data_8Z4H
# 
_entry.id   8Z4H 
# 
_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   8Z4H         pdb_00008z4h 10.2210/pdb8z4h/pdb 
WWPDB D_1300047033 ?            ?                   
# 
_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                        8Z4H 
_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' 
_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' 26271.289 4   ? ? ? ? 
2 water   nat water                   18.015    453 ? ? ? ? 
# 
_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
MDYQNTNYTCCPTSLSLASQMLYHYKSESECAKALGTSKGSGTSPAQLIANAPKLGFKIIPIKRDSKEVKKYLKKGFPVI
CHWQVNQSRNCKGDYTGNFGHYGLIWDMTSTHYVVADPAKGVNRKYKFSCLDNANKGYRQNYYVVCPA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVRFSRDMLQDGAKRMFKWLRKGEGLPNYLIMYDMDRNKEYKLVPKEYAGLYESRNIFWIKNGREPNYVTLTSVARNPLV
MDYQNTNYTCCPTSLSLASQMLYHYKSESECAKALGTSKGSGTSPAQLIANAPKLGFKIIPIKRDSKEVKKYLKKGFPVI
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  CYS 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  CYS 90  90  90  CYS CYS 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  CYS 90  90  90  CYS CYS 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  CYS 90  90  90  CYS CYS 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  CYS 90  90  90  CYS CYS 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   301 140 HOH HOH A . 
E 2 HOH 2   302 441 HOH HOH A . 
E 2 HOH 3   303 370 HOH HOH A . 
E 2 HOH 4   304 100 HOH HOH A . 
E 2 HOH 5   305 270 HOH HOH A . 
E 2 HOH 6   306 24  HOH HOH A . 
E 2 HOH 7   307 223 HOH HOH A . 
E 2 HOH 8   308 444 HOH HOH A . 
E 2 HOH 9   309 278 HOH HOH A . 
E 2 HOH 10  310 102 HOH HOH A . 
E 2 HOH 11  311 22  HOH HOH A . 
E 2 HOH 12  312 435 HOH HOH A . 
E 2 HOH 13  313 285 HOH HOH A . 
E 2 HOH 14  314 51  HOH HOH A . 
E 2 HOH 15  315 428 HOH HOH A . 
E 2 HOH 16  316 139 HOH HOH A . 
E 2 HOH 17  317 64  HOH HOH A . 
E 2 HOH 18  318 184 HOH HOH A . 
E 2 HOH 19  319 228 HOH HOH A . 
E 2 HOH 20  320 426 HOH HOH A . 
E 2 HOH 21  321 6   HOH HOH A . 
E 2 HOH 22  322 79  HOH HOH A . 
E 2 HOH 23  323 60  HOH HOH A . 
E 2 HOH 24  324 39  HOH HOH A . 
E 2 HOH 25  325 443 HOH HOH A . 
E 2 HOH 26  326 111 HOH HOH A . 
E 2 HOH 27  327 179 HOH HOH A . 
E 2 HOH 28  328 317 HOH HOH A . 
E 2 HOH 29  329 42  HOH HOH A . 
E 2 HOH 30  330 116 HOH HOH A . 
E 2 HOH 31  331 419 HOH HOH A . 
E 2 HOH 32  332 41  HOH HOH A . 
E 2 HOH 33  333 136 HOH HOH A . 
E 2 HOH 34  334 195 HOH HOH A . 
E 2 HOH 35  335 337 HOH HOH A . 
E 2 HOH 36  336 28  HOH HOH A . 
E 2 HOH 37  337 19  HOH HOH A . 
E 2 HOH 38  338 98  HOH HOH A . 
E 2 HOH 39  339 335 HOH HOH A . 
E 2 HOH 40  340 33  HOH HOH A . 
E 2 HOH 41  341 221 HOH HOH A . 
E 2 HOH 42  342 358 HOH HOH A . 
E 2 HOH 43  343 3   HOH HOH A . 
E 2 HOH 44  344 30  HOH HOH A . 
E 2 HOH 45  345 254 HOH HOH A . 
E 2 HOH 46  346 408 HOH HOH A . 
E 2 HOH 47  347 249 HOH HOH A . 
E 2 HOH 48  348 415 HOH HOH A . 
E 2 HOH 49  349 170 HOH HOH A . 
E 2 HOH 50  350 175 HOH HOH A . 
E 2 HOH 51  351 174 HOH HOH A . 
E 2 HOH 52  352 267 HOH HOH A . 
E 2 HOH 53  353 230 HOH HOH A . 
E 2 HOH 54  354 123 HOH HOH A . 
E 2 HOH 55  355 232 HOH HOH A . 
E 2 HOH 56  356 112 HOH HOH A . 
E 2 HOH 57  357 8   HOH HOH A . 
E 2 HOH 58  358 287 HOH HOH A . 
E 2 HOH 59  359 295 HOH HOH A . 
E 2 HOH 60  360 118 HOH HOH A . 
E 2 HOH 61  361 265 HOH HOH A . 
E 2 HOH 62  362 209 HOH HOH A . 
E 2 HOH 63  363 161 HOH HOH A . 
E 2 HOH 64  364 222 HOH HOH A . 
E 2 HOH 65  365 110 HOH HOH A . 
E 2 HOH 66  366 15  HOH HOH A . 
E 2 HOH 67  367 340 HOH HOH A . 
E 2 HOH 68  368 445 HOH HOH A . 
E 2 HOH 69  369 372 HOH HOH A . 
E 2 HOH 70  370 12  HOH HOH A . 
E 2 HOH 71  371 217 HOH HOH A . 
E 2 HOH 72  372 299 HOH HOH A . 
E 2 HOH 73  373 423 HOH HOH A . 
E 2 HOH 74  374 309 HOH HOH A . 
E 2 HOH 75  375 261 HOH HOH A . 
E 2 HOH 76  376 388 HOH HOH A . 
E 2 HOH 77  377 264 HOH HOH A . 
E 2 HOH 78  378 380 HOH HOH A . 
E 2 HOH 79  379 90  HOH HOH A . 
E 2 HOH 80  380 266 HOH HOH A . 
E 2 HOH 81  381 364 HOH HOH A . 
E 2 HOH 82  382 132 HOH HOH A . 
E 2 HOH 83  383 117 HOH HOH A . 
E 2 HOH 84  384 247 HOH HOH A . 
E 2 HOH 85  385 425 HOH HOH A . 
E 2 HOH 86  386 381 HOH HOH A . 
E 2 HOH 87  387 422 HOH HOH A . 
E 2 HOH 88  388 346 HOH HOH A . 
E 2 HOH 89  389 197 HOH HOH A . 
E 2 HOH 90  390 251 HOH HOH A . 
E 2 HOH 91  391 158 HOH HOH A . 
E 2 HOH 92  392 418 HOH HOH A . 
E 2 HOH 93  393 206 HOH HOH A . 
E 2 HOH 94  394 329 HOH HOH A . 
E 2 HOH 95  395 424 HOH HOH A . 
E 2 HOH 96  396 403 HOH HOH A . 
E 2 HOH 97  397 204 HOH HOH A . 
E 2 HOH 98  398 84  HOH HOH A . 
E 2 HOH 99  399 336 HOH HOH A . 
E 2 HOH 100 400 173 HOH HOH A . 
E 2 HOH 101 401 168 HOH HOH A . 
E 2 HOH 102 402 322 HOH HOH A . 
E 2 HOH 103 403 417 HOH HOH A . 
E 2 HOH 104 404 394 HOH HOH A . 
E 2 HOH 105 405 421 HOH HOH A . 
E 2 HOH 106 406 298 HOH HOH A . 
E 2 HOH 107 407 398 HOH HOH A . 
F 2 HOH 1   301 188 HOH HOH B . 
F 2 HOH 2   302 303 HOH HOH B . 
F 2 HOH 3   303 86  HOH HOH B . 
F 2 HOH 4   304 76  HOH HOH B . 
F 2 HOH 5   305 129 HOH HOH B . 
F 2 HOH 6   306 155 HOH HOH B . 
F 2 HOH 7   307 244 HOH HOH B . 
F 2 HOH 8   308 351 HOH HOH B . 
F 2 HOH 9   309 9   HOH HOH B . 
F 2 HOH 10  310 27  HOH HOH B . 
F 2 HOH 11  311 85  HOH HOH B . 
F 2 HOH 12  312 29  HOH HOH B . 
F 2 HOH 13  313 263 HOH HOH B . 
F 2 HOH 14  314 411 HOH HOH B . 
F 2 HOH 15  315 56  HOH HOH B . 
F 2 HOH 16  316 156 HOH HOH B . 
F 2 HOH 17  317 306 HOH HOH B . 
F 2 HOH 18  318 35  HOH HOH B . 
F 2 HOH 19  319 1   HOH HOH B . 
F 2 HOH 20  320 96  HOH HOH B . 
F 2 HOH 21  321 282 HOH HOH B . 
F 2 HOH 22  322 276 HOH HOH B . 
F 2 HOH 23  323 186 HOH HOH B . 
F 2 HOH 24  324 316 HOH HOH B . 
F 2 HOH 25  325 242 HOH HOH B . 
F 2 HOH 26  326 14  HOH HOH B . 
F 2 HOH 27  327 103 HOH HOH B . 
F 2 HOH 28  328 389 HOH HOH B . 
F 2 HOH 29  329 73  HOH HOH B . 
F 2 HOH 30  330 382 HOH HOH B . 
F 2 HOH 31  331 176 HOH HOH B . 
F 2 HOH 32  332 75  HOH HOH B . 
F 2 HOH 33  333 215 HOH HOH B . 
F 2 HOH 34  334 162 HOH HOH B . 
F 2 HOH 35  335 49  HOH HOH B . 
F 2 HOH 36  336 44  HOH HOH B . 
F 2 HOH 37  337 192 HOH HOH B . 
F 2 HOH 38  338 62  HOH HOH B . 
F 2 HOH 39  339 67  HOH HOH B . 
F 2 HOH 40  340 119 HOH HOH B . 
F 2 HOH 41  341 83  HOH HOH B . 
F 2 HOH 42  342 2   HOH HOH B . 
F 2 HOH 43  343 237 HOH HOH B . 
F 2 HOH 44  344 81  HOH HOH B . 
F 2 HOH 45  345 137 HOH HOH B . 
F 2 HOH 46  346 171 HOH HOH B . 
F 2 HOH 47  347 121 HOH HOH B . 
F 2 HOH 48  348 377 HOH HOH B . 
F 2 HOH 49  349 330 HOH HOH B . 
F 2 HOH 50  350 7   HOH HOH B . 
F 2 HOH 51  351 373 HOH HOH B . 
F 2 HOH 52  352 437 HOH HOH B . 
F 2 HOH 53  353 375 HOH HOH B . 
F 2 HOH 54  354 240 HOH HOH B . 
F 2 HOH 55  355 16  HOH HOH B . 
F 2 HOH 56  356 177 HOH HOH B . 
F 2 HOH 57  357 182 HOH HOH B . 
F 2 HOH 58  358 229 HOH HOH B . 
F 2 HOH 59  359 234 HOH HOH B . 
F 2 HOH 60  360 344 HOH HOH B . 
F 2 HOH 61  361 301 HOH HOH B . 
F 2 HOH 62  362 10  HOH HOH B . 
F 2 HOH 63  363 383 HOH HOH B . 
F 2 HOH 64  364 371 HOH HOH B . 
F 2 HOH 65  365 61  HOH HOH B . 
F 2 HOH 66  366 374 HOH HOH B . 
F 2 HOH 67  367 449 HOH HOH B . 
F 2 HOH 68  368 356 HOH HOH B . 
F 2 HOH 69  369 40  HOH HOH B . 
F 2 HOH 70  370 397 HOH HOH B . 
F 2 HOH 71  371 53  HOH HOH B . 
F 2 HOH 72  372 172 HOH HOH B . 
F 2 HOH 73  373 157 HOH HOH B . 
F 2 HOH 74  374 319 HOH HOH B . 
F 2 HOH 75  375 328 HOH HOH B . 
F 2 HOH 76  376 104 HOH HOH B . 
F 2 HOH 77  377 150 HOH HOH B . 
F 2 HOH 78  378 277 HOH HOH B . 
F 2 HOH 79  379 345 HOH HOH B . 
F 2 HOH 80  380 225 HOH HOH B . 
F 2 HOH 81  381 386 HOH HOH B . 
F 2 HOH 82  382 99  HOH HOH B . 
F 2 HOH 83  383 145 HOH HOH B . 
F 2 HOH 84  384 255 HOH HOH B . 
F 2 HOH 85  385 368 HOH HOH B . 
F 2 HOH 86  386 80  HOH HOH B . 
F 2 HOH 87  387 95  HOH HOH B . 
F 2 HOH 88  388 227 HOH HOH B . 
F 2 HOH 89  389 348 HOH HOH B . 
F 2 HOH 90  390 355 HOH HOH B . 
F 2 HOH 91  391 13  HOH HOH B . 
F 2 HOH 92  392 107 HOH HOH B . 
F 2 HOH 93  393 360 HOH HOH B . 
F 2 HOH 94  394 365 HOH HOH B . 
F 2 HOH 95  395 143 HOH HOH B . 
F 2 HOH 96  396 305 HOH HOH B . 
F 2 HOH 97  397 431 HOH HOH B . 
F 2 HOH 98  398 101 HOH HOH B . 
F 2 HOH 99  399 166 HOH HOH B . 
F 2 HOH 100 400 165 HOH HOH B . 
F 2 HOH 101 401 440 HOH HOH B . 
F 2 HOH 102 402 362 HOH HOH B . 
F 2 HOH 103 403 392 HOH HOH B . 
F 2 HOH 104 404 436 HOH HOH B . 
F 2 HOH 105 405 97  HOH HOH B . 
F 2 HOH 106 406 359 HOH HOH B . 
F 2 HOH 107 407 342 HOH HOH B . 
F 2 HOH 108 408 113 HOH HOH B . 
F 2 HOH 109 409 323 HOH HOH B . 
F 2 HOH 110 410 256 HOH HOH B . 
F 2 HOH 111 411 361 HOH HOH B . 
F 2 HOH 112 412 246 HOH HOH B . 
F 2 HOH 113 413 259 HOH HOH B . 
F 2 HOH 114 414 180 HOH HOH B . 
F 2 HOH 115 415 341 HOH HOH B . 
F 2 HOH 116 416 152 HOH HOH B . 
F 2 HOH 117 417 379 HOH HOH B . 
F 2 HOH 118 418 313 HOH HOH B . 
F 2 HOH 119 419 87  HOH HOH B . 
F 2 HOH 120 420 438 HOH HOH B . 
F 2 HOH 121 421 271 HOH HOH B . 
F 2 HOH 122 422 396 HOH HOH B . 
F 2 HOH 123 423 147 HOH HOH B . 
F 2 HOH 124 424 391 HOH HOH B . 
F 2 HOH 125 425 433 HOH HOH B . 
F 2 HOH 126 426 214 HOH HOH B . 
F 2 HOH 127 427 439 HOH HOH B . 
F 2 HOH 128 428 318 HOH HOH B . 
F 2 HOH 129 429 149 HOH HOH B . 
F 2 HOH 130 430 208 HOH HOH B . 
F 2 HOH 131 431 302 HOH HOH B . 
F 2 HOH 132 432 420 HOH HOH B . 
F 2 HOH 133 433 300 HOH HOH B . 
F 2 HOH 134 434 326 HOH HOH B . 
G 2 HOH 1   301 93  HOH HOH C . 
G 2 HOH 2   302 63  HOH HOH C . 
G 2 HOH 3   303 144 HOH HOH C . 
G 2 HOH 4   304 109 HOH HOH C . 
G 2 HOH 5   305 395 HOH HOH C . 
G 2 HOH 6   306 410 HOH HOH C . 
G 2 HOH 7   307 54  HOH HOH C . 
G 2 HOH 8   308 125 HOH HOH C . 
G 2 HOH 9   309 286 HOH HOH C . 
G 2 HOH 10  310 447 HOH HOH C . 
G 2 HOH 11  311 416 HOH HOH C . 
G 2 HOH 12  312 334 HOH HOH C . 
G 2 HOH 13  313 146 HOH HOH C . 
G 2 HOH 14  314 47  HOH HOH C . 
G 2 HOH 15  315 352 HOH HOH C . 
G 2 HOH 16  316 390 HOH HOH C . 
G 2 HOH 17  317 38  HOH HOH C . 
G 2 HOH 18  318 25  HOH HOH C . 
G 2 HOH 19  319 58  HOH HOH C . 
G 2 HOH 20  320 178 HOH HOH C . 
G 2 HOH 21  321 231 HOH HOH C . 
G 2 HOH 22  322 46  HOH HOH C . 
G 2 HOH 23  323 34  HOH HOH C . 
G 2 HOH 24  324 37  HOH HOH C . 
G 2 HOH 25  325 26  HOH HOH C . 
G 2 HOH 26  326 414 HOH HOH C . 
G 2 HOH 27  327 183 HOH HOH C . 
G 2 HOH 28  328 212 HOH HOH C . 
G 2 HOH 29  329 94  HOH HOH C . 
G 2 HOH 30  330 154 HOH HOH C . 
G 2 HOH 31  331 288 HOH HOH C . 
G 2 HOH 32  332 304 HOH HOH C . 
G 2 HOH 33  333 59  HOH HOH C . 
G 2 HOH 34  334 23  HOH HOH C . 
G 2 HOH 35  335 20  HOH HOH C . 
G 2 HOH 36  336 127 HOH HOH C . 
G 2 HOH 37  337 32  HOH HOH C . 
G 2 HOH 38  338 451 HOH HOH C . 
G 2 HOH 39  339 290 HOH HOH C . 
G 2 HOH 40  340 70  HOH HOH C . 
G 2 HOH 41  341 65  HOH HOH C . 
G 2 HOH 42  342 404 HOH HOH C . 
G 2 HOH 43  343 357 HOH HOH C . 
G 2 HOH 44  344 163 HOH HOH C . 
G 2 HOH 45  345 333 HOH HOH C . 
G 2 HOH 46  346 78  HOH HOH C . 
G 2 HOH 47  347 279 HOH HOH C . 
G 2 HOH 48  348 128 HOH HOH C . 
G 2 HOH 49  349 193 HOH HOH C . 
G 2 HOH 50  350 189 HOH HOH C . 
G 2 HOH 51  351 273 HOH HOH C . 
G 2 HOH 52  352 92  HOH HOH C . 
G 2 HOH 53  353 122 HOH HOH C . 
G 2 HOH 54  354 393 HOH HOH C . 
G 2 HOH 55  355 339 HOH HOH C . 
G 2 HOH 56  356 258 HOH HOH C . 
G 2 HOH 57  357 69  HOH HOH C . 
G 2 HOH 58  358 384 HOH HOH C . 
G 2 HOH 59  359 452 HOH HOH C . 
G 2 HOH 60  360 248 HOH HOH C . 
G 2 HOH 61  361 268 HOH HOH C . 
G 2 HOH 62  362 307 HOH HOH C . 
G 2 HOH 63  363 138 HOH HOH C . 
G 2 HOH 64  364 224 HOH HOH C . 
G 2 HOH 65  365 250 HOH HOH C . 
G 2 HOH 66  366 367 HOH HOH C . 
G 2 HOH 67  367 151 HOH HOH C . 
G 2 HOH 68  368 203 HOH HOH C . 
G 2 HOH 69  369 281 HOH HOH C . 
G 2 HOH 70  370 89  HOH HOH C . 
G 2 HOH 71  371 338 HOH HOH C . 
G 2 HOH 72  372 262 HOH HOH C . 
G 2 HOH 73  373 202 HOH HOH C . 
G 2 HOH 74  374 253 HOH HOH C . 
G 2 HOH 75  375 205 HOH HOH C . 
G 2 HOH 76  376 187 HOH HOH C . 
G 2 HOH 77  377 141 HOH HOH C . 
G 2 HOH 78  378 296 HOH HOH C . 
G 2 HOH 79  379 283 HOH HOH C . 
G 2 HOH 80  380 274 HOH HOH C . 
G 2 HOH 81  381 311 HOH HOH C . 
G 2 HOH 82  382 120 HOH HOH C . 
G 2 HOH 83  383 369 HOH HOH C . 
G 2 HOH 84  384 211 HOH HOH C . 
G 2 HOH 85  385 343 HOH HOH C . 
G 2 HOH 86  386 325 HOH HOH C . 
G 2 HOH 87  387 327 HOH HOH C . 
G 2 HOH 88  388 57  HOH HOH C . 
G 2 HOH 89  389 429 HOH HOH C . 
G 2 HOH 90  390 387 HOH HOH C . 
G 2 HOH 91  391 453 HOH HOH C . 
G 2 HOH 92  392 43  HOH HOH C . 
G 2 HOH 93  393 432 HOH HOH C . 
G 2 HOH 94  394 350 HOH HOH C . 
G 2 HOH 95  395 260 HOH HOH C . 
G 2 HOH 96  396 434 HOH HOH C . 
G 2 HOH 97  397 376 HOH HOH C . 
H 2 HOH 1   301 349 HOH HOH D . 
H 2 HOH 2   302 220 HOH HOH D . 
H 2 HOH 3   303 194 HOH HOH D . 
H 2 HOH 4   304 191 HOH HOH D . 
H 2 HOH 5   305 308 HOH HOH D . 
H 2 HOH 6   306 292 HOH HOH D . 
H 2 HOH 7   307 200 HOH HOH D . 
H 2 HOH 8   308 66  HOH HOH D . 
H 2 HOH 9   309 48  HOH HOH D . 
H 2 HOH 10  310 226 HOH HOH D . 
H 2 HOH 11  311 402 HOH HOH D . 
H 2 HOH 12  312 52  HOH HOH D . 
H 2 HOH 13  313 5   HOH HOH D . 
H 2 HOH 14  314 133 HOH HOH D . 
H 2 HOH 15  315 257 HOH HOH D . 
H 2 HOH 16  316 17  HOH HOH D . 
H 2 HOH 17  317 450 HOH HOH D . 
H 2 HOH 18  318 115 HOH HOH D . 
H 2 HOH 19  319 442 HOH HOH D . 
H 2 HOH 20  320 169 HOH HOH D . 
H 2 HOH 21  321 18  HOH HOH D . 
H 2 HOH 22  322 45  HOH HOH D . 
H 2 HOH 23  323 4   HOH HOH D . 
H 2 HOH 24  324 427 HOH HOH D . 
H 2 HOH 25  325 239 HOH HOH D . 
H 2 HOH 26  326 196 HOH HOH D . 
H 2 HOH 27  327 153 HOH HOH D . 
H 2 HOH 28  328 243 HOH HOH D . 
H 2 HOH 29  329 207 HOH HOH D . 
H 2 HOH 30  330 77  HOH HOH D . 
H 2 HOH 31  331 315 HOH HOH D . 
H 2 HOH 32  332 236 HOH HOH D . 
H 2 HOH 33  333 126 HOH HOH D . 
H 2 HOH 34  334 233 HOH HOH D . 
H 2 HOH 35  335 289 HOH HOH D . 
H 2 HOH 36  336 272 HOH HOH D . 
H 2 HOH 37  337 68  HOH HOH D . 
H 2 HOH 38  338 216 HOH HOH D . 
H 2 HOH 39  339 21  HOH HOH D . 
H 2 HOH 40  340 321 HOH HOH D . 
H 2 HOH 41  341 399 HOH HOH D . 
H 2 HOH 42  342 108 HOH HOH D . 
H 2 HOH 43  343 409 HOH HOH D . 
H 2 HOH 44  344 284 HOH HOH D . 
H 2 HOH 45  345 72  HOH HOH D . 
H 2 HOH 46  346 238 HOH HOH D . 
H 2 HOH 47  347 91  HOH HOH D . 
H 2 HOH 48  348 235 HOH HOH D . 
H 2 HOH 49  349 405 HOH HOH D . 
H 2 HOH 50  350 366 HOH HOH D . 
H 2 HOH 51  351 269 HOH HOH D . 
H 2 HOH 52  352 142 HOH HOH D . 
H 2 HOH 53  353 55  HOH HOH D . 
H 2 HOH 54  354 135 HOH HOH D . 
H 2 HOH 55  355 201 HOH HOH D . 
H 2 HOH 56  356 198 HOH HOH D . 
H 2 HOH 57  357 36  HOH HOH D . 
H 2 HOH 58  358 407 HOH HOH D . 
H 2 HOH 59  359 11  HOH HOH D . 
H 2 HOH 60  360 71  HOH HOH D . 
H 2 HOH 61  361 252 HOH HOH D . 
H 2 HOH 62  362 74  HOH HOH D . 
H 2 HOH 63  363 219 HOH HOH D . 
H 2 HOH 64  364 190 HOH HOH D . 
H 2 HOH 65  365 50  HOH HOH D . 
H 2 HOH 66  366 160 HOH HOH D . 
H 2 HOH 67  367 406 HOH HOH D . 
H 2 HOH 68  368 294 HOH HOH D . 
H 2 HOH 69  369 280 HOH HOH D . 
H 2 HOH 70  370 347 HOH HOH D . 
H 2 HOH 71  371 124 HOH HOH D . 
H 2 HOH 72  372 134 HOH HOH D . 
H 2 HOH 73  373 185 HOH HOH D . 
H 2 HOH 74  374 218 HOH HOH D . 
H 2 HOH 75  375 297 HOH HOH D . 
H 2 HOH 76  376 114 HOH HOH D . 
H 2 HOH 77  377 275 HOH HOH D . 
H 2 HOH 78  378 293 HOH HOH D . 
H 2 HOH 79  379 354 HOH HOH D . 
H 2 HOH 80  380 159 HOH HOH D . 
H 2 HOH 81  381 363 HOH HOH D . 
H 2 HOH 82  382 332 HOH HOH D . 
H 2 HOH 83  383 131 HOH HOH D . 
H 2 HOH 84  384 106 HOH HOH D . 
H 2 HOH 85  385 353 HOH HOH D . 
H 2 HOH 86  386 88  HOH HOH D . 
H 2 HOH 87  387 413 HOH HOH D . 
H 2 HOH 88  388 164 HOH HOH D . 
H 2 HOH 89  389 167 HOH HOH D . 
H 2 HOH 90  390 320 HOH HOH D . 
H 2 HOH 91  391 378 HOH HOH D . 
H 2 HOH 92  392 199 HOH HOH D . 
H 2 HOH 93  393 241 HOH HOH D . 
H 2 HOH 94  394 412 HOH HOH D . 
H 2 HOH 95  395 130 HOH HOH D . 
H 2 HOH 96  396 401 HOH HOH D . 
H 2 HOH 97  397 430 HOH HOH D . 
H 2 HOH 98  398 105 HOH HOH D . 
H 2 HOH 99  399 310 HOH HOH D . 
H 2 HOH 100 400 400 HOH HOH D . 
H 2 HOH 101 401 312 HOH HOH D . 
H 2 HOH 102 402 314 HOH HOH D . 
H 2 HOH 103 403 148 HOH HOH D . 
H 2 HOH 104 404 385 HOH HOH D . 
H 2 HOH 105 405 82  HOH HOH D . 
H 2 HOH 106 406 181 HOH HOH D . 
H 2 HOH 107 407 31  HOH HOH D . 
H 2 HOH 108 408 210 HOH HOH D . 
H 2 HOH 109 409 291 HOH HOH D . 
H 2 HOH 110 410 331 HOH HOH D . 
H 2 HOH 111 411 446 HOH HOH D . 
H 2 HOH 112 412 324 HOH HOH D . 
H 2 HOH 113 413 213 HOH HOH D . 
H 2 HOH 114 414 448 HOH HOH D . 
H 2 HOH 115 415 245 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                   91.85 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z4H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.828 
_cell.length_a_esd                 ? 
_cell.length_b                     86.916 
_cell.length_b_esd                 ? 
_cell.length_c                     87.993 
_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                         8Z4H 
_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                   8Z4H 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.19 
_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    
;Precipitant:25% w/v Polyethylene glycol 3,350;
Buffer:0.1 M HEPES pH 7.5;
Salt :0.2 M Ammonium sulfate;
;
_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                          ? 
_reflns.entry_id                                       8Z4H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.79 
_reflns.d_resolution_low                               73.79 
_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                                     95039 
_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                           90.86 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.77 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.05 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0676 
_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                                    1.79 
_reflns_shell.d_res_low                                     1.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4647 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.7698 
_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                                 8Z4H 
_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                            1.79 
_refine.ls_d_res_low                             73.79 
_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                     94808 
_refine.ls_number_reflns_R_free                  4674 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.86 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2546 
_refine.ls_R_factor_R_free                       0.2852 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2531 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 39.08 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.33 
_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                       1.79 
_refine_hist.d_res_low                        73.79 
_refine_hist.number_atoms_solvent             453 
_refine_hist.number_atoms_total               7824 
_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        7371 
_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         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.031  ? 7557  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 3.858  ? 10194 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.114 ? 1030  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.254  ? 1044  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.033  ? 1299  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.79 1.81 . . 135 2398 74.00  . . . . 0.5244 . . . . . . . . . . . 0.5542 
'X-RAY DIFFRACTION' 1.81 1.83 . . 129 2625 79.00  . . . . 0.5077 . . . . . . . . . . . 0.5092 
'X-RAY DIFFRACTION' 1.83 1.86 . . 137 2885 87.00  . . . . 0.4742 . . . . . . . . . . . 0.4991 
'X-RAY DIFFRACTION' 1.86 1.88 . . 132 2855 87.00  . . . . 0.4641 . . . . . . . . . . . 0.4664 
'X-RAY DIFFRACTION' 1.88 1.90 . . 94  2042 61.00  . . . . 0.4530 . . . . . . . . . . . 0.4641 
'X-RAY DIFFRACTION' 1.90 1.93 . . 84  2381 71.00  . . . . 0.4434 . . . . . . . . . . . 0.4576 
'X-RAY DIFFRACTION' 1.93 1.96 . . 118 2215 68.00  . . . . 0.4400 . . . . . . . . . . . 0.5021 
'X-RAY DIFFRACTION' 1.96 1.99 . . 175 3272 100.00 . . . . 0.3687 . . . . . . . . . . . 0.4092 
'X-RAY DIFFRACTION' 1.99 2.02 . . 170 3287 100.00 . . . . 0.3529 . . . . . . . . . . . 0.3933 
'X-RAY DIFFRACTION' 2.02 2.05 . . 178 3300 100.00 . . . . 0.3558 . . . . . . . . . . . 0.3718 
'X-RAY DIFFRACTION' 2.05 2.09 . . 122 2426 75.00  . . . . 0.3603 . . . . . . . . . . . 0.4225 
'X-RAY DIFFRACTION' 2.09 2.12 . . 179 3285 100.00 . . . . 0.3236 . . . . . . . . . . . 0.3330 
'X-RAY DIFFRACTION' 2.12 2.17 . . 197 3300 100.00 . . . . 0.3086 . . . . . . . . . . . 0.3595 
'X-RAY DIFFRACTION' 2.17 2.21 . . 194 3251 100.00 . . . . 0.2894 . . . . . . . . . . . 0.3309 
'X-RAY DIFFRACTION' 2.21 2.26 . . 148 2583 79.00  . . . . 0.2822 . . . . . . . . . . . 0.3051 
'X-RAY DIFFRACTION' 2.26 2.31 . . 190 3257 99.00  . . . . 0.2656 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 2.31 2.37 . . 198 3242 100.00 . . . . 0.2776 . . . . . . . . . . . 0.3107 
'X-RAY DIFFRACTION' 2.37 2.43 . . 170 3319 100.00 . . . . 0.2625 . . . . . . . . . . . 0.3213 
'X-RAY DIFFRACTION' 2.43 2.50 . . 170 3281 100.00 . . . . 0.2479 . . . . . . . . . . . 0.3210 
'X-RAY DIFFRACTION' 2.50 2.58 . . 151 3328 100.00 . . . . 0.2461 . . . . . . . . . . . 0.2894 
'X-RAY DIFFRACTION' 2.58 2.66 . . 154 2745 99.00  . . . . 0.2471 . . . . . . . . . . . 0.2827 
'X-RAY DIFFRACTION' 2.68 2.78 . . 200 3208 98.00  . . . . 0.2522 . . . . . . . . . . . 0.3013 
'X-RAY DIFFRACTION' 2.78 2.91 . . 176 3324 100.00 . . . . 0.2532 . . . . . . . . . . . 0.2973 
'X-RAY DIFFRACTION' 2.91 3.06 . . 133 3339 100.00 . . . . 0.2348 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 3.06 3.26 . . 154 3333 100.00 . . . . 0.2320 . . . . . . . . . . . 0.3012 
'X-RAY DIFFRACTION' 3.26 3.51 . . 130 2941 88.00  . . . . 0.2254 . . . . . . . . . . . 0.2309 
'X-RAY DIFFRACTION' 3.51 3.86 . . 139 2999 90.00  . . . . 0.2075 . . . . . . . . . . . 0.2614 
'X-RAY DIFFRACTION' 3.86 4.42 . . 139 3041 90.00  . . . . 0.1768 . . . . . . . . . . . 0.1931 
'X-RAY DIFFRACTION' 4.42 5.57 . . 198 3321 100.00 . . . . 0.1775 . . . . . . . . . . . 0.2110 
'X-RAY DIFFRACTION' 5.57 10   . . 180 3351 99.00  . . . . 0.2119 . . . . . . . . . . . 0.2119 
# 
_struct.entry_id                     8Z4H 
_struct.title                        'Pseudomurein Endoisopeptidase PeiR' 
_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        8Z4H 
_struct_keywords.text            'Methanogenic archaea, pseudomurein, endopeptidases, 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 8Z4H A 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
2 1 8Z4H B 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
3 1 8Z4H C 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
4 1 8Z4H D 1 ? 228 ? D3DZZ6 1 ? 228 ? 1 228 
# 
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)' 2280  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  19480 ? 
2 'ABSA (A^2)' 2250  ? 
2 MORE         -5    ? 
2 'SSA (A^2)'  19560 ? 
# 
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 155 ? ASP C 145 LYS C 155 1 ? 11 
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 ? ? ? ? ? ? ? 2.590 ? ? 
disulf2 disulf ? ? B CYS 171 SG ? ? ? 1_555 B CYS 210 SG ? ? B CYS 171 B CYS 210 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
disulf3 disulf ? ? C CYS 171 SG ? ? ? 1_555 C CYS 210 SG ? ? C CYS 171 C CYS 210 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf4 disulf ? ? D CYS 171 SG ? ? ? 1_555 D CYS 210 SG ? ? D CYS 171 D CYS 210 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
# 
_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 ? ILE B 142 ? PHE B 137 ILE B 142 
AA6 2 TYR B 222 ? PRO B 227 ? TYR B 222 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 LEU A 184 ? N LEU A 184 O ALA A 196 ? O ALA A 196 
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 LEU B 30  ? N LEU B 30  O LEU B 43  ? O LEU B 43  
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 LEU C 184 ? N LEU C 184 O ALA C 196 ? O ALA C 196 
AA9 5 6 N TYR C 193 ? N TYR C 193 O TYR C 206 ? O TYR C 206 
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 TYR D 193 ? N TYR D 193 O TYR D 206 ? O TYR D 206 
# 
_pdbx_entry_details.entry_id                   8Z4H 
_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 O   D HOH 331 ? ? O   D HOH 354 ? ? 1.82 
2  1 O   B HOH 419 ? ? O   B HOH 429 ? ? 1.83 
3  1 O   D GLY 25  ? ? O   D HOH 301 ? ? 1.84 
4  1 NH2 C ARG 76  ? ? O   C HOH 301 ? ? 1.86 
5  1 NH1 C ARG 76  ? ? O   C HOH 301 ? ? 1.87 
6  1 N   D GLY 25  ? ? O   D HOH 301 ? ? 1.93 
7  1 O   A HOH 317 ? ? O   A HOH 402 ? ? 1.93 
8  1 O   B HOH 390 ? ? O   D HOH 410 ? ? 1.94 
9  1 O   B HOH 423 ? ? O   D HOH 410 ? ? 1.94 
10 1 NZ  C LYS 172 ? ? O   C HOH 302 ? ? 1.95 
11 1 O   B HOH 336 ? ? O   B HOH 389 ? ? 1.95 
12 1 O   C HOH 363 ? ? O   C HOH 393 ? ? 1.96 
13 1 O   D HOH 382 ? ? O   D HOH 412 ? ? 1.96 
14 1 O   A HOH 301 ? ? O   A HOH 319 ? ? 2.00 
15 1 O   D HOH 386 ? ? O   D HOH 402 ? ? 2.01 
16 1 O   C HOH 352 ? ? O   C HOH 386 ? ? 2.04 
17 1 OD2 A ASP 11  ? ? NH1 A ARG 15  ? ? 2.05 
18 1 O   A HOH 397 ? ? O   C HOH 394 ? ? 2.06 
19 1 OG1 C THR 176 ? ? O   C HOH 303 ? ? 2.06 
20 1 O   B HOH 379 ? ? O   B HOH 395 ? ? 2.08 
21 1 O   B HOH 422 ? ? O   B HOH 429 ? ? 2.08 
22 1 ND1 A HIS 162 ? ? O   A HOH 301 ? ? 2.08 
23 1 O   B HOH 414 ? ? O   B HOH 418 ? ? 2.09 
24 1 O   B HOH 387 ? ? O   B HOH 412 ? ? 2.10 
25 1 O   C HOH 344 ? ? O   C HOH 389 ? ? 2.10 
26 1 O   A HOH 354 ? ? O   A HOH 399 ? ? 2.10 
27 1 O   A HOH 400 ? ? O   A HOH 401 ? ? 2.11 
28 1 OE2 D GLU 110 ? ? O   D HOH 302 ? ? 2.11 
29 1 O   B HOH 346 ? ? O   B HOH 385 ? ? 2.11 
30 1 OE2 D GLU 40  ? ? O   D HOH 303 ? ? 2.11 
31 1 CZ  C ARG 76  ? ? O   C HOH 301 ? ? 2.13 
32 1 O   B HOH 327 ? ? O   B HOH 413 ? ? 2.14 
33 1 OXT C ALA 228 ? ? O   C HOH 304 ? ? 2.14 
34 1 O   A HOH 352 ? ? O   A HOH 402 ? ? 2.14 
35 1 OH  C TYR 29  ? ? O   C HOH 305 ? ? 2.15 
36 1 O   B HOH 390 ? ? O   B HOH 423 ? ? 2.16 
37 1 OXT D ALA 228 ? ? O   D HOH 304 ? ? 2.17 
38 1 OG  B SER 190 ? ? O   B HOH 301 ? ? 2.17 
39 1 O   B HOH 341 ? ? O   B HOH 394 ? ? 2.17 
40 1 O   B HOH 405 ? ? O   B HOH 418 ? ? 2.18 
41 1 NZ  A LYS 151 ? ? O   A HOH 302 ? ? 2.19 
42 1 NH1 B ARG 64  ? ? O   B HOH 302 ? ? 2.19 
43 1 O   C GLY 173 ? ? O   C HOH 306 ? ? 2.19 
44 1 C   D GLU 24  ? ? O   D HOH 301 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     428 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    D 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     409 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.90 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             D 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              145 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             D 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              145 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             D 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              145 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                124.05 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.75 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 172 ? ? -160.01 97.74  
2 1 LYS A 200 ? ? -137.16 -48.47 
3 1 LYS B 172 ? ? -137.20 -55.30 
4 1 LYS B 200 ? ? -135.40 -52.42 
5 1 LYS C 172 ? ? -134.61 -59.00 
6 1 LYS C 200 ? ? -136.18 -51.06 
7 1 HIS D 104 ? ? -144.83 59.95  
8 1 LYS D 172 ? ? -130.19 -62.13 
9 1 LYS D 200 ? ? -135.15 -51.86 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 406 ? 6.64 . 
2 1 O ? A HOH 407 ? 8.06 . 
# 
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   A3DCU2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z4H 
_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]   0.013545 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000438 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011505 
_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]   0.011370 
_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   ? 45.167  -14.379 36.550  1.00 53.56 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 44.632  -13.476 35.497  1.00 51.11 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 44.729  -12.024 35.990  1.00 48.84 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 45.067  -11.817 37.155  1.00 52.16 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 43.190  -13.854 35.145  1.00 52.14 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 43.039  -15.274 34.619  1.00 47.94 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 41.390  -16.014 34.780  1.00 59.03 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 41.735  -17.396 35.858  1.00 43.12 ? 1   MET A CE  1 
ATOM   9    N N   . VAL A 1 2   ? 44.471  -11.055 35.120  1.00 48.29 ? 2   VAL A N   1 
ATOM   10   C CA  . VAL A 1 2   ? 44.621  -9.619  35.486  1.00 45.41 ? 2   VAL A CA  1 
ATOM   11   C C   . VAL A 1 2   ? 43.473  -9.218  36.407  1.00 39.03 ? 2   VAL A C   1 
ATOM   12   O O   . VAL A 1 2   ? 42.351  -9.456  36.035  1.00 39.62 ? 2   VAL A O   1 
ATOM   13   C CB  . VAL A 1 2   ? 44.641  -8.764  34.211  1.00 48.74 ? 2   VAL A CB  1 
ATOM   14   C CG1 . VAL A 1 2   ? 44.683  -7.291  34.521  1.00 42.57 ? 2   VAL A CG1 1 
ATOM   15   C CG2 . VAL A 1 2   ? 45.795  -9.135  33.307  1.00 49.36 ? 2   VAL A CG2 1 
ATOM   16   N N   . ARG A 1 3   ? 43.764  -8.650  37.571  1.00 36.27 ? 3   ARG A N   1 
ATOM   17   C CA  . ARG A 1 3   ? 42.673  -8.250  38.491  1.00 39.04 ? 3   ARG A CA  1 
ATOM   18   C C   . ARG A 1 3   ? 42.744  -6.763  38.845  1.00 36.14 ? 3   ARG A C   1 
ATOM   19   O O   . ARG A 1 3   ? 43.815  -6.186  38.845  1.00 31.69 ? 3   ARG A O   1 
ATOM   20   C CB  . ARG A 1 3   ? 42.649  -9.119  39.745  1.00 36.97 ? 3   ARG A CB  1 
ATOM   21   C CG  . ARG A 1 3   ? 43.912  -9.020  40.564  1.00 42.42 ? 3   ARG A CG  1 
ATOM   22   C CD  . ARG A 1 3   ? 44.014  -10.213 41.472  1.00 46.61 ? 3   ARG A CD  1 
ATOM   23   N NE  . ARG A 1 3   ? 43.492  -9.871  42.772  1.00 49.66 ? 3   ARG A NE  1 
ATOM   24   C CZ  . ARG A 1 3   ? 44.150  -10.043 43.898  1.00 49.48 ? 3   ARG A CZ  1 
ATOM   25   N NH1 . ARG A 1 3   ? 45.363  -10.556 43.891  1.00 48.41 ? 3   ARG A NH1 1 
ATOM   26   N NH2 . ARG A 1 3   ? 43.583  -9.709  45.033  1.00 48.90 ? 3   ARG A NH2 1 
ATOM   27   N N   . PHE A 1 4   ? 41.589  -6.205  39.172  1.00 31.60 ? 4   PHE A N   1 
ATOM   28   C CA  . PHE A 1 4   ? 41.462  -4.774  39.478  1.00 31.97 ? 4   PHE A CA  1 
ATOM   29   C C   . PHE A 1 4   ? 40.743  -4.553  40.804  1.00 31.96 ? 4   PHE A C   1 
ATOM   30   O O   . PHE A 1 4   ? 39.753  -5.223  41.106  1.00 28.07 ? 4   PHE A O   1 
ATOM   31   C CB  . PHE A 1 4   ? 40.717  -4.055  38.369  1.00 30.65 ? 4   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 4   ? 41.293  -4.287  37.016  1.00 28.93 ? 4   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 4   ? 40.872  -5.359  36.249  1.00 31.67 ? 4   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 4   ? 42.265  -3.431  36.500  1.00 33.31 ? 4   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 4   ? 41.406  -5.579  34.995  1.00 31.55 ? 4   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 4   ? 42.817  -3.648  35.249  1.00 32.56 ? 4   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 4   ? 42.387  -4.706  34.497  1.00 32.27 ? 4   PHE A CZ  1 
ATOM   38   N N   . SER A 1 5   ? 41.252  -3.621  41.596  1.00 26.40 ? 5   SER A N   1 
ATOM   39   C CA  . SER A 1 5   ? 40.752  -3.409  42.941  1.00 30.09 ? 5   SER A CA  1 
ATOM   40   C C   . SER A 1 5   ? 39.423  -2.668  42.886  1.00 25.82 ? 5   SER A C   1 
ATOM   41   O O   . SER A 1 5   ? 39.072  -2.059  41.866  1.00 26.58 ? 5   SER A O   1 
ATOM   42   C CB  . SER A 1 5   ? 41.743  -2.561  43.755  1.00 32.56 ? 5   SER A CB  1 
ATOM   43   O OG  . SER A 1 5   ? 41.683  -1.199  43.281  1.00 29.13 ? 5   SER A OG  1 
ATOM   44   N N   . ARG A 1 6   ? 38.700  -2.700  44.007  1.00 26.58 ? 6   ARG A N   1 
ATOM   45   C CA  . ARG A 1 6   ? 37.445  -1.952  44.092  1.00 28.76 ? 6   ARG A CA  1 
ATOM   46   C C   . ARG A 1 6   ? 37.663  -0.477  43.763  1.00 30.16 ? 6   ARG A C   1 
ATOM   47   O O   . ARG A 1 6   ? 36.824  0.160   43.092  1.00 28.82 ? 6   ARG A O   1 
ATOM   48   C CB  . ARG A 1 6   ? 36.828  -2.131  45.487  1.00 29.07 ? 6   ARG A CB  1 
ATOM   49   C CG  . ARG A 1 6   ? 35.535  -1.352  45.727  1.00 28.32 ? 6   ARG A CG  1 
ATOM   50   C CD  . ARG A 1 6   ? 35.772  0.081   46.154  1.00 31.20 ? 6   ARG A CD  1 
ATOM   51   N NE  . ARG A 1 6   ? 34.536  0.845   46.202  1.00 31.74 ? 6   ARG A NE  1 
ATOM   52   C CZ  . ARG A 1 6   ? 34.468  2.130   46.520  1.00 33.38 ? 6   ARG A CZ  1 
ATOM   53   N NH1 . ARG A 1 6   ? 35.562  2.833   46.813  1.00 27.45 ? 6   ARG A NH1 1 
ATOM   54   N NH2 . ARG A 1 6   ? 33.276  2.708   46.594  1.00 26.79 ? 6   ARG A NH2 1 
ATOM   55   N N   . ASP A 1 7   ? 38.792  0.097   44.218  1.00 27.10 ? 7   ASP A N   1 
ATOM   56   C CA  . ASP A 1 7   ? 38.957  1.540   44.033  1.00 27.59 ? 7   ASP A CA  1 
ATOM   57   C C   . ASP A 1 7   ? 39.113  1.896   42.560  1.00 27.30 ? 7   ASP A C   1 
ATOM   58   O O   . ASP A 1 7   ? 38.564  2.913   42.097  1.00 25.76 ? 7   ASP A O   1 
ATOM   59   C CB  . ASP A 1 7   ? 40.111  2.022   44.902  1.00 26.86 ? 7   ASP A CB  1 
ATOM   60   C CG  . ASP A 1 7   ? 39.696  2.208   46.325  1.00 29.22 ? 7   ASP A CG  1 
ATOM   61   O OD1 . ASP A 1 7   ? 38.477  2.369   46.595  1.00 30.56 ? 7   ASP A OD1 1 
ATOM   62   O OD2 . ASP A 1 7   ? 40.560  2.086   47.208  1.00 29.71 ? 7   ASP A OD2 1 
ATOM   63   N N   . MET A 1 8   ? 39.844  1.067   41.809  1.00 25.42 ? 8   MET A N   1 
ATOM   64   C CA  . MET A 1 8   ? 39.990  1.284   40.385  1.00 25.60 ? 8   MET A CA  1 
ATOM   65   C C   . MET A 1 8   ? 38.687  1.042   39.660  1.00 26.94 ? 8   MET A C   1 
ATOM   66   O O   . MET A 1 8   ? 38.397  1.717   38.668  1.00 27.45 ? 8   MET A O   1 
ATOM   67   C CB  . MET A 1 8   ? 41.083  0.409   39.779  1.00 28.01 ? 8   MET A CB  1 
ATOM   68   C CG  . MET A 1 8   ? 42.574  0.909   40.051  1.00 33.14 ? 8   MET A CG  1 
ATOM   69   S SD  . MET A 1 8   ? 43.084  1.351   41.746  1.00 35.73 ? 8   MET A SD  1 
ATOM   70   C CE  . MET A 1 8   ? 44.783  1.809   41.559  1.00 35.40 ? 8   MET A CE  1 
ATOM   71   N N   . LEU A 1 9   ? 37.911  0.046   40.103  1.00 27.62 ? 9   LEU A N   1 
ATOM   72   C CA  . LEU A 1 9   ? 36.623  -0.207  39.464  1.00 25.50 ? 9   LEU A CA  1 
ATOM   73   C C   . LEU A 1 9   ? 35.650  0.943   39.698  1.00 25.15 ? 9   LEU A C   1 
ATOM   74   O O   . LEU A 1 9   ? 34.898  1.326   38.785  1.00 23.38 ? 9   LEU A O   1 
ATOM   75   C CB  . LEU A 1 9   ? 36.033  -1.506  39.998  1.00 23.50 ? 9   LEU A CB  1 
ATOM   76   C CG  . LEU A 1 9   ? 36.814  -2.753  39.609  1.00 24.26 ? 9   LEU A CG  1 
ATOM   77   C CD1 . LEU A 1 9   ? 36.604  -3.893  40.633  1.00 27.80 ? 9   LEU A CD1 1 
ATOM   78   C CD2 . LEU A 1 9   ? 36.438  -3.198  38.185  1.00 26.57 ? 9   LEU A CD2 1 
ATOM   79   N N   . GLN A 1 10  ? 35.597  1.452   40.930  1.00 25.31 ? 10  GLN A N   1 
ATOM   80   C CA  . GLN A 1 10  ? 34.718  2.589   41.225  1.00 26.26 ? 10  GLN A CA  1 
ATOM   81   C C   . GLN A 1 10  ? 35.103  3.805   40.391  1.00 27.94 ? 10  GLN A C   1 
ATOM   82   O O   . GLN A 1 10  ? 34.246  4.498   39.813  1.00 24.78 ? 10  GLN A O   1 
ATOM   83   C CB  . GLN A 1 10  ? 34.788  2.924   42.714  1.00 27.36 ? 10  GLN A CB  1 
ATOM   84   C CG  . GLN A 1 10  ? 34.028  4.161   43.093  1.00 27.37 ? 10  GLN A CG  1 
ATOM   85   C CD  . GLN A 1 10  ? 32.528  3.927   43.126  1.00 32.75 ? 10  GLN A CD  1 
ATOM   86   O OE1 . GLN A 1 10  ? 32.021  2.857   42.706  1.00 31.20 ? 10  GLN A OE1 1 
ATOM   87   N NE2 . GLN A 1 10  ? 31.795  4.934   43.609  1.00 37.30 ? 10  GLN A NE2 1 
ATOM   88   N N   . ASP A 1 11  ? 36.407  4.062   40.284  1.00 23.81 ? 11  ASP A N   1 
ATOM   89   C CA  . ASP A 1 11  ? 36.847  5.202   39.500  1.00 26.54 ? 11  ASP A CA  1 
ATOM   90   C C   . ASP A 1 11  ? 36.576  4.987   38.019  1.00 26.70 ? 11  ASP A C   1 
ATOM   91   O O   . ASP A 1 11  ? 36.148  5.922   37.322  1.00 28.82 ? 11  ASP A O   1 
ATOM   92   C CB  . ASP A 1 11  ? 38.335  5.474   39.762  1.00 25.79 ? 11  ASP A CB  1 
ATOM   93   C CG  . ASP A 1 11  ? 38.916  6.486   38.792  1.00 29.97 ? 11  ASP A CG  1 
ATOM   94   O OD1 . ASP A 1 11  ? 38.730  7.726   38.975  1.00 28.41 ? 11  ASP A OD1 1 
ATOM   95   O OD2 . ASP A 1 11  ? 39.523  6.021   37.791  1.00 30.57 ? 11  ASP A OD2 1 
ATOM   96   N N   . GLY A 1 12  ? 36.850  3.783   37.503  1.00 23.15 ? 12  GLY A N   1 
ATOM   97   C CA  . GLY A 1 12  ? 36.556  3.548   36.099  1.00 25.89 ? 12  GLY A CA  1 
ATOM   98   C C   . GLY A 1 12  ? 35.062  3.695   35.805  1.00 24.70 ? 12  GLY A C   1 
ATOM   99   O O   . GLY A 1 12  ? 34.678  4.154   34.724  1.00 22.86 ? 12  GLY A O   1 
ATOM   100  N N   . ALA A 1 13  ? 34.209  3.322   36.767  1.00 24.04 ? 13  ALA A N   1 
ATOM   101  C CA  . ALA A 1 13  ? 32.760  3.495   36.555  1.00 25.01 ? 13  ALA A CA  1 
ATOM   102  C C   . ALA A 1 13  ? 32.412  4.969   36.461  1.00 25.23 ? 13  ALA A C   1 
ATOM   103  O O   . ALA A 1 13  ? 31.712  5.379   35.534  1.00 25.70 ? 13  ALA A O   1 
ATOM   104  C CB  . ALA A 1 13  ? 31.974  2.839   37.679  1.00 23.67 ? 13  ALA A CB  1 
ATOM   105  N N   . LYS A 1 14  ? 32.983  5.795   37.343  1.00 26.26 ? 14  LYS A N   1 
ATOM   106  C CA  . LYS A 1 14  ? 32.790  7.243   37.238  1.00 26.48 ? 14  LYS A CA  1 
ATOM   107  C C   . LYS A 1 14  ? 33.152  7.754   35.845  1.00 29.34 ? 14  LYS A C   1 
ATOM   108  O O   . LYS A 1 14  ? 32.383  8.513   35.219  1.00 25.04 ? 14  LYS A O   1 
ATOM   109  C CB  . LYS A 1 14  ? 33.656  7.963   38.274  1.00 29.84 ? 14  LYS A CB  1 
ATOM   110  C CG  . LYS A 1 14  ? 33.091  7.933   39.652  1.00 34.85 ? 14  LYS A CG  1 
ATOM   111  C CD  . LYS A 1 14  ? 33.967  8.766   40.651  1.00 37.65 ? 14  LYS A CD  1 
ATOM   112  C CE  . LYS A 1 14  ? 33.347  10.167  40.930  1.00 35.56 ? 14  LYS A CE  1 
ATOM   113  N NZ  . LYS A 1 14  ? 34.024  11.152  40.027  1.00 37.66 ? 14  LYS A NZ  1 
ATOM   114  N N   . ARG A 1 15  ? 34.327  7.327   35.329  1.00 24.52 ? 15  ARG A N   1 
ATOM   115  C CA  . ARG A 1 15  ? 34.778  7.851   34.043  1.00 26.19 ? 15  ARG A CA  1 
ATOM   116  C C   . ARG A 1 15  ? 33.899  7.371   32.906  1.00 26.63 ? 15  ARG A C   1 
ATOM   117  O O   . ARG A 1 15  ? 33.640  8.133   31.969  1.00 28.46 ? 15  ARG A O   1 
ATOM   118  C CB  . ARG A 1 15  ? 36.264  7.470   33.793  1.00 31.24 ? 15  ARG A CB  1 
ATOM   119  C CG  . ARG A 1 15  ? 37.199  8.005   34.885  1.00 27.47 ? 15  ARG A CG  1 
ATOM   120  C CD  . ARG A 1 15  ? 38.705  8.021   34.473  1.00 34.03 ? 15  ARG A CD  1 
ATOM   121  N NE  . ARG A 1 15  ? 39.135  6.790   33.818  1.00 36.36 ? 15  ARG A NE  1 
ATOM   122  C CZ  . ARG A 1 15  ? 39.551  5.708   34.452  1.00 32.89 ? 15  ARG A CZ  1 
ATOM   123  N NH1 . ARG A 1 15  ? 39.633  5.664   35.773  1.00 34.38 ? 15  ARG A NH1 1 
ATOM   124  N NH2 . ARG A 1 15  ? 39.874  4.648   33.752  1.00 31.33 ? 15  ARG A NH2 1 
ATOM   125  N N   . MET A 1 16  ? 33.431  6.110   32.961  1.00 26.65 ? 16  MET A N   1 
ATOM   126  C CA  . MET A 1 16  ? 32.442  5.639   31.998  1.00 29.07 ? 16  MET A CA  1 
ATOM   127  C C   . MET A 1 16  ? 31.162  6.471   32.088  1.00 25.70 ? 16  MET A C   1 
ATOM   128  O O   . MET A 1 16  ? 30.586  6.855   31.073  1.00 28.33 ? 16  MET A O   1 
ATOM   129  C CB  . MET A 1 16  ? 32.093  4.158   32.254  1.00 26.26 ? 16  MET A CB  1 
ATOM   130  C CG  . MET A 1 16  ? 33.168  3.091   32.012  1.00 29.00 ? 16  MET A CG  1 
ATOM   131  S SD  . MET A 1 16  ? 33.673  3.004   30.313  1.00 28.13 ? 16  MET A SD  1 
ATOM   132  C CE  . MET A 1 16  ? 32.351  2.199   29.532  1.00 31.10 ? 16  MET A CE  1 
ATOM   133  N N   . PHE A 1 17  ? 30.672  6.695   33.305  1.00 27.06 ? 17  PHE A N   1 
ATOM   134  C CA  . PHE A 1 17  ? 29.444  7.460   33.510  1.00 26.95 ? 17  PHE A CA  1 
ATOM   135  C C   . PHE A 1 17  ? 29.599  8.888   33.005  1.00 27.87 ? 17  PHE A C   1 
ATOM   136  O O   . PHE A 1 17  ? 28.735  9.396   32.285  1.00 29.91 ? 17  PHE A O   1 
ATOM   137  C CB  . PHE A 1 17  ? 29.106  7.462   34.993  1.00 26.44 ? 17  PHE A CB  1 
ATOM   138  C CG  . PHE A 1 17  ? 27.798  8.135   35.327  1.00 28.22 ? 17  PHE A CG  1 
ATOM   139  C CD1 . PHE A 1 17  ? 26.619  7.671   34.804  1.00 24.14 ? 17  PHE A CD1 1 
ATOM   140  C CD2 . PHE A 1 17  ? 27.772  9.244   36.185  1.00 27.12 ? 17  PHE A CD2 1 
ATOM   141  C CE1 . PHE A 1 17  ? 25.395  8.279   35.153  1.00 29.75 ? 17  PHE A CE1 1 
ATOM   142  C CE2 . PHE A 1 17  ? 26.551  9.867   36.524  1.00 30.55 ? 17  PHE A CE2 1 
ATOM   143  C CZ  . PHE A 1 17  ? 25.371  9.371   36.016  1.00 30.29 ? 17  PHE A CZ  1 
ATOM   144  N N   . LYS A 1 18  ? 30.733  9.535   33.340  1.00 29.15 ? 18  LYS A N   1 
ATOM   145  C CA  . LYS A 1 18  ? 31.009  10.893  32.854  1.00 29.30 ? 18  LYS A CA  1 
ATOM   146  C C   . LYS A 1 18  ? 31.119  10.926  31.336  1.00 30.69 ? 18  LYS A C   1 
ATOM   147  O O   . LYS A 1 18  ? 30.633  11.856  30.694  1.00 29.90 ? 18  LYS A O   1 
ATOM   148  C CB  . LYS A 1 18  ? 32.310  11.413  33.473  1.00 33.72 ? 18  LYS A CB  1 
ATOM   149  C CG  . LYS A 1 18  ? 32.459  12.901  33.507  1.00 39.86 ? 18  LYS A CG  1 
ATOM   150  C CD  . LYS A 1 18  ? 33.137  13.374  34.820  1.00 45.76 ? 18  LYS A CD  1 
ATOM   151  C CE  . LYS A 1 18  ? 32.417  12.820  36.074  1.00 48.72 ? 18  LYS A CE  1 
ATOM   152  N NZ  . LYS A 1 18  ? 33.201  13.065  37.346  1.00 47.26 ? 18  LYS A NZ  1 
ATOM   153  N N   . TRP A 1 19  ? 31.753  9.918   30.737  1.00 31.99 ? 19  TRP A N   1 
ATOM   154  C CA  . TRP A 1 19  ? 31.818  9.850   29.277  1.00 33.80 ? 19  TRP A CA  1 
ATOM   155  C C   . TRP A 1 19  ? 30.423  9.745   28.661  1.00 33.52 ? 19  TRP A C   1 
ATOM   156  O O   . TRP A 1 19  ? 30.078  10.493  27.734  1.00 33.51 ? 19  TRP A O   1 
ATOM   157  C CB  . TRP A 1 19  ? 32.668  8.650   28.860  1.00 32.16 ? 19  TRP A CB  1 
ATOM   158  C CG  . TRP A 1 19  ? 32.804  8.530   27.365  1.00 34.80 ? 19  TRP A CG  1 
ATOM   159  C CD1 . TRP A 1 19  ? 31.913  7.988   26.500  1.00 34.84 ? 19  TRP A CD1 1 
ATOM   160  C CD2 . TRP A 1 19  ? 33.881  9.018   26.577  1.00 38.85 ? 19  TRP A CD2 1 
ATOM   161  N NE1 . TRP A 1 19  ? 32.366  8.096   25.218  1.00 34.45 ? 19  TRP A NE1 1 
ATOM   162  C CE2 . TRP A 1 19  ? 33.584  8.717   25.233  1.00 40.29 ? 19  TRP A CE2 1 
ATOM   163  C CE3 . TRP A 1 19  ? 35.084  9.680   26.877  1.00 41.46 ? 19  TRP A CE3 1 
ATOM   164  C CZ2 . TRP A 1 19  ? 34.446  9.063   24.173  1.00 36.54 ? 19  TRP A CZ2 1 
ATOM   165  C CZ3 . TRP A 1 19  ? 35.947  9.993   25.837  1.00 38.91 ? 19  TRP A CZ3 1 
ATOM   166  C CH2 . TRP A 1 19  ? 35.608  9.698   24.498  1.00 37.78 ? 19  TRP A CH2 1 
ATOM   167  N N   . LEU A 1 20  ? 29.583  8.855   29.199  1.00 31.36 ? 20  LEU A N   1 
ATOM   168  C CA  . LEU A 1 20  ? 28.235  8.664   28.640  1.00 32.75 ? 20  LEU A CA  1 
ATOM   169  C C   . LEU A 1 20  ? 27.407  9.934   28.730  1.00 34.18 ? 20  LEU A C   1 
ATOM   170  O O   . LEU A 1 20  ? 26.530  10.165  27.886  1.00 35.08 ? 20  LEU A O   1 
ATOM   171  C CB  . LEU A 1 20  ? 27.531  7.510   29.375  1.00 28.95 ? 20  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 20  ? 27.856  6.078   28.904  1.00 29.07 ? 20  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 20  ? 27.244  5.018   29.792  1.00 27.35 ? 20  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 20  ? 27.424  5.827   27.473  1.00 32.93 ? 20  LEU A CD2 1 
ATOM   175  N N   . ARG A 1 21  ? 27.667  10.768  29.747  1.00 32.85 ? 21  ARG A N   1 
ATOM   176  C CA  . ARG A 1 21  ? 26.959  12.035  29.885  1.00 35.89 ? 21  ARG A CA  1 
ATOM   177  C C   . ARG A 1 21  ? 27.008  12.892  28.636  1.00 36.34 ? 21  ARG A C   1 
ATOM   178  O O   . ARG A 1 21  ? 26.083  13.668  28.399  1.00 34.02 ? 21  ARG A O   1 
ATOM   179  C CB  . ARG A 1 21  ? 27.506  12.803  31.081  1.00 34.15 ? 21  ARG A CB  1 
ATOM   180  C CG  . ARG A 1 21  ? 26.670  14.006  31.412  1.00 34.47 ? 21  ARG A CG  1 
ATOM   181  C CD  . ARG A 1 21  ? 27.082  14.550  32.758  1.00 38.86 ? 21  ARG A CD  1 
ATOM   182  N NE  . ARG A 1 21  ? 28.429  15.104  32.679  1.00 47.29 ? 21  ARG A NE  1 
ATOM   183  C CZ  . ARG A 1 21  ? 29.328  15.059  33.654  1.00 50.02 ? 21  ARG A CZ  1 
ATOM   184  N NH1 . ARG A 1 21  ? 29.068  14.457  34.808  1.00 45.12 ? 21  ARG A NH1 1 
ATOM   185  N NH2 . ARG A 1 21  ? 30.517  15.633  33.465  1.00 48.37 ? 21  ARG A NH2 1 
ATOM   186  N N   . LYS A 1 22  ? 28.040  12.733  27.801  1.00 36.49 ? 22  LYS A N   1 
ATOM   187  C CA  . LYS A 1 22  ? 28.165  13.522  26.574  1.00 38.35 ? 22  LYS A CA  1 
ATOM   188  C C   . LYS A 1 22  ? 27.134  13.123  25.525  1.00 42.06 ? 22  LYS A C   1 
ATOM   189  O O   . LYS A 1 22  ? 26.939  13.853  24.543  1.00 40.96 ? 22  LYS A O   1 
ATOM   190  C CB  . LYS A 1 22  ? 29.590  13.378  25.996  1.00 40.59 ? 22  LYS A CB  1 
ATOM   191  C CG  . LYS A 1 22  ? 30.696  13.485  27.053  1.00 36.15 ? 22  LYS A CG  1 
ATOM   192  C CD  . LYS A 1 22  ? 32.093  13.572  26.424  1.00 43.39 ? 22  LYS A CD  1 
ATOM   193  C CE  . LYS A 1 22  ? 32.510  12.203  25.823  1.00 42.09 ? 22  LYS A CE  1 
ATOM   194  N NZ  . LYS A 1 22  ? 33.975  12.164  25.465  1.00 40.91 ? 22  LYS A NZ  1 
ATOM   195  N N   . GLY A 1 23  ? 26.475  11.986  25.723  1.00 43.12 ? 23  GLY A N   1 
ATOM   196  C CA  . GLY A 1 23  ? 25.477  11.510  24.748  1.00 44.17 ? 23  GLY A CA  1 
ATOM   197  C C   . GLY A 1 23  ? 26.121  11.079  23.450  1.00 44.69 ? 23  GLY A C   1 
ATOM   198  O O   . GLY A 1 23  ? 25.499  11.224  22.414  1.00 48.82 ? 23  GLY A O   1 
ATOM   199  N N   . GLU A 1 24  ? 27.324  10.521  23.512  1.00 46.24 ? 24  GLU A N   1 
ATOM   200  C CA  . GLU A 1 24  ? 28.036  10.113  22.274  1.00 47.49 ? 24  GLU A CA  1 
ATOM   201  C C   . GLU A 1 24  ? 28.397  8.630   22.299  1.00 47.18 ? 24  GLU A C   1 
ATOM   202  O O   . GLU A 1 24  ? 29.330  8.271   21.606  1.00 48.11 ? 24  GLU A O   1 
ATOM   203  C CB  . GLU A 1 24  ? 29.319  10.922  22.129  1.00 54.22 ? 24  GLU A CB  1 
ATOM   204  C CG  . GLU A 1 24  ? 29.219  12.016  21.089  1.00 58.64 ? 24  GLU A CG  1 
ATOM   205  C CD  . GLU A 1 24  ? 29.898  13.329  21.418  1.00 68.37 ? 24  GLU A CD  1 
ATOM   206  O OE1 . GLU A 1 24  ? 29.307  14.371  21.109  1.00 74.03 ? 24  GLU A OE1 1 
ATOM   207  O OE2 . GLU A 1 24  ? 31.011  13.307  21.981  1.00 70.33 ? 24  GLU A OE2 1 
ATOM   208  N N   . GLY A 1 25  ? 27.705  7.831   23.108  1.00 41.75 ? 25  GLY A N   1 
ATOM   209  C CA  . GLY A 1 25  ? 27.885  6.402   23.190  1.00 40.47 ? 25  GLY A CA  1 
ATOM   210  C C   . GLY A 1 25  ? 29.039  6.067   24.093  1.00 34.35 ? 25  GLY A C   1 
ATOM   211  O O   . GLY A 1 25  ? 29.645  6.934   24.734  1.00 35.83 ? 25  GLY A O   1 
ATOM   212  N N   . LEU A 1 26  ? 29.350  4.807   24.122  1.00 35.00 ? 26  LEU A N   1 
ATOM   213  C CA  . LEU A 1 26  ? 30.389  4.250   24.973  1.00 36.05 ? 26  LEU A CA  1 
ATOM   214  C C   . LEU A 1 26  ? 31.769  4.552   24.394  1.00 34.94 ? 26  LEU A C   1 
ATOM   215  O O   . LEU A 1 26  ? 31.912  4.719   23.186  1.00 34.40 ? 26  LEU A O   1 
ATOM   216  C CB  . LEU A 1 26  ? 30.214  2.745   25.101  1.00 35.24 ? 26  LEU A CB  1 
ATOM   217  C CG  . LEU A 1 26  ? 28.992  2.266   25.900  1.00 36.83 ? 26  LEU A CG  1 
ATOM   218  C CD1 . LEU A 1 26  ? 28.692  0.788   25.611  1.00 35.17 ? 26  LEU A CD1 1 
ATOM   219  C CD2 . LEU A 1 26  ? 29.301  2.494   27.371  1.00 35.57 ? 26  LEU A CD2 1 
ATOM   220  N N   . PRO A 1 27  ? 32.784  4.653   25.242  1.00 32.61 ? 27  PRO A N   1 
ATOM   221  C CA  . PRO A 1 27  ? 34.140  4.901   24.748  1.00 35.39 ? 27  PRO A CA  1 
ATOM   222  C C   . PRO A 1 27  ? 34.724  3.663   24.083  1.00 38.11 ? 27  PRO A C   1 
ATOM   223  O O   . PRO A 1 27  ? 34.303  2.528   24.322  1.00 34.71 ? 27  PRO A O   1 
ATOM   224  C CB  . PRO A 1 27  ? 34.923  5.267   26.014  1.00 36.05 ? 27  PRO A CB  1 
ATOM   225  C CG  . PRO A 1 27  ? 34.194  4.539   27.120  1.00 34.62 ? 27  PRO A CG  1 
ATOM   226  C CD  . PRO A 1 27  ? 32.731  4.511   26.705  1.00 32.58 ? 27  PRO A CD  1 
ATOM   227  N N   . ASN A 1 28  ? 35.747  3.892   23.259  1.00 36.20 ? 28  ASN A N   1 
ATOM   228  C CA  . ASN A 1 28  ? 36.349  2.779   22.517  1.00 35.94 ? 28  ASN A CA  1 
ATOM   229  C C   . ASN A 1 28  ? 37.181  1.862   23.403  1.00 37.53 ? 28  ASN A C   1 
ATOM   230  O O   . ASN A 1 28  ? 37.474  0.722   23.012  1.00 38.88 ? 28  ASN A O   1 
ATOM   231  C CB  . ASN A 1 28  ? 37.221  3.316   21.385  1.00 40.67 ? 28  ASN A CB  1 
ATOM   232  C CG  . ASN A 1 28  ? 36.419  3.745   20.188  1.00 42.66 ? 28  ASN A CG  1 
ATOM   233  O OD1 . ASN A 1 28  ? 35.421  3.123   19.844  1.00 47.18 ? 28  ASN A OD1 1 
ATOM   234  N ND2 . ASN A 1 28  ? 36.848  4.827   19.542  1.00 49.49 ? 28  ASN A ND2 1 
ATOM   235  N N   . TYR A 1 29  ? 37.606  2.340   24.563  1.00 35.33 ? 29  TYR A N   1 
ATOM   236  C CA  . TYR A 1 29  ? 38.387  1.529   25.484  1.00 35.47 ? 29  TYR A CA  1 
ATOM   237  C C   . TYR A 1 29  ? 38.318  2.192   26.843  1.00 34.06 ? 29  TYR A C   1 
ATOM   238  O O   . TYR A 1 29  ? 37.861  3.323   26.964  1.00 33.85 ? 29  TYR A O   1 
ATOM   239  C CB  . TYR A 1 29  ? 39.843  1.387   25.015  1.00 41.14 ? 29  TYR A CB  1 
ATOM   240  C CG  . TYR A 1 29  ? 40.589  2.710   24.888  1.00 40.46 ? 29  TYR A CG  1 
ATOM   241  C CD1 . TYR A 1 29  ? 41.084  3.387   26.019  1.00 42.02 ? 29  TYR A CD1 1 
ATOM   242  C CD2 . TYR A 1 29  ? 40.785  3.292   23.641  1.00 43.77 ? 29  TYR A CD2 1 
ATOM   243  C CE1 . TYR A 1 29  ? 41.754  4.587   25.901  1.00 42.59 ? 29  TYR A CE1 1 
ATOM   244  C CE2 . TYR A 1 29  ? 41.468  4.516   23.514  1.00 43.02 ? 29  TYR A CE2 1 
ATOM   245  C CZ  . TYR A 1 29  ? 41.938  5.148   24.648  1.00 44.69 ? 29  TYR A CZ  1 
ATOM   246  O OH  . TYR A 1 29  ? 42.614  6.342   24.518  1.00 52.46 ? 29  TYR A OH  1 
ATOM   247  N N   . LEU A 1 30  ? 38.770  1.471   27.868  1.00 32.65 ? 30  LEU A N   1 
ATOM   248  C CA  . LEU A 1 30  ? 38.821  2.002   29.226  1.00 33.91 ? 30  LEU A CA  1 
ATOM   249  C C   . LEU A 1 30  ? 40.174  1.640   29.814  1.00 34.92 ? 30  LEU A C   1 
ATOM   250  O O   . LEU A 1 30  ? 40.491  0.458   29.944  1.00 34.05 ? 30  LEU A O   1 
ATOM   251  C CB  . LEU A 1 30  ? 37.690  1.424   30.088  1.00 31.72 ? 30  LEU A CB  1 
ATOM   252  C CG  . LEU A 1 30  ? 37.721  1.820   31.576  1.00 30.16 ? 30  LEU A CG  1 
ATOM   253  C CD1 . LEU A 1 30  ? 37.356  3.273   31.767  1.00 30.79 ? 30  LEU A CD1 1 
ATOM   254  C CD2 . LEU A 1 30  ? 36.790  0.905   32.444  1.00 31.76 ? 30  LEU A CD2 1 
ATOM   255  N N   . ILE A 1 31  ? 40.959  2.637   30.184  1.00 35.27 ? 31  ILE A N   1 
ATOM   256  C CA  . ILE A 1 31  ? 42.279  2.391   30.746  1.00 33.15 ? 31  ILE A CA  1 
ATOM   257  C C   . ILE A 1 31  ? 42.164  2.239   32.256  1.00 31.55 ? 31  ILE A C   1 
ATOM   258  O O   . ILE A 1 31  ? 41.590  3.090   32.932  1.00 32.79 ? 31  ILE A O   1 
ATOM   259  C CB  . ILE A 1 31  ? 43.252  3.527   30.379  1.00 39.56 ? 31  ILE A CB  1 
ATOM   260  C CG1 . ILE A 1 31  ? 43.356  3.682   28.857  1.00 41.34 ? 31  ILE A CG1 1 
ATOM   261  C CG2 . ILE A 1 31  ? 44.608  3.250   30.976  1.00 36.54 ? 31  ILE A CG2 1 
ATOM   262  C CD1 . ILE A 1 31  ? 44.614  4.374   28.405  1.00 40.37 ? 31  ILE A CD1 1 
ATOM   263  N N   . MET A 1 32  ? 42.737  1.172   32.796  1.00 30.34 ? 32  MET A N   1 
ATOM   264  C CA  . MET A 1 32  ? 42.753  0.958   34.236  1.00 33.89 ? 32  MET A CA  1 
ATOM   265  C C   . MET A 1 32  ? 44.094  0.377   34.660  1.00 34.07 ? 32  MET A C   1 
ATOM   266  O O   . MET A 1 32  ? 44.753  -0.337  33.905  1.00 31.55 ? 32  MET A O   1 
ATOM   267  C CB  . MET A 1 32  ? 41.641  0.002   34.708  1.00 34.47 ? 32  MET A CB  1 
ATOM   268  C CG  . MET A 1 32  ? 40.199  0.378   34.220  1.00 36.82 ? 32  MET A CG  1 
ATOM   269  S SD  . MET A 1 32  ? 39.118  0.396   35.633  1.00 38.19 ? 32  MET A SD  1 
ATOM   270  C CE  . MET A 1 32  ? 39.467  -1.192  36.347  1.00 25.10 ? 32  MET A CE  1 
ATOM   271  N N   . TYR A 1 33  ? 44.414  0.595   35.932  1.00 33.72 ? 33  TYR A N   1 
ATOM   272  C CA  . TYR A 1 33  ? 45.642  0.124   36.534  1.00 38.22 ? 33  TYR A CA  1 
ATOM   273  C C   . TYR A 1 33  ? 45.364  -1.167  37.288  1.00 38.76 ? 33  TYR A C   1 
ATOM   274  O O   . TYR A 1 33  ? 44.406  -1.247  38.067  1.00 34.23 ? 33  TYR A O   1 
ATOM   275  C CB  . TYR A 1 33  ? 46.236  1.166   37.489  1.00 39.26 ? 33  TYR A CB  1 
ATOM   276  C CG  . TYR A 1 33  ? 46.940  2.284   36.760  1.00 36.50 ? 33  TYR A CG  1 
ATOM   277  C CD1 . TYR A 1 33  ? 46.230  3.406   36.329  1.00 31.91 ? 33  TYR A CD1 1 
ATOM   278  C CD2 . TYR A 1 33  ? 48.297  2.183   36.446  1.00 34.34 ? 33  TYR A CD2 1 
ATOM   279  C CE1 . TYR A 1 33  ? 46.861  4.435   35.631  1.00 34.60 ? 33  TYR A CE1 1 
ATOM   280  C CE2 . TYR A 1 33  ? 48.933  3.195   35.747  1.00 37.26 ? 33  TYR A CE2 1 
ATOM   281  C CZ  . TYR A 1 33  ? 48.221  4.317   35.344  1.00 34.65 ? 33  TYR A CZ  1 
ATOM   282  O OH  . TYR A 1 33  ? 48.876  5.302   34.637  1.00 36.07 ? 33  TYR A OH  1 
ATOM   283  N N   . ASP A 1 34  ? 46.182  -2.171  36.984  1.00 35.06 ? 34  ASP A N   1 
ATOM   284  C CA  . ASP A 1 34  ? 46.203  -3.472  37.615  1.00 38.96 ? 34  ASP A CA  1 
ATOM   285  C C   . ASP A 1 34  ? 46.434  -3.339  39.120  1.00 39.66 ? 34  ASP A C   1 
ATOM   286  O O   . ASP A 1 34  ? 47.153  -2.454  39.598  1.00 35.83 ? 34  ASP A O   1 
ATOM   287  C CB  . ASP A 1 34  ? 47.359  -4.262  36.937  1.00 45.25 ? 34  ASP A CB  1 
ATOM   288  C CG  . ASP A 1 34  ? 47.752  -5.525  37.637  1.00 43.25 ? 34  ASP A CG  1 
ATOM   289  O OD1 . ASP A 1 34  ? 47.829  -5.597  38.881  1.00 39.47 ? 34  ASP A OD1 1 
ATOM   290  O OD2 . ASP A 1 34  ? 48.016  -6.486  36.892  1.00 48.03 ? 34  ASP A OD2 1 
ATOM   291  N N   . MET A 1 35  ? 45.917  -4.280  39.941  1.00 35.13 ? 35  MET A N   1 
ATOM   292  C CA  . MET A 1 35  ? 46.103  -4.329  41.429  1.00 37.59 ? 35  MET A CA  1 
ATOM   293  C C   . MET A 1 35  ? 47.273  -5.194  41.991  1.00 42.27 ? 35  MET A C   1 
ATOM   294  O O   . MET A 1 35  ? 47.457  -5.230  43.178  1.00 40.36 ? 35  MET A O   1 
ATOM   295  C CB  . MET A 1 35  ? 44.800  -4.731  42.120  1.00 38.40 ? 35  MET A CB  1 
ATOM   296  C CG  . MET A 1 35  ? 44.891  -5.955  42.969  1.00 40.68 ? 35  MET A CG  1 
ATOM   297  S SD  . MET A 1 35  ? 43.302  -6.466  43.549  1.00 39.76 ? 35  MET A SD  1 
ATOM   298  C CE  . MET A 1 35  ? 43.484  -6.241  45.309  1.00 40.34 ? 35  MET A CE  1 
ATOM   299  N N   . ASP A 1 36  ? 48.147  -5.761  41.215  1.00 39.35 ? 36  ASP A N   1 
ATOM   300  C CA  . ASP A 1 36  ? 49.313  -6.565  41.625  1.00 42.95 ? 36  ASP A CA  1 
ATOM   301  C C   . ASP A 1 36  ? 50.565  -5.858  41.105  1.00 40.57 ? 36  ASP A C   1 
ATOM   302  O O   . ASP A 1 36  ? 51.398  -5.532  41.911  1.00 44.90 ? 36  ASP A O   1 
ATOM   303  C CB  . ASP A 1 36  ? 49.163  -7.979  41.079  1.00 41.57 ? 36  ASP A CB  1 
ATOM   304  C CG  . ASP A 1 36  ? 47.876  -8.615  41.556  1.00 43.78 ? 36  ASP A CG  1 
ATOM   305  O OD1 . ASP A 1 36  ? 47.748  -8.801  42.745  1.00 41.93 ? 36  ASP A OD1 1 
ATOM   306  O OD2 . ASP A 1 36  ? 47.031  -8.878  40.734  1.00 41.20 ? 36  ASP A OD2 1 
ATOM   307  N N   . ARG A 1 37  ? 50.628  -5.645  39.792  1.00 42.10 ? 37  ARG A N   1 
ATOM   308  C CA  . ARG A 1 37  ? 51.728  -4.989  39.044  1.00 43.07 ? 37  ARG A CA  1 
ATOM   309  C C   . ARG A 1 37  ? 51.595  -3.463  39.024  1.00 46.59 ? 37  ARG A C   1 
ATOM   310  O O   . ARG A 1 37  ? 52.598  -2.817  38.741  1.00 42.89 ? 37  ARG A O   1 
ATOM   311  C CB  . ARG A 1 37  ? 51.573  -5.339  37.569  1.00 46.50 ? 37  ARG A CB  1 
ATOM   312  C CG  . ARG A 1 37  ? 52.364  -6.551  37.118  1.00 50.38 ? 37  ARG A CG  1 
ATOM   313  C CD  . ARG A 1 37  ? 51.456  -7.733  37.260  1.00 58.35 ? 37  ARG A CD  1 
ATOM   314  N NE  . ARG A 1 37  ? 51.319  -8.531  36.057  1.00 67.25 ? 37  ARG A NE  1 
ATOM   315  C CZ  . ARG A 1 37  ? 50.167  -9.022  35.616  1.00 66.11 ? 37  ARG A CZ  1 
ATOM   316  N NH1 . ARG A 1 37  ? 49.037  -8.750  36.241  1.00 63.03 ? 37  ARG A NH1 1 
ATOM   317  N NH2 . ARG A 1 37  ? 50.148  -9.770  34.530  1.00 65.55 ? 37  ARG A NH2 1 
ATOM   318  N N   . ASN A 1 38  ? 50.374  -2.951  39.195  1.00 43.99 ? 38  ASN A N   1 
ATOM   319  C CA  . ASN A 1 38  ? 50.062  -1.537  39.181  1.00 42.64 ? 38  ASN A CA  1 
ATOM   320  C C   . ASN A 1 38  ? 50.443  -0.973  37.818  1.00 41.93 ? 38  ASN A C   1 
ATOM   321  O O   . ASN A 1 38  ? 51.024  0.105   37.697  1.00 45.18 ? 38  ASN A O   1 
ATOM   322  C CB  . ASN A 1 38  ? 50.735  -0.798  40.342  1.00 46.55 ? 38  ASN A CB  1 
ATOM   323  C CG  . ASN A 1 38  ? 49.909  -0.876  41.608  1.00 49.73 ? 38  ASN A CG  1 
ATOM   324  O OD1 . ASN A 1 38  ? 50.404  -1.317  42.649  1.00 53.16 ? 38  ASN A OD1 1 
ATOM   325  N ND2 . ASN A 1 38  ? 48.616  -0.486  41.519  1.00 48.81 ? 38  ASN A ND2 1 
ATOM   326  N N   . LYS A 1 39  ? 50.195  -1.781  36.794  1.00 42.29 ? 39  LYS A N   1 
ATOM   327  C CA  . LYS A 1 39  ? 50.454  -1.513  35.387  1.00 40.65 ? 39  LYS A CA  1 
ATOM   328  C C   . LYS A 1 39  ? 49.196  -1.042  34.667  1.00 40.15 ? 39  LYS A C   1 
ATOM   329  O O   . LYS A 1 39  ? 48.075  -1.397  35.041  1.00 38.51 ? 39  LYS A O   1 
ATOM   330  C CB  . LYS A 1 39  ? 51.011  -2.772  34.698  1.00 39.88 ? 39  LYS A CB  1 
ATOM   331  C CG  . LYS A 1 39  ? 50.770  -2.820  33.195  1.00 44.17 ? 39  LYS A CG  1 
ATOM   332  C CD  . LYS A 1 39  ? 51.850  -3.569  32.437  1.00 50.75 ? 39  LYS A CD  1 
ATOM   333  C CE  . LYS A 1 39  ? 51.347  -3.911  31.061  1.00 55.03 ? 39  LYS A CE  1 
ATOM   334  N NZ  . LYS A 1 39  ? 52.239  -4.917  30.338  1.00 57.95 ? 39  LYS A NZ  1 
ATOM   335  N N   . GLU A 1 40  ? 49.384  -0.229  33.639  1.00 38.41 ? 40  GLU A N   1 
ATOM   336  C CA  . GLU A 1 40  ? 48.278  0.258   32.829  1.00 38.31 ? 40  GLU A CA  1 
ATOM   337  C C   . GLU A 1 40  ? 47.722  -0.847  31.925  1.00 41.36 ? 40  GLU A C   1 
ATOM   338  O O   . GLU A 1 40  ? 48.488  -1.532  31.253  1.00 38.40 ? 40  GLU A O   1 
ATOM   339  C CB  . GLU A 1 40  ? 48.760  1.439   31.990  1.00 41.15 ? 40  GLU A CB  1 
ATOM   340  C CG  . GLU A 1 40  ? 48.058  2.734   32.382  1.00 42.65 ? 40  GLU A CG  1 
ATOM   341  C CD  . GLU A 1 40  ? 48.472  3.923   31.539  1.00 46.19 ? 40  GLU A CD  1 
ATOM   342  O OE1 . GLU A 1 40  ? 48.664  3.730   30.321  1.00 45.59 ? 40  GLU A OE1 1 
ATOM   343  O OE2 . GLU A 1 40  ? 48.588  5.048   32.097  1.00 47.16 ? 40  GLU A OE2 1 
ATOM   344  N N   . TYR A 1 41  ? 46.385  -1.013  31.892  1.00 38.30 ? 41  TYR A N   1 
ATOM   345  C CA  . TYR A 1 41  ? 45.720  -1.983  31.011  1.00 38.38 ? 41  TYR A CA  1 
ATOM   346  C C   . TYR A 1 41  ? 44.618  -1.315  30.191  1.00 37.78 ? 41  TYR A C   1 
ATOM   347  O O   . TYR A 1 41  ? 43.776  -0.597  30.735  1.00 38.62 ? 41  TYR A O   1 
ATOM   348  C CB  . TYR A 1 41  ? 45.124  -3.145  31.806  1.00 38.11 ? 41  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 41  ? 46.132  -4.186  32.213  1.00 43.63 ? 41  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 41  ? 46.860  -4.052  33.404  1.00 43.58 ? 41  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 41  ? 46.378  -5.294  31.411  1.00 43.34 ? 41  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 41  ? 47.809  -5.014  33.788  1.00 45.22 ? 41  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 41  ? 47.318  -6.258  31.785  1.00 43.83 ? 41  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 41  ? 48.030  -6.115  32.980  1.00 49.69 ? 41  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 41  ? 48.987  -7.062  33.359  1.00 51.66 ? 41  TYR A OH  1 
ATOM   356  N N   . LYS A 1 42  ? 44.622  -1.563  28.893  1.00 37.04 ? 42  LYS A N   1 
ATOM   357  C CA  . LYS A 1 42  ? 43.656  -0.947  27.967  1.00 37.45 ? 42  LYS A CA  1 
ATOM   358  C C   . LYS A 1 42  ? 42.591  -1.980  27.607  1.00 43.26 ? 42  LYS A C   1 
ATOM   359  O O   . LYS A 1 42  ? 42.879  -2.861  26.792  1.00 43.43 ? 42  LYS A O   1 
ATOM   360  C CB  . LYS A 1 42  ? 44.402  -0.464  26.728  1.00 43.11 ? 42  LYS A CB  1 
ATOM   361  C CG  . LYS A 1 42  ? 43.635  -0.585  25.427  1.00 45.21 ? 42  LYS A CG  1 
ATOM   362  C CD  . LYS A 1 42  ? 43.185  0.749   24.913  1.00 44.69 ? 42  LYS A CD  1 
ATOM   363  C CE  . LYS A 1 42  ? 44.313  1.570   24.345  1.00 45.15 ? 42  LYS A CE  1 
ATOM   364  N NZ  . LYS A 1 42  ? 44.082  1.878   22.915  1.00 52.51 ? 42  LYS A NZ  1 
ATOM   365  N N   . LEU A 1 43  ? 41.413  -1.839  28.215  1.00 35.48 ? 43  LEU A N   1 
ATOM   366  C CA  . LEU A 1 43  ? 40.298  -2.790  28.015  1.00 33.15 ? 43  LEU A CA  1 
ATOM   367  C C   . LEU A 1 43  ? 39.433  -2.333  26.861  1.00 33.84 ? 43  LEU A C   1 
ATOM   368  O O   . LEU A 1 43  ? 38.999  -1.209  26.881  1.00 35.16 ? 43  LEU A O   1 
ATOM   369  C CB  . LEU A 1 43  ? 39.444  -2.821  29.276  1.00 33.51 ? 43  LEU A CB  1 
ATOM   370  C CG  . LEU A 1 43  ? 40.180  -3.121  30.570  1.00 35.54 ? 43  LEU A CG  1 
ATOM   371  C CD1 . LEU A 1 43  ? 39.288  -2.874  31.764  1.00 32.44 ? 43  LEU A CD1 1 
ATOM   372  C CD2 . LEU A 1 43  ? 40.676  -4.544  30.586  1.00 39.42 ? 43  LEU A CD2 1 
ATOM   373  N N   . VAL A 1 44  ? 39.167  -3.232  25.929  1.00 33.52 ? 44  VAL A N   1 
ATOM   374  C CA  . VAL A 1 44  ? 38.234  -2.943  24.808  1.00 32.26 ? 44  VAL A CA  1 
ATOM   375  C C   . VAL A 1 44  ? 36.805  -3.195  25.322  1.00 34.08 ? 44  VAL A C   1 
ATOM   376  O O   . VAL A 1 44  ? 36.654  -3.837  26.363  1.00 33.38 ? 44  VAL A O   1 
ATOM   377  C CB  . VAL A 1 44  ? 38.556  -3.829  23.598  1.00 33.91 ? 44  VAL A CB  1 
ATOM   378  C CG1 . VAL A 1 44  ? 39.881  -3.465  22.971  1.00 39.14 ? 44  VAL A CG1 1 
ATOM   379  C CG2 . VAL A 1 44  ? 38.555  -5.295  23.968  1.00 34.17 ? 44  VAL A CG2 1 
ATOM   380  N N   . PRO A 1 45  ? 35.754  -2.696  24.652  1.00 37.07 ? 45  PRO A N   1 
ATOM   381  C CA  . PRO A 1 45  ? 34.375  -2.874  25.106  1.00 37.55 ? 45  PRO A CA  1 
ATOM   382  C C   . PRO A 1 45  ? 33.963  -4.257  25.643  1.00 39.03 ? 45  PRO A C   1 
ATOM   383  O O   . PRO A 1 45  ? 33.355  -4.307  26.645  1.00 36.56 ? 45  PRO A O   1 
ATOM   384  C CB  . PRO A 1 45  ? 33.580  -2.454  23.875  1.00 39.78 ? 45  PRO A CB  1 
ATOM   385  C CG  . PRO A 1 45  ? 34.426  -1.376  23.286  1.00 38.63 ? 45  PRO A CG  1 
ATOM   386  C CD  . PRO A 1 45  ? 35.838  -1.875  23.461  1.00 36.50 ? 45  PRO A CD  1 
ATOM   387  N N   . LYS A 1 46  ? 34.360  -5.334  24.979  1.00 40.41 ? 46  LYS A N   1 
ATOM   388  C CA  . LYS A 1 46  ? 33.999  -6.687  25.456  1.00 40.33 ? 46  LYS A CA  1 
ATOM   389  C C   . LYS A 1 46  ? 34.666  -6.967  26.804  1.00 36.33 ? 46  LYS A C   1 
ATOM   390  O O   . LYS A 1 46  ? 34.077  -7.721  27.574  1.00 29.15 ? 46  LYS A O   1 
ATOM   391  C CB  . LYS A 1 46  ? 34.385  -7.742  24.420  1.00 41.89 ? 46  LYS A CB  1 
ATOM   392  C CG  . LYS A 1 46  ? 33.475  -7.785  23.204  1.00 47.64 ? 46  LYS A CG  1 
ATOM   393  C CD  . LYS A 1 46  ? 34.033  -8.588  22.052  1.00 46.41 ? 46  LYS A CD  1 
ATOM   394  C CE  . LYS A 1 46  ? 35.347  -9.284  22.334  1.00 55.76 ? 46  LYS A CE  1 
ATOM   395  N NZ  . LYS A 1 46  ? 35.991  -9.729  21.077  1.00 58.79 ? 46  LYS A NZ  1 
ATOM   396  N N   . GLU A 1 47  ? 35.843  -6.382  27.063  1.00 30.71 ? 47  GLU A N   1 
ATOM   397  C CA  . GLU A 1 47  ? 36.552  -6.649  28.337  1.00 29.07 ? 47  GLU A CA  1 
ATOM   398  C C   . GLU A 1 47  ? 35.983  -5.778  29.456  1.00 31.11 ? 47  GLU A C   1 
ATOM   399  O O   . GLU A 1 47  ? 35.798  -6.281  30.557  1.00 26.56 ? 47  GLU A O   1 
ATOM   400  C CB  . GLU A 1 47  ? 38.034  -6.325  28.201  1.00 31.99 ? 47  GLU A CB  1 
ATOM   401  C CG  . GLU A 1 47  ? 38.782  -7.348  27.391  1.00 33.55 ? 47  GLU A CG  1 
ATOM   402  C CD  . GLU A 1 47  ? 40.228  -7.024  27.089  1.00 38.67 ? 47  GLU A CD  1 
ATOM   403  O OE1 . GLU A 1 47  ? 40.491  -5.899  26.688  1.00 34.66 ? 47  GLU A OE1 1 
ATOM   404  O OE2 . GLU A 1 47  ? 41.053  -7.917  27.227  1.00 35.42 ? 47  GLU A OE2 1 
ATOM   405  N N   . TYR A 1 48  ? 35.754  -4.502  29.171  1.00 27.22 ? 48  TYR A N   1 
ATOM   406  C CA  . TYR A 1 48  ? 35.222  -3.725  30.259  1.00 28.26 ? 48  TYR A CA  1 
ATOM   407  C C   . TYR A 1 48  ? 33.749  -4.082  30.515  1.00 28.28 ? 48  TYR A C   1 
ATOM   408  O O   . TYR A 1 48  ? 33.308  -4.054  31.665  1.00 25.11 ? 48  TYR A O   1 
ATOM   409  C CB  . TYR A 1 48  ? 35.474  -2.222  30.029  1.00 27.01 ? 48  TYR A CB  1 
ATOM   410  C CG  . TYR A 1 48  ? 34.782  -1.475  28.918  1.00 28.84 ? 48  TYR A CG  1 
ATOM   411  C CD1 . TYR A 1 48  ? 33.391  -1.384  28.855  1.00 28.12 ? 48  TYR A CD1 1 
ATOM   412  C CD2 . TYR A 1 48  ? 35.538  -0.722  28.002  1.00 31.81 ? 48  TYR A CD2 1 
ATOM   413  C CE1 . TYR A 1 48  ? 32.767  -0.655  27.859  1.00 30.84 ? 48  TYR A CE1 1 
ATOM   414  C CE2 . TYR A 1 48  ? 34.916  0.041   26.993  1.00 34.20 ? 48  TYR A CE2 1 
ATOM   415  C CZ  . TYR A 1 48  ? 33.531  0.080   26.928  1.00 34.51 ? 48  TYR A CZ  1 
ATOM   416  O OH  . TYR A 1 48  ? 32.889  0.831   25.940  1.00 32.76 ? 48  TYR A OH  1 
ATOM   417  N N   . ALA A 1 49  ? 32.993  -4.494  29.485  1.00 29.41 ? 49  ALA A N   1 
ATOM   418  C CA  . ALA A 1 49  ? 31.643  -4.982  29.761  1.00 29.78 ? 49  ALA A CA  1 
ATOM   419  C C   . ALA A 1 49  ? 31.668  -6.268  30.598  1.00 26.31 ? 49  ALA A C   1 
ATOM   420  O O   . ALA A 1 49  ? 30.849  -6.434  31.503  1.00 24.14 ? 49  ALA A O   1 
ATOM   421  C CB  . ALA A 1 49  ? 30.867  -5.193  28.461  1.00 30.09 ? 49  ALA A CB  1 
ATOM   422  N N   . GLY A 1 50  ? 32.605  -7.180  30.321  1.00 24.54 ? 50  GLY A N   1 
ATOM   423  C CA  . GLY A 1 50  ? 32.680  -8.415  31.084  1.00 25.61 ? 50  GLY A CA  1 
ATOM   424  C C   . GLY A 1 50  ? 33.149  -8.196  32.506  1.00 26.39 ? 50  GLY A C   1 
ATOM   425  O O   . GLY A 1 50  ? 32.655  -8.814  33.448  1.00 22.28 ? 50  GLY A O   1 
ATOM   426  N N   . LEU A 1 51  ? 34.132  -7.329  32.682  1.00 25.26 ? 51  LEU A N   1 
ATOM   427  C CA  . LEU A 1 51  ? 34.613  -7.034  34.023  1.00 23.82 ? 51  LEU A CA  1 
ATOM   428  C C   . LEU A 1 51  ? 33.490  -6.459  34.890  1.00 23.92 ? 51  LEU A C   1 
ATOM   429  O O   . LEU A 1 51  ? 33.328  -6.846  36.056  1.00 24.84 ? 51  LEU A O   1 
ATOM   430  C CB  . LEU A 1 51  ? 35.789  -6.035  33.908  1.00 25.25 ? 51  LEU A CB  1 
ATOM   431  C CG  . LEU A 1 51  ? 36.544  -5.640  35.167  1.00 25.06 ? 51  LEU A CG  1 
ATOM   432  C CD1 . LEU A 1 51  ? 37.385  -6.821  35.643  1.00 24.71 ? 51  LEU A CD1 1 
ATOM   433  C CD2 . LEU A 1 51  ? 37.455  -4.411  34.874  1.00 25.27 ? 51  LEU A CD2 1 
ATOM   434  N N   . TYR A 1 52  ? 32.721  -5.511  34.349  1.00 22.32 ? 52  TYR A N   1 
ATOM   435  C CA  . TYR A 1 52  ? 31.702  -4.867  35.151  1.00 23.22 ? 52  TYR A CA  1 
ATOM   436  C C   . TYR A 1 52  ? 30.468  -5.756  35.297  1.00 22.73 ? 52  TYR A C   1 
ATOM   437  O O   . TYR A 1 52  ? 29.779  -5.680  36.317  1.00 22.70 ? 52  TYR A O   1 
ATOM   438  C CB  . TYR A 1 52  ? 31.337  -3.506  34.568  1.00 23.00 ? 52  TYR A CB  1 
ATOM   439  C CG  . TYR A 1 52  ? 32.340  -2.467  34.989  1.00 21.42 ? 52  TYR A CG  1 
ATOM   440  C CD1 . TYR A 1 52  ? 32.265  -1.883  36.239  1.00 22.46 ? 52  TYR A CD1 1 
ATOM   441  C CD2 . TYR A 1 52  ? 33.404  -2.118  34.151  1.00 24.85 ? 52  TYR A CD2 1 
ATOM   442  C CE1 . TYR A 1 52  ? 33.242  -0.915  36.665  1.00 23.13 ? 52  TYR A CE1 1 
ATOM   443  C CE2 . TYR A 1 52  ? 34.397  -1.159  34.562  1.00 25.33 ? 52  TYR A CE2 1 
ATOM   444  C CZ  . TYR A 1 52  ? 34.312  -0.600  35.833  1.00 24.14 ? 52  TYR A CZ  1 
ATOM   445  O OH  . TYR A 1 52  ? 35.236  0.359   36.251  1.00 24.38 ? 52  TYR A OH  1 
ATOM   446  N N   . GLU A 1 53  ? 30.239  -6.644  34.336  1.00 19.72 ? 53  GLU A N   1 
ATOM   447  C CA  . GLU A 1 53  ? 29.247  -7.698  34.533  1.00 22.91 ? 53  GLU A CA  1 
ATOM   448  C C   . GLU A 1 53  ? 29.572  -8.511  35.775  1.00 22.30 ? 53  GLU A C   1 
ATOM   449  O O   . GLU A 1 53  ? 28.691  -8.744  36.618  1.00 23.00 ? 53  GLU A O   1 
ATOM   450  C CB  . GLU A 1 53  ? 29.170  -8.601  33.297  1.00 24.67 ? 53  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 53  ? 28.113  -9.739  33.396  1.00 26.05 ? 53  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 53  ? 28.160  -10.674 32.185  1.00 28.98 ? 53  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 53  ? 29.192  -11.299 31.907  1.00 30.84 ? 53  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 53  ? 27.156  -10.747 31.456  1.00 33.49 ? 53  GLU A OE2 1 
ATOM   455  N N   . SER A 1 54  ? 30.833  -8.971  35.905  1.00 21.56 ? 54  SER A N   1 
ATOM   456  C CA  . SER A 1 54  ? 31.226  -9.807  37.047  1.00 21.70 ? 54  SER A CA  1 
ATOM   457  C C   . SER A 1 54  ? 31.127  -9.012  38.321  1.00 22.11 ? 54  SER A C   1 
ATOM   458  O O   . SER A 1 54  ? 30.700  -9.546  39.346  1.00 22.35 ? 54  SER A O   1 
ATOM   459  C CB  . SER A 1 54  ? 32.687  -10.320 36.924  1.00 22.73 ? 54  SER A CB  1 
ATOM   460  O OG  . SER A 1 54  ? 32.882  -10.972 35.684  1.00 30.46 ? 54  SER A OG  1 
ATOM   461  N N   . ARG A 1 55  ? 31.575  -7.744  38.285  1.00 22.82 ? 55  ARG A N   1 
ATOM   462  C CA  . ARG A 1 55  ? 31.417  -6.877  39.440  1.00 22.30 ? 55  ARG A CA  1 
ATOM   463  C C   . ARG A 1 55  ? 29.953  -6.811  39.858  1.00 22.00 ? 55  ARG A C   1 
ATOM   464  O O   . ARG A 1 55  ? 29.638  -6.888  41.044  1.00 21.39 ? 55  ARG A O   1 
ATOM   465  C CB  . ARG A 1 55  ? 31.925  -5.466  39.140  1.00 24.69 ? 55  ARG A CB  1 
ATOM   466  C CG  . ARG A 1 55  ? 31.821  -4.485  40.297  1.00 22.90 ? 55  ARG A CG  1 
ATOM   467  C CD  . ARG A 1 55  ? 31.844  -2.986  39.783  1.00 23.34 ? 55  ARG A CD  1 
ATOM   468  N NE  . ARG A 1 55  ? 32.140  -2.022  40.835  1.00 24.42 ? 55  ARG A NE  1 
ATOM   469  C CZ  . ARG A 1 55  ? 31.868  -0.720  40.760  1.00 24.47 ? 55  ARG A CZ  1 
ATOM   470  N NH1 . ARG A 1 55  ? 31.264  -0.186  39.690  1.00 20.50 ? 55  ARG A NH1 1 
ATOM   471  N NH2 . ARG A 1 55  ? 32.202  0.060   41.782  1.00 24.63 ? 55  ARG A NH2 1 
ATOM   472  N N   . ASN A 1 56  ? 29.060  -6.639  38.893  1.00 20.67 ? 56  ASN A N   1 
ATOM   473  C CA  . ASN A 1 56  ? 27.632  -6.435  39.196  1.00 23.76 ? 56  ASN A CA  1 
ATOM   474  C C   . ASN A 1 56  ? 26.979  -7.714  39.718  1.00 22.96 ? 56  ASN A C   1 
ATOM   475  O O   . ASN A 1 56  ? 26.097  -7.661  40.583  1.00 21.78 ? 56  ASN A O   1 
ATOM   476  C CB  . ASN A 1 56  ? 26.911  -5.939  37.947  1.00 22.86 ? 56  ASN A CB  1 
ATOM   477  C CG  . ASN A 1 56  ? 27.310  -4.513  37.592  1.00 21.34 ? 56  ASN A CG  1 
ATOM   478  O OD1 . ASN A 1 56  ? 27.879  -3.816  38.434  1.00 19.97 ? 56  ASN A OD1 1 
ATOM   479  N ND2 . ASN A 1 56  ? 27.012  -4.071  36.366  1.00 20.88 ? 56  ASN A ND2 1 
ATOM   480  N N   . ILE A 1 57  ? 27.412  -8.872  39.210  1.00 20.68 ? 57  ILE A N   1 
ATOM   481  C CA  . ILE A 1 57  ? 26.942  -10.154 39.752  1.00 23.92 ? 57  ILE A CA  1 
ATOM   482  C C   . ILE A 1 57  ? 27.226  -10.232 41.246  1.00 23.28 ? 57  ILE A C   1 
ATOM   483  O O   . ILE A 1 57  ? 26.358  -10.578 42.055  1.00 25.30 ? 57  ILE A O   1 
ATOM   484  C CB  . ILE A 1 57  ? 27.582  -11.334 39.013  1.00 21.78 ? 57  ILE A CB  1 
ATOM   485  C CG1 . ILE A 1 57  ? 27.040  -11.425 37.580  1.00 23.29 ? 57  ILE A CG1 1 
ATOM   486  C CG2 . ILE A 1 57  ? 27.246  -12.655 39.777  1.00 23.00 ? 57  ILE A CG2 1 
ATOM   487  C CD1 . ILE A 1 57  ? 27.857  -12.375 36.680  1.00 23.18 ? 57  ILE A CD1 1 
ATOM   488  N N   . PHE A 1 58  ? 28.449  -9.947  41.633  1.00 21.17 ? 58  PHE A N   1 
ATOM   489  C CA  . PHE A 1 58  ? 28.770  -10.016 43.049  1.00 25.46 ? 58  PHE A CA  1 
ATOM   490  C C   . PHE A 1 58  ? 27.975  -8.975  43.832  1.00 24.98 ? 58  PHE A C   1 
ATOM   491  O O   . PHE A 1 58  ? 27.377  -9.274  44.880  1.00 24.51 ? 58  PHE A O   1 
ATOM   492  C CB  . PHE A 1 58  ? 30.288  -9.835  43.244  1.00 24.00 ? 58  PHE A CB  1 
ATOM   493  C CG  . PHE A 1 58  ? 30.744  -10.131 44.646  1.00 26.67 ? 58  PHE A CG  1 
ATOM   494  C CD1 . PHE A 1 58  ? 30.556  -9.198  45.670  1.00 30.05 ? 58  PHE A CD1 1 
ATOM   495  C CD2 . PHE A 1 58  ? 31.350  -11.326 44.947  1.00 28.78 ? 58  PHE A CD2 1 
ATOM   496  C CE1 . PHE A 1 58  ? 30.979  -9.460  46.971  1.00 31.97 ? 58  PHE A CE1 1 
ATOM   497  C CE2 . PHE A 1 58  ? 31.778  -11.592 46.244  1.00 32.79 ? 58  PHE A CE2 1 
ATOM   498  C CZ  . PHE A 1 58  ? 31.606  -10.659 47.250  1.00 31.83 ? 58  PHE A CZ  1 
ATOM   499  N N   . TRP A 1 59  ? 27.954  -7.748  43.324  1.00 23.93 ? 59  TRP A N   1 
ATOM   500  C CA  . TRP A 1 59  ? 27.244  -6.664  44.006  1.00 26.14 ? 59  TRP A CA  1 
ATOM   501  C C   . TRP A 1 59  ? 25.770  -6.991  44.217  1.00 23.25 ? 59  TRP A C   1 
ATOM   502  O O   . TRP A 1 59  ? 25.214  -6.726  45.286  1.00 25.40 ? 59  TRP A O   1 
ATOM   503  C CB  . TRP A 1 59  ? 27.383  -5.370  43.190  1.00 24.15 ? 59  TRP A CB  1 
ATOM   504  C CG  . TRP A 1 59  ? 27.343  -4.131  44.025  1.00 27.16 ? 59  TRP A CG  1 
ATOM   505  C CD1 . TRP A 1 59  ? 26.932  -4.012  45.325  1.00 27.49 ? 59  TRP A CD1 1 
ATOM   506  C CD2 . TRP A 1 59  ? 27.805  -2.819  43.626  1.00 25.88 ? 59  TRP A CD2 1 
ATOM   507  N NE1 . TRP A 1 59  ? 27.103  -2.704  45.752  1.00 28.45 ? 59  TRP A NE1 1 
ATOM   508  C CE2 . TRP A 1 59  ? 27.646  -1.963  44.731  1.00 27.49 ? 59  TRP A CE2 1 
ATOM   509  C CE3 . TRP A 1 59  ? 28.312  -2.295  42.435  1.00 25.10 ? 59  TRP A CE3 1 
ATOM   510  C CZ2 . TRP A 1 59  ? 27.961  -0.586  44.671  1.00 28.36 ? 59  TRP A CZ2 1 
ATOM   511  C CZ3 . TRP A 1 59  ? 28.636  -0.934  42.386  1.00 25.32 ? 59  TRP A CZ3 1 
ATOM   512  C CH2 . TRP A 1 59  ? 28.449  -0.101  43.496  1.00 23.59 ? 59  TRP A CH2 1 
ATOM   513  N N   . ILE A 1 60  ? 25.094  -7.484  43.182  1.00 24.25 ? 60  ILE A N   1 
ATOM   514  C CA  . ILE A 1 60  ? 23.647  -7.708  43.296  1.00 23.45 ? 60  ILE A CA  1 
ATOM   515  C C   . ILE A 1 60  ? 23.366  -8.911  44.179  1.00 24.91 ? 60  ILE A C   1 
ATOM   516  O O   . ILE A 1 60  ? 22.507  -8.867  45.061  1.00 23.84 ? 60  ILE A O   1 
ATOM   517  C CB  . ILE A 1 60  ? 23.016  -7.855  41.903  1.00 21.86 ? 60  ILE A CB  1 
ATOM   518  C CG1 . ILE A 1 60  ? 23.125  -6.514  41.155  1.00 19.21 ? 60  ILE A CG1 1 
ATOM   519  C CG2 . ILE A 1 60  ? 21.561  -8.428  41.997  1.00 27.62 ? 60  ILE A CG2 1 
ATOM   520  C CD1 . ILE A 1 60  ? 23.098  -6.697  39.611  1.00 21.02 ? 60  ILE A CD1 1 
ATOM   521  N N   . LYS A 1 61  ? 24.142  -9.984  44.007  1.00 25.08 ? 61  LYS A N   1 
ATOM   522  C CA  . LYS A 1 61  ? 23.908  -11.208 44.765  1.00 25.85 ? 61  LYS A CA  1 
ATOM   523  C C   . LYS A 1 61  ? 24.281  -11.058 46.235  1.00 25.27 ? 61  LYS A C   1 
ATOM   524  O O   . LYS A 1 61  ? 23.649  -11.671 47.098  1.00 24.38 ? 61  LYS A O   1 
ATOM   525  C CB  . LYS A 1 61  ? 24.687  -12.337 44.126  1.00 23.60 ? 61  LYS A CB  1 
ATOM   526  C CG  . LYS A 1 61  ? 24.179  -12.659 42.760  1.00 26.11 ? 61  LYS A CG  1 
ATOM   527  C CD  . LYS A 1 61  ? 22.622  -12.793 42.705  1.00 30.57 ? 61  LYS A CD  1 
ATOM   528  C CE  . LYS A 1 61  ? 22.133  -14.178 43.204  1.00 27.03 ? 61  LYS A CE  1 
ATOM   529  N NZ  . LYS A 1 61  ? 20.677  -14.387 42.756  1.00 26.86 ? 61  LYS A NZ  1 
ATOM   530  N N   . ASN A 1 62  ? 25.293  -10.265 46.543  1.00 25.45 ? 62  ASN A N   1 
ATOM   531  C CA  . ASN A 1 62  ? 25.784  -10.170 47.909  1.00 25.77 ? 62  ASN A CA  1 
ATOM   532  C C   . ASN A 1 62  ? 25.381  -8.904  48.628  1.00 28.18 ? 62  ASN A C   1 
ATOM   533  O O   . ASN A 1 62  ? 25.660  -8.800  49.826  1.00 27.47 ? 62  ASN A O   1 
ATOM   534  C CB  . ASN A 1 62  ? 27.317  -10.296 47.943  1.00 30.22 ? 62  ASN A CB  1 
ATOM   535  C CG  . ASN A 1 62  ? 27.786  -11.685 47.507  1.00 26.16 ? 62  ASN A CG  1 
ATOM   536  O OD1 . ASN A 1 62  ? 27.503  -12.659 48.164  1.00 28.06 ? 62  ASN A OD1 1 
ATOM   537  N ND2 . ASN A 1 62  ? 28.510  -11.757 46.438  1.00 28.59 ? 62  ASN A ND2 1 
ATOM   538  N N   . GLY A 1 63  ? 24.859  -7.900  47.916  1.00 26.10 ? 63  GLY A N   1 
ATOM   539  C CA  . GLY A 1 63  ? 24.472  -6.650  48.560  1.00 27.27 ? 63  GLY A CA  1 
ATOM   540  C C   . GLY A 1 63  ? 25.633  -5.772  48.970  1.00 29.26 ? 63  GLY A C   1 
ATOM   541  O O   . GLY A 1 63  ? 25.426  -4.782  49.680  1.00 31.94 ? 63  GLY A O   1 
ATOM   542  N N   . ARG A 1 64  ? 26.843  -6.080  48.512  1.00 28.43 ? 64  ARG A N   1 
ATOM   543  C CA  . ARG A 1 64  ? 28.025  -5.286  48.823  1.00 31.96 ? 64  ARG A CA  1 
ATOM   544  C C   . ARG A 1 64  ? 29.002  -5.415  47.664  1.00 29.73 ? 64  ARG A C   1 
ATOM   545  O O   . ARG A 1 64  ? 28.940  -6.348  46.859  1.00 30.39 ? 64  ARG A O   1 
ATOM   546  C CB  . ARG A 1 64  ? 28.684  -5.709  50.146  1.00 35.67 ? 64  ARG A CB  1 
ATOM   547  C CG  . ARG A 1 64  ? 29.568  -6.927  50.033  1.00 33.82 ? 64  ARG A CG  1 
ATOM   548  C CD  . ARG A 1 64  ? 30.020  -7.343  51.426  1.00 43.48 ? 64  ARG A CD  1 
ATOM   549  N NE  . ARG A 1 64  ? 30.139  -8.798  51.495  1.00 46.76 ? 64  ARG A NE  1 
ATOM   550  C CZ  . ARG A 1 64  ? 31.188  -9.504  51.078  1.00 49.38 ? 64  ARG A CZ  1 
ATOM   551  N NH1 . ARG A 1 64  ? 32.271  -8.919  50.572  1.00 44.09 ? 64  ARG A NH1 1 
ATOM   552  N NH2 . ARG A 1 64  ? 31.122  -10.835 51.109  1.00 48.38 ? 64  ARG A NH2 1 
ATOM   553  N N   . GLU A 1 65  ? 29.884  -4.445  47.580  1.00 30.08 ? 65  GLU A N   1 
ATOM   554  C CA  . GLU A 1 65  ? 30.851  -4.379  46.513  1.00 29.66 ? 65  GLU A CA  1 
ATOM   555  C C   . GLU A 1 65  ? 31.919  -5.453  46.675  1.00 27.98 ? 65  GLU A C   1 
ATOM   556  O O   . GLU A 1 65  ? 32.317  -5.776  47.799  1.00 30.39 ? 65  GLU A O   1 
ATOM   557  C CB  . GLU A 1 65  ? 31.507  -2.990  46.540  1.00 31.27 ? 65  GLU A CB  1 
ATOM   558  C CG  . GLU A 1 65  ? 31.070  -2.099  45.393  1.00 29.41 ? 65  GLU A CG  1 
ATOM   559  C CD  . GLU A 1 65  ? 31.818  -0.775  45.379  1.00 31.67 ? 65  GLU A CD  1 
ATOM   560  O OE1 . GLU A 1 65  ? 31.545  0.131   46.221  1.00 33.31 ? 65  GLU A OE1 1 
ATOM   561  O OE2 . GLU A 1 65  ? 32.756  -0.673  44.555  1.00 31.54 ? 65  GLU A OE2 1 
ATOM   562  N N   . PRO A 1 66  ? 32.398  -6.022  45.579  1.00 25.62 ? 66  PRO A N   1 
ATOM   563  C CA  . PRO A 1 66  ? 33.565  -6.903  45.650  1.00 28.40 ? 66  PRO A CA  1 
ATOM   564  C C   . PRO A 1 66  ? 34.825  -6.082  45.886  1.00 33.15 ? 66  PRO A C   1 
ATOM   565  O O   . PRO A 1 66  ? 34.946  -4.957  45.386  1.00 30.51 ? 66  PRO A O   1 
ATOM   566  C CB  . PRO A 1 66  ? 33.594  -7.578  44.279  1.00 27.52 ? 66  PRO A CB  1 
ATOM   567  C CG  . PRO A 1 66  ? 32.851  -6.616  43.380  1.00 25.99 ? 66  PRO A CG  1 
ATOM   568  C CD  . PRO A 1 66  ? 31.821  -5.954  44.223  1.00 25.74 ? 66  PRO A CD  1 
ATOM   569  N N   . ASN A 1 67  ? 35.719  -6.632  46.719  1.00 30.49 ? 67  ASN A N   1 
ATOM   570  C CA  . ASN A 1 67  ? 37.011  -6.003  47.018  1.00 33.96 ? 67  ASN A CA  1 
ATOM   571  C C   . ASN A 1 67  ? 37.925  -5.963  45.801  1.00 30.45 ? 67  ASN A C   1 
ATOM   572  O O   . ASN A 1 67  ? 38.757  -5.064  45.682  1.00 29.88 ? 67  ASN A O   1 
ATOM   573  C CB  . ASN A 1 67  ? 37.704  -6.763  48.156  1.00 36.22 ? 67  ASN A CB  1 
ATOM   574  C CG  . ASN A 1 67  ? 37.032  -6.546  49.484  1.00 40.59 ? 67  ASN A CG  1 
ATOM   575  O OD1 . ASN A 1 67  ? 36.555  -5.455  49.770  1.00 41.94 ? 67  ASN A OD1 1 
ATOM   576  N ND2 . ASN A 1 67  ? 36.957  -7.602  50.298  1.00 49.71 ? 67  ASN A ND2 1 
ATOM   577  N N   . TYR A 1 68  ? 37.739  -6.877  44.855  1.00 30.53 ? 68  TYR A N   1 
ATOM   578  C CA  . TYR A 1 68  ? 38.433  -6.867  43.575  1.00 28.89 ? 68  TYR A CA  1 
ATOM   579  C C   . TYR A 1 68  ? 37.684  -7.782  42.620  1.00 29.61 ? 68  TYR A C   1 
ATOM   580  O O   . TYR A 1 68  ? 36.893  -8.641  43.029  1.00 33.68 ? 68  TYR A O   1 
ATOM   581  C CB  . TYR A 1 68  ? 39.905  -7.326  43.706  1.00 33.02 ? 68  TYR A CB  1 
ATOM   582  C CG  . TYR A 1 68  ? 40.027  -8.784  44.075  1.00 33.91 ? 68  TYR A CG  1 
ATOM   583  C CD1 . TYR A 1 68  ? 40.039  -9.770  43.098  1.00 34.15 ? 68  TYR A CD1 1 
ATOM   584  C CD2 . TYR A 1 68  ? 40.058  -9.180  45.402  1.00 35.87 ? 68  TYR A CD2 1 
ATOM   585  C CE1 . TYR A 1 68  ? 40.112  -11.110 43.431  1.00 37.24 ? 68  TYR A CE1 1 
ATOM   586  C CE2 . TYR A 1 68  ? 40.127  -10.530 45.740  1.00 38.19 ? 68  TYR A CE2 1 
ATOM   587  C CZ  . TYR A 1 68  ? 40.163  -11.475 44.752  1.00 38.75 ? 68  TYR A CZ  1 
ATOM   588  O OH  . TYR A 1 68  ? 40.245  -12.809 45.093  1.00 49.70 ? 68  TYR A OH  1 
ATOM   589  N N   . VAL A 1 69  ? 37.912  -7.562  41.341  1.00 27.40 ? 69  VAL A N   1 
ATOM   590  C CA  . VAL A 1 69  ? 37.301  -8.381  40.308  1.00 27.89 ? 69  VAL A CA  1 
ATOM   591  C C   . VAL A 1 69  ? 38.417  -8.815  39.383  1.00 31.97 ? 69  VAL A C   1 
ATOM   592  O O   . VAL A 1 69  ? 39.264  -7.992  38.987  1.00 27.99 ? 69  VAL A O   1 
ATOM   593  C CB  . VAL A 1 69  ? 36.210  -7.621  39.519  1.00 26.56 ? 69  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 69  ? 35.672  -8.496  38.420  1.00 25.39 ? 69  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 69  ? 35.088  -7.125  40.454  1.00 24.82 ? 69  VAL A CG2 1 
ATOM   596  N N   . THR A 1 70  ? 38.447  -10.112 39.078  1.00 28.55 ? 70  THR A N   1 
ATOM   597  C CA  . THR A 1 70  ? 39.418  -10.641 38.134  1.00 30.17 ? 70  THR A CA  1 
ATOM   598  C C   . THR A 1 70  ? 38.777  -10.660 36.754  1.00 30.91 ? 70  THR A C   1 
ATOM   599  O O   . THR A 1 70  ? 37.595  -10.992 36.617  1.00 29.72 ? 70  THR A O   1 
ATOM   600  C CB  . THR A 1 70  ? 39.856  -12.050 38.551  1.00 34.15 ? 70  THR A CB  1 
ATOM   601  O OG1 . THR A 1 70  ? 40.481  -11.999 39.837  1.00 32.76 ? 70  THR A OG1 1 
ATOM   602  C CG2 . THR A 1 70  ? 40.801  -12.663 37.545  1.00 30.83 ? 70  THR A CG2 1 
ATOM   603  N N   . LEU A 1 71  ? 39.530  -10.235 35.746  1.00 28.00 ? 71  LEU A N   1 
ATOM   604  C CA  . LEU A 1 71  ? 39.032  -10.229 34.371  1.00 31.96 ? 71  LEU A CA  1 
ATOM   605  C C   . LEU A 1 71  ? 39.064  -11.647 33.816  1.00 36.82 ? 71  LEU A C   1 
ATOM   606  O O   . LEU A 1 71  ? 40.141  -12.186 33.497  1.00 35.77 ? 71  LEU A O   1 
ATOM   607  C CB  . LEU A 1 71  ? 39.849  -9.259  33.522  1.00 36.91 ? 71  LEU A CB  1 
ATOM   608  C CG  . LEU A 1 71  ? 39.532  -9.181  32.036  1.00 35.51 ? 71  LEU A CG  1 
ATOM   609  C CD1 . LEU A 1 71  ? 38.360  -8.265  31.792  1.00 36.24 ? 71  LEU A CD1 1 
ATOM   610  C CD2 . LEU A 1 71  ? 40.756  -8.680  31.314  1.00 40.74 ? 71  LEU A CD2 1 
ATOM   611  N N   . THR A 1 72  ? 37.882  -12.244 33.665  1.00 34.12 ? 72  THR A N   1 
ATOM   612  C CA  . THR A 1 72  ? 37.757  -13.644 33.267  1.00 36.43 ? 72  THR A CA  1 
ATOM   613  C C   . THR A 1 72  ? 36.923  -13.854 32.003  1.00 36.37 ? 72  THR A C   1 
ATOM   614  O O   . THR A 1 72  ? 36.949  -14.953 31.429  1.00 34.95 ? 72  THR A O   1 
ATOM   615  C CB  . THR A 1 72  ? 37.128  -14.462 34.417  1.00 36.60 ? 72  THR A CB  1 
ATOM   616  O OG1 . THR A 1 72  ? 35.842  -13.920 34.748  1.00 33.77 ? 72  THR A OG1 1 
ATOM   617  C CG2 . THR A 1 72  ? 38.008  -14.393 35.657  1.00 35.55 ? 72  THR A CG2 1 
ATOM   618  N N   . SER A 1 73  ? 36.193  -12.842 31.551  1.00 37.08 ? 73  SER A N   1 
ATOM   619  C CA  . SER A 1 73  ? 35.098  -13.044 30.612  1.00 34.33 ? 73  SER A CA  1 
ATOM   620  C C   . SER A 1 73  ? 34.929  -11.783 29.768  1.00 33.98 ? 73  SER A C   1 
ATOM   621  O O   . SER A 1 73  ? 35.495  -10.728 30.069  1.00 35.57 ? 73  SER A O   1 
ATOM   622  C CB  . SER A 1 73  ? 33.809  -13.395 31.365  1.00 35.73 ? 73  SER A CB  1 
ATOM   623  O OG  . SER A 1 73  ? 33.484  -12.352 32.286  1.00 41.01 ? 73  SER A OG  1 
ATOM   624  N N   . VAL A 1 74  ? 34.112  -11.947 28.747  1.00 32.28 ? 74  VAL A N   1 
ATOM   625  C CA  . VAL A 1 74  ? 33.699  -10.846 27.854  1.00 31.34 ? 74  VAL A CA  1 
ATOM   626  C C   . VAL A 1 74  ? 32.167  -10.831 27.817  1.00 32.01 ? 74  VAL A C   1 
ATOM   627  O O   . VAL A 1 74  ? 31.557  -11.819 28.161  1.00 32.16 ? 74  VAL A O   1 
ATOM   628  C CB  . VAL A 1 74  ? 34.315  -11.000 26.462  1.00 32.95 ? 74  VAL A CB  1 
ATOM   629  C CG1 . VAL A 1 74  ? 35.834  -10.970 26.535  1.00 33.55 ? 74  VAL A CG1 1 
ATOM   630  C CG2 . VAL A 1 74  ? 33.828  -12.262 25.795  1.00 31.89 ? 74  VAL A CG2 1 
ATOM   631  N N   . ALA A 1 75  ? 31.594  -9.703  27.441  1.00 33.05 ? 75  ALA A N   1 
ATOM   632  C CA  . ALA A 1 75  ? 30.131  -9.538  27.352  1.00 34.97 ? 75  ALA A CA  1 
ATOM   633  C C   . ALA A 1 75  ? 29.849  -8.329  26.460  1.00 33.93 ? 75  ALA A C   1 
ATOM   634  O O   . ALA A 1 75  ? 30.692  -7.482  26.377  1.00 34.82 ? 75  ALA A O   1 
ATOM   635  C CB  . ALA A 1 75  ? 29.550  -9.376  28.725  1.00 31.61 ? 75  ALA A CB  1 
ATOM   636  N N   . ARG A 1 76  ? 28.680  -8.287  25.862  1.00 37.12 ? 76  ARG A N   1 
ATOM   637  C CA  . ARG A 1 76  ? 28.395  -7.131  24.997  1.00 41.24 ? 76  ARG A CA  1 
ATOM   638  C C   . ARG A 1 76  ? 27.907  -5.968  25.863  1.00 35.54 ? 76  ARG A C   1 
ATOM   639  O O   . ARG A 1 76  ? 27.838  -4.884  25.351  1.00 36.09 ? 76  ARG A O   1 
ATOM   640  C CB  . ARG A 1 76  ? 27.570  -7.552  23.781  1.00 50.37 ? 76  ARG A CB  1 
ATOM   641  C CG  . ARG A 1 76  ? 28.255  -7.232  22.451  1.00 56.37 ? 76  ARG A CG  1 
ATOM   642  C CD  . ARG A 1 76  ? 29.743  -7.546  22.224  1.00 55.33 ? 76  ARG A CD  1 
ATOM   643  N NE  . ARG A 1 76  ? 30.732  -6.469  22.350  1.00 59.18 ? 76  ARG A NE  1 
ATOM   644  C CZ  . ARG A 1 76  ? 31.492  -6.007  21.355  1.00 62.90 ? 76  ARG A CZ  1 
ATOM   645  N NH1 . ARG A 1 76  ? 31.376  -6.512  20.135  1.00 61.72 ? 76  ARG A NH1 1 
ATOM   646  N NH2 . ARG A 1 76  ? 32.373  -5.045  21.576  1.00 64.67 ? 76  ARG A NH2 1 
ATOM   647  N N   . ASN A 1 77  ? 27.642  -6.219  27.141  1.00 30.09 ? 77  ASN A N   1 
ATOM   648  C CA  . ASN A 1 77  ? 27.190  -5.166  28.088  1.00 24.79 ? 77  ASN A CA  1 
ATOM   649  C C   . ASN A 1 77  ? 27.347  -5.670  29.523  1.00 24.75 ? 77  ASN A C   1 
ATOM   650  O O   . ASN A 1 77  ? 27.540  -6.837  29.699  1.00 27.16 ? 77  ASN A O   1 
ATOM   651  C CB  . ASN A 1 77  ? 25.775  -4.658  27.797  1.00 27.63 ? 77  ASN A CB  1 
ATOM   652  C CG  . ASN A 1 77  ? 24.701  -5.682  28.077  1.00 27.33 ? 77  ASN A CG  1 
ATOM   653  O OD1 . ASN A 1 77  ? 24.688  -6.293  29.120  1.00 25.08 ? 77  ASN A OD1 1 
ATOM   654  N ND2 . ASN A 1 77  ? 23.808  -5.869  27.136  1.00 27.83 ? 77  ASN A ND2 1 
ATOM   655  N N   . PRO A 1 78  ? 27.278  -4.808  30.547  1.00 24.17 ? 78  PRO A N   1 
ATOM   656  C CA  . PRO A 1 78  ? 27.434  -5.247  31.913  1.00 23.63 ? 78  PRO A CA  1 
ATOM   657  C C   . PRO A 1 78  ? 26.118  -5.577  32.634  1.00 24.48 ? 78  PRO A C   1 
ATOM   658  O O   . PRO A 1 78  ? 26.125  -5.742  33.792  1.00 22.43 ? 78  PRO A O   1 
ATOM   659  C CB  . PRO A 1 78  ? 28.085  -4.008  32.521  1.00 21.61 ? 78  PRO A CB  1 
ATOM   660  C CG  . PRO A 1 78  ? 27.449  -2.872  31.817  1.00 27.79 ? 78  PRO A CG  1 
ATOM   661  C CD  . PRO A 1 78  ? 27.130  -3.376  30.434  1.00 25.28 ? 78  PRO A CD  1 
ATOM   662  N N   . LEU A 1 79  ? 25.035  -5.745  31.894  1.00 24.39 ? 79  LEU A N   1 
ATOM   663  C CA  . LEU A 1 79  ? 23.730  -5.941  32.540  1.00 24.46 ? 79  LEU A CA  1 
ATOM   664  C C   . LEU A 1 79  ? 23.601  -7.333  33.168  1.00 26.29 ? 79  LEU A C   1 
ATOM   665  O O   . LEU A 1 79  ? 23.879  -8.350  32.522  1.00 25.78 ? 79  LEU A O   1 
ATOM   666  C CB  . LEU A 1 79  ? 22.626  -5.752  31.522  1.00 23.93 ? 79  LEU A CB  1 
ATOM   667  C CG  . LEU A 1 79  ? 21.225  -5.966  32.096  1.00 25.07 ? 79  LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 79  ? 20.898  -4.795  33.023  1.00 22.94 ? 79  LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 79  ? 20.236  -6.076  30.947  1.00 26.84 ? 79  LEU A CD2 1 
ATOM   670  N N   . VAL A 1 80  ? 23.184  -7.367  34.433  1.00 24.48 ? 80  VAL A N   1 
ATOM   671  C CA  . VAL A 1 80  ? 22.903  -8.589  35.189  1.00 22.82 ? 80  VAL A CA  1 
ATOM   672  C C   . VAL A 1 80  ? 21.424  -8.578  35.574  1.00 24.04 ? 80  VAL A C   1 
ATOM   673  O O   . VAL A 1 80  ? 20.928  -7.580  36.127  1.00 21.96 ? 80  VAL A O   1 
ATOM   674  C CB  . VAL A 1 80  ? 23.802  -8.662  36.442  1.00 24.50 ? 80  VAL A CB  1 
ATOM   675  C CG1 . VAL A 1 80  ? 23.464  -9.858  37.287  1.00 26.10 ? 80  VAL A CG1 1 
ATOM   676  C CG2 . VAL A 1 80  ? 25.327  -8.714  36.019  1.00 22.86 ? 80  VAL A CG2 1 
ATOM   677  N N   . MET A 1 81  ? 20.705  -9.657  35.237  1.00 21.20 ? 81  MET A N   1 
ATOM   678  C CA  . MET A 1 81  ? 19.271  -9.707  35.574  1.00 24.93 ? 81  MET A CA  1 
ATOM   679  C C   . MET A 1 81  ? 19.091  -9.528  37.079  1.00 25.33 ? 81  MET A C   1 
ATOM   680  O O   . MET A 1 81  ? 19.839  -10.094 37.888  1.00 26.18 ? 81  MET A O   1 
ATOM   681  C CB  . MET A 1 81  ? 18.629  -11.019 35.121  1.00 27.68 ? 81  MET A CB  1 
ATOM   682  C CG  . MET A 1 81  ? 17.108  -11.057 35.386  1.00 27.37 ? 81  MET A CG  1 
ATOM   683  S SD  . MET A 1 81  ? 16.295  -9.573  34.677  1.00 27.96 ? 81  MET A SD  1 
ATOM   684  C CE  . MET A 1 81  ? 14.732  -9.597  35.544  1.00 27.95 ? 81  MET A CE  1 
ATOM   685  N N   . ASP A 1 82  ? 18.161  -8.667  37.449  1.00 19.71 ? 82  ASP A N   1 
ATOM   686  C CA  . ASP A 1 82  ? 17.851  -8.347  38.836  1.00 22.82 ? 82  ASP A CA  1 
ATOM   687  C C   . ASP A 1 82  ? 16.339  -8.323  38.961  1.00 24.74 ? 82  ASP A C   1 
ATOM   688  O O   . ASP A 1 82  ? 15.685  -7.680  38.146  1.00 25.29 ? 82  ASP A O   1 
ATOM   689  C CB  . ASP A 1 82  ? 18.419  -6.983  39.215  1.00 24.17 ? 82  ASP A CB  1 
ATOM   690  C CG  . ASP A 1 82  ? 18.406  -6.736  40.684  1.00 22.12 ? 82  ASP A CG  1 
ATOM   691  O OD1 . ASP A 1 82  ? 18.197  -7.685  41.453  1.00 23.08 ? 82  ASP A OD1 1 
ATOM   692  O OD2 . ASP A 1 82  ? 18.619  -5.568  41.080  1.00 23.69 ? 82  ASP A OD2 1 
ATOM   693  N N   . TYR A 1 83  ? 15.788  -9.067  39.911  1.00 26.34 ? 83  TYR A N   1 
ATOM   694  C CA  . TYR A 1 83  ? 14.339  -9.204  40.031  1.00 26.37 ? 83  TYR A CA  1 
ATOM   695  C C   . TYR A 1 83  ? 13.767  -8.263  41.091  1.00 26.52 ? 83  TYR A C   1 
ATOM   696  O O   . TYR A 1 83  ? 14.457  -7.830  42.021  1.00 30.07 ? 83  TYR A O   1 
ATOM   697  C CB  . TYR A 1 83  ? 13.955  -10.662 40.341  1.00 25.49 ? 83  TYR A CB  1 
ATOM   698  C CG  . TYR A 1 83  ? 14.367  -11.657 39.277  1.00 27.27 ? 83  TYR A CG  1 
ATOM   699  C CD1 . TYR A 1 83  ? 15.659  -12.235 39.250  1.00 32.42 ? 83  TYR A CD1 1 
ATOM   700  C CD2 . TYR A 1 83  ? 13.489  -11.996 38.283  1.00 31.47 ? 83  TYR A CD2 1 
ATOM   701  C CE1 . TYR A 1 83  ? 16.018  -13.145 38.252  1.00 25.63 ? 83  TYR A CE1 1 
ATOM   702  C CE2 . TYR A 1 83  ? 13.828  -12.875 37.288  1.00 32.05 ? 83  TYR A CE2 1 
ATOM   703  C CZ  . TYR A 1 83  ? 15.068  -13.442 37.248  1.00 33.84 ? 83  TYR A CZ  1 
ATOM   704  O OH  . TYR A 1 83  ? 15.315  -14.380 36.201  1.00 41.57 ? 83  TYR A OH  1 
ATOM   705  N N   . GLN A 1 84  ? 12.498  -7.894  40.926  1.00 30.29 ? 84  GLN A N   1 
ATOM   706  C CA  . GLN A 1 84  ? 11.864  -7.072  41.949  1.00 27.48 ? 84  GLN A CA  1 
ATOM   707  C C   . GLN A 1 84  ? 11.604  -7.904  43.197  1.00 28.61 ? 84  GLN A C   1 
ATOM   708  O O   . GLN A 1 84  ? 11.191  -9.062  43.109  1.00 28.51 ? 84  GLN A O   1 
ATOM   709  C CB  . GLN A 1 84  ? 10.589  -6.451  41.439  1.00 28.98 ? 84  GLN A CB  1 
ATOM   710  C CG  . GLN A 1 84  ? 9.471   -7.438  41.076  1.00 28.68 ? 84  GLN A CG  1 
ATOM   711  C CD  . GLN A 1 84  ? 8.290   -6.746  40.372  1.00 29.86 ? 84  GLN A CD  1 
ATOM   712  O OE1 . GLN A 1 84  ? 8.276   -6.653  39.144  1.00 29.91 ? 84  GLN A OE1 1 
ATOM   713  N NE2 . GLN A 1 84  ? 7.302   -6.286  41.148  1.00 29.74 ? 84  GLN A NE2 1 
ATOM   714  N N   . ASN A 1 85  ? 11.870  -7.302  44.362  1.00 31.72 ? 85  ASN A N   1 
ATOM   715  C CA  . ASN A 1 85  ? 11.797  -7.953  45.673  1.00 32.45 ? 85  ASN A CA  1 
ATOM   716  C C   . ASN A 1 85  ? 10.399  -7.972  46.269  1.00 34.36 ? 85  ASN A C   1 
ATOM   717  O O   . ASN A 1 85  ? 10.175  -8.691  47.251  1.00 36.23 ? 85  ASN A O   1 
ATOM   718  C CB  . ASN A 1 85  ? 12.752  -7.271  46.671  1.00 30.67 ? 85  ASN A CB  1 
ATOM   719  C CG  . ASN A 1 85  ? 12.171  -6.007  47.289  1.00 36.16 ? 85  ASN A CG  1 
ATOM   720  O OD1 . ASN A 1 85  ? 11.546  -5.188  46.594  1.00 38.63 ? 85  ASN A OD1 1 
ATOM   721  N ND2 . ASN A 1 85  ? 12.400  -5.812  48.599  1.00 41.30 ? 85  ASN A ND2 1 
ATOM   722  N N   . THR A 1 86  ? 9.474   -7.189  45.735  1.00 30.34 ? 86  THR A N   1 
ATOM   723  C CA  . THR A 1 86  ? 8.084   -7.147  46.183  1.00 32.60 ? 86  THR A CA  1 
ATOM   724  C C   . THR A 1 86  ? 7.202   -7.092  44.942  1.00 32.59 ? 86  THR A C   1 
ATOM   725  O O   . THR A 1 86  ? 7.691   -6.932  43.817  1.00 31.59 ? 86  THR A O   1 
ATOM   726  C CB  . THR A 1 86  ? 7.812   -5.919  47.067  1.00 32.70 ? 86  THR A CB  1 
ATOM   727  O OG1 . THR A 1 86  ? 7.857   -4.769  46.228  1.00 30.00 ? 86  THR A OG1 1 
ATOM   728  C CG2 . THR A 1 86  ? 8.844   -5.758  48.187  1.00 35.43 ? 86  THR A CG2 1 
ATOM   729  N N   . ASN A 1 87  ? 5.882   -7.144  45.138  1.00 30.78 ? 87  ASN A N   1 
ATOM   730  C CA  . ASN A 1 87  ? 4.999   -7.001  43.992  1.00 31.15 ? 87  ASN A CA  1 
ATOM   731  C C   . ASN A 1 87  ? 4.809   -5.533  43.576  1.00 34.26 ? 87  ASN A C   1 
ATOM   732  O O   . ASN A 1 87  ? 4.066   -5.260  42.619  1.00 34.96 ? 87  ASN A O   1 
ATOM   733  C CB  . ASN A 1 87  ? 3.648   -7.659  44.302  1.00 36.37 ? 87  ASN A CB  1 
ATOM   734  C CG  . ASN A 1 87  ? 2.939   -7.037  45.516  1.00 38.94 ? 87  ASN A CG  1 
ATOM   735  O OD1 . ASN A 1 87  ? 3.034   -5.841  45.778  1.00 38.84 ? 87  ASN A OD1 1 
ATOM   736  N ND2 . ASN A 1 87  ? 2.208   -7.865  46.254  1.00 43.81 ? 87  ASN A ND2 1 
ATOM   737  N N   . TYR A 1 88  ? 5.517   -4.584  44.215  1.00 32.73 ? 88  TYR A N   1 
ATOM   738  C CA  . TYR A 1 88  ? 5.336   -3.176  43.890  1.00 31.29 ? 88  TYR A CA  1 
ATOM   739  C C   . TYR A 1 88  ? 6.630   -2.410  43.606  1.00 31.54 ? 88  TYR A C   1 
ATOM   740  O O   . TYR A 1 88  ? 6.578   -1.170  43.467  1.00 30.37 ? 88  TYR A O   1 
ATOM   741  C CB  . TYR A 1 88  ? 4.558   -2.480  45.026  1.00 31.39 ? 88  TYR A CB  1 
ATOM   742  C CG  . TYR A 1 88  ? 5.279   -2.470  46.369  1.00 32.96 ? 88  TYR A CG  1 
ATOM   743  C CD1 . TYR A 1 88  ? 5.154   -3.523  47.260  1.00 34.02 ? 88  TYR A CD1 1 
ATOM   744  C CD2 . TYR A 1 88  ? 6.072   -1.393  46.748  1.00 33.55 ? 88  TYR A CD2 1 
ATOM   745  C CE1 . TYR A 1 88  ? 5.808   -3.509  48.506  1.00 33.64 ? 88  TYR A CE1 1 
ATOM   746  C CE2 . TYR A 1 88  ? 6.756   -1.379  47.967  1.00 33.37 ? 88  TYR A CE2 1 
ATOM   747  C CZ  . TYR A 1 88  ? 6.612   -2.438  48.846  1.00 35.57 ? 88  TYR A CZ  1 
ATOM   748  O OH  . TYR A 1 88  ? 7.266   -2.428  50.067  1.00 32.50 ? 88  TYR A OH  1 
ATOM   749  N N   . THR A 1 89  ? 7.791   -3.079  43.507  1.00 28.99 ? 89  THR A N   1 
ATOM   750  C CA  . THR A 1 89  ? 9.053   -2.371  43.289  1.00 27.88 ? 89  THR A CA  1 
ATOM   751  C C   . THR A 1 89  ? 9.572   -2.525  41.860  1.00 26.74 ? 89  THR A C   1 
ATOM   752  O O   . THR A 1 89  ? 10.770  -2.375  41.617  1.00 25.42 ? 89  THR A O   1 
ATOM   753  C CB  . THR A 1 89  ? 10.135  -2.832  44.272  1.00 27.45 ? 89  THR A CB  1 
ATOM   754  O OG1 . THR A 1 89  ? 10.016  -4.238  44.512  1.00 26.36 ? 89  THR A OG1 1 
ATOM   755  C CG2 . THR A 1 89  ? 10.045  -2.082  45.605  1.00 26.13 ? 89  THR A CG2 1 
ATOM   756  N N   . CYS A 1 90  ? 8.675   -2.783  40.902  1.00 25.88 ? 90  CYS A N   1 
ATOM   757  C CA  . CYS A 1 90  ? 9.072   -2.918  39.502  1.00 27.28 ? 90  CYS A CA  1 
ATOM   758  C C   . CYS A 1 90  ? 9.790   -1.662  38.974  1.00 26.22 ? 90  CYS A C   1 
ATOM   759  O O   . CYS A 1 90  ? 10.760  -1.773  38.213  1.00 23.59 ? 90  CYS A O   1 
ATOM   760  C CB  . CYS A 1 90  ? 7.856   -3.247  38.630  1.00 25.89 ? 90  CYS A CB  1 
ATOM   761  S SG  . CYS A 1 90  ? 6.228   -2.421  39.052  1.00 27.33 ? 90  CYS A SG  1 
ATOM   762  N N   . CYS A 1 91  ? 9.316   -0.455  39.348  1.00 27.76 ? 91  CYS A N   1 
ATOM   763  C CA  . CYS A 1 91  ? 9.921   0.753   38.780  1.00 26.17 ? 91  CYS A CA  1 
ATOM   764  C C   . CYS A 1 91  ? 11.327  0.999   39.311  1.00 24.19 ? 91  CYS A C   1 
ATOM   765  O O   . CYS A 1 91  ? 12.253  1.195   38.497  1.00 23.11 ? 91  CYS A O   1 
ATOM   766  C CB  . CYS A 1 91  ? 8.996   1.954   38.996  1.00 25.77 ? 91  CYS A CB  1 
ATOM   767  S SG  . CYS A 1 91  ? 9.590   3.521   38.251  1.00 27.35 ? 91  CYS A SG  1 
ATOM   768  N N   . PRO A 1 92  ? 11.575  1.019   40.624  1.00 26.71 ? 92  PRO A N   1 
ATOM   769  C CA  . PRO A 1 92  ? 12.974  1.163   41.058  1.00 24.95 ? 92  PRO A CA  1 
ATOM   770  C C   . PRO A 1 92  ? 13.862  -0.016  40.630  1.00 24.64 ? 92  PRO A C   1 
ATOM   771  O O   . PRO A 1 92  ? 15.065  0.199   40.456  1.00 23.73 ? 92  PRO A O   1 
ATOM   772  C CB  . PRO A 1 92  ? 12.882  1.248   42.590  1.00 27.04 ? 92  PRO A CB  1 
ATOM   773  C CG  . PRO A 1 92  ? 11.462  0.615   42.919  1.00 25.41 ? 92  PRO A CG  1 
ATOM   774  C CD  . PRO A 1 92  ? 10.620  0.972   41.757  1.00 22.51 ? 92  PRO A CD  1 
ATOM   775  N N   . THR A 1 93  ? 13.336  -1.246  40.483  1.00 21.67 ? 93  THR A N   1 
ATOM   776  C CA  . THR A 1 93  ? 14.165  -2.325  39.931  1.00 22.47 ? 93  THR A CA  1 
ATOM   777  C C   . THR A 1 93  ? 14.571  -2.011  38.489  1.00 25.32 ? 93  THR A C   1 
ATOM   778  O O   . THR A 1 93  ? 15.756  -2.155  38.118  1.00 20.68 ? 93  THR A O   1 
ATOM   779  C CB  . THR A 1 93  ? 13.442  -3.673  39.988  1.00 23.34 ? 93  THR A CB  1 
ATOM   780  O OG1 . THR A 1 93  ? 13.035  -3.937  41.327  1.00 25.85 ? 93  THR A OG1 1 
ATOM   781  C CG2 . THR A 1 93  ? 14.338  -4.756  39.568  1.00 24.29 ? 93  THR A CG2 1 
ATOM   782  N N   . SER A 1 94  ? 13.623  -1.488  37.692  1.00 24.16 ? 94  SER A N   1 
ATOM   783  C CA  . SER A 1 94  ? 13.918  -1.085  36.309  1.00 21.16 ? 94  SER A CA  1 
ATOM   784  C C   . SER A 1 94  ? 14.950  0.048   36.258  1.00 21.69 ? 94  SER A C   1 
ATOM   785  O O   . SER A 1 94  ? 15.867  0.035   35.414  1.00 19.62 ? 94  SER A O   1 
ATOM   786  C CB  . SER A 1 94  ? 12.611  -0.681  35.612  1.00 24.47 ? 94  SER A CB  1 
ATOM   787  O OG  . SER A 1 94  ? 11.717  -1.793  35.425  1.00 22.34 ? 94  SER A OG  1 
ATOM   788  N N   . LEU A 1 95  ? 14.859  1.012   37.183  1.00 20.55 ? 95  LEU A N   1 
ATOM   789  C CA  . LEU A 1 95  ? 15.871  2.063   37.258  1.00 23.91 ? 95  LEU A CA  1 
ATOM   790  C C   . LEU A 1 95  ? 17.226  1.516   37.692  1.00 20.98 ? 95  LEU A C   1 
ATOM   791  O O   . LEU A 1 95  ? 18.233  1.888   37.117  1.00 21.02 ? 95  LEU A O   1 
ATOM   792  C CB  . LEU A 1 95  ? 15.419  3.158   38.215  1.00 23.27 ? 95  LEU A CB  1 
ATOM   793  C CG  . LEU A 1 95  ? 16.323  4.369   38.326  1.00 23.27 ? 95  LEU A CG  1 
ATOM   794  C CD1 . LEU A 1 95  ? 16.582  5.035   36.959  1.00 23.39 ? 95  LEU A CD1 1 
ATOM   795  C CD2 . LEU A 1 95  ? 15.699  5.343   39.304  1.00 25.86 ? 95  LEU A CD2 1 
ATOM   796  N N   . SER A 1 96  ? 17.261  0.574   38.652  1.00 23.70 ? 96  SER A N   1 
ATOM   797  C CA  . SER A 1 96  ? 18.519  -0.060  39.059  1.00 20.56 ? 96  SER A CA  1 
ATOM   798  C C   . SER A 1 96  ? 19.168  -0.814  37.900  1.00 19.61 ? 96  SER A C   1 
ATOM   799  O O   . SER A 1 96  ? 20.396  -0.708  37.664  1.00 20.40 ? 96  SER A O   1 
ATOM   800  C CB  . SER A 1 96  ? 18.267  -1.007  40.237  1.00 22.29 ? 96  SER A CB  1 
ATOM   801  O OG  . SER A 1 96  ? 19.489  -1.633  40.645  1.00 25.01 ? 96  SER A OG  1 
ATOM   802  N N   . LEU A 1 97  ? 18.369  -1.577  37.150  1.00 18.09 ? 97  LEU A N   1 
ATOM   803  C CA  . LEU A 1 97  ? 18.881  -2.216  35.936  1.00 20.93 ? 97  LEU A CA  1 
ATOM   804  C C   . LEU A 1 97  ? 19.481  -1.181  34.970  1.00 23.12 ? 97  LEU A C   1 
ATOM   805  O O   . LEU A 1 97  ? 20.591  -1.371  34.452  1.00 23.25 ? 97  LEU A O   1 
ATOM   806  C CB  . LEU A 1 97  ? 17.765  -2.998  35.248  1.00 20.88 ? 97  LEU A CB  1 
ATOM   807  C CG  . LEU A 1 97  ? 17.369  -4.300  35.969  1.00 22.22 ? 97  LEU A CG  1 
ATOM   808  C CD1 . LEU A 1 97  ? 16.022  -4.782  35.489  1.00 21.00 ? 97  LEU A CD1 1 
ATOM   809  C CD2 . LEU A 1 97  ? 18.419  -5.384  35.753  1.00 19.73 ? 97  LEU A CD2 1 
ATOM   810  N N   . ALA A 1 98  ? 18.761  -0.082  34.711  1.00 19.96 ? 98  ALA A N   1 
ATOM   811  C CA  . ALA A 1 98  ? 19.327  0.996   33.902  1.00 21.32 ? 98  ALA A CA  1 
ATOM   812  C C   . ALA A 1 98  ? 20.669  1.480   34.449  1.00 21.85 ? 98  ALA A C   1 
ATOM   813  O O   . ALA A 1 98  ? 21.593  1.763   33.672  1.00 21.04 ? 98  ALA A O   1 
ATOM   814  C CB  . ALA A 1 98  ? 18.385  2.195   33.861  1.00 20.41 ? 98  ALA A CB  1 
ATOM   815  N N   . SER A 1 99  ? 20.774  1.620   35.785  1.00 19.73 ? 99  SER A N   1 
ATOM   816  C CA  . SER A 1 99  ? 21.973  2.181   36.391  1.00 20.69 ? 99  SER A CA  1 
ATOM   817  C C   . SER A 1 99  ? 23.183  1.291   36.138  1.00 22.78 ? 99  SER A C   1 
ATOM   818  O O   . SER A 1 99  ? 24.308  1.788   36.097  1.00 21.48 ? 99  SER A O   1 
ATOM   819  C CB  . SER A 1 99  ? 21.768  2.393   37.894  1.00 21.03 ? 99  SER A CB  1 
ATOM   820  O OG  . SER A 1 99  ? 21.811  1.173   38.634  1.00 24.65 ? 99  SER A OG  1 
ATOM   821  N N   . GLN A 1 100 ? 22.971  -0.016  35.939  1.00 22.19 ? 100 GLN A N   1 
ATOM   822  C CA  . GLN A 1 100 ? 24.062  -0.900  35.508  1.00 21.47 ? 100 GLN A CA  1 
ATOM   823  C C   . GLN A 1 100 ? 24.555  -0.511  34.129  1.00 24.63 ? 100 GLN A C   1 
ATOM   824  O O   . GLN A 1 100 ? 25.766  -0.464  33.877  1.00 25.90 ? 100 GLN A O   1 
ATOM   825  C CB  . GLN A 1 100 ? 23.622  -2.379  35.468  1.00 22.98 ? 100 GLN A CB  1 
ATOM   826  C CG  . GLN A 1 100 ? 23.189  -3.042  36.776  1.00 22.28 ? 100 GLN A CG  1 
ATOM   827  C CD  . GLN A 1 100 ? 22.776  -4.461  36.516  1.00 21.44 ? 100 GLN A CD  1 
ATOM   828  O OE1 . GLN A 1 100 ? 23.469  -5.198  35.778  1.00 20.76 ? 100 GLN A OE1 1 
ATOM   829  N NE2 . GLN A 1 100 ? 21.587  -4.846  37.027  1.00 23.54 ? 100 GLN A NE2 1 
ATOM   830  N N   . MET A 1 101 ? 23.628  -0.328  33.191  1.00 23.06 ? 101 MET A N   1 
ATOM   831  C CA  . MET A 1 101 ? 24.010  0.016   31.824  1.00 24.58 ? 101 MET A CA  1 
ATOM   832  C C   . MET A 1 101 ? 24.735  1.348   31.762  1.00 25.15 ? 101 MET A C   1 
ATOM   833  O O   . MET A 1 101 ? 25.533  1.563   30.852  1.00 28.55 ? 101 MET A O   1 
ATOM   834  C CB  . MET A 1 101 ? 22.791  0.085   30.910  1.00 24.52 ? 101 MET A CB  1 
ATOM   835  C CG  . MET A 1 101 ? 21.986  -1.237  30.796  1.00 28.27 ? 101 MET A CG  1 
ATOM   836  S SD  . MET A 1 101 ? 22.906  -2.437  29.819  1.00 36.47 ? 101 MET A SD  1 
ATOM   837  C CE  . MET A 1 101 ? 22.606  -1.770  28.181  1.00 29.42 ? 101 MET A CE  1 
ATOM   838  N N   . LEU A 1 102 ? 24.454  2.262   32.680  1.00 24.25 ? 102 LEU A N   1 
ATOM   839  C CA  . LEU A 1 102 ? 25.069  3.581   32.678  1.00 22.72 ? 102 LEU A CA  1 
ATOM   840  C C   . LEU A 1 102 ? 26.356  3.635   33.481  1.00 25.15 ? 102 LEU A C   1 
ATOM   841  O O   . LEU A 1 102 ? 26.997  4.696   33.518  1.00 25.98 ? 102 LEU A O   1 
ATOM   842  C CB  . LEU A 1 102 ? 24.095  4.636   33.244  1.00 22.36 ? 102 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 102 ? 22.843  4.807   32.410  1.00 23.67 ? 102 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 102 ? 21.916  5.795   33.126  1.00 24.83 ? 102 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 102 ? 23.184  5.292   31.008  1.00 26.64 ? 102 LEU A CD2 1 
ATOM   846  N N   . TYR A 1 103 ? 26.761  2.516   34.098  1.00 25.36 ? 103 TYR A N   1 
ATOM   847  C CA  . TYR A 1 103 ? 27.989  2.439   34.885  1.00 26.03 ? 103 TYR A CA  1 
ATOM   848  C C   . TYR A 1 103 ? 27.940  3.364   36.095  1.00 28.73 ? 103 TYR A C   1 
ATOM   849  O O   . TYR A 1 103 ? 28.964  3.971   36.488  1.00 25.55 ? 103 TYR A O   1 
ATOM   850  C CB  . TYR A 1 103 ? 29.220  2.741   34.024  1.00 24.85 ? 103 TYR A CB  1 
ATOM   851  C CG  . TYR A 1 103 ? 29.542  1.638   33.054  1.00 26.70 ? 103 TYR A CG  1 
ATOM   852  C CD1 . TYR A 1 103 ? 28.884  1.545   31.860  1.00 25.39 ? 103 TYR A CD1 1 
ATOM   853  C CD2 . TYR A 1 103 ? 30.486  0.653   33.376  1.00 24.94 ? 103 TYR A CD2 1 
ATOM   854  C CE1 . TYR A 1 103 ? 29.136  0.543   30.992  1.00 25.46 ? 103 TYR A CE1 1 
ATOM   855  C CE2 . TYR A 1 103 ? 30.763  -0.374  32.489  1.00 24.62 ? 103 TYR A CE2 1 
ATOM   856  C CZ  . TYR A 1 103 ? 30.092  -0.406  31.291  1.00 27.60 ? 103 TYR A CZ  1 
ATOM   857  O OH  . TYR A 1 103 ? 30.346  -1.439  30.417  1.00 26.38 ? 103 TYR A OH  1 
ATOM   858  N N   . HIS A 1 104 ? 26.733  3.449   36.693  1.00 25.48 ? 104 HIS A N   1 
ATOM   859  C CA  . HIS A 1 104 ? 26.459  4.231   37.890  1.00 24.35 ? 104 HIS A CA  1 
ATOM   860  C C   . HIS A 1 104 ? 25.454  3.470   38.782  1.00 25.76 ? 104 HIS A C   1 
ATOM   861  O O   . HIS A 1 104 ? 24.345  3.937   39.084  1.00 22.60 ? 104 HIS A O   1 
ATOM   862  C CB  . HIS A 1 104 ? 25.949  5.615   37.480  1.00 23.29 ? 104 HIS A CB  1 
ATOM   863  C CG  . HIS A 1 104 ? 25.967  6.621   38.589  1.00 28.60 ? 104 HIS A CG  1 
ATOM   864  N ND1 . HIS A 1 104 ? 27.134  7.100   39.140  1.00 27.77 ? 104 HIS A ND1 1 
ATOM   865  C CD2 . HIS A 1 104 ? 24.956  7.240   39.250  1.00 26.09 ? 104 HIS A CD2 1 
ATOM   866  C CE1 . HIS A 1 104 ? 26.849  7.973   40.086  1.00 28.12 ? 104 HIS A CE1 1 
ATOM   867  N NE2 . HIS A 1 104 ? 25.532  8.068   40.184  1.00 27.64 ? 104 HIS A NE2 1 
ATOM   868  N N   . TYR A 1 105 ? 25.869  2.265   39.216  1.00 24.58 ? 105 TYR A N   1 
ATOM   869  C CA  . TYR A 1 105 ? 24.969  1.310   39.859  1.00 20.69 ? 105 TYR A CA  1 
ATOM   870  C C   . TYR A 1 105 ? 24.408  1.857   41.151  1.00 24.32 ? 105 TYR A C   1 
ATOM   871  O O   . TYR A 1 105 ? 25.148  2.354   42.005  1.00 22.42 ? 105 TYR A O   1 
ATOM   872  C CB  . TYR A 1 105 ? 25.679  -0.012  40.128  1.00 23.66 ? 105 TYR A CB  1 
ATOM   873  C CG  . TYR A 1 105 ? 24.852  -0.976  40.963  1.00 21.34 ? 105 TYR A CG  1 
ATOM   874  C CD1 . TYR A 1 105 ? 23.733  -1.579  40.430  1.00 20.99 ? 105 TYR A CD1 1 
ATOM   875  C CD2 . TYR A 1 105 ? 25.159  -1.207  42.308  1.00 21.74 ? 105 TYR A CD2 1 
ATOM   876  C CE1 . TYR A 1 105 ? 22.953  -2.483  41.180  1.00 21.16 ? 105 TYR A CE1 1 
ATOM   877  C CE2 . TYR A 1 105 ? 24.352  -2.094  43.083  1.00 22.90 ? 105 TYR A CE2 1 
ATOM   878  C CZ  . TYR A 1 105 ? 23.281  -2.727  42.505  1.00 22.21 ? 105 TYR A CZ  1 
ATOM   879  O OH  . TYR A 1 105 ? 22.507  -3.589  43.251  1.00 21.30 ? 105 TYR A OH  1 
ATOM   880  N N   . LYS A 1 106 ? 23.070  1.778   41.272  1.00 23.46 ? 106 LYS A N   1 
ATOM   881  C CA  . LYS A 1 106 ? 22.323  2.035   42.495  1.00 23.77 ? 106 LYS A CA  1 
ATOM   882  C C   . LYS A 1 106 ? 21.396  0.845   42.702  1.00 23.14 ? 106 LYS A C   1 
ATOM   883  O O   . LYS A 1 106 ? 20.735  0.406   41.759  1.00 21.58 ? 106 LYS A O   1 
ATOM   884  C CB  . LYS A 1 106 ? 21.503  3.327   42.380  1.00 24.66 ? 106 LYS A CB  1 
ATOM   885  C CG  . LYS A 1 106 ? 22.353  4.500   42.022  1.00 23.00 ? 106 LYS A CG  1 
ATOM   886  C CD  . LYS A 1 106 ? 23.181  4.968   43.235  1.00 27.57 ? 106 LYS A CD  1 
ATOM   887  C CE  . LYS A 1 106 ? 24.069  6.184   42.811  1.00 26.87 ? 106 LYS A CE  1 
ATOM   888  N NZ  . LYS A 1 106 ? 25.211  6.414   43.734  1.00 34.66 ? 106 LYS A NZ  1 
ATOM   889  N N   . SER A 1 107 ? 21.384  0.293   43.901  1.00 22.16 ? 107 SER A N   1 
ATOM   890  C CA  . SER A 1 107 ? 20.604  -0.910  44.162  1.00 23.16 ? 107 SER A CA  1 
ATOM   891  C C   . SER A 1 107 ? 19.098  -0.619  44.091  1.00 24.44 ? 107 SER A C   1 
ATOM   892  O O   . SER A 1 107 ? 18.641  0.528   44.176  1.00 21.15 ? 107 SER A O   1 
ATOM   893  C CB  . SER A 1 107 ? 20.958  -1.450  45.546  1.00 24.21 ? 107 SER A CB  1 
ATOM   894  O OG  . SER A 1 107 ? 20.332  -0.636  46.545  1.00 25.69 ? 107 SER A OG  1 
ATOM   895  N N   . GLU A 1 108 ? 18.326  -1.699  43.994  1.00 23.50 ? 108 GLU A N   1 
ATOM   896  C CA  . GLU A 1 108 ? 16.866  -1.604  43.968  1.00 25.15 ? 108 GLU A CA  1 
ATOM   897  C C   . GLU A 1 108 ? 16.328  -0.835  45.165  1.00 22.93 ? 108 GLU A C   1 
ATOM   898  O O   . GLU A 1 108 ? 15.462  0.034   45.026  1.00 27.13 ? 108 GLU A O   1 
ATOM   899  C CB  . GLU A 1 108 ? 16.273  -3.013  43.937  1.00 24.94 ? 108 GLU A CB  1 
ATOM   900  C CG  . GLU A 1 108 ? 14.822  -3.053  44.400  1.00 23.92 ? 108 GLU A CG  1 
ATOM   901  C CD  . GLU A 1 108 ? 14.162  -4.381  43.967  1.00 31.30 ? 108 GLU A CD  1 
ATOM   902  O OE1 . GLU A 1 108 ? 12.926  -4.470  44.023  1.00 27.17 ? 108 GLU A OE1 1 
ATOM   903  O OE2 . GLU A 1 108 ? 14.927  -5.319  43.519  1.00 30.24 ? 108 GLU A OE2 1 
ATOM   904  N N   . SER A 1 109 ? 16.809  -1.144  46.362  1.00 23.28 ? 109 SER A N   1 
ATOM   905  C CA  . SER A 1 109 ? 16.316  -0.424  47.532  1.00 25.61 ? 109 SER A CA  1 
ATOM   906  C C   . SER A 1 109 ? 16.765  1.042   47.552  1.00 24.09 ? 109 SER A C   1 
ATOM   907  O O   . SER A 1 109 ? 15.995  1.897   47.986  1.00 24.82 ? 109 SER A O   1 
ATOM   908  C CB  . SER A 1 109 ? 16.711  -1.145  48.823  1.00 27.75 ? 109 SER A CB  1 
ATOM   909  O OG  . SER A 1 109 ? 18.071  -1.375  48.847  1.00 32.53 ? 109 SER A OG  1 
ATOM   910  N N   . GLU A 1 110 ? 18.005  1.353   47.133  1.00 25.66 ? 110 GLU A N   1 
ATOM   911  C CA  . GLU A 1 110 ? 18.445  2.753   47.009  1.00 25.54 ? 110 GLU A CA  1 
ATOM   912  C C   . GLU A 1 110 ? 17.533  3.519   46.054  1.00 27.39 ? 110 GLU A C   1 
ATOM   913  O O   . GLU A 1 110 ? 17.155  4.677   46.317  1.00 28.00 ? 110 GLU A O   1 
ATOM   914  C CB  . GLU A 1 110 ? 19.885  2.812   46.475  1.00 28.45 ? 110 GLU A CB  1 
ATOM   915  C CG  . GLU A 1 110 ? 21.014  2.635   47.481  1.00 32.33 ? 110 GLU A CG  1 
ATOM   916  C CD  . GLU A 1 110 ? 22.428  2.752   46.826  1.00 36.04 ? 110 GLU A CD  1 
ATOM   917  O OE1 . GLU A 1 110 ? 22.738  2.082   45.801  1.00 33.24 ? 110 GLU A OE1 1 
ATOM   918  O OE2 . GLU A 1 110 ? 23.239  3.562   47.317  1.00 44.06 ? 110 GLU A OE2 1 
ATOM   919  N N   . CYS A 1 111 ? 17.174  2.884   44.921  1.00 24.73 ? 111 CYS A N   1 
ATOM   920  C CA  . CYS A 1 111 ? 16.268  3.519   43.973  1.00 25.72 ? 111 CYS A CA  1 
ATOM   921  C C   . CYS A 1 111 ? 14.864  3.682   44.565  1.00 27.53 ? 111 CYS A C   1 
ATOM   922  O O   . CYS A 1 111 ? 14.246  4.731   44.410  1.00 26.74 ? 111 CYS A O   1 
ATOM   923  C CB  . CYS A 1 111 ? 16.210  2.707   42.680  1.00 26.10 ? 111 CYS A CB  1 
ATOM   924  S SG  . CYS A 1 111 ? 17.729  2.743   41.657  1.00 24.38 ? 111 CYS A SG  1 
ATOM   925  N N   . ALA A 1 112 ? 14.346  2.673   45.273  1.00 27.24 ? 112 ALA A N   1 
ATOM   926  C CA  . ALA A 1 112 ? 12.986  2.801   45.816  1.00 26.92 ? 112 ALA A CA  1 
ATOM   927  C C   . ALA A 1 112 ? 12.930  3.914   46.864  1.00 31.59 ? 112 ALA A C   1 
ATOM   928  O O   . ALA A 1 112 ? 11.949  4.665   46.950  1.00 30.80 ? 112 ALA A O   1 
ATOM   929  C CB  . ALA A 1 112 ? 12.521  1.495   46.449  1.00 25.08 ? 112 ALA A CB  1 
ATOM   930  N N   . LYS A 1 113 ? 13.940  3.976   47.724  1.00 28.29 ? 113 LYS A N   1 
ATOM   931  C CA  . LYS A 1 113 ? 14.005  5.051   48.692  1.00 28.31 ? 113 LYS A CA  1 
ATOM   932  C C   . LYS A 1 113 ? 13.990  6.415   47.993  1.00 32.17 ? 113 LYS A C   1 
ATOM   933  O O   . LYS A 1 113 ? 13.247  7.329   48.392  1.00 33.10 ? 113 LYS A O   1 
ATOM   934  C CB  . LYS A 1 113 ? 15.194  4.839   49.606  1.00 28.73 ? 113 LYS A CB  1 
ATOM   935  C CG  . LYS A 1 113 ? 15.455  6.006   50.499  1.00 31.48 ? 113 LYS A CG  1 
ATOM   936  C CD  . LYS A 1 113 ? 15.934  5.539   51.879  1.00 40.44 ? 113 LYS A CD  1 
ATOM   937  C CE  . LYS A 1 113 ? 16.025  6.729   52.845  1.00 39.21 ? 113 LYS A CE  1 
ATOM   938  N NZ  . LYS A 1 113 ? 17.085  7.688   52.412  1.00 49.19 ? 113 LYS A NZ  1 
ATOM   939  N N   . ALA A 1 114 ? 14.792  6.571   46.941  1.00 30.26 ? 114 ALA A N   1 
ATOM   940  C CA  . ALA A 1 114 ? 14.849  7.846   46.239  1.00 31.94 ? 114 ALA A CA  1 
ATOM   941  C C   . ALA A 1 114 ? 13.524  8.164   45.554  1.00 32.55 ? 114 ALA A C   1 
ATOM   942  O O   . ALA A 1 114 ? 13.014  9.288   45.662  1.00 30.39 ? 114 ALA A O   1 
ATOM   943  C CB  . ALA A 1 114 ? 15.986  7.829   45.217  1.00 29.65 ? 114 ALA A CB  1 
ATOM   944  N N   . LEU A 1 115 ? 12.926  7.174   44.866  1.00 27.46 ? 115 LEU A N   1 
ATOM   945  C CA  . LEU A 1 115 ? 11.725  7.445   44.086  1.00 32.86 ? 115 LEU A CA  1 
ATOM   946  C C   . LEU A 1 115 ? 10.497  7.641   44.965  1.00 28.77 ? 115 LEU A C   1 
ATOM   947  O O   . LEU A 1 115 ? 9.505   8.224   44.506  1.00 32.01 ? 115 LEU A O   1 
ATOM   948  C CB  . LEU A 1 115 ? 11.451  6.313   43.096  1.00 29.87 ? 115 LEU A CB  1 
ATOM   949  C CG  . LEU A 1 115 ? 12.556  6.034   42.073  1.00 29.10 ? 115 LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 115 ? 12.024  5.053   41.019  1.00 26.42 ? 115 LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 115 ? 13.092  7.342   41.458  1.00 29.25 ? 115 LEU A CD2 1 
ATOM   952  N N   . GLY A 1 116 ? 10.551  7.196   46.217  1.00 29.74 ? 116 GLY A N   1 
ATOM   953  C CA  . GLY A 1 116 ? 9.374   7.226   47.067  1.00 34.84 ? 116 GLY A CA  1 
ATOM   954  C C   . GLY A 1 116 ? 8.387   6.124   46.783  1.00 33.75 ? 116 GLY A C   1 
ATOM   955  O O   . GLY A 1 116 ? 7.189   6.314   46.985  1.00 31.22 ? 116 GLY A O   1 
ATOM   956  N N   . THR A 1 117 ? 8.864   4.960   46.357  1.00 32.38 ? 117 THR A N   1 
ATOM   957  C CA  . THR A 1 117 ? 7.980   3.835   46.065  1.00 31.50 ? 117 THR A CA  1 
ATOM   958  C C   . THR A 1 117 ? 7.222   3.436   47.311  1.00 30.10 ? 117 THR A C   1 
ATOM   959  O O   . THR A 1 117 ? 7.789   3.392   48.402  1.00 35.38 ? 117 THR A O   1 
ATOM   960  C CB  . THR A 1 117 ? 8.823   2.634   45.597  1.00 32.86 ? 117 THR A CB  1 
ATOM   961  O OG1 . THR A 1 117 ? 9.706   3.015   44.517  1.00 30.32 ? 117 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 117 ? 7.923   1.458   45.207  1.00 28.54 ? 117 THR A CG2 1 
ATOM   963  N N   . SER A 1 118 ? 5.940   3.102   47.159  1.00 34.90 ? 118 SER A N   1 
ATOM   964  C CA  . SER A 1 118 ? 5.124   2.752   48.311  1.00 32.27 ? 118 SER A CA  1 
ATOM   965  C C   . SER A 1 118 ? 4.357   1.467   48.052  1.00 36.17 ? 118 SER A C   1 
ATOM   966  O O   . SER A 1 118 ? 3.916   1.190   46.928  1.00 37.29 ? 118 SER A O   1 
ATOM   967  C CB  . SER A 1 118 ? 4.191   3.907   48.687  1.00 35.62 ? 118 SER A CB  1 
ATOM   968  O OG  . SER A 1 118 ? 3.149   4.035   47.758  1.00 42.39 ? 118 SER A OG  1 
ATOM   969  N N   . LYS A 1 119 ? 4.208   0.678   49.122  1.00 35.88 ? 119 LYS A N   1 
ATOM   970  C CA  . LYS A 1 119 ? 3.523   -0.615  49.040  1.00 37.84 ? 119 LYS A CA  1 
ATOM   971  C C   . LYS A 1 119 ? 2.110   -0.487  48.485  1.00 40.89 ? 119 LYS A C   1 
ATOM   972  O O   . LYS A 1 119 ? 1.630   -1.383  47.774  1.00 44.93 ? 119 LYS A O   1 
ATOM   973  C CB  . LYS A 1 119 ? 3.495   -1.246  50.424  1.00 39.26 ? 119 LYS A CB  1 
ATOM   974  C CG  . LYS A 1 119 ? 2.780   -2.618  50.493  1.00 45.62 ? 119 LYS A CG  1 
ATOM   975  C CD  . LYS A 1 119 ? 2.970   -3.281  51.867  1.00 47.13 ? 119 LYS A CD  1 
ATOM   976  C CE  . LYS A 1 119 ? 1.907   -4.358  52.118  1.00 47.80 ? 119 LYS A CE  1 
ATOM   977  N NZ  . LYS A 1 119 ? 2.410   -5.407  53.068  1.00 56.98 ? 119 LYS A NZ  1 
ATOM   978  N N   . GLY A 1 120 ? 1.467   0.619   48.815  1.00 42.50 ? 120 GLY A N   1 
ATOM   979  C CA  . GLY A 1 120 ? 0.099   0.869   48.354  1.00 46.32 ? 120 GLY A CA  1 
ATOM   980  C C   . GLY A 1 120 ? 0.002   1.169   46.876  1.00 50.14 ? 120 GLY A C   1 
ATOM   981  O O   . GLY A 1 120 ? -0.708  0.442   46.187  1.00 53.47 ? 120 GLY A O   1 
ATOM   982  N N   . SER A 1 121 ? 0.711   2.178   46.385  1.00 46.97 ? 121 SER A N   1 
ATOM   983  C CA  . SER A 1 121 ? 0.476   2.555   44.970  1.00 45.91 ? 121 SER A CA  1 
ATOM   984  C C   . SER A 1 121 ? 1.666   2.308   44.038  1.00 45.73 ? 121 SER A C   1 
ATOM   985  O O   . SER A 1 121 ? 1.563   2.693   42.880  1.00 41.66 ? 121 SER A O   1 
ATOM   986  C CB  . SER A 1 121 ? 0.150   3.975   44.940  1.00 43.89 ? 121 SER A CB  1 
ATOM   987  O OG  . SER A 1 121 ? 1.277   4.683   45.386  1.00 55.22 ? 121 SER A OG  1 
ATOM   988  N N   . GLY A 1 122 ? 2.742   1.686   44.490  1.00 40.34 ? 122 GLY A N   1 
ATOM   989  C CA  . GLY A 1 122 ? 3.845   1.541   43.526  1.00 35.96 ? 122 GLY A CA  1 
ATOM   990  C C   . GLY A 1 122 ? 4.528   2.872   43.293  1.00 32.04 ? 122 GLY A C   1 
ATOM   991  O O   . GLY A 1 122 ? 4.898   3.494   44.253  1.00 30.53 ? 122 GLY A O   1 
ATOM   992  N N   . THR A 1 123 ? 4.879   3.198   42.046  1.00 28.48 ? 123 THR A N   1 
ATOM   993  C CA  . THR A 1 123 ? 5.561   4.448   41.700  1.00 27.90 ? 123 THR A CA  1 
ATOM   994  C C   . THR A 1 123 ? 4.988   4.981   40.396  1.00 28.43 ? 123 THR A C   1 
ATOM   995  O O   . THR A 1 123 ? 4.775   4.219   39.447  1.00 29.16 ? 123 THR A O   1 
ATOM   996  C CB  . THR A 1 123 ? 7.095   4.335   41.501  1.00 34.56 ? 123 THR A CB  1 
ATOM   997  O OG1 . THR A 1 123 ? 7.332   4.006   40.140  1.00 36.00 ? 123 THR A OG1 1 
ATOM   998  C CG2 . THR A 1 123 ? 7.675   3.238   42.333  1.00 25.50 ? 123 THR A CG2 1 
ATOM   999  N N   . SER A 1 124 ? 4.733   6.267   40.345  1.00 29.36 ? 124 SER A N   1 
ATOM   1000 C CA  . SER A 1 124 ? 4.197   6.839   39.118  1.00 28.46 ? 124 SER A CA  1 
ATOM   1001 C C   . SER A 1 124 ? 5.319   7.298   38.209  1.00 27.32 ? 124 SER A C   1 
ATOM   1002 O O   . SER A 1 124 ? 6.443   7.491   38.652  1.00 27.21 ? 124 SER A O   1 
ATOM   1003 C CB  . SER A 1 124 ? 3.305   8.034   39.450  1.00 27.14 ? 124 SER A CB  1 
ATOM   1004 O OG  . SER A 1 124 ? 4.152   9.135   39.810  1.00 27.71 ? 124 SER A OG  1 
ATOM   1005 N N   . PRO A 1 125 ? 5.028   7.527   36.927  1.00 29.21 ? 125 PRO A N   1 
ATOM   1006 C CA  . PRO A 1 125 ? 6.035   8.137   36.069  1.00 28.11 ? 125 PRO A CA  1 
ATOM   1007 C C   . PRO A 1 125 ? 6.487   9.505   36.538  1.00 29.06 ? 125 PRO A C   1 
ATOM   1008 O O   . PRO A 1 125 ? 7.672   9.828   36.370  1.00 29.96 ? 125 PRO A O   1 
ATOM   1009 C CB  . PRO A 1 125 ? 5.363   8.179   34.691  1.00 31.19 ? 125 PRO A CB  1 
ATOM   1010 C CG  . PRO A 1 125 ? 3.986   7.783   34.900  1.00 31.44 ? 125 PRO A CG  1 
ATOM   1011 C CD  . PRO A 1 125 ? 3.891   6.998   36.151  1.00 28.65 ? 125 PRO A CD  1 
ATOM   1012 N N   . ALA A 1 126 ? 5.591   10.325  37.105  1.00 28.97 ? 126 ALA A N   1 
ATOM   1013 C CA  . ALA A 1 126 ? 6.023   11.632  37.616  1.00 29.08 ? 126 ALA A CA  1 
ATOM   1014 C C   . ALA A 1 126 ? 6.996   11.488  38.785  1.00 30.06 ? 126 ALA A C   1 
ATOM   1015 O O   . ALA A 1 126 ? 7.921   12.296  38.936  1.00 30.38 ? 126 ALA A O   1 
ATOM   1016 C CB  . ALA A 1 126 ? 4.810   12.464  38.054  1.00 31.63 ? 126 ALA A CB  1 
ATOM   1017 N N   . GLN A 1 127 ? 6.788   10.483  39.633  1.00 27.92 ? 127 GLN A N   1 
ATOM   1018 C CA  . GLN A 1 127 ? 7.713   10.238  40.726  1.00 28.47 ? 127 GLN A CA  1 
ATOM   1019 C C   . GLN A 1 127 ? 9.080   9.815   40.178  1.00 28.52 ? 127 GLN A C   1 
ATOM   1020 O O   . GLN A 1 127 ? 10.109  10.203  40.726  1.00 26.73 ? 127 GLN A O   1 
ATOM   1021 C CB  . GLN A 1 127 ? 7.169   9.162   41.654  1.00 28.51 ? 127 GLN A CB  1 
ATOM   1022 C CG  . GLN A 1 127 ? 6.079   9.597   42.601  1.00 28.84 ? 127 GLN A CG  1 
ATOM   1023 C CD  . GLN A 1 127 ? 5.579   8.428   43.397  1.00 29.31 ? 127 GLN A CD  1 
ATOM   1024 O OE1 . GLN A 1 127 ? 5.075   7.438   42.842  1.00 26.77 ? 127 GLN A OE1 1 
ATOM   1025 N NE2 . GLN A 1 127 ? 5.757   8.499   44.704  1.00 32.13 ? 127 GLN A NE2 1 
ATOM   1026 N N   . LEU A 1 128 ? 9.085   9.011   39.105  1.00 26.35 ? 128 LEU A N   1 
ATOM   1027 C CA  . LEU A 1 128 ? 10.325  8.602   38.463  1.00 31.40 ? 128 LEU A CA  1 
ATOM   1028 C C   . LEU A 1 128 ? 11.088  9.806   37.919  1.00 29.12 ? 128 LEU A C   1 
ATOM   1029 O O   . LEU A 1 128 ? 12.300  9.954   38.150  1.00 29.35 ? 128 LEU A O   1 
ATOM   1030 C CB  . LEU A 1 128 ? 10.025  7.616   37.327  1.00 27.02 ? 128 LEU A CB  1 
ATOM   1031 C CG  . LEU A 1 128 ? 11.262  7.351   36.449  1.00 29.52 ? 128 LEU A CG  1 
ATOM   1032 C CD1 . LEU A 1 128 ? 12.329  6.676   37.276  1.00 26.63 ? 128 LEU A CD1 1 
ATOM   1033 C CD2 . LEU A 1 128 ? 10.915  6.488   35.199  1.00 28.38 ? 128 LEU A CD2 1 
ATOM   1034 N N   . ILE A 1 129 ? 10.396  10.670  37.174  1.00 29.30 ? 129 ILE A N   1 
ATOM   1035 C CA  . ILE A 1 129 ? 11.061  11.809  36.540  1.00 29.26 ? 129 ILE A CA  1 
ATOM   1036 C C   . ILE A 1 129 ? 11.575  12.784  37.587  1.00 28.84 ? 129 ILE A C   1 
ATOM   1037 O O   . ILE A 1 129 ? 12.712  13.268  37.489  1.00 27.72 ? 129 ILE A O   1 
ATOM   1038 C CB  . ILE A 1 129 ? 10.112  12.499  35.546  1.00 31.51 ? 129 ILE A CB  1 
ATOM   1039 C CG1 . ILE A 1 129 ? 9.936   11.603  34.311  1.00 32.78 ? 129 ILE A CG1 1 
ATOM   1040 C CG2 . ILE A 1 129 ? 10.677  13.861  35.113  1.00 30.51 ? 129 ILE A CG2 1 
ATOM   1041 C CD1 . ILE A 1 129 ? 8.733   12.001  33.455  1.00 34.02 ? 129 ILE A CD1 1 
ATOM   1042 N N   . ALA A 1 130 ? 10.764  13.058  38.621  1.00 29.07 ? 130 ALA A N   1 
ATOM   1043 C CA  . ALA A 1 130 ? 11.098  14.101  39.589  1.00 29.50 ? 130 ALA A CA  1 
ATOM   1044 C C   . ALA A 1 130 ? 12.210  13.685  40.546  1.00 31.17 ? 130 ALA A C   1 
ATOM   1045 O O   . ALA A 1 130 ? 12.935  14.556  41.032  1.00 30.59 ? 130 ALA A O   1 
ATOM   1046 C CB  . ALA A 1 130 ? 9.878   14.480  40.410  1.00 28.56 ? 130 ALA A CB  1 
ATOM   1047 N N   . ASN A 1 131 ? 12.345  12.382  40.853  1.00 26.41 ? 131 ASN A N   1 
ATOM   1048 C CA  . ASN A 1 131 ? 13.285  11.951  41.877  1.00 28.86 ? 131 ASN A CA  1 
ATOM   1049 C C   . ASN A 1 131 ? 14.529  11.229  41.357  1.00 29.02 ? 131 ASN A C   1 
ATOM   1050 O O   . ASN A 1 131 ? 15.483  11.015  42.128  1.00 26.51 ? 131 ASN A O   1 
ATOM   1051 C CB  . ASN A 1 131 ? 12.565  11.060  42.879  1.00 30.11 ? 131 ASN A CB  1 
ATOM   1052 C CG  . ASN A 1 131 ? 11.593  11.848  43.707  1.00 33.50 ? 131 ASN A CG  1 
ATOM   1053 O OD1 . ASN A 1 131 ? 12.016  12.705  44.463  1.00 35.60 ? 131 ASN A OD1 1 
ATOM   1054 N ND2 . ASN A 1 131 ? 10.308  11.575  43.567  1.00 28.45 ? 131 ASN A ND2 1 
ATOM   1055 N N   . ALA A 1 132 ? 14.549  10.827  40.096  1.00 26.57 ? 132 ALA A N   1 
ATOM   1056 C CA  . ALA A 1 132 ? 15.753  10.191  39.568  1.00 26.22 ? 132 ALA A CA  1 
ATOM   1057 C C   . ALA A 1 132 ? 17.010  11.042  39.707  1.00 29.08 ? 132 ALA A C   1 
ATOM   1058 O O   . ALA A 1 132 ? 18.094  10.444  39.866  1.00 26.50 ? 132 ALA A O   1 
ATOM   1059 C CB  . ALA A 1 132 ? 15.544  9.800   38.106  1.00 28.06 ? 132 ALA A CB  1 
ATOM   1060 N N   . PRO A 1 133 ? 16.961  12.386  39.642  1.00 27.60 ? 133 PRO A N   1 
ATOM   1061 C CA  . PRO A 1 133 ? 18.202  13.171  39.844  1.00 28.29 ? 133 PRO A CA  1 
ATOM   1062 C C   . PRO A 1 133 ? 18.810  12.996  41.205  1.00 26.92 ? 133 PRO A C   1 
ATOM   1063 O O   . PRO A 1 133 ? 19.981  13.332  41.384  1.00 30.53 ? 133 PRO A O   1 
ATOM   1064 C CB  . PRO A 1 133 ? 17.760  14.626  39.611  1.00 29.60 ? 133 PRO A CB  1 
ATOM   1065 C CG  . PRO A 1 133 ? 16.547  14.544  38.785  1.00 31.49 ? 133 PRO A CG  1 
ATOM   1066 C CD  . PRO A 1 133 ? 15.920  13.194  38.974  1.00 28.28 ? 133 PRO A CD  1 
ATOM   1067 N N   . LYS A 1 134 ? 18.050  12.562  42.203  1.00 28.06 ? 134 LYS A N   1 
ATOM   1068 C CA  . LYS A 1 134 ? 18.674  12.277  43.492  1.00 27.18 ? 134 LYS A CA  1 
ATOM   1069 C C   . LYS A 1 134 ? 19.766  11.215  43.361  1.00 32.31 ? 134 LYS A C   1 
ATOM   1070 O O   . LYS A 1 134 ? 20.738  11.240  44.122  1.00 29.26 ? 134 LYS A O   1 
ATOM   1071 C CB  . LYS A 1 134 ? 17.628  11.785  44.490  1.00 29.20 ? 134 LYS A CB  1 
ATOM   1072 C CG  . LYS A 1 134 ? 16.735  12.861  45.033  1.00 31.18 ? 134 LYS A CG  1 
ATOM   1073 C CD  . LYS A 1 134 ? 15.706  12.242  45.927  1.00 32.66 ? 134 LYS A CD  1 
ATOM   1074 C CE  . LYS A 1 134 ? 14.764  13.311  46.483  1.00 38.98 ? 134 LYS A CE  1 
ATOM   1075 N NZ  . LYS A 1 134 ? 13.624  12.546  47.010  1.00 38.93 ? 134 LYS A NZ  1 
ATOM   1076 N N   . LEU A 1 135 ? 19.631  10.286  42.400  1.00 29.88 ? 135 LEU A N   1 
ATOM   1077 C CA  . LEU A 1 135 ? 20.565  9.175   42.213  1.00 28.49 ? 135 LEU A CA  1 
ATOM   1078 C C   . LEU A 1 135 ? 21.608  9.469   41.138  1.00 30.11 ? 135 LEU A C   1 
ATOM   1079 O O   . LEU A 1 135 ? 22.456  8.609   40.852  1.00 29.43 ? 135 LEU A O   1 
ATOM   1080 C CB  . LEU A 1 135 ? 19.788  7.899   41.845  1.00 27.75 ? 135 LEU A CB  1 
ATOM   1081 C CG  . LEU A 1 135 ? 18.634  7.476   42.788  1.00 27.77 ? 135 LEU A CG  1 
ATOM   1082 C CD1 . LEU A 1 135 ? 17.696  6.570   42.042  1.00 30.02 ? 135 LEU A CD1 1 
ATOM   1083 C CD2 . LEU A 1 135 ? 19.129  6.737   43.992  1.00 29.58 ? 135 LEU A CD2 1 
ATOM   1084 N N   . GLY A 1 136 ? 21.560  10.665  40.543  1.00 29.59 ? 136 GLY A N   1 
ATOM   1085 C CA  . GLY A 1 136 ? 22.437  11.088  39.487  1.00 27.14 ? 136 GLY A CA  1 
ATOM   1086 C C   . GLY A 1 136 ? 21.907  10.951  38.080  1.00 28.68 ? 136 GLY A C   1 
ATOM   1087 O O   . GLY A 1 136 ? 22.692  11.102  37.130  1.00 28.47 ? 136 GLY A O   1 
ATOM   1088 N N   . PHE A 1 137 ? 20.614  10.707  37.904  1.00 26.25 ? 137 PHE A N   1 
ATOM   1089 C CA  . PHE A 1 137 ? 20.063  10.462  36.585  1.00 25.60 ? 137 PHE A CA  1 
ATOM   1090 C C   . PHE A 1 137 ? 19.113  11.566  36.130  1.00 30.62 ? 137 PHE A C   1 
ATOM   1091 O O   . PHE A 1 137 ? 18.500  12.262  36.932  1.00 31.52 ? 137 PHE A O   1 
ATOM   1092 C CB  . PHE A 1 137 ? 19.317  9.131   36.572  1.00 26.75 ? 137 PHE A CB  1 
ATOM   1093 C CG  . PHE A 1 137 ? 20.196  7.968   36.901  1.00 22.93 ? 137 PHE A CG  1 
ATOM   1094 C CD1 . PHE A 1 137 ? 21.315  7.734   36.155  1.00 24.22 ? 137 PHE A CD1 1 
ATOM   1095 C CD2 . PHE A 1 137 ? 19.940  7.178   38.009  1.00 24.02 ? 137 PHE A CD2 1 
ATOM   1096 C CE1 . PHE A 1 137 ? 22.167  6.672   36.459  1.00 26.81 ? 137 PHE A CE1 1 
ATOM   1097 C CE2 . PHE A 1 137 ? 20.794  6.115   38.321  1.00 26.13 ? 137 PHE A CE2 1 
ATOM   1098 C CZ  . PHE A 1 137 ? 21.882  5.862   37.548  1.00 22.88 ? 137 PHE A CZ  1 
ATOM   1099 N N   . LYS A 1 138 ? 18.951  11.659  34.812  1.00 30.60 ? 138 LYS A N   1 
ATOM   1100 C CA  . LYS A 1 138 ? 17.928  12.483  34.190  1.00 32.23 ? 138 LYS A CA  1 
ATOM   1101 C C   . LYS A 1 138 ? 17.033  11.579  33.356  1.00 32.40 ? 138 LYS A C   1 
ATOM   1102 O O   . LYS A 1 138 ? 17.533  10.732  32.610  1.00 30.78 ? 138 LYS A O   1 
ATOM   1103 C CB  . LYS A 1 138 ? 18.575  13.536  33.304  1.00 32.24 ? 138 LYS A CB  1 
ATOM   1104 C CG  . LYS A 1 138 ? 17.656  14.160  32.288  1.00 34.25 ? 138 LYS A CG  1 
ATOM   1105 C CD  . LYS A 1 138 ? 17.827  15.656  32.355  1.00 43.56 ? 138 LYS A CD  1 
ATOM   1106 C CE  . LYS A 1 138 ? 18.934  16.110  31.410  1.00 42.94 ? 138 LYS A CE  1 
ATOM   1107 N NZ  . LYS A 1 138 ? 18.755  17.565  31.046  1.00 50.16 ? 138 LYS A NZ  1 
ATOM   1108 N N   . ILE A 1 139 ? 15.718  11.758  33.488  1.00 27.24 ? 139 ILE A N   1 
ATOM   1109 C CA  . ILE A 1 139 ? 14.739  11.009  32.715  1.00 29.11 ? 139 ILE A CA  1 
ATOM   1110 C C   . ILE A 1 139 ? 14.210  11.908  31.603  1.00 33.17 ? 139 ILE A C   1 
ATOM   1111 O O   . ILE A 1 139 ? 13.711  13.002  31.875  1.00 34.06 ? 139 ILE A O   1 
ATOM   1112 C CB  . ILE A 1 139 ? 13.581  10.528  33.612  1.00 30.42 ? 139 ILE A CB  1 
ATOM   1113 C CG1 . ILE A 1 139 ? 14.100  9.817   34.864  1.00 30.15 ? 139 ILE A CG1 1 
ATOM   1114 C CG2 . ILE A 1 139 ? 12.602  9.651   32.825  1.00 29.00 ? 139 ILE A CG2 1 
ATOM   1115 C CD1 . ILE A 1 139 ? 15.003  8.630   34.586  1.00 31.76 ? 139 ILE A CD1 1 
ATOM   1116 N N   . ILE A 1 140 ? 14.253  11.428  30.367  1.00 31.88 ? 140 ILE A N   1 
ATOM   1117 C CA  . ILE A 1 140 ? 13.712  12.160  29.223  1.00 33.73 ? 140 ILE A CA  1 
ATOM   1118 C C   . ILE A 1 140 ? 12.436  11.457  28.761  1.00 35.14 ? 140 ILE A C   1 
ATOM   1119 O O   . ILE A 1 140 ? 12.532  10.402  28.116  1.00 34.57 ? 140 ILE A O   1 
ATOM   1120 C CB  . ILE A 1 140 ? 14.749  12.211  28.087  1.00 32.56 ? 140 ILE A CB  1 
ATOM   1121 C CG1 . ILE A 1 140 ? 16.134  12.607  28.647  1.00 35.00 ? 140 ILE A CG1 1 
ATOM   1122 C CG2 . ILE A 1 140 ? 14.286  13.161  26.962  1.00 36.44 ? 140 ILE A CG2 1 
ATOM   1123 C CD1 . ILE A 1 140 ? 17.149  13.032  27.594  1.00 36.19 ? 140 ILE A CD1 1 
ATOM   1124 N N   . PRO A 1 141 ? 11.236  11.972  29.068  1.00 36.12 ? 141 PRO A N   1 
ATOM   1125 C CA  . PRO A 1 141 ? 10.014  11.342  28.543  1.00 35.68 ? 141 PRO A CA  1 
ATOM   1126 C C   . PRO A 1 141 ? 9.971   11.441  27.025  1.00 37.39 ? 141 PRO A C   1 
ATOM   1127 O O   . PRO A 1 141 ? 10.062  12.518  26.446  1.00 40.71 ? 141 PRO A O   1 
ATOM   1128 C CB  . PRO A 1 141 ? 8.883   12.141  29.210  1.00 35.53 ? 141 PRO A CB  1 
ATOM   1129 C CG  . PRO A 1 141 ? 9.515   13.362  29.738  1.00 36.54 ? 141 PRO A CG  1 
ATOM   1130 C CD  . PRO A 1 141 ? 10.922  13.037  30.041  1.00 34.39 ? 141 PRO A CD  1 
ATOM   1131 N N   . ILE A 1 142 ? 9.793   10.298  26.379  1.00 36.70 ? 142 ILE A N   1 
ATOM   1132 C CA  . ILE A 1 142 ? 9.932   10.182  24.932  1.00 38.22 ? 142 ILE A CA  1 
ATOM   1133 C C   . ILE A 1 142 ? 8.671   9.528   24.379  1.00 36.21 ? 142 ILE A C   1 
ATOM   1134 O O   . ILE A 1 142 ? 7.862   8.985   25.126  1.00 34.62 ? 142 ILE A O   1 
ATOM   1135 C CB  . ILE A 1 142 ? 11.221  9.408   24.576  1.00 37.07 ? 142 ILE A CB  1 
ATOM   1136 C CG1 . ILE A 1 142 ? 11.624  9.570   23.133  1.00 39.34 ? 142 ILE A CG1 1 
ATOM   1137 C CG2 . ILE A 1 142 ? 11.124  7.890   24.906  1.00 35.25 ? 142 ILE A CG2 1 
ATOM   1138 C CD1 . ILE A 1 142 ? 12.774  8.639   22.855  1.00 45.87 ? 142 ILE A CD1 1 
ATOM   1139 N N   . LYS A 1 143 ? 8.462   9.654   23.064  1.00 37.76 ? 143 LYS A N   1 
ATOM   1140 C CA  . LYS A 1 143 ? 7.279   9.031   22.462  1.00 41.10 ? 143 LYS A CA  1 
ATOM   1141 C C   . LYS A 1 143 ? 7.407   7.507   22.415  1.00 37.54 ? 143 LYS A C   1 
ATOM   1142 O O   . LYS A 1 143 ? 8.489   6.954   22.200  1.00 41.60 ? 143 LYS A O   1 
ATOM   1143 C CB  . LYS A 1 143 ? 7.057   9.568   21.042  1.00 43.13 ? 143 LYS A CB  1 
ATOM   1144 C CG  . LYS A 1 143 ? 7.358   11.072  20.872  1.00 48.21 ? 143 LYS A CG  1 
ATOM   1145 C CD  . LYS A 1 143 ? 7.061   11.578  19.461  1.00 49.57 ? 143 LYS A CD  1 
ATOM   1146 C CE  . LYS A 1 143 ? 8.351   11.823  18.648  1.00 50.85 ? 143 LYS A CE  1 
ATOM   1147 N NZ  . LYS A 1 143 ? 9.249   12.875  19.232  1.00 53.59 ? 143 LYS A NZ  1 
ATOM   1148 N N   . ARG A 1 144 ? 6.270   6.830   22.528  1.00 38.04 ? 144 ARG A N   1 
ATOM   1149 C CA  . ARG A 1 144 ? 6.208   5.368   22.435  1.00 37.92 ? 144 ARG A CA  1 
ATOM   1150 C C   . ARG A 1 144 ? 6.385   4.952   20.976  1.00 38.87 ? 144 ARG A C   1 
ATOM   1151 O O   . ARG A 1 144 ? 5.431   4.609   20.285  1.00 37.14 ? 144 ARG A O   1 
ATOM   1152 C CB  . ARG A 1 144 ? 4.894   4.854   23.022  1.00 36.65 ? 144 ARG A CB  1 
ATOM   1153 C CG  . ARG A 1 144 ? 4.682   5.253   24.466  1.00 34.94 ? 144 ARG A CG  1 
ATOM   1154 C CD  . ARG A 1 144 ? 3.400   4.734   24.997  1.00 35.53 ? 144 ARG A CD  1 
ATOM   1155 N NE  . ARG A 1 144 ? 3.415   3.276   25.228  1.00 34.28 ? 144 ARG A NE  1 
ATOM   1156 C CZ  . ARG A 1 144 ? 3.629   2.675   26.407  1.00 32.61 ? 144 ARG A CZ  1 
ATOM   1157 N NH1 . ARG A 1 144 ? 3.929   3.359   27.511  1.00 29.20 ? 144 ARG A NH1 1 
ATOM   1158 N NH2 . ARG A 1 144 ? 3.487   1.356   26.496  1.00 32.66 ? 144 ARG A NH2 1 
ATOM   1159 N N   . ASP A 1 145 ? 7.608   5.109   20.488  1.00 42.31 ? 145 ASP A N   1 
ATOM   1160 C CA  . ASP A 1 145 ? 7.904   4.823   19.064  1.00 41.69 ? 145 ASP A CA  1 
ATOM   1161 C C   . ASP A 1 145 ? 9.303   4.242   18.958  1.00 42.80 ? 145 ASP A C   1 
ATOM   1162 O O   . ASP A 1 145 ? 10.227  4.853   19.444  1.00 41.23 ? 145 ASP A O   1 
ATOM   1163 C CB  . ASP A 1 145 ? 7.673   6.081   18.221  1.00 47.17 ? 145 ASP A CB  1 
ATOM   1164 C CG  . ASP A 1 145 ? 8.527   6.254   16.985  1.00 49.72 ? 145 ASP A CG  1 
ATOM   1165 O OD1 . ASP A 1 145 ? 9.108   5.299   16.515  1.00 49.56 ? 145 ASP A OD1 1 
ATOM   1166 O OD2 . ASP A 1 145 ? 8.573   7.359   16.499  1.00 55.81 ? 145 ASP A OD2 1 
ATOM   1167 N N   . SER A 1 146 ? 9.432   3.182   18.176  1.00 44.16 ? 146 SER A N   1 
ATOM   1168 C CA  . SER A 1 146 ? 10.716  2.463   18.013  1.00 43.12 ? 146 SER A CA  1 
ATOM   1169 C C   . SER A 1 146 ? 11.806  3.385   17.477  1.00 44.49 ? 146 SER A C   1 
ATOM   1170 O O   . SER A 1 146 ? 12.929  3.203   17.887  1.00 45.82 ? 146 SER A O   1 
ATOM   1171 C CB  . SER A 1 146 ? 10.560  1.223   17.187  1.00 39.92 ? 146 SER A CB  1 
ATOM   1172 O OG  . SER A 1 146 ? 9.775   1.474   16.057  1.00 42.61 ? 146 SER A OG  1 
ATOM   1173 N N   . LYS A 1 147 ? 11.438  4.324   16.612  1.00 48.60 ? 147 LYS A N   1 
ATOM   1174 C CA  . LYS A 1 147 ? 12.417  5.274   16.028  1.00 47.26 ? 147 LYS A CA  1 
ATOM   1175 C C   . LYS A 1 147 ? 13.096  6.020   17.180  1.00 44.66 ? 147 LYS A C   1 
ATOM   1176 O O   . LYS A 1 147 ? 14.311  6.094   17.202  1.00 44.69 ? 147 LYS A O   1 
ATOM   1177 C CB  . LYS A 1 147 ? 11.687  6.232   15.079  1.00 50.73 ? 147 LYS A CB  1 
ATOM   1178 C CG  . LYS A 1 147 ? 12.154  6.249   13.631  1.00 55.57 ? 147 LYS A CG  1 
ATOM   1179 C CD  . LYS A 1 147 ? 11.280  5.498   12.644  1.00 58.10 ? 147 LYS A CD  1 
ATOM   1180 C CE  . LYS A 1 147 ? 11.367  6.082   11.248  1.00 60.81 ? 147 LYS A CE  1 
ATOM   1181 N NZ  . LYS A 1 147 ? 11.510  5.061   10.181  1.00 62.93 ? 147 LYS A NZ  1 
ATOM   1182 N N   . GLU A 1 148 ? 12.305  6.531   18.106  1.00 42.25 ? 148 GLU A N   1 
ATOM   1183 C CA  . GLU A 1 148 ? 12.849  7.275   19.262  1.00 39.54 ? 148 GLU A CA  1 
ATOM   1184 C C   . GLU A 1 148 ? 13.666  6.326   20.144  1.00 40.40 ? 148 GLU A C   1 
ATOM   1185 O O   . GLU A 1 148 ? 14.779  6.665   20.474  1.00 40.79 ? 148 GLU A O   1 
ATOM   1186 C CB  . GLU A 1 148 ? 11.720  7.984   20.001  1.00 43.43 ? 148 GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 148 ? 11.178  9.182   19.250  1.00 47.35 ? 148 GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 148 ? 12.261  10.181  18.903  1.00 48.99 ? 148 GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 148 ? 12.673  10.937  19.783  1.00 46.32 ? 148 GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 148 ? 12.699  10.172  17.766  1.00 51.26 ? 148 GLU A OE2 1 
ATOM   1191 N N   . VAL A 1 149 ? 13.121  5.165   20.481  1.00 40.04 ? 149 VAL A N   1 
ATOM   1192 C CA  . VAL A 1 149 ? 13.843  4.208   21.324  1.00 36.56 ? 149 VAL A CA  1 
ATOM   1193 C C   . VAL A 1 149 ? 15.225  3.876   20.749  1.00 39.76 ? 149 VAL A C   1 
ATOM   1194 O O   . VAL A 1 149 ? 16.215  3.801   21.488  1.00 38.17 ? 149 VAL A O   1 
ATOM   1195 C CB  . VAL A 1 149 ? 12.997  2.932   21.508  1.00 37.21 ? 149 VAL A CB  1 
ATOM   1196 C CG1 . VAL A 1 149 ? 13.774  1.865   22.296  1.00 34.13 ? 149 VAL A CG1 1 
ATOM   1197 C CG2 . VAL A 1 149 ? 11.622  3.237   22.144  1.00 35.37 ? 149 VAL A CG2 1 
ATOM   1198 N N   . LYS A 1 150 ? 15.310  3.617   19.441  1.00 37.29 ? 150 LYS A N   1 
ATOM   1199 C CA  . LYS A 1 150 ? 16.595  3.295   18.830  1.00 41.96 ? 150 LYS A CA  1 
ATOM   1200 C C   . LYS A 1 150 ? 17.566  4.469   18.932  1.00 40.50 ? 150 LYS A C   1 
ATOM   1201 O O   . LYS A 1 150 ? 18.770  4.277   19.141  1.00 41.24 ? 150 LYS A O   1 
ATOM   1202 C CB  . LYS A 1 150 ? 16.396  2.890   17.367  1.00 43.63 ? 150 LYS A CB  1 
ATOM   1203 C CG  . LYS A 1 150 ? 17.586  2.152   16.784  1.00 45.98 ? 150 LYS A CG  1 
ATOM   1204 C CD  . LYS A 1 150 ? 17.501  1.959   15.268  1.00 48.14 ? 150 LYS A CD  1 
ATOM   1205 C CE  . LYS A 1 150 ? 16.607  0.790   14.889  1.00 49.46 ? 150 LYS A CE  1 
ATOM   1206 N NZ  . LYS A 1 150 ? 15.985  0.948   13.526  1.00 56.81 ? 150 LYS A NZ  1 
ATOM   1207 N N   . LYS A 1 151 ? 17.053  5.698   18.817  1.00 44.31 ? 151 LYS A N   1 
ATOM   1208 C CA  . LYS A 1 151 ? 17.936  6.854   18.835  1.00 43.07 ? 151 LYS A CA  1 
ATOM   1209 C C   . LYS A 1 151 ? 18.710  6.934   20.145  1.00 40.56 ? 151 LYS A C   1 
ATOM   1210 O O   . LYS A 1 151 ? 19.917  7.189   20.145  1.00 45.75 ? 151 LYS A O   1 
ATOM   1211 C CB  . LYS A 1 151 ? 17.127  8.131   18.590  1.00 43.77 ? 151 LYS A CB  1 
ATOM   1212 C CG  . LYS A 1 151 ? 17.734  9.392   19.206  1.00 43.89 ? 151 LYS A CG  1 
ATOM   1213 C CD  . LYS A 1 151 ? 16.768  10.594  19.105  1.00 44.06 ? 151 LYS A CD  1 
ATOM   1214 C CE  . LYS A 1 151 ? 17.359  11.841  19.771  1.00 47.60 ? 151 LYS A CE  1 
ATOM   1215 N NZ  . LYS A 1 151 ? 17.353  13.060  18.922  1.00 49.12 ? 151 LYS A NZ  1 
ATOM   1216 N N   . TYR A 1 152 ? 18.044  6.684   21.265  1.00 39.10 ? 152 TYR A N   1 
ATOM   1217 C CA  . TYR A 1 152 ? 18.681  6.835   22.568  1.00 39.67 ? 152 TYR A CA  1 
ATOM   1218 C C   . TYR A 1 152 ? 19.470  5.602   22.980  1.00 38.04 ? 152 TYR A C   1 
ATOM   1219 O O   . TYR A 1 152 ? 20.470  5.723   23.701  1.00 40.84 ? 152 TYR A O   1 
ATOM   1220 C CB  . TYR A 1 152 ? 17.621  7.204   23.607  1.00 41.66 ? 152 TYR A CB  1 
ATOM   1221 C CG  . TYR A 1 152 ? 17.212  8.648   23.492  1.00 39.68 ? 152 TYR A CG  1 
ATOM   1222 C CD1 . TYR A 1 152 ? 17.944  9.638   24.093  1.00 39.47 ? 152 TYR A CD1 1 
ATOM   1223 C CD2 . TYR A 1 152 ? 16.099  9.016   22.746  1.00 41.92 ? 152 TYR A CD2 1 
ATOM   1224 C CE1 . TYR A 1 152 ? 17.569  10.986  23.973  1.00 41.26 ? 152 TYR A CE1 1 
ATOM   1225 C CE2 . TYR A 1 152 ? 15.733  10.346  22.601  1.00 43.24 ? 152 TYR A CE2 1 
ATOM   1226 C CZ  . TYR A 1 152 ? 16.468  11.321  23.227  1.00 40.83 ? 152 TYR A CZ  1 
ATOM   1227 O OH  . TYR A 1 152 ? 16.090  12.637  23.103  1.00 42.78 ? 152 TYR A OH  1 
ATOM   1228 N N   . LEU A 1 153 ? 19.082  4.421   22.502  1.00 37.23 ? 153 LEU A N   1 
ATOM   1229 C CA  . LEU A 1 153 ? 19.920  3.244   22.705  1.00 38.34 ? 153 LEU A CA  1 
ATOM   1230 C C   . LEU A 1 153 ? 21.259  3.412   21.999  1.00 38.97 ? 153 LEU A C   1 
ATOM   1231 O O   . LEU A 1 153 ? 22.283  2.903   22.465  1.00 36.89 ? 153 LEU A O   1 
ATOM   1232 C CB  . LEU A 1 153 ? 19.210  1.986   22.210  1.00 35.72 ? 153 LEU A CB  1 
ATOM   1233 C CG  . LEU A 1 153 ? 18.057  1.457   23.066  1.00 36.06 ? 153 LEU A CG  1 
ATOM   1234 C CD1 . LEU A 1 153 ? 17.400  0.218   22.414  1.00 33.95 ? 153 LEU A CD1 1 
ATOM   1235 C CD2 . LEU A 1 153 ? 18.507  1.126   24.473  1.00 32.34 ? 153 LEU A CD2 1 
ATOM   1236 N N   . LYS A 1 154 ? 21.255  4.123   20.873  1.00 43.10 ? 154 LYS A N   1 
ATOM   1237 C CA  . LYS A 1 154 ? 22.484  4.418   20.143  1.00 44.19 ? 154 LYS A CA  1 
ATOM   1238 C C   . LYS A 1 154 ? 23.388  5.340   20.954  1.00 40.84 ? 154 LYS A C   1 
ATOM   1239 O O   . LYS A 1 154 ? 24.609  5.272   20.817  1.00 44.72 ? 154 LYS A O   1 
ATOM   1240 C CB  . LYS A 1 154 ? 22.140  5.040   18.778  1.00 44.32 ? 154 LYS A CB  1 
ATOM   1241 C CG  . LYS A 1 154 ? 23.252  5.031   17.749  1.00 48.79 ? 154 LYS A CG  1 
ATOM   1242 C CD  . LYS A 1 154 ? 23.585  6.459   17.292  1.00 48.00 ? 154 LYS A CD  1 
ATOM   1243 C CE  . LYS A 1 154 ? 23.902  6.534   15.796  1.00 51.02 ? 154 LYS A CE  1 
ATOM   1244 N NZ  . LYS A 1 154 ? 24.295  7.923   15.409  1.00 52.72 ? 154 LYS A NZ  1 
ATOM   1245 N N   . LYS A 1 155 ? 22.807  6.237   21.747  1.00 41.38 ? 155 LYS A N   1 
ATOM   1246 C CA  . LYS A 1 155 ? 23.567  7.108   22.637  1.00 41.57 ? 155 LYS A CA  1 
ATOM   1247 C C   . LYS A 1 155 ? 24.053  6.399   23.897  1.00 40.28 ? 155 LYS A C   1 
ATOM   1248 O O   . LYS A 1 155 ? 24.747  7.021   24.706  1.00 42.93 ? 155 LYS A O   1 
ATOM   1249 C CB  . LYS A 1 155 ? 22.743  8.340   23.014  1.00 41.91 ? 155 LYS A CB  1 
ATOM   1250 C CG  . LYS A 1 155 ? 21.866  8.869   21.875  1.00 44.22 ? 155 LYS A CG  1 
ATOM   1251 C CD  . LYS A 1 155 ? 20.949  9.997   22.316  1.00 46.04 ? 155 LYS A CD  1 
ATOM   1252 C CE  . LYS A 1 155 ? 21.559  11.360  22.117  1.00 46.43 ? 155 LYS A CE  1 
ATOM   1253 N NZ  . LYS A 1 155 ? 21.590  11.749  20.679  1.00 48.75 ? 155 LYS A NZ  1 
ATOM   1254 N N   . GLY A 1 156 ? 23.720  5.124   24.079  1.00 39.98 ? 156 GLY A N   1 
ATOM   1255 C CA  . GLY A 1 156 ? 24.071  4.379   25.280  1.00 38.78 ? 156 GLY A CA  1 
ATOM   1256 C C   . GLY A 1 156 ? 23.055  4.451   26.412  1.00 40.58 ? 156 GLY A C   1 
ATOM   1257 O O   . GLY A 1 156 ? 23.374  4.023   27.539  1.00 35.30 ? 156 GLY A O   1 
ATOM   1258 N N   . PHE A 1 157 ? 21.843  4.985   26.157  1.00 34.50 ? 157 PHE A N   1 
ATOM   1259 C CA  . PHE A 1 157 ? 20.862  5.271   27.203  1.00 34.13 ? 157 PHE A CA  1 
ATOM   1260 C C   . PHE A 1 157 ? 19.731  4.252   27.147  1.00 32.98 ? 157 PHE A C   1 
ATOM   1261 O O   . PHE A 1 157 ? 19.022  4.174   26.129  1.00 31.87 ? 157 PHE A O   1 
ATOM   1262 C CB  . PHE A 1 157 ? 20.294  6.687   27.041  1.00 35.55 ? 157 PHE A CB  1 
ATOM   1263 C CG  . PHE A 1 157 ? 21.343  7.802   27.128  1.00 35.23 ? 157 PHE A CG  1 
ATOM   1264 C CD1 . PHE A 1 157 ? 22.590  7.572   27.674  1.00 35.23 ? 157 PHE A CD1 1 
ATOM   1265 C CD2 . PHE A 1 157 ? 21.037  9.082   26.698  1.00 39.35 ? 157 PHE A CD2 1 
ATOM   1266 C CE1 . PHE A 1 157 ? 23.525  8.589   27.761  1.00 37.11 ? 157 PHE A CE1 1 
ATOM   1267 C CE2 . PHE A 1 157 ? 21.958  10.115  26.774  1.00 36.73 ? 157 PHE A CE2 1 
ATOM   1268 C CZ  . PHE A 1 157 ? 23.200  9.878   27.309  1.00 35.61 ? 157 PHE A CZ  1 
ATOM   1269 N N   . PRO A 1 158 ? 19.505  3.485   28.204  1.00 29.13 ? 158 PRO A N   1 
ATOM   1270 C CA  . PRO A 1 158 ? 18.419  2.508   28.198  1.00 29.52 ? 158 PRO A CA  1 
ATOM   1271 C C   . PRO A 1 158 ? 17.085  3.223   28.428  1.00 29.59 ? 158 PRO A C   1 
ATOM   1272 O O   . PRO A 1 158 ? 17.033  4.396   28.774  1.00 26.19 ? 158 PRO A O   1 
ATOM   1273 C CB  . PRO A 1 158 ? 18.815  1.580   29.354  1.00 27.00 ? 158 PRO A CB  1 
ATOM   1274 C CG  . PRO A 1 158 ? 19.491  2.514   30.328  1.00 26.55 ? 158 PRO A CG  1 
ATOM   1275 C CD  . PRO A 1 158 ? 20.304  3.429   29.447  1.00 30.41 ? 158 PRO A CD  1 
ATOM   1276 N N   . VAL A 1 159 ? 15.986  2.506   28.210  1.00 29.14 ? 159 VAL A N   1 
ATOM   1277 C CA  . VAL A 1 159 ? 14.673  3.164   28.182  1.00 26.59 ? 159 VAL A CA  1 
ATOM   1278 C C   . VAL A 1 159 ? 13.711  2.401   29.048  1.00 26.31 ? 159 VAL A C   1 
ATOM   1279 O O   . VAL A 1 159 ? 13.365  1.262   28.731  1.00 28.49 ? 159 VAL A O   1 
ATOM   1280 C CB  . VAL A 1 159 ? 14.112  3.285   26.760  1.00 29.45 ? 159 VAL A CB  1 
ATOM   1281 C CG1 . VAL A 1 159 ? 12.805  4.034   26.814  1.00 27.58 ? 159 VAL A CG1 1 
ATOM   1282 C CG2 . VAL A 1 159 ? 15.145  3.999   25.848  1.00 30.28 ? 159 VAL A CG2 1 
ATOM   1283 N N   . ILE A 1 160 ? 13.265  3.015   30.130  1.00 26.13 ? 160 ILE A N   1 
ATOM   1284 C CA  . ILE A 1 160 ? 12.242  2.392   30.952  1.00 26.59 ? 160 ILE A CA  1 
ATOM   1285 C C   . ILE A 1 160 ? 10.913  2.427   30.217  1.00 26.54 ? 160 ILE A C   1 
ATOM   1286 O O   . ILE A 1 160 ? 10.508  3.457   29.656  1.00 27.51 ? 160 ILE A O   1 
ATOM   1287 C CB  . ILE A 1 160 ? 12.170  3.073   32.328  1.00 24.95 ? 160 ILE A CB  1 
ATOM   1288 C CG1 . ILE A 1 160 ? 13.375  2.632   33.166  1.00 23.89 ? 160 ILE A CG1 1 
ATOM   1289 C CG2 . ILE A 1 160 ? 10.809  2.777   33.045  1.00 22.69 ? 160 ILE A CG2 1 
ATOM   1290 C CD1 . ILE A 1 160 ? 13.621  3.474   34.484  1.00 21.71 ? 160 ILE A CD1 1 
ATOM   1291 N N   . CYS A 1 161 ? 10.229  1.288   30.193  1.00 28.90 ? 161 CYS A N   1 
ATOM   1292 C CA  . CYS A 1 161 ? 8.918   1.217   29.567  1.00 25.91 ? 161 CYS A CA  1 
ATOM   1293 C C   . CYS A 1 161 ? 7.845   1.006   30.618  1.00 29.24 ? 161 CYS A C   1 
ATOM   1294 O O   . CYS A 1 161 ? 8.100   0.462   31.700  1.00 28.10 ? 161 CYS A O   1 
ATOM   1295 C CB  . CYS A 1 161 ? 8.860   0.113   28.510  1.00 28.79 ? 161 CYS A CB  1 
ATOM   1296 S SG  . CYS A 1 161 ? 9.294   -1.576  29.068  1.00 30.28 ? 161 CYS A SG  1 
ATOM   1297 N N   . HIS A 1 162 ? 6.629   1.444   30.284  1.00 27.94 ? 162 HIS A N   1 
ATOM   1298 C CA  . HIS A 1 162 ? 5.488   1.325   31.178  1.00 27.92 ? 162 HIS A CA  1 
ATOM   1299 C C   . HIS A 1 162 ? 4.294   0.822   30.370  1.00 27.55 ? 162 HIS A C   1 
ATOM   1300 O O   . HIS A 1 162 ? 4.011   1.350   29.286  1.00 28.77 ? 162 HIS A O   1 
ATOM   1301 C CB  . HIS A 1 162 ? 5.184   2.679   31.846  1.00 28.79 ? 162 HIS A CB  1 
ATOM   1302 C CG  . HIS A 1 162 ? 4.058   2.633   32.829  1.00 29.78 ? 162 HIS A CG  1 
ATOM   1303 N ND1 . HIS A 1 162 ? 2.981   3.495   32.773  1.00 34.36 ? 162 HIS A ND1 1 
ATOM   1304 C CD2 . HIS A 1 162 ? 3.851   1.853   33.916  1.00 29.96 ? 162 HIS A CD2 1 
ATOM   1305 C CE1 . HIS A 1 162 ? 2.154   3.237   33.773  1.00 32.41 ? 162 HIS A CE1 1 
ATOM   1306 N NE2 . HIS A 1 162 ? 2.657   2.244   34.480  1.00 33.48 ? 162 HIS A NE2 1 
ATOM   1307 N N   . TRP A 1 163 ? 3.597   -0.198  30.879  1.00 30.18 ? 163 TRP A N   1 
ATOM   1308 C CA  . TRP A 1 163 ? 2.446   -0.720  30.138  1.00 29.66 ? 163 TRP A CA  1 
ATOM   1309 C C   . TRP A 1 163 ? 1.483   -1.445  31.079  1.00 30.61 ? 163 TRP A C   1 
ATOM   1310 O O   . TRP A 1 163 ? 1.790   -1.708  32.239  1.00 30.99 ? 163 TRP A O   1 
ATOM   1311 C CB  . TRP A 1 163 ? 2.892   -1.615  28.968  1.00 30.83 ? 163 TRP A CB  1 
ATOM   1312 C CG  . TRP A 1 163 ? 3.298   -3.046  29.272  1.00 29.67 ? 163 TRP A CG  1 
ATOM   1313 C CD1 . TRP A 1 163 ? 2.593   -4.182  28.972  1.00 30.40 ? 163 TRP A CD1 1 
ATOM   1314 C CD2 . TRP A 1 163 ? 4.535   -3.482  29.857  1.00 27.55 ? 163 TRP A CD2 1 
ATOM   1315 N NE1 . TRP A 1 163 ? 3.325   -5.312  29.329  1.00 31.90 ? 163 TRP A NE1 1 
ATOM   1316 C CE2 . TRP A 1 163 ? 4.507   -4.905  29.897  1.00 31.51 ? 163 TRP A CE2 1 
ATOM   1317 C CE3 . TRP A 1 163 ? 5.658   -2.808  30.360  1.00 28.88 ? 163 TRP A CE3 1 
ATOM   1318 C CZ2 . TRP A 1 163 ? 5.572   -5.670  30.436  1.00 28.90 ? 163 TRP A CZ2 1 
ATOM   1319 C CZ3 . TRP A 1 163 ? 6.710   -3.558  30.883  1.00 26.69 ? 163 TRP A CZ3 1 
ATOM   1320 C CH2 . TRP A 1 163 ? 6.655   -4.979  30.924  1.00 28.32 ? 163 TRP A CH2 1 
ATOM   1321 N N   . GLN A 1 164 ? 0.281   -1.716  30.573  1.00 28.93 ? 164 GLN A N   1 
ATOM   1322 C CA  . GLN A 1 164 ? -0.733  -2.474  31.307  1.00 32.85 ? 164 GLN A CA  1 
ATOM   1323 C C   . GLN A 1 164 ? -0.718  -3.908  30.801  1.00 32.30 ? 164 GLN A C   1 
ATOM   1324 O O   . GLN A 1 164 ? -0.935  -4.144  29.604  1.00 32.20 ? 164 GLN A O   1 
ATOM   1325 C CB  . GLN A 1 164 ? -2.128  -1.855  31.150  1.00 32.95 ? 164 GLN A CB  1 
ATOM   1326 C CG  . GLN A 1 164 ? -2.164  -0.350  31.333  1.00 31.83 ? 164 GLN A CG  1 
ATOM   1327 C CD  . GLN A 1 164 ? -1.849  0.058   32.766  1.00 31.91 ? 164 GLN A CD  1 
ATOM   1328 O OE1 . GLN A 1 164 ? -2.387  -0.509  33.698  1.00 34.54 ? 164 GLN A OE1 1 
ATOM   1329 N NE2 . GLN A 1 164 ? -0.934  1.005   32.941  1.00 32.27 ? 164 GLN A NE2 1 
ATOM   1330 N N   . VAL A 1 165 ? -0.418  -4.855  31.697  1.00 34.06 ? 165 VAL A N   1 
ATOM   1331 C CA  . VAL A 1 165 ? -0.097  -6.208  31.232  1.00 34.15 ? 165 VAL A CA  1 
ATOM   1332 C C   . VAL A 1 165 ? -1.301  -6.907  30.597  1.00 35.65 ? 165 VAL A C   1 
ATOM   1333 O O   . VAL A 1 165 ? -1.123  -7.798  29.759  1.00 34.64 ? 165 VAL A O   1 
ATOM   1334 C CB  . VAL A 1 165 ? 0.512   -7.065  32.363  1.00 32.15 ? 165 VAL A CB  1 
ATOM   1335 C CG1 . VAL A 1 165 ? 1.885   -6.468  32.817  1.00 25.76 ? 165 VAL A CG1 1 
ATOM   1336 C CG2 . VAL A 1 165 ? -0.459  -7.251  33.524  1.00 31.34 ? 165 VAL A CG2 1 
ATOM   1337 N N   . ASN A 1 166 ? -2.529  -6.536  30.983  1.00 37.09 ? 166 ASN A N   1 
ATOM   1338 C CA  . ASN A 1 166 ? -3.745  -7.061  30.333  1.00 37.50 ? 166 ASN A CA  1 
ATOM   1339 C C   . ASN A 1 166 ? -3.867  -6.642  28.870  1.00 37.63 ? 166 ASN A C   1 
ATOM   1340 O O   . ASN A 1 166 ? -4.444  -7.385  28.073  1.00 38.89 ? 166 ASN A O   1 
ATOM   1341 C CB  . ASN A 1 166 ? -4.976  -6.621  31.118  1.00 38.80 ? 166 ASN A CB  1 
ATOM   1342 C CG  . ASN A 1 166 ? -4.932  -5.163  31.468  1.00 39.78 ? 166 ASN A CG  1 
ATOM   1343 O OD1 . ASN A 1 166 ? -4.251  -4.762  32.426  1.00 38.46 ? 166 ASN A OD1 1 
ATOM   1344 N ND2 . ASN A 1 166 ? -5.691  -4.346  30.726  1.00 38.32 ? 166 ASN A ND2 1 
ATOM   1345 N N   . GLN A 1 167 ? -3.365  -5.458  28.523  1.00 34.90 ? 167 GLN A N   1 
ATOM   1346 C CA  . GLN A 1 167 ? -3.429  -4.936  27.134  1.00 33.26 ? 167 GLN A CA  1 
ATOM   1347 C C   . GLN A 1 167 ? -2.368  -5.625  26.277  1.00 36.08 ? 167 GLN A C   1 
ATOM   1348 O O   . GLN A 1 167 ? -2.355  -5.404  25.078  1.00 37.81 ? 167 GLN A O   1 
ATOM   1349 C CB  . GLN A 1 167 ? -3.224  -3.422  27.105  1.00 34.68 ? 167 GLN A CB  1 
ATOM   1350 C CG  . GLN A 1 167 ? -4.288  -2.639  27.856  1.00 35.62 ? 167 GLN A CG  1 
ATOM   1351 C CD  . GLN A 1 167 ? -4.153  -1.142  27.723  1.00 34.87 ? 167 GLN A CD  1 
ATOM   1352 O OE1 . GLN A 1 167 ? -3.701  -0.640  26.719  1.00 35.85 ? 167 GLN A OE1 1 
ATOM   1353 N NE2 . GLN A 1 167 ? -4.539  -0.423  28.758  1.00 31.34 ? 167 GLN A NE2 1 
ATOM   1354 N N   . SER A 1 168 ? -1.479  -6.391  26.900  1.00 35.03 ? 168 SER A N   1 
ATOM   1355 C CA  . SER A 1 168 ? -0.443  -7.100  26.117  1.00 40.16 ? 168 SER A CA  1 
ATOM   1356 C C   . SER A 1 168 ? -0.768  -8.594  26.066  1.00 39.65 ? 168 SER A C   1 
ATOM   1357 O O   . SER A 1 168 ? -0.099  -9.277  25.361  1.00 40.45 ? 168 SER A O   1 
ATOM   1358 C CB  . SER A 1 168 ? 0.965   -6.819  26.617  1.00 34.82 ? 168 SER A CB  1 
ATOM   1359 O OG  . SER A 1 168 ? 1.154   -7.254  27.942  1.00 33.98 ? 168 SER A OG  1 
ATOM   1360 N N   . ARG A 1 169 ? -1.860  -9.007  26.688  1.00 38.31 ? 169 ARG A N   1 
ATOM   1361 C CA  . ARG A 1 169 ? -2.287  -10.423 26.794  1.00 44.01 ? 169 ARG A CA  1 
ATOM   1362 C C   . ARG A 1 169 ? -2.341  -11.158 25.450  1.00 44.94 ? 169 ARG A C   1 
ATOM   1363 O O   . ARG A 1 169 ? -1.799  -12.240 25.373  1.00 45.56 ? 169 ARG A O   1 
ATOM   1364 C CB  . ARG A 1 169 ? -3.657  -10.461 27.454  1.00 30.00 ? 169 ARG A CB  1 
ATOM   1365 C CG  . ARG A 1 169 ? -4.020  -11.788 28.091  1.00 30.00 ? 169 ARG A CG  1 
ATOM   1366 C CD  . ARG A 1 169 ? -5.438  -11.622 28.581  1.00 30.00 ? 169 ARG A CD  1 
ATOM   1367 N NE  . ARG A 1 169 ? -5.558  -11.263 29.988  1.00 30.00 ? 169 ARG A NE  1 
ATOM   1368 C CZ  . ARG A 1 169 ? -6.154  -10.177 30.445  1.00 30.00 ? 169 ARG A CZ  1 
ATOM   1369 N NH1 . ARG A 1 169 ? -6.253  -9.987  31.747  1.00 30.00 ? 169 ARG A NH1 1 
ATOM   1370 N NH2 . ARG A 1 169 ? -6.664  -9.296  29.602  1.00 30.00 ? 169 ARG A NH2 1 
ATOM   1371 N N   . ASN A 1 170 ? -2.967  -10.590 24.431  1.00 42.37 ? 170 ASN A N   1 
ATOM   1372 C CA  . ASN A 1 170 ? -3.105  -11.338 23.155  1.00 43.47 ? 170 ASN A CA  1 
ATOM   1373 C C   . ASN A 1 170 ? -1.887  -11.136 22.248  1.00 45.57 ? 170 ASN A C   1 
ATOM   1374 O O   . ASN A 1 170 ? -1.700  -11.963 21.379  1.00 48.38 ? 170 ASN A O   1 
ATOM   1375 C CB  . ASN A 1 170 ? -4.433  -11.062 22.450  1.00 46.98 ? 170 ASN A CB  1 
ATOM   1376 C CG  . ASN A 1 170 ? -5.662  -11.322 23.295  1.00 49.47 ? 170 ASN A CG  1 
ATOM   1377 O OD1 . ASN A 1 170 ? -5.712  -12.244 24.101  1.00 52.30 ? 170 ASN A OD1 1 
ATOM   1378 N ND2 . ASN A 1 170 ? -6.676  -10.512 23.107  1.00 46.55 ? 170 ASN A ND2 1 
ATOM   1379 N N   . CYS A 1 171 ? -1.086  -10.094 22.439  1.00 43.73 ? 171 CYS A N   1 
ATOM   1380 C CA  . CYS A 1 171 ? 0.086   -9.936  21.541  1.00 41.21 ? 171 CYS A CA  1 
ATOM   1381 C C   . CYS A 1 171 ? 1.366   -10.463 22.203  1.00 42.38 ? 171 CYS A C   1 
ATOM   1382 O O   . CYS A 1 171 ? 2.357   -10.582 21.492  1.00 38.98 ? 171 CYS A O   1 
ATOM   1383 C CB  . CYS A 1 171 ? 0.266   -8.497  21.068  1.00 42.10 ? 171 CYS A CB  1 
ATOM   1384 S SG  . CYS A 1 171 ? 0.090   -7.260  22.373  1.00 53.52 ? 171 CYS A SG  1 
ATOM   1385 N N   . LYS A 1 172 ? 1.347   -10.720 23.513  1.00 44.20 ? 172 LYS A N   1 
ATOM   1386 C CA  . LYS A 1 172 ? 2.528   -11.296 24.171  1.00 43.23 ? 172 LYS A CA  1 
ATOM   1387 C C   . LYS A 1 172 ? 2.015   -11.915 25.476  1.00 42.11 ? 172 LYS A C   1 
ATOM   1388 O O   . LYS A 1 172 ? 1.866   -11.219 26.480  1.00 50.76 ? 172 LYS A O   1 
ATOM   1389 C CB  . LYS A 1 172 ? 3.592   -10.241 24.415  1.00 39.88 ? 172 LYS A CB  1 
ATOM   1390 C CG  . LYS A 1 172 ? 4.694   -10.690 25.383  1.00 40.91 ? 172 LYS A CG  1 
ATOM   1391 C CD  . LYS A 1 172 ? 5.846   -11.313 24.643  1.00 38.14 ? 172 LYS A CD  1 
ATOM   1392 C CE  . LYS A 1 172 ? 6.948   -11.695 25.612  1.00 36.19 ? 172 LYS A CE  1 
ATOM   1393 N NZ  . LYS A 1 172 ? 7.531   -13.027 25.282  1.00 34.85 ? 172 LYS A NZ  1 
ATOM   1394 N N   . GLY A 1 173 ? 1.781   -13.197 25.465  1.00 41.72 ? 173 GLY A N   1 
ATOM   1395 C CA  . GLY A 1 173 ? 1.104   -13.839 26.584  1.00 44.28 ? 173 GLY A CA  1 
ATOM   1396 C C   . GLY A 1 173 ? 1.784   -13.992 27.931  1.00 43.27 ? 173 GLY A C   1 
ATOM   1397 O O   . GLY A 1 173 ? 1.463   -14.959 28.640  1.00 41.47 ? 173 GLY A O   1 
ATOM   1398 N N   . ASP A 1 174 ? 2.664   -13.057 28.340  1.00 38.58 ? 174 ASP A N   1 
ATOM   1399 C CA  . ASP A 1 174 ? 3.408   -13.285 29.578  1.00 34.81 ? 174 ASP A CA  1 
ATOM   1400 C C   . ASP A 1 174 ? 2.508   -13.236 30.802  1.00 34.87 ? 174 ASP A C   1 
ATOM   1401 O O   . ASP A 1 174 ? 2.735   -13.972 31.762  1.00 34.25 ? 174 ASP A O   1 
ATOM   1402 C CB  . ASP A 1 174 ? 4.512   -12.229 29.728  1.00 35.73 ? 174 ASP A CB  1 
ATOM   1403 C CG  . ASP A 1 174 ? 5.871   -12.690 29.165  1.00 36.31 ? 174 ASP A CG  1 
ATOM   1404 O OD1 . ASP A 1 174 ? 5.940   -13.775 28.557  1.00 34.34 ? 174 ASP A OD1 1 
ATOM   1405 O OD2 . ASP A 1 174 ? 6.866   -11.941 29.306  1.00 30.23 ? 174 ASP A OD2 1 
ATOM   1406 N N   . TYR A 1 175 ? 1.457   -12.424 30.789  1.00 32.89 ? 175 TYR A N   1 
ATOM   1407 C CA  . TYR A 1 175 ? 0.705   -12.190 32.003  1.00 33.04 ? 175 TYR A CA  1 
ATOM   1408 C C   . TYR A 1 175 ? -0.774  -12.468 31.793  1.00 38.08 ? 175 TYR A C   1 
ATOM   1409 O O   . TYR A 1 175 ? -1.322  -12.284 30.700  1.00 35.62 ? 175 TYR A O   1 
ATOM   1410 C CB  . TYR A 1 175 ? 0.838   -10.711 32.504  1.00 37.70 ? 175 TYR A CB  1 
ATOM   1411 C CG  . TYR A 1 175 ? 2.204   -10.326 33.005  1.00 32.28 ? 175 TYR A CG  1 
ATOM   1412 C CD1 . TYR A 1 175 ? 2.542   -10.498 34.345  1.00 32.98 ? 175 TYR A CD1 1 
ATOM   1413 C CD2 . TYR A 1 175 ? 3.129   -9.768  32.150  1.00 33.62 ? 175 TYR A CD2 1 
ATOM   1414 C CE1 . TYR A 1 175 ? 3.799   -10.135 34.819  1.00 31.92 ? 175 TYR A CE1 1 
ATOM   1415 C CE2 . TYR A 1 175 ? 4.391   -9.416  32.585  1.00 32.02 ? 175 TYR A CE2 1 
ATOM   1416 C CZ  . TYR A 1 175 ? 4.734   -9.605  33.921  1.00 33.11 ? 175 TYR A CZ  1 
ATOM   1417 O OH  . TYR A 1 175 ? 6.009   -9.257  34.320  1.00 29.50 ? 175 TYR A OH  1 
ATOM   1418 N N   . THR A 1 176 ? -1.365  -12.918 32.874  1.00 40.81 ? 176 THR A N   1 
ATOM   1419 C CA  . THR A 1 176 ? -2.825  -12.996 33.076  1.00 41.98 ? 176 THR A CA  1 
ATOM   1420 C C   . THR A 1 176 ? -3.124  -11.941 34.157  1.00 41.17 ? 176 THR A C   1 
ATOM   1421 O O   . THR A 1 176 ? -2.206  -11.474 34.840  1.00 43.07 ? 176 THR A O   1 
ATOM   1422 C CB  . THR A 1 176 ? -3.257  -14.434 33.366  1.00 40.14 ? 176 THR A CB  1 
ATOM   1423 O OG1 . THR A 1 176 ? -2.581  -14.901 34.525  1.00 37.54 ? 176 THR A OG1 1 
ATOM   1424 C CG2 . THR A 1 176 ? -2.973  -15.368 32.217  1.00 37.55 ? 176 THR A CG2 1 
ATOM   1425 N N   . GLY A 1 177 ? -4.354  -11.483 34.290  1.00 46.49 ? 177 GLY A N   1 
ATOM   1426 C CA  . GLY A 1 177 ? -4.544  -10.451 35.329  1.00 49.44 ? 177 GLY A CA  1 
ATOM   1427 C C   . GLY A 1 177 ? -4.279  -9.025  34.870  1.00 40.38 ? 177 GLY A C   1 
ATOM   1428 O O   . GLY A 1 177 ? -3.641  -8.793  33.859  1.00 42.71 ? 177 GLY A O   1 
ATOM   1429 N N   . ASN A 1 178 ? -4.717  -8.099  35.700  1.00 50.49 ? 178 ASN A N   1 
ATOM   1430 C CA  . ASN A 1 178 ? -4.765  -6.665  35.358  1.00 43.87 ? 178 ASN A CA  1 
ATOM   1431 C C   . ASN A 1 178 ? -3.987  -5.830  36.356  1.00 44.54 ? 178 ASN A C   1 
ATOM   1432 O O   . ASN A 1 178 ? -4.369  -5.843  37.513  1.00 43.13 ? 178 ASN A O   1 
ATOM   1433 C CB  . ASN A 1 178 ? -6.201  -6.182  35.530  1.00 55.95 ? 178 ASN A CB  1 
ATOM   1434 C CG  . ASN A 1 178 ? -6.868  -5.931  34.203  1.00 58.78 ? 178 ASN A CG  1 
ATOM   1435 O OD1 . ASN A 1 178 ? -7.529  -6.808  33.660  1.00 65.12 ? 178 ASN A OD1 1 
ATOM   1436 N ND2 . ASN A 1 178 ? -6.656  -4.747  33.665  1.00 72.08 ? 178 ASN A ND2 1 
ATOM   1437 N N   . PHE A 1 179 ? -2.972  -5.130  35.861  1.00 40.45 ? 179 PHE A N   1 
ATOM   1438 C CA  . PHE A 1 179 ? -2.126  -4.207  36.653  1.00 34.97 ? 179 PHE A CA  1 
ATOM   1439 C C   . PHE A 1 179 ? -1.146  -3.523  35.705  1.00 27.36 ? 179 PHE A C   1 
ATOM   1440 O O   . PHE A 1 179 ? -0.932  -4.002  34.622  1.00 30.01 ? 179 PHE A O   1 
ATOM   1441 C CB  . PHE A 1 179 ? -1.359  -4.895  37.787  1.00 32.41 ? 179 PHE A CB  1 
ATOM   1442 C CG  . PHE A 1 179 ? -0.571  -6.129  37.426  1.00 34.46 ? 179 PHE A CG  1 
ATOM   1443 C CD1 . PHE A 1 179 ? 0.751   -6.030  37.028  1.00 33.72 ? 179 PHE A CD1 1 
ATOM   1444 C CD2 . PHE A 1 179 ? -1.125  -7.388  37.530  1.00 34.63 ? 179 PHE A CD2 1 
ATOM   1445 C CE1 . PHE A 1 179 ? 1.489   -7.154  36.713  1.00 31.17 ? 179 PHE A CE1 1 
ATOM   1446 C CE2 . PHE A 1 179 ? -0.386  -8.509  37.209  1.00 34.77 ? 179 PHE A CE2 1 
ATOM   1447 C CZ  . PHE A 1 179 ? 0.917   -8.390  36.803  1.00 32.53 ? 179 PHE A CZ  1 
ATOM   1448 N N   . GLY A 1 180 ? -0.696  -2.349  36.105  1.00 28.19 ? 180 GLY A N   1 
ATOM   1449 C CA  . GLY A 1 180 ? 0.379   -1.641  35.433  1.00 32.06 ? 180 GLY A CA  1 
ATOM   1450 C C   . GLY A 1 180 ? 1.738   -2.201  35.815  1.00 29.00 ? 180 GLY A C   1 
ATOM   1451 O O   . GLY A 1 180 ? 1.867   -2.813  36.866  1.00 26.28 ? 180 GLY A O   1 
ATOM   1452 N N   . HIS A 1 181 ? 2.731   -2.010  34.943  1.00 27.79 ? 181 HIS A N   1 
ATOM   1453 C CA  . HIS A 1 181 ? 4.021   -2.681  35.127  1.00 26.53 ? 181 HIS A CA  1 
ATOM   1454 C C   . HIS A 1 181 ? 5.123   -1.891  34.421  1.00 27.27 ? 181 HIS A C   1 
ATOM   1455 O O   . HIS A 1 181 ? 4.870   -1.203  33.427  1.00 28.61 ? 181 HIS A O   1 
ATOM   1456 C CB  . HIS A 1 181 ? 3.998   -4.119  34.602  1.00 24.69 ? 181 HIS A CB  1 
ATOM   1457 C CG  . HIS A 1 181 ? 5.156   -4.990  35.077  1.00 26.73 ? 181 HIS A CG  1 
ATOM   1458 N ND1 . HIS A 1 181 ? 5.512   -5.116  36.404  1.00 26.46 ? 181 HIS A ND1 1 
ATOM   1459 C CD2 . HIS A 1 181 ? 5.989   -5.814  34.395  1.00 22.89 ? 181 HIS A CD2 1 
ATOM   1460 C CE1 . HIS A 1 181 ? 6.490   -5.995  36.522  1.00 26.29 ? 181 HIS A CE1 1 
ATOM   1461 N NE2 . HIS A 1 181 ? 6.781   -6.449  35.318  1.00 25.63 ? 181 HIS A NE2 1 
ATOM   1462 N N   . TYR A 1 182 ? 6.353   -2.014  34.935  1.00 22.90 ? 182 TYR A N   1 
ATOM   1463 C CA  . TYR A 1 182 ? 7.531   -1.365  34.382  1.00 25.12 ? 182 TYR A CA  1 
ATOM   1464 C C   . TYR A 1 182 ? 8.576   -2.411  34.009  1.00 23.24 ? 182 TYR A C   1 
ATOM   1465 O O   . TYR A 1 182 ? 8.676   -3.461  34.650  1.00 22.59 ? 182 TYR A O   1 
ATOM   1466 C CB  . TYR A 1 182 ? 8.191   -0.415  35.389  1.00 24.18 ? 182 TYR A CB  1 
ATOM   1467 C CG  . TYR A 1 182 ? 7.433   0.868   35.671  1.00 25.37 ? 182 TYR A CG  1 
ATOM   1468 C CD1 . TYR A 1 182 ? 6.447   0.904   36.645  1.00 27.77 ? 182 TYR A CD1 1 
ATOM   1469 C CD2 . TYR A 1 182 ? 7.741   2.027   34.999  1.00 26.67 ? 182 TYR A CD2 1 
ATOM   1470 C CE1 . TYR A 1 182 ? 5.771   2.038   36.926  1.00 25.32 ? 182 TYR A CE1 1 
ATOM   1471 C CE2 . TYR A 1 182 ? 7.077   3.201   35.282  1.00 30.57 ? 182 TYR A CE2 1 
ATOM   1472 C CZ  . TYR A 1 182 ? 6.094   3.192   36.250  1.00 28.46 ? 182 TYR A CZ  1 
ATOM   1473 O OH  . TYR A 1 182 ? 5.412   4.343   36.540  1.00 31.45 ? 182 TYR A OH  1 
ATOM   1474 N N   . GLY A 1 183 ? 9.358   -2.104  32.985  1.00 24.33 ? 183 GLY A N   1 
ATOM   1475 C CA  . GLY A 1 183 ? 10.535  -2.904  32.645  1.00 23.93 ? 183 GLY A CA  1 
ATOM   1476 C C   . GLY A 1 183 ? 11.599  -2.007  32.043  1.00 26.69 ? 183 GLY A C   1 
ATOM   1477 O O   . GLY A 1 183 ? 11.460  -0.778  32.105  1.00 24.96 ? 183 GLY A O   1 
ATOM   1478 N N   . LEU A 1 184 ? 12.690  -2.583  31.531  1.00 25.75 ? 184 LEU A N   1 
ATOM   1479 C CA  . LEU A 1 184 ? 13.750  -1.808  30.885  1.00 26.70 ? 184 LEU A CA  1 
ATOM   1480 C C   . LEU A 1 184 ? 13.978  -2.319  29.472  1.00 28.65 ? 184 LEU A C   1 
ATOM   1481 O O   . LEU A 1 184 ? 14.422  -3.462  29.282  1.00 27.75 ? 184 LEU A O   1 
ATOM   1482 C CB  . LEU A 1 184 ? 15.063  -1.869  31.659  1.00 27.18 ? 184 LEU A CB  1 
ATOM   1483 C CG  . LEU A 1 184 ? 16.203  -1.014  31.047  1.00 25.49 ? 184 LEU A CG  1 
ATOM   1484 C CD1 . LEU A 1 184 ? 15.932  0.438   31.314  1.00 25.35 ? 184 LEU A CD1 1 
ATOM   1485 C CD2 . LEU A 1 184 ? 17.600  -1.450  31.553  1.00 23.96 ? 184 LEU A CD2 1 
ATOM   1486 N N   . ILE A 1 185 ? 13.736  -1.457  28.489  1.00 29.78 ? 185 ILE A N   1 
ATOM   1487 C CA  . ILE A 1 185 ? 14.165  -1.720  27.115  1.00 29.00 ? 185 ILE A CA  1 
ATOM   1488 C C   . ILE A 1 185 ? 15.671  -1.454  27.034  1.00 31.49 ? 185 ILE A C   1 
ATOM   1489 O O   . ILE A 1 185 ? 16.113  -0.319  27.237  1.00 26.78 ? 185 ILE A O   1 
ATOM   1490 C CB  . ILE A 1 185 ? 13.405  -0.827  26.118  1.00 30.10 ? 185 ILE A CB  1 
ATOM   1491 C CG1 . ILE A 1 185 ? 11.884  -0.980  26.252  1.00 31.23 ? 185 ILE A CG1 1 
ATOM   1492 C CG2 . ILE A 1 185 ? 13.838  -1.115  24.705  1.00 31.77 ? 185 ILE A CG2 1 
ATOM   1493 C CD1 . ILE A 1 185 ? 11.159  0.067   25.522  1.00 32.00 ? 185 ILE A CD1 1 
ATOM   1494 N N   . TRP A 1 186 ? 16.466  -2.501  26.741  1.00 30.67 ? 186 TRP A N   1 
ATOM   1495 C CA  . TRP A 1 186 ? 17.920  -2.352  26.655  1.00 28.86 ? 186 TRP A CA  1 
ATOM   1496 C C   . TRP A 1 186 ? 18.500  -2.752  25.306  1.00 30.91 ? 186 TRP A C   1 
ATOM   1497 O O   . TRP A 1 186 ? 19.714  -2.609  25.103  1.00 31.76 ? 186 TRP A O   1 
ATOM   1498 C CB  . TRP A 1 186 ? 18.614  -3.153  27.781  1.00 28.28 ? 186 TRP A CB  1 
ATOM   1499 C CG  . TRP A 1 186 ? 18.305  -4.627  27.784  1.00 28.52 ? 186 TRP A CG  1 
ATOM   1500 C CD1 . TRP A 1 186 ? 17.249  -5.239  28.410  1.00 28.45 ? 186 TRP A CD1 1 
ATOM   1501 C CD2 . TRP A 1 186 ? 19.068  -5.673  27.169  1.00 26.95 ? 186 TRP A CD2 1 
ATOM   1502 N NE1 . TRP A 1 186 ? 17.310  -6.595  28.211  1.00 28.16 ? 186 TRP A NE1 1 
ATOM   1503 C CE2 . TRP A 1 186 ? 18.414  -6.895  27.461  1.00 28.45 ? 186 TRP A CE2 1 
ATOM   1504 C CE3 . TRP A 1 186 ? 20.252  -5.700  26.428  1.00 30.29 ? 186 TRP A CE3 1 
ATOM   1505 C CZ2 . TRP A 1 186 ? 18.901  -8.151  27.018  1.00 27.17 ? 186 TRP A CZ2 1 
ATOM   1506 C CZ3 . TRP A 1 186 ? 20.749  -6.956  25.978  1.00 31.61 ? 186 TRP A CZ3 1 
ATOM   1507 C CH2 . TRP A 1 186 ? 20.051  -8.155  26.263  1.00 29.07 ? 186 TRP A CH2 1 
ATOM   1508 N N   . ASP A 1 187 ? 17.679  -3.259  24.393  1.00 33.79 ? 187 ASP A N   1 
ATOM   1509 C CA  . ASP A 1 187 ? 18.090  -3.615  23.041  1.00 34.16 ? 187 ASP A CA  1 
ATOM   1510 C C   . ASP A 1 187 ? 16.834  -3.736  22.189  1.00 34.00 ? 187 ASP A C   1 
ATOM   1511 O O   . ASP A 1 187 ? 15.707  -3.746  22.706  1.00 33.33 ? 187 ASP A O   1 
ATOM   1512 C CB  . ASP A 1 187 ? 18.911  -4.908  23.042  1.00 32.44 ? 187 ASP A CB  1 
ATOM   1513 C CG  . ASP A 1 187 ? 19.742  -5.070  21.792  1.00 34.81 ? 187 ASP A CG  1 
ATOM   1514 O OD1 . ASP A 1 187 ? 20.011  -4.073  21.101  1.00 38.70 ? 187 ASP A OD1 1 
ATOM   1515 O OD2 . ASP A 1 187 ? 20.179  -6.198  21.534  1.00 37.40 ? 187 ASP A OD2 1 
ATOM   1516 N N   . MET A 1 188 ? 17.030  -3.803  20.872  1.00 35.68 ? 188 MET A N   1 
ATOM   1517 C CA  . MET A 1 188 ? 15.907  -4.098  19.988  1.00 37.69 ? 188 MET A CA  1 
ATOM   1518 C C   . MET A 1 188 ? 16.398  -4.896  18.785  1.00 37.26 ? 188 MET A C   1 
ATOM   1519 O O   . MET A 1 188 ? 17.554  -4.773  18.366  1.00 36.35 ? 188 MET A O   1 
ATOM   1520 C CB  . MET A 1 188 ? 15.157  -2.826  19.516  1.00 39.48 ? 188 MET A CB  1 
ATOM   1521 C CG  . MET A 1 188 ? 16.001  -1.595  19.338  1.00 41.58 ? 188 MET A CG  1 
ATOM   1522 S SD  . MET A 1 188 ? 15.084  -0.040  19.297  1.00 46.12 ? 188 MET A SD  1 
ATOM   1523 C CE  . MET A 1 188 ? 14.602  -0.006  17.590  1.00 44.91 ? 188 MET A CE  1 
ATOM   1524 N N   . THR A 1 189 ? 15.519  -5.758  18.273  1.00 36.72 ? 189 THR A N   1 
ATOM   1525 C CA  . THR A 1 189 ? 15.710  -6.390  16.973  1.00 39.83 ? 189 THR A CA  1 
ATOM   1526 C C   . THR A 1 189 ? 15.077  -5.498  15.906  1.00 43.51 ? 189 THR A C   1 
ATOM   1527 O O   . THR A 1 189 ? 14.634  -4.375  16.180  1.00 38.24 ? 189 THR A O   1 
ATOM   1528 C CB  . THR A 1 189 ? 15.092  -7.801  16.926  1.00 41.01 ? 189 THR A CB  1 
ATOM   1529 O OG1 . THR A 1 189 ? 13.647  -7.723  16.886  1.00 43.88 ? 189 THR A OG1 1 
ATOM   1530 C CG2 . THR A 1 189 ? 15.509  -8.649  18.125  1.00 39.06 ? 189 THR A CG2 1 
ATOM   1531 N N   . SER A 1 190 ? 14.964  -6.019  14.681  1.00 44.18 ? 190 SER A N   1 
ATOM   1532 C CA  . SER A 1 190 ? 14.320  -5.248  13.622  1.00 45.55 ? 190 SER A CA  1 
ATOM   1533 C C   . SER A 1 190 ? 12.843  -5.052  13.887  1.00 43.33 ? 190 SER A C   1 
ATOM   1534 O O   . SER A 1 190 ? 12.251  -4.093  13.382  1.00 46.82 ? 190 SER A O   1 
ATOM   1535 C CB  . SER A 1 190 ? 14.519  -5.945  12.272  1.00 45.33 ? 190 SER A CB  1 
ATOM   1536 O OG  . SER A 1 190 ? 14.165  -7.317  12.356  1.00 47.56 ? 190 SER A OG  1 
ATOM   1537 N N   . THR A 1 191 ? 12.240  -5.909  14.696  1.00 42.36 ? 191 THR A N   1 
ATOM   1538 C CA  . THR A 1 191 ? 10.799  -5.873  14.907  1.00 44.60 ? 191 THR A CA  1 
ATOM   1539 C C   . THR A 1 191 ? 10.378  -5.815  16.363  1.00 42.64 ? 191 THR A C   1 
ATOM   1540 O O   . THR A 1 191 ? 9.250   -5.396  16.625  1.00 40.17 ? 191 THR A O   1 
ATOM   1541 C CB  . THR A 1 191 ? 10.135  -7.100  14.269  1.00 44.72 ? 191 THR A CB  1 
ATOM   1542 O OG1 . THR A 1 191 ? 10.873  -8.264  14.666  1.00 47.18 ? 191 THR A OG1 1 
ATOM   1543 C CG2 . THR A 1 191 ? 10.061  -6.987  12.720  1.00 45.77 ? 191 THR A CG2 1 
ATOM   1544 N N   . HIS A 1 192 ? 11.234  -6.194  17.316  1.00 41.64 ? 192 HIS A N   1 
ATOM   1545 C CA  . HIS A 1 192 ? 10.821  -6.347  18.699  1.00 38.68 ? 192 HIS A CA  1 
ATOM   1546 C C   . HIS A 1 192 ? 11.703  -5.511  19.621  1.00 39.65 ? 192 HIS A C   1 
ATOM   1547 O O   . HIS A 1 192 ? 12.922  -5.407  19.421  1.00 34.96 ? 192 HIS A O   1 
ATOM   1548 C CB  . HIS A 1 192 ? 10.951  -7.800  19.190  1.00 39.79 ? 192 HIS A CB  1 
ATOM   1549 C CG  . HIS A 1 192 ? 9.970   -8.771  18.607  1.00 43.16 ? 192 HIS A CG  1 
ATOM   1550 N ND1 . HIS A 1 192 ? 9.961   -9.122  17.271  1.00 44.95 ? 192 HIS A ND1 1 
ATOM   1551 C CD2 . HIS A 1 192 ? 9.002   -9.518  19.200  1.00 43.67 ? 192 HIS A CD2 1 
ATOM   1552 C CE1 . HIS A 1 192 ? 9.029   -10.042 17.068  1.00 41.89 ? 192 HIS A CE1 1 
ATOM   1553 N NE2 . HIS A 1 192 ? 8.430   -10.295 18.219  1.00 40.47 ? 192 HIS A NE2 1 
ATOM   1554 N N   . TYR A 1 193 ? 11.093  -4.984  20.679  1.00 35.02 ? 193 TYR A N   1 
ATOM   1555 C CA  . TYR A 1 193 ? 11.855  -4.493  21.823  1.00 35.03 ? 193 TYR A CA  1 
ATOM   1556 C C   . TYR A 1 193 ? 12.336  -5.663  22.692  1.00 34.86 ? 193 TYR A C   1 
ATOM   1557 O O   . TYR A 1 193 ? 11.573  -6.597  22.956  1.00 35.25 ? 193 TYR A O   1 
ATOM   1558 C CB  . TYR A 1 193 ? 10.985  -3.580  22.693  1.00 32.52 ? 193 TYR A CB  1 
ATOM   1559 C CG  . TYR A 1 193 ? 10.411  -2.340  22.078  1.00 31.97 ? 193 TYR A CG  1 
ATOM   1560 C CD1 . TYR A 1 193 ? 11.231  -1.323  21.560  1.00 36.70 ? 193 TYR A CD1 1 
ATOM   1561 C CD2 . TYR A 1 193 ? 9.054   -2.134  22.088  1.00 34.73 ? 193 TYR A CD2 1 
ATOM   1562 C CE1 . TYR A 1 193 ? 10.664  -0.107  21.027  1.00 33.89 ? 193 TYR A CE1 1 
ATOM   1563 C CE2 . TYR A 1 193 ? 8.490   -0.956  21.573  1.00 35.65 ? 193 TYR A CE2 1 
ATOM   1564 C CZ  . TYR A 1 193 ? 9.303   0.047   21.054  1.00 37.41 ? 193 TYR A CZ  1 
ATOM   1565 O OH  . TYR A 1 193 ? 8.707   1.186   20.557  1.00 36.29 ? 193 TYR A OH  1 
ATOM   1566 N N   . VAL A 1 194 ? 13.581  -5.588  23.182  1.00 33.62 ? 194 VAL A N   1 
ATOM   1567 C CA  . VAL A 1 194 ? 14.114  -6.539  24.162  1.00 33.38 ? 194 VAL A CA  1 
ATOM   1568 C C   . VAL A 1 194 ? 13.977  -5.902  25.541  1.00 31.84 ? 194 VAL A C   1 
ATOM   1569 O O   . VAL A 1 194 ? 14.635  -4.899  25.846  1.00 31.45 ? 194 VAL A O   1 
ATOM   1570 C CB  . VAL A 1 194 ? 15.576  -6.928  23.880  1.00 32.48 ? 194 VAL A CB  1 
ATOM   1571 C CG1 . VAL A 1 194 ? 15.991  -8.058  24.810  1.00 33.10 ? 194 VAL A CG1 1 
ATOM   1572 C CG2 . VAL A 1 194 ? 15.786  -7.371  22.403  1.00 32.55 ? 194 VAL A CG2 1 
ATOM   1573 N N   . VAL A 1 195 ? 13.145  -6.492  26.392  1.00 31.56 ? 195 VAL A N   1 
ATOM   1574 C CA  . VAL A 1 195 ? 12.795  -5.909  27.678  1.00 31.38 ? 195 VAL A CA  1 
ATOM   1575 C C   . VAL A 1 195 ? 13.324  -6.782  28.805  1.00 28.94 ? 195 VAL A C   1 
ATOM   1576 O O   . VAL A 1 195 ? 13.013  -7.977  28.878  1.00 29.38 ? 195 VAL A O   1 
ATOM   1577 C CB  . VAL A 1 195 ? 11.276  -5.720  27.808  1.00 30.43 ? 195 VAL A CB  1 
ATOM   1578 C CG1 . VAL A 1 195 ? 10.916  -5.169  29.199  1.00 27.79 ? 195 VAL A CG1 1 
ATOM   1579 C CG2 . VAL A 1 195 ? 10.780  -4.821  26.680  1.00 33.33 ? 195 VAL A CG2 1 
ATOM   1580 N N   . ALA A 1 196 ? 14.049  -6.162  29.727  1.00 28.43 ? 196 ALA A N   1 
ATOM   1581 C CA  . ALA A 1 196 ? 14.329  -6.767  31.019  1.00 30.36 ? 196 ALA A CA  1 
ATOM   1582 C C   . ALA A 1 196 ? 13.125  -6.499  31.923  1.00 28.73 ? 196 ALA A C   1 
ATOM   1583 O O   . ALA A 1 196 ? 12.927  -5.363  32.392  1.00 25.90 ? 196 ALA A O   1 
ATOM   1584 C CB  . ALA A 1 196 ? 15.612  -6.202  31.618  1.00 26.32 ? 196 ALA A CB  1 
ATOM   1585 N N   . ASP A 1 197 ? 12.329  -7.546  32.155  1.00 26.94 ? 197 ASP A N   1 
ATOM   1586 C CA  . ASP A 1 197 ? 11.118  -7.488  32.957  1.00 28.00 ? 197 ASP A CA  1 
ATOM   1587 C C   . ASP A 1 197 ? 11.441  -8.007  34.343  1.00 25.58 ? 197 ASP A C   1 
ATOM   1588 O O   . ASP A 1 197 ? 11.619  -9.226  34.514  1.00 26.05 ? 197 ASP A O   1 
ATOM   1589 C CB  . ASP A 1 197 ? 9.995   -8.314  32.310  1.00 28.04 ? 197 ASP A CB  1 
ATOM   1590 C CG  . ASP A 1 197 ? 8.660   -8.320  33.144  1.00 26.96 ? 197 ASP A CG  1 
ATOM   1591 O OD1 . ASP A 1 197 ? 8.660   -7.936  34.350  1.00 24.57 ? 197 ASP A OD1 1 
ATOM   1592 O OD2 . ASP A 1 197 ? 7.605   -8.770  32.589  1.00 29.03 ? 197 ASP A OD2 1 
ATOM   1593 N N   . PRO A 1 198 ? 11.453  -7.139  35.375  1.00 26.06 ? 198 PRO A N   1 
ATOM   1594 C CA  . PRO A 1 198 ? 11.855  -7.568  36.726  1.00 23.91 ? 198 PRO A CA  1 
ATOM   1595 C C   . PRO A 1 198 ? 10.949  -8.620  37.370  1.00 25.31 ? 198 PRO A C   1 
ATOM   1596 O O   . PRO A 1 198 ? 11.235  -9.110  38.486  1.00 21.21 ? 198 PRO A O   1 
ATOM   1597 C CB  . PRO A 1 198 ? 11.830  -6.254  37.521  1.00 24.69 ? 198 PRO A CB  1 
ATOM   1598 C CG  . PRO A 1 198 ? 10.926  -5.331  36.731  1.00 28.24 ? 198 PRO A CG  1 
ATOM   1599 C CD  . PRO A 1 198 ? 11.129  -5.703  35.308  1.00 26.61 ? 198 PRO A CD  1 
ATOM   1600 N N   . ALA A 1 199 ? 9.832   -8.956  36.707  1.00 26.85 ? 199 ALA A N   1 
ATOM   1601 C CA  . ALA A 1 199 ? 8.942   -10.020 37.173  1.00 27.69 ? 199 ALA A CA  1 
ATOM   1602 C C   . ALA A 1 199 ? 9.013   -11.302 36.354  1.00 27.27 ? 199 ALA A C   1 
ATOM   1603 O O   . ALA A 1 199 ? 8.326   -12.283 36.709  1.00 26.95 ? 199 ALA A O   1 
ATOM   1604 C CB  . ALA A 1 199 ? 7.470   -9.528  37.169  1.00 26.90 ? 199 ALA A CB  1 
ATOM   1605 N N   . LYS A 1 200 ? 9.770   -11.327 35.259  1.00 26.90 ? 200 LYS A N   1 
ATOM   1606 C CA  . LYS A 1 200 ? 9.765   -12.484 34.354  1.00 28.43 ? 200 LYS A CA  1 
ATOM   1607 C C   . LYS A 1 200 ? 11.153  -12.912 33.856  1.00 27.37 ? 200 LYS A C   1 
ATOM   1608 O O   . LYS A 1 200 ? 11.453  -14.108 33.835  1.00 26.96 ? 200 LYS A O   1 
ATOM   1609 C CB  . LYS A 1 200 ? 8.865   -12.225 33.150  1.00 29.11 ? 200 LYS A CB  1 
ATOM   1610 C CG  . LYS A 1 200 ? 7.390   -11.980 33.512  1.00 34.29 ? 200 LYS A CG  1 
ATOM   1611 C CD  . LYS A 1 200 ? 6.614   -13.244 33.643  1.00 32.52 ? 200 LYS A CD  1 
ATOM   1612 C CE  . LYS A 1 200 ? 7.035   -14.275 32.632  1.00 33.72 ? 200 LYS A CE  1 
ATOM   1613 N NZ  . LYS A 1 200 ? 6.413   -15.540 33.039  1.00 39.87 ? 200 LYS A NZ  1 
ATOM   1614 N N   . GLY A 1 201 ? 11.968  -11.980 33.375  1.00 28.19 ? 201 GLY A N   1 
ATOM   1615 C CA  . GLY A 1 201 ? 13.280  -12.349 32.851  1.00 28.55 ? 201 GLY A CA  1 
ATOM   1616 C C   . GLY A 1 201 ? 13.892  -11.206 32.067  1.00 30.62 ? 201 GLY A C   1 
ATOM   1617 O O   . GLY A 1 201 ? 13.259  -10.150 31.845  1.00 28.40 ? 201 GLY A O   1 
ATOM   1618 N N   . VAL A 1 202 ? 15.130  -11.449 31.613  1.00 28.07 ? 202 VAL A N   1 
ATOM   1619 C CA  . VAL A 1 202 ? 15.977  -10.388 31.058  1.00 27.93 ? 202 VAL A CA  1 
ATOM   1620 C C   . VAL A 1 202 ? 15.764  -10.080 29.571  1.00 29.62 ? 202 VAL A C   1 
ATOM   1621 O O   . VAL A 1 202 ? 16.142  -8.989  29.113  1.00 30.84 ? 202 VAL A O   1 
ATOM   1622 C CB  . VAL A 1 202 ? 17.446  -10.747 31.296  1.00 26.35 ? 202 VAL A CB  1 
ATOM   1623 C CG1 . VAL A 1 202 ? 17.893  -11.811 30.303  1.00 31.10 ? 202 VAL A CG1 1 
ATOM   1624 C CG2 . VAL A 1 202 ? 18.370  -9.461  31.239  1.00 26.47 ? 202 VAL A CG2 1 
ATOM   1625 N N   . ASN A 1 203 ? 15.179  -10.997 28.793  1.00 29.86 ? 203 ASN A N   1 
ATOM   1626 C CA  . ASN A 1 203 ? 15.040  -10.797 27.343  1.00 31.51 ? 203 ASN A CA  1 
ATOM   1627 C C   . ASN A 1 203 ? 13.619  -11.161 26.883  1.00 33.82 ? 203 ASN A C   1 
ATOM   1628 O O   . ASN A 1 203 ? 13.396  -12.009 26.023  1.00 35.57 ? 203 ASN A O   1 
ATOM   1629 C CB  . ASN A 1 203 ? 16.183  -11.532 26.585  1.00 36.51 ? 203 ASN A CB  1 
ATOM   1630 C CG  . ASN A 1 203 ? 15.857  -12.956 26.204  1.00 42.61 ? 203 ASN A CG  1 
ATOM   1631 O OD1 . ASN A 1 203 ? 15.082  -13.627 26.890  1.00 50.39 ? 203 ASN A OD1 1 
ATOM   1632 N ND2 . ASN A 1 203 ? 16.430  -13.431 25.098  1.00 46.79 ? 203 ASN A ND2 1 
ATOM   1633 N N   . ARG A 1 204 ? 12.637  -10.443 27.421  1.00 31.75 ? 204 ARG A N   1 
ATOM   1634 C CA  . ARG A 1 204 ? 11.251  -10.579 26.964  1.00 31.48 ? 204 ARG A CA  1 
ATOM   1635 C C   . ARG A 1 204 ? 11.065  -9.722  25.713  1.00 33.29 ? 204 ARG A C   1 
ATOM   1636 O O   . ARG A 1 204 ? 11.248  -8.499  25.755  1.00 30.97 ? 204 ARG A O   1 
ATOM   1637 C CB  . ARG A 1 204 ? 10.269  -10.190 28.057  1.00 29.75 ? 204 ARG A CB  1 
ATOM   1638 C CG  . ARG A 1 204 ? 10.577  -10.765 29.403  1.00 31.49 ? 204 ARG A CG  1 
ATOM   1639 C CD  . ARG A 1 204 ? 10.747  -12.290 29.349  1.00 31.63 ? 204 ARG A CD  1 
ATOM   1640 N NE  . ARG A 1 204 ? 9.529   -13.032 28.994  1.00 31.84 ? 204 ARG A NE  1 
ATOM   1641 C CZ  . ARG A 1 204 ? 9.553   -14.298 28.584  1.00 37.38 ? 204 ARG A CZ  1 
ATOM   1642 N NH1 . ARG A 1 204 ? 10.693  -14.955 28.444  1.00 35.04 ? 204 ARG A NH1 1 
ATOM   1643 N NH2 . ARG A 1 204 ? 8.410   -14.926 28.304  1.00 32.35 ? 204 ARG A NH2 1 
ATOM   1644 N N   . LYS A 1 205 ? 10.827  -10.369 24.579  1.00 33.23 ? 205 LYS A N   1 
ATOM   1645 C CA  . LYS A 1 205 ? 10.703  -9.690  23.297  1.00 32.40 ? 205 LYS A CA  1 
ATOM   1646 C C   . LYS A 1 205 ? 9.262   -9.260  23.054  1.00 36.30 ? 205 LYS A C   1 
ATOM   1647 O O   . LYS A 1 205 ? 8.340   -10.094 23.071  1.00 35.36 ? 205 LYS A O   1 
ATOM   1648 C CB  . LYS A 1 205 ? 11.218  -10.604 22.191  1.00 37.71 ? 205 LYS A CB  1 
ATOM   1649 C CG  . LYS A 1 205 ? 12.756  -10.804 22.260  1.00 36.13 ? 205 LYS A CG  1 
ATOM   1650 C CD  . LYS A 1 205 ? 13.259  -11.657 21.113  1.00 41.07 ? 205 LYS A CD  1 
ATOM   1651 C CE  . LYS A 1 205 ? 14.746  -11.959 21.248  1.00 43.46 ? 205 LYS A CE  1 
ATOM   1652 N NZ  . LYS A 1 205 ? 14.955  -12.892 22.394  1.00 44.40 ? 205 LYS A NZ  1 
ATOM   1653 N N   . TYR A 1 206 ? 9.103   -7.960  22.886  1.00 35.63 ? 206 TYR A N   1 
ATOM   1654 C CA  . TYR A 1 206 ? 7.794   -7.340  22.619  1.00 38.32 ? 206 TYR A CA  1 
ATOM   1655 C C   . TYR A 1 206 ? 7.822   -6.731  21.228  1.00 37.61 ? 206 TYR A C   1 
ATOM   1656 O O   . TYR A 1 206 ? 8.711   -5.959  20.924  1.00 39.17 ? 206 TYR A O   1 
ATOM   1657 C CB  . TYR A 1 206 ? 7.510   -6.242  23.637  1.00 35.45 ? 206 TYR A CB  1 
ATOM   1658 C CG  . TYR A 1 206 ? 6.874   -6.754  24.894  1.00 32.42 ? 206 TYR A CG  1 
ATOM   1659 C CD1 . TYR A 1 206 ? 7.646   -7.301  25.893  1.00 32.66 ? 206 TYR A CD1 1 
ATOM   1660 C CD2 . TYR A 1 206 ? 5.510   -6.725  25.072  1.00 32.20 ? 206 TYR A CD2 1 
ATOM   1661 C CE1 . TYR A 1 206 ? 7.092   -7.781  27.057  1.00 31.72 ? 206 TYR A CE1 1 
ATOM   1662 C CE2 . TYR A 1 206 ? 4.936   -7.203  26.229  1.00 31.44 ? 206 TYR A CE2 1 
ATOM   1663 C CZ  . TYR A 1 206 ? 5.727   -7.746  27.222  1.00 33.36 ? 206 TYR A CZ  1 
ATOM   1664 O OH  . TYR A 1 206 ? 5.189   -8.232  28.366  1.00 27.30 ? 206 TYR A OH  1 
ATOM   1665 N N   . LYS A 1 207 ? 6.849   -7.087  20.409  1.00 38.69 ? 207 LYS A N   1 
ATOM   1666 C CA  . LYS A 1 207 ? 6.761   -6.442  19.084  1.00 45.31 ? 207 LYS A CA  1 
ATOM   1667 C C   . LYS A 1 207 ? 6.438   -4.976  19.336  1.00 46.72 ? 207 LYS A C   1 
ATOM   1668 O O   . LYS A 1 207 ? 5.573   -4.737  20.162  1.00 45.59 ? 207 LYS A O   1 
ATOM   1669 C CB  . LYS A 1 207 ? 5.650   -7.083  18.259  1.00 48.18 ? 207 LYS A CB  1 
ATOM   1670 C CG  . LYS A 1 207 ? 5.979   -8.472  17.740  1.00 47.58 ? 207 LYS A CG  1 
ATOM   1671 C CD  . LYS A 1 207 ? 5.356   -8.803  16.401  1.00 49.51 ? 207 LYS A CD  1 
ATOM   1672 C CE  . LYS A 1 207 ? 4.592   -7.667  15.762  1.00 49.17 ? 207 LYS A CE  1 
ATOM   1673 N NZ  . LYS A 1 207 ? 3.473   -7.225  16.618  1.00 52.25 ? 207 LYS A NZ  1 
ATOM   1674 N N   . PHE A 1 208 ? 7.105   -4.083  18.604  1.00 40.61 ? 208 PHE A N   1 
ATOM   1675 C CA  . PHE A 1 208 ? 6.973   -2.607  18.701  1.00 39.13 ? 208 PHE A CA  1 
ATOM   1676 C C   . PHE A 1 208 ? 5.538   -2.170  18.999  1.00 41.22 ? 208 PHE A C   1 
ATOM   1677 O O   . PHE A 1 208 ? 5.341   -1.498  19.982  1.00 38.65 ? 208 PHE A O   1 
ATOM   1678 C CB  . PHE A 1 208 ? 7.486   -1.951  17.421  1.00 41.31 ? 208 PHE A CB  1 
ATOM   1679 C CG  . PHE A 1 208 ? 8.944   -2.184  17.119  1.00 40.84 ? 208 PHE A CG  1 
ATOM   1680 C CD1 . PHE A 1 208 ? 9.823   -2.541  18.114  1.00 39.93 ? 208 PHE A CD1 1 
ATOM   1681 C CD2 . PHE A 1 208 ? 9.435   -2.047  15.837  1.00 39.02 ? 208 PHE A CD2 1 
ATOM   1682 C CE1 . PHE A 1 208 ? 11.161  -2.751  17.842  1.00 38.60 ? 208 PHE A CE1 1 
ATOM   1683 C CE2 . PHE A 1 208 ? 10.771  -2.265  15.565  1.00 40.48 ? 208 PHE A CE2 1 
ATOM   1684 C CZ  . PHE A 1 208 ? 11.633  -2.625  16.566  1.00 40.18 ? 208 PHE A CZ  1 
ATOM   1685 N N   . SER A 1 209 ? 4.575   -2.587  18.180  1.00 38.26 ? 209 SER A N   1 
ATOM   1686 C CA  . SER A 1 209 ? 3.155   -2.187  18.353  1.00 41.51 ? 209 SER A CA  1 
ATOM   1687 C C   . SER A 1 209 ? 2.552   -2.718  19.652  1.00 39.95 ? 209 SER A C   1 
ATOM   1688 O O   . SER A 1 209 ? 1.828   -1.989  20.296  1.00 40.91 ? 209 SER A O   1 
ATOM   1689 C CB  . SER A 1 209 ? 2.337   -2.582  17.162  1.00 42.06 ? 209 SER A CB  1 
ATOM   1690 O OG  . SER A 1 209 ? 2.115   -3.971  17.142  1.00 44.07 ? 209 SER A OG  1 
ATOM   1691 N N   . CYS A 1 210 ? 2.766   -3.988  19.939  1.00 41.55 ? 210 CYS A N   1 
ATOM   1692 C CA  . CYS A 1 210 ? 2.303   -4.648  21.179  1.00 41.58 ? 210 CYS A CA  1 
ATOM   1693 C C   . CYS A 1 210 ? 2.696   -3.839  22.396  1.00 37.24 ? 210 CYS A C   1 
ATOM   1694 O O   . CYS A 1 210 ? 1.823   -3.512  23.198  1.00 33.24 ? 210 CYS A O   1 
ATOM   1695 C CB  . CYS A 1 210 ? 2.868   -6.099  21.276  1.00 38.49 ? 210 CYS A CB  1 
ATOM   1696 S SG  . CYS A 1 210 ? 2.638   -6.976  22.743  1.00 42.69 ? 210 CYS A SG  1 
ATOM   1697 N N   . LEU A 1 211 ? 3.966   -3.419  22.520  1.00 36.69 ? 211 LEU A N   1 
ATOM   1698 C CA  . LEU A 1 211 ? 4.342   -2.630  23.695  1.00 37.03 ? 211 LEU A CA  1 
ATOM   1699 C C   . LEU A 1 211 ? 3.806   -1.206  23.587  1.00 33.04 ? 211 LEU A C   1 
ATOM   1700 O O   . LEU A 1 211 ? 3.185   -0.696  24.532  1.00 36.92 ? 211 LEU A O   1 
ATOM   1701 C CB  . LEU A 1 211 ? 5.876   -2.618  23.888  1.00 34.12 ? 211 LEU A CB  1 
ATOM   1702 C CG  . LEU A 1 211 ? 6.364   -2.166  25.274  1.00 33.19 ? 211 LEU A CG  1 
ATOM   1703 C CD1 . LEU A 1 211 ? 5.834   -3.040  26.385  1.00 32.04 ? 211 LEU A CD1 1 
ATOM   1704 C CD2 . LEU A 1 211 ? 7.889   -2.122  25.313  1.00 35.70 ? 211 LEU A CD2 1 
ATOM   1705 N N   . ASP A 1 212 ? 3.975   -0.575  22.413  1.00 34.74 ? 212 ASP A N   1 
ATOM   1706 C CA  . ASP A 1 212 ? 3.606   0.840   22.241  1.00 35.28 ? 212 ASP A CA  1 
ATOM   1707 C C   . ASP A 1 212 ? 2.146   1.088   22.597  1.00 35.57 ? 212 ASP A C   1 
ATOM   1708 O O   . ASP A 1 212 ? 1.807   2.077   23.269  1.00 35.87 ? 212 ASP A O   1 
ATOM   1709 C CB  . ASP A 1 212 ? 3.864   1.298   20.804  1.00 35.32 ? 212 ASP A CB  1 
ATOM   1710 C CG  . ASP A 1 212 ? 5.327   1.316   20.449  1.00 39.57 ? 212 ASP A CG  1 
ATOM   1711 O OD1 . ASP A 1 212 ? 6.167   1.452   21.364  1.00 39.82 ? 212 ASP A OD1 1 
ATOM   1712 O OD2 . ASP A 1 212 ? 5.646   1.236   19.243  1.00 40.38 ? 212 ASP A OD2 1 
ATOM   1713 N N   . ASN A 1 213 ? 1.273   0.197   22.156  1.00 36.37 ? 213 ASN A N   1 
ATOM   1714 C CA  . ASN A 1 213 ? -0.156  0.387   22.225  1.00 37.00 ? 213 ASN A CA  1 
ATOM   1715 C C   . ASN A 1 213 ? -0.776  -0.275  23.438  1.00 37.61 ? 213 ASN A C   1 
ATOM   1716 O O   . ASN A 1 213 ? -1.998  -0.231  23.594  1.00 33.49 ? 213 ASN A O   1 
ATOM   1717 C CB  . ASN A 1 213 ? -0.773  -0.134  20.924  1.00 39.29 ? 213 ASN A CB  1 
ATOM   1718 C CG  . ASN A 1 213 ? -0.352  0.717   19.712  1.00 41.16 ? 213 ASN A CG  1 
ATOM   1719 O OD1 . ASN A 1 213 ? -0.078  1.908   19.848  1.00 38.51 ? 213 ASN A OD1 1 
ATOM   1720 N ND2 . ASN A 1 213 ? -0.265  0.094   18.542  1.00 41.63 ? 213 ASN A ND2 1 
ATOM   1721 N N   . ALA A 1 214 ? 0.056   -0.799  24.337  1.00 37.54 ? 214 ALA A N   1 
ATOM   1722 C CA  . ALA A 1 214 ? -0.458  -1.513  25.527  1.00 35.88 ? 214 ALA A CA  1 
ATOM   1723 C C   . ALA A 1 214 ? -0.640  -0.599  26.739  1.00 35.16 ? 214 ALA A C   1 
ATOM   1724 O O   . ALA A 1 214 ? -0.765  -1.122  27.825  1.00 33.89 ? 214 ALA A O   1 
ATOM   1725 C CB  . ALA A 1 214 ? 0.414   -2.684  25.854  1.00 33.05 ? 214 ALA A CB  1 
ATOM   1726 N N   . ASN A 1 215 ? -0.707  0.713   26.547  1.00 36.41 ? 215 ASN A N   1 
ATOM   1727 C CA  . ASN A 1 215 ? -0.883  1.614   27.712  1.00 33.77 ? 215 ASN A CA  1 
ATOM   1728 C C   . ASN A 1 215 ? -2.032  2.592   27.460  1.00 35.95 ? 215 ASN A C   1 
ATOM   1729 O O   . ASN A 1 215 ? -1.995  3.677   27.989  1.00 32.97 ? 215 ASN A O   1 
ATOM   1730 C CB  . ASN A 1 215 ? 0.401   2.373   28.031  1.00 32.41 ? 215 ASN A CB  1 
ATOM   1731 C CG  . ASN A 1 215 ? 0.559   2.669   29.501  1.00 30.53 ? 215 ASN A CG  1 
ATOM   1732 O OD1 . ASN A 1 215 ? 0.103   1.921   30.346  1.00 31.30 ? 215 ASN A OD1 1 
ATOM   1733 N ND2 . ASN A 1 215 ? 1.191   3.777   29.807  1.00 29.79 ? 215 ASN A ND2 1 
ATOM   1734 N N   . LYS A 1 216 ? -3.049  2.175   26.719  1.00 40.61 ? 216 LYS A N   1 
ATOM   1735 C CA  . LYS A 1 216 ? -4.177  3.088   26.423  1.00 40.47 ? 216 LYS A CA  1 
ATOM   1736 C C   . LYS A 1 216 ? -4.820  3.551   27.731  1.00 35.75 ? 216 LYS A C   1 
ATOM   1737 O O   . LYS A 1 216 ? -5.012  2.744   28.607  1.00 35.76 ? 216 LYS A O   1 
ATOM   1738 C CB  . LYS A 1 216 ? -5.153  2.430   25.450  1.00 47.10 ? 216 LYS A CB  1 
ATOM   1739 C CG  . LYS A 1 216 ? -6.216  3.356   24.878  1.00 44.61 ? 216 LYS A CG  1 
ATOM   1740 C CD  . LYS A 1 216 ? -5.730  4.221   23.742  1.00 55.08 ? 216 LYS A CD  1 
ATOM   1741 C CE  . LYS A 1 216 ? -6.732  5.279   23.328  1.00 58.85 ? 216 LYS A CE  1 
ATOM   1742 N NZ  . LYS A 1 216 ? -6.470  5.800   21.969  1.00 52.97 ? 216 LYS A NZ  1 
ATOM   1743 N N   . GLY A 1 217 ? -5.105  4.840   27.850  1.00 37.57 ? 217 GLY A N   1 
ATOM   1744 C CA  . GLY A 1 217 ? -5.767  5.348   29.064  1.00 38.09 ? 217 GLY A CA  1 
ATOM   1745 C C   . GLY A 1 217 ? -4.776  5.818   30.106  1.00 38.81 ? 217 GLY A C   1 
ATOM   1746 O O   . GLY A 1 217 ? -5.215  6.264   31.166  1.00 40.46 ? 217 GLY A O   1 
ATOM   1747 N N   . TYR A 1 218 ? -3.484  5.678   29.804  1.00 35.89 ? 218 TYR A N   1 
ATOM   1748 C CA  . TYR A 1 218 ? -2.372  6.058   30.712  1.00 36.82 ? 218 TYR A CA  1 
ATOM   1749 C C   . TYR A 1 218 ? -1.355  6.906   29.938  1.00 33.15 ? 218 TYR A C   1 
ATOM   1750 O O   . TYR A 1 218 ? -1.451  6.965   28.722  1.00 34.24 ? 218 TYR A O   1 
ATOM   1751 C CB  . TYR A 1 218 ? -1.791  4.803   31.369  1.00 36.90 ? 218 TYR A CB  1 
ATOM   1752 C CG  . TYR A 1 218 ? -2.792  4.005   32.164  1.00 36.23 ? 218 TYR A CG  1 
ATOM   1753 C CD1 . TYR A 1 218 ? -3.543  3.016   31.574  1.00 35.56 ? 218 TYR A CD1 1 
ATOM   1754 C CD2 . TYR A 1 218 ? -3.021  4.274   33.496  1.00 36.99 ? 218 TYR A CD2 1 
ATOM   1755 C CE1 . TYR A 1 218 ? -4.479  2.300   32.288  1.00 33.05 ? 218 TYR A CE1 1 
ATOM   1756 C CE2 . TYR A 1 218 ? -3.947  3.563   34.234  1.00 37.66 ? 218 TYR A CE2 1 
ATOM   1757 C CZ  . TYR A 1 218 ? -4.672  2.565   33.625  1.00 36.57 ? 218 TYR A CZ  1 
ATOM   1758 O OH  . TYR A 1 218 ? -5.581  1.865   34.348  1.00 43.85 ? 218 TYR A OH  1 
ATOM   1759 N N   . ARG A 1 219 ? -0.398  7.514   30.638  1.00 34.75 ? 219 ARG A N   1 
ATOM   1760 C CA  . ARG A 1 219 ? 0.556   8.424   30.009  1.00 34.88 ? 219 ARG A CA  1 
ATOM   1761 C C   . ARG A 1 219 ? 1.261   7.766   28.828  1.00 36.05 ? 219 ARG A C   1 
ATOM   1762 O O   . ARG A 1 219 ? 1.798   6.652   28.932  1.00 37.72 ? 219 ARG A O   1 
ATOM   1763 C CB  . ARG A 1 219 ? 1.580   8.903   31.027  1.00 34.42 ? 219 ARG A CB  1 
ATOM   1764 C CG  . ARG A 1 219 ? 2.556   9.917   30.470  1.00 31.87 ? 219 ARG A CG  1 
ATOM   1765 C CD  . ARG A 1 219 ? 3.368   10.560  31.578  1.00 32.14 ? 219 ARG A CD  1 
ATOM   1766 N NE  . ARG A 1 219 ? 4.458   11.369  31.034  1.00 31.84 ? 219 ARG A NE  1 
ATOM   1767 C CZ  . ARG A 1 219 ? 5.167   12.213  31.763  1.00 30.85 ? 219 ARG A CZ  1 
ATOM   1768 N NH1 . ARG A 1 219 ? 4.933   12.365  33.052  1.00 30.50 ? 219 ARG A NH1 1 
ATOM   1769 N NH2 . ARG A 1 219 ? 6.136   12.919  31.187  1.00 29.98 ? 219 ARG A NH2 1 
ATOM   1770 N N   . GLN A 1 220 ? 1.286   8.479   27.709  1.00 32.18 ? 220 GLN A N   1 
ATOM   1771 C CA  . GLN A 1 220 ? 1.796   7.945   26.446  1.00 34.84 ? 220 GLN A CA  1 
ATOM   1772 C C   . GLN A 1 220 ? 3.282   8.300   26.269  1.00 35.84 ? 220 GLN A C   1 
ATOM   1773 O O   . GLN A 1 220 ? 3.681   9.037   25.367  1.00 36.61 ? 220 GLN A O   1 
ATOM   1774 C CB  . GLN A 1 220 ? 0.971   8.501   25.293  1.00 37.07 ? 220 GLN A CB  1 
ATOM   1775 C CG  . GLN A 1 220 ? -0.471  7.996   25.242  1.00 36.33 ? 220 GLN A CG  1 
ATOM   1776 C CD  . GLN A 1 220 ? -0.526  6.501   25.228  1.00 36.07 ? 220 GLN A CD  1 
ATOM   1777 O OE1 . GLN A 1 220 ? -0.302  5.893   24.200  1.00 35.53 ? 220 GLN A OE1 1 
ATOM   1778 N NE2 . GLN A 1 220 ? -0.876  5.899   26.354  1.00 38.89 ? 220 GLN A NE2 1 
ATOM   1779 N N   . ASN A 1 221 ? 4.130   7.708   27.105  1.00 33.06 ? 221 ASN A N   1 
ATOM   1780 C CA  . ASN A 1 221 ? 5.571   7.952   26.975  1.00 33.31 ? 221 ASN A CA  1 
ATOM   1781 C C   . ASN A 1 221 ? 6.353   6.690   27.301  1.00 30.56 ? 221 ASN A C   1 
ATOM   1782 O O   . ASN A 1 221 ? 5.823   5.746   27.893  1.00 33.37 ? 221 ASN A O   1 
ATOM   1783 C CB  . ASN A 1 221 ? 6.093   9.073   27.907  1.00 31.99 ? 221 ASN A CB  1 
ATOM   1784 C CG  . ASN A 1 221 ? 5.591   10.481  27.511  1.00 35.02 ? 221 ASN A CG  1 
ATOM   1785 O OD1 . ASN A 1 221 ? 4.767   11.067  28.206  1.00 31.63 ? 221 ASN A OD1 1 
ATOM   1786 N ND2 . ASN A 1 221 ? 6.135   11.024  26.432  1.00 29.58 ? 221 ASN A ND2 1 
ATOM   1787 N N   . TYR A 1 222 ? 7.613   6.685   26.876  1.00 29.97 ? 222 TYR A N   1 
ATOM   1788 C CA  . TYR A 1 222 ? 8.680   5.885   27.456  1.00 32.25 ? 222 TYR A CA  1 
ATOM   1789 C C   . TYR A 1 222 ? 9.650   6.835   28.160  1.00 36.37 ? 222 TYR A C   1 
ATOM   1790 O O   . TYR A 1 222 ? 9.562   8.061   28.015  1.00 31.84 ? 222 TYR A O   1 
ATOM   1791 C CB  . TYR A 1 222 ? 9.409   5.064   26.382  1.00 31.94 ? 222 TYR A CB  1 
ATOM   1792 C CG  . TYR A 1 222 ? 8.585   3.990   25.733  1.00 30.98 ? 222 TYR A CG  1 
ATOM   1793 C CD1 . TYR A 1 222 ? 7.618   3.286   26.451  1.00 31.97 ? 222 TYR A CD1 1 
ATOM   1794 C CD2 . TYR A 1 222 ? 8.757   3.679   24.389  1.00 34.39 ? 222 TYR A CD2 1 
ATOM   1795 C CE1 . TYR A 1 222 ? 6.839   2.294   25.849  1.00 33.20 ? 222 TYR A CE1 1 
ATOM   1796 C CE2 . TYR A 1 222 ? 8.008   2.652   23.776  1.00 34.55 ? 222 TYR A CE2 1 
ATOM   1797 C CZ  . TYR A 1 222 ? 7.047   1.979   24.506  1.00 34.70 ? 222 TYR A CZ  1 
ATOM   1798 O OH  . TYR A 1 222 ? 6.300   0.991   23.906  1.00 31.60 ? 222 TYR A OH  1 
ATOM   1799 N N   . TYR A 1 223 ? 10.604  6.270   28.915  1.00 30.45 ? 223 TYR A N   1 
ATOM   1800 C CA  . TYR A 1 223 ? 11.404  7.073   29.843  1.00 29.90 ? 223 TYR A CA  1 
ATOM   1801 C C   . TYR A 1 223 ? 12.900  6.751   29.690  1.00 30.84 ? 223 TYR A C   1 
ATOM   1802 O O   . TYR A 1 223 ? 13.424  5.758   30.222  1.00 28.77 ? 223 TYR A O   1 
ATOM   1803 C CB  . TYR A 1 223 ? 10.881  6.883   31.262  1.00 26.81 ? 223 TYR A CB  1 
ATOM   1804 C CG  . TYR A 1 223 ? 9.405   7.161   31.334  1.00 31.39 ? 223 TYR A CG  1 
ATOM   1805 C CD1 . TYR A 1 223 ? 8.937   8.464   31.325  1.00 30.96 ? 223 TYR A CD1 1 
ATOM   1806 C CD2 . TYR A 1 223 ? 8.471   6.129   31.356  1.00 26.51 ? 223 TYR A CD2 1 
ATOM   1807 C CE1 . TYR A 1 223 ? 7.590   8.737   31.351  1.00 30.38 ? 223 TYR A CE1 1 
ATOM   1808 C CE2 . TYR A 1 223 ? 7.110   6.390   31.393  1.00 28.65 ? 223 TYR A CE2 1 
ATOM   1809 C CZ  . TYR A 1 223 ? 6.675   7.694   31.376  1.00 30.92 ? 223 TYR A CZ  1 
ATOM   1810 O OH  . TYR A 1 223 ? 5.339   7.978   31.394  1.00 29.48 ? 223 TYR A OH  1 
ATOM   1811 N N   . VAL A 1 224 ? 13.583  7.585   28.910  1.00 29.40 ? 224 VAL A N   1 
ATOM   1812 C CA  . VAL A 1 224 ? 15.013  7.412   28.725  1.00 32.47 ? 224 VAL A CA  1 
ATOM   1813 C C   . VAL A 1 224 ? 15.717  7.735   30.036  1.00 30.22 ? 224 VAL A C   1 
ATOM   1814 O O   . VAL A 1 224 ? 15.387  8.724   30.711  1.00 31.35 ? 224 VAL A O   1 
ATOM   1815 C CB  . VAL A 1 224 ? 15.506  8.306   27.575  1.00 33.45 ? 224 VAL A CB  1 
ATOM   1816 C CG1 . VAL A 1 224 ? 17.002  8.203   27.405  1.00 32.82 ? 224 VAL A CG1 1 
ATOM   1817 C CG2 . VAL A 1 224 ? 14.765  7.943   26.279  1.00 32.38 ? 224 VAL A CG2 1 
ATOM   1818 N N   . VAL A 1 225 ? 16.652  6.881   30.422  1.00 26.67 ? 225 VAL A N   1 
ATOM   1819 C CA  . VAL A 1 225 ? 17.498  7.099   31.589  1.00 28.00 ? 225 VAL A CA  1 
ATOM   1820 C C   . VAL A 1 225 ? 18.878  7.552   31.116  1.00 30.14 ? 225 VAL A C   1 
ATOM   1821 O O   . VAL A 1 225 ? 19.539  6.848   30.331  1.00 25.78 ? 225 VAL A O   1 
ATOM   1822 C CB  . VAL A 1 225 ? 17.633  5.835   32.442  1.00 26.89 ? 225 VAL A CB  1 
ATOM   1823 C CG1 . VAL A 1 225 ? 18.371  6.174   33.743  1.00 21.69 ? 225 VAL A CG1 1 
ATOM   1824 C CG2 . VAL A 1 225 ? 16.243  5.206   32.712  1.00 21.68 ? 225 VAL A CG2 1 
ATOM   1825 N N   . CYS A 1 226 ? 19.331  8.726   31.612  1.00 28.01 ? 226 CYS A N   1 
ATOM   1826 C CA  . CYS A 1 226 ? 20.666  9.167   31.225  1.00 31.11 ? 226 CYS A CA  1 
ATOM   1827 C C   . CYS A 1 226 ? 21.364  9.856   32.396  1.00 28.49 ? 226 CYS A C   1 
ATOM   1828 O O   . CYS A 1 226 ? 20.723  10.167  33.408  1.00 28.04 ? 226 CYS A O   1 
ATOM   1829 C CB  . CYS A 1 226 ? 20.617  10.111  30.020  1.00 33.06 ? 226 CYS A CB  1 
ATOM   1830 S SG  . CYS A 1 226 ? 19.736  11.626  30.343  1.00 38.03 ? 226 CYS A SG  1 
ATOM   1831 N N   . PRO A 1 227 ? 22.673  10.121  32.301  1.00 29.72 ? 227 PRO A N   1 
ATOM   1832 C CA  . PRO A 1 227 ? 23.337  10.873  33.376  1.00 29.38 ? 227 PRO A CA  1 
ATOM   1833 C C   . PRO A 1 227 ? 22.830  12.292  33.441  1.00 29.68 ? 227 PRO A C   1 
ATOM   1834 O O   . PRO A 1 227 ? 22.543  12.907  32.420  1.00 30.31 ? 227 PRO A O   1 
ATOM   1835 C CB  . PRO A 1 227 ? 24.825  10.813  33.004  1.00 31.49 ? 227 PRO A CB  1 
ATOM   1836 C CG  . PRO A 1 227 ? 24.869  10.168  31.659  1.00 34.27 ? 227 PRO A CG  1 
ATOM   1837 C CD  . PRO A 1 227 ? 23.644  9.366   31.495  1.00 32.97 ? 227 PRO A CD  1 
ATOM   1838 N N   . ALA A 1 228 ? 22.656  12.786  34.659  1.00 30.26 ? 228 ALA A N   1 
ATOM   1839 C CA  . ALA A 1 228 ? 22.234  14.173  34.842  1.00 33.73 ? 228 ALA A CA  1 
ATOM   1840 C C   . ALA A 1 228 ? 23.400  15.079  34.525  1.00 38.64 ? 228 ALA A C   1 
ATOM   1841 O O   . ALA A 1 228 ? 24.536  14.718  34.842  1.00 37.07 ? 228 ALA A O   1 
ATOM   1842 C CB  . ALA A 1 228 ? 21.747  14.420  36.248  1.00 32.81 ? 228 ALA A CB  1 
ATOM   1843 O OXT . ALA A 1 228 ? 23.207  16.170  33.969  1.00 44.45 ? 228 ALA A OXT 1 
ATOM   1844 N N   . MET B 1 1   ? 47.905  -10.677 -8.469  1.00 55.43 ? 1   MET B N   1 
ATOM   1845 C CA  . MET B 1 1   ? 46.554  -10.103 -8.551  1.00 49.38 ? 1   MET B CA  1 
ATOM   1846 C C   . MET B 1 1   ? 46.606  -8.662  -8.045  1.00 46.47 ? 1   MET B C   1 
ATOM   1847 O O   . MET B 1 1   ? 47.118  -8.425  -6.955  1.00 53.10 ? 1   MET B O   1 
ATOM   1848 C CB  . MET B 1 1   ? 45.577  -10.908 -7.692  1.00 50.76 ? 1   MET B CB  1 
ATOM   1849 C CG  . MET B 1 1   ? 45.127  -12.257 -8.257  1.00 56.51 ? 1   MET B CG  1 
ATOM   1850 S SD  . MET B 1 1   ? 43.730  -12.161 -9.415  1.00 58.26 ? 1   MET B SD  1 
ATOM   1851 C CE  . MET B 1 1   ? 42.690  -13.450 -8.764  1.00 35.84 ? 1   MET B CE  1 
ATOM   1852 N N   . VAL B 1 2   ? 46.005  -7.715  -8.758  1.00 41.07 ? 2   VAL B N   1 
ATOM   1853 C CA  . VAL B 1 2   ? 46.083  -6.299  -8.376  1.00 39.08 ? 2   VAL B CA  1 
ATOM   1854 C C   . VAL B 1 2   ? 44.924  -5.974  -7.453  1.00 34.78 ? 2   VAL B C   1 
ATOM   1855 O O   . VAL B 1 2   ? 43.778  -6.331  -7.754  1.00 34.94 ? 2   VAL B O   1 
ATOM   1856 C CB  . VAL B 1 2   ? 46.049  -5.388  -9.609  1.00 39.80 ? 2   VAL B CB  1 
ATOM   1857 C CG1 . VAL B 1 2   ? 46.617  -4.013  -9.258  1.00 40.23 ? 2   VAL B CG1 1 
ATOM   1858 C CG2 . VAL B 1 2   ? 46.862  -6.000  -10.737 1.00 45.11 ? 2   VAL B CG2 1 
ATOM   1859 N N   . ARG B 1 3   ? 45.224  -5.339  -6.318  1.00 31.40 ? 3   ARG B N   1 
ATOM   1860 C CA  . ARG B 1 3   ? 44.240  -4.959  -5.312  1.00 33.95 ? 3   ARG B CA  1 
ATOM   1861 C C   . ARG B 1 3   ? 44.227  -3.454  -5.128  1.00 35.25 ? 3   ARG B C   1 
ATOM   1862 O O   . ARG B 1 3   ? 45.262  -2.786  -5.276  1.00 27.21 ? 3   ARG B O   1 
ATOM   1863 C CB  . ARG B 1 3   ? 44.510  -5.623  -3.938  1.00 35.24 ? 3   ARG B CB  1 
ATOM   1864 C CG  . ARG B 1 3   ? 45.081  -7.022  -4.051  1.00 40.47 ? 3   ARG B CG  1 
ATOM   1865 C CD  . ARG B 1 3   ? 45.915  -7.375  -2.836  1.00 45.13 ? 3   ARG B CD  1 
ATOM   1866 N NE  . ARG B 1 3   ? 45.208  -7.017  -1.619  1.00 47.84 ? 3   ARG B NE  1 
ATOM   1867 C CZ  . ARG B 1 3   ? 45.779  -6.832  -0.437  1.00 47.10 ? 3   ARG B CZ  1 
ATOM   1868 N NH1 . ARG B 1 3   ? 47.082  -6.951  -0.279  1.00 45.29 ? 3   ARG B NH1 1 
ATOM   1869 N NH2 . ARG B 1 3   ? 45.008  -6.558  0.622   1.00 43.74 ? 3   ARG B NH2 1 
ATOM   1870 N N   . PHE B 1 4   ? 43.050  -2.924  -4.760  1.00 27.53 ? 4   PHE B N   1 
ATOM   1871 C CA  . PHE B 1 4   ? 42.918  -1.500  -4.479  1.00 27.73 ? 4   PHE B CA  1 
ATOM   1872 C C   . PHE B 1 4   ? 42.221  -1.268  -3.145  1.00 26.18 ? 4   PHE B C   1 
ATOM   1873 O O   . PHE B 1 4   ? 41.200  -1.893  -2.847  1.00 24.45 ? 4   PHE B O   1 
ATOM   1874 C CB  . PHE B 1 4   ? 42.165  -0.801  -5.590  1.00 28.76 ? 4   PHE B CB  1 
ATOM   1875 C CG  . PHE B 1 4   ? 42.729  -1.057  -6.943  1.00 29.65 ? 4   PHE B CG  1 
ATOM   1876 C CD1 . PHE B 1 4   ? 43.742  -0.246  -7.452  1.00 28.25 ? 4   PHE B CD1 1 
ATOM   1877 C CD2 . PHE B 1 4   ? 42.225  -2.085  -7.735  1.00 30.26 ? 4   PHE B CD2 1 
ATOM   1878 C CE1 . PHE B 1 4   ? 44.270  -0.483  -8.740  1.00 28.16 ? 4   PHE B CE1 1 
ATOM   1879 C CE2 . PHE B 1 4   ? 42.751  -2.324  -9.007  1.00 30.79 ? 4   PHE B CE2 1 
ATOM   1880 C CZ  . PHE B 1 4   ? 43.771  -1.492  -9.508  1.00 29.83 ? 4   PHE B CZ  1 
ATOM   1881 N N   . SER B 1 5   ? 42.741  -0.335  -2.368  1.00 22.93 ? 5   SER B N   1 
ATOM   1882 C CA  . SER B 1 5   ? 42.245  -0.123  -1.024  1.00 24.74 ? 5   SER B CA  1 
ATOM   1883 C C   . SER B 1 5   ? 40.899  0.607   -1.059  1.00 24.62 ? 5   SER B C   1 
ATOM   1884 O O   . SER B 1 5   ? 40.491  1.183   -2.081  1.00 22.81 ? 5   SER B O   1 
ATOM   1885 C CB  . SER B 1 5   ? 43.262  0.686   -0.205  1.00 26.63 ? 5   SER B CB  1 
ATOM   1886 O OG  . SER B 1 5   ? 43.358  2.052   -0.696  1.00 25.56 ? 5   SER B OG  1 
ATOM   1887 N N   . ARG B 1 6   ? 40.208  0.576   0.078   1.00 25.11 ? 6   ARG B N   1 
ATOM   1888 C CA  . ARG B 1 6   ? 38.946  1.309   0.190   1.00 25.65 ? 6   ARG B CA  1 
ATOM   1889 C C   . ARG B 1 6   ? 39.147  2.787   -0.149  1.00 26.67 ? 6   ARG B C   1 
ATOM   1890 O O   . ARG B 1 6   ? 38.330  3.391   -0.866  1.00 26.70 ? 6   ARG B O   1 
ATOM   1891 C CB  . ARG B 1 6   ? 38.370  1.135   1.591   1.00 26.48 ? 6   ARG B CB  1 
ATOM   1892 C CG  . ARG B 1 6   ? 37.041  1.822   1.810   1.00 25.93 ? 6   ARG B CG  1 
ATOM   1893 C CD  . ARG B 1 6   ? 37.201  3.311   2.231   1.00 29.25 ? 6   ARG B CD  1 
ATOM   1894 N NE  . ARG B 1 6   ? 35.965  4.076   2.327   1.00 27.06 ? 6   ARG B NE  1 
ATOM   1895 C CZ  . ARG B 1 6   ? 35.917  5.368   2.648   1.00 29.26 ? 6   ARG B CZ  1 
ATOM   1896 N NH1 . ARG B 1 6   ? 37.020  6.072   2.891   1.00 24.50 ? 6   ARG B NH1 1 
ATOM   1897 N NH2 . ARG B 1 6   ? 34.742  5.968   2.741   1.00 24.95 ? 6   ARG B NH2 1 
ATOM   1898 N N   . ASP B 1 7   ? 40.283  3.368   0.285   1.00 23.81 ? 7   ASP B N   1 
ATOM   1899 C CA  . ASP B 1 7   ? 40.468  4.802   0.088   1.00 26.65 ? 7   ASP B CA  1 
ATOM   1900 C C   . ASP B 1 7   ? 40.606  5.140   -1.381  1.00 22.66 ? 7   ASP B C   1 
ATOM   1901 O O   . ASP B 1 7   ? 40.035  6.140   -1.842  1.00 22.13 ? 7   ASP B O   1 
ATOM   1902 C CB  . ASP B 1 7   ? 41.640  5.269   0.949   1.00 26.34 ? 7   ASP B CB  1 
ATOM   1903 C CG  . ASP B 1 7   ? 41.233  5.395   2.421   1.00 29.54 ? 7   ASP B CG  1 
ATOM   1904 O OD1 . ASP B 1 7   ? 39.999  5.537   2.729   1.00 29.38 ? 7   ASP B OD1 1 
ATOM   1905 O OD2 . ASP B 1 7   ? 42.123  5.289   3.280   1.00 27.54 ? 7   ASP B OD2 1 
ATOM   1906 N N   . MET B 1 8   ? 41.298  4.294   -2.142  1.00 22.18 ? 8   MET B N   1 
ATOM   1907 C CA  . MET B 1 8   ? 41.447  4.502   -3.585  1.00 20.79 ? 8   MET B CA  1 
ATOM   1908 C C   . MET B 1 8   ? 40.134  4.280   -4.313  1.00 22.89 ? 8   MET B C   1 
ATOM   1909 O O   . MET B 1 8   ? 39.808  4.974   -5.287  1.00 21.40 ? 8   MET B O   1 
ATOM   1910 C CB  . MET B 1 8   ? 42.495  3.557   -4.187  1.00 25.54 ? 8   MET B CB  1 
ATOM   1911 C CG  . MET B 1 8   ? 43.910  4.207   -4.232  1.00 26.79 ? 8   MET B CG  1 
ATOM   1912 S SD  . MET B 1 8   ? 44.519  4.686   -2.586  1.00 30.32 ? 8   MET B SD  1 
ATOM   1913 C CE  . MET B 1 8   ? 46.274  4.821   -2.918  1.00 30.42 ? 8   MET B CE  1 
ATOM   1914 N N   . LEU B 1 9   ? 39.370  3.293   -3.879  1.00 23.24 ? 9   LEU B N   1 
ATOM   1915 C CA  . LEU B 1 9   ? 38.066  3.081   -4.510  1.00 21.68 ? 9   LEU B CA  1 
ATOM   1916 C C   . LEU B 1 9   ? 37.125  4.258   -4.261  1.00 20.67 ? 9   LEU B C   1 
ATOM   1917 O O   . LEU B 1 9   ? 36.383  4.666   -5.171  1.00 21.61 ? 9   LEU B O   1 
ATOM   1918 C CB  . LEU B 1 9   ? 37.467  1.780   -3.975  1.00 20.31 ? 9   LEU B CB  1 
ATOM   1919 C CG  . LEU B 1 9   ? 38.295  0.566   -4.340  1.00 19.31 ? 9   LEU B CG  1 
ATOM   1920 C CD1 . LEU B 1 9   ? 37.940  -0.636  -3.453  1.00 25.57 ? 9   LEU B CD1 1 
ATOM   1921 C CD2 . LEU B 1 9   ? 38.127  0.228   -5.854  1.00 20.22 ? 9   LEU B CD2 1 
ATOM   1922 N N   . GLN B 1 10  ? 37.092  4.775   -3.019  1.00 20.80 ? 10  GLN B N   1 
ATOM   1923 C CA  . GLN B 1 10  ? 36.208  5.912   -2.705  1.00 22.09 ? 10  GLN B CA  1 
ATOM   1924 C C   . GLN B 1 10  ? 36.554  7.130   -3.558  1.00 23.06 ? 10  GLN B C   1 
ATOM   1925 O O   . GLN B 1 10  ? 35.673  7.831   -4.093  1.00 21.64 ? 10  GLN B O   1 
ATOM   1926 C CB  . GLN B 1 10  ? 36.351  6.262   -1.222  1.00 24.48 ? 10  GLN B CB  1 
ATOM   1927 C CG  . GLN B 1 10  ? 35.507  7.439   -0.732  1.00 23.94 ? 10  GLN B CG  1 
ATOM   1928 C CD  . GLN B 1 10  ? 34.002  7.208   -0.821  1.00 31.23 ? 10  GLN B CD  1 
ATOM   1929 O OE1 . GLN B 1 10  ? 33.532  6.114   -1.207  1.00 27.01 ? 10  GLN B OE1 1 
ATOM   1930 N NE2 . GLN B 1 10  ? 33.230  8.252   -0.464  1.00 31.26 ? 10  GLN B NE2 1 
ATOM   1931 N N   . ASP B 1 11  ? 37.855  7.401   -3.682  1.00 22.08 ? 11  ASP B N   1 
ATOM   1932 C CA  . ASP B 1 11  ? 38.313  8.511   -4.501  1.00 22.36 ? 11  ASP B CA  1 
ATOM   1933 C C   . ASP B 1 11  ? 38.038  8.281   -5.970  1.00 23.06 ? 11  ASP B C   1 
ATOM   1934 O O   . ASP B 1 11  ? 37.580  9.205   -6.653  1.00 21.65 ? 11  ASP B O   1 
ATOM   1935 C CB  . ASP B 1 11  ? 39.799  8.730   -4.316  1.00 24.12 ? 11  ASP B CB  1 
ATOM   1936 C CG  . ASP B 1 11  ? 40.365  9.711   -5.356  1.00 26.01 ? 11  ASP B CG  1 
ATOM   1937 O OD1 . ASP B 1 11  ? 40.195  10.928  -5.164  1.00 28.97 ? 11  ASP B OD1 1 
ATOM   1938 O OD2 . ASP B 1 11  ? 40.917  9.264   -6.390  1.00 27.50 ? 11  ASP B OD2 1 
ATOM   1939 N N   . GLY B 1 12  ? 38.310  7.066   -6.487  1.00 22.05 ? 12  GLY B N   1 
ATOM   1940 C CA  . GLY B 1 12  ? 38.019  6.817   -7.893  1.00 22.86 ? 12  GLY B CA  1 
ATOM   1941 C C   . GLY B 1 12  ? 36.534  6.996   -8.186  1.00 21.19 ? 12  GLY B C   1 
ATOM   1942 O O   . GLY B 1 12  ? 36.153  7.449   -9.271  1.00 22.72 ? 12  GLY B O   1 
ATOM   1943 N N   . ALA B 1 13  ? 35.679  6.653   -7.222  1.00 21.71 ? 13  ALA B N   1 
ATOM   1944 C CA  . ALA B 1 13  ? 34.225  6.800   -7.421  1.00 23.38 ? 13  ALA B CA  1 
ATOM   1945 C C   . ALA B 1 13  ? 33.856  8.279   -7.495  1.00 22.25 ? 13  ALA B C   1 
ATOM   1946 O O   . ALA B 1 13  ? 33.154  8.708   -8.417  1.00 23.15 ? 13  ALA B O   1 
ATOM   1947 C CB  . ALA B 1 13  ? 33.462  6.082   -6.294  1.00 18.54 ? 13  ALA B CB  1 
ATOM   1948 N N   . LYS B 1 14  ? 34.412  9.090   -6.604  1.00 24.45 ? 14  LYS B N   1 
ATOM   1949 C CA  . LYS B 1 14  ? 34.219  10.532  -6.721  1.00 26.75 ? 14  LYS B CA  1 
ATOM   1950 C C   . LYS B 1 14  ? 34.612  11.041  -8.104  1.00 26.70 ? 14  LYS B C   1 
ATOM   1951 O O   . LYS B 1 14  ? 33.899  11.855  -8.704  1.00 24.13 ? 14  LYS B O   1 
ATOM   1952 C CB  . LYS B 1 14  ? 35.043  11.262  -5.665  1.00 28.76 ? 14  LYS B CB  1 
ATOM   1953 C CG  . LYS B 1 14  ? 34.703  10.887  -4.258  1.00 30.63 ? 14  LYS B CG  1 
ATOM   1954 C CD  . LYS B 1 14  ? 35.392  11.867  -3.286  1.00 34.90 ? 14  LYS B CD  1 
ATOM   1955 C CE  . LYS B 1 14  ? 35.024  13.307  -3.617  1.00 33.70 ? 14  LYS B CE  1 
ATOM   1956 N NZ  . LYS B 1 14  ? 33.992  13.737  -2.647  1.00 34.40 ? 14  LYS B NZ  1 
ATOM   1957 N N   . ARG B 1 15  ? 35.773  10.609  -8.609  1.00 23.72 ? 15  ARG B N   1 
ATOM   1958 C CA  . ARG B 1 15  ? 36.239  11.118  -9.897  1.00 24.36 ? 15  ARG B CA  1 
ATOM   1959 C C   . ARG B 1 15  ? 35.345  10.654  -11.037 1.00 25.78 ? 15  ARG B C   1 
ATOM   1960 O O   . ARG B 1 15  ? 35.111  11.404  -12.002 1.00 23.19 ? 15  ARG B O   1 
ATOM   1961 C CB  . ARG B 1 15  ? 37.702  10.666  -10.135 1.00 27.83 ? 15  ARG B CB  1 
ATOM   1962 C CG  . ARG B 1 15  ? 38.740  11.483  -9.363  1.00 25.95 ? 15  ARG B CG  1 
ATOM   1963 C CD  . ARG B 1 15  ? 40.134  11.067  -9.854  1.00 29.30 ? 15  ARG B CD  1 
ATOM   1964 N NE  . ARG B 1 15  ? 40.568  9.832   -9.219  1.00 27.20 ? 15  ARG B NE  1 
ATOM   1965 C CZ  . ARG B 1 15  ? 41.059  8.800   -9.877  1.00 25.36 ? 15  ARG B CZ  1 
ATOM   1966 N NH1 . ARG B 1 15  ? 41.138  8.809   -11.190 1.00 29.04 ? 15  ARG B NH1 1 
ATOM   1967 N NH2 . ARG B 1 15  ? 41.436  7.723   -9.200  1.00 27.89 ? 15  ARG B NH2 1 
ATOM   1968 N N   . MET B 1 16  ? 34.836  9.415   -10.947 1.00 20.79 ? 16  MET B N   1 
ATOM   1969 C CA  . MET B 1 16  ? 33.853  8.925   -11.893 1.00 24.27 ? 16  MET B CA  1 
ATOM   1970 C C   . MET B 1 16  ? 32.599  9.792   -11.853 1.00 25.14 ? 16  MET B C   1 
ATOM   1971 O O   . MET B 1 16  ? 32.093  10.228  -12.888 1.00 26.69 ? 16  MET B O   1 
ATOM   1972 C CB  . MET B 1 16  ? 33.445  7.484   -11.511 1.00 23.97 ? 16  MET B CB  1 
ATOM   1973 C CG  . MET B 1 16  ? 34.271  6.298   -12.061 1.00 30.23 ? 16  MET B CG  1 
ATOM   1974 S SD  . MET B 1 16  ? 35.163  6.420   -13.594 1.00 27.26 ? 16  MET B SD  1 
ATOM   1975 C CE  . MET B 1 16  ? 33.990  5.628   -14.623 1.00 27.94 ? 16  MET B CE  1 
ATOM   1976 N N   . PHE B 1 17  ? 32.077  10.026  -10.647 1.00 25.73 ? 17  PHE B N   1 
ATOM   1977 C CA  . PHE B 1 17  ? 30.852  10.802  -10.460 1.00 25.56 ? 17  PHE B CA  1 
ATOM   1978 C C   . PHE B 1 17  ? 31.047  12.233  -10.963 1.00 26.39 ? 17  PHE B C   1 
ATOM   1979 O O   . PHE B 1 17  ? 30.208  12.767  -11.693 1.00 28.37 ? 17  PHE B O   1 
ATOM   1980 C CB  . PHE B 1 17  ? 30.497  10.795  -8.974  1.00 24.11 ? 17  PHE B CB  1 
ATOM   1981 C CG  . PHE B 1 17  ? 29.158  11.404  -8.643  1.00 24.99 ? 17  PHE B CG  1 
ATOM   1982 C CD1 . PHE B 1 17  ? 27.996  10.970  -9.265  1.00 26.02 ? 17  PHE B CD1 1 
ATOM   1983 C CD2 . PHE B 1 17  ? 29.073  12.454  -7.739  1.00 26.61 ? 17  PHE B CD2 1 
ATOM   1984 C CE1 . PHE B 1 17  ? 26.747  11.538  -8.931  1.00 28.42 ? 17  PHE B CE1 1 
ATOM   1985 C CE2 . PHE B 1 17  ? 27.809  13.024  -7.425  1.00 28.42 ? 17  PHE B CE2 1 
ATOM   1986 C CZ  . PHE B 1 17  ? 26.684  12.553  -8.013  1.00 26.52 ? 17  PHE B CZ  1 
ATOM   1987 N N   . LYS B 1 18  ? 32.194  12.837  -10.630 1.00 25.65 ? 18  LYS B N   1 
ATOM   1988 C CA  . LYS B 1 18  ? 32.508  14.186  -11.102 1.00 28.35 ? 18  LYS B CA  1 
ATOM   1989 C C   . LYS B 1 18  ? 32.588  14.219  -12.625 1.00 29.91 ? 18  LYS B C   1 
ATOM   1990 O O   . LYS B 1 18  ? 32.048  15.127  -13.264 1.00 29.91 ? 18  LYS B O   1 
ATOM   1991 C CB  . LYS B 1 18  ? 33.834  14.620  -10.473 1.00 32.00 ? 18  LYS B CB  1 
ATOM   1992 C CG  . LYS B 1 18  ? 33.990  16.062  -10.114 1.00 40.48 ? 18  LYS B CG  1 
ATOM   1993 C CD  . LYS B 1 18  ? 33.646  16.307  -8.629  1.00 48.33 ? 18  LYS B CD  1 
ATOM   1994 C CE  . LYS B 1 18  ? 34.887  16.419  -7.713  1.00 47.92 ? 18  LYS B CE  1 
ATOM   1995 N NZ  . LYS B 1 18  ? 34.532  16.598  -6.246  1.00 46.29 ? 18  LYS B NZ  1 
ATOM   1996 N N   . TRP B 1 19  ? 33.198  13.187  -13.223 1.00 29.10 ? 19  TRP B N   1 
ATOM   1997 C CA  . TRP B 1 19  ? 33.270  13.074  -14.676 1.00 31.05 ? 19  TRP B CA  1 
ATOM   1998 C C   . TRP B 1 19  ? 31.881  12.925  -15.257 1.00 31.36 ? 19  TRP B C   1 
ATOM   1999 O O   . TRP B 1 19  ? 31.487  13.697  -16.106 1.00 32.25 ? 19  TRP B O   1 
ATOM   2000 C CB  . TRP B 1 19  ? 34.152  11.882  -15.087 1.00 29.41 ? 19  TRP B CB  1 
ATOM   2001 C CG  . TRP B 1 19  ? 34.307  11.784  -16.561 1.00 31.04 ? 19  TRP B CG  1 
ATOM   2002 C CD1 . TRP B 1 19  ? 33.452  11.235  -17.452 1.00 31.73 ? 19  TRP B CD1 1 
ATOM   2003 C CD2 . TRP B 1 19  ? 35.416  12.271  -17.312 1.00 34.57 ? 19  TRP B CD2 1 
ATOM   2004 N NE1 . TRP B 1 19  ? 33.944  11.352  -18.720 1.00 30.91 ? 19  TRP B NE1 1 
ATOM   2005 C CE2 . TRP B 1 19  ? 35.154  11.990  -18.662 1.00 35.21 ? 19  TRP B CE2 1 
ATOM   2006 C CE3 . TRP B 1 19  ? 36.616  12.913  -16.966 1.00 32.49 ? 19  TRP B CE3 1 
ATOM   2007 C CZ2 . TRP B 1 19  ? 36.047  12.328  -19.678 1.00 33.62 ? 19  TRP B CZ2 1 
ATOM   2008 C CZ3 . TRP B 1 19  ? 37.502  13.249  -17.979 1.00 32.80 ? 19  TRP B CZ3 1 
ATOM   2009 C CH2 . TRP B 1 19  ? 37.205  12.959  -19.316 1.00 32.16 ? 19  TRP B CH2 1 
ATOM   2010 N N   . LEU B 1 20  ? 31.052  12.056  -14.713 1.00 30.40 ? 20  LEU B N   1 
ATOM   2011 C CA  . LEU B 1 20  ? 29.713  11.928  -15.308 1.00 30.76 ? 20  LEU B CA  1 
ATOM   2012 C C   . LEU B 1 20  ? 28.922  13.231  -15.244 1.00 31.77 ? 20  LEU B C   1 
ATOM   2013 O O   . LEU B 1 20  ? 28.089  13.504  -16.126 1.00 34.18 ? 20  LEU B O   1 
ATOM   2014 C CB  . LEU B 1 20  ? 28.965  10.829  -14.561 1.00 27.27 ? 20  LEU B CB  1 
ATOM   2015 C CG  . LEU B 1 20  ? 29.350  9.418   -14.968 1.00 26.11 ? 20  LEU B CG  1 
ATOM   2016 C CD1 . LEU B 1 20  ? 28.766  8.443   -13.985 1.00 25.66 ? 20  LEU B CD1 1 
ATOM   2017 C CD2 . LEU B 1 20  ? 28.897  9.103   -16.398 1.00 26.53 ? 20  LEU B CD2 1 
ATOM   2018 N N   . ARG B 1 21  ? 29.181  14.034  -14.224 1.00 32.03 ? 21  ARG B N   1 
ATOM   2019 C CA  . ARG B 1 21  ? 28.418  15.287  -14.016 1.00 35.53 ? 21  ARG B CA  1 
ATOM   2020 C C   . ARG B 1 21  ? 28.423  16.156  -15.275 1.00 38.06 ? 21  ARG B C   1 
ATOM   2021 O O   . ARG B 1 21  ? 27.484  16.876  -15.483 1.00 35.74 ? 21  ARG B O   1 
ATOM   2022 C CB  . ARG B 1 21  ? 28.959  16.057  -12.817 1.00 32.06 ? 21  ARG B CB  1 
ATOM   2023 C CG  . ARG B 1 21  ? 28.171  17.323  -12.547 1.00 34.66 ? 21  ARG B CG  1 
ATOM   2024 C CD  . ARG B 1 21  ? 29.040  18.330  -11.854 1.00 41.06 ? 21  ARG B CD  1 
ATOM   2025 N NE  . ARG B 1 21  ? 29.567  17.815  -10.612 1.00 40.01 ? 21  ARG B NE  1 
ATOM   2026 C CZ  . ARG B 1 21  ? 30.608  18.331  -9.988  1.00 44.64 ? 21  ARG B CZ  1 
ATOM   2027 N NH1 . ARG B 1 21  ? 31.242  19.365  -10.505 1.00 47.33 ? 21  ARG B NH1 1 
ATOM   2028 N NH2 . ARG B 1 21  ? 31.031  17.804  -8.863  1.00 44.60 ? 21  ARG B NH2 1 
ATOM   2029 N N   . LYS B 1 22  ? 29.421  15.970  -16.124 1.00 38.40 ? 22  LYS B N   1 
ATOM   2030 C CA  . LYS B 1 22  ? 29.569  16.749  -17.370 1.00 39.75 ? 22  LYS B CA  1 
ATOM   2031 C C   . LYS B 1 22  ? 28.518  16.327  -18.403 1.00 39.01 ? 22  LYS B C   1 
ATOM   2032 O O   . LYS B 1 22  ? 28.220  17.115  -19.276 1.00 39.62 ? 22  LYS B O   1 
ATOM   2033 C CB  . LYS B 1 22  ? 30.993  16.529  -17.883 1.00 44.42 ? 22  LYS B CB  1 
ATOM   2034 C CG  . LYS B 1 22  ? 32.080  16.692  -16.837 1.00 37.22 ? 22  LYS B CG  1 
ATOM   2035 C CD  . LYS B 1 22  ? 33.457  16.843  -17.416 1.00 45.74 ? 22  LYS B CD  1 
ATOM   2036 C CE  . LYS B 1 22  ? 34.166  15.516  -17.564 1.00 38.81 ? 22  LYS B CE  1 
ATOM   2037 N NZ  . LYS B 1 22  ? 35.470  15.626  -18.240 1.00 42.03 ? 22  LYS B NZ  1 
ATOM   2038 N N   . GLY B 1 23  ? 28.011  15.105  -18.320 1.00 40.40 ? 23  GLY B N   1 
ATOM   2039 C CA  . GLY B 1 23  ? 27.004  14.628  -19.277 1.00 40.70 ? 23  GLY B CA  1 
ATOM   2040 C C   . GLY B 1 23  ? 27.605  14.232  -20.602 1.00 39.51 ? 23  GLY B C   1 
ATOM   2041 O O   . GLY B 1 23  ? 26.894  14.274  -21.593 1.00 39.31 ? 23  GLY B O   1 
ATOM   2042 N N   . GLU B 1 24  ? 28.877  13.843  -20.604 1.00 43.89 ? 24  GLU B N   1 
ATOM   2043 C CA  . GLU B 1 24  ? 29.548  13.429  -21.852 1.00 44.26 ? 24  GLU B CA  1 
ATOM   2044 C C   . GLU B 1 24  ? 29.887  11.940  -21.776 1.00 41.77 ? 24  GLU B C   1 
ATOM   2045 O O   . GLU B 1 24  ? 30.810  11.519  -22.426 1.00 44.41 ? 24  GLU B O   1 
ATOM   2046 C CB  . GLU B 1 24  ? 30.766  14.305  -22.078 1.00 43.60 ? 24  GLU B CB  1 
ATOM   2047 C CG  . GLU B 1 24  ? 30.447  15.779  -21.942 1.00 49.00 ? 24  GLU B CG  1 
ATOM   2048 C CD  . GLU B 1 24  ? 31.052  16.636  -23.031 1.00 48.57 ? 24  GLU B CD  1 
ATOM   2049 O OE1 . GLU B 1 24  ? 31.838  16.096  -23.821 1.00 50.85 ? 24  GLU B OE1 1 
ATOM   2050 O OE2 . GLU B 1 24  ? 30.717  17.832  -23.096 1.00 48.63 ? 24  GLU B OE2 1 
ATOM   2051 N N   . GLY B 1 25  ? 29.168  11.187  -20.952 1.00 39.12 ? 25  GLY B N   1 
ATOM   2052 C CA  . GLY B 1 25  ? 29.400  9.743   -20.889 1.00 37.46 ? 25  GLY B CA  1 
ATOM   2053 C C   . GLY B 1 25  ? 30.524  9.394   -19.954 1.00 33.59 ? 25  GLY B C   1 
ATOM   2054 O O   . GLY B 1 25  ? 31.036  10.268  -19.307 1.00 35.27 ? 25  GLY B O   1 
ATOM   2055 N N   . LEU B 1 26  ? 30.881  8.128   -19.932 1.00 32.80 ? 26  LEU B N   1 
ATOM   2056 C CA  . LEU B 1 26  ? 31.934  7.595   -19.052 1.00 34.15 ? 26  LEU B CA  1 
ATOM   2057 C C   . LEU B 1 26  ? 33.334  7.864   -19.614 1.00 33.90 ? 26  LEU B C   1 
ATOM   2058 O O   . LEU B 1 26  ? 33.510  7.913   -20.830 1.00 35.30 ? 26  LEU B O   1 
ATOM   2059 C CB  . LEU B 1 26  ? 31.776  6.091   -18.873 1.00 32.49 ? 26  LEU B CB  1 
ATOM   2060 C CG  . LEU B 1 26  ? 30.584  5.561   -18.044 1.00 34.10 ? 26  LEU B CG  1 
ATOM   2061 C CD1 . LEU B 1 26  ? 30.372  4.089   -18.460 1.00 31.12 ? 26  LEU B CD1 1 
ATOM   2062 C CD2 . LEU B 1 26  ? 30.836  5.707   -16.527 1.00 32.21 ? 26  LEU B CD2 1 
ATOM   2063 N N   . PRO B 1 27  ? 34.352  7.971   -18.759 1.00 30.08 ? 27  PRO B N   1 
ATOM   2064 C CA  . PRO B 1 27  ? 35.719  8.176   -19.256 1.00 34.46 ? 27  PRO B CA  1 
ATOM   2065 C C   . PRO B 1 27  ? 36.267  6.921   -19.929 1.00 34.12 ? 27  PRO B C   1 
ATOM   2066 O O   . PRO B 1 27  ? 35.803  5.807   -19.725 1.00 30.10 ? 27  PRO B O   1 
ATOM   2067 C CB  . PRO B 1 27  ? 36.533  8.482   -17.990 1.00 32.59 ? 27  PRO B CB  1 
ATOM   2068 C CG  . PRO B 1 27  ? 35.772  7.774   -16.893 1.00 32.22 ? 27  PRO B CG  1 
ATOM   2069 C CD  . PRO B 1 27  ? 34.301  7.888   -17.295 1.00 31.89 ? 27  PRO B CD  1 
ATOM   2070 N N   . ASN B 1 28  ? 37.298  7.112   -20.737 1.00 34.92 ? 28  ASN B N   1 
ATOM   2071 C CA  . ASN B 1 28  ? 37.880  5.974   -21.439 1.00 35.34 ? 28  ASN B CA  1 
ATOM   2072 C C   . ASN B 1 28  ? 38.685  5.059   -20.511 1.00 34.94 ? 28  ASN B C   1 
ATOM   2073 O O   . ASN B 1 28  ? 38.972  3.912   -20.877 1.00 34.19 ? 28  ASN B O   1 
ATOM   2074 C CB  . ASN B 1 28  ? 38.784  6.467   -22.572 1.00 38.18 ? 28  ASN B CB  1 
ATOM   2075 C CG  . ASN B 1 28  ? 38.006  6.935   -23.782 1.00 36.46 ? 28  ASN B CG  1 
ATOM   2076 O OD1 . ASN B 1 28  ? 36.879  6.560   -23.988 1.00 40.12 ? 28  ASN B OD1 1 
ATOM   2077 N ND2 . ASN B 1 28  ? 38.665  7.724   -24.633 1.00 42.97 ? 28  ASN B ND2 1 
ATOM   2078 N N   . TYR B 1 29  ? 39.100  5.546   -19.346 1.00 30.22 ? 29  TYR B N   1 
ATOM   2079 C CA  . TYR B 1 29  ? 39.871  4.728   -18.430 1.00 29.13 ? 29  TYR B CA  1 
ATOM   2080 C C   . TYR B 1 29  ? 39.825  5.402   -17.077 1.00 29.21 ? 29  TYR B C   1 
ATOM   2081 O O   . TYR B 1 29  ? 39.371  6.539   -16.948 1.00 31.71 ? 29  TYR B O   1 
ATOM   2082 C CB  . TYR B 1 29  ? 41.331  4.554   -18.905 1.00 33.57 ? 29  TYR B CB  1 
ATOM   2083 C CG  . TYR B 1 29  ? 42.055  5.890   -19.149 1.00 33.15 ? 29  TYR B CG  1 
ATOM   2084 C CD1 . TYR B 1 29  ? 42.560  6.656   -18.085 1.00 31.83 ? 29  TYR B CD1 1 
ATOM   2085 C CD2 . TYR B 1 29  ? 42.166  6.407   -20.435 1.00 37.97 ? 29  TYR B CD2 1 
ATOM   2086 C CE1 . TYR B 1 29  ? 43.200  7.871   -18.303 1.00 34.66 ? 29  TYR B CE1 1 
ATOM   2087 C CE2 . TYR B 1 29  ? 42.849  7.641   -20.675 1.00 36.57 ? 29  TYR B CE2 1 
ATOM   2088 C CZ  . TYR B 1 29  ? 43.345  8.349   -19.598 1.00 37.19 ? 29  TYR B CZ  1 
ATOM   2089 O OH  . TYR B 1 29  ? 43.980  9.558   -19.817 1.00 41.08 ? 29  TYR B OH  1 
ATOM   2090 N N   . LEU B 1 30  ? 40.281  4.675   -16.057 1.00 30.36 ? 30  LEU B N   1 
ATOM   2091 C CA  . LEU B 1 30  ? 40.386  5.211   -14.705 1.00 29.28 ? 30  LEU B CA  1 
ATOM   2092 C C   . LEU B 1 30  ? 41.723  4.791   -14.133 1.00 30.70 ? 30  LEU B C   1 
ATOM   2093 O O   . LEU B 1 30  ? 41.990  3.598   -13.998 1.00 28.44 ? 30  LEU B O   1 
ATOM   2094 C CB  . LEU B 1 30  ? 39.241  4.713   -13.815 1.00 27.76 ? 30  LEU B CB  1 
ATOM   2095 C CG  . LEU B 1 30  ? 39.247  5.165   -12.356 1.00 27.01 ? 30  LEU B CG  1 
ATOM   2096 C CD1 . LEU B 1 30  ? 38.735  6.596   -12.284 1.00 27.80 ? 30  LEU B CD1 1 
ATOM   2097 C CD2 . LEU B 1 30  ? 38.296  4.213   -11.498 1.00 25.71 ? 30  LEU B CD2 1 
ATOM   2098 N N   . ILE B 1 31  ? 42.551  5.765   -13.783 1.00 30.16 ? 31  ILE B N   1 
ATOM   2099 C CA  . ILE B 1 31  ? 43.836  5.495   -13.168 1.00 30.71 ? 31  ILE B CA  1 
ATOM   2100 C C   . ILE B 1 31  ? 43.693  5.489   -11.653 1.00 27.79 ? 31  ILE B C   1 
ATOM   2101 O O   . ILE B 1 31  ? 43.089  6.397   -11.073 1.00 28.33 ? 31  ILE B O   1 
ATOM   2102 C CB  . ILE B 1 31  ? 44.883  6.527   -13.636 1.00 31.84 ? 31  ILE B CB  1 
ATOM   2103 C CG1 . ILE B 1 31  ? 44.826  6.643   -15.166 1.00 34.71 ? 31  ILE B CG1 1 
ATOM   2104 C CG2 . ILE B 1 31  ? 46.250  6.135   -13.157 1.00 31.61 ? 31  ILE B CG2 1 
ATOM   2105 C CD1 . ILE B 1 31  ? 46.111  7.198   -15.820 1.00 35.79 ? 31  ILE B CD1 1 
ATOM   2106 N N   . MET B 1 32  ? 44.217  4.445   -11.015 1.00 26.11 ? 32  MET B N   1 
ATOM   2107 C CA  . MET B 1 32  ? 44.284  4.336   -9.561  1.00 28.50 ? 32  MET B CA  1 
ATOM   2108 C C   . MET B 1 32  ? 45.601  3.686   -9.185  1.00 29.90 ? 32  MET B C   1 
ATOM   2109 O O   . MET B 1 32  ? 46.168  2.918   -9.963  1.00 28.65 ? 32  MET B O   1 
ATOM   2110 C CB  . MET B 1 32  ? 43.142  3.488   -8.941  1.00 29.99 ? 32  MET B CB  1 
ATOM   2111 C CG  . MET B 1 32  ? 41.725  3.965   -9.331  1.00 35.02 ? 32  MET B CG  1 
ATOM   2112 S SD  . MET B 1 32  ? 40.519  3.471   -8.142  1.00 36.89 ? 32  MET B SD  1 
ATOM   2113 C CE  . MET B 1 32  ? 41.166  2.033   -7.432  1.00 19.67 ? 32  MET B CE  1 
ATOM   2114 N N   . TYR B 1 33  ? 46.021  3.917   -7.941  1.00 26.40 ? 33  TYR B N   1 
ATOM   2115 C CA  . TYR B 1 33  ? 47.232  3.328   -7.399  1.00 31.53 ? 33  TYR B CA  1 
ATOM   2116 C C   . TYR B 1 33  ? 46.845  2.076   -6.618  1.00 31.72 ? 33  TYR B C   1 
ATOM   2117 O O   . TYR B 1 33  ? 45.976  2.147   -5.734  1.00 27.40 ? 33  TYR B O   1 
ATOM   2118 C CB  . TYR B 1 33  ? 47.947  4.312   -6.475  1.00 31.64 ? 33  TYR B CB  1 
ATOM   2119 C CG  . TYR B 1 33  ? 48.622  5.461   -7.230  1.00 32.48 ? 33  TYR B CG  1 
ATOM   2120 C CD1 . TYR B 1 33  ? 47.889  6.591   -7.608  1.00 28.35 ? 33  TYR B CD1 1 
ATOM   2121 C CD2 . TYR B 1 33  ? 49.968  5.378   -7.597  1.00 29.38 ? 33  TYR B CD2 1 
ATOM   2122 C CE1 . TYR B 1 33  ? 48.472  7.636   -8.312  1.00 29.81 ? 33  TYR B CE1 1 
ATOM   2123 C CE2 . TYR B 1 33  ? 50.574  6.415   -8.306  1.00 32.56 ? 33  TYR B CE2 1 
ATOM   2124 C CZ  . TYR B 1 33  ? 49.821  7.537   -8.661  1.00 34.09 ? 33  TYR B CZ  1 
ATOM   2125 O OH  . TYR B 1 33  ? 50.400  8.562   -9.371  1.00 30.82 ? 33  TYR B OH  1 
ATOM   2126 N N   . ASP B 1 34  ? 47.456  0.934   -6.983  1.00 30.17 ? 34  ASP B N   1 
ATOM   2127 C CA  . ASP B 1 34  ? 47.258  -0.330  -6.281  1.00 34.14 ? 34  ASP B CA  1 
ATOM   2128 C C   . ASP B 1 34  ? 47.757  -0.211  -4.846  1.00 34.16 ? 34  ASP B C   1 
ATOM   2129 O O   . ASP B 1 34  ? 48.622  0.618   -4.517  1.00 32.15 ? 34  ASP B O   1 
ATOM   2130 C CB  . ASP B 1 34  ? 47.957  -1.478  -7.011  1.00 37.36 ? 34  ASP B CB  1 
ATOM   2131 C CG  . ASP B 1 34  ? 49.374  -1.619  -6.598  1.00 40.14 ? 34  ASP B CG  1 
ATOM   2132 O OD1 . ASP B 1 34  ? 50.142  -0.783  -7.106  1.00 40.02 ? 34  ASP B OD1 1 
ATOM   2133 O OD2 . ASP B 1 34  ? 49.665  -2.517  -5.778  1.00 38.42 ? 34  ASP B OD2 1 
ATOM   2134 N N   . MET B 1 35  ? 47.211  -1.065  -3.985  1.00 30.13 ? 35  MET B N   1 
ATOM   2135 C CA  . MET B 1 35  ? 47.489  -0.963  -2.557  1.00 32.30 ? 35  MET B CA  1 
ATOM   2136 C C   . MET B 1 35  ? 48.776  -1.658  -2.129  1.00 35.07 ? 35  MET B C   1 
ATOM   2137 O O   . MET B 1 35  ? 49.228  -1.414  -0.992  1.00 33.83 ? 35  MET B O   1 
ATOM   2138 C CB  . MET B 1 35  ? 46.298  -1.504  -1.741  1.00 33.58 ? 35  MET B CB  1 
ATOM   2139 C CG  . MET B 1 35  ? 46.362  -2.910  -1.217  1.00 36.49 ? 35  MET B CG  1 
ATOM   2140 S SD  . MET B 1 35  ? 44.773  -3.254  -0.398  1.00 38.58 ? 35  MET B SD  1 
ATOM   2141 C CE  . MET B 1 35  ? 45.133  -2.923  1.278   1.00 33.72 ? 35  MET B CE  1 
ATOM   2142 N N   . ASP B 1 36  ? 49.347  -2.482  -3.001  1.00 36.02 ? 36  ASP B N   1 
ATOM   2143 C CA  . ASP B 1 36  ? 50.555  -3.264  -2.643  1.00 37.87 ? 36  ASP B CA  1 
ATOM   2144 C C   . ASP B 1 36  ? 51.832  -2.576  -3.129  1.00 40.72 ? 36  ASP B C   1 
ATOM   2145 O O   . ASP B 1 36  ? 52.714  -2.373  -2.323  1.00 43.20 ? 36  ASP B O   1 
ATOM   2146 C CB  . ASP B 1 36  ? 50.468  -4.664  -3.236  1.00 34.60 ? 36  ASP B CB  1 
ATOM   2147 C CG  . ASP B 1 36  ? 49.172  -5.358  -2.894  1.00 40.45 ? 36  ASP B CG  1 
ATOM   2148 O OD1 . ASP B 1 36  ? 48.941  -5.530  -1.712  1.00 40.79 ? 36  ASP B OD1 1 
ATOM   2149 O OD2 . ASP B 1 36  ? 48.438  -5.717  -3.814  1.00 35.76 ? 36  ASP B OD2 1 
ATOM   2150 N N   . ARG B 1 37  ? 51.915  -2.298  -4.428  1.00 40.74 ? 37  ARG B N   1 
ATOM   2151 C CA  . ARG B 1 37  ? 53.099  -1.694  -5.086  1.00 40.23 ? 37  ARG B CA  1 
ATOM   2152 C C   . ARG B 1 37  ? 53.047  -0.161  -5.073  1.00 42.43 ? 37  ARG B C   1 
ATOM   2153 O O   . ARG B 1 37  ? 54.066  0.454   -5.322  1.00 37.68 ? 37  ARG B O   1 
ATOM   2154 C CB  . ARG B 1 37  ? 53.104  -2.173  -6.538  1.00 43.29 ? 37  ARG B CB  1 
ATOM   2155 C CG  . ARG B 1 37  ? 53.192  -3.685  -6.686  1.00 55.84 ? 37  ARG B CG  1 
ATOM   2156 C CD  . ARG B 1 37  ? 52.627  -4.202  -7.994  1.00 53.92 ? 37  ARG B CD  1 
ATOM   2157 N NE  . ARG B 1 37  ? 51.782  -5.379  -7.842  1.00 61.76 ? 37  ARG B NE  1 
ATOM   2158 C CZ  . ARG B 1 37  ? 50.462  -5.346  -7.744  1.00 60.92 ? 37  ARG B CZ  1 
ATOM   2159 N NH1 . ARG B 1 37  ? 49.833  -4.188  -7.793  1.00 56.28 ? 37  ARG B NH1 1 
ATOM   2160 N NH2 . ARG B 1 37  ? 49.773  -6.462  -7.599  1.00 58.71 ? 37  ARG B NH2 1 
ATOM   2161 N N   . ASN B 1 38  ? 51.873  0.406   -4.820  1.00 41.72 ? 38  ASN B N   1 
ATOM   2162 C CA  . ASN B 1 38  ? 51.641  1.870   -4.850  1.00 37.79 ? 38  ASN B CA  1 
ATOM   2163 C C   . ASN B 1 38  ? 51.976  2.382   -6.240  1.00 39.66 ? 38  ASN B C   1 
ATOM   2164 O O   . ASN B 1 38  ? 52.558  3.438   -6.334  1.00 41.14 ? 38  ASN B O   1 
ATOM   2165 C CB  . ASN B 1 38  ? 52.338  2.636   -3.731  1.00 39.62 ? 38  ASN B CB  1 
ATOM   2166 C CG  . ASN B 1 38  ? 51.687  2.347   -2.407  1.00 45.79 ? 38  ASN B CG  1 
ATOM   2167 O OD1 . ASN B 1 38  ? 52.362  2.011   -1.446  1.00 48.52 ? 38  ASN B OD1 1 
ATOM   2168 N ND2 . ASN B 1 38  ? 50.368  2.437   -2.371  1.00 51.42 ? 38  ASN B ND2 1 
ATOM   2169 N N   . LYS B 1 39  ? 51.646  1.573   -7.241  1.00 46.73 ? 39  LYS B N   1 
ATOM   2170 C CA  . LYS B 1 39  ? 51.907  1.837   -8.674  1.00 40.54 ? 39  LYS B CA  1 
ATOM   2171 C C   . LYS B 1 39  ? 50.611  2.211   -9.407  1.00 36.74 ? 39  LYS B C   1 
ATOM   2172 O O   . LYS B 1 39  ? 49.564  1.726   -9.040  1.00 36.68 ? 39  LYS B O   1 
ATOM   2173 C CB  . LYS B 1 39  ? 52.511  0.565   -9.269  1.00 42.42 ? 39  LYS B CB  1 
ATOM   2174 C CG  . LYS B 1 39  ? 53.107  0.720   -10.654 1.00 51.02 ? 39  LYS B CG  1 
ATOM   2175 C CD  . LYS B 1 39  ? 53.011  -0.525  -11.520 1.00 50.14 ? 39  LYS B CD  1 
ATOM   2176 C CE  . LYS B 1 39  ? 54.146  -1.495  -11.291 1.00 56.68 ? 39  LYS B CE  1 
ATOM   2177 N NZ  . LYS B 1 39  ? 53.988  -2.728  -12.099 1.00 57.97 ? 39  LYS B NZ  1 
ATOM   2178 N N   . GLU B 1 40  ? 50.719  3.084   -10.396 1.00 35.31 ? 40  GLU B N   1 
ATOM   2179 C CA  . GLU B 1 40  ? 49.555  3.508   -11.201 1.00 36.84 ? 40  GLU B CA  1 
ATOM   2180 C C   . GLU B 1 40  ? 49.068  2.331   -12.046 1.00 36.52 ? 40  GLU B C   1 
ATOM   2181 O O   . GLU B 1 40  ? 49.905  1.659   -12.624 1.00 31.80 ? 40  GLU B O   1 
ATOM   2182 C CB  . GLU B 1 40  ? 49.992  4.576   -12.200 1.00 38.39 ? 40  GLU B CB  1 
ATOM   2183 C CG  . GLU B 1 40  ? 50.181  5.952   -11.617 1.00 39.37 ? 40  GLU B CG  1 
ATOM   2184 C CD  . GLU B 1 40  ? 50.112  7.058   -12.646 1.00 44.57 ? 40  GLU B CD  1 
ATOM   2185 O OE1 . GLU B 1 40  ? 50.028  6.751   -13.824 1.00 46.43 ? 40  GLU B OE1 1 
ATOM   2186 O OE2 . GLU B 1 40  ? 50.123  8.220   -12.248 1.00 49.16 ? 40  GLU B OE2 1 
ATOM   2187 N N   . TYR B 1 41  ? 47.755  2.122   -12.114 1.00 32.41 ? 41  TYR B N   1 
ATOM   2188 C CA  . TYR B 1 41  ? 47.159  1.091   -12.999 1.00 32.05 ? 41  TYR B CA  1 
ATOM   2189 C C   . TYR B 1 41  ? 46.043  1.755   -13.793 1.00 31.68 ? 41  TYR B C   1 
ATOM   2190 O O   . TYR B 1 41  ? 45.232  2.445   -13.212 1.00 30.50 ? 41  TYR B O   1 
ATOM   2191 C CB  . TYR B 1 41  ? 46.626  -0.114  -12.233 1.00 34.31 ? 41  TYR B CB  1 
ATOM   2192 C CG  . TYR B 1 41  ? 47.675  -1.097  -11.789 1.00 40.44 ? 41  TYR B CG  1 
ATOM   2193 C CD1 . TYR B 1 41  ? 48.535  -0.795  -10.752 1.00 43.11 ? 41  TYR B CD1 1 
ATOM   2194 C CD2 . TYR B 1 41  ? 47.806  -2.333  -12.390 1.00 40.00 ? 41  TYR B CD2 1 
ATOM   2195 C CE1 . TYR B 1 41  ? 49.505  -1.683  -10.322 1.00 44.97 ? 41  TYR B CE1 1 
ATOM   2196 C CE2 . TYR B 1 41  ? 48.768  -3.236  -11.970 1.00 43.88 ? 41  TYR B CE2 1 
ATOM   2197 C CZ  . TYR B 1 41  ? 49.628  -2.911  -10.938 1.00 48.60 ? 41  TYR B CZ  1 
ATOM   2198 O OH  . TYR B 1 41  ? 50.581  -3.792  -10.521 1.00 53.50 ? 41  TYR B OH  1 
ATOM   2199 N N   . LYS B 1 42  ? 46.044  1.517   -15.095 1.00 33.19 ? 42  LYS B N   1 
ATOM   2200 C CA  . LYS B 1 42  ? 45.074  2.124   -16.021 1.00 32.91 ? 42  LYS B CA  1 
ATOM   2201 C C   . LYS B 1 42  ? 43.983  1.102   -16.294 1.00 30.55 ? 42  LYS B C   1 
ATOM   2202 O O   . LYS B 1 42  ? 44.248  0.148   -16.995 1.00 31.06 ? 42  LYS B O   1 
ATOM   2203 C CB  . LYS B 1 42  ? 45.785  2.535   -17.310 1.00 35.01 ? 42  LYS B CB  1 
ATOM   2204 C CG  . LYS B 1 42  ? 44.910  3.107   -18.424 1.00 39.16 ? 42  LYS B CG  1 
ATOM   2205 C CD  . LYS B 1 42  ? 45.609  4.149   -19.289 1.00 38.08 ? 42  LYS B CD  1 
ATOM   2206 C CE  . LYS B 1 42  ? 44.699  4.723   -20.343 1.00 42.82 ? 42  LYS B CE  1 
ATOM   2207 N NZ  . LYS B 1 42  ? 45.300  4.843   -21.698 1.00 39.31 ? 42  LYS B NZ  1 
ATOM   2208 N N   . LEU B 1 43  ? 42.810  1.322   -15.720 1.00 29.30 ? 43  LEU B N   1 
ATOM   2209 C CA  . LEU B 1 43  ? 41.672  0.436   -15.937 1.00 25.48 ? 43  LEU B CA  1 
ATOM   2210 C C   . LEU B 1 43  ? 40.863  0.904   -17.142 1.00 28.52 ? 43  LEU B C   1 
ATOM   2211 O O   . LEU B 1 43  ? 40.390  2.054   -17.167 1.00 29.84 ? 43  LEU B O   1 
ATOM   2212 C CB  . LEU B 1 43  ? 40.809  0.393   -14.679 1.00 30.23 ? 43  LEU B CB  1 
ATOM   2213 C CG  . LEU B 1 43  ? 41.631  0.048   -13.447 1.00 31.91 ? 43  LEU B CG  1 
ATOM   2214 C CD1 . LEU B 1 43  ? 40.927  0.541   -12.191 1.00 28.45 ? 43  LEU B CD1 1 
ATOM   2215 C CD2 . LEU B 1 43  ? 41.942  -1.447  -13.366 1.00 31.74 ? 43  LEU B CD2 1 
ATOM   2216 N N   . VAL B 1 44  ? 40.644  0.005   -18.105 1.00 27.99 ? 44  VAL B N   1 
ATOM   2217 C CA  . VAL B 1 44  ? 39.750  0.246   -19.238 1.00 28.24 ? 44  VAL B CA  1 
ATOM   2218 C C   . VAL B 1 44  ? 38.319  0.081   -18.719 1.00 30.74 ? 44  VAL B C   1 
ATOM   2219 O O   . VAL B 1 44  ? 38.159  -0.328  -17.567 1.00 28.43 ? 44  VAL B O   1 
ATOM   2220 C CB  . VAL B 1 44  ? 40.060  -0.703  -20.401 1.00 31.74 ? 44  VAL B CB  1 
ATOM   2221 C CG1 . VAL B 1 44  ? 41.494  -0.455  -20.921 1.00 34.27 ? 44  VAL B CG1 1 
ATOM   2222 C CG2 . VAL B 1 44  ? 39.908  -2.139  -19.977 1.00 29.99 ? 44  VAL B CG2 1 
ATOM   2223 N N   . PRO B 1 45  ? 37.276  0.460   -19.470 1.00 30.75 ? 45  PRO B N   1 
ATOM   2224 C CA  . PRO B 1 45  ? 35.907  0.396   -18.909 1.00 30.98 ? 45  PRO B CA  1 
ATOM   2225 C C   . PRO B 1 45  ? 35.470  -0.979  -18.407 1.00 32.05 ? 45  PRO B C   1 
ATOM   2226 O O   . PRO B 1 45  ? 34.738  -1.039  -17.413 1.00 33.04 ? 45  PRO B O   1 
ATOM   2227 C CB  . PRO B 1 45  ? 35.029  0.855   -20.076 1.00 31.30 ? 45  PRO B CB  1 
ATOM   2228 C CG  . PRO B 1 45  ? 35.929  1.812   -20.873 1.00 32.72 ? 45  PRO B CG  1 
ATOM   2229 C CD  . PRO B 1 45  ? 37.352  1.356   -20.643 1.00 29.63 ? 45  PRO B CD  1 
ATOM   2230 N N   . LYS B 1 46  ? 35.842  -2.075  -19.085 1.00 33.35 ? 46  LYS B N   1 
ATOM   2231 C CA  . LYS B 1 46  ? 35.494  -3.414  -18.605 1.00 32.82 ? 46  LYS B CA  1 
ATOM   2232 C C   . LYS B 1 46  ? 36.056  -3.678  -17.214 1.00 32.00 ? 46  LYS B C   1 
ATOM   2233 O O   . LYS B 1 46  ? 35.429  -4.410  -16.423 1.00 28.07 ? 46  LYS B O   1 
ATOM   2234 C CB  . LYS B 1 46  ? 36.051  -4.482  -19.572 1.00 36.10 ? 46  LYS B CB  1 
ATOM   2235 C CG  . LYS B 1 46  ? 35.140  -4.732  -20.749 1.00 38.37 ? 46  LYS B CG  1 
ATOM   2236 C CD  . LYS B 1 46  ? 33.997  -5.673  -20.371 1.00 47.30 ? 46  LYS B CD  1 
ATOM   2237 C CE  . LYS B 1 46  ? 33.053  -5.925  -21.557 1.00 48.89 ? 46  LYS B CE  1 
ATOM   2238 N NZ  . LYS B 1 46  ? 32.331  -4.665  -21.946 1.00 44.89 ? 46  LYS B NZ  1 
ATOM   2239 N N   . GLU B 1 47  ? 37.248  -3.114  -16.914 1.00 27.49 ? 47  GLU B N   1 
ATOM   2240 C CA  . GLU B 1 47  ? 37.932  -3.339  -15.644 1.00 28.43 ? 47  GLU B CA  1 
ATOM   2241 C C   . GLU B 1 47  ? 37.396  -2.470  -14.529 1.00 30.42 ? 47  GLU B C   1 
ATOM   2242 O O   . GLU B 1 47  ? 37.265  -2.945  -13.390 1.00 26.91 ? 47  GLU B O   1 
ATOM   2243 C CB  . GLU B 1 47  ? 39.446  -3.092  -15.768 1.00 31.63 ? 47  GLU B CB  1 
ATOM   2244 C CG  . GLU B 1 47  ? 40.120  -4.013  -16.777 1.00 30.21 ? 47  GLU B CG  1 
ATOM   2245 C CD  . GLU B 1 47  ? 41.614  -3.694  -16.952 1.00 34.49 ? 47  GLU B CD  1 
ATOM   2246 O OE1 . GLU B 1 47  ? 41.930  -2.569  -17.374 1.00 28.92 ? 47  GLU B OE1 1 
ATOM   2247 O OE2 . GLU B 1 47  ? 42.432  -4.595  -16.708 1.00 30.45 ? 47  GLU B OE2 1 
ATOM   2248 N N   . TYR B 1 48  ? 37.159  -1.171  -14.789 1.00 25.68 ? 48  TYR B N   1 
ATOM   2249 C CA  . TYR B 1 48  ? 36.634  -0.394  -13.681 1.00 27.42 ? 48  TYR B CA  1 
ATOM   2250 C C   . TYR B 1 48  ? 35.165  -0.751  -13.405 1.00 24.33 ? 48  TYR B C   1 
ATOM   2251 O O   . TYR B 1 48  ? 34.746  -0.777  -12.246 1.00 26.12 ? 48  TYR B O   1 
ATOM   2252 C CB  . TYR B 1 48  ? 36.863  1.097   -13.911 1.00 22.72 ? 48  TYR B CB  1 
ATOM   2253 C CG  . TYR B 1 48  ? 36.199  1.832   -15.036 1.00 25.76 ? 48  TYR B CG  1 
ATOM   2254 C CD1 . TYR B 1 48  ? 34.810  1.935   -15.139 1.00 25.04 ? 48  TYR B CD1 1 
ATOM   2255 C CD2 . TYR B 1 48  ? 36.988  2.583   -15.940 1.00 28.50 ? 48  TYR B CD2 1 
ATOM   2256 C CE1 . TYR B 1 48  ? 34.208  2.706   -16.177 1.00 28.11 ? 48  TYR B CE1 1 
ATOM   2257 C CE2 . TYR B 1 48  ? 36.387  3.366   -16.988 1.00 30.08 ? 48  TYR B CE2 1 
ATOM   2258 C CZ  . TYR B 1 48  ? 35.013  3.439   -17.084 1.00 29.02 ? 48  TYR B CZ  1 
ATOM   2259 O OH  . TYR B 1 48  ? 34.459  4.200   -18.101 1.00 27.50 ? 48  TYR B OH  1 
ATOM   2260 N N   . ALA B 1 49  ? 34.410  -1.146  -14.428 1.00 25.61 ? 49  ALA B N   1 
ATOM   2261 C CA  . ALA B 1 49  ? 33.059  -1.660  -14.174 1.00 27.87 ? 49  ALA B CA  1 
ATOM   2262 C C   . ALA B 1 49  ? 33.066  -2.956  -13.347 1.00 26.26 ? 49  ALA B C   1 
ATOM   2263 O O   . ALA B 1 49  ? 32.205  -3.139  -12.482 1.00 22.96 ? 49  ALA B O   1 
ATOM   2264 C CB  . ALA B 1 49  ? 32.333  -1.880  -15.487 1.00 27.77 ? 49  ALA B CB  1 
ATOM   2265 N N   . GLY B 1 50  ? 34.010  -3.871  -13.615 1.00 25.26 ? 50  GLY B N   1 
ATOM   2266 C CA  . GLY B 1 50  ? 34.101  -5.098  -12.837 1.00 24.66 ? 50  GLY B CA  1 
ATOM   2267 C C   . GLY B 1 50  ? 34.581  -4.874  -11.418 1.00 25.60 ? 50  GLY B C   1 
ATOM   2268 O O   . GLY B 1 50  ? 34.115  -5.517  -10.474 1.00 21.63 ? 50  GLY B O   1 
ATOM   2269 N N   . LEU B 1 51  ? 35.549  -3.979  -11.246 1.00 22.10 ? 51  LEU B N   1 
ATOM   2270 C CA  . LEU B 1 51  ? 36.045  -3.687  -9.913  1.00 21.35 ? 51  LEU B CA  1 
ATOM   2271 C C   . LEU B 1 51  ? 34.940  -3.127  -9.040  1.00 23.53 ? 51  LEU B C   1 
ATOM   2272 O O   . LEU B 1 51  ? 34.757  -3.537  -7.875  1.00 21.41 ? 51  LEU B O   1 
ATOM   2273 C CB  . LEU B 1 51  ? 37.203  -2.678  -10.038 1.00 24.49 ? 51  LEU B CB  1 
ATOM   2274 C CG  . LEU B 1 51  ? 37.945  -2.312  -8.774  1.00 22.63 ? 51  LEU B CG  1 
ATOM   2275 C CD1 . LEU B 1 51  ? 38.757  -3.545  -8.286  1.00 25.06 ? 51  LEU B CD1 1 
ATOM   2276 C CD2 . LEU B 1 51  ? 38.847  -1.098  -9.133  1.00 17.97 ? 51  LEU B CD2 1 
ATOM   2277 N N   . TYR B 1 52  ? 34.189  -2.163  -9.588  1.00 20.79 ? 52  TYR B N   1 
ATOM   2278 C CA  . TYR B 1 52  ? 33.170  -1.545  -8.800  1.00 21.09 ? 52  TYR B CA  1 
ATOM   2279 C C   . TYR B 1 52  ? 31.947  -2.455  -8.674  1.00 20.70 ? 52  TYR B C   1 
ATOM   2280 O O   . TYR B 1 52  ? 31.259  -2.392  -7.659  1.00 20.53 ? 52  TYR B O   1 
ATOM   2281 C CB  . TYR B 1 52  ? 32.820  -0.176  -9.390  1.00 21.88 ? 52  TYR B CB  1 
ATOM   2282 C CG  . TYR B 1 52  ? 33.824  0.859   -8.922  1.00 20.09 ? 52  TYR B CG  1 
ATOM   2283 C CD1 . TYR B 1 52  ? 33.681  1.475   -7.685  1.00 20.06 ? 52  TYR B CD1 1 
ATOM   2284 C CD2 . TYR B 1 52  ? 35.003  1.105   -9.657  1.00 25.69 ? 52  TYR B CD2 1 
ATOM   2285 C CE1 . TYR B 1 52  ? 34.604  2.369   -7.216  1.00 20.44 ? 52  TYR B CE1 1 
ATOM   2286 C CE2 . TYR B 1 52  ? 35.932  1.993   -9.215  1.00 20.99 ? 52  TYR B CE2 1 
ATOM   2287 C CZ  . TYR B 1 52  ? 35.755  2.609   -7.974  1.00 22.02 ? 52  TYR B CZ  1 
ATOM   2288 O OH  . TYR B 1 52  ? 36.675  3.523   -7.535  1.00 21.99 ? 52  TYR B OH  1 
ATOM   2289 N N   . GLU B 1 53  ? 31.708  -3.329  -9.651  1.00 18.98 ? 53  GLU B N   1 
ATOM   2290 C CA  . GLU B 1 53  ? 30.719  -4.391  -9.445  1.00 22.55 ? 53  GLU B CA  1 
ATOM   2291 C C   . GLU B 1 53  ? 31.067  -5.199  -8.200  1.00 22.17 ? 53  GLU B C   1 
ATOM   2292 O O   . GLU B 1 53  ? 30.199  -5.423  -7.340  1.00 21.82 ? 53  GLU B O   1 
ATOM   2293 C CB  . GLU B 1 53  ? 30.617  -5.302  -10.696 1.00 21.50 ? 53  GLU B CB  1 
ATOM   2294 C CG  . GLU B 1 53  ? 29.632  -6.528  -10.543 1.00 22.73 ? 53  GLU B CG  1 
ATOM   2295 C CD  . GLU B 1 53  ? 29.646  -7.460  -11.733 1.00 26.30 ? 53  GLU B CD  1 
ATOM   2296 O OE1 . GLU B 1 53  ? 30.694  -8.058  -12.033 1.00 28.20 ? 53  GLU B OE1 1 
ATOM   2297 O OE2 . GLU B 1 53  ? 28.596  -7.586  -12.400 1.00 31.65 ? 53  GLU B OE2 1 
ATOM   2298 N N   . SER B 1 54  ? 32.343  -5.629  -8.073  1.00 21.61 ? 54  SER B N   1 
ATOM   2299 C CA  . SER B 1 54  ? 32.742  -6.441  -6.923  1.00 23.80 ? 54  SER B CA  1 
ATOM   2300 C C   . SER B 1 54  ? 32.657  -5.657  -5.641  1.00 22.64 ? 54  SER B C   1 
ATOM   2301 O O   . SER B 1 54  ? 32.243  -6.207  -4.614  1.00 23.77 ? 54  SER B O   1 
ATOM   2302 C CB  . SER B 1 54  ? 34.160  -7.007  -7.080  1.00 23.99 ? 54  SER B CB  1 
ATOM   2303 O OG  . SER B 1 54  ? 34.296  -7.438  -8.410  1.00 33.81 ? 54  SER B OG  1 
ATOM   2304 N N   . ARG B 1 55  ? 33.074  -4.379  -5.663  1.00 21.52 ? 55  ARG B N   1 
ATOM   2305 C CA  . ARG B 1 55  ? 32.883  -3.538  -4.492  1.00 18.85 ? 55  ARG B CA  1 
ATOM   2306 C C   . ARG B 1 55  ? 31.410  -3.501  -4.094  1.00 21.33 ? 55  ARG B C   1 
ATOM   2307 O O   . ARG B 1 55  ? 31.059  -3.616  -2.913  1.00 20.64 ? 55  ARG B O   1 
ATOM   2308 C CB  . ARG B 1 55  ? 33.397  -2.111  -4.762  1.00 21.21 ? 55  ARG B CB  1 
ATOM   2309 C CG  . ARG B 1 55  ? 33.272  -1.179  -3.602  1.00 20.64 ? 55  ARG B CG  1 
ATOM   2310 C CD  . ARG B 1 55  ? 33.297  0.310   -4.106  1.00 22.74 ? 55  ARG B CD  1 
ATOM   2311 N NE  . ARG B 1 55  ? 33.537  1.274   -3.043  1.00 22.46 ? 55  ARG B NE  1 
ATOM   2312 C CZ  . ARG B 1 55  ? 33.290  2.580   -3.139  1.00 22.44 ? 55  ARG B CZ  1 
ATOM   2313 N NH1 . ARG B 1 55  ? 32.784  3.123   -4.246  1.00 17.88 ? 55  ARG B NH1 1 
ATOM   2314 N NH2 . ARG B 1 55  ? 33.589  3.367   -2.115  1.00 23.77 ? 55  ARG B NH2 1 
ATOM   2315 N N   . ASN B 1 56  ? 30.531  -3.316  -5.072  1.00 22.70 ? 56  ASN B N   1 
ATOM   2316 C CA  . ASN B 1 56  ? 29.110  -3.094  -4.784  1.00 22.03 ? 56  ASN B CA  1 
ATOM   2317 C C   . ASN B 1 56  ? 28.433  -4.377  -4.249  1.00 21.86 ? 56  ASN B C   1 
ATOM   2318 O O   . ASN B 1 56  ? 27.545  -4.300  -3.388  1.00 20.68 ? 56  ASN B O   1 
ATOM   2319 C CB  . ASN B 1 56  ? 28.413  -2.582  -6.052  1.00 17.51 ? 56  ASN B CB  1 
ATOM   2320 C CG  . ASN B 1 56  ? 28.803  -1.148  -6.400  1.00 18.57 ? 56  ASN B CG  1 
ATOM   2321 O OD1 . ASN B 1 56  ? 29.357  -0.459  -5.567  1.00 20.23 ? 56  ASN B OD1 1 
ATOM   2322 N ND2 . ASN B 1 56  ? 28.449  -0.677  -7.609  1.00 18.82 ? 56  ASN B ND2 1 
ATOM   2323 N N   . ILE B 1 57  ? 28.845  -5.548  -4.744  1.00 21.30 ? 57  ILE B N   1 
ATOM   2324 C CA  . ILE B 1 57  ? 28.366  -6.830  -4.207  1.00 26.00 ? 57  ILE B CA  1 
ATOM   2325 C C   . ILE B 1 57  ? 28.642  -6.916  -2.708  1.00 26.37 ? 57  ILE B C   1 
ATOM   2326 O O   . ILE B 1 57  ? 27.746  -7.214  -1.896  1.00 25.38 ? 57  ILE B O   1 
ATOM   2327 C CB  . ILE B 1 57  ? 29.012  -8.016  -4.949  1.00 21.38 ? 57  ILE B CB  1 
ATOM   2328 C CG1 . ILE B 1 57  ? 28.482  -8.115  -6.385  1.00 23.63 ? 57  ILE B CG1 1 
ATOM   2329 C CG2 . ILE B 1 57  ? 28.713  -9.309  -4.211  1.00 21.74 ? 57  ILE B CG2 1 
ATOM   2330 C CD1 . ILE B 1 57  ? 29.253  -9.157  -7.274  1.00 22.51 ? 57  ILE B CD1 1 
ATOM   2331 N N   . PHE B 1 58  ? 29.881  -6.654  -2.314  1.00 20.33 ? 58  PHE B N   1 
ATOM   2332 C CA  . PHE B 1 58  ? 30.196  -6.710  -0.891  1.00 23.33 ? 58  PHE B CA  1 
ATOM   2333 C C   . PHE B 1 58  ? 29.413  -5.641  -0.116  1.00 23.91 ? 58  PHE B C   1 
ATOM   2334 O O   . PHE B 1 58  ? 28.842  -5.912  0.955   1.00 21.48 ? 58  PHE B O   1 
ATOM   2335 C CB  . PHE B 1 58  ? 31.703  -6.559  -0.687  1.00 22.83 ? 58  PHE B CB  1 
ATOM   2336 C CG  . PHE B 1 58  ? 32.154  -6.833  0.725   1.00 28.01 ? 58  PHE B CG  1 
ATOM   2337 C CD1 . PHE B 1 58  ? 31.977  -5.864  1.737   1.00 28.73 ? 58  PHE B CD1 1 
ATOM   2338 C CD2 . PHE B 1 58  ? 32.761  -8.034  1.051   1.00 28.06 ? 58  PHE B CD2 1 
ATOM   2339 C CE1 . PHE B 1 58  ? 32.395  -6.092  3.030   1.00 31.32 ? 58  PHE B CE1 1 
ATOM   2340 C CE2 . PHE B 1 58  ? 33.178  -8.270  2.345   1.00 31.81 ? 58  PHE B CE2 1 
ATOM   2341 C CZ  . PHE B 1 58  ? 33.012  -7.310  3.325   1.00 34.55 ? 58  PHE B CZ  1 
ATOM   2342 N N   . TRP B 1 59  ? 29.416  -4.409  -0.625  1.00 19.54 ? 59  TRP B N   1 
ATOM   2343 C CA  . TRP B 1 59  ? 28.706  -3.326  0.071   1.00 25.09 ? 59  TRP B CA  1 
ATOM   2344 C C   . TRP B 1 59  ? 27.228  -3.665  0.261   1.00 20.73 ? 59  TRP B C   1 
ATOM   2345 O O   . TRP B 1 59  ? 26.653  -3.469  1.344   1.00 23.26 ? 59  TRP B O   1 
ATOM   2346 C CB  . TRP B 1 59  ? 28.844  -2.030  -0.734  1.00 23.73 ? 59  TRP B CB  1 
ATOM   2347 C CG  . TRP B 1 59  ? 28.787  -0.781  0.085   1.00 26.07 ? 59  TRP B CG  1 
ATOM   2348 C CD1 . TRP B 1 59  ? 28.291  -0.634  1.359   1.00 26.20 ? 59  TRP B CD1 1 
ATOM   2349 C CD2 . TRP B 1 59  ? 29.283  0.518   -0.311  1.00 26.16 ? 59  TRP B CD2 1 
ATOM   2350 N NE1 . TRP B 1 59  ? 28.480  0.674   1.780   1.00 30.07 ? 59  TRP B NE1 1 
ATOM   2351 C CE2 . TRP B 1 59  ? 29.066  1.397   0.770   1.00 28.12 ? 59  TRP B CE2 1 
ATOM   2352 C CE3 . TRP B 1 59  ? 29.868  1.020   -1.483  1.00 24.10 ? 59  TRP B CE3 1 
ATOM   2353 C CZ2 . TRP B 1 59  ? 29.424  2.758   0.714   1.00 26.87 ? 59  TRP B CZ2 1 
ATOM   2354 C CZ3 . TRP B 1 59  ? 30.203  2.387   -1.539  1.00 25.59 ? 59  TRP B CZ3 1 
ATOM   2355 C CH2 . TRP B 1 59  ? 29.989  3.221   -0.449  1.00 23.37 ? 59  TRP B CH2 1 
ATOM   2356 N N   . ILE B 1 60  ? 26.584  -4.154  -0.791  1.00 21.37 ? 60  ILE B N   1 
ATOM   2357 C CA  . ILE B 1 60  ? 25.141  -4.400  -0.718  1.00 21.54 ? 60  ILE B CA  1 
ATOM   2358 C C   . ILE B 1 60  ? 24.818  -5.609  0.156   1.00 24.36 ? 60  ILE B C   1 
ATOM   2359 O O   . ILE B 1 60  ? 23.860  -5.588  0.940   1.00 25.66 ? 60  ILE B O   1 
ATOM   2360 C CB  . ILE B 1 60  ? 24.567  -4.545  -2.141  1.00 22.81 ? 60  ILE B CB  1 
ATOM   2361 C CG1 . ILE B 1 60  ? 24.708  -3.193  -2.894  1.00 22.04 ? 60  ILE B CG1 1 
ATOM   2362 C CG2 . ILE B 1 60  ? 23.104  -5.019  -2.093  1.00 26.54 ? 60  ILE B CG2 1 
ATOM   2363 C CD1 . ILE B 1 60  ? 24.365  -3.383  -4.419  1.00 21.29 ? 60  ILE B CD1 1 
ATOM   2364 N N   . LYS B 1 61  ? 25.582  -6.688  0.022   1.00 25.05 ? 61  LYS B N   1 
ATOM   2365 C CA  . LYS B 1 61  ? 25.331  -7.896  0.800   1.00 26.05 ? 61  LYS B CA  1 
ATOM   2366 C C   . LYS B 1 61  ? 25.705  -7.751  2.270   1.00 25.92 ? 61  LYS B C   1 
ATOM   2367 O O   . LYS B 1 61  ? 25.064  -8.373  3.131   1.00 26.32 ? 61  LYS B O   1 
ATOM   2368 C CB  . LYS B 1 61  ? 26.080  -9.061  0.202   1.00 23.95 ? 61  LYS B CB  1 
ATOM   2369 C CG  . LYS B 1 61  ? 25.606  -9.370  -1.196  1.00 28.85 ? 61  LYS B CG  1 
ATOM   2370 C CD  . LYS B 1 61  ? 24.076  -9.502  -1.298  1.00 28.62 ? 61  LYS B CD  1 
ATOM   2371 C CE  . LYS B 1 61  ? 23.604  -10.873 -0.829  1.00 27.43 ? 61  LYS B CE  1 
ATOM   2372 N NZ  . LYS B 1 61  ? 22.058  -10.961 -1.014  1.00 26.04 ? 61  LYS B NZ  1 
ATOM   2373 N N   . ASN B 1 62  ? 26.742  -6.985  2.587   1.00 23.57 ? 62  ASN B N   1 
ATOM   2374 C CA  . ASN B 1 62  ? 27.204  -6.906  3.961   1.00 21.72 ? 62  ASN B CA  1 
ATOM   2375 C C   . ASN B 1 62  ? 26.786  -5.624  4.669   1.00 25.74 ? 62  ASN B C   1 
ATOM   2376 O O   . ASN B 1 62  ? 26.988  -5.526  5.883   1.00 28.10 ? 62  ASN B O   1 
ATOM   2377 C CB  . ASN B 1 62  ? 28.737  -7.053  4.020   1.00 25.24 ? 62  ASN B CB  1 
ATOM   2378 C CG  . ASN B 1 62  ? 29.197  -8.456  3.562   1.00 26.85 ? 62  ASN B CG  1 
ATOM   2379 O OD1 . ASN B 1 62  ? 28.753  -9.451  4.098   1.00 28.21 ? 62  ASN B OD1 1 
ATOM   2380 N ND2 . ASN B 1 62  ? 30.070  -8.515  2.593   1.00 28.74 ? 62  ASN B ND2 1 
ATOM   2381 N N   . GLY B 1 63  ? 26.292  -4.616  3.950   1.00 26.41 ? 63  GLY B N   1 
ATOM   2382 C CA  . GLY B 1 63  ? 25.927  -3.341  4.586   1.00 25.08 ? 63  GLY B CA  1 
ATOM   2383 C C   . GLY B 1 63  ? 27.103  -2.459  5.002   1.00 26.28 ? 63  GLY B C   1 
ATOM   2384 O O   . GLY B 1 63  ? 26.900  -1.506  5.745   1.00 30.03 ? 63  GLY B O   1 
ATOM   2385 N N   . ARG B 1 64  ? 28.327  -2.753  4.570   1.00 24.79 ? 64  ARG B N   1 
ATOM   2386 C CA  . ARG B 1 64  ? 29.507  -1.931  4.860   1.00 30.58 ? 64  ARG B CA  1 
ATOM   2387 C C   . ARG B 1 64  ? 30.496  -2.133  3.726   1.00 27.69 ? 64  ARG B C   1 
ATOM   2388 O O   . ARG B 1 64  ? 30.389  -3.083  2.958   1.00 23.75 ? 64  ARG B O   1 
ATOM   2389 C CB  . ARG B 1 64  ? 30.146  -2.240  6.212   1.00 30.98 ? 64  ARG B CB  1 
ATOM   2390 C CG  . ARG B 1 64  ? 30.415  -3.690  6.421   1.00 32.08 ? 64  ARG B CG  1 
ATOM   2391 C CD  . ARG B 1 64  ? 31.554  -3.892  7.404   1.00 42.54 ? 64  ARG B CD  1 
ATOM   2392 N NE  . ARG B 1 64  ? 31.788  -5.324  7.525   1.00 48.86 ? 64  ARG B NE  1 
ATOM   2393 C CZ  . ARG B 1 64  ? 32.875  -5.942  7.086   1.00 44.47 ? 64  ARG B CZ  1 
ATOM   2394 N NH1 . ARG B 1 64  ? 33.865  -5.275  6.513   1.00 42.30 ? 64  ARG B NH1 1 
ATOM   2395 N NH2 . ARG B 1 64  ? 32.944  -7.271  7.166   1.00 42.49 ? 64  ARG B NH2 1 
ATOM   2396 N N   . GLU B 1 65  ? 31.400  -1.165  3.582   1.00 27.23 ? 65  GLU B N   1 
ATOM   2397 C CA  . GLU B 1 65  ? 32.362  -1.161  2.509   1.00 26.50 ? 65  GLU B CA  1 
ATOM   2398 C C   . GLU B 1 65  ? 33.423  -2.240  2.689   1.00 26.23 ? 65  GLU B C   1 
ATOM   2399 O O   . GLU B 1 65  ? 33.859  -2.518  3.810   1.00 28.61 ? 65  GLU B O   1 
ATOM   2400 C CB  . GLU B 1 65  ? 33.088  0.207   2.443   1.00 26.92 ? 65  GLU B CB  1 
ATOM   2401 C CG  . GLU B 1 65  ? 32.312  1.339   1.854   1.00 26.45 ? 65  GLU B CG  1 
ATOM   2402 C CD  . GLU B 1 65  ? 33.136  2.616   1.748   1.00 28.25 ? 65  GLU B CD  1 
ATOM   2403 O OE1 . GLU B 1 65  ? 34.110  2.605   0.983   1.00 26.95 ? 65  GLU B OE1 1 
ATOM   2404 O OE2 . GLU B 1 65  ? 32.816  3.628   2.427   1.00 29.29 ? 65  GLU B OE2 1 
ATOM   2405 N N   . PRO B 1 66  ? 33.904  -2.811  1.594   1.00 26.66 ? 66  PRO B N   1 
ATOM   2406 C CA  . PRO B 1 66  ? 35.080  -3.672  1.660   1.00 27.68 ? 66  PRO B CA  1 
ATOM   2407 C C   . PRO B 1 66  ? 36.328  -2.833  1.892   1.00 30.98 ? 66  PRO B C   1 
ATOM   2408 O O   . PRO B 1 66  ? 36.422  -1.693  1.419   1.00 29.77 ? 66  PRO B O   1 
ATOM   2409 C CB  . PRO B 1 66  ? 35.101  -4.351  0.287   1.00 28.80 ? 66  PRO B CB  1 
ATOM   2410 C CG  . PRO B 1 66  ? 34.412  -3.398  -0.616  1.00 25.28 ? 66  PRO B CG  1 
ATOM   2411 C CD  . PRO B 1 66  ? 33.363  -2.709  0.226   1.00 25.73 ? 66  PRO B CD  1 
ATOM   2412 N N   . ASN B 1 67  ? 37.230  -3.360  2.721   1.00 29.13 ? 67  ASN B N   1 
ATOM   2413 C CA  . ASN B 1 67  ? 38.514  -2.714  3.003   1.00 31.72 ? 67  ASN B CA  1 
ATOM   2414 C C   . ASN B 1 67  ? 39.422  -2.668  1.781   1.00 30.43 ? 67  ASN B C   1 
ATOM   2415 O O   . ASN B 1 67  ? 40.284  -1.779  1.684   1.00 28.01 ? 67  ASN B O   1 
ATOM   2416 C CB  . ASN B 1 67  ? 39.249  -3.474  4.108   1.00 35.79 ? 67  ASN B CB  1 
ATOM   2417 C CG  . ASN B 1 67  ? 38.617  -3.262  5.456   1.00 43.13 ? 67  ASN B CG  1 
ATOM   2418 O OD1 . ASN B 1 67  ? 37.967  -2.249  5.683   1.00 40.75 ? 67  ASN B OD1 1 
ATOM   2419 N ND2 . ASN B 1 67  ? 38.762  -4.252  6.355   1.00 49.82 ? 67  ASN B ND2 1 
ATOM   2420 N N   . TYR B 1 68  ? 39.215  -3.574  0.830   1.00 25.98 ? 68  TYR B N   1 
ATOM   2421 C CA  . TYR B 1 68  ? 39.921  -3.554  -0.431  1.00 26.20 ? 68  TYR B CA  1 
ATOM   2422 C C   . TYR B 1 68  ? 39.168  -4.449  -1.391  1.00 27.05 ? 68  TYR B C   1 
ATOM   2423 O O   . TYR B 1 68  ? 38.382  -5.312  -0.982  1.00 30.25 ? 68  TYR B O   1 
ATOM   2424 C CB  . TYR B 1 68  ? 41.376  -4.045  -0.259  1.00 28.79 ? 68  TYR B CB  1 
ATOM   2425 C CG  . TYR B 1 68  ? 41.487  -5.518  0.041   1.00 31.61 ? 68  TYR B CG  1 
ATOM   2426 C CD1 . TYR B 1 68  ? 41.445  -6.476  -0.981  1.00 32.71 ? 68  TYR B CD1 1 
ATOM   2427 C CD2 . TYR B 1 68  ? 41.624  -5.972  1.348   1.00 35.01 ? 68  TYR B CD2 1 
ATOM   2428 C CE1 . TYR B 1 68  ? 41.562  -7.837  -0.703  1.00 35.05 ? 68  TYR B CE1 1 
ATOM   2429 C CE2 . TYR B 1 68  ? 41.725  -7.344  1.633   1.00 33.67 ? 68  TYR B CE2 1 
ATOM   2430 C CZ  . TYR B 1 68  ? 41.693  -8.254  0.600   1.00 34.92 ? 68  TYR B CZ  1 
ATOM   2431 O OH  . TYR B 1 68  ? 41.805  -9.596  0.877   1.00 42.01 ? 68  TYR B OH  1 
ATOM   2432 N N   . VAL B 1 69  ? 39.380  -4.216  -2.679  1.00 23.58 ? 69  VAL B N   1 
ATOM   2433 C CA  . VAL B 1 69  ? 38.788  -5.063  -3.713  1.00 27.89 ? 69  VAL B CA  1 
ATOM   2434 C C   . VAL B 1 69  ? 39.917  -5.443  -4.646  1.00 29.26 ? 69  VAL B C   1 
ATOM   2435 O O   . VAL B 1 69  ? 40.725  -4.580  -5.029  1.00 25.80 ? 69  VAL B O   1 
ATOM   2436 C CB  . VAL B 1 69  ? 37.666  -4.348  -4.488  1.00 23.15 ? 69  VAL B CB  1 
ATOM   2437 C CG1 . VAL B 1 69  ? 37.100  -5.280  -5.573  1.00 23.61 ? 69  VAL B CG1 1 
ATOM   2438 C CG2 . VAL B 1 69  ? 36.588  -3.886  -3.531  1.00 22.80 ? 69  VAL B CG2 1 
ATOM   2439 N N   . THR B 1 70  ? 40.016  -6.730  -4.958  1.00 25.99 ? 70  THR B N   1 
ATOM   2440 C CA  . THR B 1 70  ? 41.002  -7.221  -5.905  1.00 29.98 ? 70  THR B CA  1 
ATOM   2441 C C   . THR B 1 70  ? 40.350  -7.310  -7.287  1.00 31.51 ? 70  THR B C   1 
ATOM   2442 O O   . THR B 1 70  ? 39.183  -7.682  -7.386  1.00 29.21 ? 70  THR B O   1 
ATOM   2443 C CB  . THR B 1 70  ? 41.552  -8.573  -5.408  1.00 31.47 ? 70  THR B CB  1 
ATOM   2444 O OG1 . THR B 1 70  ? 42.228  -8.342  -4.161  1.00 41.00 ? 70  THR B OG1 1 
ATOM   2445 C CG2 . THR B 1 70  ? 42.502  -9.189  -6.448  1.00 31.83 ? 70  THR B CG2 1 
ATOM   2446 N N   . LEU B 1 71  ? 41.067  -6.893  -8.346  1.00 29.95 ? 71  LEU B N   1 
ATOM   2447 C CA  . LEU B 1 71  ? 40.525  -6.961  -9.713  1.00 31.35 ? 71  LEU B CA  1 
ATOM   2448 C C   . LEU B 1 71  ? 40.530  -8.396  -10.226 1.00 33.81 ? 71  LEU B C   1 
ATOM   2449 O O   . LEU B 1 71  ? 41.587  -8.955  -10.530 1.00 28.66 ? 71  LEU B O   1 
ATOM   2450 C CB  . LEU B 1 71  ? 41.302  -6.057  -10.665 1.00 32.89 ? 71  LEU B CB  1 
ATOM   2451 C CG  . LEU B 1 71  ? 40.863  -6.065  -12.136 1.00 34.33 ? 71  LEU B CG  1 
ATOM   2452 C CD1 . LEU B 1 71  ? 39.598  -5.206  -12.370 1.00 32.67 ? 71  LEU B CD1 1 
ATOM   2453 C CD2 . LEU B 1 71  ? 41.986  -5.575  -13.042 1.00 36.16 ? 71  LEU B CD2 1 
ATOM   2454 N N   . THR B 1 72  ? 39.332  -8.988  -10.348 1.00 32.71 ? 72  THR B N   1 
ATOM   2455 C CA  . THR B 1 72  ? 39.182  -10.386 -10.732 1.00 35.41 ? 72  THR B CA  1 
ATOM   2456 C C   . THR B 1 72  ? 38.335  -10.592 -11.980 1.00 36.13 ? 72  THR B C   1 
ATOM   2457 O O   . THR B 1 72  ? 38.404  -11.673 -12.583 1.00 34.95 ? 72  THR B O   1 
ATOM   2458 C CB  . THR B 1 72  ? 38.551  -11.188 -9.574  1.00 35.87 ? 72  THR B CB  1 
ATOM   2459 O OG1 . THR B 1 72  ? 37.229  -10.675 -9.299  1.00 34.23 ? 72  THR B OG1 1 
ATOM   2460 C CG2 . THR B 1 72  ? 39.394  -11.058 -8.311  1.00 33.88 ? 72  THR B CG2 1 
ATOM   2461 N N   . SER B 1 73  ? 37.686  -9.684  -12.509 1.00 31.69 ? 73  SER B N   1 
ATOM   2462 C CA  . SER B 1 73  ? 36.536  -9.881  -13.381 1.00 32.59 ? 73  SER B CA  1 
ATOM   2463 C C   . SER B 1 73  ? 36.310  -8.617  -14.200 1.00 34.78 ? 73  SER B C   1 
ATOM   2464 O O   . SER B 1 73  ? 36.917  -7.574  -13.949 1.00 33.65 ? 73  SER B O   1 
ATOM   2465 C CB  . SER B 1 73  ? 35.284  -10.230 -12.574 1.00 30.00 ? 73  SER B CB  1 
ATOM   2466 O OG  . SER B 1 73  ? 34.909  -9.158  -11.726 1.00 30.00 ? 73  SER B OG  1 
ATOM   2467 N N   . VAL B 1 74  ? 35.484  -8.762  -15.230 1.00 36.58 ? 74  VAL B N   1 
ATOM   2468 C CA  . VAL B 1 74  ? 35.123  -7.634  -16.124 1.00 32.97 ? 74  VAL B CA  1 
ATOM   2469 C C   . VAL B 1 74  ? 33.607  -7.518  -16.158 1.00 37.13 ? 74  VAL B C   1 
ATOM   2470 O O   . VAL B 1 74  ? 32.938  -8.485  -15.827 1.00 32.50 ? 74  VAL B O   1 
ATOM   2471 C CB  . VAL B 1 74  ? 35.697  -7.807  -17.534 1.00 34.82 ? 74  VAL B CB  1 
ATOM   2472 C CG1 . VAL B 1 74  ? 37.212  -7.782  -17.520 1.00 34.09 ? 74  VAL B CG1 1 
ATOM   2473 C CG2 . VAL B 1 74  ? 35.183  -9.068  -18.190 1.00 36.87 ? 74  VAL B CG2 1 
ATOM   2474 N N   . ALA B 1 75  ? 33.123  -6.341  -16.536 1.00 33.55 ? 75  ALA B N   1 
ATOM   2475 C CA  . ALA B 1 75  ? 31.675  -6.095  -16.618 1.00 37.88 ? 75  ALA B CA  1 
ATOM   2476 C C   . ALA B 1 75  ? 31.408  -4.890  -17.523 1.00 37.33 ? 75  ALA B C   1 
ATOM   2477 O O   . ALA B 1 75  ? 32.241  -4.010  -17.608 1.00 36.61 ? 75  ALA B O   1 
ATOM   2478 C CB  . ALA B 1 75  ? 31.083  -5.927  -15.244 1.00 31.92 ? 75  ALA B CB  1 
ATOM   2479 N N   . ARG B 1 76  ? 30.227  -4.918  -18.111 1.00 45.69 ? 76  ARG B N   1 
ATOM   2480 C CA  . ARG B 1 76  ? 29.734  -3.846  -18.994 1.00 43.52 ? 76  ARG B CA  1 
ATOM   2481 C C   . ARG B 1 76  ? 29.372  -2.651  -18.122 1.00 34.69 ? 76  ARG B C   1 
ATOM   2482 O O   . ARG B 1 76  ? 29.413  -1.551  -18.608 1.00 38.48 ? 76  ARG B O   1 
ATOM   2483 C CB  . ARG B 1 76  ? 28.526  -4.384  -19.755 1.00 46.79 ? 76  ARG B CB  1 
ATOM   2484 C CG  . ARG B 1 76  ? 28.876  -5.558  -20.650 1.00 57.40 ? 76  ARG B CG  1 
ATOM   2485 C CD  . ARG B 1 76  ? 27.832  -5.999  -21.653 1.00 61.42 ? 76  ARG B CD  1 
ATOM   2486 N NE  . ARG B 1 76  ? 27.397  -7.366  -21.425 1.00 65.16 ? 76  ARG B NE  1 
ATOM   2487 C CZ  . ARG B 1 76  ? 26.702  -8.117  -22.271 1.00 68.95 ? 76  ARG B CZ  1 
ATOM   2488 N NH1 . ARG B 1 76  ? 26.351  -9.342  -21.918 1.00 60.05 ? 76  ARG B NH1 1 
ATOM   2489 N NH2 . ARG B 1 76  ? 26.374  -7.658  -23.469 1.00 70.82 ? 76  ARG B NH2 1 
ATOM   2490 N N   . ASN B 1 77  ? 29.032  -2.907  -16.867 1.00 31.46 ? 77  ASN B N   1 
ATOM   2491 C CA  . ASN B 1 77  ? 28.628  -1.839  -15.919 1.00 28.47 ? 77  ASN B CA  1 
ATOM   2492 C C   . ASN B 1 77  ? 28.768  -2.362  -14.490 1.00 25.24 ? 77  ASN B C   1 
ATOM   2493 O O   . ASN B 1 77  ? 28.866  -3.545  -14.322 1.00 25.36 ? 77  ASN B O   1 
ATOM   2494 C CB  . ASN B 1 77  ? 27.234  -1.281  -16.223 1.00 27.50 ? 77  ASN B CB  1 
ATOM   2495 C CG  . ASN B 1 77  ? 26.130  -2.292  -16.026 1.00 29.57 ? 77  ASN B CG  1 
ATOM   2496 O OD1 . ASN B 1 77  ? 26.018  -2.889  -14.983 1.00 27.97 ? 77  ASN B OD1 1 
ATOM   2497 N ND2 . ASN B 1 77  ? 25.343  -2.512  -17.048 1.00 28.89 ? 77  ASN B ND2 1 
ATOM   2498 N N   . PRO B 1 78  ? 28.776  -1.497  -13.466 1.00 26.18 ? 78  PRO B N   1 
ATOM   2499 C CA  . PRO B 1 78  ? 28.935  -1.947  -12.105 1.00 26.28 ? 78  PRO B CA  1 
ATOM   2500 C C   . PRO B 1 78  ? 27.620  -2.243  -11.373 1.00 26.44 ? 78  PRO B C   1 
ATOM   2501 O O   . PRO B 1 78  ? 27.658  -2.383  -10.208 1.00 21.95 ? 78  PRO B O   1 
ATOM   2502 C CB  . PRO B 1 78  ? 29.593  -0.724  -11.477 1.00 22.38 ? 78  PRO B CB  1 
ATOM   2503 C CG  . PRO B 1 78  ? 28.954  0.431   -12.182 1.00 25.05 ? 78  PRO B CG  1 
ATOM   2504 C CD  . PRO B 1 78  ? 28.654  -0.059  -13.573 1.00 25.12 ? 78  PRO B CD  1 
ATOM   2505 N N   . LEU B 1 79  ? 26.520  -2.380  -12.102 1.00 21.85 ? 79  LEU B N   1 
ATOM   2506 C CA  . LEU B 1 79  ? 25.210  -2.606  -11.445 1.00 24.53 ? 79  LEU B CA  1 
ATOM   2507 C C   . LEU B 1 79  ? 25.085  -3.980  -10.779 1.00 24.39 ? 79  LEU B C   1 
ATOM   2508 O O   . LEU B 1 79  ? 25.339  -4.963  -11.409 1.00 25.83 ? 79  LEU B O   1 
ATOM   2509 C CB  . LEU B 1 79  ? 24.081  -2.455  -12.452 1.00 25.12 ? 79  LEU B CB  1 
ATOM   2510 C CG  . LEU B 1 79  ? 22.713  -2.608  -11.811 1.00 23.90 ? 79  LEU B CG  1 
ATOM   2511 C CD1 . LEU B 1 79  ? 22.437  -1.444  -10.895 1.00 19.92 ? 79  LEU B CD1 1 
ATOM   2512 C CD2 . LEU B 1 79  ? 21.651  -2.727  -12.868 1.00 26.09 ? 79  LEU B CD2 1 
ATOM   2513 N N   . VAL B 1 80  ? 24.698  -3.980  -9.516  1.00 20.71 ? 80  VAL B N   1 
ATOM   2514 C CA  . VAL B 1 80  ? 24.411  -5.210  -8.780  1.00 22.45 ? 80  VAL B CA  1 
ATOM   2515 C C   . VAL B 1 80  ? 22.933  -5.186  -8.388  1.00 24.42 ? 80  VAL B C   1 
ATOM   2516 O O   . VAL B 1 80  ? 22.463  -4.208  -7.788  1.00 21.33 ? 80  VAL B O   1 
ATOM   2517 C CB  . VAL B 1 80  ? 25.309  -5.309  -7.539  1.00 21.51 ? 80  VAL B CB  1 
ATOM   2518 C CG1 . VAL B 1 80  ? 24.914  -6.509  -6.682  1.00 23.89 ? 80  VAL B CG1 1 
ATOM   2519 C CG2 . VAL B 1 80  ? 26.817  -5.364  -7.986  1.00 21.91 ? 80  VAL B CG2 1 
ATOM   2520 N N   . MET B 1 81  ? 22.198  -6.246  -8.749  1.00 23.20 ? 81  MET B N   1 
ATOM   2521 C CA  . MET B 1 81  ? 20.770  -6.321  -8.416  1.00 21.70 ? 81  MET B CA  1 
ATOM   2522 C C   . MET B 1 81  ? 20.588  -6.157  -6.915  1.00 23.52 ? 81  MET B C   1 
ATOM   2523 O O   . MET B 1 81  ? 21.316  -6.771  -6.114  1.00 24.69 ? 81  MET B O   1 
ATOM   2524 C CB  . MET B 1 81  ? 20.154  -7.668  -8.835  1.00 25.73 ? 81  MET B CB  1 
ATOM   2525 C CG  . MET B 1 81  ? 18.609  -7.692  -8.843  1.00 27.06 ? 81  MET B CG  1 
ATOM   2526 S SD  . MET B 1 81  ? 17.781  -6.129  -9.284  1.00 26.47 ? 81  MET B SD  1 
ATOM   2527 C CE  . MET B 1 81  ? 16.091  -6.488  -8.789  1.00 26.60 ? 81  MET B CE  1 
ATOM   2528 N N   . ASP B 1 82  ? 19.633  -5.312  -6.538  1.00 18.11 ? 82  ASP B N   1 
ATOM   2529 C CA  . ASP B 1 82  ? 19.305  -5.022  -5.155  1.00 22.03 ? 82  ASP B CA  1 
ATOM   2530 C C   . ASP B 1 82  ? 17.780  -5.012  -5.051  1.00 25.02 ? 82  ASP B C   1 
ATOM   2531 O O   . ASP B 1 82  ? 17.131  -4.321  -5.829  1.00 23.95 ? 82  ASP B O   1 
ATOM   2532 C CB  . ASP B 1 82  ? 19.881  -3.651  -4.742  1.00 23.05 ? 82  ASP B CB  1 
ATOM   2533 C CG  . ASP B 1 82  ? 19.862  -3.446  -3.259  1.00 22.87 ? 82  ASP B CG  1 
ATOM   2534 O OD1 . ASP B 1 82  ? 19.658  -4.460  -2.555  1.00 22.51 ? 82  ASP B OD1 1 
ATOM   2535 O OD2 . ASP B 1 82  ? 20.043  -2.278  -2.797  1.00 27.28 ? 82  ASP B OD2 1 
ATOM   2536 N N   . TYR B 1 83  ? 17.217  -5.789  -4.137  1.00 26.99 ? 83  TYR B N   1 
ATOM   2537 C CA  . TYR B 1 83  ? 15.772  -5.933  -3.987  1.00 28.07 ? 83  TYR B CA  1 
ATOM   2538 C C   . TYR B 1 83  ? 15.253  -4.983  -2.912  1.00 28.19 ? 83  TYR B C   1 
ATOM   2539 O O   . TYR B 1 83  ? 15.961  -4.629  -1.963  1.00 33.82 ? 83  TYR B O   1 
ATOM   2540 C CB  . TYR B 1 83  ? 15.399  -7.386  -3.632  1.00 26.04 ? 83  TYR B CB  1 
ATOM   2541 C CG  . TYR B 1 83  ? 15.790  -8.388  -4.692  1.00 24.77 ? 83  TYR B CG  1 
ATOM   2542 C CD1 . TYR B 1 83  ? 17.051  -9.030  -4.692  1.00 29.73 ? 83  TYR B CD1 1 
ATOM   2543 C CD2 . TYR B 1 83  ? 14.934  -8.670  -5.702  1.00 28.88 ? 83  TYR B CD2 1 
ATOM   2544 C CE1 . TYR B 1 83  ? 17.412  -9.946  -5.702  1.00 26.00 ? 83  TYR B CE1 1 
ATOM   2545 C CE2 . TYR B 1 83  ? 15.259  -9.585  -6.701  1.00 34.95 ? 83  TYR B CE2 1 
ATOM   2546 C CZ  . TYR B 1 83  ? 16.484  -10.209 -6.722  1.00 34.18 ? 83  TYR B CZ  1 
ATOM   2547 O OH  . TYR B 1 83  ? 16.708  -11.158 -7.762  1.00 39.63 ? 83  TYR B OH  1 
ATOM   2548 N N   . GLN B 1 84  ? 14.004  -4.573  -3.045  1.00 29.06 ? 84  GLN B N   1 
ATOM   2549 C CA  . GLN B 1 84  ? 13.428  -3.717  -2.013  1.00 30.29 ? 84  GLN B CA  1 
ATOM   2550 C C   . GLN B 1 84  ? 13.168  -4.520  -0.744  1.00 32.21 ? 84  GLN B C   1 
ATOM   2551 O O   . GLN B 1 84  ? 12.697  -5.666  -0.799  1.00 30.80 ? 84  GLN B O   1 
ATOM   2552 C CB  . GLN B 1 84  ? 12.125  -3.069  -2.473  1.00 28.92 ? 84  GLN B CB  1 
ATOM   2553 C CG  . GLN B 1 84  ? 11.044  -4.047  -3.014  1.00 30.93 ? 84  GLN B CG  1 
ATOM   2554 C CD  . GLN B 1 84  ? 9.884   -3.298  -3.675  1.00 30.51 ? 84  GLN B CD  1 
ATOM   2555 O OE1 . GLN B 1 84  ? 9.818   -3.214  -4.902  1.00 29.05 ? 84  GLN B OE1 1 
ATOM   2556 N NE2 . GLN B 1 84  ? 8.964   -2.786  -2.869  1.00 30.37 ? 84  GLN B NE2 1 
ATOM   2557 N N   . ASN B 1 85  ? 13.439  -3.889  0.407   1.00 32.72 ? 85  ASN B N   1 
ATOM   2558 C CA  . ASN B 1 85  ? 13.340  -4.570  1.696   1.00 34.65 ? 85  ASN B CA  1 
ATOM   2559 C C   . ASN B 1 85  ? 11.912  -4.597  2.260   1.00 35.30 ? 85  ASN B C   1 
ATOM   2560 O O   . ASN B 1 85  ? 11.662  -5.296  3.244   1.00 32.49 ? 85  ASN B O   1 
ATOM   2561 C CB  . ASN B 1 85  ? 14.261  -3.890  2.714   1.00 33.94 ? 85  ASN B CB  1 
ATOM   2562 C CG  . ASN B 1 85  ? 13.720  -2.527  3.199   1.00 38.16 ? 85  ASN B CG  1 
ATOM   2563 O OD1 . ASN B 1 85  ? 13.033  -1.791  2.464   1.00 39.36 ? 85  ASN B OD1 1 
ATOM   2564 N ND2 . ASN B 1 85  ? 14.025  -2.196  4.457   1.00 39.65 ? 85  ASN B ND2 1 
ATOM   2565 N N   . THR B 1 86  ? 10.996  -3.808  1.710   1.00 34.03 ? 86  THR B N   1 
ATOM   2566 C CA  . THR B 1 86  ? 9.613   -3.736  2.165   1.00 33.43 ? 86  THR B CA  1 
ATOM   2567 C C   . THR B 1 86  ? 8.732   -3.728  0.930   1.00 33.04 ? 86  THR B C   1 
ATOM   2568 O O   . THR B 1 86  ? 9.223   -3.708  -0.198  1.00 34.68 ? 86  THR B O   1 
ATOM   2569 C CB  . THR B 1 86  ? 9.334   -2.468  3.006   1.00 33.37 ? 86  THR B CB  1 
ATOM   2570 O OG1 . THR B 1 86  ? 9.316   -1.332  2.144   1.00 27.68 ? 86  THR B OG1 1 
ATOM   2571 C CG2 . THR B 1 86  ? 10.384  -2.249  4.105   1.00 32.68 ? 86  THR B CG2 1 
ATOM   2572 N N   . ASN B 1 87  ? 7.417   -3.753  1.137   1.00 30.84 ? 87  ASN B N   1 
ATOM   2573 C CA  . ASN B 1 87  ? 6.505   -3.625  0.011   1.00 32.72 ? 87  ASN B CA  1 
ATOM   2574 C C   . ASN B 1 87  ? 6.270   -2.162  -0.397  1.00 32.85 ? 87  ASN B C   1 
ATOM   2575 O O   . ASN B 1 87  ? 5.486   -1.906  -1.322  1.00 33.87 ? 87  ASN B O   1 
ATOM   2576 C CB  . ASN B 1 87  ? 5.197   -4.383  0.332   1.00 37.34 ? 87  ASN B CB  1 
ATOM   2577 C CG  . ASN B 1 87  ? 4.146   -3.530  1.073   1.00 39.22 ? 87  ASN B CG  1 
ATOM   2578 O OD1 . ASN B 1 87  ? 4.453   -2.576  1.808   1.00 35.75 ? 87  ASN B OD1 1 
ATOM   2579 N ND2 . ASN B 1 87  ? 2.883   -3.885  0.871   1.00 47.14 ? 87  ASN B ND2 1 
ATOM   2580 N N   . TYR B 1 88  ? 6.986   -1.204  0.224   1.00 31.84 ? 88  TYR B N   1 
ATOM   2581 C CA  . TYR B 1 88  ? 6.823   0.218   -0.088  1.00 31.29 ? 88  TYR B CA  1 
ATOM   2582 C C   . TYR B 1 88  ? 8.135   0.967   -0.352  1.00 30.02 ? 88  TYR B C   1 
ATOM   2583 O O   . TYR B 1 88  ? 8.126   2.205   -0.449  1.00 28.66 ? 88  TYR B O   1 
ATOM   2584 C CB  . TYR B 1 88  ? 6.050   0.911   1.041   1.00 30.82 ? 88  TYR B CB  1 
ATOM   2585 C CG  . TYR B 1 88  ? 6.760   0.888   2.380   1.00 30.34 ? 88  TYR B CG  1 
ATOM   2586 C CD1 . TYR B 1 88  ? 6.576   -0.161  3.275   1.00 31.80 ? 88  TYR B CD1 1 
ATOM   2587 C CD2 . TYR B 1 88  ? 7.631   1.919   2.739   1.00 32.30 ? 88  TYR B CD2 1 
ATOM   2588 C CE1 . TYR B 1 88  ? 7.246   -0.179  4.510   1.00 32.92 ? 88  TYR B CE1 1 
ATOM   2589 C CE2 . TYR B 1 88  ? 8.306   1.925   3.952   1.00 31.13 ? 88  TYR B CE2 1 
ATOM   2590 C CZ  . TYR B 1 88  ? 8.117   0.876   4.843   1.00 35.81 ? 88  TYR B CZ  1 
ATOM   2591 O OH  . TYR B 1 88  ? 8.804   0.875   6.061   1.00 33.08 ? 88  TYR B OH  1 
ATOM   2592 N N   . THR B 1 89  ? 9.272   0.283   -0.465  1.00 30.22 ? 89  THR B N   1 
ATOM   2593 C CA  . THR B 1 89  ? 10.542  0.988   -0.696  1.00 28.64 ? 89  THR B CA  1 
ATOM   2594 C C   . THR B 1 89  ? 11.064  0.821   -2.126  1.00 26.96 ? 89  THR B C   1 
ATOM   2595 O O   . THR B 1 89  ? 12.269  0.944   -2.377  1.00 24.86 ? 89  THR B O   1 
ATOM   2596 C CB  . THR B 1 89  ? 11.606  0.562   0.320   1.00 26.88 ? 89  THR B CB  1 
ATOM   2597 O OG1 . THR B 1 89  ? 11.498  -0.841  0.601   1.00 27.88 ? 89  THR B OG1 1 
ATOM   2598 C CG2 . THR B 1 89  ? 11.426  1.325   1.634   1.00 24.11 ? 89  THR B CG2 1 
ATOM   2599 N N   . CYS B 1 90  ? 10.165  0.586   -3.085  1.00 25.71 ? 90  CYS B N   1 
ATOM   2600 C CA  . CYS B 1 90  ? 10.583  0.462   -4.482  1.00 25.95 ? 90  CYS B CA  1 
ATOM   2601 C C   . CYS B 1 90  ? 11.269  1.743   -4.995  1.00 25.32 ? 90  CYS B C   1 
ATOM   2602 O O   . CYS B 1 90  ? 12.272  1.661   -5.706  1.00 24.14 ? 90  CYS B O   1 
ATOM   2603 C CB  . CYS B 1 90  ? 9.388   0.106   -5.348  1.00 29.28 ? 90  CYS B CB  1 
ATOM   2604 S SG  . CYS B 1 90  ? 7.824   0.921   -4.841  1.00 28.81 ? 90  CYS B SG  1 
ATOM   2605 N N   . CYS B 1 91  ? 10.771  2.934   -4.637  1.00 24.40 ? 91  CYS B N   1 
ATOM   2606 C CA  . CYS B 1 91  ? 11.394  4.153   -5.167  1.00 24.97 ? 91  CYS B CA  1 
ATOM   2607 C C   . CYS B 1 91  ? 12.799  4.383   -4.623  1.00 25.91 ? 91  CYS B C   1 
ATOM   2608 O O   . CYS B 1 91  ? 13.727  4.563   -5.434  1.00 24.81 ? 91  CYS B O   1 
ATOM   2609 C CB  . CYS B 1 91  ? 10.501  5.367   -4.922  1.00 24.45 ? 91  CYS B CB  1 
ATOM   2610 S SG  . CYS B 1 91  ? 11.092  6.865   -5.725  1.00 26.61 ? 91  CYS B SG  1 
ATOM   2611 N N   . PRO B 1 92  ? 13.044  4.398   -3.305  1.00 26.76 ? 92  PRO B N   1 
ATOM   2612 C CA  . PRO B 1 92  ? 14.436  4.535   -2.856  1.00 25.46 ? 92  PRO B CA  1 
ATOM   2613 C C   . PRO B 1 92  ? 15.330  3.372   -3.291  1.00 25.26 ? 92  PRO B C   1 
ATOM   2614 O O   . PRO B 1 92  ? 16.525  3.597   -3.514  1.00 22.54 ? 92  PRO B O   1 
ATOM   2615 C CB  . PRO B 1 92  ? 14.323  4.588   -1.325  1.00 26.12 ? 92  PRO B CB  1 
ATOM   2616 C CG  . PRO B 1 92  ? 12.915  3.988   -1.019  1.00 27.72 ? 92  PRO B CG  1 
ATOM   2617 C CD  . PRO B 1 92  ? 12.096  4.405   -2.176  1.00 23.24 ? 92  PRO B CD  1 
ATOM   2618 N N   . THR B 1 93  ? 14.803  2.146   -3.454  1.00 24.93 ? 93  THR B N   1 
ATOM   2619 C CA  . THR B 1 93  ? 15.633  1.076   -4.029  1.00 24.19 ? 93  THR B CA  1 
ATOM   2620 C C   . THR B 1 93  ? 16.025  1.380   -5.476  1.00 25.11 ? 93  THR B C   1 
ATOM   2621 O O   . THR B 1 93  ? 17.172  1.119   -5.888  1.00 21.37 ? 93  THR B O   1 
ATOM   2622 C CB  . THR B 1 93  ? 14.947  -0.311  -3.957  1.00 25.05 ? 93  THR B CB  1 
ATOM   2623 O OG1 . THR B 1 93  ? 14.476  -0.584  -2.637  1.00 24.21 ? 93  THR B OG1 1 
ATOM   2624 C CG2 . THR B 1 93  ? 15.970  -1.386  -4.299  1.00 26.47 ? 93  THR B CG2 1 
ATOM   2625 N N   . SER B 1 94  ? 15.087  1.925   -6.263  1.00 23.98 ? 94  SER B N   1 
ATOM   2626 C CA  . SER B 1 94  ? 15.395  2.301   -7.647  1.00 21.00 ? 94  SER B CA  1 
ATOM   2627 C C   . SER B 1 94  ? 16.435  3.421   -7.691  1.00 21.10 ? 94  SER B C   1 
ATOM   2628 O O   . SER B 1 94  ? 17.346  3.405   -8.530  1.00 19.00 ? 94  SER B O   1 
ATOM   2629 C CB  . SER B 1 94  ? 14.107  2.686   -8.370  1.00 25.34 ? 94  SER B CB  1 
ATOM   2630 O OG  . SER B 1 94  ? 13.173  1.598   -8.474  1.00 23.35 ? 94  SER B OG  1 
ATOM   2631 N N   . LEU B 1 95  ? 16.349  4.371   -6.758  1.00 22.04 ? 95  LEU B N   1 
ATOM   2632 C CA  . LEU B 1 95  ? 17.364  5.421   -6.666  1.00 24.77 ? 95  LEU B CA  1 
ATOM   2633 C C   . LEU B 1 95  ? 18.710  4.849   -6.224  1.00 23.03 ? 95  LEU B C   1 
ATOM   2634 O O   . LEU B 1 95  ? 19.738  5.305   -6.703  1.00 20.81 ? 95  LEU B O   1 
ATOM   2635 C CB  . LEU B 1 95  ? 16.927  6.528   -5.709  1.00 19.79 ? 95  LEU B CB  1 
ATOM   2636 C CG  . LEU B 1 95  ? 17.855  7.728   -5.576  1.00 25.07 ? 95  LEU B CG  1 
ATOM   2637 C CD1 . LEU B 1 95  ? 18.093  8.383   -6.955  1.00 24.63 ? 95  LEU B CD1 1 
ATOM   2638 C CD2 . LEU B 1 95  ? 17.297  8.776   -4.570  1.00 25.06 ? 95  LEU B CD2 1 
ATOM   2639 N N   . SER B 1 96  ? 18.720  3.862   -5.305  1.00 23.92 ? 96  SER B N   1 
ATOM   2640 C CA  . SER B 1 96  ? 19.972  3.215   -4.907  1.00 22.44 ? 96  SER B CA  1 
ATOM   2641 C C   . SER B 1 96  ? 20.638  2.511   -6.084  1.00 20.13 ? 96  SER B C   1 
ATOM   2642 O O   . SER B 1 96  ? 21.848  2.674   -6.311  1.00 22.35 ? 96  SER B O   1 
ATOM   2643 C CB  . SER B 1 96  ? 19.725  2.230   -3.768  1.00 23.82 ? 96  SER B CB  1 
ATOM   2644 O OG  . SER B 1 96  ? 20.968  1.656   -3.313  1.00 23.04 ? 96  SER B OG  1 
ATOM   2645 N N   . LEU B 1 97  ? 19.854  1.753   -6.867  1.00 20.99 ? 97  LEU B N   1 
ATOM   2646 C CA  . LEU B 1 97  ? 20.364  1.124   -8.079  1.00 22.74 ? 97  LEU B CA  1 
ATOM   2647 C C   . LEU B 1 97  ? 20.953  2.154   -9.041  1.00 22.56 ? 97  LEU B C   1 
ATOM   2648 O O   . LEU B 1 97  ? 22.034  1.937   -9.609  1.00 22.59 ? 97  LEU B O   1 
ATOM   2649 C CB  . LEU B 1 97  ? 19.270  0.337   -8.770  1.00 18.48 ? 97  LEU B CB  1 
ATOM   2650 C CG  . LEU B 1 97  ? 18.774  -0.845  -7.936  1.00 22.87 ? 97  LEU B CG  1 
ATOM   2651 C CD1 . LEU B 1 97  ? 17.419  -1.310  -8.457  1.00 21.86 ? 97  LEU B CD1 1 
ATOM   2652 C CD2 . LEU B 1 97  ? 19.780  -1.974  -7.969  1.00 22.06 ? 97  LEU B CD2 1 
ATOM   2653 N N   . ALA B 1 98  ? 20.244  3.261   -9.274  1.00 20.13 ? 98  ALA B N   1 
ATOM   2654 C CA  . ALA B 1 98  ? 20.853  4.357   -10.034 1.00 20.64 ? 98  ALA B CA  1 
ATOM   2655 C C   . ALA B 1 98  ? 22.183  4.809   -9.434  1.00 20.14 ? 98  ALA B C   1 
ATOM   2656 O O   . ALA B 1 98  ? 23.134  5.103   -10.168 1.00 20.01 ? 98  ALA B O   1 
ATOM   2657 C CB  . ALA B 1 98  ? 19.917  5.577   -10.063 1.00 21.02 ? 98  ALA B CB  1 
ATOM   2658 N N   . SER B 1 99  ? 22.256  4.933   -8.102  1.00 19.15 ? 99  SER B N   1 
ATOM   2659 C CA  . SER B 1 99  ? 23.468  5.484   -7.503  1.00 21.82 ? 99  SER B CA  1 
ATOM   2660 C C   . SER B 1 99  ? 24.698  4.594   -7.781  1.00 21.67 ? 99  SER B C   1 
ATOM   2661 O O   . SER B 1 99  ? 25.832  5.097   -7.848  1.00 20.44 ? 99  SER B O   1 
ATOM   2662 C CB  . SER B 1 99  ? 23.268  5.683   -5.996  1.00 19.72 ? 99  SER B CB  1 
ATOM   2663 O OG  . SER B 1 99  ? 23.379  4.471   -5.269  1.00 23.72 ? 99  SER B OG  1 
ATOM   2664 N N   . GLN B 1 100 ? 24.499  3.290   -7.992  1.00 23.78 ? 100 GLN B N   1 
ATOM   2665 C CA  . GLN B 1 100 ? 25.612  2.425   -8.440  1.00 21.34 ? 100 GLN B CA  1 
ATOM   2666 C C   . GLN B 1 100 ? 26.104  2.820   -9.828  1.00 24.03 ? 100 GLN B C   1 
ATOM   2667 O O   . GLN B 1 100 ? 27.308  2.921   -10.061 1.00 25.28 ? 100 GLN B O   1 
ATOM   2668 C CB  . GLN B 1 100 ? 25.197  0.944   -8.477  1.00 22.71 ? 100 GLN B CB  1 
ATOM   2669 C CG  . GLN B 1 100 ? 24.619  0.356   -7.187  1.00 22.01 ? 100 GLN B CG  1 
ATOM   2670 C CD  . GLN B 1 100 ? 24.186  -1.083  -7.401  1.00 20.58 ? 100 GLN B CD  1 
ATOM   2671 O OE1 . GLN B 1 100 ? 24.900  -1.861  -8.064  1.00 19.40 ? 100 GLN B OE1 1 
ATOM   2672 N NE2 . GLN B 1 100 ? 22.966  -1.434  -6.923  1.00 20.07 ? 100 GLN B NE2 1 
ATOM   2673 N N   . MET B 1 101 ? 25.180  2.978   -10.777 1.00 23.92 ? 101 MET B N   1 
ATOM   2674 C CA  . MET B 1 101 ? 25.526  3.309   -12.159 1.00 24.44 ? 101 MET B CA  1 
ATOM   2675 C C   . MET B 1 101 ? 26.249  4.638   -12.252 1.00 25.61 ? 101 MET B C   1 
ATOM   2676 O O   . MET B 1 101 ? 27.036  4.834   -13.183 1.00 28.98 ? 101 MET B O   1 
ATOM   2677 C CB  . MET B 1 101 ? 24.266  3.388   -13.036 1.00 25.36 ? 101 MET B CB  1 
ATOM   2678 C CG  . MET B 1 101 ? 23.416  2.075   -13.131 1.00 27.94 ? 101 MET B CG  1 
ATOM   2679 S SD  . MET B 1 101 ? 24.285  0.872   -14.137 1.00 40.99 ? 101 MET B SD  1 
ATOM   2680 C CE  . MET B 1 101 ? 23.929  1.592   -15.755 1.00 38.09 ? 101 MET B CE  1 
ATOM   2681 N N   . LEU B 1 102 ? 25.976  5.572   -11.327 1.00 23.53 ? 102 LEU B N   1 
ATOM   2682 C CA  . LEU B 1 102 ? 26.611  6.892   -11.291 1.00 24.61 ? 102 LEU B CA  1 
ATOM   2683 C C   . LEU B 1 102 ? 27.895  6.917   -10.454 1.00 24.57 ? 102 LEU B C   1 
ATOM   2684 O O   . LEU B 1 102 ? 28.491  7.994   -10.289 1.00 22.17 ? 102 LEU B O   1 
ATOM   2685 C CB  . LEU B 1 102 ? 25.637  7.932   -10.729 1.00 21.69 ? 102 LEU B CB  1 
ATOM   2686 C CG  . LEU B 1 102 ? 24.390  8.189   -11.587 1.00 23.54 ? 102 LEU B CG  1 
ATOM   2687 C CD1 . LEU B 1 102 ? 23.581  9.309   -10.976 1.00 19.72 ? 102 LEU B CD1 1 
ATOM   2688 C CD2 . LEU B 1 102 ? 24.769  8.584   -12.992 1.00 25.19 ? 102 LEU B CD2 1 
ATOM   2689 N N   . TYR B 1 103 ? 28.300  5.777   -9.870  1.00 23.60 ? 103 TYR B N   1 
ATOM   2690 C CA  . TYR B 1 103 ? 29.511  5.701   -9.063  1.00 23.29 ? 103 TYR B CA  1 
ATOM   2691 C C   . TYR B 1 103 ? 29.441  6.637   -7.851  1.00 24.93 ? 103 TYR B C   1 
ATOM   2692 O O   . TYR B 1 103 ? 30.467  7.236   -7.438  1.00 24.40 ? 103 TYR B O   1 
ATOM   2693 C CB  . TYR B 1 103 ? 30.752  5.998   -9.919  1.00 22.31 ? 103 TYR B CB  1 
ATOM   2694 C CG  . TYR B 1 103 ? 31.065  4.886   -10.881 1.00 22.59 ? 103 TYR B CG  1 
ATOM   2695 C CD1 . TYR B 1 103 ? 30.396  4.785   -12.071 1.00 24.05 ? 103 TYR B CD1 1 
ATOM   2696 C CD2 . TYR B 1 103 ? 32.022  3.926   -10.588 1.00 22.88 ? 103 TYR B CD2 1 
ATOM   2697 C CE1 . TYR B 1 103 ? 30.640  3.767   -12.953 1.00 22.02 ? 103 TYR B CE1 1 
ATOM   2698 C CE2 . TYR B 1 103 ? 32.290  2.877   -11.488 1.00 20.01 ? 103 TYR B CE2 1 
ATOM   2699 C CZ  . TYR B 1 103 ? 31.604  2.829   -12.668 1.00 23.24 ? 103 TYR B CZ  1 
ATOM   2700 O OH  . TYR B 1 103 ? 31.804  1.796   -13.578 1.00 24.15 ? 103 TYR B OH  1 
ATOM   2701 N N   . HIS B 1 104 ? 28.219  6.739   -7.262  1.00 24.60 ? 104 HIS B N   1 
ATOM   2702 C CA  . HIS B 1 104 ? 27.955  7.513   -6.052  1.00 23.97 ? 104 HIS B CA  1 
ATOM   2703 C C   . HIS B 1 104 ? 26.944  6.756   -5.160  1.00 26.05 ? 104 HIS B C   1 
ATOM   2704 O O   . HIS B 1 104 ? 25.847  7.245   -4.838  1.00 22.16 ? 104 HIS B O   1 
ATOM   2705 C CB  . HIS B 1 104 ? 27.457  8.924   -6.429  1.00 24.31 ? 104 HIS B CB  1 
ATOM   2706 C CG  . HIS B 1 104 ? 27.500  9.905   -5.302  1.00 25.92 ? 104 HIS B CG  1 
ATOM   2707 N ND1 . HIS B 1 104 ? 28.681  10.336  -4.741  1.00 25.06 ? 104 HIS B ND1 1 
ATOM   2708 C CD2 . HIS B 1 104 ? 26.509  10.571  -4.651  1.00 26.05 ? 104 HIS B CD2 1 
ATOM   2709 C CE1 . HIS B 1 104 ? 28.426  11.204  -3.782  1.00 26.86 ? 104 HIS B CE1 1 
ATOM   2710 N NE2 . HIS B 1 104 ? 27.112  11.352  -3.694  1.00 27.16 ? 104 HIS B NE2 1 
ATOM   2711 N N   . TYR B 1 105 ? 27.348  5.547   -4.719  1.00 23.56 ? 105 TYR B N   1 
ATOM   2712 C CA  . TYR B 1 105 ? 26.430  4.623   -4.071  1.00 21.05 ? 105 TYR B CA  1 
ATOM   2713 C C   . TYR B 1 105 ? 25.856  5.199   -2.786  1.00 23.62 ? 105 TYR B C   1 
ATOM   2714 O O   . TYR B 1 105 ? 26.592  5.705   -1.931  1.00 23.21 ? 105 TYR B O   1 
ATOM   2715 C CB  . TYR B 1 105 ? 27.133  3.314   -3.773  1.00 23.00 ? 105 TYR B CB  1 
ATOM   2716 C CG  . TYR B 1 105 ? 26.269  2.337   -2.997  1.00 21.14 ? 105 TYR B CG  1 
ATOM   2717 C CD1 . TYR B 1 105 ? 25.176  1.739   -3.601  1.00 20.38 ? 105 TYR B CD1 1 
ATOM   2718 C CD2 . TYR B 1 105 ? 26.537  2.061   -1.673  1.00 21.96 ? 105 TYR B CD2 1 
ATOM   2719 C CE1 . TYR B 1 105 ? 24.339  0.811   -2.890  1.00 19.87 ? 105 TYR B CE1 1 
ATOM   2720 C CE2 . TYR B 1 105 ? 25.738  1.135   -0.961  1.00 25.00 ? 105 TYR B CE2 1 
ATOM   2721 C CZ  . TYR B 1 105 ? 24.648  0.538   -1.570  1.00 21.84 ? 105 TYR B CZ  1 
ATOM   2722 O OH  . TYR B 1 105 ? 23.916  -0.341  -0.830  1.00 20.73 ? 105 TYR B OH  1 
ATOM   2723 N N   . LYS B 1 106 ? 24.513  5.122   -2.664  1.00 21.09 ? 106 LYS B N   1 
ATOM   2724 C CA  . LYS B 1 106 ? 23.764  5.382   -1.441  1.00 23.78 ? 106 LYS B CA  1 
ATOM   2725 C C   . LYS B 1 106 ? 22.852  4.186   -1.220  1.00 22.42 ? 106 LYS B C   1 
ATOM   2726 O O   . LYS B 1 106 ? 22.162  3.766   -2.156  1.00 19.02 ? 106 LYS B O   1 
ATOM   2727 C CB  . LYS B 1 106 ? 22.919  6.642   -1.602  1.00 22.22 ? 106 LYS B CB  1 
ATOM   2728 C CG  . LYS B 1 106 ? 23.759  7.890   -1.938  1.00 21.52 ? 106 LYS B CG  1 
ATOM   2729 C CD  . LYS B 1 106 ? 24.632  8.274   -0.738  1.00 25.52 ? 106 LYS B CD  1 
ATOM   2730 C CE  . LYS B 1 106 ? 25.567  9.476   -1.127  1.00 27.55 ? 106 LYS B CE  1 
ATOM   2731 N NZ  . LYS B 1 106 ? 26.534  9.833   -0.063  1.00 31.63 ? 106 LYS B NZ  1 
ATOM   2732 N N   . SER B 1 107 ? 22.852  3.634   -0.013  1.00 20.74 ? 107 SER B N   1 
ATOM   2733 C CA  . SER B 1 107 ? 22.092  2.418   0.232   1.00 23.78 ? 107 SER B CA  1 
ATOM   2734 C C   . SER B 1 107 ? 20.565  2.688   0.163   1.00 24.37 ? 107 SER B C   1 
ATOM   2735 O O   . SER B 1 107 ? 20.089  3.827   0.181   1.00 20.15 ? 107 SER B O   1 
ATOM   2736 C CB  . SER B 1 107 ? 22.484  1.821   1.591   1.00 24.50 ? 107 SER B CB  1 
ATOM   2737 O OG  . SER B 1 107 ? 21.958  2.639   2.628   1.00 24.37 ? 107 SER B OG  1 
ATOM   2738 N N   . GLU B 1 108 ? 19.806  1.600   0.070   1.00 23.66 ? 108 GLU B N   1 
ATOM   2739 C CA  . GLU B 1 108 ? 18.357  1.696   0.055   1.00 24.61 ? 108 GLU B CA  1 
ATOM   2740 C C   . GLU B 1 108 ? 17.823  2.493   1.243   1.00 23.09 ? 108 GLU B C   1 
ATOM   2741 O O   . GLU B 1 108 ? 16.965  3.378   1.084   1.00 24.60 ? 108 GLU B O   1 
ATOM   2742 C CB  . GLU B 1 108 ? 17.755  0.286   0.027   1.00 26.33 ? 108 GLU B CB  1 
ATOM   2743 C CG  . GLU B 1 108 ? 16.236  0.373   0.212   1.00 23.62 ? 108 GLU B CG  1 
ATOM   2744 C CD  . GLU B 1 108 ? 15.589  -1.010  0.004   1.00 32.36 ? 108 GLU B CD  1 
ATOM   2745 O OE1 . GLU B 1 108 ? 14.451  -1.202  0.460   1.00 29.53 ? 108 GLU B OE1 1 
ATOM   2746 O OE2 . GLU B 1 108 ? 16.270  -1.906  -0.593  1.00 35.92 ? 108 GLU B OE2 1 
ATOM   2747 N N   . SER B 1 109 ? 18.322  2.203   2.448   1.00 23.32 ? 109 SER B N   1 
ATOM   2748 C CA  . SER B 1 109 ? 17.846  2.936   3.615   1.00 24.44 ? 109 SER B CA  1 
ATOM   2749 C C   . SER B 1 109 ? 18.286  4.396   3.618   1.00 25.55 ? 109 SER B C   1 
ATOM   2750 O O   . SER B 1 109 ? 17.525  5.251   4.089   1.00 26.74 ? 109 SER B O   1 
ATOM   2751 C CB  . SER B 1 109 ? 18.278  2.267   4.916   1.00 27.98 ? 109 SER B CB  1 
ATOM   2752 O OG  . SER B 1 109 ? 19.657  2.213   5.012   1.00 34.75 ? 109 SER B OG  1 
ATOM   2753 N N   . GLU B 1 110 ? 19.520  4.706   3.179   1.00 24.91 ? 110 GLU B N   1 
ATOM   2754 C CA  . GLU B 1 110 ? 19.924  6.114   3.074   1.00 25.15 ? 110 GLU B CA  1 
ATOM   2755 C C   . GLU B 1 110 ? 18.990  6.874   2.145   1.00 25.80 ? 110 GLU B C   1 
ATOM   2756 O O   . GLU B 1 110 ? 18.616  8.022   2.427   1.00 28.10 ? 110 GLU B O   1 
ATOM   2757 C CB  . GLU B 1 110 ? 21.353  6.247   2.521   1.00 27.62 ? 110 GLU B CB  1 
ATOM   2758 C CG  . GLU B 1 110 ? 22.504  6.092   3.484   1.00 29.88 ? 110 GLU B CG  1 
ATOM   2759 C CD  . GLU B 1 110 ? 23.890  6.146   2.755   1.00 35.51 ? 110 GLU B CD  1 
ATOM   2760 O OE1 . GLU B 1 110 ? 24.154  5.406   1.757   1.00 31.37 ? 110 GLU B OE1 1 
ATOM   2761 O OE2 . GLU B 1 110 ? 24.722  6.974   3.169   1.00 42.58 ? 110 GLU B OE2 1 
ATOM   2762 N N   . CYS B 1 111 ? 18.630  6.256   1.008   1.00 23.17 ? 111 CYS B N   1 
ATOM   2763 C CA  . CYS B 1 111 ? 17.729  6.902   0.066   1.00 26.69 ? 111 CYS B CA  1 
ATOM   2764 C C   . CYS B 1 111 ? 16.328  7.061   0.665   1.00 25.76 ? 111 CYS B C   1 
ATOM   2765 O O   . CYS B 1 111 ? 15.728  8.118   0.545   1.00 26.12 ? 111 CYS B O   1 
ATOM   2766 C CB  . CYS B 1 111 ? 17.660  6.104   -1.231  1.00 23.59 ? 111 CYS B CB  1 
ATOM   2767 S SG  . CYS B 1 111 ? 19.209  6.131   -2.194  1.00 24.05 ? 111 CYS B SG  1 
ATOM   2768 N N   . ALA B 1 112 ? 15.827  6.047   1.372   1.00 25.21 ? 112 ALA B N   1 
ATOM   2769 C CA  . ALA B 1 112 ? 14.472  6.137   1.918   1.00 27.31 ? 112 ALA B CA  1 
ATOM   2770 C C   . ALA B 1 112 ? 14.379  7.249   2.959   1.00 30.77 ? 112 ALA B C   1 
ATOM   2771 O O   . ALA B 1 112 ? 13.402  8.011   2.995   1.00 31.14 ? 112 ALA B O   1 
ATOM   2772 C CB  . ALA B 1 112 ? 14.080  4.799   2.544   1.00 26.43 ? 112 ALA B CB  1 
ATOM   2773 N N   . LYS B 1 113 ? 15.367  7.321   3.843   1.00 28.60 ? 113 LYS B N   1 
ATOM   2774 C CA  . LYS B 1 113 ? 15.436  8.412   4.801   1.00 28.96 ? 113 LYS B CA  1 
ATOM   2775 C C   . LYS B 1 113 ? 15.398  9.770   4.090   1.00 32.45 ? 113 LYS B C   1 
ATOM   2776 O O   . LYS B 1 113 ? 14.577  10.651  4.423   1.00 31.49 ? 113 LYS B O   1 
ATOM   2777 C CB  . LYS B 1 113 ? 16.669  8.227   5.666   1.00 28.71 ? 113 LYS B CB  1 
ATOM   2778 C CG  . LYS B 1 113 ? 16.923  9.334   6.655   1.00 35.13 ? 113 LYS B CG  1 
ATOM   2779 C CD  . LYS B 1 113 ? 16.907  8.797   8.081   1.00 41.58 ? 113 LYS B CD  1 
ATOM   2780 C CE  . LYS B 1 113 ? 16.919  9.927   9.113   1.00 44.96 ? 113 LYS B CE  1 
ATOM   2781 N NZ  . LYS B 1 113 ? 18.316  10.359  9.437   1.00 48.55 ? 113 LYS B NZ  1 
ATOM   2782 N N   . ALA B 1 114 ? 16.240  9.942   3.075   1.00 28.58 ? 114 ALA B N   1 
ATOM   2783 C CA  . ALA B 1 114 ? 16.316  11.224  2.388   1.00 29.96 ? 114 ALA B CA  1 
ATOM   2784 C C   . ALA B 1 114 ? 15.015  11.539  1.649   1.00 31.33 ? 114 ALA B C   1 
ATOM   2785 O O   . ALA B 1 114 ? 14.536  12.688  1.658   1.00 29.07 ? 114 ALA B O   1 
ATOM   2786 C CB  . ALA B 1 114 ? 17.498  11.231  1.425   1.00 28.78 ? 114 ALA B CB  1 
ATOM   2787 N N   . LEU B 1 115 ? 14.432  10.535  0.986   1.00 26.39 ? 115 LEU B N   1 
ATOM   2788 C CA  . LEU B 1 115 ? 13.242  10.800  0.199   1.00 30.41 ? 115 LEU B CA  1 
ATOM   2789 C C   . LEU B 1 115 ? 12.003  11.026  1.060   1.00 28.39 ? 115 LEU B C   1 
ATOM   2790 O O   . LEU B 1 115 ? 11.031  11.637  0.580   1.00 29.20 ? 115 LEU B O   1 
ATOM   2791 C CB  . LEU B 1 115 ? 12.969  9.647   -0.766  1.00 29.20 ? 115 LEU B CB  1 
ATOM   2792 C CG  . LEU B 1 115 ? 14.051  9.460   -1.836  1.00 28.67 ? 115 LEU B CG  1 
ATOM   2793 C CD1 . LEU B 1 115 ? 13.595  8.539   -2.948  1.00 21.27 ? 115 LEU B CD1 1 
ATOM   2794 C CD2 . LEU B 1 115 ? 14.552  10.833  -2.366  1.00 26.29 ? 115 LEU B CD2 1 
ATOM   2795 N N   . GLY B 1 116 ? 12.031  10.588  2.322   1.00 28.06 ? 116 GLY B N   1 
ATOM   2796 C CA  . GLY B 1 116 ? 10.848  10.640  3.168   1.00 30.64 ? 116 GLY B CA  1 
ATOM   2797 C C   . GLY B 1 116 ? 9.832   9.556   2.873   1.00 32.84 ? 116 GLY B C   1 
ATOM   2798 O O   . GLY B 1 116 ? 8.629   9.782   3.036   1.00 30.63 ? 116 GLY B O   1 
ATOM   2799 N N   . THR B 1 117 ? 10.289  8.391   2.418   1.00 28.71 ? 117 THR B N   1 
ATOM   2800 C CA  . THR B 1 117 ? 9.428   7.249   2.117   1.00 28.14 ? 117 THR B CA  1 
ATOM   2801 C C   . THR B 1 117 ? 8.726   6.814   3.388   1.00 29.95 ? 117 THR B C   1 
ATOM   2802 O O   . THR B 1 117 ? 9.330   6.820   4.463   1.00 31.06 ? 117 THR B O   1 
ATOM   2803 C CB  . THR B 1 117 ? 10.292  6.094   1.588   1.00 31.71 ? 117 THR B CB  1 
ATOM   2804 O OG1 . THR B 1 117 ? 11.081  6.549   0.459   1.00 31.45 ? 117 THR B OG1 1 
ATOM   2805 C CG2 . THR B 1 117 ? 9.427   4.863   1.213   1.00 27.22 ? 117 THR B CG2 1 
ATOM   2806 N N   . SER B 1 118 ? 7.461   6.440   3.256   1.00 30.73 ? 118 SER B N   1 
ATOM   2807 C CA  . SER B 1 118 ? 6.664   6.054   4.443   1.00 31.89 ? 118 SER B CA  1 
ATOM   2808 C C   . SER B 1 118 ? 5.909   4.754   4.190   1.00 32.23 ? 118 SER B C   1 
ATOM   2809 O O   . SER B 1 118 ? 5.510   4.513   3.071   1.00 33.84 ? 118 SER B O   1 
ATOM   2810 C CB  . SER B 1 118 ? 5.739   7.154   4.848   1.00 34.15 ? 118 SER B CB  1 
ATOM   2811 O OG  . SER B 1 118 ? 4.790   7.360   3.839   1.00 42.32 ? 118 SER B OG  1 
ATOM   2812 N N   . LYS B 1 119 ? 5.743   3.972   5.247   1.00 37.92 ? 119 LYS B N   1 
ATOM   2813 C CA  . LYS B 1 119 ? 5.086   2.648   5.172   1.00 38.34 ? 119 LYS B CA  1 
ATOM   2814 C C   . LYS B 1 119 ? 3.699   2.770   4.556   1.00 38.06 ? 119 LYS B C   1 
ATOM   2815 O O   . LYS B 1 119 ? 3.319   1.889   3.845   1.00 46.20 ? 119 LYS B O   1 
ATOM   2816 C CB  . LYS B 1 119 ? 4.985   2.026   6.563   1.00 41.08 ? 119 LYS B CB  1 
ATOM   2817 C CG  . LYS B 1 119 ? 4.170   0.742   6.640   1.00 48.00 ? 119 LYS B CG  1 
ATOM   2818 C CD  . LYS B 1 119 ? 3.854   0.325   8.058   1.00 52.01 ? 119 LYS B CD  1 
ATOM   2819 C CE  . LYS B 1 119 ? 2.755   -0.705  8.156   1.00 54.24 ? 119 LYS B CE  1 
ATOM   2820 N NZ  . LYS B 1 119 ? 3.205   -1.952  8.818   1.00 58.31 ? 119 LYS B NZ  1 
ATOM   2821 N N   . GLY B 1 120 ? 2.995   3.862   4.778   1.00 38.85 ? 120 GLY B N   1 
ATOM   2822 C CA  . GLY B 1 120 ? 1.639   3.906   4.202   1.00 46.76 ? 120 GLY B CA  1 
ATOM   2823 C C   . GLY B 1 120 ? 1.552   4.444   2.790   1.00 48.42 ? 120 GLY B C   1 
ATOM   2824 O O   . GLY B 1 120 ? 0.879   3.812   1.976   1.00 50.53 ? 120 GLY B O   1 
ATOM   2825 N N   . SER B 1 121 ? 2.226   5.554   2.501   1.00 48.89 ? 121 SER B N   1 
ATOM   2826 C CA  . SER B 1 121 ? 2.114   6.191   1.163   1.00 47.00 ? 121 SER B CA  1 
ATOM   2827 C C   . SER B 1 121 ? 3.242   5.800   0.205   1.00 44.19 ? 121 SER B C   1 
ATOM   2828 O O   . SER B 1 121 ? 3.094   6.071   -0.972  1.00 46.49 ? 121 SER B O   1 
ATOM   2829 C CB  . SER B 1 121 ? 2.067   7.676   1.295   1.00 51.05 ? 121 SER B CB  1 
ATOM   2830 O OG  . SER B 1 121 ? 1.463   8.080   2.512   1.00 56.02 ? 121 SER B OG  1 
ATOM   2831 N N   . GLY B 1 122 ? 4.324   5.185   0.661   1.00 37.90 ? 122 GLY B N   1 
ATOM   2832 C CA  . GLY B 1 122 ? 5.389   4.940   -0.325  1.00 35.83 ? 122 GLY B CA  1 
ATOM   2833 C C   . GLY B 1 122 ? 6.136   6.227   -0.634  1.00 29.32 ? 122 GLY B C   1 
ATOM   2834 O O   . GLY B 1 122 ? 6.449   6.908   0.290   1.00 33.39 ? 122 GLY B O   1 
ATOM   2835 N N   . THR B 1 123 ? 6.372   6.540   -1.904  1.00 29.61 ? 123 THR B N   1 
ATOM   2836 C CA  . THR B 1 123 ? 7.129   7.717   -2.323  1.00 26.57 ? 123 THR B CA  1 
ATOM   2837 C C   . THR B 1 123 ? 6.493   8.332   -3.546  1.00 24.50 ? 123 THR B C   1 
ATOM   2838 O O   . THR B 1 123 ? 6.208   7.618   -4.511  1.00 27.32 ? 123 THR B O   1 
ATOM   2839 C CB  . THR B 1 123 ? 8.599   7.347   -2.700  1.00 26.47 ? 123 THR B CB  1 
ATOM   2840 O OG1 . THR B 1 123 ? 9.148   6.490   -1.710  1.00 27.59 ? 123 THR B OG1 1 
ATOM   2841 C CG2 . THR B 1 123 ? 9.462   8.595   -2.762  1.00 26.73 ? 123 THR B CG2 1 
ATOM   2842 N N   . SER B 1 124 ? 6.307   9.626   -3.537  1.00 27.56 ? 124 SER B N   1 
ATOM   2843 C CA  . SER B 1 124 ? 5.746   10.208  -4.750  1.00 30.34 ? 124 SER B CA  1 
ATOM   2844 C C   . SER B 1 124 ? 6.853   10.662  -5.685  1.00 27.98 ? 124 SER B C   1 
ATOM   2845 O O   . SER B 1 124 ? 7.999   10.860  -5.266  1.00 29.94 ? 124 SER B O   1 
ATOM   2846 C CB  . SER B 1 124 ? 4.839   11.414  -4.410  1.00 27.41 ? 124 SER B CB  1 
ATOM   2847 O OG  . SER B 1 124 ? 5.626   12.570  -4.145  1.00 29.53 ? 124 SER B OG  1 
ATOM   2848 N N   . PRO B 1 125 ? 6.525   10.868  -6.964  1.00 28.04 ? 125 PRO B N   1 
ATOM   2849 C CA  . PRO B 1 125 ? 7.489   11.492  -7.857  1.00 29.76 ? 125 PRO B CA  1 
ATOM   2850 C C   . PRO B 1 125 ? 7.938   12.878  -7.385  1.00 30.95 ? 125 PRO B C   1 
ATOM   2851 O O   . PRO B 1 125 ? 9.122   13.226  -7.543  1.00 27.50 ? 125 PRO B O   1 
ATOM   2852 C CB  . PRO B 1 125 ? 6.732   11.527  -9.188  1.00 31.70 ? 125 PRO B CB  1 
ATOM   2853 C CG  . PRO B 1 125 ? 5.781   10.394  -9.101  1.00 30.44 ? 125 PRO B CG  1 
ATOM   2854 C CD  . PRO B 1 125 ? 5.342   10.369  -7.689  1.00 29.52 ? 125 PRO B CD  1 
ATOM   2855 N N   . ALA B 1 126 ? 7.047   13.680  -6.784  1.00 30.90 ? 126 ALA B N   1 
ATOM   2856 C CA  . ALA B 1 126 ? 7.495   14.987  -6.286  1.00 31.86 ? 126 ALA B CA  1 
ATOM   2857 C C   . ALA B 1 126 ? 8.502   14.831  -5.144  1.00 31.02 ? 126 ALA B C   1 
ATOM   2858 O O   . ALA B 1 126 ? 9.477   15.598  -5.039  1.00 28.02 ? 126 ALA B O   1 
ATOM   2859 C CB  . ALA B 1 126 ? 6.297   15.826  -5.825  1.00 32.27 ? 126 ALA B CB  1 
ATOM   2860 N N   . GLN B 1 127 ? 8.288   13.835  -4.292  1.00 27.89 ? 127 GLN B N   1 
ATOM   2861 C CA  . GLN B 1 127 ? 9.213   13.574  -3.202  1.00 31.25 ? 127 GLN B CA  1 
ATOM   2862 C C   . GLN B 1 127 ? 10.585  13.145  -3.725  1.00 28.39 ? 127 GLN B C   1 
ATOM   2863 O O   . GLN B 1 127 ? 11.609  13.585  -3.204  1.00 28.10 ? 127 GLN B O   1 
ATOM   2864 C CB  . GLN B 1 127 ? 8.654   12.489  -2.292  1.00 29.18 ? 127 GLN B CB  1 
ATOM   2865 C CG  . GLN B 1 127 ? 7.635   12.933  -1.322  1.00 28.11 ? 127 GLN B CG  1 
ATOM   2866 C CD  . GLN B 1 127 ? 7.113   11.756  -0.563  1.00 29.24 ? 127 GLN B CD  1 
ATOM   2867 O OE1 . GLN B 1 127 ? 6.648   10.776  -1.173  1.00 26.27 ? 127 GLN B OE1 1 
ATOM   2868 N NE2 . GLN B 1 127 ? 7.223   11.805  0.778   1.00 27.96 ? 127 GLN B NE2 1 
ATOM   2869 N N   . LEU B 1 128 ? 10.602  12.314  -4.777  1.00 28.32 ? 128 LEU B N   1 
ATOM   2870 C CA  . LEU B 1 128 ? 11.844  11.923  -5.439  1.00 29.28 ? 128 LEU B CA  1 
ATOM   2871 C C   . LEU B 1 128 ? 12.577  13.132  -6.026  1.00 29.22 ? 128 LEU B C   1 
ATOM   2872 O O   . LEU B 1 128 ? 13.796  13.280  -5.845  1.00 29.19 ? 128 LEU B O   1 
ATOM   2873 C CB  . LEU B 1 128 ? 11.554  10.901  -6.545  1.00 28.25 ? 128 LEU B CB  1 
ATOM   2874 C CG  . LEU B 1 128 ? 12.752  10.617  -7.486  1.00 31.39 ? 128 LEU B CG  1 
ATOM   2875 C CD1 . LEU B 1 128 ? 13.858  9.878   -6.721  1.00 23.21 ? 128 LEU B CD1 1 
ATOM   2876 C CD2 . LEU B 1 128 ? 12.343  9.822   -8.731  1.00 27.85 ? 128 LEU B CD2 1 
ATOM   2877 N N   . ILE B 1 129 ? 11.860  13.991  -6.769  1.00 29.52 ? 129 ILE B N   1 
ATOM   2878 C CA  . ILE B 1 129 ? 12.499  15.146  -7.409  1.00 28.68 ? 129 ILE B CA  1 
ATOM   2879 C C   . ILE B 1 129 ? 13.037  16.122  -6.364  1.00 30.23 ? 129 ILE B C   1 
ATOM   2880 O O   . ILE B 1 129 ? 14.141  16.676  -6.506  1.00 29.16 ? 129 ILE B O   1 
ATOM   2881 C CB  . ILE B 1 129 ? 11.521  15.834  -8.383  1.00 28.32 ? 129 ILE B CB  1 
ATOM   2882 C CG1 . ILE B 1 129 ? 11.298  14.943  -9.600  1.00 29.41 ? 129 ILE B CG1 1 
ATOM   2883 C CG2 . ILE B 1 129 ? 12.072  17.206  -8.857  1.00 30.39 ? 129 ILE B CG2 1 
ATOM   2884 C CD1 . ILE B 1 129 ? 10.131  15.316  -10.408 1.00 31.48 ? 129 ILE B CD1 1 
ATOM   2885 N N   . ALA B 1 130 ? 12.269  16.358  -5.311  1.00 30.82 ? 130 ALA B N   1 
ATOM   2886 C CA  . ALA B 1 130 ? 12.621  17.399  -4.360  1.00 31.49 ? 130 ALA B CA  1 
ATOM   2887 C C   . ALA B 1 130 ? 13.740  16.985  -3.415  1.00 32.03 ? 130 ALA B C   1 
ATOM   2888 O O   . ALA B 1 130 ? 14.513  17.841  -2.993  1.00 30.83 ? 130 ALA B O   1 
ATOM   2889 C CB  . ALA B 1 130 ? 11.393  17.792  -3.543  1.00 31.18 ? 130 ALA B CB  1 
ATOM   2890 N N   . ASN B 1 131 ? 13.859  15.695  -3.075  1.00 30.61 ? 131 ASN B N   1 
ATOM   2891 C CA  . ASN B 1 131 ? 14.780  15.276  -2.027  1.00 29.24 ? 131 ASN B CA  1 
ATOM   2892 C C   . ASN B 1 131 ? 16.017  14.546  -2.532  1.00 29.13 ? 131 ASN B C   1 
ATOM   2893 O O   . ASN B 1 131 ? 16.966  14.366  -1.756  1.00 25.47 ? 131 ASN B O   1 
ATOM   2894 C CB  . ASN B 1 131 ? 14.041  14.384  -1.023  1.00 27.97 ? 131 ASN B CB  1 
ATOM   2895 C CG  . ASN B 1 131 ? 13.007  15.183  -0.223  1.00 34.57 ? 131 ASN B CG  1 
ATOM   2896 O OD1 . ASN B 1 131 ? 13.380  16.152  0.414   1.00 32.77 ? 131 ASN B OD1 1 
ATOM   2897 N ND2 . ASN B 1 131 ? 11.702  14.831  -0.331  1.00 28.01 ? 131 ASN B ND2 1 
ATOM   2898 N N   . ALA B 1 132 ? 16.036  14.116  -3.788  1.00 25.48 ? 132 ALA B N   1 
ATOM   2899 C CA  . ALA B 1 132 ? 17.245  13.487  -4.308  1.00 26.86 ? 132 ALA B CA  1 
ATOM   2900 C C   . ALA B 1 132 ? 18.485  14.372  -4.206  1.00 28.44 ? 132 ALA B C   1 
ATOM   2901 O O   . ALA B 1 132 ? 19.578  13.812  -3.994  1.00 24.37 ? 132 ALA B O   1 
ATOM   2902 C CB  . ALA B 1 132 ? 17.029  13.019  -5.756  1.00 29.08 ? 132 ALA B CB  1 
ATOM   2903 N N   . PRO B 1 133 ? 18.402  15.710  -4.305  1.00 27.44 ? 133 PRO B N   1 
ATOM   2904 C CA  . PRO B 1 133 ? 19.629  16.520  -4.123  1.00 27.92 ? 133 PRO B CA  1 
ATOM   2905 C C   . PRO B 1 133 ? 20.268  16.346  -2.765  1.00 24.92 ? 133 PRO B C   1 
ATOM   2906 O O   . PRO B 1 133 ? 21.445  16.666  -2.610  1.00 29.42 ? 133 PRO B O   1 
ATOM   2907 C CB  . PRO B 1 133 ? 19.125  17.956  -4.336  1.00 29.28 ? 133 PRO B CB  1 
ATOM   2908 C CG  . PRO B 1 133 ? 18.061  17.773  -5.395  1.00 27.76 ? 133 PRO B CG  1 
ATOM   2909 C CD  . PRO B 1 133 ? 17.349  16.495  -4.996  1.00 25.77 ? 133 PRO B CD  1 
ATOM   2910 N N   . LYS B 1 134 ? 19.529  15.893  -1.757  1.00 26.06 ? 134 LYS B N   1 
ATOM   2911 C CA  . LYS B 1 134 ? 20.171  15.591  -0.476  1.00 26.82 ? 134 LYS B CA  1 
ATOM   2912 C C   . LYS B 1 134 ? 21.261  14.519  -0.622  1.00 27.63 ? 134 LYS B C   1 
ATOM   2913 O O   . LYS B 1 134 ? 22.169  14.458  0.205   1.00 24.90 ? 134 LYS B O   1 
ATOM   2914 C CB  . LYS B 1 134 ? 19.148  15.109  0.550   1.00 25.23 ? 134 LYS B CB  1 
ATOM   2915 C CG  . LYS B 1 134 ? 18.151  16.189  1.001   1.00 30.51 ? 134 LYS B CG  1 
ATOM   2916 C CD  . LYS B 1 134 ? 17.116  15.550  1.928   1.00 31.63 ? 134 LYS B CD  1 
ATOM   2917 C CE  . LYS B 1 134 ? 16.091  16.543  2.467   1.00 34.28 ? 134 LYS B CE  1 
ATOM   2918 N NZ  . LYS B 1 134 ? 15.058  15.700  3.137   1.00 36.48 ? 134 LYS B NZ  1 
ATOM   2919 N N   . LEU B 1 135 ? 21.140  13.618  -1.601  1.00 27.38 ? 135 LEU B N   1 
ATOM   2920 C CA  . LEU B 1 135 ? 22.108  12.536  -1.771  1.00 26.54 ? 135 LEU B CA  1 
ATOM   2921 C C   . LEU B 1 135 ? 23.133  12.854  -2.857  1.00 29.06 ? 135 LEU B C   1 
ATOM   2922 O O   . LEU B 1 135 ? 24.029  12.041  -3.107  1.00 28.58 ? 135 LEU B O   1 
ATOM   2923 C CB  . LEU B 1 135 ? 21.401  11.202  -2.066  1.00 24.79 ? 135 LEU B CB  1 
ATOM   2924 C CG  . LEU B 1 135 ? 20.381  10.645  -1.042  1.00 26.71 ? 135 LEU B CG  1 
ATOM   2925 C CD1 . LEU B 1 135 ? 19.041  10.480  -1.683  1.00 31.90 ? 135 LEU B CD1 1 
ATOM   2926 C CD2 . LEU B 1 135 ? 20.747  9.302   -0.474  1.00 30.56 ? 135 LEU B CD2 1 
ATOM   2927 N N   . GLY B 1 136 ? 23.043  14.042  -3.471  1.00 26.97 ? 136 GLY B N   1 
ATOM   2928 C CA  . GLY B 1 136 ? 23.933  14.460  -4.517  1.00 28.16 ? 136 GLY B CA  1 
ATOM   2929 C C   . GLY B 1 136 ? 23.434  14.286  -5.929  1.00 28.39 ? 136 GLY B C   1 
ATOM   2930 O O   . GLY B 1 136 ? 24.233  14.467  -6.863  1.00 30.90 ? 136 GLY B O   1 
ATOM   2931 N N   . PHE B 1 137 ? 22.148  14.005  -6.123  1.00 25.13 ? 137 PHE B N   1 
ATOM   2932 C CA  . PHE B 1 137 ? 21.591  13.772  -7.450  1.00 26.26 ? 137 PHE B CA  1 
ATOM   2933 C C   . PHE B 1 137 ? 20.628  14.894  -7.867  1.00 29.05 ? 137 PHE B C   1 
ATOM   2934 O O   . PHE B 1 137 ? 20.100  15.630  -7.045  1.00 27.57 ? 137 PHE B O   1 
ATOM   2935 C CB  . PHE B 1 137 ? 20.845  12.426  -7.499  1.00 25.71 ? 137 PHE B CB  1 
ATOM   2936 C CG  . PHE B 1 137 ? 21.688  11.285  -7.041  1.00 21.08 ? 137 PHE B CG  1 
ATOM   2937 C CD1 . PHE B 1 137 ? 22.820  10.927  -7.768  1.00 24.43 ? 137 PHE B CD1 1 
ATOM   2938 C CD2 . PHE B 1 137 ? 21.411  10.642  -5.857  1.00 22.32 ? 137 PHE B CD2 1 
ATOM   2939 C CE1 . PHE B 1 137 ? 23.649  9.858   -7.344  1.00 25.76 ? 137 PHE B CE1 1 
ATOM   2940 C CE2 . PHE B 1 137 ? 22.241  9.575   -5.399  1.00 25.93 ? 137 PHE B CE2 1 
ATOM   2941 C CZ  . PHE B 1 137 ? 23.344  9.179   -6.155  1.00 23.06 ? 137 PHE B CZ  1 
ATOM   2942 N N   . LYS B 1 138 ? 20.428  15.022  -9.169  1.00 28.00 ? 138 LYS B N   1 
ATOM   2943 C CA  . LYS B 1 138 ? 19.368  15.849  -9.710  1.00 32.01 ? 138 LYS B CA  1 
ATOM   2944 C C   . LYS B 1 138 ? 18.480  14.955  -10.560 1.00 30.53 ? 138 LYS B C   1 
ATOM   2945 O O   . LYS B 1 138 ? 18.972  14.111  -11.314 1.00 26.56 ? 138 LYS B O   1 
ATOM   2946 C CB  . LYS B 1 138 ? 19.905  17.029  -10.544 1.00 31.65 ? 138 LYS B CB  1 
ATOM   2947 C CG  . LYS B 1 138 ? 18.776  17.942  -11.026 1.00 36.82 ? 138 LYS B CG  1 
ATOM   2948 C CD  . LYS B 1 138 ? 19.293  19.289  -11.483 1.00 39.11 ? 138 LYS B CD  1 
ATOM   2949 C CE  . LYS B 1 138 ? 20.352  19.124  -12.541 1.00 42.11 ? 138 LYS B CE  1 
ATOM   2950 N NZ  . LYS B 1 138 ? 20.028  19.995  -13.728 1.00 49.61 ? 138 LYS B NZ  1 
ATOM   2951 N N   . ILE B 1 139 ? 17.173  15.137  -10.394 1.00 28.61 ? 139 ILE B N   1 
ATOM   2952 C CA  . ILE B 1 139 ? 16.187  14.362  -11.182 1.00 28.24 ? 139 ILE B CA  1 
ATOM   2953 C C   . ILE B 1 139 ? 15.700  15.257  -12.319 1.00 31.78 ? 139 ILE B C   1 
ATOM   2954 O O   . ILE B 1 139 ? 15.358  16.381  -12.054 1.00 37.80 ? 139 ILE B O   1 
ATOM   2955 C CB  . ILE B 1 139 ? 15.031  13.897  -10.285 1.00 29.60 ? 139 ILE B CB  1 
ATOM   2956 C CG1 . ILE B 1 139 ? 15.510  13.126  -9.051  1.00 32.11 ? 139 ILE B CG1 1 
ATOM   2957 C CG2 . ILE B 1 139 ? 14.018  13.108  -11.087 1.00 26.66 ? 139 ILE B CG2 1 
ATOM   2958 C CD1 . ILE B 1 139 ? 16.480  12.017  -9.321  1.00 29.72 ? 139 ILE B CD1 1 
ATOM   2959 N N   . ILE B 1 140 ? 15.687  14.740  -13.536 1.00 32.26 ? 140 ILE B N   1 
ATOM   2960 C CA  . ILE B 1 140 ? 15.201  15.486  -14.726 1.00 36.25 ? 140 ILE B CA  1 
ATOM   2961 C C   . ILE B 1 140 ? 13.935  14.806  -15.240 1.00 32.88 ? 140 ILE B C   1 
ATOM   2962 O O   . ILE B 1 140 ? 14.053  13.763  -15.828 1.00 34.53 ? 140 ILE B O   1 
ATOM   2963 C CB  . ILE B 1 140 ? 16.288  15.523  -15.805 1.00 31.46 ? 140 ILE B CB  1 
ATOM   2964 C CG1 . ILE B 1 140 ? 17.569  16.153  -15.263 1.00 36.92 ? 140 ILE B CG1 1 
ATOM   2965 C CG2 . ILE B 1 140 ? 15.786  16.250  -17.033 1.00 35.73 ? 140 ILE B CG2 1 
ATOM   2966 C CD1 . ILE B 1 140 ? 18.703  16.181  -16.231 1.00 37.52 ? 140 ILE B CD1 1 
ATOM   2967 N N   . PRO B 1 141 ? 12.724  15.311  -14.960 1.00 35.01 ? 141 PRO B N   1 
ATOM   2968 C CA  . PRO B 1 141 ? 11.521  14.693  -15.486 1.00 34.81 ? 141 PRO B CA  1 
ATOM   2969 C C   . PRO B 1 141 ? 11.578  14.732  -17.017 1.00 36.50 ? 141 PRO B C   1 
ATOM   2970 O O   . PRO B 1 141 ? 11.852  15.750  -17.564 1.00 40.43 ? 141 PRO B O   1 
ATOM   2971 C CB  . PRO B 1 141 ? 10.394  15.570  -14.954 1.00 35.25 ? 141 PRO B CB  1 
ATOM   2972 C CG  . PRO B 1 141 ? 10.989  16.266  -13.777 1.00 35.75 ? 141 PRO B CG  1 
ATOM   2973 C CD  . PRO B 1 141 ? 12.451  16.430  -14.099 1.00 32.37 ? 141 PRO B CD  1 
ATOM   2974 N N   . ILE B 1 142 ? 11.394  13.589  -17.654 1.00 35.27 ? 142 ILE B N   1 
ATOM   2975 C CA  . ILE B 1 142 ? 11.419  13.519  -19.138 1.00 38.55 ? 142 ILE B CA  1 
ATOM   2976 C C   . ILE B 1 142 ? 10.096  12.934  -19.619 1.00 36.61 ? 142 ILE B C   1 
ATOM   2977 O O   . ILE B 1 142 ? 9.367   12.404  -18.817 1.00 38.03 ? 142 ILE B O   1 
ATOM   2978 C CB  . ILE B 1 142 ? 12.598  12.672  -19.656 1.00 37.32 ? 142 ILE B CB  1 
ATOM   2979 C CG1 . ILE B 1 142 ? 12.465  11.204  -19.256 1.00 34.21 ? 142 ILE B CG1 1 
ATOM   2980 C CG2 . ILE B 1 142 ? 13.933  13.251  -19.235 1.00 38.62 ? 142 ILE B CG2 1 
ATOM   2981 C CD1 . ILE B 1 142 ? 13.277  10.273  -20.095 1.00 34.39 ? 142 ILE B CD1 1 
ATOM   2982 N N   . LYS B 1 143 ? 9.826   13.067  -20.911 1.00 49.14 ? 143 LYS B N   1 
ATOM   2983 C CA  . LYS B 1 143 ? 8.603   12.503  -21.515 1.00 43.07 ? 143 LYS B CA  1 
ATOM   2984 C C   . LYS B 1 143 ? 8.722   10.980  -21.535 1.00 41.39 ? 143 LYS B C   1 
ATOM   2985 O O   . LYS B 1 143 ? 9.820   10.490  -21.702 1.00 41.82 ? 143 LYS B O   1 
ATOM   2986 C CB  . LYS B 1 143 ? 8.469   13.036  -22.942 1.00 43.99 ? 143 LYS B CB  1 
ATOM   2987 C CG  . LYS B 1 143 ? 7.993   14.476  -23.074 1.00 51.64 ? 143 LYS B CG  1 
ATOM   2988 C CD  . LYS B 1 143 ? 6.486   14.609  -22.980 1.00 56.35 ? 143 LYS B CD  1 
ATOM   2989 C CE  . LYS B 1 143 ? 5.864   15.428  -24.096 1.00 59.32 ? 143 LYS B CE  1 
ATOM   2990 N NZ  . LYS B 1 143 ? 4.375   15.413  -24.094 1.00 61.26 ? 143 LYS B NZ  1 
ATOM   2991 N N   . ARG B 1 144 ? 7.607   10.277  -21.369 1.00 41.11 ? 144 ARG B N   1 
ATOM   2992 C CA  . ARG B 1 144 ? 7.602   8.798   -21.434 1.00 38.13 ? 144 ARG B CA  1 
ATOM   2993 C C   . ARG B 1 144 ? 7.801   8.415   -22.898 1.00 38.87 ? 144 ARG B C   1 
ATOM   2994 O O   . ARG B 1 144 ? 6.856   8.023   -23.523 1.00 39.62 ? 144 ARG B O   1 
ATOM   2995 C CB  . ARG B 1 144 ? 6.294   8.269   -20.845 1.00 36.67 ? 144 ARG B CB  1 
ATOM   2996 C CG  . ARG B 1 144 ? 6.080   8.657   -19.394 1.00 34.93 ? 144 ARG B CG  1 
ATOM   2997 C CD  . ARG B 1 144 ? 4.859   8.100   -18.710 1.00 34.16 ? 144 ARG B CD  1 
ATOM   2998 N NE  . ARG B 1 144 ? 4.841   6.670   -18.484 1.00 33.83 ? 144 ARG B NE  1 
ATOM   2999 C CZ  . ARG B 1 144 ? 5.077   6.093   -17.320 1.00 32.01 ? 144 ARG B CZ  1 
ATOM   3000 N NH1 . ARG B 1 144 ? 5.407   6.815   -16.268 1.00 28.52 ? 144 ARG B NH1 1 
ATOM   3001 N NH2 . ARG B 1 144 ? 4.996   4.787   -17.220 1.00 32.93 ? 144 ARG B NH2 1 
ATOM   3002 N N   . ASP B 1 145 ? 9.031   8.510   -23.385 1.00 41.92 ? 145 ASP B N   1 
ATOM   3003 C CA  . ASP B 1 145 ? 9.306   8.256   -24.799 1.00 41.69 ? 145 ASP B CA  1 
ATOM   3004 C C   . ASP B 1 145 ? 10.713  7.684   -24.937 1.00 42.03 ? 145 ASP B C   1 
ATOM   3005 O O   . ASP B 1 145 ? 11.662  8.210   -24.343 1.00 43.62 ? 145 ASP B O   1 
ATOM   3006 C CB  . ASP B 1 145 ? 9.107   9.535   -25.651 1.00 43.05 ? 145 ASP B CB  1 
ATOM   3007 C CG  . ASP B 1 145 ? 9.924   9.554   -26.946 1.00 44.36 ? 145 ASP B CG  1 
ATOM   3008 O OD1 . ASP B 1 145 ? 10.233  8.519   -27.563 1.00 48.43 ? 145 ASP B OD1 1 
ATOM   3009 O OD2 . ASP B 1 145 ? 10.301  10.662  -27.356 1.00 53.81 ? 145 ASP B OD2 1 
ATOM   3010 N N   . SER B 1 146 ? 10.844  6.621   -25.745 1.00 41.57 ? 146 SER B N   1 
ATOM   3011 C CA  . SER B 1 146 ? 12.100  5.879   -25.840 1.00 44.09 ? 146 SER B CA  1 
ATOM   3012 C C   . SER B 1 146 ? 13.229  6.739   -26.382 1.00 43.19 ? 146 SER B C   1 
ATOM   3013 O O   . SER B 1 146 ? 14.406  6.435   -26.129 1.00 44.82 ? 146 SER B O   1 
ATOM   3014 C CB  . SER B 1 146 ? 11.923  4.617   -26.704 1.00 44.33 ? 146 SER B CB  1 
ATOM   3015 O OG  . SER B 1 146 ? 11.618  4.920   -28.059 1.00 43.73 ? 146 SER B OG  1 
ATOM   3016 N N   . LYS B 1 147 ? 12.904  7.790   -27.153 1.00 44.10 ? 147 LYS B N   1 
ATOM   3017 C CA  . LYS B 1 147 ? 13.950  8.682   -27.674 1.00 44.61 ? 147 LYS B CA  1 
ATOM   3018 C C   . LYS B 1 147 ? 14.607  9.468   -26.550 1.00 40.25 ? 147 LYS B C   1 
ATOM   3019 O O   . LYS B 1 147 ? 15.835  9.630   -26.533 1.00 42.28 ? 147 LYS B O   1 
ATOM   3020 C CB  . LYS B 1 147 ? 13.386  9.663   -28.709 1.00 47.74 ? 147 LYS B CB  1 
ATOM   3021 C CG  . LYS B 1 147 ? 13.472  9.212   -30.156 1.00 48.42 ? 147 LYS B CG  1 
ATOM   3022 C CD  . LYS B 1 147 ? 12.127  8.705   -30.673 1.00 52.66 ? 147 LYS B CD  1 
ATOM   3023 C CE  . LYS B 1 147 ? 12.279  8.021   -32.048 1.00 56.50 ? 147 LYS B CE  1 
ATOM   3024 N NZ  . LYS B 1 147 ? 11.565  6.702   -32.110 1.00 54.45 ? 147 LYS B NZ  1 
ATOM   3025 N N   . GLU B 1 148 ? 13.819  9.976   -25.612 1.00 38.67 ? 148 GLU B N   1 
ATOM   3026 C CA  . GLU B 1 148 ? 14.425  10.687  -24.495 1.00 40.83 ? 148 GLU B CA  1 
ATOM   3027 C C   . GLU B 1 148 ? 15.216  9.724   -23.611 1.00 41.44 ? 148 GLU B C   1 
ATOM   3028 O O   . GLU B 1 148 ? 16.361  10.015  -23.240 1.00 37.97 ? 148 GLU B O   1 
ATOM   3029 C CB  . GLU B 1 148 ? 13.355  11.412  -23.683 1.00 41.54 ? 148 GLU B CB  1 
ATOM   3030 C CG  . GLU B 1 148 ? 12.772  12.651  -24.368 1.00 46.95 ? 148 GLU B CG  1 
ATOM   3031 C CD  . GLU B 1 148 ? 13.745  13.808  -24.339 1.00 45.63 ? 148 GLU B CD  1 
ATOM   3032 O OE1 . GLU B 1 148 ? 13.735  14.554  -23.341 1.00 50.62 ? 148 GLU B OE1 1 
ATOM   3033 O OE2 . GLU B 1 148 ? 14.516  13.960  -25.303 1.00 45.66 ? 148 GLU B OE2 1 
ATOM   3034 N N   . VAL B 1 149 ? 14.655  8.546   -23.325 1.00 37.04 ? 149 VAL B N   1 
ATOM   3035 C CA  . VAL B 1 149 ? 15.368  7.575   -22.500 1.00 37.35 ? 149 VAL B CA  1 
ATOM   3036 C C   . VAL B 1 149 ? 16.715  7.244   -23.124 1.00 38.59 ? 149 VAL B C   1 
ATOM   3037 O O   . VAL B 1 149 ? 17.753  7.258   -22.446 1.00 36.20 ? 149 VAL B O   1 
ATOM   3038 C CB  . VAL B 1 149 ? 14.515  6.314   -22.277 1.00 38.25 ? 149 VAL B CB  1 
ATOM   3039 C CG1 . VAL B 1 149 ? 15.272  5.290   -21.427 1.00 35.89 ? 149 VAL B CG1 1 
ATOM   3040 C CG2 . VAL B 1 149 ? 13.169  6.664   -21.629 1.00 35.05 ? 149 VAL B CG2 1 
ATOM   3041 N N   . LYS B 1 150 ? 16.733  6.995   -24.437 1.00 39.85 ? 150 LYS B N   1 
ATOM   3042 C CA  . LYS B 1 150 ? 17.984  6.639   -25.095 1.00 40.32 ? 150 LYS B CA  1 
ATOM   3043 C C   . LYS B 1 150 ? 18.988  7.788   -25.030 1.00 41.06 ? 150 LYS B C   1 
ATOM   3044 O O   . LYS B 1 150 ? 20.185  7.576   -24.793 1.00 41.24 ? 150 LYS B O   1 
ATOM   3045 C CB  . LYS B 1 150 ? 17.723  6.237   -26.550 1.00 44.98 ? 150 LYS B CB  1 
ATOM   3046 C CG  . LYS B 1 150 ? 18.960  5.616   -27.250 1.00 45.01 ? 150 LYS B CG  1 
ATOM   3047 C CD  . LYS B 1 150 ? 18.765  5.455   -28.766 1.00 53.58 ? 150 LYS B CD  1 
ATOM   3048 C CE  . LYS B 1 150 ? 17.934  4.195   -29.116 1.00 56.18 ? 150 LYS B CE  1 
ATOM   3049 N NZ  . LYS B 1 150 ? 17.359  4.208   -30.518 1.00 55.27 ? 150 LYS B NZ  1 
ATOM   3050 N N   . LYS B 1 151 ? 18.506  9.020   -25.189 1.00 42.11 ? 151 LYS B N   1 
ATOM   3051 C CA  . LYS B 1 151 ? 19.411  10.155  -25.173 1.00 42.66 ? 151 LYS B CA  1 
ATOM   3052 C C   . LYS B 1 151 ? 20.125  10.264  -23.839 1.00 42.49 ? 151 LYS B C   1 
ATOM   3053 O O   . LYS B 1 151 ? 21.344  10.494  -23.786 1.00 41.56 ? 151 LYS B O   1 
ATOM   3054 C CB  . LYS B 1 151 ? 18.645  11.433  -25.462 1.00 40.01 ? 151 LYS B CB  1 
ATOM   3055 C CG  . LYS B 1 151 ? 19.495  12.661  -25.295 1.00 42.10 ? 151 LYS B CG  1 
ATOM   3056 C CD  . LYS B 1 151 ? 18.722  13.911  -25.725 1.00 45.58 ? 151 LYS B CD  1 
ATOM   3057 C CE  . LYS B 1 151 ? 18.036  14.543  -24.566 1.00 43.96 ? 151 LYS B CE  1 
ATOM   3058 N NZ  . LYS B 1 151 ? 18.923  15.536  -23.941 1.00 47.12 ? 151 LYS B NZ  1 
ATOM   3059 N N   . TYR B 1 152 ? 19.390  10.066  -22.749 1.00 39.20 ? 152 TYR B N   1 
ATOM   3060 C CA  . TYR B 1 152 ? 19.983  10.250  -21.434 1.00 39.68 ? 152 TYR B CA  1 
ATOM   3061 C C   . TYR B 1 152 ? 20.784  9.032   -20.997 1.00 36.46 ? 152 TYR B C   1 
ATOM   3062 O O   . TYR B 1 152 ? 21.800  9.173   -20.300 1.00 38.16 ? 152 TYR B O   1 
ATOM   3063 C CB  . TYR B 1 152 ? 18.884  10.589  -20.428 1.00 37.71 ? 152 TYR B CB  1 
ATOM   3064 C CG  . TYR B 1 152 ? 18.488  12.042  -20.512 1.00 40.50 ? 152 TYR B CG  1 
ATOM   3065 C CD1 . TYR B 1 152 ? 19.279  13.037  -19.928 1.00 40.95 ? 152 TYR B CD1 1 
ATOM   3066 C CD2 . TYR B 1 152 ? 17.343  12.430  -21.209 1.00 37.76 ? 152 TYR B CD2 1 
ATOM   3067 C CE1 . TYR B 1 152 ? 18.921  14.384  -20.018 1.00 39.60 ? 152 TYR B CE1 1 
ATOM   3068 C CE2 . TYR B 1 152 ? 16.974  13.760  -21.297 1.00 40.21 ? 152 TYR B CE2 1 
ATOM   3069 C CZ  . TYR B 1 152 ? 17.766  14.733  -20.703 1.00 42.07 ? 152 TYR B CZ  1 
ATOM   3070 O OH  . TYR B 1 152 ? 17.374  16.054  -20.800 1.00 40.88 ? 152 TYR B OH  1 
ATOM   3071 N N   . LEU B 1 153 ? 20.410  7.849   -21.477 1.00 36.44 ? 153 LEU B N   1 
ATOM   3072 C CA  . LEU B 1 153 ? 21.227  6.668   -21.241 1.00 35.44 ? 153 LEU B CA  1 
ATOM   3073 C C   . LEU B 1 153 ? 22.584  6.795   -21.925 1.00 38.38 ? 153 LEU B C   1 
ATOM   3074 O O   . LEU B 1 153 ? 23.566  6.187   -21.484 1.00 38.17 ? 153 LEU B O   1 
ATOM   3075 C CB  . LEU B 1 153 ? 20.494  5.414   -21.707 1.00 34.63 ? 153 LEU B CB  1 
ATOM   3076 C CG  . LEU B 1 153 ? 19.406  4.879   -20.778 1.00 36.13 ? 153 LEU B CG  1 
ATOM   3077 C CD1 . LEU B 1 153 ? 18.810  3.614   -21.389 1.00 37.99 ? 153 LEU B CD1 1 
ATOM   3078 C CD2 . LEU B 1 153 ? 19.963  4.574   -19.415 1.00 31.96 ? 153 LEU B CD2 1 
ATOM   3079 N N   . LYS B 1 154 ? 22.648  7.531   -23.033 1.00 40.11 ? 154 LYS B N   1 
ATOM   3080 C CA  . LYS B 1 154 ? 23.923  7.733   -23.719 1.00 41.98 ? 154 LYS B CA  1 
ATOM   3081 C C   . LYS B 1 154 ? 24.867  8.665   -22.951 1.00 40.00 ? 154 LYS B C   1 
ATOM   3082 O O   . LYS B 1 154 ? 26.085  8.556   -23.105 1.00 40.09 ? 154 LYS B O   1 
ATOM   3083 C CB  . LYS B 1 154 ? 23.663  8.236   -25.136 1.00 45.93 ? 154 LYS B CB  1 
ATOM   3084 C CG  . LYS B 1 154 ? 24.897  8.236   -26.027 1.00 48.07 ? 154 LYS B CG  1 
ATOM   3085 C CD  . LYS B 1 154 ? 24.506  8.424   -27.510 1.00 49.94 ? 154 LYS B CD  1 
ATOM   3086 C CE  . LYS B 1 154 ? 25.565  9.239   -28.242 1.00 51.10 ? 154 LYS B CE  1 
ATOM   3087 N NZ  . LYS B 1 154 ? 25.145  10.638  -28.565 1.00 48.86 ? 154 LYS B NZ  1 
ATOM   3088 N N   . LYS B 1 155 ? 24.310  9.569   -22.149 1.00 39.52 ? 155 LYS B N   1 
ATOM   3089 C CA  . LYS B 1 155 ? 25.153  10.484  -21.341 1.00 40.61 ? 155 LYS B CA  1 
ATOM   3090 C C   . LYS B 1 155 ? 25.591  9.786   -20.055 1.00 37.94 ? 155 LYS B C   1 
ATOM   3091 O O   . LYS B 1 155 ? 26.278  10.401  -19.290 1.00 41.77 ? 155 LYS B O   1 
ATOM   3092 C CB  . LYS B 1 155 ? 24.435  11.784  -20.981 1.00 37.19 ? 155 LYS B CB  1 
ATOM   3093 C CG  . LYS B 1 155 ? 23.213  12.122  -21.805 1.00 42.28 ? 155 LYS B CG  1 
ATOM   3094 C CD  . LYS B 1 155 ? 22.769  13.546  -21.629 1.00 41.82 ? 155 LYS B CD  1 
ATOM   3095 C CE  . LYS B 1 155 ? 23.165  14.432  -22.781 1.00 44.32 ? 155 LYS B CE  1 
ATOM   3096 N NZ  . LYS B 1 155 ? 22.198  15.531  -22.978 1.00 45.91 ? 155 LYS B NZ  1 
ATOM   3097 N N   . GLY B 1 156 ? 25.210  8.531   -19.867 1.00 38.19 ? 156 GLY B N   1 
ATOM   3098 C CA  . GLY B 1 156 ? 25.524  7.788   -18.657 1.00 35.83 ? 156 GLY B CA  1 
ATOM   3099 C C   . GLY B 1 156 ? 24.492  7.873   -17.544 1.00 35.63 ? 156 GLY B C   1 
ATOM   3100 O O   . GLY B 1 156 ? 24.786  7.457   -16.410 1.00 31.72 ? 156 GLY B O   1 
ATOM   3101 N N   . PHE B 1 157 ? 23.293  8.386   -17.819 1.00 32.48 ? 157 PHE B N   1 
ATOM   3102 C CA  . PHE B 1 157 ? 22.333  8.642   -16.753 1.00 30.74 ? 157 PHE B CA  1 
ATOM   3103 C C   . PHE B 1 157 ? 21.214  7.619   -16.802 1.00 30.41 ? 157 PHE B C   1 
ATOM   3104 O O   . PHE B 1 157 ? 20.515  7.531   -17.818 1.00 29.63 ? 157 PHE B O   1 
ATOM   3105 C CB  . PHE B 1 157 ? 21.766  10.058  -16.865 1.00 32.76 ? 157 PHE B CB  1 
ATOM   3106 C CG  . PHE B 1 157 ? 22.817  11.149  -16.821 1.00 32.61 ? 157 PHE B CG  1 
ATOM   3107 C CD1 . PHE B 1 157 ? 24.063  10.927  -16.252 1.00 32.14 ? 157 PHE B CD1 1 
ATOM   3108 C CD2 . PHE B 1 157 ? 22.540  12.403  -17.334 1.00 35.57 ? 157 PHE B CD2 1 
ATOM   3109 C CE1 . PHE B 1 157 ? 25.019  11.929  -16.210 1.00 34.68 ? 157 PHE B CE1 1 
ATOM   3110 C CE2 . PHE B 1 157 ? 23.484  13.419  -17.293 1.00 34.44 ? 157 PHE B CE2 1 
ATOM   3111 C CZ  . PHE B 1 157 ? 24.730  13.190  -16.726 1.00 33.22 ? 157 PHE B CZ  1 
ATOM   3112 N N   . PRO B 1 158 ? 20.995  6.842   -15.752 1.00 30.28 ? 158 PRO B N   1 
ATOM   3113 C CA  . PRO B 1 158 ? 19.884  5.892   -15.761 1.00 27.74 ? 158 PRO B CA  1 
ATOM   3114 C C   . PRO B 1 158 ? 18.557  6.622   -15.517 1.00 28.77 ? 158 PRO B C   1 
ATOM   3115 O O   . PRO B 1 158 ? 18.519  7.775   -15.091 1.00 29.29 ? 158 PRO B O   1 
ATOM   3116 C CB  . PRO B 1 158 ? 20.265  4.934   -14.622 1.00 25.28 ? 158 PRO B CB  1 
ATOM   3117 C CG  . PRO B 1 158 ? 20.978  5.783   -13.679 1.00 25.68 ? 158 PRO B CG  1 
ATOM   3118 C CD  . PRO B 1 158 ? 21.752  6.801   -14.489 1.00 27.62 ? 158 PRO B CD  1 
ATOM   3119 N N   . VAL B 1 159 ? 17.450  5.925   -15.775 1.00 26.42 ? 159 VAL B N   1 
ATOM   3120 C CA  . VAL B 1 159 ? 16.132  6.569   -15.812 1.00 27.51 ? 159 VAL B CA  1 
ATOM   3121 C C   . VAL B 1 159 ? 15.162  5.782   -14.953 1.00 27.02 ? 159 VAL B C   1 
ATOM   3122 O O   . VAL B 1 159 ? 14.857  4.618   -15.259 1.00 26.78 ? 159 VAL B O   1 
ATOM   3123 C CB  . VAL B 1 159 ? 15.569  6.687   -17.237 1.00 27.13 ? 159 VAL B CB  1 
ATOM   3124 C CG1 . VAL B 1 159 ? 14.251  7.428   -17.175 1.00 27.01 ? 159 VAL B CG1 1 
ATOM   3125 C CG2 . VAL B 1 159 ? 16.561  7.380   -18.157 1.00 28.48 ? 159 VAL B CG2 1 
ATOM   3126 N N   . ILE B 1 160 ? 14.692  6.404   -13.871 1.00 29.11 ? 160 ILE B N   1 
ATOM   3127 C CA  . ILE B 1 160 ? 13.686  5.782   -13.015 1.00 24.79 ? 160 ILE B CA  1 
ATOM   3128 C C   . ILE B 1 160 ? 12.337  5.819   -13.708 1.00 25.91 ? 160 ILE B C   1 
ATOM   3129 O O   . ILE B 1 160 ? 11.890  6.874   -14.183 1.00 30.32 ? 160 ILE B O   1 
ATOM   3130 C CB  . ILE B 1 160 ? 13.626  6.464   -11.636 1.00 23.18 ? 160 ILE B CB  1 
ATOM   3131 C CG1 . ILE B 1 160 ? 14.873  6.100   -10.813 1.00 24.27 ? 160 ILE B CG1 1 
ATOM   3132 C CG2 . ILE B 1 160 ? 12.288  6.092   -10.887 1.00 22.48 ? 160 ILE B CG2 1 
ATOM   3133 C CD1 . ILE B 1 160 ? 14.959  6.808   -9.459  1.00 22.58 ? 160 ILE B CD1 1 
ATOM   3134 N N   . CYS B 1 161 ? 11.665  4.674   -13.742 1.00 28.55 ? 161 CYS B N   1 
ATOM   3135 C CA  . CYS B 1 161 ? 10.348  4.585   -14.348 1.00 28.19 ? 161 CYS B CA  1 
ATOM   3136 C C   . CYS B 1 161 ? 9.295   4.330   -13.275 1.00 31.20 ? 161 CYS B C   1 
ATOM   3137 O O   . CYS B 1 161 ? 9.555   3.710   -12.237 1.00 29.88 ? 161 CYS B O   1 
ATOM   3138 C CB  . CYS B 1 161 ? 10.271  3.480   -15.413 1.00 28.67 ? 161 CYS B CB  1 
ATOM   3139 S SG  . CYS B 1 161 ? 10.781  1.782   -14.854 1.00 31.03 ? 161 CYS B SG  1 
ATOM   3140 N N   . HIS B 1 162 ? 8.078   4.779   -13.572 1.00 28.91 ? 162 HIS B N   1 
ATOM   3141 C CA  . HIS B 1 162 ? 6.951   4.698   -12.670 1.00 29.66 ? 162 HIS B CA  1 
ATOM   3142 C C   . HIS B 1 162 ? 5.741   4.230   -13.465 1.00 30.39 ? 162 HIS B C   1 
ATOM   3143 O O   . HIS B 1 162 ? 5.466   4.760   -14.553 1.00 30.40 ? 162 HIS B O   1 
ATOM   3144 C CB  . HIS B 1 162 ? 6.721   6.064   -12.010 1.00 29.71 ? 162 HIS B CB  1 
ATOM   3145 C CG  . HIS B 1 162 ? 5.534   6.111   -11.111 1.00 31.89 ? 162 HIS B CG  1 
ATOM   3146 N ND1 . HIS B 1 162 ? 4.486   6.986   -11.311 1.00 35.32 ? 162 HIS B ND1 1 
ATOM   3147 C CD2 . HIS B 1 162 ? 5.210   5.376   -10.020 1.00 31.51 ? 162 HIS B CD2 1 
ATOM   3148 C CE1 . HIS B 1 162 ? 3.584   6.808   -10.362 1.00 37.65 ? 162 HIS B CE1 1 
ATOM   3149 N NE2 . HIS B 1 162 ? 3.991   5.828   -9.575  1.00 34.64 ? 162 HIS B NE2 1 
ATOM   3150 N N   . TRP B 1 163 ? 5.033   3.222   -12.949 1.00 34.73 ? 163 TRP B N   1 
ATOM   3151 C CA  . TRP B 1 163 ? 3.890   2.682   -13.688 1.00 33.14 ? 163 TRP B CA  1 
ATOM   3152 C C   . TRP B 1 163 ? 2.945   1.945   -12.750 1.00 32.24 ? 163 TRP B C   1 
ATOM   3153 O O   . TRP B 1 163 ? 3.277   1.640   -11.604 1.00 31.68 ? 163 TRP B O   1 
ATOM   3154 C CB  . TRP B 1 163 ? 4.358   1.797   -14.860 1.00 32.59 ? 163 TRP B CB  1 
ATOM   3155 C CG  . TRP B 1 163 ? 4.732   0.332   -14.571 1.00 35.17 ? 163 TRP B CG  1 
ATOM   3156 C CD1 . TRP B 1 163 ? 3.995   -0.772  -14.876 1.00 33.19 ? 163 TRP B CD1 1 
ATOM   3157 C CD2 . TRP B 1 163 ? 5.947   -0.153  -13.974 1.00 31.87 ? 163 TRP B CD2 1 
ATOM   3158 N NE1 . TRP B 1 163 ? 4.675   -1.917  -14.527 1.00 34.21 ? 163 TRP B NE1 1 
ATOM   3159 C CE2 . TRP B 1 163 ? 5.865   -1.566  -13.950 1.00 33.78 ? 163 TRP B CE2 1 
ATOM   3160 C CE3 . TRP B 1 163 ? 7.096   0.471   -13.456 1.00 31.17 ? 163 TRP B CE3 1 
ATOM   3161 C CZ2 . TRP B 1 163 ? 6.888   -2.377  -13.414 1.00 32.64 ? 163 TRP B CZ2 1 
ATOM   3162 C CZ3 . TRP B 1 163 ? 8.119   -0.334  -12.933 1.00 29.78 ? 163 TRP B CZ3 1 
ATOM   3163 C CH2 . TRP B 1 163 ? 8.011   -1.746  -12.928 1.00 30.26 ? 163 TRP B CH2 1 
ATOM   3164 N N   . GLN B 1 164 ? 1.737   1.681   -13.255 1.00 31.68 ? 164 GLN B N   1 
ATOM   3165 C CA  . GLN B 1 164 ? 0.727   0.908   -12.537 1.00 33.43 ? 164 GLN B CA  1 
ATOM   3166 C C   . GLN B 1 164 ? 0.765   -0.526  -13.064 1.00 33.63 ? 164 GLN B C   1 
ATOM   3167 O O   . GLN B 1 164 ? 0.575   -0.756  -14.261 1.00 33.65 ? 164 GLN B O   1 
ATOM   3168 C CB  . GLN B 1 164 ? -0.658  1.532   -12.691 1.00 35.77 ? 164 GLN B CB  1 
ATOM   3169 C CG  . GLN B 1 164 ? -0.645  3.051   -12.514 1.00 33.67 ? 164 GLN B CG  1 
ATOM   3170 C CD  . GLN B 1 164 ? -0.366  3.492   -11.092 1.00 34.64 ? 164 GLN B CD  1 
ATOM   3171 O OE1 . GLN B 1 164 ? -0.866  2.913   -10.155 1.00 34.33 ? 164 GLN B OE1 1 
ATOM   3172 N NE2 . GLN B 1 164 ? 0.479   4.507   -10.928 1.00 36.23 ? 164 GLN B NE2 1 
ATOM   3173 N N   . VAL B 1 165 ? 1.053   -1.481  -12.177 1.00 31.22 ? 165 VAL B N   1 
ATOM   3174 C CA  . VAL B 1 165 ? 1.387   -2.829  -12.650 1.00 35.39 ? 165 VAL B CA  1 
ATOM   3175 C C   . VAL B 1 165 ? 0.198   -3.504  -13.336 1.00 34.28 ? 165 VAL B C   1 
ATOM   3176 O O   . VAL B 1 165 ? 0.377   -4.319  -14.243 1.00 33.39 ? 165 VAL B O   1 
ATOM   3177 C CB  . VAL B 1 165 ? 1.919   -3.690  -11.486 1.00 34.39 ? 165 VAL B CB  1 
ATOM   3178 C CG1 . VAL B 1 165 ? 3.313   -3.151  -11.044 1.00 29.19 ? 165 VAL B CG1 1 
ATOM   3179 C CG2 . VAL B 1 165 ? 0.928   -3.727  -10.336 1.00 31.94 ? 165 VAL B CG2 1 
ATOM   3180 N N   . ASN B 1 166 ? -1.016  -3.120  -12.964 1.00 35.39 ? 166 ASN B N   1 
ATOM   3181 C CA  . ASN B 1 166 ? -2.244  -3.609  -13.604 1.00 37.83 ? 166 ASN B CA  1 
ATOM   3182 C C   . ASN B 1 166 ? -2.335  -3.225  -15.074 1.00 35.46 ? 166 ASN B C   1 
ATOM   3183 O O   . ASN B 1 166 ? -2.929  -3.947  -15.884 1.00 34.87 ? 166 ASN B O   1 
ATOM   3184 C CB  . ASN B 1 166 ? -3.413  -2.973  -12.890 1.00 38.38 ? 166 ASN B CB  1 
ATOM   3185 C CG  . ASN B 1 166 ? -3.166  -1.505  -12.611 1.00 39.99 ? 166 ASN B CG  1 
ATOM   3186 O OD1 . ASN B 1 166 ? -2.295  -1.137  -11.825 1.00 37.83 ? 166 ASN B OD1 1 
ATOM   3187 N ND2 . ASN B 1 166 ? -4.033  -0.662  -13.152 1.00 44.10 ? 166 ASN B ND2 1 
ATOM   3188 N N   . GLN B 1 167 ? -1.866  -2.028  -15.410 1.00 36.13 ? 167 GLN B N   1 
ATOM   3189 C CA  . GLN B 1 167 ? -1.920  -1.543  -16.777 1.00 34.50 ? 167 GLN B CA  1 
ATOM   3190 C C   . GLN B 1 167 ? -0.857  -2.184  -17.643 1.00 38.66 ? 167 GLN B C   1 
ATOM   3191 O O   . GLN B 1 167 ? -0.841  -1.912  -18.849 1.00 38.43 ? 167 GLN B O   1 
ATOM   3192 C CB  . GLN B 1 167 ? -1.735  -0.025  -16.810 1.00 37.02 ? 167 GLN B CB  1 
ATOM   3193 C CG  . GLN B 1 167 ? -2.679  0.744   -15.888 1.00 35.98 ? 167 GLN B CG  1 
ATOM   3194 C CD  . GLN B 1 167 ? -2.679  2.236   -16.145 1.00 35.97 ? 167 GLN B CD  1 
ATOM   3195 O OE1 . GLN B 1 167 ? -2.299  2.698   -17.223 1.00 35.84 ? 167 GLN B OE1 1 
ATOM   3196 N NE2 . GLN B 1 167 ? -3.084  3.014   -15.124 1.00 35.25 ? 167 GLN B NE2 1 
ATOM   3197 N N   . SER B 1 168 ? 0.057   -2.979  -17.064 1.00 33.99 ? 168 SER B N   1 
ATOM   3198 C CA  . SER B 1 168 ? 1.022   -3.736  -17.862 1.00 40.76 ? 168 SER B CA  1 
ATOM   3199 C C   . SER B 1 168 ? 0.727   -5.237  -17.859 1.00 40.76 ? 168 SER B C   1 
ATOM   3200 O O   . SER B 1 168 ? 1.574   -6.027  -18.302 1.00 39.63 ? 168 SER B O   1 
ATOM   3201 C CB  . SER B 1 168 ? 2.471   -3.469  -17.400 1.00 35.85 ? 168 SER B CB  1 
ATOM   3202 O OG  . SER B 1 168 ? 2.727   -3.860  -16.053 1.00 36.64 ? 168 SER B OG  1 
ATOM   3203 N N   . ARG B 1 169 ? -0.469  -5.641  -17.407 1.00 40.26 ? 169 ARG B N   1 
ATOM   3204 C CA  . ARG B 1 169 ? -0.793  -7.066  -17.253 1.00 42.33 ? 169 ARG B CA  1 
ATOM   3205 C C   . ARG B 1 169 ? -0.839  -7.817  -18.586 1.00 43.68 ? 169 ARG B C   1 
ATOM   3206 O O   . ARG B 1 169 ? -0.337  -8.943  -18.682 1.00 42.21 ? 169 ARG B O   1 
ATOM   3207 C CB  . ARG B 1 169 ? -2.123  -7.240  -16.523 1.00 39.66 ? 169 ARG B CB  1 
ATOM   3208 C CG  . ARG B 1 169 ? -2.599  -8.706  -16.511 1.00 42.48 ? 169 ARG B CG  1 
ATOM   3209 C CD  . ARG B 1 169 ? -2.775  -9.235  -15.093 1.00 44.89 ? 169 ARG B CD  1 
ATOM   3210 N NE  . ARG B 1 169 ? -3.192  -10.636 -15.045 1.00 44.56 ? 169 ARG B NE  1 
ATOM   3211 C CZ  . ARG B 1 169 ? -3.945  -11.171 -14.086 1.00 45.46 ? 169 ARG B CZ  1 
ATOM   3212 N NH1 . ARG B 1 169 ? -4.425  -10.445 -13.086 1.00 49.07 ? 169 ARG B NH1 1 
ATOM   3213 N NH2 . ARG B 1 169 ? -4.233  -12.467 -14.134 1.00 50.55 ? 169 ARG B NH2 1 
ATOM   3214 N N   . ASN B 1 170 ? -1.450  -7.229  -19.621 1.00 44.33 ? 170 ASN B N   1 
ATOM   3215 C CA  . ASN B 1 170 ? -1.553  -7.925  -20.902 1.00 44.88 ? 170 ASN B CA  1 
ATOM   3216 C C   . ASN B 1 170 ? -0.328  -7.755  -21.795 1.00 45.68 ? 170 ASN B C   1 
ATOM   3217 O O   . ASN B 1 170 ? -0.159  -8.553  -22.725 1.00 42.93 ? 170 ASN B O   1 
ATOM   3218 C CB  . ASN B 1 170 ? -2.820  -7.490  -21.657 1.00 49.45 ? 170 ASN B CB  1 
ATOM   3219 C CG  . ASN B 1 170 ? -4.037  -7.367  -20.747 1.00 49.54 ? 170 ASN B CG  1 
ATOM   3220 O OD1 . ASN B 1 170 ? -4.735  -8.343  -20.498 1.00 51.91 ? 170 ASN B OD1 1 
ATOM   3221 N ND2 . ASN B 1 170 ? -4.280  -6.168  -20.233 1.00 53.16 ? 170 ASN B ND2 1 
ATOM   3222 N N   . CYS B 1 171 ? 0.488   -6.707  -21.588 1.00 45.15 ? 171 CYS B N   1 
ATOM   3223 C CA  . CYS B 1 171 ? 1.661   -6.467  -22.429 1.00 43.32 ? 171 CYS B CA  1 
ATOM   3224 C C   . CYS B 1 171 ? 2.991   -6.905  -21.803 1.00 40.68 ? 171 CYS B C   1 
ATOM   3225 O O   . CYS B 1 171 ? 3.998   -6.960  -22.505 1.00 40.32 ? 171 CYS B O   1 
ATOM   3226 C CB  . CYS B 1 171 ? 1.729   -4.978  -22.815 1.00 40.02 ? 171 CYS B CB  1 
ATOM   3227 S SG  . CYS B 1 171 ? 1.825   -3.807  -21.431 1.00 47.91 ? 171 CYS B SG  1 
ATOM   3228 N N   . LYS B 1 172 ? 3.021   -7.265  -20.531 1.00 40.31 ? 172 LYS B N   1 
ATOM   3229 C CA  . LYS B 1 172 ? 4.249   -7.823  -19.971 1.00 42.11 ? 172 LYS B CA  1 
ATOM   3230 C C   . LYS B 1 172 ? 3.851   -9.007  -19.100 1.00 40.39 ? 172 LYS B C   1 
ATOM   3231 O O   . LYS B 1 172 ? 4.319   -10.128 -19.313 1.00 41.64 ? 172 LYS B O   1 
ATOM   3232 C CB  . LYS B 1 172 ? 5.045   -6.780  -19.174 1.00 39.57 ? 172 LYS B CB  1 
ATOM   3233 C CG  . LYS B 1 172 ? 6.085   -7.384  -18.228 1.00 39.21 ? 172 LYS B CG  1 
ATOM   3234 C CD  . LYS B 1 172 ? 7.458   -7.479  -18.866 1.00 41.25 ? 172 LYS B CD  1 
ATOM   3235 C CE  . LYS B 1 172 ? 8.318   -8.486  -18.079 1.00 36.74 ? 172 LYS B CE  1 
ATOM   3236 N NZ  . LYS B 1 172 ? 8.839   -9.621  -18.902 1.00 35.57 ? 172 LYS B NZ  1 
ATOM   3237 N N   . GLY B 1 173 ? 2.965   -8.767  -18.142 1.00 38.34 ? 173 GLY B N   1 
ATOM   3238 C CA  . GLY B 1 173 ? 2.429   -9.815  -17.308 1.00 40.57 ? 173 GLY B CA  1 
ATOM   3239 C C   . GLY B 1 173 ? 3.246   -10.234 -16.114 1.00 41.57 ? 173 GLY B C   1 
ATOM   3240 O O   . GLY B 1 173 ? 3.036   -11.345 -15.624 1.00 43.16 ? 173 GLY B O   1 
ATOM   3241 N N   . ASP B 1 174 ? 4.123   -9.363  -15.579 1.00 38.18 ? 174 ASP B N   1 
ATOM   3242 C CA  . ASP B 1 174 ? 4.874   -9.760  -14.395 1.00 36.47 ? 174 ASP B CA  1 
ATOM   3243 C C   . ASP B 1 174 ? 3.975   -9.780  -13.169 1.00 33.96 ? 174 ASP B C   1 
ATOM   3244 O O   . ASP B 1 174 ? 4.250   -10.505 -12.210 1.00 33.87 ? 174 ASP B O   1 
ATOM   3245 C CB  . ASP B 1 174 ? 6.066   -8.825  -14.160 1.00 35.44 ? 174 ASP B CB  1 
ATOM   3246 C CG  . ASP B 1 174 ? 7.358   -9.300  -14.848 1.00 37.04 ? 174 ASP B CG  1 
ATOM   3247 O OD1 . ASP B 1 174 ? 7.360   -10.305 -15.604 1.00 36.21 ? 174 ASP B OD1 1 
ATOM   3248 O OD2 . ASP B 1 174 ? 8.387   -8.636  -14.626 1.00 33.30 ? 174 ASP B OD2 1 
ATOM   3249 N N   . TYR B 1 175 ? 2.914   -8.972  -13.151 1.00 34.38 ? 175 TYR B N   1 
ATOM   3250 C CA  . TYR B 1 175 ? 2.173   -8.780  -11.921 1.00 35.58 ? 175 TYR B CA  1 
ATOM   3251 C C   . TYR B 1 175 ? 0.678   -9.048  -12.091 1.00 37.70 ? 175 TYR B C   1 
ATOM   3252 O O   . TYR B 1 175 ? 0.084   -8.751  -13.128 1.00 37.81 ? 175 TYR B O   1 
ATOM   3253 C CB  . TYR B 1 175 ? 2.351   -7.335  -11.419 1.00 36.50 ? 175 TYR B CB  1 
ATOM   3254 C CG  . TYR B 1 175 ? 3.716   -6.954  -10.909 1.00 34.64 ? 175 TYR B CG  1 
ATOM   3255 C CD1 . TYR B 1 175 ? 4.084   -7.176  -9.579  1.00 34.89 ? 175 TYR B CD1 1 
ATOM   3256 C CD2 . TYR B 1 175 ? 4.631   -6.366  -11.753 1.00 33.99 ? 175 TYR B CD2 1 
ATOM   3257 C CE1 . TYR B 1 175 ? 5.339   -6.797  -9.109  1.00 35.85 ? 175 TYR B CE1 1 
ATOM   3258 C CE2 . TYR B 1 175 ? 5.908   -5.980  -11.285 1.00 36.71 ? 175 TYR B CE2 1 
ATOM   3259 C CZ  . TYR B 1 175 ? 6.258   -6.204  -9.973  1.00 33.57 ? 175 TYR B CZ  1 
ATOM   3260 O OH  . TYR B 1 175 ? 7.514   -5.820  -9.551  1.00 32.78 ? 175 TYR B OH  1 
ATOM   3261 N N   . THR B 1 176 ? 0.129   -9.660  -11.067 1.00 39.28 ? 176 THR B N   1 
ATOM   3262 C CA  . THR B 1 176 ? -1.334  -9.674  -10.850 1.00 38.09 ? 176 THR B CA  1 
ATOM   3263 C C   . THR B 1 176 ? -1.578  -8.579  -9.795  1.00 38.98 ? 176 THR B C   1 
ATOM   3264 O O   . THR B 1 176 ? -0.615  -8.049  -9.209  1.00 44.17 ? 176 THR B O   1 
ATOM   3265 C CB  . THR B 1 176 ? -1.837  -11.046 -10.398 1.00 41.79 ? 176 THR B CB  1 
ATOM   3266 O OG1 . THR B 1 176 ? -1.318  -11.308 -9.104  1.00 39.23 ? 176 THR B OG1 1 
ATOM   3267 C CG2 . THR B 1 176 ? -1.466  -12.165 -11.335 1.00 40.98 ? 176 THR B CG2 1 
ATOM   3268 N N   . GLY B 1 177 ? -2.803  -8.144  -9.575  1.00 44.02 ? 177 GLY B N   1 
ATOM   3269 C CA  . GLY B 1 177 ? -2.934  -7.090  -8.550  1.00 45.54 ? 177 GLY B CA  1 
ATOM   3270 C C   . GLY B 1 177 ? -2.753  -5.676  -9.086  1.00 41.55 ? 177 GLY B C   1 
ATOM   3271 O O   . GLY B 1 177 ? -2.185  -5.468  -10.148 1.00 37.86 ? 177 GLY B O   1 
ATOM   3272 N N   . ASN B 1 178 ? -3.195  -4.722  -8.286  1.00 45.61 ? 178 ASN B N   1 
ATOM   3273 C CA  . ASN B 1 178 ? -3.278  -3.320  -8.728  1.00 43.16 ? 178 ASN B CA  1 
ATOM   3274 C C   . ASN B 1 178 ? -2.572  -2.415  -7.738  1.00 42.78 ? 178 ASN B C   1 
ATOM   3275 O O   . ASN B 1 178 ? -3.078  -2.287  -6.655  1.00 44.26 ? 178 ASN B O   1 
ATOM   3276 C CB  . ASN B 1 178 ? -4.744  -2.890  -8.678  1.00 48.94 ? 178 ASN B CB  1 
ATOM   3277 C CG  . ASN B 1 178 ? -5.259  -2.346  -9.985  1.00 53.86 ? 178 ASN B CG  1 
ATOM   3278 O OD1 . ASN B 1 178 ? -4.991  -1.197  -10.331 1.00 62.75 ? 178 ASN B OD1 1 
ATOM   3279 N ND2 . ASN B 1 178 ? -5.982  -3.174  -10.718 1.00 58.45 ? 178 ASN B ND2 1 
ATOM   3280 N N   . PHE B 1 179 ? -1.463  -1.812  -8.148  1.00 40.09 ? 179 PHE B N   1 
ATOM   3281 C CA  . PHE B 1 179 ? -0.724  -0.831  -7.315  1.00 36.31 ? 179 PHE B CA  1 
ATOM   3282 C C   . PHE B 1 179 ? 0.291   -0.115  -8.205  1.00 28.73 ? 179 PHE B C   1 
ATOM   3283 O O   . PHE B 1 179 ? 0.599   -0.605  -9.265  1.00 33.76 ? 179 PHE B O   1 
ATOM   3284 C CB  . PHE B 1 179 ? -0.028  -1.494  -6.125  1.00 34.35 ? 179 PHE B CB  1 
ATOM   3285 C CG  . PHE B 1 179 ? 0.814   -2.699  -6.464  1.00 37.05 ? 179 PHE B CG  1 
ATOM   3286 C CD1 . PHE B 1 179 ? 0.270   -3.974  -6.453  1.00 35.15 ? 179 PHE B CD1 1 
ATOM   3287 C CD2 . PHE B 1 179 ? 2.156   -2.558  -6.776  1.00 34.16 ? 179 PHE B CD2 1 
ATOM   3288 C CE1 . PHE B 1 179 ? 1.042   -5.082  -6.757  1.00 37.29 ? 179 PHE B CE1 1 
ATOM   3289 C CE2 . PHE B 1 179 ? 2.930   -3.668  -7.063  1.00 32.80 ? 179 PHE B CE2 1 
ATOM   3290 C CZ  . PHE B 1 179 ? 2.376   -4.929  -7.057  1.00 34.61 ? 179 PHE B CZ  1 
ATOM   3291 N N   . GLY B 1 180 ? 0.737   1.053   -7.772  1.00 27.63 ? 180 GLY B N   1 
ATOM   3292 C CA  . GLY B 1 180 ? 1.796   1.784   -8.481  1.00 30.74 ? 180 GLY B CA  1 
ATOM   3293 C C   . GLY B 1 180 ? 3.138   1.155   -8.148  1.00 30.05 ? 180 GLY B C   1 
ATOM   3294 O O   . GLY B 1 180 ? 3.259   0.543   -7.095  1.00 30.90 ? 180 GLY B O   1 
ATOM   3295 N N   . HIS B 1 181 ? 4.125   1.359   -8.999  1.00 30.96 ? 181 HIS B N   1 
ATOM   3296 C CA  . HIS B 1 181 ? 5.438   0.690   -8.814  1.00 28.45 ? 181 HIS B CA  1 
ATOM   3297 C C   . HIS B 1 181 ? 6.549   1.475   -9.508  1.00 31.05 ? 181 HIS B C   1 
ATOM   3298 O O   . HIS B 1 181 ? 6.328   2.142   -10.525 1.00 29.05 ? 181 HIS B O   1 
ATOM   3299 C CB  . HIS B 1 181 ? 5.422   -0.768  -9.319  1.00 26.74 ? 181 HIS B CB  1 
ATOM   3300 C CG  . HIS B 1 181 ? 6.592   -1.615  -8.846  1.00 30.49 ? 181 HIS B CG  1 
ATOM   3301 N ND1 . HIS B 1 181 ? 6.912   -1.769  -7.510  1.00 27.80 ? 181 HIS B ND1 1 
ATOM   3302 C CD2 . HIS B 1 181 ? 7.472   -2.388  -9.531  1.00 27.96 ? 181 HIS B CD2 1 
ATOM   3303 C CE1 . HIS B 1 181 ? 7.933   -2.600  -7.395  1.00 30.24 ? 181 HIS B CE1 1 
ATOM   3304 N NE2 . HIS B 1 181 ? 8.282   -2.999  -8.605  1.00 29.28 ? 181 HIS B NE2 1 
ATOM   3305 N N   . TYR B 1 182 ? 7.764   1.343   -8.975  1.00 28.75 ? 182 TYR B N   1 
ATOM   3306 C CA  . TYR B 1 182 ? 8.961   1.972   -9.507  1.00 26.70 ? 182 TYR B CA  1 
ATOM   3307 C C   . TYR B 1 182 ? 10.023  0.923   -9.857  1.00 26.72 ? 182 TYR B C   1 
ATOM   3308 O O   . TYR B 1 182 ? 10.136  -0.110  -9.186  1.00 24.66 ? 182 TYR B O   1 
ATOM   3309 C CB  . TYR B 1 182 ? 9.577   2.913   -8.481  1.00 27.04 ? 182 TYR B CB  1 
ATOM   3310 C CG  . TYR B 1 182 ? 8.833   4.196   -8.174  1.00 29.17 ? 182 TYR B CG  1 
ATOM   3311 C CD1 . TYR B 1 182 ? 7.898   4.248   -7.138  1.00 27.27 ? 182 TYR B CD1 1 
ATOM   3312 C CD2 . TYR B 1 182 ? 9.111   5.359   -8.870  1.00 29.07 ? 182 TYR B CD2 1 
ATOM   3313 C CE1 . TYR B 1 182 ? 7.262   5.390   -6.828  1.00 29.86 ? 182 TYR B CE1 1 
ATOM   3314 C CE2 . TYR B 1 182 ? 8.451   6.533   -8.555  1.00 29.05 ? 182 TYR B CE2 1 
ATOM   3315 C CZ  . TYR B 1 182 ? 7.542   6.537   -7.535  1.00 28.11 ? 182 TYR B CZ  1 
ATOM   3316 O OH  . TYR B 1 182 ? 6.882   7.683   -7.220  1.00 29.61 ? 182 TYR B OH  1 
ATOM   3317 N N   . GLY B 1 183 ? 10.818  1.216   -10.888 1.00 27.37 ? 183 GLY B N   1 
ATOM   3318 C CA  . GLY B 1 183 ? 12.030  0.453   -11.230 1.00 24.81 ? 183 GLY B CA  1 
ATOM   3319 C C   . GLY B 1 183 ? 13.041  1.377   -11.901 1.00 27.11 ? 183 GLY B C   1 
ATOM   3320 O O   . GLY B 1 183 ? 12.797  2.577   -12.004 1.00 27.76 ? 183 GLY B O   1 
ATOM   3321 N N   . LEU B 1 184 ? 14.160  0.842   -12.390 1.00 27.52 ? 184 LEU B N   1 
ATOM   3322 C CA  . LEU B 1 184 ? 15.205  1.626   -13.049 1.00 24.33 ? 184 LEU B CA  1 
ATOM   3323 C C   . LEU B 1 184 ? 15.425  1.097   -14.459 1.00 25.57 ? 184 LEU B C   1 
ATOM   3324 O O   . LEU B 1 184 ? 15.756  -0.081  -14.648 1.00 26.92 ? 184 LEU B O   1 
ATOM   3325 C CB  . LEU B 1 184 ? 16.507  1.583   -12.261 1.00 24.17 ? 184 LEU B CB  1 
ATOM   3326 C CG  . LEU B 1 184 ? 17.679  2.402   -12.841 1.00 26.06 ? 184 LEU B CG  1 
ATOM   3327 C CD1 . LEU B 1 184 ? 17.441  3.881   -12.670 1.00 22.77 ? 184 LEU B CD1 1 
ATOM   3328 C CD2 . LEU B 1 184 ? 19.040  1.980   -12.228 1.00 24.66 ? 184 LEU B CD2 1 
ATOM   3329 N N   . ILE B 1 185 ? 15.209  1.953   -15.452 1.00 26.90 ? 185 ILE B N   1 
ATOM   3330 C CA  . ILE B 1 185 ? 15.655  1.652   -16.809 1.00 29.98 ? 185 ILE B CA  1 
ATOM   3331 C C   . ILE B 1 185 ? 17.155  1.931   -16.899 1.00 29.97 ? 185 ILE B C   1 
ATOM   3332 O O   . ILE B 1 185 ? 17.591  3.073   -16.710 1.00 27.35 ? 185 ILE B O   1 
ATOM   3333 C CB  . ILE B 1 185 ? 14.898  2.478   -17.854 1.00 29.29 ? 185 ILE B CB  1 
ATOM   3334 C CG1 . ILE B 1 185 ? 13.383  2.417   -17.625 1.00 29.87 ? 185 ILE B CG1 1 
ATOM   3335 C CG2 . ILE B 1 185 ? 15.278  2.029   -19.246 1.00 29.03 ? 185 ILE B CG2 1 
ATOM   3336 C CD1 . ILE B 1 185 ? 12.668  3.402   -18.449 1.00 30.14 ? 185 ILE B CD1 1 
ATOM   3337 N N   . TRP B 1 186 ? 17.944  0.896   -17.189 1.00 27.51 ? 186 TRP B N   1 
ATOM   3338 C CA  . TRP B 1 186 ? 19.385  1.049   -17.300 1.00 28.92 ? 186 TRP B CA  1 
ATOM   3339 C C   . TRP B 1 186 ? 19.908  0.647   -18.667 1.00 29.27 ? 186 TRP B C   1 
ATOM   3340 O O   . TRP B 1 186 ? 21.104  0.811   -18.933 1.00 32.77 ? 186 TRP B O   1 
ATOM   3341 C CB  . TRP B 1 186 ? 20.091  0.245   -16.185 1.00 26.61 ? 186 TRP B CB  1 
ATOM   3342 C CG  . TRP B 1 186 ? 19.707  -1.219  -16.162 1.00 30.32 ? 186 TRP B CG  1 
ATOM   3343 C CD1 . TRP B 1 186 ? 18.591  -1.781  -15.573 1.00 28.44 ? 186 TRP B CD1 1 
ATOM   3344 C CD2 . TRP B 1 186 ? 20.439  -2.292  -16.742 1.00 27.88 ? 186 TRP B CD2 1 
ATOM   3345 N NE1 . TRP B 1 186 ? 18.603  -3.149  -15.767 1.00 31.92 ? 186 TRP B NE1 1 
ATOM   3346 C CE2 . TRP B 1 186 ? 19.728  -3.486  -16.473 1.00 27.20 ? 186 TRP B CE2 1 
ATOM   3347 C CE3 . TRP B 1 186 ? 21.648  -2.368  -17.442 1.00 29.93 ? 186 TRP B CE3 1 
ATOM   3348 C CZ2 . TRP B 1 186 ? 20.179  -4.747  -16.904 1.00 28.26 ? 186 TRP B CZ2 1 
ATOM   3349 C CZ3 . TRP B 1 186 ? 22.113  -3.629  -17.857 1.00 31.23 ? 186 TRP B CZ3 1 
ATOM   3350 C CH2 . TRP B 1 186 ? 21.373  -4.798  -17.592 1.00 31.26 ? 186 TRP B CH2 1 
ATOM   3351 N N   . ASP B 1 187 ? 19.051  0.139   -19.547 1.00 35.22 ? 187 ASP B N   1 
ATOM   3352 C CA  . ASP B 1 187 ? 19.446  -0.229  -20.905 1.00 36.35 ? 187 ASP B CA  1 
ATOM   3353 C C   . ASP B 1 187 ? 18.194  -0.367  -21.762 1.00 34.24 ? 187 ASP B C   1 
ATOM   3354 O O   . ASP B 1 187 ? 17.076  -0.448  -21.251 1.00 35.20 ? 187 ASP B O   1 
ATOM   3355 C CB  . ASP B 1 187 ? 20.260  -1.526  -20.909 1.00 33.81 ? 187 ASP B CB  1 
ATOM   3356 C CG  . ASP B 1 187 ? 21.084  -1.679  -22.159 1.00 35.93 ? 187 ASP B CG  1 
ATOM   3357 O OD1 . ASP B 1 187 ? 21.187  -0.718  -22.939 1.00 39.99 ? 187 ASP B OD1 1 
ATOM   3358 O OD2 . ASP B 1 187 ? 21.661  -2.746  -22.345 1.00 39.11 ? 187 ASP B OD2 1 
ATOM   3359 N N   . MET B 1 188 ? 18.388  -0.425  -23.076 1.00 37.28 ? 188 MET B N   1 
ATOM   3360 C CA  . MET B 1 188 ? 17.260  -0.694  -23.964 1.00 40.41 ? 188 MET B CA  1 
ATOM   3361 C C   . MET B 1 188 ? 17.707  -1.520  -25.168 1.00 40.83 ? 188 MET B C   1 
ATOM   3362 O O   . MET B 1 188 ? 18.843  -1.416  -25.631 1.00 39.35 ? 188 MET B O   1 
ATOM   3363 C CB  . MET B 1 188 ? 16.565  0.612   -24.407 1.00 41.64 ? 188 MET B CB  1 
ATOM   3364 C CG  . MET B 1 188 ? 17.485  1.787   -24.627 1.00 43.40 ? 188 MET B CG  1 
ATOM   3365 S SD  . MET B 1 188 ? 16.505  3.310   -24.615 1.00 47.12 ? 188 MET B SD  1 
ATOM   3366 C CE  . MET B 1 188 ? 15.453  3.079   -26.038 1.00 44.27 ? 188 MET B CE  1 
ATOM   3367 N N   . THR B 1 189 ? 16.806  -2.358  -25.652 1.00 39.23 ? 189 THR B N   1 
ATOM   3368 C CA  . THR B 1 189 ? 16.989  -3.006  -26.941 1.00 43.03 ? 189 THR B CA  1 
ATOM   3369 C C   . THR B 1 189 ? 16.438  -2.089  -28.033 1.00 48.46 ? 189 THR B C   1 
ATOM   3370 O O   . THR B 1 189 ? 16.150  -0.907  -27.802 1.00 46.38 ? 189 THR B O   1 
ATOM   3371 C CB  . THR B 1 189 ? 16.300  -4.380  -26.972 1.00 44.45 ? 189 THR B CB  1 
ATOM   3372 O OG1 . THR B 1 189 ? 14.891  -4.237  -27.259 1.00 47.53 ? 189 THR B OG1 1 
ATOM   3373 C CG2 . THR B 1 189 ? 16.453  -5.106  -25.628 1.00 46.26 ? 189 THR B CG2 1 
ATOM   3374 N N   . SER B 1 190 ? 16.303  -2.624  -29.256 1.00 50.17 ? 190 SER B N   1 
ATOM   3375 C CA  . SER B 1 190 ? 15.681  -1.853  -30.329 1.00 46.51 ? 190 SER B CA  1 
ATOM   3376 C C   . SER B 1 190 ? 14.214  -1.620  -30.052 1.00 45.06 ? 190 SER B C   1 
ATOM   3377 O O   . SER B 1 190 ? 13.638  -0.662  -30.575 1.00 48.18 ? 190 SER B O   1 
ATOM   3378 C CB  . SER B 1 190 ? 15.819  -2.595  -31.655 1.00 47.56 ? 190 SER B CB  1 
ATOM   3379 O OG  . SER B 1 190 ? 15.357  -3.935  -31.513 1.00 53.43 ? 190 SER B OG  1 
ATOM   3380 N N   . THR B 1 191 ? 13.614  -2.461  -29.213 1.00 42.40 ? 191 THR B N   1 
ATOM   3381 C CA  . THR B 1 191 ? 12.176  -2.464  -28.996 1.00 43.19 ? 191 THR B CA  1 
ATOM   3382 C C   . THR B 1 191 ? 11.747  -2.402  -27.544 1.00 40.85 ? 191 THR B C   1 
ATOM   3383 O O   . THR B 1 191 ? 10.644  -1.930  -27.290 1.00 41.26 ? 191 THR B O   1 
ATOM   3384 C CB  . THR B 1 191 ? 11.548  -3.730  -29.613 1.00 43.52 ? 191 THR B CB  1 
ATOM   3385 O OG1 . THR B 1 191 ? 12.151  -4.900  -29.029 1.00 44.09 ? 191 THR B OG1 1 
ATOM   3386 C CG2 . THR B 1 191 ? 11.746  -3.755  -31.139 1.00 44.05 ? 191 THR B CG2 1 
ATOM   3387 N N   . HIS B 1 192 ? 12.573  -2.818  -26.585 1.00 42.53 ? 192 HIS B N   1 
ATOM   3388 C CA  . HIS B 1 192 ? 12.142  -2.944  -25.199 1.00 40.06 ? 192 HIS B CA  1 
ATOM   3389 C C   . HIS B 1 192 ? 13.052  -2.121  -24.288 1.00 41.90 ? 192 HIS B C   1 
ATOM   3390 O O   . HIS B 1 192 ? 14.271  -2.032  -24.501 1.00 39.69 ? 192 HIS B O   1 
ATOM   3391 C CB  . HIS B 1 192 ? 12.223  -4.367  -24.645 1.00 42.67 ? 192 HIS B CB  1 
ATOM   3392 C CG  . HIS B 1 192 ? 11.307  -5.376  -25.255 1.00 42.66 ? 192 HIS B CG  1 
ATOM   3393 N ND1 . HIS B 1 192 ? 11.309  -5.681  -26.600 1.00 42.36 ? 192 HIS B ND1 1 
ATOM   3394 C CD2 . HIS B 1 192 ? 10.489  -6.281  -24.665 1.00 44.16 ? 192 HIS B CD2 1 
ATOM   3395 C CE1 . HIS B 1 192 ? 10.482  -6.690  -26.816 1.00 44.14 ? 192 HIS B CE1 1 
ATOM   3396 N NE2 . HIS B 1 192 ? 9.966   -7.065  -25.660 1.00 44.32 ? 192 HIS B NE2 1 
ATOM   3397 N N   . TYR B 1 193 ? 12.460  -1.573  -23.233 1.00 38.24 ? 193 TYR B N   1 
ATOM   3398 C CA  . TYR B 1 193 ? 13.228  -1.068  -22.105 1.00 36.56 ? 193 TYR B CA  1 
ATOM   3399 C C   . TYR B 1 193 ? 13.730  -2.234  -21.232 1.00 38.24 ? 193 TYR B C   1 
ATOM   3400 O O   . TYR B 1 193 ? 12.950  -3.121  -20.851 1.00 37.50 ? 193 TYR B O   1 
ATOM   3401 C CB  . TYR B 1 193 ? 12.330  -0.190  -21.252 1.00 31.50 ? 193 TYR B CB  1 
ATOM   3402 C CG  . TYR B 1 193 ? 11.807  1.064   -21.884 1.00 34.31 ? 193 TYR B CG  1 
ATOM   3403 C CD1 . TYR B 1 193 ? 12.665  2.033   -22.409 1.00 37.12 ? 193 TYR B CD1 1 
ATOM   3404 C CD2 . TYR B 1 193 ? 10.429  1.311   -21.905 1.00 36.87 ? 193 TYR B CD2 1 
ATOM   3405 C CE1 . TYR B 1 193 ? 12.142  3.248   -22.946 1.00 37.81 ? 193 TYR B CE1 1 
ATOM   3406 C CE2 . TYR B 1 193 ? 9.906   2.485   -22.435 1.00 38.21 ? 193 TYR B CE2 1 
ATOM   3407 C CZ  . TYR B 1 193 ? 10.770  3.451   -22.950 1.00 38.70 ? 193 TYR B CZ  1 
ATOM   3408 O OH  . TYR B 1 193 ? 10.206  4.593   -23.480 1.00 40.91 ? 193 TYR B OH  1 
ATOM   3409 N N   . VAL B 1 194 ? 14.991  -2.183  -20.806 1.00 31.83 ? 194 VAL B N   1 
ATOM   3410 C CA  . VAL B 1 194 ? 15.493  -3.162  -19.833 1.00 33.05 ? 194 VAL B CA  1 
ATOM   3411 C C   . VAL B 1 194 ? 15.343  -2.558  -18.439 1.00 30.21 ? 194 VAL B C   1 
ATOM   3412 O O   . VAL B 1 194 ? 16.007  -1.579  -18.100 1.00 30.79 ? 194 VAL B O   1 
ATOM   3413 C CB  . VAL B 1 194 ? 16.949  -3.570  -20.104 1.00 31.39 ? 194 VAL B CB  1 
ATOM   3414 C CG1 . VAL B 1 194 ? 17.351  -4.693  -19.161 1.00 31.19 ? 194 VAL B CG1 1 
ATOM   3415 C CG2 . VAL B 1 194 ? 17.133  -4.042  -21.532 1.00 32.97 ? 194 VAL B CG2 1 
ATOM   3416 N N   . VAL B 1 195 ? 14.487  -3.147  -17.609 1.00 30.89 ? 195 VAL B N   1 
ATOM   3417 C CA  . VAL B 1 195 ? 14.152  -2.563  -16.314 1.00 33.42 ? 195 VAL B CA  1 
ATOM   3418 C C   . VAL B 1 195 ? 14.714  -3.428  -15.191 1.00 32.91 ? 195 VAL B C   1 
ATOM   3419 O O   . VAL B 1 195 ? 14.472  -4.647  -15.135 1.00 29.76 ? 195 VAL B O   1 
ATOM   3420 C CB  . VAL B 1 195 ? 12.629  -2.377  -16.161 1.00 33.29 ? 195 VAL B CB  1 
ATOM   3421 C CG1 . VAL B 1 195 ? 12.290  -1.806  -14.755 1.00 31.08 ? 195 VAL B CG1 1 
ATOM   3422 C CG2 . VAL B 1 195 ? 12.094  -1.445  -17.275 1.00 31.61 ? 195 VAL B CG2 1 
ATOM   3423 N N   . ALA B 1 196 ? 15.433  -2.787  -14.277 1.00 30.03 ? 196 ALA B N   1 
ATOM   3424 C CA  . ALA B 1 196 ? 15.747  -3.387  -12.982 1.00 29.94 ? 196 ALA B CA  1 
ATOM   3425 C C   . ALA B 1 196 ? 14.576  -3.129  -12.035 1.00 29.12 ? 196 ALA B C   1 
ATOM   3426 O O   . ALA B 1 196 ? 14.406  -2.017  -11.520 1.00 28.13 ? 196 ALA B O   1 
ATOM   3427 C CB  . ALA B 1 196 ? 17.048  -2.822  -12.428 1.00 29.12 ? 196 ALA B CB  1 
ATOM   3428 N N   . ASP B 1 197 ? 13.784  -4.175  -11.780 1.00 27.53 ? 197 ASP B N   1 
ATOM   3429 C CA  . ASP B 1 197 ? 12.603  -4.101  -10.943 1.00 27.52 ? 197 ASP B CA  1 
ATOM   3430 C C   . ASP B 1 197 ? 12.929  -4.603  -9.534  1.00 27.02 ? 197 ASP B C   1 
ATOM   3431 O O   . ASP B 1 197 ? 13.106  -5.810  -9.348  1.00 26.13 ? 197 ASP B O   1 
ATOM   3432 C CB  . ASP B 1 197 ? 11.485  -4.938  -11.568 1.00 31.49 ? 197 ASP B CB  1 
ATOM   3433 C CG  . ASP B 1 197 ? 10.170  -4.874  -10.780 1.00 28.35 ? 197 ASP B CG  1 
ATOM   3434 O OD1 . ASP B 1 197 ? 10.169  -4.579  -9.561  1.00 27.02 ? 197 ASP B OD1 1 
ATOM   3435 O OD2 . ASP B 1 197 ? 9.118   -5.191  -11.375 1.00 34.08 ? 197 ASP B OD2 1 
ATOM   3436 N N   . PRO B 1 198 ? 12.933  -3.739  -8.512  1.00 25.24 ? 198 PRO B N   1 
ATOM   3437 C CA  . PRO B 1 198 ? 13.329  -4.166  -7.149  1.00 25.82 ? 198 PRO B CA  1 
ATOM   3438 C C   . PRO B 1 198 ? 12.415  -5.263  -6.524  1.00 27.23 ? 198 PRO B C   1 
ATOM   3439 O O   . PRO B 1 198 ? 12.654  -5.723  -5.395  1.00 22.52 ? 198 PRO B O   1 
ATOM   3440 C CB  . PRO B 1 198 ? 13.194  -2.872  -6.337  1.00 24.54 ? 198 PRO B CB  1 
ATOM   3441 C CG  . PRO B 1 198 ? 13.108  -1.766  -7.346  1.00 29.54 ? 198 PRO B CG  1 
ATOM   3442 C CD  . PRO B 1 198 ? 12.461  -2.351  -8.549  1.00 25.96 ? 198 PRO B CD  1 
ATOM   3443 N N   . ALA B 1 199 ? 11.315  -5.616  -7.166  1.00 29.85 ? 199 ALA B N   1 
ATOM   3444 C CA  . ALA B 1 199 ? 10.455  -6.694  -6.677  1.00 31.72 ? 199 ALA B CA  1 
ATOM   3445 C C   . ALA B 1 199 ? 10.515  -7.952  -7.532  1.00 29.71 ? 199 ALA B C   1 
ATOM   3446 O O   . ALA B 1 199 ? 9.840   -8.934  -7.194  1.00 31.12 ? 199 ALA B O   1 
ATOM   3447 C CB  . ALA B 1 199 ? 8.981   -6.214  -6.594  1.00 28.45 ? 199 ALA B CB  1 
ATOM   3448 N N   . LYS B 1 200 ? 11.259  -7.951  -8.636  1.00 26.92 ? 200 LYS B N   1 
ATOM   3449 C CA  . LYS B 1 200 ? 11.207  -9.075  -9.579  1.00 31.63 ? 200 LYS B CA  1 
ATOM   3450 C C   . LYS B 1 200 ? 12.590  -9.535  -10.066 1.00 30.89 ? 200 LYS B C   1 
ATOM   3451 O O   . LYS B 1 200 ? 12.906  -10.721 -9.977  1.00 28.59 ? 200 LYS B O   1 
ATOM   3452 C CB  . LYS B 1 200 ? 10.344  -8.709  -10.795 1.00 28.34 ? 200 LYS B CB  1 
ATOM   3453 C CG  . LYS B 1 200 ? 8.830   -8.550  -10.471 1.00 36.72 ? 200 LYS B CG  1 
ATOM   3454 C CD  . LYS B 1 200 ? 8.142   -9.839  -10.168 1.00 35.12 ? 200 LYS B CD  1 
ATOM   3455 C CE  . LYS B 1 200 ? 8.562   -10.949 -11.139 1.00 35.24 ? 200 LYS B CE  1 
ATOM   3456 N NZ  . LYS B 1 200 ? 7.923   -12.218 -10.767 1.00 36.03 ? 200 LYS B NZ  1 
ATOM   3457 N N   . GLY B 1 201 ? 13.419  -8.620  -10.575 1.00 32.93 ? 201 GLY B N   1 
ATOM   3458 C CA  . GLY B 1 201 ? 14.708  -9.019  -11.122 1.00 29.25 ? 201 GLY B CA  1 
ATOM   3459 C C   . GLY B 1 201 ? 15.325  -7.892  -11.910 1.00 30.45 ? 201 GLY B C   1 
ATOM   3460 O O   . GLY B 1 201 ? 14.715  -6.833  -12.112 1.00 26.07 ? 201 GLY B O   1 
ATOM   3461 N N   . VAL B 1 202 ? 16.564  -8.144  -12.379 1.00 32.81 ? 202 VAL B N   1 
ATOM   3462 C CA  . VAL B 1 202 ? 17.402  -7.062  -12.924 1.00 28.22 ? 202 VAL B CA  1 
ATOM   3463 C C   . VAL B 1 202 ? 17.180  -6.749  -14.413 1.00 29.93 ? 202 VAL B C   1 
ATOM   3464 O O   . VAL B 1 202 ? 17.563  -5.673  -14.867 1.00 28.94 ? 202 VAL B O   1 
ATOM   3465 C CB  . VAL B 1 202 ? 18.893  -7.374  -12.678 1.00 28.85 ? 202 VAL B CB  1 
ATOM   3466 C CG1 . VAL B 1 202 ? 19.370  -8.444  -13.619 1.00 29.19 ? 202 VAL B CG1 1 
ATOM   3467 C CG2 . VAL B 1 202 ? 19.796  -6.023  -12.775 1.00 23.27 ? 202 VAL B CG2 1 
ATOM   3468 N N   . ASN B 1 203 ? 16.588  -7.651  -15.195 1.00 31.21 ? 203 ASN B N   1 
ATOM   3469 C CA  . ASN B 1 203 ? 16.447  -7.429  -16.639 1.00 32.59 ? 203 ASN B CA  1 
ATOM   3470 C C   . ASN B 1 203 ? 15.007  -7.738  -17.065 1.00 33.98 ? 203 ASN B C   1 
ATOM   3471 O O   . ASN B 1 203 ? 14.743  -8.621  -17.877 1.00 37.87 ? 203 ASN B O   1 
ATOM   3472 C CB  . ASN B 1 203 ? 17.485  -8.236  -17.451 1.00 36.45 ? 203 ASN B CB  1 
ATOM   3473 C CG  . ASN B 1 203 ? 17.135  -9.701  -17.581 1.00 43.82 ? 203 ASN B CG  1 
ATOM   3474 O OD1 . ASN B 1 203 ? 16.475  -10.274 -16.689 1.00 44.42 ? 203 ASN B OD1 1 
ATOM   3475 N ND2 . ASN B 1 203 ? 17.570  -10.333 -18.691 1.00 42.03 ? 203 ASN B ND2 1 
ATOM   3476 N N   . ARG B 1 204 ? 14.071  -6.971  -16.521 1.00 33.21 ? 204 ARG B N   1 
ATOM   3477 C CA  . ARG B 1 204 ? 12.656  -7.092  -16.941 1.00 34.49 ? 204 ARG B CA  1 
ATOM   3478 C C   . ARG B 1 204 ? 12.520  -6.306  -18.248 1.00 34.76 ? 204 ARG B C   1 
ATOM   3479 O O   . ARG B 1 204 ? 12.692  -5.110  -18.228 1.00 32.80 ? 204 ARG B O   1 
ATOM   3480 C CB  . ARG B 1 204 ? 11.713  -6.582  -15.857 1.00 31.90 ? 204 ARG B CB  1 
ATOM   3481 C CG  . ARG B 1 204 ? 11.833  -7.335  -14.548 1.00 31.50 ? 204 ARG B CG  1 
ATOM   3482 C CD  . ARG B 1 204 ? 12.172  -8.790  -14.768 1.00 31.65 ? 204 ARG B CD  1 
ATOM   3483 N NE  . ARG B 1 204 ? 11.010  -9.628  -14.955 1.00 30.40 ? 204 ARG B NE  1 
ATOM   3484 C CZ  . ARG B 1 204 ? 11.055  -10.913 -15.240 1.00 36.56 ? 204 ARG B CZ  1 
ATOM   3485 N NH1 . ARG B 1 204 ? 12.216  -11.515 -15.392 1.00 32.84 ? 204 ARG B NH1 1 
ATOM   3486 N NH2 . ARG B 1 204 ? 9.942   -11.597 -15.392 1.00 31.90 ? 204 ARG B NH2 1 
ATOM   3487 N N   . LYS B 1 205 ? 12.241  -7.004  -19.337 1.00 35.80 ? 205 LYS B N   1 
ATOM   3488 C CA  . LYS B 1 205 ? 12.144  -6.385  -20.673 1.00 36.24 ? 205 LYS B CA  1 
ATOM   3489 C C   . LYS B 1 205 ? 10.725  -5.888  -20.921 1.00 39.90 ? 205 LYS B C   1 
ATOM   3490 O O   . LYS B 1 205 ? 9.810   -6.702  -20.967 1.00 41.04 ? 205 LYS B O   1 
ATOM   3491 C CB  . LYS B 1 205 ? 12.639  -7.377  -21.723 1.00 38.44 ? 205 LYS B CB  1 
ATOM   3492 C CG  . LYS B 1 205 ? 14.130  -7.289  -21.989 1.00 41.58 ? 205 LYS B CG  1 
ATOM   3493 C CD  . LYS B 1 205 ? 14.758  -8.539  -22.510 1.00 44.71 ? 205 LYS B CD  1 
ATOM   3494 C CE  . LYS B 1 205 ? 16.141  -8.757  -21.936 1.00 45.50 ? 205 LYS B CE  1 
ATOM   3495 N NZ  . LYS B 1 205 ? 16.424  -10.193 -21.737 1.00 46.16 ? 205 LYS B NZ  1 
ATOM   3496 N N   . TYR B 1 206 ? 10.590  -4.570  -21.026 1.00 39.41 ? 206 TYR B N   1 
ATOM   3497 C CA  . TYR B 1 206 ? 9.299   -3.903  -21.283 1.00 40.42 ? 206 TYR B CA  1 
ATOM   3498 C C   . TYR B 1 206 ? 9.332   -3.274  -22.671 1.00 39.70 ? 206 TYR B C   1 
ATOM   3499 O O   . TYR B 1 206 ? 10.164  -2.450  -22.987 1.00 40.58 ? 206 TYR B O   1 
ATOM   3500 C CB  . TYR B 1 206 ? 8.986   -2.836  -20.238 1.00 35.51 ? 206 TYR B CB  1 
ATOM   3501 C CG  . TYR B 1 206 ? 8.333   -3.367  -18.996 1.00 34.62 ? 206 TYR B CG  1 
ATOM   3502 C CD1 . TYR B 1 206 ? 9.095   -3.916  -17.989 1.00 33.54 ? 206 TYR B CD1 1 
ATOM   3503 C CD2 . TYR B 1 206 ? 6.971   -3.305  -18.812 1.00 32.04 ? 206 TYR B CD2 1 
ATOM   3504 C CE1 . TYR B 1 206 ? 8.536   -4.381  -16.818 1.00 34.79 ? 206 TYR B CE1 1 
ATOM   3505 C CE2 . TYR B 1 206 ? 6.392   -3.786  -17.660 1.00 32.65 ? 206 TYR B CE2 1 
ATOM   3506 C CZ  . TYR B 1 206 ? 7.172   -4.332  -16.659 1.00 34.33 ? 206 TYR B CZ  1 
ATOM   3507 O OH  . TYR B 1 206 ? 6.635   -4.821  -15.520 1.00 32.05 ? 206 TYR B OH  1 
ATOM   3508 N N   . LYS B 1 207 ? 8.356   -3.680  -23.477 1.00 43.77 ? 207 LYS B N   1 
ATOM   3509 C CA  . LYS B 1 207 ? 8.183   -3.146  -24.846 1.00 42.50 ? 207 LYS B CA  1 
ATOM   3510 C C   . LYS B 1 207 ? 7.854   -1.662  -24.665 1.00 42.03 ? 207 LYS B C   1 
ATOM   3511 O O   . LYS B 1 207 ? 6.994   -1.412  -23.838 1.00 36.58 ? 207 LYS B O   1 
ATOM   3512 C CB  . LYS B 1 207 ? 7.104   -3.978  -25.543 1.00 46.87 ? 207 LYS B CB  1 
ATOM   3513 C CG  . LYS B 1 207 ? 7.424   -5.467  -25.672 1.00 47.75 ? 207 LYS B CG  1 
ATOM   3514 C CD  . LYS B 1 207 ? 6.264   -6.440  -25.458 1.00 51.05 ? 207 LYS B CD  1 
ATOM   3515 C CE  . LYS B 1 207 ? 6.622   -7.913  -25.620 1.00 51.66 ? 207 LYS B CE  1 
ATOM   3516 N NZ  . LYS B 1 207 ? 7.286   -8.504  -24.429 1.00 52.28 ? 207 LYS B NZ  1 
ATOM   3517 N N   . PHE B 1 208 ? 8.538   -0.756  -25.388 1.00 40.81 ? 208 PHE B N   1 
ATOM   3518 C CA  . PHE B 1 208 ? 8.411   0.724   -25.215 1.00 39.93 ? 208 PHE B CA  1 
ATOM   3519 C C   . PHE B 1 208 ? 6.986   1.190   -24.920 1.00 43.45 ? 208 PHE B C   1 
ATOM   3520 O O   . PHE B 1 208 ? 6.789   1.852   -23.915 1.00 41.63 ? 208 PHE B O   1 
ATOM   3521 C CB  . PHE B 1 208 ? 8.955   1.481   -26.420 1.00 41.66 ? 208 PHE B CB  1 
ATOM   3522 C CG  . PHE B 1 208 ? 10.411  1.238   -26.686 1.00 40.74 ? 208 PHE B CG  1 
ATOM   3523 C CD1 . PHE B 1 208 ? 11.257  0.873   -25.664 1.00 40.58 ? 208 PHE B CD1 1 
ATOM   3524 C CD2 . PHE B 1 208 ? 10.926  1.357   -27.952 1.00 41.15 ? 208 PHE B CD2 1 
ATOM   3525 C CE1 . PHE B 1 208 ? 12.593  0.635   -25.908 1.00 41.59 ? 208 PHE B CE1 1 
ATOM   3526 C CE2 . PHE B 1 208 ? 12.260  1.106   -28.194 1.00 42.28 ? 208 PHE B CE2 1 
ATOM   3527 C CZ  . PHE B 1 208 ? 13.092  0.750   -27.171 1.00 41.35 ? 208 PHE B CZ  1 
ATOM   3528 N N   . SER B 1 209 ? 6.021   0.787   -25.738 1.00 41.48 ? 209 SER B N   1 
ATOM   3529 C CA  . SER B 1 209 ? 4.621   1.209   -25.498 1.00 41.65 ? 209 SER B CA  1 
ATOM   3530 C C   . SER B 1 209 ? 4.039   0.530   -24.255 1.00 41.37 ? 209 SER B C   1 
ATOM   3531 O O   . SER B 1 209 ? 3.207   1.147   -23.623 1.00 39.49 ? 209 SER B O   1 
ATOM   3532 C CB  . SER B 1 209 ? 3.770   0.978   -26.708 1.00 39.01 ? 209 SER B CB  1 
ATOM   3533 O OG  . SER B 1 209 ? 3.344   -0.359  -26.761 1.00 43.30 ? 209 SER B OG  1 
ATOM   3534 N N   . CYS B 1 210 ? 4.459   -0.693  -23.927 1.00 39.98 ? 210 CYS B N   1 
ATOM   3535 C CA  . CYS B 1 210 ? 3.904   -1.336  -22.741 1.00 40.45 ? 210 CYS B CA  1 
ATOM   3536 C C   . CYS B 1 210 ? 4.156   -0.492  -21.493 1.00 39.03 ? 210 CYS B C   1 
ATOM   3537 O O   . CYS B 1 210 ? 3.247   -0.270  -20.685 1.00 36.15 ? 210 CYS B O   1 
ATOM   3538 C CB  . CYS B 1 210 ? 4.487   -2.739  -22.606 1.00 37.53 ? 210 CYS B CB  1 
ATOM   3539 S SG  . CYS B 1 210 ? 3.899   -3.611  -21.197 1.00 43.92 ? 210 CYS B SG  1 
ATOM   3540 N N   . LEU B 1 211 ? 5.392   -0.017  -21.315 1.00 36.88 ? 211 LEU B N   1 
ATOM   3541 C CA  . LEU B 1 211 ? 5.737   0.811   -20.160 1.00 36.12 ? 211 LEU B CA  1 
ATOM   3542 C C   . LEU B 1 211 ? 5.204   2.232   -20.284 1.00 32.13 ? 211 LEU B C   1 
ATOM   3543 O O   . LEU B 1 211 ? 4.677   2.784   -19.308 1.00 33.58 ? 211 LEU B O   1 
ATOM   3544 C CB  . LEU B 1 211 ? 7.277   0.861   -19.988 1.00 33.46 ? 211 LEU B CB  1 
ATOM   3545 C CG  . LEU B 1 211 ? 7.839   1.415   -18.663 1.00 34.18 ? 211 LEU B CG  1 
ATOM   3546 C CD1 . LEU B 1 211 ? 7.271   0.711   -17.448 1.00 33.50 ? 211 LEU B CD1 1 
ATOM   3547 C CD2 . LEU B 1 211 ? 9.383   1.332   -18.606 1.00 33.50 ? 211 LEU B CD2 1 
ATOM   3548 N N   . ASP B 1 212 ? 5.363   2.850   -21.462 1.00 36.19 ? 212 ASP B N   1 
ATOM   3549 C CA  . ASP B 1 212 ? 5.008   4.269   -21.655 1.00 34.76 ? 212 ASP B CA  1 
ATOM   3550 C C   . ASP B 1 212 ? 3.546   4.539   -21.280 1.00 37.02 ? 212 ASP B C   1 
ATOM   3551 O O   . ASP B 1 212 ? 3.216   5.503   -20.564 1.00 34.98 ? 212 ASP B O   1 
ATOM   3552 C CB  . ASP B 1 212 ? 5.240   4.659   -23.116 1.00 36.76 ? 212 ASP B CB  1 
ATOM   3553 C CG  . ASP B 1 212 ? 6.715   4.666   -23.520 1.00 40.21 ? 212 ASP B CG  1 
ATOM   3554 O OD1 . ASP B 1 212 ? 7.613   4.775   -22.645 1.00 40.75 ? 212 ASP B OD1 1 
ATOM   3555 O OD2 . ASP B 1 212 ? 6.970   4.570   -24.740 1.00 40.19 ? 212 ASP B OD2 1 
ATOM   3556 N N   . ASN B 1 213 ? 2.661   3.668   -21.726 1.00 36.15 ? 213 ASN B N   1 
ATOM   3557 C CA  . ASN B 1 213 ? 1.232   3.891   -21.627 1.00 41.23 ? 213 ASN B CA  1 
ATOM   3558 C C   . ASN B 1 213 ? 0.629   3.225   -20.395 1.00 39.01 ? 213 ASN B C   1 
ATOM   3559 O O   . ASN B 1 213 ? -0.580  3.272   -20.217 1.00 39.42 ? 213 ASN B O   1 
ATOM   3560 C CB  . ASN B 1 213 ? 0.571   3.370   -22.909 1.00 43.22 ? 213 ASN B CB  1 
ATOM   3561 C CG  . ASN B 1 213 ? 1.039   4.128   -24.145 1.00 42.16 ? 213 ASN B CG  1 
ATOM   3562 O OD1 . ASN B 1 213 ? 1.415   5.297   -24.065 1.00 41.92 ? 213 ASN B OD1 1 
ATOM   3563 N ND2 . ASN B 1 213 ? 1.103   3.428   -25.276 1.00 39.62 ? 213 ASN B ND2 1 
ATOM   3564 N N   . ALA B 1 214 ? 1.448   2.602   -19.546 1.00 35.92 ? 214 ALA B N   1 
ATOM   3565 C CA  . ALA B 1 214 ? 0.981   1.919   -18.349 1.00 35.47 ? 214 ALA B CA  1 
ATOM   3566 C C   . ALA B 1 214 ? 0.829   2.811   -17.127 1.00 35.68 ? 214 ALA B C   1 
ATOM   3567 O O   . ALA B 1 214 ? 0.810   2.300   -16.007 1.00 36.16 ? 214 ALA B O   1 
ATOM   3568 C CB  . ALA B 1 214 ? 1.926   0.760   -18.016 1.00 34.78 ? 214 ALA B CB  1 
ATOM   3569 N N   . ASN B 1 215 ? 0.737   4.120   -17.319 1.00 37.79 ? 215 ASN B N   1 
ATOM   3570 C CA  . ASN B 1 215 ? 0.597   5.006   -16.135 1.00 37.37 ? 215 ASN B CA  1 
ATOM   3571 C C   . ASN B 1 215 ? -0.550  6.002   -16.354 1.00 38.95 ? 215 ASN B C   1 
ATOM   3572 O O   . ASN B 1 215 ? -0.444  7.118   -15.880 1.00 37.42 ? 215 ASN B O   1 
ATOM   3573 C CB  . ASN B 1 215 ? 1.920   5.687   -15.765 1.00 32.70 ? 215 ASN B CB  1 
ATOM   3574 C CG  . ASN B 1 215 ? 2.025   6.032   -14.297 1.00 33.29 ? 215 ASN B CG  1 
ATOM   3575 O OD1 . ASN B 1 215 ? 1.514   5.322   -13.452 1.00 36.20 ? 215 ASN B OD1 1 
ATOM   3576 N ND2 . ASN B 1 215 ? 2.683   7.128   -13.989 1.00 31.02 ? 215 ASN B ND2 1 
ATOM   3577 N N   . LYS B 1 216 ? -1.618  5.576   -17.034 1.00 44.14 ? 216 LYS B N   1 
ATOM   3578 C CA  . LYS B 1 216 ? -2.804  6.451   -17.267 1.00 39.80 ? 216 LYS B CA  1 
ATOM   3579 C C   . LYS B 1 216 ? -3.397  6.905   -15.927 1.00 40.66 ? 216 LYS B C   1 
ATOM   3580 O O   . LYS B 1 216 ? -3.468  6.095   -15.026 1.00 40.74 ? 216 LYS B O   1 
ATOM   3581 C CB  . LYS B 1 216 ? -3.826  5.747   -18.159 1.00 44.41 ? 216 LYS B CB  1 
ATOM   3582 C CG  . LYS B 1 216 ? -5.166  6.461   -18.279 1.00 50.07 ? 216 LYS B CG  1 
ATOM   3583 C CD  . LYS B 1 216 ? -6.360  5.553   -18.076 1.00 52.69 ? 216 LYS B CD  1 
ATOM   3584 C CE  . LYS B 1 216 ? -7.316  6.037   -17.010 1.00 51.02 ? 216 LYS B CE  1 
ATOM   3585 N NZ  . LYS B 1 216 ? -8.681  5.492   -17.214 1.00 57.35 ? 216 LYS B NZ  1 
ATOM   3586 N N   . GLY B 1 217 ? -3.796  8.173   -15.822 1.00 35.53 ? 217 GLY B N   1 
ATOM   3587 C CA  . GLY B 1 217 ? -4.378  8.745   -14.597 1.00 36.11 ? 217 GLY B CA  1 
ATOM   3588 C C   . GLY B 1 217 ? -3.327  9.259   -13.627 1.00 38.51 ? 217 GLY B C   1 
ATOM   3589 O O   . GLY B 1 217 ? -3.702  9.672   -12.524 1.00 42.53 ? 217 GLY B O   1 
ATOM   3590 N N   . TYR B 1 218 ? -2.042  9.118   -13.971 1.00 36.66 ? 218 TYR B N   1 
ATOM   3591 C CA  . TYR B 1 218 ? -0.905  9.497   -13.091 1.00 36.45 ? 218 TYR B CA  1 
ATOM   3592 C C   . TYR B 1 218 ? 0.117   10.316  -13.896 1.00 31.45 ? 218 TYR B C   1 
ATOM   3593 O O   . TYR B 1 218 ? -0.011  10.376  -15.103 1.00 32.95 ? 218 TYR B O   1 
ATOM   3594 C CB  . TYR B 1 218 ? -0.334  8.253   -12.400 1.00 36.30 ? 218 TYR B CB  1 
ATOM   3595 C CG  . TYR B 1 218 ? -1.322  7.479   -11.561 1.00 38.80 ? 218 TYR B CG  1 
ATOM   3596 C CD1 . TYR B 1 218 ? -2.130  6.505   -12.114 1.00 37.75 ? 218 TYR B CD1 1 
ATOM   3597 C CD2 . TYR B 1 218 ? -1.447  7.713   -10.207 1.00 35.48 ? 218 TYR B CD2 1 
ATOM   3598 C CE1 . TYR B 1 218 ? -3.061  5.819   -11.364 1.00 36.84 ? 218 TYR B CE1 1 
ATOM   3599 C CE2 . TYR B 1 218 ? -2.356  7.015   -9.433  1.00 40.02 ? 218 TYR B CE2 1 
ATOM   3600 C CZ  . TYR B 1 218 ? -3.159  6.060   -10.014 1.00 37.23 ? 218 TYR B CZ  1 
ATOM   3601 O OH  . TYR B 1 218 ? -4.059  5.379   -9.269  1.00 43.64 ? 218 TYR B OH  1 
ATOM   3602 N N   . ARG B 1 219 ? 1.116   10.893  -13.227 1.00 34.23 ? 219 ARG B N   1 
ATOM   3603 C CA  . ARG B 1 219 ? 2.091   11.799  -13.849 1.00 32.44 ? 219 ARG B CA  1 
ATOM   3604 C C   . ARG B 1 219 ? 2.761   11.151  -15.050 1.00 34.47 ? 219 ARG B C   1 
ATOM   3605 O O   . ARG B 1 219 ? 3.232   10.010  -14.988 1.00 35.28 ? 219 ARG B O   1 
ATOM   3606 C CB  . ARG B 1 219 ? 3.154   12.222  -12.835 1.00 33.58 ? 219 ARG B CB  1 
ATOM   3607 C CG  . ARG B 1 219 ? 4.162   13.257  -13.365 1.00 31.58 ? 219 ARG B CG  1 
ATOM   3608 C CD  . ARG B 1 219 ? 4.801   14.061  -12.227 1.00 32.90 ? 219 ARG B CD  1 
ATOM   3609 N NE  . ARG B 1 219 ? 5.908   14.881  -12.721 1.00 33.78 ? 219 ARG B NE  1 
ATOM   3610 C CZ  . ARG B 1 219 ? 6.634   15.688  -11.964 1.00 33.65 ? 219 ARG B CZ  1 
ATOM   3611 N NH1 . ARG B 1 219 ? 6.404   15.800  -10.668 1.00 35.73 ? 219 ARG B NH1 1 
ATOM   3612 N NH2 . ARG B 1 219 ? 7.594   16.415  -12.526 1.00 27.78 ? 219 ARG B NH2 1 
ATOM   3613 N N   . GLN B 1 220 ? 2.795   11.884  -16.151 1.00 32.15 ? 220 GLN B N   1 
ATOM   3614 C CA  . GLN B 1 220 ? 3.299   11.368  -17.426 1.00 32.69 ? 220 GLN B CA  1 
ATOM   3615 C C   . GLN B 1 220 ? 4.773   11.752  -17.611 1.00 36.35 ? 220 GLN B C   1 
ATOM   3616 O O   . GLN B 1 220 ? 5.143   12.531  -18.488 1.00 38.98 ? 220 GLN B O   1 
ATOM   3617 C CB  . GLN B 1 220 ? 2.455   11.916  -18.566 1.00 37.03 ? 220 GLN B CB  1 
ATOM   3618 C CG  . GLN B 1 220 ? 0.986   11.466  -18.529 1.00 31.16 ? 220 GLN B CG  1 
ATOM   3619 C CD  . GLN B 1 220 ? 0.897   9.977   -18.746 1.00 38.33 ? 220 GLN B CD  1 
ATOM   3620 O OE1 . GLN B 1 220 ? 1.084   9.485   -19.868 1.00 36.72 ? 220 GLN B OE1 1 
ATOM   3621 N NE2 . GLN B 1 220 ? 0.591   9.242   -17.681 1.00 38.46 ? 220 GLN B NE2 1 
ATOM   3622 N N   . ASN B 1 221 ? 5.640   11.164  -16.793 1.00 32.97 ? 221 ASN B N   1 
ATOM   3623 C CA  . ASN B 1 221 ? 7.078   11.406  -16.920 1.00 33.48 ? 221 ASN B CA  1 
ATOM   3624 C C   . ASN B 1 221 ? 7.849   10.124  -16.631 1.00 31.98 ? 221 ASN B C   1 
ATOM   3625 O O   . ASN B 1 221 ? 7.318   9.180   -16.033 1.00 34.50 ? 221 ASN B O   1 
ATOM   3626 C CB  . ASN B 1 221 ? 7.589   12.480  -15.950 1.00 30.26 ? 221 ASN B CB  1 
ATOM   3627 C CG  . ASN B 1 221 ? 7.093   13.887  -16.274 1.00 35.14 ? 221 ASN B CG  1 
ATOM   3628 O OD1 . ASN B 1 221 ? 6.429   14.516  -15.448 1.00 33.96 ? 221 ASN B OD1 1 
ATOM   3629 N ND2 . ASN B 1 221 ? 7.477   14.408  -17.444 1.00 33.79 ? 221 ASN B ND2 1 
ATOM   3630 N N   . TYR B 1 222 ? 9.112   10.091  -17.080 1.00 33.40 ? 222 TYR B N   1 
ATOM   3631 C CA  . TYR B 1 222 ? 10.155  9.271   -16.471 1.00 29.55 ? 222 TYR B CA  1 
ATOM   3632 C C   . TYR B 1 222 ? 11.127  10.218  -15.773 1.00 34.80 ? 222 TYR B C   1 
ATOM   3633 O O   . TYR B 1 222 ? 11.071  11.428  -15.985 1.00 32.33 ? 222 TYR B O   1 
ATOM   3634 C CB  . TYR B 1 222 ? 10.886  8.397   -17.502 1.00 30.26 ? 222 TYR B CB  1 
ATOM   3635 C CG  . TYR B 1 222 ? 10.057  7.324   -18.190 1.00 32.68 ? 222 TYR B CG  1 
ATOM   3636 C CD1 . TYR B 1 222 ? 9.176   6.525   -17.473 1.00 31.22 ? 222 TYR B CD1 1 
ATOM   3637 C CD2 . TYR B 1 222 ? 10.192  7.088   -19.556 1.00 34.48 ? 222 TYR B CD2 1 
ATOM   3638 C CE1 . TYR B 1 222 ? 8.412   5.559   -18.101 1.00 33.61 ? 222 TYR B CE1 1 
ATOM   3639 C CE2 . TYR B 1 222 ? 9.468   6.096   -20.187 1.00 33.47 ? 222 TYR B CE2 1 
ATOM   3640 C CZ  . TYR B 1 222 ? 8.577   5.350   -19.458 1.00 33.17 ? 222 TYR B CZ  1 
ATOM   3641 O OH  . TYR B 1 222 ? 7.838   4.388   -20.080 1.00 34.05 ? 222 TYR B OH  1 
ATOM   3642 N N   . TYR B 1 223 ? 12.052  9.674   -14.962 1.00 30.17 ? 223 TYR B N   1 
ATOM   3643 C CA  . TYR B 1 223 ? 12.875  10.485  -14.061 1.00 28.97 ? 223 TYR B CA  1 
ATOM   3644 C C   . TYR B 1 223 ? 14.365  10.128  -14.176 1.00 30.63 ? 223 TYR B C   1 
ATOM   3645 O O   . TYR B 1 223 ? 14.872  9.213   -13.503 1.00 26.92 ? 223 TYR B O   1 
ATOM   3646 C CB  . TYR B 1 223 ? 12.361  10.340  -12.632 1.00 27.83 ? 223 TYR B CB  1 
ATOM   3647 C CG  . TYR B 1 223 ? 10.878  10.597  -12.550 1.00 33.17 ? 223 TYR B CG  1 
ATOM   3648 C CD1 . TYR B 1 223 ? 10.389  11.914  -12.475 1.00 33.25 ? 223 TYR B CD1 1 
ATOM   3649 C CD2 . TYR B 1 223 ? 9.964   9.553   -12.544 1.00 28.10 ? 223 TYR B CD2 1 
ATOM   3650 C CE1 . TYR B 1 223 ? 9.045   12.188  -12.420 1.00 30.55 ? 223 TYR B CE1 1 
ATOM   3651 C CE2 . TYR B 1 223 ? 8.598   9.804   -12.490 1.00 28.24 ? 223 TYR B CE2 1 
ATOM   3652 C CZ  . TYR B 1 223 ? 8.146   11.116  -12.425 1.00 33.97 ? 223 TYR B CZ  1 
ATOM   3653 O OH  . TYR B 1 223 ? 6.799   11.363  -12.399 1.00 31.98 ? 223 TYR B OH  1 
ATOM   3654 N N   . VAL B 1 224 ? 15.085  10.904  -14.988 1.00 32.77 ? 224 VAL B N   1 
ATOM   3655 C CA  . VAL B 1 224 ? 16.527  10.709  -15.156 1.00 29.37 ? 224 VAL B CA  1 
ATOM   3656 C C   . VAL B 1 224 ? 17.253  11.057  -13.860 1.00 27.98 ? 224 VAL B C   1 
ATOM   3657 O O   . VAL B 1 224 ? 16.975  12.082  -13.227 1.00 29.67 ? 224 VAL B O   1 
ATOM   3658 C CB  . VAL B 1 224 ? 17.039  11.560  -16.327 1.00 30.21 ? 224 VAL B CB  1 
ATOM   3659 C CG1 . VAL B 1 224 ? 18.552  11.458  -16.459 1.00 29.03 ? 224 VAL B CG1 1 
ATOM   3660 C CG2 . VAL B 1 224 ? 16.354  11.169  -17.626 1.00 30.22 ? 224 VAL B CG2 1 
ATOM   3661 N N   . VAL B 1 225 ? 18.185  10.196  -13.452 1.00 26.58 ? 225 VAL B N   1 
ATOM   3662 C CA  . VAL B 1 225 ? 19.017  10.434  -12.275 1.00 26.24 ? 225 VAL B CA  1 
ATOM   3663 C C   . VAL B 1 225 ? 20.377  10.882  -12.779 1.00 26.20 ? 225 VAL B C   1 
ATOM   3664 O O   . VAL B 1 225 ? 21.003  10.180  -13.583 1.00 26.31 ? 225 VAL B O   1 
ATOM   3665 C CB  . VAL B 1 225 ? 19.175  9.176   -11.400 1.00 27.99 ? 225 VAL B CB  1 
ATOM   3666 C CG1 . VAL B 1 225 ? 19.936  9.538   -10.124 1.00 25.30 ? 225 VAL B CG1 1 
ATOM   3667 C CG2 . VAL B 1 225 ? 17.824  8.503   -11.079 1.00 22.90 ? 225 VAL B CG2 1 
ATOM   3668 N N   . CYS B 1 226 ? 20.836  12.047  -12.316 1.00 28.36 ? 226 CYS B N   1 
ATOM   3669 C CA  . CYS B 1 226 ? 22.151  12.488  -12.759 1.00 29.51 ? 226 CYS B CA  1 
ATOM   3670 C C   . CYS B 1 226 ? 22.874  13.177  -11.615 1.00 28.87 ? 226 CYS B C   1 
ATOM   3671 O O   . CYS B 1 226 ? 22.252  13.472  -10.590 1.00 26.36 ? 226 CYS B O   1 
ATOM   3672 C CB  . CYS B 1 226 ? 22.051  13.414  -13.968 1.00 32.01 ? 226 CYS B CB  1 
ATOM   3673 S SG  . CYS B 1 226 ? 21.324  14.995  -13.604 1.00 36.01 ? 226 CYS B SG  1 
ATOM   3674 N N   . PRO B 1 227 ? 24.188  13.437  -11.744 1.00 26.83 ? 227 PRO B N   1 
ATOM   3675 C CA  . PRO B 1 227 ? 24.892  14.156  -10.678 1.00 30.44 ? 227 PRO B CA  1 
ATOM   3676 C C   . PRO B 1 227 ? 24.361  15.558  -10.541 1.00 28.58 ? 227 PRO B C   1 
ATOM   3677 O O   . PRO B 1 227 ? 24.047  16.206  -11.536 1.00 29.90 ? 227 PRO B O   1 
ATOM   3678 C CB  . PRO B 1 227 ? 26.353  14.169  -11.147 1.00 30.64 ? 227 PRO B CB  1 
ATOM   3679 C CG  . PRO B 1 227 ? 26.450  12.955  -12.069 1.00 30.75 ? 227 PRO B CG  1 
ATOM   3680 C CD  . PRO B 1 227 ? 25.104  12.905  -12.765 1.00 28.15 ? 227 PRO B CD  1 
ATOM   3681 N N   . ALA B 1 228 ? 24.227  16.014  -9.302  1.00 28.76 ? 228 ALA B N   1 
ATOM   3682 C CA  . ALA B 1 228 ? 23.779  17.390  -9.091  1.00 34.25 ? 228 ALA B CA  1 
ATOM   3683 C C   . ALA B 1 228 ? 24.901  18.366  -9.452  1.00 36.26 ? 228 ALA B C   1 
ATOM   3684 O O   . ALA B 1 228 ? 26.067  18.025  -9.265  1.00 41.23 ? 228 ALA B O   1 
ATOM   3685 C CB  . ALA B 1 228 ? 23.335  17.605  -7.657  1.00 37.61 ? 228 ALA B CB  1 
ATOM   3686 N N   . MET C 1 1   ? -7.954  -12.185 41.328  1.00 49.39 ? 1   MET C N   1 
ATOM   3687 C CA  . MET C 1 1   ? -6.692  -12.918 41.118  1.00 47.52 ? 1   MET C CA  1 
ATOM   3688 C C   . MET C 1 1   ? -6.485  -13.867 42.294  1.00 45.54 ? 1   MET C C   1 
ATOM   3689 O O   . MET C 1 1   ? -6.399  -13.439 43.453  1.00 46.27 ? 1   MET C O   1 
ATOM   3690 C CB  . MET C 1 1   ? -5.505  -11.959 41.013  1.00 43.71 ? 1   MET C CB  1 
ATOM   3691 C CG  . MET C 1 1   ? -5.624  -10.859 39.969  1.00 45.31 ? 1   MET C CG  1 
ATOM   3692 S SD  . MET C 1 1   ? -4.016  -10.035 39.604  1.00 59.36 ? 1   MET C SD  1 
ATOM   3693 C CE  . MET C 1 1   ? -3.251  -11.278 38.617  1.00 42.94 ? 1   MET C CE  1 
ATOM   3694 N N   . VAL C 1 2   ? -6.285  -15.133 41.998  1.00 42.19 ? 2   VAL C N   1 
ATOM   3695 C CA  . VAL C 1 2   ? -6.245  -16.133 43.058  1.00 43.67 ? 2   VAL C CA  1 
ATOM   3696 C C   . VAL C 1 2   ? -4.829  -16.235 43.606  1.00 38.84 ? 2   VAL C C   1 
ATOM   3697 O O   . VAL C 1 2   ? -3.837  -16.092 42.879  1.00 35.36 ? 2   VAL C O   1 
ATOM   3698 C CB  . VAL C 1 2   ? -6.767  -17.491 42.555  1.00 43.86 ? 2   VAL C CB  1 
ATOM   3699 C CG1 . VAL C 1 2   ? -8.017  -17.288 41.727  1.00 44.39 ? 2   VAL C CG1 1 
ATOM   3700 C CG2 . VAL C 1 2   ? -5.705  -18.200 41.707  1.00 42.78 ? 2   VAL C CG2 1 
ATOM   3701 N N   . ARG C 1 3   ? -4.744  -16.332 44.923  1.00 37.48 ? 3   ARG C N   1 
ATOM   3702 C CA  . ARG C 1 3   ? -3.484  -16.462 45.619  1.00 39.00 ? 3   ARG C CA  1 
ATOM   3703 C C   . ARG C 1 3   ? -3.437  -17.803 46.343  1.00 39.31 ? 3   ARG C C   1 
ATOM   3704 O O   . ARG C 1 3   ? -4.481  -18.394 46.699  1.00 33.97 ? 3   ARG C O   1 
ATOM   3705 C CB  . ARG C 1 3   ? -3.274  -15.306 46.596  1.00 41.07 ? 3   ARG C CB  1 
ATOM   3706 C CG  . ARG C 1 3   ? -4.536  -14.744 47.121  1.00 39.58 ? 3   ARG C CG  1 
ATOM   3707 C CD  . ARG C 1 3   ? -4.380  -13.280 47.455  1.00 40.50 ? 3   ARG C CD  1 
ATOM   3708 N NE  . ARG C 1 3   ? -3.533  -13.085 48.624  1.00 45.89 ? 3   ARG C NE  1 
ATOM   3709 C CZ  . ARG C 1 3   ? -3.935  -13.233 49.878  1.00 45.86 ? 3   ARG C CZ  1 
ATOM   3710 N NH1 . ARG C 1 3   ? -5.179  -13.580 50.167  1.00 44.56 ? 3   ARG C NH1 1 
ATOM   3711 N NH2 . ARG C 1 3   ? -3.067  -13.017 50.868  1.00 48.87 ? 3   ARG C NH2 1 
ATOM   3712 N N   . PHE C 1 4   ? -2.215  -18.300 46.520  1.00 33.94 ? 4   PHE C N   1 
ATOM   3713 C CA  . PHE C 1 4   ? -1.992  -19.551 47.213  1.00 33.48 ? 4   PHE C CA  1 
ATOM   3714 C C   . PHE C 1 4   ? -0.965  -19.328 48.321  1.00 35.69 ? 4   PHE C C   1 
ATOM   3715 O O   . PHE C 1 4   ? 0.017   -18.597 48.142  1.00 34.67 ? 4   PHE C O   1 
ATOM   3716 C CB  . PHE C 1 4   ? -1.543  -20.598 46.234  1.00 34.78 ? 4   PHE C CB  1 
ATOM   3717 C CG  . PHE C 1 4   ? -2.464  -20.767 45.069  1.00 33.28 ? 4   PHE C CG  1 
ATOM   3718 C CD1 . PHE C 1 4   ? -3.556  -21.636 45.144  1.00 34.71 ? 4   PHE C CD1 1 
ATOM   3719 C CD2 . PHE C 1 4   ? -2.245  -20.078 43.892  1.00 32.43 ? 4   PHE C CD2 1 
ATOM   3720 C CE1 . PHE C 1 4   ? -4.395  -21.821 44.064  1.00 30.05 ? 4   PHE C CE1 1 
ATOM   3721 C CE2 . PHE C 1 4   ? -3.085  -20.266 42.801  1.00 34.24 ? 4   PHE C CE2 1 
ATOM   3722 C CZ  . PHE C 1 4   ? -4.176  -21.155 42.899  1.00 33.95 ? 4   PHE C CZ  1 
ATOM   3723 N N   . SER C 1 5   ? -1.226  -19.919 49.480  1.00 32.30 ? 5   SER C N   1 
ATOM   3724 C CA  . SER C 1 5   ? -0.438  -19.664 50.671  1.00 32.75 ? 5   SER C CA  1 
ATOM   3725 C C   . SER C 1 5   ? 0.892   -20.432 50.661  1.00 35.08 ? 5   SER C C   1 
ATOM   3726 O O   . SER C 1 5   ? 1.133   -21.318 49.849  1.00 32.68 ? 5   SER C O   1 
ATOM   3727 C CB  . SER C 1 5   ? -1.238  -20.039 51.911  1.00 34.97 ? 5   SER C CB  1 
ATOM   3728 O OG  . SER C 1 5   ? -1.292  -21.456 52.058  1.00 34.81 ? 5   SER C OG  1 
ATOM   3729 N N   . ARG C 1 6   ? 1.756   -20.075 51.608  1.00 36.23 ? 6   ARG C N   1 
ATOM   3730 C CA  . ARG C 1 6   ? 3.016   -20.790 51.774  1.00 37.46 ? 6   ARG C CA  1 
ATOM   3731 C C   . ARG C 1 6   ? 2.790   -22.282 51.971  1.00 38.20 ? 6   ARG C C   1 
ATOM   3732 O O   . ARG C 1 6   ? 3.507   -23.103 51.383  1.00 37.10 ? 6   ARG C O   1 
ATOM   3733 C CB  . ARG C 1 6   ? 3.760   -20.218 52.969  1.00 38.55 ? 6   ARG C CB  1 
ATOM   3734 C CG  . ARG C 1 6   ? 4.977   -20.970 53.374  1.00 36.88 ? 6   ARG C CG  1 
ATOM   3735 C CD  . ARG C 1 6   ? 5.809   -20.066 54.213  1.00 40.34 ? 6   ARG C CD  1 
ATOM   3736 N NE  . ARG C 1 6   ? 5.617   -20.379 55.624  1.00 47.31 ? 6   ARG C NE  1 
ATOM   3737 C CZ  . ARG C 1 6   ? 5.518   -19.465 56.576  1.00 47.03 ? 6   ARG C CZ  1 
ATOM   3738 N NH1 . ARG C 1 6   ? 5.578   -18.179 56.296  1.00 47.39 ? 6   ARG C NH1 1 
ATOM   3739 N NH2 . ARG C 1 6   ? 5.368   -19.857 57.841  1.00 54.21 ? 6   ARG C NH2 1 
ATOM   3740 N N   . ASP C 1 7   ? 1.791   -22.663 52.787  1.00 39.22 ? 7   ASP C N   1 
ATOM   3741 C CA  . ASP C 1 7   ? 1.585   -24.094 53.049  1.00 38.63 ? 7   ASP C CA  1 
ATOM   3742 C C   . ASP C 1 7   ? 1.133   -24.807 51.793  1.00 32.75 ? 7   ASP C C   1 
ATOM   3743 O O   . ASP C 1 7   ? 1.589   -25.915 51.500  1.00 38.31 ? 7   ASP C O   1 
ATOM   3744 C CB  . ASP C 1 7   ? 0.560   -24.319 54.166  1.00 43.29 ? 7   ASP C CB  1 
ATOM   3745 C CG  . ASP C 1 7   ? 1.134   -24.080 55.553  1.00 51.04 ? 7   ASP C CG  1 
ATOM   3746 O OD1 . ASP C 1 7   ? 2.318   -23.646 55.686  1.00 51.89 ? 7   ASP C OD1 1 
ATOM   3747 O OD2 . ASP C 1 7   ? 0.395   -24.331 56.523  1.00 55.63 ? 7   ASP C OD2 1 
ATOM   3748 N N   . MET C 1 8   ? 0.287   -24.158 51.010  1.00 32.15 ? 8   MET C N   1 
ATOM   3749 C CA  . MET C 1 8   ? -0.223  -24.766 49.794  1.00 32.79 ? 8   MET C CA  1 
ATOM   3750 C C   . MET C 1 8   ? 0.863   -24.926 48.734  1.00 34.63 ? 8   MET C C   1 
ATOM   3751 O O   . MET C 1 8   ? 0.891   -25.939 48.018  1.00 34.18 ? 8   MET C O   1 
ATOM   3752 C CB  . MET C 1 8   ? -1.377  -23.917 49.266  1.00 30.68 ? 8   MET C CB  1 
ATOM   3753 C CG  . MET C 1 8   ? -1.960  -24.406 47.978  1.00 30.52 ? 8   MET C CG  1 
ATOM   3754 S SD  . MET C 1 8   ? -2.778  -26.054 48.088  1.00 43.13 ? 8   MET C SD  1 
ATOM   3755 C CE  . MET C 1 8   ? -3.265  -26.153 49.788  1.00 36.06 ? 8   MET C CE  1 
ATOM   3756 N N   . LEU C 1 9   ? 1.776   -23.939 48.623  1.00 32.61 ? 9   LEU C N   1 
ATOM   3757 C CA  . LEU C 1 9   ? 2.859   -24.027 47.651  1.00 29.52 ? 9   LEU C CA  1 
ATOM   3758 C C   . LEU C 1 9   ? 3.806   -25.175 47.990  1.00 30.39 ? 9   LEU C C   1 
ATOM   3759 O O   . LEU C 1 9   ? 4.215   -25.937 47.095  1.00 27.13 ? 9   LEU C O   1 
ATOM   3760 C CB  . LEU C 1 9   ? 3.624   -22.688 47.583  1.00 30.32 ? 9   LEU C CB  1 
ATOM   3761 C CG  . LEU C 1 9   ? 2.819   -21.490 47.041  1.00 28.58 ? 9   LEU C CG  1 
ATOM   3762 C CD1 . LEU C 1 9   ? 3.524   -20.172 47.316  1.00 31.61 ? 9   LEU C CD1 1 
ATOM   3763 C CD2 . LEU C 1 9   ? 2.565   -21.681 45.560  1.00 27.99 ? 9   LEU C CD2 1 
ATOM   3764 N N   . GLN C 1 10  ? 4.150   -25.312 49.280  1.00 30.71 ? 10  GLN C N   1 
ATOM   3765 C CA  . GLN C 1 10  ? 4.996   -26.422 49.733  1.00 34.37 ? 10  GLN C CA  1 
ATOM   3766 C C   . GLN C 1 10  ? 4.346   -27.762 49.439  1.00 32.54 ? 10  GLN C C   1 
ATOM   3767 O O   . GLN C 1 10  ? 5.026   -28.705 49.003  1.00 31.34 ? 10  GLN C O   1 
ATOM   3768 C CB  . GLN C 1 10  ? 5.298   -26.304 51.233  1.00 32.89 ? 10  GLN C CB  1 
ATOM   3769 C CG  . GLN C 1 10  ? 6.100   -25.094 51.595  1.00 35.70 ? 10  GLN C CG  1 
ATOM   3770 C CD  . GLN C 1 10  ? 6.169   -24.847 53.084  1.00 39.51 ? 10  GLN C CD  1 
ATOM   3771 O OE1 . GLN C 1 10  ? 5.301   -25.294 53.833  1.00 46.50 ? 10  GLN C OE1 1 
ATOM   3772 N NE2 . GLN C 1 10  ? 7.178   -24.095 53.522  1.00 37.89 ? 10  GLN C NE2 1 
ATOM   3773 N N   . ASP C 1 11  ? 3.030   -27.871 49.685  1.00 31.32 ? 11  ASP C N   1 
ATOM   3774 C CA  . ASP C 1 11  ? 2.322   -29.112 49.400  1.00 33.73 ? 11  ASP C CA  1 
ATOM   3775 C C   . ASP C 1 11  ? 2.298   -29.402 47.907  1.00 32.88 ? 11  ASP C C   1 
ATOM   3776 O O   . ASP C 1 11  ? 2.489   -30.550 47.498  1.00 32.22 ? 11  ASP C O   1 
ATOM   3777 C CB  . ASP C 1 11  ? 0.873   -29.043 49.945  1.00 32.77 ? 11  ASP C CB  1 
ATOM   3778 C CG  . ASP C 1 11  ? 0.044   -30.271 49.581  1.00 36.15 ? 11  ASP C CG  1 
ATOM   3779 O OD1 . ASP C 1 11  ? -0.633  -30.313 48.498  1.00 34.91 ? 11  ASP C OD1 1 
ATOM   3780 O OD2 . ASP C 1 11  ? 0.110   -31.232 50.390  1.00 42.67 ? 11  ASP C OD2 1 
ATOM   3781 N N   . GLY C 1 12  ? 2.016   -28.387 47.067  1.00 32.49 ? 12  GLY C N   1 
ATOM   3782 C CA  . GLY C 1 12  ? 1.995   -28.629 45.627  1.00 28.10 ? 12  GLY C CA  1 
ATOM   3783 C C   . GLY C 1 12  ? 3.365   -29.009 45.063  1.00 29.20 ? 12  GLY C C   1 
ATOM   3784 O O   . GLY C 1 12  ? 3.467   -29.816 44.128  1.00 29.71 ? 12  GLY C O   1 
ATOM   3785 N N   . ALA C 1 13  ? 4.438   -28.430 45.612  1.00 32.41 ? 13  ALA C N   1 
ATOM   3786 C CA  . ALA C 1 13  ? 5.784   -28.721 45.121  1.00 26.53 ? 13  ALA C CA  1 
ATOM   3787 C C   . ALA C 1 13  ? 6.208   -30.137 45.481  1.00 28.59 ? 13  ALA C C   1 
ATOM   3788 O O   . ALA C 1 13  ? 6.785   -30.851 44.654  1.00 27.18 ? 13  ALA C O   1 
ATOM   3789 C CB  . ALA C 1 13  ? 6.795   -27.719 45.699  1.00 28.36 ? 13  ALA C CB  1 
ATOM   3790 N N   . LYS C 1 14  ? 5.958   -30.547 46.719  1.00 27.96 ? 14  LYS C N   1 
ATOM   3791 C CA  . LYS C 1 14  ? 6.206   -31.938 47.099  1.00 33.70 ? 14  LYS C CA  1 
ATOM   3792 C C   . LYS C 1 14  ? 5.511   -32.910 46.151  1.00 32.02 ? 14  LYS C C   1 
ATOM   3793 O O   . LYS C 1 14  ? 6.082   -33.940 45.774  1.00 30.05 ? 14  LYS C O   1 
ATOM   3794 C CB  . LYS C 1 14  ? 5.758   -32.173 48.541  1.00 33.99 ? 14  LYS C CB  1 
ATOM   3795 C CG  . LYS C 1 14  ? 6.697   -31.499 49.562  1.00 37.53 ? 14  LYS C CG  1 
ATOM   3796 C CD  . LYS C 1 14  ? 6.093   -31.454 50.968  1.00 45.94 ? 14  LYS C CD  1 
ATOM   3797 C CE  . LYS C 1 14  ? 5.121   -32.621 51.201  1.00 49.30 ? 14  LYS C CE  1 
ATOM   3798 N NZ  . LYS C 1 14  ? 5.218   -33.144 52.612  1.00 57.37 ? 14  LYS C NZ  1 
ATOM   3799 N N   . ARG C 1 15  ? 4.257   -32.621 45.784  1.00 29.88 ? 15  ARG C N   1 
ATOM   3800 C CA  . ARG C 1 15  ? 3.532   -33.518 44.885  1.00 29.40 ? 15  ARG C CA  1 
ATOM   3801 C C   . ARG C 1 15  ? 4.123   -33.496 43.485  1.00 29.97 ? 15  ARG C C   1 
ATOM   3802 O O   . ARG C 1 15  ? 4.136   -34.533 42.800  1.00 27.55 ? 15  ARG C O   1 
ATOM   3803 C CB  . ARG C 1 15  ? 2.024   -33.176 44.912  1.00 31.46 ? 15  ARG C CB  1 
ATOM   3804 C CG  . ARG C 1 15  ? 1.401   -33.477 46.290  1.00 29.72 ? 15  ARG C CG  1 
ATOM   3805 C CD  . ARG C 1 15  ? 0.038   -32.788 46.593  1.00 33.58 ? 15  ARG C CD  1 
ATOM   3806 N NE  . ARG C 1 15  ? -0.618  -32.412 45.361  1.00 35.58 ? 15  ARG C NE  1 
ATOM   3807 C CZ  . ARG C 1 15  ? -1.225  -31.254 45.158  1.00 30.11 ? 15  ARG C CZ  1 
ATOM   3808 N NH1 . ARG C 1 15  ? -1.286  -30.326 46.110  1.00 32.69 ? 15  ARG C NH1 1 
ATOM   3809 N NH2 . ARG C 1 15  ? -1.747  -31.013 43.962  1.00 30.57 ? 15  ARG C NH2 1 
ATOM   3810 N N   . MET C 1 16  ? 4.691   -32.353 43.113  1.00 30.21 ? 16  MET C N   1 
ATOM   3811 C CA  . MET C 1 16  ? 5.369   -32.202 41.803  1.00 31.09 ? 16  MET C CA  1 
ATOM   3812 C C   . MET C 1 16  ? 6.636   -33.064 41.841  1.00 29.27 ? 16  MET C C   1 
ATOM   3813 O O   . MET C 1 16  ? 6.840   -33.830 40.939  1.00 28.33 ? 16  MET C O   1 
ATOM   3814 C CB  . MET C 1 16  ? 5.774   -30.747 41.550  1.00 27.32 ? 16  MET C CB  1 
ATOM   3815 C CG  . MET C 1 16  ? 4.668   -29.860 41.016  1.00 29.31 ? 16  MET C CG  1 
ATOM   3816 S SD  . MET C 1 16  ? 3.766   -30.412 39.565  1.00 30.06 ? 16  MET C SD  1 
ATOM   3817 C CE  . MET C 1 16  ? 4.773   -29.826 38.222  1.00 31.72 ? 16  MET C CE  1 
ATOM   3818 N N   . PHE C 1 17  ? 7.433   -32.911 42.891  1.00 29.91 ? 17  PHE C N   1 
ATOM   3819 C CA  . PHE C 1 17  ? 8.710   -33.652 43.064  1.00 28.40 ? 17  PHE C CA  1 
ATOM   3820 C C   . PHE C 1 17  ? 8.417   -35.152 43.031  1.00 30.76 ? 17  PHE C C   1 
ATOM   3821 O O   . PHE C 1 17  ? 9.090   -35.885 42.355  1.00 30.75 ? 17  PHE C O   1 
ATOM   3822 C CB  . PHE C 1 17  ? 9.348   -33.254 44.393  1.00 24.46 ? 17  PHE C CB  1 
ATOM   3823 C CG  . PHE C 1 17  ? 10.773  -33.699 44.592  1.00 29.11 ? 17  PHE C CG  1 
ATOM   3824 C CD1 . PHE C 1 17  ? 11.688  -33.611 43.562  1.00 26.08 ? 17  PHE C CD1 1 
ATOM   3825 C CD2 . PHE C 1 17  ? 11.202  -34.199 45.809  1.00 28.39 ? 17  PHE C CD2 1 
ATOM   3826 C CE1 . PHE C 1 17  ? 13.002  -34.006 43.748  1.00 28.91 ? 17  PHE C CE1 1 
ATOM   3827 C CE2 . PHE C 1 17  ? 12.514  -34.603 45.989  1.00 29.98 ? 17  PHE C CE2 1 
ATOM   3828 C CZ  . PHE C 1 17  ? 13.414  -34.494 44.962  1.00 27.11 ? 17  PHE C CZ  1 
ATOM   3829 N N   . LYS C 1 18  ? 7.388   -35.540 43.775  1.00 40.72 ? 18  LYS C N   1 
ATOM   3830 C CA  . LYS C 1 18  ? 6.896   -36.931 43.872  1.00 34.28 ? 18  LYS C CA  1 
ATOM   3831 C C   . LYS C 1 18  ? 6.448   -37.387 42.482  1.00 33.23 ? 18  LYS C C   1 
ATOM   3832 O O   . LYS C 1 18  ? 6.908   -38.458 42.131  1.00 33.45 ? 18  LYS C O   1 
ATOM   3833 C CB  . LYS C 1 18  ? 5.839   -37.033 44.973  1.00 39.20 ? 18  LYS C CB  1 
ATOM   3834 C CG  . LYS C 1 18  ? 5.632   -38.391 45.621  1.00 52.00 ? 18  LYS C CG  1 
ATOM   3835 C CD  . LYS C 1 18  ? 4.400   -38.461 46.528  1.00 41.24 ? 18  LYS C CD  1 
ATOM   3836 C CE  . LYS C 1 18  ? 4.294   -37.350 47.560  1.00 46.93 ? 18  LYS C CE  1 
ATOM   3837 N NZ  . LYS C 1 18  ? 2.965   -36.696 47.561  1.00 52.71 ? 18  LYS C NZ  1 
ATOM   3838 N N   . TRP C 1 19  ? 5.645   -36.613 41.721  1.00 34.09 ? 19  TRP C N   1 
ATOM   3839 C CA  . TRP C 1 19  ? 5.306   -37.127 40.391  1.00 33.75 ? 19  TRP C CA  1 
ATOM   3840 C C   . TRP C 1 19  ? 6.555   -37.367 39.561  1.00 34.14 ? 19  TRP C C   1 
ATOM   3841 O O   . TRP C 1 19  ? 6.651   -38.347 38.825  1.00 33.83 ? 19  TRP C O   1 
ATOM   3842 C CB  . TRP C 1 19  ? 4.371   -36.091 39.863  1.00 31.31 ? 19  TRP C CB  1 
ATOM   3843 C CG  . TRP C 1 19  ? 3.886   -36.446 38.546  1.00 33.41 ? 19  TRP C CG  1 
ATOM   3844 C CD1 . TRP C 1 19  ? 4.475   -36.151 37.359  1.00 33.73 ? 19  TRP C CD1 1 
ATOM   3845 C CD2 . TRP C 1 19  ? 2.700   -37.216 38.226  1.00 35.41 ? 19  TRP C CD2 1 
ATOM   3846 N NE1 . TRP C 1 19  ? 3.749   -36.671 36.314  1.00 34.81 ? 19  TRP C NE1 1 
ATOM   3847 C CE2 . TRP C 1 19  ? 2.650   -37.319 36.814  1.00 34.07 ? 19  TRP C CE2 1 
ATOM   3848 C CE3 . TRP C 1 19  ? 1.667   -37.801 38.988  1.00 36.17 ? 19  TRP C CE3 1 
ATOM   3849 C CZ2 . TRP C 1 19  ? 1.617   -37.982 36.143  1.00 34.92 ? 19  TRP C CZ2 1 
ATOM   3850 C CZ3 . TRP C 1 19  ? 0.631   -38.468 38.317  1.00 35.70 ? 19  TRP C CZ3 1 
ATOM   3851 C CH2 . TRP C 1 19  ? 0.621   -38.550 36.906  1.00 37.06 ? 19  TRP C CH2 1 
ATOM   3852 N N   . LEU C 1 20  ? 7.505   -36.446 39.654  1.00 34.42 ? 20  LEU C N   1 
ATOM   3853 C CA  . LEU C 1 20  ? 8.736   -36.485 38.828  1.00 32.37 ? 20  LEU C CA  1 
ATOM   3854 C C   . LEU C 1 20  ? 9.568   -37.738 39.100  1.00 33.45 ? 20  LEU C C   1 
ATOM   3855 O O   . LEU C 1 20  ? 10.204  -38.197 38.184  1.00 35.44 ? 20  LEU C O   1 
ATOM   3856 C CB  . LEU C 1 20  ? 9.525   -35.199 39.052  1.00 31.45 ? 20  LEU C CB  1 
ATOM   3857 C CG  . LEU C 1 20  ? 9.033   -34.039 38.207  1.00 27.12 ? 20  LEU C CG  1 
ATOM   3858 C CD1 . LEU C 1 20  ? 9.682   -32.749 38.638  1.00 30.05 ? 20  LEU C CD1 1 
ATOM   3859 C CD2 . LEU C 1 20  ? 9.273   -34.301 36.740  1.00 30.19 ? 20  LEU C CD2 1 
ATOM   3860 N N   . ARG C 1 21  ? 9.475   -38.309 40.292  1.00 34.30 ? 21  ARG C N   1 
ATOM   3861 C CA  . ARG C 1 21  ? 10.152  -39.577 40.693  1.00 40.14 ? 21  ARG C CA  1 
ATOM   3862 C C   . ARG C 1 21  ? 10.006  -40.659 39.602  1.00 44.05 ? 21  ARG C C   1 
ATOM   3863 O O   . ARG C 1 21  ? 10.989  -41.302 39.285  1.00 45.27 ? 21  ARG C O   1 
ATOM   3864 C CB  . ARG C 1 21  ? 9.508   -40.034 42.004  1.00 42.22 ? 21  ARG C CB  1 
ATOM   3865 C CG  . ARG C 1 21  ? 10.355  -40.890 42.934  1.00 54.63 ? 21  ARG C CG  1 
ATOM   3866 C CD  . ARG C 1 21  ? 9.490   -42.039 43.440  1.00 61.33 ? 21  ARG C CD  1 
ATOM   3867 N NE  . ARG C 1 21  ? 9.669   -43.299 42.703  1.00 64.76 ? 21  ARG C NE  1 
ATOM   3868 C CZ  . ARG C 1 21  ? 8.731   -43.932 42.006  1.00 64.07 ? 21  ARG C CZ  1 
ATOM   3869 N NH1 . ARG C 1 21  ? 9.022   -45.055 41.378  1.00 68.57 ? 21  ARG C NH1 1 
ATOM   3870 N NH2 . ARG C 1 21  ? 7.506   -43.453 41.955  1.00 61.60 ? 21  ARG C NH2 1 
ATOM   3871 N N   . LYS C 1 22  ? 8.808   -40.839 39.049  1.00 40.34 ? 22  LYS C N   1 
ATOM   3872 C CA  . LYS C 1 22  ? 8.453   -41.806 37.983  1.00 39.33 ? 22  LYS C CA  1 
ATOM   3873 C C   . LYS C 1 22  ? 9.278   -41.676 36.701  1.00 39.83 ? 22  LYS C C   1 
ATOM   3874 O O   . LYS C 1 22  ? 9.241   -42.615 35.946  1.00 40.50 ? 22  LYS C O   1 
ATOM   3875 C CB  . LYS C 1 22  ? 6.971   -41.641 37.659  1.00 38.68 ? 22  LYS C CB  1 
ATOM   3876 C CG  . LYS C 1 22  ? 6.084   -41.617 38.888  1.00 39.34 ? 22  LYS C CG  1 
ATOM   3877 C CD  . LYS C 1 22  ? 4.667   -41.950 38.589  1.00 44.04 ? 22  LYS C CD  1 
ATOM   3878 C CE  . LYS C 1 22  ? 4.171   -41.265 37.344  1.00 40.32 ? 22  LYS C CE  1 
ATOM   3879 N NZ  . LYS C 1 22  ? 4.601   -39.855 37.324  1.00 43.33 ? 22  LYS C NZ  1 
ATOM   3880 N N   . GLY C 1 23  ? 9.961   -40.565 36.440  1.00 36.62 ? 23  GLY C N   1 
ATOM   3881 C CA  . GLY C 1 23  ? 10.731  -40.460 35.227  1.00 37.65 ? 23  GLY C CA  1 
ATOM   3882 C C   . GLY C 1 23  ? 9.860   -40.377 34.000  1.00 37.39 ? 23  GLY C C   1 
ATOM   3883 O O   . GLY C 1 23  ? 10.321  -40.691 32.904  1.00 38.39 ? 23  GLY C O   1 
ATOM   3884 N N   . GLU C 1 24  ? 8.610   -39.928 34.155  1.00 39.82 ? 24  GLU C N   1 
ATOM   3885 C CA  . GLU C 1 24  ? 7.648   -39.844 33.060  1.00 40.15 ? 24  GLU C CA  1 
ATOM   3886 C C   . GLU C 1 24  ? 7.294   -38.410 32.683  1.00 42.45 ? 24  GLU C C   1 
ATOM   3887 O O   . GLU C 1 24  ? 6.255   -38.180 32.051  1.00 37.60 ? 24  GLU C O   1 
ATOM   3888 C CB  . GLU C 1 24  ? 6.384   -40.630 33.418  1.00 36.01 ? 24  GLU C CB  1 
ATOM   3889 C CG  . GLU C 1 24  ? 6.707   -42.033 33.896  1.00 39.70 ? 24  GLU C CG  1 
ATOM   3890 C CD  . GLU C 1 24  ? 5.549   -42.990 33.769  1.00 43.72 ? 24  GLU C CD  1 
ATOM   3891 O OE1 . GLU C 1 24  ? 4.428   -42.647 34.250  1.00 43.12 ? 24  GLU C OE1 1 
ATOM   3892 O OE2 . GLU C 1 24  ? 5.785   -44.108 33.222  1.00 42.06 ? 24  GLU C OE2 1 
ATOM   3893 N N   . GLY C 1 25  ? 8.117   -37.432 33.077  1.00 39.75 ? 25  GLY C N   1 
ATOM   3894 C CA  . GLY C 1 25  ? 7.808   -36.048 32.780  1.00 37.82 ? 25  GLY C CA  1 
ATOM   3895 C C   . GLY C 1 25  ? 6.813   -35.391 33.740  1.00 36.13 ? 25  GLY C C   1 
ATOM   3896 O O   . GLY C 1 25  ? 6.387   -35.936 34.775  1.00 32.11 ? 25  GLY C O   1 
ATOM   3897 N N   . LEU C 1 26  ? 6.457   -34.154 33.376  1.00 32.39 ? 26  LEU C N   1 
ATOM   3898 C CA  . LEU C 1 26  ? 5.604   -33.321 34.205  1.00 34.18 ? 26  LEU C CA  1 
ATOM   3899 C C   . LEU C 1 26  ? 4.127   -33.746 34.106  1.00 32.93 ? 26  LEU C C   1 
ATOM   3900 O O   . LEU C 1 26  ? 3.666   -34.167 33.044  1.00 35.14 ? 26  LEU C O   1 
ATOM   3901 C CB  . LEU C 1 26  ? 5.754   -31.863 33.776  1.00 32.05 ? 26  LEU C CB  1 
ATOM   3902 C CG  . LEU C 1 26  ? 7.085   -31.200 34.158  1.00 35.00 ? 26  LEU C CG  1 
ATOM   3903 C CD1 . LEU C 1 26  ? 7.275   -29.858 33.412  1.00 34.67 ? 26  LEU C CD1 1 
ATOM   3904 C CD2 . LEU C 1 26  ? 7.144   -31.006 35.675  1.00 29.66 ? 26  LEU C CD2 1 
ATOM   3905 N N   . PRO C 1 27  ? 3.355   -33.589 35.180  1.00 35.20 ? 27  PRO C N   1 
ATOM   3906 C CA  . PRO C 1 27  ? 1.931   -33.960 35.123  1.00 31.50 ? 27  PRO C CA  1 
ATOM   3907 C C   . PRO C 1 27  ? 1.149   -32.990 34.266  1.00 36.22 ? 27  PRO C C   1 
ATOM   3908 O O   . PRO C 1 27  ? 1.541   -31.834 34.052  1.00 31.52 ? 27  PRO C O   1 
ATOM   3909 C CB  . PRO C 1 27  ? 1.467   -33.858 36.576  1.00 30.90 ? 27  PRO C CB  1 
ATOM   3910 C CG  . PRO C 1 27  ? 2.396   -32.885 37.238  1.00 33.73 ? 27  PRO C CG  1 
ATOM   3911 C CD  . PRO C 1 27  ? 3.653   -32.755 36.367  1.00 33.69 ? 27  PRO C CD  1 
ATOM   3912 N N   . ASN C 1 28  ? -0.027  -33.452 33.845  1.00 35.90 ? 28  ASN C N   1 
ATOM   3913 C CA  . ASN C 1 28  ? -0.876  -32.652 32.977  1.00 35.97 ? 28  ASN C CA  1 
ATOM   3914 C C   . ASN C 1 28  ? -1.504  -31.466 33.698  1.00 33.50 ? 28  ASN C C   1 
ATOM   3915 O O   . ASN C 1 28  ? -1.881  -30.489 33.048  1.00 35.16 ? 28  ASN C O   1 
ATOM   3916 C CB  . ASN C 1 28  ? -1.968  -33.551 32.387  1.00 44.10 ? 28  ASN C CB  1 
ATOM   3917 C CG  . ASN C 1 28  ? -1.455  -34.399 31.260  1.00 49.57 ? 28  ASN C CG  1 
ATOM   3918 O OD1 . ASN C 1 28  ? -0.769  -33.892 30.375  1.00 50.48 ? 28  ASN C OD1 1 
ATOM   3919 N ND2 . ASN C 1 28  ? -1.749  -35.708 31.298  1.00 53.49 ? 28  ASN C ND2 1 
ATOM   3920 N N   . TYR C 1 29  ? -1.614  -31.517 35.020  1.00 33.56 ? 29  TYR C N   1 
ATOM   3921 C CA  . TYR C 1 29  ? -2.181  -30.421 35.792  1.00 31.46 ? 29  TYR C CA  1 
ATOM   3922 C C   . TYR C 1 29  ? -1.750  -30.634 37.231  1.00 32.07 ? 29  TYR C C   1 
ATOM   3923 O O   . TYR C 1 29  ? -1.291  -31.716 37.607  1.00 32.99 ? 29  TYR C O   1 
ATOM   3924 C CB  . TYR C 1 29  ? -3.719  -30.351 35.665  1.00 40.15 ? 29  TYR C CB  1 
ATOM   3925 C CG  . TYR C 1 29  ? -4.452  -31.531 36.307  1.00 41.69 ? 29  TYR C CG  1 
ATOM   3926 C CD1 . TYR C 1 29  ? -4.435  -31.732 37.687  1.00 41.45 ? 29  TYR C CD1 1 
ATOM   3927 C CD2 . TYR C 1 29  ? -5.150  -32.443 35.529  1.00 45.31 ? 29  TYR C CD2 1 
ATOM   3928 C CE1 . TYR C 1 29  ? -5.056  -32.803 38.258  1.00 47.81 ? 29  TYR C CE1 1 
ATOM   3929 C CE2 . TYR C 1 29  ? -5.821  -33.519 36.109  1.00 48.92 ? 29  TYR C CE2 1 
ATOM   3930 C CZ  . TYR C 1 29  ? -5.767  -33.694 37.476  1.00 53.38 ? 29  TYR C CZ  1 
ATOM   3931 O OH  . TYR C 1 29  ? -6.410  -34.767 38.079  1.00 57.95 ? 29  TYR C OH  1 
ATOM   3932 N N   . LEU C 1 30  ? -1.928  -29.603 38.037  1.00 27.89 ? 30  LEU C N   1 
ATOM   3933 C CA  . LEU C 1 30  ? -1.594  -29.633 39.455  1.00 32.88 ? 30  LEU C CA  1 
ATOM   3934 C C   . LEU C 1 30  ? -2.755  -29.051 40.252  1.00 35.05 ? 30  LEU C C   1 
ATOM   3935 O O   . LEU C 1 30  ? -3.172  -27.925 39.970  1.00 32.59 ? 30  LEU C O   1 
ATOM   3936 C CB  . LEU C 1 30  ? -0.303  -28.830 39.747  1.00 30.54 ? 30  LEU C CB  1 
ATOM   3937 C CG  . LEU C 1 30  ? 0.132   -28.823 41.206  1.00 29.72 ? 30  LEU C CG  1 
ATOM   3938 C CD1 . LEU C 1 30  ? 0.649   -30.229 41.569  1.00 30.26 ? 30  LEU C CD1 1 
ATOM   3939 C CD2 . LEU C 1 30  ? 1.178   -27.752 41.510  1.00 29.73 ? 30  LEU C CD2 1 
ATOM   3940 N N   . ILE C 1 31  ? -3.244  -29.797 41.259  1.00 33.50 ? 31  ILE C N   1 
ATOM   3941 C CA  . ILE C 1 31  ? -4.378  -29.366 42.076  1.00 36.05 ? 31  ILE C CA  1 
ATOM   3942 C C   . ILE C 1 31  ? -3.871  -28.393 43.120  1.00 34.22 ? 31  ILE C C   1 
ATOM   3943 O O   . ILE C 1 31  ? -2.940  -28.714 43.864  1.00 35.89 ? 31  ILE C O   1 
ATOM   3944 C CB  . ILE C 1 31  ? -5.050  -30.564 42.792  1.00 37.72 ? 31  ILE C CB  1 
ATOM   3945 C CG1 . ILE C 1 31  ? -5.382  -31.716 41.864  1.00 37.18 ? 31  ILE C CG1 1 
ATOM   3946 C CG2 . ILE C 1 31  ? -6.279  -30.104 43.522  1.00 35.28 ? 31  ILE C CG2 1 
ATOM   3947 C CD1 . ILE C 1 31  ? -6.216  -31.328 40.767  1.00 41.95 ? 31  ILE C CD1 1 
ATOM   3948 N N   . MET C 1 32  ? -4.523  -27.234 43.227  1.00 32.94 ? 32  MET C N   1 
ATOM   3949 C CA  . MET C 1 32  ? -4.184  -26.257 44.246  1.00 34.72 ? 32  MET C CA  1 
ATOM   3950 C C   . MET C 1 32  ? -5.471  -25.644 44.813  1.00 37.06 ? 32  MET C C   1 
ATOM   3951 O O   . MET C 1 32  ? -6.482  -25.559 44.124  1.00 36.55 ? 32  MET C O   1 
ATOM   3952 C CB  . MET C 1 32  ? -3.294  -25.148 43.634  1.00 32.29 ? 32  MET C CB  1 
ATOM   3953 C CG  . MET C 1 32  ? -1.767  -25.585 43.351  1.00 32.47 ? 32  MET C CG  1 
ATOM   3954 S SD  . MET C 1 32  ? -0.855  -26.133 44.794  1.00 35.11 ? 32  MET C SD  1 
ATOM   3955 C CE  . MET C 1 32  ? 0.204   -24.646 45.105  1.00 32.09 ? 32  MET C CE  1 
ATOM   3956 N N   . TYR C 1 33  ? -5.428  -25.239 46.084  1.00 36.93 ? 33  TYR C N   1 
ATOM   3957 C CA  . TYR C 1 33  ? -6.551  -24.581 46.747  1.00 40.80 ? 33  TYR C CA  1 
ATOM   3958 C C   . TYR C 1 33  ? -6.135  -23.170 47.168  1.00 37.40 ? 33  TYR C C   1 
ATOM   3959 O O   . TYR C 1 33  ? -5.186  -23.013 47.942  1.00 37.42 ? 33  TYR C O   1 
ATOM   3960 C CB  . TYR C 1 33  ? -7.013  -25.419 47.945  1.00 40.32 ? 33  TYR C CB  1 
ATOM   3961 C CG  . TYR C 1 33  ? -7.363  -26.855 47.543  1.00 40.19 ? 33  TYR C CG  1 
ATOM   3962 C CD1 . TYR C 1 33  ? -8.657  -27.195 47.121  1.00 37.79 ? 33  TYR C CD1 1 
ATOM   3963 C CD2 . TYR C 1 33  ? -6.385  -27.855 47.532  1.00 37.91 ? 33  TYR C CD2 1 
ATOM   3964 C CE1 . TYR C 1 33  ? -8.970  -28.511 46.723  1.00 37.55 ? 33  TYR C CE1 1 
ATOM   3965 C CE2 . TYR C 1 33  ? -6.687  -29.154 47.141  1.00 36.59 ? 33  TYR C CE2 1 
ATOM   3966 C CZ  . TYR C 1 33  ? -7.977  -29.484 46.742  1.00 36.05 ? 33  TYR C CZ  1 
ATOM   3967 O OH  . TYR C 1 33  ? -8.255  -30.792 46.352  1.00 35.42 ? 33  TYR C OH  1 
ATOM   3968 N N   . ASP C 1 34  ? -6.873  -22.153 46.706  1.00 39.52 ? 34  ASP C N   1 
ATOM   3969 C CA  . ASP C 1 34  ? -6.554  -20.770 47.062  1.00 34.61 ? 34  ASP C CA  1 
ATOM   3970 C C   . ASP C 1 34  ? -6.732  -20.535 48.556  1.00 37.26 ? 34  ASP C C   1 
ATOM   3971 O O   . ASP C 1 34  ? -7.494  -21.237 49.225  1.00 40.62 ? 34  ASP C O   1 
ATOM   3972 C CB  . ASP C 1 34  ? -7.402  -19.799 46.268  1.00 35.23 ? 34  ASP C CB  1 
ATOM   3973 C CG  . ASP C 1 34  ? -8.771  -19.538 46.925  1.00 40.67 ? 34  ASP C CG  1 
ATOM   3974 O OD1 . ASP C 1 34  ? -9.683  -20.323 46.613  1.00 39.53 ? 34  ASP C OD1 1 
ATOM   3975 O OD2 . ASP C 1 34  ? -8.897  -18.564 47.727  1.00 37.67 ? 34  ASP C OD2 1 
ATOM   3976 N N   . MET C 1 35  ? -6.019  -19.536 49.087  1.00 35.25 ? 35  MET C N   1 
ATOM   3977 C CA  . MET C 1 35  ? -6.046  -19.292 50.521  1.00 37.14 ? 35  MET C CA  1 
ATOM   3978 C C   . MET C 1 35  ? -7.241  -18.457 50.945  1.00 40.42 ? 35  MET C C   1 
ATOM   3979 O O   . MET C 1 35  ? -7.456  -18.308 52.153  1.00 43.31 ? 35  MET C O   1 
ATOM   3980 C CB  . MET C 1 35  ? -4.800  -18.561 51.009  1.00 38.89 ? 35  MET C CB  1 
ATOM   3981 C CG  . MET C 1 35  ? -4.503  -17.264 50.285  1.00 38.74 ? 35  MET C CG  1 
ATOM   3982 S SD  . MET C 1 35  ? -2.934  -16.502 50.767  1.00 41.66 ? 35  MET C SD  1 
ATOM   3983 C CE  . MET C 1 35  ? -2.919  -16.486 52.534  1.00 32.63 ? 35  MET C CE  1 
ATOM   3984 N N   . ASP C 1 36  ? -8.004  -17.912 49.989  1.00 37.00 ? 36  ASP C N   1 
ATOM   3985 C CA  . ASP C 1 36  ? -9.055  -16.980 50.354  1.00 42.64 ? 36  ASP C CA  1 
ATOM   3986 C C   . ASP C 1 36  ? -10.360 -17.707 50.557  1.00 45.17 ? 36  ASP C C   1 
ATOM   3987 O O   . ASP C 1 36  ? -10.978 -17.509 51.595  1.00 49.17 ? 36  ASP C O   1 
ATOM   3988 C CB  . ASP C 1 36  ? -9.200  -15.852 49.335  1.00 36.86 ? 36  ASP C CB  1 
ATOM   3989 C CG  . ASP C 1 36  ? -7.993  -14.910 49.369  1.00 44.17 ? 36  ASP C CG  1 
ATOM   3990 O OD1 . ASP C 1 36  ? -7.688  -14.334 50.451  1.00 39.90 ? 36  ASP C OD1 1 
ATOM   3991 O OD2 . ASP C 1 36  ? -7.288  -14.820 48.332  1.00 42.37 ? 36  ASP C OD2 1 
ATOM   3992 N N   . ARG C 1 37  ? -10.776 -18.521 49.590  1.00 46.51 ? 37  ARG C N   1 
ATOM   3993 C CA  . ARG C 1 37  ? -12.067 -19.238 49.709  1.00 43.01 ? 37  ARG C CA  1 
ATOM   3994 C C   . ARG C 1 37  ? -11.866 -20.753 49.621  1.00 47.67 ? 37  ARG C C   1 
ATOM   3995 O O   . ARG C 1 37  ? -12.865 -21.476 49.595  1.00 43.30 ? 37  ARG C O   1 
ATOM   3996 C CB  . ARG C 1 37  ? -12.965 -18.792 48.560  1.00 49.51 ? 37  ARG C CB  1 
ATOM   3997 C CG  . ARG C 1 37  ? -13.504 -17.381 48.722  1.00 55.46 ? 37  ARG C CG  1 
ATOM   3998 C CD  . ARG C 1 37  ? -13.964 -16.788 47.407  1.00 57.50 ? 37  ARG C CD  1 
ATOM   3999 N NE  . ARG C 1 37  ? -15.245 -17.210 46.853  1.00 60.03 ? 37  ARG C NE  1 
ATOM   4000 C CZ  . ARG C 1 37  ? -16.214 -17.867 47.483  1.00 64.13 ? 37  ARG C CZ  1 
ATOM   4001 N NH1 . ARG C 1 37  ? -17.323 -18.155 46.834  1.00 63.91 ? 37  ARG C NH1 1 
ATOM   4002 N NH2 . ARG C 1 37  ? -16.092 -18.224 48.745  1.00 62.40 ? 37  ARG C NH2 1 
ATOM   4003 N N   . ASN C 1 38  ? -10.618 -21.207 49.594  1.00 42.18 ? 38  ASN C N   1 
ATOM   4004 C CA  . ASN C 1 38  ? -10.308 -22.626 49.427  1.00 43.54 ? 38  ASN C CA  1 
ATOM   4005 C C   . ASN C 1 38  ? -11.057 -23.344 48.300  1.00 43.85 ? 38  ASN C C   1 
ATOM   4006 O O   . ASN C 1 38  ? -11.498 -24.476 48.476  1.00 38.55 ? 38  ASN C O   1 
ATOM   4007 C CB  . ASN C 1 38  ? -10.527 -23.368 50.744  1.00 46.09 ? 38  ASN C CB  1 
ATOM   4008 C CG  . ASN C 1 38  ? -9.261  -24.051 51.234  1.00 53.09 ? 38  ASN C CG  1 
ATOM   4009 O OD1 . ASN C 1 38  ? -8.145  -23.541 51.013  1.00 55.31 ? 38  ASN C OD1 1 
ATOM   4010 N ND2 . ASN C 1 38  ? -9.409  -25.212 51.888  1.00 51.90 ? 38  ASN C ND2 1 
ATOM   4011 N N   . LYS C 1 39  ? -11.188 -22.690 47.142  1.00 40.73 ? 39  LYS C N   1 
ATOM   4012 C CA  . LYS C 1 39  ? -11.754 -23.356 45.971  1.00 38.34 ? 39  LYS C CA  1 
ATOM   4013 C C   . LYS C 1 39  ? -10.672 -24.151 45.213  1.00 42.46 ? 39  LYS C C   1 
ATOM   4014 O O   . LYS C 1 39  ? -9.479  -23.820 45.254  1.00 38.89 ? 39  LYS C O   1 
ATOM   4015 C CB  . LYS C 1 39  ? -12.463 -22.362 45.057  1.00 37.92 ? 39  LYS C CB  1 
ATOM   4016 C CG  . LYS C 1 39  ? -12.456 -22.692 43.574  1.00 41.98 ? 39  LYS C CG  1 
ATOM   4017 C CD  . LYS C 1 39  ? -12.635 -21.465 42.714  1.00 43.67 ? 39  LYS C CD  1 
ATOM   4018 C CE  . LYS C 1 39  ? -13.095 -21.807 41.274  1.00 43.74 ? 39  LYS C CE  1 
ATOM   4019 N NZ  . LYS C 1 39  ? -12.449 -23.060 40.756  1.00 48.21 ? 39  LYS C NZ  1 
ATOM   4020 N N   . GLU C 1 40  ? -11.087 -25.282 44.642  1.00 40.05 ? 40  GLU C N   1 
ATOM   4021 C CA  . GLU C 1 40  ? -10.201 -26.164 43.896  1.00 40.55 ? 40  GLU C CA  1 
ATOM   4022 C C   . GLU C 1 40  ? -9.908  -25.621 42.512  1.00 41.66 ? 40  GLU C C   1 
ATOM   4023 O O   . GLU C 1 40  ? -10.832 -25.325 41.746  1.00 38.52 ? 40  GLU C O   1 
ATOM   4024 C CB  . GLU C 1 40  ? -10.825 -27.560 43.776  1.00 37.52 ? 40  GLU C CB  1 
ATOM   4025 C CG  . GLU C 1 40  ? -9.842  -28.647 43.363  1.00 38.75 ? 40  GLU C CG  1 
ATOM   4026 C CD  . GLU C 1 40  ? -10.398 -30.044 43.588  1.00 35.24 ? 40  GLU C CD  1 
ATOM   4027 O OE1 . GLU C 1 40  ? -10.405 -30.517 44.745  1.00 34.87 ? 40  GLU C OE1 1 
ATOM   4028 O OE2 . GLU C 1 40  ? -10.781 -30.679 42.601  1.00 35.93 ? 40  GLU C OE2 1 
ATOM   4029 N N   . TYR C 1 41  ? -8.616  -25.583 42.180  1.00 38.36 ? 41  TYR C N   1 
ATOM   4030 C CA  . TYR C 1 41  ? -8.145  -25.125 40.853  1.00 37.13 ? 41  TYR C CA  1 
ATOM   4031 C C   . TYR C 1 41  ? -7.229  -26.190 40.239  1.00 38.51 ? 41  TYR C C   1 
ATOM   4032 O O   . TYR C 1 41  ? -6.366  -26.713 40.934  1.00 38.75 ? 41  TYR C O   1 
ATOM   4033 C CB  . TYR C 1 41  ? -7.391  -23.798 40.972  1.00 38.85 ? 41  TYR C CB  1 
ATOM   4034 C CG  . TYR C 1 41  ? -8.222  -22.600 41.350  1.00 38.30 ? 41  TYR C CG  1 
ATOM   4035 C CD1 . TYR C 1 41  ? -8.347  -22.209 42.665  1.00 37.72 ? 41  TYR C CD1 1 
ATOM   4036 C CD2 . TYR C 1 41  ? -8.884  -21.854 40.392  1.00 39.97 ? 41  TYR C CD2 1 
ATOM   4037 C CE1 . TYR C 1 41  ? -9.121  -21.120 43.023  1.00 39.41 ? 41  TYR C CE1 1 
ATOM   4038 C CE2 . TYR C 1 41  ? -9.647  -20.751 40.730  1.00 38.65 ? 41  TYR C CE2 1 
ATOM   4039 C CZ  . TYR C 1 41  ? -9.759  -20.376 42.053  1.00 40.32 ? 41  TYR C CZ  1 
ATOM   4040 O OH  . TYR C 1 41  ? -10.500 -19.291 42.407  1.00 36.08 ? 41  TYR C OH  1 
ATOM   4041 N N   . LYS C 1 42  ? -7.420  -26.475 38.959  1.00 37.28 ? 42  LYS C N   1 
ATOM   4042 C CA  . LYS C 1 42  ? -6.591  -27.459 38.228  1.00 39.68 ? 42  LYS C CA  1 
ATOM   4043 C C   . LYS C 1 42  ? -5.665  -26.669 37.294  1.00 37.11 ? 42  LYS C C   1 
ATOM   4044 O O   . LYS C 1 42  ? -6.033  -26.439 36.146  1.00 36.09 ? 42  LYS C O   1 
ATOM   4045 C CB  . LYS C 1 42  ? -7.487  -28.363 37.381  1.00 42.72 ? 42  LYS C CB  1 
ATOM   4046 C CG  . LYS C 1 42  ? -8.163  -29.541 38.067  1.00 46.06 ? 42  LYS C CG  1 
ATOM   4047 C CD  . LYS C 1 42  ? -8.625  -30.553 37.018  1.00 52.57 ? 42  LYS C CD  1 
ATOM   4048 C CE  . LYS C 1 42  ? -9.871  -31.334 37.380  1.00 58.13 ? 42  LYS C CE  1 
ATOM   4049 N NZ  . LYS C 1 42  ? -10.813 -31.461 36.240  1.00 57.95 ? 42  LYS C NZ  1 
ATOM   4050 N N   . LEU C 1 43  ? -4.506  -26.264 37.794  1.00 31.78 ? 43  LEU C N   1 
ATOM   4051 C CA  . LEU C 1 43  ? -3.591  -25.464 37.013  1.00 31.80 ? 43  LEU C CA  1 
ATOM   4052 C C   . LEU C 1 43  ? -2.944  -26.294 35.911  1.00 29.23 ? 43  LEU C C   1 
ATOM   4053 O O   . LEU C 1 43  ? -2.340  -27.333 36.172  1.00 31.93 ? 43  LEU C O   1 
ATOM   4054 C CB  . LEU C 1 43  ? -2.521  -24.904 37.938  1.00 31.57 ? 43  LEU C CB  1 
ATOM   4055 C CG  . LEU C 1 43  ? -3.011  -24.195 39.183  1.00 30.25 ? 43  LEU C CG  1 
ATOM   4056 C CD1 . LEU C 1 43  ? -1.824  -23.542 39.858  1.00 30.98 ? 43  LEU C CD1 1 
ATOM   4057 C CD2 . LEU C 1 43  ? -4.005  -23.128 38.799  1.00 32.99 ? 43  LEU C CD2 1 
ATOM   4058 N N   . VAL C 1 44  ? -3.046  -25.820 34.678  1.00 28.88 ? 44  VAL C N   1 
ATOM   4059 C CA  . VAL C 1 44  ? -2.359  -26.434 33.546  1.00 32.52 ? 44  VAL C CA  1 
ATOM   4060 C C   . VAL C 1 44  ? -0.859  -26.144 33.659  1.00 31.60 ? 44  VAL C C   1 
ATOM   4061 O O   . VAL C 1 44  ? -0.465  -25.297 34.472  1.00 32.26 ? 44  VAL C O   1 
ATOM   4062 C CB  . VAL C 1 44  ? -2.948  -25.908 32.230  1.00 33.62 ? 44  VAL C CB  1 
ATOM   4063 C CG1 . VAL C 1 44  ? -4.442  -26.073 32.236  1.00 31.22 ? 44  VAL C CG1 1 
ATOM   4064 C CG2 . VAL C 1 44  ? -2.586  -24.447 32.040  1.00 33.17 ? 44  VAL C CG2 1 
ATOM   4065 N N   . PRO C 1 45  ? 0.010   -26.809 32.891  1.00 33.90 ? 45  PRO C N   1 
ATOM   4066 C CA  . PRO C 1 45  ? 1.458   -26.646 33.145  1.00 31.99 ? 45  PRO C CA  1 
ATOM   4067 C C   . PRO C 1 45  ? 1.982   -25.215 33.066  1.00 32.08 ? 45  PRO C C   1 
ATOM   4068 O O   . PRO C 1 45  ? 2.734   -24.784 33.955  1.00 33.59 ? 45  PRO C O   1 
ATOM   4069 C CB  . PRO C 1 45  ? 2.083   -27.526 32.057  1.00 32.30 ? 45  PRO C CB  1 
ATOM   4070 C CG  . PRO C 1 45  ? 1.058   -28.650 31.857  1.00 32.73 ? 45  PRO C CG  1 
ATOM   4071 C CD  . PRO C 1 45  ? -0.267  -27.924 31.953  1.00 35.33 ? 45  PRO C CD  1 
ATOM   4072 N N   . LYS C 1 46  ? 1.557   -24.459 32.061  1.00 34.21 ? 46  LYS C N   1 
ATOM   4073 C CA  . LYS C 1 46  ? 2.027   -23.063 31.918  1.00 37.55 ? 46  LYS C CA  1 
ATOM   4074 C C   . LYS C 1 46  ? 1.552   -22.227 33.108  1.00 33.56 ? 46  LYS C C   1 
ATOM   4075 O O   . LYS C 1 46  ? 2.216   -21.252 33.408  1.00 32.28 ? 46  LYS C O   1 
ATOM   4076 C CB  . LYS C 1 46  ? 1.670   -22.498 30.548  1.00 41.05 ? 46  LYS C CB  1 
ATOM   4077 C CG  . LYS C 1 46  ? 0.418   -21.649 30.514  1.00 38.39 ? 46  LYS C CG  1 
ATOM   4078 C CD  . LYS C 1 46  ? -0.138  -21.494 29.124  1.00 46.65 ? 46  LYS C CD  1 
ATOM   4079 C CE  . LYS C 1 46  ? -0.866  -22.735 28.655  1.00 47.25 ? 46  LYS C CE  1 
ATOM   4080 N NZ  . LYS C 1 46  ? -1.320  -22.631 27.250  1.00 48.47 ? 46  LYS C NZ  1 
ATOM   4081 N N   . GLU C 1 47  ? 0.455   -22.629 33.753  1.00 31.49 ? 47  GLU C N   1 
ATOM   4082 C CA  . GLU C 1 47  ? -0.017  -21.924 34.941  1.00 28.51 ? 47  GLU C CA  1 
ATOM   4083 C C   . GLU C 1 47  ? 0.786   -22.283 36.196  1.00 28.58 ? 47  GLU C C   1 
ATOM   4084 O O   . GLU C 1 47  ? 1.166   -21.393 36.977  1.00 27.78 ? 47  GLU C O   1 
ATOM   4085 C CB  . GLU C 1 47  ? -1.483  -22.258 35.191  1.00 32.66 ? 47  GLU C CB  1 
ATOM   4086 C CG  . GLU C 1 47  ? -2.443  -21.321 34.536  1.00 31.83 ? 47  GLU C CG  1 
ATOM   4087 C CD  . GLU C 1 47  ? -3.859  -21.855 34.715  1.00 37.38 ? 47  GLU C CD  1 
ATOM   4088 O OE1 . GLU C 1 47  ? -3.996  -23.112 34.857  1.00 30.42 ? 47  GLU C OE1 1 
ATOM   4089 O OE2 . GLU C 1 47  ? -4.791  -21.027 34.730  1.00 34.07 ? 47  GLU C OE2 1 
ATOM   4090 N N   . TYR C 1 48  ? 1.033   -23.584 36.444  1.00 27.18 ? 48  TYR C N   1 
ATOM   4091 C CA  . TYR C 1 48  ? 1.781   -23.908 37.647  1.00 26.94 ? 48  TYR C CA  1 
ATOM   4092 C C   . TYR C 1 48  ? 3.261   -23.543 37.489  1.00 27.43 ? 48  TYR C C   1 
ATOM   4093 O O   . TYR C 1 48  ? 3.936   -23.269 38.491  1.00 26.00 ? 48  TYR C O   1 
ATOM   4094 C CB  . TYR C 1 48  ? 1.597   -25.370 38.052  1.00 24.37 ? 48  TYR C CB  1 
ATOM   4095 C CG  . TYR C 1 48  ? 2.075   -26.483 37.138  1.00 26.54 ? 48  TYR C CG  1 
ATOM   4096 C CD1 . TYR C 1 48  ? 3.444   -26.726 36.928  1.00 28.03 ? 48  TYR C CD1 1 
ATOM   4097 C CD2 . TYR C 1 48  ? 1.166   -27.411 36.627  1.00 29.36 ? 48  TYR C CD2 1 
ATOM   4098 C CE1 . TYR C 1 48  ? 3.889   -27.805 36.116  1.00 25.01 ? 48  TYR C CE1 1 
ATOM   4099 C CE2 . TYR C 1 48  ? 1.582   -28.492 35.847  1.00 31.34 ? 48  TYR C CE2 1 
ATOM   4100 C CZ  . TYR C 1 48  ? 2.953   -28.695 35.591  1.00 32.81 ? 48  TYR C CZ  1 
ATOM   4101 O OH  . TYR C 1 48  ? 3.360   -29.783 34.815  1.00 32.52 ? 48  TYR C OH  1 
ATOM   4102 N N   . ALA C 1 49  ? 3.776   -23.566 36.257  1.00 25.52 ? 49  ALA C N   1 
ATOM   4103 C CA  . ALA C 1 49  ? 5.125   -23.056 36.019  1.00 27.92 ? 49  ALA C CA  1 
ATOM   4104 C C   . ALA C 1 49  ? 5.184   -21.553 36.278  1.00 29.75 ? 49  ALA C C   1 
ATOM   4105 O O   . ALA C 1 49  ? 6.155   -21.058 36.870  1.00 25.39 ? 49  ALA C O   1 
ATOM   4106 C CB  . ALA C 1 49  ? 5.575   -23.375 34.592  1.00 28.92 ? 49  ALA C CB  1 
ATOM   4107 N N   . GLY C 1 50  ? 4.135   -20.816 35.877  1.00 26.57 ? 50  GLY C N   1 
ATOM   4108 C CA  . GLY C 1 50  ? 4.121   -19.381 36.135  1.00 24.97 ? 50  GLY C CA  1 
ATOM   4109 C C   . GLY C 1 50  ? 4.022   -19.068 37.613  1.00 26.52 ? 50  GLY C C   1 
ATOM   4110 O O   . GLY C 1 50  ? 4.679   -18.157 38.118  1.00 23.56 ? 50  GLY C O   1 
ATOM   4111 N N   . LEU C 1 51  ? 3.196   -19.817 38.330  1.00 25.95 ? 51  LEU C N   1 
ATOM   4112 C CA  . LEU C 1 51  ? 3.061   -19.616 39.766  1.00 25.64 ? 51  LEU C CA  1 
ATOM   4113 C C   . LEU C 1 51  ? 4.374   -19.890 40.498  1.00 24.46 ? 51  LEU C C   1 
ATOM   4114 O O   . LEU C 1 51  ? 4.735   -19.180 41.446  1.00 24.56 ? 51  LEU C O   1 
ATOM   4115 C CB  . LEU C 1 51  ? 1.956   -20.547 40.305  1.00 24.77 ? 51  LEU C CB  1 
ATOM   4116 C CG  . LEU C 1 51  ? 1.710   -20.524 41.808  1.00 26.31 ? 51  LEU C CG  1 
ATOM   4117 C CD1 . LEU C 1 51  ? 1.072   -19.173 42.188  1.00 32.55 ? 51  LEU C CD1 1 
ATOM   4118 C CD2 . LEU C 1 51  ? 0.758   -21.681 42.221  1.00 29.74 ? 51  LEU C CD2 1 
ATOM   4119 N N   . TYR C 1 52  ? 5.033   -21.002 40.164  1.00 22.44 ? 52  TYR C N   1 
ATOM   4120 C CA  . TYR C 1 52  ? 6.231   -21.362 40.904  1.00 25.24 ? 52  TYR C CA  1 
ATOM   4121 C C   . TYR C 1 52  ? 7.408   -20.522 40.450  1.00 23.26 ? 52  TYR C C   1 
ATOM   4122 O O   . TYR C 1 52  ? 8.323   -20.311 41.238  1.00 20.89 ? 52  TYR C O   1 
ATOM   4123 C CB  . TYR C 1 52  ? 6.515   -22.875 40.801  1.00 24.96 ? 52  TYR C CB  1 
ATOM   4124 C CG  . TYR C 1 52  ? 5.687   -23.635 41.819  1.00 23.59 ? 52  TYR C CG  1 
ATOM   4125 C CD1 . TYR C 1 52  ? 6.143   -23.764 43.143  1.00 20.83 ? 52  TYR C CD1 1 
ATOM   4126 C CD2 . TYR C 1 52  ? 4.392   -24.130 41.491  1.00 26.00 ? 52  TYR C CD2 1 
ATOM   4127 C CE1 . TYR C 1 52  ? 5.332   -24.414 44.127  1.00 26.72 ? 52  TYR C CE1 1 
ATOM   4128 C CE2 . TYR C 1 52  ? 3.576   -24.813 42.471  1.00 26.69 ? 52  TYR C CE2 1 
ATOM   4129 C CZ  . TYR C 1 52  ? 4.063   -24.933 43.768  1.00 28.61 ? 52  TYR C CZ  1 
ATOM   4130 O OH  . TYR C 1 52  ? 3.328   -25.578 44.722  1.00 27.75 ? 52  TYR C OH  1 
ATOM   4131 N N   . GLU C 1 53  ? 7.354   -19.992 39.229  1.00 21.34 ? 53  GLU C N   1 
ATOM   4132 C CA  . GLU C 1 53  ? 8.339   -18.971 38.843  1.00 26.98 ? 53  GLU C CA  1 
ATOM   4133 C C   . GLU C 1 53  ? 8.292   -17.781 39.787  1.00 24.41 ? 53  GLU C C   1 
ATOM   4134 O O   . GLU C 1 53  ? 9.337   -17.254 40.212  1.00 24.16 ? 53  GLU C O   1 
ATOM   4135 C CB  . GLU C 1 53  ? 8.098   -18.530 37.398  1.00 27.55 ? 53  GLU C CB  1 
ATOM   4136 C CG  . GLU C 1 53  ? 9.216   -17.633 36.827  1.00 28.05 ? 53  GLU C CG  1 
ATOM   4137 C CD  . GLU C 1 53  ? 8.802   -16.996 35.514  1.00 30.61 ? 53  GLU C CD  1 
ATOM   4138 O OE1 . GLU C 1 53  ? 7.732   -16.358 35.452  1.00 28.81 ? 53  GLU C OE1 1 
ATOM   4139 O OE2 . GLU C 1 53  ? 9.546   -17.151 34.529  1.00 30.28 ? 53  GLU C OE2 1 
ATOM   4140 N N   . SER C 1 54  ? 7.077   -17.289 40.062  1.00 24.56 ? 54  SER C N   1 
ATOM   4141 C CA  . SER C 1 54  ? 6.916   -16.126 40.923  1.00 23.29 ? 54  SER C CA  1 
ATOM   4142 C C   . SER C 1 54  ? 7.376   -16.452 42.317  1.00 24.67 ? 54  SER C C   1 
ATOM   4143 O O   . SER C 1 54  ? 8.071   -15.651 42.945  1.00 23.23 ? 54  SER C O   1 
ATOM   4144 C CB  . SER C 1 54  ? 5.450   -15.675 40.978  1.00 29.25 ? 54  SER C CB  1 
ATOM   4145 O OG  . SER C 1 54  ? 4.973   -15.236 39.726  1.00 34.74 ? 54  SER C OG  1 
ATOM   4146 N N   . ARG C 1 55  ? 7.024   -17.648 42.804  1.00 21.90 ? 55  ARG C N   1 
ATOM   4147 C CA  . ARG C 1 55  ? 7.509   -18.088 44.105  1.00 22.31 ? 55  ARG C CA  1 
ATOM   4148 C C   . ARG C 1 55  ? 9.046   -18.062 44.165  1.00 24.61 ? 55  ARG C C   1 
ATOM   4149 O O   . ARG C 1 55  ? 9.630   -17.533 45.119  1.00 22.06 ? 55  ARG C O   1 
ATOM   4150 C CB  . ARG C 1 55  ? 6.986   -19.497 44.404  1.00 19.28 ? 55  ARG C CB  1 
ATOM   4151 C CG  . ARG C 1 55  ? 7.350   -20.011 45.785  1.00 22.65 ? 55  ARG C CG  1 
ATOM   4152 C CD  . ARG C 1 55  ? 7.131   -21.537 45.858  1.00 21.27 ? 55  ARG C CD  1 
ATOM   4153 N NE  . ARG C 1 55  ? 7.260   -22.029 47.222  1.00 25.21 ? 55  ARG C NE  1 
ATOM   4154 C CZ  . ARG C 1 55  ? 7.688   -23.243 47.582  1.00 30.49 ? 55  ARG C CZ  1 
ATOM   4155 N NH1 . ARG C 1 55  ? 8.094   -24.147 46.690  1.00 27.64 ? 55  ARG C NH1 1 
ATOM   4156 N NH2 . ARG C 1 55  ? 7.699   -23.575 48.875  1.00 34.14 ? 55  ARG C NH2 1 
ATOM   4157 N N   . ASN C 1 56  ? 9.713   -18.620 43.141  1.00 24.05 ? 56  ASN C N   1 
ATOM   4158 C CA  . ASN C 1 56  ? 11.170  -18.735 43.189  1.00 23.79 ? 56  ASN C CA  1 
ATOM   4159 C C   . ASN C 1 56  ? 11.839  -17.358 43.075  1.00 21.23 ? 56  ASN C C   1 
ATOM   4160 O O   . ASN C 1 56  ? 12.880  -17.115 43.697  1.00 24.47 ? 56  ASN C O   1 
ATOM   4161 C CB  . ASN C 1 56  ? 11.670  -19.688 42.082  1.00 21.26 ? 56  ASN C CB  1 
ATOM   4162 C CG  . ASN C 1 56  ? 11.217  -21.139 42.294  1.00 23.21 ? 56  ASN C CG  1 
ATOM   4163 O OD1 . ASN C 1 56  ? 10.962  -21.555 43.419  1.00 25.20 ? 56  ASN C OD1 1 
ATOM   4164 N ND2 . ASN C 1 56  ? 11.110  -21.912 41.201  1.00 21.63 ? 56  ASN C ND2 1 
ATOM   4165 N N   . ILE C 1 57  ? 11.263  -16.442 42.284  1.00 24.20 ? 57  ILE C N   1 
ATOM   4166 C CA  . ILE C 1 57  ? 11.796  -15.080 42.236  1.00 20.78 ? 57  ILE C CA  1 
ATOM   4167 C C   . ILE C 1 57  ? 11.902  -14.489 43.640  1.00 26.77 ? 57  ILE C C   1 
ATOM   4168 O O   . ILE C 1 57  ? 12.991  -14.054 44.078  1.00 24.03 ? 57  ILE C O   1 
ATOM   4169 C CB  . ILE C 1 57  ? 10.950  -14.188 41.317  1.00 20.96 ? 57  ILE C CB  1 
ATOM   4170 C CG1 . ILE C 1 57  ? 11.229  -14.539 39.866  1.00 23.21 ? 57  ILE C CG1 1 
ATOM   4171 C CG2 . ILE C 1 57  ? 11.256  -12.661 41.590  1.00 20.91 ? 57  ILE C CG2 1 
ATOM   4172 C CD1 . ILE C 1 57  ? 10.290  -13.930 38.857  1.00 24.04 ? 57  ILE C CD1 1 
ATOM   4173 N N   . PHE C 1 58  ? 10.787  -14.491 44.383  1.00 23.52 ? 58  PHE C N   1 
ATOM   4174 C CA  . PHE C 1 58  ? 10.792  -13.929 45.733  1.00 26.91 ? 58  PHE C CA  1 
ATOM   4175 C C   . PHE C 1 58  ? 11.774  -14.681 46.642  1.00 25.63 ? 58  PHE C C   1 
ATOM   4176 O O   . PHE C 1 58  ? 12.540  -14.065 47.406  1.00 25.73 ? 58  PHE C O   1 
ATOM   4177 C CB  . PHE C 1 58  ? 9.361   -13.978 46.310  1.00 29.28 ? 58  PHE C CB  1 
ATOM   4178 C CG  . PHE C 1 58  ? 9.225   -13.372 47.685  1.00 31.19 ? 58  PHE C CG  1 
ATOM   4179 C CD1 . PHE C 1 58  ? 9.692   -14.054 48.807  1.00 30.96 ? 58  PHE C CD1 1 
ATOM   4180 C CD2 . PHE C 1 58  ? 8.612   -12.123 47.858  1.00 34.51 ? 58  PHE C CD2 1 
ATOM   4181 C CE1 . PHE C 1 58  ? 9.577   -13.519 50.073  1.00 33.96 ? 58  PHE C CE1 1 
ATOM   4182 C CE2 . PHE C 1 58  ? 8.486   -11.558 49.140  1.00 36.80 ? 58  PHE C CE2 1 
ATOM   4183 C CZ  . PHE C 1 58  ? 8.960   -12.271 50.254  1.00 35.67 ? 58  PHE C CZ  1 
ATOM   4184 N N   . TRP C 1 59  ? 11.724  -16.022 46.611  1.00 24.04 ? 59  TRP C N   1 
ATOM   4185 C CA  . TRP C 1 59  ? 12.603  -16.841 47.444  1.00 27.16 ? 59  TRP C CA  1 
ATOM   4186 C C   . TRP C 1 59  ? 14.080  -16.552 47.150  1.00 25.07 ? 59  TRP C C   1 
ATOM   4187 O O   . TRP C 1 59  ? 14.888  -16.370 48.063  1.00 26.61 ? 59  TRP C O   1 
ATOM   4188 C CB  . TRP C 1 59  ? 12.290  -18.307 47.207  1.00 24.56 ? 59  TRP C CB  1 
ATOM   4189 C CG  . TRP C 1 59  ? 12.579  -19.255 48.370  1.00 29.11 ? 59  TRP C CG  1 
ATOM   4190 C CD1 . TRP C 1 59  ? 13.354  -19.026 49.463  1.00 30.93 ? 59  TRP C CD1 1 
ATOM   4191 C CD2 . TRP C 1 59  ? 12.060  -20.591 48.515  1.00 23.84 ? 59  TRP C CD2 1 
ATOM   4192 N NE1 . TRP C 1 59  ? 13.335  -20.137 50.294  1.00 28.86 ? 59  TRP C NE1 1 
ATOM   4193 C CE2 . TRP C 1 59  ? 12.537  -21.098 49.736  1.00 25.75 ? 59  TRP C CE2 1 
ATOM   4194 C CE3 . TRP C 1 59  ? 11.250  -21.393 47.724  1.00 25.05 ? 59  TRP C CE3 1 
ATOM   4195 C CZ2 . TRP C 1 59  ? 12.243  -22.389 50.188  1.00 29.22 ? 59  TRP C CZ2 1 
ATOM   4196 C CZ3 . TRP C 1 59  ? 10.935  -22.682 48.179  1.00 28.06 ? 59  TRP C CZ3 1 
ATOM   4197 C CH2 . TRP C 1 59  ? 11.442  -23.165 49.398  1.00 28.51 ? 59  TRP C CH2 1 
ATOM   4198 N N   . ILE C 1 60  ? 14.449  -16.476 45.882  1.00 25.13 ? 60  ILE C N   1 
ATOM   4199 C CA  . ILE C 1 60  ? 15.873  -16.255 45.570  1.00 25.60 ? 60  ILE C CA  1 
ATOM   4200 C C   . ILE C 1 60  ? 16.288  -14.831 45.904  1.00 26.61 ? 60  ILE C C   1 
ATOM   4201 O O   . ILE C 1 60  ? 17.334  -14.609 46.521  1.00 23.02 ? 60  ILE C O   1 
ATOM   4202 C CB  . ILE C 1 60  ? 16.170  -16.577 44.097  1.00 24.60 ? 60  ILE C CB  1 
ATOM   4203 C CG1 . ILE C 1 60  ? 16.119  -18.095 43.875  1.00 20.88 ? 60  ILE C CG1 1 
ATOM   4204 C CG2 . ILE C 1 60  ? 17.545  -15.934 43.635  1.00 26.98 ? 60  ILE C CG2 1 
ATOM   4205 C CD1 . ILE C 1 60  ? 15.557  -18.434 42.492  1.00 22.65 ? 60  ILE C CD1 1 
ATOM   4206 N N   . LYS C 1 61  ? 15.440  -13.849 45.567  1.00 26.56 ? 61  LYS C N   1 
ATOM   4207 C CA  . LYS C 1 61  ? 15.807  -12.459 45.802  1.00 27.77 ? 61  LYS C CA  1 
ATOM   4208 C C   . LYS C 1 61  ? 15.794  -12.108 47.294  1.00 27.91 ? 61  LYS C C   1 
ATOM   4209 O O   . LYS C 1 61  ? 16.659  -11.366 47.773  1.00 26.31 ? 61  LYS C O   1 
ATOM   4210 C CB  . LYS C 1 61  ? 14.885  -11.556 44.987  1.00 25.41 ? 61  LYS C CB  1 
ATOM   4211 C CG  . LYS C 1 61  ? 14.808  -10.075 45.451  1.00 30.92 ? 61  LYS C CG  1 
ATOM   4212 C CD  . LYS C 1 61  ? 15.774  -9.234  44.648  1.00 32.31 ? 61  LYS C CD  1 
ATOM   4213 C CE  . LYS C 1 61  ? 16.027  -7.879  45.294  1.00 34.02 ? 61  LYS C CE  1 
ATOM   4214 N NZ  . LYS C 1 61  ? 17.514  -7.560  45.106  1.00 34.39 ? 61  LYS C NZ  1 
ATOM   4215 N N   . ASN C 1 62  ? 14.861  -12.657 48.060  1.00 27.53 ? 62  ASN C N   1 
ATOM   4216 C CA  . ASN C 1 62  ? 14.728  -12.266 49.463  1.00 29.28 ? 62  ASN C CA  1 
ATOM   4217 C C   . ASN C 1 62  ? 15.334  -13.277 50.419  1.00 32.31 ? 62  ASN C C   1 
ATOM   4218 O O   . ASN C 1 62  ? 15.579  -12.941 51.586  1.00 33.55 ? 62  ASN C O   1 
ATOM   4219 C CB  . ASN C 1 62  ? 13.242  -12.049 49.828  1.00 30.12 ? 62  ASN C CB  1 
ATOM   4220 C CG  . ASN C 1 62  ? 12.642  -10.863 49.099  1.00 31.86 ? 62  ASN C CG  1 
ATOM   4221 O OD1 . ASN C 1 62  ? 12.966  -9.729  49.416  1.00 33.80 ? 62  ASN C OD1 1 
ATOM   4222 N ND2 . ASN C 1 62  ? 11.788  -11.111 48.133  1.00 29.15 ? 62  ASN C ND2 1 
ATOM   4223 N N   . GLY C 1 63  ? 15.599  -14.491 49.951  1.00 31.32 ? 63  GLY C N   1 
ATOM   4224 C CA  . GLY C 1 63  ? 16.176  -15.518 50.798  1.00 34.68 ? 63  GLY C CA  1 
ATOM   4225 C C   . GLY C 1 63  ? 15.240  -16.186 51.784  1.00 37.58 ? 63  GLY C C   1 
ATOM   4226 O O   . GLY C 1 63  ? 15.721  -16.966 52.606  1.00 42.78 ? 63  GLY C O   1 
ATOM   4227 N N   . ARG C 1 64  ? 13.964  -15.893 51.689  1.00 35.82 ? 64  ARG C N   1 
ATOM   4228 C CA  . ARG C 1 64  ? 12.964  -16.559 52.539  1.00 36.76 ? 64  ARG C CA  1 
ATOM   4229 C C   . ARG C 1 64  ? 11.789  -16.919 51.643  1.00 35.26 ? 64  ARG C C   1 
ATOM   4230 O O   . ARG C 1 64  ? 11.590  -16.280 50.636  1.00 32.33 ? 64  ARG C O   1 
ATOM   4231 C CB  . ARG C 1 64  ? 12.554  -15.706 53.739  1.00 41.09 ? 64  ARG C CB  1 
ATOM   4232 C CG  . ARG C 1 64  ? 12.609  -14.209 53.489  1.00 48.10 ? 64  ARG C CG  1 
ATOM   4233 C CD  . ARG C 1 64  ? 12.845  -13.411 54.754  1.00 50.00 ? 64  ARG C CD  1 
ATOM   4234 N NE  . ARG C 1 64  ? 14.104  -12.691 54.696  1.00 56.34 ? 64  ARG C NE  1 
ATOM   4235 C CZ  . ARG C 1 64  ? 15.274  -13.176 55.088  1.00 60.01 ? 64  ARG C CZ  1 
ATOM   4236 N NH1 . ARG C 1 64  ? 16.361  -12.432 54.972  1.00 58.52 ? 64  ARG C NH1 1 
ATOM   4237 N NH2 . ARG C 1 64  ? 15.354  -14.400 55.582  1.00 62.03 ? 64  ARG C NH2 1 
ATOM   4238 N N   . GLU C 1 65  ? 11.055  -17.950 52.013  1.00 34.38 ? 65  GLU C N   1 
ATOM   4239 C CA  . GLU C 1 65  ? 9.916   -18.332 51.210  1.00 33.10 ? 65  GLU C CA  1 
ATOM   4240 C C   . GLU C 1 65  ? 8.844   -17.232 51.253  1.00 31.85 ? 65  GLU C C   1 
ATOM   4241 O O   . GLU C 1 65  ? 8.666   -16.583 52.279  1.00 32.84 ? 65  GLU C O   1 
ATOM   4242 C CB  . GLU C 1 65  ? 9.362   -19.624 51.774  1.00 33.19 ? 65  GLU C CB  1 
ATOM   4243 C CG  . GLU C 1 65  ? 9.010   -20.614 50.764  1.00 35.75 ? 65  GLU C CG  1 
ATOM   4244 C CD  . GLU C 1 65  ? 8.291   -21.747 51.417  1.00 32.09 ? 65  GLU C CD  1 
ATOM   4245 O OE1 . GLU C 1 65  ? 8.844   -22.248 52.409  1.00 34.79 ? 65  GLU C OE1 1 
ATOM   4246 O OE2 . GLU C 1 65  ? 7.224   -22.120 50.934  1.00 37.02 ? 65  GLU C OE2 1 
ATOM   4247 N N   . PRO C 1 66  ? 8.123   -16.985 50.153  1.00 31.63 ? 66  PRO C N   1 
ATOM   4248 C CA  . PRO C 1 66  ? 6.990   -16.043 50.213  1.00 34.72 ? 66  PRO C CA  1 
ATOM   4249 C C   . PRO C 1 66  ? 5.808   -16.635 50.984  1.00 35.91 ? 66  PRO C C   1 
ATOM   4250 O O   . PRO C 1 66  ? 5.496   -17.823 50.868  1.00 37.04 ? 66  PRO C O   1 
ATOM   4251 C CB  . PRO C 1 66  ? 6.635   -15.814 48.736  1.00 32.00 ? 66  PRO C CB  1 
ATOM   4252 C CG  . PRO C 1 66  ? 7.137   -17.060 48.028  1.00 26.53 ? 66  PRO C CG  1 
ATOM   4253 C CD  . PRO C 1 66  ? 8.350   -17.495 48.785  1.00 28.80 ? 66  PRO C CD  1 
ATOM   4254 N N   . ASN C 1 67  ? 5.189   -15.810 51.837  1.00 38.38 ? 67  ASN C N   1 
ATOM   4255 C CA  . ASN C 1 67  ? 4.019   -16.287 52.593  1.00 38.81 ? 67  ASN C CA  1 
ATOM   4256 C C   . ASN C 1 67  ? 2.802   -16.554 51.706  1.00 38.05 ? 67  ASN C C   1 
ATOM   4257 O O   . ASN C 1 67  ? 1.936   -17.358 52.081  1.00 39.24 ? 67  ASN C O   1 
ATOM   4258 C CB  . ASN C 1 67  ? 3.652   -15.297 53.698  1.00 39.56 ? 67  ASN C CB  1 
ATOM   4259 C CG  . ASN C 1 67  ? 3.880   -13.844 53.280  1.00 47.23 ? 67  ASN C CG  1 
ATOM   4260 O OD1 . ASN C 1 67  ? 3.255   -13.341 52.341  1.00 46.43 ? 67  ASN C OD1 1 
ATOM   4261 N ND2 . ASN C 1 67  ? 4.798   -13.167 53.966  1.00 51.58 ? 67  ASN C ND2 1 
ATOM   4262 N N   . TYR C 1 68  ? 2.735   -15.944 50.526  1.00 36.77 ? 68  TYR C N   1 
ATOM   4263 C CA  . TYR C 1 68  ? 1.708   -16.271 49.544  1.00 34.05 ? 68  TYR C CA  1 
ATOM   4264 C C   . TYR C 1 68  ? 2.163   -15.765 48.188  1.00 33.45 ? 68  TYR C C   1 
ATOM   4265 O O   . TYR C 1 68  ? 2.987   -14.857 48.096  1.00 32.35 ? 68  TYR C O   1 
ATOM   4266 C CB  . TYR C 1 68  ? 0.349   -15.648 49.923  1.00 36.21 ? 68  TYR C CB  1 
ATOM   4267 C CG  . TYR C 1 68  ? 0.202   -14.162 49.636  1.00 34.32 ? 68  TYR C CG  1 
ATOM   4268 C CD1 . TYR C 1 68  ? -0.161  -13.706 48.375  1.00 38.35 ? 68  TYR C CD1 1 
ATOM   4269 C CD2 . TYR C 1 68  ? 0.383   -13.216 50.638  1.00 38.19 ? 68  TYR C CD2 1 
ATOM   4270 C CE1 . TYR C 1 68  ? -0.292  -12.350 48.099  1.00 36.46 ? 68  TYR C CE1 1 
ATOM   4271 C CE2 . TYR C 1 68  ? 0.241   -11.857 50.377  1.00 38.37 ? 68  TYR C CE2 1 
ATOM   4272 C CZ  . TYR C 1 68  ? -0.104  -11.434 49.103  1.00 39.89 ? 68  TYR C CZ  1 
ATOM   4273 O OH  . TYR C 1 68  ? -0.263  -10.082 48.827  1.00 46.45 ? 68  TYR C OH  1 
ATOM   4274 N N   . VAL C 1 69  ? 1.622   -16.364 47.135  1.00 32.06 ? 69  VAL C N   1 
ATOM   4275 C CA  . VAL C 1 69  ? 1.911   -15.945 45.765  1.00 31.88 ? 69  VAL C CA  1 
ATOM   4276 C C   . VAL C 1 69  ? 0.599   -15.857 45.012  1.00 31.33 ? 69  VAL C C   1 
ATOM   4277 O O   . VAL C 1 69  ? -0.237  -16.761 45.136  1.00 31.91 ? 69  VAL C O   1 
ATOM   4278 C CB  . VAL C 1 69  ? 2.877   -16.906 45.042  1.00 28.77 ? 69  VAL C CB  1 
ATOM   4279 C CG1 . VAL C 1 69  ? 3.019   -16.493 43.591  1.00 26.84 ? 69  VAL C CG1 1 
ATOM   4280 C CG2 . VAL C 1 69  ? 4.221   -16.869 45.733  1.00 28.08 ? 69  VAL C CG2 1 
ATOM   4281 N N   . THR C 1 70  ? 0.418   -14.765 44.250  1.00 27.31 ? 70  THR C N   1 
ATOM   4282 C CA  . THR C 1 70  ? -0.746  -14.577 43.402  1.00 31.96 ? 70  THR C CA  1 
ATOM   4283 C C   . THR C 1 70  ? -0.418  -15.099 42.015  1.00 33.13 ? 70  THR C C   1 
ATOM   4284 O O   . THR C 1 70  ? 0.661   -14.832 41.488  1.00 32.75 ? 70  THR C O   1 
ATOM   4285 C CB  . THR C 1 70  ? -1.115  -13.083 43.321  1.00 35.56 ? 70  THR C CB  1 
ATOM   4286 O OG1 . THR C 1 70  ? -1.363  -12.573 44.638  1.00 33.25 ? 70  THR C OG1 1 
ATOM   4287 C CG2 . THR C 1 70  ? -2.313  -12.851 42.413  1.00 32.91 ? 70  THR C CG2 1 
ATOM   4288 N N   . LEU C 1 71  ? -1.342  -15.850 41.429  1.00 30.10 ? 71  LEU C N   1 
ATOM   4289 C CA  . LEU C 1 71  ? -1.171  -16.306 40.054  1.00 31.78 ? 71  LEU C CA  1 
ATOM   4290 C C   . LEU C 1 71  ? -1.387  -15.115 39.140  1.00 35.41 ? 71  LEU C C   1 
ATOM   4291 O O   . LEU C 1 71  ? -2.521  -14.618 39.020  1.00 36.41 ? 71  LEU C O   1 
ATOM   4292 C CB  . LEU C 1 71  ? -2.146  -17.442 39.729  1.00 32.51 ? 71  LEU C CB  1 
ATOM   4293 C CG  . LEU C 1 71  ? -1.987  -18.212 38.403  1.00 36.54 ? 71  LEU C CG  1 
ATOM   4294 C CD1 . LEU C 1 71  ? -2.357  -17.393 37.148  1.00 39.91 ? 71  LEU C CD1 1 
ATOM   4295 C CD2 . LEU C 1 71  ? -0.541  -18.663 38.249  1.00 36.16 ? 71  LEU C CD2 1 
ATOM   4296 N N   . THR C 1 72  ? -0.292  -14.629 38.530  1.00 32.80 ? 72  THR C N   1 
ATOM   4297 C CA  . THR C 1 72  ? -0.332  -13.457 37.671  1.00 35.07 ? 72  THR C CA  1 
ATOM   4298 C C   . THR C 1 72  ? 0.172   -13.719 36.270  1.00 37.22 ? 72  THR C C   1 
ATOM   4299 O O   . THR C 1 72  ? -0.108  -12.909 35.374  1.00 36.23 ? 72  THR C O   1 
ATOM   4300 C CB  . THR C 1 72  ? 0.523   -12.319 38.248  1.00 36.83 ? 72  THR C CB  1 
ATOM   4301 O OG1 . THR C 1 72  ? 1.877   -12.789 38.356  1.00 36.73 ? 72  THR C OG1 1 
ATOM   4302 C CG2 . THR C 1 72  ? -0.004  -11.866 39.611  1.00 33.43 ? 72  THR C CG2 1 
ATOM   4303 N N   . SER C 1 73  ? 0.922   -14.791 36.053  1.00 31.16 ? 73  SER C N   1 
ATOM   4304 C CA  . SER C 1 73  ? 1.646   -14.972 34.797  1.00 37.18 ? 73  SER C CA  1 
ATOM   4305 C C   . SER C 1 73  ? 1.742   -16.453 34.471  1.00 35.04 ? 73  SER C C   1 
ATOM   4306 O O   . SER C 1 73  ? 1.420   -17.307 35.291  1.00 34.43 ? 73  SER C O   1 
ATOM   4307 C CB  . SER C 1 73  ? 3.047   -14.327 34.860  1.00 35.82 ? 73  SER C CB  1 
ATOM   4308 O OG  . SER C 1 73  ? 3.761   -14.788 35.981  1.00 35.20 ? 73  SER C OG  1 
ATOM   4309 N N   . VAL C 1 74  ? 2.181   -16.745 33.254  1.00 31.79 ? 74  VAL C N   1 
ATOM   4310 C CA  . VAL C 1 74  ? 2.445   -18.104 32.823  1.00 29.42 ? 74  VAL C CA  1 
ATOM   4311 C C   . VAL C 1 74  ? 3.911   -18.199 32.374  1.00 34.71 ? 74  VAL C C   1 
ATOM   4312 O O   . VAL C 1 74  ? 4.572   -17.195 32.101  1.00 30.21 ? 74  VAL C O   1 
ATOM   4313 C CB  . VAL C 1 74  ? 1.477   -18.532 31.709  1.00 34.32 ? 74  VAL C CB  1 
ATOM   4314 C CG1 . VAL C 1 74  ? 0.027   -18.684 32.318  1.00 36.34 ? 74  VAL C CG1 1 
ATOM   4315 C CG2 . VAL C 1 74  ? 1.496   -17.544 30.580  1.00 31.31 ? 74  VAL C CG2 1 
ATOM   4316 N N   . ALA C 1 75  ? 4.410   -19.432 32.276  1.00 33.91 ? 75  ALA C N   1 
ATOM   4317 C CA  . ALA C 1 75  ? 5.809   -19.650 31.954  1.00 31.80 ? 75  ALA C CA  1 
ATOM   4318 C C   . ALA C 1 75  ? 5.981   -21.061 31.419  1.00 33.54 ? 75  ALA C C   1 
ATOM   4319 O O   . ALA C 1 75  ? 5.134   -21.938 31.622  1.00 32.28 ? 75  ALA C O   1 
ATOM   4320 C CB  . ALA C 1 75  ? 6.706   -19.432 33.169  1.00 29.56 ? 75  ALA C CB  1 
ATOM   4321 N N   . ARG C 1 76  ? 7.088   -21.266 30.727  1.00 34.97 ? 76  ARG C N   1 
ATOM   4322 C CA  . ARG C 1 76  ? 7.379   -22.573 30.163  1.00 36.07 ? 76  ARG C CA  1 
ATOM   4323 C C   . ARG C 1 76  ? 8.000   -23.508 31.188  1.00 34.46 ? 76  ARG C C   1 
ATOM   4324 O O   . ARG C 1 76  ? 7.830   -24.727 31.073  1.00 33.34 ? 76  ARG C O   1 
ATOM   4325 C CB  . ARG C 1 76  ? 8.330   -22.409 28.970  1.00 36.44 ? 76  ARG C CB  1 
ATOM   4326 C CG  . ARG C 1 76  ? 7.751   -21.568 27.802  1.00 40.21 ? 76  ARG C CG  1 
ATOM   4327 C CD  . ARG C 1 76  ? 7.692   -20.006 28.067  1.00 47.33 ? 76  ARG C CD  1 
ATOM   4328 N NE  . ARG C 1 76  ? 8.786   -19.546 28.918  1.00 47.46 ? 76  ARG C NE  1 
ATOM   4329 C CZ  . ARG C 1 76  ? 8.740   -18.511 29.737  1.00 40.61 ? 76  ARG C CZ  1 
ATOM   4330 N NH1 . ARG C 1 76  ? 7.641   -17.773 29.876  1.00 45.15 ? 76  ARG C NH1 1 
ATOM   4331 N NH2 . ARG C 1 76  ? 9.800   -18.241 30.485  1.00 37.72 ? 76  ARG C NH2 1 
ATOM   4332 N N   . ASN C 1 77  ? 8.586   -22.959 32.245  1.00 31.83 ? 77  ASN C N   1 
ATOM   4333 C CA  . ASN C 1 77  ? 9.159   -23.720 33.350  1.00 28.87 ? 77  ASN C CA  1 
ATOM   4334 C C   . ASN C 1 77  ? 9.268   -22.763 34.523  1.00 23.36 ? 77  ASN C C   1 
ATOM   4335 O O   . ASN C 1 77  ? 9.107   -21.554 34.339  1.00 25.27 ? 77  ASN C O   1 
ATOM   4336 C CB  . ASN C 1 77  ? 10.539  -24.330 32.966  1.00 28.13 ? 77  ASN C CB  1 
ATOM   4337 C CG  . ASN C 1 77  ? 11.563  -23.281 32.616  1.00 26.87 ? 77  ASN C CG  1 
ATOM   4338 O OD1 . ASN C 1 77  ? 11.812  -22.348 33.380  1.00 24.18 ? 77  ASN C OD1 1 
ATOM   4339 N ND2 . ASN C 1 77  ? 12.172  -23.427 31.445  1.00 32.76 ? 77  ASN C ND2 1 
ATOM   4340 N N   . PRO C 1 78  ? 9.552   -23.269 35.767  1.00 22.86 ? 78  PRO C N   1 
ATOM   4341 C CA  . PRO C 1 78  ? 9.685   -22.347 36.912  1.00 24.90 ? 78  PRO C CA  1 
ATOM   4342 C C   . PRO C 1 78  ? 11.112  -21.784 37.141  1.00 25.90 ? 78  PRO C C   1 
ATOM   4343 O O   . PRO C 1 78  ? 11.384  -21.220 38.205  1.00 24.22 ? 78  PRO C O   1 
ATOM   4344 C CB  . PRO C 1 78  ? 9.293   -23.225 38.103  1.00 24.15 ? 78  PRO C CB  1 
ATOM   4345 C CG  . PRO C 1 78  ? 9.704   -24.623 37.685  1.00 25.88 ? 78  PRO C CG  1 
ATOM   4346 C CD  . PRO C 1 78  ? 9.775   -24.678 36.170  1.00 25.68 ? 78  PRO C CD  1 
ATOM   4347 N N   . LEU C 1 79  ? 12.009  -21.907 36.170  1.00 22.46 ? 79  LEU C N   1 
ATOM   4348 C CA  . LEU C 1 79  ? 13.413  -21.543 36.370  1.00 23.68 ? 79  LEU C CA  1 
ATOM   4349 C C   . LEU C 1 79  ? 13.633  -20.024 36.453  1.00 22.94 ? 79  LEU C C   1 
ATOM   4350 O O   . LEU C 1 79  ? 13.181  -19.251 35.586  1.00 22.65 ? 79  LEU C O   1 
ATOM   4351 C CB  . LEU C 1 79  ? 14.253  -22.130 35.237  1.00 21.72 ? 79  LEU C CB  1 
ATOM   4352 C CG  . LEU C 1 79  ? 15.767  -21.874 35.369  1.00 24.29 ? 79  LEU C CG  1 
ATOM   4353 C CD1 . LEU C 1 79  ? 16.319  -22.577 36.631  1.00 21.16 ? 79  LEU C CD1 1 
ATOM   4354 C CD2 . LEU C 1 79  ? 16.453  -22.358 34.095  1.00 25.04 ? 79  LEU C CD2 1 
ATOM   4355 N N   . VAL C 1 80  ? 14.352  -19.598 37.497  1.00 20.99 ? 80  VAL C N   1 
ATOM   4356 C CA  . VAL C 1 80  ? 14.734  -18.195 37.701  1.00 25.79 ? 80  VAL C CA  1 
ATOM   4357 C C   . VAL C 1 80  ? 16.254  -18.088 37.755  1.00 20.27 ? 80  VAL C C   1 
ATOM   4358 O O   . VAL C 1 80  ? 16.897  -18.733 38.600  1.00 20.11 ? 80  VAL C O   1 
ATOM   4359 C CB  . VAL C 1 80  ? 14.102  -17.635 38.991  1.00 23.88 ? 80  VAL C CB  1 
ATOM   4360 C CG1 . VAL C 1 80  ? 14.602  -16.187 39.271  1.00 23.35 ? 80  VAL C CG1 1 
ATOM   4361 C CG2 . VAL C 1 80  ? 12.531  -17.742 38.934  1.00 20.95 ? 80  VAL C CG2 1 
ATOM   4362 N N   . MET C 1 81  ? 16.834  -17.258 36.894  1.00 22.42 ? 81  MET C N   1 
ATOM   4363 C CA  . MET C 1 81  ? 18.295  -17.137 36.901  1.00 21.30 ? 81  MET C CA  1 
ATOM   4364 C C   . MET C 1 81  ? 18.782  -16.800 38.310  1.00 24.05 ? 81  MET C C   1 
ATOM   4365 O O   . MET C 1 81  ? 18.282  -15.875 38.965  1.00 25.45 ? 81  MET C O   1 
ATOM   4366 C CB  . MET C 1 81  ? 18.772  -16.066 35.924  1.00 24.03 ? 81  MET C CB  1 
ATOM   4367 C CG  . MET C 1 81  ? 20.270  -16.123 35.546  1.00 28.39 ? 81  MET C CG  1 
ATOM   4368 S SD  . MET C 1 81  ? 21.037  -17.719 35.427  1.00 26.77 ? 81  MET C SD  1 
ATOM   4369 C CE  . MET C 1 81  ? 22.781  -17.314 35.631  1.00 29.46 ? 81  MET C CE  1 
ATOM   4370 N N   . ASP C 1 82  ? 19.748  -17.573 38.766  1.00 21.20 ? 82  ASP C N   1 
ATOM   4371 C CA  . ASP C 1 82  ? 20.382  -17.426 40.063  1.00 24.27 ? 82  ASP C CA  1 
ATOM   4372 C C   . ASP C 1 82  ? 21.895  -17.471 39.818  1.00 27.23 ? 82  ASP C C   1 
ATOM   4373 O O   . ASP C 1 82  ? 22.416  -18.477 39.325  1.00 29.86 ? 82  ASP C O   1 
ATOM   4374 C CB  . ASP C 1 82  ? 19.936  -18.550 40.989  1.00 21.46 ? 82  ASP C CB  1 
ATOM   4375 C CG  . ASP C 1 82  ? 20.444  -18.374 42.400  1.00 25.69 ? 82  ASP C CG  1 
ATOM   4376 O OD1 . ASP C 1 82  ? 20.837  -17.247 42.745  1.00 24.72 ? 82  ASP C OD1 1 
ATOM   4377 O OD2 . ASP C 1 82  ? 20.452  -19.355 43.181  1.00 28.37 ? 82  ASP C OD2 1 
ATOM   4378 N N   . TYR C 1 83  ? 22.602  -16.414 40.198  1.00 25.79 ? 83  TYR C N   1 
ATOM   4379 C CA  . TYR C 1 83  ? 24.025  -16.295 39.913  1.00 28.38 ? 83  TYR C CA  1 
ATOM   4380 C C   . TYR C 1 83  ? 24.785  -16.782 41.120  1.00 25.89 ? 83  TYR C C   1 
ATOM   4381 O O   . TYR C 1 83  ? 24.302  -16.667 42.247  1.00 27.90 ? 83  TYR C O   1 
ATOM   4382 C CB  . TYR C 1 83  ? 24.428  -14.825 39.611  1.00 25.77 ? 83  TYR C CB  1 
ATOM   4383 C CG  . TYR C 1 83  ? 23.746  -14.214 38.397  1.00 27.10 ? 83  TYR C CG  1 
ATOM   4384 C CD1 . TYR C 1 83  ? 22.534  -13.551 38.514  1.00 27.98 ? 83  TYR C CD1 1 
ATOM   4385 C CD2 . TYR C 1 83  ? 24.309  -14.294 37.144  1.00 28.71 ? 83  TYR C CD2 1 
ATOM   4386 C CE1 . TYR C 1 83  ? 21.887  -12.997 37.428  1.00 26.87 ? 83  TYR C CE1 1 
ATOM   4387 C CE2 . TYR C 1 83  ? 23.646  -13.725 36.022  1.00 30.16 ? 83  TYR C CE2 1 
ATOM   4388 C CZ  . TYR C 1 83  ? 22.434  -13.073 36.190  1.00 29.40 ? 83  TYR C CZ  1 
ATOM   4389 O OH  . TYR C 1 83  ? 21.753  -12.470 35.106  1.00 33.12 ? 83  TYR C OH  1 
ATOM   4390 N N   . GLN C 1 84  ? 25.999  -17.290 40.889  1.00 25.43 ? 84  GLN C N   1 
ATOM   4391 C CA  . GLN C 1 84  ? 26.805  -17.747 42.007  1.00 27.16 ? 84  GLN C CA  1 
ATOM   4392 C C   . GLN C 1 84  ? 27.285  -16.541 42.817  1.00 27.44 ? 84  GLN C C   1 
ATOM   4393 O O   . GLN C 1 84  ? 27.634  -15.501 42.257  1.00 26.62 ? 84  GLN C O   1 
ATOM   4394 C CB  . GLN C 1 84  ? 27.987  -18.601 41.504  1.00 27.48 ? 84  GLN C CB  1 
ATOM   4395 C CG  . GLN C 1 84  ? 29.073  -17.848 40.759  1.00 21.41 ? 84  GLN C CG  1 
ATOM   4396 C CD  . GLN C 1 84  ? 30.067  -18.772 40.006  1.00 28.26 ? 84  GLN C CD  1 
ATOM   4397 O OE1 . GLN C 1 84  ? 29.764  -19.338 38.933  1.00 24.22 ? 84  GLN C OE1 1 
ATOM   4398 N NE2 . GLN C 1 84  ? 31.258  -18.934 40.583  1.00 28.64 ? 84  GLN C NE2 1 
ATOM   4399 N N   . ASN C 1 85  ? 27.254  -16.668 44.146  1.00 29.74 ? 85  ASN C N   1 
ATOM   4400 C CA  . ASN C 1 85  ? 27.595  -15.557 45.032  1.00 30.37 ? 85  ASN C CA  1 
ATOM   4401 C C   . ASN C 1 85  ? 29.108  -15.424 45.259  1.00 31.15 ? 85  ASN C C   1 
ATOM   4402 O O   . ASN C 1 85  ? 29.555  -14.384 45.758  1.00 28.17 ? 85  ASN C O   1 
ATOM   4403 C CB  . ASN C 1 85  ? 26.880  -15.722 46.384  1.00 27.66 ? 85  ASN C CB  1 
ATOM   4404 C CG  . ASN C 1 85  ? 25.309  -15.687 46.270  1.00 33.88 ? 85  ASN C CG  1 
ATOM   4405 O OD1 . ASN C 1 85  ? 24.722  -15.264 45.249  1.00 33.96 ? 85  ASN C OD1 1 
ATOM   4406 N ND2 . ASN C 1 85  ? 24.638  -16.126 47.342  1.00 34.60 ? 85  ASN C ND2 1 
ATOM   4407 N N   . THR C 1 86  ? 29.901  -16.445 44.908  1.00 31.02 ? 86  THR C N   1 
ATOM   4408 C CA  . THR C 1 86  ? 31.359  -16.441 45.063  1.00 32.67 ? 86  THR C CA  1 
ATOM   4409 C C   . THR C 1 86  ? 32.001  -16.955 43.789  1.00 28.67 ? 86  THR C C   1 
ATOM   4410 O O   . THR C 1 86  ? 31.339  -17.535 42.932  1.00 28.33 ? 86  THR C O   1 
ATOM   4411 C CB  . THR C 1 86  ? 31.821  -17.340 46.223  1.00 34.07 ? 86  THR C CB  1 
ATOM   4412 O OG1 . THR C 1 86  ? 31.830  -18.688 45.762  1.00 32.98 ? 86  THR C OG1 1 
ATOM   4413 C CG2 . THR C 1 86  ? 30.892  -17.263 47.407  1.00 35.05 ? 86  THR C CG2 1 
ATOM   4414 N N   . ASN C 1 87  ? 33.324  -16.822 43.668  1.00 31.06 ? 87  ASN C N   1 
ATOM   4415 C CA  . ASN C 1 87  ? 33.942  -17.382 42.471  1.00 27.79 ? 87  ASN C CA  1 
ATOM   4416 C C   . ASN C 1 87  ? 34.206  -18.892 42.575  1.00 29.63 ? 87  ASN C C   1 
ATOM   4417 O O   . ASN C 1 87  ? 34.840  -19.477 41.692  1.00 28.24 ? 87  ASN C O   1 
ATOM   4418 C CB  . ASN C 1 87  ? 35.241  -16.643 42.121  1.00 34.02 ? 87  ASN C CB  1 
ATOM   4419 C CG  . ASN C 1 87  ? 36.345  -16.852 43.155  1.00 34.24 ? 87  ASN C CG  1 
ATOM   4420 O OD1 . ASN C 1 87  ? 36.204  -17.618 44.108  1.00 37.74 ? 87  ASN C OD1 1 
ATOM   4421 N ND2 . ASN C 1 87  ? 37.458  -16.157 42.960  1.00 39.88 ? 87  ASN C ND2 1 
ATOM   4422 N N   . TYR C 1 88  ? 33.724  -19.560 43.612  1.00 33.19 ? 88  TYR C N   1 
ATOM   4423 C CA  . TYR C 1 88  ? 33.966  -20.996 43.750  1.00 31.99 ? 88  TYR C CA  1 
ATOM   4424 C C   . TYR C 1 88  ? 32.693  -21.809 44.003  1.00 30.97 ? 88  TYR C C   1 
ATOM   4425 O O   . TYR C 1 88  ? 32.794  -23.007 44.277  1.00 30.57 ? 88  TYR C O   1 
ATOM   4426 C CB  . TYR C 1 88  ? 34.972  -21.265 44.881  1.00 30.47 ? 88  TYR C CB  1 
ATOM   4427 C CG  . TYR C 1 88  ? 34.547  -20.764 46.234  1.00 32.16 ? 88  TYR C CG  1 
ATOM   4428 C CD1 . TYR C 1 88  ? 34.815  -19.449 46.637  1.00 33.31 ? 88  TYR C CD1 1 
ATOM   4429 C CD2 . TYR C 1 88  ? 33.865  -21.578 47.102  1.00 32.11 ? 88  TYR C CD2 1 
ATOM   4430 C CE1 . TYR C 1 88  ? 34.455  -18.990 47.886  1.00 30.88 ? 88  TYR C CE1 1 
ATOM   4431 C CE2 . TYR C 1 88  ? 33.458  -21.111 48.357  1.00 34.21 ? 88  TYR C CE2 1 
ATOM   4432 C CZ  . TYR C 1 88  ? 33.757  -19.811 48.732  1.00 33.39 ? 88  TYR C CZ  1 
ATOM   4433 O OH  . TYR C 1 88  ? 33.334  -19.359 49.970  1.00 32.34 ? 88  TYR C OH  1 
ATOM   4434 N N   . THR C 1 89  ? 31.509  -21.208 43.923  1.00 24.73 ? 89  THR C N   1 
ATOM   4435 C CA  . THR C 1 89  ? 30.251  -21.905 44.194  1.00 27.76 ? 89  THR C CA  1 
ATOM   4436 C C   . THR C 1 89  ? 29.455  -22.205 42.916  1.00 25.44 ? 89  THR C C   1 
ATOM   4437 O O   . THR C 1 89  ? 28.235  -22.390 42.950  1.00 25.21 ? 89  THR C O   1 
ATOM   4438 C CB  . THR C 1 89  ? 29.379  -21.119 45.175  1.00 27.51 ? 89  THR C CB  1 
ATOM   4439 O OG1 . THR C 1 89  ? 29.403  -19.702 44.885  1.00 25.15 ? 89  THR C OG1 1 
ATOM   4440 C CG2 . THR C 1 89  ? 29.875  -21.347 46.596  1.00 30.97 ? 89  THR C CG2 1 
ATOM   4441 N N   . CYS C 1 90  ? 30.134  -22.325 41.782  1.00 22.03 ? 90  CYS C N   1 
ATOM   4442 C CA  . CYS C 1 90  ? 29.413  -22.661 40.560  1.00 24.72 ? 90  CYS C CA  1 
ATOM   4443 C C   . CYS C 1 90  ? 28.650  -24.003 40.678  1.00 25.61 ? 90  CYS C C   1 
ATOM   4444 O O   . CYS C 1 90  ? 27.504  -24.111 40.221  1.00 23.98 ? 90  CYS C O   1 
ATOM   4445 C CB  . CYS C 1 90  ? 30.391  -22.703 39.383  1.00 28.57 ? 90  CYS C CB  1 
ATOM   4446 S SG  . CYS C 1 90  ? 31.985  -23.492 39.646  1.00 30.98 ? 90  CYS C SG  1 
ATOM   4447 N N   . CYS C 1 91  ? 29.253  -25.036 41.313  1.00 24.86 ? 91  CYS C N   1 
ATOM   4448 C CA  . CYS C 1 91  ? 28.591  -26.344 41.347  1.00 24.72 ? 91  CYS C CA  1 
ATOM   4449 C C   . CYS C 1 91  ? 27.323  -26.331 42.197  1.00 23.30 ? 91  CYS C C   1 
ATOM   4450 O O   . CYS C 1 91  ? 26.263  -26.740 41.701  1.00 21.07 ? 91  CYS C O   1 
ATOM   4451 C CB  . CYS C 1 91  ? 29.565  -27.412 41.837  1.00 27.04 ? 91  CYS C CB  1 
ATOM   4452 S SG  . CYS C 1 91  ? 28.888  -29.092 41.726  1.00 26.33 ? 91  CYS C SG  1 
ATOM   4453 N N   . PRO C 1 92  ? 27.345  -25.901 43.458  1.00 25.50 ? 92  PRO C N   1 
ATOM   4454 C CA  . PRO C 1 92  ? 26.088  -25.859 44.200  1.00 24.90 ? 92  PRO C CA  1 
ATOM   4455 C C   . PRO C 1 92  ? 25.087  -24.844 43.623  1.00 26.09 ? 92  PRO C C   1 
ATOM   4456 O O   . PRO C 1 92  ? 23.874  -25.074 43.730  1.00 23.95 ? 92  PRO C O   1 
ATOM   4457 C CB  . PRO C 1 92  ? 26.530  -25.524 45.636  1.00 24.62 ? 92  PRO C CB  1 
ATOM   4458 C CG  . PRO C 1 92  ? 27.855  -24.821 45.471  1.00 27.76 ? 92  PRO C CG  1 
ATOM   4459 C CD  . PRO C 1 92  ? 28.494  -25.381 44.242  1.00 24.14 ? 92  PRO C CD  1 
ATOM   4460 N N   . THR C 1 93  ? 25.531  -23.762 42.972  1.00 21.70 ? 93  THR C N   1 
ATOM   4461 C CA  . THR C 1 93  ? 24.554  -22.897 42.282  1.00 23.40 ? 93  THR C CA  1 
ATOM   4462 C C   . THR C 1 93  ? 23.840  -23.652 41.147  1.00 23.62 ? 93  THR C C   1 
ATOM   4463 O O   . THR C 1 93  ? 22.628  -23.536 40.980  1.00 21.41 ? 93  THR C O   1 
ATOM   4464 C CB  . THR C 1 93  ? 25.222  -21.636 41.704  1.00 24.79 ? 93  THR C CB  1 
ATOM   4465 O OG1 . THR C 1 93  ? 26.042  -21.011 42.700  1.00 23.73 ? 93  THR C OG1 1 
ATOM   4466 C CG2 . THR C 1 93  ? 24.090  -20.598 41.212  1.00 24.93 ? 93  THR C CG2 1 
ATOM   4467 N N   . SER C 1 94  ? 24.573  -24.452 40.380  1.00 20.54 ? 94  SER C N   1 
ATOM   4468 C CA  . SER C 1 94  ? 23.954  -25.270 39.340  1.00 19.25 ? 94  SER C CA  1 
ATOM   4469 C C   . SER C 1 94  ? 23.000  -26.308 39.933  1.00 21.68 ? 94  SER C C   1 
ATOM   4470 O O   . SER C 1 94  ? 21.940  -26.564 39.361  1.00 20.54 ? 94  SER C O   1 
ATOM   4471 C CB  . SER C 1 94  ? 25.033  -25.995 38.512  1.00 24.14 ? 94  SER C CB  1 
ATOM   4472 O OG  . SER C 1 94  ? 25.968  -25.106 37.910  1.00 23.03 ? 94  SER C OG  1 
ATOM   4473 N N   . LEU C 1 95  ? 23.351  -26.910 41.082  1.00 19.04 ? 95  LEU C N   1 
ATOM   4474 C CA  . LEU C 1 95  ? 22.436  -27.861 41.697  1.00 21.47 ? 95  LEU C CA  1 
ATOM   4475 C C   . LEU C 1 95  ? 21.190  -27.154 42.210  1.00 20.75 ? 95  LEU C C   1 
ATOM   4476 O O   . LEU C 1 95  ? 20.093  -27.724 42.176  1.00 21.22 ? 95  LEU C O   1 
ATOM   4477 C CB  . LEU C 1 95  ? 23.138  -28.622 42.824  1.00 22.80 ? 95  LEU C CB  1 
ATOM   4478 C CG  . LEU C 1 95  ? 22.264  -29.699 43.520  1.00 22.80 ? 95  LEU C CG  1 
ATOM   4479 C CD1 . LEU C 1 95  ? 21.687  -30.736 42.526  1.00 20.39 ? 95  LEU C CD1 1 
ATOM   4480 C CD2 . LEU C 1 95  ? 23.048  -30.396 44.626  1.00 25.57 ? 95  LEU C CD2 1 
ATOM   4481 N N   . SER C 1 96  ? 21.356  -25.913 42.708  1.00 22.58 ? 96  SER C N   1 
ATOM   4482 C CA  . SER C 1 96  ? 20.209  -25.108 43.145  1.00 22.74 ? 96  SER C CA  1 
ATOM   4483 C C   . SER C 1 96  ? 19.273  -24.822 41.976  1.00 22.72 ? 96  SER C C   1 
ATOM   4484 O O   . SER C 1 96  ? 18.052  -24.984 42.081  1.00 23.73 ? 96  SER C O   1 
ATOM   4485 C CB  . SER C 1 96  ? 20.682  -23.789 43.782  1.00 23.48 ? 96  SER C CB  1 
ATOM   4486 O OG  . SER C 1 96  ? 19.525  -23.048 44.249  1.00 23.20 ? 96  SER C OG  1 
ATOM   4487 N N   . LEU C 1 97  ? 19.834  -24.425 40.839  1.00 20.23 ? 97  LEU C N   1 
ATOM   4488 C CA  . LEU C 1 97  ? 19.007  -24.236 39.648  1.00 21.57 ? 97  LEU C CA  1 
ATOM   4489 C C   . LEU C 1 97  ? 18.244  -25.525 39.268  1.00 23.81 ? 97  LEU C C   1 
ATOM   4490 O O   . LEU C 1 97  ? 17.051  -25.483 38.930  1.00 20.71 ? 97  LEU C O   1 
ATOM   4491 C CB  . LEU C 1 97  ? 19.898  -23.766 38.498  1.00 19.33 ? 97  LEU C CB  1 
ATOM   4492 C CG  . LEU C 1 97  ? 20.509  -22.353 38.620  1.00 22.34 ? 97  LEU C CG  1 
ATOM   4493 C CD1 . LEU C 1 97  ? 21.657  -22.158 37.655  1.00 19.18 ? 97  LEU C CD1 1 
ATOM   4494 C CD2 . LEU C 1 97  ? 19.417  -21.291 38.367  1.00 17.91 ? 97  LEU C CD2 1 
ATOM   4495 N N   . ALA C 1 98  ? 18.931  -26.677 39.254  1.00 20.66 ? 98  ALA C N   1 
ATOM   4496 C CA  . ALA C 1 98  ? 18.247  -27.954 39.027  1.00 21.28 ? 98  ALA C CA  1 
ATOM   4497 C C   . ALA C 1 98  ? 17.088  -28.165 40.012  1.00 23.41 ? 98  ALA C C   1 
ATOM   4498 O O   . ALA C 1 98  ? 16.014  -28.672 39.638  1.00 22.72 ? 98  ALA C O   1 
ATOM   4499 C CB  . ALA C 1 98  ? 19.232  -29.110 39.182  1.00 20.32 ? 98  ALA C CB  1 
ATOM   4500 N N   . SER C 1 99  ? 17.313  -27.812 41.289  1.00 22.20 ? 99  SER C N   1 
ATOM   4501 C CA  . SER C 1 99  ? 16.315  -28.026 42.326  1.00 24.43 ? 99  SER C CA  1 
ATOM   4502 C C   . SER C 1 99  ? 15.040  -27.236 42.047  1.00 23.79 ? 99  SER C C   1 
ATOM   4503 O O   . SER C 1 99  ? 13.935  -27.695 42.412  1.00 21.97 ? 99  SER C O   1 
ATOM   4504 C CB  . SER C 1 99  ? 16.909  -27.678 43.708  1.00 22.64 ? 99  SER C CB  1 
ATOM   4505 O OG  . SER C 1 99  ? 16.827  -26.307 44.046  1.00 22.62 ? 99  SER C OG  1 
ATOM   4506 N N   . GLN C 1 100 ? 15.161  -26.099 41.351  1.00 23.23 ? 100 GLN C N   1 
ATOM   4507 C CA  . GLN C 1 100 ? 13.988  -25.323 40.925  1.00 22.15 ? 100 GLN C CA  1 
ATOM   4508 C C   . GLN C 1 100 ? 13.150  -26.114 39.929  1.00 25.40 ? 100 GLN C C   1 
ATOM   4509 O O   . GLN C 1 100 ? 11.910  -26.192 40.048  1.00 24.72 ? 100 GLN C O   1 
ATOM   4510 C CB  . GLN C 1 100 ? 14.407  -24.020 40.272  1.00 22.86 ? 100 GLN C CB  1 
ATOM   4511 C CG  . GLN C 1 100 ? 15.077  -23.008 41.137  1.00 24.27 ? 100 GLN C CG  1 
ATOM   4512 C CD  . GLN C 1 100 ? 15.314  -21.758 40.357  1.00 23.55 ? 100 GLN C CD  1 
ATOM   4513 O OE1 . GLN C 1 100 ? 14.401  -21.257 39.710  1.00 23.44 ? 100 GLN C OE1 1 
ATOM   4514 N NE2 . GLN C 1 100 ? 16.560  -21.283 40.343  1.00 19.40 ? 100 GLN C NE2 1 
ATOM   4515 N N   . MET C 1 101 ? 13.808  -26.641 38.903  1.00 23.76 ? 101 MET C N   1 
ATOM   4516 C CA  . MET C 1 101 ? 13.125  -27.378 37.838  1.00 25.16 ? 101 MET C CA  1 
ATOM   4517 C C   . MET C 1 101 ? 12.458  -28.637 38.362  1.00 23.78 ? 101 MET C C   1 
ATOM   4518 O O   . MET C 1 101 ? 11.494  -29.122 37.745  1.00 26.09 ? 101 MET C O   1 
ATOM   4519 C CB  . MET C 1 101 ? 14.099  -27.751 36.722  1.00 26.92 ? 101 MET C CB  1 
ATOM   4520 C CG  . MET C 1 101 ? 14.849  -26.547 36.189  1.00 30.35 ? 101 MET C CG  1 
ATOM   4521 S SD  . MET C 1 101 ? 13.955  -25.963 34.779  1.00 39.07 ? 101 MET C SD  1 
ATOM   4522 C CE  . MET C 1 101 ? 14.862  -27.003 33.585  1.00 35.82 ? 101 MET C CE  1 
ATOM   4523 N N   . LEU C 1 102 ? 12.987  -29.216 39.455  1.00 25.19 ? 102 LEU C N   1 
ATOM   4524 C CA  . LEU C 1 102 ? 12.453  -30.440 40.071  1.00 27.10 ? 102 LEU C CA  1 
ATOM   4525 C C   . LEU C 1 102 ? 11.413  -30.155 41.149  1.00 26.74 ? 102 LEU C C   1 
ATOM   4526 O O   . LEU C 1 102 ? 10.931  -31.099 41.787  1.00 25.25 ? 102 LEU C O   1 
ATOM   4527 C CB  . LEU C 1 102 ? 13.590  -31.298 40.684  1.00 23.81 ? 102 LEU C CB  1 
ATOM   4528 C CG  . LEU C 1 102 ? 14.645  -31.812 39.684  1.00 27.40 ? 102 LEU C CG  1 
ATOM   4529 C CD1 . LEU C 1 102 ? 15.786  -32.530 40.403  1.00 22.57 ? 102 LEU C CD1 1 
ATOM   4530 C CD2 . LEU C 1 102 ? 13.993  -32.695 38.593  1.00 24.46 ? 102 LEU C CD2 1 
ATOM   4531 N N   . TYR C 1 103 ? 11.112  -28.876 41.407  1.00 24.59 ? 103 TYR C N   1 
ATOM   4532 C CA  . TYR C 1 103 ? 10.112  -28.458 42.379  1.00 27.83 ? 103 TYR C CA  1 
ATOM   4533 C C   . TYR C 1 103 ? 10.467  -28.909 43.789  1.00 26.09 ? 103 TYR C C   1 
ATOM   4534 O O   . TYR C 1 103 ? 9.588   -29.327 44.552  1.00 26.83 ? 103 TYR C O   1 
ATOM   4535 C CB  . TYR C 1 103 ? 8.700   -28.932 41.986  1.00 21.07 ? 103 TYR C CB  1 
ATOM   4536 C CG  . TYR C 1 103 ? 8.151   -28.178 40.756  1.00 23.55 ? 103 TYR C CG  1 
ATOM   4537 C CD1 . TYR C 1 103 ? 8.513   -28.556 39.489  1.00 22.82 ? 103 TYR C CD1 1 
ATOM   4538 C CD2 . TYR C 1 103 ? 7.270   -27.056 40.893  1.00 24.38 ? 103 TYR C CD2 1 
ATOM   4539 C CE1 . TYR C 1 103 ? 8.058   -27.886 38.387  1.00 24.66 ? 103 TYR C CE1 1 
ATOM   4540 C CE2 . TYR C 1 103 ? 6.781   -26.383 39.766  1.00 21.39 ? 103 TYR C CE2 1 
ATOM   4541 C CZ  . TYR C 1 103 ? 7.175   -26.821 38.516  1.00 24.27 ? 103 TYR C CZ  1 
ATOM   4542 O OH  . TYR C 1 103 ? 6.778   -26.163 37.363  1.00 24.06 ? 103 TYR C OH  1 
ATOM   4543 N N   . HIS C 1 104 ? 11.751  -28.821 44.136  1.00 24.85 ? 104 HIS C N   1 
ATOM   4544 C CA  . HIS C 1 104 ? 12.275  -29.178 45.471  1.00 25.18 ? 104 HIS C CA  1 
ATOM   4545 C C   . HIS C 1 104 ? 13.439  -28.237 45.785  1.00 28.48 ? 104 HIS C C   1 
ATOM   4546 O O   . HIS C 1 104 ? 14.619  -28.630 45.957  1.00 27.97 ? 104 HIS C O   1 
ATOM   4547 C CB  . HIS C 1 104 ? 12.668  -30.656 45.488  1.00 26.74 ? 104 HIS C CB  1 
ATOM   4548 C CG  . HIS C 1 104 ? 13.002  -31.203 46.851  1.00 31.76 ? 104 HIS C CG  1 
ATOM   4549 N ND1 . HIS C 1 104 ? 12.038  -31.516 47.795  1.00 30.30 ? 104 HIS C ND1 1 
ATOM   4550 C CD2 . HIS C 1 104 ? 14.184  -31.604 47.383  1.00 30.99 ? 104 HIS C CD2 1 
ATOM   4551 C CE1 . HIS C 1 104 ? 12.625  -32.003 48.880  1.00 32.65 ? 104 HIS C CE1 1 
ATOM   4552 N NE2 . HIS C 1 104 ? 13.926  -32.081 48.651  1.00 32.64 ? 104 HIS C NE2 1 
ATOM   4553 N N   . TYR C 1 105 ? 13.126  -26.950 45.842  1.00 24.83 ? 105 TYR C N   1 
ATOM   4554 C CA  . TYR C 1 105 ? 14.154  -25.908 45.848  1.00 25.91 ? 105 TYR C CA  1 
ATOM   4555 C C   . TYR C 1 105 ? 15.057  -26.003 47.072  1.00 28.30 ? 105 TYR C C   1 
ATOM   4556 O O   . TYR C 1 105 ? 14.581  -26.117 48.204  1.00 27.55 ? 105 TYR C O   1 
ATOM   4557 C CB  . TYR C 1 105 ? 13.486  -24.520 45.786  1.00 23.00 ? 105 TYR C CB  1 
ATOM   4558 C CG  . TYR C 1 105 ? 14.461  -23.368 45.979  1.00 27.78 ? 105 TYR C CG  1 
ATOM   4559 C CD1 . TYR C 1 105 ? 15.442  -23.091 45.031  1.00 23.15 ? 105 TYR C CD1 1 
ATOM   4560 C CD2 . TYR C 1 105 ? 14.436  -22.596 47.147  1.00 24.97 ? 105 TYR C CD2 1 
ATOM   4561 C CE1 . TYR C 1 105 ? 16.358  -22.056 45.222  1.00 24.34 ? 105 TYR C CE1 1 
ATOM   4562 C CE2 . TYR C 1 105 ? 15.354  -21.604 47.349  1.00 25.81 ? 105 TYR C CE2 1 
ATOM   4563 C CZ  . TYR C 1 105 ? 16.304  -21.317 46.387  1.00 26.69 ? 105 TYR C CZ  1 
ATOM   4564 O OH  . TYR C 1 105 ? 17.215  -20.288 46.616  1.00 24.19 ? 105 TYR C OH  1 
ATOM   4565 N N   . LYS C 1 106 ? 16.371  -25.938 46.838  1.00 25.88 ? 106 LYS C N   1 
ATOM   4566 C CA  . LYS C 1 106 ? 17.378  -25.770 47.884  1.00 28.90 ? 106 LYS C CA  1 
ATOM   4567 C C   . LYS C 1 106 ? 18.270  -24.613 47.471  1.00 26.62 ? 106 LYS C C   1 
ATOM   4568 O O   . LYS C 1 106 ? 18.730  -24.558 46.327  1.00 26.61 ? 106 LYS C O   1 
ATOM   4569 C CB  . LYS C 1 106 ? 18.253  -27.023 48.085  1.00 28.38 ? 106 LYS C CB  1 
ATOM   4570 C CG  . LYS C 1 106 ? 17.456  -28.358 48.330  1.00 28.72 ? 106 LYS C CG  1 
ATOM   4571 C CD  . LYS C 1 106 ? 16.769  -28.358 49.666  1.00 29.22 ? 106 LYS C CD  1 
ATOM   4572 C CE  . LYS C 1 106 ? 15.935  -29.603 49.838  1.00 34.30 ? 106 LYS C CE  1 
ATOM   4573 N NZ  . LYS C 1 106 ? 15.090  -29.457 51.035  1.00 36.59 ? 106 LYS C NZ  1 
ATOM   4574 N N   . SER C 1 107 ? 18.525  -23.708 48.397  1.00 25.10 ? 107 SER C N   1 
ATOM   4575 C CA  . SER C 1 107 ? 19.263  -22.510 48.083  1.00 26.02 ? 107 SER C CA  1 
ATOM   4576 C C   . SER C 1 107 ? 20.728  -22.848 47.740  1.00 25.71 ? 107 SER C C   1 
ATOM   4577 O O   . SER C 1 107 ? 21.218  -23.959 47.999  1.00 25.99 ? 107 SER C O   1 
ATOM   4578 C CB  . SER C 1 107 ? 19.185  -21.554 49.265  1.00 29.37 ? 107 SER C CB  1 
ATOM   4579 O OG  . SER C 1 107 ? 19.913  -22.119 50.351  1.00 30.11 ? 107 SER C OG  1 
ATOM   4580 N N   . GLU C 1 108 ? 21.423  -21.869 47.140  1.00 23.60 ? 108 GLU C N   1 
ATOM   4581 C CA  . GLU C 1 108 ? 22.841  -22.035 46.813  1.00 27.79 ? 108 GLU C CA  1 
ATOM   4582 C C   . GLU C 1 108 ? 23.658  -22.419 48.048  1.00 28.60 ? 108 GLU C C   1 
ATOM   4583 O O   . GLU C 1 108 ? 24.450  -23.379 48.002  1.00 29.72 ? 108 GLU C O   1 
ATOM   4584 C CB  . GLU C 1 108 ? 23.403  -20.761 46.154  1.00 28.75 ? 108 GLU C CB  1 
ATOM   4585 C CG  . GLU C 1 108 ? 24.907  -20.824 45.985  1.00 28.64 ? 108 GLU C CG  1 
ATOM   4586 C CD  . GLU C 1 108 ? 25.532  -19.530 45.403  1.00 31.64 ? 108 GLU C CD  1 
ATOM   4587 O OE1 . GLU C 1 108 ? 24.827  -18.793 44.651  1.00 30.54 ? 108 GLU C OE1 1 
ATOM   4588 O OE2 . GLU C 1 108 ? 26.724  -19.268 45.700  1.00 28.31 ? 108 GLU C OE2 1 
ATOM   4589 N N   . SER C 1 109 ? 23.448  -21.728 49.184  1.00 27.06 ? 109 SER C N   1 
ATOM   4590 C CA  . SER C 1 109 ? 24.268  -22.036 50.359  1.00 31.45 ? 109 SER C CA  1 
ATOM   4591 C C   . SER C 1 109 ? 23.942  -23.410 50.942  1.00 31.11 ? 109 SER C C   1 
ATOM   4592 O O   . SER C 1 109 ? 24.844  -24.147 51.371  1.00 29.92 ? 109 SER C O   1 
ATOM   4593 C CB  . SER C 1 109 ? 24.151  -20.933 51.409  1.00 30.66 ? 109 SER C CB  1 
ATOM   4594 O OG  . SER C 1 109 ? 22.861  -20.785 51.862  1.00 38.97 ? 109 SER C OG  1 
ATOM   4595 N N   . GLU C 1 110 ? 22.667  -23.775 50.951  1.00 29.38 ? 110 GLU C N   1 
ATOM   4596 C CA  . GLU C 1 110 ? 22.278  -25.109 51.398  1.00 32.82 ? 110 GLU C CA  1 
ATOM   4597 C C   . GLU C 1 110 ? 22.978  -26.198 50.597  1.00 31.49 ? 110 GLU C C   1 
ATOM   4598 O O   . GLU C 1 110 ? 23.429  -27.204 51.161  1.00 33.96 ? 110 GLU C O   1 
ATOM   4599 C CB  . GLU C 1 110 ? 20.781  -25.277 51.265  1.00 28.50 ? 110 GLU C CB  1 
ATOM   4600 C CG  . GLU C 1 110 ? 20.092  -25.185 52.546  1.00 38.05 ? 110 GLU C CG  1 
ATOM   4601 C CD  . GLU C 1 110 ? 18.652  -25.679 52.475  1.00 39.94 ? 110 GLU C CD  1 
ATOM   4602 O OE1 . GLU C 1 110 ? 18.452  -26.913 52.575  1.00 43.92 ? 110 GLU C OE1 1 
ATOM   4603 O OE2 . GLU C 1 110 ? 17.759  -24.815 52.303  1.00 43.11 ? 110 GLU C OE2 1 
ATOM   4604 N N   . CYS C 1 111 ? 23.048  -26.028 49.272  1.00 27.31 ? 111 CYS C N   1 
ATOM   4605 C CA  . CYS C 1 111 ? 23.756  -26.979 48.434  1.00 28.93 ? 111 CYS C CA  1 
ATOM   4606 C C   . CYS C 1 111 ? 25.256  -26.952 48.739  1.00 32.97 ? 111 CYS C C   1 
ATOM   4607 O O   . CYS C 1 111 ? 25.926  -28.006 48.691  1.00 29.30 ? 111 CYS C O   1 
ATOM   4608 C CB  . CYS C 1 111 ? 23.461  -26.690 46.959  1.00 27.02 ? 111 CYS C CB  1 
ATOM   4609 S SG  . CYS C 1 111 ? 21.716  -26.938 46.485  1.00 25.08 ? 111 CYS C SG  1 
ATOM   4610 N N   . ALA C 1 112 ? 25.799  -25.751 48.888  1.00 29.15 ? 112 ALA C N   1 
ATOM   4611 C CA  . ALA C 1 112 ? 27.238  -25.594 49.170  1.00 33.10 ? 112 ALA C CA  1 
ATOM   4612 C C   . ALA C 1 112 ? 27.576  -26.397 50.424  1.00 33.42 ? 112 ALA C C   1 
ATOM   4613 O O   . ALA C 1 112 ? 28.495  -27.208 50.382  1.00 37.69 ? 112 ALA C O   1 
ATOM   4614 C CB  . ALA C 1 112 ? 27.585  -24.144 49.327  1.00 29.79 ? 112 ALA C CB  1 
ATOM   4615 N N   . LYS C 1 113 ? 26.814  -26.185 51.479  1.00 35.11 ? 113 LYS C N   1 
ATOM   4616 C CA  . LYS C 1 113 ? 27.049  -26.897 52.753  1.00 35.02 ? 113 LYS C CA  1 
ATOM   4617 C C   . LYS C 1 113 ? 27.008  -28.410 52.533  1.00 39.92 ? 113 LYS C C   1 
ATOM   4618 O O   . LYS C 1 113 ? 27.907  -29.074 52.992  1.00 38.68 ? 113 LYS C O   1 
ATOM   4619 C CB  . LYS C 1 113 ? 26.028  -26.445 53.791  1.00 45.39 ? 113 LYS C CB  1 
ATOM   4620 C CG  . LYS C 1 113 ? 26.304  -25.094 54.433  1.00 51.60 ? 113 LYS C CG  1 
ATOM   4621 C CD  . LYS C 1 113 ? 25.057  -24.410 54.966  1.00 49.61 ? 113 LYS C CD  1 
ATOM   4622 C CE  . LYS C 1 113 ? 25.336  -23.043 55.537  1.00 51.90 ? 113 LYS C CE  1 
ATOM   4623 N NZ  . LYS C 1 113 ? 26.681  -22.947 56.150  1.00 56.64 ? 113 LYS C NZ  1 
ATOM   4624 N N   . ALA C 1 114 ? 26.010  -28.910 51.815  1.00 35.35 ? 114 ALA C N   1 
ATOM   4625 C CA  . ALA C 1 114 ? 25.868  -30.362 51.578  1.00 33.53 ? 114 ALA C CA  1 
ATOM   4626 C C   . ALA C 1 114 ? 27.025  -30.913 50.738  1.00 36.07 ? 114 ALA C C   1 
ATOM   4627 O O   . ALA C 1 114 ? 27.591  -31.928 51.104  1.00 35.93 ? 114 ALA C O   1 
ATOM   4628 C CB  . ALA C 1 114 ? 24.549  -30.637 50.925  1.00 32.94 ? 114 ALA C CB  1 
ATOM   4629 N N   . LEU C 1 115 ? 27.333  -30.256 49.627  1.00 35.69 ? 115 LEU C N   1 
ATOM   4630 C CA  . LEU C 1 115 ? 28.366  -30.712 48.732  1.00 32.69 ? 115 LEU C CA  1 
ATOM   4631 C C   . LEU C 1 115 ? 29.769  -30.587 49.313  1.00 35.55 ? 115 LEU C C   1 
ATOM   4632 O O   . LEU C 1 115 ? 30.690  -31.215 48.778  1.00 32.06 ? 115 LEU C O   1 
ATOM   4633 C CB  . LEU C 1 115 ? 28.268  -29.958 47.414  1.00 28.18 ? 115 LEU C CB  1 
ATOM   4634 C CG  . LEU C 1 115 ? 26.935  -30.143 46.682  1.00 31.62 ? 115 LEU C CG  1 
ATOM   4635 C CD1 . LEU C 1 115 ? 27.084  -29.718 45.219  1.00 29.88 ? 115 LEU C CD1 1 
ATOM   4636 C CD2 . LEU C 1 115 ? 26.281  -31.537 46.813  1.00 28.89 ? 115 LEU C CD2 1 
ATOM   4637 N N   . GLY C 1 116 ? 29.976  -29.788 50.357  1.00 35.09 ? 116 GLY C N   1 
ATOM   4638 C CA  . GLY C 1 116 ? 31.329  -29.584 50.834  1.00 35.51 ? 116 GLY C CA  1 
ATOM   4639 C C   . GLY C 1 116 ? 32.183  -28.668 49.983  1.00 37.72 ? 116 GLY C C   1 
ATOM   4640 O O   . GLY C 1 116 ? 33.392  -28.872 49.886  1.00 35.15 ? 116 GLY C O   1 
ATOM   4641 N N   . THR C 1 117 ? 31.548  -27.671 49.390  1.00 33.60 ? 117 THR C N   1 
ATOM   4642 C CA  . THR C 1 117 ? 32.252  -26.737 48.493  1.00 37.04 ? 117 THR C CA  1 
ATOM   4643 C C   . THR C 1 117 ? 33.326  -25.982 49.265  1.00 37.66 ? 117 THR C C   1 
ATOM   4644 O O   . THR C 1 117 ? 33.075  -25.607 50.387  1.00 40.48 ? 117 THR C O   1 
ATOM   4645 C CB  . THR C 1 117 ? 31.260  -25.827 47.772  1.00 34.73 ? 117 THR C CB  1 
ATOM   4646 O OG1 . THR C 1 117 ? 30.378  -26.721 47.113  1.00 30.16 ? 117 THR C OG1 1 
ATOM   4647 C CG2 . THR C 1 117 ? 31.941  -24.935 46.767  1.00 33.04 ? 117 THR C CG2 1 
ATOM   4648 N N   . SER C 1 118 ? 34.468  -25.756 48.631  1.00 39.24 ? 118 SER C N   1 
ATOM   4649 C CA  . SER C 1 118 ? 35.562  -25.057 49.333  1.00 37.90 ? 118 SER C CA  1 
ATOM   4650 C C   . SER C 1 118 ? 36.171  -23.959 48.477  1.00 33.92 ? 118 SER C C   1 
ATOM   4651 O O   . SER C 1 118 ? 36.199  -24.057 47.274  1.00 37.28 ? 118 SER C O   1 
ATOM   4652 C CB  . SER C 1 118 ? 36.629  -26.023 49.770  1.00 39.17 ? 118 SER C CB  1 
ATOM   4653 O OG  . SER C 1 118 ? 37.470  -26.360 48.690  1.00 39.46 ? 118 SER C OG  1 
ATOM   4654 N N   . LYS C 1 119 ? 36.714  -22.977 49.163  1.00 39.95 ? 119 LYS C N   1 
ATOM   4655 C CA  . LYS C 1 119 ? 37.435  -21.910 48.474  1.00 40.05 ? 119 LYS C CA  1 
ATOM   4656 C C   . LYS C 1 119 ? 38.662  -22.487 47.762  1.00 45.36 ? 119 LYS C C   1 
ATOM   4657 O O   . LYS C 1 119 ? 38.840  -21.981 46.654  1.00 48.18 ? 119 LYS C O   1 
ATOM   4658 C CB  . LYS C 1 119 ? 37.764  -20.774 49.445  1.00 48.47 ? 119 LYS C CB  1 
ATOM   4659 C CG  . LYS C 1 119 ? 37.946  -19.418 48.780  1.00 49.89 ? 119 LYS C CG  1 
ATOM   4660 C CD  . LYS C 1 119 ? 38.852  -19.445 47.550  1.00 52.90 ? 119 LYS C CD  1 
ATOM   4661 C CE  . LYS C 1 119 ? 38.270  -18.825 46.297  1.00 54.68 ? 119 LYS C CE  1 
ATOM   4662 N NZ  . LYS C 1 119 ? 38.480  -19.680 45.108  1.00 59.87 ? 119 LYS C NZ  1 
ATOM   4663 N N   . GLY C 1 120 ? 39.385  -23.540 48.252  1.00 48.13 ? 120 GLY C N   1 
ATOM   4664 C CA  . GLY C 1 120 ? 40.546  -23.764 47.439  1.00 46.43 ? 120 GLY C CA  1 
ATOM   4665 C C   . GLY C 1 120 ? 40.300  -24.640 46.239  1.00 49.24 ? 120 GLY C C   1 
ATOM   4666 O O   . GLY C 1 120 ? 40.937  -24.451 45.191  1.00 54.16 ? 120 GLY C O   1 
ATOM   4667 N N   . SER C 1 121 ? 39.378  -25.590 46.374  1.00 46.97 ? 121 SER C N   1 
ATOM   4668 C CA  . SER C 1 121 ? 39.209  -26.611 45.361  1.00 44.99 ? 121 SER C CA  1 
ATOM   4669 C C   . SER C 1 121 ? 37.860  -26.569 44.656  1.00 35.87 ? 121 SER C C   1 
ATOM   4670 O O   . SER C 1 121 ? 37.724  -27.204 43.613  1.00 37.49 ? 121 SER C O   1 
ATOM   4671 C CB  . SER C 1 121 ? 39.424  -27.989 45.999  1.00 41.35 ? 121 SER C CB  1 
ATOM   4672 O OG  . SER C 1 121 ? 38.405  -28.239 46.961  1.00 48.57 ? 121 SER C OG  1 
ATOM   4673 N N   . GLY C 1 122 ? 36.925  -25.729 45.092  1.00 34.90 ? 122 GLY C N   1 
ATOM   4674 C CA  . GLY C 1 122 ? 35.601  -25.760 44.479  1.00 34.07 ? 122 GLY C CA  1 
ATOM   4675 C C   . GLY C 1 122 ? 34.833  -27.024 44.877  1.00 28.93 ? 122 GLY C C   1 
ATOM   4676 O O   . GLY C 1 122 ? 34.721  -27.365 46.056  1.00 28.07 ? 122 GLY C O   1 
ATOM   4677 N N   . THR C 1 123 ? 34.291  -27.719 43.885  1.00 26.10 ? 123 THR C N   1 
ATOM   4678 C CA  . THR C 1 123 ? 33.510  -28.928 44.124  1.00 28.46 ? 123 THR C CA  1 
ATOM   4679 C C   . THR C 1 123 ? 33.888  -29.919 43.043  1.00 27.70 ? 123 THR C C   1 
ATOM   4680 O O   . THR C 1 123 ? 33.830  -29.577 41.859  1.00 28.30 ? 123 THR C O   1 
ATOM   4681 C CB  . THR C 1 123 ? 31.976  -28.708 44.048  1.00 28.31 ? 123 THR C CB  1 
ATOM   4682 O OG1 . THR C 1 123 ? 31.540  -27.563 44.824  1.00 24.72 ? 123 THR C OG1 1 
ATOM   4683 C CG2 . THR C 1 123 ? 31.251  -29.997 44.506  1.00 23.55 ? 123 THR C CG2 1 
ATOM   4684 N N   . SER C 1 124 ? 34.222  -31.156 43.438  1.00 26.94 ? 124 SER C N   1 
ATOM   4685 C CA  . SER C 1 124 ? 34.570  -32.148 42.441  1.00 26.42 ? 124 SER C CA  1 
ATOM   4686 C C   . SER C 1 124 ? 33.320  -32.892 42.013  1.00 27.15 ? 124 SER C C   1 
ATOM   4687 O O   . SER C 1 124 ? 32.307  -32.866 42.712  1.00 28.65 ? 124 SER C O   1 
ATOM   4688 C CB  . SER C 1 124 ? 35.617  -33.132 43.013  1.00 28.07 ? 124 SER C CB  1 
ATOM   4689 O OG  . SER C 1 124 ? 34.994  -33.980 43.968  1.00 25.43 ? 124 SER C OG  1 
ATOM   4690 N N   . PRO C 1 125 ? 33.357  -33.577 40.868  1.00 27.36 ? 125 PRO C N   1 
ATOM   4691 C CA  . PRO C 1 125 ? 32.194  -34.385 40.477  1.00 25.84 ? 125 PRO C CA  1 
ATOM   4692 C C   . PRO C 1 125 ? 31.803  -35.429 41.496  1.00 28.51 ? 125 PRO C C   1 
ATOM   4693 O O   . PRO C 1 125 ? 30.599  -35.544 41.822  1.00 26.30 ? 125 PRO C O   1 
ATOM   4694 C CB  . PRO C 1 125 ? 32.634  -35.031 39.158  1.00 27.11 ? 125 PRO C CB  1 
ATOM   4695 C CG  . PRO C 1 125 ? 33.682  -34.096 38.609  1.00 31.14 ? 125 PRO C CG  1 
ATOM   4696 C CD  . PRO C 1 125 ? 34.391  -33.513 39.814  1.00 30.72 ? 125 PRO C CD  1 
ATOM   4697 N N   . ALA C 1 126 ? 32.775  -36.120 42.097  1.00 25.79 ? 126 ALA C N   1 
ATOM   4698 C CA  . ALA C 1 126 ? 32.434  -37.138 43.092  1.00 23.71 ? 126 ALA C CA  1 
ATOM   4699 C C   . ALA C 1 126 ? 31.752  -36.533 44.305  1.00 24.54 ? 126 ALA C C   1 
ATOM   4700 O O   . ALA C 1 126 ? 30.943  -37.191 44.955  1.00 24.85 ? 126 ALA C O   1 
ATOM   4701 C CB  . ALA C 1 126 ? 33.694  -37.912 43.542  1.00 24.19 ? 126 ALA C CB  1 
ATOM   4702 N N   . GLN C 1 127 ? 32.119  -35.306 44.664  1.00 26.68 ? 127 GLN C N   1 
ATOM   4703 C CA  . GLN C 1 127 ? 31.461  -34.625 45.755  1.00 25.80 ? 127 GLN C CA  1 
ATOM   4704 C C   . GLN C 1 127 ? 29.985  -34.351 45.432  1.00 28.61 ? 127 GLN C C   1 
ATOM   4705 O O   . GLN C 1 127 ? 29.111  -34.527 46.285  1.00 23.97 ? 127 GLN C O   1 
ATOM   4706 C CB  . GLN C 1 127 ? 32.198  -33.323 46.023  1.00 29.34 ? 127 GLN C CB  1 
ATOM   4707 C CG  . GLN C 1 127 ? 32.980  -33.282 47.333  1.00 33.13 ? 127 GLN C CG  1 
ATOM   4708 C CD  . GLN C 1 127 ? 33.887  -32.074 47.458  1.00 30.44 ? 127 GLN C CD  1 
ATOM   4709 O OE1 . GLN C 1 127 ? 34.356  -31.542 46.476  1.00 32.40 ? 127 GLN C OE1 1 
ATOM   4710 N NE2 . GLN C 1 127 ? 34.047  -31.585 48.671  1.00 33.82 ? 127 GLN C NE2 1 
ATOM   4711 N N   . LEU C 1 128 ? 29.700  -33.940 44.195  1.00 25.64 ? 128 LEU C N   1 
ATOM   4712 C CA  . LEU C 1 128 ? 28.322  -33.707 43.775  1.00 25.63 ? 128 LEU C CA  1 
ATOM   4713 C C   . LEU C 1 128 ? 27.492  -34.990 43.796  1.00 24.94 ? 128 LEU C C   1 
ATOM   4714 O O   . LEU C 1 128 ? 26.358  -34.992 44.298  1.00 25.48 ? 128 LEU C O   1 
ATOM   4715 C CB  . LEU C 1 128 ? 28.312  -33.096 42.381  1.00 25.22 ? 128 LEU C CB  1 
ATOM   4716 C CG  . LEU C 1 128 ? 26.975  -33.068 41.657  1.00 26.64 ? 128 LEU C CG  1 
ATOM   4717 C CD1 . LEU C 1 128 ? 26.022  -32.033 42.338  1.00 26.27 ? 128 LEU C CD1 1 
ATOM   4718 C CD2 . LEU C 1 128 ? 27.216  -32.767 40.176  1.00 24.12 ? 128 LEU C CD2 1 
ATOM   4719 N N   . ILE C 1 129 ? 28.028  -36.085 43.227  1.00 24.84 ? 129 ILE C N   1 
ATOM   4720 C CA  . ILE C 1 129 ? 27.291  -37.350 43.183  1.00 27.07 ? 129 ILE C CA  1 
ATOM   4721 C C   . ILE C 1 129 ? 27.090  -37.890 44.592  1.00 29.22 ? 129 ILE C C   1 
ATOM   4722 O O   . ILE C 1 129 ? 25.993  -38.346 44.950  1.00 29.46 ? 129 ILE C O   1 
ATOM   4723 C CB  . ILE C 1 129 ? 28.021  -38.372 42.287  1.00 28.59 ? 129 ILE C CB  1 
ATOM   4724 C CG1 . ILE C 1 129 ? 28.079  -37.901 40.823  1.00 27.30 ? 129 ILE C CG1 1 
ATOM   4725 C CG2 . ILE C 1 129 ? 27.390  -39.755 42.403  1.00 27.22 ? 129 ILE C CG2 1 
ATOM   4726 C CD1 . ILE C 1 129 ? 29.475  -38.268 40.119  1.00 28.19 ? 129 ILE C CD1 1 
ATOM   4727 N N   . ALA C 1 130 ? 28.130  -37.800 45.438  1.00 27.38 ? 130 ALA C N   1 
ATOM   4728 C CA  . ALA C 1 130 ? 28.078  -38.470 46.738  1.00 30.90 ? 130 ALA C CA  1 
ATOM   4729 C C   . ALA C 1 130 ? 27.168  -37.770 47.740  1.00 30.04 ? 130 ALA C C   1 
ATOM   4730 O O   . ALA C 1 130 ? 26.612  -38.432 48.632  1.00 30.12 ? 130 ALA C O   1 
ATOM   4731 C CB  . ALA C 1 130 ? 29.487  -38.574 47.322  1.00 28.45 ? 130 ALA C CB  1 
ATOM   4732 N N   . ASN C 1 131 ? 27.020  -36.445 47.627  1.00 28.21 ? 131 ASN C N   1 
ATOM   4733 C CA  . ASN C 1 131 ? 26.326  -35.673 48.641  1.00 29.21 ? 131 ASN C CA  1 
ATOM   4734 C C   . ASN C 1 131 ? 24.959  -35.156 48.216  1.00 30.18 ? 131 ASN C C   1 
ATOM   4735 O O   . ASN C 1 131 ? 24.204  -34.692 49.080  1.00 31.63 ? 131 ASN C O   1 
ATOM   4736 C CB  . ASN C 1 131 ? 27.197  -34.496 49.092  1.00 33.58 ? 131 ASN C CB  1 
ATOM   4737 C CG  . ASN C 1 131 ? 28.364  -34.935 49.949  1.00 33.82 ? 131 ASN C CG  1 
ATOM   4738 O OD1 . ASN C 1 131 ? 28.172  -35.333 51.099  1.00 34.82 ? 131 ASN C OD1 1 
ATOM   4739 N ND2 . ASN C 1 131 ? 29.590  -34.853 49.398  1.00 31.62 ? 131 ASN C ND2 1 
ATOM   4740 N N   . ALA C 1 132 ? 24.606  -35.219 46.926  1.00 27.21 ? 132 ALA C N   1 
ATOM   4741 C CA  . ALA C 1 132 ? 23.245  -34.832 46.512  1.00 31.58 ? 132 ALA C CA  1 
ATOM   4742 C C   . ALA C 1 132 ? 22.138  -35.551 47.290  1.00 28.35 ? 132 ALA C C   1 
ATOM   4743 O O   . ALA C 1 132 ? 21.066  -34.954 47.528  1.00 28.73 ? 132 ALA C O   1 
ATOM   4744 C CB  . ALA C 1 132 ? 23.019  -35.073 45.012  1.00 29.26 ? 132 ALA C CB  1 
ATOM   4745 N N   . PRO C 1 133 ? 22.325  -36.804 47.730  1.00 31.13 ? 133 PRO C N   1 
ATOM   4746 C CA  . PRO C 1 133 ? 21.243  -37.436 48.529  1.00 30.93 ? 133 PRO C CA  1 
ATOM   4747 C C   . PRO C 1 133 ? 20.910  -36.696 49.817  1.00 30.03 ? 133 PRO C C   1 
ATOM   4748 O O   . PRO C 1 133 ? 19.767  -36.800 50.290  1.00 30.28 ? 133 PRO C O   1 
ATOM   4749 C CB  . PRO C 1 133 ? 21.787  -38.843 48.827  1.00 34.01 ? 133 PRO C CB  1 
ATOM   4750 C CG  . PRO C 1 133 ? 22.836  -39.109 47.795  1.00 30.17 ? 133 PRO C CG  1 
ATOM   4751 C CD  . PRO C 1 133 ? 23.288  -37.803 47.199  1.00 29.12 ? 133 PRO C CD  1 
ATOM   4752 N N   . LYS C 1 134 ? 21.850  -35.925 50.377  1.00 27.24 ? 134 LYS C N   1 
ATOM   4753 C CA  . LYS C 1 134 ? 21.556  -35.130 51.564  1.00 28.15 ? 134 LYS C CA  1 
ATOM   4754 C C   . LYS C 1 134 ? 20.382  -34.184 51.315  1.00 30.92 ? 134 LYS C C   1 
ATOM   4755 O O   . LYS C 1 134 ? 19.629  -33.875 52.238  1.00 32.17 ? 134 LYS C O   1 
ATOM   4756 C CB  . LYS C 1 134 ? 22.766  -34.293 51.984  1.00 27.73 ? 134 LYS C CB  1 
ATOM   4757 C CG  . LYS C 1 134 ? 23.863  -35.044 52.755  1.00 32.76 ? 134 LYS C CG  1 
ATOM   4758 C CD  . LYS C 1 134 ? 25.185  -34.201 52.821  1.00 31.88 ? 134 LYS C CD  1 
ATOM   4759 C CE  . LYS C 1 134 ? 26.191  -34.837 53.749  1.00 33.55 ? 134 LYS C CE  1 
ATOM   4760 N NZ  . LYS C 1 134 ? 27.508  -34.206 53.563  1.00 42.10 ? 134 LYS C NZ  1 
ATOM   4761 N N   . LEU C 1 135 ? 20.193  -33.751 50.069  1.00 29.99 ? 135 LEU C N   1 
ATOM   4762 C CA  . LEU C 1 135 ? 19.161  -32.793 49.704  1.00 30.37 ? 135 LEU C CA  1 
ATOM   4763 C C   . LEU C 1 135 ? 17.927  -33.454 49.105  1.00 32.16 ? 135 LEU C C   1 
ATOM   4764 O O   . LEU C 1 135 ? 17.007  -32.748 48.718  1.00 32.85 ? 135 LEU C O   1 
ATOM   4765 C CB  . LEU C 1 135 ? 19.744  -31.768 48.714  1.00 28.84 ? 135 LEU C CB  1 
ATOM   4766 C CG  . LEU C 1 135 ? 21.002  -31.076 49.203  1.00 29.66 ? 135 LEU C CG  1 
ATOM   4767 C CD1 . LEU C 1 135 ? 21.818  -30.467 48.033  1.00 30.04 ? 135 LEU C CD1 1 
ATOM   4768 C CD2 . LEU C 1 135 ? 20.654  -29.969 50.198  1.00 29.31 ? 135 LEU C CD2 1 
ATOM   4769 N N   . GLY C 1 136 ? 17.894  -34.782 48.996  1.00 30.90 ? 136 GLY C N   1 
ATOM   4770 C CA  . GLY C 1 136 ? 16.788  -35.492 48.386  1.00 27.81 ? 136 GLY C CA  1 
ATOM   4771 C C   . GLY C 1 136 ? 16.935  -35.830 46.920  1.00 30.47 ? 136 GLY C C   1 
ATOM   4772 O O   . GLY C 1 136 ? 15.950  -36.249 46.323  1.00 30.59 ? 136 GLY C O   1 
ATOM   4773 N N   . PHE C 1 137 ? 18.137  -35.685 46.324  1.00 27.80 ? 137 PHE C N   1 
ATOM   4774 C CA  . PHE C 1 137 ? 18.391  -35.933 44.908  1.00 27.00 ? 137 PHE C CA  1 
ATOM   4775 C C   . PHE C 1 137 ? 19.292  -37.147 44.689  1.00 29.73 ? 137 PHE C C   1 
ATOM   4776 O O   . PHE C 1 137 ? 20.013  -37.589 45.586  1.00 27.12 ? 137 PHE C O   1 
ATOM   4777 C CB  . PHE C 1 137 ? 19.068  -34.729 44.238  1.00 27.61 ? 137 PHE C CB  1 
ATOM   4778 C CG  . PHE C 1 137 ? 18.273  -33.446 44.371  1.00 25.81 ? 137 PHE C CG  1 
ATOM   4779 C CD1 . PHE C 1 137 ? 16.966  -33.382 43.926  1.00 27.75 ? 137 PHE C CD1 1 
ATOM   4780 C CD2 . PHE C 1 137 ? 18.834  -32.332 44.971  1.00 27.26 ? 137 PHE C CD2 1 
ATOM   4781 C CE1 . PHE C 1 137 ? 16.205  -32.173 44.062  1.00 27.30 ? 137 PHE C CE1 1 
ATOM   4782 C CE2 . PHE C 1 137 ? 18.106  -31.158 45.094  1.00 27.32 ? 137 PHE C CE2 1 
ATOM   4783 C CZ  . PHE C 1 137 ? 16.783  -31.104 44.644  1.00 26.52 ? 137 PHE C CZ  1 
ATOM   4784 N N   . LYS C 1 138 ? 19.222  -37.674 43.461  1.00 27.92 ? 138 LYS C N   1 
ATOM   4785 C CA  . LYS C 1 138 ? 20.144  -38.668 42.930  1.00 28.97 ? 138 LYS C CA  1 
ATOM   4786 C C   . LYS C 1 138 ? 20.781  -38.105 41.670  1.00 30.64 ? 138 LYS C C   1 
ATOM   4787 O O   . LYS C 1 138 ? 20.099  -37.451 40.875  1.00 30.39 ? 138 LYS C O   1 
ATOM   4788 C CB  . LYS C 1 138 ? 19.408  -39.993 42.609  1.00 31.93 ? 138 LYS C CB  1 
ATOM   4789 C CG  . LYS C 1 138 ? 20.331  -41.080 42.094  1.00 33.16 ? 138 LYS C CG  1 
ATOM   4790 C CD  . LYS C 1 138 ? 19.547  -42.344 41.721  1.00 35.77 ? 138 LYS C CD  1 
ATOM   4791 C CE  . LYS C 1 138 ? 18.948  -42.162 40.351  1.00 39.02 ? 138 LYS C CE  1 
ATOM   4792 N NZ  . LYS C 1 138 ? 17.495  -42.424 40.347  1.00 42.06 ? 138 LYS C NZ  1 
ATOM   4793 N N   . ILE C 1 139 ? 22.104  -38.286 41.526  1.00 28.77 ? 139 ILE C N   1 
ATOM   4794 C CA  . ILE C 1 139 ? 22.845  -37.845 40.342  1.00 26.96 ? 139 ILE C CA  1 
ATOM   4795 C C   . ILE C 1 139 ? 23.128  -39.063 39.481  1.00 28.03 ? 139 ILE C C   1 
ATOM   4796 O O   . ILE C 1 139 ? 23.624  -40.078 39.988  1.00 30.14 ? 139 ILE C O   1 
ATOM   4797 C CB  . ILE C 1 139 ? 24.158  -37.131 40.728  1.00 30.08 ? 139 ILE C CB  1 
ATOM   4798 C CG1 . ILE C 1 139 ? 23.900  -35.885 41.569  1.00 26.41 ? 139 ILE C CG1 1 
ATOM   4799 C CG2 . ILE C 1 139 ? 24.967  -36.788 39.482  1.00 25.78 ? 139 ILE C CG2 1 
ATOM   4800 C CD1 . ILE C 1 139 ? 23.180  -34.779 40.816  1.00 26.97 ? 139 ILE C CD1 1 
ATOM   4801 N N   . ILE C 1 140 ? 22.825  -38.977 38.189  1.00 28.76 ? 140 ILE C N   1 
ATOM   4802 C CA  . ILE C 1 140 ? 23.119  -40.059 37.251  1.00 29.75 ? 140 ILE C CA  1 
ATOM   4803 C C   . ILE C 1 140 ? 24.231  -39.595 36.300  1.00 28.23 ? 140 ILE C C   1 
ATOM   4804 O O   . ILE C 1 140 ? 23.986  -38.781 35.402  1.00 25.06 ? 140 ILE C O   1 
ATOM   4805 C CB  . ILE C 1 140 ? 21.865  -40.496 36.477  1.00 26.29 ? 140 ILE C CB  1 
ATOM   4806 C CG1 . ILE C 1 140 ? 20.928  -41.272 37.395  1.00 34.73 ? 140 ILE C CG1 1 
ATOM   4807 C CG2 . ILE C 1 140 ? 22.206  -41.499 35.360  1.00 30.75 ? 140 ILE C CG2 1 
ATOM   4808 C CD1 . ILE C 1 140 ? 19.441  -41.290 36.927  1.00 30.46 ? 140 ILE C CD1 1 
ATOM   4809 N N   . PRO C 1 141 ? 25.468  -40.077 36.449  1.00 28.73 ? 141 PRO C N   1 
ATOM   4810 C CA  . PRO C 1 141 ? 26.516  -39.751 35.462  1.00 26.76 ? 141 PRO C CA  1 
ATOM   4811 C C   . PRO C 1 141 ? 26.215  -40.373 34.104  1.00 30.41 ? 141 PRO C C   1 
ATOM   4812 O O   . PRO C 1 141 ? 25.904  -41.562 34.005  1.00 33.11 ? 141 PRO C O   1 
ATOM   4813 C CB  . PRO C 1 141 ? 27.788  -40.337 36.078  1.00 30.67 ? 141 PRO C CB  1 
ATOM   4814 C CG  . PRO C 1 141 ? 27.469  -40.606 37.510  1.00 29.92 ? 141 PRO C CG  1 
ATOM   4815 C CD  . PRO C 1 141 ? 25.989  -40.755 37.644  1.00 30.81 ? 141 PRO C CD  1 
ATOM   4816 N N   . ILE C 1 142 ? 26.223  -39.547 33.060  1.00 27.46 ? 142 ILE C N   1 
ATOM   4817 C CA  . ILE C 1 142 ? 25.888  -40.007 31.721  1.00 28.45 ? 142 ILE C CA  1 
ATOM   4818 C C   . ILE C 1 142 ? 27.038  -39.619 30.815  1.00 29.92 ? 142 ILE C C   1 
ATOM   4819 O O   . ILE C 1 142 ? 27.877  -38.800 31.174  1.00 29.61 ? 142 ILE C O   1 
ATOM   4820 C CB  . ILE C 1 142 ? 24.559  -39.441 31.164  1.00 30.78 ? 142 ILE C CB  1 
ATOM   4821 C CG1 . ILE C 1 142 ? 24.598  -37.915 31.116  1.00 30.73 ? 142 ILE C CG1 1 
ATOM   4822 C CG2 . ILE C 1 142 ? 23.361  -39.937 31.980  1.00 28.57 ? 142 ILE C CG2 1 
ATOM   4823 C CD1 . ILE C 1 142 ? 23.528  -37.300 30.236  1.00 25.93 ? 142 ILE C CD1 1 
ATOM   4824 N N   . LYS C 1 143 ? 27.082  -40.247 29.640  1.00 31.92 ? 143 LYS C N   1 
ATOM   4825 C CA  . LYS C 1 143 ? 28.081  -39.883 28.660  1.00 32.86 ? 143 LYS C CA  1 
ATOM   4826 C C   . LYS C 1 143 ? 27.808  -38.466 28.151  1.00 32.90 ? 143 LYS C C   1 
ATOM   4827 O O   . LYS C 1 143 ? 26.670  -37.978 28.152  1.00 33.01 ? 143 LYS C O   1 
ATOM   4828 C CB  . LYS C 1 143 ? 28.094  -40.861 27.482  1.00 34.35 ? 143 LYS C CB  1 
ATOM   4829 C CG  . LYS C 1 143 ? 28.827  -42.179 27.796  1.00 34.81 ? 143 LYS C CG  1 
ATOM   4830 C CD  . LYS C 1 143 ? 28.046  -43.368 27.305  1.00 40.10 ? 143 LYS C CD  1 
ATOM   4831 C CE  . LYS C 1 143 ? 27.348  -43.071 25.953  1.00 44.95 ? 143 LYS C CE  1 
ATOM   4832 N NZ  . LYS C 1 143 ? 26.175  -43.991 25.755  1.00 47.13 ? 143 LYS C NZ  1 
ATOM   4833 N N   . ARG C 1 144 ? 28.877  -37.788 27.757  1.00 31.57 ? 144 ARG C N   1 
ATOM   4834 C CA  . ARG C 1 144 ? 28.760  -36.434 27.202  1.00 33.08 ? 144 ARG C CA  1 
ATOM   4835 C C   . ARG C 1 144 ? 28.235  -36.592 25.780  1.00 33.89 ? 144 ARG C C   1 
ATOM   4836 O O   . ARG C 1 144 ? 28.953  -36.440 24.788  1.00 34.09 ? 144 ARG C O   1 
ATOM   4837 C CB  . ARG C 1 144 ? 30.106  -35.710 27.277  1.00 30.19 ? 144 ARG C CB  1 
ATOM   4838 C CG  . ARG C 1 144 ? 30.677  -35.620 28.721  1.00 28.85 ? 144 ARG C CG  1 
ATOM   4839 C CD  . ARG C 1 144 ? 32.060  -34.992 28.855  1.00 28.30 ? 144 ARG C CD  1 
ATOM   4840 N NE  . ARG C 1 144 ? 32.078  -33.569 28.557  1.00 30.34 ? 144 ARG C NE  1 
ATOM   4841 C CZ  . ARG C 1 144 ? 32.144  -32.598 29.458  1.00 30.43 ? 144 ARG C CZ  1 
ATOM   4842 N NH1 . ARG C 1 144 ? 32.111  -32.853 30.756  1.00 26.86 ? 144 ARG C NH1 1 
ATOM   4843 N NH2 . ARG C 1 144 ? 32.295  -31.339 29.041  1.00 28.74 ? 144 ARG C NH2 1 
ATOM   4844 N N   . ASP C 1 145 ? 26.981  -37.012 25.739  1.00 35.49 ? 145 ASP C N   1 
ATOM   4845 C CA  . ASP C 1 145 ? 26.268  -37.370 24.494  1.00 36.99 ? 145 ASP C CA  1 
ATOM   4846 C C   . ASP C 1 145 ? 24.957  -36.604 24.463  1.00 37.44 ? 145 ASP C C   1 
ATOM   4847 O O   . ASP C 1 145 ? 24.138  -36.801 25.340  1.00 33.58 ? 145 ASP C O   1 
ATOM   4848 C CB  . ASP C 1 145 ? 25.945  -38.863 24.515  1.00 39.54 ? 145 ASP C CB  1 
ATOM   4849 C CG  . ASP C 1 145 ? 25.237  -39.400 23.289  1.00 42.33 ? 145 ASP C CG  1 
ATOM   4850 O OD1 . ASP C 1 145 ? 24.395  -38.705 22.727  1.00 41.71 ? 145 ASP C OD1 1 
ATOM   4851 O OD2 . ASP C 1 145 ? 25.534  -40.521 22.939  1.00 46.95 ? 145 ASP C OD2 1 
ATOM   4852 N N   . SER C 1 146 ? 24.741  -35.852 23.394  1.00 37.96 ? 146 SER C N   1 
ATOM   4853 C CA  . SER C 1 146 ? 23.523  -35.027 23.239  1.00 36.07 ? 146 SER C CA  1 
ATOM   4854 C C   . SER C 1 146 ? 22.263  -35.882 23.223  1.00 38.29 ? 146 SER C C   1 
ATOM   4855 O O   . SER C 1 146 ? 21.249  -35.384 23.629  1.00 38.49 ? 146 SER C O   1 
ATOM   4856 C CB  . SER C 1 146 ? 23.601  -34.216 22.015  1.00 37.32 ? 146 SER C CB  1 
ATOM   4857 O OG  . SER C 1 146 ? 23.338  -35.031 20.901  1.00 43.53 ? 146 SER C OG  1 
ATOM   4858 N N   . LYS C 1 147 ? 22.325  -37.106 22.707  1.00 40.38 ? 147 LYS C N   1 
ATOM   4859 C CA  . LYS C 1 147 ? 21.132  -37.979 22.711  1.00 47.06 ? 147 LYS C CA  1 
ATOM   4860 C C   . LYS C 1 147 ? 20.816  -38.351 24.163  1.00 42.62 ? 147 LYS C C   1 
ATOM   4861 O O   . LYS C 1 147 ? 19.647  -38.440 24.476  1.00 41.26 ? 147 LYS C O   1 
ATOM   4862 C CB  . LYS C 1 147 ? 21.301  -39.140 21.727  1.00 45.24 ? 147 LYS C CB  1 
ATOM   4863 C CG  . LYS C 1 147 ? 21.293  -40.532 22.337  1.00 48.61 ? 147 LYS C CG  1 
ATOM   4864 C CD  . LYS C 1 147 ? 22.556  -41.344 22.045  1.00 48.96 ? 147 LYS C CD  1 
ATOM   4865 C CE  . LYS C 1 147 ? 22.894  -42.345 23.130  1.00 46.16 ? 147 LYS C CE  1 
ATOM   4866 N NZ  . LYS C 1 147 ? 21.844  -42.364 24.174  1.00 55.54 ? 147 LYS C NZ  1 
ATOM   4867 N N   . GLU C 1 148 ? 21.841  -38.546 24.999  1.00 41.20 ? 148 GLU C N   1 
ATOM   4868 C CA  . GLU C 1 148 ? 21.646  -38.842 26.437  1.00 38.31 ? 148 GLU C CA  1 
ATOM   4869 C C   . GLU C 1 148 ? 21.093  -37.608 27.162  1.00 36.74 ? 148 GLU C C   1 
ATOM   4870 O O   . GLU C 1 148 ? 20.172  -37.803 27.932  1.00 33.57 ? 148 GLU C O   1 
ATOM   4871 C CB  . GLU C 1 148 ? 22.940  -39.315 27.079  1.00 37.46 ? 148 GLU C CB  1 
ATOM   4872 C CG  . GLU C 1 148 ? 23.278  -40.736 26.718  1.00 41.79 ? 148 GLU C CG  1 
ATOM   4873 C CD  . GLU C 1 148 ? 22.369  -41.760 27.352  1.00 46.62 ? 148 GLU C CD  1 
ATOM   4874 O OE1 . GLU C 1 148 ? 22.593  -42.051 28.488  1.00 44.38 ? 148 GLU C OE1 1 
ATOM   4875 O OE2 . GLU C 1 148 ? 21.442  -42.219 26.708  1.00 49.24 ? 148 GLU C OE2 1 
ATOM   4876 N N   . VAL C 1 149 ? 21.672  -36.415 26.957  1.00 32.46 ? 149 VAL C N   1 
ATOM   4877 C CA  . VAL C 1 149 ? 21.076  -35.239 27.561  1.00 33.64 ? 149 VAL C CA  1 
ATOM   4878 C C   . VAL C 1 149 ? 19.604  -35.139 27.171  1.00 31.91 ? 149 VAL C C   1 
ATOM   4879 O O   . VAL C 1 149 ? 18.731  -34.947 28.017  1.00 33.13 ? 149 VAL C O   1 
ATOM   4880 C CB  . VAL C 1 149 ? 21.894  -34.039 27.095  1.00 31.79 ? 149 VAL C CB  1 
ATOM   4881 C CG1 . VAL C 1 149 ? 21.243  -32.814 27.535  1.00 31.80 ? 149 VAL C CG1 1 
ATOM   4882 C CG2 . VAL C 1 149 ? 23.356  -34.189 27.619  1.00 24.77 ? 149 VAL C CG2 1 
ATOM   4883 N N   . LYS C 1 150 ? 19.311  -35.324 25.879  1.00 32.81 ? 150 LYS C N   1 
ATOM   4884 C CA  . LYS C 1 150 ? 17.941  -35.190 25.391  1.00 38.38 ? 150 LYS C CA  1 
ATOM   4885 C C   . LYS C 1 150 ? 17.020  -36.237 26.019  1.00 37.93 ? 150 LYS C C   1 
ATOM   4886 O O   . LYS C 1 150 ? 15.883  -35.932 26.406  1.00 35.67 ? 150 LYS C O   1 
ATOM   4887 C CB  . LYS C 1 150 ? 17.959  -35.281 23.861  1.00 41.26 ? 150 LYS C CB  1 
ATOM   4888 C CG  . LYS C 1 150 ? 16.655  -35.619 23.199  1.00 45.49 ? 150 LYS C CG  1 
ATOM   4889 C CD  . LYS C 1 150 ? 16.449  -34.686 22.016  1.00 45.75 ? 150 LYS C CD  1 
ATOM   4890 C CE  . LYS C 1 150 ? 16.649  -35.428 20.674  1.00 49.70 ? 150 LYS C CE  1 
ATOM   4891 N NZ  . LYS C 1 150 ? 16.526  -34.502 19.491  1.00 49.94 ? 150 LYS C NZ  1 
ATOM   4892 N N   . LYS C 1 151 ? 17.516  -37.460 26.198  1.00 36.72 ? 151 LYS C N   1 
ATOM   4893 C CA  . LYS C 1 151 ? 16.679  -38.487 26.798  1.00 38.71 ? 151 LYS C CA  1 
ATOM   4894 C C   . LYS C 1 151 ? 16.283  -38.113 28.213  1.00 37.85 ? 151 LYS C C   1 
ATOM   4895 O O   . LYS C 1 151 ? 15.135  -38.343 28.628  1.00 34.70 ? 151 LYS C O   1 
ATOM   4896 C CB  . LYS C 1 151 ? 17.375  -39.821 26.814  1.00 39.63 ? 151 LYS C CB  1 
ATOM   4897 C CG  . LYS C 1 151 ? 16.762  -40.890 27.625  1.00 40.10 ? 151 LYS C CG  1 
ATOM   4898 C CD  . LYS C 1 151 ? 17.555  -42.214 27.528  1.00 42.82 ? 151 LYS C CD  1 
ATOM   4899 C CE  . LYS C 1 151 ? 17.967  -42.702 28.895  1.00 43.49 ? 151 LYS C CE  1 
ATOM   4900 N NZ  . LYS C 1 151 ? 18.760  -43.940 28.753  1.00 49.56 ? 151 LYS C NZ  1 
ATOM   4901 N N   . TYR C 1 152 ? 17.222  -37.552 28.982  1.00 31.46 ? 152 TYR C N   1 
ATOM   4902 C CA  . TYR C 1 152 ? 16.897  -37.263 30.374  1.00 31.87 ? 152 TYR C CA  1 
ATOM   4903 C C   . TYR C 1 152 ? 16.130  -35.951 30.518  1.00 31.80 ? 152 TYR C C   1 
ATOM   4904 O O   . TYR C 1 152 ? 15.368  -35.791 31.471  1.00 31.53 ? 152 TYR C O   1 
ATOM   4905 C CB  . TYR C 1 152 ? 18.174  -37.289 31.221  1.00 30.60 ? 152 TYR C CB  1 
ATOM   4906 C CG  . TYR C 1 152 ? 18.559  -38.716 31.546  1.00 31.42 ? 152 TYR C CG  1 
ATOM   4907 C CD1 . TYR C 1 152 ? 17.816  -39.455 32.460  1.00 31.58 ? 152 TYR C CD1 1 
ATOM   4908 C CD2 . TYR C 1 152 ? 19.629  -39.338 30.908  1.00 33.85 ? 152 TYR C CD2 1 
ATOM   4909 C CE1 . TYR C 1 152 ? 18.140  -40.773 32.749  1.00 34.61 ? 152 TYR C CE1 1 
ATOM   4910 C CE2 . TYR C 1 152 ? 19.951  -40.656 31.191  1.00 36.88 ? 152 TYR C CE2 1 
ATOM   4911 C CZ  . TYR C 1 152 ? 19.195  -41.365 32.114  1.00 36.07 ? 152 TYR C CZ  1 
ATOM   4912 O OH  . TYR C 1 152 ? 19.501  -42.661 32.424  1.00 34.32 ? 152 TYR C OH  1 
ATOM   4913 N N   . LEU C 1 153 ? 16.294  -35.015 29.581  1.00 33.58 ? 153 LEU C N   1 
ATOM   4914 C CA  . LEU C 1 153 ? 15.446  -33.823 29.595  1.00 33.37 ? 153 LEU C CA  1 
ATOM   4915 C C   . LEU C 1 153 ? 13.969  -34.174 29.350  1.00 40.39 ? 153 LEU C C   1 
ATOM   4916 O O   . LEU C 1 153 ? 13.066  -33.518 29.908  1.00 36.32 ? 153 LEU C O   1 
ATOM   4917 C CB  . LEU C 1 153 ? 15.949  -32.818 28.557  1.00 32.76 ? 153 LEU C CB  1 
ATOM   4918 C CG  . LEU C 1 153 ? 17.166  -31.918 28.876  1.00 32.78 ? 153 LEU C CG  1 
ATOM   4919 C CD1 . LEU C 1 153 ? 17.482  -30.997 27.699  1.00 33.36 ? 153 LEU C CD1 1 
ATOM   4920 C CD2 . LEU C 1 153 ? 16.959  -31.057 30.108  1.00 28.76 ? 153 LEU C CD2 1 
ATOM   4921 N N   . LYS C 1 154 ? 13.699  -35.213 28.552  1.00 36.94 ? 154 LYS C N   1 
ATOM   4922 C CA  . LYS C 1 154 ? 12.319  -35.618 28.331  1.00 37.89 ? 154 LYS C CA  1 
ATOM   4923 C C   . LYS C 1 154 ? 11.701  -36.119 29.618  1.00 40.45 ? 154 LYS C C   1 
ATOM   4924 O O   . LYS C 1 154 ? 10.532  -35.838 29.914  1.00 38.63 ? 154 LYS C O   1 
ATOM   4925 C CB  . LYS C 1 154 ? 12.247  -36.724 27.276  1.00 41.06 ? 154 LYS C CB  1 
ATOM   4926 C CG  . LYS C 1 154 ? 11.056  -37.741 27.503  1.00 44.37 ? 154 LYS C CG  1 
ATOM   4927 C CD  . LYS C 1 154 ? 11.472  -39.227 27.267  1.00 47.72 ? 154 LYS C CD  1 
ATOM   4928 C CE  . LYS C 1 154 ? 10.484  -40.263 27.867  1.00 43.26 ? 154 LYS C CE  1 
ATOM   4929 N NZ  . LYS C 1 154 ? 10.528  -40.505 29.361  1.00 40.69 ? 154 LYS C NZ  1 
ATOM   4930 N N   . LYS C 1 155 ? 12.497  -36.798 30.436  1.00 39.39 ? 155 LYS C N   1 
ATOM   4931 C CA  . LYS C 1 155 ? 11.984  -37.318 31.691  1.00 39.30 ? 155 LYS C CA  1 
ATOM   4932 C C   . LYS C 1 155 ? 11.715  -36.213 32.700  1.00 38.84 ? 155 LYS C C   1 
ATOM   4933 O O   . LYS C 1 155 ? 11.201  -36.504 33.779  1.00 42.47 ? 155 LYS C O   1 
ATOM   4934 C CB  . LYS C 1 155 ? 13.004  -38.321 32.259  1.00 34.73 ? 155 LYS C CB  1 
ATOM   4935 C CG  . LYS C 1 155 ? 13.029  -39.680 31.574  1.00 36.92 ? 155 LYS C CG  1 
ATOM   4936 C CD  . LYS C 1 155 ? 13.829  -40.683 32.384  1.00 37.65 ? 155 LYS C CD  1 
ATOM   4937 C CE  . LYS C 1 155 ? 13.902  -42.082 31.709  1.00 46.41 ? 155 LYS C CE  1 
ATOM   4938 N NZ  . LYS C 1 155 ? 12.978  -42.280 30.537  1.00 46.80 ? 155 LYS C NZ  1 
ATOM   4939 N N   . GLY C 1 156 ? 12.050  -34.965 32.375  1.00 37.60 ? 156 GLY C N   1 
ATOM   4940 C CA  . GLY C 1 156 ? 11.911  -33.850 33.291  1.00 37.25 ? 156 GLY C CA  1 
ATOM   4941 C C   . GLY C 1 156 ? 13.126  -33.552 34.146  1.00 34.84 ? 156 GLY C C   1 
ATOM   4942 O O   . GLY C 1 156 ? 13.006  -32.766 35.091  1.00 32.20 ? 156 GLY C O   1 
ATOM   4943 N N   . PHE C 1 157 ? 14.293  -34.168 33.859  1.00 29.37 ? 157 PHE C N   1 
ATOM   4944 C CA  . PHE C 1 157 ? 15.452  -34.037 34.725  1.00 29.87 ? 157 PHE C CA  1 
ATOM   4945 C C   . PHE C 1 157 ? 16.493  -33.139 34.061  1.00 28.81 ? 157 PHE C C   1 
ATOM   4946 O O   . PHE C 1 157 ? 16.949  -33.452 32.949  1.00 25.33 ? 157 PHE C O   1 
ATOM   4947 C CB  . PHE C 1 157 ? 16.088  -35.400 35.062  1.00 30.66 ? 157 PHE C CB  1 
ATOM   4948 C CG  . PHE C 1 157 ? 15.126  -36.430 35.608  1.00 31.10 ? 157 PHE C CG  1 
ATOM   4949 C CD1 . PHE C 1 157 ? 13.955  -36.037 36.279  1.00 33.01 ? 157 PHE C CD1 1 
ATOM   4950 C CD2 . PHE C 1 157 ? 15.401  -37.794 35.459  1.00 32.05 ? 157 PHE C CD2 1 
ATOM   4951 C CE1 . PHE C 1 157 ? 13.051  -37.009 36.783  1.00 34.29 ? 157 PHE C CE1 1 
ATOM   4952 C CE2 . PHE C 1 157 ? 14.534  -38.759 35.953  1.00 31.16 ? 157 PHE C CE2 1 
ATOM   4953 C CZ  . PHE C 1 157 ? 13.356  -38.368 36.627  1.00 31.37 ? 157 PHE C CZ  1 
ATOM   4954 N N   . PRO C 1 158 ? 16.920  -32.046 34.684  1.00 25.84 ? 158 PRO C N   1 
ATOM   4955 C CA  . PRO C 1 158 ? 17.985  -31.226 34.079  1.00 27.37 ? 158 PRO C CA  1 
ATOM   4956 C C   . PRO C 1 158 ? 19.353  -31.893 34.245  1.00 23.76 ? 158 PRO C C   1 
ATOM   4957 O O   . PRO C 1 158 ? 19.522  -32.863 34.992  1.00 26.03 ? 158 PRO C O   1 
ATOM   4958 C CB  . PRO C 1 158 ? 17.911  -29.903 34.852  1.00 24.71 ? 158 PRO C CB  1 
ATOM   4959 C CG  . PRO C 1 158 ? 17.513  -30.361 36.227  1.00 28.28 ? 158 PRO C CG  1 
ATOM   4960 C CD  . PRO C 1 158 ? 16.555  -31.576 36.027  1.00 24.01 ? 158 PRO C CD  1 
ATOM   4961 N N   . VAL C 1 159 ? 20.351  -31.362 33.540  1.00 23.32 ? 159 VAL C N   1 
ATOM   4962 C CA  . VAL C 1 159 ? 21.655  -32.044 33.462  1.00 22.77 ? 159 VAL C CA  1 
ATOM   4963 C C   . VAL C 1 159 ? 22.765  -31.059 33.782  1.00 20.39 ? 159 VAL C C   1 
ATOM   4964 O O   . VAL C 1 159 ? 23.017  -30.135 33.009  1.00 22.38 ? 159 VAL C O   1 
ATOM   4965 C CB  . VAL C 1 159 ? 21.886  -32.682 32.084  1.00 24.58 ? 159 VAL C CB  1 
ATOM   4966 C CG1 . VAL C 1 159 ? 23.287  -33.275 31.975  1.00 21.85 ? 159 VAL C CG1 1 
ATOM   4967 C CG2 . VAL C 1 159 ? 20.797  -33.750 31.808  1.00 26.19 ? 159 VAL C CG2 1 
ATOM   4968 N N   . ILE C 1 160 ? 23.454  -31.272 34.904  1.00 19.61 ? 160 ILE C N   1 
ATOM   4969 C CA  . ILE C 1 160 ? 24.597  -30.453 35.253  1.00 20.49 ? 160 ILE C CA  1 
ATOM   4970 C C   . ILE C 1 160 ? 25.777  -30.813 34.351  1.00 22.97 ? 160 ILE C C   1 
ATOM   4971 O O   . ILE C 1 160 ? 26.080  -32.000 34.139  1.00 23.38 ? 160 ILE C O   1 
ATOM   4972 C CB  . ILE C 1 160 ? 24.947  -30.644 36.734  1.00 20.91 ? 160 ILE C CB  1 
ATOM   4973 C CG1 . ILE C 1 160 ? 23.927  -29.923 37.638  1.00 21.62 ? 160 ILE C CG1 1 
ATOM   4974 C CG2 . ILE C 1 160 ? 26.430  -30.152 36.977  1.00 21.42 ? 160 ILE C CG2 1 
ATOM   4975 C CD1 . ILE C 1 160 ? 24.069  -30.208 39.174  1.00 20.50 ? 160 ILE C CD1 1 
ATOM   4976 N N   . CYS C 1 161 ? 26.406  -29.799 33.774  1.00 21.47 ? 161 CYS C N   1 
ATOM   4977 C CA  . CYS C 1 161 ? 27.554  -29.950 32.887  1.00 21.38 ? 161 CYS C CA  1 
ATOM   4978 C C   . CYS C 1 161 ? 28.782  -29.335 33.540  1.00 27.02 ? 161 CYS C C   1 
ATOM   4979 O O   . CYS C 1 161 ? 28.663  -28.452 34.403  1.00 24.67 ? 161 CYS C O   1 
ATOM   4980 C CB  . CYS C 1 161 ? 27.305  -29.314 31.519  1.00 23.60 ? 161 CYS C CB  1 
ATOM   4981 S SG  . CYS C 1 161 ? 26.885  -27.496 31.526  1.00 24.57 ? 161 CYS C SG  1 
ATOM   4982 N N   . HIS C 1 162 ? 29.959  -29.845 33.136  1.00 25.58 ? 162 HIS C N   1 
ATOM   4983 C CA  . HIS C 1 162 ? 31.266  -29.510 33.698  1.00 26.17 ? 162 HIS C CA  1 
ATOM   4984 C C   . HIS C 1 162 ? 32.234  -29.360 32.548  1.00 25.55 ? 162 HIS C C   1 
ATOM   4985 O O   . HIS C 1 162 ? 32.307  -30.250 31.699  1.00 27.08 ? 162 HIS C O   1 
ATOM   4986 C CB  . HIS C 1 162 ? 31.757  -30.617 34.636  1.00 27.04 ? 162 HIS C CB  1 
ATOM   4987 C CG  . HIS C 1 162 ? 33.089  -30.352 35.262  1.00 30.68 ? 162 HIS C CG  1 
ATOM   4988 N ND1 . HIS C 1 162 ? 34.017  -31.353 35.493  1.00 30.01 ? 162 HIS C ND1 1 
ATOM   4989 C CD2 . HIS C 1 162 ? 33.637  -29.213 35.748  1.00 28.24 ? 162 HIS C CD2 1 
ATOM   4990 C CE1 . HIS C 1 162 ? 35.084  -30.828 36.070  1.00 31.81 ? 162 HIS C CE1 1 
ATOM   4991 N NE2 . HIS C 1 162 ? 34.878  -29.534 36.234  1.00 31.11 ? 162 HIS C NE2 1 
ATOM   4992 N N   . TRP C 1 163 ? 32.981  -28.253 32.526  1.00 25.10 ? 163 TRP C N   1 
ATOM   4993 C CA  . TRP C 1 163 ? 33.926  -28.044 31.444  1.00 28.42 ? 163 TRP C CA  1 
ATOM   4994 C C   . TRP C 1 163 ? 35.004  -27.060 31.887  1.00 31.17 ? 163 TRP C C   1 
ATOM   4995 O O   . TRP C 1 163 ? 34.873  -26.390 32.914  1.00 27.99 ? 163 TRP C O   1 
ATOM   4996 C CB  . TRP C 1 163 ? 33.202  -27.591 30.174  1.00 27.18 ? 163 TRP C CB  1 
ATOM   4997 C CG  . TRP C 1 163 ? 32.804  -26.138 30.122  1.00 28.69 ? 163 TRP C CG  1 
ATOM   4998 C CD1 . TRP C 1 163 ? 33.439  -25.137 29.417  1.00 31.29 ? 163 TRP C CD1 1 
ATOM   4999 C CD2 . TRP C 1 163 ? 31.669  -25.518 30.761  1.00 27.00 ? 163 TRP C CD2 1 
ATOM   5000 N NE1 . TRP C 1 163 ? 32.767  -23.941 29.576  1.00 29.91 ? 163 TRP C NE1 1 
ATOM   5001 C CE2 . TRP C 1 163 ? 31.683  -24.141 30.396  1.00 27.20 ? 163 TRP C CE2 1 
ATOM   5002 C CE3 . TRP C 1 163 ? 30.660  -25.983 31.612  1.00 27.45 ? 163 TRP C CE3 1 
ATOM   5003 C CZ2 . TRP C 1 163 ? 30.704  -23.217 30.848  1.00 26.97 ? 163 TRP C CZ2 1 
ATOM   5004 C CZ3 . TRP C 1 163 ? 29.642  -25.055 32.060  1.00 23.46 ? 163 TRP C CZ3 1 
ATOM   5005 C CH2 . TRP C 1 163 ? 29.702  -23.696 31.685  1.00 28.24 ? 163 TRP C CH2 1 
ATOM   5006 N N   . GLN C 1 164 ? 36.103  -27.020 31.116  1.00 30.29 ? 164 GLN C N   1 
ATOM   5007 C CA  . GLN C 1 164 ? 37.204  -26.074 31.330  1.00 29.69 ? 164 GLN C CA  1 
ATOM   5008 C C   . GLN C 1 164 ? 37.009  -24.915 30.355  1.00 34.00 ? 164 GLN C C   1 
ATOM   5009 O O   . GLN C 1 164 ? 36.982  -25.137 29.138  1.00 34.92 ? 164 GLN C O   1 
ATOM   5010 C CB  . GLN C 1 164 ? 38.552  -26.761 31.122  1.00 34.78 ? 164 GLN C CB  1 
ATOM   5011 C CG  . GLN C 1 164 ? 38.635  -28.114 31.768  1.00 32.30 ? 164 GLN C CG  1 
ATOM   5012 C CD  . GLN C 1 164 ? 38.724  -28.040 33.277  1.00 32.83 ? 164 GLN C CD  1 
ATOM   5013 O OE1 . GLN C 1 164 ? 39.417  -27.186 33.829  1.00 32.04 ? 164 GLN C OE1 1 
ATOM   5014 N NE2 . GLN C 1 164 ? 37.953  -28.900 33.967  1.00 30.87 ? 164 GLN C NE2 1 
ATOM   5015 N N   . VAL C 1 165 ? 36.715  -23.728 30.895  1.00 35.36 ? 165 VAL C N   1 
ATOM   5016 C CA  . VAL C 1 165 ? 36.271  -22.573 30.049  1.00 34.54 ? 165 VAL C CA  1 
ATOM   5017 C C   . VAL C 1 165 ? 37.297  -22.232 28.982  1.00 35.48 ? 165 VAL C C   1 
ATOM   5018 O O   . VAL C 1 165 ? 36.890  -21.763 27.939  1.00 36.12 ? 165 VAL C O   1 
ATOM   5019 C CB  . VAL C 1 165 ? 35.844  -21.335 30.853  1.00 29.85 ? 165 VAL C CB  1 
ATOM   5020 C CG1 . VAL C 1 165 ? 34.786  -21.679 31.873  1.00 31.35 ? 165 VAL C CG1 1 
ATOM   5021 C CG2 . VAL C 1 165 ? 37.026  -20.658 31.497  1.00 33.78 ? 165 VAL C CG2 1 
ATOM   5022 N N   . ASN C 1 166 ? 38.572  -22.509 29.235  1.00 40.19 ? 166 ASN C N   1 
ATOM   5023 C CA  . ASN C 1 166 ? 39.619  -22.257 28.203  1.00 40.85 ? 166 ASN C CA  1 
ATOM   5024 C C   . ASN C 1 166 ? 39.349  -23.098 26.943  1.00 44.98 ? 166 ASN C C   1 
ATOM   5025 O O   . ASN C 1 166 ? 39.561  -22.586 25.853  1.00 47.54 ? 166 ASN C O   1 
ATOM   5026 C CB  . ASN C 1 166 ? 41.032  -22.376 28.768  1.00 45.28 ? 166 ASN C CB  1 
ATOM   5027 C CG  . ASN C 1 166 ? 41.244  -23.588 29.645  1.00 49.12 ? 166 ASN C CG  1 
ATOM   5028 O OD1 . ASN C 1 166 ? 40.938  -23.565 30.828  1.00 51.29 ? 166 ASN C OD1 1 
ATOM   5029 N ND2 . ASN C 1 166 ? 41.786  -24.644 29.078  1.00 48.01 ? 166 ASN C ND2 1 
ATOM   5030 N N   . GLN C 1 167 ? 38.849  -24.325 27.087  1.00 41.01 ? 167 GLN C N   1 
ATOM   5031 C CA  . GLN C 1 167 ? 38.585  -25.211 25.931  1.00 36.55 ? 167 GLN C CA  1 
ATOM   5032 C C   . GLN C 1 167 ? 37.351  -24.770 25.143  1.00 39.00 ? 167 GLN C C   1 
ATOM   5033 O O   . GLN C 1 167 ? 37.131  -25.357 24.143  1.00 40.20 ? 167 GLN C O   1 
ATOM   5034 C CB  . GLN C 1 167 ? 38.518  -26.676 26.361  1.00 39.59 ? 167 GLN C CB  1 
ATOM   5035 C CG  . GLN C 1 167 ? 39.591  -27.100 27.349  1.00 39.05 ? 167 GLN C CG  1 
ATOM   5036 C CD  . GLN C 1 167 ? 39.706  -28.600 27.503  1.00 37.96 ? 167 GLN C CD  1 
ATOM   5037 O OE1 . GLN C 1 167 ? 39.159  -29.368 26.738  1.00 35.09 ? 167 GLN C OE1 1 
ATOM   5038 N NE2 . GLN C 1 167 ? 40.422  -29.025 28.522  1.00 34.53 ? 167 GLN C NE2 1 
ATOM   5039 N N   . SER C 1 168 ? 36.566  -23.804 25.618  1.00 38.46 ? 168 SER C N   1 
ATOM   5040 C CA  . SER C 1 168 ? 35.420  -23.309 24.887  1.00 42.71 ? 168 SER C CA  1 
ATOM   5041 C C   . SER C 1 168 ? 35.698  -21.944 24.267  1.00 44.30 ? 168 SER C C   1 
ATOM   5042 O O   . SER C 1 168 ? 34.839  -21.446 23.519  1.00 46.01 ? 168 SER C O   1 
ATOM   5043 C CB  . SER C 1 168 ? 34.181  -23.230 25.803  1.00 37.83 ? 168 SER C CB  1 
ATOM   5044 O OG  . SER C 1 168 ? 34.523  -22.733 27.097  1.00 37.94 ? 168 SER C OG  1 
ATOM   5045 N N   . ARG C 1 169 ? 36.903  -21.373 24.493  1.00 43.57 ? 169 ARG C N   1 
ATOM   5046 C CA  . ARG C 1 169 ? 37.230  -20.016 24.032  1.00 46.14 ? 169 ARG C CA  1 
ATOM   5047 C C   . ARG C 1 169 ? 36.903  -19.797 22.554  1.00 48.29 ? 169 ARG C C   1 
ATOM   5048 O O   . ARG C 1 169 ? 36.267  -18.798 22.199  1.00 48.01 ? 169 ARG C O   1 
ATOM   5049 C CB  . ARG C 1 169 ? 38.696  -19.699 24.311  1.00 47.83 ? 169 ARG C CB  1 
ATOM   5050 C CG  . ARG C 1 169 ? 39.264  -18.614 23.408  1.00 53.12 ? 169 ARG C CG  1 
ATOM   5051 C CD  . ARG C 1 169 ? 39.478  -17.274 24.089  1.00 53.57 ? 169 ARG C CD  1 
ATOM   5052 N NE  . ARG C 1 169 ? 39.966  -16.313 23.103  1.00 59.34 ? 169 ARG C NE  1 
ATOM   5053 C CZ  . ARG C 1 169 ? 40.473  -15.117 23.377  1.00 62.89 ? 169 ARG C CZ  1 
ATOM   5054 N NH1 . ARG C 1 169 ? 40.631  -14.701 24.625  1.00 59.29 ? 169 ARG C NH1 1 
ATOM   5055 N NH2 . ARG C 1 169 ? 40.855  -14.327 22.372  1.00 62.26 ? 169 ARG C NH2 1 
ATOM   5056 N N   . ASN C 1 170 ? 37.317  -20.712 21.670  1.00 47.18 ? 170 ASN C N   1 
ATOM   5057 C CA  . ASN C 1 170 ? 37.069  -20.461 20.253  1.00 48.07 ? 170 ASN C CA  1 
ATOM   5058 C C   . ASN C 1 170 ? 35.709  -20.934 19.778  1.00 48.75 ? 170 ASN C C   1 
ATOM   5059 O O   . ASN C 1 170 ? 35.125  -20.297 18.890  1.00 54.32 ? 170 ASN C O   1 
ATOM   5060 C CB  . ASN C 1 170 ? 38.144  -21.122 19.386  1.00 50.44 ? 170 ASN C CB  1 
ATOM   5061 C CG  . ASN C 1 170 ? 39.520  -20.523 19.600  1.00 56.21 ? 170 ASN C CG  1 
ATOM   5062 O OD1 . ASN C 1 170 ? 39.700  -19.561 20.358  1.00 57.95 ? 170 ASN C OD1 1 
ATOM   5063 N ND2 . ASN C 1 170 ? 40.508  -21.085 18.918  1.00 63.00 ? 170 ASN C ND2 1 
ATOM   5064 N N   . CYS C 1 171 ? 35.129  -21.964 20.400  1.00 45.78 ? 171 CYS C N   1 
ATOM   5065 C CA  . CYS C 1 171 ? 33.833  -22.459 19.940  1.00 43.19 ? 171 CYS C CA  1 
ATOM   5066 C C   . CYS C 1 171 ? 32.668  -21.823 20.686  1.00 43.28 ? 171 CYS C C   1 
ATOM   5067 O O   . CYS C 1 171 ? 31.504  -22.010 20.302  1.00 45.62 ? 171 CYS C O   1 
ATOM   5068 C CB  . CYS C 1 171 ? 33.778  -24.003 20.047  1.00 44.98 ? 171 CYS C CB  1 
ATOM   5069 S SG  . CYS C 1 171 ? 34.081  -24.717 21.705  1.00 44.72 ? 171 CYS C SG  1 
ATOM   5070 N N   . LYS C 1 172 ? 32.945  -21.017 21.699  1.00 45.29 ? 172 LYS C N   1 
ATOM   5071 C CA  . LYS C 1 172 ? 31.861  -20.279 22.343  1.00 43.11 ? 172 LYS C CA  1 
ATOM   5072 C C   . LYS C 1 172 ? 32.298  -18.824 22.545  1.00 40.93 ? 172 LYS C C   1 
ATOM   5073 O O   . LYS C 1 172 ? 31.667  -17.903 22.005  1.00 39.32 ? 172 LYS C O   1 
ATOM   5074 C CB  . LYS C 1 172 ? 31.471  -20.950 23.667  1.00 37.82 ? 172 LYS C CB  1 
ATOM   5075 C CG  . LYS C 1 172 ? 30.503  -20.091 24.516  1.00 41.48 ? 172 LYS C CG  1 
ATOM   5076 C CD  . LYS C 1 172 ? 29.173  -19.943 23.868  1.00 38.92 ? 172 LYS C CD  1 
ATOM   5077 C CE  . LYS C 1 172 ? 28.373  -18.874 24.589  1.00 37.44 ? 172 LYS C CE  1 
ATOM   5078 N NZ  . LYS C 1 172 ? 27.298  -18.338 23.752  1.00 39.44 ? 172 LYS C NZ  1 
ATOM   5079 N N   . GLY C 1 173 ? 33.386  -18.596 23.277  1.00 40.28 ? 173 GLY C N   1 
ATOM   5080 C CA  . GLY C 1 173 ? 33.881  -17.243 23.464  1.00 41.31 ? 173 GLY C CA  1 
ATOM   5081 C C   . GLY C 1 173 ? 33.342  -16.444 24.637  1.00 44.18 ? 173 GLY C C   1 
ATOM   5082 O O   . GLY C 1 173 ? 33.183  -15.220 24.516  1.00 47.43 ? 173 GLY C O   1 
ATOM   5083 N N   . ASP C 1 174 ? 32.947  -17.099 25.725  1.00 40.95 ? 174 ASP C N   1 
ATOM   5084 C CA  . ASP C 1 174 ? 32.408  -16.408 26.898  1.00 39.53 ? 174 ASP C CA  1 
ATOM   5085 C C   . ASP C 1 174 ? 33.507  -16.009 27.876  1.00 38.92 ? 174 ASP C C   1 
ATOM   5086 O O   . ASP C 1 174 ? 33.321  -15.079 28.665  1.00 37.88 ? 174 ASP C O   1 
ATOM   5087 C CB  . ASP C 1 174 ? 31.374  -17.298 27.620  1.00 38.26 ? 174 ASP C CB  1 
ATOM   5088 C CG  . ASP C 1 174 ? 29.939  -16.975 27.250  1.00 37.83 ? 174 ASP C CG  1 
ATOM   5089 O OD1 . ASP C 1 174 ? 29.712  -16.317 26.215  1.00 42.16 ? 174 ASP C OD1 1 
ATOM   5090 O OD2 . ASP C 1 174 ? 29.000  -17.444 27.976  1.00 38.64 ? 174 ASP C OD2 1 
ATOM   5091 N N   . TYR C 1 175 ? 34.607  -16.759 27.905  1.00 31.57 ? 175 TYR C N   1 
ATOM   5092 C CA  . TYR C 1 175 ? 35.625  -16.653 28.943  1.00 35.96 ? 175 TYR C CA  1 
ATOM   5093 C C   . TYR C 1 175 ? 37.004  -16.459 28.325  1.00 36.42 ? 175 TYR C C   1 
ATOM   5094 O O   . TYR C 1 175 ? 37.254  -16.901 27.201  1.00 38.39 ? 175 TYR C O   1 
ATOM   5095 C CB  . TYR C 1 175 ? 35.645  -17.894 29.848  1.00 35.16 ? 175 TYR C CB  1 
ATOM   5096 C CG  . TYR C 1 175 ? 34.374  -18.076 30.646  1.00 32.44 ? 175 TYR C CG  1 
ATOM   5097 C CD1 . TYR C 1 175 ? 34.207  -17.425 31.878  1.00 32.90 ? 175 TYR C CD1 1 
ATOM   5098 C CD2 . TYR C 1 175 ? 33.336  -18.883 30.167  1.00 32.05 ? 175 TYR C CD2 1 
ATOM   5099 C CE1 . TYR C 1 175 ? 33.024  -17.560 32.618  1.00 30.09 ? 175 TYR C CE1 1 
ATOM   5100 C CE2 . TYR C 1 175 ? 32.145  -19.036 30.899  1.00 30.67 ? 175 TYR C CE2 1 
ATOM   5101 C CZ  . TYR C 1 175 ? 31.999  -18.370 32.118  1.00 30.84 ? 175 TYR C CZ  1 
ATOM   5102 O OH  . TYR C 1 175 ? 30.850  -18.534 32.866  1.00 30.58 ? 175 TYR C OH  1 
ATOM   5103 N N   . THR C 1 176 ? 37.906  -15.838 29.073  1.00 35.84 ? 176 THR C N   1 
ATOM   5104 C CA  . THR C 1 176 ? 39.301  -15.650 28.617  1.00 35.84 ? 176 THR C CA  1 
ATOM   5105 C C   . THR C 1 176 ? 40.246  -16.265 29.650  1.00 37.07 ? 176 THR C C   1 
ATOM   5106 O O   . THR C 1 176 ? 41.429  -16.336 29.377  1.00 35.90 ? 176 THR C O   1 
ATOM   5107 C CB  . THR C 1 176 ? 39.643  -14.176 28.358  1.00 33.35 ? 176 THR C CB  1 
ATOM   5108 O OG1 . THR C 1 176 ? 39.623  -13.442 29.575  1.00 30.18 ? 176 THR C OG1 1 
ATOM   5109 C CG2 . THR C 1 176 ? 38.755  -13.507 27.344  1.00 27.32 ? 176 THR C CG2 1 
ATOM   5110 N N   . GLY C 1 177 ? 39.716  -16.687 30.790  1.00 35.19 ? 177 GLY C N   1 
ATOM   5111 C CA  . GLY C 1 177 ? 40.535  -17.259 31.870  1.00 39.18 ? 177 GLY C CA  1 
ATOM   5112 C C   . GLY C 1 177 ? 40.743  -18.757 31.742  1.00 42.70 ? 177 GLY C C   1 
ATOM   5113 O O   . GLY C 1 177 ? 40.332  -19.319 30.730  1.00 39.04 ? 177 GLY C O   1 
ATOM   5114 N N   . ASN C 1 178 ? 41.346  -19.345 32.771  1.00 40.69 ? 178 ASN C N   1 
ATOM   5115 C CA  . ASN C 1 178 ? 41.629  -20.794 32.816  1.00 42.94 ? 178 ASN C CA  1 
ATOM   5116 C C   . ASN C 1 178 ? 41.184  -21.363 34.156  1.00 43.32 ? 178 ASN C C   1 
ATOM   5117 O O   . ASN C 1 178 ? 41.851  -21.126 35.163  1.00 44.39 ? 178 ASN C O   1 
ATOM   5118 C CB  . ASN C 1 178 ? 43.098  -21.113 32.578  1.00 51.58 ? 178 ASN C CB  1 
ATOM   5119 C CG  . ASN C 1 178 ? 43.396  -21.313 31.116  1.00 51.73 ? 178 ASN C CG  1 
ATOM   5120 O OD1 . ASN C 1 178 ? 42.507  -21.631 30.335  1.00 58.51 ? 178 ASN C OD1 1 
ATOM   5121 N ND2 . ASN C 1 178 ? 44.639  -21.097 30.734  1.00 55.97 ? 178 ASN C ND2 1 
ATOM   5122 N N   . PHE C 1 179 ? 40.072  -22.081 34.128  1.00 36.71 ? 179 PHE C N   1 
ATOM   5123 C CA  . PHE C 1 179 ? 39.524  -22.754 35.321  1.00 32.49 ? 179 PHE C CA  1 
ATOM   5124 C C   . PHE C 1 179 ? 38.406  -23.684 34.877  1.00 32.18 ? 179 PHE C C   1 
ATOM   5125 O O   . PHE C 1 179 ? 37.897  -23.535 33.778  1.00 32.63 ? 179 PHE C O   1 
ATOM   5126 C CB  . PHE C 1 179 ? 38.947  -21.774 36.347  1.00 34.29 ? 179 PHE C CB  1 
ATOM   5127 C CG  . PHE C 1 179 ? 38.094  -20.666 35.793  1.00 36.60 ? 179 PHE C CG  1 
ATOM   5128 C CD1 . PHE C 1 179 ? 38.648  -19.468 35.395  1.00 34.83 ? 179 PHE C CD1 1 
ATOM   5129 C CD2 . PHE C 1 179 ? 36.726  -20.810 35.699  1.00 33.45 ? 179 PHE C CD2 1 
ATOM   5130 C CE1 . PHE C 1 179 ? 37.859  -18.449 34.903  1.00 34.26 ? 179 PHE C CE1 1 
ATOM   5131 C CE2 . PHE C 1 179 ? 35.937  -19.791 35.203  1.00 33.40 ? 179 PHE C CE2 1 
ATOM   5132 C CZ  . PHE C 1 179 ? 36.506  -18.613 34.803  1.00 36.69 ? 179 PHE C CZ  1 
ATOM   5133 N N   . GLY C 1 180 ? 38.140  -24.675 35.708  1.00 28.91 ? 180 GLY C N   1 
ATOM   5134 C CA  . GLY C 1 180 ? 36.975  -25.532 35.485  1.00 29.44 ? 180 GLY C CA  1 
ATOM   5135 C C   . GLY C 1 180 ? 35.666  -24.861 35.965  1.00 28.27 ? 180 GLY C C   1 
ATOM   5136 O O   . GLY C 1 180 ? 35.661  -24.010 36.855  1.00 26.42 ? 180 GLY C O   1 
ATOM   5137 N N   . HIS C 1 181 ? 34.544  -25.274 35.389  1.00 27.20 ? 181 HIS C N   1 
ATOM   5138 C CA  . HIS C 1 181 ? 33.274  -24.571 35.620  1.00 26.01 ? 181 HIS C CA  1 
ATOM   5139 C C   . HIS C 1 181 ? 32.101  -25.537 35.460  1.00 25.68 ? 181 HIS C C   1 
ATOM   5140 O O   . HIS C 1 181 ? 32.210  -26.566 34.776  1.00 26.97 ? 181 HIS C O   1 
ATOM   5141 C CB  . HIS C 1 181 ? 33.119  -23.404 34.647  1.00 23.29 ? 181 HIS C CB  1 
ATOM   5142 C CG  . HIS C 1 181 ? 32.097  -22.381 35.060  1.00 27.03 ? 181 HIS C CG  1 
ATOM   5143 N ND1 . HIS C 1 181 ? 31.959  -21.945 36.359  1.00 28.62 ? 181 HIS C ND1 1 
ATOM   5144 C CD2 . HIS C 1 181 ? 31.177  -21.699 34.337  1.00 26.18 ? 181 HIS C CD2 1 
ATOM   5145 C CE1 . HIS C 1 181 ? 31.000  -21.029 36.420  1.00 29.40 ? 181 HIS C CE1 1 
ATOM   5146 N NE2 . HIS C 1 181 ? 30.521  -20.850 35.202  1.00 28.18 ? 181 HIS C NE2 1 
ATOM   5147 N N   . TYR C 1 182 ? 30.994  -25.221 36.158  1.00 23.19 ? 182 TYR C N   1 
ATOM   5148 C CA  . TYR C 1 182 ? 29.744  -25.977 36.098  1.00 25.34 ? 182 TYR C CA  1 
ATOM   5149 C C   . TYR C 1 182 ? 28.609  -25.056 35.668  1.00 25.47 ? 182 TYR C C   1 
ATOM   5150 O O   . TYR C 1 182 ? 28.597  -23.860 35.997  1.00 23.15 ? 182 TYR C O   1 
ATOM   5151 C CB  . TYR C 1 182 ? 29.346  -26.569 37.452  1.00 23.96 ? 182 TYR C CB  1 
ATOM   5152 C CG  . TYR C 1 182 ? 30.225  -27.678 38.009  1.00 27.56 ? 182 TYR C CG  1 
ATOM   5153 C CD1 . TYR C 1 182 ? 31.324  -27.377 38.823  1.00 26.37 ? 182 TYR C CD1 1 
ATOM   5154 C CD2 . TYR C 1 182 ? 29.925  -29.025 37.771  1.00 27.81 ? 182 TYR C CD2 1 
ATOM   5155 C CE1 . TYR C 1 182 ? 32.088  -28.370 39.360  1.00 28.02 ? 182 TYR C CE1 1 
ATOM   5156 C CE2 . TYR C 1 182 ? 30.723  -30.035 38.314  1.00 25.67 ? 182 TYR C CE2 1 
ATOM   5157 C CZ  . TYR C 1 182 ? 31.785  -29.700 39.104  1.00 26.74 ? 182 TYR C CZ  1 
ATOM   5158 O OH  . TYR C 1 182 ? 32.599  -30.691 39.661  1.00 29.23 ? 182 TYR C OH  1 
ATOM   5159 N N   . GLY C 1 183 ? 27.633  -25.628 34.964  1.00 24.06 ? 183 GLY C N   1 
ATOM   5160 C CA  . GLY C 1 183 ? 26.384  -24.964 34.658  1.00 21.02 ? 183 GLY C CA  1 
ATOM   5161 C C   . GLY C 1 183 ? 25.317  -26.023 34.581  1.00 24.26 ? 183 GLY C C   1 
ATOM   5162 O O   . GLY C 1 183 ? 25.580  -27.212 34.831  1.00 23.10 ? 183 GLY C O   1 
ATOM   5163 N N   . LEU C 1 184 ? 24.097  -25.598 34.206  1.00 23.92 ? 184 LEU C N   1 
ATOM   5164 C CA  . LEU C 1 184 ? 22.941  -26.499 34.134  1.00 20.94 ? 184 LEU C CA  1 
ATOM   5165 C C   . LEU C 1 184 ? 22.366  -26.492 32.726  1.00 23.09 ? 184 LEU C C   1 
ATOM   5166 O O   . LEU C 1 184 ? 21.869  -25.455 32.268  1.00 24.47 ? 184 LEU C O   1 
ATOM   5167 C CB  . LEU C 1 184 ? 21.837  -26.099 35.130  1.00 21.40 ? 184 LEU C CB  1 
ATOM   5168 C CG  . LEU C 1 184 ? 20.663  -27.108 35.165  1.00 23.09 ? 184 LEU C CG  1 
ATOM   5169 C CD1 . LEU C 1 184 ? 21.114  -28.413 35.931  1.00 21.56 ? 184 LEU C CD1 1 
ATOM   5170 C CD2 . LEU C 1 184 ? 19.335  -26.490 35.726  1.00 22.95 ? 184 LEU C CD2 1 
ATOM   5171 N N   . ILE C 1 185 ? 22.385  -27.647 32.058  1.00 22.51 ? 185 ILE C N   1 
ATOM   5172 C CA  . ILE C 1 185 ? 21.656  -27.806 30.801  1.00 24.05 ? 185 ILE C CA  1 
ATOM   5173 C C   . ILE C 1 185 ? 20.186  -28.024 31.136  1.00 25.74 ? 185 ILE C C   1 
ATOM   5174 O O   . ILE C 1 185 ? 19.828  -28.995 31.810  1.00 23.66 ? 185 ILE C O   1 
ATOM   5175 C CB  . ILE C 1 185 ? 22.197  -28.962 29.952  1.00 25.65 ? 185 ILE C CB  1 
ATOM   5176 C CG1 . ILE C 1 185 ? 23.714  -28.852 29.707  1.00 24.39 ? 185 ILE C CG1 1 
ATOM   5177 C CG2 . ILE C 1 185 ? 21.509  -28.978 28.599  1.00 26.16 ? 185 ILE C CG2 1 
ATOM   5178 C CD1 . ILE C 1 185 ? 24.371  -30.184 29.210  1.00 25.64 ? 185 ILE C CD1 1 
ATOM   5179 N N   . TRP C 1 186 ? 19.331  -27.104 30.690  1.00 26.37 ? 186 TRP C N   1 
ATOM   5180 C CA  . TRP C 1 186 ? 17.911  -27.235 30.941  1.00 27.53 ? 186 TRP C CA  1 
ATOM   5181 C C   . TRP C 1 186 ? 17.092  -27.315 29.653  1.00 28.66 ? 186 TRP C C   1 
ATOM   5182 O O   . TRP C 1 186 ? 15.887  -27.561 29.716  1.00 30.14 ? 186 TRP C O   1 
ATOM   5183 C CB  . TRP C 1 186 ? 17.424  -26.076 31.830  1.00 27.02 ? 186 TRP C CB  1 
ATOM   5184 C CG  . TRP C 1 186 ? 17.605  -24.704 31.263  1.00 28.11 ? 186 TRP C CG  1 
ATOM   5185 C CD1 . TRP C 1 186 ? 18.716  -23.911 31.394  1.00 27.67 ? 186 TRP C CD1 1 
ATOM   5186 C CD2 . TRP C 1 186 ? 16.662  -23.958 30.475  1.00 27.30 ? 186 TRP C CD2 1 
ATOM   5187 N NE1 . TRP C 1 186 ? 18.516  -22.713 30.751  1.00 29.19 ? 186 TRP C NE1 1 
ATOM   5188 C CE2 . TRP C 1 186 ? 17.269  -22.711 30.174  1.00 28.56 ? 186 TRP C CE2 1 
ATOM   5189 C CE3 . TRP C 1 186 ? 15.354  -24.207 30.026  1.00 31.42 ? 186 TRP C CE3 1 
ATOM   5190 C CZ2 . TRP C 1 186 ? 16.629  -21.716 29.402  1.00 28.04 ? 186 TRP C CZ2 1 
ATOM   5191 C CZ3 . TRP C 1 186 ? 14.709  -23.222 29.259  1.00 28.86 ? 186 TRP C CZ3 1 
ATOM   5192 C CH2 . TRP C 1 186 ? 15.350  -21.999 28.959  1.00 34.18 ? 186 TRP C CH2 1 
ATOM   5193 N N   . ASP C 1 187 ? 17.720  -27.180 28.493  1.00 30.59 ? 187 ASP C N   1 
ATOM   5194 C CA  . ASP C 1 187 ? 17.013  -27.238 27.218  1.00 31.20 ? 187 ASP C CA  1 
ATOM   5195 C C   . ASP C 1 187 ? 18.031  -27.550 26.131  1.00 33.14 ? 187 ASP C C   1 
ATOM   5196 O O   . ASP C 1 187 ? 19.234  -27.409 26.345  1.00 29.49 ? 187 ASP C O   1 
ATOM   5197 C CB  . ASP C 1 187 ? 16.316  -25.916 26.934  1.00 29.65 ? 187 ASP C CB  1 
ATOM   5198 C CG  . ASP C 1 187 ? 15.223  -26.017 25.859  1.00 37.43 ? 187 ASP C CG  1 
ATOM   5199 O OD1 . ASP C 1 187 ? 14.707  -27.134 25.563  1.00 35.72 ? 187 ASP C OD1 1 
ATOM   5200 O OD2 . ASP C 1 187 ? 14.869  -24.940 25.322  1.00 38.22 ? 187 ASP C OD2 1 
ATOM   5201 N N   . MET C 1 188 ? 17.548  -27.966 24.958  1.00 34.40 ? 188 MET C N   1 
ATOM   5202 C CA  . MET C 1 188 ? 18.449  -28.082 23.817  1.00 39.21 ? 188 MET C CA  1 
ATOM   5203 C C   . MET C 1 188 ? 17.713  -27.733 22.531  1.00 40.90 ? 188 MET C C   1 
ATOM   5204 O O   . MET C 1 188 ? 16.500  -27.927 22.428  1.00 38.45 ? 188 MET C O   1 
ATOM   5205 C CB  . MET C 1 188 ? 19.075  -29.489 23.673  1.00 39.57 ? 188 MET C CB  1 
ATOM   5206 C CG  . MET C 1 188 ? 18.237  -30.629 24.184  1.00 45.09 ? 188 MET C CG  1 
ATOM   5207 S SD  . MET C 1 188 ? 19.245  -32.120 24.450  1.00 40.59 ? 188 MET C SD  1 
ATOM   5208 C CE  . MET C 1 188 ? 20.048  -32.210 22.868  1.00 40.45 ? 188 MET C CE  1 
ATOM   5209 N N   . THR C 1 189 ? 18.457  -27.158 21.574  1.00 41.34 ? 189 THR C N   1 
ATOM   5210 C CA  . THR C 1 189 ? 18.005  -27.056 20.190  1.00 43.47 ? 189 THR C CA  1 
ATOM   5211 C C   . THR C 1 189 ? 18.503  -28.262 19.397  1.00 48.36 ? 189 THR C C   1 
ATOM   5212 O O   . THR C 1 189 ? 19.020  -29.231 19.952  1.00 47.48 ? 189 THR C O   1 
ATOM   5213 C CB  . THR C 1 189 ? 18.496  -25.779 19.526  1.00 41.82 ? 189 THR C CB  1 
ATOM   5214 O OG1 . THR C 1 189 ? 19.900  -25.628 19.752  1.00 46.05 ? 189 THR C OG1 1 
ATOM   5215 C CG2 . THR C 1 189 ? 17.743  -24.557 20.062  1.00 36.83 ? 189 THR C CG2 1 
ATOM   5216 N N   . SER C 1 190 ? 18.374  -28.201 18.076  1.00 47.91 ? 190 SER C N   1 
ATOM   5217 C CA  . SER C 1 190 ? 18.884  -29.270 17.237  1.00 47.42 ? 190 SER C CA  1 
ATOM   5218 C C   . SER C 1 190 ? 20.409  -29.322 17.225  1.00 48.32 ? 190 SER C C   1 
ATOM   5219 O O   . SER C 1 190 ? 20.986  -30.364 16.886  1.00 49.11 ? 190 SER C O   1 
ATOM   5220 C CB  . SER C 1 190 ? 18.311  -29.093 15.835  1.00 49.18 ? 190 SER C CB  1 
ATOM   5221 O OG  . SER C 1 190 ? 18.964  -28.019 15.199  1.00 53.08 ? 190 SER C OG  1 
ATOM   5222 N N   . THR C 1 191 ? 21.079  -28.225 17.580  1.00 44.46 ? 191 THR C N   1 
ATOM   5223 C CA  . THR C 1 191 ? 22.528  -28.152 17.500  1.00 44.57 ? 191 THR C CA  1 
ATOM   5224 C C   . THR C 1 191 ? 23.206  -27.710 18.782  1.00 41.55 ? 191 THR C C   1 
ATOM   5225 O O   . THR C 1 191 ? 24.420  -27.902 18.909  1.00 40.43 ? 191 THR C O   1 
ATOM   5226 C CB  . THR C 1 191 ? 22.964  -27.191 16.382  1.00 47.19 ? 191 THR C CB  1 
ATOM   5227 O OG1 . THR C 1 191 ? 22.526  -25.866 16.712  1.00 52.55 ? 191 THR C OG1 1 
ATOM   5228 C CG2 . THR C 1 191 ? 22.376  -27.618 15.032  1.00 46.87 ? 191 THR C CG2 1 
ATOM   5229 N N   . HIS C 1 192 ? 22.495  -27.077 19.703  1.00 44.76 ? 192 HIS C N   1 
ATOM   5230 C CA  . HIS C 1 192 ? 23.137  -26.442 20.843  1.00 41.67 ? 192 HIS C CA  1 
ATOM   5231 C C   . HIS C 1 192 ? 22.529  -26.940 22.135  1.00 36.92 ? 192 HIS C C   1 
ATOM   5232 O O   . HIS C 1 192 ? 21.324  -27.164 22.217  1.00 36.69 ? 192 HIS C O   1 
ATOM   5233 C CB  . HIS C 1 192 ? 22.994  -24.909 20.780  1.00 42.57 ? 192 HIS C CB  1 
ATOM   5234 C CG  . HIS C 1 192 ? 23.898  -24.271 19.785  1.00 43.40 ? 192 HIS C CG  1 
ATOM   5235 N ND1 . HIS C 1 192 ? 23.692  -24.374 18.426  1.00 46.34 ? 192 HIS C ND1 1 
ATOM   5236 C CD2 . HIS C 1 192 ? 25.024  -23.535 19.946  1.00 43.32 ? 192 HIS C CD2 1 
ATOM   5237 C CE1 . HIS C 1 192 ? 24.667  -23.742 17.791  1.00 49.85 ? 192 HIS C CE1 1 
ATOM   5238 N NE2 . HIS C 1 192 ? 25.471  -23.199 18.691  1.00 48.21 ? 192 HIS C NE2 1 
ATOM   5239 N N   . TYR C 1 193 ? 23.370  -27.082 23.146  1.00 33.53 ? 193 TYR C N   1 
ATOM   5240 C CA  . TYR C 1 193 ? 22.879  -27.126 24.515  1.00 34.78 ? 193 TYR C CA  1 
ATOM   5241 C C   . TYR C 1 193 ? 22.571  -25.691 24.981  1.00 33.26 ? 193 TYR C C   1 
ATOM   5242 O O   . TYR C 1 193 ? 23.324  -24.757 24.680  1.00 30.85 ? 193 TYR C O   1 
ATOM   5243 C CB  . TYR C 1 193 ? 23.918  -27.736 25.445  1.00 32.77 ? 193 TYR C CB  1 
ATOM   5244 C CG  . TYR C 1 193 ? 24.409  -29.155 25.140  1.00 32.43 ? 193 TYR C CG  1 
ATOM   5245 C CD1 . TYR C 1 193 ? 23.556  -30.247 25.184  1.00 29.69 ? 193 TYR C CD1 1 
ATOM   5246 C CD2 . TYR C 1 193 ? 25.767  -29.384 24.885  1.00 31.26 ? 193 TYR C CD2 1 
ATOM   5247 C CE1 . TYR C 1 193 ? 24.043  -31.543 24.950  1.00 29.87 ? 193 TYR C CE1 1 
ATOM   5248 C CE2 . TYR C 1 193 ? 26.262  -30.661 24.648  1.00 29.97 ? 193 TYR C CE2 1 
ATOM   5249 C CZ  . TYR C 1 193 ? 25.404  -31.749 24.688  1.00 34.16 ? 193 TYR C CZ  1 
ATOM   5250 O OH  . TYR C 1 193 ? 25.928  -33.036 24.455  1.00 34.39 ? 193 TYR C OH  1 
ATOM   5251 N N   . VAL C 1 194 ? 21.487  -25.553 25.737  1.00 29.88 ? 194 VAL C N   1 
ATOM   5252 C CA  . VAL C 1 194 ? 21.103  -24.253 26.347  1.00 27.91 ? 194 VAL C CA  1 
ATOM   5253 C C   . VAL C 1 194 ? 21.521  -24.346 27.804  1.00 25.62 ? 194 VAL C C   1 
ATOM   5254 O O   . VAL C 1 194 ? 20.898  -25.090 28.508  1.00 29.04 ? 194 VAL C O   1 
ATOM   5255 C CB  . VAL C 1 194 ? 19.591  -24.016 26.266  1.00 31.36 ? 194 VAL C CB  1 
ATOM   5256 C CG1 . VAL C 1 194 ? 19.242  -22.664 26.843  1.00 28.38 ? 194 VAL C CG1 1 
ATOM   5257 C CG2 . VAL C 1 194 ? 19.078  -24.159 24.849  1.00 32.03 ? 194 VAL C CG2 1 
ATOM   5258 N N   . VAL C 1 195 ? 22.523  -23.596 28.226  1.00 26.84 ? 195 VAL C N   1 
ATOM   5259 C CA  . VAL C 1 195 ? 22.951  -23.776 29.630  1.00 27.02 ? 195 VAL C CA  1 
ATOM   5260 C C   . VAL C 1 195 ? 22.769  -22.519 30.481  1.00 28.60 ? 195 VAL C C   1 
ATOM   5261 O O   . VAL C 1 195 ? 23.062  -21.423 30.036  1.00 28.85 ? 195 VAL C O   1 
ATOM   5262 C CB  . VAL C 1 195 ? 24.367  -24.371 29.748  1.00 27.99 ? 195 VAL C CB  1 
ATOM   5263 C CG1 . VAL C 1 195 ? 24.980  -24.787 28.425  1.00 29.29 ? 195 VAL C CG1 1 
ATOM   5264 C CG2 . VAL C 1 195 ? 25.311  -23.531 30.563  1.00 29.16 ? 195 VAL C CG2 1 
ATOM   5265 N N   . ALA C 1 196 ? 22.281  -22.752 31.688  1.00 25.95 ? 196 ALA C N   1 
ATOM   5266 C CA  . ALA C 1 196 ? 22.184  -21.723 32.728  1.00 27.22 ? 196 ALA C CA  1 
ATOM   5267 C C   . ALA C 1 196 ? 23.571  -21.709 33.363  1.00 25.43 ? 196 ALA C C   1 
ATOM   5268 O O   . ALA C 1 196 ? 23.909  -22.649 34.047  1.00 22.78 ? 196 ALA C O   1 
ATOM   5269 C CB  . ALA C 1 196 ? 21.126  -22.094 33.724  1.00 26.52 ? 196 ALA C CB  1 
ATOM   5270 N N   . ASP C 1 197 ? 24.368  -20.708 33.021  1.00 25.10 ? 197 ASP C N   1 
ATOM   5271 C CA  . ASP C 1 197 ? 25.714  -20.574 33.550  1.00 23.32 ? 197 ASP C CA  1 
ATOM   5272 C C   . ASP C 1 197 ? 25.721  -19.574 34.715  1.00 21.59 ? 197 ASP C C   1 
ATOM   5273 O O   . ASP C 1 197 ? 25.539  -18.375 34.493  1.00 24.54 ? 197 ASP C O   1 
ATOM   5274 C CB  . ASP C 1 197 ? 26.670  -20.147 32.413  1.00 25.71 ? 197 ASP C CB  1 
ATOM   5275 C CG  . ASP C 1 197 ? 28.102  -19.933 32.876  1.00 26.44 ? 197 ASP C CG  1 
ATOM   5276 O OD1 . ASP C 1 197 ? 28.354  -19.936 34.112  1.00 24.82 ? 197 ASP C OD1 1 
ATOM   5277 O OD2 . ASP C 1 197 ? 28.982  -19.764 31.984  1.00 28.35 ? 197 ASP C OD2 1 
ATOM   5278 N N   . PRO C 1 198 ? 26.006  -20.009 35.941  1.00 22.14 ? 198 PRO C N   1 
ATOM   5279 C CA  . PRO C 1 198 ? 25.869  -19.122 37.111  1.00 22.80 ? 198 PRO C CA  1 
ATOM   5280 C C   . PRO C 1 198 ? 26.812  -17.925 37.137  1.00 27.87 ? 198 PRO C C   1 
ATOM   5281 O O   . PRO C 1 198 ? 26.662  -17.083 38.041  1.00 25.19 ? 198 PRO C O   1 
ATOM   5282 C CB  . PRO C 1 198 ? 26.187  -20.046 38.295  1.00 23.70 ? 198 PRO C CB  1 
ATOM   5283 C CG  . PRO C 1 198 ? 26.073  -21.452 37.746  1.00 26.24 ? 198 PRO C CG  1 
ATOM   5284 C CD  . PRO C 1 198 ? 26.515  -21.349 36.307  1.00 21.55 ? 198 PRO C CD  1 
ATOM   5285 N N   . ALA C 1 199 ? 27.803  -17.839 36.228  1.00 26.26 ? 199 ALA C N   1 
ATOM   5286 C CA  . ALA C 1 199 ? 28.666  -16.675 36.109  1.00 23.46 ? 199 ALA C CA  1 
ATOM   5287 C C   . ALA C 1 199 ? 28.354  -15.814 34.874  1.00 27.85 ? 199 ALA C C   1 
ATOM   5288 O O   . ALA C 1 199 ? 29.061  -14.812 34.639  1.00 29.38 ? 199 ALA C O   1 
ATOM   5289 C CB  . ALA C 1 199 ? 30.139  -17.150 36.073  1.00 23.95 ? 199 ALA C CB  1 
ATOM   5290 N N   . LYS C 1 200 ? 27.383  -16.199 34.042  1.00 25.94 ? 200 LYS C N   1 
ATOM   5291 C CA  . LYS C 1 200 ? 27.151  -15.530 32.763  1.00 27.53 ? 200 LYS C CA  1 
ATOM   5292 C C   . LYS C 1 200 ? 25.671  -15.259 32.453  1.00 32.21 ? 200 LYS C C   1 
ATOM   5293 O O   . LYS C 1 200 ? 25.332  -14.128 32.072  1.00 27.50 ? 200 LYS C O   1 
ATOM   5294 C CB  . LYS C 1 200 ? 27.762  -16.329 31.614  1.00 28.58 ? 200 LYS C CB  1 
ATOM   5295 C CG  . LYS C 1 200 ? 29.310  -16.116 31.410  1.00 32.05 ? 200 LYS C CG  1 
ATOM   5296 C CD  . LYS C 1 200 ? 29.690  -14.627 31.204  1.00 29.22 ? 200 LYS C CD  1 
ATOM   5297 C CE  . LYS C 1 200 ? 29.306  -14.145 29.824  1.00 33.74 ? 200 LYS C CE  1 
ATOM   5298 N NZ  . LYS C 1 200 ? 29.099  -12.668 29.744  1.00 30.99 ? 200 LYS C NZ  1 
ATOM   5299 N N   . GLY C 1 201 ? 24.791  -16.259 32.547  1.00 30.65 ? 201 GLY C N   1 
ATOM   5300 C CA  . GLY C 1 201 ? 23.396  -16.019 32.199  1.00 30.67 ? 201 GLY C CA  1 
ATOM   5301 C C   . GLY C 1 201 ? 22.613  -17.306 32.031  1.00 31.08 ? 201 GLY C C   1 
ATOM   5302 O O   . GLY C 1 201 ? 23.167  -18.423 32.039  1.00 29.42 ? 201 GLY C O   1 
ATOM   5303 N N   . VAL C 1 202 ? 21.313  -17.129 31.804  1.00 24.74 ? 202 VAL C N   1 
ATOM   5304 C CA  . VAL C 1 202 ? 20.390  -18.266 31.862  1.00 29.37 ? 202 VAL C CA  1 
ATOM   5305 C C   . VAL C 1 202 ? 20.290  -19.072 30.563  1.00 26.55 ? 202 VAL C C   1 
ATOM   5306 O O   . VAL C 1 202 ? 19.819  -20.212 30.604  1.00 25.43 ? 202 VAL C O   1 
ATOM   5307 C CB  . VAL C 1 202 ? 18.978  -17.799 32.292  1.00 26.03 ? 202 VAL C CB  1 
ATOM   5308 C CG1 . VAL C 1 202 ? 18.269  -17.072 31.151  1.00 29.27 ? 202 VAL C CG1 1 
ATOM   5309 C CG2 . VAL C 1 202 ? 18.145  -18.989 32.776  1.00 28.61 ? 202 VAL C CG2 1 
ATOM   5310 N N   . ASN C 1 203 ? 20.677  -18.516 29.407  1.00 29.75 ? 203 ASN C N   1 
ATOM   5311 C CA  . ASN C 1 203 ? 20.543  -19.218 28.129  1.00 32.90 ? 203 ASN C CA  1 
ATOM   5312 C C   . ASN C 1 203 ? 21.838  -19.096 27.300  1.00 32.12 ? 203 ASN C C   1 
ATOM   5313 O O   . ASN C 1 203 ? 21.859  -18.652 26.151  1.00 37.18 ? 203 ASN C O   1 
ATOM   5314 C CB  . ASN C 1 203 ? 19.268  -18.744 27.397  1.00 35.79 ? 203 ASN C CB  1 
ATOM   5315 C CG  . ASN C 1 203 ? 19.474  -17.496 26.545  1.00 40.44 ? 203 ASN C CG  1 
ATOM   5316 O OD1 . ASN C 1 203 ? 20.323  -16.662 26.850  1.00 42.04 ? 203 ASN C OD1 1 
ATOM   5317 N ND2 . ASN C 1 203 ? 18.670  -17.350 25.482  1.00 42.46 ? 203 ASN C ND2 1 
ATOM   5318 N N   . ARG C 1 204 ? 22.937  -19.593 27.855  1.00 31.52 ? 204 ARG C N   1 
ATOM   5319 C CA  . ARG C 1 204 ? 24.208  -19.619 27.109  1.00 34.03 ? 204 ARG C CA  1 
ATOM   5320 C C   . ARG C 1 204 ? 24.218  -20.858 26.217  1.00 32.26 ? 204 ARG C C   1 
ATOM   5321 O O   . ARG C 1 204 ? 24.163  -21.986 26.711  1.00 33.61 ? 204 ARG C O   1 
ATOM   5322 C CB  . ARG C 1 204 ? 25.409  -19.582 28.045  1.00 33.31 ? 204 ARG C CB  1 
ATOM   5323 C CG  . ARG C 1 204 ? 25.246  -18.669 29.230  1.00 31.38 ? 204 ARG C CG  1 
ATOM   5324 C CD  . ARG C 1 204 ? 25.070  -17.230 28.820  1.00 31.13 ? 204 ARG C CD  1 
ATOM   5325 N NE  . ARG C 1 204 ? 26.146  -16.788 27.942  1.00 35.94 ? 204 ARG C NE  1 
ATOM   5326 C CZ  . ARG C 1 204 ? 26.126  -15.651 27.262  1.00 39.27 ? 204 ARG C CZ  1 
ATOM   5327 N NH1 . ARG C 1 204 ? 25.080  -14.837 27.320  1.00 36.11 ? 204 ARG C NH1 1 
ATOM   5328 N NH2 . ARG C 1 204 ? 27.188  -15.314 26.528  1.00 35.18 ? 204 ARG C NH2 1 
ATOM   5329 N N   . LYS C 1 205 ? 24.151  -20.660 24.909  1.00 33.53 ? 205 LYS C N   1 
ATOM   5330 C CA  . LYS C 1 205 ? 24.084  -21.772 23.963  1.00 33.41 ? 205 LYS C CA  1 
ATOM   5331 C C   . LYS C 1 205 ? 25.472  -22.263 23.520  1.00 40.09 ? 205 LYS C C   1 
ATOM   5332 O O   . LYS C 1 205 ? 26.270  -21.491 22.968  1.00 39.14 ? 205 LYS C O   1 
ATOM   5333 C CB  . LYS C 1 205 ? 23.236  -21.352 22.763  1.00 41.01 ? 205 LYS C CB  1 
ATOM   5334 C CG  . LYS C 1 205 ? 21.825  -20.909 23.178  1.00 35.82 ? 205 LYS C CG  1 
ATOM   5335 C CD  . LYS C 1 205 ? 21.011  -20.391 22.034  1.00 41.43 ? 205 LYS C CD  1 
ATOM   5336 C CE  . LYS C 1 205 ? 19.834  -19.530 22.538  1.00 44.54 ? 205 LYS C CE  1 
ATOM   5337 N NZ  . LYS C 1 205 ? 19.916  -18.124 21.984  1.00 54.12 ? 205 LYS C NZ  1 
ATOM   5338 N N   . TYR C 1 206 ? 25.702  -23.548 23.778  1.00 38.19 ? 206 TYR C N   1 
ATOM   5339 C CA  . TYR C 1 206 ? 26.952  -24.234 23.380  1.00 40.06 ? 206 TYR C CA  1 
ATOM   5340 C C   . TYR C 1 206 ? 26.645  -25.263 22.298  1.00 36.77 ? 206 TYR C C   1 
ATOM   5341 O O   . TYR C 1 206 ? 25.763  -26.052 22.479  1.00 37.48 ? 206 TYR C O   1 
ATOM   5342 C CB  . TYR C 1 206 ? 27.563  -24.946 24.580  1.00 34.68 ? 206 TYR C CB  1 
ATOM   5343 C CG  . TYR C 1 206 ? 28.300  -24.019 25.499  1.00 33.16 ? 206 TYR C CG  1 
ATOM   5344 C CD1 . TYR C 1 206 ? 27.626  -23.122 26.292  1.00 33.04 ? 206 TYR C CD1 1 
ATOM   5345 C CD2 . TYR C 1 206 ? 29.672  -24.026 25.562  1.00 33.87 ? 206 TYR C CD2 1 
ATOM   5346 C CE1 . TYR C 1 206 ? 28.290  -22.255 27.130  1.00 30.98 ? 206 TYR C CE1 1 
ATOM   5347 C CE2 . TYR C 1 206 ? 30.355  -23.172 26.395  1.00 31.88 ? 206 TYR C CE2 1 
ATOM   5348 C CZ  . TYR C 1 206 ? 29.663  -22.277 27.175  1.00 32.40 ? 206 TYR C CZ  1 
ATOM   5349 O OH  . TYR C 1 206 ? 30.343  -21.442 27.996  1.00 33.24 ? 206 TYR C OH  1 
ATOM   5350 N N   . LYS C 1 207 ? 27.389  -25.226 21.199  1.00 41.41 ? 207 LYS C N   1 
ATOM   5351 C CA  . LYS C 1 207 ? 27.255  -26.283 20.165  1.00 42.86 ? 207 LYS C CA  1 
ATOM   5352 C C   . LYS C 1 207 ? 27.680  -27.585 20.849  1.00 38.69 ? 207 LYS C C   1 
ATOM   5353 O O   . LYS C 1 207 ? 28.714  -27.561 21.526  1.00 36.63 ? 207 LYS C O   1 
ATOM   5354 C CB  . LYS C 1 207 ? 28.196  -26.017 18.990  1.00 44.93 ? 207 LYS C CB  1 
ATOM   5355 C CG  . LYS C 1 207 ? 27.556  -25.569 17.683  1.00 53.70 ? 207 LYS C CG  1 
ATOM   5356 C CD  . LYS C 1 207 ? 28.565  -25.027 16.692  1.00 53.53 ? 207 LYS C CD  1 
ATOM   5357 C CE  . LYS C 1 207 ? 29.927  -25.683 16.795  1.00 53.03 ? 207 LYS C CE  1 
ATOM   5358 N NZ  . LYS C 1 207 ? 30.894  -25.167 15.798  1.00 59.73 ? 207 LYS C NZ  1 
ATOM   5359 N N   . PHE C 1 208 ? 26.876  -28.635 20.689  1.00 38.28 ? 208 PHE C N   1 
ATOM   5360 C CA  . PHE C 1 208 ? 27.082  -29.966 21.311  1.00 37.88 ? 208 PHE C CA  1 
ATOM   5361 C C   . PHE C 1 208 ? 28.559  -30.341 21.359  1.00 35.81 ? 208 PHE C C   1 
ATOM   5362 O O   . PHE C 1 208 ? 29.076  -30.573 22.423  1.00 37.98 ? 208 PHE C O   1 
ATOM   5363 C CB  . PHE C 1 208 ? 26.330  -31.045 20.540  1.00 37.32 ? 208 PHE C CB  1 
ATOM   5364 C CG  . PHE C 1 208 ? 24.841  -30.871 20.424  1.00 41.60 ? 208 PHE C CG  1 
ATOM   5365 C CD1 . PHE C 1 208 ? 24.111  -30.249 21.417  1.00 39.95 ? 208 PHE C CD1 1 
ATOM   5366 C CD2 . PHE C 1 208 ? 24.161  -31.355 19.319  1.00 40.63 ? 208 PHE C CD2 1 
ATOM   5367 C CE1 . PHE C 1 208 ? 22.742  -30.115 21.305  1.00 37.45 ? 208 PHE C CE1 1 
ATOM   5368 C CE2 . PHE C 1 208 ? 22.794  -31.218 19.210  1.00 39.89 ? 208 PHE C CE2 1 
ATOM   5369 C CZ  . PHE C 1 208 ? 22.090  -30.592 20.201  1.00 43.90 ? 208 PHE C CZ  1 
ATOM   5370 N N   . SER C 1 209 ? 29.238  -30.303 20.228  1.00 38.62 ? 209 SER C N   1 
ATOM   5371 C CA  . SER C 1 209 ? 30.661  -30.670 20.237  1.00 37.18 ? 209 SER C CA  1 
ATOM   5372 C C   . SER C 1 209 ? 31.519  -29.706 21.048  1.00 37.97 ? 209 SER C C   1 
ATOM   5373 O O   . SER C 1 209 ? 32.563  -30.108 21.592  1.00 39.22 ? 209 SER C O   1 
ATOM   5374 C CB  . SER C 1 209 ? 31.210  -30.767 18.806  1.00 40.16 ? 209 SER C CB  1 
ATOM   5375 O OG  . SER C 1 209 ? 31.931  -29.581 18.449  1.00 43.80 ? 209 SER C OG  1 
ATOM   5376 N N   . CYS C 1 210 ? 31.134  -28.431 21.104  1.00 35.21 ? 210 CYS C N   1 
ATOM   5377 C CA  . CYS C 1 210 ? 31.914  -27.455 21.856  1.00 35.24 ? 210 CYS C CA  1 
ATOM   5378 C C   . CYS C 1 210 ? 32.005  -27.844 23.327  1.00 31.55 ? 210 CYS C C   1 
ATOM   5379 O O   . CYS C 1 210 ? 33.107  -27.949 23.894  1.00 32.68 ? 210 CYS C O   1 
ATOM   5380 C CB  . CYS C 1 210 ? 31.277  -26.060 21.692  1.00 36.60 ? 210 CYS C CB  1 
ATOM   5381 S SG  . CYS C 1 210 ? 32.175  -24.742 22.554  1.00 39.97 ? 210 CYS C SG  1 
ATOM   5382 N N   . LEU C 1 211 ? 30.849  -28.118 23.944  1.00 31.13 ? 211 LEU C N   1 
ATOM   5383 C CA  . LEU C 1 211 ? 30.764  -28.485 25.360  1.00 29.24 ? 211 LEU C CA  1 
ATOM   5384 C C   . LEU C 1 211 ? 31.277  -29.902 25.592  1.00 31.18 ? 211 LEU C C   1 
ATOM   5385 O O   . LEU C 1 211 ? 31.980  -30.163 26.577  1.00 28.70 ? 211 LEU C O   1 
ATOM   5386 C CB  . LEU C 1 211 ? 29.312  -28.361 25.853  1.00 31.04 ? 211 LEU C CB  1 
ATOM   5387 C CG  . LEU C 1 211 ? 29.139  -28.397 27.380  1.00 29.28 ? 211 LEU C CG  1 
ATOM   5388 C CD1 . LEU C 1 211 ? 29.883  -27.193 28.022  1.00 28.78 ? 211 LEU C CD1 1 
ATOM   5389 C CD2 . LEU C 1 211 ? 27.683  -28.380 27.772  1.00 28.50 ? 211 LEU C CD2 1 
ATOM   5390 N N   . ASP C 1 212 ? 30.901  -30.831 24.705  1.00 32.07 ? 212 ASP C N   1 
ATOM   5391 C CA  . ASP C 1 212 ? 31.319  -32.231 24.821  1.00 30.86 ? 212 ASP C CA  1 
ATOM   5392 C C   . ASP C 1 212 ? 32.827  -32.356 24.921  1.00 34.00 ? 212 ASP C C   1 
ATOM   5393 O O   . ASP C 1 212 ? 33.347  -33.161 25.721  1.00 35.92 ? 212 ASP C O   1 
ATOM   5394 C CB  . ASP C 1 212 ? 30.838  -33.007 23.604  1.00 32.64 ? 212 ASP C CB  1 
ATOM   5395 C CG  . ASP C 1 212 ? 29.349  -33.216 23.599  1.00 33.54 ? 212 ASP C CG  1 
ATOM   5396 O OD1 . ASP C 1 212 ? 28.687  -33.072 24.662  1.00 34.31 ? 212 ASP C OD1 1 
ATOM   5397 O OD2 . ASP C 1 212 ? 28.826  -33.516 22.511  1.00 34.51 ? 212 ASP C OD2 1 
ATOM   5398 N N   . ASN C 1 213 ? 33.561  -31.596 24.119  1.00 33.18 ? 213 ASN C N   1 
ATOM   5399 C CA  . ASN C 1 213 ? 35.033  -31.774 24.108  1.00 36.26 ? 213 ASN C CA  1 
ATOM   5400 C C   . ASN C 1 213 ? 35.778  -30.795 25.005  1.00 38.77 ? 213 ASN C C   1 
ATOM   5401 O O   . ASN C 1 213 ? 36.987  -30.902 25.043  1.00 38.10 ? 213 ASN C O   1 
ATOM   5402 C CB  . ASN C 1 213 ? 35.597  -31.623 22.706  1.00 36.60 ? 213 ASN C CB  1 
ATOM   5403 C CG  . ASN C 1 213 ? 35.272  -32.832 21.873  1.00 37.40 ? 213 ASN C CG  1 
ATOM   5404 O OD1 . ASN C 1 213 ? 34.240  -32.887 21.235  1.00 38.68 ? 213 ASN C OD1 1 
ATOM   5405 N ND2 . ASN C 1 213 ? 36.140  -33.814 21.932  1.00 36.92 ? 213 ASN C ND2 1 
ATOM   5406 N N   . ALA C 1 214 ? 35.086  -29.943 25.754  1.00 33.50 ? 214 ALA C N   1 
ATOM   5407 C CA  . ALA C 1 214 ? 35.792  -28.931 26.567  1.00 34.33 ? 214 ALA C CA  1 
ATOM   5408 C C   . ALA C 1 214 ? 36.230  -29.431 27.942  1.00 35.49 ? 214 ALA C C   1 
ATOM   5409 O O   . ALA C 1 214 ? 36.524  -28.594 28.759  1.00 40.94 ? 214 ALA C O   1 
ATOM   5410 C CB  . ALA C 1 214 ? 34.974  -27.679 26.681  1.00 35.68 ? 214 ALA C CB  1 
ATOM   5411 N N   . ASN C 1 215 ? 36.237  -30.727 28.198  1.00 37.72 ? 215 ASN C N   1 
ATOM   5412 C CA  . ASN C 1 215 ? 36.694  -31.221 29.520  1.00 34.67 ? 215 ASN C CA  1 
ATOM   5413 C C   . ASN C 1 215 ? 37.796  -32.257 29.278  1.00 33.56 ? 215 ASN C C   1 
ATOM   5414 O O   . ASN C 1 215 ? 37.984  -33.120 30.100  1.00 31.38 ? 215 ASN C O   1 
ATOM   5415 C CB  . ASN C 1 215 ? 35.519  -31.697 30.365  1.00 27.43 ? 215 ASN C CB  1 
ATOM   5416 C CG  . ASN C 1 215 ? 35.721  -31.535 31.852  1.00 33.68 ? 215 ASN C CG  1 
ATOM   5417 O OD1 . ASN C 1 215 ? 36.259  -30.545 32.329  1.00 31.37 ? 215 ASN C OD1 1 
ATOM   5418 N ND2 . ASN C 1 215 ? 35.264  -32.520 32.591  1.00 29.29 ? 215 ASN C ND2 1 
ATOM   5419 N N   . LYS C 1 216 ? 38.469  -32.125 28.145  1.00 38.14 ? 216 LYS C N   1 
ATOM   5420 C CA  . LYS C 1 216 ? 39.591  -33.012 27.764  1.00 37.60 ? 216 LYS C CA  1 
ATOM   5421 C C   . LYS C 1 216 ? 40.568  -33.077 28.931  1.00 34.33 ? 216 LYS C C   1 
ATOM   5422 O O   . LYS C 1 216 ? 41.002  -32.038 29.402  1.00 38.42 ? 216 LYS C O   1 
ATOM   5423 C CB  . LYS C 1 216 ? 40.199  -32.565 26.437  1.00 42.34 ? 216 LYS C CB  1 
ATOM   5424 C CG  . LYS C 1 216 ? 41.449  -31.714 26.561  1.00 44.22 ? 216 LYS C CG  1 
ATOM   5425 C CD  . LYS C 1 216 ? 41.637  -30.709 25.438  1.00 50.35 ? 216 LYS C CD  1 
ATOM   5426 C CE  . LYS C 1 216 ? 41.764  -29.279 25.915  1.00 47.55 ? 216 LYS C CE  1 
ATOM   5427 N NZ  . LYS C 1 216 ? 43.024  -28.631 25.482  1.00 52.18 ? 216 LYS C NZ  1 
ATOM   5428 N N   . GLY C 1 217 ? 40.845  -34.280 29.409  1.00 34.06 ? 217 GLY C N   1 
ATOM   5429 C CA  . GLY C 1 217 ? 41.770  -34.447 30.540  1.00 32.14 ? 217 GLY C CA  1 
ATOM   5430 C C   . GLY C 1 217 ? 41.042  -34.519 31.859  1.00 31.38 ? 217 GLY C C   1 
ATOM   5431 O O   . GLY C 1 217 ? 41.694  -34.625 32.868  1.00 27.33 ? 217 GLY C O   1 
ATOM   5432 N N   . TYR C 1 218 ? 39.714  -34.360 31.840  1.00 34.03 ? 218 TYR C N   1 
ATOM   5433 C CA  . TYR C 1 218 ? 38.944  -34.383 33.069  1.00 33.53 ? 218 TYR C CA  1 
ATOM   5434 C C   . TYR C 1 218 ? 37.780  -35.336 32.848  1.00 31.62 ? 218 TYR C C   1 
ATOM   5435 O O   . TYR C 1 218 ? 37.590  -35.866 31.743  1.00 31.29 ? 218 TYR C O   1 
ATOM   5436 C CB  . TYR C 1 218 ? 38.496  -32.968 33.482  1.00 32.51 ? 218 TYR C CB  1 
ATOM   5437 C CG  . TYR C 1 218 ? 39.657  -31.966 33.585  1.00 32.67 ? 218 TYR C CG  1 
ATOM   5438 C CD1 . TYR C 1 218 ? 40.159  -31.328 32.453  1.00 32.34 ? 218 TYR C CD1 1 
ATOM   5439 C CD2 . TYR C 1 218 ? 40.243  -31.672 34.813  1.00 31.79 ? 218 TYR C CD2 1 
ATOM   5440 C CE1 . TYR C 1 218 ? 41.220  -30.435 32.541  1.00 32.27 ? 218 TYR C CE1 1 
ATOM   5441 C CE2 . TYR C 1 218 ? 41.292  -30.765 34.906  1.00 31.22 ? 218 TYR C CE2 1 
ATOM   5442 C CZ  . TYR C 1 218 ? 41.764  -30.159 33.766  1.00 32.05 ? 218 TYR C CZ  1 
ATOM   5443 O OH  . TYR C 1 218 ? 42.820  -29.254 33.850  1.00 45.14 ? 218 TYR C OH  1 
ATOM   5444 N N   . ARG C 1 219 ? 37.019  -35.574 33.918  1.00 31.87 ? 219 ARG C N   1 
ATOM   5445 C CA  . ARG C 1 219 ? 36.011  -36.637 33.906  1.00 30.05 ? 219 ARG C CA  1 
ATOM   5446 C C   . ARG C 1 219 ? 35.033  -36.474 32.749  1.00 29.59 ? 219 ARG C C   1 
ATOM   5447 O O   . ARG C 1 219 ? 34.469  -35.392 32.538  1.00 31.08 ? 219 ARG C O   1 
ATOM   5448 C CB  . ARG C 1 219 ? 35.266  -36.663 35.233  1.00 28.24 ? 219 ARG C CB  1 
ATOM   5449 C CG  . ARG C 1 219 ? 34.243  -37.792 35.311  1.00 26.26 ? 219 ARG C CG  1 
ATOM   5450 C CD  . ARG C 1 219 ? 33.820  -38.023 36.751  1.00 27.52 ? 219 ARG C CD  1 
ATOM   5451 N NE  . ARG C 1 219 ? 32.744  -39.018 36.849  1.00 24.02 ? 219 ARG C NE  1 
ATOM   5452 C CZ  . ARG C 1 219 ? 32.296  -39.522 37.988  1.00 24.81 ? 219 ARG C CZ  1 
ATOM   5453 N NH1 . ARG C 1 219 ? 32.780  -39.137 39.145  1.00 23.87 ? 219 ARG C NH1 1 
ATOM   5454 N NH2 . ARG C 1 219 ? 31.287  -40.394 37.965  1.00 28.61 ? 219 ARG C NH2 1 
ATOM   5455 N N   . GLN C 1 220 ? 34.823  -37.563 32.003  1.00 24.96 ? 220 GLN C N   1 
ATOM   5456 C CA  . GLN C 1 220 ? 34.032  -37.518 30.772  1.00 27.91 ? 220 GLN C CA  1 
ATOM   5457 C C   . GLN C 1 220 ? 32.582  -37.912 31.056  1.00 31.18 ? 220 GLN C C   1 
ATOM   5458 O O   . GLN C 1 220 ? 32.081  -38.950 30.616  1.00 30.69 ? 220 GLN C O   1 
ATOM   5459 C CB  . GLN C 1 220 ? 34.667  -38.398 29.692  1.00 30.68 ? 220 GLN C CB  1 
ATOM   5460 C CG  . GLN C 1 220 ? 36.013  -37.876 29.246  1.00 30.49 ? 220 GLN C CG  1 
ATOM   5461 C CD  . GLN C 1 220 ? 35.897  -36.556 28.513  1.00 28.14 ? 220 GLN C CD  1 
ATOM   5462 O OE1 . GLN C 1 220 ? 35.301  -36.474 27.446  1.00 31.21 ? 220 GLN C OE1 1 
ATOM   5463 N NE2 . GLN C 1 220 ? 36.407  -35.506 29.125  1.00 32.10 ? 220 GLN C NE2 1 
ATOM   5464 N N   . ASN C 1 221 ? 31.884  -37.023 31.779  1.00 27.84 ? 221 ASN C N   1 
ATOM   5465 C CA  . ASN C 1 221 ? 30.469  -37.223 32.078  1.00 27.82 ? 221 ASN C CA  1 
ATOM   5466 C C   . ASN C 1 221 ? 29.746  -35.881 32.091  1.00 26.41 ? 221 ASN C C   1 
ATOM   5467 O O   . ASN C 1 221 ? 30.367  -34.828 32.196  1.00 23.11 ? 221 ASN C O   1 
ATOM   5468 C CB  . ASN C 1 221 ? 30.228  -37.891 33.438  1.00 27.34 ? 221 ASN C CB  1 
ATOM   5469 C CG  . ASN C 1 221 ? 30.603  -39.367 33.458  1.00 29.19 ? 221 ASN C CG  1 
ATOM   5470 O OD1 . ASN C 1 221 ? 31.537  -39.745 34.156  1.00 27.67 ? 221 ASN C OD1 1 
ATOM   5471 N ND2 . ASN C 1 221 ? 29.897  -40.186 32.677  1.00 23.89 ? 221 ASN C ND2 1 
ATOM   5472 N N   . TYR C 1 222 ? 28.423  -35.946 31.974  1.00 28.73 ? 222 TYR C N   1 
ATOM   5473 C CA  . TYR C 1 222 ? 27.491  -34.936 32.474  1.00 24.64 ? 222 TYR C CA  1 
ATOM   5474 C C   . TYR C 1 222 ? 26.746  -35.566 33.641  1.00 28.33 ? 222 TYR C C   1 
ATOM   5475 O O   . TYR C 1 222 ? 26.871  -36.772 33.906  1.00 27.37 ? 222 TYR C O   1 
ATOM   5476 C CB  . TYR C 1 222 ? 26.513  -34.442 31.391  1.00 23.62 ? 222 TYR C CB  1 
ATOM   5477 C CG  . TYR C 1 222 ? 27.133  -33.717 30.228  1.00 24.90 ? 222 TYR C CG  1 
ATOM   5478 C CD1 . TYR C 1 222 ? 28.199  -32.841 30.415  1.00 26.51 ? 222 TYR C CD1 1 
ATOM   5479 C CD2 . TYR C 1 222 ? 26.668  -33.925 28.940  1.00 28.08 ? 222 TYR C CD2 1 
ATOM   5480 C CE1 . TYR C 1 222 ? 28.808  -32.206 29.333  1.00 27.67 ? 222 TYR C CE1 1 
ATOM   5481 C CE2 . TYR C 1 222 ? 27.231  -33.292 27.866  1.00 27.34 ? 222 TYR C CE2 1 
ATOM   5482 C CZ  . TYR C 1 222 ? 28.305  -32.444 28.059  1.00 31.32 ? 222 TYR C CZ  1 
ATOM   5483 O OH  . TYR C 1 222 ? 28.870  -31.831 26.987  1.00 29.21 ? 222 TYR C OH  1 
ATOM   5484 N N   . TYR C 1 223 ? 25.976  -34.760 34.370  1.00 21.75 ? 223 TYR C N   1 
ATOM   5485 C CA  . TYR C 1 223 ? 25.415  -35.213 35.646  1.00 22.04 ? 223 TYR C CA  1 
ATOM   5486 C C   . TYR C 1 223 ? 23.918  -34.899 35.742  1.00 24.49 ? 223 TYR C C   1 
ATOM   5487 O O   . TYR C 1 223 ? 23.529  -33.784 36.099  1.00 20.91 ? 223 TYR C O   1 
ATOM   5488 C CB  . TYR C 1 223 ? 26.209  -34.595 36.808  1.00 22.26 ? 223 TYR C CB  1 
ATOM   5489 C CG  . TYR C 1 223 ? 27.693  -34.863 36.618  1.00 23.37 ? 223 TYR C CG  1 
ATOM   5490 C CD1 . TYR C 1 223 ? 28.236  -36.106 36.956  1.00 23.90 ? 223 TYR C CD1 1 
ATOM   5491 C CD2 . TYR C 1 223 ? 28.543  -33.900 36.064  1.00 22.45 ? 223 TYR C CD2 1 
ATOM   5492 C CE1 . TYR C 1 223 ? 29.617  -36.377 36.770  1.00 25.80 ? 223 TYR C CE1 1 
ATOM   5493 C CE2 . TYR C 1 223 ? 29.901  -34.162 35.878  1.00 25.73 ? 223 TYR C CE2 1 
ATOM   5494 C CZ  . TYR C 1 223 ? 30.420  -35.417 36.210  1.00 22.74 ? 223 TYR C CZ  1 
ATOM   5495 O OH  . TYR C 1 223 ? 31.765  -35.711 36.043  1.00 26.21 ? 223 TYR C OH  1 
ATOM   5496 N N   . VAL C 1 224 ? 23.086  -35.903 35.453  1.00 24.55 ? 224 VAL C N   1 
ATOM   5497 C CA  . VAL C 1 224 ? 21.643  -35.758 35.533  1.00 25.08 ? 224 VAL C CA  1 
ATOM   5498 C C   . VAL C 1 224 ? 21.232  -35.602 36.985  1.00 24.76 ? 224 VAL C C   1 
ATOM   5499 O O   . VAL C 1 224 ? 21.704  -36.351 37.849  1.00 24.81 ? 224 VAL C O   1 
ATOM   5500 C CB  . VAL C 1 224 ? 20.966  -36.990 34.909  1.00 29.05 ? 224 VAL C CB  1 
ATOM   5501 C CG1 . VAL C 1 224 ? 19.418  -36.907 35.046  1.00 26.37 ? 224 VAL C CG1 1 
ATOM   5502 C CG2 . VAL C 1 224 ? 21.408  -37.176 33.453  1.00 25.92 ? 224 VAL C CG2 1 
ATOM   5503 N N   . VAL C 1 225 ? 20.330  -34.652 37.262  1.00 24.44 ? 225 VAL C N   1 
ATOM   5504 C CA  . VAL C 1 225 ? 19.777  -34.446 38.600  1.00 24.77 ? 225 VAL C CA  1 
ATOM   5505 C C   . VAL C 1 225 ? 18.343  -34.968 38.629  1.00 25.21 ? 225 VAL C C   1 
ATOM   5506 O O   . VAL C 1 225 ? 17.501  -34.519 37.846  1.00 25.44 ? 225 VAL C O   1 
ATOM   5507 C CB  . VAL C 1 225 ? 19.821  -32.965 39.002  1.00 22.49 ? 225 VAL C CB  1 
ATOM   5508 C CG1 . VAL C 1 225 ? 19.542  -32.839 40.477  1.00 24.53 ? 225 VAL C CG1 1 
ATOM   5509 C CG2 . VAL C 1 225 ? 21.215  -32.353 38.590  1.00 18.28 ? 225 VAL C CG2 1 
ATOM   5510 N N   . CYS C 1 226 ? 18.052  -35.904 39.541  1.00 25.28 ? 226 CYS C N   1 
ATOM   5511 C CA  . CYS C 1 226 ? 16.669  -36.403 39.566  1.00 27.76 ? 226 CYS C CA  1 
ATOM   5512 C C   . CYS C 1 226 ? 16.263  -36.651 41.011  1.00 28.41 ? 226 CYS C C   1 
ATOM   5513 O O   . CYS C 1 226 ? 17.128  -36.603 41.899  1.00 28.26 ? 226 CYS C O   1 
ATOM   5514 C CB  . CYS C 1 226 ? 16.486  -37.688 38.763  1.00 29.86 ? 226 CYS C CB  1 
ATOM   5515 S SG  . CYS C 1 226 ? 17.544  -39.073 39.230  1.00 34.28 ? 226 CYS C SG  1 
ATOM   5516 N N   . PRO C 1 227 ? 14.972  -36.899 41.306  1.00 28.51 ? 227 PRO C N   1 
ATOM   5517 C CA  . PRO C 1 227 ? 14.606  -37.227 42.693  1.00 30.34 ? 227 PRO C CA  1 
ATOM   5518 C C   . PRO C 1 227 ? 15.230  -38.553 43.104  1.00 28.43 ? 227 PRO C C   1 
ATOM   5519 O O   . PRO C 1 227 ? 15.287  -39.484 42.306  1.00 29.72 ? 227 PRO C O   1 
ATOM   5520 C CB  . PRO C 1 227 ? 13.078  -37.314 42.648  1.00 28.48 ? 227 PRO C CB  1 
ATOM   5521 C CG  . PRO C 1 227 ? 12.677  -36.590 41.367  1.00 27.86 ? 227 PRO C CG  1 
ATOM   5522 C CD  . PRO C 1 227 ? 13.792  -36.876 40.425  1.00 29.52 ? 227 PRO C CD  1 
ATOM   5523 N N   . ALA C 1 228 ? 15.681  -38.626 44.357  1.00 27.28 ? 228 ALA C N   1 
ATOM   5524 C CA  . ALA C 1 228 ? 16.359  -39.818 44.922  1.00 34.89 ? 228 ALA C CA  1 
ATOM   5525 C C   . ALA C 1 228 ? 15.361  -40.885 45.149  1.00 39.47 ? 228 ALA C C   1 
ATOM   5526 O O   . ALA C 1 228 ? 14.286  -40.436 45.488  1.00 41.27 ? 228 ALA C O   1 
ATOM   5527 C CB  . ALA C 1 228 ? 17.029  -39.488 46.239  1.00 35.82 ? 228 ALA C CB  1 
ATOM   5528 O OXT . ALA C 1 228 ? 15.462  -42.115 45.034  1.00 46.29 ? 228 ALA C OXT 1 
ATOM   5529 N N   . MET D 1 1   ? -6.410  -9.144  -3.177  1.00 49.72 ? 1   MET D N   1 
ATOM   5530 C CA  . MET D 1 1   ? -5.056  -9.663  -2.918  1.00 46.22 ? 1   MET D CA  1 
ATOM   5531 C C   . MET D 1 1   ? -5.015  -10.502 -1.654  1.00 45.09 ? 1   MET D C   1 
ATOM   5532 O O   . MET D 1 1   ? -5.067  -9.978  -0.540  1.00 48.27 ? 1   MET D O   1 
ATOM   5533 C CB  . MET D 1 1   ? -4.046  -8.520  -2.805  1.00 47.27 ? 1   MET D CB  1 
ATOM   5534 C CG  . MET D 1 1   ? -4.035  -7.547  -3.961  1.00 47.95 ? 1   MET D CG  1 
ATOM   5535 S SD  . MET D 1 1   ? -2.533  -6.536  -3.865  1.00 62.82 ? 1   MET D SD  1 
ATOM   5536 C CE  . MET D 1 1   ? -1.736  -6.953  -5.378  1.00 41.56 ? 1   MET D CE  1 
ATOM   5537 N N   . VAL D 1 2   ? -4.850  -11.797 -1.831  1.00 41.23 ? 2   VAL D N   1 
ATOM   5538 C CA  . VAL D 1 2   ? -4.885  -12.730 -0.712  1.00 43.98 ? 2   VAL D CA  1 
ATOM   5539 C C   . VAL D 1 2   ? -3.488  -12.860 -0.131  1.00 36.81 ? 2   VAL D C   1 
ATOM   5540 O O   . VAL D 1 2   ? -2.480  -12.805 -0.846  1.00 36.39 ? 2   VAL D O   1 
ATOM   5541 C CB  . VAL D 1 2   ? -5.463  -14.092 -1.138  1.00 41.08 ? 2   VAL D CB  1 
ATOM   5542 C CG1 . VAL D 1 2   ? -6.684  -13.871 -2.019  1.00 39.06 ? 2   VAL D CG1 1 
ATOM   5543 C CG2 . VAL D 1 2   ? -4.426  -14.893 -1.899  1.00 39.52 ? 2   VAL D CG2 1 
ATOM   5544 N N   . ARG D 1 3   ? -3.438  -12.969 1.187   1.00 37.55 ? 3   ARG D N   1 
ATOM   5545 C CA  . ARG D 1 3   ? -2.210  -13.020 1.945   1.00 38.83 ? 3   ARG D CA  1 
ATOM   5546 C C   . ARG D 1 3   ? -2.038  -14.419 2.519   1.00 35.46 ? 3   ARG D C   1 
ATOM   5547 O O   . ARG D 1 3   ? -3.020  -15.104 2.827   1.00 35.31 ? 3   ARG D O   1 
ATOM   5548 C CB  . ARG D 1 3   ? -2.260  -12.008 3.102   1.00 40.22 ? 3   ARG D CB  1 
ATOM   5549 C CG  . ARG D 1 3   ? -2.566  -10.565 2.688   1.00 39.94 ? 3   ARG D CG  1 
ATOM   5550 C CD  . ARG D 1 3   ? -2.258  -9.635  3.851   1.00 42.87 ? 3   ARG D CD  1 
ATOM   5551 N NE  . ARG D 1 3   ? -3.085  -9.947  5.011   1.00 45.81 ? 3   ARG D NE  1 
ATOM   5552 C CZ  . ARG D 1 3   ? -2.668  -9.929  6.273   1.00 47.92 ? 3   ARG D CZ  1 
ATOM   5553 N NH1 . ARG D 1 3   ? -1.412  -9.610  6.592   1.00 44.39 ? 3   ARG D NH1 1 
ATOM   5554 N NH2 . ARG D 1 3   ? -3.536  -10.213 7.243   1.00 44.77 ? 3   ARG D NH2 1 
ATOM   5555 N N   . PHE D 1 4   ? -0.784  -14.838 2.689   1.00 34.29 ? 4   PHE D N   1 
ATOM   5556 C CA  . PHE D 1 4   ? -0.502  -16.126 3.290   1.00 32.28 ? 4   PHE D CA  1 
ATOM   5557 C C   . PHE D 1 4   ? 0.496   -15.917 4.415   1.00 33.64 ? 4   PHE D C   1 
ATOM   5558 O O   . PHE D 1 4   ? 1.453   -15.151 4.269   1.00 34.30 ? 4   PHE D O   1 
ATOM   5559 C CB  . PHE D 1 4   ? 0.003   -17.082 2.231   1.00 33.75 ? 4   PHE D CB  1 
ATOM   5560 C CG  . PHE D 1 4   ? -0.995  -17.354 1.154   1.00 30.67 ? 4   PHE D CG  1 
ATOM   5561 C CD1 . PHE D 1 4   ? -2.146  -18.100 1.427   1.00 34.90 ? 4   PHE D CD1 1 
ATOM   5562 C CD2 . PHE D 1 4   ? -0.803  -16.868 -0.132  1.00 30.28 ? 4   PHE D CD2 1 
ATOM   5563 C CE1 . PHE D 1 4   ? -3.066  -18.380 0.431   1.00 31.22 ? 4   PHE D CE1 1 
ATOM   5564 C CE2 . PHE D 1 4   ? -1.735  -17.127 -1.141  1.00 33.16 ? 4   PHE D CE2 1 
ATOM   5565 C CZ  . PHE D 1 4   ? -2.873  -17.914 -0.850  1.00 33.17 ? 4   PHE D CZ  1 
ATOM   5566 N N   . SER D 1 5   ? 0.240   -16.548 5.550   1.00 31.48 ? 5   SER D N   1 
ATOM   5567 C CA  . SER D 1 5   ? 1.024   -16.309 6.750   1.00 30.47 ? 5   SER D CA  1 
ATOM   5568 C C   . SER D 1 5   ? 2.334   -17.109 6.732   1.00 32.87 ? 5   SER D C   1 
ATOM   5569 O O   . SER D 1 5   ? 2.543   -17.982 5.903   1.00 30.33 ? 5   SER D O   1 
ATOM   5570 C CB  . SER D 1 5   ? 0.201   -16.647 7.988   1.00 33.83 ? 5   SER D CB  1 
ATOM   5571 O OG  . SER D 1 5   ? 0.179   -18.050 8.209   1.00 32.60 ? 5   SER D OG  1 
ATOM   5572 N N   . ARG D 1 6   ? 3.215   -16.779 7.673   1.00 33.14 ? 6   ARG D N   1 
ATOM   5573 C CA  . ARG D 1 6   ? 4.477   -17.495 7.827   1.00 38.01 ? 6   ARG D CA  1 
ATOM   5574 C C   . ARG D 1 6   ? 4.244   -18.987 8.022   1.00 36.22 ? 6   ARG D C   1 
ATOM   5575 O O   . ARG D 1 6   ? 5.025   -19.814 7.532   1.00 34.32 ? 6   ARG D O   1 
ATOM   5576 C CB  . ARG D 1 6   ? 5.266   -16.906 8.996   1.00 36.59 ? 6   ARG D CB  1 
ATOM   5577 C CG  . ARG D 1 6   ? 6.666   -17.377 9.028   1.00 38.12 ? 6   ARG D CG  1 
ATOM   5578 C CD  . ARG D 1 6   ? 7.226   -17.419 10.437  1.00 41.86 ? 6   ARG D CD  1 
ATOM   5579 N NE  . ARG D 1 6   ? 7.080   -16.171 11.175  1.00 50.15 ? 6   ARG D NE  1 
ATOM   5580 C CZ  . ARG D 1 6   ? 6.775   -16.102 12.462  1.00 48.43 ? 6   ARG D CZ  1 
ATOM   5581 N NH1 . ARG D 1 6   ? 6.581   -17.195 13.179  1.00 50.33 ? 6   ARG D NH1 1 
ATOM   5582 N NH2 . ARG D 1 6   ? 6.696   -14.907 13.046  1.00 49.43 ? 6   ARG D NH2 1 
ATOM   5583 N N   . ASP D 1 7   ? 3.203   -19.352 8.781   1.00 36.14 ? 7   ASP D N   1 
ATOM   5584 C CA  . ASP D 1 7   ? 2.930   -20.771 9.033   1.00 38.77 ? 7   ASP D CA  1 
ATOM   5585 C C   . ASP D 1 7   ? 2.455   -21.477 7.779   1.00 32.74 ? 7   ASP D C   1 
ATOM   5586 O O   . ASP D 1 7   ? 2.877   -22.601 7.493   1.00 34.82 ? 7   ASP D O   1 
ATOM   5587 C CB  . ASP D 1 7   ? 1.882   -20.924 10.135  1.00 41.07 ? 7   ASP D CB  1 
ATOM   5588 C CG  . ASP D 1 7   ? 2.494   -21.221 11.458  1.00 47.13 ? 7   ASP D CG  1 
ATOM   5589 O OD1 . ASP D 1 7   ? 3.079   -22.318 11.587  1.00 56.36 ? 7   ASP D OD1 1 
ATOM   5590 O OD2 . ASP D 1 7   ? 2.430   -20.357 12.355  1.00 49.34 ? 7   ASP D OD2 1 
ATOM   5591 N N   . MET D 1 8   ? 1.599   -20.820 7.012   1.00 31.30 ? 8   MET D N   1 
ATOM   5592 C CA  . MET D 1 8   ? 1.096   -21.401 5.777   1.00 31.67 ? 8   MET D CA  1 
ATOM   5593 C C   . MET D 1 8   ? 2.212   -21.562 4.748   1.00 32.02 ? 8   MET D C   1 
ATOM   5594 O O   . MET D 1 8   ? 2.253   -22.559 4.019   1.00 30.44 ? 8   MET D O   1 
ATOM   5595 C CB  . MET D 1 8   ? 0.005   -20.484 5.224   1.00 28.23 ? 8   MET D CB  1 
ATOM   5596 C CG  . MET D 1 8   ? -0.918  -21.055 4.179   1.00 35.01 ? 8   MET D CG  1 
ATOM   5597 S SD  . MET D 1 8   ? -1.498  -22.788 4.398   1.00 39.84 ? 8   MET D SD  1 
ATOM   5598 C CE  . MET D 1 8   ? -1.878  -22.839 6.148   1.00 35.34 ? 8   MET D CE  1 
ATOM   5599 N N   . LEU D 1 9   ? 3.116   -20.569 4.658   1.00 29.84 ? 9   LEU D N   1 
ATOM   5600 C CA  . LEU D 1 9   ? 4.232   -20.675 3.722   1.00 30.20 ? 9   LEU D CA  1 
ATOM   5601 C C   . LEU D 1 9   ? 5.188   -21.786 4.128   1.00 28.70 ? 9   LEU D C   1 
ATOM   5602 O O   . LEU D 1 9   ? 5.633   -22.565 3.277   1.00 25.80 ? 9   LEU D O   1 
ATOM   5603 C CB  . LEU D 1 9   ? 4.968   -19.327 3.602   1.00 29.34 ? 9   LEU D CB  1 
ATOM   5604 C CG  . LEU D 1 9   ? 4.076   -18.124 3.217   1.00 27.17 ? 9   LEU D CG  1 
ATOM   5605 C CD1 . LEU D 1 9   ? 4.635   -16.810 3.723   1.00 32.54 ? 9   LEU D CD1 1 
ATOM   5606 C CD2 . LEU D 1 9   ? 3.842   -18.065 1.728   1.00 26.25 ? 9   LEU D CD2 1 
ATOM   5607 N N   . GLN D 1 10  ? 5.507   -21.872 5.423   1.00 31.03 ? 10  GLN D N   1 
ATOM   5608 C CA  . GLN D 1 10  ? 6.372   -22.938 5.926   1.00 30.69 ? 10  GLN D CA  1 
ATOM   5609 C C   . GLN D 1 10  ? 5.751   -24.292 5.631   1.00 33.82 ? 10  GLN D C   1 
ATOM   5610 O O   . GLN D 1 10  ? 6.443   -25.238 5.217   1.00 33.08 ? 10  GLN D O   1 
ATOM   5611 C CB  . GLN D 1 10  ? 6.569   -22.767 7.432   1.00 32.52 ? 10  GLN D CB  1 
ATOM   5612 C CG  . GLN D 1 10  ? 7.711   -21.872 7.842   1.00 32.89 ? 10  GLN D CG  1 
ATOM   5613 C CD  . GLN D 1 10  ? 7.658   -21.501 9.320   1.00 37.98 ? 10  GLN D CD  1 
ATOM   5614 O OE1 . GLN D 1 10  ? 6.926   -22.123 10.111  1.00 43.18 ? 10  GLN D OE1 1 
ATOM   5615 N NE2 . GLN D 1 10  ? 8.482   -20.526 9.721   1.00 36.25 ? 10  GLN D NE2 1 
ATOM   5616 N N   . ASP D 1 11  ? 4.440   -24.405 5.841   1.00 32.71 ? 11  ASP D N   1 
ATOM   5617 C CA  . ASP D 1 11  ? 3.744   -25.651 5.556   1.00 32.48 ? 11  ASP D CA  1 
ATOM   5618 C C   . ASP D 1 11  ? 3.768   -25.983 4.069   1.00 33.27 ? 11  ASP D C   1 
ATOM   5619 O O   . ASP D 1 11  ? 3.960   -27.147 3.701   1.00 30.83 ? 11  ASP D O   1 
ATOM   5620 C CB  . ASP D 1 11  ? 2.278   -25.548 6.024   1.00 33.76 ? 11  ASP D CB  1 
ATOM   5621 C CG  . ASP D 1 11  ? 1.503   -26.845 5.817   1.00 33.61 ? 11  ASP D CG  1 
ATOM   5622 O OD1 . ASP D 1 11  ? 1.683   -27.753 6.661   1.00 37.77 ? 11  ASP D OD1 1 
ATOM   5623 O OD2 . ASP D 1 11  ? 0.780   -26.976 4.781   1.00 33.94 ? 11  ASP D OD2 1 
ATOM   5624 N N   . GLY D 1 12  ? 3.507   -24.989 3.194   1.00 30.15 ? 12  GLY D N   1 
ATOM   5625 C CA  . GLY D 1 12  ? 3.485   -25.263 1.760   1.00 27.05 ? 12  GLY D CA  1 
ATOM   5626 C C   . GLY D 1 12  ? 4.850   -25.658 1.199   1.00 28.90 ? 12  GLY D C   1 
ATOM   5627 O O   . GLY D 1 12  ? 4.932   -26.449 0.246   1.00 28.26 ? 12  GLY D O   1 
ATOM   5628 N N   . ALA D 1 13  ? 5.927   -25.091 1.755   1.00 29.48 ? 13  ALA D N   1 
ATOM   5629 C CA  . ALA D 1 13  ? 7.272   -25.415 1.289   1.00 27.56 ? 13  ALA D CA  1 
ATOM   5630 C C   . ALA D 1 13  ? 7.613   -26.858 1.628   1.00 30.36 ? 13  ALA D C   1 
ATOM   5631 O O   . ALA D 1 13  ? 8.186   -27.586 0.801   1.00 29.10 ? 13  ALA D O   1 
ATOM   5632 C CB  . ALA D 1 13  ? 8.301   -24.463 1.913   1.00 26.37 ? 13  ALA D CB  1 
ATOM   5633 N N   . LYS D 1 14  ? 7.245   -27.274 2.841   1.00 32.97 ? 14  LYS D N   1 
ATOM   5634 C CA  . LYS D 1 14  ? 7.392   -28.665 3.276   1.00 35.21 ? 14  LYS D CA  1 
ATOM   5635 C C   . LYS D 1 14  ? 6.774   -29.627 2.279   1.00 35.00 ? 14  LYS D C   1 
ATOM   5636 O O   . LYS D 1 14  ? 7.412   -30.601 1.856   1.00 32.24 ? 14  LYS D O   1 
ATOM   5637 C CB  . LYS D 1 14  ? 6.713   -28.836 4.627   1.00 35.28 ? 14  LYS D CB  1 
ATOM   5638 C CG  . LYS D 1 14  ? 7.593   -28.471 5.809   1.00 39.44 ? 14  LYS D CG  1 
ATOM   5639 C CD  . LYS D 1 14  ? 7.140   -29.246 7.037   1.00 45.98 ? 14  LYS D CD  1 
ATOM   5640 C CE  . LYS D 1 14  ? 7.045   -28.299 8.233   1.00 48.56 ? 14  LYS D CE  1 
ATOM   5641 N NZ  . LYS D 1 14  ? 8.340   -28.151 8.957   1.00 55.15 ? 14  LYS D NZ  1 
ATOM   5642 N N   . ARG D 1 15  ? 5.539   -29.341 1.855   1.00 31.25 ? 15  ARG D N   1 
ATOM   5643 C CA  . ARG D 1 15  ? 4.866   -30.242 0.926   1.00 33.97 ? 15  ARG D CA  1 
ATOM   5644 C C   . ARG D 1 15  ? 5.500   -30.196 -0.462  1.00 31.52 ? 15  ARG D C   1 
ATOM   5645 O O   . ARG D 1 15  ? 5.576   -31.226 -1.142  1.00 30.52 ? 15  ARG D O   1 
ATOM   5646 C CB  . ARG D 1 15  ? 3.356   -29.917 0.921   1.00 31.72 ? 15  ARG D CB  1 
ATOM   5647 C CG  . ARG D 1 15  ? 2.795   -29.946 2.364   1.00 31.50 ? 15  ARG D CG  1 
ATOM   5648 C CD  . ARG D 1 15  ? 1.256   -29.799 2.483   1.00 33.01 ? 15  ARG D CD  1 
ATOM   5649 N NE  . ARG D 1 15  ? 0.676   -29.232 1.272   1.00 36.77 ? 15  ARG D NE  1 
ATOM   5650 C CZ  . ARG D 1 15  ? 0.207   -27.997 1.146   1.00 31.91 ? 15  ARG D CZ  1 
ATOM   5651 N NH1 . ARG D 1 15  ? 0.210   -27.141 2.169   1.00 33.30 ? 15  ARG D NH1 1 
ATOM   5652 N NH2 . ARG D 1 15  ? -0.269  -27.612 -0.041  1.00 30.76 ? 15  ARG D NH2 1 
ATOM   5653 N N   . MET D 1 16  ? 5.958   -29.009 -0.905  1.00 31.92 ? 16  MET D N   1 
ATOM   5654 C CA  . MET D 1 16  ? 6.705   -28.893 -2.166  1.00 30.62 ? 16  MET D CA  1 
ATOM   5655 C C   . MET D 1 16  ? 7.987   -29.719 -2.136  1.00 29.87 ? 16  MET D C   1 
ATOM   5656 O O   . MET D 1 16  ? 8.331   -30.393 -3.109  1.00 27.12 ? 16  MET D O   1 
ATOM   5657 C CB  . MET D 1 16  ? 7.045   -27.412 -2.453  1.00 28.84 ? 16  MET D CB  1 
ATOM   5658 C CG  . MET D 1 16  ? 5.792   -26.587 -2.758  1.00 26.52 ? 16  MET D CG  1 
ATOM   5659 S SD  . MET D 1 16  ? 5.117   -26.989 -4.395  1.00 31.28 ? 16  MET D SD  1 
ATOM   5660 C CE  . MET D 1 16  ? 6.322   -26.514 -5.517  1.00 31.11 ? 16  MET D CE  1 
ATOM   5661 N N   . PHE D 1 17  ? 8.749   -29.581 -1.051  1.00 30.07 ? 17  PHE D N   1 
ATOM   5662 C CA  . PHE D 1 17  ? 10.004  -30.308 -0.869  1.00 32.19 ? 17  PHE D CA  1 
ATOM   5663 C C   . PHE D 1 17  ? 9.753   -31.822 -0.809  1.00 33.35 ? 17  PHE D C   1 
ATOM   5664 O O   . PHE D 1 17  ? 10.472  -32.614 -1.431  1.00 29.16 ? 17  PHE D O   1 
ATOM   5665 C CB  . PHE D 1 17  ? 10.670  -29.811 0.424   1.00 25.79 ? 17  PHE D CB  1 
ATOM   5666 C CG  . PHE D 1 17  ? 12.089  -30.262 0.612   1.00 30.01 ? 17  PHE D CG  1 
ATOM   5667 C CD1 . PHE D 1 17  ? 12.985  -30.260 -0.453  1.00 26.48 ? 17  PHE D CD1 1 
ATOM   5668 C CD2 . PHE D 1 17  ? 12.536  -30.685 1.872   1.00 31.07 ? 17  PHE D CD2 1 
ATOM   5669 C CE1 . PHE D 1 17  ? 14.308  -30.661 -0.268  1.00 29.97 ? 17  PHE D CE1 1 
ATOM   5670 C CE2 . PHE D 1 17  ? 13.861  -31.103 2.076   1.00 32.62 ? 17  PHE D CE2 1 
ATOM   5671 C CZ  . PHE D 1 17  ? 14.754  -31.080 1.019   1.00 30.70 ? 17  PHE D CZ  1 
ATOM   5672 N N   . LYS D 1 18  ? 8.735   -32.243 -0.038  1.00 35.13 ? 18  LYS D N   1 
ATOM   5673 C CA  . LYS D 1 18  ? 8.430   -33.673 0.034   1.00 33.58 ? 18  LYS D CA  1 
ATOM   5674 C C   . LYS D 1 18  ? 7.963   -34.186 -1.311  1.00 31.47 ? 18  LYS D C   1 
ATOM   5675 O O   . LYS D 1 18  ? 8.300   -35.300 -1.711  1.00 34.86 ? 18  LYS D O   1 
ATOM   5676 C CB  . LYS D 1 18  ? 7.405   -33.980 1.123   1.00 35.29 ? 18  LYS D CB  1 
ATOM   5677 C CG  . LYS D 1 18  ? 7.805   -33.534 2.532   1.00 37.58 ? 18  LYS D CG  1 
ATOM   5678 C CD  . LYS D 1 18  ? 9.257   -33.968 2.921   1.00 46.52 ? 18  LYS D CD  1 
ATOM   5679 C CE  . LYS D 1 18  ? 9.893   -33.013 3.983   1.00 44.53 ? 18  LYS D CE  1 
ATOM   5680 N NZ  . LYS D 1 18  ? 9.283   -31.621 3.897   1.00 30.36 ? 18  LYS D NZ  1 
ATOM   5681 N N   . TRP D 1 19  ? 7.203   -33.388 -2.033  1.00 31.13 ? 19  TRP D N   1 
ATOM   5682 C CA  . TRP D 1 19  ? 6.756   -33.813 -3.351  1.00 33.37 ? 19  TRP D CA  1 
ATOM   5683 C C   . TRP D 1 19  ? 7.940   -34.002 -4.282  1.00 34.56 ? 19  TRP D C   1 
ATOM   5684 O O   . TRP D 1 19  ? 7.974   -34.942 -5.083  1.00 34.90 ? 19  TRP D O   1 
ATOM   5685 C CB  . TRP D 1 19  ? 5.731   -32.812 -3.916  1.00 33.40 ? 19  TRP D CB  1 
ATOM   5686 C CG  . TRP D 1 19  ? 5.254   -33.131 -5.336  1.00 32.80 ? 19  TRP D CG  1 
ATOM   5687 C CD1 . TRP D 1 19  ? 5.880   -32.788 -6.502  1.00 34.83 ? 19  TRP D CD1 1 
ATOM   5688 C CD2 . TRP D 1 19  ? 4.096   -33.889 -5.720  1.00 34.10 ? 19  TRP D CD2 1 
ATOM   5689 N NE1 . TRP D 1 19  ? 5.188   -33.268 -7.592  1.00 33.32 ? 19  TRP D NE1 1 
ATOM   5690 C CE2 . TRP D 1 19  ? 4.087   -33.949 -7.139  1.00 35.36 ? 19  TRP D CE2 1 
ATOM   5691 C CE3 . TRP D 1 19  ? 3.058   -34.509 -5.010  1.00 37.55 ? 19  TRP D CE3 1 
ATOM   5692 C CZ2 . TRP D 1 19  ? 3.090   -34.597 -7.855  1.00 35.26 ? 19  TRP D CZ2 1 
ATOM   5693 C CZ3 . TRP D 1 19  ? 2.057   -35.170 -5.731  1.00 37.67 ? 19  TRP D CZ3 1 
ATOM   5694 C CH2 . TRP D 1 19  ? 2.089   -35.203 -7.142  1.00 39.82 ? 19  TRP D CH2 1 
ATOM   5695 N N   . LEU D 1 20  ? 8.932   -33.111 -4.192  1.00 37.71 ? 20  LEU D N   1 
ATOM   5696 C CA  . LEU D 1 20  ? 10.068  -33.149 -5.100  1.00 33.21 ? 20  LEU D CA  1 
ATOM   5697 C C   . LEU D 1 20  ? 10.939  -34.390 -4.916  1.00 33.21 ? 20  LEU D C   1 
ATOM   5698 O O   . LEU D 1 20  ? 11.471  -34.899 -5.903  1.00 35.60 ? 20  LEU D O   1 
ATOM   5699 C CB  . LEU D 1 20  ? 10.887  -31.863 -4.935  1.00 33.47 ? 20  LEU D CB  1 
ATOM   5700 C CG  . LEU D 1 20  ? 10.408  -30.722 -5.821  1.00 32.48 ? 20  LEU D CG  1 
ATOM   5701 C CD1 . LEU D 1 20  ? 11.167  -29.420 -5.430  1.00 29.50 ? 20  LEU D CD1 1 
ATOM   5702 C CD2 . LEU D 1 20  ? 10.628  -31.034 -7.300  1.00 32.34 ? 20  LEU D CD2 1 
ATOM   5703 N N   . ARG D 1 21  ? 10.927  -34.904 -3.697  1.00 31.09 ? 21  ARG D N   1 
ATOM   5704 C CA  . ARG D 1 21  ? 11.654  -36.122 -3.271  1.00 38.87 ? 21  ARG D CA  1 
ATOM   5705 C C   . ARG D 1 21  ? 11.339  -37.295 -4.216  1.00 41.52 ? 21  ARG D C   1 
ATOM   5706 O O   . ARG D 1 21  ? 12.150  -38.186 -4.302  1.00 44.53 ? 21  ARG D O   1 
ATOM   5707 C CB  . ARG D 1 21  ? 11.336  -36.363 -1.791  1.00 41.38 ? 21  ARG D CB  1 
ATOM   5708 C CG  . ARG D 1 21  ? 11.712  -37.722 -1.236  1.00 44.56 ? 21  ARG D CG  1 
ATOM   5709 C CD  . ARG D 1 21  ? 12.406  -37.672 0.104   1.00 51.45 ? 21  ARG D CD  1 
ATOM   5710 N NE  . ARG D 1 21  ? 11.703  -37.285 1.312   1.00 50.37 ? 21  ARG D NE  1 
ATOM   5711 C CZ  . ARG D 1 21  ? 10.395  -37.107 1.441   1.00 57.46 ? 21  ARG D CZ  1 
ATOM   5712 N NH1 . ARG D 1 21  ? 9.591   -37.287 0.416   1.00 53.86 ? 21  ARG D NH1 1 
ATOM   5713 N NH2 . ARG D 1 21  ? 9.893   -36.746 2.604   1.00 58.28 ? 21  ARG D NH2 1 
ATOM   5714 N N   . LYS D 1 22  ? 10.218  -37.263 -4.935  1.00 40.35 ? 22  LYS D N   1 
ATOM   5715 C CA  . LYS D 1 22  ? 9.878   -38.336 -5.851  1.00 41.39 ? 22  LYS D CA  1 
ATOM   5716 C C   . LYS D 1 22  ? 10.690  -38.279 -7.145  1.00 37.20 ? 22  LYS D C   1 
ATOM   5717 O O   . LYS D 1 22  ? 10.702  -39.261 -7.901  1.00 41.34 ? 22  LYS D O   1 
ATOM   5718 C CB  . LYS D 1 22  ? 8.375   -38.275 -6.135  1.00 37.34 ? 22  LYS D CB  1 
ATOM   5719 C CG  . LYS D 1 22  ? 7.585   -38.374 -4.846  1.00 40.57 ? 22  LYS D CG  1 
ATOM   5720 C CD  . LYS D 1 22  ? 6.132   -38.759 -5.091  1.00 43.63 ? 22  LYS D CD  1 
ATOM   5721 C CE  . LYS D 1 22  ? 5.644   -38.196 -6.408  1.00 40.51 ? 22  LYS D CE  1 
ATOM   5722 N NZ  . LYS D 1 22  ? 5.268   -36.762 -6.266  1.00 45.08 ? 22  LYS D NZ  1 
ATOM   5723 N N   . GLY D 1 23  ? 11.352  -37.168 -7.436  1.00 37.34 ? 23  GLY D N   1 
ATOM   5724 C CA  . GLY D 1 23  ? 12.103  -37.080 -8.679  1.00 39.27 ? 23  GLY D CA  1 
ATOM   5725 C C   . GLY D 1 23  ? 11.232  -37.055 -9.918  1.00 40.82 ? 23  GLY D C   1 
ATOM   5726 O O   . GLY D 1 23  ? 11.708  -37.378 -11.012 1.00 44.47 ? 23  GLY D O   1 
ATOM   5727 N N   . GLU D 1 24  ? 9.971   -36.652 -9.781  1.00 40.43 ? 24  GLU D N   1 
ATOM   5728 C CA  . GLU D 1 24  ? 9.014   -36.585 -10.884 1.00 40.88 ? 24  GLU D CA  1 
ATOM   5729 C C   . GLU D 1 24  ? 8.642   -35.143 -11.267 1.00 42.31 ? 24  GLU D C   1 
ATOM   5730 O O   . GLU D 1 24  ? 7.539   -34.904 -11.752 1.00 38.32 ? 24  GLU D O   1 
ATOM   5731 C CB  . GLU D 1 24  ? 7.764   -37.390 -10.521 1.00 35.05 ? 24  GLU D CB  1 
ATOM   5732 C CG  . GLU D 1 24  ? 8.049   -38.895 -10.396 1.00 39.95 ? 24  GLU D CG  1 
ATOM   5733 C CD  . GLU D 1 24  ? 7.014   -39.658 -9.611  1.00 43.51 ? 24  GLU D CD  1 
ATOM   5734 O OE1 . GLU D 1 24  ? 5.874   -39.153 -9.452  1.00 46.79 ? 24  GLU D OE1 1 
ATOM   5735 O OE2 . GLU D 1 24  ? 7.336   -40.778 -9.153  1.00 48.56 ? 24  GLU D OE2 1 
ATOM   5736 N N   . GLY D 1 25  ? 9.477   -34.146 -10.885 1.00 39.12 ? 25  GLY D N   1 
ATOM   5737 C CA  . GLY D 1 25  ? 9.181   -32.744 -11.143 1.00 38.10 ? 25  GLY D CA  1 
ATOM   5738 C C   . GLY D 1 25  ? 8.226   -32.080 -10.148 1.00 33.85 ? 25  GLY D C   1 
ATOM   5739 O O   . GLY D 1 25  ? 7.856   -32.618 -9.091  1.00 32.24 ? 25  GLY D O   1 
ATOM   5740 N N   . LEU D 1 26  ? 7.883   -30.823 -10.480 1.00 34.75 ? 26  LEU D N   1 
ATOM   5741 C CA  . LEU D 1 26  ? 7.048   -29.981 -9.635  1.00 37.60 ? 26  LEU D CA  1 
ATOM   5742 C C   . LEU D 1 26  ? 5.566   -30.370 -9.766  1.00 33.07 ? 26  LEU D C   1 
ATOM   5743 O O   . LEU D 1 26  ? 5.119   -30.778 -10.843 1.00 33.19 ? 26  LEU D O   1 
ATOM   5744 C CB  . LEU D 1 26  ? 7.231   -28.506 -10.007 1.00 34.70 ? 26  LEU D CB  1 
ATOM   5745 C CG  . LEU D 1 26  ? 8.586   -27.852 -9.681  1.00 33.85 ? 26  LEU D CG  1 
ATOM   5746 C CD1 . LEU D 1 26  ? 8.769   -26.583 -10.508 1.00 32.51 ? 26  LEU D CD1 1 
ATOM   5747 C CD2 . LEU D 1 26  ? 8.717   -27.509 -8.183  1.00 32.03 ? 26  LEU D CD2 1 
ATOM   5748 N N   . PRO D 1 27  ? 4.780   -30.186 -8.707  1.00 34.78 ? 27  PRO D N   1 
ATOM   5749 C CA  . PRO D 1 27  ? 3.350   -30.536 -8.780  1.00 36.01 ? 27  PRO D CA  1 
ATOM   5750 C C   . PRO D 1 27  ? 2.574   -29.580 -9.674  1.00 37.64 ? 27  PRO D C   1 
ATOM   5751 O O   . PRO D 1 27  ? 3.008   -28.464 -9.995  1.00 32.33 ? 27  PRO D O   1 
ATOM   5752 C CB  . PRO D 1 27  ? 2.877   -30.421 -7.333  1.00 33.25 ? 27  PRO D CB  1 
ATOM   5753 C CG  . PRO D 1 27  ? 3.756   -29.377 -6.752  1.00 33.90 ? 27  PRO D CG  1 
ATOM   5754 C CD  . PRO D 1 27  ? 5.112   -29.509 -7.432  1.00 30.74 ? 27  PRO D CD  1 
ATOM   5755 N N   . ASN D 1 28  ? 1.391   -30.042 -10.074 1.00 36.96 ? 28  ASN D N   1 
ATOM   5756 C CA  . ASN D 1 28  ? 0.563   -29.243 -10.959 1.00 38.77 ? 28  ASN D CA  1 
ATOM   5757 C C   . ASN D 1 28  ? -0.056  -28.057 -10.251 1.00 32.31 ? 28  ASN D C   1 
ATOM   5758 O O   . ASN D 1 28  ? -0.416  -27.088 -10.913 1.00 35.02 ? 28  ASN D O   1 
ATOM   5759 C CB  . ASN D 1 28  ? -0.532  -30.122 -11.580 1.00 41.65 ? 28  ASN D CB  1 
ATOM   5760 C CG  . ASN D 1 28  ? 0.033   -31.091 -12.595 1.00 47.56 ? 28  ASN D CG  1 
ATOM   5761 O OD1 . ASN D 1 28  ? 1.098   -30.837 -13.167 1.00 43.89 ? 28  ASN D OD1 1 
ATOM   5762 N ND2 . ASN D 1 28  ? -0.650  -32.223 -12.800 1.00 51.25 ? 28  ASN D ND2 1 
ATOM   5763 N N   . TYR D 1 29  ? -0.192  -28.114 -8.933  1.00 33.05 ? 29  TYR D N   1 
ATOM   5764 C CA  . TYR D 1 29  ? -0.746  -27.016 -8.161  1.00 32.59 ? 29  TYR D CA  1 
ATOM   5765 C C   . TYR D 1 29  ? -0.391  -27.268 -6.708  1.00 31.38 ? 29  TYR D C   1 
ATOM   5766 O O   . TYR D 1 29  ? -0.055  -28.385 -6.323  1.00 35.65 ? 29  TYR D O   1 
ATOM   5767 C CB  . TYR D 1 29  ? -2.268  -26.879 -8.368  1.00 37.65 ? 29  TYR D CB  1 
ATOM   5768 C CG  . TYR D 1 29  ? -3.077  -28.076 -7.889  1.00 42.05 ? 29  TYR D CG  1 
ATOM   5769 C CD1 . TYR D 1 29  ? -3.061  -28.478 -6.555  1.00 39.86 ? 29  TYR D CD1 1 
ATOM   5770 C CD2 . TYR D 1 29  ? -3.829  -28.825 -8.787  1.00 46.87 ? 29  TYR D CD2 1 
ATOM   5771 C CE1 . TYR D 1 29  ? -3.768  -29.560 -6.131  1.00 42.80 ? 29  TYR D CE1 1 
ATOM   5772 C CE2 . TYR D 1 29  ? -4.575  -29.908 -8.364  1.00 45.98 ? 29  TYR D CE2 1 
ATOM   5773 C CZ  . TYR D 1 29  ? -4.533  -30.280 -7.035  1.00 48.75 ? 29  TYR D CZ  1 
ATOM   5774 O OH  . TYR D 1 29  ? -5.252  -31.373 -6.579  1.00 51.74 ? 29  TYR D OH  1 
ATOM   5775 N N   . LEU D 1 30  ? -0.517  -26.234 -5.896  1.00 30.78 ? 30  LEU D N   1 
ATOM   5776 C CA  . LEU D 1 30  ? -0.177  -26.310 -4.485  1.00 31.01 ? 30  LEU D CA  1 
ATOM   5777 C C   . LEU D 1 30  ? -1.317  -25.689 -3.710  1.00 34.16 ? 30  LEU D C   1 
ATOM   5778 O O   . LEU D 1 30  ? -1.700  -24.553 -4.004  1.00 29.55 ? 30  LEU D O   1 
ATOM   5779 C CB  . LEU D 1 30  ? 1.152   -25.584 -4.172  1.00 28.88 ? 30  LEU D CB  1 
ATOM   5780 C CG  . LEU D 1 30  ? 1.520   -25.423 -2.691  1.00 27.30 ? 30  LEU D CG  1 
ATOM   5781 C CD1 . LEU D 1 30  ? 2.145   -26.757 -2.217  1.00 29.81 ? 30  LEU D CD1 1 
ATOM   5782 C CD2 . LEU D 1 30  ? 2.566   -24.269 -2.462  1.00 26.74 ? 30  LEU D CD2 1 
ATOM   5783 N N   . ILE D 1 31  ? -1.867  -26.439 -2.742  1.00 35.02 ? 31  ILE D N   1 
ATOM   5784 C CA  . ILE D 1 31  ? -3.024  -25.987 -1.981  1.00 32.88 ? 31  ILE D CA  1 
ATOM   5785 C C   . ILE D 1 31  ? -2.536  -25.111 -0.843  1.00 31.88 ? 31  ILE D C   1 
ATOM   5786 O O   . ILE D 1 31  ? -1.643  -25.512 -0.093  1.00 33.91 ? 31  ILE D O   1 
ATOM   5787 C CB  . ILE D 1 31  ? -3.823  -27.196 -1.459  1.00 33.43 ? 31  ILE D CB  1 
ATOM   5788 C CG1 . ILE D 1 31  ? -4.420  -27.956 -2.637  1.00 35.19 ? 31  ILE D CG1 1 
ATOM   5789 C CG2 . ILE D 1 31  ? -4.900  -26.756 -0.496  1.00 30.59 ? 31  ILE D CG2 1 
ATOM   5790 C CD1 . ILE D 1 31  ? -4.834  -29.380 -2.287  1.00 40.12 ? 31  ILE D CD1 1 
ATOM   5791 N N   . MET D 1 32  ? -3.121  -23.906 -0.720  1.00 33.17 ? 32  MET D N   1 
ATOM   5792 C CA  . MET D 1 32  ? -2.771  -22.939 0.311   1.00 31.33 ? 32  MET D CA  1 
ATOM   5793 C C   . MET D 1 32  ? -4.036  -22.269 0.855   1.00 35.27 ? 32  MET D C   1 
ATOM   5794 O O   . MET D 1 32  ? -5.021  -22.118 0.141   1.00 34.62 ? 32  MET D O   1 
ATOM   5795 C CB  . MET D 1 32  ? -1.811  -21.872 -0.265  1.00 30.91 ? 32  MET D CB  1 
ATOM   5796 C CG  . MET D 1 32  ? -0.377  -22.444 -0.706  1.00 27.48 ? 32  MET D CG  1 
ATOM   5797 S SD  . MET D 1 32  ? 0.573   -22.728 0.747   1.00 32.33 ? 32  MET D SD  1 
ATOM   5798 C CE  . MET D 1 32  ? 1.644   -21.190 0.881   1.00 27.77 ? 32  MET D CE  1 
ATOM   5799 N N   . TYR D 1 33  ? -4.001  -21.870 2.132   1.00 34.35 ? 33  TYR D N   1 
ATOM   5800 C CA  . TYR D 1 33  ? -5.136  -21.234 2.799   1.00 38.17 ? 33  TYR D CA  1 
ATOM   5801 C C   . TYR D 1 33  ? -4.798  -19.799 3.185   1.00 38.01 ? 33  TYR D C   1 
ATOM   5802 O O   . TYR D 1 33  ? -3.828  -19.566 3.914   1.00 40.24 ? 33  TYR D O   1 
ATOM   5803 C CB  . TYR D 1 33  ? -5.576  -22.052 4.019   1.00 37.53 ? 33  TYR D CB  1 
ATOM   5804 C CG  . TYR D 1 33  ? -5.947  -23.485 3.614   1.00 38.11 ? 33  TYR D CG  1 
ATOM   5805 C CD1 . TYR D 1 33  ? -4.951  -24.416 3.290   1.00 34.48 ? 33  TYR D CD1 1 
ATOM   5806 C CD2 . TYR D 1 33  ? -7.284  -23.872 3.469   1.00 34.82 ? 33  TYR D CD2 1 
ATOM   5807 C CE1 . TYR D 1 33  ? -5.277  -25.723 2.887   1.00 35.49 ? 33  TYR D CE1 1 
ATOM   5808 C CE2 . TYR D 1 33  ? -7.616  -25.166 3.067   1.00 34.28 ? 33  TYR D CE2 1 
ATOM   5809 C CZ  . TYR D 1 33  ? -6.608  -26.082 2.779   1.00 35.81 ? 33  TYR D CZ  1 
ATOM   5810 O OH  . TYR D 1 33  ? -6.901  -27.371 2.367   1.00 36.17 ? 33  TYR D OH  1 
ATOM   5811 N N   . ASP D 1 34  ? -5.634  -18.855 2.739   1.00 37.88 ? 34  ASP D N   1 
ATOM   5812 C CA  . ASP D 1 34  ? -5.461  -17.434 3.041   1.00 37.34 ? 34  ASP D CA  1 
ATOM   5813 C C   . ASP D 1 34  ? -5.459  -17.192 4.553   1.00 38.61 ? 34  ASP D C   1 
ATOM   5814 O O   . ASP D 1 34  ? -6.112  -17.892 5.331   1.00 41.97 ? 34  ASP D O   1 
ATOM   5815 C CB  . ASP D 1 34  ? -6.588  -16.645 2.332   1.00 43.08 ? 34  ASP D CB  1 
ATOM   5816 C CG  . ASP D 1 34  ? -6.815  -15.245 2.911   1.00 46.36 ? 34  ASP D CG  1 
ATOM   5817 O OD1 . ASP D 1 34  ? -7.512  -15.216 3.947   1.00 38.71 ? 34  ASP D OD1 1 
ATOM   5818 O OD2 . ASP D 1 34  ? -6.305  -14.184 2.358   1.00 46.44 ? 34  ASP D OD2 1 
ATOM   5819 N N   . MET D 1 35  ? -4.742  -16.173 4.978   1.00 36.09 ? 35  MET D N   1 
ATOM   5820 C CA  . MET D 1 35  ? -4.619  -15.932 6.402   1.00 34.45 ? 35  MET D CA  1 
ATOM   5821 C C   . MET D 1 35  ? -5.756  -15.097 6.975   1.00 39.10 ? 35  MET D C   1 
ATOM   5822 O O   . MET D 1 35  ? -5.869  -15.006 8.201   1.00 37.06 ? 35  MET D O   1 
ATOM   5823 C CB  . MET D 1 35  ? -3.273  -15.288 6.707   1.00 36.53 ? 35  MET D CB  1 
ATOM   5824 C CG  . MET D 1 35  ? -3.263  -13.787 6.836   1.00 37.36 ? 35  MET D CG  1 
ATOM   5825 S SD  . MET D 1 35  ? -1.553  -13.088 6.887   1.00 40.00 ? 35  MET D SD  1 
ATOM   5826 C CE  . MET D 1 35  ? -1.245  -12.974 8.639   1.00 33.02 ? 35  MET D CE  1 
ATOM   5827 N N   . ASP D 1 36  ? -6.605  -14.518 6.122   1.00 36.95 ? 36  ASP D N   1 
ATOM   5828 C CA  . ASP D 1 36  ? -7.671  -13.600 6.497   1.00 41.16 ? 36  ASP D CA  1 
ATOM   5829 C C   . ASP D 1 36  ? -9.011  -14.313 6.640   1.00 44.80 ? 36  ASP D C   1 
ATOM   5830 O O   . ASP D 1 36  ? -9.722  -14.101 7.625   1.00 48.95 ? 36  ASP D O   1 
ATOM   5831 C CB  . ASP D 1 36  ? -7.775  -12.467 5.468   1.00 39.54 ? 36  ASP D CB  1 
ATOM   5832 C CG  . ASP D 1 36  ? -6.465  -11.704 5.315   1.00 42.69 ? 36  ASP D CG  1 
ATOM   5833 O OD1 . ASP D 1 36  ? -6.041  -11.043 6.290   1.00 40.39 ? 36  ASP D OD1 1 
ATOM   5834 O OD2 . ASP D 1 36  ? -5.849  -11.792 4.225   1.00 43.18 ? 36  ASP D OD2 1 
ATOM   5835 N N   . ARG D 1 37  ? -9.395  -15.118 5.652   1.00 44.27 ? 37  ARG D N   1 
ATOM   5836 C CA  . ARG D 1 37  ? -10.645 -15.861 5.684   1.00 41.44 ? 37  ARG D CA  1 
ATOM   5837 C C   . ARG D 1 37  ? -10.455 -17.376 5.730   1.00 45.69 ? 37  ARG D C   1 
ATOM   5838 O O   . ARG D 1 37  ? -11.450 -18.110 5.723   1.00 40.41 ? 37  ARG D O   1 
ATOM   5839 C CB  . ARG D 1 37  ? -11.490 -15.454 4.475   1.00 43.72 ? 37  ARG D CB  1 
ATOM   5840 C CG  . ARG D 1 37  ? -11.702 -13.938 4.429   1.00 48.36 ? 37  ARG D CG  1 
ATOM   5841 C CD  . ARG D 1 37  ? -13.157 -13.585 4.125   1.00 52.61 ? 37  ARG D CD  1 
ATOM   5842 N NE  . ARG D 1 37  ? -14.097 -14.507 4.767   1.00 52.84 ? 37  ARG D NE  1 
ATOM   5843 C CZ  . ARG D 1 37  ? -15.290 -14.822 4.274   1.00 53.80 ? 37  ARG D CZ  1 
ATOM   5844 N NH1 . ARG D 1 37  ? -15.707 -14.336 3.113   1.00 56.13 ? 37  ARG D NH1 1 
ATOM   5845 N NH2 . ARG D 1 37  ? -16.077 -15.657 4.953   1.00 53.26 ? 37  ARG D NH2 1 
ATOM   5846 N N   . ASN D 1 38  ? -9.209  -17.858 5.731   1.00 42.66 ? 38  ASN D N   1 
ATOM   5847 C CA  . ASN D 1 38  ? -8.875  -19.289 5.743   1.00 41.93 ? 38  ASN D CA  1 
ATOM   5848 C C   . ASN D 1 38  ? -9.561  -20.052 4.617   1.00 42.32 ? 38  ASN D C   1 
ATOM   5849 O O   . ASN D 1 38  ? -10.040 -21.175 4.801   1.00 43.98 ? 38  ASN D O   1 
ATOM   5850 C CB  . ASN D 1 38  ? -9.174  -19.924 7.103   1.00 41.27 ? 38  ASN D CB  1 
ATOM   5851 C CG  . ASN D 1 38  ? -8.174  -21.017 7.461   1.00 47.77 ? 38  ASN D CG  1 
ATOM   5852 O OD1 . ASN D 1 38  ? -7.008  -20.985 7.029   1.00 52.39 ? 38  ASN D OD1 1 
ATOM   5853 N ND2 . ASN D 1 38  ? -8.613  -21.991 8.255   1.00 50.66 ? 38  ASN D ND2 1 
ATOM   5854 N N   . LYS D 1 39  ? -9.663  -19.415 3.459   1.00 35.42 ? 39  LYS D N   1 
ATOM   5855 C CA  . LYS D 1 39  ? -10.254 -20.038 2.283   1.00 38.11 ? 39  LYS D CA  1 
ATOM   5856 C C   . LYS D 1 39  ? -9.208  -20.835 1.484   1.00 41.06 ? 39  LYS D C   1 
ATOM   5857 O O   . LYS D 1 39  ? -8.010  -20.510 1.487   1.00 39.29 ? 39  LYS D O   1 
ATOM   5858 C CB  . LYS D 1 39  ? -10.928 -18.988 1.414   1.00 34.14 ? 39  LYS D CB  1 
ATOM   5859 C CG  . LYS D 1 39  ? -10.942 -19.301 -0.062  1.00 39.07 ? 39  LYS D CG  1 
ATOM   5860 C CD  . LYS D 1 39  ? -11.612 -18.202 -0.882  1.00 43.60 ? 39  LYS D CD  1 
ATOM   5861 C CE  . LYS D 1 39  ? -11.507 -18.498 -2.384  1.00 44.64 ? 39  LYS D CE  1 
ATOM   5862 N NZ  . LYS D 1 39  ? -12.833 -18.866 -2.960  1.00 46.97 ? 39  LYS D NZ  1 
ATOM   5863 N N   . GLU D 1 40  ? -9.657  -21.940 0.879   1.00 41.09 ? 40  GLU D N   1 
ATOM   5864 C CA  . GLU D 1 40  ? -8.789  -22.808 0.077   1.00 40.03 ? 40  GLU D CA  1 
ATOM   5865 C C   . GLU D 1 40  ? -8.519  -22.253 -1.319  1.00 39.54 ? 40  GLU D C   1 
ATOM   5866 O O   . GLU D 1 40  ? -9.457  -21.939 -2.052  1.00 36.36 ? 40  GLU D O   1 
ATOM   5867 C CB  . GLU D 1 40  ? -9.417  -24.196 -0.030  1.00 37.83 ? 40  GLU D CB  1 
ATOM   5868 C CG  . GLU D 1 40  ? -8.407  -25.277 -0.378  1.00 35.99 ? 40  GLU D CG  1 
ATOM   5869 C CD  . GLU D 1 40  ? -8.953  -26.671 -0.152  1.00 33.77 ? 40  GLU D CD  1 
ATOM   5870 O OE1 . GLU D 1 40  ? -8.882  -27.188 0.977   1.00 34.12 ? 40  GLU D OE1 1 
ATOM   5871 O OE2 . GLU D 1 40  ? -9.442  -27.243 -1.125  1.00 34.74 ? 40  GLU D OE2 1 
ATOM   5872 N N   . TYR D 1 41  ? -7.223  -22.200 -1.707  1.00 38.31 ? 41  TYR D N   1 
ATOM   5873 C CA  . TYR D 1 41  ? -6.762  -21.753 -3.022  1.00 34.22 ? 41  TYR D CA  1 
ATOM   5874 C C   . TYR D 1 41  ? -5.834  -22.810 -3.609  1.00 36.37 ? 41  TYR D C   1 
ATOM   5875 O O   . TYR D 1 41  ? -4.964  -23.344 -2.900  1.00 35.49 ? 41  TYR D O   1 
ATOM   5876 C CB  . TYR D 1 41  ? -6.008  -20.400 -2.941  1.00 38.19 ? 41  TYR D CB  1 
ATOM   5877 C CG  . TYR D 1 41  ? -6.849  -19.206 -2.519  1.00 35.51 ? 41  TYR D CG  1 
ATOM   5878 C CD1 . TYR D 1 41  ? -6.988  -18.873 -1.184  1.00 37.15 ? 41  TYR D CD1 1 
ATOM   5879 C CD2 . TYR D 1 41  ? -7.504  -18.423 -3.465  1.00 38.06 ? 41  TYR D CD2 1 
ATOM   5880 C CE1 . TYR D 1 41  ? -7.789  -17.775 -0.788  1.00 38.29 ? 41  TYR D CE1 1 
ATOM   5881 C CE2 . TYR D 1 41  ? -8.280  -17.330 -3.097  1.00 36.04 ? 41  TYR D CE2 1 
ATOM   5882 C CZ  . TYR D 1 41  ? -8.406  -16.997 -1.752  1.00 40.41 ? 41  TYR D CZ  1 
ATOM   5883 O OH  . TYR D 1 41  ? -9.179  -15.894 -1.367  1.00 40.33 ? 41  TYR D OH  1 
ATOM   5884 N N   . LYS D 1 42  ? -6.032  -23.153 -4.875  1.00 33.17 ? 42  LYS D N   1 
ATOM   5885 C CA  . LYS D 1 42  ? -5.108  -24.049 -5.555  1.00 38.56 ? 42  LYS D CA  1 
ATOM   5886 C C   . LYS D 1 42  ? -4.230  -23.235 -6.507  1.00 34.59 ? 42  LYS D C   1 
ATOM   5887 O O   . LYS D 1 42  ? -4.557  -23.081 -7.686  1.00 34.73 ? 42  LYS D O   1 
ATOM   5888 C CB  . LYS D 1 42  ? -5.871  -25.167 -6.268  1.00 38.72 ? 42  LYS D CB  1 
ATOM   5889 C CG  . LYS D 1 42  ? -6.453  -26.149 -5.271  1.00 40.79 ? 42  LYS D CG  1 
ATOM   5890 C CD  . LYS D 1 42  ? -7.612  -26.933 -5.879  1.00 52.84 ? 42  LYS D CD  1 
ATOM   5891 C CE  . LYS D 1 42  ? -7.269  -27.465 -7.292  1.00 52.45 ? 42  LYS D CE  1 
ATOM   5892 N NZ  . LYS D 1 42  ? -8.435  -28.186 -7.936  1.00 64.00 ? 42  LYS D NZ  1 
ATOM   5893 N N   . LEU D 1 43  ? -3.042  -22.868 -6.052  1.00 30.70 ? 43  LEU D N   1 
ATOM   5894 C CA  . LEU D 1 43  ? -2.169  -22.039 -6.879  1.00 31.14 ? 43  LEU D CA  1 
ATOM   5895 C C   . LEU D 1 43  ? -1.532  -22.868 -7.984  1.00 28.97 ? 43  LEU D C   1 
ATOM   5896 O O   . LEU D 1 43  ? -0.969  -23.931 -7.730  1.00 31.39 ? 43  LEU D O   1 
ATOM   5897 C CB  . LEU D 1 43  ? -1.086  -21.395 -6.011  1.00 30.65 ? 43  LEU D CB  1 
ATOM   5898 C CG  . LEU D 1 43  ? -1.539  -20.790 -4.703  1.00 30.41 ? 43  LEU D CG  1 
ATOM   5899 C CD1 . LEU D 1 43  ? -0.324  -20.206 -3.979  1.00 29.45 ? 43  LEU D CD1 1 
ATOM   5900 C CD2 . LEU D 1 43  ? -2.558  -19.683 -4.993  1.00 29.65 ? 43  LEU D CD2 1 
ATOM   5901 N N   . VAL D 1 44  ? -1.651  -22.403 -9.218  1.00 29.12 ? 44  VAL D N   1 
ATOM   5902 C CA  . VAL D 1 44  ? -0.953  -23.019 -10.344 1.00 30.32 ? 44  VAL D CA  1 
ATOM   5903 C C   . VAL D 1 44  ? 0.543   -22.687 -10.219 1.00 32.42 ? 44  VAL D C   1 
ATOM   5904 O O   . VAL D 1 44  ? 0.904   -21.858 -9.375  1.00 31.67 ? 44  VAL D O   1 
ATOM   5905 C CB  . VAL D 1 44  ? -1.560  -22.527 -11.674 1.00 34.66 ? 44  VAL D CB  1 
ATOM   5906 C CG1 . VAL D 1 44  ? -3.051  -22.835 -11.720 1.00 31.78 ? 44  VAL D CG1 1 
ATOM   5907 C CG2 . VAL D 1 44  ? -1.361  -21.040 -11.859 1.00 33.08 ? 44  VAL D CG2 1 
ATOM   5908 N N   . PRO D 1 45  ? 1.450   -23.333 -10.965 1.00 31.86 ? 45  PRO D N   1 
ATOM   5909 C CA  . PRO D 1 45  ? 2.909   -23.116 -10.719 1.00 31.93 ? 45  PRO D CA  1 
ATOM   5910 C C   . PRO D 1 45  ? 3.396   -21.682 -10.900 1.00 32.46 ? 45  PRO D C   1 
ATOM   5911 O O   . PRO D 1 45  ? 4.287   -21.242 -10.166 1.00 33.15 ? 45  PRO D O   1 
ATOM   5912 C CB  . PRO D 1 45  ? 3.577   -24.080 -11.697 1.00 29.82 ? 45  PRO D CB  1 
ATOM   5913 C CG  . PRO D 1 45  ? 2.510   -25.240 -11.855 1.00 32.18 ? 45  PRO D CG  1 
ATOM   5914 C CD  . PRO D 1 45  ? 1.210   -24.438 -11.911 1.00 35.82 ? 45  PRO D CD  1 
ATOM   5915 N N   . LYS D 1 46  ? 2.873   -20.943 -11.876 1.00 35.38 ? 46  LYS D N   1 
ATOM   5916 C CA  . LYS D 1 46  ? 3.245   -19.541 -11.981 1.00 33.94 ? 46  LYS D CA  1 
ATOM   5917 C C   . LYS D 1 46  ? 2.918   -18.797 -10.696 1.00 32.69 ? 46  LYS D C   1 
ATOM   5918 O O   . LYS D 1 46  ? 3.649   -17.883 -10.309 1.00 29.81 ? 46  LYS D O   1 
ATOM   5919 C CB  . LYS D 1 46  ? 2.480   -18.883 -13.125 1.00 36.57 ? 46  LYS D CB  1 
ATOM   5920 C CG  . LYS D 1 46  ? 3.167   -18.870 -14.451 1.00 37.58 ? 46  LYS D CG  1 
ATOM   5921 C CD  . LYS D 1 46  ? 2.315   -18.127 -15.497 1.00 43.46 ? 46  LYS D CD  1 
ATOM   5922 C CE  . LYS D 1 46  ? 0.807   -18.329 -15.302 1.00 48.09 ? 46  LYS D CE  1 
ATOM   5923 N NZ  . LYS D 1 46  ? 0.334   -19.713 -15.805 1.00 46.77 ? 46  LYS D NZ  1 
ATOM   5924 N N   . GLU D 1 47  ? 1.825   -19.173 -10.018 1.00 31.08 ? 47  GLU D N   1 
ATOM   5925 C CA  . GLU D 1 47  ? 1.427   -18.447 -8.823  1.00 27.56 ? 47  GLU D CA  1 
ATOM   5926 C C   . GLU D 1 47  ? 2.224   -18.858 -7.611  1.00 28.16 ? 47  GLU D C   1 
ATOM   5927 O O   . GLU D 1 47  ? 2.608   -17.998 -6.811  1.00 28.42 ? 47  GLU D O   1 
ATOM   5928 C CB  . GLU D 1 47  ? -0.061  -18.647 -8.550  1.00 32.87 ? 47  GLU D CB  1 
ATOM   5929 C CG  . GLU D 1 47  ? -0.955  -18.198 -9.679  1.00 29.74 ? 47  GLU D CG  1 
ATOM   5930 C CD  . GLU D 1 47  ? -2.404  -18.539 -9.357  1.00 38.10 ? 47  GLU D CD  1 
ATOM   5931 O OE1 . GLU D 1 47  ? -2.685  -19.748 -9.197  1.00 34.37 ? 47  GLU D OE1 1 
ATOM   5932 O OE2 . GLU D 1 47  ? -3.243  -17.612 -9.240  1.00 35.04 ? 47  GLU D OE2 1 
ATOM   5933 N N   . TYR D 1 48  ? 2.452   -20.168 -7.416  1.00 26.60 ? 48  TYR D N   1 
ATOM   5934 C CA  . TYR D 1 48  ? 3.207   -20.528 -6.233  1.00 28.28 ? 48  TYR D CA  1 
ATOM   5935 C C   . TYR D 1 48  ? 4.688   -20.184 -6.402  1.00 27.39 ? 48  TYR D C   1 
ATOM   5936 O O   . TYR D 1 48  ? 5.363   -19.915 -5.409  1.00 29.63 ? 48  TYR D O   1 
ATOM   5937 C CB  . TYR D 1 48  ? 2.978   -22.008 -5.863  1.00 26.66 ? 48  TYR D CB  1 
ATOM   5938 C CG  . TYR D 1 48  ? 3.468   -23.125 -6.778  1.00 29.22 ? 48  TYR D CG  1 
ATOM   5939 C CD1 . TYR D 1 48  ? 4.834   -23.275 -7.117  1.00 29.43 ? 48  TYR D CD1 1 
ATOM   5940 C CD2 . TYR D 1 48  ? 2.568   -24.119 -7.220  1.00 28.98 ? 48  TYR D CD2 1 
ATOM   5941 C CE1 . TYR D 1 48  ? 5.277   -24.361 -7.925  1.00 24.88 ? 48  TYR D CE1 1 
ATOM   5942 C CE2 . TYR D 1 48  ? 2.983   -25.166 -8.024  1.00 31.60 ? 48  TYR D CE2 1 
ATOM   5943 C CZ  . TYR D 1 48  ? 4.341   -25.297 -8.373  1.00 33.74 ? 48  TYR D CZ  1 
ATOM   5944 O OH  . TYR D 1 48  ? 4.729   -26.382 -9.159  1.00 33.10 ? 48  TYR D OH  1 
ATOM   5945 N N   . ALA D 1 49  ? 5.205   -20.211 -7.635  1.00 26.04 ? 49  ALA D N   1 
ATOM   5946 C CA  . ALA D 1 49  ? 6.555   -19.698 -7.888  1.00 26.83 ? 49  ALA D CA  1 
ATOM   5947 C C   . ALA D 1 49  ? 6.623   -18.193 -7.626  1.00 29.36 ? 49  ALA D C   1 
ATOM   5948 O O   . ALA D 1 49  ? 7.581   -17.711 -7.013  1.00 25.60 ? 49  ALA D O   1 
ATOM   5949 C CB  . ALA D 1 49  ? 6.977   -20.006 -9.321  1.00 28.68 ? 49  ALA D CB  1 
ATOM   5950 N N   . GLY D 1 50  ? 5.587   -17.445 -8.029  1.00 25.79 ? 50  GLY D N   1 
ATOM   5951 C CA  . GLY D 1 50  ? 5.579   -16.013 -7.749  1.00 28.72 ? 50  GLY D CA  1 
ATOM   5952 C C   . GLY D 1 50  ? 5.479   -15.721 -6.264  1.00 29.08 ? 50  GLY D C   1 
ATOM   5953 O O   . GLY D 1 50  ? 6.126   -14.804 -5.753  1.00 24.09 ? 50  GLY D O   1 
ATOM   5954 N N   . LEU D 1 51  ? 4.663   -16.503 -5.550  1.00 28.58 ? 51  LEU D N   1 
ATOM   5955 C CA  . LEU D 1 51  ? 4.508   -16.311 -4.108  1.00 25.71 ? 51  LEU D CA  1 
ATOM   5956 C C   . LEU D 1 51  ? 5.808   -16.581 -3.364  1.00 25.89 ? 51  LEU D C   1 
ATOM   5957 O O   . LEU D 1 51  ? 6.163   -15.867 -2.416  1.00 24.85 ? 51  LEU D O   1 
ATOM   5958 C CB  . LEU D 1 51  ? 3.396   -17.231 -3.586  1.00 23.13 ? 51  LEU D CB  1 
ATOM   5959 C CG  . LEU D 1 51  ? 3.136   -17.229 -2.084  1.00 26.37 ? 51  LEU D CG  1 
ATOM   5960 C CD1 . LEU D 1 51  ? 2.541   -15.887 -1.631  1.00 29.42 ? 51  LEU D CD1 1 
ATOM   5961 C CD2 . LEU D 1 51  ? 2.142   -18.366 -1.742  1.00 24.60 ? 51  LEU D CD2 1 
ATOM   5962 N N   . TYR D 1 52  ? 6.475   -17.677 -3.701  1.00 22.36 ? 52  TYR D N   1 
ATOM   5963 C CA  . TYR D 1 52  ? 7.681   -18.019 -2.958  1.00 26.49 ? 52  TYR D CA  1 
ATOM   5964 C C   . TYR D 1 52  ? 8.869   -17.172 -3.409  1.00 23.41 ? 52  TYR D C   1 
ATOM   5965 O O   . TYR D 1 52  ? 9.725   -16.847 -2.588  1.00 23.08 ? 52  TYR D O   1 
ATOM   5966 C CB  . TYR D 1 52  ? 7.966   -19.518 -3.061  1.00 21.08 ? 52  TYR D CB  1 
ATOM   5967 C CG  . TYR D 1 52  ? 7.127   -20.268 -2.064  1.00 22.41 ? 52  TYR D CG  1 
ATOM   5968 C CD1 . TYR D 1 52  ? 7.548   -20.392 -0.744  1.00 22.33 ? 52  TYR D CD1 1 
ATOM   5969 C CD2 . TYR D 1 52  ? 5.868   -20.773 -2.419  1.00 25.25 ? 52  TYR D CD2 1 
ATOM   5970 C CE1 . TYR D 1 52  ? 6.767   -21.050 0.208   1.00 24.31 ? 52  TYR D CE1 1 
ATOM   5971 C CE2 . TYR D 1 52  ? 5.036   -21.444 -1.456  1.00 24.99 ? 52  TYR D CE2 1 
ATOM   5972 C CZ  . TYR D 1 52  ? 5.518   -21.558 -0.148  1.00 29.13 ? 52  TYR D CZ  1 
ATOM   5973 O OH  . TYR D 1 52  ? 4.820   -22.194 0.839   1.00 26.00 ? 52  TYR D OH  1 
ATOM   5974 N N   . GLU D 1 53  ? 8.839   -16.690 -4.648  1.00 23.95 ? 53  GLU D N   1 
ATOM   5975 C CA  . GLU D 1 53  ? 9.794   -15.661 -5.065  1.00 27.43 ? 53  GLU D CA  1 
ATOM   5976 C C   . GLU D 1 53  ? 9.721   -14.434 -4.157  1.00 25.12 ? 53  GLU D C   1 
ATOM   5977 O O   . GLU D 1 53  ? 10.752  -13.935 -3.680  1.00 23.21 ? 53  GLU D O   1 
ATOM   5978 C CB  . GLU D 1 53  ? 9.543   -15.290 -6.534  1.00 25.68 ? 53  GLU D CB  1 
ATOM   5979 C CG  . GLU D 1 53  ? 10.600  -14.286 -7.080  1.00 27.12 ? 53  GLU D CG  1 
ATOM   5980 C CD  . GLU D 1 53  ? 10.201  -13.660 -8.396  1.00 30.66 ? 53  GLU D CD  1 
ATOM   5981 O OE1 . GLU D 1 53  ? 9.109   -13.072 -8.508  1.00 30.07 ? 53  GLU D OE1 1 
ATOM   5982 O OE2 . GLU D 1 53  ? 10.981  -13.840 -9.357  1.00 32.64 ? 53  GLU D OE2 1 
ATOM   5983 N N   . SER D 1 54  ? 8.504   -13.930 -3.902  1.00 23.87 ? 54  SER D N   1 
ATOM   5984 C CA  . SER D 1 54  ? 8.348   -12.762 -3.051  1.00 24.07 ? 54  SER D CA  1 
ATOM   5985 C C   . SER D 1 54  ? 8.794   -13.079 -1.645  1.00 24.50 ? 54  SER D C   1 
ATOM   5986 O O   . SER D 1 54  ? 9.452   -12.254 -1.001  1.00 26.68 ? 54  SER D O   1 
ATOM   5987 C CB  . SER D 1 54  ? 6.890   -12.252 -3.028  1.00 27.93 ? 54  SER D CB  1 
ATOM   5988 O OG  . SER D 1 54  ? 6.396   -12.011 -4.338  1.00 32.07 ? 54  SER D OG  1 
ATOM   5989 N N   . ARG D 1 55  ? 8.450   -14.268 -1.156  1.00 21.39 ? 55  ARG D N   1 
ATOM   5990 C CA  . ARG D 1 55  ? 8.925   -14.715 0.150   1.00 22.76 ? 55  ARG D CA  1 
ATOM   5991 C C   . ARG D 1 55  ? 10.467  -14.701 0.223   1.00 21.95 ? 55  ARG D C   1 
ATOM   5992 O O   . ARG D 1 55  ? 11.050  -14.208 1.199   1.00 20.85 ? 55  ARG D O   1 
ATOM   5993 C CB  . ARG D 1 55  ? 8.355   -16.122 0.445   1.00 19.71 ? 55  ARG D CB  1 
ATOM   5994 C CG  . ARG D 1 55  ? 8.769   -16.671 1.817   1.00 22.68 ? 55  ARG D CG  1 
ATOM   5995 C CD  . ARG D 1 55  ? 8.558   -18.200 1.901   1.00 22.06 ? 55  ARG D CD  1 
ATOM   5996 N NE  . ARG D 1 55  ? 8.741   -18.701 3.264   1.00 27.02 ? 55  ARG D NE  1 
ATOM   5997 C CZ  . ARG D 1 55  ? 9.168   -19.923 3.564   1.00 28.15 ? 55  ARG D CZ  1 
ATOM   5998 N NH1 . ARG D 1 55  ? 9.488   -20.782 2.625   1.00 26.63 ? 55  ARG D NH1 1 
ATOM   5999 N NH2 . ARG D 1 55  ? 9.249   -20.298 4.844   1.00 31.49 ? 55  ARG D NH2 1 
ATOM   6000 N N   . ASN D 1 56  ? 11.137  -15.232 -0.807  1.00 22.09 ? 56  ASN D N   1 
ATOM   6001 C CA  . ASN D 1 56  ? 12.588  -15.342 -0.784  1.00 21.31 ? 56  ASN D CA  1 
ATOM   6002 C C   . ASN D 1 56  ? 13.262  -13.975 -0.876  1.00 22.31 ? 56  ASN D C   1 
ATOM   6003 O O   . ASN D 1 56  ? 14.304  -13.767 -0.255  1.00 24.96 ? 56  ASN D O   1 
ATOM   6004 C CB  . ASN D 1 56  ? 13.069  -16.229 -1.925  1.00 20.35 ? 56  ASN D CB  1 
ATOM   6005 C CG  . ASN D 1 56  ? 12.656  -17.675 -1.731  1.00 23.23 ? 56  ASN D CG  1 
ATOM   6006 O OD1 . ASN D 1 56  ? 12.386  -18.100 -0.612  1.00 22.87 ? 56  ASN D OD1 1 
ATOM   6007 N ND2 . ASN D 1 56  ? 12.603  -18.428 -2.808  1.00 23.27 ? 56  ASN D ND2 1 
ATOM   6008 N N   . ILE D 1 57  ? 12.691  -13.041 -1.657  1.00 21.57 ? 57  ILE D N   1 
ATOM   6009 C CA  . ILE D 1 57  ? 13.220  -11.682 -1.692  1.00 20.42 ? 57  ILE D CA  1 
ATOM   6010 C C   . ILE D 1 57  ? 13.313  -11.109 -0.287  1.00 23.76 ? 57  ILE D C   1 
ATOM   6011 O O   . ILE D 1 57  ? 14.385  -10.642 0.141   1.00 24.53 ? 57  ILE D O   1 
ATOM   6012 C CB  . ILE D 1 57  ? 12.369  -10.780 -2.597  1.00 21.52 ? 57  ILE D CB  1 
ATOM   6013 C CG1 . ILE D 1 57  ? 12.632  -11.089 -4.051  1.00 24.76 ? 57  ILE D CG1 1 
ATOM   6014 C CG2 . ILE D 1 57  ? 12.651  -9.304  -2.303  1.00 23.37 ? 57  ILE D CG2 1 
ATOM   6015 C CD1 . ILE D 1 57  ? 11.570  -10.543 -4.977  1.00 28.88 ? 57  ILE D CD1 1 
ATOM   6016 N N   . PHE D 1 58  ? 12.201  -11.135 0.456   1.00 22.74 ? 58  PHE D N   1 
ATOM   6017 C CA  . PHE D 1 58  ? 12.182  -10.595 1.812   1.00 23.07 ? 58  PHE D CA  1 
ATOM   6018 C C   . PHE D 1 58  ? 13.173  -11.331 2.709   1.00 24.21 ? 58  PHE D C   1 
ATOM   6019 O O   . PHE D 1 58  ? 13.958  -10.706 3.433   1.00 26.33 ? 58  PHE D O   1 
ATOM   6020 C CB  . PHE D 1 58  ? 10.751  -10.690 2.401   1.00 26.69 ? 58  PHE D CB  1 
ATOM   6021 C CG  . PHE D 1 58  ? 10.611  -10.033 3.753   1.00 28.95 ? 58  PHE D CG  1 
ATOM   6022 C CD1 . PHE D 1 58  ? 11.130  -10.647 4.898   1.00 29.84 ? 58  PHE D CD1 1 
ATOM   6023 C CD2 . PHE D 1 58  ? 9.984   -8.799  3.880   1.00 31.96 ? 58  PHE D CD2 1 
ATOM   6024 C CE1 . PHE D 1 58  ? 11.055  -10.059 6.137   1.00 32.97 ? 58  PHE D CE1 1 
ATOM   6025 C CE2 . PHE D 1 58  ? 9.889   -8.176  5.135   1.00 35.41 ? 58  PHE D CE2 1 
ATOM   6026 C CZ  . PHE D 1 58  ? 10.418  -8.811  6.271   1.00 37.59 ? 58  PHE D CZ  1 
ATOM   6027 N N   . TRP D 1 59  ? 13.145  -12.670 2.676   1.00 24.20 ? 59  TRP D N   1 
ATOM   6028 C CA  . TRP D 1 59  ? 14.025  -13.481 3.515   1.00 26.85 ? 59  TRP D CA  1 
ATOM   6029 C C   . TRP D 1 59  ? 15.496  -13.196 3.201   1.00 25.56 ? 59  TRP D C   1 
ATOM   6030 O O   . TRP D 1 59  ? 16.315  -13.033 4.113   1.00 25.58 ? 59  TRP D O   1 
ATOM   6031 C CB  . TRP D 1 59  ? 13.691  -14.965 3.316   1.00 24.77 ? 59  TRP D CB  1 
ATOM   6032 C CG  . TRP D 1 59  ? 14.056  -15.891 4.457   1.00 29.10 ? 59  TRP D CG  1 
ATOM   6033 C CD1 . TRP D 1 59  ? 14.847  -15.615 5.531   1.00 29.36 ? 59  TRP D CD1 1 
ATOM   6034 C CD2 . TRP D 1 59  ? 13.600  -17.243 4.630   1.00 24.57 ? 59  TRP D CD2 1 
ATOM   6035 N NE1 . TRP D 1 59  ? 14.911  -16.718 6.372   1.00 28.86 ? 59  TRP D NE1 1 
ATOM   6036 C CE2 . TRP D 1 59  ? 14.144  -17.718 5.847   1.00 27.07 ? 59  TRP D CE2 1 
ATOM   6037 C CE3 . TRP D 1 59  ? 12.769  -18.084 3.886   1.00 27.89 ? 59  TRP D CE3 1 
ATOM   6038 C CZ2 . TRP D 1 59  ? 13.908  -19.031 6.328   1.00 28.99 ? 59  TRP D CZ2 1 
ATOM   6039 C CZ3 . TRP D 1 59  ? 12.512  -19.391 4.373   1.00 27.63 ? 59  TRP D CZ3 1 
ATOM   6040 C CH2 . TRP D 1 59  ? 13.079  -19.836 5.594   1.00 26.34 ? 59  TRP D CH2 1 
ATOM   6041 N N   . ILE D 1 60  ? 15.859  -13.132 1.922   1.00 24.02 ? 60  ILE D N   1 
ATOM   6042 C CA  . ILE D 1 60  ? 17.275  -12.902 1.592   1.00 23.10 ? 60  ILE D CA  1 
ATOM   6043 C C   . ILE D 1 60  ? 17.695  -11.471 1.917   1.00 27.09 ? 60  ILE D C   1 
ATOM   6044 O O   . ILE D 1 60  ? 18.792  -11.239 2.456   1.00 24.69 ? 60  ILE D O   1 
ATOM   6045 C CB  . ILE D 1 60  ? 17.535  -13.236 0.119   1.00 24.52 ? 60  ILE D CB  1 
ATOM   6046 C CG1 . ILE D 1 60  ? 17.274  -14.729 -0.121  1.00 21.52 ? 60  ILE D CG1 1 
ATOM   6047 C CG2 . ILE D 1 60  ? 18.981  -12.814 -0.300  1.00 26.60 ? 60  ILE D CG2 1 
ATOM   6048 C CD1 . ILE D 1 60  ? 17.253  -15.086 -1.566  1.00 22.43 ? 60  ILE D CD1 1 
ATOM   6049 N N   . LYS D 1 61  ? 16.833  -10.489 1.607   1.00 24.74 ? 61  LYS D N   1 
ATOM   6050 C CA  . LYS D 1 61  ? 17.200  -9.091  1.826   1.00 25.42 ? 61  LYS D CA  1 
ATOM   6051 C C   . LYS D 1 61  ? 17.197  -8.735  3.317   1.00 27.53 ? 61  LYS D C   1 
ATOM   6052 O O   . LYS D 1 61  ? 18.028  -7.949  3.777   1.00 26.18 ? 61  LYS D O   1 
ATOM   6053 C CB  . LYS D 1 61  ? 16.279  -8.201  1.006   1.00 27.26 ? 61  LYS D CB  1 
ATOM   6054 C CG  . LYS D 1 61  ? 16.252  -6.721  1.410   1.00 32.58 ? 61  LYS D CG  1 
ATOM   6055 C CD  . LYS D 1 61  ? 17.245  -5.887  0.625   1.00 35.33 ? 61  LYS D CD  1 
ATOM   6056 C CE  . LYS D 1 61  ? 17.391  -4.498  1.235   1.00 32.87 ? 61  LYS D CE  1 
ATOM   6057 N NZ  . LYS D 1 61  ? 18.756  -4.004  0.853   1.00 36.58 ? 61  LYS D NZ  1 
ATOM   6058 N N   . ASN D 1 62  ? 16.270  -9.297  4.083   1.00 26.05 ? 62  ASN D N   1 
ATOM   6059 C CA  . ASN D 1 62  ? 16.135  -8.925  5.516   1.00 24.11 ? 62  ASN D CA  1 
ATOM   6060 C C   . ASN D 1 62  ? 16.834  -9.912  6.443   1.00 28.22 ? 62  ASN D C   1 
ATOM   6061 O O   . ASN D 1 62  ? 17.078  -9.557  7.575   1.00 27.38 ? 62  ASN D O   1 
ATOM   6062 C CB  . ASN D 1 62  ? 14.679  -8.730  5.920   1.00 28.69 ? 62  ASN D CB  1 
ATOM   6063 C CG  . ASN D 1 62  ? 14.049  -7.585  5.168   1.00 28.52 ? 62  ASN D CG  1 
ATOM   6064 O OD1 . ASN D 1 62  ? 14.446  -6.458  5.334   1.00 29.07 ? 62  ASN D OD1 1 
ATOM   6065 N ND2 . ASN D 1 62  ? 13.096  -7.878  4.318   1.00 28.81 ? 62  ASN D ND2 1 
ATOM   6066 N N   . GLY D 1 63  ? 17.062  -11.137 5.989   1.00 27.41 ? 63  GLY D N   1 
ATOM   6067 C CA  . GLY D 1 63  ? 17.743  -12.130 6.835   1.00 31.45 ? 63  GLY D CA  1 
ATOM   6068 C C   . GLY D 1 63  ? 16.797  -12.845 7.775   1.00 36.17 ? 63  GLY D C   1 
ATOM   6069 O O   . GLY D 1 63  ? 17.253  -13.607 8.600   1.00 41.94 ? 63  GLY D O   1 
ATOM   6070 N N   . ARG D 1 64  ? 15.512  -12.583 7.637   1.00 32.53 ? 64  ARG D N   1 
ATOM   6071 C CA  . ARG D 1 64  ? 14.512  -13.252 8.481   1.00 34.82 ? 64  ARG D CA  1 
ATOM   6072 C C   . ARG D 1 64  ? 13.273  -13.489 7.629   1.00 33.28 ? 64  ARG D C   1 
ATOM   6073 O O   . ARG D 1 64  ? 13.038  -12.737 6.729   1.00 29.88 ? 64  ARG D O   1 
ATOM   6074 C CB  . ARG D 1 64  ? 14.269  -12.465 9.768   1.00 37.25 ? 64  ARG D CB  1 
ATOM   6075 C CG  . ARG D 1 64  ? 13.315  -11.292 9.643   1.00 48.99 ? 64  ARG D CG  1 
ATOM   6076 C CD  . ARG D 1 64  ? 12.946  -10.739 11.014  1.00 59.66 ? 64  ARG D CD  1 
ATOM   6077 N NE  . ARG D 1 64  ? 11.769  -11.316 11.669  1.00 63.23 ? 64  ARG D NE  1 
ATOM   6078 C CZ  . ARG D 1 64  ? 11.402  -11.096 12.938  1.00 66.00 ? 64  ARG D CZ  1 
ATOM   6079 N NH1 . ARG D 1 64  ? 10.306  -11.664 13.419  1.00 61.80 ? 64  ARG D NH1 1 
ATOM   6080 N NH2 . ARG D 1 64  ? 12.116  -10.297 13.713  1.00 63.12 ? 64  ARG D NH2 1 
ATOM   6081 N N   . GLU D 1 65  ? 12.538  -14.536 7.933   1.00 32.14 ? 65  GLU D N   1 
ATOM   6082 C CA  . GLU D 1 65  ? 11.335  -14.936 7.179   1.00 33.85 ? 65  GLU D CA  1 
ATOM   6083 C C   . GLU D 1 65  ? 10.231  -13.892 7.300   1.00 30.96 ? 65  GLU D C   1 
ATOM   6084 O O   . GLU D 1 65  ? 10.028  -13.426 8.366   1.00 32.27 ? 65  GLU D O   1 
ATOM   6085 C CB  . GLU D 1 65  ? 10.791  -16.190 7.837   1.00 31.39 ? 65  GLU D CB  1 
ATOM   6086 C CG  . GLU D 1 65  ? 10.627  -17.315 6.875   1.00 35.42 ? 65  GLU D CG  1 
ATOM   6087 C CD  . GLU D 1 65  ? 9.951   -18.469 7.564   1.00 31.70 ? 65  GLU D CD  1 
ATOM   6088 O OE1 . GLU D 1 65  ? 8.966   -18.898 7.060   1.00 38.85 ? 65  GLU D OE1 1 
ATOM   6089 O OE2 . GLU D 1 65  ? 10.431  -18.890 8.598   1.00 36.47 ? 65  GLU D OE2 1 
ATOM   6090 N N   . PRO D 1 66  ? 9.496   -13.560 6.229   1.00 33.48 ? 66  PRO D N   1 
ATOM   6091 C CA  . PRO D 1 66  ? 8.410   -12.599 6.310   1.00 37.74 ? 66  PRO D CA  1 
ATOM   6092 C C   . PRO D 1 66  ? 7.241   -13.200 7.102   1.00 38.42 ? 66  PRO D C   1 
ATOM   6093 O O   . PRO D 1 66  ? 6.936   -14.339 6.895   1.00 37.49 ? 66  PRO D O   1 
ATOM   6094 C CB  . PRO D 1 66  ? 7.976   -12.405 4.863   1.00 27.79 ? 66  PRO D CB  1 
ATOM   6095 C CG  . PRO D 1 66  ? 8.416   -13.656 4.180   1.00 29.04 ? 66  PRO D CG  1 
ATOM   6096 C CD  . PRO D 1 66  ? 9.669   -14.090 4.895   1.00 28.99 ? 66  PRO D CD  1 
ATOM   6097 N N   . ASN D 1 67  ? 6.609   -12.384 7.950   1.00 46.05 ? 67  ASN D N   1 
ATOM   6098 C CA  . ASN D 1 67  ? 5.485   -12.872 8.789   1.00 43.92 ? 67  ASN D CA  1 
ATOM   6099 C C   . ASN D 1 67  ? 4.248   -13.166 7.928   1.00 41.82 ? 67  ASN D C   1 
ATOM   6100 O O   . ASN D 1 67  ? 3.405   -13.885 8.410   1.00 42.54 ? 67  ASN D O   1 
ATOM   6101 C CB  . ASN D 1 67  ? 5.352   -12.133 10.124  1.00 48.78 ? 67  ASN D CB  1 
ATOM   6102 C CG  . ASN D 1 67  ? 5.014   -10.670 9.988   1.00 52.42 ? 67  ASN D CG  1 
ATOM   6103 O OD1 . ASN D 1 67  ? 4.776   -9.995  10.984  1.00 59.70 ? 67  ASN D OD1 1 
ATOM   6104 N ND2 . ASN D 1 67  ? 4.984   -10.171 8.767   1.00 57.88 ? 67  ASN D ND2 1 
ATOM   6105 N N   . TYR D 1 68  ? 4.188   -12.644 6.702   1.00 41.81 ? 68  TYR D N   1 
ATOM   6106 C CA  . TYR D 1 68  ? 3.121   -12.955 5.734   1.00 34.23 ? 68  TYR D CA  1 
ATOM   6107 C C   . TYR D 1 68  ? 3.566   -12.446 4.370   1.00 33.08 ? 68  TYR D C   1 
ATOM   6108 O O   . TYR D 1 68  ? 4.387   -11.563 4.322   1.00 31.81 ? 68  TYR D O   1 
ATOM   6109 C CB  . TYR D 1 68  ? 1.780   -12.341 6.130   1.00 36.30 ? 68  TYR D CB  1 
ATOM   6110 C CG  . TYR D 1 68  ? 1.659   -10.861 5.896   1.00 33.69 ? 68  TYR D CG  1 
ATOM   6111 C CD1 . TYR D 1 68  ? 1.393   -10.359 4.644   1.00 34.71 ? 68  TYR D CD1 1 
ATOM   6112 C CD2 . TYR D 1 68  ? 1.798   -9.970  6.932   1.00 39.66 ? 68  TYR D CD2 1 
ATOM   6113 C CE1 . TYR D 1 68  ? 1.285   -9.004  4.418   1.00 37.04 ? 68  TYR D CE1 1 
ATOM   6114 C CE2 . TYR D 1 68  ? 1.700   -8.609  6.733   1.00 38.12 ? 68  TYR D CE2 1 
ATOM   6115 C CZ  . TYR D 1 68  ? 1.425   -8.132  5.472   1.00 40.92 ? 68  TYR D CZ  1 
ATOM   6116 O OH  . TYR D 1 68  ? 1.308   -6.800  5.271   1.00 49.65 ? 68  TYR D OH  1 
ATOM   6117 N N   . VAL D 1 69  ? 2.996   -13.010 3.316   1.00 31.35 ? 69  VAL D N   1 
ATOM   6118 C CA  . VAL D 1 69  ? 3.314   -12.586 1.927   1.00 32.01 ? 69  VAL D CA  1 
ATOM   6119 C C   . VAL D 1 69  ? 2.003   -12.430 1.164   1.00 32.94 ? 69  VAL D C   1 
ATOM   6120 O O   . VAL D 1 69  ? 1.156   -13.297 1.289   1.00 33.65 ? 69  VAL D O   1 
ATOM   6121 C CB  . VAL D 1 69  ? 4.213   -13.600 1.204   1.00 28.08 ? 69  VAL D CB  1 
ATOM   6122 C CG1 . VAL D 1 69  ? 4.471   -13.199 -0.229  1.00 25.71 ? 69  VAL D CG1 1 
ATOM   6123 C CG2 . VAL D 1 69  ? 5.502   -13.824 1.944   1.00 28.81 ? 69  VAL D CG2 1 
ATOM   6124 N N   . THR D 1 70  ? 1.879   -11.353 0.402   1.00 30.64 ? 70  THR D N   1 
ATOM   6125 C CA  . THR D 1 70  ? 0.672   -11.126 -0.405  1.00 33.69 ? 70  THR D CA  1 
ATOM   6126 C C   . THR D 1 70  ? 0.971   -11.626 -1.805  1.00 33.67 ? 70  THR D C   1 
ATOM   6127 O O   . THR D 1 70  ? 2.008   -11.299 -2.345  1.00 32.48 ? 70  THR D O   1 
ATOM   6128 C CB  . THR D 1 70  ? 0.293   -9.643  -0.447  1.00 34.26 ? 70  THR D CB  1 
ATOM   6129 O OG1 . THR D 1 70  ? 0.045   -9.173  0.873   1.00 32.76 ? 70  THR D OG1 1 
ATOM   6130 C CG2 . THR D 1 70  ? -0.877  -9.367  -1.356  1.00 31.58 ? 70  THR D CG2 1 
ATOM   6131 N N   . LEU D 1 71  ? 0.088   -12.433 -2.340  1.00 26.80 ? 71  LEU D N   1 
ATOM   6132 C CA  . LEU D 1 71  ? 0.276   -12.921 -3.700  1.00 31.32 ? 71  LEU D CA  1 
ATOM   6133 C C   . LEU D 1 71  ? 0.042   -11.775 -4.686  1.00 36.15 ? 71  LEU D C   1 
ATOM   6134 O O   . LEU D 1 71  ? -1.093  -11.296 -4.841  1.00 35.02 ? 71  LEU D O   1 
ATOM   6135 C CB  . LEU D 1 71  ? -0.657  -14.094 -3.983  1.00 30.91 ? 71  LEU D CB  1 
ATOM   6136 C CG  . LEU D 1 71  ? -0.708  -14.546 -5.450  1.00 35.88 ? 71  LEU D CG  1 
ATOM   6137 C CD1 . LEU D 1 71  ? 0.649   -15.152 -5.875  1.00 31.83 ? 71  LEU D CD1 1 
ATOM   6138 C CD2 . LEU D 1 71  ? -1.817  -15.597 -5.644  1.00 35.70 ? 71  LEU D CD2 1 
ATOM   6139 N N   . THR D 1 72  ? 1.130   -11.284 -5.319  1.00 33.20 ? 72  THR D N   1 
ATOM   6140 C CA  . THR D 1 72  ? 1.040   -10.157 -6.235  1.00 33.84 ? 72  THR D CA  1 
ATOM   6141 C C   . THR D 1 72  ? 1.596   -10.421 -7.615  1.00 36.80 ? 72  THR D C   1 
ATOM   6142 O O   . THR D 1 72  ? 1.273   -9.664  -8.533  1.00 32.33 ? 72  THR D O   1 
ATOM   6143 C CB  . THR D 1 72  ? 1.786   -8.932  -5.681  1.00 39.20 ? 72  THR D CB  1 
ATOM   6144 O OG1 . THR D 1 72  ? 3.194   -9.212  -5.699  1.00 33.15 ? 72  THR D OG1 1 
ATOM   6145 C CG2 . THR D 1 72  ? 1.322   -8.566  -4.264  1.00 37.87 ? 72  THR D CG2 1 
ATOM   6146 N N   . SER D 1 73  ? 2.448   -11.430 -7.789  1.00 32.80 ? 73  SER D N   1 
ATOM   6147 C CA  . SER D 1 73  ? 3.193   -11.617 -9.022  1.00 35.10 ? 73  SER D CA  1 
ATOM   6148 C C   . SER D 1 73  ? 3.291   -13.096 -9.362  1.00 34.19 ? 73  SER D C   1 
ATOM   6149 O O   . SER D 1 73  ? 3.126   -13.955 -8.503  1.00 35.64 ? 73  SER D O   1 
ATOM   6150 C CB  . SER D 1 73  ? 4.598   -11.005 -8.892  1.00 33.91 ? 73  SER D CB  1 
ATOM   6151 O OG  . SER D 1 73  ? 5.201   -11.590 -7.756  1.00 36.08 ? 73  SER D OG  1 
ATOM   6152 N N   . VAL D 1 74  ? 3.535   -13.381 -10.637 1.00 31.23 ? 74  VAL D N   1 
ATOM   6153 C CA  . VAL D 1 74  ? 3.831   -14.719 -11.101 1.00 30.35 ? 74  VAL D CA  1 
ATOM   6154 C C   . VAL D 1 74  ? 5.293   -14.784 -11.557 1.00 33.45 ? 74  VAL D C   1 
ATOM   6155 O O   . VAL D 1 74  ? 5.941   -13.756 -11.829 1.00 31.42 ? 74  VAL D O   1 
ATOM   6156 C CB  . VAL D 1 74  ? 2.862   -15.142 -12.225 1.00 37.09 ? 74  VAL D CB  1 
ATOM   6157 C CG1 . VAL D 1 74  ? 1.392   -15.213 -11.674 1.00 33.24 ? 74  VAL D CG1 1 
ATOM   6158 C CG2 . VAL D 1 74  ? 2.971   -14.145 -13.373 1.00 30.85 ? 74  VAL D CG2 1 
ATOM   6159 N N   . ALA D 1 75  ? 5.810   -16.012 -11.658 1.00 31.23 ? 75  ALA D N   1 
ATOM   6160 C CA  . ALA D 1 75  ? 7.204   -16.256 -12.000 1.00 31.25 ? 75  ALA D CA  1 
ATOM   6161 C C   . ALA D 1 75  ? 7.373   -17.690 -12.486 1.00 34.89 ? 75  ALA D C   1 
ATOM   6162 O O   . ALA D 1 75  ? 6.552   -18.579 -12.202 1.00 34.10 ? 75  ALA D O   1 
ATOM   6163 C CB  . ALA D 1 75  ? 8.125   -15.984 -10.817 1.00 28.68 ? 75  ALA D CB  1 
ATOM   6164 N N   . ARG D 1 76  ? 8.443   -17.901 -13.231 1.00 32.35 ? 76  ARG D N   1 
ATOM   6165 C CA  . ARG D 1 76  ? 8.739   -19.217 -13.784 1.00 37.02 ? 76  ARG D CA  1 
ATOM   6166 C C   . ARG D 1 76  ? 9.362   -20.150 -12.756 1.00 34.63 ? 76  ARG D C   1 
ATOM   6167 O O   . ARG D 1 76  ? 9.253   -21.364 -12.918 1.00 36.25 ? 76  ARG D O   1 
ATOM   6168 C CB  . ARG D 1 76  ? 9.739   -19.069 -14.953 1.00 38.35 ? 76  ARG D CB  1 
ATOM   6169 C CG  . ARG D 1 76  ? 9.302   -18.073 -16.035 1.00 41.47 ? 76  ARG D CG  1 
ATOM   6170 C CD  . ARG D 1 76  ? 10.385  -17.009 -16.340 1.00 49.11 ? 76  ARG D CD  1 
ATOM   6171 N NE  . ARG D 1 76  ? 10.944  -16.307 -15.166 1.00 53.38 ? 76  ARG D NE  1 
ATOM   6172 C CZ  . ARG D 1 76  ? 10.359  -15.322 -14.486 1.00 44.06 ? 76  ARG D CZ  1 
ATOM   6173 N NH1 . ARG D 1 76  ? 9.151   -14.886 -14.796 1.00 47.22 ? 76  ARG D NH1 1 
ATOM   6174 N NH2 . ARG D 1 76  ? 10.997  -14.768 -13.462 1.00 36.95 ? 76  ARG D NH2 1 
ATOM   6175 N N   . ASN D 1 77  ? 9.950   -19.610 -11.688 1.00 29.92 ? 77  ASN D N   1 
ATOM   6176 C CA  . ASN D 1 77  ? 10.509  -20.386 -10.586 1.00 28.10 ? 77  ASN D CA  1 
ATOM   6177 C C   . ASN D 1 77  ? 10.638  -19.438 -9.405  1.00 27.02 ? 77  ASN D C   1 
ATOM   6178 O O   . ASN D 1 77  ? 10.421  -18.235 -9.562  1.00 24.79 ? 77  ASN D O   1 
ATOM   6179 C CB  . ASN D 1 77  ? 11.869  -21.040 -10.981 1.00 30.46 ? 77  ASN D CB  1 
ATOM   6180 C CG  . ASN D 1 77  ? 12.965  -20.029 -11.316 1.00 28.74 ? 77  ASN D CG  1 
ATOM   6181 O OD1 . ASN D 1 77  ? 13.164  -19.025 -10.626 1.00 27.12 ? 77  ASN D OD1 1 
ATOM   6182 N ND2 . ASN D 1 77  ? 13.679  -20.293 -12.398 1.00 30.92 ? 77  ASN D ND2 1 
ATOM   6183 N N   . PRO D 1 78  ? 10.933  -19.939 -8.204  1.00 25.01 ? 78  PRO D N   1 
ATOM   6184 C CA  . PRO D 1 78  ? 11.075  -19.033 -7.040  1.00 24.26 ? 78  PRO D CA  1 
ATOM   6185 C C   . PRO D 1 78  ? 12.483  -18.451 -6.808  1.00 26.37 ? 78  PRO D C   1 
ATOM   6186 O O   . PRO D 1 78  ? 12.732  -17.872 -5.736  1.00 23.62 ? 78  PRO D O   1 
ATOM   6187 C CB  . PRO D 1 78  ? 10.696  -19.957 -5.876  1.00 22.73 ? 78  PRO D CB  1 
ATOM   6188 C CG  . PRO D 1 78  ? 11.240  -21.333 -6.349  1.00 24.10 ? 78  PRO D CG  1 
ATOM   6189 C CD  . PRO D 1 78  ? 11.036  -21.374 -7.833  1.00 22.37 ? 78  PRO D CD  1 
ATOM   6190 N N   . LEU D 1 79  ? 13.393  -18.547 -7.770  1.00 23.15 ? 79  LEU D N   1 
ATOM   6191 C CA  . LEU D 1 79  ? 14.801  -18.171 -7.553  1.00 24.15 ? 79  LEU D CA  1 
ATOM   6192 C C   . LEU D 1 79  ? 15.022  -16.657 -7.435  1.00 23.55 ? 79  LEU D C   1 
ATOM   6193 O O   . LEU D 1 79  ? 14.550  -15.874 -8.267  1.00 23.62 ? 79  LEU D O   1 
ATOM   6194 C CB  . LEU D 1 79  ? 15.654  -18.721 -8.688  1.00 23.06 ? 79  LEU D CB  1 
ATOM   6195 C CG  . LEU D 1 79  ? 17.155  -18.469 -8.580  1.00 22.16 ? 79  LEU D CG  1 
ATOM   6196 C CD1 . LEU D 1 79  ? 17.680  -19.180 -7.326  1.00 21.11 ? 79  LEU D CD1 1 
ATOM   6197 C CD2 . LEU D 1 79  ? 17.834  -18.965 -9.858  1.00 23.94 ? 79  LEU D CD2 1 
ATOM   6198 N N   . VAL D 1 80  ? 15.753  -16.245 -6.392  1.00 22.51 ? 80  VAL D N   1 
ATOM   6199 C CA  . VAL D 1 80  ? 16.149  -14.849 -6.177  1.00 25.25 ? 80  VAL D CA  1 
ATOM   6200 C C   . VAL D 1 80  ? 17.674  -14.794 -6.148  1.00 22.71 ? 80  VAL D C   1 
ATOM   6201 O O   . VAL D 1 80  ? 18.300  -15.517 -5.358  1.00 22.01 ? 80  VAL D O   1 
ATOM   6202 C CB  . VAL D 1 80  ? 15.545  -14.292 -4.873  1.00 20.85 ? 80  VAL D CB  1 
ATOM   6203 C CG1 . VAL D 1 80  ? 16.041  -12.853 -4.610  1.00 24.82 ? 80  VAL D CG1 1 
ATOM   6204 C CG2 . VAL D 1 80  ? 13.993  -14.371 -4.936  1.00 21.51 ? 80  VAL D CG2 1 
ATOM   6205 N N   . MET D 1 81  ? 18.266  -13.966 -7.004  1.00 21.41 ? 81  MET D N   1 
ATOM   6206 C CA  . MET D 1 81  ? 19.734  -13.845 -7.027  1.00 24.21 ? 81  MET D CA  1 
ATOM   6207 C C   . MET D 1 81  ? 20.246  -13.521 -5.630  1.00 25.59 ? 81  MET D C   1 
ATOM   6208 O O   . MET D 1 81  ? 19.730  -12.615 -4.955  1.00 25.32 ? 81  MET D O   1 
ATOM   6209 C CB  . MET D 1 81  ? 20.189  -12.745 -7.979  1.00 23.13 ? 81  MET D CB  1 
ATOM   6210 C CG  . MET D 1 81  ? 21.714  -12.772 -8.338  1.00 26.54 ? 81  MET D CG  1 
ATOM   6211 S SD  . MET D 1 81  ? 22.472  -14.399 -8.379  1.00 27.69 ? 81  MET D SD  1 
ATOM   6212 C CE  . MET D 1 81  ? 24.176  -14.004 -7.919  1.00 29.75 ? 81  MET D CE  1 
ATOM   6213 N N   . ASP D 1 82  ? 21.250  -14.272 -5.202  1.00 24.32 ? 82  ASP D N   1 
ATOM   6214 C CA  . ASP D 1 82  ? 21.892  -14.102 -3.901  1.00 21.73 ? 82  ASP D CA  1 
ATOM   6215 C C   . ASP D 1 82  ? 23.410  -14.087 -4.118  1.00 26.72 ? 82  ASP D C   1 
ATOM   6216 O O   . ASP D 1 82  ? 23.977  -15.032 -4.664  1.00 29.99 ? 82  ASP D O   1 
ATOM   6217 C CB  . ASP D 1 82  ? 21.428  -15.223 -2.977  1.00 21.66 ? 82  ASP D CB  1 
ATOM   6218 C CG  . ASP D 1 82  ? 21.881  -15.041 -1.548  1.00 24.81 ? 82  ASP D CG  1 
ATOM   6219 O OD1 . ASP D 1 82  ? 22.279  -13.920 -1.172  1.00 21.44 ? 82  ASP D OD1 1 
ATOM   6220 O OD2 . ASP D 1 82  ? 21.823  -16.044 -0.792  1.00 26.63 ? 82  ASP D OD2 1 
ATOM   6221 N N   . TYR D 1 83  ? 24.091  -13.029 -3.681  1.00 28.47 ? 83  TYR D N   1 
ATOM   6222 C CA  . TYR D 1 83  ? 25.525  -12.920 -3.950  1.00 26.35 ? 83  TYR D CA  1 
ATOM   6223 C C   . TYR D 1 83  ? 26.307  -13.437 -2.759  1.00 24.12 ? 83  TYR D C   1 
ATOM   6224 O O   . TYR D 1 83  ? 25.843  -13.376 -1.623  1.00 26.06 ? 83  TYR D O   1 
ATOM   6225 C CB  . TYR D 1 83  ? 25.902  -11.460 -4.252  1.00 24.46 ? 83  TYR D CB  1 
ATOM   6226 C CG  . TYR D 1 83  ? 25.224  -10.881 -5.492  1.00 24.16 ? 83  TYR D CG  1 
ATOM   6227 C CD1 . TYR D 1 83  ? 25.789  -11.009 -6.739  1.00 27.02 ? 83  TYR D CD1 1 
ATOM   6228 C CD2 . TYR D 1 83  ? 24.038  -10.155 -5.387  1.00 25.79 ? 83  TYR D CD2 1 
ATOM   6229 C CE1 . TYR D 1 83  ? 25.170  -10.452 -7.876  1.00 29.66 ? 83  TYR D CE1 1 
ATOM   6230 C CE2 . TYR D 1 83  ? 23.406  -9.612  -6.498  1.00 26.78 ? 83  TYR D CE2 1 
ATOM   6231 C CZ  . TYR D 1 83  ? 23.970  -9.759  -7.745  1.00 31.21 ? 83  TYR D CZ  1 
ATOM   6232 O OH  . TYR D 1 83  ? 23.330  -9.182  -8.880  1.00 34.21 ? 83  TYR D OH  1 
ATOM   6233 N N   . GLN D 1 84  ? 27.522  -13.935 -3.007  1.00 26.16 ? 84  GLN D N   1 
ATOM   6234 C CA  . GLN D 1 84  ? 28.313  -14.421 -1.897  1.00 22.58 ? 84  GLN D CA  1 
ATOM   6235 C C   . GLN D 1 84  ? 28.810  -13.249 -1.053  1.00 27.61 ? 84  GLN D C   1 
ATOM   6236 O O   . GLN D 1 84  ? 29.154  -12.191 -1.573  1.00 25.53 ? 84  GLN D O   1 
ATOM   6237 C CB  . GLN D 1 84  ? 29.482  -15.271 -2.408  1.00 27.90 ? 84  GLN D CB  1 
ATOM   6238 C CG  . GLN D 1 84  ? 30.499  -14.526 -3.300  1.00 23.99 ? 84  GLN D CG  1 
ATOM   6239 C CD  . GLN D 1 84  ? 31.484  -15.455 -3.960  1.00 26.20 ? 84  GLN D CD  1 
ATOM   6240 O OE1 . GLN D 1 84  ? 31.175  -16.080 -4.990  1.00 23.94 ? 84  GLN D OE1 1 
ATOM   6241 N NE2 . GLN D 1 84  ? 32.687  -15.547 -3.385  1.00 27.50 ? 84  GLN D NE2 1 
ATOM   6242 N N   . ASN D 1 85  ? 28.786  -13.417 0.273   1.00 31.15 ? 85  ASN D N   1 
ATOM   6243 C CA  . ASN D 1 85  ? 29.130  -12.315 1.163   1.00 30.79 ? 85  ASN D CA  1 
ATOM   6244 C C   . ASN D 1 85  ? 30.635  -12.180 1.377   1.00 31.09 ? 85  ASN D C   1 
ATOM   6245 O O   . ASN D 1 85  ? 31.058  -11.184 1.984   1.00 29.36 ? 85  ASN D O   1 
ATOM   6246 C CB  . ASN D 1 85  ? 28.443  -12.477 2.528   1.00 30.23 ? 85  ASN D CB  1 
ATOM   6247 C CG  . ASN D 1 85  ? 26.896  -12.521 2.450   1.00 36.70 ? 85  ASN D CG  1 
ATOM   6248 O OD1 . ASN D 1 85  ? 26.268  -12.177 1.428   1.00 36.68 ? 85  ASN D OD1 1 
ATOM   6249 N ND2 . ASN D 1 85  ? 26.279  -12.960 3.550   1.00 39.96 ? 85  ASN D ND2 1 
ATOM   6250 N N   . THR D 1 86  ? 31.436  -13.179 0.956   1.00 29.40 ? 86  THR D N   1 
ATOM   6251 C CA  . THR D 1 86  ? 32.891  -13.186 1.069   1.00 27.89 ? 86  THR D CA  1 
ATOM   6252 C C   . THR D 1 86  ? 33.484  -13.680 -0.239  1.00 27.95 ? 86  THR D C   1 
ATOM   6253 O O   . THR D 1 86  ? 32.767  -14.181 -1.107  1.00 26.75 ? 86  THR D O   1 
ATOM   6254 C CB  . THR D 1 86  ? 33.390  -14.131 2.164   1.00 31.15 ? 86  THR D CB  1 
ATOM   6255 O OG1 . THR D 1 86  ? 33.244  -15.464 1.684   1.00 28.36 ? 86  THR D OG1 1 
ATOM   6256 C CG2 . THR D 1 86  ? 32.597  -13.996 3.427   1.00 31.66 ? 86  THR D CG2 1 
ATOM   6257 N N   . ASN D 1 87  ? 34.824  -13.574 -0.385  1.00 28.16 ? 87  ASN D N   1 
ATOM   6258 C CA  . ASN D 1 87  ? 35.461  -14.143 -1.566  1.00 26.57 ? 87  ASN D CA  1 
ATOM   6259 C C   . ASN D 1 87  ? 35.692  -15.665 -1.443  1.00 29.55 ? 87  ASN D C   1 
ATOM   6260 O O   . ASN D 1 87  ? 36.411  -16.254 -2.273  1.00 30.73 ? 87  ASN D O   1 
ATOM   6261 C CB  . ASN D 1 87  ? 36.794  -13.455 -1.879  1.00 31.31 ? 87  ASN D CB  1 
ATOM   6262 C CG  . ASN D 1 87  ? 37.766  -13.522 -0.725  1.00 35.04 ? 87  ASN D CG  1 
ATOM   6263 O OD1 . ASN D 1 87  ? 37.711  -14.430 0.090   1.00 37.64 ? 87  ASN D OD1 1 
ATOM   6264 N ND2 . ASN D 1 87  ? 38.685  -12.578 -0.669  1.00 41.75 ? 87  ASN D ND2 1 
ATOM   6265 N N   . TYR D 1 88  ? 35.155  -16.319 -0.409  1.00 28.85 ? 88  TYR D N   1 
ATOM   6266 C CA  . TYR D 1 88  ? 35.380  -17.756 -0.256  1.00 28.25 ? 88  TYR D CA  1 
ATOM   6267 C C   . TYR D 1 88  ? 34.104  -18.553 0.022   1.00 28.20 ? 88  TYR D C   1 
ATOM   6268 O O   . TYR D 1 88  ? 34.200  -19.746 0.333   1.00 25.82 ? 88  TYR D O   1 
ATOM   6269 C CB  . TYR D 1 88  ? 36.418  -18.032 0.856   1.00 28.59 ? 88  TYR D CB  1 
ATOM   6270 C CG  . TYR D 1 88  ? 36.017  -17.509 2.213   1.00 29.65 ? 88  TYR D CG  1 
ATOM   6271 C CD1 . TYR D 1 88  ? 36.293  -16.177 2.590   1.00 30.97 ? 88  TYR D CD1 1 
ATOM   6272 C CD2 . TYR D 1 88  ? 35.372  -18.328 3.123   1.00 27.93 ? 88  TYR D CD2 1 
ATOM   6273 C CE1 . TYR D 1 88  ? 35.919  -15.687 3.843   1.00 30.40 ? 88  TYR D CE1 1 
ATOM   6274 C CE2 . TYR D 1 88  ? 34.972  -17.850 4.368   1.00 31.48 ? 88  TYR D CE2 1 
ATOM   6275 C CZ  . TYR D 1 88  ? 35.234  -16.521 4.719   1.00 34.38 ? 88  TYR D CZ  1 
ATOM   6276 O OH  . TYR D 1 88  ? 34.852  -16.048 5.958   1.00 30.71 ? 88  TYR D OH  1 
ATOM   6277 N N   . THR D 1 89  ? 32.918  -17.940 -0.056  1.00 25.37 ? 89  THR D N   1 
ATOM   6278 C CA  . THR D 1 89  ? 31.664  -18.635 0.252   1.00 24.30 ? 89  THR D CA  1 
ATOM   6279 C C   . THR D 1 89  ? 30.831  -18.926 -1.000  1.00 24.98 ? 89  THR D C   1 
ATOM   6280 O O   . THR D 1 89  ? 29.597  -19.128 -0.931  1.00 24.84 ? 89  THR D O   1 
ATOM   6281 C CB  . THR D 1 89  ? 30.847  -17.834 1.258   1.00 24.66 ? 89  THR D CB  1 
ATOM   6282 O OG1 . THR D 1 89  ? 30.846  -16.446 0.901   1.00 23.10 ? 89  THR D OG1 1 
ATOM   6283 C CG2 . THR D 1 89  ? 31.430  -17.966 2.638   1.00 26.38 ? 89  THR D CG2 1 
ATOM   6284 N N   . CYS D 1 90  ? 31.494  -19.008 -2.153  1.00 22.16 ? 90  CYS D N   1 
ATOM   6285 C CA  . CYS D 1 90  ? 30.772  -19.323 -3.387  1.00 24.57 ? 90  CYS D CA  1 
ATOM   6286 C C   . CYS D 1 90  ? 29.999  -20.646 -3.286  1.00 23.45 ? 90  CYS D C   1 
ATOM   6287 O O   . CYS D 1 90  ? 28.872  -20.750 -3.799  1.00 21.90 ? 90  CYS D O   1 
ATOM   6288 C CB  . CYS D 1 90  ? 31.740  -19.368 -4.565  1.00 26.67 ? 90  CYS D CB  1 
ATOM   6289 S SG  . CYS D 1 90  ? 33.346  -20.224 -4.303  1.00 28.05 ? 90  CYS D SG  1 
ATOM   6290 N N   . CYS D 1 91  ? 30.586  -21.665 -2.639  1.00 21.92 ? 91  CYS D N   1 
ATOM   6291 C CA  . CYS D 1 91  ? 29.933  -22.978 -2.597  1.00 23.07 ? 91  CYS D CA  1 
ATOM   6292 C C   . CYS D 1 91  ? 28.697  -22.981 -1.702  1.00 21.15 ? 91  CYS D C   1 
ATOM   6293 O O   . CYS D 1 91  ? 27.631  -23.421 -2.149  1.00 21.53 ? 91  CYS D O   1 
ATOM   6294 C CB  . CYS D 1 91  ? 30.924  -24.048 -2.140  1.00 22.63 ? 91  CYS D CB  1 
ATOM   6295 S SG  . CYS D 1 91  ? 30.297  -25.759 -2.212  1.00 24.50 ? 91  CYS D SG  1 
ATOM   6296 N N   . PRO D 1 92  ? 28.763  -22.563 -0.443  1.00 23.20 ? 92  PRO D N   1 
ATOM   6297 C CA  . PRO D 1 92  ? 27.530  -22.533 0.330   1.00 20.34 ? 92  PRO D CA  1 
ATOM   6298 C C   . PRO D 1 92  ? 26.502  -21.525 -0.251  1.00 24.04 ? 92  PRO D C   1 
ATOM   6299 O O   . PRO D 1 92  ? 25.297  -21.745 -0.109  1.00 20.55 ? 92  PRO D O   1 
ATOM   6300 C CB  . PRO D 1 92  ? 28.003  -22.184 1.747   1.00 20.77 ? 92  PRO D CB  1 
ATOM   6301 C CG  . PRO D 1 92  ? 29.360  -21.508 1.586   1.00 23.04 ? 92  PRO D CG  1 
ATOM   6302 C CD  . PRO D 1 92  ? 29.968  -22.160 0.347   1.00 22.36 ? 92  PRO D CD  1 
ATOM   6303 N N   . THR D 1 93  ? 26.928  -20.445 -0.938  1.00 23.02 ? 93  THR D N   1 
ATOM   6304 C CA  . THR D 1 93  ? 25.942  -19.585 -1.635  1.00 22.06 ? 93  THR D CA  1 
ATOM   6305 C C   . THR D 1 93  ? 25.269  -20.325 -2.787  1.00 22.04 ? 93  THR D C   1 
ATOM   6306 O O   . THR D 1 93  ? 24.077  -20.135 -3.056  1.00 19.46 ? 93  THR D O   1 
ATOM   6307 C CB  . THR D 1 93  ? 26.603  -18.313 -2.192  1.00 23.73 ? 93  THR D CB  1 
ATOM   6308 O OG1 . THR D 1 93  ? 27.381  -17.675 -1.173  1.00 24.48 ? 93  THR D OG1 1 
ATOM   6309 C CG2 . THR D 1 93  ? 25.489  -17.340 -2.738  1.00 26.61 ? 93  THR D CG2 1 
ATOM   6310 N N   . SER D 1 94  ? 26.028  -21.126 -3.535  1.00 21.57 ? 94  SER D N   1 
ATOM   6311 C CA  . SER D 1 94  ? 25.406  -21.948 -4.583  1.00 19.79 ? 94  SER D CA  1 
ATOM   6312 C C   . SER D 1 94  ? 24.439  -22.980 -3.996  1.00 19.98 ? 94  SER D C   1 
ATOM   6313 O O   . SER D 1 94  ? 23.375  -23.229 -4.565  1.00 19.93 ? 94  SER D O   1 
ATOM   6314 C CB  . SER D 1 94  ? 26.492  -22.667 -5.408  1.00 23.99 ? 94  SER D CB  1 
ATOM   6315 O OG  . SER D 1 94  ? 27.352  -21.737 -6.066  1.00 21.24 ? 94  SER D OG  1 
ATOM   6316 N N   . LEU D 1 95  ? 24.791  -23.583 -2.846  1.00 19.34 ? 95  LEU D N   1 
ATOM   6317 C CA  . LEU D 1 95  ? 23.896  -24.532 -2.207  1.00 21.20 ? 95  LEU D CA  1 
ATOM   6318 C C   . LEU D 1 95  ? 22.650  -23.829 -1.692  1.00 20.81 ? 95  LEU D C   1 
ATOM   6319 O O   . LEU D 1 95  ? 21.542  -24.382 -1.769  1.00 21.15 ? 95  LEU D O   1 
ATOM   6320 C CB  . LEU D 1 95  ? 24.624  -25.283 -1.084  1.00 21.67 ? 95  LEU D CB  1 
ATOM   6321 C CG  . LEU D 1 95  ? 23.768  -26.324 -0.311  1.00 23.15 ? 95  LEU D CG  1 
ATOM   6322 C CD1 . LEU D 1 95  ? 23.095  -27.282 -1.257  1.00 21.85 ? 95  LEU D CD1 1 
ATOM   6323 C CD2 . LEU D 1 95  ? 24.613  -27.092 0.728   1.00 26.63 ? 95  LEU D CD2 1 
ATOM   6324 N N   . SER D 1 96  ? 22.815  -22.583 -1.193  1.00 21.48 ? 96  SER D N   1 
ATOM   6325 C CA  . SER D 1 96  ? 21.658  -21.798 -0.778  1.00 21.42 ? 96  SER D CA  1 
ATOM   6326 C C   . SER D 1 96  ? 20.737  -21.530 -1.960  1.00 21.14 ? 96  SER D C   1 
ATOM   6327 O O   . SER D 1 96  ? 19.512  -21.645 -1.842  1.00 21.58 ? 96  SER D O   1 
ATOM   6328 C CB  . SER D 1 96  ? 22.091  -20.469 -0.137  1.00 22.29 ? 96  SER D CB  1 
ATOM   6329 O OG  . SER D 1 96  ? 20.948  -19.669 0.291   1.00 23.52 ? 96  SER D OG  1 
ATOM   6330 N N   . LEU D 1 97  ? 21.305  -21.139 -3.104  1.00 20.44 ? 97  LEU D N   1 
ATOM   6331 C CA  . LEU D 1 97  ? 20.465  -20.924 -4.281  1.00 20.12 ? 97  LEU D CA  1 
ATOM   6332 C C   . LEU D 1 97  ? 19.670  -22.194 -4.642  1.00 24.88 ? 97  LEU D C   1 
ATOM   6333 O O   . LEU D 1 97  ? 18.476  -22.123 -4.972  1.00 19.33 ? 97  LEU D O   1 
ATOM   6334 C CB  . LEU D 1 97  ? 21.315  -20.473 -5.445  1.00 16.09 ? 97  LEU D CB  1 
ATOM   6335 C CG  . LEU D 1 97  ? 21.882  -19.049 -5.288  1.00 22.14 ? 97  LEU D CG  1 
ATOM   6336 C CD1 . LEU D 1 97  ? 23.119  -18.847 -6.161  1.00 20.95 ? 97  LEU D CD1 1 
ATOM   6337 C CD2 . LEU D 1 97  ? 20.827  -17.948 -5.577  1.00 21.84 ? 97  LEU D CD2 1 
ATOM   6338 N N   . ALA D 1 98  ? 20.335  -23.362 -4.637  1.00 19.72 ? 98  ALA D N   1 
ATOM   6339 C CA  . ALA D 1 98  ? 19.630  -24.622 -4.867  1.00 24.42 ? 98  ALA D CA  1 
ATOM   6340 C C   . ALA D 1 98  ? 18.469  -24.810 -3.872  1.00 21.58 ? 98  ALA D C   1 
ATOM   6341 O O   . ALA D 1 98  ? 17.387  -25.281 -4.238  1.00 22.78 ? 98  ALA D O   1 
ATOM   6342 C CB  . ALA D 1 98  ? 20.616  -25.796 -4.796  1.00 17.03 ? 98  ALA D CB  1 
ATOM   6343 N N   . SER D 1 99  ? 18.689  -24.450 -2.606  1.00 22.24 ? 99  SER D N   1 
ATOM   6344 C CA  . SER D 1 99  ? 17.684  -24.672 -1.580  1.00 24.23 ? 99  SER D CA  1 
ATOM   6345 C C   . SER D 1 99  ? 16.420  -23.866 -1.865  1.00 25.38 ? 99  SER D C   1 
ATOM   6346 O O   . SER D 1 99  ? 15.316  -24.313 -1.526  1.00 25.16 ? 99  SER D O   1 
ATOM   6347 C CB  . SER D 1 99  ? 18.263  -24.356 -0.187  1.00 22.24 ? 99  SER D CB  1 
ATOM   6348 O OG  . SER D 1 99  ? 18.326  -22.953 0.068   1.00 24.05 ? 99  SER D OG  1 
ATOM   6349 N N   . GLN D 1 100 ? 16.564  -22.730 -2.556  1.00 26.65 ? 100 GLN D N   1 
ATOM   6350 C CA  . GLN D 1 100 ? 15.425  -21.962 -3.050  1.00 24.13 ? 100 GLN D CA  1 
ATOM   6351 C C   . GLN D 1 100 ? 14.618  -22.758 -4.070  1.00 26.25 ? 100 GLN D C   1 
ATOM   6352 O O   . GLN D 1 100 ? 13.375  -22.788 -4.014  1.00 24.76 ? 100 GLN D O   1 
ATOM   6353 C CB  . GLN D 1 100 ? 15.899  -20.666 -3.723  1.00 26.54 ? 100 GLN D CB  1 
ATOM   6354 C CG  . GLN D 1 100 ? 16.507  -19.627 -2.845  1.00 23.78 ? 100 GLN D CG  1 
ATOM   6355 C CD  . GLN D 1 100 ? 16.681  -18.347 -3.601  1.00 26.10 ? 100 GLN D CD  1 
ATOM   6356 O OE1 . GLN D 1 100 ? 15.771  -17.917 -4.302  1.00 24.29 ? 100 GLN D OE1 1 
ATOM   6357 N NE2 . GLN D 1 100 ? 17.875  -17.763 -3.536  1.00 22.23 ? 100 GLN D NE2 1 
ATOM   6358 N N   . MET D 1 101 ? 15.305  -23.316 -5.061  1.00 25.15 ? 101 MET D N   1 
ATOM   6359 C CA  . MET D 1 101 ? 14.650  -24.055 -6.140  1.00 24.59 ? 101 MET D CA  1 
ATOM   6360 C C   . MET D 1 101 ? 13.899  -25.268 -5.587  1.00 25.10 ? 101 MET D C   1 
ATOM   6361 O O   . MET D 1 101 ? 12.911  -25.714 -6.190  1.00 30.44 ? 101 MET D O   1 
ATOM   6362 C CB  . MET D 1 101 ? 15.709  -24.559 -7.121  1.00 27.69 ? 101 MET D CB  1 
ATOM   6363 C CG  . MET D 1 101 ? 16.429  -23.539 -8.075  1.00 29.72 ? 101 MET D CG  1 
ATOM   6364 S SD  . MET D 1 101 ? 15.224  -22.512 -8.822  1.00 37.30 ? 101 MET D SD  1 
ATOM   6365 C CE  . MET D 1 101 ? 15.179  -23.266 -10.482 1.00 39.72 ? 101 MET D CE  1 
ATOM   6366 N N   . LEU D 1 102 ? 14.378  -25.830 -4.456  1.00 24.95 ? 102 LEU D N   1 
ATOM   6367 C CA  . LEU D 1 102 ? 13.849  -27.036 -3.808  1.00 26.10 ? 102 LEU D CA  1 
ATOM   6368 C C   . LEU D 1 102 ? 12.800  -26.751 -2.740  1.00 25.52 ? 102 LEU D C   1 
ATOM   6369 O O   . LEU D 1 102 ? 12.283  -27.710 -2.131  1.00 25.49 ? 102 LEU D O   1 
ATOM   6370 C CB  . LEU D 1 102 ? 15.009  -27.870 -3.171  1.00 21.36 ? 102 LEU D CB  1 
ATOM   6371 C CG  . LEU D 1 102 ? 15.919  -28.565 -4.172  1.00 26.19 ? 102 LEU D CG  1 
ATOM   6372 C CD1 . LEU D 1 102 ? 17.096  -29.239 -3.468  1.00 25.86 ? 102 LEU D CD1 1 
ATOM   6373 C CD2 . LEU D 1 102 ? 15.115  -29.583 -5.037  1.00 25.41 ? 102 LEU D CD2 1 
ATOM   6374 N N   . TYR D 1 103 ? 12.515  -25.468 -2.475  1.00 21.94 ? 103 TYR D N   1 
ATOM   6375 C CA  . TYR D 1 103 ? 11.530  -25.049 -1.514  1.00 26.09 ? 103 TYR D CA  1 
ATOM   6376 C C   . TYR D 1 103 ? 11.895  -25.518 -0.114  1.00 25.61 ? 103 TYR D C   1 
ATOM   6377 O O   . TYR D 1 103 ? 11.023  -25.952 0.655   1.00 27.64 ? 103 TYR D O   1 
ATOM   6378 C CB  . TYR D 1 103 ? 10.120  -25.527 -1.921  1.00 20.46 ? 103 TYR D CB  1 
ATOM   6379 C CG  . TYR D 1 103 ? 9.580   -24.791 -3.178  1.00 21.10 ? 103 TYR D CG  1 
ATOM   6380 C CD1 . TYR D 1 103 ? 9.924   -25.200 -4.451  1.00 24.41 ? 103 TYR D CD1 1 
ATOM   6381 C CD2 . TYR D 1 103 ? 8.753   -23.670 -3.063  1.00 21.66 ? 103 TYR D CD2 1 
ATOM   6382 C CE1 . TYR D 1 103 ? 9.450   -24.558 -5.576  1.00 23.03 ? 103 TYR D CE1 1 
ATOM   6383 C CE2 . TYR D 1 103 ? 8.224   -23.035 -4.201  1.00 19.86 ? 103 TYR D CE2 1 
ATOM   6384 C CZ  . TYR D 1 103 ? 8.571   -23.470 -5.436  1.00 23.15 ? 103 TYR D CZ  1 
ATOM   6385 O OH  . TYR D 1 103 ? 8.128   -22.783 -6.549  1.00 24.14 ? 103 TYR D OH  1 
ATOM   6386 N N   . HIS D 1 104 ? 13.190  -25.455 0.211   1.00 24.13 ? 104 HIS D N   1 
ATOM   6387 C CA  . HIS D 1 104 ? 13.731  -25.829 1.537   1.00 22.51 ? 104 HIS D CA  1 
ATOM   6388 C C   . HIS D 1 104 ? 14.904  -24.889 1.865   1.00 29.29 ? 104 HIS D C   1 
ATOM   6389 O O   . HIS D 1 104 ? 16.066  -25.298 2.086   1.00 25.44 ? 104 HIS D O   1 
ATOM   6390 C CB  . HIS D 1 104 ? 14.141  -27.307 1.526   1.00 24.68 ? 104 HIS D CB  1 
ATOM   6391 C CG  . HIS D 1 104 ? 14.473  -27.871 2.880   1.00 31.30 ? 104 HIS D CG  1 
ATOM   6392 N ND1 . HIS D 1 104 ? 13.521  -28.073 3.868   1.00 29.95 ? 104 HIS D ND1 1 
ATOM   6393 C CD2 . HIS D 1 104 ? 15.635  -28.371 3.372   1.00 29.89 ? 104 HIS D CD2 1 
ATOM   6394 C CE1 . HIS D 1 104 ? 14.104  -28.613 4.930   1.00 33.29 ? 104 HIS D CE1 1 
ATOM   6395 N NE2 . HIS D 1 104 ? 15.390  -28.791 4.657   1.00 31.04 ? 104 HIS D NE2 1 
ATOM   6396 N N   . TYR D 1 105 ? 14.579  -23.591 1.913   1.00 23.29 ? 105 TYR D N   1 
ATOM   6397 C CA  . TYR D 1 105 ? 15.589  -22.534 1.924   1.00 23.06 ? 105 TYR D CA  1 
ATOM   6398 C C   . TYR D 1 105 ? 16.479  -22.658 3.136   1.00 24.78 ? 105 TYR D C   1 
ATOM   6399 O O   . TYR D 1 105 ? 15.993  -22.827 4.259   1.00 25.76 ? 105 TYR D O   1 
ATOM   6400 C CB  . TYR D 1 105 ? 14.912  -21.145 1.925   1.00 24.89 ? 105 TYR D CB  1 
ATOM   6401 C CG  . TYR D 1 105 ? 15.900  -19.989 2.106   1.00 22.24 ? 105 TYR D CG  1 
ATOM   6402 C CD1 . TYR D 1 105 ? 16.849  -19.686 1.121   1.00 21.95 ? 105 TYR D CD1 1 
ATOM   6403 C CD2 . TYR D 1 105 ? 15.947  -19.284 3.293   1.00 21.14 ? 105 TYR D CD2 1 
ATOM   6404 C CE1 . TYR D 1 105 ? 17.777  -18.650 1.282   1.00 21.48 ? 105 TYR D CE1 1 
ATOM   6405 C CE2 . TYR D 1 105 ? 16.868  -18.244 3.468   1.00 24.17 ? 105 TYR D CE2 1 
ATOM   6406 C CZ  . TYR D 1 105 ? 17.775  -17.933 2.450   1.00 22.54 ? 105 TYR D CZ  1 
ATOM   6407 O OH  . TYR D 1 105 ? 18.698  -16.934 2.626   1.00 22.12 ? 105 TYR D OH  1 
ATOM   6408 N N   . LYS D 1 106 ? 17.789  -22.578 2.900   1.00 23.79 ? 106 LYS D N   1 
ATOM   6409 C CA  . LYS D 1 106 ? 18.811  -22.449 3.934   1.00 28.40 ? 106 LYS D CA  1 
ATOM   6410 C C   . LYS D 1 106 ? 19.691  -21.280 3.545   1.00 23.49 ? 106 LYS D C   1 
ATOM   6411 O O   . LYS D 1 106 ? 20.124  -21.189 2.393   1.00 22.85 ? 106 LYS D O   1 
ATOM   6412 C CB  . LYS D 1 106 ? 19.685  -23.718 4.077   1.00 24.81 ? 106 LYS D CB  1 
ATOM   6413 C CG  . LYS D 1 106 ? 18.889  -25.014 4.395   1.00 30.24 ? 106 LYS D CG  1 
ATOM   6414 C CD  . LYS D 1 106 ? 18.233  -24.976 5.770   1.00 29.54 ? 106 LYS D CD  1 
ATOM   6415 C CE  . LYS D 1 106 ? 17.372  -26.203 6.009   1.00 30.21 ? 106 LYS D CE  1 
ATOM   6416 N NZ  . LYS D 1 106 ? 16.617  -26.074 7.269   1.00 37.42 ? 106 LYS D NZ  1 
ATOM   6417 N N   . SER D 1 107 ? 19.948  -20.393 4.488   1.00 23.54 ? 107 SER D N   1 
ATOM   6418 C CA  . SER D 1 107 ? 20.722  -19.200 4.177   1.00 23.36 ? 107 SER D CA  1 
ATOM   6419 C C   . SER D 1 107 ? 22.189  -19.546 3.828   1.00 23.17 ? 107 SER D C   1 
ATOM   6420 O O   . SER D 1 107 ? 22.693  -20.633 4.125   1.00 23.48 ? 107 SER D O   1 
ATOM   6421 C CB  . SER D 1 107 ? 20.683  -18.249 5.364   1.00 24.70 ? 107 SER D CB  1 
ATOM   6422 O OG  . SER D 1 107 ? 21.497  -18.771 6.405   1.00 25.42 ? 107 SER D OG  1 
ATOM   6423 N N   . GLU D 1 108 ? 22.884  -18.567 3.214   1.00 22.69 ? 108 GLU D N   1 
ATOM   6424 C CA  . GLU D 1 108 ? 24.297  -18.715 2.909   1.00 26.61 ? 108 GLU D CA  1 
ATOM   6425 C C   . GLU D 1 108 ? 25.085  -19.074 4.150   1.00 25.19 ? 108 GLU D C   1 
ATOM   6426 O O   . GLU D 1 108 ? 25.909  -20.009 4.119   1.00 24.21 ? 108 GLU D O   1 
ATOM   6427 C CB  . GLU D 1 108 ? 24.859  -17.432 2.278   1.00 27.63 ? 108 GLU D CB  1 
ATOM   6428 C CG  . GLU D 1 108 ? 26.291  -17.607 1.889   1.00 26.64 ? 108 GLU D CG  1 
ATOM   6429 C CD  . GLU D 1 108 ? 26.963  -16.298 1.424   1.00 32.49 ? 108 GLU D CD  1 
ATOM   6430 O OE1 . GLU D 1 108 ? 26.285  -15.491 0.728   1.00 29.78 ? 108 GLU D OE1 1 
ATOM   6431 O OE2 . GLU D 1 108 ? 28.173  -16.108 1.723   1.00 29.12 ? 108 GLU D OE2 1 
ATOM   6432 N N   . SER D 1 109 ? 24.805  -18.381 5.264   1.00 23.57 ? 109 SER D N   1 
ATOM   6433 C CA  . SER D 1 109 ? 25.547  -18.600 6.501   1.00 26.70 ? 109 SER D CA  1 
ATOM   6434 C C   . SER D 1 109 ? 25.292  -20.003 7.065   1.00 29.42 ? 109 SER D C   1 
ATOM   6435 O O   . SER D 1 109 ? 26.227  -20.720 7.445   1.00 29.46 ? 109 SER D O   1 
ATOM   6436 C CB  . SER D 1 109 ? 25.140  -17.528 7.524   1.00 30.17 ? 109 SER D CB  1 
ATOM   6437 O OG  . SER D 1 109 ? 25.877  -17.693 8.729   1.00 37.02 ? 109 SER D OG  1 
ATOM   6438 N N   . GLU D 1 110 ? 24.042  -20.433 7.067   1.00 26.84 ? 110 GLU D N   1 
ATOM   6439 C CA  . GLU D 1 110 ? 23.722  -21.783 7.495   1.00 31.46 ? 110 GLU D CA  1 
ATOM   6440 C C   . GLU D 1 110 ? 24.448  -22.834 6.669   1.00 28.13 ? 110 GLU D C   1 
ATOM   6441 O O   . GLU D 1 110 ? 24.896  -23.853 7.203   1.00 25.96 ? 110 GLU D O   1 
ATOM   6442 C CB  . GLU D 1 110 ? 22.222  -21.994 7.383   1.00 29.05 ? 110 GLU D CB  1 
ATOM   6443 C CG  . GLU D 1 110 ? 21.513  -21.827 8.653   1.00 36.01 ? 110 GLU D CG  1 
ATOM   6444 C CD  . GLU D 1 110 ? 20.361  -22.828 8.766   1.00 39.91 ? 110 GLU D CD  1 
ATOM   6445 O OE1 . GLU D 1 110 ? 20.552  -24.006 9.202   1.00 41.99 ? 110 GLU D OE1 1 
ATOM   6446 O OE2 . GLU D 1 110 ? 19.254  -22.412 8.411   1.00 39.82 ? 110 GLU D OE2 1 
ATOM   6447 N N   . CYS D 1 111 ? 24.507  -22.630 5.353   1.00 25.34 ? 111 CYS D N   1 
ATOM   6448 C CA  . CYS D 1 111 ? 25.175  -23.592 4.496   1.00 26.25 ? 111 CYS D CA  1 
ATOM   6449 C C   . CYS D 1 111 ? 26.670  -23.608 4.772   1.00 27.48 ? 111 CYS D C   1 
ATOM   6450 O O   . CYS D 1 111 ? 27.307  -24.682 4.782   1.00 26.24 ? 111 CYS D O   1 
ATOM   6451 C CB  . CYS D 1 111 ? 24.872  -23.272 3.022   1.00 24.31 ? 111 CYS D CB  1 
ATOM   6452 S SG  . CYS D 1 111 ? 23.152  -23.661 2.520   1.00 24.17 ? 111 CYS D SG  1 
ATOM   6453 N N   . ALA D 1 112 ? 27.241  -22.433 5.012   1.00 25.15 ? 112 ALA D N   1 
ATOM   6454 C CA  . ALA D 1 112 ? 28.670  -22.339 5.251   1.00 27.41 ? 112 ALA D CA  1 
ATOM   6455 C C   . ALA D 1 112 ? 29.046  -23.064 6.539   1.00 29.34 ? 112 ALA D C   1 
ATOM   6456 O O   . ALA D 1 112 ? 30.061  -23.792 6.593   1.00 28.26 ? 112 ALA D O   1 
ATOM   6457 C CB  . ALA D 1 112 ? 29.080  -20.856 5.308   1.00 25.10 ? 112 ALA D CB  1 
ATOM   6458 N N   . LYS D 1 113 ? 28.252  -22.853 7.589   1.00 28.20 ? 113 LYS D N   1 
ATOM   6459 C CA  . LYS D 1 113 ? 28.443  -23.576 8.842   1.00 28.94 ? 113 LYS D CA  1 
ATOM   6460 C C   . LYS D 1 113 ? 28.401  -25.092 8.621   1.00 30.27 ? 113 LYS D C   1 
ATOM   6461 O O   . LYS D 1 113 ? 29.279  -25.812 9.098   1.00 27.90 ? 113 LYS D O   1 
ATOM   6462 C CB  . LYS D 1 113 ? 27.398  -23.153 9.870   1.00 31.31 ? 113 LYS D CB  1 
ATOM   6463 C CG  . LYS D 1 113 ? 27.638  -21.773 10.483  1.00 35.35 ? 113 LYS D CG  1 
ATOM   6464 C CD  . LYS D 1 113 ? 26.311  -21.258 11.130  1.00 39.75 ? 113 LYS D CD  1 
ATOM   6465 C CE  . LYS D 1 113 ? 26.526  -19.983 11.962  1.00 43.77 ? 113 LYS D CE  1 
ATOM   6466 N NZ  . LYS D 1 113 ? 27.964  -19.875 12.467  1.00 42.86 ? 113 LYS D NZ  1 
ATOM   6467 N N   . ALA D 1 114 ? 27.375  -25.600 7.925   1.00 28.28 ? 114 ALA D N   1 
ATOM   6468 C CA  . ALA D 1 114 ? 27.271  -27.052 7.734   1.00 28.64 ? 114 ALA D CA  1 
ATOM   6469 C C   . ALA D 1 114 ? 28.432  -27.594 6.894   1.00 30.41 ? 114 ALA D C   1 
ATOM   6470 O O   . ALA D 1 114 ? 29.037  -28.624 7.222   1.00 28.12 ? 114 ALA D O   1 
ATOM   6471 C CB  . ALA D 1 114 ? 25.940  -27.415 7.074   1.00 26.39 ? 114 ALA D CB  1 
ATOM   6472 N N   . LEU D 1 115 ? 28.773  -26.914 5.818   1.00 28.49 ? 115 LEU D N   1 
ATOM   6473 C CA  . LEU D 1 115 ? 29.776  -27.437 4.916   1.00 27.15 ? 115 LEU D CA  1 
ATOM   6474 C C   . LEU D 1 115 ? 31.195  -27.349 5.484   1.00 28.70 ? 115 LEU D C   1 
ATOM   6475 O O   . LEU D 1 115 ? 32.098  -28.011 4.952   1.00 28.30 ? 115 LEU D O   1 
ATOM   6476 C CB  . LEU D 1 115 ? 29.700  -26.693 3.574   1.00 24.10 ? 115 LEU D CB  1 
ATOM   6477 C CG  . LEU D 1 115 ? 28.404  -26.838 2.776   1.00 27.57 ? 115 LEU D CG  1 
ATOM   6478 C CD1 . LEU D 1 115 ? 28.565  -26.348 1.332   1.00 23.90 ? 115 LEU D CD1 1 
ATOM   6479 C CD2 . LEU D 1 115 ? 27.777  -28.238 2.825   1.00 27.64 ? 115 LEU D CD2 1 
ATOM   6480 N N   . GLY D 1 116 ? 31.423  -26.544 6.520   1.00 25.89 ? 116 GLY D N   1 
ATOM   6481 C CA  . GLY D 1 116 ? 32.776  -26.299 6.968   1.00 30.20 ? 116 GLY D CA  1 
ATOM   6482 C C   . GLY D 1 116 ? 33.587  -25.383 6.063   1.00 31.15 ? 116 GLY D C   1 
ATOM   6483 O O   . GLY D 1 116 ? 34.805  -25.552 5.941   1.00 30.66 ? 116 GLY D O   1 
ATOM   6484 N N   . THR D 1 117 ? 32.950  -24.424 5.410   1.00 26.65 ? 117 THR D N   1 
ATOM   6485 C CA  . THR D 1 117 ? 33.674  -23.508 4.531   1.00 29.41 ? 117 THR D CA  1 
ATOM   6486 C C   . THR D 1 117 ? 34.704  -22.701 5.310   1.00 29.61 ? 117 THR D C   1 
ATOM   6487 O O   . THR D 1 117 ? 34.417  -22.169 6.388   1.00 30.05 ? 117 THR D O   1 
ATOM   6488 C CB  . THR D 1 117 ? 32.665  -22.575 3.852   1.00 29.51 ? 117 THR D CB  1 
ATOM   6489 O OG1 . THR D 1 117 ? 31.708  -23.377 3.154   1.00 29.05 ? 117 THR D OG1 1 
ATOM   6490 C CG2 . THR D 1 117 ? 33.324  -21.593 2.900   1.00 25.77 ? 117 THR D CG2 1 
ATOM   6491 N N   . SER D 1 118 ? 35.878  -22.514 4.717   1.00 30.11 ? 118 SER D N   1 
ATOM   6492 C CA  . SER D 1 118 ? 36.972  -21.834 5.404   1.00 33.23 ? 118 SER D CA  1 
ATOM   6493 C C   . SER D 1 118 ? 37.577  -20.708 4.564   1.00 32.27 ? 118 SER D C   1 
ATOM   6494 O O   . SER D 1 118 ? 37.634  -20.775 3.335   1.00 32.81 ? 118 SER D O   1 
ATOM   6495 C CB  . SER D 1 118 ? 38.071  -22.855 5.793   1.00 34.88 ? 118 SER D CB  1 
ATOM   6496 O OG  . SER D 1 118 ? 39.018  -22.971 4.730   1.00 35.76 ? 118 SER D OG  1 
ATOM   6497 N N   . LYS D 1 119 ? 38.047  -19.660 5.258   1.00 35.77 ? 119 LYS D N   1 
ATOM   6498 C CA  . LYS D 1 119 ? 38.687  -18.531 4.590   1.00 37.53 ? 119 LYS D CA  1 
ATOM   6499 C C   . LYS D 1 119 ? 39.894  -18.938 3.757   1.00 37.83 ? 119 LYS D C   1 
ATOM   6500 O O   . LYS D 1 119 ? 40.149  -18.322 2.716   1.00 42.43 ? 119 LYS D O   1 
ATOM   6501 C CB  . LYS D 1 119 ? 39.144  -17.489 5.614   1.00 39.99 ? 119 LYS D CB  1 
ATOM   6502 C CG  . LYS D 1 119 ? 38.013  -16.841 6.376   1.00 39.27 ? 119 LYS D CG  1 
ATOM   6503 C CD  . LYS D 1 119 ? 38.293  -16.744 7.869   1.00 42.79 ? 119 LYS D CD  1 
ATOM   6504 C CE  . LYS D 1 119 ? 37.878  -15.361 8.398   1.00 46.71 ? 119 LYS D CE  1 
ATOM   6505 N NZ  . LYS D 1 119 ? 38.201  -15.204 9.851   1.00 51.36 ? 119 LYS D NZ  1 
ATOM   6506 N N   . GLY D 1 120 ? 40.633  -19.964 4.174   1.00 39.43 ? 120 GLY D N   1 
ATOM   6507 C CA  . GLY D 1 120 ? 41.867  -20.321 3.493   1.00 40.97 ? 120 GLY D CA  1 
ATOM   6508 C C   . GLY D 1 120 ? 41.688  -21.213 2.281   1.00 46.55 ? 120 GLY D C   1 
ATOM   6509 O O   . GLY D 1 120 ? 42.435  -21.094 1.291   1.00 48.96 ? 120 GLY D O   1 
ATOM   6510 N N   . SER D 1 121 ? 40.735  -22.150 2.356   1.00 40.40 ? 121 SER D N   1 
ATOM   6511 C CA  . SER D 1 121 ? 40.569  -23.128 1.290   1.00 39.57 ? 121 SER D CA  1 
ATOM   6512 C C   . SER D 1 121 ? 39.178  -23.123 0.662   1.00 36.21 ? 121 SER D C   1 
ATOM   6513 O O   . SER D 1 121 ? 38.991  -23.763 -0.376  1.00 35.97 ? 121 SER D O   1 
ATOM   6514 C CB  . SER D 1 121 ? 40.943  -24.535 1.799   1.00 39.32 ? 121 SER D CB  1 
ATOM   6515 O OG  . SER D 1 121 ? 39.846  -25.150 2.452   1.00 42.54 ? 121 SER D OG  1 
ATOM   6516 N N   . GLY D 1 122 ? 38.231  -22.342 1.183   1.00 30.62 ? 122 GLY D N   1 
ATOM   6517 C CA  . GLY D 1 122 ? 36.893  -22.409 0.632   1.00 33.69 ? 122 GLY D CA  1 
ATOM   6518 C C   . GLY D 1 122 ? 36.194  -23.721 1.006   1.00 29.27 ? 122 GLY D C   1 
ATOM   6519 O O   . GLY D 1 122 ? 36.139  -24.112 2.171   1.00 28.73 ? 122 GLY D O   1 
ATOM   6520 N N   . THR D 1 123 ? 35.650  -24.405 0.004   1.00 25.97 ? 123 THR D N   1 
ATOM   6521 C CA  . THR D 1 123 ? 34.893  -25.636 0.209   1.00 27.48 ? 123 THR D CA  1 
ATOM   6522 C C   . THR D 1 123 ? 35.284  -26.625 -0.872  1.00 26.37 ? 123 THR D C   1 
ATOM   6523 O O   . THR D 1 123 ? 35.250  -26.280 -2.054  1.00 26.20 ? 123 THR D O   1 
ATOM   6524 C CB  . THR D 1 123 ? 33.373  -25.420 0.104   1.00 25.36 ? 123 THR D CB  1 
ATOM   6525 O OG1 . THR D 1 123 ? 32.985  -24.173 0.687   1.00 23.53 ? 123 THR D OG1 1 
ATOM   6526 C CG2 . THR D 1 123 ? 32.634  -26.622 0.753   1.00 25.01 ? 123 THR D CG2 1 
ATOM   6527 N N   . SER D 1 124 ? 35.624  -27.856 -0.483  1.00 28.06 ? 124 SER D N   1 
ATOM   6528 C CA  . SER D 1 124 ? 35.954  -28.852 -1.491  1.00 28.84 ? 124 SER D CA  1 
ATOM   6529 C C   . SER D 1 124 ? 34.698  -29.589 -1.931  1.00 25.25 ? 124 SER D C   1 
ATOM   6530 O O   . SER D 1 124 ? 33.676  -29.569 -1.243  1.00 25.26 ? 124 SER D O   1 
ATOM   6531 C CB  . SER D 1 124 ? 36.996  -29.852 -0.938  1.00 28.87 ? 124 SER D CB  1 
ATOM   6532 O OG  . SER D 1 124 ? 36.375  -30.718 0.010   1.00 26.76 ? 124 SER D OG  1 
ATOM   6533 N N   . PRO D 1 125 ? 34.733  -30.255 -3.081  1.00 27.01 ? 125 PRO D N   1 
ATOM   6534 C CA  . PRO D 1 125 ? 33.554  -31.056 -3.481  1.00 25.17 ? 125 PRO D CA  1 
ATOM   6535 C C   . PRO D 1 125 ? 33.188  -32.131 -2.484  1.00 25.52 ? 125 PRO D C   1 
ATOM   6536 O O   . PRO D 1 125 ? 31.980  -32.396 -2.258  1.00 25.16 ? 125 PRO D O   1 
ATOM   6537 C CB  . PRO D 1 125 ? 33.958  -31.654 -4.838  1.00 26.38 ? 125 PRO D CB  1 
ATOM   6538 C CG  . PRO D 1 125 ? 35.030  -30.738 -5.352  1.00 28.50 ? 125 PRO D CG  1 
ATOM   6539 C CD  . PRO D 1 125 ? 35.728  -30.108 -4.157  1.00 29.50 ? 125 PRO D CD  1 
ATOM   6540 N N   . ALA D 1 126 ? 34.184  -32.773 -1.866  1.00 25.36 ? 126 ALA D N   1 
ATOM   6541 C CA  . ALA D 1 126 ? 33.843  -33.809 -0.896  1.00 26.76 ? 126 ALA D CA  1 
ATOM   6542 C C   . ALA D 1 126 ? 33.155  -33.213 0.331   1.00 24.87 ? 126 ALA D C   1 
ATOM   6543 O O   . ALA D 1 126 ? 32.366  -33.900 0.979   1.00 23.64 ? 126 ALA D O   1 
ATOM   6544 C CB  . ALA D 1 126 ? 35.092  -34.656 -0.521  1.00 25.23 ? 126 ALA D CB  1 
ATOM   6545 N N   . GLN D 1 127 ? 33.501  -31.976 0.713   1.00 25.24 ? 127 GLN D N   1 
ATOM   6546 C CA  . GLN D 1 127 ? 32.836  -31.316 1.830   1.00 25.03 ? 127 GLN D CA  1 
ATOM   6547 C C   . GLN D 1 127 ? 31.375  -31.024 1.515   1.00 25.81 ? 127 GLN D C   1 
ATOM   6548 O O   . GLN D 1 127 ? 30.498  -31.200 2.372   1.00 26.27 ? 127 GLN D O   1 
ATOM   6549 C CB  . GLN D 1 127 ? 33.568  -30.019 2.181   1.00 28.97 ? 127 GLN D CB  1 
ATOM   6550 C CG  . GLN D 1 127 ? 34.767  -30.152 3.124   1.00 29.76 ? 127 GLN D CG  1 
ATOM   6551 C CD  . GLN D 1 127 ? 35.447  -28.801 3.378   1.00 31.37 ? 127 GLN D CD  1 
ATOM   6552 O OE1 . GLN D 1 127 ? 35.953  -28.172 2.455   1.00 29.97 ? 127 GLN D OE1 1 
ATOM   6553 N NE2 . GLN D 1 127 ? 35.383  -28.322 4.623   1.00 33.68 ? 127 GLN D NE2 1 
ATOM   6554 N N   . LEU D 1 128 ? 31.099  -30.603 0.282   1.00 24.62 ? 128 LEU D N   1 
ATOM   6555 C CA  . LEU D 1 128 ? 29.727  -30.352 -0.126  1.00 25.44 ? 128 LEU D CA  1 
ATOM   6556 C C   . LEU D 1 128 ? 28.907  -31.633 -0.095  1.00 24.27 ? 128 LEU D C   1 
ATOM   6557 O O   . LEU D 1 128 ? 27.784  -31.661 0.435   1.00 23.77 ? 128 LEU D O   1 
ATOM   6558 C CB  . LEU D 1 128 ? 29.715  -29.749 -1.536  1.00 23.85 ? 128 LEU D CB  1 
ATOM   6559 C CG  . LEU D 1 128 ? 28.331  -29.754 -2.170  1.00 22.47 ? 128 LEU D CG  1 
ATOM   6560 C CD1 . LEU D 1 128 ? 27.424  -28.703 -1.469  1.00 23.76 ? 128 LEU D CD1 1 
ATOM   6561 C CD2 . LEU D 1 128 ? 28.482  -29.468 -3.664  1.00 22.57 ? 128 LEU D CD2 1 
ATOM   6562 N N   . ILE D 1 129 ? 29.451  -32.707 -0.689  1.00 22.81 ? 129 ILE D N   1 
ATOM   6563 C CA  . ILE D 1 129 ? 28.732  -33.977 -0.749  1.00 26.33 ? 129 ILE D CA  1 
ATOM   6564 C C   . ILE D 1 129 ? 28.516  -34.527 0.655   1.00 30.96 ? 129 ILE D C   1 
ATOM   6565 O O   . ILE D 1 129 ? 27.412  -35.011 1.003   1.00 25.07 ? 129 ILE D O   1 
ATOM   6566 C CB  . ILE D 1 129 ? 29.506  -34.981 -1.630  1.00 27.41 ? 129 ILE D CB  1 
ATOM   6567 C CG1 . ILE D 1 129 ? 29.518  -34.533 -3.098  1.00 27.14 ? 129 ILE D CG1 1 
ATOM   6568 C CG2 . ILE D 1 129 ? 28.886  -36.354 -1.535  1.00 26.25 ? 129 ILE D CG2 1 
ATOM   6569 C CD1 . ILE D 1 129 ? 30.825  -35.044 -3.864  1.00 26.96 ? 129 ILE D CD1 1 
ATOM   6570 N N   . ALA D 1 130 ? 29.559  -34.428 1.508   1.00 26.17 ? 130 ALA D N   1 
ATOM   6571 C CA  . ALA D 1 130 ? 29.493  -35.107 2.803   1.00 28.66 ? 130 ALA D CA  1 
ATOM   6572 C C   . ALA D 1 130 ? 28.556  -34.427 3.804   1.00 29.14 ? 130 ALA D C   1 
ATOM   6573 O O   . ALA D 1 130 ? 28.035  -35.102 4.709   1.00 28.57 ? 130 ALA D O   1 
ATOM   6574 C CB  . ALA D 1 130 ? 30.879  -35.204 3.421   1.00 25.13 ? 130 ALA D CB  1 
ATOM   6575 N N   . ASN D 1 131 ? 28.368  -33.110 3.690   1.00 27.11 ? 131 ASN D N   1 
ATOM   6576 C CA  . ASN D 1 131 ? 27.660  -32.320 4.697   1.00 26.37 ? 131 ASN D CA  1 
ATOM   6577 C C   . ASN D 1 131 ? 26.292  -31.821 4.257   1.00 28.18 ? 131 ASN D C   1 
ATOM   6578 O O   . ASN D 1 131 ? 25.505  -31.390 5.106   1.00 26.61 ? 131 ASN D O   1 
ATOM   6579 C CB  . ASN D 1 131 ? 28.528  -31.133 5.118   1.00 30.45 ? 131 ASN D CB  1 
ATOM   6580 C CG  . ASN D 1 131 ? 29.712  -31.556 5.991   1.00 27.69 ? 131 ASN D CG  1 
ATOM   6581 O OD1 . ASN D 1 131 ? 29.534  -31.929 7.143   1.00 28.36 ? 131 ASN D OD1 1 
ATOM   6582 N ND2 . ASN D 1 131 ? 30.921  -31.464 5.449   1.00 31.08 ? 131 ASN D ND2 1 
ATOM   6583 N N   . ALA D 1 132 ? 25.954  -31.909 2.979   1.00 28.99 ? 132 ALA D N   1 
ATOM   6584 C CA  . ALA D 1 132 ? 24.615  -31.535 2.536   1.00 29.78 ? 132 ALA D CA  1 
ATOM   6585 C C   . ALA D 1 132 ? 23.502  -32.241 3.319   1.00 28.73 ? 132 ALA D C   1 
ATOM   6586 O O   . ALA D 1 132 ? 22.432  -31.632 3.522   1.00 27.89 ? 132 ALA D O   1 
ATOM   6587 C CB  . ALA D 1 132 ? 24.444  -31.830 1.040   1.00 30.33 ? 132 ALA D CB  1 
ATOM   6588 N N   . PRO D 1 133 ? 23.679  -33.493 3.784   1.00 27.85 ? 133 PRO D N   1 
ATOM   6589 C CA  . PRO D 1 133 ? 22.594  -34.106 4.583   1.00 29.54 ? 133 PRO D CA  1 
ATOM   6590 C C   . PRO D 1 133 ? 22.288  -33.357 5.861   1.00 27.61 ? 133 PRO D C   1 
ATOM   6591 O O   . PRO D 1 133 ? 21.169  -33.494 6.362   1.00 27.83 ? 133 PRO D O   1 
ATOM   6592 C CB  . PRO D 1 133 ? 23.097  -35.530 4.898   1.00 26.68 ? 133 PRO D CB  1 
ATOM   6593 C CG  . PRO D 1 133 ? 24.199  -35.814 3.927   1.00 29.06 ? 133 PRO D CG  1 
ATOM   6594 C CD  . PRO D 1 133 ? 24.723  -34.480 3.391   1.00 27.70 ? 133 PRO D CD  1 
ATOM   6595 N N   . LYS D 1 134 ? 23.224  -32.588 6.415   1.00 23.72 ? 134 LYS D N   1 
ATOM   6596 C CA  . LYS D 1 134 ? 22.939  -31.788 7.611   1.00 24.41 ? 134 LYS D CA  1 
ATOM   6597 C C   . LYS D 1 134 ? 21.776  -30.831 7.361   1.00 29.23 ? 134 LYS D C   1 
ATOM   6598 O O   . LYS D 1 134 ? 21.046  -30.471 8.297   1.00 26.54 ? 134 LYS D O   1 
ATOM   6599 C CB  . LYS D 1 134 ? 24.192  -30.997 8.051   1.00 29.14 ? 134 LYS D CB  1 
ATOM   6600 C CG  . LYS D 1 134 ? 24.916  -31.699 9.205   1.00 32.97 ? 134 LYS D CG  1 
ATOM   6601 C CD  . LYS D 1 134 ? 26.431  -31.806 9.057   1.00 35.60 ? 134 LYS D CD  1 
ATOM   6602 C CE  . LYS D 1 134 ? 27.108  -30.523 9.064   1.00 31.77 ? 134 LYS D CE  1 
ATOM   6603 N NZ  . LYS D 1 134 ? 28.455  -30.742 9.666   1.00 38.17 ? 134 LYS D NZ  1 
ATOM   6604 N N   . LEU D 1 135 ? 21.590  -30.413 6.106   1.00 28.95 ? 135 LEU D N   1 
ATOM   6605 C CA  . LEU D 1 135 ? 20.557  -29.452 5.728   1.00 29.22 ? 135 LEU D CA  1 
ATOM   6606 C C   . LEU D 1 135 ? 19.329  -30.119 5.120   1.00 29.27 ? 135 LEU D C   1 
ATOM   6607 O O   . LEU D 1 135 ? 18.419  -29.410 4.695   1.00 28.29 ? 135 LEU D O   1 
ATOM   6608 C CB  . LEU D 1 135 ? 21.127  -28.422 4.736   1.00 28.11 ? 135 LEU D CB  1 
ATOM   6609 C CG  . LEU D 1 135 ? 22.433  -27.782 5.169   1.00 26.26 ? 135 LEU D CG  1 
ATOM   6610 C CD1 . LEU D 1 135 ? 23.084  -27.137 3.981   1.00 28.49 ? 135 LEU D CD1 1 
ATOM   6611 C CD2 . LEU D 1 135 ? 22.213  -26.742 6.269   1.00 31.22 ? 135 LEU D CD2 1 
ATOM   6612 N N   . GLY D 1 136 ? 19.301  -31.459 5.024   1.00 27.31 ? 136 GLY D N   1 
ATOM   6613 C CA  . GLY D 1 136 ? 18.182  -32.149 4.433   1.00 26.53 ? 136 GLY D CA  1 
ATOM   6614 C C   . GLY D 1 136 ? 18.323  -32.473 2.971   1.00 31.22 ? 136 GLY D C   1 
ATOM   6615 O O   . GLY D 1 136 ? 17.321  -32.852 2.351   1.00 30.46 ? 136 GLY D O   1 
ATOM   6616 N N   . PHE D 1 137 ? 19.534  -32.353 2.399   1.00 27.49 ? 137 PHE D N   1 
ATOM   6617 C CA  . PHE D 1 137 ? 19.797  -32.574 0.983   1.00 28.43 ? 137 PHE D CA  1 
ATOM   6618 C C   . PHE D 1 137 ? 20.685  -33.784 0.742   1.00 28.60 ? 137 PHE D C   1 
ATOM   6619 O O   . PHE D 1 137 ? 21.371  -34.270 1.640   1.00 28.78 ? 137 PHE D O   1 
ATOM   6620 C CB  . PHE D 1 137 ? 20.486  -31.358 0.356   1.00 26.33 ? 137 PHE D CB  1 
ATOM   6621 C CG  . PHE D 1 137 ? 19.694  -30.086 0.517   1.00 27.16 ? 137 PHE D CG  1 
ATOM   6622 C CD1 . PHE D 1 137 ? 18.396  -30.018 0.041   1.00 23.17 ? 137 PHE D CD1 1 
ATOM   6623 C CD2 . PHE D 1 137 ? 20.258  -28.968 1.131   1.00 24.95 ? 137 PHE D CD2 1 
ATOM   6624 C CE1 . PHE D 1 137 ? 17.649  -28.821 0.184   1.00 27.83 ? 137 PHE D CE1 1 
ATOM   6625 C CE2 . PHE D 1 137 ? 19.519  -27.773 1.268   1.00 26.36 ? 137 PHE D CE2 1 
ATOM   6626 C CZ  . PHE D 1 137 ? 18.226  -27.711 0.796   1.00 27.09 ? 137 PHE D CZ  1 
ATOM   6627 N N   . LYS D 1 138 ? 20.628  -34.284 -0.487  1.00 27.21 ? 138 LYS D N   1 
ATOM   6628 C CA  . LYS D 1 138 ? 21.575  -35.275 -0.983  1.00 29.99 ? 138 LYS D CA  1 
ATOM   6629 C C   . LYS D 1 138 ? 22.208  -34.745 -2.258  1.00 29.03 ? 138 LYS D C   1 
ATOM   6630 O O   . LYS D 1 138 ? 21.521  -34.135 -3.082  1.00 28.56 ? 138 LYS D O   1 
ATOM   6631 C CB  . LYS D 1 138 ? 20.885  -36.617 -1.220  1.00 33.08 ? 138 LYS D CB  1 
ATOM   6632 C CG  . LYS D 1 138 ? 21.843  -37.638 -1.688  1.00 33.32 ? 138 LYS D CG  1 
ATOM   6633 C CD  . LYS D 1 138 ? 21.474  -38.087 -3.041  1.00 35.96 ? 138 LYS D CD  1 
ATOM   6634 C CE  . LYS D 1 138 ? 20.144  -38.788 -3.003  1.00 36.17 ? 138 LYS D CE  1 
ATOM   6635 N NZ  . LYS D 1 138 ? 19.562  -38.753 -4.389  1.00 42.86 ? 138 LYS D NZ  1 
ATOM   6636 N N   . ILE D 1 139 ? 23.524  -34.923 -2.401  1.00 28.62 ? 139 ILE D N   1 
ATOM   6637 C CA  . ILE D 1 139 ? 24.244  -34.510 -3.605  1.00 26.81 ? 139 ILE D CA  1 
ATOM   6638 C C   . ILE D 1 139 ? 24.530  -35.734 -4.464  1.00 28.04 ? 139 ILE D C   1 
ATOM   6639 O O   . ILE D 1 139 ? 25.054  -36.740 -3.962  1.00 29.14 ? 139 ILE D O   1 
ATOM   6640 C CB  . ILE D 1 139 ? 25.544  -33.799 -3.238  1.00 29.05 ? 139 ILE D CB  1 
ATOM   6641 C CG1 . ILE D 1 139 ? 25.260  -32.615 -2.317  1.00 27.79 ? 139 ILE D CG1 1 
ATOM   6642 C CG2 . ILE D 1 139 ? 26.286  -33.396 -4.500  1.00 27.74 ? 139 ILE D CG2 1 
ATOM   6643 C CD1 . ILE D 1 139 ? 24.444  -31.490 -2.959  1.00 27.73 ? 139 ILE D CD1 1 
ATOM   6644 N N   . ILE D 1 140 ? 24.198  -35.654 -5.753  1.00 26.84 ? 140 ILE D N   1 
ATOM   6645 C CA  . ILE D 1 140 ? 24.529  -36.733 -6.702  1.00 29.11 ? 140 ILE D CA  1 
ATOM   6646 C C   . ILE D 1 140 ? 25.610  -36.243 -7.669  1.00 30.17 ? 140 ILE D C   1 
ATOM   6647 O O   . ILE D 1 140 ? 25.332  -35.432 -8.570  1.00 27.78 ? 140 ILE D O   1 
ATOM   6648 C CB  . ILE D 1 140 ? 23.292  -37.232 -7.472  1.00 28.68 ? 140 ILE D CB  1 
ATOM   6649 C CG1 . ILE D 1 140 ? 22.163  -37.591 -6.508  1.00 31.76 ? 140 ILE D CG1 1 
ATOM   6650 C CG2 . ILE D 1 140 ? 23.637  -38.511 -8.249  1.00 29.95 ? 140 ILE D CG2 1 
ATOM   6651 C CD1 . ILE D 1 140 ? 20.874  -38.032 -7.190  1.00 31.89 ? 140 ILE D CD1 1 
ATOM   6652 N N   . PRO D 1 141 ? 26.864  -36.687 -7.510  1.00 30.52 ? 141 PRO D N   1 
ATOM   6653 C CA  . PRO D 1 141 ? 27.907  -36.347 -8.499  1.00 25.75 ? 141 PRO D CA  1 
ATOM   6654 C C   . PRO D 1 141 ? 27.610  -36.995 -9.841  1.00 29.49 ? 141 PRO D C   1 
ATOM   6655 O O   . PRO D 1 141 ? 27.298  -38.181 -9.917  1.00 29.87 ? 141 PRO D O   1 
ATOM   6656 C CB  . PRO D 1 141 ? 29.186  -36.898 -7.868  1.00 26.64 ? 141 PRO D CB  1 
ATOM   6657 C CG  . PRO D 1 141 ? 28.737  -37.898 -6.872  1.00 32.83 ? 141 PRO D CG  1 
ATOM   6658 C CD  . PRO D 1 141 ? 27.386  -37.482 -6.385  1.00 30.72 ? 141 PRO D CD  1 
ATOM   6659 N N   . ILE D 1 142 ? 27.596  -36.189 -10.891 1.00 28.47 ? 142 ILE D N   1 
ATOM   6660 C CA  . ILE D 1 142 ? 27.266  -36.669 -12.227 1.00 30.53 ? 142 ILE D CA  1 
ATOM   6661 C C   . ILE D 1 142 ? 28.416  -36.260 -13.129 1.00 30.61 ? 142 ILE D C   1 
ATOM   6662 O O   . ILE D 1 142 ? 29.251  -35.451 -12.740 1.00 30.34 ? 142 ILE D O   1 
ATOM   6663 C CB  . ILE D 1 142 ? 25.930  -36.125 -12.765 1.00 31.97 ? 142 ILE D CB  1 
ATOM   6664 C CG1 . ILE D 1 142 ? 25.980  -34.603 -12.866 1.00 31.53 ? 142 ILE D CG1 1 
ATOM   6665 C CG2 . ILE D 1 142 ? 24.760  -36.568 -11.867 1.00 27.51 ? 142 ILE D CG2 1 
ATOM   6666 C CD1 . ILE D 1 142 ? 24.998  -34.008 -13.831 1.00 30.01 ? 142 ILE D CD1 1 
ATOM   6667 N N   . LYS D 1 143 ? 28.498  -36.875 -14.313 1.00 30.54 ? 143 LYS D N   1 
ATOM   6668 C CA  . LYS D 1 143 ? 29.524  -36.474 -15.277 1.00 35.50 ? 143 LYS D CA  1 
ATOM   6669 C C   . LYS D 1 143 ? 29.233  -35.068 -15.806 1.00 34.53 ? 143 LYS D C   1 
ATOM   6670 O O   . LYS D 1 143 ? 28.080  -34.613 -15.847 1.00 36.22 ? 143 LYS D O   1 
ATOM   6671 C CB  . LYS D 1 143 ? 29.618  -37.460 -16.453 1.00 34.37 ? 143 LYS D CB  1 
ATOM   6672 C CG  . LYS D 1 143 ? 30.022  -38.876 -16.063 1.00 34.93 ? 143 LYS D CG  1 
ATOM   6673 C CD  . LYS D 1 143 ? 29.738  -39.890 -17.188 1.00 41.10 ? 143 LYS D CD  1 
ATOM   6674 C CE  . LYS D 1 143 ? 28.444  -39.553 -17.947 1.00 44.95 ? 143 LYS D CE  1 
ATOM   6675 N NZ  . LYS D 1 143 ? 27.571  -40.721 -18.233 1.00 50.18 ? 143 LYS D NZ  1 
ATOM   6676 N N   . ARG D 1 144 ? 30.296  -34.369 -16.192 1.00 32.66 ? 144 ARG D N   1 
ATOM   6677 C CA  . ARG D 1 144 ? 30.150  -33.012 -16.730 1.00 32.24 ? 144 ARG D CA  1 
ATOM   6678 C C   . ARG D 1 144 ? 29.607  -33.117 -18.156 1.00 34.34 ? 144 ARG D C   1 
ATOM   6679 O O   . ARG D 1 144 ? 30.298  -32.911 -19.148 1.00 35.10 ? 144 ARG D O   1 
ATOM   6680 C CB  . ARG D 1 144 ? 31.479  -32.272 -16.653 1.00 30.43 ? 144 ARG D CB  1 
ATOM   6681 C CG  . ARG D 1 144 ? 32.077  -32.259 -15.206 1.00 30.14 ? 144 ARG D CG  1 
ATOM   6682 C CD  . ARG D 1 144 ? 33.474  -31.621 -15.113 1.00 27.48 ? 144 ARG D CD  1 
ATOM   6683 N NE  . ARG D 1 144 ? 33.461  -30.201 -15.427 1.00 30.54 ? 144 ARG D NE  1 
ATOM   6684 C CZ  . ARG D 1 144 ? 33.465  -29.229 -14.519 1.00 29.18 ? 144 ARG D CZ  1 
ATOM   6685 N NH1 . ARG D 1 144 ? 33.395  -29.500 -13.227 1.00 24.12 ? 144 ARG D NH1 1 
ATOM   6686 N NH2 . ARG D 1 144 ? 33.550  -27.947 -14.925 1.00 28.02 ? 144 ARG D NH2 1 
ATOM   6687 N N   . ASP D 1 145 ? 28.316  -33.393 -18.265 1.00 35.95 ? 145 ASP D N   1 
ATOM   6688 C CA  . ASP D 1 145 ? 27.724  -33.719 -19.555 1.00 33.32 ? 145 ASP D CA  1 
ATOM   6689 C C   . ASP D 1 145 ? 26.306  -33.166 -19.588 1.00 38.05 ? 145 ASP D C   1 
ATOM   6690 O O   . ASP D 1 145 ? 25.504  -33.447 -18.694 1.00 37.43 ? 145 ASP D O   1 
ATOM   6691 C CB  . ASP D 1 145 ? 27.789  -35.243 -19.723 1.00 38.92 ? 145 ASP D CB  1 
ATOM   6692 C CG  . ASP D 1 145 ? 26.767  -35.826 -20.679 1.00 45.90 ? 145 ASP D CG  1 
ATOM   6693 O OD1 . ASP D 1 145 ? 26.086  -35.141 -21.487 1.00 49.15 ? 145 ASP D OD1 1 
ATOM   6694 O OD2 . ASP D 1 145 ? 26.688  -37.062 -20.632 1.00 52.36 ? 145 ASP D OD2 1 
ATOM   6695 N N   . SER D 1 146 ? 25.994  -32.424 -20.651 1.00 41.04 ? 146 SER D N   1 
ATOM   6696 C CA  . SER D 1 146 ? 24.746  -31.663 -20.726 1.00 39.51 ? 146 SER D CA  1 
ATOM   6697 C C   . SER D 1 146 ? 23.529  -32.567 -20.765 1.00 42.22 ? 146 SER D C   1 
ATOM   6698 O O   . SER D 1 146 ? 22.448  -32.157 -20.322 1.00 41.80 ? 146 SER D O   1 
ATOM   6699 C CB  . SER D 1 146 ? 24.765  -30.714 -21.920 1.00 37.45 ? 146 SER D CB  1 
ATOM   6700 O OG  . SER D 1 146 ? 24.768  -31.440 -23.133 1.00 42.03 ? 146 SER D OG  1 
ATOM   6701 N N   . LYS D 1 147 ? 23.673  -33.795 -21.266 1.00 41.68 ? 147 LYS D N   1 
ATOM   6702 C CA  . LYS D 1 147 ? 22.534  -34.704 -21.262 1.00 42.25 ? 147 LYS D CA  1 
ATOM   6703 C C   . LYS D 1 147 ? 22.162  -35.066 -19.828 1.00 40.10 ? 147 LYS D C   1 
ATOM   6704 O O   . LYS D 1 147 ? 20.974  -35.157 -19.481 1.00 35.33 ? 147 LYS D O   1 
ATOM   6705 C CB  . LYS D 1 147 ? 22.863  -35.967 -22.080 1.00 43.49 ? 147 LYS D CB  1 
ATOM   6706 C CG  . LYS D 1 147 ? 22.062  -37.227 -21.687 1.00 46.67 ? 147 LYS D CG  1 
ATOM   6707 C CD  . LYS D 1 147 ? 22.832  -38.215 -20.695 1.00 48.88 ? 147 LYS D CD  1 
ATOM   6708 C CE  . LYS D 1 147 ? 24.239  -38.612 -21.208 1.00 48.00 ? 147 LYS D CE  1 
ATOM   6709 N NZ  . LYS D 1 147 ? 24.706  -39.905 -20.606 1.00 52.38 ? 147 LYS D NZ  1 
ATOM   6710 N N   . GLU D 1 148 ? 23.175  -35.307 -18.988 1.00 39.03 ? 148 GLU D N   1 
ATOM   6711 C CA  . GLU D 1 148 ? 22.924  -35.627 -17.586 1.00 39.91 ? 148 GLU D CA  1 
ATOM   6712 C C   . GLU D 1 148 ? 22.392  -34.412 -16.841 1.00 35.89 ? 148 GLU D C   1 
ATOM   6713 O O   . GLU D 1 148 ? 21.485  -34.540 -16.006 1.00 35.09 ? 148 GLU D O   1 
ATOM   6714 C CB  . GLU D 1 148 ? 24.198  -36.143 -16.924 1.00 39.78 ? 148 GLU D CB  1 
ATOM   6715 C CG  . GLU D 1 148 ? 24.527  -37.598 -17.230 1.00 42.05 ? 148 GLU D CG  1 
ATOM   6716 C CD  . GLU D 1 148 ? 23.645  -38.562 -16.502 1.00 45.54 ? 148 GLU D CD  1 
ATOM   6717 O OE1 . GLU D 1 148 ? 23.833  -38.742 -15.274 1.00 45.22 ? 148 GLU D OE1 1 
ATOM   6718 O OE2 . GLU D 1 148 ? 22.748  -39.120 -17.154 1.00 47.69 ? 148 GLU D OE2 1 
ATOM   6719 N N   . VAL D 1 149 ? 22.960  -33.236 -17.108 1.00 32.40 ? 149 VAL D N   1 
ATOM   6720 C CA  . VAL D 1 149 ? 22.447  -32.006 -16.489 1.00 35.85 ? 149 VAL D CA  1 
ATOM   6721 C C   . VAL D 1 149 ? 20.966  -31.818 -16.827 1.00 34.82 ? 149 VAL D C   1 
ATOM   6722 O O   . VAL D 1 149 ? 20.143  -31.511 -15.957 1.00 34.35 ? 149 VAL D O   1 
ATOM   6723 C CB  . VAL D 1 149 ? 23.270  -30.788 -16.933 1.00 35.96 ? 149 VAL D CB  1 
ATOM   6724 C CG1 . VAL D 1 149 ? 22.529  -29.509 -16.583 1.00 32.89 ? 149 VAL D CG1 1 
ATOM   6725 C CG2 . VAL D 1 149 ? 24.675  -30.814 -16.299 1.00 29.50 ? 149 VAL D CG2 1 
ATOM   6726 N N   . LYS D 1 150 ? 20.609  -32.009 -18.103 1.00 37.52 ? 150 LYS D N   1 
ATOM   6727 C CA  . LYS D 1 150 ? 19.224  -31.857 -18.525 1.00 37.86 ? 150 LYS D CA  1 
ATOM   6728 C C   . LYS D 1 150 ? 18.326  -32.879 -17.846 1.00 39.00 ? 150 LYS D C   1 
ATOM   6729 O O   . LYS D 1 150 ? 17.194  -32.562 -17.468 1.00 38.80 ? 150 LYS D O   1 
ATOM   6730 C CB  . LYS D 1 150 ? 19.124  -31.975 -20.044 1.00 39.41 ? 150 LYS D CB  1 
ATOM   6731 C CG  . LYS D 1 150 ? 17.726  -31.760 -20.552 1.00 42.08 ? 150 LYS D CG  1 
ATOM   6732 C CD  . LYS D 1 150 ? 17.616  -32.111 -22.034 1.00 46.10 ? 150 LYS D CD  1 
ATOM   6733 C CE  . LYS D 1 150 ? 18.321  -31.086 -22.890 1.00 47.46 ? 150 LYS D CE  1 
ATOM   6734 N NZ  . LYS D 1 150 ? 18.204  -31.392 -24.347 1.00 48.66 ? 150 LYS D NZ  1 
ATOM   6735 N N   . LYS D 1 151 ? 18.822  -34.106 -17.646 1.00 37.99 ? 151 LYS D N   1 
ATOM   6736 C CA  . LYS D 1 151 ? 17.980  -35.133 -17.042 1.00 38.38 ? 151 LYS D CA  1 
ATOM   6737 C C   . LYS D 1 151 ? 17.577  -34.739 -15.636 1.00 38.21 ? 151 LYS D C   1 
ATOM   6738 O O   . LYS D 1 151 ? 16.416  -34.909 -15.241 1.00 37.43 ? 151 LYS D O   1 
ATOM   6739 C CB  . LYS D 1 151 ? 18.698  -36.482 -17.012 1.00 39.23 ? 151 LYS D CB  1 
ATOM   6740 C CG  . LYS D 1 151 ? 17.880  -37.548 -16.328 1.00 41.50 ? 151 LYS D CG  1 
ATOM   6741 C CD  . LYS D 1 151 ? 18.630  -38.244 -15.208 1.00 41.71 ? 151 LYS D CD  1 
ATOM   6742 C CE  . LYS D 1 151 ? 19.713  -39.141 -15.774 1.00 44.01 ? 151 LYS D CE  1 
ATOM   6743 N NZ  . LYS D 1 151 ? 19.793  -40.430 -14.969 1.00 48.63 ? 151 LYS D NZ  1 
ATOM   6744 N N   . TYR D 1 152 ? 18.522  -34.186 -14.863 1.00 35.01 ? 152 TYR D N   1 
ATOM   6745 C CA  . TYR D 1 152 ? 18.190  -33.888 -13.481 1.00 31.92 ? 152 TYR D CA  1 
ATOM   6746 C C   . TYR D 1 152 ? 17.438  -32.577 -13.357 1.00 32.96 ? 152 TYR D C   1 
ATOM   6747 O O   . TYR D 1 152 ? 16.597  -32.434 -12.468 1.00 34.92 ? 152 TYR D O   1 
ATOM   6748 C CB  . TYR D 1 152 ? 19.460  -33.929 -12.627 1.00 32.84 ? 152 TYR D CB  1 
ATOM   6749 C CG  . TYR D 1 152 ? 19.877  -35.352 -12.342 1.00 34.51 ? 152 TYR D CG  1 
ATOM   6750 C CD1 . TYR D 1 152 ? 19.174  -36.132 -11.422 1.00 35.09 ? 152 TYR D CD1 1 
ATOM   6751 C CD2 . TYR D 1 152 ? 20.944  -35.936 -13.020 1.00 35.85 ? 152 TYR D CD2 1 
ATOM   6752 C CE1 . TYR D 1 152 ? 19.540  -37.429 -11.171 1.00 36.35 ? 152 TYR D CE1 1 
ATOM   6753 C CE2 . TYR D 1 152 ? 21.303  -37.244 -12.777 1.00 37.66 ? 152 TYR D CE2 1 
ATOM   6754 C CZ  . TYR D 1 152 ? 20.608  -37.977 -11.846 1.00 36.48 ? 152 TYR D CZ  1 
ATOM   6755 O OH  . TYR D 1 152 ? 20.965  -39.265 -11.578 1.00 37.13 ? 152 TYR D OH  1 
ATOM   6756 N N   . LEU D 1 153 ? 17.645  -31.651 -14.285 1.00 33.76 ? 153 LEU D N   1 
ATOM   6757 C CA  . LEU D 1 153 ? 16.816  -30.454 -14.284 1.00 34.29 ? 153 LEU D CA  1 
ATOM   6758 C C   . LEU D 1 153 ? 15.342  -30.807 -14.519 1.00 40.20 ? 153 LEU D C   1 
ATOM   6759 O O   . LEU D 1 153 ? 14.430  -30.161 -13.947 1.00 34.85 ? 153 LEU D O   1 
ATOM   6760 C CB  . LEU D 1 153 ? 17.337  -29.487 -15.350 1.00 35.26 ? 153 LEU D CB  1 
ATOM   6761 C CG  . LEU D 1 153 ? 18.562  -28.602 -15.009 1.00 32.87 ? 153 LEU D CG  1 
ATOM   6762 C CD1 . LEU D 1 153 ? 18.849  -27.660 -16.159 1.00 31.50 ? 153 LEU D CD1 1 
ATOM   6763 C CD2 . LEU D 1 153 ? 18.341  -27.798 -13.728 1.00 27.93 ? 153 LEU D CD2 1 
ATOM   6764 N N   . LYS D 1 154 ? 15.093  -31.858 -15.314 1.00 38.53 ? 154 LYS D N   1 
ATOM   6765 C CA  . LYS D 1 154 ? 13.725  -32.312 -15.549 1.00 39.10 ? 154 LYS D CA  1 
ATOM   6766 C C   . LYS D 1 154 ? 13.100  -32.849 -14.272 1.00 41.62 ? 154 LYS D C   1 
ATOM   6767 O O   . LYS D 1 154 ? 11.904  -32.639 -14.015 1.00 42.87 ? 154 LYS D O   1 
ATOM   6768 C CB  . LYS D 1 154 ? 13.709  -33.399 -16.624 1.00 41.03 ? 154 LYS D CB  1 
ATOM   6769 C CG  . LYS D 1 154 ? 12.278  -33.905 -17.001 1.00 47.67 ? 154 LYS D CG  1 
ATOM   6770 C CD  . LYS D 1 154 ? 12.113  -35.447 -16.765 1.00 45.30 ? 154 LYS D CD  1 
ATOM   6771 C CE  . LYS D 1 154 ? 12.025  -35.788 -15.259 1.00 45.98 ? 154 LYS D CE  1 
ATOM   6772 N NZ  . LYS D 1 154 ? 11.936  -37.266 -14.918 1.00 42.51 ? 154 LYS D NZ  1 
ATOM   6773 N N   . LYS D 1 155 ? 13.896  -33.522 -13.443 1.00 39.19 ? 155 LYS D N   1 
ATOM   6774 C CA  . LYS D 1 155 ? 13.358  -34.039 -12.196 1.00 40.70 ? 155 LYS D CA  1 
ATOM   6775 C C   . LYS D 1 155 ? 13.093  -32.950 -11.161 1.00 36.71 ? 155 LYS D C   1 
ATOM   6776 O O   . LYS D 1 155 ? 12.621  -33.291 -10.074 1.00 40.19 ? 155 LYS D O   1 
ATOM   6777 C CB  . LYS D 1 155 ? 14.336  -35.079 -11.622 1.00 39.55 ? 155 LYS D CB  1 
ATOM   6778 C CG  . LYS D 1 155 ? 14.529  -36.342 -12.479 1.00 41.58 ? 155 LYS D CG  1 
ATOM   6779 C CD  . LYS D 1 155 ? 15.313  -37.424 -11.722 1.00 40.02 ? 155 LYS D CD  1 
ATOM   6780 C CE  . LYS D 1 155 ? 14.551  -38.792 -11.726 1.00 50.32 ? 155 LYS D CE  1 
ATOM   6781 N NZ  . LYS D 1 155 ? 13.951  -39.136 -13.063 1.00 50.88 ? 155 LYS D NZ  1 
ATOM   6782 N N   . GLY D 1 156 ? 13.403  -31.678 -11.450 1.00 38.21 ? 156 GLY D N   1 
ATOM   6783 C CA  . GLY D 1 156 ? 13.293  -30.579 -10.494 1.00 37.10 ? 156 GLY D CA  1 
ATOM   6784 C C   . GLY D 1 156 ? 14.546  -30.271 -9.685  1.00 34.50 ? 156 GLY D C   1 
ATOM   6785 O O   . GLY D 1 156 ? 14.477  -29.483 -8.733  1.00 33.01 ? 156 GLY D O   1 
ATOM   6786 N N   . PHE D 1 157 ? 15.691  -30.863 -10.025 1.00 33.13 ? 157 PHE D N   1 
ATOM   6787 C CA  . PHE D 1 157 ? 16.874  -30.708 -9.192  1.00 31.76 ? 157 PHE D CA  1 
ATOM   6788 C C   . PHE D 1 157 ? 17.873  -29.786 -9.877  1.00 31.26 ? 157 PHE D C   1 
ATOM   6789 O O   . PHE D 1 157 ? 18.293  -30.088 -11.009 1.00 29.29 ? 157 PHE D O   1 
ATOM   6790 C CB  . PHE D 1 157 ? 17.537  -32.061 -8.896  1.00 32.18 ? 157 PHE D CB  1 
ATOM   6791 C CG  . PHE D 1 157 ? 16.603  -33.112 -8.343  1.00 34.01 ? 157 PHE D CG  1 
ATOM   6792 C CD1 . PHE D 1 157 ? 15.503  -32.755 -7.557  1.00 33.96 ? 157 PHE D CD1 1 
ATOM   6793 C CD2 . PHE D 1 157 ? 16.856  -34.475 -8.570  1.00 36.08 ? 157 PHE D CD2 1 
ATOM   6794 C CE1 . PHE D 1 157 ? 14.635  -33.748 -7.033  1.00 35.13 ? 157 PHE D CE1 1 
ATOM   6795 C CE2 . PHE D 1 157 ? 15.993  -35.454 -8.071  1.00 36.19 ? 157 PHE D CE2 1 
ATOM   6796 C CZ  . PHE D 1 157 ? 14.888  -35.089 -7.285  1.00 32.71 ? 157 PHE D CZ  1 
ATOM   6797 N N   . PRO D 1 158 ? 18.302  -28.681 -9.257  1.00 30.67 ? 158 PRO D N   1 
ATOM   6798 C CA  . PRO D 1 158 ? 19.360  -27.858 -9.862  1.00 28.20 ? 158 PRO D CA  1 
ATOM   6799 C C   . PRO D 1 158 ? 20.710  -28.540 -9.672  1.00 25.91 ? 158 PRO D C   1 
ATOM   6800 O O   . PRO D 1 158 ? 20.844  -29.501 -8.903  1.00 27.22 ? 158 PRO D O   1 
ATOM   6801 C CB  . PRO D 1 158 ? 19.287  -26.550 -9.081  1.00 24.33 ? 158 PRO D CB  1 
ATOM   6802 C CG  . PRO D 1 158 ? 18.930  -27.022 -7.701  1.00 26.61 ? 158 PRO D CG  1 
ATOM   6803 C CD  . PRO D 1 158 ? 17.946  -28.196 -7.904  1.00 26.49 ? 158 PRO D CD  1 
ATOM   6804 N N   . VAL D 1 159 ? 21.727  -28.023 -10.369 1.00 25.92 ? 159 VAL D N   1 
ATOM   6805 C CA  . VAL D 1 159 ? 23.030  -28.704 -10.443 1.00 26.99 ? 159 VAL D CA  1 
ATOM   6806 C C   . VAL D 1 159 ? 24.154  -27.717 -10.136 1.00 21.36 ? 159 VAL D C   1 
ATOM   6807 O O   . VAL D 1 159 ? 24.430  -26.814 -10.929 1.00 23.31 ? 159 VAL D O   1 
ATOM   6808 C CB  . VAL D 1 159 ? 23.246  -29.367 -11.809 1.00 25.91 ? 159 VAL D CB  1 
ATOM   6809 C CG1 . VAL D 1 159 ? 24.553  -30.128 -11.809 1.00 27.31 ? 159 VAL D CG1 1 
ATOM   6810 C CG2 . VAL D 1 159 ? 22.077  -30.324 -12.135 1.00 27.05 ? 159 VAL D CG2 1 
ATOM   6811 N N   . ILE D 1 160 ? 24.824  -27.908 -9.006  1.00 20.06 ? 160 ILE D N   1 
ATOM   6812 C CA  . ILE D 1 160 ? 25.960  -27.068 -8.657  1.00 21.73 ? 160 ILE D CA  1 
ATOM   6813 C C   . ILE D 1 160 ? 27.131  -27.408 -9.570  1.00 25.10 ? 160 ILE D C   1 
ATOM   6814 O O   . ILE D 1 160 ? 27.433  -28.586 -9.783  1.00 23.53 ? 160 ILE D O   1 
ATOM   6815 C CB  . ILE D 1 160 ? 26.349  -27.284 -7.184  1.00 23.06 ? 160 ILE D CB  1 
ATOM   6816 C CG1 . ILE D 1 160 ? 25.315  -26.627 -6.257  1.00 20.74 ? 160 ILE D CG1 1 
ATOM   6817 C CG2 . ILE D 1 160 ? 27.791  -26.788 -6.961  1.00 22.25 ? 160 ILE D CG2 1 
ATOM   6818 C CD1 . ILE D 1 160 ? 25.533  -26.860 -4.708  1.00 21.75 ? 160 ILE D CD1 1 
ATOM   6819 N N   . CYS D 1 161 ? 27.754  -26.384 -10.152 1.00 22.83 ? 161 CYS D N   1 
ATOM   6820 C CA  . CYS D 1 161 ? 28.874  -26.556 -11.068 1.00 25.14 ? 161 CYS D CA  1 
ATOM   6821 C C   . CYS D 1 161 ? 30.134  -25.989 -10.429 1.00 27.74 ? 161 CYS D C   1 
ATOM   6822 O O   . CYS D 1 161 ? 30.052  -25.103 -9.572  1.00 24.18 ? 161 CYS D O   1 
ATOM   6823 C CB  . CYS D 1 161 ? 28.582  -25.875 -12.411 1.00 26.14 ? 161 CYS D CB  1 
ATOM   6824 S SG  . CYS D 1 161 ? 28.325  -24.027 -12.340 1.00 29.59 ? 161 CYS D SG  1 
ATOM   6825 N N   . HIS D 1 162 ? 31.303  -26.511 -10.858 1.00 26.78 ? 162 HIS D N   1 
ATOM   6826 C CA  . HIS D 1 162 ? 32.620  -26.185 -10.311 1.00 26.43 ? 162 HIS D CA  1 
ATOM   6827 C C   . HIS D 1 162 ? 33.605  -26.031 -11.456 1.00 26.62 ? 162 HIS D C   1 
ATOM   6828 O O   . HIS D 1 162 ? 33.698  -26.905 -12.324 1.00 27.96 ? 162 HIS D O   1 
ATOM   6829 C CB  . HIS D 1 162 ? 33.094  -27.287 -9.338  1.00 28.72 ? 162 HIS D CB  1 
ATOM   6830 C CG  . HIS D 1 162 ? 34.441  -27.058 -8.714  1.00 28.96 ? 162 HIS D CG  1 
ATOM   6831 N ND1 . HIS D 1 162 ? 35.402  -28.044 -8.633  1.00 30.55 ? 162 HIS D ND1 1 
ATOM   6832 C CD2 . HIS D 1 162 ? 34.974  -25.971 -8.105  1.00 28.61 ? 162 HIS D CD2 1 
ATOM   6833 C CE1 . HIS D 1 162 ? 36.463  -27.575 -8.000  1.00 32.63 ? 162 HIS D CE1 1 
ATOM   6834 N NE2 . HIS D 1 162 ? 36.231  -26.315 -7.678  1.00 31.00 ? 162 HIS D NE2 1 
ATOM   6835 N N   . TRP D 1 163 ? 34.348  -24.934 -11.464 1.00 25.66 ? 163 TRP D N   1 
ATOM   6836 C CA  . TRP D 1 163 ? 35.278  -24.743 -12.556 1.00 27.02 ? 163 TRP D CA  1 
ATOM   6837 C C   . TRP D 1 163 ? 36.393  -23.809 -12.119 1.00 30.72 ? 163 TRP D C   1 
ATOM   6838 O O   . TRP D 1 163 ? 36.302  -23.150 -11.075 1.00 28.62 ? 163 TRP D O   1 
ATOM   6839 C CB  . TRP D 1 163 ? 34.547  -24.252 -13.800 1.00 24.16 ? 163 TRP D CB  1 
ATOM   6840 C CG  . TRP D 1 163 ? 34.149  -22.791 -13.855 1.00 29.12 ? 163 TRP D CG  1 
ATOM   6841 C CD1 . TRP D 1 163 ? 34.757  -21.811 -14.568 1.00 29.70 ? 163 TRP D CD1 1 
ATOM   6842 C CD2 . TRP D 1 163 ? 33.016  -22.173 -13.201 1.00 27.03 ? 163 TRP D CD2 1 
ATOM   6843 N NE1 . TRP D 1 163 ? 34.058  -20.612 -14.421 1.00 31.05 ? 163 TRP D NE1 1 
ATOM   6844 C CE2 . TRP D 1 163 ? 33.000  -20.813 -13.578 1.00 28.66 ? 163 TRP D CE2 1 
ATOM   6845 C CE3 . TRP D 1 163 ? 32.018  -22.647 -12.342 1.00 28.66 ? 163 TRP D CE3 1 
ATOM   6846 C CZ2 . TRP D 1 163 ? 32.025  -19.907 -13.113 1.00 28.00 ? 163 TRP D CZ2 1 
ATOM   6847 C CZ3 . TRP D 1 163 ? 31.062  -21.760 -11.872 1.00 26.42 ? 163 TRP D CZ3 1 
ATOM   6848 C CH2 . TRP D 1 163 ? 31.070  -20.402 -12.264 1.00 30.27 ? 163 TRP D CH2 1 
ATOM   6849 N N   . GLN D 1 164 ? 37.469  -23.789 -12.920 1.00 26.16 ? 164 GLN D N   1 
ATOM   6850 C CA  . GLN D 1 164 ? 38.565  -22.838 -12.731 1.00 28.64 ? 164 GLN D CA  1 
ATOM   6851 C C   . GLN D 1 164 ? 38.358  -21.687 -13.710 1.00 32.16 ? 164 GLN D C   1 
ATOM   6852 O O   . GLN D 1 164 ? 38.250  -21.919 -14.919 1.00 32.23 ? 164 GLN D O   1 
ATOM   6853 C CB  . GLN D 1 164 ? 39.920  -23.508 -12.943 1.00 34.57 ? 164 GLN D CB  1 
ATOM   6854 C CG  . GLN D 1 164 ? 40.000  -24.864 -12.302 1.00 31.98 ? 164 GLN D CG  1 
ATOM   6855 C CD  . GLN D 1 164 ? 40.067  -24.777 -10.783 1.00 32.37 ? 164 GLN D CD  1 
ATOM   6856 O OE1 . GLN D 1 164 ? 40.762  -23.938 -10.231 1.00 33.10 ? 164 GLN D OE1 1 
ATOM   6857 N NE2 . GLN D 1 164 ? 39.297  -25.619 -10.103 1.00 34.10 ? 164 GLN D NE2 1 
ATOM   6858 N N   . VAL D 1 165 ? 38.192  -20.464 -13.184 1.00 32.05 ? 165 VAL D N   1 
ATOM   6859 C CA  . VAL D 1 165 ? 37.695  -19.378 -14.035 1.00 31.53 ? 165 VAL D CA  1 
ATOM   6860 C C   . VAL D 1 165 ? 38.717  -19.022 -15.107 1.00 34.41 ? 165 VAL D C   1 
ATOM   6861 O O   . VAL D 1 165 ? 38.344  -18.554 -16.193 1.00 35.60 ? 165 VAL D O   1 
ATOM   6862 C CB  . VAL D 1 165 ? 37.317  -18.127 -13.217 1.00 31.37 ? 165 VAL D CB  1 
ATOM   6863 C CG1 . VAL D 1 165 ? 36.108  -18.420 -12.339 1.00 28.72 ? 165 VAL D CG1 1 
ATOM   6864 C CG2 . VAL D 1 165 ? 38.497  -17.604 -12.408 1.00 31.78 ? 165 VAL D CG2 1 
ATOM   6865 N N   . ASN D 1 166 ? 40.008  -19.267 -14.846 1.00 36.14 ? 166 ASN D N   1 
ATOM   6866 C CA  . ASN D 1 166 ? 41.022  -19.050 -15.886 1.00 40.05 ? 166 ASN D CA  1 
ATOM   6867 C C   . ASN D 1 166 ? 40.790  -19.944 -17.107 1.00 40.25 ? 166 ASN D C   1 
ATOM   6868 O O   . ASN D 1 166 ? 41.041  -19.523 -18.248 1.00 42.25 ? 166 ASN D O   1 
ATOM   6869 C CB  . ASN D 1 166 ? 42.423  -19.273 -15.328 1.00 39.51 ? 166 ASN D CB  1 
ATOM   6870 C CG  . ASN D 1 166 ? 42.507  -20.487 -14.405 1.00 45.65 ? 166 ASN D CG  1 
ATOM   6871 O OD1 . ASN D 1 166 ? 42.261  -20.385 -13.177 1.00 44.91 ? 166 ASN D OD1 1 
ATOM   6872 N ND2 . ASN D 1 166 ? 42.891  -21.639 -14.979 1.00 41.30 ? 166 ASN D ND2 1 
ATOM   6873 N N   . GLN D 1 167 ? 40.289  -21.153 -16.888 1.00 39.02 ? 167 GLN D N   1 
ATOM   6874 C CA  . GLN D 1 167 ? 40.055  -22.084 -18.017 1.00 36.51 ? 167 GLN D CA  1 
ATOM   6875 C C   . GLN D 1 167 ? 38.824  -21.672 -18.823 1.00 38.56 ? 167 GLN D C   1 
ATOM   6876 O O   . GLN D 1 167 ? 38.608  -22.265 -19.857 1.00 34.72 ? 167 GLN D O   1 
ATOM   6877 C CB  . GLN D 1 167 ? 39.981  -23.519 -17.515 1.00 35.33 ? 167 GLN D CB  1 
ATOM   6878 C CG  . GLN D 1 167 ? 41.144  -23.901 -16.622 1.00 36.17 ? 167 GLN D CG  1 
ATOM   6879 C CD  . GLN D 1 167 ? 41.188  -25.386 -16.391 1.00 31.65 ? 167 GLN D CD  1 
ATOM   6880 O OE1 . GLN D 1 167 ? 40.604  -26.142 -17.133 1.00 32.10 ? 167 GLN D OE1 1 
ATOM   6881 N NE2 . GLN D 1 167 ? 41.848  -25.792 -15.328 1.00 29.31 ? 167 GLN D NE2 1 
ATOM   6882 N N   . SER D 1 168 ? 38.056  -20.695 -18.350 1.00 35.49 ? 168 SER D N   1 
ATOM   6883 C CA  . SER D 1 168 ? 36.860  -20.269 -19.109 1.00 40.09 ? 168 SER D CA  1 
ATOM   6884 C C   . SER D 1 168 ? 37.082  -18.863 -19.663 1.00 42.46 ? 168 SER D C   1 
ATOM   6885 O O   . SER D 1 168 ? 36.175  -18.330 -20.264 1.00 43.69 ? 168 SER D O   1 
ATOM   6886 C CB  . SER D 1 168 ? 35.620  -20.343 -18.259 1.00 34.65 ? 168 SER D CB  1 
ATOM   6887 O OG  . SER D 1 168 ? 35.642  -19.387 -17.230 1.00 34.09 ? 168 SER D OG  1 
ATOM   6888 N N   . ARG D 1 169 ? 38.278  -18.319 -19.472 1.00 43.90 ? 169 ARG D N   1 
ATOM   6889 C CA  . ARG D 1 169 ? 38.624  -16.936 -19.886 1.00 44.43 ? 169 ARG D CA  1 
ATOM   6890 C C   . ARG D 1 169 ? 38.335  -16.674 -21.364 1.00 46.59 ? 169 ARG D C   1 
ATOM   6891 O O   . ARG D 1 169 ? 37.691  -15.683 -21.655 1.00 44.85 ? 169 ARG D O   1 
ATOM   6892 C CB  . ARG D 1 169 ? 40.082  -16.647 -19.530 1.00 30.00 ? 169 ARG D CB  1 
ATOM   6893 C CG  . ARG D 1 169 ? 40.568  -15.287 -19.991 1.00 30.00 ? 169 ARG D CG  1 
ATOM   6894 C CD  . ARG D 1 169 ? 41.478  -14.534 -19.041 1.00 30.00 ? 169 ARG D CD  1 
ATOM   6895 N NE  . ARG D 1 169 ? 41.691  -13.210 -19.595 1.00 30.00 ? 169 ARG D NE  1 
ATOM   6896 C CZ  . ARG D 1 169 ? 42.423  -12.263 -19.042 1.00 30.00 ? 169 ARG D CZ  1 
ATOM   6897 N NH1 . ARG D 1 169 ? 43.027  -12.473 -17.885 1.00 30.00 ? 169 ARG D NH1 1 
ATOM   6898 N NH2 . ARG D 1 169 ? 42.541  -11.096 -19.647 1.00 30.00 ? 169 ARG D NH2 1 
ATOM   6899 N N   . ASN D 1 170 ? 38.795  -17.558 -22.243 1.00 48.18 ? 170 ASN D N   1 
ATOM   6900 C CA  . ASN D 1 170 ? 38.666  -17.397 -23.712 1.00 47.22 ? 170 ASN D CA  1 
ATOM   6901 C C   . ASN D 1 170 ? 37.270  -17.790 -24.196 1.00 45.89 ? 170 ASN D C   1 
ATOM   6902 O O   . ASN D 1 170 ? 36.829  -17.206 -25.168 1.00 50.26 ? 170 ASN D O   1 
ATOM   6903 C CB  . ASN D 1 170 ? 39.733  -18.210 -24.448 1.00 50.83 ? 170 ASN D CB  1 
ATOM   6904 C CG  . ASN D 1 170 ? 41.084  -17.528 -24.538 1.00 53.12 ? 170 ASN D CG  1 
ATOM   6905 O OD1 . ASN D 1 170 ? 41.650  -17.416 -25.610 1.00 58.39 ? 170 ASN D OD1 1 
ATOM   6906 N ND2 . ASN D 1 170 ? 41.629  -17.091 -23.419 1.00 50.53 ? 170 ASN D ND2 1 
ATOM   6907 N N   . CYS D 1 171 ? 36.596  -18.736 -23.547 1.00 45.31 ? 171 CYS D N   1 
ATOM   6908 C CA  . CYS D 1 171 ? 35.262  -19.146 -24.057 1.00 41.37 ? 171 CYS D CA  1 
ATOM   6909 C C   . CYS D 1 171 ? 34.116  -18.402 -23.369 1.00 41.96 ? 171 CYS D C   1 
ATOM   6910 O O   . CYS D 1 171 ? 32.996  -18.507 -23.861 1.00 41.53 ? 171 CYS D O   1 
ATOM   6911 C CB  . CYS D 1 171 ? 35.063  -20.653 -23.989 1.00 40.15 ? 171 CYS D CB  1 
ATOM   6912 S SG  . CYS D 1 171 ? 35.273  -21.384 -22.350 1.00 48.86 ? 171 CYS D SG  1 
ATOM   6913 N N   . LYS D 1 172 ? 34.383  -17.703 -22.267 1.00 43.05 ? 172 LYS D N   1 
ATOM   6914 C CA  . LYS D 1 172 ? 33.322  -16.943 -21.600 1.00 42.10 ? 172 LYS D CA  1 
ATOM   6915 C C   . LYS D 1 172 ? 33.808  -15.517 -21.343 1.00 39.27 ? 172 LYS D C   1 
ATOM   6916 O O   . LYS D 1 172 ? 33.233  -14.555 -21.867 1.00 43.36 ? 172 LYS D O   1 
ATOM   6917 C CB  . LYS D 1 172 ? 32.917  -17.616 -20.281 1.00 37.96 ? 172 LYS D CB  1 
ATOM   6918 C CG  . LYS D 1 172 ? 31.874  -16.827 -19.467 1.00 41.03 ? 172 LYS D CG  1 
ATOM   6919 C CD  . LYS D 1 172 ? 30.550  -16.702 -20.197 1.00 40.66 ? 172 LYS D CD  1 
ATOM   6920 C CE  . LYS D 1 172 ? 29.566  -15.910 -19.352 1.00 38.58 ? 172 LYS D CE  1 
ATOM   6921 N NZ  . LYS D 1 172 ? 28.869  -14.891 -20.144 1.00 38.92 ? 172 LYS D NZ  1 
ATOM   6922 N N   . GLY D 1 173 ? 34.857  -15.377 -20.546 1.00 39.29 ? 173 GLY D N   1 
ATOM   6923 C CA  . GLY D 1 173 ? 35.480  -14.092 -20.270 1.00 41.14 ? 173 GLY D CA  1 
ATOM   6924 C C   . GLY D 1 173 ? 34.957  -13.261 -19.110 1.00 40.84 ? 173 GLY D C   1 
ATOM   6925 O O   . GLY D 1 173 ? 35.255  -12.061 -19.058 1.00 38.02 ? 173 GLY D O   1 
ATOM   6926 N N   . ASP D 1 174 ? 34.284  -13.866 -18.128 1.00 39.51 ? 174 ASP D N   1 
ATOM   6927 C CA  . ASP D 1 174 ? 33.790  -13.100 -16.988 1.00 36.55 ? 174 ASP D CA  1 
ATOM   6928 C C   . ASP D 1 174 ? 34.933  -12.737 -16.060 1.00 37.81 ? 174 ASP D C   1 
ATOM   6929 O O   . ASP D 1 174 ? 34.905  -11.670 -15.437 1.00 35.59 ? 174 ASP D O   1 
ATOM   6930 C CB  . ASP D 1 174 ? 32.752  -13.908 -16.198 1.00 33.79 ? 174 ASP D CB  1 
ATOM   6931 C CG  . ASP D 1 174 ? 31.344  -13.685 -16.674 1.00 38.04 ? 174 ASP D CG  1 
ATOM   6932 O OD1 . ASP D 1 174 ? 31.116  -12.956 -17.670 1.00 40.16 ? 174 ASP D OD1 1 
ATOM   6933 O OD2 . ASP D 1 174 ? 30.423  -14.262 -16.052 1.00 39.27 ? 174 ASP D OD2 1 
ATOM   6934 N N   . TYR D 1 175 ? 35.963  -13.588 -15.994 1.00 32.17 ? 175 TYR D N   1 
ATOM   6935 C CA  . TYR D 1 175 ? 37.002  -13.464 -14.992 1.00 34.49 ? 175 TYR D CA  1 
ATOM   6936 C C   . TYR D 1 175 ? 38.359  -13.316 -15.675 1.00 37.31 ? 175 TYR D C   1 
ATOM   6937 O O   . TYR D 1 175 ? 38.603  -13.877 -16.750 1.00 37.45 ? 175 TYR D O   1 
ATOM   6938 C CB  . TYR D 1 175 ? 37.014  -14.668 -14.032 1.00 33.63 ? 175 TYR D CB  1 
ATOM   6939 C CG  . TYR D 1 175 ? 35.750  -14.840 -13.201 1.00 35.82 ? 175 TYR D CG  1 
ATOM   6940 C CD1 . TYR D 1 175 ? 34.679  -15.598 -13.662 1.00 32.67 ? 175 TYR D CD1 1 
ATOM   6941 C CD2 . TYR D 1 175 ? 35.622  -14.205 -11.967 1.00 31.56 ? 175 TYR D CD2 1 
ATOM   6942 C CE1 . TYR D 1 175 ? 33.543  -15.727 -12.897 1.00 29.96 ? 175 TYR D CE1 1 
ATOM   6943 C CE2 . TYR D 1 175 ? 34.504  -14.333 -11.214 1.00 30.56 ? 175 TYR D CE2 1 
ATOM   6944 C CZ  . TYR D 1 175 ? 33.460  -15.079 -11.677 1.00 30.83 ? 175 TYR D CZ  1 
ATOM   6945 O OH  . TYR D 1 175 ? 32.339  -15.172 -10.888 1.00 31.22 ? 175 TYR D OH  1 
ATOM   6946 N N   . THR D 1 176 ? 39.236  -12.531 -15.047 1.00 36.91 ? 176 THR D N   1 
ATOM   6947 C CA  . THR D 1 176 ? 40.632  -12.437 -15.457 1.00 37.47 ? 176 THR D CA  1 
ATOM   6948 C C   . THR D 1 176 ? 41.582  -13.065 -14.452 1.00 37.36 ? 176 THR D C   1 
ATOM   6949 O O   . THR D 1 176 ? 42.798  -13.088 -14.694 1.00 38.19 ? 176 THR D O   1 
ATOM   6950 C CB  . THR D 1 176 ? 41.043  -10.973 -15.661 1.00 34.92 ? 176 THR D CB  1 
ATOM   6951 O OG1 . THR D 1 176 ? 40.930  -10.281 -14.409 1.00 33.94 ? 176 THR D OG1 1 
ATOM   6952 C CG2 . THR D 1 176 ? 40.184  -10.296 -16.706 1.00 34.87 ? 176 THR D CG2 1 
ATOM   6953 N N   . GLY D 1 177 ? 41.074  -13.546 -13.325 1.00 36.37 ? 177 GLY D N   1 
ATOM   6954 C CA  . GLY D 1 177 ? 41.897  -14.123 -12.280 1.00 38.34 ? 177 GLY D CA  1 
ATOM   6955 C C   . GLY D 1 177 ? 42.069  -15.629 -12.409 1.00 35.39 ? 177 GLY D C   1 
ATOM   6956 O O   . GLY D 1 177 ? 41.672  -16.253 -13.399 1.00 32.86 ? 177 GLY D O   1 
ATOM   6957 N N   . ASN D 1 178 ? 42.660  -16.212 -11.351 1.00 34.39 ? 178 ASN D N   1 
ATOM   6958 C CA  . ASN D 1 178 ? 43.130  -17.601 -11.294 1.00 37.84 ? 178 ASN D CA  1 
ATOM   6959 C C   . ASN D 1 178 ? 42.637  -18.215 -9.989  1.00 36.08 ? 178 ASN D C   1 
ATOM   6960 O O   . ASN D 1 178 ? 43.248  -18.016 -8.931  1.00 37.11 ? 178 ASN D O   1 
ATOM   6961 C CB  . ASN D 1 178 ? 44.661  -17.698 -11.330 1.00 39.42 ? 178 ASN D CB  1 
ATOM   6962 C CG  . ASN D 1 178 ? 45.206  -17.934 -12.702 1.00 44.76 ? 178 ASN D CG  1 
ATOM   6963 O OD1 . ASN D 1 178 ? 44.466  -18.251 -13.620 1.00 50.34 ? 178 ASN D OD1 1 
ATOM   6964 N ND2 . ASN D 1 178 ? 46.521  -17.795 -12.855 1.00 50.35 ? 178 ASN D ND2 1 
ATOM   6965 N N   . PHE D 1 179 ? 41.517  -18.932 -10.050 1.00 33.39 ? 179 PHE D N   1 
ATOM   6966 C CA  . PHE D 1 179 ? 40.964  -19.567 -8.859  1.00 32.21 ? 179 PHE D CA  1 
ATOM   6967 C C   . PHE D 1 179 ? 39.832  -20.491 -9.285  1.00 28.29 ? 179 PHE D C   1 
ATOM   6968 O O   . PHE D 1 179 ? 39.336  -20.403 -10.411 1.00 29.59 ? 179 PHE D O   1 
ATOM   6969 C CB  . PHE D 1 179 ? 40.469  -18.559 -7.819  1.00 30.95 ? 179 PHE D CB  1 
ATOM   6970 C CG  . PHE D 1 179 ? 39.561  -17.489 -8.382  1.00 29.86 ? 179 PHE D CG  1 
ATOM   6971 C CD1 . PHE D 1 179 ? 38.202  -17.690 -8.479  1.00 30.61 ? 179 PHE D CD1 1 
ATOM   6972 C CD2 . PHE D 1 179 ? 40.083  -16.275 -8.805  1.00 32.80 ? 179 PHE D CD2 1 
ATOM   6973 C CE1 . PHE D 1 179 ? 37.351  -16.703 -8.990  1.00 30.03 ? 179 PHE D CE1 1 
ATOM   6974 C CE2 . PHE D 1 179 ? 39.253  -15.274 -9.320  1.00 33.33 ? 179 PHE D CE2 1 
ATOM   6975 C CZ  . PHE D 1 179 ? 37.881  -15.484 -9.400  1.00 33.92 ? 179 PHE D CZ  1 
ATOM   6976 N N   . GLY D 1 180 ? 39.527  -21.462 -8.412  1.00 28.00 ? 180 GLY D N   1 
ATOM   6977 C CA  . GLY D 1 180 ? 38.365  -22.309 -8.607  1.00 28.25 ? 180 GLY D CA  1 
ATOM   6978 C C   . GLY D 1 180 ? 37.101  -21.613 -8.113  1.00 25.95 ? 180 GLY D C   1 
ATOM   6979 O O   . GLY D 1 180 ? 37.143  -20.755 -7.238  1.00 25.36 ? 180 GLY D O   1 
ATOM   6980 N N   . HIS D 1 181 ? 35.962  -22.017 -8.648  1.00 25.35 ? 181 HIS D N   1 
ATOM   6981 C CA  . HIS D 1 181 ? 34.721  -21.267 -8.406  1.00 27.24 ? 181 HIS D CA  1 
ATOM   6982 C C   . HIS D 1 181 ? 33.517  -22.203 -8.519  1.00 25.06 ? 181 HIS D C   1 
ATOM   6983 O O   . HIS D 1 181 ? 33.598  -23.260 -9.151  1.00 26.31 ? 181 HIS D O   1 
ATOM   6984 C CB  . HIS D 1 181 ? 34.592  -20.094 -9.382  1.00 24.82 ? 181 HIS D CB  1 
ATOM   6985 C CG  . HIS D 1 181 ? 33.566  -19.073 -8.975  1.00 26.91 ? 181 HIS D CG  1 
ATOM   6986 N ND1 . HIS D 1 181 ? 33.450  -18.603 -7.680  1.00 28.20 ? 181 HIS D ND1 1 
ATOM   6987 C CD2 . HIS D 1 181 ? 32.632  -18.412 -9.699  1.00 27.17 ? 181 HIS D CD2 1 
ATOM   6988 C CE1 . HIS D 1 181 ? 32.471  -17.707 -7.622  1.00 28.26 ? 181 HIS D CE1 1 
ATOM   6989 N NE2 . HIS D 1 181 ? 31.958  -17.571 -8.834  1.00 27.21 ? 181 HIS D NE2 1 
ATOM   6990 N N   . TYR D 1 182 ? 32.421  -21.844 -7.829  1.00 23.78 ? 182 TYR D N   1 
ATOM   6991 C CA  . TYR D 1 182 ? 31.166  -22.596 -7.856  1.00 24.70 ? 182 TYR D CA  1 
ATOM   6992 C C   . TYR D 1 182 ? 30.020  -21.686 -8.284  1.00 24.99 ? 182 TYR D C   1 
ATOM   6993 O O   . TYR D 1 182 ? 30.015  -20.493 -7.986  1.00 23.10 ? 182 TYR D O   1 
ATOM   6994 C CB  . TYR D 1 182 ? 30.759  -23.166 -6.474  1.00 23.83 ? 182 TYR D CB  1 
ATOM   6995 C CG  . TYR D 1 182 ? 31.611  -24.298 -5.922  1.00 27.59 ? 182 TYR D CG  1 
ATOM   6996 C CD1 . TYR D 1 182 ? 32.687  -24.039 -5.096  1.00 24.72 ? 182 TYR D CD1 1 
ATOM   6997 C CD2 . TYR D 1 182 ? 31.273  -25.630 -6.164  1.00 26.35 ? 182 TYR D CD2 1 
ATOM   6998 C CE1 . TYR D 1 182 ? 33.449  -25.078 -4.557  1.00 29.16 ? 182 TYR D CE1 1 
ATOM   6999 C CE2 . TYR D 1 182 ? 32.039  -26.676 -5.624  1.00 26.12 ? 182 TYR D CE2 1 
ATOM   7000 C CZ  . TYR D 1 182 ? 33.106  -26.391 -4.827  1.00 26.27 ? 182 TYR D CZ  1 
ATOM   7001 O OH  . TYR D 1 182 ? 33.857  -27.408 -4.287  1.00 29.49 ? 182 TYR D OH  1 
ATOM   7002 N N   . GLY D 1 183 ? 29.046  -22.267 -8.981  1.00 25.76 ? 183 GLY D N   1 
ATOM   7003 C CA  . GLY D 1 183 ? 27.795  -21.594 -9.278  1.00 22.04 ? 183 GLY D CA  1 
ATOM   7004 C C   . GLY D 1 183 ? 26.718  -22.645 -9.371  1.00 24.40 ? 183 GLY D C   1 
ATOM   7005 O O   . GLY D 1 183 ? 26.971  -23.833 -9.131  1.00 23.49 ? 183 GLY D O   1 
ATOM   7006 N N   . LEU D 1 184 ? 25.506  -22.219 -9.748  1.00 23.01 ? 184 LEU D N   1 
ATOM   7007 C CA  . LEU D 1 184 ? 24.355  -23.129 -9.813  1.00 21.71 ? 184 LEU D CA  1 
ATOM   7008 C C   . LEU D 1 184 ? 23.780  -23.132 -11.216 1.00 23.45 ? 184 LEU D C   1 
ATOM   7009 O O   . LEU D 1 184 ? 23.303  -22.091 -11.685 1.00 26.88 ? 184 LEU D O   1 
ATOM   7010 C CB  . LEU D 1 184 ? 23.230  -22.736 -8.835  1.00 19.80 ? 184 LEU D CB  1 
ATOM   7011 C CG  . LEU D 1 184 ? 22.104  -23.792 -8.785  1.00 22.38 ? 184 LEU D CG  1 
ATOM   7012 C CD1 . LEU D 1 184 ? 22.566  -25.053 -7.943  1.00 21.81 ? 184 LEU D CD1 1 
ATOM   7013 C CD2 . LEU D 1 184 ? 20.768  -23.186 -8.245  1.00 25.13 ? 184 LEU D CD2 1 
ATOM   7014 N N   . ILE D 1 185 ? 23.776  -24.304 -11.862 1.00 26.75 ? 185 ILE D N   1 
ATOM   7015 C CA  . ILE D 1 185 ? 23.063  -24.479 -13.124 1.00 26.98 ? 185 ILE D CA  1 
ATOM   7016 C C   . ILE D 1 185 ? 21.594  -24.680 -12.814 1.00 28.59 ? 185 ILE D C   1 
ATOM   7017 O O   . ILE D 1 185 ? 21.220  -25.691 -12.211 1.00 26.00 ? 185 ILE D O   1 
ATOM   7018 C CB  . ILE D 1 185 ? 23.602  -25.663 -13.927 1.00 29.03 ? 185 ILE D CB  1 
ATOM   7019 C CG1 . ILE D 1 185 ? 25.102  -25.516 -14.178 1.00 27.83 ? 185 ILE D CG1 1 
ATOM   7020 C CG2 . ILE D 1 185 ? 22.868  -25.722 -15.267 1.00 29.09 ? 185 ILE D CG2 1 
ATOM   7021 C CD1 . ILE D 1 185 ? 25.769  -26.735 -14.941 1.00 28.86 ? 185 ILE D CD1 1 
ATOM   7022 N N   . TRP D 1 186 ? 20.757  -23.749 -13.262 1.00 26.88 ? 186 TRP D N   1 
ATOM   7023 C CA  . TRP D 1 186 ? 19.323  -23.861 -13.018 1.00 29.87 ? 186 TRP D CA  1 
ATOM   7024 C C   . TRP D 1 186 ? 18.467  -23.928 -14.286 1.00 28.78 ? 186 TRP D C   1 
ATOM   7025 O O   . TRP D 1 186 ? 17.265  -24.150 -14.181 1.00 33.33 ? 186 TRP D O   1 
ATOM   7026 C CB  . TRP D 1 186 ? 18.837  -22.718 -12.109 1.00 27.41 ? 186 TRP D CB  1 
ATOM   7027 C CG  . TRP D 1 186 ? 19.033  -21.353 -12.652 1.00 29.08 ? 186 TRP D CG  1 
ATOM   7028 C CD1 . TRP D 1 186 ? 20.142  -20.571 -12.508 1.00 28.58 ? 186 TRP D CD1 1 
ATOM   7029 C CD2 . TRP D 1 186 ? 18.088  -20.579 -13.412 1.00 28.46 ? 186 TRP D CD2 1 
ATOM   7030 N NE1 . TRP D 1 186 ? 19.943  -19.356 -13.122 1.00 28.96 ? 186 TRP D NE1 1 
ATOM   7031 C CE2 . TRP D 1 186 ? 18.704  -19.342 -13.703 1.00 29.62 ? 186 TRP D CE2 1 
ATOM   7032 C CE3 . TRP D 1 186 ? 16.776  -20.810 -13.863 1.00 31.05 ? 186 TRP D CE3 1 
ATOM   7033 C CZ2 . TRP D 1 186 ? 18.071  -18.345 -14.451 1.00 29.05 ? 186 TRP D CZ2 1 
ATOM   7034 C CZ3 . TRP D 1 186 ? 16.149  -19.829 -14.602 1.00 28.62 ? 186 TRP D CZ3 1 
ATOM   7035 C CH2 . TRP D 1 186 ? 16.788  -18.600 -14.873 1.00 34.31 ? 186 TRP D CH2 1 
ATOM   7036 N N   . ASP D 1 187 ? 19.048  -23.806 -15.470 1.00 31.66 ? 187 ASP D N   1 
ATOM   7037 C CA  . ASP D 1 187 ? 18.309  -23.908 -16.723 1.00 33.54 ? 187 ASP D CA  1 
ATOM   7038 C C   . ASP D 1 187 ? 19.321  -24.172 -17.828 1.00 34.24 ? 187 ASP D C   1 
ATOM   7039 O O   . ASP D 1 187 ? 20.527  -24.017 -17.632 1.00 30.22 ? 187 ASP D O   1 
ATOM   7040 C CB  . ASP D 1 187 ? 17.504  -22.639 -16.985 1.00 32.28 ? 187 ASP D CB  1 
ATOM   7041 C CG  . ASP D 1 187 ? 16.411  -22.819 -18.054 1.00 36.53 ? 187 ASP D CG  1 
ATOM   7042 O OD1 . ASP D 1 187 ? 15.987  -23.947 -18.334 1.00 35.26 ? 187 ASP D OD1 1 
ATOM   7043 O OD2 . ASP D 1 187 ? 15.956  -21.795 -18.592 1.00 41.47 ? 187 ASP D OD2 1 
ATOM   7044 N N   . MET D 1 188 ? 18.831  -24.583 -18.997 1.00 38.39 ? 188 MET D N   1 
ATOM   7045 C CA  . MET D 1 188 ? 19.731  -24.670 -20.141 1.00 38.76 ? 188 MET D CA  1 
ATOM   7046 C C   . MET D 1 188 ? 18.984  -24.300 -21.414 1.00 41.73 ? 188 MET D C   1 
ATOM   7047 O O   . MET D 1 188 ? 17.769  -24.482 -21.511 1.00 38.46 ? 188 MET D O   1 
ATOM   7048 C CB  . MET D 1 188 ? 20.365  -26.060 -20.329 1.00 39.20 ? 188 MET D CB  1 
ATOM   7049 C CG  . MET D 1 188 ? 19.531  -27.228 -19.850 1.00 46.07 ? 188 MET D CG  1 
ATOM   7050 S SD  . MET D 1 188 ? 20.565  -28.658 -19.431 1.00 43.60 ? 188 MET D SD  1 
ATOM   7051 C CE  . MET D 1 188 ? 21.032  -29.106 -21.088 1.00 41.07 ? 188 MET D CE  1 
ATOM   7052 N N   . THR D 1 189 ? 19.724  -23.716 -22.363 1.00 42.37 ? 189 THR D N   1 
ATOM   7053 C CA  . THR D 1 189 ? 19.249  -23.573 -23.733 1.00 44.65 ? 189 THR D CA  1 
ATOM   7054 C C   . THR D 1 189 ? 19.694  -24.798 -24.523 1.00 46.51 ? 189 THR D C   1 
ATOM   7055 O O   . THR D 1 189 ? 20.217  -25.762 -23.960 1.00 47.75 ? 189 THR D O   1 
ATOM   7056 C CB  . THR D 1 189 ? 19.778  -22.295 -24.365 1.00 40.29 ? 189 THR D CB  1 
ATOM   7057 O OG1 . THR D 1 189 ? 21.193  -22.417 -24.556 1.00 43.58 ? 189 THR D OG1 1 
ATOM   7058 C CG2 . THR D 1 189 ? 19.468  -21.089 -23.495 1.00 39.87 ? 189 THR D CG2 1 
ATOM   7059 N N   . SER D 1 190 ? 19.527  -24.772 -25.844 1.00 46.03 ? 190 SER D N   1 
ATOM   7060 C CA  . SER D 1 190 ? 19.980  -25.903 -26.643 1.00 47.28 ? 190 SER D CA  1 
ATOM   7061 C C   . SER D 1 190 ? 21.501  -26.007 -26.649 1.00 49.61 ? 190 SER D C   1 
ATOM   7062 O O   . SER D 1 190 ? 22.062  -27.081 -26.937 1.00 47.04 ? 190 SER D O   1 
ATOM   7063 C CB  . SER D 1 190 ? 19.432  -25.768 -28.067 1.00 49.31 ? 190 SER D CB  1 
ATOM   7064 O OG  . SER D 1 190 ? 19.942  -24.600 -28.700 1.00 50.12 ? 190 SER D OG  1 
ATOM   7065 N N   . THR D 1 191 ? 22.176  -24.916 -26.320 1.00 46.80 ? 191 THR D N   1 
ATOM   7066 C CA  . THR D 1 191 ? 23.622  -24.837 -26.442 1.00 45.94 ? 191 THR D CA  1 
ATOM   7067 C C   . THR D 1 191 ? 24.331  -24.390 -25.174 1.00 42.58 ? 191 THR D C   1 
ATOM   7068 O O   . THR D 1 191 ? 25.530  -24.639 -25.055 1.00 41.06 ? 191 THR D O   1 
ATOM   7069 C CB  . THR D 1 191 ? 23.987  -23.873 -27.576 1.00 48.33 ? 191 THR D CB  1 
ATOM   7070 O OG1 . THR D 1 191 ? 23.415  -22.590 -27.279 1.00 47.72 ? 191 THR D OG1 1 
ATOM   7071 C CG2 . THR D 1 191 ? 23.410  -24.385 -28.908 1.00 47.58 ? 191 THR D CG2 1 
ATOM   7072 N N   . HIS D 1 192 ? 23.642  -23.742 -24.227 1.00 45.18 ? 192 HIS D N   1 
ATOM   7073 C CA  . HIS D 1 192 ? 24.302  -23.108 -23.091 1.00 41.71 ? 192 HIS D CA  1 
ATOM   7074 C C   . HIS D 1 192 ? 23.725  -23.581 -21.769 1.00 37.67 ? 192 HIS D C   1 
ATOM   7075 O O   . HIS D 1 192 ? 22.518  -23.769 -21.638 1.00 37.22 ? 192 HIS D O   1 
ATOM   7076 C CB  . HIS D 1 192 ? 24.158  -21.579 -23.150 1.00 43.15 ? 192 HIS D CB  1 
ATOM   7077 C CG  . HIS D 1 192 ? 25.073  -20.918 -24.128 1.00 42.72 ? 192 HIS D CG  1 
ATOM   7078 N ND1 . HIS D 1 192 ? 24.887  -20.992 -25.493 1.00 43.40 ? 192 HIS D ND1 1 
ATOM   7079 C CD2 . HIS D 1 192 ? 26.195  -20.181 -23.936 1.00 44.33 ? 192 HIS D CD2 1 
ATOM   7080 C CE1 . HIS D 1 192 ? 25.854  -20.318 -26.099 1.00 47.14 ? 192 HIS D CE1 1 
ATOM   7081 N NE2 . HIS D 1 192 ? 26.650  -19.804 -25.176 1.00 45.84 ? 192 HIS D NE2 1 
ATOM   7082 N N   . TYR D 1 193 ? 24.602  -23.726 -20.779 1.00 36.35 ? 193 TYR D N   1 
ATOM   7083 C CA  . TYR D 1 193 ? 24.171  -23.768 -19.397 1.00 33.99 ? 193 TYR D CA  1 
ATOM   7084 C C   . TYR D 1 193 ? 23.853  -22.340 -18.952 1.00 33.18 ? 193 TYR D C   1 
ATOM   7085 O O   . TYR D 1 193 ? 24.548  -21.397 -19.336 1.00 34.79 ? 193 TYR D O   1 
ATOM   7086 C CB  . TYR D 1 193 ? 25.257  -24.346 -18.503 1.00 29.51 ? 193 TYR D CB  1 
ATOM   7087 C CG  . TYR D 1 193 ? 25.739  -25.750 -18.814 1.00 33.86 ? 193 TYR D CG  1 
ATOM   7088 C CD1 . TYR D 1 193 ? 24.862  -26.843 -18.824 1.00 35.56 ? 193 TYR D CD1 1 
ATOM   7089 C CD2 . TYR D 1 193 ? 27.101  -25.991 -19.052 1.00 34.78 ? 193 TYR D CD2 1 
ATOM   7090 C CE1 . TYR D 1 193 ? 25.324  -28.138 -19.078 1.00 30.13 ? 193 TYR D CE1 1 
ATOM   7091 C CE2 . TYR D 1 193 ? 27.581  -27.279 -19.300 1.00 33.09 ? 193 TYR D CE2 1 
ATOM   7092 C CZ  . TYR D 1 193 ? 26.688  -28.348 -19.312 1.00 35.69 ? 193 TYR D CZ  1 
ATOM   7093 O OH  . TYR D 1 193 ? 27.171  -29.627 -19.566 1.00 35.45 ? 193 TYR D OH  1 
ATOM   7094 N N   . VAL D 1 194 ? 22.781  -22.183 -18.192 1.00 31.22 ? 194 VAL D N   1 
ATOM   7095 C CA  . VAL D 1 194 ? 22.454  -20.924 -17.533 1.00 31.66 ? 194 VAL D CA  1 
ATOM   7096 C C   . VAL D 1 194 ? 22.911  -21.037 -16.090 1.00 32.32 ? 194 VAL D C   1 
ATOM   7097 O O   . VAL D 1 194 ? 22.332  -21.817 -15.317 1.00 33.28 ? 194 VAL D O   1 
ATOM   7098 C CB  . VAL D 1 194 ? 20.955  -20.604 -17.574 1.00 32.65 ? 194 VAL D CB  1 
ATOM   7099 C CG1 . VAL D 1 194 ? 20.754  -19.173 -16.973 1.00 31.84 ? 194 VAL D CG1 1 
ATOM   7100 C CG2 . VAL D 1 194 ? 20.351  -20.710 -18.989 1.00 32.16 ? 194 VAL D CG2 1 
ATOM   7101 N N   . VAL D 1 195 ? 23.899  -20.232 -15.700 1.00 30.08 ? 195 VAL D N   1 
ATOM   7102 C CA  . VAL D 1 195 ? 24.528  -20.341 -14.391 1.00 28.56 ? 195 VAL D CA  1 
ATOM   7103 C C   . VAL D 1 195 ? 24.183  -19.116 -13.537 1.00 30.01 ? 195 VAL D C   1 
ATOM   7104 O O   . VAL D 1 195 ? 24.449  -17.961 -13.925 1.00 27.39 ? 195 VAL D O   1 
ATOM   7105 C CB  . VAL D 1 195 ? 26.048  -20.500 -14.525 1.00 30.67 ? 195 VAL D CB  1 
ATOM   7106 C CG1 . VAL D 1 195 ? 26.702  -20.504 -13.170 1.00 28.08 ? 195 VAL D CG1 1 
ATOM   7107 C CG2 . VAL D 1 195 ? 26.412  -21.786 -15.335 1.00 26.94 ? 195 VAL D CG2 1 
ATOM   7108 N N   . ALA D 1 196 ? 23.682  -19.379 -12.335 1.00 24.98 ? 196 ALA D N   1 
ATOM   7109 C CA  . ALA D 1 196 ? 23.622  -18.350 -11.304 1.00 26.85 ? 196 ALA D CA  1 
ATOM   7110 C C   . ALA D 1 196 ? 24.991  -18.330 -10.649 1.00 25.86 ? 196 ALA D C   1 
ATOM   7111 O O   . ALA D 1 196 ? 25.327  -19.235 -9.882  1.00 24.62 ? 196 ALA D O   1 
ATOM   7112 C CB  . ALA D 1 196 ? 22.532  -18.654 -10.293 1.00 26.27 ? 196 ALA D CB  1 
ATOM   7113 N N   . ASP D 1 197 ? 25.790  -17.313 -10.968 1.00 22.20 ? 197 ASP D N   1 
ATOM   7114 C CA  . ASP D 1 197 ? 27.134  -17.162 -10.435 1.00 25.71 ? 197 ASP D CA  1 
ATOM   7115 C C   . ASP D 1 197 ? 27.135  -16.186 -9.254  1.00 21.99 ? 197 ASP D C   1 
ATOM   7116 O O   . ASP D 1 197 ? 26.951  -14.988 -9.467  1.00 24.40 ? 197 ASP D O   1 
ATOM   7117 C CB  . ASP D 1 197 ? 28.067  -16.683 -11.557 1.00 25.80 ? 197 ASP D CB  1 
ATOM   7118 C CG  . ASP D 1 197 ? 29.537  -16.558 -11.122 1.00 27.46 ? 197 ASP D CG  1 
ATOM   7119 O OD1 . ASP D 1 197 ? 29.795  -16.420 -9.904  1.00 23.41 ? 197 ASP D OD1 1 
ATOM   7120 O OD2 . ASP D 1 197 ? 30.434  -16.562 -12.018 1.00 28.21 ? 197 ASP D OD2 1 
ATOM   7121 N N   . PRO D 1 198 ? 27.405  -16.643 -8.017  1.00 23.64 ? 198 PRO D N   1 
ATOM   7122 C CA  . PRO D 1 198 ? 27.297  -15.763 -6.830  1.00 23.64 ? 198 PRO D CA  1 
ATOM   7123 C C   . PRO D 1 198 ? 28.252  -14.587 -6.797  1.00 25.20 ? 198 PRO D C   1 
ATOM   7124 O O   . PRO D 1 198 ? 28.122  -13.745 -5.891  1.00 23.60 ? 198 PRO D O   1 
ATOM   7125 C CB  . PRO D 1 198 ? 27.617  -16.700 -5.649  1.00 26.06 ? 198 PRO D CB  1 
ATOM   7126 C CG  . PRO D 1 198 ? 27.593  -18.085 -6.201  1.00 27.97 ? 198 PRO D CG  1 
ATOM   7127 C CD  . PRO D 1 198 ? 27.944  -17.971 -7.671  1.00 24.95 ? 198 PRO D CD  1 
ATOM   7128 N N   . ALA D 1 199 ? 29.207  -14.504 -7.716  1.00 25.45 ? 199 ALA D N   1 
ATOM   7129 C CA  . ALA D 1 199 ? 30.104  -13.361 -7.826  1.00 26.20 ? 199 ALA D CA  1 
ATOM   7130 C C   . ALA D 1 199 ? 29.817  -12.482 -9.045  1.00 28.53 ? 199 ALA D C   1 
ATOM   7131 O O   . ALA D 1 199 ? 30.531  -11.478 -9.240  1.00 26.44 ? 199 ALA D O   1 
ATOM   7132 C CB  . ALA D 1 199 ? 31.573  -13.859 -7.884  1.00 22.14 ? 199 ALA D CB  1 
ATOM   7133 N N   . LYS D 1 200 ? 28.846  -12.848 -9.895  1.00 24.99 ? 200 LYS D N   1 
ATOM   7134 C CA  . LYS D 1 200 ? 28.594  -12.154 -11.167 1.00 26.57 ? 200 LYS D CA  1 
ATOM   7135 C C   . LYS D 1 200 ? 27.099  -11.872 -11.450 1.00 30.20 ? 200 LYS D C   1 
ATOM   7136 O O   . LYS D 1 200 ? 26.733  -10.743 -11.778 1.00 30.88 ? 200 LYS D O   1 
ATOM   7137 C CB  . LYS D 1 200 ? 29.166  -12.975 -12.337 1.00 27.97 ? 200 LYS D CB  1 
ATOM   7138 C CG  . LYS D 1 200 ? 30.713  -12.900 -12.507 1.00 31.39 ? 200 LYS D CG  1 
ATOM   7139 C CD  . LYS D 1 200 ? 31.237  -11.506 -12.924 1.00 30.42 ? 200 LYS D CD  1 
ATOM   7140 C CE  . LYS D 1 200 ? 30.373  -10.913 -14.047 1.00 35.67 ? 200 LYS D CE  1 
ATOM   7141 N NZ  . LYS D 1 200 ? 30.551  -9.435  -14.223 1.00 35.58 ? 200 LYS D NZ  1 
ATOM   7142 N N   . GLY D 1 201 ? 26.221  -12.868 -11.374 1.00 27.61 ? 201 GLY D N   1 
ATOM   7143 C CA  . GLY D 1 201 ? 24.836  -12.619 -11.734 1.00 31.03 ? 201 GLY D CA  1 
ATOM   7144 C C   . GLY D 1 201 ? 24.069  -13.921 -11.917 1.00 28.65 ? 201 GLY D C   1 
ATOM   7145 O O   . GLY D 1 201 ? 24.633  -15.041 -11.916 1.00 26.37 ? 201 GLY D O   1 
ATOM   7146 N N   . VAL D 1 202 ? 22.772  -13.751 -12.149 1.00 25.62 ? 202 VAL D N   1 
ATOM   7147 C CA  . VAL D 1 202 ? 21.851  -14.881 -12.072 1.00 26.39 ? 202 VAL D CA  1 
ATOM   7148 C C   . VAL D 1 202 ? 21.757  -15.694 -13.358 1.00 27.97 ? 202 VAL D C   1 
ATOM   7149 O O   . VAL D 1 202 ? 21.322  -16.845 -13.304 1.00 28.13 ? 202 VAL D O   1 
ATOM   7150 C CB  . VAL D 1 202 ? 20.453  -14.391 -11.633 1.00 25.15 ? 202 VAL D CB  1 
ATOM   7151 C CG1 . VAL D 1 202 ? 19.690  -13.826 -12.789 1.00 27.09 ? 202 VAL D CG1 1 
ATOM   7152 C CG2 . VAL D 1 202 ? 19.642  -15.521 -10.966 1.00 24.70 ? 202 VAL D CG2 1 
ATOM   7153 N N   . ASN D 1 203 ? 22.133  -15.114 -14.495 1.00 33.07 ? 203 ASN D N   1 
ATOM   7154 C CA  . ASN D 1 203 ? 21.968  -15.844 -15.779 1.00 35.45 ? 203 ASN D CA  1 
ATOM   7155 C C   . ASN D 1 203 ? 23.228  -15.787 -16.639 1.00 36.31 ? 203 ASN D C   1 
ATOM   7156 O O   . ASN D 1 203 ? 23.144  -15.333 -17.755 1.00 42.30 ? 203 ASN D O   1 
ATOM   7157 C CB  . ASN D 1 203 ? 20.710  -15.438 -16.552 1.00 36.46 ? 203 ASN D CB  1 
ATOM   7158 C CG  . ASN D 1 203 ? 20.803  -14.090 -17.225 1.00 41.13 ? 203 ASN D CG  1 
ATOM   7159 O OD1 . ASN D 1 203 ? 21.441  -13.194 -16.718 1.00 46.17 ? 203 ASN D OD1 1 
ATOM   7160 N ND2 . ASN D 1 203 ? 20.152  -13.923 -18.357 1.00 43.80 ? 203 ASN D ND2 1 
ATOM   7161 N N   . ARG D 1 204 ? 24.335  -16.300 -16.130 1.00 36.80 ? 204 ARG D N   1 
ATOM   7162 C CA  . ARG D 1 204 ? 25.590  -16.363 -16.911 1.00 37.81 ? 204 ARG D CA  1 
ATOM   7163 C C   . ARG D 1 204 ? 25.514  -17.584 -17.821 1.00 33.42 ? 204 ARG D C   1 
ATOM   7164 O O   . ARG D 1 204 ? 25.553  -18.684 -17.316 1.00 40.25 ? 204 ARG D O   1 
ATOM   7165 C CB  . ARG D 1 204 ? 26.761  -16.482 -15.953 1.00 34.07 ? 204 ARG D CB  1 
ATOM   7166 C CG  . ARG D 1 204 ? 26.756  -15.396 -14.900 1.00 31.66 ? 204 ARG D CG  1 
ATOM   7167 C CD  . ARG D 1 204 ? 27.678  -14.337 -15.427 1.00 38.85 ? 204 ARG D CD  1 
ATOM   7168 N NE  . ARG D 1 204 ? 26.871  -13.214 -15.789 1.00 36.33 ? 204 ARG D NE  1 
ATOM   7169 C CZ  . ARG D 1 204 ? 27.230  -12.249 -16.601 1.00 37.53 ? 204 ARG D CZ  1 
ATOM   7170 N NH1 . ARG D 1 204 ? 28.418  -12.242 -17.160 1.00 37.01 ? 204 ARG D NH1 1 
ATOM   7171 N NH2 . ARG D 1 204 ? 26.390  -11.272 -16.836 1.00 40.96 ? 204 ARG D NH2 1 
ATOM   7172 N N   . LYS D 1 205 ? 25.427  -17.340 -19.123 1.00 48.66 ? 205 LYS D N   1 
ATOM   7173 C CA  . LYS D 1 205 ? 25.260  -18.399 -20.150 1.00 41.16 ? 205 LYS D CA  1 
ATOM   7174 C C   . LYS D 1 205 ? 26.614  -18.955 -20.582 1.00 41.78 ? 205 LYS D C   1 
ATOM   7175 O O   . LYS D 1 205 ? 27.401  -18.218 -21.146 1.00 39.89 ? 205 LYS D O   1 
ATOM   7176 C CB  . LYS D 1 205 ? 24.441  -17.848 -21.316 1.00 47.39 ? 205 LYS D CB  1 
ATOM   7177 C CG  . LYS D 1 205 ? 22.977  -17.564 -21.008 1.00 45.20 ? 205 LYS D CG  1 
ATOM   7178 C CD  . LYS D 1 205 ? 22.319  -16.718 -22.069 1.00 55.31 ? 205 LYS D CD  1 
ATOM   7179 C CE  . LYS D 1 205 ? 21.157  -15.890 -21.568 1.00 52.46 ? 205 LYS D CE  1 
ATOM   7180 N NZ  . LYS D 1 205 ? 19.867  -16.537 -21.873 1.00 56.88 ? 205 LYS D NZ  1 
ATOM   7181 N N   . TYR D 1 206 ? 26.862  -20.222 -20.264 1.00 39.04 ? 206 TYR D N   1 
ATOM   7182 C CA  . TYR D 1 206 ? 28.145  -20.862 -20.631 1.00 39.60 ? 206 TYR D CA  1 
ATOM   7183 C C   . TYR D 1 206 ? 27.891  -21.953 -21.648 1.00 37.88 ? 206 TYR D C   1 
ATOM   7184 O O   . TYR D 1 206 ? 27.098  -22.805 -21.380 1.00 41.29 ? 206 TYR D O   1 
ATOM   7185 C CB  . TYR D 1 206 ? 28.778  -21.601 -19.454 1.00 37.09 ? 206 TYR D CB  1 
ATOM   7186 C CG  . TYR D 1 206 ? 29.590  -20.725 -18.547 1.00 33.44 ? 206 TYR D CG  1 
ATOM   7187 C CD1 . TYR D 1 206 ? 28.970  -19.860 -17.673 1.00 33.78 ? 206 TYR D CD1 1 
ATOM   7188 C CD2 . TYR D 1 206 ? 30.968  -20.735 -18.579 1.00 35.18 ? 206 TYR D CD2 1 
ATOM   7189 C CE1 . TYR D 1 206 ? 29.693  -19.026 -16.854 1.00 29.52 ? 206 TYR D CE1 1 
ATOM   7190 C CE2 . TYR D 1 206 ? 31.707  -19.919 -17.752 1.00 28.35 ? 206 TYR D CE2 1 
ATOM   7191 C CZ  . TYR D 1 206 ? 31.068  -19.053 -16.896 1.00 31.43 ? 206 TYR D CZ  1 
ATOM   7192 O OH  . TYR D 1 206 ? 31.782  -18.247 -16.078 1.00 30.67 ? 206 TYR D OH  1 
ATOM   7193 N N   . LYS D 1 207 ? 28.597  -21.911 -22.769 1.00 42.81 ? 207 LYS D N   1 
ATOM   7194 C CA  . LYS D 1 207 ? 28.521  -22.996 -23.746 1.00 43.60 ? 207 LYS D CA  1 
ATOM   7195 C C   . LYS D 1 207 ? 28.864  -24.316 -23.054 1.00 42.12 ? 207 LYS D C   1 
ATOM   7196 O O   . LYS D 1 207 ? 29.847  -24.395 -22.300 1.00 41.49 ? 207 LYS D O   1 
ATOM   7197 C CB  . LYS D 1 207 ? 29.500  -22.748 -24.898 1.00 45.22 ? 207 LYS D CB  1 
ATOM   7198 C CG  . LYS D 1 207 ? 28.916  -22.017 -26.087 1.00 47.52 ? 207 LYS D CG  1 
ATOM   7199 C CD  . LYS D 1 207 ? 29.536  -22.509 -27.375 1.00 49.25 ? 207 LYS D CD  1 
ATOM   7200 C CE  . LYS D 1 207 ? 30.638  -21.566 -27.807 1.00 51.33 ? 207 LYS D CE  1 
ATOM   7201 N NZ  . LYS D 1 207 ? 30.055  -20.442 -28.640 1.00 52.58 ? 207 LYS D NZ  1 
ATOM   7202 N N   . PHE D 1 208 ? 28.040  -25.341 -23.290 1.00 41.12 ? 208 PHE D N   1 
ATOM   7203 C CA  . PHE D 1 208 ? 28.251  -26.635 -22.655 1.00 41.19 ? 208 PHE D CA  1 
ATOM   7204 C C   . PHE D 1 208 ? 29.734  -26.979 -22.565 1.00 38.35 ? 208 PHE D C   1 
ATOM   7205 O O   . PHE D 1 208 ? 30.287  -27.170 -21.478 1.00 38.01 ? 208 PHE D O   1 
ATOM   7206 C CB  . PHE D 1 208 ? 27.525  -27.736 -23.439 1.00 40.87 ? 208 PHE D CB  1 
ATOM   7207 C CG  . PHE D 1 208 ? 26.049  -27.566 -23.512 1.00 42.04 ? 208 PHE D CG  1 
ATOM   7208 C CD1 . PHE D 1 208 ? 25.328  -27.025 -22.445 1.00 40.29 ? 208 PHE D CD1 1 
ATOM   7209 C CD2 . PHE D 1 208 ? 25.355  -28.002 -24.633 1.00 42.72 ? 208 PHE D CD2 1 
ATOM   7210 C CE1 . PHE D 1 208 ? 23.961  -26.903 -22.507 1.00 39.59 ? 208 PHE D CE1 1 
ATOM   7211 C CE2 . PHE D 1 208 ? 23.982  -27.880 -24.701 1.00 44.23 ? 208 PHE D CE2 1 
ATOM   7212 C CZ  . PHE D 1 208 ? 23.276  -27.323 -23.635 1.00 44.17 ? 208 PHE D CZ  1 
ATOM   7213 N N   . SER D 1 209 ? 30.408  -27.000 -23.709 1.00 40.52 ? 209 SER D N   1 
ATOM   7214 C CA  . SER D 1 209 ? 31.815  -27.387 -23.734 1.00 40.17 ? 209 SER D CA  1 
ATOM   7215 C C   . SER D 1 209 ? 32.693  -26.420 -22.948 1.00 41.13 ? 209 SER D C   1 
ATOM   7216 O O   . SER D 1 209 ? 33.681  -26.839 -22.318 1.00 41.62 ? 209 SER D O   1 
ATOM   7217 C CB  . SER D 1 209 ? 32.273  -27.481 -25.182 1.00 40.12 ? 209 SER D CB  1 
ATOM   7218 O OG  . SER D 1 209 ? 33.620  -27.101 -25.296 1.00 48.03 ? 209 SER D OG  1 
ATOM   7219 N N   . CYS D 1 210 ? 32.333  -25.138 -22.938 1.00 39.33 ? 210 CYS D N   1 
ATOM   7220 C CA  . CYS D 1 210 ? 33.127  -24.153 -22.212 1.00 36.14 ? 210 CYS D CA  1 
ATOM   7221 C C   . CYS D 1 210 ? 33.208  -24.498 -20.720 1.00 33.66 ? 210 CYS D C   1 
ATOM   7222 O O   . CYS D 1 210 ? 34.292  -24.501 -20.132 1.00 35.14 ? 210 CYS D O   1 
ATOM   7223 C CB  . CYS D 1 210 ? 32.533  -22.764 -22.450 1.00 37.15 ? 210 CYS D CB  1 
ATOM   7224 S SG  . CYS D 1 210 ? 33.366  -21.411 -21.592 1.00 40.78 ? 210 CYS D SG  1 
ATOM   7225 N N   . LEU D 1 211 ? 32.059  -24.808 -20.094 1.00 35.54 ? 211 LEU D N   1 
ATOM   7226 C CA  . LEU D 1 211 ? 32.012  -25.167 -18.672 1.00 33.42 ? 211 LEU D CA  1 
ATOM   7227 C C   . LEU D 1 211 ? 32.552  -26.567 -18.436 1.00 32.78 ? 211 LEU D C   1 
ATOM   7228 O O   . LEU D 1 211 ? 33.295  -26.799 -17.468 1.00 30.08 ? 211 LEU D O   1 
ATOM   7229 C CB  . LEU D 1 211 ? 30.563  -25.078 -18.148 1.00 33.32 ? 211 LEU D CB  1 
ATOM   7230 C CG  . LEU D 1 211 ? 30.434  -25.028 -16.623 1.00 33.56 ? 211 LEU D CG  1 
ATOM   7231 C CD1 . LEU D 1 211 ? 31.165  -23.755 -16.044 1.00 30.66 ? 211 LEU D CD1 1 
ATOM   7232 C CD2 . LEU D 1 211 ? 28.965  -25.038 -16.206 1.00 28.65 ? 211 LEU D CD2 1 
ATOM   7233 N N   . ASP D 1 212 ? 32.181  -27.510 -19.317 1.00 34.58 ? 212 ASP D N   1 
ATOM   7234 C CA  . ASP D 1 212 ? 32.561  -28.920 -19.161 1.00 32.23 ? 212 ASP D CA  1 
ATOM   7235 C C   . ASP D 1 212 ? 34.068  -29.078 -19.006 1.00 34.93 ? 212 ASP D C   1 
ATOM   7236 O O   . ASP D 1 212 ? 34.545  -29.790 -18.113 1.00 34.87 ? 212 ASP D O   1 
ATOM   7237 C CB  . ASP D 1 212 ? 32.102  -29.722 -20.385 1.00 34.64 ? 212 ASP D CB  1 
ATOM   7238 C CG  . ASP D 1 212 ? 30.598  -29.875 -20.462 1.00 32.81 ? 212 ASP D CG  1 
ATOM   7239 O OD1 . ASP D 1 212 ? 29.906  -29.689 -19.442 1.00 33.20 ? 212 ASP D OD1 1 
ATOM   7240 O OD2 . ASP D 1 212 ? 30.099  -30.159 -21.565 1.00 34.18 ? 212 ASP D OD2 1 
ATOM   7241 N N   . ASN D 1 213 ? 34.834  -28.398 -19.853 1.00 32.79 ? 213 ASN D N   1 
ATOM   7242 C CA  . ASN D 1 213 ? 36.273  -28.625 -19.954 1.00 39.93 ? 213 ASN D CA  1 
ATOM   7243 C C   . ASN D 1 213 ? 37.084  -27.639 -19.128 1.00 36.88 ? 213 ASN D C   1 
ATOM   7244 O O   . ASN D 1 213 ? 38.316  -27.705 -19.143 1.00 36.83 ? 213 ASN D O   1 
ATOM   7245 C CB  . ASN D 1 213 ? 36.715  -28.555 -21.433 1.00 38.55 ? 213 ASN D CB  1 
ATOM   7246 C CG  . ASN D 1 213 ? 35.914  -29.506 -22.339 1.00 44.56 ? 213 ASN D CG  1 
ATOM   7247 O OD1 . ASN D 1 213 ? 35.470  -29.107 -23.425 1.00 47.40 ? 213 ASN D OD1 1 
ATOM   7248 N ND2 . ASN D 1 213 ? 35.693  -30.746 -21.883 1.00 41.27 ? 213 ASN D ND2 1 
ATOM   7249 N N   . ALA D 1 214 ? 36.428  -26.748 -18.392 1.00 34.02 ? 214 ALA D N   1 
ATOM   7250 C CA  . ALA D 1 214 ? 37.114  -25.746 -17.590 1.00 34.13 ? 214 ALA D CA  1 
ATOM   7251 C C   . ALA D 1 214 ? 37.571  -26.252 -16.222 1.00 32.06 ? 214 ALA D C   1 
ATOM   7252 O O   . ALA D 1 214 ? 37.939  -25.431 -15.377 1.00 32.09 ? 214 ALA D O   1 
ATOM   7253 C CB  . ALA D 1 214 ? 36.216  -24.509 -17.423 1.00 33.81 ? 214 ALA D CB  1 
ATOM   7254 N N   . ASN D 1 215 ? 37.559  -27.559 -15.958 1.00 31.64 ? 215 ASN D N   1 
ATOM   7255 C CA  . ASN D 1 215 ? 38.044  -28.050 -14.671 1.00 31.97 ? 215 ASN D CA  1 
ATOM   7256 C C   . ASN D 1 215 ? 39.192  -29.053 -14.841 1.00 32.90 ? 215 ASN D C   1 
ATOM   7257 O O   . ASN D 1 215 ? 39.382  -29.946 -14.014 1.00 31.65 ? 215 ASN D O   1 
ATOM   7258 C CB  . ASN D 1 215 ? 36.892  -28.634 -13.850 1.00 30.84 ? 215 ASN D CB  1 
ATOM   7259 C CG  . ASN D 1 215 ? 37.028  -28.307 -12.382 1.00 31.22 ? 215 ASN D CG  1 
ATOM   7260 O OD1 . ASN D 1 215 ? 37.680  -27.294 -11.996 1.00 30.49 ? 215 ASN D OD1 1 
ATOM   7261 N ND2 . ASN D 1 215 ? 36.448  -29.148 -11.543 1.00 28.54 ? 215 ASN D ND2 1 
ATOM   7262 N N   . LYS D 1 216 ? 40.045  -28.833 -15.840 1.00 34.02 ? 216 LYS D N   1 
ATOM   7263 C CA  . LYS D 1 216 ? 41.151  -29.761 -16.056 1.00 34.17 ? 216 LYS D CA  1 
ATOM   7264 C C   . LYS D 1 216 ? 42.071  -29.722 -14.860 1.00 31.25 ? 216 LYS D C   1 
ATOM   7265 O O   . LYS D 1 216 ? 42.364  -28.655 -14.309 1.00 34.94 ? 216 LYS D O   1 
ATOM   7266 C CB  . LYS D 1 216 ? 41.920  -29.367 -17.302 1.00 34.25 ? 216 LYS D CB  1 
ATOM   7267 C CG  . LYS D 1 216 ? 41.044  -29.009 -18.475 1.00 39.54 ? 216 LYS D CG  1 
ATOM   7268 C CD  . LYS D 1 216 ? 41.832  -28.270 -19.577 1.00 40.98 ? 216 LYS D CD  1 
ATOM   7269 C CE  . LYS D 1 216 ? 41.160  -26.904 -19.930 1.00 39.61 ? 216 LYS D CE  1 
ATOM   7270 N NZ  . LYS D 1 216 ? 42.216  -25.869 -20.202 1.00 46.60 ? 216 LYS D NZ  1 
ATOM   7271 N N   . GLY D 1 217 ? 42.506  -30.886 -14.440 1.00 31.51 ? 217 GLY D N   1 
ATOM   7272 C CA  . GLY D 1 217 ? 43.300  -30.990 -13.239 1.00 33.75 ? 217 GLY D CA  1 
ATOM   7273 C C   . GLY D 1 217 ? 42.528  -31.066 -11.956 1.00 30.30 ? 217 GLY D C   1 
ATOM   7274 O O   . GLY D 1 217 ? 43.144  -31.140 -10.885 1.00 32.46 ? 217 GLY D O   1 
ATOM   7275 N N   . TYR D 1 218 ? 41.200  -31.069 -12.021 1.00 31.63 ? 218 TYR D N   1 
ATOM   7276 C CA  . TYR D 1 218 ? 40.369  -31.084 -10.838 1.00 31.08 ? 218 TYR D CA  1 
ATOM   7277 C C   . TYR D 1 218 ? 39.220  -32.054 -11.071 1.00 30.41 ? 218 TYR D C   1 
ATOM   7278 O O   . TYR D 1 218 ? 39.057  -32.605 -12.164 1.00 31.07 ? 218 TYR D O   1 
ATOM   7279 C CB  . TYR D 1 218 ? 39.879  -29.669 -10.504 1.00 31.14 ? 218 TYR D CB  1 
ATOM   7280 C CG  . TYR D 1 218 ? 41.024  -28.682 -10.257 1.00 33.54 ? 218 TYR D CG  1 
ATOM   7281 C CD1 . TYR D 1 218 ? 41.628  -27.999 -11.298 1.00 31.95 ? 218 TYR D CD1 1 
ATOM   7282 C CD2 . TYR D 1 218 ? 41.499  -28.452 -8.975  1.00 35.16 ? 218 TYR D CD2 1 
ATOM   7283 C CE1 . TYR D 1 218 ? 42.683  -27.130 -11.068 1.00 31.70 ? 218 TYR D CE1 1 
ATOM   7284 C CE2 . TYR D 1 218 ? 42.547  -27.572 -8.744  1.00 34.47 ? 218 TYR D CE2 1 
ATOM   7285 C CZ  . TYR D 1 218 ? 43.121  -26.923 -9.788  1.00 33.37 ? 218 TYR D CZ  1 
ATOM   7286 O OH  . TYR D 1 218 ? 44.151  -26.042 -9.533  1.00 41.01 ? 218 TYR D OH  1 
ATOM   7287 N N   . ARG D 1 219 ? 38.427  -32.268 -10.021 1.00 27.39 ? 219 ARG D N   1 
ATOM   7288 C CA  . ARG D 1 219 ? 37.410  -33.321 -10.032 1.00 28.35 ? 219 ARG D CA  1 
ATOM   7289 C C   . ARG D 1 219 ? 36.425  -33.168 -11.181 1.00 29.98 ? 219 ARG D C   1 
ATOM   7290 O O   . ARG D 1 219 ? 35.818  -32.096 -11.371 1.00 29.15 ? 219 ARG D O   1 
ATOM   7291 C CB  . ARG D 1 219 ? 36.652  -33.335 -8.713  1.00 26.13 ? 219 ARG D CB  1 
ATOM   7292 C CG  . ARG D 1 219 ? 35.668  -34.475 -8.626  1.00 26.96 ? 219 ARG D CG  1 
ATOM   7293 C CD  . ARG D 1 219 ? 35.242  -34.691 -7.191  1.00 28.07 ? 219 ARG D CD  1 
ATOM   7294 N NE  . ARG D 1 219 ? 34.154  -35.657 -7.118  1.00 26.70 ? 219 ARG D NE  1 
ATOM   7295 C CZ  . ARG D 1 219 ? 33.694  -36.162 -5.988  1.00 26.65 ? 219 ARG D CZ  1 
ATOM   7296 N NH1 . ARG D 1 219 ? 34.193  -35.801 -4.817  1.00 27.05 ? 219 ARG D NH1 1 
ATOM   7297 N NH2 . ARG D 1 219 ? 32.693  -37.028 -6.031  1.00 31.29 ? 219 ARG D NH2 1 
ATOM   7298 N N   . GLN D 1 220 ? 36.200  -34.272 -11.896 1.00 26.15 ? 220 GLN D N   1 
ATOM   7299 C CA  . GLN D 1 220 ? 35.412  -34.241 -13.124 1.00 28.07 ? 220 GLN D CA  1 
ATOM   7300 C C   . GLN D 1 220 ? 33.959  -34.626 -12.851 1.00 30.99 ? 220 GLN D C   1 
ATOM   7301 O O   . GLN D 1 220 ? 33.473  -35.681 -13.280 1.00 30.97 ? 220 GLN D O   1 
ATOM   7302 C CB  . GLN D 1 220 ? 36.060  -35.128 -14.180 1.00 32.39 ? 220 GLN D CB  1 
ATOM   7303 C CG  . GLN D 1 220 ? 37.428  -34.624 -14.592 1.00 25.40 ? 220 GLN D CG  1 
ATOM   7304 C CD  . GLN D 1 220 ? 37.342  -33.383 -15.449 1.00 30.19 ? 220 GLN D CD  1 
ATOM   7305 O OE1 . GLN D 1 220 ? 36.795  -33.401 -16.550 1.00 32.12 ? 220 GLN D OE1 1 
ATOM   7306 N NE2 . GLN D 1 220 ? 37.857  -32.293 -14.935 1.00 30.84 ? 220 GLN D NE2 1 
ATOM   7307 N N   . ASN D 1 221 ? 33.259  -33.730 -12.135 1.00 26.70 ? 221 ASN D N   1 
ATOM   7308 C CA  . ASN D 1 221 ? 31.826  -33.903 -11.849 1.00 27.56 ? 221 ASN D CA  1 
ATOM   7309 C C   . ASN D 1 221 ? 31.102  -32.556 -11.828 1.00 26.32 ? 221 ASN D C   1 
ATOM   7310 O O   . ASN D 1 221 ? 31.725  -31.493 -11.772 1.00 25.57 ? 221 ASN D O   1 
ATOM   7311 C CB  . ASN D 1 221 ? 31.570  -34.567 -10.497 1.00 27.91 ? 221 ASN D CB  1 
ATOM   7312 C CG  . ASN D 1 221 ? 32.015  -36.022 -10.468 1.00 28.29 ? 221 ASN D CG  1 
ATOM   7313 O OD1 . ASN D 1 221 ? 32.911  -36.358 -9.697  1.00 28.16 ? 221 ASN D OD1 1 
ATOM   7314 N ND2 . ASN D 1 221 ? 31.385  -36.879 -11.286 1.00 27.04 ? 221 ASN D ND2 1 
ATOM   7315 N N   . TYR D 1 222 ? 29.774  -32.619 -11.921 1.00 28.72 ? 222 TYR D N   1 
ATOM   7316 C CA  . TYR D 1 222 ? 28.886  -31.577 -11.417 1.00 25.13 ? 222 TYR D CA  1 
ATOM   7317 C C   . TYR D 1 222 ? 28.135  -32.206 -10.257 1.00 31.92 ? 222 TYR D C   1 
ATOM   7318 O O   . TYR D 1 222 ? 28.247  -33.414 -10.008 1.00 27.18 ? 222 TYR D O   1 
ATOM   7319 C CB  . TYR D 1 222 ? 27.901  -31.065 -12.470 1.00 23.37 ? 222 TYR D CB  1 
ATOM   7320 C CG  . TYR D 1 222 ? 28.472  -30.347 -13.628 1.00 25.93 ? 222 TYR D CG  1 
ATOM   7321 C CD1 . TYR D 1 222 ? 29.584  -29.521 -13.485 1.00 27.79 ? 222 TYR D CD1 1 
ATOM   7322 C CD2 . TYR D 1 222 ? 27.953  -30.539 -14.908 1.00 29.30 ? 222 TYR D CD2 1 
ATOM   7323 C CE1 . TYR D 1 222 ? 30.140  -28.880 -14.569 1.00 26.90 ? 222 TYR D CE1 1 
ATOM   7324 C CE2 . TYR D 1 222 ? 28.495  -29.882 -16.010 1.00 29.12 ? 222 TYR D CE2 1 
ATOM   7325 C CZ  . TYR D 1 222 ? 29.574  -29.057 -15.834 1.00 30.10 ? 222 TYR D CZ  1 
ATOM   7326 O OH  . TYR D 1 222 ? 30.106  -28.423 -16.928 1.00 30.56 ? 222 TYR D OH  1 
ATOM   7327 N N   . TYR D 1 223 ? 27.350  -31.395 -9.548  1.00 23.96 ? 223 TYR D N   1 
ATOM   7328 C CA  . TYR D 1 223 ? 26.792  -31.837 -8.274  1.00 25.00 ? 223 TYR D CA  1 
ATOM   7329 C C   . TYR D 1 223 ? 25.292  -31.548 -8.222  1.00 25.80 ? 223 TYR D C   1 
ATOM   7330 O O   . TYR D 1 223 ? 24.878  -30.411 -7.959  1.00 23.27 ? 223 TYR D O   1 
ATOM   7331 C CB  . TYR D 1 223 ? 27.578  -31.193 -7.139  1.00 22.28 ? 223 TYR D CB  1 
ATOM   7332 C CG  . TYR D 1 223 ? 29.065  -31.479 -7.326  1.00 23.74 ? 223 TYR D CG  1 
ATOM   7333 C CD1 . TYR D 1 223 ? 29.596  -32.744 -7.011  1.00 25.92 ? 223 TYR D CD1 1 
ATOM   7334 C CD2 . TYR D 1 223 ? 29.931  -30.512 -7.868  1.00 25.10 ? 223 TYR D CD2 1 
ATOM   7335 C CE1 . TYR D 1 223 ? 30.971  -33.019 -7.205  1.00 25.14 ? 223 TYR D CE1 1 
ATOM   7336 C CE2 . TYR D 1 223 ? 31.280  -30.771 -8.063  1.00 25.64 ? 223 TYR D CE2 1 
ATOM   7337 C CZ  . TYR D 1 223 ? 31.809  -32.033 -7.748  1.00 23.36 ? 223 TYR D CZ  1 
ATOM   7338 O OH  . TYR D 1 223 ? 33.184  -32.302 -7.955  1.00 25.69 ? 223 TYR D OH  1 
ATOM   7339 N N   . VAL D 1 224 ? 24.481  -32.585 -8.497  1.00 23.96 ? 224 VAL D N   1 
ATOM   7340 C CA  . VAL D 1 224 ? 23.027  -32.452 -8.443  1.00 22.62 ? 224 VAL D CA  1 
ATOM   7341 C C   . VAL D 1 224 ? 22.602  -32.285 -7.000  1.00 23.27 ? 224 VAL D C   1 
ATOM   7342 O O   . VAL D 1 224 ? 23.041  -33.039 -6.131  1.00 27.04 ? 224 VAL D O   1 
ATOM   7343 C CB  . VAL D 1 224 ? 22.336  -33.683 -9.063  1.00 26.39 ? 224 VAL D CB  1 
ATOM   7344 C CG1 . VAL D 1 224 ? 20.789  -33.543 -8.969  1.00 27.05 ? 224 VAL D CG1 1 
ATOM   7345 C CG2 . VAL D 1 224 ? 22.762  -33.878 -10.503 1.00 28.67 ? 224 VAL D CG2 1 
ATOM   7346 N N   . VAL D 1 225 ? 21.706  -31.328 -6.737  1.00 24.87 ? 225 VAL D N   1 
ATOM   7347 C CA  . VAL D 1 225 ? 21.160  -31.094 -5.403  1.00 25.17 ? 225 VAL D CA  1 
ATOM   7348 C C   . VAL D 1 225 ? 19.733  -31.586 -5.389  1.00 24.81 ? 225 VAL D C   1 
ATOM   7349 O O   . VAL D 1 225 ? 18.917  -31.155 -6.213  1.00 24.27 ? 225 VAL D O   1 
ATOM   7350 C CB  . VAL D 1 225 ? 21.230  -29.611 -5.009  1.00 23.44 ? 225 VAL D CB  1 
ATOM   7351 C CG1 . VAL D 1 225 ? 20.740  -29.414 -3.583  1.00 25.15 ? 225 VAL D CG1 1 
ATOM   7352 C CG2 . VAL D 1 225 ? 22.725  -29.077 -5.176  1.00 16.11 ? 225 VAL D CG2 1 
ATOM   7353 N N   . CYS D 1 226 ? 19.429  -32.505 -4.467  1.00 28.84 ? 226 CYS D N   1 
ATOM   7354 C CA  . CYS D 1 226 ? 18.061  -33.010 -4.401  1.00 29.08 ? 226 CYS D CA  1 
ATOM   7355 C C   . CYS D 1 226 ? 17.712  -33.274 -2.945  1.00 29.44 ? 226 CYS D C   1 
ATOM   7356 O O   . CYS D 1 226 ? 18.605  -33.204 -2.078  1.00 31.77 ? 226 CYS D O   1 
ATOM   7357 C CB  . CYS D 1 226 ? 17.922  -34.264 -5.259  1.00 32.13 ? 226 CYS D CB  1 
ATOM   7358 S SG  . CYS D 1 226 ? 18.894  -35.675 -4.734  1.00 36.33 ? 226 CYS D SG  1 
ATOM   7359 N N   . PRO D 1 227 ? 16.439  -33.542 -2.617  1.00 28.63 ? 227 PRO D N   1 
ATOM   7360 C CA  . PRO D 1 227 ? 16.102  -33.885 -1.230  1.00 32.01 ? 227 PRO D CA  1 
ATOM   7361 C C   . PRO D 1 227 ? 16.698  -35.222 -0.813  1.00 31.13 ? 227 PRO D C   1 
ATOM   7362 O O   . PRO D 1 227 ? 16.815  -36.149 -1.616  1.00 33.61 ? 227 PRO D O   1 
ATOM   7363 C CB  . PRO D 1 227 ? 14.567  -33.934 -1.221  1.00 30.22 ? 227 PRO D CB  1 
ATOM   7364 C CG  . PRO D 1 227 ? 14.136  -33.321 -2.545  1.00 30.89 ? 227 PRO D CG  1 
ATOM   7365 C CD  . PRO D 1 227 ? 15.254  -33.540 -3.494  1.00 29.64 ? 227 PRO D CD  1 
ATOM   7366 N N   . ALA D 1 228 ? 17.082  -35.308 0.456   1.00 27.98 ? 228 ALA D N   1 
ATOM   7367 C CA  . ALA D 1 228 ? 17.648  -36.554 0.979   1.00 34.98 ? 228 ALA D CA  1 
ATOM   7368 C C   . ALA D 1 228 ? 16.599  -37.644 1.107   1.00 42.81 ? 228 ALA D C   1 
ATOM   7369 O O   . ALA D 1 228 ? 15.400  -37.356 1.292   1.00 43.86 ? 228 ALA D O   1 
ATOM   7370 C CB  . ALA D 1 228 ? 18.287  -36.308 2.313   1.00 33.50 ? 228 ALA D CB  1 
ATOM   7371 O OXT . ALA D 1 228 ? 16.879  -38.849 0.980   1.00 45.43 ? 228 ALA D OXT 1 
HETATM 7372 O O   . HOH E 2 .   ? 2.211   5.284   32.029  1.00 40.55 ? 301 HOH A O   1 
HETATM 7373 O O   . HOH E 2 .   ? 17.877  15.161  18.622  1.00 50.09 ? 302 HOH A O   1 
HETATM 7374 O O   . HOH E 2 .   ? 26.319  8.600   24.761  1.00 42.86 ? 303 HOH A O   1 
HETATM 7375 O O   . HOH E 2 .   ? 29.217  -1.859  28.523  1.00 32.62 ? 304 HOH A O   1 
HETATM 7376 O O   . HOH E 2 .   ? 20.002  -11.344 39.757  1.00 37.25 ? 305 HOH A O   1 
HETATM 7377 O O   . HOH E 2 .   ? 20.269  -14.207 40.532  1.00 29.39 ? 306 HOH A O   1 
HETATM 7378 O O   . HOH E 2 .   ? -2.655  -8.355  22.880  1.00 43.98 ? 307 HOH A O   1 
HETATM 7379 O O   . HOH E 2 .   ? 51.261  -4.024  28.348  1.00 51.30 ? 308 HOH A O   1 
HETATM 7380 O O   . HOH E 2 .   ? 31.596  8.164   22.381  1.00 37.00 ? 309 HOH A O   1 
HETATM 7381 O O   . HOH E 2 .   ? 9.815   -13.390 24.646  1.00 36.11 ? 310 HOH A O   1 
HETATM 7382 O O   . HOH E 2 .   ? 31.421  -11.459 33.226  1.00 30.02 ? 311 HOH A O   1 
HETATM 7383 O O   . HOH E 2 .   ? 47.484  -2.998  44.191  1.00 46.95 ? 312 HOH A O   1 
HETATM 7384 O O   . HOH E 2 .   ? 45.122  -13.407 39.092  1.00 49.33 ? 313 HOH A O   1 
HETATM 7385 O O   . HOH E 2 .   ? 46.591  -8.418  38.306  1.00 38.13 ? 314 HOH A O   1 
HETATM 7386 O O   . HOH E 2 .   ? 6.867   9.187   16.868  1.00 57.36 ? 315 HOH A O   1 
HETATM 7387 O O   . HOH E 2 .   ? 35.405  -12.157 37.148  1.00 35.84 ? 316 HOH A O   1 
HETATM 7388 O O   . HOH E 2 .   ? 43.649  0.065   44.282  1.00 34.08 ? 317 HOH A O   1 
HETATM 7389 O O   . HOH E 2 .   ? 40.136  3.272   37.656  1.00 31.98 ? 318 HOH A O   1 
HETATM 7390 O O   . HOH E 2 .   ? 3.715   6.063   30.969  1.00 34.17 ? 319 HOH A O   1 
HETATM 7391 O O   . HOH E 2 .   ? 1.681   -4.336  47.348  1.00 47.12 ? 320 HOH A O   1 
HETATM 7392 O O   . HOH E 2 .   ? 19.514  -4.274  43.104  1.00 24.06 ? 321 HOH A O   1 
HETATM 7393 O O   . HOH E 2 .   ? 2.673   -9.515  28.222  1.00 35.42 ? 322 HOH A O   1 
HETATM 7394 O O   . HOH E 2 .   ? 6.918   2.177   17.217  1.00 42.32 ? 323 HOH A O   1 
HETATM 7395 O O   . HOH E 2 .   ? 25.620  -9.101  30.188  1.00 28.31 ? 324 HOH A O   1 
HETATM 7396 O O   . HOH E 2 .   ? 29.189  -12.553 50.986  1.00 55.75 ? 325 HOH A O   1 
HETATM 7397 O O   . HOH E 2 .   ? 18.644  -10.069 42.374  1.00 32.74 ? 326 HOH A O   1 
HETATM 7398 O O   . HOH E 2 .   ? 7.694   1.135   14.537  1.00 41.41 ? 327 HOH A O   1 
HETATM 7399 O O   . HOH E 2 .   ? 23.910  17.355  31.762  1.00 45.01 ? 328 HOH A O   1 
HETATM 7400 O O   . HOH E 2 .   ? 7.195   -9.437  29.941  1.00 31.99 ? 329 HOH A O   1 
HETATM 7401 O O   . HOH E 2 .   ? 18.223  6.454   47.901  1.00 34.65 ? 330 HOH A O   1 
HETATM 7402 O O   . HOH E 2 .   ? 33.975  3.088   17.665  1.00 50.90 ? 331 HOH A O   1 
HETATM 7403 O O   . HOH E 2 .   ? 23.409  -4.563  45.513  1.00 26.24 ? 332 HOH A O   1 
HETATM 7404 O O   . HOH E 2 .   ? -0.470  2.644   24.781  1.00 37.05 ? 333 HOH A O   1 
HETATM 7405 O O   . HOH E 2 .   ? 29.302  9.795   25.099  1.00 38.82 ? 334 HOH A O   1 
HETATM 7406 O O   . HOH E 2 .   ? 48.248  1.784   42.821  1.00 40.21 ? 335 HOH A O   1 
HETATM 7407 O O   . HOH E 2 .   ? 43.466  -2.153  40.370  1.00 31.17 ? 336 HOH A O   1 
HETATM 7408 O O   . HOH E 2 .   ? 29.659  5.903   38.166  1.00 27.11 ? 337 HOH A O   1 
HETATM 7409 O O   . HOH E 2 .   ? 14.550  13.603  35.588  1.00 27.98 ? 338 HOH A O   1 
HETATM 7410 O O   . HOH E 2 .   ? 25.772  4.812   45.794  1.00 56.33 ? 339 HOH A O   1 
HETATM 7411 O O   . HOH E 2 .   ? 21.430  -6.790  46.367  1.00 29.88 ? 340 HOH A O   1 
HETATM 7412 O O   . HOH E 2 .   ? 7.668   14.639  37.648  1.00 35.62 ? 341 HOH A O   1 
HETATM 7413 O O   . HOH E 2 .   ? 43.663  -5.452  26.574  1.00 42.46 ? 342 HOH A O   1 
HETATM 7414 O O   . HOH E 2 .   ? 28.348  1.353   38.529  1.00 22.46 ? 343 HOH A O   1 
HETATM 7415 O O   . HOH E 2 .   ? 29.164  -1.485  37.805  1.00 23.61 ? 344 HOH A O   1 
HETATM 7416 O O   . HOH E 2 .   ? 25.345  1.928   28.146  1.00 42.48 ? 345 HOH A O   1 
HETATM 7417 O O   . HOH E 2 .   ? 11.814  15.436  44.566  1.00 47.74 ? 346 HOH A O   1 
HETATM 7418 O O   . HOH E 2 .   ? 33.796  -3.365  43.442  1.00 28.39 ? 347 HOH A O   1 
HETATM 7419 O O   . HOH E 2 .   ? 14.213  -16.168 26.185  1.00 46.99 ? 348 HOH A O   1 
HETATM 7420 O O   . HOH E 2 .   ? -0.676  1.974   35.532  1.00 39.21 ? 349 HOH A O   1 
HETATM 7421 O O   . HOH E 2 .   ? 27.786  3.218   41.872  1.00 29.36 ? 350 HOH A O   1 
HETATM 7422 O O   . HOH E 2 .   ? 5.310   -9.237  21.269  1.00 40.27 ? 351 HOH A O   1 
HETATM 7423 O O   . HOH E 2 .   ? 42.707  0.324   47.543  1.00 34.80 ? 352 HOH A O   1 
HETATM 7424 O O   . HOH E 2 .   ? 35.461  10.190  31.417  1.00 34.40 ? 353 HOH A O   1 
HETATM 7425 O O   . HOH E 2 .   ? 2.673   10.883  41.434  1.00 32.45 ? 354 HOH A O   1 
HETATM 7426 O O   . HOH E 2 .   ? 9.580   1.247   48.718  1.00 33.82 ? 355 HOH A O   1 
HETATM 7427 O O   . HOH E 2 .   ? 25.507  2.230   44.794  1.00 28.28 ? 356 HOH A O   1 
HETATM 7428 O O   . HOH E 2 .   ? 19.874  -3.959  39.107  1.00 22.35 ? 357 HOH A O   1 
HETATM 7429 O O   . HOH E 2 .   ? 16.142  6.620   15.128  1.00 45.81 ? 358 HOH A O   1 
HETATM 7430 O O   . HOH E 2 .   ? 10.651  15.277  26.638  1.00 42.36 ? 359 HOH A O   1 
HETATM 7431 O O   . HOH E 2 .   ? 4.756   0.858   40.413  1.00 31.06 ? 360 HOH A O   1 
HETATM 7432 O O   . HOH E 2 .   ? 19.781  -9.733  44.947  1.00 34.05 ? 361 HOH A O   1 
HETATM 7433 O O   . HOH E 2 .   ? 4.560   5.770   45.968  1.00 34.98 ? 362 HOH A O   1 
HETATM 7434 O O   . HOH E 2 .   ? 31.448  4.891   40.379  1.00 28.01 ? 363 HOH A O   1 
HETATM 7435 O O   . HOH E 2 .   ? 12.183  1.038   14.534  1.00 47.37 ? 364 HOH A O   1 
HETATM 7436 O O   . HOH E 2 .   ? 18.387  -3.591  47.014  1.00 25.99 ? 365 HOH A O   1 
HETATM 7437 O O   . HOH E 2 .   ? 30.075  2.378   40.397  1.00 24.45 ? 366 HOH A O   1 
HETATM 7438 O O   . HOH E 2 .   ? 40.485  -1.122  46.261  1.00 30.20 ? 367 HOH A O   1 
HETATM 7439 O O   . HOH E 2 .   ? 29.782  -2.224  49.485  1.00 35.19 ? 368 HOH A O   1 
HETATM 7440 O O   . HOH E 2 .   ? 24.488  17.558  36.224  1.00 45.19 ? 369 HOH A O   1 
HETATM 7441 O O   . HOH E 2 .   ? 7.098   0.555   41.137  1.00 25.70 ? 370 HOH A O   1 
HETATM 7442 O O   . HOH E 2 .   ? -1.033  -3.721  22.424  1.00 37.37 ? 371 HOH A O   1 
HETATM 7443 O O   . HOH E 2 .   ? 51.789  4.992   34.169  1.00 44.02 ? 372 HOH A O   1 
HETATM 7444 O O   . HOH E 2 .   ? 9.414   -11.134 44.290  1.00 39.28 ? 373 HOH A O   1 
HETATM 7445 O O   . HOH E 2 .   ? 0.117   -10.387 28.913  1.00 39.16 ? 374 HOH A O   1 
HETATM 7446 O O   . HOH E 2 .   ? 29.391  3.251   44.224  1.00 39.03 ? 375 HOH A O   1 
HETATM 7447 O O   . HOH E 2 .   ? 52.062  2.288   39.499  1.00 37.10 ? 376 HOH A O   1 
HETATM 7448 O O   . HOH E 2 .   ? 21.557  6.032   46.891  1.00 36.44 ? 377 HOH A O   1 
HETATM 7449 O O   . HOH E 2 .   ? 22.085  -10.316 31.075  1.00 39.92 ? 378 HOH A O   1 
HETATM 7450 O O   . HOH E 2 .   ? 28.310  -1.315  35.310  1.00 26.34 ? 379 HOH A O   1 
HETATM 7451 O O   . HOH E 2 .   ? 40.315  5.594   29.831  1.00 40.12 ? 380 HOH A O   1 
HETATM 7452 O O   . HOH E 2 .   ? 11.109  13.971  23.966  1.00 47.43 ? 381 HOH A O   1 
HETATM 7453 O O   . HOH E 2 .   ? 43.046  3.117   37.114  1.00 35.34 ? 382 HOH A O   1 
HETATM 7454 O O   . HOH E 2 .   ? 25.006  9.941   42.617  1.00 33.61 ? 383 HOH A O   1 
HETATM 7455 O O   . HOH E 2 .   ? 16.609  -13.878 32.907  1.00 34.26 ? 384 HOH A O   1 
HETATM 7456 O O   . HOH E 2 .   ? 24.923  -11.100 33.633  1.00 35.34 ? 385 HOH A O   1 
HETATM 7457 O O   . HOH E 2 .   ? -1.866  -1.019  38.705  1.00 37.57 ? 386 HOH A O   1 
HETATM 7458 O O   . HOH E 2 .   ? 16.950  -15.365 28.755  1.00 41.66 ? 387 HOH A O   1 
HETATM 7459 O O   . HOH E 2 .   ? -0.058  -6.371  47.932  1.00 41.94 ? 388 HOH A O   1 
HETATM 7460 O O   . HOH E 2 .   ? 7.535   15.677  32.004  1.00 38.43 ? 389 HOH A O   1 
HETATM 7461 O O   . HOH E 2 .   ? 30.193  7.313   41.848  1.00 42.31 ? 390 HOH A O   1 
HETATM 7462 O O   . HOH E 2 .   ? 28.640  5.713   42.677  1.00 43.35 ? 391 HOH A O   1 
HETATM 7463 O O   . HOH E 2 .   ? 10.188  -5.872  51.234  1.00 44.60 ? 392 HOH A O   1 
HETATM 7464 O O   . HOH E 2 .   ? 29.941  9.070   39.727  1.00 33.46 ? 393 HOH A O   1 
HETATM 7465 O O   . HOH E 2 .   ? 35.836  -11.848 44.328  1.00 40.33 ? 394 HOH A O   1 
HETATM 7466 O O   . HOH E 2 .   ? 3.963   -1.772  40.956  1.00 36.06 ? 395 HOH A O   1 
HETATM 7467 O O   . HOH E 2 .   ? 34.236  12.434  29.605  1.00 38.52 ? 396 HOH A O   1 
HETATM 7468 O O   . HOH E 2 .   ? 31.691  -13.663 38.038  1.00 34.21 ? 397 HOH A O   1 
HETATM 7469 O O   . HOH E 2 .   ? 1.246   1.235   37.924  1.00 37.16 ? 398 HOH A O   1 
HETATM 7470 O O   . HOH E 2 .   ? 1.599   9.641   42.748  1.00 43.33 ? 399 HOH A O   1 
HETATM 7471 O O   . HOH E 2 .   ? 0.747   -2.384  40.620  1.00 45.96 ? 400 HOH A O   1 
HETATM 7472 O O   . HOH E 2 .   ? 0.998   -0.379  40.029  1.00 39.25 ? 401 HOH A O   1 
HETATM 7473 O O   . HOH E 2 .   ? 44.285  0.226   46.095  1.00 46.83 ? 402 HOH A O   1 
HETATM 7474 O O   . HOH E 2 .   ? 0.186   -4.027  41.996  1.00 44.06 ? 403 HOH A O   1 
HETATM 7475 O O   . HOH E 2 .   ? 4.720   9.303   17.471  1.00 50.23 ? 404 HOH A O   1 
HETATM 7476 O O   . HOH E 2 .   ? 36.597  11.795  33.784  1.00 35.86 ? 405 HOH A O   1 
HETATM 7477 O O   . HOH E 2 .   ? 25.049  -9.515  18.479  1.00 56.35 ? 406 HOH A O   1 
HETATM 7478 O O   . HOH E 2 .   ? 24.913  -10.023 16.247  1.00 51.02 ? 407 HOH A O   1 
HETATM 7479 O O   . HOH F 2 .   ? 15.535  -5.734  -30.310 1.00 48.55 ? 301 HOH B O   1 
HETATM 7480 O O   . HOH F 2 .   ? 35.376  -6.857  6.455   1.00 45.33 ? 302 HOH B O   1 
HETATM 7481 O O   . HOH F 2 .   ? 21.950  -11.001 -3.260  1.00 30.54 ? 303 HOH B O   1 
HETATM 7482 O O   . HOH F 2 .   ? 32.901  -8.293  -10.087 1.00 29.86 ? 304 HOH B O   1 
HETATM 7483 O O   . HOH F 2 .   ? 11.200  -9.792  -19.284 1.00 36.64 ? 305 HOH B O   1 
HETATM 7484 O O   . HOH F 2 .   ? 33.167  11.287  -21.889 1.00 37.56 ? 306 HOH B O   1 
HETATM 7485 O O   . HOH F 2 .   ? 23.230  1.451   -19.960 1.00 46.01 ? 307 HOH B O   1 
HETATM 7486 O O   . HOH F 2 .   ? 27.807  12.293  -18.888 1.00 40.62 ? 308 HOH B O   1 
HETATM 7487 O O   . HOH F 2 .   ? 21.014  -0.995  -0.844  1.00 25.79 ? 309 HOH B O   1 
HETATM 7488 O O   . HOH F 2 .   ? 45.033  1.122   -3.598  1.00 28.87 ? 310 HOH B O   1 
HETATM 7489 O O   . HOH F 2 .   ? 47.890  -4.840  -6.154  1.00 35.86 ? 311 HOH B O   1 
HETATM 7490 O O   . HOH F 2 .   ? 20.129  -6.838  -1.726  1.00 26.43 ? 312 HOH B O   1 
HETATM 7491 O O   . HOH F 2 .   ? 48.757  0.699   0.396   1.00 37.25 ? 313 HOH B O   1 
HETATM 7492 O O   . HOH F 2 .   ? 1.792   4.562   -27.479 1.00 45.05 ? 314 HOH B O   1 
HETATM 7493 O O   . HOH F 2 .   ? 8.433   -5.926  -13.988 1.00 32.87 ? 315 HOH B O   1 
HETATM 7494 O O   . HOH F 2 .   ? 37.052  -1.791  -21.408 1.00 37.46 ? 316 HOH B O   1 
HETATM 7495 O O   . HOH F 2 .   ? 22.364  18.162  -22.964 1.00 54.53 ? 317 HOH B O   1 
HETATM 7496 O O   . HOH F 2 .   ? 41.661  6.727   -6.522  1.00 28.31 ? 318 HOH B O   1 
HETATM 7497 O O   . HOH F 2 .   ? 21.300  -0.519  -4.795  1.00 17.94 ? 319 HOH B O   1 
HETATM 7498 O O   . HOH F 2 .   ? 27.300  -5.683  -13.732 1.00 30.69 ? 320 HOH B O   1 
HETATM 7499 O O   . HOH F 2 .   ? 22.937  18.205  -4.187  1.00 44.63 ? 321 HOH B O   1 
HETATM 7500 O O   . HOH F 2 .   ? 44.308  3.756   3.313   1.00 33.81 ? 322 HOH B O   1 
HETATM 7501 O O   . HOH F 2 .   ? 22.591  11.949  -25.650 1.00 40.34 ? 323 HOH B O   1 
HETATM 7502 O O   . HOH F 2 .   ? 39.700  8.639   -15.318 1.00 45.13 ? 324 HOH B O   1 
HETATM 7503 O O   . HOH F 2 .   ? 21.281  -10.446 1.498   1.00 35.70 ? 325 HOH B O   1 
HETATM 7504 O O   . HOH F 2 .   ? 24.824  -1.228  1.532   1.00 23.31 ? 326 HOH B O   1 
HETATM 7505 O O   . HOH F 2 .   ? 27.135  8.139   1.933   1.00 46.59 ? 327 HOH B O   1 
HETATM 7506 O O   . HOH F 2 .   ? 41.986  -7.233  -16.448 1.00 35.19 ? 328 HOH B O   1 
HETATM 7507 O O   . HOH F 2 .   ? 19.993  9.779   3.949   1.00 34.27 ? 329 HOH B O   1 
HETATM 7508 O O   . HOH F 2 .   ? -1.034  -4.607  -20.822 1.00 46.36 ? 330 HOH B O   1 
HETATM 7509 O O   . HOH F 2 .   ? 13.245  18.856  0.289   1.00 34.85 ? 331 HOH B O   1 
HETATM 7510 O O   . HOH F 2 .   ? 30.420  1.591   -15.918 1.00 32.52 ? 332 HOH B O   1 
HETATM 7511 O O   . HOH F 2 .   ? 45.258  3.201   0.888   1.00 34.26 ? 333 HOH B O   1 
HETATM 7512 O O   . HOH F 2 .   ? 1.500   -7.005  -14.673 1.00 37.13 ? 334 HOH B O   1 
HETATM 7513 O O   . HOH F 2 .   ? 39.944  13.318  -6.458  1.00 28.35 ? 335 HOH B O   1 
HETATM 7514 O O   . HOH F 2 .   ? 8.286   5.625   -26.890 1.00 42.34 ? 336 HOH B O   1 
HETATM 7515 O O   . HOH F 2 .   ? 36.855  -8.944  -6.697  1.00 34.55 ? 337 HOH B O   1 
HETATM 7516 O O   . HOH F 2 .   ? 36.885  13.427  -12.530 1.00 30.05 ? 338 HOH B O   1 
HETATM 7517 O O   . HOH F 2 .   ? 16.125  16.871  -8.406  1.00 29.27 ? 339 HOH B O   1 
HETATM 7518 O O   . HOH F 2 .   ? 5.095   9.242   -12.879 1.00 34.60 ? 340 HOH B O   1 
HETATM 7519 O O   . HOH F 2 .   ? -4.707  1.977   -12.664 1.00 36.60 ? 341 HOH B O   1 
HETATM 7520 O O   . HOH F 2 .   ? 31.082  9.345   -5.720  1.00 22.20 ? 342 HOH B O   1 
HETATM 7521 O O   . HOH F 2 .   ? 29.249  6.498   -2.061  1.00 25.95 ? 343 HOH B O   1 
HETATM 7522 O O   . HOH F 2 .   ? 26.986  5.576   0.821   1.00 28.34 ? 344 HOH B O   1 
HETATM 7523 O O   . HOH F 2 .   ? 18.025  -12.076 -15.240 1.00 40.22 ? 345 HOH B O   1 
HETATM 7524 O O   . HOH F 2 .   ? 4.303   13.939  -7.185  1.00 40.17 ? 346 HOH B O   1 
HETATM 7525 O O   . HOH F 2 .   ? 0.862   6.156   -19.216 1.00 37.16 ? 347 HOH B O   1 
HETATM 7526 O O   . HOH F 2 .   ? 6.061   9.163   2.136   1.00 37.10 ? 348 HOH B O   1 
HETATM 7527 O O   . HOH F 2 .   ? 32.631  -1.758  -19.206 1.00 35.86 ? 349 HOH B O   1 
HETATM 7528 O O   . HOH F 2 .   ? 8.629   3.918   -2.672  1.00 26.67 ? 350 HOH B O   1 
HETATM 7529 O O   . HOH F 2 .   ? 21.225  -6.536  0.927   1.00 30.30 ? 351 HOH B O   1 
HETATM 7530 O O   . HOH F 2 .   ? 11.137  4.736   4.979   1.00 33.95 ? 352 HOH B O   1 
HETATM 7531 O O   . HOH F 2 .   ? 11.075  -7.475  0.609   1.00 38.51 ? 353 HOH B O   1 
HETATM 7532 O O   . HOH F 2 .   ? 12.591  16.530  4.203   1.00 39.91 ? 354 HOH B O   1 
HETATM 7533 O O   . HOH F 2 .   ? 30.711  1.928   -6.193  1.00 22.99 ? 355 HOH B O   1 
HETATM 7534 O O   . HOH F 2 .   ? 4.201   14.223  -2.363  1.00 34.15 ? 356 HOH B O   1 
HETATM 7535 O O   . HOH F 2 .   ? 9.078   18.152  -6.184  1.00 37.18 ? 357 HOH B O   1 
HETATM 7536 O O   . HOH F 2 .   ? 23.188  9.345   3.023   1.00 36.93 ? 358 HOH B O   1 
HETATM 7537 O O   . HOH F 2 .   ? 0.805   5.333   -8.242  1.00 37.29 ? 359 HOH B O   1 
HETATM 7538 O O   . HOH F 2 .   ? 41.701  2.152   2.412   1.00 28.35 ? 360 HOH B O   1 
HETATM 7539 O O   . HOH F 2 .   ? 2.647   -0.774  3.095   1.00 43.29 ? 361 HOH B O   1 
HETATM 7540 O O   . HOH F 2 .   ? 29.931  4.622   -5.500  1.00 21.38 ? 362 HOH B O   1 
HETATM 7541 O O   . HOH F 2 .   ? 23.067  1.669   5.076   1.00 50.41 ? 363 HOH B O   1 
HETATM 7542 O O   . HOH F 2 .   ? 26.446  16.169  -6.218  1.00 32.99 ? 364 HOH B O   1 
HETATM 7543 O O   . HOH F 2 .   ? 4.107   -6.281  -15.375 1.00 36.61 ? 365 HOH B O   1 
HETATM 7544 O O   . HOH F 2 .   ? 28.099  1.729   4.432   1.00 42.40 ? 366 HOH B O   1 
HETATM 7545 O O   . HOH F 2 .   ? 39.555  3.819   4.999   1.00 40.46 ? 367 HOH B O   1 
HETATM 7546 O O   . HOH F 2 .   ? 6.498   -2.084  -4.660  1.00 38.71 ? 368 HOH B O   1 
HETATM 7547 O O   . HOH F 2 .   ? 19.876  -0.199  2.929   1.00 28.04 ? 369 HOH B O   1 
HETATM 7548 O O   . HOH F 2 .   ? 14.341  19.091  -11.830 1.00 43.81 ? 370 HOH B O   1 
HETATM 7549 O O   . HOH F 2 .   ? 29.694  1.944   -8.717  1.00 21.40 ? 371 HOH B O   1 
HETATM 7550 O O   . HOH F 2 .   ? 12.067  18.626  -17.173 1.00 43.01 ? 372 HOH B O   1 
HETATM 7551 O O   . HOH F 2 .   ? 26.373  13.321  -1.677  1.00 33.31 ? 373 HOH B O   1 
HETATM 7552 O O   . HOH F 2 .   ? 25.903  -7.819  -11.030 1.00 36.06 ? 374 HOH B O   1 
HETATM 7553 O O   . HOH F 2 .   ? 7.555   17.314  -18.065 1.00 43.33 ? 375 HOH B O   1 
HETATM 7554 O O   . HOH F 2 .   ? 36.734  -7.411  -10.142 1.00 30.36 ? 376 HOH B O   1 
HETATM 7555 O O   . HOH F 2 .   ? 35.270  0.144   -0.641  1.00 26.77 ? 377 HOH B O   1 
HETATM 7556 O O   . HOH F 2 .   ? -3.360  1.168   -9.496  1.00 47.39 ? 378 HOH B O   1 
HETATM 7557 O O   . HOH F 2 .   ? 16.944  -11.106 -12.651 1.00 39.11 ? 379 HOH B O   1 
HETATM 7558 O O   . HOH F 2 .   ? 41.771  8.663   -14.122 1.00 35.05 ? 380 HOH B O   1 
HETATM 7559 O O   . HOH F 2 .   ? 7.337   17.472  -15.329 1.00 40.38 ? 381 HOH B O   1 
HETATM 7560 O O   . HOH F 2 .   ? 32.737  8.240   -3.557  1.00 24.95 ? 382 HOH B O   1 
HETATM 7561 O O   . HOH F 2 .   ? 31.122  1.196   5.453   1.00 33.76 ? 383 HOH B O   1 
HETATM 7562 O O   . HOH F 2 .   ? -0.636  -14.244 -8.809  1.00 37.61 ? 384 HOH B O   1 
HETATM 7563 O O   . HOH F 2 .   ? 4.040   14.634  -9.159  1.00 48.30 ? 385 HOH B O   1 
HETATM 7564 O O   . HOH F 2 .   ? 14.994  0.480   3.395   1.00 36.65 ? 386 HOH B O   1 
HETATM 7565 O O   . HOH F 2 .   ? 6.015   4.043   -3.602  1.00 30.54 ? 387 HOH B O   1 
HETATM 7566 O O   . HOH F 2 .   ? 31.022  6.381   0.506   1.00 38.70 ? 388 HOH B O   1 
HETATM 7567 O O   . HOH F 2 .   ? 8.622   4.895   -28.663 1.00 51.38 ? 389 HOH B O   1 
HETATM 7568 O O   . HOH F 2 .   ? 32.610  -9.215  -4.072  1.00 43.42 ? 390 HOH B O   1 
HETATM 7569 O O   . HOH F 2 .   ? 31.369  5.753   -3.491  1.00 22.18 ? 391 HOH B O   1 
HETATM 7570 O O   . HOH F 2 .   ? 22.692  -3.231  2.573   1.00 31.54 ? 392 HOH B O   1 
HETATM 7571 O O   . HOH F 2 .   ? 35.071  -9.497  6.748   1.00 44.78 ? 393 HOH B O   1 
HETATM 7572 O O   . HOH F 2 .   ? -4.678  2.626   -10.591 1.00 52.45 ? 394 HOH B O   1 
HETATM 7573 O O   . HOH F 2 .   ? 18.164  -10.489 -11.087 1.00 33.55 ? 395 HOH B O   1 
HETATM 7574 O O   . HOH F 2 .   ? 17.042  -1.512  4.011   1.00 40.44 ? 396 HOH B O   1 
HETATM 7575 O O   . HOH F 2 .   ? -7.091  5.825   -9.904  1.00 51.36 ? 397 HOH B O   1 
HETATM 7576 O O   . HOH F 2 .   ? 26.462  20.792  -7.851  1.00 43.03 ? 398 HOH B O   1 
HETATM 7577 O O   . HOH F 2 .   ? 23.688  -7.163  -12.993 1.00 41.98 ? 399 HOH B O   1 
HETATM 7578 O O   . HOH F 2 .   ? 31.918  10.583  -2.176  1.00 36.98 ? 400 HOH B O   1 
HETATM 7579 O O   . HOH F 2 .   ? 31.395  -10.609 5.438   1.00 39.76 ? 401 HOH B O   1 
HETATM 7580 O O   . HOH F 2 .   ? 0.231   -0.290  -21.747 1.00 39.36 ? 402 HOH B O   1 
HETATM 7581 O O   . HOH F 2 .   ? 2.866   14.428  -4.242  1.00 48.38 ? 403 HOH B O   1 
HETATM 7582 O O   . HOH F 2 .   ? 25.347  -0.043  -19.287 1.00 38.56 ? 404 HOH B O   1 
HETATM 7583 O O   . HOH F 2 .   ? 36.919  -6.529  3.951   1.00 39.39 ? 405 HOH B O   1 
HETATM 7584 O O   . HOH F 2 .   ? 13.482  5.976   6.354   1.00 33.91 ? 406 HOH B O   1 
HETATM 7585 O O   . HOH F 2 .   ? 31.509  12.260  -4.738  1.00 30.73 ? 407 HOH B O   1 
HETATM 7586 O O   . HOH F 2 .   ? 45.469  -4.139  -15.041 1.00 39.71 ? 408 HOH B O   1 
HETATM 7587 O O   . HOH F 2 .   ? 24.861  0.150   3.366   1.00 38.50 ? 409 HOH B O   1 
HETATM 7588 O O   . HOH F 2 .   ? 26.001  21.549  -9.991  1.00 46.65 ? 410 HOH B O   1 
HETATM 7589 O O   . HOH F 2 .   ? 35.800  15.621  -14.148 1.00 33.94 ? 411 HOH B O   1 
HETATM 7590 O O   . HOH F 2 .   ? 5.078   3.223   -5.289  1.00 39.21 ? 412 HOH B O   1 
HETATM 7591 O O   . HOH F 2 .   ? 28.457  9.366   3.079   1.00 46.39 ? 413 HOH B O   1 
HETATM 7592 O O   . HOH F 2 .   ? 37.342  -8.666  0.360   1.00 44.06 ? 414 HOH B O   1 
HETATM 7593 O O   . HOH F 2 .   ? 5.232   1.578   -3.000  1.00 38.97 ? 415 HOH B O   1 
HETATM 7594 O O   . HOH F 2 .   ? 38.430  -9.089  2.726   1.00 43.43 ? 416 HOH B O   1 
HETATM 7595 O O   . HOH F 2 .   ? 2.034   -0.140  -0.974  1.00 52.96 ? 417 HOH B O   1 
HETATM 7596 O O   . HOH F 2 .   ? 36.797  -7.466  1.985   1.00 41.65 ? 418 HOH B O   1 
HETATM 7597 O O   . HOH F 2 .   ? 32.085  12.220  0.536   1.00 48.25 ? 419 HOH B O   1 
HETATM 7598 O O   . HOH F 2 .   ? 25.617  20.843  -12.116 1.00 51.10 ? 420 HOH B O   1 
HETATM 7599 O O   . HOH F 2 .   ? 0.773   -0.410  0.864   1.00 53.84 ? 421 HOH B O   1 
HETATM 7600 O O   . HOH F 2 .   ? 29.738  13.273  -1.237  1.00 44.31 ? 422 HOH B O   1 
HETATM 7601 O O   . HOH F 2 .   ? 32.805  -10.323 -5.915  1.00 31.23 ? 423 HOH B O   1 
HETATM 7602 O O   . HOH F 2 .   ? 13.920  1.935   5.087   1.00 43.47 ? 424 HOH B O   1 
HETATM 7603 O O   . HOH F 2 .   ? 39.318  11.644  -13.802 1.00 44.94 ? 425 HOH B O   1 
HETATM 7604 O O   . HOH F 2 .   ? 21.074  -8.713  -16.856 1.00 39.49 ? 426 HOH B O   1 
HETATM 7605 O O   . HOH F 2 .   ? 39.935  10.732  -16.289 1.00 41.69 ? 427 HOH B O   1 
HETATM 7606 O O   . HOH F 2 .   ? 35.415  6.389   6.966   1.00 41.28 ? 428 HOH B O   1 
HETATM 7607 O O   . HOH F 2 .   ? 30.320  11.890  0.203   1.00 47.21 ? 429 HOH B O   1 
HETATM 7608 O O   . HOH F 2 .   ? 16.501  -14.502 -15.327 1.00 43.74 ? 430 HOH B O   1 
HETATM 7609 O O   . HOH F 2 .   ? 47.382  -3.001  -17.299 1.00 49.55 ? 431 HOH B O   1 
HETATM 7610 O O   . HOH F 2 .   ? 5.606   -5.622  -4.083  1.00 48.24 ? 432 HOH B O   1 
HETATM 7611 O O   . HOH F 2 .   ? 2.708   12.738  -9.294  1.00 43.13 ? 433 HOH B O   1 
HETATM 7612 O O   . HOH F 2 .   ? 38.312  14.853  -10.254 1.00 34.73 ? 434 HOH B O   1 
HETATM 7613 O O   . HOH G 2 .   ? 8.566   -17.177 31.389  1.00 48.97 ? 301 HOH C O   1 
HETATM 7614 O O   . HOH G 2 .   ? 25.455  -17.712 23.724  1.00 41.87 ? 302 HOH C O   1 
HETATM 7615 O O   . HOH G 2 .   ? 40.752  -13.474 31.296  1.00 37.30 ? 303 HOH C O   1 
HETATM 7616 O O   . HOH G 2 .   ? 13.842  -42.185 43.638  1.00 58.03 ? 304 HOH C O   1 
HETATM 7617 O O   . HOH G 2 .   ? -7.486  -35.282 39.873  1.00 44.79 ? 305 HOH C O   1 
HETATM 7618 O O   . HOH G 2 .   ? 31.353  -14.283 23.766  1.00 43.71 ? 306 HOH C O   1 
HETATM 7619 O O   . HOH G 2 .   ? -7.219  -16.323 46.667  1.00 38.82 ? 307 HOH C O   1 
HETATM 7620 O O   . HOH G 2 .   ? 7.086   -38.270 36.542  1.00 34.23 ? 308 HOH C O   1 
HETATM 7621 O O   . HOH G 2 .   ? 22.822  -28.084 53.337  1.00 41.77 ? 309 HOH C O   1 
HETATM 7622 O O   . HOH G 2 .   ? -6.880  -20.602 36.005  1.00 46.49 ? 310 HOH C O   1 
HETATM 7623 O O   . HOH G 2 .   ? 21.806  -43.255 30.521  1.00 48.15 ? 311 HOH C O   1 
HETATM 7624 O O   . HOH G 2 .   ? 26.395  -35.077 21.701  1.00 39.22 ? 312 HOH C O   1 
HETATM 7625 O O   . HOH G 2 .   ? 19.138  -5.669  45.366  1.00 33.62 ? 313 HOH C O   1 
HETATM 7626 O O   . HOH G 2 .   ? 28.825  -19.802 29.190  1.00 34.30 ? 314 HOH C O   1 
HETATM 7627 O O   . HOH G 2 .   ? 29.228  -22.862 21.024  1.00 41.51 ? 315 HOH C O   1 
HETATM 7628 O O   . HOH G 2 .   ? 29.088  -35.167 55.306  1.00 40.43 ? 316 HOH C O   1 
HETATM 7629 O O   . HOH G 2 .   ? 19.891  -19.702 45.641  1.00 27.24 ? 317 HOH C O   1 
HETATM 7630 O O   . HOH G 2 .   ? 18.774  -21.450 42.355  1.00 22.78 ? 318 HOH C O   1 
HETATM 7631 O O   . HOH G 2 .   ? 7.361   -26.668 34.889  1.00 30.29 ? 319 HOH C O   1 
HETATM 7632 O O   . HOH G 2 .   ? 31.318  -13.708 35.341  1.00 31.84 ? 320 HOH C O   1 
HETATM 7633 O O   . HOH G 2 .   ? -10.777 -33.260 42.181  1.00 39.87 ? 321 HOH C O   1 
HETATM 7634 O O   . HOH G 2 .   ? 17.201  -18.537 48.573  1.00 30.71 ? 322 HOH C O   1 
HETATM 7635 O O   . HOH G 2 .   ? 9.616   -23.729 44.042  1.00 21.62 ? 323 HOH C O   1 
HETATM 7636 O O   . HOH G 2 .   ? 2.937   -13.368 40.705  1.00 29.90 ? 324 HOH C O   1 
HETATM 7637 O O   . HOH G 2 .   ? 6.190   -20.096 49.576  1.00 31.17 ? 325 HOH C O   1 
HETATM 7638 O O   . HOH G 2 .   ? 33.930  -34.980 19.607  1.00 42.47 ? 326 HOH C O   1 
HETATM 7639 O O   . HOH G 2 .   ? 2.562   -36.632 43.319  1.00 31.00 ? 327 HOH C O   1 
HETATM 7640 O O   . HOH G 2 .   ? 9.538   -30.427 47.005  1.00 30.54 ? 328 HOH C O   1 
HETATM 7641 O O   . HOH G 2 .   ? 33.081  -33.886 34.533  1.00 28.30 ? 329 HOH C O   1 
HETATM 7642 O O   . HOH G 2 .   ? 19.584  -20.362 52.389  1.00 42.30 ? 330 HOH C O   1 
HETATM 7643 O O   . HOH G 2 .   ? 27.912  -37.805 52.181  1.00 36.13 ? 331 HOH C O   1 
HETATM 7644 O O   . HOH G 2 .   ? 14.739  -24.882 50.613  1.00 33.69 ? 332 HOH C O   1 
HETATM 7645 O O   . HOH G 2 .   ? 25.136  -42.365 29.416  1.00 35.22 ? 333 HOH C O   1 
HETATM 7646 O O   . HOH G 2 .   ? 31.772  -25.495 43.056  1.00 25.08 ? 334 HOH C O   1 
HETATM 7647 O O   . HOH G 2 .   ? 9.908   -24.843 41.328  1.00 24.06 ? 335 HOH C O   1 
HETATM 7648 O O   . HOH G 2 .   ? 14.037  -37.281 47.983  1.00 29.27 ? 336 HOH C O   1 
HETATM 7649 O O   . HOH G 2 .   ? 35.746  -33.316 27.035  1.00 31.16 ? 337 HOH C O   1 
HETATM 7650 O O   . HOH G 2 .   ? 13.358  -31.021 52.475  1.00 49.33 ? 338 HOH C O   1 
HETATM 7651 O O   . HOH G 2 .   ? 3.796   -37.944 33.245  1.00 34.58 ? 339 HOH C O   1 
HETATM 7652 O O   . HOH G 2 .   ? 10.523  -26.240 45.340  1.00 26.26 ? 340 HOH C O   1 
HETATM 7653 O O   . HOH G 2 .   ? 10.972  -19.415 33.873  1.00 28.82 ? 341 HOH C O   1 
HETATM 7654 O O   . HOH G 2 .   ? 15.715  -26.591 52.868  1.00 42.09 ? 342 HOH C O   1 
HETATM 7655 O O   . HOH G 2 .   ? 18.710  -16.410 48.128  1.00 49.29 ? 343 HOH C O   1 
HETATM 7656 O O   . HOH G 2 .   ? 11.148  -30.695 35.214  1.00 34.05 ? 344 HOH C O   1 
HETATM 7657 O O   . HOH G 2 .   ? 27.348  -31.711 54.802  1.00 40.45 ? 345 HOH C O   1 
HETATM 7658 O O   . HOH G 2 .   ? 31.330  -39.045 27.288  1.00 32.65 ? 346 HOH C O   1 
HETATM 7659 O O   . HOH G 2 .   ? 12.678  -16.527 35.196  1.00 31.14 ? 347 HOH C O   1 
HETATM 7660 O O   . HOH G 2 .   ? 13.163  -30.960 31.045  1.00 42.08 ? 348 HOH C O   1 
HETATM 7661 O O   . HOH G 2 .   ? 32.775  -33.332 50.475  1.00 39.20 ? 349 HOH C O   1 
HETATM 7662 O O   . HOH G 2 .   ? -3.593  -21.421 49.746  1.00 35.62 ? 350 HOH C O   1 
HETATM 7663 O O   . HOH G 2 .   ? 0.575   -25.374 29.577  1.00 42.65 ? 351 HOH C O   1 
HETATM 7664 O O   . HOH G 2 .   ? 33.913  -26.130 41.579  1.00 30.97 ? 352 HOH C O   1 
HETATM 7665 O O   . HOH G 2 .   ? 4.287   -11.290 38.340  1.00 33.63 ? 353 HOH C O   1 
HETATM 7666 O O   . HOH G 2 .   ? 10.443  -27.629 35.558  1.00 48.00 ? 354 HOH C O   1 
HETATM 7667 O O   . HOH G 2 .   ? 4.991   -24.992 31.053  1.00 43.23 ? 355 HOH C O   1 
HETATM 7668 O O   . HOH G 2 .   ? 30.605  -42.350 36.005  1.00 32.61 ? 356 HOH C O   1 
HETATM 7669 O O   . HOH G 2 .   ? 23.625  -39.378 43.734  1.00 30.64 ? 357 HOH C O   1 
HETATM 7670 O O   . HOH G 2 .   ? 34.051  -17.962 17.607  1.00 51.60 ? 358 HOH C O   1 
HETATM 7671 O O   . HOH G 2 .   ? 33.876  -13.987 43.842  1.00 50.30 ? 359 HOH C O   1 
HETATM 7672 O O   . HOH G 2 .   ? 22.205  -19.115 49.142  1.00 35.98 ? 360 HOH C O   1 
HETATM 7673 O O   . HOH G 2 .   ? -3.804  -22.648 52.861  1.00 51.38 ? 361 HOH C O   1 
HETATM 7674 O O   . HOH G 2 .   ? 24.193  -42.231 41.840  1.00 36.50 ? 362 HOH C O   1 
HETATM 7675 O O   . HOH G 2 .   ? 14.366  -18.171 33.172  1.00 33.41 ? 363 HOH C O   1 
HETATM 7676 O O   . HOH G 2 .   ? 32.617  -20.174 26.708  1.00 37.26 ? 364 HOH C O   1 
HETATM 7677 O O   . HOH G 2 .   ? 31.816  -36.732 24.365  1.00 32.75 ? 365 HOH C O   1 
HETATM 7678 O O   . HOH G 2 .   ? 0.974   -18.116 54.755  1.00 41.37 ? 366 HOH C O   1 
HETATM 7679 O O   . HOH G 2 .   ? 7.974   -28.618 48.847  1.00 35.50 ? 367 HOH C O   1 
HETATM 7680 O O   . HOH G 2 .   ? 18.248  -44.369 34.507  1.00 45.91 ? 368 HOH C O   1 
HETATM 7681 O O   . HOH G 2 .   ? 2.364   -16.195 38.562  1.00 32.04 ? 369 HOH C O   1 
HETATM 7682 O O   . HOH G 2 .   ? 36.219  -40.171 32.592  1.00 33.10 ? 370 HOH C O   1 
HETATM 7683 O O   . HOH G 2 .   ? 30.392  -32.892 51.722  1.00 35.66 ? 371 HOH C O   1 
HETATM 7684 O O   . HOH G 2 .   ? 9.381   -26.392 48.265  1.00 38.60 ? 372 HOH C O   1 
HETATM 7685 O O   . HOH G 2 .   ? 37.083  -36.204 43.941  1.00 34.82 ? 373 HOH C O   1 
HETATM 7686 O O   . HOH G 2 .   ? 19.944  -40.648 45.785  1.00 35.68 ? 374 HOH C O   1 
HETATM 7687 O O   . HOH G 2 .   ? 23.607  -14.638 49.829  1.00 46.94 ? 375 HOH C O   1 
HETATM 7688 O O   . HOH G 2 .   ? 11.865  -26.087 29.883  1.00 34.92 ? 376 HOH C O   1 
HETATM 7689 O O   . HOH G 2 .   ? 0.955   -20.610 54.999  1.00 39.61 ? 377 HOH C O   1 
HETATM 7690 O O   . HOH G 2 .   ? 15.071  -33.801 51.011  1.00 39.21 ? 378 HOH C O   1 
HETATM 7691 O O   . HOH G 2 .   ? 38.066  -29.018 37.104  1.00 34.93 ? 379 HOH C O   1 
HETATM 7692 O O   . HOH G 2 .   ? 10.614  -8.023  50.625  1.00 39.44 ? 380 HOH C O   1 
HETATM 7693 O O   . HOH G 2 .   ? 27.240  -22.359 52.359  1.00 40.27 ? 381 HOH C O   1 
HETATM 7694 O O   . HOH G 2 .   ? 21.088  -18.166 51.745  1.00 40.30 ? 382 HOH C O   1 
HETATM 7695 O O   . HOH G 2 .   ? 34.766  -32.318 51.686  1.00 38.70 ? 383 HOH C O   1 
HETATM 7696 O O   . HOH G 2 .   ? 42.654  -27.375 30.770  1.00 40.41 ? 384 HOH C O   1 
HETATM 7697 O O   . HOH G 2 .   ? 9.551   -25.326 51.027  1.00 36.59 ? 385 HOH C O   1 
HETATM 7698 O O   . HOH G 2 .   ? 34.355  -25.615 39.652  1.00 45.54 ? 386 HOH C O   1 
HETATM 7699 O O   . HOH G 2 .   ? 19.268  -13.810 33.061  1.00 41.73 ? 387 HOH C O   1 
HETATM 7700 O O   . HOH G 2 .   ? 36.482  -27.612 38.665  1.00 35.73 ? 388 HOH C O   1 
HETATM 7701 O O   . HOH G 2 .   ? 11.478  -30.170 33.207  1.00 54.41 ? 389 HOH C O   1 
HETATM 7702 O O   . HOH G 2 .   ? 35.163  -23.230 41.621  1.00 33.40 ? 390 HOH C O   1 
HETATM 7703 O O   . HOH G 2 .   ? 34.111  -14.817 46.610  1.00 33.72 ? 391 HOH C O   1 
HETATM 7704 O O   . HOH G 2 .   ? 20.971  -17.593 47.148  1.00 35.80 ? 392 HOH C O   1 
HETATM 7705 O O   . HOH G 2 .   ? 14.475  -19.325 31.597  1.00 40.15 ? 393 HOH C O   1 
HETATM 7706 O O   . HOH G 2 .   ? 31.900  -14.458 39.924  1.00 49.50 ? 394 HOH C O   1 
HETATM 7707 O O   . HOH G 2 .   ? 15.602  -38.418 50.246  1.00 39.48 ? 395 HOH C O   1 
HETATM 7708 O O   . HOH G 2 .   ? 6.749   -24.792 26.166  1.00 50.46 ? 396 HOH C O   1 
HETATM 7709 O O   . HOH G 2 .   ? 28.546  -20.768 50.781  1.00 48.77 ? 397 HOH C O   1 
HETATM 7710 O O   . HOH H 2 .   ? 8.501   -34.332 -9.234  1.00 36.75 ? 301 HOH D O   1 
HETATM 7711 O O   . HOH H 2 .   ? 18.816  -20.754 7.189   1.00 36.77 ? 302 HOH D O   1 
HETATM 7712 O O   . HOH H 2 .   ? -10.395 -26.237 -2.722  1.00 44.61 ? 303 HOH D O   1 
HETATM 7713 O O   . HOH H 2 .   ? 15.400  -39.061 -0.592  1.00 53.33 ? 304 HOH D O   1 
HETATM 7714 O O   . HOH H 2 .   ? 42.257  -10.625 -12.633 1.00 44.71 ? 305 HOH D O   1 
HETATM 7715 O O   . HOH H 2 .   ? 41.746  -23.776 -20.906 1.00 48.13 ? 306 HOH D O   1 
HETATM 7716 O O   . HOH H 2 .   ? 26.627  -14.386 -20.121 1.00 42.10 ? 307 HOH D O   1 
HETATM 7717 O O   . HOH H 2 .   ? 20.460  -2.434  1.016   1.00 31.22 ? 308 HOH D O   1 
HETATM 7718 O O   . HOH H 2 .   ? 8.670   -23.376 -8.789  1.00 29.54 ? 309 HOH D O   1 
HETATM 7719 O O   . HOH H 2 .   ? -6.622  -23.311 7.700   1.00 44.02 ? 310 HOH D O   1 
HETATM 7720 O O   . HOH H 2 .   ? 39.817  -16.138 1.631   1.00 43.37 ? 311 HOH D O   1 
HETATM 7721 O O   . HOH H 2 .   ? 34.350  -30.609 -9.323  1.00 30.04 ? 312 HOH D O   1 
HETATM 7722 O O   . HOH H 2 .   ? 20.091  -18.254 -1.545  1.00 21.45 ? 313 HOH D O   1 
HETATM 7723 O O   . HOH H 2 .   ? 32.608  -10.264 -8.673  1.00 31.14 ? 314 HOH D O   1 
HETATM 7724 O O   . HOH H 2 .   ? 5.369   -7.961  -5.703  1.00 36.92 ? 315 HOH D O   1 
HETATM 7725 O O   . HOH H 2 .   ? 30.392  -16.525 -14.527 1.00 31.10 ? 316 HOH D O   1 
HETATM 7726 O O   . HOH H 2 .   ? 20.112  -30.764 -25.880 1.00 49.80 ? 317 HOH D O   1 
HETATM 7727 O O   . HOH H 2 .   ? -9.296  -29.721 -1.605  1.00 32.44 ? 318 HOH D O   1 
HETATM 7728 O O   . HOH H 2 .   ? 19.491  -13.559 9.795   1.00 48.08 ? 319 HOH D O   1 
HETATM 7729 O O   . HOH H 2 .   ? -2.927  -15.222 -10.070 1.00 38.68 ? 320 HOH D O   1 
HETATM 7730 O O   . HOH H 2 .   ? 18.467  -15.205 4.580   1.00 30.00 ? 321 HOH D O   1 
HETATM 7731 O O   . HOH H 2 .   ? 37.137  -29.976 -16.887 1.00 30.14 ? 322 HOH D O   1 
HETATM 7732 O O   . HOH H 2 .   ? 33.202  -22.045 -0.835  1.00 23.96 ? 323 HOH D O   1 
HETATM 7733 O O   . HOH H 2 .   ? 30.668  -19.579 -23.171 1.00 40.70 ? 324 HOH D O   1 
HETATM 7734 O O   . HOH H 2 .   ? 3.931   -33.271 -0.688  1.00 33.08 ? 325 HOH D O   1 
HETATM 7735 O O   . HOH H 2 .   ? 14.063  -13.297 -8.756  1.00 29.75 ? 326 HOH D O   1 
HETATM 7736 O O   . HOH H 2 .   ? -10.939 -23.284 6.170   1.00 35.71 ? 327 HOH D O   1 
HETATM 7737 O O   . HOH H 2 .   ? 20.626  -10.978 -15.447 1.00 41.99 ? 328 HOH D O   1 
HETATM 7738 O O   . HOH H 2 .   ? 42.704  -22.448 -11.326 1.00 39.10 ? 329 HOH D O   1 
HETATM 7739 O O   . HOH H 2 .   ? 12.381  -16.020 -10.065 1.00 28.85 ? 330 HOH D O   1 
HETATM 7740 O O   . HOH H 2 .   ? 29.491  -14.592 3.523   1.00 46.47 ? 331 HOH D O   1 
HETATM 7741 O O   . HOH H 2 .   ? 42.340  -23.842 -8.022  1.00 40.50 ? 332 HOH D O   1 
HETATM 7742 O O   . HOH H 2 .   ? 16.222  -21.662 6.719   1.00 30.59 ? 333 HOH D O   1 
HETATM 7743 O O   . HOH H 2 .   ? 12.543  -27.559 -8.509  1.00 35.02 ? 334 HOH D O   1 
HETATM 7744 O O   . HOH H 2 .   ? 35.267  -13.422 6.644   1.00 43.67 ? 335 HOH D O   1 
HETATM 7745 O O   . HOH H 2 .   ? 19.768  -10.421 -3.299  1.00 32.12 ? 336 HOH D O   1 
HETATM 7746 O O   . HOH H 2 .   ? 25.146  -36.055 -0.159  1.00 28.73 ? 337 HOH D O   1 
HETATM 7747 O O   . HOH H 2 .   ? 28.417  -18.638 8.249   1.00 41.08 ? 338 HOH D O   1 
HETATM 7748 O O   . HOH H 2 .   ? 21.333  -16.439 1.897   1.00 23.44 ? 339 HOH D O   1 
HETATM 7749 O O   . HOH H 2 .   ? 14.883  -40.492 1.980   1.00 54.07 ? 340 HOH D O   1 
HETATM 7750 O O   . HOH H 2 .   ? 18.799  -28.150 -24.052 1.00 48.17 ? 341 HOH D O   1 
HETATM 7751 O O   . HOH H 2 .   ? 31.805  -38.997 -7.789  1.00 35.19 ? 342 HOH D O   1 
HETATM 7752 O O   . HOH H 2 .   ? 1.524   -21.916 -14.122 1.00 42.44 ? 343 HOH D O   1 
HETATM 7753 O O   . HOH H 2 .   ? 9.178   -9.473  -0.937  1.00 33.11 ? 344 HOH D O   1 
HETATM 7754 O O   . HOH H 2 .   ? 6.080   -21.420 -12.310 1.00 37.18 ? 345 HOH D O   1 
HETATM 7755 O O   . HOH H 2 .   ? 24.090  -24.855 9.693   1.00 32.82 ? 346 HOH D O   1 
HETATM 7756 O O   . HOH H 2 .   ? -2.241  -17.981 5.603   1.00 35.32 ? 347 HOH D O   1 
HETATM 7757 O O   . HOH H 2 .   ? 14.767  -27.678 -12.670 1.00 40.75 ? 348 HOH D O   1 
HETATM 7758 O O   . HOH H 2 .   ? 20.193  -13.047 4.107   1.00 43.54 ? 349 HOH D O   1 
HETATM 7759 O O   . HOH H 2 .   ? 29.038  -34.607 7.883   1.00 35.66 ? 350 HOH D O   1 
HETATM 7760 O O   . HOH H 2 .   ? 34.523  -17.112 -5.522  1.00 38.76 ? 351 HOH D O   1 
HETATM 7761 O O   . HOH H 2 .   ? 10.840  -27.358 3.266   1.00 30.04 ? 352 HOH D O   1 
HETATM 7762 O O   . HOH H 2 .   ? 38.368  -32.741 0.026   1.00 27.96 ? 353 HOH D O   1 
HETATM 7763 O O   . HOH H 2 .   ? 28.913  -16.029 4.471   1.00 37.12 ? 354 HOH D O   1 
HETATM 7764 O O   . HOH H 2 .   ? 11.879  -22.856 1.375   1.00 26.01 ? 355 HOH D O   1 
HETATM 7765 O O   . HOH H 2 .   ? 15.515  -33.967 4.255   1.00 32.41 ? 356 HOH D O   1 
HETATM 7766 O O   . HOH H 2 .   ? 7.633   -16.885 5.538   1.00 30.87 ? 357 HOH D O   1 
HETATM 7767 O O   . HOH H 2 .   ? 16.618  -23.623 8.753   1.00 36.46 ? 358 HOH D O   1 
HETATM 7768 O O   . HOH H 2 .   ? 11.099  -20.517 0.253   1.00 22.33 ? 359 HOH D O   1 
HETATM 7769 O O   . HOH H 2 .   ? 11.195  -21.503 -2.634  1.00 26.83 ? 360 HOH D O   1 
HETATM 7770 O O   . HOH H 2 .   ? 26.598  -39.142 -14.540 1.00 36.80 ? 361 HOH D O   1 
HETATM 7771 O O   . HOH H 2 .   ? 4.447   -9.871  -2.990  1.00 27.78 ? 362 HOH D O   1 
HETATM 7772 O O   . HOH H 2 .   ? 36.941  -16.158 -17.415 1.00 40.76 ? 363 HOH D O   1 
HETATM 7773 O O   . HOH H 2 .   ? -2.221  -19.398 9.152   1.00 45.73 ? 364 HOH D O   1 
HETATM 7774 O O   . HOH H 2 .   ? 29.122  -36.712 6.878   1.00 31.27 ? 365 HOH D O   1 
HETATM 7775 O O   . HOH H 2 .   ? 13.407  -23.917 5.075   1.00 33.27 ? 366 HOH D O   1 
HETATM 7776 O O   . HOH H 2 .   ? 24.076  -13.269 -19.609 1.00 48.70 ? 367 HOH D O   1 
HETATM 7777 O O   . HOH H 2 .   ? 8.714   -22.834 -15.393 1.00 45.97 ? 368 HOH D O   1 
HETATM 7778 O O   . HOH H 2 .   ? 37.646  -36.741 -11.262 1.00 35.72 ? 369 HOH D O   1 
HETATM 7779 O O   . HOH H 2 .   ? 40.517  -16.034 -16.224 1.00 36.84 ? 370 HOH D O   1 
HETATM 7780 O O   . HOH H 2 .   ? 34.074  -16.814 -17.222 1.00 37.56 ? 371 HOH D O   1 
HETATM 7781 O O   . HOH H 2 .   ? 25.791  -39.159 -2.447  1.00 37.31 ? 372 HOH D O   1 
HETATM 7782 O O   . HOH H 2 .   ? 31.786  -29.446 7.899   1.00 31.39 ? 373 HOH D O   1 
HETATM 7783 O O   . HOH H 2 .   ? 3.660   -12.910 -5.526  1.00 34.36 ? 374 HOH D O   1 
HETATM 7784 O O   . HOH H 2 .   ? 29.029  -28.195 11.094  1.00 39.14 ? 375 HOH D O   1 
HETATM 7785 O O   . HOH H 2 .   ? 10.745  -23.070 4.064   1.00 36.38 ? 376 HOH D O   1 
HETATM 7786 O O   . HOH H 2 .   ? 37.215  -24.604 -21.100 1.00 41.83 ? 377 HOH D O   1 
HETATM 7787 O O   . HOH H 2 .   ? 9.451   -25.229 5.240   1.00 37.55 ? 378 HOH D O   1 
HETATM 7788 O O   . HOH H 2 .   ? 35.499  -22.644 -2.450  1.00 26.40 ? 379 HOH D O   1 
HETATM 7789 O O   . HOH H 2 .   ? 23.316  -15.745 5.272   1.00 30.07 ? 380 HOH D O   1 
HETATM 7790 O O   . HOH H 2 .   ? 32.258  -39.761 -11.635 1.00 49.33 ? 381 HOH D O   1 
HETATM 7791 O O   . HOH H 2 .   ? 0.083   -32.746 -9.609  1.00 49.58 ? 382 HOH D O   1 
HETATM 7792 O O   . HOH H 2 .   ? 29.409  -27.025 -26.606 1.00 43.83 ? 383 HOH D O   1 
HETATM 7793 O O   . HOH H 2 .   ? 2.392   -17.467 11.063  1.00 37.34 ? 384 HOH D O   1 
HETATM 7794 O O   . HOH H 2 .   ? -12.588 -22.966 1.102   1.00 38.89 ? 385 HOH D O   1 
HETATM 7795 O O   . HOH H 2 .   ? 3.901   -9.011  0.799   1.00 35.63 ? 386 HOH D O   1 
HETATM 7796 O O   . HOH H 2 .   ? 15.960  -16.845 9.315   1.00 38.35 ? 387 HOH D O   1 
HETATM 7797 O O   . HOH H 2 .   ? 36.572  -15.735 -5.394  1.00 37.68 ? 388 HOH D O   1 
HETATM 7798 O O   . HOH H 2 .   ? 44.149  -24.028 -13.149 1.00 38.03 ? 389 HOH D O   1 
HETATM 7799 O O   . HOH H 2 .   ? 35.990  -29.003 7.763   1.00 36.94 ? 390 HOH D O   1 
HETATM 7800 O O   . HOH H 2 .   ? 13.392  -25.783 6.657   1.00 42.04 ? 391 HOH D O   1 
HETATM 7801 O O   . HOH H 2 .   ? 39.512  -25.658 -6.773  1.00 33.02 ? 392 HOH D O   1 
HETATM 7802 O O   . HOH H 2 .   ? 5.758   -7.346  7.091   1.00 53.46 ? 393 HOH D O   1 
HETATM 7803 O O   . HOH H 2 .   ? 15.808  -38.359 -3.975  1.00 51.45 ? 394 HOH D O   1 
HETATM 7804 O O   . HOH H 2 .   ? 20.742  -10.540 -10.654 1.00 32.78 ? 395 HOH D O   1 
HETATM 7805 O O   . HOH H 2 .   ? 9.694   -25.188 7.719   1.00 45.32 ? 396 HOH D O   1 
HETATM 7806 O O   . HOH H 2 .   ? -2.575  -30.589 1.268   1.00 43.61 ? 397 HOH D O   1 
HETATM 7807 O O   . HOH H 2 .   ? 37.825  -24.248 -5.092  1.00 36.36 ? 398 HOH D O   1 
HETATM 7808 O O   . HOH H 2 .   ? 27.993  -7.909  -16.845 1.00 42.36 ? 399 HOH D O   1 
HETATM 7809 O O   . HOH H 2 .   ? 15.402  -38.867 -6.100  1.00 44.36 ? 400 HOH D O   1 
HETATM 7810 O O   . HOH H 2 .   ? 36.075  -38.926 -6.857  1.00 36.58 ? 401 HOH D O   1 
HETATM 7811 O O   . HOH H 2 .   ? 4.134   -8.167  2.604   1.00 43.11 ? 402 HOH D O   1 
HETATM 7812 O O   . HOH H 2 .   ? 8.280   -8.855  -3.182  1.00 37.03 ? 403 HOH D O   1 
HETATM 7813 O O   . HOH H 2 .   ? 12.628  -27.043 -11.227 1.00 45.77 ? 404 HOH D O   1 
HETATM 7814 O O   . HOH H 2 .   ? 5.605   -7.820  4.714   1.00 45.93 ? 405 HOH D O   1 
HETATM 7815 O O   . HOH H 2 .   ? 38.798  -21.594 -3.716  1.00 43.88 ? 406 HOH D O   1 
HETATM 7816 O O   . HOH H 2 .   ? 22.142  -14.630 3.318   1.00 31.29 ? 407 HOH D O   1 
HETATM 7817 O O   . HOH H 2 .   ? -0.671  -32.611 -6.313  1.00 44.11 ? 408 HOH D O   1 
HETATM 7818 O O   . HOH H 2 .   ? 38.678  -36.331 -8.692  1.00 38.12 ? 409 HOH D O   1 
HETATM 7819 O O   . HOH H 2 .   ? 32.675  -11.151 -4.161  1.00 44.12 ? 410 HOH D O   1 
HETATM 7820 O O   . HOH H 2 .   ? 41.346  -22.764 -23.189 1.00 50.90 ? 411 HOH D O   1 
HETATM 7821 O O   . HOH H 2 .   ? -1.582  -33.097 -8.627  1.00 49.46 ? 412 HOH D O   1 
HETATM 7822 O O   . HOH H 2 .   ? 39.541  -19.287 -3.897  1.00 50.78 ? 413 HOH D O   1 
HETATM 7823 O O   . HOH H 2 .   ? 22.290  -14.696 7.858   1.00 43.19 ? 414 HOH D O   1 
HETATM 7824 O O   . HOH H 2 .   ? 16.871  -35.247 6.243   1.00 37.34 ? 415 HOH D O   1 
# 
