data_9BWQ
# 
_entry.id   9BWQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BWQ         pdb_00009bwq 10.2210/pdb9bwq/pdb 
WWPDB D_1000284286 ?            ?                   
# 
_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       2025-03-12 
_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                        9BWQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9BVY 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gborgstahl@unmc.edu 
_pdbx_contact_author.name_first         Gloria 
_pdbx_contact_author.name_last          Borgstahl 
_pdbx_contact_author.name_mi            E.O. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8070-0258 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Azadmanesh, J.'    1  0000-0002-3615-7785 
'Slobodnik, K.'     2  0009-0004-0951-5315 
'Struble, L.R.'     3  0000-0002-0671-259X 
'Cone, E.A.'        4  0000-0002-7407-7743 
'Dasgupta, M.'      5  0000-0003-2509-3699 
'Lutz, W.E.'        6  0000-0002-7248-4994 
'Kumar, S.'         7  0000-0002-6794-2794 
'Natarajan, A.'     8  0000-0001-5067-0203 
'Coates, L.'        9  0000-0003-2342-049X 
'Weiss, K.L.'       10 0000-0002-6486-8007 
'Myles, D.A.A.'     11 0000-0002-7693-4964 
'Kroll, T.'         12 0000-0003-2176-6905 
'Borgstahl, G.E.O.' 13 0000-0001-8070-0258 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1887 
_citation.page_last                 1887 
_citation.title                     
'The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57180-3 
_citation.pdbx_database_id_PubMed   39987263 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Azadmanesh, J.'    1  0000-0002-3615-7785 
primary 'Slobodnik, K.'     2  0009-0004-0951-5315 
primary 'Struble, L.R.'     3  ?                   
primary 'Lovelace, J.J.'    4  ?                   
primary 'Cone, E.A.'        5  ?                   
primary 'Dasgupta, M.'      6  0000-0003-2509-3699 
primary 'Lutz, W.E.'        7  ?                   
primary 'Kumar, S.'         8  ?                   
primary 'Natarajan, A.'     9  0000-0001-5067-0203 
primary 'Coates, L.'        10 0000-0003-2342-049X 
primary 'Weiss, K.L.'       11 0000-0002-6486-8007 
primary 'Myles, D.A.A.'     12 0000-0002-7693-4964 
primary 'Kroll, T.'         13 ?                   
primary 'Borgstahl, G.E.O.' 14 0000-0001-8070-0258 
# 
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 'Superoxide dismutase [Mn], mitochondrial' 22348.307 2   1.15.1.1 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                       54.938    2   ?        ? ? ? 
3 non-polymer syn 'HYDROGEN PEROXIDE'                        34.015    1   ?        ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'                            94.971    3   ?        ? ? ? 
5 non-polymer syn 'POTASSIUM ION'                            39.098    1   ?        ? ? ? 
6 water       nat water                                      18.015    571 ?        ? ? ? 
# 
_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       
;MKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWT
NLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGID
VWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWT
NLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGID
VWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN  
3 'HYDROGEN PEROXIDE'  PEO 
4 'PHOSPHATE ION'      PO4 
5 'POTASSIUM ION'      K   
6 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   HIS n 
1 4   SER n 
1 5   LEU n 
1 6   PRO n 
1 7   ASP n 
1 8   LEU n 
1 9   PRO n 
1 10  TYR n 
1 11  ASP n 
1 12  TYR n 
1 13  GLY n 
1 14  ALA n 
1 15  LEU n 
1 16  GLU n 
1 17  PRO n 
1 18  HIS n 
1 19  ILE n 
1 20  ASN n 
1 21  ALA n 
1 22  GLN n 
1 23  ILE n 
1 24  MET n 
1 25  GLN n 
1 26  LEU n 
1 27  HIS n 
1 28  HIS n 
1 29  SER n 
1 30  LYS n 
1 31  HIS n 
1 32  HIS n 
1 33  ALA n 
1 34  ALA n 
1 35  PHE n 
1 36  VAL n 
1 37  ASN n 
1 38  ASN n 
1 39  LEU n 
1 40  ASN n 
1 41  VAL n 
1 42  THR n 
1 43  GLU n 
1 44  GLU n 
1 45  LYS n 
1 46  TYR n 
1 47  GLN n 
1 48  GLU n 
1 49  ALA n 
1 50  LEU n 
1 51  ALA n 
1 52  LYS n 
1 53  GLY n 
1 54  ASP n 
1 55  VAL n 
1 56  THR n 
1 57  ALA n 
1 58  GLN n 
1 59  ILE n 
1 60  ALA n 
1 61  LEU n 
1 62  GLN n 
1 63  PRO n 
1 64  ALA n 
1 65  LEU n 
1 66  LYS n 
1 67  PHE n 
1 68  ASN n 
1 69  GLY n 
1 70  GLY n 
1 71  GLY n 
1 72  HIS n 
1 73  ILE n 
1 74  ASN n 
1 75  HIS n 
1 76  SER n 
1 77  ILE n 
1 78  PHE n 
1 79  TRP n 
1 80  THR n 
1 81  ASN n 
1 82  LEU n 
1 83  SER n 
1 84  PRO n 
1 85  ASN n 
1 86  GLY n 
1 87  GLY n 
1 88  GLY n 
1 89  GLU n 
1 90  PRO n 
1 91  LYS n 
1 92  GLY n 
1 93  GLU n 
1 94  LEU n 
1 95  LEU n 
1 96  GLU n 
1 97  ALA n 
1 98  ILE n 
1 99  LYS n 
1 100 ARG n 
1 101 ASP n 
1 102 PHE n 
1 103 GLY n 
1 104 SER n 
1 105 PHE n 
1 106 ASP n 
1 107 LYS n 
1 108 PHE n 
1 109 LYS n 
1 110 GLU n 
1 111 LYS n 
1 112 LEU n 
1 113 THR n 
1 114 ALA n 
1 115 ALA n 
1 116 SER n 
1 117 VAL n 
1 118 GLY n 
1 119 VAL n 
1 120 GLN n 
1 121 GLY n 
1 122 SER n 
1 123 GLY n 
1 124 TRP n 
1 125 GLY n 
1 126 TRP n 
1 127 LEU n 
1 128 GLY n 
1 129 PHE n 
1 130 ASN n 
1 131 LYS n 
1 132 GLU n 
1 133 ARG n 
1 134 GLY n 
1 135 HIS n 
1 136 LEU n 
1 137 GLN n 
1 138 ILE n 
1 139 ALA n 
1 140 ALA n 
1 141 CYS n 
1 142 PRO n 
1 143 ASN n 
1 144 GLN n 
1 145 ASP n 
1 146 PRO n 
1 147 LEU n 
1 148 GLN n 
1 149 GLY n 
1 150 THR n 
1 151 THR n 
1 152 GLY n 
1 153 LEU n 
1 154 ILE n 
1 155 PRO n 
1 156 LEU n 
1 157 LEU n 
1 158 GLY n 
1 159 ILE n 
1 160 ASP n 
1 161 VAL n 
1 162 TRP n 
1 163 GLU n 
1 164 HIS n 
1 165 ALA n 
1 166 TYR n 
1 167 TYR n 
1 168 LEU n 
1 169 GLN n 
1 170 TYR n 
1 171 LYS n 
1 172 ASN n 
1 173 VAL n 
1 174 ARG n 
1 175 PRO n 
1 176 ASP n 
1 177 TYR n 
1 178 LEU n 
1 179 LYS n 
1 180 ALA n 
1 181 ILE n 
1 182 TRP n 
1 183 ASN n 
1 184 VAL n 
1 185 ILE n 
1 186 ASN n 
1 187 TRP n 
1 188 GLU n 
1 189 ASN n 
1 190 VAL n 
1 191 THR n 
1 192 GLU n 
1 193 ARG n 
1 194 TYR n 
1 195 MET n 
1 196 ALA n 
1 197 CYS n 
1 198 LYS n 
1 199 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   199 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD2 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
K   non-polymer         . 'POTASSIUM ION'      ? 'K 1'            39.098  
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 
MN  non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'           54.938  
PEO non-polymer         . 'HYDROGEN PEROXIDE'  ? 'H2 O2'          34.015  
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'      ? 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
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   0   0   MET MET A . n 
A 1 2   LYS 2   1   1   LYS LYS A . n 
A 1 3   HIS 3   2   2   HIS HIS A . n 
A 1 4   SER 4   3   3   SER SER A . n 
A 1 5   LEU 5   4   4   LEU LEU A . n 
A 1 6   PRO 6   5   5   PRO PRO A . n 
A 1 7   ASP 7   6   6   ASP ASP A . n 
A 1 8   LEU 8   7   7   LEU LEU A . n 
A 1 9   PRO 9   8   8   PRO PRO A . n 
A 1 10  TYR 10  9   9   TYR TYR A . n 
A 1 11  ASP 11  10  10  ASP ASP A . n 
A 1 12  TYR 12  11  11  TYR TYR A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  ALA 14  13  13  ALA ALA A . n 
A 1 15  LEU 15  14  14  LEU LEU A . n 
A 1 16  GLU 16  15  15  GLU GLU A . n 
A 1 17  PRO 17  16  16  PRO PRO A . n 
A 1 18  HIS 18  17  17  HIS HIS A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  ALA 21  20  20  ALA ALA A . n 
A 1 22  GLN 22  21  21  GLN GLN A . n 
A 1 23  ILE 23  22  22  ILE ILE A . n 
A 1 24  MET 24  23  23  MET MET A . n 
A 1 25  GLN 25  24  24  GLN GLN A . n 
A 1 26  LEU 26  25  25  LEU LEU A . n 
A 1 27  HIS 27  26  26  HIS HIS A . n 
A 1 28  HIS 28  27  27  HIS HIS A . n 
A 1 29  SER 29  28  28  SER SER A . n 
A 1 30  LYS 30  29  29  LYS LYS A . n 
A 1 31  HIS 31  30  30  HIS HIS A . n 
A 1 32  HIS 32  31  31  HIS HIS A . n 
A 1 33  ALA 33  32  32  ALA ALA A . n 
A 1 34  ALA 34  33  33  ALA ALA A . n 
A 1 35  PHE 35  34  34  PHE PHE A . n 
A 1 36  VAL 36  35  35  VAL VAL A . n 
A 1 37  ASN 37  36  36  ASN ASN A . n 
A 1 38  ASN 38  37  37  ASN ASN A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  ASN 40  39  39  ASN ASN A . n 
A 1 41  VAL 41  40  40  VAL VAL A . n 
A 1 42  THR 42  41  41  THR THR A . n 
A 1 43  GLU 43  42  42  GLU GLU A . n 
A 1 44  GLU 44  43  43  GLU GLU A . n 
A 1 45  LYS 45  44  44  LYS LYS A . n 
A 1 46  TYR 46  45  45  TYR TYR A . n 
A 1 47  GLN 47  46  46  GLN GLN A . n 
A 1 48  GLU 48  47  47  GLU GLU A . n 
A 1 49  ALA 49  48  48  ALA ALA A . n 
A 1 50  LEU 50  49  49  LEU LEU A . n 
A 1 51  ALA 51  50  50  ALA ALA A . n 
A 1 52  LYS 52  51  51  LYS LYS A . n 
A 1 53  GLY 53  52  52  GLY GLY A . n 
A 1 54  ASP 54  53  53  ASP ASP A . n 
A 1 55  VAL 55  54  54  VAL VAL A . n 
A 1 56  THR 56  55  55  THR THR A . n 
A 1 57  ALA 57  56  56  ALA ALA A . n 
A 1 58  GLN 58  57  57  GLN GLN A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  LEU 61  60  60  LEU LEU A . n 
A 1 62  GLN 62  61  61  GLN GLN A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  ALA 64  63  63  ALA ALA A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  LYS 66  65  65  LYS LYS A . n 
A 1 67  PHE 67  66  66  PHE PHE A . n 
A 1 68  ASN 68  67  67  ASN ASN A . n 
A 1 69  GLY 69  68  68  GLY GLY A . n 
A 1 70  GLY 70  69  69  GLY GLY A . n 
A 1 71  GLY 71  70  70  GLY GLY A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  ILE 73  72  72  ILE ILE A . n 
A 1 74  ASN 74  73  73  ASN ASN A . n 
A 1 75  HIS 75  74  74  HIS HIS A . n 
A 1 76  SER 76  75  75  SER SER A . n 
A 1 77  ILE 77  76  76  ILE ILE A . n 
A 1 78  PHE 78  77  77  PHE PHE A . n 
A 1 79  TRP 79  78  78  TRP TRP A . n 
A 1 80  THR 80  79  79  THR THR A . n 
A 1 81  ASN 81  80  80  ASN ASN A . n 
A 1 82  LEU 82  81  81  LEU LEU A . n 
A 1 83  SER 83  82  82  SER SER A . n 
A 1 84  PRO 84  83  83  PRO PRO A . n 
A 1 85  ASN 85  84  84  ASN ASN A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  GLY 87  86  86  GLY GLY A . n 
A 1 88  GLY 88  87  87  GLY GLY A . n 
A 1 89  GLU 89  88  88  GLU GLU A . n 
A 1 90  PRO 90  89  89  PRO PRO A . n 
A 1 91  LYS 91  90  90  LYS LYS A . n 
A 1 92  GLY 92  91  91  GLY GLY A . n 
A 1 93  GLU 93  92  92  GLU GLU A . n 
A 1 94  LEU 94  93  93  LEU LEU A . n 
A 1 95  LEU 95  94  94  LEU LEU A . n 
A 1 96  GLU 96  95  95  GLU GLU A . n 
A 1 97  ALA 97  96  96  ALA ALA A . n 
A 1 98  ILE 98  97  97  ILE ILE A . n 
A 1 99  LYS 99  98  98  LYS LYS A . n 
A 1 100 ARG 100 99  99  ARG ARG A . n 
A 1 101 ASP 101 100 100 ASP ASP A . n 
A 1 102 PHE 102 101 101 PHE PHE A . n 
A 1 103 GLY 103 102 102 GLY GLY A . n 
A 1 104 SER 104 103 103 SER SER A . n 
A 1 105 PHE 105 104 104 PHE PHE A . n 
A 1 106 ASP 106 105 105 ASP ASP A . n 
A 1 107 LYS 107 106 106 LYS LYS A . n 
A 1 108 PHE 108 107 107 PHE PHE A . n 
A 1 109 LYS 109 108 108 LYS LYS A . n 
A 1 110 GLU 110 109 109 GLU GLU A . n 
A 1 111 LYS 111 110 110 LYS LYS A . n 
A 1 112 LEU 112 111 111 LEU LEU A . n 
A 1 113 THR 113 112 112 THR THR A . n 
A 1 114 ALA 114 113 113 ALA ALA A . n 
A 1 115 ALA 115 114 114 ALA ALA A . n 
A 1 116 SER 116 115 115 SER SER A . n 
A 1 117 VAL 117 116 116 VAL VAL A . n 
A 1 118 GLY 118 117 117 GLY GLY A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 GLN 120 119 119 GLN GLN A . n 
A 1 121 GLY 121 120 120 GLY GLY A . n 
A 1 122 SER 122 121 121 SER SER A . n 
A 1 123 GLY 123 122 122 GLY GLY A . n 
A 1 124 TRP 124 123 123 TRP TRP A . n 
A 1 125 GLY 125 124 124 GLY GLY A . n 
A 1 126 TRP 126 125 125 TRP TRP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 PHE 129 128 128 PHE PHE A . n 
A 1 130 ASN 130 129 129 ASN ASN A . n 
A 1 131 LYS 131 130 130 LYS LYS A . n 
A 1 132 GLU 132 131 131 GLU GLU A . n 
A 1 133 ARG 133 132 132 ARG ARG A . n 
A 1 134 GLY 134 133 133 GLY GLY A . n 
A 1 135 HIS 135 134 134 HIS HIS A . n 
A 1 136 LEU 136 135 135 LEU LEU A . n 
A 1 137 GLN 137 136 136 GLN GLN A . n 
A 1 138 ILE 138 137 137 ILE ILE A . n 
A 1 139 ALA 139 138 138 ALA ALA A . n 
A 1 140 ALA 140 139 139 ALA ALA A . n 
A 1 141 CYS 141 140 140 CYS CYS A . n 
A 1 142 PRO 142 141 141 PRO PRO A . n 
A 1 143 ASN 143 142 142 ASN ASN A . n 
A 1 144 GLN 144 143 143 GLN GLN A . n 
A 1 145 ASP 145 144 144 ASP ASP A . n 
A 1 146 PRO 146 145 145 PRO PRO A . n 
A 1 147 LEU 147 146 146 LEU LEU A . n 
A 1 148 GLN 148 147 147 GLN GLN A . n 
A 1 149 GLY 149 148 148 GLY GLY A . n 
A 1 150 THR 150 149 149 THR THR A . n 
A 1 151 THR 151 150 150 THR THR A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 LEU 153 152 152 LEU LEU A . n 
A 1 154 ILE 154 153 153 ILE ILE A . n 
A 1 155 PRO 155 154 154 PRO PRO A . n 
A 1 156 LEU 156 155 155 LEU LEU A . n 
A 1 157 LEU 157 156 156 LEU LEU A . n 
A 1 158 GLY 158 157 157 GLY GLY A . n 
A 1 159 ILE 159 158 158 ILE ILE A . n 
A 1 160 ASP 160 159 159 ASP ASP A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 TRP 162 161 161 TRP TRP A . n 
A 1 163 GLU 163 162 162 GLU GLU A . n 
A 1 164 HIS 164 163 163 HIS HIS A . n 
A 1 165 ALA 165 164 164 ALA ALA A . n 
A 1 166 TYR 166 165 165 TYR TYR A . n 
A 1 167 TYR 167 166 166 TYR TYR A . n 
A 1 168 LEU 168 167 167 LEU LEU A . n 
A 1 169 GLN 169 168 168 GLN GLN A . n 
A 1 170 TYR 170 169 169 TYR TYR A . n 
A 1 171 LYS 171 170 170 LYS LYS A . n 
A 1 172 ASN 172 171 171 ASN ASN A . n 
A 1 173 VAL 173 172 172 VAL VAL A . n 
A 1 174 ARG 174 173 173 ARG ARG A . n 
A 1 175 PRO 175 174 174 PRO PRO A . n 
A 1 176 ASP 176 175 175 ASP ASP A . n 
A 1 177 TYR 177 176 176 TYR TYR A . n 
A 1 178 LEU 178 177 177 LEU LEU A . n 
A 1 179 LYS 179 178 178 LYS LYS A . n 
A 1 180 ALA 180 179 179 ALA ALA A . n 
A 1 181 ILE 181 180 180 ILE ILE A . n 
A 1 182 TRP 182 181 181 TRP TRP A . n 
A 1 183 ASN 183 182 182 ASN ASN A . n 
A 1 184 VAL 184 183 183 VAL VAL A . n 
A 1 185 ILE 185 184 184 ILE ILE A . n 
A 1 186 ASN 186 185 185 ASN ASN A . n 
A 1 187 TRP 187 186 186 TRP TRP A . n 
A 1 188 GLU 188 187 187 GLU GLU A . n 
A 1 189 ASN 189 188 188 ASN ASN A . n 
A 1 190 VAL 190 189 189 VAL VAL A . n 
A 1 191 THR 191 190 190 THR THR A . n 
A 1 192 GLU 192 191 191 GLU GLU A . n 
A 1 193 ARG 193 192 192 ARG ARG A . n 
A 1 194 TYR 194 193 193 TYR TYR A . n 
A 1 195 MET 195 194 194 MET MET A . n 
A 1 196 ALA 196 195 195 ALA ALA A . n 
A 1 197 CYS 197 196 196 CYS CYS A . n 
A 1 198 LYS 198 197 197 LYS LYS A . n 
A 1 199 LYS 199 198 198 LYS LYS A . n 
B 1 1   MET 1   0   0   MET MET B . n 
B 1 2   LYS 2   1   1   LYS LYS B . n 
B 1 3   HIS 3   2   2   HIS HIS B . n 
B 1 4   SER 4   3   3   SER SER B . n 
B 1 5   LEU 5   4   4   LEU LEU B . n 
B 1 6   PRO 6   5   5   PRO PRO B . n 
B 1 7   ASP 7   6   6   ASP ASP B . n 
B 1 8   LEU 8   7   7   LEU LEU B . n 
B 1 9   PRO 9   8   8   PRO PRO B . n 
B 1 10  TYR 10  9   9   TYR TYR B . n 
B 1 11  ASP 11  10  10  ASP ASP B . n 
B 1 12  TYR 12  11  11  TYR TYR B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  ALA 14  13  13  ALA ALA B . n 
B 1 15  LEU 15  14  14  LEU LEU B . n 
B 1 16  GLU 16  15  15  GLU GLU B . n 
B 1 17  PRO 17  16  16  PRO PRO B . n 
B 1 18  HIS 18  17  17  HIS HIS B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  ALA 21  20  20  ALA ALA B . n 
B 1 22  GLN 22  21  21  GLN GLN B . n 
B 1 23  ILE 23  22  22  ILE ILE B . n 
B 1 24  MET 24  23  23  MET MET B . n 
B 1 25  GLN 25  24  24  GLN GLN B . n 
B 1 26  LEU 26  25  25  LEU LEU B . n 
B 1 27  HIS 27  26  26  HIS HIS B . n 
B 1 28  HIS 28  27  27  HIS HIS B . n 
B 1 29  SER 29  28  28  SER SER B . n 
B 1 30  LYS 30  29  29  LYS LYS B . n 
B 1 31  HIS 31  30  30  HIS HIS B . n 
B 1 32  HIS 32  31  31  HIS HIS B . n 
B 1 33  ALA 33  32  32  ALA ALA B . n 
B 1 34  ALA 34  33  33  ALA ALA B . n 
B 1 35  PHE 35  34  34  PHE PHE B . n 
B 1 36  VAL 36  35  35  VAL VAL B . n 
B 1 37  ASN 37  36  36  ASN ASN B . n 
B 1 38  ASN 38  37  37  ASN ASN B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  ASN 40  39  39  ASN ASN B . n 
B 1 41  VAL 41  40  40  VAL VAL B . n 
B 1 42  THR 42  41  41  THR THR B . n 
B 1 43  GLU 43  42  42  GLU GLU B . n 
B 1 44  GLU 44  43  43  GLU GLU B . n 
B 1 45  LYS 45  44  44  LYS LYS B . n 
B 1 46  TYR 46  45  45  TYR TYR B . n 
B 1 47  GLN 47  46  46  GLN GLN B . n 
B 1 48  GLU 48  47  47  GLU GLU B . n 
B 1 49  ALA 49  48  48  ALA ALA B . n 
B 1 50  LEU 50  49  49  LEU LEU B . n 
B 1 51  ALA 51  50  50  ALA ALA B . n 
B 1 52  LYS 52  51  51  LYS LYS B . n 
B 1 53  GLY 53  52  52  GLY GLY B . n 
B 1 54  ASP 54  53  53  ASP ASP B . n 
B 1 55  VAL 55  54  54  VAL VAL B . n 
B 1 56  THR 56  55  55  THR THR B . n 
B 1 57  ALA 57  56  56  ALA ALA B . n 
B 1 58  GLN 58  57  57  GLN GLN B . n 
B 1 59  ILE 59  58  58  ILE ILE B . n 
B 1 60  ALA 60  59  59  ALA ALA B . n 
B 1 61  LEU 61  60  60  LEU LEU B . n 
B 1 62  GLN 62  61  61  GLN GLN B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  ALA 64  63  63  ALA ALA B . n 
B 1 65  LEU 65  64  64  LEU LEU B . n 
B 1 66  LYS 66  65  65  LYS LYS B . n 
B 1 67  PHE 67  66  66  PHE PHE B . n 
B 1 68  ASN 68  67  67  ASN ASN B . n 
B 1 69  GLY 69  68  68  GLY GLY B . n 
B 1 70  GLY 70  69  69  GLY GLY B . n 
B 1 71  GLY 71  70  70  GLY GLY B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  ILE 73  72  72  ILE ILE B . n 
B 1 74  ASN 74  73  73  ASN ASN B . n 
B 1 75  HIS 75  74  74  HIS HIS B . n 
B 1 76  SER 76  75  75  SER SER B . n 
B 1 77  ILE 77  76  76  ILE ILE B . n 
B 1 78  PHE 78  77  77  PHE PHE B . n 
B 1 79  TRP 79  78  78  TRP TRP B . n 
B 1 80  THR 80  79  79  THR THR B . n 
B 1 81  ASN 81  80  80  ASN ASN B . n 
B 1 82  LEU 82  81  81  LEU LEU B . n 
B 1 83  SER 83  82  82  SER SER B . n 
B 1 84  PRO 84  83  83  PRO PRO B . n 
B 1 85  ASN 85  84  84  ASN ASN B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  GLY 87  86  86  GLY GLY B . n 
B 1 88  GLY 88  87  87  GLY GLY B . n 
B 1 89  GLU 89  88  88  GLU GLU B . n 
B 1 90  PRO 90  89  89  PRO PRO B . n 
B 1 91  LYS 91  90  90  LYS LYS B . n 
B 1 92  GLY 92  91  91  GLY GLY B . n 
B 1 93  GLU 93  92  92  GLU GLU B . n 
B 1 94  LEU 94  93  93  LEU LEU B . n 
B 1 95  LEU 95  94  94  LEU LEU B . n 
B 1 96  GLU 96  95  95  GLU GLU B . n 
B 1 97  ALA 97  96  96  ALA ALA B . n 
B 1 98  ILE 98  97  97  ILE ILE B . n 
B 1 99  LYS 99  98  98  LYS LYS B . n 
B 1 100 ARG 100 99  99  ARG ARG B . n 
B 1 101 ASP 101 100 100 ASP ASP B . n 
B 1 102 PHE 102 101 101 PHE PHE B . n 
B 1 103 GLY 103 102 102 GLY GLY B . n 
B 1 104 SER 104 103 103 SER SER B . n 
B 1 105 PHE 105 104 104 PHE PHE B . n 
B 1 106 ASP 106 105 105 ASP ASP B . n 
B 1 107 LYS 107 106 106 LYS LYS B . n 
B 1 108 PHE 108 107 107 PHE PHE B . n 
B 1 109 LYS 109 108 108 LYS LYS B . n 
B 1 110 GLU 110 109 109 GLU GLU B . n 
B 1 111 LYS 111 110 110 LYS LYS B . n 
B 1 112 LEU 112 111 111 LEU LEU B . n 
B 1 113 THR 113 112 112 THR THR B . n 
B 1 114 ALA 114 113 113 ALA ALA B . n 
B 1 115 ALA 115 114 114 ALA ALA B . n 
B 1 116 SER 116 115 115 SER SER B . n 
B 1 117 VAL 117 116 116 VAL VAL B . n 
B 1 118 GLY 118 117 117 GLY GLY B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 GLN 120 119 119 GLN GLN B . n 
B 1 121 GLY 121 120 120 GLY GLY B . n 
B 1 122 SER 122 121 121 SER SER B . n 
B 1 123 GLY 123 122 122 GLY GLY B . n 
B 1 124 TRP 124 123 123 TRP TRP B . n 
B 1 125 GLY 125 124 124 GLY GLY B . n 
B 1 126 TRP 126 125 125 TRP TRP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 PHE 129 128 128 PHE PHE B . n 
B 1 130 ASN 130 129 129 ASN ASN B . n 
B 1 131 LYS 131 130 130 LYS LYS B . n 
B 1 132 GLU 132 131 131 GLU GLU B . n 
B 1 133 ARG 133 132 132 ARG ARG B . n 
B 1 134 GLY 134 133 133 GLY GLY B . n 
B 1 135 HIS 135 134 134 HIS HIS B . n 
B 1 136 LEU 136 135 135 LEU LEU B . n 
B 1 137 GLN 137 136 136 GLN GLN B . n 
B 1 138 ILE 138 137 137 ILE ILE B . n 
B 1 139 ALA 139 138 138 ALA ALA B . n 
B 1 140 ALA 140 139 139 ALA ALA B . n 
B 1 141 CYS 141 140 140 CYS CYS B . n 
B 1 142 PRO 142 141 141 PRO PRO B . n 
B 1 143 ASN 143 142 142 ASN ASN B . n 
B 1 144 GLN 144 143 143 GLN GLN B . n 
B 1 145 ASP 145 144 144 ASP ASP B . n 
B 1 146 PRO 146 145 145 PRO PRO B . n 
B 1 147 LEU 147 146 146 LEU LEU B . n 
B 1 148 GLN 148 147 147 GLN GLN B . n 
B 1 149 GLY 149 148 148 GLY GLY B . n 
B 1 150 THR 150 149 149 THR THR B . n 
B 1 151 THR 151 150 150 THR THR B . n 
B 1 152 GLY 152 151 151 GLY GLY B . n 
B 1 153 LEU 153 152 152 LEU LEU B . n 
B 1 154 ILE 154 153 153 ILE ILE B . n 
B 1 155 PRO 155 154 154 PRO PRO B . n 
B 1 156 LEU 156 155 155 LEU LEU B . n 
B 1 157 LEU 157 156 156 LEU LEU B . n 
B 1 158 GLY 158 157 157 GLY GLY B . n 
B 1 159 ILE 159 158 158 ILE ILE B . n 
B 1 160 ASP 160 159 159 ASP ASP B . n 
B 1 161 VAL 161 160 160 VAL VAL B . n 
B 1 162 TRP 162 161 161 TRP TRP B . n 
B 1 163 GLU 163 162 162 GLU GLU B . n 
B 1 164 HIS 164 163 163 HIS HIS B . n 
B 1 165 ALA 165 164 164 ALA ALA B . n 
B 1 166 TYR 166 165 165 TYR TYR B . n 
B 1 167 TYR 167 166 166 TYR TYR B . n 
B 1 168 LEU 168 167 167 LEU LEU B . n 
B 1 169 GLN 169 168 168 GLN GLN B . n 
B 1 170 TYR 170 169 169 TYR TYR B . n 
B 1 171 LYS 171 170 170 LYS LYS B . n 
B 1 172 ASN 172 171 171 ASN ASN B . n 
B 1 173 VAL 173 172 172 VAL VAL B . n 
B 1 174 ARG 174 173 173 ARG ARG B . n 
B 1 175 PRO 175 174 174 PRO PRO B . n 
B 1 176 ASP 176 175 175 ASP ASP B . n 
B 1 177 TYR 177 176 176 TYR TYR B . n 
B 1 178 LEU 178 177 177 LEU LEU B . n 
B 1 179 LYS 179 178 178 LYS LYS B . n 
B 1 180 ALA 180 179 179 ALA ALA B . n 
B 1 181 ILE 181 180 180 ILE ILE B . n 
B 1 182 TRP 182 181 181 TRP TRP B . n 
B 1 183 ASN 183 182 182 ASN ASN B . n 
B 1 184 VAL 184 183 183 VAL VAL B . n 
B 1 185 ILE 185 184 184 ILE ILE B . n 
B 1 186 ASN 186 185 185 ASN ASN B . n 
B 1 187 TRP 187 186 186 TRP TRP B . n 
B 1 188 GLU 188 187 187 GLU GLU B . n 
B 1 189 ASN 189 188 188 ASN ASN B . n 
B 1 190 VAL 190 189 189 VAL VAL B . n 
B 1 191 THR 191 190 190 THR THR B . n 
B 1 192 GLU 192 191 191 GLU GLU B . n 
B 1 193 ARG 193 192 192 ARG ARG B . n 
B 1 194 TYR 194 193 193 TYR TYR B . n 
B 1 195 MET 195 194 194 MET MET B . n 
B 1 196 ALA 196 195 195 ALA ALA B . n 
B 1 197 CYS 197 196 196 CYS CYS B . n 
B 1 198 LYS 198 197 197 LYS LYS B . n 
B 1 199 LYS 199 198 198 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PEO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PEO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 MN  1   201 202 MN  MN  A . 
D 3 PEO 1   202 203 PEO PEO A . 
E 4 PO4 1   203 1   PO4 PO4 A . 
F 4 PO4 1   204 3   PO4 PO4 A . 
G 5 K   1   205 2   K   K   A . 
H 2 MN  1   201 202 MN  MN  B . 
I 4 PO4 1   202 2   PO4 PO4 B . 
J 6 HOH 1   301 152 HOH HOH A . 
J 6 HOH 2   302 627 HOH HOH A . 
J 6 HOH 3   303 568 HOH HOH A . 
J 6 HOH 4   304 530 HOH HOH A . 
J 6 HOH 5   305 670 HOH HOH A . 
J 6 HOH 6   306 395 HOH HOH A . 
J 6 HOH 7   307 185 HOH HOH A . 
J 6 HOH 8   308 93  HOH HOH A . 
J 6 HOH 9   309 672 HOH HOH A . 
J 6 HOH 10  310 121 HOH HOH A . 
J 6 HOH 11  311 534 HOH HOH A . 
J 6 HOH 12  312 287 HOH HOH A . 
J 6 HOH 13  313 506 HOH HOH A . 
J 6 HOH 14  314 311 HOH HOH A . 
J 6 HOH 15  315 269 HOH HOH A . 
J 6 HOH 16  316 654 HOH HOH A . 
J 6 HOH 17  317 411 HOH HOH A . 
J 6 HOH 18  318 495 HOH HOH A . 
J 6 HOH 19  319 673 HOH HOH A . 
J 6 HOH 20  320 245 HOH HOH A . 
J 6 HOH 21  321 96  HOH HOH A . 
J 6 HOH 22  322 484 HOH HOH A . 
J 6 HOH 23  323 483 HOH HOH A . 
J 6 HOH 24  324 401 HOH HOH A . 
J 6 HOH 25  325 224 HOH HOH A . 
J 6 HOH 26  326 502 HOH HOH A . 
J 6 HOH 27  327 62  HOH HOH A . 
J 6 HOH 28  328 34  HOH HOH A . 
J 6 HOH 29  329 57  HOH HOH A . 
J 6 HOH 30  330 487 HOH HOH A . 
J 6 HOH 31  331 10  HOH HOH A . 
J 6 HOH 32  332 383 HOH HOH A . 
J 6 HOH 33  333 295 HOH HOH A . 
J 6 HOH 34  334 32  HOH HOH A . 
J 6 HOH 35  335 235 HOH HOH A . 
J 6 HOH 36  336 315 HOH HOH A . 
J 6 HOH 37  337 314 HOH HOH A . 
J 6 HOH 38  338 208 HOH HOH A . 
J 6 HOH 39  339 11  HOH HOH A . 
J 6 HOH 40  340 19  HOH HOH A . 
J 6 HOH 41  341 240 HOH HOH A . 
J 6 HOH 42  342 365 HOH HOH A . 
J 6 HOH 43  343 309 HOH HOH A . 
J 6 HOH 44  344 628 HOH HOH A . 
J 6 HOH 45  345 104 HOH HOH A . 
J 6 HOH 46  346 473 HOH HOH A . 
J 6 HOH 47  347 277 HOH HOH A . 
J 6 HOH 48  348 182 HOH HOH A . 
J 6 HOH 49  349 742 HOH HOH A . 
J 6 HOH 50  350 23  HOH HOH A . 
J 6 HOH 51  351 12  HOH HOH A . 
J 6 HOH 52  352 362 HOH HOH A . 
J 6 HOH 53  353 257 HOH HOH A . 
J 6 HOH 54  354 8   HOH HOH A . 
J 6 HOH 55  355 48  HOH HOH A . 
J 6 HOH 56  356 85  HOH HOH A . 
J 6 HOH 57  357 42  HOH HOH A . 
J 6 HOH 58  358 147 HOH HOH A . 
J 6 HOH 59  359 92  HOH HOH A . 
J 6 HOH 60  360 274 HOH HOH A . 
J 6 HOH 61  361 41  HOH HOH A . 
J 6 HOH 62  362 579 HOH HOH A . 
J 6 HOH 63  363 509 HOH HOH A . 
J 6 HOH 64  364 169 HOH HOH A . 
J 6 HOH 65  365 707 HOH HOH A . 
J 6 HOH 66  366 652 HOH HOH A . 
J 6 HOH 67  367 129 HOH HOH A . 
J 6 HOH 68  368 710 HOH HOH A . 
J 6 HOH 69  369 230 HOH HOH A . 
J 6 HOH 70  370 577 HOH HOH A . 
J 6 HOH 71  371 173 HOH HOH A . 
J 6 HOH 72  372 130 HOH HOH A . 
J 6 HOH 73  373 38  HOH HOH A . 
J 6 HOH 74  374 25  HOH HOH A . 
J 6 HOH 75  375 213 HOH HOH A . 
J 6 HOH 76  376 774 HOH HOH A . 
J 6 HOH 77  377 328 HOH HOH A . 
J 6 HOH 78  378 199 HOH HOH A . 
J 6 HOH 79  379 359 HOH HOH A . 
J 6 HOH 80  380 120 HOH HOH A . 
J 6 HOH 81  381 304 HOH HOH A . 
J 6 HOH 82  382 69  HOH HOH A . 
J 6 HOH 83  383 543 HOH HOH A . 
J 6 HOH 84  384 256 HOH HOH A . 
J 6 HOH 85  385 477 HOH HOH A . 
J 6 HOH 86  386 102 HOH HOH A . 
J 6 HOH 87  387 361 HOH HOH A . 
J 6 HOH 88  388 203 HOH HOH A . 
J 6 HOH 89  389 36  HOH HOH A . 
J 6 HOH 90  390 317 HOH HOH A . 
J 6 HOH 91  391 84  HOH HOH A . 
J 6 HOH 92  392 113 HOH HOH A . 
J 6 HOH 93  393 60  HOH HOH A . 
J 6 HOH 94  394 49  HOH HOH A . 
J 6 HOH 95  395 109 HOH HOH A . 
J 6 HOH 96  396 137 HOH HOH A . 
J 6 HOH 97  397 406 HOH HOH A . 
J 6 HOH 98  398 574 HOH HOH A . 
J 6 HOH 99  399 100 HOH HOH A . 
J 6 HOH 100 400 52  HOH HOH A . 
J 6 HOH 101 401 737 HOH HOH A . 
J 6 HOH 102 402 87  HOH HOH A . 
J 6 HOH 103 403 74  HOH HOH A . 
J 6 HOH 104 404 424 HOH HOH A . 
J 6 HOH 105 405 15  HOH HOH A . 
J 6 HOH 106 406 427 HOH HOH A . 
J 6 HOH 107 407 123 HOH HOH A . 
J 6 HOH 108 408 232 HOH HOH A . 
J 6 HOH 109 409 503 HOH HOH A . 
J 6 HOH 110 410 9   HOH HOH A . 
J 6 HOH 111 411 336 HOH HOH A . 
J 6 HOH 112 412 535 HOH HOH A . 
J 6 HOH 113 413 398 HOH HOH A . 
J 6 HOH 114 414 139 HOH HOH A . 
J 6 HOH 115 415 330 HOH HOH A . 
J 6 HOH 116 416 265 HOH HOH A . 
J 6 HOH 117 417 318 HOH HOH A . 
J 6 HOH 118 418 95  HOH HOH A . 
J 6 HOH 119 419 386 HOH HOH A . 
J 6 HOH 120 420 693 HOH HOH A . 
J 6 HOH 121 421 134 HOH HOH A . 
J 6 HOH 122 422 369 HOH HOH A . 
J 6 HOH 123 423 135 HOH HOH A . 
J 6 HOH 124 424 29  HOH HOH A . 
J 6 HOH 125 425 263 HOH HOH A . 
J 6 HOH 126 426 496 HOH HOH A . 
J 6 HOH 127 427 141 HOH HOH A . 
J 6 HOH 128 428 103 HOH HOH A . 
J 6 HOH 129 429 47  HOH HOH A . 
J 6 HOH 130 430 410 HOH HOH A . 
J 6 HOH 131 431 186 HOH HOH A . 
J 6 HOH 132 432 743 HOH HOH A . 
J 6 HOH 133 433 634 HOH HOH A . 
J 6 HOH 134 434 196 HOH HOH A . 
J 6 HOH 135 435 153 HOH HOH A . 
J 6 HOH 136 436 273 HOH HOH A . 
J 6 HOH 137 437 345 HOH HOH A . 
J 6 HOH 138 438 516 HOH HOH A . 
J 6 HOH 139 439 419 HOH HOH A . 
J 6 HOH 140 440 507 HOH HOH A . 
J 6 HOH 141 441 827 HOH HOH A . 
J 6 HOH 142 442 397 HOH HOH A . 
J 6 HOH 143 443 462 HOH HOH A . 
J 6 HOH 144 444 267 HOH HOH A . 
J 6 HOH 145 445 305 HOH HOH A . 
J 6 HOH 146 446 71  HOH HOH A . 
J 6 HOH 147 447 90  HOH HOH A . 
J 6 HOH 148 448 63  HOH HOH A . 
J 6 HOH 149 449 471 HOH HOH A . 
J 6 HOH 150 450 297 HOH HOH A . 
J 6 HOH 151 451 281 HOH HOH A . 
J 6 HOH 152 452 7   HOH HOH A . 
J 6 HOH 153 453 133 HOH HOH A . 
J 6 HOH 154 454 22  HOH HOH A . 
J 6 HOH 155 455 255 HOH HOH A . 
J 6 HOH 156 456 17  HOH HOH A . 
J 6 HOH 157 457 518 HOH HOH A . 
J 6 HOH 158 458 118 HOH HOH A . 
J 6 HOH 159 459 778 HOH HOH A . 
J 6 HOH 160 460 55  HOH HOH A . 
J 6 HOH 161 461 43  HOH HOH A . 
J 6 HOH 162 462 242 HOH HOH A . 
J 6 HOH 163 463 97  HOH HOH A . 
J 6 HOH 164 464 445 HOH HOH A . 
J 6 HOH 165 465 191 HOH HOH A . 
J 6 HOH 166 466 155 HOH HOH A . 
J 6 HOH 167 467 244 HOH HOH A . 
J 6 HOH 168 468 246 HOH HOH A . 
J 6 HOH 169 469 233 HOH HOH A . 
J 6 HOH 170 470 145 HOH HOH A . 
J 6 HOH 171 471 524 HOH HOH A . 
J 6 HOH 172 472 714 HOH HOH A . 
J 6 HOH 173 473 77  HOH HOH A . 
J 6 HOH 174 474 532 HOH HOH A . 
J 6 HOH 175 475 143 HOH HOH A . 
J 6 HOH 176 476 396 HOH HOH A . 
J 6 HOH 177 477 371 HOH HOH A . 
J 6 HOH 178 478 553 HOH HOH A . 
J 6 HOH 179 479 447 HOH HOH A . 
J 6 HOH 180 480 407 HOH HOH A . 
J 6 HOH 181 481 72  HOH HOH A . 
J 6 HOH 182 482 301 HOH HOH A . 
J 6 HOH 183 483 290 HOH HOH A . 
J 6 HOH 184 484 178 HOH HOH A . 
J 6 HOH 185 485 91  HOH HOH A . 
J 6 HOH 186 486 211 HOH HOH A . 
J 6 HOH 187 487 373 HOH HOH A . 
J 6 HOH 188 488 566 HOH HOH A . 
J 6 HOH 189 489 379 HOH HOH A . 
J 6 HOH 190 490 124 HOH HOH A . 
J 6 HOH 191 491 352 HOH HOH A . 
J 6 HOH 192 492 258 HOH HOH A . 
J 6 HOH 193 493 339 HOH HOH A . 
J 6 HOH 194 494 635 HOH HOH A . 
J 6 HOH 195 495 607 HOH HOH A . 
J 6 HOH 196 496 630 HOH HOH A . 
J 6 HOH 197 497 655 HOH HOH A . 
J 6 HOH 198 498 446 HOH HOH A . 
J 6 HOH 199 499 312 HOH HOH A . 
J 6 HOH 200 500 469 HOH HOH A . 
J 6 HOH 201 501 404 HOH HOH A . 
J 6 HOH 202 502 486 HOH HOH A . 
J 6 HOH 203 503 172 HOH HOH A . 
J 6 HOH 204 504 260 HOH HOH A . 
J 6 HOH 205 505 389 HOH HOH A . 
J 6 HOH 206 506 195 HOH HOH A . 
J 6 HOH 207 507 79  HOH HOH A . 
J 6 HOH 208 508 334 HOH HOH A . 
J 6 HOH 209 509 451 HOH HOH A . 
J 6 HOH 210 510 620 HOH HOH A . 
J 6 HOH 211 511 415 HOH HOH A . 
J 6 HOH 212 512 302 HOH HOH A . 
J 6 HOH 213 513 132 HOH HOH A . 
J 6 HOH 214 514 216 HOH HOH A . 
J 6 HOH 215 515 691 HOH HOH A . 
J 6 HOH 216 516 294 HOH HOH A . 
J 6 HOH 217 517 228 HOH HOH A . 
J 6 HOH 218 518 789 HOH HOH A . 
J 6 HOH 219 519 288 HOH HOH A . 
J 6 HOH 220 520 360 HOH HOH A . 
J 6 HOH 221 521 657 HOH HOH A . 
J 6 HOH 222 522 480 HOH HOH A . 
J 6 HOH 223 523 333 HOH HOH A . 
J 6 HOH 224 524 283 HOH HOH A . 
J 6 HOH 225 525 482 HOH HOH A . 
J 6 HOH 226 526 341 HOH HOH A . 
J 6 HOH 227 527 146 HOH HOH A . 
J 6 HOH 228 528 259 HOH HOH A . 
J 6 HOH 229 529 94  HOH HOH A . 
J 6 HOH 230 530 59  HOH HOH A . 
J 6 HOH 231 531 437 HOH HOH A . 
J 6 HOH 232 532 558 HOH HOH A . 
J 6 HOH 233 533 231 HOH HOH A . 
J 6 HOH 234 534 456 HOH HOH A . 
J 6 HOH 235 535 222 HOH HOH A . 
J 6 HOH 236 536 243 HOH HOH A . 
J 6 HOH 237 537 358 HOH HOH A . 
J 6 HOH 238 538 284 HOH HOH A . 
J 6 HOH 239 539 545 HOH HOH A . 
J 6 HOH 240 540 468 HOH HOH A . 
J 6 HOH 241 541 266 HOH HOH A . 
J 6 HOH 242 542 466 HOH HOH A . 
J 6 HOH 243 543 221 HOH HOH A . 
J 6 HOH 244 544 282 HOH HOH A . 
J 6 HOH 245 545 675 HOH HOH A . 
J 6 HOH 246 546 329 HOH HOH A . 
J 6 HOH 247 547 525 HOH HOH A . 
J 6 HOH 248 548 349 HOH HOH A . 
J 6 HOH 249 549 163 HOH HOH A . 
J 6 HOH 250 550 176 HOH HOH A . 
J 6 HOH 251 551 819 HOH HOH A . 
J 6 HOH 252 552 385 HOH HOH A . 
J 6 HOH 253 553 549 HOH HOH A . 
J 6 HOH 254 554 788 HOH HOH A . 
J 6 HOH 255 555 177 HOH HOH A . 
J 6 HOH 256 556 453 HOH HOH A . 
J 6 HOH 257 557 342 HOH HOH A . 
J 6 HOH 258 558 347 HOH HOH A . 
J 6 HOH 259 559 457 HOH HOH A . 
J 6 HOH 260 560 335 HOH HOH A . 
J 6 HOH 261 561 600 HOH HOH A . 
J 6 HOH 262 562 382 HOH HOH A . 
J 6 HOH 263 563 428 HOH HOH A . 
J 6 HOH 264 564 161 HOH HOH A . 
J 6 HOH 265 565 249 HOH HOH A . 
J 6 HOH 266 566 776 HOH HOH A . 
J 6 HOH 267 567 351 HOH HOH A . 
J 6 HOH 268 568 210 HOH HOH A . 
J 6 HOH 269 569 140 HOH HOH A . 
J 6 HOH 270 570 192 HOH HOH A . 
J 6 HOH 271 571 56  HOH HOH A . 
J 6 HOH 272 572 432 HOH HOH A . 
J 6 HOH 273 573 261 HOH HOH A . 
J 6 HOH 274 574 364 HOH HOH A . 
J 6 HOH 275 575 271 HOH HOH A . 
J 6 HOH 276 576 270 HOH HOH A . 
J 6 HOH 277 577 510 HOH HOH A . 
J 6 HOH 278 578 400 HOH HOH A . 
J 6 HOH 279 579 394 HOH HOH A . 
J 6 HOH 280 580 207 HOH HOH A . 
J 6 HOH 281 581 618 HOH HOH A . 
J 6 HOH 282 582 326 HOH HOH A . 
K 6 HOH 1   301 220 HOH HOH B . 
K 6 HOH 2   302 460 HOH HOH B . 
K 6 HOH 3   303 128 HOH HOH B . 
K 6 HOH 4   304 293 HOH HOH B . 
K 6 HOH 5   305 485 HOH HOH B . 
K 6 HOH 6   306 203 HOH HOH B . 
K 6 HOH 7   307 279 HOH HOH B . 
K 6 HOH 8   308 513 HOH HOH B . 
K 6 HOH 9   309 348 HOH HOH B . 
K 6 HOH 10  310 772 HOH HOH B . 
K 6 HOH 11  311 214 HOH HOH B . 
K 6 HOH 12  312 658 HOH HOH B . 
K 6 HOH 13  313 76  HOH HOH B . 
K 6 HOH 14  314 215 HOH HOH B . 
K 6 HOH 15  315 528 HOH HOH B . 
K 6 HOH 16  316 499 HOH HOH B . 
K 6 HOH 17  317 674 HOH HOH B . 
K 6 HOH 18  318 46  HOH HOH B . 
K 6 HOH 19  319 310 HOH HOH B . 
K 6 HOH 20  320 181 HOH HOH B . 
K 6 HOH 21  321 116 HOH HOH B . 
K 6 HOH 22  322 238 HOH HOH B . 
K 6 HOH 23  323 126 HOH HOH B . 
K 6 HOH 24  324 2   HOH HOH B . 
K 6 HOH 25  325 327 HOH HOH B . 
K 6 HOH 26  326 3   HOH HOH B . 
K 6 HOH 27  327 292 HOH HOH B . 
K 6 HOH 28  328 54  HOH HOH B . 
K 6 HOH 29  329 200 HOH HOH B . 
K 6 HOH 30  330 489 HOH HOH B . 
K 6 HOH 31  331 425 HOH HOH B . 
K 6 HOH 32  332 639 HOH HOH B . 
K 6 HOH 33  333 138 HOH HOH B . 
K 6 HOH 34  334 825 HOH HOH B . 
K 6 HOH 35  335 65  HOH HOH B . 
K 6 HOH 36  336 504 HOH HOH B . 
K 6 HOH 37  337 212 HOH HOH B . 
K 6 HOH 38  338 350 HOH HOH B . 
K 6 HOH 39  339 175 HOH HOH B . 
K 6 HOH 40  340 160 HOH HOH B . 
K 6 HOH 41  341 67  HOH HOH B . 
K 6 HOH 42  342 597 HOH HOH B . 
K 6 HOH 43  343 368 HOH HOH B . 
K 6 HOH 44  344 217 HOH HOH B . 
K 6 HOH 45  345 393 HOH HOH B . 
K 6 HOH 46  346 174 HOH HOH B . 
K 6 HOH 47  347 4   HOH HOH B . 
K 6 HOH 48  348 475 HOH HOH B . 
K 6 HOH 49  349 241 HOH HOH B . 
K 6 HOH 50  350 16  HOH HOH B . 
K 6 HOH 51  351 154 HOH HOH B . 
K 6 HOH 52  352 252 HOH HOH B . 
K 6 HOH 53  353 1   HOH HOH B . 
K 6 HOH 54  354 421 HOH HOH B . 
K 6 HOH 55  355 332 HOH HOH B . 
K 6 HOH 56  356 6   HOH HOH B . 
K 6 HOH 57  357 150 HOH HOH B . 
K 6 HOH 58  358 388 HOH HOH B . 
K 6 HOH 59  359 27  HOH HOH B . 
K 6 HOH 60  360 291 HOH HOH B . 
K 6 HOH 61  361 26  HOH HOH B . 
K 6 HOH 62  362 51  HOH HOH B . 
K 6 HOH 63  363 237 HOH HOH B . 
K 6 HOH 64  364 61  HOH HOH B . 
K 6 HOH 65  365 375 HOH HOH B . 
K 6 HOH 66  366 380 HOH HOH B . 
K 6 HOH 67  367 39  HOH HOH B . 
K 6 HOH 68  368 372 HOH HOH B . 
K 6 HOH 69  369 75  HOH HOH B . 
K 6 HOH 70  370 168 HOH HOH B . 
K 6 HOH 71  371 713 HOH HOH B . 
K 6 HOH 72  372 602 HOH HOH B . 
K 6 HOH 73  373 744 HOH HOH B . 
K 6 HOH 74  374 50  HOH HOH B . 
K 6 HOH 75  375 58  HOH HOH B . 
K 6 HOH 76  376 171 HOH HOH B . 
K 6 HOH 77  377 73  HOH HOH B . 
K 6 HOH 78  378 515 HOH HOH B . 
K 6 HOH 79  379 44  HOH HOH B . 
K 6 HOH 80  380 498 HOH HOH B . 
K 6 HOH 81  381 357 HOH HOH B . 
K 6 HOH 82  382 184 HOH HOH B . 
K 6 HOH 83  383 78  HOH HOH B . 
K 6 HOH 84  384 20  HOH HOH B . 
K 6 HOH 85  385 591 HOH HOH B . 
K 6 HOH 86  386 40  HOH HOH B . 
K 6 HOH 87  387 21  HOH HOH B . 
K 6 HOH 88  388 165 HOH HOH B . 
K 6 HOH 89  389 64  HOH HOH B . 
K 6 HOH 90  390 209 HOH HOH B . 
K 6 HOH 91  391 157 HOH HOH B . 
K 6 HOH 92  392 198 HOH HOH B . 
K 6 HOH 93  393 300 HOH HOH B . 
K 6 HOH 94  394 268 HOH HOH B . 
K 6 HOH 95  395 529 HOH HOH B . 
K 6 HOH 96  396 70  HOH HOH B . 
K 6 HOH 97  397 225 HOH HOH B . 
K 6 HOH 98  398 324 HOH HOH B . 
K 6 HOH 99  399 381 HOH HOH B . 
K 6 HOH 100 400 166 HOH HOH B . 
K 6 HOH 101 401 226 HOH HOH B . 
K 6 HOH 102 402 13  HOH HOH B . 
K 6 HOH 103 403 89  HOH HOH B . 
K 6 HOH 104 404 325 HOH HOH B . 
K 6 HOH 105 405 149 HOH HOH B . 
K 6 HOH 106 406 122 HOH HOH B . 
K 6 HOH 107 407 125 HOH HOH B . 
K 6 HOH 108 408 162 HOH HOH B . 
K 6 HOH 109 409 251 HOH HOH B . 
K 6 HOH 110 410 671 HOH HOH B . 
K 6 HOH 111 411 276 HOH HOH B . 
K 6 HOH 112 412 491 HOH HOH B . 
K 6 HOH 113 413 24  HOH HOH B . 
K 6 HOH 114 414 448 HOH HOH B . 
K 6 HOH 115 415 35  HOH HOH B . 
K 6 HOH 116 416 81  HOH HOH B . 
K 6 HOH 117 417 299 HOH HOH B . 
K 6 HOH 118 418 110 HOH HOH B . 
K 6 HOH 119 419 37  HOH HOH B . 
K 6 HOH 120 420 5   HOH HOH B . 
K 6 HOH 121 421 202 HOH HOH B . 
K 6 HOH 122 422 68  HOH HOH B . 
K 6 HOH 123 423 538 HOH HOH B . 
K 6 HOH 124 424 45  HOH HOH B . 
K 6 HOH 125 425 18  HOH HOH B . 
K 6 HOH 126 426 119 HOH HOH B . 
K 6 HOH 127 427 193 HOH HOH B . 
K 6 HOH 128 428 376 HOH HOH B . 
K 6 HOH 129 429 219 HOH HOH B . 
K 6 HOH 130 430 117 HOH HOH B . 
K 6 HOH 131 431 106 HOH HOH B . 
K 6 HOH 132 432 346 HOH HOH B . 
K 6 HOH 133 433 164 HOH HOH B . 
K 6 HOH 134 434 818 HOH HOH B . 
K 6 HOH 135 435 197 HOH HOH B . 
K 6 HOH 136 436 467 HOH HOH B . 
K 6 HOH 137 437 236 HOH HOH B . 
K 6 HOH 138 438 31  HOH HOH B . 
K 6 HOH 139 439 144 HOH HOH B . 
K 6 HOH 140 440 817 HOH HOH B . 
K 6 HOH 141 441 170 HOH HOH B . 
K 6 HOH 142 442 523 HOH HOH B . 
K 6 HOH 143 443 83  HOH HOH B . 
K 6 HOH 144 444 227 HOH HOH B . 
K 6 HOH 145 445 399 HOH HOH B . 
K 6 HOH 146 446 112 HOH HOH B . 
K 6 HOH 147 447 88  HOH HOH B . 
K 6 HOH 148 448 223 HOH HOH B . 
K 6 HOH 149 449 759 HOH HOH B . 
K 6 HOH 150 450 82  HOH HOH B . 
K 6 HOH 151 451 455 HOH HOH B . 
K 6 HOH 152 452 280 HOH HOH B . 
K 6 HOH 153 453 285 HOH HOH B . 
K 6 HOH 154 454 105 HOH HOH B . 
K 6 HOH 155 455 98  HOH HOH B . 
K 6 HOH 156 456 167 HOH HOH B . 
K 6 HOH 157 457 272 HOH HOH B . 
K 6 HOH 158 458 131 HOH HOH B . 
K 6 HOH 159 459 435 HOH HOH B . 
K 6 HOH 160 460 536 HOH HOH B . 
K 6 HOH 161 461 53  HOH HOH B . 
K 6 HOH 162 462 66  HOH HOH B . 
K 6 HOH 163 463 14  HOH HOH B . 
K 6 HOH 164 464 248 HOH HOH B . 
K 6 HOH 165 465 114 HOH HOH B . 
K 6 HOH 166 466 234 HOH HOH B . 
K 6 HOH 167 467 206 HOH HOH B . 
K 6 HOH 168 468 28  HOH HOH B . 
K 6 HOH 169 469 412 HOH HOH B . 
K 6 HOH 170 470 86  HOH HOH B . 
K 6 HOH 171 471 582 HOH HOH B . 
K 6 HOH 172 472 321 HOH HOH B . 
K 6 HOH 173 473 218 HOH HOH B . 
K 6 HOH 174 474 356 HOH HOH B . 
K 6 HOH 175 475 418 HOH HOH B . 
K 6 HOH 176 476 108 HOH HOH B . 
K 6 HOH 177 477 201 HOH HOH B . 
K 6 HOH 178 478 107 HOH HOH B . 
K 6 HOH 179 479 420 HOH HOH B . 
K 6 HOH 180 480 229 HOH HOH B . 
K 6 HOH 181 481 296 HOH HOH B . 
K 6 HOH 182 482 711 HOH HOH B . 
K 6 HOH 183 483 307 HOH HOH B . 
K 6 HOH 184 484 158 HOH HOH B . 
K 6 HOH 185 485 416 HOH HOH B . 
K 6 HOH 186 486 449 HOH HOH B . 
K 6 HOH 187 487 820 HOH HOH B . 
K 6 HOH 188 488 187 HOH HOH B . 
K 6 HOH 189 489 344 HOH HOH B . 
K 6 HOH 190 490 409 HOH HOH B . 
K 6 HOH 191 491 239 HOH HOH B . 
K 6 HOH 192 492 384 HOH HOH B . 
K 6 HOH 193 493 422 HOH HOH B . 
K 6 HOH 194 494 459 HOH HOH B . 
K 6 HOH 195 495 355 HOH HOH B . 
K 6 HOH 196 496 623 HOH HOH B . 
K 6 HOH 197 497 822 HOH HOH B . 
K 6 HOH 198 498 275 HOH HOH B . 
K 6 HOH 199 499 533 HOH HOH B . 
K 6 HOH 200 500 322 HOH HOH B . 
K 6 HOH 201 501 303 HOH HOH B . 
K 6 HOH 202 502 286 HOH HOH B . 
K 6 HOH 203 503 278 HOH HOH B . 
K 6 HOH 204 504 588 HOH HOH B . 
K 6 HOH 205 505 556 HOH HOH B . 
K 6 HOH 206 506 403 HOH HOH B . 
K 6 HOH 207 507 127 HOH HOH B . 
K 6 HOH 208 508 247 HOH HOH B . 
K 6 HOH 209 509 289 HOH HOH B . 
K 6 HOH 210 510 250 HOH HOH B . 
K 6 HOH 211 511 392 HOH HOH B . 
K 6 HOH 212 512 180 HOH HOH B . 
K 6 HOH 213 513 391 HOH HOH B . 
K 6 HOH 214 514 101 HOH HOH B . 
K 6 HOH 215 515 354 HOH HOH B . 
K 6 HOH 216 516 308 HOH HOH B . 
K 6 HOH 217 517 262 HOH HOH B . 
K 6 HOH 218 518 142 HOH HOH B . 
K 6 HOH 219 519 159 HOH HOH B . 
K 6 HOH 220 520 816 HOH HOH B . 
K 6 HOH 221 521 205 HOH HOH B . 
K 6 HOH 222 522 33  HOH HOH B . 
K 6 HOH 223 523 387 HOH HOH B . 
K 6 HOH 224 524 488 HOH HOH B . 
K 6 HOH 225 525 377 HOH HOH B . 
K 6 HOH 226 526 115 HOH HOH B . 
K 6 HOH 227 527 30  HOH HOH B . 
K 6 HOH 228 528 708 HOH HOH B . 
K 6 HOH 229 529 452 HOH HOH B . 
K 6 HOH 230 530 99  HOH HOH B . 
K 6 HOH 231 531 340 HOH HOH B . 
K 6 HOH 232 532 179 HOH HOH B . 
K 6 HOH 233 533 414 HOH HOH B . 
K 6 HOH 234 534 434 HOH HOH B . 
K 6 HOH 235 535 188 HOH HOH B . 
K 6 HOH 236 536 441 HOH HOH B . 
K 6 HOH 237 537 331 HOH HOH B . 
K 6 HOH 238 538 470 HOH HOH B . 
K 6 HOH 239 539 343 HOH HOH B . 
K 6 HOH 240 540 370 HOH HOH B . 
K 6 HOH 241 541 559 HOH HOH B . 
K 6 HOH 242 542 190 HOH HOH B . 
K 6 HOH 243 543 478 HOH HOH B . 
K 6 HOH 244 544 656 HOH HOH B . 
K 6 HOH 245 545 481 HOH HOH B . 
K 6 HOH 246 546 402 HOH HOH B . 
K 6 HOH 247 547 323 HOH HOH B . 
K 6 HOH 248 548 474 HOH HOH B . 
K 6 HOH 249 549 319 HOH HOH B . 
K 6 HOH 250 550 156 HOH HOH B . 
K 6 HOH 251 551 479 HOH HOH B . 
K 6 HOH 252 552 694 HOH HOH B . 
K 6 HOH 253 553 429 HOH HOH B . 
K 6 HOH 254 554 151 HOH HOH B . 
K 6 HOH 255 555 298 HOH HOH B . 
K 6 HOH 256 556 511 HOH HOH B . 
K 6 HOH 257 557 111 HOH HOH B . 
K 6 HOH 258 558 264 HOH HOH B . 
K 6 HOH 259 559 440 HOH HOH B . 
K 6 HOH 260 560 183 HOH HOH B . 
K 6 HOH 261 561 436 HOH HOH B . 
K 6 HOH 262 562 189 HOH HOH B . 
K 6 HOH 263 563 519 HOH HOH B . 
K 6 HOH 264 564 431 HOH HOH B . 
K 6 HOH 265 565 823 HOH HOH B . 
K 6 HOH 266 566 438 HOH HOH B . 
K 6 HOH 267 567 367 HOH HOH B . 
K 6 HOH 268 568 338 HOH HOH B . 
K 6 HOH 269 569 417 HOH HOH B . 
K 6 HOH 270 570 253 HOH HOH B . 
K 6 HOH 271 571 472 HOH HOH B . 
K 6 HOH 272 572 405 HOH HOH B . 
K 6 HOH 273 573 148 HOH HOH B . 
K 6 HOH 274 574 313 HOH HOH B . 
K 6 HOH 275 575 80  HOH HOH B . 
K 6 HOH 276 576 493 HOH HOH B . 
K 6 HOH 277 577 492 HOH HOH B . 
K 6 HOH 278 578 204 HOH HOH B . 
K 6 HOH 279 579 490 HOH HOH B . 
K 6 HOH 280 580 136 HOH HOH B . 
K 6 HOH 281 581 611 HOH HOH B . 
K 6 HOH 282 582 775 HOH HOH B . 
K 6 HOH 283 583 337 HOH HOH B . 
K 6 HOH 284 584 366 HOH HOH B . 
K 6 HOH 285 585 194 HOH HOH B . 
K 6 HOH 286 586 413 HOH HOH B . 
K 6 HOH 287 587 363 HOH HOH B . 
K 6 HOH 288 588 378 HOH HOH B . 
K 6 HOH 289 589 501 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BWQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.221 
_cell.length_a_esd                 ? 
_cell.length_b                     78.221 
_cell.length_b_esd                 ? 
_cell.length_c                     239.501 
_cell.length_c_esd                 ? 
_cell.volume                       1269067.407 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9BWQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            'P 61 2 (x,y,z+5/12)' 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BWQ 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.02 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.8 M potassium phosphate pH 7.8' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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 PILATUS 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         2023-12-17 
_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   0.9795 
_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                        'SSRL BEAMLINE BL14-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL14-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          14.85 
_reflns.entry_id                                       9BWQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               39.13 
_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                                     85139 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.40 
_reflns_shell.d_res_low                                     1.45 
_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                             8221 
_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                               0.324 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.788 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.65 
_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                                 9BWQ 
_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                            1.40 
_refine.ls_d_res_low                             39.11 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     85129 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  83129 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.84 
_refine.ls_percent_reflns_R_free                 2.35 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1849 
_refine.ls_R_factor_R_free                       0.2052 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1844 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 21.1179 
_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                            0.1530 
_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                       1.40 
_refine_hist.d_res_low                        39.11 
_refine_hist.number_atoms_solvent             571 
_refine_hist.number_atoms_total               3751 
_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        3160 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.0037  ? 3276 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6829  ? 4449 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0688  ? 455  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0048  ? 578  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.6139 ? 1175 ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    0.716736371786 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
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' 1.40 1.44  . . 138 5711 97.34  . . . . 0.2886 . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 1.44 1.47  . . 138 5795 97.71  . . . . 0.2683 . . . . . . . . . . . 0.3012 
'X-RAY DIFFRACTION' 1.47 1.52  . . 139 5762 98.17  . . . . 0.2359 . . . . . . . . . . . 0.2577 
'X-RAY DIFFRACTION' 1.52 1.57  . . 141 5855 98.62  . . . . 0.2116 . . . . . . . . . . . 0.2478 
'X-RAY DIFFRACTION' 1.57 1.62  . . 140 5825 98.82  . . . . 0.1953 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 1.62 1.69  . . 140 5799 98.20  . . . . 0.1988 . . . . . . . . . . . 0.2230 
'X-RAY DIFFRACTION' 1.69 1.76  . . 142 5928 99.18  . . . . 0.1894 . . . . . . . . . . . 0.2161 
'X-RAY DIFFRACTION' 1.76 1.86  . . 143 5928 99.31  . . . . 0.1888 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 1.86 1.97  . . 143 5930 99.54  . . . . 0.1781 . . . . . . . . . . . 0.1983 
'X-RAY DIFFRACTION' 1.97 2.13  . . 144 5975 99.61  . . . . 0.1720 . . . . . . . . . . . 0.2105 
'X-RAY DIFFRACTION' 2.13 2.34  . . 143 5929 98.41  . . . . 0.1756 . . . . . . . . . . . 0.2060 
'X-RAY DIFFRACTION' 2.34 2.68  . . 146 6077 99.95  . . . . 0.1852 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 2.68 3.37  . . 148 6170 100.00 . . . . 0.1915 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 3.37 39.11 . . 155 6445 98.73  . . . . 0.1593 . . . . . . . . . . . 0.1810 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   -0.991190421017 
_struct_ncs_oper.matrix[1][2]   0.013872955909 
_struct_ncs_oper.matrix[1][3]   -0.131715945803 
_struct_ncs_oper.matrix[2][1]   0.0160580160965 
_struct_ncs_oper.matrix[2][2]   -0.974574657999 
_struct_ncs_oper.matrix[2][3]   -0.22348685891 
_struct_ncs_oper.matrix[3][1]   -0.131467446174 
_struct_ncs_oper.matrix[3][2]   -0.223633130552 
_struct_ncs_oper.matrix[3][3]   0.965766293425 
_struct_ncs_oper.vector[1]      72.1173753396 
_struct_ncs_oper.vector[2]      76.8624660502 
_struct_ncs_oper.vector[3]      13.6549170528 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 0 through 44 or resid 46 through 198 or resid 202))
;
ens_1 d_2 
;(chain "B" and (resid 0 through 44 or resid 46 through 198 or resid 202))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A MET 1  . A LYS 45  . A MET 0  A LYS 44  ? ? 
ens_1 d_1 2 A GLN 47 . A LYS 199 . A GLN 46 A LYS 198 ? ? 
ens_1 d_2 1 B MET 1  . B LYS 45  . B MET 0  B LYS 44  ? ? 
ens_1 d_2 2 B GLN 47 . B LYS 199 . B GLN 46 B LYS 198 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     9BWQ 
_struct.title                        'X-ray Counterpart to the Neutron Structure of Peroxide-Soaked Tyr34Phe MnSOD' 
_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        9BWQ 
_struct_keywords.text            'Oxidoreductase, MnSOD, SOD2, PCET' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 2 ? 
I N N 4 ? 
J N N 6 ? 
K N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODM_HUMAN 
_struct_ref.pdbx_db_accession          P04179 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN
LSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDV
WEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
;
_struct_ref.pdbx_align_begin           25 
# 
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 9BWQ A 2 ? 199 ? P04179 25 ? 222 ? 1 198 
2 1 9BWQ B 2 ? 199 ? P04179 25 ? 222 ? 1 198 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BWQ MET A 1  ? UNP P04179 ?   ?  'initiating methionine' 0  1 
1 9BWQ PHE A 35 ? UNP P04179 TYR 58 'engineered mutation'   34 2 
2 9BWQ MET B 1  ? UNP P04179 ?   ?  'initiating methionine' 0  3 
2 9BWQ PHE B 35 ? UNP P04179 TYR 58 'engineered mutation'   34 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     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)' 2650  ? 
1 MORE         -27   ? 
1 'SSA (A^2)'  18710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_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 ASN A 20  ? LYS A 30  ? ASN A 19  LYS A 29  1 ? 11 
HELX_P HELX_P2  AA2 LYS A 30  ? LYS A 52  ? LYS A 29  LYS A 51  1 ? 23 
HELX_P HELX_P3  AA3 ASP A 54  ? LEU A 61  ? ASP A 53  LEU A 60  1 ? 8  
HELX_P HELX_P4  AA4 LEU A 61  ? LEU A 82  ? LEU A 60  LEU A 81  1 ? 22 
HELX_P HELX_P5  AA5 LYS A 91  ? GLY A 103 ? LYS A 90  GLY A 102 1 ? 13 
HELX_P HELX_P6  AA6 SER A 104 ? GLY A 118 ? SER A 103 GLY A 117 1 ? 15 
HELX_P HELX_P7  AA7 PRO A 146 ? GLY A 152 ? PRO A 145 GLY A 151 1 ? 7  
HELX_P HELX_P8  AA8 TRP A 162 ? ALA A 165 ? TRP A 161 ALA A 164 5 ? 4  
HELX_P HELX_P9  AA9 TYR A 166 ? LYS A 171 ? TYR A 165 LYS A 170 1 ? 6  
HELX_P HELX_P10 AB1 VAL A 173 ? TRP A 182 ? VAL A 172 TRP A 181 1 ? 10 
HELX_P HELX_P11 AB2 ASN A 183 ? ILE A 185 ? ASN A 182 ILE A 184 5 ? 3  
HELX_P HELX_P12 AB3 ASN A 186 ? LYS A 198 ? ASN A 185 LYS A 197 1 ? 13 
HELX_P HELX_P13 AB4 ASN B 20  ? LYS B 30  ? ASN B 19  LYS B 29  1 ? 11 
HELX_P HELX_P14 AB5 LYS B 30  ? GLY B 53  ? LYS B 29  GLY B 52  1 ? 24 
HELX_P HELX_P15 AB6 ASP B 54  ? ASN B 81  ? ASP B 53  ASN B 80  1 ? 28 
HELX_P HELX_P16 AB7 LYS B 91  ? GLY B 103 ? LYS B 90  GLY B 102 1 ? 13 
HELX_P HELX_P17 AB8 SER B 104 ? GLY B 118 ? SER B 103 GLY B 117 1 ? 15 
HELX_P HELX_P18 AB9 PRO B 146 ? GLY B 152 ? PRO B 145 GLY B 151 1 ? 7  
HELX_P HELX_P19 AC1 TRP B 162 ? ALA B 165 ? TRP B 161 ALA B 164 5 ? 4  
HELX_P HELX_P20 AC2 TYR B 166 ? LYS B 171 ? TYR B 165 LYS B 170 1 ? 6  
HELX_P HELX_P21 AC3 VAL B 173 ? TRP B 182 ? VAL B 172 TRP B 181 1 ? 10 
HELX_P HELX_P22 AC4 ASN B 183 ? ILE B 185 ? ASN B 182 ILE B 184 5 ? 3  
HELX_P HELX_P23 AC5 ASN B 186 ? LYS B 198 ? ASN B 185 LYS B 197 1 ? 13 
# 
_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 
metalc1  metalc ? ? A GLY 13  O   ? ? ? 1_555 G K   .   K  ? ? A GLY 12  A K   205 1_555 ? ? ? ? ? ? ? 3.058 ? ? 
metalc2  metalc ? ? A HIS 27  NE2 ? ? ? 1_555 C MN  .   MN ? ? A HIS 26  A MN  201 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc3  metalc ? ? A HIS 75  NE2 ? ? ? 1_555 C MN  .   MN ? ? A HIS 74  A MN  201 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc4  metalc ? ? A ASP 160 OD2 ? ? ? 1_555 C MN  .   MN ? ? A ASP 159 A MN  201 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc5  metalc ? ? A HIS 164 NE2 ? ? ? 1_555 C MN  .   MN ? ? A HIS 163 A MN  201 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc6  metalc ? ? C MN  .   MN  ? ? ? 1_555 D PEO .   O1 A ? A MN  201 A PEO 202 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc7  metalc ? ? C MN  .   MN  ? ? ? 1_555 D PEO .   O2 A ? A MN  201 A PEO 202 1_555 ? ? ? ? ? ? ? 1.979 ? ? 
metalc8  metalc ? ? C MN  .   MN  ? ? ? 1_555 J HOH .   O  B ? A MN  201 A HOH 388 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc9  metalc ? ? G K   .   K   ? ? ? 1_555 J HOH .   O  ? ? A K   205 A HOH 358 1_555 ? ? ? ? ? ? ? 2.797 ? ? 
metalc10 metalc ? ? G K   .   K   ? ? ? 1_555 J HOH .   O  ? ? A K   205 A HOH 451 1_555 ? ? ? ? ? ? ? 2.952 ? ? 
metalc11 metalc ? ? G K   .   K   ? ? ? 1_455 B GLY 86  O  ? ? A K   205 B GLY 85  1_555 ? ? ? ? ? ? ? 2.893 ? ? 
metalc12 metalc ? ? G K   .   K   ? ? ? 1_455 B ASN 183 O  ? ? A K   205 B ASN 182 1_555 ? ? ? ? ? ? ? 2.739 ? ? 
metalc13 metalc ? ? G K   .   K   ? ? ? 1_555 K HOH .   O  ? ? A K   205 B HOH 367 1_655 ? ? ? ? ? ? ? 2.851 ? ? 
metalc14 metalc ? ? G K   .   K   ? ? ? 1_555 K HOH .   O  ? ? A K   205 B HOH 387 1_655 ? ? ? ? ? ? ? 3.164 ? ? 
metalc15 metalc ? ? G K   .   K   ? ? ? 1_555 K HOH .   O  ? ? A K   205 B HOH 477 1_655 ? ? ? ? ? ? ? 2.852 ? ? 
metalc16 metalc ? ? B HIS 27  NE2 ? ? ? 1_555 H MN  .   MN ? ? B HIS 26  B MN  201 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc17 metalc ? ? B HIS 75  NE2 ? ? ? 1_555 H MN  .   MN ? ? B HIS 74  B MN  201 1_555 ? ? ? ? ? ? ? 2.160 ? ? 
metalc18 metalc ? ? B ASP 160 OD2 ? ? ? 1_555 H MN  .   MN ? ? B ASP 159 B MN  201 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc19 metalc ? ? B HIS 164 NE2 ? ? ? 1_555 H MN  .   MN ? ? B HIS 163 B MN  201 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc20 metalc ? ? H MN  .   MN  ? ? ? 1_555 K HOH .   O  ? ? B MN  201 B HOH 402 1_555 ? ? ? ? ? ? ? 1.952 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? J HOH .   ? A HOH 358 ? 1_555 71.6  ? 
2  O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? J HOH .   ? A HOH 451 ? 1_555 80.6  ? 
3  O   ? J HOH .   ? A HOH 358 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? J HOH .   ? A HOH 451 ? 1_555 80.7  ? 
4  O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B GLY 86  ? B GLY 85  ? 1_555 17.1  ? 
5  O   ? J HOH .   ? A HOH 358 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B GLY 86  ? B GLY 85  ? 1_555 64.5  ? 
6  O   ? J HOH .   ? A HOH 451 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B GLY 86  ? B GLY 85  ? 1_555 64.7  ? 
7  O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B ASN 183 ? B ASN 182 ? 1_555 15.1  ? 
8  O   ? J HOH .   ? A HOH 358 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B ASN 183 ? B ASN 182 ? 1_555 66.1  ? 
9  O   ? J HOH .   ? A HOH 451 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B ASN 183 ? B ASN 182 ? 1_555 66.2  ? 
10 O   ? B GLY 86  ? B GLY 85  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? B ASN 183 ? B ASN 182 ? 1_555 2.3   ? 
11 O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 367 ? 1_655 93.4  ? 
12 O   ? J HOH .   ? A HOH 358 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 367 ? 1_655 149.4 ? 
13 O   ? J HOH .   ? A HOH 451 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 367 ? 1_655 70.3  ? 
14 O   ? B GLY 86  ? B GLY 85  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 367 ? 1_655 93.4  ? 
15 O   ? B ASN 183 ? B ASN 182 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 367 ? 1_655 92.5  ? 
16 O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 387 ? 1_655 54.8  ? 
17 O   ? J HOH .   ? A HOH 358 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 387 ? 1_655 113.0 ? 
18 O   ? J HOH .   ? A HOH 451 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 387 ? 1_655 121.0 ? 
19 O   ? B GLY 86  ? B GLY 85  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 387 ? 1_655 71.1  ? 
20 O   ? B ASN 183 ? B ASN 182 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 387 ? 1_655 68.8  ? 
21 O   ? K HOH .   ? B HOH 367 ? 1_655 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 387 ? 1_655 75.6  ? 
22 O   ? A GLY 13  ? A GLY 12  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 83.6  ? 
23 O   ? J HOH .   ? A HOH 358 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 69.9  ? 
24 O   ? J HOH .   ? A HOH 451 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 149.8 ? 
25 O   ? B GLY 86  ? B GLY 85  ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 95.4  ? 
26 O   ? B ASN 183 ? B ASN 182 ? 1_555 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 94.6  ? 
27 O   ? K HOH .   ? B HOH 367 ? 1_655 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 136.5 ? 
28 O   ? K HOH .   ? B HOH 387 ? 1_655 K  ? G K  . ? A K  205 ? 1_555 O   ? K HOH .   ? B HOH 477 ? 1_655 67.3  ? 
29 NE2 ? A HIS 27  ? A HIS 26  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 NE2 ? A HIS 75  ? A HIS 74  ? 1_555 89.6  ? 
30 NE2 ? A HIS 27  ? A HIS 26  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 OD2 ? A ASP 160 ? A ASP 159 ? 1_555 83.9  ? 
31 NE2 ? A HIS 75  ? A HIS 74  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 OD2 ? A ASP 160 ? A ASP 159 ? 1_555 107.6 ? 
32 NE2 ? A HIS 27  ? A HIS 26  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 NE2 ? A HIS 164 ? A HIS 163 ? 1_555 91.3  ? 
33 NE2 ? A HIS 75  ? A HIS 74  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 NE2 ? A HIS 164 ? A HIS 163 ? 1_555 132.3 ? 
34 OD2 ? A ASP 160 ? A ASP 159 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 NE2 ? A HIS 164 ? A HIS 163 ? 1_555 120.0 ? 
35 NE2 ? A HIS 27  ? A HIS 26  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O1  A D PEO .   ? A PEO 202 ? 1_555 156.4 ? 
36 NE2 ? A HIS 75  ? A HIS 74  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O1  A D PEO .   ? A PEO 202 ? 1_555 102.8 ? 
37 OD2 ? A ASP 160 ? A ASP 159 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O1  A D PEO .   ? A PEO 202 ? 1_555 73.3  ? 
38 NE2 ? A HIS 164 ? A HIS 163 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O1  A D PEO .   ? A PEO 202 ? 1_555 94.8  ? 
39 NE2 ? A HIS 27  ? A HIS 26  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O2  A D PEO .   ? A PEO 202 ? 1_555 163.0 ? 
40 NE2 ? A HIS 75  ? A HIS 74  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O2  A D PEO .   ? A PEO 202 ? 1_555 74.2  ? 
41 OD2 ? A ASP 160 ? A ASP 159 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O2  A D PEO .   ? A PEO 202 ? 1_555 105.6 ? 
42 NE2 ? A HIS 164 ? A HIS 163 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O2  A D PEO .   ? A PEO 202 ? 1_555 95.7  ? 
43 O1  A D PEO .   ? A PEO 202 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O2  A D PEO .   ? A PEO 202 ? 1_555 38.1  ? 
44 NE2 ? A HIS 27  ? A HIS 26  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O   B J HOH .   ? A HOH 388 ? 1_555 172.6 ? 
45 NE2 ? A HIS 75  ? A HIS 74  ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O   B J HOH .   ? A HOH 388 ? 1_555 95.7  ? 
46 OD2 ? A ASP 160 ? A ASP 159 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O   B J HOH .   ? A HOH 388 ? 1_555 89.6  ? 
47 NE2 ? A HIS 164 ? A HIS 163 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O   B J HOH .   ? A HOH 388 ? 1_555 88.8  ? 
48 O1  A D PEO .   ? A PEO 202 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O   B J HOH .   ? A HOH 388 ? 1_555 16.5  ? 
49 O2  A D PEO .   ? A PEO 202 ? 1_555 MN ? C MN . ? A MN 201 ? 1_555 O   B J HOH .   ? A HOH 388 ? 1_555 23.8  ? 
50 NE2 ? B HIS 27  ? B HIS 26  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 NE2 ? B HIS 75  ? B HIS 74  ? 1_555 88.7  ? 
51 NE2 ? B HIS 27  ? B HIS 26  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 OD2 ? B ASP 160 ? B ASP 159 ? 1_555 84.6  ? 
52 NE2 ? B HIS 75  ? B HIS 74  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 OD2 ? B ASP 160 ? B ASP 159 ? 1_555 105.5 ? 
53 NE2 ? B HIS 27  ? B HIS 26  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 NE2 ? B HIS 164 ? B HIS 163 ? 1_555 90.6  ? 
54 NE2 ? B HIS 75  ? B HIS 74  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 NE2 ? B HIS 164 ? B HIS 163 ? 1_555 134.3 ? 
55 OD2 ? B ASP 160 ? B ASP 159 ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 NE2 ? B HIS 164 ? B HIS 163 ? 1_555 119.8 ? 
56 NE2 ? B HIS 27  ? B HIS 26  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 O   ? K HOH .   ? B HOH 402 ? 1_555 174.1 ? 
57 NE2 ? B HIS 75  ? B HIS 74  ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 O   ? K HOH .   ? B HOH 402 ? 1_555 93.7  ? 
58 OD2 ? B ASP 160 ? B ASP 159 ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 O   ? K HOH .   ? B HOH 402 ? 1_555 89.6  ? 
59 NE2 ? B HIS 164 ? B HIS 163 ? 1_555 MN ? H MN . ? B MN 201 ? 1_555 O   ? K HOH .   ? B HOH 402 ? 1_555 91.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 16 A . ? GLU 15 A PRO 17 A ? PRO 16 A 1 5.16 
2 GLU 16 B . ? GLU 15 B PRO 17 B ? PRO 16 B 1 2.14 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? 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 HIS A 135 ? PRO A 142 ? HIS A 134 PRO A 141 
AA1 2 GLY A 123 ? ASN A 130 ? GLY A 122 ASN A 129 
AA1 3 ILE A 154 ? ASP A 160 ? ILE A 153 ASP A 159 
AA2 1 HIS B 135 ? PRO B 142 ? HIS B 134 PRO B 141 
AA2 2 GLY B 123 ? ASN B 130 ? GLY B 122 ASN B 129 
AA2 3 ILE B 154 ? ASP B 160 ? ILE B 153 ASP B 159 
# 
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 O GLN A 137 ? O GLN A 136 N GLY A 128 ? N GLY A 127 
AA1 2 3 N GLY A 125 ? N GLY A 124 O ILE A 159 ? O ILE A 158 
AA2 1 2 O GLN B 137 ? O GLN B 136 N GLY B 128 ? N GLY B 127 
AA2 2 3 N GLY B 125 ? N GLY B 124 O ILE B 159 ? O ILE B 158 
# 
_pdbx_entry_details.entry_id                   9BWQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 ASN A 142 ? ? 56.74   -123.89 
2 1 TYR A 165 ? ? -147.42 -16.26  
3 1 LYS A 170 ? ? 53.73   -136.07 
4 1 ASN B 142 ? ? 56.83   -124.44 
5 1 TYR B 165 ? ? -148.15 -16.07  
6 1 LYS B 170 ? ? 53.64   -135.32 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 334 ? J HOH . 
2 1 A HOH 353 ? J HOH . 
3 1 B HOH 324 ? K HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z          
2  x-y,x,z+1/6    
3  y,-x+y,z+5/6   
4  -y,x-y,z+1/3   
5  -x+y,-x,z+2/3  
6  x-y,-y,-z      
7  -x,-x+y,-z+2/3 
8  -x,-y,z+1/2    
9  y,x,-z+1/3     
10 -y,-x,-z+5/6   
11 -x+y,y,-z+1/2  
12 x,x-y,-z+1/6   
# 
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 582 ? 5.86 . 
2 1 O ? B HOH 589 ? 6.39 . 
# 
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 
K   K    K  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MN  MN   MN N N 251 
PEO O1   O  N N 252 
PEO O2   O  N N 253 
PEO HO1  H  N N 254 
PEO HO2  H  N N 255 
PHE N    N  N N 256 
PHE CA   C  N S 257 
PHE C    C  N N 258 
PHE O    O  N N 259 
PHE CB   C  N N 260 
PHE CG   C  Y N 261 
PHE CD1  C  Y N 262 
PHE CD2  C  Y N 263 
PHE CE1  C  Y N 264 
PHE CE2  C  Y N 265 
PHE CZ   C  Y N 266 
PHE OXT  O  N N 267 
PHE H    H  N N 268 
PHE H2   H  N N 269 
PHE HA   H  N N 270 
PHE HB2  H  N N 271 
PHE HB3  H  N N 272 
PHE HD1  H  N N 273 
PHE HD2  H  N N 274 
PHE HE1  H  N N 275 
PHE HE2  H  N N 276 
PHE HZ   H  N N 277 
PHE HXT  H  N N 278 
PO4 P    P  N N 279 
PO4 O1   O  N N 280 
PO4 O2   O  N N 281 
PO4 O3   O  N N 282 
PO4 O4   O  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
# 
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 
PEO O1  O2   sing N N 237 
PEO O1  HO1  sing N N 238 
PEO O2  HO2  sing N N 239 
PHE N   CA   sing N N 240 
PHE N   H    sing N N 241 
PHE N   H2   sing N N 242 
PHE CA  C    sing N N 243 
PHE CA  CB   sing N N 244 
PHE CA  HA   sing N N 245 
PHE C   O    doub N N 246 
PHE C   OXT  sing N N 247 
PHE CB  CG   sing N N 248 
PHE CB  HB2  sing N N 249 
PHE CB  HB3  sing N N 250 
PHE CG  CD1  doub Y N 251 
PHE CG  CD2  sing Y N 252 
PHE CD1 CE1  sing Y N 253 
PHE CD1 HD1  sing N N 254 
PHE CD2 CE2  doub Y N 255 
PHE CD2 HD2  sing N N 256 
PHE CE1 CZ   doub Y N 257 
PHE CE1 HE1  sing N N 258 
PHE CE2 CZ   sing Y N 259 
PHE CE2 HE2  sing N N 260 
PHE CZ  HZ   sing N N 261 
PHE OXT HXT  sing N N 262 
PO4 P   O1   doub N N 263 
PO4 P   O2   sing N N 264 
PO4 P   O3   sing N N 265 
PO4 P   O4   sing N N 266 
PRO N   CA   sing N N 267 
PRO N   CD   sing N N 268 
PRO N   H    sing N N 269 
PRO CA  C    sing N N 270 
PRO CA  CB   sing N N 271 
PRO CA  HA   sing N N 272 
PRO C   O    doub N N 273 
PRO C   OXT  sing N N 274 
PRO CB  CG   sing N N 275 
PRO CB  HB2  sing N N 276 
PRO CB  HB3  sing N N 277 
PRO CG  CD   sing N N 278 
PRO CG  HG2  sing N N 279 
PRO CG  HG3  sing N N 280 
PRO CD  HD2  sing N N 281 
PRO CD  HD3  sing N N 282 
PRO OXT HXT  sing N N 283 
SER N   CA   sing N N 284 
SER N   H    sing N N 285 
SER N   H2   sing N N 286 
SER CA  C    sing N N 287 
SER CA  CB   sing N N 288 
SER CA  HA   sing N N 289 
SER C   O    doub N N 290 
SER C   OXT  sing N N 291 
SER CB  OG   sing N N 292 
SER CB  HB2  sing N N 293 
SER CB  HB3  sing N N 294 
SER OG  HG   sing N N 295 
SER OXT HXT  sing N N 296 
THR N   CA   sing N N 297 
THR N   H    sing N N 298 
THR N   H2   sing N N 299 
THR CA  C    sing N N 300 
THR CA  CB   sing N N 301 
THR CA  HA   sing N N 302 
THR C   O    doub N N 303 
THR C   OXT  sing N N 304 
THR CB  OG1  sing N N 305 
THR CB  CG2  sing N N 306 
THR CB  HB   sing N N 307 
THR OG1 HG1  sing N N 308 
THR CG2 HG21 sing N N 309 
THR CG2 HG22 sing N N 310 
THR CG2 HG23 sing N N 311 
THR OXT HXT  sing N N 312 
TRP N   CA   sing N N 313 
TRP N   H    sing N N 314 
TRP N   H2   sing N N 315 
TRP CA  C    sing N N 316 
TRP CA  CB   sing N N 317 
TRP CA  HA   sing N N 318 
TRP C   O    doub N N 319 
TRP C   OXT  sing N N 320 
TRP CB  CG   sing N N 321 
TRP CB  HB2  sing N N 322 
TRP CB  HB3  sing N N 323 
TRP CG  CD1  doub Y N 324 
TRP CG  CD2  sing Y N 325 
TRP CD1 NE1  sing Y N 326 
TRP CD1 HD1  sing N N 327 
TRP CD2 CE2  doub Y N 328 
TRP CD2 CE3  sing Y N 329 
TRP NE1 CE2  sing Y N 330 
TRP NE1 HE1  sing N N 331 
TRP CE2 CZ2  sing Y N 332 
TRP CE3 CZ3  doub Y N 333 
TRP CE3 HE3  sing N N 334 
TRP CZ2 CH2  doub Y N 335 
TRP CZ2 HZ2  sing N N 336 
TRP CZ3 CH2  sing Y N 337 
TRP CZ3 HZ3  sing N N 338 
TRP CH2 HH2  sing N N 339 
TRP OXT HXT  sing N N 340 
TYR N   CA   sing N N 341 
TYR N   H    sing N N 342 
TYR N   H2   sing N N 343 
TYR CA  C    sing N N 344 
TYR CA  CB   sing N N 345 
TYR CA  HA   sing N N 346 
TYR C   O    doub N N 347 
TYR C   OXT  sing N N 348 
TYR CB  CG   sing N N 349 
TYR CB  HB2  sing N N 350 
TYR CB  HB3  sing N N 351 
TYR CG  CD1  doub Y N 352 
TYR CG  CD2  sing Y N 353 
TYR CD1 CE1  sing Y N 354 
TYR CD1 HD1  sing N N 355 
TYR CD2 CE2  doub Y N 356 
TYR CD2 HD2  sing N N 357 
TYR CE1 CZ   doub Y N 358 
TYR CE1 HE1  sing N N 359 
TYR CE2 CZ   sing Y N 360 
TYR CE2 HE2  sing N N 361 
TYR CZ  OH   sing N N 362 
TYR OH  HH   sing N N 363 
TYR OXT HXT  sing N N 364 
VAL N   CA   sing N N 365 
VAL N   H    sing N N 366 
VAL N   H2   sing N N 367 
VAL CA  C    sing N N 368 
VAL CA  CB   sing N N 369 
VAL CA  HA   sing N N 370 
VAL C   O    doub N N 371 
VAL C   OXT  sing N N 372 
VAL CB  CG1  sing N N 373 
VAL CB  CG2  sing N N 374 
VAL CB  HB   sing N N 375 
VAL CG1 HG11 sing N N 376 
VAL CG1 HG12 sing N N 377 
VAL CG1 HG13 sing N N 378 
VAL CG2 HG21 sing N N 379 
VAL CG2 HG22 sing N N 380 
VAL CG2 HG23 sing N N 381 
VAL OXT HXT  sing N N 382 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R01-GM145647     1 
'National Aeronautics and Space Administration (NASA, United States)'                      'United States' 44-0307-1021-201 2 
'Department of Energy (DOE, United States)'                                                'United States' ?                3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5VF9 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 61 2 2' 
_space_group.name_Hall        'P 61 2 (x,y,z+5/12)' 
_space_group.IT_number        178 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BWQ 
_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]   0.012784 
_atom_sites.fract_transf_matrix[1][2]   0.007381 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014762 
_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]   0.004175 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ?       ? 25.62398 1.50364  ?         ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
K  ? ? 8.66788  8.58341 1.68052 ? 12.31593 0.56275  110.00227 ? 0.0 
;3-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MN ? ? 20.23591 4.67902 ?       ? 2.76514  44.01191 ?         ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ?       ? 19.97189 1.75589  ?         ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ?       ? 15.80542 1.70748  ?         ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135  5.44231 ?       ? 1.42069  35.72801 ?         ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ?       ? 1.23737  29.19336 ?         ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   ? 44.69831 31.01340 70.83911  1.000 41.10455  ? 0   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 43.38764 30.38481 70.94810  1.000 46.30014  ? 0   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 43.34873 29.35593 72.07535  1.000 49.06926  ? 0   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 42.38669 29.29812 72.84259  1.000 66.82503  ? 0   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 43.00112 29.72178 69.62223  1.000 58.71305  ? 0   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 41.74757 28.86010 69.69593  1.000 74.87104  ? 0   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 41.24353 28.19874 68.09388  1.000 120.36308 ? 0   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 41.22298 29.68854 67.09849  1.000 78.30711  ? 0   MET A CE  1 
ATOM   9    N  N   . LYS A 1 2   ? 44.40160 28.54998 72.17387  1.000 32.57118  ? 1   LYS A N   1 
ATOM   10   C  CA  . LYS A 1 2   ? 44.50972 27.51489 73.19436  1.000 26.80915  ? 1   LYS A CA  1 
ATOM   11   C  C   . LYS A 1 2   ? 45.47263 27.93471 74.29615  1.000 20.16162  ? 1   LYS A C   1 
ATOM   12   O  O   . LYS A 1 2   ? 46.56694 28.43573 74.01534  1.000 26.46310  ? 1   LYS A O   1 
ATOM   13   C  CB  . LYS A 1 2   ? 44.92338 26.16930 72.59669  1.000 28.09867  ? 1   LYS A CB  1 
ATOM   14   C  CG  . LYS A 1 2   ? 43.78559 25.45083 71.88674  1.000 32.40396  ? 1   LYS A CG  1 
ATOM   15   C  CD  . LYS A 1 2   ? 44.03862 23.95255 71.78411  1.000 27.35274  ? 1   LYS A CD  1 
ATOM   16   C  CE  . LYS A 1 2   ? 42.97351 23.27807 70.93455  1.000 27.88219  ? 1   LYS A CE  1 
ATOM   17   N  NZ  . LYS A 1 2   ? 41.60834 23.52819 71.47189  1.000 32.84690  ? 1   LYS A NZ  1 
ATOM   18   N  N   . HIS A 1 3   ? 45.04696 27.76156 75.54428  1.000 16.84356  ? 2   HIS A N   1 
ATOM   19   C  CA  . HIS A 1 3   ? 45.92764 28.01771 76.67195  1.000 19.24728  ? 2   HIS A CA  1 
ATOM   20   C  C   . HIS A 1 3   ? 47.07231 27.00925 76.66886  1.000 17.76976  ? 2   HIS A C   1 
ATOM   21   O  O   . HIS A 1 3   ? 46.93191 25.87330 76.20781  1.000 17.93458  ? 2   HIS A O   1 
ATOM   22   C  CB  . HIS A 1 3   ? 45.13713 27.90136 77.97170  1.000 17.73086  ? 2   HIS A CB  1 
ATOM   23   C  CG  . HIS A 1 3   ? 43.92138 28.77313 78.00514  1.000 16.80816  ? 2   HIS A CG  1 
ATOM   24   N  ND1 . HIS A 1 3   ? 43.98413 30.12939 78.24272  1.000 16.98607  ? 2   HIS A ND1 1 
ATOM   25   C  CD2 . HIS A 1 3   ? 42.61007 28.48124 77.83425  1.000 16.51933  ? 2   HIS A CD2 1 
ATOM   26   C  CE1 . HIS A 1 3   ? 42.76617 30.63799 78.19869  1.000 16.11507  ? 2   HIS A CE1 1 
ATOM   27   N  NE2 . HIS A 1 3   ? 41.91402 29.65738 77.96191  1.000 17.95465  ? 2   HIS A NE2 1 
ATOM   28   N  N   . SER A 1 4   ? 48.22965 27.44107 77.16639  1.000 16.64587  ? 3   SER A N   1 
ATOM   29   C  CA  . SER A 1 4   ? 49.42845 26.62009 77.08656  1.000 16.23846  ? 3   SER A CA  1 
ATOM   30   C  C   . SER A 1 4   ? 50.18928 26.62391 78.40474  1.000 15.96927  ? 3   SER A C   1 
ATOM   31   O  O   . SER A 1 4   ? 50.19978 27.61589 79.13970  1.000 15.30153  ? 3   SER A O   1 
ATOM   32   C  CB  . SER A 1 4   ? 50.34733 27.08879 75.95166  1.000 21.71700  ? 3   SER A CB  1 
ATOM   33   O  OG  . SER A 1 4   ? 50.58944 28.47772 76.05742  1.000 22.48183  ? 3   SER A OG  1 
ATOM   34   N  N   . LEU A 1 5   ? 50.83389 25.50266 78.68523  1.000 15.15832  ? 4   LEU A N   1 
ATOM   35   C  CA  . LEU A 1 5   ? 51.67209 25.38379 79.86808  1.000 15.29328  ? 4   LEU A CA  1 
ATOM   36   C  C   . LEU A 1 5   ? 52.93478 26.21518 79.68788  1.000 17.00474  ? 4   LEU A C   1 
ATOM   37   O  O   . LEU A 1 5   ? 53.72180 25.94212 78.77017  1.000 17.32241  ? 4   LEU A O   1 
ATOM   38   C  CB  . LEU A 1 5   ? 52.06070 23.92380 80.05911  1.000 17.39251  ? 4   LEU A CB  1 
ATOM   39   C  CG  . LEU A 1 5   ? 52.95634 23.63981 81.26171  1.000 14.93873  ? 4   LEU A CG  1 
ATOM   40   C  CD1 . LEU A 1 5   ? 52.21930 23.87247 82.57204  1.000 15.18978  ? 4   LEU A CD1 1 
ATOM   41   C  CD2 . LEU A 1 5   ? 53.48807 22.21223 81.18288  1.000 18.37599  ? 4   LEU A CD2 1 
ATOM   42   N  N   . PRO A 1 6   ? 53.16414 27.23071 80.51328  1.000 13.95198  ? 5   PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? 54.40853 27.99796 80.40310  1.000 16.55772  ? 5   PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? 55.56779 27.18595 80.94982  1.000 16.40603  ? 5   PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? 55.42683 26.46716 81.94217  1.000 17.74907  ? 5   PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? 54.14257 29.21839 81.28919  1.000 18.14728  ? 5   PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? 53.18018 28.69915 82.33040  1.000 15.14264  ? 5   PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? 52.30031 27.71128 81.60517  1.000 12.53781  ? 5   PRO A CD  1 
ATOM   49   N  N   . ASP A 1 7   ? 56.72386 27.31339 80.30347  1.000 18.48672  ? 6   ASP A N   1 
ATOM   50   C  CA  . ASP A 1 7   ? 57.93594 26.73318 80.86369  1.000 19.55254  ? 6   ASP A CA  1 
ATOM   51   C  C   . ASP A 1 7   ? 58.23667 27.37596 82.21004  1.000 15.78832  ? 6   ASP A C   1 
ATOM   52   O  O   . ASP A 1 7   ? 57.95167 28.55228 82.43867  1.000 18.15795  ? 6   ASP A O   1 
ATOM   53   C  CB  . ASP A 1 7   ? 59.13016 26.96023 79.93256  1.000 22.36320  ? 6   ASP A CB  1 
ATOM   54   C  CG  . ASP A 1 7   ? 59.13224 26.03341 78.73580  1.000 31.02267  ? 6   ASP A CG  1 
ATOM   55   O  OD1 . ASP A 1 7   ? 58.28757 25.11615 78.68104  1.000 30.53170  ? 6   ASP A OD1 1 
ATOM   56   O  OD2 . ASP A 1 7   ? 59.99356 26.21833 77.84961  1.000 30.86546  ? 6   ASP A OD2 1 
ATOM   57   N  N   . LEU A 1 8   ? 58.80332 26.59104 83.10939  1.000 18.05018  ? 7   LEU A N   1 
ATOM   58   C  CA  . LEU A 1 8   ? 59.32950 27.15625 84.34111  1.000 20.31329  ? 7   LEU A CA  1 
ATOM   59   C  C   . LEU A 1 8   ? 60.53876 28.01635 83.98431  1.000 16.99909  ? 7   LEU A C   1 
ATOM   60   O  O   . LEU A 1 8   ? 61.37480 27.59123 83.17824  1.000 21.77865  ? 7   LEU A O   1 
ATOM   61   C  CB  . LEU A 1 8   ? 59.76487 26.00895 85.24693  1.000 19.55726  ? 7   LEU A CB  1 
ATOM   62   C  CG  . LEU A 1 8   ? 59.85146 26.26523 86.74764  1.000 18.06072  ? 7   LEU A CG  1 
ATOM   63   C  CD1 . LEU A 1 8   ? 58.47686 26.60395 87.31226  1.000 19.79561  ? 7   LEU A CD1 1 
ATOM   64   C  CD2 . LEU A 1 8   ? 60.45350 25.06102 87.46416  1.000 18.48656  ? 7   LEU A CD2 1 
ATOM   65   N  N   . PRO A 1 9   ? 60.66433 29.22334 84.54622  1.000 19.97714  ? 8   PRO A N   1 
ATOM   66   C  CA  . PRO A 1 9   ? 61.75750 30.13377 84.17012  1.000 21.22886  ? 8   PRO A CA  1 
ATOM   67   C  C   . PRO A 1 9   ? 63.11432 29.81795 84.78601  1.000 17.46061  ? 8   PRO A C   1 
ATOM   68   O  O   . PRO A 1 9   ? 64.02366 30.65016 84.69074  1.000 19.37375  ? 8   PRO A O   1 
ATOM   69   C  CB  . PRO A 1 9   ? 61.23710 31.50813 84.62506  1.000 21.57620  ? 8   PRO A CB  1 
ATOM   70   C  CG  . PRO A 1 9   ? 60.29113 31.22200 85.71376  1.000 24.01357  ? 8   PRO A CG  1 
ATOM   71   C  CD  . PRO A 1 9   ? 59.72597 29.84162 85.49909  1.000 21.16283  ? 8   PRO A CD  1 
ATOM   72   N  N   . TYR A 1 10  ? 63.26369 28.66579 85.43401  1.000 16.56632  ? 9   TYR A N   1 
ATOM   73   C  CA  . TYR A 1 10  ? 64.50423 28.26592 86.08810  1.000 15.57024  ? 9   TYR A CA  1 
ATOM   74   C  C   . TYR A 1 10  ? 64.49791 26.74576 86.17985  1.000 16.26576  ? 9   TYR A C   1 
ATOM   75   O  O   . TYR A 1 10  ? 63.48888 26.09084 85.90582  1.000 17.46596  ? 9   TYR A O   1 
ATOM   76   C  CB  . TYR A 1 10  ? 64.62229 28.90450 87.47967  1.000 17.71560  ? 9   TYR A CB  1 
ATOM   77   C  CG  . TYR A 1 10  ? 63.28069 29.03244 88.16458  1.000 18.09570  ? 9   TYR A CG  1 
ATOM   78   C  CD1 . TYR A 1 10  ? 62.66607 27.93331 88.74198  1.000 19.61208  ? 9   TYR A CD1 1 
ATOM   79   C  CD2 . TYR A 1 10  ? 62.61593 30.25243 88.20564  1.000 15.34553  ? 9   TYR A CD2 1 
ATOM   80   C  CE1 . TYR A 1 10  ? 61.42471 28.04225 89.34714  1.000 19.48086  ? 9   TYR A CE1 1 
ATOM   81   C  CE2 . TYR A 1 10  ? 61.37824 30.37418 88.81404  1.000 15.73084  ? 9   TYR A CE2 1 
ATOM   82   C  CZ  . TYR A 1 10  ? 60.78834 29.26396 89.37536  1.000 15.86379  ? 9   TYR A CZ  1 
ATOM   83   O  OH  . TYR A 1 10  ? 59.55706 29.37376 89.97519  1.000 17.01511  ? 9   TYR A OH  1 
ATOM   84   N  N   . ASP A 1 11  ? 65.63776 26.18841 86.57061  1.000 15.88581  ? 10  ASP A N   1 
ATOM   85   C  CA  . ASP A 1 11  ? 65.76282 24.74208 86.70630  1.000 16.07129  ? 10  ASP A CA  1 
ATOM   86   C  C   . ASP A 1 11  ? 64.89500 24.22097 87.84917  1.000 13.88319  ? 10  ASP A C   1 
ATOM   87   O  O   . ASP A 1 11  ? 64.62234 24.92719 88.82277  1.000 14.41051  ? 10  ASP A O   1 
ATOM   88   C  CB  . ASP A 1 11  ? 67.22894 24.37022 86.94985  1.000 15.11659  ? 10  ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 11  ? 67.47029 22.86696 86.94330  1.000 20.86062  ? 10  ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 11  ? 67.46725 22.27420 85.84598  1.000 29.27827  ? 10  ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 11  ? 67.70189 22.28630 88.02656  1.000 22.14402  ? 10  ASP A OD2 1 
ATOM   92   N  N   . TYR A 1 12  ? 64.46902 22.95632 87.72736  1.000 15.15456  ? 11  TYR A N   1 
ATOM   93   C  CA  . TYR A 1 12  ? 63.64746 22.34824 88.76987  1.000 17.59094  ? 11  TYR A CA  1 
ATOM   94   C  C   . TYR A 1 12  ? 64.33199 22.37029 90.12983  1.000 14.17036  ? 11  TYR A C   1 
ATOM   95   O  O   . TYR A 1 12  ? 63.65255 22.41619 91.16153  1.000 14.64029  ? 11  TYR A O   1 
ATOM   96   C  CB  . TYR A 1 12  ? 63.28803 20.90877 88.39168  1.000 17.64484  ? 11  TYR A CB  1 
ATOM   97   C  CG  . TYR A 1 12  ? 62.20784 20.80510 87.34084  1.000 22.94840  ? 11  TYR A CG  1 
ATOM   98   C  CD1 . TYR A 1 12  ? 61.10933 21.64050 87.37931  1.000 17.02823  ? 11  TYR A CD1 1 
ATOM   99   C  CD2 . TYR A 1 12  ? 62.28406 19.86827 86.31547  1.000 27.94455  ? 11  TYR A CD2 1 
ATOM   100  C  CE1 . TYR A 1 12  ? 60.11249 21.56738 86.42964  1.000 29.08654  ? 11  TYR A CE1 1 
ATOM   101  C  CE2 . TYR A 1 12  ? 61.28161 19.78178 85.35372  1.000 27.77522  ? 11  TYR A CE2 1 
ATOM   102  C  CZ  . TYR A 1 12  ? 60.19915 20.63880 85.41975  1.000 26.06555  ? 11  TYR A CZ  1 
ATOM   103  O  OH  . TYR A 1 12  ? 59.19030 20.57686 84.47990  1.000 33.30870  ? 11  TYR A OH  1 
ATOM   104  N  N   . GLY A 1 13  ? 65.66129 22.32098 90.16157  1.000 14.54331  ? 12  GLY A N   1 
ATOM   105  C  CA  . GLY A 1 13  ? 66.40370 22.37102 91.40252  1.000 13.77264  ? 12  GLY A CA  1 
ATOM   106  C  C   . GLY A 1 13  ? 66.90176 23.73999 91.80870  1.000 13.98162  ? 12  GLY A C   1 
ATOM   107  O  O   . GLY A 1 13  ? 67.69853 23.83400 92.75037  1.000 14.81206  ? 12  GLY A O   1 
ATOM   108  N  N   . ALA A 1 14  ? 66.44916 24.80598 91.14110  1.000 13.76922  ? 13  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 66.98042 26.14642 91.36917  1.000 13.39474  ? 13  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 66.57822 26.72578 92.71910  1.000 13.87874  ? 13  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 67.22806 27.66825 93.19242  1.000 14.22305  ? 13  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 66.47785 27.08164 90.26892  1.000 13.68671  ? 13  ALA A CB  1 
ATOM   113  N  N   . LEU A 1 15  ? 65.51136 26.21312 93.33424  1.000 14.65015  ? 14  LEU A N   1 
ATOM   114  C  CA  . LEU A 1 15  ? 65.01210 26.75157 94.59102  1.000 13.28696  ? 14  LEU A CA  1 
ATOM   115  C  C   . LEU A 1 15  ? 65.43011 25.93006 95.80194  1.000 11.73821  ? 14  LEU A C   1 
ATOM   116  O  O   . LEU A 1 15  ? 64.99445 26.23157 96.91593  1.000 14.11285  ? 14  LEU A O   1 
ATOM   117  C  CB  . LEU A 1 15  ? 63.48119 26.90100 94.54100  1.000 13.01140  ? 14  LEU A CB  1 
ATOM   118  C  CG  . LEU A 1 15  ? 62.93484 27.67926 93.33903  1.000 13.44812  ? 14  LEU A CG  1 
ATOM   119  C  CD1 . LEU A 1 15  ? 61.42629 27.87297 93.48302  1.000 13.39176  ? 14  LEU A CD1 1 
ATOM   120  C  CD2 . LEU A 1 15  ? 63.64182 29.02136 93.15444  1.000 13.68867  ? 14  LEU A CD2 1 
ATOM   121  N  N   . GLU A 1 16  ? 66.26241 24.90428 95.61478  1.000 12.46921  ? 15  GLU A N   1 
ATOM   122  C  CA  . GLU A 1 16  ? 66.79599 24.16350 96.74842  1.000 13.37981  ? 15  GLU A CA  1 
ATOM   123  C  C   . GLU A 1 16  ? 67.73923 25.04778 97.56841  1.000 12.00779  ? 15  GLU A C   1 
ATOM   124  O  O   . GLU A 1 16  ? 68.48283 25.86293 97.01434  1.000 15.80620  ? 15  GLU A O   1 
ATOM   125  C  CB  . GLU A 1 16  ? 67.51196 22.90406 96.26733  1.000 14.97567  ? 15  GLU A CB  1 
ATOM   126  C  CG  . GLU A 1 16  ? 66.52918 21.89800 95.66157  1.000 16.26272  ? 15  GLU A CG  1 
ATOM   127  C  CD  . GLU A 1 16  ? 67.15214 20.57741 95.26082  1.000 19.12173  ? 15  GLU A CD  1 
ATOM   128  O  OE1 . GLU A 1 16  ? 68.39058 20.50244 95.11680  1.000 18.47945  ? 15  GLU A OE1 1 
ATOM   129  O  OE2 . GLU A 1 16  ? 66.39040 19.60459 95.07523  1.000 18.95840  ? 15  GLU A OE2 1 
ATOM   130  N  N   . PRO A 1 17  ? 67.75908 24.87858 98.89727  1.000 15.08701  ? 16  PRO A N   1 
ATOM   131  C  CA  . PRO A 1 17  ? 67.05133 23.86074 99.68661  1.000 17.02075  ? 16  PRO A CA  1 
ATOM   132  C  C   . PRO A 1 17  ? 65.62449 24.22832 100.11750 1.000 17.12952  ? 16  PRO A C   1 
ATOM   133  O  O   . PRO A 1 17  ? 65.00546 23.47272 100.86237 1.000 19.35431  ? 16  PRO A O   1 
ATOM   134  C  CB  . PRO A 1 17  ? 67.94151 23.72683 100.91972 1.000 16.13165  ? 16  PRO A CB  1 
ATOM   135  C  CG  . PRO A 1 17  ? 68.47296 25.11322 101.12193 1.000 20.34661  ? 16  PRO A CG  1 
ATOM   136  C  CD  . PRO A 1 17  ? 68.67311 25.68111 99.73433  1.000 15.99511  ? 16  PRO A CD  1 
ATOM   137  N  N   . HIS A 1 18  ? 65.12370 25.37999 99.66786  1.000 12.86774  ? 17  HIS A N   1 
ATOM   138  C  CA  . HIS A 1 18  ? 63.84554 25.88296 100.16887 1.000 12.70212  ? 17  HIS A CA  1 
ATOM   139  C  C   . HIS A 1 18  ? 62.65632 25.08943 99.63280  1.000 14.17996  ? 17  HIS A C   1 
ATOM   140  O  O   . HIS A 1 18  ? 61.74438 24.75099 100.39204 1.000 16.66834  ? 17  HIS A O   1 
ATOM   141  C  CB  . HIS A 1 18  ? 63.72471 27.37313 99.86045  1.000 13.48532  ? 17  HIS A CB  1 
ATOM   142  C  CG  . HIS A 1 18  ? 64.94569 28.14117 100.24523 1.000 15.34839  ? 17  HIS A CG  1 
ATOM   143  N  ND1 . HIS A 1 18  ? 65.30897 28.32463 101.56058 1.000 15.68653  ? 17  HIS A ND1 1 
ATOM   144  C  CD2 . HIS A 1 18  ? 65.91863 28.71311 99.49926  1.000 17.63793  ? 17  HIS A CD2 1 
ATOM   145  C  CE1 . HIS A 1 18  ? 66.44600 28.99544 101.61035 1.000 17.74778  ? 17  HIS A CE1 1 
ATOM   146  N  NE2 . HIS A 1 18  ? 66.83767 29.24339 100.37368 1.000 16.99288  ? 17  HIS A NE2 1 
ATOM   147  N  N   . ILE A 1 19  ? 62.63706 24.79687 98.33573  1.000 14.42602  ? 18  ILE A N   1 
ATOM   148  C  CA  . ILE A 1 19  ? 61.64061 23.91163 97.73458  1.000 14.11776  ? 18  ILE A CA  1 
ATOM   149  C  C   . ILE A 1 19  ? 62.39124 22.94093 96.83530  1.000 16.47809  ? 18  ILE A C   1 
ATOM   150  O  O   . ILE A 1 19  ? 63.11908 23.37271 95.93064  1.000 15.24732  ? 18  ILE A O   1 
ATOM   151  C  CB  . ILE A 1 19  ? 60.58152 24.68128 96.92653  1.000 14.31689  ? 18  ILE A CB  1 
ATOM   152  C  CG1 . ILE A 1 19  ? 59.93231 25.77840 97.77212  1.000 14.14825  ? 18  ILE A CG1 1 
ATOM   153  C  CG2 . ILE A 1 19  ? 59.52195 23.70566 96.42028  1.000 15.33040  ? 18  ILE A CG2 1 
ATOM   154  C  CD1 . ILE A 1 19  ? 59.04744 26.71048 96.97695  1.000 15.24180  ? 18  ILE A CD1 1 
ATOM   155  N  N   . ASN A 1 20  ? 62.24450 21.64136 97.09199  1.000 14.17678  ? 19  ASN A N   1 
ATOM   156  C  CA  . ASN A 1 20  ? 63.11614 20.69562 96.41287  1.000 15.50167  ? 19  ASN A CA  1 
ATOM   157  C  C   . ASN A 1 20  ? 62.68242 20.43688 94.96521  1.000 14.70776  ? 19  ASN A C   1 
ATOM   158  O  O   . ASN A 1 20  ? 61.56772 20.76031 94.53455  1.000 13.66349  ? 19  ASN A O   1 
ATOM   159  C  CB  . ASN A 1 20  ? 63.34338 19.41963 97.23770  1.000 15.72320  ? 19  ASN A CB  1 
ATOM   160  C  CG  . ASN A 1 20  ? 62.13540 18.48976 97.28512  1.000 20.22442  ? 19  ASN A CG  1 
ATOM   161  O  OD1 . ASN A 1 20  ? 61.33331 18.41272 96.35397  1.000 19.59949  ? 19  ASN A OD1 1 
ATOM   162  N  ND2 . ASN A 1 20  ? 62.02528 17.74608 98.38185  1.000 17.96475  ? 19  ASN A ND2 1 
ATOM   163  N  N   . ALA A 1 21  ? 63.59978 19.82885 94.21295  1.000 15.46086  ? 20  ALA A N   1 
ATOM   164  C  CA  . ALA A 1 21  ? 63.39126 19.62226 92.78471  1.000 13.82476  ? 20  ALA A CA  1 
ATOM   165  C  C   . ALA A 1 21  ? 62.27550 18.62804 92.50287  1.000 13.63210  ? 20  ALA A C   1 
ATOM   166  O  O   . ALA A 1 21  ? 61.60122 18.74000 91.47072  1.000 15.56334  ? 20  ALA A O   1 
ATOM   167  C  CB  . ALA A 1 21  ? 64.68357 19.13517 92.13423  1.000 12.92841  ? 20  ALA A CB  1 
ATOM   168  N  N   . GLN A 1 22  ? 62.08041 17.63628 93.37640  1.000 13.36315  ? 21  GLN A N   1 
ATOM   169  C  CA  . GLN A 1 22  ? 60.98817 16.69459 93.15339  1.000 14.91642  ? 21  GLN A CA  1 
ATOM   170  C  C   . GLN A 1 22  ? 59.64526 17.41198 93.18814  1.000 13.47428  ? 21  GLN A C   1 
ATOM   171  O  O   . GLN A 1 22  ? 58.78351 17.17727 92.33030  1.000 14.41343  ? 21  GLN A O   1 
ATOM   172  C  CB  . GLN A 1 22  ? 61.03461 15.55701 94.17448  1.000 15.27752  ? 21  GLN A CB  1 
ATOM   173  C  CG  . GLN A 1 22  ? 59.97716 14.48039 93.91335  1.000 14.51311  ? 21  GLN A CG  1 
ATOM   174  C  CD  . GLN A 1 22  ? 59.98770 13.35731 94.93586  1.000 16.58174  ? 21  GLN A CD  1 
ATOM   175  O  OE1 . GLN A 1 22  ? 60.50059 13.50554 96.04404  1.000 23.63917  ? 21  GLN A OE1 1 
ATOM   176  N  NE2 . GLN A 1 22  ? 59.40273 12.22270 94.56442  1.000 21.75982  ? 21  GLN A NE2 1 
ATOM   177  N  N   . ILE A 1 23  ? 59.46656 18.32252 94.15002  1.000 13.71112  ? 22  ILE A N   1 
ATOM   178  C  CA  . ILE A 1 23  ? 58.23871 19.11326 94.21753  1.000 14.29752  ? 22  ILE A CA  1 
ATOM   179  C  C   . ILE A 1 23  ? 58.09988 19.98533 92.98031  1.000 12.40159  ? 22  ILE A C   1 
ATOM   180  O  O   . ILE A 1 23  ? 57.04496 20.01120 92.33991  1.000 12.25886  ? 22  ILE A O   1 
ATOM   181  C  CB  . ILE A 1 23  ? 58.19767 19.95195 95.50822  1.000 12.50890  ? 22  ILE A CB  1 
ATOM   182  C  CG1 . ILE A 1 23  ? 58.00635 19.04883 96.72600  1.000 12.99247  ? 22  ILE A CG1 1 
ATOM   183  C  CG2 . ILE A 1 23  ? 57.13020 21.04274 95.41924  1.000 15.58642  ? 22  ILE A CG2 1 
ATOM   184  C  CD1 . ILE A 1 23  ? 58.08182 19.79316 98.04199  1.000 16.80146  ? 22  ILE A CD1 1 
ATOM   185  N  N   . MET A 1 24  ? 59.15920 20.72573 92.62938  1.000 13.16448  ? 23  MET A N   1 
ATOM   186  C  CA  . MET A 1 24  ? 59.04817 21.63838 91.49375  1.000 12.82041  ? 23  MET A CA  1 
ATOM   187  C  C   . MET A 1 24  ? 58.67117 20.89473 90.21998  1.000 14.89377  ? 23  MET A C   1 
ATOM   188  O  O   . MET A 1 24  ? 57.81948 21.36078 89.45137  1.000 12.75547  ? 23  MET A O   1 
ATOM   189  C  CB  . MET A 1 24  ? 60.33303 22.44848 91.29803  1.000 12.35983  ? 23  MET A CB  1 
ATOM   190  C  CG  . MET A 1 24  ? 60.68048 23.34737 92.46881  1.000 14.36436  ? 23  MET A CG  1 
ATOM   191  S  SD  . MET A 1 24  ? 59.40565 24.55387 92.91823  1.000 14.68700  ? 23  MET A SD  1 
ATOM   192  C  CE  . MET A 1 24  ? 59.17976 25.44805 91.38391  1.000 19.52305  ? 23  MET A CE  1 
ATOM   193  N  N   . GLN A 1 25  ? 59.27102 19.72253 89.99425  1.000 13.12115  ? 24  GLN A N   1 
ATOM   194  C  CA  . GLN A 1 25  ? 58.98695 18.96824 88.77690  1.000 12.12964  ? 24  GLN A CA  1 
ATOM   195  C  C   . GLN A 1 25  ? 57.55226 18.44683 88.76542  1.000 15.01549  ? 24  GLN A C   1 
ATOM   196  O  O   . GLN A 1 25  ? 56.84827 18.57039 87.75769  1.000 13.57381  ? 24  GLN A O   1 
ATOM   197  C  CB  . GLN A 1 25  ? 59.99610 17.82815 88.60308  1.000 16.14491  ? 24  GLN A CB  1 
ATOM   198  C  CG  . GLN A 1 25  ? 59.75540 16.98975 87.35473  1.000 20.82992  ? 24  GLN A CG  1 
ATOM   199  C  CD  . GLN A 1 25  ? 60.88842 16.02296 87.06616  1.000 30.28869  ? 24  GLN A CD  1 
ATOM   200  O  OE1 . GLN A 1 25  ? 62.02821 16.24697 87.47240  1.000 33.75130  ? 24  GLN A OE1 1 
ATOM   201  N  NE2 . GLN A 1 25  ? 60.58053 14.94584 86.34963  1.000 30.83088  ? 24  GLN A NE2 1 
ATOM   202  N  N   . LEU A 1 26  ? 57.10423 17.84909 89.87105  1.000 13.29294  ? 25  LEU A N   1 
ATOM   203  C  CA  . LEU A 1 26  ? 55.72143 17.37481 89.93947  1.000 14.14122  ? 25  LEU A CA  1 
ATOM   204  C  C   . LEU A 1 26  ? 54.74631 18.53608 89.83149  1.000 15.86390  ? 25  LEU A C   1 
ATOM   205  O  O   . LEU A 1 26  ? 53.76010 18.47302 89.08808  1.000 14.03226  ? 25  LEU A O   1 
ATOM   206  C  CB  . LEU A 1 26  ? 55.48401 16.63410 91.25372  1.000 13.80433  ? 25  LEU A CB  1 
ATOM   207  C  CG  . LEU A 1 26  ? 56.02279 15.20866 91.37344  1.000 11.54260  ? 25  LEU A CG  1 
ATOM   208  C  CD1 . LEU A 1 26  ? 55.99134 14.77672 92.82467  1.000 14.84053  ? 25  LEU A CD1 1 
ATOM   209  C  CD2 . LEU A 1 26  ? 55.19879 14.24751 90.52782  1.000 18.39720  ? 25  LEU A CD2 1 
ATOM   210  N  N   . HIS A 1 27  ? 55.01160 19.61164 90.57264  1.000 13.76837  ? 26  HIS A N   1 
ATOM   211  C  CA  . HIS A 1 27  ? 54.08404 20.73455 90.61460  1.000 11.87176  ? 26  HIS A CA  1 
ATOM   212  C  C   . HIS A 1 27  ? 53.89574 21.33897 89.23318  1.000 12.51110  ? 26  HIS A C   1 
ATOM   213  O  O   . HIS A 1 27  ? 52.76908 21.65156 88.83074  1.000 13.82936  ? 26  HIS A O   1 
ATOM   214  C  CB  . HIS A 1 27  ? 54.61735 21.78466 91.58597  1.000 13.56209  ? 26  HIS A CB  1 
ATOM   215  C  CG  . HIS A 1 27  ? 53.55932 22.65070 92.18593  1.000 11.49783  ? 26  HIS A CG  1 
ATOM   216  N  ND1 . HIS A 1 27  ? 53.84662 23.64058 93.09926  1.000 14.00410  ? 26  HIS A ND1 1 
ATOM   217  C  CD2 . HIS A 1 27  ? 52.21693 22.66567 92.01951  1.000 11.63408  ? 26  HIS A CD2 1 
ATOM   218  C  CE1 . HIS A 1 27  ? 52.72651 24.23972 93.46043  1.000 13.57914  ? 26  HIS A CE1 1 
ATOM   219  N  NE2 . HIS A 1 27  ? 51.72213 23.66262 92.82320  1.000 12.01533  ? 26  HIS A NE2 1 
ATOM   220  N  N   . HIS A 1 28  ? 54.98625 21.48454 88.48021  1.000 13.44194  ? 27  HIS A N   1 
ATOM   221  C  CA  . HIS A 1 28  ? 54.89788 22.10338 87.16560  1.000 12.93074  ? 27  HIS A CA  1 
ATOM   222  C  C   . HIS A 1 28  ? 54.46106 21.10122 86.09950  1.000 14.92968  ? 27  HIS A C   1 
ATOM   223  O  O   . HIS A 1 28  ? 53.47439 21.32667 85.38854  1.000 14.54771  ? 27  HIS A O   1 
ATOM   224  C  CB  . HIS A 1 28  ? 56.24554 22.72264 86.79500  1.000 14.46872  ? 27  HIS A CB  1 
ATOM   225  C  CG  . HIS A 1 28  ? 56.27792 23.27191 85.40763  1.000 13.55857  ? 27  HIS A CG  1 
ATOM   226  N  ND1 . HIS A 1 28  ? 56.85076 22.59162 84.35438  1.000 16.56431  ? 27  HIS A ND1 1 
ATOM   227  C  CD2 . HIS A 1 28  ? 55.80283 24.43027 84.89664  1.000 15.71926  ? 27  HIS A CD2 1 
ATOM   228  C  CE1 . HIS A 1 28  ? 56.72056 23.30831 83.25191  1.000 18.37153  ? 27  HIS A CE1 1 
ATOM   229  N  NE2 . HIS A 1 28  ? 56.09265 24.42894 83.55463  1.000 17.57413  ? 27  HIS A NE2 1 
ATOM   230  N  N   . SER A 1 29  ? 55.17959 19.98305 85.97768  1.000 14.70447  ? 28  SER A N   1 
ATOM   231  C  CA  . SER A 1 29  ? 54.98003 19.07799 84.84823  1.000 13.22117  ? 28  SER A CA  1 
ATOM   232  C  C   . SER A 1 29  ? 53.77732 18.15843 85.01353  1.000 15.37786  ? 28  SER A C   1 
ATOM   233  O  O   . SER A 1 29  ? 53.32021 17.58165 84.02142  1.000 17.37200  ? 28  SER A O   1 
ATOM   234  C  CB  . SER A 1 29  ? 56.23247 18.23396 84.59051  1.000 16.46872  ? 28  SER A CB  1 
ATOM   235  O  OG  . SER A 1 29  ? 56.35955 17.19214 85.54162  1.000 20.75406  ? 28  SER A OG  1 
ATOM   236  N  N   . LYS A 1 30  ? 53.27116 17.97743 86.23195  1.000 13.35011  ? 29  LYS A N   1 
ATOM   237  C  CA  . LYS A 1 30  ? 52.08344 17.16066 86.45224  1.000 14.12698  ? 29  LYS A CA  1 
ATOM   238  C  C   . LYS A 1 30  ? 50.87621 18.00709 86.83506  1.000 13.27289  ? 29  LYS A C   1 
ATOM   239  O  O   . LYS A 1 30  ? 49.85797 17.98802 86.13497  1.000 14.14360  ? 29  LYS A O   1 
ATOM   240  C  CB  . LYS A 1 30  ? 52.32802 16.06658 87.50572  1.000 14.47879  ? 29  LYS A CB  1 
ATOM   241  C  CG  . LYS A 1 30  ? 53.43391 15.08835 87.16684  1.000 17.75800  ? 29  LYS A CG  1 
ATOM   242  C  CD  . LYS A 1 30  ? 53.14151 14.33066 85.89062  1.000 22.32477  ? 29  LYS A CD  1 
ATOM   243  C  CE  . LYS A 1 30  ? 54.19697 13.25624 85.64287  1.000 27.59969  ? 29  LYS A CE  1 
ATOM   244  N  NZ  . LYS A 1 30  ? 55.54889 13.84647 85.45940  1.000 40.24291  ? 29  LYS A NZ  1 
ATOM   245  N  N   . HIS A 1 31  ? 50.96388 18.77132 87.92560  1.000 14.83511  ? 30  HIS A N   1 
ATOM   246  C  CA  . HIS A 1 31  ? 49.78872 19.48891 88.41393  1.000 13.25504  ? 30  HIS A CA  1 
ATOM   247  C  C   . HIS A 1 31  ? 49.37662 20.60944 87.46452  1.000 14.10634  ? 30  HIS A C   1 
ATOM   248  O  O   . HIS A 1 31  ? 48.22407 20.66753 87.02319  1.000 13.61869  ? 30  HIS A O   1 
ATOM   249  C  CB  . HIS A 1 31  ? 50.03105 20.01231 89.82903  1.000 11.54720  ? 30  HIS A CB  1 
ATOM   250  C  CG  . HIS A 1 31  ? 50.13379 18.93985 90.87172  1.000 13.25784  ? 30  HIS A CG  1 
ATOM   251  N  ND1 . HIS A 1 31  ? 49.04537 18.49506 91.59313  1.000 15.51113  ? 30  HIS A ND1 1 
ATOM   252  C  CD2 . HIS A 1 31  ? 51.19683 18.22388 91.31349  1.000 12.80857  ? 30  HIS A CD2 1 
ATOM   253  C  CE1 . HIS A 1 31  ? 49.43733 17.56092 92.44178  1.000 14.56609  ? 30  HIS A CE1 1 
ATOM   254  N  NE2 . HIS A 1 31  ? 50.73781 17.37750 92.29260  1.000 15.07571  ? 30  HIS A NE2 1 
ATOM   255  N  N   . HIS A 1 32  ? 50.30027 21.51199 87.13377  1.000 13.10523  ? 31  HIS A N   1 
ATOM   256  C  CA  . HIS A 1 32  ? 49.93360 22.60133 86.23856  1.000 11.51662  ? 31  HIS A CA  1 
ATOM   257  C  C   . HIS A 1 32  ? 49.57556 22.07823 84.85281  1.000 13.12186  ? 31  HIS A C   1 
ATOM   258  O  O   . HIS A 1 32  ? 48.58218 22.51012 84.25780  1.000 13.23443  ? 31  HIS A O   1 
ATOM   259  C  CB  . HIS A 1 32  ? 51.05946 23.63054 86.16205  1.000 13.15754  ? 31  HIS A CB  1 
ATOM   260  C  CG  . HIS A 1 32  ? 50.64706 24.91354 85.51145  1.000 12.30591  ? 31  HIS A CG  1 
ATOM   261  N  ND1 . HIS A 1 32  ? 51.48817 26.00030 85.40701  1.000 13.34227  ? 31  HIS A ND1 1 
ATOM   262  C  CD2 . HIS A 1 32  ? 49.47518 25.29030 84.94385  1.000 12.71016  ? 31  HIS A CD2 1 
ATOM   263  C  CE1 . HIS A 1 32  ? 50.85666 26.98784 84.79761  1.000 14.36983  ? 31  HIS A CE1 1 
ATOM   264  N  NE2 . HIS A 1 32  ? 49.63355 26.58037 84.50193  1.000 12.50845  ? 31  HIS A NE2 1 
ATOM   265  N  N   . ALA A 1 33  ? 50.33856 21.11389 84.34165  1.000 13.16544  ? 32  ALA A N   1 
ATOM   266  C  CA  . ALA A 1 33  ? 50.03915 20.56137 83.02546  1.000 13.45438  ? 32  ALA A CA  1 
ATOM   267  C  C   . ALA A 1 33  ? 48.61060 20.03888 82.94752  1.000 14.06127  ? 32  ALA A C   1 
ATOM   268  O  O   . ALA A 1 33  ? 47.91054 20.28755 81.96131  1.000 14.58204  ? 32  ALA A O   1 
ATOM   269  C  CB  . ALA A 1 33  ? 51.03936 19.45939 82.67690  1.000 15.60172  ? 32  ALA A CB  1 
ATOM   270  N  N   . ALA A 1 34  ? 48.15083 19.33318 83.98393  1.000 13.30059  ? 33  ALA A N   1 
ATOM   271  C  CA  . ALA A 1 34  ? 46.78134 18.82269 83.97175  1.000 13.44883  ? 33  ALA A CA  1 
ATOM   272  C  C   . ALA A 1 34  ? 45.76281 19.95784 83.95502  1.000 14.30783  ? 33  ALA A C   1 
ATOM   273  O  O   . ALA A 1 34  ? 44.77370 19.89860 83.21907  1.000 14.32992  ? 33  ALA A O   1 
ATOM   274  C  CB  . ALA A 1 34  ? 46.54467 17.92865 85.18518  1.000 14.46275  ? 33  ALA A CB  1 
ATOM   275  N  N   . PHE A 1 35  ? 45.99968 21.01273 84.73669  1.000 13.29116  ? 34  PHE A N   1 
ATOM   276  C  CA  . PHE A 1 35  ? 45.08287 22.15083 84.72783  1.000 12.69690  ? 34  PHE A CA  1 
ATOM   277  C  C   . PHE A 1 35  ? 44.96011 22.76769 83.34050  1.000 14.71048  ? 34  PHE A C   1 
ATOM   278  O  O   . PHE A 1 35  ? 43.85392 23.09382 82.90089  1.000 13.94996  ? 34  PHE A O   1 
ATOM   279  C  CB  . PHE A 1 35  ? 45.52450 23.20828 85.74455  1.000 14.07256  ? 34  PHE A CB  1 
ATOM   280  C  CG  . PHE A 1 35  ? 45.23651 22.84447 87.17364  1.000 13.59567  ? 34  PHE A CG  1 
ATOM   281  C  CD1 . PHE A 1 35  ? 43.99689 22.33740 87.53597  1.000 17.83883  ? 34  PHE A CD1 1 
ATOM   282  C  CD2 . PHE A 1 35  ? 46.20830 22.99337 88.15226  1.000 15.25463  ? 34  PHE A CD2 1 
ATOM   283  C  CE1 . PHE A 1 35  ? 43.72058 22.00287 88.85025  1.000 18.98972  ? 34  PHE A CE1 1 
ATOM   284  C  CE2 . PHE A 1 35  ? 45.93715 22.65796 89.46896  1.000 13.06919  ? 34  PHE A CE2 1 
ATOM   285  C  CZ  . PHE A 1 35  ? 44.68651 22.16188 89.81508  1.000 15.96437  ? 34  PHE A CZ  1 
ATOM   286  N  N   . VAL A 1 36  ? 46.08119 22.95200 82.64115  1.000 13.87957  ? 35  VAL A N   1 
ATOM   287  C  CA  . VAL A 1 36  ? 46.03922 23.57706 81.31954  1.000 14.77306  ? 35  VAL A CA  1 
ATOM   288  C  C   . VAL A 1 36  ? 45.23868 22.72417 80.34638  1.000 14.62076  ? 35  VAL A C   1 
ATOM   289  O  O   . VAL A 1 36  ? 44.32696 23.21539 79.66610  1.000 13.17783  ? 35  VAL A O   1 
ATOM   290  C  CB  . VAL A 1 36  ? 47.46369 23.82738 80.79388  1.000 18.29786  ? 35  VAL A CB  1 
ATOM   291  C  CG1 . VAL A 1 36  ? 47.40456 24.40192 79.38438  1.000 25.76416  ? 35  VAL A CG1 1 
ATOM   292  C  CG2 . VAL A 1 36  ? 48.24092 24.74185 81.72816  1.000 22.99684  ? 35  VAL A CG2 1 
ATOM   293  N  N   . ASN A 1 37  ? 45.57841 21.43362 80.25155  1.000 14.17827  ? 36  ASN A N   1 
ATOM   294  C  CA  . ASN A 1 37  ? 44.85839 20.55976 79.33199  1.000 13.07909  ? 36  ASN A CA  1 
ATOM   295  C  C   . ASN A 1 37  ? 43.39057 20.46231 79.70224  1.000 13.37058  ? 36  ASN A C   1 
ATOM   296  O  O   . ASN A 1 37  ? 42.51599 20.55149 78.83188  1.000 14.68822  ? 36  ASN A O   1 
ATOM   297  C  CB  . ASN A 1 37  ? 45.48611 19.16861 79.27064  1.000 15.09211  ? 36  ASN A CB  1 
ATOM   298  C  CG  . ASN A 1 37  ? 46.81320 19.16304 78.56049  1.000 18.31862  ? 36  ASN A CG  1 
ATOM   299  O  OD1 . ASN A 1 37  ? 47.17043 20.12784 77.88071  1.000 17.14549  ? 36  ASN A OD1 1 
ATOM   300  N  ND2 . ASN A 1 37  ? 47.52418 18.04467 78.64825  1.000 17.09017  ? 36  ASN A ND2 1 
ATOM   301  N  N   . ASN A 1 38  ? 43.09806 20.29240 80.99208  1.000 13.66207  ? 37  ASN A N   1 
ATOM   302  C  CA  . ASN A 1 38  ? 41.70501 20.15134 81.39080  1.000 12.88317  ? 37  ASN A CA  1 
ATOM   303  C  C   . ASN A 1 38  ? 40.95504 21.46122 81.21040  1.000 13.80449  ? 37  ASN A C   1 
ATOM   304  O  O   . ASN A 1 38  ? 39.76242 21.45121 80.88060  1.000 13.01932  ? 37  ASN A O   1 
ATOM   305  C  CB  . ASN A 1 38  ? 41.59957 19.63985 82.83124  1.000 16.11781  ? 37  ASN A CB  1 
ATOM   306  C  CG  . ASN A 1 38  ? 42.19907 18.25095 83.00714  1.000 14.92004  ? 37  ASN A CG  1 
ATOM   307  O  OD1 . ASN A 1 38  ? 42.36841 17.50495 82.04396  1.000 18.73487  ? 37  ASN A OD1 1 
ATOM   308  N  ND2 . ASN A 1 38  ? 42.50594 17.89350 84.24615  1.000 16.55332  ? 37  ASN A ND2 1 
ATOM   309  N  N   . LEU A 1 39  ? 41.63941 22.59537 81.37840  1.000 14.59954  ? 38  LEU A N   1 
ATOM   310  C  CA  . LEU A 1 39  ? 41.01859 23.88030 81.08239  1.000 13.10948  ? 38  LEU A CA  1 
ATOM   311  C  C   . LEU A 1 39  ? 40.60922 23.96918 79.61865  1.000 14.38529  ? 38  LEU A C   1 
ATOM   312  O  O   . LEU A 1 39  ? 39.48992 24.38131 79.30521  1.000 13.53182  ? 38  LEU A O   1 
ATOM   313  C  CB  . LEU A 1 39  ? 41.98207 25.01283 81.42581  1.000 11.97391  ? 38  LEU A CB  1 
ATOM   314  C  CG  . LEU A 1 39  ? 41.61263 26.39508 80.89867  1.000 12.26312  ? 38  LEU A CG  1 
ATOM   315  C  CD1 . LEU A 1 39  ? 40.26418 26.84456 81.45271  1.000 14.00732  ? 38  LEU A CD1 1 
ATOM   316  C  CD2 . LEU A 1 39  ? 42.71254 27.38345 81.26695  1.000 13.38393  ? 38  LEU A CD2 1 
ATOM   317  N  N   . ASN A 1 40  ? 41.49695 23.56925 78.70520  1.000 13.63967  ? 39  ASN A N   1 
ATOM   318  C  CA  . ASN A 1 40  ? 41.15622 23.62832 77.28723  1.000 14.45100  ? 39  ASN A CA  1 
ATOM   319  C  C   . ASN A 1 40  ? 39.95797 22.73530 76.97029  1.000 12.76999  ? 39  ASN A C   1 
ATOM   320  O  O   . ASN A 1 40  ? 39.07349 23.12608 76.20018  1.000 14.74077  ? 39  ASN A O   1 
ATOM   321  C  CB  . ASN A 1 40  ? 42.37504 23.28142 76.43405  1.000 15.88953  ? 39  ASN A CB  1 
ATOM   322  C  CG  . ASN A 1 40  ? 43.35984 24.43299 76.34271  1.000 14.77949  ? 39  ASN A CG  1 
ATOM   323  O  OD1 . ASN A 1 40  ? 42.96122 25.59647 76.27281  1.000 16.72801  ? 39  ASN A OD1 1 
ATOM   324  N  ND2 . ASN A 1 40  ? 44.65376 24.11598 76.37970  1.000 18.59203  ? 39  ASN A ND2 1 
ATOM   325  N  N   . VAL A 1 41  ? 39.88600 21.55677 77.59243  1.000 13.58204  ? 40  VAL A N   1 
ATOM   326  C  CA  . VAL A 1 41  ? 38.73901 20.67267 77.39151  1.000 13.69457  ? 40  VAL A CA  1 
ATOM   327  C  C   . VAL A 1 41  ? 37.46219 21.32759 77.89828  1.000 16.21433  ? 40  VAL A C   1 
ATOM   328  O  O   . VAL A 1 41  ? 36.41965 21.28799 77.23213  1.000 14.80301  ? 40  VAL A O   1 
ATOM   329  C  CB  . VAL A 1 41  ? 38.98402 19.31443 78.06976  1.000 14.94330  ? 40  VAL A CB  1 
ATOM   330  C  CG1 . VAL A 1 41  ? 37.73729 18.44114 78.00373  1.000 17.65088  ? 40  VAL A CG1 1 
ATOM   331  C  CG2 . VAL A 1 41  ? 40.16374 18.61774 77.42465  1.000 13.49157  ? 40  VAL A CG2 1 
ATOM   332  N  N   . THR A 1 42  ? 37.52040 21.93678 79.08636  1.000 14.99590  ? 41  THR A N   1 
ATOM   333  C  CA  . THR A 1 42  ? 36.32315 22.55007 79.65748  1.000 15.48045  ? 41  THR A CA  1 
ATOM   334  C  C   . THR A 1 42  ? 35.86075 23.73681 78.82367  1.000 17.66916  ? 41  THR A C   1 
ATOM   335  O  O   . THR A 1 42  ? 34.65502 23.90463 78.59090  1.000 14.33806  ? 41  THR A O   1 
ATOM   336  C  CB  . THR A 1 42  ? 36.59307 22.99054 81.09464  1.000 15.33861  ? 41  THR A CB  1 
ATOM   337  O  OG1 . THR A 1 42  ? 37.03720 21.87661 81.87090  1.000 18.97629  ? 41  THR A OG1 1 
ATOM   338  C  CG2 . THR A 1 42  ? 35.33369 23.56063 81.72076  1.000 16.85891  ? 41  THR A CG2 1 
ATOM   339  N  N   . GLU A 1 43  ? 36.80566 24.56717 78.36536  1.000 14.67965  ? 42  GLU A N   1 
ATOM   340  C  CA  . GLU A 1 43  ? 36.45621 25.71238 77.52972  1.000 14.95465  ? 42  GLU A CA  1 
ATOM   341  C  C   . GLU A 1 43  ? 35.76793 25.27923 76.24732  1.000 16.14773  ? 42  GLU A C   1 
ATOM   342  O  O   . GLU A 1 43  ? 34.81486 25.92690 75.80389  1.000 16.31271  ? 42  GLU A O   1 
ATOM   343  C  CB  . GLU A 1 43  ? 37.69451 26.53334 77.17285  1.000 15.94368  ? 42  GLU A CB  1 
ATOM   344  C  CG  . GLU A 1 43  ? 38.01833 27.65694 78.11701  1.000 24.45430  ? 42  GLU A CG  1 
ATOM   345  C  CD  . GLU A 1 43  ? 38.99686 28.63965 77.50386  1.000 19.09348  ? 42  GLU A CD  1 
ATOM   346  O  OE1 . GLU A 1 43  ? 39.48981 28.38340 76.38177  1.000 25.09999  ? 42  GLU A OE1 1 
ATOM   347  O  OE2 . GLU A 1 43  ? 39.27754 29.66661 78.14449  1.000 18.80190  ? 42  GLU A OE2 1 
ATOM   348  N  N   . GLU A 1 44  ? 36.25205 24.20233 75.62073  1.000 18.09558  ? 43  GLU A N   1 
ATOM   349  C  CA  . GLU A 1 44  ? 35.62706 23.74356 74.38644  1.000 19.18621  ? 43  GLU A CA  1 
ATOM   350  C  C   . GLU A 1 44  ? 34.19951 23.29156 74.64684  1.000 15.88193  ? 43  GLU A C   1 
ATOM   351  O  O   . GLU A 1 44  ? 33.28487 23.62861 73.88587  1.000 16.56114  ? 43  GLU A O   1 
ATOM   352  C  CB  . GLU A 1 44  ? 36.45634 22.62032 73.76348  1.000 19.30802  ? 43  GLU A CB  1 
ATOM   353  C  CG  . GLU A 1 44  ? 36.11058 22.31358 72.31098  1.000 23.52138  ? 43  GLU A CG  1 
ATOM   354  C  CD  . GLU A 1 44  ? 34.91881 21.38651 72.15879  1.000 41.42844  ? 43  GLU A CD  1 
ATOM   355  O  OE1 . GLU A 1 44  ? 34.60634 20.63911 73.11410  1.000 34.63900  ? 43  GLU A OE1 1 
ATOM   356  O  OE2 . GLU A 1 44  ? 34.29579 21.40389 71.07494  1.000 42.48702  ? 43  GLU A OE2 1 
ATOM   357  N  N   . LYS A 1 45  ? 33.98508 22.56739 75.74604  1.000 15.77878  ? 44  LYS A N   1 
ATOM   358  C  CA  . LYS A 1 45  ? 32.63197 22.19388 76.13816  1.000 15.33662  ? 44  LYS A CA  1 
ATOM   359  C  C   . LYS A 1 45  ? 31.77699 23.42691 76.38377  1.000 16.27611  ? 44  LYS A C   1 
ATOM   360  O  O   . LYS A 1 45  ? 30.60737 23.46943 75.98747  1.000 17.43036  ? 44  LYS A O   1 
ATOM   361  C  CB  . LYS A 1 45  ? 32.67548 21.34357 77.40396  1.000 17.99682  ? 44  LYS A CB  1 
ATOM   362  C  CG  . LYS A 1 45  ? 33.18203 19.93220 77.20665  1.000 20.86840  ? 44  LYS A CG  1 
ATOM   363  C  CD  . LYS A 1 45  ? 33.14864 19.17377 78.52649  1.000 25.49699  ? 44  LYS A CD  1 
ATOM   364  C  CE  . LYS A 1 45  ? 33.70543 17.77335 78.38627  1.000 37.16952  ? 44  LYS A CE  1 
ATOM   365  N  NZ  . LYS A 1 45  ? 33.71142 17.07184 79.69720  1.000 45.49308  ? 44  LYS A NZ  1 
ATOM   366  N  N   . TYR A 1 46  ? 32.34032 24.44089 77.03981  1.000 17.70758  ? 45  TYR A N   1 
ATOM   367  C  CA  . TYR A 1 46  ? 31.55612 25.63641 77.32292  1.000 19.04279  ? 45  TYR A CA  1 
ATOM   368  C  C   . TYR A 1 46  ? 31.17260 26.36115 76.03925  1.000 18.39098  ? 45  TYR A C   1 
ATOM   369  O  O   . TYR A 1 46  ? 30.03167 26.81895 75.90190  1.000 20.24221  ? 45  TYR A O   1 
ATOM   370  C  CB  . TYR A 1 46  ? 32.29038 26.56384 78.29861  1.000 19.94660  ? 45  TYR A CB  1 
ATOM   371  C  CG  . TYR A 1 46  ? 31.33544 27.48951 79.01172  1.000 15.29188  ? 45  TYR A CG  1 
ATOM   372  C  CD1 . TYR A 1 46  ? 30.82429 28.60421 78.36692  1.000 22.37671  ? 45  TYR A CD1 1 
ATOM   373  C  CD2 . TYR A 1 46  ? 30.92009 27.23549 80.31606  1.000 17.73273  ? 45  TYR A CD2 1 
ATOM   374  C  CE1 . TYR A 1 46  ? 29.93037 29.45127 78.99401  1.000 17.15800  ? 45  TYR A CE1 1 
ATOM   375  C  CE2 . TYR A 1 46  ? 30.01928 28.07849 80.95487  1.000 16.63431  ? 45  TYR A CE2 1 
ATOM   376  C  CZ  . TYR A 1 46  ? 29.53499 29.18766 80.28661  1.000 18.44684  ? 45  TYR A CZ  1 
ATOM   377  O  OH  . TYR A 1 46  ? 28.64435 30.04551 80.89412  1.000 16.92458  ? 45  TYR A OH  1 
ATOM   378  N  N   . GLN A 1 47  ? 32.10284 26.47046 75.08531  1.000 18.49624  ? 46  GLN A N   1 
ATOM   379  C  CA  . GLN A 1 47  ? 31.78224 27.11697 73.81522  1.000 18.72256  ? 46  GLN A CA  1 
ATOM   380  C  C   . GLN A 1 47  ? 30.60634 26.43198 73.12718  1.000 20.08930  ? 46  GLN A C   1 
ATOM   381  O  O   . GLN A 1 47  ? 29.70063 27.10339 72.61840  1.000 22.20275  ? 46  GLN A O   1 
ATOM   382  C  CB  . GLN A 1 47  ? 33.00790 27.13709 72.89802  1.000 24.99268  ? 46  GLN A CB  1 
ATOM   383  C  CG  . GLN A 1 47  ? 32.79468 27.88417 71.57574  1.000 24.68540  ? 46  GLN A CG  1 
ATOM   384  C  CD  . GLN A 1 47  ? 32.34379 29.32737 71.76205  1.000 45.17425  ? 46  GLN A CD  1 
ATOM   385  O  OE1 . GLN A 1 47  ? 33.14636 30.20098 72.09288  1.000 31.09375  ? 46  GLN A OE1 1 
ATOM   386  N  NE2 . GLN A 1 47  ? 31.05414 29.58196 71.54961  1.000 32.53490  ? 46  GLN A NE2 1 
ATOM   387  N  N   . GLU A 1 48  ? 30.58646 25.09570 73.12848  1.000 16.95283  ? 47  GLU A N   1 
ATOM   388  C  CA  . GLU A 1 48  ? 29.47475 24.37616 72.51470  1.000 19.27416  ? 47  GLU A CA  1 
ATOM   389  C  C   . GLU A 1 48  ? 28.16483 24.65941 73.23977  1.000 20.02412  ? 47  GLU A C   1 
ATOM   390  O  O   . GLU A 1 48  ? 27.12963 24.88692 72.60210  1.000 20.25321  ? 47  GLU A O   1 
ATOM   391  C  CB  . GLU A 1 48  ? 29.75634 22.87442 72.50361  1.000 19.77318  ? 47  GLU A CB  1 
ATOM   392  C  CG  . GLU A 1 48  ? 30.90010 22.45511 71.59674  1.000 36.62574  ? 47  GLU A CG  1 
ATOM   393  C  CD  . GLU A 1 48  ? 30.97056 20.95158 71.40845  1.000 52.62025  ? 47  GLU A CD  1 
ATOM   394  O  OE1 . GLU A 1 48  ? 30.26766 20.22292 72.14513  1.000 48.51610  ? 47  GLU A OE1 1 
ATOM   395  O  OE2 . GLU A 1 48  ? 31.72565 20.50055 70.51948  1.000 36.72668  ? 47  GLU A OE2 1 
ATOM   396  N  N   . ALA A 1 49  ? 28.18808 24.64236 74.57360  1.000 16.66058  ? 48  ALA A N   1 
ATOM   397  C  CA  . ALA A 1 49  ? 26.97015 24.88557 75.33923  1.000 18.36729  ? 48  ALA A CA  1 
ATOM   398  C  C   . ALA A 1 49  ? 26.46867 26.30565 75.13033  1.000 18.81280  ? 48  ALA A C   1 
ATOM   399  O  O   . ALA A 1 49  ? 25.25787 26.53895 75.01681  1.000 18.42479  ? 48  ALA A O   1 
ATOM   400  C  CB  . ALA A 1 49  ? 27.22814 24.61095 76.81989  1.000 17.28096  ? 48  ALA A CB  1 
ATOM   401  N  N   . LEU A 1 50  ? 27.39094 27.26478 75.06525  1.000 17.59630  ? 49  LEU A N   1 
ATOM   402  C  CA  . LEU A 1 50  ? 27.01546 28.65104 74.83225  1.000 18.94132  ? 49  LEU A CA  1 
ATOM   403  C  C   . LEU A 1 50  ? 26.35511 28.81468 73.46757  1.000 22.40648  ? 49  LEU A C   1 
ATOM   404  O  O   . LEU A 1 50  ? 25.30282 29.45334 73.34648  1.000 22.64879  ? 49  LEU A O   1 
ATOM   405  C  CB  . LEU A 1 50  ? 28.26225 29.52840 74.95191  1.000 18.33764  ? 49  LEU A CB  1 
ATOM   406  C  CG  . LEU A 1 50  ? 28.05235 31.03863 74.87699  1.000 22.82255  ? 49  LEU A CG  1 
ATOM   407  C  CD1 . LEU A 1 50  ? 27.12357 31.50008 75.98565  1.000 21.75825  ? 49  LEU A CD1 1 
ATOM   408  C  CD2 . LEU A 1 50  ? 29.39047 31.75454 74.95711  1.000 28.01333  ? 49  LEU A CD2 1 
ATOM   409  N  N   . ALA A 1 51  ? 26.94435 28.21102 72.42932  1.000 20.99610  ? 50  ALA A N   1 
ATOM   410  C  CA  . ALA A 1 51  ? 26.38194 28.32600 71.08691  1.000 24.56740  ? 50  ALA A CA  1 
ATOM   411  C  C   . ALA A 1 51  ? 24.99205 27.70884 71.00547  1.000 29.33090  ? 50  ALA A C   1 
ATOM   412  O  O   . ALA A 1 51  ? 24.13002 28.20978 70.27180  1.000 28.64000  ? 50  ALA A O   1 
ATOM   413  C  CB  . ALA A 1 51  ? 27.31838 27.67526 70.06873  1.000 26.58261  ? 50  ALA A CB  1 
ATOM   414  N  N   . LYS A 1 52  ? 24.75279 26.63363 71.75347  1.000 22.47116  ? 51  LYS A N   1 
ATOM   415  C  CA  . LYS A 1 52  ? 23.45147 25.98073 71.79645  1.000 23.96918  ? 51  LYS A CA  1 
ATOM   416  C  C   . LYS A 1 52  ? 22.48423 26.65621 72.75408  1.000 27.41329  ? 51  LYS A C   1 
ATOM   417  O  O   . LYS A 1 52  ? 21.31740 26.25341 72.81245  1.000 27.24857  ? 51  LYS A O   1 
ATOM   418  C  CB  . LYS A 1 52  ? 23.61407 24.52529 72.23790  1.000 21.45796  ? 51  LYS A CB  1 
ATOM   419  C  CG  . LYS A 1 52  ? 24.22682 23.60680 71.20533  1.000 37.67088  ? 51  LYS A CG  1 
ATOM   420  C  CD  . LYS A 1 52  ? 24.28448 22.17989 71.72959  1.000 41.93629  ? 51  LYS A CD  1 
ATOM   421  C  CE  . LYS A 1 52  ? 22.93026 21.73359 72.26245  1.000 50.53037  ? 51  LYS A CE  1 
ATOM   422  N  NZ  . LYS A 1 52  ? 22.98133 20.36036 72.83852  1.000 61.44333  ? 51  LYS A NZ  1 
ATOM   423  N  N   . GLY A 1 53  ? 22.93038 27.66400 73.49879  1.000 19.62797  ? 52  GLY A N   1 
ATOM   424  C  CA  . GLY A 1 53  ? 22.09461 28.23800 74.53856  1.000 23.72938  ? 52  GLY A CA  1 
ATOM   425  C  C   . GLY A 1 53  ? 21.72380 27.26006 75.63033  1.000 19.57108  ? 52  GLY A C   1 
ATOM   426  O  O   . GLY A 1 53  ? 20.66016 27.40328 76.24427  1.000 19.64513  ? 52  GLY A O   1 
ATOM   427  N  N   . ASP A 1 54  ? 22.57374 26.26097 75.89143  1.000 18.15907  ? 53  ASP A N   1 
ATOM   428  C  CA  . ASP A 1 54  ? 22.30085 25.25726 76.92029  1.000 15.56892  ? 53  ASP A CA  1 
ATOM   429  C  C   . ASP A 1 54  ? 22.80881 25.81170 78.24451  1.000 16.15500  ? 53  ASP A C   1 
ATOM   430  O  O   . ASP A 1 54  ? 23.99127 25.68111 78.57996  1.000 16.35647  ? 53  ASP A O   1 
ATOM   431  C  CB  . ASP A 1 54  ? 22.95894 23.92434 76.58222  1.000 19.36654  ? 53  ASP A CB  1 
ATOM   432  C  CG  . ASP A 1 54  ? 22.45137 22.78522 77.45191  1.000 20.38085  ? 53  ASP A CG  1 
ATOM   433  O  OD1 . ASP A 1 54  ? 21.94486 23.04425 78.56544  1.000 18.60180  ? 53  ASP A OD1 1 
ATOM   434  O  OD2 . ASP A 1 54  ? 22.57733 21.61911 77.02982  1.000 25.87978  ? 53  ASP A OD2 1 
ATOM   435  N  N   . VAL A 1 55  ? 21.89918 26.41408 79.00957  1.000 15.47125  ? 54  VAL A N   1 
ATOM   436  C  CA  . VAL A 1 55  ? 22.27918 27.05676 80.26093  1.000 15.58221  ? 54  VAL A CA  1 
ATOM   437  C  C   . VAL A 1 55  ? 22.57694 26.01848 81.33215  1.000 15.47826  ? 54  VAL A C   1 
ATOM   438  O  O   . VAL A 1 55  ? 23.48378 26.20428 82.15346  1.000 14.34768  ? 54  VAL A O   1 
ATOM   439  C  CB  . VAL A 1 55  ? 21.18878 28.05257 80.69960  1.000 15.91377  ? 54  VAL A CB  1 
ATOM   440  C  CG1 . VAL A 1 55  ? 21.61498 28.79398 81.94876  1.000 14.99673  ? 54  VAL A CG1 1 
ATOM   441  C  CG2 . VAL A 1 55  ? 20.88373 29.03440 79.57799  1.000 20.00740  ? 54  VAL A CG2 1 
ATOM   442  N  N   . THR A 1 56  ? 21.82532 24.91340 81.34874  1.000 14.67276  ? 55  THR A N   1 
ATOM   443  C  CA  . THR A 1 56  ? 22.12362 23.84056 82.29156  1.000 13.98811  ? 55  THR A CA  1 
ATOM   444  C  C   . THR A 1 56  ? 23.53988 23.32713 82.08057  1.000 16.90040  ? 55  THR A C   1 
ATOM   445  O  O   . THR A 1 56  ? 24.30350 23.15873 83.03859  1.000 15.72874  ? 55  THR A O   1 
ATOM   446  C  CB  . THR A 1 56  ? 21.11150 22.70130 82.14978  1.000 13.93657  ? 55  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 56  ? 19.84279 23.11364 82.67510  1.000 15.32791  ? 55  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 56  ? 21.57847 21.46485 82.90675  1.000 14.66138  ? 55  THR A CG2 1 
ATOM   449  N  N   . ALA A 1 57  ? 23.91681 23.09881 80.82040  1.000 15.73711  ? 56  ALA A N   1 
ATOM   450  C  CA  . ALA A 1 57  ? 25.26325 22.61842 80.53077  1.000 14.83034  ? 56  ALA A CA  1 
ATOM   451  C  C   . ALA A 1 57  ? 26.31399 23.64790 80.92770  1.000 16.99935  ? 56  ALA A C   1 
ATOM   452  O  O   . ALA A 1 57  ? 27.35119 23.28664 81.49244  1.000 17.46522  ? 56  ALA A O   1 
ATOM   453  C  CB  . ALA A 1 57  ? 25.39046 22.25139 79.05286  1.000 20.45450  ? 56  ALA A CB  1 
ATOM   454  N  N   . GLN A 1 58  ? 26.06137 24.93578 80.65009  1.000 14.07801  ? 57  GLN A N   1 
ATOM   455  C  CA  . GLN A 1 58  ? 26.98975 25.98580 81.06742  1.000 13.09906  ? 57  GLN A CA  1 
ATOM   456  C  C   . GLN A 1 58  ? 27.21461 25.94602 82.57046  1.000 16.42935  ? 57  GLN A C   1 
ATOM   457  O  O   . GLN A 1 58  ? 28.35570 25.99973 83.04428  1.000 16.29999  ? 57  GLN A O   1 
ATOM   458  C  CB  . GLN A 1 58  ? 26.46848 27.36932 80.66550  1.000 13.96463  ? 57  GLN A CB  1 
ATOM   459  C  CG  . GLN A 1 58  ? 26.50909 27.67305 79.17801  1.000 15.04570  ? 57  GLN A CG  1 
ATOM   460  C  CD  . GLN A 1 58  ? 25.96002 29.04887 78.86774  1.000 15.57245  ? 57  GLN A CD  1 
ATOM   461  O  OE1 . GLN A 1 58  ? 26.50038 30.05844 79.31127  1.000 16.10396  ? 57  GLN A OE1 1 
ATOM   462  N  NE2 . GLN A 1 58  ? 24.85537 29.09265 78.13050  1.000 16.37597  ? 57  GLN A NE2 1 
ATOM   463  N  N   . ILE A 1 59  ? 26.13253 25.82688 83.33627  1.000 15.32207  ? 58  ILE A N   1 
ATOM   464  C  CA  . ILE A 1 59  ? 26.23767 25.87794 84.78904  1.000 14.08093  ? 58  ILE A CA  1 
ATOM   465  C  C   . ILE A 1 59  ? 26.91730 24.62305 85.32698  1.000 14.43546  ? 58  ILE A C   1 
ATOM   466  O  O   . ILE A 1 59  ? 27.73130 24.69519 86.25686  1.000 13.79569  ? 58  ILE A O   1 
ATOM   467  C  CB  . ILE A 1 59  ? 24.84846 26.14624 85.40111  1.000 14.19598  ? 58  ILE A CB  1 
ATOM   468  C  CG1 . ILE A 1 59  ? 24.42422 27.58505 85.07863  1.000 14.04263  ? 58  ILE A CG1 1 
ATOM   469  C  CG2 . ILE A 1 59  ? 24.82983 25.86078 86.89759  1.000 16.24487  ? 58  ILE A CG2 1 
ATOM   470  C  CD1 . ILE A 1 59  ? 23.01227 27.93913 85.50887  1.000 13.52410  ? 58  ILE A CD1 1 
ATOM   471  N  N   . ALA A 1 60  ? 26.63346 23.46316 84.72568  1.000 12.22184  ? 59  ALA A N   1 
ATOM   472  C  CA  . ALA A 1 60  ? 27.28410 22.22975 85.15560  1.000 12.20965  ? 59  ALA A CA  1 
ATOM   473  C  C   . ALA A 1 60  ? 28.79098 22.27558 84.92875  1.000 14.22976  ? 59  ALA A C   1 
ATOM   474  O  O   . ALA A 1 60  ? 29.54241 21.59472 85.63469  1.000 16.27306  ? 59  ALA A O   1 
ATOM   475  C  CB  . ALA A 1 60  ? 26.66200 21.03558 84.43195  1.000 15.93853  ? 59  ALA A CB  1 
ATOM   476  N  N   . LEU A 1 61  ? 29.24818 23.06580 83.95498  1.000 12.72035  ? 60  LEU A N   1 
ATOM   477  C  CA  . LEU A 1 61  ? 30.66766 23.18693 83.64637  1.000 14.29689  ? 60  LEU A CA  1 
ATOM   478  C  C   . LEU A 1 61  ? 31.38738 24.19814 84.52222  1.000 15.66058  ? 60  LEU A C   1 
ATOM   479  O  O   . LEU A 1 61  ? 32.61625 24.25501 84.47531  1.000 13.80866  ? 60  LEU A O   1 
ATOM   480  C  CB  . LEU A 1 61  ? 30.84761 23.59677 82.18336  1.000 15.46866  ? 60  LEU A CB  1 
ATOM   481  C  CG  . LEU A 1 61  ? 30.51421 22.54869 81.12437  1.000 13.39275  ? 60  LEU A CG  1 
ATOM   482  C  CD1 . LEU A 1 61  ? 30.34856 23.24495 79.77997  1.000 15.70095  ? 60  LEU A CD1 1 
ATOM   483  C  CD2 . LEU A 1 61  ? 31.60683 21.49512 81.05716  1.000 20.03771  ? 60  LEU A CD2 1 
ATOM   484  N  N   . GLN A 1 62  ? 30.66529 25.00114 85.29895  1.000 12.80067  ? 61  GLN A N   1 
ATOM   485  C  CA  . GLN A 1 62  ? 31.31881 26.05332 86.07730  1.000 11.57986  ? 61  GLN A CA  1 
ATOM   486  C  C   . GLN A 1 62  ? 32.35991 25.53959 87.06173  1.000 13.50217  ? 61  GLN A C   1 
ATOM   487  O  O   . GLN A 1 62  ? 33.43908 26.15214 87.15528  1.000 12.78966  ? 61  GLN A O   1 
ATOM   488  C  CB  . GLN A 1 62  ? 30.27834 26.94215 86.76142  1.000 12.78780  ? 61  GLN A CB  1 
ATOM   489  C  CG  . GLN A 1 62  ? 29.51982 27.83083 85.82498  1.000 13.64752  ? 61  GLN A CG  1 
ATOM   490  C  CD  . GLN A 1 62  ? 28.65184 28.81618 86.57329  1.000 15.56310  ? 61  GLN A CD  1 
ATOM   491  O  OE1 . GLN A 1 62  ? 28.31064 28.60722 87.73874  1.000 21.24830  ? 61  GLN A OE1 1 
ATOM   492  N  NE2 . GLN A 1 62  ? 28.30667 29.90938 85.91576  1.000 14.53666  ? 61  GLN A NE2 1 
ATOM   493  N  N   . PRO A 1 63  ? 32.10797 24.48585 87.84637  1.000 15.58944  ? 62  PRO A N   1 
ATOM   494  C  CA  . PRO A 1 63  ? 33.14954 24.03510 88.78142  1.000 15.39705  ? 62  PRO A CA  1 
ATOM   495  C  C   . PRO A 1 63  ? 34.43458 23.63443 88.08172  1.000 14.79305  ? 62  PRO A C   1 
ATOM   496  O  O   . PRO A 1 63  ? 35.52346 23.99179 88.54777  1.000 14.77170  ? 62  PRO A O   1 
ATOM   497  C  CB  . PRO A 1 63  ? 32.47747 22.86505 89.51403  1.000 14.78361  ? 62  PRO A CB  1 
ATOM   498  C  CG  . PRO A 1 63  ? 31.00544 23.17297 89.41827  1.000 15.30400  ? 62  PRO A CG  1 
ATOM   499  C  CD  . PRO A 1 63  ? 30.83393 23.76947 88.06208  1.000 13.52098  ? 62  PRO A CD  1 
ATOM   500  N  N   . ALA A 1 64  ? 34.34607 22.92569 86.95306  1.000 12.63327  ? 63  ALA A N   1 
ATOM   501  C  CA  . ALA A 1 64  ? 35.56442 22.56758 86.23447  1.000 15.36795  ? 63  ALA A CA  1 
ATOM   502  C  C   . ALA A 1 64  ? 36.24102 23.78769 85.62364  1.000 14.86565  ? 63  ALA A C   1 
ATOM   503  O  O   . ALA A 1 64  ? 37.47514 23.84139 85.56458  1.000 13.35066  ? 63  ALA A O   1 
ATOM   504  C  CB  . ALA A 1 64  ? 35.27459 21.51900 85.15888  1.000 15.57267  ? 63  ALA A CB  1 
ATOM   505  N  N   . LEU A 1 65  ? 35.46643 24.77124 85.16211  1.000 13.82823  ? 64  LEU A N   1 
ATOM   506  C  CA  . LEU A 1 65  ? 36.07581 25.95692 84.57032  1.000 13.99080  ? 64  LEU A CA  1 
ATOM   507  C  C   . LEU A 1 65  ? 36.81773 26.76965 85.62464  1.000 12.00102  ? 64  LEU A C   1 
ATOM   508  O  O   . LEU A 1 65  ? 37.95266 27.20303 85.39999  1.000 14.07246  ? 64  LEU A O   1 
ATOM   509  C  CB  . LEU A 1 65  ? 35.02054 26.79475 83.84112  1.000 13.44426  ? 64  LEU A CB  1 
ATOM   510  C  CG  . LEU A 1 65  ? 35.49643 27.86940 82.84988  1.000 13.63093  ? 64  LEU A CG  1 
ATOM   511  C  CD1 . LEU A 1 65  ? 35.97731 29.14006 83.55158  1.000 15.33300  ? 64  LEU A CD1 1 
ATOM   512  C  CD2 . LEU A 1 65  ? 36.58427 27.34432 81.91041  1.000 16.19759  ? 64  LEU A CD2 1 
ATOM   513  N  N   . LYS A 1 66  ? 36.19332 26.99077 86.78364  1.000 13.13468  ? 65  LYS A N   1 
ATOM   514  C  CA  . LYS A 1 66  ? 36.87156 27.74472 87.83186  1.000 12.88058  ? 65  LYS A CA  1 
ATOM   515  C  C   . LYS A 1 66  ? 38.07091 26.97596 88.37093  1.000 12.22656  ? 65  LYS A C   1 
ATOM   516  O  O   . LYS A 1 66  ? 39.12995 27.56302 88.62257  1.000 12.56297  ? 65  LYS A O   1 
ATOM   517  C  CB  . LYS A 1 66  ? 35.90645 28.10794 88.96313  1.000 14.29017  ? 65  LYS A CB  1 
ATOM   518  C  CG  . LYS A 1 66  ? 36.57441 28.91694 90.08378  1.000 12.57125  ? 65  LYS A CG  1 
ATOM   519  C  CD  . LYS A 1 66  ? 35.54589 29.47182 91.07128  1.000 16.81665  ? 65  LYS A CD  1 
ATOM   520  C  CE  . LYS A 1 66  ? 34.85051 28.34388 91.81682  1.000 16.53077  ? 65  LYS A CE  1 
ATOM   521  N  NZ  . LYS A 1 66  ? 34.18336 28.81037 93.06488  1.000 24.13396  ? 65  LYS A NZ  1 
ATOM   522  N  N   . PHE A 1 67  ? 37.93265 25.65584 88.52187  1.000 11.90959  ? 66  PHE A N   1 
ATOM   523  C  CA  . PHE A 1 67  ? 39.00506 24.84486 89.08816  1.000 11.73156  ? 66  PHE A CA  1 
ATOM   524  C  C   . PHE A 1 67  ? 40.21187 24.78533 88.15849  1.000 13.05611  ? 66  PHE A C   1 
ATOM   525  O  O   . PHE A 1 67  ? 41.34097 25.07211 88.57225  1.000 12.28208  ? 66  PHE A O   1 
ATOM   526  C  CB  . PHE A 1 67  ? 38.45973 23.44850 89.38869  1.000 11.75014  ? 66  PHE A CB  1 
ATOM   527  C  CG  . PHE A 1 67  ? 39.44223 22.54366 90.05970  1.000 12.20142  ? 66  PHE A CG  1 
ATOM   528  C  CD1 . PHE A 1 67  ? 39.92209 22.84420 91.32473  1.000 14.16438  ? 66  PHE A CD1 1 
ATOM   529  C  CD2 . PHE A 1 67  ? 39.83960 21.35968 89.45697  1.000 12.64076  ? 66  PHE A CD2 1 
ATOM   530  C  CE1 . PHE A 1 67  ? 40.80713 21.99394 91.96897  1.000 14.13890  ? 66  PHE A CE1 1 
ATOM   531  C  CE2 . PHE A 1 67  ? 40.73214 20.50219 90.09279  1.000 18.24780  ? 66  PHE A CE2 1 
ATOM   532  C  CZ  . PHE A 1 67  ? 41.21816 20.82316 91.35231  1.000 14.30907  ? 66  PHE A CZ  1 
ATOM   533  N  N   . ASN A 1 68  ? 39.99294 24.42649 86.89412  1.000 13.21795  ? 67  ASN A N   1 
ATOM   534  C  CA  . ASN A 1 68  ? 41.11028 24.28953 85.96830  1.000 14.07083  ? 67  ASN A CA  1 
ATOM   535  C  C   . ASN A 1 68  ? 41.58118 25.64307 85.46914  1.000 12.71233  ? 67  ASN A C   1 
ATOM   536  O  O   . ASN A 1 68  ? 42.78901 25.86429 85.31793  1.000 12.45419  ? 67  ASN A O   1 
ATOM   537  C  CB  . ASN A 1 68  ? 40.72167 23.41185 84.78592  1.000 14.55056  ? 67  ASN A CB  1 
ATOM   538  C  CG  . ASN A 1 68  ? 40.45809 21.99655 85.19584  1.000 13.66189  ? 67  ASN A CG  1 
ATOM   539  O  OD1 . ASN A 1 68  ? 41.35258 21.31659 85.68826  1.000 18.99794  ? 67  ASN A OD1 1 
ATOM   540  N  ND2 . ASN A 1 68  ? 39.23901 21.52584 84.95960  1.000 15.74870  ? 67  ASN A ND2 1 
ATOM   541  N  N   . GLY A 1 69  ? 40.64358 26.55261 85.19623  1.000 12.39788  ? 68  GLY A N   1 
ATOM   542  C  CA  . GLY A 1 69  ? 41.02989 27.89964 84.81053  1.000 12.16912  ? 68  GLY A CA  1 
ATOM   543  C  C   . GLY A 1 69  ? 41.78569 28.61584 85.91125  1.000 13.42202  ? 68  GLY A C   1 
ATOM   544  O  O   . GLY A 1 69  ? 42.84348 29.20561 85.67410  1.000 13.02261  ? 68  GLY A O   1 
ATOM   545  N  N   . GLY A 1 70  ? 41.27077 28.54084 87.13907  1.000 12.80613  ? 69  GLY A N   1 
ATOM   546  C  CA  . GLY A 1 70  ? 41.99659 29.09605 88.26746  1.000 12.20108  ? 69  GLY A CA  1 
ATOM   547  C  C   . GLY A 1 70  ? 43.33726 28.42106 88.48487  1.000 12.40192  ? 69  GLY A C   1 
ATOM   548  O  O   . GLY A 1 70  ? 44.33264 29.08586 88.77379  1.000 13.49015  ? 69  GLY A O   1 
ATOM   549  N  N   . GLY A 1 71  ? 43.38744 27.09410 88.34143  1.000 10.55032  ? 70  GLY A N   1 
ATOM   550  C  CA  . GLY A 1 71  ? 44.66003 26.40055 88.46940  1.000 12.13547  ? 70  GLY A CA  1 
ATOM   551  C  C   . GLY A 1 71  ? 45.69642 26.93092 87.50155  1.000 12.15182  ? 70  GLY A C   1 
ATOM   552  O  O   . GLY A 1 71  ? 46.85534 27.12787 87.86734  1.000 13.89451  ? 70  GLY A O   1 
ATOM   553  N  N   . HIS A 1 72  ? 45.28857 27.19061 86.25997  1.000 12.57667  ? 71  HIS A N   1 
ATOM   554  C  CA  . HIS A 1 72  ? 46.20744 27.73649 85.26714  1.000 11.14901  ? 71  HIS A CA  1 
ATOM   555  C  C   . HIS A 1 72  ? 46.61165 29.16239 85.61759  1.000 11.43296  ? 71  HIS A C   1 
ATOM   556  O  O   . HIS A 1 72  ? 47.79798 29.51732 85.56706  1.000 12.30044  ? 71  HIS A O   1 
ATOM   557  C  CB  . HIS A 1 72  ? 45.55200 27.67845 83.88816  1.000 12.88366  ? 71  HIS A CB  1 
ATOM   558  C  CG  . HIS A 1 72  ? 46.41953 28.19595 82.78517  1.000 11.80625  ? 71  HIS A CG  1 
ATOM   559  N  ND1 . HIS A 1 72  ? 47.75164 27.85999 82.67155  1.000 13.83328  ? 71  HIS A ND1 1 
ATOM   560  C  CD2 . HIS A 1 72  ? 46.13948 28.99554 81.72851  1.000 13.16393  ? 71  HIS A CD2 1 
ATOM   561  C  CE1 . HIS A 1 72  ? 48.25779 28.44009 81.59876  1.000 15.08614  ? 71  HIS A CE1 1 
ATOM   562  N  NE2 . HIS A 1 72  ? 47.30136 29.12998 81.00562  1.000 13.56049  ? 71  HIS A NE2 1 
ATOM   563  N  N   . ILE A 1 73  ? 45.63315 29.99012 85.98815  1.000 11.56986  ? 72  ILE A N   1 
ATOM   564  C  CA  . ILE A 1 73  ? 45.91810 31.37467 86.36114  1.000 12.30548  ? 72  ILE A CA  1 
ATOM   565  C  C   . ILE A 1 73  ? 46.86884 31.42086 87.54631  1.000 11.23671  ? 72  ILE A C   1 
ATOM   566  O  O   . ILE A 1 73  ? 47.86917 32.15109 87.53585  1.000 12.12680  ? 72  ILE A O   1 
ATOM   567  C  CB  . ILE A 1 73  ? 44.60939 32.11521 86.68766  1.000 12.26283  ? 72  ILE A CB  1 
ATOM   568  C  CG1 . ILE A 1 73  ? 43.75076 32.31041 85.43731  1.000 13.30047  ? 72  ILE A CG1 1 
ATOM   569  C  CG2 . ILE A 1 73  ? 44.90635 33.44445 87.39467  1.000 12.68741  ? 72  ILE A CG2 1 
ATOM   570  C  CD1 . ILE A 1 73  ? 42.31177 32.69500 85.75088  1.000 15.44351  ? 72  ILE A CD1 1 
ATOM   571  N  N   . ASN A 1 74  ? 46.55679 30.65662 88.59592  1.000 11.83808  ? 73  ASN A N   1 
ATOM   572  C  CA  . ASN A 1 74  ? 47.30480 30.74809 89.84586  1.000 12.55251  ? 73  ASN A CA  1 
ATOM   573  C  C   . ASN A 1 74  ? 48.73250 30.25740 89.67756  1.000 11.28849  ? 73  ASN A C   1 
ATOM   574  O  O   . ASN A 1 74  ? 49.68045 30.90594 90.14070  1.000 12.71849  ? 73  ASN A O   1 
ATOM   575  C  CB  . ASN A 1 74  ? 46.61418 29.95039 90.94498  1.000 11.48680  ? 73  ASN A CB  1 
ATOM   576  C  CG  . ASN A 1 74  ? 45.21593 30.44681 91.23281  1.000 10.40724  ? 73  ASN A CG  1 
ATOM   577  O  OD1 . ASN A 1 74  ? 44.88777 31.60748 90.96917  1.000 12.03442  ? 73  ASN A OD1 1 
ATOM   578  N  ND2 . ASN A 1 74  ? 44.38397 29.57478 91.78619  1.000 12.79797  ? 73  ASN A ND2 1 
ATOM   579  N  N   . HIS A 1 75  ? 48.90946 29.09639 89.04104  1.000 11.78561  ? 74  HIS A N   1 
ATOM   580  C  CA  . HIS A 1 75  ? 50.26103 28.56571 88.90035  1.000 11.15746  ? 74  HIS A CA  1 
ATOM   581  C  C   . HIS A 1 75  ? 51.10467 29.39722 87.94085  1.000 14.74987  ? 74  HIS A C   1 
ATOM   582  O  O   . HIS A 1 75  ? 52.31277 29.53994 88.15588  1.000 14.34597  ? 74  HIS A O   1 
ATOM   583  C  CB  . HIS A 1 75  ? 50.24026 27.08686 88.51461  1.000 12.93134  ? 74  HIS A CB  1 
ATOM   584  C  CG  . HIS A 1 75  ? 49.72007 26.20139 89.60285  1.000 11.82601  ? 74  HIS A CG  1 
ATOM   585  N  ND1 . HIS A 1 75  ? 48.37389 25.97829 89.79463  1.000 13.02800  ? 74  HIS A ND1 1 
ATOM   586  C  CD2 . HIS A 1 75  ? 50.35752 25.53614 90.59609  1.000 13.83349  ? 74  HIS A CD2 1 
ATOM   587  C  CE1 . HIS A 1 75  ? 48.20654 25.18772 90.83975  1.000 13.88232  ? 74  HIS A CE1 1 
ATOM   588  N  NE2 . HIS A 1 75  ? 49.39418 24.90739 91.34732  1.000 13.96270  ? 74  HIS A NE2 1 
ATOM   589  N  N   . SER A 1 76  ? 50.49810 29.95367 86.88838  1.000 12.21250  ? 75  SER A N   1 
ATOM   590  C  CA  . SER A 1 76  ? 51.26019 30.79475 85.97062  1.000 12.69125  ? 75  SER A CA  1 
ATOM   591  C  C   . SER A 1 76  ? 51.83848 31.99889 86.69931  1.000 12.52376  ? 75  SER A C   1 
ATOM   592  O  O   . SER A 1 76  ? 52.98605 32.39415 86.45620  1.000 14.73541  ? 75  SER A O   1 
ATOM   593  C  CB  . SER A 1 76  ? 50.38839 31.24254 84.79868  1.000 14.44025  ? 75  SER A CB  1 
ATOM   594  O  OG  . SER A 1 76  ? 49.99389 30.13667 83.99909  1.000 14.50759  ? 75  SER A OG  1 
ATOM   595  N  N   . ILE A 1 77  ? 51.06844 32.57611 87.62325  1.000 12.57191  ? 76  ILE A N   1 
ATOM   596  C  CA  . ILE A 1 77  ? 51.59153 33.66347 88.44328  1.000 10.71755  ? 76  ILE A CA  1 
ATOM   597  C  C   . ILE A 1 77  ? 52.63552 33.13355 89.41508  1.000 12.25632  ? 76  ILE A C   1 
ATOM   598  O  O   . ILE A 1 77  ? 53.69640 33.74098 89.60112  1.000 12.18847  ? 76  ILE A O   1 
ATOM   599  C  CB  . ILE A 1 77  ? 50.44560 34.38486 89.17787  1.000 12.67902  ? 76  ILE A CB  1 
ATOM   600  C  CG1 . ILE A 1 77  ? 49.50480 35.07156 88.18598  1.000 14.80817  ? 76  ILE A CG1 1 
ATOM   601  C  CG2 . ILE A 1 77  ? 50.99847 35.41668 90.16288  1.000 15.25274  ? 76  ILE A CG2 1 
ATOM   602  C  CD1 . ILE A 1 77  ? 48.13991 35.40911 88.78292  1.000 13.53521  ? 76  ILE A CD1 1 
ATOM   603  N  N   . PHE A 1 78  ? 52.35461 31.98319 90.03368  1.000 12.51836  ? 77  PHE A N   1 
ATOM   604  C  CA  . PHE A 1 78  ? 53.20314 31.45676 91.09721  1.000 12.35415  ? 77  PHE A CA  1 
ATOM   605  C  C   . PHE A 1 78  ? 54.63644 31.25489 90.62365  1.000 12.88836  ? 77  PHE A C   1 
ATOM   606  O  O   . PHE A 1 78  ? 55.58375 31.61763 91.33303  1.000 12.99019  ? 77  PHE A O   1 
ATOM   607  C  CB  . PHE A 1 78  ? 52.61314 30.13823 91.59785  1.000 11.61519  ? 77  PHE A CB  1 
ATOM   608  C  CG  . PHE A 1 78  ? 53.25634 29.60476 92.85080  1.000 11.83185  ? 77  PHE A CG  1 
ATOM   609  C  CD1 . PHE A 1 78  ? 53.33962 30.38929 93.99196  1.000 12.37558  ? 77  PHE A CD1 1 
ATOM   610  C  CD2 . PHE A 1 78  ? 53.72601 28.29697 92.90220  1.000 12.09487  ? 77  PHE A CD2 1 
ATOM   611  C  CE1 . PHE A 1 78  ? 53.91287 29.89362 95.15717  1.000 12.97133  ? 77  PHE A CE1 1 
ATOM   612  C  CE2 . PHE A 1 78  ? 54.29985 27.79209 94.06139  1.000 11.86166  ? 77  PHE A CE2 1 
ATOM   613  C  CZ  . PHE A 1 78  ? 54.38913 28.59548 95.19261  1.000 12.60482  ? 77  PHE A CZ  1 
ATOM   614  N  N   . TRP A 1 79  ? 54.82496 30.69219 89.42428  1.000 13.32777  ? 78  TRP A N   1 
ATOM   615  C  CA  . TRP A 1 79  ? 56.19087 30.43980 88.96350  1.000 12.88826  ? 78  TRP A CA  1 
ATOM   616  C  C   . TRP A 1 79  ? 56.97384 31.73598 88.83458  1.000 13.18908  ? 78  TRP A C   1 
ATOM   617  O  O   . TRP A 1 79  ? 58.16908 31.77536 89.13989  1.000 14.17855  ? 78  TRP A O   1 
ATOM   618  C  CB  . TRP A 1 79  ? 56.22651 29.68451 87.63268  1.000 12.84619  ? 78  TRP A CB  1 
ATOM   619  C  CG  . TRP A 1 79  ? 55.34706 28.48138 87.55483  1.000 12.11217  ? 78  TRP A CG  1 
ATOM   620  C  CD1 . TRP A 1 79  ? 54.50149 28.16919 86.53347  1.000 14.90976  ? 78  TRP A CD1 1 
ATOM   621  C  CD2 . TRP A 1 79  ? 55.21162 27.42813 88.52304  1.000 12.28832  ? 78  TRP A CD2 1 
ATOM   622  N  NE1 . TRP A 1 79  ? 53.85128 26.99516 86.79676  1.000 13.25165  ? 78  TRP A NE1 1 
ATOM   623  C  CE2 . TRP A 1 79  ? 54.26174 26.51908 88.01315  1.000 12.14723  ? 78  TRP A CE2 1 
ATOM   624  C  CE3 . TRP A 1 79  ? 55.79849 27.16310 89.76720  1.000 13.56879  ? 78  TRP A CE3 1 
ATOM   625  C  CZ2 . TRP A 1 79  ? 53.88485 25.36449 88.69870  1.000 12.59390  ? 78  TRP A CZ2 1 
ATOM   626  C  CZ3 . TRP A 1 79  ? 55.42595 26.01205 90.44599  1.000 13.81720  ? 78  TRP A CZ3 1 
ATOM   627  C  CH2 . TRP A 1 79  ? 54.46892 25.13422 89.91342  1.000 14.68460  ? 78  TRP A CH2 1 
ATOM   628  N  N   . THR A 1 80  ? 56.32440 32.80279 88.36417  1.000 12.45779  ? 79  THR A N   1 
ATOM   629  C  CA  . THR A 1 80  ? 57.01853 34.07916 88.24110  1.000 14.89858  ? 79  THR A CA  1 
ATOM   630  C  C   . THR A 1 80  ? 57.22486 34.75573 89.58979  1.000 14.57091  ? 79  THR A C   1 
ATOM   631  O  O   . THR A 1 80  ? 58.11118 35.60682 89.70704  1.000 14.36201  ? 79  THR A O   1 
ATOM   632  C  CB  . THR A 1 80  ? 56.27608 35.02182 87.28691  1.000 16.58489  ? 79  THR A CB  1 
ATOM   633  O  OG1 . THR A 1 80  ? 55.05249 35.46470 87.89062  1.000 16.07366  ? 79  THR A OG1 1 
ATOM   634  C  CG2 . THR A 1 80  ? 55.97268 34.33069 85.96696  1.000 16.64897  ? 79  THR A CG2 1 
ATOM   635  N  N   . ASN A 1 81  ? 56.42895 34.40118 90.60253  1.000 13.36785  ? 80  ASN A N   1 
ATOM   636  C  CA  . ASN A 1 81  ? 56.58979 34.94949 91.94340  1.000 15.14951  ? 80  ASN A CA  1 
ATOM   637  C  C   . ASN A 1 81  ? 57.78433 34.35924 92.68331  1.000 13.54612  ? 80  ASN A C   1 
ATOM   638  O  O   . ASN A 1 81  ? 58.10830 34.84636 93.77205  1.000 14.16901  ? 80  ASN A O   1 
ATOM   639  C  CB  . ASN A 1 81  ? 55.35048 34.68458 92.80477  1.000 12.67577  ? 80  ASN A CB  1 
ATOM   640  C  CG  . ASN A 1 81  ? 54.16775 35.58533 92.48273  1.000 13.90998  ? 80  ASN A CG  1 
ATOM   641  O  OD1 . ASN A 1 81  ? 53.05698 35.27871 92.89952  1.000 12.65459  ? 80  ASN A OD1 1 
ATOM   642  N  ND2 . ASN A 1 81  ? 54.39188 36.69339 91.77693  1.000 13.78832  ? 80  ASN A ND2 1 
ATOM   643  N  N   . LEU A 1 82  ? 58.41346 33.31253 92.15224  1.000 14.29522  ? 81  LEU A N   1 
ATOM   644  C  CA  . LEU A 1 82  ? 59.55315 32.67710 92.79822  1.000 13.30254  ? 81  LEU A CA  1 
ATOM   645  C  C   . LEU A 1 82  ? 60.76001 32.79682 91.88333  1.000 12.81161  ? 81  LEU A C   1 
ATOM   646  O  O   . LEU A 1 82  ? 60.62450 32.89489 90.66018  1.000 13.61543  ? 81  LEU A O   1 
ATOM   647  C  CB  . LEU A 1 82  ? 59.31621 31.18530 93.05208  1.000 14.29234  ? 81  LEU A CB  1 
ATOM   648  C  CG  . LEU A 1 82  ? 57.98005 30.78486 93.66854  1.000 13.56583  ? 81  LEU A CG  1 
ATOM   649  C  CD1 . LEU A 1 82  ? 57.85079 29.26173 93.71610  1.000 16.06123  ? 81  LEU A CD1 1 
ATOM   650  C  CD2 . LEU A 1 82  ? 57.84056 31.39296 95.05251  1.000 15.33006  ? 81  LEU A CD2 1 
ATOM   651  N  N   . SER A 1 83  ? 61.94859 32.78028 92.48533  1.000 15.40312  ? 82  SER A N   1 
ATOM   652  C  CA  . SER A 1 83  ? 63.16439 32.87325 91.69385  1.000 13.96678  ? 82  SER A CA  1 
ATOM   653  C  C   . SER A 1 83  ? 64.37464 32.48573 92.52943  1.000 16.18891  ? 82  SER A C   1 
ATOM   654  O  O   . SER A 1 83  ? 64.40913 32.75755 93.73745  1.000 15.26277  ? 82  SER A O   1 
ATOM   655  C  CB  . SER A 1 83  ? 63.34845 34.29788 91.17391  1.000 18.32503  ? 82  SER A CB  1 
ATOM   656  O  OG  . SER A 1 83  ? 64.57769 34.42348 90.48330  1.000 20.19947  ? 82  SER A OG  1 
ATOM   657  N  N   . PRO A 1 84  ? 65.39286 31.87578 91.92042  1.000 13.29116  ? 83  PRO A N   1 
ATOM   658  C  CA  . PRO A 1 84  ? 66.65728 31.67249 92.64613  1.000 15.02385  ? 83  PRO A CA  1 
ATOM   659  C  C   . PRO A 1 84  ? 67.30560 32.97202 93.08627  1.000 19.42298  ? 83  PRO A C   1 
ATOM   660  O  O   . PRO A 1 84  ? 68.04569 32.98361 94.07792  1.000 19.14004  ? 83  PRO A O   1 
ATOM   661  C  CB  . PRO A 1 84  ? 67.51863 30.89143 91.64323  1.000 17.12638  ? 83  PRO A CB  1 
ATOM   662  C  CG  . PRO A 1 84  ? 66.90832 31.16254 90.31247  1.000 18.75042  ? 83  PRO A CG  1 
ATOM   663  C  CD  . PRO A 1 84  ? 65.43750 31.33721 90.55362  1.000 14.63429  ? 83  PRO A CD  1 
ATOM   664  N  N   . ASN A 1 85  ? 67.02480 34.07031 92.38791  1.000 18.40358  ? 84  ASN A N   1 
ATOM   665  C  CA  . ASN A 1 85  ? 67.49843 35.40093 92.73750  1.000 25.01850  ? 84  ASN A CA  1 
ATOM   666  C  C   . ASN A 1 85  ? 66.58414 36.10247 93.74138  1.000 26.22995  ? 84  ASN A C   1 
ATOM   667  O  O   . ASN A 1 85  ? 66.76740 37.29624 94.00551  1.000 27.43658  ? 84  ASN A O   1 
ATOM   668  C  CB  . ASN A 1 85  ? 67.60652 36.24075 91.45957  1.000 31.86083  ? 84  ASN A CB  1 
ATOM   669  C  CG  . ASN A 1 85  ? 68.32401 37.55543 91.67593  1.000 44.29617  ? 84  ASN A CG  1 
ATOM   670  O  OD1 . ASN A 1 85  ? 67.77875 38.62344 91.40030  1.000 56.75052  ? 84  ASN A OD1 1 
ATOM   671  N  ND2 . ASN A 1 85  ? 69.54777 37.48629 92.18666  1.000 48.50729  ? 84  ASN A ND2 1 
ATOM   672  N  N   . GLY A 1 86  ? 65.60649 35.39440 94.30411  1.000 17.75882  ? 85  GLY A N   1 
ATOM   673  C  CA  . GLY A 1 86  ? 64.62718 35.99629 95.18166  1.000 18.84270  ? 85  GLY A CA  1 
ATOM   674  C  C   . GLY A 1 86  ? 65.06975 36.07125 96.63220  1.000 20.31122  ? 85  GLY A C   1 
ATOM   675  O  O   . GLY A 1 86  ? 66.23945 35.89050 96.97792  1.000 21.44215  ? 85  GLY A O   1 
ATOM   676  N  N   . GLY A 1 87  ? 64.09317 36.34866 97.49687  1.000 17.19865  ? 86  GLY A N   1 
ATOM   677  C  CA  . GLY A 1 87  ? 64.34554 36.48670 98.91568  1.000 18.35333  ? 86  GLY A CA  1 
ATOM   678  C  C   . GLY A 1 87  ? 64.60720 37.92286 99.32006  1.000 18.64845  ? 86  GLY A C   1 
ATOM   679  O  O   . GLY A 1 87  ? 64.57710 38.85848 98.51599  1.000 19.87309  ? 86  GLY A O   1 
ATOM   680  N  N   . GLY A 1 88  ? 64.87932 38.09216 100.61321 1.000 21.69231  ? 87  GLY A N   1 
ATOM   681  C  CA  . GLY A 1 88  ? 65.15490 39.42315 101.11163 1.000 23.02782  ? 87  GLY A CA  1 
ATOM   682  C  C   . GLY A 1 88  ? 63.89773 40.27517 101.11769 1.000 26.55155  ? 87  GLY A C   1 
ATOM   683  O  O   . GLY A 1 88  ? 62.78025 39.79136 101.31648 1.000 24.76084  ? 87  GLY A O   1 
ATOM   684  N  N   . GLU A 1 89  ? 64.08625 41.57102 100.89850 1.000 24.38900  ? 88  GLU A N   1 
ATOM   685  C  CA  . GLU A 1 89  ? 62.96097 42.48508 100.91222 1.000 23.80216  ? 88  GLU A CA  1 
ATOM   686  C  C   . GLU A 1 89  ? 62.84843 43.20572 99.57467  1.000 22.18044  ? 88  GLU A C   1 
ATOM   687  O  O   . GLU A 1 89  ? 63.85166 43.38254 98.87164  1.000 24.14800  ? 88  GLU A O   1 
ATOM   688  C  CB  . GLU A 1 89  ? 63.12149 43.53059 102.02386 1.000 25.84714  ? 88  GLU A CB  1 
ATOM   689  C  CG  . GLU A 1 89  ? 63.32207 42.94542 103.41207 1.000 27.10659  ? 88  GLU A CG  1 
ATOM   690  C  CD  . GLU A 1 89  ? 63.17587 43.98675 104.50634 1.000 31.19376  ? 88  GLU A CD  1 
ATOM   691  O  OE1 . GLU A 1 89  ? 62.85648 45.15183 104.18224 1.000 25.39913  ? 88  GLU A OE1 1 
ATOM   692  O  OE2 . GLU A 1 89  ? 63.36361 43.63594 105.69075 1.000 33.86840  ? 88  GLU A OE2 1 
ATOM   693  N  N   . PRO A 1 90  ? 61.64700 43.63882 99.19777  1.000 18.67655  ? 89  PRO A N   1 
ATOM   694  C  CA  . PRO A 1 90  ? 61.50971 44.50555 98.02571  1.000 19.32968  ? 89  PRO A CA  1 
ATOM   695  C  C   . PRO A 1 90  ? 62.02906 45.89623 98.35360  1.000 22.92862  ? 89  PRO A C   1 
ATOM   696  O  O   . PRO A 1 90  ? 62.35389 46.22055 99.49672  1.000 20.92856  ? 89  PRO A O   1 
ATOM   697  C  CB  . PRO A 1 90  ? 59.99738 44.52789 97.78573  1.000 24.41825  ? 89  PRO A CB  1 
ATOM   698  C  CG  . PRO A 1 90  ? 59.42231 44.35125 99.14072  1.000 18.63501  ? 89  PRO A CG  1 
ATOM   699  C  CD  . PRO A 1 90  ? 60.34970 43.40151 99.85450  1.000 20.83395  ? 89  PRO A CD  1 
ATOM   700  N  N   . LYS A 1 91  ? 62.08758 46.73129 97.32552  1.000 24.41151  ? 90  LYS A N   1 
ATOM   701  C  CA  . LYS A 1 91  ? 62.57641 48.09385 97.45425  1.000 27.85021  ? 90  LYS A CA  1 
ATOM   702  C  C   . LYS A 1 91  ? 61.58474 49.03586 96.78698  1.000 32.93839  ? 90  LYS A C   1 
ATOM   703  O  O   . LYS A 1 91  ? 60.56095 48.61295 96.24051  1.000 30.73662  ? 90  LYS A O   1 
ATOM   704  C  CB  . LYS A 1 91  ? 63.96302 48.23722 96.81150  1.000 32.70841  ? 90  LYS A CB  1 
ATOM   705  C  CG  . LYS A 1 91  ? 63.97924 47.90673 95.32488  1.000 49.32501  ? 90  LYS A CG  1 
ATOM   706  C  CD  . LYS A 1 91  ? 65.33738 48.17461 94.69188  1.000 64.25713  ? 90  LYS A CD  1 
ATOM   707  C  CE  . LYS A 1 91  ? 65.28783 47.96455 93.18282  1.000 68.28175  ? 90  LYS A CE  1 
ATOM   708  N  NZ  . LYS A 1 91  ? 66.58132 48.28987 92.51717  1.000 64.24696  ? 90  LYS A NZ  1 
ATOM   709  N  N   . GLY A 1 92  ? 61.89247 50.32847 96.84481  1.000 26.94158  ? 91  GLY A N   1 
ATOM   710  C  CA  . GLY A 1 92  ? 61.12941 51.31864 96.12020  1.000 25.79740  ? 91  GLY A CA  1 
ATOM   711  C  C   . GLY A 1 92  ? 59.69343 51.43844 96.59623  1.000 22.31770  ? 91  GLY A C   1 
ATOM   712  O  O   . GLY A 1 92  ? 59.36862 51.25020 97.77547  1.000 24.04264  ? 91  GLY A O   1 
ATOM   713  N  N   . GLU A 1 93  ? 58.81252 51.75202 95.64398  1.000 25.62260  ? 92  GLU A N   1 
ATOM   714  C  CA  . GLU A 1 93  ? 57.42746 52.06847 95.97592  1.000 23.34681  ? 92  GLU A CA  1 
ATOM   715  C  C   . GLU A 1 93  ? 56.68150 50.87254 96.55730  1.000 18.46765  ? 92  GLU A C   1 
ATOM   716  O  O   . GLU A 1 93  ? 55.76013 51.05592 97.36164  1.000 19.27896  ? 92  GLU A O   1 
ATOM   717  C  CB  . GLU A 1 93  ? 56.70787 52.61705 94.74741  1.000 27.31979  ? 92  GLU A CB  1 
ATOM   718  C  CG  . GLU A 1 93  ? 57.27720 53.93805 94.25947  1.000 36.93555  ? 92  GLU A CG  1 
ATOM   719  C  CD  . GLU A 1 93  ? 56.62164 54.42155 92.98483  1.000 40.28493  ? 92  GLU A CD  1 
ATOM   720  O  OE1 . GLU A 1 93  ? 55.41634 54.15719 92.79895  1.000 40.17812  ? 92  GLU A OE1 1 
ATOM   721  O  OE2 . GLU A 1 93  ? 57.31246 55.06598 92.16857  1.000 50.10445  ? 92  GLU A OE2 1 
ATOM   722  N  N   . LEU A 1 94  ? 57.03982 49.64967 96.15979  1.000 22.87539  ? 93  LEU A N   1 
ATOM   723  C  CA  . LEU A 1 94  ? 56.38216 48.49011 96.75475  1.000 18.27838  ? 93  LEU A CA  1 
ATOM   724  C  C   . LEU A 1 94  ? 56.71592 48.37293 98.23642  1.000 19.28483  ? 93  LEU A C   1 
ATOM   725  O  O   . LEU A 1 94  ? 55.82959 48.11939 99.05976  1.000 18.27710  ? 93  LEU A O   1 
ATOM   726  C  CB  . LEU A 1 94  ? 56.74978 47.20938 96.00765  1.000 19.69004  ? 93  LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 94  ? 56.12397 45.94607 96.60840  1.000 18.96751  ? 93  LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 94  ? 54.60477 46.04949 96.64887  1.000 22.61015  ? 93  LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 94  ? 56.55642 44.71604 95.83395  1.000 19.13555  ? 93  LEU A CD2 1 
ATOM   730  N  N   . LEU A 1 95  ? 57.98745 48.56135 98.59929  1.000 20.47581  ? 94  LEU A N   1 
ATOM   731  C  CA  . LEU A 1 95  ? 58.34929 48.52908 100.01231 1.000 21.05542  ? 94  LEU A CA  1 
ATOM   732  C  C   . LEU A 1 95  ? 57.65894 49.64928 100.77784 1.000 19.87181  ? 94  LEU A C   1 
ATOM   733  O  O   . LEU A 1 95  ? 57.18838 49.44324 101.90261 1.000 19.83746  ? 94  LEU A O   1 
ATOM   734  C  CB  . LEU A 1 95  ? 59.86742 48.61527 100.17963 1.000 21.74869  ? 94  LEU A CB  1 
ATOM   735  C  CG  . LEU A 1 95  ? 60.33746 48.58605 101.63672 1.000 19.78575  ? 94  LEU A CG  1 
ATOM   736  C  CD1 . LEU A 1 95  ? 60.03089 47.24434 102.28617 1.000 24.48107  ? 94  LEU A CD1 1 
ATOM   737  C  CD2 . LEU A 1 95  ? 61.82283 48.91048 101.73183 1.000 21.75301  ? 94  LEU A CD2 1 
ATOM   738  N  N   . GLU A 1 96  ? 57.57230 50.83709 100.17413 1.000 23.34761  ? 95  GLU A N   1 
ATOM   739  C  CA  . GLU A 1 96  ? 56.87044 51.94687 100.81447 1.000 22.55701  ? 95  GLU A CA  1 
ATOM   740  C  C   . GLU A 1 96  ? 55.40792 51.60362 101.05367 1.000 20.37409  ? 95  GLU A C   1 
ATOM   741  O  O   . GLU A 1 96  ? 54.86641 51.87751 102.13101 1.000 21.30937  ? 95  GLU A O   1 
ATOM   742  C  CB  . GLU A 1 96  ? 56.96629 53.20224 99.94564  1.000 21.76758  ? 95  GLU A CB  1 
ATOM   743  C  CG  . GLU A 1 96  ? 58.38504 53.69544 99.69479  1.000 36.46122  ? 95  GLU A CG  1 
ATOM   744  C  CD  . GLU A 1 96  ? 58.44900 54.77722 98.62754  1.000 51.86388  ? 95  GLU A CD  1 
ATOM   745  O  OE1 . GLU A 1 96  ? 57.41159 55.42473 98.36717  1.000 48.10690  ? 95  GLU A OE1 1 
ATOM   746  O  OE2 . GLU A 1 96  ? 59.53586 54.97218 98.03997  1.000 39.93210  ? 95  GLU A OE2 1 
ATOM   747  N  N   . ALA A 1 97  ? 54.75609 50.99217 100.06038 1.000 19.47436  ? 96  ALA A N   1 
ATOM   748  C  CA  . ALA A 1 97  ? 53.34847 50.63233 100.20017 1.000 17.81803  ? 96  ALA A CA  1 
ATOM   749  C  C   . ALA A 1 97  ? 53.15904 49.56870 101.26931 1.000 17.23791  ? 96  ALA A C   1 
ATOM   750  O  O   . ALA A 1 97  ? 52.18969 49.61393 102.03591 1.000 19.07975  ? 96  ALA A O   1 
ATOM   751  C  CB  . ALA A 1 97  ? 52.80177 50.14800 98.85834  1.000 18.59852  ? 96  ALA A CB  1 
ATOM   752  N  N   . ILE A 1 98  ? 54.07695 48.60378 101.33469 1.000 16.52714  ? 97  ILE A N   1 
ATOM   753  C  CA  . ILE A 1 98  ? 53.99771 47.56953 102.35987 1.000 18.91730  ? 97  ILE A CA  1 
ATOM   754  C  C   . ILE A 1 98  ? 54.09685 48.19043 103.74757 1.000 19.07162  ? 97  ILE A C   1 
ATOM   755  O  O   . ILE A 1 98  ? 53.29818 47.88824 104.64110 1.000 20.59018  ? 97  ILE A O   1 
ATOM   756  C  CB  . ILE A 1 98  ? 55.07658 46.50042 102.11853 1.000 16.82365  ? 97  ILE A CB  1 
ATOM   757  C  CG1 . ILE A 1 98  ? 54.69782 45.65889 100.89639 1.000 18.94166  ? 97  ILE A CG1 1 
ATOM   758  C  CG2 . ILE A 1 98  ? 55.24191 45.62385 103.34489 1.000 20.60350  ? 97  ILE A CG2 1 
ATOM   759  C  CD1 . ILE A 1 98  ? 55.75465 44.66754 100.48558 1.000 19.33081  ? 97  ILE A CD1 1 
ATOM   760  N  N   . LYS A 1 99  ? 55.06473 49.09171 103.94005 1.000 20.04968  ? 98  LYS A N   1 
ATOM   761  C  CA  . LYS A 1 99  ? 55.20116 49.75731 105.23299 1.000 23.92084  ? 98  LYS A CA  1 
ATOM   762  C  C   . LYS A 1 99  ? 53.96930 50.59562 105.55338 1.000 21.24326  ? 98  LYS A C   1 
ATOM   763  O  O   . LYS A 1 99  ? 53.49968 50.61258 106.69608 1.000 21.90554  ? 98  LYS A O   1 
ATOM   764  C  CB  . LYS A 1 99  ? 56.45277 50.63720 105.24231 1.000 23.42127  ? 98  LYS A CB  1 
ATOM   765  C  CG  . LYS A 1 99  ? 57.76698 49.87564 105.15578 1.000 23.58369  ? 98  LYS A CG  1 
ATOM   766  C  CD  . LYS A 1 99  ? 58.94013 50.84100 105.08712 1.000 25.00837  ? 98  LYS A CD  1 
ATOM   767  C  CE  . LYS A 1 99  ? 60.26742 50.11187 105.03203 1.000 29.70378  ? 98  LYS A CE  1 
ATOM   768  N  NZ  . LYS A 1 99  ? 61.39438 51.07220 104.85890 1.000 30.43026  ? 98  LYS A NZ  1 
ATOM   769  N  N   . ARG A 1 100 ? 53.42444 51.28629 104.55271 1.000 21.37689  ? 99  ARG A N   1 
ATOM   770  C  CA  . ARG A 1 100 ? 52.27171 52.14999 104.78703 1.000 23.63358  ? 99  ARG A CA  1 
ATOM   771  C  C   . ARG A 1 100 ? 51.02674 51.33858 105.12574 1.000 22.85504  ? 99  ARG A C   1 
ATOM   772  O  O   . ARG A 1 100 ? 50.28537 51.68204 106.05525 1.000 24.60656  ? 99  ARG A O   1 
ATOM   773  C  CB  . ARG A 1 100 ? 52.03007 53.02602 103.55791 1.000 22.30528  ? 99  ARG A CB  1 
ATOM   774  C  CG  . ARG A 1 100 ? 50.77542 53.88130 103.63462 1.000 32.81009  ? 99  ARG A CG  1 
ATOM   775  C  CD  . ARG A 1 100 ? 50.66029 54.84070 102.45092 1.000 38.52095  ? 99  ARG A CD  1 
ATOM   776  N  NE  . ARG A 1 100 ? 50.75363 54.15975 101.16402 1.000 46.38993  ? 99  ARG A NE  1 
ATOM   777  C  CZ  . ARG A 1 100 ? 51.79133 54.24356 100.34129 1.000 44.87317  ? 99  ARG A CZ  1 
ATOM   778  N  NH1 . ARG A 1 100 ? 52.84534 54.98965 100.63117 1.000 41.10205  ? 99  ARG A NH1 1 
ATOM   779  N  NH2 . ARG A 1 100 ? 51.77039 53.56205 99.19805  1.000 25.67355  ? 99  ARG A NH2 1 
ATOM   780  N  N   . ASP A 1 101 ? 50.78800 50.24901 104.39994 1.000 19.83557  ? 100 ASP A N   1 
ATOM   781  C  CA  . ASP A 1 101 ? 49.53488 49.52231 104.54835 1.000 18.68582  ? 100 ASP A CA  1 
ATOM   782  C  C   . ASP A 1 101 ? 49.56600 48.47926 105.65465 1.000 22.19559  ? 100 ASP A C   1 
ATOM   783  O  O   . ASP A 1 101 ? 48.51665 48.17930 106.23561 1.000 23.73667  ? 100 ASP A O   1 
ATOM   784  C  CB  . ASP A 1 101 ? 49.13498 48.88032 103.21747 1.000 17.40877  ? 100 ASP A CB  1 
ATOM   785  C  CG  . ASP A 1 101 ? 48.76563 49.90938 102.16661 1.000 18.23446  ? 100 ASP A CG  1 
ATOM   786  O  OD1 . ASP A 1 101 ? 48.34684 51.02999 102.54315 1.000 18.29739  ? 100 ASP A OD1 1 
ATOM   787  O  OD2 . ASP A 1 101 ? 48.87977 49.60746 100.96180 1.000 17.61189  ? 100 ASP A OD2 1 
ATOM   788  N  N   . PHE A 1 102 ? 50.73866 47.94040 105.98765 1.000 18.77142  ? 101 PHE A N   1 
ATOM   789  C  CA  . PHE A 1 102 ? 50.83289 46.88735 106.98728 1.000 20.00102  ? 101 PHE A CA  1 
ATOM   790  C  C   . PHE A 1 102 ? 51.69008 47.24468 108.19307 1.000 17.10969  ? 101 PHE A C   1 
ATOM   791  O  O   . PHE A 1 102 ? 51.78267 46.43416 109.12360 1.000 26.01221  ? 101 PHE A O   1 
ATOM   792  C  CB  . PHE A 1 102 ? 51.33289 45.58238 106.34976 1.000 20.81064  ? 101 PHE A CB  1 
ATOM   793  C  CG  . PHE A 1 102 ? 50.47048 45.10135 105.21997 1.000 18.99380  ? 101 PHE A CG  1 
ATOM   794  C  CD1 . PHE A 1 102 ? 49.24130 44.51206 105.47366 1.000 18.46410  ? 101 PHE A CD1 1 
ATOM   795  C  CD2 . PHE A 1 102 ? 50.87606 45.25462 103.90489 1.000 16.36542  ? 101 PHE A CD2 1 
ATOM   796  C  CE1 . PHE A 1 102 ? 48.43657 44.07544 104.43633 1.000 18.46799  ? 101 PHE A CE1 1 
ATOM   797  C  CE2 . PHE A 1 102 ? 50.07626 44.82187 102.86112 1.000 18.34688  ? 101 PHE A CE2 1 
ATOM   798  C  CZ  . PHE A 1 102 ? 48.85278 44.22854 103.12955 1.000 20.89226  ? 101 PHE A CZ  1 
ATOM   799  N  N   . GLY A 1 103 ? 52.32052 48.41460 108.20668 1.000 20.67890  ? 102 GLY A N   1 
ATOM   800  C  CA  . GLY A 1 103 ? 53.13302 48.80934 109.34047 1.000 19.10970  ? 102 GLY A CA  1 
ATOM   801  C  C   . GLY A 1 103 ? 54.61427 48.60023 109.10477 1.000 24.18779  ? 102 GLY A C   1 
ATOM   802  O  O   . GLY A 1 103 ? 55.42691 49.49922 109.35111 1.000 27.56157  ? 102 GLY A O   1 
ATOM   803  N  N   . SER A 1 104 ? 54.97781 47.40965 108.63428 1.000 20.63682  ? 103 SER A N   1 
ATOM   804  C  CA  . SER A 1 104 ? 56.36664 47.08669 108.34597 1.000 21.00557  ? 103 SER A CA  1 
ATOM   805  C  C   . SER A 1 104 ? 56.38708 45.86180 107.44610 1.000 20.33902  ? 103 SER A C   1 
ATOM   806  O  O   . SER A 1 104 ? 55.38996 45.14526 107.31544 1.000 18.73297  ? 103 SER A O   1 
ATOM   807  C  CB  . SER A 1 104 ? 57.14740 46.80626 109.63074 1.000 25.04127  ? 103 SER A CB  1 
ATOM   808  O  OG  . SER A 1 104 ? 56.70614 45.60265 110.23599 1.000 20.16347  ? 103 SER A OG  1 
ATOM   809  N  N   . PHE A 1 105 ? 57.55167 45.61103 106.84400 1.000 20.31685  ? 104 PHE A N   1 
ATOM   810  C  CA  . PHE A 1 105 ? 57.69301 44.40990 106.03232 1.000 17.42203  ? 104 PHE A CA  1 
ATOM   811  C  C   . PHE A 1 105 ? 57.48789 43.15783 106.87470 1.000 21.50677  ? 104 PHE A C   1 
ATOM   812  O  O   . PHE A 1 105 ? 56.81656 42.21317 106.44164 1.000 19.13656  ? 104 PHE A O   1 
ATOM   813  C  CB  . PHE A 1 105 ? 59.05872 44.39260 105.34509 1.000 17.23417  ? 104 PHE A CB  1 
ATOM   814  C  CG  . PHE A 1 105 ? 59.29558 43.16966 104.51397 1.000 18.37299  ? 104 PHE A CG  1 
ATOM   815  C  CD1 . PHE A 1 105 ? 58.68176 43.02399 103.28217 1.000 22.00527  ? 104 PHE A CD1 1 
ATOM   816  C  CD2 . PHE A 1 105 ? 60.12316 42.15945 104.96715 1.000 20.92283  ? 104 PHE A CD2 1 
ATOM   817  C  CE1 . PHE A 1 105 ? 58.89303 41.89037 102.51920 1.000 19.47541  ? 104 PHE A CE1 1 
ATOM   818  C  CE2 . PHE A 1 105 ? 60.34448 41.02924 104.20170 1.000 27.74504  ? 104 PHE A CE2 1 
ATOM   819  C  CZ  . PHE A 1 105 ? 59.72814 40.89534 102.97898 1.000 22.58874  ? 104 PHE A CZ  1 
ATOM   820  N  N   . ASP A 1 106 ? 58.03308 43.14192 108.09562 1.000 18.22516  ? 105 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 106 ? 57.86819 41.97731 108.96262 1.000 19.89231  ? 105 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 106 ? 56.40729 41.76015 109.33588 1.000 21.39934  ? 105 ASP A C   1 
ATOM   823  O  O   . ASP A 1 106 ? 55.93919 40.61780 109.39622 1.000 19.08193  ? 105 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 106 ? 58.73156 42.10198 110.21960 1.000 20.84227  ? 105 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 106 ? 60.17387 41.70381 109.98290 1.000 38.98964  ? 105 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 106 ? 60.51944 41.34541 108.83717 1.000 34.17040  ? 105 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 106 ? 60.95924 41.73287 110.95401 1.000 51.85495  ? 105 ASP A OD2 1 
ATOM   828  N  N   . LYS A 1 107 ? 55.67105 42.84229 109.59835 1.000 17.71430  ? 106 LYS A N   1 
ATOM   829  C  CA  . LYS A 1 107 ? 54.25090 42.69397 109.90593 1.000 19.69300  ? 106 LYS A CA  1 
ATOM   830  C  C   . LYS A 1 107 ? 53.47872 42.18303 108.69916 1.000 20.53257  ? 106 LYS A C   1 
ATOM   831  O  O   . LYS A 1 107 ? 52.56737 41.35906 108.84426 1.000 21.06238  ? 106 LYS A O   1 
ATOM   832  C  CB  . LYS A 1 107 ? 53.65939 44.01844 110.38160 1.000 20.83910  ? 106 LYS A CB  1 
ATOM   833  C  CG  . LYS A 1 107 ? 54.08267 44.43853 111.77890 1.000 18.58363  ? 106 LYS A CG  1 
ATOM   834  C  CD  . LYS A 1 107 ? 53.43510 45.76513 112.14598 1.000 24.04421  ? 106 LYS A CD  1 
ATOM   835  C  CE  . LYS A 1 107 ? 53.69680 46.13542 113.59530 1.000 27.24642  ? 106 LYS A CE  1 
ATOM   836  N  NZ  . LYS A 1 107 ? 53.16342 47.49286 113.90642 1.000 26.27447  ? 106 LYS A NZ  1 
ATOM   837  N  N   . PHE A 1 108 ? 53.83361 42.65419 107.50159 1.000 19.03711  ? 107 PHE A N   1 
ATOM   838  C  CA  . PHE A 1 108 ? 53.22568 42.11901 106.28682 1.000 19.24950  ? 107 PHE A CA  1 
ATOM   839  C  C   . PHE A 1 108 ? 53.48497 40.62279 106.15043 1.000 23.25145  ? 107 PHE A C   1 
ATOM   840  O  O   . PHE A 1 108 ? 52.56625 39.85066 105.84927 1.000 17.24033  ? 107 PHE A O   1 
ATOM   841  C  CB  . PHE A 1 108 ? 53.75198 42.86218 105.05968 1.000 17.44667  ? 107 PHE A CB  1 
ATOM   842  C  CG  . PHE A 1 108 ? 53.77184 42.02014 103.81856 1.000 17.03630  ? 107 PHE A CG  1 
ATOM   843  C  CD1 . PHE A 1 108 ? 52.59766 41.74028 103.13492 1.000 19.24052  ? 107 PHE A CD1 1 
ATOM   844  C  CD2 . PHE A 1 108 ? 54.96283 41.49584 103.34333 1.000 19.13053  ? 107 PHE A CD2 1 
ATOM   845  C  CE1 . PHE A 1 108 ? 52.61613 40.95350 101.99814 1.000 19.75497  ? 107 PHE A CE1 1 
ATOM   846  C  CE2 . PHE A 1 108 ? 54.98435 40.70727 102.20893 1.000 20.33881  ? 107 PHE A CE2 1 
ATOM   847  C  CZ  . PHE A 1 108 ? 53.80909 40.43680 101.53485 1.000 22.36078  ? 107 PHE A CZ  1 
ATOM   848  N  N   . LYS A 1 109 ? 54.73827 40.19507 106.35567 1.000 18.19228  ? 108 LYS A N   1 
ATOM   849  C  CA  . LYS A 1 109 ? 55.05725 38.76981 106.28310 1.000 17.33993  ? 108 LYS A CA  1 
ATOM   850  C  C   . LYS A 1 109 ? 54.20012 37.96736 107.24721 1.000 18.16140  ? 108 LYS A C   1 
ATOM   851  O  O   . LYS A 1 109 ? 53.68573 36.89910 106.89313 1.000 18.90500  ? 108 LYS A O   1 
ATOM   852  C  CB  . LYS A 1 109 ? 56.53496 38.53054 106.60141 1.000 18.32442  ? 108 LYS A CB  1 
ATOM   853  C  CG  . LYS A 1 109 ? 57.47871 38.71362 105.43094 1.000 23.69857  ? 108 LYS A CG  1 
ATOM   854  C  CD  . LYS A 1 109 ? 58.92036 38.44775 105.85102 1.000 27.29560  ? 108 LYS A CD  1 
ATOM   855  C  CE  . LYS A 1 109 ? 59.09888 37.06400 106.44631 1.000 34.68193  ? 108 LYS A CE  1 
ATOM   856  N  NZ  . LYS A 1 109 ? 60.52738 36.81492 106.80189 1.000 39.65136  ? 108 LYS A NZ  1 
ATOM   857  N  N   . GLU A 1 110 ? 54.04679 38.46097 108.47720 1.000 19.53118  ? 109 GLU A N   1 
ATOM   858  C  CA  . GLU A 1 110 ? 53.20773 37.77914 109.45583 1.000 22.43633  ? 109 GLU A CA  1 
ATOM   859  C  C   . GLU A 1 110 ? 51.76240 37.69723 108.98000 1.000 21.30075  ? 109 GLU A C   1 
ATOM   860  O  O   . GLU A 1 110 ? 51.11345 36.65333 109.12467 1.000 19.80370  ? 109 GLU A O   1 
ATOM   861  C  CB  . GLU A 1 110 ? 53.30342 38.49238 110.80617 1.000 26.16408  ? 109 GLU A CB  1 
ATOM   862  C  CG  . GLU A 1 110 ? 52.64164 37.75979 111.96181 1.000 30.08486  ? 109 GLU A CG  1 
ATOM   863  C  CD  . GLU A 1 110 ? 51.16303 38.06584 112.08450 1.000 45.75220  ? 109 GLU A CD  1 
ATOM   864  O  OE1 . GLU A 1 110 ? 50.73336 39.13309 111.59602 1.000 58.66592  ? 109 GLU A OE1 1 
ATOM   865  O  OE2 . GLU A 1 110 ? 50.43041 37.23652 112.66536 1.000 54.70212  ? 109 GLU A OE2 1 
ATOM   866  N  N   . LYS A 1 111 ? 51.24399 38.78183 108.39512 1.000 17.99199  ? 110 LYS A N   1 
ATOM   867  C  CA  . LYS A 1 111 ? 49.85059 38.77931 107.95355 1.000 17.76231  ? 110 LYS A CA  1 
ATOM   868  C  C   . LYS A 1 111 ? 49.63745 37.82086 106.78803 1.000 18.82133  ? 110 LYS A C   1 
ATOM   869  O  O   . LYS A 1 111 ? 48.64286 37.08737 106.75849 1.000 17.62093  ? 110 LYS A O   1 
ATOM   870  C  CB  . LYS A 1 111 ? 49.39754 40.19475 107.58956 1.000 18.39569  ? 110 LYS A CB  1 
ATOM   871  C  CG  . LYS A 1 111 ? 49.30371 41.14854 108.76627 1.000 22.42710  ? 110 LYS A CG  1 
ATOM   872  C  CD  . LYS A 1 111 ? 48.16516 40.75795 109.69622 1.000 29.66754  ? 110 LYS A CD  1 
ATOM   873  C  CE  . LYS A 1 111 ? 48.04212 41.73007 110.85968 1.000 34.85929  ? 110 LYS A CE  1 
ATOM   874  N  NZ  . LYS A 1 111 ? 47.16906 41.19099 111.93718 1.000 47.58216  ? 110 LYS A NZ  1 
ATOM   875  N  N   . LEU A 1 112 ? 50.55626 37.80554 105.81986 1.000 16.56777  ? 111 LEU A N   1 
ATOM   876  C  CA  . LEU A 1 112 ? 50.38944 36.88968 104.69678 1.000 17.54381  ? 111 LEU A CA  1 
ATOM   877  C  C   . LEU A 1 112 ? 50.62925 35.44987 105.12881 1.000 17.48831  ? 111 LEU A C   1 
ATOM   878  O  O   . LEU A 1 112 ? 49.93581 34.53747 104.66386 1.000 17.48860  ? 111 LEU A O   1 
ATOM   879  C  CB  . LEU A 1 112 ? 51.30062 37.27556 103.53219 1.000 15.25340  ? 111 LEU A CB  1 
ATOM   880  C  CG  . LEU A 1 112 ? 51.15921 36.40294 102.27661 1.000 14.51866  ? 111 LEU A CG  1 
ATOM   881  C  CD1 . LEU A 1 112 ? 49.71093 36.31745 101.79207 1.000 15.77756  ? 111 LEU A CD1 1 
ATOM   882  C  CD2 . LEU A 1 112 ? 52.07016 36.88372 101.15571 1.000 17.32968  ? 111 LEU A CD2 1 
ATOM   883  N  N   . THR A 1 113 ? 51.59060 35.22657 106.03428 1.000 15.08322  ? 112 THR A N   1 
ATOM   884  C  CA  . THR A 1 113 ? 51.77095 33.88910 106.59145 1.000 17.32710  ? 112 THR A CA  1 
ATOM   885  C  C   . THR A 1 113 ? 50.51525 33.42075 107.31111 1.000 16.03329  ? 112 THR A C   1 
ATOM   886  O  O   . THR A 1 113 ? 50.08879 32.27249 107.14577 1.000 17.32154  ? 112 THR A O   1 
ATOM   887  C  CB  . THR A 1 113 ? 52.96200 33.84952 107.54868 1.000 20.12218  ? 112 THR A CB  1 
ATOM   888  O  OG1 . THR A 1 113 ? 54.16300 34.18856 106.84331 1.000 21.95909  ? 112 THR A OG1 1 
ATOM   889  C  CG2 . THR A 1 113 ? 53.10099 32.45070 108.14626 1.000 19.74496  ? 112 THR A CG2 1 
ATOM   890  N  N   . ALA A 1 114 ? 49.90596 34.30174 108.11098 1.000 19.07560  ? 113 ALA A N   1 
ATOM   891  C  CA  . ALA A 1 114 ? 48.71090 33.92389 108.85560 1.000 18.37010  ? 113 ALA A CA  1 
ATOM   892  C  C   . ALA A 1 114 ? 47.57594 33.55354 107.91367 1.000 17.27278  ? 113 ALA A C   1 
ATOM   893  O  O   . ALA A 1 114 ? 46.88367 32.55336 108.13166 1.000 18.86287  ? 113 ALA A O   1 
ATOM   894  C  CB  . ALA A 1 114 ? 48.29185 35.06461 109.78311 1.000 20.54498  ? 113 ALA A CB  1 
ATOM   895  N  N   . ALA A 1 115 ? 47.39310 34.32777 106.84045 1.000 16.61573  ? 114 ALA A N   1 
ATOM   896  C  CA  . ALA A 1 115 ? 46.35724 33.99834 105.86665 1.000 15.45094  ? 114 ALA A CA  1 
ATOM   897  C  C   . ALA A 1 115 ? 46.65976 32.67402 105.17974 1.000 16.10573  ? 114 ALA A C   1 
ATOM   898  O  O   . ALA A 1 115 ? 45.75018 31.88388 104.89881 1.000 16.85278  ? 114 ALA A O   1 
ATOM   899  C  CB  . ALA A 1 115 ? 46.24801 35.11943 104.83412 1.000 16.90718  ? 114 ALA A CB  1 
ATOM   900  N  N   . SER A 1 116 ? 47.93887 32.40841 104.91363 1.000 15.41977  ? 115 SER A N   1 
ATOM   901  C  CA  . SER A 1 116 ? 48.31230 31.17803 104.22621 1.000 15.03597  ? 115 SER A CA  1 
ATOM   902  C  C   . SER A 1 116 ? 48.18391 29.96705 105.14355 1.000 15.89310  ? 115 SER A C   1 
ATOM   903  O  O   . SER A 1 116 ? 47.62943 28.93485 104.74462 1.000 17.22344  ? 115 SER A O   1 
ATOM   904  C  CB  . SER A 1 116 ? 49.73347 31.30693 103.67949 1.000 16.39071  ? 115 SER A CB  1 
ATOM   905  O  OG  . SER A 1 116 ? 49.81878 32.38739 102.76342 1.000 17.17513  ? 115 SER A OG  1 
ATOM   906  N  N   . VAL A 1 117 ? 48.66710 30.08359 106.38344 1.000 16.48004  ? 116 VAL A N   1 
ATOM   907  C  CA  . VAL A 1 117 ? 48.52749 28.99778 107.34840 1.000 18.06090  ? 116 VAL A CA  1 
ATOM   908  C  C   . VAL A 1 117 ? 47.06083 28.76600 107.69715 1.000 18.62919  ? 116 VAL A C   1 
ATOM   909  O  O   . VAL A 1 117 ? 46.65970 27.63569 108.00761 1.000 20.46888  ? 116 VAL A O   1 
ATOM   910  C  CB  . VAL A 1 117 ? 49.39715 29.27546 108.59294 1.000 23.04927  ? 116 VAL A CB  1 
ATOM   911  C  CG1 . VAL A 1 117 ? 48.55447 29.30992 109.86038 1.000 33.69454  ? 116 VAL A CG1 1 
ATOM   912  C  CG2 . VAL A 1 117 ? 50.49331 28.23415 108.72407 1.000 36.06618  ? 116 VAL A CG2 1 
ATOM   913  N  N   . GLY A 1 118 ? 46.23369 29.81270 107.62149 1.000 17.31647  ? 117 GLY A N   1 
ATOM   914  C  CA  . GLY A 1 118 ? 44.84455 29.70373 108.02045 1.000 21.81897  ? 117 GLY A CA  1 
ATOM   915  C  C   . GLY A 1 118 ? 43.93166 29.02163 107.02883 1.000 20.56070  ? 117 GLY A C   1 
ATOM   916  O  O   . GLY A 1 118 ? 42.78022 28.74143 107.37444 1.000 19.96794  ? 117 GLY A O   1 
ATOM   917  N  N   . VAL A 1 119 ? 44.40537 28.73460 105.81631 1.000 15.77164  ? 118 VAL A N   1 
ATOM   918  C  CA  . VAL A 1 119 ? 43.57170 28.03121 104.84508 1.000 15.29890  ? 118 VAL A CA  1 
ATOM   919  C  C   . VAL A 1 119 ? 43.31069 26.61921 105.35344 1.000 14.77615  ? 118 VAL A C   1 
ATOM   920  O  O   . VAL A 1 119 ? 44.24719 25.83792 105.56786 1.000 15.90904  ? 118 VAL A O   1 
ATOM   921  C  CB  . VAL A 1 119 ? 44.22860 28.00784 103.45779 1.000 15.28713  ? 118 VAL A CB  1 
ATOM   922  C  CG1 . VAL A 1 119 ? 43.43192 27.11692 102.50282 1.000 14.37783  ? 118 VAL A CG1 1 
ATOM   923  C  CG2 . VAL A 1 119 ? 44.35538 29.41926 102.89174 1.000 17.04077  ? 118 VAL A CG2 1 
ATOM   924  N  N   . GLN A 1 120 ? 42.03738 26.28939 105.55584 1.000 15.43490  ? 119 GLN A N   1 
ATOM   925  C  CA  . GLN A 1 120 ? 41.62819 24.95807 105.97953 1.000 14.50639  ? 119 GLN A CA  1 
ATOM   926  C  C   . GLN A 1 120 ? 41.26309 24.18395 104.71901 1.000 14.22651  ? 119 GLN A C   1 
ATOM   927  O  O   . GLN A 1 120 ? 40.31151 24.54140 104.01231 1.000 16.94387  ? 119 GLN A O   1 
ATOM   928  C  CB  . GLN A 1 120 ? 40.45604 25.05186 106.95443 1.000 19.14299  ? 119 GLN A CB  1 
ATOM   929  C  CG  . GLN A 1 120 ? 40.83462 25.77901 108.24198 1.000 19.64256  ? 119 GLN A CG  1 
ATOM   930  C  CD  . GLN A 1 120 ? 39.66855 25.97493 109.18762 1.000 24.90374  ? 119 GLN A CD  1 
ATOM   931  O  OE1 . GLN A 1 120 ? 38.51594 26.03396 108.76624 1.000 24.54432  ? 119 GLN A OE1 1 
ATOM   932  N  NE2 . GLN A 1 120 ? 39.96835 26.10184 110.47434 1.000 28.60157  ? 119 GLN A NE2 1 
ATOM   933  N  N   . GLY A 1 121 ? 42.03608 23.14550 104.42631 1.000 15.37599  ? 120 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 121 ? 41.92864 22.47948 103.14629 1.000 15.14032  ? 120 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 121 ? 42.93279 23.03211 102.15675 1.000 13.29373  ? 120 GLY A C   1 
ATOM   936  O  O   . GLY A 1 121 ? 44.00884 23.50197 102.53741 1.000 14.07652  ? 120 GLY A O   1 
ATOM   937  N  N   . SER A 1 122 ? 42.58272 22.98232 100.88150 1.000 13.21735  ? 121 SER A N   1 
ATOM   938  C  CA  . SER A 1 122 ? 43.44535 23.46214 99.81517  1.000 13.66070  ? 121 SER A CA  1 
ATOM   939  C  C   . SER A 1 122 ? 43.15067 24.92681 99.51406  1.000 13.87708  ? 121 SER A C   1 
ATOM   940  O  O   . SER A 1 122 ? 42.01469 25.39001 99.64136  1.000 14.97017  ? 121 SER A O   1 
ATOM   941  C  CB  . SER A 1 122 ? 43.19208 22.63143 98.55934  1.000 12.07789  ? 121 SER A CB  1 
ATOM   942  O  OG  . SER A 1 122 ? 43.41529 21.24934 98.79677  1.000 14.42037  ? 121 SER A OG  1 
ATOM   943  N  N   . GLY A 1 123 ? 44.18167 25.66259 99.11142  1.000 12.65801  ? 122 GLY A N   1 
ATOM   944  C  CA  . GLY A 1 123 ? 43.96031 27.04491 98.73409  1.000 13.65412  ? 122 GLY A CA  1 
ATOM   945  C  C   . GLY A 1 123 ? 45.25756 27.81042 98.57630  1.000 11.64806  ? 122 GLY A C   1 
ATOM   946  O  O   . GLY A 1 123 ? 46.33589 27.22142 98.43162  1.000 12.05914  ? 122 GLY A O   1 
ATOM   947  N  N   . TRP A 1 124 ? 45.11997 29.14121 98.61986  1.000 12.88106  ? 123 TRP A N   1 
ATOM   948  C  CA  . TRP A 1 124 ? 46.18689 30.08990 98.32219  1.000 10.99987  ? 123 TRP A CA  1 
ATOM   949  C  C   . TRP A 1 124 ? 46.07273 31.29000 99.24754  1.000 12.96993  ? 123 TRP A C   1 
ATOM   950  O  O   . TRP A 1 124 ? 44.96557 31.73724 99.56064  1.000 13.49392  ? 123 TRP A O   1 
ATOM   951  C  CB  . TRP A 1 124 ? 46.03923 30.62199 96.88773  1.000 12.10013  ? 123 TRP A CB  1 
ATOM   952  C  CG  . TRP A 1 124 ? 46.34212 29.62341 95.82434  1.000 11.45678  ? 123 TRP A CG  1 
ATOM   953  C  CD1 . TRP A 1 124 ? 45.54518 28.59841 95.41526  1.000 13.60986  ? 123 TRP A CD1 1 
ATOM   954  C  CD2 . TRP A 1 124 ? 47.52793 29.55674 95.02362  1.000 12.24124  ? 123 TRP A CD2 1 
ATOM   955  N  NE1 . TRP A 1 124 ? 46.16183 27.89116 94.41411  1.000 14.19655  ? 123 TRP A NE1 1 
ATOM   956  C  CE2 . TRP A 1 124 ? 47.38319 28.45722 94.15735  1.000 13.61748  ? 123 TRP A CE2 1 
ATOM   957  C  CE3 . TRP A 1 124 ? 48.69912 30.31881 94.95877  1.000 12.67804  ? 123 TRP A CE3 1 
ATOM   958  C  CZ2 . TRP A 1 124 ? 48.36369 28.09688 93.23608  1.000 13.31689  ? 123 TRP A CZ2 1 
ATOM   959  C  CZ3 . TRP A 1 124 ? 49.67297 29.96072 94.04042  1.000 13.63099  ? 123 TRP A CZ3 1 
ATOM   960  C  CH2 . TRP A 1 124 ? 49.50046 28.85835 93.19273  1.000 15.04421  ? 123 TRP A CH2 1 
ATOM   961  N  N   . GLY A 1 125 ? 47.21578 31.83627 99.64991  1.000 11.71767  ? 124 GLY A N   1 
ATOM   962  C  CA  . GLY A 1 125 ? 47.26642 33.15136 100.27010 1.000 14.77159  ? 124 GLY A CA  1 
ATOM   963  C  C   . GLY A 1 125 ? 47.77804 34.15828 99.25414  1.000 14.02543  ? 124 GLY A C   1 
ATOM   964  O  O   . GLY A 1 125 ? 48.67648 33.85180 98.46929  1.000 13.81218  ? 124 GLY A O   1 
ATOM   965  N  N   . TRP A 1 126 ? 47.20667 35.36578 99.27801  1.000 13.73879  ? 125 TRP A N   1 
ATOM   966  C  CA  . TRP A 1 126 ? 47.52564 36.38396 98.28362  1.000 13.24214  ? 125 TRP A CA  1 
ATOM   967  C  C   . TRP A 1 126 ? 47.80154 37.73582 98.91532  1.000 11.39582  ? 125 TRP A C   1 
ATOM   968  O  O   . TRP A 1 126 ? 47.06859 38.18514 99.80402  1.000 13.43347  ? 125 TRP A O   1 
ATOM   969  C  CB  . TRP A 1 126 ? 46.38880 36.59541 97.26090  1.000 13.04873  ? 125 TRP A CB  1 
ATOM   970  C  CG  . TRP A 1 126 ? 46.26279 35.47487 96.30239  1.000 11.53473  ? 125 TRP A CG  1 
ATOM   971  C  CD1 . TRP A 1 126 ? 45.39043 34.42974 96.37898  1.000 13.69435  ? 125 TRP A CD1 1 
ATOM   972  C  CD2 . TRP A 1 126 ? 47.05629 35.25232 95.12882  1.000 12.17902  ? 125 TRP A CD2 1 
ATOM   973  N  NE1 . TRP A 1 126 ? 45.58793 33.57444 95.32586  1.000 13.63627  ? 125 TRP A NE1 1 
ATOM   974  C  CE2 . TRP A 1 126 ? 46.60427 34.05391 94.54298  1.000 13.18310  ? 125 TRP A CE2 1 
ATOM   975  C  CE3 . TRP A 1 126 ? 48.09791 35.95349 94.50964  1.000 14.82451  ? 125 TRP A CE3 1 
ATOM   976  C  CZ2 . TRP A 1 126 ? 47.16278 33.53541 93.37640  1.000 13.99680  ? 125 TRP A CZ2 1 
ATOM   977  C  CZ3 . TRP A 1 126 ? 48.65187 35.43171 93.34858  1.000 15.06729  ? 125 TRP A CZ3 1 
ATOM   978  C  CH2 . TRP A 1 126 ? 48.17588 34.24006 92.79271  1.000 14.78813  ? 125 TRP A CH2 1 
ATOM   979  N  N   . LEU A 1 127 ? 48.86016 38.37587 98.42886  1.000 13.95942  ? 126 LEU A N   1 
ATOM   980  C  CA  . LEU A 1 127 ? 48.97530 39.82429 98.46112  1.000 12.54225  ? 126 LEU A CA  1 
ATOM   981  C  C   . LEU A 1 127 ? 48.41857 40.34792 97.14324  1.000 12.86522  ? 126 LEU A C   1 
ATOM   982  O  O   . LEU A 1 127 ? 48.88694 39.95686 96.06683  1.000 13.77763  ? 126 LEU A O   1 
ATOM   983  C  CB  . LEU A 1 127 ? 50.43416 40.25304 98.61889  1.000 13.00243  ? 126 LEU A CB  1 
ATOM   984  C  CG  . LEU A 1 127 ? 50.63503 41.76583 98.48153  1.000 14.19631  ? 126 LEU A CG  1 
ATOM   985  C  CD1 . LEU A 1 127 ? 49.96587 42.50813 99.63961  1.000 13.36490  ? 126 LEU A CD1 1 
ATOM   986  C  CD2 . LEU A 1 127 ? 52.11121 42.12043 98.38787  1.000 13.18970  ? 126 LEU A CD2 1 
ATOM   987  N  N   . GLY A 1 128 ? 47.41637 41.22377 97.22428  1.000 13.66151  ? 127 GLY A N   1 
ATOM   988  C  CA  . GLY A 1 128 ? 46.80653 41.79191 96.04570  1.000 12.85401  ? 127 GLY A CA  1 
ATOM   989  C  C   . GLY A 1 128 ? 46.79882 43.30834 96.11243  1.000 15.11689  ? 127 GLY A C   1 
ATOM   990  O  O   . GLY A 1 128 ? 47.18294 43.91297 97.11542  1.000 16.00150  ? 127 GLY A O   1 
ATOM   991  N  N   . PHE A 1 129 ? 46.36608 43.91133 95.01307  1.000 14.34897  ? 128 PHE A N   1 
ATOM   992  C  CA  . PHE A 1 129 ? 46.17063 45.35082 94.93288  1.000 14.95508  ? 128 PHE A CA  1 
ATOM   993  C  C   . PHE A 1 129 ? 44.68901 45.62446 94.73311  1.000 16.92662  ? 128 PHE A C   1 
ATOM   994  O  O   . PHE A 1 129 ? 44.06651 45.05775 93.82817  1.000 15.73090  ? 128 PHE A O   1 
ATOM   995  C  CB  . PHE A 1 129 ? 46.97922 45.94827 93.78368  1.000 15.14158  ? 128 PHE A CB  1 
ATOM   996  C  CG  . PHE A 1 129 ? 46.95068 47.44691 93.74315  1.000 16.85673  ? 128 PHE A CG  1 
ATOM   997  C  CD1 . PHE A 1 129 ? 47.76778 48.19053 94.58257  1.000 17.04756  ? 128 PHE A CD1 1 
ATOM   998  C  CD2 . PHE A 1 129 ? 46.10478 48.11204 92.87103  1.000 18.88842  ? 128 PHE A CD2 1 
ATOM   999  C  CE1 . PHE A 1 129 ? 47.74377 49.57674 94.54708  1.000 17.45122  ? 128 PHE A CE1 1 
ATOM   1000 C  CE2 . PHE A 1 129 ? 46.08187 49.50005 92.83046  1.000 20.27131  ? 128 PHE A CE2 1 
ATOM   1001 C  CZ  . PHE A 1 129 ? 46.89904 50.22728 93.67191  1.000 19.20522  ? 128 PHE A CZ  1 
ATOM   1002 N  N   . ASN A 1 130 ? 44.12408 46.47175 95.59133  1.000 15.58065  ? 129 ASN A N   1 
ATOM   1003 C  CA  . ASN A 1 130 ? 42.73350 46.89761 95.47327  1.000 13.78664  ? 129 ASN A CA  1 
ATOM   1004 C  C   . ASN A 1 130 ? 42.71188 48.15383 94.61074  1.000 17.20837  ? 129 ASN A C   1 
ATOM   1005 O  O   . ASN A 1 130 ? 43.15518 49.22288 95.04787  1.000 18.34127  ? 129 ASN A O   1 
ATOM   1006 C  CB  . ASN A 1 130 ? 42.13262 47.14159 96.85689  1.000 15.35117  ? 129 ASN A CB  1 
ATOM   1007 C  CG  . ASN A 1 130 ? 40.62902 47.42596 96.80819  1.000 15.76602  ? 129 ASN A CG  1 
ATOM   1008 O  OD1 . ASN A 1 130 ? 40.15566 48.16405 95.94742  1.000 17.47186  ? 129 ASN A OD1 1 
ATOM   1009 N  ND2 . ASN A 1 130 ? 39.88006 46.84806 97.74241  1.000 15.34334  ? 129 ASN A ND2 1 
ATOM   1010 N  N   . LYS A 1 131 ? 42.22476 48.01658 93.37288  1.000 18.11468  ? 130 LYS A N   1 
ATOM   1011 C  CA  . LYS A 1 131 ? 42.24818 49.13351 92.43028  1.000 24.54622  ? 130 LYS A CA  1 
ATOM   1012 C  C   . LYS A 1 131 ? 41.36006 50.27934 92.89515  1.000 21.91333  ? 130 LYS A C   1 
ATOM   1013 O  O   . LYS A 1 131 ? 41.71900 51.45174 92.73902  1.000 23.62238  ? 130 LYS A O   1 
ATOM   1014 C  CB  . LYS A 1 131 ? 41.80865 48.66675 91.04209  1.000 26.78011  ? 130 LYS A CB  1 
ATOM   1015 C  CG  . LYS A 1 131 ? 42.84981 47.86862 90.27734  1.000 37.27703  ? 130 LYS A CG  1 
ATOM   1016 C  CD  . LYS A 1 131 ? 42.32574 47.47552 88.90094  1.000 56.84025  ? 130 LYS A CD  1 
ATOM   1017 C  CE  . LYS A 1 131 ? 43.46181 47.19852 87.92539  1.000 67.14024  ? 130 LYS A CE  1 
ATOM   1018 N  NZ  . LYS A 1 131 ? 42.96950 46.62853 86.63721  1.000 54.35610  ? 130 LYS A NZ  1 
ATOM   1019 N  N   . GLU A 1 132 ? 40.19292 49.96139 93.45426  1.000 19.13670  ? 131 GLU A N   1 
ATOM   1020 C  CA  . GLU A 1 132 ? 39.26229 51.00798 93.86149  1.000 21.08662  ? 131 GLU A CA  1 
ATOM   1021 C  C   . GLU A 1 132 ? 39.79428 51.79297 95.05258  1.000 21.81834  ? 131 GLU A C   1 
ATOM   1022 O  O   . GLU A 1 132 ? 39.71079 53.02843 95.07714  1.000 21.61290  ? 131 GLU A O   1 
ATOM   1023 C  CB  . GLU A 1 132 ? 37.89619 50.39759 94.17261  1.000 24.52271  ? 131 GLU A CB  1 
ATOM   1024 C  CG  . GLU A 1 132 ? 37.21905 49.73854 92.97540  1.000 48.31839  ? 131 GLU A CG  1 
ATOM   1025 C  CD  . GLU A 1 132 ? 37.62816 48.28621 92.77327  1.000 57.79224  ? 131 GLU A CD  1 
ATOM   1026 O  OE1 . GLU A 1 132 ? 38.78352 47.92910 93.09211  1.000 41.92338  ? 131 GLU A OE1 1 
ATOM   1027 O  OE2 . GLU A 1 132 ? 36.78812 47.49889 92.28807  1.000 72.60347  ? 131 GLU A OE2 1 
ATOM   1028 N  N   . ARG A 1 133 ? 40.35313 51.09575 96.04452  1.000 18.30555  ? 132 ARG A N   1 
ATOM   1029 C  CA  . ARG A 1 133 ? 40.91683 51.75497 97.21518  1.000 17.13929  ? 132 ARG A CA  1 
ATOM   1030 C  C   . ARG A 1 133 ? 42.33132 52.27076 96.98374  1.000 18.59197  ? 132 ARG A C   1 
ATOM   1031 O  O   . ARG A 1 133 ? 42.80196 53.11128 97.75854  1.000 19.81811  ? 132 ARG A O   1 
ATOM   1032 C  CB  . ARG A 1 133 ? 40.91860 50.79664 98.40780  1.000 16.25661  ? 132 ARG A CB  1 
ATOM   1033 C  CG  . ARG A 1 133 ? 39.54200 50.34405 98.85643  1.000 15.76140  ? 132 ARG A CG  1 
ATOM   1034 C  CD  . ARG A 1 133 ? 38.76290 51.47879 99.51304  1.000 17.41108  ? 132 ARG A CD  1 
ATOM   1035 N  NE  . ARG A 1 133 ? 39.40653 51.95563 100.73421 1.000 18.00635  ? 132 ARG A NE  1 
ATOM   1036 C  CZ  . ARG A 1 133 ? 39.13710 51.50274 101.95156 1.000 16.54117  ? 132 ARG A CZ  1 
ATOM   1037 N  NH1 . ARG A 1 133 ? 38.23286 50.55571 102.15231 1.000 16.33640  ? 132 ARG A NH1 1 
ATOM   1038 N  NH2 . ARG A 1 133 ? 39.77898 52.02253 102.99525 1.000 15.53381  ? 132 ARG A NH2 1 
ATOM   1039 N  N   . GLY A 1 134 ? 43.01398 51.79211 95.94827  1.000 17.66540  ? 133 GLY A N   1 
ATOM   1040 C  CA  . GLY A 1 134 ? 44.37626 52.21540 95.67536  1.000 17.42488  ? 133 GLY A CA  1 
ATOM   1041 C  C   . GLY A 1 134 ? 45.39116 51.80467 96.72152  1.000 16.94674  ? 133 GLY A C   1 
ATOM   1042 O  O   . GLY A 1 134 ? 46.31539 52.57562 97.01836  1.000 18.39110  ? 133 GLY A O   1 
ATOM   1043 N  N   . HIS A 1 135 ? 45.25604 50.60416 97.28414  1.000 15.68973  ? 134 HIS A N   1 
ATOM   1044 C  CA  . HIS A 1 135 ? 46.19616 50.15089 98.29684  1.000 15.85964  ? 134 HIS A CA  1 
ATOM   1045 C  C   . HIS A 1 135 ? 46.28589 48.63214 98.26709  1.000 14.74568  ? 134 HIS A C   1 
ATOM   1046 O  O   . HIS A 1 135 ? 45.49124 47.95202 97.61341  1.000 14.89734  ? 134 HIS A O   1 
ATOM   1047 C  CB  . HIS A 1 135 ? 45.86129 50.70039 99.69665  1.000 17.43476  ? 134 HIS A CB  1 
ATOM   1048 C  CG  . HIS A 1 135 ? 44.52324 50.28336 100.23089 1.000 17.38648  ? 134 HIS A CG  1 
ATOM   1049 N  ND1 . HIS A 1 135 ? 43.76074 51.10767 101.03215 1.000 18.33333  ? 134 HIS A ND1 1 
ATOM   1050 C  CD2 . HIS A 1 135 ? 43.82384 49.12960 100.10939 1.000 15.32312  ? 134 HIS A CD2 1 
ATOM   1051 C  CE1 . HIS A 1 135 ? 42.64559 50.48549 101.36897 1.000 18.13865  ? 134 HIS A CE1 1 
ATOM   1052 N  NE2 . HIS A 1 135 ? 42.66002 49.28153 100.82579 1.000 17.02185  ? 134 HIS A NE2 1 
ATOM   1053 N  N   . LEU A 1 136 ? 47.26157 48.11061 99.00259  1.000 16.01429  ? 135 LEU A N   1 
ATOM   1054 C  CA  . LEU A 1 136 ? 47.47847 46.67563 99.08509  1.000 14.34454  ? 135 LEU A CA  1 
ATOM   1055 C  C   . LEU A 1 136 ? 46.39895 46.02587 99.94394  1.000 14.01942  ? 135 LEU A C   1 
ATOM   1056 O  O   . LEU A 1 136 ? 45.72792 46.67699 100.75122 1.000 14.94590  ? 135 LEU A O   1 
ATOM   1057 C  CB  . LEU A 1 136 ? 48.85135 46.39496 99.69628  1.000 16.47649  ? 135 LEU A CB  1 
ATOM   1058 C  CG  . LEU A 1 136 ? 50.01969 46.99934 98.91931  1.000 16.48282  ? 135 LEU A CG  1 
ATOM   1059 C  CD1 . LEU A 1 136 ? 51.31213 46.83238 99.70183  1.000 17.08188  ? 135 LEU A CD1 1 
ATOM   1060 C  CD2 . LEU A 1 136 ? 50.12461 46.32665 97.56229  1.000 16.57443  ? 135 LEU A CD2 1 
ATOM   1061 N  N   . GLN A 1 137 ? 46.23093 44.71791 99.75565  1.000 13.87100  ? 136 GLN A N   1 
ATOM   1062 C  CA  . GLN A 1 137 ? 45.21543 43.97208 100.48673 1.000 14.12836  ? 136 GLN A CA  1 
ATOM   1063 C  C   . GLN A 1 137 ? 45.57171 42.49258 100.46574 1.000 15.34786  ? 136 GLN A C   1 
ATOM   1064 O  O   . GLN A 1 137 ? 45.94381 41.95420 99.42036  1.000 17.23075  ? 136 GLN A O   1 
ATOM   1065 C  CB  . GLN A 1 137 ? 43.82823 44.18026 99.87173  1.000 14.84938  ? 136 GLN A CB  1 
ATOM   1066 C  CG  . GLN A 1 137 ? 42.69724 43.57533 100.68046 1.000 14.68075  ? 136 GLN A CG  1 
ATOM   1067 C  CD  . GLN A 1 137 ? 41.34015 44.07973 100.24358 1.000 16.05380  ? 136 GLN A CD  1 
ATOM   1068 O  OE1 . GLN A 1 137 ? 41.22277 45.17089 99.68287  1.000 15.64969  ? 136 GLN A OE1 1 
ATOM   1069 N  NE2 . GLN A 1 137 ? 40.30865 43.28348 100.48782 1.000 15.97483  ? 136 GLN A NE2 1 
ATOM   1070 N  N   . ILE A 1 138 ? 45.45083 41.84356 101.62164 1.000 13.74632  ? 137 ILE A N   1 
ATOM   1071 C  CA  . ILE A 1 138 ? 45.68894 40.40787 101.74935 1.000 14.45019  ? 137 ILE A CA  1 
ATOM   1072 C  C   . ILE A 1 138 ? 44.35632 39.67309 101.72278 1.000 14.98696  ? 137 ILE A C   1 
ATOM   1073 O  O   . ILE A 1 138 ? 43.36878 40.12890 102.31116 1.000 16.32405  ? 137 ILE A O   1 
ATOM   1074 C  CB  . ILE A 1 138 ? 46.48734 40.08951 103.02878 1.000 13.71443  ? 137 ILE A CB  1 
ATOM   1075 C  CG1 . ILE A 1 138 ? 47.94437 40.54639 102.86130 1.000 17.80861  ? 137 ILE A CG1 1 
ATOM   1076 C  CG2 . ILE A 1 138 ? 46.42303 38.60047 103.35887 1.000 15.18664  ? 137 ILE A CG2 1 
ATOM   1077 C  CD1 . ILE A 1 138 ? 48.76147 40.47766 104.12879 1.000 17.38013  ? 137 ILE A CD1 1 
ATOM   1078 N  N   . ALA A 1 139 ? 44.32128 38.54556 101.01216 1.000 14.62170  ? 138 ALA A N   1 
ATOM   1079 C  CA  . ALA A 1 139 ? 43.14054 37.69873 100.96617 1.000 11.80555  ? 138 ALA A CA  1 
ATOM   1080 C  C   . ALA A 1 139 ? 43.57505 36.25135 100.79315 1.000 14.06279  ? 138 ALA A C   1 
ATOM   1081 O  O   . ALA A 1 139 ? 44.66988 35.96360 100.30819 1.000 16.98778  ? 138 ALA A O   1 
ATOM   1082 C  CB  . ALA A 1 139 ? 42.20012 38.09727 99.82371  1.000 14.75867  ? 138 ALA A CB  1 
ATOM   1083 N  N   . ALA A 1 140 ? 42.69260 35.33840 101.18651 1.000 13.44008  ? 139 ALA A N   1 
ATOM   1084 C  CA  . ALA A 1 140 ? 42.88661 33.91341 100.97601 1.000 12.58239  ? 139 ALA A CA  1 
ATOM   1085 C  C   . ALA A 1 140 ? 41.79863 33.39301 100.04745 1.000 14.72073  ? 139 ALA A C   1 
ATOM   1086 O  O   . ALA A 1 140 ? 40.65950 33.87692 100.06369 1.000 15.37759  ? 139 ALA A O   1 
ATOM   1087 C  CB  . ALA A 1 140 ? 42.83922 33.14239 102.30247 1.000 16.04055  ? 139 ALA A CB  1 
ATOM   1088 N  N   . CYS A 1 141 ? 42.15378 32.39309 99.24145  1.000 12.97763  ? 140 CYS A N   1 
ATOM   1089 C  CA  . CYS A 1 141 ? 41.22360 31.82130 98.28310  1.000 12.09839  ? 140 CYS A CA  1 
ATOM   1090 C  C   . CYS A 1 141 ? 41.20474 30.30609 98.42144  1.000 12.50320  ? 140 CYS A C   1 
ATOM   1091 O  O   . CYS A 1 141 ? 42.25546 29.67855 98.57955  1.000 12.55440  ? 140 CYS A O   1 
ATOM   1092 C  CB  . CYS A 1 141 ? 41.62151 32.18177 96.84474  1.000 13.03116  ? 140 CYS A CB  1 
ATOM   1093 S  SG  . CYS A 1 141 ? 41.67215 33.94683 96.46540  1.000 15.11057  ? 140 CYS A SG  1 
ATOM   1094 N  N   . PRO A 1 142 ? 40.02865 29.69387 98.35487  1.000 11.65533  ? 141 PRO A N   1 
ATOM   1095 C  CA  . PRO A 1 142 ? 39.94577 28.23647 98.47704  1.000 13.16751  ? 141 PRO A CA  1 
ATOM   1096 C  C   . PRO A 1 142 ? 40.23486 27.55122 97.15076  1.000 13.55274  ? 141 PRO A C   1 
ATOM   1097 O  O   . PRO A 1 142 ? 39.95434 28.08434 96.07505  1.000 13.25991  ? 141 PRO A O   1 
ATOM   1098 C  CB  . PRO A 1 142 ? 38.48207 28.01739 98.88353  1.000 12.77642  ? 141 PRO A CB  1 
ATOM   1099 C  CG  . PRO A 1 142 ? 37.75302 29.14102 98.18510  1.000 12.53134  ? 141 PRO A CG  1 
ATOM   1100 C  CD  . PRO A 1 142 ? 38.69808 30.32251 98.24348  1.000 11.80759  ? 141 PRO A CD  1 
ATOM   1101 N  N   . ASN A 1 143 ? 40.79632 26.33971 97.24632  1.000 12.04573  ? 142 ASN A N   1 
ATOM   1102 C  CA  . ASN A 1 143 ? 40.98433 25.44502 96.09563  1.000 12.23683  ? 142 ASN A CA  1 
ATOM   1103 C  C   . ASN A 1 143 ? 41.80048 26.15652 95.02392  1.000 11.83879  ? 142 ASN A C   1 
ATOM   1104 O  O   . ASN A 1 143 ? 42.92532 26.59656 95.32231  1.000 12.30353  ? 142 ASN A O   1 
ATOM   1105 C  CB  . ASN A 1 143 ? 39.61379 24.90959 95.68095  1.000 13.15134  ? 142 ASN A CB  1 
ATOM   1106 C  CG  . ASN A 1 143 ? 38.96108 24.13448 96.78163  1.000 15.06539  ? 142 ASN A CG  1 
ATOM   1107 O  OD1 . ASN A 1 143 ? 39.62746 23.36175 97.47478  1.000 14.18883  ? 142 ASN A OD1 1 
ATOM   1108 N  ND2 . ASN A 1 143 ? 37.66063 24.34768 96.97832  1.000 14.97156  ? 142 ASN A ND2 1 
ATOM   1109 N  N   . GLN A 1 144 ? 41.31376 26.27989 93.78779  1.000 12.86828  ? 143 GLN A N   1 
ATOM   1110 C  CA  . GLN A 1 144 ? 41.99009 27.05994 92.76119  1.000 13.14427  ? 143 GLN A CA  1 
ATOM   1111 C  C   . GLN A 1 144 ? 41.25032 28.34539 92.42307  1.000 13.08382  ? 143 GLN A C   1 
ATOM   1112 O  O   . GLN A 1 144 ? 41.53876 28.96123 91.39133  1.000 12.98453  ? 143 GLN A O   1 
ATOM   1113 C  CB  . GLN A 1 144 ? 42.22671 26.24899 91.48788  1.000 13.60041  ? 143 GLN A CB  1 
ATOM   1114 C  CG  . GLN A 1 144 ? 43.13325 25.03860 91.65893  1.000 10.61589  ? 143 GLN A CG  1 
ATOM   1115 C  CD  . GLN A 1 144 ? 44.55223 25.39712 92.09739  1.000 12.71052  ? 143 GLN A CD  1 
ATOM   1116 O  OE1 . GLN A 1 144 ? 44.97815 26.54923 92.00699  1.000 12.82405  ? 143 GLN A OE1 1 
ATOM   1117 N  NE2 . GLN A 1 144 ? 45.28470 24.40500 92.58582  1.000 16.00989  ? 143 GLN A NE2 1 
ATOM   1118 N  N   . ASP A 1 145 ? 40.30782 28.76210 93.26209  1.000 10.81574  ? 144 ASP A N   1 
ATOM   1119 C  CA  . ASP A 1 145 ? 39.58641 29.99795 93.00855  1.000 13.14157  ? 144 ASP A CA  1 
ATOM   1120 C  C   . ASP A 1 145 ? 40.59630 31.12839 92.83513  1.000 11.30864  ? 144 ASP A C   1 
ATOM   1121 O  O   . ASP A 1 145 ? 41.38902 31.38423 93.75482  1.000 13.16071  ? 144 ASP A O   1 
ATOM   1122 C  CB  . ASP A 1 145 ? 38.64924 30.32389 94.16724  1.000 13.06877  ? 144 ASP A CB  1 
ATOM   1123 C  CG  . ASP A 1 145 ? 37.43358 29.42340 94.21253  1.000 12.58861  ? 144 ASP A CG  1 
ATOM   1124 O  OD1 . ASP A 1 145 ? 37.48529 28.30536 93.66047  1.000 15.02422  ? 144 ASP A OD1 1 
ATOM   1125 O  OD2 . ASP A 1 145 ? 36.42450 29.84316 94.81364  1.000 17.68705  ? 144 ASP A OD2 1 
ATOM   1126 N  N   . PRO A 1 146 ? 40.64884 31.77553 91.67336  1.000 11.30050  ? 145 PRO A N   1 
ATOM   1127 C  CA  . PRO A 1 146 ? 41.69210 32.77910 91.44019  1.000 11.86331  ? 145 PRO A CA  1 
ATOM   1128 C  C   . PRO A 1 146 ? 41.31863 34.12174 92.04903  1.000 11.04690  ? 145 PRO A C   1 
ATOM   1129 O  O   . PRO A 1 146 ? 40.14329 34.45250 92.21656  1.000 12.96976  ? 145 PRO A O   1 
ATOM   1130 C  CB  . PRO A 1 146 ? 41.75660 32.86216 89.91234  1.000 13.31517  ? 145 PRO A CB  1 
ATOM   1131 C  CG  . PRO A 1 146 ? 40.34979 32.55688 89.48508  1.000 14.29874  ? 145 PRO A CG  1 
ATOM   1132 C  CD  . PRO A 1 146 ? 39.83129 31.53411 90.47014  1.000 11.88923  ? 145 PRO A CD  1 
ATOM   1133 N  N   . LEU A 1 147 ? 42.34571 34.90415 92.37875  1.000 11.80454  ? 146 LEU A N   1 
ATOM   1134 C  CA  . LEU A 1 147 ? 42.12653 36.12438 93.15032  1.000 11.45490  ? 146 LEU A CA  1 
ATOM   1135 C  C   . LEU A 1 147 ? 41.28272 37.14266 92.38634  1.000 14.57646  ? 146 LEU A C   1 
ATOM   1136 O  O   . LEU A 1 147 ? 40.25782 37.60986 92.88631  1.000 13.46140  ? 146 LEU A O   1 
ATOM   1137 C  CB  . LEU A 1 147 ? 43.46784 36.72901 93.56728  1.000 12.88052  ? 146 LEU A CB  1 
ATOM   1138 C  CG  . LEU A 1 147 ? 43.35442 37.94185 94.49399  1.000 11.22823  ? 146 LEU A CG  1 
ATOM   1139 C  CD1 . LEU A 1 147 ? 42.82673 37.50986 95.85939  1.000 13.61396  ? 146 LEU A CD1 1 
ATOM   1140 C  CD2 . LEU A 1 147 ? 44.68362 38.65859 94.62121  1.000 14.19780  ? 146 LEU A CD2 1 
ATOM   1141 N  N   . GLN A 1 148 ? 41.71149 37.52101 91.18020  1.000 12.86529  ? 147 GLN A N   1 
ATOM   1142 C  CA  . GLN A 1 148 ? 41.02227 38.60194 90.47749  1.000 12.75030  ? 147 GLN A CA  1 
ATOM   1143 C  C   . GLN A 1 148 ? 39.62615 38.17704 90.04111  1.000 15.22721  ? 147 GLN A C   1 
ATOM   1144 O  O   . GLN A 1 148 ? 38.66424 38.93976 90.18362  1.000 14.54687  ? 147 GLN A O   1 
ATOM   1145 C  CB  . GLN A 1 148 ? 41.85851 39.07691 89.28927  1.000 15.56799  ? 147 GLN A CB  1 
ATOM   1146 C  CG  . GLN A 1 148 ? 41.33939 40.34767 88.62805  1.000 15.54928  ? 147 GLN A CG  1 
ATOM   1147 C  CD  . GLN A 1 148 ? 42.15283 40.73560 87.40500  1.000 23.01882  ? 147 GLN A CD  1 
ATOM   1148 O  OE1 . GLN A 1 148 ? 43.22681 40.18452 87.15872  1.000 24.24468  ? 147 GLN A OE1 1 
ATOM   1149 N  NE2 . GLN A 1 148 ? 41.63212 41.66684 86.61913  1.000 21.27773  ? 147 GLN A NE2 1 
ATOM   1150 N  N   . GLY A 1 149 ? 39.48969 36.95127 89.54168  1.000 13.16699  ? 148 GLY A N   1 
ATOM   1151 C  CA  . GLY A 1 149 ? 38.19446 36.50017 89.06534  1.000 12.51154  ? 148 GLY A CA  1 
ATOM   1152 C  C   . GLY A 1 149 ? 37.14519 36.39561 90.15460  1.000 15.82069  ? 148 GLY A C   1 
ATOM   1153 O  O   . GLY A 1 149 ? 35.95282 36.55272 89.88260  1.000 17.10437  ? 148 GLY A O   1 
ATOM   1154 N  N   . THR A 1 150 ? 37.55796 36.13928 91.39888  1.000 14.49593  ? 149 THR A N   1 
ATOM   1155 C  CA  . THR A 1 150 ? 36.59118 35.96312 92.47773  1.000 14.54930  ? 149 THR A CA  1 
ATOM   1156 C  C   . THR A 1 150 ? 36.50859 37.12622 93.46105  1.000 15.52933  ? 149 THR A C   1 
ATOM   1157 O  O   . THR A 1 150 ? 35.53716 37.19112 94.22132  1.000 20.31161  ? 149 THR A O   1 
ATOM   1158 C  CB  . THR A 1 150 ? 36.83483 34.65744 93.25243  1.000 15.84313  ? 149 THR A CB  1 
ATOM   1159 O  OG1 . THR A 1 150 ? 38.10552 34.71457 93.91308  1.000 15.75746  ? 149 THR A OG1 1 
ATOM   1160 C  CG2 . THR A 1 150 ? 36.81845 33.45740 92.31708  1.000 16.95340  ? 149 THR A CG2 1 
ATOM   1161 N  N   . THR A 1 151 ? 37.49955 38.02742 93.48737  1.000 15.80688  ? 150 THR A N   1 
ATOM   1162 C  CA  . THR A 1 151 ? 37.50495 39.16320 94.41280  1.000 17.55998  ? 150 THR A CA  1 
ATOM   1163 C  C   . THR A 1 151 ? 37.72541 40.51527 93.75244  1.000 15.71167  ? 150 THR A C   1 
ATOM   1164 O  O   . THR A 1 151 ? 37.50484 41.54126 94.41068  1.000 16.64217  ? 150 THR A O   1 
ATOM   1165 C  CB  . THR A 1 151 ? 38.59462 39.00513 95.48985  1.000 18.82131  ? 150 THR A CB  1 
ATOM   1166 O  OG1 . THR A 1 151 ? 39.88154 39.27941 94.91363  1.000 16.06940  ? 150 THR A OG1 1 
ATOM   1167 C  CG2 . THR A 1 151 ? 38.58839 37.60726 96.08407  1.000 18.90929  ? 150 THR A CG2 1 
ATOM   1168 N  N   . GLY A 1 152 ? 38.17155 40.55919 92.49947  1.000 14.23922  ? 151 GLY A N   1 
ATOM   1169 C  CA  . GLY A 1 152 ? 38.53462 41.80565 91.86409  1.000 17.18086  ? 151 GLY A CA  1 
ATOM   1170 C  C   . GLY A 1 152 ? 39.90487 42.34517 92.22091  1.000 14.73883  ? 151 GLY A C   1 
ATOM   1171 O  O   . GLY A 1 152 ? 40.37996 43.26647 91.54594  1.000 17.15578  ? 151 GLY A O   1 
ATOM   1172 N  N   . LEU A 1 153 ? 40.55763 41.81144 93.25314  1.000 14.67316  ? 152 LEU A N   1 
ATOM   1173 C  CA  . LEU A 1 153 ? 41.89773 42.25880 93.60545  1.000 13.09478  ? 152 LEU A CA  1 
ATOM   1174 C  C   . LEU A 1 153 ? 42.89628 41.77225 92.55975  1.000 13.41110  ? 152 LEU A C   1 
ATOM   1175 O  O   . LEU A 1 153 ? 42.78606 40.65557 92.04686  1.000 14.78816  ? 152 LEU A O   1 
ATOM   1176 C  CB  . LEU A 1 153 ? 42.28749 41.70181 94.97584  1.000 15.68172  ? 152 LEU A CB  1 
ATOM   1177 C  CG  . LEU A 1 153 ? 41.41847 42.07505 96.17707  1.000 16.46586  ? 152 LEU A CG  1 
ATOM   1178 C  CD1 . LEU A 1 153 ? 41.89599 41.34891 97.42165  1.000 20.14121  ? 152 LEU A CD1 1 
ATOM   1179 C  CD2 . LEU A 1 153 ? 41.44787 43.57850 96.39330  1.000 17.27921  ? 152 LEU A CD2 1 
ATOM   1180 N  N   . ILE A 1 154 ? 43.86814 42.61841 92.23364  1.000 14.58616  ? 153 ILE A N   1 
ATOM   1181 C  CA  . ILE A 1 154 ? 44.90108 42.25757 91.26180  1.000 15.44293  ? 153 ILE A CA  1 
ATOM   1182 C  C   . ILE A 1 154 ? 45.99415 41.46791 91.97519  1.000 15.15361  ? 153 ILE A C   1 
ATOM   1183 O  O   . ILE A 1 154 ? 46.55389 41.95420 92.96626  1.000 14.39357  ? 153 ILE A O   1 
ATOM   1184 C  CB  . ILE A 1 154 ? 45.48259 43.50272 90.57479  1.000 13.32008  ? 153 ILE A CB  1 
ATOM   1185 C  CG1 . ILE A 1 154 ? 44.36622 44.37942 89.99146  1.000 18.73172  ? 153 ILE A CG1 1 
ATOM   1186 C  CG2 . ILE A 1 154 ? 46.49470 43.09154 89.50974  1.000 15.72293  ? 153 ILE A CG2 1 
ATOM   1187 C  CD1 . ILE A 1 154 ? 43.48342 43.67769 88.99102  1.000 22.68809  ? 153 ILE A CD1 1 
ATOM   1188 N  N   . PRO A 1 155 ? 46.33733 40.26208 91.52154  1.000 12.54443  ? 154 PRO A N   1 
ATOM   1189 C  CA  . PRO A 1 155 ? 47.34092 39.46510 92.24493  1.000 12.17796  ? 154 PRO A CA  1 
ATOM   1190 C  C   . PRO A 1 155 ? 48.74039 40.05082 92.10636  1.000 13.58896  ? 154 PRO A C   1 
ATOM   1191 O  O   . PRO A 1 155 ? 49.18490 40.39809 91.00942  1.000 14.94169  ? 154 PRO A O   1 
ATOM   1192 C  CB  . PRO A 1 155 ? 47.24932 38.08885 91.57346  1.000 14.34718  ? 154 PRO A CB  1 
ATOM   1193 C  CG  . PRO A 1 155 ? 46.76273 38.39299 90.18893  1.000 15.19981  ? 154 PRO A CG  1 
ATOM   1194 C  CD  . PRO A 1 155 ? 45.80387 39.54249 90.35084  1.000 13.09089  ? 154 PRO A CD  1 
ATOM   1195 N  N   . LEU A 1 156 ? 49.44084 40.13618 93.23512  1.000 12.99132  ? 155 LEU A N   1 
ATOM   1196 C  CA  . LEU A 1 156 ? 50.84416 40.52406 93.26923  1.000 12.95262  ? 155 LEU A CA  1 
ATOM   1197 C  C   . LEU A 1 156 ? 51.74887 39.37300 93.67917  1.000 13.60290  ? 155 LEU A C   1 
ATOM   1198 O  O   . LEU A 1 156 ? 52.76116 39.11719 93.02242  1.000 13.36683  ? 155 LEU A O   1 
ATOM   1199 C  CB  . LEU A 1 156 ? 51.04844 41.69310 94.23692  1.000 13.31494  ? 155 LEU A CB  1 
ATOM   1200 C  CG  . LEU A 1 156 ? 50.19333 42.92715 93.95973  1.000 13.25634  ? 155 LEU A CG  1 
ATOM   1201 C  CD1 . LEU A 1 156 ? 50.55769 44.01056 94.95558  1.000 16.29447  ? 155 LEU A CD1 1 
ATOM   1202 C  CD2 . LEU A 1 156 ? 50.38953 43.40896 92.52915  1.000 16.62680  ? 155 LEU A CD2 1 
ATOM   1203 N  N   . LEU A 1 157 ? 51.40639 38.66988 94.75648  1.000 12.81129  ? 156 LEU A N   1 
ATOM   1204 C  CA  . LEU A 1 157 ? 52.19145 37.55285 95.25749  1.000 13.47199  ? 156 LEU A CA  1 
ATOM   1205 C  C   . LEU A 1 157 ? 51.24702 36.49490 95.80229  1.000 12.82709  ? 156 LEU A C   1 
ATOM   1206 O  O   . LEU A 1 157 ? 50.40395 36.78948 96.65517  1.000 13.07857  ? 156 LEU A O   1 
ATOM   1207 C  CB  . LEU A 1 157 ? 53.15167 38.01716 96.36029  1.000 14.53532  ? 156 LEU A CB  1 
ATOM   1208 C  CG  . LEU A 1 157 ? 53.85574 36.92421 97.16156  1.000 14.21547  ? 156 LEU A CG  1 
ATOM   1209 C  CD1 . LEU A 1 157 ? 54.69914 36.05189 96.25116  1.000 14.65834  ? 156 LEU A CD1 1 
ATOM   1210 C  CD2 . LEU A 1 157 ? 54.70727 37.53205 98.26743  1.000 15.23951  ? 156 LEU A CD2 1 
ATOM   1211 N  N   . GLY A 1 158 ? 51.38079 35.27729 95.30251  1.000 12.89459  ? 157 GLY A N   1 
ATOM   1212 C  CA  . GLY A 1 158 ? 50.56225 34.15999 95.75001  1.000 11.24620  ? 157 GLY A CA  1 
ATOM   1213 C  C   . GLY A 1 158 ? 51.41211 33.08640 96.39573  1.000 11.86201  ? 157 GLY A C   1 
ATOM   1214 O  O   . GLY A 1 158 ? 52.51333 32.79522 95.92715  1.000 12.38381  ? 157 GLY A O   1 
ATOM   1215 N  N   . ILE A 1 159 ? 50.88254 32.49377 97.46133  1.000 13.08822  ? 158 ILE A N   1 
ATOM   1216 C  CA  . ILE A 1 159 ? 51.52371 31.40092 98.18108  1.000 15.38644  ? 158 ILE A CA  1 
ATOM   1217 C  C   . ILE A 1 159 ? 50.59290 30.20236 98.07801  1.000 12.70736  ? 158 ILE A C   1 
ATOM   1218 O  O   . ILE A 1 159 ? 49.50159 30.19965 98.66317  1.000 13.83716  ? 158 ILE A O   1 
ATOM   1219 C  CB  . ILE A 1 159 ? 51.78310 31.75639 99.65021  1.000 13.99258  ? 158 ILE A CB  1 
ATOM   1220 C  CG1 . ILE A 1 159 ? 52.47375 33.12090 99.76813  1.000 23.73648  ? 158 ILE A CG1 1 
ATOM   1221 C  CG2 . ILE A 1 159 ? 52.56513 30.64164 100.33009 1.000 17.13621  ? 158 ILE A CG2 1 
ATOM   1222 C  CD1 . ILE A 1 159 ? 53.87281 33.16114 99.21925  1.000 23.73816  ? 158 ILE A CD1 1 
ATOM   1223 N  N   . ASP A 1 160 ? 51.02397 29.18296 97.34610  1.000 13.53528  ? 159 ASP A N   1 
ATOM   1224 C  CA  . ASP A 1 160 ? 50.24827 27.96028 97.18290  1.000 12.13816  ? 159 ASP A CA  1 
ATOM   1225 C  C   . ASP A 1 160 ? 50.35838 27.13213 98.46172  1.000 13.49192  ? 159 ASP A C   1 
ATOM   1226 O  O   . ASP A 1 160 ? 51.46039 26.73738 98.85801  1.000 13.64300  ? 159 ASP A O   1 
ATOM   1227 C  CB  . ASP A 1 160 ? 50.82749 27.19793 95.99123  1.000 13.43076  ? 159 ASP A CB  1 
ATOM   1228 C  CG  . ASP A 1 160 ? 49.97168 26.03023 95.54189  1.000 13.57467  ? 159 ASP A CG  1 
ATOM   1229 O  OD1 . ASP A 1 160 ? 48.90787 25.76478 96.14170  1.000 13.44270  ? 159 ASP A OD1 1 
ATOM   1230 O  OD2 . ASP A 1 160 ? 50.36961 25.36731 94.55992  1.000 14.56283  ? 159 ASP A OD2 1 
ATOM   1231 N  N   . VAL A 1 161 ? 49.22683 26.86782 99.11254  1.000 12.84147  ? 160 VAL A N   1 
ATOM   1232 C  CA  . VAL A 1 161 ? 49.21784 26.05835 100.32712 1.000 13.84288  ? 160 VAL A CA  1 
ATOM   1233 C  C   . VAL A 1 161 ? 48.44734 24.75047 100.15458 1.000 15.00591  ? 160 VAL A C   1 
ATOM   1234 O  O   . VAL A 1 161 ? 48.08275 24.10340 101.14100 1.000 13.65362  ? 160 VAL A O   1 
ATOM   1235 C  CB  . VAL A 1 161 ? 48.80040 26.84610 101.58607 1.000 11.52599  ? 160 VAL A CB  1 
ATOM   1236 C  CG1 . VAL A 1 161 ? 49.85237 27.90144 101.92051 1.000 14.16075  ? 160 VAL A CG1 1 
ATOM   1237 C  CG2 . VAL A 1 161 ? 47.40896 27.46058 101.43229 1.000 15.71804  ? 160 VAL A CG2 1 
ATOM   1238 N  N   . TRP A 1 162 ? 48.20042 24.34382 98.91182  1.000 13.24711  ? 161 TRP A N   1 
ATOM   1239 C  CA  . TRP A 1 162 ? 47.83594 22.95885 98.66639  1.000 12.67342  ? 161 TRP A CA  1 
ATOM   1240 C  C   . TRP A 1 162 ? 48.94761 22.05680 99.18495  1.000 13.21642  ? 161 TRP A C   1 
ATOM   1241 O  O   . TRP A 1 162 ? 50.13108 22.40427 99.13835  1.000 11.96151  ? 161 TRP A O   1 
ATOM   1242 C  CB  . TRP A 1 162 ? 47.70516 22.72381 97.16701  1.000 12.90299  ? 161 TRP A CB  1 
ATOM   1243 C  CG  . TRP A 1 162 ? 46.41414 23.16796 96.57236  1.000 12.24547  ? 161 TRP A CG  1 
ATOM   1244 C  CD1 . TRP A 1 162 ? 45.93465 24.44763 96.50147  1.000 13.39077  ? 161 TRP A CD1 1 
ATOM   1245 C  CD2 . TRP A 1 162 ? 45.44836 22.33649 95.92046  1.000 11.79185  ? 161 TRP A CD2 1 
ATOM   1246 N  NE1 . TRP A 1 162 ? 44.72018 24.45814 95.85341  1.000 12.88810  ? 161 TRP A NE1 1 
ATOM   1247 C  CE2 . TRP A 1 162 ? 44.40337 23.17629 95.48408  1.000 11.66900  ? 161 TRP A CE2 1 
ATOM   1248 C  CE3 . TRP A 1 162 ? 45.36749 20.96347 95.66423  1.000 14.01879  ? 161 TRP A CE3 1 
ATOM   1249 C  CZ2 . TRP A 1 162 ? 43.28188 22.68571 94.81760  1.000 12.89430  ? 161 TRP A CZ2 1 
ATOM   1250 C  CZ3 . TRP A 1 162 ? 44.25175 20.47373 95.00102  1.000 13.16228  ? 161 TRP A CZ3 1 
ATOM   1251 C  CH2 . TRP A 1 162 ? 43.22744 21.33785 94.57711  1.000 12.77056  ? 161 TRP A CH2 1 
ATOM   1252 N  N   . GLU A 1 163 ? 48.56634 20.87522 99.66789  1.000 13.50281  ? 162 GLU A N   1 
ATOM   1253 C  CA  . GLU A 1 163 ? 49.56488 19.97836 100.23891 1.000 12.64193  ? 162 GLU A CA  1 
ATOM   1254 C  C   . GLU A 1 163 ? 50.63272 19.57791 99.22266  1.000 13.03587  ? 162 GLU A C   1 
ATOM   1255 O  O   . GLU A 1 163 ? 51.79976 19.41878 99.59280  1.000 13.84572  ? 162 GLU A O   1 
ATOM   1256 C  CB  . GLU A 1 163 ? 48.89394 18.77377 100.90354 1.000 13.65592  ? 162 GLU A CB  1 
ATOM   1257 C  CG  . GLU A 1 163 ? 48.22302 19.14728 102.22553 1.000 13.60821  ? 162 GLU A CG  1 
ATOM   1258 C  CD  . GLU A 1 163 ? 47.43710 18.01861 102.85709 1.000 15.26964  ? 162 GLU A CD  1 
ATOM   1259 O  OE1 . GLU A 1 163 ? 46.81249 17.22584 102.12105 1.000 13.01250  ? 162 GLU A OE1 1 
ATOM   1260 O  OE2 . GLU A 1 163 ? 47.44253 17.93028 104.10293 1.000 14.64718  ? 162 GLU A OE2 1 
ATOM   1261 N  N   . HIS A 1 164 ? 50.27620 19.45953 97.93737  1.000 12.60866  ? 163 HIS A N   1 
ATOM   1262 C  CA  . HIS A 1 164 ? 51.27428 19.11681 96.92712  1.000 13.31202  ? 163 HIS A CA  1 
ATOM   1263 C  C   . HIS A 1 164 ? 52.35551 20.17863 96.78121  1.000 13.13075  ? 163 HIS A C   1 
ATOM   1264 O  O   . HIS A 1 164 ? 53.40711 19.89757 96.20357  1.000 15.49256  ? 163 HIS A O   1 
ATOM   1265 C  CB  . HIS A 1 164 ? 50.63782 18.81291 95.56494  1.000 14.17452  ? 163 HIS A CB  1 
ATOM   1266 C  CG  . HIS A 1 164 ? 49.98821 19.99269 94.90846  1.000 13.91031  ? 163 HIS A CG  1 
ATOM   1267 N  ND1 . HIS A 1 164 ? 48.64026 20.03054 94.62682  1.000 14.51487  ? 163 HIS A ND1 1 
ATOM   1268 C  CD2 . HIS A 1 164 ? 50.49837 21.16671 94.46372  1.000 15.49469  ? 163 HIS A CD2 1 
ATOM   1269 C  CE1 . HIS A 1 164 ? 48.34667 21.17953 94.04175  1.000 12.64517  ? 163 HIS A CE1 1 
ATOM   1270 N  NE2 . HIS A 1 164 ? 49.45753 21.88711 93.93092  1.000 12.36045  ? 163 HIS A NE2 1 
ATOM   1271 N  N   . ALA A 1 165 ? 52.11913 21.39309 97.27358  1.000 13.20210  ? 164 ALA A N   1 
ATOM   1272 C  CA  . ALA A 1 165 ? 53.14590 22.42139 97.20019  1.000 14.39708  ? 164 ALA A CA  1 
ATOM   1273 C  C   . ALA A 1 165 ? 54.26846 22.19823 98.20522  1.000 13.49464  ? 164 ALA A C   1 
ATOM   1274 O  O   . ALA A 1 165 ? 55.33742 22.80195 98.05445  1.000 13.18579  ? 164 ALA A O   1 
ATOM   1275 C  CB  . ALA A 1 165 ? 52.52400 23.80187 97.41472  1.000 13.69081  ? 164 ALA A CB  1 
ATOM   1276 N  N   . TYR A 1 166 ? 54.06822 21.33668 99.20970  1.000 14.06206  ? 165 TYR A N   1 
ATOM   1277 C  CA  . TYR A 1 166 ? 55.05014 21.24075 100.28410 1.000 12.86030  ? 165 TYR A CA  1 
ATOM   1278 C  C   . TYR A 1 166 ? 55.21749 19.86142 100.91131 1.000 12.85216  ? 165 TYR A C   1 
ATOM   1279 O  O   . TYR A 1 166 ? 56.23263 19.61757 101.57448 1.000 13.58732  ? 165 TYR A O   1 
ATOM   1280 C  CB  . TYR A 1 166 ? 54.75535 22.26915 101.38434 1.000 13.11294  ? 165 TYR A CB  1 
ATOM   1281 C  CG  . TYR A 1 166 ? 53.42187 22.13216 102.10054 1.000 13.20943  ? 165 TYR A CG  1 
ATOM   1282 C  CD1 . TYR A 1 166 ? 53.26374 21.25008 103.16894 1.000 13.77392  ? 165 TYR A CD1 1 
ATOM   1283 C  CD2 . TYR A 1 166 ? 52.33556 22.91361 101.73358 1.000 14.75876  ? 165 TYR A CD2 1 
ATOM   1284 C  CE1 . TYR A 1 166 ? 52.05085 21.13618 103.83966 1.000 12.34743  ? 165 TYR A CE1 1 
ATOM   1285 C  CE2 . TYR A 1 166 ? 51.12305 22.81062 102.39727 1.000 13.29443  ? 165 TYR A CE2 1 
ATOM   1286 C  CZ  . TYR A 1 166 ? 50.98203 21.92209 103.44691 1.000 12.20760  ? 165 TYR A CZ  1 
ATOM   1287 O  OH  . TYR A 1 166 ? 49.76424 21.84074 104.09852 1.000 14.36213  ? 165 TYR A OH  1 
ATOM   1288 N  N   . TYR A 1 167 ? 54.26559 18.94649 100.69181 1.000 14.38480  ? 166 TYR A N   1 
ATOM   1289 C  CA  . TYR A 1 167 ? 54.16705 17.77321 101.55850 1.000 12.40590  ? 166 TYR A CA  1 
ATOM   1290 C  C   . TYR A 1 167 ? 55.38355 16.85645 101.45193 1.000 14.52939  ? 166 TYR A C   1 
ATOM   1291 O  O   . TYR A 1 167 ? 55.84232 16.31694 102.46621 1.000 14.46146  ? 166 TYR A O   1 
ATOM   1292 C  CB  . TYR A 1 167 ? 52.87216 16.99304 101.29809 1.000 10.59463  ? 166 TYR A CB  1 
ATOM   1293 C  CG  . TYR A 1 167 ? 52.47193 16.16350 102.50166 1.000 13.15495  ? 166 TYR A CG  1 
ATOM   1294 C  CD1 . TYR A 1 167 ? 51.69578 16.71554 103.51276 1.000 14.38917  ? 166 TYR A CD1 1 
ATOM   1295 C  CD2 . TYR A 1 167 ? 52.90560 14.84740 102.64733 1.000 13.92395  ? 166 TYR A CD2 1 
ATOM   1296 C  CE1 . TYR A 1 167 ? 51.35143 15.99262 104.62548 1.000 14.39758  ? 166 TYR A CE1 1 
ATOM   1297 C  CE2 . TYR A 1 167 ? 52.55973 14.10672 103.76094 1.000 12.76233  ? 166 TYR A CE2 1 
ATOM   1298 C  CZ  . TYR A 1 167 ? 51.78459 14.68378 104.74463 1.000 13.15179  ? 166 TYR A CZ  1 
ATOM   1299 O  OH  . TYR A 1 167 ? 51.43593 13.96627 105.85712 1.000 13.53103  ? 166 TYR A OH  1 
ATOM   1300 N  N   . LEU A 1 168 ? 55.90770 16.64390 100.24237 1.000 13.70730  ? 167 LEU A N   1 
ATOM   1301 C  CA  . LEU A 1 168 ? 57.02941 15.71751 100.09608 1.000 14.16086  ? 167 LEU A CA  1 
ATOM   1302 C  C   . LEU A 1 168 ? 58.20135 16.12641 100.97841 1.000 13.94898  ? 167 LEU A C   1 
ATOM   1303 O  O   . LEU A 1 168 ? 58.89217 15.27225 101.54904 1.000 16.52958  ? 167 LEU A O   1 
ATOM   1304 C  CB  . LEU A 1 168 ? 57.46809 15.63876 98.63365  1.000 14.45145  ? 167 LEU A CB  1 
ATOM   1305 C  CG  . LEU A 1 168 ? 56.54314 14.88859 97.67552  1.000 18.38935  ? 167 LEU A CG  1 
ATOM   1306 C  CD1 . LEU A 1 168 ? 57.05902 15.01909 96.25790  1.000 18.33035  ? 167 LEU A CD1 1 
ATOM   1307 C  CD2 . LEU A 1 168 ? 56.46051 13.42569 98.07383  1.000 21.89017  ? 167 LEU A CD2 1 
ATOM   1308 N  N   . GLN A 1 169 ? 58.41736 17.42913 101.13129 1.000 15.66241  ? 168 GLN A N   1 
ATOM   1309 C  CA  . GLN A 1 169 ? 59.57049 17.95633 101.84420 1.000 14.30173  ? 168 GLN A CA  1 
ATOM   1310 C  C   . GLN A 1 169 ? 59.26753 18.27979 103.30128 1.000 16.97559  ? 168 GLN A C   1 
ATOM   1311 O  O   . GLN A 1 169 ? 60.03490 17.90475 104.19384 1.000 20.72456  ? 168 GLN A O   1 
ATOM   1312 C  CB  . GLN A 1 169 ? 60.08635 19.19875 101.10791 1.000 16.13964  ? 168 GLN A CB  1 
ATOM   1313 C  CG  . GLN A 1 169 ? 61.28118 19.87142 101.74415 1.000 15.39116  ? 168 GLN A CG  1 
ATOM   1314 C  CD  . GLN A 1 169 ? 61.85293 20.95744 100.85669 1.000 18.35725  ? 168 GLN A CD  1 
ATOM   1315 O  OE1 . GLN A 1 169 ? 61.35946 21.19091 99.75505  1.000 18.36388  ? 168 GLN A OE1 1 
ATOM   1316 N  NE2 . GLN A 1 169 ? 62.90338 21.61834 101.32684 1.000 18.68237  ? 168 GLN A NE2 1 
ATOM   1317 N  N   . TYR A 1 170 ? 58.15465 18.95918 103.56062 1.000 13.07201  ? 169 TYR A N   1 
ATOM   1318 C  CA  . TYR A 1 170 ? 57.82347 19.47061 104.88394 1.000 14.19412  ? 169 TYR A CA  1 
ATOM   1319 C  C   . TYR A 1 170 ? 56.72757 18.68276 105.58614 1.000 13.64457  ? 169 TYR A C   1 
ATOM   1320 O  O   . TYR A 1 170 ? 56.39981 18.99707 106.73657 1.000 14.99194  ? 169 TYR A O   1 
ATOM   1321 C  CB  . TYR A 1 170 ? 57.44010 20.95525 104.79539 1.000 14.55985  ? 169 TYR A CB  1 
ATOM   1322 C  CG  . TYR A 1 170 ? 58.58066 21.80475 104.28281 1.000 13.91664  ? 169 TYR A CG  1 
ATOM   1323 C  CD1 . TYR A 1 170 ? 59.62858 22.16193 105.12419 1.000 16.95445  ? 169 TYR A CD1 1 
ATOM   1324 C  CD2 . TYR A 1 170 ? 58.62410 22.23441 102.95840 1.000 13.29294  ? 169 TYR A CD2 1 
ATOM   1325 C  CE1 . TYR A 1 170 ? 60.68362 22.92678 104.67029 1.000 17.83071  ? 169 TYR A CE1 1 
ATOM   1326 C  CE2 . TYR A 1 170 ? 59.68851 23.01185 102.49390 1.000 14.37000  ? 169 TYR A CE2 1 
ATOM   1327 C  CZ  . TYR A 1 170 ? 60.70750 23.35217 103.35909 1.000 14.68706  ? 169 TYR A CZ  1 
ATOM   1328 O  OH  . TYR A 1 170 ? 61.76599 24.11116 102.91124 1.000 18.18101  ? 169 TYR A OH  1 
ATOM   1329 N  N   . LYS A 1 171 ? 56.15206 17.67505 104.92746 1.000 13.55710  ? 170 LYS A N   1 
ATOM   1330 C  CA  . LYS A 1 171 ? 55.08111 16.86203 105.49434 1.000 13.99694  ? 170 LYS A CA  1 
ATOM   1331 C  C   . LYS A 1 171 ? 53.94343 17.75446 105.97926 1.000 15.65861  ? 170 LYS A C   1 
ATOM   1332 O  O   . LYS A 1 171 ? 53.56407 18.70176 105.28625 1.000 16.70923  ? 170 LYS A O   1 
ATOM   1333 C  CB  . LYS A 1 171 ? 55.61486 15.93929 106.60271 1.000 16.25668  ? 170 LYS A CB  1 
ATOM   1334 C  CG  . LYS A 1 171 ? 56.91950 15.20458 106.27259 1.000 23.04797  ? 170 LYS A CG  1 
ATOM   1335 C  CD  . LYS A 1 171 ? 56.81760 14.35734 105.01774 1.000 22.42683  ? 170 LYS A CD  1 
ATOM   1336 C  CE  . LYS A 1 171 ? 58.09536 13.54336 104.76367 1.000 24.97124  ? 170 LYS A CE  1 
ATOM   1337 N  NZ  . LYS A 1 171 ? 59.31276 14.35322 104.45062 1.000 23.45868  ? 170 LYS A NZ  1 
ATOM   1338 N  N   . ASN A 1 172 ? 53.40496 17.47500 107.16758 1.000 15.16606  ? 171 ASN A N   1 
ATOM   1339 C  CA  . ASN A 1 172 ? 52.25791 18.20704 107.68916 1.000 15.18779  ? 171 ASN A CA  1 
ATOM   1340 C  C   . ASN A 1 172 ? 52.59981 19.60060 108.19440 1.000 13.94078  ? 171 ASN A C   1 
ATOM   1341 O  O   . ASN A 1 172 ? 51.67621 20.36227 108.49824 1.000 16.00746  ? 171 ASN A O   1 
ATOM   1342 C  CB  . ASN A 1 172 ? 51.63183 17.42538 108.84754 1.000 16.41252  ? 171 ASN A CB  1 
ATOM   1343 C  CG  . ASN A 1 172 ? 52.59906 17.23121 109.99696 1.000 16.82220  ? 171 ASN A CG  1 
ATOM   1344 O  OD1 . ASN A 1 172 ? 53.58921 16.52239 109.86928 1.000 16.83922  ? 171 ASN A OD1 1 
ATOM   1345 N  ND2 . ASN A 1 172 ? 52.33148 17.88836 111.11622 1.000 18.31448  ? 171 ASN A ND2 1 
ATOM   1346 N  N   . VAL A 1 173 ? 53.87823 19.94483 108.30853 1.000 14.89117  ? 172 VAL A N   1 
ATOM   1347 C  CA  . VAL A 1 173 ? 54.28172 21.18299 108.99731 1.000 15.93829  ? 172 VAL A CA  1 
ATOM   1348 C  C   . VAL A 1 173 ? 54.27968 22.29811 107.95764 1.000 15.38830  ? 172 VAL A C   1 
ATOM   1349 O  O   . VAL A 1 173 ? 55.31913 22.78647 107.50450 1.000 15.20234  ? 172 VAL A O   1 
ATOM   1350 C  CB  . VAL A 1 173 ? 55.61594 21.03971 109.73008 1.000 15.35884  ? 172 VAL A CB  1 
ATOM   1351 C  CG1 . VAL A 1 173 ? 55.78521 22.19031 110.71246 1.000 18.63987  ? 172 VAL A CG1 1 
ATOM   1352 C  CG2 . VAL A 1 173 ? 55.66626 19.71523 110.45818 1.000 15.42310  ? 172 VAL A CG2 1 
ATOM   1353 N  N   . ARG A 1 174 ? 53.07673 22.75333 107.61814 1.000 16.81742  ? 173 ARG A N   1 
ATOM   1354 C  CA  . ARG A 1 174 ? 52.96006 23.87309 106.68951 1.000 15.19842  ? 173 ARG A CA  1 
ATOM   1355 C  C   . ARG A 1 174 ? 53.74240 25.10737 107.13373 1.000 15.82382  ? 173 ARG A C   1 
ATOM   1356 O  O   . ARG A 1 174 ? 54.30615 25.78675 106.25848 1.000 14.80103  ? 173 ARG A O   1 
ATOM   1357 C  CB  . ARG A 1 174 ? 51.48368 24.19141 106.41156 1.000 16.52842  ? 173 ARG A CB  1 
ATOM   1358 C  CG  . ARG A 1 174 ? 51.28746 25.17733 105.27535 1.000 15.49084  ? 173 ARG A CG  1 
ATOM   1359 C  CD  . ARG A 1 174 ? 49.87000 25.73055 105.23258 1.000 16.19815  ? 173 ARG A CD  1 
ATOM   1360 N  NE  . ARG A 1 174 ? 48.87123 24.72086 104.90410 1.000 16.07574  ? 173 ARG A NE  1 
ATOM   1361 C  CZ  . ARG A 1 174 ? 47.56344 24.94667 104.86457 1.000 15.51355  ? 173 ARG A CZ  1 
ATOM   1362 N  NH1 . ARG A 1 174 ? 47.06064 26.14768 105.10955 1.000 15.46346  ? 173 ARG A NH1 1 
ATOM   1363 N  NH2 . ARG A 1 174 ? 46.74026 23.94660 104.56621 1.000 18.07205  ? 173 ARG A NH2 1 
ATOM   1364 N  N   . PRO A 1 175 ? 53.83879 25.44762 108.42660 1.000 15.66125  ? 174 PRO A N   1 
ATOM   1365 C  CA  . PRO A 1 175 ? 54.65338 26.61730 108.80197 1.000 17.27933  ? 174 PRO A CA  1 
ATOM   1366 C  C   . PRO A 1 175 ? 56.12082 26.53162 108.39712 1.000 18.22659  ? 174 PRO A C   1 
ATOM   1367 O  O   . PRO A 1 175 ? 56.72344 27.57493 108.11704 1.000 16.53584  ? 174 PRO A O   1 
ATOM   1368 C  CB  . PRO A 1 175 ? 54.45470 26.71340 110.32116 1.000 17.35489  ? 174 PRO A CB  1 
ATOM   1369 C  CG  . PRO A 1 175 ? 53.10447 26.12722 110.53618 1.000 17.74859  ? 174 PRO A CG  1 
ATOM   1370 C  CD  . PRO A 1 175 ? 53.04172 24.97121 109.57457 1.000 17.13381  ? 174 PRO A CD  1 
ATOM   1371 N  N   . ASP A 1 176 ? 56.71465 25.33191 108.34967 1.000 18.07941  ? 175 ASP A N   1 
ATOM   1372 C  CA  . ASP A 1 176 ? 58.10097 25.20542 107.89628 1.000 18.54385  ? 175 ASP A CA  1 
ATOM   1373 C  C   . ASP A 1 176 ? 58.22622 25.57253 106.42440 1.000 14.56821  ? 175 ASP A C   1 
ATOM   1374 O  O   . ASP A 1 176 ? 59.20097 26.21139 106.01278 1.000 14.37652  ? 175 ASP A O   1 
ATOM   1375 C  CB  . ASP A 1 176 ? 58.59019 23.76999 108.11138 1.000 17.29993  ? 175 ASP A CB  1 
ATOM   1376 C  CG  . ASP A 1 176 ? 58.91424 23.46465 109.55858 1.000 19.86435  ? 175 ASP A CG  1 
ATOM   1377 O  OD1 . ASP A 1 176 ? 58.83252 24.38068 110.40120 1.000 24.06039  ? 175 ASP A OD1 1 
ATOM   1378 O  OD2 . ASP A 1 176 ? 59.20753 22.28460 109.85186 1.000 26.70943  ? 175 ASP A OD2 1 
ATOM   1379 N  N   . TYR A 1 177 ? 57.23751 25.18086 105.61926 1.000 13.95962  ? 176 TYR A N   1 
ATOM   1380 C  CA  . TYR A 1 177 ? 57.21971 25.56615 104.21465 1.000 13.75477  ? 176 TYR A CA  1 
ATOM   1381 C  C   . TYR A 1 177 ? 57.07661 27.07365 104.05997 1.000 12.78467  ? 176 TYR A C   1 
ATOM   1382 O  O   . TYR A 1 177 ? 57.79705 27.69402 103.26850 1.000 14.26992  ? 176 TYR A O   1 
ATOM   1383 C  CB  . TYR A 1 177 ? 56.06675 24.83685 103.53401 1.000 10.93261  ? 176 TYR A CB  1 
ATOM   1384 C  CG  . TYR A 1 177 ? 55.59871 25.38966 102.21061 1.000 14.15246  ? 176 TYR A CG  1 
ATOM   1385 C  CD1 . TYR A 1 177 ? 56.42152 25.38381 101.08817 1.000 14.14787  ? 176 TYR A CD1 1 
ATOM   1386 C  CD2 . TYR A 1 177 ? 54.29656 25.86095 102.06947 1.000 13.23661  ? 176 TYR A CD2 1 
ATOM   1387 C  CE1 . TYR A 1 177 ? 55.96427 25.86781 99.86677  1.000 13.78447  ? 176 TYR A CE1 1 
ATOM   1388 C  CE2 . TYR A 1 177 ? 53.83290 26.33687 100.85999 1.000 13.95750  ? 176 TYR A CE2 1 
ATOM   1389 C  CZ  . TYR A 1 177 ? 54.66464 26.33146 99.76330  1.000 11.97753  ? 176 TYR A CZ  1 
ATOM   1390 O  OH  . TYR A 1 177 ? 54.18294 26.80902 98.56375  1.000 13.65212  ? 176 TYR A OH  1 
ATOM   1391 N  N   . LEU A 1 178 ? 56.16545 27.68434 104.82569 1.000 15.55599  ? 177 LEU A N   1 
ATOM   1392 C  CA  . LEU A 1 178 ? 55.96852 29.12873 104.73168 1.000 15.35982  ? 177 LEU A CA  1 
ATOM   1393 C  C   . LEU A 1 178 ? 57.22625 29.88622 105.14314 1.000 18.16292  ? 177 LEU A C   1 
ATOM   1394 O  O   . LEU A 1 178 ? 57.58175 30.89122 104.52024 1.000 19.86155  ? 177 LEU A O   1 
ATOM   1395 C  CB  . LEU A 1 178 ? 54.78055 29.55948 105.59107 1.000 15.54221  ? 177 LEU A CB  1 
ATOM   1396 C  CG  . LEU A 1 178 ? 53.38893 29.70917 104.96245 1.000 27.97046  ? 177 LEU A CG  1 
ATOM   1397 C  CD1 . LEU A 1 178 ? 53.30559 29.13885 103.55970 1.000 20.13804  ? 177 LEU A CD1 1 
ATOM   1398 C  CD2 . LEU A 1 178 ? 52.34805 29.07289 105.85549 1.000 24.93387  ? 177 LEU A CD2 1 
ATOM   1399 N  N   . LYS A 1 179 ? 57.92416 29.40779 106.17787 1.000 14.73732  ? 178 LYS A N   1 
ATOM   1400 C  CA  . LYS A 1 179 ? 59.18310 30.04112 106.56121 1.000 15.95837  ? 178 LYS A CA  1 
ATOM   1401 C  C   . LYS A 1 179 ? 60.19033 29.96400 105.42520 1.000 14.57780  ? 178 LYS A C   1 
ATOM   1402 O  O   . LYS A 1 179 ? 60.88423 30.94328 105.12850 1.000 18.06856  ? 178 LYS A O   1 
ATOM   1403 C  CB  . LYS A 1 179 ? 59.74788 29.35945 107.80790 1.000 16.68441  ? 178 LYS A CB  1 
ATOM   1404 C  CG  . LYS A 1 179 ? 58.94991 29.59564 109.07118 1.000 33.25148  ? 178 LYS A CG  1 
ATOM   1405 C  CD  . LYS A 1 179 ? 59.34803 28.61787 110.16912 1.000 47.49927  ? 178 LYS A CD  1 
ATOM   1406 C  CE  . LYS A 1 179 ? 60.83763 28.68494 110.46633 1.000 57.45292  ? 178 LYS A CE  1 
ATOM   1407 N  NZ  . LYS A 1 179 ? 61.19150 27.89347 111.67929 1.000 64.33950  ? 178 LYS A NZ  1 
ATOM   1408 N  N   . ALA A 1 180 ? 60.27906 28.80334 104.77305 1.000 15.30772  ? 179 ALA A N   1 
ATOM   1409 C  CA  . ALA A 1 180 ? 61.27117 28.61442 103.72466 1.000 15.44954  ? 179 ALA A CA  1 
ATOM   1410 C  C   . ALA A 1 180 ? 60.96431 29.45534 102.49167 1.000 14.17596  ? 179 ALA A C   1 
ATOM   1411 O  O   . ALA A 1 180 ? 61.88269 29.98105 101.85044 1.000 15.37411  ? 179 ALA A O   1 
ATOM   1412 C  CB  . ALA A 1 180 ? 61.33337 27.13599 103.34854 1.000 14.41349  ? 179 ALA A CB  1 
ATOM   1413 N  N   . ILE A 1 181 ? 59.68219 29.60662 102.14618 1.000 15.21868  ? 180 ILE A N   1 
ATOM   1414 C  CA  . ILE A 1 181 ? 59.35584 30.21346 100.85702 1.000 15.07903  ? 180 ILE A CA  1 
ATOM   1415 C  C   . ILE A 1 181 ? 59.75869 31.68251 100.79281 1.000 16.96138  ? 180 ILE A C   1 
ATOM   1416 O  O   . ILE A 1 181 ? 60.03566 32.20355 99.70526  1.000 14.71260  ? 180 ILE A O   1 
ATOM   1417 C  CB  . ILE A 1 181 ? 57.88442 29.98144 100.46488 1.000 13.13070  ? 180 ILE A CB  1 
ATOM   1418 C  CG1 . ILE A 1 181 ? 57.72072 30.18575 98.95681  1.000 14.78936  ? 180 ILE A CG1 1 
ATOM   1419 C  CG2 . ILE A 1 181 ? 56.97381 30.89943 101.25918 1.000 15.37667  ? 180 ILE A CG2 1 
ATOM   1420 C  CD1 . ILE A 1 181 ? 56.33964 29.84148 98.42536  1.000 16.00885  ? 180 ILE A CD1 1 
ATOM   1421 N  N   . TRP A 1 182 ? 59.83842 32.36975 101.93699 1.000 14.78175  ? 181 TRP A N   1 
ATOM   1422 C  CA  . TRP A 1 182 ? 60.25950 33.76866 101.90840 1.000 14.59214  ? 181 TRP A CA  1 
ATOM   1423 C  C   . TRP A 1 182 ? 61.65714 33.93751 101.32628 1.000 15.74059  ? 181 TRP A C   1 
ATOM   1424 O  O   . TRP A 1 182 ? 61.98507 35.02335 100.83155 1.000 16.77960  ? 181 TRP A O   1 
ATOM   1425 C  CB  . TRP A 1 182 ? 60.16813 34.40008 103.30339 1.000 16.50698  ? 181 TRP A CB  1 
ATOM   1426 C  CG  . TRP A 1 182 ? 58.76378 34.50608 103.79042 1.000 18.95032  ? 181 TRP A CG  1 
ATOM   1427 C  CD1 . TRP A 1 182 ? 58.17103 33.75216 104.76168 1.000 22.63941  ? 181 TRP A CD1 1 
ATOM   1428 C  CD2 . TRP A 1 182 ? 57.76514 35.41578 103.32341 1.000 18.71962  ? 181 TRP A CD2 1 
ATOM   1429 N  NE1 . TRP A 1 182 ? 56.86096 34.13341 104.92339 1.000 20.11345  ? 181 TRP A NE1 1 
ATOM   1430 C  CE2 . TRP A 1 182 ? 56.58495 35.15294 104.05141 1.000 20.47148  ? 181 TRP A CE2 1 
ATOM   1431 C  CE3 . TRP A 1 182 ? 57.74924 36.42264 102.35496 1.000 19.55840  ? 181 TRP A CE3 1 
ATOM   1432 C  CZ2 . TRP A 1 182 ? 55.40673 35.86601 103.84494 1.000 21.77010  ? 181 TRP A CZ2 1 
ATOM   1433 C  CZ3 . TRP A 1 182 ? 56.57466 37.13030 102.15048 1.000 24.08863  ? 181 TRP A CZ3 1 
ATOM   1434 C  CH2 . TRP A 1 182 ? 55.42068 36.84808 102.89322 1.000 22.28606  ? 181 TRP A CH2 1 
ATOM   1435 N  N   . ASN A 1 183 ? 62.47752 32.88720 101.35537 1.000 16.86941  ? 182 ASN A N   1 
ATOM   1436 C  CA  . ASN A 1 183 ? 63.82527 32.97255 100.81417 1.000 16.94690  ? 182 ASN A CA  1 
ATOM   1437 C  C   . ASN A 1 183 ? 63.86101 32.99448 99.29090  1.000 14.72042  ? 182 ASN A C   1 
ATOM   1438 O  O   . ASN A 1 183 ? 64.90580 33.32933 98.72070  1.000 18.88188  ? 182 ASN A O   1 
ATOM   1439 C  CB  . ASN A 1 183 ? 64.66344 31.81385 101.35266 1.000 17.41435  ? 182 ASN A CB  1 
ATOM   1440 C  CG  . ASN A 1 183 ? 64.84981 31.88527 102.85321 1.000 19.31498  ? 182 ASN A CG  1 
ATOM   1441 O  OD1 . ASN A 1 183 ? 65.57189 32.74941 103.35595 1.000 22.71568  ? 182 ASN A OD1 1 
ATOM   1442 N  ND2 . ASN A 1 183 ? 64.20242 30.98288 103.57886 1.000 18.76989  ? 182 ASN A ND2 1 
ATOM   1443 N  N   . VAL A 1 184 ? 62.75323 32.68004 98.61429  1.000 15.03734  ? 183 VAL A N   1 
ATOM   1444 C  CA  . VAL A 1 184 ? 62.75470 32.59350 97.15946  1.000 15.70654  ? 183 VAL A CA  1 
ATOM   1445 C  C   . VAL A 1 184 ? 61.72646 33.51240 96.50633  1.000 13.96869  ? 183 VAL A C   1 
ATOM   1446 O  O   . VAL A 1 184 ? 61.48345 33.39711 95.30280  1.000 15.57532  ? 183 VAL A O   1 
ATOM   1447 C  CB  . VAL A 1 184 ? 62.60257 31.14140 96.66035  1.000 14.18715  ? 183 VAL A CB  1 
ATOM   1448 C  CG1 . VAL A 1 184 ? 63.81360 30.30536 97.06612  1.000 16.34494  ? 183 VAL A CG1 1 
ATOM   1449 C  CG2 . VAL A 1 184 ? 61.31865 30.52696 97.19408  1.000 17.38462  ? 183 VAL A CG2 1 
ATOM   1450 N  N   . ILE A 1 185 ? 61.12244 34.43258 97.26140  1.000 13.99546  ? 184 ILE A N   1 
ATOM   1451 C  CA  . ILE A 1 185 ? 60.15176 35.34221 96.66101  1.000 15.93359  ? 184 ILE A CA  1 
ATOM   1452 C  C   . ILE A 1 185 ? 60.85595 36.24037 95.65405  1.000 14.76697  ? 184 ILE A C   1 
ATOM   1453 O  O   . ILE A 1 185 ? 61.84356 36.91537 95.97804  1.000 15.50422  ? 184 ILE A O   1 
ATOM   1454 C  CB  . ILE A 1 185 ? 59.42767 36.17232 97.73109  1.000 16.63206  ? 184 ILE A CB  1 
ATOM   1455 C  CG1 . ILE A 1 185 ? 58.73738 35.26351 98.74695  1.000 22.83416  ? 184 ILE A CG1 1 
ATOM   1456 C  CG2 . ILE A 1 185 ? 58.42584 37.11236 97.07015  1.000 15.32247  ? 184 ILE A CG2 1 
ATOM   1457 C  CD1 . ILE A 1 185 ? 57.74741 34.31373 98.13684  1.000 18.19612  ? 184 ILE A CD1 1 
ATOM   1458 N  N   . ASN A 1 186 ? 60.33711 36.26796 94.42797  1.000 13.43661  ? 185 ASN A N   1 
ATOM   1459 C  CA  . ASN A 1 186 ? 60.89098 37.09920 93.36255  1.000 14.69372  ? 185 ASN A CA  1 
ATOM   1460 C  C   . ASN A 1 186 ? 60.28446 38.49053 93.49056  1.000 13.89501  ? 185 ASN A C   1 
ATOM   1461 O  O   . ASN A 1 186 ? 59.30253 38.82960 92.83182  1.000 15.08025  ? 185 ASN A O   1 
ATOM   1462 C  CB  . ASN A 1 186 ? 60.58924 36.47699 92.00838  1.000 14.35317  ? 185 ASN A CB  1 
ATOM   1463 C  CG  . ASN A 1 186 ? 61.20997 37.24084 90.86437  1.000 14.96894  ? 185 ASN A CG  1 
ATOM   1464 O  OD1 . ASN A 1 186 ? 61.90705 38.23867 91.07125  1.000 18.74299  ? 185 ASN A OD1 1 
ATOM   1465 N  ND2 . ASN A 1 186 ? 60.97740 36.77260 89.64874  1.000 16.68243  ? 185 ASN A ND2 1 
ATOM   1466 N  N   . TRP A 1 187 ? 60.89560 39.31858 94.34280  1.000 13.87817  ? 186 TRP A N   1 
ATOM   1467 C  CA  . TRP A 1 187 ? 60.38726 40.67058 94.54869  1.000 13.90599  ? 186 TRP A CA  1 
ATOM   1468 C  C   . TRP A 1 187 ? 60.48823 41.53843 93.30161  1.000 14.47526  ? 186 TRP A C   1 
ATOM   1469 O  O   . TRP A 1 187 ? 59.70815 42.48632 93.16734  1.000 15.31581  ? 186 TRP A O   1 
ATOM   1470 C  CB  . TRP A 1 187 ? 61.07006 41.33077 95.75119  1.000 16.59748  ? 186 TRP A CB  1 
ATOM   1471 C  CG  . TRP A 1 187 ? 60.67384 40.68670 97.04160  1.000 17.52624  ? 186 TRP A CG  1 
ATOM   1472 C  CD1 . TRP A 1 187 ? 61.46946 39.95466 97.87472  1.000 18.08240  ? 186 TRP A CD1 1 
ATOM   1473 C  CD2 . TRP A 1 187 ? 59.37266 40.69927 97.63720  1.000 17.40662  ? 186 TRP A CD2 1 
ATOM   1474 N  NE1 . TRP A 1 187 ? 60.74401 39.51606 98.95470  1.000 24.15484  ? 186 TRP A NE1 1 
ATOM   1475 C  CE2 . TRP A 1 187 ? 59.45219 39.95448 98.83078  1.000 18.18939  ? 186 TRP A CE2 1 
ATOM   1476 C  CE3 . TRP A 1 187 ? 58.14662 41.27025 97.27806  1.000 20.21245  ? 186 TRP A CE3 1 
ATOM   1477 C  CZ2 . TRP A 1 187 ? 58.35707 39.77172 99.66955  1.000 21.79521  ? 186 TRP A CZ2 1 
ATOM   1478 C  CZ3 . TRP A 1 187 ? 57.05816 41.08072 98.11089  1.000 26.21715  ? 186 TRP A CZ3 1 
ATOM   1479 C  CH2 . TRP A 1 187 ? 57.17173 40.33602 99.29137  1.000 22.45469  ? 186 TRP A CH2 1 
ATOM   1480 N  N   . GLU A 1 188 ? 61.40141 41.23411 92.37433  1.000 14.63881  ? 187 GLU A N   1 
ATOM   1481 C  CA  . GLU A 1 188 ? 61.40969 41.96618 91.11064  1.000 17.94831  ? 187 GLU A CA  1 
ATOM   1482 C  C   . GLU A 1 188 ? 60.09001 41.78273 90.36874  1.000 14.82525  ? 187 GLU A C   1 
ATOM   1483 O  O   . GLU A 1 188 ? 59.52379 42.74870 89.84149  1.000 16.44398  ? 187 GLU A O   1 
ATOM   1484 C  CB  . GLU A 1 188 ? 62.58622 41.52585 90.23782  1.000 19.79644  ? 187 GLU A CB  1 
ATOM   1485 C  CG  . GLU A 1 188 ? 62.64274 42.24438 88.89472  1.000 21.88501  ? 187 GLU A CG  1 
ATOM   1486 C  CD  . GLU A 1 188 ? 63.73939 41.71530 87.98505  1.000 37.27787  ? 187 GLU A CD  1 
ATOM   1487 O  OE1 . GLU A 1 188 ? 63.73136 40.50374 87.68271  1.000 34.57661  ? 187 GLU A OE1 1 
ATOM   1488 O  OE2 . GLU A 1 188 ? 64.60625 42.51245 87.56768  1.000 37.20697  ? 187 GLU A OE2 1 
ATOM   1489 N  N   . ASN A 1 189 ? 59.57165 40.54911 90.34401  1.000 14.15165  ? 188 ASN A N   1 
ATOM   1490 C  CA  . ASN A 1 189 ? 58.29626 40.28515 89.67849  1.000 13.99061  ? 188 ASN A CA  1 
ATOM   1491 C  C   . ASN A 1 189 ? 57.12577 40.91182 90.42894  1.000 13.35859  ? 188 ASN A C   1 
ATOM   1492 O  O   . ASN A 1 189 ? 56.23624 41.50922 89.80963  1.000 14.46441  ? 188 ASN A O   1 
ATOM   1493 C  CB  . ASN A 1 189 ? 58.07174 38.78125 89.52234  1.000 14.75381  ? 188 ASN A CB  1 
ATOM   1494 C  CG  . ASN A 1 189 ? 56.71082 38.45987 88.93336  1.000 14.27522  ? 188 ASN A CG  1 
ATOM   1495 O  OD1 . ASN A 1 189 ? 55.75193 38.18168 89.65934  1.000 14.68336  ? 188 ASN A OD1 1 
ATOM   1496 N  ND2 . ASN A 1 189 ? 56.60897 38.53171 87.61065  1.000 15.63560  ? 188 ASN A ND2 1 
ATOM   1497 N  N   . VAL A 1 190 ? 57.09581 40.77134 91.75750  1.000 14.32300  ? 189 VAL A N   1 
ATOM   1498 C  CA  . VAL A 1 190 ? 56.01336 41.36896 92.53423  1.000 13.86203  ? 189 VAL A CA  1 
ATOM   1499 C  C   . VAL A 1 190 ? 55.99227 42.87628 92.33096  1.000 13.34817  ? 189 VAL A C   1 
ATOM   1500 O  O   . VAL A 1 190 ? 54.92408 43.48772 92.19178  1.000 14.85338  ? 189 VAL A O   1 
ATOM   1501 C  CB  . VAL A 1 190 ? 56.13141 40.99002 94.02366  1.000 12.93014  ? 189 VAL A CB  1 
ATOM   1502 C  CG1 . VAL A 1 190 ? 54.93727 41.53361 94.80753  1.000 14.32368  ? 189 VAL A CG1 1 
ATOM   1503 C  CG2 . VAL A 1 190 ? 56.23023 39.47987 94.19209  1.000 12.23501  ? 189 VAL A CG2 1 
ATOM   1504 N  N   . THR A 1 191 ? 57.17730 43.49219 92.27488  1.000 16.34891  ? 190 THR A N   1 
ATOM   1505 C  CA  . THR A 1 191 ? 57.26610 44.92705 92.03112  1.000 15.23109  ? 190 THR A CA  1 
ATOM   1506 C  C   . THR A 1 191 ? 56.72105 45.28498 90.65624  1.000 16.66683  ? 190 THR A C   1 
ATOM   1507 O  O   . THR A 1 191 ? 55.97935 46.26552 90.51256  1.000 16.84768  ? 190 THR A O   1 
ATOM   1508 C  CB  . THR A 1 191 ? 58.72025 45.38196 92.17525  1.000 14.34402  ? 190 THR A CB  1 
ATOM   1509 O  OG1 . THR A 1 191 ? 59.11089 45.29143 93.55016  1.000 21.42486  ? 190 THR A OG1 1 
ATOM   1510 C  CG2 . THR A 1 191 ? 58.89328 46.82458 91.70189  1.000 19.47658  ? 190 THR A CG2 1 
ATOM   1511 N  N   . GLU A 1 192 ? 57.08136 44.50589 89.63250  1.000 16.39804  ? 191 GLU A N   1 
ATOM   1512 C  CA  . GLU A 1 192 ? 56.55022 44.74523 88.29451  1.000 18.40485  ? 191 GLU A CA  1 
ATOM   1513 C  C   . GLU A 1 192 ? 55.02967 44.68218 88.28715  1.000 19.03195  ? 191 GLU A C   1 
ATOM   1514 O  O   . GLU A 1 192 ? 54.36588 45.54417 87.70005  1.000 17.57637  ? 191 GLU A O   1 
ATOM   1515 C  CB  . GLU A 1 192 ? 57.12659 43.72873 87.31223  1.000 17.04401  ? 191 GLU A CB  1 
ATOM   1516 C  CG  . GLU A 1 192 ? 58.57329 43.97010 86.97833  1.000 17.65534  ? 191 GLU A CG  1 
ATOM   1517 C  CD  . GLU A 1 192 ? 59.13870 42.90387 86.06611  1.000 24.40540  ? 191 GLU A CD  1 
ATOM   1518 O  OE1 . GLU A 1 192 ? 58.38135 41.99161 85.67170  1.000 25.38379  ? 191 GLU A OE1 1 
ATOM   1519 O  OE2 . GLU A 1 192 ? 60.34038 42.98049 85.74328  1.000 29.94339  ? 191 GLU A OE2 1 
ATOM   1520 N  N   . ARG A 1 193 ? 54.45682 43.66570 88.93774  1.000 17.89370  ? 192 ARG A N   1 
ATOM   1521 C  CA  . ARG A 1 193 ? 53.00124 43.55491 88.98900  1.000 16.85608  ? 192 ARG A CA  1 
ATOM   1522 C  C   . ARG A 1 193 ? 52.38301 44.73057 89.73760  1.000 15.80003  ? 192 ARG A C   1 
ATOM   1523 O  O   . ARG A 1 193 ? 51.31973 45.23611 89.35284  1.000 17.36165  ? 192 ARG A O   1 
ATOM   1524 C  CB  . ARG A 1 193 ? 52.59673 42.22482 89.62780  1.000 14.54283  ? 192 ARG A CB  1 
ATOM   1525 C  CG  . ARG A 1 193 ? 53.00559 41.00683 88.82442  1.000 15.30064  ? 192 ARG A CG  1 
ATOM   1526 C  CD  . ARG A 1 193 ? 52.60032 39.70815 89.51590  1.000 13.50373  ? 192 ARG A CD  1 
ATOM   1527 N  NE  . ARG A 1 193 ? 52.98920 38.54516 88.72933  1.000 15.63245  ? 192 ARG A NE  1 
ATOM   1528 C  CZ  . ARG A 1 193 ? 52.28044 38.05145 87.72424  1.000 16.72168  ? 192 ARG A CZ  1 
ATOM   1529 N  NH1 . ARG A 1 193 ? 51.12215 38.58222 87.36834  1.000 18.13367  ? 192 ARG A NH1 1 
ATOM   1530 N  NH2 . ARG A 1 193 ? 52.74320 36.99743 87.05980  1.000 18.12539  ? 192 ARG A NH2 1 
ATOM   1531 N  N   . TYR A 1 194 ? 53.04338 45.18681 90.80216  1.000 17.68634  ? 193 TYR A N   1 
ATOM   1532 C  CA  . TYR A 1 194 ? 52.54695 46.32881 91.56267  1.000 17.05362  ? 193 TYR A CA  1 
ATOM   1533 C  C   . TYR A 1 194 ? 52.59232 47.60536 90.73427  1.000 19.53341  ? 193 TYR A C   1 
ATOM   1534 O  O   . TYR A 1 194 ? 51.60574 48.34908 90.67015  1.000 17.94471  ? 193 TYR A O   1 
ATOM   1535 C  CB  . TYR A 1 194 ? 53.35939 46.48985 92.84618  1.000 17.51280  ? 193 TYR A CB  1 
ATOM   1536 C  CG  . TYR A 1 194 ? 53.08087 47.78066 93.58451  1.000 16.11242  ? 193 TYR A CG  1 
ATOM   1537 C  CD1 . TYR A 1 194 ? 51.91781 47.94024 94.32408  1.000 21.15183  ? 193 TYR A CD1 1 
ATOM   1538 C  CD2 . TYR A 1 194 ? 53.98781 48.83179 93.55163  1.000 21.20936  ? 193 TYR A CD2 1 
ATOM   1539 C  CE1 . TYR A 1 194 ? 51.65423 49.12063 94.99850  1.000 17.23812  ? 193 TYR A CE1 1 
ATOM   1540 C  CE2 . TYR A 1 194 ? 53.73668 50.00673 94.22555  1.000 21.44628  ? 193 TYR A CE2 1 
ATOM   1541 C  CZ  . TYR A 1 194 ? 52.56976 50.14394 94.95037  1.000 21.96518  ? 193 TYR A CZ  1 
ATOM   1542 O  OH  . TYR A 1 194 ? 52.30178 51.31039 95.62793  1.000 22.36757  ? 193 TYR A OH  1 
ATOM   1543 N  N   . MET A 1 195 ? 53.72853 47.87048 90.08339  1.000 17.06721  ? 194 MET A N   1 
ATOM   1544 C  CA  . MET A 1 195 ? 53.85722 49.08815 89.28960  1.000 17.72999  ? 194 MET A CA  1 
ATOM   1545 C  C   . MET A 1 195 ? 52.88566 49.09600 88.11581  1.000 21.65251  ? 194 MET A C   1 
ATOM   1546 O  O   . MET A 1 195 ? 52.44036 50.16735 87.68755  1.000 22.02420  ? 194 MET A O   1 
ATOM   1547 C  CB  . MET A 1 195 ? 55.30720 49.26523 88.82159  1.000 15.90293  ? 194 MET A CB  1 
ATOM   1548 C  CG  . MET A 1 195 ? 56.30997 49.44193 89.95462  1.000 22.96596  ? 194 MET A CG  1 
ATOM   1549 S  SD  . MET A 1 195 ? 55.99155 50.89889 90.97611  1.000 23.87104  ? 194 MET A SD  1 
ATOM   1550 C  CE  . MET A 1 195 ? 56.39149 52.22612 89.83806  1.000 30.50598  ? 194 MET A CE  1 
ATOM   1551 N  N   . ALA A 1 196 ? 52.52956 47.91916 87.59389  1.000 20.10631  ? 195 ALA A N   1 
ATOM   1552 C  CA  . ALA A 1 196 ? 51.53450 47.84929 86.53230  1.000 19.64338  ? 195 ALA A CA  1 
ATOM   1553 C  C   . ALA A 1 196 ? 50.14918 48.26014 87.01298  1.000 23.63147  ? 195 ALA A C   1 
ATOM   1554 O  O   . ALA A 1 196 ? 49.33285 48.69948 86.19658  1.000 30.56833  ? 195 ALA A O   1 
ATOM   1555 C  CB  . ALA A 1 196 ? 51.48706 46.43953 85.93943  1.000 22.90204  ? 195 ALA A CB  1 
ATOM   1556 N  N   . CYS A 1 197 ? 49.87249 48.13795 88.31644  1.000 21.04001  ? 196 CYS A N   1 
ATOM   1557 C  CA  . CYS A 1 197 ? 48.58280 48.56583 88.85477  1.000 23.42216  ? 196 CYS A CA  1 
ATOM   1558 C  C   . CYS A 1 197 ? 48.47793 50.08059 88.92350  1.000 29.13881  ? 196 CYS A C   1 
ATOM   1559 O  O   . CYS A 1 197 ? 47.42511 50.64839 88.61208  1.000 41.59967  ? 196 CYS A O   1 
ATOM   1560 C  CB  . CYS A 1 197 ? 48.37858 47.98812 90.24961  1.000 24.47475  ? 196 CYS A CB  1 
ATOM   1561 S  SG  . CYS A 1 197 ? 48.19994 46.22406 90.28389  1.000 22.41972  ? 196 CYS A SG  1 
ATOM   1562 N  N   . LYS A 1 198 ? 49.54055 50.74940 89.35644  1.000 33.91926  ? 197 LYS A N   1 
ATOM   1563 C  CA  . LYS A 1 198 ? 49.52692 52.20065 89.41748  1.000 37.66829  ? 197 LYS A CA  1 
ATOM   1564 C  C   . LYS A 1 198 ? 49.84394 52.77377 88.04348  1.000 51.51770  ? 197 LYS A C   1 
ATOM   1565 O  O   . LYS A 1 198 ? 50.54228 52.15667 87.23386  1.000 45.45619  ? 197 LYS A O   1 
ATOM   1566 C  CB  . LYS A 1 198 ? 50.52092 52.70310 90.46429  1.000 38.80230  ? 197 LYS A CB  1 
ATOM   1567 C  CG  . LYS A 1 198 ? 50.38220 51.99927 91.80839  1.000 37.64414  ? 197 LYS A CG  1 
ATOM   1568 C  CD  . LYS A 1 198 ? 50.98192 52.81716 92.93985  1.000 37.05217  ? 197 LYS A CD  1 
ATOM   1569 C  CE  . LYS A 1 198 ? 52.47015 53.03153 92.73824  1.000 41.21986  ? 197 LYS A CE  1 
ATOM   1570 N  NZ  . LYS A 1 198 ? 53.08647 53.78166 93.87151  1.000 41.07804  ? 197 LYS A NZ  1 
ATOM   1571 N  N   . LYS A 1 199 ? 49.31035 53.95825 87.77555  1.000 63.99021  ? 198 LYS A N   1 
ATOM   1572 C  CA  . LYS A 1 199 ? 49.48022 54.54755 86.45807  1.000 79.91896  ? 198 LYS A CA  1 
ATOM   1573 C  C   . LYS A 1 199 ? 50.22730 55.87397 86.55510  1.000 93.79064  ? 198 LYS A C   1 
ATOM   1574 O  O   . LYS A 1 199 ? 50.20924 56.53628 87.59365  1.000 88.35689  ? 198 LYS A O   1 
ATOM   1575 C  CB  . LYS A 1 199 ? 48.11487 54.74957 85.80087  1.000 69.20379  ? 198 LYS A CB  1 
ATOM   1576 C  CG  . LYS A 1 199 ? 48.13969 54.67307 84.28723  1.000 84.18144  ? 198 LYS A CG  1 
ATOM   1577 C  CD  . LYS A 1 199 ? 48.39641 53.23498 83.85155  1.000 80.92812  ? 198 LYS A CD  1 
ATOM   1578 C  CE  . LYS A 1 199 ? 48.29558 53.06680 82.34546  1.000 76.99941  ? 198 LYS A CE  1 
ATOM   1579 N  NZ  . LYS A 1 199 ? 48.43730 51.63808 81.94693  1.000 78.81703  ? 198 LYS A NZ  1 
ATOM   1580 O  OXT . LYS A 1 199 ? 50.87059 56.31184 85.60062  1.000 89.74822  ? 198 LYS A OXT 1 
ATOM   1581 N  N   . MET B 1 1   ? 22.57781 32.58151 70.37763  1.000 56.04595  ? 0   MET B N   1 
ATOM   1582 C  CA  . MET B 1 1   ? 21.18606 32.38097 70.76814  1.000 58.23138  ? 0   MET B CA  1 
ATOM   1583 C  C   . MET B 1 1   ? 20.71898 33.38861 71.80946  1.000 53.53763  ? 0   MET B C   1 
ATOM   1584 O  O   . MET B 1 1   ? 21.38349 33.60137 72.82483  1.000 45.98197  ? 0   MET B O   1 
ATOM   1585 C  CB  . MET B 1 1   ? 20.97446 30.96640 71.30905  1.000 54.77974  ? 0   MET B CB  1 
ATOM   1586 C  CG  . MET B 1 1   ? 19.60918 30.76167 71.94924  1.000 48.98659  ? 0   MET B CG  1 
ATOM   1587 S  SD  . MET B 1 1   ? 19.31360 29.05974 72.45340  1.000 79.81420  ? 0   MET B SD  1 
ATOM   1588 C  CE  . MET B 1 1   ? 19.72060 28.20153 70.93507  1.000 60.67328  ? 0   MET B CE  1 
ATOM   1589 N  N   . LYS B 1 2   ? 19.56183 33.99712 71.56806  1.000 42.69544  ? 1   LYS B N   1 
ATOM   1590 C  CA  . LYS B 1 2   ? 18.98249 34.93712 72.51272  1.000 34.56883  ? 1   LYS B CA  1 
ATOM   1591 C  C   . LYS B 1 2   ? 17.85550 34.22798 73.25032  1.000 37.12582  ? 1   LYS B C   1 
ATOM   1592 O  O   . LYS B 1 2   ? 16.89073 33.76637 72.62981  1.000 38.76344  ? 1   LYS B O   1 
ATOM   1593 C  CB  . LYS B 1 2   ? 18.44039 36.16457 71.77980  1.000 31.27606  ? 1   LYS B CB  1 
ATOM   1594 C  CG  . LYS B 1 2   ? 17.85352 37.22069 72.69849  1.000 34.85287  ? 1   LYS B CG  1 
ATOM   1595 C  CD  . LYS B 1 2   ? 17.33438 38.41519 71.92014  1.000 35.99236  ? 1   LYS B CD  1 
ATOM   1596 C  CE  . LYS B 1 2   ? 16.76343 39.46956 72.85742  1.000 35.34028  ? 1   LYS B CE  1 
ATOM   1597 N  NZ  . LYS B 1 2   ? 16.41720 40.72653 72.13491  1.000 37.99035  ? 1   LYS B NZ  1 
ATOM   1598 N  N   . HIS B 1 3   ? 17.97660 34.15784 74.57054  1.000 15.87319  ? 2   HIS B N   1 
ATOM   1599 C  CA  . HIS B 1 3   ? 16.91192 33.62963 75.40544  1.000 15.54200  ? 2   HIS B CA  1 
ATOM   1600 C  C   . HIS B 1 3   ? 15.73434 34.58933 75.44199  1.000 16.22974  ? 2   HIS B C   1 
ATOM   1601 O  O   . HIS B 1 3   ? 15.88572 35.80501 75.30306  1.000 15.76733  ? 2   HIS B O   1 
ATOM   1602 C  CB  . HIS B 1 3   ? 17.42997 33.36775 76.81421  1.000 17.28098  ? 2   HIS B CB  1 
ATOM   1603 C  CG  . HIS B 1 3   ? 18.59181 32.42730 76.85031  1.000 14.69686  ? 2   HIS B CG  1 
ATOM   1604 N  ND1 . HIS B 1 3   ? 18.43964 31.06044 76.76646  1.000 15.62023  ? 2   HIS B ND1 1 
ATOM   1605 C  CD2 . HIS B 1 3   ? 19.92532 32.65613 76.90845  1.000 16.16257  ? 2   HIS B CD2 1 
ATOM   1606 C  CE1 . HIS B 1 3   ? 19.62800 30.48482 76.80339  1.000 17.58066  ? 2   HIS B CE1 1 
ATOM   1607 N  NE2 . HIS B 1 3   ? 20.54600 31.43073 76.88894  1.000 16.83264  ? 2   HIS B NE2 1 
ATOM   1608 N  N   . SER B 1 4   ? 14.54844 34.02635 75.62202  1.000 17.76848  ? 3   SER B N   1 
ATOM   1609 C  CA  . SER B 1 4   ? 13.32175 34.80136 75.59079  1.000 19.70254  ? 3   SER B CA  1 
ATOM   1610 C  C   . SER B 1 4   ? 12.44721 34.42002 76.77336  1.000 14.39199  ? 3   SER B C   1 
ATOM   1611 O  O   . SER B 1 4   ? 12.44581 33.27092 77.22184  1.000 15.83838  ? 3   SER B O   1 
ATOM   1612 C  CB  . SER B 1 4   ? 12.55138 34.57052 74.28372  1.000 23.31417  ? 3   SER B CB  1 
ATOM   1613 O  OG  . SER B 1 4   ? 13.25142 35.13439 73.18648  1.000 32.16089  ? 3   SER B OG  1 
ATOM   1614 N  N   . LEU B 1 5   ? 11.71076 35.39568 77.27328  1.000 15.15505  ? 4   LEU B N   1 
ATOM   1615 C  CA  . LEU B 1 5   ? 10.77414 35.15052 78.36195  1.000 13.28450  ? 4   LEU B CA  1 
ATOM   1616 C  C   . LEU B 1 5   ? 9.60434  34.33946 77.82483  1.000 13.27744  ? 4   LEU B C   1 
ATOM   1617 O  O   . LEU B 1 5   ? 8.87759  34.82862 76.94914  1.000 17.04541  ? 4   LEU B O   1 
ATOM   1618 C  CB  . LEU B 1 5   ? 10.26872 36.48124 78.91100  1.000 13.98352  ? 4   LEU B CB  1 
ATOM   1619 C  CG  . LEU B 1 5   ? 9.26280  36.37624 80.05949  1.000 15.23880  ? 4   LEU B CG  1 
ATOM   1620 C  CD1 . LEU B 1 5   ? 9.96038  35.79881 81.28303  1.000 15.52183  ? 4   LEU B CD1 1 
ATOM   1621 C  CD2 . LEU B 1 5   ? 8.63354  37.73732 80.36738  1.000 18.76355  ? 4   LEU B CD2 1 
ATOM   1622 N  N   . PRO B 1 6   ? 9.36640  33.12995 78.31819  1.000 12.69202  ? 5   PRO B N   1 
ATOM   1623 C  CA  . PRO B 1 6   ? 8.23292  32.35445 77.80897  1.000 13.27330  ? 5   PRO B CA  1 
ATOM   1624 C  C   . PRO B 1 6   ? 6.92462  32.96840 78.26496  1.000 15.18646  ? 5   PRO B C   1 
ATOM   1625 O  O   . PRO B 1 6   ? 6.83150  33.55236 79.34652  1.000 14.57907  ? 5   PRO B O   1 
ATOM   1626 C  CB  . PRO B 1 6   ? 8.43536  30.97497 78.44304  1.000 16.86271  ? 5   PRO B CB  1 
ATOM   1627 C  CG  . PRO B 1 6   ? 9.14613  31.26360 79.71755  1.000 17.56727  ? 5   PRO B CG  1 
ATOM   1628 C  CD  . PRO B 1 6   ? 10.06430 32.42981 79.41211  1.000 15.71765  ? 5   PRO B CD  1 
ATOM   1629 N  N   . ASP B 1 7   ? 5.91647  32.86526 77.40438  1.000 14.57642  ? 6   ASP B N   1 
ATOM   1630 C  CA  . ASP B 1 7   ? 4.57391  33.24319 77.81506  1.000 16.26896  ? 6   ASP B CA  1 
ATOM   1631 C  C   . ASP B 1 7   ? 4.15537  32.36323 78.98475  1.000 12.75857  ? 6   ASP B C   1 
ATOM   1632 O  O   . ASP B 1 7   ? 4.49643  31.17988 79.04542  1.000 15.45719  ? 6   ASP B O   1 
ATOM   1633 C  CB  . ASP B 1 7   ? 3.58914  32.98633 76.67285  1.000 15.75532  ? 6   ASP B CB  1 
ATOM   1634 C  CG  . ASP B 1 7   ? 3.68859  34.00127 75.55100  1.000 17.77203  ? 6   ASP B CG  1 
ATOM   1635 O  OD1 . ASP B 1 7   ? 4.42228  35.00080 75.67973  1.000 19.38009  ? 6   ASP B OD1 1 
ATOM   1636 O  OD2 . ASP B 1 7   ? 3.00759  33.78401 74.52507  1.000 19.36245  ? 6   ASP B OD2 1 
ATOM   1637 N  N   . LEU B 1 8   ? 3.39696  32.94008 79.90611  1.000 13.65557  ? 7   LEU B N   1 
ATOM   1638 C  CA  . LEU B 1 8   ? 2.78376  32.14723 80.95745  1.000 17.03889  ? 7   LEU B CA  1 
ATOM   1639 C  C   . LEU B 1 8   ? 1.68983  31.26559 80.35189  1.000 17.01052  ? 7   LEU B C   1 
ATOM   1640 O  O   . LEU B 1 8   ? 0.99354  31.69200 79.42386  1.000 17.81390  ? 7   LEU B O   1 
ATOM   1641 C  CB  . LEU B 1 8   ? 2.19876  33.07704 82.01815  1.000 20.70219  ? 7   LEU B CB  1 
ATOM   1642 C  CG  . LEU B 1 8   ? 1.99912  32.55734 83.43918  1.000 20.41907  ? 7   LEU B CG  1 
ATOM   1643 C  CD1 . LEU B 1 8   ? 3.33556  32.17387 84.05748  1.000 19.08836  ? 7   LEU B CD1 1 
ATOM   1644 C  CD2 . LEU B 1 8   ? 1.32381  33.62623 84.27447  1.000 17.53980  ? 7   LEU B CD2 1 
ATOM   1645 N  N   . PRO B 1 9   ? 1.54064  30.02069 80.81136  1.000 15.76763  ? 8   PRO B N   1 
ATOM   1646 C  CA  . PRO B 1 9   ? 0.54189  29.12887 80.20520  1.000 17.23328  ? 8   PRO B CA  1 
ATOM   1647 C  C   . PRO B 1 9   ? -0.89310 29.44417 80.59942  1.000 13.71461  ? 8   PRO B C   1 
ATOM   1648 O  O   . PRO B 1 9   ? -1.80313 28.72231 80.17765  1.000 18.33536  ? 8   PRO B O   1 
ATOM   1649 C  CB  . PRO B 1 9   ? 0.93542  27.73930 80.74946  1.000 19.00306  ? 8   PRO B CB  1 
ATOM   1650 C  CG  . PRO B 1 9   ? 2.27897  27.91051 81.41650  1.000 19.39866  ? 8   PRO B CG  1 
ATOM   1651 C  CD  . PRO B 1 9   ? 2.33699  29.34053 81.84570  1.000 17.64044  ? 8   PRO B CD  1 
ATOM   1652 N  N   . TYR B 1 10  ? -1.12316 30.50650 81.36269  1.000 13.76491  ? 9   TYR B N   1 
ATOM   1653 C  CA  . TYR B 1 10  ? -2.44749 30.85520 81.85689  1.000 16.03003  ? 9   TYR B CA  1 
ATOM   1654 C  C   . TYR B 1 10  ? -2.41559 32.32735 82.22199  1.000 16.02987  ? 9   TYR B C   1 
ATOM   1655 O  O   . TYR B 1 10  ? -1.36455 32.97199 82.20857  1.000 14.08262  ? 9   TYR B O   1 
ATOM   1656 C  CB  . TYR B 1 10  ? -2.82232 30.01753 83.08493  1.000 15.60379  ? 9   TYR B CB  1 
ATOM   1657 C  CG  . TYR B 1 10  ? -1.62024 29.73889 83.94494  1.000 15.09068  ? 9   TYR B CG  1 
ATOM   1658 C  CD1 . TYR B 1 10  ? -1.09661 30.72060 84.77902  1.000 14.49995  ? 9   TYR B CD1 1 
ATOM   1659 C  CD2 . TYR B 1 10  ? -0.97820 28.51267 83.88651  1.000 15.99503  ? 9   TYR B CD2 1 
ATOM   1660 C  CE1 . TYR B 1 10  ? 0.04269  30.48086 85.54309  1.000 14.41776  ? 9   TYR B CE1 1 
ATOM   1661 C  CE2 . TYR B 1 10  ? 0.15144  28.26234 84.64239  1.000 14.92562  ? 9   TYR B CE2 1 
ATOM   1662 C  CZ  . TYR B 1 10  ? 0.65020  29.24538 85.47046  1.000 16.25825  ? 9   TYR B CZ  1 
ATOM   1663 O  OH  . TYR B 1 10  ? 1.78014  28.98834 86.21346  1.000 14.28887  ? 9   TYR B OH  1 
ATOM   1664 N  N   . ASP B 1 11  ? -3.59178 32.83692 82.55766  1.000 17.40316  ? 10  ASP B N   1 
ATOM   1665 C  CA  . ASP B 1 11  ? -3.78053 34.20810 82.98875  1.000 18.55623  ? 10  ASP B CA  1 
ATOM   1666 C  C   . ASP B 1 11  ? -3.07211 34.45085 84.32415  1.000 14.91886  ? 10  ASP B C   1 
ATOM   1667 O  O   . ASP B 1 11  ? -2.93789 33.54308 85.14599  1.000 16.40547  ? 10  ASP B O   1 
ATOM   1668 C  CB  . ASP B 1 11  ? -5.28565 34.38964 83.17785  1.000 18.66479  ? 10  ASP B CB  1 
ATOM   1669 C  CG  . ASP B 1 11  ? -5.67003 35.79165 83.48904  1.000 24.09577  ? 10  ASP B CG  1 
ATOM   1670 O  OD1 . ASP B 1 11  ? -5.69558 36.61548 82.55513  1.000 24.95401  ? 10  ASP B OD1 1 
ATOM   1671 O  OD2 . ASP B 1 11  ? -5.93171 36.06744 84.67605  1.000 22.85046  ? 10  ASP B OD2 1 
ATOM   1672 N  N   . TYR B 1 12  ? -2.64456 35.70348 84.55405  1.000 13.92584  ? 11  TYR B N   1 
ATOM   1673 C  CA  . TYR B 1 12  ? -1.97015 36.04115 85.81107  1.000 14.83361  ? 11  TYR B CA  1 
ATOM   1674 C  C   . TYR B 1 12  ? -2.83232 35.73902 87.02933  1.000 16.80782  ? 11  TYR B C   1 
ATOM   1675 O  O   . TYR B 1 12  ? -2.29859 35.46782 88.11015  1.000 15.77415  ? 11  TYR B O   1 
ATOM   1676 C  CB  . TYR B 1 12  ? -1.54756 37.50945 85.84043  1.000 15.17873  ? 11  TYR B CB  1 
ATOM   1677 C  CG  . TYR B 1 12  ? -0.33306 37.82401 85.00808  1.000 14.91358  ? 11  TYR B CG  1 
ATOM   1678 C  CD1 . TYR B 1 12  ? 0.77218  36.98195 84.99510  1.000 15.56016  ? 11  TYR B CD1 1 
ATOM   1679 C  CD2 . TYR B 1 12  ? -0.29901 38.96066 84.21684  1.000 13.65974  ? 11  TYR B CD2 1 
ATOM   1680 C  CE1 . TYR B 1 12  ? 1.88078  37.27353 84.21950  1.000 14.05108  ? 11  TYR B CE1 1 
ATOM   1681 C  CE2 . TYR B 1 12  ? 0.80512  39.26076 83.43926  1.000 14.98828  ? 11  TYR B CE2 1 
ATOM   1682 C  CZ  . TYR B 1 12  ? 1.89259  38.41410 83.44162  1.000 15.03433  ? 11  TYR B CZ  1 
ATOM   1683 O  OH  . TYR B 1 12  ? 2.98532  38.71570 82.66008  1.000 14.51468  ? 11  TYR B OH  1 
ATOM   1684 N  N   . GLY B 1 13  ? -4.15265 35.79998 86.89152  1.000 15.85125  ? 12  GLY B N   1 
ATOM   1685 C  CA  . GLY B 1 13  ? -5.02976 35.47274 87.99571  1.000 15.07291  ? 12  GLY B CA  1 
ATOM   1686 C  C   . GLY B 1 13  ? -5.51837 34.04153 88.03049  1.000 15.43093  ? 12  GLY B C   1 
ATOM   1687 O  O   . GLY B 1 13  ? -6.39908 33.72498 88.83569  1.000 17.81138  ? 12  GLY B O   1 
ATOM   1688 N  N   . ALA B 1 14  ? -4.95243 33.15461 87.20656  1.000 16.86805  ? 13  ALA B N   1 
ATOM   1689 C  CA  . ALA B 1 14  ? -5.47507 31.79742 87.08282  1.000 14.98479  ? 13  ALA B CA  1 
ATOM   1690 C  C   . ALA B 1 14  ? -5.22751 30.94235 88.31857  1.000 16.89802  ? 13  ALA B C   1 
ATOM   1691 O  O   . ALA B 1 14  ? -5.88758 29.90962 88.48291  1.000 18.54745  ? 13  ALA B O   1 
ATOM   1692 C  CB  . ALA B 1 14  ? -4.88508 31.10901 85.85189  1.000 18.80066  ? 13  ALA B CB  1 
ATOM   1693 N  N   . LEU B 1 15  ? -4.27867 31.32141 89.17101  1.000 15.40427  ? 14  LEU B N   1 
ATOM   1694 C  CA  . LEU B 1 15  ? -3.93374 30.52490 90.34166  1.000 15.71089  ? 14  LEU B CA  1 
ATOM   1695 C  C   . LEU B 1 15  ? -4.54863 31.07016 91.62469  1.000 13.91952  ? 14  LEU B C   1 
ATOM   1696 O  O   . LEU B 1 15  ? -4.23853 30.57611 92.71330  1.000 13.26044  ? 14  LEU B O   1 
ATOM   1697 C  CB  . LEU B 1 15  ? -2.41456 30.37541 90.46318  1.000 13.25982  ? 14  LEU B CB  1 
ATOM   1698 C  CG  . LEU B 1 15  ? -1.70367 29.88826 89.19408  1.000 13.38076  ? 14  LEU B CG  1 
ATOM   1699 C  CD1 . LEU B 1 15  ? -0.23733 29.65709 89.47098  1.000 14.74841  ? 14  LEU B CD1 1 
ATOM   1700 C  CD2 . LEU B 1 15  ? -2.33174 28.62216 88.62558  1.000 14.70731  ? 14  LEU B CD2 1 
ATOM   1701 N  N   . GLU B 1 16  ? -5.42429 32.06434 91.51542  1.000 14.77177  ? 15  GLU B N   1 
ATOM   1702 C  CA  . GLU B 1 16  ? -6.14001 32.57072 92.67098  1.000 14.82625  ? 15  GLU B CA  1 
ATOM   1703 C  C   . GLU B 1 16  ? -7.03140 31.46883 93.24210  1.000 14.69503  ? 15  GLU B C   1 
ATOM   1704 O  O   . GLU B 1 16  ? -7.54448 30.62447 92.49836  1.000 15.31572  ? 15  GLU B O   1 
ATOM   1705 C  CB  . GLU B 1 16  ? -7.03330 33.73356 92.24077  1.000 17.45915  ? 15  GLU B CB  1 
ATOM   1706 C  CG  . GLU B 1 16  ? -6.27675 34.96738 91.79251  1.000 19.58991  ? 15  GLU B CG  1 
ATOM   1707 C  CD  . GLU B 1 16  ? -6.05847 35.94387 92.92191  1.000 18.07999  ? 15  GLU B CD  1 
ATOM   1708 O  OE1 . GLU B 1 16  ? -6.25791 35.53285 94.08428  1.000 20.12084  ? 15  GLU B OE1 1 
ATOM   1709 O  OE2 . GLU B 1 16  ? -5.69947 37.11699 92.65526  1.000 16.88993  ? 15  GLU B OE2 1 
ATOM   1710 N  N   . PRO B 1 17  ? -7.22681 31.44202 94.56963  1.000 14.16832  ? 16  PRO B N   1 
ATOM   1711 C  CA  . PRO B 1 17  ? -6.70388 32.39768 95.54989  1.000 14.73267  ? 16  PRO B CA  1 
ATOM   1712 C  C   . PRO B 1 17  ? -5.34506 31.97333 96.09823  1.000 13.69340  ? 16  PRO B C   1 
ATOM   1713 O  O   . PRO B 1 17  ? -4.78410 32.67229 96.94573  1.000 16.54832  ? 16  PRO B O   1 
ATOM   1714 C  CB  . PRO B 1 17  ? -7.71647 32.29432 96.68125  1.000 14.22216  ? 16  PRO B CB  1 
ATOM   1715 C  CG  . PRO B 1 17  ? -8.09369 30.83063 96.65780  1.000 15.02971  ? 16  PRO B CG  1 
ATOM   1716 C  CD  . PRO B 1 17  ? -8.10334 30.43689 95.20049  1.000 15.44375  ? 16  PRO B CD  1 
ATOM   1717 N  N   . HIS B 1 18  ? -4.81685 30.86036 95.58923  1.000 14.75440  ? 17  HIS B N   1 
ATOM   1718 C  CA  . HIS B 1 18  ? -3.64355 30.23855 96.20236  1.000 13.44986  ? 17  HIS B CA  1 
ATOM   1719 C  C   . HIS B 1 18  ? -2.38637 31.07497 96.00327  1.000 15.62071  ? 17  HIS B C   1 
ATOM   1720 O  O   . HIS B 1 18  ? -1.57555 31.21238 96.92713  1.000 14.78285  ? 17  HIS B O   1 
ATOM   1721 C  CB  . HIS B 1 18  ? -3.49448 28.82585 95.65142  1.000 13.03997  ? 17  HIS B CB  1 
ATOM   1722 C  CG  . HIS B 1 18  ? -4.79011 28.08305 95.63743  1.000 13.89097  ? 17  HIS B CG  1 
ATOM   1723 N  ND1 . HIS B 1 18  ? -5.43078 27.69451 96.79362  1.000 15.60709  ? 17  HIS B ND1 1 
ATOM   1724 C  CD2 . HIS B 1 18  ? -5.59731 27.71686 94.61524  1.000 15.35127  ? 17  HIS B CD2 1 
ATOM   1725 C  CE1 . HIS B 1 18  ? -6.56793 27.09649 96.48293  1.000 11.84586  ? 17  HIS B CE1 1 
ATOM   1726 N  NE2 . HIS B 1 18  ? -6.69730 27.10402 95.16773  1.000 14.47793  ? 17  HIS B NE2 1 
ATOM   1727 N  N   . ILE B 1 19  ? -2.19211 31.61649 94.80587  1.000 15.57791  ? 18  ILE B N   1 
ATOM   1728 C  CA  . ILE B 1 19  ? -1.14285 32.59464 94.54146  1.000 13.99314  ? 18  ILE B CA  1 
ATOM   1729 C  C   . ILE B 1 19  ? -1.82128 33.73501 93.79941  1.000 12.31647  ? 18  ILE B C   1 
ATOM   1730 O  O   . ILE B 1 19  ? -2.37031 33.52509 92.71109  1.000 16.60771  ? 18  ILE B O   1 
ATOM   1731 C  CB  . ILE B 1 19  ? 0.00936  32.01620 93.69836  1.000 13.83755  ? 18  ILE B CB  1 
ATOM   1732 C  CG1 . ILE B 1 19  ? 0.58363  30.73653 94.32280  1.000 12.79799  ? 18  ILE B CG1 1 
ATOM   1733 C  CG2 . ILE B 1 19  ? 1.11204  33.06017 93.54706  1.000 14.36401  ? 18  ILE B CG2 1 
ATOM   1734 C  CD1 . ILE B 1 19  ? 1.59824  30.01036 93.42240  1.000 16.20737  ? 18  ILE B CD1 1 
ATOM   1735 N  N   . ASN B 1 20  ? -1.77932 34.93640 94.37132  1.000 13.63055  ? 19  ASN B N   1 
ATOM   1736 C  CA  . ASN B 1 20  ? -2.62352 35.99905 93.83966  1.000 15.08085  ? 19  ASN B CA  1 
ATOM   1737 C  C   . ASN B 1 20  ? -2.05741 36.57728 92.54128  1.000 15.63009  ? 19  ASN B C   1 
ATOM   1738 O  O   . ASN B 1 20  ? -0.90881 36.33461 92.15910  1.000 15.26237  ? 19  ASN B O   1 
ATOM   1739 C  CB  . ASN B 1 20  ? -2.98019 37.05183 94.90079  1.000 19.67054  ? 19  ASN B CB  1 
ATOM   1740 C  CG  . ASN B 1 20  ? -1.81874 37.95398 95.28716  1.000 17.77067  ? 19  ASN B CG  1 
ATOM   1741 O  OD1 . ASN B 1 20  ? -0.91785 38.22359 94.49404  1.000 18.17562  ? 19  ASN B OD1 1 
ATOM   1742 N  ND2 . ASN B 1 20  ? -1.86362 38.46562 96.51317  1.000 18.86478  ? 19  ASN B ND2 1 
ATOM   1743 N  N   . ALA B 1 21  ? -2.90217 37.34614 91.85323  1.000 16.15878  ? 20  ALA B N   1 
ATOM   1744 C  CA  . ALA B 1 21  ? -2.55708 37.84976 90.52888  1.000 14.51013  ? 20  ALA B CA  1 
ATOM   1745 C  C   . ALA B 1 21  ? -1.43041 38.86731 90.57851  1.000 14.71654  ? 20  ALA B C   1 
ATOM   1746 O  O   . ALA B 1 21  ? -0.62066 38.93333 89.64528  1.000 15.56822  ? 20  ALA B O   1 
ATOM   1747 C  CB  . ALA B 1 21  ? -3.79021 38.46691 89.86699  1.000 15.89827  ? 20  ALA B CB  1 
ATOM   1748 N  N   . GLN B 1 22  ? -1.34746 39.65726 91.64846  1.000 13.70404  ? 21  GLN B N   1 
ATOM   1749 C  CA  . GLN B 1 22  ? -0.25388 40.61801 91.74706  1.000 13.29567  ? 21  GLN B CA  1 
ATOM   1750 C  C   . GLN B 1 22  ? 1.09367  39.91339 91.80339  1.000 13.08893  ? 21  GLN B C   1 
ATOM   1751 O  O   . GLN B 1 22  ? 2.04647  40.32602 91.13048  1.000 13.74836  ? 21  GLN B O   1 
ATOM   1752 C  CB  . GLN B 1 22  ? -0.43808 41.52461 92.96210  1.000 15.63246  ? 21  GLN B CB  1 
ATOM   1753 C  CG  . GLN B 1 22  ? 0.61406  42.61838 93.05892  1.000 18.07968  ? 21  GLN B CG  1 
ATOM   1754 C  CD  . GLN B 1 22  ? 0.42092  43.50797 94.27094  1.000 23.60493  ? 21  GLN B CD  1 
ATOM   1755 O  OE1 . GLN B 1 22  ? -0.24510 43.12655 95.23227  1.000 27.12321  ? 21  GLN B OE1 1 
ATOM   1756 N  NE2 . GLN B 1 22  ? 1.00261  44.69929 94.22964  1.000 28.69270  ? 21  GLN B NE2 1 
ATOM   1757 N  N   . ILE B 1 23  ? 1.18424  38.83474 92.58597  1.000 15.11822  ? 22  ILE B N   1 
ATOM   1758 C  CA  . ILE B 1 23  ? 2.42481  38.06599 92.66301  1.000 13.81757  ? 22  ILE B CA  1 
ATOM   1759 C  C   . ILE B 1 23  ? 2.76641  37.46290 91.30949  1.000 13.70155  ? 22  ILE B C   1 
ATOM   1760 O  O   . ILE B 1 23  ? 3.89654  37.59307 90.82802  1.000 13.22425  ? 22  ILE B O   1 
ATOM   1761 C  CB  . ILE B 1 23  ? 2.33971  36.99249 93.76301  1.000 12.29515  ? 22  ILE B CB  1 
ATOM   1762 C  CG1 . ILE B 1 23  ? 2.32326  37.65797 95.14161  1.000 13.06335  ? 22  ILE B CG1 1 
ATOM   1763 C  CG2 . ILE B 1 23  ? 3.48660  35.98527 93.62308  1.000 13.16018  ? 22  ILE B CG2 1 
ATOM   1764 C  CD1 . ILE B 1 23  ? 2.10647  36.70202 96.29754  1.000 14.12064  ? 22  ILE B CD1 1 
ATOM   1765 N  N   . MET B 1 24  ? 1.80134  36.78619 90.67734  1.000 13.31284  ? 23  MET B N   1 
ATOM   1766 C  CA  . MET B 1 24  ? 2.08716  36.12901 89.40508  1.000 13.22717  ? 23  MET B CA  1 
ATOM   1767 C  C   . MET B 1 24  ? 2.59101  37.12172 88.36632  1.000 13.90768  ? 23  MET B C   1 
ATOM   1768 O  O   . MET B 1 24  ? 3.56332  36.84285 87.65389  1.000 12.25159  ? 23  MET B O   1 
ATOM   1769 C  CB  . MET B 1 24  ? 0.84778  35.39678 88.88807  1.000 13.42387  ? 23  MET B CB  1 
ATOM   1770 C  CG  . MET B 1 24  ? 0.36428  34.24928 89.77804  1.000 14.38242  ? 23  MET B CG  1 
ATOM   1771 S  SD  . MET B 1 24  ? 1.60487  32.95585 90.04067  1.000 14.04851  ? 23  MET B SD  1 
ATOM   1772 C  CE  . MET B 1 24  ? 1.94556  32.42867 88.36743  1.000 15.52872  ? 23  MET B CE  1 
ATOM   1773 N  N   . GLN B 1 25  ? 1.96793  38.29931 88.29288  1.000 13.96629  ? 24  GLN B N   1 
ATOM   1774 C  CA  . GLN B 1 25  ? 2.36744  39.29483 87.30344  1.000 12.47778  ? 24  GLN B CA  1 
ATOM   1775 C  C   . GLN B 1 25  ? 3.76728  39.83095 87.58797  1.000 13.54740  ? 24  GLN B C   1 
ATOM   1776 O  O   . GLN B 1 25  ? 4.59612  39.93618 86.67807  1.000 14.53319  ? 24  GLN B O   1 
ATOM   1777 C  CB  . GLN B 1 25  ? 1.34041  40.42612 87.25110  1.000 13.44894  ? 24  GLN B CB  1 
ATOM   1778 C  CG  . GLN B 1 25  ? 1.72621  41.54645 86.28978  1.000 13.99273  ? 24  GLN B CG  1 
ATOM   1779 C  CD  . GLN B 1 25  ? 0.61041  42.54137 86.05756  1.000 13.98308  ? 24  GLN B CD  1 
ATOM   1780 O  OE1 . GLN B 1 25  ? -0.57144 42.21197 86.17850  1.000 15.79101  ? 24  GLN B OE1 1 
ATOM   1781 N  NE2 . GLN B 1 25  ? 0.98264  43.77505 85.73915  1.000 16.00864  ? 24  GLN B NE2 1 
ATOM   1782 N  N   . LEU B 1 26  ? 4.04778  40.18199 88.84596  1.000 12.10283  ? 25  LEU B N   1 
ATOM   1783 C  CA  . LEU B 1 26  ? 5.39660  40.61511 89.20552  1.000 14.32512  ? 25  LEU B CA  1 
ATOM   1784 C  C   . LEU B 1 26  ? 6.41201  39.51127 88.95858  1.000 13.25341  ? 25  LEU B C   1 
ATOM   1785 O  O   . LEU B 1 26  ? 7.50777  39.76513 88.43553  1.000 12.67849  ? 25  LEU B O   1 
ATOM   1786 C  CB  . LEU B 1 26  ? 5.44667  41.00139 90.68229  1.000 12.85298  ? 25  LEU B CB  1 
ATOM   1787 C  CG  . LEU B 1 26  ? 4.90352  42.37232 91.05015  1.000 15.76369  ? 25  LEU B CG  1 
ATOM   1788 C  CD1 . LEU B 1 26  ? 4.70696  42.46236 92.54598  1.000 17.29385  ? 25  LEU B CD1 1 
ATOM   1789 C  CD2 . LEU B 1 26  ? 5.90121  43.40403 90.57648  1.000 17.37699  ? 25  LEU B CD2 1 
ATOM   1790 N  N   . HIS B 1 27  ? 6.07244  38.28645 89.36079  1.000 13.44286  ? 26  HIS B N   1 
ATOM   1791 C  CA  . HIS B 1 27  ? 7.01638  37.18040 89.29613  1.000 13.16032  ? 26  HIS B CA  1 
ATOM   1792 C  C   . HIS B 1 27  ? 7.42401  36.89802 87.85997  1.000 14.61420  ? 26  HIS B C   1 
ATOM   1793 O  O   . HIS B 1 27  ? 8.60293  36.65776 87.57091  1.000 13.51537  ? 26  HIS B O   1 
ATOM   1794 C  CB  . HIS B 1 27  ? 6.36724  35.95472 89.92759  1.000 13.61345  ? 26  HIS B CB  1 
ATOM   1795 C  CG  . HIS B 1 27  ? 7.34289  34.99515 90.52064  1.000 14.00710  ? 26  HIS B CG  1 
ATOM   1796 N  ND1 . HIS B 1 27  ? 6.94912  33.84022 91.15869  1.000 15.31596  ? 26  HIS B ND1 1 
ATOM   1797 C  CD2 . HIS B 1 27  ? 8.69525  35.02134 90.58301  1.000 14.12999  ? 26  HIS B CD2 1 
ATOM   1798 C  CE1 . HIS B 1 27  ? 8.01836  33.18951 91.58218  1.000 14.14541  ? 26  HIS B CE1 1 
ATOM   1799 N  NE2 . HIS B 1 27  ? 9.09090  33.88688 91.25120  1.000 12.50224  ? 26  HIS B NE2 1 
ATOM   1800 N  N   . HIS B 1 28  ? 6.45992  36.93876 86.94419  1.000 12.00782  ? 27  HIS B N   1 
ATOM   1801 C  CA  . HIS B 1 28  ? 6.72324  36.64560 85.54323  1.000 12.44556  ? 27  HIS B CA  1 
ATOM   1802 C  C   . HIS B 1 28  ? 7.29246  37.85809 84.81656  1.000 13.15141  ? 27  HIS B C   1 
ATOM   1803 O  O   . HIS B 1 28  ? 8.36873  37.77654 84.21181  1.000 13.79180  ? 27  HIS B O   1 
ATOM   1804 C  CB  . HIS B 1 28  ? 5.42711  36.17216 84.88275  1.000 12.78362  ? 27  HIS B CB  1 
ATOM   1805 C  CG  . HIS B 1 28  ? 5.53104  35.96443 83.40451  1.000 13.17146  ? 27  HIS B CG  1 
ATOM   1806 N  ND1 . HIS B 1 28  ? 5.00067  36.84798 82.48764  1.000 13.68624  ? 27  HIS B ND1 1 
ATOM   1807 C  CD2 . HIS B 1 28  ? 6.10987  34.97350 82.68408  1.000 12.90138  ? 27  HIS B CD2 1 
ATOM   1808 C  CE1 . HIS B 1 28  ? 5.24005  36.40337 81.26614  1.000 14.18120  ? 27  HIS B CE1 1 
ATOM   1809 N  NE2 . HIS B 1 28  ? 5.91321  35.26959 81.35790  1.000 14.45574  ? 27  HIS B NE2 1 
ATOM   1810 N  N   . SER B 1 29  ? 6.59711  38.99985 84.88362  1.000 12.43979  ? 28  SER B N   1 
ATOM   1811 C  CA  . SER B 1 29  ? 6.93625  40.13795 84.03695  1.000 12.00137  ? 28  SER B CA  1 
ATOM   1812 C  C   . SER B 1 29  ? 8.09638  40.97012 84.56223  1.000 13.97925  ? 28  SER B C   1 
ATOM   1813 O  O   . SER B 1 29  ? 8.66971  41.74914 83.79324  1.000 13.68366  ? 28  SER B O   1 
ATOM   1814 C  CB  . SER B 1 29  ? 5.71709  41.03726 83.82995  1.000 14.12753  ? 28  SER B CB  1 
ATOM   1815 O  OG  . SER B 1 29  ? 5.43215  41.81977 84.98089  1.000 15.12554  ? 28  SER B OG  1 
ATOM   1816 N  N   . LYS B 1 30  ? 8.42904  40.86584 85.84648  1.000 13.60429  ? 29  LYS B N   1 
ATOM   1817 C  CA  . LYS B 1 30  ? 9.55275  41.60487 86.40793  1.000 14.28197  ? 29  LYS B CA  1 
ATOM   1818 C  C   . LYS B 1 30  ? 10.70846 40.68271 86.77598  1.000 13.28489  ? 29  LYS B C   1 
ATOM   1819 O  O   . LYS B 1 30  ? 11.81143 40.83001 86.24271  1.000 14.99871  ? 29  LYS B O   1 
ATOM   1820 C  CB  . LYS B 1 30  ? 9.11817  42.45021 87.61937  1.000 14.59106  ? 29  LYS B CB  1 
ATOM   1821 C  CG  . LYS B 1 30  ? 8.02797  43.47491 87.33974  1.000 13.66935  ? 29  LYS B CG  1 
ATOM   1822 C  CD  . LYS B 1 30  ? 8.43287  44.50107 86.30057  1.000 20.48750  ? 29  LYS B CD  1 
ATOM   1823 C  CE  . LYS B 1 30  ? 7.34359  45.55889 86.18016  1.000 20.02433  ? 29  LYS B CE  1 
ATOM   1824 N  NZ  . LYS B 1 30  ? 7.68442  46.60414 85.17533  1.000 31.35361  ? 29  LYS B NZ  1 
ATOM   1825 N  N   . HIS B 1 31  ? 10.47883 39.70529 87.65608  1.000 12.47390  ? 30  HIS B N   1 
ATOM   1826 C  CA  . HIS B 1 31  ? 11.58093 38.87426 88.13386  1.000 15.39145  ? 30  HIS B CA  1 
ATOM   1827 C  C   . HIS B 1 31  ? 12.12558 37.97936 87.02615  1.000 12.92737  ? 30  HIS B C   1 
ATOM   1828 O  O   . HIS B 1 31  ? 13.32784 37.99937 86.73771  1.000 13.45989  ? 30  HIS B O   1 
ATOM   1829 C  CB  . HIS B 1 31  ? 11.14266 38.04604 89.34168  1.000 14.07843  ? 30  HIS B CB  1 
ATOM   1830 C  CG  . HIS B 1 31  ? 10.84754 38.86345 90.56126  1.000 13.02555  ? 30  HIS B CG  1 
ATOM   1831 N  ND1 . HIS B 1 31  ? 11.80747 39.16103 91.50531  1.000 16.33079  ? 30  HIS B ND1 1 
ATOM   1832 C  CD2 . HIS B 1 31  ? 9.70114  39.43846 90.99603  1.000 15.41657  ? 30  HIS B CD2 1 
ATOM   1833 C  CE1 . HIS B 1 31  ? 11.26375 39.88662 92.46746  1.000 16.39638  ? 30  HIS B CE1 1 
ATOM   1834 N  NE2 . HIS B 1 31  ? 9.98832  40.07429 92.17924  1.000 14.53990  ? 30  HIS B NE2 1 
ATOM   1835 N  N   . HIS B 1 32  ? 11.25831 37.19002 86.38554  1.000 13.15550  ? 31  HIS B N   1 
ATOM   1836 C  CA  . HIS B 1 32  ? 11.73541 36.30769 85.32457  1.000 12.68278  ? 31  HIS B CA  1 
ATOM   1837 C  C   . HIS B 1 32  ? 12.26882 37.10714 84.14008  1.000 13.13710  ? 31  HIS B C   1 
ATOM   1838 O  O   . HIS B 1 32  ? 13.32754 36.78053 83.59058  1.000 12.43960  ? 31  HIS B O   1 
ATOM   1839 C  CB  . HIS B 1 32  ? 10.64498 35.31110 84.91210  1.000 12.31310  ? 31  HIS B CB  1 
ATOM   1840 C  CG  . HIS B 1 32  ? 11.13971 34.20647 84.02978  1.000 14.78780  ? 31  HIS B CG  1 
ATOM   1841 N  ND1 . HIS B 1 32  ? 10.33134 33.17444 83.60544  1.000 13.56390  ? 31  HIS B ND1 1 
ATOM   1842 C  CD2 . HIS B 1 32  ? 12.35915 33.97615 83.48460  1.000 13.46247  ? 31  HIS B CD2 1 
ATOM   1843 C  CE1 . HIS B 1 32  ? 11.02784 32.35753 82.83705  1.000 11.09026  ? 31  HIS B CE1 1 
ATOM   1844 N  NE2 . HIS B 1 32  ? 12.26277 32.82069 82.74835  1.000 13.69559  ? 31  HIS B NE2 1 
ATOM   1845 N  N   . ALA B 1 33  ? 11.57827 38.18326 83.75975  1.000 14.40852  ? 32  ALA B N   1 
ATOM   1846 C  CA  . ALA B 1 33  ? 12.06988 39.01374 82.66476  1.000 13.60052  ? 32  ALA B CA  1 
ATOM   1847 C  C   . ALA B 1 33  ? 13.49164 39.50104 82.92793  1.000 15.72658  ? 32  ALA B C   1 
ATOM   1848 O  O   . ALA B 1 33  ? 14.34056 39.48396 82.02676  1.000 15.93407  ? 32  ALA B O   1 
ATOM   1849 C  CB  . ALA B 1 33  ? 11.13138 40.19864 82.45911  1.000 14.46280  ? 32  ALA B CB  1 
ATOM   1850 N  N   . ALA B 1 34  ? 13.77525 39.92106 84.16330  1.000 12.46638  ? 33  ALA B N   1 
ATOM   1851 C  CA  . ALA B 1 34  ? 15.11251 40.40823 84.49260  1.000 13.48171  ? 33  ALA B CA  1 
ATOM   1852 C  C   . ALA B 1 34  ? 16.15285 39.30455 84.35604  1.000 13.48720  ? 33  ALA B C   1 
ATOM   1853 O  O   . ALA B 1 34  ? 17.27377 39.55396 83.89363  1.000 15.18860  ? 33  ALA B O   1 
ATOM   1854 C  CB  . ALA B 1 34  ? 15.12769 41.01254 85.89600  1.000 16.71040  ? 33  ALA B CB  1 
ATOM   1855 N  N   . PHE B 1 35  ? 15.80869 38.07816 84.76320  1.000 13.80478  ? 34  PHE B N   1 
ATOM   1856 C  CA  . PHE B 1 35  ? 16.73810 36.96514 84.59115  1.000 15.00441  ? 34  PHE B CA  1 
ATOM   1857 C  C   . PHE B 1 35  ? 17.07373 36.76354 83.12227  1.000 14.83591  ? 34  PHE B C   1 
ATOM   1858 O  O   . PHE B 1 35  ? 18.24097 36.57743 82.76566  1.000 14.59613  ? 34  PHE B O   1 
ATOM   1859 C  CB  . PHE B 1 35  ? 16.14538 35.68132 85.17197  1.000 14.74700  ? 34  PHE B CB  1 
ATOM   1860 C  CG  . PHE B 1 35  ? 16.07925 35.66856 86.66728  1.000 13.08921  ? 34  PHE B CG  1 
ATOM   1861 C  CD1 . PHE B 1 35  ? 17.15004 36.10558 87.42688  1.000 17.58897  ? 34  PHE B CD1 1 
ATOM   1862 C  CD2 . PHE B 1 35  ? 14.93362 35.22136 87.31546  1.000 18.70906  ? 34  PHE B CD2 1 
ATOM   1863 C  CE1 . PHE B 1 35  ? 17.08686 36.09649 88.80483  1.000 23.15195  ? 34  PHE B CE1 1 
ATOM   1864 C  CE2 . PHE B 1 35  ? 14.86707 35.21531 88.69755  1.000 17.60491  ? 34  PHE B CE2 1 
ATOM   1865 C  CZ  . PHE B 1 35  ? 15.94764 35.65284 89.43521  1.000 22.13357  ? 34  PHE B CZ  1 
ATOM   1866 N  N   . VAL B 1 36  ? 16.06252 36.80885 82.25308  1.000 17.25154  ? 35  VAL B N   1 
ATOM   1867 C  CA  . VAL B 1 36  ? 16.29713 36.63349 80.82170  1.000 14.19623  ? 35  VAL B CA  1 
ATOM   1868 C  C   . VAL B 1 36  ? 17.20198 37.73528 80.29529  1.000 16.10010  ? 35  VAL B C   1 
ATOM   1869 O  O   . VAL B 1 36  ? 18.19028 37.47507 79.60096  1.000 13.58103  ? 35  VAL B O   1 
ATOM   1870 C  CB  . VAL B 1 36  ? 14.96350 36.60785 80.05485  1.000 15.45250  ? 35  VAL B CB  1 
ATOM   1871 C  CG1 . VAL B 1 36  ? 15.23300 36.57724 78.54943  1.000 16.85405  ? 35  VAL B CG1 1 
ATOM   1872 C  CG2 . VAL B 1 36  ? 14.12108 35.41387 80.48017  1.000 16.85190  ? 35  VAL B CG2 1 
ATOM   1873 N  N   . ASN B 1 37  ? 16.86567 38.98556 80.61183  1.000 15.34321  ? 36  ASN B N   1 
ATOM   1874 C  CA  . ASN B 1 37  ? 17.63415 40.11980 80.11098  1.000 14.34906  ? 36  ASN B CA  1 
ATOM   1875 C  C   . ASN B 1 37  ? 19.08150 40.04645 80.58030  1.000 15.04894  ? 36  ASN B C   1 
ATOM   1876 O  O   . ASN B 1 37  ? 20.01365 40.25157 79.79337  1.000 16.12163  ? 36  ASN B O   1 
ATOM   1877 C  CB  . ASN B 1 37  ? 16.98264 41.41598 80.59927  1.000 16.19310  ? 36  ASN B CB  1 
ATOM   1878 C  CG  . ASN B 1 37  ? 15.60263 41.64204 79.99275  1.000 25.96766  ? 36  ASN B CG  1 
ATOM   1879 O  OD1 . ASN B 1 37  ? 15.24270 41.02916 78.98659  1.000 30.23496  ? 36  ASN B OD1 1 
ATOM   1880 N  ND2 . ASN B 1 37  ? 14.81076 42.49642 80.63093  1.000 20.28882  ? 36  ASN B ND2 1 
ATOM   1881 N  N   . ASN B 1 38  ? 19.28805 39.76205 81.86837  1.000 13.98024  ? 37  ASN B N   1 
ATOM   1882 C  CA  . ASN B 1 38  ? 20.64335 39.69745 82.40655  1.000 13.80807  ? 37  ASN B CA  1 
ATOM   1883 C  C   . ASN B 1 38  ? 21.38680 38.45725 81.93267  1.000 14.28395  ? 37  ASN B C   1 
ATOM   1884 O  O   . ASN B 1 38  ? 22.60726 38.50222 81.75624  1.000 15.26766  ? 37  ASN B O   1 
ATOM   1885 C  CB  . ASN B 1 38  ? 20.61505 39.80215 83.93034  1.000 16.45924  ? 37  ASN B CB  1 
ATOM   1886 C  CG  . ASN B 1 38  ? 20.12724 41.15160 84.40385  1.000 21.45480  ? 37  ASN B CG  1 
ATOM   1887 O  OD1 . ASN B 1 38  ? 20.19709 42.13218 83.66520  1.000 24.60566  ? 37  ASN B OD1 1 
ATOM   1888 N  ND2 . ASN B 1 38  ? 19.61626 41.21006 85.62910  1.000 23.55184  ? 37  ASN B ND2 1 
ATOM   1889 N  N   . LEU B 1 39  ? 20.67655 37.34863 81.71609  1.000 13.84934  ? 38  LEU B N   1 
ATOM   1890 C  CA  . LEU B 1 39  ? 21.30890 36.17078 81.13605  1.000 15.14871  ? 38  LEU B CA  1 
ATOM   1891 C  C   . LEU B 1 39  ? 21.85860 36.47210 79.74853  1.000 12.65341  ? 38  LEU B C   1 
ATOM   1892 O  O   . LEU B 1 39  ? 22.99067 36.09008 79.42237  1.000 14.68356  ? 38  LEU B O   1 
ATOM   1893 C  CB  . LEU B 1 39  ? 20.29862 35.02999 81.07369  1.000 15.40507  ? 38  LEU B CB  1 
ATOM   1894 C  CG  . LEU B 1 39  ? 20.69503 33.81614 80.25217  1.000 12.99481  ? 38  LEU B CG  1 
ATOM   1895 C  CD1 . LEU B 1 39  ? 21.96776 33.19684 80.81977  1.000 15.55803  ? 38  LEU B CD1 1 
ATOM   1896 C  CD2 . LEU B 1 39  ? 19.55152 32.82399 80.26845  1.000 16.71477  ? 38  LEU B CD2 1 
ATOM   1897 N  N   . ASN B 1 40  ? 21.07888 37.16556 78.91805  1.000 14.92931  ? 39  ASN B N   1 
ATOM   1898 C  CA  . ASN B 1 40  ? 21.55093 37.47974 77.57580  1.000 16.98287  ? 39  ASN B CA  1 
ATOM   1899 C  C   . ASN B 1 40  ? 22.77865 38.38257 77.62017  1.000 15.55256  ? 39  ASN B C   1 
ATOM   1900 O  O   . ASN B 1 40  ? 23.73077 38.18050 76.85766  1.000 15.40309  ? 39  ASN B O   1 
ATOM   1901 C  CB  . ASN B 1 40  ? 20.42721 38.10388 76.74452  1.000 15.87268  ? 39  ASN B CB  1 
ATOM   1902 C  CG  . ASN B 1 40  ? 19.39678 37.07956 76.28742  1.000 15.89236  ? 39  ASN B CG  1 
ATOM   1903 O  OD1 . ASN B 1 40  ? 19.72481 35.92599 76.00680  1.000 16.02144  ? 39  ASN B OD1 1 
ATOM   1904 N  ND2 . ASN B 1 40  ? 18.14460 37.51672 76.17190  1.000 18.68128  ? 39  ASN B ND2 1 
ATOM   1905 N  N   . VAL B 1 41  ? 22.78672 39.37049 78.52238  1.000 15.45866  ? 40  VAL B N   1 
ATOM   1906 C  CA  . VAL B 1 41  ? 23.95453 40.24319 78.66019  1.000 13.84196  ? 40  VAL B CA  1 
ATOM   1907 C  C   . VAL B 1 41  ? 25.17304 39.44051 79.09496  1.000 17.75661  ? 40  VAL B C   1 
ATOM   1908 O  O   . VAL B 1 41  ? 26.27401 39.60651 78.55649  1.000 17.18611  ? 40  VAL B O   1 
ATOM   1909 C  CB  . VAL B 1 41  ? 23.66220 41.39448 79.63943  1.000 17.11067  ? 40  VAL B CB  1 
ATOM   1910 C  CG1 . VAL B 1 41  ? 24.94399 42.17423 79.93417  1.000 16.92554  ? 40  VAL B CG1 1 
ATOM   1911 C  CG2 . VAL B 1 41  ? 22.59519 42.31845 79.07932  1.000 18.65533  ? 40  VAL B CG2 1 
ATOM   1912 N  N   . THR B 1 42  ? 24.99240 38.56096 80.08067  1.000 13.96668  ? 41  THR B N   1 
ATOM   1913 C  CA  . THR B 1 42  ? 26.11498 37.78711 80.60286  1.000 13.54088  ? 41  THR B CA  1 
ATOM   1914 C  C   . THR B 1 42  ? 26.65111 36.81580 79.56050  1.000 18.37783  ? 41  THR B C   1 
ATOM   1915 O  O   . THR B 1 42  ? 27.87120 36.66521 79.41420  1.000 15.58652  ? 41  THR B O   1 
ATOM   1916 C  CB  . THR B 1 42  ? 25.69227 37.04789 81.87146  1.000 13.30338  ? 41  THR B CB  1 
ATOM   1917 O  OG1 . THR B 1 42  ? 25.18612 37.98692 82.82749  1.000 16.23286  ? 41  THR B OG1 1 
ATOM   1918 C  CG2 . THR B 1 42  ? 26.87798 36.30620 82.48175  1.000 18.65406  ? 41  THR B CG2 1 
ATOM   1919 N  N   . GLU B 1 43  ? 25.75735 36.15364 78.82263  1.000 14.61232  ? 42  GLU B N   1 
ATOM   1920 C  CA  . GLU B 1 43  ? 26.19077 35.23012 77.78073  1.000 14.25009  ? 42  GLU B CA  1 
ATOM   1921 C  C   . GLU B 1 43  ? 27.02603 35.94004 76.72327  1.000 18.09675  ? 42  GLU B C   1 
ATOM   1922 O  O   . GLU B 1 43  ? 28.04425 35.40485 76.26530  1.000 16.92572  ? 42  GLU B O   1 
ATOM   1923 C  CB  . GLU B 1 43  ? 24.97253 34.55523 77.14899  1.000 19.96002  ? 42  GLU B CB  1 
ATOM   1924 C  CG  . GLU B 1 43  ? 24.55216 33.27350 77.84631  1.000 18.28302  ? 42  GLU B CG  1 
ATOM   1925 C  CD  . GLU B 1 43  ? 23.53616 32.46760 77.05390  1.000 17.07453  ? 42  GLU B CD  1 
ATOM   1926 O  OE1 . GLU B 1 43  ? 23.05879 32.95889 76.00586  1.000 20.58897  ? 42  GLU B OE1 1 
ATOM   1927 O  OE2 . GLU B 1 43  ? 23.21677 31.33857 77.48211  1.000 19.02511  ? 42  GLU B OE2 1 
ATOM   1928 N  N   . GLU B 1 44  ? 26.62222 37.15168 76.33022  1.000 14.73687  ? 43  GLU B N   1 
ATOM   1929 C  CA  . GLU B 1 44  ? 27.39301 37.88780 75.33592  1.000 14.94805  ? 43  GLU B CA  1 
ATOM   1930 C  C   . GLU B 1 44  ? 28.77561 38.23035 75.86968  1.000 15.85378  ? 43  GLU B C   1 
ATOM   1931 O  O   . GLU B 1 44  ? 29.76751 38.14934 75.13645  1.000 17.41813  ? 43  GLU B O   1 
ATOM   1932 C  CB  . GLU B 1 44  ? 26.65175 39.15472 74.90497  1.000 16.76925  ? 43  GLU B CB  1 
ATOM   1933 C  CG  . GLU B 1 44  ? 27.19497 39.78062 73.61615  1.000 19.27649  ? 43  GLU B CG  1 
ATOM   1934 C  CD  . GLU B 1 44  ? 28.40871 40.66632 73.84357  1.000 22.34174  ? 43  GLU B CD  1 
ATOM   1935 O  OE1 . GLU B 1 44  ? 28.58375 41.14578 74.98356  1.000 19.93771  ? 43  GLU B OE1 1 
ATOM   1936 O  OE2 . GLU B 1 44  ? 29.18247 40.87882 72.88262  1.000 22.29209  ? 43  GLU B OE2 1 
ATOM   1937 N  N   . LYS B 1 45  ? 28.85649 38.63665 77.14004  1.000 14.94045  ? 44  LYS B N   1 
ATOM   1938 C  CA  . LYS B 1 45  ? 30.15790 38.88100 77.75636  1.000 18.40175  ? 44  LYS B CA  1 
ATOM   1939 C  C   . LYS B 1 45  ? 31.00045 37.61388 77.77902  1.000 18.57855  ? 44  LYS B C   1 
ATOM   1940 O  O   . LYS B 1 45  ? 32.22465 37.67143 77.61031  1.000 16.79973  ? 44  LYS B O   1 
ATOM   1941 C  CB  . LYS B 1 45  ? 29.97582 39.44454 79.16528  1.000 18.43611  ? 44  LYS B CB  1 
ATOM   1942 C  CG  . LYS B 1 45  ? 29.49119 40.88678 79.19572  1.000 20.35536  ? 44  LYS B CG  1 
ATOM   1943 C  CD  . LYS B 1 45  ? 29.36343 41.39102 80.62651  1.000 27.22127  ? 44  LYS B CD  1 
ATOM   1944 C  CE  . LYS B 1 45  ? 28.83168 42.81351 80.67615  1.000 37.14553  ? 44  LYS B CE  1 
ATOM   1945 N  NZ  . LYS B 1 45  ? 29.75402 43.76871 80.00348  1.000 50.44348  ? 44  LYS B NZ  1 
ATOM   1946 N  N   . TYR B 1 46  ? 30.36554 36.45690 77.98588  1.000 18.46038  ? 45  TYR B N   1 
ATOM   1947 C  CA  A TYR B 1 46  ? 31.12606 35.21585 77.98584  0.610 17.66038  ? 45  TYR B CA  1 
ATOM   1948 C  CA  B TYR B 1 46  ? 31.09101 35.18721 77.96788  0.390 17.69130  ? 45  TYR B CA  1 
ATOM   1949 C  C   . TYR B 1 46  ? 31.65997 34.89553 76.59210  1.000 21.75229  ? 45  TYR B C   1 
ATOM   1950 O  O   . TYR B 1 46  ? 32.79419 34.41945 76.45882  1.000 22.31666  ? 45  TYR B O   1 
ATOM   1951 C  CB  A TYR B 1 46  ? 30.29343 34.07086 78.57452  0.610 17.76701  ? 45  TYR B CB  1 
ATOM   1952 C  CB  B TYR B 1 46  ? 30.16106 34.04567 78.37231  0.390 17.21606  ? 45  TYR B CB  1 
ATOM   1953 C  CG  A TYR B 1 46  ? 31.12887 33.02812 79.28800  0.610 16.87351  ? 45  TYR B CG  1 
ATOM   1954 C  CG  B TYR B 1 46  ? 30.34985 33.63662 79.79597  0.390 15.23148  ? 45  TYR B CG  1 
ATOM   1955 C  CD1 A TYR B 1 46  ? 31.92795 32.16507 78.56874  0.610 16.03190  ? 45  TYR B CD1 1 
ATOM   1956 C  CD1 B TYR B 1 46  ? 31.48541 32.94538 80.18755  0.390 17.55559  ? 45  TYR B CD1 1 
ATOM   1957 C  CD2 A TYR B 1 46  ? 31.12824 32.91597 80.67720  0.610 16.65691  ? 45  TYR B CD2 1 
ATOM   1958 C  CD2 B TYR B 1 46  ? 29.41030 33.96236 80.75712  0.390 16.00377  ? 45  TYR B CD2 1 
ATOM   1959 C  CE1 A TYR B 1 46  ? 32.70559 31.21394 79.19329  0.610 15.55599  ? 45  TYR B CE1 1 
ATOM   1960 C  CE1 B TYR B 1 46  ? 31.67386 32.58040 81.49328  0.390 14.42410  ? 45  TYR B CE1 1 
ATOM   1961 C  CE2 A TYR B 1 46  ? 31.90865 31.95636 81.31909  0.610 15.57017  ? 45  TYR B CE2 1 
ATOM   1962 C  CE2 B TYR B 1 46  ? 29.58527 33.59586 82.06191  0.390 16.01112  ? 45  TYR B CE2 1 
ATOM   1963 C  CZ  A TYR B 1 46  ? 32.69288 31.10340 80.56242  0.610 14.37106  ? 45  TYR B CZ  1 
ATOM   1964 C  CZ  B TYR B 1 46  ? 30.72306 32.91256 82.42582  0.390 12.97486  ? 45  TYR B CZ  1 
ATOM   1965 O  OH  A TYR B 1 46  ? 33.48147 30.12662 81.14479  0.610 13.91251  ? 45  TYR B OH  1 
ATOM   1966 O  OH  B TYR B 1 46  ? 30.90425 32.55010 83.72989  0.390 12.78160  ? 45  TYR B OH  1 
ATOM   1967 N  N   . GLN B 1 47  ? 30.87127 35.15569 75.54877  1.000 19.29221  ? 46  GLN B N   1 
ATOM   1968 C  CA  . GLN B 1 47  ? 31.35891 34.94870 74.19197  1.000 22.47949  ? 46  GLN B CA  1 
ATOM   1969 C  C   . GLN B 1 47  ? 32.60585 35.78472 73.93271  1.000 20.77674  ? 46  GLN B C   1 
ATOM   1970 O  O   . GLN B 1 47  ? 33.59231 35.29156 73.36703  1.000 19.92974  ? 46  GLN B O   1 
ATOM   1971 C  CB  . GLN B 1 47  ? 30.25754 35.29571 73.19134  1.000 23.16657  ? 46  GLN B CB  1 
ATOM   1972 C  CG  . GLN B 1 47  ? 30.63465 35.01213 71.75603  1.000 31.26661  ? 46  GLN B CG  1 
ATOM   1973 C  CD  . GLN B 1 47  ? 31.07564 33.57589 71.56396  1.000 46.56382  ? 46  GLN B CD  1 
ATOM   1974 O  OE1 . GLN B 1 47  ? 30.25320 32.66080 71.53791  1.000 37.99475  ? 46  GLN B OE1 1 
ATOM   1975 N  NE2 . GLN B 1 47  ? 32.38406 33.36941 71.43701  1.000 43.04117  ? 46  GLN B NE2 1 
ATOM   1976 N  N   . GLU B 1 48  ? 32.59231 37.04305 74.37378  1.000 15.72831  ? 47  GLU B N   1 
ATOM   1977 C  CA  . GLU B 1 48  ? 33.76238 37.89726 74.21124  1.000 20.15372  ? 47  GLU B CA  1 
ATOM   1978 C  C   . GLU B 1 48  ? 34.95078 37.36496 75.00270  1.000 20.79809  ? 47  GLU B C   1 
ATOM   1979 O  O   . GLU B 1 48  ? 36.07801 37.33260 74.49490  1.000 20.25504  ? 47  GLU B O   1 
ATOM   1980 C  CB  . GLU B 1 48  ? 33.43012 39.33006 74.62840  1.000 20.97842  ? 47  GLU B CB  1 
ATOM   1981 C  CG  . GLU B 1 48  ? 32.43450 40.03218 73.70480  1.000 29.85011  ? 47  GLU B CG  1 
ATOM   1982 C  CD  . GLU B 1 48  ? 32.32850 41.52282 73.97315  1.000 54.41702  ? 47  GLU B CD  1 
ATOM   1983 O  OE1 . GLU B 1 48  ? 32.86072 41.98403 75.00608  1.000 53.65284  ? 47  GLU B OE1 1 
ATOM   1984 O  OE2 . GLU B 1 48  ? 31.71259 42.23569 73.14927  1.000 51.28324  ? 47  GLU B OE2 1 
ATOM   1985 N  N   . ALA B 1 49  ? 34.72099 36.94065 76.24802  1.000 17.40159  ? 48  ALA B N   1 
ATOM   1986 C  CA  . ALA B 1 49  ? 35.82188 36.43245 77.06321  1.000 16.54739  ? 48  ALA B CA  1 
ATOM   1987 C  C   . ALA B 1 49  ? 36.40308 35.14840 76.48275  1.000 21.77257  ? 48  ALA B C   1 
ATOM   1988 O  O   . ALA B 1 49  ? 37.62502 34.95592 76.49682  1.000 19.59520  ? 48  ALA B O   1 
ATOM   1989 C  CB  . ALA B 1 49  ? 35.35505 36.21977 78.50323  1.000 18.47529  ? 48  ALA B CB  1 
ATOM   1990 N  N   . LEU B 1 50  ? 35.54661 34.26232 75.96418  1.000 20.29464  ? 49  LEU B N   1 
ATOM   1991 C  CA  . LEU B 1 50  ? 36.02472 33.01692 75.36751  1.000 20.86918  ? 49  LEU B CA  1 
ATOM   1992 C  C   . LEU B 1 50  ? 36.89935 33.27979 74.15079  1.000 23.52333  ? 49  LEU B C   1 
ATOM   1993 O  O   . LEU B 1 50  ? 37.94820 32.64347 73.97999  1.000 22.16846  ? 49  LEU B O   1 
ATOM   1994 C  CB  . LEU B 1 50  ? 34.83983 32.14171 74.96423  1.000 19.56667  ? 49  LEU B CB  1 
ATOM   1995 C  CG  . LEU B 1 50  ? 34.25116 31.24156 76.04337  1.000 28.46934  ? 49  LEU B CG  1 
ATOM   1996 C  CD1 . LEU B 1 50  ? 32.93205 30.66341 75.56538  1.000 30.63913  ? 49  LEU B CD1 1 
ATOM   1997 C  CD2 . LEU B 1 50  ? 35.22949 30.13124 76.39814  1.000 27.93554  ? 49  LEU B CD2 1 
ATOM   1998 N  N   . ALA B 1 51  ? 36.47005 34.19657 73.28041  1.000 21.39173  ? 50  ALA B N   1 
ATOM   1999 C  CA  . ALA B 1 51  ? 37.24040 34.50715 72.08247  1.000 25.71814  ? 50  ALA B CA  1 
ATOM   2000 C  C   . ALA B 1 51  ? 38.60651 35.07676 72.43096  1.000 24.25167  ? 50  ALA B C   1 
ATOM   2001 O  O   . ALA B 1 51  ? 39.58621 34.81086 71.72507  1.000 32.82094  ? 50  ALA B O   1 
ATOM   2002 C  CB  . ALA B 1 51  ? 36.46743 35.49604 71.20622  1.000 25.53737  ? 50  ALA B CB  1 
ATOM   2003 N  N   . LYS B 1 52  ? 38.69348 35.85351 73.51104  1.000 21.60233  ? 51  LYS B N   1 
ATOM   2004 C  CA  . LYS B 1 52  ? 39.95362 36.42679 73.97032  1.000 22.10710  ? 51  LYS B CA  1 
ATOM   2005 C  C   . LYS B 1 52  ? 40.76737 35.47471 74.83877  1.000 20.02035  ? 51  LYS B C   1 
ATOM   2006 O  O   . LYS B 1 52  ? 41.90435 35.80888 75.18907  1.000 25.46270  ? 51  LYS B O   1 
ATOM   2007 C  CB  . LYS B 1 52  ? 39.67575 37.69935 74.77453  1.000 20.03235  ? 51  LYS B CB  1 
ATOM   2008 C  CG  . LYS B 1 52  ? 39.20729 38.88773 73.95322  1.000 27.38234  ? 51  LYS B CG  1 
ATOM   2009 C  CD  . LYS B 1 52  ? 39.01560 40.11418 74.83596  1.000 35.10931  ? 51  LYS B CD  1 
ATOM   2010 C  CE  . LYS B 1 52  ? 38.47858 41.29252 74.03791  1.000 57.00990  ? 51  LYS B CE  1 
ATOM   2011 N  NZ  . LYS B 1 52  ? 38.23490 42.48560 74.89721  1.000 71.14169  ? 51  LYS B NZ  1 
ATOM   2012 N  N   . GLY B 1 53  ? 40.23342 34.30269 75.18078  1.000 19.41194  ? 52  GLY B N   1 
ATOM   2013 C  CA  . GLY B 1 53  ? 40.90491 33.43412 76.13527  1.000 21.45812  ? 52  GLY B CA  1 
ATOM   2014 C  C   . GLY B 1 53  ? 41.06079 34.04689 77.50958  1.000 19.03312  ? 52  GLY B C   1 
ATOM   2015 O  O   . GLY B 1 53  ? 42.02946 33.73880 78.21445  1.000 17.01618  ? 52  GLY B O   1 
ATOM   2016 N  N   . ASP B 1 54  ? 40.14090 34.92663 77.90544  1.000 17.04758  ? 53  ASP B N   1 
ATOM   2017 C  CA  . ASP B 1 54  ? 40.21229 35.61102 79.19656  1.000 17.55747  ? 53  ASP B CA  1 
ATOM   2018 C  C   . ASP B 1 54  ? 39.53005 34.74477 80.24814  1.000 18.19436  ? 53  ASP B C   1 
ATOM   2019 O  O   . ASP B 1 54  ? 38.30554 34.78460 80.40819  1.000 17.00413  ? 53  ASP B O   1 
ATOM   2020 C  CB  . ASP B 1 54  ? 39.58548 36.99827 79.11045  1.000 19.51425  ? 53  ASP B CB  1 
ATOM   2021 C  CG  . ASP B 1 54  ? 39.90562 37.85694 80.31655  1.000 21.23602  ? 53  ASP B CG  1 
ATOM   2022 O  OD1 . ASP B 1 54  ? 40.20322 37.29960 81.39479  1.000 17.80338  ? 53  ASP B OD1 1 
ATOM   2023 O  OD2 . ASP B 1 54  ? 39.87071 39.09919 80.18722  1.000 24.70467  ? 53  ASP B OD2 1 
ATOM   2024 N  N   . VAL B 1 55  ? 40.33496 33.97033 80.97689  1.000 14.07896  ? 54  VAL B N   1 
ATOM   2025 C  CA  . VAL B 1 55  ? 39.80635 33.06643 81.99186  1.000 16.41968  ? 54  VAL B CA  1 
ATOM   2026 C  C   . VAL B 1 55  ? 39.36474 33.83897 83.22751  1.000 14.77090  ? 54  VAL B C   1 
ATOM   2027 O  O   . VAL B 1 55  ? 38.38275 33.47105 83.88489  1.000 13.60597  ? 54  VAL B O   1 
ATOM   2028 C  CB  . VAL B 1 55  ? 40.83834 31.97413 82.32302  1.000 13.99954  ? 54  VAL B CB  1 
ATOM   2029 C  CG1 . VAL B 1 55  ? 40.25314 30.98075 83.31598  1.000 15.31786  ? 54  VAL B CG1 1 
ATOM   2030 C  CG2 . VAL B 1 55  ? 41.24739 31.24608 81.05936  1.000 17.61313  ? 54  VAL B CG2 1 
ATOM   2031 N  N   . THR B 1 56  ? 40.08253 34.90982 83.57403  1.000 14.73452  ? 55  THR B N   1 
ATOM   2032 C  CA  . THR B 1 56  ? 39.66294 35.74257 84.69800  1.000 13.23374  ? 55  THR B CA  1 
ATOM   2033 C  C   . THR B 1 56  ? 38.25742 36.28732 84.46943  1.000 15.48808  ? 55  THR B C   1 
ATOM   2034 O  O   . THR B 1 56  ? 37.39524 36.20378 85.35139  1.000 15.12268  ? 55  THR B O   1 
ATOM   2035 C  CB  . THR B 1 56  ? 40.66670 36.88158 84.90985  1.000 13.82556  ? 55  THR B CB  1 
ATOM   2036 O  OG1 . THR B 1 56  ? 41.89934 36.35211 85.42232  1.000 16.28949  ? 55  THR B OG1 1 
ATOM   2037 C  CG2 . THR B 1 56  ? 40.12596 37.90349 85.89624  1.000 15.42113  ? 55  THR B CG2 1 
ATOM   2038 N  N   . ALA B 1 57  ? 37.99758 36.81735 83.27261  1.000 15.06677  ? 56  ALA B N   1 
ATOM   2039 C  CA  . ALA B 1 57  ? 36.66874 37.34184 82.97485  1.000 17.11080  ? 56  ALA B CA  1 
ATOM   2040 C  C   . ALA B 1 57  ? 35.61785 36.23617 82.99048  1.000 15.71669  ? 56  ALA B C   1 
ATOM   2041 O  O   . ALA B 1 57  ? 34.51475 36.42826 83.51999  1.000 17.04447  ? 56  ALA B O   1 
ATOM   2042 C  CB  . ALA B 1 57  ? 36.67757 38.07108 81.63009  1.000 17.03511  ? 56  ALA B CB  1 
ATOM   2043 N  N   . GLN B 1 58  ? 35.93849 35.06778 82.42660  1.000 16.20987  ? 57  GLN B N   1 
ATOM   2044 C  CA  . GLN B 1 58  ? 34.99371 33.95511 82.47045  1.000 16.91781  ? 57  GLN B CA  1 
ATOM   2045 C  C   . GLN B 1 58  ? 34.59659 33.64589 83.90517  1.000 16.10829  ? 57  GLN B C   1 
ATOM   2046 O  O   . GLN B 1 58  ? 33.41379 33.46154 84.21431  1.000 18.82499  ? 57  GLN B O   1 
ATOM   2047 C  CB  . GLN B 1 58  ? 35.60198 32.71226 81.81829  1.000 14.43574  ? 57  GLN B CB  1 
ATOM   2048 C  CG  . GLN B 1 58  ? 35.73866 32.77042 80.31231  1.000 13.86422  ? 57  GLN B CG  1 
ATOM   2049 C  CD  . GLN B 1 58  ? 36.38095 31.51179 79.75906  1.000 16.12020  ? 57  GLN B CD  1 
ATOM   2050 O  OE1 . GLN B 1 58  ? 35.85024 30.40895 79.90176  1.000 15.36661  ? 57  GLN B OE1 1 
ATOM   2051 N  NE2 . GLN B 1 58  ? 37.54644 31.67073 79.14137  1.000 16.24401  ? 57  GLN B NE2 1 
ATOM   2052 N  N   . ILE B 1 59  ? 35.57835 33.59476 84.80303  1.000 12.66477  ? 58  ILE B N   1 
ATOM   2053 C  CA  . ILE B 1 59  ? 35.28488 33.22715 86.18122  1.000 12.48572  ? 58  ILE B CA  1 
ATOM   2054 C  C   . ILE B 1 59  ? 34.52476 34.34890 86.88871  1.000 12.89755  ? 58  ILE B C   1 
ATOM   2055 O  O   . ILE B 1 59  ? 33.58661 34.09034 87.65140  1.000 11.84864  ? 58  ILE B O   1 
ATOM   2056 C  CB  . ILE B 1 59  ? 36.58308 32.80008 86.89357  1.000 12.36665  ? 58  ILE B CB  1 
ATOM   2057 C  CG1 . ILE B 1 59  ? 37.08652 31.47379 86.30402  1.000 12.62995  ? 58  ILE B CG1 1 
ATOM   2058 C  CG2 . ILE B 1 59  ? 36.38836 32.71408 88.40730  1.000 13.88179  ? 58  ILE B CG2 1 
ATOM   2059 C  CD1 . ILE B 1 59  ? 38.44370 31.04000 86.83151  1.000 12.51704  ? 58  ILE B CD1 1 
ATOM   2060 N  N   . ALA B 1 60  ? 34.87487 35.60918 86.61021  1.000 12.71409  ? 59  ALA B N   1 
ATOM   2061 C  CA  . ALA B 1 60  ? 34.15228 36.72365 87.21684  1.000 11.77160  ? 59  ALA B CA  1 
ATOM   2062 C  C   . ALA B 1 60  ? 32.69305 36.75637 86.78032  1.000 12.70709  ? 59  ALA B C   1 
ATOM   2063 O  O   . ALA B 1 60  ? 31.83751 37.26588 87.51078  1.000 16.22030  ? 59  ALA B O   1 
ATOM   2064 C  CB  . ALA B 1 60  ? 34.83573 38.03862 86.85429  1.000 14.64023  ? 59  ALA B CB  1 
ATOM   2065 N  N   . LEU B 1 61  ? 32.39294 36.22382 85.60023  1.000 12.32152  ? 60  LEU B N   1 
ATOM   2066 C  CA  . LEU B 1 61  ? 31.02657 36.20858 85.09817  1.000 13.90134  ? 60  LEU B CA  1 
ATOM   2067 C  C   . LEU B 1 61  ? 30.20684 35.03677 85.62512  1.000 13.66695  ? 60  LEU B C   1 
ATOM   2068 O  O   . LEU B 1 61  ? 28.98271 35.02910 85.44355  1.000 12.52010  ? 60  LEU B O   1 
ATOM   2069 C  CB  . LEU B 1 61  ? 31.05407 36.17735 83.57114  1.000 13.17302  ? 60  LEU B CB  1 
ATOM   2070 C  CG  . LEU B 1 61  ? 31.50872 37.45893 82.86851  1.000 15.20127  ? 60  LEU B CG  1 
ATOM   2071 C  CD1 . LEU B 1 61  ? 31.87704 37.15640 81.42745  1.000 19.28885  ? 60  LEU B CD1 1 
ATOM   2072 C  CD2 . LEU B 1 61  ? 30.41810 38.52535 82.94030  1.000 17.32156  ? 60  LEU B CD2 1 
ATOM   2073 N  N   . GLN B 1 62  ? 30.83647 34.05908 86.27714  1.000 13.15645  ? 61  GLN B N   1 
ATOM   2074 C  CA  . GLN B 1 62  ? 30.10274 32.88336 86.73649  1.000 11.75241  ? 61  GLN B CA  1 
ATOM   2075 C  C   . GLN B 1 62  ? 28.95301 33.20389 87.68183  1.000 14.37451  ? 61  GLN B C   1 
ATOM   2076 O  O   . GLN B 1 62  ? 27.87202 32.61294 87.50664  1.000 13.13942  ? 61  GLN B O   1 
ATOM   2077 C  CB  . GLN B 1 62  ? 31.05877 31.85584 87.35537  1.000 15.14505  ? 61  GLN B CB  1 
ATOM   2078 C  CG  . GLN B 1 62  ? 31.94250 31.14139 86.35786  1.000 15.84589  ? 61  GLN B CG  1 
ATOM   2079 C  CD  . GLN B 1 62  ? 32.73218 30.01736 86.98945  1.000 15.53645  ? 61  GLN B CD  1 
ATOM   2080 O  OE1 . GLN B 1 62  ? 32.93145 29.98939 88.20293  1.000 18.52502  ? 61  GLN B OE1 1 
ATOM   2081 N  NE2 . GLN B 1 62  ? 33.17161 29.07185 86.16995  1.000 14.52773  ? 61  GLN B NE2 1 
ATOM   2082 N  N   . PRO B 1 63  ? 29.09741 34.07887 88.68769  1.000 12.47109  ? 62  PRO B N   1 
ATOM   2083 C  CA  . PRO B 1 63  ? 27.95190 34.31567 89.57474  1.000 16.99091  ? 62  PRO B CA  1 
ATOM   2084 C  C   . PRO B 1 63  ? 26.74219 34.85462 88.84024  1.000 13.77403  ? 62  PRO B C   1 
ATOM   2085 O  O   . PRO B 1 63  ? 25.62063 34.40813 89.10538  1.000 15.64872  ? 62  PRO B O   1 
ATOM   2086 C  CB  . PRO B 1 63  ? 28.50824 35.27803 90.63120  1.000 13.75472  ? 62  PRO B CB  1 
ATOM   2087 C  CG  . PRO B 1 63  ? 29.98117 34.99937 90.64019  1.000 15.60319  ? 62  PRO B CG  1 
ATOM   2088 C  CD  . PRO B 1 63  ? 30.31850 34.73101 89.20107  1.000 13.95333  ? 62  PRO B CD  1 
ATOM   2089 N  N   . ALA B 1 64  ? 26.93944 35.78108 87.89912  1.000 12.75347  ? 63  ALA B N   1 
ATOM   2090 C  CA  . ALA B 1 64  ? 25.80944 36.30580 87.13976  1.000 13.52561  ? 63  ALA B CA  1 
ATOM   2091 C  C   . ALA B 1 64  ? 25.21562 35.24863 86.22154  1.000 15.43917  ? 63  ALA B C   1 
ATOM   2092 O  O   . ALA B 1 64  ? 23.99596 35.21140 86.02166  1.000 12.99201  ? 63  ALA B O   1 
ATOM   2093 C  CB  . ALA B 1 64  ? 26.23295 37.52956 86.33125  1.000 14.52214  ? 63  ALA B CB  1 
ATOM   2094 N  N   . LEU B 1 65  ? 26.05735 34.38176 85.65451  1.000 12.99404  ? 64  LEU B N   1 
ATOM   2095 C  CA  . LEU B 1 65  ? 25.55254 33.34579 84.76201  1.000 13.74037  ? 64  LEU B CA  1 
ATOM   2096 C  C   . LEU B 1 65  ? 24.70796 32.33619 85.52808  1.000 13.11922  ? 64  LEU B C   1 
ATOM   2097 O  O   . LEU B 1 65  ? 23.61264 31.97152 85.08706  1.000 14.55114  ? 64  LEU B O   1 
ATOM   2098 C  CB  . LEU B 1 65  ? 26.71351 32.65519 84.04262  1.000 14.97159  ? 64  LEU B CB  1 
ATOM   2099 C  CG  . LEU B 1 65  ? 26.40391 31.81042 82.79261  1.000 13.90789  ? 64  LEU B CG  1 
ATOM   2100 C  CD1 . LEU B 1 65  ? 25.81452 30.42058 83.11154  1.000 16.57107  ? 64  LEU B CD1 1 
ATOM   2101 C  CD2 . LEU B 1 65  ? 25.51744 32.56555 81.81472  1.000 18.63785  ? 64  LEU B CD2 1 
ATOM   2102 N  N   . LYS B 1 66  ? 25.20144 31.86906 86.67921  1.000 13.01254  ? 65  LYS B N   1 
ATOM   2103 C  CA  . LYS B 1 66  ? 24.43320 30.89573 87.44612  1.000 13.25326  ? 65  LYS B CA  1 
ATOM   2104 C  C   . LYS B 1 66  ? 23.15942 31.51691 87.99975  1.000 13.80075  ? 65  LYS B C   1 
ATOM   2105 O  O   . LYS B 1 66  ? 22.09517 30.89046 87.97114  1.000 12.80467  ? 65  LYS B O   1 
ATOM   2106 C  CB  . LYS B 1 66  ? 25.27513 30.29951 88.57286  1.000 15.44844  ? 65  LYS B CB  1 
ATOM   2107 C  CG  . LYS B 1 66  ? 24.50212 29.25079 89.37767  1.000 14.79969  ? 65  LYS B CG  1 
ATOM   2108 C  CD  . LYS B 1 66  ? 25.38118 28.45832 90.33694  1.000 16.52594  ? 65  LYS B CD  1 
ATOM   2109 C  CE  . LYS B 1 66  ? 25.93647 29.33523 91.43903  1.000 16.78823  ? 65  LYS B CE  1 
ATOM   2110 N  NZ  . LYS B 1 66  ? 26.39387 28.49984 92.58631  1.000 19.34888  ? 65  LYS B NZ  1 
ATOM   2111 N  N   . PHE B 1 67  ? 23.24317 32.76236 88.46885  1.000 14.49152  ? 66  PHE B N   1 
ATOM   2112 C  CA  . PHE B 1 67  ? 22.08692 33.41720 89.07412  1.000 13.95807  ? 66  PHE B CA  1 
ATOM   2113 C  C   . PHE B 1 67  ? 20.99622 33.68239 88.04193  1.000 12.76986  ? 66  PHE B C   1 
ATOM   2114 O  O   . PHE B 1 67  ? 19.83363 33.30507 88.23791  1.000 12.84756  ? 66  PHE B O   1 
ATOM   2115 C  CB  . PHE B 1 67  ? 22.52913 34.72036 89.73982  1.000 13.35120  ? 66  PHE B CB  1 
ATOM   2116 C  CG  . PHE B 1 67  ? 21.42410 35.44469 90.46404  1.000 13.68294  ? 66  PHE B CG  1 
ATOM   2117 C  CD1 . PHE B 1 67  ? 20.84490 34.89553 91.59278  1.000 13.75130  ? 66  PHE B CD1 1 
ATOM   2118 C  CD2 . PHE B 1 67  ? 20.97311 36.67836 90.01511  1.000 19.25732  ? 66  PHE B CD2 1 
ATOM   2119 C  CE1 . PHE B 1 67  ? 19.83387 35.55731 92.26576  1.000 15.37844  ? 66  PHE B CE1 1 
ATOM   2120 C  CE2 . PHE B 1 67  ? 19.95410 37.34594 90.68066  1.000 19.27995  ? 66  PHE B CE2 1 
ATOM   2121 C  CZ  . PHE B 1 67  ? 19.38364 36.78113 91.80880  1.000 17.22779  ? 66  PHE B CZ  1 
ATOM   2122 N  N   . ASN B 1 68  ? 21.35046 34.32867 86.93232  1.000 12.52866  ? 67  ASN B N   1 
ATOM   2123 C  CA  . ASN B 1 68  ? 20.34073 34.66689 85.93366  1.000 13.87230  ? 67  ASN B CA  1 
ATOM   2124 C  C   . ASN B 1 68  ? 19.98045 33.47358 85.06856  1.000 13.74058  ? 67  ASN B C   1 
ATOM   2125 O  O   . ASN B 1 68  ? 18.80657 33.27696 84.73291  1.000 13.86429  ? 67  ASN B O   1 
ATOM   2126 C  CB  . ASN B 1 68  ? 20.82659 35.82472 85.07329  1.000 14.47195  ? 67  ASN B CB  1 
ATOM   2127 C  CG  . ASN B 1 68  ? 20.92443 37.09683 85.85473  1.000 16.05340  ? 67  ASN B CG  1 
ATOM   2128 O  OD1 . ASN B 1 68  ? 19.91385 37.62599 86.31744  1.000 17.50500  ? 67  ASN B OD1 1 
ATOM   2129 N  ND2 . ASN B 1 68  ? 22.14366 37.58868 86.03843  1.000 17.22563  ? 67  ASN B ND2 1 
ATOM   2130 N  N   . GLY B 1 69  ? 20.97496 32.67047 84.69371  1.000 12.39373  ? 68  GLY B N   1 
ATOM   2131 C  CA  . GLY B 1 69  ? 20.68275 31.45972 83.94701  1.000 15.36832  ? 68  GLY B CA  1 
ATOM   2132 C  C   . GLY B 1 69  ? 19.85174 30.48136 84.75069  1.000 12.71049  ? 68  GLY B C   1 
ATOM   2133 O  O   . GLY B 1 69  ? 18.87835 29.91212 84.24856  1.000 13.97718  ? 68  GLY B O   1 
ATOM   2134 N  N   . GLY B 1 70  ? 20.22779 30.27190 86.01396  1.000 13.00865  ? 69  GLY B N   1 
ATOM   2135 C  CA  . GLY B 1 70  ? 19.41681 29.43583 86.88465  1.000 13.17322  ? 69  GLY B CA  1 
ATOM   2136 C  C   . GLY B 1 70  ? 18.02683 30.00229 87.10707  1.000 12.65111  ? 69  GLY B C   1 
ATOM   2137 O  O   . GLY B 1 70  ? 17.04045 29.26097 87.10250  1.000 14.01304  ? 69  GLY B O   1 
ATOM   2138 N  N   . GLY B 1 71  ? 17.92513 31.32057 87.30607  1.000 14.04001  ? 70  GLY B N   1 
ATOM   2139 C  CA  . GLY B 1 71  ? 16.61038 31.92799 87.44249  1.000 12.19293  ? 70  GLY B CA  1 
ATOM   2140 C  C   . GLY B 1 71  ? 15.73225 31.65667 86.23726  1.000 11.21131  ? 70  GLY B C   1 
ATOM   2141 O  O   . GLY B 1 71  ? 14.54771 31.33736 86.37492  1.000 12.72482  ? 70  GLY B O   1 
ATOM   2142 N  N   . HIS B 1 72  ? 16.31265 31.74681 85.03878  1.000 13.43563  ? 71  HIS B N   1 
ATOM   2143 C  CA  . HIS B 1 72  ? 15.55684 31.46680 83.82275  1.000 12.36521  ? 71  HIS B CA  1 
ATOM   2144 C  C   . HIS B 1 72  ? 15.14221 30.00246 83.75714  1.000 13.73481  ? 71  HIS B C   1 
ATOM   2145 O  O   . HIS B 1 72  ? 13.99048 29.69157 83.42915  1.000 15.31998  ? 71  HIS B O   1 
ATOM   2146 C  CB  . HIS B 1 72  ? 16.41163 31.83554 82.61498  1.000 15.41864  ? 71  HIS B CB  1 
ATOM   2147 C  CG  . HIS B 1 72  ? 15.76119 31.55727 81.29870  1.000 12.71591  ? 71  HIS B CG  1 
ATOM   2148 N  ND1 . HIS B 1 72  ? 14.45869 31.91012 81.01451  1.000 15.55625  ? 71  HIS B ND1 1 
ATOM   2149 C  CD2 . HIS B 1 72  ? 16.24063 30.95438 80.18617  1.000 14.78191  ? 71  HIS B CD2 1 
ATOM   2150 C  CE1 . HIS B 1 72  ? 14.16746 31.54063 79.77986  1.000 16.06291  ? 71  HIS B CE1 1 
ATOM   2151 N  NE2 . HIS B 1 72  ? 15.23225 30.95957 79.25500  1.000 17.24363  ? 71  HIS B NE2 1 
ATOM   2152 N  N   . ILE B 1 73  ? 16.06626 29.09252 84.06679  1.000 12.45534  ? 72  ILE B N   1 
ATOM   2153 C  CA  . ILE B 1 73  ? 15.75278 27.66390 84.06157  1.000 13.20957  ? 72  ILE B CA  1 
ATOM   2154 C  C   . ILE B 1 73  ? 14.64286 27.35956 85.05927  1.000 12.14024  ? 72  ILE B C   1 
ATOM   2155 O  O   . ILE B 1 73  ? 13.65260 26.68778 84.73617  1.000 14.41381  ? 72  ILE B O   1 
ATOM   2156 C  CB  . ILE B 1 73  ? 17.01521 26.84036 84.37999  1.000 12.61768  ? 72  ILE B CB  1 
ATOM   2157 C  CG1 . ILE B 1 73  ? 18.04224 26.93509 83.24882  1.000 13.50283  ? 72  ILE B CG1 1 
ATOM   2158 C  CG2 . ILE B 1 73  ? 16.65239 25.39162 84.68381  1.000 15.50380  ? 72  ILE B CG2 1 
ATOM   2159 C  CD1 . ILE B 1 73  ? 19.42747 26.44420 83.65641  1.000 16.66870  ? 72  ILE B CD1 1 
ATOM   2160 N  N   . ASN B 1 74  ? 14.79592 27.85296 86.29177  1.000 13.66049  ? 73  ASN B N   1 
ATOM   2161 C  CA  . ASN B 1 74  ? 13.89371 27.47343 87.37521  1.000 14.14925  ? 73  ASN B CA  1 
ATOM   2162 C  C   . ASN B 1 74  ? 12.48618 27.98741 87.12626  1.000 12.74889  ? 73  ASN B C   1 
ATOM   2163 O  O   . ASN B 1 74  ? 11.50591 27.25152 87.29419  1.000 12.05311  ? 73  ASN B O   1 
ATOM   2164 C  CB  . ASN B 1 74  ? 14.40955 28.03506 88.69834  1.000 12.33575  ? 73  ASN B CB  1 
ATOM   2165 C  CG  . ASN B 1 74  ? 15.78068 27.51121 89.05789  1.000 10.10772  ? 73  ASN B CG  1 
ATOM   2166 O  OD1 . ASN B 1 74  ? 16.18485 26.44052 88.60853  1.000 12.94305  ? 73  ASN B OD1 1 
ATOM   2167 N  ND2 . ASN B 1 74  ? 16.50837 28.27381 89.87269  1.000 12.60323  ? 73  ASN B ND2 1 
ATOM   2168 N  N   . HIS B 1 75  ? 12.36709 29.26491 86.75567  1.000 12.38906  ? 74  HIS B N   1 
ATOM   2169 C  CA  . HIS B 1 75  ? 11.04337 29.84179 86.55522  1.000 11.60072  ? 74  HIS B CA  1 
ATOM   2170 C  C   . HIS B 1 75  ? 10.36742 29.27037 85.31930  1.000 14.61182  ? 74  HIS B C   1 
ATOM   2171 O  O   . HIS B 1 75  ? 9.15006  29.07526 85.32350  1.000 13.53453  ? 74  HIS B O   1 
ATOM   2172 C  CB  . HIS B 1 75  ? 11.11136 31.37095 86.53317  1.000 13.15499  ? 74  HIS B CB  1 
ATOM   2173 C  CG  . HIS B 1 75  ? 11.46472 31.96204 87.86066  1.000 15.56698  ? 74  HIS B CG  1 
ATOM   2174 N  ND1 . HIS B 1 75  ? 12.76539 32.05389 88.30318  1.000 14.62250  ? 74  HIS B ND1 1 
ATOM   2175 C  CD2 . HIS B 1 75  ? 10.69131 32.44996 88.85900  1.000 13.15008  ? 74  HIS B CD2 1 
ATOM   2176 C  CE1 . HIS B 1 75  ? 12.78170 32.59644 89.50854  1.000 15.26990  ? 74  HIS B CE1 1 
ATOM   2177 N  NE2 . HIS B 1 75  ? 11.53461 32.84399 89.87011  1.000 12.84244  ? 74  HIS B NE2 1 
ATOM   2178 N  N   . SER B 1 76  ? 11.13358 28.96851 84.26740  1.000 13.59509  ? 75  SER B N   1 
ATOM   2179 C  CA  . SER B 1 76  ? 10.52603 28.37320 83.08268  1.000 13.75227  ? 75  SER B CA  1 
ATOM   2180 C  C   . SER B 1 76  ? 9.86332  27.04577 83.42217  1.000 13.54942  ? 75  SER B C   1 
ATOM   2181 O  O   . SER B 1 76  ? 8.77315  26.74420 82.92326  1.000 14.25323  ? 75  SER B O   1 
ATOM   2182 C  CB  . SER B 1 76  ? 11.56394 28.20559 81.97090  1.000 14.19698  ? 75  SER B CB  1 
ATOM   2183 O  OG  . SER B 1 76  ? 12.02507 29.46632 81.51516  1.000 14.75155  ? 75  SER B OG  1 
ATOM   2184 N  N   . ILE B 1 77  ? 10.48882 26.25300 84.29370  1.000 11.91034  ? 76  ILE B N   1 
ATOM   2185 C  CA  . ILE B 1 77  ? 9.86570  25.01677 84.75585  1.000 14.01683  ? 76  ILE B CA  1 
ATOM   2186 C  C   . ILE B 1 77  ? 8.69252  25.31753 85.67597  1.000 14.31791  ? 76  ILE B C   1 
ATOM   2187 O  O   . ILE B 1 77  ? 7.60850  24.73674 85.53525  1.000 13.71903  ? 76  ILE B O   1 
ATOM   2188 C  CB  . ILE B 1 77  ? 10.91637 24.13561 85.45357  1.000 12.14626  ? 76  ILE B CB  1 
ATOM   2189 C  CG1 . ILE B 1 77  ? 11.98060 23.68616 84.45332  1.000 14.71891  ? 76  ILE B CG1 1 
ATOM   2190 C  CG2 . ILE B 1 77  ? 10.24144 22.93597 86.13489  1.000 12.67821  ? 76  ILE B CG2 1 
ATOM   2191 C  CD1 . ILE B 1 77  ? 13.27207 23.24882 85.10912  1.000 15.63476  ? 76  ILE B CD1 1 
ATOM   2192 N  N   . PHE B 1 78  ? 8.88251  26.25124 86.60785  1.000 13.18566  ? 77  PHE B N   1 
ATOM   2193 C  CA  . PHE B 1 78  ? 7.88390  26.52757 87.63584  1.000 13.59610  ? 77  PHE B CA  1 
ATOM   2194 C  C   . PHE B 1 78  ? 6.52786  26.87697 87.02758  1.000 11.94675  ? 77  PHE B C   1 
ATOM   2195 O  O   . PHE B 1 78  ? 5.49278  26.35700 87.46798  1.000 13.06194  ? 77  PHE B O   1 
ATOM   2196 C  CB  . PHE B 1 78  ? 8.40288  27.66827 88.51588  1.000 12.61149  ? 77  PHE B CB  1 
ATOM   2197 C  CG  . PHE B 1 78  ? 7.55984  27.96150 89.73596  1.000 12.66871  ? 77  PHE B CG  1 
ATOM   2198 C  CD1 . PHE B 1 78  ? 7.25000  26.96970 90.65593  1.000 12.36316  ? 77  PHE B CD1 1 
ATOM   2199 C  CD2 . PHE B 1 78  ? 7.13263  29.25807 89.98901  1.000 11.68116  ? 77  PHE B CD2 1 
ATOM   2200 C  CE1 . PHE B 1 78  ? 6.49464  27.25634 91.78643  1.000 13.76448  ? 77  PHE B CE1 1 
ATOM   2201 C  CE2 . PHE B 1 78  ? 6.38075  29.55325 91.12352  1.000 13.38966  ? 77  PHE B CE2 1 
ATOM   2202 C  CZ  . PHE B 1 78  ? 6.06550  28.55012 92.02278  1.000 14.00032  ? 77  PHE B CZ  1 
ATOM   2203 N  N   . TRP B 1 79  ? 6.50617  27.71625 85.98607  1.000 12.86093  ? 78  TRP B N   1 
ATOM   2204 C  CA  . TRP B 1 79  ? 5.21455  28.11205 85.42428  1.000 11.68684  ? 78  TRP B CA  1 
ATOM   2205 C  C   . TRP B 1 79  ? 4.44482  26.90706 84.90780  1.000 13.85286  ? 78  TRP B C   1 
ATOM   2206 O  O   . TRP B 1 79  ? 3.22343  26.82561 85.07514  1.000 13.48637  ? 78  TRP B O   1 
ATOM   2207 C  CB  . TRP B 1 79  ? 5.36877  29.12678 84.28981  1.000 14.03073  ? 78  TRP B CB  1 
ATOM   2208 C  CG  . TRP B 1 79  ? 6.23917  30.30083 84.57091  1.000 11.67111  ? 78  TRP B CG  1 
ATOM   2209 C  CD1 . TRP B 1 79  ? 7.20173  30.80460 83.74909  1.000 13.17832  ? 78  TRP B CD1 1 
ATOM   2210 C  CD2 . TRP B 1 79  ? 6.23540  31.13201 85.74372  1.000 14.70064  ? 78  TRP B CD2 1 
ATOM   2211 N  NE1 . TRP B 1 79  ? 7.79541  31.89827 84.32916  1.000 13.46255  ? 78  TRP B NE1 1 
ATOM   2212 C  CE2 . TRP B 1 79  ? 7.22746  32.11541 85.55613  1.000 14.44095  ? 78  TRP B CE2 1 
ATOM   2213 C  CE3 . TRP B 1 79  ? 5.49179  31.14205 86.93025  1.000 13.51871  ? 78  TRP B CE3 1 
ATOM   2214 C  CZ2 . TRP B 1 79  ? 7.50763  33.09132 86.51339  1.000 13.33698  ? 78  TRP B CZ2 1 
ATOM   2215 C  CZ3 . TRP B 1 79  ? 5.77044  32.11783 87.88198  1.000 14.13133  ? 78  TRP B CZ3 1 
ATOM   2216 C  CH2 . TRP B 1 79  ? 6.77048  33.07527 87.66499  1.000 14.33356  ? 78  TRP B CH2 1 
ATOM   2217 N  N   . THR B 1 80  ? 5.14309  25.96128 84.28070  1.000 12.54426  ? 79  THR B N   1 
ATOM   2218 C  CA  . THR B 1 80  ? 4.48730  24.77736 83.74291  1.000 13.12490  ? 79  THR B CA  1 
ATOM   2219 C  C   . THR B 1 80  ? 4.08416  23.79325 84.83197  1.000 14.00503  ? 79  THR B C   1 
ATOM   2220 O  O   . THR B 1 80  ? 3.22557  22.93899 84.58344  1.000 13.92838  ? 79  THR B O   1 
ATOM   2221 C  CB  . THR B 1 80  ? 5.38328  24.07694 82.71819  1.000 15.83427  ? 79  THR B CB  1 
ATOM   2222 O  OG1 . THR B 1 80  ? 6.48448  23.44953 83.39016  1.000 14.98391  ? 79  THR B OG1 1 
ATOM   2223 C  CG2 . THR B 1 80  ? 5.92116  25.06901 81.69655  1.000 14.87619  ? 79  THR B CG2 1 
ATOM   2224 N  N   . ASN B 1 81  ? 4.69048  23.88051 86.01952  1.000 13.15705  ? 80  ASN B N   1 
ATOM   2225 C  CA  . ASN B 1 81  ? 4.35317  23.00297 87.13737  1.000 13.52767  ? 80  ASN B CA  1 
ATOM   2226 C  C   . ASN B 1 81  ? 3.03620  23.36801 87.81432  1.000 12.28315  ? 80  ASN B C   1 
ATOM   2227 O  O   . ASN B 1 81  ? 2.59974  22.62561 88.69965  1.000 14.53352  ? 80  ASN B O   1 
ATOM   2228 C  CB  . ASN B 1 81  ? 5.43546  23.05834 88.22664  1.000 12.26902  ? 80  ASN B CB  1 
ATOM   2229 C  CG  . ASN B 1 81  ? 6.71512  22.30881 87.86907  1.000 14.14861  ? 80  ASN B CG  1 
ATOM   2230 O  OD1 . ASN B 1 81  ? 7.73816  22.52686 88.51076  1.000 13.82414  ? 80  ASN B OD1 1 
ATOM   2231 N  ND2 . ASN B 1 81  ? 6.66665  21.42497 86.87330  1.000 12.09511  ? 80  ASN B ND2 1 
ATOM   2232 N  N   . LEU B 1 82  ? 2.43058  24.50209 87.46574  1.000 13.34135  ? 81  LEU B N   1 
ATOM   2233 C  CA  . LEU B 1 82  ? 1.20580  24.99177 88.08339  1.000 13.88386  ? 81  LEU B CA  1 
ATOM   2234 C  C   . LEU B 1 82  ? 0.11187  25.11741 87.02945  1.000 15.12999  ? 81  LEU B C   1 
ATOM   2235 O  O   . LEU B 1 82  ? 0.39342  25.25804 85.83852  1.000 13.32103  ? 81  LEU B O   1 
ATOM   2236 C  CB  . LEU B 1 82  ? 1.44259  26.36826 88.72133  1.000 14.04681  ? 81  LEU B CB  1 
ATOM   2237 C  CG  . LEU B 1 82  ? 2.71228  26.50022 89.57216  1.000 13.13869  ? 81  LEU B CG  1 
ATOM   2238 C  CD1 . LEU B 1 82  ? 2.91503  27.94145 90.00859  1.000 17.80691  ? 81  LEU B CD1 1 
ATOM   2239 C  CD2 . LEU B 1 82  ? 2.63787  25.57220 90.78028  1.000 17.76350  ? 81  LEU B CD2 1 
ATOM   2240 N  N   . SER B 1 83  ? -1.14822 25.08303 87.47420  1.000 14.10114  ? 82  SER B N   1 
ATOM   2241 C  CA  . SER B 1 83  ? -2.27462 25.19486 86.55541  1.000 15.66235  ? 82  SER B CA  1 
ATOM   2242 C  C   . SER B 1 83  ? -3.53113 25.56391 87.32710  1.000 16.16187  ? 82  SER B C   1 
ATOM   2243 O  O   . SER B 1 83  ? -3.71053 25.11233 88.46369  1.000 14.06321  ? 82  SER B O   1 
ATOM   2244 C  CB  . SER B 1 83  ? -2.50641 23.86869 85.82346  1.000 14.70339  ? 82  SER B CB  1 
ATOM   2245 O  OG  . SER B 1 83  ? -3.69237 23.94925 85.04771  1.000 20.40601  ? 82  SER B OG  1 
ATOM   2246 N  N   . PRO B 1 84  ? -4.43508 26.34737 86.72783  1.000 14.45910  ? 83  PRO B N   1 
ATOM   2247 C  CA  . PRO B 1 84  ? -5.74958 26.55221 87.35820  1.000 15.55750  ? 83  PRO B CA  1 
ATOM   2248 C  C   . PRO B 1 84  ? -6.53455 25.26679 87.50886  1.000 18.42815  ? 83  PRO B C   1 
ATOM   2249 O  O   . PRO B 1 84  ? -7.37593 25.16489 88.40995  1.000 18.83016  ? 83  PRO B O   1 
ATOM   2250 C  CB  . PRO B 1 84  ? -6.45375 27.52864 86.40177  1.000 15.89743  ? 83  PRO B CB  1 
ATOM   2251 C  CG  . PRO B 1 84  ? -5.74685 27.37595 85.10061  1.000 17.41966  ? 83  PRO B CG  1 
ATOM   2252 C  CD  . PRO B 1 84  ? -4.31602 27.06030 85.44610  1.000 15.78183  ? 83  PRO B CD  1 
ATOM   2253 N  N   . ASN B 1 85  ? -6.28527 24.28424 86.64798  1.000 14.85652  ? 84  ASN B N   1 
ATOM   2254 C  CA  . ASN B 1 85  ? -6.91943 22.97425 86.71114  1.000 17.50914  ? 84  ASN B CA  1 
ATOM   2255 C  C   . ASN B 1 85  ? -6.15421 21.98778 87.58276  1.000 18.02218  ? 84  ASN B C   1 
ATOM   2256 O  O   . ASN B 1 85  ? -6.48694 20.79867 87.59137  1.000 19.51141  ? 84  ASN B O   1 
ATOM   2257 C  CB  . ASN B 1 85  ? -7.07592 22.40809 85.29829  1.000 21.36248  ? 84  ASN B CB  1 
ATOM   2258 C  CG  . ASN B 1 85  ? -7.63029 23.43030 84.32155  1.000 39.31537  ? 84  ASN B CG  1 
ATOM   2259 O  OD1 . ASN B 1 85  ? -8.81443 23.76415 84.36032  1.000 46.81260  ? 84  ASN B OD1 1 
ATOM   2260 N  ND2 . ASN B 1 85  ? -6.77346 23.93197 83.43831  1.000 39.77731  ? 84  ASN B ND2 1 
ATOM   2261 N  N   . GLY B 1 86  ? -5.14934 22.45205 88.31806  1.000 16.34549  ? 85  GLY B N   1 
ATOM   2262 C  CA  . GLY B 1 86  ? -4.28690 21.57727 89.08176  1.000 17.06178  ? 85  GLY B CA  1 
ATOM   2263 C  C   . GLY B 1 86  ? -4.87266 21.19434 90.42494  1.000 17.29421  ? 85  GLY B C   1 
ATOM   2264 O  O   . GLY B 1 86  ? -6.06778 21.34969 90.69097  1.000 17.30140  ? 85  GLY B O   1 
ATOM   2265 N  N   . GLY B 1 87  ? -3.99946 20.68540 91.28744  1.000 16.47179  ? 86  GLY B N   1 
ATOM   2266 C  CA  . GLY B 1 87  ? -4.39092 20.19507 92.59398  1.000 14.94330  ? 86  GLY B CA  1 
ATOM   2267 C  C   . GLY B 1 87  ? -4.60872 18.69761 92.58160  1.000 14.87366  ? 86  GLY B C   1 
ATOM   2268 O  O   . GLY B 1 87  ? -4.42379 18.01143 91.57211  1.000 16.71544  ? 86  GLY B O   1 
ATOM   2269 N  N   . GLY B 1 88  ? -4.99981 18.19164 93.75011  1.000 15.77506  ? 87  GLY B N   1 
ATOM   2270 C  CA  . GLY B 1 88  ? -5.24353 16.76819 93.89050  1.000 18.90779  ? 87  GLY B CA  1 
ATOM   2271 C  C   . GLY B 1 88  ? -3.96018 15.95284 93.84188  1.000 18.30187  ? 87  GLY B C   1 
ATOM   2272 O  O   . GLY B 1 88  ? -2.87694 16.41088 94.22129  1.000 17.69978  ? 87  GLY B O   1 
ATOM   2273 N  N   . GLU B 1 89  ? -4.08363 14.72596 93.33578  1.000 18.00912  ? 88  GLU B N   1 
ATOM   2274 C  CA  . GLU B 1 89  ? -2.95877 13.81141 93.28577  1.000 19.07368  ? 88  GLU B CA  1 
ATOM   2275 C  C   . GLU B 1 89  ? -2.67262 13.39119 91.84981  1.000 20.28038  ? 88  GLU B C   1 
ATOM   2276 O  O   . GLU B 1 89  ? -3.56860 13.41340 90.99874  1.000 21.25027  ? 88  GLU B O   1 
ATOM   2277 C  CB  . GLU B 1 89  ? -3.24885 12.55534 94.11836  1.000 19.43818  ? 88  GLU B CB  1 
ATOM   2278 C  CG  . GLU B 1 89  ? -3.62606 12.83729 95.56032  1.000 20.10490  ? 88  GLU B CG  1 
ATOM   2279 C  CD  . GLU B 1 89  ? -3.62411 11.59131 96.42572  1.000 24.29030  ? 88  GLU B CD  1 
ATOM   2280 O  OE1 . GLU B 1 89  ? -3.24714 10.51263 95.92152  1.000 24.30742  ? 88  GLU B OE1 1 
ATOM   2281 O  OE2 . GLU B 1 89  ? -4.00599 11.69123 97.60889  1.000 27.97361  ? 88  GLU B OE2 1 
ATOM   2282 N  N   . PRO B 1 90  ? -1.43537 13.01370 91.54598  1.000 17.88418  ? 89  PRO B N   1 
ATOM   2283 C  CA  . PRO B 1 90  ? -1.14735 12.42018 90.23958  1.000 15.76831  ? 89  PRO B CA  1 
ATOM   2284 C  C   . PRO B 1 90  ? -1.69291 11.00314 90.18941  1.000 20.13108  ? 89  PRO B C   1 
ATOM   2285 O  O   . PRO B 1 90  ? -2.18780 10.46146 91.17705  1.000 20.12916  ? 89  PRO B O   1 
ATOM   2286 C  CB  . PRO B 1 90  ? 0.38016  12.40673 90.19797  1.000 21.09090  ? 89  PRO B CB  1 
ATOM   2287 C  CG  . PRO B 1 90  ? 0.76801  12.25448 91.63195  1.000 16.74569  ? 89  PRO B CG  1 
ATOM   2288 C  CD  . PRO B 1 90  ? -0.23889 13.05293 92.40747  1.000 16.96233  ? 89  PRO B CD  1 
ATOM   2289 N  N   . LYS B 1 91  ? -1.59554 10.40045 89.01124  1.000 20.74023  ? 90  LYS B N   1 
ATOM   2290 C  CA  . LYS B 1 91  ? -2.05924 9.03914  88.79698  1.000 22.01350  ? 90  LYS B CA  1 
ATOM   2291 C  C   . LYS B 1 91  ? -0.97380 8.25382  88.07186  1.000 24.50021  ? 90  LYS B C   1 
ATOM   2292 O  O   . LYS B 1 91  ? 0.10727  8.77161  87.77342  1.000 25.30485  ? 90  LYS B O   1 
ATOM   2293 C  CB  . LYS B 1 91  ? -3.38936 9.02212  88.03148  1.000 25.88677  ? 90  LYS B CB  1 
ATOM   2294 C  CG  . LYS B 1 91  ? -3.32594 9.67222  86.66297  1.000 30.80034  ? 90  LYS B CG  1 
ATOM   2295 C  CD  . LYS B 1 91  ? -4.64455 9.52397  85.92140  1.000 43.04570  ? 90  LYS B CD  1 
ATOM   2296 C  CE  . LYS B 1 91  ? -4.54776 10.06326 84.50197  1.000 50.69600  ? 90  LYS B CE  1 
ATOM   2297 N  NZ  . LYS B 1 91  ? -5.81560 9.86064  83.74521  1.000 58.19798  ? 90  LYS B NZ  1 
ATOM   2298 N  N   . GLY B 1 92  ? -1.25867 6.98228  87.81252  1.000 24.12389  ? 91  GLY B N   1 
ATOM   2299 C  CA  . GLY B 1 92  ? -0.37312 6.18336  86.99748  1.000 20.62889  ? 91  GLY B CA  1 
ATOM   2300 C  C   . GLY B 1 92  ? 0.98751  5.96857  87.63351  1.000 19.19415  ? 91  GLY B C   1 
ATOM   2301 O  O   . GLY B 1 92  ? 1.14107  5.89501  88.85845  1.000 20.43200  ? 91  GLY B O   1 
ATOM   2302 N  N   . GLU B 1 93  ? 1.99968  5.87325  86.77083  1.000 20.33472  ? 92  GLU B N   1 
ATOM   2303 C  CA  . GLU B 1 93  ? 3.33522  5.49217  87.22093  1.000 22.51986  ? 92  GLU B CA  1 
ATOM   2304 C  C   . GLU B 1 93  ? 3.95030  6.52989  88.15221  1.000 22.50936  ? 92  GLU B C   1 
ATOM   2305 O  O   . GLU B 1 93  ? 4.73654  6.17052  89.03638  1.000 23.41874  ? 92  GLU B O   1 
ATOM   2306 C  CB  . GLU B 1 93  ? 4.24385  5.23221  86.02005  1.000 24.35720  ? 92  GLU B CB  1 
ATOM   2307 C  CG  . GLU B 1 93  ? 3.79975  4.04948  85.17422  1.000 27.27715  ? 92  GLU B CG  1 
ATOM   2308 C  CD  . GLU B 1 93  ? 4.64807  3.86734  83.93663  1.000 35.50628  ? 92  GLU B CD  1 
ATOM   2309 O  OE1 . GLU B 1 93  ? 5.85503  4.17389  83.99659  1.000 34.11354  ? 92  GLU B OE1 1 
ATOM   2310 O  OE2 . GLU B 1 93  ? 4.11032  3.41703  82.90371  1.000 39.76307  ? 92  GLU B OE2 1 
ATOM   2311 N  N   . LEU B 1 94  ? 3.61146  7.80996  87.98095  1.000 20.94030  ? 93  LEU B N   1 
ATOM   2312 C  CA  . LEU B 1 94  ? 4.14913  8.81780  88.89010  1.000 19.71339  ? 93  LEU B CA  1 
ATOM   2313 C  C   . LEU B 1 94  ? 3.62557  8.61712  90.30555  1.000 18.62794  ? 93  LEU B C   1 
ATOM   2314 O  O   . LEU B 1 94  ? 4.40059  8.66097  91.26915  1.000 16.69969  ? 93  LEU B O   1 
ATOM   2315 C  CB  . LEU B 1 94  ? 3.83993  10.22615 88.38940  1.000 18.93130  ? 93  LEU B CB  1 
ATOM   2316 C  CG  . LEU B 1 94  ? 4.33530  11.33728 89.32419  1.000 16.43148  ? 93  LEU B CG  1 
ATOM   2317 C  CD1 . LEU B 1 94  ? 5.84129  11.24175 89.55225  1.000 18.29409  ? 93  LEU B CD1 1 
ATOM   2318 C  CD2 . LEU B 1 94  ? 3.96055  12.70122 88.77504  1.000 20.13058  ? 93  LEU B CD2 1 
ATOM   2319 N  N   . LEU B 1 95  ? 2.31995  8.37005  90.45182  1.000 17.17361  ? 94  LEU B N   1 
ATOM   2320 C  CA  . LEU B 1 95  ? 1.77408  8.10393  91.77765  1.000 18.61304  ? 94  LEU B CA  1 
ATOM   2321 C  C   . LEU B 1 95  ? 2.37559  6.83535  92.36708  1.000 18.99068  ? 94  LEU B C   1 
ATOM   2322 O  O   . LEU B 1 95  ? 2.68977  6.78513  93.56219  1.000 19.17112  ? 94  LEU B O   1 
ATOM   2323 C  CB  . LEU B 1 95  ? 0.25197  7.99248  91.70971  1.000 19.53354  ? 94  LEU B CB  1 
ATOM   2324 C  CG  . LEU B 1 95  ? -0.43776 7.74355  93.05142  1.000 19.84842  ? 94  LEU B CG  1 
ATOM   2325 C  CD1 . LEU B 1 95  ? -0.27917 8.93584  93.97943  1.000 21.44472  ? 94  LEU B CD1 1 
ATOM   2326 C  CD2 . LEU B 1 95  ? -1.91223 7.40307  92.84510  1.000 19.86663  ? 94  LEU B CD2 1 
ATOM   2327 N  N   . GLU B 1 96  ? 2.55589  5.80381  91.53518  1.000 19.34517  ? 95  GLU B N   1 
ATOM   2328 C  CA  . GLU B 1 96  ? 3.19092  4.57244  91.99345  1.000 21.96506  ? 95  GLU B CA  1 
ATOM   2329 C  C   . GLU B 1 96  ? 4.60781  4.83795  92.48024  1.000 16.13283  ? 95  GLU B C   1 
ATOM   2330 O  O   . GLU B 1 96  ? 5.02775  4.30131  93.51165  1.000 17.70799  ? 95  GLU B O   1 
ATOM   2331 C  CB  . GLU B 1 96  ? 3.21314  3.54203  90.86568  1.000 24.19374  ? 95  GLU B CB  1 
ATOM   2332 C  CG  . GLU B 1 96  ? 1.84581  3.12656  90.36202  1.000 28.92193  ? 95  GLU B CG  1 
ATOM   2333 C  CD  . GLU B 1 96  ? 1.92175  2.30926  89.08593  1.000 46.59742  ? 95  GLU B CD  1 
ATOM   2334 O  OE1 . GLU B 1 96  ? 2.99822  1.73821  88.80638  1.000 48.46486  ? 95  GLU B OE1 1 
ATOM   2335 O  OE2 . GLU B 1 96  ? 0.90545  2.23995  88.36178  1.000 51.26821  ? 95  GLU B OE2 1 
ATOM   2336 N  N   . ALA B 1 97  ? 5.35893  5.66237  91.74392  1.000 17.81233  ? 96  ALA B N   1 
ATOM   2337 C  CA  . ALA B 1 97  ? 6.72185  5.98783  92.15163  1.000 16.55125  ? 96  ALA B CA  1 
ATOM   2338 C  C   . ALA B 1 97  ? 6.73360  6.79686  93.44210  1.000 20.46175  ? 96  ALA B C   1 
ATOM   2339 O  O   . ALA B 1 97  ? 7.57940  6.57160  94.31353  1.000 17.90594  ? 96  ALA B O   1 
ATOM   2340 C  CB  . ALA B 1 97  ? 7.43547  6.73947  91.03028  1.000 19.47820  ? 96  ALA B CB  1 
ATOM   2341 N  N   . ILE B 1 98  ? 5.79588  7.73634  93.58785  1.000 16.99853  ? 97  ILE B N   1 
ATOM   2342 C  CA  . ILE B 1 98  ? 5.70797  8.51879  94.81899  1.000 16.16599  ? 97  ILE B CA  1 
ATOM   2343 C  C   . ILE B 1 98  ? 5.43639  7.60902  96.01340  1.000 17.85145  ? 97  ILE B C   1 
ATOM   2344 O  O   . ILE B 1 98  ? 6.07848  7.72530  97.06448  1.000 17.30177  ? 97  ILE B O   1 
ATOM   2345 C  CB  . ILE B 1 98  ? 4.65124  9.63012  94.67451  1.000 14.07266  ? 97  ILE B CB  1 
ATOM   2346 C  CG1 . ILE B 1 98  ? 5.18407  10.74592 93.76245  1.000 18.52886  ? 97  ILE B CG1 1 
ATOM   2347 C  CG2 . ILE B 1 98  ? 4.23174  10.15632 96.03705  1.000 16.83913  ? 97  ILE B CG2 1 
ATOM   2348 C  CD1 . ILE B 1 98  ? 4.16538  11.83732 93.43098  1.000 16.72612  ? 97  ILE B CD1 1 
ATOM   2349 N  N   . LYS B 1 99  ? 4.48663  6.68052  95.86726  1.000 18.17445  ? 98  LYS B N   1 
ATOM   2350 C  CA  . LYS B 1 99  ? 4.20225  5.74842  96.95484  1.000 19.00950  ? 98  LYS B CA  1 
ATOM   2351 C  C   . LYS B 1 99  ? 5.40277  4.86340  97.25072  1.000 16.21064  ? 98  LYS B C   1 
ATOM   2352 O  O   . LYS B 1 99  ? 5.70605  4.58282  98.41502  1.000 19.76525  ? 98  LYS B O   1 
ATOM   2353 C  CB  . LYS B 1 99  ? 2.99496  4.88322  96.59997  1.000 18.51845  ? 98  LYS B CB  1 
ATOM   2354 C  CG  . LYS B 1 99  ? 1.69233  5.65033  96.51652  1.000 19.34671  ? 98  LYS B CG  1 
ATOM   2355 C  CD  . LYS B 1 99  ? 0.57723  4.71928  96.06770  1.000 21.53328  ? 98  LYS B CD  1 
ATOM   2356 C  CE  . LYS B 1 99  ? -0.76764 5.42504  96.00259  1.000 18.74754  ? 98  LYS B CE  1 
ATOM   2357 N  NZ  . LYS B 1 99  ? -1.82232 4.52410  95.44857  1.000 20.32017  ? 98  LYS B NZ  1 
ATOM   2358 N  N   . ARG B 1 100 ? 6.09319  4.41341  96.20893  1.000 16.31584  ? 99  ARG B N   1 
ATOM   2359 C  CA  . ARG B 1 100 ? 7.22481  3.51551  96.40667  1.000 19.07607  ? 99  ARG B CA  1 
ATOM   2360 C  C   . ARG B 1 100 ? 8.39026  4.22139  97.09352  1.000 20.50859  ? 99  ARG B C   1 
ATOM   2361 O  O   . ARG B 1 100 ? 9.00492  3.66857  98.01518  1.000 20.77571  ? 99  ARG B O   1 
ATOM   2362 C  CB  . ARG B 1 100 ? 7.65559  2.93331  95.06110  1.000 18.60830  ? 99  ARG B CB  1 
ATOM   2363 C  CG  . ARG B 1 100 ? 8.92296  2.10553  95.11878  1.000 22.56740  ? 99  ARG B CG  1 
ATOM   2364 C  CD  . ARG B 1 100 ? 9.22151  1.43534  93.78668  1.000 31.43517  ? 99  ARG B CD  1 
ATOM   2365 N  NE  . ARG B 1 100 ? 9.24015  2.38108  92.67690  1.000 41.19283  ? 99  ARG B NE  1 
ATOM   2366 C  CZ  . ARG B 1 100 ? 8.30844  2.44927  91.73444  1.000 44.28297  ? 99  ARG B CZ  1 
ATOM   2367 N  NH1 . ARG B 1 100 ? 7.27176  1.62588  91.72555  1.000 36.57759  ? 99  ARG B NH1 1 
ATOM   2368 N  NH2 . ARG B 1 100 ? 8.42138  3.36403  90.77467  1.000 29.46755  ? 99  ARG B NH2 1 
ATOM   2369 N  N   . ASP B 1 101 ? 8.70437  5.44222  96.66699  1.000 16.76831  ? 100 ASP B N   1 
ATOM   2370 C  CA  . ASP B 1 101 ? 9.90708  6.12157  97.13282  1.000 15.43876  ? 100 ASP B CA  1 
ATOM   2371 C  C   . ASP B 1 101 ? 9.69633  6.92751  98.40867  1.000 20.58606  ? 100 ASP B C   1 
ATOM   2372 O  O   . ASP B 1 101 ? 10.65951 7.15175  99.15247  1.000 20.00979  ? 100 ASP B O   1 
ATOM   2373 C  CB  . ASP B 1 101 ? 10.48092 7.00647  96.02218  1.000 17.35160  ? 100 ASP B CB  1 
ATOM   2374 C  CG  . ASP B 1 101 ? 11.00332 6.19953  94.85183  1.000 15.73581  ? 100 ASP B CG  1 
ATOM   2375 O  OD1 . ASP B 1 101 ? 11.37415 5.01621  95.05270  1.000 18.97836  ? 100 ASP B OD1 1 
ATOM   2376 O  OD2 . ASP B 1 101 ? 11.05917 6.73979  93.73048  1.000 15.60100  ? 100 ASP B OD2 1 
ATOM   2377 N  N   . PHE B 1 102 ? 8.47015  7.37681  98.68171  1.000 17.42686  ? 101 PHE B N   1 
ATOM   2378 C  CA  . PHE B 1 102 ? 8.19695  8.19810  99.85270  1.000 17.31987  ? 101 PHE B CA  1 
ATOM   2379 C  C   . PHE B 1 102 ? 7.19570  7.58371  100.81926 1.000 19.07553  ? 101 PHE B C   1 
ATOM   2380 O  O   . PHE B 1 102 ? 6.96293  8.15804  101.89031 1.000 23.22461  ? 101 PHE B O   1 
ATOM   2381 C  CB  . PHE B 1 102 ? 7.76002  9.60737  99.43125  1.000 19.90723  ? 101 PHE B CB  1 
ATOM   2382 C  CG  . PHE B 1 102 ? 8.77035  10.29931 98.56484  1.000 19.48627  ? 101 PHE B CG  1 
ATOM   2383 C  CD1 . PHE B 1 102 ? 9.94193  10.79563 99.11722  1.000 16.95975  ? 101 PHE B CD1 1 
ATOM   2384 C  CD2 . PHE B 1 102 ? 8.56887  10.42478 97.19792  1.000 17.00725  ? 101 PHE B CD2 1 
ATOM   2385 C  CE1 . PHE B 1 102 ? 10.89134 11.41290 98.32656  1.000 16.81719  ? 101 PHE B CE1 1 
ATOM   2386 C  CE2 . PHE B 1 102 ? 9.51743  11.04984 96.40014  1.000 17.57358  ? 101 PHE B CE2 1 
ATOM   2387 C  CZ  . PHE B 1 102 ? 10.67843 11.54374 96.96763  1.000 20.43818  ? 101 PHE B CZ  1 
ATOM   2388 N  N   . GLY B 1 103 ? 6.61136  6.43433  100.48358 1.000 19.40472  ? 102 GLY B N   1 
ATOM   2389 C  CA  . GLY B 1 103 ? 5.67485  5.76565  101.36510 1.000 20.86484  ? 102 GLY B CA  1 
ATOM   2390 C  C   . GLY B 1 103 ? 4.23266  6.00825  100.97543 1.000 20.15796  ? 102 GLY B C   1 
ATOM   2391 O  O   . GLY B 1 103 ? 3.43353  5.07267  100.87234 1.000 21.29454  ? 102 GLY B O   1 
ATOM   2392 N  N   . SER B 1 104 ? 3.89288  7.27108  100.74784 1.000 18.17675  ? 103 SER B N   1 
ATOM   2393 C  CA  . SER B 1 104 ? 2.54135  7.65271  100.36632 1.000 18.52880  ? 103 SER B CA  1 
ATOM   2394 C  C   . SER B 1 104 ? 2.61058  9.04673  99.76498  1.000 18.42346  ? 103 SER B C   1 
ATOM   2395 O  O   . SER B 1 104 ? 3.62362  9.74015  99.87863  1.000 18.74694  ? 103 SER B O   1 
ATOM   2396 C  CB  . SER B 1 104 ? 1.61107  7.65114  101.57990 1.000 19.25651  ? 103 SER B CB  1 
ATOM   2397 O  OG  . SER B 1 104 ? 1.95639  8.69491  102.47752 1.000 21.25642  ? 103 SER B OG  1 
ATOM   2398 N  N   . PHE B 1 105 ? 1.51873  9.45128  99.11396  1.000 18.73595  ? 104 PHE B N   1 
ATOM   2399 C  CA  . PHE B 1 105 ? 1.44889  10.81524 98.60236  1.000 15.97240  ? 104 PHE B CA  1 
ATOM   2400 C  C   . PHE B 1 105 ? 1.52453  11.82453 99.73986  1.000 19.35038  ? 104 PHE B C   1 
ATOM   2401 O  O   . PHE B 1 105 ? 2.21971  12.84114 99.63182  1.000 17.54943  ? 104 PHE B O   1 
ATOM   2402 C  CB  . PHE B 1 105 ? 0.16460  11.01935 97.79515  1.000 15.94773  ? 104 PHE B CB  1 
ATOM   2403 C  CG  . PHE B 1 105 ? -0.00126 12.41955 97.26405  1.000 16.82653  ? 104 PHE B CG  1 
ATOM   2404 C  CD1 . PHE B 1 105 ? 0.72926  12.85134 96.17183  1.000 18.64486  ? 104 PHE B CD1 1 
ATOM   2405 C  CD2 . PHE B 1 105 ? -0.88481 13.30158 97.86341  1.000 21.52599  ? 104 PHE B CD2 1 
ATOM   2406 C  CE1 . PHE B 1 105 ? 0.58303  14.14162 95.68229  1.000 16.47061  ? 104 PHE B CE1 1 
ATOM   2407 C  CE2 . PHE B 1 105 ? -1.04076 14.59042 97.37460  1.000 18.32887  ? 104 PHE B CE2 1 
ATOM   2408 C  CZ  . PHE B 1 105 ? -0.30044 15.01203 96.28750  1.000 17.58183  ? 104 PHE B CZ  1 
ATOM   2409 N  N   . ASP B 1 106 ? 0.82659  11.55100 100.84696 1.000 17.87909  ? 105 ASP B N   1 
ATOM   2410 C  CA  . ASP B 1 106 ? 0.83293  12.46488 101.98599 1.000 20.78603  ? 105 ASP B CA  1 
ATOM   2411 C  C   . ASP B 1 106 ? 2.22611  12.59227 102.58896 1.000 18.96582  ? 105 ASP B C   1 
ATOM   2412 O  O   . ASP B 1 106 ? 2.64086  13.68883 102.98151 1.000 18.35399  ? 105 ASP B O   1 
ATOM   2413 C  CB  . ASP B 1 106 ? -0.16207 11.98394 103.04648 1.000 18.98159  ? 105 ASP B CB  1 
ATOM   2414 C  CG  . ASP B 1 106 ? -1.59200 12.36384 102.72534 1.000 24.90276  ? 105 ASP B CG  1 
ATOM   2415 O  OD1 . ASP B 1 106 ? -1.82512 13.00665 101.68222 1.000 25.67559  ? 105 ASP B OD1 1 
ATOM   2416 O  OD2 . ASP B 1 106 ? -2.49316 12.00087 103.51261 1.000 34.16415  ? 105 ASP B OD2 1 
ATOM   2417 N  N   . LYS B 1 107 ? 2.96076  11.47961 102.68157 1.000 18.87646  ? 106 LYS B N   1 
ATOM   2418 C  CA  . LYS B 1 107 ? 4.32277  11.54374 103.20350 1.000 18.00179  ? 106 LYS B CA  1 
ATOM   2419 C  C   . LYS B 1 107 ? 5.24081  12.29740 102.25203 1.000 16.86506  ? 106 LYS B C   1 
ATOM   2420 O  O   . LYS B 1 107 ? 6.10195  13.06666 102.69305 1.000 17.59413  ? 106 LYS B O   1 
ATOM   2421 C  CB  . LYS B 1 107 ? 4.84823  10.14098 103.50984 1.000 17.10918  ? 106 LYS B CB  1 
ATOM   2422 C  CG  . LYS B 1 107 ? 4.17817  9.53066  104.72997 1.000 22.09368  ? 106 LYS B CG  1 
ATOM   2423 C  CD  . LYS B 1 107 ? 4.69574  8.13863  105.03040 1.000 28.42454  ? 106 LYS B CD  1 
ATOM   2424 C  CE  . LYS B 1 107 ? 4.12352  7.62305  106.34051 1.000 41.32459  ? 106 LYS B CE  1 
ATOM   2425 N  NZ  . LYS B 1 107 ? 4.51798  6.21202  106.60699 1.000 70.48099  ? 106 LYS B NZ  1 
ATOM   2426 N  N   . PHE B 1 108 ? 5.05239  12.10845 100.94413 1.000 19.47508  ? 107 PHE B N   1 
ATOM   2427 C  CA  . PHE B 1 108 ? 5.79183  12.89714 99.96501  1.000 18.81364  ? 107 PHE B CA  1 
ATOM   2428 C  C   . PHE B 1 108 ? 5.52426  14.38789 100.14604 1.000 15.69950  ? 107 PHE B C   1 
ATOM   2429 O  O   . PHE B 1 108 ? 6.45756  15.20009 100.13781 1.000 15.64267  ? 107 PHE B O   1 
ATOM   2430 C  CB  . PHE B 1 108 ? 5.43723  12.45151 98.54706  1.000 15.77271  ? 107 PHE B CB  1 
ATOM   2431 C  CG  . PHE B 1 108 ? 5.55813  13.54504 97.53177  1.000 15.77275  ? 107 PHE B CG  1 
ATOM   2432 C  CD1 . PHE B 1 108 ? 6.80249  13.95452 97.07810  1.000 16.67832  ? 107 PHE B CD1 1 
ATOM   2433 C  CD2 . PHE B 1 108 ? 4.42530  14.17683 97.04041  1.000 18.06474  ? 107 PHE B CD2 1 
ATOM   2434 C  CE1 . PHE B 1 108 ? 6.91507  14.97362 96.15115  1.000 17.92051  ? 107 PHE B CE1 1 
ATOM   2435 C  CE2 . PHE B 1 108 ? 4.53242  15.19652 96.11581  1.000 19.35981  ? 107 PHE B CE2 1 
ATOM   2436 C  CZ  . PHE B 1 108 ? 5.78489  15.59277 95.66874  1.000 19.41088  ? 107 PHE B CZ  1 
ATOM   2437 N  N   . LYS B 1 109 ? 4.25088  14.77012 100.30046 1.000 15.98738  ? 108 LYS B N   1 
ATOM   2438 C  CA  . LYS B 1 109 ? 3.92666  16.17465 100.54093 1.000 17.21762  ? 108 LYS B CA  1 
ATOM   2439 C  C   . LYS B 1 109 ? 4.63885  16.70632 101.77641 1.000 15.66739  ? 108 LYS B C   1 
ATOM   2440 O  O   . LYS B 1 109 ? 5.17475  17.82097 101.76339 1.000 17.93893  ? 108 LYS B O   1 
ATOM   2441 C  CB  . LYS B 1 109 ? 2.41632  16.36083 100.68825 1.000 20.96437  ? 108 LYS B CB  1 
ATOM   2442 C  CG  . LYS B 1 109 ? 1.66782  16.51661 99.38324  1.000 24.05347  ? 108 LYS B CG  1 
ATOM   2443 C  CD  . LYS B 1 109 ? 0.17249  16.70230 99.62108  1.000 24.52238  ? 108 LYS B CD  1 
ATOM   2444 C  CE  . LYS B 1 109 ? -0.14648 17.88881 100.51291 1.000 26.46686  ? 108 LYS B CE  1 
ATOM   2445 N  NZ  . LYS B 1 109 ? -1.62899 18.05044 100.66278 1.000 26.43250  ? 108 LYS B NZ  1 
ATOM   2446 N  N   . GLU B 1 110 ? 4.64695  15.92820 102.85869 1.000 17.48535  ? 109 GLU B N   1 
ATOM   2447 C  CA  . GLU B 1 110 ? 5.34591  16.35961 104.06264 1.000 17.14794  ? 109 GLU B CA  1 
ATOM   2448 C  C   . GLU B 1 110 ? 6.82479  16.57619 103.78374 1.000 16.08809  ? 109 GLU B C   1 
ATOM   2449 O  O   . GLU B 1 110 ? 7.41505  17.55873 104.24681 1.000 16.86395  ? 109 GLU B O   1 
ATOM   2450 C  CB  . GLU B 1 110 ? 5.18243  15.31510 105.16604 1.000 19.74020  ? 109 GLU B CB  1 
ATOM   2451 C  CG  . GLU B 1 110 ? 3.76684  15.16567 105.68842 1.000 26.56000  ? 109 GLU B CG  1 
ATOM   2452 C  CD  . GLU B 1 110 ? 3.63017  14.02793 106.68541 1.000 39.33891  ? 109 GLU B CD  1 
ATOM   2453 O  OE1 . GLU B 1 110 ? 4.60468  13.26340 106.85849 1.000 35.63663  ? 109 GLU B OE1 1 
ATOM   2454 O  OE2 . GLU B 1 110 ? 2.54708  13.89808 107.29471 1.000 49.34920  ? 109 GLU B OE2 1 
ATOM   2455 N  N   . LYS B 1 111 ? 7.43891  15.67560 103.01481 1.000 15.87892  ? 110 LYS B N   1 
ATOM   2456 C  CA  . LYS B 1 111 ? 8.87183  15.78552 102.75984 1.000 14.12696  ? 110 LYS B CA  1 
ATOM   2457 C  C   . LYS B 1 111 ? 9.19916  16.98477 101.87686 1.000 15.54978  ? 110 LYS B C   1 
ATOM   2458 O  O   . LYS B 1 111 ? 10.16222 17.71656 102.14370 1.000 14.75664  ? 110 LYS B O   1 
ATOM   2459 C  CB  . LYS B 1 111 ? 9.39183  14.49313 102.13196 1.000 16.94980  ? 110 LYS B CB  1 
ATOM   2460 C  CG  . LYS B 1 111 ? 9.30047  13.27814 103.04764 1.000 20.12417  ? 110 LYS B CG  1 
ATOM   2461 C  CD  . LYS B 1 111 ? 10.24741 13.38354 104.22840 1.000 39.39708  ? 110 LYS B CD  1 
ATOM   2462 C  CE  . LYS B 1 111 ? 10.15848 12.14230 105.10376 1.000 40.77934  ? 110 LYS B CE  1 
ATOM   2463 N  NZ  . LYS B 1 111 ? 10.81604 12.34103 106.42413 1.000 53.31645  ? 110 LYS B NZ  1 
ATOM   2464 N  N   . LEU B 1 112 ? 8.41321  17.21498 100.82381 1.000 16.45309  ? 111 LEU B N   1 
ATOM   2465 C  CA  . LEU B 1 112 ? 8.71839  18.34850 99.95969  1.000 14.85361  ? 111 LEU B CA  1 
ATOM   2466 C  C   . LEU B 1 112 ? 8.40450  19.66193 100.66282 1.000 15.30816  ? 111 LEU B C   1 
ATOM   2467 O  O   . LEU B 1 112 ? 9.14241  20.64603 100.51444 1.000 14.74955  ? 111 LEU B O   1 
ATOM   2468 C  CB  . LEU B 1 112 ? 7.97729  18.23556 98.62865  1.000 16.37083  ? 111 LEU B CB  1 
ATOM   2469 C  CG  . LEU B 1 112 ? 8.32710  19.34450 97.63502  1.000 14.80532  ? 111 LEU B CG  1 
ATOM   2470 C  CD1 . LEU B 1 112 ? 9.84508  19.43557 97.42383  1.000 17.05113  ? 111 LEU B CD1 1 
ATOM   2471 C  CD2 . LEU B 1 112 ? 7.62240  19.12354 96.31285  1.000 17.41881  ? 111 LEU B CD2 1 
ATOM   2472 N  N   . THR B 1 113 ? 7.33058  19.69101 101.45969 1.000 16.74697  ? 112 THR B N   1 
ATOM   2473 C  CA  . THR B 1 113 ? 7.05319  20.86873 102.27701 1.000 16.10827  ? 112 THR B CA  1 
ATOM   2474 C  C   . THR B 1 113 ? 8.20200  21.15358 103.23637 1.000 17.72150  ? 112 THR B C   1 
ATOM   2475 O  O   . THR B 1 113 ? 8.63224  22.30414 103.37572 1.000 16.61562  ? 112 THR B O   1 
ATOM   2476 C  CB  . THR B 1 113 ? 5.74537  20.68116 103.05234 1.000 17.96164  ? 112 THR B CB  1 
ATOM   2477 O  OG1 . THR B 1 113 ? 4.65643  20.52641 102.13491 1.000 16.45076  ? 112 THR B OG1 1 
ATOM   2478 C  CG2 . THR B 1 113 ? 5.48295  21.87823 103.95833 1.000 20.64815  ? 112 THR B CG2 1 
ATOM   2479 N  N   . ALA B 1 114 ? 8.71994  20.11366 103.89542 1.000 15.71472  ? 113 ALA B N   1 
ATOM   2480 C  CA  . ALA B 1 114 ? 9.79927  20.30600 104.85896 1.000 18.06303  ? 113 ALA B CA  1 
ATOM   2481 C  C   . ALA B 1 114 ? 11.06218 20.83532 104.18990 1.000 18.26656  ? 113 ALA B C   1 
ATOM   2482 O  O   . ALA B 1 114 ? 11.73940 21.71482 104.73596 1.000 17.71403  ? 113 ALA B O   1 
ATOM   2483 C  CB  . ALA B 1 114 ? 10.08060 18.99762 105.59802 1.000 18.96367  ? 113 ALA B CB  1 
ATOM   2484 N  N   . ALA B 1 115 ? 11.40546 20.30443 103.01378 1.000 15.86320  ? 114 ALA B N   1 
ATOM   2485 C  CA  . ALA B 1 115 ? 12.57738 20.79806 102.29892 1.000 13.35504  ? 114 ALA B CA  1 
ATOM   2486 C  C   . ALA B 1 115 ? 12.38523 22.24913 101.88297 1.000 16.50424  ? 114 ALA B C   1 
ATOM   2487 O  O   . ALA B 1 115 ? 13.33044 23.04581 101.91209 1.000 16.93510  ? 114 ALA B O   1 
ATOM   2488 C  CB  . ALA B 1 115 ? 12.84545 19.92311 101.07452 1.000 15.52180  ? 114 ALA B CB  1 
ATOM   2489 N  N   . SER B 1 116 ? 11.15897 22.61067 101.50662 1.000 15.53711  ? 115 SER B N   1 
ATOM   2490 C  CA  . SER B 1 116 ? 10.87654 23.97088 101.06558 1.000 14.85878  ? 115 SER B CA  1 
ATOM   2491 C  C   . SER B 1 116 ? 10.86840 24.94336 102.23933 1.000 15.82418  ? 115 SER B C   1 
ATOM   2492 O  O   . SER B 1 116 ? 11.42465 26.04574 102.14542 1.000 15.95557  ? 115 SER B O   1 
ATOM   2493 C  CB  . SER B 1 116 ? 9.55273  23.98805 100.30469 1.000 15.22847  ? 115 SER B CB  1 
ATOM   2494 O  OG  . SER B 1 116 ? 9.62813  23.13002 99.17535  1.000 15.09927  ? 115 SER B OG  1 
ATOM   2495 N  N   . VAL B 1 117 ? 10.24653 24.54954 103.35378 1.000 19.69894  ? 116 VAL B N   1 
ATOM   2496 C  CA  . VAL B 1 117 ? 10.24626 25.38015 104.55542 1.000 17.70487  ? 116 VAL B CA  1 
ATOM   2497 C  C   . VAL B 1 117 ? 11.65679 25.51421 105.11536 1.000 18.94036  ? 116 VAL B C   1 
ATOM   2498 O  O   . VAL B 1 117 ? 12.01076 26.54934 105.70011 1.000 21.61927  ? 116 VAL B O   1 
ATOM   2499 C  CB  . VAL B 1 117 ? 9.26593  24.78459 105.59027 1.000 20.80967  ? 116 VAL B CB  1 
ATOM   2500 C  CG1 . VAL B 1 117 ? 9.81060  24.91196 107.00894 1.000 32.31637  ? 116 VAL B CG1 1 
ATOM   2501 C  CG2 . VAL B 1 117 ? 7.90844  25.45566 105.50088 1.000 31.48872  ? 116 VAL B CG2 1 
ATOM   2502 N  N   . GLY B 1 118 ? 12.49892 24.50175 104.91015 1.000 18.11553  ? 117 GLY B N   1 
ATOM   2503 C  CA  . GLY B 1 118 ? 13.82881 24.49922 105.49136 1.000 19.08140  ? 117 GLY B CA  1 
ATOM   2504 C  C   . GLY B 1 118 ? 14.85248 25.37028 104.79975 1.000 19.15097  ? 117 GLY B C   1 
ATOM   2505 O  O   . GLY B 1 118 ? 15.94815 25.54221 105.34028 1.000 21.78521  ? 117 GLY B O   1 
ATOM   2506 N  N   . VAL B 1 119 ? 14.53483 25.92695 103.63124 1.000 16.15430  ? 118 VAL B N   1 
ATOM   2507 C  CA  . VAL B 1 119 ? 15.47360 26.81518 102.95355 1.000 16.83676  ? 118 VAL B CA  1 
ATOM   2508 C  C   . VAL B 1 119 ? 15.64755 28.07940 103.78258 1.000 13.62168  ? 118 VAL B C   1 
ATOM   2509 O  O   . VAL B 1 119 ? 14.68255 28.80649 104.04850 1.000 14.70361  ? 118 VAL B O   1 
ATOM   2510 C  CB  . VAL B 1 119 ? 15.01229 27.13385 101.52521 1.000 13.94047  ? 118 VAL B CB  1 
ATOM   2511 C  CG1 . VAL B 1 119 ? 15.89025 28.22698 100.91013 1.000 16.68351  ? 118 VAL B CG1 1 
ATOM   2512 C  CG2 . VAL B 1 119 ? 15.05923 25.87929 100.66414 1.000 14.42656  ? 118 VAL B CG2 1 
ATOM   2513 N  N   . GLN B 1 120 ? 16.87939 28.33095 104.21134 1.000 14.40566  ? 119 GLN B N   1 
ATOM   2514 C  CA  . GLN B 1 120 ? 17.23850 29.53545 104.94446 1.000 14.76516  ? 119 GLN B CA  1 
ATOM   2515 C  C   . GLN B 1 120 ? 17.80735 30.54511 103.95480 1.000 13.69471  ? 119 GLN B C   1 
ATOM   2516 O  O   . GLN B 1 120 ? 18.85071 30.29806 103.34056 1.000 16.68911  ? 119 GLN B O   1 
ATOM   2517 C  CB  . GLN B 1 120 ? 18.23897 29.20512 106.05396 1.000 17.24528  ? 119 GLN B CB  1 
ATOM   2518 C  CG  . GLN B 1 120 ? 17.63828 28.31465 107.14376 1.000 18.41282  ? 119 GLN B CG  1 
ATOM   2519 C  CD  . GLN B 1 120 ? 18.63988 27.86747 108.19748 1.000 21.63586  ? 119 GLN B CD  1 
ATOM   2520 O  OE1 . GLN B 1 120 ? 19.82990 27.71093 107.92290 1.000 24.41203  ? 119 GLN B OE1 1 
ATOM   2521 N  NE2 . GLN B 1 120 ? 18.16350 27.70311 109.42525 1.000 23.98697  ? 119 GLN B NE2 1 
ATOM   2522 N  N   . GLY B 1 121 ? 17.11454 31.66690 103.78690 1.000 14.70732  ? 120 GLY B N   1 
ATOM   2523 C  CA  . GLY B 1 121 ? 17.44881 32.58786 102.72048 1.000 12.95359  ? 120 GLY B CA  1 
ATOM   2524 C  C   . GLY B 1 121 ? 16.58833 32.30731 101.50713 1.000 14.31231  ? 120 GLY B C   1 
ATOM   2525 O  O   . GLY B 1 121 ? 15.48163 31.77305 101.63420 1.000 15.24779  ? 120 GLY B O   1 
ATOM   2526 N  N   . SER B 1 122 ? 17.09854 32.62655 100.32577 1.000 14.18487  ? 121 SER B N   1 
ATOM   2527 C  CA  . SER B 1 122 ? 16.36261 32.41498 99.08999  1.000 13.48264  ? 121 SER B CA  1 
ATOM   2528 C  C   . SER B 1 122 ? 16.67640 31.03212 98.52552  1.000 14.37982  ? 121 SER B C   1 
ATOM   2529 O  O   . SER B 1 122 ? 17.78072 30.50834 98.69515  1.000 14.28197  ? 121 SER B O   1 
ATOM   2530 C  CB  . SER B 1 122 ? 16.76357 33.48640 98.07419  1.000 11.75529  ? 121 SER B CB  1 
ATOM   2531 O  OG  . SER B 1 122 ? 16.52160 34.80556 98.56192  1.000 14.66765  ? 121 SER B OG  1 
ATOM   2532 N  N   . GLY B 1 123 ? 15.69558 30.42833 97.85999  1.000 12.54485  ? 122 GLY B N   1 
ATOM   2533 C  CA  . GLY B 1 123 ? 15.96940 29.15234 97.22596  1.000 12.72847  ? 122 GLY B CA  1 
ATOM   2534 C  C   . GLY B 1 123 ? 14.70866 28.46141 96.74366  1.000 12.00777  ? 122 GLY B C   1 
ATOM   2535 O  O   . GLY B 1 123 ? 13.65473 29.08426 96.59649  1.000 14.08696  ? 122 GLY B O   1 
ATOM   2536 N  N   . TRP B 1 124 ? 14.85212 27.15279 96.50918  1.000 11.69333  ? 123 TRP B N   1 
ATOM   2537 C  CA  . TRP B 1 124 ? 13.84563 26.31410 95.87381  1.000 13.06684  ? 123 TRP B CA  1 
ATOM   2538 C  C   . TRP B 1 124 ? 13.84333 24.93490 96.51149  1.000 15.45840  ? 123 TRP B C   1 
ATOM   2539 O  O   . TRP B 1 124 ? 14.89288 24.40938 96.88731  1.000 13.60457  ? 123 TRP B O   1 
ATOM   2540 C  CB  . TRP B 1 124 ? 14.17984 26.07987 94.39224  1.000 13.99902  ? 123 TRP B CB  1 
ATOM   2541 C  CG  . TRP B 1 124 ? 14.00055 27.26669 93.51994  1.000 12.55411  ? 123 TRP B CG  1 
ATOM   2542 C  CD1 . TRP B 1 124 ? 14.82882 28.35995 93.42490  1.000 12.39472  ? 123 TRP B CD1 1 
ATOM   2543 C  CD2 . TRP B 1 124 ? 12.92658 27.49913 92.60635  1.000 11.86989  ? 123 TRP B CD2 1 
ATOM   2544 N  NE1 . TRP B 1 124 ? 14.32817 29.25125 92.50926  1.000 12.79045  ? 123 TRP B NE1 1 
ATOM   2545 C  CE2 . TRP B 1 124 ? 13.16153 28.74980 91.99342  1.000 11.32156  ? 123 TRP B CE2 1 
ATOM   2546 C  CE3 . TRP B 1 124 ? 11.78422 26.77594 92.24816  1.000 12.88670  ? 123 TRP B CE3 1 
ATOM   2547 C  CZ2 . TRP B 1 124 ? 12.28925 29.29319 91.05076  1.000 12.77163  ? 123 TRP B CZ2 1 
ATOM   2548 C  CZ3 . TRP B 1 124 ? 10.92431 27.31788 91.29855  1.000 13.15169  ? 123 TRP B CZ3 1 
ATOM   2549 C  CH2 . TRP B 1 124 ? 11.18811 28.55440 90.70829  1.000 14.29591  ? 123 TRP B CH2 1 
ATOM   2550 N  N   . GLY B 1 125 ? 12.65679 24.34293 96.60786  1.000 11.88888  ? 124 GLY B N   1 
ATOM   2551 C  CA  . GLY B 1 125 ? 12.51555 22.91926 96.89100  1.000 16.00228  ? 124 GLY B CA  1 
ATOM   2552 C  C   . GLY B 1 125 ? 12.15442 22.18129 95.61501  1.000 12.63603  ? 124 GLY B C   1 
ATOM   2553 O  O   . GLY B 1 125 ? 11.40966 22.69809 94.78265  1.000 15.35784  ? 124 GLY B O   1 
ATOM   2554 N  N   . TRP B 1 126 ? 12.69924 20.97237 95.44914  1.000 13.31562  ? 125 TRP B N   1 
ATOM   2555 C  CA  . TRP B 1 126 ? 12.49817 20.21137 94.21842  1.000 14.64751  ? 125 TRP B CA  1 
ATOM   2556 C  C   . TRP B 1 126 ? 12.14335 18.76233 94.49473  1.000 15.40926  ? 125 TRP B C   1 
ATOM   2557 O  O   . TRP B 1 126 ? 12.75687 18.11259 95.34551  1.000 13.30849  ? 125 TRP B O   1 
ATOM   2558 C  CB  . TRP B 1 126 ? 13.75000 20.20320 93.31938  1.000 14.71322  ? 125 TRP B CB  1 
ATOM   2559 C  CG  . TRP B 1 126 ? 14.00428 21.50313 92.66556  1.000 14.25554  ? 125 TRP B CG  1 
ATOM   2560 C  CD1 . TRP B 1 126 ? 14.86762 22.46960 93.08530  1.000 14.57977  ? 125 TRP B CD1 1 
ATOM   2561 C  CD2 . TRP B 1 126 ? 13.37950 22.00788 91.47832  1.000 11.75184  ? 125 TRP B CD2 1 
ATOM   2562 N  NE1 . TRP B 1 126 ? 14.82322 23.54518 92.23726  1.000 13.63387  ? 125 TRP B NE1 1 
ATOM   2563 C  CE2 . TRP B 1 126 ? 13.92180 23.28769 91.23831  1.000 13.69385  ? 125 TRP B CE2 1 
ATOM   2564 C  CE3 . TRP B 1 126 ? 12.42312 21.49992 90.58921  1.000 15.61847  ? 125 TRP B CE3 1 
ATOM   2565 C  CZ2 . TRP B 1 126 ? 13.53509 24.07296 90.15488  1.000 14.00171  ? 125 TRP B CZ2 1 
ATOM   2566 C  CZ3 . TRP B 1 126 ? 12.03756 22.28558 89.50850  1.000 15.92151  ? 125 TRP B CZ3 1 
ATOM   2567 C  CH2 . TRP B 1 126 ? 12.60039 23.55762 89.30191  1.000 14.26471  ? 125 TRP B CH2 1 
ATOM   2568 N  N   . LEU B 1 127 ? 11.16159 18.26200 93.75079  1.000 13.08492  ? 126 LEU B N   1 
ATOM   2569 C  CA  . LEU B 1 127 ? 11.06757 16.84109 93.45586  1.000 12.73722  ? 126 LEU B CA  1 
ATOM   2570 C  C   . LEU B 1 127 ? 11.80274 16.60831 92.14322  1.000 13.73242  ? 126 LEU B C   1 
ATOM   2571 O  O   . LEU B 1 127 ? 11.47623 17.22878 91.12390  1.000 13.60508  ? 126 LEU B O   1 
ATOM   2572 C  CB  . LEU B 1 127 ? 9.61048  16.40762 93.31684  1.000 13.55330  ? 126 LEU B CB  1 
ATOM   2573 C  CG  . LEU B 1 127 ? 9.45938  14.96767 92.82675  1.000 14.30351  ? 126 LEU B CG  1 
ATOM   2574 C  CD1 . LEU B 1 127 ? 9.96408  13.98672 93.88044  1.000 16.29075  ? 126 LEU B CD1 1 
ATOM   2575 C  CD2 . LEU B 1 127 ? 8.01345  14.68509 92.45551  1.000 15.33979  ? 126 LEU B CD2 1 
ATOM   2576 N  N   . GLY B 1 128 ? 12.79992 15.72441 92.16843  1.000 13.51004  ? 127 GLY B N   1 
ATOM   2577 C  CA  . GLY B 1 128 ? 13.56488 15.41169 90.98601  1.000 12.23498  ? 127 GLY B CA  1 
ATOM   2578 C  C   . GLY B 1 128 ? 13.58752 13.91615 90.72793  1.000 13.27175  ? 127 GLY B C   1 
ATOM   2579 O  O   . GLY B 1 128 ? 13.10136 13.11353 91.52921  1.000 14.18881  ? 127 GLY B O   1 
ATOM   2580 N  N   . PHE B 1 129 ? 14.17343 13.56061 89.58687  1.000 15.24476  ? 128 PHE B N   1 
ATOM   2581 C  CA  . PHE B 1 129 ? 14.41602 12.17387 89.22241  1.000 14.56711  ? 128 PHE B CA  1 
ATOM   2582 C  C   . PHE B 1 129 ? 15.91797 11.92450 89.17450  1.000 15.19256  ? 128 PHE B C   1 
ATOM   2583 O  O   . PHE B 1 129 ? 16.65852 12.64688 88.49303  1.000 15.25390  ? 128 PHE B O   1 
ATOM   2584 C  CB  . PHE B 1 129 ? 13.78315 11.84250 87.87073  1.000 16.30561  ? 128 PHE B CB  1 
ATOM   2585 C  CG  . PHE B 1 129 ? 13.86604 10.38866 87.51177  1.000 17.79978  ? 128 PHE B CG  1 
ATOM   2586 C  CD1 . PHE B 1 129 ? 12.97111 9.48004  88.05499  1.000 17.35038  ? 128 PHE B CD1 1 
ATOM   2587 C  CD2 . PHE B 1 129 ? 14.84170 9.92910  86.64316  1.000 21.29162  ? 128 PHE B CD2 1 
ATOM   2588 C  CE1 . PHE B 1 129 ? 13.04761 8.13447  87.73472  1.000 22.83216  ? 128 PHE B CE1 1 
ATOM   2589 C  CE2 . PHE B 1 129 ? 14.92215 8.58660  86.31607  1.000 22.83842  ? 128 PHE B CE2 1 
ATOM   2590 C  CZ  . PHE B 1 129 ? 14.02325 7.68905  86.86435  1.000 20.76612  ? 128 PHE B CZ  1 
ATOM   2591 N  N   . ASN B 1 130 ? 16.36759 10.91137 89.90846  1.000 18.14028  ? 129 ASN B N   1 
ATOM   2592 C  CA  . ASN B 1 130 ? 17.76465 10.50161 89.88240  1.000 16.32546  ? 129 ASN B CA  1 
ATOM   2593 C  C   . ASN B 1 130 ? 17.91307 9.45135  88.78707  1.000 18.51267  ? 129 ASN B C   1 
ATOM   2594 O  O   . ASN B 1 130 ? 17.49656 8.30159  88.96080  1.000 17.81407  ? 129 ASN B O   1 
ATOM   2595 C  CB  . ASN B 1 130 ? 18.16577 9.95131  91.24835  1.000 17.10128  ? 129 ASN B CB  1 
ATOM   2596 C  CG  . ASN B 1 130 ? 19.64753 9.65536  91.34417  1.000 15.78362  ? 129 ASN B CG  1 
ATOM   2597 O  OD1 . ASN B 1 130 ? 20.23829 9.09816  90.42360  1.000 19.54701  ? 129 ASN B OD1 1 
ATOM   2598 N  ND2 . ASN B 1 130 ? 20.25938 10.04851 92.45385  1.000 17.86350  ? 129 ASN B ND2 1 
ATOM   2599 N  N   . LYS B 1 131 ? 18.51701 9.84666  87.66229  1.000 21.75246  ? 130 LYS B N   1 
ATOM   2600 C  CA  . LYS B 1 131 ? 18.60647 8.94952  86.51304  1.000 24.47742  ? 130 LYS B CA  1 
ATOM   2601 C  C   . LYS B 1 131 ? 19.46423 7.73039  86.82095  1.000 23.90953  ? 130 LYS B C   1 
ATOM   2602 O  O   . LYS B 1 131 ? 19.13730 6.61284  86.40527  1.000 26.12012  ? 130 LYS B O   1 
ATOM   2603 C  CB  . LYS B 1 131 ? 19.15357 9.69462  85.29446  1.000 30.69714  ? 130 LYS B CB  1 
ATOM   2604 C  CG  . LYS B 1 131 ? 18.15948 10.62266 84.61831  1.000 39.55734  ? 130 LYS B CG  1 
ATOM   2605 C  CD  . LYS B 1 131 ? 18.78439 11.29116 83.40079  1.000 50.39670  ? 130 LYS B CD  1 
ATOM   2606 C  CE  . LYS B 1 131 ? 17.72306 11.74910 82.41033  1.000 63.29081  ? 130 LYS B CE  1 
ATOM   2607 N  NZ  . LYS B 1 131 ? 18.30372 12.57335 81.31210  1.000 62.62686  ? 130 LYS B NZ  1 
ATOM   2608 N  N   . GLU B 1 132 ? 20.56199 7.92550  87.55117  1.000 22.51945  ? 131 GLU B N   1 
ATOM   2609 C  CA  . GLU B 1 132 ? 21.46894 6.81777  87.83511  1.000 21.01966  ? 131 GLU B CA  1 
ATOM   2610 C  C   . GLU B 1 132 ? 20.82653 5.80474  88.77241  1.000 25.72921  ? 131 GLU B C   1 
ATOM   2611 O  O   . GLU B 1 132 ? 20.93756 4.59145  88.55671  1.000 25.81000  ? 131 GLU B O   1 
ATOM   2612 C  CB  . GLU B 1 132 ? 22.76770 7.35492  88.43626  1.000 25.08527  ? 131 GLU B CB  1 
ATOM   2613 C  CG  . GLU B 1 132 ? 23.56413 8.26364  87.50788  1.000 45.09710  ? 131 GLU B CG  1 
ATOM   2614 C  CD  . GLU B 1 132 ? 23.13346 9.72163  87.57682  1.000 66.88386  ? 131 GLU B CD  1 
ATOM   2615 O  OE1 . GLU B 1 132 ? 21.93565 9.99017  87.81521  1.000 45.39635  ? 131 GLU B OE1 1 
ATOM   2616 O  OE2 . GLU B 1 132 ? 23.99874 10.60287 87.38722  1.000 78.84711  ? 131 GLU B OE2 1 
ATOM   2617 N  N   . ARG B 1 133 ? 20.14854 6.28480  89.81482  1.000 19.53138  ? 132 ARG B N   1 
ATOM   2618 C  CA  . ARG B 1 133 ? 19.46196 5.40949  90.75335  1.000 20.25842  ? 132 ARG B CA  1 
ATOM   2619 C  C   . ARG B 1 133 ? 18.09751 4.96412  90.24611  1.000 19.41581  ? 132 ARG B C   1 
ATOM   2620 O  O   . ARG B 1 133 ? 17.53477 4.00457  90.78346  1.000 19.44772  ? 132 ARG B O   1 
ATOM   2621 C  CB  . ARG B 1 133 ? 19.31748 6.11065  92.10863  1.000 17.56839  ? 132 ARG B CB  1 
ATOM   2622 C  CG  . ARG B 1 133 ? 20.64465 6.42819  92.78622  1.000 17.48666  ? 132 ARG B CG  1 
ATOM   2623 C  CD  . ARG B 1 133 ? 21.33633 5.16565  93.26941  1.000 19.81635  ? 132 ARG B CD  1 
ATOM   2624 N  NE  . ARG B 1 133 ? 20.55560 4.46542  94.28414  1.000 18.12568  ? 132 ARG B NE  1 
ATOM   2625 C  CZ  . ARG B 1 133 ? 20.67727 4.65774  95.59111  1.000 18.98973  ? 132 ARG B CZ  1 
ATOM   2626 N  NH1 . ARG B 1 133 ? 21.54408 5.52878  96.08419  1.000 15.88990  ? 132 ARG B NH1 1 
ATOM   2627 N  NH2 . ARG B 1 133 ? 19.91533 3.95455  96.42514  1.000 16.80559  ? 132 ARG B NH2 1 
ATOM   2628 N  N   . GLY B 1 134 ? 17.55021 5.64759  89.24560  1.000 20.59258  ? 133 GLY B N   1 
ATOM   2629 C  CA  . GLY B 1 134 ? 16.24869 5.28278  88.70893  1.000 17.14969  ? 133 GLY B CA  1 
ATOM   2630 C  C   . GLY B 1 134 ? 15.09636 5.45102  89.67518  1.000 19.75172  ? 133 GLY B C   1 
ATOM   2631 O  O   . GLY B 1 134 ? 14.17158 4.62886  89.67945  1.000 20.31670  ? 133 GLY B O   1 
ATOM   2632 N  N   . HIS B 1 135 ? 15.12218 6.50006  90.49419  1.000 16.29374  ? 134 HIS B N   1 
ATOM   2633 C  CA  . HIS B 1 135 ? 14.04578 6.73902  91.44688  1.000 15.70591  ? 134 HIS B CA  1 
ATOM   2634 C  C   . HIS B 1 135 ? 13.93160 8.23075  91.72429  1.000 15.31860  ? 134 HIS B C   1 
ATOM   2635 O  O   . HIS B 1 135 ? 14.77122 9.03025  91.30252  1.000 15.33930  ? 134 HIS B O   1 
ATOM   2636 C  CB  . HIS B 1 135 ? 14.19602 5.90353  92.73288  1.000 19.11792  ? 134 HIS B CB  1 
ATOM   2637 C  CG  . HIS B 1 135 ? 15.44660 6.18096  93.51473  1.000 16.78354  ? 134 HIS B CG  1 
ATOM   2638 N  ND1 . HIS B 1 135 ? 16.11260 5.19603  94.21402  1.000 17.22991  ? 134 HIS B ND1 1 
ATOM   2639 C  CD2 . HIS B 1 135 ? 16.13147 7.32798  93.73999  1.000 15.95712  ? 134 HIS B CD2 1 
ATOM   2640 C  CE1 . HIS B 1 135 ? 17.16380 5.72061  94.81949  1.000 16.95831  ? 134 HIS B CE1 1 
ATOM   2641 N  NE2 . HIS B 1 135 ? 17.19458 7.01408  94.55296  1.000 17.04828  ? 134 HIS B NE2 1 
ATOM   2642 N  N   . LEU B 1 136 ? 12.86653 8.59400  92.43097  1.000 15.85561  ? 135 LEU B N   1 
ATOM   2643 C  CA  . LEU B 1 136 ? 12.61826 9.97965  92.79288  1.000 14.04842  ? 135 LEU B CA  1 
ATOM   2644 C  C   . LEU B 1 136 ? 13.54601 10.41706 93.92236  1.000 15.40231  ? 135 LEU B C   1 
ATOM   2645 O  O   . LEU B 1 136 ? 14.09737 9.60108  94.66722  1.000 15.96518  ? 135 LEU B O   1 
ATOM   2646 C  CB  . LEU B 1 136 ? 11.16242 10.15688 93.22316  1.000 14.55736  ? 135 LEU B CB  1 
ATOM   2647 C  CG  . LEU B 1 136 ? 10.12549 9.74897  92.17577  1.000 13.39138  ? 135 LEU B CG  1 
ATOM   2648 C  CD1 . LEU B 1 136 ? 8.72059  9.80344  92.75775  1.000 16.85826  ? 135 LEU B CD1 1 
ATOM   2649 C  CD2 . LEU B 1 136 ? 10.25103 10.64500 90.96047  1.000 19.42655  ? 135 LEU B CD2 1 
ATOM   2650 N  N   . GLN B 1 137 ? 13.70746 11.73195 94.04660  1.000 13.87493  ? 136 GLN B N   1 
ATOM   2651 C  CA  . GLN B 1 137 ? 14.59701 12.29643 95.05020  1.000 15.00730  ? 136 GLN B CA  1 
ATOM   2652 C  C   . GLN B 1 137 ? 14.19785 13.74214 95.29259  1.000 14.90311  ? 136 GLN B C   1 
ATOM   2653 O  O   . GLN B 1 137 ? 13.94207 14.48636 94.34412  1.000 16.47758  ? 136 GLN B O   1 
ATOM   2654 C  CB  . GLN B 1 137 ? 16.05237 12.23307 94.57309  1.000 15.73785  ? 136 GLN B CB  1 
ATOM   2655 C  CG  . GLN B 1 137 ? 17.08338 12.64769 95.61275  1.000 16.58584  ? 136 GLN B CG  1 
ATOM   2656 C  CD  . GLN B 1 137 ? 18.49621 12.24921 95.21659  1.000 15.72841  ? 136 GLN B CD  1 
ATOM   2657 O  OE1 . GLN B 1 137 ? 18.69653 11.31425 94.43904  1.000 15.81456  ? 136 GLN B OE1 1 
ATOM   2658 N  NE2 . GLN B 1 137 ? 19.48374 12.94946 95.75907  1.000 16.63297  ? 136 GLN B NE2 1 
ATOM   2659 N  N   . ILE B 1 138 ? 14.13973 14.12547 96.56210  1.000 13.98204  ? 137 ILE B N   1 
ATOM   2660 C  CA  . ILE B 1 138 ? 13.87571 15.50170 96.96053  1.000 15.25649  ? 137 ILE B CA  1 
ATOM   2661 C  C   . ILE B 1 138 ? 15.19799 16.19036 97.27578  1.000 14.84301  ? 137 ILE B C   1 
ATOM   2662 O  O   . ILE B 1 138 ? 16.08744 15.60271 97.90684  1.000 15.28170  ? 137 ILE B O   1 
ATOM   2663 C  CB  . ILE B 1 138 ? 12.90345 15.54807 98.15241  1.000 12.97351  ? 137 ILE B CB  1 
ATOM   2664 C  CG1 . ILE B 1 138 ? 11.49798 15.18823 97.66924  1.000 14.90185  ? 137 ILE B CG1 1 
ATOM   2665 C  CG2 . ILE B 1 138 ? 12.92059 16.91836 98.82313  1.000 14.63722  ? 137 ILE B CG2 1 
ATOM   2666 C  CD1 . ILE B 1 138 ? 10.48917 15.00507 98.77394  1.000 19.51955  ? 137 ILE B CD1 1 
ATOM   2667 N  N   . ALA B 1 139 ? 15.33453 17.43692 96.82599  1.000 15.35943  ? 138 ALA B N   1 
ATOM   2668 C  CA  . ALA B 1 139 ? 16.52061 18.23399 97.10166  1.000 13.49936  ? 138 ALA B CA  1 
ATOM   2669 C  C   . ALA B 1 139 ? 16.11078 19.69294 97.20982  1.000 14.27898  ? 138 ALA B C   1 
ATOM   2670 O  O   . ALA B 1 139 ? 15.06601 20.10159 96.69932  1.000 17.20184  ? 138 ALA B O   1 
ATOM   2671 C  CB  . ALA B 1 139 ? 17.57484 18.08570 96.00005  1.000 15.22601  ? 138 ALA B CB  1 
ATOM   2672 N  N   . ALA B 1 140 ? 16.93884 20.47204 97.89680  1.000 14.56972  ? 139 ALA B N   1 
ATOM   2673 C  CA  . ALA B 1 140 ? 16.76669 21.91308 97.98738  1.000 15.55564  ? 139 ALA B CA  1 
ATOM   2674 C  C   . ALA B 1 140 ? 17.96538 22.59064 97.33911  1.000 14.90212  ? 139 ALA B C   1 
ATOM   2675 O  O   . ALA B 1 140 ? 19.08183 22.06141 97.36237  1.000 16.00968  ? 139 ALA B O   1 
ATOM   2676 C  CB  . ALA B 1 140 ? 16.63355 22.36906 99.44494  1.000 15.05704  ? 139 ALA B CB  1 
ATOM   2677 N  N   . CYS B 1 141 ? 17.72581 23.75957 96.74653  1.000 12.44022  ? 140 CYS B N   1 
ATOM   2678 C  CA  . CYS B 1 141 ? 18.77177 24.49749 96.06348  1.000 14.37926  ? 140 CYS B CA  1 
ATOM   2679 C  C   . CYS B 1 141 ? 18.75921 25.94058 96.54081  1.000 14.00383  ? 140 CYS B C   1 
ATOM   2680 O  O   . CYS B 1 141 ? 17.68715 26.53843 96.68834  1.000 12.81357  ? 140 CYS B O   1 
ATOM   2681 C  CB  . CYS B 1 141 ? 18.55955 24.48541 94.54451  1.000 13.89415  ? 140 CYS B CB  1 
ATOM   2682 S  SG  . CYS B 1 141 ? 18.54950 22.84225 93.80505  1.000 15.49863  ? 140 CYS B SG  1 
ATOM   2683 N  N   . PRO B 1 142 ? 19.92917 26.53010 96.77040  1.000 11.90564  ? 141 PRO B N   1 
ATOM   2684 C  CA  . PRO B 1 142 ? 19.98382 27.92787 97.21176  1.000 14.76202  ? 141 PRO B CA  1 
ATOM   2685 C  C   . PRO B 1 142 ? 19.87162 28.89644 96.04306  1.000 14.20661  ? 141 PRO B C   1 
ATOM   2686 O  O   . PRO B 1 142 ? 20.26941 28.59787 94.91388  1.000 13.06810  ? 141 PRO B O   1 
ATOM   2687 C  CB  . PRO B 1 142 ? 21.37946 28.02852 97.83856  1.000 13.51205  ? 141 PRO B CB  1 
ATOM   2688 C  CG  . PRO B 1 142 ? 22.19602 27.06728 97.01413  1.000 13.08277  ? 141 PRO B CG  1 
ATOM   2689 C  CD  . PRO B 1 142 ? 21.26724 25.91156 96.69450  1.000 14.25216  ? 141 PRO B CD  1 
ATOM   2690 N  N   . ASN B 1 143 ? 19.30969 30.07341 96.33344  1.000 12.33993  ? 142 ASN B N   1 
ATOM   2691 C  CA  . ASN B 1 143 ? 19.27698 31.20939 95.40146  1.000 12.49463  ? 142 ASN B CA  1 
ATOM   2692 C  C   . ASN B 1 143 ? 18.60164 30.77649 94.10549  1.000 13.00431  ? 142 ASN B C   1 
ATOM   2693 O  O   . ASN B 1 143 ? 17.44423 30.32132 94.15849  1.000 12.76575  ? 142 ASN B O   1 
ATOM   2694 C  CB  . ASN B 1 143 ? 20.68525 31.79875 95.28988  1.000 13.55877  ? 142 ASN B CB  1 
ATOM   2695 C  CG  . ASN B 1 143 ? 21.19002 32.30477 96.61049  1.000 13.29174  ? 142 ASN B CG  1 
ATOM   2696 O  OD1 . ASN B 1 143 ? 20.44077 32.92162 97.36709  1.000 15.27287  ? 142 ASN B OD1 1 
ATOM   2697 N  ND2 . ASN B 1 143 ? 22.44878 32.02955 96.91331  1.000 17.51130  ? 142 ASN B ND2 1 
ATOM   2698 N  N   . GLN B 1 144 ? 19.23678 30.92243 92.94275  1.000 11.52847  ? 143 GLN B N   1 
ATOM   2699 C  CA  . GLN B 1 144 ? 18.69944 30.39719 91.69461  1.000 12.13181  ? 143 GLN B CA  1 
ATOM   2700 C  C   . GLN B 1 144 ? 19.50016 29.21272 91.17152  1.000 12.95619  ? 143 GLN B C   1 
ATOM   2701 O  O   . GLN B 1 144 ? 19.34498 28.84779 90.00429  1.000 13.64260  ? 143 GLN B O   1 
ATOM   2702 C  CB  . GLN B 1 144 ? 18.61036 31.48425 90.62057  1.000 13.65612  ? 143 GLN B CB  1 
ATOM   2703 C  CG  . GLN B 1 144 ? 17.68706 32.65296 90.95664  1.000 14.08327  ? 143 GLN B CG  1 
ATOM   2704 C  CD  . GLN B 1 144 ? 16.22373 32.25327 91.14133  1.000 13.71870  ? 143 GLN B CD  1 
ATOM   2705 O  OE1 . GLN B 1 144 ? 15.79431 31.16302 90.74685  1.000 13.67280  ? 143 GLN B OE1 1 
ATOM   2706 N  NE2 . GLN B 1 144 ? 15.45119 33.14708 91.75035  1.000 14.58932  ? 143 GLN B NE2 1 
ATOM   2707 N  N   . ASP B 1 145 ? 20.35599 28.61031 92.00339  1.000 13.52560  ? 144 ASP B N   1 
ATOM   2708 C  CA  . ASP B 1 145 ? 21.12105 27.44790 91.57825  1.000 13.67944  ? 144 ASP B CA  1 
ATOM   2709 C  C   . ASP B 1 145 ? 20.15712 26.40057 91.02803  1.000 13.88187  ? 144 ASP B C   1 
ATOM   2710 O  O   . ASP B 1 145 ? 19.25539 25.96201 91.75522  1.000 14.32426  ? 144 ASP B O   1 
ATOM   2711 C  CB  . ASP B 1 145 ? 21.89407 26.84509 92.75039  1.000 12.33969  ? 144 ASP B CB  1 
ATOM   2712 C  CG  . ASP B 1 145 ? 23.07946 27.68130 93.17904  1.000 15.12047  ? 144 ASP B CG  1 
ATOM   2713 O  OD1 . ASP B 1 145 ? 23.10040 28.89727 92.90490  1.000 16.17701  ? 144 ASP B OD1 1 
ATOM   2714 O  OD2 . ASP B 1 145 ? 24.00382 27.09827 93.79501  1.000 17.93738  ? 144 ASP B OD2 1 
ATOM   2715 N  N   . PRO B 1 146 ? 20.27114 26.01957 89.75836  1.000 12.56713  ? 145 PRO B N   1 
ATOM   2716 C  CA  . PRO B 1 146 ? 19.28352 25.10740 89.17530  1.000 13.24856  ? 145 PRO B CA  1 
ATOM   2717 C  C   . PRO B 1 146 ? 19.56543 23.65652 89.53011  1.000 13.98563  ? 145 PRO B C   1 
ATOM   2718 O  O   . PRO B 1 146 ? 20.70813 23.25167 89.76136  1.000 14.53116  ? 145 PRO B O   1 
ATOM   2719 C  CB  . PRO B 1 146 ? 19.44583 25.33981 87.67001  1.000 13.89568  ? 145 PRO B CB  1 
ATOM   2720 C  CG  . PRO B 1 146 ? 20.88555 25.70320 87.51951  1.000 15.35737  ? 145 PRO B CG  1 
ATOM   2721 C  CD  . PRO B 1 146 ? 21.23749 26.50140 88.75731  1.000 14.93854  ? 145 PRO B CD  1 
ATOM   2722 N  N   . LEU B 1 147 ? 18.49234 22.86145 89.54328  1.000 13.87054  ? 146 LEU B N   1 
ATOM   2723 C  CA  . LEU B 1 147 ? 18.59265 21.49198 90.03822  1.000 12.81467  ? 146 LEU B CA  1 
ATOM   2724 C  C   . LEU B 1 147 ? 19.52680 20.64814 89.17712  1.000 14.02626  ? 146 LEU B C   1 
ATOM   2725 O  O   . LEU B 1 147 ? 20.49402 20.06667 89.67832  1.000 14.48220  ? 146 LEU B O   1 
ATOM   2726 C  CB  . LEU B 1 147 ? 17.20293 20.85439 90.12239  1.000 12.44105  ? 146 LEU B CB  1 
ATOM   2727 C  CG  . LEU B 1 147 ? 17.21009 19.44635 90.72388  1.000 14.01373  ? 146 LEU B CG  1 
ATOM   2728 C  CD1 . LEU B 1 147 ? 17.56357 19.48623 92.19639  1.000 16.33509  ? 146 LEU B CD1 1 
ATOM   2729 C  CD2 . LEU B 1 147 ? 15.86413 18.77456 90.51505  1.000 14.82648  ? 146 LEU B CD2 1 
ATOM   2730 N  N   . GLN B 1 148 ? 19.25248 20.56523 87.87329  1.000 13.21346  ? 147 GLN B N   1 
ATOM   2731 C  CA  . GLN B 1 148 ? 20.02652 19.65688 87.03286  1.000 15.66184  ? 147 GLN B CA  1 
ATOM   2732 C  C   . GLN B 1 148 ? 21.46672 20.13102 86.89011  1.000 16.95963  ? 147 GLN B C   1 
ATOM   2733 O  O   . GLN B 1 148 ? 22.40156 19.32339 86.96097  1.000 15.34542  ? 147 GLN B O   1 
ATOM   2734 C  CB  . GLN B 1 148 ? 19.36664 19.49591 85.66285  1.000 15.02866  ? 147 GLN B CB  1 
ATOM   2735 C  CG  . GLN B 1 148 ? 19.98960 18.39788 84.81493  1.000 17.64117  ? 147 GLN B CG  1 
ATOM   2736 C  CD  . GLN B 1 148 ? 19.39374 18.32505 83.41904  1.000 23.44092  ? 147 GLN B CD  1 
ATOM   2737 O  OE1 . GLN B 1 148 ? 18.38081 18.95854 83.12760  1.000 23.60290  ? 147 GLN B OE1 1 
ATOM   2738 N  NE2 . GLN B 1 148 ? 20.03406 17.55988 82.54385  1.000 25.97456  ? 147 GLN B NE2 1 
ATOM   2739 N  N   . GLY B 1 149 ? 21.66500 21.43817 86.71775  1.000 14.35154  ? 148 GLY B N   1 
ATOM   2740 C  CA  . GLY B 1 149 ? 23.00766 21.95801 86.51738  1.000 12.98246  ? 148 GLY B CA  1 
ATOM   2741 C  C   . GLY B 1 149 ? 23.92071 21.78989 87.71418  1.000 15.88629  ? 148 GLY B C   1 
ATOM   2742 O  O   . GLY B 1 149 ? 25.13848 21.68538 87.55049  1.000 18.65487  ? 148 GLY B O   1 
ATOM   2743 N  N   . THR B 1 150 ? 23.36354 21.77008 88.92859  1.000 14.96498  ? 149 THR B N   1 
ATOM   2744 C  CA  . THR B 1 150 ? 24.18517 21.67821 90.12737  1.000 16.28300  ? 149 THR B CA  1 
ATOM   2745 C  C   . THR B 1 150 ? 24.15065 20.32235 90.82065  1.000 17.53190  ? 149 THR B C   1 
ATOM   2746 O  O   . THR B 1 150 ? 25.04225 20.04953 91.63200  1.000 20.22407  ? 149 THR B O   1 
ATOM   2747 C  CB  . THR B 1 150 ? 23.81961 22.77462 91.14132  1.000 18.18497  ? 149 THR B CB  1 
ATOM   2748 O  OG1 . THR B 1 150 ? 22.47126 22.58552 91.59435  1.000 18.36153  ? 149 THR B OG1 1 
ATOM   2749 C  CG2 . THR B 1 150 ? 23.94918 24.14276 90.50645  1.000 15.30989  ? 149 THR B CG2 1 
ATOM   2750 N  N   . THR B 1 151 ? 23.16050 19.46662 90.52702  1.000 15.19686  ? 150 THR B N   1 
ATOM   2751 C  CA  . THR B 1 151 ? 23.04368 18.15882 91.16784  1.000 19.92316  ? 150 THR B CA  1 
ATOM   2752 C  C   . THR B 1 151 ? 22.91171 16.99630 90.19971  1.000 19.24137  ? 150 THR B C   1 
ATOM   2753 O  O   . THR B 1 151 ? 23.06051 15.84882 90.63225  1.000 17.73917  ? 150 THR B O   1 
ATOM   2754 C  CB  . THR B 1 151 ? 21.83697 18.10439 92.12382  1.000 17.74362  ? 150 THR B CB  1 
ATOM   2755 O  OG1 . THR B 1 151 ? 20.62174 17.98737 91.36743  1.000 17.15097  ? 150 THR B OG1 1 
ATOM   2756 C  CG2 . THR B 1 151 ? 21.76697 19.34654 92.99777  1.000 18.03684  ? 150 THR B CG2 1 
ATOM   2757 N  N   . GLY B 1 152 ? 22.62044 17.24177 88.92272  1.000 15.82257  ? 151 GLY B N   1 
ATOM   2758 C  CA  . GLY B 1 152 ? 22.35974 16.17698 87.97943  1.000 16.73699  ? 151 GLY B CA  1 
ATOM   2759 C  C   . GLY B 1 152 ? 20.96122 15.59759 88.02365  1.000 15.22558  ? 151 GLY B C   1 
ATOM   2760 O  O   . GLY B 1 152 ? 20.58163 14.86828 87.09575  1.000 17.40994  ? 151 GLY B O   1 
ATOM   2761 N  N   . LEU B 1 153 ? 20.17948 15.89992 89.05715  1.000 16.17881  ? 152 LEU B N   1 
ATOM   2762 C  CA  . LEU B 1 153 ? 18.81181 15.40813 89.13282  1.000 14.87872  ? 152 LEU B CA  1 
ATOM   2763 C  C   . LEU B 1 153 ? 17.94346 16.12460 88.10829  1.000 16.77312  ? 152 LEU B C   1 
ATOM   2764 O  O   . LEU B 1 153 ? 18.11119 17.31889 87.85715  1.000 15.29506  ? 152 LEU B O   1 
ATOM   2765 C  CB  . LEU B 1 153 ? 18.24636 15.65852 90.53036  1.000 16.75064  ? 152 LEU B CB  1 
ATOM   2766 C  CG  . LEU B 1 153 ? 18.99097 15.00580 91.69590  1.000 15.38455  ? 152 LEU B CG  1 
ATOM   2767 C  CD1 . LEU B 1 153 ? 18.37139 15.42801 93.01263  1.000 18.50684  ? 152 LEU B CD1 1 
ATOM   2768 C  CD2 . LEU B 1 153 ? 18.98156 13.48638 91.56630  1.000 16.28322  ? 152 LEU B CD2 1 
ATOM   2769 N  N   . ILE B 1 154 ? 17.02372 15.38537 87.49892  1.000 15.41274  ? 153 ILE B N   1 
ATOM   2770 C  CA  . ILE B 1 154 ? 16.10219 15.96121 86.52059  1.000 14.25607  ? 153 ILE B CA  1 
ATOM   2771 C  C   . ILE B 1 154 ? 14.92185 16.58030 87.25860  1.000 14.88587  ? 153 ILE B C   1 
ATOM   2772 O  O   . ILE B 1 154 ? 14.23831 15.87922 88.02202  1.000 14.71011  ? 153 ILE B O   1 
ATOM   2773 C  CB  . ILE B 1 154 ? 15.62147 14.90433 85.51465  1.000 17.77862  ? 153 ILE B CB  1 
ATOM   2774 C  CG1 . ILE B 1 154 ? 16.81777 14.19023 84.88003  1.000 17.67648  ? 153 ILE B CG1 1 
ATOM   2775 C  CG2 . ILE B 1 154 ? 14.73890 15.54675 84.45594  1.000 17.91351  ? 153 ILE B CG2 1 
ATOM   2776 C  CD1 . ILE B 1 154 ? 17.78334 15.10942 84.16432  1.000 25.69196  ? 153 ILE B CD1 1 
ATOM   2777 N  N   . PRO B 1 155 ? 14.63190 17.86580 87.05200  1.000 14.19941  ? 154 PRO B N   1 
ATOM   2778 C  CA  . PRO B 1 155 ? 13.53673 18.50428 87.79548  1.000 16.18279  ? 154 PRO B CA  1 
ATOM   2779 C  C   . PRO B 1 155 ? 12.17645 17.99949 87.32902  1.000 16.26109  ? 154 PRO B C   1 
ATOM   2780 O  O   . PRO B 1 155 ? 11.90659 17.90290 86.12907  1.000 16.67652  ? 154 PRO B O   1 
ATOM   2781 C  CB  . PRO B 1 155 ? 13.71733 19.99108 87.47696  1.000 13.11972  ? 154 PRO B CB  1 
ATOM   2782 C  CG  . PRO B 1 155 ? 14.37303 19.99540 86.12705  1.000 15.82800  ? 154 PRO B CG  1 
ATOM   2783 C  CD  . PRO B 1 155 ? 15.30563 18.80791 86.14119  1.000 14.88244  ? 154 PRO B CD  1 
ATOM   2784 N  N   . LEU B 1 156 ? 11.31546 17.68460 88.29384  1.000 12.15420  ? 155 LEU B N   1 
ATOM   2785 C  CA  . LEU B 1 156 ? 9.93080  17.31576 88.02985  1.000 13.29291  ? 155 LEU B CA  1 
ATOM   2786 C  C   . LEU B 1 156 ? 8.94184  18.35027 88.54720  1.000 14.13224  ? 155 LEU B C   1 
ATOM   2787 O  O   . LEU B 1 156 ? 8.00634  18.73238 87.83217  1.000 13.83064  ? 155 LEU B O   1 
ATOM   2788 C  CB  . LEU B 1 156 ? 9.64141  15.94941 88.66690  1.000 15.27690  ? 155 LEU B CB  1 
ATOM   2789 C  CG  . LEU B 1 156 ? 10.56509 14.80281 88.25192  1.000 14.60947  ? 155 LEU B CG  1 
ATOM   2790 C  CD1 . LEU B 1 156 ? 10.13543 13.53150 88.94050  1.000 16.27214  ? 155 LEU B CD1 1 
ATOM   2791 C  CD2 . LEU B 1 156 ? 10.55729 14.62002 86.74460  1.000 16.80564  ? 155 LEU B CD2 1 
ATOM   2792 N  N   . LEU B 1 157 ? 9.11490  18.79599 89.79085  1.000 13.78145  ? 156 LEU B N   1 
ATOM   2793 C  CA  . LEU B 1 157 ? 8.23800  19.76760 90.42798  1.000 10.60858  ? 156 LEU B CA  1 
ATOM   2794 C  C   . LEU B 1 157 ? 9.08689  20.66376 91.31577  1.000 13.36932  ? 156 LEU B C   1 
ATOM   2795 O  O   . LEU B 1 157 ? 9.80816  20.17431 92.18986  1.000 14.31704  ? 156 LEU B O   1 
ATOM   2796 C  CB  . LEU B 1 157 ? 7.16899  19.06213 91.27818  1.000 12.23396  ? 156 LEU B CB  1 
ATOM   2797 C  CG  . LEU B 1 157 ? 6.34510  19.99133 92.17109  1.000 12.71726  ? 156 LEU B CG  1 
ATOM   2798 C  CD1 . LEU B 1 157 ? 5.59215  21.00082 91.32013  1.000 14.93486  ? 156 LEU B CD1 1 
ATOM   2799 C  CD2 . LEU B 1 157 ? 5.38929  19.19584 93.03217  1.000 15.62690  ? 156 LEU B CD2 1 
ATOM   2800 N  N   . GLY B 1 158 ? 8.99671  21.96239 91.09985  1.000 13.07316  ? 157 GLY B N   1 
ATOM   2801 C  CA  . GLY B 1 158 ? 9.74810  22.93150 91.88429  1.000 12.70217  ? 157 GLY B CA  1 
ATOM   2802 C  C   . GLY B 1 158 ? 8.82714  23.84081 92.67095  1.000 12.57916  ? 157 GLY B C   1 
ATOM   2803 O  O   . GLY B 1 158 ? 7.75078  24.21031 92.19160  1.000 14.20600  ? 157 GLY B O   1 
ATOM   2804 N  N   . ILE B 1 159 ? 9.25266  24.18625 93.88375  1.000 14.42830  ? 158 ILE B N   1 
ATOM   2805 C  CA  . ILE B 1 159 ? 8.54637  25.12488 94.75329  1.000 14.67198  ? 158 ILE B CA  1 
ATOM   2806 C  C   . ILE B 1 159 ? 9.48211  26.30065 95.01819  1.000 14.16955  ? 158 ILE B C   1 
ATOM   2807 O  O   . ILE B 1 159 ? 10.51020 26.14919 95.69306  1.000 13.04787  ? 158 ILE B O   1 
ATOM   2808 C  CB  . ILE B 1 159 ? 8.10681  24.47683 96.07258  1.000 14.86421  ? 158 ILE B CB  1 
ATOM   2809 C  CG1 . ILE B 1 159 ? 7.39455  23.14500 95.81735  1.000 23.92563  ? 158 ILE B CG1 1 
ATOM   2810 C  CG2 . ILE B 1 159 ? 7.20204  25.42777 96.84497  1.000 17.46109  ? 158 ILE B CG2 1 
ATOM   2811 C  CD1 . ILE B 1 159 ? 6.06282  23.27982 95.12835  1.000 24.24226  ? 158 ILE B CD1 1 
ATOM   2812 N  N   . ASP B 1 160 ? 9.13260  27.47001 94.49154  1.000 12.85306  ? 159 ASP B N   1 
ATOM   2813 C  CA  . ASP B 1 160 ? 9.92718  28.67672 94.69800  1.000 12.39311  ? 159 ASP B CA  1 
ATOM   2814 C  C   . ASP B 1 160 ? 9.65647  29.21106 96.09887  1.000 12.35167  ? 159 ASP B C   1 
ATOM   2815 O  O   . ASP B 1 160 ? 8.50665  29.51530 96.43154  1.000 13.38846  ? 159 ASP B O   1 
ATOM   2816 C  CB  . ASP B 1 160 ? 9.52578  29.70622 93.64556  1.000 12.24066  ? 159 ASP B CB  1 
ATOM   2817 C  CG  . ASP B 1 160 ? 10.42629 30.92040 93.61391  1.000 14.59254  ? 159 ASP B CG  1 
ATOM   2818 O  OD1 . ASP B 1 160 ? 11.38989 31.02949 94.41018  1.000 13.93151  ? 159 ASP B OD1 1 
ATOM   2819 O  OD2 . ASP B 1 160 ? 10.17647 31.76666 92.73995  1.000 13.79468  ? 159 ASP B OD2 1 
ATOM   2820 N  N   . VAL B 1 161 ? 10.69842 29.30672 96.92775  1.000 11.67402  ? 160 VAL B N   1 
ATOM   2821 C  CA  . VAL B 1 161 ? 10.53885 29.83031 98.27970  1.000 13.78246  ? 160 VAL B CA  1 
ATOM   2822 C  C   . VAL B 1 161 ? 11.32089 31.12585 98.50689  1.000 13.35313  ? 160 VAL B C   1 
ATOM   2823 O  O   . VAL B 1 161 ? 11.54210 31.51793 99.64521  1.000 13.42612  ? 160 VAL B O   1 
ATOM   2824 C  CB  . VAL B 1 161 ? 10.79911 28.77093 99.37105  1.000 13.42006  ? 160 VAL B CB  1 
ATOM   2825 C  CG1 . VAL B 1 161 ? 9.74480  27.66480 99.29264  1.000 15.09637  ? 160 VAL B CG1 1 
ATOM   2826 C  CG2 . VAL B 1 161 ? 12.21380 28.20303 99.27349  1.000 13.48283  ? 160 VAL B CG2 1 
ATOM   2827 N  N   . TRP B 1 162 ? 11.74664 31.79633 97.43538  1.000 12.39524  ? 161 TRP B N   1 
ATOM   2828 C  CA  . TRP B 1 162 ? 12.13767 33.19389 97.55711  1.000 11.58960  ? 161 TRP B CA  1 
ATOM   2829 C  C   . TRP B 1 162 ? 10.95740 33.98856 98.10420  1.000 13.10933  ? 161 TRP B C   1 
ATOM   2830 O  O   . TRP B 1 162 ? 9.79251  33.68518 97.82540  1.000 12.89678  ? 161 TRP B O   1 
ATOM   2831 C  CB  . TRP B 1 162 ? 12.46923 33.76018 96.18038  1.000 12.61507  ? 161 TRP B CB  1 
ATOM   2832 C  CG  . TRP B 1 162 ? 13.82595 33.43099 95.66398  1.000 10.44459  ? 161 TRP B CG  1 
ATOM   2833 C  CD1 . TRP B 1 162 ? 14.31156 32.19277 95.35256  1.000 12.87245  ? 161 TRP B CD1 1 
ATOM   2834 C  CD2 . TRP B 1 162 ? 14.86652 34.36301 95.35095  1.000 11.13362  ? 161 TRP B CD2 1 
ATOM   2835 N  NE1 . TRP B 1 162 ? 15.60512 32.29702 94.88862  1.000 14.97917  ? 161 TRP B NE1 1 
ATOM   2836 C  CE2 . TRP B 1 162 ? 15.96516 33.61905 94.87334  1.000 13.51342  ? 161 TRP B CE2 1 
ATOM   2837 C  CE3 . TRP B 1 162 ? 14.98036 35.75326 95.44474  1.000 14.76721  ? 161 TRP B CE3 1 
ATOM   2838 C  CZ2 . TRP B 1 162 ? 17.16171 34.21916 94.49229  1.000 15.67413  ? 161 TRP B CZ2 1 
ATOM   2839 C  CZ3 . TRP B 1 162 ? 16.16686 36.34860 95.06823  1.000 15.50306  ? 161 TRP B CZ3 1 
ATOM   2840 C  CH2 . TRP B 1 162 ? 17.23975 35.58214 94.58932  1.000 14.82548  ? 161 TRP B CH2 1 
ATOM   2841 N  N   . GLU B 1 163 ? 11.26086 35.02825 98.88189  1.000 11.78279  ? 162 GLU B N   1 
ATOM   2842 C  CA  . GLU B 1 163 ? 10.18378 35.80340 99.48738  1.000 12.40097  ? 162 GLU B CA  1 
ATOM   2843 C  C   . GLU B 1 163 ? 9.27031  36.43092 98.43979  1.000 13.03230  ? 162 GLU B C   1 
ATOM   2844 O  O   . GLU B 1 163 ? 8.05978  36.52527 98.65878  1.000 13.57702  ? 162 GLU B O   1 
ATOM   2845 C  CB  . GLU B 1 163 ? 10.75634 36.83409 100.46498 1.000 12.76163  ? 162 GLU B CB  1 
ATOM   2846 C  CG  . GLU B 1 163 ? 11.24914 36.17604 101.75008 1.000 14.33082  ? 162 GLU B CG  1 
ATOM   2847 C  CD  . GLU B 1 163 ? 11.94580 37.12360 102.70385 1.000 13.83615  ? 162 GLU B CD  1 
ATOM   2848 O  OE1 . GLU B 1 163 ? 12.64654 38.04606 102.23311 1.000 13.09769  ? 162 GLU B OE1 1 
ATOM   2849 O  OE2 . GLU B 1 163 ? 11.81083 36.93043 103.93265 1.000 14.90723  ? 162 GLU B OE2 1 
ATOM   2850 N  N   . HIS B 1 164 ? 9.80737  36.82275 97.28044  1.000 13.12774  ? 163 HIS B N   1 
ATOM   2851 C  CA  . HIS B 1 164 ? 8.94432  37.38279 96.24449  1.000 13.09628  ? 163 HIS B CA  1 
ATOM   2852 C  C   . HIS B 1 164 ? 7.91019  36.38147 95.73748  1.000 12.32936  ? 163 HIS B C   1 
ATOM   2853 O  O   . HIS B 1 164 ? 6.91930  36.79136 95.12456  1.000 15.94179  ? 163 HIS B O   1 
ATOM   2854 C  CB  . HIS B 1 164 ? 9.75831  37.95722 95.07710  1.000 13.05445  ? 163 HIS B CB  1 
ATOM   2855 C  CG  . HIS B 1 164 ? 10.49738 36.92571 94.27880  1.000 14.10782  ? 163 HIS B CG  1 
ATOM   2856 N  ND1 . HIS B 1 164 ? 11.87215 36.90259 94.18795  1.000 12.87398  ? 163 HIS B ND1 1 
ATOM   2857 C  CD2 . HIS B 1 164 ? 10.05306 35.89418 93.52184  1.000 12.97091  ? 163 HIS B CD2 1 
ATOM   2858 C  CE1 . HIS B 1 164 ? 12.24348 35.89390 93.41807  1.000 13.83315  ? 163 HIS B CE1 1 
ATOM   2859 N  NE2 . HIS B 1 164 ? 11.15974 35.26087 93.00725  1.000 16.00078  ? 163 HIS B NE2 1 
ATOM   2860 N  N   . ALA B 1 165 ? 8.10098  35.08687 95.98667  1.000 12.31389  ? 164 ALA B N   1 
ATOM   2861 C  CA  . ALA B 1 165 ? 7.11061  34.11706 95.54234  1.000 11.99898  ? 164 ALA B CA  1 
ATOM   2862 C  C   . ALA B 1 165 ? 5.84646  34.14163 96.39281  1.000 10.73371  ? 164 ALA B C   1 
ATOM   2863 O  O   . ALA B 1 165 ? 4.82222  33.59800 95.96047  1.000 12.78468  ? 164 ALA B O   1 
ATOM   2864 C  CB  . ALA B 1 165 ? 7.71012  32.70919 95.53269  1.000 13.70057  ? 164 ALA B CB  1 
ATOM   2865 N  N   . TYR B 1 166 ? 5.88366  34.76078 97.57966  1.000 11.28572  ? 165 TYR B N   1 
ATOM   2866 C  CA  . TYR B 1 166 ? 4.75292  34.65376 98.50131  1.000 11.48032  ? 165 TYR B CA  1 
ATOM   2867 C  C   . TYR B 1 166 ? 4.50532  35.87002 99.38939  1.000 11.67007  ? 165 TYR B C   1 
ATOM   2868 O  O   . TYR B 1 166 ? 3.41907  35.99348 99.96188  1.000 12.90635  ? 165 TYR B O   1 
ATOM   2869 C  CB  . TYR B 1 166 ? 4.90654  33.41183 99.39341  1.000 12.98639  ? 165 TYR B CB  1 
ATOM   2870 C  CG  . TYR B 1 166 ? 6.13326  33.37230 100.29758 1.000 13.23777  ? 165 TYR B CG  1 
ATOM   2871 C  CD1 . TYR B 1 166 ? 6.14497  34.00561 101.54063 1.000 13.67247  ? 165 TYR B CD1 1 
ATOM   2872 C  CD2 . TYR B 1 166 ? 7.27226  32.68213 99.91217  1.000 11.52783  ? 165 TYR B CD2 1 
ATOM   2873 C  CE1 . TYR B 1 166 ? 7.26154  33.95131 102.37056 1.000 13.23948  ? 165 TYR B CE1 1 
ATOM   2874 C  CE2 . TYR B 1 166 ? 8.39356  32.61115 100.74042 1.000 11.66838  ? 165 TYR B CE2 1 
ATOM   2875 C  CZ  . TYR B 1 166 ? 8.38672  33.25593 101.95957 1.000 13.03801  ? 165 TYR B CZ  1 
ATOM   2876 O  OH  . TYR B 1 166 ? 9.49921  33.17734 102.77235 1.000 14.12644  ? 165 TYR B OH  1 
ATOM   2877 N  N   . TYR B 1 167 ? 5.47832  36.77717 99.51377  1.000 12.42768  ? 166 TYR B N   1 
ATOM   2878 C  CA  . TYR B 1 167 ? 5.46177  37.72868 100.62786 1.000 11.46624  ? 166 TYR B CA  1 
ATOM   2879 C  C   . TYR B 1 167 ? 4.28646  38.69850 100.56417 1.000 13.86086  ? 166 TYR B C   1 
ATOM   2880 O  O   . TYR B 1 167 ? 3.70356  39.02633 101.60171 1.000 13.37592  ? 166 TYR B O   1 
ATOM   2881 C  CB  . TYR B 1 167 ? 6.77943  38.49825 100.72141 1.000 15.56568  ? 166 TYR B CB  1 
ATOM   2882 C  CG  . TYR B 1 167 ? 7.02585  39.01629 102.12148 1.000 14.01581  ? 166 TYR B CG  1 
ATOM   2883 C  CD1 . TYR B 1 167 ? 7.66176  38.22043 103.06876 1.000 11.42064  ? 166 TYR B CD1 1 
ATOM   2884 C  CD2 . TYR B 1 167 ? 6.57110  40.26929 102.51487 1.000 13.95146  ? 166 TYR B CD2 1 
ATOM   2885 C  CE1 . TYR B 1 167 ? 7.87471  38.67506 104.35783 1.000 13.08486  ? 166 TYR B CE1 1 
ATOM   2886 C  CE2 . TYR B 1 167 ? 6.77449  40.72892 103.80300 1.000 14.26267  ? 166 TYR B CE2 1 
ATOM   2887 C  CZ  . TYR B 1 167 ? 7.42562  39.93108 104.71793 1.000 12.66761  ? 166 TYR B CZ  1 
ATOM   2888 O  OH  . TYR B 1 167 ? 7.62664  40.39919 105.99808 1.000 14.98386  ? 166 TYR B OH  1 
ATOM   2889 N  N   . LEU B 1 168 ? 3.94832  39.20318 99.37405  1.000 14.32661  ? 167 LEU B N   1 
ATOM   2890 C  CA  . LEU B 1 168 ? 2.86073  40.17642 99.28615  1.000 14.80655  ? 167 LEU B CA  1 
ATOM   2891 C  C   . LEU B 1 168 ? 1.57264  39.61933 99.87766  1.000 13.71954  ? 167 LEU B C   1 
ATOM   2892 O  O   . LEU B 1 168 ? 0.78789  40.35587 100.49075 1.000 15.58338  ? 167 LEU B O   1 
ATOM   2893 C  CB  . LEU B 1 168 ? 2.62804  40.58288 97.83307  1.000 16.44186  ? 167 LEU B CB  1 
ATOM   2894 C  CG  . LEU B 1 168 ? 3.64215  41.48313 97.14240  1.000 15.12179  ? 167 LEU B CG  1 
ATOM   2895 C  CD1 . LEU B 1 168 ? 3.24829  41.63566 95.69316  1.000 17.59780  ? 167 LEU B CD1 1 
ATOM   2896 C  CD2 . LEU B 1 168 ? 3.71393  42.84435 97.82529  1.000 21.63029  ? 167 LEU B CD2 1 
ATOM   2897 N  N   . GLN B 1 169 ? 1.34365  38.31939 99.71504  1.000 11.05992  ? 168 GLN B N   1 
ATOM   2898 C  CA  . GLN B 1 169 ? 0.09642  37.68806 100.12168 1.000 12.45718  ? 168 GLN B CA  1 
ATOM   2899 C  C   . GLN B 1 169 ? 0.17841  37.06709 101.50815 1.000 14.87969  ? 168 GLN B C   1 
ATOM   2900 O  O   . GLN B 1 169 ? -0.71198 37.27251 102.34092 1.000 15.89032  ? 168 GLN B O   1 
ATOM   2901 C  CB  . GLN B 1 169 ? -0.25913 36.61482 99.09602  1.000 14.97863  ? 168 GLN B CB  1 
ATOM   2902 C  CG  . GLN B 1 169 ? -1.51842 35.84935 99.42162  1.000 14.58757  ? 168 GLN B CG  1 
ATOM   2903 C  CD  . GLN B 1 169 ? -1.92630 34.92779 98.29771  1.000 13.82366  ? 168 GLN B CD  1 
ATOM   2904 O  OE1 . GLN B 1 169 ? -1.26678 34.87341 97.25650  1.000 17.49501  ? 168 GLN B OE1 1 
ATOM   2905 N  NE2 . GLN B 1 169 ? -3.01725 34.19068 98.50087  1.000 15.81863  ? 168 GLN B NE2 1 
ATOM   2906 N  N   . TYR B 1 170 ? 1.24537  36.31911 101.77439 1.000 13.67524  ? 169 TYR B N   1 
ATOM   2907 C  CA  . TYR B 1 170 ? 1.38310  35.53460 102.98962 1.000 12.44206  ? 169 TYR B CA  1 
ATOM   2908 C  C   . TYR B 1 170 ? 2.35598  36.13699 103.98801 1.000 14.80814  ? 169 TYR B C   1 
ATOM   2909 O  O   . TYR B 1 170 ? 2.50582  35.58779 105.08757 1.000 15.21111  ? 169 TYR B O   1 
ATOM   2910 C  CB  . TYR B 1 170 ? 1.81901  34.10885 102.63568 1.000 15.16869  ? 169 TYR B CB  1 
ATOM   2911 C  CG  . TYR B 1 170 ? 0.80571  33.36452 101.79142 1.000 12.36775  ? 169 TYR B CG  1 
ATOM   2912 C  CD1 . TYR B 1 170 ? -0.32213 32.78079 102.37232 1.000 13.03750  ? 169 TYR B CD1 1 
ATOM   2913 C  CD2 . TYR B 1 170 ? 0.95752  33.26241 100.41066 1.000 13.22298  ? 169 TYR B CD2 1 
ATOM   2914 C  CE1 . TYR B 1 170 ? -1.24947 32.10715 101.60816 1.000 14.50420  ? 169 TYR B CE1 1 
ATOM   2915 C  CE2 . TYR B 1 170 ? 0.03311  32.57974 99.63698  1.000 12.85457  ? 169 TYR B CE2 1 
ATOM   2916 C  CZ  . TYR B 1 170 ? -1.07159 32.00762 100.24412 1.000 14.41470  ? 169 TYR B CZ  1 
ATOM   2917 O  OH  . TYR B 1 170 ? -2.00515 31.33058 99.49011  1.000 14.55308  ? 169 TYR B OH  1 
ATOM   2918 N  N   . LYS B 1 171 ? 3.01733  37.24319 103.63523 1.000 13.95528  ? 170 LYS B N   1 
ATOM   2919 C  CA  . LYS B 1 171 ? 3.99907  37.88647 104.49855 1.000 12.63583  ? 170 LYS B CA  1 
ATOM   2920 C  C   . LYS B 1 171 ? 5.05243  36.87508 104.93297 1.000 15.46243  ? 170 LYS B C   1 
ATOM   2921 O  O   . LYS B 1 171 ? 5.53443  36.07998 104.11925 1.000 16.17528  ? 170 LYS B O   1 
ATOM   2922 C  CB  . LYS B 1 171 ? 3.31294  38.55360 105.69893 1.000 14.86917  ? 170 LYS B CB  1 
ATOM   2923 C  CG  . LYS B 1 171 ? 2.06002  39.38435 105.34354 1.000 18.77315  ? 170 LYS B CG  1 
ATOM   2924 C  CD  . LYS B 1 171 ? 2.35630  40.49717 104.35081 1.000 18.17523  ? 170 LYS B CD  1 
ATOM   2925 C  CE  . LYS B 1 171 ? 1.12005  41.36877 104.06874 1.000 19.29473  ? 170 LYS B CE  1 
ATOM   2926 N  NZ  . LYS B 1 171 ? 0.03570  40.63947 103.36353 1.000 26.24393  ? 170 LYS B NZ  1 
ATOM   2927 N  N   . ASN B 1 172 ? 5.40239  36.88006 106.21609 1.000 15.55838  ? 171 ASN B N   1 
ATOM   2928 C  CA  . ASN B 1 172 ? 6.44193  35.99503 106.72350 1.000 15.87586  ? 171 ASN B CA  1 
ATOM   2929 C  C   . ASN B 1 172 ? 5.99993  34.53902 106.81317 1.000 13.90649  ? 171 ASN B C   1 
ATOM   2930 O  O   . ASN B 1 172 ? 6.85007  33.67040 107.04192 1.000 18.07741  ? 171 ASN B O   1 
ATOM   2931 C  CB  . ASN B 1 172 ? 6.85055  36.47470 108.11277 1.000 16.84421  ? 171 ASN B CB  1 
ATOM   2932 C  CG  . ASN B 1 172 ? 5.67945  36.49264 109.07083 1.000 17.22501  ? 171 ASN B CG  1 
ATOM   2933 O  OD1 . ASN B 1 172 ? 4.74035  37.27596 108.89579 1.000 16.37399  ? 171 ASN B OD1 1 
ATOM   2934 N  ND2 . ASN B 1 172 ? 5.72227  35.63734 110.08837 1.000 18.31131  ? 171 ASN B ND2 1 
ATOM   2935 N  N   . VAL B 1 173 ? 4.71410  34.24123 106.62142 1.000 14.03007  ? 172 VAL B N   1 
ATOM   2936 C  CA  . VAL B 1 173 ? 4.19604  32.90568 106.90236 1.000 14.86588  ? 172 VAL B CA  1 
ATOM   2937 C  C   . VAL B 1 173 ? 4.35739  32.00220 105.68672 1.000 15.38943  ? 172 VAL B C   1 
ATOM   2938 O  O   . VAL B 1 173 ? 3.37788  31.63616 105.02362 1.000 15.01115  ? 172 VAL B O   1 
ATOM   2939 C  CB  . VAL B 1 173 ? 2.73558  32.97567 107.38446 1.000 12.78962  ? 172 VAL B CB  1 
ATOM   2940 C  CG1 . VAL B 1 173 ? 2.33200  31.66079 108.04665 1.000 17.79116  ? 172 VAL B CG1 1 
ATOM   2941 C  CG2 . VAL B 1 173 ? 2.54973  34.14630 108.34980 1.000 16.86560  ? 172 VAL B CG2 1 
ATOM   2942 N  N   . ARG B 1 174 ? 5.59919  31.60356 105.42010 1.000 14.11953  ? 173 ARG B N   1 
ATOM   2943 C  CA  . ARG B 1 174 ? 5.86230  30.68869 104.31393 1.000 13.31895  ? 173 ARG B CA  1 
ATOM   2944 C  C   . ARG B 1 174 ? 5.08433  29.38145 104.39997 1.000 17.44161  ? 173 ARG B C   1 
ATOM   2945 O  O   . ARG B 1 174 ? 4.66523  28.88142 103.34199 1.000 15.93169  ? 173 ARG B O   1 
ATOM   2946 C  CB  . ARG B 1 174 ? 7.36853  30.42785 104.19254 1.000 16.31375  ? 173 ARG B CB  1 
ATOM   2947 C  CG  . ARG B 1 174 ? 7.76223  29.69495 102.91663 1.000 12.66155  ? 173 ARG B CG  1 
ATOM   2948 C  CD  . ARG B 1 174 ? 9.18387  29.14211 102.98649 1.000 14.77641  ? 173 ARG B CD  1 
ATOM   2949 N  NE  . ARG B 1 174 ? 10.19677 30.18649 103.08514 1.000 16.43979  ? 173 ARG B NE  1 
ATOM   2950 C  CZ  . ARG B 1 174 ? 11.49530 29.95006 103.21400 1.000 16.85314  ? 173 ARG B CZ  1 
ATOM   2951 N  NH1 . ARG B 1 174 ? 11.97333 28.71745 103.23126 1.000 15.93884  ? 173 ARG B NH1 1 
ATOM   2952 N  NH2 . ARG B 1 174 ? 12.33390 30.97476 103.34294 1.000 18.21156  ? 173 ARG B NH2 1 
ATOM   2953 N  N   . PRO B 1 175 ? 4.85541  28.77978 105.57345 1.000 16.72171  ? 174 PRO B N   1 
ATOM   2954 C  CA  . PRO B 1 175 ? 4.06962  27.53663 105.59288 1.000 14.12826  ? 174 PRO B CA  1 
ATOM   2955 C  C   . PRO B 1 175 ? 2.66998  27.67619 105.02042 1.000 14.71748  ? 174 PRO B C   1 
ATOM   2956 O  O   . PRO B 1 175 ? 2.15905  26.71818 104.43114 1.000 14.06307  ? 174 PRO B O   1 
ATOM   2957 C  CB  . PRO B 1 175 ? 4.05776  27.15563 107.07910 1.000 16.38739  ? 174 PRO B CB  1 
ATOM   2958 C  CG  . PRO B 1 175 ? 5.33405  27.73501 107.60618 1.000 15.76564  ? 174 PRO B CG  1 
ATOM   2959 C  CD  . PRO B 1 175 ? 5.44552  29.05354 106.89898 1.000 14.81307  ? 174 PRO B CD  1 
ATOM   2960 N  N   . ASP B 1 176 ? 2.03459  28.84024 105.15339 1.000 13.90397  ? 175 ASP B N   1 
ATOM   2961 C  CA  . ASP B 1 176 ? 0.70301  29.00256 104.57184 1.000 15.04694  ? 175 ASP B CA  1 
ATOM   2962 C  C   . ASP B 1 176 ? 0.76325  28.98494 103.04923 1.000 16.49872  ? 175 ASP B C   1 
ATOM   2963 O  O   . ASP B 1 176 ? -0.14210 28.45729 102.38906 1.000 13.90215  ? 175 ASP B O   1 
ATOM   2964 C  CB  . ASP B 1 176 ? 0.02590  30.27854 105.07673 1.000 17.11038  ? 175 ASP B CB  1 
ATOM   2965 C  CG  . ASP B 1 176 ? -0.43833 30.16601 106.51625 1.000 15.19348  ? 175 ASP B CG  1 
ATOM   2966 O  OD1 . ASP B 1 176 ? -0.20768 29.11549 107.14505 1.000 19.25817  ? 175 ASP B OD1 1 
ATOM   2967 O  OD2 . ASP B 1 176 ? -1.07388 31.12084 107.00740 1.000 22.50630  ? 175 ASP B OD2 1 
ATOM   2968 N  N   . TYR B 1 177 ? 1.81592  29.58098 102.48005 1.000 13.44486  ? 176 TYR B N   1 
ATOM   2969 C  CA  . TYR B 1 177 ? 2.03031  29.52614 101.03847 1.000 12.34359  ? 176 TYR B CA  1 
ATOM   2970 C  C   . TYR B 1 177 ? 2.24341  28.09297 100.57842 1.000 13.58113  ? 176 TYR B C   1 
ATOM   2971 O  O   . TYR B 1 177 ? 1.67448  27.66306 99.56799  1.000 14.64291  ? 176 TYR B O   1 
ATOM   2972 C  CB  . TYR B 1 177 ? 3.24174  30.39476 100.69363 1.000 13.37951  ? 176 TYR B CB  1 
ATOM   2973 C  CG  . TYR B 1 177 ? 3.90735  30.13655 99.35373  1.000 13.68323  ? 176 TYR B CG  1 
ATOM   2974 C  CD1 . TYR B 1 177 ? 3.24359  30.37610 98.15996  1.000 14.16191  ? 176 TYR B CD1 1 
ATOM   2975 C  CD2 . TYR B 1 177 ? 5.22643  29.70006 99.29201  1.000 12.79044  ? 176 TYR B CD2 1 
ATOM   2976 C  CE1 . TYR B 1 177 ? 3.86347  30.17233 96.93939  1.000 13.08607  ? 176 TYR B CE1 1 
ATOM   2977 C  CE2 . TYR B 1 177 ? 5.85835  29.49442 98.07551  1.000 14.87557  ? 176 TYR B CE2 1 
ATOM   2978 C  CZ  . TYR B 1 177 ? 5.17794  29.73481 96.90350  1.000 13.86776  ? 176 TYR B CZ  1 
ATOM   2979 O  OH  . TYR B 1 177 ? 5.80826  29.53706 95.69581  1.000 13.09197  ? 176 TYR B OH  1 
ATOM   2980 N  N   . LEU B 1 178 ? 3.04875  27.33082 101.32044 1.000 12.76192  ? 177 LEU B N   1 
ATOM   2981 C  CA  . LEU B 1 178 ? 3.31872  25.94832 100.94049 1.000 12.32554  ? 177 LEU B CA  1 
ATOM   2982 C  C   . LEU B 1 178 ? 2.05823  25.08972 100.98843 1.000 16.79011  ? 177 LEU B C   1 
ATOM   2983 O  O   . LEU B 1 178 ? 1.84922  24.24062 100.11642 1.000 18.09770  ? 177 LEU B O   1 
ATOM   2984 C  CB  . LEU B 1 178 ? 4.41760  25.36429 101.82595 1.000 17.32480  ? 177 LEU B CB  1 
ATOM   2985 C  CG  . LEU B 1 178 ? 5.80103  26.00179 101.66491 1.000 26.55285  ? 177 LEU B CG  1 
ATOM   2986 C  CD1 . LEU B 1 178 ? 6.84892  25.10666 102.27304 1.000 32.80290  ? 177 LEU B CD1 1 
ATOM   2987 C  CD2 . LEU B 1 178 ? 6.12690  26.27191 100.21195 1.000 19.96106  ? 177 LEU B CD2 1 
ATOM   2988 N  N   . LYS B 1 179 ? 1.20304  25.29404 101.99357 1.000 12.06136  ? 178 LYS B N   1 
ATOM   2989 C  CA  . LYS B 1 179 ? -0.05843 24.55920 102.02511 1.000 14.00448  ? 178 LYS B CA  1 
ATOM   2990 C  C   . LYS B 1 179 ? -0.93277 24.90673 100.82551 1.000 13.28561  ? 178 LYS B C   1 
ATOM   2991 O  O   . LYS B 1 179 ? -1.51484 24.01756 100.19107 1.000 15.65669  ? 178 LYS B O   1 
ATOM   2992 C  CB  . LYS B 1 179 ? -0.80374 24.82396 103.33005 1.000 17.10079  ? 178 LYS B CB  1 
ATOM   2993 C  CG  . LYS B 1 179 ? -2.08814 24.02255 103.43199 1.000 18.67938  ? 178 LYS B CG  1 
ATOM   2994 C  CD  . LYS B 1 179 ? -2.80025 24.24271 104.75110 1.000 22.74115  ? 178 LYS B CD  1 
ATOM   2995 C  CE  . LYS B 1 179 ? -4.01146 23.32572 104.85491 1.000 32.63563  ? 178 LYS B CE  1 
ATOM   2996 N  NZ  . LYS B 1 179 ? -4.73864 23.49904 106.14237 1.000 31.81323  ? 178 LYS B NZ  1 
ATOM   2997 N  N   . ALA B 1 180 ? -1.01634 26.19521 100.48438 1.000 13.08127  ? 179 ALA B N   1 
ATOM   2998 C  CA  . ALA B 1 180 ? -1.89734 26.62933 99.40686  1.000 14.14724  ? 179 ALA B CA  1 
ATOM   2999 C  C   . ALA B 1 180 ? -1.44443 26.13032 98.04202  1.000 12.75541  ? 179 ALA B C   1 
ATOM   3000 O  O   . ALA B 1 180 ? -2.28880 25.82516 97.19251  1.000 13.83692  ? 179 ALA B O   1 
ATOM   3001 C  CB  . ALA B 1 180 ? -1.99507 28.15370 99.39435  1.000 14.07932  ? 179 ALA B CB  1 
ATOM   3002 N  N   . ILE B 1 181 ? -0.13003 26.04125 97.80344  1.000 13.60068  ? 180 ILE B N   1 
ATOM   3003 C  CA  . ILE B 1 181 ? 0.34313  25.76071 96.45196  1.000 11.87768  ? 180 ILE B CA  1 
ATOM   3004 C  C   . ILE B 1 181 ? -0.06007 24.36438 95.98608  1.000 14.43322  ? 180 ILE B C   1 
ATOM   3005 O  O   . ILE B 1 181 ? -0.17706 24.12551 94.77825  1.000 13.94412  ? 180 ILE B O   1 
ATOM   3006 C  CB  . ILE B 1 181 ? 1.85394  26.04655 96.30672  1.000 14.41303  ? 180 ILE B CB  1 
ATOM   3007 C  CG1 . ILE B 1 181 ? 2.22934  26.21822 94.83007  1.000 13.50539  ? 180 ILE B CG1 1 
ATOM   3008 C  CG2 . ILE B 1 181 ? 2.67216  24.94055 96.94719  1.000 13.96465  ? 180 ILE B CG2 1 
ATOM   3009 C  CD1 . ILE B 1 181 ? 3.67417  26.65130 94.60817  1.000 13.42514  ? 180 ILE B CD1 1 
ATOM   3010 N  N   . TRP B 1 182 ? -0.30644 23.43702 96.91301  1.000 12.55675  ? 181 TRP B N   1 
ATOM   3011 C  CA  . TRP B 1 182 ? -0.72874 22.09876 96.51496  1.000 13.74179  ? 181 TRP B CA  1 
ATOM   3012 C  C   . TRP B 1 182 ? -2.03084 22.11622 95.72154  1.000 15.59209  ? 181 TRP B C   1 
ATOM   3013 O  O   . TRP B 1 182 ? -2.27342 21.19858 94.93285  1.000 15.49027  ? 181 TRP B O   1 
ATOM   3014 C  CB  . TRP B 1 182 ? -0.86399 21.19348 97.74330  1.000 14.74063  ? 181 TRP B CB  1 
ATOM   3015 C  CG  . TRP B 1 182 ? 0.44642  20.94926 98.41482  1.000 14.36579  ? 181 TRP B CG  1 
ATOM   3016 C  CD1 . TRP B 1 182 ? 0.86394  21.46813 99.60390  1.000 18.76530  ? 181 TRP B CD1 1 
ATOM   3017 C  CD2 . TRP B 1 182 ? 1.52454  20.14103 97.92583  1.000 13.51141  ? 181 TRP B CD2 1 
ATOM   3018 N  NE1 . TRP B 1 182 ? 2.13704  21.03355 99.88779  1.000 17.83428  ? 181 TRP B NE1 1 
ATOM   3019 C  CE2 . TRP B 1 182 ? 2.56585  20.21898 98.87300  1.000 18.37324  ? 181 TRP B CE2 1 
ATOM   3020 C  CE3 . TRP B 1 182 ? 1.71467  19.37004 96.77588  1.000 16.60547  ? 181 TRP B CE3 1 
ATOM   3021 C  CZ2 . TRP B 1 182 ? 3.77445  19.54602 98.71105  1.000 17.77563  ? 181 TRP B CZ2 1 
ATOM   3022 C  CZ3 . TRP B 1 182 ? 2.91687  18.70251 96.61572  1.000 21.84704  ? 181 TRP B CZ3 1 
ATOM   3023 C  CH2 . TRP B 1 182 ? 3.93159  18.79392 97.57999  1.000 17.10527  ? 181 TRP B CH2 1 
ATOM   3024 N  N   . ASN B 1 183 ? -2.85249 23.15456 95.87757  1.000 13.46534  ? 182 ASN B N   1 
ATOM   3025 C  CA  . ASN B 1 183 ? -4.11263 23.23337 95.14867  1.000 14.69976  ? 182 ASN B CA  1 
ATOM   3026 C  C   . ASN B 1 183 ? -3.92727 23.52797 93.66424  1.000 16.85482  ? 182 ASN B C   1 
ATOM   3027 O  O   . ASN B 1 183 ? -4.89394 23.41116 92.90823  1.000 15.85735  ? 182 ASN B O   1 
ATOM   3028 C  CB  . ASN B 1 183 ? -5.01227 24.31077 95.75895  1.000 13.80066  ? 182 ASN B CB  1 
ATOM   3029 C  CG  . ASN B 1 183 ? -5.45114 23.98650 97.17945  1.000 14.87251  ? 182 ASN B CG  1 
ATOM   3030 O  OD1 . ASN B 1 183 ? -4.87118 24.47375 98.15421  1.000 18.34949  ? 182 ASN B OD1 1 
ATOM   3031 N  ND2 . ASN B 1 183 ? -6.49285 23.17835 97.30133  1.000 15.47156  ? 182 ASN B ND2 1 
ATOM   3032 N  N   . VAL B 1 184 ? -2.72892 23.92090 93.22313  1.000 13.11874  ? 183 VAL B N   1 
ATOM   3033 C  CA  . VAL B 1 184 ? -2.51972 24.29083 91.82908  1.000 14.52202  ? 183 VAL B CA  1 
ATOM   3034 C  C   . VAL B 1 184 ? -1.40425 23.49941 91.15719  1.000 14.25028  ? 183 VAL B C   1 
ATOM   3035 O  O   . VAL B 1 184 ? -0.98785 23.84873 90.05357  1.000 13.70857  ? 183 VAL B O   1 
ATOM   3036 C  CB  . VAL B 1 184 ? -2.33064 25.80796 91.63824  1.000 12.66674  ? 183 VAL B CB  1 
ATOM   3037 C  CG1 . VAL B 1 184 ? -3.61245 26.55186 91.99538  1.000 15.76558  ? 183 VAL B CG1 1 
ATOM   3038 C  CG2 . VAL B 1 184 ? -1.15296 26.30572 92.46495  1.000 13.59291  ? 183 VAL B CG2 1 
ATOM   3039 N  N   . ILE B 1 185 ? -0.91662 22.42725 91.78230  1.000 15.64899  ? 184 ILE B N   1 
ATOM   3040 C  CA  . ILE B 1 185 ? 0.12706  21.63493 91.13716  1.000 15.54427  ? 184 ILE B CA  1 
ATOM   3041 C  C   . ILE B 1 185 ? -0.42543 20.99936 89.87015  1.000 15.45269  ? 184 ILE B C   1 
ATOM   3042 O  O   . ILE B 1 185 ? -1.46752 20.32752 89.88947  1.000 15.94348  ? 184 ILE B O   1 
ATOM   3043 C  CB  . ILE B 1 185 ? 0.69075  20.57126 92.09261  1.000 16.21505  ? 184 ILE B CB  1 
ATOM   3044 C  CG1 . ILE B 1 185 ? 1.24077  21.22155 93.36006  1.000 22.04622  ? 184 ILE B CG1 1 
ATOM   3045 C  CG2 . ILE B 1 185 ? 1.77599  19.75758 91.39157  1.000 15.46965  ? 184 ILE B CG2 1 
ATOM   3046 C  CD1 . ILE B 1 185 ? 2.30664  22.23666 93.09326  1.000 18.82515  ? 184 ILE B CD1 1 
ATOM   3047 N  N   . ASN B 1 186 ? 0.26709  21.22123 88.75460  1.000 15.53322  ? 185 ASN B N   1 
ATOM   3048 C  CA  . ASN B 1 186 ? -0.11481 20.64638 87.46617  1.000 15.89298  ? 185 ASN B CA  1 
ATOM   3049 C  C   . ASN B 1 186 ? 0.51007  19.26348 87.36801  1.000 16.30975  ? 185 ASN B C   1 
ATOM   3050 O  O   . ASN B 1 186 ? 1.59013  19.07974 86.80453  1.000 16.58896  ? 185 ASN B O   1 
ATOM   3051 C  CB  . ASN B 1 186 ? 0.32371  21.54940 86.32248  1.000 14.30954  ? 185 ASN B CB  1 
ATOM   3052 C  CG  . ASN B 1 186 ? -0.14350 21.04769 84.97275  1.000 17.99556  ? 185 ASN B CG  1 
ATOM   3053 O  OD1 . ASN B 1 186 ? -0.83316 20.03114 84.87834  1.000 20.80967  ? 185 ASN B OD1 1 
ATOM   3054 N  ND2 . ASN B 1 186 ? 0.19865  21.77779 83.92246  1.000 17.70854  ? 185 ASN B ND2 1 
ATOM   3055 N  N   . TRP B 1 187 ? -0.19011 18.27100 87.92108  1.000 16.19982  ? 186 TRP B N   1 
ATOM   3056 C  CA  . TRP B 1 187 ? 0.32612  16.90869 87.89524  1.000 16.01469  ? 186 TRP B CA  1 
ATOM   3057 C  C   . TRP B 1 187 ? 0.42835  16.35020 86.48279  1.000 15.06160  ? 186 TRP B C   1 
ATOM   3058 O  O   . TRP B 1 187 ? 1.19302  15.40841 86.25874  1.000 17.70285  ? 186 TRP B O   1 
ATOM   3059 C  CB  . TRP B 1 187 ? -0.50567 15.99084 88.79091  1.000 18.09255  ? 186 TRP B CB  1 
ATOM   3060 C  CG  . TRP B 1 187 ? -0.34851 16.30844 90.23278  1.000 16.40585  ? 186 TRP B CG  1 
ATOM   3061 C  CD1 . TRP B 1 187 ? -1.30156 16.79801 91.07467  1.000 22.10017  ? 186 TRP B CD1 1 
ATOM   3062 C  CD2 . TRP B 1 187 ? 0.84913  16.18464 91.00805  1.000 18.82065  ? 186 TRP B CD2 1 
ATOM   3063 N  NE1 . TRP B 1 187 ? -0.77502 16.97432 92.33147  1.000 22.29131  ? 186 TRP B NE1 1 
ATOM   3064 C  CE2 . TRP B 1 187 ? 0.54512  16.61021 92.31626  1.000 20.11858  ? 186 TRP B CE2 1 
ATOM   3065 C  CE3 . TRP B 1 187 ? 2.14848  15.75596 90.72269  1.000 17.28381  ? 186 TRP B CE3 1 
ATOM   3066 C  CZ2 . TRP B 1 187 ? 1.49112  16.61364 93.33872  1.000 21.10683  ? 186 TRP B CZ2 1 
ATOM   3067 C  CZ3 . TRP B 1 187 ? 3.08767  15.75967 91.74236  1.000 20.22551  ? 186 TRP B CZ3 1 
ATOM   3068 C  CH2 . TRP B 1 187 ? 2.75193  16.18838 93.03309  1.000 21.09850  ? 186 TRP B CH2 1 
ATOM   3069 N  N   . GLU B 1 188 ? -0.33382 16.89024 85.52934  1.000 16.87443  ? 187 GLU B N   1 
ATOM   3070 C  CA  . GLU B 1 188 ? -0.15192 16.47763 84.14217  1.000 19.41711  ? 187 GLU B CA  1 
ATOM   3071 C  C   . GLU B 1 188 ? 1.25343  16.81062 83.65540  1.000 15.57969  ? 187 GLU B C   1 
ATOM   3072 O  O   . GLU B 1 188 ? 1.91629  15.98032 83.02103  1.000 16.59689  ? 187 GLU B O   1 
ATOM   3073 C  CB  . GLU B 1 188 ? -1.20680 17.14229 83.25746  1.000 22.63176  ? 187 GLU B CB  1 
ATOM   3074 C  CG  . GLU B 1 188 ? -1.09343 16.78258 81.78532  1.000 35.88794  ? 187 GLU B CG  1 
ATOM   3075 C  CD  . GLU B 1 188 ? -2.08003 17.54623 80.92464  1.000 55.03520  ? 187 GLU B CD  1 
ATOM   3076 O  OE1 . GLU B 1 188 ? -2.04661 18.79462 80.94874  1.000 56.38364  ? 187 GLU B OE1 1 
ATOM   3077 O  OE2 . GLU B 1 188 ? -2.88929 16.89966 80.22632  1.000 63.15041  ? 187 GLU B OE2 1 
ATOM   3078 N  N   . ASN B 1 189 ? 1.73918  18.01114 83.97867  1.000 15.47067  ? 188 ASN B N   1 
ATOM   3079 C  CA  . ASN B 1 189 ? 3.08242  18.40341 83.57102  1.000 13.73071  ? 188 ASN B CA  1 
ATOM   3080 C  C   . ASN B 1 189 ? 4.14821  17.60922 84.31799  1.000 14.72889  ? 188 ASN B C   1 
ATOM   3081 O  O   . ASN B 1 189 ? 5.12631  17.14949 83.71622  1.000 15.40613  ? 188 ASN B O   1 
ATOM   3082 C  CB  . ASN B 1 189 ? 3.28194  19.90054 83.79537  1.000 14.73394  ? 188 ASN B CB  1 
ATOM   3083 C  CG  . ASN B 1 189 ? 4.69605  20.33792 83.50654  1.000 17.44116  ? 188 ASN B CG  1 
ATOM   3084 O  OD1 . ASN B 1 189 ? 5.52651  20.42261 84.41089  1.000 16.50153  ? 188 ASN B OD1 1 
ATOM   3085 N  ND2 . ASN B 1 189 ? 4.98619  20.60482 82.23946  1.000 18.50930  ? 188 ASN B ND2 1 
ATOM   3086 N  N   . VAL B 1 190 ? 3.98143  17.44721 85.63203  1.000 15.48038  ? 189 VAL B N   1 
ATOM   3087 C  CA  . VAL B 1 190 ? 4.94712  16.67069 86.40353  1.000 16.55104  ? 189 VAL B CA  1 
ATOM   3088 C  C   . VAL B 1 190 ? 5.02719  15.24782 85.86560  1.000 14.42758  ? 189 VAL B C   1 
ATOM   3089 O  O   . VAL B 1 190 ? 6.11728  14.67242 85.74751  1.000 15.61115  ? 189 VAL B O   1 
ATOM   3090 C  CB  . VAL B 1 190 ? 4.60391  16.72006 87.90543  1.000 15.71157  ? 189 VAL B CB  1 
ATOM   3091 C  CG1 . VAL B 1 190 ? 5.65263  15.98961 88.71619  1.000 14.38287  ? 189 VAL B CG1 1 
ATOM   3092 C  CG2 . VAL B 1 190 ? 4.50101  18.16411 88.37741  1.000 13.96907  ? 189 VAL B CG2 1 
ATOM   3093 N  N   . THR B 1 191 ? 3.87705  14.67879 85.48364  1.000 14.76109  ? 190 THR B N   1 
ATOM   3094 C  CA  . THR B 1 191 ? 3.85974  13.34194 84.89868  1.000 18.35779  ? 190 THR B CA  1 
ATOM   3095 C  C   . THR B 1 191 ? 4.61315  13.29767 83.57494  1.000 16.02092  ? 190 THR B C   1 
ATOM   3096 O  O   . THR B 1 191 ? 5.39730  12.37298 83.33327  1.000 17.86112  ? 190 THR B O   1 
ATOM   3097 C  CB  . THR B 1 191 ? 2.41644  12.88069 84.71717  1.000 16.13013  ? 190 THR B CB  1 
ATOM   3098 O  OG1 . THR B 1 191 ? 1.83428  12.63605 86.00456  1.000 21.28649  ? 190 THR B OG1 1 
ATOM   3099 C  CG2 . THR B 1 191 ? 2.36107  11.61247 83.87284  1.000 18.14954  ? 190 THR B CG2 1 
ATOM   3100 N  N   . GLU B 1 192 ? 4.39376  14.28727 82.70430  1.000 16.13012  ? 191 GLU B N   1 
ATOM   3101 C  CA  . GLU B 1 192 ? 5.12575  14.33116 81.44192  1.000 17.83917  ? 191 GLU B CA  1 
ATOM   3102 C  C   . GLU B 1 192 ? 6.62891  14.37091 81.68444  1.000 20.31618  ? 191 GLU B C   1 
ATOM   3103 O  O   . GLU B 1 192 ? 7.39678  13.64288 81.04122  1.000 20.43828  ? 191 GLU B O   1 
ATOM   3104 C  CB  . GLU B 1 192 ? 4.68785  15.54462 80.62158  1.000 18.29072  ? 191 GLU B CB  1 
ATOM   3105 C  CG  . GLU B 1 192 ? 3.29661  15.42888 80.02962  1.000 23.69280  ? 191 GLU B CG  1 
ATOM   3106 C  CD  . GLU B 1 192 ? 2.88739  16.67396 79.26552  1.000 30.83755  ? 191 GLU B CD  1 
ATOM   3107 O  OE1 . GLU B 1 192 ? 3.71072  17.60881 79.16316  1.000 31.91254  ? 191 GLU B OE1 1 
ATOM   3108 O  OE2 . GLU B 1 192 ? 1.74223  16.71766 78.77039  1.000 38.65808  ? 191 GLU B OE2 1 
ATOM   3109 N  N   . ARG B 1 193 ? 7.06777  15.21578 82.62045  1.000 17.67727  ? 192 ARG B N   1 
ATOM   3110 C  CA  . ARG B 1 193 ? 8.49224  15.29616 82.93041  1.000 17.07392  ? 192 ARG B CA  1 
ATOM   3111 C  C   . ARG B 1 193 ? 9.00410  13.97922 83.49897  1.000 17.47516  ? 192 ARG B C   1 
ATOM   3112 O  O   . ARG B 1 193 ? 10.12380 13.55320 83.19190  1.000 19.35805  ? 192 ARG B O   1 
ATOM   3113 C  CB  . ARG B 1 193 ? 8.75413  16.43790 83.91393  1.000 15.86678  ? 192 ARG B CB  1 
ATOM   3114 C  CG  . ARG B 1 193 ? 8.43075  17.81478 83.36415  1.000 15.48435  ? 192 ARG B CG  1 
ATOM   3115 C  CD  . ARG B 1 193 ? 8.70649  18.91921 84.38047  1.000 15.21407  ? 192 ARG B CD  1 
ATOM   3116 N  NE  . ARG B 1 193 ? 8.40991  20.22413 83.81011  1.000 16.54061  ? 192 ARG B NE  1 
ATOM   3117 C  CZ  . ARG B 1 193 ? 9.24830  20.90733 83.04474  1.000 12.84126  ? 192 ARG B CZ  1 
ATOM   3118 N  NH1 . ARG B 1 193 ? 10.45843 20.45083 82.76347  1.000 15.49074  ? 192 ARG B NH1 1 
ATOM   3119 N  NH2 . ARG B 1 193 ? 8.86647  22.08124 82.55072  1.000 17.40173  ? 192 ARG B NH2 1 
ATOM   3120 N  N   . TYR B 1 194 ? 8.19135  13.31874 84.32532  1.000 17.58635  ? 193 TYR B N   1 
ATOM   3121 C  CA  . TYR B 1 194 ? 8.58940  12.03858 84.89708  1.000 16.95588  ? 193 TYR B CA  1 
ATOM   3122 C  C   . TYR B 1 194 ? 8.70187  10.97239 83.81608  1.000 19.70619  ? 193 TYR B C   1 
ATOM   3123 O  O   . TYR B 1 194 ? 9.70146  10.24847 83.74505  1.000 21.31507  ? 193 TYR B O   1 
ATOM   3124 C  CB  . TYR B 1 194 ? 7.58427  11.62012 85.97025  1.000 17.32390  ? 193 TYR B CB  1 
ATOM   3125 C  CG  . TYR B 1 194 ? 7.79866  10.21207 86.46711  1.000 17.75891  ? 193 TYR B CG  1 
ATOM   3126 C  CD1 . TYR B 1 194 ? 8.82670  9.91954  87.34817  1.000 18.49614  ? 193 TYR B CD1 1 
ATOM   3127 C  CD2 . TYR B 1 194 ? 6.97647  9.17413  86.04896  1.000 19.84631  ? 193 TYR B CD2 1 
ATOM   3128 C  CE1 . TYR B 1 194 ? 9.03461  8.63297  87.80329  1.000 19.22025  ? 193 TYR B CE1 1 
ATOM   3129 C  CE2 . TYR B 1 194 ? 7.17615  7.88388  86.49843  1.000 21.25440  ? 193 TYR B CE2 1 
ATOM   3130 C  CZ  . TYR B 1 194 ? 8.20739  7.62004  87.37503  1.000 20.11824  ? 193 TYR B CZ  1 
ATOM   3131 O  OH  . TYR B 1 194 ? 8.41720  6.33835  87.82797  1.000 21.66534  ? 193 TYR B OH  1 
ATOM   3132 N  N   . MET B 1 195 ? 7.68836  10.87103 82.95466  1.000 21.78650  ? 194 MET B N   1 
ATOM   3133 C  CA  . MET B 1 195 ? 7.70852  9.85556  81.90767  1.000 22.99705  ? 194 MET B CA  1 
ATOM   3134 C  C   . MET B 1 195 ? 8.83216  10.09337 80.90610  1.000 22.58169  ? 194 MET B C   1 
ATOM   3135 O  O   . MET B 1 195 ? 9.37440  9.13308  80.34685  1.000 25.36021  ? 194 MET B O   1 
ATOM   3136 C  CB  . MET B 1 195 ? 6.34809  9.79604  81.21490  1.000 17.88672  ? 194 MET B CB  1 
ATOM   3137 C  CG  . MET B 1 195 ? 5.20818  9.38016  82.13728  1.000 25.11792  ? 194 MET B CG  1 
ATOM   3138 S  SD  . MET B 1 195 ? 5.41258  7.72605  82.84464  1.000 25.04350  ? 194 MET B SD  1 
ATOM   3139 C  CE  . MET B 1 195 ? 5.18286  6.70441  81.38964  1.000 32.30341  ? 194 MET B CE  1 
ATOM   3140 N  N   . ALA B 1 196 ? 9.21565  11.35322 80.68854  1.000 21.16851  ? 195 ALA B N   1 
ATOM   3141 C  CA  . ALA B 1 196 ? 10.33708 11.65018 79.80568  1.000 29.52783  ? 195 ALA B CA  1 
ATOM   3142 C  C   . ALA B 1 196 ? 11.66066 11.14264 80.36323  1.000 34.57880  ? 195 ALA B C   1 
ATOM   3143 O  O   . ALA B 1 196 ? 12.59270 10.90260 79.58811  1.000 31.76585  ? 195 ALA B O   1 
ATOM   3144 C  CB  . ALA B 1 196 ? 10.41738 13.15320 79.53373  1.000 27.16128  ? 195 ALA B CB  1 
ATOM   3145 N  N   . CYS B 1 197 ? 11.75915 10.96452 81.68373  1.000 28.68909  ? 196 CYS B N   1 
ATOM   3146 C  CA  . CYS B 1 197 ? 12.97540 10.40973 82.27051  1.000 32.28869  ? 196 CYS B CA  1 
ATOM   3147 C  C   . CYS B 1 197 ? 13.10087 8.92548  81.96818  1.000 36.21217  ? 196 CYS B C   1 
ATOM   3148 O  O   . CYS B 1 197 ? 14.19721 8.43468  81.67611  1.000 47.30391  ? 196 CYS B O   1 
ATOM   3149 C  CB  . CYS B 1 197 ? 12.96484 10.61150 83.78233  1.000 27.41969  ? 196 CYS B CB  1 
ATOM   3150 S  SG  . CYS B 1 197 ? 13.07303 12.31691 84.30794  1.000 24.73956  ? 196 CYS B SG  1 
ATOM   3151 N  N   . LYS B 1 198 ? 11.99511 8.19400  82.05254  1.000 41.54351  ? 197 LYS B N   1 
ATOM   3152 C  CA  . LYS B 1 198 ? 11.97924 6.76815  81.76290  1.000 45.34709  ? 197 LYS B CA  1 
ATOM   3153 C  C   . LYS B 1 198 ? 11.86293 6.46781  80.27065  1.000 53.68665  ? 197 LYS B C   1 
ATOM   3154 O  O   . LYS B 1 198 ? 11.70119 5.30150  79.89515  1.000 70.25983  ? 197 LYS B O   1 
ATOM   3155 C  CB  . LYS B 1 198 ? 10.86317 6.09026  82.56332  1.000 45.33906  ? 197 LYS B CB  1 
ATOM   3156 C  CG  . LYS B 1 198 ? 10.87011 6.49036  84.03675  1.000 37.35956  ? 197 LYS B CG  1 
ATOM   3157 C  CD  . LYS B 1 198 ? 10.15049 5.48167  84.91565  1.000 36.07477  ? 197 LYS B CD  1 
ATOM   3158 C  CE  . LYS B 1 198 ? 8.68640  5.35268  84.54362  1.000 42.83036  ? 197 LYS B CE  1 
ATOM   3159 N  NZ  . LYS B 1 198 ? 7.96731  4.40271  85.44683  1.000 36.45104  ? 197 LYS B NZ  1 
ATOM   3160 N  N   . LYS B 1 199 ? 11.94609 7.48970  79.42301  1.000 55.00113  ? 198 LYS B N   1 
ATOM   3161 C  CA  . LYS B 1 199 ? 11.82909 7.32809  77.97778  1.000 62.92493  ? 198 LYS B CA  1 
ATOM   3162 C  C   . LYS B 1 199 ? 13.10978 7.77975  77.28571  1.000 72.62941  ? 198 LYS B C   1 
ATOM   3163 O  O   . LYS B 1 199 ? 13.74118 7.01196  76.55946  1.000 79.91013  ? 198 LYS B O   1 
ATOM   3164 C  CB  . LYS B 1 199 ? 10.63659 8.12234  77.43795  1.000 51.32160  ? 198 LYS B CB  1 
ATOM   3165 C  CG  . LYS B 1 199 ? 10.07998 7.59732  76.12086  1.000 67.08008  ? 198 LYS B CG  1 
ATOM   3166 C  CD  . LYS B 1 199 ? 9.38617  6.25362  76.28157  1.000 74.64051  ? 198 LYS B CD  1 
ATOM   3167 C  CE  . LYS B 1 199 ? 8.73634  5.81893  74.97441  1.000 73.79766  ? 198 LYS B CE  1 
ATOM   3168 N  NZ  . LYS B 1 199 ? 7.96068  4.55602  75.11816  1.000 60.25480  ? 198 LYS B NZ  1 
ATOM   3169 O  OXT . LYS B 1 199 ? 13.54613 8.92091  77.44207  1.000 73.90469  ? 198 LYS B OXT 1 
HETATM 3170 MN MN  . MN  C 2 .   ? 49.66382 23.95783 93.27292  1.000 13.83143  ? 201 MN  A MN  1 
HETATM 3171 O  O1  A PEO D 3 .   ? 47.87423 24.71473 94.46287  0.350 15.98993  ? 202 PEO A O1  1 
HETATM 3172 O  O2  A PEO D 3 .   ? 47.72213 24.30655 93.11296  0.350 17.64715  ? 202 PEO A O2  1 
HETATM 3173 P  P   . PO4 E 4 .   ? 47.26606 31.43416 78.11617  1.000 18.88840  ? 203 PO4 A P   1 
HETATM 3174 O  O1  . PO4 E 4 .   ? 47.97532 30.15506 78.49067  1.000 21.01183  ? 203 PO4 A O1  1 
HETATM 3175 O  O2  . PO4 E 4 .   ? 46.98680 31.46102 76.63265  1.000 22.78922  ? 203 PO4 A O2  1 
HETATM 3176 O  O3  . PO4 E 4 .   ? 45.96362 31.49946 78.87175  1.000 24.70567  ? 203 PO4 A O3  1 
HETATM 3177 O  O4  . PO4 E 4 .   ? 48.12511 32.61882 78.48647  1.000 22.63723  ? 203 PO4 A O4  1 
HETATM 3178 P  P   . PO4 F 4 .   ? 52.26001 48.88084 117.19135 1.000 88.06046  ? 204 PO4 A P   1 
HETATM 3179 O  O1  . PO4 F 4 .   ? 52.27140 47.44662 116.71889 1.000 74.41267  ? 204 PO4 A O1  1 
HETATM 3180 O  O2  . PO4 F 4 .   ? 51.65597 48.94777 118.57438 1.000 83.56448  ? 204 PO4 A O2  1 
HETATM 3181 O  O3  . PO4 F 4 .   ? 53.67434 49.40937 117.23296 1.000 60.35006  ? 204 PO4 A O3  1 
HETATM 3182 O  O4  . PO4 F 4 .   ? 51.43716 49.71512 116.23834 1.000 71.74435  ? 204 PO4 A O4  1 
HETATM 3183 K  K   . K   G 5 .   ? 70.64632 23.07602 92.45610  1.000 17.65757  ? 205 K   A K   1 
HETATM 3184 MN MN  . MN  H 2 .   ? 11.05736 33.41482 91.89816  1.000 14.58756  ? 201 MN  B MN  1 
HETATM 3185 P  P   . PO4 I 4 .   ? 15.20383 29.78272 75.68965  1.000 34.02156  ? 202 PO4 B P   1 
HETATM 3186 O  O1  . PO4 I 4 .   ? 16.14211 29.44463 74.55376  1.000 54.83650  ? 202 PO4 B O1  1 
HETATM 3187 O  O2  . PO4 I 4 .   ? 14.49789 31.09314 75.39136  1.000 21.02814  ? 202 PO4 B O2  1 
HETATM 3188 O  O3  . PO4 I 4 .   ? 14.19898 28.66673 75.84259  1.000 43.04594  ? 202 PO4 B O3  1 
HETATM 3189 O  O4  . PO4 I 4 .   ? 16.00704 29.88049 76.96278  1.000 20.30096  ? 202 PO4 B O4  1 
HETATM 3190 O  O   . HOH J 6 .   ? 71.042   38.496   90.699    1.000 25.41095  ? 301 HOH A O   1 
HETATM 3191 O  O   . HOH J 6 .   ? 53.085   45.389   117.538   1.000 28.67763  ? 302 HOH A O   1 
HETATM 3192 O  O   . HOH J 6 .   ? 24.32823 20.37149 75.97765  1.000 33.91540  ? 303 HOH A O   1 
HETATM 3193 O  O   . HOH J 6 .   ? 29.20318 28.83781 89.96483  1.000 34.08973  ? 304 HOH A O   1 
HETATM 3194 O  O   . HOH J 6 .   ? 51.66176 41.39140 111.64576 1.000 32.40113  ? 305 HOH A O   1 
HETATM 3195 O  O   . HOH J 6 .   ? 30.18004 19.35194 74.45201  1.000 31.54845  ? 306 HOH A O   1 
HETATM 3196 O  O   . HOH J 6 .   ? 63.02897 17.09498 89.57116  1.000 23.61073  ? 307 HOH A O   1 
HETATM 3197 O  O   . HOH J 6 .   ? 46.83558 22.30927 76.72244  1.000 21.83158  ? 308 HOH A O   1 
HETATM 3198 O  O   . HOH J 6 .   ? 32.40909 27.35730 94.05530  1.000 31.62421  ? 309 HOH A O   1 
HETATM 3199 O  O   . HOH J 6 .   ? 41.70341 19.07795 86.83353  1.000 19.82613  ? 310 HOH A O   1 
HETATM 3200 O  O   . HOH J 6 .   ? 64.55833 46.57711 102.90832 1.000 32.70734  ? 311 HOH A O   1 
HETATM 3201 O  O   . HOH J 6 .   ? 61.88665 44.78448 86.70337  1.000 31.81839  ? 312 HOH A O   1 
HETATM 3202 O  O   . HOH J 6 .   ? 40.136   22.396   69.695    1.000 31.69200  ? 313 HOH A O   1 
HETATM 3203 O  O   . HOH J 6 .   ? 39.47592 44.15322 89.29772  1.000 29.01132  ? 314 HOH A O   1 
HETATM 3204 O  O   . HOH J 6 .   ? 66.38738 31.01377 83.72149  1.000 30.57549  ? 315 HOH A O   1 
HETATM 3205 O  O   . HOH J 6 .   ? 41.883   16.812   79.598    1.000 27.29207  ? 316 HOH A O   1 
HETATM 3206 O  O   . HOH J 6 .   ? 47.88498 48.04746 108.77189 1.000 32.03249  ? 317 HOH A O   1 
HETATM 3207 O  O   . HOH J 6 .   ? 64.67778 46.85679 100.52451 1.000 31.28847  ? 318 HOH A O   1 
HETATM 3208 O  O   . HOH J 6 .   ? 55.81881 24.21988 78.78139  1.000 28.66410  ? 319 HOH A O   1 
HETATM 3209 O  O   . HOH J 6 .   ? 48.80432 32.87004 81.01783  1.000 23.20661  ? 320 HOH A O   1 
HETATM 3210 O  O   . HOH J 6 .   ? 40.86508 26.80577 74.78041  1.000 23.28912  ? 321 HOH A O   1 
HETATM 3211 O  O   . HOH J 6 .   ? 68.63337 34.92917 95.75622  1.000 29.10476  ? 322 HOH A O   1 
HETATM 3212 O  O   . HOH J 6 .   ? 61.88366 32.99421 106.45702 1.000 28.92134  ? 323 HOH A O   1 
HETATM 3213 O  O   . HOH J 6 .   ? 61.41947 45.81335 94.72305  1.000 29.22749  ? 324 HOH A O   1 
HETATM 3214 O  O   . HOH J 6 .   ? 55.88188 41.35423 85.06205  1.000 26.65421  ? 325 HOH A O   1 
HETATM 3215 O  O   . HOH J 6 .   ? 58.90608 49.03088 94.20736  1.000 32.98706  ? 326 HOH A O   1 
HETATM 3216 O  O   . HOH J 6 .   ? 35.97463 32.02060 96.26821  1.000 21.15249  ? 327 HOH A O   1 
HETATM 3217 O  O   . HOH J 6 .   ? 49.42107 40.89051 88.40790  1.000 18.28673  ? 328 HOH A O   1 
HETATM 3218 O  O   . HOH J 6 .   ? 46.11906 51.20951 103.99732 1.000 19.64124  ? 329 HOH A O   1 
HETATM 3219 O  O   . HOH J 6 .   ? 58.03833 30.56201 80.68682  1.000 31.29548  ? 330 HOH A O   1 
HETATM 3220 O  O   . HOH J 6 .   ? 40.00448 25.52958 101.39064 1.000 15.37051  ? 331 HOH A O   1 
HETATM 3221 O  O   . HOH J 6 .   ? 61.00614 24.02473 76.70653  1.000 30.21305  ? 332 HOH A O   1 
HETATM 3222 O  O   . HOH J 6 .   ? 62.63156 26.30150 78.31301  1.000 21.96872  ? 333 HOH A O   1 
HETATM 3223 O  O   . HOH J 6 .   ? 39.99796 22.06808 99.79208  0.50  13.92602  ? 334 HOH A O   1 
HETATM 3224 O  O   . HOH J 6 .   ? 49.802   34.298   77.241    1.000 27.84462  ? 335 HOH A O   1 
HETATM 3225 O  O   . HOH J 6 .   ? 49.91895 44.65317 109.85686 1.000 28.81849  ? 336 HOH A O   1 
HETATM 3226 O  O   . HOH J 6 .   ? 36.15622 42.06449 96.66798  1.000 27.80858  ? 337 HOH A O   1 
HETATM 3227 O  O   . HOH J 6 .   ? 49.84043 51.51162 96.67753  1.000 22.44513  ? 338 HOH A O   1 
HETATM 3228 O  O   . HOH J 6 .   ? 64.27069 23.67667 93.52540  1.000 14.37637  ? 339 HOH A O   1 
HETATM 3229 O  O   . HOH J 6 .   ? 43.99776 31.43966 94.42106  1.000 13.64422  ? 340 HOH A O   1 
HETATM 3230 O  O   . HOH J 6 .   ? 46.10963 31.82171 110.60540 1.000 26.60751  ? 341 HOH A O   1 
HETATM 3231 O  O   . HOH J 6 .   ? 55.31812 47.04117 85.67191  1.000 23.57526  ? 342 HOH A O   1 
HETATM 3232 O  O   . HOH J 6 .   ? 57.19272 25.76642 112.03318 1.000 27.90680  ? 343 HOH A O   1 
HETATM 3233 O  O   . HOH J 6 .   ? 48.604   50.751   107.948   1.000 34.62263  ? 344 HOH A O   1 
HETATM 3234 O  O   . HOH J 6 .   ? 67.60699 33.34905 98.66661  1.000 26.33598  ? 345 HOH A O   1 
HETATM 3235 O  O   . HOH J 6 .   ? 44.52394 53.26349 102.47381 1.000 24.20003  ? 346 HOH A O   1 
HETATM 3236 O  O   . HOH J 6 .   ? 61.19709 37.59963 101.34534 1.000 23.16880  ? 347 HOH A O   1 
HETATM 3237 O  O   . HOH J 6 .   ? 55.76537 54.05728 103.47436 1.000 25.47695  ? 348 HOH A O   1 
HETATM 3238 O  O   . HOH J 6 .   ? 45.04786 34.31030 91.20612  1.000 13.50930  ? 349 HOH A O   1 
HETATM 3239 O  O   . HOH J 6 .   ? 19.73774 23.06998 85.39705  1.000 14.85217  ? 350 HOH A O   1 
HETATM 3240 O  O   . HOH J 6 .   ? 56.27471 24.57142 93.92946  1.000 14.43692  ? 351 HOH A O   1 
HETATM 3241 O  O   . HOH J 6 .   ? 38.68033 32.46056 101.30289 1.000 29.15825  ? 352 HOH A O   1 
HETATM 3242 O  O   . HOH J 6 .   ? 61.61979 54.74563 99.79208  0.50  32.38925  ? 353 HOH A O   1 
HETATM 3243 O  O   . HOH J 6 .   ? 45.82303 19.97944 99.07292  1.000 14.04711  ? 354 HOH A O   1 
HETATM 3244 O  O   . HOH J 6 .   ? 32.19567 21.06775 86.05822  1.000 16.79034  ? 355 HOH A O   1 
HETATM 3245 O  O   . HOH J 6 .   ? 38.05017 33.76472 96.48053  1.000 24.01813  ? 356 HOH A O   1 
HETATM 3246 O  O   . HOH J 6 .   ? 49.59765 15.95359 84.31756  1.000 16.59478  ? 357 HOH A O   1 
HETATM 3247 O  O   . HOH J 6 .   ? 69.49776 23.15415 89.90698  1.000 20.17826  ? 358 HOH A O   1 
HETATM 3248 O  O   . HOH J 6 .   ? 35.82054 19.34674 75.20462  1.000 19.73725  ? 359 HOH A O   1 
HETATM 3249 O  O   . HOH J 6 .   ? 28.86707 19.57912 87.37551  1.000 28.14260  ? 360 HOH A O   1 
HETATM 3250 O  O   . HOH J 6 .   ? 48.67886 30.05314 74.85930  1.000 19.19368  ? 361 HOH A O   1 
HETATM 3251 O  O   . HOH J 6 .   ? 67.38227 17.63585 93.42725  1.000 32.31231  ? 362 HOH A O   1 
HETATM 3252 O  O   . HOH J 6 .   ? 54.61854 26.73934 76.29108  1.000 26.69236  ? 363 HOH A O   1 
HETATM 3253 O  O   . HOH J 6 .   ? 47.45052 53.52657 101.80121 1.000 26.83063  ? 364 HOH A O   1 
HETATM 3254 O  O   . HOH J 6 .   ? 50.74367 30.27304 78.64591  1.000 9.13093   ? 365 HOH A O   1 
HETATM 3255 O  O   . HOH J 6 .   ? 60.63058 15.56219 106.55467 1.000 34.62572  ? 366 HOH A O   1 
HETATM 3256 O  O   . HOH J 6 .   ? 28.94736 21.25368 76.02102  1.000 22.77926  ? 367 HOH A O   1 
HETATM 3257 O  O   . HOH J 6 .   ? 45.67519 21.66349 92.60384  1.000 31.31871  ? 368 HOH A O   1 
HETATM 3258 O  O   . HOH J 6 .   ? 56.17092 15.87504 110.63457 1.000 22.41725  ? 369 HOH A O   1 
HETATM 3259 O  O   . HOH J 6 .   ? 38.42413 44.13535 94.72440  1.000 33.81379  ? 370 HOH A O   1 
HETATM 3260 O  O   . HOH J 6 .   ? 40.52214 45.69628 92.86908  1.000 22.45719  ? 371 HOH A O   1 
HETATM 3261 O  O   . HOH J 6 .   ? 49.40672 51.78105 99.32446  1.000 21.72711  ? 372 HOH A O   1 
HETATM 3262 O  O   . HOH J 6 .   ? 46.37603 22.04274 101.88177 1.000 16.39454  ? 373 HOH A O   1 
HETATM 3263 O  O   . HOH J 6 .   ? 55.67534 25.07787 96.50072  1.000 14.47470  ? 374 HOH A O   1 
HETATM 3264 O  O   . HOH J 6 .   ? 58.60712 19.84273 108.19672 1.000 26.09147  ? 375 HOH A O   1 
HETATM 3265 O  O   . HOH J 6 .   ? 27.07700 24.08974 69.93543  1.000 33.18140  ? 376 HOH A O   1 
HETATM 3266 O  O   . HOH J 6 .   ? 35.58901 19.09472 70.20976  1.000 27.79510  ? 377 HOH A O   1 
HETATM 3267 O  O   . HOH J 6 .   ? 46.44300 19.44220 91.27872  1.000 22.50006  ? 378 HOH A O   1 
HETATM 3268 O  O   . HOH J 6 .   ? 54.35526 53.46567 97.34706  1.000 33.94900  ? 379 HOH A O   1 
HETATM 3269 O  O   . HOH J 6 .   ? 61.75789 26.09200 107.12308 1.000 19.19255  ? 380 HOH A O   1 
HETATM 3270 O  O   . HOH J 6 .   ? 39.04076 42.56062 87.14247  1.000 27.33089  ? 381 HOH A O   1 
HETATM 3271 O  O   . HOH J 6 .   ? 49.31456 19.42870 105.53141 1.000 18.38422  ? 382 HOH A O   1 
HETATM 3272 O  O   . HOH J 6 .   ? 58.99620 21.18686 112.40933 1.000 32.24160  ? 383 HOH A O   1 
HETATM 3273 O  O   . HOH J 6 .   ? 60.73097 45.18701 89.21410  1.000 22.37732  ? 384 HOH A O   1 
HETATM 3274 O  O   . HOH J 6 .   ? 44.250   15.463   81.720    1.000 27.80020  ? 385 HOH A O   1 
HETATM 3275 O  O   . HOH J 6 .   ? 40.66391 40.75499 101.96163 1.000 17.78397  ? 386 HOH A O   1 
HETATM 3276 O  O   . HOH J 6 .   ? 19.27470 22.25681 78.85016  1.000 29.77416  ? 387 HOH A O   1 
HETATM 3277 O  O   B HOH J 6 .   ? 47.72710 24.32262 93.95832  0.650 11.55836  ? 388 HOH A O   1 
HETATM 3278 O  O   . HOH J 6 .   ? 40.65929 47.34576 101.36092 1.000 17.42263  ? 389 HOH A O   1 
HETATM 3279 O  O   . HOH J 6 .   ? 66.36454 17.32808 96.71449  1.000 25.72001  ? 390 HOH A O   1 
HETATM 3280 O  O   . HOH J 6 .   ? 44.72576 32.14470 81.30551  1.000 20.70337  ? 391 HOH A O   1 
HETATM 3281 O  O   . HOH J 6 .   ? 54.20650 31.24175 84.20478  1.000 18.19210  ? 392 HOH A O   1 
HETATM 3282 O  O   . HOH J 6 .   ? 43.10444 32.02391 105.83152 1.000 17.96709  ? 393 HOH A O   1 
HETATM 3283 O  O   . HOH J 6 .   ? 36.18951 26.36571 95.22897  1.000 18.16455  ? 394 HOH A O   1 
HETATM 3284 O  O   . HOH J 6 .   ? 46.13536 37.65688 107.89533 1.000 20.63499  ? 395 HOH A O   1 
HETATM 3285 O  O   . HOH J 6 .   ? 64.92580 26.79003 103.89595 1.000 20.95773  ? 396 HOH A O   1 
HETATM 3286 O  O   . HOH J 6 .   ? 44.86760 24.46144 107.95259 1.000 26.01405  ? 397 HOH A O   1 
HETATM 3287 O  O   . HOH J 6 .   ? 41.10608 55.34663 95.88644  1.000 35.62188  ? 398 HOH A O   1 
HETATM 3288 O  O   . HOH J 6 .   ? 60.83843 33.98682 88.06434  1.000 22.69279  ? 399 HOH A O   1 
HETATM 3289 O  O   . HOH J 6 .   ? 54.83082 17.87179 94.84405  1.000 16.73885  ? 400 HOH A O   1 
HETATM 3290 O  O   . HOH J 6 .   ? 49.69409 20.53861 79.78476  1.000 32.85818  ? 401 HOH A O   1 
HETATM 3291 O  O   . HOH J 6 .   ? 59.82772 47.24252 107.23525 1.000 20.71009  ? 402 HOH A O   1 
HETATM 3292 O  O   . HOH J 6 .   ? 50.70562 30.94513 81.38347  1.000 18.57899  ? 403 HOH A O   1 
HETATM 3293 O  O   . HOH J 6 .   ? 63.77369 20.90011 103.92113 1.000 26.50734  ? 404 HOH A O   1 
HETATM 3294 O  O   . HOH J 6 .   ? 40.02495 28.20567 105.01809 1.000 17.46179  ? 405 HOH A O   1 
HETATM 3295 O  O   . HOH J 6 .   ? 47.789   33.939   75.521    1.000 31.94814  ? 406 HOH A O   1 
HETATM 3296 O  O   . HOH J 6 .   ? 67.61129 28.44428 95.89444  1.000 19.25425  ? 407 HOH A O   1 
HETATM 3297 O  O   . HOH J 6 .   ? 52.65743 34.95699 85.08928  1.000 21.39966  ? 408 HOH A O   1 
HETATM 3298 O  O   . HOH J 6 .   ? 64.47750 38.23891 89.86630  1.000 28.21694  ? 409 HOH A O   1 
HETATM 3299 O  O   . HOH J 6 .   ? 38.76514 26.03127 92.53229  1.000 14.55531  ? 410 HOH A O   1 
HETATM 3300 O  O   . HOH J 6 .   ? 47.61218 54.03131 99.08825  1.000 26.97147  ? 411 HOH A O   1 
HETATM 3301 O  O   . HOH J 6 .   ? 34.18801 29.14293 96.42430  1.000 35.42036  ? 412 HOH A O   1 
HETATM 3302 O  O   . HOH J 6 .   ? 47.95084 25.10276 108.14633 1.000 31.15430  ? 413 HOH A O   1 
HETATM 3303 O  O   . HOH J 6 .   ? 68.84450 31.24601 100.10230 1.000 25.89364  ? 414 HOH A O   1 
HETATM 3304 O  O   . HOH J 6 .   ? 38.63569 35.53122 98.93164  1.000 26.30862  ? 415 HOH A O   1 
HETATM 3305 O  O   . HOH J 6 .   ? 69.92394 18.12940 95.47989  1.000 33.63508  ? 416 HOH A O   1 
HETATM 3306 O  O   . HOH J 6 .   ? 35.34174 25.07161 91.17776  1.000 26.35190  ? 417 HOH A O   1 
HETATM 3307 O  O   . HOH J 6 .   ? 54.17070 18.26396 81.38940  1.000 20.85035  ? 418 HOH A O   1 
HETATM 3308 O  O   . HOH J 6 .   ? 35.12702 19.76541 81.71130  1.000 29.43419  ? 419 HOH A O   1 
HETATM 3309 O  O   . HOH J 6 .   ? 62.03665 37.42389 104.45783 1.000 28.70836  ? 420 HOH A O   1 
HETATM 3310 O  O   . HOH J 6 .   ? 41.33759 53.98668 100.04629 1.000 18.08476  ? 421 HOH A O   1 
HETATM 3311 O  O   . HOH J 6 .   ? 62.12293 47.29406 105.92163 1.000 29.72190  ? 422 HOH A O   1 
HETATM 3312 O  O   . HOH J 6 .   ? 37.69490 25.44139 104.72084 1.000 21.01743  ? 423 HOH A O   1 
HETATM 3313 O  O   . HOH J 6 .   ? 41.61607 35.62150 88.17175  1.000 13.44181  ? 424 HOH A O   1 
HETATM 3314 O  O   . HOH J 6 .   ? 61.68788 38.52309 87.41523  1.000 24.18997  ? 425 HOH A O   1 
HETATM 3315 O  O   . HOH J 6 .   ? 60.02090 24.09400 82.42270  1.000 29.21148  ? 426 HOH A O   1 
HETATM 3316 O  O   . HOH J 6 .   ? 49.86471 37.69153 84.95467  1.000 27.25070  ? 427 HOH A O   1 
HETATM 3317 O  O   . HOH J 6 .   ? 56.78245 30.63082 84.02743  1.000 21.41272  ? 428 HOH A O   1 
HETATM 3318 O  O   . HOH J 6 .   ? 49.78743 43.54779 87.61353  1.000 19.79187  ? 429 HOH A O   1 
HETATM 3319 O  O   . HOH J 6 .   ? 63.62920 34.23548 87.78340  1.000 30.82691  ? 430 HOH A O   1 
HETATM 3320 O  O   . HOH J 6 .   ? 48.88912 19.76182 108.15378 1.000 22.88047  ? 431 HOH A O   1 
HETATM 3321 O  O   . HOH J 6 .   ? 54.57777 52.20084 108.87083 1.000 26.04487  ? 432 HOH A O   1 
HETATM 3322 O  O   . HOH J 6 .   ? 66.71511 42.72171 101.03389 1.000 34.23704  ? 433 HOH A O   1 
HETATM 3323 O  O   . HOH J 6 .   ? 55.72227 30.13137 108.97798 1.000 21.11565  ? 434 HOH A O   1 
HETATM 3324 O  O   . HOH J 6 .   ? 67.98481 27.84347 86.84807  1.000 18.97409  ? 435 HOH A O   1 
HETATM 3325 O  O   . HOH J 6 .   ? 38.18624 18.83981 85.06621  1.000 28.77702  ? 436 HOH A O   1 
HETATM 3326 O  O   . HOH J 6 .   ? 37.19935 40.53942 88.27504  1.000 29.80145  ? 437 HOH A O   1 
HETATM 3327 O  O   . HOH J 6 .   ? 48.45437 53.61698 95.37574  1.000 30.64025  ? 438 HOH A O   1 
HETATM 3328 O  O   . HOH J 6 .   ? 59.52860 22.52833 79.04886  1.000 27.41068  ? 439 HOH A O   1 
HETATM 3329 O  O   . HOH J 6 .   ? 61.17519 14.98291 98.57083  1.000 27.74100  ? 440 HOH A O   1 
HETATM 3330 O  O   . HOH J 6 .   ? 62.52082 16.52795 103.61785 1.000 30.51909  ? 441 HOH A O   1 
HETATM 3331 O  O   . HOH J 6 .   ? 59.97843 52.46608 93.08602  1.000 34.50284  ? 442 HOH A O   1 
HETATM 3332 O  O   . HOH J 6 .   ? 65.43894 35.92116 102.45795 1.000 29.37288  ? 443 HOH A O   1 
HETATM 3333 O  O   . HOH J 6 .   ? 63.25791 25.21386 83.14752  1.000 28.78073  ? 444 HOH A O   1 
HETATM 3334 O  O   . HOH J 6 .   ? 64.48939 30.32696 106.39793 1.000 27.47700  ? 445 HOH A O   1 
HETATM 3335 O  O   . HOH J 6 .   ? 47.89767 33.92393 85.22647  1.000 18.51558  ? 446 HOH A O   1 
HETATM 3336 O  O   . HOH J 6 .   ? 40.37922 36.32521 102.65951 1.000 17.79028  ? 447 HOH A O   1 
HETATM 3337 O  O   . HOH J 6 .   ? 46.24364 19.25928 88.63267  1.000 18.41257  ? 448 HOH A O   1 
HETATM 3338 O  O   . HOH J 6 .   ? 19.03404 25.95189 78.68467  1.000 24.72266  ? 449 HOH A O   1 
HETATM 3339 O  O   . HOH J 6 .   ? 35.90163 29.22157 72.11523  1.000 32.18395  ? 450 HOH A O   1 
HETATM 3340 O  O   . HOH J 6 .   ? 69.44468 20.38088 92.39128  1.000 27.21302  ? 451 HOH A O   1 
HETATM 3341 O  O   . HOH J 6 .   ? 64.53627 23.84893 103.82382 1.000 15.82884  ? 452 HOH A O   1 
HETATM 3342 O  O   . HOH J 6 .   ? 54.75042 17.77342 97.80047  1.000 15.21239  ? 453 HOH A O   1 
HETATM 3343 O  O   . HOH J 6 .   ? 43.91200 36.30920 89.67249  1.000 13.45301  ? 454 HOH A O   1 
HETATM 3344 O  O   . HOH J 6 .   ? 37.87939 28.05748 106.74451 1.000 23.43964  ? 455 HOH A O   1 
HETATM 3345 O  O   . HOH J 6 .   ? 36.17338 22.92463 99.06513  1.000 16.03049  ? 456 HOH A O   1 
HETATM 3346 O  O   . HOH J 6 .   ? 59.54064 12.56116 100.63710 1.000 28.30912  ? 457 HOH A O   1 
HETATM 3347 O  O   . HOH J 6 .   ? 59.19506 39.26652 86.39472  1.000 24.62189  ? 458 HOH A O   1 
HETATM 3348 O  O   . HOH J 6 .   ? 64.59334 42.36946 96.21613  1.000 32.33749  ? 459 HOH A O   1 
HETATM 3349 O  O   . HOH J 6 .   ? 35.95956 49.12062 100.96759 1.000 15.81293  ? 460 HOH A O   1 
HETATM 3350 O  O   . HOH J 6 .   ? 44.86501 43.43515 104.02261 1.000 17.95580  ? 461 HOH A O   1 
HETATM 3351 O  O   . HOH J 6 .   ? 54.66279 38.99318 85.45313  1.000 28.82488  ? 462 HOH A O   1 
HETATM 3352 O  O   . HOH J 6 .   ? 60.21409 44.92437 108.95419 1.000 20.99526  ? 463 HOH A O   1 
HETATM 3353 O  O   . HOH J 6 .   ? 58.50149 12.20437 91.75785  1.000 26.83154  ? 464 HOH A O   1 
HETATM 3354 O  O   . HOH J 6 .   ? 27.39945 23.66434 88.99882  1.000 26.16158  ? 465 HOH A O   1 
HETATM 3355 O  O   . HOH J 6 .   ? 56.38830 32.43522 107.66089 1.000 21.55251  ? 466 HOH A O   1 
HETATM 3356 O  O   . HOH J 6 .   ? 39.69942 24.34655 73.58465  1.000 25.05635  ? 467 HOH A O   1 
HETATM 3357 O  O   . HOH J 6 .   ? 37.08782 47.79867 97.58892  1.000 27.29401  ? 468 HOH A O   1 
HETATM 3358 O  O   . HOH J 6 .   ? 44.95167 55.02012 98.50542  1.000 25.44426  ? 469 HOH A O   1 
HETATM 3359 O  O   . HOH J 6 .   ? 46.43214 20.99078 104.58833 1.000 18.19576  ? 470 HOH A O   1 
HETATM 3360 O  O   . HOH J 6 .   ? 19.94779 24.15655 74.41750  1.000 33.27610  ? 471 HOH A O   1 
HETATM 3361 O  O   . HOH J 6 .   ? 62.63399 23.59981 84.52222  1.000 32.16060  ? 472 HOH A O   1 
HETATM 3362 O  O   . HOH J 6 .   ? 44.30790 22.18178 106.09079 1.000 17.42860  ? 473 HOH A O   1 
HETATM 3363 O  O   . HOH J 6 .   ? 65.93848 20.71049 100.24479 1.000 28.52979  ? 474 HOH A O   1 
HETATM 3364 O  O   . HOH J 6 .   ? 42.70227 39.38615 105.12409 1.000 22.41225  ? 475 HOH A O   1 
HETATM 3365 O  O   . HOH J 6 .   ? 34.58899 39.12994 90.54128  1.000 32.77913  ? 476 HOH A O   1 
HETATM 3366 O  O   . HOH J 6 .   ? 59.32893 14.85361 90.52048  1.000 28.10407  ? 477 HOH A O   1 
HETATM 3367 O  O   . HOH J 6 .   ? 57.012   28.203   77.434    1.000 31.22138  ? 478 HOH A O   1 
HETATM 3368 O  O   . HOH J 6 .   ? 63.83085 39.69661 93.29917  1.000 26.46128  ? 479 HOH A O   1 
HETATM 3369 O  O   . HOH J 6 .   ? 46.83844 35.30024 79.04407  1.000 32.78206  ? 480 HOH A O   1 
HETATM 3370 O  O   . HOH J 6 .   ? 64.12772 16.58002 95.34106  1.000 18.97164  ? 481 HOH A O   1 
HETATM 3371 O  O   . HOH J 6 .   ? 27.87079 20.35607 80.85451  1.000 23.21117  ? 482 HOH A O   1 
HETATM 3372 O  O   . HOH J 6 .   ? 63.19555 14.55565 97.03134  1.000 32.04283  ? 483 HOH A O   1 
HETATM 3373 O  O   . HOH J 6 .   ? 37.56539 44.54863 99.99211  1.000 18.91521  ? 484 HOH A O   1 
HETATM 3374 O  O   . HOH J 6 .   ? 44.86974 37.61160 87.42834  1.000 19.00267  ? 485 HOH A O   1 
HETATM 3375 O  O   . HOH J 6 .   ? 51.29872 22.34071 110.83483 1.000 24.12349  ? 486 HOH A O   1 
HETATM 3376 O  O   . HOH J 6 .   ? 63.89511 39.46130 95.55733  1.000 26.45841  ? 487 HOH A O   1 
HETATM 3377 O  O   . HOH J 6 .   ? 51.88932 52.30666 108.72802 1.000 34.35281  ? 488 HOH A O   1 
HETATM 3378 O  O   . HOH J 6 .   ? 21.66015 20.02441 79.52914  1.000 33.08984  ? 489 HOH A O   1 
HETATM 3379 O  O   . HOH J 6 .   ? 18.40467 24.15017 80.12384  1.000 30.24716  ? 490 HOH A O   1 
HETATM 3380 O  O   . HOH J 6 .   ? 65.21425 36.46496 88.21460  1.000 34.20197  ? 491 HOH A O   1 
HETATM 3381 O  O   . HOH J 6 .   ? 54.01383 18.30635 113.75476 1.000 23.21083  ? 492 HOH A O   1 
HETATM 3382 O  O   . HOH J 6 .   ? 64.52508 18.19606 100.26062 1.000 29.77467  ? 493 HOH A O   1 
HETATM 3383 O  O   . HOH J 6 .   ? 63.934   51.141   99.135    1.000 34.37289  ? 494 HOH A O   1 
HETATM 3384 O  O   . HOH J 6 .   ? 66.95147 31.13894 96.41792  1.000 30.68254  ? 495 HOH A O   1 
HETATM 3385 O  O   . HOH J 6 .   ? 38.10652 18.88633 81.94259  1.000 32.83275  ? 496 HOH A O   1 
HETATM 3386 O  O   . HOH J 6 .   ? 32.504   18.859   67.909    1.000 29.89423  ? 497 HOH A O   1 
HETATM 3387 O  O   . HOH J 6 .   ? 36.80935 53.30908 96.35394  1.000 33.35488  ? 498 HOH A O   1 
HETATM 3388 O  O   . HOH J 6 .   ? 57.01396 22.51675 80.08647  1.000 34.06037  ? 499 HOH A O   1 
HETATM 3389 O  O   . HOH J 6 .   ? 18.22256 25.29880 76.31449  1.000 25.64507  ? 500 HOH A O   1 
HETATM 3390 O  O   . HOH J 6 .   ? 29.35382 17.52868 70.62128  1.000 33.48738  ? 501 HOH A O   1 
HETATM 3391 O  O   . HOH J 6 .   ? 38.815   28.913   111.706   1.000 31.66887  ? 502 HOH A O   1 
HETATM 3392 O  O   . HOH J 6 .   ? 70.12806 28.94111 100.18497 1.000 18.32970  ? 503 HOH A O   1 
HETATM 3393 O  O   . HOH J 6 .   ? 47.42558 16.78295 89.21361  1.000 22.20050  ? 504 HOH A O   1 
HETATM 3394 O  O   . HOH J 6 .   ? 57.70043 14.18350 88.01894  1.000 32.18106  ? 505 HOH A O   1 
HETATM 3395 O  O   . HOH J 6 .   ? 34.71601 40.42596 92.82390  1.000 23.78589  ? 506 HOH A O   1 
HETATM 3396 O  O   . HOH J 6 .   ? 37.89707 47.19872 100.57295 1.000 19.03332  ? 507 HOH A O   1 
HETATM 3397 O  O   . HOH J 6 .   ? 53.26595 30.10824 77.59480  1.000 27.64531  ? 508 HOH A O   1 
HETATM 3398 O  O   . HOH J 6 .   ? 53.85671 43.03694 85.32272  1.000 33.53639  ? 509 HOH A O   1 
HETATM 3399 O  O   . HOH J 6 .   ? 65.70276 32.67702 87.07358  1.000 35.24391  ? 510 HOH A O   1 
HETATM 3400 O  O   . HOH J 6 .   ? 26.51480 21.51193 74.79926  1.000 25.17526  ? 511 HOH A O   1 
HETATM 3401 O  O   . HOH J 6 .   ? 31.86036 17.04976 71.48227  1.000 31.30670  ? 512 HOH A O   1 
HETATM 3402 O  O   . HOH J 6 .   ? 40.32474 30.47316 101.85998 1.000 20.52924  ? 513 HOH A O   1 
HETATM 3403 O  O   . HOH J 6 .   ? 41.12638 14.65374 85.05421  1.000 26.87022  ? 514 HOH A O   1 
HETATM 3404 O  O   . HOH J 6 .   ? 61.57762 11.60122 103.65864 1.000 29.67431  ? 515 HOH A O   1 
HETATM 3405 O  O   . HOH J 6 .   ? 32.53505 25.66469 91.93597  1.000 26.92993  ? 516 HOH A O   1 
HETATM 3406 O  O   . HOH J 6 .   ? 36.65325 23.74791 106.46624 1.000 24.48298  ? 517 HOH A O   1 
HETATM 3407 O  O   . HOH J 6 .   ? 68.332   20.291   98.852    1.000 29.70574  ? 518 HOH A O   1 
HETATM 3408 O  O   . HOH J 6 .   ? 58.58311 37.19239 84.70249  1.000 28.11357  ? 519 HOH A O   1 
HETATM 3409 O  O   . HOH J 6 .   ? 67.48740 30.56239 86.24347  1.000 34.71106  ? 520 HOH A O   1 
HETATM 3410 O  O   . HOH J 6 .   ? 67.87753 19.07387 90.08129  1.000 33.00936  ? 521 HOH A O   1 
HETATM 3411 O  O   . HOH J 6 .   ? 45.98666 37.80451 110.59506 1.000 31.16739  ? 522 HOH A O   1 
HETATM 3412 O  O   . HOH J 6 .   ? 44.09995 35.78683 108.15336 1.000 26.18494  ? 523 HOH A O   1 
HETATM 3413 O  O   . HOH J 6 .   ? 38.45521 34.41803 103.24887 1.000 24.38372  ? 524 HOH A O   1 
HETATM 3414 O  O   . HOH J 6 .   ? 38.64943 29.92903 109.14752 1.000 29.60673  ? 525 HOH A O   1 
HETATM 3415 O  O   . HOH J 6 .   ? 65.28007 15.37972 93.21062  1.000 31.00015  ? 526 HOH A O   1 
HETATM 3416 O  O   . HOH J 6 .   ? 63.79759 27.71596 106.21685 1.000 21.45560  ? 527 HOH A O   1 
HETATM 3417 O  O   . HOH J 6 .   ? 47.14525 39.71618 86.87636  1.000 31.28679  ? 528 HOH A O   1 
HETATM 3418 O  O   . HOH J 6 .   ? 40.93088 30.81670 104.53700 1.000 17.89969  ? 529 HOH A O   1 
HETATM 3419 O  O   . HOH J 6 .   ? 39.26592 28.01773 102.39346 1.000 19.09586  ? 530 HOH A O   1 
HETATM 3420 O  O   . HOH J 6 .   ? 29.85496 18.88679 82.73145  1.000 32.72701  ? 531 HOH A O   1 
HETATM 3421 O  O   . HOH J 6 .   ? 59.25236 47.57006 88.22922  1.000 34.74607  ? 532 HOH A O   1 
HETATM 3422 O  O   . HOH J 6 .   ? 56.16313 37.43815 83.72867  1.000 31.47056  ? 533 HOH A O   1 
HETATM 3423 O  O   . HOH J 6 .   ? 64.11267 15.16897 90.85866  1.000 30.37116  ? 534 HOH A O   1 
HETATM 3424 O  O   . HOH J 6 .   ? 40.062   14.889   79.919    1.000 32.29559  ? 535 HOH A O   1 
HETATM 3425 O  O   . HOH J 6 .   ? 69.90873 27.90803 102.75469 1.000 27.31305  ? 536 HOH A O   1 
HETATM 3426 O  O   . HOH J 6 .   ? 63.51401 24.09789 106.63991 1.000 33.15514  ? 537 HOH A O   1 
HETATM 3427 O  O   . HOH J 6 .   ? 59.53098 49.50479 108.95771 1.000 29.86935  ? 538 HOH A O   1 
HETATM 3428 O  O   . HOH J 6 .   ? 57.78030 32.67604 82.49868  1.000 29.85583  ? 539 HOH A O   1 
HETATM 3429 O  O   . HOH J 6 .   ? 64.29095 18.05491 102.93289 1.000 34.19363  ? 540 HOH A O   1 
HETATM 3430 O  O   . HOH J 6 .   ? 33.67098 32.94427 94.93476  1.000 29.98325  ? 541 HOH A O   1 
HETATM 3431 O  O   . HOH J 6 .   ? 36.29966 50.85298 96.96382  1.000 31.81673  ? 542 HOH A O   1 
HETATM 3432 O  O   . HOH J 6 .   ? 15.76701 23.20799 81.81375  1.000 26.51695  ? 543 HOH A O   1 
HETATM 3433 O  O   . HOH J 6 .   ? 41.67406 36.88543 104.95795 1.000 25.66691  ? 544 HOH A O   1 
HETATM 3434 O  O   . HOH J 6 .   ? 34.57028 27.36795 97.70261  1.000 33.96698  ? 545 HOH A O   1 
HETATM 3435 O  O   . HOH J 6 .   ? 32.70606 19.50003 83.73190  1.000 28.66194  ? 546 HOH A O   1 
HETATM 3436 O  O   . HOH J 6 .   ? 65.77975 17.87668 88.76193  1.000 29.84643  ? 547 HOH A O   1 
HETATM 3437 O  O   . HOH J 6 .   ? 50.11486 35.12440 84.22884  1.000 26.46424  ? 548 HOH A O   1 
HETATM 3438 O  O   . HOH J 6 .   ? 42.75997 34.68122 106.25409 1.000 24.84278  ? 549 HOH A O   1 
HETATM 3439 O  O   . HOH J 6 .   ? 53.07803 32.50984 82.02396  1.000 25.74467  ? 550 HOH A O   1 
HETATM 3440 O  O   . HOH J 6 .   ? 59.78510 34.91300 85.68356  1.000 29.44922  ? 551 HOH A O   1 
HETATM 3441 O  O   . HOH J 6 .   ? 33.62214 42.78548 96.12438  1.000 30.02384  ? 552 HOH A O   1 
HETATM 3442 O  O   . HOH J 6 .   ? 33.90284 38.28130 98.18577  1.000 33.91703  ? 553 HOH A O   1 
HETATM 3443 O  O   . HOH J 6 .   ? 29.24270 24.44041 68.73990  1.000 35.48349  ? 554 HOH A O   1 
HETATM 3444 O  O   . HOH J 6 .   ? 46.78881 33.13756 82.90162  1.000 25.15913  ? 555 HOH A O   1 
HETATM 3445 O  O   . HOH J 6 .   ? 56.46409 17.31227 113.15805 1.000 26.86455  ? 556 HOH A O   1 
HETATM 3446 O  O   . HOH J 6 .   ? 70.271   35.281   98.805    1.000 29.78324  ? 557 HOH A O   1 
HETATM 3447 O  O   . HOH J 6 .   ? 57.95645 47.69961 86.10257  1.000 30.88587  ? 558 HOH A O   1 
HETATM 3448 O  O   . HOH J 6 .   ? 47.53538 38.41644 84.65769  1.000 37.31752  ? 559 HOH A O   1 
HETATM 3449 O  O   . HOH J 6 .   ? 56.37900 19.62160 81.00451  1.000 28.68984  ? 560 HOH A O   1 
HETATM 3450 O  O   . HOH J 6 .   ? 65.44050 49.30562 100.69240 1.000 34.45704  ? 561 HOH A O   1 
HETATM 3451 O  O   . HOH J 6 .   ? 47.64034 44.49820 86.13761  1.000 30.80391  ? 562 HOH A O   1 
HETATM 3452 O  O   . HOH J 6 .   ? 34.88143 31.54989 98.73702  1.000 29.63796  ? 563 HOH A O   1 
HETATM 3453 O  O   . HOH J 6 .   ? 43.85779 15.65767 88.00050  1.000 24.57469  ? 564 HOH A O   1 
HETATM 3454 O  O   . HOH J 6 .   ? 44.80454 39.62397 106.85167 1.000 22.35411  ? 565 HOH A O   1 
HETATM 3455 O  O   . HOH J 6 .   ? 67.08323 41.74147 95.92963  1.000 32.74567  ? 566 HOH A O   1 
HETATM 3456 O  O   . HOH J 6 .   ? 35.53501 26.83377 100.24027 1.000 22.28408  ? 567 HOH A O   1 
HETATM 3457 O  O   . HOH J 6 .   ? 46.03094 42.20381 106.19579 1.000 26.79245  ? 568 HOH A O   1 
HETATM 3458 O  O   . HOH J 6 .   ? 43.87177 18.43377 88.64212  1.000 21.93044  ? 569 HOH A O   1 
HETATM 3459 O  O   . HOH J 6 .   ? 51.18692 42.83151 85.36886  1.000 26.34144  ? 570 HOH A O   1 
HETATM 3460 O  O   . HOH J 6 .   ? 38.89470 38.74844 102.08274 1.000 18.77943  ? 571 HOH A O   1 
HETATM 3461 O  O   . HOH J 6 .   ? 36.10495 40.13262 98.71738  1.000 29.55136  ? 572 HOH A O   1 
HETATM 3462 O  O   . HOH J 6 .   ? 28.68538 19.79232 78.47332  1.000 26.78648  ? 573 HOH A O   1 
HETATM 3463 O  O   . HOH J 6 .   ? 44.04418 18.29190 91.49707  1.000 22.09151  ? 574 HOH A O   1 
HETATM 3464 O  O   . HOH J 6 .   ? 37.63792 37.96844 99.77146  1.000 27.39440  ? 575 HOH A O   1 
HETATM 3465 O  O   . HOH J 6 .   ? 36.60286 28.76584 102.11665 1.000 27.35889  ? 576 HOH A O   1 
HETATM 3466 O  O   . HOH J 6 .   ? 60.07151 49.60537 89.46615  1.000 32.18875  ? 577 HOH A O   1 
HETATM 3467 O  O   . HOH J 6 .   ? 54.52986 32.39295 79.57084  1.000 30.92420  ? 578 HOH A O   1 
HETATM 3468 O  O   . HOH J 6 .   ? 30.97145 24.00621 93.17066  1.000 30.50010  ? 579 HOH A O   1 
HETATM 3469 O  O   . HOH J 6 .   ? 38.95778 32.78361 105.26217 1.000 28.62491  ? 580 HOH A O   1 
HETATM 3470 O  O   . HOH J 6 .   ? 55.99940 34.63026 82.12599  1.000 33.08737  ? 581 HOH A O   1 
HETATM 3471 O  O   . HOH J 6 .   ? 71.33056 29.91549 104.07665 1.000 31.07483  ? 582 HOH A O   1 
HETATM 3472 O  O   . HOH K 6 .   ? 32.82932 42.14251 77.40412  1.000 34.17300  ? 301 HOH B O   1 
HETATM 3473 O  O   . HOH K 6 .   ? -8.01895 30.00089 89.69455  1.000 28.24659  ? 302 HOH B O   1 
HETATM 3474 O  O   . HOH K 6 .   ? 22.37169 35.11753 74.50459  1.000 19.38255  ? 303 HOH B O   1 
HETATM 3475 O  O   . HOH K 6 .   ? -2.25093 20.02466 102.01349 1.000 29.08160  ? 304 HOH B O   1 
HETATM 3476 O  O   . HOH K 6 .   ? 6.09881  18.45655 79.16647  1.000 32.94098  ? 305 HOH B O   1 
HETATM 3477 O  O   . HOH K 6 .   ? 32.94882 44.01338 71.82613  1.000 24.62062  ? 306 HOH B O   1 
HETATM 3478 O  O   . HOH K 6 .   ? 43.60051 35.97269 83.53443  1.000 23.89860  ? 307 HOH B O   1 
HETATM 3479 O  O   . HOH K 6 .   ? 38.20035 40.81122 79.23842  1.000 26.34413  ? 308 HOH B O   1 
HETATM 3480 O  O   . HOH K 6 .   ? -6.10531 38.47850 85.56338  1.000 24.81740  ? 309 HOH B O   1 
HETATM 3481 O  O   . HOH K 6 .   ? 19.62628 39.71013 87.80405  1.000 26.40988  ? 310 HOH B O   1 
HETATM 3482 O  O   . HOH K 6 .   ? 10.65998 5.93000  89.04366  1.000 20.75328  ? 311 HOH B O   1 
HETATM 3483 O  O   . HOH K 6 .   ? 17.253   23.741   106.656   1.000 32.92596  ? 312 HOH B O   1 
HETATM 3484 O  O   . HOH K 6 .   ? 3.02428  34.15561 71.96364  1.000 20.73305  ? 313 HOH B O   1 
HETATM 3485 O  O   . HOH K 6 .   ? 0.60853  8.57072  104.68728 1.000 27.49356  ? 314 HOH B O   1 
HETATM 3486 O  O   . HOH K 6 .   ? -0.93579 26.63091 107.00937 1.000 30.07056  ? 315 HOH B O   1 
HETATM 3487 O  O   . HOH K 6 .   ? 21.66960 14.80118 84.73150  1.000 30.31342  ? 316 HOH B O   1 
HETATM 3488 O  O   . HOH K 6 .   ? -1.18321 33.59532 107.84002 1.000 31.04789  ? 317 HOH B O   1 
HETATM 3489 O  O   . HOH K 6 .   ? 29.57419 30.31017 83.50105  1.000 16.59737  ? 318 HOH B O   1 
HETATM 3490 O  O   . HOH K 6 .   ? 10.91838 7.00450  101.75654 1.000 31.84296  ? 319 HOH B O   1 
HETATM 3491 O  O   . HOH K 6 .   ? 32.37103 38.74200 89.61152  1.000 26.96338  ? 320 HOH B O   1 
HETATM 3492 O  O   . HOH K 6 .   ? 24.16609 24.62782 94.68478  1.000 18.86717  ? 321 HOH B O   1 
HETATM 3493 O  O   . HOH K 6 .   ? -7.64296 21.74850 99.20334  1.000 28.23232  ? 322 HOH B O   1 
HETATM 3494 O  O   . HOH K 6 .   ? 26.71104 41.78396 76.74678  1.000 21.28129  ? 323 HOH B O   1 
HETATM 3495 O  O   . HOH K 6 .   ? 19.75660 33.75444 99.79208  0.50  14.86314  ? 324 HOH B O   1 
HETATM 3496 O  O   . HOH K 6 .   ? -6.01277 39.28288 94.15813  1.000 28.62234  ? 325 HOH B O   1 
HETATM 3497 O  O   . HOH K 6 .   ? -8.17846 20.15318 89.60162  1.000 15.16901  ? 326 HOH B O   1 
HETATM 3498 O  O   . HOH K 6 .   ? 21.05247 20.82260 96.06781  1.000 26.20647  ? 327 HOH B O   1 
HETATM 3499 O  O   . HOH K 6 .   ? -1.57496 18.49363 95.28967  1.000 17.77642  ? 328 HOH B O   1 
HETATM 3500 O  O   . HOH K 6 .   ? -3.55391 10.98690 100.15390 1.000 27.40117  ? 329 HOH B O   1 
HETATM 3501 O  O   . HOH K 6 .   ? -4.84701 14.05700 98.55071  1.000 32.28423  ? 330 HOH B O   1 
HETATM 3502 O  O   . HOH K 6 .   ? -7.95264 34.60127 85.66374  1.000 30.93111  ? 331 HOH B O   1 
HETATM 3503 O  O   . HOH K 6 .   ? 14.75936 43.61664 83.07282  1.000 33.88530  ? 332 HOH B O   1 
HETATM 3504 O  O   . HOH K 6 .   ? 2.21854  37.91777 109.57712 1.000 23.27086  ? 333 HOH B O   1 
HETATM 3505 O  O   . HOH K 6 .   ? -3.02255 38.64998 102.25316 1.000 33.52487  ? 334 HOH B O   1 
HETATM 3506 O  O   . HOH K 6 .   ? 24.09519 30.44458 94.87369  1.000 17.17308  ? 335 HOH B O   1 
HETATM 3507 O  O   . HOH K 6 .   ? 23.613   37.223   74.339    1.000 31.31466  ? 336 HOH B O   1 
HETATM 3508 O  O   . HOH K 6 .   ? 12.03384 21.84604 107.41585 1.000 26.29236  ? 337 HOH B O   1 
HETATM 3509 O  O   . HOH K 6 .   ? 26.51764 19.43262 88.11472  1.000 30.08639  ? 338 HOH B O   1 
HETATM 3510 O  O   . HOH K 6 .   ? -8.36219 28.05098 92.40636  1.000 18.01106  ? 339 HOH B O   1 
HETATM 3511 O  O   . HOH K 6 .   ? -3.31121 22.00684 100.42392 1.000 20.50107  ? 340 HOH B O   1 
HETATM 3512 O  O   . HOH K 6 .   ? 12.04771 17.92814 83.42408  1.000 18.66913  ? 341 HOH B O   1 
HETATM 3513 O  O   . HOH K 6 .   ? -6.54376 17.70134 89.90934  1.000 32.64467  ? 342 HOH B O   1 
HETATM 3514 O  O   . HOH K 6 .   ? 16.30654 39.90494 76.75811  1.000 31.48135  ? 343 HOH B O   1 
HETATM 3515 O  O   . HOH K 6 .   ? 3.95402  2.00967  94.49358  1.000 26.46203  ? 344 HOH B O   1 
HETATM 3516 O  O   . HOH K 6 .   ? 5.04568  29.28919 77.17612  1.000 24.32567  ? 345 HOH B O   1 
HETATM 3517 O  O   . HOH K 6 .   ? 20.86416 23.15228 99.10620  1.000 22.18979  ? 346 HOH B O   1 
HETATM 3518 O  O   . HOH K 6 .   ? 15.92977 23.75531 88.23075  1.000 14.20135  ? 347 HOH B O   1 
HETATM 3519 O  O   . HOH K 6 .   ? 15.09551 2.72391  94.76060  1.000 24.06019  ? 348 HOH B O   1 
HETATM 3520 O  O   . HOH K 6 .   ? -0.71022 11.93724 86.71203  1.000 27.70789  ? 349 HOH B O   1 
HETATM 3521 O  O   . HOH K 6 .   ? -3.21507 33.84211 90.13125  1.000 15.04682  ? 350 HOH B O   1 
HETATM 3522 O  O   . HOH K 6 .   ? 6.54231  12.75796 78.60004  1.000 30.44492  ? 351 HOH B O   1 
HETATM 3523 O  O   . HOH K 6 .   ? 6.31025  18.85914 106.38266 1.000 23.99226  ? 352 HOH B O   1 
HETATM 3524 O  O   . HOH K 6 .   ? 16.54264 25.76338 92.03588  1.000 14.76920  ? 353 HOH B O   1 
HETATM 3525 O  O   . HOH K 6 .   ? 22.58522 16.75436 83.11337  1.000 30.40493  ? 354 HOH B O   1 
HETATM 3526 O  O   . HOH K 6 .   ? -6.15693 18.24142 86.67655  1.000 30.55360  ? 355 HOH B O   1 
HETATM 3527 O  O   . HOH K 6 .   ? 19.58091 29.99118 100.72017 1.000 14.10049  ? 356 HOH B O   1 
HETATM 3528 O  O   . HOH K 6 .   ? 23.98563 14.96580 93.05347  1.000 23.75201  ? 357 HOH B O   1 
HETATM 3529 O  O   . HOH K 6 .   ? 2.04548  9.06510  85.85935  1.000 30.73858  ? 358 HOH B O   1 
HETATM 3530 O  O   . HOH K 6 .   ? 29.14511 37.72894 87.74967  1.000 16.45066  ? 359 HOH B O   1 
HETATM 3531 O  O   . HOH K 6 .   ? 6.92196  20.78994 80.30504  1.000 28.99356  ? 360 HOH B O   1 
HETATM 3532 O  O   . HOH K 6 .   ? 4.72336  31.70902 93.97363  1.000 14.42645  ? 361 HOH B O   1 
HETATM 3533 O  O   . HOH K 6 .   ? 12.36660 16.79088 103.50194 1.000 21.33039  ? 362 HOH B O   1 
HETATM 3534 O  O   . HOH K 6 .   ? 13.36510 4.49214  96.87707  1.000 20.68967  ? 363 HOH B O   1 
HETATM 3535 O  O   . HOH K 6 .   ? 4.47265  32.68037 91.45689  1.000 15.35821  ? 364 HOH B O   1 
HETATM 3536 O  O   . HOH K 6 .   ? 20.21257 12.25361 87.86827  1.000 26.47732  ? 365 HOH B O   1 
HETATM 3537 O  O   . HOH K 6 .   ? 30.52283 42.86421 76.16596  1.000 32.89121  ? 366 HOH B O   1 
HETATM 3538 O  O   . HOH K 6 .   ? -7.44119 21.90361 95.05091  1.000 15.37620  ? 367 HOH B O   1 
HETATM 3539 O  O   . HOH K 6 .   ? -5.17136 9.38643  94.30322  1.000 27.95683  ? 368 HOH B O   1 
HETATM 3540 O  O   . HOH K 6 .   ? 13.19865 33.22691 101.03475 1.000 15.15145  ? 369 HOH B O   1 
HETATM 3541 O  O   . HOH K 6 .   ? 18.76877 14.95075 97.85495  1.000 19.14719  ? 370 HOH B O   1 
HETATM 3542 O  O   . HOH K 6 .   ? -8.63591 35.29005 89.27314  1.000 31.38477  ? 371 HOH B O   1 
HETATM 3543 O  O   . HOH K 6 .   ? 8.802    9.762    103.191   1.000 35.91618  ? 372 HOH B O   1 
HETATM 3544 O  O   . HOH K 6 .   ? 25.80611 27.38500 95.87502  1.000 32.87453  ? 373 HOH B O   1 
HETATM 3545 O  O   . HOH K 6 .   ? 14.00956 35.93657 98.85029  1.000 15.55394  ? 374 HOH B O   1 
HETATM 3546 O  O   . HOH K 6 .   ? 32.21440 29.21646 83.44466  1.000 17.55031  ? 375 HOH B O   1 
HETATM 3547 O  O   . HOH K 6 .   ? 6.36912  36.22817 77.23991  1.000 21.31635  ? 376 HOH B O   1 
HETATM 3548 O  O   . HOH K 6 .   ? 33.73668 39.78749 78.59610  1.000 20.50519  ? 377 HOH B O   1 
HETATM 3549 O  O   . HOH K 6 .   ? 0.73686  13.96530 81.50643  1.000 30.96781  ? 378 HOH B O   1 
HETATM 3550 O  O   . HOH K 6 .   ? 3.90422  44.05801 85.62060  1.000 19.36203  ? 379 HOH B O   1 
HETATM 3551 O  O   . HOH K 6 .   ? 27.25436 21.41270 92.63394  1.000 31.94633  ? 380 HOH B O   1 
HETATM 3552 O  O   . HOH K 6 .   ? -2.59015 24.81550 82.63902  1.000 31.12183  ? 381 HOH B O   1 
HETATM 3553 O  O   . HOH K 6 .   ? 0.40803  30.56570 76.93795  1.000 25.32559  ? 382 HOH B O   1 
HETATM 3554 O  O   . HOH K 6 .   ? 7.88408  28.34125 80.81163  1.000 18.80138  ? 383 HOH B O   1 
HETATM 3555 O  O   . HOH K 6 .   ? 21.87013 31.34486 92.11248  1.000 15.44803  ? 384 HOH B O   1 
HETATM 3556 O  O   . HOH K 6 .   ? 24.04686 18.50505 84.85693  1.000 30.77135  ? 385 HOH B O   1 
HETATM 3557 O  O   . HOH K 6 .   ? 15.00046 38.98190 88.74812  1.000 17.63894  ? 386 HOH B O   1 
HETATM 3558 O  O   . HOH K 6 .   ? -8.69732 25.31443 94.38964  1.000 17.23729  ? 387 HOH B O   1 
HETATM 3559 O  O   . HOH K 6 .   ? 25.57172 32.96036 91.49495  1.000 21.94885  ? 388 HOH B O   1 
HETATM 3560 O  O   . HOH K 6 .   ? 15.80962 22.58907 103.12011 1.000 19.48964  ? 389 HOH B O   1 
HETATM 3561 O  O   . HOH K 6 .   ? -2.86201 8.07117  97.23052  1.000 23.69406  ? 390 HOH B O   1 
HETATM 3562 O  O   . HOH K 6 .   ? -5.71914 35.31013 96.95474  1.000 22.11356  ? 391 HOH B O   1 
HETATM 3563 O  O   . HOH K 6 .   ? 0.20235  24.88207 83.07027  1.000 25.99727  ? 392 HOH B O   1 
HETATM 3564 O  O   . HOH K 6 .   ? -4.77998 9.64522  91.86598  1.000 24.59260  ? 393 HOH B O   1 
HETATM 3565 O  O   . HOH K 6 .   ? 10.66331 4.90741  91.64394  1.000 22.77088  ? 394 HOH B O   1 
HETATM 3566 O  O   . HOH K 6 .   ? 19.51847 2.17122  88.49738  1.000 32.95216  ? 395 HOH B O   1 
HETATM 3567 O  O   . HOH K 6 .   ? 9.75842  35.17312 104.73191 1.000 19.54278  ? 396 HOH B O   1 
HETATM 3568 O  O   . HOH K 6 .   ? 22.07826 22.92449 94.35615  1.000 25.54276  ? 397 HOH B O   1 
HETATM 3569 O  O   . HOH K 6 .   ? 9.05221  34.54465 74.15808  1.000 27.74896  ? 398 HOH B O   1 
HETATM 3570 O  O   . HOH K 6 .   ? -8.90045 27.46113 88.96292  1.000 26.88549  ? 399 HOH B O   1 
HETATM 3571 O  O   . HOH K 6 .   ? 5.34414  28.90128 80.46229  1.000 24.39198  ? 400 HOH B O   1 
HETATM 3572 O  O   . HOH K 6 .   ? 0.94036  15.76258 103.83522 1.000 24.99094  ? 401 HOH B O   1 
HETATM 3573 O  O   . HOH K 6 .   ? 12.78322 32.83408 92.60244  1.000 15.58022  ? 402 HOH B O   1 
HETATM 3574 O  O   . HOH K 6 .   ? 2.69072  24.00535 104.98909 1.000 21.82431  ? 403 HOH B O   1 
HETATM 3575 O  O   . HOH K 6 .   ? 12.51582 2.84144  91.10039  1.000 24.40119  ? 404 HOH B O   1 
HETATM 3576 O  O   . HOH K 6 .   ? -0.75266 7.78965  98.90630  1.000 20.47551  ? 405 HOH B O   1 
HETATM 3577 O  O   . HOH K 6 .   ? 4.43917  2.51226  99.85714  1.000 21.12218  ? 406 HOH B O   1 
HETATM 3578 O  O   . HOH K 6 .   ? 14.53527 38.43584 91.37402  1.000 22.68678  ? 407 HOH B O   1 
HETATM 3579 O  O   . HOH K 6 .   ? 12.06265 28.95070 78.73460  1.000 30.08188  ? 408 HOH B O   1 
HETATM 3580 O  O   . HOH K 6 .   ? 20.80294 26.63557 105.49415 1.000 24.97204  ? 409 HOH B O   1 
HETATM 3581 O  O   . HOH K 6 .   ? -4.12500 6.08082  95.97695  1.000 28.87317  ? 410 HOH B O   1 
HETATM 3582 O  O   . HOH K 6 .   ? 6.48735  3.86630  88.77091  1.000 29.15676  ? 411 HOH B O   1 
HETATM 3583 O  O   . HOH K 6 .   ? -0.94910 4.66621  90.32204  1.000 30.41468  ? 412 HOH B O   1 
HETATM 3584 O  O   . HOH K 6 .   ? 3.96730  37.50459 74.43662  1.000 20.05651  ? 413 HOH B O   1 
HETATM 3585 O  O   . HOH K 6 .   ? 43.02292 37.14663 77.42241  1.000 30.59506  ? 414 HOH B O   1 
HETATM 3586 O  O   . HOH K 6 .   ? 5.70698  39.14858 94.11751  1.000 16.29963  ? 415 HOH B O   1 
HETATM 3587 O  O   . HOH K 6 .   ? 19.08967 8.78787  95.69785  1.000 17.78175  ? 416 HOH B O   1 
HETATM 3588 O  O   . HOH K 6 .   ? 12.15247 37.53955 72.14595  1.000 31.20242  ? 417 HOH B O   1 
HETATM 3589 O  O   . HOH K 6 .   ? 43.11450 34.33346 81.45176  1.000 19.53476  ? 418 HOH B O   1 
HETATM 3590 O  O   . HOH K 6 .   ? -5.48973 28.41013 99.54501  1.000 17.15573  ? 419 HOH B O   1 
HETATM 3591 O  O   . HOH K 6 .   ? -2.86449 28.17833 103.17635 1.000 18.49292  ? 420 HOH B O   1 
HETATM 3592 O  O   . HOH K 6 .   ? -5.95581 31.28574 82.21826  1.000 21.72993  ? 421 HOH B O   1 
HETATM 3593 O  O   . HOH K 6 .   ? -4.67479 30.91688 100.40224 1.000 18.65628  ? 422 HOH B O   1 
HETATM 3594 O  O   . HOH K 6 .   ? 23.16804 40.16625 86.70432  1.000 32.33169  ? 423 HOH B O   1 
HETATM 3595 O  O   . HOH K 6 .   ? 23.61717 33.05918 99.30487  1.000 17.26930  ? 424 HOH B O   1 
HETATM 3596 O  O   . HOH K 6 .   ? 2.08122  35.39029 79.23861  1.000 17.79811  ? 425 HOH B O   1 
HETATM 3597 O  O   . HOH K 6 .   ? -5.32055 23.86526 100.91414 1.000 24.24104  ? 426 HOH B O   1 
HETATM 3598 O  O   . HOH K 6 .   ? 9.38485  24.49856 81.10859  1.000 21.55761  ? 427 HOH B O   1 
HETATM 3599 O  O   . HOH K 6 .   ? 2.39872  22.12662 102.86961 1.000 21.37429  ? 428 HOH B O   1 
HETATM 3600 O  O   . HOH K 6 .   ? 10.53133 43.83097 83.15642  1.000 24.65745  ? 429 HOH B O   1 
HETATM 3601 O  O   . HOH K 6 .   ? 8.26335  41.70296 80.95697  1.000 20.20386  ? 430 HOH B O   1 
HETATM 3602 O  O   . HOH K 6 .   ? 18.62335 2.62454  93.04926  1.000 19.09288  ? 431 HOH B O   1 
HETATM 3603 O  O   . HOH K 6 .   ? -1.04192 41.06794 97.39424  1.000 27.94664  ? 432 HOH B O   1 
HETATM 3604 O  O   . HOH K 6 .   ? 14.62368 38.37218 75.10092  1.000 21.71125  ? 433 HOH B O   1 
HETATM 3605 O  O   . HOH K 6 .   ? 32.57580 31.51392 90.60861  1.000 31.10234  ? 434 HOH B O   1 
HETATM 3606 O  O   . HOH K 6 .   ? -0.12347 35.50845 106.24659 1.000 22.69748  ? 435 HOH B O   1 
HETATM 3607 O  O   . HOH K 6 .   ? 10.53265 4.10298  100.41266 1.000 33.22812  ? 436 HOH B O   1 
HETATM 3608 O  O   . HOH K 6 .   ? 26.98075 40.08690 83.63345  1.000 27.18100  ? 437 HOH B O   1 
HETATM 3609 O  O   . HOH K 6 .   ? 14.67193 32.24512 105.19765 1.000 15.59475  ? 438 HOH B O   1 
HETATM 3610 O  O   . HOH K 6 .   ? 12.12345 38.15498 76.55589  1.000 22.84553  ? 439 HOH B O   1 
HETATM 3611 O  O   . HOH K 6 .   ? 30.30839 38.49179 71.72742  1.000 26.34656  ? 440 HOH B O   1 
HETATM 3612 O  O   . HOH K 6 .   ? 12.72703 33.78952 103.83315 1.000 16.46096  ? 441 HOH B O   1 
HETATM 3613 O  O   . HOH K 6 .   ? 32.01604 27.75902 89.78761  1.000 30.84528  ? 442 HOH B O   1 
HETATM 3614 O  O   . HOH K 6 .   ? 21.40910 29.30228 104.23316 1.000 18.32299  ? 443 HOH B O   1 
HETATM 3615 O  O   . HOH K 6 .   ? 27.81027 30.18906 94.45478  1.000 24.51510  ? 444 HOH B O   1 
HETATM 3616 O  O   . HOH K 6 .   ? 12.53092 2.74564  93.68516  1.000 25.05690  ? 445 HOH B O   1 
HETATM 3617 O  O   . HOH K 6 .   ? 11.91906 15.55436 82.11771  1.000 18.85597  ? 446 HOH B O   1 
HETATM 3618 O  O   . HOH K 6 .   ? 18.96215 19.12009 99.46530  1.000 20.05283  ? 447 HOH B O   1 
HETATM 3619 O  O   . HOH K 6 .   ? 11.77632 30.59048 76.34390  1.000 22.49554  ? 448 HOH B O   1 
HETATM 3620 O  O   . HOH K 6 .   ? -8.74414 32.04316 88.51394  1.000 27.49295  ? 449 HOH B O   1 
HETATM 3621 O  O   . HOH K 6 .   ? 0.30233  34.04271 77.86364  1.000 18.25334  ? 450 HOH B O   1 
HETATM 3622 O  O   . HOH K 6 .   ? 7.95852  33.88739 110.70781 1.000 27.78324  ? 451 HOH B O   1 
HETATM 3623 O  O   . HOH K 6 .   ? 12.47462 43.35167 84.95752  1.000 26.37116  ? 452 HOH B O   1 
HETATM 3624 O  O   . HOH K 6 .   ? 15.35179 2.08575  90.72052  1.000 23.64728  ? 453 HOH B O   1 
HETATM 3625 O  O   . HOH K 6 .   ? 16.58797 21.11627 83.89530  1.000 21.11150  ? 454 HOH B O   1 
HETATM 3626 O  O   . HOH K 6 .   ? 22.16500 11.83487 95.56196  1.000 18.64975  ? 455 HOH B O   1 
HETATM 3627 O  O   . HOH K 6 .   ? -1.29560 9.55956  100.92698 1.000 19.13140  ? 456 HOH B O   1 
HETATM 3628 O  O   . HOH K 6 .   ? 11.87157 21.84291 80.62370  1.000 27.76715  ? 457 HOH B O   1 
HETATM 3629 O  O   . HOH K 6 .   ? -5.78166 19.89869 95.98428  1.000 17.56911  ? 458 HOH B O   1 
HETATM 3630 O  O   . HOH K 6 .   ? 12.15622 4.18674  87.61361  1.000 30.97127  ? 459 HOH B O   1 
HETATM 3631 O  O   . HOH K 6 .   ? 42.96429 38.07317 81.94769  1.000 29.05653  ? 460 HOH B O   1 
HETATM 3632 O  O   . HOH K 6 .   ? 19.02021 26.46949 103.51422 1.000 16.86448  ? 461 HOH B O   1 
HETATM 3633 O  O   . HOH K 6 .   ? 5.37656  38.54529 96.91017  1.000 16.64347  ? 462 HOH B O   1 
HETATM 3634 O  O   . HOH K 6 .   ? 17.29830 22.13364 86.33572  1.000 15.16272  ? 463 HOH B O   1 
HETATM 3635 O  O   . HOH K 6 .   ? 16.17442 15.72456 100.84794 1.000 23.63138  ? 464 HOH B O   1 
HETATM 3636 O  O   . HOH K 6 .   ? 33.61737 34.08976 90.60067  1.000 21.92358  ? 465 HOH B O   1 
HETATM 3637 O  O   . HOH K 6 .   ? 3.58589  35.02893 112.02879 1.000 25.29705  ? 466 HOH B O   1 
HETATM 3638 O  O   . HOH K 6 .   ? 0.57226  43.27959 100.16412 1.000 24.18923  ? 467 HOH B O   1 
HETATM 3639 O  O   . HOH K 6 .   ? 14.06923 25.42700 82.07445  1.000 18.01540  ? 468 HOH B O   1 
HETATM 3640 O  O   . HOH K 6 .   ? -2.94248 18.51611 86.33252  1.000 30.10237  ? 469 HOH B O   1 
HETATM 3641 O  O   . HOH K 6 .   ? 6.10826  31.60436 74.71470  1.000 20.48258  ? 470 HOH B O   1 
HETATM 3642 O  O   . HOH K 6 .   ? 18.65066 20.40076 80.53718  1.000 35.83089  ? 471 HOH B O   1 
HETATM 3643 O  O   . HOH K 6 .   ? 9.75995  34.24286 107.32297 1.000 24.60684  ? 472 HOH B O   1 
HETATM 3644 O  O   . HOH K 6 .   ? -3.64631 40.30928 93.42869  1.000 20.37691  ? 473 HOH B O   1 
HETATM 3645 O  O   . HOH K 6 .   ? 23.13323 9.25339  92.45171  1.000 26.54892  ? 474 HOH B O   1 
HETATM 3646 O  O   . HOH K 6 .   ? -6.93201 13.84479 93.25058  1.000 29.62148  ? 475 HOH B O   1 
HETATM 3647 O  O   . HOH K 6 .   ? 2.61386  20.11529 80.36346  1.000 25.26168  ? 476 HOH B O   1 
HETATM 3648 O  O   . HOH K 6 .   ? -7.34231 25.69675 91.35636  1.000 20.65154  ? 477 HOH B O   1 
HETATM 3649 O  O   . HOH K 6 .   ? -2.78364 18.03679 97.89642  1.000 20.79449  ? 478 HOH B O   1 
HETATM 3650 O  O   . HOH K 6 .   ? 19.08396 33.65298 68.61657  1.000 36.19112  ? 479 HOH B O   1 
HETATM 3651 O  O   . HOH K 6 .   ? -4.14622 34.62433 101.25895 1.000 25.05006  ? 480 HOH B O   1 
HETATM 3652 O  O   . HOH K 6 .   ? -0.57168 3.93013  92.77226  1.000 30.32026  ? 481 HOH B O   1 
HETATM 3653 O  O   . HOH K 6 .   ? 42.07679 33.16853 72.22691  1.000 32.03517  ? 482 HOH B O   1 
HETATM 3654 O  O   . HOH K 6 .   ? 6.38321  34.18205 73.51874  1.000 28.09231  ? 483 HOH B O   1 
HETATM 3655 O  O   . HOH K 6 .   ? -4.36948 37.51628 97.93331  1.000 21.07780  ? 484 HOH B O   1 
HETATM 3656 O  O   . HOH K 6 .   ? 11.91469 43.36586 80.38144  1.000 32.48778  ? 485 HOH B O   1 
HETATM 3657 O  O   . HOH K 6 .   ? 44.48359 34.35038 74.53381  1.000 31.30068  ? 486 HOH B O   1 
HETATM 3658 O  O   . HOH K 6 .   ? -3.00199 41.94428 95.81075  1.000 28.12107  ? 487 HOH B O   1 
HETATM 3659 O  O   . HOH K 6 .   ? 2.61094  45.55159 91.77226  1.000 28.29623  ? 488 HOH B O   1 
HETATM 3660 O  O   . HOH K 6 .   ? 1.59317  43.06177 89.81696  1.000 26.06479  ? 489 HOH B O   1 
HETATM 3661 O  O   . HOH K 6 .   ? 10.07644 28.89972 106.19630 1.000 28.40748  ? 490 HOH B O   1 
HETATM 3662 O  O   . HOH K 6 .   ? 12.58131 39.42156 79.12731  1.000 19.90100  ? 491 HOH B O   1 
HETATM 3663 O  O   . HOH K 6 .   ? 15.33332 36.22135 92.23647  1.000 26.63253  ? 492 HOH B O   1 
HETATM 3664 O  O   . HOH K 6 .   ? 7.17915  2.30692  100.17374 1.000 32.47769  ? 493 HOH B O   1 
HETATM 3665 O  O   . HOH K 6 .   ? -3.97578 22.68881 82.16992  1.000 34.57537  ? 494 HOH B O   1 
HETATM 3666 O  O   . HOH K 6 .   ? -1.84768 16.15209 103.17886 1.000 31.88608  ? 495 HOH B O   1 
HETATM 3667 O  O   . HOH K 6 .   ? -3.43932 18.03110 88.56825  1.000 33.14799  ? 496 HOH B O   1 
HETATM 3668 O  O   . HOH K 6 .   ? -9.612   26.861   84.389    1.000 29.12819  ? 497 HOH B O   1 
HETATM 3669 O  O   . HOH K 6 .   ? 17.58695 27.95854 79.07162  1.000 31.78722  ? 498 HOH B O   1 
HETATM 3670 O  O   . HOH K 6 .   ? -3.54052 5.61512  89.72357  1.000 34.53990  ? 499 HOH B O   1 
HETATM 3671 O  O   . HOH K 6 .   ? -3.27676 32.16296 104.78295 1.000 31.57725  ? 500 HOH B O   1 
HETATM 3672 O  O   . HOH K 6 .   ? 25.96079 17.24441 89.69094  1.000 26.40136  ? 501 HOH B O   1 
HETATM 3673 O  O   . HOH K 6 .   ? 13.78130 41.38115 89.91003  1.000 26.04452  ? 502 HOH B O   1 
HETATM 3674 O  O   . HOH K 6 .   ? 34.07799 39.77406 83.62607  1.000 26.00386  ? 503 HOH B O   1 
HETATM 3675 O  O   . HOH K 6 .   ? 23.742   4.214    90.534    1.000 33.57897  ? 504 HOH B O   1 
HETATM 3676 O  O   . HOH K 6 .   ? 1.95569  23.78991 81.41436  1.000 30.41709  ? 505 HOH B O   1 
HETATM 3677 O  O   . HOH K 6 .   ? 27.01153 17.25263 92.50987  1.000 29.97216  ? 506 HOH B O   1 
HETATM 3678 O  O   . HOH K 6 .   ? 21.91655 9.14026  95.44497  1.000 18.86742  ? 507 HOH B O   1 
HETATM 3679 O  O   . HOH K 6 .   ? 36.37338 39.77760 77.66093  1.000 29.74283  ? 508 HOH B O   1 
HETATM 3680 O  O   . HOH K 6 .   ? 2.11587  18.30512 103.96950 1.000 27.80806  ? 509 HOH B O   1 
HETATM 3681 O  O   . HOH K 6 .   ? -3.33471 27.74823 105.80031 1.000 26.42488  ? 510 HOH B O   1 
HETATM 3682 O  O   . HOH K 6 .   ? -2.41692 13.98954 86.40411  1.000 31.43524  ? 511 HOH B O   1 
HETATM 3683 O  O   . HOH K 6 .   ? 19.02607 24.86282 100.00943 1.000 21.49174  ? 512 HOH B O   1 
HETATM 3684 O  O   . HOH K 6 .   ? 25.99740 33.01216 97.07658  1.000 30.40658  ? 513 HOH B O   1 
HETATM 3685 O  O   . HOH K 6 .   ? 44.50233 36.03811 79.69644  1.000 21.96850  ? 514 HOH B O   1 
HETATM 3686 O  O   . HOH K 6 .   ? 4.22446  1.37972  97.24010  1.000 28.32409  ? 515 HOH B O   1 
HETATM 3687 O  O   . HOH K 6 .   ? 11.65254 15.92052 105.91488 1.000 31.05467  ? 516 HOH B O   1 
HETATM 3688 O  O   . HOH K 6 .   ? -1.63453 8.20528  103.30922 1.000 31.52920  ? 517 HOH B O   1 
HETATM 3689 O  O   . HOH K 6 .   ? 3.72043  44.17969 88.25220  1.000 24.42755  ? 518 HOH B O   1 
HETATM 3690 O  O   . HOH K 6 .   ? -4.36066 20.30142 98.37982  1.000 21.24756  ? 519 HOH B O   1 
HETATM 3691 O  O   . HOH K 6 .   ? 14.32690 18.47588 104.55077 1.000 23.69420  ? 520 HOH B O   1 
HETATM 3692 O  O   . HOH K 6 .   ? -6.36463 33.00400 100.36121 1.000 26.31671  ? 521 HOH B O   1 
HETATM 3693 O  O   . HOH K 6 .   ? -4.60248 26.68829 101.59160 1.000 17.81899  ? 522 HOH B O   1 
HETATM 3694 O  O   . HOH K 6 .   ? 19.686   23.939   107.522   1.000 27.70211  ? 523 HOH B O   1 
HETATM 3695 O  O   . HOH K 6 .   ? -4.90001 16.45398 97.44574  1.000 29.15533  ? 524 HOH B O   1 
HETATM 3696 O  O   . HOH K 6 .   ? 7.33181  21.33141 107.25010 1.000 31.10137  ? 525 HOH B O   1 
HETATM 3697 O  O   . HOH K 6 .   ? 23.81510 32.86705 93.38639  1.000 19.79673  ? 526 HOH B O   1 
HETATM 3698 O  O   . HOH K 6 .   ? 18.10072 24.03134 102.49213 1.000 17.67549  ? 527 HOH B O   1 
HETATM 3699 O  O   . HOH K 6 .   ? 21.321   37.770   72.976    1.000 30.39885  ? 528 HOH B O   1 
HETATM 3700 O  O   . HOH K 6 .   ? 31.97936 40.46263 85.29603  1.000 29.00624  ? 529 HOH B O   1 
HETATM 3701 O  O   . HOH K 6 .   ? 20.10948 27.38182 101.08761 1.000 20.77179  ? 530 HOH B O   1 
HETATM 3702 O  O   . HOH K 6 .   ? 20.76200 20.86450 100.67473 1.000 23.94026  ? 531 HOH B O   1 
HETATM 3703 O  O   . HOH K 6 .   ? 19.295   23.942   109.772   1.000 27.41481  ? 532 HOH B O   1 
HETATM 3704 O  O   . HOH K 6 .   ? 0.27401  20.42234 103.35063 1.000 27.39539  ? 533 HOH B O   1 
HETATM 3705 O  O   . HOH K 6 .   ? 2.35638  11.77922 80.34017  1.000 33.12302  ? 534 HOH B O   1 
HETATM 3706 O  O   . HOH K 6 .   ? 45.89878 36.26453 85.21740  1.000 24.77657  ? 535 HOH B O   1 
HETATM 3707 O  O   . HOH K 6 .   ? 14.32513 19.38948 82.53453  1.000 30.12659  ? 536 HOH B O   1 
HETATM 3708 O  O   . HOH K 6 .   ? -5.61842 39.75176 97.19748  1.000 34.60346  ? 537 HOH B O   1 
HETATM 3709 O  O   . HOH K 6 .   ? 2.55239  29.21029 76.03741  1.000 25.82684  ? 538 HOH B O   1 
HETATM 3710 O  O   . HOH K 6 .   ? 28.04668 32.26345 92.55227  1.000 26.27622  ? 539 HOH B O   1 
HETATM 3711 O  O   . HOH K 6 .   ? -7.09054 17.39534 97.24084  1.000 34.41056  ? 540 HOH B O   1 
HETATM 3712 O  O   . HOH K 6 .   ? 14.04222 14.63817 80.84115  1.000 33.21579  ? 541 HOH B O   1 
HETATM 3713 O  O   . HOH K 6 .   ? -0.65044 5.17118  99.77418  1.000 24.21502  ? 542 HOH B O   1 
HETATM 3714 O  O   . HOH K 6 .   ? 24.193   29.190   99.532    1.000 28.03090  ? 543 HOH B O   1 
HETATM 3715 O  O   . HOH K 6 .   ? -6.556   26.145   103.360   1.000 32.33395  ? 544 HOH B O   1 
HETATM 3716 O  O   . HOH K 6 .   ? 24.47671 42.22308 75.28108  1.000 29.38240  ? 545 HOH B O   1 
HETATM 3717 O  O   . HOH K 6 .   ? 3.67571  32.30129 111.76931 1.000 30.18177  ? 546 HOH B O   1 
HETATM 3718 O  O   . HOH K 6 .   ? 15.24659 26.78984 80.15917  1.000 24.35553  ? 547 HOH B O   1 
HETATM 3719 O  O   . HOH K 6 .   ? 9.66613  37.44725 73.21397  1.000 30.88331  ? 548 HOH B O   1 
HETATM 3720 O  O   . HOH K 6 .   ? 17.34182 18.13192 101.46404 1.000 25.40620  ? 549 HOH B O   1 
HETATM 3721 O  O   . HOH K 6 .   ? 11.98865 24.58611 80.60908  1.000 22.97784  ? 550 HOH B O   1 
HETATM 3722 O  O   . HOH K 6 .   ? 4.67916  26.87664 78.77734  1.000 29.12818  ? 551 HOH B O   1 
HETATM 3723 O  O   . HOH K 6 .   ? -5.99432 9.94805  101.02974 1.000 33.71499  ? 552 HOH B O   1 
HETATM 3724 O  O   . HOH K 6 .   ? 26.56726 23.57506 93.62770  1.000 33.03023  ? 553 HOH B O   1 
HETATM 3725 O  O   . HOH K 6 .   ? 28.81401 39.85065 85.80226  1.000 23.49543  ? 554 HOH B O   1 
HETATM 3726 O  O   . HOH K 6 .   ? -5.04521 37.43509 100.57936 1.000 29.70829  ? 555 HOH B O   1 
HETATM 3727 O  O   . HOH K 6 .   ? 24.253   6.456    91.277    1.000 32.81065  ? 556 HOH B O   1 
HETATM 3728 O  O   . HOH K 6 .   ? -4.36109 30.38279 103.04681 1.000 22.08850  ? 557 HOH B O   1 
HETATM 3729 O  O   . HOH K 6 .   ? 46.03973 36.05314 76.58408  1.000 24.70706  ? 558 HOH B O   1 
HETATM 3730 O  O   . HOH K 6 .   ? 3.51486  18.86721 106.04385 1.000 28.34989  ? 559 HOH B O   1 
HETATM 3731 O  O   . HOH K 6 .   ? 9.12972  27.58631 78.62161  1.000 24.75628  ? 560 HOH B O   1 
HETATM 3732 O  O   . HOH K 6 .   ? -5.96999 28.51264 81.63495  1.000 31.92094  ? 561 HOH B O   1 
HETATM 3733 O  O   . HOH K 6 .   ? 16.15727 19.86668 103.17274 1.000 22.87423  ? 562 HOH B O   1 
HETATM 3734 O  O   . HOH K 6 .   ? 7.198    38.959   76.994    1.000 32.79360  ? 563 HOH B O   1 
HETATM 3735 O  O   . HOH K 6 .   ? 24.94253 24.53931 97.34396  1.000 31.04930  ? 564 HOH B O   1 
HETATM 3736 O  O   . HOH K 6 .   ? 9.79943  39.02617 75.43483  1.000 28.99336  ? 565 HOH B O   1 
HETATM 3737 O  O   . HOH K 6 .   ? 24.05244 12.28644 93.41398  1.000 28.37887  ? 566 HOH B O   1 
HETATM 3738 O  O   . HOH K 6 .   ? 4.00581  11.76691 78.70861  1.000 29.24391  ? 567 HOH B O   1 
HETATM 3739 O  O   . HOH K 6 .   ? -4.72172 7.62044  99.53989  1.000 32.72419  ? 568 HOH B O   1 
HETATM 3740 O  O   . HOH K 6 .   ? 17.31832 39.93139 89.38877  1.000 27.91532  ? 569 HOH B O   1 
HETATM 3741 O  O   . HOH K 6 .   ? 10.72724 16.83960 79.93145  1.000 27.74718  ? 570 HOH B O   1 
HETATM 3742 O  O   . HOH K 6 .   ? 12.897   12.677   100.787   1.000 25.87905  ? 571 HOH B O   1 
HETATM 3743 O  O   . HOH K 6 .   ? 14.41705 21.31437 80.45979  1.000 32.91525  ? 572 HOH B O   1 
HETATM 3744 O  O   . HOH K 6 .   ? 13.90029 14.88394 102.23502 1.000 26.39547  ? 573 HOH B O   1 
HETATM 3745 O  O   . HOH K 6 .   ? 17.25892 42.76584 89.38490  1.000 30.14133  ? 574 HOH B O   1 
HETATM 3746 O  O   . HOH K 6 .   ? 20.56393 16.98820 98.57433  1.000 20.20682  ? 575 HOH B O   1 
HETATM 3747 O  O   . HOH K 6 .   ? 8.12955  29.76371 74.52508  1.000 31.94645  ? 576 HOH B O   1 
HETATM 3748 O  O   . HOH K 6 .   ? 3.22587  28.63566 110.43965 1.000 33.44888  ? 577 HOH B O   1 
HETATM 3749 O  O   . HOH K 6 .   ? 23.88784 16.44674 95.33473  1.000 21.91818  ? 578 HOH B O   1 
HETATM 3750 O  O   . HOH K 6 .   ? -7.10482 22.42577 102.02913 1.000 31.86362  ? 579 HOH B O   1 
HETATM 3751 O  O   . HOH K 6 .   ? 10.40394 41.17706 79.09862  1.000 23.45137  ? 580 HOH B O   1 
HETATM 3752 O  O   . HOH K 6 .   ? 7.22171  28.13290 76.41249  1.000 34.19472  ? 581 HOH B O   1 
HETATM 3753 O  O   . HOH K 6 .   ? 16.64361 39.47070 92.15797  1.000 32.97348  ? 582 HOH B O   1 
HETATM 3754 O  O   . HOH K 6 .   ? 33.75676 40.67915 81.18742  1.000 27.86395  ? 583 HOH B O   1 
HETATM 3755 O  O   . HOH K 6 .   ? 4.52716  23.28923 107.04550 1.000 34.68174  ? 584 HOH B O   1 
HETATM 3756 O  O   . HOH K 6 .   ? 22.17520 18.12239 96.79182  1.000 27.26965  ? 585 HOH B O   1 
HETATM 3757 O  O   . HOH K 6 .   ? 22.73943 26.61067 101.08159 1.000 30.56136  ? 586 HOH B O   1 
HETATM 3758 O  O   . HOH K 6 .   ? 1.33051  9.32837  81.15152  1.000 27.02874  ? 587 HOH B O   1 
HETATM 3759 O  O   . HOH K 6 .   ? 20.08904 22.15883 102.99805 1.000 26.88396  ? 588 HOH B O   1 
HETATM 3760 O  O   . HOH K 6 .   ? 24.35876 18.63253 98.46412  1.000 29.70767  ? 589 HOH B O   1 
# 
