11.953  1.00 30.43 ? 44  VAL A CB  1 
ATOM   378  C CG1 . VAL A 1 44  ? 39.350  -0.088  11.979  1.00 29.97 ? 44  VAL A CG1 1 
ATOM   379  C CG2 . VAL A 1 44  ? 37.720  1.792   12.188  1.00 34.16 ? 44  VAL A CG2 1 
ATOM   380  N N   . PRO A 1 45  ? 34.875  -0.393  11.242  1.00 31.10 ? 45  PRO A N   1 
ATOM   381  C CA  . PRO A 1 45  ? 33.437  -0.173  10.996  1.00 30.74 ? 45  PRO A CA  1 
ATOM   382  C C   . PRO A 1 45  ? 32.992  1.276   11.054  1.00 29.43 ? 45  PRO A C   1 
ATOM   383  O O   . PRO A 1 45  ? 32.257  1.732   10.164  1.00 31.71 ? 45  PRO A O   1 
ATOM   384  C CB  . PRO A 1 45  ? 32.786  -1.001  12.101  1.00 33.93 ? 45  PRO A CB  1 
ATOM   385  C CG  . PRO A 1 45  ? 33.763  -2.162  12.314  1.00 31.18 ? 45  PRO A CG  1 
ATOM   386  C CD  . PRO A 1 45  ? 35.113  -1.667  11.944  1.00 31.51 ? 45  PRO A CD  1 
ATOM   387  N N   . LYS A 1 46  ? 33.427  2.032   12.058  1.00 31.16 ? 46  LYS A N   1 
ATOM   388  C CA  . LYS A 1 46  ? 33.026  3.434   12.063  1.00 31.66 ? 46  LYS A CA  1 
ATOM   389  C C   . LYS A 1 46  ? 33.522  4.181   10.837  1.00 31.84 ? 46  LYS A C   1 
ATOM   390  O O   . LYS A 1 46  ? 32.914  5.182   10.430  1.00 30.36 ? 46  LYS A O   1 
ATOM   391  C CB  . LYS A 1 46  ? 33.475  4.191   13.305  1.00 30.45 ? 46  LYS A CB  1 
ATOM   392  C CG  . LYS A 1 46  ? 34.895  4.796   13.339  1.00 37.10 ? 46  LYS A CG  1 
ATOM   393  C CD  . LYS A 1 46  ? 35.327  4.962   14.813  1.00 39.61 ? 46  LYS A CD  1 
ATOM   394  C CE  . LYS A 1 46  ? 36.815  4.993   15.263  1.00 46.30 ? 46  LYS A CE  1 
ATOM   395  N NZ  . LYS A 1 46  ? 37.736  3.807   15.193  1.00 55.53 ? 46  LYS A NZ  1 
ATOM   396  N N   . GLU A 1 47  ? 34.617  3.730   10.232  1.00 27.83 ? 47  GLU A N   1 
ATOM   397  C CA  . GLU A 1 47  ? 35.110  4.421   9.055   1.00 27.32 ? 47  GLU A CA  1 
ATOM   398  C C   . GLU A 1 47  ? 34.330  4.038   7.815   1.00 25.95 ? 47  GLU A C   1 
ATOM   399  O O   . GLU A 1 47  ? 34.028  4.900   6.982   1.00 25.81 ? 47  GLU A O   1 
ATOM   400  C CB  . GLU A 1 47  ? 36.589  4.107   8.837   1.00 30.25 ? 47  GLU A CB  1 
ATOM   401  C CG  . GLU A 1 47  ? 37.500  4.515   9.949   1.00 30.84 ? 47  GLU A CG  1 
ATOM   402  C CD  . GLU A 1 47  ? 38.935  4.198   9.593   1.00 35.79 ? 47  GLU A CD  1 
ATOM   403  O OE1 . GLU A 1 47  ? 39.191  3.041   9.202   1.00 33.79 ? 47  GLU A OE1 1 
ATOM   404  O OE2 . GLU A 1 47  ? 39.790  5.099   9.661   1.00 41.01 ? 47  GLU A OE2 1 
ATOM   405  N N   . TYR A 1 48  ? 34.061  2.745   7.618   1.00 25.08 ? 48  TYR A N   1 
ATOM   406  C CA  . TYR A 1 48  ? 33.313  2.409   6.417   1.00 23.10 ? 48  TYR A CA  1 
ATOM   407  C C   . TYR A 1 48  ? 31.860  2.859   6.543   1.00 24.77 ? 48  TYR A C   1 
ATOM   408  O O   . TYR A 1 48  ? 31.235  3.195   5.530   1.00 24.89 ? 48  TYR A O   1 
ATOM   409  C CB  . TYR A 1 48  ? 33.462  0.919   6.064   1.00 24.98 ? 48  TYR A CB  1 
ATOM   410  C CG  . TYR A 1 48  ? 32.930  -0.190  7.007   1.00 29.16 ? 48  TYR A CG  1 
ATOM   411  C CD1 . TYR A 1 48  ? 31.601  -0.259  7.400   1.00 27.16 ? 48  TYR A CD1 1 
ATOM   412  C CD2 . TYR A 1 48  ? 33.773  -1.217  7.415   1.00 28.30 ? 48  TYR A CD2 1 
ATOM   413  C CE1 . TYR A 1 48  ? 31.138  -1.300  8.228   1.00 28.79 ? 48  TYR A CE1 1 
ATOM   414  C CE2 . TYR A 1 48  ? 33.338  -2.250  8.210   1.00 29.13 ? 48  TYR A CE2 1 
ATOM   415  C CZ  . TYR A 1 48  ? 32.010  -2.290  8.627   1.00 32.10 ? 48  TYR A CZ  1 
ATOM   416  O OH  . TYR A 1 48  ? 31.569  -3.324  9.423   1.00 29.72 ? 48  TYR A OH  1 
ATOM   417  N N   . ALA A 1 49  ? 31.313  2.886   7.758   1.00 23.92 ? 49  ALA A N   1 
ATOM   418  C CA  . ALA A 1 49  ? 29.976  3.477   7.941   1.00 27.47 ? 49  ALA A CA  1 
ATOM   419  C C   . ALA A 1 49  ? 29.974  4.975   7.641   1.00 25.48 ? 49  ALA A C   1 
ATOM   420  O O   . ALA A 1 49  ? 29.035  5.496   7.019   1.00 26.08 ? 49  ALA A O   1 
ATOM   421  C CB  . ALA A 1 49  ? 29.462  3.239   9.363   1.00 26.87 ? 49  ALA A CB  1 
ATOM   422  N N   . GLY A 1 50  ? 31.001  5.697   8.107   1.00 25.21 ? 50  GLY A N   1 
ATOM   423  C CA  . GLY A 1 50  ? 31.084  7.111   7.794   1.00 27.60 ? 50  GLY A CA  1 
ATOM   424  C C   . GLY A 1 50  ? 31.215  7.358   6.304   1.00 28.53 ? 50  GLY A C   1 
ATOM   425  O O   . GLY A 1 50  ? 30.618  8.289   5.766   1.00 25.31 ? 50  GLY A O   1 
ATOM   426  N N   . LEU A 1 51  ? 32.012  6.534   5.616   1.00 26.52 ? 51  LEU A N   1 
ATOM   427  C CA  . LEU A 1 51  ? 32.214  6.704   4.175   1.00 24.48 ? 51  LEU A CA  1 
ATOM   428  C C   . LEU A 1 51  ? 30.915  6.534   3.398   1.00 24.58 ? 51  LEU A C   1 
ATOM   429  O O   . LEU A 1 51  ? 30.628  7.292   2.462   1.00 26.18 ? 51  LEU A O   1 
ATOM   430  C CB  . LEU A 1 51  ? 33.259  5.690   3.680   1.00 24.46 ? 51  LEU A CB  1 
ATOM   431  C CG  . LEU A 1 51  ? 33.677  5.822   2.217   1.00 26.31 ? 51  LEU A CG  1 
ATOM   432  C CD1 . LEU A 1 51  ? 34.423  7.099   1.991   1.00 27.06 ? 51  LEU A CD1 1 
ATOM   433  C CD2 . LEU A 1 51  ? 34.566  4.611   1.797   1.00 25.01 ? 51  LEU A CD2 1 
ATOM   434  N N   . TYR A 1 52  ? 30.165  5.471   3.705   1.00 24.98 ? 52  TYR A N   1 
ATOM   435  C CA  . TYR A 1 52  ? 28.935  5.197   2.974   1.00 24.67 ? 52  TYR A CA  1 
ATOM   436  C C   . TYR A 1 52  ? 27.792  6.095   3.426   1.00 21.58 ? 52  TYR A C   1 
ATOM   437  O O   . TYR A 1 52  ? 26.931  6.434   2.609   1.00 22.27 ? 52  TYR A O   1 
ATOM   438  C CB  . TYR A 1 52  ? 28.592  3.698   3.090   1.00 24.59 ? 52  TYR A CB  1 
ATOM   439  C CG  . TYR A 1 52  ? 29.443  2.879   2.122   1.00 25.99 ? 52  TYR A CG  1 
ATOM   440  C CD1 . TYR A 1 52  ? 29.078  2.769   0.793   1.00 25.62 ? 52  TYR A CD1 1 
ATOM   441  C CD2 . TYR A 1 52  ? 30.647  2.319   2.517   1.00 25.47 ? 52  TYR A CD2 1 
ATOM   442  C CE1 . TYR A 1 52  ? 29.870  2.090   -0.114  1.00 27.63 ? 52  TYR A CE1 1 
ATOM   443  C CE2 . TYR A 1 52  ? 31.461  1.616   1.612   1.00 24.32 ? 52  TYR A CE2 1 
ATOM   444  C CZ  . TYR A 1 52  ? 31.061  1.505   0.298   1.00 27.97 ? 52  TYR A CZ  1 
ATOM   445  O OH  . TYR A 1 52  ? 31.823  0.818   -0.636  1.00 26.44 ? 52  TYR A OH  1 
ATOM   446  N N   . GLU A 1 53  ? 27.803  6.549   4.679   1.00 21.06 ? 53  GLU A N   1 
ATOM   447  C CA  . GLU A 1 53  ? 26.860  7.600   5.081   1.00 27.97 ? 53  GLU A CA  1 
ATOM   448  C C   . GLU A 1 53  ? 27.022  8.839   4.201   1.00 25.07 ? 53  GLU A C   1 
ATOM   449  O O   . GLU A 1 53  ? 26.042  9.398   3.694   1.00 25.19 ? 53  GLU A O   1 
ATOM   450  C CB  . GLU A 1 53  ? 27.098  7.998   6.540   1.00 29.21 ? 53  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 53  ? 26.263  9.228   7.001   1.00 26.40 ? 53  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 53  ? 26.519  9.571   8.454   1.00 28.60 ? 53  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 53  ? 27.581  10.164  8.747   1.00 28.27 ? 53  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 53  ? 25.671  9.241   9.311   1.00 29.98 ? 53  GLU A OE2 1 
ATOM   455  N N   . SER A 1 54  ? 28.264  9.280   4.009   1.00 23.92 ? 54  SER A N   1 
ATOM   456  C CA  . SER A 1 54  ? 28.525  10.438  3.155   1.00 21.23 ? 54  SER A CA  1 
ATOM   457  C C   . SER A 1 54  ? 28.109  10.149  1.720   1.00 22.91 ? 54  SER A C   1 
ATOM   458  O O   . SER A 1 54  ? 27.521  10.999  1.051   1.00 24.87 ? 54  SER A O   1 
ATOM   459  C CB  . SER A 1 54  ? 30.010  10.800  3.240   1.00 25.28 ? 54  SER A CB  1 
ATOM   460  O OG  . SER A 1 54  ? 30.356  11.920  2.444   1.00 31.93 ? 54  SER A OG  1 
ATOM   461  N N   . ARG A 1 55  ? 28.409  8.946   1.225   1.00 25.69 ? 55  ARG A N   1 
ATOM   462  C CA  . ARG A 1 55  ? 27.949  8.561   -0.104  1.00 23.24 ? 55  ARG A CA  1 
ATOM   463  C C   . ARG A 1 55  ? 26.424  8.635   -0.214  1.00 23.93 ? 55  ARG A C   1 
ATOM   464  O O   . ARG A 1 55  ? 25.890  9.162   -1.199  1.00 23.90 ? 55  ARG A O   1 
ATOM   465  C CB  . ARG A 1 55  ? 28.463  7.151   -0.422  1.00 23.60 ? 55  ARG A CB  1 
ATOM   466  C CG  . ARG A 1 55  ? 28.128  6.668   -1.827  1.00 24.74 ? 55  ARG A CG  1 
ATOM   467  C CD  . ARG A 1 55  ? 28.119  5.125   -1.877  1.00 23.50 ? 55  ARG A CD  1 
ATOM   468  N NE  . ARG A 1 55  ? 27.944  4.610   -3.233  1.00 25.62 ? 55  ARG A NE  1 
ATOM   469  C CZ  . ARG A 1 55  ? 27.610  3.355   -3.512  1.00 29.01 ? 55  ARG A CZ  1 
ATOM   470  N NH1 . ARG A 1 55  ? 27.354  2.476   -2.554  1.00 26.66 ? 55  ARG A NH1 1 
ATOM   471  N NH2 . ARG A 1 55  ? 27.548  2.966   -4.785  1.00 29.25 ? 55  ARG A NH2 1 
ATOM   472  N N   . ASN A 1 56  ? 25.706  8.131   0.799   1.00 22.43 ? 56  ASN A N   1 
ATOM   473  C CA  . ASN A 1 56  ? 24.242  8.084   0.763   1.00 22.92 ? 56  ASN A CA  1 
ATOM   474  C C   . ASN A 1 56  ? 23.611  9.474   0.895   1.00 20.77 ? 56  ASN A C   1 
ATOM   475  O O   . ASN A 1 56  ? 22.581  9.746   0.268   1.00 23.64 ? 56  ASN A O   1 
ATOM   476  C CB  . ASN A 1 56  ? 23.729  7.171   1.869   1.00 22.24 ? 56  ASN A CB  1 
ATOM   477  C CG  . ASN A 1 56  ? 24.096  5.692   1.660   1.00 25.50 ? 56  ASN A CG  1 
ATOM   478  O OD1 . ASN A 1 56  ? 24.467  5.255   0.552   1.00 22.73 ? 56  ASN A OD1 1 
ATOM   479  N ND2 . ASN A 1 56  ? 23.964  4.917   2.726   1.00 22.90 ? 56  ASN A ND2 1 
ATOM   480  N N   . ILE A 1 57  ? 24.237  10.384  1.639   1.00 23.58 ? 57  ILE A N   1 
ATOM   481  C CA  . ILE A 1 57  ? 23.760  11.772  1.657   1.00 25.66 ? 57  ILE A CA  1 
ATOM   482  C C   . ILE A 1 57  ? 23.748  12.337  0.242   1.00 27.92 ? 57  ILE A C   1 
ATOM   483  O O   . ILE A 1 57  ? 22.736  12.879  -0.221  1.00 22.38 ? 57  ILE A O   1 
ATOM   484  C CB  . ILE A 1 57  ? 24.642  12.625  2.588   1.00 25.04 ? 57  ILE A CB  1 
ATOM   485  C CG1 . ILE A 1 57  ? 24.469  12.164  4.035   1.00 27.04 ? 57  ILE A CG1 1 
ATOM   486  C CG2 . ILE A 1 57  ? 24.329  14.113  2.428   1.00 23.85 ? 57  ILE A CG2 1 
ATOM   487  C CD1 . ILE A 1 57  ? 25.364  12.891  5.020   1.00 27.41 ? 57  ILE A CD1 1 
ATOM   488  N N   . PHE A 1 58  ? 24.877  12.208  -0.478  1.00 22.51 ? 58  PHE A N   1 
ATOM   489  C CA  . PHE A 1 58  ? 24.925  12.714  -1.843  1.00 25.30 ? 58  PHE A CA  1 
ATOM   490  C C   . PHE A 1 58  ? 23.888  12.034  -2.714  1.00 25.84 ? 58  PHE A C   1 
ATOM   491  O O   . PHE A 1 58  ? 23.184  12.689  -3.496  1.00 23.73 ? 58  PHE A O   1 
ATOM   492  C CB  . PHE A 1 58  ? 26.314  12.516  -2.459  1.00 26.45 ? 58  PHE A CB  1 
ATOM   493  C CG  . PHE A 1 58  ? 26.482  13.213  -3.781  1.00 28.98 ? 58  PHE A CG  1 
ATOM   494  C CD1 . PHE A 1 58  ? 25.920  12.687  -4.939  1.00 24.79 ? 58  PHE A CD1 1 
ATOM   495  C CD2 . PHE A 1 58  ? 27.194  14.405  -3.862  1.00 30.57 ? 58  PHE A CD2 1 
ATOM   496  C CE1 . PHE A 1 58  ? 26.087  13.336  -6.171  1.00 29.57 ? 58  PHE A CE1 1 
ATOM   497  C CE2 . PHE A 1 58  ? 27.358  15.064  -5.092  1.00 33.08 ? 58  PHE A CE2 1 
ATOM   498  C CZ  . PHE A 1 58  ? 26.801  14.529  -6.238  1.00 33.43 ? 58  PHE A CZ  1 
ATOM   499  N N   . TRP A 1 59  ? 23.824  10.707  -2.628  1.00 21.91 ? 59  TRP A N   1 
ATOM   500  C CA  . TRP A 1 59  ? 22.903  9.935   -3.450  1.00 25.12 ? 59  TRP A CA  1 
ATOM   501  C C   . TRP A 1 59  ? 21.452  10.318  -3.167  1.00 25.77 ? 59  TRP A C   1 
ATOM   502  O O   . TRP A 1 59  ? 20.643  10.457  -4.095  1.00 27.54 ? 59  TRP A O   1 
ATOM   503  C CB  . TRP A 1 59  ? 23.127  8.452   -3.185  1.00 26.50 ? 59  TRP A CB  1 
ATOM   504  C CG  . TRP A 1 59  ? 22.768  7.560   -4.335  1.00 28.51 ? 59  TRP A CG  1 
ATOM   505  C CD1 . TRP A 1 59  ? 21.974  7.866   -5.395  1.00 30.24 ? 59  TRP A CD1 1 
ATOM   506  C CD2 . TRP A 1 59  ? 23.214  6.221   -4.534  1.00 25.15 ? 59  TRP A CD2 1 
ATOM   507  N NE1 . TRP A 1 59  ? 21.894  6.787   -6.250  1.00 29.32 ? 59  TRP A NE1 1 
ATOM   508  C CE2 . TRP A 1 59  ? 22.645  5.764   -5.738  1.00 28.11 ? 59  TRP A CE2 1 
ATOM   509  C CE3 . TRP A 1 59  ? 24.036  5.359   -3.806  1.00 24.96 ? 59  TRP A CE3 1 
ATOM   510  C CZ2 . TRP A 1 59  ? 22.867  4.483   -6.232  1.00 26.67 ? 59  TRP A CZ2 1 
ATOM   511  C CZ3 . TRP A 1 59  ? 24.246  4.082   -4.292  1.00 27.83 ? 59  TRP A CZ3 1 
ATOM   512  C CH2 . TRP A 1 59  ? 23.659  3.660   -5.498  1.00 26.85 ? 59  TRP A CH2 1 
ATOM   513  N N   . ILE A 1 60  ? 21.113  10.458  -1.901  1.00 24.10 ? 60  ILE A N   1 
ATOM   514  C CA  . ILE A 1 60  ? 19.701  10.774  -1.555  1.00 21.57 ? 60  ILE A CA  1 
ATOM   515  C C   . ILE A 1 60  ? 19.333  12.192  -1.999  1.00 25.56 ? 60  ILE A C   1 
ATOM   516  O O   . ILE A 1 60  ? 18.311  12.323  -2.594  1.00 27.36 ? 60  ILE A O   1 
ATOM   517  C CB  . ILE A 1 60  ? 19.385  10.472  -0.076  1.00 22.65 ? 60  ILE A CB  1 
ATOM   518  C CG1 . ILE A 1 60  ? 19.355  8.968   0.182   1.00 24.30 ? 60  ILE A CG1 1 
ATOM   519  C CG2 . ILE A 1 60  ? 18.087  11.110  0.378   1.00 24.89 ? 60  ILE A CG2 1 
ATOM   520  C CD1 . ILE A 1 60  ? 19.596  8.608   1.614   1.00 22.35 ? 60  ILE A CD1 1 
ATOM   521  N N   . LYS A 1 61  ? 20.199  13.159  -1.769  1.00 26.65 ? 61  LYS A N   1 
ATOM   522  C CA  . LYS A 1 61  ? 19.870  14.564  -2.085  1.00 28.51 ? 61  LYS A CA  1 
ATOM   523  C C   . LYS A 1 61  ? 19.914  14.865  -3.584  1.00 29.95 ? 61  LYS A C   1 
ATOM   524  O O   . LYS A 1 61  ? 19.129  15.675  -4.016  1.00 27.67 ? 61  LYS A O   1 
ATOM   525  C CB  . LYS A 1 61  ? 20.811  15.453  -1.281  1.00 31.93 ? 61  LYS A CB  1 
ATOM   526  C CG  . LYS A 1 61  ? 20.574  15.342  0.214   1.00 36.19 ? 61  LYS A CG  1 
ATOM   527  C CD  . LYS A 1 61  ? 19.102  15.381  0.589   1.00 39.42 ? 61  LYS A CD  1 
ATOM   528  C CE  . LYS A 1 61  ? 18.570  16.776  0.827   1.00 38.46 ? 61  LYS A CE  1 
ATOM   529  N NZ  . LYS A 1 61  ? 17.228  16.790  1.449   1.00 27.47 ? 61  LYS A NZ  1 
ATOM   530  N N   . ASN A 1 62  ? 20.780  14.188  -4.327  1.00 26.58 ? 62  ASN A N   1 
ATOM   531  C CA  . ASN A 1 62  ? 21.007  14.497  -5.756  1.00 29.11 ? 62  ASN A CA  1 
ATOM   532  C C   . ASN A 1 62  ? 20.344  13.483  -6.683  1.00 29.86 ? 62  ASN A C   1 
ATOM   533  O O   . ASN A 1 62  ? 20.291  13.753  -7.841  1.00 33.46 ? 62  ASN A O   1 
ATOM   534  C CB  . ASN A 1 62  ? 22.497  14.646  -6.041  1.00 30.05 ? 62  ASN A CB  1 
ATOM   535  C CG  . ASN A 1 62  ? 23.098  15.795  -5.269  1.00 32.60 ? 62  ASN A CG  1 
ATOM   536  O OD1 . ASN A 1 62  ? 22.680  16.912  -5.449  1.00 34.02 ? 62  ASN A OD1 1 
ATOM   537  N ND2 . ASN A 1 62  ? 24.042  15.524  -4.394  1.00 30.16 ? 62  ASN A ND2 1 
ATOM   538  N N   . GLY A 1 63  ? 19.862  12.363  -6.172  1.00 29.28 ? 63  GLY A N   1 
ATOM   539  C CA  . GLY A 1 63  ? 19.250  11.388  -7.040  1.00 33.89 ? 63  GLY A CA  1 
ATOM   540  C C   . GLY A 1 63  ? 20.220  10.586  -7.874  1.00 33.90 ? 63  GLY A C   1 
ATOM   541  O O   . GLY A 1 63  ? 19.780  9.876   -8.790  1.00 36.80 ? 63  GLY A O   1 
ATOM   542  N N   . ARG A 1 64  ? 21.523  10.692  -7.607  1.00 33.89 ? 64  ARG A N   1 
ATOM   543  C CA  . ARG A 1 64  ? 22.536  9.921   -8.321  1.00 31.22 ? 64  ARG A CA  1 
ATOM   544  C C   . ARG A 1 64  ? 23.760  9.716   -7.428  1.00 31.78 ? 64  ARG A C   1 
ATOM   545  O O   . ARG A 1 64  ? 24.019  10.499  -6.506  1.00 30.68 ? 64  ARG A O   1 
ATOM   546  C CB  . ARG A 1 64  ? 22.968  10.612  -9.620  1.00 32.65 ? 64  ARG A CB  1 
ATOM   547  C CG  . ARG A 1 64  ? 23.454  12.039  -9.384  1.00 34.99 ? 64  ARG A CG  1 
ATOM   548  C CD  . ARG A 1 64  ? 23.624  12.800  -10.679 1.00 39.61 ? 64  ARG A CD  1 
ATOM   549  N NE  . ARG A 1 64  ? 24.326  14.058  -10.459 1.00 44.17 ? 64  ARG A NE  1 
ATOM   550  C CZ  . ARG A 1 64  ? 25.638  14.155  -10.286 1.00 48.64 ? 64  ARG A CZ  1 
ATOM   551  N NH1 . ARG A 1 64  ? 26.436  13.103  -10.430 1.00 48.07 ? 64  ARG A NH1 1 
ATOM   552  N NH2 . ARG A 1 64  ? 26.171  15.347  -10.024 1.00 50.20 ? 64  ARG A NH2 1 
ATOM   553  N N   . GLU A 1 65  ? 24.529  8.664   -7.735  1.00 31.13 ? 65  GLU A N   1 
ATOM   554  C CA  . GLU A 1 65  ? 25.781  8.367   -7.039  1.00 31.44 ? 65  GLU A CA  1 
ATOM   555  C C   . GLU A 1 65  ? 26.782  9.509   -7.166  1.00 31.60 ? 65  GLU A C   1 
ATOM   556  O O   . GLU A 1 65  ? 26.899  10.108  -8.241  1.00 35.57 ? 65  GLU A O   1 
ATOM   557  C CB  . GLU A 1 65  ? 26.465  7.146   -7.664  1.00 32.74 ? 65  GLU A CB  1 
ATOM   558  C CG  . GLU A 1 65  ? 25.688  5.916   -7.791  1.00 36.52 ? 65  GLU A CG  1 
ATOM   559  C CD  . GLU A 1 65  ? 26.603  4.707   -7.859  1.00 34.68 ? 65  GLU A CD  1 
ATOM   560  O OE1 . GLU A 1 65  ? 27.567  4.556   -7.064  1.00 29.31 ? 65  GLU A OE1 1 
ATOM   561  O OE2 . GLU A 1 65  ? 26.327  3.895   -8.754  1.00 42.10 ? 65  GLU A OE2 1 
ATOM   562  N N   . PRO A 1 66  ? 27.561  9.790   -6.119  1.00 31.66 ? 66  PRO A N   1 
ATOM   563  C CA  . PRO A 1 66  ? 28.719  10.686  -6.269  1.00 32.16 ? 66  PRO A CA  1 
ATOM   564  C C   . PRO A 1 66  ? 29.832  9.973   -7.019  1.00 33.44 ? 66  PRO A C   1 
ATOM   565  O O   . PRO A 1 66  ? 29.994  8.757   -6.905  1.00 30.11 ? 66  PRO A O   1 
ATOM   566  C CB  . PRO A 1 66  ? 29.138  10.982  -4.823  1.00 31.08 ? 66  PRO A CB  1 
ATOM   567  C CG  . PRO A 1 66  ? 28.589  9.839   -4.025  1.00 28.08 ? 66  PRO A CG  1 
ATOM   568  C CD  . PRO A 1 66  ? 27.344  9.375   -4.724  1.00 29.70 ? 66  PRO A CD  1 
ATOM   569  N N   . ASN A 1 67  ? 30.636  10.753  -7.757  1.00 35.45 ? 67  ASN A N   1 
ATOM   570  C CA  . ASN A 1 67  ? 31.748  10.174  -8.523  1.00 32.37 ? 67  ASN A CA  1 
ATOM   571  C C   . ASN A 1 67  ? 32.855  9.685   -7.613  1.00 32.90 ? 67  ASN A C   1 
ATOM   572  O O   . ASN A 1 67  ? 33.602  8.765   -7.967  1.00 28.98 ? 67  ASN A O   1 
ATOM   573  C CB  . ASN A 1 67  ? 32.292  11.203  -9.516  1.00 31.91 ? 67  ASN A CB  1 
ATOM   574  C CG  . ASN A 1 67  ? 31.377  11.374  -10.696 1.00 36.13 ? 67  ASN A CG  1 
ATOM   575  O OD1 . ASN A 1 67  ? 30.866  10.394  -11.226 1.00 37.29 ? 67  ASN A OD1 1 
ATOM   576  N ND2 . ASN A 1 67  ? 31.167  12.613  -11.125 1.00 43.03 ? 67  ASN A ND2 1 
ATOM   577  N N   . TYR A 1 68  ? 32.962  10.273  -6.431  1.00 30.96 ? 68  TYR A N   1 
ATOM   578  C CA  . TYR A 1 68  ? 33.902  9.818   -5.420  1.00 30.23 ? 68  TYR A CA  1 
ATOM   579  C C   . TYR A 1 68  ? 33.413  10.364  -4.099  1.00 27.17 ? 68  TYR A C   1 
ATOM   580  O O   . TYR A 1 68  ? 32.573  11.264  -4.054  1.00 29.60 ? 68  TYR A O   1 
ATOM   581  C CB  . TYR A 1 68  ? 35.345  10.289  -5.681  1.00 33.81 ? 68  TYR A CB  1 
ATOM   582  C CG  . TYR A 1 68  ? 35.484  11.800  -5.613  1.00 33.32 ? 68  TYR A CG  1 
ATOM   583  C CD1 . TYR A 1 68  ? 35.078  12.602  -6.674  1.00 37.08 ? 68  TYR A CD1 1 
ATOM   584  C CD2 . TYR A 1 68  ? 35.960  12.423  -4.469  1.00 33.68 ? 68  TYR A CD2 1 
ATOM   585  C CE1 . TYR A 1 68  ? 35.179  13.986  -6.610  1.00 35.47 ? 68  TYR A CE1 1 
ATOM   586  C CE2 . TYR A 1 68  ? 36.060  13.794  -4.397  1.00 34.28 ? 68  TYR A CE2 1 
ATOM   587  C CZ  . TYR A 1 68  ? 35.665  14.572  -5.467  1.00 37.88 ? 68  TYR A CZ  1 
ATOM   588  O OH  . TYR A 1 68  ? 35.757  15.953  -5.396  1.00 48.44 ? 68  TYR A OH  1 
ATOM   589  N N   . VAL A 1 69  ? 33.946  9.799   -3.028  1.00 28.34 ? 69  VAL A N   1 
ATOM   590  C CA  . VAL A 1 69  ? 33.661  10.230  -1.670  1.00 30.26 ? 69  VAL A CA  1 
ATOM   591  C C   . VAL A 1 69  ? 34.985  10.292  -0.928  1.00 32.51 ? 69  VAL A C   1 
ATOM   592  O O   . VAL A 1 69  ? 35.755  9.324   -0.938  1.00 28.89 ? 69  VAL A O   1 
ATOM   593  C CB  . VAL A 1 69  ? 32.674  9.286   -0.950  1.00 25.05 ? 69  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 69  ? 32.377  9.797   0.452   1.00 26.11 ? 69  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 69  ? 31.405  9.166   -1.749  1.00 25.21 ? 69  VAL A CG2 1 
ATOM   596  N N   . THR A 1 70  ? 35.259  11.437  -0.322  1.00 28.55 ? 70  THR A N   1 
ATOM   597  C CA  . THR A 1 70  ? 36.411  11.586  0.545   1.00 31.42 ? 70  THR A CA  1 
ATOM   598  C C   . THR A 1 70  ? 36.037  11.080  1.922   1.00 31.15 ? 70  THR A C   1 
ATOM   599  O O   . THR A 1 70  ? 34.939  11.356  2.412   1.00 27.36 ? 70  THR A O   1 
ATOM   600  C CB  . THR A 1 70  ? 36.813  13.064  0.624   1.00 31.23 ? 70  THR A CB  1 
ATOM   601  O OG1 . THR A 1 70  ? 37.076  13.529  -0.699  1.00 33.58 ? 70  THR A OG1 1 
ATOM   602  C CG2 . THR A 1 70  ? 38.078  13.250  1.452   1.00 37.51 ? 70  THR A CG2 1 
ATOM   603  N N   . LEU A 1 71  ? 36.934  10.317  2.532   1.00 31.31 ? 71  LEU A N   1 
ATOM   604  C CA  . LEU A 1 71  ? 36.745  9.849   3.900   1.00 31.12 ? 71  LEU A CA  1 
ATOM   605  C C   . LEU A 1 71  ? 36.965  11.034  4.828   1.00 34.40 ? 71  LEU A C   1 
ATOM   606  O O   . LEU A 1 71  ? 38.105  11.446  5.062   1.00 33.03 ? 71  LEU A O   1 
ATOM   607  C CB  . LEU A 1 71  ? 37.711  8.714   4.222   1.00 29.53 ? 71  LEU A CB  1 
ATOM   608  C CG  . LEU A 1 71  ? 37.343  7.726   5.338   1.00 37.48 ? 71  LEU A CG  1 
ATOM   609  C CD1 . LEU A 1 71  ? 38.458  6.681   5.502   1.00 38.11 ? 71  LEU A CD1 1 
ATOM   610  C CD2 . LEU A 1 71  ? 37.024  8.378   6.692   1.00 40.82 ? 71  LEU A CD2 1 
ATOM   611  N N   . THR A 1 72  ? 35.878  11.588  5.374   1.00 30.94 ? 72  THR A N   1 
ATOM   612  C CA  . THR A 1 72  ? 35.961  12.768  6.227   1.00 33.77 ? 72  THR A CA  1 
ATOM   613  C C   . THR A 1 72  ? 35.413  12.559  7.629   1.00 32.87 ? 72  THR A C   1 
ATOM   614  O O   . THR A 1 72  ? 35.652  13.407  8.498   1.00 29.45 ? 72  THR A O   1 
ATOM   615  C CB  . THR A 1 72  ? 35.188  13.943  5.606   1.00 32.61 ? 72  THR A CB  1 
ATOM   616  O OG1 . THR A 1 72  ? 33.827  13.544  5.422   1.00 34.99 ? 72  THR A OG1 1 
ATOM   617  C CG2 . THR A 1 72  ? 35.751  14.330  4.262   1.00 31.89 ? 72  THR A CG2 1 
ATOM   618  N N   . SER A 1 73  ? 34.696  11.466  7.881   1.00 31.52 ? 73  SER A N   1 
ATOM   619  C CA  . SER A 1 73  ? 33.880  11.369  9.077   1.00 31.63 ? 73  SER A CA  1 
ATOM   620  C C   . SER A 1 73  ? 33.771  9.914   9.520   1.00 33.30 ? 73  SER A C   1 
ATOM   621  O O   . SER A 1 73  ? 34.113  8.983   8.786   1.00 31.24 ? 73  SER A O   1 
ATOM   622  C CB  . SER A 1 73  ? 32.500  11.955  8.804   1.00 32.91 ? 73  SER A CB  1 
ATOM   623  O OG  . SER A 1 73  ? 31.854  11.120  7.854   1.00 37.27 ? 73  SER A OG  1 
ATOM   624  N N   . VAL A 1 74  ? 33.255  9.721   10.728  1.00 29.51 ? 74  VAL A N   1 
ATOM   625  C CA  . VAL A 1 74  ? 32.946  8.387   11.224  1.00 30.92 ? 74  VAL A CA  1 
ATOM   626  C C   . VAL A 1 74  ? 31.459  8.363   11.579  1.00 30.35 ? 74  VAL A C   1 
ATOM   627  O O   . VAL A 1 74  ? 30.845  9.405   11.784  1.00 29.67 ? 74  VAL A O   1 
ATOM   628  C CB  . VAL A 1 74  ? 33.814  8.017   12.444  1.00 30.55 ? 74  VAL A CB  1 
ATOM   629  C CG1 . VAL A 1 74  ? 35.293  7.906   12.030  1.00 32.42 ? 74  VAL A CG1 1 
ATOM   630  C CG2 . VAL A 1 74  ? 33.649  9.045   13.555  1.00 31.90 ? 74  VAL A CG2 1 
ATOM   631  N N   . ALA A 1 75  ? 30.888  7.160   11.659  1.00 30.57 ? 75  ALA A N   1 
ATOM   632  C CA  . ALA A 1 75  ? 29.475  7.010   12.004  1.00 29.98 ? 75  ALA A CA  1 
ATOM   633  C C   . ALA A 1 75  ? 29.229  5.613   12.560  1.00 32.93 ? 75  ALA A C   1 
ATOM   634  O O   . ALA A 1 75  ? 30.038  4.696   12.378  1.00 30.44 ? 75  ALA A O   1 
ATOM   635  C CB  . ALA A 1 75  ? 28.566  7.258   10.792  1.00 27.50 ? 75  ALA A CB  1 
ATOM   636  N N   . ARG A 1 76  ? 28.079  5.462   13.230  1.00 32.36 ? 76  ARG A N   1 
ATOM   637  C CA  . ARG A 1 76  ? 27.665  4.172   13.772  1.00 32.91 ? 76  ARG A CA  1 
ATOM   638  C C   . ARG A 1 76  ? 27.091  3.254   12.707  1.00 31.81 ? 76  ARG A C   1 
ATOM   639  O O   . ARG A 1 76  ? 27.115  2.034   12.887  1.00 35.91 ? 76  ARG A O   1 
ATOM   640  C CB  . ARG A 1 76  ? 26.618  4.373   14.874  1.00 34.60 ? 76  ARG A CB  1 
ATOM   641  C CG  . ARG A 1 76  ? 27.168  4.850   16.221  1.00 40.65 ? 76  ARG A CG  1 
ATOM   642  C CD  . ARG A 1 76  ? 26.119  4.730   17.348  1.00 42.82 ? 76  ARG A CD  1 
ATOM   643  N NE  . ARG A 1 76  ? 24.868  5.397   17.001  1.00 48.11 ? 76  ARG A NE  1 
ATOM   644  C CZ  . ARG A 1 76  ? 23.651  4.865   17.098  1.00 49.96 ? 76  ARG A CZ  1 
ATOM   645  N NH1 . ARG A 1 76  ? 23.463  3.610   17.489  1.00 45.25 ? 76  ARG A NH1 1 
ATOM   646  N NH2 . ARG A 1 76  ? 22.592  5.616   16.792  1.00 43.64 ? 76  ARG A NH2 1 
ATOM   647  N N   . ASN A 1 77  ? 26.565  3.819   11.624  1.00 27.56 ? 77  ASN A N   1 
ATOM   648  C CA  . ASN A 1 77  ? 25.962  3.071   10.528  1.00 27.98 ? 77  ASN A CA  1 
ATOM   649  C C   . ASN A 1 77  ? 25.844  4.020   9.345   1.00 23.68 ? 77  ASN A C   1 
ATOM   650  O O   . ASN A 1 77  ? 26.046  5.232   9.498   1.00 23.45 ? 77  ASN A O   1 
ATOM   651  C CB  . ASN A 1 77  ? 24.578  2.514   10.922  1.00 30.80 ? 77  ASN A CB  1 
ATOM   652  C CG  . ASN A 1 77  ? 23.644  3.617   11.345  1.00 29.83 ? 77  ASN A CG  1 
ATOM   653  O OD1 . ASN A 1 77  ? 23.347  4.516   10.549  1.00 27.70 ? 77  ASN A OD1 1 
ATOM   654  N ND2 . ASN A 1 77  ? 23.149  3.546   12.565  1.00 32.98 ? 77  ASN A ND2 1 
ATOM   655  N N   . PRO A 1 78  ? 25.530  3.512   8.152   1.00 25.25 ? 78  PRO A N   1 
ATOM   656  C CA  . PRO A 1 78  ? 25.456  4.382   6.971   1.00 23.26 ? 78  PRO A CA  1 
ATOM   657  C C   . PRO A 1 78  ? 24.105  5.038   6.734   1.00 26.58 ? 78  PRO A C   1 
ATOM   658  O O   . PRO A 1 78  ? 23.915  5.596   5.647   1.00 22.36 ? 78  PRO A O   1 
ATOM   659  C CB  . PRO A 1 78  ? 25.766  3.404   5.826   1.00 27.72 ? 78  PRO A CB  1 
ATOM   660  C CG  . PRO A 1 78  ? 25.113  2.151   6.270   1.00 24.47 ? 78  PRO A CG  1 
ATOM   661  C CD  . PRO A 1 78  ? 25.361  2.092   7.769   1.00 28.54 ? 78  PRO A CD  1 
ATOM   662  N N   . LEU A 1 79  ? 23.161  4.926   7.684   1.00 25.41 ? 79  LEU A N   1 
ATOM   663  C CA  . LEU A 1 79  ? 21.790  5.364   7.459   1.00 28.07 ? 79  LEU A CA  1 
ATOM   664  C C   . LEU A 1 79  ? 21.714  6.883   7.351   1.00 24.24 ? 79  LEU A C   1 
ATOM   665  O O   . LEU A 1 79  ? 22.281  7.599   8.180   1.00 26.82 ? 79  LEU A O   1 
ATOM   666  C CB  . LEU A 1 79  ? 20.898  4.907   8.606   1.00 26.06 ? 79  LEU A CB  1 
ATOM   667  C CG  . LEU A 1 79  ? 19.420  5.302   8.534   1.00 28.39 ? 79  LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 79  ? 18.756  4.700   7.311   1.00 26.30 ? 79  LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 79  ? 18.741  4.820   9.792   1.00 28.70 ? 79  LEU A CD2 1 
ATOM   670  N N   . VAL A 1 80  ? 20.987  7.354   6.343   1.00 24.24 ? 80  VAL A N   1 
ATOM   671  C CA  . VAL A 1 80  ? 20.704  8.771   6.114   1.00 26.95 ? 80  VAL A CA  1 
ATOM   672  C C   . VAL A 1 80  ? 19.187  8.918   6.070   1.00 25.37 ? 80  VAL A C   1 
ATOM   673  O O   . VAL A 1 80  ? 18.515  8.202   5.313   1.00 25.99 ? 80  VAL A O   1 
ATOM   674  C CB  . VAL A 1 80  ? 21.358  9.252   4.801   1.00 24.94 ? 80  VAL A CB  1 
ATOM   675  C CG1 . VAL A 1 80  ? 20.951  10.696  4.454   1.00 25.61 ? 80  VAL A CG1 1 
ATOM   676  C CG2 . VAL A 1 80  ? 22.900  9.091   4.855   1.00 26.29 ? 80  VAL A CG2 1 
ATOM   677  N N   . MET A 1 81  ? 18.632  9.807   6.895   1.00 26.99 ? 81  MET A N   1 
ATOM   678  C CA  . MET A 1 81  ? 17.172  9.941   6.892   1.00 26.14 ? 81  MET A CA  1 
ATOM   679  C C   . MET A 1 81  ? 16.692  10.256  5.486   1.00 29.52 ? 81  MET A C   1 
ATOM   680  O O   . MET A 1 81  ? 17.251  11.121  4.805   1.00 27.91 ? 81  MET A O   1 
ATOM   681  C CB  . MET A 1 81  ? 16.696  11.036  7.856   1.00 31.02 ? 81  MET A CB  1 
ATOM   682  C CG  . MET A 1 81  ? 15.143  11.117  7.998   1.00 27.58 ? 81  MET A CG  1 
ATOM   683  S SD  . MET A 1 81  ? 14.381  9.464   8.288   1.00 30.47 ? 81  MET A SD  1 
ATOM   684  C CE  . MET A 1 81  ? 12.835  9.643   7.419   1.00 32.68 ? 81  MET A CE  1 
ATOM   685  N N   . ASP A 1 82  ? 15.650  9.558   5.055   1.00 24.31 ? 82  ASP A N   1 
ATOM   686  C CA  . ASP A 1 82  ? 15.065  9.768   3.740   1.00 23.90 ? 82  ASP A CA  1 
ATOM   687  C C   . ASP A 1 82  ? 13.551  9.781   3.933   1.00 29.11 ? 82  ASP A C   1 
ATOM   688  O O   . ASP A 1 82  ? 12.964  8.808   4.417   1.00 28.93 ? 82  ASP A O   1 
ATOM   689  C CB  . ASP A 1 82  ? 15.509  8.667   2.786   1.00 25.19 ? 82  ASP A CB  1 
ATOM   690  C CG  . ASP A 1 82  ? 15.015  8.872   1.388   1.00 29.82 ? 82  ASP A CG  1 
ATOM   691  O OD1 . ASP A 1 82  ? 14.768  10.026  0.974   1.00 26.47 ? 82  ASP A OD1 1 
ATOM   692  O OD2 . ASP A 1 82  ? 14.910  7.846   0.690   1.00 30.29 ? 82  ASP A OD2 1 
ATOM   693  N N   . TYR A 1 83  ? 12.925  10.890  3.598   1.00 29.12 ? 83  TYR A N   1 
ATOM   694  C CA  . TYR A 1 83  ? 11.503  11.068  3.862   1.00 30.67 ? 83  TYR A CA  1 
ATOM   695  C C   . TYR A 1 83  ? 10.701  10.579  2.669   1.00 29.66 ? 83  TYR A C   1 
ATOM   696  O O   . TYR A 1 83  ? 11.210  10.527  1.549   1.00 27.24 ? 83  TYR A O   1 
ATOM   697  C CB  . TYR A 1 83  ? 11.197  12.547  4.160   1.00 22.93 ? 83  TYR A CB  1 
ATOM   698  C CG  . TYR A 1 83  ? 11.860  13.142  5.411   1.00 26.03 ? 83  TYR A CG  1 
ATOM   699  C CD1 . TYR A 1 83  ? 11.243  13.041  6.632   1.00 30.56 ? 83  TYR A CD1 1 
ATOM   700  C CD2 . TYR A 1 83  ? 13.077  13.863  5.350   1.00 30.81 ? 83  TYR A CD2 1 
ATOM   701  C CE1 . TYR A 1 83  ? 11.808  13.607  7.797   1.00 32.06 ? 83  TYR A CE1 1 
ATOM   702  C CE2 . TYR A 1 83  ? 13.669  14.419  6.518   1.00 23.68 ? 83  TYR A CE2 1 
ATOM   703  C CZ  . TYR A 1 83  ? 13.012  14.294  7.749   1.00 33.53 ? 83  TYR A CZ  1 
ATOM   704  O OH  . TYR A 1 83  ? 13.510  14.845  8.960   1.00 27.70 ? 83  TYR A OH  1 
ATOM   705  N N   . GLN A 1 84  ? 9.455   10.174  2.910   1.00 24.67 ? 84  GLN A N   1 
ATOM   706  C CA  . GLN A 1 84  ? 8.621   9.814   1.775   1.00 28.41 ? 84  GLN A CA  1 
ATOM   707  C C   . GLN A 1 84  ? 8.245   11.072  1.009   1.00 30.43 ? 84  GLN A C   1 
ATOM   708  O O   . GLN A 1 84  ? 7.935   12.110  1.594   1.00 27.75 ? 84  GLN A O   1 
ATOM   709  C CB  . GLN A 1 84  ? 7.330   9.104   2.199   1.00 26.96 ? 84  GLN A CB  1 
ATOM   710  C CG  . GLN A 1 84  ? 6.534   9.799   3.321   1.00 25.05 ? 84  GLN A CG  1 
ATOM   711  C CD  . GLN A 1 84  ? 5.441   8.903   3.885   1.00 30.68 ? 84  GLN A CD  1 
ATOM   712  O OE1 . GLN A 1 84  ? 5.677   8.131   4.820   1.00 29.65 ? 84  GLN A OE1 1 
ATOM   713  N NE2 . GLN A 1 84  ? 4.231   9.040   3.365   1.00 32.30 ? 84  GLN A NE2 1 
ATOM   714  N N   . ASN A 1 85  ? 8.245   10.952  -0.304  1.00 34.93 ? 85  ASN A N   1 
ATOM   715  C CA  . ASN A 1 85  ? 7.880   12.014  -1.227  1.00 39.07 ? 85  ASN A CA  1 
ATOM   716  C C   . ASN A 1 85  ? 6.463   11.915  -1.755  1.00 39.57 ? 85  ASN A C   1 
ATOM   717  O O   . ASN A 1 85  ? 6.049   12.772  -2.549  1.00 38.85 ? 85  ASN A O   1 
ATOM   718  C CB  . ASN A 1 85  ? 9.039   12.184  -2.234  1.00 44.23 ? 85  ASN A CB  1 
ATOM   719  C CG  . ASN A 1 85  ? 9.194   11.103  -3.171  1.00 44.92 ? 85  ASN A CG  1 
ATOM   720  O OD1 . ASN A 1 85  ? 8.776   10.028  -2.849  1.00 51.50 ? 85  ASN A OD1 1 
ATOM   721  N ND2 . ASN A 1 85  ? 10.128  11.263  -4.127  1.00 49.64 ? 85  ASN A ND2 1 
ATOM   722  N N   . THR A 1 86  ? 5.688   10.945  -1.271  1.00 34.91 ? 86  THR A N   1 
ATOM   723  C CA  . THR A 1 86  ? 4.239   10.983  -1.389  1.00 33.49 ? 86  THR A CA  1 
ATOM   724  C C   . THR A 1 86  ? 3.602   10.529  -0.079  1.00 35.08 ? 86  THR A C   1 
ATOM   725  O O   . THR A 1 86  ? 4.269   10.038  0.831   1.00 33.54 ? 86  THR A O   1 
ATOM   726  C CB  . THR A 1 86  ? 3.691   10.109  -2.525  1.00 38.41 ? 86  THR A CB  1 
ATOM   727  O OG1 . THR A 1 86  ? 3.673   8.735   -2.115  1.00 32.75 ? 86  THR A OG1 1 
ATOM   728  C CG2 . THR A 1 86  ? 4.461   10.296  -3.822  1.00 36.53 ? 86  THR A CG2 1 
ATOM   729  N N   . ASN A 1 87  ? 2.286   10.679  -0.004  1.00 33.59 ? 87  ASN A N   1 
ATOM   730  C CA  . ASN A 1 87  ? 1.507   10.236  1.144   1.00 37.45 ? 87  ASN A CA  1 
ATOM   731  C C   . ASN A 1 87  ? 1.217   8.742   1.118   1.00 33.15 ? 87  ASN A C   1 
ATOM   732  O O   . ASN A 1 87  ? 0.533   8.243   2.015   1.00 33.54 ? 87  ASN A O   1 
ATOM   733  C CB  . ASN A 1 87  ? 0.172   10.963  1.161   1.00 41.96 ? 87  ASN A CB  1 
ATOM   734  C CG  . ASN A 1 87  ? -0.665  10.596  -0.045  1.00 42.75 ? 87  ASN A CG  1 
ATOM   735  O OD1 . ASN A 1 87  ? -0.362  11.012  -1.166  1.00 48.17 ? 87  ASN A OD1 1 
ATOM   736  N ND2 . ASN A 1 87  ? -1.691  9.791   0.163   1.00 43.27 ? 87  ASN A ND2 1 
ATOM   737  N N   . TYR A 1 88  ? 1.684   8.024   0.099   1.00 29.77 ? 88  TYR A N   1 
ATOM   738  C CA  . TYR A 1 88  ? 1.393   6.604   -0.032  1.00 31.14 ? 88  TYR A CA  1 
ATOM   739  C C   . TYR A 1 88  ? 2.644   5.759   -0.253  1.00 32.50 ? 88  TYR A C   1 
ATOM   740  O O   . TYR A 1 88  ? 2.516   4.583   -0.596  1.00 29.32 ? 88  TYR A O   1 
ATOM   741  C CB  . TYR A 1 88  ? 0.378   6.365   -1.172  1.00 31.27 ? 88  TYR A CB  1 
ATOM   742  C CG  . TYR A 1 88  ? 0.831   6.866   -2.532  1.00 35.93 ? 88  TYR A CG  1 
ATOM   743  C CD1 . TYR A 1 88  ? 0.576   8.166   -2.930  1.00 38.46 ? 88  TYR A CD1 1 
ATOM   744  C CD2 . TYR A 1 88  ? 1.503   6.035   -3.419  1.00 34.47 ? 88  TYR A CD2 1 
ATOM   745  C CE1 . TYR A 1 88  ? 0.993   8.640   -4.173  1.00 38.29 ? 88  TYR A CE1 1 
ATOM   746  C CE2 . TYR A 1 88  ? 1.916   6.489   -4.657  1.00 38.68 ? 88  TYR A CE2 1 
ATOM   747  C CZ  . TYR A 1 88  ? 1.661   7.798   -5.027  1.00 42.72 ? 88  TYR A CZ  1 
ATOM   748  O OH  . TYR A 1 88  ? 2.073   8.252   -6.259  1.00 45.85 ? 88  TYR A OH  1 
ATOM   749  N N   . THR A 1 89  ? 3.850   6.300   -0.044  1.00 27.25 ? 89  THR A N   1 
ATOM   750  C CA  . THR A 1 89  ? 5.078   5.541   -0.298  1.00 27.31 ? 89  THR A CA  1 
ATOM   751  C C   . THR A 1 89  ? 5.875   5.274   0.982   1.00 27.20 ? 89  THR A C   1 
ATOM   752  O O   . THR A 1 89  ? 7.102   5.109   0.928   1.00 24.30 ? 89  THR A O   1 
ATOM   753  C CB  . THR A 1 89  ? 5.976   6.267   -1.302  1.00 28.33 ? 89  THR A CB  1 
ATOM   754  O OG1 . THR A 1 89  ? 6.044   7.651   -0.949  1.00 28.59 ? 89  THR A OG1 1 
ATOM   755  C CG2 . THR A 1 89  ? 5.415   6.154   -2.719  1.00 27.16 ? 89  THR A CG2 1 
ATOM   756  N N   . ALA A 1 90  ? 5.204   5.223   2.140   1.00 23.22 ? 90  ALA A N   1 
ATOM   757  C CA  . ALA A 1 90  ? 5.909   4.872   3.372   1.00 25.45 ? 90  ALA A CA  1 
ATOM   758  C C   . ALA A 1 90  ? 6.598   3.504   3.276   1.00 25.07 ? 90  ALA A C   1 
ATOM   759  O O   . ALA A 1 90  ? 7.704   3.321   3.804   1.00 22.25 ? 90  ALA A O   1 
ATOM   760  C CB  . ALA A 1 90  ? 4.946   4.878   4.559   1.00 25.15 ? 90  ALA A CB  1 
ATOM   761  N N   . CYS A 1 91  ? 5.943   2.520   2.650   1.00 25.67 ? 91  CYS A N   1 
ATOM   762  C CA  . CYS A 1 91  ? 6.536   1.180   2.613   1.00 23.61 ? 91  CYS A CA  1 
ATOM   763  C C   . CYS A 1 91  ? 7.772   1.122   1.721   1.00 22.87 ? 91  CYS A C   1 
ATOM   764  O O   . CYS A 1 91  ? 8.828   0.694   2.208   1.00 22.46 ? 91  CYS A O   1 
ATOM   765  C CB  . CYS A 1 91  ? 5.489   0.139   2.204   1.00 22.97 ? 91  CYS A CB  1 
ATOM   766  S SG  . CYS A 1 91  ? 6.116   -1.577  2.332   1.00 22.84 ? 91  CYS A SG  1 
ATOM   767  N N   . PRO A 1 92  ? 7.736   1.514   0.447   1.00 23.88 ? 92  PRO A N   1 
ATOM   768  C CA  . PRO A 1 92  ? 9.003   1.558   -0.311  1.00 26.04 ? 92  PRO A CA  1 
ATOM   769  C C   . PRO A 1 92  ? 10.046  2.503   0.285   1.00 24.59 ? 92  PRO A C   1 
ATOM   770  O O   . PRO A 1 92  ? 11.246  2.255   0.117   1.00 22.55 ? 92  PRO A O   1 
ATOM   771  C CB  . PRO A 1 92  ? 8.578   2.022   -1.711  1.00 25.04 ? 92  PRO A CB  1 
ATOM   772  C CG  . PRO A 1 92  ? 7.204   2.627   -1.515  1.00 23.40 ? 92  PRO A CG  1 
ATOM   773  C CD  . PRO A 1 92  ? 6.587   1.920   -0.374  1.00 24.32 ? 92  PRO A CD  1 
ATOM   774  N N   . THR A 1 93  ? 9.646   3.579   0.971   1.00 23.31 ? 93  THR A N   1 
ATOM   775  C CA  . THR A 1 93  ? 10.661  4.407   1.622   1.00 24.94 ? 93  THR A CA  1 
ATOM   776  C C   . THR A 1 93  ? 11.354  3.675   2.768   1.00 22.46 ? 93  THR A C   1 
ATOM   777  O O   . THR A 1 93  ? 12.577  3.808   2.945   1.00 20.28 ? 93  THR A O   1 
ATOM   778  C CB  . THR A 1 93  ? 10.054  5.723   2.120   1.00 21.53 ? 93  THR A CB  1 
ATOM   779  O OG1 . THR A 1 93  ? 9.339   6.329   1.039   1.00 19.90 ? 93  THR A OG1 1 
ATOM   780  C CG2 . THR A 1 93  ? 11.176  6.656   2.550   1.00 27.28 ? 93  THR A CG2 1 
ATOM   781  N N   . SER A 1 94  ? 10.590  2.914   3.563   1.00 20.58 ? 94  SER A N   1 
ATOM   782  C CA  . SER A 1 94  ? 11.176  2.096   4.622   1.00 20.45 ? 94  SER A CA  1 
ATOM   783  C C   . SER A 1 94  ? 12.074  1.002   4.048   1.00 22.40 ? 94  SER A C   1 
ATOM   784  O O   . SER A 1 94  ? 13.084  0.633   4.656   1.00 22.42 ? 94  SER A O   1 
ATOM   785  C CB  . SER A 1 94  ? 10.065  1.465   5.482   1.00 22.24 ? 94  SER A CB  1 
ATOM   786  O OG  . SER A 1 94  ? 9.156   2.443   6.038   1.00 21.56 ? 94  SER A OG  1 
ATOM   787  N N   . LEU A 1 95  ? 11.705  0.435   2.902   1.00 22.26 ? 95  LEU A N   1 
ATOM   788  C CA  . LEU A 1 95  ? 12.574  -0.571  2.307   1.00 22.20 ? 95  LEU A CA  1 
ATOM   789  C C   . LEU A 1 95  ? 13.844  0.084   1.779   1.00 23.01 ? 95  LEU A C   1 
ATOM   790  O O   . LEU A 1 95  ? 14.942  -0.467  1.933   1.00 23.14 ? 95  LEU A O   1 
ATOM   791  C CB  . LEU A 1 95  ? 11.835  -1.335  1.204   1.00 23.00 ? 95  LEU A CB  1 
ATOM   792  C CG  . LEU A 1 95  ? 12.660  -2.389  0.448   1.00 24.33 ? 95  LEU A CG  1 
ATOM   793  C CD1 . LEU A 1 95  ? 13.184  -3.466  1.400   1.00 20.02 ? 95  LEU A CD1 1 
ATOM   794  C CD2 . LEU A 1 95  ? 11.870  -3.019  -0.699  1.00 23.89 ? 95  LEU A CD2 1 
ATOM   795  N N   . SER A 1 96  ? 13.717  1.290   1.214   1.00 22.08 ? 96  SER A N   1 
ATOM   796  C CA  . SER A 1 96  ? 14.898  2.031   0.771   1.00 22.92 ? 96  SER A CA  1 
ATOM   797  C C   . SER A 1 96  ? 15.818  2.339   1.938   1.00 23.72 ? 96  SER A C   1 
ATOM   798  O O   . SER A 1 96  ? 17.045  2.194   1.829   1.00 24.44 ? 96  SER A O   1 
ATOM   799  C CB  . SER A 1 96  ? 14.487  3.336   0.094   1.00 23.53 ? 96  SER A CB  1 
ATOM   800  O OG  . SER A 1 96  ? 15.654  4.023   -0.369  1.00 23.85 ? 96  SER A OG  1 
ATOM   801  N N   . LEU A 1 97  ? 15.244  2.730   3.077   1.00 21.92 ? 97  LEU A N   1 
ATOM   802  C CA  . LEU A 1 97  ? 16.062  2.953   4.263   1.00 20.35 ? 97  LEU A CA  1 
ATOM   803  C C   . LEU A 1 97  ? 16.803  1.685   4.627   1.00 22.36 ? 97  LEU A C   1 
ATOM   804  O O   . LEU A 1 97  ? 17.999  1.713   4.930   1.00 21.97 ? 97  LEU A O   1 
ATOM   805  C CB  . LEU A 1 97  ? 15.190  3.408   5.432   1.00 20.98 ? 97  LEU A CB  1 
ATOM   806  C CG  . LEU A 1 97  ? 14.616  4.805   5.220   1.00 21.89 ? 97  LEU A CG  1 
ATOM   807  C CD1 . LEU A 1 97  ? 13.481  5.010   6.203   1.00 20.03 ? 97  LEU A CD1 1 
ATOM   808  C CD2 . LEU A 1 97  ? 15.709  5.859   5.399   1.00 21.00 ? 97  LEU A CD2 1 
ATOM   809  N N   . ALA A 1 98  ? 16.092  0.557   4.619   1.00 24.20 ? 98  ALA A N   1 
ATOM   810  C CA  . ALA A 1 98  ? 16.731  -0.721  4.896   1.00 20.97 ? 98  ALA A CA  1 
ATOM   811  C C   . ALA A 1 98  ? 17.857  -0.989  3.920   1.00 21.90 ? 98  ALA A C   1 
ATOM   812  O O   . ALA A 1 98  ? 18.919  -1.469  4.310   1.00 24.97 ? 98  ALA A O   1 
ATOM   813  C CB  . ALA A 1 98  ? 15.700  -1.841  4.818   1.00 21.74 ? 98  ALA A CB  1 
ATOM   814  N N   . SER A 1 99  ? 17.648  -0.679  2.641   1.00 22.27 ? 99  SER A N   1 
ATOM   815  C CA  . SER A 1 99  ? 18.668  -0.992  1.644   1.00 23.40 ? 99  SER A CA  1 
ATOM   816  C C   . SER A 1 99  ? 19.969  -0.251  1.920   1.00 25.64 ? 99  SER A C   1 
ATOM   817  O O   . SER A 1 99  ? 21.048  -0.728  1.526   1.00 24.02 ? 99  SER A O   1 
ATOM   818  C CB  . SER A 1 99  ? 18.161  -0.662  0.236   1.00 23.14 ? 99  SER A CB  1 
ATOM   819  O OG  . SER A 1 99  ? 18.150  0.734   -0.013  1.00 24.11 ? 99  SER A OG  1 
ATOM   820  N N   . GLN A 1 100 ? 19.902  0.912   2.587   1.00 21.67 ? 100 GLN A N   1 
ATOM   821  C CA  . GLN A 1 100 ? 21.132  1.606   2.988   1.00 25.67 ? 100 GLN A CA  1 
ATOM   822  C C   . GLN A 1 100 ? 21.915  0.792   4.012   1.00 28.12 ? 100 GLN A C   1 
ATOM   823  O O   . GLN A 1 100 ? 23.148  0.672   3.940   1.00 25.12 ? 100 GLN A O   1 
ATOM   824  C CB  . GLN A 1 100 ? 20.808  2.972   3.589   1.00 22.93 ? 100 GLN A CB  1 
ATOM   825  C CG  . GLN A 1 100 ? 19.963  3.920   2.765   1.00 22.58 ? 100 GLN A CG  1 
ATOM   826  C CD  . GLN A 1 100 ? 19.884  5.279   3.471   1.00 26.48 ? 100 GLN A CD  1 
ATOM   827  O OE1 . GLN A 1 100 ? 20.836  5.680   4.140   1.00 25.23 ? 100 GLN A OE1 1 
ATOM   828  N NE2 . GLN A 1 100 ? 18.730  5.956   3.380   1.00 21.20 ? 100 GLN A NE2 1 
ATOM   829  N N   . MET A 1 101 ? 21.206  0.303   5.021   1.00 23.04 ? 101 MET A N   1 
ATOM   830  C CA  . MET A 1 101 ? 21.782  -0.487  6.102   1.00 28.05 ? 101 MET A CA  1 
ATOM   831  C C   . MET A 1 101 ? 22.415  -1.771  5.596   1.00 23.86 ? 101 MET A C   1 
ATOM   832  O O   . MET A 1 101 ? 23.350  -2.283  6.221   1.00 27.24 ? 101 MET A O   1 
ATOM   833  C CB  . MET A 1 101 ? 20.669  -0.848  7.094   1.00 26.64 ? 101 MET A CB  1 
ATOM   834  C CG  . MET A 1 101 ? 20.018  0.274   7.923   1.00 31.19 ? 101 MET A CG  1 
ATOM   835  S SD  . MET A 1 101 ? 21.224  1.274   8.779   1.00 42.66 ? 101 MET A SD  1 
ATOM   836  C CE  . MET A 1 101 ? 20.776  0.840   10.431  1.00 36.72 ? 101 MET A CE  1 
ATOM   837  N N   . LEU A 1 102 ? 21.895  -2.332  4.505   1.00 22.06 ? 102 LEU A N   1 
ATOM   838  C CA  . LEU A 1 102 ? 22.414  -3.575  3.930   1.00 24.26 ? 102 LEU A CA  1 
ATOM   839  C C   . LEU A 1 102 ? 23.464  -3.328  2.848   1.00 27.06 ? 102 LEU A C   1 
ATOM   840  O O   . LEU A 1 102 ? 23.973  -4.289  2.257   1.00 26.33 ? 102 LEU A O   1 
ATOM   841  C CB  . LEU A 1 102 ? 21.267  -4.403  3.346   1.00 25.01 ? 102 LEU A CB  1 
ATOM   842  C CG  . LEU A 1 102 ? 20.225  -4.867  4.369   1.00 26.23 ? 102 LEU A CG  1 
ATOM   843  C CD1 . LEU A 1 102 ? 19.056  -5.511  3.640   1.00 24.30 ? 102 LEU A CD1 1 
ATOM   844  C CD2 . LEU A 1 102 ? 20.824  -5.819  5.398   1.00 25.19 ? 102 LEU A CD2 1 
ATOM   845  N N   . TYR A 1 103 ? 23.811  -2.068  2.596   1.00 23.99 ? 103 TYR A N   1 
ATOM   846  C CA  . TYR A 1 103 ? 24.820  -1.704  1.598   1.00 24.89 ? 103 TYR A CA  1 
ATOM   847  C C   . TYR A 1 103 ? 24.417  -2.190  0.212   1.00 26.23 ? 103 TYR A C   1 
ATOM   848  O O   . TYR A 1 103 ? 25.247  -2.676  -0.561  1.00 29.69 ? 103 TYR A O   1 
ATOM   849  C CB  . TYR A 1 103 ? 26.204  -2.227  1.990   1.00 24.87 ? 103 TYR A CB  1 
ATOM   850  C CG  . TYR A 1 103 ? 26.771  -1.524  3.208   1.00 27.19 ? 103 TYR A CG  1 
ATOM   851  C CD1 . TYR A 1 103 ? 26.420  -1.923  4.485   1.00 24.64 ? 103 TYR A CD1 1 
ATOM   852  C CD2 . TYR A 1 103 ? 27.702  -0.478  3.076   1.00 24.36 ? 103 TYR A CD2 1 
ATOM   853  C CE1 . TYR A 1 103 ? 26.934  -1.303  5.596   1.00 24.48 ? 103 TYR A CE1 1 
ATOM   854  C CE2 . TYR A 1 103 ? 28.230  0.145   4.192   1.00 22.72 ? 103 TYR A CE2 1 
ATOM   855  C CZ  . TYR A 1 103 ? 27.858  -0.268  5.441   1.00 23.53 ? 103 TYR A CZ  1 
ATOM   856  O OH  . TYR A 1 103 ? 28.390  0.369   6.546   1.00 24.71 ? 103 TYR A OH  1 
ATOM   857  N N   . HIS A 1 104 ? 23.132  -2.037  -0.107  1.00 25.23 ? 104 HIS A N   1 
ATOM   858  C CA  . HIS A 1 104 ? 22.604  -2.402  -1.417  1.00 26.61 ? 104 HIS A CA  1 
ATOM   859  C C   . HIS A 1 104 ? 21.515  -1.387  -1.742  1.00 24.79 ? 104 HIS A C   1 
ATOM   860  O O   . HIS A 1 104 ? 20.330  -1.710  -1.893  1.00 25.60 ? 104 HIS A O   1 
ATOM   861  C CB  . HIS A 1 104 ? 22.099  -3.847  -1.404  1.00 26.76 ? 104 HIS A CB  1 
ATOM   862  C CG  . HIS A 1 104 ? 21.863  -4.432  -2.766  1.00 29.21 ? 104 HIS A CG  1 
ATOM   863  N ND1 . HIS A 1 104 ? 22.880  -4.658  -3.669  1.00 27.77 ? 104 HIS A ND1 1 
ATOM   864  C CD2 . HIS A 1 104 ? 20.721  -4.827  -3.382  1.00 29.73 ? 104 HIS A CD2 1 
ATOM   865  C CE1 . HIS A 1 104 ? 22.377  -5.153  -4.785  1.00 30.31 ? 104 HIS A CE1 1 
ATOM   866  N NE2 . HIS A 1 104 ? 21.069  -5.268  -4.637  1.00 34.77 ? 104 HIS A NE2 1 
ATOM   867  N N   . TYR A 1 105 ? 21.922  -0.120  -1.810  1.00 25.91 ? 105 TYR A N   1 
ATOM   868  C CA  . TYR A 1 105 ? 20.966  0.983   -1.831  1.00 24.67 ? 105 TYR A CA  1 
ATOM   869  C C   . TYR A 1 105 ? 20.086  0.906   -3.064  1.00 26.00 ? 105 TYR A C   1 
ATOM   870  O O   . TYR A 1 105 ? 20.573  0.704   -4.178  1.00 26.26 ? 105 TYR A O   1 
ATOM   871  C CB  . TYR A 1 105 ? 21.690  2.337   -1.770  1.00 23.54 ? 105 TYR A CB  1 
ATOM   872  C CG  . TYR A 1 105 ? 20.748  3.507   -1.977  1.00 24.87 ? 105 TYR A CG  1 
ATOM   873  C CD1 . TYR A 1 105 ? 19.737  3.806   -1.050  1.00 22.86 ? 105 TYR A CD1 1 
ATOM   874  C CD2 . TYR A 1 105 ? 20.833  4.286   -3.125  1.00 25.46 ? 105 TYR A CD2 1 
ATOM   875  C CE1 . TYR A 1 105 ? 18.857  4.902   -1.265  1.00 23.92 ? 105 TYR A CE1 1 
ATOM   876  C CE2 . TYR A 1 105 ? 19.970  5.347   -3.345  1.00 27.88 ? 105 TYR A CE2 1 
ATOM   877  C CZ  . TYR A 1 105 ? 18.985  5.656   -2.416  1.00 24.82 ? 105 TYR A CZ  1 
ATOM   878  O OH  . TYR A 1 105 ? 18.131  6.704   -2.664  1.00 26.33 ? 105 TYR A OH  1 
ATOM   879  N N   . LYS A 1 106 ? 18.779  1.012   -2.844  1.00 24.24 ? 106 LYS A N   1 
ATOM   880  C CA  . LYS A 1 106 ? 17.778  1.178   -3.887  1.00 24.99 ? 106 LYS A CA  1 
ATOM   881  C C   . LYS A 1 106 ? 16.916  2.356   -3.453  1.00 26.11 ? 106 LYS A C   1 
ATOM   882  O O   . LYS A 1 106 ? 16.492  2.418   -2.293  1.00 27.76 ? 106 LYS A O   1 
ATOM   883  C CB  . LYS A 1 106 ? 16.894  -0.083  -4.058  1.00 26.36 ? 106 LYS A CB  1 
ATOM   884  C CG  . LYS A 1 106 ? 17.679  -1.383  -4.354  1.00 26.09 ? 106 LYS A CG  1 
ATOM   885  C CD  . LYS A 1 106 ? 18.339  -1.348  -5.724  1.00 28.72 ? 106 LYS A CD  1 
ATOM   886  C CE  . LYS A 1 106 ? 19.102  -2.643  -6.032  1.00 28.98 ? 106 LYS A CE  1 
ATOM   887  N NZ  . LYS A 1 106 ? 19.729  -2.602  -7.393  1.00 34.62 ? 106 LYS A NZ  1 
ATOM   888  N N   . SER A 1 107 ? 16.671  3.274   -4.369  1.00 23.37 ? 107 SER A N   1 
ATOM   889  C CA  . SER A 1 107 ? 15.950  4.504   -4.101  1.00 25.39 ? 107 SER A CA  1 
ATOM   890  C C   . SER A 1 107 ? 14.478  4.226   -3.772  1.00 26.74 ? 107 SER A C   1 
ATOM   891  O O   . SER A 1 107 ? 13.936  3.182   -4.116  1.00 23.70 ? 107 SER A O   1 
ATOM   892  C CB  . SER A 1 107 ? 16.074  5.413   -5.323  1.00 25.91 ? 107 SER A CB  1 
ATOM   893  O OG  . SER A 1 107 ? 15.093  5.090   -6.295  1.00 27.90 ? 107 SER A OG  1 
ATOM   894  N N   . GLU A 1 108 ? 13.820  5.201   -3.130  1.00 25.03 ? 108 GLU A N   1 
ATOM   895  C CA  . GLU A 1 108 ? 12.385  5.067   -2.865  1.00 26.85 ? 108 GLU A CA  1 
ATOM   896  C C   . GLU A 1 108 ? 11.620  4.750   -4.141  1.00 26.84 ? 108 GLU A C   1 
ATOM   897  O O   . GLU A 1 108 ? 10.790  3.832   -4.176  1.00 25.82 ? 108 GLU A O   1 
ATOM   898  C CB  . GLU A 1 108 ? 11.833  6.365   -2.257  1.00 28.16 ? 108 GLU A CB  1 
ATOM   899  C CG  . GLU A 1 108 ? 10.350  6.302   -1.997  1.00 31.19 ? 108 GLU A CG  1 
ATOM   900  C CD  . GLU A 1 108 ? 9.754   7.620   -1.520  1.00 34.11 ? 108 GLU A CD  1 
ATOM   901  O OE1 . GLU A 1 108 ? 10.438  8.363   -0.797  1.00 33.72 ? 108 GLU A OE1 1 
ATOM   902  O OE2 . GLU A 1 108 ? 8.562   7.873   -1.788  1.00 31.63 ? 108 GLU A OE2 1 
ATOM   903  N N   . SER A 1 109 ? 11.949  5.463   -5.218  1.00 28.32 ? 109 SER A N   1 
ATOM   904  C CA  . SER A 1 109 ? 11.271  5.307   -6.499  1.00 28.65 ? 109 SER A CA  1 
ATOM   905  C C   . SER A 1 109 ? 11.462  3.904   -7.065  1.00 30.54 ? 109 SER A C   1 
ATOM   906  O O   . SER A 1 109 ? 10.503  3.298   -7.554  1.00 29.65 ? 109 SER A O   1 
ATOM   907  C CB  . SER A 1 109 ? 11.781  6.371   -7.481  1.00 32.62 ? 109 SER A CB  1 
ATOM   908  O OG  . SER A 1 109 ? 11.204  6.185   -8.756  1.00 41.50 ? 109 SER A OG  1 
ATOM   909  N N   . GLU A 1 110 ? 12.707  3.392   -7.057  1.00 27.15 ? 110 GLU A N   1 
ATOM   910  C CA  . GLU A 1 110 ? 12.946  2.013   -7.492  1.00 29.29 ? 110 GLU A CA  1 
ATOM   911  C C   . GLU A 1 110 ? 12.143  1.029   -6.648  1.00 30.61 ? 110 GLU A C   1 
ATOM   912  O O   . GLU A 1 110 ? 11.561  0.071   -7.174  1.00 28.95 ? 110 GLU A O   1 
ATOM   913  C CB  . GLU A 1 110 ? 14.422  1.636   -7.387  1.00 26.32 ? 110 GLU A CB  1 
ATOM   914  C CG  . GLU A 1 110 ? 15.414  2.652   -7.868  1.00 33.01 ? 110 GLU A CG  1 
ATOM   915  C CD  . GLU A 1 110 ? 16.854  2.116   -7.892  1.00 36.92 ? 110 GLU A CD  1 
ATOM   916  O OE1 . GLU A 1 110 ? 17.053  0.990   -8.403  1.00 45.63 ? 110 GLU A OE1 1 
ATOM   917  O OE2 . GLU A 1 110 ? 17.770  2.809   -7.381  1.00 38.71 ? 110 GLU A OE2 1 
ATOM   918  N N   . CYS A 1 111 ? 12.139  1.236   -5.339  1.00 27.23 ? 111 CYS A N   1 
ATOM   919  C CA  . CYS A 1 111 ? 11.400  0.323   -4.436  1.00 29.06 ? 111 CYS A CA  1 
ATOM   920  C C   . CYS A 1 111 ? 9.897   0.385   -4.752  1.00 27.42 ? 111 CYS A C   1 
ATOM   921  O O   . CYS A 1 111 ? 9.279   -0.647  -4.822  1.00 30.03 ? 111 CYS A O   1 
ATOM   922  C CB  . CYS A 1 111 ? 11.703  0.639   -2.980  1.00 25.66 ? 111 CYS A CB  1 
ATOM   923  S SG  . CYS A 1 111 ? 13.366  0.143   -2.469  1.00 21.62 ? 111 CYS A SG  1 
ATOM   924  N N   . ALA A 1 112 ? 9.358   1.577   -4.957  1.00 29.30 ? 112 ALA A N   1 
ATOM   925  C CA  . ALA A 1 112 ? 7.923   1.750   -5.256  1.00 30.91 ? 112 ALA A CA  1 
ATOM   926  C C   . ALA A 1 112 ? 7.550   1.014   -6.542  1.00 35.48 ? 112 ALA A C   1 
ATOM   927  O O   . ALA A 1 112 ? 6.505   0.375   -6.579  1.00 31.31 ? 112 ALA A O   1 
ATOM   928  C CB  . ALA A 1 112 ? 7.599   3.213   -5.381  1.00 28.93 ? 112 ALA A CB  1 
ATOM   929  N N   . LYS A 1 113 ? 8.393   1.139   -7.555  1.00 37.66 ? 113 LYS A N   1 
ATOM   930  C CA  . LYS A 1 113 ? 8.080   0.534   -8.865  1.00 37.21 ? 113 LYS A CA  1 
ATOM   931  C C   . LYS A 1 113 ? 8.078   -0.979  -8.713  1.00 40.10 ? 113 LYS A C   1 
ATOM   932  O O   . LYS A 1 113 ? 7.179   -1.602  -9.224  1.00 47.66 ? 113 LYS A O   1 
ATOM   933  C CB  . LYS A 1 113 ? 9.068   1.010   -9.930  1.00 39.93 ? 113 LYS A CB  1 
ATOM   934  C CG  . LYS A 1 113 ? 8.966   2.494   -10.260 1.00 44.34 ? 113 LYS A CG  1 
ATOM   935  C CD  . LYS A 1 113 ? 9.732   2.953   -11.492 1.00 47.83 ? 113 LYS A CD  1 
ATOM   936  C CE  . LYS A 1 113 ? 10.107  4.417   -11.431 1.00 54.14 ? 113 LYS A CE  1 
ATOM   937  N NZ  . LYS A 1 113 ? 10.457  4.959   -12.762 1.00 54.76 ? 113 LYS A NZ  1 
ATOM   938  N N   . ALA A 1 114 ? 9.040   -1.504  -7.980  1.00 28.71 ? 114 ALA A N   1 
ATOM   939  C CA  . ALA A 1 114 ? 9.164   -2.958  -7.793  1.00 36.16 ? 114 ALA A CA  1 
ATOM   940  C C   . ALA A 1 114 ? 8.044   -3.503  -6.907  1.00 32.54 ? 114 ALA A C   1 
ATOM   941  O O   . ALA A 1 114 ? 7.539   -4.561  -7.199  1.00 29.55 ? 114 ALA A O   1 
ATOM   942  C CB  . ALA A 1 114 ? 10.511  -3.270  -7.218  1.00 30.94 ? 114 ALA A CB  1 
ATOM   943  N N   . LEU A 1 115 ? 7.666   -2.774  -5.869  1.00 31.23 ? 115 LEU A N   1 
ATOM   944  C CA  . LEU A 1 115 ? 6.658   -3.320  -4.961  1.00 28.85 ? 115 LEU A CA  1 
ATOM   945  C C   . LEU A 1 115 ? 5.252   -3.220  -5.536  1.00 27.44 ? 115 LEU A C   1 
ATOM   946  O O   . LEU A 1 115 ? 4.332   -3.890  -5.036  1.00 31.91 ? 115 LEU A O   1 
ATOM   947  C CB  . LEU A 1 115 ? 6.711   -2.612  -3.609  1.00 27.67 ? 115 LEU A CB  1 
ATOM   948  C CG  . LEU A 1 115 ? 7.972   -2.734  -2.769  1.00 29.07 ? 115 LEU A CG  1 
ATOM   949  C CD1 . LEU A 1 115 ? 7.711   -2.272  -1.341  1.00 28.00 ? 115 LEU A CD1 1 
ATOM   950  C CD2 . LEU A 1 115 ? 8.551   -4.157  -2.823  1.00 28.08 ? 115 LEU A CD2 1 
ATOM   951  N N   . GLY A 1 116 ? 5.052   -2.404  -6.559  1.00 27.91 ? 116 GLY A N   1 
ATOM   952  C CA  . GLY A 1 116 ? 3.714   -2.142  -7.050  1.00 31.54 ? 116 GLY A CA  1 
ATOM   953  C C   . GLY A 1 116 ? 2.933   -1.162  -6.206  1.00 34.06 ? 116 GLY A C   1 
ATOM   954  O O   . GLY A 1 116 ? 1.697   -1.158  -6.256  1.00 32.85 ? 116 GLY A O   1 
ATOM   955  N N   . THR A 1 117 ? 3.626   -0.314  -5.451  1.00 32.88 ? 117 THR A N   1 
ATOM   956  C CA  . THR A 1 117 ? 2.977   0.669   -4.592  1.00 33.76 ? 117 THR A CA  1 
ATOM   957  C C   . THR A 1 117 ? 2.016   1.550   -5.384  1.00 33.07 ? 117 THR A C   1 
ATOM   958  O O   . THR A 1 117 ? 2.314   1.973   -6.503  1.00 35.73 ? 117 THR A O   1 
ATOM   959  C CB  . THR A 1 117 ? 4.058   1.513   -3.909  1.00 30.44 ? 117 THR A CB  1 
ATOM   960  O OG1 . THR A 1 117 ? 4.856   0.662   -3.067  1.00 26.10 ? 117 THR A OG1 1 
ATOM   961  C CG2 . THR A 1 117 ? 3.427   2.651   -3.075  1.00 31.53 ? 117 THR A CG2 1 
ATOM   962  N N   . SER A 1 118 ? 0.847   1.818   -4.806  1.00 37.42 ? 118 SER A N   1 
ATOM   963  C CA  . SER A 1 118 ? -0.202  2.546   -5.504  1.00 35.73 ? 118 SER A CA  1 
ATOM   964  C C   . SER A 1 118 ? -0.779  3.641   -4.609  1.00 34.40 ? 118 SER A C   1 
ATOM   965  O O   . SER A 1 118 ? -0.696  3.582   -3.383  1.00 34.52 ? 118 SER A O   1 
ATOM   966  C CB  . SER A 1 118 ? -1.299  1.568   -5.978  1.00 40.31 ? 118 SER A CB  1 
ATOM   967  O OG  . SER A 1 118 ? -2.288  1.343   -4.971  1.00 46.21 ? 118 SER A OG  1 
ATOM   968  N N   . LYS A 1 119 ? -1.301  4.669   -5.263  1.00 36.95 ? 119 LYS A N   1 
ATOM   969  C CA  . LYS A 1 119 ? -1.889  5.856   -4.593  1.00 41.75 ? 119 LYS A CA  1 
ATOM   970  C C   . LYS A 1 119 ? -3.106  5.428   -3.792  1.00 39.68 ? 119 LYS A C   1 
ATOM   971  O O   . LYS A 1 119 ? -3.347  5.990   -2.766  1.00 46.10 ? 119 LYS A O   1 
ATOM   972  C CB  . LYS A 1 119 ? -2.377  6.881   -5.616  1.00 43.32 ? 119 LYS A CB  1 
ATOM   973  C CG  . LYS A 1 119 ? -1.333  7.421   -6.586  1.00 45.13 ? 119 LYS A CG  1 
ATOM   974  C CD  . LYS A 1 119 ? -0.416  6.379   -7.195  1.00 47.09 ? 119 LYS A CD  1 
ATOM   975  C CE  . LYS A 1 119 ? -1.113  5.331   -8.039  1.00 47.39 ? 119 LYS A CE  1 
ATOM   976  N NZ  . LYS A 1 119 ? -0.137  4.485   -8.761  1.00 46.84 ? 119 LYS A NZ  1 
ATOM   977  N N   . GLY A 1 120 ? -3.821  4.432   -4.276  1.00 42.59 ? 120 GLY A N   1 
ATOM   978  C CA  . GLY A 1 120 ? -5.031  3.997   -3.576  1.00 45.10 ? 120 GLY A CA  1 
ATOM   979  C C   . GLY A 1 120 ? -4.755  3.026   -2.461  1.00 45.58 ? 120 GLY A C   1 
ATOM   980  O O   . GLY A 1 120 ? -5.287  3.218   -1.394  1.00 53.71 ? 120 GLY A O   1 
ATOM   981  N N   . SER A 1 121 ? -3.923  2.028   -2.673  1.00 44.89 ? 121 SER A N   1 
ATOM   982  C CA  . SER A 1 121 ? -3.800  1.046   -1.575  1.00 42.44 ? 121 SER A CA  1 
ATOM   983  C C   . SER A 1 121 ? -2.486  1.173   -0.816  1.00 41.71 ? 121 SER A C   1 
ATOM   984  O O   . SER A 1 121 ? -2.366  0.546   0.224   1.00 40.56 ? 121 SER A O   1 
ATOM   985  C CB  . SER A 1 121 ? -4.010  -0.332  -2.114  1.00 45.74 ? 121 SER A CB  1 
ATOM   986  O OG  . SER A 1 121 ? -5.278  -0.396  -2.743  1.00 56.49 ? 121 SER A OG  1 
ATOM   987  N N   . GLY A 1 122 ? -1.576  2.016   -1.276  1.00 35.31 ? 122 GLY A N   1 
ATOM   988  C CA  . GLY A 1 122 ? -0.277  2.045   -0.599  1.00 31.43 ? 122 GLY A CA  1 
ATOM   989  C C   . GLY A 1 122 ? 0.404   0.734   -0.899  1.00 31.20 ? 122 GLY A C   1 
ATOM   990  O O   . GLY A 1 122 ? 0.371   0.334   -2.038  1.00 31.60 ? 122 GLY A O   1 
ATOM   991  N N   . THR A 1 123 ? 0.930   0.075   0.114   1.00 28.65 ? 123 THR A N   1 
ATOM   992  C CA  . THR A 1 123 ? 1.582   -1.234  -0.092  1.00 28.14 ? 123 THR A CA  1 
ATOM   993  C C   . THR A 1 123 ? 1.144   -2.199  1.006   1.00 27.43 ? 123 THR A C   1 
ATOM   994  O O   . THR A 1 123 ? 1.193   -1.818  2.151   1.00 26.19 ? 123 THR A O   1 
ATOM   995  C CB  . THR A 1 123 ? 3.104   -1.115  -0.006  1.00 27.43 ? 123 THR A CB  1 
ATOM   996  O OG1 . THR A 1 123 ? 3.536   -0.010  -0.786  1.00 24.53 ? 123 THR A OG1 1 
ATOM   997  C CG2 . THR A 1 123 ? 3.790   -2.382  -0.455  1.00 26.92 ? 123 THR A CG2 1 
ATOM   998  N N   . SER A 1 124 ? 0.725   -3.401  0.634   1.00 26.13 ? 124 SER A N   1 
ATOM   999  C CA  . SER A 1 124 ? 0.384   -4.396  1.645   1.00 27.28 ? 124 SER A CA  1 
ATOM   1000 C C   . SER A 1 124 ? 1.619   -5.196  2.048   1.00 28.55 ? 124 SER A C   1 
ATOM   1001 O O   . SER A 1 124 ? 2.613   -5.247  1.308   1.00 26.14 ? 124 SER A O   1 
ATOM   1002 C CB  . SER A 1 124 ? -0.700  -5.329  1.109   1.00 26.55 ? 124 SER A CB  1 
ATOM   1003 O OG  . SER A 1 124 ? -0.084  -6.343  0.350   1.00 27.21 ? 124 SER A OG  1 
ATOM   1004 N N   . PRO A 1 125 ? 1.599   -5.824  3.231   1.00 25.64 ? 125 PRO A N   1 
ATOM   1005 C CA  . PRO A 1 125 ? 2.734   -6.684  3.607   1.00 23.00 ? 125 PRO A CA  1 
ATOM   1006 C C   . PRO A 1 125 ? 3.012   -7.779  2.590   1.00 30.93 ? 125 PRO A C   1 
ATOM   1007 O O   . PRO A 1 125 ? 4.183   -8.042  2.284   1.00 26.83 ? 125 PRO A O   1 
ATOM   1008 C CB  . PRO A 1 125 ? 2.318   -7.244  4.971   1.00 23.52 ? 125 PRO A CB  1 
ATOM   1009 C CG  . PRO A 1 125 ? 1.386   -6.137  5.539   1.00 25.45 ? 125 PRO A CG  1 
ATOM   1010 C CD  . PRO A 1 125 ? 0.622   -5.662  4.333   1.00 25.05 ? 125 PRO A CD  1 
ATOM   1011 N N   . ALA A 1 126 ? 1.973   -8.389  2.008   1.00 28.64 ? 126 ALA A N   1 
ATOM   1012 C CA  . ALA A 1 126 ? 2.218   -9.396  0.978   1.00 28.94 ? 126 ALA A CA  1 
ATOM   1013 C C   . ALA A 1 126 ? 2.958   -8.805  -0.225  1.00 29.08 ? 126 ALA A C   1 
ATOM   1014 O O   . ALA A 1 126 ? 3.861   -9.450  -0.773  1.00 27.57 ? 126 ALA A O   1 
ATOM   1015 C CB  . ALA A 1 126 ? 0.906   -10.036 0.537   1.00 29.61 ? 126 ALA A CB  1 
ATOM   1016 N N   . GLN A 1 127 ? 2.590   -7.590  -0.668  1.00 30.08 ? 127 GLN A N   1 
ATOM   1017 C CA  . GLN A 1 127 ? 3.347   -6.983  -1.769  1.00 28.56 ? 127 GLN A CA  1 
ATOM   1018 C C   . GLN A 1 127 ? 4.805   -6.793  -1.396  1.00 26.75 ? 127 GLN A C   1 
ATOM   1019 O O   . GLN A 1 127 ? 5.698   -7.030  -2.217  1.00 27.31 ? 127 GLN A O   1 
ATOM   1020 C CB  . GLN A 1 127 ? 2.787   -5.635  -2.195  1.00 29.20 ? 127 GLN A CB  1 
ATOM   1021 C CG  . GLN A 1 127 ? 1.374   -5.592  -2.612  1.00 34.34 ? 127 GLN A CG  1 
ATOM   1022 C CD  . GLN A 1 127 ? 0.937   -4.165  -2.790  1.00 30.60 ? 127 GLN A CD  1 
ATOM   1023 O OE1 . GLN A 1 127 ? 0.464   -3.538  -1.855  1.00 31.83 ? 127 GLN A OE1 1 
ATOM   1024 N NE2 . GLN A 1 127 ? 1.121   -3.631  -3.989  1.00 36.34 ? 127 GLN A NE2 1 
ATOM   1025 N N   . LEU A 1 128 ? 5.062   -6.309  -0.180  1.00 25.06 ? 128 LEU A N   1 
ATOM   1026 C CA  . LEU A 1 128 ? 6.437   -6.157  0.277   1.00 28.37 ? 128 LEU A CA  1 
ATOM   1027 C C   . LEU A 1 128 ? 7.189   -7.485  0.228   1.00 28.64 ? 128 LEU A C   1 
ATOM   1028 O O   . LEU A 1 128 ? 8.284   -7.571  -0.356  1.00 26.65 ? 128 LEU A O   1 
ATOM   1029 C CB  . LEU A 1 128 ? 6.442   -5.575  1.690   1.00 23.88 ? 128 LEU A CB  1 
ATOM   1030 C CG  . LEU A 1 128 ? 7.772   -5.539  2.458   1.00 27.56 ? 128 LEU A CG  1 
ATOM   1031 C CD1 . LEU A 1 128 ? 8.799   -4.599  1.737   1.00 22.96 ? 128 LEU A CD1 1 
ATOM   1032 C CD2 . LEU A 1 128 ? 7.503   -5.043  3.866   1.00 21.67 ? 128 LEU A CD2 1 
ATOM   1033 N N   . ILE A 1 129 ? 6.601   -8.543  0.801   1.00 26.12 ? 129 ILE A N   1 
ATOM   1034 C CA  . ILE A 1 129 ? 7.302   -9.831  0.856   1.00 26.77 ? 129 ILE A CA  1 
ATOM   1035 C C   . ILE A 1 129 ? 7.507   -10.394 -0.544  1.00 28.92 ? 129 ILE A C   1 
ATOM   1036 O O   . ILE A 1 129 ? 8.591   -10.889 -0.875  1.00 30.42 ? 129 ILE A O   1 
ATOM   1037 C CB  . ILE A 1 129 ? 6.545   -10.839 1.744   1.00 27.92 ? 129 ILE A CB  1 
ATOM   1038 C CG1 . ILE A 1 129 ? 6.457   -10.362 3.206   1.00 26.43 ? 129 ILE A CG1 1 
ATOM   1039 C CG2 . ILE A 1 129 ? 7.200   -12.236 1.658   1.00 27.15 ? 129 ILE A CG2 1 
ATOM   1040 C CD1 . ILE A 1 129 ? 5.147   -10.866 3.965   1.00 27.61 ? 129 ILE A CD1 1 
ATOM   1041 N N   . ALA A 1 130 ? 6.480   -10.304 -1.393  1.00 27.65 ? 130 ALA A N   1 
ATOM   1042 C CA  . ALA A 1 130 ? 6.497   -10.975 -2.685  1.00 26.28 ? 130 ALA A CA  1 
ATOM   1043 C C   . ALA A 1 130 ? 7.468   -10.329 -3.659  1.00 30.56 ? 130 ALA A C   1 
ATOM   1044 O O   . ALA A 1 130 ? 7.998   -11.003 -4.549  1.00 28.80 ? 130 ALA A O   1 
ATOM   1045 C CB  . ALA A 1 130 ? 5.102   -10.968 -3.295  1.00 25.66 ? 130 ALA A CB  1 
ATOM   1046 N N   . ASN A 1 131 ? 7.684   -9.028  -3.542  1.00 29.84 ? 131 ASN A N   1 
ATOM   1047 C CA  . ASN A 1 131 ? 8.363   -8.310  -4.592  1.00 26.89 ? 131 ASN A CA  1 
ATOM   1048 C C   . ASN A 1 131 ? 9.748   -7.844  -4.206  1.00 30.96 ? 131 ASN A C   1 
ATOM   1049 O O   . ASN A 1 131 ? 10.523  -7.482  -5.095  1.00 29.52 ? 131 ASN A O   1 
ATOM   1050 C CB  . ASN A 1 131 ? 7.495   -7.128  -5.026  1.00 26.93 ? 131 ASN A CB  1 
ATOM   1051 C CG  . ASN A 1 131 ? 6.329   -7.579  -5.845  1.00 30.72 ? 131 ASN A CG  1 
ATOM   1052 O OD1 . ASN A 1 131 ? 6.524   -8.093  -6.959  1.00 30.19 ? 131 ASN A OD1 1 
ATOM   1053 N ND2 . ASN A 1 131 ? 5.107   -7.485  -5.281  1.00 27.41 ? 131 ASN A ND2 1 
ATOM   1054 N N   . ALA A 1 132 ? 10.087  -7.863  -2.917  1.00 31.52 ? 132 ALA A N   1 
ATOM   1055 C CA  . ALA A 1 132 ? 11.416  -7.472  -2.475  1.00 31.26 ? 132 ALA A CA  1 
ATOM   1056 C C   . ALA A 1 132 ? 12.524  -8.252  -3.181  1.00 30.21 ? 132 ALA A C   1 
ATOM   1057 O O   . ALA A 1 132 ? 13.595  -7.678  -3.407  1.00 27.91 ? 132 ALA A O   1 
ATOM   1058 C CB  . ALA A 1 132 ? 11.551  -7.642  -0.961  1.00 29.26 ? 132 ALA A CB  1 
ATOM   1059 N N   . PRO A 1 133 ? 12.345  -9.540  -3.533  1.00 31.85 ? 133 PRO A N   1 
ATOM   1060 C CA  . PRO A 1 133 ? 13.410  -10.234 -4.285  1.00 30.04 ? 133 PRO A CA  1 
ATOM   1061 C C   . PRO A 1 133 ? 13.803  -9.552  -5.580  1.00 31.54 ? 133 PRO A C   1 
ATOM   1062 O O   . PRO A 1 133 ? 14.919  -9.799  -6.069  1.00 33.54 ? 133 PRO A O   1 
ATOM   1063 C CB  . PRO A 1 133 ? 12.802  -11.611 -4.554  1.00 31.87 ? 133 PRO A CB  1 
ATOM   1064 C CG  . PRO A 1 133 ? 11.939  -11.841 -3.351  1.00 28.55 ? 133 PRO A CG  1 
ATOM   1065 C CD  . PRO A 1 133 ? 11.334  -10.509 -3.042  1.00 27.54 ? 133 PRO A CD  1 
ATOM   1066 N N   . LYS A 1 134 ? 12.914  -8.751  -6.181  1.00 28.98 ? 134 LYS A N   1 
ATOM   1067 C CA  . LYS A 1 134 ? 13.277  -8.014  -7.383  1.00 30.06 ? 134 LYS A CA  1 
ATOM   1068 C C   . LYS A 1 134 ? 14.447  -7.092  -7.127  1.00 30.78 ? 134 LYS A C   1 
ATOM   1069 O O   . LYS A 1 134 ? 15.157  -6.737  -8.072  1.00 32.78 ? 134 LYS A O   1 
ATOM   1070 C CB  . LYS A 1 134 ? 12.108  -7.169  -7.877  1.00 31.48 ? 134 LYS A CB  1 
ATOM   1071 C CG  . LYS A 1 134 ? 10.944  -7.921  -8.499  1.00 33.63 ? 134 LYS A CG  1 
ATOM   1072 C CD  . LYS A 1 134 ? 10.021  -6.886  -9.191  1.00 35.64 ? 134 LYS A CD  1 
ATOM   1073 C CE  . LYS A 1 134 ? 8.576   -7.330  -9.265  1.00 36.31 ? 134 LYS A CE  1 
ATOM   1074 N NZ  . LYS A 1 134 ? 7.671   -6.172  -9.563  1.00 32.84 ? 134 LYS A NZ  1 
ATOM   1075 N N   . LEU A 1 135 ? 14.661  -6.694  -5.870  1.00 29.87 ? 135 LEU A N   1 
ATOM   1076 C CA  . LEU A 1 135 ? 15.711  -5.741  -5.523  1.00 27.71 ? 135 LEU A CA  1 
ATOM   1077 C C   . LEU A 1 135 ? 16.906  -6.397  -4.856  1.00 29.21 ? 135 LEU A C   1 
ATOM   1078 O O   . LEU A 1 135 ? 17.834  -5.697  -4.449  1.00 32.91 ? 135 LEU A O   1 
ATOM   1079 C CB  . LEU A 1 135 ? 15.136  -4.628  -4.616  1.00 25.70 ? 135 LEU A CB  1 
ATOM   1080 C CG  . LEU A 1 135 ? 13.981  -3.853  -5.234  1.00 29.18 ? 135 LEU A CG  1 
ATOM   1081 C CD1 . LEU A 1 135 ? 13.080  -3.226  -4.169  1.00 34.46 ? 135 LEU A CD1 1 
ATOM   1082 C CD2 . LEU A 1 135 ? 14.473  -2.777  -6.169  1.00 33.99 ? 135 LEU A CD2 1 
ATOM   1083 N N   . GLY A 1 136 ? 16.902  -7.717  -4.724  1.00 29.71 ? 136 GLY A N   1 
ATOM   1084 C CA  . GLY A 1 136 ? 17.955  -8.428  -4.051  1.00 25.84 ? 136 GLY A CA  1 
ATOM   1085 C C   . GLY A 1 136 ? 17.720  -8.711  -2.588  1.00 28.21 ? 136 GLY A C   1 
ATOM   1086 O O   . GLY A 1 136 ? 18.649  -9.145  -1.910  1.00 28.53 ? 136 GLY A O   1 
ATOM   1087 N N   . PHE A 1 137 ? 16.499  -8.532  -2.078  1.00 29.50 ? 137 PHE A N   1 
ATOM   1088 C CA  . PHE A 1 137 ? 16.229  -8.708  -0.657  1.00 27.80 ? 137 PHE A CA  1 
ATOM   1089 C C   . PHE A 1 137 ? 15.265  -9.856  -0.465  1.00 27.06 ? 137 PHE A C   1 
ATOM   1090 O O   . PHE A 1 137 ? 14.515  -10.215 -1.377  1.00 28.38 ? 137 PHE A O   1 
ATOM   1091 C CB  . PHE A 1 137 ? 15.640  -7.443  -0.006  1.00 27.23 ? 137 PHE A CB  1 
ATOM   1092 C CG  . PHE A 1 137 ? 16.474  -6.241  -0.239  1.00 25.48 ? 137 PHE A CG  1 
ATOM   1093 C CD1 . PHE A 1 137 ? 17.735  -6.148  0.330   1.00 27.97 ? 137 PHE A CD1 1 
ATOM   1094 C CD2 . PHE A 1 137 ? 16.032  -5.236  -1.065  1.00 26.15 ? 137 PHE A CD2 1 
ATOM   1095 C CE1 . PHE A 1 137 ? 18.546  -5.040  0.075   1.00 28.51 ? 137 PHE A CE1 1 
ATOM   1096 C CE2 . PHE A 1 137 ? 16.826  -4.125  -1.309  1.00 28.20 ? 137 PHE A CE2 1 
ATOM   1097 C CZ  . PHE A 1 137 ? 18.089  -4.045  -0.754  1.00 24.41 ? 137 PHE A CZ  1 
ATOM   1098 N N   . LYS A 1 138 ? 15.363  -10.462 0.707   1.00 24.38 ? 138 LYS A N   1 
ATOM   1099 C CA  . LYS A 1 138 ? 14.408  -11.425 1.229   1.00 29.94 ? 138 LYS A CA  1 
ATOM   1100 C C   . LYS A 1 138 ? 13.791  -10.794 2.464   1.00 29.20 ? 138 LYS A C   1 
ATOM   1101 O O   . LYS A 1 138 ? 14.497  -10.127 3.226   1.00 29.92 ? 138 LYS A O   1 
ATOM   1102 C CB  . LYS A 1 138 ? 15.097  -12.760 1.592   1.00 26.89 ? 138 LYS A CB  1 
ATOM   1103 C CG  . LYS A 1 138 ? 14.187  -13.737 2.360   1.00 39.61 ? 138 LYS A CG  1 
ATOM   1104 C CD  . LYS A 1 138 ? 14.840  -15.100 2.575   1.00 38.73 ? 138 LYS A CD  1 
ATOM   1105 C CE  . LYS A 1 138 ? 13.951  -16.200 1.992   1.00 46.02 ? 138 LYS A CE  1 
ATOM   1106 N NZ  . LYS A 1 138 ? 12.912  -16.668 2.951   1.00 47.10 ? 138 LYS A NZ  1 
ATOM   1107 N N   . ILE A 1 139 ? 12.478  -10.964 2.641   1.00 27.59 ? 139 ILE A N   1 
ATOM   1108 C CA  . ILE A 1 139 ? 11.756  -10.428 3.797   1.00 25.19 ? 139 ILE A CA  1 
ATOM   1109 C C   . ILE A 1 139 ? 11.382  -11.593 4.692   1.00 28.17 ? 139 ILE A C   1 
ATOM   1110 O O   . ILE A 1 139 ? 10.725  -12.530 4.230   1.00 27.44 ? 139 ILE A O   1 
ATOM   1111 C CB  . ILE A 1 139 ? 10.487  -9.673  3.380   1.00 26.55 ? 139 ILE A CB  1 
ATOM   1112 C CG1 . ILE A 1 139 ? 10.794  -8.537  2.425   1.00 26.56 ? 139 ILE A CG1 1 
ATOM   1113 C CG2 . ILE A 1 139 ? 9.664   -9.243  4.638   1.00 26.72 ? 139 ILE A CG2 1 
ATOM   1114 C CD1 . ILE A 1 139 ? 11.771  -7.461  2.961   1.00 28.49 ? 139 ILE A CD1 1 
ATOM   1115 N N   . ILE A 1 140 ? 11.770  -11.542 5.962   1.00 27.42 ? 140 ILE A N   1 
ATOM   1116 C CA  . ILE A 1 140 ? 11.379  -12.594 6.894   1.00 27.71 ? 140 ILE A CA  1 
ATOM   1117 C C   . ILE A 1 140 ? 10.280  -12.045 7.807   1.00 26.53 ? 140 ILE A C   1 
ATOM   1118 O O   . ILE A 1 140 ? 10.553  -11.224 8.692   1.00 25.44 ? 140 ILE A O   1 
ATOM   1119 C CB  . ILE A 1 140 ? 12.558  -13.127 7.715   1.00 29.55 ? 140 ILE A CB  1 
ATOM   1120 C CG1 . ILE A 1 140 ? 13.660  -13.670 6.797   1.00 30.31 ? 140 ILE A CG1 1 
ATOM   1121 C CG2 . ILE A 1 140 ? 12.069  -14.270 8.635   1.00 27.50 ? 140 ILE A CG2 1 
ATOM   1122 C CD1 . ILE A 1 140 ? 14.926  -14.087 7.563   1.00 34.70 ? 140 ILE A CD1 1 
ATOM   1123 N N   . PRO A 1 141 ? 9.035   -12.490 7.663   1.00 27.70 ? 141 PRO A N   1 
ATOM   1124 C CA  . PRO A 1 141 ? 8.004   -12.089 8.642   1.00 27.89 ? 141 PRO A CA  1 
ATOM   1125 C C   . PRO A 1 141 ? 8.304   -12.710 10.001  1.00 28.40 ? 141 PRO A C   1 
ATOM   1126 O O   . PRO A 1 141 ? 8.586   -13.901 10.110  1.00 27.59 ? 141 PRO A O   1 
ATOM   1127 C CB  . PRO A 1 141 ? 6.690   -12.600 8.038   1.00 27.95 ? 141 PRO A CB  1 
ATOM   1128 C CG  . PRO A 1 141 ? 7.041   -13.378 6.817   1.00 30.79 ? 141 PRO A CG  1 
ATOM   1129 C CD  . PRO A 1 141 ? 8.514   -13.252 6.518   1.00 31.33 ? 141 PRO A CD  1 
ATOM   1130 N N   . ILE A 1 142 ? 8.310   -11.878 11.036  1.00 27.62 ? 142 ILE A N   1 
ATOM   1131 C CA  . ILE A 1 142 ? 8.581   -12.326 12.395  1.00 26.77 ? 142 ILE A CA  1 
ATOM   1132 C C   . ILE A 1 142 ? 7.417   -11.888 13.264  1.00 27.49 ? 142 ILE A C   1 
ATOM   1133 O O   . ILE A 1 142 ? 6.635   -11.012 12.897  1.00 23.80 ? 142 ILE A O   1 
ATOM   1134 C CB  . ILE A 1 142 ? 9.883   -11.748 12.969  1.00 27.02 ? 142 ILE A CB  1 
ATOM   1135 C CG1 . ILE A 1 142 ? 9.838   -10.206 12.895  1.00 25.66 ? 142 ILE A CG1 1 
ATOM   1136 C CG2 . ILE A 1 142 ? 11.132  -12.324 12.264  1.00 27.73 ? 142 ILE A CG2 1 
ATOM   1137 C CD1 . ILE A 1 142 ? 10.837  -9.529  13.830  1.00 25.40 ? 142 ILE A CD1 1 
ATOM   1138 N N   . LYS A 1 143 ? 7.352   -12.473 14.455  1.00 24.99 ? 143 LYS A N   1 
ATOM   1139 C CA  . LYS A 1 143 ? 6.322   -12.080 15.400  1.00 25.66 ? 143 LYS A CA  1 
ATOM   1140 C C   . LYS A 1 143 ? 6.603   -10.665 15.879  1.00 27.54 ? 143 LYS A C   1 
ATOM   1141 O O   . LYS A 1 143 ? 7.737   -10.184 15.831  1.00 26.16 ? 143 LYS A O   1 
ATOM   1142 C CB  . LYS A 1 143 ? 6.265   -13.036 16.582  1.00 29.45 ? 143 LYS A CB  1 
ATOM   1143 C CG  . LYS A 1 143 ? 5.830   -14.455 16.204  1.00 31.16 ? 143 LYS A CG  1 
ATOM   1144 C CD  . LYS A 1 143 ? 6.102   -15.435 17.358  1.00 41.71 ? 143 LYS A CD  1 
ATOM   1145 C CE  . LYS A 1 143 ? 7.552   -15.355 17.842  1.00 38.14 ? 143 LYS A CE  1 
ATOM   1146 N NZ  . LYS A 1 143 ? 8.467   -16.256 17.054  1.00 47.52 ? 143 LYS A NZ  1 
ATOM   1147 N N   . ARG A 1 144 ? 5.551   -9.992  16.337  1.00 24.46 ? 144 ARG A N   1 
ATOM   1148 C CA  . ARG A 1 144 ? 5.690   -8.631  16.859  1.00 28.55 ? 144 ARG A CA  1 
ATOM   1149 C C   . ARG A 1 144 ? 6.236   -8.707  18.280  1.00 27.36 ? 144 ARG A C   1 
ATOM   1150 O O   . ARG A 1 144 ? 5.537   -8.493  19.275  1.00 27.32 ? 144 ARG A O   1 
ATOM   1151 C CB  . ARG A 1 144 ? 4.361   -7.891  16.781  1.00 25.02 ? 144 ARG A CB  1 
ATOM   1152 C CG  . ARG A 1 144 ? 3.880   -7.677  15.351  1.00 25.97 ? 144 ARG A CG  1 
ATOM   1153 C CD  . ARG A 1 144 ? 2.524   -7.001  15.260  1.00 23.40 ? 144 ARG A CD  1 
ATOM   1154 N NE  . ARG A 1 144 ? 2.575   -5.551  15.444  1.00 22.82 ? 144 ARG A NE  1 
ATOM   1155 C CZ  . ARG A 1 144 ? 2.574   -4.656  14.463  1.00 24.14 ? 144 ARG A CZ  1 
ATOM   1156 N NH1 . ARG A 1 144 ? 2.636   -5.022  13.189  1.00 23.43 ? 144 ARG A NH1 1 
ATOM   1157 N NH2 . ARG A 1 144 ? 2.485   -3.356  14.764  1.00 23.16 ? 144 ARG A NH2 1 
ATOM   1158 N N   . ASP A 1 145 ? 7.530   -8.991  18.366  1.00 26.76 ? 145 ASP A N   1 
ATOM   1159 C CA  . ASP A 1 145 ? 8.152   -9.313  19.640  1.00 28.30 ? 145 ASP A CA  1 
ATOM   1160 C C   . ASP A 1 145 ? 9.550   -8.713  19.694  1.00 28.06 ? 145 ASP A C   1 
ATOM   1161 O O   . ASP A 1 145 ? 10.359  -8.920  18.784  1.00 28.93 ? 145 ASP A O   1 
ATOM   1162 C CB  . ASP A 1 145 ? 8.190   -10.842 19.816  1.00 29.59 ? 145 ASP A CB  1 
ATOM   1163 C CG  . ASP A 1 145 ? 9.166   -11.287 20.866  1.00 35.29 ? 145 ASP A CG  1 
ATOM   1164 O OD1 . ASP A 1 145 ? 10.357  -11.467 20.569  1.00 40.76 ? 145 ASP A OD1 1 
ATOM   1165 O OD2 . ASP A 1 145 ? 8.738   -11.419 22.022  1.00 37.80 ? 145 ASP A OD2 1 
ATOM   1166 N N   . SER A 1 146 ? 9.838   -7.990  20.773  1.00 28.21 ? 146 SER A N   1 
ATOM   1167 C CA  . SER A 1 146 ? 11.108  -7.279  20.856  1.00 30.91 ? 146 SER A CA  1 
ATOM   1168 C C   . SER A 1 146 ? 12.290  -8.240  20.857  1.00 30.29 ? 146 SER A C   1 
ATOM   1169 O O   . SER A 1 146 ? 13.378  -7.887  20.389  1.00 30.54 ? 146 SER A O   1 
ATOM   1170 C CB  . SER A 1 146 ? 11.142  -6.397  22.098  1.00 28.88 ? 146 SER A CB  1 
ATOM   1171 O OG  . SER A 1 146 ? 11.140  -7.215  23.241  1.00 32.28 ? 146 SER A OG  1 
ATOM   1172 N N   . LYS A 1 147 ? 12.114  -9.456  21.386  1.00 29.86 ? 147 LYS A N   1 
ATOM   1173 C CA  . LYS A 1 147 ? 13.227  -10.402 21.373  1.00 32.31 ? 147 LYS A CA  1 
ATOM   1174 C C   . LYS A 1 147 ? 13.580  -10.807 19.941  1.00 33.37 ? 147 LYS A C   1 
ATOM   1175 O O   . LYS A 1 147 ? 14.761  -10.876 19.582  1.00 32.12 ? 147 LYS A O   1 
ATOM   1176 C CB  . LYS A 1 147 ? 12.890  -11.637 22.220  1.00 34.71 ? 147 LYS A CB  1 
ATOM   1177 C CG  . LYS A 1 147 ? 13.975  -12.724 22.163  1.00 41.19 ? 147 LYS A CG  1 
ATOM   1178 C CD  . LYS A 1 147 ? 13.498  -14.007 21.450  1.00 46.11 ? 147 LYS A CD  1 
ATOM   1179 C CE  . LYS A 1 147 ? 14.588  -15.103 21.388  1.00 46.45 ? 147 LYS A CE  1 
ATOM   1180 N NZ  . LYS A 1 147 ? 15.949  -14.634 20.927  1.00 44.51 ? 147 LYS A NZ  1 
ATOM   1181 N N   . GLU A 1 148 ? 12.572  -11.045 19.103  1.00 31.56 ? 148 GLU A N   1 
ATOM   1182 C CA  . GLU A 1 148 ? 12.834  -11.386 17.707  1.00 32.19 ? 148 GLU A CA  1 
ATOM   1183 C C   . GLU A 1 148 ? 13.480  -10.221 16.957  1.00 32.89 ? 148 GLU A C   1 
ATOM   1184 O O   . GLU A 1 148 ? 14.401  -10.430 16.143  1.00 27.59 ? 148 GLU A O   1 
ATOM   1185 C CB  . GLU A 1 148 ? 11.531  -11.808 17.017  1.00 31.76 ? 148 GLU A CB  1 
ATOM   1186 C CG  . GLU A 1 148 ? 11.037  -13.219 17.357  1.00 35.25 ? 148 GLU A CG  1 
ATOM   1187 C CD  . GLU A 1 148 ? 11.941  -14.318 16.822  1.00 41.73 ? 148 GLU A CD  1 
ATOM   1188 O OE1 . GLU A 1 148 ? 11.817  -14.681 15.629  1.00 40.98 ? 148 GLU A OE1 1 
ATOM   1189 O OE2 . GLU A 1 148 ? 12.777  -14.827 17.601  1.00 40.87 ? 148 GLU A OE2 1 
ATOM   1190 N N   . VAL A 1 149 ? 13.004  -8.994  17.205  1.00 26.56 ? 149 VAL A N   1 
ATOM   1191 C CA  . VAL A 1 149 ? 13.596  -7.814  16.564  1.00 30.09 ? 149 VAL A CA  1 
ATOM   1192 C C   . VAL A 1 149 ? 15.078  -7.714  16.906  1.00 27.82 ? 149 VAL A C   1 
ATOM   1193 O O   . VAL A 1 149 ? 15.923  -7.620  16.014  1.00 30.77 ? 149 VAL A O   1 
ATOM   1194 C CB  . VAL A 1 149 ? 12.850  -6.531  16.977  1.00 30.39 ? 149 VAL A CB  1 
ATOM   1195 C CG1 . VAL A 1 149 ? 13.559  -5.290  16.389  1.00 27.27 ? 149 VAL A CG1 1 
ATOM   1196 C CG2 . VAL A 1 149 ? 11.400  -6.579  16.548  1.00 27.02 ? 149 VAL A CG2 1 
ATOM   1197 N N   . LYS A 1 150 ? 15.367  -7.851  18.187  1.00 28.90 ? 150 LYS A N   1 
ATOM   1198 C CA  . LYS A 1 150 ? 16.770  -7.827  18.640  1.00 34.48 ? 150 LYS A CA  1 
ATOM   1199 C C   . LYS A 1 150 ? 17.551  -8.976  17.999  1.00 34.37 ? 150 LYS A C   1 
ATOM   1200 O O   . LYS A 1 150 ? 18.686  -8.709  17.660  1.00 33.70 ? 150 LYS A O   1 
ATOM   1201 C CB  . LYS A 1 150 ? 16.904  -7.838  20.164  1.00 37.51 ? 150 LYS A CB  1 
ATOM   1202 C CG  . LYS A 1 150 ? 18.246  -7.329  20.665  1.00 45.79 ? 150 LYS A CG  1 
ATOM   1203 C CD  . LYS A 1 150 ? 18.355  -7.237  22.167  1.00 51.52 ? 150 LYS A CD  1 
ATOM   1204 C CE  . LYS A 1 150 ? 19.234  -8.307  22.778  1.00 52.61 ? 150 LYS A CE  1 
ATOM   1205 N NZ  . LYS A 1 150 ? 18.659  -8.879  24.019  1.00 54.71 ? 150 LYS A NZ  1 
ATOM   1206 N N   . LYS A 1 151 ? 16.973  -10.177 17.870  1.00 30.86 ? 151 LYS A N   1 
ATOM   1207 C CA  . LYS A 1 151 ? 17.741  -11.249 17.253  1.00 33.57 ? 151 LYS A CA  1 
ATOM   1208 C C   . LYS A 1 151 ? 18.233  -10.827 15.876  1.00 31.95 ? 151 LYS A C   1 
ATOM   1209 O O   . LYS A 1 151 ? 19.399  -11.044 15.534  1.00 33.96 ? 151 LYS A O   1 
ATOM   1210 C CB  . LYS A 1 151 ? 16.897  -12.504 17.153  1.00 29.98 ? 151 LYS A CB  1 
ATOM   1211 C CG  . LYS A 1 151 ? 17.533  -13.564 16.280  1.00 35.00 ? 151 LYS A CG  1 
ATOM   1212 C CD  . LYS A 1 151 ? 16.872  -14.873 16.542  1.00 41.79 ? 151 LYS A CD  1 
ATOM   1213 C CE  . LYS A 1 151 ? 16.033  -15.293 15.362  1.00 45.74 ? 151 LYS A CE  1 
ATOM   1214 N NZ  . LYS A 1 151 ? 16.224  -16.748 15.074  1.00 44.24 ? 151 LYS A NZ  1 
ATOM   1215 N N   . TYR A 1 152 ? 17.369  -10.188 15.075  1.00 31.39 ? 152 TYR A N   1 
ATOM   1216 C CA  . TYR A 1 152 ? 17.772  -9.859  13.709  1.00 32.17 ? 152 TYR A CA  1 
ATOM   1217 C C   . TYR A 1 152 ? 18.580  -8.573  13.606  1.00 31.83 ? 152 TYR A C   1 
ATOM   1218 O O   . TYR A 1 152 ? 19.486  -8.496  12.767  1.00 30.10 ? 152 TYR A O   1 
ATOM   1219 C CB  . TYR A 1 152 ? 16.550  -9.814  12.810  1.00 28.80 ? 152 TYR A CB  1 
ATOM   1220 C CG  . TYR A 1 152 ? 16.039  -11.213 12.571  1.00 30.92 ? 152 TYR A CG  1 
ATOM   1221 C CD1 . TYR A 1 152 ? 16.650  -12.038 11.630  1.00 29.36 ? 152 TYR A CD1 1 
ATOM   1222 C CD2 . TYR A 1 152 ? 14.980  -11.726 13.318  1.00 29.98 ? 152 TYR A CD2 1 
ATOM   1223 C CE1 . TYR A 1 152 ? 16.196  -13.326 11.413  1.00 31.61 ? 152 TYR A CE1 1 
ATOM   1224 C CE2 . TYR A 1 152 ? 14.525  -13.011 13.111  1.00 31.20 ? 152 TYR A CE2 1 
ATOM   1225 C CZ  . TYR A 1 152 ? 15.150  -13.807 12.161  1.00 32.19 ? 152 TYR A CZ  1 
ATOM   1226 O OH  . TYR A 1 152 ? 14.708  -15.083 11.932  1.00 34.25 ? 152 TYR A OH  1 
ATOM   1227 N N   . LEU A 1 153 ? 18.310  -7.577  14.454  1.00 30.26 ? 153 LEU A N   1 
ATOM   1228 C CA  . LEU A 1 153 ? 19.172  -6.398  14.475  1.00 32.37 ? 153 LEU A CA  1 
ATOM   1229 C C   . LEU A 1 153 ? 20.617  -6.793  14.760  1.00 33.55 ? 153 LEU A C   1 
ATOM   1230 O O   . LEU A 1 153 ? 21.557  -6.216  14.194  1.00 34.77 ? 153 LEU A O   1 
ATOM   1231 C CB  . LEU A 1 153 ? 18.673  -5.395  15.515  1.00 33.57 ? 153 LEU A CB  1 
ATOM   1232 C CG  . LEU A 1 153 ? 17.323  -4.752  15.180  1.00 32.80 ? 153 LEU A CG  1 
ATOM   1233 C CD1 . LEU A 1 153 ? 16.814  -3.938  16.370  1.00 31.10 ? 153 LEU A CD1 1 
ATOM   1234 C CD2 . LEU A 1 153 ? 17.395  -3.907  13.913  1.00 28.24 ? 153 LEU A CD2 1 
ATOM   1235 N N   . LYS A 1 154 ? 20.802  -7.802  15.610  1.00 32.82 ? 154 LYS A N   1 
ATOM   1236 C CA  . LYS A 1 154 ? 22.123  -8.270  16.006  1.00 34.35 ? 154 LYS A CA  1 
ATOM   1237 C C   . LYS A 1 154 ? 22.864  -8.885  14.832  1.00 36.03 ? 154 LYS A C   1 
ATOM   1238 O O   . LYS A 1 154 ? 24.097  -8.860  14.806  1.00 40.86 ? 154 LYS A O   1 
ATOM   1239 C CB  . LYS A 1 154 ? 21.952  -9.299  17.132  1.00 36.26 ? 154 LYS A CB  1 
ATOM   1240 C CG  . LYS A 1 154 ? 22.218  -8.814  18.559  1.00 39.74 ? 154 LYS A CG  1 
ATOM   1241 C CD  . LYS A 1 154 ? 21.805  -9.917  19.585  1.00 45.45 ? 154 LYS A CD  1 
ATOM   1242 C CE  . LYS A 1 154 ? 23.013  -10.748 20.085  1.00 48.21 ? 154 LYS A CE  1 
ATOM   1243 N NZ  . LYS A 1 154 ? 22.579  -11.893 20.958  1.00 53.43 ? 154 LYS A NZ  1 
ATOM   1244 N N   . LYS A 1 155 ? 22.136  -9.376  13.830  1.00 38.17 ? 155 LYS A N   1 
ATOM   1245 C CA  . LYS A 1 155 ? 22.726  -9.851  12.587  1.00 38.71 ? 155 LYS A CA  1 
ATOM   1246 C C   . LYS A 1 155 ? 22.977  -8.725  11.592  1.00 37.50 ? 155 LYS A C   1 
ATOM   1247 O O   . LYS A 1 155 ? 23.486  -8.983  10.497  1.00 39.19 ? 155 LYS A O   1 
ATOM   1248 C CB  . LYS A 1 155 ? 21.806  -10.892 11.936  1.00 35.22 ? 155 LYS A CB  1 
ATOM   1249 C CG  . LYS A 1 155 ? 21.624  -12.177 12.719  1.00 40.60 ? 155 LYS A CG  1 
ATOM   1250 C CD  . LYS A 1 155 ? 20.736  -13.150 11.946  1.00 35.19 ? 155 LYS A CD  1 
ATOM   1251 C CE  . LYS A 1 155 ? 20.012  -14.107 12.869  1.00 38.34 ? 155 LYS A CE  1 
ATOM   1252 N NZ  . LYS A 1 155 ? 21.021  -15.009 13.503  1.00 48.20 ? 155 LYS A NZ  1 
ATOM   1253 N N   . GLY A 1 156 ? 22.645  -7.491  11.948  1.00 33.21 ? 156 GLY A N   1 
ATOM   1254 C CA  . GLY A 1 156 ? 22.736  -6.386  11.017  1.00 33.62 ? 156 GLY A CA  1 
ATOM   1255 C C   . GLY A 1 156 ? 21.573  -6.264  10.060  1.00 34.37 ? 156 GLY A C   1 
ATOM   1256 O O   . GLY A 1 156 ? 21.687  -5.516  9.084   1.00 32.67 ? 156 GLY A O   1 
ATOM   1257 N N   . PHE A 1 157 ? 20.451  -6.975  10.304  1.00 29.50 ? 157 PHE A N   1 
ATOM   1258 C CA  . PHE A 1 157 ? 19.274  -6.891  9.432   1.00 26.00 ? 157 PHE A CA  1 
ATOM   1259 C C   . PHE A 1 157 ? 18.253  -5.940  10.048  1.00 29.33 ? 157 PHE A C   1 
ATOM   1260 O O   . PHE A 1 157 ? 17.796  -6.189  11.176  1.00 28.64 ? 157 PHE A O   1 
ATOM   1261 C CB  . PHE A 1 157 ? 18.634  -8.261  9.216   1.00 29.60 ? 157 PHE A CB  1 
ATOM   1262 C CG  . PHE A 1 157 ? 19.556  -9.308  8.624   1.00 29.00 ? 157 PHE A CG  1 
ATOM   1263 C CD1 . PHE A 1 157 ? 20.669  -8.946  7.863   1.00 30.42 ? 157 PHE A CD1 1 
ATOM   1264 C CD2 . PHE A 1 157 ? 19.278  -10.663 8.790   1.00 32.04 ? 157 PHE A CD2 1 
ATOM   1265 C CE1 . PHE A 1 157 ? 21.500  -9.901  7.323   1.00 32.85 ? 157 PHE A CE1 1 
ATOM   1266 C CE2 . PHE A 1 157 ? 20.101  -11.629 8.232   1.00 35.48 ? 157 PHE A CE2 1 
ATOM   1267 C CZ  . PHE A 1 157 ? 21.226  -11.235 7.496   1.00 32.99 ? 157 PHE A CZ  1 
ATOM   1268 N N   . PRO A 1 158 ? 17.851  -4.864  9.378   1.00 28.03 ? 158 PRO A N   1 
ATOM   1269 C CA  . PRO A 1 158 ? 16.835  -3.973  9.951   1.00 27.34 ? 158 PRO A CA  1 
ATOM   1270 C C   . PRO A 1 158 ? 15.440  -4.561  9.773   1.00 23.23 ? 158 PRO A C   1 
ATOM   1271 O O   . PRO A 1 158 ? 15.234  -5.505  9.019   1.00 23.69 ? 158 PRO A O   1 
ATOM   1272 C CB  . PRO A 1 158 ? 17.013  -2.690  9.139   1.00 23.14 ? 158 PRO A CB  1 
ATOM   1273 C CG  . PRO A 1 158 ? 17.405  -3.161  7.812   1.00 25.20 ? 158 PRO A CG  1 
ATOM   1274 C CD  . PRO A 1 158 ? 18.275  -4.405  8.041   1.00 28.98 ? 158 PRO A CD  1 
ATOM   1275 N N   . VAL A 1 159 ? 14.457  -3.971  10.459  1.00 25.01 ? 159 VAL A N   1 
ATOM   1276 C CA  . VAL A 1 159 ? 13.135  -4.604  10.547  1.00 22.12 ? 159 VAL A CA  1 
ATOM   1277 C C   . VAL A 1 159 ? 12.053  -3.588  10.212  1.00 23.38 ? 159 VAL A C   1 
ATOM   1278 O O   . VAL A 1 159 ? 11.855  -2.607  10.950  1.00 22.30 ? 159 VAL A O   1 
ATOM   1279 C CB  . VAL A 1 159 ? 12.875  -5.219  11.929  1.00 25.47 ? 159 VAL A CB  1 
ATOM   1280 C CG1 . VAL A 1 159 ? 11.440  -5.799  11.984  1.00 24.70 ? 159 VAL A CG1 1 
ATOM   1281 C CG2 . VAL A 1 159 ? 13.896  -6.326  12.241  1.00 22.49 ? 159 VAL A CG2 1 
ATOM   1282 N N   . ILE A 1 160 ? 11.341  -3.828  9.111   1.00 22.47 ? 160 ILE A N   1 
ATOM   1283 C CA  . ILE A 1 160 ? 10.260  -2.927  8.740   1.00 24.44 ? 160 ILE A CA  1 
ATOM   1284 C C   . ILE A 1 160 ? 9.080   -3.161  9.672   1.00 24.92 ? 160 ILE A C   1 
ATOM   1285 O O   . ILE A 1 160 ? 8.700   -4.304  9.951   1.00 22.69 ? 160 ILE A O   1 
ATOM   1286 C CB  . ILE A 1 160 ? 9.892   -3.104  7.260   1.00 21.41 ? 160 ILE A CB  1 
ATOM   1287 C CG1 . ILE A 1 160 ? 10.994  -2.443  6.390   1.00 21.77 ? 160 ILE A CG1 1 
ATOM   1288 C CG2 . ILE A 1 160 ? 8.551   -2.460  6.970   1.00 21.01 ? 160 ILE A CG2 1 
ATOM   1289 C CD1 . ILE A 1 160 ? 10.814  -2.601  4.856   1.00 22.65 ? 160 ILE A CD1 1 
ATOM   1290 N N   . CYS A 1 161 ? 8.545   -2.081  10.219  1.00 24.27 ? 161 CYS A N   1 
ATOM   1291 C CA  . CYS A 1 161 ? 7.375   -2.173  11.071  1.00 21.04 ? 161 CYS A CA  1 
ATOM   1292 C C   . CYS A 1 161 ? 6.161   -1.611  10.351  1.00 25.06 ? 161 CYS A C   1 
ATOM   1293 O O   . CYS A 1 161 ? 6.286   -0.764  9.467   1.00 24.48 ? 161 CYS A O   1 
ATOM   1294 C CB  . CYS A 1 161 ? 7.649   -1.497  12.419  1.00 22.86 ? 161 CYS A CB  1 
ATOM   1295 S SG  . CYS A 1 161 ? 8.049   0.273   12.363  1.00 25.04 ? 161 CYS A SG  1 
ATOM   1296 N N   . HIS A 1 162 ? 4.986   -2.142  10.702  1.00 22.11 ? 162 HIS A N   1 
ATOM   1297 C CA  . HIS A 1 162 ? 3.703   -1.787  10.102  1.00 23.84 ? 162 HIS A CA  1 
ATOM   1298 C C   . HIS A 1 162 ? 2.723   -1.518  11.234  1.00 24.46 ? 162 HIS A C   1 
ATOM   1299 O O   . HIS A 1 162 ? 2.665   -2.291  12.189  1.00 24.76 ? 162 HIS A O   1 
ATOM   1300 C CB  . HIS A 1 162 ? 3.209   -2.939  9.206   1.00 24.00 ? 162 HIS A CB  1 
ATOM   1301 C CG  . HIS A 1 162 ? 1.907   -2.682  8.507   1.00 28.04 ? 162 HIS A CG  1 
ATOM   1302 N ND1 . HIS A 1 162 ? 0.867   -3.593  8.506   1.00 26.76 ? 162 HIS A ND1 1 
ATOM   1303 C CD2 . HIS A 1 162 ? 1.478   -1.623  7.784   1.00 25.91 ? 162 HIS A CD2 1 
ATOM   1304 C CE1 . HIS A 1 162 ? -0.127  -3.117  7.780   1.00 26.68 ? 162 HIS A CE1 1 
ATOM   1305 N NE2 . HIS A 1 162 ? 0.218   -1.922  7.336   1.00 26.68 ? 162 HIS A NE2 1 
ATOM   1306 N N   . TRP A 1 163 ? 2.000   -0.400  11.180  1.00 24.69 ? 163 TRP A N   1 
ATOM   1307 C CA  . TRP A 1 163 ? 1.068   -0.124  12.269  1.00 23.20 ? 163 TRP A CA  1 
ATOM   1308 C C   . TRP A 1 163 ? 0.052   0.910   11.819  1.00 26.36 ? 163 TRP A C   1 
ATOM   1309 O O   . TRP A 1 163 ? 0.240   1.590   10.811  1.00 26.32 ? 163 TRP A O   1 
ATOM   1310 C CB  . TRP A 1 163 ? 1.804   0.310   13.544  1.00 21.04 ? 163 TRP A CB  1 
ATOM   1311 C CG  . TRP A 1 163 ? 2.260   1.768   13.695  1.00 22.56 ? 163 TRP A CG  1 
ATOM   1312 C CD1 . TRP A 1 163 ? 1.723   2.720   14.520  1.00 22.64 ? 163 TRP A CD1 1 
ATOM   1313 C CD2 . TRP A 1 163 ? 3.386   2.389   13.052  1.00 21.36 ? 163 TRP A CD2 1 
ATOM   1314 N NE1 . TRP A 1 163 ? 2.440   3.903   14.418  1.00 24.67 ? 163 TRP A NE1 1 
ATOM   1315 C CE2 . TRP A 1 163 ? 3.471   3.715   13.532  1.00 22.51 ? 163 TRP A CE2 1 
ATOM   1316 C CE3 . TRP A 1 163 ? 4.345   1.940   12.137  1.00 24.22 ? 163 TRP A CE3 1 
ATOM   1317 C CZ2 . TRP A 1 163 ? 4.448   4.613   13.090  1.00 24.48 ? 163 TRP A CZ2 1 
ATOM   1318 C CZ3 . TRP A 1 163 ? 5.322   2.834   11.706  1.00 22.83 ? 163 TRP A CZ3 1 
ATOM   1319 C CH2 . TRP A 1 163 ? 5.369   4.148   12.191  1.00 22.36 ? 163 TRP A CH2 1 
ATOM   1320 N N   . GLN A 1 164 ? -1.058  0.990   12.575  1.00 26.39 ? 164 GLN A N   1 
ATOM   1321 C CA  . GLN A 1 164 ? -2.125  1.953   12.333  1.00 25.21 ? 164 GLN A CA  1 
ATOM   1322 C C   . GLN A 1 164 ? -1.849  3.115   13.278  1.00 28.21 ? 164 GLN A C   1 
ATOM   1323 O O   . GLN A 1 164 ? -1.893  2.946   14.496  1.00 25.14 ? 164 GLN A O   1 
ATOM   1324 C CB  . GLN A 1 164 ? -3.499  1.329   12.570  1.00 28.00 ? 164 GLN A CB  1 
ATOM   1325 C CG  . GLN A 1 164 ? -3.673  -0.027  11.896  1.00 25.86 ? 164 GLN A CG  1 
ATOM   1326 C CD  . GLN A 1 164 ? -3.588  0.089   10.386  1.00 29.63 ? 164 GLN A CD  1 
ATOM   1327 O OE1 . GLN A 1 164 ? -4.288  0.909   9.773   1.00 27.26 ? 164 GLN A OE1 1 
ATOM   1328 N NE2 . GLN A 1 164 ? -2.729  -0.736  9.766   1.00 25.66 ? 164 GLN A NE2 1 
ATOM   1329 N N   . VAL A 1 165 ? -1.500  4.282   12.718  1.00 24.53 ? 165 VAL A N   1 
ATOM   1330 C CA  . VAL A 1 165 ? -0.990  5.348   13.574  1.00 25.11 ? 165 VAL A CA  1 
ATOM   1331 C C   . VAL A 1 165 ? -2.027  5.781   14.614  1.00 25.46 ? 165 VAL A C   1 
ATOM   1332 O O   . VAL A 1 165 ? -1.661  6.212   15.710  1.00 26.61 ? 165 VAL A O   1 
ATOM   1333 C CB  . VAL A 1 165 ? -0.486  6.537   12.731  1.00 29.11 ? 165 VAL A CB  1 
ATOM   1334 C CG1 . VAL A 1 165 ? 0.683   6.075   11.871  1.00 22.97 ? 165 VAL A CG1 1 
ATOM   1335 C CG2 . VAL A 1 165 ? -1.623  7.183   11.883  1.00 27.85 ? 165 VAL A CG2 1 
ATOM   1336 N N   . ASN A 1 166 ? -3.321  5.653   14.313  1.00 26.61 ? 166 ASN A N   1 
ATOM   1337 C CA  . ASN A 1 166 ? -4.337  6.012   15.313  1.00 29.97 ? 166 ASN A CA  1 
ATOM   1338 C C   . ASN A 1 166 ? -4.258  5.141   16.554  1.00 29.00 ? 166 ASN A C   1 
ATOM   1339 O O   . ASN A 1 166 ? -4.578  5.604   17.653  1.00 29.21 ? 166 ASN A O   1 
ATOM   1340 C CB  . ASN A 1 166 ? -5.734  5.910   14.722  1.00 31.43 ? 166 ASN A CB  1 
ATOM   1341 C CG  . ASN A 1 166 ? -5.926  4.641   13.956  1.00 33.86 ? 166 ASN A CG  1 
ATOM   1342 O OD1 . ASN A 1 166 ? -5.246  4.424   12.938  1.00 37.48 ? 166 ASN A OD1 1 
ATOM   1343 N ND2 . ASN A 1 166 ? -6.829  3.792   14.408  1.00 33.16 ? 166 ASN A ND2 1 
ATOM   1344 N N   . GLN A 1 167 ? -3.791  3.898   16.413  1.00 26.72 ? 167 GLN A N   1 
ATOM   1345 C CA  . GLN A 1 167 ? -3.668  3.015   17.561  1.00 24.50 ? 167 GLN A CA  1 
ATOM   1346 C C   . GLN A 1 167 ? -2.470  3.330   18.443  1.00 27.81 ? 167 GLN A C   1 
ATOM   1347 O O   . GLN A 1 167 ? -2.378  2.766   19.538  1.00 27.20 ? 167 GLN A O   1 
ATOM   1348 C CB  . GLN A 1 167 ? -3.597  1.569   17.059  1.00 24.42 ? 167 GLN A CB  1 
ATOM   1349 C CG  . GLN A 1 167 ? -4.856  1.160   16.266  1.00 28.69 ? 167 GLN A CG  1 
ATOM   1350 C CD  . GLN A 1 167 ? -4.928  -0.326  15.974  1.00 26.61 ? 167 GLN A CD  1 
ATOM   1351 O OE1 . GLN A 1 167 ? -4.329  -1.140  16.683  1.00 26.61 ? 167 GLN A OE1 1 
ATOM   1352 N NE2 . GLN A 1 167 ? -5.631  -0.689  14.893  1.00 24.98 ? 167 GLN A NE2 1 
ATOM   1353 N N   . SER A 1 168 ? -1.570  4.235   18.024  1.00 24.42 ? 168 SER A N   1 
ATOM   1354 C CA  . SER A 1 168 ? -0.420  4.615   18.834  1.00 25.23 ? 168 SER A CA  1 
ATOM   1355 C C   . SER A 1 168 ? -0.533  6.036   19.366  1.00 30.27 ? 168 SER A C   1 
ATOM   1356 O O   . SER A 1 168 ? 0.439   6.577   19.903  1.00 32.67 ? 168 SER A O   1 
ATOM   1357 C CB  . SER A 1 168 ? 0.870   4.456   18.015  1.00 29.18 ? 168 SER A CB  1 
ATOM   1358 O OG  . SER A 1 168 ? 0.888   5.380   16.934  1.00 26.36 ? 168 SER A OG  1 
ATOM   1359 N N   . ARG A 1 169 ? -1.708  6.639   19.256  1.00 30.00 ? 169 ARG A N   1 
ATOM   1360 C CA  . ARG A 1 169 ? -1.826  8.050   19.585  1.00 35.81 ? 169 ARG A CA  1 
ATOM   1361 C C   . ARG A 1 169 ? -1.737  8.291   21.090  1.00 33.41 ? 169 ARG A C   1 
ATOM   1362 O O   . ARG A 1 169 ? -1.160  9.284   21.518  1.00 37.49 ? 169 ARG A O   1 
ATOM   1363 C CB  . ARG A 1 169 ? -3.091  8.624   18.966  1.00 35.63 ? 169 ARG A CB  1 
ATOM   1364 C CG  . ARG A 1 169 ? -3.550  9.889   19.630  1.00 42.97 ? 169 ARG A CG  1 
ATOM   1365 C CD  . ARG A 1 169 ? -4.730  10.448  18.902  1.00 40.06 ? 169 ARG A CD  1 
ATOM   1366 N NE  . ARG A 1 169 ? -4.982  11.793  19.395  1.00 46.21 ? 169 ARG A NE  1 
ATOM   1367 C CZ  . ARG A 1 169 ? -5.679  12.710  18.747  1.00 40.77 ? 169 ARG A CZ  1 
ATOM   1368 N NH1 . ARG A 1 169 ? -6.299  12.432  17.612  1.00 41.13 ? 169 ARG A NH1 1 
ATOM   1369 N NH2 . ARG A 1 169 ? -5.810  13.917  19.284  1.00 47.82 ? 169 ARG A NH2 1 
ATOM   1370 N N   . ASN A 1 170 ? -2.248  7.385   21.912  1.00 33.56 ? 170 ASN A N   1 
ATOM   1371 C CA  . ASN A 1 170 ? -2.152  7.605   23.349  1.00 35.60 ? 170 ASN A CA  1 
ATOM   1372 C C   . ASN A 1 170 ? -0.821  7.148   23.919  1.00 32.97 ? 170 ASN A C   1 
ATOM   1373 O O   . ASN A 1 170 ? -0.367  7.720   24.914  1.00 38.13 ? 170 ASN A O   1 
ATOM   1374 C CB  . ASN A 1 170 ? -3.327  6.922   24.058  1.00 36.74 ? 170 ASN A CB  1 
ATOM   1375 C CG  . ASN A 1 170 ? -4.637  7.657   23.807  1.00 44.62 ? 170 ASN A CG  1 
ATOM   1376 O OD1 . ASN A 1 170 ? -4.620  8.795   23.319  1.00 41.81 ? 170 ASN A OD1 1 
ATOM   1377 N ND2 . ASN A 1 170 ? -5.769  7.003   24.071  1.00 42.75 ? 170 ASN A ND2 1 
ATOM   1378 N N   . CYS A 1 171 ? -0.174  6.145   23.311  1.00 28.00 ? 171 CYS A N   1 
ATOM   1379 C CA  . CYS A 1 171 ? 1.086   5.611   23.820  1.00 27.91 ? 171 CYS A CA  1 
ATOM   1380 C C   . CYS A 1 171 ? 2.334   6.185   23.131  1.00 31.68 ? 171 CYS A C   1 
ATOM   1381 O O   . CYS A 1 171 ? 3.436   6.007   23.646  1.00 29.52 ? 171 CYS A O   1 
ATOM   1382 C CB  . CYS A 1 171 ? 1.092   4.071   23.738  1.00 28.21 ? 171 CYS A CB  1 
ATOM   1383 S SG  . CYS A 1 171 ? 0.789   3.330   22.097  1.00 32.13 ? 171 CYS A SG  1 
ATOM   1384 N N   . LYS A 1 172 ? 2.191   6.923   22.037  1.00 28.85 ? 172 LYS A N   1 
ATOM   1385 C CA  . LYS A 1 172 ? 3.350   7.609   21.462  1.00 31.67 ? 172 LYS A CA  1 
ATOM   1386 C C   . LYS A 1 172 ? 2.928   9.010   21.051  1.00 28.60 ? 172 LYS A C   1 
ATOM   1387 O O   . LYS A 1 172 ? 3.487   9.993   21.550  1.00 28.76 ? 172 LYS A O   1 
ATOM   1388 C CB  . LYS A 1 172 ? 3.951   6.852   20.272  1.00 30.01 ? 172 LYS A CB  1 
ATOM   1389 C CG  . LYS A 1 172 ? 4.807   7.763   19.358  1.00 31.48 ? 172 LYS A CG  1 
ATOM   1390 C CD  . LYS A 1 172 ? 6.242   7.657   19.726  1.00 34.44 ? 172 LYS A CD  1 
ATOM   1391 C CE  . LYS A 1 172 ? 6.994   8.956   19.414  1.00 30.49 ? 172 LYS A CE  1 
ATOM   1392 N NZ  . LYS A 1 172 ? 8.298   8.990   20.094  1.00 34.75 ? 172 LYS A NZ  1 
ATOM   1393 N N   . GLY A 1 173 ? 1.954   9.114   20.148  1.00 29.77 ? 173 GLY A N   1 
ATOM   1394 C CA  . GLY A 1 173 ? 1.322   10.395  19.840  1.00 30.88 ? 173 GLY A CA  1 
ATOM   1395 C C   . GLY A 1 173 ? 1.922   11.256  18.746  1.00 35.38 ? 173 GLY A C   1 
ATOM   1396 O O   . GLY A 1 173 ? 1.651   12.463  18.713  1.00 29.09 ? 173 GLY A O   1 
ATOM   1397 N N   . ASP A 1 174 ? 2.680   10.685  17.812  1.00 29.80 ? 174 ASP A N   1 
ATOM   1398 C CA  . ASP A 1 174 ? 3.159   11.504  16.706  1.00 28.07 ? 174 ASP A CA  1 
ATOM   1399 C C   . ASP A 1 174 ? 2.014   11.934  15.791  1.00 27.47 ? 174 ASP A C   1 
ATOM   1400 O O   . ASP A 1 174 ? 2.127   12.956  15.106  1.00 29.16 ? 174 ASP A O   1 
ATOM   1401 C CB  . ASP A 1 174 ? 4.198   10.741  15.875  1.00 25.35 ? 174 ASP A CB  1 
ATOM   1402 C CG  . ASP A 1 174 ? 5.586   10.792  16.462  1.00 29.85 ? 174 ASP A CG  1 
ATOM   1403 O OD1 . ASP A 1 174 ? 5.802   11.496  17.475  1.00 31.73 ? 174 ASP A OD1 1 
ATOM   1404 O OD2 . ASP A 1 174 ? 6.476   10.099  15.898  1.00 29.45 ? 174 ASP A OD2 1 
ATOM   1405 N N   . TYR A 1 175 ? 0.931   11.153  15.727  1.00 28.54 ? 175 TYR A N   1 
ATOM   1406 C CA  . TYR A 1 175 ? -0.108  11.326  14.722  1.00 26.03 ? 175 TYR A CA  1 
ATOM   1407 C C   . TYR A 1 175 ? -1.479  11.530  15.344  1.00 30.92 ? 175 TYR A C   1 
ATOM   1408 O O   . TYR A 1 175 ? -1.814  10.894  16.340  1.00 30.05 ? 175 TYR A O   1 
ATOM   1409 C CB  . TYR A 1 175 ? -0.179  10.108  13.824  1.00 26.95 ? 175 TYR A CB  1 
ATOM   1410 C CG  . TYR A 1 175 ? 1.099   9.874   13.038  1.00 26.07 ? 175 TYR A CG  1 
ATOM   1411 C CD1 . TYR A 1 175 ? 1.326   10.563  11.855  1.00 26.23 ? 175 TYR A CD1 1 
ATOM   1412 C CD2 . TYR A 1 175 ? 2.065   8.986   13.488  1.00 22.40 ? 175 TYR A CD2 1 
ATOM   1413 C CE1 . TYR A 1 175 ? 2.481   10.362  11.122  1.00 28.37 ? 175 TYR A CE1 1 
ATOM   1414 C CE2 . TYR A 1 175 ? 3.245   8.789   12.766  1.00 26.35 ? 175 TYR A CE2 1 
ATOM   1415 C CZ  . TYR A 1 175 ? 3.443   9.486   11.587  1.00 26.46 ? 175 TYR A CZ  1 
ATOM   1416 O OH  . TYR A 1 175 ? 4.580   9.294   10.835  1.00 27.11 ? 175 TYR A OH  1 
ATOM   1417 N N   . THR A 1 176 ? -2.280  12.394  14.713  1.00 27.88 ? 176 THR A N   1 
ATOM   1418 C CA  . THR A 1 176 ? -3.681  12.581  15.048  1.00 32.23 ? 176 THR A CA  1 
ATOM   1419 C C   . THR A 1 176 ? -4.599  11.948  14.016  1.00 31.22 ? 176 THR A C   1 
ATOM   1420 O O   . THR A 1 176 ? -5.781  11.741  14.297  1.00 29.31 ? 176 THR A O   1 
ATOM   1421 C CB  . THR A 1 176 ? -4.010  14.081  15.135  1.00 32.67 ? 176 THR A CB  1 
ATOM   1422 O OG1 . THR A 1 176 ? -3.605  14.697  13.912  1.00 30.73 ? 176 THR A OG1 1 
ATOM   1423 C CG2 . THR A 1 176 ? -3.250  14.736  16.279  1.00 27.66 ? 176 THR A CG2 1 
ATOM   1424 N N   . GLY A 1 177 ? -4.063  11.592  12.854  1.00 30.22 ? 177 GLY A N   1 
ATOM   1425 C CA  . GLY A 1 177 ? -4.830  11.033  11.767  1.00 31.30 ? 177 GLY A CA  1 
ATOM   1426 C C   . GLY A 1 177 ? -5.088  9.547   11.930  1.00 31.88 ? 177 GLY A C   1 
ATOM   1427 O O   . GLY A 1 177 ? -4.814  8.934   12.966  1.00 26.51 ? 177 GLY A O   1 
ATOM   1428 N N   . ASN A 1 178 ? -5.722  8.991   10.895  1.00 30.82 ? 178 ASN A N   1 
ATOM   1429 C CA  . ASN A 1 178 ? -6.151  7.591   10.811  1.00 31.99 ? 178 ASN A CA  1 
ATOM   1430 C C   . ASN A 1 178 ? -5.665  7.000   9.485   1.00 37.15 ? 178 ASN A C   1 
ATOM   1431 O O   . ASN A 1 178 ? -6.229  7.319   8.430   1.00 37.42 ? 178 ASN A O   1 
ATOM   1432 C CB  . ASN A 1 178 ? -7.667  7.526   10.909  1.00 37.02 ? 178 ASN A CB  1 
ATOM   1433 C CG  . ASN A 1 178 ? -8.141  7.223   12.297  1.00 41.33 ? 178 ASN A CG  1 
ATOM   1434 O OD1 . ASN A 1 178 ? -8.598  8.112   13.016  1.00 47.01 ? 178 ASN A OD1 1 
ATOM   1435 N ND2 . ASN A 1 178 ? -8.119  5.950   12.659  1.00 40.82 ? 178 ASN A ND2 1 
ATOM   1436 N N   . PHE A 1 179 ? -4.621  6.162   9.529   1.00 25.60 ? 179 PHE A N   1 
ATOM   1437 C CA  . PHE A 1 179 ? -4.130  5.488   8.330   1.00 27.61 ? 179 PHE A CA  1 
ATOM   1438 C C   . PHE A 1 179 ? -3.120  4.427   8.742   1.00 26.02 ? 179 PHE A C   1 
ATOM   1439 O O   . PHE A 1 179 ? -2.547  4.498   9.835   1.00 26.50 ? 179 PHE A O   1 
ATOM   1440 C CB  . PHE A 1 179 ? -3.491  6.476   7.325   1.00 28.91 ? 179 PHE A CB  1 
ATOM   1441 C CG  . PHE A 1 179 ? -2.453  7.412   7.925   1.00 29.80 ? 179 PHE A CG  1 
ATOM   1442 C CD1 . PHE A 1 179 ? -1.106  7.051   7.967   1.00 28.42 ? 179 PHE A CD1 1 
ATOM   1443 C CD2 . PHE A 1 179 ? -2.811  8.673   8.402   1.00 33.96 ? 179 PHE A CD2 1 
ATOM   1444 C CE1 . PHE A 1 179 ? -0.144  7.907   8.509   1.00 27.43 ? 179 PHE A CE1 1 
ATOM   1445 C CE2 . PHE A 1 179 ? -1.837  9.540   8.937   1.00 31.78 ? 179 PHE A CE2 1 
ATOM   1446 C CZ  . PHE A 1 179 ? -0.508  9.149   8.980   1.00 28.07 ? 179 PHE A CZ  1 
ATOM   1447 N N   . GLY A 1 180 ? -2.918  3.437   7.855   1.00 25.71 ? 180 GLY A N   1 
ATOM   1448 C CA  . GLY A 1 180 ? -1.827  2.465   8.030   1.00 22.82 ? 180 GLY A CA  1 
ATOM   1449 C C   . GLY A 1 180 ? -0.477  3.031   7.608   1.00 25.40 ? 180 GLY A C   1 
ATOM   1450 O O   . GLY A 1 180 ? -0.380  3.930   6.779   1.00 23.27 ? 180 GLY A O   1 
ATOM   1451 N N   . HIS A 1 181 ? 0.588   2.541   8.233   1.00 25.04 ? 181 HIS A N   1 
ATOM   1452 C CA  . HIS A 1 181 ? 1.868   3.205   8.048   1.00 25.95 ? 181 HIS A CA  1 
ATOM   1453 C C   . HIS A 1 181 ? 3.005   2.201   8.202   1.00 24.94 ? 181 HIS A C   1 
ATOM   1454 O O   . HIS A 1 181 ? 2.824   1.115   8.757   1.00 24.37 ? 181 HIS A O   1 
ATOM   1455 C CB  . HIS A 1 181 ? 2.012   4.369   9.042   1.00 25.19 ? 181 HIS A CB  1 
ATOM   1456 C CG  . HIS A 1 181 ? 3.094   5.345   8.686   1.00 25.49 ? 181 HIS A CG  1 
ATOM   1457 N ND1 . HIS A 1 181 ? 3.283   5.806   7.399   1.00 24.91 ? 181 HIS A ND1 1 
ATOM   1458 C CD2 . HIS A 1 181 ? 4.007   5.981   9.454   1.00 19.84 ? 181 HIS A CD2 1 
ATOM   1459 C CE1 . HIS A 1 181 ? 4.268   6.688   7.387   1.00 26.70 ? 181 HIS A CE1 1 
ATOM   1460 N NE2 . HIS A 1 181 ? 4.733   6.803   8.620   1.00 25.36 ? 181 HIS A NE2 1 
ATOM   1461 N N   . TYR A 1 182 ? 4.188   2.568   7.671   1.00 22.42 ? 182 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 182 ? 5.381   1.739   7.785   1.00 22.24 ? 182 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 182 ? 6.560   2.605   8.210   1.00 26.61 ? 182 TYR A C   1 
ATOM   1464 O O   . TYR A 1 182 ? 6.621   3.800   7.880   1.00 21.63 ? 182 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 182 ? 5.766   1.078   6.456   1.00 25.44 ? 182 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 182 ? 4.797   0.054   5.922   1.00 24.24 ? 182 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 182 ? 3.726   0.432   5.116   1.00 24.55 ? 182 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 182 ? 4.984   -1.289  6.191   1.00 25.11 ? 182 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 182 ? 2.841   -0.516  4.606   1.00 27.65 ? 182 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 182 ? 4.120   -2.238  5.697   1.00 24.42 ? 182 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 182 ? 3.053   -1.853  4.902   1.00 27.22 ? 182 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 182 ? 2.194   -2.816  4.396   1.00 28.24 ? 182 TYR A OH  1 
ATOM   1473 N N   . GLY A 1 183 ? 7.500   1.987   8.921   1.00 22.14 ? 183 GLY A N   1 
ATOM   1474 C CA  . GLY A 1 183 ? 8.756   2.611   9.286   1.00 23.08 ? 183 GLY A CA  1 
ATOM   1475 C C   . GLY A 1 183 ? 9.793   1.512   9.353   1.00 27.41 ? 183 GLY A C   1 
ATOM   1476 O O   . GLY A 1 183 ? 9.486   0.349   9.086   1.00 24.63 ? 183 GLY A O   1 
ATOM   1477 N N   . LEU A 1 184 ? 11.026  1.880   9.715   1.00 23.77 ? 184 LEU A N   1 
ATOM   1478 C CA  . LEU A 1 184 ? 12.136  0.931   9.806   1.00 20.80 ? 184 LEU A CA  1 
ATOM   1479 C C   . LEU A 1 184 ? 12.722  0.934   11.215  1.00 22.42 ? 184 LEU A C   1 
ATOM   1480 O O   . LEU A 1 184 ? 13.285  1.938   11.656  1.00 24.72 ? 184 LEU A O   1 
ATOM   1481 C CB  . LEU A 1 184 ? 13.223  1.254   8.773   1.00 22.93 ? 184 LEU A CB  1 
ATOM   1482 C CG  . LEU A 1 184 ? 14.364  0.244   8.845   1.00 21.63 ? 184 LEU A CG  1 
ATOM   1483 C CD1 . LEU A 1 184 ? 13.950  -0.970  8.025   1.00 21.58 ? 184 LEU A CD1 1 
ATOM   1484 C CD2 . LEU A 1 184 ? 15.670  0.858   8.223   1.00 21.85 ? 184 LEU A CD2 1 
ATOM   1485 N N   . ILE A 1 185 ? 12.600  -0.185  11.924  1.00 19.89 ? 185 ILE A N   1 
ATOM   1486 C CA  . ILE A 1 185 ? 13.282  -0.351  13.202  1.00 21.73 ? 185 ILE A CA  1 
ATOM   1487 C C   . ILE A 1 185 ? 14.746  -0.636  12.903  1.00 25.37 ? 185 ILE A C   1 
ATOM   1488 O O   . ILE A 1 185 ? 15.071  -1.699  12.371  1.00 22.90 ? 185 ILE A O   1 
ATOM   1489 C CB  . ILE A 1 185 ? 12.668  -1.492  14.024  1.00 25.46 ? 185 ILE A CB  1 
ATOM   1490 C CG1 . ILE A 1 185 ? 11.154  -1.309  14.204  1.00 21.38 ? 185 ILE A CG1 1 
ATOM   1491 C CG2 . ILE A 1 185 ? 13.399  -1.650  15.364  1.00 23.37 ? 185 ILE A CG2 1 
ATOM   1492 C CD1 . ILE A 1 185 ? 10.525  -2.564  14.759  1.00 22.67 ? 185 ILE A CD1 1 
ATOM   1493 N N   . TRP A 1 186 ? 15.636  0.298   13.262  1.00 24.16 ? 186 TRP A N   1 
ATOM   1494 C CA  . TRP A 1 186 ? 17.061  0.097   13.038  1.00 28.73 ? 186 TRP A CA  1 
ATOM   1495 C C   . TRP A 1 186 ? 17.850  0.005   14.338  1.00 28.46 ? 186 TRP A C   1 
ATOM   1496 O O   . TRP A 1 186 ? 19.056  -0.268  14.288  1.00 27.66 ? 186 TRP A O   1 
ATOM   1497 C CB  . TRP A 1 186 ? 17.637  1.228   12.162  1.00 27.22 ? 186 TRP A CB  1 
ATOM   1498 C CG  . TRP A 1 186 ? 17.445  2.597   12.690  1.00 27.74 ? 186 TRP A CG  1 
ATOM   1499 C CD1 . TRP A 1 186 ? 16.329  3.386   12.553  1.00 25.41 ? 186 TRP A CD1 1 
ATOM   1500 C CD2 . TRP A 1 186 ? 18.399  3.380   13.434  1.00 28.60 ? 186 TRP A CD2 1 
ATOM   1501 N NE1 . TRP A 1 186 ? 16.535  4.598   13.162  1.00 27.56 ? 186 TRP A NE1 1 
ATOM   1502 C CE2 . TRP A 1 186 ? 17.785  4.621   13.723  1.00 27.12 ? 186 TRP A CE2 1 
ATOM   1503 C CE3 . TRP A 1 186 ? 19.706  3.153   13.888  1.00 29.01 ? 186 TRP A CE3 1 
ATOM   1504 C CZ2 . TRP A 1 186 ? 18.433  5.633   14.447  1.00 27.09 ? 186 TRP A CZ2 1 
ATOM   1505 C CZ3 . TRP A 1 186 ? 20.345  4.154   14.617  1.00 30.44 ? 186 TRP A CZ3 1 
ATOM   1506 C CH2 . TRP A 1 186 ? 19.703  5.374   14.894  1.00 33.10 ? 186 TRP A CH2 1 
ATOM   1507 N N   . ASP A 1 187 ? 17.199  0.201   15.492  1.00 27.52 ? 187 ASP A N   1 
ATOM   1508 C CA  . ASP A 1 187 ? 17.864  0.143   16.790  1.00 29.63 ? 187 ASP A CA  1 
ATOM   1509 C C   . ASP A 1 187 ? 16.810  -0.078  17.876  1.00 31.30 ? 187 ASP A C   1 
ATOM   1510 O O   . ASP A 1 187 ? 15.602  0.005   17.624  1.00 26.86 ? 187 ASP A O   1 
ATOM   1511 C CB  . ASP A 1 187 ? 18.648  1.433   17.047  1.00 32.78 ? 187 ASP A CB  1 
ATOM   1512 C CG  . ASP A 1 187 ? 19.731  1.268   18.087  1.00 34.02 ? 187 ASP A CG  1 
ATOM   1513 O OD1 . ASP A 1 187 ? 19.989  0.128   18.535  1.00 33.44 ? 187 ASP A OD1 1 
ATOM   1514 O OD2 . ASP A 1 187 ? 20.311  2.292   18.465  1.00 37.16 ? 187 ASP A OD2 1 
ATOM   1515 N N   . MET A 1 188 ? 17.285  -0.378  19.090  1.00 32.55 ? 188 MET A N   1 
ATOM   1516 C CA  . MET A 1 188 ? 16.428  -0.575  20.260  1.00 34.34 ? 188 MET A CA  1 
ATOM   1517 C C   . MET A 1 188 ? 17.167  -0.172  21.522  1.00 31.78 ? 188 MET A C   1 
ATOM   1518 O O   . MET A 1 188 ? 18.371  -0.391  21.636  1.00 33.61 ? 188 MET A O   1 
ATOM   1519 C CB  . MET A 1 188 ? 15.950  -2.025  20.478  1.00 33.99 ? 188 MET A CB  1 
ATOM   1520 C CG  . MET A 1 188 ? 15.224  -2.728  19.371  1.00 38.16 ? 188 MET A CG  1 
ATOM   1521 S SD  . MET A 1 188 ? 15.131  -4.539  19.663  1.00 39.12 ? 188 MET A SD  1 
ATOM   1522 C CE  . MET A 1 188 ? 14.776  -4.676  21.397  1.00 31.74 ? 188 MET A CE  1 
ATOM   1523 N N   . THR A 1 189 ? 16.426  0.377   22.483  1.00 32.66 ? 189 THR A N   1 
ATOM   1524 C CA  . THR A 1 189 ? 16.903  0.465   23.852  1.00 32.70 ? 189 THR A CA  1 
ATOM   1525 C C   . THR A 1 189 ? 16.334  -0.725  24.617  1.00 33.54 ? 189 THR A C   1 
ATOM   1526 O O   . THR A 1 189 ? 15.753  -1.639  24.033  1.00 35.70 ? 189 THR A O   1 
ATOM   1527 C CB  . THR A 1 189 ? 16.484  1.777   24.507  1.00 34.92 ? 189 THR A CB  1 
ATOM   1528 O OG1 . THR A 1 189 ? 15.065  1.785   24.701  1.00 33.13 ? 189 THR A OG1 1 
ATOM   1529 C CG2 . THR A 1 189 ? 16.850  2.950   23.599  1.00 35.25 ? 189 THR A CG2 1 
ATOM   1530 N N   . SER A 1 190 ? 16.456  -0.707  25.943  1.00 36.37 ? 190 SER A N   1 
ATOM   1531 C CA  . SER A 1 190 ? 15.884  -1.776  26.752  1.00 35.69 ? 190 SER A CA  1 
ATOM   1532 C C   . SER A 1 190 ? 14.367  -1.721  26.799  1.00 36.93 ? 190 SER A C   1 
ATOM   1533 O O   . SER A 1 190 ? 13.738  -2.712  27.189  1.00 34.45 ? 190 SER A O   1 
ATOM   1534 C CB  . SER A 1 190 ? 16.444  -1.717  28.168  1.00 38.04 ? 190 SER A CB  1 
ATOM   1535 O OG  . SER A 1 190 ? 15.964  -0.552  28.813  1.00 45.50 ? 190 SER A OG  1 
ATOM   1536 N N   . THR A 1 191 ? 13.768  -0.605  26.390  1.00 33.68 ? 191 THR A N   1 
ATOM   1537 C CA  . THR A 1 191 ? 12.327  -0.424  26.476  1.00 34.12 ? 191 THR A CA  1 
ATOM   1538 C C   . THR A 1 191 ? 11.665  -0.007  25.174  1.00 33.62 ? 191 THR A C   1 
ATOM   1539 O O   . THR A 1 191 ? 10.452  -0.227  25.042  1.00 28.36 ? 191 THR A O   1 
ATOM   1540 C CB  . THR A 1 191 ? 11.987  0.620   27.553  1.00 37.63 ? 191 THR A CB  1 
ATOM   1541 O OG1 . THR A 1 191 ? 12.657  1.850   27.237  1.00 35.76 ? 191 THR A OG1 1 
ATOM   1542 C CG2 . THR A 1 191 ? 12.427  0.140   28.944  1.00 34.94 ? 191 THR A CG2 1 
ATOM   1543 N N   . HIS A 1 192 ? 12.406  0.574   24.206  1.00 30.43 ? 192 HIS A N   1 
ATOM   1544 C CA  . HIS A 1 192 ? 11.821  1.211   23.025  1.00 28.58 ? 192 HIS A CA  1 
ATOM   1545 C C   . HIS A 1 192 ? 12.392  0.668   21.724  1.00 29.53 ? 192 HIS A C   1 
ATOM   1546 O O   . HIS A 1 192 ? 13.586  0.368   21.639  1.00 31.59 ? 192 HIS A O   1 
ATOM   1547 C CB  . HIS A 1 192 ? 12.049  2.741   23.040  1.00 28.18 ? 192 HIS A CB  1 
ATOM   1548 C CG  . HIS A 1 192 ? 11.191  3.468   24.024  1.00 29.64 ? 192 HIS A CG  1 
ATOM   1549 N ND1 . HIS A 1 192 ? 11.371  3.362   25.385  1.00 35.61 ? 192 HIS A ND1 1 
ATOM   1550 C CD2 . HIS A 1 192 ? 10.123  4.280   23.848  1.00 28.94 ? 192 HIS A CD2 1 
ATOM   1551 C CE1 . HIS A 1 192 ? 10.461  4.092   26.005  1.00 31.69 ? 192 HIS A CE1 1 
ATOM   1552 N NE2 . HIS A 1 192 ? 9.696   4.662   25.095  1.00 28.53 ? 192 HIS A NE2 1 
ATOM   1553 N N   . TYR A 1 193 ? 11.540  0.550   20.703  1.00 25.59 ? 193 TYR A N   1 
ATOM   1554 C CA  . TYR A 1 193 ? 12.046  0.448   19.337  1.00 26.19 ? 193 TYR A CA  1 
ATOM   1555 C C   . TYR A 1 193 ? 12.507  1.831   18.877  1.00 28.03 ? 193 TYR A C   1 
ATOM   1556 O O   . TYR A 1 193 ? 11.864  2.840   19.173  1.00 24.47 ? 193 TYR A O   1 
ATOM   1557 C CB  . TYR A 1 193 ? 10.969  -0.046  18.376  1.00 24.87 ? 193 TYR A CB  1 
ATOM   1558 C CG  . TYR A 1 193 ? 10.432  -1.441  18.665  1.00 26.64 ? 193 TYR A CG  1 
ATOM   1559 C CD1 . TYR A 1 193 ? 11.271  -2.559  18.642  1.00 24.11 ? 193 TYR A CD1 1 
ATOM   1560 C CD2 . TYR A 1 193 ? 9.077   -1.632  18.958  1.00 26.04 ? 193 TYR A CD2 1 
ATOM   1561 C CE1 . TYR A 1 193 ? 10.763  -3.834  18.892  1.00 28.01 ? 193 TYR A CE1 1 
ATOM   1562 C CE2 . TYR A 1 193 ? 8.556   -2.917  19.219  1.00 25.67 ? 193 TYR A CE2 1 
ATOM   1563 C CZ  . TYR A 1 193 ? 9.410   -4.008  19.190  1.00 26.87 ? 193 TYR A CZ  1 
ATOM   1564 O OH  . TYR A 1 193 ? 8.927   -5.287  19.438  1.00 28.57 ? 193 TYR A OH  1 
ATOM   1565 N N   . VAL A 1 194 ? 13.594  1.883   18.121  1.00 25.55 ? 194 VAL A N   1 
ATOM   1566 C CA  . VAL A 1 194 ? 14.005  3.130   17.486  1.00 25.77 ? 194 VAL A CA  1 
ATOM   1567 C C   . VAL A 1 194 ? 13.589  3.033   16.026  1.00 25.77 ? 194 VAL A C   1 
ATOM   1568 O O   . VAL A 1 194 ? 14.154  2.233   15.266  1.00 24.62 ? 194 VAL A O   1 
ATOM   1569 C CB  . VAL A 1 194 ? 15.509  3.384   17.618  1.00 29.10 ? 194 VAL A CB  1 
ATOM   1570 C CG1 . VAL A 1 194 ? 15.868  4.670   16.888  1.00 27.61 ? 194 VAL A CG1 1 
ATOM   1571 C CG2 . VAL A 1 194 ? 15.922  3.446   19.087  1.00 29.87 ? 194 VAL A CG2 1 
ATOM   1572 N N   . VAL A 1 195 ? 12.622  3.862   15.634  1.00 26.10 ? 195 VAL A N   1 
ATOM   1573 C CA  . VAL A 1 195 ? 11.961  3.769   14.331  1.00 26.37 ? 195 VAL A CA  1 
ATOM   1574 C C   . VAL A 1 195 ? 12.340  4.971   13.469  1.00 29.02 ? 195 VAL A C   1 
ATOM   1575 O O   . VAL A 1 195 ? 12.077  6.132   13.842  1.00 22.59 ? 195 VAL A O   1 
ATOM   1576 C CB  . VAL A 1 195 ? 10.437  3.704   14.477  1.00 25.87 ? 195 VAL A CB  1 
ATOM   1577 C CG1 . VAL A 1 195 ? 9.786   3.834   13.101  1.00 25.40 ? 195 VAL A CG1 1 
ATOM   1578 C CG2 . VAL A 1 195 ? 9.994   2.403   15.229  1.00 24.49 ? 195 VAL A CG2 1 
ATOM   1579 N N   . ALA A 1 196 ? 12.902  4.679   12.290  1.00 22.83 ? 196 ALA A N   1 
ATOM   1580 C CA  . ALA A 1 196 ? 12.999  5.643   11.202  1.00 23.52 ? 196 ALA A CA  1 
ATOM   1581 C C   . ALA A 1 196 ? 11.653  5.697   10.509  1.00 24.97 ? 196 ALA A C   1 
ATOM   1582 O O   . ALA A 1 196 ? 11.287  4.766   9.781   1.00 20.85 ? 196 ALA A O   1 
ATOM   1583 C CB  . ALA A 1 196 ? 14.105  5.259   10.219  1.00 24.24 ? 196 ALA A CB  1 
ATOM   1584 N N   . ASP A 1 197 ? 10.919  6.801   10.737  1.00 25.11 ? 197 ASP A N   1 
ATOM   1585 C CA  . ASP A 1 197 ? 9.579   7.006   10.219  1.00 24.25 ? 197 ASP A CA  1 
ATOM   1586 C C   . ASP A 1 197 ? 9.633   7.942   9.021   1.00 22.99 ? 197 ASP A C   1 
ATOM   1587 O O   . ASP A 1 197 ? 9.886   9.143   9.203   1.00 25.93 ? 197 ASP A O   1 
ATOM   1588 C CB  . ASP A 1 197 ? 8.667   7.587   11.327  1.00 23.08 ? 197 ASP A CB  1 
ATOM   1589 C CG  . ASP A 1 197 ? 7.229   7.812   10.873  1.00 27.81 ? 197 ASP A CG  1 
ATOM   1590 O OD1 . ASP A 1 197 ? 7.032   7.958   9.652   1.00 23.44 ? 197 ASP A OD1 1 
ATOM   1591 O OD2 . ASP A 1 197 ? 6.279   7.881   11.732  1.00 25.99 ? 197 ASP A OD2 1 
ATOM   1592 N N   . PRO A 1 198 ? 9.267   7.481   7.820   1.00 25.74 ? 198 PRO A N   1 
ATOM   1593 C CA  . PRO A 1 198 ? 9.448   8.315   6.615   1.00 28.29 ? 198 PRO A CA  1 
ATOM   1594 C C   . PRO A 1 198 ? 8.602   9.576   6.613   1.00 27.16 ? 198 PRO A C   1 
ATOM   1595 O O   . PRO A 1 198 ? 8.783   10.413  5.717   1.00 25.12 ? 198 PRO A O   1 
ATOM   1596 C CB  . PRO A 1 198 ? 9.010   7.387   5.471   1.00 28.78 ? 198 PRO A CB  1 
ATOM   1597 C CG  . PRO A 1 198 ? 9.033   5.987   6.065   1.00 28.41 ? 198 PRO A CG  1 
ATOM   1598 C CD  . PRO A 1 198 ? 8.672   6.163   7.503   1.00 25.33 ? 198 PRO A CD  1 
ATOM   1599 N N   . ALA A 1 199 ? 7.682   9.721   7.566   1.00 26.69 ? 199 ALA A N   1 
ATOM   1600 C CA  . ALA A 1 199 ? 6.827   10.889  7.669   1.00 27.10 ? 199 ALA A CA  1 
ATOM   1601 C C   . ALA A 1 199 ? 7.159   11.765  8.868   1.00 27.25 ? 199 ALA A C   1 
ATOM   1602 O O   . ALA A 1 199 ? 6.477   12.775  9.075   1.00 28.31 ? 199 ALA A O   1 
ATOM   1603 C CB  . ALA A 1 199 ? 5.350   10.447  7.742   1.00 25.73 ? 199 ALA A CB  1 
ATOM   1604 N N   . LYS A 1 200 ? 8.182   11.407  9.642   1.00 26.76 ? 200 LYS A N   1 
ATOM   1605 C CA  . LYS A 1 200 ? 8.428   12.182  10.876  1.00 27.12 ? 200 LYS A CA  1 
ATOM   1606 C C   . LYS A 1 200 ? 9.903   12.391  11.211  1.00 28.11 ? 200 LYS A C   1 
ATOM   1607 O O   . LYS A 1 200 ? 10.239  13.479  11.577  1.00 31.41 ? 200 LYS A O   1 
ATOM   1608 C CB  . LYS A 1 200 ? 7.749   11.491  12.058  1.00 27.79 ? 200 LYS A CB  1 
ATOM   1609 C CG  . LYS A 1 200 ? 6.264   11.769  12.183  1.00 29.16 ? 200 LYS A CG  1 
ATOM   1610 C CD  . LYS A 1 200 ? 5.947   12.543  13.408  1.00 30.08 ? 200 LYS A CD  1 
ATOM   1611 C CE  . LYS A 1 200 ? 5.695   14.002  13.174  1.00 30.41 ? 200 LYS A CE  1 
ATOM   1612 N NZ  . LYS A 1 200 ? 6.264   14.835  14.253  1.00 27.31 ? 200 LYS A NZ  1 
ATOM   1613 N N   . GLY A 1 201 ? 10.730  11.363  11.133  1.00 27.97 ? 201 GLY A N   1 
ATOM   1614 C CA  . GLY A 1 201 ? 12.108  11.537  11.543  1.00 27.13 ? 201 GLY A CA  1 
ATOM   1615 C C   . GLY A 1 201 ? 12.777  10.200  11.720  1.00 29.36 ? 201 GLY A C   1 
ATOM   1616 O O   . GLY A 1 201 ? 12.124  9.143   11.773  1.00 29.11 ? 201 GLY A O   1 
ATOM   1617 N N   . VAL A 1 202 ? 14.109  10.259  11.847  1.00 25.18 ? 202 VAL A N   1 
ATOM   1618 C CA  . VAL A 1 202 ? 14.910  9.031   11.826  1.00 26.70 ? 202 VAL A CA  1 
ATOM   1619 C C   . VAL A 1 202 ? 14.892  8.301   13.156  1.00 29.04 ? 202 VAL A C   1 
ATOM   1620 O O   . VAL A 1 202 ? 15.280  7.131   13.220  1.00 29.96 ? 202 VAL A O   1 
ATOM   1621 C CB  . VAL A 1 202 ? 16.364  9.373   11.443  1.00 28.51 ? 202 VAL A CB  1 
ATOM   1622 C CG1 . VAL A 1 202 ? 17.094  9.975   12.637  1.00 31.01 ? 202 VAL A CG1 1 
ATOM   1623 C CG2 . VAL A 1 202 ? 17.107  8.149   10.899  1.00 26.92 ? 202 VAL A CG2 1 
ATOM   1624 N N   . ASN A 1 203 ? 14.358  8.933   14.202  1.00 31.75 ? 203 ASN A N   1 
ATOM   1625 C CA  . ASN A 1 203 ? 14.647  8.578   15.584  1.00 32.14 ? 203 ASN A CA  1 
ATOM   1626 C C   . ASN A 1 203 ? 13.383  8.465   16.454  1.00 32.44 ? 203 ASN A C   1 
ATOM   1627 O O   . ASN A 1 203 ? 13.428  8.777   17.648  1.00 35.21 ? 203 ASN A O   1 
ATOM   1628 C CB  . ASN A 1 203 ? 15.592  9.645   16.154  1.00 36.47 ? 203 ASN A CB  1 
ATOM   1629 C CG  . ASN A 1 203 ? 16.381  9.156   17.315  1.00 44.17 ? 203 ASN A CG  1 
ATOM   1630 O OD1 . ASN A 1 203 ? 16.607  7.951   17.463  1.00 43.64 ? 203 ASN A OD1 1 
ATOM   1631 N ND2 . ASN A 1 203 ? 16.834  10.094  18.157  1.00 41.75 ? 203 ASN A ND2 1 
ATOM   1632 N N   . ARG A 1 204 ? 12.260  8.002   15.905  1.00 28.30 ? 204 ARG A N   1 
ATOM   1633 C CA  . ARG A 1 204 ? 11.006  7.954   16.663  1.00 29.54 ? 204 ARG A CA  1 
ATOM   1634 C C   . ARG A 1 204 ? 10.996  6.740   17.604  1.00 29.44 ? 204 ARG A C   1 
ATOM   1635 O O   . ARG A 1 204 ? 11.062  5.589   17.156  1.00 28.45 ? 204 ARG A O   1 
ATOM   1636 C CB  . ARG A 1 204 ? 9.818   7.898   15.703  1.00 27.51 ? 204 ARG A CB  1 
ATOM   1637 C CG  . ARG A 1 204 ? 9.850   8.924   14.578  1.00 29.49 ? 204 ARG A CG  1 
ATOM   1638 C CD  . ARG A 1 204 ? 10.285  10.311  15.057  1.00 30.85 ? 204 ARG A CD  1 
ATOM   1639 N NE  . ARG A 1 204 ? 9.242   10.925  15.872  1.00 30.99 ? 204 ARG A NE  1 
ATOM   1640 C CZ  . ARG A 1 204 ? 9.324   12.150  16.372  1.00 36.29 ? 204 ARG A CZ  1 
ATOM   1641 N NH1 . ARG A 1 204 ? 10.393  12.911  16.161  1.00 38.86 ? 204 ARG A NH1 1 
ATOM   1642 N NH2 . ARG A 1 204 ? 8.311   12.628  17.095  1.00 34.36 ? 204 ARG A NH2 1 
ATOM   1643 N N   . LYS A 1 205 ? 10.865  6.984   18.902  1.00 25.60 ? 205 LYS A N   1 
ATOM   1644 C CA  . LYS A 1 205 ? 11.010  5.941   19.906  1.00 27.15 ? 205 LYS A CA  1 
ATOM   1645 C C   . LYS A 1 205 ? 9.632   5.452   20.354  1.00 27.45 ? 205 LYS A C   1 
ATOM   1646 O O   . LYS A 1 205 ? 8.843   6.225   20.914  1.00 25.76 ? 205 LYS A O   1 
ATOM   1647 C CB  . LYS A 1 205 ? 11.821  6.460   21.092  1.00 28.76 ? 205 LYS A CB  1 
ATOM   1648 C CG  . LYS A 1 205 ? 13.304  6.202   20.914  1.00 37.29 ? 205 LYS A CG  1 
ATOM   1649 C CD  . LYS A 1 205 ? 14.174  7.079   21.767  1.00 39.37 ? 205 LYS A CD  1 
ATOM   1650 C CE  . LYS A 1 205 ? 15.583  7.056   21.211  1.00 40.37 ? 205 LYS A CE  1 
ATOM   1651 N NZ  . LYS A 1 205 ? 16.385  8.214   21.706  1.00 50.21 ? 205 LYS A NZ  1 
ATOM   1652 N N   . TYR A 1 206 ? 9.357   4.168   20.114  1.00 27.19 ? 206 TYR A N   1 
ATOM   1653 C CA  . TYR A 1 206 ? 8.083   3.539   20.443  1.00 25.71 ? 206 TYR A CA  1 
ATOM   1654 C C   . TYR A 1 206 ? 8.315   2.504   21.529  1.00 26.50 ? 206 TYR A C   1 
ATOM   1655 O O   . TYR A 1 206 ? 9.146   1.602   21.367  1.00 28.12 ? 206 TYR A O   1 
ATOM   1656 C CB  . TYR A 1 206 ? 7.478   2.834   19.223  1.00 25.79 ? 206 TYR A CB  1 
ATOM   1657 C CG  . TYR A 1 206 ? 6.739   3.768   18.299  1.00 27.56 ? 206 TYR A CG  1 
ATOM   1658 C CD1 . TYR A 1 206 ? 7.442   4.668   17.490  1.00 25.24 ? 206 TYR A CD1 1 
ATOM   1659 C CD2 . TYR A 1 206 ? 5.352   3.783   18.253  1.00 24.78 ? 206 TYR A CD2 1 
ATOM   1660 C CE1 . TYR A 1 206 ? 6.792   5.551   16.657  1.00 23.27 ? 206 TYR A CE1 1 
ATOM   1661 C CE2 . TYR A 1 206 ? 4.675   4.666   17.417  1.00 27.88 ? 206 TYR A CE2 1 
ATOM   1662 C CZ  . TYR A 1 206 ? 5.414   5.567   16.631  1.00 24.89 ? 206 TYR A CZ  1 
ATOM   1663 O OH  . TYR A 1 206 ? 4.770   6.443   15.805  1.00 21.60 ? 206 TYR A OH  1 
ATOM   1664 N N   . LYS A 1 207 ? 7.560   2.613   22.616  1.00 28.89 ? 207 LYS A N   1 
ATOM   1665 C CA  . LYS A 1 207 ? 7.594   1.573   23.635  1.00 26.70 ? 207 LYS A CA  1 
ATOM   1666 C C   . LYS A 1 207 ? 7.175   0.260   22.986  1.00 26.53 ? 207 LYS A C   1 
ATOM   1667 O O   . LYS A 1 207 ? 6.310   0.248   22.105  1.00 27.03 ? 207 LYS A O   1 
ATOM   1668 C CB  . LYS A 1 207 ? 6.646   1.913   24.787  1.00 29.21 ? 207 LYS A CB  1 
ATOM   1669 C CG  . LYS A 1 207 ? 7.223   2.825   25.836  1.00 35.03 ? 207 LYS A CG  1 
ATOM   1670 C CD  . LYS A 1 207 ? 7.023   2.200   27.209  1.00 44.12 ? 207 LYS A CD  1 
ATOM   1671 C CE  . LYS A 1 207 ? 8.055   2.706   28.227  1.00 45.81 ? 207 LYS A CE  1 
ATOM   1672 N NZ  . LYS A 1 207 ? 8.385   1.611   29.230  1.00 47.98 ? 207 LYS A NZ  1 
ATOM   1673 N N   . PHE A 1 208 ? 7.889   -0.828  23.303  1.00 28.18 ? 208 PHE A N   1 
ATOM   1674 C CA  . PHE A 1 208 ? 7.620   -2.106  22.632  1.00 25.88 ? 208 PHE A CA  1 
ATOM   1675 C C   . PHE A 1 208 ? 6.129   -2.400  22.575  1.00 29.51 ? 208 PHE A C   1 
ATOM   1676 O O   . PHE A 1 208 ? 5.570   -2.680  21.507  1.00 28.82 ? 208 PHE A O   1 
ATOM   1677 C CB  . PHE A 1 208 ? 8.324   -3.258  23.348  1.00 27.69 ? 208 PHE A CB  1 
ATOM   1678 C CG  . PHE A 1 208 ? 9.818   -3.132  23.393  1.00 28.64 ? 208 PHE A CG  1 
ATOM   1679 C CD1 . PHE A 1 208 ? 10.519  -2.625  22.320  1.00 28.21 ? 208 PHE A CD1 1 
ATOM   1680 C CD2 . PHE A 1 208 ? 10.521  -3.518  24.528  1.00 31.28 ? 208 PHE A CD2 1 
ATOM   1681 C CE1 . PHE A 1 208 ? 11.897  -2.506  22.368  1.00 28.70 ? 208 PHE A CE1 1 
ATOM   1682 C CE2 . PHE A 1 208 ? 11.907  -3.382  24.584  1.00 33.29 ? 208 PHE A CE2 1 
ATOM   1683 C CZ  . PHE A 1 208 ? 12.589  -2.878  23.499  1.00 28.79 ? 208 PHE A CZ  1 
ATOM   1684 N N   . SER A 1 209 ? 5.460   -2.357  23.730  1.00 25.73 ? 209 SER A N   1 
ATOM   1685 C CA  . SER A 1 209 ? 4.051   -2.736  23.744  1.00 30.48 ? 209 SER A CA  1 
ATOM   1686 C C   . SER A 1 209 ? 3.196   -1.779  22.912  1.00 28.40 ? 209 SER A C   1 
ATOM   1687 O O   . SER A 1 209 ? 2.193   -2.202  22.313  1.00 29.52 ? 209 SER A O   1 
ATOM   1688 C CB  . SER A 1 209 ? 3.567   -2.812  25.192  1.00 31.65 ? 209 SER A CB  1 
ATOM   1689 O OG  . SER A 1 209 ? 2.175   -2.652  25.245  1.00 42.74 ? 209 SER A OG  1 
ATOM   1690 N N   . CYS A 1 210 ? 3.587   -0.501  22.850  1.00 26.21 ? 210 CYS A N   1 
ATOM   1691 C CA  . CYS A 1 210 ? 2.861   0.496   22.060  1.00 27.70 ? 210 CYS A CA  1 
ATOM   1692 C C   . CYS A 1 210 ? 2.883   0.157   20.572  1.00 26.07 ? 210 CYS A C   1 
ATOM   1693 O O   . CYS A 1 210 ? 1.840   0.115   19.915  1.00 25.19 ? 210 CYS A O   1 
ATOM   1694 C CB  . CYS A 1 210 ? 3.454   1.893   22.307  1.00 28.03 ? 210 CYS A CB  1 
ATOM   1695 S SG  . CYS A 1 210 ? 2.718   3.218   21.290  1.00 28.79 ? 210 CYS A SG  1 
ATOM   1696 N N   . LEU A 1 211 ? 4.073   -0.091  20.012  1.00 26.92 ? 211 LEU A N   1 
ATOM   1697 C CA  . LEU A 1 211 ? 4.136   -0.498  18.608  1.00 24.05 ? 211 LEU A CA  1 
ATOM   1698 C C   . LEU A 1 211 ? 3.561   -1.901  18.394  1.00 24.33 ? 211 LEU A C   1 
ATOM   1699 O O   . LEU A 1 211 ? 2.813   -2.120  17.431  1.00 22.12 ? 211 LEU A O   1 
ATOM   1700 C CB  . LEU A 1 211 ? 5.587   -0.440  18.104  1.00 22.91 ? 211 LEU A CB  1 
ATOM   1701 C CG  . LEU A 1 211 ? 5.726   -0.494  16.586  1.00 24.18 ? 211 LEU A CG  1 
ATOM   1702 C CD1 . LEU A 1 211 ? 4.989   0.666   15.944  1.00 22.85 ? 211 LEU A CD1 1 
ATOM   1703 C CD2 . LEU A 1 211 ? 7.215   -0.527  16.182  1.00 22.93 ? 211 LEU A CD2 1 
ATOM   1704 N N   . ASP A 1 212 ? 3.917   -2.866  19.261  1.00 23.75 ? 212 ASP A N   1 
ATOM   1705 C CA  . ASP A 1 212 ? 3.459   -4.254  19.084  1.00 25.10 ? 212 ASP A CA  1 
ATOM   1706 C C   . ASP A 1 212 ? 1.940   -4.341  18.951  1.00 25.90 ? 212 ASP A C   1 
ATOM   1707 O O   . ASP A 1 212 ? 1.411   -5.093  18.107  1.00 22.68 ? 212 ASP A O   1 
ATOM   1708 C CB  . ASP A 1 212 ? 3.897   -5.138  20.265  1.00 25.07 ? 212 ASP A CB  1 
ATOM   1709 C CG  . ASP A 1 212 ? 5.403   -5.378  20.317  1.00 29.40 ? 212 ASP A CG  1 
ATOM   1710 O OD1 . ASP A 1 212 ? 6.114   -5.137  19.302  1.00 26.46 ? 212 ASP A OD1 1 
ATOM   1711 O OD2 . ASP A 1 212 ? 5.881   -5.823  21.383  1.00 27.44 ? 212 ASP A OD2 1 
ATOM   1712 N N   . ASN A 1 213 ? 1.218   -3.592  19.779  1.00 24.54 ? 213 ASN A N   1 
ATOM   1713 C CA  . ASN A 1 213 ? -0.234  -3.702  19.850  1.00 25.52 ? 213 ASN A CA  1 
ATOM   1714 C C   . ASN A 1 213 ? -0.939  -2.722  18.935  1.00 27.70 ? 213 ASN A C   1 
ATOM   1715 O O   . ASN A 1 213 ? -2.167  -2.603  19.007  1.00 25.14 ? 213 ASN A O   1 
ATOM   1716 C CB  . ASN A 1 213 ? -0.723  -3.451  21.289  1.00 25.89 ? 213 ASN A CB  1 
ATOM   1717 C CG  . ASN A 1 213 ? -0.565  -4.667  22.173  1.00 28.17 ? 213 ASN A CG  1 
ATOM   1718 O OD1 . ASN A 1 213 ? -1.365  -5.606  22.088  1.00 26.72 ? 213 ASN A OD1 1 
ATOM   1719 N ND2 . ASN A 1 213 ? 0.502   -4.693  22.973  1.00 27.73 ? 213 ASN A ND2 1 
ATOM   1720 N N   . ALA A 1 214 ? -0.193  -1.984  18.112  1.00 24.75 ? 214 ALA A N   1 
ATOM   1721 C CA  . ALA A 1 214 ? -0.784  -0.906  17.339  1.00 27.52 ? 214 ALA A CA  1 
ATOM   1722 C C   . ALA A 1 214 ? -1.223  -1.338  15.959  1.00 27.18 ? 214 ALA A C   1 
ATOM   1723 O O   . ALA A 1 214 ? -1.400  -0.480  15.081  1.00 28.34 ? 214 ALA A O   1 
ATOM   1724 C CB  . ALA A 1 214 ? 0.208   0.258   17.228  1.00 23.64 ? 214 ALA A CB  1 
ATOM   1725 N N   . ASN A 1 215 ? -1.423  -2.636  15.746  1.00 22.48 ? 215 ASN A N   1 
ATOM   1726 C CA  . ASN A 1 215 ? -1.880  -3.105  14.448  1.00 23.93 ? 215 ASN A CA  1 
ATOM   1727 C C   . ASN A 1 215 ? -3.065  -4.053  14.617  1.00 26.93 ? 215 ASN A C   1 
ATOM   1728 O O   . ASN A 1 215 ? -3.239  -4.982  13.828  1.00 26.12 ? 215 ASN A O   1 
ATOM   1729 C CB  . ASN A 1 215 ? -0.731  -3.780  13.684  1.00 25.50 ? 215 ASN A CB  1 
ATOM   1730 C CG  . ASN A 1 215 ? -0.806  -3.542  12.181  1.00 27.86 ? 215 ASN A CG  1 
ATOM   1731 O OD1 . ASN A 1 215 ? -1.247  -2.463  11.733  1.00 27.24 ? 215 ASN A OD1 1 
ATOM   1732 N ND2 . ASN A 1 215 ? -0.395  -4.541  11.392  1.00 22.21 ? 215 ASN A ND2 1 
ATOM   1733 N N   . LYS A 1 216 ? -3.934  -3.775  15.595  1.00 28.83 ? 216 LYS A N   1 
ATOM   1734 C CA  . LYS A 1 216 ? -5.104  -4.626  15.840  1.00 25.66 ? 216 LYS A CA  1 
ATOM   1735 C C   . LYS A 1 216 ? -6.008  -4.612  14.615  1.00 26.85 ? 216 LYS A C   1 
ATOM   1736 O O   . LYS A 1 216 ? -6.263  -3.557  14.028  1.00 27.60 ? 216 LYS A O   1 
ATOM   1737 C CB  . LYS A 1 216 ? -5.863  -4.137  17.081  1.00 28.54 ? 216 LYS A CB  1 
ATOM   1738 C CG  . LYS A 1 216 ? -6.974  -5.114  17.543  1.00 37.92 ? 216 LYS A CG  1 
ATOM   1739 C CD  . LYS A 1 216 ? -6.721  -5.674  18.961  1.00 36.85 ? 216 LYS A CD  1 
ATOM   1740 C CE  . LYS A 1 216 ? -7.815  -6.679  19.363  1.00 40.08 ? 216 LYS A CE  1 
ATOM   1741 N NZ  . LYS A 1 216 ? -9.157  -6.175  18.889  1.00 46.53 ? 216 LYS A NZ  1 
ATOM   1742 N N   . GLY A 1 217 ? -6.429  -5.794  14.180  1.00 28.84 ? 217 GLY A N   1 
ATOM   1743 C CA  . GLY A 1 217 ? -7.223  -5.942  12.976  1.00 28.97 ? 217 GLY A CA  1 
ATOM   1744 C C   . GLY A 1 217 ? -6.413  -6.209  11.727  1.00 34.10 ? 217 GLY A C   1 
ATOM   1745 O O   . GLY A 1 217 ? -6.990  -6.550  10.685  1.00 28.61 ? 217 GLY A O   1 
ATOM   1746 N N   . TYR A 1 218 ? -5.088  -6.105  11.811  1.00 30.35 ? 218 TYR A N   1 
ATOM   1747 C CA  . TYR A 1 218 ? -4.209  -6.263  10.667  1.00 29.84 ? 218 TYR A CA  1 
ATOM   1748 C C   . TYR A 1 218 ? -3.125  -7.275  11.015  1.00 26.36 ? 218 TYR A C   1 
ATOM   1749 O O   . TYR A 1 218 ? -3.015  -7.745  12.156  1.00 27.71 ? 218 TYR A O   1 
ATOM   1750 C CB  . TYR A 1 218 ? -3.620  -4.900  10.258  1.00 27.28 ? 218 TYR A CB  1 
ATOM   1751 C CG  . TYR A 1 218 ? -4.692  -3.892  9.892   1.00 30.82 ? 218 TYR A CG  1 
ATOM   1752 C CD1 . TYR A 1 218 ? -5.324  -3.137  10.868  1.00 31.23 ? 218 TYR A CD1 1 
ATOM   1753 C CD2 . TYR A 1 218 ? -5.100  -3.729  8.576   1.00 32.82 ? 218 TYR A CD2 1 
ATOM   1754 C CE1 . TYR A 1 218 ? -6.310  -2.226  10.549  1.00 33.85 ? 218 TYR A CE1 1 
ATOM   1755 C CE2 . TYR A 1 218 ? -6.089  -2.805  8.239   1.00 33.98 ? 218 TYR A CE2 1 
ATOM   1756 C CZ  . TYR A 1 218 ? -6.692  -2.070  9.236   1.00 37.06 ? 218 TYR A CZ  1 
ATOM   1757 O OH  . TYR A 1 218 ? -7.680  -1.162  8.934   1.00 40.47 ? 218 TYR A OH  1 
ATOM   1758 N N   . ARG A 1 219 ? -2.305  -7.586  10.019  1.00 27.73 ? 219 ARG A N   1 
ATOM   1759 C CA  . ARG A 1 219 ? -1.365  -8.702  10.112  1.00 27.00 ? 219 ARG A CA  1 
ATOM   1760 C C   . ARG A 1 219 ? -0.386  -8.525  11.268  1.00 27.48 ? 219 ARG A C   1 
ATOM   1761 O O   . ARG A 1 219 ? 0.244   -7.469  11.425  1.00 27.43 ? 219 ARG A O   1 
ATOM   1762 C CB  . ARG A 1 219 ? -0.622  -8.840  8.795   1.00 28.89 ? 219 ARG A CB  1 
ATOM   1763 C CG  . ARG A 1 219 ? 0.294   -10.016 8.735   1.00 26.67 ? 219 ARG A CG  1 
ATOM   1764 C CD  . ARG A 1 219 ? 0.842   -10.159 7.317   1.00 28.42 ? 219 ARG A CD  1 
ATOM   1765 N NE  . ARG A 1 219 ? 1.858   -11.200 7.242   1.00 33.01 ? 219 ARG A NE  1 
ATOM   1766 C CZ  . ARG A 1 219 ? 2.228   -11.804 6.120   1.00 32.39 ? 219 ARG A CZ  1 
ATOM   1767 N NH1 . ARG A 1 219 ? 1.689   -11.486 4.951   1.00 29.17 ? 219 ARG A NH1 1 
ATOM   1768 N NH2 . ARG A 1 219 ? 3.175   -12.728 6.169   1.00 28.92 ? 219 ARG A NH2 1 
ATOM   1769 N N   . GLN A 1 220 ? -0.242  -9.571  12.068  1.00 22.99 ? 220 GLN A N   1 
ATOM   1770 C CA  . GLN A 1 220 ? 0.563   -9.508  13.289  1.00 23.73 ? 220 GLN A CA  1 
ATOM   1771 C C   . GLN A 1 220 ? 2.014   -9.920  13.035  1.00 28.07 ? 220 GLN A C   1 
ATOM   1772 O O   . GLN A 1 220 ? 2.512   -10.903 13.587  1.00 24.41 ? 220 GLN A O   1 
ATOM   1773 C CB  . GLN A 1 220 ? -0.066  -10.376 14.379  1.00 22.67 ? 220 GLN A CB  1 
ATOM   1774 C CG  . GLN A 1 220 ? -1.435  -9.822  14.837  1.00 22.82 ? 220 GLN A CG  1 
ATOM   1775 C CD  . GLN A 1 220 ? -1.292  -8.484  15.514  1.00 26.00 ? 220 GLN A CD  1 
ATOM   1776 O OE1 . GLN A 1 220 ? -0.659  -8.375  16.566  1.00 27.52 ? 220 GLN A OE1 1 
ATOM   1777 N NE2 . GLN A 1 220 ? -1.881  -7.446  14.916  1.00 23.56 ? 220 GLN A NE2 1 
ATOM   1778 N N   . ASN A 1 221 ? 2.711   -9.124  12.210  1.00 26.25 ? 221 ASN A N   1 
ATOM   1779 C CA  . ASN A 1 221 ? 4.115   -9.359  11.931  1.00 23.74 ? 221 ASN A CA  1 
ATOM   1780 C C   . ASN A 1 221 ? 4.862   -8.034  11.862  1.00 25.31 ? 221 ASN A C   1 
ATOM   1781 O O   . ASN A 1 221 ? 4.267   -6.968  11.687  1.00 23.53 ? 221 ASN A O   1 
ATOM   1782 C CB  . ASN A 1 221 ? 4.345   -10.109 10.602  1.00 26.39 ? 221 ASN A CB  1 
ATOM   1783 C CG  . ASN A 1 221 ? 3.841   -11.577 10.628  1.00 27.77 ? 221 ASN A CG  1 
ATOM   1784 O OD1 . ASN A 1 221 ? 2.926   -11.942 9.881   1.00 27.75 ? 221 ASN A OD1 1 
ATOM   1785 N ND2 . ASN A 1 221 ? 4.466   -12.409 11.455  1.00 24.69 ? 221 ASN A ND2 1 
ATOM   1786 N N   . TYR A 1 222 ? 6.173   -8.131  12.058  1.00 24.72 ? 222 TYR A N   1 
ATOM   1787 C CA  . TYR A 1 222 ? 7.188   -7.221  11.531  1.00 25.19 ? 222 TYR A CA  1 
ATOM   1788 C C   . TYR A 1 222 ? 7.922   -7.945  10.408  1.00 26.12 ? 222 TYR A C   1 
ATOM   1789 O O   . TYR A 1 222 ? 7.772   -9.157  10.214  1.00 24.60 ? 222 TYR A O   1 
ATOM   1790 C CB  . TYR A 1 222 ? 8.168   -6.782  12.624  1.00 24.99 ? 222 TYR A CB  1 
ATOM   1791 C CG  . TYR A 1 222 ? 7.540   -5.990  13.744  1.00 22.51 ? 222 TYR A CG  1 
ATOM   1792 C CD1 . TYR A 1 222 ? 6.515   -5.088  13.498  1.00 22.88 ? 222 TYR A CD1 1 
ATOM   1793 C CD2 . TYR A 1 222 ? 7.963   -6.167  15.053  1.00 24.29 ? 222 TYR A CD2 1 
ATOM   1794 C CE1 . TYR A 1 222 ? 5.920   -4.371  14.550  1.00 23.54 ? 222 TYR A CE1 1 
ATOM   1795 C CE2 . TYR A 1 222 ? 7.402   -5.450  16.096  1.00 25.24 ? 222 TYR A CE2 1 
ATOM   1796 C CZ  . TYR A 1 222 ? 6.381   -4.568  15.843  1.00 24.58 ? 222 TYR A CZ  1 
ATOM   1797 O OH  . TYR A 1 222 ? 5.851   -3.905  16.929  1.00 23.38 ? 222 TYR A OH  1 
ATOM   1798 N N   . TYR A 1 223 ? 8.746   -7.212  9.665   1.00 24.47 ? 223 TYR A N   1 
ATOM   1799 C CA  . TYR A 1 223 ? 9.304   -7.724  8.409   1.00 24.89 ? 223 TYR A CA  1 
ATOM   1800 C C   . TYR A 1 223 ? 10.811  -7.487  8.354   1.00 24.66 ? 223 TYR A C   1 
ATOM   1801 O O   . TYR A 1 223 ? 11.274  -6.388  8.048   1.00 22.91 ? 223 TYR A O   1 
ATOM   1802 C CB  . TYR A 1 223 ? 8.569   -7.090  7.218   1.00 22.86 ? 223 TYR A CB  1 
ATOM   1803 C CG  . TYR A 1 223 ? 7.079   -7.269  7.402   1.00 22.84 ? 223 TYR A CG  1 
ATOM   1804 C CD1 . TYR A 1 223 ? 6.479   -8.494  7.088   1.00 25.68 ? 223 TYR A CD1 1 
ATOM   1805 C CD2 . TYR A 1 223 ? 6.289   -6.267  7.941   1.00 21.17 ? 223 TYR A CD2 1 
ATOM   1806 C CE1 . TYR A 1 223 ? 5.124   -8.714  7.291   1.00 24.85 ? 223 TYR A CE1 1 
ATOM   1807 C CE2 . TYR A 1 223 ? 4.904   -6.478  8.169   1.00 23.19 ? 223 TYR A CE2 1 
ATOM   1808 C CZ  . TYR A 1 223 ? 4.333   -7.700  7.831   1.00 23.02 ? 223 TYR A CZ  1 
ATOM   1809 O OH  . TYR A 1 223 ? 2.991   -7.939  8.031   1.00 24.86 ? 223 TYR A OH  1 
ATOM   1810 N N   . VAL A 1 224 ? 11.586  -8.534  8.619   1.00 25.62 ? 224 VAL A N   1 
ATOM   1811 C CA  . VAL A 1 224 ? 13.030  -8.390  8.568   1.00 24.42 ? 224 VAL A CA  1 
ATOM   1812 C C   . VAL A 1 224 ? 13.465  -8.259  7.114   1.00 23.95 ? 224 VAL A C   1 
ATOM   1813 O O   . VAL A 1 224 ? 12.986  -8.984  6.236   1.00 23.27 ? 224 VAL A O   1 
ATOM   1814 C CB  . VAL A 1 224 ? 13.712  -9.606  9.218   1.00 26.90 ? 224 VAL A CB  1 
ATOM   1815 C CG1 . VAL A 1 224 ? 15.227  -9.520  8.995   1.00 28.01 ? 224 VAL A CG1 1 
ATOM   1816 C CG2 . VAL A 1 224 ? 13.364  -9.709  10.697  1.00 25.09 ? 224 VAL A CG2 1 
ATOM   1817 N N   . VAL A 1 225 ? 14.380  -7.332  6.836   1.00 25.83 ? 225 VAL A N   1 
ATOM   1818 C CA  . VAL A 1 225 ? 14.930  -7.199  5.493   1.00 24.77 ? 225 VAL A CA  1 
ATOM   1819 C C   . VAL A 1 225 ? 16.331  -7.801  5.514   1.00 25.92 ? 225 VAL A C   1 
ATOM   1820 O O   . VAL A 1 225 ? 17.166  -7.417  6.343   1.00 23.84 ? 225 VAL A O   1 
ATOM   1821 C CB  . VAL A 1 225 ? 14.942  -5.735  5.026   1.00 23.43 ? 225 VAL A CB  1 
ATOM   1822 C CG1 . VAL A 1 225 ? 15.318  -5.667  3.559   1.00 22.75 ? 225 VAL A CG1 1 
ATOM   1823 C CG2 . VAL A 1 225 ? 13.559  -5.084  5.240   1.00 22.90 ? 225 VAL A CG2 1 
ATOM   1824 N N   . CYS A 1 226 ? 16.594  -8.772  4.646   1.00 29.15 ? 226 CYS A N   1 
ATOM   1825 C CA  . CYS A 1 226 ? 17.940  -9.319  4.560   1.00 29.92 ? 226 CYS A CA  1 
ATOM   1826 C C   . CYS A 1 226 ? 18.328  -9.582  3.112   1.00 27.76 ? 226 CYS A C   1 
ATOM   1827 O O   . CYS A 1 226 ? 17.474  -9.571  2.214   1.00 25.83 ? 226 CYS A O   1 
ATOM   1828 C CB  . CYS A 1 226 ? 18.068  -10.603 5.386   1.00 35.14 ? 226 CYS A CB  1 
ATOM   1829 S SG  . CYS A 1 226 ? 16.974  -11.858 4.857   1.00 39.42 ? 226 CYS A SG  1 
ATOM   1830 N N   . PRO A 1 227 ? 19.624  -9.796  2.849   1.00 28.65 ? 227 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 227 ? 20.049  -10.112 1.481   1.00 29.47 ? 227 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 227 ? 19.468  -11.441 1.039   1.00 31.23 ? 227 PRO A C   1 
ATOM   1833 O O   . PRO A 1 227 ? 19.464  -12.414 1.789   1.00 33.51 ? 227 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 227 ? 21.581  -10.173 1.587   1.00 30.63 ? 227 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 227 ? 21.913  -9.379  2.822   1.00 29.25 ? 227 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 227 ? 20.774  -9.647  3.759   1.00 28.78 ? 227 PRO A CD  1 
ATOM   1837 N N   . ALA A 1 228 ? 19.003  -11.486 -0.199  1.00 30.67 ? 228 ALA A N   1 
ATOM   1838 C CA  . ALA A 1 228 ? 18.411  -12.708 -0.726  1.00 32.72 ? 228 ALA A CA  1 
ATOM   1839 C C   . ALA A 1 228 ? 19.517  -13.678 -1.132  1.00 38.91 ? 228 ALA A C   1 
ATOM   1840 O O   . ALA A 1 228 ? 20.572  -13.224 -1.587  1.00 41.11 ? 228 ALA A O   1 
ATOM   1841 C CB  . ALA A 1 228 ? 17.543  -12.388 -1.913  1.00 34.26 ? 228 ALA A CB  1 
ATOM   1842 N N   . MET B 1 1   ? 42.515  17.215  -39.971 1.00 59.05 ? 1   MET B N   1 
ATOM   1843 C CA  . MET B 1 1   ? 43.744  17.061  -40.799 1.00 57.49 ? 1   MET B CA  1 
ATOM   1844 C C   . MET B 1 1   ? 43.590  15.951  -41.860 1.00 52.02 ? 1   MET B C   1 
ATOM   1845 O O   . MET B 1 1   ? 43.760  16.279  -43.010 1.00 57.43 ? 1   MET B O   1 
ATOM   1846 C CB  . MET B 1 1   ? 44.993  16.881  -39.921 1.00 59.80 ? 1   MET B CB  1 
ATOM   1847 C CG  . MET B 1 1   ? 46.295  16.663  -40.676 1.00 63.29 ? 1   MET B CG  1 
ATOM   1848 S SD  . MET B 1 1   ? 47.274  18.144  -41.081 1.00 82.21 ? 1   MET B SD  1 
ATOM   1849 C CE  . MET B 1 1   ? 48.140  17.588  -42.550 1.00 60.40 ? 1   MET B CE  1 
ATOM   1850 N N   . VAL B 1 2   ? 43.194  14.732  -41.494 1.00 49.65 ? 2   VAL B N   1 
ATOM   1851 C CA  . VAL B 1 2   ? 43.101  13.568  -42.432 1.00 44.18 ? 2   VAL B CA  1 
ATOM   1852 C C   . VAL B 1 2   ? 41.751  13.584  -43.161 1.00 39.55 ? 2   VAL B C   1 
ATOM   1853 O O   . VAL B 1 2   ? 40.775  13.828  -42.473 1.00 38.39 ? 2   VAL B O   1 
ATOM   1854 C CB  . VAL B 1 2   ? 43.248  12.282  -41.603 1.00 44.28 ? 2   VAL B CB  1 
ATOM   1855 C CG1 . VAL B 1 2   ? 43.080  11.034  -42.425 1.00 42.58 ? 2   VAL B CG1 1 
ATOM   1856 C CG2 . VAL B 1 2   ? 44.538  12.250  -40.810 1.00 48.98 ? 2   VAL B CG2 1 
ATOM   1857 N N   . ARG B 1 3   ? 41.700  13.277  -44.470 1.00 36.97 ? 3   ARG B N   1 
ATOM   1858 C CA  . ARG B 1 3   ? 40.461  13.309  -45.209 1.00 36.51 ? 3   ARG B CA  1 
ATOM   1859 C C   . ARG B 1 3   ? 40.283  11.945  -45.838 1.00 37.33 ? 3   ARG B C   1 
ATOM   1860 O O   . ARG B 1 3   ? 41.265  11.269  -46.184 1.00 34.13 ? 3   ARG B O   1 
ATOM   1861 C CB  . ARG B 1 3   ? 40.493  14.403  -46.280 1.00 39.72 ? 3   ARG B CB  1 
ATOM   1862 C CG  . ARG B 1 3   ? 41.414  15.546  -45.914 1.00 45.63 ? 3   ARG B CG  1 
ATOM   1863 C CD  . ARG B 1 3   ? 41.345  16.670  -46.924 1.00 46.89 ? 3   ARG B CD  1 
ATOM   1864 N NE  . ARG B 1 3   ? 41.961  16.292  -48.193 1.00 49.80 ? 3   ARG B NE  1 
ATOM   1865 C CZ  . ARG B 1 3   ? 41.879  17.020  -49.299 1.00 53.16 ? 3   ARG B CZ  1 
ATOM   1866 N NH1 . ARG B 1 3   ? 41.114  18.103  -49.355 1.00 48.32 ? 3   ARG B NH1 1 
ATOM   1867 N NH2 . ARG B 1 3   ? 42.578  16.653  -50.375 1.00 49.23 ? 3   ARG B NH2 1 
ATOM   1868 N N   . PHE B 1 4   ? 39.028  11.531  -45.965 1.00 31.68 ? 4   PHE B N   1 
ATOM   1869 C CA  . PHE B 1 4   ? 38.720  10.248  -46.563 1.00 28.56 ? 4   PHE B CA  1 
ATOM   1870 C C   . PHE B 1 4   ? 37.756  10.481  -47.713 1.00 29.04 ? 4   PHE B C   1 
ATOM   1871 O O   . PHE B 1 4   ? 36.755  11.190  -47.566 1.00 30.79 ? 4   PHE B O   1 
ATOM   1872 C CB  . PHE B 1 4   ? 38.145  9.301   -45.508 1.00 27.74 ? 4   PHE B CB  1 
ATOM   1873 C CG  . PHE B 1 4   ? 39.121  8.982   -44.421 1.00 26.76 ? 4   PHE B CG  1 
ATOM   1874 C CD1 . PHE B 1 4   ? 40.146  8.062   -44.647 1.00 29.45 ? 4   PHE B CD1 1 
ATOM   1875 C CD2 . PHE B 1 4   ? 39.057  9.629   -43.192 1.00 27.11 ? 4   PHE B CD2 1 
ATOM   1876 C CE1 . PHE B 1 4   ? 41.066  7.763   -43.661 1.00 30.28 ? 4   PHE B CE1 1 
ATOM   1877 C CE2 . PHE B 1 4   ? 39.990  9.344   -42.194 1.00 31.65 ? 4   PHE B CE2 1 
ATOM   1878 C CZ  . PHE B 1 4   ? 41.003  8.393   -42.436 1.00 29.94 ? 4   PHE B CZ  1 
ATOM   1879 N N   . SER B 1 5   ? 38.053  9.885   -48.855 1.00 28.71 ? 5   SER B N   1 
ATOM   1880 C CA  . SER B 1 5   ? 37.276  10.131  -50.058 1.00 31.23 ? 5   SER B CA  1 
ATOM   1881 C C   . SER B 1 5   ? 35.920  9.426   -49.985 1.00 31.16 ? 5   SER B C   1 
ATOM   1882 O O   . SER B 1 5   ? 35.673  8.579   -49.133 1.00 28.65 ? 5   SER B O   1 
ATOM   1883 C CB  . SER B 1 5   ? 38.045  9.629   -51.287 1.00 36.47 ? 5   SER B CB  1 
ATOM   1884 O OG  . SER B 1 5   ? 38.028  8.198   -51.303 1.00 34.11 ? 5   SER B OG  1 
ATOM   1885 N N   . ARG B 1 6   ? 35.041  9.784   -50.919 1.00 30.03 ? 6   ARG B N   1 
ATOM   1886 C CA  . ARG B 1 6   ? 33.742  9.133   -51.003 1.00 30.78 ? 6   ARG B CA  1 
ATOM   1887 C C   . ARG B 1 6   ? 33.887  7.642   -51.255 1.00 34.27 ? 6   ARG B C   1 
ATOM   1888 O O   . ARG B 1 6   ? 33.199  6.828   -50.632 1.00 29.67 ? 6   ARG B O   1 
ATOM   1889 C CB  . ARG B 1 6   ? 32.919  9.766   -52.116 1.00 34.61 ? 6   ARG B CB  1 
ATOM   1890 C CG  . ARG B 1 6   ? 31.511  9.222   -52.202 1.00 35.85 ? 6   ARG B CG  1 
ATOM   1891 C CD  . ARG B 1 6   ? 30.817  9.781   -53.424 1.00 38.58 ? 6   ARG B CD  1 
ATOM   1892 N NE  . ARG B 1 6   ? 31.586  9.507   -54.630 1.00 47.00 ? 6   ARG B NE  1 
ATOM   1893 C CZ  . ARG B 1 6   ? 31.367  10.074  -55.809 1.00 52.11 ? 6   ARG B CZ  1 
ATOM   1894 N NH1 . ARG B 1 6   ? 30.462  11.031  -55.960 1.00 52.79 ? 6   ARG B NH1 1 
ATOM   1895 N NH2 . ARG B 1 6   ? 32.083  9.681   -56.859 1.00 50.68 ? 6   ARG B NH2 1 
ATOM   1896 N N   . ASP B 1 7   ? 34.788  7.261   -52.160 1.00 32.28 ? 7   ASP B N   1 
ATOM   1897 C CA  . ASP B 1 7   ? 34.997  5.839   -52.428 1.00 37.51 ? 7   ASP B CA  1 
ATOM   1898 C C   . ASP B 1 7   ? 35.403  5.099   -51.162 1.00 30.39 ? 7   ASP B C   1 
ATOM   1899 O O   . ASP B 1 7   ? 34.878  4.014   -50.870 1.00 32.25 ? 7   ASP B O   1 
ATOM   1900 C CB  . ASP B 1 7   ? 36.060  5.682   -53.521 1.00 36.52 ? 7   ASP B CB  1 
ATOM   1901 C CG  . ASP B 1 7   ? 35.462  5.731   -54.917 1.00 45.74 ? 7   ASP B CG  1 
ATOM   1902 O OD1 . ASP B 1 7   ? 34.283  6.149   -55.040 1.00 46.76 ? 7   ASP B OD1 1 
ATOM   1903 O OD2 . ASP B 1 7   ? 36.136  5.316   -55.886 1.00 49.24 ? 7   ASP B OD2 1 
ATOM   1904 N N   . MET B 1 8   ? 36.321  5.685   -50.389 1.00 26.78 ? 8   MET B N   1 
ATOM   1905 C CA  . MET B 1 8   ? 36.743  5.094   -49.122 1.00 24.31 ? 8   MET B CA  1 
ATOM   1906 C C   . MET B 1 8   ? 35.590  5.025   -48.125 1.00 30.39 ? 8   MET B C   1 
ATOM   1907 O O   . MET B 1 8   ? 35.471  4.056   -47.366 1.00 30.09 ? 8   MET B O   1 
ATOM   1908 C CB  . MET B 1 8   ? 37.864  5.930   -48.521 1.00 24.85 ? 8   MET B CB  1 
ATOM   1909 C CG  . MET B 1 8   ? 38.669  5.319   -47.385 1.00 29.42 ? 8   MET B CG  1 
ATOM   1910 S SD  . MET B 1 8   ? 39.455  3.706   -47.682 1.00 34.23 ? 8   MET B SD  1 
ATOM   1911 C CE  . MET B 1 8   ? 38.180  2.549   -47.241 1.00 33.07 ? 8   MET B CE  1 
ATOM   1912 N N   . LEU B 1 9   ? 34.760  6.073   -48.075 1.00 26.37 ? 9   LEU B N   1 
ATOM   1913 C CA  . LEU B 1 9   ? 33.646  6.085   -47.132 1.00 28.83 ? 9   LEU B CA  1 
ATOM   1914 C C   . LEU B 1 9   ? 32.636  4.998   -47.462 1.00 28.61 ? 9   LEU B C   1 
ATOM   1915 O O   . LEU B 1 9   ? 32.145  4.300   -46.557 1.00 30.88 ? 9   LEU B O   1 
ATOM   1916 C CB  . LEU B 1 9   ? 32.979  7.457   -47.137 1.00 28.63 ? 9   LEU B CB  1 
ATOM   1917 C CG  . LEU B 1 9   ? 33.866  8.563   -46.577 1.00 26.91 ? 9   LEU B CG  1 
ATOM   1918 C CD1 . LEU B 1 9   ? 33.375  9.941   -47.035 1.00 31.61 ? 9   LEU B CD1 1 
ATOM   1919 C CD2 . LEU B 1 9   ? 33.967  8.468   -45.063 1.00 28.82 ? 9   LEU B CD2 1 
ATOM   1920 N N   . GLN B 1 10  ? 32.319  4.828   -48.749 1.00 27.90 ? 10  GLN B N   1 
ATOM   1921 C CA  . GLN B 1 10  ? 31.394  3.769   -49.148 1.00 31.57 ? 10  GLN B CA  1 
ATOM   1922 C C   . GLN B 1 10  ? 31.949  2.396   -48.797 1.00 32.38 ? 10  GLN B C   1 
ATOM   1923 O O   . GLN B 1 10  ? 31.206  1.505   -48.356 1.00 33.13 ? 10  GLN B O   1 
ATOM   1924 C CB  . GLN B 1 10  ? 31.109  3.860   -50.643 1.00 31.94 ? 10  GLN B CB  1 
ATOM   1925 C CG  . GLN B 1 10  ? 30.421  5.140   -51.069 1.00 35.63 ? 10  GLN B CG  1 
ATOM   1926 C CD  . GLN B 1 10  ? 30.292  5.258   -52.586 1.00 41.12 ? 10  GLN B CD  1 
ATOM   1927 O OE1 . GLN B 1 10  ? 29.656  6.178   -53.111 1.00 41.50 ? 10  GLN B OE1 1 
ATOM   1928 N NE2 . GLN B 1 10  ? 30.904  4.329   -53.295 1.00 39.15 ? 10  GLN B NE2 1 
ATOM   1929 N N   . ASP B 1 11  ? 33.250  2.189   -49.033 1.00 30.65 ? 11  ASP B N   1 
ATOM   1930 C CA  . ASP B 1 11  ? 33.880  0.902   -48.741 1.00 31.07 ? 11  ASP B CA  1 
ATOM   1931 C C   . ASP B 1 11  ? 33.905  0.611   -47.249 1.00 31.53 ? 11  ASP B C   1 
ATOM   1932 O O   . ASP B 1 11  ? 33.575  -0.506  -46.816 1.00 28.57 ? 11  ASP B O   1 
ATOM   1933 C CB  . ASP B 1 11  ? 35.311  0.884   -49.297 1.00 29.37 ? 11  ASP B CB  1 
ATOM   1934 C CG  . ASP B 1 11  ? 36.043  -0.413  -48.972 1.00 33.39 ? 11  ASP B CG  1 
ATOM   1935 O OD1 . ASP B 1 11  ? 35.804  -1.434  -49.634 1.00 33.84 ? 11  ASP B OD1 1 
ATOM   1936 O OD2 . ASP B 1 11  ? 36.812  -0.433  -47.995 1.00 32.99 ? 11  ASP B OD2 1 
ATOM   1937 N N   . GLY B 1 12  ? 34.186  1.631   -46.455 1.00 29.75 ? 12  GLY B N   1 
ATOM   1938 C CA  . GLY B 1 12  ? 34.174  1.443   -45.001 1.00 25.90 ? 12  GLY B CA  1 
ATOM   1939 C C   . GLY B 1 12  ? 32.773  1.136   -44.501 1.00 31.03 ? 12  GLY B C   1 
ATOM   1940 O O   . GLY B 1 12  ? 32.645  0.342   -43.612 1.00 26.95 ? 12  GLY B O   1 
ATOM   1941 N N   . ALA B 1 13  ? 31.763  1.787   -45.064 1.00 26.74 ? 13  ALA B N   1 
ATOM   1942 C CA  . ALA B 1 13  ? 30.368  1.563   -44.627 1.00 32.35 ? 13  ALA B CA  1 
ATOM   1943 C C   . ALA B 1 13  ? 29.963  0.125   -44.962 1.00 33.20 ? 13  ALA B C   1 
ATOM   1944 O O   . ALA B 1 13  ? 29.338  -0.518  -44.136 1.00 31.58 ? 13  ALA B O   1 
ATOM   1945 C CB  . ALA B 1 13  ? 29.457  2.556   -45.288 1.00 29.80 ? 13  ALA B CB  1 
ATOM   1946 N N   . LYS B 1 14  ? 30.337  -0.339  -46.149 1.00 38.89 ? 14  LYS B N   1 
ATOM   1947 C CA  . LYS B 1 14  ? 30.040  -1.729  -46.560 1.00 35.72 ? 14  LYS B CA  1 
ATOM   1948 C C   . LYS B 1 14  ? 30.639  -2.683  -45.536 1.00 34.42 ? 14  LYS B C   1 
ATOM   1949 O O   . LYS B 1 14  ? 29.935  -3.556  -45.080 1.00 41.09 ? 14  LYS B O   1 
ATOM   1950 C CB  . LYS B 1 14  ? 30.607  -2.040  -47.941 1.00 49.75 ? 14  LYS B CB  1 
ATOM   1951 C CG  . LYS B 1 14  ? 29.933  -3.212  -48.636 1.00 47.01 ? 14  LYS B CG  1 
ATOM   1952 C CD  . LYS B 1 14  ? 29.066  -4.062  -47.707 1.00 45.88 ? 14  LYS B CD  1 
ATOM   1953 C CE  . LYS B 1 14  ? 27.617  -4.123  -48.144 1.00 49.38 ? 14  LYS B CE  1 
ATOM   1954 N NZ  . LYS B 1 14  ? 27.089  -2.788  -48.512 1.00 51.41 ? 14  LYS B NZ  1 
ATOM   1955 N N   . ARG B 1 15  ? 31.897  -2.468  -45.172 1.00 34.14 ? 15  ARG B N   1 
ATOM   1956 C CA  . ARG B 1 15  ? 32.574  -3.338  -44.189 1.00 32.42 ? 15  ARG B CA  1 
ATOM   1957 C C   . ARG B 1 15  ? 31.875  -3.250  -42.836 1.00 33.25 ? 15  ARG B C   1 
ATOM   1958 O O   . ARG B 1 15  ? 31.820  -4.273  -42.164 1.00 25.34 ? 15  ARG B O   1 
ATOM   1959 C CB  . ARG B 1 15  ? 34.051  -2.964  -44.082 1.00 31.68 ? 15  ARG B CB  1 
ATOM   1960 C CG  . ARG B 1 15  ? 34.913  -3.539  -45.192 1.00 29.16 ? 15  ARG B CG  1 
ATOM   1961 C CD  . ARG B 1 15  ? 36.367  -3.237  -44.934 1.00 28.50 ? 15  ARG B CD  1 
ATOM   1962 N NE  . ARG B 1 15  ? 36.705  -1.919  -45.419 1.00 26.92 ? 15  ARG B NE  1 
ATOM   1963 C CZ  . ARG B 1 15  ? 37.389  -1.043  -44.724 1.00 27.56 ? 15  ARG B CZ  1 
ATOM   1964 N NH1 . ARG B 1 15  ? 37.808  -1.348  -43.520 1.00 25.89 ? 15  ARG B NH1 1 
ATOM   1965 N NH2 . ARG B 1 15  ? 37.669  0.132   -45.236 1.00 31.07 ? 15  ARG B NH2 1 
ATOM   1966 N N   . MET B 1 16  ? 31.406  -2.066  -42.446 1.00 29.88 ? 16  MET B N   1 
ATOM   1967 C CA  . MET B 1 16  ? 30.724  -1.989  -41.156 1.00 30.10 ? 16  MET B CA  1 
ATOM   1968 C C   . MET B 1 16  ? 29.396  -2.714  -41.206 1.00 27.26 ? 16  MET B C   1 
ATOM   1969 O O   . MET B 1 16  ? 29.032  -3.412  -40.260 1.00 33.68 ? 16  MET B O   1 
ATOM   1970 C CB  . MET B 1 16  ? 30.500  -0.527  -40.751 1.00 27.44 ? 16  MET B CB  1 
ATOM   1971 C CG  . MET B 1 16  ? 31.780  0.236   -40.517 1.00 28.25 ? 16  MET B CG  1 
ATOM   1972 S SD  . MET B 1 16  ? 32.388  -0.170  -38.867 1.00 30.19 ? 16  MET B SD  1 
ATOM   1973 C CE  . MET B 1 16  ? 31.050  0.341   -37.806 1.00 31.87 ? 16  MET B CE  1 
ATOM   1974 N N   . PHE B 1 17  ? 28.669  -2.565  -42.314 1.00 31.11 ? 17  PHE B N   1 
ATOM   1975 C CA  . PHE B 1 17  ? 27.393  -3.246  -42.505 1.00 29.20 ? 17  PHE B CA  1 
ATOM   1976 C C   . PHE B 1 17  ? 27.580  -4.764  -42.467 1.00 31.89 ? 17  PHE B C   1 
ATOM   1977 O O   . PHE B 1 17  ? 26.868  -5.476  -41.753 1.00 31.21 ? 17  PHE B O   1 
ATOM   1978 C CB  . PHE B 1 17  ? 26.810  -2.782  -43.847 1.00 28.47 ? 17  PHE B CB  1 
ATOM   1979 C CG  . PHE B 1 17  ? 25.417  -3.249  -44.137 1.00 30.10 ? 17  PHE B CG  1 
ATOM   1980 C CD1 . PHE B 1 17  ? 24.385  -3.010  -43.246 1.00 28.71 ? 17  PHE B CD1 1 
ATOM   1981 C CD2 . PHE B 1 17  ? 25.131  -3.918  -45.331 1.00 33.01 ? 17  PHE B CD2 1 
ATOM   1982 C CE1 . PHE B 1 17  ? 23.069  -3.434  -43.533 1.00 30.88 ? 17  PHE B CE1 1 
ATOM   1983 C CE2 . PHE B 1 17  ? 23.828  -4.361  -45.620 1.00 34.44 ? 17  PHE B CE2 1 
ATOM   1984 C CZ  . PHE B 1 17  ? 22.801  -4.108  -44.727 1.00 32.44 ? 17  PHE B CZ  1 
ATOM   1985 N N   . LYS B 1 18  ? 28.569  -5.275  -43.200 1.00 30.64 ? 18  LYS B N   1 
ATOM   1986 C CA  . LYS B 1 18  ? 28.840  -6.713  -43.180 1.00 30.23 ? 18  LYS B CA  1 
ATOM   1987 C C   . LYS B 1 18  ? 29.270  -7.186  -41.796 1.00 30.13 ? 18  LYS B C   1 
ATOM   1988 O O   . LYS B 1 18  ? 28.881  -8.272  -41.362 1.00 35.37 ? 18  LYS B O   1 
ATOM   1989 C CB  . LYS B 1 18  ? 29.895  -7.063  -44.230 1.00 33.08 ? 18  LYS B CB  1 
ATOM   1990 C CG  . LYS B 1 18  ? 29.399  -7.076  -45.672 1.00 37.06 ? 18  LYS B CG  1 
ATOM   1991 C CD  . LYS B 1 18  ? 30.507  -7.571  -46.619 1.00 44.36 ? 18  LYS B CD  1 
ATOM   1992 C CE  . LYS B 1 18  ? 30.151  -7.439  -48.099 1.00 47.18 ? 18  LYS B CE  1 
ATOM   1993 N NZ  . LYS B 1 18  ? 29.022  -8.350  -48.486 1.00 56.52 ? 18  LYS B NZ  1 
ATOM   1994 N N   . TRP B 1 19  ? 30.058  -6.386  -41.079 1.00 29.72 ? 19  TRP B N   1 
ATOM   1995 C CA  . TRP B 1 19  ? 30.433  -6.757  -39.714 1.00 31.75 ? 19  TRP B CA  1 
ATOM   1996 C C   . TRP B 1 19  ? 29.214  -6.840  -38.795 1.00 34.96 ? 19  TRP B C   1 
ATOM   1997 O O   . TRP B 1 19  ? 29.097  -7.771  -37.981 1.00 33.11 ? 19  TRP B O   1 
ATOM   1998 C CB  . TRP B 1 19  ? 31.439  -5.765  -39.141 1.00 30.72 ? 19  TRP B CB  1 
ATOM   1999 C CG  . TRP B 1 19  ? 31.908  -6.201  -37.764 1.00 36.88 ? 19  TRP B CG  1 
ATOM   2000 C CD1 . TRP B 1 19  ? 31.289  -5.965  -36.559 1.00 35.34 ? 19  TRP B CD1 1 
ATOM   2001 C CD2 . TRP B 1 19  ? 33.080  -6.977  -37.464 1.00 38.75 ? 19  TRP B CD2 1 
ATOM   2002 N NE1 . TRP B 1 19  ? 32.012  -6.533  -35.533 1.00 35.24 ? 19  TRP B NE1 1 
ATOM   2003 C CE2 . TRP B 1 19  ? 33.113  -7.161  -36.061 1.00 38.37 ? 19  TRP B CE2 1 
ATOM   2004 C CE3 . TRP B 1 19  ? 34.112  -7.520  -38.245 1.00 37.80 ? 19  TRP B CE3 1 
ATOM   2005 C CZ2 . TRP B 1 19  ? 34.138  -7.865  -35.423 1.00 41.91 ? 19  TRP B CZ2 1 
ATOM   2006 C CZ3 . TRP B 1 19  ? 35.130  -8.232  -37.604 1.00 39.67 ? 19  TRP B CZ3 1 
ATOM   2007 C CH2 . TRP B 1 19  ? 35.131  -8.395  -36.211 1.00 42.41 ? 19  TRP B CH2 1 
ATOM   2008 N N   . LEU B 1 20  ? 28.334  -5.824  -38.858 1.00 31.25 ? 20  LEU B N   1 
ATOM   2009 C CA  . LEU B 1 20  ? 27.126  -5.814  -38.027 1.00 32.46 ? 20  LEU B CA  1 
ATOM   2010 C C   . LEU B 1 20  ? 26.230  -7.010  -38.307 1.00 34.35 ? 20  LEU B C   1 
ATOM   2011 O O   . LEU B 1 20  ? 25.484  -7.447  -37.425 1.00 34.85 ? 20  LEU B O   1 
ATOM   2012 C CB  . LEU B 1 20  ? 26.344  -4.526  -38.263 1.00 27.03 ? 20  LEU B CB  1 
ATOM   2013 C CG  . LEU B 1 20  ? 26.942  -3.335  -37.535 1.00 30.11 ? 20  LEU B CG  1 
ATOM   2014 C CD1 . LEU B 1 20  ? 26.320  -2.017  -38.031 1.00 30.93 ? 20  LEU B CD1 1 
ATOM   2015 C CD2 . LEU B 1 20  ? 26.798  -3.508  -36.021 1.00 31.61 ? 20  LEU B CD2 1 
ATOM   2016 N N   . ARG B 1 21  ? 26.289  -7.550  -39.526 1.00 34.05 ? 21  ARG B N   1 
ATOM   2017 C CA  . ARG B 1 21  ? 25.472  -8.703  -39.882 1.00 40.83 ? 21  ARG B CA  1 
ATOM   2018 C C   . ARG B 1 21  ? 25.737  -9.919  -39.000 1.00 39.91 ? 21  ARG B C   1 
ATOM   2019 O O   . ARG B 1 21  ? 24.877  -10.804 -38.915 1.00 36.40 ? 21  ARG B O   1 
ATOM   2020 C CB  . ARG B 1 21  ? 25.685  -9.045  -41.359 1.00 38.58 ? 21  ARG B CB  1 
ATOM   2021 C CG  . ARG B 1 21  ? 24.476  -9.734  -41.979 1.00 41.57 ? 21  ARG B CG  1 
ATOM   2022 C CD  . ARG B 1 21  ? 24.506  -9.724  -43.498 1.00 42.74 ? 21  ARG B CD  1 
ATOM   2023 N NE  . ARG B 1 21  ? 25.812  -10.038 -44.056 1.00 41.69 ? 21  ARG B NE  1 
ATOM   2024 C CZ  . ARG B 1 21  ? 26.152  -9.773  -45.309 1.00 45.23 ? 21  ARG B CZ  1 
ATOM   2025 N NH1 . ARG B 1 21  ? 25.297  -9.210  -46.149 1.00 50.03 ? 21  ARG B NH1 1 
ATOM   2026 N NH2 . ARG B 1 21  ? 27.380  -10.065 -45.727 1.00 42.11 ? 21  ARG B NH2 1 
ATOM   2027 N N   . LYS B 1 22  ? 26.897  -9.983  -38.343 1.00 38.66 ? 22  LYS B N   1 
ATOM   2028 C CA  . LYS B 1 22  ? 27.223  -11.092 -37.450 1.00 37.32 ? 22  LYS B CA  1 
ATOM   2029 C C   . LYS B 1 22  ? 26.429  -11.080 -36.153 1.00 40.03 ? 22  LYS B C   1 
ATOM   2030 O O   . LYS B 1 22  ? 26.467  -12.065 -35.415 1.00 42.03 ? 22  LYS B O   1 
ATOM   2031 C CB  . LYS B 1 22  ? 28.712  -11.060 -37.118 1.00 37.46 ? 22  LYS B CB  1 
ATOM   2032 C CG  . LYS B 1 22  ? 29.578  -11.420 -38.298 1.00 37.22 ? 22  LYS B CG  1 
ATOM   2033 C CD  . LYS B 1 22  ? 30.821  -10.555 -38.372 1.00 42.05 ? 22  LYS B CD  1 
ATOM   2034 C CE  . LYS B 1 22  ? 31.748  -10.795 -37.196 1.00 42.61 ? 22  LYS B CE  1 
ATOM   2035 N NZ  . LYS B 1 22  ? 33.017  -11.413 -37.703 1.00 49.87 ? 22  LYS B NZ  1 
ATOM   2036 N N   . GLY B 1 23  ? 25.729  -9.998  -35.836 1.00 41.57 ? 23  GLY B N   1 
ATOM   2037 C CA  . GLY B 1 23  ? 24.990  -9.975  -34.591 1.00 38.94 ? 23  GLY B CA  1 
ATOM   2038 C C   . GLY B 1 23  ? 25.855  -9.870  -33.363 1.00 40.92 ? 23  GLY B C   1 
ATOM   2039 O O   . GLY B 1 23  ? 25.359  -10.068 -32.255 1.00 40.53 ? 23  GLY B O   1 
ATOM   2040 N N   . GLU B 1 24  ? 27.129  -9.502  -33.522 1.00 40.62 ? 24  GLU B N   1 
ATOM   2041 C CA  . GLU B 1 24  ? 28.059  -9.395  -32.404 1.00 39.32 ? 24  GLU B CA  1 
ATOM   2042 C C   . GLU B 1 24  ? 28.460  -7.953  -32.093 1.00 42.23 ? 24  GLU B C   1 
ATOM   2043 O O   . GLU B 1 24  ? 29.518  -7.727  -31.498 1.00 41.44 ? 24  GLU B O   1 
ATOM   2044 C CB  . GLU B 1 24  ? 29.296  -10.240 -32.685 1.00 39.45 ? 24  GLU B CB  1 
ATOM   2045 C CG  . GLU B 1 24  ? 28.949  -11.631 -33.185 1.00 42.72 ? 24  GLU B CG  1 
ATOM   2046 C CD  . GLU B 1 24  ? 30.185  -12.452 -33.505 1.00 44.74 ? 24  GLU B CD  1 
ATOM   2047 O OE1 . GLU B 1 24  ? 30.172  -13.167 -34.521 1.00 46.88 ? 24  GLU B OE1 1 
ATOM   2048 O OE2 . GLU B 1 24  ? 31.177  -12.360 -32.752 1.00 47.87 ? 24  GLU B OE2 1 
ATOM   2049 N N   . GLY B 1 25  ? 27.648  -6.964  -32.483 1.00 38.05 ? 25  GLY B N   1 
ATOM   2050 C CA  . GLY B 1 25  ? 27.960  -5.601  -32.131 1.00 35.85 ? 25  GLY B CA  1 
ATOM   2051 C C   . GLY B 1 25  ? 28.960  -4.983  -33.088 1.00 35.78 ? 25  GLY B C   1 
ATOM   2052 O O   . GLY B 1 25  ? 29.355  -5.571  -34.097 1.00 33.27 ? 25  GLY B O   1 
ATOM   2053 N N   . LEU B 1 26  ? 29.370  -3.754  -32.751 1.00 34.95 ? 26  LEU B N   1 
ATOM   2054 C CA  . LEU B 1 26  ? 30.273  -2.942  -33.555 1.00 35.06 ? 26  LEU B CA  1 
ATOM   2055 C C   . LEU B 1 26  ? 31.716  -3.420  -33.404 1.00 36.99 ? 26  LEU B C   1 
ATOM   2056 O O   . LEU B 1 26  ? 32.104  -3.913  -32.344 1.00 38.26 ? 26  LEU B O   1 
ATOM   2057 C CB  . LEU B 1 26  ? 30.188  -1.483  -33.135 1.00 33.22 ? 26  LEU B CB  1 
ATOM   2058 C CG  . LEU B 1 26  ? 28.909  -0.759  -33.551 1.00 35.67 ? 26  LEU B CG  1 
ATOM   2059 C CD1 . LEU B 1 26  ? 28.717  0.529   -32.744 1.00 35.21 ? 26  LEU B CD1 1 
ATOM   2060 C CD2 . LEU B 1 26  ? 28.942  -0.479  -35.040 1.00 33.13 ? 26  LEU B CD2 1 
ATOM   2061 N N   . PRO B 1 27  ? 32.539  -3.245  -34.433 1.00 35.29 ? 27  PRO B N   1 
ATOM   2062 C CA  . PRO B 1 27  ? 33.949  -3.641  -34.322 1.00 36.43 ? 27  PRO B CA  1 
ATOM   2063 C C   . PRO B 1 27  ? 34.722  -2.699  -33.414 1.00 37.79 ? 27  PRO B C   1 
ATOM   2064 O O   . PRO B 1 27  ? 34.303  -1.577  -33.121 1.00 33.62 ? 27  PRO B O   1 
ATOM   2065 C CB  . PRO B 1 27  ? 34.477  -3.547  -35.760 1.00 35.14 ? 27  PRO B CB  1 
ATOM   2066 C CG  . PRO B 1 27  ? 33.294  -3.349  -36.626 1.00 42.49 ? 27  PRO B CG  1 
ATOM   2067 C CD  . PRO B 1 27  ? 32.220  -2.717  -35.768 1.00 34.79 ? 27  PRO B CD  1 
ATOM   2068 N N   . ASN B 1 28  ? 35.872  -3.192  -32.949 1.00 38.45 ? 28  ASN B N   1 
ATOM   2069 C CA  . ASN B 1 28  ? 36.738  -2.401  -32.081 1.00 35.16 ? 28  ASN B CA  1 
ATOM   2070 C C   . ASN B 1 28  ? 37.464  -1.305  -32.855 1.00 33.59 ? 28  ASN B C   1 
ATOM   2071 O O   . ASN B 1 28  ? 37.968  -0.354  -32.248 1.00 31.47 ? 28  ASN B O   1 
ATOM   2072 C CB  . ASN B 1 28  ? 37.739  -3.318  -31.367 1.00 37.56 ? 28  ASN B CB  1 
ATOM   2073 C CG  . ASN B 1 28  ? 37.062  -4.246  -30.364 1.00 41.67 ? 28  ASN B CG  1 
ATOM   2074 O OD1 . ASN B 1 28  ? 36.249  -3.811  -29.556 1.00 44.53 ? 28  ASN B OD1 1 
ATOM   2075 N ND2 . ASN B 1 28  ? 37.387  -5.527  -30.425 1.00 40.77 ? 28  ASN B ND2 1 
ATOM   2076 N N   . TYR B 1 29  ? 37.540  -1.427  -34.172 1.00 30.59 ? 29  TYR B N   1 
ATOM   2077 C CA  . TYR B 1 29  ? 38.155  -0.405  -35.000 1.00 30.37 ? 29  TYR B CA  1 
ATOM   2078 C C   . TYR B 1 29  ? 37.682  -0.633  -36.424 1.00 31.29 ? 29  TYR B C   1 
ATOM   2079 O O   . TYR B 1 29  ? 37.106  -1.675  -36.748 1.00 34.17 ? 29  TYR B O   1 
ATOM   2080 C CB  . TYR B 1 29  ? 39.684  -0.447  -34.878 1.00 36.44 ? 29  TYR B CB  1 
ATOM   2081 C CG  . TYR B 1 29  ? 40.316  -1.769  -35.285 1.00 36.95 ? 29  TYR B CG  1 
ATOM   2082 C CD1 . TYR B 1 29  ? 40.345  -2.191  -36.620 1.00 37.86 ? 29  TYR B CD1 1 
ATOM   2083 C CD2 . TYR B 1 29  ? 40.808  -2.632  -34.316 1.00 38.08 ? 29  TYR B CD2 1 
ATOM   2084 C CE1 . TYR B 1 29  ? 40.925  -3.416  -36.980 1.00 43.43 ? 29  TYR B CE1 1 
ATOM   2085 C CE2 . TYR B 1 29  ? 41.373  -3.848  -34.657 1.00 42.60 ? 29  TYR B CE2 1 
ATOM   2086 C CZ  . TYR B 1 29  ? 41.427  -4.242  -35.983 1.00 46.15 ? 29  TYR B CZ  1 
ATOM   2087 O OH  . TYR B 1 29  ? 41.984  -5.462  -36.303 1.00 49.92 ? 29  TYR B OH  1 
ATOM   2088 N N   . LEU B 1 30  ? 37.941  0.356   -37.269 1.00 29.26 ? 30  LEU B N   1 
ATOM   2089 C CA  . LEU B 1 30  ? 37.625  0.322   -38.689 1.00 27.67 ? 30  LEU B CA  1 
ATOM   2090 C C   . LEU B 1 30  ? 38.850  0.825   -39.429 1.00 29.41 ? 30  LEU B C   1 
ATOM   2091 O O   . LEU B 1 30  ? 39.322  1.939   -39.154 1.00 28.53 ? 30  LEU B O   1 
ATOM   2092 C CB  . LEU B 1 30  ? 36.417  1.211   -39.021 1.00 28.09 ? 30  LEU B CB  1 
ATOM   2093 C CG  . LEU B 1 30  ? 36.114  1.372   -40.522 1.00 29.49 ? 30  LEU B CG  1 
ATOM   2094 C CD1 . LEU B 1 30  ? 35.591  0.042   -41.115 1.00 30.10 ? 30  LEU B CD1 1 
ATOM   2095 C CD2 . LEU B 1 30  ? 35.129  2.536   -40.795 1.00 30.78 ? 30  LEU B CD2 1 
ATOM   2096 N N   . ILE B 1 31  ? 39.367  0.015   -40.358 1.00 31.21 ? 31  ILE B N   1 
ATOM   2097 C CA  . ILE B 1 31  ? 40.540  0.403   -41.142 1.00 31.09 ? 31  ILE B CA  1 
ATOM   2098 C C   . ILE B 1 31  ? 40.121  1.307   -42.287 1.00 30.32 ? 31  ILE B C   1 
ATOM   2099 O O   . ILE B 1 31  ? 39.224  0.963   -43.064 1.00 32.21 ? 31  ILE B O   1 
ATOM   2100 C CB  . ILE B 1 31  ? 41.285  -0.828  -41.684 1.00 32.20 ? 31  ILE B CB  1 
ATOM   2101 C CG1 . ILE B 1 31  ? 41.678  -1.780  -40.563 1.00 33.27 ? 31  ILE B CG1 1 
ATOM   2102 C CG2 . ILE B 1 31  ? 42.522  -0.374  -42.442 1.00 33.14 ? 31  ILE B CG2 1 
ATOM   2103 C CD1 . ILE B 1 31  ? 42.482  -1.115  -39.493 1.00 35.73 ? 31  ILE B CD1 1 
ATOM   2104 N N   . MET B 1 32  ? 40.814  2.439   -42.429 1.00 28.68 ? 32  MET B N   1 
ATOM   2105 C CA  . MET B 1 32  ? 40.580  3.390   -43.509 1.00 29.66 ? 32  MET B CA  1 
ATOM   2106 C C   . MET B 1 32  ? 41.910  3.940   -44.036 1.00 31.43 ? 32  MET B C   1 
ATOM   2107 O O   . MET B 1 32  ? 42.897  4.032   -43.307 1.00 32.86 ? 32  MET B O   1 
ATOM   2108 C CB  . MET B 1 32  ? 39.708  4.553   -43.022 1.00 27.73 ? 32  MET B CB  1 
ATOM   2109 C CG  . MET B 1 32  ? 38.318  4.176   -42.464 1.00 25.78 ? 32  MET B CG  1 
ATOM   2110 S SD  . MET B 1 32  ? 37.226  3.607   -43.767 1.00 28.92 ? 32  MET B SD  1 
ATOM   2111 C CE  . MET B 1 32  ? 36.479  5.161   -44.247 1.00 26.07 ? 32  MET B CE  1 
ATOM   2112 N N   . TYR B 1 33  ? 41.922  4.308   -45.313 1.00 29.48 ? 33  TYR B N   1 
ATOM   2113 C CA  . TYR B 1 33  ? 43.081  4.922   -45.968 1.00 33.88 ? 33  TYR B CA  1 
ATOM   2114 C C   . TYR B 1 33  ? 42.759  6.347   -46.411 1.00 33.13 ? 33  TYR B C   1 
ATOM   2115 O O   . TYR B 1 33  ? 41.761  6.578   -47.111 1.00 34.59 ? 33  TYR B O   1 
ATOM   2116 C CB  . TYR B 1 33  ? 43.526  4.065   -47.156 1.00 31.18 ? 33  TYR B CB  1 
ATOM   2117 C CG  . TYR B 1 33  ? 43.687  2.633   -46.740 1.00 30.84 ? 33  TYR B CG  1 
ATOM   2118 C CD1 . TYR B 1 33  ? 42.575  1.788   -46.652 1.00 34.82 ? 33  TYR B CD1 1 
ATOM   2119 C CD2 . TYR B 1 33  ? 44.931  2.128   -46.384 1.00 32.94 ? 33  TYR B CD2 1 
ATOM   2120 C CE1 . TYR B 1 33  ? 42.695  0.473   -46.234 1.00 34.17 ? 33  TYR B CE1 1 
ATOM   2121 C CE2 . TYR B 1 33  ? 45.069  0.801   -45.985 1.00 33.09 ? 33  TYR B CE2 1 
ATOM   2122 C CZ  . TYR B 1 33  ? 43.940  -0.015  -45.898 1.00 35.22 ? 33  TYR B CZ  1 
ATOM   2123 O OH  . TYR B 1 33  ? 44.034  -1.327  -45.486 1.00 32.60 ? 33  TYR B OH  1 
ATOM   2124 N N   . ASP B 1 34  ? 43.617  7.297   -46.042 1.00 33.97 ? 34  ASP B N   1 
ATOM   2125 C CA  . ASP B 1 34  ? 43.311  8.680   -46.379 1.00 36.23 ? 34  ASP B CA  1 
ATOM   2126 C C   . ASP B 1 34  ? 43.578  8.947   -47.860 1.00 36.68 ? 34  ASP B C   1 
ATOM   2127 O O   . ASP B 1 34  ? 44.322  8.230   -48.526 1.00 37.28 ? 34  ASP B O   1 
ATOM   2128 C CB  . ASP B 1 34  ? 44.103  9.631   -45.506 1.00 40.60 ? 34  ASP B CB  1 
ATOM   2129 C CG  . ASP B 1 34  ? 45.483  9.857   -46.024 1.00 42.23 ? 34  ASP B CG  1 
ATOM   2130 O OD1 . ASP B 1 34  ? 46.361  8.991   -45.857 1.00 42.77 ? 34  ASP B OD1 1 
ATOM   2131 O OD2 . ASP B 1 34  ? 45.638  10.898  -46.662 1.00 43.30 ? 34  ASP B OD2 1 
ATOM   2132 N N   . MET B 1 35  ? 42.879  9.933   -48.399 1.00 34.01 ? 35  MET B N   1 
ATOM   2133 C CA  . MET B 1 35  ? 42.923  10.169  -49.856 1.00 38.98 ? 35  MET B CA  1 
ATOM   2134 C C   . MET B 1 35  ? 44.154  10.965  -50.278 1.00 38.13 ? 35  MET B C   1 
ATOM   2135 O O   . MET B 1 35  ? 44.381  11.027  -51.459 1.00 40.44 ? 35  MET B O   1 
ATOM   2136 C CB  . MET B 1 35  ? 41.668  10.905  -50.328 1.00 34.22 ? 35  MET B CB  1 
ATOM   2137 C CG  . MET B 1 35  ? 41.624  12.336  -49.907 1.00 38.23 ? 35  MET B CG  1 
ATOM   2138 S SD  . MET B 1 35  ? 40.013  13.124  -50.042 1.00 39.61 ? 35  MET B SD  1 
ATOM   2139 C CE  . MET B 1 35  ? 39.658  12.920  -51.778 1.00 35.65 ? 35  MET B CE  1 
ATOM   2140 N N   . ASP B 1 36  ? 44.891  11.547  -49.337 1.00 47.32 ? 36  ASP B N   1 
ATOM   2141 C CA  . ASP B 1 36  ? 46.050  12.396  -49.707 1.00 46.01 ? 36  ASP B CA  1 
ATOM   2142 C C   . ASP B 1 36  ? 47.348  11.599  -49.689 1.00 49.76 ? 36  ASP B C   1 
ATOM   2143 O O   . ASP B 1 36  ? 48.063  11.683  -50.659 1.00 58.08 ? 36  ASP B O   1 
ATOM   2144 C CB  . ASP B 1 36  ? 46.145  13.637  -48.829 1.00 48.08 ? 36  ASP B CB  1 
ATOM   2145 C CG  . ASP B 1 36  ? 44.880  14.445  -48.869 1.00 45.85 ? 36  ASP B CG  1 
ATOM   2146 O OD1 . ASP B 1 36  ? 44.470  14.766  -49.954 1.00 46.09 ? 36  ASP B OD1 1 
ATOM   2147 O OD2 . ASP B 1 36  ? 44.318  14.677  -47.829 1.00 45.55 ? 36  ASP B OD2 1 
ATOM   2148 N N   . ARG B 1 37  ? 47.615  10.856  -48.623 1.00 56.18 ? 37  ARG B N   1 
ATOM   2149 C CA  . ARG B 1 37  ? 48.882  10.101  -48.523 1.00 47.79 ? 37  ARG B CA  1 
ATOM   2150 C C   . ARG B 1 37  ? 48.628  8.595   -48.618 1.00 51.12 ? 37  ARG B C   1 
ATOM   2151 O O   . ARG B 1 37  ? 49.583  7.845   -48.513 1.00 48.60 ? 37  ARG B O   1 
ATOM   2152 C CB  . ARG B 1 37  ? 49.555  10.447  -47.194 1.00 55.87 ? 37  ARG B CB  1 
ATOM   2153 C CG  . ARG B 1 37  ? 49.987  11.898  -47.087 1.00 57.13 ? 37  ARG B CG  1 
ATOM   2154 C CD  . ARG B 1 37  ? 50.489  12.428  -48.417 1.00 55.95 ? 37  ARG B CD  1 
ATOM   2155 N NE  . ARG B 1 37  ? 51.942  12.436  -48.509 1.00 65.75 ? 37  ARG B NE  1 
ATOM   2156 C CZ  . ARG B 1 37  ? 52.674  13.539  -48.535 1.00 65.01 ? 37  ARG B CZ  1 
ATOM   2157 N NH1 . ARG B 1 37  ? 53.990  13.458  -48.624 1.00 64.60 ? 37  ARG B NH1 1 
ATOM   2158 N NH2 . ARG B 1 37  ? 52.087  14.723  -48.483 1.00 61.29 ? 37  ARG B NH2 1 
ATOM   2159 N N   . ASN B 1 38  ? 47.381  8.176   -48.784 1.00 48.74 ? 38  ASN B N   1 
ATOM   2160 C CA  . ASN B 1 38  ? 47.074  6.729   -48.893 1.00 40.73 ? 38  ASN B CA  1 
ATOM   2161 C C   . ASN B 1 38  ? 47.589  5.986   -47.662 1.00 40.33 ? 38  ASN B C   1 
ATOM   2162 O O   . ASN B 1 38  ? 47.852  4.818   -47.801 1.00 39.65 ? 38  ASN B O   1 
ATOM   2163 C CB  . ASN B 1 38  ? 47.473  6.158   -50.255 1.00 45.22 ? 38  ASN B CB  1 
ATOM   2164 C CG  . ASN B 1 38  ? 46.920  6.963   -51.410 1.00 48.78 ? 38  ASN B CG  1 
ATOM   2165 O OD1 . ASN B 1 38  ? 45.749  6.860   -51.737 1.00 49.85 ? 38  ASN B OD1 1 
ATOM   2166 N ND2 . ASN B 1 38  ? 47.752  7.773   -52.035 1.00 50.02 ? 38  ASN B ND2 1 
ATOM   2167 N N   . LYS B 1 39  ? 47.657  6.634   -46.501 1.00 35.95 ? 39  LYS B N   1 
ATOM   2168 C CA  . LYS B 1 39  ? 48.209  5.947   -45.328 1.00 37.52 ? 39  LYS B CA  1 
ATOM   2169 C C   . LYS B 1 39  ? 47.094  5.195   -44.587 1.00 38.12 ? 39  LYS B C   1 
ATOM   2170 O O   . LYS B 1 39  ? 45.931  5.592   -44.630 1.00 35.42 ? 39  LYS B O   1 
ATOM   2171 C CB  . LYS B 1 39  ? 48.873  6.958   -44.389 1.00 37.69 ? 39  LYS B CB  1 
ATOM   2172 C CG  . LYS B 1 39  ? 49.118  6.464   -42.974 1.00 43.43 ? 39  LYS B CG  1 
ATOM   2173 C CD  . LYS B 1 39  ? 49.709  7.568   -42.093 1.00 48.79 ? 39  LYS B CD  1 
ATOM   2174 C CE  . LYS B 1 39  ? 50.006  7.036   -40.692 1.00 50.28 ? 39  LYS B CE  1 
ATOM   2175 N NZ  . LYS B 1 39  ? 51.372  6.437   -40.609 1.00 54.09 ? 39  LYS B NZ  1 
ATOM   2176 N N   . GLU B 1 40  ? 47.446  4.078   -43.948 1.00 35.19 ? 40  GLU B N   1 
ATOM   2177 C CA  . GLU B 1 40  ? 46.473  3.282   -43.203 1.00 33.76 ? 40  GLU B CA  1 
ATOM   2178 C C   . GLU B 1 40  ? 46.171  3.867   -41.830 1.00 36.25 ? 40  GLU B C   1 
ATOM   2179 O O   . GLU B 1 40  ? 47.085  4.097   -41.033 1.00 36.30 ? 40  GLU B O   1 
ATOM   2180 C CB  . GLU B 1 40  ? 46.969  1.850   -43.022 1.00 31.55 ? 40  GLU B CB  1 
ATOM   2181 C CG  . GLU B 1 40  ? 45.858  0.871   -42.743 1.00 32.12 ? 40  GLU B CG  1 
ATOM   2182 C CD  . GLU B 1 40  ? 46.352  -0.566  -42.729 1.00 34.32 ? 40  GLU B CD  1 
ATOM   2183 O OE1 . GLU B 1 40  ? 47.162  -0.895  -41.848 1.00 35.63 ? 40  GLU B OE1 1 
ATOM   2184 O OE2 . GLU B 1 40  ? 45.964  -1.338  -43.625 1.00 35.11 ? 40  GLU B OE2 1 
ATOM   2185 N N   . TYR B 1 41  ? 44.877  4.035   -41.523 1.00 31.65 ? 41  TYR B N   1 
ATOM   2186 C CA  . TYR B 1 41  ? 44.447  4.462   -40.196 1.00 31.86 ? 41  TYR B CA  1 
ATOM   2187 C C   . TYR B 1 41  ? 43.513  3.432   -39.566 1.00 34.27 ? 41  TYR B C   1 
ATOM   2188 O O   . TYR B 1 41  ? 42.612  2.901   -40.225 1.00 32.92 ? 41  TYR B O   1 
ATOM   2189 C CB  . TYR B 1 41  ? 43.742  5.823   -40.248 1.00 34.20 ? 41  TYR B CB  1 
ATOM   2190 C CG  . TYR B 1 41  ? 44.652  6.948   -40.677 1.00 38.72 ? 41  TYR B CG  1 
ATOM   2191 C CD1 . TYR B 1 41  ? 44.936  7.157   -42.015 1.00 36.45 ? 41  TYR B CD1 1 
ATOM   2192 C CD2 . TYR B 1 41  ? 45.263  7.772   -39.734 1.00 40.29 ? 41  TYR B CD2 1 
ATOM   2193 C CE1 . TYR B 1 41  ? 45.784  8.178   -42.413 1.00 39.35 ? 41  TYR B CE1 1 
ATOM   2194 C CE2 . TYR B 1 41  ? 46.111  8.790   -40.122 1.00 39.46 ? 41  TYR B CE2 1 
ATOM   2195 C CZ  . TYR B 1 41  ? 46.369  8.984   -41.465 1.00 39.73 ? 41  TYR B CZ  1 
ATOM   2196 O OH  . TYR B 1 41  ? 47.205  10.000  -41.874 1.00 46.49 ? 41  TYR B OH  1 
ATOM   2197 N N   . LYS B 1 42  ? 43.739  3.155   -38.283 1.00 32.80 ? 42  LYS B N   1 
ATOM   2198 C CA  . LYS B 1 42  ? 42.878  2.285   -37.493 1.00 36.52 ? 42  LYS B CA  1 
ATOM   2199 C C   . LYS B 1 42  ? 42.025  3.190   -36.601 1.00 34.66 ? 42  LYS B C   1 
ATOM   2200 O O   . LYS B 1 42  ? 42.421  3.546   -35.489 1.00 32.46 ? 42  LYS B O   1 
ATOM   2201 C CB  . LYS B 1 42  ? 43.733  1.309   -36.688 1.00 38.59 ? 42  LYS B CB  1 
ATOM   2202 C CG  . LYS B 1 42  ? 42.957  0.212   -36.001 1.00 39.23 ? 42  LYS B CG  1 
ATOM   2203 C CD  . LYS B 1 42  ? 43.858  -0.909  -35.487 1.00 40.63 ? 42  LYS B CD  1 
ATOM   2204 C CE  . LYS B 1 42  ? 44.570  -1.594  -36.629 1.00 42.63 ? 42  LYS B CE  1 
ATOM   2205 N NZ  . LYS B 1 42  ? 44.984  -2.997  -36.269 1.00 49.92 ? 42  LYS B NZ  1 
ATOM   2206 N N   . LEU B 1 43  ? 40.824  3.516   -37.082 1.00 29.97 ? 43  LEU B N   1 
ATOM   2207 C CA  . LEU B 1 43  ? 39.908  4.410   -36.371 1.00 32.43 ? 43  LEU B CA  1 
ATOM   2208 C C   . LEU B 1 43  ? 39.179  3.672   -35.256 1.00 30.16 ? 43  LEU B C   1 
ATOM   2209 O O   . LEU B 1 43  ? 38.547  2.642   -35.494 1.00 27.38 ? 43  LEU B O   1 
ATOM   2210 C CB  . LEU B 1 43  ? 38.882  4.995   -37.345 1.00 30.09 ? 43  LEU B CB  1 
ATOM   2211 C CG  . LEU B 1 43  ? 39.447  5.666   -38.600 1.00 31.58 ? 43  LEU B CG  1 
ATOM   2212 C CD1 . LEU B 1 43  ? 38.315  6.153   -39.492 1.00 33.52 ? 43  LEU B CD1 1 
ATOM   2213 C CD2 . LEU B 1 43  ? 40.381  6.825   -38.244 1.00 29.86 ? 43  LEU B CD2 1 
ATOM   2214 N N   . VAL B 1 44  ? 39.239  4.222   -34.047 1.00 31.38 ? 44  VAL B N   1 
ATOM   2215 C CA  . VAL B 1 44  ? 38.515  3.678   -32.903 1.00 31.40 ? 44  VAL B CA  1 
ATOM   2216 C C   . VAL B 1 44  ? 37.033  4.053   -33.023 1.00 32.46 ? 44  VAL B C   1 
ATOM   2217 O O   . VAL B 1 44  ? 36.678  4.881   -33.877 1.00 31.41 ? 44  VAL B O   1 
ATOM   2218 C CB  . VAL B 1 44  ? 39.153  4.166   -31.592 1.00 30.16 ? 44  VAL B CB  1 
ATOM   2219 C CG1 . VAL B 1 44  ? 40.579  3.628   -31.474 1.00 32.19 ? 44  VAL B CG1 1 
ATOM   2220 C CG2 . VAL B 1 44  ? 39.151  5.682   -31.526 1.00 33.64 ? 44  VAL B CG2 1 
ATOM   2221 N N   . PRO B 1 45  ? 36.125  3.422   -32.262 1.00 31.51 ? 45  PRO B N   1 
ATOM   2222 C CA  . PRO B 1 45  ? 34.685  3.653   -32.509 1.00 29.19 ? 45  PRO B CA  1 
ATOM   2223 C C   . PRO B 1 45  ? 34.245  5.107   -32.441 1.00 29.64 ? 45  PRO B C   1 
ATOM   2224 O O   . PRO B 1 45  ? 33.474  5.550   -33.306 1.00 30.41 ? 45  PRO B O   1 
ATOM   2225 C CB  . PRO B 1 45  ? 34.007  2.801   -31.434 1.00 32.83 ? 45  PRO B CB  1 
ATOM   2226 C CG  . PRO B 1 45  ? 34.989  1.744   -31.094 1.00 33.05 ? 45  PRO B CG  1 
ATOM   2227 C CD  . PRO B 1 45  ? 36.358  2.197   -31.475 1.00 32.24 ? 45  PRO B CD  1 
ATOM   2228 N N   . LYS B 1 46  ? 34.694  5.871   -31.444 1.00 31.41 ? 46  LYS B N   1 
ATOM   2229 C CA  . LYS B 1 46  ? 34.306  7.276   -31.410 1.00 31.03 ? 46  LYS B CA  1 
ATOM   2230 C C   . LYS B 1 46  ? 34.804  8.028   -32.640 1.00 32.88 ? 46  LYS B C   1 
ATOM   2231 O O   . LYS B 1 46  ? 34.206  9.038   -33.030 1.00 29.80 ? 46  LYS B O   1 
ATOM   2232 C CB  . LYS B 1 46  ? 34.784  7.928   -30.117 1.00 31.34 ? 46  LYS B CB  1 
ATOM   2233 C CG  . LYS B 1 46  ? 36.167  8.545   -30.155 1.00 36.39 ? 46  LYS B CG  1 
ATOM   2234 C CD  . LYS B 1 46  ? 36.743  8.632   -28.743 1.00 39.22 ? 46  LYS B CD  1 
ATOM   2235 C CE  . LYS B 1 46  ? 38.116  9.291   -28.718 1.00 43.10 ? 46  LYS B CE  1 
ATOM   2236 N NZ  . LYS B 1 46  ? 38.679  9.328   -27.323 1.00 48.06 ? 46  LYS B NZ  1 
ATOM   2237 N N   . GLU B 1 47  ? 35.884  7.548   -33.277 1.00 29.65 ? 47  GLU B N   1 
ATOM   2238 C CA  . GLU B 1 47  ? 36.403  8.199   -34.471 1.00 29.00 ? 47  GLU B CA  1 
ATOM   2239 C C   . GLU B 1 47  ? 35.623  7.816   -35.721 1.00 27.57 ? 47  GLU B C   1 
ATOM   2240 O O   . GLU B 1 47  ? 35.324  8.673   -36.558 1.00 28.49 ? 47  GLU B O   1 
ATOM   2241 C CB  . GLU B 1 47  ? 37.882  7.857   -34.660 1.00 30.39 ? 47  GLU B CB  1 
ATOM   2242 C CG  . GLU B 1 47  ? 38.836  8.567   -33.713 1.00 28.03 ? 47  GLU B CG  1 
ATOM   2243 C CD  . GLU B 1 47  ? 40.269  8.165   -33.997 1.00 35.79 ? 47  GLU B CD  1 
ATOM   2244 O OE1 . GLU B 1 47  ? 40.509  6.960   -34.219 1.00 33.46 ? 47  GLU B OE1 1 
ATOM   2245 O OE2 . GLU B 1 47  ? 41.152  9.049   -34.011 1.00 38.92 ? 47  GLU B OE2 1 
ATOM   2246 N N   . TYR B 1 48  ? 35.337  6.529   -35.918 1.00 27.63 ? 48  TYR B N   1 
ATOM   2247 C CA  . TYR B 1 48  ? 34.580  6.204   -37.122 1.00 24.81 ? 48  TYR B CA  1 
ATOM   2248 C C   . TYR B 1 48  ? 33.118  6.647   -36.989 1.00 25.57 ? 48  TYR B C   1 
ATOM   2249 O O   . TYR B 1 48  ? 32.497  6.991   -37.998 1.00 27.44 ? 48  TYR B O   1 
ATOM   2250 C CB  . TYR B 1 48  ? 34.733  4.717   -37.516 1.00 24.35 ? 48  TYR B CB  1 
ATOM   2251 C CG  . TYR B 1 48  ? 34.178  3.624   -36.585 1.00 28.29 ? 48  TYR B CG  1 
ATOM   2252 C CD1 . TYR B 1 48  ? 32.820  3.549   -36.243 1.00 25.53 ? 48  TYR B CD1 1 
ATOM   2253 C CD2 . TYR B 1 48  ? 35.020  2.622   -36.113 1.00 28.14 ? 48  TYR B CD2 1 
ATOM   2254 C CE1 . TYR B 1 48  ? 32.334  2.532   -35.406 1.00 23.97 ? 48  TYR B CE1 1 
ATOM   2255 C CE2 . TYR B 1 48  ? 34.565  1.604   -35.320 1.00 28.75 ? 48  TYR B CE2 1 
ATOM   2256 C CZ  . TYR B 1 48  ? 33.234  1.550   -34.955 1.00 30.64 ? 48  TYR B CZ  1 
ATOM   2257 O OH  . TYR B 1 48  ? 32.838  0.509   -34.145 1.00 32.33 ? 48  TYR B OH  1 
ATOM   2258 N N   . ALA B 1 49  ? 32.559  6.678   -35.773 1.00 24.44 ? 49  ALA B N   1 
ATOM   2259 C CA  . ALA B 1 49  ? 31.214  7.271   -35.599 1.00 26.37 ? 49  ALA B CA  1 
ATOM   2260 C C   . ALA B 1 49  ? 31.196  8.770   -35.924 1.00 28.40 ? 49  ALA B C   1 
ATOM   2261 O O   . ALA B 1 49  ? 30.272  9.263   -36.591 1.00 27.04 ? 49  ALA B O   1 
ATOM   2262 C CB  . ALA B 1 49  ? 30.706  7.041   -34.177 1.00 26.50 ? 49  ALA B CB  1 
ATOM   2263 N N   . GLY B 1 50  ? 32.215  9.515   -35.472 1.00 28.22 ? 50  GLY B N   1 
ATOM   2264 C CA  . GLY B 1 50  ? 32.295  10.936  -35.805 1.00 28.81 ? 50  GLY B CA  1 
ATOM   2265 C C   . GLY B 1 50  ? 32.462  11.180  -37.294 1.00 27.65 ? 50  GLY B C   1 
ATOM   2266 O O   . GLY B 1 50  ? 31.838  12.078  -37.864 1.00 24.16 ? 50  GLY B O   1 
ATOM   2267 N N   . LEU B 1 51  ? 33.299  10.372  -37.947 1.00 25.04 ? 51  LEU B N   1 
ATOM   2268 C CA  . LEU B 1 51  ? 33.521  10.520  -39.381 1.00 24.15 ? 51  LEU B CA  1 
ATOM   2269 C C   . LEU B 1 51  ? 32.223  10.334  -40.154 1.00 26.99 ? 51  LEU B C   1 
ATOM   2270 O O   . LEU B 1 51  ? 31.895  11.123  -41.052 1.00 29.09 ? 51  LEU B O   1 
ATOM   2271 C CB  . LEU B 1 51  ? 34.544  9.469   -39.845 1.00 23.99 ? 51  LEU B CB  1 
ATOM   2272 C CG  . LEU B 1 51  ? 35.050  9.523   -41.292 1.00 29.96 ? 51  LEU B CG  1 
ATOM   2273 C CD1 . LEU B 1 51  ? 35.867  10.770  -41.491 1.00 25.22 ? 51  LEU B CD1 1 
ATOM   2274 C CD2 . LEU B 1 51  ? 35.893  8.275   -41.693 1.00 27.58 ? 51  LEU B CD2 1 
ATOM   2275 N N   . TYR B 1 52  ? 31.493  9.253   -39.849 1.00 25.27 ? 52  TYR B N   1 
ATOM   2276 C CA  . TYR B 1 52  ? 30.277  8.943   -40.581 1.00 25.33 ? 52  TYR B CA  1 
ATOM   2277 C C   . TYR B 1 52  ? 29.127  9.832   -40.141 1.00 22.32 ? 52  TYR B C   1 
ATOM   2278 O O   . TYR B 1 52  ? 28.256  10.156  -40.957 1.00 22.42 ? 52  TYR B O   1 
ATOM   2279 C CB  . TYR B 1 52  ? 29.955  7.442   -40.423 1.00 26.79 ? 52  TYR B CB  1 
ATOM   2280 C CG  . TYR B 1 52  ? 30.799  6.634   -41.404 1.00 24.03 ? 52  TYR B CG  1 
ATOM   2281 C CD1 . TYR B 1 52  ? 30.414  6.524   -42.733 1.00 25.72 ? 52  TYR B CD1 1 
ATOM   2282 C CD2 . TYR B 1 52  ? 32.033  6.105   -41.036 1.00 29.27 ? 52  TYR B CD2 1 
ATOM   2283 C CE1 . TYR B 1 52  ? 31.193  5.860   -43.667 1.00 28.53 ? 52  TYR B CE1 1 
ATOM   2284 C CE2 . TYR B 1 52  ? 32.835  5.420   -41.974 1.00 26.62 ? 52  TYR B CE2 1 
ATOM   2285 C CZ  . TYR B 1 52  ? 32.394  5.302   -43.287 1.00 28.52 ? 52  TYR B CZ  1 
ATOM   2286 O OH  . TYR B 1 52  ? 33.136  4.633   -44.241 1.00 28.85 ? 52  TYR B OH  1 
ATOM   2287 N N   . GLU B 1 53  ? 29.131  10.289  -38.894 1.00 22.65 ? 53  GLU B N   1 
ATOM   2288 C CA  . GLU B 1 53  ? 28.174  11.342  -38.510 1.00 27.92 ? 53  GLU B CA  1 
ATOM   2289 C C   . GLU B 1 53  ? 28.358  12.596  -39.372 1.00 26.70 ? 53  GLU B C   1 
ATOM   2290 O O   . GLU B 1 53  ? 27.383  13.213  -39.824 1.00 25.83 ? 53  GLU B O   1 
ATOM   2291 C CB  . GLU B 1 53  ? 28.337  11.698  -37.033 1.00 28.98 ? 53  GLU B CB  1 
ATOM   2292 C CG  . GLU B 1 53  ? 27.483  12.908  -36.585 1.00 27.29 ? 53  GLU B CG  1 
ATOM   2293 C CD  . GLU B 1 53  ? 27.788  13.331  -35.165 1.00 30.28 ? 53  GLU B CD  1 
ATOM   2294 O OE1 . GLU B 1 53  ? 28.819  14.018  -34.959 1.00 28.03 ? 53  GLU B OE1 1 
ATOM   2295 O OE2 . GLU B 1 53  ? 26.987  12.991  -34.260 1.00 27.76 ? 53  GLU B OE2 1 
ATOM   2296 N N   . SER B 1 54  ? 29.607  13.023  -39.563 1.00 24.33 ? 54  SER B N   1 
ATOM   2297 C CA  . SER B 1 54  ? 29.870  14.170  -40.423 1.00 23.33 ? 54  SER B CA  1 
ATOM   2298 C C   . SER B 1 54  ? 29.469  13.862  -41.865 1.00 25.53 ? 54  SER B C   1 
ATOM   2299 O O   . SER B 1 54  ? 28.860  14.693  -42.548 1.00 24.11 ? 54  SER B O   1 
ATOM   2300 C CB  . SER B 1 54  ? 31.352  14.550  -40.306 1.00 25.68 ? 54  SER B CB  1 
ATOM   2301 O OG  . SER B 1 54  ? 31.707  15.628  -41.139 1.00 27.68 ? 54  SER B OG  1 
ATOM   2302 N N   . ARG B 1 55  ? 29.789  12.657  -42.346 1.00 24.57 ? 55  ARG B N   1 
ATOM   2303 C CA  . ARG B 1 55  ? 29.330  12.268  -43.674 1.00 23.58 ? 55  ARG B CA  1 
ATOM   2304 C C   . ARG B 1 55  ? 27.808  12.347  -43.777 1.00 24.30 ? 55  ARG B C   1 
ATOM   2305 O O   . ARG B 1 55  ? 27.269  12.841  -44.774 1.00 22.17 ? 55  ARG B O   1 
ATOM   2306 C CB  . ARG B 1 55  ? 29.814  10.852  -43.988 1.00 23.78 ? 55  ARG B CB  1 
ATOM   2307 C CG  . ARG B 1 55  ? 29.415  10.336  -45.362 1.00 26.47 ? 55  ARG B CG  1 
ATOM   2308 C CD  . ARG B 1 55  ? 29.447  8.795   -45.411 1.00 24.15 ? 55  ARG B CD  1 
ATOM   2309 N NE  . ARG B 1 55  ? 29.305  8.257   -46.760 1.00 28.57 ? 55  ARG B NE  1 
ATOM   2310 C CZ  . ARG B 1 55  ? 28.940  7.006   -47.031 1.00 29.46 ? 55  ARG B CZ  1 
ATOM   2311 N NH1 . ARG B 1 55  ? 28.609  6.159   -46.069 1.00 26.86 ? 55  ARG B NH1 1 
ATOM   2312 N NH2 . ARG B 1 55  ? 28.896  6.599   -48.301 1.00 26.94 ? 55  ARG B NH2 1 
ATOM   2313 N N   . ASN B 1 56  ? 27.099  11.868  -42.746 1.00 21.94 ? 56  ASN B N   1 
ATOM   2314 C CA  . ASN B 1 56  ? 25.636  11.786  -42.787 1.00 23.50 ? 56  ASN B CA  1 
ATOM   2315 C C   . ASN B 1 56  ? 24.970  13.162  -42.686 1.00 22.94 ? 56  ASN B C   1 
ATOM   2316 O O   . ASN B 1 56  ? 23.920  13.383  -43.301 1.00 21.98 ? 56  ASN B O   1 
ATOM   2317 C CB  . ASN B 1 56  ? 25.139  10.879  -41.657 1.00 21.79 ? 56  ASN B CB  1 
ATOM   2318 C CG  . ASN B 1 56  ? 25.452  9.393   -41.893 1.00 25.59 ? 56  ASN B CG  1 
ATOM   2319 O OD1 . ASN B 1 56  ? 25.637  8.951   -43.023 1.00 23.48 ? 56  ASN B OD1 1 
ATOM   2320 N ND2 . ASN B 1 56  ? 25.470  8.621   -40.817 1.00 25.73 ? 56  ASN B ND2 1 
ATOM   2321 N N   . ILE B 1 57  ? 25.569  14.099  -41.948 1.00 22.81 ? 57  ILE B N   1 
ATOM   2322 C CA  . ILE B 1 57  ? 25.072  15.476  -41.942 1.00 25.02 ? 57  ILE B CA  1 
ATOM   2323 C C   . ILE B 1 57  ? 25.068  16.033  -43.359 1.00 26.26 ? 57  ILE B C   1 
ATOM   2324 O O   . ILE B 1 57  ? 24.034  16.496  -43.847 1.00 24.33 ? 57  ILE B O   1 
ATOM   2325 C CB  . ILE B 1 57  ? 25.921  16.361  -41.004 1.00 26.00 ? 57  ILE B CB  1 
ATOM   2326 C CG1 . ILE B 1 57  ? 25.649  16.048  -39.539 1.00 26.82 ? 57  ILE B CG1 1 
ATOM   2327 C CG2 . ILE B 1 57  ? 25.663  17.848  -41.239 1.00 25.11 ? 57  ILE B CG2 1 
ATOM   2328 C CD1 . ILE B 1 57  ? 26.701  16.608  -38.634 1.00 27.58 ? 57  ILE B CD1 1 
ATOM   2329 N N   . PHE B 1 58  ? 26.211  15.943  -44.070 1.00 22.17 ? 58  PHE B N   1 
ATOM   2330 C CA  . PHE B 1 58  ? 26.246  16.435  -45.441 1.00 25.55 ? 58  PHE B CA  1 
ATOM   2331 C C   . PHE B 1 58  ? 25.198  15.746  -46.302 1.00 25.65 ? 58  PHE B C   1 
ATOM   2332 O O   . PHE B 1 58  ? 24.469  16.397  -47.062 1.00 25.73 ? 58  PHE B O   1 
ATOM   2333 C CB  . PHE B 1 58  ? 27.630  16.231  -46.074 1.00 25.88 ? 58  PHE B CB  1 
ATOM   2334 C CG  . PHE B 1 58  ? 27.782  16.966  -47.380 1.00 27.90 ? 58  PHE B CG  1 
ATOM   2335 C CD1 . PHE B 1 58  ? 27.197  16.474  -48.544 1.00 24.57 ? 58  PHE B CD1 1 
ATOM   2336 C CD2 . PHE B 1 58  ? 28.462  18.178  -47.429 1.00 26.76 ? 58  PHE B CD2 1 
ATOM   2337 C CE1 . PHE B 1 58  ? 27.322  17.159  -49.750 1.00 31.28 ? 58  PHE B CE1 1 
ATOM   2338 C CE2 . PHE B 1 58  ? 28.579  18.876  -48.638 1.00 32.01 ? 58  PHE B CE2 1 
ATOM   2339 C CZ  . PHE B 1 58  ? 28.009  18.364  -49.791 1.00 30.38 ? 58  PHE B CZ  1 
ATOM   2340 N N   . TRP B 1 59  ? 25.129  14.423  -46.209 1.00 23.98 ? 59  TRP B N   1 
ATOM   2341 C CA  . TRP B 1 59  ? 24.212  13.636  -47.028 1.00 25.77 ? 59  TRP B CA  1 
ATOM   2342 C C   . TRP B 1 59  ? 22.746  13.989  -46.754 1.00 24.35 ? 59  TRP B C   1 
ATOM   2343 O O   . TRP B 1 59  ? 21.960  14.169  -47.695 1.00 24.80 ? 59  TRP B O   1 
ATOM   2344 C CB  . TRP B 1 59  ? 24.465  12.160  -46.767 1.00 25.42 ? 59  TRP B CB  1 
ATOM   2345 C CG  . TRP B 1 59  ? 24.145  11.268  -47.917 1.00 27.14 ? 59  TRP B CG  1 
ATOM   2346 C CD1 . TRP B 1 59  ? 23.376  11.559  -48.998 1.00 28.62 ? 59  TRP B CD1 1 
ATOM   2347 C CD2 . TRP B 1 59  ? 24.559  9.912   -48.064 1.00 25.00 ? 59  TRP B CD2 1 
ATOM   2348 N NE1 . TRP B 1 59  ? 23.320  10.469  -49.843 1.00 28.69 ? 59  TRP B NE1 1 
ATOM   2349 C CE2 . TRP B 1 59  ? 24.034  9.444   -49.284 1.00 25.32 ? 59  TRP B CE2 1 
ATOM   2350 C CE3 . TRP B 1 59  ? 25.335  9.052   -47.288 1.00 26.10 ? 59  TRP B CE3 1 
ATOM   2351 C CZ2 . TRP B 1 59  ? 24.244  8.155   -49.736 1.00 25.62 ? 59  TRP B CZ2 1 
ATOM   2352 C CZ3 . TRP B 1 59  ? 25.563  7.785   -47.748 1.00 26.14 ? 59  TRP B CZ3 1 
ATOM   2353 C CH2 . TRP B 1 59  ? 25.016  7.342   -48.961 1.00 28.77 ? 59  TRP B CH2 1 
ATOM   2354 N N   . ILE B 1 60  ? 22.361  14.103  -45.475 1.00 25.59 ? 60  ILE B N   1 
ATOM   2355 C CA  . ILE B 1 60  ? 20.959  14.426  -45.147 1.00 25.34 ? 60  ILE B CA  1 
ATOM   2356 C C   . ILE B 1 60  ? 20.613  15.832  -45.631 1.00 27.23 ? 60  ILE B C   1 
ATOM   2357 O O   . ILE B 1 60  ? 19.574  16.055  -46.260 1.00 28.67 ? 60  ILE B O   1 
ATOM   2358 C CB  . ILE B 1 60  ? 20.693  14.327  -43.627 1.00 25.52 ? 60  ILE B CB  1 
ATOM   2359 C CG1 . ILE B 1 60  ? 20.955  12.947  -43.007 1.00 26.55 ? 60  ILE B CG1 1 
ATOM   2360 C CG2 . ILE B 1 60  ? 19.238  14.791  -43.279 1.00 24.52 ? 60  ILE B CG2 1 
ATOM   2361 C CD1 . ILE B 1 60  ? 20.321  11.880  -43.687 1.00 30.01 ? 60  ILE B CD1 1 
ATOM   2362 N N   . LYS B 1 61  ? 21.486  16.804  -45.350 1.00 26.59 ? 61  LYS B N   1 
ATOM   2363 C CA  . LYS B 1 61  ? 21.176  18.205  -45.651 1.00 26.46 ? 61  LYS B CA  1 
ATOM   2364 C C   . LYS B 1 61  ? 21.185  18.497  -47.153 1.00 28.53 ? 61  LYS B C   1 
ATOM   2365 O O   . LYS B 1 61  ? 20.398  19.317  -47.634 1.00 26.35 ? 61  LYS B O   1 
ATOM   2366 C CB  . LYS B 1 61  ? 22.153  19.105  -44.910 1.00 27.62 ? 61  LYS B CB  1 
ATOM   2367 C CG  . LYS B 1 61  ? 21.893  19.114  -43.428 1.00 31.95 ? 61  LYS B CG  1 
ATOM   2368 C CD  . LYS B 1 61  ? 20.349  19.163  -43.197 1.00 31.38 ? 61  LYS B CD  1 
ATOM   2369 C CE  . LYS B 1 61  ? 19.860  20.592  -42.929 1.00 28.71 ? 61  LYS B CE  1 
ATOM   2370 N NZ  . LYS B 1 61  ? 18.679  20.634  -41.993 1.00 24.53 ? 61  LYS B NZ  1 
ATOM   2371 N N   . ASN B 1 62  ? 22.086  17.872  -47.912 1.00 27.22 ? 62  ASN B N   1 
ATOM   2372 C CA  . ASN B 1 62  ? 22.257  18.222  -49.320 1.00 26.51 ? 62  ASN B CA  1 
ATOM   2373 C C   . ASN B 1 62  ? 21.634  17.228  -50.286 1.00 27.48 ? 62  ASN B C   1 
ATOM   2374 O O   . ASN B 1 62  ? 21.579  17.513  -51.487 1.00 28.97 ? 62  ASN B O   1 
ATOM   2375 C CB  . ASN B 1 62  ? 23.752  18.380  -49.658 1.00 31.09 ? 62  ASN B CB  1 
ATOM   2376 C CG  . ASN B 1 62  ? 24.382  19.559  -48.929 1.00 30.60 ? 62  ASN B CG  1 
ATOM   2377 O OD1 . ASN B 1 62  ? 24.086  20.700  -49.251 1.00 32.23 ? 62  ASN B OD1 1 
ATOM   2378 N ND2 . ASN B 1 62  ? 25.253  19.291  -47.968 1.00 28.15 ? 62  ASN B ND2 1 
ATOM   2379 N N   . GLY B 1 63  ? 21.167  16.081  -49.807 1.00 29.47 ? 63  GLY B N   1 
ATOM   2380 C CA  . GLY B 1 63  ? 20.583  15.111  -50.711 1.00 28.19 ? 63  GLY B CA  1 
ATOM   2381 C C   . GLY B 1 63  ? 21.584  14.358  -51.555 1.00 32.85 ? 63  GLY B C   1 
ATOM   2382 O O   . GLY B 1 63  ? 21.176  13.657  -52.487 1.00 33.48 ? 63  GLY B O   1 
ATOM   2383 N N   . ARG B 1 64  ? 22.885  14.498  -51.275 1.00 28.71 ? 64  ARG B N   1 
ATOM   2384 C CA  . ARG B 1 64  ? 23.927  13.782  -51.996 1.00 32.23 ? 64  ARG B CA  1 
ATOM   2385 C C   . ARG B 1 64  ? 25.144  13.581  -51.093 1.00 29.89 ? 64  ARG B C   1 
ATOM   2386 O O   . ARG B 1 64  ? 25.392  14.363  -50.173 1.00 29.89 ? 64  ARG B O   1 
ATOM   2387 C CB  . ARG B 1 64  ? 24.355  14.540  -53.256 1.00 33.51 ? 64  ARG B CB  1 
ATOM   2388 C CG  . ARG B 1 64  ? 24.840  15.953  -52.922 1.00 33.82 ? 64  ARG B CG  1 
ATOM   2389 C CD  . ARG B 1 64  ? 25.356  16.689  -54.130 1.00 40.12 ? 64  ARG B CD  1 
ATOM   2390 N NE  . ARG B 1 64  ? 25.619  18.089  -53.816 1.00 45.92 ? 64  ARG B NE  1 
ATOM   2391 C CZ  . ARG B 1 64  ? 26.780  18.538  -53.360 1.00 43.70 ? 64  ARG B CZ  1 
ATOM   2392 N NH1 . ARG B 1 64  ? 27.856  17.765  -53.335 1.00 44.62 ? 64  ARG B NH1 1 
ATOM   2393 N NH2 . ARG B 1 64  ? 26.884  19.810  -52.986 1.00 44.07 ? 64  ARG B NH2 1 
ATOM   2394 N N   . GLU B 1 65  ? 25.906  12.534  -51.381 1.00 29.08 ? 65  GLU B N   1 
ATOM   2395 C CA  . GLU B 1 65  ? 27.098  12.213  -50.610 1.00 29.59 ? 65  GLU B CA  1 
ATOM   2396 C C   . GLU B 1 65  ? 28.139  13.316  -50.721 1.00 29.11 ? 65  GLU B C   1 
ATOM   2397 O O   . GLU B 1 65  ? 28.280  13.925  -51.782 1.00 31.90 ? 65  GLU B O   1 
ATOM   2398 C CB  . GLU B 1 65  ? 27.758  10.938  -51.124 1.00 33.29 ? 65  GLU B CB  1 
ATOM   2399 C CG  . GLU B 1 65  ? 27.121  9.660   -50.781 1.00 34.16 ? 65  GLU B CG  1 
ATOM   2400 C CD  . GLU B 1 65  ? 28.004  8.500   -51.239 1.00 34.05 ? 65  GLU B CD  1 
ATOM   2401 O OE1 . GLU B 1 65  ? 29.094  8.301   -50.660 1.00 32.35 ? 65  GLU B OE1 1 
ATOM   2402 O OE2 . GLU B 1 65  ? 27.610  7.814   -52.199 1.00 38.76 ? 65  GLU B OE2 1 
ATOM   2403 N N   . PRO B 1 66  ? 28.908  13.573  -49.671 1.00 28.60 ? 66  PRO B N   1 
ATOM   2404 C CA  . PRO B 1 66  ? 30.071  14.447  -49.828 1.00 29.08 ? 66  PRO B CA  1 
ATOM   2405 C C   . PRO B 1 66  ? 31.156  13.703  -50.589 1.00 31.82 ? 66  PRO B C   1 
ATOM   2406 O O   . PRO B 1 66  ? 31.296  12.486  -50.466 1.00 30.25 ? 66  PRO B O   1 
ATOM   2407 C CB  . PRO B 1 66  ? 30.504  14.735  -48.390 1.00 27.81 ? 66  PRO B CB  1 
ATOM   2408 C CG  . PRO B 1 66  ? 30.037  13.537  -47.620 1.00 26.98 ? 66  PRO B CG  1 
ATOM   2409 C CD  . PRO B 1 66  ? 28.769  13.060  -48.294 1.00 27.47 ? 66  PRO B CD  1 
ATOM   2410 N N   . ASN B 1 67  ? 31.953  14.461  -51.345 1.00 31.83 ? 67  ASN B N   1 
ATOM   2411 C CA  . ASN B 1 67  ? 33.053  13.885  -52.117 1.00 30.65 ? 67  ASN B CA  1 
ATOM   2412 C C   . ASN B 1 67  ? 34.169  13.384  -51.222 1.00 32.24 ? 67  ASN B C   1 
ATOM   2413 O O   . ASN B 1 67  ? 34.958  12.519  -51.626 1.00 30.54 ? 67  ASN B O   1 
ATOM   2414 C CB  . ASN B 1 67  ? 33.586  14.937  -53.078 1.00 33.49 ? 67  ASN B CB  1 
ATOM   2415 C CG  . ASN B 1 67  ? 32.757  15.028  -54.319 1.00 37.34 ? 67  ASN B CG  1 
ATOM   2416 O OD1 . ASN B 1 67  ? 32.040  14.096  -54.658 1.00 40.98 ? 67  ASN B OD1 1 
ATOM   2417 N ND2 . ASN B 1 67  ? 32.814  16.163  -54.987 1.00 46.43 ? 67  ASN B ND2 1 
ATOM   2418 N N   . TYR B 1 68  ? 34.288  13.952  -50.030 1.00 29.60 ? 68  TYR B N   1 
ATOM   2419 C CA  . TYR B 1 68  ? 35.249  13.498  -49.040 1.00 29.50 ? 68  TYR B CA  1 
ATOM   2420 C C   . TYR B 1 68  ? 34.789  14.059  -47.710 1.00 28.01 ? 68  TYR B C   1 
ATOM   2421 O O   . TYR B 1 68  ? 33.971  14.983  -47.662 1.00 31.26 ? 68  TYR B O   1 
ATOM   2422 C CB  . TYR B 1 68  ? 36.671  13.966  -49.384 1.00 33.67 ? 68  TYR B CB  1 
ATOM   2423 C CG  . TYR B 1 68  ? 36.812  15.470  -49.337 1.00 32.74 ? 68  TYR B CG  1 
ATOM   2424 C CD1 . TYR B 1 68  ? 37.010  16.138  -48.133 1.00 35.52 ? 68  TYR B CD1 1 
ATOM   2425 C CD2 . TYR B 1 68  ? 36.659  16.233  -50.489 1.00 35.96 ? 68  TYR B CD2 1 
ATOM   2426 C CE1 . TYR B 1 68  ? 37.111  17.508  -48.086 1.00 37.73 ? 68  TYR B CE1 1 
ATOM   2427 C CE2 . TYR B 1 68  ? 36.753  17.619  -50.447 1.00 35.84 ? 68  TYR B CE2 1 
ATOM   2428 C CZ  . TYR B 1 68  ? 36.978  18.244  -49.244 1.00 40.66 ? 68  TYR B CZ  1 
ATOM   2429 O OH  . TYR B 1 68  ? 37.065  19.618  -49.192 1.00 48.70 ? 68  TYR B OH  1 
ATOM   2430 N N   . VAL B 1 69  ? 35.318  13.495  -46.635 1.00 25.74 ? 69  VAL B N   1 
ATOM   2431 C CA  . VAL B 1 69  ? 35.019  13.954  -45.286 1.00 29.64 ? 69  VAL B CA  1 
ATOM   2432 C C   . VAL B 1 69  ? 36.319  13.996  -44.508 1.00 32.11 ? 69  VAL B C   1 
ATOM   2433 O O   . VAL B 1 69  ? 37.076  13.017  -44.504 1.00 29.51 ? 69  VAL B O   1 
ATOM   2434 C CB  . VAL B 1 69  ? 33.987  13.066  -44.559 1.00 29.12 ? 69  VAL B CB  1 
ATOM   2435 C CG1 . VAL B 1 69  ? 33.722  13.611  -43.143 1.00 29.41 ? 69  VAL B CG1 1 
ATOM   2436 C CG2 . VAL B 1 69  ? 32.695  13.010  -45.341 1.00 27.39 ? 69  VAL B CG2 1 
ATOM   2437 N N   . THR B 1 70  ? 36.582  15.142  -43.878 1.00 30.78 ? 70  THR B N   1 
ATOM   2438 C CA  . THR B 1 70  ? 37.721  15.308  -42.991 1.00 31.08 ? 70  THR B CA  1 
ATOM   2439 C C   . THR B 1 70  ? 37.363  14.791  -41.617 1.00 31.97 ? 70  THR B C   1 
ATOM   2440 O O   . THR B 1 70  ? 36.280  15.085  -41.107 1.00 28.91 ? 70  THR B O   1 
ATOM   2441 C CB  . THR B 1 70  ? 38.082  16.789  -42.882 1.00 31.31 ? 70  THR B CB  1 
ATOM   2442 O OG1 . THR B 1 70  ? 38.364  17.307  -44.184 1.00 31.52 ? 70  THR B OG1 1 
ATOM   2443 C CG2 . THR B 1 70  ? 39.280  16.994  -41.972 1.00 33.30 ? 70  THR B CG2 1 
ATOM   2444 N N   . LEU B 1 71  ? 38.267  14.041  -41.009 1.00 30.75 ? 71  LEU B N   1 
ATOM   2445 C CA  . LEU B 1 71  ? 38.070  13.578  -39.640 1.00 30.98 ? 71  LEU B CA  1 
ATOM   2446 C C   . LEU B 1 71  ? 38.252  14.764  -38.701 1.00 34.45 ? 71  LEU B C   1 
ATOM   2447 O O   . LEU B 1 71  ? 39.378  15.177  -38.430 1.00 33.37 ? 71  LEU B O   1 
ATOM   2448 C CB  . LEU B 1 71  ? 39.064  12.471  -39.321 1.00 31.38 ? 71  LEU B CB  1 
ATOM   2449 C CG  . LEU B 1 71  ? 38.824  11.727  -38.016 1.00 36.51 ? 71  LEU B CG  1 
ATOM   2450 C CD1 . LEU B 1 71  ? 37.345  11.312  -37.925 1.00 35.14 ? 71  LEU B CD1 1 
ATOM   2451 C CD2 . LEU B 1 71  ? 39.758  10.528  -37.928 1.00 39.29 ? 71  LEU B CD2 1 
ATOM   2452 N N   . THR B 1 72  ? 37.154  15.321  -38.178 1.00 31.29 ? 72  THR B N   1 
ATOM   2453 C CA  . THR B 1 72  ? 37.252  16.510  -37.341 1.00 34.30 ? 72  THR B CA  1 
ATOM   2454 C C   . THR B 1 72  ? 36.690  16.317  -35.948 1.00 34.93 ? 72  THR B C   1 
ATOM   2455 O O   . THR B 1 72  ? 36.913  17.181  -35.094 1.00 30.72 ? 72  THR B O   1 
ATOM   2456 C CB  . THR B 1 72  ? 36.489  17.700  -37.952 1.00 35.78 ? 72  THR B CB  1 
ATOM   2457 O OG1 . THR B 1 72  ? 35.182  17.282  -38.351 1.00 34.23 ? 72  THR B OG1 1 
ATOM   2458 C CG2 . THR B 1 72  ? 37.206  18.217  -39.176 1.00 34.45 ? 72  THR B CG2 1 
ATOM   2459 N N   . SER B 1 73  ? 35.960  15.232  -35.696 1.00 33.11 ? 73  SER B N   1 
ATOM   2460 C CA  . SER B 1 73  ? 35.140  15.127  -34.500 1.00 34.28 ? 73  SER B CA  1 
ATOM   2461 C C   . SER B 1 73  ? 35.019  13.661  -34.095 1.00 34.33 ? 73  SER B C   1 
ATOM   2462 O O   . SER B 1 73  ? 35.342  12.744  -34.862 1.00 31.58 ? 73  SER B O   1 
ATOM   2463 C CB  . SER B 1 73  ? 33.764  15.714  -34.754 1.00 34.60 ? 73  SER B CB  1 
ATOM   2464 O OG  . SER B 1 73  ? 33.184  14.998  -35.831 1.00 39.14 ? 73  SER B OG  1 
ATOM   2465 N N   . VAL B 1 74  ? 34.496  13.451  -32.892 1.00 30.71 ? 74  VAL B N   1 
ATOM   2466 C CA  . VAL B 1 74  ? 34.190  12.128  -32.376 1.00 30.08 ? 74  VAL B CA  1 
ATOM   2467 C C   . VAL B 1 74  ? 32.707  12.124  -32.035 1.00 32.97 ? 74  VAL B C   1 
ATOM   2468 O O   . VAL B 1 74  ? 32.084  13.181  -31.928 1.00 31.13 ? 74  VAL B O   1 
ATOM   2469 C CB  . VAL B 1 74  ? 35.042  11.790  -31.135 1.00 32.11 ? 74  VAL B CB  1 
ATOM   2470 C CG1 . VAL B 1 74  ? 36.540  11.741  -31.509 1.00 35.59 ? 74  VAL B CG1 1 
ATOM   2471 C CG2 . VAL B 1 74  ? 34.807  12.796  -30.027 1.00 32.94 ? 74  VAL B CG2 1 
ATOM   2472 N N   . ALA B 1 75  ? 32.131  10.926  -31.918 1.00 27.48 ? 75  ALA B N   1 
ATOM   2473 C CA  . ALA B 1 75  ? 30.721  10.781  -31.565 1.00 29.75 ? 75  ALA B CA  1 
ATOM   2474 C C   . ALA B 1 75  ? 30.485  9.375   -31.036 1.00 31.34 ? 75  ALA B C   1 
ATOM   2475 O O   . ALA B 1 75  ? 31.310  8.478   -31.225 1.00 28.85 ? 75  ALA B O   1 
ATOM   2476 C CB  . ALA B 1 75  ? 29.802  11.067  -32.757 1.00 28.08 ? 75  ALA B CB  1 
ATOM   2477 N N   . ARG B 1 76  ? 29.346  9.196   -30.358 1.00 28.44 ? 76  ARG B N   1 
ATOM   2478 C CA  . ARG B 1 76  ? 28.965  7.894   -29.828 1.00 29.93 ? 76  ARG B CA  1 
ATOM   2479 C C   . ARG B 1 76  ? 28.388  6.988   -30.904 1.00 31.84 ? 76  ARG B C   1 
ATOM   2480 O O   . ARG B 1 76  ? 28.430  5.767   -30.755 1.00 35.44 ? 76  ARG B O   1 
ATOM   2481 C CB  . ARG B 1 76  ? 27.926  8.064   -28.710 1.00 34.85 ? 76  ARG B CB  1 
ATOM   2482 C CG  . ARG B 1 76  ? 28.488  8.391   -27.335 1.00 38.45 ? 76  ARG B CG  1 
ATOM   2483 C CD  . ARG B 1 76  ? 27.375  8.395   -26.267 1.00 47.07 ? 76  ARG B CD  1 
ATOM   2484 N NE  . ARG B 1 76  ? 26.329  9.384   -26.526 1.00 51.31 ? 76  ARG B NE  1 
ATOM   2485 C CZ  . ARG B 1 76  ? 25.019  9.142   -26.482 1.00 51.42 ? 76  ARG B CZ  1 
ATOM   2486 N NH1 . ARG B 1 76  ? 24.540  7.932   -26.216 1.00 47.35 ? 76  ARG B NH1 1 
ATOM   2487 N NH2 . ARG B 1 76  ? 24.165  10.138  -26.721 1.00 47.57 ? 76  ARG B NH2 1 
ATOM   2488 N N   . ASN B 1 77  ? 27.846  7.568   -31.970 1.00 29.31 ? 77  ASN B N   1 
ATOM   2489 C CA  . ASN B 1 77  ? 27.232  6.834   -33.066 1.00 25.02 ? 77  ASN B CA  1 
ATOM   2490 C C   . ASN B 1 77  ? 27.137  7.782   -34.242 1.00 22.81 ? 77  ASN B C   1 
ATOM   2491 O O   . ASN B 1 77  ? 27.334  8.989   -34.085 1.00 23.03 ? 77  ASN B O   1 
ATOM   2492 C CB  . ASN B 1 77  ? 25.839  6.308   -32.675 1.00 30.79 ? 77  ASN B CB  1 
ATOM   2493 C CG  . ASN B 1 77  ? 24.910  7.418   -32.286 1.00 29.45 ? 77  ASN B CG  1 
ATOM   2494 O OD1 . ASN B 1 77  ? 24.648  8.336   -33.069 1.00 27.77 ? 77  ASN B OD1 1 
ATOM   2495 N ND2 . ASN B 1 77  ? 24.422  7.362   -31.066 1.00 31.39 ? 77  ASN B ND2 1 
ATOM   2496 N N   . PRO B 1 78  ? 26.853  7.279   -35.439 1.00 25.98 ? 78  PRO B N   1 
ATOM   2497 C CA  . PRO B 1 78  ? 26.787  8.169   -36.606 1.00 26.31 ? 78  PRO B CA  1 
ATOM   2498 C C   . PRO B 1 78  ? 25.428  8.812   -36.837 1.00 25.75 ? 78  PRO B C   1 
ATOM   2499 O O   . PRO B 1 78  ? 25.237  9.401   -37.905 1.00 23.39 ? 78  PRO B O   1 
ATOM   2500 C CB  . PRO B 1 78  ? 27.130  7.223   -37.769 1.00 26.96 ? 78  PRO B CB  1 
ATOM   2501 C CG  . PRO B 1 78  ? 26.607  5.880   -37.293 1.00 26.61 ? 78  PRO B CG  1 
ATOM   2502 C CD  . PRO B 1 78  ? 26.873  5.852   -35.824 1.00 26.54 ? 78  PRO B CD  1 
ATOM   2503 N N   . LEU B 1 79  ? 24.479  8.677   -35.898 1.00 25.70 ? 79  LEU B N   1 
ATOM   2504 C CA  . LEU B 1 79  ? 23.104  9.084   -36.155 1.00 25.36 ? 79  LEU B CA  1 
ATOM   2505 C C   . LEU B 1 79  ? 23.004  10.604  -36.258 1.00 26.34 ? 79  LEU B C   1 
ATOM   2506 O O   . LEU B 1 79  ? 23.592  11.332  -35.450 1.00 26.12 ? 79  LEU B O   1 
ATOM   2507 C CB  . LEU B 1 79  ? 22.179  8.571   -35.048 1.00 27.13 ? 79  LEU B CB  1 
ATOM   2508 C CG  . LEU B 1 79  ? 20.749  9.128   -35.089 1.00 29.45 ? 79  LEU B CG  1 
ATOM   2509 C CD1 . LEU B 1 79  ? 20.066  8.557   -36.282 1.00 26.80 ? 79  LEU B CD1 1 
ATOM   2510 C CD2 . LEU B 1 79  ? 19.977  8.787   -33.817 1.00 29.24 ? 79  LEU B CD2 1 
ATOM   2511 N N   . VAL B 1 80  ? 22.277  11.075  -37.273 1.00 25.11 ? 80  VAL B N   1 
ATOM   2512 C CA  . VAL B 1 80  ? 21.964  12.492  -37.469 1.00 25.14 ? 80  VAL B CA  1 
ATOM   2513 C C   . VAL B 1 80  ? 20.441  12.622  -37.529 1.00 24.65 ? 80  VAL B C   1 
ATOM   2514 O O   . VAL B 1 80  ? 19.782  11.877  -38.274 1.00 22.73 ? 80  VAL B O   1 
ATOM   2515 C CB  . VAL B 1 80  ? 22.618  13.043  -38.753 1.00 23.76 ? 80  VAL B CB  1 
ATOM   2516 C CG1 . VAL B 1 80  ? 22.068  14.421  -39.100 1.00 26.77 ? 80  VAL B CG1 1 
ATOM   2517 C CG2 . VAL B 1 80  ? 24.176  13.060  -38.640 1.00 24.37 ? 80  VAL B CG2 1 
ATOM   2518 N N   . MET B 1 81  ? 19.876  13.527  -36.718 1.00 24.00 ? 81  MET B N   1 
ATOM   2519 C CA  . MET B 1 81  ? 18.422  13.731  -36.742 1.00 24.06 ? 81  MET B CA  1 
ATOM   2520 C C   . MET B 1 81  ? 17.965  14.007  -38.156 1.00 26.45 ? 81  MET B C   1 
ATOM   2521 O O   . MET B 1 81  ? 18.612  14.750  -38.899 1.00 26.66 ? 81  MET B O   1 
ATOM   2522 C CB  . MET B 1 81  ? 18.008  14.905  -35.857 1.00 25.88 ? 81  MET B CB  1 
ATOM   2523 C CG  . MET B 1 81  ? 16.503  14.963  -35.488 1.00 27.39 ? 81  MET B CG  1 
ATOM   2524 S SD  . MET B 1 81  ? 15.695  13.343  -35.394 1.00 30.03 ? 81  MET B SD  1 
ATOM   2525 C CE  . MET B 1 81  ? 14.014  13.801  -35.842 1.00 30.77 ? 81  MET B CE  1 
ATOM   2526 N N   . ASP B 1 82  ? 16.877  13.351  -38.542 1.00 22.12 ? 82  ASP B N   1 
ATOM   2527 C CA  . ASP B 1 82  ? 16.267  13.526  -39.857 1.00 21.99 ? 82  ASP B CA  1 
ATOM   2528 C C   . ASP B 1 82  ? 14.748  13.537  -39.681 1.00 26.50 ? 82  ASP B C   1 
ATOM   2529 O O   . ASP B 1 82  ? 14.198  12.649  -39.033 1.00 29.41 ? 82  ASP B O   1 
ATOM   2530 C CB  . ASP B 1 82  ? 16.703  12.428  -40.818 1.00 22.89 ? 82  ASP B CB  1 
ATOM   2531 C CG  . ASP B 1 82  ? 16.292  12.718  -42.227 1.00 27.18 ? 82  ASP B CG  1 
ATOM   2532 O OD1 . ASP B 1 82  ? 15.985  13.897  -42.519 1.00 24.16 ? 82  ASP B OD1 1 
ATOM   2533 O OD2 . ASP B 1 82  ? 16.284  11.770  -43.048 1.00 26.17 ? 82  ASP B OD2 1 
ATOM   2534 N N   . TYR B 1 83  ? 14.080  14.571  -40.174 1.00 27.77 ? 83  TYR B N   1 
ATOM   2535 C CA  . TYR B 1 83  ? 12.637  14.736  -39.985 1.00 27.62 ? 83  TYR B CA  1 
ATOM   2536 C C   . TYR B 1 83  ? 11.833  14.192  -41.155 1.00 26.97 ? 83  TYR B C   1 
ATOM   2537 O O   . TYR B 1 83  ? 12.292  14.180  -42.295 1.00 28.84 ? 83  TYR B O   1 
ATOM   2538 C CB  . TYR B 1 83  ? 12.301  16.217  -39.788 1.00 25.29 ? 83  TYR B CB  1 
ATOM   2539 C CG  . TYR B 1 83  ? 13.116  16.855  -38.718 1.00 24.96 ? 83  TYR B CG  1 
ATOM   2540 C CD1 . TYR B 1 83  ? 14.356  17.453  -39.023 1.00 28.77 ? 83  TYR B CD1 1 
ATOM   2541 C CD2 . TYR B 1 83  ? 12.668  16.897  -37.414 1.00 27.13 ? 83  TYR B CD2 1 
ATOM   2542 C CE1 . TYR B 1 83  ? 15.112  18.077  -38.041 1.00 25.19 ? 83  TYR B CE1 1 
ATOM   2543 C CE2 . TYR B 1 83  ? 13.422  17.514  -36.419 1.00 28.28 ? 83  TYR B CE2 1 
ATOM   2544 C CZ  . TYR B 1 83  ? 14.657  18.092  -36.765 1.00 29.60 ? 83  TYR B CZ  1 
ATOM   2545 O OH  . TYR B 1 83  ? 15.415  18.698  -35.798 1.00 35.95 ? 83  TYR B OH  1 
ATOM   2546 N N   . GLN B 1 84  ? 10.596  13.803  -40.883 1.00 25.51 ? 84  GLN B N   1 
ATOM   2547 C CA  . GLN B 1 84  ? 9.739   13.398  -41.982 1.00 25.32 ? 84  GLN B CA  1 
ATOM   2548 C C   . GLN B 1 84  ? 9.387   14.610  -42.835 1.00 30.01 ? 84  GLN B C   1 
ATOM   2549 O O   . GLN B 1 84  ? 9.153   15.709  -42.319 1.00 26.09 ? 84  GLN B O   1 
ATOM   2550 C CB  . GLN B 1 84  ? 8.475   12.727  -41.465 1.00 27.50 ? 84  GLN B CB  1 
ATOM   2551 C CG  . GLN B 1 84  ? 7.644   13.527  -40.440 1.00 25.99 ? 84  GLN B CG  1 
ATOM   2552 C CD  . GLN B 1 84  ? 6.520   12.667  -39.852 1.00 29.53 ? 84  GLN B CD  1 
ATOM   2553 O OE1 . GLN B 1 84  ? 6.714   11.978  -38.849 1.00 26.94 ? 84  GLN B OE1 1 
ATOM   2554 N NE2 . GLN B 1 84  ? 5.366   12.685  -40.487 1.00 30.95 ? 84  GLN B NE2 1 
ATOM   2555 N N   . ASN B 1 85  ? 9.300   14.384  -44.148 1.00 29.87 ? 85  ASN B N   1 
ATOM   2556 C CA  . ASN B 1 85  ? 9.042   15.445  -45.101 1.00 32.11 ? 85  ASN B CA  1 
ATOM   2557 C C   . ASN B 1 85  ? 7.567   15.665  -45.351 1.00 33.36 ? 85  ASN B C   1 
ATOM   2558 O O   . ASN B 1 85  ? 7.218   16.657  -45.999 1.00 30.01 ? 85  ASN B O   1 
ATOM   2559 C CB  . ASN B 1 85  ? 9.768   15.176  -46.440 1.00 34.07 ? 85  ASN B CB  1 
ATOM   2560 C CG  . ASN B 1 85  ? 9.166   14.006  -47.236 1.00 42.98 ? 85  ASN B CG  1 
ATOM   2561 O OD1 . ASN B 1 85  ? 8.333   13.228  -46.745 1.00 36.01 ? 85  ASN B OD1 1 
ATOM   2562 N ND2 . ASN B 1 85  ? 9.622   13.868  -48.486 1.00 46.93 ? 85  ASN B ND2 1 
ATOM   2563 N N   . THR B 1 86  ? 6.719   14.726  -44.918 1.00 29.90 ? 86  THR B N   1 
ATOM   2564 C CA  . THR B 1 86  ? 5.279   14.825  -45.007 1.00 32.32 ? 86  THR B CA  1 
ATOM   2565 C C   . THR B 1 86  ? 4.666   14.323  -43.707 1.00 33.34 ? 86  THR B C   1 
ATOM   2566 O O   . THR B 1 86  ? 5.347   13.751  -42.851 1.00 29.77 ? 86  THR B O   1 
ATOM   2567 C CB  . THR B 1 86  ? 4.735   13.988  -46.158 1.00 38.73 ? 86  THR B CB  1 
ATOM   2568 O OG1 . THR B 1 86  ? 4.724   12.607  -45.756 1.00 34.75 ? 86  THR B OG1 1 
ATOM   2569 C CG2 . THR B 1 86  ? 5.606   14.148  -47.414 1.00 33.64 ? 86  THR B CG2 1 
ATOM   2570 N N   . ASN B 1 87  ? 3.355   14.490  -43.579 1.00 32.56 ? 87  ASN B N   1 
ATOM   2571 C CA  . ASN B 1 87  ? 2.697   13.968  -42.388 1.00 37.76 ? 87  ASN B CA  1 
ATOM   2572 C C   . ASN B 1 87  ? 2.463   12.464  -42.477 1.00 32.60 ? 87  ASN B C   1 
ATOM   2573 O O   . ASN B 1 87  ? 1.895   11.887  -41.546 1.00 33.70 ? 87  ASN B O   1 
ATOM   2574 C CB  . ASN B 1 87  ? 1.353   14.669  -42.154 1.00 37.95 ? 87  ASN B CB  1 
ATOM   2575 C CG  . ASN B 1 87  ? 0.423   14.509  -43.328 1.00 42.63 ? 87  ASN B CG  1 
ATOM   2576 O OD1 . ASN B 1 87  ? 0.862   14.492  -44.476 1.00 47.71 ? 87  ASN B OD1 1 
ATOM   2577 N ND2 . ASN B 1 87  ? -0.862  14.375  -43.056 1.00 49.13 ? 87  ASN B ND2 1 
ATOM   2578 N N   . TYR B 1 88  ? 2.897   11.801  -43.554 1.00 29.59 ? 88  TYR B N   1 
ATOM   2579 C CA  . TYR B 1 88  ? 2.644   10.371  -43.689 1.00 32.42 ? 88  TYR B CA  1 
ATOM   2580 C C   . TYR B 1 88  ? 3.904   9.539   -43.915 1.00 30.12 ? 88  TYR B C   1 
ATOM   2581 O O   . TYR B 1 88  ? 3.781   8.345   -44.235 1.00 27.77 ? 88  TYR B O   1 
ATOM   2582 C CB  . TYR B 1 88  ? 1.640   10.092  -44.827 1.00 34.28 ? 88  TYR B CB  1 
ATOM   2583 C CG  . TYR B 1 88  ? 2.105   10.605  -46.163 1.00 36.55 ? 88  TYR B CG  1 
ATOM   2584 C CD1 . TYR B 1 88  ? 2.922   9.822   -46.997 1.00 34.23 ? 88  TYR B CD1 1 
ATOM   2585 C CD2 . TYR B 1 88  ? 1.763   11.889  -46.596 1.00 36.00 ? 88  TYR B CD2 1 
ATOM   2586 C CE1 . TYR B 1 88  ? 3.348   10.313  -48.250 1.00 37.25 ? 88  TYR B CE1 1 
ATOM   2587 C CE2 . TYR B 1 88  ? 2.182   12.373  -47.847 1.00 38.19 ? 88  TYR B CE2 1 
ATOM   2588 C CZ  . TYR B 1 88  ? 2.959   11.579  -48.656 1.00 39.46 ? 88  TYR B CZ  1 
ATOM   2589 O OH  . TYR B 1 88  ? 3.388   12.073  -49.854 1.00 43.54 ? 88  TYR B OH  1 
ATOM   2590 N N   . THR B 1 89  ? 5.109   10.095  -43.695 1.00 24.42 ? 89  THR B N   1 
ATOM   2591 C CA  . THR B 1 89  ? 6.351   9.363   -43.948 1.00 26.93 ? 89  THR B CA  1 
ATOM   2592 C C   . THR B 1 89  ? 7.125   9.068   -42.658 1.00 25.27 ? 89  THR B C   1 
ATOM   2593 O O   . THR B 1 89  ? 8.336   8.824   -42.698 1.00 24.43 ? 89  THR B O   1 
ATOM   2594 C CB  . THR B 1 89  ? 7.256   10.101  -44.951 1.00 25.88 ? 89  THR B CB  1 
ATOM   2595 O OG1 . THR B 1 89  ? 7.350   11.497  -44.636 1.00 27.51 ? 89  THR B OG1 1 
ATOM   2596 C CG2 . THR B 1 89  ? 6.681   9.982   -46.363 1.00 27.23 ? 89  THR B CG2 1 
ATOM   2597 N N   . ALA B 1 90  ? 6.432   9.002   -41.513 1.00 20.96 ? 90  ALA B N   1 
ATOM   2598 C CA  . ALA B 1 90  ? 7.117   8.644   -40.268 1.00 24.39 ? 90  ALA B CA  1 
ATOM   2599 C C   . ALA B 1 90  ? 7.822   7.281   -40.360 1.00 24.82 ? 90  ALA B C   1 
ATOM   2600 O O   . ALA B 1 90  ? 8.948   7.126   -39.856 1.00 22.73 ? 90  ALA B O   1 
ATOM   2601 C CB  . ALA B 1 90  ? 6.137   8.640   -39.107 1.00 23.68 ? 90  ALA B CB  1 
ATOM   2602 N N   . CYS B 1 91  ? 7.186   6.279   -40.995 1.00 22.42 ? 91  CYS B N   1 
ATOM   2603 C CA  . CYS B 1 91  ? 7.812   4.953   -41.048 1.00 23.83 ? 91  CYS B CA  1 
ATOM   2604 C C   . CYS B 1 91  ? 9.055   4.930   -41.936 1.00 22.05 ? 91  CYS B C   1 
ATOM   2605 O O   . CYS B 1 91  ? 10.121  4.534   -41.448 1.00 24.49 ? 91  CYS B O   1 
ATOM   2606 C CB  . CYS B 1 91  ? 6.798   3.892   -41.487 1.00 23.16 ? 91  CYS B CB  1 
ATOM   2607 S SG  . CYS B 1 91  ? 7.403   2.167   -41.271 1.00 26.11 ? 91  CYS B SG  1 
ATOM   2608 N N   . PRO B 1 92  ? 9.019   5.332   -43.205 1.00 22.90 ? 92  PRO B N   1 
ATOM   2609 C CA  . PRO B 1 92  ? 10.295  5.369   -43.955 1.00 25.10 ? 92  PRO B CA  1 
ATOM   2610 C C   . PRO B 1 92  ? 11.341  6.287   -43.341 1.00 22.90 ? 92  PRO B C   1 
ATOM   2611 O O   . PRO B 1 92  ? 12.536  6.028   -43.510 1.00 23.34 ? 92  PRO B O   1 
ATOM   2612 C CB  . PRO B 1 92  ? 9.887   5.864   -45.347 1.00 26.34 ? 92  PRO B CB  1 
ATOM   2613 C CG  . PRO B 1 92  ? 8.538   6.527   -45.136 1.00 23.99 ? 92  PRO B CG  1 
ATOM   2614 C CD  . PRO B 1 92  ? 7.887   5.779   -44.031 1.00 23.57 ? 92  PRO B CD  1 
ATOM   2615 N N   . THR B 1 93  ? 10.959  7.363   -42.648 1.00 23.50 ? 93  THR B N   1 
ATOM   2616 C CA  . THR B 1 93  ? 11.996  8.170   -42.001 1.00 25.16 ? 93  THR B CA  1 
ATOM   2617 C C   . THR B 1 93  ? 12.669  7.417   -40.860 1.00 24.82 ? 93  THR B C   1 
ATOM   2618 O O   . THR B 1 93  ? 13.889  7.518   -40.685 1.00 21.03 ? 93  THR B O   1 
ATOM   2619 C CB  . THR B 1 93  ? 11.425  9.492   -41.490 1.00 25.46 ? 93  THR B CB  1 
ATOM   2620 O OG1 . THR B 1 93  ? 10.656  10.077  -42.531 1.00 25.02 ? 93  THR B OG1 1 
ATOM   2621 C CG2 . THR B 1 93  ? 12.565  10.451  -41.129 1.00 26.66 ? 93  THR B CG2 1 
ATOM   2622 N N   . SER B 1 94  ? 11.893  6.667   -40.067 1.00 20.23 ? 94  SER B N   1 
ATOM   2623 C CA  . SER B 1 94  ? 12.485  5.851   -39.005 1.00 21.55 ? 94  SER B CA  1 
ATOM   2624 C C   . SER B 1 94  ? 13.396  4.774   -39.584 1.00 22.00 ? 94  SER B C   1 
ATOM   2625 O O   . SER B 1 94  ? 14.411  4.420   -38.983 1.00 21.26 ? 94  SER B O   1 
ATOM   2626 C CB  . SER B 1 94  ? 11.384  5.188   -38.161 1.00 23.05 ? 94  SER B CB  1 
ATOM   2627 O OG  . SER B 1 94  ? 10.470  6.168   -37.655 1.00 22.97 ? 94  SER B OG  1 
ATOM   2628 N N   . LEU B 1 95  ? 13.023  4.209   -40.735 1.00 21.51 ? 95  LEU B N   1 
ATOM   2629 C CA  . LEU B 1 95  ? 13.869  3.203   -41.363 1.00 22.41 ? 95  LEU B CA  1 
ATOM   2630 C C   . LEU B 1 95  ? 15.140  3.848   -41.908 1.00 22.57 ? 95  LEU B C   1 
ATOM   2631 O O   . LEU B 1 95  ? 16.238  3.292   -41.769 1.00 22.49 ? 95  LEU B O   1 
ATOM   2632 C CB  . LEU B 1 95  ? 13.089  2.483   -42.457 1.00 21.88 ? 95  LEU B CB  1 
ATOM   2633 C CG  . LEU B 1 95  ? 13.890  1.414   -43.221 1.00 22.32 ? 95  LEU B CG  1 
ATOM   2634 C CD1 . LEU B 1 95  ? 14.513  0.408   -42.259 1.00 20.82 ? 95  LEU B CD1 1 
ATOM   2635 C CD2 . LEU B 1 95  ? 13.016  0.721   -44.237 1.00 23.02 ? 95  LEU B CD2 1 
ATOM   2636 N N   . SER B 1 96  ? 15.013  5.061   -42.453 1.00 21.25 ? 96  SER B N   1 
ATOM   2637 C CA  . SER B 1 96  ? 16.190  5.808   -42.878 1.00 21.90 ? 96  SER B CA  1 
ATOM   2638 C C   . SER B 1 96  ? 17.093  6.117   -41.695 1.00 23.44 ? 96  SER B C   1 
ATOM   2639 O O   . SER B 1 96  ? 18.322  5.962   -41.779 1.00 21.99 ? 96  SER B O   1 
ATOM   2640 C CB  . SER B 1 96  ? 15.748  7.100   -43.565 1.00 25.48 ? 96  SER B CB  1 
ATOM   2641 O OG  . SER B 1 96  ? 16.871  7.830   -44.050 1.00 24.61 ? 96  SER B OG  1 
ATOM   2642 N N   . LEU B 1 97  ? 16.505  6.508   -40.561 1.00 21.25 ? 97  LEU B N   1 
ATOM   2643 C CA  . LEU B 1 97  ? 17.308  6.712   -39.355 1.00 20.79 ? 97  LEU B CA  1 
ATOM   2644 C C   . LEU B 1 97  ? 18.047  5.438   -38.971 1.00 23.71 ? 97  LEU B C   1 
ATOM   2645 O O   . LEU B 1 97  ? 19.239  5.471   -38.639 1.00 25.62 ? 97  LEU B O   1 
ATOM   2646 C CB  . LEU B 1 97  ? 16.426  7.178   -38.199 1.00 21.05 ? 97  LEU B CB  1 
ATOM   2647 C CG  . LEU B 1 97  ? 15.822  8.573   -38.355 1.00 24.76 ? 97  LEU B CG  1 
ATOM   2648 C CD1 . LEU B 1 97  ? 14.825  8.841   -37.280 1.00 21.23 ? 97  LEU B CD1 1 
ATOM   2649 C CD2 . LEU B 1 97  ? 16.939  9.602   -38.281 1.00 25.08 ? 97  LEU B CD2 1 
ATOM   2650 N N   . ALA B 1 98  ? 17.349  4.299   -38.989 1.00 23.98 ? 98  ALA B N   1 
ATOM   2651 C CA  . ALA B 1 98  ? 18.021  3.036   -38.690 1.00 22.60 ? 98  ALA B CA  1 
ATOM   2652 C C   . ALA B 1 98  ? 19.172  2.784   -39.660 1.00 20.74 ? 98  ALA B C   1 
ATOM   2653 O O   . ALA B 1 98  ? 20.232  2.294   -39.262 1.00 21.92 ? 98  ALA B O   1 
ATOM   2654 C CB  . ALA B 1 98  ? 17.023  1.881   -38.741 1.00 19.64 ? 98  ALA B CB  1 
ATOM   2655 N N   . SER B 1 99  ? 18.969  3.080   -40.944 1.00 21.00 ? 99  SER B N   1 
ATOM   2656 C CA  . SER B 1 99  ? 19.989  2.759   -41.933 1.00 23.07 ? 99  SER B CA  1 
ATOM   2657 C C   . SER B 1 99  ? 21.278  3.517   -41.659 1.00 24.82 ? 99  SER B C   1 
ATOM   2658 O O   . SER B 1 99  ? 22.357  3.046   -42.034 1.00 24.77 ? 99  SER B O   1 
ATOM   2659 C CB  . SER B 1 99  ? 19.487  3.063   -43.347 1.00 22.40 ? 99  SER B CB  1 
ATOM   2660 O OG  . SER B 1 99  ? 19.455  4.456   -43.597 1.00 24.93 ? 99  SER B OG  1 
ATOM   2661 N N   . GLN B 1 100 ? 21.193  4.692   -41.017 1.00 21.04 ? 100 GLN B N   1 
ATOM   2662 C CA  . GLN B 1 100 ? 22.409  5.390   -40.591 1.00 25.11 ? 100 GLN B CA  1 
ATOM   2663 C C   . GLN B 1 100 ? 23.168  4.578   -39.552 1.00 25.73 ? 100 GLN B C   1 
ATOM   2664 O O   . GLN B 1 100 ? 24.388  4.391   -39.654 1.00 25.72 ? 100 GLN B O   1 
ATOM   2665 C CB  . GLN B 1 100 ? 22.078  6.759   -39.993 1.00 20.57 ? 100 GLN B CB  1 
ATOM   2666 C CG  . GLN B 1 100 ? 21.283  7.709   -40.830 1.00 21.30 ? 100 GLN B CG  1 
ATOM   2667 C CD  . GLN B 1 100 ? 21.187  9.071   -40.118 1.00 26.52 ? 100 GLN B CD  1 
ATOM   2668 O OE1 . GLN B 1 100 ? 22.147  9.517   -39.491 1.00 25.67 ? 100 GLN B OE1 1 
ATOM   2669 N NE2 . GLN B 1 100 ? 20.012  9.710   -40.182 1.00 20.11 ? 100 GLN B NE2 1 
ATOM   2670 N N   . MET B 1 101 ? 22.460  4.109   -38.530 1.00 22.52 ? 101 MET B N   1 
ATOM   2671 C CA  . MET B 1 101 ? 23.067  3.331   -37.458 1.00 23.00 ? 101 MET B CA  1 
ATOM   2672 C C   . MET B 1 101 ? 23.699  2.049   -37.985 1.00 24.17 ? 101 MET B C   1 
ATOM   2673 O O   . MET B 1 101 ? 24.646  1.535   -37.381 1.00 28.23 ? 101 MET B O   1 
ATOM   2674 C CB  . MET B 1 101 ? 22.004  2.950   -36.419 1.00 24.54 ? 101 MET B CB  1 
ATOM   2675 C CG  . MET B 1 101 ? 21.333  4.079   -35.650 1.00 31.52 ? 101 MET B CG  1 
ATOM   2676 S SD  . MET B 1 101 ? 22.591  4.850   -34.636 1.00 47.50 ? 101 MET B SD  1 
ATOM   2677 C CE  . MET B 1 101 ? 21.660  5.248   -33.183 1.00 39.22 ? 101 MET B CE  1 
ATOM   2678 N N   . LEU B 1 102 ? 23.167  1.496   -39.074 1.00 23.22 ? 102 LEU B N   1 
ATOM   2679 C CA  . LEU B 1 102 ? 23.672  0.244   -39.641 1.00 25.46 ? 102 LEU B CA  1 
ATOM   2680 C C   . LEU B 1 102 ? 24.738  0.465   -40.715 1.00 27.69 ? 102 LEU B C   1 
ATOM   2681 O O   . LEU B 1 102 ? 25.230  -0.506  -41.294 1.00 24.94 ? 102 LEU B O   1 
ATOM   2682 C CB  . LEU B 1 102 ? 22.513  -0.565  -40.233 1.00 24.19 ? 102 LEU B CB  1 
ATOM   2683 C CG  . LEU B 1 102 ? 21.466  -1.072  -39.233 1.00 23.61 ? 102 LEU B CG  1 
ATOM   2684 C CD1 . LEU B 1 102 ? 20.490  -1.940  -39.954 1.00 25.98 ? 102 LEU B CD1 1 
ATOM   2685 C CD2 . LEU B 1 102 ? 22.149  -1.862  -38.119 1.00 25.53 ? 102 LEU B CD2 1 
ATOM   2686 N N   . TYR B 1 103 ? 25.107  1.711   -40.981 1.00 23.34 ? 103 TYR B N   1 
ATOM   2687 C CA  . TYR B 1 103 ? 26.129  2.048   -41.965 1.00 27.83 ? 103 TYR B CA  1 
ATOM   2688 C C   . TYR B 1 103 ? 25.751  1.554   -43.350 1.00 26.95 ? 103 TYR B C   1 
ATOM   2689 O O   . TYR B 1 103 ? 26.594  1.046   -44.093 1.00 30.08 ? 103 TYR B O   1 
ATOM   2690 C CB  . TYR B 1 103 ? 27.505  1.512   -41.552 1.00 25.83 ? 103 TYR B CB  1 
ATOM   2691 C CG  . TYR B 1 103 ? 28.078  2.237   -40.349 1.00 27.73 ? 103 TYR B CG  1 
ATOM   2692 C CD1 . TYR B 1 103 ? 27.694  1.894   -39.063 1.00 27.41 ? 103 TYR B CD1 1 
ATOM   2693 C CD2 . TYR B 1 103 ? 29.006  3.260   -40.501 1.00 25.79 ? 103 TYR B CD2 1 
ATOM   2694 C CE1 . TYR B 1 103 ? 28.201  2.547   -37.973 1.00 25.65 ? 103 TYR B CE1 1 
ATOM   2695 C CE2 . TYR B 1 103 ? 29.530  3.916   -39.405 1.00 24.32 ? 103 TYR B CE2 1 
ATOM   2696 C CZ  . TYR B 1 103 ? 29.129  3.566   -38.155 1.00 25.68 ? 103 TYR B CZ  1 
ATOM   2697 O OH  . TYR B 1 103 ? 29.643  4.235   -37.055 1.00 27.83 ? 103 TYR B OH  1 
ATOM   2698 N N   . HIS B 1 104 ? 24.473  1.702   -43.691 1.00 24.80 ? 104 HIS B N   1 
ATOM   2699 C CA  . HIS B 1 104 ? 23.948  1.338   -45.006 1.00 27.99 ? 104 HIS B CA  1 
ATOM   2700 C C   . HIS B 1 104 ? 22.850  2.341   -45.348 1.00 26.09 ? 104 HIS B C   1 
ATOM   2701 O O   . HIS B 1 104 ? 21.679  2.011   -45.563 1.00 26.53 ? 104 HIS B O   1 
ATOM   2702 C CB  . HIS B 1 104 ? 23.456  -0.109  -44.998 1.00 27.10 ? 104 HIS B CB  1 
ATOM   2703 C CG  . HIS B 1 104 ? 23.207  -0.683  -46.359 1.00 28.65 ? 104 HIS B CG  1 
ATOM   2704 N ND1 . HIS B 1 104 ? 24.218  -0.962  -47.256 1.00 29.45 ? 104 HIS B ND1 1 
ATOM   2705 C CD2 . HIS B 1 104 ? 22.055  -1.049  -46.968 1.00 31.83 ? 104 HIS B CD2 1 
ATOM   2706 C CE1 . HIS B 1 104 ? 23.699  -1.455  -48.366 1.00 33.31 ? 104 HIS B CE1 1 
ATOM   2707 N NE2 . HIS B 1 104 ? 22.388  -1.530  -48.212 1.00 35.21 ? 104 HIS B NE2 1 
ATOM   2708 N N   . TYR B 1 105 ? 23.240  3.606   -45.410 1.00 26.61 ? 105 TYR B N   1 
ATOM   2709 C CA  . TYR B 1 105 ? 22.276  4.694   -45.443 1.00 23.86 ? 105 TYR B CA  1 
ATOM   2710 C C   . TYR B 1 105 ? 21.383  4.615   -46.662 1.00 25.92 ? 105 TYR B C   1 
ATOM   2711 O O   . TYR B 1 105 ? 21.857  4.462   -47.790 1.00 28.53 ? 105 TYR B O   1 
ATOM   2712 C CB  . TYR B 1 105 ? 22.990  6.049   -45.428 1.00 24.23 ? 105 TYR B CB  1 
ATOM   2713 C CG  . TYR B 1 105 ? 22.050  7.232   -45.616 1.00 22.92 ? 105 TYR B CG  1 
ATOM   2714 C CD1 . TYR B 1 105 ? 21.094  7.568   -44.653 1.00 22.07 ? 105 TYR B CD1 1 
ATOM   2715 C CD2 . TYR B 1 105 ? 22.115  7.991   -46.768 1.00 25.34 ? 105 TYR B CD2 1 
ATOM   2716 C CE1 . TYR B 1 105 ? 20.227  8.684   -44.844 1.00 23.15 ? 105 TYR B CE1 1 
ATOM   2717 C CE2 . TYR B 1 105 ? 21.282  9.079   -46.971 1.00 27.00 ? 105 TYR B CE2 1 
ATOM   2718 C CZ  . TYR B 1 105 ? 20.346  9.425   -46.015 1.00 23.66 ? 105 TYR B CZ  1 
ATOM   2719 O OH  . TYR B 1 105 ? 19.548  10.500  -46.289 1.00 26.49 ? 105 TYR B OH  1 
ATOM   2720 N N   . LYS B 1 106 ? 20.081  4.743   -46.423 1.00 21.59 ? 106 LYS B N   1 
ATOM   2721 C CA  . LYS B 1 106 ? 19.077  4.900   -47.459 1.00 23.07 ? 106 LYS B CA  1 
ATOM   2722 C C   . LYS B 1 106 ? 18.227  6.107   -47.077 1.00 26.46 ? 106 LYS B C   1 
ATOM   2723 O O   . LYS B 1 106 ? 17.815  6.219   -45.920 1.00 22.04 ? 106 LYS B O   1 
ATOM   2724 C CB  . LYS B 1 106 ? 18.204  3.640   -47.553 1.00 25.33 ? 106 LYS B CB  1 
ATOM   2725 C CG  . LYS B 1 106 ? 18.993  2.362   -47.868 1.00 26.51 ? 106 LYS B CG  1 
ATOM   2726 C CD  . LYS B 1 106 ? 19.412  2.287   -49.341 1.00 30.61 ? 106 LYS B CD  1 
ATOM   2727 C CE  . LYS B 1 106 ? 20.498  1.232   -49.556 1.00 29.84 ? 106 LYS B CE  1 
ATOM   2728 N NZ  . LYS B 1 106 ? 20.778  1.078   -51.014 1.00 35.64 ? 106 LYS B NZ  1 
ATOM   2729 N N   . SER B 1 107 ? 17.992  7.012   -48.031 1.00 20.96 ? 107 SER B N   1 
ATOM   2730 C CA  . SER B 1 107 ? 17.284  8.248   -47.764 1.00 26.13 ? 107 SER B CA  1 
ATOM   2731 C C   . SER B 1 107 ? 15.814  7.988   -47.415 1.00 27.47 ? 107 SER B C   1 
ATOM   2732 O O   . SER B 1 107 ? 15.247  6.934   -47.724 1.00 26.01 ? 107 SER B O   1 
ATOM   2733 C CB  . SER B 1 107 ? 17.400  9.177   -48.972 1.00 25.54 ? 107 SER B CB  1 
ATOM   2734 O OG  . SER B 1 107 ? 16.439  8.857   -49.958 1.00 26.27 ? 107 SER B OG  1 
ATOM   2735 N N   . GLU B 1 108 ? 15.190  8.980   -46.774 1.00 25.60 ? 108 GLU B N   1 
ATOM   2736 C CA  . GLU B 1 108 ? 13.759  8.862   -46.494 1.00 25.84 ? 108 GLU B CA  1 
ATOM   2737 C C   . GLU B 1 108 ? 12.979  8.576   -47.773 1.00 27.88 ? 108 GLU B C   1 
ATOM   2738 O O   . GLU B 1 108 ? 12.125  7.679   -47.812 1.00 22.80 ? 108 GLU B O   1 
ATOM   2739 C CB  . GLU B 1 108 ? 13.239  10.135  -45.824 1.00 27.68 ? 108 GLU B CB  1 
ATOM   2740 C CG  . GLU B 1 108 ? 11.711  10.174  -45.729 1.00 28.81 ? 108 GLU B CG  1 
ATOM   2741 C CD  . GLU B 1 108 ? 11.206  11.454  -45.101 1.00 33.35 ? 108 GLU B CD  1 
ATOM   2742 O OE1 . GLU B 1 108 ? 12.020  12.177  -44.487 1.00 34.69 ? 108 GLU B OE1 1 
ATOM   2743 O OE2 . GLU B 1 108 ? 10.008  11.757  -45.262 1.00 31.14 ? 108 GLU B OE2 1 
ATOM   2744 N N   . SER B 1 109 ? 13.314  9.292   -48.845 1.00 28.81 ? 109 SER B N   1 
ATOM   2745 C CA  . SER B 1 109 ? 12.638  9.104   -50.125 1.00 29.43 ? 109 SER B CA  1 
ATOM   2746 C C   . SER B 1 109 ? 12.844  7.687   -50.665 1.00 27.91 ? 109 SER B C   1 
ATOM   2747 O O   . SER B 1 109 ? 11.894  7.058   -51.146 1.00 28.82 ? 109 SER B O   1 
ATOM   2748 C CB  . SER B 1 109 ? 13.135  10.149  -51.132 1.00 31.50 ? 109 SER B CB  1 
ATOM   2749 O OG  . SER B 1 109 ? 12.460  9.991   -52.365 1.00 36.06 ? 109 SER B OG  1 
ATOM   2750 N N   . GLU B 1 110 ? 14.086  7.176   -50.629 1.00 26.86 ? 110 GLU B N   1 
ATOM   2751 C CA  . GLU B 1 110 ? 14.314  5.798   -51.072 1.00 26.67 ? 110 GLU B CA  1 
ATOM   2752 C C   . GLU B 1 110 ? 13.484  4.815   -50.253 1.00 30.21 ? 110 GLU B C   1 
ATOM   2753 O O   . GLU B 1 110 ? 12.906  3.865   -50.796 1.00 30.17 ? 110 GLU B O   1 
ATOM   2754 C CB  . GLU B 1 110 ? 15.783  5.403   -50.939 1.00 27.08 ? 110 GLU B CB  1 
ATOM   2755 C CG  . GLU B 1 110 ? 16.747  6.175   -51.756 1.00 34.43 ? 110 GLU B CG  1 
ATOM   2756 C CD  . GLU B 1 110 ? 18.149  5.654   -51.554 1.00 38.13 ? 110 GLU B CD  1 
ATOM   2757 O OE1 . GLU B 1 110 ? 18.986  6.375   -50.953 1.00 34.41 ? 110 GLU B OE1 1 
ATOM   2758 O OE2 . GLU B 1 110 ? 18.382  4.501   -51.972 1.00 41.21 ? 110 GLU B OE2 1 
ATOM   2759 N N   . CYS B 1 111 ? 13.446  5.008   -48.939 1.00 26.05 ? 111 CYS B N   1 
ATOM   2760 C CA  . CYS B 1 111 ? 12.703  4.084   -48.088 1.00 28.13 ? 111 CYS B CA  1 
ATOM   2761 C C   . CYS B 1 111 ? 11.201  4.170   -48.364 1.00 29.66 ? 111 CYS B C   1 
ATOM   2762 O O   . CYS B 1 111 ? 10.505  3.139   -48.381 1.00 28.92 ? 111 CYS B O   1 
ATOM   2763 C CB  . CYS B 1 111 ? 13.008  4.374   -46.612 1.00 24.52 ? 111 CYS B CB  1 
ATOM   2764 S SG  . CYS B 1 111 ? 14.728  3.992   -46.096 1.00 25.27 ? 111 CYS B SG  1 
ATOM   2765 N N   . ALA B 1 112 ? 10.670  5.384   -48.564 1.00 29.35 ? 112 ALA B N   1 
ATOM   2766 C CA  . ALA B 1 112 ? 9.231   5.503   -48.814 1.00 29.45 ? 112 ALA B CA  1 
ATOM   2767 C C   . ALA B 1 112 ? 8.831   4.783   -50.094 1.00 30.33 ? 112 ALA B C   1 
ATOM   2768 O O   . ALA B 1 112 ? 7.836   4.041   -50.128 1.00 30.40 ? 112 ALA B O   1 
ATOM   2769 C CB  . ALA B 1 112 ? 8.824   6.979   -48.888 1.00 29.15 ? 112 ALA B CB  1 
ATOM   2770 N N   . LYS B 1 113 ? 9.601   4.982   -51.156 1.00 28.08 ? 113 LYS B N   1 
ATOM   2771 C CA  . LYS B 1 113 ? 9.302   4.305   -52.410 1.00 32.78 ? 113 LYS B CA  1 
ATOM   2772 C C   . LYS B 1 113 ? 9.381   2.795   -52.258 1.00 31.46 ? 113 LYS B C   1 
ATOM   2773 O O   . LYS B 1 113 ? 8.521   2.075   -52.769 1.00 29.50 ? 113 LYS B O   1 
ATOM   2774 C CB  . LYS B 1 113 ? 10.247  4.797   -53.503 1.00 35.41 ? 113 LYS B CB  1 
ATOM   2775 C CG  . LYS B 1 113 ? 10.099  6.309   -53.754 1.00 33.88 ? 113 LYS B CG  1 
ATOM   2776 C CD  . LYS B 1 113 ? 10.660  6.674   -55.133 1.00 43.71 ? 113 LYS B CD  1 
ATOM   2777 C CE  . LYS B 1 113 ? 11.453  7.962   -55.098 1.00 39.28 ? 113 LYS B CE  1 
ATOM   2778 N NZ  . LYS B 1 113 ? 11.835  8.373   -56.488 1.00 46.79 ? 113 LYS B NZ  1 
ATOM   2779 N N   . ALA B 1 114 ? 10.403  2.290   -51.564 1.00 30.25 ? 114 ALA B N   1 
ATOM   2780 C CA  . ALA B 1 114 ? 10.509  0.835   -51.433 1.00 30.77 ? 114 ALA B CA  1 
ATOM   2781 C C   . ALA B 1 114 ? 9.369   0.266   -50.589 1.00 31.31 ? 114 ALA B C   1 
ATOM   2782 O O   . ALA B 1 114 ? 8.795   -0.776  -50.930 1.00 30.02 ? 114 ALA B O   1 
ATOM   2783 C CB  . ALA B 1 114 ? 11.869  0.440   -50.845 1.00 30.59 ? 114 ALA B CB  1 
ATOM   2784 N N   . LEU B 1 115 ? 9.008   0.943   -49.500 1.00 29.11 ? 115 LEU B N   1 
ATOM   2785 C CA  . LEU B 1 115 ? 7.961   0.421   -48.638 1.00 32.88 ? 115 LEU B CA  1 
ATOM   2786 C C   . LEU B 1 115 ? 6.567   0.561   -49.243 1.00 29.89 ? 115 LEU B C   1 
ATOM   2787 O O   . LEU B 1 115 ? 5.633   -0.093  -48.771 1.00 30.83 ? 115 LEU B O   1 
ATOM   2788 C CB  . LEU B 1 115 ? 8.007   1.130   -47.279 1.00 32.11 ? 115 LEU B CB  1 
ATOM   2789 C CG  . LEU B 1 115 ? 9.296   1.005   -46.467 1.00 30.51 ? 115 LEU B CG  1 
ATOM   2790 C CD1 . LEU B 1 115 ? 9.067   1.618   -45.083 1.00 26.88 ? 115 LEU B CD1 1 
ATOM   2791 C CD2 . LEU B 1 115 ? 9.850   -0.445  -46.388 1.00 25.64 ? 115 LEU B CD2 1 
ATOM   2792 N N   . GLY B 1 116 ? 6.398   1.415   -50.245 1.00 32.07 ? 116 GLY B N   1 
ATOM   2793 C CA  . GLY B 1 116 ? 5.081   1.720   -50.760 1.00 30.73 ? 116 GLY B CA  1 
ATOM   2794 C C   . GLY B 1 116 ? 4.276   2.666   -49.890 1.00 32.39 ? 116 GLY B C   1 
ATOM   2795 O O   . GLY B 1 116 ? 3.048   2.637   -49.935 1.00 35.33 ? 116 GLY B O   1 
ATOM   2796 N N   . THR B 1 117 ? 4.913   3.482   -49.068 1.00 30.87 ? 117 THR B N   1 
ATOM   2797 C CA  . THR B 1 117 ? 4.186   4.458   -48.235 1.00 28.95 ? 117 THR B CA  1 
ATOM   2798 C C   . THR B 1 117 ? 3.289   5.402   -49.062 1.00 32.56 ? 117 THR B C   1 
ATOM   2799 O O   . THR B 1 117 ? 3.684   5.817   -50.140 1.00 34.25 ? 117 THR B O   1 
ATOM   2800 C CB  . THR B 1 117 ? 5.238   5.275   -47.469 1.00 30.52 ? 117 THR B CB  1 
ATOM   2801 O OG1 . THR B 1 117 ? 6.071   4.407   -46.685 1.00 25.70 ? 117 THR B OG1 1 
ATOM   2802 C CG2 . THR B 1 117 ? 4.588   6.324   -46.568 1.00 33.45 ? 117 THR B CG2 1 
ATOM   2803 N N   . SER B 1 118 ? 2.092   5.628   -48.535 1.00 36.34 ? 118 SER B N   1 
ATOM   2804 C CA  . SER B 1 118 ? 1.072   6.414   -49.254 1.00 37.78 ? 118 SER B CA  1 
ATOM   2805 C C   . SER B 1 118 ? 0.470   7.510   -48.382 1.00 32.97 ? 118 SER B C   1 
ATOM   2806 O O   . SER B 1 118 ? 0.387   7.360   -47.189 1.00 36.47 ? 118 SER B O   1 
ATOM   2807 C CB  . SER B 1 118 ? 0.029   5.517   -49.851 1.00 40.60 ? 118 SER B CB  1 
ATOM   2808 O OG  . SER B 1 118 ? -0.822  4.984   -48.870 1.00 41.82 ? 118 SER B OG  1 
ATOM   2809 N N   . LYS B 1 119 ? 0.074   8.574   -49.056 1.00 46.58 ? 119 LYS B N   1 
ATOM   2810 C CA  . LYS B 1 119 ? -0.534  9.783   -48.471 1.00 45.16 ? 119 LYS B CA  1 
ATOM   2811 C C   . LYS B 1 119 ? -1.773  9.375   -47.690 1.00 42.26 ? 119 LYS B C   1 
ATOM   2812 O O   . LYS B 1 119 ? -1.873  9.694   -46.533 1.00 49.08 ? 119 LYS B O   1 
ATOM   2813 C CB  . LYS B 1 119 ? -0.875  10.722  -49.628 1.00 42.49 ? 119 LYS B CB  1 
ATOM   2814 C CG  . LYS B 1 119 ? 0.188   10.782  -50.715 1.00 51.28 ? 119 LYS B CG  1 
ATOM   2815 C CD  . LYS B 1 119 ? 0.294   9.532   -51.589 1.00 52.38 ? 119 LYS B CD  1 
ATOM   2816 C CE  . LYS B 1 119 ? 1.380   9.618   -52.642 1.00 53.22 ? 119 LYS B CE  1 
ATOM   2817 N NZ  . LYS B 1 119 ? 0.892   10.320  -53.856 1.00 53.52 ? 119 LYS B NZ  1 
ATOM   2818 N N   . GLY B 1 120 ? -2.659  8.626   -48.314 1.00 44.95 ? 120 GLY B N   1 
ATOM   2819 C CA  . GLY B 1 120 ? -3.896  8.275   -47.563 1.00 45.88 ? 120 GLY B CA  1 
ATOM   2820 C C   . GLY B 1 120 ? -3.721  7.371   -46.326 1.00 50.89 ? 120 GLY B C   1 
ATOM   2821 O O   . GLY B 1 120 ? -4.215  7.665   -45.205 1.00 51.89 ? 120 GLY B O   1 
ATOM   2822 N N   . SER B 1 121 ? -2.908  6.351   -46.465 1.00 47.66 ? 121 SER B N   1 
ATOM   2823 C CA  . SER B 1 121 ? -2.867  5.295   -45.478 1.00 45.80 ? 121 SER B CA  1 
ATOM   2824 C C   . SER B 1 121 ? -1.509  5.123   -44.774 1.00 42.88 ? 121 SER B C   1 
ATOM   2825 O O   . SER B 1 121 ? -1.401  4.275   -43.886 1.00 39.12 ? 121 SER B O   1 
ATOM   2826 C CB  . SER B 1 121 ? -3.337  4.012   -46.167 1.00 45.69 ? 121 SER B CB  1 
ATOM   2827 O OG  . SER B 1 121 ? -3.119  2.896   -45.349 1.00 50.50 ? 121 SER B OG  1 
ATOM   2828 N N   . GLY B 1 122 ? -0.474  5.893   -45.125 1.00 39.32 ? 122 GLY B N   1 
ATOM   2829 C CA  . GLY B 1 122 ? 0.819   5.757   -44.441 1.00 36.40 ? 122 GLY B CA  1 
ATOM   2830 C C   . GLY B 1 122 ? 1.556   4.455   -44.751 1.00 30.53 ? 122 GLY B C   1 
ATOM   2831 O O   . GLY B 1 122 ? 1.646   4.029   -45.902 1.00 30.61 ? 122 GLY B O   1 
ATOM   2832 N N   . THR B 1 123 ? 2.090   3.813   -43.706 1.00 30.23 ? 123 THR B N   1 
ATOM   2833 C CA  . THR B 1 123 ? 2.760   2.514   -43.807 1.00 27.20 ? 123 THR B CA  1 
ATOM   2834 C C   . THR B 1 123 ? 2.312   1.569   -42.703 1.00 27.87 ? 123 THR B C   1 
ATOM   2835 O O   . THR B 1 123 ? 2.439   1.895   -41.521 1.00 26.00 ? 123 THR B O   1 
ATOM   2836 C CB  . THR B 1 123 ? 4.276   2.628   -43.661 1.00 28.50 ? 123 THR B CB  1 
ATOM   2837 O OG1 . THR B 1 123 ? 4.750   3.761   -44.379 1.00 23.76 ? 123 THR B OG1 1 
ATOM   2838 C CG2 . THR B 1 123 ? 4.961   1.334   -44.177 1.00 27.37 ? 123 THR B CG2 1 
ATOM   2839 N N   . SER B 1 124 ? 1.930   0.361   -43.071 1.00 29.03 ? 124 SER B N   1 
ATOM   2840 C CA  . SER B 1 124 ? 1.615   -0.636  -42.054 1.00 29.06 ? 124 SER B CA  1 
ATOM   2841 C C   . SER B 1 124 ? 2.876   -1.404  -41.643 1.00 29.00 ? 124 SER B C   1 
ATOM   2842 O O   . SER B 1 124 ? 3.862   -1.455  -42.392 1.00 26.83 ? 124 SER B O   1 
ATOM   2843 C CB  . SER B 1 124 ? 0.585   -1.615  -42.599 1.00 30.70 ? 124 SER B CB  1 
ATOM   2844 O OG  . SER B 1 124 ? 1.261   -2.604  -43.350 1.00 29.53 ? 124 SER B OG  1 
ATOM   2845 N N   . PRO B 1 125 ? 2.877   -2.005  -40.443 1.00 28.08 ? 125 PRO B N   1 
ATOM   2846 C CA  . PRO B 1 125 ? 4.017   -2.854  -40.051 1.00 27.00 ? 125 PRO B CA  1 
ATOM   2847 C C   . PRO B 1 125 ? 4.303   -3.989  -41.016 1.00 29.66 ? 125 PRO B C   1 
ATOM   2848 O O   . PRO B 1 125 ? 5.475   -4.241  -41.326 1.00 27.17 ? 125 PRO B O   1 
ATOM   2849 C CB  . PRO B 1 125 ? 3.602   -3.379  -38.670 1.00 27.38 ? 125 PRO B CB  1 
ATOM   2850 C CG  . PRO B 1 125 ? 2.641   -2.315  -38.152 1.00 25.93 ? 125 PRO B CG  1 
ATOM   2851 C CD  . PRO B 1 125 ? 1.887   -1.859  -39.357 1.00 28.62 ? 125 PRO B CD  1 
ATOM   2852 N N   . ALA B 1 126 ? 3.274   -4.663  -41.536 1.00 27.45 ? 126 ALA B N   1 
ATOM   2853 C CA  . ALA B 1 126 ? 3.523   -5.711  -42.516 1.00 28.07 ? 126 ALA B CA  1 
ATOM   2854 C C   . ALA B 1 126 ? 4.220   -5.141  -43.748 1.00 28.01 ? 126 ALA B C   1 
ATOM   2855 O O   . ALA B 1 126 ? 5.100   -5.788  -44.327 1.00 26.28 ? 126 ALA B O   1 
ATOM   2856 C CB  . ALA B 1 126 ? 2.219   -6.408  -42.902 1.00 27.63 ? 126 ALA B CB  1 
ATOM   2857 N N   . GLN B 1 127 ? 3.823   -3.939  -44.165 1.00 27.94 ? 127 GLN B N   1 
ATOM   2858 C CA  . GLN B 1 127 ? 4.489   -3.257  -45.276 1.00 31.24 ? 127 GLN B CA  1 
ATOM   2859 C C   . GLN B 1 127 ? 5.974   -3.061  -45.003 1.00 25.52 ? 127 GLN B C   1 
ATOM   2860 O O   . GLN B 1 127 ? 6.813   -3.276  -45.882 1.00 24.42 ? 127 GLN B O   1 
ATOM   2861 C CB  . GLN B 1 127 ? 3.837   -1.889  -45.494 1.00 30.35 ? 127 GLN B CB  1 
ATOM   2862 C CG  . GLN B 1 127 ? 3.380   -1.585  -46.868 1.00 32.78 ? 127 GLN B CG  1 
ATOM   2863 C CD  . GLN B 1 127 ? 2.580   -0.303  -46.908 1.00 34.14 ? 127 GLN B CD  1 
ATOM   2864 O OE1 . GLN B 1 127 ? 1.957   0.087   -45.920 1.00 31.19 ? 127 GLN B OE1 1 
ATOM   2865 N NE2 . GLN B 1 127 ? 2.669   0.411   -48.030 1.00 37.82 ? 127 GLN B NE2 1 
ATOM   2866 N N   . LEU B 1 128 ? 6.302   -2.600  -43.795 1.00 25.37 ? 128 LEU B N   1 
ATOM   2867 C CA  . LEU B 1 128 ? 7.691   -2.418  -43.388 1.00 28.45 ? 128 LEU B CA  1 
ATOM   2868 C C   . LEU B 1 128 ? 8.461   -3.735  -43.447 1.00 28.35 ? 128 LEU B C   1 
ATOM   2869 O O   . LEU B 1 128 ? 9.587   -3.791  -43.968 1.00 26.86 ? 128 LEU B O   1 
ATOM   2870 C CB  . LEU B 1 128 ? 7.730   -1.830  -41.974 1.00 25.71 ? 128 LEU B CB  1 
ATOM   2871 C CG  . LEU B 1 128 ? 9.069   -1.757  -41.234 1.00 28.32 ? 128 LEU B CG  1 
ATOM   2872 C CD1 . LEU B 1 128 ? 10.075  -0.762  -41.962 1.00 24.53 ? 128 LEU B CD1 1 
ATOM   2873 C CD2 . LEU B 1 128 ? 8.830   -1.320  -39.787 1.00 21.85 ? 128 LEU B CD2 1 
ATOM   2874 N N   . ILE B 1 129 ? 7.888   -4.797  -42.865 1.00 27.23 ? 129 ILE B N   1 
ATOM   2875 C CA  . ILE B 1 129 ? 8.574   -6.090  -42.807 1.00 25.33 ? 129 ILE B CA  1 
ATOM   2876 C C   . ILE B 1 129 ? 8.749   -6.665  -44.201 1.00 27.89 ? 129 ILE B C   1 
ATOM   2877 O O   . ILE B 1 129 ? 9.823   -7.189  -44.549 1.00 31.33 ? 129 ILE B O   1 
ATOM   2878 C CB  . ILE B 1 129 ? 7.800   -7.061  -41.894 1.00 30.38 ? 129 ILE B CB  1 
ATOM   2879 C CG1 . ILE B 1 129 ? 7.637   -6.488  -40.477 1.00 27.66 ? 129 ILE B CG1 1 
ATOM   2880 C CG2 . ILE B 1 129 ? 8.457   -8.462  -41.895 1.00 29.82 ? 129 ILE B CG2 1 
ATOM   2881 C CD1 . ILE B 1 129 ? 6.421   -7.101  -39.691 1.00 25.77 ? 129 ILE B CD1 1 
ATOM   2882 N N   . ALA B 1 130 ? 7.709   -6.573  -45.029 1.00 25.89 ? 130 ALA B N   1 
ATOM   2883 C CA  . ALA B 1 130 ? 7.737   -7.243  -46.325 1.00 28.62 ? 130 ALA B CA  1 
ATOM   2884 C C   . ALA B 1 130 ? 8.692   -6.572  -47.302 1.00 31.67 ? 130 ALA B C   1 
ATOM   2885 O O   . ALA B 1 130 ? 9.192   -7.233  -48.222 1.00 29.27 ? 130 ALA B O   1 
ATOM   2886 C CB  . ALA B 1 130 ? 6.342   -7.292  -46.935 1.00 25.92 ? 130 ALA B CB  1 
ATOM   2887 N N   . ASN B 1 131 ? 8.904   -5.257  -47.173 1.00 28.37 ? 131 ASN B N   1 
ATOM   2888 C CA  . ASN B 1 131 ? 9.617   -4.517  -48.204 1.00 25.18 ? 131 ASN B CA  1 
ATOM   2889 C C   . ASN B 1 131 ? 10.991  -4.029  -47.791 1.00 28.97 ? 131 ASN B C   1 
ATOM   2890 O O   . ASN B 1 131 ? 11.760  -3.610  -48.663 1.00 28.51 ? 131 ASN B O   1 
ATOM   2891 C CB  . ASN B 1 131 ? 8.770   -3.334  -48.686 1.00 25.44 ? 131 ASN B CB  1 
ATOM   2892 C CG  . ASN B 1 131 ? 7.564   -3.788  -49.477 1.00 29.66 ? 131 ASN B CG  1 
ATOM   2893 O OD1 . ASN B 1 131 ? 7.707   -4.234  -50.624 1.00 28.93 ? 131 ASN B OD1 1 
ATOM   2894 N ND2 . ASN B 1 131 ? 6.373   -3.732  -48.866 1.00 29.27 ? 131 ASN B ND2 1 
ATOM   2895 N N   . ALA B 1 132 ? 11.318  -4.049  -46.510 1.00 26.27 ? 132 ALA B N   1 
ATOM   2896 C CA  . ALA B 1 132 ? 12.650  -3.670  -46.064 1.00 26.57 ? 132 ALA B CA  1 
ATOM   2897 C C   . ALA B 1 132 ? 13.770  -4.436  -46.774 1.00 29.42 ? 132 ALA B C   1 
ATOM   2898 O O   . ALA B 1 132 ? 14.858  -3.869  -46.962 1.00 24.58 ? 132 ALA B O   1 
ATOM   2899 C CB  . ALA B 1 132 ? 12.784  -3.899  -44.555 1.00 24.98 ? 132 ALA B CB  1 
ATOM   2900 N N   . PRO B 1 133 ? 13.585  -5.724  -47.128 1.00 29.17 ? 133 PRO B N   1 
ATOM   2901 C CA  . PRO B 1 133 ? 14.644  -6.433  -47.874 1.00 27.57 ? 133 PRO B CA  1 
ATOM   2902 C C   . PRO B 1 133 ? 15.045  -5.765  -49.175 1.00 29.57 ? 133 PRO B C   1 
ATOM   2903 O O   . PRO B 1 133 ? 16.175  -5.970  -49.640 1.00 31.28 ? 133 PRO B O   1 
ATOM   2904 C CB  . PRO B 1 133 ? 14.023  -7.813  -48.117 1.00 31.37 ? 133 PRO B CB  1 
ATOM   2905 C CG  . PRO B 1 133 ? 13.175  -8.033  -46.883 1.00 25.88 ? 133 PRO B CG  1 
ATOM   2906 C CD  . PRO B 1 133 ? 12.571  -6.679  -46.610 1.00 28.90 ? 133 PRO B CD  1 
ATOM   2907 N N   . LYS B 1 134 ? 14.154  -4.980  -49.789 1.00 27.46 ? 134 LYS B N   1 
ATOM   2908 C CA  . LYS B 1 134 ? 14.534  -4.247  -50.988 1.00 29.22 ? 134 LYS B CA  1 
ATOM   2909 C C   . LYS B 1 134 ? 15.706  -3.317  -50.744 1.00 30.09 ? 134 LYS B C   1 
ATOM   2910 O O   . LYS B 1 134 ? 16.382  -2.926  -51.706 1.00 34.40 ? 134 LYS B O   1 
ATOM   2911 C CB  . LYS B 1 134 ? 13.363  -3.414  -51.492 1.00 31.65 ? 134 LYS B CB  1 
ATOM   2912 C CG  . LYS B 1 134 ? 12.239  -4.185  -52.128 1.00 33.64 ? 134 LYS B CG  1 
ATOM   2913 C CD  . LYS B 1 134 ? 11.311  -3.194  -52.866 1.00 32.00 ? 134 LYS B CD  1 
ATOM   2914 C CE  . LYS B 1 134 ? 9.881   -3.468  -52.562 1.00 33.71 ? 134 LYS B CE  1 
ATOM   2915 N NZ  . LYS B 1 134 ? 8.972   -2.407  -53.069 1.00 38.02 ? 134 LYS B NZ  1 
ATOM   2916 N N   . LEU B 1 135 ? 15.933  -2.916  -49.491 1.00 28.92 ? 135 LEU B N   1 
ATOM   2917 C CA  . LEU B 1 135 ? 16.998  -1.980  -49.144 1.00 27.72 ? 135 LEU B CA  1 
ATOM   2918 C C   . LEU B 1 135 ? 18.172  -2.667  -48.477 1.00 28.14 ? 135 LEU B C   1 
ATOM   2919 O O   . LEU B 1 135 ? 19.097  -1.985  -48.025 1.00 28.71 ? 135 LEU B O   1 
ATOM   2920 C CB  . LEU B 1 135 ? 16.462  -0.856  -48.225 1.00 25.46 ? 135 LEU B CB  1 
ATOM   2921 C CG  . LEU B 1 135 ? 15.216  -0.133  -48.705 1.00 28.18 ? 135 LEU B CG  1 
ATOM   2922 C CD1 . LEU B 1 135 ? 14.523  0.542   -47.538 1.00 31.17 ? 135 LEU B CD1 1 
ATOM   2923 C CD2 . LEU B 1 135 ? 15.530  0.889   -49.792 1.00 30.83 ? 135 LEU B CD2 1 
ATOM   2924 N N   . GLY B 1 136 ? 18.126  -3.988  -48.344 1.00 29.70 ? 136 GLY B N   1 
ATOM   2925 C CA  . GLY B 1 136 ? 19.195  -4.727  -47.704 1.00 27.59 ? 136 GLY B CA  1 
ATOM   2926 C C   . GLY B 1 136 ? 18.992  -4.995  -46.239 1.00 26.86 ? 136 GLY B C   1 
ATOM   2927 O O   . GLY B 1 136 ? 19.953  -5.369  -45.557 1.00 26.60 ? 136 GLY B O   1 
ATOM   2928 N N   . PHE B 1 137 ? 17.772  -4.828  -45.724 1.00 26.28 ? 137 PHE B N   1 
ATOM   2929 C CA  . PHE B 1 137 ? 17.497  -4.981  -44.302 1.00 28.04 ? 137 PHE B CA  1 
ATOM   2930 C C   . PHE B 1 137 ? 16.549  -6.143  -44.061 1.00 26.60 ? 137 PHE B C   1 
ATOM   2931 O O   . PHE B 1 137 ? 15.779  -6.531  -44.939 1.00 28.61 ? 137 PHE B O   1 
ATOM   2932 C CB  . PHE B 1 137 ? 16.879  -3.698  -43.698 1.00 28.55 ? 137 PHE B CB  1 
ATOM   2933 C CG  . PHE B 1 137 ? 17.735  -2.493  -43.889 1.00 27.53 ? 137 PHE B CG  1 
ATOM   2934 C CD1 . PHE B 1 137 ? 19.027  -2.475  -43.396 1.00 27.20 ? 137 PHE B CD1 1 
ATOM   2935 C CD2 . PHE B 1 137 ? 17.279  -1.417  -44.627 1.00 27.54 ? 137 PHE B CD2 1 
ATOM   2936 C CE1 . PHE B 1 137 ? 19.841  -1.367  -43.591 1.00 27.92 ? 137 PHE B CE1 1 
ATOM   2937 C CE2 . PHE B 1 137 ? 18.077  -0.305  -44.829 1.00 28.78 ? 137 PHE B CE2 1 
ATOM   2938 C CZ  . PHE B 1 137 ? 19.381  -0.290  -44.327 1.00 28.69 ? 137 PHE B CZ  1 
ATOM   2939 N N   . LYS B 1 138 ? 16.654  -6.707  -42.873 1.00 22.60 ? 138 LYS B N   1 
ATOM   2940 C CA  . LYS B 1 138 ? 15.693  -7.663  -42.349 1.00 29.07 ? 138 LYS B CA  1 
ATOM   2941 C C   . LYS B 1 138 ? 15.033  -7.041  -41.132 1.00 27.68 ? 138 LYS B C   1 
ATOM   2942 O O   . LYS B 1 138 ? 15.706  -6.377  -40.333 1.00 29.21 ? 138 LYS B O   1 
ATOM   2943 C CB  . LYS B 1 138 ? 16.384  -8.969  -41.968 1.00 28.32 ? 138 LYS B CB  1 
ATOM   2944 C CG  . LYS B 1 138 ? 15.485  -10.010 -41.321 1.00 33.84 ? 138 LYS B CG  1 
ATOM   2945 C CD  . LYS B 1 138 ? 16.092  -11.391 -41.492 1.00 38.72 ? 138 LYS B CD  1 
ATOM   2946 C CE  . LYS B 1 138 ? 14.990  -12.455 -41.519 1.00 46.86 ? 138 LYS B CE  1 
ATOM   2947 N NZ  . LYS B 1 138 ? 15.522  -13.802 -41.149 1.00 53.32 ? 138 LYS B NZ  1 
ATOM   2948 N N   . ILE B 1 139 ? 13.721  -7.221  -40.997 1.00 29.26 ? 139 ILE B N   1 
ATOM   2949 C CA  . ILE B 1 139 ? 12.992  -6.680  -39.847 1.00 25.65 ? 139 ILE B CA  1 
ATOM   2950 C C   . ILE B 1 139 ? 12.586  -7.834  -38.941 1.00 29.73 ? 139 ILE B C   1 
ATOM   2951 O O   . ILE B 1 139 ? 11.887  -8.758  -39.382 1.00 28.05 ? 139 ILE B O   1 
ATOM   2952 C CB  . ILE B 1 139 ? 11.772  -5.868  -40.279 1.00 25.84 ? 139 ILE B CB  1 
ATOM   2953 C CG1 . ILE B 1 139 ? 12.175  -4.760  -41.247 1.00 27.71 ? 139 ILE B CG1 1 
ATOM   2954 C CG2 . ILE B 1 139 ? 11.089  -5.307  -39.043 1.00 28.04 ? 139 ILE B CG2 1 
ATOM   2955 C CD1 . ILE B 1 139 ? 13.059  -3.594  -40.634 1.00 23.77 ? 139 ILE B CD1 1 
ATOM   2956 N N   . ILE B 1 140 ? 12.978  -7.775  -37.671 1.00 28.38 ? 140 ILE B N   1 
ATOM   2957 C CA  . ILE B 1 140 ? 12.584  -8.825  -36.739 1.00 30.42 ? 140 ILE B CA  1 
ATOM   2958 C C   . ILE B 1 140 ? 11.509  -8.255  -35.807 1.00 30.31 ? 140 ILE B C   1 
ATOM   2959 O O   . ILE B 1 140 ? 11.840  -7.488  -34.889 1.00 28.77 ? 140 ILE B O   1 
ATOM   2960 C CB  . ILE B 1 140 ? 13.772  -9.346  -35.926 1.00 28.21 ? 140 ILE B CB  1 
ATOM   2961 C CG1 . ILE B 1 140 ? 14.748  -10.124 -36.795 1.00 33.61 ? 140 ILE B CG1 1 
ATOM   2962 C CG2 . ILE B 1 140 ? 13.270  -10.367 -34.883 1.00 32.62 ? 140 ILE B CG2 1 
ATOM   2963 C CD1 . ILE B 1 140 ? 16.149  -10.156 -36.200 1.00 36.03 ? 140 ILE B CD1 1 
ATOM   2964 N N   . PRO B 1 141 ? 10.242  -8.667  -35.925 1.00 28.99 ? 141 PRO B N   1 
ATOM   2965 C CA  . PRO B 1 141 ? 9.230   -8.230  -34.937 1.00 28.88 ? 141 PRO B CA  1 
ATOM   2966 C C   . PRO B 1 141 ? 9.569   -8.810  -33.581 1.00 33.04 ? 141 PRO B C   1 
ATOM   2967 O O   . PRO B 1 141 ? 9.912   -9.992  -33.462 1.00 32.73 ? 141 PRO B O   1 
ATOM   2968 C CB  . PRO B 1 141 ? 7.916   -8.812  -35.463 1.00 30.10 ? 141 PRO B CB  1 
ATOM   2969 C CG  . PRO B 1 141 ? 8.187   -9.260  -36.853 1.00 30.88 ? 141 PRO B CG  1 
ATOM   2970 C CD  . PRO B 1 141 ? 9.671   -9.596  -36.909 1.00 32.14 ? 141 PRO B CD  1 
ATOM   2971 N N   . ILE B 1 142 ? 9.551   -7.955  -32.574 1.00 31.47 ? 142 ILE B N   1 
ATOM   2972 C CA  . ILE B 1 142 ? 9.813   -8.375  -31.218 1.00 29.75 ? 142 ILE B CA  1 
ATOM   2973 C C   . ILE B 1 142 ? 8.653   -7.954  -30.355 1.00 36.57 ? 142 ILE B C   1 
ATOM   2974 O O   . ILE B 1 142 ? 7.733   -7.247  -30.771 1.00 32.69 ? 142 ILE B O   1 
ATOM   2975 C CB  . ILE B 1 142 ? 11.146  -7.847  -30.668 1.00 32.50 ? 142 ILE B CB  1 
ATOM   2976 C CG1 . ILE B 1 142 ? 11.223  -6.305  -30.735 1.00 32.52 ? 142 ILE B CG1 1 
ATOM   2977 C CG2 . ILE B 1 142 ? 12.281  -8.542  -31.381 1.00 31.06 ? 142 ILE B CG2 1 
ATOM   2978 C CD1 . ILE B 1 142 ? 12.127  -5.642  -29.659 1.00 30.23 ? 142 ILE B CD1 1 
ATOM   2979 N N   . LYS B 1 143 ? 8.647   -8.525  -29.155 1.00 36.17 ? 143 LYS B N   1 
ATOM   2980 C CA  . LYS B 1 143 ? 7.628   -8.249  -28.120 1.00 36.37 ? 143 LYS B CA  1 
ATOM   2981 C C   . LYS B 1 143 ? 7.804   -6.802  -27.670 1.00 35.75 ? 143 LYS B C   1 
ATOM   2982 O O   . LYS B 1 143 ? 8.944   -6.338  -27.623 1.00 32.00 ? 143 LYS B O   1 
ATOM   2983 C CB  . LYS B 1 143 ? 7.912   -9.111  -26.889 1.00 40.74 ? 143 LYS B CB  1 
ATOM   2984 C CG  . LYS B 1 143 ? 7.315   -10.512 -26.861 1.00 48.01 ? 143 LYS B CG  1 
ATOM   2985 C CD  . LYS B 1 143 ? 7.991   -11.458 -25.857 1.00 48.91 ? 143 LYS B CD  1 
ATOM   2986 C CE  . LYS B 1 143 ? 7.746   -12.931 -26.130 1.00 53.33 ? 143 LYS B CE  1 
ATOM   2987 N NZ  . LYS B 1 143 ? 8.248   -13.824 -25.052 1.00 56.19 ? 143 LYS B NZ  1 
ATOM   2988 N N   . ARG B 1 144 ? 6.719   -6.131  -27.310 1.00 31.22 ? 144 ARG B N   1 
ATOM   2989 C CA  . ARG B 1 144 ? 6.897   -4.757  -26.823 1.00 33.39 ? 144 ARG B CA  1 
ATOM   2990 C C   . ARG B 1 144 ? 7.441   -4.798  -25.387 1.00 32.76 ? 144 ARG B C   1 
ATOM   2991 O O   . ARG B 1 144 ? 6.736   -4.563  -24.404 1.00 32.06 ? 144 ARG B O   1 
ATOM   2992 C CB  . ARG B 1 144 ? 5.615   -3.947  -26.960 1.00 31.53 ? 144 ARG B CB  1 
ATOM   2993 C CG  . ARG B 1 144 ? 5.158   -3.845  -28.422 1.00 31.49 ? 144 ARG B CG  1 
ATOM   2994 C CD  . ARG B 1 144 ? 3.794   -3.200  -28.531 1.00 29.41 ? 144 ARG B CD  1 
ATOM   2995 N NE  . ARG B 1 144 ? 3.843   -1.762  -28.268 1.00 29.90 ? 144 ARG B NE  1 
ATOM   2996 C CZ  . ARG B 1 144 ? 3.969   -0.826  -29.204 1.00 27.76 ? 144 ARG B CZ  1 
ATOM   2997 N NH1 . ARG B 1 144 ? 4.146   -1.138  -30.478 1.00 26.00 ? 144 ARG B NH1 1 
ATOM   2998 N NH2 . ARG B 1 144 ? 3.872   0.457   -28.861 1.00 28.11 ? 144 ARG B NH2 1 
ATOM   2999 N N   . ASP B 1 145 ? 8.742   -5.105  -25.270 1.00 32.55 ? 145 ASP B N   1 
ATOM   3000 C CA  . ASP B 1 145 ? 9.371   -5.399  -23.977 1.00 34.21 ? 145 ASP B CA  1 
ATOM   3001 C C   . ASP B 1 145 ? 10.807  -4.868  -23.929 1.00 32.66 ? 145 ASP B C   1 
ATOM   3002 O O   . ASP B 1 145 ? 11.566  -5.085  -24.883 1.00 34.38 ? 145 ASP B O   1 
ATOM   3003 C CB  . ASP B 1 145 ? 9.361   -6.921  -23.704 1.00 31.78 ? 145 ASP B CB  1 
ATOM   3004 C CG  . ASP B 1 145 ? 10.431  -7.345  -22.734 1.00 35.73 ? 145 ASP B CG  1 
ATOM   3005 O OD1 . ASP B 1 145 ? 10.312  -7.043  -21.539 1.00 44.27 ? 145 ASP B OD1 1 
ATOM   3006 O OD2 . ASP B 1 145 ? 11.412  -7.962  -23.156 1.00 49.06 ? 145 ASP B OD2 1 
ATOM   3007 N N   . SER B 1 146 ? 11.162  -4.145  -22.865 1.00 34.26 ? 146 SER B N   1 
ATOM   3008 C CA  . SER B 1 146 ? 12.474  -3.451  -22.757 1.00 33.12 ? 146 SER B CA  1 
ATOM   3009 C C   . SER B 1 146 ? 13.661  -4.410  -22.786 1.00 37.69 ? 146 SER B C   1 
ATOM   3010 O O   . SER B 1 146 ? 14.718  -4.014  -23.236 1.00 32.71 ? 146 SER B O   1 
ATOM   3011 C CB  . SER B 1 146 ? 12.542  -2.539  -21.576 1.00 30.87 ? 146 SER B CB  1 
ATOM   3012 O OG  . SER B 1 146 ? 12.399  -3.254  -20.377 1.00 36.02 ? 146 SER B OG  1 
ATOM   3013 N N   . LYS B 1 147 ? 13.469  -5.621  -22.281 1.00 43.59 ? 147 LYS B N   1 
ATOM   3014 C CA  . LYS B 1 147 ? 14.563  -6.610  -22.304 1.00 37.41 ? 147 LYS B CA  1 
ATOM   3015 C C   . LYS B 1 147 ? 14.813  -6.992  -23.761 1.00 40.42 ? 147 LYS B C   1 
ATOM   3016 O O   . LYS B 1 147 ? 15.945  -7.018  -24.163 1.00 42.65 ? 147 LYS B O   1 
ATOM   3017 C CB  . LYS B 1 147 ? 14.227  -7.781  -21.381 1.00 43.76 ? 147 LYS B CB  1 
ATOM   3018 C CG  . LYS B 1 147 ? 15.046  -7.824  -20.102 1.00 52.78 ? 147 LYS B CG  1 
ATOM   3019 C CD  . LYS B 1 147 ? 16.403  -8.506  -20.292 1.00 50.07 ? 147 LYS B CD  1 
ATOM   3020 C CE  . LYS B 1 147 ? 17.643  -7.689  -19.963 1.00 55.42 ? 147 LYS B CE  1 
ATOM   3021 N NZ  . LYS B 1 147 ? 17.676  -7.217  -18.556 1.00 58.99 ? 147 LYS B NZ  1 
ATOM   3022 N N   . GLU B 1 148 ? 13.763  -7.260  -24.520 1.00 37.08 ? 148 GLU B N   1 
ATOM   3023 C CA  . GLU B 1 148 ? 13.986  -7.586  -25.946 1.00 38.66 ? 148 GLU B CA  1 
ATOM   3024 C C   . GLU B 1 148 ? 14.671  -6.395  -26.632 1.00 34.59 ? 148 GLU B C   1 
ATOM   3025 O O   . GLU B 1 148 ? 15.610  -6.608  -27.351 1.00 34.77 ? 148 GLU B O   1 
ATOM   3026 C CB  . GLU B 1 148 ? 12.682  -7.998  -26.624 1.00 37.22 ? 148 GLU B CB  1 
ATOM   3027 C CG  . GLU B 1 148 ? 12.244  -9.407  -26.285 1.00 42.17 ? 148 GLU B CG  1 
ATOM   3028 C CD  . GLU B 1 148 ? 13.109  -10.505 -26.869 1.00 46.69 ? 148 GLU B CD  1 
ATOM   3029 O OE1 . GLU B 1 148 ? 14.040  -10.900 -26.203 1.00 44.39 ? 148 GLU B OE1 1 
ATOM   3030 O OE2 . GLU B 1 148 ? 12.839  -10.932 -27.989 1.00 44.51 ? 148 GLU B OE2 1 
ATOM   3031 N N   . VAL B 1 149 ? 14.218  -5.173  -26.380 1.00 36.26 ? 149 VAL B N   1 
ATOM   3032 C CA  . VAL B 1 149 ? 14.840  -4.021  -27.036 1.00 33.03 ? 149 VAL B CA  1 
ATOM   3033 C C   . VAL B 1 149 ? 16.319  -3.937  -26.676 1.00 33.79 ? 149 VAL B C   1 
ATOM   3034 O O   . VAL B 1 149 ? 17.186  -3.856  -27.555 1.00 32.85 ? 149 VAL B O   1 
ATOM   3035 C CB  . VAL B 1 149 ? 14.095  -2.720  -26.674 1.00 33.89 ? 149 VAL B CB  1 
ATOM   3036 C CG1 . VAL B 1 149 ? 14.825  -1.500  -27.269 1.00 31.17 ? 149 VAL B CG1 1 
ATOM   3037 C CG2 . VAL B 1 149 ? 12.665  -2.776  -27.155 1.00 29.04 ? 149 VAL B CG2 1 
ATOM   3038 N N   . LYS B 1 150 ? 16.626  -3.964  -25.378 1.00 34.95 ? 150 LYS B N   1 
ATOM   3039 C CA  . LYS B 1 150 ? 18.012  -3.953  -24.917 1.00 35.27 ? 150 LYS B CA  1 
ATOM   3040 C C   . LYS B 1 150 ? 18.843  -5.035  -25.603 1.00 37.33 ? 150 LYS B C   1 
ATOM   3041 O O   . LYS B 1 150 ? 19.987  -4.791  -26.010 1.00 33.56 ? 150 LYS B O   1 
ATOM   3042 C CB  . LYS B 1 150 ? 18.054  -4.127  -23.395 1.00 34.93 ? 150 LYS B CB  1 
ATOM   3043 C CG  . LYS B 1 150 ? 19.386  -3.775  -22.784 1.00 41.26 ? 150 LYS B CG  1 
ATOM   3044 C CD  . LYS B 1 150 ? 19.230  -3.380  -21.325 1.00 43.55 ? 150 LYS B CD  1 
ATOM   3045 C CE  . LYS B 1 150 ? 20.518  -3.631  -20.535 1.00 50.91 ? 150 LYS B CE  1 
ATOM   3046 N NZ  . LYS B 1 150 ? 21.232  -2.307  -20.258 1.00 49.13 ? 150 LYS B NZ  1 
ATOM   3047 N N   . LYS B 1 151 ? 18.279  -6.237  -25.739 1.00 33.12 ? 151 LYS B N   1 
ATOM   3048 C CA  . LYS B 1 151 ? 19.020  -7.344  -26.335 1.00 37.86 ? 151 LYS B CA  1 
ATOM   3049 C C   . LYS B 1 151 ? 19.498  -6.992  -27.736 1.00 35.82 ? 151 LYS B C   1 
ATOM   3050 O O   . LYS B 1 151 ? 20.651  -7.248  -28.103 1.00 36.09 ? 151 LYS B O   1 
ATOM   3051 C CB  . LYS B 1 151 ? 18.135  -8.588  -26.403 1.00 34.09 ? 151 LYS B CB  1 
ATOM   3052 C CG  . LYS B 1 151 ? 18.765  -9.730  -27.201 1.00 35.72 ? 151 LYS B CG  1 
ATOM   3053 C CD  . LYS B 1 151 ? 17.929  -10.999 -27.099 1.00 44.13 ? 151 LYS B CD  1 
ATOM   3054 C CE  . LYS B 1 151 ? 17.758  -11.646 -28.468 1.00 47.17 ? 151 LYS B CE  1 
ATOM   3055 N NZ  . LYS B 1 151 ? 17.820  -13.143 -28.421 1.00 45.33 ? 151 LYS B NZ  1 
ATOM   3056 N N   . TYR B 1 152 ? 18.612  -6.403  -28.536 1.00 34.09 ? 152 TYR B N   1 
ATOM   3057 C CA  . TYR B 1 152 ? 18.941  -6.124  -29.922 1.00 35.73 ? 152 TYR B CA  1 
ATOM   3058 C C   . TYR B 1 152 ? 19.728  -4.832  -30.082 1.00 33.06 ? 152 TYR B C   1 
ATOM   3059 O O   . TYR B 1 152 ? 20.593  -4.756  -30.960 1.00 35.53 ? 152 TYR B O   1 
ATOM   3060 C CB  . TYR B 1 152 ? 17.667  -6.132  -30.750 1.00 33.51 ? 152 TYR B CB  1 
ATOM   3061 C CG  . TYR B 1 152 ? 17.161  -7.544  -30.968 1.00 33.21 ? 152 TYR B CG  1 
ATOM   3062 C CD1 . TYR B 1 152 ? 17.811  -8.403  -31.852 1.00 33.37 ? 152 TYR B CD1 1 
ATOM   3063 C CD2 . TYR B 1 152 ? 16.032  -8.018  -30.293 1.00 34.93 ? 152 TYR B CD2 1 
ATOM   3064 C CE1 . TYR B 1 152 ? 17.340  -9.708  -32.062 1.00 38.55 ? 152 TYR B CE1 1 
ATOM   3065 C CE2 . TYR B 1 152 ? 15.558  -9.316  -30.493 1.00 33.87 ? 152 TYR B CE2 1 
ATOM   3066 C CZ  . TYR B 1 152 ? 16.221  -10.148 -31.377 1.00 37.33 ? 152 TYR B CZ  1 
ATOM   3067 O OH  . TYR B 1 152 ? 15.748  -11.414 -31.578 1.00 40.24 ? 152 TYR B OH  1 
ATOM   3068 N N   . LEU B 1 153 ? 19.484  -3.831  -29.236 1.00 32.22 ? 153 LEU B N   1 
ATOM   3069 C CA  . LEU B 1 153 ? 20.340  -2.642  -29.239 1.00 33.31 ? 153 LEU B CA  1 
ATOM   3070 C C   . LEU B 1 153 ? 21.797  -3.011  -28.957 1.00 35.95 ? 153 LEU B C   1 
ATOM   3071 O O   . LEU B 1 153 ? 22.726  -2.474  -29.577 1.00 36.27 ? 153 LEU B O   1 
ATOM   3072 C CB  . LEU B 1 153 ? 19.836  -1.645  -28.200 1.00 36.02 ? 153 LEU B CB  1 
ATOM   3073 C CG  . LEU B 1 153 ? 18.565  -0.843  -28.506 1.00 34.12 ? 153 LEU B CG  1 
ATOM   3074 C CD1 . LEU B 1 153 ? 18.215  0.015   -27.300 1.00 35.95 ? 153 LEU B CD1 1 
ATOM   3075 C CD2 . LEU B 1 153 ? 18.714  0.030   -29.772 1.00 29.60 ? 153 LEU B CD2 1 
ATOM   3076 N N   . LYS B 1 154 ? 22.009  -3.975  -28.065 1.00 36.18 ? 154 LYS B N   1 
ATOM   3077 C CA  . LYS B 1 154 ? 23.353  -4.379  -27.679 1.00 38.24 ? 154 LYS B CA  1 
ATOM   3078 C C   . LYS B 1 154 ? 24.109  -5.039  -28.822 1.00 39.66 ? 154 LYS B C   1 
ATOM   3079 O O   . LYS B 1 154 ? 25.340  -5.025  -28.816 1.00 45.31 ? 154 LYS B O   1 
ATOM   3080 C CB  . LYS B 1 154 ? 23.258  -5.326  -26.483 1.00 42.81 ? 154 LYS B CB  1 
ATOM   3081 C CG  . LYS B 1 154 ? 23.521  -4.644  -25.142 1.00 44.16 ? 154 LYS B CG  1 
ATOM   3082 C CD  . LYS B 1 154 ? 23.072  -5.542  -23.995 1.00 48.08 ? 154 LYS B CD  1 
ATOM   3083 C CE  . LYS B 1 154 ? 23.730  -6.911  -24.078 1.00 50.62 ? 154 LYS B CE  1 
ATOM   3084 N NZ  . LYS B 1 154 ? 24.846  -7.021  -23.084 1.00 52.91 ? 154 LYS B NZ  1 
ATOM   3085 N N   . LYS B 1 155 ? 23.409  -5.592  -29.809 1.00 38.94 ? 155 LYS B N   1 
ATOM   3086 C CA  . LYS B 1 155 ? 24.047  -6.060  -31.034 1.00 40.33 ? 155 LYS B CA  1 
ATOM   3087 C C   . LYS B 1 155 ? 24.233  -4.940  -32.055 1.00 39.43 ? 155 LYS B C   1 
ATOM   3088 O O   . LYS B 1 155 ? 24.696  -5.201  -33.171 1.00 41.11 ? 155 LYS B O   1 
ATOM   3089 C CB  . LYS B 1 155 ? 23.230  -7.199  -31.651 1.00 40.92 ? 155 LYS B CB  1 
ATOM   3090 C CG  . LYS B 1 155 ? 22.677  -8.154  -30.627 1.00 40.19 ? 155 LYS B CG  1 
ATOM   3091 C CD  . LYS B 1 155 ? 21.811  -9.205  -31.253 1.00 35.84 ? 155 LYS B CD  1 
ATOM   3092 C CE  . LYS B 1 155 ? 22.135  -10.567 -30.664 1.00 45.14 ? 155 LYS B CE  1 
ATOM   3093 N NZ  . LYS B 1 155 ? 20.920  -11.426 -30.560 1.00 47.67 ? 155 LYS B NZ  1 
ATOM   3094 N N   . GLY B 1 156 ? 23.865  -3.710  -31.713 1.00 34.77 ? 156 GLY B N   1 
ATOM   3095 C CA  . GLY B 1 156 ? 23.920  -2.616  -32.662 1.00 37.08 ? 156 GLY B CA  1 
ATOM   3096 C C   . GLY B 1 156 ? 22.749  -2.526  -33.612 1.00 33.70 ? 156 GLY B C   1 
ATOM   3097 O O   . GLY B 1 156 ? 22.842  -1.821  -34.620 1.00 32.64 ? 156 GLY B O   1 
ATOM   3098 N N   . PHE B 1 157 ? 21.655  -3.228  -33.342 1.00 32.31 ? 157 PHE B N   1 
ATOM   3099 C CA  . PHE B 1 157 ? 20.491  -3.133  -34.205 1.00 27.80 ? 157 PHE B CA  1 
ATOM   3100 C C   . PHE B 1 157 ? 19.501  -2.166  -33.570 1.00 31.93 ? 157 PHE B C   1 
ATOM   3101 O O   . PHE B 1 157 ? 19.094  -2.382  -32.413 1.00 29.01 ? 157 PHE B O   1 
ATOM   3102 C CB  . PHE B 1 157 ? 19.844  -4.498  -34.398 1.00 31.94 ? 157 PHE B CB  1 
ATOM   3103 C CG  . PHE B 1 157 ? 20.747  -5.545  -35.025 1.00 31.20 ? 157 PHE B CG  1 
ATOM   3104 C CD1 . PHE B 1 157 ? 21.832  -5.186  -35.818 1.00 32.04 ? 157 PHE B CD1 1 
ATOM   3105 C CD2 . PHE B 1 157 ? 20.481  -6.895  -34.842 1.00 36.29 ? 157 PHE B CD2 1 
ATOM   3106 C CE1 . PHE B 1 157 ? 22.639  -6.154  -36.388 1.00 36.23 ? 157 PHE B CE1 1 
ATOM   3107 C CE2 . PHE B 1 157 ? 21.279  -7.864  -35.428 1.00 36.28 ? 157 PHE B CE2 1 
ATOM   3108 C CZ  . PHE B 1 157 ? 22.360  -7.491  -36.198 1.00 33.88 ? 157 PHE B CZ  1 
ATOM   3109 N N   . PRO B 1 158 ? 19.116  -1.088  -34.247 1.00 29.93 ? 158 PRO B N   1 
ATOM   3110 C CA  . PRO B 1 158 ? 18.134  -0.164  -33.678 1.00 29.47 ? 158 PRO B CA  1 
ATOM   3111 C C   . PRO B 1 158 ? 16.725  -0.716  -33.864 1.00 27.94 ? 158 PRO B C   1 
ATOM   3112 O O   . PRO B 1 158 ? 16.494  -1.647  -34.638 1.00 27.24 ? 158 PRO B O   1 
ATOM   3113 C CB  . PRO B 1 158 ? 18.355  1.096   -34.500 1.00 27.30 ? 158 PRO B CB  1 
ATOM   3114 C CG  . PRO B 1 158 ? 18.685  0.577   -35.852 1.00 26.85 ? 158 PRO B CG  1 
ATOM   3115 C CD  . PRO B 1 158 ? 19.493  -0.699  -35.620 1.00 27.01 ? 158 PRO B CD  1 
ATOM   3116 N N   . VAL B 1 159 ? 15.761  -0.107  -33.178 1.00 25.31 ? 159 VAL B N   1 
ATOM   3117 C CA  . VAL B 1 159 ? 14.438  -0.729  -33.076 1.00 25.93 ? 159 VAL B CA  1 
ATOM   3118 C C   . VAL B 1 159 ? 13.365  0.297   -33.410 1.00 25.68 ? 159 VAL B C   1 
ATOM   3119 O O   . VAL B 1 159 ? 13.182  1.279   -32.681 1.00 23.30 ? 159 VAL B O   1 
ATOM   3120 C CB  . VAL B 1 159 ? 14.204  -1.346  -31.691 1.00 26.21 ? 159 VAL B CB  1 
ATOM   3121 C CG1 . VAL B 1 159 ? 12.762  -1.889  -31.568 1.00 28.85 ? 159 VAL B CG1 1 
ATOM   3122 C CG2 . VAL B 1 159 ? 15.217  -2.469  -31.445 1.00 27.33 ? 159 VAL B CG2 1 
ATOM   3123 N N   . ILE B 1 160 ? 12.654  0.069   -34.511 1.00 24.60 ? 160 ILE B N   1 
ATOM   3124 C CA  . ILE B 1 160 ? 11.560  0.948   -34.879 1.00 24.31 ? 160 ILE B CA  1 
ATOM   3125 C C   . ILE B 1 160 ? 10.379  0.676   -33.961 1.00 27.75 ? 160 ILE B C   1 
ATOM   3126 O O   . ILE B 1 160 ? 9.980   -0.478  -33.772 1.00 26.07 ? 160 ILE B O   1 
ATOM   3127 C CB  . ILE B 1 160 ? 11.176  0.745   -36.350 1.00 23.34 ? 160 ILE B CB  1 
ATOM   3128 C CG1 . ILE B 1 160 ? 12.286  1.311   -37.258 1.00 24.08 ? 160 ILE B CG1 1 
ATOM   3129 C CG2 . ILE B 1 160 ? 9.792   1.393   -36.625 1.00 23.19 ? 160 ILE B CG2 1 
ATOM   3130 C CD1 . ILE B 1 160 ? 12.052  1.097   -38.754 1.00 21.90 ? 160 ILE B CD1 1 
ATOM   3131 N N   . CYS B 1 161 ? 9.827   1.735   -33.381 1.00 26.17 ? 161 CYS B N   1 
ATOM   3132 C CA  . CYS B 1 161 ? 8.645   1.631   -32.542 1.00 25.46 ? 161 CYS B CA  1 
ATOM   3133 C C   . CYS B 1 161 ? 7.445   2.213   -33.272 1.00 25.95 ? 161 CYS B C   1 
ATOM   3134 O O   . CYS B 1 161 ? 7.582   3.116   -34.099 1.00 25.84 ? 161 CYS B O   1 
ATOM   3135 C CB  . CYS B 1 161 ? 8.850   2.344   -31.202 1.00 26.14 ? 161 CYS B CB  1 
ATOM   3136 S SG  . CYS B 1 161 ? 9.358   4.085   -31.333 1.00 27.90 ? 161 CYS B SG  1 
ATOM   3137 N N   . HIS B 1 162 ? 6.267   1.685   -32.956 1.00 21.52 ? 162 HIS B N   1 
ATOM   3138 C CA  . HIS B 1 162 ? 4.995   2.060   -33.566 1.00 23.96 ? 162 HIS B CA  1 
ATOM   3139 C C   . HIS B 1 162 ? 4.032   2.329   -32.423 1.00 26.68 ? 162 HIS B C   1 
ATOM   3140 O O   . HIS B 1 162 ? 3.943   1.519   -31.497 1.00 26.47 ? 162 HIS B O   1 
ATOM   3141 C CB  . HIS B 1 162 ? 4.473   0.912   -34.458 1.00 26.46 ? 162 HIS B CB  1 
ATOM   3142 C CG  . HIS B 1 162 ? 3.162   1.166   -35.143 1.00 28.66 ? 162 HIS B CG  1 
ATOM   3143 N ND1 . HIS B 1 162 ? 2.172   0.203   -35.235 1.00 26.87 ? 162 HIS B ND1 1 
ATOM   3144 C CD2 . HIS B 1 162 ? 2.680   2.257   -35.782 1.00 28.85 ? 162 HIS B CD2 1 
ATOM   3145 C CE1 . HIS B 1 162 ? 1.154   0.685   -35.924 1.00 27.14 ? 162 HIS B CE1 1 
ATOM   3146 N NE2 . HIS B 1 162 ? 1.428   1.935   -36.253 1.00 28.32 ? 162 HIS B NE2 1 
ATOM   3147 N N   . TRP B 1 163 ? 3.322   3.454   -32.459 1.00 24.56 ? 163 TRP B N   1 
ATOM   3148 C CA  . TRP B 1 163 ? 2.393   3.714   -31.352 1.00 25.75 ? 163 TRP B CA  1 
ATOM   3149 C C   . TRP B 1 163 ? 1.341   4.721   -31.775 1.00 27.53 ? 163 TRP B C   1 
ATOM   3150 O O   . TRP B 1 163 ? 1.474   5.373   -32.805 1.00 26.53 ? 163 TRP B O   1 
ATOM   3151 C CB  . TRP B 1 163 ? 3.130   4.183   -30.095 1.00 23.15 ? 163 TRP B CB  1 
ATOM   3152 C CG  . TRP B 1 163 ? 3.595   5.638   -29.968 1.00 27.33 ? 163 TRP B CG  1 
ATOM   3153 C CD1 . TRP B 1 163 ? 3.050   6.606   -29.149 1.00 27.81 ? 163 TRP B CD1 1 
ATOM   3154 C CD2 . TRP B 1 163 ? 4.742   6.257   -30.599 1.00 24.17 ? 163 TRP B CD2 1 
ATOM   3155 N NE1 . TRP B 1 163 ? 3.780   7.779   -29.247 1.00 27.80 ? 163 TRP B NE1 1 
ATOM   3156 C CE2 . TRP B 1 163 ? 4.817   7.595   -30.126 1.00 25.44 ? 163 TRP B CE2 1 
ATOM   3157 C CE3 . TRP B 1 163 ? 5.704   5.815   -31.507 1.00 27.89 ? 163 TRP B CE3 1 
ATOM   3158 C CZ2 . TRP B 1 163 ? 5.807   8.496   -30.546 1.00 26.17 ? 163 TRP B CZ2 1 
ATOM   3159 C CZ3 . TRP B 1 163 ? 6.701   6.719   -31.927 1.00 27.95 ? 163 TRP B CZ3 1 
ATOM   3160 C CH2 . TRP B 1 163 ? 6.741   8.043   -31.436 1.00 26.38 ? 163 TRP B CH2 1 
ATOM   3161 N N   . GLN B 1 164 ? 0.249   4.786   -30.992 1.00 27.02 ? 164 GLN B N   1 
ATOM   3162 C CA  . GLN B 1 164 ? -0.814  5.769   -31.203 1.00 26.60 ? 164 GLN B CA  1 
ATOM   3163 C C   . GLN B 1 164 ? -0.524  6.916   -30.247 1.00 29.38 ? 164 GLN B C   1 
ATOM   3164 O O   . GLN B 1 164 ? -0.546  6.725   -29.027 1.00 28.12 ? 164 GLN B O   1 
ATOM   3165 C CB  . GLN B 1 164 ? -2.195  5.156   -30.958 1.00 29.67 ? 164 GLN B CB  1 
ATOM   3166 C CG  . GLN B 1 164 ? -2.384  3.777   -31.592 1.00 28.20 ? 164 GLN B CG  1 
ATOM   3167 C CD  . GLN B 1 164 ? -2.267  3.809   -33.111 1.00 31.08 ? 164 GLN B CD  1 
ATOM   3168 O OE1 . GLN B 1 164 ? -2.950  4.599   -33.793 1.00 28.59 ? 164 GLN B OE1 1 
ATOM   3169 N NE2 . GLN B 1 164 ? -1.365  2.969   -33.654 1.00 28.05 ? 164 GLN B NE2 1 
ATOM   3170 N N   . VAL B 1 165 ? -0.194  8.098   -30.798 1.00 27.86 ? 165 VAL B N   1 
ATOM   3171 C CA  . VAL B 1 165 ? 0.301   9.167   -29.938 1.00 28.14 ? 165 VAL B CA  1 
ATOM   3172 C C   . VAL B 1 165 ? -0.742  9.568   -28.895 1.00 29.47 ? 165 VAL B C   1 
ATOM   3173 O O   . VAL B 1 165 ? -0.381  9.978   -27.788 1.00 31.05 ? 165 VAL B O   1 
ATOM   3174 C CB  . VAL B 1 165 ? 0.778   10.378  -30.762 1.00 28.79 ? 165 VAL B CB  1 
ATOM   3175 C CG1 . VAL B 1 165 ? 1.962   9.969   -31.650 1.00 27.74 ? 165 VAL B CG1 1 
ATOM   3176 C CG2 . VAL B 1 165 ? -0.372  10.993  -31.582 1.00 27.39 ? 165 VAL B CG2 1 
ATOM   3177 N N   . ASN B 1 166 ? -2.033  9.417   -29.209 1.00 28.37 ? 166 ASN B N   1 
ATOM   3178 C CA  . ASN B 1 166 ? -3.093  9.756   -28.250 1.00 32.47 ? 166 ASN B CA  1 
ATOM   3179 C C   . ASN B 1 166 ? -3.036  8.892   -27.008 1.00 31.78 ? 166 ASN B C   1 
ATOM   3180 O O   . ASN B 1 166 ? -3.447  9.328   -25.928 1.00 32.02 ? 166 ASN B O   1 
ATOM   3181 C CB  . ASN B 1 166 ? -4.459  9.584   -28.897 1.00 35.19 ? 166 ASN B CB  1 
ATOM   3182 C CG  . ASN B 1 166 ? -4.490  8.411   -29.855 1.00 37.81 ? 166 ASN B CG  1 
ATOM   3183 O OD1 . ASN B 1 166 ? -3.686  8.338   -30.808 1.00 35.63 ? 166 ASN B OD1 1 
ATOM   3184 N ND2 . ASN B 1 166 ? -5.397  7.478   -29.609 1.00 38.17 ? 166 ASN B ND2 1 
ATOM   3185 N N   . GLN B 1 167 ? -2.549  7.658   -27.139 1.00 29.61 ? 167 GLN B N   1 
ATOM   3186 C CA  . GLN B 1 167 ? -2.404  6.774   -25.995 1.00 28.49 ? 167 GLN B CA  1 
ATOM   3187 C C   . GLN B 1 167 ? -1.184  7.106   -25.157 1.00 32.20 ? 167 GLN B C   1 
ATOM   3188 O O   . GLN B 1 167 ? -0.986  6.481   -24.115 1.00 32.62 ? 167 GLN B O   1 
ATOM   3189 C CB  . GLN B 1 167 ? -2.332  5.312   -26.466 1.00 28.42 ? 167 GLN B CB  1 
ATOM   3190 C CG  . GLN B 1 167 ? -3.570  4.873   -27.241 1.00 28.80 ? 167 GLN B CG  1 
ATOM   3191 C CD  . GLN B 1 167 ? -3.594  3.389   -27.516 1.00 28.47 ? 167 GLN B CD  1 
ATOM   3192 O OE1 . GLN B 1 167 ? -2.909  2.606   -26.848 1.00 28.62 ? 167 GLN B OE1 1 
ATOM   3193 N NE2 . GLN B 1 167 ? -4.366  2.988   -28.523 1.00 26.10 ? 167 GLN B NE2 1 
ATOM   3194 N N   . SER B 1 168 ? -0.327  8.033   -25.595 1.00 30.05 ? 168 SER B N   1 
ATOM   3195 C CA  . SER B 1 168 ? 0.810   8.422   -24.775 1.00 29.18 ? 168 SER B CA  1 
ATOM   3196 C C   . SER B 1 168 ? 0.656   9.833   -24.225 1.00 33.63 ? 168 SER B C   1 
ATOM   3197 O O   . SER B 1 168 ? 1.595   10.355  -23.639 1.00 34.54 ? 168 SER B O   1 
ATOM   3198 C CB  . SER B 1 168 ? 2.130   8.275   -25.551 1.00 30.45 ? 168 SER B CB  1 
ATOM   3199 O OG  . SER B 1 168 ? 2.271   9.234   -26.578 1.00 30.30 ? 168 SER B OG  1 
ATOM   3200 N N   . ARG B 1 169 ? -0.542  10.407  -24.294 1.00 34.49 ? 169 ARG B N   1 
ATOM   3201 C CA  . ARG B 1 169 ? -0.713  11.815  -23.947 1.00 36.70 ? 169 ARG B CA  1 
ATOM   3202 C C   . ARG B 1 169 ? -0.463  12.078  -22.466 1.00 37.11 ? 169 ARG B C   1 
ATOM   3203 O O   . ARG B 1 169 ? 0.166   13.076  -22.117 1.00 39.00 ? 169 ARG B O   1 
ATOM   3204 C CB  . ARG B 1 169 ? -2.114  12.266  -24.332 1.00 35.46 ? 169 ARG B CB  1 
ATOM   3205 C CG  . ARG B 1 169 ? -2.460  13.655  -23.819 1.00 41.94 ? 169 ARG B CG  1 
ATOM   3206 C CD  . ARG B 1 169 ? -3.485  14.324  -24.694 1.00 43.08 ? 169 ARG B CD  1 
ATOM   3207 N NE  . ARG B 1 169 ? -3.774  15.664  -24.197 1.00 50.71 ? 169 ARG B NE  1 
ATOM   3208 C CZ  . ARG B 1 169 ? -4.492  16.571  -24.843 1.00 48.43 ? 169 ARG B CZ  1 
ATOM   3209 N NH1 . ARG B 1 169 ? -5.125  16.279  -25.971 1.00 44.73 ? 169 ARG B NH1 1 
ATOM   3210 N NH2 . ARG B 1 169 ? -4.622  17.785  -24.317 1.00 51.13 ? 169 ARG B NH2 1 
ATOM   3211 N N   . ASN B 1 170 ? -0.901  11.174  -21.584 1.00 39.12 ? 170 ASN B N   1 
ATOM   3212 C CA  . ASN B 1 170 ? -0.746  11.386  -20.148 1.00 37.76 ? 170 ASN B CA  1 
ATOM   3213 C C   . ASN B 1 170 ? 0.609   10.928  -19.627 1.00 37.47 ? 170 ASN B C   1 
ATOM   3214 O O   . ASN B 1 170 ? 1.125   11.511  -18.667 1.00 38.94 ? 170 ASN B O   1 
ATOM   3215 C CB  . ASN B 1 170 ? -1.871  10.670  -19.393 1.00 36.43 ? 170 ASN B CB  1 
ATOM   3216 C CG  . ASN B 1 170 ? -3.234  11.317  -19.614 1.00 43.79 ? 170 ASN B CG  1 
ATOM   3217 O OD1 . ASN B 1 170 ? -3.344  12.395  -20.212 1.00 47.37 ? 170 ASN B OD1 1 
ATOM   3218 N ND2 . ASN B 1 170 ? -4.283  10.646  -19.158 1.00 49.10 ? 170 ASN B ND2 1 
ATOM   3219 N N   . CYS B 1 171 ? 1.215   9.910   -20.233 1.00 35.87 ? 171 CYS B N   1 
ATOM   3220 C CA  . CYS B 1 171 ? 2.509   9.459   -19.731 1.00 35.09 ? 171 CYS B CA  1 
ATOM   3221 C C   . CYS B 1 171 ? 3.677   10.114  -20.462 1.00 37.00 ? 171 CYS B C   1 
ATOM   3222 O O   . CYS B 1 171 ? 4.817   9.975   -20.009 1.00 36.87 ? 171 CYS B O   1 
ATOM   3223 C CB  . CYS B 1 171 ? 2.613   7.930   -19.820 1.00 33.72 ? 171 CYS B CB  1 
ATOM   3224 S SG  . CYS B 1 171 ? 2.264   7.221   -21.459 1.00 40.62 ? 171 CYS B SG  1 
ATOM   3225 N N   . LYS B 1 172 ? 3.407   10.800  -21.580 1.00 32.85 ? 172 LYS B N   1 
ATOM   3226 C CA  . LYS B 1 172 ? 4.392   11.593  -22.321 1.00 36.63 ? 172 LYS B CA  1 
ATOM   3227 C C   . LYS B 1 172 ? 3.598   12.615  -23.136 1.00 38.29 ? 172 LYS B C   1 
ATOM   3228 O O   . LYS B 1 172 ? 2.911   12.253  -24.090 1.00 44.92 ? 172 LYS B O   1 
ATOM   3229 C CB  . LYS B 1 172 ? 5.248   10.698  -23.205 1.00 31.45 ? 172 LYS B CB  1 
ATOM   3230 C CG  . LYS B 1 172 ? 6.158   11.451  -24.163 1.00 35.57 ? 172 LYS B CG  1 
ATOM   3231 C CD  . LYS B 1 172 ? 7.473   11.754  -23.525 1.00 34.88 ? 172 LYS B CD  1 
ATOM   3232 C CE  . LYS B 1 172 ? 8.323   12.645  -24.419 1.00 33.00 ? 172 LYS B CE  1 
ATOM   3233 N NZ  . LYS B 1 172 ? 9.468   13.083  -23.621 1.00 32.49 ? 172 LYS B NZ  1 
ATOM   3234 N N   . GLY B 1 173 ? 3.694   13.872  -22.816 1.00 34.31 ? 173 GLY B N   1 
ATOM   3235 C CA  . GLY B 1 173 ? 2.748   14.761  -23.487 1.00 37.75 ? 173 GLY B CA  1 
ATOM   3236 C C   . GLY B 1 173 ? 3.153   15.381  -24.817 1.00 36.63 ? 173 GLY B C   1 
ATOM   3237 O O   . GLY B 1 173 ? 2.759   16.516  -25.082 1.00 34.60 ? 173 GLY B O   1 
ATOM   3238 N N   . ASP B 1 174 ? 3.927   14.696  -25.667 1.00 31.02 ? 174 ASP B N   1 
ATOM   3239 C CA  . ASP B 1 174 ? 4.407   15.393  -26.862 1.00 32.02 ? 174 ASP B CA  1 
ATOM   3240 C C   . ASP B 1 174 ? 3.279   15.777  -27.817 1.00 28.37 ? 174 ASP B C   1 
ATOM   3241 O O   . ASP B 1 174 ? 3.376   16.806  -28.497 1.00 29.50 ? 174 ASP B O   1 
ATOM   3242 C CB  . ASP B 1 174 ? 5.428   14.524  -27.613 1.00 28.87 ? 174 ASP B CB  1 
ATOM   3243 C CG  . ASP B 1 174 ? 6.831   14.695  -27.099 1.00 32.70 ? 174 ASP B CG  1 
ATOM   3244 O OD1 . ASP B 1 174 ? 7.029   15.505  -26.173 1.00 33.14 ? 174 ASP B OD1 1 
ATOM   3245 O OD2 . ASP B 1 174 ? 7.741   14.005  -27.615 1.00 31.46 ? 174 ASP B OD2 1 
ATOM   3246 N N   . TYR B 1 175 ? 2.206   14.996  -27.879 1.00 27.43 ? 175 TYR B N   1 
ATOM   3247 C CA  . TYR B 1 175 ? 1.187   15.154  -28.902 1.00 25.80 ? 175 TYR B CA  1 
ATOM   3248 C C   . TYR B 1 175 ? -0.198  15.342  -28.295 1.00 31.39 ? 175 TYR B C   1 
ATOM   3249 O O   . TYR B 1 175 ? -0.524  14.752  -27.267 1.00 30.87 ? 175 TYR B O   1 
ATOM   3250 C CB  . TYR B 1 175 ? 1.135   13.956  -29.836 1.00 27.25 ? 175 TYR B CB  1 
ATOM   3251 C CG  . TYR B 1 175 ? 2.398   13.765  -30.635 1.00 27.68 ? 175 TYR B CG  1 
ATOM   3252 C CD1 . TYR B 1 175 ? 2.593   14.449  -31.831 1.00 26.68 ? 175 TYR B CD1 1 
ATOM   3253 C CD2 . TYR B 1 175 ? 3.370   12.879  -30.209 1.00 28.65 ? 175 TYR B CD2 1 
ATOM   3254 C CE1 . TYR B 1 175 ? 3.760   14.260  -32.585 1.00 30.48 ? 175 TYR B CE1 1 
ATOM   3255 C CE2 . TYR B 1 175 ? 4.532   12.676  -30.941 1.00 26.87 ? 175 TYR B CE2 1 
ATOM   3256 C CZ  . TYR B 1 175 ? 4.720   13.361  -32.124 1.00 28.98 ? 175 TYR B CZ  1 
ATOM   3257 O OH  . TYR B 1 175 ? 5.878   13.146  -32.817 1.00 26.45 ? 175 TYR B OH  1 
ATOM   3258 N N   . THR B 1 176 ? -0.997  16.192  -28.939 1.00 29.85 ? 176 THR B N   1 
ATOM   3259 C CA  . THR B 1 176 ? -2.403  16.370  -28.627 1.00 33.86 ? 176 THR B CA  1 
ATOM   3260 C C   . THR B 1 176 ? -3.300  15.743  -29.673 1.00 32.80 ? 176 THR B C   1 
ATOM   3261 O O   . THR B 1 176 ? -4.503  15.610  -29.435 1.00 33.86 ? 176 THR B O   1 
ATOM   3262 C CB  . THR B 1 176 ? -2.746  17.867  -28.547 1.00 32.28 ? 176 THR B CB  1 
ATOM   3263 O OG1 . THR B 1 176 ? -2.409  18.447  -29.803 1.00 31.50 ? 176 THR B OG1 1 
ATOM   3264 C CG2 . THR B 1 176 ? -1.947  18.555  -27.457 1.00 29.17 ? 176 THR B CG2 1 
ATOM   3265 N N   . GLY B 1 177 ? -2.752  15.376  -30.829 1.00 30.40 ? 177 GLY B N   1 
ATOM   3266 C CA  . GLY B 1 177 ? -3.533  14.825  -31.909 1.00 32.81 ? 177 GLY B CA  1 
ATOM   3267 C C   . GLY B 1 177 ? -3.804  13.345  -31.709 1.00 34.62 ? 177 GLY B C   1 
ATOM   3268 O O   . GLY B 1 177 ? -3.498  12.758  -30.670 1.00 33.12 ? 177 GLY B O   1 
ATOM   3269 N N   . ASN B 1 178 ? -4.469  12.761  -32.700 1.00 31.18 ? 178 ASN B N   1 
ATOM   3270 C CA  . ASN B 1 178 ? -4.845  11.346  -32.696 1.00 33.03 ? 178 ASN B CA  1 
ATOM   3271 C C   . ASN B 1 178 ? -4.404  10.733  -34.026 1.00 37.35 ? 178 ASN B C   1 
ATOM   3272 O O   . ASN B 1 178 ? -5.055  10.952  -35.058 1.00 37.64 ? 178 ASN B O   1 
ATOM   3273 C CB  . ASN B 1 178 ? -6.343  11.202  -32.468 1.00 37.46 ? 178 ASN B CB  1 
ATOM   3274 C CG  . ASN B 1 178 ? -6.772  11.792  -31.143 1.00 39.38 ? 178 ASN B CG  1 
ATOM   3275 O OD1 . ASN B 1 178 ? -6.998  13.000  -31.027 1.00 46.58 ? 178 ASN B OD1 1 
ATOM   3276 N ND2 . ASN B 1 178 ? -6.893  10.945  -30.136 1.00 42.72 ? 178 ASN B ND2 1 
ATOM   3277 N N   . PHE B 1 179 ? -3.310  9.962   -33.998 1.00 28.86 ? 179 PHE B N   1 
ATOM   3278 C CA  . PHE B 1 179 ? -2.816  9.269   -35.182 1.00 28.12 ? 179 PHE B CA  1 
ATOM   3279 C C   . PHE B 1 179 ? -1.813  8.207   -34.762 1.00 26.77 ? 179 PHE B C   1 
ATOM   3280 O O   . PHE B 1 179 ? -1.251  8.271   -33.664 1.00 26.72 ? 179 PHE B O   1 
ATOM   3281 C CB  . PHE B 1 179 ? -2.164  10.233  -36.186 1.00 30.13 ? 179 PHE B CB  1 
ATOM   3282 C CG  . PHE B 1 179 ? -1.109  11.167  -35.590 1.00 31.51 ? 179 PHE B CG  1 
ATOM   3283 C CD1 . PHE B 1 179 ? -1.469  12.420  -35.062 1.00 34.99 ? 179 PHE B CD1 1 
ATOM   3284 C CD2 . PHE B 1 179 ? 0.237   10.817  -35.593 1.00 27.81 ? 179 PHE B CD2 1 
ATOM   3285 C CE1 . PHE B 1 179 ? -0.475  13.300  -34.542 1.00 30.16 ? 179 PHE B CE1 1 
ATOM   3286 C CE2 . PHE B 1 179 ? 1.222   11.677  -35.071 1.00 28.19 ? 179 PHE B CE2 1 
ATOM   3287 C CZ  . PHE B 1 179 ? 0.868   12.915  -34.556 1.00 27.67 ? 179 PHE B CZ  1 
ATOM   3288 N N   . GLY B 1 180 ? -1.617  7.211   -35.641 1.00 23.02 ? 180 GLY B N   1 
ATOM   3289 C CA  . GLY B 1 180 ? -0.517  6.272   -35.469 1.00 23.49 ? 180 GLY B CA  1 
ATOM   3290 C C   . GLY B 1 180 ? 0.822   6.835   -35.947 1.00 26.30 ? 180 GLY B C   1 
ATOM   3291 O O   . GLY B 1 180 ? 0.911   7.617   -36.890 1.00 23.85 ? 180 GLY B O   1 
ATOM   3292 N N   . HIS B 1 181 ? 1.902   6.386   -35.323 1.00 25.73 ? 181 HIS B N   1 
ATOM   3293 C CA  . HIS B 1 181 ? 3.174   7.040   -35.561 1.00 26.49 ? 181 HIS B CA  1 
ATOM   3294 C C   . HIS B 1 181 ? 4.304   6.024   -35.445 1.00 28.58 ? 181 HIS B C   1 
ATOM   3295 O O   . HIS B 1 181 ? 4.124   4.928   -34.901 1.00 23.04 ? 181 HIS B O   1 
ATOM   3296 C CB  . HIS B 1 181 ? 3.358   8.203   -34.586 1.00 25.65 ? 181 HIS B CB  1 
ATOM   3297 C CG  . HIS B 1 181 ? 4.436   9.161   -34.973 1.00 27.59 ? 181 HIS B CG  1 
ATOM   3298 N ND1 . HIS B 1 181 ? 4.544   9.694   -36.241 1.00 24.48 ? 181 HIS B ND1 1 
ATOM   3299 C CD2 . HIS B 1 181 ? 5.409   9.740   -34.237 1.00 25.54 ? 181 HIS B CD2 1 
ATOM   3300 C CE1 . HIS B 1 181 ? 5.554   10.547  -36.270 1.00 27.21 ? 181 HIS B CE1 1 
ATOM   3301 N NE2 . HIS B 1 181 ? 6.098   10.591  -35.067 1.00 25.95 ? 181 HIS B NE2 1 
ATOM   3302 N N   . TYR B 1 182 ? 5.483   6.398   -35.996 1.00 21.71 ? 182 TYR B N   1 
ATOM   3303 C CA  . TYR B 1 182 ? 6.681   5.584   -35.896 1.00 25.71 ? 182 TYR B CA  1 
ATOM   3304 C C   . TYR B 1 182 ? 7.843   6.451   -35.429 1.00 27.28 ? 182 TYR B C   1 
ATOM   3305 O O   . TYR B 1 182 ? 7.859   7.663   -35.682 1.00 23.91 ? 182 TYR B O   1 
ATOM   3306 C CB  . TYR B 1 182 ? 7.066   4.947   -37.229 1.00 24.67 ? 182 TYR B CB  1 
ATOM   3307 C CG  . TYR B 1 182 ? 6.138   3.861   -37.717 1.00 25.75 ? 182 TYR B CG  1 
ATOM   3308 C CD1 . TYR B 1 182 ? 4.990   4.182   -38.421 1.00 26.73 ? 182 TYR B CD1 1 
ATOM   3309 C CD2 . TYR B 1 182 ? 6.455   2.528   -37.545 1.00 25.35 ? 182 TYR B CD2 1 
ATOM   3310 C CE1 . TYR B 1 182 ? 4.150   3.212   -38.906 1.00 26.71 ? 182 TYR B CE1 1 
ATOM   3311 C CE2 . TYR B 1 182 ? 5.619   1.531   -38.023 1.00 29.85 ? 182 TYR B CE2 1 
ATOM   3312 C CZ  . TYR B 1 182 ? 4.470   1.875   -38.703 1.00 30.65 ? 182 TYR B CZ  1 
ATOM   3313 O OH  . TYR B 1 182 ? 3.633   0.888   -39.196 1.00 28.74 ? 182 TYR B OH  1 
ATOM   3314 N N   . GLY B 1 183 ? 8.794   5.813   -34.730 1.00 22.66 ? 183 GLY B N   1 
ATOM   3315 C CA  . GLY B 1 183 ? 10.031  6.400   -34.249 1.00 25.00 ? 183 GLY B CA  1 
ATOM   3316 C C   . GLY B 1 183 ? 11.140  5.344   -34.276 1.00 24.75 ? 183 GLY B C   1 
ATOM   3317 O O   . GLY B 1 183 ? 10.880  4.185   -34.575 1.00 25.74 ? 183 GLY B O   1 
ATOM   3318 N N   . LEU B 1 184 ? 12.337  5.764   -33.933 1.00 23.83 ? 184 LEU B N   1 
ATOM   3319 C CA  . LEU B 1 184 ? 13.460  4.818   -33.903 1.00 21.92 ? 184 LEU B CA  1 
ATOM   3320 C C   . LEU B 1 184 ? 14.006  4.755   -32.485 1.00 23.53 ? 184 LEU B C   1 
ATOM   3321 O O   . LEU B 1 184 ? 14.502  5.764   -32.006 1.00 26.06 ? 184 LEU B O   1 
ATOM   3322 C CB  . LEU B 1 184 ? 14.541  5.328   -34.848 1.00 21.99 ? 184 LEU B CB  1 
ATOM   3323 C CG  . LEU B 1 184 ? 15.485  4.277   -35.410 1.00 24.77 ? 184 LEU B CG  1 
ATOM   3324 C CD1 . LEU B 1 184 ? 16.915  4.545   -35.026 1.00 26.28 ? 184 LEU B CD1 1 
ATOM   3325 C CD2 . LEU B 1 184 ? 15.059  2.872   -35.082 1.00 32.43 ? 184 LEU B CD2 1 
ATOM   3326 N N   . ILE B 1 185 ? 13.847  3.615   -31.836 1.00 24.03 ? 185 ILE B N   1 
ATOM   3327 C CA  . ILE B 1 185 ? 14.508  3.492   -30.562 1.00 23.79 ? 185 ILE B CA  1 
ATOM   3328 C C   . ILE B 1 185 ? 15.989  3.244   -30.808 1.00 26.29 ? 185 ILE B C   1 
ATOM   3329 O O   . ILE B 1 185 ? 16.344  2.172   -31.305 1.00 25.88 ? 185 ILE B O   1 
ATOM   3330 C CB  . ILE B 1 185 ? 13.913  2.377   -29.701 1.00 29.05 ? 185 ILE B CB  1 
ATOM   3331 C CG1 . ILE B 1 185 ? 12.404  2.513   -29.524 1.00 23.55 ? 185 ILE B CG1 1 
ATOM   3332 C CG2 . ILE B 1 185 ? 14.731  2.202   -28.358 1.00 25.51 ? 185 ILE B CG2 1 
ATOM   3333 C CD1 . ILE B 1 185 ? 11.779  1.218   -28.962 1.00 27.05 ? 185 ILE B CD1 1 
ATOM   3334 N N   . TRP B 1 186 ? 16.865  4.171   -30.394 1.00 25.45 ? 186 TRP B N   1 
ATOM   3335 C CA  . TRP B 1 186 ? 18.294  3.958   -30.608 1.00 30.01 ? 186 TRP B CA  1 
ATOM   3336 C C   . TRP B 1 186 ? 19.137  3.859   -29.327 1.00 32.19 ? 186 TRP B C   1 
ATOM   3337 O O   . TRP B 1 186 ? 20.357  3.617   -29.414 1.00 30.09 ? 186 TRP B O   1 
ATOM   3338 C CB  . TRP B 1 186 ? 18.854  5.063   -31.526 1.00 29.77 ? 186 TRP B CB  1 
ATOM   3339 C CG  . TRP B 1 186 ? 18.676  6.453   -31.010 1.00 29.12 ? 186 TRP B CG  1 
ATOM   3340 C CD1 . TRP B 1 186 ? 17.575  7.262   -31.140 1.00 28.70 ? 186 TRP B CD1 1 
ATOM   3341 C CD2 . TRP B 1 186 ? 19.648  7.216   -30.289 1.00 29.89 ? 186 TRP B CD2 1 
ATOM   3342 N NE1 . TRP B 1 186 ? 17.805  8.477   -30.525 1.00 27.79 ? 186 TRP B NE1 1 
ATOM   3343 C CE2 . TRP B 1 186 ? 19.061  8.464   -29.980 1.00 29.57 ? 186 TRP B CE2 1 
ATOM   3344 C CE3 . TRP B 1 186 ? 20.945  6.949   -29.835 1.00 32.37 ? 186 TRP B CE3 1 
ATOM   3345 C CZ2 . TRP B 1 186 ? 19.741  9.452   -29.263 1.00 29.40 ? 186 TRP B CZ2 1 
ATOM   3346 C CZ3 . TRP B 1 186 ? 21.620  7.946   -29.122 1.00 33.30 ? 186 TRP B CZ3 1 
ATOM   3347 C CH2 . TRP B 1 186 ? 21.014  9.170   -28.845 1.00 31.91 ? 186 TRP B CH2 1 
ATOM   3348 N N   . ASP B 1 187 ? 18.535  4.051   -28.151 1.00 34.13 ? 187 ASP B N   1 
ATOM   3349 C CA  . ASP B 1 187 ? 19.237  3.953   -26.873 1.00 34.06 ? 187 ASP B CA  1 
ATOM   3350 C C   . ASP B 1 187 ? 18.210  3.756   -25.764 1.00 32.15 ? 187 ASP B C   1 
ATOM   3351 O O   . ASP B 1 187 ? 17.006  3.866   -25.986 1.00 30.47 ? 187 ASP B O   1 
ATOM   3352 C CB  . ASP B 1 187 ? 20.083  5.201   -26.598 1.00 34.88 ? 187 ASP B CB  1 
ATOM   3353 C CG  . ASP B 1 187 ? 21.155  4.965   -25.541 1.00 37.66 ? 187 ASP B CG  1 
ATOM   3354 O OD1 . ASP B 1 187 ? 21.381  3.792   -25.144 1.00 37.13 ? 187 ASP B OD1 1 
ATOM   3355 O OD2 . ASP B 1 187 ? 21.760  5.963   -25.100 1.00 37.37 ? 187 ASP B OD2 1 
ATOM   3356 N N   . MET B 1 188 ? 18.701  3.439   -24.567 1.00 34.61 ? 188 MET B N   1 
ATOM   3357 C CA  . MET B 1 188 ? 17.839  3.299   -23.395 1.00 39.43 ? 188 MET B CA  1 
ATOM   3358 C C   . MET B 1 188 ? 18.600  3.708   -22.150 1.00 38.65 ? 188 MET B C   1 
ATOM   3359 O O   . MET B 1 188 ? 19.808  3.495   -22.049 1.00 40.21 ? 188 MET B O   1 
ATOM   3360 C CB  . MET B 1 188 ? 17.306  1.884   -23.105 1.00 36.87 ? 188 MET B CB  1 
ATOM   3361 C CG  . MET B 1 188 ? 16.552  1.131   -24.179 1.00 38.56 ? 188 MET B CG  1 
ATOM   3362 S SD  . MET B 1 188 ? 16.783  -0.655  -23.952 1.00 40.25 ? 188 MET B SD  1 
ATOM   3363 C CE  . MET B 1 188 ? 15.961  -0.912  -22.399 1.00 32.34 ? 188 MET B CE  1 
ATOM   3364 N N   . THR B 1 189 ? 17.872  4.274   -21.196 1.00 38.67 ? 189 THR B N   1 
ATOM   3365 C CA  . THR B 1 189 ? 18.348  4.341   -19.826 1.00 40.21 ? 189 THR B CA  1 
ATOM   3366 C C   . THR B 1 189 ? 17.767  3.146   -19.062 1.00 39.03 ? 189 THR B C   1 
ATOM   3367 O O   . THR B 1 189 ? 17.146  2.249   -19.639 1.00 40.28 ? 189 THR B O   1 
ATOM   3368 C CB  . THR B 1 189 ? 17.938  5.651   -19.169 1.00 38.92 ? 189 THR B CB  1 
ATOM   3369 O OG1 . THR B 1 189 ? 16.511  5.698   -19.088 1.00 42.44 ? 189 THR B OG1 1 
ATOM   3370 C CG2 . THR B 1 189 ? 18.413  6.833   -19.994 1.00 40.47 ? 189 THR B CG2 1 
ATOM   3371 N N   . SER B 1 190 ? 17.921  3.151   -17.740 1.00 41.66 ? 190 SER B N   1 
ATOM   3372 C CA  . SER B 1 190 ? 17.348  2.094   -16.914 1.00 41.16 ? 190 SER B CA  1 
ATOM   3373 C C   . SER B 1 190 ? 15.823  2.166   -16.832 1.00 40.80 ? 190 SER B C   1 
ATOM   3374 O O   . SER B 1 190 ? 15.194  1.186   -16.417 1.00 41.62 ? 190 SER B O   1 
ATOM   3375 C CB  . SER B 1 190 ? 17.949  2.161   -15.509 1.00 45.28 ? 190 SER B CB  1 
ATOM   3376 O OG  . SER B 1 190 ? 17.534  3.358   -14.859 1.00 49.61 ? 190 SER B OG  1 
ATOM   3377 N N   . THR B 1 191 ? 15.215  3.284   -17.227 1.00 39.10 ? 191 THR B N   1 
ATOM   3378 C CA  . THR B 1 191 ? 13.771  3.474   -17.115 1.00 39.34 ? 191 THR B CA  1 
ATOM   3379 C C   . THR B 1 191 ? 13.075  3.898   -18.402 1.00 39.55 ? 191 THR B C   1 
ATOM   3380 O O   . THR B 1 191 ? 11.856  3.697   -18.505 1.00 37.15 ? 191 THR B O   1 
ATOM   3381 C CB  . THR B 1 191 ? 13.444  4.527   -16.042 1.00 39.20 ? 191 THR B CB  1 
ATOM   3382 O OG1 . THR B 1 191 ? 14.150  5.735   -16.348 1.00 37.80 ? 191 THR B OG1 1 
ATOM   3383 C CG2 . THR B 1 191 ? 13.836  4.043   -14.658 1.00 41.37 ? 191 THR B CG2 1 
ATOM   3384 N N   . HIS B 1 192 ? 13.785  4.487   -19.372 1.00 37.57 ? 192 HIS B N   1 
ATOM   3385 C CA  . HIS B 1 192 ? 13.170  5.108   -20.541 1.00 36.27 ? 192 HIS B CA  1 
ATOM   3386 C C   . HIS B 1 192 ? 13.767  4.588   -21.839 1.00 34.25 ? 192 HIS B C   1 
ATOM   3387 O O   . HIS B 1 192 ? 14.978  4.387   -21.925 1.00 33.90 ? 192 HIS B O   1 
ATOM   3388 C CB  . HIS B 1 192 ? 13.368  6.641   -20.523 1.00 35.21 ? 192 HIS B CB  1 
ATOM   3389 C CG  . HIS B 1 192 ? 12.524  7.355   -19.526 1.00 36.66 ? 192 HIS B CG  1 
ATOM   3390 N ND1 . HIS B 1 192 ? 12.853  7.426   -18.191 1.00 41.44 ? 192 HIS B ND1 1 
ATOM   3391 C CD2 . HIS B 1 192 ? 11.393  8.082   -19.673 1.00 38.02 ? 192 HIS B CD2 1 
ATOM   3392 C CE1 . HIS B 1 192 ? 11.941  8.137   -17.553 1.00 38.17 ? 192 HIS B CE1 1 
ATOM   3393 N NE2 . HIS B 1 192 ? 11.046  8.547   -18.429 1.00 36.70 ? 192 HIS B NE2 1 
ATOM   3394 N N   . TYR B 1 193 ? 12.923  4.434   -22.865 1.00 31.16 ? 193 TYR B N   1 
ATOM   3395 C CA  . TYR B 1 193 ? 13.416  4.343   -24.237 1.00 29.08 ? 193 TYR B CA  1 
ATOM   3396 C C   . TYR B 1 193 ? 13.853  5.723   -24.731 1.00 31.69 ? 193 TYR B C   1 
ATOM   3397 O O   . TYR B 1 193 ? 13.199  6.725   -24.442 1.00 29.14 ? 193 TYR B O   1 
ATOM   3398 C CB  . TYR B 1 193 ? 12.332  3.830   -25.174 1.00 26.74 ? 193 TYR B CB  1 
ATOM   3399 C CG  . TYR B 1 193 ? 11.788  2.454   -24.897 1.00 32.47 ? 193 TYR B CG  1 
ATOM   3400 C CD1 . TYR B 1 193 ? 12.595  1.319   -25.000 1.00 29.66 ? 193 TYR B CD1 1 
ATOM   3401 C CD2 . TYR B 1 193 ? 10.430  2.277   -24.577 1.00 30.64 ? 193 TYR B CD2 1 
ATOM   3402 C CE1 . TYR B 1 193 ? 12.068  0.035   -24.762 1.00 30.28 ? 193 TYR B CE1 1 
ATOM   3403 C CE2 . TYR B 1 193 ? 9.900   1.005   -24.351 1.00 29.93 ? 193 TYR B CE2 1 
ATOM   3404 C CZ  . TYR B 1 193 ? 10.719  -0.107  -24.435 1.00 30.06 ? 193 TYR B CZ  1 
ATOM   3405 O OH  . TYR B 1 193 ? 10.184  -1.356  -24.207 1.00 32.62 ? 193 TYR B OH  1 
ATOM   3406 N N   . VAL B 1 194 ? 14.933  5.777   -25.516 1.00 28.11 ? 194 VAL B N   1 
ATOM   3407 C CA  . VAL B 1 194 ? 15.350  7.011   -26.181 1.00 25.53 ? 194 VAL B CA  1 
ATOM   3408 C C   . VAL B 1 194 ? 14.912  6.907   -27.637 1.00 27.93 ? 194 VAL B C   1 
ATOM   3409 O O   . VAL B 1 194 ? 15.395  6.055   -28.393 1.00 26.79 ? 194 VAL B O   1 
ATOM   3410 C CB  . VAL B 1 194 ? 16.859  7.256   -26.059 1.00 32.73 ? 194 VAL B CB  1 
ATOM   3411 C CG1 . VAL B 1 194 ? 17.270  8.531   -26.829 1.00 28.97 ? 194 VAL B CG1 1 
ATOM   3412 C CG2 . VAL B 1 194 ? 17.267  7.368   -24.589 1.00 32.13 ? 194 VAL B CG2 1 
ATOM   3413 N N   . VAL B 1 195 ? 13.966  7.749   -28.031 1.00 26.73 ? 195 VAL B N   1 
ATOM   3414 C CA  . VAL B 1 195 ? 13.301  7.623   -29.320 1.00 25.87 ? 195 VAL B CA  1 
ATOM   3415 C C   . VAL B 1 195 ? 13.694  8.814   -30.188 1.00 29.31 ? 195 VAL B C   1 
ATOM   3416 O O   . VAL B 1 195 ? 13.457  9.977   -29.820 1.00 26.70 ? 195 VAL B O   1 
ATOM   3417 C CB  . VAL B 1 195 ? 11.774  7.551   -29.166 1.00 28.40 ? 195 VAL B CB  1 
ATOM   3418 C CG1 . VAL B 1 195 ? 11.103  7.621   -30.528 1.00 27.93 ? 195 VAL B CG1 1 
ATOM   3419 C CG2 . VAL B 1 195 ? 11.332  6.293   -28.383 1.00 26.45 ? 195 VAL B CG2 1 
ATOM   3420 N N   . ALA B 1 196 ? 14.255  8.518   -31.354 1.00 25.18 ? 196 ALA B N   1 
ATOM   3421 C CA  . ALA B 1 196 ? 14.349  9.490   -32.431 1.00 27.73 ? 196 ALA B CA  1 
ATOM   3422 C C   . ALA B 1 196 ? 12.986  9.557   -33.104 1.00 28.04 ? 196 ALA B C   1 
ATOM   3423 O O   . ALA B 1 196 ? 12.580  8.620   -33.799 1.00 29.17 ? 196 ALA B O   1 
ATOM   3424 C CB  . ALA B 1 196 ? 15.442  9.094   -33.427 1.00 25.14 ? 196 ALA B CB  1 
ATOM   3425 N N   . ASP B 1 197 ? 12.261  10.652  -32.876 1.00 25.25 ? 197 ASP B N   1 
ATOM   3426 C CA  . ASP B 1 197 ? 10.920  10.812  -33.405 1.00 25.87 ? 197 ASP B CA  1 
ATOM   3427 C C   . ASP B 1 197 ? 10.964  11.732  -34.614 1.00 25.72 ? 197 ASP B C   1 
ATOM   3428 O O   . ASP B 1 197 ? 11.242  12.928  -34.446 1.00 26.63 ? 197 ASP B O   1 
ATOM   3429 C CB  . ASP B 1 197 ? 9.986   11.391  -32.327 1.00 23.66 ? 197 ASP B CB  1 
ATOM   3430 C CG  . ASP B 1 197 ? 8.601   11.675  -32.839 1.00 24.37 ? 197 ASP B CG  1 
ATOM   3431 O OD1 . ASP B 1 197 ? 8.408   11.791  -34.062 1.00 23.74 ? 197 ASP B OD1 1 
ATOM   3432 O OD2 . ASP B 1 197 ? 7.668   11.800  -32.003 1.00 28.69 ? 197 ASP B OD2 1 
ATOM   3433 N N   . PRO B 1 198 ? 10.602  11.258  -35.813 1.00 26.55 ? 198 PRO B N   1 
ATOM   3434 C CA  . PRO B 1 198 ? 10.760  12.087  -37.030 1.00 27.04 ? 198 PRO B CA  1 
ATOM   3435 C C   . PRO B 1 198 ? 9.888   13.344  -37.095 1.00 28.09 ? 198 PRO B C   1 
ATOM   3436 O O   . PRO B 1 198 ? 10.097  14.155  -38.014 1.00 25.05 ? 198 PRO B O   1 
ATOM   3437 C CB  . PRO B 1 198 ? 10.429  11.108  -38.175 1.00 29.42 ? 198 PRO B CB  1 
ATOM   3438 C CG  . PRO B 1 198 ? 9.697   9.914   -37.516 1.00 28.85 ? 198 PRO B CG  1 
ATOM   3439 C CD  . PRO B 1 198 ? 10.235  9.853   -36.103 1.00 26.49 ? 198 PRO B CD  1 
ATOM   3440 N N   . ALA B 1 199 ? 8.943   13.531  -36.173 1.00 26.55 ? 199 ALA B N   1 
ATOM   3441 C CA  . ALA B 1 199 ? 8.112   14.727  -36.095 1.00 25.79 ? 199 ALA B CA  1 
ATOM   3442 C C   . ALA B 1 199 ? 8.419   15.585  -34.876 1.00 25.59 ? 199 ALA B C   1 
ATOM   3443 O O   . ALA B 1 199 ? 7.716   16.580  -34.653 1.00 28.15 ? 199 ALA B O   1 
ATOM   3444 C CB  . ALA B 1 199 ? 6.611   14.343  -36.070 1.00 27.26 ? 199 ALA B CB  1 
ATOM   3445 N N   . LYS B 1 200 ? 9.422   15.229  -34.062 1.00 26.29 ? 200 LYS B N   1 
ATOM   3446 C CA  . LYS B 1 200 ? 9.630   15.942  -32.800 1.00 27.24 ? 200 LYS B CA  1 
ATOM   3447 C C   . LYS B 1 200 ? 11.100  16.211  -32.472 1.00 28.03 ? 200 LYS B C   1 
ATOM   3448 O O   . LYS B 1 200 ? 11.450  17.330  -32.073 1.00 26.77 ? 200 LYS B O   1 
ATOM   3449 C CB  . LYS B 1 200 ? 8.979   15.177  -31.635 1.00 29.07 ? 200 LYS B CB  1 
ATOM   3450 C CG  . LYS B 1 200 ? 7.436   15.419  -31.454 1.00 28.40 ? 200 LYS B CG  1 
ATOM   3451 C CD  . LYS B 1 200 ? 7.110   16.892  -31.213 1.00 26.62 ? 200 LYS B CD  1 
ATOM   3452 C CE  . LYS B 1 200 ? 7.747   17.346  -29.923 1.00 32.79 ? 200 LYS B CE  1 
ATOM   3453 N NZ  . LYS B 1 200 ? 7.214   18.634  -29.447 1.00 29.55 ? 200 LYS B NZ  1 
ATOM   3454 N N   . GLY B 1 201 ? 11.953  15.197  -32.571 1.00 23.58 ? 201 GLY B N   1 
ATOM   3455 C CA  . GLY B 1 201 ? 13.336  15.346  -32.166 1.00 23.57 ? 201 GLY B CA  1 
ATOM   3456 C C   . GLY B 1 201 ? 14.000  14.000  -31.986 1.00 26.99 ? 201 GLY B C   1 
ATOM   3457 O O   . GLY B 1 201 ? 13.347  12.952  -31.912 1.00 29.96 ? 201 GLY B O   1 
ATOM   3458 N N   . VAL B 1 202 ? 15.330  14.047  -31.867 1.00 26.48 ? 202 VAL B N   1 
ATOM   3459 C CA  . VAL B 1 202 ? 16.147  12.826  -31.870 1.00 27.03 ? 202 VAL B CA  1 
ATOM   3460 C C   . VAL B 1 202 ? 16.169  12.143  -30.517 1.00 29.63 ? 202 VAL B C   1 
ATOM   3461 O O   . VAL B 1 202 ? 16.581  10.980  -30.420 1.00 29.76 ? 202 VAL B O   1 
ATOM   3462 C CB  . VAL B 1 202 ? 17.577  13.170  -32.346 1.00 25.93 ? 202 VAL B CB  1 
ATOM   3463 C CG1 . VAL B 1 202 ? 18.369  13.922  -31.274 1.00 27.37 ? 202 VAL B CG1 1 
ATOM   3464 C CG2 . VAL B 1 202 ? 18.351  11.921  -32.767 1.00 25.92 ? 202 VAL B CG2 1 
ATOM   3465 N N   . ASN B 1 203 ? 15.655  12.804  -29.483 1.00 31.41 ? 203 ASN B N   1 
ATOM   3466 C CA  . ASN B 1 203 ? 15.945  12.469  -28.093 1.00 33.89 ? 203 ASN B CA  1 
ATOM   3467 C C   . ASN B 1 203 ? 14.685  12.355  -27.226 1.00 34.34 ? 203 ASN B C   1 
ATOM   3468 O O   . ASN B 1 203 ? 14.738  12.642  -26.032 1.00 37.93 ? 203 ASN B O   1 
ATOM   3469 C CB  . ASN B 1 203 ? 16.865  13.545  -27.502 1.00 38.23 ? 203 ASN B CB  1 
ATOM   3470 C CG  . ASN B 1 203 ? 17.630  13.053  -26.332 1.00 45.37 ? 203 ASN B CG  1 
ATOM   3471 O OD1 . ASN B 1 203 ? 17.886  11.857  -26.216 1.00 47.06 ? 203 ASN B OD1 1 
ATOM   3472 N ND2 . ASN B 1 203 ? 18.014  13.968  -25.442 1.00 45.30 ? 203 ASN B ND2 1 
ATOM   3473 N N   . ARG B 1 204 ? 13.564  11.896  -27.769 1.00 31.13 ? 204 ARG B N   1 
ATOM   3474 C CA  . ARG B 1 204 ? 12.315  11.860  -27.003 1.00 29.04 ? 204 ARG B CA  1 
ATOM   3475 C C   . ARG B 1 204 ? 12.339  10.656  -26.054 1.00 31.65 ? 204 ARG B C   1 
ATOM   3476 O O   . ARG B 1 204 ? 12.461  9.519   -26.502 1.00 31.82 ? 204 ARG B O   1 
ATOM   3477 C CB  . ARG B 1 204 ? 11.121  11.780  -27.956 1.00 25.58 ? 204 ARG B CB  1 
ATOM   3478 C CG  . ARG B 1 204 ? 11.078  12.835  -29.057 1.00 29.64 ? 204 ARG B CG  1 
ATOM   3479 C CD  . ARG B 1 204 ? 11.521  14.237  -28.527 1.00 32.08 ? 204 ARG B CD  1 
ATOM   3480 N NE  . ARG B 1 204 ? 10.573  14.728  -27.524 1.00 32.38 ? 204 ARG B NE  1 
ATOM   3481 C CZ  . ARG B 1 204 ? 10.431  15.998  -27.168 1.00 37.64 ? 204 ARG B CZ  1 
ATOM   3482 N NH1 . ARG B 1 204 ? 11.194  16.952  -27.688 1.00 41.41 ? 204 ARG B NH1 1 
ATOM   3483 N NH2 . ARG B 1 204 ? 9.516   16.318  -26.256 1.00 37.09 ? 204 ARG B NH2 1 
ATOM   3484 N N   . LYS B 1 205 ? 12.217  10.890  -24.750 1.00 29.80 ? 205 LYS B N   1 
ATOM   3485 C CA  . LYS B 1 205 ? 12.415  9.843   -23.751 1.00 31.02 ? 205 LYS B CA  1 
ATOM   3486 C C   . LYS B 1 205 ? 11.074  9.294   -23.265 1.00 30.73 ? 205 LYS B C   1 
ATOM   3487 O O   . LYS B 1 205 ? 10.278  10.019  -22.659 1.00 33.00 ? 205 LYS B O   1 
ATOM   3488 C CB  . LYS B 1 205 ? 13.244  10.383  -22.585 1.00 33.87 ? 205 LYS B CB  1 
ATOM   3489 C CG  . LYS B 1 205 ? 14.746  10.275  -22.845 1.00 38.51 ? 205 LYS B CG  1 
ATOM   3490 C CD  . LYS B 1 205 ? 15.577  11.018  -21.828 1.00 42.02 ? 205 LYS B CD  1 
ATOM   3491 C CE  . LYS B 1 205 ? 16.987  11.220  -22.375 1.00 45.60 ? 205 LYS B CE  1 
ATOM   3492 N NZ  . LYS B 1 205 ? 17.859  11.853  -21.354 1.00 52.32 ? 205 LYS B NZ  1 
ATOM   3493 N N   . TYR B 1 206 ? 10.833  8.015   -23.511 1.00 32.16 ? 206 TYR B N   1 
ATOM   3494 C CA  . TYR B 1 206 ? 9.571   7.375   -23.170 1.00 32.68 ? 206 TYR B CA  1 
ATOM   3495 C C   . TYR B 1 206 ? 9.791   6.326   -22.097 1.00 33.81 ? 206 TYR B C   1 
ATOM   3496 O O   . TYR B 1 206 ? 10.585  5.398   -22.290 1.00 31.91 ? 206 TYR B O   1 
ATOM   3497 C CB  . TYR B 1 206 ? 8.971   6.692   -24.403 1.00 31.53 ? 206 TYR B CB  1 
ATOM   3498 C CG  . TYR B 1 206 ? 8.220   7.622   -25.307 1.00 31.39 ? 206 TYR B CG  1 
ATOM   3499 C CD1 . TYR B 1 206 ? 8.900   8.540   -26.113 1.00 28.73 ? 206 TYR B CD1 1 
ATOM   3500 C CD2 . TYR B 1 206 ? 6.838   7.577   -25.370 1.00 28.43 ? 206 TYR B CD2 1 
ATOM   3501 C CE1 . TYR B 1 206 ? 8.220   9.392   -26.948 1.00 28.98 ? 206 TYR B CE1 1 
ATOM   3502 C CE2 . TYR B 1 206 ? 6.143   8.420   -26.196 1.00 29.65 ? 206 TYR B CE2 1 
ATOM   3503 C CZ  . TYR B 1 206 ? 6.829   9.338   -26.976 1.00 29.11 ? 206 TYR B CZ  1 
ATOM   3504 O OH  . TYR B 1 206 ? 6.108   10.189  -27.784 1.00 27.10 ? 206 TYR B OH  1 
ATOM   3505 N N   . LYS B 1 207 ? 9.042   6.443   -20.999 1.00 34.83 ? 207 LYS B N   1 
ATOM   3506 C CA  . LYS B 1 207 ? 9.026   5.402   -19.978 1.00 34.88 ? 207 LYS B CA  1 
ATOM   3507 C C   . LYS B 1 207 ? 8.590   4.100   -20.630 1.00 31.69 ? 207 LYS B C   1 
ATOM   3508 O O   . LYS B 1 207 ? 7.697   4.101   -21.478 1.00 29.48 ? 207 LYS B O   1 
ATOM   3509 C CB  . LYS B 1 207 ? 8.034   5.747   -18.863 1.00 36.69 ? 207 LYS B CB  1 
ATOM   3510 C CG  . LYS B 1 207 ? 8.403   6.859   -17.922 1.00 41.72 ? 207 LYS B CG  1 
ATOM   3511 C CD  . LYS B 1 207 ? 7.856   6.545   -16.515 1.00 46.00 ? 207 LYS B CD  1 
ATOM   3512 C CE  . LYS B 1 207 ? 7.571   7.834   -15.737 1.00 47.09 ? 207 LYS B CE  1 
ATOM   3513 N NZ  . LYS B 1 207 ? 8.220   7.908   -14.371 1.00 53.05 ? 207 LYS B NZ  1 
ATOM   3514 N N   . PHE B 1 208 ? 9.290   3.005   -20.317 1.00 33.67 ? 208 PHE B N   1 
ATOM   3515 C CA  . PHE B 1 208 ? 9.023   1.728   -20.984 1.00 33.02 ? 208 PHE B CA  1 
ATOM   3516 C C   . PHE B 1 208 ? 7.522   1.446   -21.091 1.00 33.45 ? 208 PHE B C   1 
ATOM   3517 O O   . PHE B 1 208 ? 6.997   1.215   -22.186 1.00 34.02 ? 208 PHE B O   1 
ATOM   3518 C CB  . PHE B 1 208 ? 9.698   0.586   -20.214 1.00 31.91 ? 208 PHE B CB  1 
ATOM   3519 C CG  . PHE B 1 208 ? 11.193  0.680   -20.144 1.00 32.68 ? 208 PHE B CG  1 
ATOM   3520 C CD1 . PHE B 1 208 ? 11.923  1.336   -21.129 1.00 34.40 ? 208 PHE B CD1 1 
ATOM   3521 C CD2 . PHE B 1 208 ? 11.866  0.159   -19.054 1.00 32.46 ? 208 PHE B CD2 1 
ATOM   3522 C CE1 . PHE B 1 208 ? 13.305  1.437   -21.050 1.00 30.96 ? 208 PHE B CE1 1 
ATOM   3523 C CE2 . PHE B 1 208 ? 13.248  0.252   -18.966 1.00 36.40 ? 208 PHE B CE2 1 
ATOM   3524 C CZ  . PHE B 1 208 ? 13.970  0.900   -19.965 1.00 34.40 ? 208 PHE B CZ  1 
ATOM   3525 N N   . SER B 1 209 ? 6.806   1.460   -19.956 1.00 31.36 ? 209 SER B N   1 
ATOM   3526 C CA  . SER B 1 209 ? 5.383   1.112   -20.003 1.00 34.83 ? 209 SER B CA  1 
ATOM   3527 C C   . SER B 1 209 ? 4.583   2.126   -20.806 1.00 30.96 ? 209 SER B C   1 
ATOM   3528 O O   . SER B 1 209 ? 3.566   1.770   -21.407 1.00 32.19 ? 209 SER B O   1 
ATOM   3529 C CB  . SER B 1 209 ? 4.802   0.960   -18.589 1.00 37.27 ? 209 SER B CB  1 
ATOM   3530 O OG  . SER B 1 209 ? 4.965   2.147   -17.818 1.00 42.05 ? 209 SER B OG  1 
ATOM   3531 N N   . CYS B 1 210 ? 5.026   3.384   -20.835 1.00 32.45 ? 210 CYS B N   1 
ATOM   3532 C CA  . CYS B 1 210 ? 4.324   4.400   -21.613 1.00 31.86 ? 210 CYS B CA  1 
ATOM   3533 C C   . CYS B 1 210 ? 4.308   4.047   -23.096 1.00 31.30 ? 210 CYS B C   1 
ATOM   3534 O O   . CYS B 1 210 ? 3.250   4.054   -23.735 1.00 31.73 ? 210 CYS B O   1 
ATOM   3535 C CB  . CYS B 1 210 ? 4.956   5.772   -21.392 1.00 32.96 ? 210 CYS B CB  1 
ATOM   3536 S SG  . CYS B 1 210 ? 4.126   7.050   -22.356 1.00 34.88 ? 210 CYS B SG  1 
ATOM   3537 N N   . LEU B 1 211 ? 5.477   3.754   -23.671 1.00 29.89 ? 211 LEU B N   1 
ATOM   3538 C CA  . LEU B 1 211 ? 5.526   3.345   -25.072 1.00 28.08 ? 211 LEU B CA  1 
ATOM   3539 C C   . LEU B 1 211 ? 4.985   1.931   -25.276 1.00 25.95 ? 211 LEU B C   1 
ATOM   3540 O O   . LEU B 1 211 ? 4.260   1.679   -26.242 1.00 25.98 ? 211 LEU B O   1 
ATOM   3541 C CB  . LEU B 1 211 ? 6.959   3.436   -25.588 1.00 29.14 ? 211 LEU B CB  1 
ATOM   3542 C CG  . LEU B 1 211 ? 7.114   3.320   -27.101 1.00 31.32 ? 211 LEU B CG  1 
ATOM   3543 C CD1 . LEU B 1 211 ? 6.246   4.384   -27.763 1.00 26.79 ? 211 LEU B CD1 1 
ATOM   3544 C CD2 . LEU B 1 211 ? 8.582   3.474   -27.482 1.00 27.60 ? 211 LEU B CD2 1 
ATOM   3545 N N   . ASP B 1 212 ? 5.376   0.974   -24.423 1.00 29.72 ? 212 ASP B N   1 
ATOM   3546 C CA  . ASP B 1 212 ? 4.911   -0.408  -24.614 1.00 29.62 ? 212 ASP B CA  1 
ATOM   3547 C C   . ASP B 1 212 ? 3.390   -0.464  -24.724 1.00 30.06 ? 212 ASP B C   1 
ATOM   3548 O O   . ASP B 1 212 ? 2.832   -1.195  -25.556 1.00 31.75 ? 212 ASP B O   1 
ATOM   3549 C CB  . ASP B 1 212 ? 5.328   -1.304  -23.446 1.00 28.19 ? 212 ASP B CB  1 
ATOM   3550 C CG  . ASP B 1 212 ? 6.814   -1.495  -23.331 1.00 33.37 ? 212 ASP B CG  1 
ATOM   3551 O OD1 . ASP B 1 212 ? 7.589   -1.237  -24.297 1.00 29.68 ? 212 ASP B OD1 1 
ATOM   3552 O OD2 . ASP B 1 212 ? 7.210   -1.910  -22.230 1.00 34.26 ? 212 ASP B OD2 1 
ATOM   3553 N N   . ASN B 1 213 ? 2.700   0.293   -23.888 1.00 30.46 ? 213 ASN B N   1 
ATOM   3554 C CA  . ASN B 1 213 ? 1.255   0.160   -23.801 1.00 31.27 ? 213 ASN B CA  1 
ATOM   3555 C C   . ASN B 1 213 ? 0.505   1.143   -24.696 1.00 34.14 ? 213 ASN B C   1 
ATOM   3556 O O   . ASN B 1 213 ? -0.724  1.242   -24.591 1.00 33.70 ? 213 ASN B O   1 
ATOM   3557 C CB  . ASN B 1 213 ? 0.810   0.327   -22.348 1.00 33.32 ? 213 ASN B CB  1 
ATOM   3558 C CG  . ASN B 1 213 ? 1.174   -0.856  -21.507 1.00 36.97 ? 213 ASN B CG  1 
ATOM   3559 O OD1 . ASN B 1 213 ? 1.884   -0.747  -20.514 1.00 39.96 ? 213 ASN B OD1 1 
ATOM   3560 N ND2 . ASN B 1 213 ? 0.716   -2.016  -21.926 1.00 43.46 ? 213 ASN B ND2 1 
ATOM   3561 N N   . ALA B 1 214 ? 1.218   1.893   -25.527 1.00 30.42 ? 214 ALA B N   1 
ATOM   3562 C CA  . ALA B 1 214 ? 0.538   2.953   -26.304 1.00 32.71 ? 214 ALA B CA  1 
ATOM   3563 C C   . ALA B 1 214 ? 0.078   2.468   -27.672 1.00 29.16 ? 214 ALA B C   1 
ATOM   3564 O O   . ALA B 1 214 ? -0.099  3.302   -28.526 1.00 32.25 ? 214 ALA B O   1 
ATOM   3565 C CB  . ALA B 1 214 ? 1.396   4.181   -26.411 1.00 27.77 ? 214 ALA B CB  1 
ATOM   3566 N N   . ASN B 1 215 ? -0.147  1.175   -27.833 1.00 27.12 ? 215 ASN B N   1 
ATOM   3567 C CA  . ASN B 1 215 ? -0.597  0.672   -29.151 1.00 31.16 ? 215 ASN B CA  1 
ATOM   3568 C C   . ASN B 1 215 ? -1.803  -0.243  -28.944 1.00 32.30 ? 215 ASN B C   1 
ATOM   3569 O O   . ASN B 1 215 ? -1.983  -1.153  -29.723 1.00 31.26 ? 215 ASN B O   1 
ATOM   3570 C CB  . ASN B 1 215 ? 0.552   0.025   -29.918 1.00 27.29 ? 215 ASN B CB  1 
ATOM   3571 C CG  . ASN B 1 215 ? 0.499   0.299   -31.401 1.00 28.83 ? 215 ASN B CG  1 
ATOM   3572 O OD1 . ASN B 1 215 ? -0.001  1.324   -31.817 1.00 27.11 ? 215 ASN B OD1 1 
ATOM   3573 N ND2 . ASN B 1 215 ? 1.013   -0.617  -32.191 1.00 24.73 ? 215 ASN B ND2 1 
ATOM   3574 N N   . LYS B 1 216 ? -2.588  0.036   -27.907 1.00 39.57 ? 216 LYS B N   1 
ATOM   3575 C CA  . LYS B 1 216 ? -3.771  -0.789  -27.588 1.00 38.35 ? 216 LYS B CA  1 
ATOM   3576 C C   . LYS B 1 216 ? -4.654  -0.868  -28.820 1.00 30.08 ? 216 LYS B C   1 
ATOM   3577 O O   . LYS B 1 216 ? -4.963  0.137   -29.399 1.00 30.42 ? 216 LYS B O   1 
ATOM   3578 C CB  . LYS B 1 216 ? -4.542  -0.255  -26.386 1.00 39.81 ? 216 LYS B CB  1 
ATOM   3579 C CG  . LYS B 1 216 ? -5.982  -0.736  -26.316 1.00 47.18 ? 216 LYS B CG  1 
ATOM   3580 C CD  . LYS B 1 216 ? -6.203  -1.820  -25.280 1.00 54.91 ? 216 LYS B CD  1 
ATOM   3581 C CE  . LYS B 1 216 ? -7.503  -2.576  -25.463 1.00 56.76 ? 216 LYS B CE  1 
ATOM   3582 N NZ  . LYS B 1 216 ? -7.301  -4.047  -25.450 1.00 55.17 ? 216 LYS B NZ  1 
ATOM   3583 N N   . GLY B 1 217 ? -4.981  -2.082  -29.211 1.00 37.79 ? 217 GLY B N   1 
ATOM   3584 C CA  . GLY B 1 217 ? -5.825  -2.278  -30.384 1.00 27.53 ? 217 GLY B CA  1 
ATOM   3585 C C   . GLY B 1 217 ? -5.020  -2.440  -31.654 1.00 37.96 ? 217 GLY B C   1 
ATOM   3586 O O   . GLY B 1 217 ? -5.655  -2.634  -32.656 1.00 32.68 ? 217 GLY B O   1 
ATOM   3587 N N   . TYR B 1 218 ? -3.682  -2.309  -31.621 1.00 32.68 ? 218 TYR B N   1 
ATOM   3588 C CA  . TYR B 1 218 ? -2.975  -2.437  -32.883 1.00 32.17 ? 218 TYR B CA  1 
ATOM   3589 C C   . TYR B 1 218 ? -1.891  -3.459  -32.633 1.00 28.09 ? 218 TYR B C   1 
ATOM   3590 O O   . TYR B 1 218 ? -1.814  -4.027  -31.535 1.00 29.01 ? 218 TYR B O   1 
ATOM   3591 C CB  . TYR B 1 218 ? -2.447  -1.073  -33.362 1.00 28.01 ? 218 TYR B CB  1 
ATOM   3592 C CG  . TYR B 1 218 ? -3.544  -0.093  -33.648 1.00 31.46 ? 218 TYR B CG  1 
ATOM   3593 C CD1 . TYR B 1 218 ? -4.140  0.656   -32.645 1.00 35.12 ? 218 TYR B CD1 1 
ATOM   3594 C CD2 . TYR B 1 218 ? -3.972  0.098   -34.953 1.00 30.66 ? 218 TYR B CD2 1 
ATOM   3595 C CE1 . TYR B 1 218 ? -5.150  1.556   -32.937 1.00 34.23 ? 218 TYR B CE1 1 
ATOM   3596 C CE2 . TYR B 1 218 ? -4.965  0.990   -35.256 1.00 33.80 ? 218 TYR B CE2 1 
ATOM   3597 C CZ  . TYR B 1 218 ? -5.548  1.719   -34.248 1.00 38.28 ? 218 TYR B CZ  1 
ATOM   3598 O OH  . TYR B 1 218 ? -6.550  2.612   -34.551 1.00 44.21 ? 218 TYR B OH  1 
ATOM   3599 N N   . ARG B 1 219 ? -1.082  -3.730  -33.647 1.00 29.89 ? 219 ARG B N   1 
ATOM   3600 C CA  . ARG B 1 219 ? -0.132  -4.840  -33.556 1.00 28.76 ? 219 ARG B CA  1 
ATOM   3601 C C   . ARG B 1 219 ? 0.823   -4.667  -32.377 1.00 29.76 ? 219 ARG B C   1 
ATOM   3602 O O   . ARG B 1 219 ? 1.471   -3.620  -32.212 1.00 31.49 ? 219 ARG B O   1 
ATOM   3603 C CB  . ARG B 1 219 ? 0.650   -4.965  -34.861 1.00 30.29 ? 219 ARG B CB  1 
ATOM   3604 C CG  . ARG B 1 219 ? 1.521   -6.210  -34.944 1.00 29.11 ? 219 ARG B CG  1 
ATOM   3605 C CD  . ARG B 1 219 ? 2.126   -6.336  -36.324 1.00 29.04 ? 219 ARG B CD  1 
ATOM   3606 N NE  . ARG B 1 219 ? 3.117   -7.401  -36.371 1.00 31.69 ? 219 ARG B NE  1 
ATOM   3607 C CZ  . ARG B 1 219 ? 3.520   -7.985  -37.491 1.00 32.12 ? 219 ARG B CZ  1 
ATOM   3608 N NH1 . ARG B 1 219 ? 3.034   -7.626  -38.668 1.00 32.73 ? 219 ARG B NH1 1 
ATOM   3609 N NH2 . ARG B 1 219 ? 4.475   -8.905  -37.432 1.00 30.62 ? 219 ARG B NH2 1 
ATOM   3610 N N   . GLN B 1 220 ? 0.949   -5.715  -31.578 1.00 24.77 ? 220 GLN B N   1 
ATOM   3611 C CA  . GLN B 1 220 ? 1.756   -5.654  -30.357 1.00 26.19 ? 220 GLN B CA  1 
ATOM   3612 C C   . GLN B 1 220 ? 3.208   -6.068  -30.626 1.00 30.72 ? 220 GLN B C   1 
ATOM   3613 O O   . GLN B 1 220 ? 3.723   -7.038  -30.058 1.00 28.84 ? 220 GLN B O   1 
ATOM   3614 C CB  . GLN B 1 220 ? 1.130   -6.528  -29.268 1.00 28.55 ? 220 GLN B CB  1 
ATOM   3615 C CG  . GLN B 1 220 ? -0.214  -6.030  -28.710 1.00 27.21 ? 220 GLN B CG  1 
ATOM   3616 C CD  . GLN B 1 220 ? -0.126  -4.621  -28.183 1.00 29.20 ? 220 GLN B CD  1 
ATOM   3617 O OE1 . GLN B 1 220 ? -0.688  -3.697  -28.768 1.00 31.15 ? 220 GLN B OE1 1 
ATOM   3618 N NE2 . GLN B 1 220 ? 0.609   -4.435  -27.096 1.00 29.06 ? 220 GLN B NE2 1 
ATOM   3619 N N   . ASN B 1 221 ? 3.902   -5.270  -31.454 1.00 29.06 ? 221 ASN B N   1 
ATOM   3620 C CA  . ASN B 1 221 ? 5.313   -5.510  -31.719 1.00 28.05 ? 221 ASN B CA  1 
ATOM   3621 C C   . ASN B 1 221 ? 6.095   -4.194  -31.776 1.00 30.01 ? 221 ASN B C   1 
ATOM   3622 O O   . ASN B 1 221 ? 5.526   -3.102  -31.956 1.00 25.30 ? 221 ASN B O   1 
ATOM   3623 C CB  . ASN B 1 221 ? 5.544   -6.262  -33.047 1.00 28.51 ? 221 ASN B CB  1 
ATOM   3624 C CG  . ASN B 1 221 ? 5.049   -7.723  -33.020 1.00 30.15 ? 221 ASN B CG  1 
ATOM   3625 O OD1 . ASN B 1 221 ? 4.109   -8.067  -33.726 1.00 31.96 ? 221 ASN B OD1 1 
ATOM   3626 N ND2 . ASN B 1 221 ? 5.680   -8.566  -32.213 1.00 28.20 ? 221 ASN B ND2 1 
ATOM   3627 N N   . TYR B 1 222 ? 7.412   -4.318  -31.552 1.00 28.44 ? 222 TYR B N   1 
ATOM   3628 C CA  . TYR B 1 222 ? 8.451   -3.423  -32.060 1.00 25.87 ? 222 TYR B CA  1 
ATOM   3629 C C   . TYR B 1 222 ? 9.189   -4.161  -33.169 1.00 30.29 ? 222 TYR B C   1 
ATOM   3630 O O   . TYR B 1 222 ? 9.024   -5.377  -33.344 1.00 28.24 ? 222 TYR B O   1 
ATOM   3631 C CB  . TYR B 1 222 ? 9.435   -2.997  -30.963 1.00 26.48 ? 222 TYR B CB  1 
ATOM   3632 C CG  . TYR B 1 222 ? 8.837   -2.164  -29.846 1.00 26.84 ? 222 TYR B CG  1 
ATOM   3633 C CD1 . TYR B 1 222 ? 7.805   -1.267  -30.082 1.00 26.62 ? 222 TYR B CD1 1 
ATOM   3634 C CD2 . TYR B 1 222 ? 9.296   -2.302  -28.547 1.00 28.69 ? 222 TYR B CD2 1 
ATOM   3635 C CE1 . TYR B 1 222 ? 7.256   -0.524  -29.038 1.00 28.41 ? 222 TYR B CE1 1 
ATOM   3636 C CE2 . TYR B 1 222 ? 8.765   -1.576  -27.517 1.00 28.51 ? 222 TYR B CE2 1 
ATOM   3637 C CZ  . TYR B 1 222 ? 7.753   -0.686  -27.753 1.00 31.22 ? 222 TYR B CZ  1 
ATOM   3638 O OH  . TYR B 1 222 ? 7.224   0.022   -26.675 1.00 27.85 ? 222 TYR B OH  1 
ATOM   3639 N N   . TYR B 1 223 ? 10.012  -3.428  -33.925 1.00 25.69 ? 223 TYR B N   1 
ATOM   3640 C CA  . TYR B 1 223 ? 10.580  -3.944  -35.172 1.00 27.60 ? 223 TYR B CA  1 
ATOM   3641 C C   . TYR B 1 223 ? 12.075  -3.663  -35.235 1.00 29.67 ? 223 TYR B C   1 
ATOM   3642 O O   . TYR B 1 223 ? 12.497  -2.545  -35.536 1.00 26.05 ? 223 TYR B O   1 
ATOM   3643 C CB  . TYR B 1 223 ? 9.831   -3.354  -36.372 1.00 25.54 ? 223 TYR B CB  1 
ATOM   3644 C CG  . TYR B 1 223 ? 8.343   -3.504  -36.179 1.00 27.50 ? 223 TYR B CG  1 
ATOM   3645 C CD1 . TYR B 1 223 ? 7.726   -4.734  -36.420 1.00 27.25 ? 223 TYR B CD1 1 
ATOM   3646 C CD2 . TYR B 1 223 ? 7.552   -2.448  -35.711 1.00 26.26 ? 223 TYR B CD2 1 
ATOM   3647 C CE1 . TYR B 1 223 ? 6.380   -4.915  -36.222 1.00 28.14 ? 223 TYR B CE1 1 
ATOM   3648 C CE2 . TYR B 1 223 ? 6.210   -2.623  -35.503 1.00 25.74 ? 223 TYR B CE2 1 
ATOM   3649 C CZ  . TYR B 1 223 ? 5.623   -3.871  -35.764 1.00 28.77 ? 223 TYR B CZ  1 
ATOM   3650 O OH  . TYR B 1 223 ? 4.278   -4.095  -35.574 1.00 27.27 ? 223 TYR B OH  1 
ATOM   3651 N N   . VAL B 1 224 ? 12.901  -4.660  -34.941 1.00 29.28 ? 224 VAL B N   1 
ATOM   3652 C CA  . VAL B 1 224 ? 14.334  -4.408  -35.016 1.00 25.87 ? 224 VAL B CA  1 
ATOM   3653 C C   . VAL B 1 224 ? 14.791  -4.424  -36.467 1.00 27.83 ? 224 VAL B C   1 
ATOM   3654 O O   . VAL B 1 224 ? 14.277  -5.173  -37.305 1.00 26.83 ? 224 VAL B O   1 
ATOM   3655 C CB  . VAL B 1 224 ? 15.134  -5.366  -34.112 1.00 31.48 ? 224 VAL B CB  1 
ATOM   3656 C CG1 . VAL B 1 224 ? 14.220  -6.284  -33.360 1.00 28.57 ? 224 VAL B CG1 1 
ATOM   3657 C CG2 . VAL B 1 224 ? 16.237  -6.081  -34.894 1.00 31.01 ? 224 VAL B CG2 1 
ATOM   3658 N N   . VAL B 1 225 ? 15.706  -3.512  -36.792 1.00 29.40 ? 225 VAL B N   1 
ATOM   3659 C CA  . VAL B 1 225 ? 16.234  -3.387  -38.141 1.00 27.49 ? 225 VAL B CA  1 
ATOM   3660 C C   . VAL B 1 225 ? 17.608  -4.037  -38.151 1.00 28.95 ? 225 VAL B C   1 
ATOM   3661 O O   . VAL B 1 225 ? 18.470  -3.700  -37.327 1.00 30.41 ? 225 VAL B O   1 
ATOM   3662 C CB  . VAL B 1 225 ? 16.279  -1.907  -38.573 1.00 26.76 ? 225 VAL B CB  1 
ATOM   3663 C CG1 . VAL B 1 225 ? 16.622  -1.779  -40.041 1.00 23.46 ? 225 VAL B CG1 1 
ATOM   3664 C CG2 . VAL B 1 225 ? 14.902  -1.216  -38.261 1.00 25.39 ? 225 VAL B CG2 1 
ATOM   3665 N N   . CYS B 1 226 ? 17.810  -5.009  -39.034 1.00 27.75 ? 226 CYS B N   1 
ATOM   3666 C CA  . CYS B 1 226 ? 19.167  -5.548  -39.062 1.00 31.19 ? 226 CYS B CA  1 
ATOM   3667 C C   . CYS B 1 226 ? 19.613  -5.824  -40.494 1.00 31.50 ? 226 CYS B C   1 
ATOM   3668 O O   . CYS B 1 226 ? 18.788  -5.788  -41.425 1.00 29.15 ? 226 CYS B O   1 
ATOM   3669 C CB  . CYS B 1 226 ? 19.277  -6.822  -38.222 1.00 34.03 ? 226 CYS B CB  1 
ATOM   3670 S SG  . CYS B 1 226 ? 18.297  -8.150  -38.836 1.00 40.41 ? 226 CYS B SG  1 
ATOM   3671 N N   . PRO B 1 227 ? 20.907  -6.058  -40.722 1.00 28.94 ? 227 PRO B N   1 
ATOM   3672 C CA  . PRO B 1 227 ? 21.352  -6.378  -42.081 1.00 30.49 ? 227 PRO B CA  1 
ATOM   3673 C C   . PRO B 1 227 ? 20.762  -7.697  -42.540 1.00 32.86 ? 227 PRO B C   1 
ATOM   3674 O O   . PRO B 1 227 ? 20.704  -8.673  -41.790 1.00 34.73 ? 227 PRO B O   1 
ATOM   3675 C CB  . PRO B 1 227 ? 22.884  -6.444  -41.973 1.00 34.27 ? 227 PRO B CB  1 
ATOM   3676 C CG  . PRO B 1 227 ? 23.245  -6.000  -40.612 1.00 33.91 ? 227 PRO B CG  1 
ATOM   3677 C CD  . PRO B 1 227 ? 22.017  -5.753  -39.802 1.00 29.99 ? 227 PRO B CD  1 
ATOM   3678 N N   . ALA B 1 228 ? 20.331  -7.720  -43.788 1.00 29.90 ? 228 ALA B N   1 
ATOM   3679 C CA  . ALA B 1 228 ? 19.752  -8.912  -44.350 1.00 31.53 ? 228 ALA B CA  1 
ATOM   3680 C C   . ALA B 1 228 ? 20.875  -9.855  -44.764 1.00 42.33 ? 228 ALA B C   1 
ATOM   3681 O O   . ALA B 1 228 ? 21.797  -9.397  -45.449 1.00 42.65 ? 228 ALA B O   1 
ATOM   3682 C CB  . ALA B 1 228 ? 18.896  -8.555  -45.525 1.00 34.44 ? 228 ALA B CB  1 
ATOM   3683 O OXT . ALA B 1 228 ? 20.896  -11.057 -44.428 1.00 44.05 ? 228 ALA B OXT 1 
ATOM   3684 N N   . MET C 1 1   ? -11.022 14.467  7.703   1.00 54.00 ? 1   MET C N   1 
ATOM   3685 C CA  . MET C 1 1   ? -9.843  15.199  8.165   1.00 53.04 ? 1   MET C CA  1 
ATOM   3686 C C   . MET C 1 1   ? -9.774  16.616  7.571   1.00 49.53 ? 1   MET C C   1 
ATOM   3687 O O   . MET C 1 1   ? -10.580 16.995  6.707   1.00 49.42 ? 1   MET C O   1 
ATOM   3688 C CB  . MET C 1 1   ? -8.551  14.418  7.851   1.00 54.17 ? 1   MET C CB  1 
ATOM   3689 C CG  . MET C 1 1   ? -8.263  13.269  8.840   1.00 52.56 ? 1   MET C CG  1 
ATOM   3690 S SD  . MET C 1 1   ? -6.748  12.315  8.535   1.00 61.67 ? 1   MET C SD  1 
ATOM   3691 C CE  . MET C 1 1   ? -7.432  10.666  8.764   1.00 48.59 ? 1   MET C CE  1 
ATOM   3692 N N   . VAL C 1 2   ? -8.865  17.426  8.106   1.00 38.80 ? 2   VAL C N   1 
ATOM   3693 C CA  . VAL C 1 2   ? -8.796  18.846  7.786   1.00 39.28 ? 2   VAL C CA  1 
ATOM   3694 C C   . VAL C 1 2   ? -7.570  19.115  6.912   1.00 37.15 ? 2   VAL C C   1 
ATOM   3695 O O   . VAL C 1 2   ? -6.452  18.707  7.252   1.00 32.78 ? 2   VAL C O   1 
ATOM   3696 C CB  . VAL C 1 2   ? -8.786  19.685  9.070   1.00 38.10 ? 2   VAL C CB  1 
ATOM   3697 C CG1 . VAL C 1 2   ? -8.960  21.170  8.736   1.00 38.75 ? 2   VAL C CG1 1 
ATOM   3698 C CG2 . VAL C 1 2   ? -9.895  19.214  9.991   1.00 38.80 ? 2   VAL C CG2 1 
ATOM   3699 N N   . ARG C 1 3   ? -7.790  19.786  5.783   1.00 33.94 ? 3   ARG C N   1 
ATOM   3700 C CA  . ARG C 1 3   ? -6.745  20.117  4.828   1.00 31.53 ? 3   ARG C CA  1 
ATOM   3701 C C   . ARG C 1 3   ? -6.661  21.623  4.636   1.00 32.99 ? 3   ARG C C   1 
ATOM   3702 O O   . ARG C 1 3   ? -7.673  22.332  4.697   1.00 30.67 ? 3   ARG C O   1 
ATOM   3703 C CB  . ARG C 1 3   ? -6.995  19.426  3.476   1.00 32.62 ? 3   ARG C CB  1 
ATOM   3704 C CG  . ARG C 1 3   ? -7.908  18.209  3.580   1.00 37.58 ? 3   ARG C CG  1 
ATOM   3705 C CD  . ARG C 1 3   ? -8.056  17.473  2.257   1.00 36.92 ? 3   ARG C CD  1 
ATOM   3706 N NE  . ARG C 1 3   ? -8.858  18.224  1.297   1.00 40.44 ? 3   ARG C NE  1 
ATOM   3707 C CZ  . ARG C 1 3   ? -8.604  18.310  0.000   1.00 41.87 ? 3   ARG C CZ  1 
ATOM   3708 N NH1 . ARG C 1 3   ? -7.491  17.818  -0.518  1.00 44.05 ? 3   ARG C NH1 1 
ATOM   3709 N NH2 . ARG C 1 3   ? -9.489  18.909  -0.796  1.00 43.49 ? 3   ARG C NH2 1 
ATOM   3710 N N   . PHE C 1 4   ? -5.449  22.109  4.380   1.00 29.66 ? 4   PHE C N   1 
ATOM   3711 C CA  . PHE C 1 4   ? -5.220  23.533  4.184   1.00 27.46 ? 4   PHE C CA  1 
ATOM   3712 C C   . PHE C 1 4   ? -4.496  23.726  2.867   1.00 28.98 ? 4   PHE C C   1 
ATOM   3713 O O   . PHE C 1 4   ? -3.515  23.029  2.604   1.00 26.12 ? 4   PHE C O   1 
ATOM   3714 C CB  . PHE C 1 4   ? -4.422  24.091  5.346   1.00 27.69 ? 4   PHE C CB  1 
ATOM   3715 C CG  . PHE C 1 4   ? -5.142  24.005  6.666   1.00 30.20 ? 4   PHE C CG  1 
ATOM   3716 C CD1 . PHE C 1 4   ? -6.131  24.916  6.983   1.00 30.04 ? 4   PHE C CD1 1 
ATOM   3717 C CD2 . PHE C 1 4   ? -4.829  23.016  7.586   1.00 31.43 ? 4   PHE C CD2 1 
ATOM   3718 C CE1 . PHE C 1 4   ? -6.805  24.852  8.196   1.00 31.43 ? 4   PHE C CE1 1 
ATOM   3719 C CE2 . PHE C 1 4   ? -5.494  22.942  8.805   1.00 31.13 ? 4   PHE C CE2 1 
ATOM   3720 C CZ  . PHE C 1 4   ? -6.494  23.860  9.102   1.00 32.54 ? 4   PHE C CZ  1 
ATOM   3721 N N   . SER C 1 5   ? -4.985  24.647  2.035   1.00 27.17 ? 5   SER C N   1 
ATOM   3722 C CA  . SER C 1 5   ? -4.436  24.818  0.699   1.00 27.92 ? 5   SER C CA  1 
ATOM   3723 C C   . SER C 1 5   ? -3.094  25.532  0.761   1.00 27.76 ? 5   SER C C   1 
ATOM   3724 O O   . SER C 1 5   ? -2.684  26.056  1.796   1.00 26.48 ? 5   SER C O   1 
ATOM   3725 C CB  . SER C 1 5   ? -5.389  25.608  -0.182  1.00 30.44 ? 5   SER C CB  1 
ATOM   3726 O OG  . SER C 1 5   ? -5.522  26.917  0.344   1.00 29.90 ? 5   SER C OG  1 
ATOM   3727 N N   . ARG C 1 6   ? -2.402  25.534  -0.379  1.00 28.10 ? 6   ARG C N   1 
ATOM   3728 C CA  . ARG C 1 6   ? -1.136  26.245  -0.494  1.00 26.90 ? 6   ARG C CA  1 
ATOM   3729 C C   . ARG C 1 6   ? -1.297  27.733  -0.176  1.00 28.89 ? 6   ARG C C   1 
ATOM   3730 O O   . ARG C 1 6   ? -0.446  28.332  0.489   1.00 28.17 ? 6   ARG C O   1 
ATOM   3731 C CB  . ARG C 1 6   ? -0.608  26.063  -1.916  1.00 28.89 ? 6   ARG C CB  1 
ATOM   3732 C CG  . ARG C 1 6   ? 0.700   26.759  -2.214  1.00 36.78 ? 6   ARG C CG  1 
ATOM   3733 C CD  . ARG C 1 6   ? 1.152   26.442  -3.664  1.00 37.79 ? 6   ARG C CD  1 
ATOM   3734 N NE  . ARG C 1 6   ? 0.003   26.407  -4.566  1.00 41.98 ? 6   ARG C NE  1 
ATOM   3735 C CZ  . ARG C 1 6   ? -0.235  27.321  -5.499  1.00 50.90 ? 6   ARG C CZ  1 
ATOM   3736 N NH1 . ARG C 1 6   ? 0.632   28.292  -5.753  1.00 53.41 ? 6   ARG C NH1 1 
ATOM   3737 N NH2 . ARG C 1 6   ? -1.371  27.267  -6.192  1.00 47.20 ? 6   ARG C NH2 1 
ATOM   3738 N N   . ASP C 1 7   ? -2.376  28.349  -0.658  1.00 27.65 ? 7   ASP C N   1 
ATOM   3739 C CA  . ASP C 1 7   ? -2.589  29.770  -0.411  1.00 28.22 ? 7   ASP C CA  1 
ATOM   3740 C C   . ASP C 1 7   ? -2.681  30.061  1.083   1.00 26.74 ? 7   ASP C C   1 
ATOM   3741 O O   . ASP C 1 7   ? -2.039  30.992  1.581   1.00 23.60 ? 7   ASP C O   1 
ATOM   3742 C CB  . ASP C 1 7   ? -3.855  30.230  -1.132  1.00 26.86 ? 7   ASP C CB  1 
ATOM   3743 C CG  . ASP C 1 7   ? -3.722  30.166  -2.642  1.00 26.97 ? 7   ASP C CG  1 
ATOM   3744 O OD1 . ASP C 1 7   ? -2.729  30.635  -3.188  1.00 31.26 ? 7   ASP C OD1 1 
ATOM   3745 O OD2 . ASP C 1 7   ? -4.626  29.645  -3.307  1.00 35.88 ? 7   ASP C OD2 1 
ATOM   3746 N N   . MET C 1 8   ? -3.480  29.276  1.825   1.00 26.14 ? 8   MET C N   1 
ATOM   3747 C CA  . MET C 1 8   ? -3.536  29.484  3.272   1.00 24.85 ? 8   MET C CA  1 
ATOM   3748 C C   . MET C 1 8   ? -2.212  29.173  3.933   1.00 25.80 ? 8   MET C C   1 
ATOM   3749 O O   . MET C 1 8   ? -1.831  29.822  4.911   1.00 24.18 ? 8   MET C O   1 
ATOM   3750 C CB  . MET C 1 8   ? -4.636  28.652  3.961   1.00 27.26 ? 8   MET C CB  1 
ATOM   3751 C CG  . MET C 1 8   ? -6.084  29.189  3.880   1.00 24.50 ? 8   MET C CG  1 
ATOM   3752 S SD  . MET C 1 8   ? -6.741  29.467  2.234   1.00 32.46 ? 8   MET C SD  1 
ATOM   3753 C CE  . MET C 1 8   ? -8.402  30.054  2.662   1.00 29.61 ? 8   MET C CE  1 
ATOM   3754 N N   . LEU C 1 9   ? -1.522  28.134  3.466   1.00 25.66 ? 9   LEU C N   1 
ATOM   3755 C CA  . LEU C 1 9   ? -0.242  27.823  4.086   1.00 25.61 ? 9   LEU C CA  1 
ATOM   3756 C C   . LEU C 1 9   ? 0.757   28.957  3.871   1.00 23.06 ? 9   LEU C C   1 
ATOM   3757 O O   . LEU C 1 9   ? 1.512   29.298  4.790   1.00 24.12 ? 9   LEU C O   1 
ATOM   3758 C CB  . LEU C 1 9   ? 0.302   26.499  3.533   1.00 23.87 ? 9   LEU C CB  1 
ATOM   3759 C CG  . LEU C 1 9   ? -0.503  25.236  3.892   1.00 26.00 ? 9   LEU C CG  1 
ATOM   3760 C CD1 . LEU C 1 9   ? 0.036   24.020  3.098   1.00 23.30 ? 9   LEU C CD1 1 
ATOM   3761 C CD2 . LEU C 1 9   ? -0.437  24.959  5.363   1.00 27.40 ? 9   LEU C CD2 1 
ATOM   3762 N N   . GLN C 1 10  ? 0.782   29.559  2.670   1.00 23.78 ? 10  GLN C N   1 
ATOM   3763 C CA  . GLN C 1 10  ? 1.724   30.658  2.449   1.00 23.71 ? 10  GLN C CA  1 
ATOM   3764 C C   . GLN C 1 10  ? 1.404   31.851  3.334   1.00 23.08 ? 10  GLN C C   1 
ATOM   3765 O O   . GLN C 1 10  ? 2.310   32.470  3.908   1.00 24.81 ? 10  GLN C O   1 
ATOM   3766 C CB  . GLN C 1 10  ? 1.751   31.084  0.982   1.00 29.48 ? 10  GLN C CB  1 
ATOM   3767 C CG  . GLN C 1 10  ? 2.230   29.979  0.046   1.00 33.99 ? 10  GLN C CG  1 
ATOM   3768 C CD  . GLN C 1 10  ? 2.055   30.329  -1.421  1.00 40.07 ? 10  GLN C CD  1 
ATOM   3769 O OE1 . GLN C 1 10  ? 1.341   31.273  -1.765  1.00 35.37 ? 10  GLN C OE1 1 
ATOM   3770 N NE2 . GLN C 1 10  ? 2.633   29.510  -2.297  1.00 37.30 ? 10  GLN C NE2 1 
ATOM   3771 N N   . ASP C 1 11  ? 0.124   32.220  3.422   1.00 26.21 ? 11  ASP C N   1 
ATOM   3772 C CA  . ASP C 1 11  ? -0.267  33.334  4.272   1.00 24.22 ? 11  ASP C CA  1 
ATOM   3773 C C   . ASP C 1 11  ? 0.012   33.037  5.734   1.00 23.96 ? 11  ASP C C   1 
ATOM   3774 O O   . ASP C 1 11  ? 0.514   33.899  6.458   1.00 26.33 ? 11  ASP C O   1 
ATOM   3775 C CB  . ASP C 1 11  ? -1.736  33.678  4.050   1.00 26.38 ? 11  ASP C CB  1 
ATOM   3776 C CG  . ASP C 1 11  ? -2.256  34.640  5.103   1.00 31.43 ? 11  ASP C CG  1 
ATOM   3777 O OD1 . ASP C 1 11  ? -2.147  35.877  4.869   1.00 31.09 ? 11  ASP C OD1 1 
ATOM   3778 O OD2 . ASP C 1 11  ? -2.805  34.161  6.125   1.00 29.55 ? 11  ASP C OD2 1 
ATOM   3779 N N   . GLY C 1 12  ? -0.290  31.814  6.180   1.00 27.75 ? 12  GLY C N   1 
ATOM   3780 C CA  . GLY C 1 12  ? -0.025  31.451  7.564   1.00 25.80 ? 12  GLY C CA  1 
ATOM   3781 C C   . GLY C 1 12  ? 1.444   31.519  7.924   1.00 23.72 ? 12  GLY C C   1 
ATOM   3782 O O   . GLY C 1 12  ? 1.795   31.982  9.013   1.00 23.88 ? 12  GLY C O   1 
ATOM   3783 N N   . ALA C 1 13  ? 2.332   31.074  7.013   1.00 21.79 ? 13  ALA C N   1 
ATOM   3784 C CA  . ALA C 1 13  ? 3.767   31.171  7.302   1.00 24.48 ? 13  ALA C CA  1 
ATOM   3785 C C   . ALA C 1 13  ? 4.219   32.628  7.353   1.00 22.00 ? 13  ALA C C   1 
ATOM   3786 O O   . ALA C 1 13  ? 5.017   33.010  8.217   1.00 24.99 ? 13  ALA C O   1 
ATOM   3787 C CB  . ALA C 1 13  ? 4.594   30.381  6.263   1.00 22.51 ? 13  ALA C CB  1 
ATOM   3788 N N   . LYS C 1 14  ? 3.700   33.469  6.466   1.00 23.42 ? 14  LYS C N   1 
ATOM   3789 C CA  . LYS C 1 14  ? 4.101   34.879  6.503   1.00 23.00 ? 14  LYS C CA  1 
ATOM   3790 C C   . LYS C 1 14  ? 3.661   35.526  7.818   1.00 26.95 ? 14  LYS C C   1 
ATOM   3791 O O   . LYS C 1 14  ? 4.408   36.299  8.426   1.00 25.89 ? 14  LYS C O   1 
ATOM   3792 C CB  . LYS C 1 14  ? 3.463   35.627  5.334   1.00 28.61 ? 14  LYS C CB  1 
ATOM   3793 C CG  . LYS C 1 14  ? 4.188   36.930  4.893   1.00 36.99 ? 14  LYS C CG  1 
ATOM   3794 C CD  . LYS C 1 14  ? 5.709   36.895  5.157   1.00 34.48 ? 14  LYS C CD  1 
ATOM   3795 C CE  . LYS C 1 14  ? 6.434   37.919  4.295   1.00 43.47 ? 14  LYS C CE  1 
ATOM   3796 N NZ  . LYS C 1 14  ? 6.350   37.567  2.857   1.00 44.63 ? 14  LYS C NZ  1 
ATOM   3797 N N   . ARG C 1 15  ? 2.480   35.163  8.312   1.00 26.32 ? 15  ARG C N   1 
ATOM   3798 C CA  . ARG C 1 15  ? 2.043   35.704  9.590   1.00 27.15 ? 15  ARG C CA  1 
ATOM   3799 C C   . ARG C 1 15  ? 2.913   35.213  10.726  1.00 25.69 ? 15  ARG C C   1 
ATOM   3800 O O   . ARG C 1 15  ? 3.243   35.978  11.636  1.00 27.38 ? 15  ARG C O   1 
ATOM   3801 C CB  . ARG C 1 15  ? 0.587   35.329  9.852   1.00 26.77 ? 15  ARG C CB  1 
ATOM   3802 C CG  . ARG C 1 15  ? -0.390  36.064  8.948   1.00 33.01 ? 15  ARG C CG  1 
ATOM   3803 C CD  . ARG C 1 15  ? -1.815  35.883  9.450   1.00 29.76 ? 15  ARG C CD  1 
ATOM   3804 N NE  . ARG C 1 15  ? -2.453  34.719  8.865   1.00 31.05 ? 15  ARG C NE  1 
ATOM   3805 C CZ  . ARG C 1 15  ? -3.089  33.783  9.559   1.00 33.52 ? 15  ARG C CZ  1 
ATOM   3806 N NH1 . ARG C 1 15  ? -3.211  33.861  10.872  1.00 33.24 ? 15  ARG C NH1 1 
ATOM   3807 N NH2 . ARG C 1 15  ? -3.611  32.741  8.917   1.00 35.76 ? 15  ARG C NH2 1 
ATOM   3808 N N   . MET C 1 16  ? 3.333   33.951  10.670  1.00 25.39 ? 16  MET C N   1 
ATOM   3809 C CA  . MET C 1 16  ? 4.215   33.422  11.705  1.00 26.25 ? 16  MET C CA  1 
ATOM   3810 C C   . MET C 1 16  ? 5.563   34.127  11.669  1.00 26.26 ? 16  MET C C   1 
ATOM   3811 O O   . MET C 1 16  ? 6.172   34.410  12.705  1.00 25.90 ? 16  MET C O   1 
ATOM   3812 C CB  . MET C 1 16  ? 4.412   31.919  11.484  1.00 25.66 ? 16  MET C CB  1 
ATOM   3813 C CG  . MET C 1 16  ? 3.163   31.073  11.728  1.00 27.49 ? 16  MET C CG  1 
ATOM   3814 S SD  . MET C 1 16  ? 2.781   30.787  13.435  1.00 27.17 ? 16  MET C SD  1 
ATOM   3815 C CE  . MET C 1 16  ? 4.390   30.368  14.113  1.00 30.73 ? 16  MET C CE  1 
ATOM   3816 N N   . PHE C 1 17  ? 6.066   34.346  10.467  1.00 28.06 ? 17  PHE C N   1 
ATOM   3817 C CA  . PHE C 1 17  ? 7.328   35.049  10.270  1.00 25.83 ? 17  PHE C CA  1 
ATOM   3818 C C   . PHE C 1 17  ? 7.242   36.494  10.773  1.00 29.28 ? 17  PHE C C   1 
ATOM   3819 O O   . PHE C 1 17  ? 8.127   36.963  11.502  1.00 28.96 ? 17  PHE C O   1 
ATOM   3820 C CB  . PHE C 1 17  ? 7.665   34.957  8.789   1.00 23.82 ? 17  PHE C CB  1 
ATOM   3821 C CG  . PHE C 1 17  ? 8.938   35.638  8.383   1.00 27.95 ? 17  PHE C CG  1 
ATOM   3822 C CD1 . PHE C 1 17  ? 10.166  35.086  8.680   1.00 28.54 ? 17  PHE C CD1 1 
ATOM   3823 C CD2 . PHE C 1 17  ? 8.894   36.791  7.611   1.00 33.83 ? 17  PHE C CD2 1 
ATOM   3824 C CE1 . PHE C 1 17  ? 11.337  35.680  8.238   1.00 29.96 ? 17  PHE C CE1 1 
ATOM   3825 C CE2 . PHE C 1 17  ? 10.073  37.403  7.178   1.00 35.82 ? 17  PHE C CE2 1 
ATOM   3826 C CZ  . PHE C 1 17  ? 11.296  36.821  7.488   1.00 30.01 ? 17  PHE C CZ  1 
ATOM   3827 N N   . LYS C 1 18  ? 6.163   37.204  10.417  1.00 29.31 ? 18  LYS C N   1 
ATOM   3828 C CA  . LYS C 1 18  ? 5.979   38.580  10.895  1.00 32.04 ? 18  LYS C CA  1 
ATOM   3829 C C   . LYS C 1 18  ? 5.857   38.626  12.415  1.00 30.01 ? 18  LYS C C   1 
ATOM   3830 O O   . LYS C 1 18  ? 6.422   39.507  13.063  1.00 29.75 ? 18  LYS C O   1 
ATOM   3831 C CB  . LYS C 1 18  ? 4.735   39.199  10.263  1.00 30.65 ? 18  LYS C CB  1 
ATOM   3832 C CG  . LYS C 1 18  ? 4.710   39.235  8.734   1.00 33.76 ? 18  LYS C CG  1 
ATOM   3833 C CD  . LYS C 1 18  ? 4.860   40.583  8.135   1.00 40.95 ? 18  LYS C CD  1 
ATOM   3834 C CE  . LYS C 1 18  ? 3.524   41.078  7.562   1.00 45.61 ? 18  LYS C CE  1 
ATOM   3835 N NZ  . LYS C 1 18  ? 3.699   42.300  6.682   1.00 49.31 ? 18  LYS C NZ  1 
ATOM   3836 N N   . TRP C 1 19  ? 5.167   37.650  13.006  1.00 28.03 ? 19  TRP C N   1 
ATOM   3837 C CA  . TRP C 1 19  ? 5.054   37.580  14.462  1.00 31.49 ? 19  TRP C CA  1 
ATOM   3838 C C   . TRP C 1 19  ? 6.413   37.405  15.128  1.00 33.91 ? 19  TRP C C   1 
ATOM   3839 O O   . TRP C 1 19  ? 6.736   38.091  16.109  1.00 30.19 ? 19  TRP C O   1 
ATOM   3840 C CB  . TRP C 1 19  ? 4.145   36.409  14.851  1.00 30.76 ? 19  TRP C CB  1 
ATOM   3841 C CG  . TRP C 1 19  ? 3.895   36.348  16.322  1.00 35.85 ? 19  TRP C CG  1 
ATOM   3842 C CD1 . TRP C 1 19  ? 4.660   35.719  17.266  1.00 33.49 ? 19  TRP C CD1 1 
ATOM   3843 C CD2 . TRP C 1 19  ? 2.814   36.956  17.024  1.00 32.50 ? 19  TRP C CD2 1 
ATOM   3844 N NE1 . TRP C 1 19  ? 4.112   35.900  18.510  1.00 34.38 ? 19  TRP C NE1 1 
ATOM   3845 C CE2 . TRP C 1 19  ? 2.978   36.654  18.386  1.00 34.41 ? 19  TRP C CE2 1 
ATOM   3846 C CE3 . TRP C 1 19  ? 1.711   37.716  16.630  1.00 35.07 ? 19  TRP C CE3 1 
ATOM   3847 C CZ2 . TRP C 1 19  ? 2.076   37.089  19.360  1.00 39.10 ? 19  TRP C CZ2 1 
ATOM   3848 C CZ3 . TRP C 1 19  ? 0.815   38.136  17.596  1.00 37.23 ? 19  TRP C CZ3 1 
ATOM   3849 C CH2 . TRP C 1 19  ? 1.005   37.826  18.941  1.00 36.69 ? 19  TRP C CH2 1 
ATOM   3850 N N   . LEU C 1 20  ? 7.211   36.452  14.623  1.00 31.67 ? 20  LEU C N   1 
ATOM   3851 C CA  . LEU C 1 20  ? 8.522   36.182  15.204  1.00 33.14 ? 20  LEU C CA  1 
ATOM   3852 C C   . LEU C 1 20  ? 9.410   37.410  15.138  1.00 32.10 ? 20  LEU C C   1 
ATOM   3853 O O   . LEU C 1 20  ? 10.306  37.573  15.973  1.00 34.45 ? 20  LEU C O   1 
ATOM   3854 C CB  . LEU C 1 20  ? 9.176   34.989  14.488  1.00 29.74 ? 20  LEU C CB  1 
ATOM   3855 C CG  . LEU C 1 20  ? 8.726   33.595  14.922  1.00 31.96 ? 20  LEU C CG  1 
ATOM   3856 C CD1 . LEU C 1 20  ? 9.243   32.508  13.931  1.00 31.00 ? 20  LEU C CD1 1 
ATOM   3857 C CD2 . LEU C 1 20  ? 9.208   33.297  16.337  1.00 32.45 ? 20  LEU C CD2 1 
ATOM   3858 N N   . ARG C 1 21  ? 9.156   38.296  14.175  1.00 31.53 ? 21  ARG C N   1 
ATOM   3859 C CA  . ARG C 1 21  ? 9.931   39.521  14.050  1.00 33.01 ? 21  ARG C CA  1 
ATOM   3860 C C   . ARG C 1 21  ? 9.859   40.394  15.289  1.00 36.35 ? 21  ARG C C   1 
ATOM   3861 O O   . ARG C 1 21  ? 10.746  41.229  15.485  1.00 39.36 ? 21  ARG C O   1 
ATOM   3862 C CB  . ARG C 1 21  ? 9.456   40.329  12.840  1.00 34.44 ? 21  ARG C CB  1 
ATOM   3863 C CG  . ARG C 1 21  ? 10.554  41.198  12.226  1.00 37.91 ? 21  ARG C CG  1 
ATOM   3864 C CD  . ARG C 1 21  ? 10.139  41.703  10.854  1.00 35.79 ? 21  ARG C CD  1 
ATOM   3865 N NE  . ARG C 1 21  ? 8.712   41.992  10.808  1.00 40.90 ? 21  ARG C NE  1 
ATOM   3866 C CZ  . ARG C 1 21  ? 8.040   42.216  9.689   1.00 39.74 ? 21  ARG C CZ  1 
ATOM   3867 N NH1 . ARG C 1 21  ? 8.637   42.194  8.513   1.00 42.75 ? 21  ARG C NH1 1 
ATOM   3868 N NH2 . ARG C 1 21  ? 6.748   42.501  9.758   1.00 46.28 ? 21  ARG C NH2 1 
ATOM   3869 N N   . LYS C 1 22  ? 8.819   40.239  16.114  1.00 32.11 ? 22  LYS C N   1 
ATOM   3870 C CA  . LYS C 1 22  ? 8.700   41.011  17.336  1.00 33.79 ? 22  LYS C CA  1 
ATOM   3871 C C   . LYS C 1 22  ? 9.684   40.579  18.410  1.00 37.65 ? 22  LYS C C   1 
ATOM   3872 O O   . LYS C 1 22  ? 9.806   41.272  19.423  1.00 42.36 ? 22  LYS C O   1 
ATOM   3873 C CB  . LYS C 1 22  ? 7.264   40.916  17.864  1.00 38.88 ? 22  LYS C CB  1 
ATOM   3874 C CG  . LYS C 1 22  ? 6.282   41.666  16.975  1.00 36.83 ? 22  LYS C CG  1 
ATOM   3875 C CD  . LYS C 1 22  ? 4.937   40.986  16.954  1.00 43.25 ? 22  LYS C CD  1 
ATOM   3876 C CE  . LYS C 1 22  ? 4.384   40.874  18.349  1.00 40.68 ? 22  LYS C CE  1 
ATOM   3877 N NZ  . LYS C 1 22  ? 3.242   39.933  18.393  1.00 43.91 ? 22  LYS C NZ  1 
ATOM   3878 N N   . GLY C 1 23  ? 10.372  39.455  18.235  1.00 37.20 ? 23  GLY C N   1 
ATOM   3879 C CA  . GLY C 1 23  ? 11.309  39.014  19.248  1.00 35.05 ? 23  GLY C CA  1 
ATOM   3880 C C   . GLY C 1 23  ? 10.682  38.471  20.510  1.00 35.51 ? 23  GLY C C   1 
ATOM   3881 O O   . GLY C 1 23  ? 11.362  38.399  21.535  1.00 37.59 ? 23  GLY C O   1 
ATOM   3882 N N   . GLU C 1 24  ? 9.402   38.090  20.473  1.00 31.85 ? 24  GLU C N   1 
ATOM   3883 C CA  . GLU C 1 24  ? 8.692   37.567  21.632  1.00 36.54 ? 24  GLU C CA  1 
ATOM   3884 C C   . GLU C 1 24  ? 8.331   36.087  21.509  1.00 39.04 ? 24  GLU C C   1 
ATOM   3885 O O   . GLU C 1 24  ? 7.469   35.589  22.243  1.00 35.76 ? 24  GLU C O   1 
ATOM   3886 C CB  . GLU C 1 24  ? 7.461   38.431  21.849  1.00 36.35 ? 24  GLU C CB  1 
ATOM   3887 C CG  . GLU C 1 24  ? 7.829   39.906  22.175  1.00 40.34 ? 24  GLU C CG  1 
ATOM   3888 C CD  . GLU C 1 24  ? 6.692   40.814  21.825  1.00 44.67 ? 24  GLU C CD  1 
ATOM   3889 O OE1 . GLU C 1 24  ? 6.859   41.912  21.269  1.00 53.30 ? 24  GLU C OE1 1 
ATOM   3890 O OE2 . GLU C 1 24  ? 5.562   40.267  21.852  1.00 50.91 ? 24  GLU C OE2 1 
ATOM   3891 N N   . GLY C 1 25  ? 9.003   35.354  20.629  1.00 37.89 ? 25  GLY C N   1 
ATOM   3892 C CA  . GLY C 1 25  ? 8.732   33.937  20.521  1.00 37.06 ? 25  GLY C CA  1 
ATOM   3893 C C   . GLY C 1 25  ? 7.539   33.637  19.635  1.00 34.81 ? 25  GLY C C   1 
ATOM   3894 O O   . GLY C 1 25  ? 6.934   34.525  19.016  1.00 35.22 ? 25  GLY C O   1 
ATOM   3895 N N   . LEU C 1 26  ? 7.193   32.346  19.592  1.00 34.51 ? 26  LEU C N   1 
ATOM   3896 C CA  . LEU C 1 26  ? 6.111   31.877  18.738  1.00 34.86 ? 26  LEU C CA  1 
ATOM   3897 C C   . LEU C 1 26  ? 4.768   32.278  19.336  1.00 32.15 ? 26  LEU C C   1 
ATOM   3898 O O   . LEU C 1 26  ? 4.660   32.428  20.550  1.00 33.00 ? 26  LEU C O   1 
ATOM   3899 C CB  . LEU C 1 26  ? 6.163   30.355  18.575  1.00 34.92 ? 26  LEU C CB  1 
ATOM   3900 C CG  . LEU C 1 26  ? 7.390   29.711  17.929  1.00 37.75 ? 26  LEU C CG  1 
ATOM   3901 C CD1 . LEU C 1 26  ? 7.447   28.211  18.233  1.00 38.47 ? 26  LEU C CD1 1 
ATOM   3902 C CD2 . LEU C 1 26  ? 7.353   29.946  16.433  1.00 34.35 ? 26  LEU C CD2 1 
ATOM   3903 N N   . PRO C 1 27  ? 3.739   32.474  18.499  1.00 33.72 ? 27  PRO C N   1 
ATOM   3904 C CA  . PRO C 1 27  ? 2.405   32.808  19.015  1.00 31.86 ? 27  PRO C CA  1 
ATOM   3905 C C   . PRO C 1 27  ? 1.736   31.612  19.675  1.00 33.11 ? 27  PRO C C   1 
ATOM   3906 O O   . PRO C 1 27  ? 2.071   30.456  19.425  1.00 34.44 ? 27  PRO C O   1 
ATOM   3907 C CB  . PRO C 1 27  ? 1.634   33.209  17.757  1.00 33.23 ? 27  PRO C CB  1 
ATOM   3908 C CG  . PRO C 1 27  ? 2.262   32.323  16.670  1.00 31.28 ? 27  PRO C CG  1 
ATOM   3909 C CD  . PRO C 1 27  ? 3.729   32.319  17.032  1.00 29.87 ? 27  PRO C CD  1 
ATOM   3910 N N   . ASN C 1 28  ? 0.729   31.902  20.495  1.00 32.54 ? 28  ASN C N   1 
ATOM   3911 C CA  . ASN C 1 28  ? 0.036   30.827  21.194  1.00 29.88 ? 28  ASN C CA  1 
ATOM   3912 C C   . ASN C 1 28  ? -0.842  29.993  20.273  1.00 30.46 ? 28  ASN C C   1 
ATOM   3913 O O   . ASN C 1 28  ? -1.209  28.875  20.642  1.00 30.83 ? 28  ASN C O   1 
ATOM   3914 C CB  . ASN C 1 28  ? -0.804  31.388  22.338  1.00 36.22 ? 28  ASN C CB  1 
ATOM   3915 C CG  . ASN C 1 28  ? 0.051   31.861  23.500  1.00 39.16 ? 28  ASN C CG  1 
ATOM   3916 O OD1 . ASN C 1 28  ? 1.029   31.207  23.871  1.00 44.57 ? 28  ASN C OD1 1 
ATOM   3917 N ND2 . ASN C 1 28  ? -0.338  32.982  24.107  1.00 42.54 ? 28  ASN C ND2 1 
ATOM   3918 N N   . TYR C 1 29  ? -1.214  30.502  19.103  1.00 30.00 ? 29  TYR C N   1 
ATOM   3919 C CA  . TYR C 1 29  ? -2.001  29.723  18.157  1.00 30.23 ? 29  TYR C CA  1 
ATOM   3920 C C   . TYR C 1 29  ? -1.895  30.373  16.784  1.00 30.72 ? 29  TYR C C   1 
ATOM   3921 O O   . TYR C 1 29  ? -1.352  31.467  16.642  1.00 28.40 ? 29  TYR C O   1 
ATOM   3922 C CB  . TYR C 1 29  ? -3.433  29.592  18.656  1.00 30.93 ? 29  TYR C CB  1 
ATOM   3923 C CG  . TYR C 1 29  ? -4.159  30.904  18.784  1.00 32.65 ? 29  TYR C CG  1 
ATOM   3924 C CD1 . TYR C 1 29  ? -4.422  31.705  17.679  1.00 35.27 ? 29  TYR C CD1 1 
ATOM   3925 C CD2 . TYR C 1 29  ? -4.451  31.412  20.039  1.00 36.41 ? 29  TYR C CD2 1 
ATOM   3926 C CE1 . TYR C 1 29  ? -5.068  32.924  17.803  1.00 37.26 ? 29  TYR C CE1 1 
ATOM   3927 C CE2 . TYR C 1 29  ? -5.095  32.636  20.177  1.00 38.78 ? 29  TYR C CE2 1 
ATOM   3928 C CZ  . TYR C 1 29  ? -5.388  33.391  19.051  1.00 42.03 ? 29  TYR C CZ  1 
ATOM   3929 O OH  . TYR C 1 29  ? -6.014  34.619  19.178  1.00 47.99 ? 29  TYR C OH  1 
ATOM   3930 N N   . LEU C 1 30  ? -2.390  29.663  15.767  1.00 27.43 ? 30  LEU C N   1 
ATOM   3931 C CA  . LEU C 1 30  ? -2.431  30.157  14.396  1.00 28.57 ? 30  LEU C CA  1 
ATOM   3932 C C   . LEU C 1 30  ? -3.806  29.828  13.839  1.00 31.54 ? 30  LEU C C   1 
ATOM   3933 O O   . LEU C 1 30  ? -4.178  28.656  13.759  1.00 32.65 ? 30  LEU C O   1 
ATOM   3934 C CB  . LEU C 1 30  ? -1.313  29.522  13.536  1.00 27.74 ? 30  LEU C CB  1 
ATOM   3935 C CG  . LEU C 1 30  ? -1.255  29.912  12.053  1.00 31.94 ? 30  LEU C CG  1 
ATOM   3936 C CD1 . LEU C 1 30  ? -0.825  31.397  11.951  1.00 25.53 ? 30  LEU C CD1 1 
ATOM   3937 C CD2 . LEU C 1 30  ? -0.224  29.069  11.238  1.00 26.85 ? 30  LEU C CD2 1 
ATOM   3938 N N   . ILE C 1 31  ? -4.560  30.856  13.472  1.00 31.05 ? 31  ILE C N   1 
ATOM   3939 C CA  . ILE C 1 31  ? -5.887  30.682  12.897  1.00 34.00 ? 31  ILE C CA  1 
ATOM   3940 C C   . ILE C 1 31  ? -5.740  30.440  11.406  1.00 33.08 ? 31  ILE C C   1 
ATOM   3941 O O   . ILE C 1 31  ? -5.051  31.202  10.719  1.00 34.04 ? 31  ILE C O   1 
ATOM   3942 C CB  . ILE C 1 31  ? -6.755  31.928  13.147  1.00 36.00 ? 31  ILE C CB  1 
ATOM   3943 C CG1 . ILE C 1 31  ? -7.046  32.117  14.628  1.00 37.89 ? 31  ILE C CG1 1 
ATOM   3944 C CG2 . ILE C 1 31  ? -8.024  31.834  12.354  1.00 36.94 ? 31  ILE C CG2 1 
ATOM   3945 C CD1 . ILE C 1 31  ? -7.479  30.911  15.237  1.00 36.64 ? 31  ILE C CD1 1 
ATOM   3946 N N   . MET C 1 32  ? -6.391  29.400  10.891  1.00 30.57 ? 32  MET C N   1 
ATOM   3947 C CA  . MET C 1 32  ? -6.376  29.176  9.456   1.00 31.11 ? 32  MET C CA  1 
ATOM   3948 C C   . MET C 1 32  ? -7.722  28.607  9.028   1.00 29.38 ? 32  MET C C   1 
ATOM   3949 O O   . MET C 1 32  ? -8.408  27.935  9.801   1.00 30.80 ? 32  MET C O   1 
ATOM   3950 C CB  . MET C 1 32  ? -5.200  28.255  9.067   1.00 30.96 ? 32  MET C CB  1 
ATOM   3951 C CG  . MET C 1 32  ? -3.958  29.088  8.763   1.00 34.64 ? 32  MET C CG  1 
ATOM   3952 S SD  . MET C 1 32  ? -2.547  28.254  8.028   1.00 37.60 ? 32  MET C SD  1 
ATOM   3953 C CE  . MET C 1 32  ? -3.261  26.738  7.485   1.00 26.94 ? 32  MET C CE  1 
ATOM   3954 N N   . TYR C 1 33  ? -8.060  28.821  7.757   1.00 29.47 ? 33  TYR C N   1 
ATOM   3955 C CA  . TYR C 1 33  ? -9.316  28.354  7.175   1.00 34.33 ? 33  TYR C CA  1 
ATOM   3956 C C   . TYR C 1 33  ? -9.048  27.140  6.296   1.00 35.74 ? 33  TYR C C   1 
ATOM   3957 O O   . TYR C 1 33  ? -8.123  27.166  5.487   1.00 29.29 ? 33  TYR C O   1 
ATOM   3958 C CB  . TYR C 1 33  ? -9.962  29.459  6.332   1.00 32.68 ? 33  TYR C CB  1 
ATOM   3959 C CG  . TYR C 1 33  ? -10.659 30.479  7.176   1.00 32.45 ? 33  TYR C CG  1 
ATOM   3960 C CD1 . TYR C 1 33  ? -9.960  31.542  7.728   1.00 33.33 ? 33  TYR C CD1 1 
ATOM   3961 C CD2 . TYR C 1 33  ? -12.014 30.349  7.468   1.00 33.92 ? 33  TYR C CD2 1 
ATOM   3962 C CE1 . TYR C 1 33  ? -10.597 32.469  8.536   1.00 35.20 ? 33  TYR C CE1 1 
ATOM   3963 C CE2 . TYR C 1 33  ? -12.657 31.270  8.267   1.00 34.93 ? 33  TYR C CE2 1 
ATOM   3964 C CZ  . TYR C 1 33  ? -11.942 32.317  8.801   1.00 34.00 ? 33  TYR C CZ  1 
ATOM   3965 O OH  . TYR C 1 33  ? -12.566 33.244  9.604   1.00 39.78 ? 33  TYR C OH  1 
ATOM   3966 N N   . ASP C 1 34  ? -9.832  26.069  6.477   1.00 32.93 ? 34  ASP C N   1 
ATOM   3967 C CA  . ASP C 1 34  ? -9.627  24.852  5.702   1.00 30.88 ? 34  ASP C CA  1 
ATOM   3968 C C   . ASP C 1 34  ? -10.145 25.036  4.273   1.00 34.44 ? 34  ASP C C   1 
ATOM   3969 O O   . ASP C 1 34  ? -10.958 25.919  3.995   1.00 35.07 ? 34  ASP C O   1 
ATOM   3970 C CB  . ASP C 1 34  ? -10.292 23.643  6.383   1.00 35.04 ? 34  ASP C CB  1 
ATOM   3971 C CG  . ASP C 1 34  ? -11.795 23.545  6.099   1.00 36.76 ? 34  ASP C CG  1 
ATOM   3972 O OD1 . ASP C 1 34  ? -12.559 24.401  6.586   1.00 36.92 ? 34  ASP C OD1 1 
ATOM   3973 O OD2 . ASP C 1 34  ? -12.203 22.625  5.364   1.00 38.35 ? 34  ASP C OD2 1 
ATOM   3974 N N   . MET C 1 35  ? -9.633  24.215  3.343   1.00 34.57 ? 35  MET C N   1 
ATOM   3975 C CA  . MET C 1 35  ? -9.971  24.446  1.939   1.00 34.61 ? 35  MET C CA  1 
ATOM   3976 C C   . MET C 1 35  ? -11.299 23.827  1.542   1.00 36.89 ? 35  MET C C   1 
ATOM   3977 O O   . MET C 1 35  ? -11.862 24.207  0.510   1.00 38.63 ? 35  MET C O   1 
ATOM   3978 C CB  . MET C 1 35  ? -8.924  23.871  0.974   1.00 35.21 ? 35  MET C CB  1 
ATOM   3979 C CG  . MET C 1 35  ? -8.489  22.456  1.235   1.00 37.06 ? 35  MET C CG  1 
ATOM   3980 S SD  . MET C 1 35  ? -7.080  22.030  0.191   1.00 38.41 ? 35  MET C SD  1 
ATOM   3981 C CE  . MET C 1 35  ? -7.782  22.074  -1.445  1.00 35.58 ? 35  MET C CE  1 
ATOM   3982 N N   . ASP C 1 36  ? -11.837 22.927  2.353   1.00 36.21 ? 36  ASP C N   1 
ATOM   3983 C CA  . ASP C 1 36  ? -13.044 22.202  1.985   1.00 39.63 ? 36  ASP C CA  1 
ATOM   3984 C C   . ASP C 1 36  ? -14.285 22.821  2.595   1.00 42.61 ? 36  ASP C C   1 
ATOM   3985 O O   . ASP C 1 36  ? -15.344 22.837  1.966   1.00 47.54 ? 36  ASP C O   1 
ATOM   3986 C CB  . ASP C 1 36  ? -12.950 20.721  2.397   1.00 36.15 ? 36  ASP C CB  1 
ATOM   3987 C CG  . ASP C 1 36  ? -11.745 20.007  1.785   1.00 38.36 ? 36  ASP C CG  1 
ATOM   3988 O OD1 . ASP C 1 36  ? -11.668 19.936  0.537   1.00 41.41 ? 36  ASP C OD1 1 
ATOM   3989 O OD2 . ASP C 1 36  ? -10.882 19.507  2.544   1.00 37.48 ? 36  ASP C OD2 1 
ATOM   3990 N N   . ARG C 1 37  ? -14.201 23.248  3.841   1.00 40.13 ? 37  ARG C N   1 
ATOM   3991 C CA  . ARG C 1 37  ? -15.310 23.917  4.485   1.00 41.67 ? 37  ARG C CA  1 
ATOM   3992 C C   . ARG C 1 37  ? -15.201 25.431  4.630   1.00 41.25 ? 37  ARG C C   1 
ATOM   3993 O O   . ARG C 1 37  ? -16.211 26.056  4.973   1.00 44.45 ? 37  ARG C O   1 
ATOM   3994 C CB  . ARG C 1 37  ? -15.526 23.287  5.858   1.00 41.13 ? 37  ARG C CB  1 
ATOM   3995 C CG  . ARG C 1 37  ? -15.893 21.833  5.772   1.00 42.93 ? 37  ARG C CG  1 
ATOM   3996 C CD  . ARG C 1 37  ? -15.621 21.166  7.118   1.00 45.94 ? 37  ARG C CD  1 
ATOM   3997 N NE  . ARG C 1 37  ? -14.247 20.676  7.163   1.00 54.17 ? 37  ARG C NE  1 
ATOM   3998 C CZ  . ARG C 1 37  ? -13.896 19.446  7.515   1.00 51.18 ? 37  ARG C CZ  1 
ATOM   3999 N NH1 . ARG C 1 37  ? -14.788 18.564  7.923   1.00 51.54 ? 37  ARG C NH1 1 
ATOM   4000 N NH2 . ARG C 1 37  ? -12.624 19.076  7.395   1.00 50.69 ? 37  ARG C NH2 1 
ATOM   4001 N N   . ASN C 1 38  ? -14.036 26.053  4.427   1.00 38.44 ? 38  ASN C N   1 
ATOM   4002 C CA  . ASN C 1 38  ? -13.952 27.495  4.675   1.00 41.36 ? 38  ASN C CA  1 
ATOM   4003 C C   . ASN C 1 38  ? -14.384 27.818  6.109   1.00 40.49 ? 38  ASN C C   1 
ATOM   4004 O O   . ASN C 1 38  ? -15.097 28.784  6.372   1.00 44.09 ? 38  ASN C O   1 
ATOM   4005 C CB  . ASN C 1 38  ? -14.760 28.236  3.608   1.00 44.40 ? 38  ASN C CB  1 
ATOM   4006 C CG  . ASN C 1 38  ? -14.300 27.855  2.197   1.00 48.19 ? 38  ASN C CG  1 
ATOM   4007 O OD1 . ASN C 1 38  ? -15.099 27.476  1.328   1.00 52.29 ? 38  ASN C OD1 1 
ATOM   4008 N ND2 . ASN C 1 38  ? -13.019 28.097  1.927   1.00 45.58 ? 38  ASN C ND2 1 
ATOM   4009 N N   . LYS C 1 39  ? -14.048 26.903  7.017   1.00 40.58 ? 39  LYS C N   1 
ATOM   4010 C CA  . LYS C 1 39  ? -14.249 27.022  8.456   1.00 39.72 ? 39  LYS C CA  1 
ATOM   4011 C C   . LYS C 1 39  ? -12.943 27.430  9.142   1.00 38.04 ? 39  LYS C C   1 
ATOM   4012 O O   . LYS C 1 39  ? -11.864 26.939  8.789   1.00 35.18 ? 39  LYS C O   1 
ATOM   4013 C CB  . LYS C 1 39  ? -14.754 25.680  9.005   1.00 39.27 ? 39  LYS C CB  1 
ATOM   4014 C CG  . LYS C 1 39  ? -14.493 25.383  10.484  1.00 42.59 ? 39  LYS C CG  1 
ATOM   4015 C CD  . LYS C 1 39  ? -15.498 26.125  11.385  1.00 49.13 ? 39  LYS C CD  1 
ATOM   4016 C CE  . LYS C 1 39  ? -15.023 26.244  12.841  1.00 46.91 ? 39  LYS C CE  1 
ATOM   4017 N NZ  . LYS C 1 39  ? -14.503 27.623  13.140  1.00 47.03 ? 39  LYS C NZ  1 
ATOM   4018 N N   . GLU C 1 40  ? -13.061 28.221  10.201  1.00 38.03 ? 40  GLU C N   1 
ATOM   4019 C CA  . GLU C 1 40  ? -11.913 28.688  10.966  1.00 35.46 ? 40  GLU C CA  1 
ATOM   4020 C C   . GLU C 1 40  ? -11.374 27.587  11.885  1.00 40.11 ? 40  GLU C C   1 
ATOM   4021 O O   . GLU C 1 40  ? -12.132 26.989  12.658  1.00 37.57 ? 40  GLU C O   1 
ATOM   4022 C CB  . GLU C 1 40  ? -12.335 29.892  11.799  1.00 36.28 ? 40  GLU C CB  1 
ATOM   4023 C CG  . GLU C 1 40  ? -11.254 30.457  12.666  1.00 39.33 ? 40  GLU C CG  1 
ATOM   4024 C CD  . GLU C 1 40  ? -11.561 31.875  13.104  1.00 44.76 ? 40  GLU C CD  1 
ATOM   4025 O OE1 . GLU C 1 40  ? -11.575 32.147  14.322  1.00 47.24 ? 40  GLU C OE1 1 
ATOM   4026 O OE2 . GLU C 1 40  ? -11.835 32.717  12.223  1.00 50.67 ? 40  GLU C OE2 1 
ATOM   4027 N N   . TYR C 1 41  ? -10.063 27.339  11.833  1.00 35.15 ? 41  TYR C N   1 
ATOM   4028 C CA  . TYR C 1 41  ? -9.404  26.408  12.751  1.00 33.62 ? 41  TYR C CA  1 
ATOM   4029 C C   . TYR C 1 41  ? -8.344  27.156  13.547  1.00 33.24 ? 41  TYR C C   1 
ATOM   4030 O O   . TYR C 1 41  ? -7.541  27.908  12.981  1.00 38.78 ? 41  TYR C O   1 
ATOM   4031 C CB  . TYR C 1 41  ? -8.770  25.223  11.996  1.00 33.62 ? 41  TYR C CB  1 
ATOM   4032 C CG  . TYR C 1 41  ? -9.796  24.275  11.451  1.00 33.72 ? 41  TYR C CG  1 
ATOM   4033 C CD1 . TYR C 1 41  ? -10.273 23.208  12.215  1.00 34.61 ? 41  TYR C CD1 1 
ATOM   4034 C CD2 . TYR C 1 41  ? -10.350 24.491  10.200  1.00 34.93 ? 41  TYR C CD2 1 
ATOM   4035 C CE1 . TYR C 1 41  ? -11.249 22.342  11.711  1.00 38.68 ? 41  TYR C CE1 1 
ATOM   4036 C CE2 . TYR C 1 41  ? -11.325 23.651  9.693   1.00 37.63 ? 41  TYR C CE2 1 
ATOM   4037 C CZ  . TYR C 1 41  ? -11.779 22.585  10.453  1.00 39.79 ? 41  TYR C CZ  1 
ATOM   4038 O OH  . TYR C 1 41  ? -12.748 21.763  9.931   1.00 38.58 ? 41  TYR C OH  1 
ATOM   4039 N N   . LYS C 1 42  ? -8.322  26.922  14.849  1.00 32.18 ? 42  LYS C N   1 
ATOM   4040 C CA  . LYS C 1 42  ? -7.346  27.521  15.753  1.00 32.48 ? 42  LYS C CA  1 
ATOM   4041 C C   . LYS C 1 42  ? -6.305  26.450  16.079  1.00 34.13 ? 42  LYS C C   1 
ATOM   4042 O O   . LYS C 1 42  ? -6.540  25.578  16.920  1.00 30.77 ? 42  LYS C O   1 
ATOM   4043 C CB  . LYS C 1 42  ? -8.063  28.041  16.992  1.00 32.33 ? 42  LYS C CB  1 
ATOM   4044 C CG  . LYS C 1 42  ? -7.206  28.637  18.074  1.00 33.10 ? 42  LYS C CG  1 
ATOM   4045 C CD  . LYS C 1 42  ? -7.861  29.949  18.532  1.00 39.74 ? 42  LYS C CD  1 
ATOM   4046 C CE  . LYS C 1 42  ? -7.561  30.293  19.968  1.00 43.94 ? 42  LYS C CE  1 
ATOM   4047 N NZ  . LYS C 1 42  ? -8.783  30.809  20.689  1.00 50.62 ? 42  LYS C NZ  1 
ATOM   4048 N N   . LEU C 1 43  ? -5.172  26.480  15.377  1.00 29.69 ? 43  LEU C N   1 
ATOM   4049 C CA  . LEU C 1 43  ? -4.139  25.468  15.584  1.00 27.19 ? 43  LEU C CA  1 
ATOM   4050 C C   . LEU C 1 43  ? -3.258  25.825  16.772  1.00 26.43 ? 43  LEU C C   1 
ATOM   4051 O O   . LEU C 1 43  ? -2.691  26.914  16.821  1.00 30.40 ? 43  LEU C O   1 
ATOM   4052 C CB  . LEU C 1 43  ? -3.291  25.315  14.324  1.00 26.17 ? 43  LEU C CB  1 
ATOM   4053 C CG  . LEU C 1 43  ? -4.065  25.033  13.035  1.00 30.79 ? 43  LEU C CG  1 
ATOM   4054 C CD1 . LEU C 1 43  ? -3.085  24.961  11.859  1.00 30.55 ? 43  LEU C CD1 1 
ATOM   4055 C CD2 . LEU C 1 43  ? -4.897  23.742  13.129  1.00 26.03 ? 43  LEU C CD2 1 
ATOM   4056 N N   . VAL C 1 44  ? -3.130  24.909  17.726  1.00 25.87 ? 44  VAL C N   1 
ATOM   4057 C CA  . VAL C 1 44  ? -2.226  25.098  18.858  1.00 25.08 ? 44  VAL C CA  1 
ATOM   4058 C C   . VAL C 1 44  ? -0.817  24.837  18.339  1.00 28.31 ? 44  VAL C C   1 
ATOM   4059 O O   . VAL C 1 44  ? -0.675  24.312  17.226  1.00 27.65 ? 44  VAL C O   1 
ATOM   4060 C CB  . VAL C 1 44  ? -2.606  24.189  20.037  1.00 29.03 ? 44  VAL C CB  1 
ATOM   4061 C CG1 . VAL C 1 44  ? -4.058  24.467  20.485  1.00 26.36 ? 44  VAL C CG1 1 
ATOM   4062 C CG2 . VAL C 1 44  ? -2.464  22.738  19.661  1.00 27.74 ? 44  VAL C CG2 1 
ATOM   4063 N N   . PRO C 1 45  ? 0.241   25.233  19.064  1.00 30.12 ? 45  PRO C N   1 
ATOM   4064 C CA  . PRO C 1 45  ? 1.608   25.124  18.504  1.00 28.10 ? 45  PRO C CA  1 
ATOM   4065 C C   . PRO C 1 45  ? 2.010   23.733  18.040  1.00 27.88 ? 45  PRO C C   1 
ATOM   4066 O O   . PRO C 1 45  ? 2.681   23.630  17.004  1.00 27.82 ? 45  PRO C O   1 
ATOM   4067 C CB  . PRO C 1 45  ? 2.493   25.622  19.656  1.00 30.44 ? 45  PRO C CB  1 
ATOM   4068 C CG  . PRO C 1 45  ? 1.578   26.673  20.348  1.00 31.66 ? 45  PRO C CG  1 
ATOM   4069 C CD  . PRO C 1 45  ? 0.216   26.025  20.315  1.00 31.07 ? 45  PRO C CD  1 
ATOM   4070 N N   . LYS C 1 46  ? 1.675   22.664  18.776  1.00 26.68 ? 46  LYS C N   1 
ATOM   4071 C CA  . LYS C 1 46  ? 2.034   21.326  18.290  1.00 26.43 ? 46  LYS C CA  1 
ATOM   4072 C C   . LYS C 1 46  ? 1.341   21.019  16.966  1.00 27.49 ? 46  LYS C C   1 
ATOM   4073 O O   . LYS C 1 46  ? 1.877   20.252  16.147  1.00 28.20 ? 46  LYS C O   1 
ATOM   4074 C CB  . LYS C 1 46  ? 1.686   20.250  19.322  1.00 28.93 ? 46  LYS C CB  1 
ATOM   4075 C CG  . LYS C 1 46  ? 0.173   20.049  19.433  1.00 30.00 ? 46  LYS C CG  1 
ATOM   4076 C CD  . LYS C 1 46  ? -0.277  18.916  20.343  1.00 37.92 ? 46  LYS C CD  1 
ATOM   4077 C CE  . LYS C 1 46  ? 0.678   18.612  21.484  1.00 40.46 ? 46  LYS C CE  1 
ATOM   4078 N NZ  . LYS C 1 46  ? -0.090  17.840  22.570  1.00 49.04 ? 46  LYS C NZ  1 
ATOM   4079 N N   . GLU C 1 47  ? 0.173   21.630  16.724  1.00 24.80 ? 47  GLU C N   1 
ATOM   4080 C CA  . GLU C 1 47  ? -0.564  21.398  15.488  1.00 23.44 ? 47  GLU C CA  1 
ATOM   4081 C C   . GLU C 1 47  ? -0.003  22.204  14.330  1.00 23.01 ? 47  GLU C C   1 
ATOM   4082 O O   . GLU C 1 47  ? 0.143   21.673  13.232  1.00 25.36 ? 47  GLU C O   1 
ATOM   4083 C CB  . GLU C 1 47  ? -2.058  21.711  15.647  1.00 26.86 ? 47  GLU C CB  1 
ATOM   4084 C CG  . GLU C 1 47  ? -2.786  20.805  16.625  1.00 28.44 ? 47  GLU C CG  1 
ATOM   4085 C CD  . GLU C 1 47  ? -4.243  21.188  16.811  1.00 31.40 ? 47  GLU C CD  1 
ATOM   4086 O OE1 . GLU C 1 47  ? -4.550  22.399  16.884  1.00 27.16 ? 47  GLU C OE1 1 
ATOM   4087 O OE2 . GLU C 1 47  ? -5.064  20.262  16.942  1.00 34.36 ? 47  GLU C OE2 1 
ATOM   4088 N N   . TYR C 1 48  ? 0.273   23.498  14.517  1.00 25.06 ? 48  TYR C N   1 
ATOM   4089 C CA  . TYR C 1 48  ? 0.819   24.195  13.363  1.00 24.89 ? 48  TYR C CA  1 
ATOM   4090 C C   . TYR C 1 48  ? 2.253   23.755  13.093  1.00 22.96 ? 48  TYR C C   1 
ATOM   4091 O O   . TYR C 1 48  ? 2.673   23.715  11.941  1.00 24.77 ? 48  TYR C O   1 
ATOM   4092 C CB  . TYR C 1 48  ? 0.695   25.711  13.502  1.00 25.00 ? 48  TYR C CB  1 
ATOM   4093 C CG  . TYR C 1 48  ? 1.407   26.448  14.617  1.00 26.87 ? 48  TYR C CG  1 
ATOM   4094 C CD1 . TYR C 1 48  ? 2.785   26.544  14.653  1.00 24.09 ? 48  TYR C CD1 1 
ATOM   4095 C CD2 . TYR C 1 48  ? 0.667   27.141  15.596  1.00 28.79 ? 48  TYR C CD2 1 
ATOM   4096 C CE1 . TYR C 1 48  ? 3.430   27.280  15.658  1.00 27.14 ? 48  TYR C CE1 1 
ATOM   4097 C CE2 . TYR C 1 48  ? 1.297   27.900  16.598  1.00 28.96 ? 48  TYR C CE2 1 
ATOM   4098 C CZ  . TYR C 1 48  ? 2.676   27.960  16.631  1.00 29.81 ? 48  TYR C CZ  1 
ATOM   4099 O OH  . TYR C 1 48  ? 3.328   28.695  17.610  1.00 28.89 ? 48  TYR C OH  1 
ATOM   4100 N N   . ALA C 1 49  ? 3.003   23.386  14.129  1.00 23.18 ? 49  ALA C N   1 
ATOM   4101 C CA  . ALA C 1 49  ? 4.328   22.830  13.891  1.00 25.38 ? 49  ALA C CA  1 
ATOM   4102 C C   . ALA C 1 49  ? 4.243   21.514  13.114  1.00 23.59 ? 49  ALA C C   1 
ATOM   4103 O O   . ALA C 1 49  ? 5.050   21.259  12.209  1.00 24.13 ? 49  ALA C O   1 
ATOM   4104 C CB  . ALA C 1 49  ? 5.060   22.633  15.228  1.00 24.35 ? 49  ALA C CB  1 
ATOM   4105 N N   . GLY C 1 50  ? 3.281   20.661  13.470  1.00 22.78 ? 50  GLY C N   1 
ATOM   4106 C CA  . GLY C 1 50  ? 3.093   19.410  12.746  1.00 24.70 ? 50  GLY C CA  1 
ATOM   4107 C C   . GLY C 1 50  ? 2.661   19.622  11.310  1.00 25.83 ? 50  GLY C C   1 
ATOM   4108 O O   . GLY C 1 50  ? 3.151   18.943  10.400  1.00 21.62 ? 50  GLY C O   1 
ATOM   4109 N N   . LEU C 1 51  ? 1.739   20.576  11.088  1.00 22.97 ? 51  LEU C N   1 
ATOM   4110 C CA  . LEU C 1 51  ? 1.279   20.895  9.734   1.00 22.04 ? 51  LEU C CA  1 
ATOM   4111 C C   . LEU C 1 51  ? 2.432   21.395  8.860   1.00 23.96 ? 51  LEU C C   1 
ATOM   4112 O O   . LEU C 1 51  ? 2.600   20.959  7.711   1.00 23.00 ? 51  LEU C O   1 
ATOM   4113 C CB  . LEU C 1 51  ? 0.182   21.962  9.804   1.00 21.95 ? 51  LEU C CB  1 
ATOM   4114 C CG  . LEU C 1 51  ? -0.435  22.471  8.506   1.00 22.81 ? 51  LEU C CG  1 
ATOM   4115 C CD1 . LEU C 1 51  ? -1.339  21.398  7.938   1.00 24.03 ? 51  LEU C CD1 1 
ATOM   4116 C CD2 . LEU C 1 51  ? -1.282  23.703  8.804   1.00 22.80 ? 51  LEU C CD2 1 
ATOM   4117 N N   . TYR C 1 52  ? 3.210   22.337  9.372   1.00 19.32 ? 52  TYR C N   1 
ATOM   4118 C CA  . TYR C 1 52  ? 4.302   22.878  8.565   1.00 21.00 ? 52  TYR C CA  1 
ATOM   4119 C C   . TYR C 1 52  ? 5.477   21.911  8.471   1.00 21.90 ? 52  TYR C C   1 
ATOM   4120 O O   . TYR C 1 52  ? 6.244   21.959  7.506   1.00 22.54 ? 52  TYR C O   1 
ATOM   4121 C CB  . TYR C 1 52  ? 4.741   24.239  9.112   1.00 20.46 ? 52  TYR C CB  1 
ATOM   4122 C CG  . TYR C 1 52  ? 3.793   25.322  8.626   1.00 22.73 ? 52  TYR C CG  1 
ATOM   4123 C CD1 . TYR C 1 52  ? 3.991   25.956  7.412   1.00 24.24 ? 52  TYR C CD1 1 
ATOM   4124 C CD2 . TYR C 1 52  ? 2.665   25.658  9.365   1.00 25.20 ? 52  TYR C CD2 1 
ATOM   4125 C CE1 . TYR C 1 52  ? 3.098   26.921  6.955   1.00 24.36 ? 52  TYR C CE1 1 
ATOM   4126 C CE2 . TYR C 1 52  ? 1.761   26.615  8.917   1.00 27.40 ? 52  TYR C CE2 1 
ATOM   4127 C CZ  . TYR C 1 52  ? 1.993   27.242  7.710   1.00 24.92 ? 52  TYR C CZ  1 
ATOM   4128 O OH  . TYR C 1 52  ? 1.106   28.193  7.263   1.00 25.85 ? 52  TYR C OH  1 
ATOM   4129 N N   . GLU C 1 53  ? 5.658   21.039  9.452   1.00 24.05 ? 53  GLU C N   1 
ATOM   4130 C CA  . GLU C 1 53  ? 6.628   19.966  9.267   1.00 22.31 ? 53  GLU C CA  1 
ATOM   4131 C C   . GLU C 1 53  ? 6.250   19.107  8.077   1.00 23.16 ? 53  GLU C C   1 
ATOM   4132 O O   . GLU C 1 53  ? 7.108   18.756  7.261   1.00 24.91 ? 53  GLU C O   1 
ATOM   4133 C CB  . GLU C 1 53  ? 6.742   19.119  10.528  1.00 25.23 ? 53  GLU C CB  1 
ATOM   4134 C CG  . GLU C 1 53  ? 7.806   18.035  10.453  1.00 24.77 ? 53  GLU C CG  1 
ATOM   4135 C CD  . GLU C 1 53  ? 7.694   17.095  11.629  1.00 28.27 ? 53  GLU C CD  1 
ATOM   4136 O OE1 . GLU C 1 53  ? 6.624   16.462  11.803  1.00 27.08 ? 53  GLU C OE1 1 
ATOM   4137 O OE2 . GLU C 1 53  ? 8.646   17.043  12.427  1.00 28.60 ? 53  GLU C OE2 1 
ATOM   4138 N N   . SER C 1 54  ? 4.968   18.752  7.971   1.00 23.17 ? 54  SER C N   1 
ATOM   4139 C CA  . SER C 1 54  ? 4.499   17.943  6.852   1.00 25.05 ? 54  SER C CA  1 
ATOM   4140 C C   . SER C 1 54  ? 4.665   18.680  5.532   1.00 25.26 ? 54  SER C C   1 
ATOM   4141 O O   . SER C 1 54  ? 5.160   18.112  4.548   1.00 25.43 ? 54  SER C O   1 
ATOM   4142 C CB  . SER C 1 54  ? 3.029   17.550  7.082   1.00 25.68 ? 54  SER C CB  1 
ATOM   4143 O OG  . SER C 1 54  ? 2.511   16.816  5.986   1.00 27.39 ? 54  SER C OG  1 
ATOM   4144 N N   . ARG C 1 55  ? 4.300   19.959  5.502   1.00 24.23 ? 55  ARG C N   1 
ATOM   4145 C CA  . ARG C 1 55  ? 4.517   20.766  4.314   1.00 24.93 ? 55  ARG C CA  1 
ATOM   4146 C C   . ARG C 1 55  ? 5.984   20.757  3.912   1.00 22.36 ? 55  ARG C C   1 
ATOM   4147 O O   . ARG C 1 55  ? 6.308   20.647  2.726   1.00 23.28 ? 55  ARG C O   1 
ATOM   4148 C CB  . ARG C 1 55  ? 4.026   22.206  4.579   1.00 25.38 ? 55  ARG C CB  1 
ATOM   4149 C CG  . ARG C 1 55  ? 4.289   23.196  3.457   1.00 25.90 ? 55  ARG C CG  1 
ATOM   4150 C CD  . ARG C 1 55  ? 4.207   24.648  3.942   1.00 27.06 ? 55  ARG C CD  1 
ATOM   4151 N NE  . ARG C 1 55  ? 4.052   25.596  2.838   1.00 29.36 ? 55  ARG C NE  1 
ATOM   4152 C CZ  . ARG C 1 55  ? 4.444   26.873  2.854   1.00 27.36 ? 55  ARG C CZ  1 
ATOM   4153 N NH1 . ARG C 1 55  ? 5.056   27.408  3.904   1.00 23.97 ? 55  ARG C NH1 1 
ATOM   4154 N NH2 . ARG C 1 55  ? 4.250   27.622  1.772   1.00 26.06 ? 55  ARG C NH2 1 
ATOM   4155 N N   . ASN C 1 56  ? 6.884   20.880  4.892   1.00 23.39 ? 56  ASN C N   1 
ATOM   4156 C CA  . ASN C 1 56  ? 8.307   20.994  4.602   1.00 23.36 ? 56  ASN C CA  1 
ATOM   4157 C C   . ASN C 1 56  ? 8.907   19.677  4.126   1.00 24.40 ? 56  ASN C C   1 
ATOM   4158 O O   . ASN C 1 56  ? 9.853   19.694  3.327   1.00 23.68 ? 56  ASN C O   1 
ATOM   4159 C CB  . ASN C 1 56  ? 9.063   21.490  5.838   1.00 22.44 ? 56  ASN C CB  1 
ATOM   4160 C CG  . ASN C 1 56  ? 8.797   22.947  6.130   1.00 23.28 ? 56  ASN C CG  1 
ATOM   4161 O OD1 . ASN C 1 56  ? 8.283   23.646  5.282   1.00 20.43 ? 56  ASN C OD1 1 
ATOM   4162 N ND2 . ASN C 1 56  ? 9.155   23.405  7.326   1.00 19.39 ? 56  ASN C ND2 1 
ATOM   4163 N N   . ILE C 1 57  ? 8.390   18.529  4.595   1.00 23.67 ? 57  ILE C N   1 
ATOM   4164 C CA  . ILE C 1 57  ? 8.865   17.234  4.077   1.00 23.98 ? 57  ILE C CA  1 
ATOM   4165 C C   . ILE C 1 57  ? 8.628   17.145  2.578   1.00 25.31 ? 57  ILE C C   1 
ATOM   4166 O O   . ILE C 1 57  ? 9.537   16.826  1.797   1.00 25.70 ? 57  ILE C O   1 
ATOM   4167 C CB  . ILE C 1 57  ? 8.174   16.067  4.815   1.00 24.84 ? 57  ILE C CB  1 
ATOM   4168 C CG1 . ILE C 1 57  ? 8.614   16.043  6.283   1.00 26.59 ? 57  ILE C CG1 1 
ATOM   4169 C CG2 . ILE C 1 57  ? 8.403   14.727  4.086   1.00 26.15 ? 57  ILE C CG2 1 
ATOM   4170 C CD1 . ILE C 1 57  ? 8.086   14.884  7.107   1.00 28.46 ? 57  ILE C CD1 1 
ATOM   4171 N N   . PHE C 1 58  ? 7.395   17.423  2.157   1.00 22.95 ? 58  PHE C N   1 
ATOM   4172 C CA  . PHE C 1 58  ? 7.059   17.399  0.737   1.00 25.56 ? 58  PHE C CA  1 
ATOM   4173 C C   . PHE C 1 58  ? 7.918   18.382  -0.037  1.00 25.55 ? 58  PHE C C   1 
ATOM   4174 O O   . PHE C 1 58  ? 8.426   18.057  -1.114  1.00 22.73 ? 58  PHE C O   1 
ATOM   4175 C CB  . PHE C 1 58  ? 5.585   17.742  0.527   1.00 26.97 ? 58  PHE C CB  1 
ATOM   4176 C CG  . PHE C 1 58  ? 5.128   17.579  -0.897  1.00 28.53 ? 58  PHE C CG  1 
ATOM   4177 C CD1 . PHE C 1 58  ? 5.396   18.563  -1.853  1.00 26.88 ? 58  PHE C CD1 1 
ATOM   4178 C CD2 . PHE C 1 58  ? 4.444   16.432  -1.290  1.00 29.76 ? 58  PHE C CD2 1 
ATOM   4179 C CE1 . PHE C 1 58  ? 4.997   18.403  -3.173  1.00 28.58 ? 58  PHE C CE1 1 
ATOM   4180 C CE2 . PHE C 1 58  ? 4.026   16.281  -2.593  1.00 32.53 ? 58  PHE C CE2 1 
ATOM   4181 C CZ  . PHE C 1 58  ? 4.307   17.260  -3.540  1.00 32.74 ? 58  PHE C CZ  1 
ATOM   4182 N N   . TRP C 1 59  ? 8.042   19.609  0.481   1.00 25.10 ? 59  TRP C N   1 
ATOM   4183 C CA  . TRP C 1 59  ? 8.790   20.652  -0.219  1.00 23.88 ? 59  TRP C CA  1 
ATOM   4184 C C   . TRP C 1 59  ? 10.243  20.249  -0.426  1.00 25.98 ? 59  TRP C C   1 
ATOM   4185 O O   . TRP C 1 59  ? 10.793  20.407  -1.518  1.00 29.84 ? 59  TRP C O   1 
ATOM   4186 C CB  . TRP C 1 59  ? 8.721   21.937  0.579   1.00 25.00 ? 59  TRP C CB  1 
ATOM   4187 C CG  . TRP C 1 59  ? 8.843   23.202  -0.232  1.00 30.90 ? 59  TRP C CG  1 
ATOM   4188 C CD1 . TRP C 1 59  ? 9.401   23.353  -1.476  1.00 28.21 ? 59  TRP C CD1 1 
ATOM   4189 C CD2 . TRP C 1 59  ? 8.381   24.499  0.168   1.00 26.42 ? 59  TRP C CD2 1 
ATOM   4190 N NE1 . TRP C 1 59  ? 9.310   24.683  -1.867  1.00 26.36 ? 59  TRP C NE1 1 
ATOM   4191 C CE2 . TRP C 1 59  ? 8.684   25.394  -0.876  1.00 27.98 ? 59  TRP C CE2 1 
ATOM   4192 C CE3 . TRP C 1 59  ? 7.751   24.986  1.313   1.00 25.29 ? 59  TRP C CE3 1 
ATOM   4193 C CZ2 . TRP C 1 59  ? 8.382   26.756  -0.799  1.00 28.38 ? 59  TRP C CZ2 1 
ATOM   4194 C CZ3 . TRP C 1 59  ? 7.458   26.328  1.384   1.00 27.91 ? 59  TRP C CZ3 1 
ATOM   4195 C CH2 . TRP C 1 59  ? 7.766   27.196  0.330   1.00 26.81 ? 59  TRP C CH2 1 
ATOM   4196 N N   . ILE C 1 60  ? 10.893  19.758  0.627   1.00 24.79 ? 60  ILE C N   1 
ATOM   4197 C CA  . ILE C 1 60  ? 12.304  19.413  0.531   1.00 27.49 ? 60  ILE C CA  1 
ATOM   4198 C C   . ILE C 1 60  ? 12.497  18.191  -0.355  1.00 28.67 ? 60  ILE C C   1 
ATOM   4199 O O   . ILE C 1 60  ? 13.385  18.139  -1.202  1.00 27.69 ? 60  ILE C O   1 
ATOM   4200 C CB  . ILE C 1 60  ? 12.897  19.175  1.932   1.00 28.52 ? 60  ILE C CB  1 
ATOM   4201 C CG1 . ILE C 1 60  ? 12.935  20.500  2.701   1.00 25.65 ? 60  ILE C CG1 1 
ATOM   4202 C CG2 . ILE C 1 60  ? 14.333  18.533  1.792   1.00 28.90 ? 60  ILE C CG2 1 
ATOM   4203 C CD1 . ILE C 1 60  ? 13.089  20.341  4.180   1.00 23.54 ? 60  ILE C CD1 1 
ATOM   4204 N N   . LYS C 1 61  ? 11.682  17.177  -0.158  1.00 30.17 ? 61  LYS C N   1 
ATOM   4205 C CA  . LYS C 1 61  ? 11.895  15.960  -0.914  1.00 28.52 ? 61  LYS C CA  1 
ATOM   4206 C C   . LYS C 1 61  ? 11.508  16.123  -2.397  1.00 28.71 ? 61  LYS C C   1 
ATOM   4207 O O   . LYS C 1 61  ? 12.133  15.514  -3.261  1.00 26.63 ? 61  LYS C O   1 
ATOM   4208 C CB  . LYS C 1 61  ? 11.223  14.842  -0.136  1.00 28.69 ? 61  LYS C CB  1 
ATOM   4209 C CG  . LYS C 1 61  ? 11.231  13.538  -0.806  1.00 39.64 ? 61  LYS C CG  1 
ATOM   4210 C CD  . LYS C 1 61  ? 12.367  12.574  -0.539  1.00 36.81 ? 61  LYS C CD  1 
ATOM   4211 C CE  . LYS C 1 61  ? 12.023  11.217  -1.221  1.00 37.80 ? 61  LYS C CE  1 
ATOM   4212 N NZ  . LYS C 1 61  ? 12.464  9.903   -0.468  1.00 24.98 ? 61  LYS C NZ  1 
ATOM   4213 N N   . ASN C 1 62  ? 10.510  16.959  -2.732  1.00 26.16 ? 62  ASN C N   1 
ATOM   4214 C CA  . ASN C 1 62  ? 10.066  17.095  -4.127  1.00 27.99 ? 62  ASN C CA  1 
ATOM   4215 C C   . ASN C 1 62  ? 10.547  18.362  -4.840  1.00 30.12 ? 62  ASN C C   1 
ATOM   4216 O O   . ASN C 1 62  ? 10.304  18.497  -6.041  1.00 29.03 ? 62  ASN C O   1 
ATOM   4217 C CB  . ASN C 1 62  ? 8.534   17.031  -4.217  1.00 26.61 ? 62  ASN C CB  1 
ATOM   4218 C CG  . ASN C 1 62  ? 8.000   15.668  -3.858  1.00 32.68 ? 62  ASN C CG  1 
ATOM   4219 O OD1 . ASN C 1 62  ? 8.296   14.703  -4.548  1.00 35.12 ? 62  ASN C OD1 1 
ATOM   4220 N ND2 . ASN C 1 62  ? 7.223   15.573  -2.799  1.00 29.72 ? 62  ASN C ND2 1 
ATOM   4221 N N   . GLY C 1 63  ? 11.177  19.305  -4.150  1.00 27.26 ? 63  GLY C N   1 
ATOM   4222 C CA  . GLY C 1 63  ? 11.630  20.514  -4.816  1.00 28.12 ? 63  GLY C CA  1 
ATOM   4223 C C   . GLY C 1 63  ? 10.529  21.497  -5.151  1.00 32.53 ? 63  GLY C C   1 
ATOM   4224 O O   . GLY C 1 63  ? 10.791  22.493  -5.831  1.00 30.62 ? 63  GLY C O   1 
ATOM   4225 N N   . ARG C 1 64  ? 9.328   21.223  -4.655  1.00 29.16 ? 64  ARG C N   1 
ATOM   4226 C CA  . ARG C 1 64  ? 8.206   22.144  -4.901  1.00 30.43 ? 64  ARG C CA  1 
ATOM   4227 C C   . ARG C 1 64  ? 7.196   22.058  -3.759  1.00 28.95 ? 64  ARG C C   1 
ATOM   4228 O O   . ARG C 1 64  ? 7.060   21.019  -3.173  1.00 27.99 ? 64  ARG C O   1 
ATOM   4229 C CB  . ARG C 1 64  ? 7.560   21.827  -6.245  1.00 34.29 ? 64  ARG C CB  1 
ATOM   4230 C CG  . ARG C 1 64  ? 6.876   20.475  -6.278  1.00 37.52 ? 64  ARG C CG  1 
ATOM   4231 C CD  . ARG C 1 64  ? 5.914   20.376  -7.432  1.00 43.92 ? 64  ARG C CD  1 
ATOM   4232 N NE  . ARG C 1 64  ? 5.039   19.226  -7.383  1.00 49.86 ? 64  ARG C NE  1 
ATOM   4233 C CZ  . ARG C 1 64  ? 5.438   17.991  -7.644  1.00 51.01 ? 64  ARG C CZ  1 
ATOM   4234 N NH1 . ARG C 1 64  ? 6.706   17.764  -7.923  1.00 48.71 ? 64  ARG C NH1 1 
ATOM   4235 N NH2 . ARG C 1 64  ? 4.580   16.988  -7.635  1.00 52.33 ? 64  ARG C NH2 1 
ATOM   4236 N N   . GLU C 1 65  ? 6.506   23.155  -3.500  1.00 28.35 ? 65  GLU C N   1 
ATOM   4237 C CA  . GLU C 1 65  ? 5.515   23.278  -2.447  1.00 28.93 ? 65  GLU C CA  1 
ATOM   4238 C C   . GLU C 1 65  ? 4.344   22.336  -2.721  1.00 28.99 ? 65  GLU C C   1 
ATOM   4239 O O   . GLU C 1 65  ? 3.944   22.177  -3.873  1.00 29.46 ? 65  GLU C O   1 
ATOM   4240 C CB  . GLU C 1 65  ? 5.054   24.742  -2.430  1.00 30.47 ? 65  GLU C CB  1 
ATOM   4241 C CG  . GLU C 1 65  ? 4.673   25.277  -1.147  1.00 34.73 ? 65  GLU C CG  1 
ATOM   4242 C CD  . GLU C 1 65  ? 4.143   26.673  -1.294  1.00 34.23 ? 65  GLU C CD  1 
ATOM   4243 O OE1 . GLU C 1 65  ? 4.601   27.400  -2.207  1.00 38.99 ? 65  GLU C OE1 1 
ATOM   4244 O OE2 . GLU C 1 65  ? 3.258   27.035  -0.513  1.00 37.72 ? 65  GLU C OE2 1 
ATOM   4245 N N   . PRO C 1 66  ? 3.757   21.711  -1.693  1.00 26.17 ? 66  PRO C N   1 
ATOM   4246 C CA  . PRO C 1 66  ? 2.522   20.948  -1.898  1.00 27.36 ? 66  PRO C CA  1 
ATOM   4247 C C   . PRO C 1 66  ? 1.338   21.870  -2.167  1.00 29.28 ? 66  PRO C C   1 
ATOM   4248 O O   . PRO C 1 66  ? 1.265   22.975  -1.643  1.00 28.78 ? 66  PRO C O   1 
ATOM   4249 C CB  . PRO C 1 66  ? 2.332   20.225  -0.556  1.00 29.05 ? 66  PRO C CB  1 
ATOM   4250 C CG  . PRO C 1 66  ? 3.031   21.074  0.420   1.00 26.20 ? 66  PRO C CG  1 
ATOM   4251 C CD  . PRO C 1 66  ? 4.245   21.589  -0.310  1.00 25.53 ? 66  PRO C CD  1 
ATOM   4252 N N   . ASN C 1 67  ? 0.381   21.381  -2.962  1.00 28.37 ? 67  ASN C N   1 
ATOM   4253 C CA  . ASN C 1 67  ? -0.841  22.137  -3.236  1.00 33.83 ? 67  ASN C CA  1 
ATOM   4254 C C   . ASN C 1 67  ? -1.742  22.221  -2.011  1.00 32.90 ? 67  ASN C C   1 
ATOM   4255 O O   . ASN C 1 67  ? -2.529  23.164  -1.878  1.00 31.77 ? 67  ASN C O   1 
ATOM   4256 C CB  . ASN C 1 67  ? -1.599  21.505  -4.400  1.00 34.56 ? 67  ASN C CB  1 
ATOM   4257 C CG  . ASN C 1 67  ? -0.924  21.754  -5.723  1.00 38.55 ? 67  ASN C CG  1 
ATOM   4258 O OD1 . ASN C 1 67  ? -0.115  22.674  -5.851  1.00 45.08 ? 67  ASN C OD1 1 
ATOM   4259 N ND2 . ASN C 1 67  ? -1.214  20.914  -6.708  1.00 44.81 ? 67  ASN C ND2 1 
ATOM   4260 N N   . TYR C 1 68  ? -1.641  21.255  -1.111  1.00 31.95 ? 68  TYR C N   1 
ATOM   4261 C CA  . TYR C 1 68  ? -2.337  21.306  0.162   1.00 29.21 ? 68  TYR C CA  1 
ATOM   4262 C C   . TYR C 1 68  ? -1.652  20.339  1.113   1.00 30.19 ? 68  TYR C C   1 
ATOM   4263 O O   . TYR C 1 68  ? -0.910  19.445  0.696   1.00 29.28 ? 68  TYR C O   1 
ATOM   4264 C CB  . TYR C 1 68  ? -3.827  20.948  0.019   1.00 34.56 ? 68  TYR C CB  1 
ATOM   4265 C CG  . TYR C 1 68  ? -4.070  19.512  -0.407  1.00 32.28 ? 68  TYR C CG  1 
ATOM   4266 C CD1 . TYR C 1 68  ? -4.151  19.174  -1.737  1.00 35.03 ? 68  TYR C CD1 1 
ATOM   4267 C CD2 . TYR C 1 68  ? -4.194  18.500  0.536   1.00 34.61 ? 68  TYR C CD2 1 
ATOM   4268 C CE1 . TYR C 1 68  ? -4.370  17.853  -2.130  1.00 41.58 ? 68  TYR C CE1 1 
ATOM   4269 C CE2 . TYR C 1 68  ? -4.408  17.179  0.157   1.00 39.44 ? 68  TYR C CE2 1 
ATOM   4270 C CZ  . TYR C 1 68  ? -4.485  16.865  -1.178  1.00 41.86 ? 68  TYR C CZ  1 
ATOM   4271 O OH  . TYR C 1 68  ? -4.696  15.561  -1.553  1.00 41.95 ? 68  TYR C OH  1 
ATOM   4272 N N   . VAL C 1 69  ? -1.922  20.518  2.401   1.00 27.53 ? 69  VAL C N   1 
ATOM   4273 C CA  . VAL C 1 69  ? -1.402  19.628  3.428   1.00 26.58 ? 69  VAL C CA  1 
ATOM   4274 C C   . VAL C 1 69  ? -2.553  19.268  4.355   1.00 30.61 ? 69  VAL C C   1 
ATOM   4275 O O   . VAL C 1 69  ? -3.292  20.151  4.802   1.00 26.48 ? 69  VAL C O   1 
ATOM   4276 C CB  . VAL C 1 69  ? -0.236  20.258  4.210   1.00 24.97 ? 69  VAL C CB  1 
ATOM   4277 C CG1 . VAL C 1 69  ? 0.252   19.290  5.294   1.00 26.24 ? 69  VAL C CG1 1 
ATOM   4278 C CG2 . VAL C 1 69  ? 0.897   20.606  3.252   1.00 26.01 ? 69  VAL C CG2 1 
ATOM   4279 N N   . THR C 1 70  ? -2.751  17.968  4.575   1.00 27.20 ? 70  THR C N   1 
ATOM   4280 C CA  . THR C 1 70  ? -3.753  17.499  5.522   1.00 27.08 ? 70  THR C CA  1 
ATOM   4281 C C   . THR C 1 70  ? -3.136  17.504  6.914   1.00 27.43 ? 70  THR C C   1 
ATOM   4282 O O   . THR C 1 70  ? -1.984  17.130  7.082   1.00 29.28 ? 70  THR C O   1 
ATOM   4283 C CB  . THR C 1 70  ? -4.222  16.088  5.129   1.00 29.70 ? 70  THR C CB  1 
ATOM   4284 O OG1 . THR C 1 70  ? -4.714  16.133  3.784   1.00 30.27 ? 70  THR C OG1 1 
ATOM   4285 C CG2 . THR C 1 70  ? -5.351  15.573  6.063   1.00 32.43 ? 70  THR C CG2 1 
ATOM   4286 N N   . LEU C 1 71  ? -3.880  17.980  7.905   1.00 26.24 ? 71  LEU C N   1 
ATOM   4287 C CA  . LEU C 1 71  ? -3.402  17.941  9.291   1.00 27.28 ? 71  LEU C CA  1 
ATOM   4288 C C   . LEU C 1 71  ? -3.448  16.504  9.809   1.00 29.16 ? 71  LEU C C   1 
ATOM   4289 O O   . LEU C 1 71  ? -4.532  15.988  10.078  1.00 31.30 ? 71  LEU C O   1 
ATOM   4290 C CB  . LEU C 1 71  ? -4.271  18.843  10.166  1.00 30.38 ? 71  LEU C CB  1 
ATOM   4291 C CG  . LEU C 1 71  ? -3.895  18.999  11.648  1.00 31.49 ? 71  LEU C CG  1 
ATOM   4292 C CD1 . LEU C 1 71  ? -2.398  19.254  11.843  1.00 27.88 ? 71  LEU C CD1 1 
ATOM   4293 C CD2 . LEU C 1 71  ? -4.754  20.028  12.369  1.00 35.36 ? 71  LEU C CD2 1 
ATOM   4294 N N   . THR C 1 72  ? -2.287  15.842  9.935   1.00 27.99 ? 72  THR C N   1 
ATOM   4295 C CA  . THR C 1 72  ? -2.229  14.441  10.357  1.00 31.24 ? 72  THR C CA  1 
ATOM   4296 C C   . THR C 1 72  ? -1.366  14.182  11.590  1.00 29.63 ? 72  THR C C   1 
ATOM   4297 O O   . THR C 1 72  ? -1.364  13.050  12.103  1.00 27.91 ? 72  THR C O   1 
ATOM   4298 C CB  . THR C 1 72  ? -1.717  13.552  9.210   1.00 28.63 ? 72  THR C CB  1 
ATOM   4299 O OG1 . THR C 1 72  ? -0.410  13.973  8.798   1.00 30.26 ? 72  THR C OG1 1 
ATOM   4300 C CG2 . THR C 1 72  ? -2.661  13.641  8.030   1.00 32.41 ? 72  THR C CG2 1 
ATOM   4301 N N   . SER C 1 73  ? -0.611  15.169  12.054  1.00 28.61 ? 73  SER C N   1 
ATOM   4302 C CA  . SER C 1 73  ? 0.475   14.927  12.983  1.00 26.99 ? 73  SER C CA  1 
ATOM   4303 C C   . SER C 1 73  ? 0.624   16.139  13.884  1.00 31.42 ? 73  SER C C   1 
ATOM   4304 O O   . SER C 1 73  ? -0.044  17.161  13.702  1.00 31.98 ? 73  SER C O   1 
ATOM   4305 C CB  . SER C 1 73  ? 1.777   14.671  12.220  1.00 30.71 ? 73  SER C CB  1 
ATOM   4306 O OG  . SER C 1 73  ? 2.058   15.808  11.404  1.00 33.50 ? 73  SER C OG  1 
ATOM   4307 N N   . VAL C 1 74  ? 1.446   15.977  14.918  1.00 29.08 ? 74  VAL C N   1 
ATOM   4308 C CA  . VAL C 1 74  ? 1.914   17.073  15.756  1.00 26.41 ? 74  VAL C CA  1 
ATOM   4309 C C   . VAL C 1 74  ? 3.443   17.026  15.790  1.00 25.29 ? 74  VAL C C   1 
ATOM   4310 O O   . VAL C 1 74  ? 4.059   15.998  15.510  1.00 25.50 ? 74  VAL C O   1 
ATOM   4311 C CB  . VAL C 1 74  ? 1.318   17.000  17.176  1.00 30.05 ? 74  VAL C CB  1 
ATOM   4312 C CG1 . VAL C 1 74  ? -0.226  16.972  17.123  1.00 27.54 ? 74  VAL C CG1 1 
ATOM   4313 C CG2 . VAL C 1 74  ? 1.806   15.740  17.841  1.00 29.97 ? 74  VAL C CG2 1 
ATOM   4314 N N   . ALA C 1 75  ? 4.062   18.151  16.146  1.00 24.97 ? 75  ALA C N   1 
ATOM   4315 C CA  . ALA C 1 75  ? 5.519   18.203  16.239  1.00 26.97 ? 75  ALA C CA  1 
ATOM   4316 C C   . ALA C 1 75  ? 5.907   19.340  17.165  1.00 25.29 ? 75  ALA C C   1 
ATOM   4317 O O   . ALA C 1 75  ? 5.094   20.208  17.477  1.00 25.22 ? 75  ALA C O   1 
ATOM   4318 C CB  . ALA C 1 75  ? 6.189   18.399  14.871  1.00 24.46 ? 75  ALA C CB  1 
ATOM   4319 N N   . ARG C 1 76  ? 7.161   19.304  17.619  1.00 25.73 ? 76  ARG C N   1 
ATOM   4320 C CA  . ARG C 1 76  ? 7.718   20.330  18.488  1.00 28.76 ? 76  ARG C CA  1 
ATOM   4321 C C   . ARG C 1 76  ? 8.167   21.566  17.725  1.00 26.34 ? 76  ARG C C   1 
ATOM   4322 O O   . ARG C 1 76  ? 8.360   22.614  18.342  1.00 25.67 ? 76  ARG C O   1 
ATOM   4323 C CB  . ARG C 1 76  ? 8.911   19.796  19.290  1.00 31.53 ? 76  ARG C CB  1 
ATOM   4324 C CG  . ARG C 1 76  ? 8.659   18.552  20.124  1.00 36.94 ? 76  ARG C CG  1 
ATOM   4325 C CD  . ARG C 1 76  ? 10.019  18.000  20.631  1.00 45.16 ? 76  ARG C CD  1 
ATOM   4326 N NE  . ARG C 1 76  ? 10.930  19.090  20.982  1.00 49.69 ? 76  ARG C NE  1 
ATOM   4327 C CZ  . ARG C 1 76  ? 12.234  19.125  20.717  1.00 47.28 ? 76  ARG C CZ  1 
ATOM   4328 N NH1 . ARG C 1 76  ? 12.850  18.120  20.109  1.00 41.18 ? 76  ARG C NH1 1 
ATOM   4329 N NH2 . ARG C 1 76  ? 12.939  20.199  21.071  1.00 44.32 ? 76  ARG C NH2 1 
ATOM   4330 N N   . ASN C 1 77  ? 8.438   21.422  16.434  1.00 24.17 ? 77  ASN C N   1 
ATOM   4331 C CA  . ASN C 1 77  ? 8.836   22.515  15.563  1.00 24.67 ? 77  ASN C CA  1 
ATOM   4332 C C   . ASN C 1 77  ? 8.669   22.017  14.138  1.00 22.69 ? 77  ASN C C   1 
ATOM   4333 O O   . ASN C 1 77  ? 8.408   20.821  13.921  1.00 23.61 ? 77  ASN C O   1 
ATOM   4334 C CB  . ASN C 1 77  ? 10.278  22.969  15.851  1.00 24.94 ? 77  ASN C CB  1 
ATOM   4335 C CG  . ASN C 1 77  ? 11.293  21.849  15.622  1.00 27.21 ? 77  ASN C CG  1 
ATOM   4336 O OD1 . ASN C 1 77  ? 11.310  21.215  14.565  1.00 24.61 ? 77  ASN C OD1 1 
ATOM   4337 N ND2 . ASN C 1 77  ? 12.109  21.586  16.620  1.00 29.51 ? 77  ASN C ND2 1 
ATOM   4338 N N   . PRO C 1 78  ? 8.740   22.898  13.145  1.00 24.96 ? 78  PRO C N   1 
ATOM   4339 C CA  . PRO C 1 78  ? 8.520   22.441  11.767  1.00 21.94 ? 78  PRO C CA  1 
ATOM   4340 C C   . PRO C 1 78  ? 9.771   21.922  11.076  1.00 22.07 ? 78  PRO C C   1 
ATOM   4341 O O   . PRO C 1 78  ? 9.709   21.641  9.878   1.00 21.97 ? 78  PRO C O   1 
ATOM   4342 C CB  . PRO C 1 78  ? 8.015   23.718  11.079  1.00 22.69 ? 78  PRO C CB  1 
ATOM   4343 C CG  . PRO C 1 78  ? 8.743   24.829  11.805  1.00 21.18 ? 78  PRO C CG  1 
ATOM   4344 C CD  . PRO C 1 78  ? 8.905   24.375  13.223  1.00 21.34 ? 78  PRO C CD  1 
ATOM   4345 N N   . LEU C 1 79  ? 10.881  21.785  11.795  1.00 21.54 ? 79  LEU C N   1 
ATOM   4346 C CA  . LEU C 1 79  ? 12.170  21.491  11.164  1.00 23.46 ? 79  LEU C CA  1 
ATOM   4347 C C   . LEU C 1 79  ? 12.192  20.079  10.573  1.00 23.66 ? 79  LEU C C   1 
ATOM   4348 O O   . LEU C 1 79  ? 11.764  19.107  11.211  1.00 23.58 ? 79  LEU C O   1 
ATOM   4349 C CB  . LEU C 1 79  ? 13.299  21.633  12.188  1.00 23.32 ? 79  LEU C CB  1 
ATOM   4350 C CG  . LEU C 1 79  ? 14.732  21.343  11.694  1.00 25.54 ? 79  LEU C CG  1 
ATOM   4351 C CD1 . LEU C 1 79  ? 15.165  22.397  10.702  1.00 24.60 ? 79  LEU C CD1 1 
ATOM   4352 C CD2 . LEU C 1 79  ? 15.688  21.280  12.902  1.00 26.92 ? 79  LEU C CD2 1 
ATOM   4353 N N   . VAL C 1 80  ? 12.701  19.975  9.340   1.00 22.31 ? 80  VAL C N   1 
ATOM   4354 C CA  . VAL C 1 80  ? 12.870  18.711  8.611   1.00 22.16 ? 80  VAL C CA  1 
ATOM   4355 C C   . VAL C 1 80  ? 14.340  18.624  8.203   1.00 23.89 ? 80  VAL C C   1 
ATOM   4356 O O   . VAL C 1 80  ? 14.868  19.577  7.622   1.00 23.79 ? 80  VAL C O   1 
ATOM   4357 C CB  . VAL C 1 80  ? 11.946  18.677  7.368   1.00 24.48 ? 80  VAL C CB  1 
ATOM   4358 C CG1 . VAL C 1 80  ? 12.267  17.496  6.410   1.00 23.69 ? 80  VAL C CG1 1 
ATOM   4359 C CG2 . VAL C 1 80  ? 10.438  18.681  7.765   1.00 22.82 ? 80  VAL C CG2 1 
ATOM   4360 N N   . MET C 1 81  ? 15.017  17.522  8.551   1.00 22.34 ? 81  MET C N   1 
ATOM   4361 C CA  . MET C 1 81  ? 16.427  17.399  8.174   1.00 23.92 ? 81  MET C CA  1 
ATOM   4362 C C   . MET C 1 81  ? 16.633  17.588  6.687   1.00 20.50 ? 81  MET C C   1 
ATOM   4363 O O   . MET C 1 81  ? 15.904  17.062  5.858   1.00 22.64 ? 81  MET C O   1 
ATOM   4364 C CB  . MET C 1 81  ? 17.013  16.050  8.605   1.00 29.72 ? 81  MET C CB  1 
ATOM   4365 C CG  . MET C 1 81  ? 18.579  16.007  8.691   1.00 29.97 ? 81  MET C CG  1 
ATOM   4366 S SD  . MET C 1 81  ? 19.426  17.558  9.106   1.00 31.35 ? 81  MET C SD  1 
ATOM   4367 C CE  . MET C 1 81  ? 21.114  17.198  8.640   1.00 31.85 ? 81  MET C CE  1 
ATOM   4368 N N   . ASP C 1 82  ? 17.648  18.364  6.352   1.00 25.15 ? 82  ASP C N   1 
ATOM   4369 C CA  . ASP C 1 82  ? 17.974  18.658  4.971   1.00 25.37 ? 82  ASP C CA  1 
ATOM   4370 C C   . ASP C 1 82  ? 19.492  18.649  4.870   1.00 24.99 ? 82  ASP C C   1 
ATOM   4371 O O   . ASP C 1 82  ? 20.168  19.371  5.592   1.00 26.39 ? 82  ASP C O   1 
ATOM   4372 C CB  . ASP C 1 82  ? 17.379  20.004  4.549   1.00 26.38 ? 82  ASP C CB  1 
ATOM   4373 C CG  . ASP C 1 82  ? 17.515  20.264  3.072   1.00 25.93 ? 82  ASP C CG  1 
ATOM   4374 O OD1 . ASP C 1 82  ? 17.708  19.305  2.288   1.00 26.56 ? 82  ASP C OD1 1 
ATOM   4375 O OD2 . ASP C 1 82  ? 17.432  21.443  2.696   1.00 26.78 ? 82  ASP C OD2 1 
ATOM   4376 N N   . TYR C 1 83  ? 20.022  17.762  4.062   1.00 32.16 ? 83  TYR C N   1 
ATOM   4377 C CA  . TYR C 1 83  ? 21.461  17.600  3.958   1.00 30.63 ? 83  TYR C CA  1 
ATOM   4378 C C   . TYR C 1 83  ? 21.991  18.493  2.844   1.00 28.83 ? 83  TYR C C   1 
ATOM   4379 O O   . TYR C 1 83  ? 21.266  18.804  1.907   1.00 36.34 ? 83  TYR C O   1 
ATOM   4380 C CB  . TYR C 1 83  ? 21.777  16.111  3.718   1.00 27.84 ? 83  TYR C CB  1 
ATOM   4381 C CG  . TYR C 1 83  ? 21.195  15.129  4.736   1.00 29.79 ? 83  TYR C CG  1 
ATOM   4382 C CD1 . TYR C 1 83  ? 21.900  14.804  5.873   1.00 31.78 ? 83  TYR C CD1 1 
ATOM   4383 C CD2 . TYR C 1 83  ? 19.973  14.478  4.529   1.00 30.33 ? 83  TYR C CD2 1 
ATOM   4384 C CE1 . TYR C 1 83  ? 21.410  13.891  6.810   1.00 31.43 ? 83  TYR C CE1 1 
ATOM   4385 C CE2 . TYR C 1 83  ? 19.458  13.552  5.474   1.00 31.10 ? 83  TYR C CE2 1 
ATOM   4386 C CZ  . TYR C 1 83  ? 20.197  13.263  6.614   1.00 35.13 ? 83  TYR C CZ  1 
ATOM   4387 O OH  . TYR C 1 83  ? 19.784  12.348  7.590   1.00 34.64 ? 83  TYR C OH  1 
ATOM   4388 N N   . GLN C 1 84  ? 23.264  18.854  2.953   1.00 26.91 ? 84  GLN C N   1 
ATOM   4389 C CA  . GLN C 1 84  ? 23.923  19.668  1.916   1.00 30.96 ? 84  GLN C CA  1 
ATOM   4390 C C   . GLN C 1 84  ? 24.062  18.794  0.678   1.00 36.20 ? 84  GLN C C   1 
ATOM   4391 O O   . GLN C 1 84  ? 24.333  17.622  0.832   1.00 31.46 ? 84  GLN C O   1 
ATOM   4392 C CB  . GLN C 1 84  ? 25.252  20.216  2.417   1.00 29.16 ? 84  GLN C CB  1 
ATOM   4393 C CG  . GLN C 1 84  ? 26.312  19.171  2.702   1.00 27.68 ? 84  GLN C CG  1 
ATOM   4394 C CD  . GLN C 1 84  ? 27.474  19.789  3.435   1.00 30.17 ? 84  GLN C CD  1 
ATOM   4395 O OE1 . GLN C 1 84  ? 27.454  19.945  4.636   1.00 32.42 ? 84  GLN C OE1 1 
ATOM   4396 N NE2 . GLN C 1 84  ? 28.483  20.193  2.703   1.00 34.56 ? 84  GLN C NE2 1 
ATOM   4397 N N   . ASN C 1 85  ? 23.813  19.386  -0.482  1.00 36.34 ? 85  ASN C N   1 
ATOM   4398 C CA  . ASN C 1 85  ? 23.818  18.630  -1.756  1.00 37.59 ? 85  ASN C CA  1 
ATOM   4399 C C   . ASN C 1 85  ? 25.210  18.630  -2.401  1.00 39.82 ? 85  ASN C C   1 
ATOM   4400 O O   . ASN C 1 85  ? 25.347  18.016  -3.428  1.00 42.19 ? 85  ASN C O   1 
ATOM   4401 C CB  . ASN C 1 85  ? 22.706  19.112  -2.692  1.00 45.24 ? 85  ASN C CB  1 
ATOM   4402 C CG  . ASN C 1 85  ? 21.299  19.126  -2.113  1.00 47.03 ? 85  ASN C CG  1 
ATOM   4403 O OD1 . ASN C 1 85  ? 20.865  18.221  -1.401  1.00 50.36 ? 85  ASN C OD1 1 
ATOM   4404 N ND2 . ASN C 1 85  ? 20.540  20.142  -2.475  1.00 49.32 ? 85  ASN C ND2 1 
ATOM   4405 N N   . THR C 1 86  ? 26.181  19.348  -1.831  1.00 33.82 ? 86  THR C N   1 
ATOM   4406 C CA  . THR C 1 86  ? 27.572  19.459  -2.322  1.00 36.06 ? 86  THR C CA  1 
ATOM   4407 C C   . THR C 1 86  ? 28.500  19.458  -1.105  1.00 35.99 ? 86  THR C C   1 
ATOM   4408 O O   . THR C 1 86  ? 28.027  19.559  0.008   1.00 32.41 ? 86  THR C O   1 
ATOM   4409 C CB  . THR C 1 86  ? 27.844  20.714  -3.155  1.00 40.52 ? 86  THR C CB  1 
ATOM   4410 O OG1 . THR C 1 86  ? 28.081  21.792  -2.260  1.00 38.54 ? 86  THR C OG1 1 
ATOM   4411 C CG2 . THR C 1 86  ? 26.741  21.081  -4.117  1.00 40.00 ? 86  THR C CG2 1 
ATOM   4412 N N   . ASN C 1 87  ? 29.797  19.363  -1.327  1.00 35.17 ? 87  ASN C N   1 
ATOM   4413 C CA  . ASN C 1 87  ? 30.716  19.369  -0.173  1.00 36.29 ? 87  ASN C CA  1 
ATOM   4414 C C   . ASN C 1 87  ? 31.041  20.821  0.182   1.00 34.43 ? 87  ASN C C   1 
ATOM   4415 O O   . ASN C 1 87  ? 31.842  21.010  1.062   1.00 35.08 ? 87  ASN C O   1 
ATOM   4416 C CB  . ASN C 1 87  ? 31.984  18.595  -0.493  1.00 38.08 ? 87  ASN C CB  1 
ATOM   4417 C CG  . ASN C 1 87  ? 32.478  19.010  -1.849  1.00 41.25 ? 87  ASN C CG  1 
ATOM   4418 O OD1 . ASN C 1 87  ? 32.742  20.177  -2.070  1.00 42.03 ? 87  ASN C OD1 1 
ATOM   4419 N ND2 . ASN C 1 87  ? 32.528  18.075  -2.773  1.00 51.05 ? 87  ASN C ND2 1 
ATOM   4420 N N   . TYR C 1 88  ? 30.404  21.797  -0.462  1.00 30.31 ? 88  TYR C N   1 
ATOM   4421 C CA  . TYR C 1 88  ? 30.753  23.181  -0.153  1.00 33.67 ? 88  TYR C CA  1 
ATOM   4422 C C   . TYR C 1 88  ? 29.532  24.041  0.189   1.00 33.46 ? 88  TYR C C   1 
ATOM   4423 O O   . TYR C 1 88  ? 29.649  25.278  0.245   1.00 28.18 ? 88  TYR C O   1 
ATOM   4424 C CB  . TYR C 1 88  ? 31.563  23.810  -1.301  1.00 33.86 ? 88  TYR C CB  1 
ATOM   4425 C CG  . TYR C 1 88  ? 30.821  23.811  -2.607  1.00 36.67 ? 88  TYR C CG  1 
ATOM   4426 C CD1 . TYR C 1 88  ? 30.905  22.727  -3.476  1.00 37.09 ? 88  TYR C CD1 1 
ATOM   4427 C CD2 . TYR C 1 88  ? 30.011  24.877  -2.965  1.00 35.16 ? 88  TYR C CD2 1 
ATOM   4428 C CE1 . TYR C 1 88  ? 30.197  22.717  -4.667  1.00 38.14 ? 88  TYR C CE1 1 
ATOM   4429 C CE2 . TYR C 1 88  ? 29.309  24.877  -4.141  1.00 34.81 ? 88  TYR C CE2 1 
ATOM   4430 C CZ  . TYR C 1 88  ? 29.398  23.801  -4.985  1.00 40.19 ? 88  TYR C CZ  1 
ATOM   4431 O OH  . TYR C 1 88  ? 28.684  23.810  -6.161  1.00 41.86 ? 88  TYR C OH  1 
ATOM   4432 N N   . THR C 1 89  ? 28.368  23.433  0.471   1.00 28.08 ? 89  THR C N   1 
ATOM   4433 C CA  . THR C 1 89  ? 27.154  24.216  0.699   1.00 26.72 ? 89  THR C CA  1 
ATOM   4434 C C   . THR C 1 89  ? 26.603  24.081  2.120   1.00 26.02 ? 89  THR C C   1 
ATOM   4435 O O   . THR C 1 89  ? 25.398  24.291  2.345   1.00 25.18 ? 89  THR C O   1 
ATOM   4436 C CB  . THR C 1 89  ? 26.078  23.850  -0.321  1.00 30.78 ? 89  THR C CB  1 
ATOM   4437 O OG1 . THR C 1 89  ? 26.064  22.430  -0.517  1.00 30.75 ? 89  THR C OG1 1 
ATOM   4438 C CG2 . THR C 1 89  ? 26.345  24.558  -1.656  1.00 28.74 ? 89  THR C CG2 1 
ATOM   4439 N N   . ALA C 1 90  ? 27.479  23.798  3.093   1.00 25.37 ? 90  ALA C N   1 
ATOM   4440 C CA  . ALA C 1 90  ? 27.057  23.706  4.490   1.00 27.32 ? 90  ALA C CA  1 
ATOM   4441 C C   . ALA C 1 90  ? 26.384  24.987  4.966   1.00 28.55 ? 90  ALA C C   1 
ATOM   4442 O O   . ALA C 1 90  ? 25.394  24.936  5.718   1.00 24.41 ? 90  ALA C O   1 
ATOM   4443 C CB  . ALA C 1 90  ? 28.244  23.386  5.391   1.00 25.01 ? 90  ALA C CB  1 
ATOM   4444 N N   . CYS C 1 91  ? 26.916  26.148  4.549   1.00 25.16 ? 91  CYS C N   1 
ATOM   4445 C CA  . CYS C 1 91  ? 26.378  27.420  5.028   1.00 25.00 ? 91  CYS C CA  1 
ATOM   4446 C C   . CYS C 1 91  ? 24.987  27.702  4.468   1.00 24.44 ? 91  CYS C C   1 
ATOM   4447 O O   . CYS C 1 91  ? 24.062  27.949  5.263   1.00 24.61 ? 91  CYS C O   1 
ATOM   4448 C CB  . CYS C 1 91  ? 27.378  28.558  4.740   1.00 23.87 ? 91  CYS C CB  1 
ATOM   4449 S SG  . CYS C 1 91  ? 26.921  30.141  5.589   1.00 27.42 ? 91  CYS C SG  1 
ATOM   4450 N N   . PRO C 1 92  ? 24.750  27.669  3.154   1.00 24.19 ? 92  PRO C N   1 
ATOM   4451 C CA  . PRO C 1 92  ? 23.369  27.854  2.671   1.00 23.62 ? 92  PRO C CA  1 
ATOM   4452 C C   . PRO C 1 92  ? 22.404  26.784  3.144   1.00 24.50 ? 92  PRO C C   1 
ATOM   4453 O O   . PRO C 1 92  ? 21.197  27.058  3.259   1.00 22.42 ? 92  PRO C O   1 
ATOM   4454 C CB  . PRO C 1 92  ? 23.522  27.839  1.141   1.00 24.70 ? 92  PRO C CB  1 
ATOM   4455 C CG  . PRO C 1 92  ? 24.832  27.176  0.885   1.00 23.70 ? 92  PRO C CG  1 
ATOM   4456 C CD  . PRO C 1 92  ? 25.708  27.547  2.039   1.00 25.22 ? 92  PRO C CD  1 
ATOM   4457 N N   . THR C 1 93  ? 22.878  25.562  3.378   1.00 22.59 ? 93  THR C N   1 
ATOM   4458 C CA  . THR C 1 93  ? 21.990  24.555  3.945   1.00 23.74 ? 93  THR C CA  1 
ATOM   4459 C C   . THR C 1 93  ? 21.605  24.910  5.374   1.00 23.07 ? 93  THR C C   1 
ATOM   4460 O O   . THR C 1 93  ? 20.442  24.728  5.775   1.00 21.98 ? 93  THR C O   1 
ATOM   4461 C CB  . THR C 1 93  ? 22.627  23.157  3.913   1.00 24.02 ? 93  THR C CB  1 
ATOM   4462 O OG1 . THR C 1 93  ? 23.183  22.857  2.623   1.00 25.58 ? 93  THR C OG1 1 
ATOM   4463 C CG2 . THR C 1 93  ? 21.569  22.075  4.264   1.00 24.57 ? 93  THR C CG2 1 
ATOM   4464 N N   . SER C 1 94  ? 22.560  25.419  6.160   1.00 22.32 ? 94  SER C N   1 
ATOM   4465 C CA  . SER C 1 94  ? 22.246  25.822  7.532   1.00 20.82 ? 94  SER C CA  1 
ATOM   4466 C C   . SER C 1 94  ? 21.267  26.989  7.543   1.00 22.54 ? 94  SER C C   1 
ATOM   4467 O O   . SER C 1 94  ? 20.373  27.054  8.394   1.00 22.56 ? 94  SER C O   1 
ATOM   4468 C CB  . SER C 1 94  ? 23.522  26.202  8.287   1.00 22.79 ? 94  SER C CB  1 
ATOM   4469 O OG  . SER C 1 94  ? 24.397  25.097  8.426   1.00 23.28 ? 94  SER C OG  1 
ATOM   4470 N N   . LEU C 1 95  ? 21.410  27.906  6.586   1.00 23.23 ? 95  LEU C N   1 
ATOM   4471 C CA  . LEU C 1 95  ? 20.492  29.029  6.472   1.00 22.66 ? 95  LEU C CA  1 
ATOM   4472 C C   . LEU C 1 95  ? 19.106  28.547  6.051   1.00 25.64 ? 95  LEU C C   1 
ATOM   4473 O O   . LEU C 1 95  ? 18.090  29.032  6.560   1.00 23.65 ? 95  LEU C O   1 
ATOM   4474 C CB  . LEU C 1 95  ? 21.047  30.050  5.460   1.00 22.10 ? 95  LEU C CB  1 
ATOM   4475 C CG  . LEU C 1 95  ? 20.228  31.349  5.380   1.00 24.11 ? 95  LEU C CG  1 
ATOM   4476 C CD1 . LEU C 1 95  ? 20.039  31.981  6.764   1.00 24.45 ? 95  LEU C CD1 1 
ATOM   4477 C CD2 . LEU C 1 95  ? 20.841  32.320  4.386   1.00 23.65 ? 95  LEU C CD2 1 
ATOM   4478 N N   . SER C 1 96  ? 19.050  27.568  5.137   1.00 25.39 ? 96  SER C N   1 
ATOM   4479 C CA  . SER C 1 96  ? 17.772  26.997  4.713   1.00 23.60 ? 96  SER C CA  1 
ATOM   4480 C C   . SER C 1 96  ? 17.080  26.252  5.863   1.00 24.74 ? 96  SER C C   1 
ATOM   4481 O O   . SER C 1 96  ? 15.846  26.324  6.022   1.00 24.51 ? 96  SER C O   1 
ATOM   4482 C CB  . SER C 1 96  ? 18.002  26.070  3.515   1.00 25.99 ? 96  SER C CB  1 
ATOM   4483 O OG  . SER C 1 96  ? 16.798  25.449  3.102   1.00 24.73 ? 96  SER C OG  1 
ATOM   4484 N N   . LEU C 1 97  ? 17.847  25.520  6.670   1.00 20.10 ? 97  LEU C N   1 
ATOM   4485 C CA  . LEU C 1 97  ? 17.272  24.925  7.872   1.00 22.02 ? 97  LEU C CA  1 
ATOM   4486 C C   . LEU C 1 97  ? 16.707  26.005  8.796   1.00 23.03 ? 97  LEU C C   1 
ATOM   4487 O O   . LEU C 1 97  ? 15.600  25.862  9.330   1.00 23.93 ? 97  LEU C O   1 
ATOM   4488 C CB  . LEU C 1 97  ? 18.336  24.097  8.581   1.00 21.25 ? 97  LEU C CB  1 
ATOM   4489 C CG  . LEU C 1 97  ? 18.765  22.807  7.857   1.00 20.99 ? 97  LEU C CG  1 
ATOM   4490 C CD1 . LEU C 1 97  ? 20.053  22.289  8.490   1.00 19.98 ? 97  LEU C CD1 1 
ATOM   4491 C CD2 . LEU C 1 97  ? 17.688  21.750  8.007   1.00 20.76 ? 97  LEU C CD2 1 
ATOM   4492 N N   . ALA C 1 98  ? 17.467  27.088  9.011   1.00 20.98 ? 98  ALA C N   1 
ATOM   4493 C CA  . ALA C 1 98  ? 16.960  28.206  9.808   1.00 23.76 ? 98  ALA C CA  1 
ATOM   4494 C C   . ALA C 1 98  ? 15.662  28.756  9.230   1.00 21.56 ? 98  ALA C C   1 
ATOM   4495 O O   . ALA C 1 98  ? 14.737  29.096  9.979   1.00 23.90 ? 98  ALA C O   1 
ATOM   4496 C CB  . ALA C 1 98  ? 18.013  29.326  9.888   1.00 23.31 ? 98  ALA C CB  1 
ATOM   4497 N N   . SER C 1 99  ? 15.573  28.851  7.900   1.00 21.22 ? 99  SER C N   1 
ATOM   4498 C CA  . SER C 1 99  ? 14.389  29.416  7.258   1.00 20.61 ? 99  SER C CA  1 
ATOM   4499 C C   . SER C 1 99  ? 13.143  28.580  7.532   1.00 23.05 ? 99  SER C C   1 
ATOM   4500 O O   . SER C 1 99  ? 12.028  29.121  7.578   1.00 21.79 ? 99  SER C O   1 
ATOM   4501 C CB  . SER C 1 99  ? 14.621  29.540  5.743   1.00 21.62 ? 99  SER C CB  1 
ATOM   4502 O OG  . SER C 1 99  ? 14.715  28.249  5.124   1.00 23.65 ? 99  SER C OG  1 
ATOM   4503 N N   . GLN C 1 100 ? 13.307  27.272  7.740   1.00 19.55 ? 100 GLN C N   1 
ATOM   4504 C CA  . GLN C 1 100 ? 12.170  26.445  8.140   1.00 21.38 ? 100 GLN C CA  1 
ATOM   4505 C C   . GLN C 1 100 ? 11.648  26.860  9.507   1.00 20.65 ? 100 GLN C C   1 
ATOM   4506 O O   . GLN C 1 100 ? 10.434  26.988  9.711   1.00 25.68 ? 100 GLN C O   1 
ATOM   4507 C CB  . GLN C 1 100 ? 12.587  24.977  8.201   1.00 22.01 ? 100 GLN C CB  1 
ATOM   4508 C CG  . GLN C 1 100 ? 12.910  24.308  6.903   1.00 20.49 ? 100 GLN C CG  1 
ATOM   4509 C CD  . GLN C 1 100 ? 13.197  22.832  7.149   1.00 22.55 ? 100 GLN C CD  1 
ATOM   4510 O OE1 . GLN C 1 100 ? 12.436  22.157  7.844   1.00 23.33 ? 100 GLN C OE1 1 
ATOM   4511 N NE2 . GLN C 1 100 ? 14.300  22.329  6.589   1.00 18.66 ? 100 GLN C NE2 1 
ATOM   4512 N N   . MET C 1 101 ? 12.561  26.992  10.470  1.00 22.55 ? 101 MET C N   1 
ATOM   4513 C CA  . MET C 1 101 ? 12.225  27.341  11.843  1.00 23.98 ? 101 MET C CA  1 
ATOM   4514 C C   . MET C 1 101 ? 11.580  28.715  11.944  1.00 25.64 ? 101 MET C C   1 
ATOM   4515 O O   . MET C 1 101 ? 10.812  28.962  12.872  1.00 24.83 ? 101 MET C O   1 
ATOM   4516 C CB  . MET C 1 101 ? 13.472  27.278  12.730  1.00 23.69 ? 101 MET C CB  1 
ATOM   4517 C CG  . MET C 1 101 ? 14.132  25.876  12.900  1.00 28.20 ? 101 MET C CG  1 
ATOM   4518 S SD  . MET C 1 101 ? 13.059  24.952  14.006  1.00 44.36 ? 101 MET C SD  1 
ATOM   4519 C CE  . MET C 1 101 ? 14.176  24.629  15.365  1.00 38.85 ? 101 MET C CE  1 
ATOM   4520 N N   . LEU C 1 102 ? 11.896  29.616  11.025  1.00 24.11 ? 102 LEU C N   1 
ATOM   4521 C CA  . LEU C 1 102 ? 11.340  30.966  10.982  1.00 26.21 ? 102 LEU C CA  1 
ATOM   4522 C C   . LEU C 1 102 ? 10.089  31.060  10.120  1.00 26.75 ? 102 LEU C C   1 
ATOM   4523 O O   . LEU C 1 102 ? 9.561   32.167  9.947   1.00 22.98 ? 102 LEU C O   1 
ATOM   4524 C CB  . LEU C 1 102 ? 12.392  31.947  10.440  1.00 20.88 ? 102 LEU C CB  1 
ATOM   4525 C CG  . LEU C 1 102 ? 13.593  32.089  11.391  1.00 24.33 ? 102 LEU C CG  1 
ATOM   4526 C CD1 . LEU C 1 102 ? 14.677  33.024  10.804  1.00 23.40 ? 102 LEU C CD1 1 
ATOM   4527 C CD2 . LEU C 1 102 ? 13.148  32.596  12.791  1.00 23.76 ? 102 LEU C CD2 1 
ATOM   4528 N N   . TYR C 1 103 ? 9.617   29.933  9.562   1.00 22.68 ? 103 TYR C N   1 
ATOM   4529 C CA  . TYR C 1 103 ? 8.419   29.909  8.716   1.00 22.64 ? 103 TYR C CA  1 
ATOM   4530 C C   . TYR C 1 103 ? 8.576   30.827  7.503   1.00 23.54 ? 103 TYR C C   1 
ATOM   4531 O O   . TYR C 1 103 ? 7.640   31.505  7.074   1.00 23.88 ? 103 TYR C O   1 
ATOM   4532 C CB  . TYR C 1 103 ? 7.152   30.261  9.513   1.00 22.41 ? 103 TYR C CB  1 
ATOM   4533 C CG  . TYR C 1 103 ? 6.779   29.189  10.507  1.00 24.65 ? 103 TYR C CG  1 
ATOM   4534 C CD1 . TYR C 1 103 ? 7.451   29.089  11.726  1.00 25.54 ? 103 TYR C CD1 1 
ATOM   4535 C CD2 . TYR C 1 103 ? 5.770   28.262  10.234  1.00 21.46 ? 103 TYR C CD2 1 
ATOM   4536 C CE1 . TYR C 1 103 ? 7.125   28.089  12.645  1.00 22.59 ? 103 TYR C CE1 1 
ATOM   4537 C CE2 . TYR C 1 103 ? 5.440   27.257  11.160  1.00 19.73 ? 103 TYR C CE2 1 
ATOM   4538 C CZ  . TYR C 1 103 ? 6.123   27.185  12.352  1.00 21.16 ? 103 TYR C CZ  1 
ATOM   4539 O OH  . TYR C 1 103 ? 5.824   26.209  13.284  1.00 23.38 ? 103 TYR C OH  1 
ATOM   4540 N N   . HIS C 1 104 ? 9.757   30.801  6.895   1.00 22.56 ? 104 HIS C N   1 
ATOM   4541 C CA  . HIS C 1 104 ? 10.027  31.572  5.692   1.00 22.79 ? 104 HIS C CA  1 
ATOM   4542 C C   . HIS C 1 104 ? 10.961  30.767  4.791   1.00 25.47 ? 104 HIS C C   1 
ATOM   4543 O O   . HIS C 1 104 ? 12.079  31.187  4.488   1.00 25.88 ? 104 HIS C O   1 
ATOM   4544 C CB  . HIS C 1 104 ? 10.628  32.931  6.041   1.00 23.57 ? 104 HIS C CB  1 
ATOM   4545 C CG  . HIS C 1 104 ? 10.627  33.907  4.904   1.00 23.98 ? 104 HIS C CG  1 
ATOM   4546 N ND1 . HIS C 1 104 ? 9.471   34.355  4.304   1.00 27.45 ? 104 HIS C ND1 1 
ATOM   4547 C CD2 . HIS C 1 104 ? 11.647  34.541  4.272   1.00 27.58 ? 104 HIS C CD2 1 
ATOM   4548 C CE1 . HIS C 1 104 ? 9.774   35.223  3.356   1.00 30.71 ? 104 HIS C CE1 1 
ATOM   4549 N NE2 . HIS C 1 104 ? 11.089  35.344  3.305   1.00 27.77 ? 104 HIS C NE2 1 
ATOM   4550 N N   . TYR C 1 105 ? 10.476  29.597  4.361   1.00 24.56 ? 105 TYR C N   1 
ATOM   4551 C CA  . TYR C 1 105 ? 11.336  28.605  3.730   1.00 24.20 ? 105 TYR C CA  1 
ATOM   4552 C C   . TYR C 1 105 ? 11.973  29.116  2.450   1.00 24.68 ? 105 TYR C C   1 
ATOM   4553 O O   . TYR C 1 105 ? 11.284  29.588  1.540   1.00 26.85 ? 105 TYR C O   1 
ATOM   4554 C CB  . TYR C 1 105 ? 10.548  27.341  3.411   1.00 24.01 ? 105 TYR C CB  1 
ATOM   4555 C CG  . TYR C 1 105 ? 11.422  26.327  2.674   1.00 22.05 ? 105 TYR C CG  1 
ATOM   4556 C CD1 . TYR C 1 105 ? 12.515  25.756  3.291   1.00 21.99 ? 105 TYR C CD1 1 
ATOM   4557 C CD2 . TYR C 1 105 ? 11.154  25.979  1.357   1.00 24.25 ? 105 TYR C CD2 1 
ATOM   4558 C CE1 . TYR C 1 105 ? 13.317  24.808  2.618   1.00 26.02 ? 105 TYR C CE1 1 
ATOM   4559 C CE2 . TYR C 1 105 ? 11.935  25.023  0.671   1.00 25.24 ? 105 TYR C CE2 1 
ATOM   4560 C CZ  . TYR C 1 105 ? 13.010  24.448  1.305   1.00 26.24 ? 105 TYR C CZ  1 
ATOM   4561 O OH  . TYR C 1 105 ? 13.786  23.522  0.634   1.00 24.18 ? 105 TYR C OH  1 
ATOM   4562 N N   . LYS C 1 106 ? 13.293  28.987  2.384   1.00 25.36 ? 106 LYS C N   1 
ATOM   4563 C CA  . LYS C 1 106 ? 14.088  29.221  1.192   1.00 26.02 ? 106 LYS C CA  1 
ATOM   4564 C C   . LYS C 1 106 ? 14.979  27.999  1.019   1.00 26.17 ? 106 LYS C C   1 
ATOM   4565 O O   . LYS C 1 106 ? 15.615  27.549  1.978   1.00 24.99 ? 106 LYS C O   1 
ATOM   4566 C CB  . LYS C 1 106 ? 14.927  30.513  1.297   1.00 24.02 ? 106 LYS C CB  1 
ATOM   4567 C CG  . LYS C 1 106 ? 14.117  31.772  1.649   1.00 19.99 ? 106 LYS C CG  1 
ATOM   4568 C CD  . LYS C 1 106 ? 13.288  32.185  0.468   1.00 23.72 ? 106 LYS C CD  1 
ATOM   4569 C CE  . LYS C 1 106 ? 12.715  33.602  0.674   1.00 26.40 ? 106 LYS C CE  1 
ATOM   4570 N NZ  . LYS C 1 106 ? 11.796  33.968  -0.434  1.00 29.30 ? 106 LYS C NZ  1 
ATOM   4571 N N   . SER C 1 107 ? 14.974  27.433  -0.179  1.00 24.93 ? 107 SER C N   1 
ATOM   4572 C CA  . SER C 1 107 ? 15.693  26.192  -0.430  1.00 27.97 ? 107 SER C CA  1 
ATOM   4573 C C   . SER C 1 107 ? 17.200  26.416  -0.355  1.00 27.49 ? 107 SER C C   1 
ATOM   4574 O O   . SER C 1 107 ? 17.694  27.545  -0.445  1.00 23.52 ? 107 SER C O   1 
ATOM   4575 C CB  . SER C 1 107 ? 15.304  25.624  -1.789  1.00 28.51 ? 107 SER C CB  1 
ATOM   4576 O OG  . SER C 1 107 ? 16.021  26.290  -2.808  1.00 28.34 ? 107 SER C OG  1 
ATOM   4577 N N   . GLU C 1 108 ? 17.925  25.312  -0.162  1.00 25.09 ? 108 GLU C N   1 
ATOM   4578 C CA  . GLU C 1 108 ? 19.379  25.380  -0.121  1.00 24.54 ? 108 GLU C CA  1 
ATOM   4579 C C   . GLU C 1 108 ? 19.920  26.083  -1.365  1.00 25.74 ? 108 GLU C C   1 
ATOM   4580 O O   . GLU C 1 108 ? 20.829  26.913  -1.278  1.00 25.15 ? 108 GLU C O   1 
ATOM   4581 C CB  . GLU C 1 108 ? 19.959  23.972  -0.015  1.00 25.64 ? 108 GLU C CB  1 
ATOM   4582 C CG  . GLU C 1 108 ? 21.418  23.937  -0.409  1.00 29.55 ? 108 GLU C CG  1 
ATOM   4583 C CD  . GLU C 1 108 ? 22.068  22.575  -0.256  1.00 32.60 ? 108 GLU C CD  1 
ATOM   4584 O OE1 . GLU C 1 108 ? 21.488  21.706  0.420   1.00 34.20 ? 108 GLU C OE1 1 
ATOM   4585 O OE2 . GLU C 1 108 ? 23.163  22.377  -0.829  1.00 29.95 ? 108 GLU C OE2 1 
ATOM   4586 N N   . SER C 1 109 ? 19.368  25.759  -2.533  1.00 24.73 ? 109 SER C N   1 
ATOM   4587 C CA  . SER C 1 109 ? 19.812  26.366  -3.785  1.00 26.63 ? 109 SER C CA  1 
ATOM   4588 C C   . SER C 1 109 ? 19.567  27.865  -3.786  1.00 28.56 ? 109 SER C C   1 
ATOM   4589 O O   . SER C 1 109 ? 20.436  28.655  -4.183  1.00 26.50 ? 109 SER C O   1 
ATOM   4590 C CB  . SER C 1 109 ? 19.066  25.728  -4.950  1.00 28.53 ? 109 SER C CB  1 
ATOM   4591 O OG  . SER C 1 109 ? 19.747  25.969  -6.156  1.00 39.99 ? 109 SER C OG  1 
ATOM   4592 N N   . GLU C 1 110 ? 18.364  28.267  -3.367  1.00 26.53 ? 110 GLU C N   1 
ATOM   4593 C CA  . GLU C 1 110 ? 18.042  29.685  -3.256  1.00 27.61 ? 110 GLU C CA  1 
ATOM   4594 C C   . GLU C 1 110 ? 19.030  30.391  -2.343  1.00 26.72 ? 110 GLU C C   1 
ATOM   4595 O O   . GLU C 1 110 ? 19.489  31.496  -2.645  1.00 27.44 ? 110 GLU C O   1 
ATOM   4596 C CB  . GLU C 1 110 ? 16.628  29.858  -2.694  1.00 31.71 ? 110 GLU C CB  1 
ATOM   4597 C CG  . GLU C 1 110 ? 15.508  29.879  -3.703  1.00 34.98 ? 110 GLU C CG  1 
ATOM   4598 C CD  . GLU C 1 110 ? 14.104  29.887  -3.034  1.00 39.56 ? 110 GLU C CD  1 
ATOM   4599 O OE1 . GLU C 1 110 ? 13.793  29.009  -2.155  1.00 30.84 ? 110 GLU C OE1 1 
ATOM   4600 O OE2 . GLU C 1 110 ? 13.326  30.811  -3.387  1.00 37.22 ? 110 GLU C OE2 1 
ATOM   4601 N N   . CYS C 1 111 ? 19.357  29.766  -1.208  1.00 25.33 ? 111 CYS C N   1 
ATOM   4602 C CA  . CYS C 1 111 ? 20.254  30.392  -0.246  1.00 24.77 ? 111 CYS C CA  1 
ATOM   4603 C C   . CYS C 1 111 ? 21.667  30.494  -0.799  1.00 27.91 ? 111 CYS C C   1 
ATOM   4604 O O   . CYS C 1 111 ? 22.345  31.508  -0.593  1.00 25.56 ? 111 CYS C O   1 
ATOM   4605 C CB  . CYS C 1 111 ? 20.250  29.606  1.061   1.00 21.97 ? 111 CYS C CB  1 
ATOM   4606 S SG  . CYS C 1 111 ? 18.685  29.783  2.025   1.00 26.34 ? 111 CYS C SG  1 
ATOM   4607 N N   . ALA C 1 112 ? 22.136  29.438  -1.475  1.00 26.98 ? 112 ALA C N   1 
ATOM   4608 C CA  . ALA C 1 112 ? 23.488  29.454  -2.051  1.00 26.41 ? 112 ALA C CA  1 
ATOM   4609 C C   . ALA C 1 112 ? 23.639  30.551  -3.099  1.00 28.70 ? 112 ALA C C   1 
ATOM   4610 O O   . ALA C 1 112 ? 24.675  31.223  -3.157  1.00 28.40 ? 112 ALA C O   1 
ATOM   4611 C CB  . ALA C 1 112 ? 23.813  28.103  -2.680  1.00 26.24 ? 112 ALA C CB  1 
ATOM   4612 N N   . LYS C 1 113 ? 22.645  30.708  -3.972  1.00 27.10 ? 113 LYS C N   1 
ATOM   4613 C CA  . LYS C 1 113 ? 22.709  31.772  -4.962  1.00 29.62 ? 113 LYS C CA  1 
ATOM   4614 C C   . LYS C 1 113 ? 22.734  33.126  -4.277  1.00 29.76 ? 113 LYS C C   1 
ATOM   4615 O O   . LYS C 1 113 ? 23.491  34.016  -4.670  1.00 28.78 ? 113 LYS C O   1 
ATOM   4616 C CB  . LYS C 1 113 ? 21.524  31.674  -5.923  1.00 33.42 ? 113 LYS C CB  1 
ATOM   4617 C CG  . LYS C 1 113 ? 20.956  33.050  -6.283  1.00 40.85 ? 113 LYS C CG  1 
ATOM   4618 C CD  . LYS C 1 113 ? 19.606  32.987  -7.015  1.00 40.66 ? 113 LYS C CD  1 
ATOM   4619 C CE  . LYS C 1 113 ? 18.467  32.561  -6.039  1.00 40.01 ? 113 LYS C CE  1 
ATOM   4620 N NZ  . LYS C 1 113 ? 18.332  33.351  -4.735  1.00 31.34 ? 113 LYS C NZ  1 
ATOM   4621 N N   . ALA C 1 114 ? 21.916  33.306  -3.238  1.00 30.21 ? 114 ALA C N   1 
ATOM   4622 C CA  . ALA C 1 114 ? 21.857  34.609  -2.577  1.00 27.82 ? 114 ALA C CA  1 
ATOM   4623 C C   . ALA C 1 114 ? 23.163  34.931  -1.866  1.00 30.53 ? 114 ALA C C   1 
ATOM   4624 O O   . ALA C 1 114 ? 23.633  36.076  -1.905  1.00 30.45 ? 114 ALA C O   1 
ATOM   4625 C CB  . ALA C 1 114 ? 20.691  34.637  -1.584  1.00 30.13 ? 114 ALA C CB  1 
ATOM   4626 N N   . LEU C 1 115 ? 23.760  33.944  -1.193  1.00 27.41 ? 115 LEU C N   1 
ATOM   4627 C CA  . LEU C 1 115 ? 24.984  34.179  -0.441  1.00 27.72 ? 115 LEU C CA  1 
ATOM   4628 C C   . LEU C 1 115 ? 26.220  34.281  -1.320  1.00 28.77 ? 115 LEU C C   1 
ATOM   4629 O O   . LEU C 1 115 ? 27.232  34.799  -0.855  1.00 29.82 ? 115 LEU C O   1 
ATOM   4630 C CB  . LEU C 1 115 ? 25.190  33.079  0.598   1.00 27.00 ? 115 LEU C CB  1 
ATOM   4631 C CG  . LEU C 1 115 ? 24.118  32.903  1.692   1.00 27.53 ? 115 LEU C CG  1 
ATOM   4632 C CD1 . LEU C 1 115 ? 24.681  32.009  2.790   1.00 25.79 ? 115 LEU C CD1 1 
ATOM   4633 C CD2 . LEU C 1 115 ? 23.668  34.219  2.283   1.00 25.01 ? 115 LEU C CD2 1 
ATOM   4634 N N   . GLY C 1 116 ? 26.167  33.803  -2.563  1.00 31.09 ? 116 GLY C N   1 
ATOM   4635 C CA  . GLY C 1 116 ? 27.370  33.729  -3.373  1.00 32.04 ? 116 GLY C CA  1 
ATOM   4636 C C   . GLY C 1 116 ? 28.263  32.560  -3.040  1.00 34.57 ? 116 GLY C C   1 
ATOM   4637 O O   . GLY C 1 116 ? 29.480  32.619  -3.280  1.00 32.04 ? 116 GLY C O   1 
ATOM   4638 N N   . THR C 1 117 ? 27.672  31.488  -2.527  1.00 29.89 ? 117 THR C N   1 
ATOM   4639 C CA  . THR C 1 117 ? 28.448  30.271  -2.188  1.00 30.57 ? 117 THR C CA  1 
ATOM   4640 C C   . THR C 1 117 ? 29.162  29.755  -3.438  1.00 34.06 ? 117 THR C C   1 
ATOM   4641 O O   . THR C 1 117 ? 28.563  29.740  -4.504  1.00 33.45 ? 117 THR C O   1 
ATOM   4642 C CB  . THR C 1 117 ? 27.555  29.182  -1.580  1.00 30.35 ? 117 THR C CB  1 
ATOM   4643 O OG1 . THR C 1 117 ? 26.856  29.746  -0.478  1.00 26.00 ? 117 THR C OG1 1 
ATOM   4644 C CG2 . THR C 1 117 ? 28.318  27.949  -1.155  1.00 27.99 ? 117 THR C CG2 1 
ATOM   4645 N N   . SER C 1 118 ? 30.394  29.296  -3.276  1.00 35.15 ? 118 SER C N   1 
ATOM   4646 C CA  . SER C 1 118 ? 31.147  28.827  -4.460  1.00 37.20 ? 118 SER C CA  1 
ATOM   4647 C C   . SER C 1 118 ? 31.898  27.531  -4.180  1.00 39.26 ? 118 SER C C   1 
ATOM   4648 O O   . SER C 1 118 ? 32.276  27.280  -3.050  1.00 37.40 ? 118 SER C O   1 
ATOM   4649 C CB  . SER C 1 118 ? 32.077  29.894  -4.977  1.00 38.09 ? 118 SER C CB  1 
ATOM   4650 O OG  . SER C 1 118 ? 33.248  29.945  -4.208  1.00 42.45 ? 118 SER C OG  1 
ATOM   4651 N N   . LYS C 1 119 ? 32.108  26.791  -5.263  1.00 43.08 ? 119 LYS C N   1 
ATOM   4652 C CA  . LYS C 1 119 ? 32.839  25.508  -5.231  1.00 45.38 ? 119 LYS C CA  1 
ATOM   4653 C C   . LYS C 1 119 ? 34.209  25.760  -4.630  1.00 46.34 ? 119 LYS C C   1 
ATOM   4654 O O   . LYS C 1 119 ? 34.617  24.994  -3.784  1.00 50.26 ? 119 LYS C O   1 
ATOM   4655 C CB  . LYS C 1 119 ? 33.017  24.963  -6.646  1.00 50.80 ? 119 LYS C CB  1 
ATOM   4656 C CG  . LYS C 1 119 ? 33.738  23.628  -6.705  1.00 55.23 ? 119 LYS C CG  1 
ATOM   4657 C CD  . LYS C 1 119 ? 33.392  22.793  -7.917  1.00 60.09 ? 119 LYS C CD  1 
ATOM   4658 C CE  . LYS C 1 119 ? 31.990  22.220  -7.908  1.00 56.72 ? 119 LYS C CE  1 
ATOM   4659 N NZ  . LYS C 1 119 ? 31.984  20.738  -7.835  1.00 62.87 ? 119 LYS C NZ  1 
ATOM   4660 N N   . GLY C 1 120 ? 34.867  26.823  -5.070  1.00 43.93 ? 120 GLY C N   1 
ATOM   4661 C CA  . GLY C 1 120 ? 36.217  27.136  -4.586  1.00 46.75 ? 120 GLY C CA  1 
ATOM   4662 C C   . GLY C 1 120 ? 36.310  27.422  -3.104  1.00 47.41 ? 120 GLY C C   1 
ATOM   4663 O O   . GLY C 1 120 ? 37.027  26.703  -2.422  1.00 51.86 ? 120 GLY C O   1 
ATOM   4664 N N   . SER C 1 121 ? 35.552  28.384  -2.601  1.00 41.31 ? 121 SER C N   1 
ATOM   4665 C CA  . SER C 1 121 ? 35.803  28.820  -1.212  1.00 41.13 ? 121 SER C CA  1 
ATOM   4666 C C   . SER C 1 121 ? 34.634  28.597  -0.259  1.00 42.07 ? 121 SER C C   1 
ATOM   4667 O O   . SER C 1 121 ? 34.780  29.027  0.865   1.00 39.39 ? 121 SER C O   1 
ATOM   4668 C CB  . SER C 1 121 ? 36.143  30.263  -1.228  1.00 42.75 ? 121 SER C CB  1 
ATOM   4669 O OG  . SER C 1 121 ? 35.273  30.950  -2.103  1.00 48.09 ? 121 SER C OG  1 
ATOM   4670 N N   . GLY C 1 122 ? 33.551  27.944  -0.664  1.00 37.13 ? 122 GLY C N   1 
ATOM   4671 C CA  . GLY C 1 122 ? 32.463  27.824  0.310   1.00 37.11 ? 122 GLY C CA  1 
ATOM   4672 C C   . GLY C 1 122 ? 31.755  29.145  0.555   1.00 34.11 ? 122 GLY C C   1 
ATOM   4673 O O   . GLY C 1 122 ? 31.397  29.867  -0.382  1.00 33.45 ? 122 GLY C O   1 
ATOM   4674 N N   . THR C 1 123 ? 31.495  29.440  1.833   1.00 32.52 ? 123 THR C N   1 
ATOM   4675 C CA  . THR C 1 123 ? 30.833  30.674  2.267   1.00 31.68 ? 123 THR C CA  1 
ATOM   4676 C C   . THR C 1 123 ? 31.537  31.192  3.511   1.00 31.25 ? 123 THR C C   1 
ATOM   4677 O O   . THR C 1 123 ? 31.809  30.423  4.441   1.00 30.05 ? 123 THR C O   1 
ATOM   4678 C CB  . THR C 1 123 ? 29.333  30.487  2.581   1.00 28.19 ? 123 THR C CB  1 
ATOM   4679 O OG1 . THR C 1 123 ? 28.704  29.703  1.571   1.00 26.19 ? 123 THR C OG1 1 
ATOM   4680 C CG2 . THR C 1 123 ? 28.603  31.870  2.644   1.00 29.13 ? 123 THR C CG2 1 
ATOM   4681 N N   . SER C 1 124 ? 31.848  32.466  3.517   1.00 27.86 ? 124 SER C N   1 
ATOM   4682 C CA  . SER C 1 124 ? 32.413  33.100  4.694   1.00 27.54 ? 124 SER C CA  1 
ATOM   4683 C C   . SER C 1 124 ? 31.304  33.646  5.570   1.00 27.94 ? 124 SER C C   1 
ATOM   4684 O O   . SER C 1 124 ? 30.193  33.872  5.097   1.00 28.65 ? 124 SER C O   1 
ATOM   4685 C CB  . SER C 1 124 ? 33.348  34.242  4.276   1.00 28.99 ? 124 SER C CB  1 
ATOM   4686 O OG  . SER C 1 124 ? 32.579  35.347  3.801   1.00 29.03 ? 124 SER C OG  1 
ATOM   4687 N N   . PRO C 1 125 ? 31.570  33.855  6.863   1.00 26.88 ? 125 PRO C N   1 
ATOM   4688 C CA  . PRO C 1 125 ? 30.577  34.539  7.695   1.00 27.85 ? 125 PRO C CA  1 
ATOM   4689 C C   . PRO C 1 125 ? 30.215  35.908  7.157   1.00 28.92 ? 125 PRO C C   1 
ATOM   4690 O O   . PRO C 1 125 ? 29.058  36.313  7.278   1.00 27.32 ? 125 PRO C O   1 
ATOM   4691 C CB  . PRO C 1 125 ? 31.255  34.603  9.071   1.00 26.79 ? 125 PRO C CB  1 
ATOM   4692 C CG  . PRO C 1 125 ? 32.196  33.431  9.045   1.00 31.91 ? 125 PRO C CG  1 
ATOM   4693 C CD  . PRO C 1 125 ? 32.715  33.366  7.654   1.00 28.07 ? 125 PRO C CD  1 
ATOM   4694 N N   . ALA C 1 126 ? 31.171  36.646  6.577   1.00 28.96 ? 126 ALA C N   1 
ATOM   4695 C CA  . ALA C 1 126 ? 30.858  37.965  6.016   1.00 28.35 ? 126 ALA C CA  1 
ATOM   4696 C C   . ALA C 1 126 ? 29.832  37.876  4.885   1.00 29.09 ? 126 ALA C C   1 
ATOM   4697 O O   . ALA C 1 126 ? 28.893  38.685  4.826   1.00 30.85 ? 126 ALA C O   1 
ATOM   4698 C CB  . ALA C 1 126 ? 32.135  38.632  5.499   1.00 28.64 ? 126 ALA C CB  1 
ATOM   4699 N N   . GLN C 1 127 ? 29.984  36.897  3.982   1.00 26.76 ? 127 GLN C N   1 
ATOM   4700 C CA  . GLN C 1 127 ? 28.968  36.682  2.949   1.00 28.59 ? 127 GLN C CA  1 
ATOM   4701 C C   . GLN C 1 127 ? 27.601  36.356  3.567   1.00 28.85 ? 127 GLN C C   1 
ATOM   4702 O O   . GLN C 1 127 ? 26.561  36.856  3.108   1.00 26.87 ? 127 GLN C O   1 
ATOM   4703 C CB  . GLN C 1 127 ? 29.391  35.557  2.010   1.00 28.83 ? 127 GLN C CB  1 
ATOM   4704 C CG  . GLN C 1 127 ? 30.621  35.848  1.147   1.00 28.41 ? 127 GLN C CG  1 
ATOM   4705 C CD  . GLN C 1 127 ? 31.052  34.618  0.344   1.00 30.92 ? 127 GLN C CD  1 
ATOM   4706 O OE1 . GLN C 1 127 ? 31.547  33.632  0.902   1.00 31.19 ? 127 GLN C OE1 1 
ATOM   4707 N NE2 . GLN C 1 127 ? 30.865  34.678  -0.978  1.00 30.83 ? 127 GLN C NE2 1 
ATOM   4708 N N   . LEU C 1 128 ? 27.579  35.492  4.585   1.00 28.06 ? 128 LEU C N   1 
ATOM   4709 C CA  . LEU C 1 128 ? 26.315  35.179  5.248   1.00 30.30 ? 128 LEU C CA  1 
ATOM   4710 C C   . LEU C 1 128 ? 25.636  36.439  5.792   1.00 28.13 ? 128 LEU C C   1 
ATOM   4711 O O   . LEU C 1 128 ? 24.444  36.664  5.557   1.00 29.57 ? 128 LEU C O   1 
ATOM   4712 C CB  . LEU C 1 128 ? 26.552  34.166  6.373   1.00 30.43 ? 128 LEU C CB  1 
ATOM   4713 C CG  . LEU C 1 128 ? 25.378  33.944  7.342   1.00 30.46 ? 128 LEU C CG  1 
ATOM   4714 C CD1 . LEU C 1 128 ? 24.204  33.286  6.644   1.00 27.70 ? 128 LEU C CD1 1 
ATOM   4715 C CD2 . LEU C 1 128 ? 25.798  33.126  8.549   1.00 28.17 ? 128 LEU C CD2 1 
ATOM   4716 N N   . ILE C 1 129 ? 26.376  37.270  6.534   1.00 27.81 ? 129 ILE C N   1 
ATOM   4717 C CA  . ILE C 1 129 ? 25.774  38.440  7.173   1.00 29.09 ? 129 ILE C CA  1 
ATOM   4718 C C   . ILE C 1 129 ? 25.305  39.449  6.134   1.00 27.43 ? 129 ILE C C   1 
ATOM   4719 O O   . ILE C 1 129 ? 24.214  40.031  6.256   1.00 26.58 ? 129 ILE C O   1 
ATOM   4720 C CB  . ILE C 1 129 ? 26.771  39.083  8.151   1.00 29.61 ? 129 ILE C CB  1 
ATOM   4721 C CG1 . ILE C 1 129 ? 27.091  38.124  9.296   1.00 29.36 ? 129 ILE C CG1 1 
ATOM   4722 C CG2 . ILE C 1 129 ? 26.219  40.413  8.673   1.00 31.68 ? 129 ILE C CG2 1 
ATOM   4723 C CD1 . ILE C 1 129 ? 28.462  38.351  9.895   1.00 31.66 ? 129 ILE C CD1 1 
ATOM   4724 N N   . ALA C 1 130 ? 26.133  39.693  5.112   1.00 27.71 ? 130 ALA C N   1 
ATOM   4725 C CA  . ALA C 1 130 ? 25.860  40.754  4.149   1.00 29.64 ? 130 ALA C CA  1 
ATOM   4726 C C   . ALA C 1 130 ? 24.710  40.388  3.231   1.00 31.73 ? 130 ALA C C   1 
ATOM   4727 O O   . ALA C 1 130 ? 23.981  41.270  2.769   1.00 29.68 ? 130 ALA C O   1 
ATOM   4728 C CB  . ALA C 1 130 ? 27.116  41.059  3.312   1.00 27.86 ? 130 ALA C CB  1 
ATOM   4729 N N   . ASN C 1 131 ? 24.524  39.100  2.948   1.00 29.38 ? 131 ASN C N   1 
ATOM   4730 C CA  . ASN C 1 131 ? 23.595  38.719  1.895   1.00 30.52 ? 131 ASN C CA  1 
ATOM   4731 C C   . ASN C 1 131 ? 22.302  38.071  2.378   1.00 28.46 ? 131 ASN C C   1 
ATOM   4732 O O   . ASN C 1 131 ? 21.349  38.002  1.596   1.00 28.39 ? 131 ASN C O   1 
ATOM   4733 C CB  . ASN C 1 131 ? 24.287  37.762  0.919   1.00 30.96 ? 131 ASN C CB  1 
ATOM   4734 C CG  . ASN C 1 131 ? 25.317  38.457  0.063   1.00 30.54 ? 131 ASN C CG  1 
ATOM   4735 O OD1 . ASN C 1 131 ? 26.479  38.071  0.023   1.00 32.60 ? 131 ASN C OD1 1 
ATOM   4736 N ND2 . ASN C 1 131 ? 24.889  39.484  -0.633  1.00 33.43 ? 131 ASN C ND2 1 
ATOM   4737 N N   . ALA C 1 132 ? 22.235  37.604  3.624   1.00 26.96 ? 132 ALA C N   1 
ATOM   4738 C CA  . ALA C 1 132 ? 20.985  36.998  4.119   1.00 28.05 ? 132 ALA C CA  1 
ATOM   4739 C C   . ALA C 1 132 ? 19.768  37.915  3.962   1.00 31.43 ? 132 ALA C C   1 
ATOM   4740 O O   . ALA C 1 132 ? 18.665  37.418  3.671   1.00 27.43 ? 132 ALA C O   1 
ATOM   4741 C CB  . ALA C 1 132 ? 21.128  36.601  5.591   1.00 28.26 ? 132 ALA C CB  1 
ATOM   4742 N N   . PRO C 1 133 ? 19.910  39.248  4.106   1.00 29.28 ? 133 PRO C N   1 
ATOM   4743 C CA  . PRO C 1 133 ? 18.750  40.118  3.858   1.00 28.17 ? 133 PRO C CA  1 
ATOM   4744 C C   . PRO C 1 133 ? 18.105  39.918  2.497   1.00 27.47 ? 133 PRO C C   1 
ATOM   4745 O O   . PRO C 1 133 ? 16.905  40.145  2.378   1.00 28.26 ? 133 PRO C O   1 
ATOM   4746 C CB  . PRO C 1 133 ? 19.350  41.529  3.988   1.00 30.54 ? 133 PRO C CB  1 
ATOM   4747 C CG  . PRO C 1 133 ? 20.419  41.376  5.025   1.00 29.63 ? 133 PRO C CG  1 
ATOM   4748 C CD  . PRO C 1 133 ? 21.001  39.998  4.781   1.00 29.31 ? 133 PRO C CD  1 
ATOM   4749 N N   . LYS C 1 134 ? 18.841  39.474  1.467   1.00 29.25 ? 134 LYS C N   1 
ATOM   4750 C CA  . LYS C 1 134 ? 18.194  39.219  0.178   1.00 28.58 ? 134 LYS C CA  1 
ATOM   4751 C C   . LYS C 1 134 ? 17.093  38.170  0.289   1.00 28.75 ? 134 LYS C C   1 
ATOM   4752 O O   . LYS C 1 134 ? 16.217  38.098  -0.579  1.00 25.21 ? 134 LYS C O   1 
ATOM   4753 C CB  . LYS C 1 134 ? 19.233  38.784  -0.862  1.00 30.69 ? 134 LYS C CB  1 
ATOM   4754 C CG  . LYS C 1 134 ? 20.369  39.823  -1.000  1.00 34.29 ? 134 LYS C CG  1 
ATOM   4755 C CD  . LYS C 1 134 ? 21.083  39.722  -2.347  1.00 39.36 ? 134 LYS C CD  1 
ATOM   4756 C CE  . LYS C 1 134 ? 21.947  38.477  -2.385  1.00 36.94 ? 134 LYS C CE  1 
ATOM   4757 N NZ  . LYS C 1 134 ? 22.850  38.346  -3.601  1.00 37.14 ? 134 LYS C NZ  1 
ATOM   4758 N N   . LEU C 1 135 ? 17.139  37.336  1.313   1.00 25.99 ? 135 LEU C N   1 
ATOM   4759 C CA  . LEU C 1 135 ? 16.140  36.292  1.481   1.00 29.47 ? 135 LEU C CA  1 
ATOM   4760 C C   . LEU C 1 135 ? 15.129  36.623  2.569   1.00 30.88 ? 135 LEU C C   1 
ATOM   4761 O O   . LEU C 1 135 ? 14.230  35.805  2.834   1.00 30.72 ? 135 LEU C O   1 
ATOM   4762 C CB  . LEU C 1 135 ? 16.824  34.973  1.801   1.00 26.80 ? 135 LEU C CB  1 
ATOM   4763 C CG  . LEU C 1 135 ? 17.905  34.475  0.819   1.00 27.66 ? 135 LEU C CG  1 
ATOM   4764 C CD1 . LEU C 1 135 ? 18.961  33.702  1.571   1.00 28.77 ? 135 LEU C CD1 1 
ATOM   4765 C CD2 . LEU C 1 135 ? 17.371  33.575  -0.249  1.00 28.63 ? 135 LEU C CD2 1 
ATOM   4766 N N   . GLY C 1 136 ? 15.246  37.800  3.186   1.00 30.23 ? 136 GLY C N   1 
ATOM   4767 C CA  . GLY C 1 136 ? 14.376  38.210  4.274   1.00 28.36 ? 136 GLY C CA  1 
ATOM   4768 C C   . GLY C 1 136 ? 14.902  37.981  5.680   1.00 29.89 ? 136 GLY C C   1 
ATOM   4769 O O   . GLY C 1 136 ? 14.107  38.019  6.627   1.00 30.68 ? 136 GLY C O   1 
ATOM   4770 N N   . PHE C 1 137 ? 16.198  37.729  5.856   1.00 28.20 ? 137 PHE C N   1 
ATOM   4771 C CA  . PHE C 1 137 ? 16.727  37.459  7.184   1.00 26.90 ? 137 PHE C CA  1 
ATOM   4772 C C   . PHE C 1 137 ? 17.754  38.508  7.598   1.00 31.60 ? 137 PHE C C   1 
ATOM   4773 O O   . PHE C 1 137 ? 18.453  39.095  6.758   1.00 30.74 ? 137 PHE C O   1 
ATOM   4774 C CB  . PHE C 1 137 ? 17.342  36.060  7.251   1.00 29.35 ? 137 PHE C CB  1 
ATOM   4775 C CG  . PHE C 1 137 ? 16.387  34.984  6.810   1.00 27.43 ? 137 PHE C CG  1 
ATOM   4776 C CD1 . PHE C 1 137 ? 15.232  34.741  7.520   1.00 26.34 ? 137 PHE C CD1 1 
ATOM   4777 C CD2 . PHE C 1 137 ? 16.623  34.268  5.654   1.00 25.12 ? 137 PHE C CD2 1 
ATOM   4778 C CE1 . PHE C 1 137 ? 14.346  33.784  7.096   1.00 27.15 ? 137 PHE C CE1 1 
ATOM   4779 C CE2 . PHE C 1 137 ? 15.737  33.310  5.230   1.00 28.08 ? 137 PHE C CE2 1 
ATOM   4780 C CZ  . PHE C 1 137 ? 14.594  33.069  5.957   1.00 24.39 ? 137 PHE C CZ  1 
ATOM   4781 N N   . LYS C 1 138 ? 17.857  38.713  8.912   1.00 31.04 ? 138 LYS C N   1 
ATOM   4782 C CA  . LYS C 1 138 ? 18.916  39.513  9.503   1.00 29.22 ? 138 LYS C CA  1 
ATOM   4783 C C   . LYS C 1 138 ? 19.777  38.575  10.329  1.00 31.50 ? 138 LYS C C   1 
ATOM   4784 O O   . LYS C 1 138 ? 19.262  37.680  10.994  1.00 28.63 ? 138 LYS C O   1 
ATOM   4785 C CB  . LYS C 1 138 ? 18.366  40.648  10.380  1.00 29.85 ? 138 LYS C CB  1 
ATOM   4786 C CG  . LYS C 1 138 ? 19.464  41.381  11.154  1.00 35.89 ? 138 LYS C CG  1 
ATOM   4787 C CD  . LYS C 1 138 ? 18.920  42.321  12.231  1.00 40.85 ? 138 LYS C CD  1 
ATOM   4788 C CE  . LYS C 1 138 ? 20.074  42.994  12.997  1.00 44.75 ? 138 LYS C CE  1 
ATOM   4789 N NZ  . LYS C 1 138 ? 19.634  43.451  14.367  1.00 50.34 ? 138 LYS C NZ  1 
ATOM   4790 N N   . ILE C 1 139 ? 21.083  38.733  10.192  1.00 28.25 ? 139 ILE C N   1 
ATOM   4791 C CA  . ILE C 1 139 ? 22.029  37.879  10.943  1.00 26.99 ? 139 ILE C CA  1 
ATOM   4792 C C   . ILE C 1 139 ? 22.651  38.703  12.062  1.00 31.89 ? 139 ILE C C   1 
ATOM   4793 O O   . ILE C 1 139 ? 23.210  39.727  11.765  1.00 32.81 ? 139 ILE C O   1 
ATOM   4794 C CB  . ILE C 1 139 ? 23.096  37.334  10.001  1.00 26.86 ? 139 ILE C CB  1 
ATOM   4795 C CG1 . ILE C 1 139 ? 22.460  36.531  8.871   1.00 29.06 ? 139 ILE C CG1 1 
ATOM   4796 C CG2 . ILE C 1 139 ? 24.078  36.513  10.791  1.00 28.36 ? 139 ILE C CG2 1 
ATOM   4797 C CD1 . ILE C 1 139 ? 21.992  35.189  9.314   1.00 29.01 ? 139 ILE C CD1 1 
ATOM   4798 N N   . ILE C 1 140 ? 22.564  38.216  13.289  1.00 31.75 ? 140 ILE C N   1 
ATOM   4799 C CA  . ILE C 1 140 ? 23.149  38.932  14.449  1.00 32.80 ? 140 ILE C CA  1 
ATOM   4800 C C   . ILE C 1 140 ? 24.375  38.157  14.934  1.00 35.43 ? 140 ILE C C   1 
ATOM   4801 O O   . ILE C 1 140 ? 24.196  37.118  15.549  1.00 33.71 ? 140 ILE C O   1 
ATOM   4802 C CB  . ILE C 1 140 ? 22.107  39.092  15.563  1.00 33.27 ? 140 ILE C CB  1 
ATOM   4803 C CG1 . ILE C 1 140 ? 20.870  39.806  15.040  1.00 37.94 ? 140 ILE C CG1 1 
ATOM   4804 C CG2 . ILE C 1 140 ? 22.705  39.822  16.742  1.00 33.91 ? 140 ILE C CG2 1 
ATOM   4805 C CD1 . ILE C 1 140 ? 19.639  39.004  15.103  1.00 34.92 ? 140 ILE C CD1 1 
ATOM   4806 N N   . PRO C 1 141 ? 25.603  38.630  14.653  1.00 32.98 ? 141 PRO C N   1 
ATOM   4807 C CA  . PRO C 1 141 ? 26.790  37.978  15.134  1.00 33.38 ? 141 PRO C CA  1 
ATOM   4808 C C   . PRO C 1 141 ? 26.742  38.058  16.660  1.00 34.77 ? 141 PRO C C   1 
ATOM   4809 O O   . PRO C 1 141 ? 26.570  39.109  17.170  1.00 35.51 ? 141 PRO C O   1 
ATOM   4810 C CB  . PRO C 1 141 ? 27.938  38.824  14.581  1.00 36.66 ? 141 PRO C CB  1 
ATOM   4811 C CG  . PRO C 1 141 ? 27.324  39.561  13.433  1.00 34.34 ? 141 PRO C CG  1 
ATOM   4812 C CD  . PRO C 1 141 ? 25.900  39.797  13.859  1.00 33.66 ? 141 PRO C CD  1 
ATOM   4813 N N   . ILE C 1 142 ? 26.870  36.926  17.331  1.00 31.68 ? 142 ILE C N   1 
ATOM   4814 C CA  . ILE C 1 142 ? 26.848  36.934  18.816  1.00 35.17 ? 142 ILE C CA  1 
ATOM   4815 C C   . ILE C 1 142 ? 28.101  36.251  19.353  1.00 36.65 ? 142 ILE C C   1 
ATOM   4816 O O   . ILE C 1 142 ? 28.876  35.714  18.579  1.00 38.70 ? 142 ILE C O   1 
ATOM   4817 C CB  . ILE C 1 142 ? 25.607  36.201  19.347  1.00 37.03 ? 142 ILE C CB  1 
ATOM   4818 C CG1 . ILE C 1 142 ? 25.469  34.802  18.743  1.00 32.75 ? 142 ILE C CG1 1 
ATOM   4819 C CG2 . ILE C 1 142 ? 24.362  37.038  19.152  1.00 36.56 ? 142 ILE C CG2 1 
ATOM   4820 C CD1 . ILE C 1 142 ? 24.598  33.891  19.537  1.00 30.50 ? 142 ILE C CD1 1 
ATOM   4821 N N   . LYS C 1 143 ? 28.256  36.331  20.665  1.00 40.48 ? 143 LYS C N   1 
ATOM   4822 C CA  . LYS C 1 143 ? 29.313  35.597  21.364  1.00 43.45 ? 143 LYS C CA  1 
ATOM   4823 C C   . LYS C 1 143 ? 28.956  34.106  21.318  1.00 33.70 ? 143 LYS C C   1 
ATOM   4824 O O   . LYS C 1 143 ? 27.828  33.727  21.325  1.00 40.81 ? 143 LYS C O   1 
ATOM   4825 C CB  . LYS C 1 143 ? 29.499  36.146  22.782  1.00 40.80 ? 143 LYS C CB  1 
ATOM   4826 C CG  . LYS C 1 143 ? 30.049  37.564  22.858  1.00 48.84 ? 143 LYS C CG  1 
ATOM   4827 C CD  . LYS C 1 143 ? 29.271  38.606  22.064  1.00 55.34 ? 143 LYS C CD  1 
ATOM   4828 C CE  . LYS C 1 143 ? 30.125  39.741  21.531  1.00 60.35 ? 143 LYS C CE  1 
ATOM   4829 N NZ  . LYS C 1 143 ? 29.745  40.181  20.164  1.00 60.15 ? 143 LYS C NZ  1 
ATOM   4830 N N   . ARG C 1 144 ? 30.002  33.333  21.269  1.00 40.41 ? 144 ARG C N   1 
ATOM   4831 C CA  . ARG C 1 144 ? 30.176  31.876  21.231  1.00 38.81 ? 144 ARG C CA  1 
ATOM   4832 C C   . ARG C 1 144 ? 30.119  31.523  22.691  1.00 38.89 ? 144 ARG C C   1 
ATOM   4833 O O   . ARG C 1 144 ? 31.048  31.002  23.299  1.00 38.31 ? 144 ARG C O   1 
ATOM   4834 C CB  . ARG C 1 144 ? 31.452  31.376  20.556  1.00 31.16 ? 144 ARG C CB  1 
ATOM   4835 C CG  . ARG C 1 144 ? 31.702  31.740  19.099  1.00 31.89 ? 144 ARG C CG  1 
ATOM   4836 C CD  . ARG C 1 144 ? 33.053  31.224  18.551  1.00 33.83 ? 144 ARG C CD  1 
ATOM   4837 N NE  . ARG C 1 144 ? 33.016  29.783  18.257  1.00 30.56 ? 144 ARG C NE  1 
ATOM   4838 C CZ  . ARG C 1 144 ? 32.702  29.255  17.073  1.00 31.76 ? 144 ARG C CZ  1 
ATOM   4839 N NH1 . ARG C 1 144 ? 32.264  30.000  16.076  1.00 30.31 ? 144 ARG C NH1 1 
ATOM   4840 N NH2 . ARG C 1 144 ? 32.885  27.952  16.870  1.00 31.15 ? 144 ARG C NH2 1 
ATOM   4841 N N   . ASP C 1 145 ? 28.914  31.728  23.203  1.00 38.06 ? 145 ASP C N   1 
ATOM   4842 C CA  . ASP C 1 145 ? 28.621  31.591  24.607  1.00 40.02 ? 145 ASP C CA  1 
ATOM   4843 C C   . ASP C 1 145 ? 27.226  31.000  24.719  1.00 38.77 ? 145 ASP C C   1 
ATOM   4844 O O   . ASP C 1 145 ? 26.284  31.519  24.110  1.00 39.08 ? 145 ASP C O   1 
ATOM   4845 C CB  . ASP C 1 145 ? 28.704  32.950  25.308  1.00 42.21 ? 145 ASP C CB  1 
ATOM   4846 C CG  . ASP C 1 145 ? 28.093  32.915  26.680  1.00 43.02 ? 145 ASP C CG  1 
ATOM   4847 O OD1 . ASP C 1 145 ? 26.858  32.876  26.795  1.00 46.11 ? 145 ASP C OD1 1 
ATOM   4848 O OD2 . ASP C 1 145 ? 28.849  32.879  27.661  1.00 50.84 ? 145 ASP C OD2 1 
ATOM   4849 N N   . SER C 1 146 ? 27.085  29.949  25.526  1.00 35.89 ? 146 SER C N   1 
ATOM   4850 C CA  . SER C 1 146 ? 25.805  29.252  25.591  1.00 39.00 ? 146 SER C CA  1 
ATOM   4851 C C   . SER C 1 146 ? 24.686  30.152  26.099  1.00 41.41 ? 146 SER C C   1 
ATOM   4852 O O   . SER C 1 146 ? 23.522  29.944  25.737  1.00 38.05 ? 146 SER C O   1 
ATOM   4853 C CB  . SER C 1 146 ? 25.898  28.009  26.474  1.00 38.88 ? 146 SER C CB  1 
ATOM   4854 O OG  . SER C 1 146 ? 26.198  28.373  27.808  1.00 44.08 ? 146 SER C OG  1 
ATOM   4855 N N   . LYS C 1 147 ? 25.002  31.133  26.958  1.00 42.32 ? 147 LYS C N   1 
ATOM   4856 C CA  . LYS C 1 147 ? 23.946  32.002  27.474  1.00 39.19 ? 147 LYS C CA  1 
ATOM   4857 C C   . LYS C 1 147 ? 23.390  32.877  26.365  1.00 39.81 ? 147 LYS C C   1 
ATOM   4858 O O   . LYS C 1 147 ? 22.171  33.056  26.267  1.00 38.44 ? 147 LYS C O   1 
ATOM   4859 C CB  . LYS C 1 147 ? 24.461  32.842  28.644  1.00 41.89 ? 147 LYS C CB  1 
ATOM   4860 C CG  . LYS C 1 147 ? 24.847  32.032  29.886  1.00 41.98 ? 147 LYS C CG  1 
ATOM   4861 C CD  . LYS C 1 147 ? 23.742  31.046  30.317  1.00 49.65 ? 147 LYS C CD  1 
ATOM   4862 C CE  . LYS C 1 147 ? 24.318  29.743  30.904  1.00 51.81 ? 147 LYS C CE  1 
ATOM   4863 N NZ  . LYS C 1 147 ? 24.395  28.606  29.908  1.00 40.18 ? 147 LYS C NZ  1 
ATOM   4864 N N   . GLU C 1 148 ? 24.268  33.401  25.500  1.00 37.98 ? 148 GLU C N   1 
ATOM   4865 C CA  . GLU C 1 148 ? 23.812  34.171  24.345  1.00 38.81 ? 148 GLU C CA  1 
ATOM   4866 C C   . GLU C 1 148 ? 23.022  33.304  23.371  1.00 37.19 ? 148 GLU C C   1 
ATOM   4867 O O   . GLU C 1 148 ? 22.001  33.745  22.828  1.00 36.41 ? 148 GLU C O   1 
ATOM   4868 C CB  . GLU C 1 148 ? 24.998  34.825  23.634  1.00 38.69 ? 148 GLU C CB  1 
ATOM   4869 C CG  . GLU C 1 148 ? 25.580  35.968  24.394  1.00 41.94 ? 148 GLU C CG  1 
ATOM   4870 C CD  . GLU C 1 148 ? 24.586  37.100  24.535  1.00 42.84 ? 148 GLU C CD  1 
ATOM   4871 O OE1 . GLU C 1 148 ? 24.319  37.775  23.519  1.00 44.11 ? 148 GLU C OE1 1 
ATOM   4872 O OE2 . GLU C 1 148 ? 24.058  37.298  25.648  1.00 42.53 ? 148 GLU C OE2 1 
ATOM   4873 N N   . VAL C 1 149 ? 23.474  32.074  23.123  1.00 34.60 ? 149 VAL C N   1 
ATOM   4874 C CA  . VAL C 1 149 ? 22.709  31.188  22.250  1.00 35.31 ? 149 VAL C CA  1 
ATOM   4875 C C   . VAL C 1 149 ? 21.312  30.964  22.815  1.00 35.06 ? 149 VAL C C   1 
ATOM   4876 O O   . VAL C 1 149 ? 20.313  31.119  22.103  1.00 32.65 ? 149 VAL C O   1 
ATOM   4877 C CB  . VAL C 1 149 ? 23.452  29.857  22.030  1.00 34.96 ? 149 VAL C CB  1 
ATOM   4878 C CG1 . VAL C 1 149 ? 22.575  28.917  21.206  1.00 31.16 ? 149 VAL C CG1 1 
ATOM   4879 C CG2 . VAL C 1 149 ? 24.796  30.116  21.322  1.00 31.46 ? 149 VAL C CG2 1 
ATOM   4880 N N   . LYS C 1 150 ? 21.227  30.583  24.102  1.00 35.10 ? 150 LYS C N   1 
ATOM   4881 C CA  . LYS C 1 150 ? 19.937  30.418  24.789  1.00 35.68 ? 150 LYS C CA  1 
ATOM   4882 C C   . LYS C 1 150 ? 19.048  31.658  24.688  1.00 34.90 ? 150 LYS C C   1 
ATOM   4883 O O   . LYS C 1 150 ? 17.824  31.538  24.526  1.00 36.82 ? 150 LYS C O   1 
ATOM   4884 C CB  . LYS C 1 150 ? 20.155  30.062  26.256  1.00 38.10 ? 150 LYS C CB  1 
ATOM   4885 C CG  . LYS C 1 150 ? 18.892  29.532  26.942  1.00 42.30 ? 150 LYS C CG  1 
ATOM   4886 C CD  . LYS C 1 150 ? 19.191  29.083  28.372  1.00 51.43 ? 150 LYS C CD  1 
ATOM   4887 C CE  . LYS C 1 150 ? 18.180  28.032  28.888  1.00 50.51 ? 150 LYS C CE  1 
ATOM   4888 N NZ  . LYS C 1 150 ? 17.375  27.361  27.812  1.00 55.27 ? 150 LYS C NZ  1 
ATOM   4889 N N   . LYS C 1 151 ? 19.633  32.852  24.843  1.00 35.69 ? 151 LYS C N   1 
ATOM   4890 C CA  . LYS C 1 151 ? 18.840  34.079  24.813  1.00 37.09 ? 151 LYS C CA  1 
ATOM   4891 C C   . LYS C 1 151 ? 18.062  34.201  23.504  1.00 39.03 ? 151 LYS C C   1 
ATOM   4892 O O   . LYS C 1 151 ? 16.869  34.542  23.511  1.00 37.22 ? 151 LYS C O   1 
ATOM   4893 C CB  . LYS C 1 151 ? 19.733  35.293  25.025  1.00 39.66 ? 151 LYS C CB  1 
ATOM   4894 C CG  . LYS C 1 151 ? 19.068  36.627  24.738  1.00 37.07 ? 151 LYS C CG  1 
ATOM   4895 C CD  . LYS C 1 151 ? 20.065  37.764  24.914  1.00 41.71 ? 151 LYS C CD  1 
ATOM   4896 C CE  . LYS C 1 151 ? 19.697  38.966  24.073  1.00 43.58 ? 151 LYS C CE  1 
ATOM   4897 N NZ  . LYS C 1 151 ? 20.342  40.187  24.593  1.00 48.72 ? 151 LYS C NZ  1 
ATOM   4898 N N   . TYR C 1 152 ? 18.711  33.892  22.373  1.00 36.59 ? 152 TYR C N   1 
ATOM   4899 C CA  . TYR C 1 152 ? 18.044  34.009  21.080  1.00 33.75 ? 152 TYR C CA  1 
ATOM   4900 C C   . TYR C 1 152 ? 17.194  32.788  20.738  1.00 32.59 ? 152 TYR C C   1 
ATOM   4901 O O   . TYR C 1 152 ? 16.140  32.942  20.110  1.00 33.97 ? 152 TYR C O   1 
ATOM   4902 C CB  . TYR C 1 152 ? 19.089  34.303  20.009  1.00 31.64 ? 152 TYR C CB  1 
ATOM   4903 C CG  . TYR C 1 152 ? 19.627  35.684  20.195  1.00 34.03 ? 152 TYR C CG  1 
ATOM   4904 C CD1 . TYR C 1 152 ? 18.876  36.792  19.817  1.00 34.97 ? 152 TYR C CD1 1 
ATOM   4905 C CD2 . TYR C 1 152 ? 20.849  35.898  20.824  1.00 36.35 ? 152 TYR C CD2 1 
ATOM   4906 C CE1 . TYR C 1 152 ? 19.352  38.088  20.009  1.00 34.96 ? 152 TYR C CE1 1 
ATOM   4907 C CE2 . TYR C 1 152 ? 21.337  37.191  21.026  1.00 38.80 ? 152 TYR C CE2 1 
ATOM   4908 C CZ  . TYR C 1 152 ? 20.578  38.284  20.618  1.00 40.57 ? 152 TYR C CZ  1 
ATOM   4909 O OH  . TYR C 1 152 ? 21.043  39.574  20.811  1.00 43.91 ? 152 TYR C OH  1 
ATOM   4910 N N   . LEU C 1 153 ? 17.602  31.582  21.152  1.00 29.52 ? 153 LEU C N   1 
ATOM   4911 C CA  . LEU C 1 153 ? 16.736  30.420  20.992  1.00 31.80 ? 153 LEU C CA  1 
ATOM   4912 C C   . LEU C 1 153 ? 15.407  30.639  21.710  1.00 35.45 ? 153 LEU C C   1 
ATOM   4913 O O   . LEU C 1 153 ? 14.350  30.189  21.247  1.00 34.78 ? 153 LEU C O   1 
ATOM   4914 C CB  . LEU C 1 153 ? 17.418  29.163  21.534  1.00 32.42 ? 153 LEU C CB  1 
ATOM   4915 C CG  . LEU C 1 153 ? 18.613  28.594  20.769  1.00 32.16 ? 153 LEU C CG  1 
ATOM   4916 C CD1 . LEU C 1 153 ? 19.150  27.334  21.466  1.00 31.04 ? 153 LEU C CD1 1 
ATOM   4917 C CD2 . LEU C 1 153 ? 18.189  28.282  19.338  1.00 28.92 ? 153 LEU C CD2 1 
ATOM   4918 N N   . LYS C 1 154 ? 15.445  31.313  22.859  1.00 36.70 ? 154 LYS C N   1 
ATOM   4919 C CA  . LYS C 1 154 ? 14.214  31.565  23.604  1.00 38.45 ? 154 LYS C CA  1 
ATOM   4920 C C   . LYS C 1 154 ? 13.287  32.506  22.851  1.00 39.84 ? 154 LYS C C   1 
ATOM   4921 O O   . LYS C 1 154 ? 12.080  32.501  23.111  1.00 40.18 ? 154 LYS C O   1 
ATOM   4922 C CB  . LYS C 1 154 ? 14.533  32.150  24.981  1.00 37.96 ? 154 LYS C CB  1 
ATOM   4923 C CG  . LYS C 1 154 ? 14.490  31.158  26.128  1.00 43.04 ? 154 LYS C CG  1 
ATOM   4924 C CD  . LYS C 1 154 ? 13.796  31.773  27.341  1.00 49.05 ? 154 LYS C CD  1 
ATOM   4925 C CE  . LYS C 1 154 ? 14.115  31.043  28.643  1.00 54.87 ? 154 LYS C CE  1 
ATOM   4926 N NZ  . LYS C 1 154 ? 14.474  32.004  29.740  1.00 56.63 ? 154 LYS C NZ  1 
ATOM   4927 N N   . LYS C 1 155 ? 13.818  33.293  21.916  1.00 35.20 ? 155 LYS C N   1 
ATOM   4928 C CA  . LYS C 1 155 ? 13.003  34.126  21.047  1.00 37.45 ? 155 LYS C CA  1 
ATOM   4929 C C   . LYS C 1 155 ? 12.500  33.391  19.812  1.00 36.97 ? 155 LYS C C   1 
ATOM   4930 O O   . LYS C 1 155 ? 11.798  34.000  18.995  1.00 39.50 ? 155 LYS C O   1 
ATOM   4931 C CB  . LYS C 1 155 ? 13.793  35.352  20.607  1.00 35.73 ? 155 LYS C CB  1 
ATOM   4932 C CG  . LYS C 1 155 ? 14.296  36.170  21.750  1.00 37.10 ? 155 LYS C CG  1 
ATOM   4933 C CD  . LYS C 1 155 ? 15.088  37.339  21.246  1.00 37.16 ? 155 LYS C CD  1 
ATOM   4934 C CE  . LYS C 1 155 ? 15.439  38.246  22.411  1.00 39.31 ? 155 LYS C CE  1 
ATOM   4935 N NZ  . LYS C 1 155 ? 14.553  39.443  22.379  1.00 47.76 ? 155 LYS C NZ  1 
ATOM   4936 N N   . GLY C 1 156 ? 12.817  32.110  19.670  1.00 32.38 ? 156 GLY C N   1 
ATOM   4937 C CA  . GLY C 1 156 ? 12.495  31.360  18.477  1.00 32.42 ? 156 GLY C CA  1 
ATOM   4938 C C   . GLY C 1 156 ? 13.467  31.554  17.327  1.00 34.12 ? 156 GLY C C   1 
ATOM   4939 O O   . GLY C 1 156 ? 13.173  31.113  16.208  1.00 32.29 ? 156 GLY C O   1 
ATOM   4940 N N   . PHE C 1 157 ? 14.635  32.163  17.563  1.00 25.78 ? 157 PHE C N   1 
ATOM   4941 C CA  . PHE C 1 157 ? 15.589  32.383  16.480  1.00 27.72 ? 157 PHE C CA  1 
ATOM   4942 C C   . PHE C 1 157 ? 16.665  31.308  16.546  1.00 29.95 ? 157 PHE C C   1 
ATOM   4943 O O   . PHE C 1 157 ? 17.363  31.230  17.567  1.00 30.22 ? 157 PHE C O   1 
ATOM   4944 C CB  . PHE C 1 157 ? 16.241  33.759  16.584  1.00 27.92 ? 157 PHE C CB  1 
ATOM   4945 C CG  . PHE C 1 157 ? 15.282  34.922  16.597  1.00 29.78 ? 157 PHE C CG  1 
ATOM   4946 C CD1 . PHE C 1 157 ? 14.043  34.851  15.986  1.00 28.23 ? 157 PHE C CD1 1 
ATOM   4947 C CD2 . PHE C 1 157 ? 15.668  36.128  17.181  1.00 32.05 ? 157 PHE C CD2 1 
ATOM   4948 C CE1 . PHE C 1 157 ? 13.195  35.948  15.989  1.00 32.39 ? 157 PHE C CE1 1 
ATOM   4949 C CE2 . PHE C 1 157 ? 14.828  37.218  17.182  1.00 27.61 ? 157 PHE C CE2 1 
ATOM   4950 C CZ  . PHE C 1 157 ? 13.587  37.122  16.583  1.00 29.90 ? 157 PHE C CZ  1 
ATOM   4951 N N   . PRO C 1 158 ? 16.862  30.488  15.518  1.00 23.61 ? 158 PRO C N   1 
ATOM   4952 C CA  . PRO C 1 158 ? 17.948  29.504  15.550  1.00 22.54 ? 158 PRO C CA  1 
ATOM   4953 C C   . PRO C 1 158 ? 19.286  30.181  15.258  1.00 26.13 ? 158 PRO C C   1 
ATOM   4954 O O   . PRO C 1 158 ? 19.348  31.318  14.799  1.00 26.51 ? 158 PRO C O   1 
ATOM   4955 C CB  . PRO C 1 158 ? 17.559  28.527  14.432  1.00 25.70 ? 158 PRO C CB  1 
ATOM   4956 C CG  . PRO C 1 158 ? 16.876  29.421  13.424  1.00 26.63 ? 158 PRO C CG  1 
ATOM   4957 C CD  . PRO C 1 158 ? 16.162  30.509  14.219  1.00 25.33 ? 158 PRO C CD  1 
ATOM   4958 N N   . VAL C 1 159 ? 20.378  29.453  15.498  1.00 23.75 ? 159 VAL C N   1 
ATOM   4959 C CA  . VAL C 1 159 ? 21.702  30.068  15.507  1.00 24.67 ? 159 VAL C CA  1 
ATOM   4960 C C   . VAL C 1 159 ? 22.637  29.239  14.642  1.00 25.18 ? 159 VAL C C   1 
ATOM   4961 O O   . VAL C 1 159 ? 22.897  28.069  14.946  1.00 25.35 ? 159 VAL C O   1 
ATOM   4962 C CB  . VAL C 1 159 ? 22.264  30.198  16.938  1.00 28.70 ? 159 VAL C CB  1 
ATOM   4963 C CG1 . VAL C 1 159 ? 23.656  30.839  16.912  1.00 28.60 ? 159 VAL C CG1 1 
ATOM   4964 C CG2 . VAL C 1 159 ? 21.299  30.990  17.844  1.00 27.37 ? 159 VAL C CG2 1 
ATOM   4965 N N   . ILE C 1 160 ? 23.134  29.836  13.563  1.00 27.21 ? 160 ILE C N   1 
ATOM   4966 C CA  . ILE C 1 160 ? 24.116  29.167  12.728  1.00 27.04 ? 160 ILE C CA  1 
ATOM   4967 C C   . ILE C 1 160 ? 25.450  29.136  13.465  1.00 27.80 ? 160 ILE C C   1 
ATOM   4968 O O   . ILE C 1 160 ? 25.912  30.161  13.976  1.00 26.95 ? 160 ILE C O   1 
ATOM   4969 C CB  . ILE C 1 160 ? 24.235  29.882  11.377  1.00 22.94 ? 160 ILE C CB  1 
ATOM   4970 C CG1 . ILE C 1 160 ? 22.955  29.690  10.562  1.00 26.26 ? 160 ILE C CG1 1 
ATOM   4971 C CG2 . ILE C 1 160 ? 25.473  29.384  10.584  1.00 23.27 ? 160 ILE C CG2 1 
ATOM   4972 C CD1 . ILE C 1 160 ? 22.975  30.424  9.197   1.00 25.29 ? 160 ILE C CD1 1 
ATOM   4973 N N   . CYS C 1 161 ? 26.064  27.953  13.547  1.00 25.49 ? 161 CYS C N   1 
ATOM   4974 C CA  . CYS C 1 161 ? 27.380  27.810  14.152  1.00 27.82 ? 161 CYS C CA  1 
ATOM   4975 C C   . CYS C 1 161 ? 28.433  27.560  13.075  1.00 28.39 ? 161 CYS C C   1 
ATOM   4976 O O   . CYS C 1 161 ? 28.130  27.016  12.005  1.00 27.84 ? 161 CYS C O   1 
ATOM   4977 C CB  . CYS C 1 161 ? 27.405  26.666  15.170  1.00 29.02 ? 161 CYS C CB  1 
ATOM   4978 S SG  . CYS C 1 161 ? 26.839  25.083  14.544  1.00 30.34 ? 161 CYS C SG  1 
ATOM   4979 N N   . HIS C 1 162 ? 29.663  27.995  13.354  1.00 25.89 ? 162 HIS C N   1 
ATOM   4980 C CA  . HIS C 1 162 ? 30.790  27.894  12.428  1.00 28.57 ? 162 HIS C CA  1 
ATOM   4981 C C   . HIS C 1 162 ? 31.972  27.345  13.220  1.00 29.57 ? 162 HIS C C   1 
ATOM   4982 O O   . HIS C 1 162 ? 32.247  27.820  14.332  1.00 29.06 ? 162 HIS C O   1 
ATOM   4983 C CB  . HIS C 1 162 ? 31.119  29.279  11.800  1.00 28.56 ? 162 HIS C CB  1 
ATOM   4984 C CG  . HIS C 1 162 ? 32.331  29.302  10.912  1.00 30.72 ? 162 HIS C CG  1 
ATOM   4985 N ND1 . HIS C 1 162 ? 33.263  30.324  10.951  1.00 33.10 ? 162 HIS C ND1 1 
ATOM   4986 C CD2 . HIS C 1 162 ? 32.727  28.475  9.912   1.00 30.52 ? 162 HIS C CD2 1 
ATOM   4987 C CE1 . HIS C 1 162 ? 34.189  30.112  10.032  1.00 32.39 ? 162 HIS C CE1 1 
ATOM   4988 N NE2 . HIS C 1 162 ? 33.894  28.992  9.393   1.00 35.39 ? 162 HIS C NE2 1 
ATOM   4989 N N   . TRP C 1 163 ? 32.638  26.322  12.683  1.00 29.59 ? 163 TRP C N   1 
ATOM   4990 C CA  . TRP C 1 163 ? 33.748  25.726  13.418  1.00 30.11 ? 163 TRP C CA  1 
ATOM   4991 C C   . TRP C 1 163 ? 34.613  24.888  12.492  1.00 29.59 ? 163 TRP C C   1 
ATOM   4992 O O   . TRP C 1 163 ? 34.230  24.562  11.362  1.00 31.05 ? 163 TRP C O   1 
ATOM   4993 C CB  . TRP C 1 163 ? 33.240  24.906  14.619  1.00 29.62 ? 163 TRP C CB  1 
ATOM   4994 C CG  . TRP C 1 163 ? 32.791  23.467  14.389  1.00 30.25 ? 163 TRP C CG  1 
ATOM   4995 C CD1 . TRP C 1 163 ? 33.457  22.334  14.763  1.00 32.71 ? 163 TRP C CD1 1 
ATOM   4996 C CD2 . TRP C 1 163 ? 31.554  23.022  13.801  1.00 29.18 ? 163 TRP C CD2 1 
ATOM   4997 N NE1 . TRP C 1 163 ? 32.718  21.211  14.435  1.00 29.49 ? 163 TRP C NE1 1 
ATOM   4998 C CE2 . TRP C 1 163 ? 31.557  21.610  13.831  1.00 30.90 ? 163 TRP C CE2 1 
ATOM   4999 C CE3 . TRP C 1 163 ? 30.462  23.678  13.228  1.00 27.94 ? 163 TRP C CE3 1 
ATOM   5000 C CZ2 . TRP C 1 163 ? 30.505  20.849  13.326  1.00 29.57 ? 163 TRP C CZ2 1 
ATOM   5001 C CZ3 . TRP C 1 163 ? 29.422  22.919  12.725  1.00 27.37 ? 163 TRP C CZ3 1 
ATOM   5002 C CH2 . TRP C 1 163 ? 29.448  21.524  12.779  1.00 30.11 ? 163 TRP C CH2 1 
ATOM   5003 N N   . GLN C 1 164 ? 35.804  24.574  12.982  1.00 28.77 ? 164 GLN C N   1 
ATOM   5004 C CA  . GLN C 1 164 ? 36.758  23.731  12.270  1.00 31.05 ? 164 GLN C CA  1 
ATOM   5005 C C   . GLN C 1 164 ? 36.611  22.321  12.819  1.00 30.65 ? 164 GLN C C   1 
ATOM   5006 O O   . GLN C 1 164 ? 36.830  22.095  14.015  1.00 30.90 ? 164 GLN C O   1 
ATOM   5007 C CB  . GLN C 1 164 ? 38.189  24.248  12.446  1.00 33.52 ? 164 GLN C CB  1 
ATOM   5008 C CG  . GLN C 1 164 ? 38.308  25.747  12.250  1.00 32.13 ? 164 GLN C CG  1 
ATOM   5009 C CD  . GLN C 1 164 ? 37.958  26.166  10.839  1.00 34.05 ? 164 GLN C CD  1 
ATOM   5010 O OE1 . GLN C 1 164 ? 38.476  25.608  9.870   1.00 36.22 ? 164 GLN C OE1 1 
ATOM   5011 N NE2 . GLN C 1 164 ? 37.049  27.122  10.711  1.00 31.49 ? 164 GLN C NE2 1 
ATOM   5012 N N   . VAL C 1 165 ? 36.184  21.388  11.965  1.00 31.66 ? 165 VAL C N   1 
ATOM   5013 C CA  . VAL C 1 165 ? 35.820  20.068  12.469  1.00 32.99 ? 165 VAL C CA  1 
ATOM   5014 C C   . VAL C 1 165 ? 37.021  19.379  13.116  1.00 35.81 ? 165 VAL C C   1 
ATOM   5015 O O   . VAL C 1 165 ? 36.867  18.650  14.103  1.00 34.11 ? 165 VAL C O   1 
ATOM   5016 C CB  . VAL C 1 165 ? 35.189  19.225  11.344  1.00 31.48 ? 165 VAL C CB  1 
ATOM   5017 C CG1 . VAL C 1 165 ? 33.936  19.908  10.821  1.00 30.16 ? 165 VAL C CG1 1 
ATOM   5018 C CG2 . VAL C 1 165 ? 36.178  18.973  10.209  1.00 30.51 ? 165 VAL C CG2 1 
ATOM   5019 N N   . ASN C 1 166 ? 38.234  19.658  12.627  1.00 33.92 ? 166 ASN C N   1 
ATOM   5020 C CA  . ASN C 1 166 ? 39.433  19.076  13.219  1.00 31.79 ? 166 ASN C CA  1 
ATOM   5021 C C   . ASN C 1 166 ? 39.628  19.535  14.656  1.00 33.92 ? 166 ASN C C   1 
ATOM   5022 O O   . ASN C 1 166 ? 40.226  18.817  15.462  1.00 35.06 ? 166 ASN C O   1 
ATOM   5023 C CB  . ASN C 1 166 ? 40.660  19.454  12.389  1.00 37.45 ? 166 ASN C CB  1 
ATOM   5024 C CG  . ASN C 1 166 ? 40.618  20.906  11.910  1.00 39.90 ? 166 ASN C CG  1 
ATOM   5025 O OD1 . ASN C 1 166 ? 39.796  21.301  11.053  1.00 38.59 ? 166 ASN C OD1 1 
ATOM   5026 N ND2 . ASN C 1 166 ? 41.478  21.722  12.509  1.00 38.57 ? 166 ASN C ND2 1 
ATOM   5027 N N   . GLN C 1 167 ? 39.141  20.733  14.996  1.00 34.77 ? 167 GLN C N   1 
ATOM   5028 C CA  . GLN C 1 167 ? 39.236  21.246  16.361  1.00 35.72 ? 167 GLN C CA  1 
ATOM   5029 C C   . GLN C 1 167 ? 38.195  20.646  17.309  1.00 39.21 ? 167 GLN C C   1 
ATOM   5030 O O   . GLN C 1 167 ? 38.248  20.899  18.519  1.00 39.77 ? 167 GLN C O   1 
ATOM   5031 C CB  . GLN C 1 167 ? 39.120  22.781  16.340  1.00 34.94 ? 167 GLN C CB  1 
ATOM   5032 C CG  . GLN C 1 167 ? 40.333  23.499  15.735  1.00 34.17 ? 167 GLN C CG  1 
ATOM   5033 C CD  . GLN C 1 167 ? 40.295  25.011  15.961  1.00 35.03 ? 167 GLN C CD  1 
ATOM   5034 O OE1 . GLN C 1 167 ? 39.849  25.477  17.011  1.00 36.03 ? 167 GLN C OE1 1 
ATOM   5035 N NE2 . GLN C 1 167 ? 40.728  25.779  14.961  1.00 34.34 ? 167 GLN C NE2 1 
ATOM   5036 N N   . SER C 1 168 ? 37.244  19.870  16.794  1.00 37.32 ? 168 SER C N   1 
ATOM   5037 C CA  . SER C 1 168 ? 36.273  19.172  17.625  1.00 38.70 ? 168 SER C CA  1 
ATOM   5038 C C   . SER C 1 168 ? 36.460  17.659  17.568  1.00 39.88 ? 168 SER C C   1 
ATOM   5039 O O   . SER C 1 168 ? 35.603  16.915  18.054  1.00 39.43 ? 168 SER C O   1 
ATOM   5040 C CB  . SER C 1 168 ? 34.859  19.578  17.211  1.00 36.81 ? 168 SER C CB  1 
ATOM   5041 O OG  . SER C 1 168 ? 34.530  19.109  15.905  1.00 33.81 ? 168 SER C OG  1 
ATOM   5042 N N   . ARG C 1 169 ? 37.586  17.198  17.032  1.00 41.62 ? 169 ARG C N   1 
ATOM   5043 C CA  . ARG C 1 169 ? 37.793  15.739  16.838  1.00 41.31 ? 169 ARG C CA  1 
ATOM   5044 C C   . ARG C 1 169 ? 37.753  15.003  18.166  1.00 42.88 ? 169 ARG C C   1 
ATOM   5045 O O   . ARG C 1 169 ? 37.150  13.963  18.284  1.00 44.36 ? 169 ARG C O   1 
ATOM   5046 C CB  . ARG C 1 169 ? 39.137  15.429  16.177  1.00 44.62 ? 169 ARG C CB  1 
ATOM   5047 C CG  . ARG C 1 169 ? 39.207  14.008  15.639  1.00 52.74 ? 169 ARG C CG  1 
ATOM   5048 C CD  . ARG C 1 169 ? 40.534  13.286  15.657  1.00 54.68 ? 169 ARG C CD  1 
ATOM   5049 N NE  . ARG C 1 169 ? 41.182  13.149  14.355  1.00 57.54 ? 169 ARG C NE  1 
ATOM   5050 C CZ  . ARG C 1 169 ? 41.519  12.015  13.758  1.00 59.43 ? 169 ARG C CZ  1 
ATOM   5051 N NH1 . ARG C 1 169 ? 42.116  12.050  12.579  1.00 58.47 ? 169 ARG C NH1 1 
ATOM   5052 N NH2 . ARG C 1 169 ? 41.274  10.852  14.323  1.00 63.30 ? 169 ARG C NH2 1 
ATOM   5053 N N   . ASN C 1 170 ? 38.401  15.575  19.137  1.00 44.28 ? 170 ASN C N   1 
ATOM   5054 C CA  . ASN C 1 170 ? 38.512  14.901  20.469  1.00 46.81 ? 170 ASN C CA  1 
ATOM   5055 C C   . ASN C 1 170 ? 37.360  15.133  21.450  1.00 46.06 ? 170 ASN C C   1 
ATOM   5056 O O   . ASN C 1 170 ? 37.136  14.281  22.319  1.00 48.50 ? 170 ASN C O   1 
ATOM   5057 C CB  . ASN C 1 170 ? 39.800  15.312  21.199  1.00 46.40 ? 170 ASN C CB  1 
ATOM   5058 C CG  . ASN C 1 170 ? 41.044  15.031  20.397  1.00 50.70 ? 170 ASN C CG  1 
ATOM   5059 O OD1 . ASN C 1 170 ? 41.148  13.984  19.753  1.00 52.45 ? 170 ASN C OD1 1 
ATOM   5060 N ND2 . ASN C 1 170 ? 42.008  15.940  20.446  1.00 54.31 ? 170 ASN C ND2 1 
ATOM   5061 N N   . CYS C 1 171 ? 36.667  16.270  21.392  1.00 41.96 ? 171 CYS C N   1 
ATOM   5062 C CA  . CYS C 1 171 ? 35.560  16.538  22.305  1.00 42.77 ? 171 CYS C CA  1 
ATOM   5063 C C   . CYS C 1 171 ? 34.223  16.128  21.711  1.00 41.56 ? 171 CYS C C   1 
ATOM   5064 O O   . CYS C 1 171 ? 33.211  16.161  22.410  1.00 46.50 ? 171 CYS C O   1 
ATOM   5065 C CB  . CYS C 1 171 ? 35.523  18.029  22.693  1.00 45.16 ? 171 CYS C CB  1 
ATOM   5066 S SG  . CYS C 1 171 ? 35.568  19.207  21.326  1.00 70.95 ? 171 CYS C SG  1 
ATOM   5067 N N   . LYS C 1 172 ? 34.202  15.726  20.446  1.00 42.90 ? 172 LYS C N   1 
ATOM   5068 C CA  . LYS C 1 172 ? 32.993  15.239  19.802  1.00 40.74 ? 172 LYS C CA  1 
ATOM   5069 C C   . LYS C 1 172 ? 33.325  14.056  18.901  1.00 38.34 ? 172 LYS C C   1 
ATOM   5070 O O   . LYS C 1 172 ? 32.740  12.979  19.051  1.00 37.80 ? 172 LYS C O   1 
ATOM   5071 C CB  . LYS C 1 172 ? 32.319  16.368  19.011  1.00 38.36 ? 172 LYS C CB  1 
ATOM   5072 C CG  . LYS C 1 172 ? 31.127  15.912  18.162  1.00 38.83 ? 172 LYS C CG  1 
ATOM   5073 C CD  . LYS C 1 172 ? 29.920  15.644  19.001  1.00 36.24 ? 172 LYS C CD  1 
ATOM   5074 C CE  . LYS C 1 172 ? 29.004  14.651  18.320  1.00 38.22 ? 172 LYS C CE  1 
ATOM   5075 N NZ  . LYS C 1 172 ? 27.775  14.491  19.120  1.00 39.55 ? 172 LYS C NZ  1 
ATOM   5076 N N   . GLY C 1 173 ? 34.238  14.246  17.952  1.00 38.35 ? 173 GLY C N   1 
ATOM   5077 C CA  . GLY C 1 173 ? 34.714  13.147  17.125  1.00 37.51 ? 173 GLY C CA  1 
ATOM   5078 C C   . GLY C 1 173 ? 33.862  12.721  15.959  1.00 39.65 ? 173 GLY C C   1 
ATOM   5079 O O   . GLY C 1 173 ? 34.015  11.591  15.487  1.00 38.05 ? 173 GLY C O   1 
ATOM   5080 N N   . ASP C 1 174 ? 32.989  13.591  15.447  1.00 36.52 ? 174 ASP C N   1 
ATOM   5081 C CA  . ASP C 1 174 ? 32.232  13.211  14.258  1.00 32.03 ? 174 ASP C CA  1 
ATOM   5082 C C   . ASP C 1 174 ? 33.126  13.162  13.017  1.00 34.48 ? 174 ASP C C   1 
ATOM   5083 O O   . ASP C 1 174 ? 32.832  12.426  12.069  1.00 33.70 ? 174 ASP C O   1 
ATOM   5084 C CB  . ASP C 1 174 ? 31.072  14.178  14.033  1.00 32.58 ? 174 ASP C CB  1 
ATOM   5085 C CG  . ASP C 1 174 ? 29.790  13.750  14.755  1.00 35.29 ? 174 ASP C CG  1 
ATOM   5086 O OD1 . ASP C 1 174 ? 29.824  12.782  15.555  1.00 36.95 ? 174 ASP C OD1 1 
ATOM   5087 O OD2 . ASP C 1 174 ? 28.747  14.400  14.530  1.00 33.75 ? 174 ASP C OD2 1 
ATOM   5088 N N   . TYR C 1 175 ? 34.194  13.955  12.984  1.00 33.52 ? 175 TYR C N   1 
ATOM   5089 C CA  . TYR C 1 175 ? 34.974  14.143  11.770  1.00 33.51 ? 175 TYR C CA  1 
ATOM   5090 C C   . TYR C 1 175 ? 36.431  13.773  11.994  1.00 34.76 ? 175 TYR C C   1 
ATOM   5091 O O   . TYR C 1 175 ? 36.988  14.004  13.071  1.00 36.15 ? 175 TYR C O   1 
ATOM   5092 C CB  . TYR C 1 175 ? 34.888  15.577  11.276  1.00 31.45 ? 175 TYR C CB  1 
ATOM   5093 C CG  . TYR C 1 175 ? 33.505  15.985  10.817  1.00 31.03 ? 175 TYR C CG  1 
ATOM   5094 C CD1 . TYR C 1 175 ? 33.091  15.729  9.523   1.00 32.16 ? 175 TYR C CD1 1 
ATOM   5095 C CD2 . TYR C 1 175 ? 32.630  16.636  11.671  1.00 27.80 ? 175 TYR C CD2 1 
ATOM   5096 C CE1 . TYR C 1 175 ? 31.835  16.088  9.092   1.00 33.65 ? 175 TYR C CE1 1 
ATOM   5097 C CE2 . TYR C 1 175 ? 31.371  17.012  11.248  1.00 28.99 ? 175 TYR C CE2 1 
ATOM   5098 C CZ  . TYR C 1 175 ? 30.978  16.735  9.957   1.00 30.96 ? 175 TYR C CZ  1 
ATOM   5099 O OH  . TYR C 1 175 ? 29.732  17.093  9.513   1.00 27.61 ? 175 TYR C OH  1 
ATOM   5100 N N   . THR C 1 176 ? 37.035  13.190  10.969  1.00 33.65 ? 176 THR C N   1 
ATOM   5101 C CA  . THR C 1 176 ? 38.463  12.922  10.976  1.00 35.70 ? 176 THR C CA  1 
ATOM   5102 C C   . THR C 1 176 ? 39.237  13.890  10.090  1.00 39.47 ? 176 THR C C   1 
ATOM   5103 O O   . THR C 1 176 ? 40.462  13.954  10.194  1.00 38.99 ? 176 THR C O   1 
ATOM   5104 C CB  . THR C 1 176 ? 38.743  11.485  10.505  1.00 34.33 ? 176 THR C CB  1 
ATOM   5105 O OG1 . THR C 1 176 ? 38.119  11.279  9.234   1.00 32.47 ? 176 THR C OG1 1 
ATOM   5106 C CG2 . THR C 1 176 ? 38.190  10.462  11.485  1.00 35.77 ? 176 THR C CG2 1 
ATOM   5107 N N   . GLY C 1 177 ? 38.547  14.641  9.229   1.00 39.01 ? 177 GLY C N   1 
ATOM   5108 C CA  . GLY C 1 177 ? 39.177  15.565  8.312   1.00 36.21 ? 177 GLY C CA  1 
ATOM   5109 C C   . GLY C 1 177 ? 39.452  16.937  8.912   1.00 36.81 ? 177 GLY C C   1 
ATOM   5110 O O   . GLY C 1 177 ? 39.274  17.187  10.100  1.00 34.14 ? 177 GLY C O   1 
ATOM   5111 N N   . ASN C 1 178 ? 39.974  17.819  8.064   1.00 37.97 ? 178 ASN C N   1 
ATOM   5112 C CA  . ASN C 1 178 ? 40.326  19.193  8.433   1.00 37.18 ? 178 ASN C CA  1 
ATOM   5113 C C   . ASN C 1 178 ? 39.666  20.129  7.425   1.00 38.39 ? 178 ASN C C   1 
ATOM   5114 O O   . ASN C 1 178 ? 40.148  20.277  6.299   1.00 39.40 ? 178 ASN C O   1 
ATOM   5115 C CB  . ASN C 1 178 ? 41.839  19.394  8.459   1.00 39.86 ? 178 ASN C CB  1 
ATOM   5116 C CG  . ASN C 1 178 ? 42.549  18.275  9.169   1.00 46.08 ? 178 ASN C CG  1 
ATOM   5117 O OD1 . ASN C 1 178 ? 42.776  17.203  8.598   1.00 55.24 ? 178 ASN C OD1 1 
ATOM   5118 N ND2 . ASN C 1 178 ? 42.943  18.524  10.413  1.00 49.02 ? 178 ASN C ND2 1 
ATOM   5119 N N   . PHE C 1 179 ? 38.585  20.783  7.850   1.00 37.21 ? 179 PHE C N   1 
ATOM   5120 C CA  . PHE C 1 179 ? 37.881  21.770  7.045   1.00 31.71 ? 179 PHE C CA  1 
ATOM   5121 C C   . PHE C 1 179 ? 36.957  22.570  7.954   1.00 31.56 ? 179 PHE C C   1 
ATOM   5122 O O   . PHE C 1 179 ? 36.567  22.103  9.031   1.00 34.71 ? 179 PHE C O   1 
ATOM   5123 C CB  . PHE C 1 179 ? 37.102  21.096  5.905   1.00 29.77 ? 179 PHE C CB  1 
ATOM   5124 C CG  . PHE C 1 179 ? 36.166  19.995  6.356   1.00 32.34 ? 179 PHE C CG  1 
ATOM   5125 C CD1 . PHE C 1 179 ? 34.890  20.294  6.798   1.00 32.46 ? 179 PHE C CD1 1 
ATOM   5126 C CD2 . PHE C 1 179 ? 36.548  18.665  6.310   1.00 32.95 ? 179 PHE C CD2 1 
ATOM   5127 C CE1 . PHE C 1 179 ? 34.006  19.286  7.203   1.00 33.82 ? 179 PHE C CE1 1 
ATOM   5128 C CE2 . PHE C 1 179 ? 35.665  17.659  6.713   1.00 34.24 ? 179 PHE C CE2 1 
ATOM   5129 C CZ  . PHE C 1 179 ? 34.396  17.984  7.162   1.00 29.49 ? 179 PHE C CZ  1 
ATOM   5130 N N   . GLY C 1 180 ? 36.636  23.789  7.522   1.00 30.06 ? 180 GLY C N   1 
ATOM   5131 C CA  . GLY C 1 180 ? 35.644  24.584  8.216   1.00 29.22 ? 180 GLY C CA  1 
ATOM   5132 C C   . GLY C 1 180 ? 34.240  24.171  7.821   1.00 29.24 ? 180 GLY C C   1 
ATOM   5133 O O   . GLY C 1 180 ? 33.981  23.760  6.690   1.00 27.80 ? 180 GLY C O   1 
ATOM   5134 N N   . HIS C 1 181 ? 33.310  24.314  8.758   1.00 27.31 ? 181 HIS C N   1 
ATOM   5135 C CA  . HIS C 1 181 ? 31.992  23.737  8.552   1.00 26.41 ? 181 HIS C CA  1 
ATOM   5136 C C   . HIS C 1 181 ? 30.951  24.596  9.253   1.00 25.25 ? 181 HIS C C   1 
ATOM   5137 O O   . HIS C 1 181 ? 31.271  25.400  10.127  1.00 26.95 ? 181 HIS C O   1 
ATOM   5138 C CB  . HIS C 1 181 ? 31.974  22.287  9.064   1.00 26.41 ? 181 HIS C CB  1 
ATOM   5139 C CG  . HIS C 1 181 ? 30.774  21.501  8.654   1.00 24.13 ? 181 HIS C CG  1 
ATOM   5140 N ND1 . HIS C 1 181 ? 30.308  21.471  7.358   1.00 25.34 ? 181 HIS C ND1 1 
ATOM   5141 C CD2 . HIS C 1 181 ? 29.992  20.644  9.357   1.00 25.54 ? 181 HIS C CD2 1 
ATOM   5142 C CE1 . HIS C 1 181 ? 29.259  20.667  7.289   1.00 28.12 ? 181 HIS C CE1 1 
ATOM   5143 N NE2 . HIS C 1 181 ? 29.045  20.157  8.489   1.00 26.65 ? 181 HIS C NE2 1 
ATOM   5144 N N   . TYR C 1 182 ? 29.692  24.427  8.850   1.00 25.31 ? 182 TYR C N   1 
ATOM   5145 C CA  . TYR C 1 182 ? 28.578  25.143  9.457   1.00 26.41 ? 182 TYR C CA  1 
ATOM   5146 C C   . TYR C 1 182 ? 27.465  24.163  9.796   1.00 25.78 ? 182 TYR C C   1 
ATOM   5147 O O   . TYR C 1 182 ? 27.285  23.159  9.110   1.00 24.56 ? 182 TYR C O   1 
ATOM   5148 C CB  . TYR C 1 182 ? 27.964  26.201  8.518   1.00 27.15 ? 182 TYR C CB  1 
ATOM   5149 C CG  . TYR C 1 182 ? 28.844  27.388  8.131   1.00 27.87 ? 182 TYR C CG  1 
ATOM   5150 C CD1 . TYR C 1 182 ? 29.710  27.303  7.050   1.00 30.79 ? 182 TYR C CD1 1 
ATOM   5151 C CD2 . TYR C 1 182 ? 28.729  28.616  8.784   1.00 30.25 ? 182 TYR C CD2 1 
ATOM   5152 C CE1 . TYR C 1 182 ? 30.498  28.392  6.643   1.00 30.48 ? 182 TYR C CE1 1 
ATOM   5153 C CE2 . TYR C 1 182 ? 29.528  29.708  8.390   1.00 31.54 ? 182 TYR C CE2 1 
ATOM   5154 C CZ  . TYR C 1 182 ? 30.401  29.580  7.323   1.00 28.25 ? 182 TYR C CZ  1 
ATOM   5155 O OH  . TYR C 1 182 ? 31.174  30.651  6.913   1.00 29.84 ? 182 TYR C OH  1 
ATOM   5156 N N   . GLY C 1 183 ? 26.687  24.503  10.827  1.00 25.88 ? 183 GLY C N   1 
ATOM   5157 C CA  . GLY C 1 183 ? 25.480  23.796  11.211  1.00 23.82 ? 183 GLY C CA  1 
ATOM   5158 C C   . GLY C 1 183 ? 24.505  24.797  11.804  1.00 25.24 ? 183 GLY C C   1 
ATOM   5159 O O   . GLY C 1 183 ? 24.779  25.998  11.844  1.00 25.16 ? 183 GLY C O   1 
ATOM   5160 N N   . LEU C 1 184 ? 23.357  24.294  12.270  1.00 22.50 ? 184 LEU C N   1 
ATOM   5161 C CA  . LEU C 1 184 ? 22.315  25.119  12.866  1.00 23.52 ? 184 LEU C CA  1 
ATOM   5162 C C   . LEU C 1 184 ? 22.054  24.647  14.289  1.00 25.75 ? 184 LEU C C   1 
ATOM   5163 O O   . LEU C 1 184 ? 21.530  23.547  14.495  1.00 27.56 ? 184 LEU C O   1 
ATOM   5164 C CB  . LEU C 1 184 ? 21.027  25.046  12.052  1.00 24.28 ? 184 LEU C CB  1 
ATOM   5165 C CG  . LEU C 1 184 ? 19.958  26.040  12.528  1.00 23.32 ? 184 LEU C CG  1 
ATOM   5166 C CD1 . LEU C 1 184 ? 20.284  27.471  12.129  1.00 23.75 ? 184 LEU C CD1 1 
ATOM   5167 C CD2 . LEU C 1 184 ? 18.576  25.625  11.994  1.00 26.44 ? 184 LEU C CD2 1 
ATOM   5168 N N   . ILE C 1 185 ? 22.398  25.474  15.271  1.00 25.97 ? 185 ILE C N   1 
ATOM   5169 C CA  . ILE C 1 185 ? 21.985  25.205  16.641  1.00 28.32 ? 185 ILE C CA  1 
ATOM   5170 C C   . ILE C 1 185 ? 20.505  25.549  16.718  1.00 30.62 ? 185 ILE C C   1 
ATOM   5171 O O   . ILE C 1 185 ? 20.120  26.711  16.558  1.00 27.62 ? 185 ILE C O   1 
ATOM   5172 C CB  . ILE C 1 185 ? 22.786  26.003  17.673  1.00 26.32 ? 185 ILE C CB  1 
ATOM   5173 C CG1 . ILE C 1 185 ? 24.290  25.848  17.460  1.00 28.20 ? 185 ILE C CG1 1 
ATOM   5174 C CG2 . ILE C 1 185 ? 22.323  25.618  19.096  1.00 29.10 ? 185 ILE C CG2 1 
ATOM   5175 C CD1 . ILE C 1 185 ? 25.082  26.777  18.312  1.00 29.32 ? 185 ILE C CD1 1 
ATOM   5176 N N   . TRP C 1 186 ? 19.673  24.536  16.928  1.00 28.32 ? 186 TRP C N   1 
ATOM   5177 C CA  . TRP C 1 186 ? 18.246  24.762  17.036  1.00 30.27 ? 186 TRP C CA  1 
ATOM   5178 C C   . TRP C 1 186 ? 17.693  24.416  18.404  1.00 31.65 ? 186 TRP C C   1 
ATOM   5179 O O   . TRP C 1 186 ? 16.496  24.610  18.631  1.00 29.96 ? 186 TRP C O   1 
ATOM   5180 C CB  . TRP C 1 186 ? 17.506  23.971  15.946  1.00 26.84 ? 186 TRP C CB  1 
ATOM   5181 C CG  . TRP C 1 186 ? 17.708  22.495  15.974  1.00 29.35 ? 186 TRP C CG  1 
ATOM   5182 C CD1 . TRP C 1 186 ? 18.693  21.787  15.360  1.00 29.14 ? 186 TRP C CD1 1 
ATOM   5183 C CD2 . TRP C 1 186 ? 16.844  21.526  16.596  1.00 31.73 ? 186 TRP C CD2 1 
ATOM   5184 N NE1 . TRP C 1 186 ? 18.529  20.436  15.600  1.00 29.15 ? 186 TRP C NE1 1 
ATOM   5185 C CE2 . TRP C 1 186 ? 17.393  20.257  16.349  1.00 29.41 ? 186 TRP C CE2 1 
ATOM   5186 C CE3 . TRP C 1 186 ? 15.667  21.620  17.349  1.00 32.10 ? 186 TRP C CE3 1 
ATOM   5187 C CZ2 . TRP C 1 186 ? 16.806  19.089  16.820  1.00 31.99 ? 186 TRP C CZ2 1 
ATOM   5188 C CZ3 . TRP C 1 186 ? 15.087  20.462  17.820  1.00 32.10 ? 186 TRP C CZ3 1 
ATOM   5189 C CH2 . TRP C 1 186 ? 15.663  19.211  17.565  1.00 36.91 ? 186 TRP C CH2 1 
ATOM   5190 N N   . ASP C 1 187 ? 18.515  23.899  19.316  1.00 31.68 ? 187 ASP C N   1 
ATOM   5191 C CA  . ASP C 1 187 ? 18.040  23.517  20.642  1.00 33.84 ? 187 ASP C CA  1 
ATOM   5192 C C   . ASP C 1 187 ? 19.256  23.371  21.547  1.00 34.74 ? 187 ASP C C   1 
ATOM   5193 O O   . ASP C 1 187 ? 20.404  23.424  21.091  1.00 30.46 ? 187 ASP C O   1 
ATOM   5194 C CB  . ASP C 1 187 ? 17.207  22.232  20.584  1.00 32.33 ? 187 ASP C CB  1 
ATOM   5195 C CG  . ASP C 1 187 ? 16.311  22.034  21.827  1.00 37.16 ? 187 ASP C CG  1 
ATOM   5196 O OD1 . ASP C 1 187 ? 16.283  22.912  22.704  1.00 33.08 ? 187 ASP C OD1 1 
ATOM   5197 O OD2 . ASP C 1 187 ? 15.620  20.999  21.902  1.00 35.17 ? 187 ASP C OD2 1 
ATOM   5198 N N   . MET C 1 188 ? 18.996  23.199  22.842  1.00 33.12 ? 188 MET C N   1 
ATOM   5199 C CA  . MET C 1 188 ? 20.072  23.070  23.817  1.00 36.01 ? 188 MET C CA  1 
ATOM   5200 C C   . MET C 1 188 ? 19.591  22.173  24.951  1.00 39.71 ? 188 MET C C   1 
ATOM   5201 O O   . MET C 1 188 ? 18.419  22.249  25.335  1.00 35.95 ? 188 MET C O   1 
ATOM   5202 C CB  . MET C 1 188 ? 20.431  24.444  24.385  1.00 36.30 ? 188 MET C CB  1 
ATOM   5203 C CG  . MET C 1 188 ? 21.541  25.215  23.723  1.00 34.69 ? 188 MET C CG  1 
ATOM   5204 S SD  . MET C 1 188 ? 21.500  26.896  24.478  1.00 45.93 ? 188 MET C SD  1 
ATOM   5205 C CE  . MET C 1 188 ? 22.466  26.633  25.977  1.00 40.12 ? 188 MET C CE  1 
ATOM   5206 N N   . THR C 1 189 ? 20.497  21.361  25.506  1.00 37.03 ? 189 THR C N   1 
ATOM   5207 C CA  . THR C 1 189 ? 20.295  20.719  26.799  1.00 38.28 ? 189 THR C CA  1 
ATOM   5208 C C   . THR C 1 189 ? 20.951  21.580  27.871  1.00 42.60 ? 189 THR C C   1 
ATOM   5209 O O   . THR C 1 189 ? 21.324  22.736  27.629  1.00 41.15 ? 189 THR C O   1 
ATOM   5210 C CB  . THR C 1 189 ? 20.895  19.316  26.836  1.00 38.64 ? 189 THR C CB  1 
ATOM   5211 O OG1 . THR C 1 189 ? 22.326  19.398  26.697  1.00 39.48 ? 189 THR C OG1 1 
ATOM   5212 C CG2 . THR C 1 189 ? 20.297  18.463  25.729  1.00 36.04 ? 189 THR C CG2 1 
ATOM   5213 N N   . SER C 1 190 ? 21.110  21.026  29.075  1.00 39.86 ? 190 SER C N   1 
ATOM   5214 C CA  . SER C 1 190 ? 21.841  21.767  30.097  1.00 41.21 ? 190 SER C CA  1 
ATOM   5215 C C   . SER C 1 190 ? 23.332  21.816  29.817  1.00 38.90 ? 190 SER C C   1 
ATOM   5216 O O   . SER C 1 190 ? 24.036  22.649  30.399  1.00 40.57 ? 190 SER C O   1 
ATOM   5217 C CB  . SER C 1 190 ? 21.601  21.145  31.467  1.00 39.42 ? 190 SER C CB  1 
ATOM   5218 O OG  . SER C 1 190 ? 20.272  20.654  31.547  1.00 51.99 ? 190 SER C OG  1 
ATOM   5219 N N   . THR C 1 191 ? 23.829  20.948  28.938  1.00 38.38 ? 191 THR C N   1 
ATOM   5220 C CA  . THR C 1 191 ? 25.257  20.835  28.700  1.00 39.65 ? 191 THR C CA  1 
ATOM   5221 C C   . THR C 1 191 ? 25.658  20.909  27.236  1.00 36.87 ? 191 THR C C   1 
ATOM   5222 O O   . THR C 1 191 ? 26.812  21.258  26.957  1.00 37.79 ? 191 THR C O   1 
ATOM   5223 C CB  . THR C 1 191 ? 25.779  19.511  29.273  1.00 37.90 ? 191 THR C CB  1 
ATOM   5224 O OG1 . THR C 1 191 ? 24.900  18.450  28.870  1.00 40.33 ? 191 THR C OG1 1 
ATOM   5225 C CG2 . THR C 1 191 ? 25.835  19.582  30.782  1.00 41.60 ? 191 THR C CG2 1 
ATOM   5226 N N   . HIS C 1 192 ? 24.760  20.593  26.298  1.00 37.85 ? 192 HIS C N   1 
ATOM   5227 C CA  . HIS C 1 192 ? 25.122  20.448  24.897  1.00 38.33 ? 192 HIS C CA  1 
ATOM   5228 C C   . HIS C 1 192 ? 24.251  21.331  24.020  1.00 39.03 ? 192 HIS C C   1 
ATOM   5229 O O   . HIS C 1 192 ? 23.040  21.429  24.238  1.00 32.49 ? 192 HIS C O   1 
ATOM   5230 C CB  . HIS C 1 192 ? 24.949  19.014  24.421  1.00 37.28 ? 192 HIS C CB  1 
ATOM   5231 C CG  . HIS C 1 192 ? 25.940  18.060  24.992  1.00 39.53 ? 192 HIS C CG  1 
ATOM   5232 N ND1 . HIS C 1 192 ? 26.054  17.835  26.349  1.00 39.75 ? 192 HIS C ND1 1 
ATOM   5233 C CD2 . HIS C 1 192 ? 26.813  17.218  24.391  1.00 39.02 ? 192 HIS C CD2 1 
ATOM   5234 C CE1 . HIS C 1 192 ? 26.970  16.905  26.560  1.00 43.54 ? 192 HIS C CE1 1 
ATOM   5235 N NE2 . HIS C 1 192 ? 27.428  16.500  25.388  1.00 42.96 ? 192 HIS C NE2 1 
ATOM   5236 N N   . TYR C 1 193 ? 24.866  21.915  22.992  1.00 32.52 ? 193 TYR C N   1 
ATOM   5237 C CA  . TYR C 1 193 ? 24.100  22.465  21.888  1.00 32.78 ? 193 TYR C CA  1 
ATOM   5238 C C   . TYR C 1 193 ? 23.584  21.307  21.051  1.00 31.81 ? 193 TYR C C   1 
ATOM   5239 O O   . TYR C 1 193 ? 24.266  20.288  20.902  1.00 31.96 ? 193 TYR C O   1 
ATOM   5240 C CB  . TYR C 1 193 ? 24.968  23.361  21.003  1.00 32.10 ? 193 TYR C CB  1 
ATOM   5241 C CG  . TYR C 1 193 ? 25.604  24.569  21.639  1.00 30.24 ? 193 TYR C CG  1 
ATOM   5242 C CD1 . TYR C 1 193 ? 24.845  25.621  22.122  1.00 31.25 ? 193 TYR C CD1 1 
ATOM   5243 C CD2 . TYR C 1 193 ? 26.990  24.692  21.671  1.00 36.29 ? 193 TYR C CD2 1 
ATOM   5244 C CE1 . TYR C 1 193 ? 25.457  26.750  22.666  1.00 34.15 ? 193 TYR C CE1 1 
ATOM   5245 C CE2 . TYR C 1 193 ? 27.607  25.813  22.202  1.00 33.17 ? 193 TYR C CE2 1 
ATOM   5246 C CZ  . TYR C 1 193 ? 26.841  26.833  22.698  1.00 31.21 ? 193 TYR C CZ  1 
ATOM   5247 O OH  . TYR C 1 193 ? 27.475  27.936  23.217  1.00 34.65 ? 193 TYR C OH  1 
ATOM   5248 N N   . VAL C 1 194 ? 22.378  21.445  20.504  1.00 29.53 ? 194 VAL C N   1 
ATOM   5249 C CA  . VAL C 1 194 ? 21.850  20.460  19.563  1.00 31.22 ? 194 VAL C CA  1 
ATOM   5250 C C   . VAL C 1 194 ? 21.995  21.042  18.164  1.00 33.30 ? 194 VAL C C   1 
ATOM   5251 O O   . VAL C 1 194 ? 21.347  22.048  17.827  1.00 29.17 ? 194 VAL C O   1 
ATOM   5252 C CB  . VAL C 1 194 ? 20.392  20.098  19.855  1.00 32.03 ? 194 VAL C CB  1 
ATOM   5253 C CG1 . VAL C 1 194 ? 19.940  18.976  18.913  1.00 29.26 ? 194 VAL C CG1 1 
ATOM   5254 C CG2 . VAL C 1 194 ? 20.218  19.733  21.320  1.00 32.70 ? 194 VAL C CG2 1 
ATOM   5255 N N   . VAL C 1 195 ? 22.844  20.415  17.351  1.00 29.22 ? 195 VAL C N   1 
ATOM   5256 C CA  . VAL C 1 195 ? 23.249  20.973  16.065  1.00 28.85 ? 195 VAL C CA  1 
ATOM   5257 C C   . VAL C 1 195 ? 22.665  20.106  14.963  1.00 28.16 ? 195 VAL C C   1 
ATOM   5258 O O   . VAL C 1 195 ? 22.931  18.895  14.905  1.00 30.36 ? 195 VAL C O   1 
ATOM   5259 C CB  . VAL C 1 195 ? 24.781  21.058  15.929  1.00 28.72 ? 195 VAL C CB  1 
ATOM   5260 C CG1 . VAL C 1 195 ? 25.148  21.536  14.539  1.00 24.58 ? 195 VAL C CG1 1 
ATOM   5261 C CG2 . VAL C 1 195 ? 25.362  21.974  16.982  1.00 29.48 ? 195 VAL C CG2 1 
ATOM   5262 N N   . ALA C 1 196 ? 21.891  20.730  14.079  1.00 24.70 ? 196 ALA C N   1 
ATOM   5263 C CA  . ALA C 1 196 ? 21.559  20.152  12.785  1.00 26.20 ? 196 ALA C CA  1 
ATOM   5264 C C   . ALA C 1 196 ? 22.753  20.371  11.871  1.00 30.94 ? 196 ALA C C   1 
ATOM   5265 O O   . ALA C 1 196 ? 23.015  21.506  11.446  1.00 27.54 ? 196 ALA C O   1 
ATOM   5266 C CB  . ALA C 1 196 ? 20.310  20.803  12.195  1.00 26.71 ? 196 ALA C CB  1 
ATOM   5267 N N   . ASP C 1 197 ? 23.482  19.288  11.581  1.00 26.96 ? 197 ASP C N   1 
ATOM   5268 C CA  . ASP C 1 197 ? 24.711  19.349  10.794  1.00 27.22 ? 197 ASP C CA  1 
ATOM   5269 C C   . ASP C 1 197 ? 24.412  18.849  9.396   1.00 26.01 ? 197 ASP C C   1 
ATOM   5270 O O   . ASP C 1 197 ? 24.102  17.661  9.234   1.00 25.94 ? 197 ASP C O   1 
ATOM   5271 C CB  . ASP C 1 197 ? 25.787  18.491  11.453  1.00 27.56 ? 197 ASP C CB  1 
ATOM   5272 C CG  . ASP C 1 197 ? 27.078  18.377  10.635  1.00 29.40 ? 197 ASP C CG  1 
ATOM   5273 O OD1 . ASP C 1 197 ? 27.106  18.607  9.393   1.00 24.92 ? 197 ASP C OD1 1 
ATOM   5274 O OD2 . ASP C 1 197 ? 28.080  18.007  11.284  1.00 27.07 ? 197 ASP C OD2 1 
ATOM   5275 N N   . PRO C 1 198 ? 24.547  19.682  8.364   1.00 26.43 ? 198 PRO C N   1 
ATOM   5276 C CA  . PRO C 1 198 ? 24.102  19.285  7.018   1.00 27.08 ? 198 PRO C CA  1 
ATOM   5277 C C   . PRO C 1 198 ? 24.884  18.115  6.433   1.00 27.78 ? 198 PRO C C   1 
ATOM   5278 O O   . PRO C 1 198 ? 24.472  17.581  5.393   1.00 26.80 ? 198 PRO C O   1 
ATOM   5279 C CB  . PRO C 1 198 ? 24.360  20.548  6.186   1.00 27.97 ? 198 PRO C CB  1 
ATOM   5280 C CG  . PRO C 1 198 ? 24.443  21.640  7.175   1.00 29.60 ? 198 PRO C CG  1 
ATOM   5281 C CD  . PRO C 1 198 ? 25.126  21.031  8.360   1.00 28.01 ? 198 PRO C CD  1 
ATOM   5282 N N   . ALA C 1 199 ? 25.977  17.692  7.060   1.00 25.49 ? 199 ALA C N   1 
ATOM   5283 C CA  . ALA C 1 199 ? 26.733  16.543  6.568   1.00 29.86 ? 199 ALA C CA  1 
ATOM   5284 C C   . ALA C 1 199 ? 26.608  15.314  7.449   1.00 29.99 ? 199 ALA C C   1 
ATOM   5285 O O   . ALA C 1 199 ? 27.258  14.304  7.159   1.00 30.28 ? 199 ALA C O   1 
ATOM   5286 C CB  . ALA C 1 199 ? 28.226  16.899  6.409   1.00 30.93 ? 199 ALA C CB  1 
ATOM   5287 N N   . LYS C 1 200 ? 25.801  15.359  8.512   1.00 28.28 ? 200 LYS C N   1 
ATOM   5288 C CA  . LYS C 1 200 ? 25.781  14.248  9.465   1.00 30.42 ? 200 LYS C CA  1 
ATOM   5289 C C   . LYS C 1 200 ? 24.384  13.897  9.967   1.00 31.47 ? 200 LYS C C   1 
ATOM   5290 O O   . LYS C 1 200 ? 23.981  12.730  9.914   1.00 31.25 ? 200 LYS C O   1 
ATOM   5291 C CB  . LYS C 1 200 ? 26.696  14.564  10.664  1.00 30.44 ? 200 LYS C CB  1 
ATOM   5292 C CG  . LYS C 1 200 ? 28.194  14.569  10.342  1.00 35.31 ? 200 LYS C CG  1 
ATOM   5293 C CD  . LYS C 1 200 ? 28.796  13.188  10.300  1.00 33.92 ? 200 LYS C CD  1 
ATOM   5294 C CE  . LYS C 1 200 ? 28.294  12.330  11.416  1.00 34.24 ? 200 LYS C CE  1 
ATOM   5295 N NZ  . LYS C 1 200 ? 28.570  10.904  11.077  1.00 37.74 ? 200 LYS C NZ  1 
ATOM   5296 N N   . GLY C 1 201 ? 23.622  14.874  10.434  1.00 28.28 ? 201 GLY C N   1 
ATOM   5297 C CA  . GLY C 1 201 ? 22.332  14.548  11.021  1.00 29.17 ? 201 GLY C CA  1 
ATOM   5298 C C   . GLY C 1 201 ? 21.771  15.740  11.752  1.00 31.93 ? 201 GLY C C   1 
ATOM   5299 O O   . GLY C 1 201 ? 22.457  16.745  11.975  1.00 27.27 ? 201 GLY C O   1 
ATOM   5300 N N   . VAL C 1 202 ? 20.485  15.616  12.119  1.00 29.61 ? 202 VAL C N   1 
ATOM   5301 C CA  . VAL C 1 202 ? 19.738  16.753  12.664  1.00 28.82 ? 202 VAL C CA  1 
ATOM   5302 C C   . VAL C 1 202 ? 20.002  16.961  14.139  1.00 30.06 ? 202 VAL C C   1 
ATOM   5303 O O   . VAL C 1 202 ? 19.658  18.018  14.674  1.00 31.00 ? 202 VAL C O   1 
ATOM   5304 C CB  . VAL C 1 202 ? 18.221  16.593  12.409  1.00 29.57 ? 202 VAL C CB  1 
ATOM   5305 C CG1 . VAL C 1 202 ? 17.575  15.583  13.394  1.00 33.27 ? 202 VAL C CG1 1 
ATOM   5306 C CG2 . VAL C 1 202 ? 17.496  17.936  12.432  1.00 27.30 ? 202 VAL C CG2 1 
ATOM   5307 N N   . ASN C 1 203 ? 20.674  16.017  14.791  1.00 28.39 ? 203 ASN C N   1 
ATOM   5308 C CA  . ASN C 1 203 ? 20.685  15.914  16.236  1.00 34.43 ? 203 ASN C CA  1 
ATOM   5309 C C   . ASN C 1 203 ? 22.088  15.762  16.799  1.00 38.37 ? 203 ASN C C   1 
ATOM   5310 O O   . ASN C 1 203 ? 22.311  14.988  17.735  1.00 43.03 ? 203 ASN C O   1 
ATOM   5311 C CB  . ASN C 1 203 ? 19.802  14.750  16.681  1.00 41.64 ? 203 ASN C CB  1 
ATOM   5312 C CG  . ASN C 1 203 ? 19.510  14.801  18.124  1.00 46.46 ? 203 ASN C CG  1 
ATOM   5313 O OD1 . ASN C 1 203 ? 19.060  15.830  18.625  1.00 50.77 ? 203 ASN C OD1 1 
ATOM   5314 N ND2 . ASN C 1 203 ? 19.707  13.671  18.818  1.00 47.54 ? 203 ASN C ND2 1 
ATOM   5315 N N   . ARG C 1 204 ? 23.075  16.459  16.237  1.00 34.36 ? 204 ARG C N   1 
ATOM   5316 C CA  . ARG C 1 204 ? 24.442  16.316  16.730  1.00 34.58 ? 204 ARG C CA  1 
ATOM   5317 C C   . ARG C 1 204 ? 24.610  17.162  17.994  1.00 35.69 ? 204 ARG C C   1 
ATOM   5318 O O   . ARG C 1 204 ? 24.361  18.370  17.971  1.00 36.21 ? 204 ARG C O   1 
ATOM   5319 C CB  . ARG C 1 204 ? 25.454  16.736  15.666  1.00 31.34 ? 204 ARG C CB  1 
ATOM   5320 C CG  . ARG C 1 204 ? 25.099  16.267  14.274  1.00 30.66 ? 204 ARG C CG  1 
ATOM   5321 C CD  . ARG C 1 204 ? 24.848  14.763  14.212  1.00 34.62 ? 204 ARG C CD  1 
ATOM   5322 N NE  . ARG C 1 204 ? 25.904  14.023  14.887  1.00 34.29 ? 204 ARG C NE  1 
ATOM   5323 C CZ  . ARG C 1 204 ? 25.911  12.711  15.033  1.00 40.71 ? 204 ARG C CZ  1 
ATOM   5324 N NH1 . ARG C 1 204 ? 24.915  11.964  14.583  1.00 44.90 ? 204 ARG C NH1 1 
ATOM   5325 N NH2 . ARG C 1 204 ? 26.942  12.130  15.646  1.00 41.40 ? 204 ARG C NH2 1 
ATOM   5326 N N   . LYS C 1 205 ? 24.985  16.502  19.086  1.00 34.29 ? 205 LYS C N   1 
ATOM   5327 C CA  . LYS C 1 205 ? 25.081  17.121  20.426  1.00 32.44 ? 205 LYS C CA  1 
ATOM   5328 C C   . LYS C 1 205 ? 26.524  17.498  20.732  1.00 34.37 ? 205 LYS C C   1 
ATOM   5329 O O   . LYS C 1 205 ? 27.368  16.629  20.811  1.00 35.04 ? 205 LYS C O   1 
ATOM   5330 C CB  . LYS C 1 205 ? 24.433  16.202  21.461  1.00 35.75 ? 205 LYS C CB  1 
ATOM   5331 C CG  . LYS C 1 205 ? 22.916  16.203  21.416  1.00 38.35 ? 205 LYS C CG  1 
ATOM   5332 C CD  . LYS C 1 205 ? 22.271  15.158  22.264  1.00 45.11 ? 205 LYS C CD  1 
ATOM   5333 C CE  . LYS C 1 205 ? 20.878  14.806  21.794  1.00 41.33 ? 205 LYS C CE  1 
ATOM   5334 N NZ  . LYS C 1 205 ? 20.199  13.892  22.729  1.00 51.18 ? 205 LYS C NZ  1 
ATOM   5335 N N   . TYR C 1 206 ? 26.759  18.788  20.878  1.00 31.98 ? 206 TYR C N   1 
ATOM   5336 C CA  . TYR C 1 206 ? 28.126  19.271  21.132  1.00 36.93 ? 206 TYR C CA  1 
ATOM   5337 C C   . TYR C 1 206 ? 28.174  19.917  22.516  1.00 37.51 ? 206 TYR C C   1 
ATOM   5338 O O   . TYR C 1 206 ? 27.387  20.806  22.791  1.00 40.51 ? 206 TYR C O   1 
ATOM   5339 C CB  . TYR C 1 206 ? 28.514  20.312  20.080  1.00 30.02 ? 206 TYR C CB  1 
ATOM   5340 C CG  . TYR C 1 206 ? 29.012  19.772  18.768  1.00 30.44 ? 206 TYR C CG  1 
ATOM   5341 C CD1 . TYR C 1 206 ? 28.146  19.298  17.806  1.00 26.83 ? 206 TYR C CD1 1 
ATOM   5342 C CD2 . TYR C 1 206 ? 30.356  19.765  18.472  1.00 32.02 ? 206 TYR C CD2 1 
ATOM   5343 C CE1 . TYR C 1 206 ? 28.597  18.808  16.597  1.00 31.40 ? 206 TYR C CE1 1 
ATOM   5344 C CE2 . TYR C 1 206 ? 30.833  19.281  17.270  1.00 30.10 ? 206 TYR C CE2 1 
ATOM   5345 C CZ  . TYR C 1 206 ? 29.952  18.793  16.330  1.00 32.71 ? 206 TYR C CZ  1 
ATOM   5346 O OH  . TYR C 1 206 ? 30.438  18.329  15.157  1.00 29.72 ? 206 TYR C OH  1 
ATOM   5347 N N   . LYS C 1 207 ? 29.144  19.523  23.329  1.00 48.51 ? 207 LYS C N   1 
ATOM   5348 C CA  . LYS C 1 207 ? 29.336  20.189  24.631  1.00 36.22 ? 207 LYS C CA  1 
ATOM   5349 C C   . LYS C 1 207 ? 29.628  21.666  24.338  1.00 39.55 ? 207 LYS C C   1 
ATOM   5350 O O   . LYS C 1 207 ? 30.440  21.927  23.441  1.00 34.64 ? 207 LYS C O   1 
ATOM   5351 C CB  . LYS C 1 207 ? 30.577  19.600  25.292  1.00 40.80 ? 207 LYS C CB  1 
ATOM   5352 C CG  . LYS C 1 207 ? 30.360  18.525  26.328  1.00 46.89 ? 207 LYS C CG  1 
ATOM   5353 C CD  . LYS C 1 207 ? 30.557  19.049  27.732  1.00 52.28 ? 207 LYS C CD  1 
ATOM   5354 C CE  . LYS C 1 207 ? 31.959  18.867  28.271  1.00 54.96 ? 207 LYS C CE  1 
ATOM   5355 N NZ  . LYS C 1 207 ? 32.775  20.096  28.141  1.00 59.22 ? 207 LYS C NZ  1 
ATOM   5356 N N   . PHE C 1 208 ? 29.021  22.575  25.107  1.00 40.86 ? 208 PHE C N   1 
ATOM   5357 C CA  . PHE C 1 208 ? 29.186  24.032  24.902  1.00 36.97 ? 208 PHE C CA  1 
ATOM   5358 C C   . PHE C 1 208 ? 30.651  24.385  24.713  1.00 38.43 ? 208 PHE C C   1 
ATOM   5359 O O   . PHE C 1 208 ? 30.948  25.037  23.744  1.00 36.04 ? 208 PHE C O   1 
ATOM   5360 C CB  . PHE C 1 208 ? 28.657  24.834  26.087  1.00 40.22 ? 208 PHE C CB  1 
ATOM   5361 C CG  . PHE C 1 208 ? 27.226  24.577  26.459  1.00 35.89 ? 208 PHE C CG  1 
ATOM   5362 C CD1 . PHE C 1 208 ? 26.280  24.320  25.496  1.00 34.50 ? 208 PHE C CD1 1 
ATOM   5363 C CD2 . PHE C 1 208 ? 26.825  24.615  27.778  1.00 37.16 ? 208 PHE C CD2 1 
ATOM   5364 C CE1 . PHE C 1 208 ? 24.965  24.098  25.844  1.00 37.32 ? 208 PHE C CE1 1 
ATOM   5365 C CE2 . PHE C 1 208 ? 25.509  24.390  28.128  1.00 38.53 ? 208 PHE C CE2 1 
ATOM   5366 C CZ  . PHE C 1 208 ? 24.577  24.141  27.158  1.00 38.16 ? 208 PHE C CZ  1 
ATOM   5367 N N   . SER C 1 209 ? 31.538  23.818  25.520  1.00 40.53 ? 209 SER C N   1 
ATOM   5368 C CA  . SER C 1 209 ? 32.921  24.300  25.330  1.00 39.96 ? 209 SER C CA  1 
ATOM   5369 C C   . SER C 1 209 ? 33.551  23.725  24.073  1.00 37.73 ? 209 SER C C   1 
ATOM   5370 O O   . SER C 1 209 ? 34.449  24.341  23.479  1.00 41.08 ? 209 SER C O   1 
ATOM   5371 C CB  . SER C 1 209 ? 33.775  23.875  26.526  1.00 40.19 ? 209 SER C CB  1 
ATOM   5372 O OG  . SER C 1 209 ? 33.542  22.490  26.778  1.00 44.90 ? 209 SER C OG  1 
ATOM   5373 N N   . CYS C 1 210 ? 33.116  22.525  23.682  1.00 37.68 ? 210 CYS C N   1 
ATOM   5374 C CA  . CYS C 1 210 ? 33.653  21.869  22.493  1.00 39.22 ? 210 CYS C CA  1 
ATOM   5375 C C   . CYS C 1 210 ? 33.413  22.705  21.242  1.00 37.55 ? 210 CYS C C   1 
ATOM   5376 O O   . CYS C 1 210 ? 34.351  23.019  20.496  1.00 38.24 ? 210 CYS C O   1 
ATOM   5377 C CB  . CYS C 1 210 ? 33.020  20.488  22.350  1.00 37.98 ? 210 CYS C CB  1 
ATOM   5378 S SG  . CYS C 1 210 ? 33.591  19.565  20.932  1.00 43.86 ? 210 CYS C SG  1 
ATOM   5379 N N   . LEU C 1 211 ? 32.161  23.098  21.019  1.00 34.90 ? 211 LEU C N   1 
ATOM   5380 C CA  . LEU C 1 211 ? 31.813  23.952  19.889  1.00 35.06 ? 211 LEU C CA  1 
ATOM   5381 C C   . LEU C 1 211 ? 32.391  25.354  20.040  1.00 32.71 ? 211 LEU C C   1 
ATOM   5382 O O   . LEU C 1 211 ? 32.933  25.909  19.079  1.00 31.37 ? 211 LEU C O   1 
ATOM   5383 C CB  . LEU C 1 211 ? 30.292  24.044  19.764  1.00 32.99 ? 211 LEU C CB  1 
ATOM   5384 C CG  . LEU C 1 211 ? 29.731  24.412  18.383  1.00 35.39 ? 211 LEU C CG  1 
ATOM   5385 C CD1 . LEU C 1 211 ? 30.492  23.709  17.262  1.00 29.57 ? 211 LEU C CD1 1 
ATOM   5386 C CD2 . LEU C 1 211 ? 28.213  24.214  18.295  1.00 31.07 ? 211 LEU C CD2 1 
ATOM   5387 N N   . ASP C 1 212 ? 32.257  25.956  21.230  1.00 35.05 ? 212 ASP C N   1 
ATOM   5388 C CA  . ASP C 1 212 ? 32.733  27.330  21.429  1.00 33.92 ? 212 ASP C CA  1 
ATOM   5389 C C   . ASP C 1 212 ? 34.201  27.485  21.055  1.00 33.14 ? 212 ASP C C   1 
ATOM   5390 O O   . ASP C 1 212 ? 34.578  28.464  20.409  1.00 37.31 ? 212 ASP C O   1 
ATOM   5391 C CB  . ASP C 1 212 ? 32.537  27.784  22.880  1.00 35.46 ? 212 ASP C CB  1 
ATOM   5392 C CG  . ASP C 1 212 ? 31.079  27.926  23.274  1.00 37.30 ? 212 ASP C CG  1 
ATOM   5393 O OD1 . ASP C 1 212 ? 30.190  27.834  22.400  1.00 37.02 ? 212 ASP C OD1 1 
ATOM   5394 O OD2 . ASP C 1 212 ? 30.814  28.110  24.480  1.00 39.11 ? 212 ASP C OD2 1 
ATOM   5395 N N   . ASN C 1 213 ? 35.039  26.539  21.449  1.00 36.09 ? 213 ASN C N   1 
ATOM   5396 C CA  . ASN C 1 213 ? 36.478  26.680  21.289  1.00 39.81 ? 213 ASN C CA  1 
ATOM   5397 C C   . ASN C 1 213 ? 37.012  26.046  20.012  1.00 38.04 ? 213 ASN C C   1 
ATOM   5398 O O   . ASN C 1 213 ? 38.227  26.083  19.789  1.00 38.74 ? 213 ASN C O   1 
ATOM   5399 C CB  . ASN C 1 213 ? 37.190  26.080  22.500  1.00 39.85 ? 213 ASN C CB  1 
ATOM   5400 C CG  . ASN C 1 213 ? 36.867  26.823  23.764  1.00 41.79 ? 213 ASN C CG  1 
ATOM   5401 O OD1 . ASN C 1 213 ? 36.585  28.020  23.723  1.00 42.91 ? 213 ASN C OD1 1 
ATOM   5402 N ND2 . ASN C 1 213 ? 36.894  26.129  24.893  1.00 41.29 ? 213 ASN C ND2 1 
ATOM   5403 N N   . ALA C 1 214 ? 36.147  25.516  19.143  1.00 35.43 ? 214 ALA C N   1 
ATOM   5404 C CA  . ALA C 1 214 ? 36.616  24.822  17.951  1.00 34.13 ? 214 ALA C CA  1 
ATOM   5405 C C   . ALA C 1 214 ? 36.753  25.753  16.767  1.00 35.08 ? 214 ALA C C   1 
ATOM   5406 O O   . ALA C 1 214 ? 36.658  25.294  15.622  1.00 33.10 ? 214 ALA C O   1 
ATOM   5407 C CB  . ALA C 1 214 ? 35.700  23.652  17.595  1.00 33.49 ? 214 ALA C CB  1 
ATOM   5408 N N   . ASN C 1 215 ? 36.960  27.061  17.011  1.00 34.41 ? 215 ASN C N   1 
ATOM   5409 C CA  . ASN C 1 215 ? 37.170  27.996  15.914  1.00 32.83 ? 215 ASN C CA  1 
ATOM   5410 C C   . ASN C 1 215 ? 38.390  28.891  16.155  1.00 36.44 ? 215 ASN C C   1 
ATOM   5411 O O   . ASN C 1 215 ? 38.423  30.040  15.698  1.00 35.57 ? 215 ASN C O   1 
ATOM   5412 C CB  . ASN C 1 215 ? 35.906  28.827  15.642  1.00 32.55 ? 215 ASN C CB  1 
ATOM   5413 C CG  . ASN C 1 215 ? 35.660  29.030  14.151  1.00 31.23 ? 215 ASN C CG  1 
ATOM   5414 O OD1 . ASN C 1 215 ? 36.055  28.184  13.323  1.00 35.60 ? 215 ASN C OD1 1 
ATOM   5415 N ND2 . ASN C 1 215 ? 35.012  30.127  13.793  1.00 31.83 ? 215 ASN C ND2 1 
ATOM   5416 N N   . LYS C 1 216 ? 39.457  28.347  16.752  1.00 39.40 ? 216 LYS C N   1 
ATOM   5417 C CA  . LYS C 1 216 ? 40.682  29.141  16.911  1.00 40.81 ? 216 LYS C CA  1 
ATOM   5418 C C   . LYS C 1 216 ? 41.214  29.539  15.555  1.00 36.71 ? 216 LYS C C   1 
ATOM   5419 O O   . LYS C 1 216 ? 41.217  28.721  14.633  1.00 37.84 ? 216 LYS C O   1 
ATOM   5420 C CB  . LYS C 1 216 ? 41.850  28.387  17.524  1.00 43.38 ? 216 LYS C CB  1 
ATOM   5421 C CG  . LYS C 1 216 ? 41.547  27.662  18.731  1.00 44.45 ? 216 LYS C CG  1 
ATOM   5422 C CD  . LYS C 1 216 ? 41.718  28.453  19.962  1.00 50.93 ? 216 LYS C CD  1 
ATOM   5423 C CE  . LYS C 1 216 ? 40.939  27.578  20.897  1.00 49.66 ? 216 LYS C CE  1 
ATOM   5424 N NZ  . LYS C 1 216 ? 40.211  28.264  21.985  1.00 53.22 ? 216 LYS C NZ  1 
ATOM   5425 N N   . GLY C 1 217 ? 41.630  30.790  15.426  1.00 38.50 ? 217 GLY C N   1 
ATOM   5426 C CA  . GLY C 1 217 ? 42.155  31.309  14.185  1.00 37.05 ? 217 GLY C CA  1 
ATOM   5427 C C   . GLY C 1 217 ? 41.107  31.917  13.298  1.00 39.67 ? 217 GLY C C   1 
ATOM   5428 O O   . GLY C 1 217 ? 41.459  32.571  12.308  1.00 38.30 ? 217 GLY C O   1 
ATOM   5429 N N   . TYR C 1 218 ? 39.830  31.765  13.646  1.00 35.45 ? 218 TYR C N   1 
ATOM   5430 C CA  . TYR C 1 218 ? 38.748  32.238  12.803  1.00 38.36 ? 218 TYR C CA  1 
ATOM   5431 C C   . TYR C 1 218 ? 37.804  33.107  13.620  1.00 34.68 ? 218 TYR C C   1 
ATOM   5432 O O   . TYR C 1 218 ? 37.966  33.273  14.831  1.00 37.60 ? 218 TYR C O   1 
ATOM   5433 C CB  . TYR C 1 218 ? 38.017  31.050  12.164  1.00 36.92 ? 218 TYR C CB  1 
ATOM   5434 C CG  . TYR C 1 218 ? 38.941  30.194  11.328  1.00 35.73 ? 218 TYR C CG  1 
ATOM   5435 C CD1 . TYR C 1 218 ? 39.745  29.232  11.921  1.00 36.01 ? 218 TYR C CD1 1 
ATOM   5436 C CD2 . TYR C 1 218 ? 39.041  30.381  9.954   1.00 36.06 ? 218 TYR C CD2 1 
ATOM   5437 C CE1 . TYR C 1 218 ? 40.612  28.466  11.175  1.00 37.14 ? 218 TYR C CE1 1 
ATOM   5438 C CE2 . TYR C 1 218 ? 39.899  29.616  9.193   1.00 40.44 ? 218 TYR C CE2 1 
ATOM   5439 C CZ  . TYR C 1 218 ? 40.682  28.660  9.809   1.00 39.20 ? 218 TYR C CZ  1 
ATOM   5440 O OH  . TYR C 1 218 ? 41.523  27.886  9.059   1.00 46.32 ? 218 TYR C OH  1 
ATOM   5441 N N   . ARG C 1 219 ? 36.802  33.663  12.947  1.00 33.86 ? 219 ARG C N   1 
ATOM   5442 C CA  . ARG C 1 219 ? 35.926  34.636  13.586  1.00 36.61 ? 219 ARG C CA  1 
ATOM   5443 C C   . ARG C 1 219 ? 35.237  34.040  14.810  1.00 33.78 ? 219 ARG C C   1 
ATOM   5444 O O   . ARG C 1 219 ? 34.637  32.965  14.739  1.00 36.62 ? 219 ARG C O   1 
ATOM   5445 C CB  . ARG C 1 219 ? 34.885  35.130  12.589  1.00 34.45 ? 219 ARG C CB  1 
ATOM   5446 C CG  . ARG C 1 219 ? 34.167  36.360  13.061  1.00 32.02 ? 219 ARG C CG  1 
ATOM   5447 C CD  . ARG C 1 219 ? 33.349  36.943  11.946  1.00 32.58 ? 219 ARG C CD  1 
ATOM   5448 N NE  . ARG C 1 219 ? 32.330  37.842  12.463  1.00 32.67 ? 219 ARG C NE  1 
ATOM   5449 C CZ  . ARG C 1 219 ? 31.690  38.717  11.711  1.00 35.21 ? 219 ARG C CZ  1 
ATOM   5450 N NH1 . ARG C 1 219 ? 31.948  38.818  10.418  1.00 33.31 ? 219 ARG C NH1 1 
ATOM   5451 N NH2 . ARG C 1 219 ? 30.776  39.512  12.270  1.00 33.98 ? 219 ARG C NH2 1 
ATOM   5452 N N   . GLN C 1 220 ? 35.304  34.755  15.930  1.00 34.01 ? 220 GLN C N   1 
ATOM   5453 C CA  . GLN C 1 220 ? 34.787  34.269  17.208  1.00 34.83 ? 220 GLN C CA  1 
ATOM   5454 C C   . GLN C 1 220 ? 33.326  34.680  17.403  1.00 37.18 ? 220 GLN C C   1 
ATOM   5455 O O   . GLN C 1 220 ? 32.957  35.384  18.347  1.00 40.13 ? 220 GLN C O   1 
ATOM   5456 C CB  . GLN C 1 220 ? 35.660  34.782  18.345  1.00 39.62 ? 220 GLN C CB  1 
ATOM   5457 C CG  . GLN C 1 220 ? 37.046  34.174  18.346  1.00 37.77 ? 220 GLN C CG  1 
ATOM   5458 C CD  . GLN C 1 220 ? 36.992  32.682  18.508  1.00 36.20 ? 220 GLN C CD  1 
ATOM   5459 O OE1 . GLN C 1 220 ? 37.331  31.937  17.591  1.00 40.93 ? 220 GLN C OE1 1 
ATOM   5460 N NE2 . GLN C 1 220 ? 36.592  32.230  19.684  1.00 35.86 ? 220 GLN C NE2 1 
ATOM   5461 N N   . ASN C 1 221 ? 32.470  34.174  16.519  1.00 32.82 ? 221 ASN C N   1 
ATOM   5462 C CA  . ASN C 1 221 ? 31.050  34.477  16.592  1.00 32.59 ? 221 ASN C CA  1 
ATOM   5463 C C   . ASN C 1 221 ? 30.244  33.230  16.274  1.00 33.55 ? 221 ASN C C   1 
ATOM   5464 O O   . ASN C 1 221 ? 30.758  32.271  15.681  1.00 29.60 ? 221 ASN C O   1 
ATOM   5465 C CB  . ASN C 1 221 ? 30.653  35.592  15.613  1.00 32.40 ? 221 ASN C CB  1 
ATOM   5466 C CG  . ASN C 1 221 ? 31.048  36.963  16.085  1.00 34.24 ? 221 ASN C CG  1 
ATOM   5467 O OD1 . ASN C 1 221 ? 31.715  37.707  15.367  1.00 35.16 ? 221 ASN C OD1 1 
ATOM   5468 N ND2 . ASN C 1 221 ? 30.634  37.314  17.286  1.00 33.30 ? 221 ASN C ND2 1 
ATOM   5469 N N   . TYR C 1 222 ? 28.984  33.246  16.729  1.00 32.42 ? 222 TYR C N   1 
ATOM   5470 C CA  . TYR C 1 222 ? 27.869  32.492  16.157  1.00 28.78 ? 222 TYR C CA  1 
ATOM   5471 C C   . TYR C 1 222 ? 26.950  33.470  15.435  1.00 31.36 ? 222 TYR C C   1 
ATOM   5472 O O   . TYR C 1 222 ? 27.112  34.692  15.538  1.00 32.62 ? 222 TYR C O   1 
ATOM   5473 C CB  . TYR C 1 222 ? 27.094  31.725  17.230  1.00 29.34 ? 222 TYR C CB  1 
ATOM   5474 C CG  . TYR C 1 222 ? 27.847  30.603  17.914  1.00 30.80 ? 222 TYR C CG  1 
ATOM   5475 C CD1 . TYR C 1 222 ? 28.732  29.790  17.213  1.00 30.66 ? 222 TYR C CD1 1 
ATOM   5476 C CD2 . TYR C 1 222 ? 27.665  30.362  19.269  1.00 29.71 ? 222 TYR C CD2 1 
ATOM   5477 C CE1 . TYR C 1 222 ? 29.418  28.744  17.865  1.00 32.02 ? 222 TYR C CE1 1 
ATOM   5478 C CE2 . TYR C 1 222 ? 28.328  29.355  19.918  1.00 32.17 ? 222 TYR C CE2 1 
ATOM   5479 C CZ  . TYR C 1 222 ? 29.205  28.541  19.220  1.00 32.45 ? 222 TYR C CZ  1 
ATOM   5480 O OH  . TYR C 1 222 ? 29.859  27.536  19.902  1.00 32.67 ? 222 TYR C OH  1 
ATOM   5481 N N   . TYR C 1 223 ? 25.974  32.955  14.683  1.00 28.15 ? 223 TYR C N   1 
ATOM   5482 C CA  . TYR C 1 223 ? 25.172  33.828  13.811  1.00 31.01 ? 223 TYR C CA  1 
ATOM   5483 C C   . TYR C 1 223 ? 23.681  33.541  13.975  1.00 29.25 ? 223 TYR C C   1 
ATOM   5484 O O   . TYR C 1 223 ? 23.157  32.583  13.404  1.00 27.23 ? 223 TYR C O   1 
ATOM   5485 C CB  . TYR C 1 223 ? 25.640  33.696  12.356  1.00 26.60 ? 223 TYR C CB  1 
ATOM   5486 C CG  . TYR C 1 223 ? 27.154  33.862  12.301  1.00 28.15 ? 223 TYR C CG  1 
ATOM   5487 C CD1 . TYR C 1 223 ? 27.719  35.130  12.345  1.00 28.70 ? 223 TYR C CD1 1 
ATOM   5488 C CD2 . TYR C 1 223 ? 28.005  32.769  12.318  1.00 28.73 ? 223 TYR C CD2 1 
ATOM   5489 C CE1 . TYR C 1 223 ? 29.081  35.313  12.352  1.00 30.24 ? 223 TYR C CE1 1 
ATOM   5490 C CE2 . TYR C 1 223 ? 29.389  32.937  12.335  1.00 27.94 ? 223 TYR C CE2 1 
ATOM   5491 C CZ  . TYR C 1 223 ? 29.916  34.222  12.344  1.00 31.24 ? 223 TYR C CZ  1 
ATOM   5492 O OH  . TYR C 1 223 ? 31.274  34.438  12.356  1.00 29.67 ? 223 TYR C OH  1 
ATOM   5493 N N   . VAL C 1 224 ? 22.996  34.387  14.731  1.00 31.14 ? 224 VAL C N   1 
ATOM   5494 C CA  . VAL C 1 224 ? 21.547  34.151  14.920  1.00 26.93 ? 224 VAL C CA  1 
ATOM   5495 C C   . VAL C 1 224 ? 20.802  34.607  13.672  1.00 27.65 ? 224 VAL C C   1 
ATOM   5496 O O   . VAL C 1 224 ? 21.187  35.592  13.086  1.00 29.16 ? 224 VAL C O   1 
ATOM   5497 C CB  . VAL C 1 224 ? 20.996  34.727  16.231  1.00 31.72 ? 224 VAL C CB  1 
ATOM   5498 C CG1 . VAL C 1 224 ? 21.989  35.607  16.941  1.00 34.69 ? 224 VAL C CG1 1 
ATOM   5499 C CG2 . VAL C 1 224 ? 19.644  35.375  16.089  1.00 29.36 ? 224 VAL C CG2 1 
ATOM   5500 N N   . VAL C 1 225 ? 19.832  33.808  13.260  1.00 24.59 ? 225 VAL C N   1 
ATOM   5501 C CA  . VAL C 1 225 ? 19.014  34.123  12.097  1.00 26.47 ? 225 VAL C CA  1 
ATOM   5502 C C   . VAL C 1 225 ? 17.665  34.621  12.603  1.00 27.21 ? 225 VAL C C   1 
ATOM   5503 O O   . VAL C 1 225 ? 16.996  33.939  13.392  1.00 25.72 ? 225 VAL C O   1 
ATOM   5504 C CB  . VAL C 1 225 ? 18.846  32.891  11.192  1.00 24.65 ? 225 VAL C CB  1 
ATOM   5505 C CG1 . VAL C 1 225 ? 18.167  33.272  9.891   1.00 21.98 ? 225 VAL C CG1 1 
ATOM   5506 C CG2 . VAL C 1 225 ? 20.221  32.217  10.969  1.00 22.47 ? 225 VAL C CG2 1 
ATOM   5507 N N   . CYS C 1 226 ? 17.273  35.806  12.182  1.00 27.12 ? 226 CYS C N   1 
ATOM   5508 C CA  . CYS C 1 226 ? 15.930  36.235  12.555  1.00 28.36 ? 226 CYS C CA  1 
ATOM   5509 C C   . CYS C 1 226 ? 15.260  36.958  11.392  1.00 27.97 ? 226 CYS C C   1 
ATOM   5510 O O   . CYS C 1 226 ? 15.918  37.254  10.379  1.00 29.04 ? 226 CYS C O   1 
ATOM   5511 C CB  . CYS C 1 226 ? 15.985  37.088  13.820  1.00 30.30 ? 226 CYS C CB  1 
ATOM   5512 S SG  . CYS C 1 226 ? 17.005  38.563  13.636  1.00 37.79 ? 226 CYS C SG  1 
ATOM   5513 N N   . PRO C 1 227 ? 13.951  37.200  11.459  1.00 30.21 ? 227 PRO C N   1 
ATOM   5514 C CA  . PRO C 1 227 ? 13.312  37.974  10.393  1.00 31.83 ? 227 PRO C CA  1 
ATOM   5515 C C   . PRO C 1 227 ? 13.841  39.398  10.355  1.00 31.36 ? 227 PRO C C   1 
ATOM   5516 O O   . PRO C 1 227 ? 14.093  40.018  11.388  1.00 30.21 ? 227 PRO C O   1 
ATOM   5517 C CB  . PRO C 1 227 ? 11.815  37.918  10.742  1.00 30.20 ? 227 PRO C CB  1 
ATOM   5518 C CG  . PRO C 1 227 ? 11.714  37.166  12.016  1.00 32.42 ? 227 PRO C CG  1 
ATOM   5519 C CD  . PRO C 1 227 ? 12.963  36.429  12.240  1.00 32.50 ? 227 PRO C CD  1 
ATOM   5520 N N   . ALA C 1 228 ? 14.083  39.872  9.142   1.00 31.98 ? 228 ALA C N   1 
ATOM   5521 C CA  . ALA C 1 228 ? 14.565  41.220  8.888   1.00 33.56 ? 228 ALA C CA  1 
ATOM   5522 C C   . ALA C 1 228 ? 13.394  42.190  8.856   1.00 37.97 ? 228 ALA C C   1 
ATOM   5523 O O   . ALA C 1 228 ? 12.263  41.758  8.602   1.00 43.66 ? 228 ALA C O   1 
ATOM   5524 C CB  . ALA C 1 228 ? 15.320  41.259  7.595   1.00 31.36 ? 228 ALA C CB  1 
ATOM   5525 N N   . MET D 1 1   ? -9.714  18.301  -36.514 1.00 61.53 ? 1   MET D N   1 
ATOM   5526 C CA  . MET D 1 1   ? -8.777  18.985  -35.593 1.00 58.72 ? 1   MET D CA  1 
ATOM   5527 C C   . MET D 1 1   ? -8.618  20.454  -36.011 1.00 55.18 ? 1   MET D C   1 
ATOM   5528 O O   . MET D 1 1   ? -9.460  20.937  -36.768 1.00 58.89 ? 1   MET D O   1 
ATOM   5529 C CB  . MET D 1 1   ? -7.427  18.265  -35.553 1.00 57.80 ? 1   MET D CB  1 
ATOM   5530 C CG  . MET D 1 1   ? -7.229  17.491  -34.280 1.00 63.94 ? 1   MET D CG  1 
ATOM   5531 S SD  . MET D 1 1   ? -7.633  15.731  -34.385 1.00 83.46 ? 1   MET D SD  1 
ATOM   5532 C CE  . MET D 1 1   ? -9.381  15.750  -33.975 1.00 62.77 ? 1   MET D CE  1 
ATOM   5533 N N   . VAL D 1 2   ? -7.564  21.133  -35.554 1.00 44.04 ? 2   VAL D N   1 
ATOM   5534 C CA  . VAL D 1 2   ? -7.484  22.588  -35.856 1.00 37.80 ? 2   VAL D CA  1 
ATOM   5535 C C   . VAL D 1 2   ? -6.295  22.897  -36.770 1.00 35.73 ? 2   VAL D C   1 
ATOM   5536 O O   . VAL D 1 2   ? -5.204  22.526  -36.414 1.00 34.42 ? 2   VAL D O   1 
ATOM   5537 C CB  . VAL D 1 2   ? -7.428  23.382  -34.545 1.00 39.35 ? 2   VAL D CB  1 
ATOM   5538 C CG1 . VAL D 1 2   ? -7.201  24.852  -34.793 1.00 35.24 ? 2   VAL D CG1 1 
ATOM   5539 C CG2 . VAL D 1 2   ? -8.686  23.165  -33.734 1.00 45.12 ? 2   VAL D CG2 1 
ATOM   5540 N N   . ARG D 1 3   ? -6.542  23.569  -37.892 1.00 34.58 ? 3   ARG D N   1 
ATOM   5541 C CA  . ARG D 1 3   ? -5.475  23.901  -38.864 1.00 31.83 ? 3   ARG D CA  1 
ATOM   5542 C C   . ARG D 1 3   ? -5.411  25.410  -39.078 1.00 32.24 ? 3   ARG D C   1 
ATOM   5543 O O   . ARG D 1 3   ? -6.444  26.054  -39.082 1.00 30.72 ? 3   ARG D O   1 
ATOM   5544 C CB  . ARG D 1 3   ? -5.734  23.283  -40.239 1.00 32.23 ? 3   ARG D CB  1 
ATOM   5545 C CG  . ARG D 1 3   ? -6.575  22.023  -40.229 1.00 38.40 ? 3   ARG D CG  1 
ATOM   5546 C CD  . ARG D 1 3   ? -6.553  21.348  -41.577 1.00 42.37 ? 3   ARG D CD  1 
ATOM   5547 N NE  . ARG D 1 3   ? -7.395  22.039  -42.528 1.00 42.42 ? 3   ARG D NE  1 
ATOM   5548 C CZ  . ARG D 1 3   ? -7.377  21.824  -43.819 1.00 42.26 ? 3   ARG D CZ  1 
ATOM   5549 N NH1 . ARG D 1 3   ? -6.548  20.933  -44.313 1.00 49.47 ? 3   ARG D NH1 1 
ATOM   5550 N NH2 . ARG D 1 3   ? -8.170  22.496  -44.616 1.00 42.04 ? 3   ARG D NH2 1 
ATOM   5551 N N   . PHE D 1 4   ? -4.216  25.893  -39.365 1.00 25.40 ? 4   PHE D N   1 
ATOM   5552 C CA  . PHE D 1 4   ? -3.971  27.308  -39.597 1.00 28.42 ? 4   PHE D CA  1 
ATOM   5553 C C   . PHE D 1 4   ? -3.256  27.478  -40.921 1.00 28.72 ? 4   PHE D C   1 
ATOM   5554 O O   . PHE D 1 4   ? -2.296  26.750  -41.208 1.00 25.40 ? 4   PHE D O   1 
ATOM   5555 C CB  . PHE D 1 4   ? -3.145  27.913  -38.466 1.00 26.50 ? 4   PHE D CB  1 
ATOM   5556 C CG  . PHE D 1 4   ? -3.800  27.792  -37.131 1.00 28.76 ? 4   PHE D CG  1 
ATOM   5557 C CD1 . PHE D 1 4   ? -4.811  28.669  -36.770 1.00 28.12 ? 4   PHE D CD1 1 
ATOM   5558 C CD2 . PHE D 1 4   ? -3.412  26.812  -36.236 1.00 27.10 ? 4   PHE D CD2 1 
ATOM   5559 C CE1 . PHE D 1 4   ? -5.443  28.572  -35.527 1.00 27.60 ? 4   PHE D CE1 1 
ATOM   5560 C CE2 . PHE D 1 4   ? -4.031  26.699  -34.991 1.00 29.68 ? 4   PHE D CE2 1 
ATOM   5561 C CZ  . PHE D 1 4   ? -5.062  27.585  -34.641 1.00 28.63 ? 4   PHE D CZ  1 
ATOM   5562 N N   . SER D 1 5   ? -3.737  28.417  -41.732 1.00 26.11 ? 5   SER D N   1 
ATOM   5563 C CA  . SER D 1 5   ? -3.168  28.624  -43.055 1.00 26.77 ? 5   SER D CA  1 
ATOM   5564 C C   . SER D 1 5   ? -1.821  29.340  -42.952 1.00 28.32 ? 5   SER D C   1 
ATOM   5565 O O   . SER D 1 5   ? -1.472  29.933  -41.922 1.00 26.13 ? 5   SER D O   1 
ATOM   5566 C CB  . SER D 1 5   ? -4.127  29.434  -43.924 1.00 27.29 ? 5   SER D CB  1 
ATOM   5567 O OG  . SER D 1 5   ? -4.212  30.770  -43.421 1.00 29.31 ? 5   SER D OG  1 
ATOM   5568 N N   . ARG D 1 6   ? -1.087  29.339  -44.070 1.00 25.85 ? 6   ARG D N   1 
ATOM   5569 C CA  . ARG D 1 6   ? 0.200   30.030  -44.128 1.00 25.18 ? 6   ARG D CA  1 
ATOM   5570 C C   . ARG D 1 6   ? 0.064   31.524  -43.814 1.00 28.22 ? 6   ARG D C   1 
ATOM   5571 O O   . ARG D 1 6   ? 0.928   32.119  -43.151 1.00 28.64 ? 6   ARG D O   1 
ATOM   5572 C CB  . ARG D 1 6   ? 0.811   29.836  -45.510 1.00 29.46 ? 6   ARG D CB  1 
ATOM   5573 C CG  . ARG D 1 6   ? 1.710   30.984  -45.924 1.00 37.63 ? 6   ARG D CG  1 
ATOM   5574 C CD  . ARG D 1 6   ? 2.644   30.586  -47.042 1.00 41.75 ? 6   ARG D CD  1 
ATOM   5575 N NE  . ARG D 1 6   ? 2.026   30.892  -48.324 1.00 48.96 ? 6   ARG D NE  1 
ATOM   5576 C CZ  . ARG D 1 6   ? 1.414   29.997  -49.084 1.00 53.51 ? 6   ARG D CZ  1 
ATOM   5577 N NH1 . ARG D 1 6   ? 1.267   28.740  -48.690 1.00 49.84 ? 6   ARG D NH1 1 
ATOM   5578 N NH2 . ARG D 1 6   ? 0.897   30.380  -50.249 1.00 58.63 ? 6   ARG D NH2 1 
ATOM   5579 N N   . ASP D 1 7   ? -0.984  32.161  -44.323 1.00 26.50 ? 7   ASP D N   1 
ATOM   5580 C CA  . ASP D 1 7   ? -1.185  33.585  -44.071 1.00 29.25 ? 7   ASP D CA  1 
ATOM   5581 C C   . ASP D 1 7   ? -1.339  33.870  -42.577 1.00 27.88 ? 7   ASP D C   1 
ATOM   5582 O O   . ASP D 1 7   ? -0.728  34.804  -42.044 1.00 25.38 ? 7   ASP D O   1 
ATOM   5583 C CB  . ASP D 1 7   ? -2.412  34.059  -44.840 1.00 27.34 ? 7   ASP D CB  1 
ATOM   5584 C CG  . ASP D 1 7   ? -2.195  34.067  -46.339 1.00 30.92 ? 7   ASP D CG  1 
ATOM   5585 O OD1 . ASP D 1 7   ? -1.119  34.490  -46.800 1.00 33.97 ? 7   ASP D OD1 1 
ATOM   5586 O OD2 . ASP D 1 7   ? -3.099  33.605  -47.057 1.00 35.02 ? 7   ASP D OD2 1 
ATOM   5587 N N   . MET D 1 8   ? -2.175  33.089  -41.882 1.00 25.44 ? 8   MET D N   1 
ATOM   5588 C CA  . MET D 1 8   ? -2.280  33.261  -40.434 1.00 24.52 ? 8   MET D CA  1 
ATOM   5589 C C   . MET D 1 8   ? -0.959  32.944  -39.750 1.00 25.37 ? 8   MET D C   1 
ATOM   5590 O O   . MET D 1 8   ? -0.579  33.597  -38.772 1.00 25.74 ? 8   MET D O   1 
ATOM   5591 C CB  . MET D 1 8   ? -3.412  32.392  -39.890 1.00 23.81 ? 8   MET D CB  1 
ATOM   5592 C CG  . MET D 1 8   ? -4.805  33.075  -39.882 1.00 25.19 ? 8   MET D CG  1 
ATOM   5593 S SD  . MET D 1 8   ? -5.525  33.098  -41.526 1.00 30.23 ? 8   MET D SD  1 
ATOM   5594 C CE  . MET D 1 8   ? -7.122  33.882  -41.201 1.00 31.28 ? 8   MET D CE  1 
ATOM   5595 N N   . LEU D 1 9   ? -0.248  31.930  -40.238 1.00 25.57 ? 9   LEU D N   1 
ATOM   5596 C CA  . LEU D 1 9   ? 1.030   31.596  -39.617 1.00 26.59 ? 9   LEU D CA  1 
ATOM   5597 C C   . LEU D 1 9   ? 2.021   32.725  -39.806 1.00 21.73 ? 9   LEU D C   1 
ATOM   5598 O O   . LEU D 1 9   ? 2.778   33.058  -38.882 1.00 24.17 ? 9   LEU D O   1 
ATOM   5599 C CB  . LEU D 1 9   ? 1.571   30.302  -40.217 1.00 21.39 ? 9   LEU D CB  1 
ATOM   5600 C CG  . LEU D 1 9   ? 0.723   29.084  -39.852 1.00 23.46 ? 9   LEU D CG  1 
ATOM   5601 C CD1 . LEU D 1 9   ? 1.284   27.903  -40.580 1.00 24.61 ? 9   LEU D CD1 1 
ATOM   5602 C CD2 . LEU D 1 9   ? 0.804   28.832  -38.373 1.00 24.96 ? 9   LEU D CD2 1 
ATOM   5603 N N   . GLN D 1 10  ? 2.033   33.318  -41.002 1.00 21.88 ? 10  GLN D N   1 
ATOM   5604 C CA  . GLN D 1 10  ? 2.964   34.416  -41.270 1.00 24.46 ? 10  GLN D CA  1 
ATOM   5605 C C   . GLN D 1 10  ? 2.654   35.627  -40.403 1.00 25.44 ? 10  GLN D C   1 
ATOM   5606 O O   . GLN D 1 10  ? 3.558   36.234  -39.814 1.00 23.93 ? 10  GLN D O   1 
ATOM   5607 C CB  . GLN D 1 10  ? 2.935   34.786  -42.746 1.00 26.06 ? 10  GLN D CB  1 
ATOM   5608 C CG  . GLN D 1 10  ? 3.782   33.860  -43.606 1.00 30.99 ? 10  GLN D CG  1 
ATOM   5609 C CD  . GLN D 1 10  ? 3.576   34.099  -45.100 1.00 38.06 ? 10  GLN D CD  1 
ATOM   5610 O OE1 . GLN D 1 10  ? 4.151   33.392  -45.937 1.00 39.81 ? 10  GLN D OE1 1 
ATOM   5611 N NE2 . GLN D 1 10  ? 2.769   35.106  -45.439 1.00 27.84 ? 10  GLN D NE2 1 
ATOM   5612 N N   . ASP D 1 11  ? 1.366   35.993  -40.310 1.00 25.70 ? 11  ASP D N   1 
ATOM   5613 C CA  . ASP D 1 11  ? 0.977   37.117  -39.468 1.00 27.62 ? 11  ASP D CA  1 
ATOM   5614 C C   . ASP D 1 11  ? 1.257   36.809  -38.010 1.00 26.39 ? 11  ASP D C   1 
ATOM   5615 O O   . ASP D 1 11  ? 1.794   37.650  -37.286 1.00 23.31 ? 11  ASP D O   1 
ATOM   5616 C CB  . ASP D 1 11  ? -0.503  37.440  -39.673 1.00 27.31 ? 11  ASP D CB  1 
ATOM   5617 C CG  . ASP D 1 11  ? -1.068  38.371  -38.580 1.00 31.94 ? 11  ASP D CG  1 
ATOM   5618 O OD1 . ASP D 1 11  ? -0.822  39.595  -38.637 1.00 30.35 ? 11  ASP D OD1 1 
ATOM   5619 O OD2 . ASP D 1 11  ? -1.724  37.862  -37.647 1.00 31.73 ? 11  ASP D OD2 1 
ATOM   5620 N N   . GLY D 1 12  ? 0.917   35.597  -37.565 1.00 26.36 ? 12  GLY D N   1 
ATOM   5621 C CA  . GLY D 1 12  ? 1.177   35.241  -36.177 1.00 25.53 ? 12  GLY D CA  1 
ATOM   5622 C C   . GLY D 1 12  ? 2.653   35.298  -35.836 1.00 24.55 ? 12  GLY D C   1 
ATOM   5623 O O   . GLY D 1 12  ? 3.031   35.782  -34.768 1.00 24.37 ? 12  GLY D O   1 
ATOM   5624 N N   . ALA D 1 13  ? 3.515   34.860  -36.763 1.00 22.72 ? 13  ALA D N   1 
ATOM   5625 C CA  . ALA D 1 13  ? 4.956   34.931  -36.510 1.00 23.68 ? 13  ALA D CA  1 
ATOM   5626 C C   . ALA D 1 13  ? 5.435   36.376  -36.428 1.00 23.62 ? 13  ALA D C   1 
ATOM   5627 O O   . ALA D 1 13  ? 6.243   36.713  -35.561 1.00 24.72 ? 13  ALA D O   1 
ATOM   5628 C CB  . ALA D 1 13  ? 5.733   34.162  -37.591 1.00 22.66 ? 13  ALA D CB  1 
ATOM   5629 N N   . LYS D 1 14  ? 4.912   37.261  -37.282 1.00 24.08 ? 14  LYS D N   1 
ATOM   5630 C CA  . LYS D 1 14  ? 5.351   38.655  -37.224 1.00 26.50 ? 14  LYS D CA  1 
ATOM   5631 C C   . LYS D 1 14  ? 4.904   39.292  -35.911 1.00 28.71 ? 14  LYS D C   1 
ATOM   5632 O O   . LYS D 1 14  ? 5.628   40.102  -35.324 1.00 27.76 ? 14  LYS D O   1 
ATOM   5633 C CB  . LYS D 1 14  ? 4.783   39.443  -38.407 1.00 30.54 ? 14  LYS D CB  1 
ATOM   5634 C CG  . LYS D 1 14  ? 5.444   40.846  -38.609 1.00 33.25 ? 14  LYS D CG  1 
ATOM   5635 C CD  . LYS D 1 14  ? 6.980   40.737  -38.626 1.00 33.30 ? 14  LYS D CD  1 
ATOM   5636 C CE  . LYS D 1 14  ? 7.651   41.991  -39.192 1.00 44.33 ? 14  LYS D CE  1 
ATOM   5637 N NZ  . LYS D 1 14  ? 7.758   41.975  -40.678 1.00 50.64 ? 14  LYS D NZ  1 
ATOM   5638 N N   . ARG D 1 15  ? 3.723   38.907  -35.413 1.00 24.31 ? 15  ARG D N   1 
ATOM   5639 C CA  . ARG D 1 15  ? 3.240   39.455  -34.148 1.00 26.61 ? 15  ARG D CA  1 
ATOM   5640 C C   . ARG D 1 15  ? 4.099   39.000  -32.981 1.00 25.51 ? 15  ARG D C   1 
ATOM   5641 O O   . ARG D 1 15  ? 4.375   39.793  -32.080 1.00 27.38 ? 15  ARG D O   1 
ATOM   5642 C CB  . ARG D 1 15  ? 1.763   39.072  -33.923 1.00 24.38 ? 15  ARG D CB  1 
ATOM   5643 C CG  . ARG D 1 15  ? 0.824   39.840  -34.863 1.00 27.18 ? 15  ARG D CG  1 
ATOM   5644 C CD  . ARG D 1 15  ? -0.559  39.166  -35.044 1.00 31.17 ? 15  ARG D CD  1 
ATOM   5645 N NE  . ARG D 1 15  ? -1.147  38.746  -33.785 1.00 30.19 ? 15  ARG D NE  1 
ATOM   5646 C CZ  . ARG D 1 15  ? -1.967  37.712  -33.620 1.00 32.78 ? 15  ARG D CZ  1 
ATOM   5647 N NH1 . ARG D 1 15  ? -2.313  36.923  -34.629 1.00 31.61 ? 15  ARG D NH1 1 
ATOM   5648 N NH2 . ARG D 1 15  ? -2.489  37.490  -32.417 1.00 31.56 ? 15  ARG D NH2 1 
ATOM   5649 N N   . MET D 1 16  ? 4.559   37.733  -32.995 1.00 24.83 ? 16  MET D N   1 
ATOM   5650 C CA  . MET D 1 16  ? 5.496   37.245  -31.974 1.00 23.55 ? 16  MET D CA  1 
ATOM   5651 C C   . MET D 1 16  ? 6.836   37.960  -32.049 1.00 25.68 ? 16  MET D C   1 
ATOM   5652 O O   . MET D 1 16  ? 7.446   38.280  -31.024 1.00 24.54 ? 16  MET D O   1 
ATOM   5653 C CB  . MET D 1 16  ? 5.747   35.746  -32.154 1.00 24.06 ? 16  MET D CB  1 
ATOM   5654 C CG  . MET D 1 16  ? 4.547   34.851  -32.141 1.00 27.47 ? 16  MET D CG  1 
ATOM   5655 S SD  . MET D 1 16  ? 3.839   34.755  -30.496 1.00 27.23 ? 16  MET D SD  1 
ATOM   5656 C CE  . MET D 1 16  ? 5.235   34.242  -29.520 1.00 22.00 ? 16  MET D CE  1 
ATOM   5657 N N   . PHE D 1 17  ? 7.333   38.138  -33.261 1.00 25.74 ? 17  PHE D N   1 
ATOM   5658 C CA  . PHE D 1 17  ? 8.589   38.835  -33.493 1.00 25.90 ? 17  PHE D CA  1 
ATOM   5659 C C   . PHE D 1 17  ? 8.520   40.274  -32.992 1.00 28.63 ? 17  PHE D C   1 
ATOM   5660 O O   . PHE D 1 17  ? 9.412   40.734  -32.267 1.00 29.57 ? 17  PHE D O   1 
ATOM   5661 C CB  . PHE D 1 17  ? 8.863   38.784  -34.989 1.00 24.17 ? 17  PHE D CB  1 
ATOM   5662 C CG  . PHE D 1 17  ? 10.119  39.460  -35.421 1.00 26.45 ? 17  PHE D CG  1 
ATOM   5663 C CD1 . PHE D 1 17  ? 11.350  38.919  -35.125 1.00 25.78 ? 17  PHE D CD1 1 
ATOM   5664 C CD2 . PHE D 1 17  ? 10.061  40.604  -36.189 1.00 32.64 ? 17  PHE D CD2 1 
ATOM   5665 C CE1 . PHE D 1 17  ? 12.488  39.514  -35.562 1.00 28.18 ? 17  PHE D CE1 1 
ATOM   5666 C CE2 . PHE D 1 17  ? 11.224  41.219  -36.629 1.00 33.52 ? 17  PHE D CE2 1 
ATOM   5667 C CZ  . PHE D 1 17  ? 12.439  40.651  -36.321 1.00 30.30 ? 17  PHE D CZ  1 
ATOM   5668 N N   . LYS D 1 18  ? 7.449   40.993  -33.350 1.00 27.93 ? 18  LYS D N   1 
ATOM   5669 C CA  . LYS D 1 18  ? 7.289   42.369  -32.880 1.00 27.71 ? 18  LYS D CA  1 
ATOM   5670 C C   . LYS D 1 18  ? 7.141   42.417  -31.365 1.00 30.70 ? 18  LYS D C   1 
ATOM   5671 O O   . LYS D 1 18  ? 7.647   43.339  -30.711 1.00 30.05 ? 18  LYS D O   1 
ATOM   5672 C CB  . LYS D 1 18  ? 6.093   43.012  -33.578 1.00 31.59 ? 18  LYS D CB  1 
ATOM   5673 C CG  . LYS D 1 18  ? 6.281   43.138  -35.085 1.00 33.37 ? 18  LYS D CG  1 
ATOM   5674 C CD  . LYS D 1 18  ? 5.229   44.028  -35.745 1.00 35.05 ? 18  LYS D CD  1 
ATOM   5675 C CE  . LYS D 1 18  ? 5.140   45.389  -35.084 1.00 44.59 ? 18  LYS D CE  1 
ATOM   5676 N NZ  . LYS D 1 18  ? 3.864   46.088  -35.430 1.00 47.48 ? 18  LYS D NZ  1 
ATOM   5677 N N   . TRP D 1 19  ? 6.436   41.438  -30.788 1.00 28.37 ? 19  TRP D N   1 
ATOM   5678 C CA  . TRP D 1 19  ? 6.299   41.373  -29.335 1.00 29.71 ? 19  TRP D CA  1 
ATOM   5679 C C   . TRP D 1 19  ? 7.647   41.163  -28.662 1.00 28.87 ? 19  TRP D C   1 
ATOM   5680 O O   . TRP D 1 19  ? 7.987   41.854  -27.690 1.00 25.82 ? 19  TRP D O   1 
ATOM   5681 C CB  . TRP D 1 19  ? 5.327   40.244  -28.941 1.00 28.58 ? 19  TRP D CB  1 
ATOM   5682 C CG  . TRP D 1 19  ? 5.093   40.142  -27.450 1.00 27.97 ? 19  TRP D CG  1 
ATOM   5683 C CD1 . TRP D 1 19  ? 5.916   39.568  -26.521 1.00 26.37 ? 19  TRP D CD1 1 
ATOM   5684 C CD2 . TRP D 1 19  ? 3.958   40.633  -26.725 1.00 29.19 ? 19  TRP D CD2 1 
ATOM   5685 N NE1 . TRP D 1 19  ? 5.360   39.674  -25.261 1.00 28.98 ? 19  TRP D NE1 1 
ATOM   5686 C CE2 . TRP D 1 19  ? 4.158   40.321  -25.364 1.00 29.19 ? 19  TRP D CE2 1 
ATOM   5687 C CE3 . TRP D 1 19  ? 2.781   41.296  -27.097 1.00 32.48 ? 19  TRP D CE3 1 
ATOM   5688 C CZ2 . TRP D 1 19  ? 3.227   40.676  -24.371 1.00 29.69 ? 19  TRP D CZ2 1 
ATOM   5689 C CZ3 . TRP D 1 19  ? 1.857   41.627  -26.114 1.00 34.10 ? 19  TRP D CZ3 1 
ATOM   5690 C CH2 . TRP D 1 19  ? 2.081   41.309  -24.776 1.00 31.17 ? 19  TRP D CH2 1 
ATOM   5691 N N   . LEU D 1 20  ? 8.421   40.182  -29.150 1.00 26.91 ? 20  LEU D N   1 
ATOM   5692 C CA  . LEU D 1 20  ? 9.740   39.913  -28.582 1.00 30.18 ? 20  LEU D CA  1 
ATOM   5693 C C   . LEU D 1 20  ? 10.643  41.133  -28.689 1.00 29.56 ? 20  LEU D C   1 
ATOM   5694 O O   . LEU D 1 20  ? 11.549  41.322  -27.862 1.00 30.92 ? 20  LEU D O   1 
ATOM   5695 C CB  . LEU D 1 20  ? 10.395  38.704  -29.293 1.00 27.13 ? 20  LEU D CB  1 
ATOM   5696 C CG  . LEU D 1 20  ? 9.949   37.277  -28.933 1.00 30.80 ? 20  LEU D CG  1 
ATOM   5697 C CD1 . LEU D 1 20  ? 10.492  36.202  -29.911 1.00 26.75 ? 20  LEU D CD1 1 
ATOM   5698 C CD2 . LEU D 1 20  ? 10.339  36.892  -27.495 1.00 29.08 ? 20  LEU D CD2 1 
ATOM   5699 N N   . ARG D 1 21  ? 10.392  41.991  -29.675 1.00 26.31 ? 21  ARG D N   1 
ATOM   5700 C CA  . ARG D 1 21  ? 11.221  43.174  -29.863 1.00 30.73 ? 21  ARG D CA  1 
ATOM   5701 C C   . ARG D 1 21  ? 11.211  44.086  -28.645 1.00 32.24 ? 21  ARG D C   1 
ATOM   5702 O O   . ARG D 1 21  ? 12.158  44.855  -28.451 1.00 30.81 ? 21  ARG D O   1 
ATOM   5703 C CB  . ARG D 1 21  ? 10.739  43.926  -31.098 1.00 30.76 ? 21  ARG D CB  1 
ATOM   5704 C CG  . ARG D 1 21  ? 11.572  45.131  -31.479 1.00 37.07 ? 21  ARG D CG  1 
ATOM   5705 C CD  . ARG D 1 21  ? 11.358  45.431  -32.944 1.00 37.43 ? 21  ARG D CD  1 
ATOM   5706 N NE  . ARG D 1 21  ? 9.987   45.880  -33.177 1.00 35.77 ? 21  ARG D NE  1 
ATOM   5707 C CZ  . ARG D 1 21  ? 9.473   46.051  -34.385 1.00 37.54 ? 21  ARG D CZ  1 
ATOM   5708 N NH1 . ARG D 1 21  ? 10.191  45.830  -35.474 1.00 40.48 ? 21  ARG D NH1 1 
ATOM   5709 N NH2 . ARG D 1 21  ? 8.225   46.483  -34.505 1.00 41.35 ? 21  ARG D NH2 1 
ATOM   5710 N N   . LYS D 1 22  ? 10.176  43.992  -27.805 1.00 29.10 ? 22  LYS D N   1 
ATOM   5711 C CA  . LYS D 1 22  ? 10.087  44.792  -26.593 1.00 30.58 ? 22  LYS D CA  1 
ATOM   5712 C C   . LYS D 1 22  ? 11.073  44.356  -25.523 1.00 34.15 ? 22  LYS D C   1 
ATOM   5713 O O   . LYS D 1 22  ? 11.317  45.121  -24.587 1.00 34.16 ? 22  LYS D O   1 
ATOM   5714 C CB  . LYS D 1 22  ? 8.661   44.725  -26.039 1.00 32.58 ? 22  LYS D CB  1 
ATOM   5715 C CG  . LYS D 1 22  ? 7.624   45.256  -27.024 1.00 36.26 ? 22  LYS D CG  1 
ATOM   5716 C CD  . LYS D 1 22  ? 6.166   45.046  -26.583 1.00 37.14 ? 22  LYS D CD  1 
ATOM   5717 C CE  . LYS D 1 22  ? 5.963   43.795  -25.768 1.00 38.16 ? 22  LYS D CE  1 
ATOM   5718 N NZ  . LYS D 1 22  ? 4.624   43.836  -25.134 1.00 40.39 ? 22  LYS D NZ  1 
ATOM   5719 N N   . GLY D 1 23  ? 11.693  43.186  -25.665 1.00 34.34 ? 23  GLY D N   1 
ATOM   5720 C CA  . GLY D 1 23  ? 12.622  42.722  -24.653 1.00 33.36 ? 23  GLY D CA  1 
ATOM   5721 C C   . GLY D 1 23  ? 11.992  42.242  -23.366 1.00 33.35 ? 23  GLY D C   1 
ATOM   5722 O O   . GLY D 1 23  ? 12.686  42.153  -22.347 1.00 31.25 ? 23  GLY D O   1 
ATOM   5723 N N   . GLU D 1 24  ? 10.693  41.930  -23.371 1.00 32.77 ? 24  GLU D N   1 
ATOM   5724 C CA  . GLU D 1 24  ? 10.005  41.466  -22.170 1.00 34.51 ? 24  GLU D CA  1 
ATOM   5725 C C   . GLU D 1 24  ? 9.586   39.997  -22.257 1.00 36.52 ? 24  GLU D C   1 
ATOM   5726 O O   . GLU D 1 24  ? 8.698   39.564  -21.508 1.00 32.81 ? 24  GLU D O   1 
ATOM   5727 C CB  . GLU D 1 24  ? 8.780   42.339  -21.891 1.00 34.19 ? 24  GLU D CB  1 
ATOM   5728 C CG  . GLU D 1 24  ? 9.055   43.841  -21.836 1.00 38.34 ? 24  GLU D CG  1 
ATOM   5729 C CD  . GLU D 1 24  ? 7.769   44.645  -21.840 1.00 43.73 ? 24  GLU D CD  1 
ATOM   5730 O OE1 . GLU D 1 24  ? 7.480   45.343  -22.834 1.00 51.87 ? 24  GLU D OE1 1 
ATOM   5731 O OE2 . GLU D 1 24  ? 7.006   44.534  -20.861 1.00 58.53 ? 24  GLU D OE2 1 
ATOM   5732 N N   . GLY D 1 25  ? 10.217  39.208  -23.133 1.00 32.98 ? 25  GLY D N   1 
ATOM   5733 C CA  . GLY D 1 25  ? 9.885   37.799  -23.210 1.00 31.56 ? 25  GLY D CA  1 
ATOM   5734 C C   . GLY D 1 25  ? 8.684   37.516  -24.098 1.00 31.56 ? 25  GLY D C   1 
ATOM   5735 O O   . GLY D 1 25  ? 8.161   38.385  -24.804 1.00 29.96 ? 25  GLY D O   1 
ATOM   5736 N N   . LEU D 1 26  ? 8.254   36.236  -24.072 1.00 30.74 ? 26  LEU D N   1 
ATOM   5737 C CA  . LEU D 1 26  ? 7.170   35.731  -24.899 1.00 28.25 ? 26  LEU D CA  1 
ATOM   5738 C C   . LEU D 1 26  ? 5.820   36.185  -24.345 1.00 28.03 ? 26  LEU D C   1 
ATOM   5739 O O   . LEU D 1 26  ? 5.689   36.428  -23.147 1.00 27.99 ? 26  LEU D O   1 
ATOM   5740 C CB  . LEU D 1 26  ? 7.216   34.200  -24.965 1.00 27.38 ? 26  LEU D CB  1 
ATOM   5741 C CG  . LEU D 1 26  ? 8.348   33.536  -25.775 1.00 30.79 ? 26  LEU D CG  1 
ATOM   5742 C CD1 . LEU D 1 26  ? 8.299   32.044  -25.587 1.00 32.80 ? 26  LEU D CD1 1 
ATOM   5743 C CD2 . LEU D 1 26  ? 8.241   33.865  -27.259 1.00 28.16 ? 26  LEU D CD2 1 
ATOM   5744 N N   . PRO D 1 27  ? 4.822   36.347  -25.206 1.00 24.87 ? 27  PRO D N   1 
ATOM   5745 C CA  . PRO D 1 27  ? 3.477   36.704  -24.732 1.00 26.16 ? 27  PRO D CA  1 
ATOM   5746 C C   . PRO D 1 27  ? 2.793   35.521  -24.063 1.00 26.63 ? 27  PRO D C   1 
ATOM   5747 O O   . PRO D 1 27  ? 3.137   34.363  -24.291 1.00 24.49 ? 27  PRO D O   1 
ATOM   5748 C CB  . PRO D 1 27  ? 2.743   37.103  -26.015 1.00 27.77 ? 27  PRO D CB  1 
ATOM   5749 C CG  . PRO D 1 27  ? 3.425   36.219  -27.101 1.00 26.35 ? 27  PRO D CG  1 
ATOM   5750 C CD  . PRO D 1 27  ? 4.884   36.206  -26.672 1.00 24.18 ? 27  PRO D CD  1 
ATOM   5751 N N   . ASN D 1 28  ? 1.755   35.826  -23.275 1.00 26.55 ? 28  ASN D N   1 
ATOM   5752 C CA  . ASN D 1 28  ? 1.050   34.761  -22.565 1.00 24.97 ? 28  ASN D CA  1 
ATOM   5753 C C   . ASN D 1 28  ? 0.280   33.846  -23.506 1.00 23.71 ? 28  ASN D C   1 
ATOM   5754 O O   . ASN D 1 28  ? 0.015   32.699  -23.148 1.00 26.56 ? 28  ASN D O   1 
ATOM   5755 C CB  . ASN D 1 28  ? 0.061   35.367  -21.562 1.00 25.42 ? 28  ASN D CB  1 
ATOM   5756 C CG  . ASN D 1 28  ? 0.705   35.695  -20.224 1.00 29.20 ? 28  ASN D CG  1 
ATOM   5757 O OD1 . ASN D 1 28  ? 1.922   35.617  -20.081 1.00 26.69 ? 28  ASN D OD1 1 
ATOM   5758 N ND2 . ASN D 1 28  ? -0.103  36.193  -19.274 1.00 26.34 ? 28  ASN D ND2 1 
ATOM   5759 N N   . TYR D 1 29  ? -0.078  34.309  -24.698 1.00 24.01 ? 29  TYR D N   1 
ATOM   5760 C CA  . TYR D 1 29  ? -0.808  33.475  -25.642 1.00 26.29 ? 29  TYR D CA  1 
ATOM   5761 C C   . TYR D 1 29  ? -0.712  34.115  -27.012 1.00 26.33 ? 29  TYR D C   1 
ATOM   5762 O O   . TYR D 1 29  ? -0.196  35.222  -27.160 1.00 25.97 ? 29  TYR D O   1 
ATOM   5763 C CB  . TYR D 1 29  ? -2.273  33.297  -25.239 1.00 26.56 ? 29  TYR D CB  1 
ATOM   5764 C CG  . TYR D 1 29  ? -2.958  34.592  -24.842 1.00 25.34 ? 29  TYR D CG  1 
ATOM   5765 C CD1 . TYR D 1 29  ? -3.464  35.469  -25.796 1.00 25.68 ? 29  TYR D CD1 1 
ATOM   5766 C CD2 . TYR D 1 29  ? -3.068  34.943  -23.512 1.00 29.38 ? 29  TYR D CD2 1 
ATOM   5767 C CE1 . TYR D 1 29  ? -4.079  36.651  -25.421 1.00 28.09 ? 29  TYR D CE1 1 
ATOM   5768 C CE2 . TYR D 1 29  ? -3.699  36.135  -23.129 1.00 31.31 ? 29  TYR D CE2 1 
ATOM   5769 C CZ  . TYR D 1 29  ? -4.203  36.970  -24.082 1.00 28.07 ? 29  TYR D CZ  1 
ATOM   5770 O OH  . TYR D 1 29  ? -4.811  38.150  -23.678 1.00 25.53 ? 29  TYR D OH  1 
ATOM   5771 N N   . LEU D 1 30  ? -1.196  33.392  -28.021 1.00 26.13 ? 30  LEU D N   1 
ATOM   5772 C CA  . LEU D 1 30  ? -1.244  33.899  -29.385 1.00 27.94 ? 30  LEU D CA  1 
ATOM   5773 C C   . LEU D 1 30  ? -2.614  33.565  -29.948 1.00 27.32 ? 30  LEU D C   1 
ATOM   5774 O O   . LEU D 1 30  ? -2.977  32.393  -30.033 1.00 27.41 ? 30  LEU D O   1 
ATOM   5775 C CB  . LEU D 1 30  ? -0.126  33.285  -30.241 1.00 21.72 ? 30  LEU D CB  1 
ATOM   5776 C CG  . LEU D 1 30  ? -0.144  33.663  -31.716 1.00 26.73 ? 30  LEU D CG  1 
ATOM   5777 C CD1 . LEU D 1 30  ? 0.232   35.164  -31.919 1.00 25.58 ? 30  LEU D CD1 1 
ATOM   5778 C CD2 . LEU D 1 30  ? 0.827   32.769  -32.542 1.00 27.31 ? 30  LEU D CD2 1 
ATOM   5779 N N   . ILE D 1 31  ? -3.374  34.592  -30.312 1.00 27.51 ? 31  ILE D N   1 
ATOM   5780 C CA  . ILE D 1 31  ? -4.706  34.425  -30.876 1.00 30.54 ? 31  ILE D CA  1 
ATOM   5781 C C   . ILE D 1 31  ? -4.593  34.234  -32.375 1.00 30.38 ? 31  ILE D C   1 
ATOM   5782 O O   . ILE D 1 31  ? -3.935  35.029  -33.056 1.00 27.88 ? 31  ILE D O   1 
ATOM   5783 C CB  . ILE D 1 31  ? -5.595  35.636  -30.554 1.00 35.62 ? 31  ILE D CB  1 
ATOM   5784 C CG1 . ILE D 1 31  ? -5.772  35.761  -29.043 1.00 37.97 ? 31  ILE D CG1 1 
ATOM   5785 C CG2 . ILE D 1 31  ? -6.936  35.505  -31.278 1.00 37.84 ? 31  ILE D CG2 1 
ATOM   5786 C CD1 . ILE D 1 31  ? -6.820  34.850  -28.514 1.00 36.51 ? 31  ILE D CD1 1 
ATOM   5787 N N   . MET D 1 32  ? -5.236  33.194  -32.894 1.00 27.43 ? 32  MET D N   1 
ATOM   5788 C CA  . MET D 1 32  ? -5.232  32.987  -34.330 1.00 29.30 ? 32  MET D CA  1 
ATOM   5789 C C   . MET D 1 32  ? -6.558  32.362  -34.742 1.00 28.69 ? 32  MET D C   1 
ATOM   5790 O O   . MET D 1 32  ? -7.199  31.647  -33.968 1.00 31.37 ? 32  MET D O   1 
ATOM   5791 C CB  . MET D 1 32  ? -4.026  32.121  -34.716 1.00 27.47 ? 32  MET D CB  1 
ATOM   5792 C CG  . MET D 1 32  ? -2.836  32.995  -35.086 1.00 33.46 ? 32  MET D CG  1 
ATOM   5793 S SD  . MET D 1 32  ? -1.412  32.143  -35.789 1.00 40.02 ? 32  MET D SD  1 
ATOM   5794 C CE  . MET D 1 32  ? -2.140  30.621  -36.272 1.00 24.93 ? 32  MET D CE  1 
ATOM   5795 N N   . TYR D 1 33  ? -6.918  32.572  -36.002 1.00 31.58 ? 33  TYR D N   1 
ATOM   5796 C CA  . TYR D 1 33  ? -8.171  32.093  -36.569 1.00 30.78 ? 33  TYR D CA  1 
ATOM   5797 C C   . TYR D 1 33  ? -7.890  30.897  -37.455 1.00 32.41 ? 33  TYR D C   1 
ATOM   5798 O O   . TYR D 1 33  ? -7.013  30.956  -38.318 1.00 30.17 ? 33  TYR D O   1 
ATOM   5799 C CB  . TYR D 1 33  ? -8.838  33.185  -37.408 1.00 31.93 ? 33  TYR D CB  1 
ATOM   5800 C CG  . TYR D 1 33  ? -9.552  34.220  -36.570 1.00 32.49 ? 33  TYR D CG  1 
ATOM   5801 C CD1 . TYR D 1 33  ? -8.863  35.299  -36.051 1.00 32.64 ? 33  TYR D CD1 1 
ATOM   5802 C CD2 . TYR D 1 33  ? -10.905 34.090  -36.267 1.00 31.67 ? 33  TYR D CD2 1 
ATOM   5803 C CE1 . TYR D 1 33  ? -9.502  36.253  -35.274 1.00 34.06 ? 33  TYR D CE1 1 
ATOM   5804 C CE2 . TYR D 1 33  ? -11.555 35.037  -35.489 1.00 35.19 ? 33  TYR D CE2 1 
ATOM   5805 C CZ  . TYR D 1 33  ? -10.841 36.115  -34.987 1.00 34.03 ? 33  TYR D CZ  1 
ATOM   5806 O OH  . TYR D 1 33  ? -11.446 37.082  -34.200 1.00 34.35 ? 33  TYR D OH  1 
ATOM   5807 N N   . ASP D 1 34  ? -8.632  29.817  -37.245 1.00 32.78 ? 34  ASP D N   1 
ATOM   5808 C CA  . ASP D 1 34  ? -8.379  28.616  -38.013 1.00 31.46 ? 34  ASP D CA  1 
ATOM   5809 C C   . ASP D 1 34  ? -8.905  28.797  -39.437 1.00 33.96 ? 34  ASP D C   1 
ATOM   5810 O O   . ASP D 1 34  ? -9.754  29.648  -39.708 1.00 33.26 ? 34  ASP D O   1 
ATOM   5811 C CB  . ASP D 1 34  ? -9.018  27.413  -37.323 1.00 32.02 ? 34  ASP D CB  1 
ATOM   5812 C CG  . ASP D 1 34  ? -10.484 27.257  -37.683 1.00 34.40 ? 34  ASP D CG  1 
ATOM   5813 O OD1 . ASP D 1 34  ? -11.284 28.084  -37.218 1.00 33.81 ? 34  ASP D OD1 1 
ATOM   5814 O OD2 . ASP D 1 34  ? -10.827 26.316  -38.429 1.00 36.56 ? 34  ASP D OD2 1 
ATOM   5815 N N   . MET D 1 35  ? -8.363  28.007  -40.365 1.00 29.31 ? 35  MET D N   1 
ATOM   5816 C CA  . MET D 1 35  ? -8.667  28.208  -41.779 1.00 33.78 ? 35  MET D CA  1 
ATOM   5817 C C   . MET D 1 35  ? -9.949  27.531  -42.189 1.00 37.15 ? 35  MET D C   1 
ATOM   5818 O O   . MET D 1 35  ? -10.485 27.832  -43.278 1.00 38.59 ? 35  MET D O   1 
ATOM   5819 C CB  . MET D 1 35  ? -7.529  27.685  -42.635 1.00 33.40 ? 35  MET D CB  1 
ATOM   5820 C CG  . MET D 1 35  ? -7.427  26.193  -42.746 1.00 35.32 ? 35  MET D CG  1 
ATOM   5821 S SD  . MET D 1 35  ? -5.948  25.710  -43.696 1.00 39.04 ? 35  MET D SD  1 
ATOM   5822 C CE  . MET D 1 35  ? -6.544  25.964  -45.367 1.00 40.94 ? 35  MET D CE  1 
ATOM   5823 N N   . ASP D 1 36  ? -10.488 26.657  -41.340 1.00 37.01 ? 36  ASP D N   1 
ATOM   5824 C CA  . ASP D 1 36  ? -11.709 25.870  -41.687 1.00 40.48 ? 36  ASP D CA  1 
ATOM   5825 C C   . ASP D 1 36  ? -13.007 26.500  -41.159 1.00 42.31 ? 36  ASP D C   1 
ATOM   5826 O O   . ASP D 1 36  ? -13.975 26.520  -41.895 1.00 42.61 ? 36  ASP D O   1 
ATOM   5827 C CB  . ASP D 1 36  ? -11.571 24.408  -41.262 1.00 36.35 ? 36  ASP D CB  1 
ATOM   5828 C CG  . ASP D 1 36  ? -10.401 23.689  -41.915 1.00 39.50 ? 36  ASP D CG  1 
ATOM   5829 O OD1 . ASP D 1 36  ? -10.336 23.679  -43.130 1.00 38.89 ? 36  ASP D OD1 1 
ATOM   5830 O OD2 . ASP D 1 36  ? -9.591  23.150  -41.200 1.00 37.03 ? 36  ASP D OD2 1 
ATOM   5831 N N   . ARG D 1 37  ? -13.027 26.988  -39.927 1.00 44.08 ? 37  ARG D N   1 
ATOM   5832 C CA  . ARG D 1 37  ? -14.272 27.552  -39.355 1.00 44.27 ? 37  ARG D CA  1 
ATOM   5833 C C   . ARG D 1 37  ? -14.150 29.060  -39.157 1.00 43.67 ? 37  ARG D C   1 
ATOM   5834 O O   . ARG D 1 37  ? -15.142 29.676  -38.849 1.00 45.14 ? 37  ARG D O   1 
ATOM   5835 C CB  . ARG D 1 37  ? -14.437 27.013  -37.940 1.00 50.26 ? 37  ARG D CB  1 
ATOM   5836 C CG  . ARG D 1 37  ? -15.065 25.637  -37.868 1.00 51.95 ? 37  ARG D CG  1 
ATOM   5837 C CD  . ARG D 1 37  ? -14.629 24.970  -36.588 1.00 57.86 ? 37  ARG D CD  1 
ATOM   5838 N NE  . ARG D 1 37  ? -13.284 24.541  -36.856 1.00 57.26 ? 37  ARG D NE  1 
ATOM   5839 C CZ  . ARG D 1 37  ? -12.665 23.568  -36.239 1.00 54.52 ? 37  ARG D CZ  1 
ATOM   5840 N NH1 . ARG D 1 37  ? -13.270 22.907  -35.275 1.00 56.85 ? 37  ARG D NH1 1 
ATOM   5841 N NH2 . ARG D 1 37  ? -11.425 23.285  -36.576 1.00 57.99 ? 37  ARG D NH2 1 
ATOM   5842 N N   . ASN D 1 38  ? -12.956 29.600  -39.323 1.00 35.88 ? 38  ASN D N   1 
ATOM   5843 C CA  . ASN D 1 38  ? -12.695 31.026  -39.030 1.00 43.25 ? 38  ASN D CA  1 
ATOM   5844 C C   . ASN D 1 38  ? -13.109 31.350  -37.611 1.00 41.21 ? 38  ASN D C   1 
ATOM   5845 O O   . ASN D 1 38  ? -13.652 32.418  -37.401 1.00 42.86 ? 38  ASN D O   1 
ATOM   5846 C CB  . ASN D 1 38  ? -13.295 32.025  -40.012 1.00 41.60 ? 38  ASN D CB  1 
ATOM   5847 C CG  . ASN D 1 38  ? -12.595 31.914  -41.335 1.00 43.41 ? 38  ASN D CG  1 
ATOM   5848 O OD1 . ASN D 1 38  ? -13.166 31.394  -42.275 1.00 48.63 ? 38  ASN D OD1 1 
ATOM   5849 N ND2 . ASN D 1 38  ? -11.339 32.315  -41.377 1.00 45.19 ? 38  ASN D ND2 1 
ATOM   5850 N N   . LYS D 1 39  ? -12.812 30.437  -36.711 1.00 37.59 ? 39  LYS D N   1 
ATOM   5851 C CA  . LYS D 1 39  ? -13.108 30.612  -35.279 1.00 39.02 ? 39  LYS D CA  1 
ATOM   5852 C C   . LYS D 1 39  ? -11.815 31.043  -34.592 1.00 38.49 ? 39  LYS D C   1 
ATOM   5853 O O   . LYS D 1 39  ? -10.776 30.587  -34.994 1.00 35.48 ? 39  LYS D O   1 
ATOM   5854 C CB  . LYS D 1 39  ? -13.567 29.269  -34.724 1.00 45.97 ? 39  LYS D CB  1 
ATOM   5855 C CG  . LYS D 1 39  ? -13.761 29.228  -33.215 1.00 51.46 ? 39  LYS D CG  1 
ATOM   5856 C CD  . LYS D 1 39  ? -14.257 27.891  -32.708 1.00 57.59 ? 39  LYS D CD  1 
ATOM   5857 C CE  . LYS D 1 39  ? -14.496 27.876  -31.210 1.00 56.57 ? 39  LYS D CE  1 
ATOM   5858 N NZ  . LYS D 1 39  ? -13.977 26.639  -30.585 1.00 60.47 ? 39  LYS D NZ  1 
ATOM   5859 N N   . GLU D 1 40  ? -11.921 31.879  -33.574 1.00 38.51 ? 40  GLU D N   1 
ATOM   5860 C CA  . GLU D 1 40  ? -10.807 32.358  -32.822 1.00 36.63 ? 40  GLU D CA  1 
ATOM   5861 C C   . GLU D 1 40  ? -10.267 31.245  -31.965 1.00 38.13 ? 40  GLU D C   1 
ATOM   5862 O O   . GLU D 1 40  ? -11.011 30.595  -31.234 1.00 33.17 ? 40  GLU D O   1 
ATOM   5863 C CB  . GLU D 1 40  ? -11.244 33.518  -31.954 1.00 39.25 ? 40  GLU D CB  1 
ATOM   5864 C CG  . GLU D 1 40  ? -10.110 34.287  -31.374 1.00 40.15 ? 40  GLU D CG  1 
ATOM   5865 C CD  . GLU D 1 40  ? -10.596 35.560  -30.737 1.00 43.57 ? 40  GLU D CD  1 
ATOM   5866 O OE1 . GLU D 1 40  ? -11.678 36.001  -31.121 1.00 47.97 ? 40  GLU D OE1 1 
ATOM   5867 O OE2 . GLU D 1 40  ? -9.929  36.099  -29.839 1.00 45.49 ? 40  GLU D OE2 1 
ATOM   5868 N N   . TYR D 1 41  ? -8.954  31.016  -32.056 1.00 32.03 ? 41  TYR D N   1 
ATOM   5869 C CA  . TYR D 1 41  ? -8.285  30.069  -31.169 1.00 33.96 ? 41  TYR D CA  1 
ATOM   5870 C C   . TYR D 1 41  ? -7.200  30.797  -30.387 1.00 33.40 ? 41  TYR D C   1 
ATOM   5871 O O   . TYR D 1 41  ? -6.391  31.533  -30.959 1.00 34.04 ? 41  TYR D O   1 
ATOM   5872 C CB  . TYR D 1 41  ? -7.668  28.887  -31.945 1.00 31.59 ? 41  TYR D CB  1 
ATOM   5873 C CG  . TYR D 1 41  ? -8.694  27.909  -32.408 1.00 33.26 ? 41  TYR D CG  1 
ATOM   5874 C CD1 . TYR D 1 41  ? -9.296  28.055  -33.642 1.00 34.72 ? 41  TYR D CD1 1 
ATOM   5875 C CD2 . TYR D 1 41  ? -9.078  26.840  -31.600 1.00 37.73 ? 41  TYR D CD2 1 
ATOM   5876 C CE1 . TYR D 1 41  ? -10.264 27.179  -34.073 1.00 37.30 ? 41  TYR D CE1 1 
ATOM   5877 C CE2 . TYR D 1 41  ? -10.056 25.942  -32.021 1.00 41.28 ? 41  TYR D CE2 1 
ATOM   5878 C CZ  . TYR D 1 41  ? -10.644 26.125  -33.260 1.00 39.47 ? 41  TYR D CZ  1 
ATOM   5879 O OH  . TYR D 1 41  ? -11.603 25.262  -33.709 1.00 43.56 ? 41  TYR D OH  1 
ATOM   5880 N N   . LYS D 1 42  ? -7.165  30.536  -29.091 1.00 29.21 ? 42  LYS D N   1 
ATOM   5881 C CA  . LYS D 1 42  ? -6.153  31.063  -28.186 1.00 31.89 ? 42  LYS D CA  1 
ATOM   5882 C C   . LYS D 1 42  ? -5.118  29.986  -27.897 1.00 32.53 ? 42  LYS D C   1 
ATOM   5883 O O   . LYS D 1 42  ? -5.416  29.006  -27.218 1.00 28.17 ? 42  LYS D O   1 
ATOM   5884 C CB  . LYS D 1 42  ? -6.752  31.583  -26.886 1.00 31.30 ? 42  LYS D CB  1 
ATOM   5885 C CG  . LYS D 1 42  ? -5.757  32.466  -26.169 1.00 31.45 ? 42  LYS D CG  1 
ATOM   5886 C CD  . LYS D 1 42  ? -5.970  32.511  -24.676 1.00 36.65 ? 42  LYS D CD  1 
ATOM   5887 C CE  . LYS D 1 42  ? -6.756  33.769  -24.295 1.00 36.91 ? 42  LYS D CE  1 
ATOM   5888 N NZ  . LYS D 1 42  ? -6.912  33.852  -22.800 1.00 40.52 ? 42  LYS D NZ  1 
ATOM   5889 N N   . LEU D 1 43  ? -3.936  30.118  -28.507 1.00 29.78 ? 43  LEU D N   1 
ATOM   5890 C CA  . LEU D 1 43  ? -2.844  29.175  -28.288 1.00 24.81 ? 43  LEU D CA  1 
ATOM   5891 C C   . LEU D 1 43  ? -2.042  29.559  -27.044 1.00 25.16 ? 43  LEU D C   1 
ATOM   5892 O O   . LEU D 1 43  ? -1.496  30.665  -26.973 1.00 27.51 ? 43  LEU D O   1 
ATOM   5893 C CB  . LEU D 1 43  ? -1.945  29.162  -29.524 1.00 24.27 ? 43  LEU D CB  1 
ATOM   5894 C CG  . LEU D 1 43  ? -2.735  28.805  -30.781 1.00 27.15 ? 43  LEU D CG  1 
ATOM   5895 C CD1 . LEU D 1 43  ? -1.837  28.879  -32.023 1.00 30.99 ? 43  LEU D CD1 1 
ATOM   5896 C CD2 . LEU D 1 43  ? -3.382  27.404  -30.637 1.00 28.59 ? 43  LEU D CD2 1 
ATOM   5897 N N   . VAL D 1 44  ? -1.916  28.644  -26.088 1.00 23.10 ? 44  VAL D N   1 
ATOM   5898 C CA  . VAL D 1 44  ? -1.045  28.862  -24.929 1.00 22.94 ? 44  VAL D CA  1 
ATOM   5899 C C   . VAL D 1 44  ? 0.393   28.638  -25.405 1.00 26.91 ? 44  VAL D C   1 
ATOM   5900 O O   . VAL D 1 44  ? 0.588   28.133  -26.519 1.00 24.16 ? 44  VAL D O   1 
ATOM   5901 C CB  . VAL D 1 44  ? -1.438  27.958  -23.749 1.00 23.60 ? 44  VAL D CB  1 
ATOM   5902 C CG1 . VAL D 1 44  ? -2.903  28.264  -23.285 1.00 22.98 ? 44  VAL D CG1 1 
ATOM   5903 C CG2 . VAL D 1 44  ? -1.352  26.522  -24.159 1.00 25.62 ? 44  VAL D CG2 1 
ATOM   5904 N N   . PRO D 1 45  ? 1.420   29.058  -24.651 1.00 25.32 ? 45  PRO D N   1 
ATOM   5905 C CA  . PRO D 1 45  ? 2.789   29.017  -25.210 1.00 25.74 ? 45  PRO D CA  1 
ATOM   5906 C C   . PRO D 1 45  ? 3.251   27.646  -25.689 1.00 26.11 ? 45  PRO D C   1 
ATOM   5907 O O   . PRO D 1 45  ? 3.856   27.549  -26.768 1.00 24.97 ? 45  PRO D O   1 
ATOM   5908 C CB  . PRO D 1 45  ? 3.644   29.546  -24.051 1.00 25.82 ? 45  PRO D CB  1 
ATOM   5909 C CG  . PRO D 1 45  ? 2.686   30.553  -23.347 1.00 28.67 ? 45  PRO D CG  1 
ATOM   5910 C CD  . PRO D 1 45  ? 1.351   29.846  -23.400 1.00 25.58 ? 45  PRO D CD  1 
ATOM   5911 N N   . LYS D 1 46  ? 3.004   26.578  -24.929 1.00 26.31 ? 46  LYS D N   1 
ATOM   5912 C CA  . LYS D 1 46  ? 3.396   25.251  -25.416 1.00 26.93 ? 46  LYS D CA  1 
ATOM   5913 C C   . LYS D 1 46  ? 2.667   24.888  -26.710 1.00 25.51 ? 46  LYS D C   1 
ATOM   5914 O O   . LYS D 1 46  ? 3.173   24.082  -27.503 1.00 26.43 ? 46  LYS D O   1 
ATOM   5915 C CB  . LYS D 1 46  ? 3.164   24.197  -24.327 1.00 30.21 ? 46  LYS D CB  1 
ATOM   5916 C CG  . LYS D 1 46  ? 1.688   23.824  -24.178 1.00 29.22 ? 46  LYS D CG  1 
ATOM   5917 C CD  . LYS D 1 46  ? 1.428   22.580  -23.344 1.00 34.47 ? 46  LYS D CD  1 
ATOM   5918 C CE  . LYS D 1 46  ? 1.174   22.904  -21.878 1.00 43.96 ? 46  LYS D CE  1 
ATOM   5919 N NZ  . LYS D 1 46  ? 0.678   21.688  -21.096 1.00 44.96 ? 46  LYS D NZ  1 
ATOM   5920 N N   . GLU D 1 47  ? 1.491   25.473  -26.951 1.00 24.19 ? 47  GLU D N   1 
ATOM   5921 C CA  . GLU D 1 47  ? 0.749   25.207  -28.182 1.00 24.14 ? 47  GLU D CA  1 
ATOM   5922 C C   . GLU D 1 47  ? 1.300   26.006  -29.356 1.00 25.03 ? 47  GLU D C   1 
ATOM   5923 O O   . GLU D 1 47  ? 1.460   25.471  -30.460 1.00 26.74 ? 47  GLU D O   1 
ATOM   5924 C CB  . GLU D 1 47  ? -0.726  25.557  -28.007 1.00 27.48 ? 47  GLU D CB  1 
ATOM   5925 C CG  . GLU D 1 47  ? -1.488  24.627  -27.090 1.00 28.64 ? 47  GLU D CG  1 
ATOM   5926 C CD  . GLU D 1 47  ? -2.953  24.985  -27.060 1.00 31.58 ? 47  GLU D CD  1 
ATOM   5927 O OE1 . GLU D 1 47  ? -3.254  26.146  -26.676 1.00 29.65 ? 47  GLU D OE1 1 
ATOM   5928 O OE2 . GLU D 1 47  ? -3.787  24.096  -27.334 1.00 32.97 ? 47  GLU D OE2 1 
ATOM   5929 N N   . TYR D 1 48  ? 1.562   27.303  -29.169 1.00 21.50 ? 48  TYR D N   1 
ATOM   5930 C CA  . TYR D 1 48  ? 2.103   27.993  -30.328 1.00 25.27 ? 48  TYR D CA  1 
ATOM   5931 C C   . TYR D 1 48  ? 3.538   27.556  -30.603 1.00 22.21 ? 48  TYR D C   1 
ATOM   5932 O O   . TYR D 1 48  ? 3.937   27.487  -31.760 1.00 26.37 ? 48  TYR D O   1 
ATOM   5933 C CB  . TYR D 1 48  ? 1.974   29.517  -30.205 1.00 24.00 ? 48  TYR D CB  1 
ATOM   5934 C CG  . TYR D 1 48  ? 2.632   30.294  -29.077 1.00 25.44 ? 48  TYR D CG  1 
ATOM   5935 C CD1 . TYR D 1 48  ? 4.015   30.402  -28.977 1.00 23.59 ? 48  TYR D CD1 1 
ATOM   5936 C CD2 . TYR D 1 48  ? 1.834   31.036  -28.166 1.00 26.22 ? 48  TYR D CD2 1 
ATOM   5937 C CE1 . TYR D 1 48  ? 4.617   31.192  -27.973 1.00 25.00 ? 48  TYR D CE1 1 
ATOM   5938 C CE2 . TYR D 1 48  ? 2.408   31.822  -27.152 1.00 25.42 ? 48  TYR D CE2 1 
ATOM   5939 C CZ  . TYR D 1 48  ? 3.809   31.907  -27.058 1.00 27.89 ? 48  TYR D CZ  1 
ATOM   5940 O OH  . TYR D 1 48  ? 4.408   32.692  -26.058 1.00 24.11 ? 48  TYR D OH  1 
ATOM   5941 N N   . ALA D 1 49  ? 4.307   27.194  -29.580 1.00 21.56 ? 49  ALA D N   1 
ATOM   5942 C CA  . ALA D 1 49  ? 5.643   26.667  -29.846 1.00 25.23 ? 49  ALA D CA  1 
ATOM   5943 C C   . ALA D 1 49  ? 5.561   25.361  -30.623 1.00 23.61 ? 49  ALA D C   1 
ATOM   5944 O O   . ALA D 1 49  ? 6.317   25.148  -31.575 1.00 25.66 ? 49  ALA D O   1 
ATOM   5945 C CB  . ALA D 1 49  ? 6.410   26.464  -28.541 1.00 24.12 ? 49  ALA D CB  1 
ATOM   5946 N N   . GLY D 1 50  ? 4.624   24.491  -30.240 1.00 24.32 ? 50  GLY D N   1 
ATOM   5947 C CA  . GLY D 1 50  ? 4.423   23.237  -30.957 1.00 27.27 ? 50  GLY D CA  1 
ATOM   5948 C C   . GLY D 1 50  ? 3.983   23.447  -32.390 1.00 26.72 ? 50  GLY D C   1 
ATOM   5949 O O   . GLY D 1 50  ? 4.464   22.768  -33.303 1.00 24.86 ? 50  GLY D O   1 
ATOM   5950 N N   . LEU D 1 51  ? 3.071   24.393  -32.608 1.00 23.45 ? 51  LEU D N   1 
ATOM   5951 C CA  . LEU D 1 51  ? 2.602   24.699  -33.956 1.00 23.91 ? 51  LEU D CA  1 
ATOM   5952 C C   . LEU D 1 51  ? 3.749   25.206  -34.838 1.00 24.65 ? 51  LEU D C   1 
ATOM   5953 O O   . LEU D 1 51  ? 3.919   24.764  -35.985 1.00 22.66 ? 51  LEU D O   1 
ATOM   5954 C CB  . LEU D 1 51  ? 1.481   25.742  -33.870 1.00 21.18 ? 51  LEU D CB  1 
ATOM   5955 C CG  . LEU D 1 51  ? 0.797   26.115  -35.186 1.00 24.26 ? 51  LEU D CG  1 
ATOM   5956 C CD1 . LEU D 1 51  ? -0.120  24.967  -35.635 1.00 25.45 ? 51  LEU D CD1 1 
ATOM   5957 C CD2 . LEU D 1 51  ? -0.013  27.390  -34.995 1.00 25.21 ? 51  LEU D CD2 1 
ATOM   5958 N N   . TYR D 1 52  ? 4.525   26.165  -34.327 1.00 20.13 ? 52  TYR D N   1 
ATOM   5959 C CA  . TYR D 1 52  ? 5.602   26.729  -35.141 1.00 22.10 ? 52  TYR D CA  1 
ATOM   5960 C C   . TYR D 1 52  ? 6.775   25.757  -35.236 1.00 21.82 ? 52  TYR D C   1 
ATOM   5961 O O   . TYR D 1 52  ? 7.519   25.771  -36.229 1.00 24.18 ? 52  TYR D O   1 
ATOM   5962 C CB  . TYR D 1 52  ? 6.017   28.115  -34.597 1.00 21.61 ? 52  TYR D CB  1 
ATOM   5963 C CG  . TYR D 1 52  ? 5.037   29.172  -35.070 1.00 21.15 ? 52  TYR D CG  1 
ATOM   5964 C CD1 . TYR D 1 52  ? 5.131   29.706  -36.347 1.00 23.44 ? 52  TYR D CD1 1 
ATOM   5965 C CD2 . TYR D 1 52  ? 3.940   29.538  -34.286 1.00 24.52 ? 52  TYR D CD2 1 
ATOM   5966 C CE1 . TYR D 1 52  ? 4.198   30.631  -36.813 1.00 23.74 ? 52  TYR D CE1 1 
ATOM   5967 C CE2 . TYR D 1 52  ? 2.997   30.465  -34.741 1.00 24.85 ? 52  TYR D CE2 1 
ATOM   5968 C CZ  . TYR D 1 52  ? 3.125   30.996  -36.008 1.00 24.55 ? 52  TYR D CZ  1 
ATOM   5969 O OH  . TYR D 1 52  ? 2.190   31.913  -36.467 1.00 24.13 ? 52  TYR D OH  1 
ATOM   5970 N N   . GLU D 1 53  ? 6.933   24.875  -34.251 1.00 21.59 ? 53  GLU D N   1 
ATOM   5971 C CA  . GLU D 1 53  ? 7.897   23.788  -34.408 1.00 26.21 ? 53  GLU D CA  1 
ATOM   5972 C C   . GLU D 1 53  ? 7.570   22.931  -35.620 1.00 23.45 ? 53  GLU D C   1 
ATOM   5973 O O   . GLU D 1 53  ? 8.457   22.609  -36.428 1.00 23.13 ? 53  GLU D O   1 
ATOM   5974 C CB  . GLU D 1 53  ? 7.941   22.923  -33.151 1.00 22.90 ? 53  GLU D CB  1 
ATOM   5975 C CG  . GLU D 1 53  ? 9.043   21.852  -33.196 1.00 27.57 ? 53  GLU D CG  1 
ATOM   5976 C CD  . GLU D 1 53  ? 8.950   20.912  -32.025 1.00 26.73 ? 53  GLU D CD  1 
ATOM   5977 O OE1 . GLU D 1 53  ? 7.878   20.283  -31.863 1.00 24.46 ? 53  GLU D OE1 1 
ATOM   5978 O OE2 . GLU D 1 53  ? 9.934   20.827  -31.246 1.00 25.82 ? 53  GLU D OE2 1 
ATOM   5979 N N   . SER D 1 54  ? 6.296   22.546  -35.752 1.00 23.00 ? 54  SER D N   1 
ATOM   5980 C CA  . SER D 1 54  ? 5.851   21.712  -36.859 1.00 24.74 ? 54  SER D CA  1 
ATOM   5981 C C   . SER D 1 54  ? 5.963   22.440  -38.183 1.00 23.24 ? 54  SER D C   1 
ATOM   5982 O O   . SER D 1 54  ? 6.415   21.857  -39.177 1.00 22.12 ? 54  SER D O   1 
ATOM   5983 C CB  . SER D 1 54  ? 4.411   21.231  -36.604 1.00 27.33 ? 54  SER D CB  1 
ATOM   5984 O OG  . SER D 1 54  ? 3.892   20.557  -37.745 1.00 28.22 ? 54  SER D OG  1 
ATOM   5985 N N   . ARG D 1 55  ? 5.558   23.716  -38.219 1.00 22.82 ? 55  ARG D N   1 
ATOM   5986 C CA  . ARG D 1 55  ? 5.772   24.530  -39.406 1.00 21.77 ? 55  ARG D CA  1 
ATOM   5987 C C   . ARG D 1 55  ? 7.253   24.562  -39.778 1.00 23.00 ? 55  ARG D C   1 
ATOM   5988 O O   . ARG D 1 55  ? 7.599   24.429  -40.958 1.00 24.94 ? 55  ARG D O   1 
ATOM   5989 C CB  . ARG D 1 55  ? 5.218   25.959  -39.174 1.00 22.97 ? 55  ARG D CB  1 
ATOM   5990 C CG  . ARG D 1 55  ? 5.603   26.974  -40.225 1.00 24.75 ? 55  ARG D CG  1 
ATOM   5991 C CD  . ARG D 1 55  ? 5.377   28.406  -39.766 1.00 21.48 ? 55  ARG D CD  1 
ATOM   5992 N NE  . ARG D 1 55  ? 5.231   29.342  -40.884 1.00 26.82 ? 55  ARG D NE  1 
ATOM   5993 C CZ  . ARG D 1 55  ? 5.638   30.615  -40.878 1.00 24.18 ? 55  ARG D CZ  1 
ATOM   5994 N NH1 . ARG D 1 55  ? 6.271   31.146  -39.839 1.00 23.81 ? 55  ARG D NH1 1 
ATOM   5995 N NH2 . ARG D 1 55  ? 5.427   31.373  -41.953 1.00 24.21 ? 55  ARG D NH2 1 
ATOM   5996 N N   . ASN D 1 56  ? 8.150   24.707  -38.786 1.00 20.92 ? 56  ASN D N   1 
ATOM   5997 C CA  . ASN D 1 56  ? 9.584   24.801  -39.092 1.00 21.55 ? 56  ASN D CA  1 
ATOM   5998 C C   . ASN D 1 56  ? 10.181  23.466  -39.538 1.00 21.70 ? 56  ASN D C   1 
ATOM   5999 O O   . ASN D 1 56  ? 11.153  23.454  -40.296 1.00 21.54 ? 56  ASN D O   1 
ATOM   6000 C CB  . ASN D 1 56  ? 10.361  25.319  -37.881 1.00 21.70 ? 56  ASN D CB  1 
ATOM   6001 C CG  . ASN D 1 56  ? 10.079  26.786  -37.595 1.00 23.52 ? 56  ASN D CG  1 
ATOM   6002 O OD1 . ASN D 1 56  ? 9.570   27.491  -38.465 1.00 22.94 ? 56  ASN D OD1 1 
ATOM   6003 N ND2 . ASN D 1 56  ? 10.375  27.239  -36.368 1.00 19.54 ? 56  ASN D ND2 1 
ATOM   6004 N N   . ILE D 1 57  ? 9.653   22.337  -39.056 1.00 20.37 ? 57  ILE D N   1 
ATOM   6005 C CA  . ILE D 1 57  ? 10.119  21.029  -39.547 1.00 23.76 ? 57  ILE D CA  1 
ATOM   6006 C C   . ILE D 1 57  ? 9.873   20.915  -41.049 1.00 24.93 ? 57  ILE D C   1 
ATOM   6007 O O   . ILE D 1 57  ? 10.776  20.570  -41.828 1.00 25.71 ? 57  ILE D O   1 
ATOM   6008 C CB  . ILE D 1 57  ? 9.439   19.883  -38.769 1.00 24.46 ? 57  ILE D CB  1 
ATOM   6009 C CG1 . ILE D 1 57  ? 10.001  19.837  -37.346 1.00 21.27 ? 57  ILE D CG1 1 
ATOM   6010 C CG2 . ILE D 1 57  ? 9.671   18.546  -39.502 1.00 24.64 ? 57  ILE D CG2 1 
ATOM   6011 C CD1 . ILE D 1 57  ? 9.344   18.824  -36.423 1.00 27.01 ? 57  ILE D CD1 1 
ATOM   6012 N N   . PHE D 1 58  ? 8.648   21.201  -41.479 1.00 22.50 ? 58  PHE D N   1 
ATOM   6013 C CA  . PHE D 1 58  ? 8.341   21.144  -42.904 1.00 23.74 ? 58  PHE D CA  1 
ATOM   6014 C C   . PHE D 1 58  ? 9.215   22.113  -43.686 1.00 25.35 ? 58  PHE D C   1 
ATOM   6015 O O   . PHE D 1 58  ? 9.774   21.764  -44.737 1.00 22.58 ? 58  PHE D O   1 
ATOM   6016 C CB  . PHE D 1 58  ? 6.869   21.466  -43.127 1.00 23.16 ? 58  PHE D CB  1 
ATOM   6017 C CG  . PHE D 1 58  ? 6.420   21.328  -44.555 1.00 27.17 ? 58  PHE D CG  1 
ATOM   6018 C CD1 . PHE D 1 58  ? 6.747   22.290  -45.511 1.00 25.60 ? 58  PHE D CD1 1 
ATOM   6019 C CD2 . PHE D 1 58  ? 5.668   20.234  -44.944 1.00 27.96 ? 58  PHE D CD2 1 
ATOM   6020 C CE1 . PHE D 1 58  ? 6.341   22.156  -46.810 1.00 28.79 ? 58  PHE D CE1 1 
ATOM   6021 C CE2 . PHE D 1 58  ? 5.247   20.110  -46.254 1.00 29.72 ? 58  PHE D CE2 1 
ATOM   6022 C CZ  . PHE D 1 58  ? 5.572   21.066  -47.179 1.00 29.04 ? 58  PHE D CZ  1 
ATOM   6023 N N   . TRP D 1 59  ? 9.320   23.351  -43.195 1.00 24.91 ? 59  TRP D N   1 
ATOM   6024 C CA  . TRP D 1 59  ? 10.083  24.368  -43.909 1.00 22.78 ? 59  TRP D CA  1 
ATOM   6025 C C   . TRP D 1 59  ? 11.539  23.958  -44.061 1.00 24.10 ? 59  TRP D C   1 
ATOM   6026 O O   . TRP D 1 59  ? 12.125  24.102  -45.139 1.00 27.38 ? 59  TRP D O   1 
ATOM   6027 C CB  . TRP D 1 59  ? 9.969   25.688  -43.154 1.00 22.84 ? 59  TRP D CB  1 
ATOM   6028 C CG  . TRP D 1 59  ? 10.122  26.929  -43.961 1.00 27.07 ? 59  TRP D CG  1 
ATOM   6029 C CD1 . TRP D 1 59  ? 10.686  27.063  -45.192 1.00 26.68 ? 59  TRP D CD1 1 
ATOM   6030 C CD2 . TRP D 1 59  ? 9.673   28.233  -43.574 1.00 26.82 ? 59  TRP D CD2 1 
ATOM   6031 N NE1 . TRP D 1 59  ? 10.619  28.380  -45.595 1.00 27.55 ? 59  TRP D NE1 1 
ATOM   6032 C CE2 . TRP D 1 59  ? 10.004  29.116  -44.615 1.00 27.61 ? 59  TRP D CE2 1 
ATOM   6033 C CE3 . TRP D 1 59  ? 9.026   28.733  -42.439 1.00 23.46 ? 59  TRP D CE3 1 
ATOM   6034 C CZ2 . TRP D 1 59  ? 9.709   30.498  -44.555 1.00 27.43 ? 59  TRP D CZ2 1 
ATOM   6035 C CZ3 . TRP D 1 59  ? 8.746   30.097  -42.379 1.00 27.23 ? 59  TRP D CZ3 1 
ATOM   6036 C CH2 . TRP D 1 59  ? 9.078   30.957  -43.430 1.00 26.42 ? 59  TRP D CH2 1 
ATOM   6037 N N   . ILE D 1 60  ? 12.160  23.491  -42.978 1.00 24.16 ? 60  ILE D N   1 
ATOM   6038 C CA  . ILE D 1 60  ? 13.573  23.116  -43.028 1.00 24.17 ? 60  ILE D CA  1 
ATOM   6039 C C   . ILE D 1 60  ? 13.772  21.868  -43.889 1.00 26.21 ? 60  ILE D C   1 
ATOM   6040 O O   . ILE D 1 60  ? 14.732  21.757  -44.658 1.00 26.32 ? 60  ILE D O   1 
ATOM   6041 C CB  . ILE D 1 60  ? 14.108  22.907  -41.597 1.00 24.40 ? 60  ILE D CB  1 
ATOM   6042 C CG1 . ILE D 1 60  ? 14.332  24.264  -40.907 1.00 23.09 ? 60  ILE D CG1 1 
ATOM   6043 C CG2 . ILE D 1 60  ? 15.483  22.137  -41.654 1.00 26.34 ? 60  ILE D CG2 1 
ATOM   6044 C CD1 . ILE D 1 60  ? 14.688  24.143  -39.426 1.00 23.70 ? 60  ILE D CD1 1 
ATOM   6045 N N   . LYS D 1 61  ? 12.915  20.877  -43.725 1.00 25.55 ? 61  LYS D N   1 
ATOM   6046 C CA  . LYS D 1 61  ? 13.095  19.642  -44.481 1.00 25.27 ? 61  LYS D CA  1 
ATOM   6047 C C   . LYS D 1 61  ? 12.777  19.848  -45.962 1.00 26.68 ? 61  LYS D C   1 
ATOM   6048 O O   . LYS D 1 61  ? 13.470  19.321  -46.831 1.00 28.76 ? 61  LYS D O   1 
ATOM   6049 C CB  . LYS D 1 61  ? 12.238  18.543  -43.859 1.00 24.66 ? 61  LYS D CB  1 
ATOM   6050 C CG  . LYS D 1 61  ? 12.083  17.318  -44.739 1.00 34.15 ? 61  LYS D CG  1 
ATOM   6051 C CD  . LYS D 1 61  ? 13.081  16.230  -44.357 1.00 31.41 ? 61  LYS D CD  1 
ATOM   6052 C CE  . LYS D 1 61  ? 13.307  15.194  -45.452 1.00 36.59 ? 61  LYS D CE  1 
ATOM   6053 N NZ  . LYS D 1 61  ? 14.715  14.621  -45.394 1.00 36.83 ? 61  LYS D NZ  1 
ATOM   6054 N N   . ASN D 1 62  ? 11.759  20.636  -46.285 1.00 25.95 ? 62  ASN D N   1 
ATOM   6055 C CA  . ASN D 1 62  ? 11.377  20.732  -47.686 1.00 26.70 ? 62  ASN D CA  1 
ATOM   6056 C C   . ASN D 1 62  ? 11.874  21.988  -48.358 1.00 27.62 ? 62  ASN D C   1 
ATOM   6057 O O   . ASN D 1 62  ? 11.744  22.102  -49.573 1.00 28.71 ? 62  ASN D O   1 
ATOM   6058 C CB  . ASN D 1 62  ? 9.856   20.655  -47.840 1.00 27.60 ? 62  ASN D CB  1 
ATOM   6059 C CG  . ASN D 1 62  ? 9.329   19.309  -47.463 1.00 28.72 ? 62  ASN D CG  1 
ATOM   6060 O OD1 . ASN D 1 62  ? 9.760   18.306  -48.022 1.00 31.61 ? 62  ASN D OD1 1 
ATOM   6061 N ND2 . ASN D 1 62  ? 8.417   19.264  -46.509 1.00 26.49 ? 62  ASN D ND2 1 
ATOM   6062 N N   . GLY D 1 63  ? 12.416  22.933  -47.606 1.00 28.91 ? 63  GLY D N   1 
ATOM   6063 C CA  . GLY D 1 63  ? 12.907  24.142  -48.224 1.00 28.78 ? 63  GLY D CA  1 
ATOM   6064 C C   . GLY D 1 63  ? 11.844  25.103  -48.700 1.00 32.86 ? 63  GLY D C   1 
ATOM   6065 O O   . GLY D 1 63  ? 12.181  26.073  -49.377 1.00 30.96 ? 63  GLY D O   1 
ATOM   6066 N N   . ARG D 1 64  ? 10.578  24.883  -48.362 1.00 29.50 ? 64  ARG D N   1 
ATOM   6067 C CA  . ARG D 1 64  ? 9.514   25.808  -48.741 1.00 32.31 ? 64  ARG D CA  1 
ATOM   6068 C C   . ARG D 1 64  ? 8.487   25.780  -47.621 1.00 31.00 ? 64  ARG D C   1 
ATOM   6069 O O   . ARG D 1 64  ? 8.373   24.799  -46.881 1.00 27.10 ? 64  ARG D O   1 
ATOM   6070 C CB  . ARG D 1 64  ? 8.878   25.470  -50.112 1.00 33.42 ? 64  ARG D CB  1 
ATOM   6071 C CG  . ARG D 1 64  ? 8.326   24.051  -50.193 1.00 33.79 ? 64  ARG D CG  1 
ATOM   6072 C CD  . ARG D 1 64  ? 7.056   23.734  -51.016 1.00 44.34 ? 64  ARG D CD  1 
ATOM   6073 N NE  . ARG D 1 64  ? 7.130   22.281  -51.162 1.00 51.42 ? 64  ARG D NE  1 
ATOM   6074 C CZ  . ARG D 1 64  ? 6.126   21.416  -51.263 1.00 55.24 ? 64  ARG D CZ  1 
ATOM   6075 N NH1 . ARG D 1 64  ? 6.337   20.168  -51.645 1.00 52.04 ? 64  ARG D NH1 1 
ATOM   6076 N NH2 . ARG D 1 64  ? 4.897   21.780  -50.890 1.00 53.58 ? 64  ARG D NH2 1 
ATOM   6077 N N   . GLU D 1 65  ? 7.793   26.901  -47.448 1.00 29.19 ? 65  GLU D N   1 
ATOM   6078 C CA  . GLU D 1 65  ? 6.829   27.044  -46.367 1.00 29.80 ? 65  GLU D CA  1 
ATOM   6079 C C   . GLU D 1 65  ? 5.654   26.080  -46.543 1.00 27.78 ? 65  GLU D C   1 
ATOM   6080 O O   . GLU D 1 65  ? 5.196   25.869  -47.660 1.00 31.82 ? 65  GLU D O   1 
ATOM   6081 C CB  . GLU D 1 65  ? 6.357   28.506  -46.354 1.00 32.76 ? 65  GLU D CB  1 
ATOM   6082 C CG  . GLU D 1 65  ? 5.837   28.990  -45.074 1.00 35.02 ? 65  GLU D CG  1 
ATOM   6083 C CD  . GLU D 1 65  ? 5.446   30.447  -45.152 1.00 31.88 ? 65  GLU D CD  1 
ATOM   6084 O OE1 . GLU D 1 65  ? 5.987   31.204  -46.013 1.00 32.58 ? 65  GLU D OE1 1 
ATOM   6085 O OE2 . GLU D 1 65  ? 4.555   30.810  -44.388 1.00 34.42 ? 65  GLU D OE2 1 
ATOM   6086 N N   . PRO D 1 66  ? 5.108   25.507  -45.462 1.00 27.68 ? 66  PRO D N   1 
ATOM   6087 C CA  . PRO D 1 66  ? 3.868   24.739  -45.616 1.00 29.98 ? 66  PRO D CA  1 
ATOM   6088 C C   . PRO D 1 66  ? 2.685   25.645  -45.907 1.00 30.85 ? 66  PRO D C   1 
ATOM   6089 O O   . PRO D 1 66  ? 2.610   26.773  -45.430 1.00 30.30 ? 66  PRO D O   1 
ATOM   6090 C CB  . PRO D 1 66  ? 3.690   24.044  -44.256 1.00 31.51 ? 66  PRO D CB  1 
ATOM   6091 C CG  . PRO D 1 66  ? 4.435   24.898  -43.302 1.00 30.39 ? 66  PRO D CG  1 
ATOM   6092 C CD  . PRO D 1 66  ? 5.605   25.458  -44.073 1.00 25.44 ? 66  PRO D CD  1 
ATOM   6093 N N   . ASN D 1 67  ? 1.742   25.109  -46.683 1.00 30.59 ? 67  ASN D N   1 
ATOM   6094 C CA  . ASN D 1 67  ? 0.519   25.828  -47.007 1.00 34.61 ? 67  ASN D CA  1 
ATOM   6095 C C   . ASN D 1 67  ? -0.407  25.928  -45.807 1.00 35.30 ? 67  ASN D C   1 
ATOM   6096 O O   . ASN D 1 67  ? -1.222  26.853  -45.732 1.00 32.44 ? 67  ASN D O   1 
ATOM   6097 C CB  . ASN D 1 67  ? -0.198  25.152  -48.170 1.00 31.92 ? 67  ASN D CB  1 
ATOM   6098 C CG  . ASN D 1 67  ? 0.482   25.423  -49.483 1.00 41.35 ? 67  ASN D CG  1 
ATOM   6099 O OD1 . ASN D 1 67  ? 1.147   26.452  -49.643 1.00 43.02 ? 67  ASN D OD1 1 
ATOM   6100 N ND2 . ASN D 1 67  ? 0.356   24.490  -50.425 1.00 45.12 ? 67  ASN D ND2 1 
ATOM   6101 N N   . TYR D 1 68  ? -0.307  24.984  -44.878 1.00 32.75 ? 68  TYR D N   1 
ATOM   6102 C CA  . TYR D 1 68  ? -1.047  25.029  -43.627 1.00 30.12 ? 68  TYR D CA  1 
ATOM   6103 C C   . TYR D 1 68  ? -0.365  24.073  -42.668 1.00 30.28 ? 68  TYR D C   1 
ATOM   6104 O O   . TYR D 1 68  ? 0.443   23.233  -43.077 1.00 27.01 ? 68  TYR D O   1 
ATOM   6105 C CB  . TYR D 1 68  ? -2.534  24.675  -43.824 1.00 32.68 ? 68  TYR D CB  1 
ATOM   6106 C CG  . TYR D 1 68  ? -2.781  23.235  -44.197 1.00 32.43 ? 68  TYR D CG  1 
ATOM   6107 C CD1 . TYR D 1 68  ? -2.949  22.261  -43.216 1.00 35.97 ? 68  TYR D CD1 1 
ATOM   6108 C CD2 . TYR D 1 68  ? -2.862  22.847  -45.521 1.00 35.22 ? 68  TYR D CD2 1 
ATOM   6109 C CE1 . TYR D 1 68  ? -3.180  20.931  -43.543 1.00 40.37 ? 68  TYR D CE1 1 
ATOM   6110 C CE2 . TYR D 1 68  ? -3.088  21.513  -45.867 1.00 40.12 ? 68  TYR D CE2 1 
ATOM   6111 C CZ  . TYR D 1 68  ? -3.250  20.563  -44.868 1.00 43.56 ? 68  TYR D CZ  1 
ATOM   6112 O OH  . TYR D 1 68  ? -3.482  19.244  -45.178 1.00 47.88 ? 68  TYR D OH  1 
ATOM   6113 N N   . VAL D 1 69  ? -0.666  24.236  -41.383 1.00 25.60 ? 69  VAL D N   1 
ATOM   6114 C CA  . VAL D 1 69  ? -0.119  23.388  -40.331 1.00 25.83 ? 69  VAL D CA  1 
ATOM   6115 C C   . VAL D 1 69  ? -1.260  23.032  -39.393 1.00 31.09 ? 69  VAL D C   1 
ATOM   6116 O O   . VAL D 1 69  ? -1.993  23.916  -38.930 1.00 27.85 ? 69  VAL D O   1 
ATOM   6117 C CB  . VAL D 1 69  ? 1.031   24.071  -39.561 1.00 26.49 ? 69  VAL D CB  1 
ATOM   6118 C CG1 . VAL D 1 69  ? 1.568   23.148  -38.468 1.00 25.96 ? 69  VAL D CG1 1 
ATOM   6119 C CG2 . VAL D 1 69  ? 2.167   24.466  -40.504 1.00 26.84 ? 69  VAL D CG2 1 
ATOM   6120 N N   . THR D 1 70  ? -1.446  21.732  -39.156 1.00 29.82 ? 70  THR D N   1 
ATOM   6121 C CA  . THR D 1 70  ? -2.442  21.248  -38.211 1.00 28.90 ? 70  THR D CA  1 
ATOM   6122 C C   . THR D 1 70  ? -1.834  21.261  -36.815 1.00 28.88 ? 70  THR D C   1 
ATOM   6123 O O   . THR D 1 70  ? -0.705  20.817  -36.622 1.00 29.01 ? 70  THR D O   1 
ATOM   6124 C CB  . THR D 1 70  ? -2.878  19.823  -38.596 1.00 30.21 ? 70  THR D CB  1 
ATOM   6125 O OG1 . THR D 1 70  ? -3.444  19.853  -39.910 1.00 32.23 ? 70  THR D OG1 1 
ATOM   6126 C CG2 . THR D 1 70  ? -3.930  19.273  -37.613 1.00 31.94 ? 70  THR D CG2 1 
ATOM   6127 N N   . LEU D 1 71  ? -2.573  21.749  -35.836 1.00 27.35 ? 71  LEU D N   1 
ATOM   6128 C CA  . LEU D 1 71  ? -2.084  21.723  -34.458 1.00 28.84 ? 71  LEU D CA  1 
ATOM   6129 C C   . LEU D 1 71  ? -2.153  20.294  -33.920 1.00 32.48 ? 71  LEU D C   1 
ATOM   6130 O O   . LEU D 1 71  ? -3.244  19.782  -33.642 1.00 32.50 ? 71  LEU D O   1 
ATOM   6131 C CB  . LEU D 1 71  ? -2.906  22.675  -33.594 1.00 29.77 ? 71  LEU D CB  1 
ATOM   6132 C CG  . LEU D 1 71  ? -2.543  22.797  -32.113 1.00 31.23 ? 71  LEU D CG  1 
ATOM   6133 C CD1 . LEU D 1 71  ? -1.107  23.286  -31.908 1.00 30.36 ? 71  LEU D CD1 1 
ATOM   6134 C CD2 . LEU D 1 71  ? -3.559  23.714  -31.396 1.00 37.74 ? 71  LEU D CD2 1 
ATOM   6135 N N   . THR D 1 72  ? -0.995  19.636  -33.793 1.00 26.28 ? 72  THR D N   1 
ATOM   6136 C CA  . THR D 1 72  ? -0.938  18.245  -33.369 1.00 32.54 ? 72  THR D CA  1 
ATOM   6137 C C   . THR D 1 72  ? -0.102  18.009  -32.118 1.00 31.18 ? 72  THR D C   1 
ATOM   6138 O O   . THR D 1 72  ? -0.160  16.912  -31.559 1.00 29.86 ? 72  THR D O   1 
ATOM   6139 C CB  . THR D 1 72  ? -0.367  17.370  -34.501 1.00 31.60 ? 72  THR D CB  1 
ATOM   6140 O OG1 . THR D 1 72  ? 0.950   17.840  -34.832 1.00 30.64 ? 72  THR D OG1 1 
ATOM   6141 C CG2 . THR D 1 72  ? -1.231  17.458  -35.745 1.00 31.18 ? 72  THR D CG2 1 
ATOM   6142 N N   . SER D 1 73  ? 0.670   18.987  -31.665 1.00 29.30 ? 73  SER D N   1 
ATOM   6143 C CA  . SER D 1 73  ? 1.729   18.709  -30.710 1.00 28.61 ? 73  SER D CA  1 
ATOM   6144 C C   . SER D 1 73  ? 1.939   19.915  -29.819 1.00 30.03 ? 73  SER D C   1 
ATOM   6145 O O   . SER D 1 73  ? 1.445   21.006  -30.096 1.00 31.30 ? 73  SER D O   1 
ATOM   6146 C CB  . SER D 1 73  ? 3.041   18.399  -31.445 1.00 31.45 ? 73  SER D CB  1 
ATOM   6147 O OG  . SER D 1 73  ? 3.502   19.601  -32.039 1.00 33.06 ? 73  SER D OG  1 
ATOM   6148 N N   . VAL D 1 74  ? 2.717   19.723  -28.758 1.00 31.14 ? 74  VAL D N   1 
ATOM   6149 C CA  . VAL D 1 74  ? 3.182   20.833  -27.933 1.00 27.91 ? 74  VAL D CA  1 
ATOM   6150 C C   . VAL D 1 74  ? 4.705   20.797  -27.886 1.00 29.01 ? 74  VAL D C   1 
ATOM   6151 O O   . VAL D 1 74  ? 5.340   19.791  -28.215 1.00 26.63 ? 74  VAL D O   1 
ATOM   6152 C CB  . VAL D 1 74  ? 2.565   20.829  -26.510 1.00 32.28 ? 74  VAL D CB  1 
ATOM   6153 C CG1 . VAL D 1 74  ? 1.049   20.913  -26.590 1.00 27.18 ? 74  VAL D CG1 1 
ATOM   6154 C CG2 . VAL D 1 74  ? 2.940   19.564  -25.758 1.00 27.88 ? 74  VAL D CG2 1 
ATOM   6155 N N   . ALA D 1 75  ? 5.295   21.930  -27.519 1.00 26.02 ? 75  ALA D N   1 
ATOM   6156 C CA  . ALA D 1 75  ? 6.750   22.011  -27.438 1.00 30.19 ? 75  ALA D CA  1 
ATOM   6157 C C   . ALA D 1 75  ? 7.139   23.140  -26.499 1.00 31.60 ? 75  ALA D C   1 
ATOM   6158 O O   . ALA D 1 75  ? 6.326   24.015  -26.169 1.00 29.00 ? 75  ALA D O   1 
ATOM   6159 C CB  . ALA D 1 75  ? 7.381   22.220  -28.816 1.00 25.18 ? 75  ALA D CB  1 
ATOM   6160 N N   . ARG D 1 76  ? 8.398   23.096  -26.061 1.00 31.83 ? 76  ARG D N   1 
ATOM   6161 C CA  . ARG D 1 76  ? 8.942   24.130  -25.188 1.00 33.56 ? 76  ARG D CA  1 
ATOM   6162 C C   . ARG D 1 76  ? 9.341   25.380  -25.958 1.00 32.16 ? 76  ARG D C   1 
ATOM   6163 O O   . ARG D 1 76  ? 9.333   26.479  -25.395 1.00 35.52 ? 76  ARG D O   1 
ATOM   6164 C CB  . ARG D 1 76  ? 10.179  23.598  -24.454 1.00 37.81 ? 76  ARG D CB  1 
ATOM   6165 C CG  . ARG D 1 76  ? 9.906   22.797  -23.184 1.00 41.25 ? 76  ARG D CG  1 
ATOM   6166 C CD  . ARG D 1 76  ? 11.097  22.952  -22.214 1.00 46.76 ? 76  ARG D CD  1 
ATOM   6167 N NE  . ARG D 1 76  ? 12.292  22.250  -22.678 1.00 47.33 ? 76  ARG D NE  1 
ATOM   6168 C CZ  . ARG D 1 76  ? 13.514  22.778  -22.758 1.00 46.71 ? 76  ARG D CZ  1 
ATOM   6169 N NH1 . ARG D 1 76  ? 13.755  24.038  -22.433 1.00 43.23 ? 76  ARG D NH1 1 
ATOM   6170 N NH2 . ARG D 1 76  ? 14.522  22.022  -23.184 1.00 41.95 ? 76  ARG D NH2 1 
ATOM   6171 N N   . ASN D 1 77  ? 9.675   25.229  -27.232 1.00 27.80 ? 77  ASN D N   1 
ATOM   6172 C CA  . ASN D 1 77  ? 10.076  26.323  -28.103 1.00 27.61 ? 77  ASN D CA  1 
ATOM   6173 C C   . ASN D 1 77  ? 9.922   25.820  -29.535 1.00 25.85 ? 77  ASN D C   1 
ATOM   6174 O O   . ASN D 1 77  ? 9.676   24.618  -29.749 1.00 25.55 ? 77  ASN D O   1 
ATOM   6175 C CB  . ASN D 1 77  ? 11.522  26.769  -27.808 1.00 27.84 ? 77  ASN D CB  1 
ATOM   6176 C CG  . ASN D 1 77  ? 12.517  25.651  -28.028 1.00 25.63 ? 77  ASN D CG  1 
ATOM   6177 O OD1 . ASN D 1 77  ? 12.532  25.054  -29.089 1.00 24.65 ? 77  ASN D OD1 1 
ATOM   6178 N ND2 . ASN D 1 77  ? 13.312  25.332  -27.023 1.00 27.35 ? 77  ASN D ND2 1 
ATOM   6179 N N   . PRO D 1 78  ? 9.993   26.704  -30.532 1.00 25.81 ? 78  PRO D N   1 
ATOM   6180 C CA  . PRO D 1 78  ? 9.795   26.268  -31.923 1.00 22.44 ? 78  PRO D CA  1 
ATOM   6181 C C   . PRO D 1 78  ? 11.046  25.742  -32.609 1.00 24.98 ? 78  PRO D C   1 
ATOM   6182 O O   . PRO D 1 78  ? 10.998  25.490  -33.820 1.00 22.61 ? 78  PRO D O   1 
ATOM   6183 C CB  . PRO D 1 78  ? 9.329   27.558  -32.618 1.00 25.66 ? 78  PRO D CB  1 
ATOM   6184 C CG  . PRO D 1 78  ? 10.046  28.639  -31.865 1.00 24.20 ? 78  PRO D CG  1 
ATOM   6185 C CD  . PRO D 1 78  ? 10.116  28.184  -30.433 1.00 22.96 ? 78  PRO D CD  1 
ATOM   6186 N N   . LEU D 1 79  ? 12.141  25.576  -31.870 1.00 23.87 ? 79  LEU D N   1 
ATOM   6187 C CA  . LEU D 1 79  ? 13.433  25.300  -32.488 1.00 25.23 ? 79  LEU D CA  1 
ATOM   6188 C C   . LEU D 1 79  ? 13.463  23.892  -33.084 1.00 24.10 ? 79  LEU D C   1 
ATOM   6189 O O   . LEU D 1 79  ? 12.989  22.927  -32.476 1.00 23.65 ? 79  LEU D O   1 
ATOM   6190 C CB  . LEU D 1 79  ? 14.553  25.462  -31.460 1.00 26.75 ? 79  LEU D CB  1 
ATOM   6191 C CG  . LEU D 1 79  ? 15.984  25.179  -31.965 1.00 29.24 ? 79  LEU D CG  1 
ATOM   6192 C CD1 . LEU D 1 79  ? 16.341  26.158  -33.065 1.00 25.36 ? 79  LEU D CD1 1 
ATOM   6193 C CD2 . LEU D 1 79  ? 16.998  25.278  -30.816 1.00 30.16 ? 79  LEU D CD2 1 
ATOM   6194 N N   . VAL D 1 80  ? 13.991  23.795  -34.302 1.00 23.95 ? 80  VAL D N   1 
ATOM   6195 C CA  . VAL D 1 80  ? 14.177  22.535  -35.011 1.00 26.97 ? 80  VAL D CA  1 
ATOM   6196 C C   . VAL D 1 80  ? 15.648  22.435  -35.372 1.00 27.04 ? 80  VAL D C   1 
ATOM   6197 O O   . VAL D 1 80  ? 16.190  23.356  -35.989 1.00 26.05 ? 80  VAL D O   1 
ATOM   6198 C CB  . VAL D 1 80  ? 13.301  22.477  -36.282 1.00 27.13 ? 80  VAL D CB  1 
ATOM   6199 C CG1 . VAL D 1 80  ? 13.681  21.259  -37.165 1.00 26.09 ? 80  VAL D CG1 1 
ATOM   6200 C CG2 . VAL D 1 80  ? 11.807  22.465  -35.932 1.00 23.48 ? 80  VAL D CG2 1 
ATOM   6201 N N   . MET D 1 81  ? 16.299  21.339  -34.983 1.00 25.03 ? 81  MET D N   1 
ATOM   6202 C CA  . MET D 1 81  ? 17.721  21.201  -35.308 1.00 26.04 ? 81  MET D CA  1 
ATOM   6203 C C   . MET D 1 81  ? 17.906  21.368  -36.809 1.00 25.98 ? 81  MET D C   1 
ATOM   6204 O O   . MET D 1 81  ? 17.178  20.779  -37.608 1.00 28.81 ? 81  MET D O   1 
ATOM   6205 C CB  . MET D 1 81  ? 18.277  19.832  -34.895 1.00 27.57 ? 81  MET D CB  1 
ATOM   6206 C CG  . MET D 1 81  ? 19.835  19.784  -34.899 1.00 28.83 ? 81  MET D CG  1 
ATOM   6207 S SD  . MET D 1 81  ? 20.621  21.367  -34.480 1.00 30.95 ? 81  MET D SD  1 
ATOM   6208 C CE  . MET D 1 81  ? 22.325  21.041  -34.965 1.00 30.92 ? 81  MET D CE  1 
ATOM   6209 N N   . ASP D 1 82  ? 18.891  22.165  -37.193 1.00 25.32 ? 82  ASP D N   1 
ATOM   6210 C CA  . ASP D 1 82  ? 19.193  22.436  -38.591 1.00 26.66 ? 82  ASP D CA  1 
ATOM   6211 C C   . ASP D 1 82  ? 20.707  22.396  -38.695 1.00 27.07 ? 82  ASP D C   1 
ATOM   6212 O O   . ASP D 1 82  ? 21.386  23.263  -38.150 1.00 26.52 ? 82  ASP D O   1 
ATOM   6213 C CB  . ASP D 1 82  ? 18.618  23.798  -39.014 1.00 28.22 ? 82  ASP D CB  1 
ATOM   6214 C CG  . ASP D 1 82  ? 18.853  24.134  -40.486 1.00 28.60 ? 82  ASP D CG  1 
ATOM   6215 O OD1 . ASP D 1 82  ? 18.979  23.217  -41.334 1.00 26.84 ? 82  ASP D OD1 1 
ATOM   6216 O OD2 . ASP D 1 82  ? 18.811  25.341  -40.811 1.00 27.19 ? 82  ASP D OD2 1 
ATOM   6217 N N   . TYR D 1 83  ? 21.234  21.419  -39.416 1.00 28.84 ? 83  TYR D N   1 
ATOM   6218 C CA  . TYR D 1 83  ? 22.679  21.276  -39.505 1.00 27.22 ? 83  TYR D CA  1 
ATOM   6219 C C   . TYR D 1 83  ? 23.190  22.180  -40.613 1.00 27.43 ? 83  TYR D C   1 
ATOM   6220 O O   . TYR D 1 83  ? 22.447  22.536  -41.525 1.00 29.76 ? 83  TYR D O   1 
ATOM   6221 C CB  . TYR D 1 83  ? 23.060  19.813  -39.787 1.00 27.70 ? 83  TYR D CB  1 
ATOM   6222 C CG  . TYR D 1 83  ? 22.582  18.824  -38.735 1.00 29.68 ? 83  TYR D CG  1 
ATOM   6223 C CD1 . TYR D 1 83  ? 23.360  18.535  -37.634 1.00 29.87 ? 83  TYR D CD1 1 
ATOM   6224 C CD2 . TYR D 1 83  ? 21.350  18.173  -38.855 1.00 27.84 ? 83  TYR D CD2 1 
ATOM   6225 C CE1 . TYR D 1 83  ? 22.924  17.623  -36.665 1.00 32.30 ? 83  TYR D CE1 1 
ATOM   6226 C CE2 . TYR D 1 83  ? 20.899  17.263  -37.887 1.00 27.63 ? 83  TYR D CE2 1 
ATOM   6227 C CZ  . TYR D 1 83  ? 21.701  16.991  -36.797 1.00 32.25 ? 83  TYR D CZ  1 
ATOM   6228 O OH  . TYR D 1 83  ? 21.306  16.077  -35.825 1.00 34.25 ? 83  TYR D OH  1 
ATOM   6229 N N   . GLN D 1 84  ? 24.468  22.558  -40.537 1.00 24.52 ? 84  GLN D N   1 
ATOM   6230 C CA  . GLN D 1 84  ? 25.035  23.358  -41.614 1.00 28.14 ? 84  GLN D CA  1 
ATOM   6231 C C   . GLN D 1 84  ? 25.164  22.530  -42.882 1.00 32.28 ? 84  GLN D C   1 
ATOM   6232 O O   . GLN D 1 84  ? 25.567  21.356  -42.851 1.00 32.14 ? 84  GLN D O   1 
ATOM   6233 C CB  . GLN D 1 84  ? 26.407  23.926  -41.235 1.00 27.71 ? 84  GLN D CB  1 
ATOM   6234 C CG  . GLN D 1 84  ? 27.444  22.915  -40.709 1.00 27.31 ? 84  GLN D CG  1 
ATOM   6235 C CD  . GLN D 1 84  ? 28.658  23.610  -40.114 1.00 30.49 ? 84  GLN D CD  1 
ATOM   6236 O OE1 . GLN D 1 84  ? 28.712  23.866  -38.902 1.00 30.92 ? 84  GLN D OE1 1 
ATOM   6237 N NE2 . GLN D 1 84  ? 29.646  23.914  -40.958 1.00 31.81 ? 84  GLN D NE2 1 
ATOM   6238 N N   . ASN D 1 85  ? 24.906  23.174  -44.015 1.00 29.62 ? 85  ASN D N   1 
ATOM   6239 C CA  . ASN D 1 85  ? 24.951  22.450  -45.273 1.00 32.61 ? 85  ASN D CA  1 
ATOM   6240 C C   . ASN D 1 85  ? 26.364  22.376  -45.856 1.00 33.12 ? 85  ASN D C   1 
ATOM   6241 O O   . ASN D 1 85  ? 26.596  21.607  -46.803 1.00 34.49 ? 85  ASN D O   1 
ATOM   6242 C CB  . ASN D 1 85  ? 23.985  23.083  -46.294 1.00 29.69 ? 85  ASN D CB  1 
ATOM   6243 C CG  . ASN D 1 85  ? 22.477  23.058  -45.836 1.00 37.55 ? 85  ASN D CG  1 
ATOM   6244 O OD1 . ASN D 1 85  ? 22.097  22.463  -44.808 1.00 33.44 ? 85  ASN D OD1 1 
ATOM   6245 N ND2 . ASN D 1 85  ? 21.613  23.654  -46.668 1.00 37.51 ? 85  ASN D ND2 1 
ATOM   6246 N N   . THR D 1 86  ? 27.314  23.157  -45.336 1.00 33.37 ? 86  THR D N   1 
ATOM   6247 C CA  . THR D 1 86  ? 28.696  23.096  -45.788 1.00 33.02 ? 86  THR D CA  1 
ATOM   6248 C C   . THR D 1 86  ? 29.621  23.157  -44.583 1.00 33.76 ? 86  THR D C   1 
ATOM   6249 O O   . THR D 1 86  ? 29.190  23.416  -43.462 1.00 30.58 ? 86  THR D O   1 
ATOM   6250 C CB  . THR D 1 86  ? 29.063  24.252  -46.722 1.00 37.21 ? 86  THR D CB  1 
ATOM   6251 O OG1 . THR D 1 86  ? 29.346  25.408  -45.931 1.00 32.16 ? 86  THR D OG1 1 
ATOM   6252 C CG2 . THR D 1 86  ? 27.927  24.575  -47.694 1.00 33.23 ? 86  THR D CG2 1 
ATOM   6253 N N   . ASN D 1 87  ? 30.922  22.973  -44.829 1.00 35.74 ? 87  ASN D N   1 
ATOM   6254 C CA  . ASN D 1 87  ? 31.886  23.079  -43.738 1.00 34.54 ? 87  ASN D CA  1 
ATOM   6255 C C   . ASN D 1 87  ? 32.257  24.519  -43.411 1.00 32.50 ? 87  ASN D C   1 
ATOM   6256 O O   . ASN D 1 87  ? 33.074  24.735  -42.511 1.00 31.35 ? 87  ASN D O   1 
ATOM   6257 C CB  . ASN D 1 87  ? 33.158  22.257  -44.025 1.00 36.26 ? 87  ASN D CB  1 
ATOM   6258 C CG  . ASN D 1 87  ? 33.765  22.558  -45.371 1.00 37.29 ? 87  ASN D CG  1 
ATOM   6259 O OD1 . ASN D 1 87  ? 33.646  23.665  -45.893 1.00 39.17 ? 87  ASN D OD1 1 
ATOM   6260 N ND2 . ASN D 1 87  ? 34.440  21.573  -45.937 1.00 43.96 ? 87  ASN D ND2 1 
ATOM   6261 N N   . TYR D 1 88  ? 31.660  25.516  -44.080 1.00 28.77 ? 88  TYR D N   1 
ATOM   6262 C CA  . TYR D 1 88  ? 32.016  26.902  -43.799 1.00 29.44 ? 88  TYR D CA  1 
ATOM   6263 C C   . TYR D 1 88  ? 30.812  27.790  -43.473 1.00 29.31 ? 88  TYR D C   1 
ATOM   6264 O O   . TYR D 1 88  ? 30.977  29.010  -43.408 1.00 26.45 ? 88  TYR D O   1 
ATOM   6265 C CB  . TYR D 1 88  ? 32.832  27.498  -44.966 1.00 31.68 ? 88  TYR D CB  1 
ATOM   6266 C CG  . TYR D 1 88  ? 32.066  27.522  -46.261 1.00 31.03 ? 88  TYR D CG  1 
ATOM   6267 C CD1 . TYR D 1 88  ? 32.119  26.435  -47.136 1.00 34.68 ? 88  TYR D CD1 1 
ATOM   6268 C CD2 . TYR D 1 88  ? 31.268  28.606  -46.598 1.00 29.70 ? 88  TYR D CD2 1 
ATOM   6269 C CE1 . TYR D 1 88  ? 31.391  26.429  -48.311 1.00 35.62 ? 88  TYR D CE1 1 
ATOM   6270 C CE2 . TYR D 1 88  ? 30.552  28.621  -47.770 1.00 31.01 ? 88  TYR D CE2 1 
ATOM   6271 C CZ  . TYR D 1 88  ? 30.611  27.529  -48.623 1.00 37.90 ? 88  TYR D CZ  1 
ATOM   6272 O OH  . TYR D 1 88  ? 29.883  27.536  -49.797 1.00 39.40 ? 88  TYR D OH  1 
ATOM   6273 N N   . THR D 1 89  ? 29.621  27.224  -43.186 1.00 25.72 ? 89  THR D N   1 
ATOM   6274 C CA  . THR D 1 89  ? 28.416  28.028  -42.957 1.00 25.31 ? 89  THR D CA  1 
ATOM   6275 C C   . THR D 1 89  ? 27.882  27.906  -41.531 1.00 26.26 ? 89  THR D C   1 
ATOM   6276 O O   . THR D 1 89  ? 26.680  28.097  -41.288 1.00 25.23 ? 89  THR D O   1 
ATOM   6277 C CB  . THR D 1 89  ? 27.331  27.654  -43.964 1.00 28.24 ? 89  THR D CB  1 
ATOM   6278 O OG1 . THR D 1 89  ? 27.293  26.214  -44.110 1.00 26.44 ? 89  THR D OG1 1 
ATOM   6279 C CG2 . THR D 1 89  ? 27.626  28.299  -45.314 1.00 28.12 ? 89  THR D CG2 1 
ATOM   6280 N N   . ALA D 1 90  ? 28.764  27.632  -40.565 1.00 25.41 ? 90  ALA D N   1 
ATOM   6281 C CA  . ALA D 1 90  ? 28.319  27.528  -39.177 1.00 29.37 ? 90  ALA D CA  1 
ATOM   6282 C C   . ALA D 1 90  ? 27.625  28.803  -38.716 1.00 29.20 ? 90  ALA D C   1 
ATOM   6283 O O   . ALA D 1 90  ? 26.581  28.746  -38.039 1.00 25.35 ? 90  ALA D O   1 
ATOM   6284 C CB  . ALA D 1 90  ? 29.495  27.204  -38.261 1.00 25.86 ? 90  ALA D CB  1 
ATOM   6285 N N   . CYS D 1 91  ? 28.166  29.961  -39.110 1.00 24.65 ? 91  CYS D N   1 
ATOM   6286 C CA  . CYS D 1 91  ? 27.618  31.233  -38.639 1.00 28.41 ? 91  CYS D CA  1 
ATOM   6287 C C   . CYS D 1 91  ? 26.249  31.532  -39.229 1.00 25.87 ? 91  CYS D C   1 
ATOM   6288 O O   . CYS D 1 91  ? 25.313  31.809  -38.457 1.00 28.38 ? 91  CYS D O   1 
ATOM   6289 C CB  . CYS D 1 91  ? 28.612  32.369  -38.923 1.00 26.47 ? 91  CYS D CB  1 
ATOM   6290 S SG  . CYS D 1 91  ? 28.124  33.908  -38.106 1.00 30.71 ? 91  CYS D SG  1 
ATOM   6291 N N   . PRO D 1 92  ? 26.047  31.523  -40.546 1.00 27.46 ? 92  PRO D N   1 
ATOM   6292 C CA  . PRO D 1 92  ? 24.677  31.713  -41.037 1.00 24.64 ? 92  PRO D CA  1 
ATOM   6293 C C   . PRO D 1 92  ? 23.718  30.631  -40.559 1.00 26.51 ? 92  PRO D C   1 
ATOM   6294 O O   . PRO D 1 92  ? 22.531  30.927  -40.394 1.00 24.97 ? 92  PRO D O   1 
ATOM   6295 C CB  . PRO D 1 92  ? 24.847  31.718  -42.564 1.00 26.31 ? 92  PRO D CB  1 
ATOM   6296 C CG  . PRO D 1 92  ? 26.206  31.099  -42.833 1.00 23.93 ? 92  PRO D CG  1 
ATOM   6297 C CD  . PRO D 1 92  ? 27.030  31.481  -41.651 1.00 24.43 ? 92  PRO D CD  1 
ATOM   6298 N N   . THR D 1 93  ? 24.182  29.394  -40.323 1.00 24.27 ? 93  THR D N   1 
ATOM   6299 C CA  . THR D 1 93  ? 23.287  28.382  -39.760 1.00 25.73 ? 93  THR D CA  1 
ATOM   6300 C C   . THR D 1 93  ? 22.884  28.726  -38.328 1.00 25.00 ? 93  THR D C   1 
ATOM   6301 O O   . THR D 1 93  ? 21.722  28.510  -37.937 1.00 22.68 ? 93  THR D O   1 
ATOM   6302 C CB  . THR D 1 93  ? 23.914  26.979  -39.824 1.00 25.94 ? 93  THR D CB  1 
ATOM   6303 O OG1 . THR D 1 93  ? 24.412  26.726  -41.138 1.00 22.79 ? 93  THR D OG1 1 
ATOM   6304 C CG2 . THR D 1 93  ? 22.853  25.919  -39.484 1.00 23.30 ? 93  THR D CG2 1 
ATOM   6305 N N   . SER D 1 94  ? 23.821  29.252  -37.529 1.00 23.48 ? 94  SER D N   1 
ATOM   6306 C CA  . SER D 1 94  ? 23.482  29.657  -36.163 1.00 22.74 ? 94  SER D CA  1 
ATOM   6307 C C   . SER D 1 94  ? 22.488  30.822  -36.157 1.00 23.93 ? 94  SER D C   1 
ATOM   6308 O O   . SER D 1 94  ? 21.591  30.884  -35.300 1.00 23.93 ? 94  SER D O   1 
ATOM   6309 C CB  . SER D 1 94  ? 24.749  30.029  -35.394 1.00 24.51 ? 94  SER D CB  1 
ATOM   6310 O OG  . SER D 1 94  ? 25.673  28.945  -35.363 1.00 26.63 ? 94  SER D OG  1 
ATOM   6311 N N   . LEU D 1 95  ? 22.630  31.748  -37.104 1.00 23.18 ? 95  LEU D N   1 
ATOM   6312 C CA  . LEU D 1 95  ? 21.696  32.864  -37.211 1.00 24.86 ? 95  LEU D CA  1 
ATOM   6313 C C   . LEU D 1 95  ? 20.318  32.377  -37.650 1.00 25.29 ? 95  LEU D C   1 
ATOM   6314 O O   . LEU D 1 95  ? 19.288  32.855  -37.152 1.00 25.17 ? 95  LEU D O   1 
ATOM   6315 C CB  . LEU D 1 95  ? 22.260  33.893  -38.192 1.00 25.70 ? 95  LEU D CB  1 
ATOM   6316 C CG  . LEU D 1 95  ? 21.435  35.171  -38.318 1.00 27.26 ? 95  LEU D CG  1 
ATOM   6317 C CD1 . LEU D 1 95  ? 21.237  35.805  -36.936 1.00 23.40 ? 95  LEU D CD1 1 
ATOM   6318 C CD2 . LEU D 1 95  ? 22.116  36.104  -39.286 1.00 27.50 ? 95  LEU D CD2 1 
ATOM   6319 N N   . SER D 1 96  ? 20.284  31.398  -38.560 1.00 24.23 ? 96  SER D N   1 
ATOM   6320 C CA  . SER D 1 96  ? 19.027  30.792  -38.981 1.00 23.97 ? 96  SER D CA  1 
ATOM   6321 C C   . SER D 1 96  ? 18.328  30.075  -37.819 1.00 25.41 ? 96  SER D C   1 
ATOM   6322 O O   . SER D 1 96  ? 17.110  30.215  -37.633 1.00 23.72 ? 96  SER D O   1 
ATOM   6323 C CB  . SER D 1 96  ? 19.304  29.819  -40.131 1.00 25.55 ? 96  SER D CB  1 
ATOM   6324 O OG  . SER D 1 96  ? 18.121  29.166  -40.564 1.00 25.78 ? 96  SER D OG  1 
ATOM   6325 N N   . LEU D 1 97  ? 19.081  29.330  -37.002 1.00 23.95 ? 97  LEU D N   1 
ATOM   6326 C CA  . LEU D 1 97  ? 18.501  28.763  -35.786 1.00 23.14 ? 97  LEU D CA  1 
ATOM   6327 C C   . LEU D 1 97  ? 17.955  29.864  -34.863 1.00 23.30 ? 97  LEU D C   1 
ATOM   6328 O O   . LEU D 1 97  ? 16.853  29.736  -34.318 1.00 24.33 ? 97  LEU D O   1 
ATOM   6329 C CB  . LEU D 1 97  ? 19.553  27.940  -35.067 1.00 21.10 ? 97  LEU D CB  1 
ATOM   6330 C CG  . LEU D 1 97  ? 20.064  26.683  -35.807 1.00 20.17 ? 97  LEU D CG  1 
ATOM   6331 C CD1 . LEU D 1 97  ? 21.334  26.220  -35.112 1.00 23.82 ? 97  LEU D CD1 1 
ATOM   6332 C CD2 . LEU D 1 97  ? 19.072  25.530  -35.838 1.00 23.80 ? 97  LEU D CD2 1 
ATOM   6333 N N   . ALA D 1 98  ? 18.726  30.943  -34.652 1.00 22.44 ? 98  ALA D N   1 
ATOM   6334 C CA  . ALA D 1 98  ? 18.215  32.068  -33.873 1.00 23.81 ? 98  ALA D CA  1 
ATOM   6335 C C   . ALA D 1 98  ? 16.919  32.590  -34.473 1.00 22.63 ? 98  ALA D C   1 
ATOM   6336 O O   . ALA D 1 98  ? 15.978  32.937  -33.743 1.00 26.10 ? 98  ALA D O   1 
ATOM   6337 C CB  . ALA D 1 98  ? 19.254  33.204  -33.811 1.00 22.98 ? 98  ALA D CB  1 
ATOM   6338 N N   . SER D 1 99  ? 16.845  32.636  -35.806 1.00 20.80 ? 99  SER D N   1 
ATOM   6339 C CA  . SER D 1 99  ? 15.667  33.166  -36.472 1.00 23.93 ? 99  SER D CA  1 
ATOM   6340 C C   . SER D 1 99  ? 14.422  32.323  -36.181 1.00 24.52 ? 99  SER D C   1 
ATOM   6341 O O   . SER D 1 99  ? 13.310  32.864  -36.115 1.00 20.93 ? 99  SER D O   1 
ATOM   6342 C CB  . SER D 1 99  ? 15.942  33.278  -37.975 1.00 23.65 ? 99  SER D CB  1 
ATOM   6343 O OG  . SER D 1 99  ? 15.696  32.042  -38.633 1.00 26.31 ? 99  SER D OG  1 
ATOM   6344 N N   . GLN D 1 100 ? 14.585  31.016  -35.945 1.00 22.61 ? 100 GLN D N   1 
ATOM   6345 C CA  . GLN D 1 100 ? 13.446  30.210  -35.496 1.00 23.19 ? 100 GLN D CA  1 
ATOM   6346 C C   . GLN D 1 100 ? 12.958  30.674  -34.131 1.00 23.11 ? 100 GLN D C   1 
ATOM   6347 O O   . GLN D 1 100 ? 11.754  30.862  -33.917 1.00 23.87 ? 100 GLN D O   1 
ATOM   6348 C CB  . GLN D 1 100 ? 13.836  28.734  -35.397 1.00 24.41 ? 100 GLN D CB  1 
ATOM   6349 C CG  . GLN D 1 100 ? 14.288  28.085  -36.669 1.00 20.36 ? 100 GLN D CG  1 
ATOM   6350 C CD  . GLN D 1 100 ? 14.484  26.594  -36.483 1.00 23.93 ? 100 GLN D CD  1 
ATOM   6351 O OE1 . GLN D 1 100 ? 13.618  25.907  -35.919 1.00 23.86 ? 100 GLN D OE1 1 
ATOM   6352 N NE2 . GLN D 1 100 ? 15.628  26.079  -36.950 1.00 21.64 ? 100 GLN D NE2 1 
ATOM   6353 N N   . MET D 1 101 ? 13.890  30.838  -33.182 1.00 24.44 ? 101 MET D N   1 
ATOM   6354 C CA  . MET D 1 101 ? 13.545  31.243  -31.818 1.00 25.14 ? 101 MET D CA  1 
ATOM   6355 C C   . MET D 1 101 ? 12.836  32.592  -31.782 1.00 25.76 ? 101 MET D C   1 
ATOM   6356 O O   . MET D 1 101 ? 12.000  32.833  -30.903 1.00 23.29 ? 101 MET D O   1 
ATOM   6357 C CB  . MET D 1 101 ? 14.814  31.311  -30.969 1.00 27.56 ? 101 MET D CB  1 
ATOM   6358 C CG  . MET D 1 101 ? 15.593  29.996  -30.794 1.00 28.63 ? 101 MET D CG  1 
ATOM   6359 S SD  . MET D 1 101 ? 14.548  28.726  -30.128 1.00 45.33 ? 101 MET D SD  1 
ATOM   6360 C CE  . MET D 1 101 ? 15.144  28.643  -28.447 1.00 35.59 ? 101 MET D CE  1 
ATOM   6361 N N   . LEU D 1 102 ? 13.126  33.466  -32.738 1.00 24.41 ? 102 LEU D N   1 
ATOM   6362 C CA  . LEU D 1 102 ? 12.532  34.796  -32.803 1.00 25.50 ? 102 LEU D CA  1 
ATOM   6363 C C   . LEU D 1 102 ? 11.274  34.880  -33.673 1.00 24.40 ? 102 LEU D C   1 
ATOM   6364 O O   . LEU D 1 102 ? 10.762  35.987  -33.880 1.00 25.08 ? 102 LEU D O   1 
ATOM   6365 C CB  . LEU D 1 102 ? 13.610  35.789  -33.307 1.00 22.53 ? 102 LEU D CB  1 
ATOM   6366 C CG  . LEU D 1 102 ? 14.777  35.879  -32.321 1.00 21.82 ? 102 LEU D CG  1 
ATOM   6367 C CD1 . LEU D 1 102 ? 15.920  36.710  -32.898 1.00 20.99 ? 102 LEU D CD1 1 
ATOM   6368 C CD2 . LEU D 1 102 ? 14.311  36.509  -31.015 1.00 21.61 ? 102 LEU D CD2 1 
ATOM   6369 N N   . TYR D 1 103 ? 10.785  33.761  -34.222 1.00 23.45 ? 103 TYR D N   1 
ATOM   6370 C CA  . TYR D 1 103 ? 9.596   33.755  -35.078 1.00 21.80 ? 103 TYR D CA  1 
ATOM   6371 C C   . TYR D 1 103 ? 9.796   34.669  -36.281 1.00 23.60 ? 103 TYR D C   1 
ATOM   6372 O O   . TYR D 1 103 ? 8.908   35.445  -36.646 1.00 23.53 ? 103 TYR D O   1 
ATOM   6373 C CB  . TYR D 1 103 ? 8.312   34.138  -34.301 1.00 23.67 ? 103 TYR D CB  1 
ATOM   6374 C CG  . TYR D 1 103 ? 7.961   33.108  -33.282 1.00 22.35 ? 103 TYR D CG  1 
ATOM   6375 C CD1 . TYR D 1 103 ? 8.623   33.078  -32.059 1.00 23.38 ? 103 TYR D CD1 1 
ATOM   6376 C CD2 . TYR D 1 103 ? 7.000   32.121  -33.545 1.00 21.56 ? 103 TYR D CD2 1 
ATOM   6377 C CE1 . TYR D 1 103 ? 8.333   32.092  -31.110 1.00 23.46 ? 103 TYR D CE1 1 
ATOM   6378 C CE2 . TYR D 1 103 ? 6.696   31.123  -32.587 1.00 21.56 ? 103 TYR D CE2 1 
ATOM   6379 C CZ  . TYR D 1 103 ? 7.374   31.127  -31.386 1.00 22.82 ? 103 TYR D CZ  1 
ATOM   6380 O OH  . TYR D 1 103 ? 7.125   30.164  -30.450 1.00 24.21 ? 103 TYR D OH  1 
ATOM   6381 N N   . HIS D 1 104 ? 10.986  34.611  -36.882 1.00 23.87 ? 104 HIS D N   1 
ATOM   6382 C CA  . HIS D 1 104 ? 11.261  35.353  -38.113 1.00 22.95 ? 104 HIS D CA  1 
ATOM   6383 C C   . HIS D 1 104 ? 12.224  34.529  -38.963 1.00 24.57 ? 104 HIS D C   1 
ATOM   6384 O O   . HIS D 1 104 ? 13.352  34.945  -39.251 1.00 25.15 ? 104 HIS D O   1 
ATOM   6385 C CB  . HIS D 1 104 ? 11.817  36.740  -37.796 1.00 23.61 ? 104 HIS D CB  1 
ATOM   6386 C CG  . HIS D 1 104 ? 11.744  37.706  -38.939 1.00 26.55 ? 104 HIS D CG  1 
ATOM   6387 N ND1 . HIS D 1 104 ? 10.546  38.168  -39.451 1.00 30.51 ? 104 HIS D ND1 1 
ATOM   6388 C CD2 . HIS D 1 104 ? 12.718  38.340  -39.636 1.00 29.04 ? 104 HIS D CD2 1 
ATOM   6389 C CE1 . HIS D 1 104 ? 10.785  39.031  -40.422 1.00 31.61 ? 104 HIS D CE1 1 
ATOM   6390 N NE2 . HIS D 1 104 ? 12.095  39.147  -40.561 1.00 31.55 ? 104 HIS D NE2 1 
ATOM   6391 N N   . TYR D 1 105 ? 11.773  33.335  -39.356 1.00 25.35 ? 105 TYR D N   1 
ATOM   6392 C CA  . TYR D 1 105 ? 12.667  32.336  -39.928 1.00 23.86 ? 105 TYR D CA  1 
ATOM   6393 C C   . TYR D 1 105 ? 13.294  32.833  -41.221 1.00 24.95 ? 105 TYR D C   1 
ATOM   6394 O O   . TYR D 1 105 ? 12.608  33.310  -42.133 1.00 26.40 ? 105 TYR D O   1 
ATOM   6395 C CB  . TYR D 1 105 ? 11.909  31.031  -40.177 1.00 25.67 ? 105 TYR D CB  1 
ATOM   6396 C CG  . TYR D 1 105 ? 12.744  30.010  -40.936 1.00 24.14 ? 105 TYR D CG  1 
ATOM   6397 C CD1 . TYR D 1 105 ? 13.878  29.443  -40.371 1.00 23.67 ? 105 TYR D CD1 1 
ATOM   6398 C CD2 . TYR D 1 105 ? 12.412  29.664  -42.232 1.00 25.21 ? 105 TYR D CD2 1 
ATOM   6399 C CE1 . TYR D 1 105 ? 14.656  28.513  -41.098 1.00 24.47 ? 105 TYR D CE1 1 
ATOM   6400 C CE2 . TYR D 1 105 ? 13.170  28.753  -42.953 1.00 27.90 ? 105 TYR D CE2 1 
ATOM   6401 C CZ  . TYR D 1 105 ? 14.284  28.196  -42.390 1.00 22.47 ? 105 TYR D CZ  1 
ATOM   6402 O OH  . TYR D 1 105 ? 14.987  27.302  -43.130 1.00 23.93 ? 105 TYR D OH  1 
ATOM   6403 N N   . LYS D 1 106 ? 14.610  32.731  -41.284 1.00 25.25 ? 106 LYS D N   1 
ATOM   6404 C CA  . LYS D 1 106 ? 15.387  32.957  -42.492 1.00 26.20 ? 106 LYS D CA  1 
ATOM   6405 C C   . LYS D 1 106 ? 16.279  31.737  -42.664 1.00 23.15 ? 106 LYS D C   1 
ATOM   6406 O O   . LYS D 1 106 ? 16.976  31.344  -41.722 1.00 23.28 ? 106 LYS D O   1 
ATOM   6407 C CB  . LYS D 1 106 ? 16.253  34.234  -42.378 1.00 24.75 ? 106 LYS D CB  1 
ATOM   6408 C CG  . LYS D 1 106 ? 15.466  35.512  -42.103 1.00 21.34 ? 106 LYS D CG  1 
ATOM   6409 C CD  . LYS D 1 106 ? 14.690  35.925  -43.315 1.00 24.50 ? 106 LYS D CD  1 
ATOM   6410 C CE  . LYS D 1 106 ? 13.899  37.233  -42.998 1.00 29.44 ? 106 LYS D CE  1 
ATOM   6411 N NZ  . LYS D 1 106 ? 13.204  37.744  -44.216 1.00 33.54 ? 106 LYS D NZ  1 
ATOM   6412 N N   . SER D 1 107 ? 16.266  31.148  -43.852 1.00 22.96 ? 107 SER D N   1 
ATOM   6413 C CA  . SER D 1 107 ? 17.008  29.909  -44.073 1.00 27.19 ? 107 SER D CA  1 
ATOM   6414 C C   . SER D 1 107 ? 18.515  30.146  -44.006 1.00 24.84 ? 107 SER D C   1 
ATOM   6415 O O   . SER D 1 107 ? 18.999  31.256  -44.186 1.00 23.41 ? 107 SER D O   1 
ATOM   6416 C CB  . SER D 1 107 ? 16.652  29.314  -45.430 1.00 27.29 ? 107 SER D CB  1 
ATOM   6417 O OG  . SER D 1 107 ? 17.298  30.070  -46.427 1.00 28.49 ? 107 SER D OG  1 
ATOM   6418 N N   . GLU D 1 108 ? 19.259  29.064  -43.776 1.00 24.40 ? 108 GLU D N   1 
ATOM   6419 C CA  . GLU D 1 108 ? 20.715  29.161  -43.779 1.00 23.25 ? 108 GLU D CA  1 
ATOM   6420 C C   . GLU D 1 108 ? 21.195  29.840  -45.052 1.00 27.68 ? 108 GLU D C   1 
ATOM   6421 O O   . GLU D 1 108 ? 22.077  30.705  -45.018 1.00 25.67 ? 108 GLU D O   1 
ATOM   6422 C CB  . GLU D 1 108 ? 21.337  27.764  -43.673 1.00 25.74 ? 108 GLU D CB  1 
ATOM   6423 C CG  . GLU D 1 108 ? 22.824  27.745  -44.035 1.00 27.25 ? 108 GLU D CG  1 
ATOM   6424 C CD  . GLU D 1 108 ? 23.428  26.365  -44.032 1.00 28.66 ? 108 GLU D CD  1 
ATOM   6425 O OE1 . GLU D 1 108 ? 22.868  25.463  -43.387 1.00 31.96 ? 108 GLU D OE1 1 
ATOM   6426 O OE2 . GLU D 1 108 ? 24.468  26.189  -44.682 1.00 30.13 ? 108 GLU D OE2 1 
ATOM   6427 N N   . SER D 1 109 ? 20.601  29.479  -46.189 1.00 26.66 ? 109 SER D N   1 
ATOM   6428 C CA  . SER D 1 109 ? 21.024  30.057  -47.457 1.00 30.32 ? 109 SER D CA  1 
ATOM   6429 C C   . SER D 1 109 ? 20.799  31.565  -47.488 1.00 30.15 ? 109 SER D C   1 
ATOM   6430 O O   . SER D 1 109 ? 21.680  32.328  -47.923 1.00 25.69 ? 109 SER D O   1 
ATOM   6431 C CB  . SER D 1 109 ? 20.274  29.390  -48.602 1.00 32.26 ? 109 SER D CB  1 
ATOM   6432 O OG  . SER D 1 109 ? 20.729  29.925  -49.831 1.00 40.30 ? 109 SER D OG  1 
ATOM   6433 N N   . GLU D 1 110 ? 19.606  32.011  -47.071 1.00 25.81 ? 110 GLU D N   1 
ATOM   6434 C CA  . GLU D 1 110 ? 19.346  33.444  -46.999 1.00 26.90 ? 110 GLU D CA  1 
ATOM   6435 C C   . GLU D 1 110 ? 20.326  34.132  -46.067 1.00 26.81 ? 110 GLU D C   1 
ATOM   6436 O O   . GLU D 1 110 ? 20.812  35.230  -46.359 1.00 26.30 ? 110 GLU D O   1 
ATOM   6437 C CB  . GLU D 1 110 ? 17.925  33.741  -46.519 1.00 26.20 ? 110 GLU D CB  1 
ATOM   6438 C CG  . GLU D 1 110 ? 16.795  33.235  -47.377 1.00 31.08 ? 110 GLU D CG  1 
ATOM   6439 C CD  . GLU D 1 110 ? 15.427  33.452  -46.699 1.00 36.61 ? 110 GLU D CD  1 
ATOM   6440 O OE1 . GLU D 1 110 ? 14.829  34.506  -47.025 1.00 37.15 ? 110 GLU D OE1 1 
ATOM   6441 O OE2 . GLU D 1 110 ? 14.961  32.597  -45.871 1.00 33.21 ? 110 GLU D OE2 1 
ATOM   6442 N N   . CYS D 1 111 ? 20.593  33.528  -44.913 1.00 25.31 ? 111 CYS D N   1 
ATOM   6443 C CA  . CYS D 1 111 ? 21.504  34.175  -43.978 1.00 25.75 ? 111 CYS D CA  1 
ATOM   6444 C C   . CYS D 1 111 ? 22.917  34.247  -44.553 1.00 27.77 ? 111 CYS D C   1 
ATOM   6445 O O   . CYS D 1 111 ? 23.602  35.264  -44.390 1.00 25.77 ? 111 CYS D O   1 
ATOM   6446 C CB  . CYS D 1 111 ? 21.490  33.433  -42.642 1.00 24.49 ? 111 CYS D CB  1 
ATOM   6447 S SG  . CYS D 1 111 ? 19.893  33.562  -41.728 1.00 24.55 ? 111 CYS D SG  1 
ATOM   6448 N N   . ALA D 1 112 ? 23.380  33.172  -45.210 1.00 27.89 ? 112 ALA D N   1 
ATOM   6449 C CA  . ALA D 1 112 ? 24.737  33.187  -45.779 1.00 25.37 ? 112 ALA D CA  1 
ATOM   6450 C C   . ALA D 1 112 ? 24.877  34.278  -46.832 1.00 26.78 ? 112 ALA D C   1 
ATOM   6451 O O   . ALA D 1 112 ? 25.883  35.003  -46.870 1.00 28.75 ? 112 ALA D O   1 
ATOM   6452 C CB  . ALA D 1 112 ? 25.074  31.826  -46.377 1.00 26.13 ? 112 ALA D CB  1 
ATOM   6453 N N   . LYS D 1 113 ? 23.880  34.412  -47.693 1.00 27.32 ? 113 LYS D N   1 
ATOM   6454 C CA  . LYS D 1 113 ? 23.920  35.466  -48.696 1.00 30.96 ? 113 LYS D CA  1 
ATOM   6455 C C   . LYS D 1 113 ? 23.950  36.842  -48.034 1.00 29.90 ? 113 LYS D C   1 
ATOM   6456 O O   . LYS D 1 113 ? 24.750  37.702  -48.407 1.00 29.26 ? 113 LYS D O   1 
ATOM   6457 C CB  . LYS D 1 113 ? 22.717  35.324  -49.635 1.00 34.39 ? 113 LYS D CB  1 
ATOM   6458 C CG  . LYS D 1 113 ? 22.199  36.647  -50.194 1.00 38.71 ? 113 LYS D CG  1 
ATOM   6459 C CD  . LYS D 1 113 ? 20.711  36.592  -50.557 1.00 41.21 ? 113 LYS D CD  1 
ATOM   6460 C CE  . LYS D 1 113 ? 19.790  36.151  -49.386 1.00 39.51 ? 113 LYS D CE  1 
ATOM   6461 N NZ  . LYS D 1 113 ? 19.921  36.917  -48.094 1.00 36.43 ? 113 LYS D NZ  1 
ATOM   6462 N N   . ALA D 1 114 ? 23.122  37.059  -47.012 1.00 30.93 ? 114 ALA D N   1 
ATOM   6463 C CA  . ALA D 1 114 ? 23.073  38.383  -46.397 1.00 28.47 ? 114 ALA D CA  1 
ATOM   6464 C C   . ALA D 1 114 ? 24.374  38.714  -45.675 1.00 30.44 ? 114 ALA D C   1 
ATOM   6465 O O   . ALA D 1 114 ? 24.861  39.852  -45.751 1.00 32.01 ? 114 ALA D O   1 
ATOM   6466 C CB  . ALA D 1 114 ? 21.893  38.466  -45.432 1.00 28.50 ? 114 ALA D CB  1 
ATOM   6467 N N   . LEU D 1 115 ? 24.950  37.741  -44.959 1.00 27.20 ? 115 LEU D N   1 
ATOM   6468 C CA  . LEU D 1 115 ? 26.179  37.983  -44.221 1.00 25.69 ? 115 LEU D CA  1 
ATOM   6469 C C   . LEU D 1 115 ? 27.407  38.045  -45.125 1.00 30.04 ? 115 LEU D C   1 
ATOM   6470 O O   . LEU D 1 115 ? 28.427  38.596  -44.712 1.00 30.12 ? 115 LEU D O   1 
ATOM   6471 C CB  . LEU D 1 115 ? 26.385  36.896  -43.164 1.00 27.48 ? 115 LEU D CB  1 
ATOM   6472 C CG  . LEU D 1 115 ? 25.317  36.741  -42.047 1.00 29.38 ? 115 LEU D CG  1 
ATOM   6473 C CD1 . LEU D 1 115 ? 25.791  35.846  -40.874 1.00 26.05 ? 115 LEU D CD1 1 
ATOM   6474 C CD2 . LEU D 1 115 ? 24.800  38.062  -41.547 1.00 23.27 ? 115 LEU D CD2 1 
ATOM   6475 N N   . GLY D 1 116 ? 27.335  37.515  -46.344 1.00 28.88 ? 116 GLY D N   1 
ATOM   6476 C CA  . GLY D 1 116 ? 28.525  37.429  -47.166 1.00 27.48 ? 116 GLY D CA  1 
ATOM   6477 C C   . GLY D 1 116 ? 29.453  36.289  -46.807 1.00 31.37 ? 116 GLY D C   1 
ATOM   6478 O O   . GLY D 1 116 ? 30.663  36.372  -47.070 1.00 33.01 ? 116 GLY D O   1 
ATOM   6479 N N   . THR D 1 117 ? 28.923  35.234  -46.192 1.00 30.29 ? 117 THR D N   1 
ATOM   6480 C CA  . THR D 1 117 ? 29.703  34.048  -45.863 1.00 31.08 ? 117 THR D CA  1 
ATOM   6481 C C   . THR D 1 117 ? 30.379  33.520  -47.111 1.00 31.57 ? 117 THR D C   1 
ATOM   6482 O O   . THR D 1 117 ? 29.779  33.493  -48.184 1.00 35.29 ? 117 THR D O   1 
ATOM   6483 C CB  . THR D 1 117 ? 28.789  32.956  -45.281 1.00 29.13 ? 117 THR D CB  1 
ATOM   6484 O OG1 . THR D 1 117 ? 28.126  33.470  -44.125 1.00 25.53 ? 117 THR D OG1 1 
ATOM   6485 C CG2 . THR D 1 117 ? 29.586  31.709  -44.911 1.00 26.36 ? 117 THR D CG2 1 
ATOM   6486 N N   . SER D 1 118 ? 31.637  33.118  -46.976 1.00 35.40 ? 118 SER D N   1 
ATOM   6487 C CA  . SER D 1 118 ? 32.404  32.673  -48.131 1.00 35.27 ? 118 SER D CA  1 
ATOM   6488 C C   . SER D 1 118 ? 33.141  31.372  -47.853 1.00 35.79 ? 118 SER D C   1 
ATOM   6489 O O   . SER D 1 118 ? 33.548  31.085  -46.722 1.00 32.09 ? 118 SER D O   1 
ATOM   6490 C CB  . SER D 1 118 ? 33.406  33.757  -48.560 1.00 34.72 ? 118 SER D CB  1 
ATOM   6491 O OG  . SER D 1 118 ? 34.554  33.702  -47.740 1.00 38.10 ? 118 SER D OG  1 
ATOM   6492 N N   . LYS D 1 119 ? 33.438  30.659  -48.943 1.00 36.29 ? 119 LYS D N   1 
ATOM   6493 C CA  . LYS D 1 119 ? 34.093  29.363  -48.818 1.00 40.89 ? 119 LYS D CA  1 
ATOM   6494 C C   . LYS D 1 119 ? 35.497  29.521  -48.274 1.00 39.04 ? 119 LYS D C   1 
ATOM   6495 O O   . LYS D 1 119 ? 35.929  28.735  -47.425 1.00 37.95 ? 119 LYS D O   1 
ATOM   6496 C CB  . LYS D 1 119 ? 34.174  28.667  -50.183 1.00 42.20 ? 119 LYS D CB  1 
ATOM   6497 C CG  . LYS D 1 119 ? 34.642  27.198  -50.139 1.00 46.38 ? 119 LYS D CG  1 
ATOM   6498 C CD  . LYS D 1 119 ? 34.586  26.534  -51.532 1.00 47.26 ? 119 LYS D CD  1 
ATOM   6499 C CE  . LYS D 1 119 ? 35.600  25.375  -51.640 1.00 51.92 ? 119 LYS D CE  1 
ATOM   6500 N NZ  . LYS D 1 119 ? 36.532  25.481  -52.831 1.00 49.19 ? 119 LYS D NZ  1 
ATOM   6501 N N   . GLY D 1 120 ? 36.182  30.595  -48.660 1.00 38.66 ? 120 GLY D N   1 
ATOM   6502 C CA  . GLY D 1 120 ? 37.560  30.746  -48.225 1.00 40.85 ? 120 GLY D CA  1 
ATOM   6503 C C   . GLY D 1 120 ? 37.697  31.100  -46.755 1.00 44.63 ? 120 GLY D C   1 
ATOM   6504 O O   . GLY D 1 120 ? 38.519  30.517  -46.049 1.00 44.87 ? 120 GLY D O   1 
ATOM   6505 N N   . SER D 1 121 ? 36.884  32.031  -46.262 1.00 40.45 ? 121 SER D N   1 
ATOM   6506 C CA  . SER D 1 121 ? 37.096  32.548  -44.919 1.00 40.75 ? 121 SER D CA  1 
ATOM   6507 C C   . SER D 1 121 ? 35.955  32.275  -43.940 1.00 42.58 ? 121 SER D C   1 
ATOM   6508 O O   . SER D 1 121 ? 36.082  32.629  -42.758 1.00 41.47 ? 121 SER D O   1 
ATOM   6509 C CB  . SER D 1 121 ? 37.359  34.054  -44.988 1.00 41.03 ? 121 SER D CB  1 
ATOM   6510 O OG  . SER D 1 121 ? 36.358  34.673  -45.777 1.00 46.15 ? 121 SER D OG  1 
ATOM   6511 N N   . GLY D 1 122 ? 34.858  31.657  -44.371 1.00 35.97 ? 122 GLY D N   1 
ATOM   6512 C CA  . GLY D 1 122 ? 33.742  31.508  -43.447 1.00 35.86 ? 122 GLY D CA  1 
ATOM   6513 C C   . GLY D 1 122 ? 33.064  32.848  -43.211 1.00 32.85 ? 122 GLY D C   1 
ATOM   6514 O O   . GLY D 1 122 ? 32.759  33.577  -44.166 1.00 31.02 ? 122 GLY D O   1 
ATOM   6515 N N   . THR D 1 123 ? 32.799  33.171  -41.939 1.00 30.04 ? 123 THR D N   1 
ATOM   6516 C CA  . THR D 1 123 ? 32.117  34.410  -41.545 1.00 31.20 ? 123 THR D CA  1 
ATOM   6517 C C   . THR D 1 123 ? 32.803  34.988  -40.314 1.00 30.16 ? 123 THR D C   1 
ATOM   6518 O O   . THR D 1 123 ? 32.987  34.273  -39.320 1.00 30.12 ? 123 THR D O   1 
ATOM   6519 C CB  . THR D 1 123 ? 30.640  34.164  -41.164 1.00 28.27 ? 123 THR D CB  1 
ATOM   6520 O OG1 . THR D 1 123 ? 29.984  33.392  -42.170 1.00 25.94 ? 123 THR D OG1 1 
ATOM   6521 C CG2 . THR D 1 123 ? 29.907  35.522  -41.081 1.00 32.39 ? 123 THR D CG2 1 
ATOM   6522 N N   . SER D 1 124 ? 33.125  36.286  -40.341 1.00 27.61 ? 124 SER D N   1 
ATOM   6523 C CA  . SER D 1 124 ? 33.681  36.926  -39.157 1.00 28.81 ? 124 SER D CA  1 
ATOM   6524 C C   . SER D 1 124 ? 32.574  37.493  -38.285 1.00 29.69 ? 124 SER D C   1 
ATOM   6525 O O   . SER D 1 124 ? 31.494  37.815  -38.774 1.00 29.29 ? 124 SER D O   1 
ATOM   6526 C CB  . SER D 1 124 ? 34.618  38.071  -39.567 1.00 26.89 ? 124 SER D CB  1 
ATOM   6527 O OG  . SER D 1 124 ? 33.854  39.161  -40.069 1.00 26.47 ? 124 SER D OG  1 
ATOM   6528 N N   . PRO D 1 125 ? 32.833  37.686  -36.992 1.00 29.34 ? 125 PRO D N   1 
ATOM   6529 C CA  . PRO D 1 125 ? 31.843  38.377  -36.161 1.00 28.88 ? 125 PRO D CA  1 
ATOM   6530 C C   . PRO D 1 125 ? 31.454  39.741  -36.699 1.00 26.55 ? 125 PRO D C   1 
ATOM   6531 O O   . PRO D 1 125 ? 30.284  40.131  -36.592 1.00 32.17 ? 125 PRO D O   1 
ATOM   6532 C CB  . PRO D 1 125 ? 32.546  38.478  -34.806 1.00 29.25 ? 125 PRO D CB  1 
ATOM   6533 C CG  . PRO D 1 125 ? 33.475  37.326  -34.799 1.00 32.02 ? 125 PRO D CG  1 
ATOM   6534 C CD  . PRO D 1 125 ? 33.975  37.189  -36.199 1.00 29.56 ? 125 PRO D CD  1 
ATOM   6535 N N   . ALA D 1 126 ? 32.399  40.493  -37.275 1.00 32.28 ? 126 ALA D N   1 
ATOM   6536 C CA  . ALA D 1 126 ? 32.057  41.806  -37.832 1.00 30.68 ? 126 ALA D CA  1 
ATOM   6537 C C   . ALA D 1 126 ? 31.032  41.691  -38.961 1.00 29.48 ? 126 ALA D C   1 
ATOM   6538 O O   . ALA D 1 126 ? 30.099  42.503  -39.040 1.00 33.14 ? 126 ALA D O   1 
ATOM   6539 C CB  . ALA D 1 126 ? 33.318  42.526  -38.321 1.00 29.89 ? 126 ALA D CB  1 
ATOM   6540 N N   . GLN D 1 127 ? 31.185  40.691  -39.846 1.00 29.26 ? 127 GLN D N   1 
ATOM   6541 C CA  . GLN D 1 127 ? 30.162  40.457  -40.870 1.00 28.98 ? 127 GLN D CA  1 
ATOM   6542 C C   . GLN D 1 127 ? 28.805  40.161  -40.240 1.00 27.47 ? 127 GLN D C   1 
ATOM   6543 O O   . GLN D 1 127 ? 27.773  40.679  -40.684 1.00 27.55 ? 127 GLN D O   1 
ATOM   6544 C CB  . GLN D 1 127 ? 30.556  39.302  -41.788 1.00 28.49 ? 127 GLN D CB  1 
ATOM   6545 C CG  . GLN D 1 127 ? 31.744  39.604  -42.700 1.00 29.29 ? 127 GLN D CG  1 
ATOM   6546 C CD  . GLN D 1 127 ? 32.235  38.356  -43.409 1.00 31.96 ? 127 GLN D CD  1 
ATOM   6547 O OE1 . GLN D 1 127 ? 32.646  37.385  -42.766 1.00 30.31 ? 127 GLN D OE1 1 
ATOM   6548 N NE2 . GLN D 1 127 ? 32.177  38.370  -44.747 1.00 27.75 ? 127 GLN D NE2 1 
ATOM   6549 N N   . LEU D 1 128 ? 28.796  39.312  -39.215 1.00 27.30 ? 128 LEU D N   1 
ATOM   6550 C CA  . LEU D 1 128 ? 27.557  38.982  -38.523 1.00 30.01 ? 128 LEU D CA  1 
ATOM   6551 C C   . LEU D 1 128 ? 26.878  40.232  -37.970 1.00 28.61 ? 128 LEU D C   1 
ATOM   6552 O O   . LEU D 1 128 ? 25.689  40.462  -38.216 1.00 30.95 ? 128 LEU D O   1 
ATOM   6553 C CB  . LEU D 1 128 ? 27.849  37.982  -37.401 1.00 28.43 ? 128 LEU D CB  1 
ATOM   6554 C CG  . LEU D 1 128 ? 26.704  37.712  -36.419 1.00 27.62 ? 128 LEU D CG  1 
ATOM   6555 C CD1 . LEU D 1 128 ? 25.529  37.006  -37.100 1.00 26.33 ? 128 LEU D CD1 1 
ATOM   6556 C CD2 . LEU D 1 128 ? 27.200  36.918  -35.202 1.00 25.40 ? 128 LEU D CD2 1 
ATOM   6557 N N   . ILE D 1 129 ? 27.627  41.064  -37.240 1.00 30.76 ? 129 ILE D N   1 
ATOM   6558 C CA  . ILE D 1 129 ? 27.037  42.244  -36.610 1.00 29.99 ? 129 ILE D CA  1 
ATOM   6559 C C   . ILE D 1 129 ? 26.553  43.229  -37.666 1.00 29.06 ? 129 ILE D C   1 
ATOM   6560 O O   . ILE D 1 129 ? 25.426  43.747  -37.591 1.00 27.59 ? 129 ILE D O   1 
ATOM   6561 C CB  . ILE D 1 129 ? 28.050  42.903  -35.651 1.00 31.39 ? 129 ILE D CB  1 
ATOM   6562 C CG1 . ILE D 1 129 ? 28.352  41.988  -34.455 1.00 30.30 ? 129 ILE D CG1 1 
ATOM   6563 C CG2 . ILE D 1 129 ? 27.532  44.253  -35.174 1.00 31.32 ? 129 ILE D CG2 1 
ATOM   6564 C CD1 . ILE D 1 129 ? 29.691  42.240  -33.774 1.00 31.43 ? 129 ILE D CD1 1 
ATOM   6565 N N   . ALA D 1 130 ? 27.381  43.473  -38.684 1.00 26.50 ? 130 ALA D N   1 
ATOM   6566 C CA  . ALA D 1 130 ? 27.098  44.521  -39.664 1.00 27.38 ? 130 ALA D CA  1 
ATOM   6567 C C   . ALA D 1 130 ? 25.954  44.143  -40.598 1.00 30.23 ? 130 ALA D C   1 
ATOM   6568 O O   . ALA D 1 130 ? 25.240  45.032  -41.075 1.00 28.72 ? 130 ALA D O   1 
ATOM   6569 C CB  . ALA D 1 130 ? 28.349  44.843  -40.490 1.00 28.01 ? 130 ALA D CB  1 
ATOM   6570 N N   . ASN D 1 131 ? 25.758  42.845  -40.887 1.00 27.93 ? 131 ASN D N   1 
ATOM   6571 C CA  . ASN D 1 131 ? 24.832  42.458  -41.950 1.00 26.54 ? 131 ASN D CA  1 
ATOM   6572 C C   . ASN D 1 131 ? 23.546  41.801  -41.457 1.00 28.13 ? 131 ASN D C   1 
ATOM   6573 O O   . ASN D 1 131 ? 22.589  41.708  -42.234 1.00 26.23 ? 131 ASN D O   1 
ATOM   6574 C CB  . ASN D 1 131 ? 25.519  41.518  -42.941 1.00 29.71 ? 131 ASN D CB  1 
ATOM   6575 C CG  . ASN D 1 131 ? 26.500  42.249  -43.842 1.00 29.79 ? 131 ASN D CG  1 
ATOM   6576 O OD1 . ASN D 1 131 ? 26.150  43.220  -44.504 1.00 32.21 ? 131 ASN D OD1 1 
ATOM   6577 N ND2 . ASN D 1 131 ? 27.737  41.809  -43.833 1.00 28.63 ? 131 ASN D ND2 1 
ATOM   6578 N N   . ALA D 1 132 ? 23.494  41.348  -40.209 1.00 25.73 ? 132 ALA D N   1 
ATOM   6579 C CA  . ALA D 1 132 ? 22.243  40.773  -39.707 1.00 27.93 ? 132 ALA D CA  1 
ATOM   6580 C C   . ALA D 1 132 ? 21.039  41.711  -39.825 1.00 28.29 ? 132 ALA D C   1 
ATOM   6581 O O   . ALA D 1 132 ? 19.922  41.194  -40.004 1.00 28.62 ? 132 ALA D O   1 
ATOM   6582 C CB  . ALA D 1 132 ? 22.417  40.312  -38.254 1.00 28.90 ? 132 ALA D CB  1 
ATOM   6583 N N   . PRO D 1 133 ? 21.169  43.048  -39.714 1.00 30.73 ? 133 PRO D N   1 
ATOM   6584 C CA  . PRO D 1 133 ? 19.998  43.910  -39.949 1.00 28.86 ? 133 PRO D CA  1 
ATOM   6585 C C   . PRO D 1 133 ? 19.325  43.698  -41.295 1.00 27.76 ? 133 PRO D C   1 
ATOM   6586 O O   . PRO D 1 133 ? 18.127  43.972  -41.424 1.00 27.37 ? 133 PRO D O   1 
ATOM   6587 C CB  . PRO D 1 133 ? 20.598  45.321  -39.829 1.00 29.90 ? 133 PRO D CB  1 
ATOM   6588 C CG  . PRO D 1 133 ? 21.630  45.159  -38.781 1.00 28.27 ? 133 PRO D CG  1 
ATOM   6589 C CD  . PRO D 1 133 ? 22.256  43.813  -39.056 1.00 27.81 ? 133 PRO D CD  1 
ATOM   6590 N N   . LYS D 1 134 ? 20.050  43.241  -42.315 1.00 26.87 ? 134 LYS D N   1 
ATOM   6591 C CA  . LYS D 1 134 ? 19.417  42.976  -43.608 1.00 26.86 ? 134 LYS D CA  1 
ATOM   6592 C C   . LYS D 1 134 ? 18.354  41.897  -43.513 1.00 27.20 ? 134 LYS D C   1 
ATOM   6593 O O   . LYS D 1 134 ? 17.459  41.828  -44.363 1.00 27.35 ? 134 LYS D O   1 
ATOM   6594 C CB  . LYS D 1 134 ? 20.476  42.596  -44.645 1.00 28.56 ? 134 LYS D CB  1 
ATOM   6595 C CG  . LYS D 1 134 ? 21.413  43.767  -44.912 1.00 27.71 ? 134 LYS D CG  1 
ATOM   6596 C CD  . LYS D 1 134 ? 22.177  43.629  -46.214 1.00 37.48 ? 134 LYS D CD  1 
ATOM   6597 C CE  . LYS D 1 134 ? 23.061  42.412  -46.190 1.00 36.82 ? 134 LYS D CE  1 
ATOM   6598 N NZ  . LYS D 1 134 ? 23.709  42.162  -47.521 1.00 43.31 ? 134 LYS D NZ  1 
ATOM   6599 N N   . LEU D 1 135 ? 18.437  41.060  -42.503 1.00 24.92 ? 135 LEU D N   1 
ATOM   6600 C CA  . LEU D 1 135 ? 17.486  39.980  -42.305 1.00 30.30 ? 135 LEU D CA  1 
ATOM   6601 C C   . LEU D 1 135 ? 16.467  40.311  -41.224 1.00 30.00 ? 135 LEU D C   1 
ATOM   6602 O O   . LEU D 1 135 ? 15.625  39.461  -40.892 1.00 31.34 ? 135 LEU D O   1 
ATOM   6603 C CB  . LEU D 1 135 ? 18.245  38.711  -41.933 1.00 25.61 ? 135 LEU D CB  1 
ATOM   6604 C CG  . LEU D 1 135 ? 19.286  38.213  -42.930 1.00 28.52 ? 135 LEU D CG  1 
ATOM   6605 C CD1 . LEU D 1 135 ? 20.276  37.323  -42.218 1.00 29.42 ? 135 LEU D CD1 1 
ATOM   6606 C CD2 . LEU D 1 135 ? 18.654  37.440  -44.037 1.00 27.74 ? 135 LEU D CD2 1 
ATOM   6607 N N   . GLY D 1 136 ? 16.539  41.508  -40.655 1.00 30.30 ? 136 GLY D N   1 
ATOM   6608 C CA  . GLY D 1 136 ? 15.637  41.919  -39.596 1.00 29.71 ? 136 GLY D CA  1 
ATOM   6609 C C   . GLY D 1 136 ? 16.148  41.744  -38.183 1.00 30.59 ? 136 GLY D C   1 
ATOM   6610 O O   . GLY D 1 136 ? 15.343  41.807  -37.244 1.00 31.51 ? 136 GLY D O   1 
ATOM   6611 N N   . PHE D 1 137 ? 17.448  41.525  -37.994 1.00 27.26 ? 137 PHE D N   1 
ATOM   6612 C CA  . PHE D 1 137 ? 17.995  41.259  -36.671 1.00 27.71 ? 137 PHE D CA  1 
ATOM   6613 C C   . PHE D 1 137 ? 19.000  42.326  -36.262 1.00 30.69 ? 137 PHE D C   1 
ATOM   6614 O O   . PHE D 1 137 ? 19.674  42.936  -37.104 1.00 32.41 ? 137 PHE D O   1 
ATOM   6615 C CB  . PHE D 1 137 ? 18.644  39.870  -36.623 1.00 26.15 ? 137 PHE D CB  1 
ATOM   6616 C CG  . PHE D 1 137 ? 17.687  38.777  -36.995 1.00 27.50 ? 137 PHE D CG  1 
ATOM   6617 C CD1 . PHE D 1 137 ? 16.578  38.517  -36.196 1.00 26.28 ? 137 PHE D CD1 1 
ATOM   6618 C CD2 . PHE D 1 137 ? 17.841  38.068  -38.178 1.00 27.58 ? 137 PHE D CD2 1 
ATOM   6619 C CE1 . PHE D 1 137 ? 15.681  37.541  -36.551 1.00 24.60 ? 137 PHE D CE1 1 
ATOM   6620 C CE2 . PHE D 1 137 ? 16.939  37.091  -38.528 1.00 28.60 ? 137 PHE D CE2 1 
ATOM   6621 C CZ  . PHE D 1 137 ? 15.858  36.837  -37.711 1.00 22.88 ? 137 PHE D CZ  1 
ATOM   6622 N N   . LYS D 1 138 ? 19.109  42.522  -34.953 1.00 29.15 ? 138 LYS D N   1 
ATOM   6623 C CA  . LYS D 1 138 ? 20.155  43.333  -34.353 1.00 30.90 ? 138 LYS D CA  1 
ATOM   6624 C C   . LYS D 1 138 ? 21.020  42.416  -33.512 1.00 31.97 ? 138 LYS D C   1 
ATOM   6625 O O   . LYS D 1 138 ? 20.504  41.574  -32.777 1.00 29.44 ? 138 LYS D O   1 
ATOM   6626 C CB  . LYS D 1 138 ? 19.580  44.470  -33.477 1.00 32.64 ? 138 LYS D CB  1 
ATOM   6627 C CG  . LYS D 1 138 ? 20.642  45.196  -32.665 1.00 36.28 ? 138 LYS D CG  1 
ATOM   6628 C CD  . LYS D 1 138 ? 20.209  46.598  -32.259 1.00 45.95 ? 138 LYS D CD  1 
ATOM   6629 C CE  . LYS D 1 138 ? 19.760  46.648  -30.820 1.00 46.09 ? 138 LYS D CE  1 
ATOM   6630 N NZ  . LYS D 1 138 ? 20.934  46.781  -29.909 1.00 50.65 ? 138 LYS D NZ  1 
ATOM   6631 N N   . ILE D 1 139 ? 22.334  42.575  -33.621 1.00 28.59 ? 139 ILE D N   1 
ATOM   6632 C CA  . ILE D 1 139 ? 23.276  41.759  -32.873 1.00 29.40 ? 139 ILE D CA  1 
ATOM   6633 C C   . ILE D 1 139 ? 23.885  42.623  -31.783 1.00 30.98 ? 139 ILE D C   1 
ATOM   6634 O O   . ILE D 1 139 ? 24.470  43.670  -32.069 1.00 34.07 ? 139 ILE D O   1 
ATOM   6635 C CB  . ILE D 1 139 ? 24.360  41.168  -33.782 1.00 30.19 ? 139 ILE D CB  1 
ATOM   6636 C CG1 . ILE D 1 139 ? 23.734  40.437  -34.979 1.00 28.37 ? 139 ILE D CG1 1 
ATOM   6637 C CG2 . ILE D 1 139 ? 25.244  40.214  -32.990 1.00 33.51 ? 139 ILE D CG2 1 
ATOM   6638 C CD1 . ILE D 1 139 ? 23.099  39.090  -34.609 1.00 26.76 ? 139 ILE D CD1 1 
ATOM   6639 N N   . ILE D 1 140 ? 23.833  42.124  -30.561 1.00 30.76 ? 140 ILE D N   1 
ATOM   6640 C CA  . ILE D 1 140 ? 24.430  42.848  -29.415 1.00 33.13 ? 140 ILE D CA  1 
ATOM   6641 C C   . ILE D 1 140 ? 25.650  42.062  -28.935 1.00 32.83 ? 140 ILE D C   1 
ATOM   6642 O O   . ILE D 1 140 ? 25.478  40.978  -28.408 1.00 32.96 ? 140 ILE D O   1 
ATOM   6643 C CB  . ILE D 1 140 ? 23.406  42.993  -28.288 1.00 33.23 ? 140 ILE D CB  1 
ATOM   6644 C CG1 . ILE D 1 140 ? 22.097  43.577  -28.799 1.00 32.64 ? 140 ILE D CG1 1 
ATOM   6645 C CG2 . ILE D 1 140 ? 23.978  43.813  -27.152 1.00 31.55 ? 140 ILE D CG2 1 
ATOM   6646 C CD1 . ILE D 1 140 ? 21.134  43.837  -27.699 1.00 35.47 ? 140 ILE D CD1 1 
ATOM   6647 N N   . PRO D 1 141 ? 26.880  42.557  -29.146 1.00 29.94 ? 141 PRO D N   1 
ATOM   6648 C CA  . PRO D 1 141 ? 28.039  41.875  -28.648 1.00 33.56 ? 141 PRO D CA  1 
ATOM   6649 C C   . PRO D 1 141 ? 27.953  41.956  -27.126 1.00 34.25 ? 141 PRO D C   1 
ATOM   6650 O O   . PRO D 1 141 ? 27.675  42.990  -26.617 1.00 33.99 ? 141 PRO D O   1 
ATOM   6651 C CB  . PRO D 1 141 ? 29.235  42.682  -29.149 1.00 34.26 ? 141 PRO D CB  1 
ATOM   6652 C CG  . PRO D 1 141 ? 28.681  43.541  -30.234 1.00 36.32 ? 141 PRO D CG  1 
ATOM   6653 C CD  . PRO D 1 141 ? 27.203  43.700  -29.954 1.00 31.61 ? 141 PRO D CD  1 
ATOM   6654 N N   . ILE D 1 142 ? 28.149  40.833  -26.462 1.00 32.48 ? 142 ILE D N   1 
ATOM   6655 C CA  . ILE D 1 142 ? 28.151  40.840  -24.980 1.00 31.86 ? 142 ILE D CA  1 
ATOM   6656 C C   . ILE D 1 142 ? 29.436  40.180  -24.504 1.00 35.69 ? 142 ILE D C   1 
ATOM   6657 O O   . ILE D 1 142 ? 30.132  39.570  -25.296 1.00 33.90 ? 142 ILE D O   1 
ATOM   6658 C CB  . ILE D 1 142 ? 26.917  40.142  -24.386 1.00 34.61 ? 142 ILE D CB  1 
ATOM   6659 C CG1 . ILE D 1 142 ? 26.781  38.705  -24.884 1.00 34.08 ? 142 ILE D CG1 1 
ATOM   6660 C CG2 . ILE D 1 142 ? 25.670  40.964  -24.643 1.00 36.72 ? 142 ILE D CG2 1 
ATOM   6661 C CD1 . ILE D 1 142 ? 25.940  37.834  -24.017 1.00 34.66 ? 142 ILE D CD1 1 
ATOM   6662 N N   . LYS D 1 143 ? 29.671  40.273  -23.205 1.00 37.93 ? 143 LYS D N   1 
ATOM   6663 C CA  . LYS D 1 143 ? 30.845  39.649  -22.580 1.00 36.78 ? 143 LYS D CA  1 
ATOM   6664 C C   . LYS D 1 143 ? 30.646  38.131  -22.556 1.00 35.29 ? 143 LYS D C   1 
ATOM   6665 O O   . LYS D 1 143 ? 29.523  37.672  -22.528 1.00 36.35 ? 143 LYS D O   1 
ATOM   6666 C CB  . LYS D 1 143 ? 31.046  40.241  -21.187 1.00 40.94 ? 143 LYS D CB  1 
ATOM   6667 C CG  . LYS D 1 143 ? 31.755  41.583  -21.168 1.00 44.26 ? 143 LYS D CG  1 
ATOM   6668 C CD  . LYS D 1 143 ? 31.525  42.355  -19.904 1.00 53.06 ? 143 LYS D CD  1 
ATOM   6669 C CE  . LYS D 1 143 ? 32.375  43.602  -19.803 1.00 58.83 ? 143 LYS D CE  1 
ATOM   6670 N NZ  . LYS D 1 143 ? 31.873  44.690  -20.673 1.00 58.91 ? 143 LYS D NZ  1 
ATOM   6671 N N   . ARG D 1 144 ? 31.738  37.385  -22.604 1.00 38.04 ? 144 ARG D N   1 
ATOM   6672 C CA  . ARG D 1 144 ? 31.628  35.909  -22.543 1.00 36.86 ? 144 ARG D CA  1 
ATOM   6673 C C   . ARG D 1 144 ? 31.458  35.567  -21.068 1.00 37.82 ? 144 ARG D C   1 
ATOM   6674 O O   . ARG D 1 144 ? 32.404  35.160  -20.455 1.00 38.86 ? 144 ARG D O   1 
ATOM   6675 C CB  . ARG D 1 144 ? 32.853  35.278  -23.206 1.00 34.50 ? 144 ARG D CB  1 
ATOM   6676 C CG  . ARG D 1 144 ? 33.043  35.701  -24.651 1.00 33.94 ? 144 ARG D CG  1 
ATOM   6677 C CD  . ARG D 1 144 ? 34.288  35.117  -25.265 1.00 33.16 ? 144 ARG D CD  1 
ATOM   6678 N NE  . ARG D 1 144 ? 34.278  33.690  -25.494 1.00 34.67 ? 144 ARG D NE  1 
ATOM   6679 C CZ  . ARG D 1 144 ? 33.964  33.107  -26.634 1.00 32.87 ? 144 ARG D CZ  1 
ATOM   6680 N NH1 . ARG D 1 144 ? 33.581  33.817  -27.672 1.00 29.20 ? 144 ARG D NH1 1 
ATOM   6681 N NH2 . ARG D 1 144 ? 34.028  31.800  -26.723 1.00 34.65 ? 144 ARG D NH2 1 
ATOM   6682 N N   . ASP D 1 145 ? 30.249  35.731  -20.557 1.00 38.83 ? 145 ASP D N   1 
ATOM   6683 C CA  . ASP D 1 145 ? 29.980  35.576  -19.147 1.00 37.86 ? 145 ASP D CA  1 
ATOM   6684 C C   . ASP D 1 145 ? 28.591  34.981  -19.004 1.00 38.96 ? 145 ASP D C   1 
ATOM   6685 O O   . ASP D 1 145 ? 27.641  35.491  -19.605 1.00 38.15 ? 145 ASP D O   1 
ATOM   6686 C CB  . ASP D 1 145 ? 30.090  36.938  -18.454 1.00 42.48 ? 145 ASP D CB  1 
ATOM   6687 C CG  . ASP D 1 145 ? 29.470  36.938  -17.081 1.00 45.95 ? 145 ASP D CG  1 
ATOM   6688 O OD1 . ASP D 1 145 ? 28.239  37.069  -16.995 1.00 47.56 ? 145 ASP D OD1 1 
ATOM   6689 O OD2 . ASP D 1 145 ? 30.205  36.782  -16.088 1.00 50.95 ? 145 ASP D OD2 1 
ATOM   6690 N N   . SER D 1 146 ? 28.464  33.928  -18.194 1.00 35.79 ? 146 SER D N   1 
ATOM   6691 C CA  . SER D 1 146 ? 27.192  33.216  -18.125 1.00 40.32 ? 146 SER D CA  1 
ATOM   6692 C C   . SER D 1 146 ? 26.060  34.112  -17.636 1.00 42.60 ? 146 SER D C   1 
ATOM   6693 O O   . SER D 1 146 ? 24.903  33.907  -18.022 1.00 41.48 ? 146 SER D O   1 
ATOM   6694 C CB  . SER D 1 146 ? 27.314  31.984  -17.221 1.00 40.52 ? 146 SER D CB  1 
ATOM   6695 O OG  . SER D 1 146 ? 27.728  32.329  -15.906 1.00 42.00 ? 146 SER D OG  1 
ATOM   6696 N N   . LYS D 1 147 ? 26.361  35.096  -16.779 1.00 43.31 ? 147 LYS D N   1 
ATOM   6697 C CA  . LYS D 1 147 ? 25.305  35.972  -16.266 1.00 41.70 ? 147 LYS D CA  1 
ATOM   6698 C C   . LYS D 1 147 ? 24.764  36.875  -17.370 1.00 40.24 ? 147 LYS D C   1 
ATOM   6699 O O   . LYS D 1 147 ? 23.554  37.118  -17.442 1.00 39.71 ? 147 LYS D O   1 
ATOM   6700 C CB  . LYS D 1 147 ? 25.834  36.777  -15.078 1.00 43.23 ? 147 LYS D CB  1 
ATOM   6701 C CG  . LYS D 1 147 ? 26.516  35.865  -14.044 1.00 43.44 ? 147 LYS D CG  1 
ATOM   6702 C CD  . LYS D 1 147 ? 25.509  34.911  -13.399 1.00 52.80 ? 147 LYS D CD  1 
ATOM   6703 C CE  . LYS D 1 147 ? 26.092  33.516  -13.076 1.00 52.94 ? 147 LYS D CE  1 
ATOM   6704 N NZ  . LYS D 1 147 ? 25.568  32.456  -14.028 1.00 45.73 ? 147 LYS D NZ  1 
ATOM   6705 N N   . GLU D 1 148 ? 25.647  37.390  -18.235 1.00 36.99 ? 148 GLU D N   1 
ATOM   6706 C CA  . GLU D 1 148 ? 25.196  38.182  -19.379 1.00 37.30 ? 148 GLU D CA  1 
ATOM   6707 C C   . GLU D 1 148 ? 24.357  37.333  -20.334 1.00 38.09 ? 148 GLU D C   1 
ATOM   6708 O O   . GLU D 1 148 ? 23.336  37.796  -20.869 1.00 39.58 ? 148 GLU D O   1 
ATOM   6709 C CB  . GLU D 1 148 ? 26.393  38.799  -20.081 1.00 39.51 ? 148 GLU D CB  1 
ATOM   6710 C CG  . GLU D 1 148 ? 26.931  39.994  -19.346 1.00 44.60 ? 148 GLU D CG  1 
ATOM   6711 C CD  . GLU D 1 148 ? 25.939  41.117  -19.320 1.00 47.39 ? 148 GLU D CD  1 
ATOM   6712 O OE1 . GLU D 1 148 ? 25.845  41.829  -20.340 1.00 47.28 ? 148 GLU D OE1 1 
ATOM   6713 O OE2 . GLU D 1 148 ? 25.232  41.257  -18.299 1.00 43.65 ? 148 GLU D OE2 1 
ATOM   6714 N N   . VAL D 1 149 ? 24.751  36.078  -20.548 1.00 34.12 ? 149 VAL D N   1 
ATOM   6715 C CA  . VAL D 1 149 ? 23.935  35.212  -21.366 1.00 36.09 ? 149 VAL D CA  1 
ATOM   6716 C C   . VAL D 1 149 ? 22.613  35.078  -20.674 1.00 38.49 ? 149 VAL D C   1 
ATOM   6717 O O   . VAL D 1 149 ? 21.525  35.004  -21.320 1.00 37.38 ? 149 VAL D O   1 
ATOM   6718 C CB  . VAL D 1 149 ? 24.642  33.867  -21.634 1.00 36.55 ? 149 VAL D CB  1 
ATOM   6719 C CG1 . VAL D 1 149 ? 23.740  32.887  -22.373 1.00 33.28 ? 149 VAL D CG1 1 
ATOM   6720 C CG2 . VAL D 1 149 ? 26.012  34.077  -22.402 1.00 34.56 ? 149 VAL D CG2 1 
ATOM   6721 N N   . LYS D 1 150 ? 22.611  34.787  -19.384 1.00 41.64 ? 150 LYS D N   1 
ATOM   6722 C CA  . LYS D 1 150 ? 21.310  34.461  -18.735 1.00 40.99 ? 150 LYS D CA  1 
ATOM   6723 C C   . LYS D 1 150 ? 20.256  35.559  -18.902 1.00 40.18 ? 150 LYS D C   1 
ATOM   6724 O O   . LYS D 1 150 ? 19.100  35.233  -19.068 1.00 40.89 ? 150 LYS D O   1 
ATOM   6725 C CB  . LYS D 1 150 ? 21.516  34.193  -17.250 1.00 49.58 ? 150 LYS D CB  1 
ATOM   6726 C CG  . LYS D 1 150 ? 20.239  34.271  -16.433 1.00 47.05 ? 150 LYS D CG  1 
ATOM   6727 C CD  . LYS D 1 150 ? 19.701  32.933  -16.034 1.00 55.79 ? 150 LYS D CD  1 
ATOM   6728 C CE  . LYS D 1 150 ? 19.754  32.699  -14.539 1.00 58.93 ? 150 LYS D CE  1 
ATOM   6729 N NZ  . LYS D 1 150 ? 18.435  32.903  -13.886 1.00 58.68 ? 150 LYS D NZ  1 
ATOM   6730 N N   . LYS D 1 151 ? 20.722  36.776  -19.095 1.00 39.27 ? 151 LYS D N   1 
ATOM   6731 C CA  . LYS D 1 151 ? 19.940  38.000  -19.116 1.00 38.73 ? 151 LYS D CA  1 
ATOM   6732 C C   . LYS D 1 151 ? 19.219  38.169  -20.432 1.00 37.67 ? 151 LYS D C   1 
ATOM   6733 O O   . LYS D 1 151 ? 18.051  38.583  -20.489 1.00 35.48 ? 151 LYS D O   1 
ATOM   6734 C CB  . LYS D 1 151 ? 20.858  39.202  -18.859 1.00 39.22 ? 151 LYS D CB  1 
ATOM   6735 C CG  . LYS D 1 151 ? 20.289  40.545  -19.222 1.00 38.85 ? 151 LYS D CG  1 
ATOM   6736 C CD  . LYS D 1 151 ? 21.382  41.554  -19.592 1.00 39.85 ? 151 LYS D CD  1 
ATOM   6737 C CE  . LYS D 1 151 ? 21.353  42.844  -18.800 1.00 44.93 ? 151 LYS D CE  1 
ATOM   6738 N NZ  . LYS D 1 151 ? 22.241  43.881  -19.456 1.00 49.61 ? 151 LYS D NZ  1 
ATOM   6739 N N   . TYR D 1 152 ? 19.921  37.850  -21.502 1.00 33.16 ? 152 TYR D N   1 
ATOM   6740 C CA  . TYR D 1 152 ? 19.296  37.970  -22.790 1.00 34.84 ? 152 TYR D CA  1 
ATOM   6741 C C   . TYR D 1 152 ? 18.429  36.758  -23.086 1.00 33.35 ? 152 TYR D C   1 
ATOM   6742 O O   . TYR D 1 152 ? 17.368  36.913  -23.699 1.00 32.52 ? 152 TYR D O   1 
ATOM   6743 C CB  . TYR D 1 152 ? 20.372  38.233  -23.827 1.00 33.47 ? 152 TYR D CB  1 
ATOM   6744 C CG  . TYR D 1 152 ? 20.935  39.625  -23.637 1.00 36.52 ? 152 TYR D CG  1 
ATOM   6745 C CD1 . TYR D 1 152 ? 20.238  40.734  -24.091 1.00 34.56 ? 152 TYR D CD1 1 
ATOM   6746 C CD2 . TYR D 1 152 ? 22.134  39.839  -22.960 1.00 36.23 ? 152 TYR D CD2 1 
ATOM   6747 C CE1 . TYR D 1 152 ? 20.729  42.002  -23.929 1.00 37.35 ? 152 TYR D CE1 1 
ATOM   6748 C CE2 . TYR D 1 152 ? 22.625  41.124  -22.775 1.00 35.14 ? 152 TYR D CE2 1 
ATOM   6749 C CZ  . TYR D 1 152 ? 21.917  42.203  -23.270 1.00 37.75 ? 152 TYR D CZ  1 
ATOM   6750 O OH  . TYR D 1 152 ? 22.361  43.508  -23.120 1.00 42.53 ? 152 TYR D OH  1 
ATOM   6751 N N   . LEU D 1 153 ? 18.820  35.568  -22.618 1.00 34.42 ? 153 LEU D N   1 
ATOM   6752 C CA  . LEU D 1 153 ? 17.944  34.403  -22.747 1.00 36.65 ? 153 LEU D CA  1 
ATOM   6753 C C   . LEU D 1 153 ? 16.611  34.643  -22.037 1.00 38.15 ? 153 LEU D C   1 
ATOM   6754 O O   . LEU D 1 153 ? 15.545  34.260  -22.535 1.00 36.55 ? 153 LEU D O   1 
ATOM   6755 C CB  . LEU D 1 153 ? 18.621  33.156  -22.176 1.00 33.66 ? 153 LEU D CB  1 
ATOM   6756 C CG  . LEU D 1 153 ? 19.824  32.566  -22.917 1.00 38.13 ? 153 LEU D CG  1 
ATOM   6757 C CD1 . LEU D 1 153 ? 20.369  31.342  -22.160 1.00 35.23 ? 153 LEU D CD1 1 
ATOM   6758 C CD2 . LEU D 1 153 ? 19.495  32.208  -24.363 1.00 30.12 ? 153 LEU D CD2 1 
ATOM   6759 N N   . LYS D 1 154 ? 16.653  35.299  -20.878 1.00 38.35 ? 154 LYS D N   1 
ATOM   6760 C CA  . LYS D 1 154 ? 15.424  35.570  -20.143 1.00 38.11 ? 154 LYS D CA  1 
ATOM   6761 C C   . LYS D 1 154 ? 14.548  36.573  -20.878 1.00 39.13 ? 154 LYS D C   1 
ATOM   6762 O O   . LYS D 1 154 ? 13.348  36.637  -20.615 1.00 41.71 ? 154 LYS D O   1 
ATOM   6763 C CB  . LYS D 1 154 ? 15.759  36.067  -18.733 1.00 40.34 ? 154 LYS D CB  1 
ATOM   6764 C CG  . LYS D 1 154 ? 15.820  34.959  -17.690 1.00 43.40 ? 154 LYS D CG  1 
ATOM   6765 C CD  . LYS D 1 154 ? 15.686  35.519  -16.272 1.00 50.13 ? 154 LYS D CD  1 
ATOM   6766 C CE  . LYS D 1 154 ? 14.557  34.814  -15.518 1.00 54.45 ? 154 LYS D CE  1 
ATOM   6767 N NZ  . LYS D 1 154 ? 14.754  34.815  -14.038 1.00 58.60 ? 154 LYS D NZ  1 
ATOM   6768 N N   . LYS D 1 155 ? 15.118  37.365  -21.787 1.00 33.64 ? 155 LYS D N   1 
ATOM   6769 C CA  . LYS D 1 155 ? 14.316  38.213  -22.654 1.00 34.65 ? 155 LYS D CA  1 
ATOM   6770 C C   . LYS D 1 155 ? 13.801  37.468  -23.882 1.00 35.36 ? 155 LYS D C   1 
ATOM   6771 O O   . LYS D 1 155 ? 13.049  38.052  -24.667 1.00 40.44 ? 155 LYS D O   1 
ATOM   6772 C CB  . LYS D 1 155 ? 15.139  39.412  -23.116 1.00 36.53 ? 155 LYS D CB  1 
ATOM   6773 C CG  . LYS D 1 155 ? 15.835  40.138  -21.997 1.00 37.02 ? 155 LYS D CG  1 
ATOM   6774 C CD  . LYS D 1 155 ? 16.337  41.474  -22.435 1.00 38.20 ? 155 LYS D CD  1 
ATOM   6775 C CE  . LYS D 1 155 ? 17.269  42.050  -21.379 1.00 43.71 ? 155 LYS D CE  1 
ATOM   6776 N NZ  . LYS D 1 155 ? 17.146  43.536  -21.248 1.00 51.42 ? 155 LYS D NZ  1 
ATOM   6777 N N   . GLY D 1 156 ? 14.131  36.193  -24.030 1.00 34.18 ? 156 GLY D N   1 
ATOM   6778 C CA  . GLY D 1 156 ? 13.780  35.401  -25.193 1.00 35.09 ? 156 GLY D CA  1 
ATOM   6779 C C   . GLY D 1 156 ? 14.718  35.549  -26.371 1.00 34.53 ? 156 GLY D C   1 
ATOM   6780 O O   . GLY D 1 156 ? 14.375  35.105  -27.470 1.00 35.01 ? 156 GLY D O   1 
ATOM   6781 N N   . PHE D 1 157 ? 15.898  36.145  -26.176 1.00 29.58 ? 157 PHE D N   1 
ATOM   6782 C CA  . PHE D 1 157 ? 16.860  36.332  -27.264 1.00 30.61 ? 157 PHE D CA  1 
ATOM   6783 C C   . PHE D 1 157 ? 17.941  35.266  -27.163 1.00 30.52 ? 157 PHE D C   1 
ATOM   6784 O O   . PHE D 1 157 ? 18.613  35.200  -26.123 1.00 31.09 ? 157 PHE D O   1 
ATOM   6785 C CB  . PHE D 1 157 ? 17.499  37.716  -27.205 1.00 27.58 ? 157 PHE D CB  1 
ATOM   6786 C CG  . PHE D 1 157 ? 16.521  38.865  -27.174 1.00 29.52 ? 157 PHE D CG  1 
ATOM   6787 C CD1 . PHE D 1 157 ? 15.288  38.781  -27.792 1.00 28.30 ? 157 PHE D CD1 1 
ATOM   6788 C CD2 . PHE D 1 157 ? 16.890  40.069  -26.584 1.00 29.68 ? 157 PHE D CD2 1 
ATOM   6789 C CE1 . PHE D 1 157 ? 14.402  39.852  -27.758 1.00 28.45 ? 157 PHE D CE1 1 
ATOM   6790 C CE2 . PHE D 1 157 ? 16.025  41.146  -26.559 1.00 30.52 ? 157 PHE D CE2 1 
ATOM   6791 C CZ  . PHE D 1 157 ? 14.774  41.035  -27.149 1.00 28.35 ? 157 PHE D CZ  1 
ATOM   6792 N N   . PRO D 1 158 ? 18.158  34.430  -28.178 1.00 29.36 ? 158 PRO D N   1 
ATOM   6793 C CA  . PRO D 1 158 ? 19.234  33.431  -28.113 1.00 28.57 ? 158 PRO D CA  1 
ATOM   6794 C C   . PRO D 1 158 ? 20.575  34.096  -28.407 1.00 28.19 ? 158 PRO D C   1 
ATOM   6795 O O   . PRO D 1 158 ? 20.637  35.245  -28.827 1.00 28.96 ? 158 PRO D O   1 
ATOM   6796 C CB  . PRO D 1 158 ? 18.838  32.439  -29.208 1.00 26.79 ? 158 PRO D CB  1 
ATOM   6797 C CG  . PRO D 1 158 ? 18.249  33.365  -30.270 1.00 28.37 ? 158 PRO D CG  1 
ATOM   6798 C CD  . PRO D 1 158 ? 17.549  34.488  -29.517 1.00 28.42 ? 158 PRO D CD  1 
ATOM   6799 N N   . VAL D 1 159 ? 21.666  33.364  -28.179 1.00 25.49 ? 159 VAL D N   1 
ATOM   6800 C CA  . VAL D 1 159 ? 22.994  33.979  -28.192 1.00 28.03 ? 159 VAL D CA  1 
ATOM   6801 C C   . VAL D 1 159 ? 23.934  33.168  -29.068 1.00 26.85 ? 159 VAL D C   1 
ATOM   6802 O O   . VAL D 1 159 ? 24.258  32.016  -28.747 1.00 28.66 ? 159 VAL D O   1 
ATOM   6803 C CB  . VAL D 1 159 ? 23.577  34.114  -26.777 1.00 30.54 ? 159 VAL D CB  1 
ATOM   6804 C CG1 . VAL D 1 159 ? 24.988  34.681  -26.847 1.00 31.17 ? 159 VAL D CG1 1 
ATOM   6805 C CG2 . VAL D 1 159 ? 22.667  35.005  -25.910 1.00 30.49 ? 159 VAL D CG2 1 
ATOM   6806 N N   . ILE D 1 160 ? 24.396  33.772  -30.155 1.00 28.92 ? 160 ILE D N   1 
ATOM   6807 C CA  . ILE D 1 160 ? 25.379  33.101  -30.997 1.00 26.63 ? 160 ILE D CA  1 
ATOM   6808 C C   . ILE D 1 160 ? 26.728  33.088  -30.284 1.00 29.49 ? 160 ILE D C   1 
ATOM   6809 O O   . ILE D 1 160 ? 27.187  34.122  -29.777 1.00 28.47 ? 160 ILE D O   1 
ATOM   6810 C CB  . ILE D 1 160 ? 25.472  33.786  -32.363 1.00 24.97 ? 160 ILE D CB  1 
ATOM   6811 C CG1 . ILE D 1 160 ? 24.185  33.547  -33.167 1.00 24.95 ? 160 ILE D CG1 1 
ATOM   6812 C CG2 . ILE D 1 160 ? 26.709  33.249  -33.135 1.00 27.95 ? 160 ILE D CG2 1 
ATOM   6813 C CD1 . ILE D 1 160 ? 24.146  34.287  -34.522 1.00 23.30 ? 160 ILE D CD1 1 
ATOM   6814 N N   . CYS D 1 161 ? 27.347  31.900  -30.199 1.00 25.82 ? 161 CYS D N   1 
ATOM   6815 C CA  . CYS D 1 161 ? 28.667  31.744  -29.605 1.00 27.43 ? 161 CYS D CA  1 
ATOM   6816 C C   . CYS D 1 161 ? 29.705  31.448  -30.683 1.00 26.82 ? 161 CYS D C   1 
ATOM   6817 O O   . CYS D 1 161 ? 29.395  30.884  -31.734 1.00 24.74 ? 161 CYS D O   1 
ATOM   6818 C CB  . CYS D 1 161 ? 28.679  30.640  -28.528 1.00 30.13 ? 161 CYS D CB  1 
ATOM   6819 S SG  . CYS D 1 161 ? 28.105  28.976  -29.008 1.00 32.02 ? 161 CYS D SG  1 
ATOM   6820 N N   . HIS D 1 162 ? 30.935  31.884  -30.422 1.00 27.86 ? 162 HIS D N   1 
ATOM   6821 C CA  . HIS D 1 162 ? 32.063  31.782  -31.337 1.00 28.08 ? 162 HIS D CA  1 
ATOM   6822 C C   . HIS D 1 162 ? 33.222  31.204  -30.542 1.00 31.08 ? 162 HIS D C   1 
ATOM   6823 O O   . HIS D 1 162 ? 33.530  31.698  -29.448 1.00 31.28 ? 162 HIS D O   1 
ATOM   6824 C CB  . HIS D 1 162 ? 32.449  33.170  -31.901 1.00 28.94 ? 162 HIS D CB  1 
ATOM   6825 C CG  . HIS D 1 162 ? 33.605  33.156  -32.861 1.00 30.01 ? 162 HIS D CG  1 
ATOM   6826 N ND1 . HIS D 1 162 ? 34.519  34.192  -32.933 1.00 32.96 ? 162 HIS D ND1 1 
ATOM   6827 C CD2 . HIS D 1 162 ? 33.953  32.282  -33.838 1.00 28.57 ? 162 HIS D CD2 1 
ATOM   6828 C CE1 . HIS D 1 162 ? 35.404  33.934  -33.883 1.00 30.10 ? 162 HIS D CE1 1 
ATOM   6829 N NE2 . HIS D 1 162 ? 35.087  32.776  -34.444 1.00 31.79 ? 162 HIS D NE2 1 
ATOM   6830 N N   . TRP D 1 163 ? 33.868  30.170  -31.078 1.00 28.40 ? 163 TRP D N   1 
ATOM   6831 C CA  . TRP D 1 163 ? 34.959  29.581  -30.319 1.00 31.81 ? 163 TRP D CA  1 
ATOM   6832 C C   . TRP D 1 163 ? 35.853  28.755  -31.234 1.00 30.45 ? 163 TRP D C   1 
ATOM   6833 O O   . TRP D 1 163 ? 35.516  28.466  -32.388 1.00 28.70 ? 163 TRP D O   1 
ATOM   6834 C CB  . TRP D 1 163 ? 34.422  28.768  -29.126 1.00 29.21 ? 163 TRP D CB  1 
ATOM   6835 C CG  . TRP D 1 163 ? 33.987  27.328  -29.342 1.00 30.89 ? 163 TRP D CG  1 
ATOM   6836 C CD1 . TRP D 1 163 ? 34.671  26.211  -28.971 1.00 30.99 ? 163 TRP D CD1 1 
ATOM   6837 C CD2 . TRP D 1 163 ? 32.747  26.864  -29.917 1.00 32.06 ? 163 TRP D CD2 1 
ATOM   6838 N NE1 . TRP D 1 163 ? 33.952  25.077  -29.285 1.00 30.41 ? 163 TRP D NE1 1 
ATOM   6839 C CE2 . TRP D 1 163 ? 32.773  25.447  -29.875 1.00 30.41 ? 163 TRP D CE2 1 
ATOM   6840 C CE3 . TRP D 1 163 ? 31.627  27.505  -30.468 1.00 30.22 ? 163 TRP D CE3 1 
ATOM   6841 C CZ2 . TRP D 1 163 ? 31.721  24.660  -30.353 1.00 30.20 ? 163 TRP D CZ2 1 
ATOM   6842 C CZ3 . TRP D 1 163 ? 30.577  26.717  -30.950 1.00 30.13 ? 163 TRP D CZ3 1 
ATOM   6843 C CH2 . TRP D 1 163 ? 30.631  25.308  -30.882 1.00 28.97 ? 163 TRP D CH2 1 
ATOM   6844 N N   . GLN D 1 164 ? 37.035  28.456  -30.720 1.00 31.64 ? 164 GLN D N   1 
ATOM   6845 C CA  . GLN D 1 164 ? 38.012  27.623  -31.406 1.00 31.96 ? 164 GLN D CA  1 
ATOM   6846 C C   . GLN D 1 164 ? 37.881  26.225  -30.824 1.00 34.86 ? 164 GLN D C   1 
ATOM   6847 O O   . GLN D 1 164 ? 38.167  26.017  -29.640 1.00 35.48 ? 164 GLN D O   1 
ATOM   6848 C CB  . GLN D 1 164 ? 39.429  28.164  -31.218 1.00 36.39 ? 164 GLN D CB  1 
ATOM   6849 C CG  . GLN D 1 164 ? 39.576  29.664  -31.493 1.00 36.21 ? 164 GLN D CG  1 
ATOM   6850 C CD  . GLN D 1 164 ? 39.165  30.090  -32.903 1.00 35.63 ? 164 GLN D CD  1 
ATOM   6851 O OE1 . GLN D 1 164 ? 39.661  29.562  -33.896 1.00 35.99 ? 164 GLN D OE1 1 
ATOM   6852 N NE2 . GLN D 1 164 ? 38.262  31.065  -32.990 1.00 34.24 ? 164 GLN D NE2 1 
ATOM   6853 N N   . VAL D 1 165 ? 37.448  25.271  -31.654 1.00 33.75 ? 165 VAL D N   1 
ATOM   6854 C CA  . VAL D 1 165 ? 37.083  23.954  -31.142 1.00 34.31 ? 165 VAL D CA  1 
ATOM   6855 C C   . VAL D 1 165 ? 38.290  23.264  -30.513 1.00 36.01 ? 165 VAL D C   1 
ATOM   6856 O O   . VAL D 1 165 ? 38.147  22.492  -29.555 1.00 35.62 ? 165 VAL D O   1 
ATOM   6857 C CB  . VAL D 1 165 ? 36.442  23.119  -32.267 1.00 33.21 ? 165 VAL D CB  1 
ATOM   6858 C CG1 . VAL D 1 165 ? 35.160  23.776  -32.769 1.00 26.85 ? 165 VAL D CG1 1 
ATOM   6859 C CG2 . VAL D 1 165 ? 37.408  22.968  -33.424 1.00 33.81 ? 165 VAL D CG2 1 
ATOM   6860 N N   . ASN D 1 166 ? 39.499  23.552  -31.009 1.00 38.48 ? 166 ASN D N   1 
ATOM   6861 C CA  . ASN D 1 166 ? 40.691  22.971  -30.398 1.00 36.57 ? 166 ASN D CA  1 
ATOM   6862 C C   . ASN D 1 166 ? 40.870  23.446  -28.966 1.00 38.54 ? 166 ASN D C   1 
ATOM   6863 O O   . ASN D 1 166 ? 41.439  22.724  -28.140 1.00 38.92 ? 166 ASN D O   1 
ATOM   6864 C CB  . ASN D 1 166 ? 41.936  23.327  -31.207 1.00 37.93 ? 166 ASN D CB  1 
ATOM   6865 C CG  . ASN D 1 166 ? 41.912  24.749  -31.698 1.00 40.81 ? 166 ASN D CG  1 
ATOM   6866 O OD1 . ASN D 1 166 ? 41.092  25.119  -32.552 1.00 40.94 ? 166 ASN D OD1 1 
ATOM   6867 N ND2 . ASN D 1 166 ? 42.782  25.573  -31.136 1.00 39.96 ? 166 ASN D ND2 1 
ATOM   6868 N N   . GLN D 1 167 ? 40.399  24.652  -28.651 1.00 36.24 ? 167 GLN D N   1 
ATOM   6869 C CA  . GLN D 1 167 ? 40.502  25.170  -27.298 1.00 35.85 ? 167 GLN D CA  1 
ATOM   6870 C C   . GLN D 1 167 ? 39.473  24.572  -26.355 1.00 37.31 ? 167 GLN D C   1 
ATOM   6871 O O   . GLN D 1 167 ? 39.529  24.858  -25.152 1.00 40.83 ? 167 GLN D O   1 
ATOM   6872 C CB  . GLN D 1 167 ? 40.391  26.696  -27.323 1.00 35.55 ? 167 GLN D CB  1 
ATOM   6873 C CG  . GLN D 1 167 ? 41.526  27.362  -28.133 1.00 36.85 ? 167 GLN D CG  1 
ATOM   6874 C CD  . GLN D 1 167 ? 41.593  28.832  -27.860 1.00 37.44 ? 167 GLN D CD  1 
ATOM   6875 O OE1 . GLN D 1 167 ? 41.212  29.272  -26.776 1.00 39.10 ? 167 GLN D OE1 1 
ATOM   6876 N NE2 . GLN D 1 167 ? 42.050  29.612  -28.838 1.00 36.62 ? 167 GLN D NE2 1 
ATOM   6877 N N   . SER D 1 168 ? 38.531  23.765  -26.862 1.00 36.90 ? 168 SER D N   1 
ATOM   6878 C CA  . SER D 1 168 ? 37.549  23.079  -26.027 1.00 36.72 ? 168 SER D CA  1 
ATOM   6879 C C   . SER D 1 168 ? 37.797  21.575  -26.009 1.00 40.29 ? 168 SER D C   1 
ATOM   6880 O O   . SER D 1 168 ? 36.941  20.800  -25.573 1.00 40.76 ? 168 SER D O   1 
ATOM   6881 C CB  . SER D 1 168 ? 36.117  23.396  -26.484 1.00 37.35 ? 168 SER D CB  1 
ATOM   6882 O OG  . SER D 1 168 ? 35.829  22.901  -27.790 1.00 34.33 ? 168 SER D OG  1 
ATOM   6883 N N   . ARG D 1 169 ? 38.975  21.150  -26.454 1.00 41.19 ? 169 ARG D N   1 
ATOM   6884 C CA  . ARG D 1 169 ? 39.224  19.724  -26.634 1.00 40.49 ? 169 ARG D CA  1 
ATOM   6885 C C   . ARG D 1 169 ? 39.242  18.967  -25.313 1.00 39.16 ? 169 ARG D C   1 
ATOM   6886 O O   . ARG D 1 169 ? 38.774  17.826  -25.249 1.00 45.06 ? 169 ARG D O   1 
ATOM   6887 C CB  . ARG D 1 169 ? 40.538  19.526  -27.389 1.00 37.74 ? 169 ARG D CB  1 
ATOM   6888 C CG  . ARG D 1 169 ? 41.108  18.126  -27.292 1.00 43.78 ? 169 ARG D CG  1 
ATOM   6889 C CD  . ARG D 1 169 ? 40.341  17.125  -28.098 1.00 42.36 ? 169 ARG D CD  1 
ATOM   6890 N NE  . ARG D 1 169 ? 41.209  16.190  -28.816 1.00 49.92 ? 169 ARG D NE  1 
ATOM   6891 C CZ  . ARG D 1 169 ? 41.471  14.949  -28.425 1.00 49.55 ? 169 ARG D CZ  1 
ATOM   6892 N NH1 . ARG D 1 169 ? 40.868  14.411  -27.374 1.00 51.73 ? 169 ARG D NH1 1 
ATOM   6893 N NH2 . ARG D 1 169 ? 42.308  14.206  -29.147 1.00 51.54 ? 169 ARG D NH2 1 
ATOM   6894 N N   . ASN D 1 170 ? 39.793  19.556  -24.253 1.00 41.70 ? 170 ASN D N   1 
ATOM   6895 C CA  . ASN D 1 170 ? 39.879  18.828  -22.989 1.00 43.83 ? 170 ASN D CA  1 
ATOM   6896 C C   . ASN D 1 170 ? 38.662  19.002  -22.089 1.00 45.06 ? 170 ASN D C   1 
ATOM   6897 O O   . ASN D 1 170 ? 38.339  18.088  -21.318 1.00 47.87 ? 170 ASN D O   1 
ATOM   6898 C CB  . ASN D 1 170 ? 41.141  19.230  -22.232 1.00 44.22 ? 170 ASN D CB  1 
ATOM   6899 C CG  . ASN D 1 170 ? 42.394  18.698  -22.901 1.00 48.93 ? 170 ASN D CG  1 
ATOM   6900 O OD1 . ASN D 1 170 ? 42.502  17.500  -23.198 1.00 52.64 ? 170 ASN D OD1 1 
ATOM   6901 N ND2 . ASN D 1 170 ? 43.350  19.583  -23.138 1.00 47.55 ? 170 ASN D ND2 1 
ATOM   6902 N N   . CYS D 1 171 ? 37.978  20.140  -22.165 1.00 42.26 ? 171 CYS D N   1 
ATOM   6903 C CA  . CYS D 1 171 ? 36.831  20.396  -21.303 1.00 43.30 ? 171 CYS D CA  1 
ATOM   6904 C C   . CYS D 1 171 ? 35.503  20.033  -21.949 1.00 41.49 ? 171 CYS D C   1 
ATOM   6905 O O   . CYS D 1 171 ? 34.491  19.987  -21.253 1.00 47.97 ? 171 CYS D O   1 
ATOM   6906 C CB  . CYS D 1 171 ? 36.824  21.860  -20.846 1.00 42.74 ? 171 CYS D CB  1 
ATOM   6907 S SG  . CYS D 1 171 ? 36.886  23.089  -22.143 1.00 44.97 ? 171 CYS D SG  1 
ATOM   6908 N N   . LYS D 1 172 ? 35.495  19.682  -23.225 1.00 42.18 ? 172 LYS D N   1 
ATOM   6909 C CA  . LYS D 1 172 ? 34.275  19.246  -23.889 1.00 40.52 ? 172 LYS D CA  1 
ATOM   6910 C C   . LYS D 1 172 ? 34.583  18.040  -24.767 1.00 38.39 ? 172 LYS D C   1 
ATOM   6911 O O   . LYS D 1 172 ? 33.992  16.970  -24.584 1.00 38.42 ? 172 LYS D O   1 
ATOM   6912 C CB  . LYS D 1 172 ? 33.690  20.393  -24.719 1.00 39.32 ? 172 LYS D CB  1 
ATOM   6913 C CG  . LYS D 1 172 ? 32.475  20.024  -25.560 1.00 40.71 ? 172 LYS D CG  1 
ATOM   6914 C CD  . LYS D 1 172 ? 31.241  19.775  -24.732 1.00 38.24 ? 172 LYS D CD  1 
ATOM   6915 C CE  . LYS D 1 172 ? 30.423  18.653  -25.357 1.00 37.50 ? 172 LYS D CE  1 
ATOM   6916 N NZ  . LYS D 1 172 ? 29.125  18.474  -24.671 1.00 41.61 ? 172 LYS D NZ  1 
ATOM   6917 N N   . GLY D 1 173 ? 35.495  18.201  -25.717 1.00 38.52 ? 173 GLY D N   1 
ATOM   6918 C CA  . GLY D 1 173 ? 35.962  17.086  -26.525 1.00 40.47 ? 173 GLY D CA  1 
ATOM   6919 C C   . GLY D 1 173 ? 35.071  16.609  -27.651 1.00 39.68 ? 173 GLY D C   1 
ATOM   6920 O O   . GLY D 1 173 ? 35.219  15.468  -28.086 1.00 41.84 ? 173 GLY D O   1 
ATOM   6921 N N   . ASP D 1 174 ? 34.158  17.445  -28.158 1.00 39.34 ? 174 ASP D N   1 
ATOM   6922 C CA  . ASP D 1 174 ? 33.414  17.060  -29.353 1.00 35.25 ? 174 ASP D CA  1 
ATOM   6923 C C   . ASP D 1 174 ? 34.323  17.033  -30.585 1.00 33.70 ? 174 ASP D C   1 
ATOM   6924 O O   . ASP D 1 174 ? 34.074  16.276  -31.529 1.00 34.53 ? 174 ASP D O   1 
ATOM   6925 C CB  . ASP D 1 174 ? 32.245  18.019  -29.600 1.00 33.91 ? 174 ASP D CB  1 
ATOM   6926 C CG  . ASP D 1 174 ? 30.981  17.661  -28.810 1.00 36.50 ? 174 ASP D CG  1 
ATOM   6927 O OD1 . ASP D 1 174 ? 30.977  16.704  -28.006 1.00 38.78 ? 174 ASP D OD1 1 
ATOM   6928 O OD2 . ASP D 1 174 ? 29.960  18.350  -29.019 1.00 37.15 ? 174 ASP D OD2 1 
ATOM   6929 N N   . TYR D 1 175 ? 35.378  17.839  -30.605 1.00 33.69 ? 175 TYR D N   1 
ATOM   6930 C CA  . TYR D 1 175 ? 36.158  18.035  -31.820 1.00 34.65 ? 175 TYR D CA  1 
ATOM   6931 C C   . TYR D 1 175 ? 37.617  17.676  -31.596 1.00 38.12 ? 175 TYR D C   1 
ATOM   6932 O O   . TYR D 1 175 ? 38.179  17.926  -30.521 1.00 36.09 ? 175 TYR D O   1 
ATOM   6933 C CB  . TYR D 1 175 ? 36.070  19.465  -32.310 1.00 33.12 ? 175 TYR D CB  1 
ATOM   6934 C CG  . TYR D 1 175 ? 34.695  19.882  -32.765 1.00 34.61 ? 175 TYR D CG  1 
ATOM   6935 C CD1 . TYR D 1 175 ? 34.284  19.654  -34.071 1.00 35.67 ? 175 TYR D CD1 1 
ATOM   6936 C CD2 . TYR D 1 175 ? 33.802  20.499  -31.890 1.00 34.42 ? 175 TYR D CD2 1 
ATOM   6937 C CE1 . TYR D 1 175 ? 33.028  20.035  -34.503 1.00 35.05 ? 175 TYR D CE1 1 
ATOM   6938 C CE2 . TYR D 1 175 ? 32.537  20.892  -32.321 1.00 32.58 ? 175 TYR D CE2 1 
ATOM   6939 C CZ  . TYR D 1 175 ? 32.160  20.651  -33.634 1.00 32.48 ? 175 TYR D CZ  1 
ATOM   6940 O OH  . TYR D 1 175 ? 30.926  21.018  -34.103 1.00 31.06 ? 175 TYR D OH  1 
ATOM   6941 N N   . THR D 1 176 ? 38.253  17.132  -32.622 1.00 36.04 ? 176 THR D N   1 
ATOM   6942 C CA  . THR D 1 176 ? 39.687  16.792  -32.489 1.00 36.50 ? 176 THR D CA  1 
ATOM   6943 C C   . THR D 1 176 ? 40.512  17.723  -33.370 1.00 37.73 ? 176 THR D C   1 
ATOM   6944 O O   . THR D 1 176 ? 41.709  17.737  -33.223 1.00 38.95 ? 176 THR D O   1 
ATOM   6945 C CB  . THR D 1 176 ? 39.943  15.335  -32.883 1.00 37.36 ? 176 THR D CB  1 
ATOM   6946 O OG1 . THR D 1 176 ? 39.491  15.144  -34.217 1.00 33.25 ? 176 THR D OG1 1 
ATOM   6947 C CG2 . THR D 1 176 ? 39.293  14.355  -31.937 1.00 35.93 ? 176 THR D CG2 1 
ATOM   6948 N N   . GLY D 1 177 ? 39.850  18.494  -34.218 1.00 39.30 ? 177 GLY D N   1 
ATOM   6949 C CA  . GLY D 1 177 ? 40.534  19.368  -35.178 1.00 40.17 ? 177 GLY D CA  1 
ATOM   6950 C C   . GLY D 1 177 ? 40.726  20.787  -34.702 1.00 38.86 ? 177 GLY D C   1 
ATOM   6951 O O   . GLY D 1 177 ? 40.389  21.081  -33.584 1.00 45.34 ? 177 GLY D O   1 
ATOM   6952 N N   . ASN D 1 178 ? 41.221  21.618  -35.614 1.00 45.32 ? 178 ASN D N   1 
ATOM   6953 C CA  . ASN D 1 178 ? 41.572  23.040  -35.400 1.00 38.66 ? 178 ASN D CA  1 
ATOM   6954 C C   . ASN D 1 178 ? 40.890  23.914  -36.449 1.00 39.44 ? 178 ASN D C   1 
ATOM   6955 O O   . ASN D 1 178 ? 41.311  23.884  -37.582 1.00 39.64 ? 178 ASN D O   1 
ATOM   6956 C CB  . ASN D 1 178 ? 43.079  23.216  -35.517 1.00 42.13 ? 178 ASN D CB  1 
ATOM   6957 C CG  . ASN D 1 178 ? 43.791  22.649  -34.316 1.00 47.61 ? 178 ASN D CG  1 
ATOM   6958 O OD1 . ASN D 1 178 ? 43.854  21.442  -34.148 1.00 50.38 ? 178 ASN D OD1 1 
ATOM   6959 N ND2 . ASN D 1 178 ? 44.280  23.514  -33.450 1.00 54.52 ? 178 ASN D ND2 1 
ATOM   6960 N N   . PHE D 1 179 ? 39.872  24.662  -36.030 1.00 35.72 ? 179 PHE D N   1 
ATOM   6961 C CA  . PHE D 1 179 ? 39.092  25.594  -36.832 1.00 30.78 ? 179 PHE D CA  1 
ATOM   6962 C C   . PHE D 1 179 ? 38.224  26.404  -35.865 1.00 30.46 ? 179 PHE D C   1 
ATOM   6963 O O   . PHE D 1 179 ? 37.889  25.943  -34.767 1.00 31.73 ? 179 PHE D O   1 
ATOM   6964 C CB  . PHE D 1 179 ? 38.251  24.903  -37.918 1.00 31.47 ? 179 PHE D CB  1 
ATOM   6965 C CG  . PHE D 1 179 ? 37.295  23.856  -37.404 1.00 33.59 ? 179 PHE D CG  1 
ATOM   6966 C CD1 . PHE D 1 179 ? 37.721  22.553  -37.198 1.00 37.02 ? 179 PHE D CD1 1 
ATOM   6967 C CD2 . PHE D 1 179 ? 35.981  24.172  -37.131 1.00 34.78 ? 179 PHE D CD2 1 
ATOM   6968 C CE1 . PHE D 1 179 ? 36.833  21.570  -36.750 1.00 37.03 ? 179 PHE D CE1 1 
ATOM   6969 C CE2 . PHE D 1 179 ? 35.090  23.210  -36.666 1.00 34.15 ? 179 PHE D CE2 1 
ATOM   6970 C CZ  . PHE D 1 179 ? 35.513  21.914  -36.467 1.00 32.71 ? 179 PHE D CZ  1 
ATOM   6971 N N   . GLY D 1 180 ? 37.895  27.622  -36.273 1.00 28.27 ? 180 GLY D N   1 
ATOM   6972 C CA  . GLY D 1 180 ? 36.937  28.409  -35.535 1.00 30.13 ? 180 GLY D CA  1 
ATOM   6973 C C   . GLY D 1 180 ? 35.528  27.998  -35.901 1.00 29.96 ? 180 GLY D C   1 
ATOM   6974 O O   . GLY D 1 180 ? 35.266  27.548  -37.015 1.00 29.78 ? 180 GLY D O   1 
ATOM   6975 N N   . HIS D 1 181 ? 34.604  28.167  -34.958 1.00 28.20 ? 181 HIS D N   1 
ATOM   6976 C CA  . HIS D 1 181 ? 33.284  27.589  -35.126 1.00 26.76 ? 181 HIS D CA  1 
ATOM   6977 C C   . HIS D 1 181 ? 32.247  28.460  -34.439 1.00 26.00 ? 181 HIS D C   1 
ATOM   6978 O O   . HIS D 1 181 ? 32.568  29.281  -33.574 1.00 28.43 ? 181 HIS D O   1 
ATOM   6979 C CB  . HIS D 1 181 ? 33.270  26.158  -34.562 1.00 26.84 ? 181 HIS D CB  1 
ATOM   6980 C CG  . HIS D 1 181 ? 32.088  25.341  -34.974 1.00 25.89 ? 181 HIS D CG  1 
ATOM   6981 N ND1 . HIS D 1 181 ? 31.624  25.294  -36.271 1.00 24.89 ? 181 HIS D ND1 1 
ATOM   6982 C CD2 . HIS D 1 181 ? 31.301  24.503  -34.261 1.00 25.88 ? 181 HIS D CD2 1 
ATOM   6983 C CE1 . HIS D 1 181 ? 30.596  24.465  -36.335 1.00 29.44 ? 181 HIS D CE1 1 
ATOM   6984 N NE2 . HIS D 1 181 ? 30.375  23.980  -35.127 1.00 26.55 ? 181 HIS D NE2 1 
ATOM   6985 N N   . TYR D 1 182 ? 30.981  28.283  -34.840 1.00 27.58 ? 182 TYR D N   1 
ATOM   6986 C CA  . TYR D 1 182 ? 29.872  29.006  -34.233 1.00 25.56 ? 182 TYR D CA  1 
ATOM   6987 C C   . TYR D 1 182 ? 28.756  28.028  -33.876 1.00 28.41 ? 182 TYR D C   1 
ATOM   6988 O O   . TYR D 1 182 ? 28.531  27.045  -34.585 1.00 24.49 ? 182 TYR D O   1 
ATOM   6989 C CB  . TYR D 1 182 ? 29.241  30.071  -35.164 1.00 29.50 ? 182 TYR D CB  1 
ATOM   6990 C CG  . TYR D 1 182 ? 30.105  31.252  -35.595 1.00 27.12 ? 182 TYR D CG  1 
ATOM   6991 C CD1 . TYR D 1 182 ? 31.001  31.128  -36.636 1.00 29.32 ? 182 TYR D CD1 1 
ATOM   6992 C CD2 . TYR D 1 182 ? 29.976  32.494  -34.985 1.00 29.19 ? 182 TYR D CD2 1 
ATOM   6993 C CE1 . TYR D 1 182 ? 31.774  32.192  -37.059 1.00 31.07 ? 182 TYR D CE1 1 
ATOM   6994 C CE2 . TYR D 1 182 ? 30.755  33.580  -35.401 1.00 30.38 ? 182 TYR D CE2 1 
ATOM   6995 C CZ  . TYR D 1 182 ? 31.657  33.411  -36.432 1.00 32.14 ? 182 TYR D CZ  1 
ATOM   6996 O OH  . TYR D 1 182 ? 32.424  34.474  -36.866 1.00 29.46 ? 182 TYR D OH  1 
ATOM   6997 N N   . GLY D 1 183 ? 28.007  28.371  -32.824 1.00 25.57 ? 183 GLY D N   1 
ATOM   6998 C CA  . GLY D 1 183 ? 26.803  27.679  -32.416 1.00 23.25 ? 183 GLY D CA  1 
ATOM   6999 C C   . GLY D 1 183 ? 25.829  28.689  -31.828 1.00 28.09 ? 183 GLY D C   1 
ATOM   7000 O O   . GLY D 1 183 ? 26.108  29.892  -31.776 1.00 29.42 ? 183 GLY D O   1 
ATOM   7001 N N   . LEU D 1 184 ? 24.682  28.185  -31.367 1.00 25.01 ? 184 LEU D N   1 
ATOM   7002 C CA  . LEU D 1 184 ? 23.617  29.000  -30.773 1.00 25.36 ? 184 LEU D CA  1 
ATOM   7003 C C   . LEU D 1 184 ? 23.360  28.556  -29.339 1.00 26.91 ? 184 LEU D C   1 
ATOM   7004 O O   . LEU D 1 184 ? 22.863  27.447  -29.105 1.00 26.54 ? 184 LEU D O   1 
ATOM   7005 C CB  . LEU D 1 184 ? 22.325  28.891  -31.591 1.00 23.58 ? 184 LEU D CB  1 
ATOM   7006 C CG  . LEU D 1 184 ? 21.206  29.855  -31.161 1.00 24.86 ? 184 LEU D CG  1 
ATOM   7007 C CD1 . LEU D 1 184 ? 21.590  31.265  -31.462 1.00 24.75 ? 184 LEU D CD1 1 
ATOM   7008 C CD2 . LEU D 1 184 ? 19.881  29.514  -31.862 1.00 26.82 ? 184 LEU D CD2 1 
ATOM   7009 N N   . ILE D 1 185 ? 23.665  29.416  -28.371 1.00 26.77 ? 185 ILE D N   1 
ATOM   7010 C CA  . ILE D 1 185 ? 23.242  29.151  -26.999 1.00 28.57 ? 185 ILE D CA  1 
ATOM   7011 C C   . ILE D 1 185 ? 21.752  29.482  -26.911 1.00 30.80 ? 185 ILE D C   1 
ATOM   7012 O O   . ILE D 1 185 ? 21.357  30.634  -27.098 1.00 28.72 ? 185 ILE D O   1 
ATOM   7013 C CB  . ILE D 1 185 ? 24.043  29.958  -25.974 1.00 29.30 ? 185 ILE D CB  1 
ATOM   7014 C CG1 . ILE D 1 185 ? 25.545  29.733  -26.146 1.00 30.79 ? 185 ILE D CG1 1 
ATOM   7015 C CG2 . ILE D 1 185 ? 23.630  29.536  -24.566 1.00 27.94 ? 185 ILE D CG2 1 
ATOM   7016 C CD1 . ILE D 1 185 ? 26.381  30.782  -25.403 1.00 33.07 ? 185 ILE D CD1 1 
ATOM   7017 N N   . TRP D 1 186 ? 20.916  28.477  -26.676 1.00 26.88 ? 186 TRP D N   1 
ATOM   7018 C CA  . TRP D 1 186 ? 19.488  28.730  -26.549 1.00 31.60 ? 186 TRP D CA  1 
ATOM   7019 C C   . TRP D 1 186 ? 18.946  28.396  -25.169 1.00 33.58 ? 186 TRP D C   1 
ATOM   7020 O O   . TRP D 1 186 ? 17.773  28.672  -24.900 1.00 31.97 ? 186 TRP D O   1 
ATOM   7021 C CB  . TRP D 1 186 ? 18.707  27.963  -27.632 1.00 31.52 ? 186 TRP D CB  1 
ATOM   7022 C CG  . TRP D 1 186 ? 18.915  26.504  -27.612 1.00 28.87 ? 186 TRP D CG  1 
ATOM   7023 C CD1 . TRP D 1 186 ? 19.934  25.805  -28.200 1.00 27.90 ? 186 TRP D CD1 1 
ATOM   7024 C CD2 . TRP D 1 186 ? 18.068  25.538  -26.990 1.00 33.27 ? 186 TRP D CD2 1 
ATOM   7025 N NE1 . TRP D 1 186 ? 19.782  24.462  -27.958 1.00 32.53 ? 186 TRP D NE1 1 
ATOM   7026 C CE2 . TRP D 1 186 ? 18.639  24.274  -27.216 1.00 31.99 ? 186 TRP D CE2 1 
ATOM   7027 C CE3 . TRP D 1 186 ? 16.881  25.622  -26.256 1.00 32.92 ? 186 TRP D CE3 1 
ATOM   7028 C CZ2 . TRP D 1 186 ? 18.061  23.106  -26.737 1.00 31.72 ? 186 TRP D CZ2 1 
ATOM   7029 C CZ3 . TRP D 1 186 ? 16.309  24.461  -25.785 1.00 34.06 ? 186 TRP D CZ3 1 
ATOM   7030 C CH2 . TRP D 1 186 ? 16.899  23.221  -26.027 1.00 33.48 ? 186 TRP D CH2 1 
ATOM   7031 N N   . ASP D 1 187 ? 19.768  27.848  -24.274 1.00 33.67 ? 187 ASP D N   1 
ATOM   7032 C CA  . ASP D 1 187 ? 19.315  27.524  -22.923 1.00 35.00 ? 187 ASP D CA  1 
ATOM   7033 C C   . ASP D 1 187 ? 20.543  27.383  -22.027 1.00 38.83 ? 187 ASP D C   1 
ATOM   7034 O O   . ASP D 1 187 ? 21.688  27.355  -22.496 1.00 35.09 ? 187 ASP D O   1 
ATOM   7035 C CB  . ASP D 1 187 ? 18.441  26.258  -22.917 1.00 34.29 ? 187 ASP D CB  1 
ATOM   7036 C CG  . ASP D 1 187 ? 17.557  26.148  -21.667 1.00 39.45 ? 187 ASP D CG  1 
ATOM   7037 O OD1 . ASP D 1 187 ? 17.506  27.105  -20.865 1.00 38.60 ? 187 ASP D OD1 1 
ATOM   7038 O OD2 . ASP D 1 187 ? 16.855  25.128  -21.535 1.00 37.83 ? 187 ASP D OD2 1 
ATOM   7039 N N   . MET D 1 188 ? 20.287  27.277  -20.721 1.00 42.16 ? 188 MET D N   1 
ATOM   7040 C CA  . MET D 1 188 ? 21.346  27.188  -19.723 1.00 41.40 ? 188 MET D CA  1 
ATOM   7041 C C   . MET D 1 188 ? 20.881  26.281  -18.598 1.00 41.18 ? 188 MET D C   1 
ATOM   7042 O O   . MET D 1 188 ? 19.704  26.293  -18.256 1.00 44.03 ? 188 MET D O   1 
ATOM   7043 C CB  . MET D 1 188 ? 21.658  28.564  -19.121 1.00 37.16 ? 188 MET D CB  1 
ATOM   7044 C CG  . MET D 1 188 ? 22.878  29.272  -19.660 1.00 41.47 ? 188 MET D CG  1 
ATOM   7045 S SD  . MET D 1 188 ? 22.850  31.038  -19.195 1.00 40.82 ? 188 MET D SD  1 
ATOM   7046 C CE  . MET D 1 188 ? 23.675  30.951  -17.615 1.00 38.65 ? 188 MET D CE  1 
ATOM   7047 N N   . THR D 1 189 ? 21.798  25.516  -18.021 1.00 41.65 ? 189 THR D N   1 
ATOM   7048 C CA  . THR D 1 189 ? 21.587  24.908  -16.716 1.00 42.28 ? 189 THR D CA  1 
ATOM   7049 C C   . THR D 1 189 ? 22.263  25.775  -15.655 1.00 45.54 ? 189 THR D C   1 
ATOM   7050 O O   . THR D 1 189 ? 22.664  26.919  -15.910 1.00 45.84 ? 189 THR D O   1 
ATOM   7051 C CB  . THR D 1 189 ? 22.115  23.470  -16.674 1.00 40.91 ? 189 THR D CB  1 
ATOM   7052 O OG1 . THR D 1 189 ? 23.545  23.477  -16.616 1.00 44.28 ? 189 THR D OG1 1 
ATOM   7053 C CG2 . THR D 1 189 ? 21.658  22.692  -17.885 1.00 39.93 ? 189 THR D CG2 1 
ATOM   7054 N N   . SER D 1 190 ? 22.408  25.234  -14.444 1.00 45.89 ? 190 SER D N   1 
ATOM   7055 C CA  . SER D 1 190 ? 23.170  25.951  -13.424 1.00 44.63 ? 190 SER D CA  1 
ATOM   7056 C C   . SER D 1 190 ? 24.668  25.940  -13.707 1.00 45.03 ? 190 SER D C   1 
ATOM   7057 O O   . SER D 1 190 ? 25.411  26.735  -13.119 1.00 46.88 ? 190 SER D O   1 
ATOM   7058 C CB  . SER D 1 190 ? 22.913  25.339  -12.049 1.00 47.41 ? 190 SER D CB  1 
ATOM   7059 O OG  . SER D 1 190 ? 22.754  23.935  -12.165 1.00 49.00 ? 190 SER D OG  1 
ATOM   7060 N N   . THR D 1 191 ? 25.137  25.053  -14.580 1.00 40.77 ? 191 THR D N   1 
ATOM   7061 C CA  . THR D 1 191 ? 26.563  24.906  -14.829 1.00 42.88 ? 191 THR D CA  1 
ATOM   7062 C C   . THR D 1 191 ? 26.962  24.943  -16.299 1.00 41.19 ? 191 THR D C   1 
ATOM   7063 O O   . THR D 1 191 ? 28.123  25.258  -16.587 1.00 42.46 ? 191 THR D O   1 
ATOM   7064 C CB  . THR D 1 191 ? 27.075  23.595  -14.212 1.00 43.38 ? 191 THR D CB  1 
ATOM   7065 O OG1 . THR D 1 191 ? 26.436  22.490  -14.862 1.00 41.84 ? 191 THR D OG1 1 
ATOM   7066 C CG2 . THR D 1 191 ? 26.803  23.547  -12.702 1.00 47.11 ? 191 THR D CG2 1 
ATOM   7067 N N   . HIS D 1 192 ? 26.059  24.636  -17.232 1.00 40.89 ? 192 HIS D N   1 
ATOM   7068 C CA  . HIS D 1 192 ? 26.405  24.474  -18.637 1.00 39.35 ? 192 HIS D CA  1 
ATOM   7069 C C   . HIS D 1 192 ? 25.548  25.358  -19.535 1.00 41.49 ? 192 HIS D C   1 
ATOM   7070 O O   . HIS D 1 192 ? 24.359  25.567  -19.265 1.00 37.80 ? 192 HIS D O   1 
ATOM   7071 C CB  . HIS D 1 192 ? 26.243  23.021  -19.110 1.00 39.17 ? 192 HIS D CB  1 
ATOM   7072 C CG  . HIS D 1 192 ? 27.194  22.060  -18.469 1.00 43.09 ? 192 HIS D CG  1 
ATOM   7073 N ND1 . HIS D 1 192 ? 27.389  22.004  -17.107 1.00 44.86 ? 192 HIS D ND1 1 
ATOM   7074 C CD2 . HIS D 1 192 ? 28.012  21.122  -19.007 1.00 43.47 ? 192 HIS D CD2 1 
ATOM   7075 C CE1 . HIS D 1 192 ? 28.277  21.062  -16.833 1.00 45.69 ? 192 HIS D CE1 1 
ATOM   7076 N NE2 . HIS D 1 192 ? 28.678  20.519  -17.969 1.00 42.58 ? 192 HIS D NE2 1 
ATOM   7077 N N   . TYR D 1 193 ? 26.163  25.872  -20.606 1.00 36.69 ? 193 TYR D N   1 
ATOM   7078 C CA  . TYR D 1 193 ? 25.408  26.377  -21.741 1.00 34.79 ? 193 TYR D CA  1 
ATOM   7079 C C   . TYR D 1 193 ? 24.870  25.208  -22.545 1.00 35.25 ? 193 TYR D C   1 
ATOM   7080 O O   . TYR D 1 193 ? 25.552  24.190  -22.703 1.00 34.33 ? 193 TYR D O   1 
ATOM   7081 C CB  . TYR D 1 193 ? 26.267  27.228  -22.673 1.00 34.21 ? 193 TYR D CB  1 
ATOM   7082 C CG  . TYR D 1 193 ? 26.930  28.436  -22.061 1.00 35.16 ? 193 TYR D CG  1 
ATOM   7083 C CD1 . TYR D 1 193 ? 26.180  29.478  -21.527 1.00 35.29 ? 193 TYR D CD1 1 
ATOM   7084 C CD2 . TYR D 1 193 ? 28.311  28.563  -22.087 1.00 35.77 ? 193 TYR D CD2 1 
ATOM   7085 C CE1 . TYR D 1 193 ? 26.793  30.588  -20.991 1.00 36.11 ? 193 TYR D CE1 1 
ATOM   7086 C CE2 . TYR D 1 193 ? 28.933  29.664  -21.567 1.00 36.59 ? 193 TYR D CE2 1 
ATOM   7087 C CZ  . TYR D 1 193 ? 28.168  30.670  -21.013 1.00 36.75 ? 193 TYR D CZ  1 
ATOM   7088 O OH  . TYR D 1 193 ? 28.798  31.760  -20.499 1.00 37.36 ? 193 TYR D OH  1 
ATOM   7089 N N   . VAL D 1 194 ? 23.656  25.371  -23.073 1.00 32.44 ? 194 VAL D N   1 
ATOM   7090 C CA  . VAL D 1 194 ? 23.059  24.425  -24.006 1.00 29.74 ? 194 VAL D CA  1 
ATOM   7091 C C   . VAL D 1 194 ? 23.186  25.014  -25.404 1.00 32.80 ? 194 VAL D C   1 
ATOM   7092 O O   . VAL D 1 194 ? 22.538  26.018  -25.727 1.00 29.88 ? 194 VAL D O   1 
ATOM   7093 C CB  . VAL D 1 194 ? 21.596  24.128  -23.666 1.00 32.95 ? 194 VAL D CB  1 
ATOM   7094 C CG1 . VAL D 1 194 ? 21.088  23.013  -24.554 1.00 31.32 ? 194 VAL D CG1 1 
ATOM   7095 C CG2 . VAL D 1 194 ? 21.460  23.771  -22.201 1.00 31.30 ? 194 VAL D CG2 1 
ATOM   7096 N N   . VAL D 1 195 ? 24.009  24.376  -26.238 1.00 31.43 ? 195 VAL D N   1 
ATOM   7097 C CA  . VAL D 1 195 ? 24.435  24.916  -27.529 1.00 27.82 ? 195 VAL D CA  1 
ATOM   7098 C C   . VAL D 1 195 ? 23.852  24.076  -28.649 1.00 29.22 ? 195 VAL D C   1 
ATOM   7099 O O   . VAL D 1 195 ? 24.140  22.870  -28.748 1.00 33.36 ? 195 VAL D O   1 
ATOM   7100 C CB  . VAL D 1 195 ? 25.969  24.941  -27.652 1.00 28.71 ? 195 VAL D CB  1 
ATOM   7101 C CG1 . VAL D 1 195 ? 26.384  25.348  -29.070 1.00 25.64 ? 195 VAL D CG1 1 
ATOM   7102 C CG2 . VAL D 1 195 ? 26.572  25.853  -26.612 1.00 26.44 ? 195 VAL D CG2 1 
ATOM   7103 N N   . ALA D 1 196 ? 23.112  24.721  -29.546 1.00 25.98 ? 196 ALA D N   1 
ATOM   7104 C CA  . ALA D 1 196 ? 22.800  24.112  -30.836 1.00 25.76 ? 196 ALA D CA  1 
ATOM   7105 C C   . ALA D 1 196 ? 24.019  24.272  -31.742 1.00 29.44 ? 196 ALA D C   1 
ATOM   7106 O O   . ALA D 1 196 ? 24.352  25.391  -32.150 1.00 28.80 ? 196 ALA D O   1 
ATOM   7107 C CB  . ALA D 1 196 ? 21.568  24.756  -31.463 1.00 25.98 ? 196 ALA D CB  1 
ATOM   7108 N N   . ASP D 1 197 ? 24.716  23.158  -32.016 1.00 28.42 ? 197 ASP D N   1 
ATOM   7109 C CA  . ASP D 1 197 ? 25.936  23.150  -32.811 1.00 29.07 ? 197 ASP D CA  1 
ATOM   7110 C C   . ASP D 1 197 ? 25.620  22.669  -34.214 1.00 28.34 ? 197 ASP D C   1 
ATOM   7111 O O   . ASP D 1 197 ? 25.295  21.487  -34.395 1.00 28.79 ? 197 ASP D O   1 
ATOM   7112 C CB  . ASP D 1 197 ? 26.976  22.238  -32.161 1.00 28.97 ? 197 ASP D CB  1 
ATOM   7113 C CG  . ASP D 1 197 ? 28.320  22.230  -32.888 1.00 30.29 ? 197 ASP D CG  1 
ATOM   7114 O OD1 . ASP D 1 197 ? 28.373  22.463  -34.130 1.00 25.17 ? 197 ASP D OD1 1 
ATOM   7115 O OD2 . ASP D 1 197 ? 29.331  21.924  -32.207 1.00 28.82 ? 197 ASP D OD2 1 
ATOM   7116 N N   . PRO D 1 198 ? 25.785  23.508  -35.237 1.00 26.87 ? 198 PRO D N   1 
ATOM   7117 C CA  . PRO D 1 198 ? 25.363  23.118  -36.594 1.00 29.62 ? 198 PRO D CA  1 
ATOM   7118 C C   . PRO D 1 198 ? 26.151  21.942  -37.182 1.00 26.39 ? 198 PRO D C   1 
ATOM   7119 O O   . PRO D 1 198 ? 25.766  21.441  -38.237 1.00 26.00 ? 198 PRO D O   1 
ATOM   7120 C CB  . PRO D 1 198 ? 25.594  24.403  -37.416 1.00 25.98 ? 198 PRO D CB  1 
ATOM   7121 C CG  . PRO D 1 198 ? 25.764  25.488  -36.395 1.00 27.81 ? 198 PRO D CG  1 
ATOM   7122 C CD  . PRO D 1 198 ? 26.405  24.841  -35.215 1.00 25.52 ? 198 PRO D CD  1 
ATOM   7123 N N   . ALA D 1 199 ? 27.225  21.500  -36.548 1.00 25.19 ? 199 ALA D N   1 
ATOM   7124 C CA  . ALA D 1 199 ? 27.987  20.341  -37.012 1.00 30.58 ? 199 ALA D CA  1 
ATOM   7125 C C   . ALA D 1 199 ? 27.874  19.130  -36.090 1.00 31.86 ? 199 ALA D C   1 
ATOM   7126 O O   . ALA D 1 199 ? 28.567  18.128  -36.322 1.00 29.84 ? 199 ALA D O   1 
ATOM   7127 C CB  . ALA D 1 199 ? 29.468  20.709  -37.200 1.00 29.35 ? 199 ALA D CB  1 
ATOM   7128 N N   . LYS D 1 200 ? 27.061  19.197  -35.031 1.00 30.46 ? 200 LYS D N   1 
ATOM   7129 C CA  . LYS D 1 200 ? 27.021  18.105  -34.057 1.00 29.84 ? 200 LYS D CA  1 
ATOM   7130 C C   . LYS D 1 200 ? 25.624  17.788  -33.531 1.00 32.75 ? 200 LYS D C   1 
ATOM   7131 O O   . LYS D 1 200 ? 25.242  16.617  -33.479 1.00 34.34 ? 200 LYS D O   1 
ATOM   7132 C CB  . LYS D 1 200 ? 27.940  18.417  -32.875 1.00 32.31 ? 200 LYS D CB  1 
ATOM   7133 C CG  . LYS D 1 200 ? 29.430  18.392  -33.223 1.00 37.31 ? 200 LYS D CG  1 
ATOM   7134 C CD  . LYS D 1 200 ? 30.008  16.983  -33.309 1.00 35.90 ? 200 LYS D CD  1 
ATOM   7135 C CE  . LYS D 1 200 ? 29.511  16.110  -32.161 1.00 34.28 ? 200 LYS D CE  1 
ATOM   7136 N NZ  . LYS D 1 200 ? 29.504  14.677  -32.565 1.00 36.84 ? 200 LYS D NZ  1 
ATOM   7137 N N   . GLY D 1 201 ? 24.866  18.788  -33.092 1.00 31.50 ? 201 GLY D N   1 
ATOM   7138 C CA  . GLY D 1 201 ? 23.574  18.491  -32.489 1.00 30.55 ? 201 GLY D CA  1 
ATOM   7139 C C   . GLY D 1 201 ? 22.994  19.682  -31.757 1.00 32.49 ? 201 GLY D C   1 
ATOM   7140 O O   . GLY D 1 201 ? 23.666  20.693  -31.491 1.00 26.64 ? 201 GLY D O   1 
ATOM   7141 N N   . VAL D 1 202 ? 21.715  19.531  -31.396 1.00 29.51 ? 202 VAL D N   1 
ATOM   7142 C CA  . VAL D 1 202 ? 20.951  20.654  -30.854 1.00 29.86 ? 202 VAL D CA  1 
ATOM   7143 C C   . VAL D 1 202 ? 21.235  20.905  -29.385 1.00 28.38 ? 202 VAL D C   1 
ATOM   7144 O O   . VAL D 1 202 ? 20.907  21.988  -28.877 1.00 29.91 ? 202 VAL D O   1 
ATOM   7145 C CB  . VAL D 1 202 ? 19.445  20.404  -31.077 1.00 29.06 ? 202 VAL D CB  1 
ATOM   7146 C CG1 . VAL D 1 202 ? 18.878  19.486  -29.982 1.00 28.63 ? 202 VAL D CG1 1 
ATOM   7147 C CG2 . VAL D 1 202 ? 18.687  21.728  -31.123 1.00 29.15 ? 202 VAL D CG2 1 
ATOM   7148 N N   . ASN D 1 203 ? 21.946  19.990  -28.733 1.00 28.80 ? 203 ASN D N   1 
ATOM   7149 C CA  . ASN D 1 203 ? 21.969  19.841  -27.287 1.00 35.04 ? 203 ASN D CA  1 
ATOM   7150 C C   . ASN D 1 203 ? 23.373  19.723  -26.693 1.00 38.32 ? 203 ASN D C   1 
ATOM   7151 O O   . ASN D 1 203 ? 23.559  19.020  -25.697 1.00 40.40 ? 203 ASN D O   1 
ATOM   7152 C CB  . ASN D 1 203 ? 21.167  18.591  -26.928 1.00 43.02 ? 203 ASN D CB  1 
ATOM   7153 C CG  . ASN D 1 203 ? 20.636  18.628  -25.554 1.00 46.69 ? 203 ASN D CG  1 
ATOM   7154 O OD1 . ASN D 1 203 ? 20.580  17.593  -24.872 1.00 50.71 ? 203 ASN D OD1 1 
ATOM   7155 N ND2 . ASN D 1 203 ? 20.257  19.816  -25.099 1.00 50.34 ? 203 ASN D ND2 1 
ATOM   7156 N N   . ARG D 1 204 ? 24.375  20.397  -27.255 1.00 35.70 ? 204 ARG D N   1 
ATOM   7157 C CA  . ARG D 1 204 ? 25.754  20.256  -26.774 1.00 34.67 ? 204 ARG D CA  1 
ATOM   7158 C C   . ARG D 1 204 ? 25.948  21.118  -25.526 1.00 35.58 ? 204 ARG D C   1 
ATOM   7159 O O   . ARG D 1 204 ? 25.708  22.333  -25.566 1.00 35.63 ? 204 ARG D O   1 
ATOM   7160 C CB  . ARG D 1 204 ? 26.748  20.653  -27.868 1.00 33.08 ? 204 ARG D CB  1 
ATOM   7161 C CG  . ARG D 1 204 ? 26.499  20.016  -29.234 1.00 30.53 ? 204 ARG D CG  1 
ATOM   7162 C CD  . ARG D 1 204 ? 26.079  18.557  -29.097 1.00 36.68 ? 204 ARG D CD  1 
ATOM   7163 N NE  . ARG D 1 204 ? 27.230  17.718  -28.792 1.00 33.22 ? 204 ARG D NE  1 
ATOM   7164 C CZ  . ARG D 1 204 ? 27.171  16.422  -28.544 1.00 40.75 ? 204 ARG D CZ  1 
ATOM   7165 N NH1 . ARG D 1 204 ? 26.015  15.778  -28.514 1.00 43.94 ? 204 ARG D NH1 1 
ATOM   7166 N NH2 . ARG D 1 204 ? 28.301  15.755  -28.311 1.00 45.66 ? 204 ARG D NH2 1 
ATOM   7167 N N   . LYS D 1 205 ? 26.369  20.496  -24.414 1.00 35.06 ? 205 LYS D N   1 
ATOM   7168 C CA  . LYS D 1 205 ? 26.433  21.164  -23.113 1.00 35.13 ? 205 LYS D CA  1 
ATOM   7169 C C   . LYS D 1 205 ? 27.865  21.586  -22.806 1.00 39.83 ? 205 LYS D C   1 
ATOM   7170 O O   . LYS D 1 205 ? 28.753  20.742  -22.624 1.00 40.11 ? 205 LYS D O   1 
ATOM   7171 C CB  . LYS D 1 205 ? 25.851  20.273  -22.016 1.00 37.19 ? 205 LYS D CB  1 
ATOM   7172 C CG  . LYS D 1 205 ? 24.308  20.081  -22.149 1.00 41.92 ? 205 LYS D CG  1 
ATOM   7173 C CD  . LYS D 1 205 ? 23.615  19.849  -20.790 1.00 42.68 ? 205 LYS D CD  1 
ATOM   7174 C CE  . LYS D 1 205 ? 22.145  19.419  -20.929 1.00 43.60 ? 205 LYS D CE  1 
ATOM   7175 N NZ  . LYS D 1 205 ? 21.921  18.214  -21.808 1.00 47.74 ? 205 LYS D NZ  1 
ATOM   7176 N N   . TYR D 1 206 ? 28.078  22.886  -22.797 1.00 36.77 ? 206 TYR D N   1 
ATOM   7177 C CA  . TYR D 1 206 ? 29.418  23.432  -22.530 1.00 40.65 ? 206 TYR D CA  1 
ATOM   7178 C C   . TYR D 1 206 ? 29.443  24.027  -21.133 1.00 41.79 ? 206 TYR D C   1 
ATOM   7179 O O   . TYR D 1 206 ? 28.584  24.800  -20.775 1.00 38.10 ? 206 TYR D O   1 
ATOM   7180 C CB  . TYR D 1 206 ? 29.789  24.475  -23.576 1.00 32.62 ? 206 TYR D CB  1 
ATOM   7181 C CG  . TYR D 1 206 ? 30.301  23.854  -24.837 1.00 32.73 ? 206 TYR D CG  1 
ATOM   7182 C CD1 . TYR D 1 206 ? 29.449  23.207  -25.707 1.00 32.04 ? 206 TYR D CD1 1 
ATOM   7183 C CD2 . TYR D 1 206 ? 31.640  23.885  -25.149 1.00 32.20 ? 206 TYR D CD2 1 
ATOM   7184 C CE1 . TYR D 1 206 ? 29.906  22.613  -26.864 1.00 32.32 ? 206 TYR D CE1 1 
ATOM   7185 C CE2 . TYR D 1 206 ? 32.114  23.298  -26.303 1.00 33.58 ? 206 TYR D CE2 1 
ATOM   7186 C CZ  . TYR D 1 206 ? 31.249  22.658  -27.163 1.00 33.14 ? 206 TYR D CZ  1 
ATOM   7187 O OH  . TYR D 1 206 ? 31.724  22.085  -28.289 1.00 31.06 ? 206 TYR D OH  1 
ATOM   7188 N N   . LYS D 1 207 ? 30.452  23.621  -20.384 1.00 46.48 ? 207 LYS D N   1 
ATOM   7189 C CA  . LYS D 1 207 ? 30.666  24.140  -19.029 1.00 41.57 ? 207 LYS D CA  1 
ATOM   7190 C C   . LYS D 1 207 ? 31.021  25.599  -19.254 1.00 42.30 ? 207 LYS D C   1 
ATOM   7191 O O   . LYS D 1 207 ? 31.880  25.831  -20.079 1.00 39.75 ? 207 LYS D O   1 
ATOM   7192 C CB  . LYS D 1 207 ? 31.773  23.314  -18.377 1.00 47.79 ? 207 LYS D CB  1 
ATOM   7193 C CG  . LYS D 1 207 ? 31.870  21.873  -18.879 1.00 49.15 ? 207 LYS D CG  1 
ATOM   7194 C CD  . LYS D 1 207 ? 32.362  21.691  -20.318 1.00 50.13 ? 207 LYS D CD  1 
ATOM   7195 C CE  . LYS D 1 207 ? 31.595  20.669  -21.122 1.00 48.95 ? 207 LYS D CE  1 
ATOM   7196 N NZ  . LYS D 1 207 ? 31.004  19.566  -20.319 1.00 57.66 ? 207 LYS D NZ  1 
ATOM   7197 N N   . PHE D 1 208 ? 30.318  26.497  -18.573 1.00 39.97 ? 208 PHE D N   1 
ATOM   7198 C CA  . PHE D 1 208 ? 30.478  27.963  -18.717 1.00 39.27 ? 208 PHE D CA  1 
ATOM   7199 C C   . PHE D 1 208 ? 31.934  28.350  -18.909 1.00 41.09 ? 208 PHE D C   1 
ATOM   7200 O O   . PHE D 1 208 ? 32.188  28.996  -19.911 1.00 40.40 ? 208 PHE D O   1 
ATOM   7201 C CB  . PHE D 1 208 ? 29.988  28.733  -17.491 1.00 41.98 ? 208 PHE D CB  1 
ATOM   7202 C CG  . PHE D 1 208 ? 28.538  28.554  -17.152 1.00 38.53 ? 208 PHE D CG  1 
ATOM   7203 C CD1 . PHE D 1 208 ? 27.599  28.366  -18.141 1.00 37.29 ? 208 PHE D CD1 1 
ATOM   7204 C CD2 . PHE D 1 208 ? 28.117  28.586  -15.841 1.00 38.87 ? 208 PHE D CD2 1 
ATOM   7205 C CE1 . PHE D 1 208 ? 26.265  28.216  -17.827 1.00 38.78 ? 208 PHE D CE1 1 
ATOM   7206 C CE2 . PHE D 1 208 ? 26.782  28.416  -15.528 1.00 40.69 ? 208 PHE D CE2 1 
ATOM   7207 C CZ  . PHE D 1 208 ? 25.860  28.242  -16.523 1.00 39.59 ? 208 PHE D CZ  1 
ATOM   7208 N N   . SER D 1 209 ? 32.851  27.836  -18.086 1.00 40.05 ? 209 SER D N   1 
ATOM   7209 C CA  . SER D 1 209 ? 34.190  28.368  -18.327 1.00 41.27 ? 209 SER D CA  1 
ATOM   7210 C C   . SER D 1 209 ? 34.828  27.762  -19.573 1.00 38.06 ? 209 SER D C   1 
ATOM   7211 O O   . SER D 1 209 ? 35.717  28.380  -20.179 1.00 40.74 ? 209 SER D O   1 
ATOM   7212 C CB  . SER D 1 209 ? 35.099  28.134  -17.125 1.00 39.97 ? 209 SER D CB  1 
ATOM   7213 O OG  . SER D 1 209 ? 35.263  26.750  -16.900 1.00 42.73 ? 209 SER D OG  1 
ATOM   7214 N N   . CYS D 1 210 ? 34.447  26.533  -19.923 1.00 38.93 ? 210 CYS D N   1 
ATOM   7215 C CA  . CYS D 1 210 ? 34.992  25.875  -21.111 1.00 37.72 ? 210 CYS D CA  1 
ATOM   7216 C C   . CYS D 1 210 ? 34.698  26.671  -22.373 1.00 38.28 ? 210 CYS D C   1 
ATOM   7217 O O   . CYS D 1 210 ? 35.605  26.965  -23.166 1.00 37.90 ? 210 CYS D O   1 
ATOM   7218 C CB  . CYS D 1 210 ? 34.403  24.481  -21.224 1.00 38.33 ? 210 CYS D CB  1 
ATOM   7219 S SG  . CYS D 1 210 ? 34.920  23.476  -22.597 1.00 39.92 ? 210 CYS D SG  1 
ATOM   7220 N N   . LEU D 1 211 ? 33.428  27.030  -22.581 1.00 36.52 ? 211 LEU D N   1 
ATOM   7221 C CA  . LEU D 1 211 ? 33.079  27.840  -23.745 1.00 35.78 ? 211 LEU D CA  1 
ATOM   7222 C C   . LEU D 1 211 ? 33.627  29.261  -23.626 1.00 35.82 ? 211 LEU D C   1 
ATOM   7223 O O   . LEU D 1 211 ? 34.174  29.797  -24.594 1.00 34.01 ? 211 LEU D O   1 
ATOM   7224 C CB  . LEU D 1 211 ? 31.558  27.868  -23.937 1.00 33.12 ? 211 LEU D CB  1 
ATOM   7225 C CG  . LEU D 1 211 ? 31.078  28.426  -25.296 1.00 36.25 ? 211 LEU D CG  1 
ATOM   7226 C CD1 . LEU D 1 211 ? 31.566  27.559  -26.456 1.00 32.76 ? 211 LEU D CD1 1 
ATOM   7227 C CD2 . LEU D 1 211 ? 29.556  28.635  -25.374 1.00 30.22 ? 211 LEU D CD2 1 
ATOM   7228 N N   . ASP D 1 212 ? 33.475  29.892  -22.452 1.00 38.91 ? 212 ASP D N   1 
ATOM   7229 C CA  . ASP D 1 212 ? 33.929  31.274  -22.264 1.00 38.25 ? 212 ASP D CA  1 
ATOM   7230 C C   . ASP D 1 212 ? 35.394  31.429  -22.647 1.00 38.34 ? 212 ASP D C   1 
ATOM   7231 O O   . ASP D 1 212 ? 35.797  32.444  -23.234 1.00 39.10 ? 212 ASP D O   1 
ATOM   7232 C CB  . ASP D 1 212 ? 33.745  31.712  -20.810 1.00 36.84 ? 212 ASP D CB  1 
ATOM   7233 C CG  . ASP D 1 212 ? 32.298  31.880  -20.431 1.00 38.30 ? 212 ASP D CG  1 
ATOM   7234 O OD1 . ASP D 1 212 ? 31.455  31.951  -21.341 1.00 38.72 ? 212 ASP D OD1 1 
ATOM   7235 O OD2 . ASP D 1 212 ? 32.006  31.910  -19.220 1.00 38.46 ? 212 ASP D OD2 1 
ATOM   7236 N N   . ASN D 1 213 ? 36.221  30.453  -22.281 1.00 39.33 ? 213 ASN D N   1 
ATOM   7237 C CA  . ASN D 1 213 ? 37.697  30.552  -22.449 1.00 42.35 ? 213 ASN D CA  1 
ATOM   7238 C C   . ASN D 1 213 ? 38.226  29.891  -23.726 1.00 42.52 ? 213 ASN D C   1 
ATOM   7239 O O   . ASN D 1 213 ? 39.427  29.911  -23.903 1.00 41.97 ? 213 ASN D O   1 
ATOM   7240 C CB  . ASN D 1 213 ? 38.432  29.963  -21.246 1.00 43.09 ? 213 ASN D CB  1 
ATOM   7241 C CG  . ASN D 1 213 ? 38.230  30.750  -19.969 1.00 43.66 ? 213 ASN D CG  1 
ATOM   7242 O OD1 . ASN D 1 213 ? 38.086  31.955  -19.995 1.00 47.25 ? 213 ASN D OD1 1 
ATOM   7243 N ND2 . ASN D 1 213 ? 38.211  30.066  -18.848 1.00 44.95 ? 213 ASN D ND2 1 
ATOM   7244 N N   . ALA D 1 214 ? 37.372  29.403  -24.619 1.00 40.69 ? 214 ALA D N   1 
ATOM   7245 C CA  . ALA D 1 214 ? 37.911  28.715  -25.811 1.00 36.21 ? 214 ALA D CA  1 
ATOM   7246 C C   . ALA D 1 214 ? 38.060  29.653  -27.016 1.00 40.06 ? 214 ALA D C   1 
ATOM   7247 O O   . ALA D 1 214 ? 37.992  29.164  -28.122 1.00 36.60 ? 214 ALA D O   1 
ATOM   7248 C CB  . ALA D 1 214 ? 37.060  27.526  -26.144 1.00 36.12 ? 214 ALA D CB  1 
ATOM   7249 N N   . ASN D 1 215 ? 38.289  30.946  -26.797 1.00 40.86 ? 215 ASN D N   1 
ATOM   7250 C CA  . ASN D 1 215 ? 38.465  31.887  -27.931 1.00 36.74 ? 215 ASN D CA  1 
ATOM   7251 C C   . ASN D 1 215 ? 39.702  32.768  -27.706 1.00 41.24 ? 215 ASN D C   1 
ATOM   7252 O O   . ASN D 1 215 ? 39.722  33.871  -28.222 1.00 36.26 ? 215 ASN D O   1 
ATOM   7253 C CB  . ASN D 1 215 ? 37.205  32.701  -28.219 1.00 32.34 ? 215 ASN D CB  1 
ATOM   7254 C CG  . ASN D 1 215 ? 36.962  32.906  -29.697 1.00 34.68 ? 215 ASN D CG  1 
ATOM   7255 O OD1 . ASN D 1 215 ? 37.263  32.042  -30.502 1.00 35.06 ? 215 ASN D OD1 1 
ATOM   7256 N ND2 . ASN D 1 215 ? 36.433  34.051  -30.067 1.00 32.97 ? 215 ASN D ND2 1 
ATOM   7257 N N   . LYS D 1 216 ? 40.688  32.279  -26.960 1.00 50.29 ? 216 LYS D N   1 
ATOM   7258 C CA  . LYS D 1 216 ? 41.946  33.032  -26.722 1.00 45.01 ? 216 LYS D CA  1 
ATOM   7259 C C   . LYS D 1 216 ? 42.519  33.497  -28.055 1.00 39.55 ? 216 LYS D C   1 
ATOM   7260 O O   . LYS D 1 216 ? 42.684  32.669  -28.924 1.00 36.58 ? 216 LYS D O   1 
ATOM   7261 C CB  . LYS D 1 216 ? 42.992  32.106  -26.116 1.00 41.19 ? 216 LYS D CB  1 
ATOM   7262 C CG  . LYS D 1 216 ? 43.351  32.385  -24.674 1.00 53.10 ? 216 LYS D CG  1 
ATOM   7263 C CD  . LYS D 1 216 ? 42.477  31.627  -23.713 1.00 54.66 ? 216 LYS D CD  1 
ATOM   7264 C CE  . LYS D 1 216 ? 43.222  31.198  -22.470 1.00 48.81 ? 216 LYS D CE  1 
ATOM   7265 N NZ  . LYS D 1 216 ? 43.069  29.749  -22.216 1.00 50.19 ? 216 LYS D NZ  1 
ATOM   7266 N N   . GLY D 1 217 ? 42.811  34.785  -28.174 1.00 44.95 ? 217 GLY D N   1 
ATOM   7267 C CA  . GLY D 1 217 ? 43.379  35.323  -29.416 1.00 35.92 ? 217 GLY D CA  1 
ATOM   7268 C C   . GLY D 1 217 ? 42.310  35.814  -30.365 1.00 41.77 ? 217 GLY D C   1 
ATOM   7269 O O   . GLY D 1 217 ? 42.678  36.380  -31.386 1.00 41.47 ? 217 GLY D O   1 
ATOM   7270 N N   . TYR D 1 218 ? 41.032  35.653  -30.025 1.00 38.39 ? 218 TYR D N   1 
ATOM   7271 C CA  . TYR D 1 218 ? 40.067  36.095  -30.968 1.00 37.26 ? 218 TYR D CA  1 
ATOM   7272 C C   . TYR D 1 218 ? 39.099  36.963  -30.195 1.00 34.86 ? 218 TYR D C   1 
ATOM   7273 O O   . TYR D 1 218 ? 39.256  37.193  -28.990 1.00 37.12 ? 218 TYR D O   1 
ATOM   7274 C CB  . TYR D 1 218 ? 39.395  34.878  -31.605 1.00 37.04 ? 218 TYR D CB  1 
ATOM   7275 C CG  . TYR D 1 218 ? 40.304  34.041  -32.481 1.00 37.38 ? 218 TYR D CG  1 
ATOM   7276 C CD1 . TYR D 1 218 ? 41.121  33.043  -31.964 1.00 37.61 ? 218 TYR D CD1 1 
ATOM   7277 C CD2 . TYR D 1 218 ? 40.334  34.271  -33.857 1.00 37.99 ? 218 TYR D CD2 1 
ATOM   7278 C CE1 . TYR D 1 218 ? 41.951  32.281  -32.796 1.00 35.13 ? 218 TYR D CE1 1 
ATOM   7279 C CE2 . TYR D 1 218 ? 41.156  33.527  -34.694 1.00 39.40 ? 218 TYR D CE2 1 
ATOM   7280 C CZ  . TYR D 1 218 ? 41.950  32.530  -34.155 1.00 36.77 ? 218 TYR D CZ  1 
ATOM   7281 O OH  . TYR D 1 218 ? 42.752  31.789  -34.982 1.00 47.20 ? 218 TYR D OH  1 
ATOM   7282 N N   . ARG D 1 219 ? 38.103  37.469  -30.896 1.00 33.76 ? 219 ARG D N   1 
ATOM   7283 C CA  . ARG D 1 219 ? 37.211  38.449  -30.293 1.00 34.27 ? 219 ARG D CA  1 
ATOM   7284 C C   . ARG D 1 219 ? 36.526  37.883  -29.054 1.00 33.29 ? 219 ARG D C   1 
ATOM   7285 O O   . ARG D 1 219 ? 35.910  36.817  -29.097 1.00 31.47 ? 219 ARG D O   1 
ATOM   7286 C CB  . ARG D 1 219 ? 36.172  38.894  -31.312 1.00 35.52 ? 219 ARG D CB  1 
ATOM   7287 C CG  . ARG D 1 219 ? 35.298  40.028  -30.816 1.00 34.21 ? 219 ARG D CG  1 
ATOM   7288 C CD  . ARG D 1 219 ? 34.903  40.951  -31.939 1.00 34.96 ? 219 ARG D CD  1 
ATOM   7289 N NE  . ARG D 1 219 ? 33.794  41.782  -31.500 1.00 31.41 ? 219 ARG D NE  1 
ATOM   7290 C CZ  . ARG D 1 219 ? 33.049  42.514  -32.312 1.00 35.62 ? 219 ARG D CZ  1 
ATOM   7291 N NH1 . ARG D 1 219 ? 33.269  42.531  -33.616 1.00 33.89 ? 219 ARG D NH1 1 
ATOM   7292 N NH2 . ARG D 1 219 ? 32.086  43.281  -31.798 1.00 37.73 ? 219 ARG D NH2 1 
ATOM   7293 N N   . GLN D 1 220 ? 36.619  38.617  -27.950 1.00 32.62 ? 220 GLN D N   1 
ATOM   7294 C CA  . GLN D 1 220 ? 36.107  38.151  -26.664 1.00 36.35 ? 220 GLN D CA  1 
ATOM   7295 C C   . GLN D 1 220 ? 34.646  38.578  -26.474 1.00 34.79 ? 220 GLN D C   1 
ATOM   7296 O O   . GLN D 1 220 ? 34.296  39.320  -25.561 1.00 37.78 ? 220 GLN D O   1 
ATOM   7297 C CB  . GLN D 1 220 ? 36.984  38.686  -25.536 1.00 36.94 ? 220 GLN D CB  1 
ATOM   7298 C CG  . GLN D 1 220 ? 38.331  37.997  -25.423 1.00 38.42 ? 220 GLN D CG  1 
ATOM   7299 C CD  . GLN D 1 220 ? 38.181  36.548  -25.074 1.00 38.91 ? 220 GLN D CD  1 
ATOM   7300 O OE1 . GLN D 1 220 ? 38.544  35.677  -25.861 1.00 45.85 ? 220 GLN D OE1 1 
ATOM   7301 N NE2 . GLN D 1 220 ? 37.632  36.270  -23.897 1.00 42.97 ? 220 GLN D NE2 1 
ATOM   7302 N N   . ASN D 1 221 ? 33.774  38.070  -27.343 1.00 33.92 ? 221 ASN D N   1 
ATOM   7303 C CA  . ASN D 1 221 ? 32.354  38.392  -27.253 1.00 32.50 ? 221 ASN D CA  1 
ATOM   7304 C C   . ASN D 1 221 ? 31.516  37.158  -27.552 1.00 31.69 ? 221 ASN D C   1 
ATOM   7305 O O   . ASN D 1 221 ? 31.981  36.216  -28.201 1.00 30.96 ? 221 ASN D O   1 
ATOM   7306 C CB  . ASN D 1 221 ? 31.970  39.512  -28.243 1.00 32.98 ? 221 ASN D CB  1 
ATOM   7307 C CG  . ASN D 1 221 ? 32.472  40.877  -27.821 1.00 36.44 ? 221 ASN D CG  1 
ATOM   7308 O OD1 . ASN D 1 221 ? 33.185  41.546  -28.573 1.00 37.34 ? 221 ASN D OD1 1 
ATOM   7309 N ND2 . ASN D 1 221 ? 32.095  41.306  -26.622 1.00 35.97 ? 221 ASN D ND2 1 
ATOM   7310 N N   . TYR D 1 222 ? 30.264  37.181  -27.063 1.00 32.90 ? 222 TYR D N   1 
ATOM   7311 C CA  . TYR D 1 222 ? 29.143  36.413  -27.598 1.00 30.71 ? 222 TYR D CA  1 
ATOM   7312 C C   . TYR D 1 222 ? 28.223  37.390  -28.324 1.00 32.53 ? 222 TYR D C   1 
ATOM   7313 O O   . TYR D 1 222 ? 28.354  38.610  -28.195 1.00 30.97 ? 222 TYR D O   1 
ATOM   7314 C CB  . TYR D 1 222 ? 28.368  35.692  -26.481 1.00 34.14 ? 222 TYR D CB  1 
ATOM   7315 C CG  . TYR D 1 222 ? 29.094  34.539  -25.812 1.00 33.80 ? 222 TYR D CG  1 
ATOM   7316 C CD1 . TYR D 1 222 ? 30.040  33.775  -26.480 1.00 32.86 ? 222 TYR D CD1 1 
ATOM   7317 C CD2 . TYR D 1 222 ? 28.888  34.282  -24.461 1.00 34.16 ? 222 TYR D CD2 1 
ATOM   7318 C CE1 . TYR D 1 222 ? 30.722  32.724  -25.817 1.00 32.83 ? 222 TYR D CE1 1 
ATOM   7319 C CE2 . TYR D 1 222 ? 29.554  33.268  -23.800 1.00 35.52 ? 222 TYR D CE2 1 
ATOM   7320 C CZ  . TYR D 1 222 ? 30.469  32.495  -24.477 1.00 32.73 ? 222 TYR D CZ  1 
ATOM   7321 O OH  . TYR D 1 222 ? 31.121  31.499  -23.790 1.00 36.25 ? 222 TYR D OH  1 
ATOM   7322 N N   . TYR D 1 223 ? 27.252  36.870  -29.069 1.00 32.35 ? 223 TYR D N   1 
ATOM   7323 C CA  . TYR D 1 223 ? 26.464  37.717  -29.968 1.00 30.43 ? 223 TYR D CA  1 
ATOM   7324 C C   . TYR D 1 223 ? 24.969  37.458  -29.811 1.00 29.38 ? 223 TYR D C   1 
ATOM   7325 O O   . TYR D 1 223 ? 24.425  36.508  -30.381 1.00 25.80 ? 223 TYR D O   1 
ATOM   7326 C CB  . TYR D 1 223 ? 26.937  37.533  -31.405 1.00 28.89 ? 223 TYR D CB  1 
ATOM   7327 C CG  . TYR D 1 223 ? 28.430  37.707  -31.473 1.00 29.98 ? 223 TYR D CG  1 
ATOM   7328 C CD1 . TYR D 1 223 ? 28.989  38.989  -31.485 1.00 32.08 ? 223 TYR D CD1 1 
ATOM   7329 C CD2 . TYR D 1 223 ? 29.286  36.613  -31.468 1.00 28.90 ? 223 TYR D CD2 1 
ATOM   7330 C CE1 . TYR D 1 223 ? 30.364  39.171  -31.517 1.00 32.64 ? 223 TYR D CE1 1 
ATOM   7331 C CE2 . TYR D 1 223 ? 30.666  36.789  -31.504 1.00 30.56 ? 223 TYR D CE2 1 
ATOM   7332 C CZ  . TYR D 1 223 ? 31.188  38.078  -31.531 1.00 29.30 ? 223 TYR D CZ  1 
ATOM   7333 O OH  . TYR D 1 223 ? 32.535  38.289  -31.558 1.00 31.98 ? 223 TYR D OH  1 
ATOM   7334 N N   . VAL D 1 224 ? 24.299  38.363  -29.093 1.00 29.20 ? 224 VAL D N   1 
ATOM   7335 C CA  . VAL D 1 224 ? 22.869  38.219  -28.856 1.00 29.23 ? 224 VAL D CA  1 
ATOM   7336 C C   . VAL D 1 224 ? 22.131  38.542  -30.146 1.00 29.03 ? 224 VAL D C   1 
ATOM   7337 O O   . VAL D 1 224 ? 22.461  39.511  -30.840 1.00 30.40 ? 224 VAL D O   1 
ATOM   7338 C CB  . VAL D 1 224 ? 22.405  39.156  -27.729 1.00 29.42 ? 224 VAL D CB  1 
ATOM   7339 C CG1 . VAL D 1 224 ? 20.878  39.069  -27.576 1.00 28.46 ? 224 VAL D CG1 1 
ATOM   7340 C CG2 . VAL D 1 224 ? 23.114  38.857  -26.434 1.00 28.59 ? 224 VAL D CG2 1 
ATOM   7341 N N   . VAL D 1 225 ? 21.154  37.718  -30.495 1.00 24.78 ? 225 VAL D N   1 
ATOM   7342 C CA  . VAL D 1 225 ? 20.312  37.974  -31.657 1.00 26.54 ? 225 VAL D CA  1 
ATOM   7343 C C   . VAL D 1 225 ? 18.978  38.473  -31.135 1.00 26.98 ? 225 VAL D C   1 
ATOM   7344 O O   . VAL D 1 225 ? 18.310  37.781  -30.351 1.00 26.34 ? 225 VAL D O   1 
ATOM   7345 C CB  . VAL D 1 225 ? 20.127  36.719  -32.529 1.00 25.43 ? 225 VAL D CB  1 
ATOM   7346 C CG1 . VAL D 1 225 ? 19.436  37.085  -33.827 1.00 22.35 ? 225 VAL D CG1 1 
ATOM   7347 C CG2 . VAL D 1 225 ? 21.474  36.049  -32.824 1.00 23.70 ? 225 VAL D CG2 1 
ATOM   7348 N N   . CYS D 1 226 ? 18.565  39.647  -31.577 1.00 25.98 ? 226 CYS D N   1 
ATOM   7349 C CA  . CYS D 1 226 ? 17.249  40.134  -31.193 1.00 29.38 ? 226 CYS D CA  1 
ATOM   7350 C C   . CYS D 1 226 ? 16.590  40.807  -32.385 1.00 28.85 ? 226 CYS D C   1 
ATOM   7351 O O   . CYS D 1 226 ? 17.249  41.071  -33.400 1.00 30.28 ? 226 CYS D O   1 
ATOM   7352 C CB  . CYS D 1 226 ? 17.363  41.066  -29.980 1.00 30.49 ? 226 CYS D CB  1 
ATOM   7353 S SG  . CYS D 1 226 ? 18.320  42.540  -30.313 1.00 37.32 ? 226 CYS D SG  1 
ATOM   7354 N N   . PRO D 1 227 ? 15.280  41.036  -32.317 1.00 28.39 ? 227 PRO D N   1 
ATOM   7355 C CA  . PRO D 1 227 ? 14.602  41.745  -33.398 1.00 31.46 ? 227 PRO D CA  1 
ATOM   7356 C C   . PRO D 1 227 ? 15.128  43.162  -33.543 1.00 29.24 ? 227 PRO D C   1 
ATOM   7357 O O   . PRO D 1 227 ? 15.404  43.850  -32.562 1.00 29.56 ? 227 PRO D O   1 
ATOM   7358 C CB  . PRO D 1 227 ? 13.125  41.733  -32.955 1.00 31.95 ? 227 PRO D CB  1 
ATOM   7359 C CG  . PRO D 1 227 ? 13.002  40.523  -32.092 1.00 29.73 ? 227 PRO D CG  1 
ATOM   7360 C CD  . PRO D 1 227 ? 14.311  40.489  -31.343 1.00 30.35 ? 227 PRO D CD  1 
ATOM   7361 N N   . ALA D 1 228 ? 15.315  43.571  -34.779 1.00 28.53 ? 228 ALA D N   1 
ATOM   7362 C CA  . ALA D 1 228 ? 15.759  44.923  -35.059 1.00 35.74 ? 228 ALA D CA  1 
ATOM   7363 C C   . ALA D 1 228 ? 14.514  45.794  -35.060 1.00 40.14 ? 228 ALA D C   1 
ATOM   7364 O O   . ALA D 1 228 ? 13.470  45.320  -35.525 1.00 41.82 ? 228 ALA D O   1 
ATOM   7365 C CB  . ALA D 1 228 ? 16.470  44.990  -36.369 1.00 30.29 ? 228 ALA D CB  1 
ATOM   7366 O OXT . ALA D 1 228 ? 14.507  46.939  -34.593 1.00 43.73 ? 228 ALA D OXT 1 
HETATM 7367 O O   . HOH E 2 .   ? 7.103   9.464   -3.703  1.00 45.15 ? 301 HOH A O   1 
HETATM 7368 O O   . HOH E 2 .   ? -5.977  9.908   22.425  1.00 55.39 ? 302 HOH A O   1 
HETATM 7369 O O   . HOH E 2 .   ? 1.705   5.865   -9.240  1.00 53.89 ? 303 HOH A O   1 
HETATM 7370 O O   . HOH E 2 .   ? 9.328   -12.574 23.991  1.00 38.19 ? 304 HOH A O   1 
HETATM 7371 O O   . HOH E 2 .   ? 25.836  10.061  11.516  1.00 43.93 ? 305 HOH A O   1 
HETATM 7372 O O   . HOH E 2 .   ? 5.798   10.544  21.579  1.00 51.88 ? 306 HOH A O   1 
HETATM 7373 O O   . HOH E 2 .   ? 31.946  15.012  5.655   1.00 38.64 ? 307 HOH A O   1 
HETATM 7374 O O   . HOH E 2 .   ? 24.440  16.283  -8.653  1.00 50.93 ? 308 HOH A O   1 
HETATM 7375 O O   . HOH E 2 .   ? 27.340  -11.864 7.861   1.00 36.33 ? 309 HOH A O   1 
HETATM 7376 O O   . HOH E 2 .   ? 16.785  -12.346 21.065  1.00 52.60 ? 310 HOH A O   1 
HETATM 7377 O O   . HOH E 2 .   ? 29.537  10.661  7.238   1.00 31.89 ? 311 HOH A O   1 
HETATM 7378 O O   . HOH E 2 .   ? 1.722   -6.271  9.299   1.00 26.40 ? 312 HOH A O   1 
HETATM 7379 O O   . HOH E 2 .   ? 10.637  9.730   20.041  1.00 35.07 ? 313 HOH A O   1 
HETATM 7380 O O   . HOH E 2 .   ? 1.725   6.144   5.487   1.00 36.17 ? 314 HOH A O   1 
HETATM 7381 O O   . HOH E 2 .   ? 8.882   -4.782  -11.241 1.00 47.96 ? 315 HOH A O   1 
HETATM 7382 O O   . HOH E 2 .   ? 6.340   8.009   14.527  1.00 25.37 ? 316 HOH A O   1 
HETATM 7383 O O   . HOH E 2 .   ? 0.976   12.833  -2.286  1.00 49.36 ? 317 HOH A O   1 
HETATM 7384 O O   . HOH E 2 .   ? 4.269   13.927  8.633   1.00 31.95 ? 318 HOH A O   1 
HETATM 7385 O O   . HOH E 2 .   ? 32.722  12.696  2.893   1.00 33.38 ? 319 HOH A O   1 
HETATM 7386 O O   . HOH E 2 .   ? 15.044  3.936   26.073  1.00 46.69 ? 320 HOH A O   1 
HETATM 7387 O O   . HOH E 2 .   ? -5.691  14.659  12.442  1.00 46.93 ? 321 HOH A O   1 
HETATM 7388 O O   . HOH E 2 .   ? 24.640  -10.825 9.134   1.00 43.53 ? 322 HOH A O   1 
HETATM 7389 O O   . HOH E 2 .   ? 16.990  15.674  3.749   1.00 42.50 ? 323 HOH A O   1 
HETATM 7390 O O   . HOH E 2 .   ? 20.210  2.124   -6.845  1.00 33.89 ? 324 HOH A O   1 
HETATM 7391 O O   . HOH E 2 .   ? 5.711   5.016   22.878  1.00 30.49 ? 325 HOH A O   1 
HETATM 7392 O O   . HOH E 2 .   ? 16.579  5.596   1.482   1.00 25.35 ? 326 HOH A O   1 
HETATM 7393 O O   . HOH E 2 .   ? 42.798  9.578   -2.224  1.00 43.06 ? 327 HOH A O   1 
HETATM 7394 O O   . HOH E 2 .   ? 12.704  10.641  19.327  1.00 50.14 ? 328 HOH A O   1 
HETATM 7395 O O   . HOH E 2 .   ? 10.733  -11.931 0.238   1.00 27.30 ? 329 HOH A O   1 
HETATM 7396 O O   . HOH E 2 .   ? 6.933   -10.280 -8.390  1.00 35.24 ? 330 HOH A O   1 
HETATM 7397 O O   . HOH E 2 .   ? 23.560  -3.685  8.690   1.00 33.19 ? 331 HOH A O   1 
HETATM 7398 O O   . HOH E 2 .   ? 18.289  8.518   -4.588  1.00 30.29 ? 332 HOH A O   1 
HETATM 7399 O O   . HOH E 2 .   ? 6.388   14.124  0.838   1.00 39.13 ? 333 HOH A O   1 
HETATM 7400 O O   . HOH E 2 .   ? 8.986   -1.138  27.077  1.00 33.08 ? 334 HOH A O   1 
HETATM 7401 O O   . HOH E 2 .   ? 3.180   -11.172 16.665  1.00 29.60 ? 335 HOH A O   1 
HETATM 7402 O O   . HOH E 2 .   ? 19.471  -0.316  -8.749  1.00 40.55 ? 336 HOH A O   1 
HETATM 7403 O O   . HOH E 2 .   ? 18.768  6.942   18.684  1.00 51.03 ? 337 HOH A O   1 
HETATM 7404 O O   . HOH E 2 .   ? 25.570  2.873   -0.019  1.00 29.80 ? 338 HOH A O   1 
HETATM 7405 O O   . HOH E 2 .   ? 43.469  -9.314  8.659   1.00 57.14 ? 339 HOH A O   1 
HETATM 7406 O O   . HOH E 2 .   ? 40.810  -10.020 4.723   1.00 47.36 ? 340 HOH A O   1 
HETATM 7407 O O   . HOH E 2 .   ? -0.779  -1.511  -3.627  1.00 41.22 ? 341 HOH A O   1 
HETATM 7408 O O   . HOH E 2 .   ? -3.885  -5.559  21.130  1.00 32.48 ? 342 HOH A O   1 
HETATM 7409 O O   . HOH E 2 .   ? 24.185  7.088   10.100  1.00 13.80 ? 343 HOH A O   1 
HETATM 7410 O O   . HOH E 2 .   ? -0.723  -10.473 4.263   1.00 46.49 ? 344 HOH A O   1 
HETATM 7411 O O   . HOH E 2 .   ? 10.765  8.809   -5.082  1.00 53.45 ? 345 HOH A O   1 
HETATM 7412 O O   . HOH E 2 .   ? -4.017  9.343   15.523  1.00 32.86 ? 346 HOH A O   1 
HETATM 7413 O O   . HOH E 2 .   ? 7.841   -7.203  22.648  1.00 31.26 ? 347 HOH A O   1 
HETATM 7414 O O   . HOH E 2 .   ? 25.145  1.893   2.567   1.00 29.07 ? 348 HOH A O   1 
HETATM 7415 O O   . HOH E 2 .   ? 29.103  6.228   -5.576  1.00 31.63 ? 349 HOH A O   1 
HETATM 7416 O O   . HOH E 2 .   ? 45.457  -7.447  2.201   1.00 34.34 ? 350 HOH A O   1 
HETATM 7417 O O   . HOH E 2 .   ? 32.035  -10.312 1.153   1.00 32.21 ? 351 HOH A O   1 
HETATM 7418 O O   . HOH E 2 .   ? -1.102  -5.226  16.956  1.00 25.24 ? 352 HOH A O   1 
HETATM 7419 O O   . HOH E 2 .   ? 2.807   -8.706  19.746  1.00 27.82 ? 353 HOH A O   1 
HETATM 7420 O O   . HOH E 2 .   ? 0.919   -6.688  24.866  1.00 28.05 ? 354 HOH A O   1 
HETATM 7421 O O   . HOH E 2 .   ? 38.878  4.373   -5.527  1.00 28.96 ? 355 HOH A O   1 
HETATM 7422 O O   . HOH E 2 .   ? -11.430 -4.561  18.936  1.00 56.29 ? 356 HOH A O   1 
HETATM 7423 O O   . HOH E 2 .   ? 9.161   -14.666 14.753  1.00 33.89 ? 357 HOH A O   1 
HETATM 7424 O O   . HOH E 2 .   ? 3.375   2.436   0.986   1.00 27.44 ? 358 HOH A O   1 
HETATM 7425 O O   . HOH E 2 .   ? 21.183  -12.902 16.647  1.00 38.61 ? 359 HOH A O   1 
HETATM 7426 O O   . HOH E 2 .   ? 46.957  -0.812  -6.328  1.00 36.26 ? 360 HOH A O   1 
HETATM 7427 O O   . HOH E 2 .   ? 15.348  7.285   -2.027  1.00 25.83 ? 361 HOH A O   1 
HETATM 7428 O O   . HOH E 2 .   ? 16.779  10.914  -4.492  1.00 36.55 ? 362 HOH A O   1 
HETATM 7429 O O   . HOH E 2 .   ? -4.390  3.526   5.454   1.00 40.42 ? 363 HOH A O   1 
HETATM 7430 O O   . HOH E 2 .   ? -6.114  2.924   10.556  1.00 37.17 ? 364 HOH A O   1 
HETATM 7431 O O   . HOH E 2 .   ? -0.360  8.555   16.999  1.00 33.14 ? 365 HOH A O   1 
HETATM 7432 O O   . HOH E 2 .   ? 40.349  -6.539  -2.339  1.00 38.24 ? 366 HOH A O   1 
HETATM 7433 O O   . HOH E 2 .   ? 2.588   7.804   17.009  1.00 30.60 ? 367 HOH A O   1 
HETATM 7434 O O   . HOH E 2 .   ? 25.579  -3.981  -3.084  1.00 32.27 ? 368 HOH A O   1 
HETATM 7435 O O   . HOH E 2 .   ? 4.120   -15.223 11.124  1.00 36.09 ? 369 HOH A O   1 
HETATM 7436 O O   . HOH E 2 .   ? 27.131  -1.909  -4.953  1.00 33.24 ? 370 HOH A O   1 
HETATM 7437 O O   . HOH E 2 .   ? 13.423  7.917   -5.344  1.00 33.51 ? 371 HOH A O   1 
HETATM 7438 O O   . HOH E 2 .   ? -7.024  1.232   13.130  1.00 32.64 ? 372 HOH A O   1 
HETATM 7439 O O   . HOH E 2 .   ? 14.939  12.890  1.119   1.00 33.33 ? 373 HOH A O   1 
HETATM 7440 O O   . HOH E 2 .   ? 33.329  10.238  5.452   1.00 31.79 ? 374 HOH A O   1 
HETATM 7441 O O   . HOH E 2 .   ? 20.552  6.832   -8.806  1.00 50.16 ? 375 HOH A O   1 
HETATM 7442 O O   . HOH E 2 .   ? 26.990  -14.173 -4.954  1.00 58.69 ? 376 HOH A O   1 
HETATM 7443 O O   . HOH E 2 .   ? -1.598  -12.068 11.502  1.00 36.10 ? 377 HOH A O   1 
HETATM 7444 O O   . HOH E 2 .   ? 42.024  2.708   8.636   1.00 50.76 ? 378 HOH A O   1 
HETATM 7445 O O   . HOH E 2 .   ? 17.006  -11.827 -6.022  1.00 50.18 ? 379 HOH A O   1 
HETATM 7446 O O   . HOH E 2 .   ? 6.661   -12.618 -6.574  1.00 31.58 ? 380 HOH A O   1 
HETATM 7447 O O   . HOH E 2 .   ? 34.737  5.153   -10.648 1.00 33.03 ? 381 HOH A O   1 
HETATM 7448 O O   . HOH E 2 .   ? 38.414  -4.465  -4.764  1.00 40.14 ? 382 HOH A O   1 
HETATM 7449 O O   . HOH E 2 .   ? 39.421  3.362   -8.107  1.00 44.14 ? 383 HOH A O   1 
HETATM 7450 O O   . HOH E 2 .   ? 24.753  0.527   -1.341  1.00 27.77 ? 384 HOH A O   1 
HETATM 7451 O O   . HOH E 2 .   ? 25.878  0.348   -3.964  1.00 32.56 ? 385 HOH A O   1 
HETATM 7452 O O   . HOH E 2 .   ? -5.037  0.871   6.916   1.00 38.99 ? 386 HOH A O   1 
HETATM 7453 O O   . HOH E 2 .   ? 19.243  10.798  19.715  1.00 56.74 ? 387 HOH A O   1 
HETATM 7454 O O   . HOH E 2 .   ? 6.601   -2.222  26.456  1.00 33.06 ? 388 HOH A O   1 
HETATM 7455 O O   . HOH E 2 .   ? 48.859  -0.594  -0.578  1.00 39.05 ? 389 HOH A O   1 
HETATM 7456 O O   . HOH E 2 .   ? -0.895  -8.491  2.776   1.00 30.33 ? 390 HOH A O   1 
HETATM 7457 O O   . HOH E 2 .   ? 23.141  6.556   14.025  1.00 43.20 ? 391 HOH A O   1 
HETATM 7458 O O   . HOH E 2 .   ? -4.751  -1.271  19.672  1.00 34.06 ? 392 HOH A O   1 
HETATM 7459 O O   . HOH E 2 .   ? 5.324   12.239  20.324  1.00 46.13 ? 393 HOH A O   1 
HETATM 7460 O O   . HOH E 2 .   ? 31.072  -11.044 10.954  1.00 38.99 ? 394 HOH A O   1 
HETATM 7461 O O   . HOH E 2 .   ? 23.491  1.362   14.582  1.00 40.86 ? 395 HOH A O   1 
HETATM 7462 O O   . HOH E 2 .   ? 30.051  1.514   13.302  1.00 46.73 ? 396 HOH A O   1 
HETATM 7463 O O   . HOH E 2 .   ? 35.445  -7.294  1.727   1.00 38.61 ? 397 HOH A O   1 
HETATM 7464 O O   . HOH E 2 .   ? 27.519  -0.283  9.357   1.00 32.61 ? 398 HOH A O   1 
HETATM 7465 O O   . HOH E 2 .   ? 33.241  13.688  -0.451  1.00 36.52 ? 399 HOH A O   1 
HETATM 7466 O O   . HOH E 2 .   ? -0.884  0.219   21.242  1.00 32.41 ? 400 HOH A O   1 
HETATM 7467 O O   . HOH E 2 .   ? 2.231   5.483   2.730   1.00 28.87 ? 401 HOH A O   1 
HETATM 7468 O O   . HOH E 2 .   ? 23.169  -0.592  -5.130  1.00 38.38 ? 402 HOH A O   1 
HETATM 7469 O O   . HOH E 2 .   ? 8.524   7.487   -4.828  1.00 37.82 ? 403 HOH A O   1 
HETATM 7470 O O   . HOH E 2 .   ? 15.573  13.085  3.145   1.00 43.80 ? 404 HOH A O   1 
HETATM 7471 O O   . HOH E 2 .   ? 28.730  14.357  3.364   1.00 36.55 ? 405 HOH A O   1 
HETATM 7472 O O   . HOH E 2 .   ? 8.670   -7.045  25.067  1.00 35.26 ? 406 HOH A O   1 
HETATM 7473 O O   . HOH E 2 .   ? 20.747  -2.835  18.877  1.00 49.76 ? 407 HOH A O   1 
HETATM 7474 O O   . HOH E 2 .   ? 19.225  9.410   22.032  1.00 60.21 ? 408 HOH A O   1 
HETATM 7475 O O   . HOH E 2 .   ? 42.452  5.401   8.103   1.00 48.68 ? 409 HOH A O   1 
HETATM 7476 O O   . HOH E 2 .   ? 15.015  12.992  12.998  1.00 39.04 ? 410 HOH A O   1 
HETATM 7477 O O   . HOH E 2 .   ? 18.462  7.491   -7.271  1.00 41.40 ? 411 HOH A O   1 
HETATM 7478 O O   . HOH E 2 .   ? 30.155  13.858  -7.814  1.00 41.43 ? 412 HOH A O   1 
HETATM 7479 O O   . HOH E 2 .   ? 13.176  12.018  14.986  1.00 36.51 ? 413 HOH A O   1 
HETATM 7480 O O   . HOH E 2 .   ? 0.823   -4.937  27.082  1.00 41.17 ? 414 HOH A O   1 
HETATM 7481 O O   . HOH E 2 .   ? 10.064  -14.929 2.127   1.00 44.24 ? 415 HOH A O   1 
HETATM 7482 O O   . HOH E 2 .   ? 29.692  -0.184  10.821  1.00 49.10 ? 416 HOH A O   1 
HETATM 7483 O O   . HOH E 2 .   ? 1.030   8.986   5.175   1.00 39.63 ? 417 HOH A O   1 
HETATM 7484 O O   . HOH E 2 .   ? 31.213  13.727  -2.334  1.00 49.26 ? 418 HOH A O   1 
HETATM 7485 O O   . HOH E 2 .   ? 4.876   6.672   -7.058  1.00 54.75 ? 419 HOH A O   1 
HETATM 7486 O O   . HOH E 2 .   ? 36.797  -6.738  3.452   1.00 39.04 ? 420 HOH A O   1 
HETATM 7487 O O   . HOH E 2 .   ? 24.958  8.576   16.039  1.00 51.95 ? 421 HOH A O   1 
HETATM 7488 O O   . HOH E 2 .   ? -4.499  5.114   20.998  1.00 47.78 ? 422 HOH A O   1 
HETATM 7489 O O   . HOH E 2 .   ? -2.734  -8.432  0.293   1.00 47.09 ? 423 HOH A O   1 
HETATM 7490 O O   . HOH E 2 .   ? 46.281  -9.805  7.665   1.00 51.73 ? 424 HOH A O   1 
HETATM 7491 O O   . HOH E 2 .   ? -3.859  -1.489  6.547   1.00 48.39 ? 425 HOH A O   1 
HETATM 7492 O O   . HOH E 2 .   ? 16.012  13.095  10.665  1.00 47.26 ? 426 HOH A O   1 
HETATM 7493 O O   . HOH E 2 .   ? 23.097  -1.854  -6.670  1.00 54.15 ? 427 HOH A O   1 
HETATM 7494 O O   . HOH E 2 .   ? 7.913   -16.510 13.545  1.00 38.24 ? 428 HOH A O   1 
HETATM 7495 O O   . HOH E 2 .   ? -5.020  2.213   -7.118  1.00 53.51 ? 429 HOH A O   1 
HETATM 7496 O O   . HOH E 2 .   ? 19.574  5.331   20.294  1.00 54.04 ? 430 HOH A O   1 
HETATM 7497 O O   . HOH E 2 .   ? 25.015  -0.744  9.162   1.00 45.78 ? 431 HOH A O   1 
HETATM 7498 O O   . HOH E 2 .   ? 3.951   12.768  3.820   1.00 46.48 ? 432 HOH A O   1 
HETATM 7499 O O   . HOH E 2 .   ? 4.482   13.633  2.021   1.00 42.27 ? 433 HOH A O   1 
HETATM 7500 O O   . HOH E 2 .   ? 1.681   2.357   3.084   1.00 32.53 ? 434 HOH A O   1 
HETATM 7501 O O   . HOH E 2 .   ? 20.490  -15.257 6.911   1.00 46.22 ? 435 HOH A O   1 
HETATM 7502 O O   . HOH E 2 .   ? 19.621  -14.799 4.915   1.00 53.99 ? 436 HOH A O   1 
HETATM 7503 O O   . HOH E 2 .   ? 36.401  3.772   18.910  1.00 49.52 ? 437 HOH A O   1 
HETATM 7504 O O   . HOH E 2 .   ? 24.896  -14.453 -6.182  1.00 53.80 ? 438 HOH A O   1 
HETATM 7505 O O   . HOH E 2 .   ? -4.019  3.569   -8.403  1.00 47.80 ? 439 HOH A O   1 
HETATM 7506 O O   . HOH E 2 .   ? 16.325  12.917  15.324  1.00 36.44 ? 440 HOH A O   1 
HETATM 7507 O O   . HOH E 2 .   ? -0.674  0.299   23.668  1.00 44.24 ? 441 HOH A O   1 
HETATM 7508 O O   . HOH E 2 .   ? 31.444  16.589  4.177   1.00 50.45 ? 442 HOH A O   1 
HETATM 7509 O O   . HOH E 2 .   ? 1.423   14.702  0.144   1.00 43.14 ? 443 HOH A O   1 
HETATM 7510 O O   . HOH E 2 .   ? 23.514  -12.671 16.257  1.00 49.28 ? 444 HOH A O   1 
HETATM 7511 O O   . HOH E 2 .   ? -5.212  11.015  6.876   1.00 47.08 ? 445 HOH A O   1 
HETATM 7512 O O   . HOH E 2 .   ? 31.125  6.687   15.840  1.00 47.55 ? 446 HOH A O   1 
HETATM 7513 O O   . HOH E 2 .   ? 3.058   13.966  -5.166  1.00 51.21 ? 447 HOH A O   1 
HETATM 7514 O O   . HOH E 2 .   ? 18.704  12.121  15.035  1.00 45.37 ? 448 HOH A O   1 
HETATM 7515 O O   . HOH E 2 .   ? 34.400  -7.708  3.463   1.00 50.70 ? 449 HOH A O   1 
HETATM 7516 O O   . HOH E 2 .   ? 21.672  8.322   12.382  1.00 50.51 ? 450 HOH A O   1 
HETATM 7517 O O   . HOH E 2 .   ? 6.868   6.717   -6.505  1.00 43.84 ? 451 HOH A O   1 
HETATM 7518 O O   . HOH F 2 .   ? 34.689  -1.757  -51.258 1.00 41.15 ? 301 HOH B O   1 
HETATM 7519 O O   . HOH F 2 .   ? 17.354  2.877   -52.882 1.00 45.25 ? 302 HOH B O   1 
HETATM 7520 O O   . HOH F 2 .   ? 32.105  6.483   -55.125 1.00 51.52 ? 303 HOH B O   1 
HETATM 7521 O O   . HOH F 2 .   ? 43.033  18.056  -44.124 1.00 52.94 ? 304 HOH B O   1 
HETATM 7522 O O   . HOH F 2 .   ? 21.141  -12.595 -46.037 1.00 47.32 ? 305 HOH B O   1 
HETATM 7523 O O   . HOH F 2 .   ? 33.465  7.078   -56.933 1.00 52.63 ? 306 HOH B O   1 
HETATM 7524 O O   . HOH F 2 .   ? 25.480  -7.019  -34.273 1.00 52.10 ? 307 HOH B O   1 
HETATM 7525 O O   . HOH F 2 .   ? 11.834  13.343  -49.060 1.00 53.51 ? 308 HOH B O   1 
HETATM 7526 O O   . HOH F 2 .   ? 18.463  19.445  -39.901 1.00 31.78 ? 309 HOH B O   1 
HETATM 7527 O O   . HOH F 2 .   ? 14.564  -13.211 -27.003 1.00 54.42 ? 310 HOH B O   1 
HETATM 7528 O O   . HOH F 2 .   ? 34.023  16.455  -40.643 1.00 32.45 ? 311 HOH B O   1 
HETATM 7529 O O   . HOH F 2 .   ? -5.785  5.066   -30.229 1.00 36.62 ? 312 HOH B O   1 
HETATM 7530 O O   . HOH F 2 .   ? 19.789  12.085  -48.237 1.00 27.40 ? 313 HOH B O   1 
HETATM 7531 O O   . HOH F 2 .   ? 30.693  14.534  -36.569 1.00 31.16 ? 314 HOH B O   1 
HETATM 7532 O O   . HOH F 2 .   ? 2.882   -2.351  -34.379 1.00 27.72 ? 315 HOH B O   1 
HETATM 7533 O O   . HOH F 2 .   ? 9.647   11.329  -48.506 1.00 41.51 ? 316 HOH B O   1 
HETATM 7534 O O   . HOH F 2 .   ? 10.417  -10.900 -28.813 1.00 39.95 ? 317 HOH B O   1 
HETATM 7535 O O   . HOH F 2 .   ? -2.760  13.144  -28.246 1.00 35.19 ? 318 HOH B O   1 
HETATM 7536 O O   . HOH F 2 .   ? 2.887   9.708   -38.233 1.00 32.01 ? 319 HOH B O   1 
HETATM 7537 O O   . HOH F 2 .   ? 4.354   -6.960  -26.640 1.00 44.89 ? 320 HOH B O   1 
HETATM 7538 O O   . HOH F 2 .   ? 16.767  10.352  -52.058 1.00 42.66 ? 321 HOH B O   1 
HETATM 7539 O O   . HOH F 2 .   ? 7.588   11.815  -29.173 1.00 23.17 ? 322 HOH B O   1 
HETATM 7540 O O   . HOH F 2 .   ? 28.632  -7.979  -35.412 1.00 36.42 ? 323 HOH B O   1 
HETATM 7541 O O   . HOH F 2 .   ? 4.634   6.265   -42.887 1.00 27.97 ? 324 HOH B O   1 
HETATM 7542 O O   . HOH F 2 .   ? 0.867   12.618  -26.646 1.00 33.53 ? 325 HOH B O   1 
HETATM 7543 O O   . HOH F 2 .   ? 43.779  12.617  -45.946 1.00 54.85 ? 326 HOH B O   1 
HETATM 7544 O O   . HOH F 2 .   ? 16.457  16.492  -42.464 1.00 31.83 ? 327 HOH B O   1 
HETATM 7545 O O   . HOH F 2 .   ? 25.435  10.941  -33.501 1.00 12.21 ? 328 HOH B O   1 
HETATM 7546 O O   . HOH F 2 .   ? 18.095  16.822  -40.528 1.00 41.15 ? 329 HOH B O   1 
HETATM 7547 O O   . HOH F 2 .   ? 26.843  6.663   -43.757 1.00 29.68 ? 330 HOH B O   1 
HETATM 7548 O O   . HOH F 2 .   ? 5.399   17.894  -35.073 1.00 42.42 ? 331 HOH B O   1 
HETATM 7549 O O   . HOH F 2 .   ? 4.893   -10.676 -35.440 1.00 43.63 ? 332 HOH B O   1 
HETATM 7550 O O   . HOH F 2 .   ? 24.771  0.101   -35.097 1.00 42.76 ? 333 HOH B O   1 
HETATM 7551 O O   . HOH F 2 .   ? 16.678  10.986  -45.722 1.00 27.33 ? 334 HOH B O   1 
HETATM 7552 O O   . HOH F 2 .   ? 33.258  -6.535  -42.589 1.00 31.74 ? 335 HOH B O   1 
HETATM 7553 O O   . HOH F 2 .   ? 28.496  1.635   -48.231 1.00 33.16 ? 336 HOH B O   1 
HETATM 7554 O O   . HOH F 2 .   ? 20.984  3.527   -52.187 1.00 40.64 ? 337 HOH B O   1 
HETATM 7555 O O   . HOH F 2 .   ? 43.123  6.151   -34.354 1.00 45.74 ? 338 HOH B O   1 
HETATM 7556 O O   . HOH F 2 .   ? 17.877  9.468   -42.092 1.00 25.43 ? 339 HOH B O   1 
HETATM 7557 O O   . HOH F 2 .   ? 12.160  13.677  -23.599 1.00 37.80 ? 340 HOH B O   1 
HETATM 7558 O O   . HOH F 2 .   ? 10.294  2.471   -16.587 1.00 40.05 ? 341 HOH B O   1 
HETATM 7559 O O   . HOH F 2 .   ? 30.489  10.054  -49.038 1.00 30.93 ? 342 HOH B O   1 
HETATM 7560 O O   . HOH F 2 .   ? 8.066   -8.854  -50.181 1.00 27.64 ? 343 HOH B O   1 
HETATM 7561 O O   . HOH F 2 .   ? 21.664  5.803   -50.448 1.00 34.86 ? 344 HOH B O   1 
HETATM 7562 O O   . HOH F 2 .   ? 7.349   8.629   -20.626 1.00 36.20 ? 345 HOH B O   1 
HETATM 7563 O O   . HOH F 2 .   ? 19.103  -14.060 -30.739 1.00 58.82 ? 346 HOH B O   1 
HETATM 7564 O O   . HOH F 2 .   ? 9.945   -12.571 -34.564 1.00 45.08 ? 347 HOH B O   1 
HETATM 7565 O O   . HOH F 2 .   ? 42.029  14.295  -38.696 1.00 40.43 ? 348 HOH B O   1 
HETATM 7566 O O   . HOH F 2 .   ? -0.350  -8.140  -32.136 1.00 36.09 ? 349 HOH B O   1 
HETATM 7567 O O   . HOH F 2 .   ? 12.033  -8.233  -43.163 1.00 31.54 ? 350 HOH B O   1 
HETATM 7568 O O   . HOH F 2 .   ? 26.911  -0.175  -46.614 1.00 33.53 ? 351 HOH B O   1 
HETATM 7569 O O   . HOH F 2 .   ? 40.236  8.062   -48.965 1.00 29.94 ? 352 HOH B O   1 
HETATM 7570 O O   . HOH F 2 .   ? 41.697  -2.908  -45.669 1.00 36.24 ? 353 HOH B O   1 
HETATM 7571 O O   . HOH F 2 .   ? 0.568   2.575   -48.077 1.00 43.86 ? 354 HOH B O   1 
HETATM 7572 O O   . HOH F 2 .   ? 3.872   11.605  -26.674 1.00 34.65 ? 355 HOH B O   1 
HETATM 7573 O O   . HOH F 2 .   ? 34.830  17.379  -43.785 1.00 36.06 ? 356 HOH B O   1 
HETATM 7574 O O   . HOH F 2 .   ? 32.919  19.014  -38.289 1.00 43.74 ? 357 HOH B O   1 
HETATM 7575 O O   . HOH F 2 .   ? 28.861  3.444   -34.428 1.00 30.13 ? 358 HOH B O   1 
HETATM 7576 O O   . HOH F 2 .   ? 0.212   -1.493  -26.654 1.00 30.23 ? 359 HOH B O   1 
HETATM 7577 O O   . HOH F 2 .   ? 7.779   1.476   -17.269 1.00 38.83 ? 360 HOH B O   1 
HETATM 7578 O O   . HOH F 2 .   ? 3.666   9.243   -40.801 1.00 29.20 ? 361 HOH B O   1 
HETATM 7579 O O   . HOH F 2 .   ? 46.582  -3.680  -41.435 1.00 31.94 ? 362 HOH B O   1 
HETATM 7580 O O   . HOH F 2 .   ? 0.567   -4.852  -40.581 1.00 33.17 ? 363 HOH B O   1 
HETATM 7581 O O   . HOH F 2 .   ? 17.962  14.603  -48.175 1.00 44.65 ? 364 HOH B O   1 
HETATM 7582 O O   . HOH F 2 .   ? 27.128  4.083   -47.440 1.00 32.13 ? 365 HOH B O   1 
HETATM 7583 O O   . HOH F 2 .   ? 26.602  5.677   -41.024 1.00 26.55 ? 366 HOH B O   1 
HETATM 7584 O O   . HOH F 2 .   ? 43.805  9.262   -35.183 1.00 45.49 ? 367 HOH B O   1 
HETATM 7585 O O   . HOH F 2 .   ? 30.601  18.767  -53.475 1.00 52.90 ? 368 HOH B O   1 
HETATM 7586 O O   . HOH F 2 .   ? -2.346  8.842   -43.284 1.00 49.84 ? 369 HOH B O   1 
HETATM 7587 O O   . HOH F 2 .   ? 32.191  -7.170  -32.678 1.00 42.62 ? 370 HOH B O   1 
HETATM 7588 O O   . HOH F 2 .   ? 14.718  11.862  -48.987 1.00 32.16 ? 371 HOH B O   1 
HETATM 7589 O O   . HOH F 2 .   ? 20.340  13.267  -22.063 1.00 55.11 ? 372 HOH B O   1 
HETATM 7590 O O   . HOH F 2 .   ? 22.479  -9.074  -26.680 1.00 38.19 ? 373 HOH B O   1 
HETATM 7591 O O   . HOH F 2 .   ? 2.588   16.571  -45.665 1.00 47.36 ? 374 HOH B O   1 
HETATM 7592 O O   . HOH F 2 .   ? 20.251  11.941  -24.444 1.00 59.30 ? 375 HOH B O   1 
HETATM 7593 O O   . HOH F 2 .   ? 5.930   -11.504 -32.509 1.00 37.70 ? 376 HOH B O   1 
HETATM 7594 O O   . HOH F 2 .   ? -3.054  7.415   -38.235 1.00 39.62 ? 377 HOH B O   1 
HETATM 7595 O O   . HOH F 2 .   ? -0.348  -4.328  -23.485 1.00 50.85 ? 378 HOH B O   1 
HETATM 7596 O O   . HOH F 2 .   ? 7.250   17.958  -42.808 1.00 37.18 ? 379 HOH B O   1 
HETATM 7597 O O   . HOH F 2 .   ? 34.477  14.008  -38.379 1.00 33.43 ? 380 HOH B O   1 
HETATM 7598 O O   . HOH F 2 .   ? 48.120  2.943   -50.113 1.00 36.16 ? 381 HOH B O   1 
HETATM 7599 O O   . HOH F 2 .   ? 30.094  18.057  -40.471 1.00 35.71 ? 382 HOH B O   1 
HETATM 7600 O O   . HOH F 2 .   ? -5.021  6.618   -33.022 1.00 44.84 ? 383 HOH B O   1 
HETATM 7601 O O   . HOH F 2 .   ? 10.513  19.825  -28.261 1.00 35.37 ? 384 HOH B O   1 
HETATM 7602 O O   . HOH F 2 .   ? 36.150  5.041   -28.943 1.00 32.38 ? 385 HOH B O   1 
HETATM 7603 O O   . HOH F 2 .   ? 46.227  4.248   -36.979 1.00 46.24 ? 386 HOH B O   1 
HETATM 7604 O O   . HOH F 2 .   ? 25.913  12.538  -27.254 1.00 52.54 ? 387 HOH B O   1 
HETATM 7605 O O   . HOH F 2 .   ? 24.502  3.302   -48.719 1.00 33.85 ? 388 HOH B O   1 
HETATM 7606 O O   . HOH F 2 .   ? 36.087  8.999   -54.286 1.00 36.80 ? 389 HOH B O   1 
HETATM 7607 O O   . HOH F 2 .   ? 0.537   3.979   -22.353 1.00 39.70 ? 390 HOH B O   1 
HETATM 7608 O O   . HOH F 2 .   ? 27.835  -2.465  -30.454 1.00 36.72 ? 391 HOH B O   1 
HETATM 7609 O O   . HOH F 2 .   ? 6.633   16.453  -23.295 1.00 40.57 ? 392 HOH B O   1 
HETATM 7610 O O   . HOH F 2 .   ? 26.174  4.351   -44.967 1.00 28.95 ? 393 HOH B O   1 
HETATM 7611 O O   . HOH F 2 .   ? 24.998  5.167   -28.977 1.00 40.48 ? 394 HOH B O   1 
HETATM 7612 O O   . HOH F 2 .   ? -3.462  2.460   -23.816 1.00 35.67 ? 395 HOH B O   1 
HETATM 7613 O O   . HOH F 2 .   ? 21.063  -2.015  -51.077 1.00 41.73 ? 396 HOH B O   1 
HETATM 7614 O O   . HOH F 2 .   ? 24.810  10.831  -53.743 1.00 39.97 ? 397 HOH B O   1 
HETATM 7615 O O   . HOH F 2 .   ? 40.781  6.707   -51.496 1.00 45.56 ? 398 HOH B O   1 
HETATM 7616 O O   . HOH F 2 .   ? 36.946  -6.094  -33.485 1.00 47.55 ? 399 HOH B O   1 
HETATM 7617 O O   . HOH F 2 .   ? 33.622  2.264   -53.172 1.00 42.77 ? 400 HOH B O   1 
HETATM 7618 O O   . HOH F 2 .   ? 5.975   2.295   -14.830 1.00 54.75 ? 401 HOH B O   1 
HETATM 7619 O O   . HOH F 2 .   ? -1.324  -2.401  -36.524 1.00 31.25 ? 402 HOH B O   1 
HETATM 7620 O O   . HOH F 2 .   ? 23.862  1.321   -50.245 1.00 43.30 ? 403 HOH B O   1 
HETATM 7621 O O   . HOH F 2 .   ? 40.907  19.774  -38.864 1.00 46.19 ? 404 HOH B O   1 
HETATM 7622 O O   . HOH F 2 .   ? 19.971  11.012  -51.048 1.00 48.86 ? 405 HOH B O   1 
HETATM 7623 O O   . HOH F 2 .   ? 32.722  17.769  -46.501 1.00 54.68 ? 406 HOH B O   1 
HETATM 7624 O O   . HOH F 2 .   ? -1.294  -2.718  -25.031 1.00 40.04 ? 407 HOH B O   1 
HETATM 7625 O O   . HOH F 2 .   ? 21.774  10.431  -52.765 1.00 49.07 ? 408 HOH B O   1 
HETATM 7626 O O   . HOH F 2 .   ? 18.396  -8.230  -22.286 1.00 52.05 ? 409 HOH B O   1 
HETATM 7627 O O   . HOH F 2 .   ? 2.941   13.059  -38.232 1.00 40.25 ? 410 HOH B O   1 
HETATM 7628 O O   . HOH F 2 .   ? 38.745  8.404   -54.581 1.00 50.65 ? 411 HOH B O   1 
HETATM 7629 O O   . HOH F 2 .   ? 0.804   4.713   -40.619 1.00 41.98 ? 412 HOH B O   1 
HETATM 7630 O O   . HOH F 2 .   ? 12.500  15.434  -49.329 1.00 49.85 ? 413 HOH B O   1 
HETATM 7631 O O   . HOH F 2 .   ? 31.707  17.912  -51.235 1.00 44.86 ? 414 HOH B O   1 
HETATM 7632 O O   . HOH F 2 .   ? 0.168   3.949   -38.813 1.00 44.36 ? 415 HOH B O   1 
HETATM 7633 O O   . HOH F 2 .   ? -1.416  10.745  -41.463 1.00 48.47 ? 416 HOH B O   1 
HETATM 7634 O O   . HOH F 2 .   ? 32.121  -9.362  -42.288 1.00 47.97 ? 417 HOH B O   1 
HETATM 7635 O O   . HOH F 2 .   ? -1.677  -4.491  -44.227 1.00 47.69 ? 418 HOH B O   1 
HETATM 7636 O O   . HOH F 2 .   ? 26.214  2.740   -34.329 1.00 36.27 ? 419 HOH B O   1 
HETATM 7637 O O   . HOH F 2 .   ? 17.919  16.695  -27.982 1.00 38.05 ? 420 HOH B O   1 
HETATM 7638 O O   . HOH F 2 .   ? 23.230  12.195  -31.707 1.00 48.88 ? 421 HOH B O   1 
HETATM 7639 O O   . HOH F 2 .   ? 8.518   10.524  -50.177 1.00 48.65 ? 422 HOH B O   1 
HETATM 7640 O O   . HOH F 2 .   ? -5.086  15.458  -35.517 1.00 49.99 ? 423 HOH B O   1 
HETATM 7641 O O   . HOH F 2 .   ? 3.008   6.189   -40.684 1.00 43.72 ? 424 HOH B O   1 
HETATM 7642 O O   . HOH F 2 .   ? 33.156  20.571  -39.678 1.00 44.26 ? 425 HOH B O   1 
HETATM 7643 O O   . HOH F 2 .   ? 29.433  19.037  -42.217 1.00 47.00 ? 426 HOH B O   1 
HETATM 7644 O O   . HOH F 2 .   ? 6.837   -16.235 -28.356 1.00 54.51 ? 427 HOH B O   1 
HETATM 7645 O O   . HOH F 2 .   ? 24.982  -9.054  -27.157 1.00 46.06 ? 428 HOH B O   1 
HETATM 7646 O O   . HOH F 2 .   ? -2.353  -2.671  -40.480 1.00 48.83 ? 429 HOH B O   1 
HETATM 7647 O O   . HOH F 2 .   ? 32.527  5.864   -59.431 1.00 55.05 ? 430 HOH B O   1 
HETATM 7648 O O   . HOH F 2 .   ? -1.097  -3.707  -38.363 1.00 39.38 ? 431 HOH B O   1 
HETATM 7649 O O   . HOH F 2 .   ? 45.117  10.692  -36.106 1.00 51.16 ? 432 HOH B O   1 
HETATM 7650 O O   . HOH F 2 .   ? 8.664   -15.827 -30.145 1.00 57.11 ? 433 HOH B O   1 
HETATM 7651 O O   . HOH G 2 .   ? 30.025  40.213  18.313  1.00 53.50 ? 301 HOH C O   1 
HETATM 7652 O O   . HOH G 2 .   ? -10.695 34.353  11.766  1.00 47.04 ? 302 HOH C O   1 
HETATM 7653 O O   . HOH G 2 .   ? 17.556  15.733  20.045  1.00 50.15 ? 303 HOH C O   1 
HETATM 7654 O O   . HOH G 2 .   ? 39.452  12.053  7.740   1.00 43.16 ? 304 HOH C O   1 
HETATM 7655 O O   . HOH G 2 .   ? -11.240 28.852  2.950   1.00 54.08 ? 305 HOH C O   1 
HETATM 7656 O O   . HOH G 2 .   ? 0.114   30.417  -3.503  1.00 56.35 ? 306 HOH C O   1 
HETATM 7657 O O   . HOH G 2 .   ? 16.396  18.739  21.480  1.00 45.85 ? 307 HOH C O   1 
HETATM 7658 O O   . HOH G 2 .   ? 26.579  30.849  -5.388  1.00 48.02 ? 308 HOH C O   1 
HETATM 7659 O O   . HOH G 2 .   ? 6.947   25.978  15.469  1.00 25.51 ? 309 HOH C O   1 
HETATM 7660 O O   . HOH G 2 .   ? 29.074  13.508  5.681   1.00 35.25 ? 310 HOH C O   1 
HETATM 7661 O O   . HOH G 2 .   ? 23.107  39.810  22.801  1.00 43.38 ? 311 HOH C O   1 
HETATM 7662 O O   . HOH G 2 .   ? 11.292  31.920  -2.476  1.00 38.69 ? 312 HOH C O   1 
HETATM 7663 O O   . HOH G 2 .   ? 1.175   30.710  -6.040  1.00 45.35 ? 313 HOH C O   1 
HETATM 7664 O O   . HOH G 2 .   ? 32.693  32.390  12.591  1.00 31.14 ? 314 HOH C O   1 
HETATM 7665 O O   . HOH G 2 .   ? 33.719  32.432  0.443   1.00 34.49 ? 315 HOH C O   1 
HETATM 7666 O O   . HOH G 2 .   ? 4.461   16.336  10.499  1.00 29.78 ? 316 HOH C O   1 
HETATM 7667 O O   . HOH G 2 .   ? 11.226  29.640  15.539  1.00 39.54 ? 317 HOH C O   1 
HETATM 7668 O O   . HOH G 2 .   ? 10.462  36.114  18.590  1.00 33.90 ? 318 HOH C O   1 
HETATM 7669 O O   . HOH G 2 .   ? 28.661  17.167  13.716  1.00 26.57 ? 319 HOH C O   1 
HETATM 7670 O O   . HOH G 2 .   ? 29.151  28.778  26.502  1.00 40.11 ? 320 HOH C O   1 
HETATM 7671 O O   . HOH G 2 .   ? 26.958  38.179  21.925  1.00 43.67 ? 321 HOH C O   1 
HETATM 7672 O O   . HOH G 2 .   ? 0.127   15.683  6.694   1.00 29.52 ? 322 HOH C O   1 
HETATM 7673 O O   . HOH G 2 .   ? 16.610  22.762  0.624   1.00 26.71 ? 323 HOH C O   1 
HETATM 7674 O O   . HOH G 2 .   ? 12.876  22.544  -1.590  1.00 30.36 ? 324 HOH C O   1 
HETATM 7675 O O   . HOH G 2 .   ? -10.605 20.167  5.041   1.00 36.67 ? 325 HOH C O   1 
HETATM 7676 O O   . HOH G 2 .   ? 7.389   37.263  18.492  1.00 35.20 ? 326 HOH C O   1 
HETATM 7677 O O   . HOH G 2 .   ? 39.115  15.861  12.341  1.00 42.61 ? 327 HOH C O   1 
HETATM 7678 O O   . HOH G 2 .   ? 31.108  11.329  17.312  1.00 47.00 ? 328 HOH C O   1 
HETATM 7679 O O   . HOH G 2 .   ? -2.481  38.108  6.272   1.00 34.02 ? 329 HOH C O   1 
HETATM 7680 O O   . HOH G 2 .   ? 30.895  17.499  22.597  1.00 38.53 ? 330 HOH C O   1 
HETATM 7681 O O   . HOH G 2 .   ? 10.332  18.936  13.538  1.00 11.10 ? 331 HOH C O   1 
HETATM 7682 O O   . HOH G 2 .   ? 40.276  23.651  9.482   1.00 43.68 ? 332 HOH C O   1 
HETATM 7683 O O   . HOH G 2 .   ? 24.349  9.343   14.232  1.00 48.99 ? 333 HOH C O   1 
HETATM 7684 O O   . HOH G 2 .   ? 14.583  10.763  -1.927  1.00 46.82 ? 334 HOH C O   1 
HETATM 7685 O O   . HOH G 2 .   ? 5.469   44.335  6.323   1.00 48.12 ? 335 HOH C O   1 
HETATM 7686 O O   . HOH G 2 .   ? 22.321  40.443  8.170   1.00 27.82 ? 336 HOH C O   1 
HETATM 7687 O O   . HOH G 2 .   ? -4.757  17.724  15.999  1.00 36.26 ? 337 HOH C O   1 
HETATM 7688 O O   . HOH G 2 .   ? 22.839  16.960  29.880  1.00 46.15 ? 338 HOH C O   1 
HETATM 7689 O O   . HOH G 2 .   ? 11.594  37.113  1.279   1.00 33.26 ? 339 HOH C O   1 
HETATM 7690 O O   . HOH G 2 .   ? 15.387  35.466  25.624  1.00 39.54 ? 340 HOH C O   1 
HETATM 7691 O O   . HOH G 2 .   ? 16.168  23.169  4.507   1.00 24.37 ? 341 HOH C O   1 
HETATM 7692 O O   . HOH G 2 .   ? -4.948  15.284  -4.284  1.00 55.24 ? 342 HOH C O   1 
HETATM 7693 O O   . HOH G 2 .   ? 36.791  29.112  18.857  1.00 35.27 ? 343 HOH C O   1 
HETATM 7694 O O   . HOH G 2 .   ? 31.573  21.782  4.917   1.00 36.98 ? 344 HOH C O   1 
HETATM 7695 O O   . HOH G 2 .   ? 40.943  24.595  19.400  1.00 37.98 ? 345 HOH C O   1 
HETATM 7696 O O   . HOH G 2 .   ? 6.918   33.390  5.173   1.00 27.94 ? 346 HOH C O   1 
HETATM 7697 O O   . HOH G 2 .   ? 25.271  13.301  19.210  1.00 38.85 ? 347 HOH C O   1 
HETATM 7698 O O   . HOH G 2 .   ? 4.846   35.432  21.328  1.00 36.59 ? 348 HOH C O   1 
HETATM 7699 O O   . HOH G 2 .   ? 29.120  26.815  2.518   1.00 28.27 ? 349 HOH C O   1 
HETATM 7700 O O   . HOH G 2 .   ? 2.172   24.644  0.468   1.00 30.97 ? 350 HOH C O   1 
HETATM 7701 O O   . HOH G 2 .   ? 20.140  18.295  30.026  1.00 45.79 ? 351 HOH C O   1 
HETATM 7702 O O   . HOH G 2 .   ? 11.080  29.223  -1.239  1.00 32.85 ? 352 HOH C O   1 
HETATM 7703 O O   . HOH G 2 .   ? 24.763  42.262  -1.076  1.00 52.98 ? 353 HOH C O   1 
HETATM 7704 O O   . HOH G 2 .   ? 35.812  16.057  14.598  1.00 41.01 ? 354 HOH C O   1 
HETATM 7705 O O   . HOH G 2 .   ? 5.028   32.444  3.163   1.00 24.73 ? 355 HOH C O   1 
HETATM 7706 O O   . HOH G 2 .   ? 0.483   36.881  4.684   1.00 44.79 ? 356 HOH C O   1 
HETATM 7707 O O   . HOH G 2 .   ? 4.042   14.448  5.880   1.00 33.82 ? 357 HOH C O   1 
HETATM 7708 O O   . HOH G 2 .   ? 0.243   17.256  9.800   1.00 27.82 ? 358 HOH C O   1 
HETATM 7709 O O   . HOH G 2 .   ? -7.231  28.192  -1.509  1.00 36.34 ? 359 HOH C O   1 
HETATM 7710 O O   . HOH G 2 .   ? 25.908  15.849  -0.711  1.00 34.73 ? 360 HOH C O   1 
HETATM 7711 O O   . HOH G 2 .   ? 22.859  10.370  8.818   1.00 30.31 ? 361 HOH C O   1 
HETATM 7712 O O   . HOH G 2 .   ? -7.175  26.261  2.970   1.00 29.35 ? 362 HOH C O   1 
HETATM 7713 O O   . HOH G 2 .   ? 6.187   29.873  3.065   1.00 25.99 ? 363 HOH C O   1 
HETATM 7714 O O   . HOH G 2 .   ? 42.067  24.500  12.330  1.00 36.70 ? 364 HOH C O   1 
HETATM 7715 O O   . HOH G 2 .   ? -3.909  31.475  6.384   1.00 30.71 ? 365 HOH C O   1 
HETATM 7716 O O   . HOH G 2 .   ? 0.845   22.793  21.500  1.00 32.40 ? 366 HOH C O   1 
HETATM 7717 O O   . HOH G 2 .   ? 34.851  21.610  -3.365  1.00 52.09 ? 367 HOH C O   1 
HETATM 7718 O O   . HOH G 2 .   ? 32.092  31.946  -2.231  1.00 37.39 ? 368 HOH C O   1 
HETATM 7719 O O   . HOH G 2 .   ? 7.795   28.763  4.992   1.00 26.66 ? 369 HOH C O   1 
HETATM 7720 O O   . HOH G 2 .   ? 38.361  18.436  20.536  1.00 48.02 ? 370 HOH C O   1 
HETATM 7721 O O   . HOH G 2 .   ? 8.678   30.817  1.711   1.00 34.40 ? 371 HOH C O   1 
HETATM 7722 O O   . HOH G 2 .   ? 8.040   26.237  8.275   1.00 23.95 ? 372 HOH C O   1 
HETATM 7723 O O   . HOH G 2 .   ? -3.414  33.465  13.969  1.00 34.66 ? 373 HOH C O   1 
HETATM 7724 O O   . HOH G 2 .   ? 32.752  16.650  15.646  1.00 37.56 ? 374 HOH C O   1 
HETATM 7725 O O   . HOH G 2 .   ? 1.920   12.360  8.106   1.00 36.53 ? 375 HOH C O   1 
HETATM 7726 O O   . HOH G 2 .   ? 37.076  22.771  21.513  1.00 42.01 ? 376 HOH C O   1 
HETATM 7727 O O   . HOH G 2 .   ? 30.586  23.258  28.236  1.00 41.64 ? 377 HOH C O   1 
HETATM 7728 O O   . HOH G 2 .   ? 14.669  25.823  -5.376  1.00 49.19 ? 378 HOH C O   1 
HETATM 7729 O O   . HOH G 2 .   ? 10.855  30.815  25.201  1.00 53.77 ? 379 HOH C O   1 
HETATM 7730 O O   . HOH G 2 .   ? 30.385  23.266  2.985   1.00 33.29 ? 380 HOH C O   1 
HETATM 7731 O O   . HOH G 2 .   ? 36.899  37.190  15.406  1.00 49.05 ? 381 HOH C O   1 
HETATM 7732 O O   . HOH G 2 .   ? -0.911  16.048  3.280   1.00 35.77 ? 382 HOH C O   1 
HETATM 7733 O O   . HOH G 2 .   ? -10.613 32.344  17.113  1.00 51.05 ? 383 HOH C O   1 
HETATM 7734 O O   . HOH G 2 .   ? 37.661  24.675  4.873   1.00 38.73 ? 384 HOH C O   1 
HETATM 7735 O O   . HOH G 2 .   ? -10.190 25.347  16.569  1.00 36.83 ? 385 HOH C O   1 
HETATM 7736 O O   . HOH G 2 .   ? 1.610   38.366  12.389  1.00 33.99 ? 386 HOH C O   1 
HETATM 7737 O O   . HOH G 2 .   ? 5.931   13.247  -5.670  1.00 41.26 ? 387 HOH C O   1 
HETATM 7738 O O   . HOH G 2 .   ? 12.065  18.366  17.223  1.00 37.49 ? 388 HOH C O   1 
HETATM 7739 O O   . HOH G 2 .   ? 11.110  16.245  10.553  1.00 31.32 ? 389 HOH C O   1 
HETATM 7740 O O   . HOH G 2 .   ? 5.426   29.605  -0.161  1.00 41.87 ? 390 HOH C O   1 
HETATM 7741 O O   . HOH G 2 .   ? 38.906  26.329  6.958   1.00 47.69 ? 391 HOH C O   1 
HETATM 7742 O O   . HOH G 2 .   ? 1.959   15.684  21.962  1.00 50.99 ? 392 HOH C O   1 
HETATM 7743 O O   . HOH G 2 .   ? 34.930  24.144  3.827   1.00 49.31 ? 393 HOH C O   1 
HETATM 7744 O O   . HOH G 2 .   ? -0.201  34.760  20.987  1.00 38.00 ? 394 HOH C O   1 
HETATM 7745 O O   . HOH G 2 .   ? 33.284  34.431  21.247  1.00 41.48 ? 395 HOH C O   1 
HETATM 7746 O O   . HOH G 2 .   ? 7.070   25.689  -5.149  1.00 36.26 ? 396 HOH C O   1 
HETATM 7747 O O   . HOH G 2 .   ? 9.098   30.798  21.481  1.00 44.85 ? 397 HOH C O   1 
HETATM 7748 O O   . HOH G 2 .   ? 12.188  23.191  19.268  1.00 38.94 ? 398 HOH C O   1 
HETATM 7749 O O   . HOH G 2 .   ? 7.847   37.063  0.161   1.00 38.11 ? 399 HOH C O   1 
HETATM 7750 O O   . HOH G 2 .   ? 21.336  12.985  14.334  1.00 46.59 ? 400 HOH C O   1 
HETATM 7751 O O   . HOH G 2 .   ? 29.600  42.070  10.878  1.00 43.43 ? 401 HOH C O   1 
HETATM 7752 O O   . HOH G 2 .   ? 36.518  33.663  9.813   1.00 48.41 ? 402 HOH C O   1 
HETATM 7753 O O   . HOH G 2 .   ? 0.570   16.785  1.525   1.00 42.87 ? 403 HOH C O   1 
HETATM 7754 O O   . HOH G 2 .   ? 17.773  23.119  -3.217  1.00 31.54 ? 404 HOH C O   1 
HETATM 7755 O O   . HOH G 2 .   ? 39.511  22.557  20.916  1.00 45.21 ? 405 HOH C O   1 
HETATM 7756 O O   . HOH G 2 .   ? 10.595  35.028  24.336  1.00 48.27 ? 406 HOH C O   1 
HETATM 7757 O O   . HOH G 2 .   ? -15.714 32.917  10.091  1.00 49.55 ? 407 HOH C O   1 
HETATM 7758 O O   . HOH G 2 .   ? -1.477  34.044  14.744  1.00 45.82 ? 408 HOH C O   1 
HETATM 7759 O O   . HOH G 2 .   ? 40.401  18.324  18.642  1.00 42.77 ? 409 HOH C O   1 
HETATM 7760 O O   . HOH G 2 .   ? 34.728  27.775  6.523   1.00 37.59 ? 410 HOH C O   1 
HETATM 7761 O O   . HOH G 2 .   ? 0.501   18.437  -4.303  1.00 39.90 ? 411 HOH C O   1 
HETATM 7762 O O   . HOH G 2 .   ? 31.838  19.544  3.961   1.00 45.96 ? 412 HOH C O   1 
HETATM 7763 O O   . HOH G 2 .   ? -1.525  33.844  19.159  1.00 47.28 ? 413 HOH C O   1 
HETATM 7764 O O   . HOH G 2 .   ? 29.423  28.209  28.477  1.00 53.11 ? 414 HOH C O   1 
HETATM 7765 O O   . HOH G 2 .   ? 18.397  13.208  10.486  1.00 38.70 ? 415 HOH C O   1 
HETATM 7766 O O   . HOH G 2 .   ? 33.846  39.193  17.451  1.00 56.21 ? 416 HOH C O   1 
HETATM 7767 O O   . HOH G 2 .   ? 3.784   29.584  22.794  1.00 44.08 ? 417 HOH C O   1 
HETATM 7768 O O   . HOH G 2 .   ? 4.395   14.969  3.579   1.00 51.09 ? 418 HOH C O   1 
HETATM 7769 O O   . HOH G 2 .   ? 42.186  16.204  12.848  1.00 54.42 ? 419 HOH C O   1 
HETATM 7770 O O   . HOH G 2 .   ? 16.038  15.344  17.013  1.00 38.68 ? 420 HOH C O   1 
HETATM 7771 O O   . HOH G 2 .   ? 33.414  27.404  3.870   1.00 42.54 ? 421 HOH C O   1 
HETATM 7772 O O   . HOH G 2 .   ? 14.452  9.486   -3.304  1.00 43.72 ? 422 HOH C O   1 
HETATM 7773 O O   . HOH G 2 .   ? 19.838  40.946  28.045  1.00 56.21 ? 423 HOH C O   1 
HETATM 7774 O O   . HOH G 2 .   ? 31.216  26.548  3.992   1.00 45.94 ? 424 HOH C O   1 
HETATM 7775 O O   . HOH G 2 .   ? 33.332  40.368  19.606  1.00 57.73 ? 425 HOH C O   1 
HETATM 7776 O O   . HOH G 2 .   ? 22.791  24.008  -4.061  1.00 39.68 ? 426 HOH C O   1 
HETATM 7777 O O   . HOH G 2 .   ? 1.234   17.623  -6.259  1.00 49.71 ? 427 HOH C O   1 
HETATM 7778 O O   . HOH G 2 .   ? 26.131  8.782   13.092  1.00 37.12 ? 428 HOH C O   1 
HETATM 7779 O O   . HOH G 2 .   ? 17.046  21.295  -1.509  1.00 36.06 ? 429 HOH C O   1 
HETATM 7780 O O   . HOH G 2 .   ? 35.512  35.591  1.280   1.00 38.43 ? 430 HOH C O   1 
HETATM 7781 O O   . HOH G 2 .   ? 16.299  23.462  -5.523  1.00 44.64 ? 431 HOH C O   1 
HETATM 7782 O O   . HOH G 2 .   ? 5.597   34.058  1.243   1.00 44.79 ? 432 HOH C O   1 
HETATM 7783 O O   . HOH G 2 .   ? 28.187  15.525  0.516   1.00 43.82 ? 433 HOH C O   1 
HETATM 7784 O O   . HOH G 2 .   ? 1.556   11.470  6.000   1.00 41.89 ? 434 HOH C O   1 
HETATM 7785 O O   . HOH G 2 .   ? -5.235  35.516  14.245  1.00 43.41 ? 435 HOH C O   1 
HETATM 7786 O O   . HOH G 2 .   ? 2.704   23.576  22.986  1.00 44.10 ? 436 HOH C O   1 
HETATM 7787 O O   . HOH G 2 .   ? -0.470  17.008  -3.248  1.00 55.67 ? 437 HOH C O   1 
HETATM 7788 O O   . HOH G 2 .   ? 5.632   28.171  22.425  1.00 50.87 ? 438 HOH C O   1 
HETATM 7789 O O   . HOH G 2 .   ? -3.758  11.527  4.643   1.00 53.21 ? 439 HOH C O   1 
HETATM 7790 O O   . HOH G 2 .   ? 27.055  42.789  11.854  1.00 41.08 ? 440 HOH C O   1 
HETATM 7791 O O   . HOH H 2 .   ? 13.236  48.671  -35.063 1.00 44.34 ? 301 HOH D O   1 
HETATM 7792 O O   . HOH H 2 .   ? 40.418  15.806  -36.145 1.00 38.29 ? 302 HOH D O   1 
HETATM 7793 O O   . HOH H 2 .   ? 14.303  26.427  -45.207 1.00 28.72 ? 303 HOH D O   1 
HETATM 7794 O O   . HOH H 2 .   ? 16.000  13.252  -46.866 1.00 36.43 ? 304 HOH D O   1 
HETATM 7795 O O   . HOH H 2 .   ? 11.729  39.955  -25.388 1.00 33.81 ? 305 HOH D O   1 
HETATM 7796 O O   . HOH H 2 .   ? -3.408  17.098  -43.946 1.00 55.24 ? 306 HOH D O   1 
HETATM 7797 O O   . HOH H 2 .   ? -3.081  21.721  -27.175 1.00 35.93 ? 307 HOH D O   1 
HETATM 7798 O O   . HOH H 2 .   ? 20.889  23.916  -42.881 1.00 16.27 ? 308 HOH D O   1 
HETATM 7799 O O   . HOH H 2 .   ? 1.433   19.562  -36.855 1.00 31.25 ? 309 HOH D O   1 
HETATM 7800 O O   . HOH H 2 .   ? 5.856   20.165  -33.322 1.00 30.59 ? 310 HOH D O   1 
HETATM 7801 O O   . HOH H 2 .   ? 30.599  17.220  -37.511 1.00 32.30 ? 311 HOH D O   1 
HETATM 7802 O O   . HOH H 2 .   ? 29.871  21.184  -29.765 1.00 32.68 ? 312 HOH D O   1 
HETATM 7803 O O   . HOH H 2 .   ? 34.056  36.292  -31.194 1.00 32.26 ? 313 HOH D O   1 
HETATM 7804 O O   . HOH H 2 .   ? -9.357  24.082  -38.827 1.00 35.50 ? 314 HOH D O   1 
HETATM 7805 O O   . HOH H 2 .   ? 40.253  19.881  -31.306 1.00 40.29 ? 315 HOH D O   1 
HETATM 7806 O O   . HOH H 2 .   ? 32.805  25.748  -38.543 1.00 40.17 ? 316 HOH D O   1 
HETATM 7807 O O   . HOH H 2 .   ? 37.876  32.883  -25.081 1.00 40.49 ? 317 HOH D O   1 
HETATM 7808 O O   . HOH H 2 .   ? 4.627   24.038  -49.449 1.00 41.15 ? 318 HOH D O   1 
HETATM 7809 O O   . HOH H 2 .   ? 8.264   37.234  -38.472 1.00 26.69 ? 319 HOH D O   1 
HETATM 7810 O O   . HOH H 2 .   ? -2.530  37.363  -29.778 1.00 31.97 ? 320 HOH D O   1 
HETATM 7811 O O   . HOH H 2 .   ? 3.197   16.602  -35.490 1.00 38.11 ? 321 HOH D O   1 
HETATM 7812 O O   . HOH H 2 .   ? 2.828   37.546  -18.505 1.00 27.23 ? 322 HOH D O   1 
HETATM 7813 O O   . HOH H 2 .   ? 8.325   29.931  -28.095 1.00 29.98 ? 323 HOH D O   1 
HETATM 7814 O O   . HOH H 2 .   ? -1.072  41.901  -37.341 1.00 29.61 ? 324 HOH D O   1 
HETATM 7815 O O   . HOH H 2 .   ? 11.507  22.732  -30.137 1.00 11.10 ? 325 HOH D O   1 
HETATM 7816 O O   . HOH H 2 .   ? -2.512  35.329  -37.469 1.00 28.50 ? 326 HOH D O   1 
HETATM 7817 O O   . HOH H 2 .   ? 2.795   41.864  -31.534 1.00 33.08 ? 327 HOH D O   1 
HETATM 7818 O O   . HOH H 2 .   ? 17.848  26.556  -42.994 1.00 23.21 ? 328 HOH D O   1 
HETATM 7819 O O   . HOH H 2 .   ? 17.420  27.067  -39.056 1.00 25.61 ? 329 HOH D O   1 
HETATM 7820 O O   . HOH H 2 .   ? 30.297  30.577  -41.345 1.00 30.10 ? 330 HOH D O   1 
HETATM 7821 O O   . HOH H 2 .   ? 30.656  32.918  -17.011 1.00 40.70 ? 331 HOH D O   1 
HETATM 7822 O O   . HOH H 2 .   ? 28.142  42.181  -21.701 1.00 41.33 ? 332 HOH D O   1 
HETATM 7823 O O   . HOH H 2 .   ? 8.800   41.117  -25.137 1.00 33.18 ? 333 HOH D O   1 
HETATM 7824 O O   . HOH H 2 .   ? 33.920  20.485  -28.211 1.00 35.55 ? 334 HOH D O   1 
HETATM 7825 O O   . HOH H 2 .   ? 32.427  31.249  -51.413 1.00 43.28 ? 335 HOH D O   1 
HETATM 7826 O O   . HOH H 2 .   ? 5.321   18.257  -38.133 1.00 34.63 ? 336 HOH D O   1 
HETATM 7827 O O   . HOH H 2 .   ? 12.336  33.009  -44.840 1.00 31.06 ? 337 HOH D O   1 
HETATM 7828 O O   . HOH H 2 .   ? 24.896  46.226  -32.959 1.00 43.43 ? 338 HOH D O   1 
HETATM 7829 O O   . HOH H 2 .   ? 38.498  12.681  -34.949 1.00 37.24 ? 339 HOH D O   1 
HETATM 7830 O O   . HOH H 2 .   ? 6.070   39.399  -22.339 1.00 35.27 ? 340 HOH D O   1 
HETATM 7831 O O   . HOH H 2 .   ? 23.642  44.231  -35.526 1.00 32.96 ? 341 HOH D O   1 
HETATM 7832 O O   . HOH H 2 .   ? 43.193  28.312  -31.266 1.00 39.69 ? 342 HOH D O   1 
HETATM 7833 O O   . HOH H 2 .   ? -6.017  31.833  -45.239 1.00 38.82 ? 343 HOH D O   1 
HETATM 7834 O O   . HOH H 2 .   ? 8.499   29.965  -37.800 1.00 25.15 ? 344 HOH D O   1 
HETATM 7835 O O   . HOH H 2 .   ? 12.519  35.845  -46.136 1.00 40.44 ? 345 HOH D O   1 
HETATM 7836 O O   . HOH H 2 .   ? 17.134  47.907  -34.543 1.00 46.32 ? 346 HOH D O   1 
HETATM 7837 O O   . HOH H 2 .   ? 37.032  19.997  -28.895 1.00 39.13 ? 347 HOH D O   1 
HETATM 7838 O O   . HOH H 2 .   ? 6.319   36.102  -40.385 1.00 26.97 ? 348 HOH D O   1 
HETATM 7839 O O   . HOH H 2 .   ? -5.940  30.025  -40.766 1.00 29.52 ? 349 HOH D O   1 
HETATM 7840 O O   . HOH H 2 .   ? 35.000  36.045  -43.595 1.00 34.42 ? 350 HOH D O   1 
HETATM 7841 O O   . HOH H 2 .   ? 33.554  35.694  -45.877 1.00 37.73 ? 351 HOH D O   1 
HETATM 7842 O O   . HOH H 2 .   ? 38.051  41.033  -28.387 1.00 39.77 ? 352 HOH D O   1 
HETATM 7843 O O   . HOH H 2 .   ? 3.504   28.415  -43.226 1.00 29.91 ? 353 HOH D O   1 
HETATM 7844 O O   . HOH H 2 .   ? 24.402  14.220  -34.815 1.00 32.35 ? 354 HOH D O   1 
HETATM 7845 O O   . HOH H 2 .   ? 38.689  28.445  -38.914 1.00 36.08 ? 355 HOH D O   1 
HETATM 7846 O O   . HOH H 2 .   ? 15.727  29.486  -48.768 1.00 53.87 ? 356 HOH D O   1 
HETATM 7847 O O   . HOH H 2 .   ? 19.187  27.033  -46.762 1.00 27.29 ? 357 HOH D O   1 
HETATM 7848 O O   . HOH H 2 .   ? 9.373   30.068  -35.338 1.00 25.65 ? 358 HOH D O   1 
HETATM 7849 O O   . HOH H 2 .   ? 39.554  30.505  -36.622 1.00 42.44 ? 359 HOH D O   1 
HETATM 7850 O O   . HOH H 2 .   ? 20.986  16.732  -31.258 1.00 32.71 ? 360 HOH D O   1 
HETATM 7851 O O   . HOH H 2 .   ? 26.583  17.102  -24.469 1.00 40.18 ? 361 HOH D O   1 
HETATM 7852 O O   . HOH H 2 .   ? 1.859   26.685  -22.271 1.00 28.41 ? 362 HOH D O   1 
HETATM 7853 O O   . HOH H 2 .   ? 8.426   29.214  -49.079 1.00 40.09 ? 363 HOH D O   1 
HETATM 7854 O O   . HOH H 2 .   ? 9.960   34.482  -41.960 1.00 30.12 ? 364 HOH D O   1 
HETATM 7855 O O   . HOH H 2 .   ? 30.417  32.450  -14.798 1.00 51.43 ? 365 HOH D O   1 
HETATM 7856 O O   . HOH H 2 .   ? 24.170  27.437  -47.302 1.00 35.59 ? 366 HOH D O   1 
HETATM 7857 O O   . HOH H 2 .   ? 9.041   32.617  -38.624 1.00 28.91 ? 367 HOH D O   1 
HETATM 7858 O O   . HOH H 2 .   ? 27.357  19.540  -44.307 1.00 37.02 ? 368 HOH D O   1 
HETATM 7859 O O   . HOH H 2 .   ? 20.817  14.752  -24.166 1.00 52.15 ? 369 HOH D O   1 
HETATM 7860 O O   . HOH H 2 .   ? 35.236  43.601  -28.097 1.00 50.20 ? 370 HOH D O   1 
HETATM 7861 O O   . HOH H 2 .   ? 4.814   48.669  -34.360 1.00 56.11 ? 371 HOH D O   1 
HETATM 7862 O O   . HOH H 2 .   ? 12.464  20.052  -32.936 1.00 26.63 ? 372 HOH D O   1 
HETATM 7863 O O   . HOH H 2 .   ? 30.722  44.935  -37.453 1.00 36.49 ? 373 HOH D O   1 
HETATM 7864 O O   . HOH H 2 .   ? 31.659  26.964  -40.590 1.00 32.50 ? 374 HOH D O   1 
HETATM 7865 O O   . HOH H 2 .   ? 12.762  40.857  -42.898 1.00 34.69 ? 375 HOH D O   1 
HETATM 7866 O O   . HOH H 2 .   ? 7.602   33.703  -40.566 1.00 26.57 ? 376 HOH D O   1 
HETATM 7867 O O   . HOH H 2 .   ? -0.411  37.611  -28.918 1.00 33.56 ? 377 HOH D O   1 
HETATM 7868 O O   . HOH H 2 .   ? 16.579  39.474  -18.060 1.00 41.91 ? 378 HOH D O   1 
HETATM 7869 O O   . HOH H 2 .   ? 1.627   21.080  -33.852 1.00 29.09 ? 379 HOH D O   1 
HETATM 7870 O O   . HOH H 2 .   ? 10.769  21.870  -27.426 1.00 38.56 ? 380 HOH D O   1 
HETATM 7871 O O   . HOH H 2 .   ? 2.362   37.183  -47.576 1.00 47.67 ? 381 HOH D O   1 
HETATM 7872 O O   . HOH H 2 .   ? 0.710   20.003  -40.360 1.00 34.10 ? 382 HOH D O   1 
HETATM 7873 O O   . HOH H 2 .   ? 36.334  31.769  -37.038 1.00 41.22 ? 383 HOH D O   1 
HETATM 7874 O O   . HOH H 2 .   ? 2.266   45.548  -26.039 1.00 54.84 ? 384 HOH D O   1 
HETATM 7875 O O   . HOH H 2 .   ? 13.363  22.284  -26.715 1.00 36.70 ? 385 HOH D O   1 
HETATM 7876 O O   . HOH H 2 .   ? 7.378   28.093  -23.658 1.00 48.99 ? 386 HOH D O   1 
HETATM 7877 O O   . HOH H 2 .   ? -9.177  28.773  -27.576 1.00 36.47 ? 387 HOH D O   1 
HETATM 7878 O O   . HOH H 2 .   ? 1.805   22.261  -47.901 1.00 39.98 ? 388 HOH D O   1 
HETATM 7879 O O   . HOH H 2 .   ? -14.809 33.001  -33.279 1.00 45.83 ? 389 HOH D O   1 
HETATM 7880 O O   . HOH H 2 .   ? 37.640  37.138  -33.961 1.00 45.42 ? 390 HOH D O   1 
HETATM 7881 O O   . HOH H 2 .   ? 13.218  41.317  -19.376 1.00 49.16 ? 391 HOH D O   1 
HETATM 7882 O O   . HOH H 2 .   ? 31.049  21.848  -47.750 1.00 46.51 ? 392 HOH D O   1 
HETATM 7883 O O   . HOH H 2 .   ? 10.001  34.526  -22.090 1.00 41.70 ? 393 HOH D O   1 
HETATM 7884 O O   . HOH H 2 .   ? 33.264  23.293  -39.672 1.00 45.32 ? 394 HOH D O   1 
HETATM 7885 O O   . HOH H 2 .   ? 6.657   28.952  -26.002 1.00 31.60 ? 395 HOH D O   1 
HETATM 7886 O O   . HOH H 2 .   ? 13.497  48.647  -37.138 1.00 51.67 ? 396 HOH D O   1 
HETATM 7887 O O   . HOH H 2 .   ? 1.624   20.227  -42.926 1.00 53.38 ? 397 HOH D O   1 
HETATM 7888 O O   . HOH H 2 .   ? 32.373  45.059  -35.431 1.00 49.07 ? 398 HOH D O   1 
HETATM 7889 O O   . HOH H 2 .   ? 34.379  31.226  -39.847 1.00 45.42 ? 399 HOH D O   1 
HETATM 7890 O O   . HOH H 2 .   ? 30.896  46.023  -33.195 1.00 41.51 ? 400 HOH D O   1 
HETATM 7891 O O   . HOH H 2 .   ? 12.696  29.840  -47.735 1.00 43.68 ? 401 HOH D O   1 
HETATM 7892 O O   . HOH H 2 .   ? 18.308  23.386  -47.015 1.00 46.99 ? 402 HOH D O   1 
HETATM 7893 O O   . HOH H 2 .   ? -11.769 26.982  -28.069 1.00 54.00 ? 403 HOH D O   1 
HETATM 7894 O O   . HOH H 2 .   ? 14.216  27.919  -47.429 1.00 45.29 ? 404 HOH D O   1 
HETATM 7895 O O   . HOH H 2 .   ? 22.930  16.660  -29.605 1.00 37.69 ? 405 HOH D O   1 
HETATM 7896 O O   . HOH H 2 .   ? 19.693  17.060  -32.959 1.00 33.48 ? 406 HOH D O   1 
HETATM 7897 O O   . HOH H 2 .   ? 17.195  19.007  -26.519 1.00 51.39 ? 407 HOH D O   1 
HETATM 7898 O O   . HOH H 2 .   ? 43.533  20.029  -30.943 1.00 48.48 ? 408 HOH D O   1 
HETATM 7899 O O   . HOH H 2 .   ? 18.609  24.603  -44.549 1.00 37.24 ? 409 HOH D O   1 
HETATM 7900 O O   . HOH H 2 .   ? 10.137  36.602  -42.754 1.00 52.13 ? 410 HOH D O   1 
HETATM 7901 O O   . HOH H 2 .   ? 9.034   40.476  -43.774 1.00 41.23 ? 411 HOH D O   1 
HETATM 7902 O O   . HOH H 2 .   ? 15.192  31.641  -19.892 1.00 49.85 ? 412 HOH D O   1 
HETATM 7903 O O   . HOH H 2 .   ? 16.976  30.445  -19.229 1.00 52.46 ? 413 HOH D O   1 
HETATM 7904 O O   . HOH H 2 .   ? 2.208   44.844  -27.911 1.00 43.35 ? 414 HOH D O   1 
HETATM 7905 O O   . HOH H 2 .   ? -8.923  32.721  -44.369 1.00 48.65 ? 415 HOH D O   1 
HETATM 7906 O O   . HOH H 2 .   ? 2.372   46.938  -24.510 1.00 50.82 ? 416 HOH D O   1 
HETATM 7907 O O   . HOH H 2 .   ? 3.781   44.052  -29.689 1.00 43.61 ? 417 HOH D O   1 
HETATM 7908 O O   . HOH H 2 .   ? 16.225  23.285  -48.346 1.00 48.13 ? 418 HOH D O   1 
HETATM 7909 O O   . HOH H 2 .   ? 33.018  18.899  -48.449 1.00 44.78 ? 419 HOH D O   1 
HETATM 7910 O O   . HOH H 2 .   ? 2.759   15.523  -37.475 1.00 43.51 ? 420 HOH D O   1 
HETATM 7911 O O   . HOH H 2 .   ? 32.090  29.915  -39.647 1.00 44.37 ? 421 HOH D O   1 
HETATM 7912 O O   . HOH H 2 .   ? 36.639  39.251  -42.944 1.00 38.76 ? 422 HOH D O   1 
HETATM 7913 O O   . HOH H 2 .   ? 5.970   20.965  -23.497 1.00 49.60 ? 423 HOH D O   1 
HETATM 7914 O O   . HOH H 2 .   ? 20.081  15.977  -28.688 1.00 36.69 ? 424 HOH D O   1 
HETATM 7915 O O   . HOH H 2 .   ? 6.421   38.338  -42.305 1.00 41.38 ? 425 HOH D O   1 
HETATM 7916 O O   . HOH H 2 .   ? 17.605  27.129  -49.429 1.00 46.32 ? 426 HOH D O   1 
HETATM 7917 O O   . HOH H 2 .   ? 24.805  28.854  -48.874 1.00 48.73 ? 427 HOH D O   1 
HETATM 7918 O O   . HOH H 2 .   ? 5.409   17.245  -40.082 1.00 50.49 ? 428 HOH D O   1 
HETATM 7919 O O   . HOH H 2 .   ? 23.416  46.784  -35.030 1.00 49.93 ? 429 HOH D O   1 
HETATM 7920 O O   . HOH H 2 .   ? 0.396   20.703  -46.976 1.00 55.86 ? 430 HOH D O   1 
HETATM 7921 O O   . HOH H 2 .   ? -4.727  38.908  -28.715 1.00 42.84 ? 431 HOH D O   1 
HETATM 7922 O O   . HOH H 2 .   ? 0.655   17.122  -39.415 1.00 41.00 ? 432 HOH D O   1 
# 
