data_8XZZ
# 
_entry.id   8XZZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8XZZ         pdb_00008xzz 10.2210/pdb8xzz/pdb 
WWPDB D_1300044474 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_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                        8XZZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              guoreyting@hubu.edu.cn 
_pdbx_contact_author.name_first         Rey-Ting 
_pdbx_contact_author.name_last          Guo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2942-7246 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xiang, W.L.'  1 ? 
'Huang, J.-W.' 2 ? 
'Yang, Y.'     3 ? 
'Chen, C.-C.'  4 ? 
'Guo, R.-T.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J.Agric.Food Chem.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5118 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            72 
_citation.language                  ? 
_citation.page_first                18201 
_citation.page_last                 18213 
_citation.title                     
'Unleashing the Power of Evolution in Xylanase Engineering: Investigating the Role of Distal Mutation Regulation.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jafc.4c03245 
_citation.pdbx_database_id_PubMed   39082219 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, Y.'      1  ?                   
primary 'Yang, Y.'    2  ?                   
primary 'Lu, G.'      3  ?                   
primary 'Xiang, W.L.' 4  ?                   
primary 'Sun, T.Y.'   5  0000-0002-7746-479X 
primary 'Chen, K.W.'  6  ?                   
primary 'Lv, X.'      7  ?                   
primary 'Gui, Y.F.'   8  ?                   
primary 'Zeng, R.Q.'  9  ?                   
primary 'Du, Y.K.'    10 ?                   
primary 'Fu, C.H.'    11 ?                   
primary 'Huang, J.W.' 12 ?                   
primary 'Chen, C.C.'  13 ?                   
primary 'Guo, R.T.'   14 0000-0003-2942-7246 
primary 'Yu, L.J.'    15 0000-0003-2517-2266 
# 
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 Endo-1,4-beta-xylanase                          21502.773 4   3.2.1.8 E176A,D31P,A34Q,K118Q,A168H ? ? 
2 branched    syn 'beta-D-xylopyranose-(1-4)-beta-D-xylopyranose' 282.245   1   ?       ?                           ? ? 
3 non-polymer syn 'ZINC ION'                                      65.409    6   ?       ?                           ? ? 
4 non-polymer nat beta-D-xylopyranose                             150.130   6   ?       ?                           ? ? 
5 water       nat water                                           18.015    740 ?       ?                           ? ? 
# 
_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       
;GAGAGAGAGAGMEITSSETGTNNGYYYSFWTDGGGQVTYTNGPAGQYSVEWSNSGNFVAGKGWNPGSSQTITYSGEWNPN
GNSYLSVYGWTQNPLVEYYIVESFSTYDPSTGAQELGTVETDDGTYKIYQTTRENAPSIEGTATFNQYWSVRTDHRVGGT
VTTQNHFDAWKNAGLEMGTHNYMIVATAGYQSSGSASITVQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAGAGAGAGAGMEITSSETGTNNGYYYSFWTDGGGQVTYTNGPAGQYSVEWSNSGNFVAGKGWNPGSSQTITYSGEWNPN
GNSYLSVYGWTQNPLVEYYIVESFSTYDPSTGAQELGTVETDDGTYKIYQTTRENAPSIEGTATFNQYWSVRTDHRVGGT
VTTQNHFDAWKNAGLEMGTHNYMIVATAGYQSSGSASITVQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'ZINC ION'          ZN  
4 beta-D-xylopyranose XYP 
5 water               HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   GLY n 
1 4   ALA n 
1 5   GLY n 
1 6   ALA n 
1 7   GLY n 
1 8   ALA n 
1 9   GLY n 
1 10  ALA n 
1 11  GLY n 
1 12  MET n 
1 13  GLU n 
1 14  ILE n 
1 15  THR n 
1 16  SER n 
1 17  SER n 
1 18  GLU n 
1 19  THR n 
1 20  GLY n 
1 21  THR n 
1 22  ASN n 
1 23  ASN n 
1 24  GLY n 
1 25  TYR n 
1 26  TYR n 
1 27  TYR n 
1 28  SER n 
1 29  PHE n 
1 30  TRP n 
1 31  THR n 
1 32  ASP n 
1 33  GLY n 
1 34  GLY n 
1 35  GLY n 
1 36  GLN n 
1 37  VAL n 
1 38  THR n 
1 39  TYR n 
1 40  THR n 
1 41  ASN n 
1 42  GLY n 
1 43  PRO n 
1 44  ALA n 
1 45  GLY n 
1 46  GLN n 
1 47  TYR n 
1 48  SER n 
1 49  VAL n 
1 50  GLU n 
1 51  TRP n 
1 52  SER n 
1 53  ASN n 
1 54  SER n 
1 55  GLY n 
1 56  ASN n 
1 57  PHE n 
1 58  VAL n 
1 59  ALA n 
1 60  GLY n 
1 61  LYS n 
1 62  GLY n 
1 63  TRP n 
1 64  ASN n 
1 65  PRO n 
1 66  GLY n 
1 67  SER n 
1 68  SER n 
1 69  GLN n 
1 70  THR n 
1 71  ILE n 
1 72  THR n 
1 73  TYR n 
1 74  SER n 
1 75  GLY n 
1 76  GLU n 
1 77  TRP n 
1 78  ASN n 
1 79  PRO n 
1 80  ASN n 
1 81  GLY n 
1 82  ASN n 
1 83  SER n 
1 84  TYR n 
1 85  LEU n 
1 86  SER n 
1 87  VAL n 
1 88  TYR n 
1 89  GLY n 
1 90  TRP n 
1 91  THR n 
1 92  GLN n 
1 93  ASN n 
1 94  PRO n 
1 95  LEU n 
1 96  VAL n 
1 97  GLU n 
1 98  TYR n 
1 99  TYR n 
1 100 ILE n 
1 101 VAL n 
1 102 GLU n 
1 103 SER n 
1 104 PHE n 
1 105 SER n 
1 106 THR n 
1 107 TYR n 
1 108 ASP n 
1 109 PRO n 
1 110 SER n 
1 111 THR n 
1 112 GLY n 
1 113 ALA n 
1 114 GLN n 
1 115 GLU n 
1 116 LEU n 
1 117 GLY n 
1 118 THR n 
1 119 VAL n 
1 120 GLU n 
1 121 THR n 
1 122 ASP n 
1 123 ASP n 
1 124 GLY n 
1 125 THR n 
1 126 TYR n 
1 127 LYS n 
1 128 ILE n 
1 129 TYR n 
1 130 GLN n 
1 131 THR n 
1 132 THR n 
1 133 ARG n 
1 134 GLU n 
1 135 ASN n 
1 136 ALA n 
1 137 PRO n 
1 138 SER n 
1 139 ILE n 
1 140 GLU n 
1 141 GLY n 
1 142 THR n 
1 143 ALA n 
1 144 THR n 
1 145 PHE n 
1 146 ASN n 
1 147 GLN n 
1 148 TYR n 
1 149 TRP n 
1 150 SER n 
1 151 VAL n 
1 152 ARG n 
1 153 THR n 
1 154 ASP n 
1 155 HIS n 
1 156 ARG n 
1 157 VAL n 
1 158 GLY n 
1 159 GLY n 
1 160 THR n 
1 161 VAL n 
1 162 THR n 
1 163 THR n 
1 164 GLN n 
1 165 ASN n 
1 166 HIS n 
1 167 PHE n 
1 168 ASP n 
1 169 ALA n 
1 170 TRP n 
1 171 LYS n 
1 172 ASN n 
1 173 ALA n 
1 174 GLY n 
1 175 LEU n 
1 176 GLU n 
1 177 MET n 
1 178 GLY n 
1 179 THR n 
1 180 HIS n 
1 181 ASN n 
1 182 TYR n 
1 183 MET n 
1 184 ILE n 
1 185 VAL n 
1 186 ALA n 
1 187 THR n 
1 188 ALA n 
1 189 GLY n 
1 190 TYR n 
1 191 GLN n 
1 192 SER n 
1 193 SER n 
1 194 GLY n 
1 195 SER n 
1 196 ALA n 
1 197 SER n 
1 198 ILE n 
1 199 THR n 
1 200 VAL n 
1 201 GLN 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                   201 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ATEG_04943 
_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      'Aspergillus terreus NIH2624' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     341663 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DXylpb1-4DXylpb1-ROH                       'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a212h-1b_1-5]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][b-D-Xylp]{[(4+1)][b-D-Xylp]{}}'        LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  XYP 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  XYP 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE             ?                                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE            ?                                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE          ?                                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'     ?                                 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking'          y GLUTAMINE           ?                                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'     ?                                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE             ?                                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE           ?                                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER               ?                                 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE          ?                                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE             ?                                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE              ?                                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE          ?                                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'          y PHENYLALANINE       ?                                 'C9 H11 N O2'    165.189 
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 
XYP 'D-saccharide, beta linking' . beta-D-xylopyranose 'beta-D-xylose; D-xylose; xylose' 'C5 H10 O5'      150.130 
ZN  non-polymer                  . 'ZINC ION'          ?                                 'Zn 2'           65.409  
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
XYP 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DXylpb           
XYP 'COMMON NAME'                         GMML     1.0 b-D-xylopyranose 
XYP 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Xylp         
XYP 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Xyl              
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -11 ?   ?   ?   A . n 
A 1 2   ALA 2   -10 ?   ?   ?   A . n 
A 1 3   GLY 3   -9  ?   ?   ?   A . n 
A 1 4   ALA 4   -8  ?   ?   ?   A . n 
A 1 5   GLY 5   -7  ?   ?   ?   A . n 
A 1 6   ALA 6   -6  -6  ALA ALA A . n 
A 1 7   GLY 7   -5  -5  GLY GLY A . n 
A 1 8   ALA 8   -4  -4  ALA ALA A . n 
A 1 9   GLY 9   -3  -3  GLY GLY A . n 
A 1 10  ALA 10  -2  -2  ALA ALA A . n 
A 1 11  GLY 11  -1  -1  GLY GLY A . n 
A 1 12  MET 12  0   0   MET MET A . n 
A 1 13  GLU 13  1   1   GLU GLU A . n 
A 1 14  ILE 14  2   2   ILE ILE A . n 
A 1 15  THR 15  3   3   THR THR A . n 
A 1 16  SER 16  4   4   SER SER A . n 
A 1 17  SER 17  5   5   SER SER A . n 
A 1 18  GLU 18  6   6   GLU GLU A . n 
A 1 19  THR 19  7   7   THR THR A . n 
A 1 20  GLY 20  8   8   GLY GLY A . n 
A 1 21  THR 21  9   9   THR THR A . n 
A 1 22  ASN 22  10  10  ASN ASN A . n 
A 1 23  ASN 23  11  11  ASN ASN A . n 
A 1 24  GLY 24  12  12  GLY GLY A . n 
A 1 25  TYR 25  13  13  TYR TYR A . n 
A 1 26  TYR 26  14  14  TYR TYR A . n 
A 1 27  TYR 27  15  15  TYR TYR A . n 
A 1 28  SER 28  16  16  SER SER A . n 
A 1 29  PHE 29  17  17  PHE PHE A . n 
A 1 30  TRP 30  18  18  TRP TRP A . n 
A 1 31  THR 31  19  19  THR THR A . n 
A 1 32  ASP 32  20  20  ASP ASP A . n 
A 1 33  GLY 33  21  21  GLY GLY A . n 
A 1 34  GLY 34  22  22  GLY GLY A . n 
A 1 35  GLY 35  23  23  GLY GLY A . n 
A 1 36  GLN 36  24  24  GLN GLN A . n 
A 1 37  VAL 37  25  25  VAL VAL A . n 
A 1 38  THR 38  26  26  THR THR A . n 
A 1 39  TYR 39  27  27  TYR TYR A . n 
A 1 40  THR 40  28  28  THR THR A . n 
A 1 41  ASN 41  29  29  ASN ASN A . n 
A 1 42  GLY 42  30  30  GLY GLY A . n 
A 1 43  PRO 43  31  31  PRO PRO A . n 
A 1 44  ALA 44  32  32  ALA ALA A . n 
A 1 45  GLY 45  33  33  GLY GLY A . n 
A 1 46  GLN 46  34  34  GLN GLN A . n 
A 1 47  TYR 47  35  35  TYR TYR A . n 
A 1 48  SER 48  36  36  SER SER A . n 
A 1 49  VAL 49  37  37  VAL VAL A . n 
A 1 50  GLU 50  38  38  GLU GLU A . n 
A 1 51  TRP 51  39  39  TRP TRP A . n 
A 1 52  SER 52  40  40  SER SER A . n 
A 1 53  ASN 53  41  41  ASN ASN A . n 
A 1 54  SER 54  42  42  SER SER A . n 
A 1 55  GLY 55  43  43  GLY GLY A . n 
A 1 56  ASN 56  44  44  ASN ASN A . n 
A 1 57  PHE 57  45  45  PHE PHE A . n 
A 1 58  VAL 58  46  46  VAL VAL A . n 
A 1 59  ALA 59  47  47  ALA ALA A . n 
A 1 60  GLY 60  48  48  GLY GLY A . n 
A 1 61  LYS 61  49  49  LYS LYS A . n 
A 1 62  GLY 62  50  50  GLY GLY A . n 
A 1 63  TRP 63  51  51  TRP TRP A . n 
A 1 64  ASN 64  52  52  ASN ASN A . n 
A 1 65  PRO 65  53  53  PRO PRO A . n 
A 1 66  GLY 66  54  54  GLY GLY A . n 
A 1 67  SER 67  55  55  SER SER A . n 
A 1 68  SER 68  56  56  SER SER A . n 
A 1 69  GLN 69  57  57  GLN GLN A . n 
A 1 70  THR 70  58  58  THR THR A . n 
A 1 71  ILE 71  59  59  ILE ILE A . n 
A 1 72  THR 72  60  60  THR THR A . n 
A 1 73  TYR 73  61  61  TYR TYR A . n 
A 1 74  SER 74  62  62  SER SER A . n 
A 1 75  GLY 75  63  63  GLY GLY A . n 
A 1 76  GLU 76  64  64  GLU GLU A . n 
A 1 77  TRP 77  65  65  TRP TRP A . n 
A 1 78  ASN 78  66  66  ASN ASN A . n 
A 1 79  PRO 79  67  67  PRO PRO A . n 
A 1 80  ASN 80  68  68  ASN ASN A . n 
A 1 81  GLY 81  69  69  GLY GLY A . n 
A 1 82  ASN 82  70  70  ASN ASN A . n 
A 1 83  SER 83  71  71  SER SER A . n 
A 1 84  TYR 84  72  72  TYR TYR A . n 
A 1 85  LEU 85  73  73  LEU LEU A . n 
A 1 86  SER 86  74  74  SER SER A . n 
A 1 87  VAL 87  75  75  VAL VAL A . n 
A 1 88  TYR 88  76  76  TYR TYR A . n 
A 1 89  GLY 89  77  77  GLY GLY A . n 
A 1 90  TRP 90  78  78  TRP TRP A . n 
A 1 91  THR 91  79  79  THR THR A . n 
A 1 92  GLN 92  80  80  GLN GLN A . n 
A 1 93  ASN 93  81  81  ASN ASN A . n 
A 1 94  PRO 94  82  82  PRO PRO A . n 
A 1 95  LEU 95  83  83  LEU LEU A . n 
A 1 96  VAL 96  84  84  VAL VAL A . n 
A 1 97  GLU 97  85  85  GLU GLU A . n 
A 1 98  TYR 98  86  86  TYR TYR A . n 
A 1 99  TYR 99  87  87  TYR TYR A . n 
A 1 100 ILE 100 88  88  ILE ILE A . n 
A 1 101 VAL 101 89  89  VAL VAL A . n 
A 1 102 GLU 102 90  90  GLU GLU A . n 
A 1 103 SER 103 91  91  SER SER A . n 
A 1 104 PHE 104 92  92  PHE PHE A . n 
A 1 105 SER 105 93  93  SER SER A . n 
A 1 106 THR 106 94  94  THR THR A . n 
A 1 107 TYR 107 95  95  TYR TYR A . n 
A 1 108 ASP 108 96  96  ASP ASP A . n 
A 1 109 PRO 109 97  97  PRO PRO A . n 
A 1 110 SER 110 98  98  SER SER A . n 
A 1 111 THR 111 99  99  THR THR A . n 
A 1 112 GLY 112 100 100 GLY GLY A . n 
A 1 113 ALA 113 101 101 ALA ALA A . n 
A 1 114 GLN 114 102 102 GLN GLN A . n 
A 1 115 GLU 115 103 103 GLU GLU A . n 
A 1 116 LEU 116 104 104 LEU LEU A . n 
A 1 117 GLY 117 105 105 GLY GLY A . n 
A 1 118 THR 118 106 106 THR THR A . n 
A 1 119 VAL 119 107 107 VAL VAL A . n 
A 1 120 GLU 120 108 108 GLU GLU A . n 
A 1 121 THR 121 109 109 THR THR A . n 
A 1 122 ASP 122 110 110 ASP ASP A . n 
A 1 123 ASP 123 111 111 ASP ASP A . n 
A 1 124 GLY 124 112 112 GLY GLY A . n 
A 1 125 THR 125 113 113 THR THR A . n 
A 1 126 TYR 126 114 114 TYR TYR A . n 
A 1 127 LYS 127 115 115 LYS LYS A . n 
A 1 128 ILE 128 116 116 ILE ILE A . n 
A 1 129 TYR 129 117 117 TYR TYR A . n 
A 1 130 GLN 130 118 118 GLN GLN A . n 
A 1 131 THR 131 119 119 THR THR A . n 
A 1 132 THR 132 120 120 THR THR A . n 
A 1 133 ARG 133 121 121 ARG ARG A . n 
A 1 134 GLU 134 122 122 GLU GLU A . n 
A 1 135 ASN 135 123 123 ASN ASN A . n 
A 1 136 ALA 136 124 124 ALA ALA A . n 
A 1 137 PRO 137 125 125 PRO PRO A . n 
A 1 138 SER 138 126 126 SER SER A . n 
A 1 139 ILE 139 127 127 ILE ILE A . n 
A 1 140 GLU 140 128 128 GLU GLU A . n 
A 1 141 GLY 141 129 129 GLY GLY A . n 
A 1 142 THR 142 130 130 THR THR A . n 
A 1 143 ALA 143 131 131 ALA ALA A . n 
A 1 144 THR 144 132 132 THR THR A . n 
A 1 145 PHE 145 133 133 PHE PHE A . n 
A 1 146 ASN 146 134 134 ASN ASN A . n 
A 1 147 GLN 147 135 135 GLN GLN A . n 
A 1 148 TYR 148 136 136 TYR TYR A . n 
A 1 149 TRP 149 137 137 TRP TRP A . n 
A 1 150 SER 150 138 138 SER SER A . n 
A 1 151 VAL 151 139 139 VAL VAL A . n 
A 1 152 ARG 152 140 140 ARG ARG A . n 
A 1 153 THR 153 141 141 THR THR A . n 
A 1 154 ASP 154 142 142 ASP ASP A . n 
A 1 155 HIS 155 143 143 HIS HIS A . n 
A 1 156 ARG 156 144 144 ARG ARG A . n 
A 1 157 VAL 157 145 145 VAL VAL A . n 
A 1 158 GLY 158 146 146 GLY GLY A . n 
A 1 159 GLY 159 147 147 GLY GLY A . n 
A 1 160 THR 160 148 148 THR THR A . n 
A 1 161 VAL 161 149 149 VAL VAL A . n 
A 1 162 THR 162 150 150 THR THR A . n 
A 1 163 THR 163 151 151 THR THR A . n 
A 1 164 GLN 164 152 152 GLN GLN A . n 
A 1 165 ASN 165 153 153 ASN ASN A . n 
A 1 166 HIS 166 154 154 HIS HIS A . n 
A 1 167 PHE 167 155 155 PHE PHE A . n 
A 1 168 ASP 168 156 156 ASP ASP A . n 
A 1 169 ALA 169 157 157 ALA ALA A . n 
A 1 170 TRP 170 158 158 TRP TRP A . n 
A 1 171 LYS 171 159 159 LYS LYS A . n 
A 1 172 ASN 172 160 160 ASN ASN A . n 
A 1 173 ALA 173 161 161 ALA ALA A . n 
A 1 174 GLY 174 162 162 GLY GLY A . n 
A 1 175 LEU 175 163 163 LEU LEU A . n 
A 1 176 GLU 176 164 164 GLU GLU A . n 
A 1 177 MET 177 165 165 MET MET A . n 
A 1 178 GLY 178 166 166 GLY GLY A . n 
A 1 179 THR 179 167 167 THR THR A . n 
A 1 180 HIS 180 168 168 HIS HIS A . n 
A 1 181 ASN 181 169 169 ASN ASN A . n 
A 1 182 TYR 182 170 170 TYR TYR A . n 
A 1 183 MET 183 171 171 MET MET A . n 
A 1 184 ILE 184 172 172 ILE ILE A . n 
A 1 185 VAL 185 173 173 VAL VAL A . n 
A 1 186 ALA 186 174 174 ALA ALA A . n 
A 1 187 THR 187 175 175 THR THR A . n 
A 1 188 ALA 188 176 176 ALA ALA A . n 
A 1 189 GLY 189 177 177 GLY GLY A . n 
A 1 190 TYR 190 178 178 TYR TYR A . n 
A 1 191 GLN 191 179 179 GLN GLN A . n 
A 1 192 SER 192 180 180 SER SER A . n 
A 1 193 SER 193 181 181 SER SER A . n 
A 1 194 GLY 194 182 182 GLY GLY A . n 
A 1 195 SER 195 183 183 SER SER A . n 
A 1 196 ALA 196 184 184 ALA ALA A . n 
A 1 197 SER 197 185 185 SER SER A . n 
A 1 198 ILE 198 186 186 ILE ILE A . n 
A 1 199 THR 199 187 187 THR THR A . n 
A 1 200 VAL 200 188 188 VAL VAL A . n 
A 1 201 GLN 201 189 189 GLN GLN A . n 
B 1 1   GLY 1   -11 ?   ?   ?   B . n 
B 1 2   ALA 2   -10 ?   ?   ?   B . n 
B 1 3   GLY 3   -9  ?   ?   ?   B . n 
B 1 4   ALA 4   -8  ?   ?   ?   B . n 
B 1 5   GLY 5   -7  ?   ?   ?   B . n 
B 1 6   ALA 6   -6  ?   ?   ?   B . n 
B 1 7   GLY 7   -5  ?   ?   ?   B . n 
B 1 8   ALA 8   -4  ?   ?   ?   B . n 
B 1 9   GLY 9   -3  ?   ?   ?   B . n 
B 1 10  ALA 10  -2  ?   ?   ?   B . n 
B 1 11  GLY 11  -1  ?   ?   ?   B . n 
B 1 12  MET 12  0   0   MET MET B . n 
B 1 13  GLU 13  1   1   GLU GLU B . n 
B 1 14  ILE 14  2   2   ILE ILE B . n 
B 1 15  THR 15  3   3   THR THR B . n 
B 1 16  SER 16  4   4   SER SER B . n 
B 1 17  SER 17  5   5   SER SER B . n 
B 1 18  GLU 18  6   6   GLU GLU B . n 
B 1 19  THR 19  7   7   THR THR B . n 
B 1 20  GLY 20  8   8   GLY GLY B . n 
B 1 21  THR 21  9   9   THR THR B . n 
B 1 22  ASN 22  10  10  ASN ASN B . n 
B 1 23  ASN 23  11  11  ASN ASN B . n 
B 1 24  GLY 24  12  12  GLY GLY B . n 
B 1 25  TYR 25  13  13  TYR TYR B . n 
B 1 26  TYR 26  14  14  TYR TYR B . n 
B 1 27  TYR 27  15  15  TYR TYR B . n 
B 1 28  SER 28  16  16  SER SER B . n 
B 1 29  PHE 29  17  17  PHE PHE B . n 
B 1 30  TRP 30  18  18  TRP TRP B . n 
B 1 31  THR 31  19  19  THR THR B . n 
B 1 32  ASP 32  20  20  ASP ASP B . n 
B 1 33  GLY 33  21  21  GLY GLY B . n 
B 1 34  GLY 34  22  22  GLY GLY B . n 
B 1 35  GLY 35  23  23  GLY GLY B . n 
B 1 36  GLN 36  24  24  GLN GLN B . n 
B 1 37  VAL 37  25  25  VAL VAL B . n 
B 1 38  THR 38  26  26  THR THR B . n 
B 1 39  TYR 39  27  27  TYR TYR B . n 
B 1 40  THR 40  28  28  THR THR B . n 
B 1 41  ASN 41  29  29  ASN ASN B . n 
B 1 42  GLY 42  30  30  GLY GLY B . n 
B 1 43  PRO 43  31  31  PRO PRO B . n 
B 1 44  ALA 44  32  32  ALA ALA B . n 
B 1 45  GLY 45  33  33  GLY GLY B . n 
B 1 46  GLN 46  34  34  GLN GLN B . n 
B 1 47  TYR 47  35  35  TYR TYR B . n 
B 1 48  SER 48  36  36  SER SER B . n 
B 1 49  VAL 49  37  37  VAL VAL B . n 
B 1 50  GLU 50  38  38  GLU GLU B . n 
B 1 51  TRP 51  39  39  TRP TRP B . n 
B 1 52  SER 52  40  40  SER SER B . n 
B 1 53  ASN 53  41  41  ASN ASN B . n 
B 1 54  SER 54  42  42  SER SER B . n 
B 1 55  GLY 55  43  43  GLY GLY B . n 
B 1 56  ASN 56  44  44  ASN ASN B . n 
B 1 57  PHE 57  45  45  PHE PHE B . n 
B 1 58  VAL 58  46  46  VAL VAL B . n 
B 1 59  ALA 59  47  47  ALA ALA B . n 
B 1 60  GLY 60  48  48  GLY GLY B . n 
B 1 61  LYS 61  49  49  LYS LYS B . n 
B 1 62  GLY 62  50  50  GLY GLY B . n 
B 1 63  TRP 63  51  51  TRP TRP B . n 
B 1 64  ASN 64  52  52  ASN ASN B . n 
B 1 65  PRO 65  53  53  PRO PRO B . n 
B 1 66  GLY 66  54  54  GLY GLY B . n 
B 1 67  SER 67  55  55  SER SER B . n 
B 1 68  SER 68  56  56  SER SER B . n 
B 1 69  GLN 69  57  57  GLN GLN B . n 
B 1 70  THR 70  58  58  THR THR B . n 
B 1 71  ILE 71  59  59  ILE ILE B . n 
B 1 72  THR 72  60  60  THR THR B . n 
B 1 73  TYR 73  61  61  TYR TYR B . n 
B 1 74  SER 74  62  62  SER SER B . n 
B 1 75  GLY 75  63  63  GLY GLY B . n 
B 1 76  GLU 76  64  64  GLU GLU B . n 
B 1 77  TRP 77  65  65  TRP TRP B . n 
B 1 78  ASN 78  66  66  ASN ASN B . n 
B 1 79  PRO 79  67  67  PRO PRO B . n 
B 1 80  ASN 80  68  68  ASN ASN B . n 
B 1 81  GLY 81  69  69  GLY GLY B . n 
B 1 82  ASN 82  70  70  ASN ASN B . n 
B 1 83  SER 83  71  71  SER SER B . n 
B 1 84  TYR 84  72  72  TYR TYR B . n 
B 1 85  LEU 85  73  73  LEU LEU B . n 
B 1 86  SER 86  74  74  SER SER B . n 
B 1 87  VAL 87  75  75  VAL VAL B . n 
B 1 88  TYR 88  76  76  TYR TYR B . n 
B 1 89  GLY 89  77  77  GLY GLY B . n 
B 1 90  TRP 90  78  78  TRP TRP B . n 
B 1 91  THR 91  79  79  THR THR B . n 
B 1 92  GLN 92  80  80  GLN GLN B . n 
B 1 93  ASN 93  81  81  ASN ASN B . n 
B 1 94  PRO 94  82  82  PRO PRO B . n 
B 1 95  LEU 95  83  83  LEU LEU B . n 
B 1 96  VAL 96  84  84  VAL VAL B . n 
B 1 97  GLU 97  85  85  GLU GLU B . n 
B 1 98  TYR 98  86  86  TYR TYR B . n 
B 1 99  TYR 99  87  87  TYR TYR B . n 
B 1 100 ILE 100 88  88  ILE ILE B . n 
B 1 101 VAL 101 89  89  VAL VAL B . n 
B 1 102 GLU 102 90  90  GLU GLU B . n 
B 1 103 SER 103 91  91  SER SER B . n 
B 1 104 PHE 104 92  92  PHE PHE B . n 
B 1 105 SER 105 93  93  SER SER B . n 
B 1 106 THR 106 94  94  THR THR B . n 
B 1 107 TYR 107 95  95  TYR TYR B . n 
B 1 108 ASP 108 96  96  ASP ASP B . n 
B 1 109 PRO 109 97  97  PRO PRO B . n 
B 1 110 SER 110 98  98  SER SER B . n 
B 1 111 THR 111 99  99  THR THR B . n 
B 1 112 GLY 112 100 100 GLY GLY B . n 
B 1 113 ALA 113 101 101 ALA ALA B . n 
B 1 114 GLN 114 102 102 GLN GLN B . n 
B 1 115 GLU 115 103 103 GLU GLU B . n 
B 1 116 LEU 116 104 104 LEU LEU B . n 
B 1 117 GLY 117 105 105 GLY GLY B . n 
B 1 118 THR 118 106 106 THR THR B . n 
B 1 119 VAL 119 107 107 VAL VAL B . n 
B 1 120 GLU 120 108 108 GLU GLU B . n 
B 1 121 THR 121 109 109 THR THR B . n 
B 1 122 ASP 122 110 110 ASP ASP B . n 
B 1 123 ASP 123 111 111 ASP ASP B . n 
B 1 124 GLY 124 112 112 GLY GLY B . n 
B 1 125 THR 125 113 113 THR THR B . n 
B 1 126 TYR 126 114 114 TYR TYR B . n 
B 1 127 LYS 127 115 115 LYS LYS B . n 
B 1 128 ILE 128 116 116 ILE ILE B . n 
B 1 129 TYR 129 117 117 TYR TYR B . n 
B 1 130 GLN 130 118 118 GLN GLN B . n 
B 1 131 THR 131 119 119 THR THR B . n 
B 1 132 THR 132 120 120 THR THR B . n 
B 1 133 ARG 133 121 121 ARG ARG B . n 
B 1 134 GLU 134 122 122 GLU GLU B . n 
B 1 135 ASN 135 123 123 ASN ASN B . n 
B 1 136 ALA 136 124 124 ALA ALA B . n 
B 1 137 PRO 137 125 125 PRO PRO B . n 
B 1 138 SER 138 126 126 SER SER B . n 
B 1 139 ILE 139 127 127 ILE ILE B . n 
B 1 140 GLU 140 128 128 GLU GLU B . n 
B 1 141 GLY 141 129 129 GLY GLY B . n 
B 1 142 THR 142 130 130 THR THR B . n 
B 1 143 ALA 143 131 131 ALA ALA B . n 
B 1 144 THR 144 132 132 THR THR B . n 
B 1 145 PHE 145 133 133 PHE PHE B . n 
B 1 146 ASN 146 134 134 ASN ASN B . n 
B 1 147 GLN 147 135 135 GLN GLN B . n 
B 1 148 TYR 148 136 136 TYR TYR B . n 
B 1 149 TRP 149 137 137 TRP TRP B . n 
B 1 150 SER 150 138 138 SER SER B . n 
B 1 151 VAL 151 139 139 VAL VAL B . n 
B 1 152 ARG 152 140 140 ARG ARG B . n 
B 1 153 THR 153 141 141 THR THR B . n 
B 1 154 ASP 154 142 142 ASP ASP B . n 
B 1 155 HIS 155 143 143 HIS HIS B . n 
B 1 156 ARG 156 144 144 ARG ARG B . n 
B 1 157 VAL 157 145 145 VAL VAL B . n 
B 1 158 GLY 158 146 146 GLY GLY B . n 
B 1 159 GLY 159 147 147 GLY GLY B . n 
B 1 160 THR 160 148 148 THR THR B . n 
B 1 161 VAL 161 149 149 VAL VAL B . n 
B 1 162 THR 162 150 150 THR THR B . n 
B 1 163 THR 163 151 151 THR THR B . n 
B 1 164 GLN 164 152 152 GLN GLN B . n 
B 1 165 ASN 165 153 153 ASN ASN B . n 
B 1 166 HIS 166 154 154 HIS HIS B . n 
B 1 167 PHE 167 155 155 PHE PHE B . n 
B 1 168 ASP 168 156 156 ASP ASP B . n 
B 1 169 ALA 169 157 157 ALA ALA B . n 
B 1 170 TRP 170 158 158 TRP TRP B . n 
B 1 171 LYS 171 159 159 LYS LYS B . n 
B 1 172 ASN 172 160 160 ASN ASN B . n 
B 1 173 ALA 173 161 161 ALA ALA B . n 
B 1 174 GLY 174 162 162 GLY GLY B . n 
B 1 175 LEU 175 163 163 LEU LEU B . n 
B 1 176 GLU 176 164 164 GLU GLU B . n 
B 1 177 MET 177 165 165 MET MET B . n 
B 1 178 GLY 178 166 166 GLY GLY B . n 
B 1 179 THR 179 167 167 THR THR B . n 
B 1 180 HIS 180 168 168 HIS HIS B . n 
B 1 181 ASN 181 169 169 ASN ASN B . n 
B 1 182 TYR 182 170 170 TYR TYR B . n 
B 1 183 MET 183 171 171 MET MET B . n 
B 1 184 ILE 184 172 172 ILE ILE B . n 
B 1 185 VAL 185 173 173 VAL VAL B . n 
B 1 186 ALA 186 174 174 ALA ALA B . n 
B 1 187 THR 187 175 175 THR THR B . n 
B 1 188 ALA 188 176 176 ALA ALA B . n 
B 1 189 GLY 189 177 177 GLY GLY B . n 
B 1 190 TYR 190 178 178 TYR TYR B . n 
B 1 191 GLN 191 179 179 GLN GLN B . n 
B 1 192 SER 192 180 180 SER SER B . n 
B 1 193 SER 193 181 181 SER SER B . n 
B 1 194 GLY 194 182 182 GLY GLY B . n 
B 1 195 SER 195 183 183 SER SER B . n 
B 1 196 ALA 196 184 184 ALA ALA B . n 
B 1 197 SER 197 185 185 SER SER B . n 
B 1 198 ILE 198 186 186 ILE ILE B . n 
B 1 199 THR 199 187 187 THR THR B . n 
B 1 200 VAL 200 188 188 VAL VAL B . n 
B 1 201 GLN 201 189 189 GLN GLN B . n 
C 1 1   GLY 1   -11 ?   ?   ?   C . n 
C 1 2   ALA 2   -10 ?   ?   ?   C . n 
C 1 3   GLY 3   -9  ?   ?   ?   C . n 
C 1 4   ALA 4   -8  ?   ?   ?   C . n 
C 1 5   GLY 5   -7  ?   ?   ?   C . n 
C 1 6   ALA 6   -6  ?   ?   ?   C . n 
C 1 7   GLY 7   -5  ?   ?   ?   C . n 
C 1 8   ALA 8   -4  ?   ?   ?   C . n 
C 1 9   GLY 9   -3  ?   ?   ?   C . n 
C 1 10  ALA 10  -2  ?   ?   ?   C . n 
C 1 11  GLY 11  -1  ?   ?   ?   C . n 
C 1 12  MET 12  0   ?   ?   ?   C . n 
C 1 13  GLU 13  1   1   GLU GLU C . n 
C 1 14  ILE 14  2   2   ILE ILE C . n 
C 1 15  THR 15  3   3   THR THR C . n 
C 1 16  SER 16  4   4   SER SER C . n 
C 1 17  SER 17  5   5   SER SER C . n 
C 1 18  GLU 18  6   6   GLU GLU C . n 
C 1 19  THR 19  7   7   THR THR C . n 
C 1 20  GLY 20  8   8   GLY GLY C . n 
C 1 21  THR 21  9   9   THR THR C . n 
C 1 22  ASN 22  10  10  ASN ASN C . n 
C 1 23  ASN 23  11  11  ASN ASN C . n 
C 1 24  GLY 24  12  12  GLY GLY C . n 
C 1 25  TYR 25  13  13  TYR TYR C . n 
C 1 26  TYR 26  14  14  TYR TYR C . n 
C 1 27  TYR 27  15  15  TYR TYR C . n 
C 1 28  SER 28  16  16  SER SER C . n 
C 1 29  PHE 29  17  17  PHE PHE C . n 
C 1 30  TRP 30  18  18  TRP TRP C . n 
C 1 31  THR 31  19  19  THR THR C . n 
C 1 32  ASP 32  20  20  ASP ASP C . n 
C 1 33  GLY 33  21  21  GLY GLY C . n 
C 1 34  GLY 34  22  22  GLY GLY C . n 
C 1 35  GLY 35  23  23  GLY GLY C . n 
C 1 36  GLN 36  24  24  GLN GLN C . n 
C 1 37  VAL 37  25  25  VAL VAL C . n 
C 1 38  THR 38  26  26  THR THR C . n 
C 1 39  TYR 39  27  27  TYR TYR C . n 
C 1 40  THR 40  28  28  THR THR C . n 
C 1 41  ASN 41  29  29  ASN ASN C . n 
C 1 42  GLY 42  30  30  GLY GLY C . n 
C 1 43  PRO 43  31  31  PRO PRO C . n 
C 1 44  ALA 44  32  32  ALA ALA C . n 
C 1 45  GLY 45  33  33  GLY GLY C . n 
C 1 46  GLN 46  34  34  GLN GLN C . n 
C 1 47  TYR 47  35  35  TYR TYR C . n 
C 1 48  SER 48  36  36  SER SER C . n 
C 1 49  VAL 49  37  37  VAL VAL C . n 
C 1 50  GLU 50  38  38  GLU GLU C . n 
C 1 51  TRP 51  39  39  TRP TRP C . n 
C 1 52  SER 52  40  40  SER SER C . n 
C 1 53  ASN 53  41  41  ASN ASN C . n 
C 1 54  SER 54  42  42  SER SER C . n 
C 1 55  GLY 55  43  43  GLY GLY C . n 
C 1 56  ASN 56  44  44  ASN ASN C . n 
C 1 57  PHE 57  45  45  PHE PHE C . n 
C 1 58  VAL 58  46  46  VAL VAL C . n 
C 1 59  ALA 59  47  47  ALA ALA C . n 
C 1 60  GLY 60  48  48  GLY GLY C . n 
C 1 61  LYS 61  49  49  LYS LYS C . n 
C 1 62  GLY 62  50  50  GLY GLY C . n 
C 1 63  TRP 63  51  51  TRP TRP C . n 
C 1 64  ASN 64  52  52  ASN ASN C . n 
C 1 65  PRO 65  53  53  PRO PRO C . n 
C 1 66  GLY 66  54  54  GLY GLY C . n 
C 1 67  SER 67  55  55  SER SER C . n 
C 1 68  SER 68  56  56  SER SER C . n 
C 1 69  GLN 69  57  57  GLN GLN C . n 
C 1 70  THR 70  58  58  THR THR C . n 
C 1 71  ILE 71  59  59  ILE ILE C . n 
C 1 72  THR 72  60  60  THR THR C . n 
C 1 73  TYR 73  61  61  TYR TYR C . n 
C 1 74  SER 74  62  62  SER SER C . n 
C 1 75  GLY 75  63  63  GLY GLY C . n 
C 1 76  GLU 76  64  64  GLU GLU C . n 
C 1 77  TRP 77  65  65  TRP TRP C . n 
C 1 78  ASN 78  66  66  ASN ASN C . n 
C 1 79  PRO 79  67  67  PRO PRO C . n 
C 1 80  ASN 80  68  68  ASN ASN C . n 
C 1 81  GLY 81  69  69  GLY GLY C . n 
C 1 82  ASN 82  70  70  ASN ASN C . n 
C 1 83  SER 83  71  71  SER SER C . n 
C 1 84  TYR 84  72  72  TYR TYR C . n 
C 1 85  LEU 85  73  73  LEU LEU C . n 
C 1 86  SER 86  74  74  SER SER C . n 
C 1 87  VAL 87  75  75  VAL VAL C . n 
C 1 88  TYR 88  76  76  TYR TYR C . n 
C 1 89  GLY 89  77  77  GLY GLY C . n 
C 1 90  TRP 90  78  78  TRP TRP C . n 
C 1 91  THR 91  79  79  THR THR C . n 
C 1 92  GLN 92  80  80  GLN GLN C . n 
C 1 93  ASN 93  81  81  ASN ASN C . n 
C 1 94  PRO 94  82  82  PRO PRO C . n 
C 1 95  LEU 95  83  83  LEU LEU C . n 
C 1 96  VAL 96  84  84  VAL VAL C . n 
C 1 97  GLU 97  85  85  GLU GLU C . n 
C 1 98  TYR 98  86  86  TYR TYR C . n 
C 1 99  TYR 99  87  87  TYR TYR C . n 
C 1 100 ILE 100 88  88  ILE ILE C . n 
C 1 101 VAL 101 89  89  VAL VAL C . n 
C 1 102 GLU 102 90  90  GLU GLU C . n 
C 1 103 SER 103 91  91  SER SER C . n 
C 1 104 PHE 104 92  92  PHE PHE C . n 
C 1 105 SER 105 93  93  SER SER C . n 
C 1 106 THR 106 94  94  THR THR C . n 
C 1 107 TYR 107 95  95  TYR TYR C . n 
C 1 108 ASP 108 96  96  ASP ASP C . n 
C 1 109 PRO 109 97  97  PRO PRO C . n 
C 1 110 SER 110 98  98  SER SER C . n 
C 1 111 THR 111 99  99  THR THR C . n 
C 1 112 GLY 112 100 100 GLY GLY C . n 
C 1 113 ALA 113 101 101 ALA ALA C . n 
C 1 114 GLN 114 102 102 GLN GLN C . n 
C 1 115 GLU 115 103 103 GLU GLU C . n 
C 1 116 LEU 116 104 104 LEU LEU C . n 
C 1 117 GLY 117 105 105 GLY GLY C . n 
C 1 118 THR 118 106 106 THR THR C . n 
C 1 119 VAL 119 107 107 VAL VAL C . n 
C 1 120 GLU 120 108 108 GLU GLU C . n 
C 1 121 THR 121 109 109 THR THR C . n 
C 1 122 ASP 122 110 110 ASP ASP C . n 
C 1 123 ASP 123 111 111 ASP ASP C . n 
C 1 124 GLY 124 112 112 GLY GLY C . n 
C 1 125 THR 125 113 113 THR THR C . n 
C 1 126 TYR 126 114 114 TYR TYR C . n 
C 1 127 LYS 127 115 115 LYS LYS C . n 
C 1 128 ILE 128 116 116 ILE ILE C . n 
C 1 129 TYR 129 117 117 TYR TYR C . n 
C 1 130 GLN 130 118 118 GLN GLN C . n 
C 1 131 THR 131 119 119 THR THR C . n 
C 1 132 THR 132 120 120 THR THR C . n 
C 1 133 ARG 133 121 121 ARG ARG C . n 
C 1 134 GLU 134 122 122 GLU GLU C . n 
C 1 135 ASN 135 123 123 ASN ASN C . n 
C 1 136 ALA 136 124 124 ALA ALA C . n 
C 1 137 PRO 137 125 125 PRO PRO C . n 
C 1 138 SER 138 126 126 SER SER C . n 
C 1 139 ILE 139 127 127 ILE ILE C . n 
C 1 140 GLU 140 128 128 GLU GLU C . n 
C 1 141 GLY 141 129 129 GLY GLY C . n 
C 1 142 THR 142 130 130 THR THR C . n 
C 1 143 ALA 143 131 131 ALA ALA C . n 
C 1 144 THR 144 132 132 THR THR C . n 
C 1 145 PHE 145 133 133 PHE PHE C . n 
C 1 146 ASN 146 134 134 ASN ASN C . n 
C 1 147 GLN 147 135 135 GLN GLN C . n 
C 1 148 TYR 148 136 136 TYR TYR C . n 
C 1 149 TRP 149 137 137 TRP TRP C . n 
C 1 150 SER 150 138 138 SER SER C . n 
C 1 151 VAL 151 139 139 VAL VAL C . n 
C 1 152 ARG 152 140 140 ARG ARG C . n 
C 1 153 THR 153 141 141 THR THR C . n 
C 1 154 ASP 154 142 142 ASP ASP C . n 
C 1 155 HIS 155 143 143 HIS HIS C . n 
C 1 156 ARG 156 144 144 ARG ARG C . n 
C 1 157 VAL 157 145 145 VAL VAL C . n 
C 1 158 GLY 158 146 146 GLY GLY C . n 
C 1 159 GLY 159 147 147 GLY GLY C . n 
C 1 160 THR 160 148 148 THR THR C . n 
C 1 161 VAL 161 149 149 VAL VAL C . n 
C 1 162 THR 162 150 150 THR THR C . n 
C 1 163 THR 163 151 151 THR THR C . n 
C 1 164 GLN 164 152 152 GLN GLN C . n 
C 1 165 ASN 165 153 153 ASN ASN C . n 
C 1 166 HIS 166 154 154 HIS HIS C . n 
C 1 167 PHE 167 155 155 PHE PHE C . n 
C 1 168 ASP 168 156 156 ASP ASP C . n 
C 1 169 ALA 169 157 157 ALA ALA C . n 
C 1 170 TRP 170 158 158 TRP TRP C . n 
C 1 171 LYS 171 159 159 LYS LYS C . n 
C 1 172 ASN 172 160 160 ASN ASN C . n 
C 1 173 ALA 173 161 161 ALA ALA C . n 
C 1 174 GLY 174 162 162 GLY GLY C . n 
C 1 175 LEU 175 163 163 LEU LEU C . n 
C 1 176 GLU 176 164 164 GLU GLU C . n 
C 1 177 MET 177 165 165 MET MET C . n 
C 1 178 GLY 178 166 166 GLY GLY C . n 
C 1 179 THR 179 167 167 THR THR C . n 
C 1 180 HIS 180 168 168 HIS HIS C . n 
C 1 181 ASN 181 169 169 ASN ASN C . n 
C 1 182 TYR 182 170 170 TYR TYR C . n 
C 1 183 MET 183 171 171 MET MET C . n 
C 1 184 ILE 184 172 172 ILE ILE C . n 
C 1 185 VAL 185 173 173 VAL VAL C . n 
C 1 186 ALA 186 174 174 ALA ALA C . n 
C 1 187 THR 187 175 175 THR THR C . n 
C 1 188 ALA 188 176 176 ALA ALA C . n 
C 1 189 GLY 189 177 177 GLY GLY C . n 
C 1 190 TYR 190 178 178 TYR TYR C . n 
C 1 191 GLN 191 179 179 GLN GLN C . n 
C 1 192 SER 192 180 180 SER SER C . n 
C 1 193 SER 193 181 181 SER SER C . n 
C 1 194 GLY 194 182 182 GLY GLY C . n 
C 1 195 SER 195 183 183 SER SER C . n 
C 1 196 ALA 196 184 184 ALA ALA C . n 
C 1 197 SER 197 185 185 SER SER C . n 
C 1 198 ILE 198 186 186 ILE ILE C . n 
C 1 199 THR 199 187 187 THR THR C . n 
C 1 200 VAL 200 188 188 VAL VAL C . n 
C 1 201 GLN 201 189 189 GLN GLN C . n 
D 1 1   GLY 1   -11 ?   ?   ?   D . n 
D 1 2   ALA 2   -10 ?   ?   ?   D . n 
D 1 3   GLY 3   -9  ?   ?   ?   D . n 
D 1 4   ALA 4   -8  ?   ?   ?   D . n 
D 1 5   GLY 5   -7  ?   ?   ?   D . n 
D 1 6   ALA 6   -6  ?   ?   ?   D . n 
D 1 7   GLY 7   -5  ?   ?   ?   D . n 
D 1 8   ALA 8   -4  ?   ?   ?   D . n 
D 1 9   GLY 9   -3  ?   ?   ?   D . n 
D 1 10  ALA 10  -2  ?   ?   ?   D . n 
D 1 11  GLY 11  -1  ?   ?   ?   D . n 
D 1 12  MET 12  0   0   MET MET D . n 
D 1 13  GLU 13  1   1   GLU GLU D . n 
D 1 14  ILE 14  2   2   ILE ILE D . n 
D 1 15  THR 15  3   3   THR THR D . n 
D 1 16  SER 16  4   4   SER SER D . n 
D 1 17  SER 17  5   5   SER SER D . n 
D 1 18  GLU 18  6   6   GLU GLU D . n 
D 1 19  THR 19  7   7   THR THR D . n 
D 1 20  GLY 20  8   8   GLY GLY D . n 
D 1 21  THR 21  9   9   THR THR D . n 
D 1 22  ASN 22  10  10  ASN ASN D . n 
D 1 23  ASN 23  11  11  ASN ASN D . n 
D 1 24  GLY 24  12  12  GLY GLY D . n 
D 1 25  TYR 25  13  13  TYR TYR D . n 
D 1 26  TYR 26  14  14  TYR TYR D . n 
D 1 27  TYR 27  15  15  TYR TYR D . n 
D 1 28  SER 28  16  16  SER SER D . n 
D 1 29  PHE 29  17  17  PHE PHE D . n 
D 1 30  TRP 30  18  18  TRP TRP D . n 
D 1 31  THR 31  19  19  THR THR D . n 
D 1 32  ASP 32  20  20  ASP ASP D . n 
D 1 33  GLY 33  21  21  GLY GLY D . n 
D 1 34  GLY 34  22  22  GLY GLY D . n 
D 1 35  GLY 35  23  23  GLY GLY D . n 
D 1 36  GLN 36  24  24  GLN GLN D . n 
D 1 37  VAL 37  25  25  VAL VAL D . n 
D 1 38  THR 38  26  26  THR THR D . n 
D 1 39  TYR 39  27  27  TYR TYR D . n 
D 1 40  THR 40  28  28  THR THR D . n 
D 1 41  ASN 41  29  29  ASN ASN D . n 
D 1 42  GLY 42  30  30  GLY GLY D . n 
D 1 43  PRO 43  31  31  PRO PRO D . n 
D 1 44  ALA 44  32  32  ALA ALA D . n 
D 1 45  GLY 45  33  33  GLY GLY D . n 
D 1 46  GLN 46  34  34  GLN GLN D . n 
D 1 47  TYR 47  35  35  TYR TYR D . n 
D 1 48  SER 48  36  36  SER SER D . n 
D 1 49  VAL 49  37  37  VAL VAL D . n 
D 1 50  GLU 50  38  38  GLU GLU D . n 
D 1 51  TRP 51  39  39  TRP TRP D . n 
D 1 52  SER 52  40  40  SER SER D . n 
D 1 53  ASN 53  41  41  ASN ASN D . n 
D 1 54  SER 54  42  42  SER SER D . n 
D 1 55  GLY 55  43  43  GLY GLY D . n 
D 1 56  ASN 56  44  44  ASN ASN D . n 
D 1 57  PHE 57  45  45  PHE PHE D . n 
D 1 58  VAL 58  46  46  VAL VAL D . n 
D 1 59  ALA 59  47  47  ALA ALA D . n 
D 1 60  GLY 60  48  48  GLY GLY D . n 
D 1 61  LYS 61  49  49  LYS LYS D . n 
D 1 62  GLY 62  50  50  GLY GLY D . n 
D 1 63  TRP 63  51  51  TRP TRP D . n 
D 1 64  ASN 64  52  52  ASN ASN D . n 
D 1 65  PRO 65  53  53  PRO PRO D . n 
D 1 66  GLY 66  54  54  GLY GLY D . n 
D 1 67  SER 67  55  55  SER SER D . n 
D 1 68  SER 68  56  56  SER SER D . n 
D 1 69  GLN 69  57  57  GLN GLN D . n 
D 1 70  THR 70  58  58  THR THR D . n 
D 1 71  ILE 71  59  59  ILE ILE D . n 
D 1 72  THR 72  60  60  THR THR D . n 
D 1 73  TYR 73  61  61  TYR TYR D . n 
D 1 74  SER 74  62  62  SER SER D . n 
D 1 75  GLY 75  63  63  GLY GLY D . n 
D 1 76  GLU 76  64  64  GLU GLU D . n 
D 1 77  TRP 77  65  65  TRP TRP D . n 
D 1 78  ASN 78  66  66  ASN ASN D . n 
D 1 79  PRO 79  67  67  PRO PRO D . n 
D 1 80  ASN 80  68  68  ASN ASN D . n 
D 1 81  GLY 81  69  69  GLY GLY D . n 
D 1 82  ASN 82  70  70  ASN ASN D . n 
D 1 83  SER 83  71  71  SER SER D . n 
D 1 84  TYR 84  72  72  TYR TYR D . n 
D 1 85  LEU 85  73  73  LEU LEU D . n 
D 1 86  SER 86  74  74  SER SER D . n 
D 1 87  VAL 87  75  75  VAL VAL D . n 
D 1 88  TYR 88  76  76  TYR TYR D . n 
D 1 89  GLY 89  77  77  GLY GLY D . n 
D 1 90  TRP 90  78  78  TRP TRP D . n 
D 1 91  THR 91  79  79  THR THR D . n 
D 1 92  GLN 92  80  80  GLN GLN D . n 
D 1 93  ASN 93  81  81  ASN ASN D . n 
D 1 94  PRO 94  82  82  PRO PRO D . n 
D 1 95  LEU 95  83  83  LEU LEU D . n 
D 1 96  VAL 96  84  84  VAL VAL D . n 
D 1 97  GLU 97  85  85  GLU GLU D . n 
D 1 98  TYR 98  86  86  TYR TYR D . n 
D 1 99  TYR 99  87  87  TYR TYR D . n 
D 1 100 ILE 100 88  88  ILE ILE D . n 
D 1 101 VAL 101 89  89  VAL VAL D . n 
D 1 102 GLU 102 90  90  GLU GLU D . n 
D 1 103 SER 103 91  91  SER SER D . n 
D 1 104 PHE 104 92  92  PHE PHE D . n 
D 1 105 SER 105 93  93  SER SER D . n 
D 1 106 THR 106 94  94  THR THR D . n 
D 1 107 TYR 107 95  95  TYR TYR D . n 
D 1 108 ASP 108 96  96  ASP ASP D . n 
D 1 109 PRO 109 97  97  PRO PRO D . n 
D 1 110 SER 110 98  98  SER SER D . n 
D 1 111 THR 111 99  99  THR THR D . n 
D 1 112 GLY 112 100 100 GLY GLY D . n 
D 1 113 ALA 113 101 101 ALA ALA D . n 
D 1 114 GLN 114 102 102 GLN GLN D . n 
D 1 115 GLU 115 103 103 GLU GLU D . n 
D 1 116 LEU 116 104 104 LEU LEU D . n 
D 1 117 GLY 117 105 105 GLY GLY D . n 
D 1 118 THR 118 106 106 THR THR D . n 
D 1 119 VAL 119 107 107 VAL VAL D . n 
D 1 120 GLU 120 108 108 GLU GLU D . n 
D 1 121 THR 121 109 109 THR THR D . n 
D 1 122 ASP 122 110 110 ASP ASP D . n 
D 1 123 ASP 123 111 111 ASP ASP D . n 
D 1 124 GLY 124 112 112 GLY GLY D . n 
D 1 125 THR 125 113 113 THR THR D . n 
D 1 126 TYR 126 114 114 TYR TYR D . n 
D 1 127 LYS 127 115 115 LYS LYS D . n 
D 1 128 ILE 128 116 116 ILE ILE D . n 
D 1 129 TYR 129 117 117 TYR TYR D . n 
D 1 130 GLN 130 118 118 GLN GLN D . n 
D 1 131 THR 131 119 119 THR THR D . n 
D 1 132 THR 132 120 120 THR THR D . n 
D 1 133 ARG 133 121 121 ARG ARG D . n 
D 1 134 GLU 134 122 122 GLU GLU D . n 
D 1 135 ASN 135 123 123 ASN ASN D . n 
D 1 136 ALA 136 124 124 ALA ALA D . n 
D 1 137 PRO 137 125 125 PRO PRO D . n 
D 1 138 SER 138 126 126 SER SER D . n 
D 1 139 ILE 139 127 127 ILE ILE D . n 
D 1 140 GLU 140 128 128 GLU GLU D . n 
D 1 141 GLY 141 129 129 GLY GLY D . n 
D 1 142 THR 142 130 130 THR THR D . n 
D 1 143 ALA 143 131 131 ALA ALA D . n 
D 1 144 THR 144 132 132 THR THR D . n 
D 1 145 PHE 145 133 133 PHE PHE D . n 
D 1 146 ASN 146 134 134 ASN ASN D . n 
D 1 147 GLN 147 135 135 GLN GLN D . n 
D 1 148 TYR 148 136 136 TYR TYR D . n 
D 1 149 TRP 149 137 137 TRP TRP D . n 
D 1 150 SER 150 138 138 SER SER D . n 
D 1 151 VAL 151 139 139 VAL VAL D . n 
D 1 152 ARG 152 140 140 ARG ARG D . n 
D 1 153 THR 153 141 141 THR THR D . n 
D 1 154 ASP 154 142 142 ASP ASP D . n 
D 1 155 HIS 155 143 143 HIS HIS D . n 
D 1 156 ARG 156 144 144 ARG ARG D . n 
D 1 157 VAL 157 145 145 VAL VAL D . n 
D 1 158 GLY 158 146 146 GLY GLY D . n 
D 1 159 GLY 159 147 147 GLY GLY D . n 
D 1 160 THR 160 148 148 THR THR D . n 
D 1 161 VAL 161 149 149 VAL VAL D . n 
D 1 162 THR 162 150 150 THR THR D . n 
D 1 163 THR 163 151 151 THR THR D . n 
D 1 164 GLN 164 152 152 GLN GLN D . n 
D 1 165 ASN 165 153 153 ASN ASN D . n 
D 1 166 HIS 166 154 154 HIS HIS D . n 
D 1 167 PHE 167 155 155 PHE PHE D . n 
D 1 168 ASP 168 156 156 ASP ASP D . n 
D 1 169 ALA 169 157 157 ALA ALA D . n 
D 1 170 TRP 170 158 158 TRP TRP D . n 
D 1 171 LYS 171 159 159 LYS LYS D . n 
D 1 172 ASN 172 160 160 ASN ASN D . n 
D 1 173 ALA 173 161 161 ALA ALA D . n 
D 1 174 GLY 174 162 162 GLY GLY D . n 
D 1 175 LEU 175 163 163 LEU LEU D . n 
D 1 176 GLU 176 164 164 GLU GLU D . n 
D 1 177 MET 177 165 165 MET MET D . n 
D 1 178 GLY 178 166 166 GLY GLY D . n 
D 1 179 THR 179 167 167 THR THR D . n 
D 1 180 HIS 180 168 168 HIS HIS D . n 
D 1 181 ASN 181 169 169 ASN ASN D . n 
D 1 182 TYR 182 170 170 TYR TYR D . n 
D 1 183 MET 183 171 171 MET MET D . n 
D 1 184 ILE 184 172 172 ILE ILE D . n 
D 1 185 VAL 185 173 173 VAL VAL D . n 
D 1 186 ALA 186 174 174 ALA ALA D . n 
D 1 187 THR 187 175 175 THR THR D . n 
D 1 188 ALA 188 176 176 ALA ALA D . n 
D 1 189 GLY 189 177 177 GLY GLY D . n 
D 1 190 TYR 190 178 178 TYR TYR D . n 
D 1 191 GLN 191 179 179 GLN GLN D . n 
D 1 192 SER 192 180 180 SER SER D . n 
D 1 193 SER 193 181 181 SER SER D . n 
D 1 194 GLY 194 182 182 GLY GLY D . n 
D 1 195 SER 195 183 183 SER SER D . n 
D 1 196 ALA 196 184 184 ALA ALA D . n 
D 1 197 SER 197 185 185 SER SER D . n 
D 1 198 ILE 198 186 186 ILE ILE D . n 
D 1 199 THR 199 187 187 THR THR D . n 
D 1 200 VAL 200 188 188 VAL VAL D . n 
D 1 201 GLN 201 189 189 GLN GLN D . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 2 XYP 1 E XYP 1 E XYP 2 n 
E 2 XYP 2 E XYP 2 E XYP 1 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XYP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XYP 
_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 
F 3 ZN  1   300 300 ZN  ZN  A . 
G 3 ZN  1   301 301 ZN  ZN  A . 
H 3 ZN  1   201 300 ZN  ZN  B . 
I 3 ZN  1   202 301 ZN  ZN  B . 
J 4 XYP 1   203 3   XYP XYP B . 
K 4 XYP 1   204 4   XYP XYP B . 
L 4 XYP 1   201 13  XYP XYP C . 
M 4 XYP 1   202 14  XYP XYP C . 
N 3 ZN  1   201 300 ZN  ZN  D . 
O 3 ZN  1   202 301 ZN  ZN  D . 
P 4 XYP 1   203 15  XYP XYP D . 
Q 4 XYP 1   204 16  XYP XYP D . 
R 5 HOH 1   401 704 HOH HOH A . 
R 5 HOH 2   402 647 HOH HOH A . 
R 5 HOH 3   403 649 HOH HOH A . 
R 5 HOH 4   404 495 HOH HOH A . 
R 5 HOH 5   405 94  HOH HOH A . 
R 5 HOH 6   406 717 HOH HOH A . 
R 5 HOH 7   407 673 HOH HOH A . 
R 5 HOH 8   408 399 HOH HOH A . 
R 5 HOH 9   409 493 HOH HOH A . 
R 5 HOH 10  410 517 HOH HOH A . 
R 5 HOH 11  411 654 HOH HOH A . 
R 5 HOH 12  412 653 HOH HOH A . 
R 5 HOH 13  413 280 HOH HOH A . 
R 5 HOH 14  414 680 HOH HOH A . 
R 5 HOH 15  415 256 HOH HOH A . 
R 5 HOH 16  416 635 HOH HOH A . 
R 5 HOH 17  417 675 HOH HOH A . 
R 5 HOH 18  418 452 HOH HOH A . 
R 5 HOH 19  419 590 HOH HOH A . 
R 5 HOH 20  420 356 HOH HOH A . 
R 5 HOH 21  421 676 HOH HOH A . 
R 5 HOH 22  422 458 HOH HOH A . 
R 5 HOH 23  423 81  HOH HOH A . 
R 5 HOH 24  424 740 HOH HOH A . 
R 5 HOH 25  425 705 HOH HOH A . 
R 5 HOH 26  426 376 HOH HOH A . 
R 5 HOH 27  427 115 HOH HOH A . 
R 5 HOH 28  428 286 HOH HOH A . 
R 5 HOH 29  429 6   HOH HOH A . 
R 5 HOH 30  430 443 HOH HOH A . 
R 5 HOH 31  431 550 HOH HOH A . 
R 5 HOH 32  432 141 HOH HOH A . 
R 5 HOH 33  433 330 HOH HOH A . 
R 5 HOH 34  434 258 HOH HOH A . 
R 5 HOH 35  435 282 HOH HOH A . 
R 5 HOH 36  436 515 HOH HOH A . 
R 5 HOH 37  437 65  HOH HOH A . 
R 5 HOH 38  438 314 HOH HOH A . 
R 5 HOH 39  439 194 HOH HOH A . 
R 5 HOH 40  440 540 HOH HOH A . 
R 5 HOH 41  441 514 HOH HOH A . 
R 5 HOH 42  442 220 HOH HOH A . 
R 5 HOH 43  443 33  HOH HOH A . 
R 5 HOH 44  444 137 HOH HOH A . 
R 5 HOH 45  445 116 HOH HOH A . 
R 5 HOH 46  446 677 HOH HOH A . 
R 5 HOH 47  447 225 HOH HOH A . 
R 5 HOH 48  448 90  HOH HOH A . 
R 5 HOH 49  449 10  HOH HOH A . 
R 5 HOH 50  450 145 HOH HOH A . 
R 5 HOH 51  451 193 HOH HOH A . 
R 5 HOH 52  452 355 HOH HOH A . 
R 5 HOH 53  453 177 HOH HOH A . 
R 5 HOH 54  454 537 HOH HOH A . 
R 5 HOH 55  455 401 HOH HOH A . 
R 5 HOH 56  456 201 HOH HOH A . 
R 5 HOH 57  457 728 HOH HOH A . 
R 5 HOH 58  458 524 HOH HOH A . 
R 5 HOH 59  459 8   HOH HOH A . 
R 5 HOH 60  460 188 HOH HOH A . 
R 5 HOH 61  461 28  HOH HOH A . 
R 5 HOH 62  462 189 HOH HOH A . 
R 5 HOH 63  463 357 HOH HOH A . 
R 5 HOH 64  464 110 HOH HOH A . 
R 5 HOH 65  465 97  HOH HOH A . 
R 5 HOH 66  466 153 HOH HOH A . 
R 5 HOH 67  467 622 HOH HOH A . 
R 5 HOH 68  468 175 HOH HOH A . 
R 5 HOH 69  469 610 HOH HOH A . 
R 5 HOH 70  470 35  HOH HOH A . 
R 5 HOH 71  471 51  HOH HOH A . 
R 5 HOH 72  472 343 HOH HOH A . 
R 5 HOH 73  473 501 HOH HOH A . 
R 5 HOH 74  474 74  HOH HOH A . 
R 5 HOH 75  475 159 HOH HOH A . 
R 5 HOH 76  476 165 HOH HOH A . 
R 5 HOH 77  477 138 HOH HOH A . 
R 5 HOH 78  478 261 HOH HOH A . 
R 5 HOH 79  479 454 HOH HOH A . 
R 5 HOH 80  480 156 HOH HOH A . 
R 5 HOH 81  481 88  HOH HOH A . 
R 5 HOH 82  482 625 HOH HOH A . 
R 5 HOH 83  483 400 HOH HOH A . 
R 5 HOH 84  484 111 HOH HOH A . 
R 5 HOH 85  485 1   HOH HOH A . 
R 5 HOH 86  486 202 HOH HOH A . 
R 5 HOH 87  487 71  HOH HOH A . 
R 5 HOH 88  488 89  HOH HOH A . 
R 5 HOH 89  489 122 HOH HOH A . 
R 5 HOH 90  490 347 HOH HOH A . 
R 5 HOH 91  491 5   HOH HOH A . 
R 5 HOH 92  492 377 HOH HOH A . 
R 5 HOH 93  493 381 HOH HOH A . 
R 5 HOH 94  494 139 HOH HOH A . 
R 5 HOH 95  495 168 HOH HOH A . 
R 5 HOH 96  496 243 HOH HOH A . 
R 5 HOH 97  497 279 HOH HOH A . 
R 5 HOH 98  498 448 HOH HOH A . 
R 5 HOH 99  499 167 HOH HOH A . 
R 5 HOH 100 500 456 HOH HOH A . 
R 5 HOH 101 501 180 HOH HOH A . 
R 5 HOH 102 502 459 HOH HOH A . 
R 5 HOH 103 503 342 HOH HOH A . 
R 5 HOH 104 504 24  HOH HOH A . 
R 5 HOH 105 505 62  HOH HOH A . 
R 5 HOH 106 506 393 HOH HOH A . 
R 5 HOH 107 507 43  HOH HOH A . 
R 5 HOH 108 508 235 HOH HOH A . 
R 5 HOH 109 509 199 HOH HOH A . 
R 5 HOH 110 510 198 HOH HOH A . 
R 5 HOH 111 511 224 HOH HOH A . 
R 5 HOH 112 512 287 HOH HOH A . 
R 5 HOH 113 513 288 HOH HOH A . 
R 5 HOH 114 514 305 HOH HOH A . 
R 5 HOH 115 515 372 HOH HOH A . 
R 5 HOH 116 516 72  HOH HOH A . 
R 5 HOH 117 517 55  HOH HOH A . 
R 5 HOH 118 518 46  HOH HOH A . 
R 5 HOH 119 519 396 HOH HOH A . 
R 5 HOH 120 520 326 HOH HOH A . 
R 5 HOH 121 521 384 HOH HOH A . 
R 5 HOH 122 522 232 HOH HOH A . 
R 5 HOH 123 523 87  HOH HOH A . 
R 5 HOH 124 524 327 HOH HOH A . 
R 5 HOH 125 525 686 HOH HOH A . 
R 5 HOH 126 526 624 HOH HOH A . 
R 5 HOH 127 527 526 HOH HOH A . 
R 5 HOH 128 528 317 HOH HOH A . 
R 5 HOH 129 529 60  HOH HOH A . 
R 5 HOH 130 530 64  HOH HOH A . 
R 5 HOH 131 531 275 HOH HOH A . 
R 5 HOH 132 532 360 HOH HOH A . 
R 5 HOH 133 533 361 HOH HOH A . 
R 5 HOH 134 534 2   HOH HOH A . 
R 5 HOH 135 535 506 HOH HOH A . 
R 5 HOH 136 536 538 HOH HOH A . 
R 5 HOH 137 537 734 HOH HOH A . 
R 5 HOH 138 538 498 HOH HOH A . 
R 5 HOH 139 539 534 HOH HOH A . 
R 5 HOH 140 540 311 HOH HOH A . 
R 5 HOH 141 541 422 HOH HOH A . 
R 5 HOH 142 542 196 HOH HOH A . 
R 5 HOH 143 543 190 HOH HOH A . 
R 5 HOH 144 544 718 HOH HOH A . 
R 5 HOH 145 545 67  HOH HOH A . 
R 5 HOH 146 546 366 HOH HOH A . 
R 5 HOH 147 547 541 HOH HOH A . 
R 5 HOH 148 548 213 HOH HOH A . 
R 5 HOH 149 549 313 HOH HOH A . 
R 5 HOH 150 550 582 HOH HOH A . 
R 5 HOH 151 551 38  HOH HOH A . 
R 5 HOH 152 552 623 HOH HOH A . 
R 5 HOH 153 553 301 HOH HOH A . 
R 5 HOH 154 554 341 HOH HOH A . 
R 5 HOH 155 555 536 HOH HOH A . 
R 5 HOH 156 556 57  HOH HOH A . 
R 5 HOH 157 557 83  HOH HOH A . 
R 5 HOH 158 558 382 HOH HOH A . 
R 5 HOH 159 559 557 HOH HOH A . 
R 5 HOH 160 560 627 HOH HOH A . 
R 5 HOH 161 561 373 HOH HOH A . 
R 5 HOH 162 562 516 HOH HOH A . 
R 5 HOH 163 563 494 HOH HOH A . 
R 5 HOH 164 564 457 HOH HOH A . 
R 5 HOH 165 565 470 HOH HOH A . 
R 5 HOH 166 566 468 HOH HOH A . 
R 5 HOH 167 567 368 HOH HOH A . 
R 5 HOH 168 568 544 HOH HOH A . 
R 5 HOH 169 569 695 HOH HOH A . 
R 5 HOH 170 570 584 HOH HOH A . 
R 5 HOH 171 571 556 HOH HOH A . 
R 5 HOH 172 572 219 HOH HOH A . 
R 5 HOH 173 573 681 HOH HOH A . 
R 5 HOH 174 574 563 HOH HOH A . 
R 5 HOH 175 575 720 HOH HOH A . 
R 5 HOH 176 576 696 HOH HOH A . 
R 5 HOH 177 577 77  HOH HOH A . 
R 5 HOH 178 578 364 HOH HOH A . 
R 5 HOH 179 579 701 HOH HOH A . 
R 5 HOH 180 580 107 HOH HOH A . 
R 5 HOH 181 581 612 HOH HOH A . 
R 5 HOH 182 582 465 HOH HOH A . 
R 5 HOH 183 583 729 HOH HOH A . 
R 5 HOH 184 584 467 HOH HOH A . 
R 5 HOH 185 585 476 HOH HOH A . 
R 5 HOH 186 586 269 HOH HOH A . 
R 5 HOH 187 587 708 HOH HOH A . 
R 5 HOH 188 588 559 HOH HOH A . 
R 5 HOH 189 589 158 HOH HOH A . 
R 5 HOH 190 590 554 HOH HOH A . 
R 5 HOH 191 591 698 HOH HOH A . 
R 5 HOH 192 592 689 HOH HOH A . 
R 5 HOH 193 593 566 HOH HOH A . 
R 5 HOH 194 594 715 HOH HOH A . 
S 5 HOH 1   301 714 HOH HOH B . 
S 5 HOH 2   302 650 HOH HOH B . 
S 5 HOH 3   303 434 HOH HOH B . 
S 5 HOH 4   304 669 HOH HOH B . 
S 5 HOH 5   305 661 HOH HOH B . 
S 5 HOH 6   306 631 HOH HOH B . 
S 5 HOH 7   307 179 HOH HOH B . 
S 5 HOH 8   308 634 HOH HOH B . 
S 5 HOH 9   309 497 HOH HOH B . 
S 5 HOH 10  310 283 HOH HOH B . 
S 5 HOH 11  311 574 HOH HOH B . 
S 5 HOH 12  312 732 HOH HOH B . 
S 5 HOH 13  313 413 HOH HOH B . 
S 5 HOH 14  314 722 HOH HOH B . 
S 5 HOH 15  315 691 HOH HOH B . 
S 5 HOH 16  316 589 HOH HOH B . 
S 5 HOH 17  317 221 HOH HOH B . 
S 5 HOH 18  318 632 HOH HOH B . 
S 5 HOH 19  319 117 HOH HOH B . 
S 5 HOH 20  320 181 HOH HOH B . 
S 5 HOH 21  321 227 HOH HOH B . 
S 5 HOH 22  322 386 HOH HOH B . 
S 5 HOH 23  323 597 HOH HOH B . 
S 5 HOH 24  324 651 HOH HOH B . 
S 5 HOH 25  325 7   HOH HOH B . 
S 5 HOH 26  326 143 HOH HOH B . 
S 5 HOH 27  327 20  HOH HOH B . 
S 5 HOH 28  328 733 HOH HOH B . 
S 5 HOH 29  329 486 HOH HOH B . 
S 5 HOH 30  330 254 HOH HOH B . 
S 5 HOH 31  331 573 HOH HOH B . 
S 5 HOH 32  332 438 HOH HOH B . 
S 5 HOH 33  333 596 HOH HOH B . 
S 5 HOH 34  334 27  HOH HOH B . 
S 5 HOH 35  335 257 HOH HOH B . 
S 5 HOH 36  336 3   HOH HOH B . 
S 5 HOH 37  337 592 HOH HOH B . 
S 5 HOH 38  338 82  HOH HOH B . 
S 5 HOH 39  339 108 HOH HOH B . 
S 5 HOH 40  340 218 HOH HOH B . 
S 5 HOH 41  341 118 HOH HOH B . 
S 5 HOH 42  342 416 HOH HOH B . 
S 5 HOH 43  343 354 HOH HOH B . 
S 5 HOH 44  344 339 HOH HOH B . 
S 5 HOH 45  345 433 HOH HOH B . 
S 5 HOH 46  346 607 HOH HOH B . 
S 5 HOH 47  347 285 HOH HOH B . 
S 5 HOH 48  348 36  HOH HOH B . 
S 5 HOH 49  349 491 HOH HOH B . 
S 5 HOH 50  350 447 HOH HOH B . 
S 5 HOH 51  351 290 HOH HOH B . 
S 5 HOH 52  352 617 HOH HOH B . 
S 5 HOH 53  353 214 HOH HOH B . 
S 5 HOH 54  354 242 HOH HOH B . 
S 5 HOH 55  355 216 HOH HOH B . 
S 5 HOH 56  356 509 HOH HOH B . 
S 5 HOH 57  357 665 HOH HOH B . 
S 5 HOH 58  358 593 HOH HOH B . 
S 5 HOH 59  359 329 HOH HOH B . 
S 5 HOH 60  360 338 HOH HOH B . 
S 5 HOH 61  361 265 HOH HOH B . 
S 5 HOH 62  362 535 HOH HOH B . 
S 5 HOH 63  363 259 HOH HOH B . 
S 5 HOH 64  364 66  HOH HOH B . 
S 5 HOH 65  365 539 HOH HOH B . 
S 5 HOH 66  366 598 HOH HOH B . 
S 5 HOH 67  367 543 HOH HOH B . 
S 5 HOH 68  368 171 HOH HOH B . 
S 5 HOH 69  369 101 HOH HOH B . 
S 5 HOH 70  370 132 HOH HOH B . 
S 5 HOH 71  371 186 HOH HOH B . 
S 5 HOH 72  372 212 HOH HOH B . 
S 5 HOH 73  373 374 HOH HOH B . 
S 5 HOH 74  374 588 HOH HOH B . 
S 5 HOH 75  375 4   HOH HOH B . 
S 5 HOH 76  376 152 HOH HOH B . 
S 5 HOH 77  377 192 HOH HOH B . 
S 5 HOH 78  378 30  HOH HOH B . 
S 5 HOH 79  379 50  HOH HOH B . 
S 5 HOH 80  380 519 HOH HOH B . 
S 5 HOH 81  381 54  HOH HOH B . 
S 5 HOH 82  382 70  HOH HOH B . 
S 5 HOH 83  383 441 HOH HOH B . 
S 5 HOH 84  384 293 HOH HOH B . 
S 5 HOH 85  385 394 HOH HOH B . 
S 5 HOH 86  386 150 HOH HOH B . 
S 5 HOH 87  387 716 HOH HOH B . 
S 5 HOH 88  388 76  HOH HOH B . 
S 5 HOH 89  389 348 HOH HOH B . 
S 5 HOH 90  390 47  HOH HOH B . 
S 5 HOH 91  391 324 HOH HOH B . 
S 5 HOH 92  392 266 HOH HOH B . 
S 5 HOH 93  393 173 HOH HOH B . 
S 5 HOH 94  394 505 HOH HOH B . 
S 5 HOH 95  395 510 HOH HOH B . 
S 5 HOH 96  396 14  HOH HOH B . 
S 5 HOH 97  397 127 HOH HOH B . 
S 5 HOH 98  398 229 HOH HOH B . 
S 5 HOH 99  399 726 HOH HOH B . 
S 5 HOH 100 400 203 HOH HOH B . 
S 5 HOH 101 401 92  HOH HOH B . 
S 5 HOH 102 402 304 HOH HOH B . 
S 5 HOH 103 403 56  HOH HOH B . 
S 5 HOH 104 404 306 HOH HOH B . 
S 5 HOH 105 405 451 HOH HOH B . 
S 5 HOH 106 406 126 HOH HOH B . 
S 5 HOH 107 407 251 HOH HOH B . 
S 5 HOH 108 408 426 HOH HOH B . 
S 5 HOH 109 409 725 HOH HOH B . 
S 5 HOH 110 410 531 HOH HOH B . 
S 5 HOH 111 411 22  HOH HOH B . 
S 5 HOH 112 412 136 HOH HOH B . 
S 5 HOH 113 413 450 HOH HOH B . 
S 5 HOH 114 414 521 HOH HOH B . 
S 5 HOH 115 415 652 HOH HOH B . 
S 5 HOH 116 416 463 HOH HOH B . 
S 5 HOH 117 417 430 HOH HOH B . 
S 5 HOH 118 418 298 HOH HOH B . 
S 5 HOH 119 419 21  HOH HOH B . 
S 5 HOH 120 420 371 HOH HOH B . 
S 5 HOH 121 421 387 HOH HOH B . 
S 5 HOH 122 422 174 HOH HOH B . 
S 5 HOH 123 423 207 HOH HOH B . 
S 5 HOH 124 424 340 HOH HOH B . 
S 5 HOH 125 425 105 HOH HOH B . 
S 5 HOH 126 426 255 HOH HOH B . 
S 5 HOH 127 427 640 HOH HOH B . 
S 5 HOH 128 428 104 HOH HOH B . 
S 5 HOH 129 429 13  HOH HOH B . 
S 5 HOH 130 430 736 HOH HOH B . 
S 5 HOH 131 431 684 HOH HOH B . 
S 5 HOH 132 432 161 HOH HOH B . 
S 5 HOH 133 433 660 HOH HOH B . 
S 5 HOH 134 434 113 HOH HOH B . 
S 5 HOH 135 435 490 HOH HOH B . 
S 5 HOH 136 436 109 HOH HOH B . 
S 5 HOH 137 437 667 HOH HOH B . 
S 5 HOH 138 438 579 HOH HOH B . 
S 5 HOH 139 439 187 HOH HOH B . 
S 5 HOH 140 440 659 HOH HOH B . 
S 5 HOH 141 441 131 HOH HOH B . 
S 5 HOH 142 442 230 HOH HOH B . 
S 5 HOH 143 443 419 HOH HOH B . 
S 5 HOH 144 444 643 HOH HOH B . 
S 5 HOH 145 445 234 HOH HOH B . 
S 5 HOH 146 446 308 HOH HOH B . 
S 5 HOH 147 447 319 HOH HOH B . 
S 5 HOH 148 448 664 HOH HOH B . 
S 5 HOH 149 449 629 HOH HOH B . 
S 5 HOH 150 450 481 HOH HOH B . 
S 5 HOH 151 451 628 HOH HOH B . 
S 5 HOH 152 452 683 HOH HOH B . 
S 5 HOH 153 453 321 HOH HOH B . 
S 5 HOH 154 454 471 HOH HOH B . 
S 5 HOH 155 455 466 HOH HOH B . 
S 5 HOH 156 456 594 HOH HOH B . 
S 5 HOH 157 457 639 HOH HOH B . 
S 5 HOH 158 458 682 HOH HOH B . 
S 5 HOH 159 459 479 HOH HOH B . 
S 5 HOH 160 460 587 HOH HOH B . 
S 5 HOH 161 461 296 HOH HOH B . 
S 5 HOH 162 462 547 HOH HOH B . 
S 5 HOH 163 463 668 HOH HOH B . 
S 5 HOH 164 464 723 HOH HOH B . 
S 5 HOH 165 465 484 HOH HOH B . 
S 5 HOH 166 466 663 HOH HOH B . 
S 5 HOH 167 467 697 HOH HOH B . 
S 5 HOH 168 468 231 HOH HOH B . 
S 5 HOH 169 469 449 HOH HOH B . 
S 5 HOH 170 470 641 HOH HOH B . 
S 5 HOH 171 471 278 HOH HOH B . 
S 5 HOH 172 472 474 HOH HOH B . 
S 5 HOH 173 473 575 HOH HOH B . 
S 5 HOH 174 474 688 HOH HOH B . 
S 5 HOH 175 475 709 HOH HOH B . 
S 5 HOH 176 476 657 HOH HOH B . 
S 5 HOH 177 477 432 HOH HOH B . 
S 5 HOH 178 478 404 HOH HOH B . 
S 5 HOH 179 479 731 HOH HOH B . 
S 5 HOH 180 480 693 HOH HOH B . 
S 5 HOH 181 481 678 HOH HOH B . 
S 5 HOH 182 482 473 HOH HOH B . 
S 5 HOH 183 483 408 HOH HOH B . 
S 5 HOH 184 484 626 HOH HOH B . 
S 5 HOH 185 485 585 HOH HOH B . 
S 5 HOH 186 486 552 HOH HOH B . 
S 5 HOH 187 487 378 HOH HOH B . 
S 5 HOH 188 488 562 HOH HOH B . 
S 5 HOH 189 489 477 HOH HOH B . 
S 5 HOH 190 490 707 HOH HOH B . 
S 5 HOH 191 491 737 HOH HOH B . 
S 5 HOH 192 492 337 HOH HOH B . 
S 5 HOH 193 493 642 HOH HOH B . 
S 5 HOH 194 494 469 HOH HOH B . 
S 5 HOH 195 495 551 HOH HOH B . 
S 5 HOH 196 496 619 HOH HOH B . 
S 5 HOH 197 497 555 HOH HOH B . 
T 5 HOH 1   301 123 HOH HOH C . 
T 5 HOH 2   302 630 HOH HOH C . 
T 5 HOH 3   303 738 HOH HOH C . 
T 5 HOH 4   304 369 HOH HOH C . 
T 5 HOH 5   305 613 HOH HOH C . 
T 5 HOH 6   306 323 HOH HOH C . 
T 5 HOH 7   307 403 HOH HOH C . 
T 5 HOH 8   308 656 HOH HOH C . 
T 5 HOH 9   309 263 HOH HOH C . 
T 5 HOH 10  310 281 HOH HOH C . 
T 5 HOH 11  311 352 HOH HOH C . 
T 5 HOH 12  312 527 HOH HOH C . 
T 5 HOH 13  313 34  HOH HOH C . 
T 5 HOH 14  314 370 HOH HOH C . 
T 5 HOH 15  315 658 HOH HOH C . 
T 5 HOH 16  316 395 HOH HOH C . 
T 5 HOH 17  317 711 HOH HOH C . 
T 5 HOH 18  318 553 HOH HOH C . 
T 5 HOH 19  319 530 HOH HOH C . 
T 5 HOH 20  320 542 HOH HOH C . 
T 5 HOH 21  321 600 HOH HOH C . 
T 5 HOH 22  322 210 HOH HOH C . 
T 5 HOH 23  323 80  HOH HOH C . 
T 5 HOH 24  324 407 HOH HOH C . 
T 5 HOH 25  325 58  HOH HOH C . 
T 5 HOH 26  326 240 HOH HOH C . 
T 5 HOH 27  327 31  HOH HOH C . 
T 5 HOH 28  328 32  HOH HOH C . 
T 5 HOH 29  329 655 HOH HOH C . 
T 5 HOH 30  330 149 HOH HOH C . 
T 5 HOH 31  331 446 HOH HOH C . 
T 5 HOH 32  332 359 HOH HOH C . 
T 5 HOH 33  333 222 HOH HOH C . 
T 5 HOH 34  334 119 HOH HOH C . 
T 5 HOH 35  335 320 HOH HOH C . 
T 5 HOH 36  336 273 HOH HOH C . 
T 5 HOH 37  337 264 HOH HOH C . 
T 5 HOH 38  338 253 HOH HOH C . 
T 5 HOH 39  339 289 HOH HOH C . 
T 5 HOH 40  340 148 HOH HOH C . 
T 5 HOH 41  341 29  HOH HOH C . 
T 5 HOH 42  342 98  HOH HOH C . 
T 5 HOH 43  343 615 HOH HOH C . 
T 5 HOH 44  344 162 HOH HOH C . 
T 5 HOH 45  345 15  HOH HOH C . 
T 5 HOH 46  346 154 HOH HOH C . 
T 5 HOH 47  347 262 HOH HOH C . 
T 5 HOH 48  348 295 HOH HOH C . 
T 5 HOH 49  349 502 HOH HOH C . 
T 5 HOH 50  350 52  HOH HOH C . 
T 5 HOH 51  351 397 HOH HOH C . 
T 5 HOH 52  352 492 HOH HOH C . 
T 5 HOH 53  353 383 HOH HOH C . 
T 5 HOH 54  354 69  HOH HOH C . 
T 5 HOH 55  355 276 HOH HOH C . 
T 5 HOH 56  356 525 HOH HOH C . 
T 5 HOH 57  357 421 HOH HOH C . 
T 5 HOH 58  358 350 HOH HOH C . 
T 5 HOH 59  359 26  HOH HOH C . 
T 5 HOH 60  360 363 HOH HOH C . 
T 5 HOH 61  361 157 HOH HOH C . 
T 5 HOH 62  362 39  HOH HOH C . 
T 5 HOH 63  363 233 HOH HOH C . 
T 5 HOH 64  364 9   HOH HOH C . 
T 5 HOH 65  365 488 HOH HOH C . 
T 5 HOH 66  366 417 HOH HOH C . 
T 5 HOH 67  367 19  HOH HOH C . 
T 5 HOH 68  368 437 HOH HOH C . 
T 5 HOH 69  369 411 HOH HOH C . 
T 5 HOH 70  370 130 HOH HOH C . 
T 5 HOH 71  371 135 HOH HOH C . 
T 5 HOH 72  372 511 HOH HOH C . 
T 5 HOH 73  373 331 HOH HOH C . 
T 5 HOH 74  374 182 HOH HOH C . 
T 5 HOH 75  375 40  HOH HOH C . 
T 5 HOH 76  376 644 HOH HOH C . 
T 5 HOH 77  377 504 HOH HOH C . 
T 5 HOH 78  378 699 HOH HOH C . 
T 5 HOH 79  379 507 HOH HOH C . 
T 5 HOH 80  380 380 HOH HOH C . 
T 5 HOH 81  381 385 HOH HOH C . 
T 5 HOH 82  382 223 HOH HOH C . 
T 5 HOH 83  383 694 HOH HOH C . 
T 5 HOH 84  384 398 HOH HOH C . 
T 5 HOH 85  385 206 HOH HOH C . 
T 5 HOH 86  386 25  HOH HOH C . 
T 5 HOH 87  387 346 HOH HOH C . 
T 5 HOH 88  388 155 HOH HOH C . 
T 5 HOH 89  389 730 HOH HOH C . 
T 5 HOH 90  390 16  HOH HOH C . 
T 5 HOH 91  391 292 HOH HOH C . 
T 5 HOH 92  392 103 HOH HOH C . 
T 5 HOH 93  393 17  HOH HOH C . 
T 5 HOH 94  394 425 HOH HOH C . 
T 5 HOH 95  395 23  HOH HOH C . 
T 5 HOH 96  396 512 HOH HOH C . 
T 5 HOH 97  397 238 HOH HOH C . 
T 5 HOH 98  398 205 HOH HOH C . 
T 5 HOH 99  399 59  HOH HOH C . 
T 5 HOH 100 400 252 HOH HOH C . 
T 5 HOH 101 401 102 HOH HOH C . 
T 5 HOH 102 402 379 HOH HOH C . 
T 5 HOH 103 403 44  HOH HOH C . 
T 5 HOH 104 404 73  HOH HOH C . 
T 5 HOH 105 405 423 HOH HOH C . 
T 5 HOH 106 406 391 HOH HOH C . 
T 5 HOH 107 407 499 HOH HOH C . 
T 5 HOH 108 408 215 HOH HOH C . 
T 5 HOH 109 409 114 HOH HOH C . 
T 5 HOH 110 410 96  HOH HOH C . 
T 5 HOH 111 411 208 HOH HOH C . 
T 5 HOH 112 412 334 HOH HOH C . 
T 5 HOH 113 413 268 HOH HOH C . 
T 5 HOH 114 414 84  HOH HOH C . 
T 5 HOH 115 415 79  HOH HOH C . 
T 5 HOH 116 416 503 HOH HOH C . 
T 5 HOH 117 417 85  HOH HOH C . 
T 5 HOH 118 418 322 HOH HOH C . 
T 5 HOH 119 419 336 HOH HOH C . 
T 5 HOH 120 420 580 HOH HOH C . 
T 5 HOH 121 421 45  HOH HOH C . 
T 5 HOH 122 422 99  HOH HOH C . 
T 5 HOH 123 423 133 HOH HOH C . 
T 5 HOH 124 424 197 HOH HOH C . 
T 5 HOH 125 425 166 HOH HOH C . 
T 5 HOH 126 426 244 HOH HOH C . 
T 5 HOH 127 427 284 HOH HOH C . 
T 5 HOH 128 428 75  HOH HOH C . 
T 5 HOH 129 429 719 HOH HOH C . 
T 5 HOH 130 430 61  HOH HOH C . 
T 5 HOH 131 431 291 HOH HOH C . 
T 5 HOH 132 432 209 HOH HOH C . 
T 5 HOH 133 433 318 HOH HOH C . 
T 5 HOH 134 434 246 HOH HOH C . 
T 5 HOH 135 435 164 HOH HOH C . 
T 5 HOH 136 436 267 HOH HOH C . 
T 5 HOH 137 437 572 HOH HOH C . 
T 5 HOH 138 438 601 HOH HOH C . 
T 5 HOH 139 439 518 HOH HOH C . 
T 5 HOH 140 440 124 HOH HOH C . 
T 5 HOH 141 441 599 HOH HOH C . 
T 5 HOH 142 442 614 HOH HOH C . 
T 5 HOH 143 443 294 HOH HOH C . 
T 5 HOH 144 444 344 HOH HOH C . 
T 5 HOH 145 445 702 HOH HOH C . 
T 5 HOH 146 446 405 HOH HOH C . 
T 5 HOH 147 447 489 HOH HOH C . 
T 5 HOH 148 448 565 HOH HOH C . 
T 5 HOH 149 449 365 HOH HOH C . 
T 5 HOH 150 450 712 HOH HOH C . 
T 5 HOH 151 451 146 HOH HOH C . 
T 5 HOH 152 452 741 HOH HOH C . 
T 5 HOH 153 453 545 HOH HOH C . 
T 5 HOH 154 454 618 HOH HOH C . 
T 5 HOH 155 455 576 HOH HOH C . 
T 5 HOH 156 456 548 HOH HOH C . 
T 5 HOH 157 457 546 HOH HOH C . 
T 5 HOH 158 458 351 HOH HOH C . 
T 5 HOH 159 459 482 HOH HOH C . 
T 5 HOH 160 460 577 HOH HOH C . 
T 5 HOH 161 461 583 HOH HOH C . 
T 5 HOH 162 462 700 HOH HOH C . 
T 5 HOH 163 463 564 HOH HOH C . 
T 5 HOH 164 464 578 HOH HOH C . 
T 5 HOH 165 465 692 HOH HOH C . 
T 5 HOH 166 466 706 HOH HOH C . 
T 5 HOH 167 467 586 HOH HOH C . 
T 5 HOH 168 468 406 HOH HOH C . 
T 5 HOH 169 469 480 HOH HOH C . 
T 5 HOH 170 470 671 HOH HOH C . 
T 5 HOH 171 471 721 HOH HOH C . 
T 5 HOH 172 472 670 HOH HOH C . 
T 5 HOH 173 473 236 HOH HOH C . 
T 5 HOH 174 474 478 HOH HOH C . 
T 5 HOH 175 475 645 HOH HOH C . 
T 5 HOH 176 476 424 HOH HOH C . 
T 5 HOH 177 477 606 HOH HOH C . 
T 5 HOH 178 478 666 HOH HOH C . 
T 5 HOH 179 479 388 HOH HOH C . 
U 5 HOH 1   301 679 HOH HOH D . 
U 5 HOH 2   302 672 HOH HOH D . 
U 5 HOH 3   303 440 HOH HOH D . 
U 5 HOH 4   304 608 HOH HOH D . 
U 5 HOH 5   305 172 HOH HOH D . 
U 5 HOH 6   306 569 HOH HOH D . 
U 5 HOH 7   307 217 HOH HOH D . 
U 5 HOH 8   308 662 HOH HOH D . 
U 5 HOH 9   309 739 HOH HOH D . 
U 5 HOH 10  310 685 HOH HOH D . 
U 5 HOH 11  311 633 HOH HOH D . 
U 5 HOH 12  312 496 HOH HOH D . 
U 5 HOH 13  313 91  HOH HOH D . 
U 5 HOH 14  314 410 HOH HOH D . 
U 5 HOH 15  315 637 HOH HOH D . 
U 5 HOH 16  316 325 HOH HOH D . 
U 5 HOH 17  317 53  HOH HOH D . 
U 5 HOH 18  318 170 HOH HOH D . 
U 5 HOH 19  319 353 HOH HOH D . 
U 5 HOH 20  320 392 HOH HOH D . 
U 5 HOH 21  321 674 HOH HOH D . 
U 5 HOH 22  322 191 HOH HOH D . 
U 5 HOH 23  323 402 HOH HOH D . 
U 5 HOH 24  324 112 HOH HOH D . 
U 5 HOH 25  325 445 HOH HOH D . 
U 5 HOH 26  326 160 HOH HOH D . 
U 5 HOH 27  327 204 HOH HOH D . 
U 5 HOH 28  328 315 HOH HOH D . 
U 5 HOH 29  329 121 HOH HOH D . 
U 5 HOH 30  330 312 HOH HOH D . 
U 5 HOH 31  331 390 HOH HOH D . 
U 5 HOH 32  332 500 HOH HOH D . 
U 5 HOH 33  333 37  HOH HOH D . 
U 5 HOH 34  334 142 HOH HOH D . 
U 5 HOH 35  335 78  HOH HOH D . 
U 5 HOH 36  336 727 HOH HOH D . 
U 5 HOH 37  337 63  HOH HOH D . 
U 5 HOH 38  338 140 HOH HOH D . 
U 5 HOH 39  339 302 HOH HOH D . 
U 5 HOH 40  340 349 HOH HOH D . 
U 5 HOH 41  341 184 HOH HOH D . 
U 5 HOH 42  342 307 HOH HOH D . 
U 5 HOH 43  343 487 HOH HOH D . 
U 5 HOH 44  344 303 HOH HOH D . 
U 5 HOH 45  345 513 HOH HOH D . 
U 5 HOH 46  346 428 HOH HOH D . 
U 5 HOH 47  347 435 HOH HOH D . 
U 5 HOH 48  348 375 HOH HOH D . 
U 5 HOH 49  349 18  HOH HOH D . 
U 5 HOH 50  350 453 HOH HOH D . 
U 5 HOH 51  351 86  HOH HOH D . 
U 5 HOH 52  352 332 HOH HOH D . 
U 5 HOH 53  353 151 HOH HOH D . 
U 5 HOH 54  354 431 HOH HOH D . 
U 5 HOH 55  355 12  HOH HOH D . 
U 5 HOH 56  356 41  HOH HOH D . 
U 5 HOH 57  357 461 HOH HOH D . 
U 5 HOH 58  358 147 HOH HOH D . 
U 5 HOH 59  359 247 HOH HOH D . 
U 5 HOH 60  360 68  HOH HOH D . 
U 5 HOH 61  361 616 HOH HOH D . 
U 5 HOH 62  362 106 HOH HOH D . 
U 5 HOH 63  363 485 HOH HOH D . 
U 5 HOH 64  364 200 HOH HOH D . 
U 5 HOH 65  365 442 HOH HOH D . 
U 5 HOH 66  366 125 HOH HOH D . 
U 5 HOH 67  367 249 HOH HOH D . 
U 5 HOH 68  368 528 HOH HOH D . 
U 5 HOH 69  369 211 HOH HOH D . 
U 5 HOH 70  370 581 HOH HOH D . 
U 5 HOH 71  371 427 HOH HOH D . 
U 5 HOH 72  372 409 HOH HOH D . 
U 5 HOH 73  373 239 HOH HOH D . 
U 5 HOH 74  374 638 HOH HOH D . 
U 5 HOH 75  375 250 HOH HOH D . 
U 5 HOH 76  376 362 HOH HOH D . 
U 5 HOH 77  377 529 HOH HOH D . 
U 5 HOH 78  378 571 HOH HOH D . 
U 5 HOH 79  379 358 HOH HOH D . 
U 5 HOH 80  380 129 HOH HOH D . 
U 5 HOH 81  381 335 HOH HOH D . 
U 5 HOH 82  382 420 HOH HOH D . 
U 5 HOH 83  383 237 HOH HOH D . 
U 5 HOH 84  384 345 HOH HOH D . 
U 5 HOH 85  385 533 HOH HOH D . 
U 5 HOH 86  386 464 HOH HOH D . 
U 5 HOH 87  387 176 HOH HOH D . 
U 5 HOH 88  388 568 HOH HOH D . 
U 5 HOH 89  389 163 HOH HOH D . 
U 5 HOH 90  390 299 HOH HOH D . 
U 5 HOH 91  391 272 HOH HOH D . 
U 5 HOH 92  392 418 HOH HOH D . 
U 5 HOH 93  393 520 HOH HOH D . 
U 5 HOH 94  394 270 HOH HOH D . 
U 5 HOH 95  395 241 HOH HOH D . 
U 5 HOH 96  396 367 HOH HOH D . 
U 5 HOH 97  397 595 HOH HOH D . 
U 5 HOH 98  398 260 HOH HOH D . 
U 5 HOH 99  399 93  HOH HOH D . 
U 5 HOH 100 400 508 HOH HOH D . 
U 5 HOH 101 401 271 HOH HOH D . 
U 5 HOH 102 402 309 HOH HOH D . 
U 5 HOH 103 403 316 HOH HOH D . 
U 5 HOH 104 404 144 HOH HOH D . 
U 5 HOH 105 405 11  HOH HOH D . 
U 5 HOH 106 406 436 HOH HOH D . 
U 5 HOH 107 407 226 HOH HOH D . 
U 5 HOH 108 408 245 HOH HOH D . 
U 5 HOH 109 409 185 HOH HOH D . 
U 5 HOH 110 410 134 HOH HOH D . 
U 5 HOH 111 411 412 HOH HOH D . 
U 5 HOH 112 412 300 HOH HOH D . 
U 5 HOH 113 413 455 HOH HOH D . 
U 5 HOH 114 414 195 HOH HOH D . 
U 5 HOH 115 415 248 HOH HOH D . 
U 5 HOH 116 416 48  HOH HOH D . 
U 5 HOH 117 417 415 HOH HOH D . 
U 5 HOH 118 418 128 HOH HOH D . 
U 5 HOH 119 419 178 HOH HOH D . 
U 5 HOH 120 420 310 HOH HOH D . 
U 5 HOH 121 421 389 HOH HOH D . 
U 5 HOH 122 422 49  HOH HOH D . 
U 5 HOH 123 423 183 HOH HOH D . 
U 5 HOH 124 424 439 HOH HOH D . 
U 5 HOH 125 425 100 HOH HOH D . 
U 5 HOH 126 426 120 HOH HOH D . 
U 5 HOH 127 427 169 HOH HOH D . 
U 5 HOH 128 428 297 HOH HOH D . 
U 5 HOH 129 429 483 HOH HOH D . 
U 5 HOH 130 430 636 HOH HOH D . 
U 5 HOH 131 431 713 HOH HOH D . 
U 5 HOH 132 432 523 HOH HOH D . 
U 5 HOH 133 433 703 HOH HOH D . 
U 5 HOH 134 434 95  HOH HOH D . 
U 5 HOH 135 435 532 HOH HOH D . 
U 5 HOH 136 436 429 HOH HOH D . 
U 5 HOH 137 437 724 HOH HOH D . 
U 5 HOH 138 438 522 HOH HOH D . 
U 5 HOH 139 439 277 HOH HOH D . 
U 5 HOH 140 440 648 HOH HOH D . 
U 5 HOH 141 441 735 HOH HOH D . 
U 5 HOH 142 442 558 HOH HOH D . 
U 5 HOH 143 443 570 HOH HOH D . 
U 5 HOH 144 444 611 HOH HOH D . 
U 5 HOH 145 445 605 HOH HOH D . 
U 5 HOH 146 446 549 HOH HOH D . 
U 5 HOH 147 447 328 HOH HOH D . 
U 5 HOH 148 448 609 HOH HOH D . 
U 5 HOH 149 449 710 HOH HOH D . 
U 5 HOH 150 450 560 HOH HOH D . 
U 5 HOH 151 451 460 HOH HOH D . 
U 5 HOH 152 452 561 HOH HOH D . 
U 5 HOH 153 453 472 HOH HOH D . 
U 5 HOH 154 454 333 HOH HOH D . 
U 5 HOH 155 455 602 HOH HOH D . 
U 5 HOH 156 456 462 HOH HOH D . 
U 5 HOH 157 457 444 HOH HOH D . 
U 5 HOH 158 458 567 HOH HOH D . 
U 5 HOH 159 459 603 HOH HOH D . 
U 5 HOH 160 460 228 HOH HOH D . 
U 5 HOH 161 461 690 HOH HOH D . 
U 5 HOH 162 462 274 HOH HOH D . 
U 5 HOH 163 463 620 HOH HOH D . 
U 5 HOH 164 464 475 HOH HOH D . 
U 5 HOH 165 465 646 HOH HOH D . 
U 5 HOH 166 466 414 HOH HOH D . 
U 5 HOH 167 467 604 HOH HOH D . 
U 5 HOH 168 468 621 HOH HOH D . 
U 5 HOH 169 469 42  HOH HOH D . 
U 5 HOH 170 470 687 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.17.1_3660: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.83 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XZZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.074 
_cell.length_a_esd                 ? 
_cell.length_b                     137.540 
_cell.length_b_esd                 ? 
_cell.length_c                     52.848 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XZZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XZZ 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.57 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M sodium formate, 0.1 M Bis-Tris propane, pH 6.5, and 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99987 
_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                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XZZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               24.27 
_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                                     73843 
_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                           95.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.369 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.060 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.051 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           13.45 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6968 
_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                               4.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          90.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.152 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XZZ 
_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                            1.72 
_refine.ls_d_res_low                             24.27 
_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                     73804 
_refine.ls_number_reflns_R_free                  2006 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.11 
_refine.ls_percent_reflns_R_free                 2.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1617 
_refine.ls_R_factor_R_free                       0.1917 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1608 
_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                          1.43 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3WP4 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.04 
_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                            0.17 
_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                       1.72 
_refine_hist.d_res_low                        24.27 
_refine_hist.number_atoms_solvent             740 
_refine_hist.number_atoms_total               6725 
_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        5903 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         82 
_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' ? 0.006 ? 6151 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.897 ? 8418 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.387 ? 877  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060 ? 886  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 1089 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.72 1.76  . . 129 4483 84.00 . . . . 0.1889 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.76 1.81  . . 138 5007 93.00 . . . . 0.1814 . . . . . . . . . . . 0.2118 
'X-RAY DIFFRACTION' 1.81 1.87  . . 140 5107 94.00 . . . . 0.1711 . . . . . . . . . . . 0.2544 
'X-RAY DIFFRACTION' 1.87 1.93  . . 151 5102 95.00 . . . . 0.1655 . . . . . . . . . . . 0.2181 
'X-RAY DIFFRACTION' 1.93 1.99  . . 145 5136 96.00 . . . . 0.1634 . . . . . . . . . . . 0.2000 
'X-RAY DIFFRACTION' 1.99 2.07  . . 142 5205 96.00 . . . . 0.1623 . . . . . . . . . . . 0.2221 
'X-RAY DIFFRACTION' 2.07 2.17  . . 141 5187 96.00 . . . . 0.1631 . . . . . . . . . . . 0.1974 
'X-RAY DIFFRACTION' 2.17 2.28  . . 142 5165 96.00 . . . . 0.1591 . . . . . . . . . . . 0.1845 
'X-RAY DIFFRACTION' 2.28 2.43  . . 150 5210 97.00 . . . . 0.1691 . . . . . . . . . . . 0.2078 
'X-RAY DIFFRACTION' 2.43 2.61  . . 146 5282 97.00 . . . . 0.1724 . . . . . . . . . . . 0.2162 
'X-RAY DIFFRACTION' 2.61 2.88  . . 144 5278 98.00 . . . . 0.1734 . . . . . . . . . . . 0.1957 
'X-RAY DIFFRACTION' 2.88 3.29  . . 151 5292 98.00 . . . . 0.1581 . . . . . . . . . . . 0.1826 
'X-RAY DIFFRACTION' 3.29 4.14  . . 144 5143 95.00 . . . . 0.1437 . . . . . . . . . . . 0.1597 
'X-RAY DIFFRACTION' 4.14 24.27 . . 143 5201 95.00 . . . . 0.1526 . . . . . . . . . . . 0.1699 
# 
_struct.entry_id                     8XZZ 
_struct.title                        'Structure of a xylanase Xyl-1 M4 E175A in complex with xylobiose' 
_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        8XZZ 
_struct_keywords.text            
;Evolutionarily conserved mutations; Xylanase robustness; Non-loop region; Substrate binding patterns; Conformational dynamics, HYDROLASE
;
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 3 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 5 ? 
S N N 5 ? 
T N N 5 ? 
U N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q0CMZ1_ASPTN 
_struct_ref.pdbx_db_accession          Q0CMZ1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ITSSETGTNNGYYYSFWTDGGGQVTYTNGDAGAYSVEWSNSGNFVAGKGWNPGSSQTITYSGEWNPNGNSYLSVYGWTQN
PLVEYYIVESFSTYDPSTGAQELGTVETDDGTYKIYKTTRENAPSIEGTATFNQYWSVRTDHRVGGTVTTQNHFDAWKNA
GLEMGTANYMIVATEGYQSSGSASITVQ
;
_struct_ref.pdbx_align_begin           0 
# 
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 8XZZ A 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
2 1 8XZZ B 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
3 1 8XZZ C 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
4 1 8XZZ D 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
# 
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 8XZZ GLY A 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 1  
1 8XZZ ALA A 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 2  
1 8XZZ GLY A 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  3  
1 8XZZ ALA A 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  4  
1 8XZZ GLY A 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  5  
1 8XZZ ALA A 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  6  
1 8XZZ GLY A 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  7  
1 8XZZ ALA A 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  8  
1 8XZZ GLY A 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  9  
1 8XZZ ALA A 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  10 
1 8XZZ GLY A 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  11 
1 8XZZ MET A 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   12 
1 8XZZ GLU A 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   13 
1 8XZZ PRO A 43  ? UNP Q0CMZ1 ASP 62  conflict              31  14 
1 8XZZ GLN A 46  ? UNP Q0CMZ1 ALA 65  conflict              34  15 
1 8XZZ GLN A 130 ? UNP Q0CMZ1 LYS 149 conflict              118 16 
1 8XZZ HIS A 180 ? UNP Q0CMZ1 ALA 199 conflict              168 17 
1 8XZZ ALA A 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 18 
2 8XZZ GLY B 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 19 
2 8XZZ ALA B 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 20 
2 8XZZ GLY B 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  21 
2 8XZZ ALA B 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  22 
2 8XZZ GLY B 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  23 
2 8XZZ ALA B 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  24 
2 8XZZ GLY B 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  25 
2 8XZZ ALA B 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  26 
2 8XZZ GLY B 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  27 
2 8XZZ ALA B 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  28 
2 8XZZ GLY B 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  29 
2 8XZZ MET B 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   30 
2 8XZZ GLU B 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   31 
2 8XZZ PRO B 43  ? UNP Q0CMZ1 ASP 62  conflict              31  32 
2 8XZZ GLN B 46  ? UNP Q0CMZ1 ALA 65  conflict              34  33 
2 8XZZ GLN B 130 ? UNP Q0CMZ1 LYS 149 conflict              118 34 
2 8XZZ HIS B 180 ? UNP Q0CMZ1 ALA 199 conflict              168 35 
2 8XZZ ALA B 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 36 
3 8XZZ GLY C 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 37 
3 8XZZ ALA C 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 38 
3 8XZZ GLY C 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  39 
3 8XZZ ALA C 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  40 
3 8XZZ GLY C 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  41 
3 8XZZ ALA C 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  42 
3 8XZZ GLY C 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  43 
3 8XZZ ALA C 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  44 
3 8XZZ GLY C 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  45 
3 8XZZ ALA C 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  46 
3 8XZZ GLY C 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  47 
3 8XZZ MET C 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   48 
3 8XZZ GLU C 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   49 
3 8XZZ PRO C 43  ? UNP Q0CMZ1 ASP 62  conflict              31  50 
3 8XZZ GLN C 46  ? UNP Q0CMZ1 ALA 65  conflict              34  51 
3 8XZZ GLN C 130 ? UNP Q0CMZ1 LYS 149 conflict              118 52 
3 8XZZ HIS C 180 ? UNP Q0CMZ1 ALA 199 conflict              168 53 
3 8XZZ ALA C 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 54 
4 8XZZ GLY D 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 55 
4 8XZZ ALA D 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 56 
4 8XZZ GLY D 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  57 
4 8XZZ ALA D 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  58 
4 8XZZ GLY D 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  59 
4 8XZZ ALA D 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  60 
4 8XZZ GLY D 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  61 
4 8XZZ ALA D 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  62 
4 8XZZ GLY D 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  63 
4 8XZZ ALA D 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  64 
4 8XZZ GLY D 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  65 
4 8XZZ MET D 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   66 
4 8XZZ GLU D 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   67 
4 8XZZ PRO D 43  ? UNP Q0CMZ1 ASP 62  conflict              31  68 
4 8XZZ GLN D 46  ? UNP Q0CMZ1 ALA 65  conflict              34  69 
4 8XZZ GLN D 130 ? UNP Q0CMZ1 LYS 149 conflict              118 70 
4 8XZZ HIS D 180 ? UNP Q0CMZ1 ALA 199 conflict              168 71 
4 8XZZ ALA D 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 72 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,G,R   
2 1 B,H,I,J,K,S 
3 1 C,L,M,T     
4 1 D,N,O,P,Q,U 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 6   ? ALA A 10  ? ALA A -6  ALA A -2  5 ? 5  
HELX_P HELX_P2 AA2 THR A 163 ? ALA A 173 ? THR A 151 ALA A 161 1 ? 11 
HELX_P HELX_P3 AA3 THR B 163 ? ALA B 173 ? THR B 151 ALA B 161 1 ? 11 
HELX_P HELX_P4 AA4 THR C 163 ? ALA C 173 ? THR C 151 ALA C 161 1 ? 11 
HELX_P HELX_P5 AA5 THR D 163 ? ALA D 173 ? THR D 151 ALA D 161 1 ? 11 
# 
_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 
covale1  covale both ? J XYP .   C1  ? ? ? 1_555 K XYP . O4 ? ? B XYP 203 B XYP 204 1_555 ? ? ? ? ? ? ? 1.373 ?    ? 
covale2  covale both ? L XYP .   O4  ? ? ? 1_555 M XYP . C1 ? ? C XYP 201 C XYP 202 1_555 ? ? ? ? ? ? ? 1.373 ?    ? 
covale3  covale both ? P XYP .   C1  ? ? ? 1_555 Q XYP . O4 ? ? D XYP 203 D XYP 204 1_555 ? ? ? ? ? ? ? 1.376 ?    ? 
covale4  covale both ? E XYP .   O4  ? ? ? 1_555 E XYP . C1 ? ? E XYP 1   E XYP 2   1_555 ? ? ? ? ? ? ? 1.397 sing ? 
metalc1  metalc ?    ? A PHE 104 O   ? ? ? 1_555 G ZN  . ZN ? ? A PHE 92  A ZN  301 1_555 ? ? ? ? ? ? ? 2.422 ?    ? 
metalc2  metalc ?    ? A ASP 154 OD1 ? ? ? 1_555 F ZN  . ZN ? ? A ASP 142 A ZN  300 1_555 ? ? ? ? ? ? ? 2.548 ?    ? 
metalc3  metalc ?    ? A ASP 154 OD2 ? ? ? 1_555 F ZN  . ZN ? ? A ASP 142 A ZN  300 1_555 ? ? ? ? ? ? ? 2.580 ?    ? 
metalc4  metalc ?    ? A HIS 155 ND1 ? ? ? 1_555 G ZN  . ZN ? ? A HIS 143 A ZN  301 1_555 ? ? ? ? ? ? ? 1.964 ?    ? 
metalc5  metalc ?    ? F ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  300 A HOH 537 1_555 ? ? ? ? ? ? ? 2.355 ?    ? 
metalc6  metalc ?    ? F ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? A ZN  300 B HOH 312 1_554 ? ? ? ? ? ? ? 2.218 ?    ? 
metalc7  metalc ?    ? F ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? A ZN  300 B HOH 328 1_554 ? ? ? ? ? ? ? 2.338 ?    ? 
metalc8  metalc ?    ? F ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? A ZN  300 B HOH 430 1_554 ? ? ? ? ? ? ? 2.484 ?    ? 
metalc9  metalc ?    ? G ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  301 A HOH 467 1_555 ? ? ? ? ? ? ? 2.235 ?    ? 
metalc10 metalc ?    ? G ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  301 A HOH 526 1_555 ? ? ? ? ? ? ? 2.047 ?    ? 
metalc11 metalc ?    ? G ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  301 A HOH 552 1_555 ? ? ? ? ? ? ? 2.201 ?    ? 
metalc12 metalc ?    ? R HOH .   O   ? ? ? 1_455 H ZN  . ZN ? ? A HOH 411 B ZN  201 1_555 ? ? ? ? ? ? ? 2.215 ?    ? 
metalc13 metalc ?    ? R HOH .   O   ? ? ? 1_455 H ZN  . ZN ? ? A HOH 412 B ZN  201 1_555 ? ? ? ? ? ? ? 2.434 ?    ? 
metalc14 metalc ?    ? B PHE 104 O   ? ? ? 1_555 I ZN  . ZN ? ? B PHE 92  B ZN  202 1_555 ? ? ? ? ? ? ? 2.629 ?    ? 
metalc15 metalc ?    ? B ASP 154 OD1 ? ? ? 1_555 H ZN  . ZN ? ? B ASP 142 B ZN  201 1_555 ? ? ? ? ? ? ? 2.682 ?    ? 
metalc16 metalc ?    ? B ASP 154 OD2 ? ? ? 1_555 H ZN  . ZN ? ? B ASP 142 B ZN  201 1_555 ? ? ? ? ? ? ? 2.325 ?    ? 
metalc17 metalc ?    ? B HIS 155 ND1 ? ? ? 1_555 I ZN  . ZN ? ? B HIS 143 B ZN  202 1_555 ? ? ? ? ? ? ? 2.105 ?    ? 
metalc18 metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? B ZN  202 B HOH 392 1_555 ? ? ? ? ? ? ? 2.378 ?    ? 
metalc19 metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? B ZN  202 B HOH 449 1_555 ? ? ? ? ? ? ? 2.234 ?    ? 
metalc20 metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? B ZN  202 B HOH 451 1_555 ? ? ? ? ? ? ? 2.111 ?    ? 
metalc21 metalc ?    ? T HOH .   O   ? ? ? 1_556 N ZN  . ZN ? ? C HOH 308 D ZN  201 1_555 ? ? ? ? ? ? ? 2.222 ?    ? 
metalc22 metalc ?    ? T HOH .   O   ? ? ? 1_556 N ZN  . ZN ? ? C HOH 329 D ZN  201 1_555 ? ? ? ? ? ? ? 2.531 ?    ? 
metalc23 metalc ?    ? T HOH .   O   ? ? ? 1_556 N ZN  . ZN ? ? C HOH 452 D ZN  201 1_555 ? ? ? ? ? ? ? 2.522 ?    ? 
metalc24 metalc ?    ? D PHE 104 O   ? ? ? 1_555 O ZN  . ZN ? ? D PHE 92  D ZN  202 1_555 ? ? ? ? ? ? ? 2.392 ?    ? 
metalc25 metalc ?    ? D ASP 154 OD1 ? ? ? 1_555 N ZN  . ZN ? ? D ASP 142 D ZN  201 1_555 ? ? ? ? ? ? ? 2.502 ?    ? 
metalc26 metalc ?    ? D HIS 155 ND1 ? ? ? 1_555 O ZN  . ZN ? ? D HIS 143 D ZN  202 1_555 ? ? ? ? ? ? ? 1.995 ?    ? 
metalc27 metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 U HOH . O  ? ? D ZN  201 D HOH 301 1_555 ? ? ? ? ? ? ? 1.742 ?    ? 
metalc28 metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 U HOH . O  ? ? D ZN  201 D HOH 441 1_555 ? ? ? ? ? ? ? 2.282 ?    ? 
metalc29 metalc ?    ? O ZN  .   ZN  ? ? ? 1_555 U HOH . O  ? ? D ZN  202 D HOH 315 1_555 ? ? ? ? ? ? ? 2.213 ?    ? 
metalc30 metalc ?    ? O ZN  .   ZN  ? ? ? 1_555 U HOH . O  ? ? D ZN  202 D HOH 374 1_555 ? ? ? ? ? ? ? 2.070 ?    ? 
metalc31 metalc ?    ? O ZN  .   ZN  ? ? ? 1_555 U HOH . O  ? ? D ZN  202 D HOH 430 1_555 ? ? ? ? ? ? ? 2.148 ?    ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 PHE 104 ? A PHE 92  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 155 ? A HIS 143 ? 1_555 90.3  ? 
2  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 467 ? 1_555 75.2  ? 
3  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 467 ? 1_555 109.9 ? 
4  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 526 ? 1_555 173.0 ? 
5  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 526 ? 1_555 95.5  ? 
6  O   ? R HOH .   ? A HOH 467 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 526 ? 1_555 99.1  ? 
7  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 552 ? 1_555 85.2  ? 
8  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 552 ? 1_555 117.8 ? 
9  O   ? R HOH .   ? A HOH 467 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 552 ? 1_555 128.2 ? 
10 O   ? R HOH .   ? A HOH 526 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O   ? R HOH .   ? A HOH 552 ? 1_555 95.4  ? 
11 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 50.7  ? 
12 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? R HOH .   ? A HOH 537 ? 1_555 82.1  ? 
13 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? R HOH .   ? A HOH 537 ? 1_555 75.0  ? 
14 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 312 ? 1_554 94.8  ? 
15 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 312 ? 1_554 110.3 ? 
16 O   ? R HOH .   ? A HOH 537 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 312 ? 1_554 170.2 ? 
17 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 328 ? 1_554 120.9 ? 
18 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 328 ? 1_554 75.8  ? 
19 O   ? R HOH .   ? A HOH 537 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 328 ? 1_554 109.3 ? 
20 O   ? S HOH .   ? B HOH 312 ? 1_554 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 328 ? 1_554 80.3  ? 
21 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 430 ? 1_554 128.9 ? 
22 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 430 ? 1_554 161.7 ? 
23 O   ? R HOH .   ? A HOH 537 ? 1_555 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 430 ? 1_554 86.8  ? 
24 O   ? S HOH .   ? B HOH 312 ? 1_554 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 430 ? 1_554 88.0  ? 
25 O   ? S HOH .   ? B HOH 328 ? 1_554 ZN ? F ZN . ? A ZN 300 ? 1_555 O   ? S HOH .   ? B HOH 430 ? 1_554 109.8 ? 
26 O   ? R HOH .   ? A HOH 411 ? 1_455 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? R HOH .   ? A HOH 412 ? 1_455 67.7  ? 
27 O   ? R HOH .   ? A HOH 411 ? 1_455 ZN ? H ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 88.6  ? 
28 O   ? R HOH .   ? A HOH 412 ? 1_455 ZN ? H ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 61.5  ? 
29 O   ? R HOH .   ? A HOH 411 ? 1_455 ZN ? H ZN . ? B ZN 201 ? 1_555 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 102.3 ? 
30 O   ? R HOH .   ? A HOH 412 ? 1_455 ZN ? H ZN . ? B ZN 201 ? 1_555 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 112.5 ? 
31 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 51.4  ? 
32 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 86.4  ? 
33 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 392 ? 1_555 73.8  ? 
34 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 392 ? 1_555 103.5 ? 
35 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 449 ? 1_555 80.9  ? 
36 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 449 ? 1_555 113.2 ? 
37 O   ? S HOH .   ? B HOH 392 ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 449 ? 1_555 133.6 ? 
38 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 451 ? 1_555 172.5 ? 
39 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 451 ? 1_555 99.1  ? 
40 O   ? S HOH .   ? B HOH 392 ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 451 ? 1_555 99.8  ? 
41 O   ? S HOH .   ? B HOH 449 ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 O   ? S HOH .   ? B HOH 451 ? 1_555 101.5 ? 
42 O   ? T HOH .   ? C HOH 308 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? T HOH .   ? C HOH 329 ? 1_556 88.0  ? 
43 O   ? T HOH .   ? C HOH 308 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? T HOH .   ? C HOH 452 ? 1_556 94.5  ? 
44 O   ? T HOH .   ? C HOH 329 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? T HOH .   ? C HOH 452 ? 1_556 114.9 ? 
45 O   ? T HOH .   ? C HOH 308 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 95.1  ? 
46 O   ? T HOH .   ? C HOH 329 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 120.6 ? 
47 O   ? T HOH .   ? C HOH 452 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 123.9 ? 
48 O   ? T HOH .   ? C HOH 308 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 301 ? 1_555 92.0  ? 
49 O   ? T HOH .   ? C HOH 329 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 301 ? 1_555 177.3 ? 
50 O   ? T HOH .   ? C HOH 452 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 301 ? 1_555 67.8  ? 
51 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 301 ? 1_555 56.7  ? 
52 O   ? T HOH .   ? C HOH 308 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 441 ? 1_555 176.5 ? 
53 O   ? T HOH .   ? C HOH 329 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 441 ? 1_555 89.0  ? 
54 O   ? T HOH .   ? C HOH 452 ? 1_556 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 441 ? 1_555 85.2  ? 
55 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 441 ? 1_555 87.9  ? 
56 O   ? U HOH .   ? D HOH 301 ? 1_555 ZN ? N ZN . ? D ZN 201 ? 1_555 O   ? U HOH .   ? D HOH 441 ? 1_555 91.1  ? 
57 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 91.3  ? 
58 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 315 ? 1_555 74.4  ? 
59 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 315 ? 1_555 109.3 ? 
60 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 374 ? 1_555 169.1 ? 
61 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 374 ? 1_555 87.7  ? 
62 O   ? U HOH .   ? D HOH 315 ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 374 ? 1_555 95.7  ? 
63 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 430 ? 1_555 84.9  ? 
64 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 430 ? 1_555 121.1 ? 
65 O   ? U HOH .   ? D HOH 315 ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 430 ? 1_555 125.6 ? 
66 O   ? U HOH .   ? D HOH 374 ? 1_555 ZN ? O ZN . ? D ZN 202 ? 1_555 O   ? U HOH .   ? D HOH 430 ? 1_555 104.9 ? 
# 
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 ASN 64 A . ? ASN 52 A PRO 65 A ? PRO 53 A 1 2.56  
2 ASN 93 A . ? ASN 81 A PRO 94 A ? PRO 82 A 1 6.32  
3 ASN 64 B . ? ASN 52 B PRO 65 B ? PRO 53 B 1 -4.40 
4 ASN 93 B . ? ASN 81 B PRO 94 B ? PRO 82 B 1 4.44  
5 ASN 64 C . ? ASN 52 C PRO 65 C ? PRO 53 C 1 -3.87 
6 ASN 93 C . ? ASN 81 C PRO 94 C ? PRO 82 C 1 4.97  
7 ASN 64 D . ? ASN 52 D PRO 65 D ? PRO 53 D 1 -0.07 
8 ASN 93 D . ? ASN 81 D PRO 94 D ? PRO 82 D 1 3.60  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 5 ? 
AA3 ? 9 ? 
AA4 ? 5 ? 
AA5 ? 9 ? 
AA6 ? 5 ? 
AA7 ? 6 ? 
AA8 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? parallel      
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? parallel      
AA5 7 8 ? anti-parallel 
AA5 8 9 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? parallel      
AA8 7 8 ? anti-parallel 
AA8 8 9 ? 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 GLU A 18  ? ASN A 22  ? GLU A 6   ASN A 10  
AA1 2 TYR A 25  ? THR A 31  ? TYR A 13  THR A 19  
AA1 3 ASN A 56  ? TRP A 63  ? ASN A 44  TRP A 51  
AA1 4 THR A 179 ? TYR A 190 ? THR A 167 TYR A 178 
AA1 5 SER A 83  ? GLN A 92  ? SER A 71  GLN A 80  
AA1 6 VAL A 96  ? PHE A 104 ? VAL A 84  PHE A 92  
AA1 7 ALA A 143 ? ARG A 152 ? ALA A 131 ARG A 140 
AA1 8 GLY A 124 ? ALA A 136 ? GLY A 112 ALA A 124 
AA1 9 GLU A 115 ? THR A 121 ? GLU A 103 THR A 109 
AA2 1 GLN A 36  ? ASN A 41  ? GLN A 24  ASN A 29  
AA2 2 GLN A 46  ? SER A 52  ? GLN A 34  SER A 40  
AA2 3 SER A 193 ? VAL A 200 ? SER A 181 VAL A 188 
AA2 4 THR A 70  ? ASN A 80  ? THR A 58  ASN A 68  
AA2 5 GLY A 159 ? THR A 162 ? GLY A 147 THR A 150 
AA3 1 GLU B 18  ? ASN B 22  ? GLU B 6   ASN B 10  
AA3 2 TYR B 25  ? THR B 31  ? TYR B 13  THR B 19  
AA3 3 ASN B 56  ? TRP B 63  ? ASN B 44  TRP B 51  
AA3 4 THR B 179 ? TYR B 190 ? THR B 167 TYR B 178 
AA3 5 SER B 83  ? GLN B 92  ? SER B 71  GLN B 80  
AA3 6 VAL B 96  ? PHE B 104 ? VAL B 84  PHE B 92  
AA3 7 ALA B 143 ? ARG B 152 ? ALA B 131 ARG B 140 
AA3 8 GLY B 124 ? ALA B 136 ? GLY B 112 ALA B 124 
AA3 9 GLN B 114 ? THR B 121 ? GLN B 102 THR B 109 
AA4 1 GLN B 36  ? ASN B 41  ? GLN B 24  ASN B 29  
AA4 2 GLN B 46  ? SER B 52  ? GLN B 34  SER B 40  
AA4 3 SER B 193 ? VAL B 200 ? SER B 181 VAL B 188 
AA4 4 THR B 70  ? ASN B 80  ? THR B 58  ASN B 68  
AA4 5 GLY B 159 ? THR B 162 ? GLY B 147 THR B 150 
AA5 1 GLU C 18  ? ASN C 22  ? GLU C 6   ASN C 10  
AA5 2 TYR C 25  ? THR C 31  ? TYR C 13  THR C 19  
AA5 3 PHE C 57  ? TRP C 63  ? PHE C 45  TRP C 51  
AA5 4 THR C 179 ? GLY C 189 ? THR C 167 GLY C 177 
AA5 5 SER C 83  ? GLN C 92  ? SER C 71  GLN C 80  
AA5 6 VAL C 96  ? PHE C 104 ? VAL C 84  PHE C 92  
AA5 7 ALA C 143 ? ARG C 152 ? ALA C 131 ARG C 140 
AA5 8 GLY C 124 ? ALA C 136 ? GLY C 112 ALA C 124 
AA5 9 GLN C 114 ? THR C 121 ? GLN C 102 THR C 109 
AA6 1 GLN C 36  ? ASN C 41  ? GLN C 24  ASN C 29  
AA6 2 GLN C 46  ? SER C 52  ? GLN C 34  SER C 40  
AA6 3 SER C 193 ? VAL C 200 ? SER C 181 VAL C 188 
AA6 4 THR C 70  ? ASN C 80  ? THR C 58  ASN C 68  
AA6 5 GLY C 159 ? THR C 162 ? GLY C 147 THR C 150 
AA7 1 GLU D 13  ? ILE D 14  ? GLU D 1   ILE D 2   
AA7 2 GLN D 36  ? ASN D 41  ? GLN D 24  ASN D 29  
AA7 3 GLN D 46  ? SER D 52  ? GLN D 34  SER D 40  
AA7 4 SER D 193 ? VAL D 200 ? SER D 181 VAL D 188 
AA7 5 THR D 70  ? ASN D 80  ? THR D 58  ASN D 68  
AA7 6 GLY D 159 ? THR D 162 ? GLY D 147 THR D 150 
AA8 1 GLU D 18  ? ASN D 22  ? GLU D 6   ASN D 10  
AA8 2 TYR D 25  ? THR D 31  ? TYR D 13  THR D 19  
AA8 3 ASN D 56  ? TRP D 63  ? ASN D 44  TRP D 51  
AA8 4 THR D 179 ? TYR D 190 ? THR D 167 TYR D 178 
AA8 5 SER D 83  ? GLN D 92  ? SER D 71  GLN D 80  
AA8 6 VAL D 96  ? PHE D 104 ? VAL D 84  PHE D 92  
AA8 7 ALA D 143 ? ARG D 152 ? ALA D 131 ARG D 140 
AA8 8 GLY D 124 ? ALA D 136 ? GLY D 112 ALA D 124 
AA8 9 GLU D 115 ? THR D 121 ? GLU D 103 THR D 109 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASN A 22  ? N ASN A 10  O TYR A 25  ? O TYR A 13  
AA1 2 3 N TYR A 26  ? N TYR A 14  O GLY A 62  ? O GLY A 50  
AA1 3 4 N ALA A 59  ? N ALA A 47  O THR A 187 ? O THR A 175 
AA1 4 5 O ILE A 184 ? O ILE A 172 N TYR A 88  ? N TYR A 76  
AA1 5 6 N VAL A 87  ? N VAL A 75  O ILE A 100 ? O ILE A 88  
AA1 6 7 N VAL A 101 ? N VAL A 89  O SER A 150 ? O SER A 138 
AA1 7 8 O ALA A 143 ? O ALA A 131 N ALA A 136 ? N ALA A 124 
AA1 8 9 O ILE A 128 ? O ILE A 116 N LEU A 116 ? N LEU A 104 
AA2 1 2 N THR A 38  ? N THR A 26  O GLU A 50  ? O GLU A 38  
AA2 2 3 N TRP A 51  ? N TRP A 39  O GLY A 194 ? O GLY A 182 
AA2 3 4 O SER A 193 ? O SER A 181 N ASN A 80  ? N ASN A 68  
AA2 4 5 N ILE A 71  ? N ILE A 59  O VAL A 161 ? O VAL A 149 
AA3 1 2 N GLU B 18  ? N GLU B 6   O PHE B 29  ? O PHE B 17  
AA3 2 3 N TYR B 26  ? N TYR B 14  O GLY B 62  ? O GLY B 50  
AA3 3 4 N ALA B 59  ? N ALA B 47  O THR B 187 ? O THR B 175 
AA3 4 5 O ASN B 181 ? O ASN B 169 N TRP B 90  ? N TRP B 78  
AA3 5 6 N VAL B 87  ? N VAL B 75  O ILE B 100 ? O ILE B 88  
AA3 6 7 N VAL B 101 ? N VAL B 89  O SER B 150 ? O SER B 138 
AA3 7 8 O ALA B 143 ? O ALA B 131 N ALA B 136 ? N ALA B 124 
AA3 8 9 O ILE B 128 ? O ILE B 116 N LEU B 116 ? N LEU B 104 
AA4 1 2 N THR B 38  ? N THR B 26  O GLU B 50  ? O GLU B 38  
AA4 2 3 N TRP B 51  ? N TRP B 39  O GLY B 194 ? O GLY B 182 
AA4 3 4 O SER B 193 ? O SER B 181 N ASN B 80  ? N ASN B 68  
AA4 4 5 N ILE B 71  ? N ILE B 59  O VAL B 161 ? O VAL B 149 
AA5 1 2 N ASN C 22  ? N ASN C 10  O TYR C 25  ? O TYR C 13  
AA5 2 3 N TYR C 26  ? N TYR C 14  O GLY C 62  ? O GLY C 50  
AA5 3 4 N ALA C 59  ? N ALA C 47  O THR C 187 ? O THR C 175 
AA5 4 5 O ILE C 184 ? O ILE C 172 N TYR C 88  ? N TYR C 76  
AA5 5 6 N VAL C 87  ? N VAL C 75  O ILE C 100 ? O ILE C 88  
AA5 6 7 N VAL C 101 ? N VAL C 89  O SER C 150 ? O SER C 138 
AA5 7 8 O ALA C 143 ? O ALA C 131 N ALA C 136 ? N ALA C 124 
AA5 8 9 O ILE C 128 ? O ILE C 116 N LEU C 116 ? N LEU C 104 
AA6 1 2 N THR C 38  ? N THR C 26  O GLU C 50  ? O GLU C 38  
AA6 2 3 N TRP C 51  ? N TRP C 39  O GLY C 194 ? O GLY C 182 
AA6 3 4 O THR C 199 ? O THR C 187 N SER C 74  ? N SER C 62  
AA6 4 5 N ILE C 71  ? N ILE C 59  O VAL C 161 ? O VAL C 149 
AA7 1 2 N ILE D 14  ? N ILE D 2   O TYR D 39  ? O TYR D 27  
AA7 2 3 N THR D 38  ? N THR D 26  O GLU D 50  ? O GLU D 38  
AA7 3 4 N TRP D 51  ? N TRP D 39  O GLY D 194 ? O GLY D 182 
AA7 4 5 O SER D 193 ? O SER D 181 N ASN D 80  ? N ASN D 68  
AA7 5 6 N ILE D 71  ? N ILE D 59  O VAL D 161 ? O VAL D 149 
AA8 1 2 N ASN D 22  ? N ASN D 10  O TYR D 25  ? O TYR D 13  
AA8 2 3 N TRP D 30  ? N TRP D 18  O VAL D 58  ? O VAL D 46  
AA8 3 4 N TRP D 63  ? N TRP D 51  O MET D 183 ? O MET D 171 
AA8 4 5 O ALA D 186 ? O ALA D 174 N SER D 86  ? N SER D 74  
AA8 5 6 N VAL D 87  ? N VAL D 75  O ILE D 100 ? O ILE D 88  
AA8 6 7 N VAL D 101 ? N VAL D 89  O SER D 150 ? O SER D 138 
AA8 7 8 O PHE D 145 ? O PHE D 133 N ARG D 133 ? N ARG D 121 
AA8 8 9 O ILE D 128 ? O ILE D 116 N LEU D 116 ? N LEU D 104 
# 
_pdbx_entry_details.entry_id                   8XZZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 ZN  A ZN  300 ? ? O  A HOH 402 ? ? 1.67 
2  1 O   C HOH 409 ? ? O  C HOH 441 ? ? 1.95 
3  1 NZ  B LYS 115 ? ? O  B HOH 301 ? ? 2.00 
4  1 OE1 B GLU 164 ? ? O  B HOH 302 ? ? 2.00 
5  1 O   B HOH 323 ? ? O  B HOH 389 ? ? 2.00 
6  1 O   C HOH 441 ? ? O  C HOH 457 ? ? 2.01 
7  1 OD2 B ASP 111 ? ? O  B HOH 303 ? ? 2.03 
8  1 O   A THR 99  ? ? O  A HOH 401 ? ? 2.03 
9  1 O   A HOH 556 ? ? O  A HOH 563 ? ? 2.04 
10 1 O   C HOH 365 ? ? O  C HOH 455 ? ? 2.05 
11 1 O4  C XYP 201 ? ? O5 C XYP 202 ? ? 2.07 
12 1 O   A HOH 431 ? ? O  A HOH 566 ? ? 2.08 
13 1 O   D HOH 326 ? ? O  D HOH 432 ? ? 2.08 
14 1 O5  B XYP 203 ? ? O4 B XYP 204 ? ? 2.10 
15 1 O   B HOH 479 ? ? O  B HOH 484 ? ? 2.11 
16 1 O   A HOH 431 ? ? O  A HOH 466 ? ? 2.12 
17 1 OD1 D ASP 142 ? ? O  D HOH 301 ? ? 2.12 
18 1 O   C HOH 379 ? ? O  D HOH 425 ? ? 2.14 
19 1 OE1 D GLN 179 ? ? O  D HOH 302 ? ? 2.14 
20 1 O5  D XYP 203 ? ? O4 D XYP 204 ? ? 2.14 
21 1 O   C HOH 303 ? ? O  C HOH 440 ? ? 2.15 
22 1 O   C HOH 382 ? ? O  C HOH 453 ? ? 2.15 
23 1 OD1 A ASP 142 ? ? O  A HOH 402 ? ? 2.15 
24 1 O   D HOH 428 ? ? O  D HOH 452 ? ? 2.16 
25 1 O   C HOH 417 ? ? O  D HOH 463 ? ? 2.17 
26 1 O   A HOH 407 ? ? O  A HOH 421 ? ? 2.18 
27 1 OE1 C GLU 38  ? ? O  C HOH 301 ? ? 2.19 
28 1 O   D HOH 347 ? ? O  D HOH 382 ? ? 2.19 
29 1 O   B HOH 387 ? ? O  B HOH 484 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 421 ? ? 1_555 O B HOH 302 ? ? 1_554 1.95 
2 1 O   A HOH 403 ? ? 1_555 O B HOH 305 ? ? 1_655 1.98 
3 1 O   B HOH 474 ? ? 1_555 O C HOH 377 ? ? 1_556 2.00 
4 1 O   A HOH 477 ? ? 1_555 O B HOH 362 ? ? 1_554 2.04 
5 1 OE2 A GLU 64  ? ? 1_555 O B HOH 302 ? ? 1_554 2.05 
6 1 O   A HOH 421 ? ? 1_555 O B HOH 480 ? ? 1_554 2.18 
7 1 O   B HOH 455 ? ? 1_555 O C HOH 365 ? ? 1_556 2.18 
# 
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 ALA A 32  ? ? 52.81   -128.16 
2  1 SER A 93  ? ? -99.19  -84.84  
3  1 ASN A 169 ? ? -103.47 -139.10 
4  1 ALA B 32  ? ? 53.51   -128.59 
5  1 SER B 93  ? ? -96.50  -87.85  
6  1 ASN B 169 ? ? -100.66 -137.25 
7  1 ALA C 32  ? ? 49.83   -127.37 
8  1 SER C 93  ? ? -99.83  -86.76  
9  1 ASN C 169 ? ? -101.78 -135.43 
10 1 ALA D 32  ? ? 51.83   -127.61 
11 1 SER D 93  ? ? -98.39  -91.26  
12 1 ASN D 169 ? ? -97.83  -139.21 
# 
_pdbx_molecule_features.prd_id    PRD_900116 
_pdbx_molecule_features.name      4beta-beta-xylobiose 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     Metabolism 
_pdbx_molecule_features.details   oligosaccharide 
# 
_pdbx_molecule.instance_id   1 
_pdbx_molecule.prd_id        PRD_900116 
_pdbx_molecule.asym_id       E 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       594 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   8.06 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -11 ? A GLY 1  
2  1 Y 1 A ALA -10 ? A ALA 2  
3  1 Y 1 A GLY -9  ? A GLY 3  
4  1 Y 1 A ALA -8  ? A ALA 4  
5  1 Y 1 A GLY -7  ? A GLY 5  
6  1 Y 1 B GLY -11 ? B GLY 1  
7  1 Y 1 B ALA -10 ? B ALA 2  
8  1 Y 1 B GLY -9  ? B GLY 3  
9  1 Y 1 B ALA -8  ? B ALA 4  
10 1 Y 1 B GLY -7  ? B GLY 5  
11 1 Y 1 B ALA -6  ? B ALA 6  
12 1 Y 1 B GLY -5  ? B GLY 7  
13 1 Y 1 B ALA -4  ? B ALA 8  
14 1 Y 1 B GLY -3  ? B GLY 9  
15 1 Y 1 B ALA -2  ? B ALA 10 
16 1 Y 1 B GLY -1  ? B GLY 11 
17 1 Y 1 C GLY -11 ? C GLY 1  
18 1 Y 1 C ALA -10 ? C ALA 2  
19 1 Y 1 C GLY -9  ? C GLY 3  
20 1 Y 1 C ALA -8  ? C ALA 4  
21 1 Y 1 C GLY -7  ? C GLY 5  
22 1 Y 1 C ALA -6  ? C ALA 6  
23 1 Y 1 C GLY -5  ? C GLY 7  
24 1 Y 1 C ALA -4  ? C ALA 8  
25 1 Y 1 C GLY -3  ? C GLY 9  
26 1 Y 1 C ALA -2  ? C ALA 10 
27 1 Y 1 C GLY -1  ? C GLY 11 
28 1 Y 1 C MET 0   ? C MET 12 
29 1 Y 1 D GLY -11 ? D GLY 1  
30 1 Y 1 D ALA -10 ? D ALA 2  
31 1 Y 1 D GLY -9  ? D GLY 3  
32 1 Y 1 D ALA -8  ? D ALA 4  
33 1 Y 1 D GLY -7  ? D GLY 5  
34 1 Y 1 D ALA -6  ? D ALA 6  
35 1 Y 1 D GLY -5  ? D GLY 7  
36 1 Y 1 D ALA -4  ? D ALA 8  
37 1 Y 1 D GLY -3  ? D GLY 9  
38 1 Y 1 D ALA -2  ? D ALA 10 
39 1 Y 1 D GLY -1  ? D GLY 11 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
GLN N    N  N N 74  
GLN CA   C  N S 75  
GLN C    C  N N 76  
GLN O    O  N N 77  
GLN CB   C  N N 78  
GLN CG   C  N N 79  
GLN CD   C  N N 80  
GLN OE1  O  N N 81  
GLN NE2  N  N N 82  
GLN OXT  O  N N 83  
GLN H    H  N N 84  
GLN H2   H  N N 85  
GLN HA   H  N N 86  
GLN HB2  H  N N 87  
GLN HB3  H  N N 88  
GLN HG2  H  N N 89  
GLN HG3  H  N N 90  
GLN HE21 H  N N 91  
GLN HE22 H  N N 92  
GLN HXT  H  N N 93  
GLU N    N  N N 94  
GLU CA   C  N S 95  
GLU C    C  N N 96  
GLU O    O  N N 97  
GLU CB   C  N N 98  
GLU CG   C  N N 99  
GLU CD   C  N N 100 
GLU OE1  O  N N 101 
GLU OE2  O  N N 102 
GLU OXT  O  N N 103 
GLU H    H  N N 104 
GLU H2   H  N N 105 
GLU HA   H  N N 106 
GLU HB2  H  N N 107 
GLU HB3  H  N N 108 
GLU HG2  H  N N 109 
GLU HG3  H  N N 110 
GLU HE2  H  N N 111 
GLU HXT  H  N N 112 
GLY N    N  N N 113 
GLY CA   C  N N 114 
GLY C    C  N N 115 
GLY O    O  N N 116 
GLY OXT  O  N N 117 
GLY H    H  N N 118 
GLY H2   H  N N 119 
GLY HA2  H  N N 120 
GLY HA3  H  N N 121 
GLY HXT  H  N N 122 
HIS N    N  N N 123 
HIS CA   C  N S 124 
HIS C    C  N N 125 
HIS O    O  N N 126 
HIS CB   C  N N 127 
HIS CG   C  Y N 128 
HIS ND1  N  Y N 129 
HIS CD2  C  Y N 130 
HIS CE1  C  Y N 131 
HIS NE2  N  Y N 132 
HIS OXT  O  N N 133 
HIS H    H  N N 134 
HIS H2   H  N N 135 
HIS HA   H  N N 136 
HIS HB2  H  N N 137 
HIS HB3  H  N N 138 
HIS HD1  H  N N 139 
HIS HD2  H  N N 140 
HIS HE1  H  N N 141 
HIS HE2  H  N N 142 
HIS HXT  H  N N 143 
HOH O    O  N N 144 
HOH H1   H  N N 145 
HOH H2   H  N N 146 
ILE N    N  N N 147 
ILE CA   C  N S 148 
ILE C    C  N N 149 
ILE O    O  N N 150 
ILE CB   C  N S 151 
ILE CG1  C  N N 152 
ILE CG2  C  N N 153 
ILE CD1  C  N N 154 
ILE OXT  O  N N 155 
ILE H    H  N N 156 
ILE H2   H  N N 157 
ILE HA   H  N N 158 
ILE HB   H  N N 159 
ILE HG12 H  N N 160 
ILE HG13 H  N N 161 
ILE HG21 H  N N 162 
ILE HG22 H  N N 163 
ILE HG23 H  N N 164 
ILE HD11 H  N N 165 
ILE HD12 H  N N 166 
ILE HD13 H  N N 167 
ILE HXT  H  N N 168 
LEU N    N  N N 169 
LEU CA   C  N S 170 
LEU C    C  N N 171 
LEU O    O  N N 172 
LEU CB   C  N N 173 
LEU CG   C  N N 174 
LEU CD1  C  N N 175 
LEU CD2  C  N N 176 
LEU OXT  O  N N 177 
LEU H    H  N N 178 
LEU H2   H  N N 179 
LEU HA   H  N N 180 
LEU HB2  H  N N 181 
LEU HB3  H  N N 182 
LEU HG   H  N N 183 
LEU HD11 H  N N 184 
LEU HD12 H  N N 185 
LEU HD13 H  N N 186 
LEU HD21 H  N N 187 
LEU HD22 H  N N 188 
LEU HD23 H  N N 189 
LEU HXT  H  N N 190 
LYS N    N  N N 191 
LYS CA   C  N S 192 
LYS C    C  N N 193 
LYS O    O  N N 194 
LYS CB   C  N N 195 
LYS CG   C  N N 196 
LYS CD   C  N N 197 
LYS CE   C  N N 198 
LYS NZ   N  N N 199 
LYS OXT  O  N N 200 
LYS H    H  N N 201 
LYS H2   H  N N 202 
LYS HA   H  N N 203 
LYS HB2  H  N N 204 
LYS HB3  H  N N 205 
LYS HG2  H  N N 206 
LYS HG3  H  N N 207 
LYS HD2  H  N N 208 
LYS HD3  H  N N 209 
LYS HE2  H  N N 210 
LYS HE3  H  N N 211 
LYS HZ1  H  N N 212 
LYS HZ2  H  N N 213 
LYS HZ3  H  N N 214 
LYS HXT  H  N N 215 
MET N    N  N N 216 
MET CA   C  N S 217 
MET C    C  N N 218 
MET O    O  N N 219 
MET CB   C  N N 220 
MET CG   C  N N 221 
MET SD   S  N N 222 
MET CE   C  N N 223 
MET OXT  O  N N 224 
MET H    H  N N 225 
MET H2   H  N N 226 
MET HA   H  N N 227 
MET HB2  H  N N 228 
MET HB3  H  N N 229 
MET HG2  H  N N 230 
MET HG3  H  N N 231 
MET HE1  H  N N 232 
MET HE2  H  N N 233 
MET HE3  H  N N 234 
MET HXT  H  N N 235 
PHE N    N  N N 236 
PHE CA   C  N S 237 
PHE C    C  N N 238 
PHE O    O  N N 239 
PHE CB   C  N N 240 
PHE CG   C  Y N 241 
PHE CD1  C  Y N 242 
PHE CD2  C  Y N 243 
PHE CE1  C  Y N 244 
PHE CE2  C  Y N 245 
PHE CZ   C  Y N 246 
PHE OXT  O  N N 247 
PHE H    H  N N 248 
PHE H2   H  N N 249 
PHE HA   H  N N 250 
PHE HB2  H  N N 251 
PHE HB3  H  N N 252 
PHE HD1  H  N N 253 
PHE HD2  H  N N 254 
PHE HE1  H  N N 255 
PHE HE2  H  N N 256 
PHE HZ   H  N N 257 
PHE HXT  H  N N 258 
PRO N    N  N N 259 
PRO CA   C  N S 260 
PRO C    C  N N 261 
PRO O    O  N N 262 
PRO CB   C  N N 263 
PRO CG   C  N N 264 
PRO CD   C  N N 265 
PRO OXT  O  N N 266 
PRO H    H  N N 267 
PRO HA   H  N N 268 
PRO HB2  H  N N 269 
PRO HB3  H  N N 270 
PRO HG2  H  N N 271 
PRO HG3  H  N N 272 
PRO HD2  H  N N 273 
PRO HD3  H  N N 274 
PRO HXT  H  N N 275 
SER N    N  N N 276 
SER CA   C  N S 277 
SER C    C  N N 278 
SER O    O  N N 279 
SER CB   C  N N 280 
SER OG   O  N N 281 
SER OXT  O  N N 282 
SER H    H  N N 283 
SER H2   H  N N 284 
SER HA   H  N N 285 
SER HB2  H  N N 286 
SER HB3  H  N N 287 
SER HG   H  N N 288 
SER HXT  H  N N 289 
THR N    N  N N 290 
THR CA   C  N S 291 
THR C    C  N N 292 
THR O    O  N N 293 
THR CB   C  N R 294 
THR OG1  O  N N 295 
THR CG2  C  N N 296 
THR OXT  O  N N 297 
THR H    H  N N 298 
THR H2   H  N N 299 
THR HA   H  N N 300 
THR HB   H  N N 301 
THR HG1  H  N N 302 
THR HG21 H  N N 303 
THR HG22 H  N N 304 
THR HG23 H  N N 305 
THR HXT  H  N N 306 
TRP N    N  N N 307 
TRP CA   C  N S 308 
TRP C    C  N N 309 
TRP O    O  N N 310 
TRP CB   C  N N 311 
TRP CG   C  Y N 312 
TRP CD1  C  Y N 313 
TRP CD2  C  Y N 314 
TRP NE1  N  Y N 315 
TRP CE2  C  Y N 316 
TRP CE3  C  Y N 317 
TRP CZ2  C  Y N 318 
TRP CZ3  C  Y N 319 
TRP CH2  C  Y N 320 
TRP OXT  O  N N 321 
TRP H    H  N N 322 
TRP H2   H  N N 323 
TRP HA   H  N N 324 
TRP HB2  H  N N 325 
TRP HB3  H  N N 326 
TRP HD1  H  N N 327 
TRP HE1  H  N N 328 
TRP HE3  H  N N 329 
TRP HZ2  H  N N 330 
TRP HZ3  H  N N 331 
TRP HH2  H  N N 332 
TRP HXT  H  N N 333 
TYR N    N  N N 334 
TYR CA   C  N S 335 
TYR C    C  N N 336 
TYR O    O  N N 337 
TYR CB   C  N N 338 
TYR CG   C  Y N 339 
TYR CD1  C  Y N 340 
TYR CD2  C  Y N 341 
TYR CE1  C  Y N 342 
TYR CE2  C  Y N 343 
TYR CZ   C  Y N 344 
TYR OH   O  N N 345 
TYR OXT  O  N N 346 
TYR H    H  N N 347 
TYR H2   H  N N 348 
TYR HA   H  N N 349 
TYR HB2  H  N N 350 
TYR HB3  H  N N 351 
TYR HD1  H  N N 352 
TYR HD2  H  N N 353 
TYR HE1  H  N N 354 
TYR HE2  H  N N 355 
TYR HH   H  N N 356 
TYR HXT  H  N N 357 
VAL N    N  N N 358 
VAL CA   C  N S 359 
VAL C    C  N N 360 
VAL O    O  N N 361 
VAL CB   C  N N 362 
VAL CG1  C  N N 363 
VAL CG2  C  N N 364 
VAL OXT  O  N N 365 
VAL H    H  N N 366 
VAL H2   H  N N 367 
VAL HA   H  N N 368 
VAL HB   H  N N 369 
VAL HG11 H  N N 370 
VAL HG12 H  N N 371 
VAL HG13 H  N N 372 
VAL HG21 H  N N 373 
VAL HG22 H  N N 374 
VAL HG23 H  N N 375 
VAL HXT  H  N N 376 
XYP O1   O  N N 377 
XYP C1   C  N R 378 
XYP C2   C  N R 379 
XYP C3   C  N S 380 
XYP C4   C  N R 381 
XYP C5   C  N N 382 
XYP O2   O  N N 383 
XYP O3   O  N N 384 
XYP O4   O  N N 385 
XYP O5   O  N N 386 
XYP HO1  H  N N 387 
XYP H1   H  N N 388 
XYP H2   H  N N 389 
XYP H3   H  N N 390 
XYP H4   H  N N 391 
XYP H51  H  N N 392 
XYP H52  H  N N 393 
XYP HO2  H  N N 394 
XYP HO3  H  N N 395 
XYP HO4  H  N N 396 
ZN  ZN   ZN N N 397 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
XYP O1  C1   sing N N 363 
XYP O1  HO1  sing N N 364 
XYP C1  C2   sing N N 365 
XYP C1  O5   sing N N 366 
XYP C1  H1   sing N N 367 
XYP C2  C3   sing N N 368 
XYP C2  O2   sing N N 369 
XYP C2  H2   sing N N 370 
XYP C3  C4   sing N N 371 
XYP C3  O3   sing N N 372 
XYP C3  H3   sing N N 373 
XYP C4  C5   sing N N 374 
XYP C4  O4   sing N N 375 
XYP C4  H4   sing N N 376 
XYP C5  O5   sing N N 377 
XYP C5  H51  sing N N 378 
XYP C5  H52  sing N N 379 
XYP O2  HO2  sing N N 380 
XYP O3  HO3  sing N N 381 
XYP O4  HO4  sing N N 382 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 XYP 1 n 
2 XYP 2 n 
# 
_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   3WP4 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XZZ 
_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]   0.019203 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002641 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007271 
_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]   0.019100 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 6   ? 9.571   -16.341 7.568   1.00 26.65 ? -6  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 6   ? 10.363  -17.419 6.978   1.00 30.06 ? -6  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 6   ? 9.509   -18.648 6.741   1.00 32.96 ? -6  ALA A C   1 
ATOM   4    O  O   . ALA A 1 6   ? 9.954   -19.626 6.124   1.00 30.39 ? -6  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 6   ? 11.541  -17.773 7.869   1.00 24.15 ? -6  ALA A CB  1 
ATOM   6    N  N   . GLY A 1 7   ? 8.274   -18.598 7.244   1.00 30.92 ? -5  GLY A N   1 
ATOM   7    C  CA  . GLY A 1 7   ? 7.420   -19.776 7.225   1.00 29.46 ? -5  GLY A CA  1 
ATOM   8    C  C   . GLY A 1 7   ? 8.109   -20.933 7.931   1.00 32.71 ? -5  GLY A C   1 
ATOM   9    O  O   . GLY A 1 7   ? 8.646   -20.780 9.037   1.00 31.39 ? -5  GLY A O   1 
ATOM   10   N  N   . ALA A 1 8   ? 8.148   -22.088 7.262   1.00 31.70 ? -4  ALA A N   1 
ATOM   11   C  CA  . ALA A 1 8   ? 8.895   -23.209 7.808   1.00 32.38 ? -4  ALA A CA  1 
ATOM   12   C  C   . ALA A 1 8   ? 10.365  -22.829 8.022   1.00 36.76 ? -4  ALA A C   1 
ATOM   13   O  O   . ALA A 1 8   ? 10.991  -23.243 9.013   1.00 44.35 ? -4  ALA A O   1 
ATOM   14   C  CB  . ALA A 1 8   ? 8.756   -24.428 6.885   1.00 28.46 ? -4  ALA A CB  1 
ATOM   15   N  N   . GLY A 1 9   ? 10.937  -22.043 7.097   1.00 27.64 ? -3  GLY A N   1 
ATOM   16   C  CA  . GLY A 1 9   ? 12.360  -21.694 7.111   1.00 29.40 ? -3  GLY A CA  1 
ATOM   17   C  C   . GLY A 1 9   ? 12.916  -21.151 8.422   1.00 30.83 ? -3  GLY A C   1 
ATOM   18   O  O   . GLY A 1 9   ? 14.128  -20.971 8.542   1.00 28.90 ? -3  GLY A O   1 
ATOM   19   N  N   . ALA A 1 10  ? 12.071  -20.918 9.425   1.00 29.35 ? -2  ALA A N   1 
ATOM   20   C  CA  . ALA A 1 10  ? 12.540  -20.389 10.705  1.00 26.67 ? -2  ALA A CA  1 
ATOM   21   C  C   . ALA A 1 10  ? 13.350  -21.441 11.457  1.00 32.26 ? -2  ALA A C   1 
ATOM   22   O  O   . ALA A 1 10  ? 13.007  -22.630 11.459  1.00 34.47 ? -2  ALA A O   1 
ATOM   23   C  CB  . ALA A 1 10  ? 11.351  -19.920 11.558  1.00 26.99 ? -2  ALA A CB  1 
ATOM   24   N  N   . GLY A 1 11  ? 14.432  -20.997 12.091  1.00 28.63 ? -1  GLY A N   1 
ATOM   25   C  CA  . GLY A 1 11  ? 15.237  -21.861 12.926  1.00 25.00 ? -1  GLY A CA  1 
ATOM   26   C  C   . GLY A 1 11  ? 14.537  -22.191 14.238  1.00 31.10 ? -1  GLY A C   1 
ATOM   27   O  O   . GLY A 1 11  ? 13.358  -21.903 14.457  1.00 27.01 ? -1  GLY A O   1 
ATOM   28   N  N   . MET A 1 12  ? 15.305  -22.814 15.136  1.00 30.75 ? 0   MET A N   1 
ATOM   29   C  CA  . MET A 1 12  ? 14.772  -23.201 16.438  1.00 26.47 ? 0   MET A CA  1 
ATOM   30   C  C   . MET A 1 12  ? 14.391  -21.971 17.257  1.00 24.00 ? 0   MET A C   1 
ATOM   31   O  O   . MET A 1 12  ? 15.066  -20.940 17.213  1.00 26.15 ? 0   MET A O   1 
ATOM   32   C  CB  . MET A 1 12  ? 15.800  -24.047 17.194  1.00 31.00 ? 0   MET A CB  1 
ATOM   33   C  CG  . MET A 1 12  ? 16.092  -25.393 16.514  1.00 35.21 ? 0   MET A CG  1 
ATOM   34   S  SD  . MET A 1 12  ? 14.636  -26.461 16.331  1.00 57.76 ? 0   MET A SD  1 
ATOM   35   C  CE  . MET A 1 12  ? 14.238  -26.249 14.593  1.00 40.05 ? 0   MET A CE  1 
ATOM   36   N  N   . GLU A 1 13  ? 13.302  -22.087 18.010  1.00 22.56 ? 1   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 13  ? 12.814  -20.966 18.799  1.00 19.94 ? 1   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 13  ? 13.763  -20.683 19.958  1.00 19.43 ? 1   GLU A C   1 
ATOM   39   O  O   . GLU A 1 13  ? 14.212  -21.600 20.649  1.00 20.93 ? 1   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 13  ? 11.405  -21.255 19.308  1.00 24.99 ? 1   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 13  ? 10.409  -21.480 18.179  1.00 27.39 ? 1   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 13  ? 8.958   -21.461 18.639  1.00 37.13 ? 1   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 13  ? 8.088   -21.056 17.833  1.00 39.79 ? 1   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 13  ? 8.686   -21.850 19.795  1.00 36.84 ? 1   GLU A OE2 1 
ATOM   45   N  N   . ILE A 1 14  ? 14.087  -19.407 20.143  1.00 15.28 ? 2   ILE A N   1 
ATOM   46   C  CA  . ILE A 1 14  ? 14.973  -18.932 21.198  1.00 17.01 ? 2   ILE A CA  1 
ATOM   47   C  C   . ILE A 1 14  ? 14.127  -18.081 22.139  1.00 18.55 ? 2   ILE A C   1 
ATOM   48   O  O   . ILE A 1 14  ? 13.428  -17.170 21.685  1.00 17.14 ? 2   ILE A O   1 
ATOM   49   C  CB  . ILE A 1 14  ? 16.136  -18.113 20.603  1.00 15.85 ? 2   ILE A CB  1 
ATOM   50   C  CG1 . ILE A 1 14  ? 16.974  -18.975 19.640  1.00 25.60 ? 2   ILE A CG1 1 
ATOM   51   C  CG2 . ILE A 1 14  ? 16.975  -17.474 21.700  1.00 20.97 ? 2   ILE A CG2 1 
ATOM   52   C  CD1 . ILE A 1 14  ? 18.031  -18.204 18.865  1.00 22.01 ? 2   ILE A CD1 1 
ATOM   53   N  N   . THR A 1 15  ? 14.181  -18.366 23.446  1.00 15.95 ? 3   THR A N   1 
ATOM   54   C  CA  . THR A 1 15  ? 13.348  -17.636 24.399  1.00 17.61 ? 3   THR A CA  1 
ATOM   55   C  C   . THR A 1 15  ? 14.132  -16.976 25.527  1.00 17.66 ? 3   THR A C   1 
ATOM   56   O  O   . THR A 1 15  ? 13.518  -16.344 26.404  1.00 16.63 ? 3   THR A O   1 
ATOM   57   C  CB  . THR A 1 15  ? 12.282  -18.557 25.010  1.00 20.75 ? 3   THR A CB  1 
ATOM   58   O  OG1 . THR A 1 15  ? 12.923  -19.677 25.637  1.00 21.72 ? 3   THR A OG1 1 
ATOM   59   C  CG2 . THR A 1 15  ? 11.334  -19.063 23.933  1.00 22.44 ? 3   THR A CG2 1 
ATOM   60   N  N   . SER A 1 16  ? 15.453  -17.112 25.546  1.00 15.39 ? 4   SER A N   1 
ATOM   61   C  CA  . SER A 1 16  ? 16.303  -16.402 26.487  1.00 18.89 ? 4   SER A CA  1 
ATOM   62   C  C   . SER A 1 16  ? 17.485  -15.818 25.730  1.00 14.31 ? 4   SER A C   1 
ATOM   63   O  O   . SER A 1 16  ? 17.796  -16.231 24.606  1.00 13.84 ? 4   SER A O   1 
ATOM   64   C  CB  . SER A 1 16  ? 16.774  -17.314 27.638  1.00 19.65 ? 4   SER A CB  1 
ATOM   65   O  OG  . SER A 1 16  ? 17.502  -18.419 27.150  1.00 24.57 ? 4   SER A OG  1 
ATOM   66   N  N   . SER A 1 17  ? 18.120  -14.831 26.360  1.00 14.08 ? 5   SER A N   1 
ATOM   67   C  CA  . SER A 1 17  ? 19.127  -14.002 25.703  1.00 13.60 ? 5   SER A CA  1 
ATOM   68   C  C   . SER A 1 17  ? 20.258  -14.841 25.122  1.00 15.87 ? 5   SER A C   1 
ATOM   69   O  O   . SER A 1 17  ? 20.755  -15.776 25.756  1.00 15.80 ? 5   SER A O   1 
ATOM   70   C  CB  . SER A 1 17  ? 19.696  -12.982 26.684  1.00 14.79 ? 5   SER A CB  1 
ATOM   71   O  OG  . SER A 1 17  ? 18.651  -12.240 27.290  1.00 14.61 ? 5   SER A OG  1 
ATOM   72   N  N   . GLU A 1 18  ? 20.669  -14.486 23.905  1.00 14.13 ? 6   GLU A N   1 
ATOM   73   C  CA  . GLU A 1 18  ? 21.661  -15.238 23.151  1.00 15.91 ? 6   GLU A CA  1 
ATOM   74   C  C   . GLU A 1 18  ? 22.190  -14.352 22.033  1.00 14.77 ? 6   GLU A C   1 
ATOM   75   O  O   . GLU A 1 18  ? 21.453  -13.533 21.488  1.00 14.78 ? 6   GLU A O   1 
ATOM   76   C  CB  . GLU A 1 18  ? 21.029  -16.517 22.579  1.00 22.56 ? 6   GLU A CB  1 
ATOM   77   C  CG  . GLU A 1 18  ? 21.941  -17.369 21.722  1.00 28.99 ? 6   GLU A CG  1 
ATOM   78   C  CD  . GLU A 1 18  ? 21.233  -18.605 21.197  1.00 31.00 ? 6   GLU A CD  1 
ATOM   79   O  OE1 . GLU A 1 18  ? 21.233  -18.810 19.963  1.00 26.04 ? 6   GLU A OE1 1 
ATOM   80   O  OE2 . GLU A 1 18  ? 20.677  -19.369 22.020  1.00 29.31 ? 6   GLU A OE2 1 
ATOM   81   N  N   . THR A 1 19  ? 23.462  -14.535 21.685  1.00 14.07 ? 7   THR A N   1 
ATOM   82   C  CA  . THR A 1 19  ? 24.036  -13.903 20.506  1.00 10.83 ? 7   THR A CA  1 
ATOM   83   C  C   . THR A 1 19  ? 24.786  -14.942 19.685  1.00 14.98 ? 7   THR A C   1 
ATOM   84   O  O   . THR A 1 19  ? 25.139  -16.019 20.170  1.00 14.82 ? 7   THR A O   1 
ATOM   85   C  CB  . THR A 1 19  ? 24.994  -12.741 20.852  1.00 14.93 ? 7   THR A CB  1 
ATOM   86   O  OG1 . THR A 1 19  ? 26.203  -13.257 21.450  1.00 16.10 ? 7   THR A OG1 1 
ATOM   87   C  CG2 . THR A 1 19  ? 24.331  -11.742 21.800  1.00 13.93 ? 7   THR A CG2 1 
ATOM   88   N  N   . GLY A 1 20  ? 25.024  -14.608 18.426  1.00 13.46 ? 8   GLY A N   1 
ATOM   89   C  CA  . GLY A 1 20  ? 25.767  -15.512 17.573  1.00 12.07 ? 8   GLY A CA  1 
ATOM   90   C  C   . GLY A 1 20  ? 25.840  -14.962 16.169  1.00 14.27 ? 8   GLY A C   1 
ATOM   91   O  O   . GLY A 1 20  ? 25.540  -13.793 15.924  1.00 12.57 ? 8   GLY A O   1 
ATOM   92   N  N   . THR A 1 21  ? 26.257  -15.821 15.244  1.00 12.04 ? 9   THR A N   1 
ATOM   93   C  CA  . THR A 1 21  ? 26.284  -15.477 13.832  1.00 11.42 ? 9   THR A CA  1 
ATOM   94   C  C   . THR A 1 21  ? 25.546  -16.570 13.074  1.00 13.70 ? 9   THR A C   1 
ATOM   95   O  O   . THR A 1 21  ? 25.805  -17.757 13.288  1.00 14.96 ? 9   THR A O   1 
ATOM   96   C  CB  . THR A 1 21  ? 27.723  -15.320 13.323  1.00 14.03 ? 9   THR A CB  1 
ATOM   97   O  OG1 . THR A 1 21  ? 28.360  -14.224 14.008  1.00 15.31 ? 9   THR A OG1 1 
ATOM   98   C  CG2 . THR A 1 21  ? 27.716  -15.034 11.837  1.00 13.12 ? 9   THR A CG2 1 
ATOM   99   N  N   . ASN A 1 22  ? 24.613  -16.173 12.214  1.00 12.27 ? 10  ASN A N   1 
ATOM   100  C  CA  . ASN A 1 22  ? 23.708  -17.106 11.546  1.00 14.51 ? 10  ASN A CA  1 
ATOM   101  C  C   . ASN A 1 22  ? 23.607  -16.680 10.093  1.00 10.98 ? 10  ASN A C   1 
ATOM   102  O  O   . ASN A 1 22  ? 23.284  -15.525 9.811   1.00 11.22 ? 10  ASN A O   1 
ATOM   103  C  CB  . ASN A 1 22  ? 22.329  -17.101 12.224  1.00 12.77 ? 10  ASN A CB  1 
ATOM   104  C  CG  . ASN A 1 22  ? 21.270  -17.853 11.432  1.00 14.91 ? 10  ASN A CG  1 
ATOM   105  O  OD1 . ASN A 1 22  ? 20.529  -17.263 10.636  1.00 14.98 ? 10  ASN A OD1 1 
ATOM   106  N  ND2 . ASN A 1 22  ? 21.182  -19.159 11.660  1.00 15.40 ? 10  ASN A ND2 1 
ATOM   107  N  N   . ASN A 1 23  ? 23.944  -17.586 9.177   1.00 12.58 ? 11  ASN A N   1 
ATOM   108  C  CA  . ASN A 1 23  ? 23.883  -17.294 7.739   1.00 12.06 ? 11  ASN A CA  1 
ATOM   109  C  C   . ASN A 1 23  ? 24.669  -16.031 7.396   1.00 14.60 ? 11  ASN A C   1 
ATOM   110  O  O   . ASN A 1 23  ? 24.266  -15.229 6.547   1.00 17.20 ? 11  ASN A O   1 
ATOM   111  C  CB  . ASN A 1 23  ? 22.433  -17.182 7.268   1.00 13.49 ? 11  ASN A CB  1 
ATOM   112  C  CG  . ASN A 1 23  ? 21.716  -18.516 7.255   1.00 17.21 ? 11  ASN A CG  1 
ATOM   113  O  OD1 . ASN A 1 23  ? 22.158  -19.463 6.603   1.00 18.75 ? 11  ASN A OD1 1 
ATOM   114  N  ND2 . ASN A 1 23  ? 20.600  -18.599 7.976   1.00 13.53 ? 11  ASN A ND2 1 
ATOM   115  N  N   . GLY A 1 24  ? 25.799  -15.846 8.077   1.00 15.15 ? 12  GLY A N   1 
ATOM   116  C  CA  . GLY A 1 24  ? 26.690  -14.735 7.839   1.00 12.80 ? 12  GLY A CA  1 
ATOM   117  C  C   . GLY A 1 24  ? 26.321  -13.441 8.537   1.00 13.80 ? 12  GLY A C   1 
ATOM   118  O  O   . GLY A 1 24  ? 27.061  -12.456 8.415   1.00 14.28 ? 12  GLY A O   1 
ATOM   119  N  N   . TYR A 1 25  ? 25.213  -13.402 9.260   1.00 12.77 ? 13  TYR A N   1 
ATOM   120  C  CA  . TYR A 1 25  ? 24.797  -12.206 9.980   1.00 11.29 ? 13  TYR A CA  1 
ATOM   121  C  C   . TYR A 1 25  ? 24.932  -12.410 11.479  1.00 9.59  ? 13  TYR A C   1 
ATOM   122  O  O   . TYR A 1 25  ? 24.474  -13.423 12.014  1.00 12.52 ? 13  TYR A O   1 
ATOM   123  C  CB  . TYR A 1 25  ? 23.346  -11.855 9.652   1.00 10.99 ? 13  TYR A CB  1 
ATOM   124  C  CG  . TYR A 1 25  ? 23.209  -11.311 8.267   1.00 11.33 ? 13  TYR A CG  1 
ATOM   125  C  CD1 . TYR A 1 25  ? 23.368  -9.956  8.025   1.00 14.15 ? 13  TYR A CD1 1 
ATOM   126  C  CD2 . TYR A 1 25  ? 22.952  -12.157 7.192   1.00 12.30 ? 13  TYR A CD2 1 
ATOM   127  C  CE1 . TYR A 1 25  ? 23.267  -9.445  6.736   1.00 19.27 ? 13  TYR A CE1 1 
ATOM   128  C  CE2 . TYR A 1 25  ? 22.841  -11.656 5.899   1.00 15.12 ? 13  TYR A CE2 1 
ATOM   129  C  CZ  . TYR A 1 25  ? 23.001  -10.295 5.685   1.00 17.73 ? 13  TYR A CZ  1 
ATOM   130  O  OH  . TYR A 1 25  ? 22.902  -9.762  4.417   1.00 20.82 ? 13  TYR A OH  1 
ATOM   131  N  N   . TYR A 1 26  ? 25.536  -11.433 12.152  1.00 9.53  ? 14  TYR A N   1 
ATOM   132  C  CA  . TYR A 1 26  ? 25.459  -11.379 13.602  1.00 11.19 ? 14  TYR A CA  1 
ATOM   133  C  C   . TYR A 1 26  ? 24.001  -11.241 14.026  1.00 12.54 ? 14  TYR A C   1 
ATOM   134  O  O   . TYR A 1 26  ? 23.219  -10.562 13.359  1.00 10.64 ? 14  TYR A O   1 
ATOM   135  C  CB  . TYR A 1 26  ? 26.266  -10.188 14.115  1.00 9.39  ? 14  TYR A CB  1 
ATOM   136  C  CG  . TYR A 1 26  ? 26.261  -10.046 15.603  1.00 11.69 ? 14  TYR A CG  1 
ATOM   137  C  CD1 . TYR A 1 26  ? 27.045  -10.868 16.395  1.00 12.85 ? 14  TYR A CD1 1 
ATOM   138  C  CD2 . TYR A 1 26  ? 25.466  -9.095  16.226  1.00 10.78 ? 14  TYR A CD2 1 
ATOM   139  C  CE1 . TYR A 1 26  ? 27.033  -10.752 17.756  1.00 13.64 ? 14  TYR A CE1 1 
ATOM   140  C  CE2 . TYR A 1 26  ? 25.455  -8.974  17.589  1.00 12.70 ? 14  TYR A CE2 1 
ATOM   141  C  CZ  . TYR A 1 26  ? 26.243  -9.791  18.343  1.00 13.07 ? 14  TYR A CZ  1 
ATOM   142  O  OH  . TYR A 1 26  ? 26.233  -9.678  19.702  1.00 17.04 ? 14  TYR A OH  1 
ATOM   143  N  N   . TYR A 1 27  ? 23.629  -11.895 15.130  1.00 10.87 ? 15  TYR A N   1 
ATOM   144  C  CA  . TYR A 1 27  ? 22.323  -11.659 15.739  1.00 8.07  ? 15  TYR A CA  1 
ATOM   145  C  C   . TYR A 1 27  ? 22.488  -11.450 17.229  1.00 10.10 ? 15  TYR A C   1 
ATOM   146  O  O   . TYR A 1 27  ? 23.348  -12.072 17.863  1.00 10.61 ? 15  TYR A O   1 
ATOM   147  C  CB  . TYR A 1 27  ? 21.319  -12.804 15.483  1.00 10.16 ? 15  TYR A CB  1 
ATOM   148  C  CG  . TYR A 1 27  ? 21.672  -14.134 16.122  1.00 11.58 ? 15  TYR A CG  1 
ATOM   149  C  CD1 . TYR A 1 27  ? 22.491  -15.049 15.459  1.00 11.83 ? 15  TYR A CD1 1 
ATOM   150  C  CD2 . TYR A 1 27  ? 21.178  -14.480 17.372  1.00 14.00 ? 15  TYR A CD2 1 
ATOM   151  C  CE1 . TYR A 1 27  ? 22.807  -16.269 16.025  1.00 12.17 ? 15  TYR A CE1 1 
ATOM   152  C  CE2 . TYR A 1 27  ? 21.495  -15.713 17.955  1.00 13.91 ? 15  TYR A CE2 1 
ATOM   153  C  CZ  . TYR A 1 27  ? 22.312  -16.593 17.271  1.00 14.20 ? 15  TYR A CZ  1 
ATOM   154  O  OH  . TYR A 1 27  ? 22.644  -17.813 17.820  1.00 17.79 ? 15  TYR A OH  1 
ATOM   155  N  N   . SER A 1 28  ? 21.661  -10.564 17.785  1.00 9.83  ? 16  SER A N   1 
ATOM   156  C  CA  . SER A 1 28  ? 21.609  -10.356 19.227  1.00 10.41 ? 16  SER A CA  1 
ATOM   157  C  C   . SER A 1 28  ? 20.153  -10.461 19.645  1.00 10.91 ? 16  SER A C   1 
ATOM   158  O  O   . SER A 1 28  ? 19.299  -9.755  19.099  1.00 10.07 ? 16  SER A O   1 
ATOM   159  C  CB  . SER A 1 28  ? 22.187  -8.995  19.616  1.00 10.64 ? 16  SER A CB  1 
ATOM   160  O  OG  . SER A 1 28  ? 22.029  -8.758  21.008  1.00 14.21 ? 16  SER A OG  1 
ATOM   161  N  N   . PHE A 1 29  ? 19.860  -11.360 20.575  1.00 9.68  ? 17  PHE A N   1 
ATOM   162  C  CA  . PHE A 1 29  ? 18.541  -11.427 21.193  1.00 9.53  ? 17  PHE A CA  1 
ATOM   163  C  C   . PHE A 1 29  ? 18.716  -11.183 22.684  1.00 12.77 ? 17  PHE A C   1 
ATOM   164  O  O   . PHE A 1 29  ? 19.450  -11.921 23.357  1.00 12.63 ? 17  PHE A O   1 
ATOM   165  C  CB  . PHE A 1 29  ? 17.880  -12.779 20.942  1.00 11.79 ? 17  PHE A CB  1 
ATOM   166  C  CG  . PHE A 1 29  ? 16.582  -12.955 21.672  1.00 12.41 ? 17  PHE A CG  1 
ATOM   167  C  CD1 . PHE A 1 29  ? 15.529  -12.086 21.447  1.00 13.77 ? 17  PHE A CD1 1 
ATOM   168  C  CD2 . PHE A 1 29  ? 16.418  -13.965 22.608  1.00 12.15 ? 17  PHE A CD2 1 
ATOM   169  C  CE1 . PHE A 1 29  ? 14.325  -12.241 22.126  1.00 12.25 ? 17  PHE A CE1 1 
ATOM   170  C  CE2 . PHE A 1 29  ? 15.222  -14.120 23.286  1.00 15.07 ? 17  PHE A CE2 1 
ATOM   171  C  CZ  . PHE A 1 29  ? 14.181  -13.256 23.049  1.00 13.62 ? 17  PHE A CZ  1 
ATOM   172  N  N   . TRP A 1 30  ? 18.067  -10.147 23.206  1.00 9.11  ? 18  TRP A N   1 
ATOM   173  C  CA  . TRP A 1 30  ? 18.172  -9.873  24.634  1.00 10.84 ? 18  TRP A CA  1 
ATOM   174  C  C   . TRP A 1 30  ? 16.780  -9.697  25.201  1.00 11.66 ? 18  TRP A C   1 
ATOM   175  O  O   . TRP A 1 30  ? 15.973  -8.954  24.636  1.00 11.73 ? 18  TRP A O   1 
ATOM   176  C  CB  . TRP A 1 30  ? 19.009  -8.625  24.925  1.00 13.08 ? 18  TRP A CB  1 
ATOM   177  C  CG  . TRP A 1 30  ? 19.008  -8.271  26.394  1.00 13.75 ? 18  TRP A CG  1 
ATOM   178  C  CD1 . TRP A 1 30  ? 19.786  -8.827  27.381  1.00 16.32 ? 18  TRP A CD1 1 
ATOM   179  C  CD2 . TRP A 1 30  ? 18.185  -7.290  27.042  1.00 15.57 ? 18  TRP A CD2 1 
ATOM   180  N  NE1 . TRP A 1 30  ? 19.491  -8.247  28.597  1.00 15.57 ? 18  TRP A NE1 1 
ATOM   181  C  CE2 . TRP A 1 30  ? 18.520  -7.299  28.414  1.00 18.39 ? 18  TRP A CE2 1 
ATOM   182  C  CE3 . TRP A 1 30  ? 17.208  -6.397  26.593  1.00 16.66 ? 18  TRP A CE3 1 
ATOM   183  C  CZ2 . TRP A 1 30  ? 17.891  -6.459  29.347  1.00 18.91 ? 18  TRP A CZ2 1 
ATOM   184  C  CZ3 . TRP A 1 30  ? 16.591  -5.562  27.517  1.00 18.56 ? 18  TRP A CZ3 1 
ATOM   185  C  CH2 . TRP A 1 30  ? 16.939  -5.600  28.877  1.00 18.13 ? 18  TRP A CH2 1 
ATOM   186  N  N   . THR A 1 31  ? 16.490  -10.385 26.303  1.00 11.29 ? 19  THR A N   1 
ATOM   187  C  CA  . THR A 1 31  ? 15.236  -10.138 27.000  1.00 11.08 ? 19  THR A CA  1 
ATOM   188  C  C   . THR A 1 31  ? 15.495  -10.136 28.495  1.00 14.22 ? 19  THR A C   1 
ATOM   189  O  O   . THR A 1 31  ? 16.337  -10.899 28.987  1.00 15.54 ? 19  THR A O   1 
ATOM   190  C  CB  . THR A 1 31  ? 14.148  -11.167 26.660  1.00 16.42 ? 19  THR A CB  1 
ATOM   191  O  OG1 . THR A 1 31  ? 12.999  -10.903 27.474  1.00 14.65 ? 19  THR A OG1 1 
ATOM   192  C  CG2 . THR A 1 31  ? 14.635  -12.597 26.907  1.00 15.83 ? 19  THR A CG2 1 
ATOM   193  N  N   . ASP A 1 32  ? 14.784  -9.266  29.211  1.00 13.26 ? 20  ASP A N   1 
ATOM   194  C  CA  . ASP A 1 32  ? 14.903  -9.277  30.668  1.00 15.33 ? 20  ASP A CA  1 
ATOM   195  C  C   . ASP A 1 32  ? 14.127  -10.420 31.316  1.00 18.63 ? 20  ASP A C   1 
ATOM   196  O  O   . ASP A 1 32  ? 14.186  -10.573 32.541  1.00 20.64 ? 20  ASP A O   1 
ATOM   197  C  CB  . ASP A 1 32  ? 14.480  -7.923  31.259  1.00 16.11 ? 20  ASP A CB  1 
ATOM   198  C  CG  . ASP A 1 32  ? 12.989  -7.617  31.089  1.00 17.15 ? 20  ASP A CG  1 
ATOM   199  O  OD1 . ASP A 1 32  ? 12.218  -8.496  30.670  1.00 16.00 ? 20  ASP A OD1 1 
ATOM   200  O  OD2 . ASP A 1 32  ? 12.586  -6.470  31.396  1.00 19.17 ? 20  ASP A OD2 1 
ATOM   201  N  N   . GLY A 1 33  ? 13.418  -11.233 30.530  1.00 16.53 ? 21  GLY A N   1 
ATOM   202  C  CA  . GLY A 1 33  ? 12.709  -12.389 31.032  1.00 19.99 ? 21  GLY A CA  1 
ATOM   203  C  C   . GLY A 1 33  ? 11.224  -12.187 31.259  1.00 18.48 ? 21  GLY A C   1 
ATOM   204  O  O   . GLY A 1 33  ? 10.526  -13.162 31.569  1.00 21.91 ? 21  GLY A O   1 
ATOM   205  N  N   . GLY A 1 34  ? 10.721  -10.966 31.103  1.00 17.13 ? 22  GLY A N   1 
ATOM   206  C  CA  . GLY A 1 34  ? 9.306   -10.719 31.338  1.00 18.26 ? 22  GLY A CA  1 
ATOM   207  C  C   . GLY A 1 34  ? 8.439   -11.315 30.240  1.00 17.14 ? 22  GLY A C   1 
ATOM   208  O  O   . GLY A 1 34  ? 8.815   -11.349 29.065  1.00 18.57 ? 22  GLY A O   1 
ATOM   209  N  N   . GLY A 1 35  ? 7.260   -11.789 30.637  1.00 17.11 ? 23  GLY A N   1 
ATOM   210  C  CA  . GLY A 1 35  ? 6.293   -12.320 29.686  1.00 15.85 ? 23  GLY A CA  1 
ATOM   211  C  C   . GLY A 1 35  ? 6.875   -13.443 28.856  1.00 19.05 ? 23  GLY A C   1 
ATOM   212  O  O   . GLY A 1 35  ? 7.653   -14.275 29.340  1.00 18.00 ? 23  GLY A O   1 
ATOM   213  N  N   . GLN A 1 36  ? 6.502   -13.471 27.579  1.00 14.44 ? 24  GLN A N   1 
ATOM   214  C  CA  . GLN A 1 36  ? 7.019   -14.463 26.650  1.00 17.62 ? 24  GLN A CA  1 
ATOM   215  C  C   . GLN A 1 36  ? 7.545   -13.747 25.414  1.00 18.67 ? 24  GLN A C   1 
ATOM   216  O  O   . GLN A 1 36  ? 6.822   -12.969 24.789  1.00 14.42 ? 24  GLN A O   1 
ATOM   217  C  CB  . GLN A 1 36  ? 5.941   -15.486 26.273  1.00 18.26 ? 24  GLN A CB  1 
ATOM   218  C  CG  . GLN A 1 36  ? 6.356   -16.472 25.188  1.00 27.58 ? 24  GLN A CG  1 
ATOM   219  C  CD  . GLN A 1 36  ? 7.516   -17.367 25.592  1.00 36.87 ? 24  GLN A CD  1 
ATOM   220  O  OE1 . GLN A 1 36  ? 8.417   -17.638 24.791  1.00 39.18 ? 24  GLN A OE1 1 
ATOM   221  N  NE2 . GLN A 1 36  ? 7.501   -17.831 26.839  1.00 40.59 ? 24  GLN A NE2 1 
ATOM   222  N  N   . VAL A 1 37  ? 8.803   -13.995 25.074  1.00 14.41 ? 25  VAL A N   1 
ATOM   223  C  CA  . VAL A 1 37  ? 9.414   -13.428 23.879  1.00 13.39 ? 25  VAL A CA  1 
ATOM   224  C  C   . VAL A 1 37  ? 10.116  -14.570 23.162  1.00 16.61 ? 25  VAL A C   1 
ATOM   225  O  O   . VAL A 1 37  ? 10.935  -15.270 23.769  1.00 15.39 ? 25  VAL A O   1 
ATOM   226  C  CB  . VAL A 1 37  ? 10.405  -12.293 24.204  1.00 12.40 ? 25  VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 37  ? 10.938  -11.653 22.924  1.00 11.96 ? 25  VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 37  ? 9.776   -11.239 25.114  1.00 12.74 ? 25  VAL A CG2 1 
ATOM   229  N  N   . THR A 1 38  ? 9.773   -14.784 21.892  1.00 12.84 ? 26  THR A N   1 
ATOM   230  C  CA  . THR A 1 38  ? 10.295  -15.899 21.106  1.00 12.88 ? 26  THR A CA  1 
ATOM   231  C  C   . THR A 1 38  ? 10.921  -15.367 19.829  1.00 12.90 ? 26  THR A C   1 
ATOM   232  O  O   . THR A 1 38  ? 10.247  -14.703 19.034  1.00 13.07 ? 26  THR A O   1 
ATOM   233  C  CB  . THR A 1 38  ? 9.192   -16.897 20.755  1.00 16.32 ? 26  THR A CB  1 
ATOM   234  O  OG1 . THR A 1 38  ? 8.590   -17.376 21.960  1.00 20.39 ? 26  THR A OG1 1 
ATOM   235  C  CG2 . THR A 1 38  ? 9.760   -18.076 19.976  1.00 19.58 ? 26  THR A CG2 1 
ATOM   236  N  N   . TYR A 1 39  ? 12.182  -15.718 19.611  1.00 12.41 ? 27  TYR A N   1 
ATOM   237  C  CA  . TYR A 1 39  ? 12.995  -15.202 18.522  1.00 12.89 ? 27  TYR A CA  1 
ATOM   238  C  C   . TYR A 1 39  ? 13.435  -16.358 17.637  1.00 11.97 ? 27  TYR A C   1 
ATOM   239  O  O   . TYR A 1 39  ? 13.755  -17.431 18.143  1.00 12.55 ? 27  TYR A O   1 
ATOM   240  C  CB  . TYR A 1 39  ? 14.217  -14.469 19.094  1.00 11.14 ? 27  TYR A CB  1 
ATOM   241  C  CG  . TYR A 1 39  ? 15.246  -14.072 18.050  1.00 12.28 ? 27  TYR A CG  1 
ATOM   242  C  CD1 . TYR A 1 39  ? 16.248  -14.951 17.659  1.00 11.40 ? 27  TYR A CD1 1 
ATOM   243  C  CD2 . TYR A 1 39  ? 15.201  -12.819 17.451  1.00 10.43 ? 27  TYR A CD2 1 
ATOM   244  C  CE1 . TYR A 1 39  ? 17.195  -14.584 16.716  1.00 11.56 ? 27  TYR A CE1 1 
ATOM   245  C  CE2 . TYR A 1 39  ? 16.127  -12.445 16.506  1.00 10.93 ? 27  TYR A CE2 1 
ATOM   246  C  CZ  . TYR A 1 39  ? 17.121  -13.332 16.138  1.00 10.90 ? 27  TYR A CZ  1 
ATOM   247  O  OH  . TYR A 1 39  ? 18.036  -12.959 15.191  1.00 12.51 ? 27  TYR A OH  1 
ATOM   248  N  N   . THR A 1 40  ? 13.428  -16.161 16.317  1.00 11.38 ? 28  THR A N   1 
ATOM   249  C  CA  . THR A 1 40  ? 13.926  -17.191 15.407  1.00 11.34 ? 28  THR A CA  1 
ATOM   250  C  C   . THR A 1 40  ? 14.786  -16.562 14.316  1.00 12.64 ? 28  THR A C   1 
ATOM   251  O  O   . THR A 1 40  ? 14.462  -15.489 13.799  1.00 13.47 ? 28  THR A O   1 
ATOM   252  C  CB  . THR A 1 40  ? 12.791  -18.013 14.742  1.00 17.57 ? 28  THR A CB  1 
ATOM   253  O  OG1 . THR A 1 40  ? 11.986  -17.160 13.926  1.00 19.21 ? 28  THR A OG1 1 
ATOM   254  C  CG2 . THR A 1 40  ? 11.898  -18.706 15.778  1.00 19.13 ? 28  THR A CG2 1 
ATOM   255  N  N   . ASN A 1 41  ? 15.878  -17.247 13.955  1.00 10.63 ? 29  ASN A N   1 
ATOM   256  C  CA  . ASN A 1 41  ? 16.687  -16.860 12.799  1.00 11.23 ? 29  ASN A CA  1 
ATOM   257  C  C   . ASN A 1 41  ? 16.156  -17.552 11.551  1.00 13.03 ? 29  ASN A C   1 
ATOM   258  O  O   . ASN A 1 41  ? 15.901  -18.761 11.565  1.00 17.69 ? 29  ASN A O   1 
ATOM   259  C  CB  . ASN A 1 41  ? 18.160  -17.239 12.986  1.00 12.05 ? 29  ASN A CB  1 
ATOM   260  C  CG  . ASN A 1 41  ? 18.892  -16.313 13.935  1.00 12.90 ? 29  ASN A CG  1 
ATOM   261  O  OD1 . ASN A 1 41  ? 18.832  -15.091 13.805  1.00 13.66 ? 29  ASN A OD1 1 
ATOM   262  N  ND2 . ASN A 1 41  ? 19.586  -16.898 14.906  1.00 13.01 ? 29  ASN A ND2 1 
ATOM   263  N  N   . GLY A 1 42  ? 16.011  -16.790 10.478  1.00 10.51 ? 30  GLY A N   1 
ATOM   264  C  CA  . GLY A 1 42  ? 15.639  -17.333 9.191   1.00 13.62 ? 30  GLY A CA  1 
ATOM   265  C  C   . GLY A 1 42  ? 16.806  -17.324 8.219   1.00 12.67 ? 30  GLY A C   1 
ATOM   266  O  O   . GLY A 1 42  ? 17.945  -17.005 8.581   1.00 14.37 ? 30  GLY A O   1 
ATOM   267  N  N   . PRO A 1 43  ? 16.546  -17.684 6.963   1.00 11.55 ? 31  PRO A N   1 
ATOM   268  C  CA  . PRO A 1 43  ? 17.617  -17.671 5.957   1.00 16.11 ? 31  PRO A CA  1 
ATOM   269  C  C   . PRO A 1 43  ? 18.181  -16.268 5.770   1.00 14.75 ? 31  PRO A C   1 
ATOM   270  O  O   . PRO A 1 43  ? 17.492  -15.271 5.986   1.00 14.63 ? 31  PRO A O   1 
ATOM   271  C  CB  . PRO A 1 43  ? 16.920  -18.172 4.681   1.00 21.04 ? 31  PRO A CB  1 
ATOM   272  C  CG  . PRO A 1 43  ? 15.590  -18.728 5.129   1.00 24.62 ? 31  PRO A CG  1 
ATOM   273  C  CD  . PRO A 1 43  ? 15.228  -17.999 6.383   1.00 19.89 ? 31  PRO A CD  1 
ATOM   274  N  N   . ALA A 1 44  ? 19.461  -16.202 5.381   1.00 14.35 ? 32  ALA A N   1 
ATOM   275  C  CA  . ALA A 1 44  ? 20.156  -14.947 5.029   1.00 16.44 ? 32  ALA A CA  1 
ATOM   276  C  C   . ALA A 1 44  ? 19.988  -13.944 6.173   1.00 13.71 ? 32  ALA A C   1 
ATOM   277  O  O   . ALA A 1 44  ? 20.271  -14.283 7.328   1.00 13.19 ? 32  ALA A O   1 
ATOM   278  C  CB  . ALA A 1 44  ? 19.658  -14.470 3.668   1.00 16.20 ? 32  ALA A CB  1 
ATOM   279  N  N   . GLY A 1 45  ? 19.537  -12.718 5.913   1.00 11.57 ? 33  GLY A N   1 
ATOM   280  C  CA  . GLY A 1 45  ? 19.458  -11.732 6.977   1.00 12.03 ? 33  GLY A CA  1 
ATOM   281  C  C   . GLY A 1 45  ? 18.120  -11.651 7.693   1.00 8.93  ? 33  GLY A C   1 
ATOM   282  O  O   . GLY A 1 45  ? 17.835  -10.634 8.328   1.00 9.33  ? 33  GLY A O   1 
ATOM   283  N  N   . GLN A 1 46  ? 17.313  -12.713 7.631   1.00 9.98  ? 34  GLN A N   1 
ATOM   284  C  CA  . GLN A 1 46  ? 15.958  -12.716 8.185   1.00 10.04 ? 34  GLN A CA  1 
ATOM   285  C  C   . GLN A 1 46  ? 15.949  -13.113 9.656   1.00 9.07  ? 34  GLN A C   1 
ATOM   286  O  O   . GLN A 1 46  ? 16.683  -14.016 10.077  1.00 10.90 ? 34  GLN A O   1 
ATOM   287  C  CB  . GLN A 1 46  ? 15.060  -13.689 7.417   1.00 10.47 ? 34  GLN A CB  1 
ATOM   288  C  CG  . GLN A 1 46  ? 13.557  -13.434 7.615   1.00 13.86 ? 34  GLN A CG  1 
ATOM   289  C  CD  . GLN A 1 46  ? 12.951  -14.152 8.829   1.00 16.14 ? 34  GLN A CD  1 
ATOM   290  O  OE1 . GLN A 1 46  ? 13.596  -14.967 9.490   1.00 17.64 ? 34  GLN A OE1 1 
ATOM   291  N  NE2 . GLN A 1 46  ? 11.693  -13.848 9.111   1.00 16.38 ? 34  GLN A NE2 1 
ATOM   292  N  N   . TYR A 1 47  ? 15.090  -12.446 10.430  1.00 9.34  ? 35  TYR A N   1 
ATOM   293  C  CA  . TYR A 1 47  ? 14.721  -12.909 11.759  1.00 10.53 ? 35  TYR A CA  1 
ATOM   294  C  C   . TYR A 1 47  ? 13.256  -12.594 12.023  1.00 9.98  ? 35  TYR A C   1 
ATOM   295  O  O   . TYR A 1 47  ? 12.668  -11.684 11.430  1.00 9.12  ? 35  TYR A O   1 
ATOM   296  C  CB  . TYR A 1 47  ? 15.603  -12.274 12.847  1.00 8.74  ? 35  TYR A CB  1 
ATOM   297  C  CG  . TYR A 1 47  ? 15.321  -10.809 13.104  1.00 9.85  ? 35  TYR A CG  1 
ATOM   298  C  CD1 . TYR A 1 47  ? 15.984  -9.821  12.391  1.00 8.62  ? 35  TYR A CD1 1 
ATOM   299  C  CD2 . TYR A 1 47  ? 14.394  -10.417 14.075  1.00 9.02  ? 35  TYR A CD2 1 
ATOM   300  C  CE1 . TYR A 1 47  ? 15.726  -8.468  12.633  1.00 8.17  ? 35  TYR A CE1 1 
ATOM   301  C  CE2 . TYR A 1 47  ? 14.136  -9.085  14.324  1.00 9.60  ? 35  TYR A CE2 1 
ATOM   302  C  CZ  . TYR A 1 47  ? 14.807  -8.119  13.605  1.00 9.08  ? 35  TYR A CZ  1 
ATOM   303  O  OH  . TYR A 1 47  ? 14.556  -6.799  13.864  1.00 9.83  ? 35  TYR A OH  1 
ATOM   304  N  N   . SER A 1 48  ? 12.675  -13.364 12.930  1.00 9.72  ? 36  SER A N   1 
ATOM   305  C  CA  . SER A 1 48  ? 11.321  -13.130 13.407  1.00 11.69 ? 36  SER A CA  1 
ATOM   306  C  C   . SER A 1 48  ? 11.331  -13.062 14.924  1.00 9.98  ? 36  SER A C   1 
ATOM   307  O  O   . SER A 1 48  ? 12.152  -13.701 15.585  1.00 11.53 ? 36  SER A O   1 
ATOM   308  C  CB  . SER A 1 48  ? 10.365  -14.234 12.934  1.00 15.02 ? 36  SER A CB  1 
ATOM   309  O  OG  . SER A 1 48  ? 10.092  -14.108 11.550  1.00 16.55 ? 36  SER A OG  1 
ATOM   310  N  N   . VAL A 1 49  ? 10.440  -12.249 15.481  1.00 11.37 ? 37  VAL A N   1 
ATOM   311  C  CA  . VAL A 1 49  ? 10.256  -12.202 16.920  1.00 10.49 ? 37  VAL A CA  1 
ATOM   312  C  C   . VAL A 1 49  ? 8.766   -12.059 17.191  1.00 12.76 ? 37  VAL A C   1 
ATOM   313  O  O   . VAL A 1 49  ? 8.053   -11.354 16.467  1.00 13.11 ? 37  VAL A O   1 
ATOM   314  C  CB  . VAL A 1 49  ? 11.086  -11.074 17.582  1.00 13.65 ? 37  VAL A CB  1 
ATOM   315  C  CG1 . VAL A 1 49  ? 10.694  -9.708  17.039  1.00 11.30 ? 37  VAL A CG1 1 
ATOM   316  C  CG2 . VAL A 1 49  ? 10.981  -11.124 19.115  1.00 12.69 ? 37  VAL A CG2 1 
ATOM   317  N  N   . GLU A 1 50  ? 8.292   -12.780 18.199  1.00 9.76  ? 38  GLU A N   1 
ATOM   318  C  CA  . GLU A 1 50  ? 6.903   -12.748 18.630  1.00 9.94  ? 38  GLU A CA  1 
ATOM   319  C  C   . GLU A 1 50  ? 6.892   -12.541 20.138  1.00 12.44 ? 38  GLU A C   1 
ATOM   320  O  O   . GLU A 1 50  ? 7.668   -13.178 20.859  1.00 13.68 ? 38  GLU A O   1 
ATOM   321  C  CB  . GLU A 1 50  ? 6.183   -14.066 18.254  1.00 16.85 ? 38  GLU A CB  1 
ATOM   322  C  CG  . GLU A 1 50  ? 4.726   -14.153 18.655  1.00 27.68 ? 38  GLU A CG  1 
ATOM   323  C  CD  . GLU A 1 50  ? 3.873   -14.825 17.591  1.00 38.16 ? 38  GLU A CD  1 
ATOM   324  O  OE1 . GLU A 1 50  ? 2.921   -14.184 17.099  1.00 42.55 ? 38  GLU A OE1 1 
ATOM   325  O  OE2 . GLU A 1 50  ? 4.161   -15.992 17.241  1.00 41.53 ? 38  GLU A OE2 1 
ATOM   326  N  N   . TRP A 1 51  ? 6.040   -11.652 20.635  1.00 10.39 ? 39  TRP A N   1 
ATOM   327  C  CA  . TRP A 1 51  ? 6.094   -11.405 22.071  1.00 10.11 ? 39  TRP A CA  1 
ATOM   328  C  C   . TRP A 1 51  ? 4.708   -11.155 22.653  1.00 13.63 ? 39  TRP A C   1 
ATOM   329  O  O   . TRP A 1 51  ? 3.778   -10.727 21.969  1.00 10.78 ? 39  TRP A O   1 
ATOM   330  C  CB  . TRP A 1 51  ? 7.055   -10.251 22.413  1.00 10.15 ? 39  TRP A CB  1 
ATOM   331  C  CG  . TRP A 1 51  ? 6.674   -8.871  21.955  1.00 10.20 ? 39  TRP A CG  1 
ATOM   332  C  CD1 . TRP A 1 51  ? 6.118   -7.886  22.722  1.00 9.97  ? 39  TRP A CD1 1 
ATOM   333  C  CD2 . TRP A 1 51  ? 6.869   -8.304  20.647  1.00 10.15 ? 39  TRP A CD2 1 
ATOM   334  N  NE1 . TRP A 1 51  ? 5.953   -6.740  21.976  1.00 9.32  ? 39  TRP A NE1 1 
ATOM   335  C  CE2 . TRP A 1 51  ? 6.403   -6.970  20.700  1.00 10.20 ? 39  TRP A CE2 1 
ATOM   336  C  CE3 . TRP A 1 51  ? 7.406   -8.790  19.442  1.00 11.02 ? 39  TRP A CE3 1 
ATOM   337  C  CZ2 . TRP A 1 51  ? 6.442   -6.116  19.596  1.00 9.39  ? 39  TRP A CZ2 1 
ATOM   338  C  CZ3 . TRP A 1 51  ? 7.448   -7.936  18.338  1.00 9.60  ? 39  TRP A CZ3 1 
ATOM   339  C  CH2 . TRP A 1 51  ? 6.962   -6.612  18.428  1.00 11.30 ? 39  TRP A CH2 1 
ATOM   340  N  N   . SER A 1 52  ? 4.586   -11.454 23.946  1.00 11.64 ? 40  SER A N   1 
ATOM   341  C  CA  . SER A 1 52  ? 3.296   -11.455 24.633  1.00 12.24 ? 40  SER A CA  1 
ATOM   342  C  C   . SER A 1 52  ? 3.507   -10.937 26.050  1.00 12.35 ? 40  SER A C   1 
ATOM   343  O  O   . SER A 1 52  ? 4.191   -11.585 26.845  1.00 13.85 ? 40  SER A O   1 
ATOM   344  C  CB  . SER A 1 52  ? 2.699   -12.866 24.642  1.00 17.79 ? 40  SER A CB  1 
ATOM   345  O  OG  . SER A 1 52  ? 1.475   -12.868 25.334  1.00 25.97 ? 40  SER A OG  1 
ATOM   346  N  N   . ASN A 1 53  ? 2.923   -9.779  26.358  1.00 11.68 ? 41  ASN A N   1 
ATOM   347  C  CA  . ASN A 1 53  ? 3.049   -9.143  27.669  1.00 11.90 ? 41  ASN A CA  1 
ATOM   348  C  C   . ASN A 1 53  ? 4.504   -9.105  28.136  1.00 13.39 ? 41  ASN A C   1 
ATOM   349  O  O   . ASN A 1 53  ? 4.835   -9.482  29.265  1.00 12.87 ? 41  ASN A O   1 
ATOM   350  C  CB  . ASN A 1 53  ? 2.158   -9.845  28.700  1.00 12.71 ? 41  ASN A CB  1 
ATOM   351  C  CG  . ASN A 1 53  ? 0.693   -9.661  28.411  1.00 17.25 ? 41  ASN A CG  1 
ATOM   352  O  OD1 . ASN A 1 53  ? 0.215   -8.541  28.242  1.00 14.66 ? 41  ASN A OD1 1 
ATOM   353  N  ND2 . ASN A 1 53  ? -0.034  -10.771 28.348  1.00 17.91 ? 41  ASN A ND2 1 
ATOM   354  N  N   . SER A 1 54  ? 5.369   -8.606  27.259  1.00 14.35 ? 42  SER A N   1 
ATOM   355  C  CA  . SER A 1 54  ? 6.809   -8.690  27.442  1.00 12.88 ? 42  SER A CA  1 
ATOM   356  C  C   . SER A 1 54  ? 7.285   -7.780  28.569  1.00 11.17 ? 42  SER A C   1 
ATOM   357  O  O   . SER A 1 54  ? 6.628   -6.816  28.950  1.00 12.40 ? 42  SER A O   1 
ATOM   358  C  CB  . SER A 1 54  ? 7.523   -8.308  26.134  1.00 12.65 ? 42  SER A CB  1 
ATOM   359  O  OG  . SER A 1 54  ? 7.386   -6.920  25.874  1.00 12.26 ? 42  SER A OG  1 
ATOM   360  N  N   . GLY A 1 55  ? 8.458   -8.101  29.092  1.00 11.69 ? 43  GLY A N   1 
ATOM   361  C  CA  . GLY A 1 55  ? 9.257   -7.085  29.739  1.00 12.51 ? 43  GLY A CA  1 
ATOM   362  C  C   . GLY A 1 55  ? 9.979   -6.282  28.670  1.00 14.29 ? 43  GLY A C   1 
ATOM   363  O  O   . GLY A 1 55  ? 9.424   -6.031  27.590  1.00 16.59 ? 43  GLY A O   1 
ATOM   364  N  N   . ASN A 1 56  ? 11.219  -5.890  28.944  1.00 12.11 ? 44  ASN A N   1 
ATOM   365  C  CA  . ASN A 1 56  ? 12.077  -5.236  27.963  1.00 13.25 ? 44  ASN A CA  1 
ATOM   366  C  C   . ASN A 1 56  ? 12.773  -6.286  27.106  1.00 13.74 ? 44  ASN A C   1 
ATOM   367  O  O   . ASN A 1 56  ? 13.285  -7.276  27.628  1.00 11.99 ? 44  ASN A O   1 
ATOM   368  C  CB  . ASN A 1 56  ? 13.147  -4.388  28.665  1.00 14.37 ? 44  ASN A CB  1 
ATOM   369  C  CG  . ASN A 1 56  ? 12.680  -2.993  28.983  1.00 25.87 ? 44  ASN A CG  1 
ATOM   370  O  OD1 . ASN A 1 56  ? 12.601  -2.610  30.149  1.00 38.31 ? 44  ASN A OD1 1 
ATOM   371  N  ND2 . ASN A 1 56  ? 12.364  -2.220  27.950  1.00 29.85 ? 44  ASN A ND2 1 
ATOM   372  N  N   . PHE A 1 57  ? 12.808  -6.067  25.791  1.00 9.93  ? 45  PHE A N   1 
ATOM   373  C  CA  . PHE A 1 57  ? 13.597  -6.939  24.930  1.00 10.01 ? 45  PHE A CA  1 
ATOM   374  C  C   . PHE A 1 57  ? 14.105  -6.142  23.736  1.00 11.51 ? 45  PHE A C   1 
ATOM   375  O  O   . PHE A 1 57  ? 13.528  -5.123  23.356  1.00 9.71  ? 45  PHE A O   1 
ATOM   376  C  CB  . PHE A 1 57  ? 12.793  -8.166  24.443  1.00 9.22  ? 45  PHE A CB  1 
ATOM   377  C  CG  . PHE A 1 57  ? 11.789  -7.847  23.351  1.00 9.26  ? 45  PHE A CG  1 
ATOM   378  C  CD1 . PHE A 1 57  ? 10.494  -7.443  23.670  1.00 11.18 ? 45  PHE A CD1 1 
ATOM   379  C  CD2 . PHE A 1 57  ? 12.140  -7.967  22.015  1.00 10.47 ? 45  PHE A CD2 1 
ATOM   380  C  CE1 . PHE A 1 57  ? 9.578   -7.157  22.666  1.00 11.31 ? 45  PHE A CE1 1 
ATOM   381  C  CE2 . PHE A 1 57  ? 11.221  -7.678  20.994  1.00 12.93 ? 45  PHE A CE2 1 
ATOM   382  C  CZ  . PHE A 1 57  ? 9.945   -7.265  21.329  1.00 11.50 ? 45  PHE A CZ  1 
ATOM   383  N  N   . VAL A 1 58  ? 15.194  -6.633  23.133  1.00 8.13  ? 46  VAL A N   1 
ATOM   384  C  CA  . VAL A 1 58  ? 15.752  -6.058  21.910  1.00 7.41  ? 46  VAL A CA  1 
ATOM   385  C  C   . VAL A 1 58  ? 16.295  -7.201  21.068  1.00 11.17 ? 46  VAL A C   1 
ATOM   386  O  O   . VAL A 1 58  ? 17.098  -8.001  21.563  1.00 12.77 ? 46  VAL A O   1 
ATOM   387  C  CB  . VAL A 1 58  ? 16.910  -5.073  22.191  1.00 13.07 ? 46  VAL A CB  1 
ATOM   388  C  CG1 . VAL A 1 58  ? 17.497  -4.553  20.869  1.00 14.06 ? 46  VAL A CG1 1 
ATOM   389  C  CG2 . VAL A 1 58  ? 16.483  -3.938  23.091  1.00 14.41 ? 46  VAL A CG2 1 
ATOM   390  N  N   . ALA A 1 59  ? 15.927  -7.253  19.790  1.00 6.92  ? 47  ALA A N   1 
ATOM   391  C  CA  . ALA A 1 59  ? 16.372  -8.389  18.995  1.00 10.12 ? 47  ALA A CA  1 
ATOM   392  C  C   . ALA A 1 59  ? 16.622  -7.977  17.555  1.00 8.10  ? 47  ALA A C   1 
ATOM   393  O  O   . ALA A 1 59  ? 15.868  -7.173  16.990  1.00 9.28  ? 47  ALA A O   1 
ATOM   394  C  CB  . ALA A 1 59  ? 15.335  -9.513  19.021  1.00 13.14 ? 47  ALA A CB  1 
ATOM   395  N  N   . GLY A 1 60  ? 17.640  -8.563  16.943  1.00 7.18  ? 48  GLY A N   1 
ATOM   396  C  CA  . GLY A 1 60  ? 17.818  -8.317  15.524  1.00 7.67  ? 48  GLY A CA  1 
ATOM   397  C  C   . GLY A 1 60  ? 19.095  -8.902  14.959  1.00 8.92  ? 48  GLY A C   1 
ATOM   398  O  O   . GLY A 1 60  ? 19.910  -9.510  15.663  1.00 8.71  ? 48  GLY A O   1 
ATOM   399  N  N   . LYS A 1 61  ? 19.258  -8.676  13.651  1.00 9.22  ? 49  LYS A N   1 
ATOM   400  C  CA  . LYS A 1 61  ? 20.403  -9.159  12.888  1.00 8.45  ? 49  LYS A CA  1 
ATOM   401  C  C   . LYS A 1 61  ? 21.182  -7.996  12.298  1.00 8.32  ? 49  LYS A C   1 
ATOM   402  O  O   . LYS A 1 61  ? 20.626  -6.934  11.992  1.00 7.76  ? 49  LYS A O   1 
ATOM   403  C  CB  . LYS A 1 61  ? 19.979  -10.081 11.727  1.00 7.33  ? 49  LYS A CB  1 
ATOM   404  C  CG  . LYS A 1 61  ? 19.998  -11.564 12.062  1.00 8.84  ? 49  LYS A CG  1 
ATOM   405  C  CD  . LYS A 1 61  ? 19.532  -12.406 10.877  1.00 9.46  ? 49  LYS A CD  1 
ATOM   406  C  CE  . LYS A 1 61  ? 19.935  -13.875 11.072  1.00 10.81 ? 49  LYS A CE  1 
ATOM   407  N  NZ  . LYS A 1 61  ? 19.436  -14.759 9.956   1.00 11.11 ? 49  LYS A NZ  1 
ATOM   408  N  N   . GLY A 1 62  ? 22.479  -8.222  12.109  1.00 7.59  ? 50  GLY A N   1 
ATOM   409  C  CA  . GLY A 1 62  ? 23.326  -7.219  11.508  1.00 8.67  ? 50  GLY A CA  1 
ATOM   410  C  C   . GLY A 1 62  ? 24.774  -7.667  11.494  1.00 12.39 ? 50  GLY A C   1 
ATOM   411  O  O   . GLY A 1 62  ? 25.093  -8.755  10.998  1.00 10.96 ? 50  GLY A O   1 
ATOM   412  N  N   . TRP A 1 63  ? 25.643  -6.850  12.076  1.00 10.15 ? 51  TRP A N   1 
ATOM   413  C  CA  . TRP A 1 63  ? 27.086  -7.019  11.973  1.00 11.65 ? 51  TRP A CA  1 
ATOM   414  C  C   . TRP A 1 63  ? 27.723  -6.799  13.334  1.00 12.11 ? 51  TRP A C   1 
ATOM   415  O  O   . TRP A 1 63  ? 27.231  -6.017  14.148  1.00 11.40 ? 51  TRP A O   1 
ATOM   416  C  CB  . TRP A 1 63  ? 27.688  -6.025  10.969  1.00 12.18 ? 51  TRP A CB  1 
ATOM   417  C  CG  . TRP A 1 63  ? 27.086  -6.171  9.639   1.00 13.67 ? 51  TRP A CG  1 
ATOM   418  C  CD1 . TRP A 1 63  ? 27.534  -6.953  8.611   1.00 18.34 ? 51  TRP A CD1 1 
ATOM   419  C  CD2 . TRP A 1 63  ? 25.890  -5.544  9.181   1.00 14.50 ? 51  TRP A CD2 1 
ATOM   420  N  NE1 . TRP A 1 63  ? 26.689  -6.838  7.530   1.00 21.15 ? 51  TRP A NE1 1 
ATOM   421  C  CE2 . TRP A 1 63  ? 25.671  -5.979  7.855   1.00 16.51 ? 51  TRP A CE2 1 
ATOM   422  C  CE3 . TRP A 1 63  ? 24.988  -4.646  9.755   1.00 15.59 ? 51  TRP A CE3 1 
ATOM   423  C  CZ2 . TRP A 1 63  ? 24.585  -5.554  7.102   1.00 18.09 ? 51  TRP A CZ2 1 
ATOM   424  C  CZ3 . TRP A 1 63  ? 23.908  -4.223  9.005   1.00 16.93 ? 51  TRP A CZ3 1 
ATOM   425  C  CH2 . TRP A 1 63  ? 23.715  -4.679  7.691   1.00 18.64 ? 51  TRP A CH2 1 
ATOM   426  N  N   . ASN A 1 64  ? 28.848  -7.473  13.564  1.00 12.18 ? 52  ASN A N   1 
ATOM   427  C  CA  . ASN A 1 64  ? 29.611  -7.203  14.774  1.00 12.29 ? 52  ASN A CA  1 
ATOM   428  C  C   . ASN A 1 64  ? 31.091  -7.379  14.459  1.00 12.75 ? 52  ASN A C   1 
ATOM   429  O  O   . ASN A 1 64  ? 31.544  -8.513  14.272  1.00 17.35 ? 52  ASN A O   1 
ATOM   430  C  CB  . ASN A 1 64  ? 29.186  -8.127  15.916  1.00 12.47 ? 52  ASN A CB  1 
ATOM   431  C  CG  . ASN A 1 64  ? 29.859  -7.764  17.236  1.00 14.77 ? 52  ASN A CG  1 
ATOM   432  O  OD1 . ASN A 1 64  ? 30.469  -6.708  17.353  1.00 14.88 ? 52  ASN A OD1 1 
ATOM   433  N  ND2 . ASN A 1 64  ? 29.743  -8.635  18.230  1.00 20.02 ? 52  ASN A ND2 1 
ATOM   434  N  N   . PRO A 1 65  ? 31.875  -6.294  14.396  1.00 13.69 ? 53  PRO A N   1 
ATOM   435  C  CA  . PRO A 1 65  ? 31.427  -4.929  14.662  1.00 14.21 ? 53  PRO A CA  1 
ATOM   436  C  C   . PRO A 1 65  ? 30.720  -4.291  13.480  1.00 12.75 ? 53  PRO A C   1 
ATOM   437  O  O   . PRO A 1 65  ? 30.944  -4.700  12.335  1.00 15.04 ? 53  PRO A O   1 
ATOM   438  C  CB  . PRO A 1 65  ? 32.735  -4.184  14.947  1.00 14.90 ? 53  PRO A CB  1 
ATOM   439  C  CG  . PRO A 1 65  ? 33.730  -4.887  14.084  1.00 16.83 ? 53  PRO A CG  1 
ATOM   440  C  CD  . PRO A 1 65  ? 33.325  -6.347  14.100  1.00 17.16 ? 53  PRO A CD  1 
ATOM   441  N  N   . GLY A 1 66  ? 29.879  -3.294  13.757  1.00 12.82 ? 54  GLY A N   1 
ATOM   442  C  CA  . GLY A 1 66  ? 29.387  -2.447  12.691  1.00 14.30 ? 54  GLY A CA  1 
ATOM   443  C  C   . GLY A 1 66  ? 30.503  -1.597  12.110  1.00 17.36 ? 54  GLY A C   1 
ATOM   444  O  O   . GLY A 1 66  ? 31.503  -1.302  12.768  1.00 16.22 ? 54  GLY A O   1 
ATOM   445  N  N   . SER A 1 67  ? 30.346  -1.213  10.844  1.00 14.72 ? 55  SER A N   1 
ATOM   446  C  CA  . SER A 1 67  ? 31.335  -0.344  10.208  1.00 17.65 ? 55  SER A CA  1 
ATOM   447  C  C   . SER A 1 67  ? 30.651  0.739   9.390   1.00 19.36 ? 55  SER A C   1 
ATOM   448  O  O   . SER A 1 67  ? 31.052  1.041   8.260   1.00 20.75 ? 55  SER A O   1 
ATOM   449  C  CB  . SER A 1 67  ? 32.309  -1.144  9.351   1.00 20.74 ? 55  SER A CB  1 
ATOM   450  O  OG  . SER A 1 67  ? 31.623  -1.872  8.360   1.00 24.00 ? 55  SER A OG  1 
ATOM   451  N  N   . SER A 1 68  ? 29.604  1.340   9.960   1.00 15.63 ? 56  SER A N   1 
ATOM   452  C  CA  . SER A 1 68  ? 28.944  2.513   9.387   1.00 17.95 ? 56  SER A CA  1 
ATOM   453  C  C   . SER A 1 68  ? 28.411  2.248   7.982   1.00 18.49 ? 56  SER A C   1 
ATOM   454  O  O   . SER A 1 68  ? 28.364  3.151   7.140   1.00 23.26 ? 56  SER A O   1 
ATOM   455  C  CB  . SER A 1 68  ? 29.885  3.726   9.390   1.00 20.51 ? 56  SER A CB  1 
ATOM   456  O  OG  . SER A 1 68  ? 30.430  3.940   10.683  1.00 20.72 ? 56  SER A OG  1 
ATOM   457  N  N   . GLN A 1 69  ? 27.970  1.027   7.715   1.00 19.90 ? 57  GLN A N   1 
ATOM   458  C  CA  . GLN A 1 69  ? 27.522  0.759   6.359   1.00 20.80 ? 57  GLN A CA  1 
ATOM   459  C  C   . GLN A 1 69  ? 26.118  1.301   6.125   1.00 17.55 ? 57  GLN A C   1 
ATOM   460  O  O   . GLN A 1 69  ? 25.384  1.666   7.049   1.00 15.27 ? 57  GLN A O   1 
ATOM   461  C  CB  . GLN A 1 69  ? 27.552  -0.734  6.040   1.00 23.60 ? 57  GLN A CB  1 
ATOM   462  C  CG  . GLN A 1 69  ? 26.878  -1.619  7.057   1.00 20.91 ? 57  GLN A CG  1 
ATOM   463  C  CD  . GLN A 1 69  ? 27.880  -2.182  8.040   1.00 22.36 ? 57  GLN A CD  1 
ATOM   464  O  OE1 . GLN A 1 69  ? 28.335  -1.479  8.934   1.00 20.46 ? 57  GLN A OE1 1 
ATOM   465  N  NE2 . GLN A 1 69  ? 28.243  -3.447  7.865   1.00 24.03 ? 57  GLN A NE2 1 
ATOM   466  N  N   . THR A 1 70  ? 25.768  1.374   4.848   1.00 15.65 ? 58  THR A N   1 
ATOM   467  C  CA  . THR A 1 70  ? 24.422  1.731   4.432   1.00 14.62 ? 58  THR A CA  1 
ATOM   468  C  C   . THR A 1 70  ? 23.553  0.479   4.454   1.00 17.65 ? 58  THR A C   1 
ATOM   469  O  O   . THR A 1 70  ? 23.856  -0.507  3.778   1.00 22.53 ? 58  THR A O   1 
ATOM   470  C  CB  . THR A 1 70  ? 24.470  2.360   3.046   1.00 19.79 ? 58  THR A CB  1 
ATOM   471  O  OG1 . THR A 1 70  ? 25.246  3.564   3.119   1.00 20.63 ? 58  THR A OG1 1 
ATOM   472  C  CG2 . THR A 1 70  ? 23.079  2.690   2.564   1.00 17.35 ? 58  THR A CG2 1 
ATOM   473  N  N   . ILE A 1 71  ? 22.482  0.515   5.238   1.00 13.60 ? 59  ILE A N   1 
ATOM   474  C  CA  . ILE A 1 71  ? 21.675  -0.660  5.534   1.00 14.78 ? 59  ILE A CA  1 
ATOM   475  C  C   . ILE A 1 71  ? 20.411  -0.611  4.691   1.00 14.07 ? 59  ILE A C   1 
ATOM   476  O  O   . ILE A 1 71  ? 19.753  0.430   4.618   1.00 15.77 ? 59  ILE A O   1 
ATOM   477  C  CB  . ILE A 1 71  ? 21.312  -0.710  7.027   1.00 12.87 ? 59  ILE A CB  1 
ATOM   478  C  CG1 . ILE A 1 71  ? 22.567  -0.868  7.882   1.00 14.98 ? 59  ILE A CG1 1 
ATOM   479  C  CG2 . ILE A 1 71  ? 20.323  -1.847  7.290   1.00 15.89 ? 59  ILE A CG2 1 
ATOM   480  C  CD1 . ILE A 1 71  ? 22.279  -0.794  9.380   1.00 16.03 ? 59  ILE A CD1 1 
ATOM   481  N  N   . THR A 1 72  ? 20.061  -1.731  4.071   1.00 10.59 ? 60  THR A N   1 
ATOM   482  C  CA  . THR A 1 72  ? 18.740  -1.907  3.477   1.00 14.12 ? 60  THR A CA  1 
ATOM   483  C  C   . THR A 1 72  ? 18.009  -2.989  4.251   1.00 13.05 ? 60  THR A C   1 
ATOM   484  O  O   . THR A 1 72  ? 18.568  -4.064  4.500   1.00 16.51 ? 60  THR A O   1 
ATOM   485  C  CB  . THR A 1 72  ? 18.830  -2.293  1.998   1.00 19.26 ? 60  THR A CB  1 
ATOM   486  O  OG1 . THR A 1 72  ? 19.712  -3.410  1.858   1.00 35.51 ? 60  THR A OG1 1 
ATOM   487  C  CG2 . THR A 1 72  ? 19.341  -1.143  1.174   1.00 19.44 ? 60  THR A CG2 1 
ATOM   488  N  N   . TYR A 1 73  ? 16.773  -2.711  4.645   1.00 10.80 ? 61  TYR A N   1 
ATOM   489  C  CA  . TYR A 1 73  ? 16.017  -3.716  5.364   1.00 12.88 ? 61  TYR A CA  1 
ATOM   490  C  C   . TYR A 1 73  ? 14.586  -3.724  4.851   1.00 13.19 ? 61  TYR A C   1 
ATOM   491  O  O   . TYR A 1 73  ? 14.105  -2.753  4.261   1.00 12.85 ? 61  TYR A O   1 
ATOM   492  C  CB  . TYR A 1 73  ? 16.078  -3.478  6.885   1.00 13.18 ? 61  TYR A CB  1 
ATOM   493  C  CG  . TYR A 1 73  ? 15.253  -2.308  7.332   1.00 13.99 ? 61  TYR A CG  1 
ATOM   494  C  CD1 . TYR A 1 73  ? 15.707  -1.012  7.164   1.00 12.38 ? 61  TYR A CD1 1 
ATOM   495  C  CD2 . TYR A 1 73  ? 13.993  -2.502  7.870   1.00 14.32 ? 61  TYR A CD2 1 
ATOM   496  C  CE1 . TYR A 1 73  ? 14.937  0.065   7.543   1.00 14.38 ? 61  TYR A CE1 1 
ATOM   497  C  CE2 . TYR A 1 73  ? 13.223  -1.437  8.258   1.00 15.07 ? 61  TYR A CE2 1 
ATOM   498  C  CZ  . TYR A 1 73  ? 13.691  -0.162  8.092   1.00 13.03 ? 61  TYR A CZ  1 
ATOM   499  O  OH  . TYR A 1 73  ? 12.903  0.904   8.463   1.00 17.61 ? 61  TYR A OH  1 
ATOM   500  N  N   . SER A 1 74  ? 13.920  -4.852  5.069   1.00 11.34 ? 62  SER A N   1 
ATOM   501  C  CA  . SER A 1 74  ? 12.571  -5.078  4.560   1.00 11.92 ? 62  SER A CA  1 
ATOM   502  C  C   . SER A 1 74  ? 11.807  -5.932  5.562   1.00 13.86 ? 62  SER A C   1 
ATOM   503  O  O   . SER A 1 74  ? 12.383  -6.498  6.498   1.00 11.20 ? 62  SER A O   1 
ATOM   504  C  CB  . SER A 1 74  ? 12.609  -5.763  3.181   1.00 16.46 ? 62  SER A CB  1 
ATOM   505  O  OG  . SER A 1 74  ? 13.142  -7.076  3.290   1.00 21.43 ? 62  SER A OG  1 
ATOM   506  N  N   . GLY A 1 75  ? 10.493  -6.016  5.357   1.00 11.13 ? 63  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 75  ? 9.669   -6.901  6.153   1.00 12.77 ? 63  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 75  ? 8.456   -6.226  6.765   1.00 9.43  ? 63  GLY A C   1 
ATOM   509  O  O   . GLY A 1 75  ? 7.924   -5.250  6.228   1.00 9.94  ? 63  GLY A O   1 
ATOM   510  N  N   . GLU A 1 76  ? 8.019   -6.736  7.908   1.00 9.24  ? 64  GLU A N   1 
ATOM   511  C  CA  . GLU A 1 76  ? 6.826   -6.213  8.551   1.00 9.33  ? 64  GLU A CA  1 
ATOM   512  C  C   . GLU A 1 76  ? 7.052   -6.172  10.052  1.00 9.66  ? 64  GLU A C   1 
ATOM   513  O  O   . GLU A 1 76  ? 7.843   -6.940  10.602  1.00 10.32 ? 64  GLU A O   1 
ATOM   514  C  CB  . GLU A 1 76  ? 5.592   -7.046  8.226   1.00 12.72 ? 64  GLU A CB  1 
ATOM   515  C  CG  . GLU A 1 76  ? 5.706   -8.459  8.705   1.00 16.38 ? 64  GLU A CG  1 
ATOM   516  C  CD  . GLU A 1 76  ? 4.547   -9.311  8.252   1.00 23.07 ? 64  GLU A CD  1 
ATOM   517  O  OE1 . GLU A 1 76  ? 3.557   -8.762  7.723   1.00 25.37 ? 64  GLU A OE1 1 
ATOM   518  O  OE2 . GLU A 1 76  ? 4.632   -10.538 8.431   1.00 23.98 ? 64  GLU A OE2 1 
ATOM   519  N  N   . TRP A 1 77  ? 6.351   -5.250  10.697  1.00 8.28  ? 65  TRP A N   1 
ATOM   520  C  CA  . TRP A 1 77  ? 6.523   -4.948  12.111  1.00 8.95  ? 65  TRP A CA  1 
ATOM   521  C  C   . TRP A 1 77  ? 5.132   -4.636  12.642  1.00 10.57 ? 65  TRP A C   1 
ATOM   522  O  O   . TRP A 1 77  ? 4.543   -3.619  12.274  1.00 10.51 ? 65  TRP A O   1 
ATOM   523  C  CB  . TRP A 1 77  ? 7.493   -3.777  12.272  1.00 10.18 ? 65  TRP A CB  1 
ATOM   524  C  CG  . TRP A 1 77  ? 7.613   -3.160  13.628  1.00 10.46 ? 65  TRP A CG  1 
ATOM   525  C  CD1 . TRP A 1 77  ? 8.298   -3.648  14.711  1.00 11.77 ? 65  TRP A CD1 1 
ATOM   526  C  CD2 . TRP A 1 77  ? 7.082   -1.892  14.025  1.00 10.50 ? 65  TRP A CD2 1 
ATOM   527  N  NE1 . TRP A 1 77  ? 8.205   -2.761  15.761  1.00 12.23 ? 65  TRP A NE1 1 
ATOM   528  C  CE2 . TRP A 1 77  ? 7.465   -1.676  15.367  1.00 11.49 ? 65  TRP A CE2 1 
ATOM   529  C  CE3 . TRP A 1 77  ? 6.316   -0.917  13.373  1.00 12.92 ? 65  TRP A CE3 1 
ATOM   530  C  CZ2 . TRP A 1 77  ? 7.109   -0.525  16.068  1.00 11.92 ? 65  TRP A CZ2 1 
ATOM   531  C  CZ3 . TRP A 1 77  ? 5.951   0.212   14.074  1.00 13.61 ? 65  TRP A CZ3 1 
ATOM   532  C  CH2 . TRP A 1 77  ? 6.343   0.401   15.403  1.00 12.29 ? 65  TRP A CH2 1 
ATOM   533  N  N   . ASN A 1 78  ? 4.600   -5.522  13.482  1.00 8.95  ? 66  ASN A N   1 
ATOM   534  C  CA  . ASN A 1 78  ? 3.196   -5.489  13.892  1.00 10.57 ? 66  ASN A CA  1 
ATOM   535  C  C   . ASN A 1 78  ? 3.066   -5.474  15.410  1.00 8.95  ? 66  ASN A C   1 
ATOM   536  O  O   . ASN A 1 78  ? 2.632   -6.462  16.013  1.00 10.77 ? 66  ASN A O   1 
ATOM   537  C  CB  . ASN A 1 78  ? 2.448   -6.689  13.311  1.00 11.42 ? 66  ASN A CB  1 
ATOM   538  C  CG  . ASN A 1 78  ? 2.493   -6.712  11.811  1.00 15.89 ? 66  ASN A CG  1 
ATOM   539  O  OD1 . ASN A 1 78  ? 1.964   -5.813  11.163  1.00 19.59 ? 66  ASN A OD1 1 
ATOM   540  N  ND2 . ASN A 1 78  ? 3.129   -7.730  11.250  1.00 19.25 ? 66  ASN A ND2 1 
ATOM   541  N  N   . PRO A 1 79  ? 3.387   -4.355  16.054  1.00 11.39 ? 67  PRO A N   1 
ATOM   542  C  CA  . PRO A 1 79  ? 3.259   -4.282  17.515  1.00 10.51 ? 67  PRO A CA  1 
ATOM   543  C  C   . PRO A 1 79  ? 1.829   -3.995  17.938  1.00 13.11 ? 67  PRO A C   1 
ATOM   544  O  O   . PRO A 1 79  ? 1.051   -3.378  17.212  1.00 14.60 ? 67  PRO A O   1 
ATOM   545  C  CB  . PRO A 1 79  ? 4.163   -3.105  17.881  1.00 12.16 ? 67  PRO A CB  1 
ATOM   546  C  CG  . PRO A 1 79  ? 4.010   -2.180  16.700  1.00 12.83 ? 67  PRO A CG  1 
ATOM   547  C  CD  . PRO A 1 79  ? 3.869   -3.080  15.487  1.00 14.95 ? 67  PRO A CD  1 
ATOM   548  N  N   . ASN A 1 80  ? 1.500   -4.442  19.142  1.00 12.84 ? 68  ASN A N   1 
ATOM   549  C  CA  . ASN A 1 80  ? 0.278   -4.038  19.832  1.00 14.68 ? 68  ASN A CA  1 
ATOM   550  C  C   . ASN A 1 80  ? 0.755   -3.452  21.156  1.00 12.42 ? 68  ASN A C   1 
ATOM   551  O  O   . ASN A 1 80  ? 0.853   -4.156  22.162  1.00 13.02 ? 68  ASN A O   1 
ATOM   552  C  CB  . ASN A 1 80  ? -0.686  -5.194  20.034  1.00 14.31 ? 68  ASN A CB  1 
ATOM   553  C  CG  . ASN A 1 80  ? -1.976  -4.758  20.729  1.00 23.67 ? 68  ASN A CG  1 
ATOM   554  O  OD1 . ASN A 1 80  ? -2.520  -5.484  21.567  1.00 33.57 ? 68  ASN A OD1 1 
ATOM   555  N  ND2 . ASN A 1 80  ? -2.461  -3.566  20.391  1.00 25.89 ? 68  ASN A ND2 1 
ATOM   556  N  N   . GLY A 1 81  ? 1.078   -2.170  21.145  1.00 13.28 ? 69  GLY A N   1 
ATOM   557  C  CA  . GLY A 1 81  ? 1.683   -1.514  22.287  1.00 15.41 ? 69  GLY A CA  1 
ATOM   558  C  C   . GLY A 1 81  ? 3.101   -1.066  21.981  1.00 13.37 ? 69  GLY A C   1 
ATOM   559  O  O   . GLY A 1 81  ? 3.548   -1.052  20.833  1.00 14.32 ? 69  GLY A O   1 
ATOM   560  N  N   . ASN A 1 82  ? 3.818   -0.724  23.042  1.00 11.87 ? 70  ASN A N   1 
ATOM   561  C  CA  . ASN A 1 82  ? 5.109   -0.035  22.957  1.00 10.98 ? 70  ASN A CA  1 
ATOM   562  C  C   . ASN A 1 82  ? 6.177   -0.887  22.278  1.00 10.70 ? 70  ASN A C   1 
ATOM   563  O  O   . ASN A 1 82  ? 6.569   -1.943  22.796  1.00 9.94  ? 70  ASN A O   1 
ATOM   564  C  CB  . ASN A 1 82  ? 5.533   0.332   24.378  1.00 11.78 ? 70  ASN A CB  1 
ATOM   565  C  CG  . ASN A 1 82  ? 6.823   1.135   24.451  1.00 12.70 ? 70  ASN A CG  1 
ATOM   566  O  OD1 . ASN A 1 82  ? 7.461   1.462   23.442  1.00 14.47 ? 70  ASN A OD1 1 
ATOM   567  N  ND2 . ASN A 1 82  ? 7.226   1.449   25.677  1.00 18.40 ? 70  ASN A ND2 1 
ATOM   568  N  N   . SER A 1 83  ? 6.673   -0.400  21.137  1.00 10.00 ? 71  SER A N   1 
ATOM   569  C  CA  . SER A 1 83  ? 7.708   -1.106  20.392  1.00 8.89  ? 71  SER A CA  1 
ATOM   570  C  C   . SER A 1 83  ? 8.443   -0.091  19.519  1.00 10.96 ? 71  SER A C   1 
ATOM   571  O  O   . SER A 1 83  ? 7.851   0.907   19.099  1.00 12.35 ? 71  SER A O   1 
ATOM   572  C  CB  . SER A 1 83  ? 7.078   -2.210  19.537  1.00 9.07  ? 71  SER A CB  1 
ATOM   573  O  OG  . SER A 1 83  ? 8.035   -2.898  18.758  1.00 10.57 ? 71  SER A OG  1 
ATOM   574  N  N   . TYR A 1 84  ? 9.735   -0.344  19.258  1.00 10.28 ? 72  TYR A N   1 
ATOM   575  C  CA  . TYR A 1 84  ? 10.557  0.465   18.350  1.00 13.09 ? 72  TYR A CA  1 
ATOM   576  C  C   . TYR A 1 84  ? 11.111  -0.441  17.260  1.00 9.94  ? 72  TYR A C   1 
ATOM   577  O  O   . TYR A 1 84  ? 11.435  -1.592  17.531  1.00 10.29 ? 72  TYR A O   1 
ATOM   578  C  CB  . TYR A 1 84  ? 11.794  1.164   19.031  1.00 13.39 ? 72  TYR A CB  1 
ATOM   579  C  CG  . TYR A 1 84  ? 11.651  1.766   20.403  1.00 13.56 ? 72  TYR A CG  1 
ATOM   580  C  CD1 . TYR A 1 84  ? 10.503  2.439   20.782  1.00 15.69 ? 72  TYR A CD1 1 
ATOM   581  C  CD2 . TYR A 1 84  ? 12.703  1.688   21.321  1.00 17.92 ? 72  TYR A CD2 1 
ATOM   582  C  CE1 . TYR A 1 84  ? 10.379  2.998   22.053  1.00 20.58 ? 72  TYR A CE1 1 
ATOM   583  C  CE2 . TYR A 1 84  ? 12.590  2.239   22.597  1.00 22.88 ? 72  TYR A CE2 1 
ATOM   584  C  CZ  . TYR A 1 84  ? 11.422  2.896   22.956  1.00 27.80 ? 72  TYR A CZ  1 
ATOM   585  O  OH  . TYR A 1 84  ? 11.293  3.458   24.218  1.00 27.42 ? 72  TYR A OH  1 
ATOM   586  N  N   . LEU A 1 85  ? 11.237  0.087   16.042  1.00 10.14 ? 73  LEU A N   1 
ATOM   587  C  CA  . LEU A 1 85  ? 11.973  -0.549  14.953  1.00 9.53  ? 73  LEU A CA  1 
ATOM   588  C  C   . LEU A 1 85  ? 13.119  0.388   14.608  1.00 10.47 ? 73  LEU A C   1 
ATOM   589  O  O   . LEU A 1 85  ? 12.868  1.527   14.213  1.00 8.70  ? 73  LEU A O   1 
ATOM   590  C  CB  . LEU A 1 85  ? 11.075  -0.779  13.726  1.00 9.21  ? 73  LEU A CB  1 
ATOM   591  C  CG  . LEU A 1 85  ? 11.734  -1.408  12.495  1.00 11.57 ? 73  LEU A CG  1 
ATOM   592  C  CD1 . LEU A 1 85  ? 12.251  -2.820  12.828  1.00 14.62 ? 73  LEU A CD1 1 
ATOM   593  C  CD2 . LEU A 1 85  ? 10.768  -1.454  11.292  1.00 12.30 ? 73  LEU A CD2 1 
ATOM   594  N  N   . SER A 1 86  ? 14.367  -0.070  14.775  1.00 8.58  ? 74  SER A N   1 
ATOM   595  C  CA  . SER A 1 86  ? 15.499  0.851   14.693  1.00 8.64  ? 74  SER A CA  1 
ATOM   596  C  C   . SER A 1 86  ? 16.735  0.168   14.129  1.00 9.55  ? 74  SER A C   1 
ATOM   597  O  O   . SER A 1 86  ? 16.887  -1.055  14.211  1.00 10.75 ? 74  SER A O   1 
ATOM   598  C  CB  . SER A 1 86  ? 15.874  1.420   16.071  1.00 10.83 ? 74  SER A CB  1 
ATOM   599  O  OG  . SER A 1 86  ? 14.716  1.635   16.855  1.00 17.17 ? 74  SER A OG  1 
ATOM   600  N  N   . VAL A 1 87  ? 17.642  0.978   13.584  1.00 7.67  ? 75  VAL A N   1 
ATOM   601  C  CA  . VAL A 1 87  ? 19.038  0.558   13.494  1.00 6.33  ? 75  VAL A CA  1 
ATOM   602  C  C   . VAL A 1 87  ? 19.651  0.844   14.856  1.00 8.11  ? 75  VAL A C   1 
ATOM   603  O  O   . VAL A 1 87  ? 19.590  1.975   15.342  1.00 11.33 ? 75  VAL A O   1 
ATOM   604  C  CB  . VAL A 1 87  ? 19.798  1.293   12.378  1.00 7.19  ? 75  VAL A CB  1 
ATOM   605  C  CG1 . VAL A 1 87  ? 21.316  0.959   12.480  1.00 9.13  ? 75  VAL A CG1 1 
ATOM   606  C  CG2 . VAL A 1 87  ? 19.259  0.920   11.007  1.00 9.10  ? 75  VAL A CG2 1 
ATOM   607  N  N   . TYR A 1 88  ? 20.224  -0.177  15.475  1.00 7.46  ? 76  TYR A N   1 
ATOM   608  C  CA  . TYR A 1 88  ? 20.524  -0.153  16.897  1.00 5.91  ? 76  TYR A CA  1 
ATOM   609  C  C   . TYR A 1 88  ? 21.925  -0.695  17.099  1.00 7.06  ? 76  TYR A C   1 
ATOM   610  O  O   . TYR A 1 88  ? 22.304  -1.677  16.459  1.00 8.51  ? 76  TYR A O   1 
ATOM   611  C  CB  . TYR A 1 88  ? 19.493  -1.011  17.653  1.00 8.24  ? 76  TYR A CB  1 
ATOM   612  C  CG  . TYR A 1 88  ? 19.840  -1.326  19.086  1.00 9.88  ? 76  TYR A CG  1 
ATOM   613  C  CD1 . TYR A 1 88  ? 19.689  -0.377  20.082  1.00 10.53 ? 76  TYR A CD1 1 
ATOM   614  C  CD2 . TYR A 1 88  ? 20.280  -2.591  19.446  1.00 10.00 ? 76  TYR A CD2 1 
ATOM   615  C  CE1 . TYR A 1 88  ? 20.002  -0.668  21.406  1.00 10.52 ? 76  TYR A CE1 1 
ATOM   616  C  CE2 . TYR A 1 88  ? 20.591  -2.898  20.765  1.00 10.08 ? 76  TYR A CE2 1 
ATOM   617  C  CZ  . TYR A 1 88  ? 20.443  -1.933  21.740  1.00 11.25 ? 76  TYR A CZ  1 
ATOM   618  O  OH  . TYR A 1 88  ? 20.750  -2.240  23.052  1.00 11.76 ? 76  TYR A OH  1 
ATOM   619  N  N   . GLY A 1 89  ? 22.693  -0.067  17.979  1.00 7.81  ? 77  GLY A N   1 
ATOM   620  C  CA  . GLY A 1 89  ? 23.985  -0.654  18.267  1.00 7.62  ? 77  GLY A CA  1 
ATOM   621  C  C   . GLY A 1 89  ? 24.697  0.036   19.405  1.00 8.45  ? 77  GLY A C   1 
ATOM   622  O  O   . GLY A 1 89  ? 24.112  0.826   20.153  1.00 8.54  ? 77  GLY A O   1 
ATOM   623  N  N   . TRP A 1 90  ? 25.984  -0.291  19.523  1.00 8.58  ? 78  TRP A N   1 
ATOM   624  C  CA  . TRP A 1 90  ? 26.798  0.146   20.653  1.00 7.87  ? 78  TRP A CA  1 
ATOM   625  C  C   . TRP A 1 90  ? 28.173  0.577   20.168  1.00 8.34  ? 78  TRP A C   1 
ATOM   626  O  O   . TRP A 1 90  ? 28.694  0.032   19.193  1.00 8.83  ? 78  TRP A O   1 
ATOM   627  C  CB  . TRP A 1 90  ? 26.995  -0.975  21.678  1.00 8.55  ? 78  TRP A CB  1 
ATOM   628  C  CG  . TRP A 1 90  ? 25.752  -1.380  22.413  1.00 9.54  ? 78  TRP A CG  1 
ATOM   629  C  CD1 . TRP A 1 90  ? 24.768  -2.219  21.960  1.00 10.06 ? 78  TRP A CD1 1 
ATOM   630  C  CD2 . TRP A 1 90  ? 25.355  -0.966  23.725  1.00 11.45 ? 78  TRP A CD2 1 
ATOM   631  N  NE1 . TRP A 1 90  ? 23.784  -2.347  22.909  1.00 9.81  ? 78  TRP A NE1 1 
ATOM   632  C  CE2 . TRP A 1 90  ? 24.122  -1.592  24.005  1.00 11.86 ? 78  TRP A CE2 1 
ATOM   633  C  CE3 . TRP A 1 90  ? 25.927  -0.127  24.697  1.00 9.58  ? 78  TRP A CE3 1 
ATOM   634  C  CZ2 . TRP A 1 90  ? 23.443  -1.405  25.213  1.00 11.81 ? 78  TRP A CZ2 1 
ATOM   635  C  CZ3 . TRP A 1 90  ? 25.256  0.054   25.898  1.00 11.58 ? 78  TRP A CZ3 1 
ATOM   636  C  CH2 . TRP A 1 90  ? 24.028  -0.591  26.149  1.00 12.23 ? 78  TRP A CH2 1 
ATOM   637  N  N   . THR A 1 91  ? 28.753  1.565   20.853  1.00 9.32  ? 79  THR A N   1 
ATOM   638  C  CA  . THR A 1 91  ? 30.194  1.781   20.805  1.00 9.28  ? 79  THR A CA  1 
ATOM   639  C  C   . THR A 1 91  ? 30.777  1.525   22.192  1.00 7.95  ? 79  THR A C   1 
ATOM   640  O  O   . THR A 1 91  ? 30.065  1.486   23.195  1.00 9.15  ? 79  THR A O   1 
ATOM   641  C  CB  . THR A 1 91  ? 30.608  3.197   20.328  1.00 10.80 ? 79  THR A CB  1 
ATOM   642  O  OG1 . THR A 1 91  ? 30.329  4.170   21.338  1.00 11.81 ? 79  THR A OG1 1 
ATOM   643  C  CG2 . THR A 1 91  ? 29.904  3.589   19.041  1.00 12.12 ? 79  THR A CG2 1 
ATOM   644  N  N   . GLN A 1 92  ? 32.086  1.312   22.225  1.00 10.17 ? 80  GLN A N   1 
ATOM   645  C  CA  . GLN A 1 92  ? 32.823  1.144   23.471  1.00 9.67  ? 80  GLN A CA  1 
ATOM   646  C  C   . GLN A 1 92  ? 33.883  2.232   23.587  1.00 10.63 ? 80  GLN A C   1 
ATOM   647  O  O   . GLN A 1 92  ? 34.437  2.690   22.581  1.00 12.22 ? 80  GLN A O   1 
ATOM   648  C  CB  . GLN A 1 92  ? 33.482  -0.240  23.532  1.00 11.73 ? 80  GLN A CB  1 
ATOM   649  C  CG  . GLN A 1 92  ? 32.477  -1.383  23.690  1.00 13.84 ? 80  GLN A CG  1 
ATOM   650  C  CD  . GLN A 1 92  ? 33.048  -2.706  23.246  1.00 20.72 ? 80  GLN A CD  1 
ATOM   651  O  OE1 . GLN A 1 92  ? 33.378  -2.884  22.074  1.00 24.96 ? 80  GLN A OE1 1 
ATOM   652  N  NE2 . GLN A 1 92  ? 33.181  -3.641  24.181  1.00 24.41 ? 80  GLN A NE2 1 
ATOM   653  N  N   . ASN A 1 93  ? 34.143  2.655   24.822  1.00 11.30 ? 81  ASN A N   1 
ATOM   654  C  CA  . ASN A 1 93  ? 35.244  3.572   25.113  1.00 10.64 ? 81  ASN A CA  1 
ATOM   655  C  C   . ASN A 1 93  ? 35.160  4.854   24.281  1.00 12.57 ? 81  ASN A C   1 
ATOM   656  O  O   . ASN A 1 93  ? 36.045  5.125   23.455  1.00 12.56 ? 81  ASN A O   1 
ATOM   657  C  CB  . ASN A 1 93  ? 36.566  2.848   24.865  1.00 12.53 ? 81  ASN A CB  1 
ATOM   658  C  CG  . ASN A 1 93  ? 37.745  3.652   25.331  1.00 13.65 ? 81  ASN A CG  1 
ATOM   659  O  OD1 . ASN A 1 93  ? 37.613  4.489   26.216  1.00 12.50 ? 81  ASN A OD1 1 
ATOM   660  N  ND2 . ASN A 1 93  ? 38.908  3.412   24.733  1.00 16.87 ? 81  ASN A ND2 1 
ATOM   661  N  N   . PRO A 1 94  ? 34.128  5.693   24.478  1.00 11.34 ? 82  PRO A N   1 
ATOM   662  C  CA  . PRO A 1 94  ? 33.110  5.575   25.520  1.00 11.61 ? 82  PRO A CA  1 
ATOM   663  C  C   . PRO A 1 94  ? 31.969  4.624   25.159  1.00 12.53 ? 82  PRO A C   1 
ATOM   664  O  O   . PRO A 1 94  ? 31.606  4.464   23.983  1.00 11.24 ? 82  PRO A O   1 
ATOM   665  C  CB  . PRO A 1 94  ? 32.580  7.004   25.645  1.00 13.01 ? 82  PRO A CB  1 
ATOM   666  C  CG  . PRO A 1 94  ? 32.686  7.540   24.255  1.00 14.05 ? 82  PRO A CG  1 
ATOM   667  C  CD  . PRO A 1 94  ? 33.957  6.923   23.686  1.00 11.61 ? 82  PRO A CD  1 
ATOM   668  N  N   . LEU A 1 95  ? 31.430  4.008   26.197  1.00 11.00 ? 83  LEU A N   1 
ATOM   669  C  CA  . LEU A 1 95  ? 30.264  3.144   26.061  1.00 11.57 ? 83  LEU A CA  1 
ATOM   670  C  C   . LEU A 1 95  ? 29.040  3.974   25.677  1.00 12.24 ? 83  LEU A C   1 
ATOM   671  O  O   . LEU A 1 95  ? 28.648  4.901   26.397  1.00 11.26 ? 83  LEU A O   1 
ATOM   672  C  CB  . LEU A 1 95  ? 30.044  2.405   27.376  1.00 9.19  ? 83  LEU A CB  1 
ATOM   673  C  CG  . LEU A 1 95  ? 28.937  1.359   27.465  1.00 10.90 ? 83  LEU A CG  1 
ATOM   674  C  CD1 . LEU A 1 95  ? 29.167  0.258   26.439  1.00 9.39  ? 83  LEU A CD1 1 
ATOM   675  C  CD2 . LEU A 1 95  ? 28.870  0.797   28.885  1.00 13.24 ? 83  LEU A CD2 1 
ATOM   676  N  N   . VAL A 1 96  ? 28.430  3.642   24.542  1.00 8.26  ? 84  VAL A N   1 
ATOM   677  C  CA  . VAL A 1 96  ? 27.291  4.394   24.018  1.00 8.07  ? 84  VAL A CA  1 
ATOM   678  C  C   . VAL A 1 96  ? 26.296  3.405   23.441  1.00 8.45  ? 84  VAL A C   1 
ATOM   679  O  O   . VAL A 1 96  ? 26.673  2.514   22.677  1.00 9.07  ? 84  VAL A O   1 
ATOM   680  C  CB  . VAL A 1 96  ? 27.712  5.392   22.922  1.00 10.21 ? 84  VAL A CB  1 
ATOM   681  C  CG1 . VAL A 1 96  ? 26.475  5.964   22.234  1.00 9.96  ? 84  VAL A CG1 1 
ATOM   682  C  CG2 . VAL A 1 96  ? 28.559  6.522   23.492  1.00 10.88 ? 84  VAL A CG2 1 
ATOM   683  N  N   . GLU A 1 97  ? 25.019  3.595   23.757  1.00 8.25  ? 85  GLU A N   1 
ATOM   684  C  CA  . GLU A 1 97  ? 23.942  2.879   23.091  1.00 9.97  ? 85  GLU A CA  1 
ATOM   685  C  C   . GLU A 1 97  ? 23.285  3.846   22.113  1.00 8.00  ? 85  GLU A C   1 
ATOM   686  O  O   . GLU A 1 97  ? 22.987  4.978   22.486  1.00 8.78  ? 85  GLU A O   1 
ATOM   687  C  CB  . GLU A 1 97  ? 22.930  2.373   24.120  1.00 8.57  ? 85  GLU A CB  1 
ATOM   688  C  CG  . GLU A 1 97  ? 21.846  1.469   23.554  1.00 10.34 ? 85  GLU A CG  1 
ATOM   689  C  CD  . GLU A 1 97  ? 20.827  1.054   24.614  1.00 14.81 ? 85  GLU A CD  1 
ATOM   690  O  OE1 . GLU A 1 97  ? 20.360  -0.105  24.577  1.00 13.06 ? 85  GLU A OE1 1 
ATOM   691  O  OE2 . GLU A 1 97  ? 20.493  1.880   25.488  1.00 14.99 ? 85  GLU A OE2 1 
ATOM   692  N  N   . TYR A 1 98  ? 23.058  3.429   20.872  1.00 9.08  ? 86  TYR A N   1 
ATOM   693  C  CA  . TYR A 1 98  ? 22.460  4.373   19.930  1.00 8.47  ? 86  TYR A CA  1 
ATOM   694  C  C   . TYR A 1 98  ? 21.315  3.742   19.147  1.00 11.63 ? 86  TYR A C   1 
ATOM   695  O  O   . TYR A 1 98  ? 21.268  2.523   18.950  1.00 7.53  ? 86  TYR A O   1 
ATOM   696  C  CB  . TYR A 1 98  ? 23.501  4.941   18.974  1.00 8.54  ? 86  TYR A CB  1 
ATOM   697  C  CG  . TYR A 1 98  ? 24.104  3.933   18.023  1.00 9.36  ? 86  TYR A CG  1 
ATOM   698  C  CD1 . TYR A 1 98  ? 23.435  3.566   16.851  1.00 9.90  ? 86  TYR A CD1 1 
ATOM   699  C  CD2 . TYR A 1 98  ? 25.346  3.369   18.276  1.00 11.32 ? 86  TYR A CD2 1 
ATOM   700  C  CE1 . TYR A 1 98  ? 23.981  2.654   15.985  1.00 11.56 ? 86  TYR A CE1 1 
ATOM   701  C  CE2 . TYR A 1 98  ? 25.899  2.454   17.412  1.00 11.49 ? 86  TYR A CE2 1 
ATOM   702  C  CZ  . TYR A 1 98  ? 25.210  2.097   16.271  1.00 12.69 ? 86  TYR A CZ  1 
ATOM   703  O  OH  . TYR A 1 98  ? 25.765  1.187   15.415  1.00 14.49 ? 86  TYR A OH  1 
ATOM   704  N  N   . TYR A 1 99  ? 20.398  4.607   18.698  1.00 9.15  ? 87  TYR A N   1 
ATOM   705  C  CA  . TYR A 1 99  ? 19.184  4.210   17.994  1.00 9.71  ? 87  TYR A CA  1 
ATOM   706  C  C   . TYR A 1 99  ? 18.932  5.148   16.828  1.00 10.44 ? 87  TYR A C   1 
ATOM   707  O  O   . TYR A 1 99  ? 18.883  6.369   17.012  1.00 12.51 ? 87  TYR A O   1 
ATOM   708  C  CB  . TYR A 1 99  ? 17.945  4.274   18.884  1.00 10.32 ? 87  TYR A CB  1 
ATOM   709  C  CG  . TYR A 1 99  ? 17.931  3.440   20.128  1.00 14.00 ? 87  TYR A CG  1 
ATOM   710  C  CD1 . TYR A 1 99  ? 18.617  3.852   21.260  1.00 14.09 ? 87  TYR A CD1 1 
ATOM   711  C  CD2 . TYR A 1 99  ? 17.169  2.288   20.194  1.00 18.73 ? 87  TYR A CD2 1 
ATOM   712  C  CE1 . TYR A 1 99  ? 18.575  3.117   22.412  1.00 20.83 ? 87  TYR A CE1 1 
ATOM   713  C  CE2 . TYR A 1 99  ? 17.124  1.544   21.345  1.00 23.77 ? 87  TYR A CE2 1 
ATOM   714  C  CZ  . TYR A 1 99  ? 17.830  1.965   22.448  1.00 17.83 ? 87  TYR A CZ  1 
ATOM   715  O  OH  . TYR A 1 99  ? 17.801  1.236   23.614  1.00 27.10 ? 87  TYR A OH  1 
ATOM   716  N  N   . ILE A 1 100 ? 18.750  4.581   15.647  1.00 9.31  ? 88  ILE A N   1 
ATOM   717  C  CA  . ILE A 1 100 ? 18.173  5.292   14.511  1.00 10.12 ? 88  ILE A CA  1 
ATOM   718  C  C   . ILE A 1 100 ? 16.761  4.736   14.369  1.00 8.32  ? 88  ILE A C   1 
ATOM   719  O  O   . ILE A 1 100 ? 16.556  3.667   13.785  1.00 9.80  ? 88  ILE A O   1 
ATOM   720  C  CB  . ILE A 1 100 ? 19.011  5.112   13.237  1.00 9.01  ? 88  ILE A CB  1 
ATOM   721  C  CG1 . ILE A 1 100 ? 20.428  5.662   13.481  1.00 8.42  ? 88  ILE A CG1 1 
ATOM   722  C  CG2 . ILE A 1 100 ? 18.392  5.862   12.060  1.00 9.40  ? 88  ILE A CG2 1 
ATOM   723  C  CD1 . ILE A 1 100 ? 21.461  5.106   12.539  1.00 8.48  ? 88  ILE A CD1 1 
ATOM   724  N  N   . VAL A 1 101 ? 15.783  5.443   14.933  1.00 7.17  ? 89  VAL A N   1 
ATOM   725  C  CA  . VAL A 1 101 ? 14.436  4.902   15.087  1.00 9.17  ? 89  VAL A CA  1 
ATOM   726  C  C   . VAL A 1 101 ? 13.648  5.174   13.812  1.00 8.90  ? 89  VAL A C   1 
ATOM   727  O  O   . VAL A 1 101 ? 13.403  6.330   13.450  1.00 10.58 ? 89  VAL A O   1 
ATOM   728  C  CB  . VAL A 1 101 ? 13.727  5.495   16.315  1.00 9.49  ? 89  VAL A CB  1 
ATOM   729  C  CG1 . VAL A 1 101 ? 12.308  4.910   16.436  1.00 11.05 ? 89  VAL A CG1 1 
ATOM   730  C  CG2 . VAL A 1 101 ? 14.533  5.195   17.583  1.00 9.19  ? 89  VAL A CG2 1 
ATOM   731  N  N   . GLU A 1 102 ? 13.237  4.103   13.149  1.00 6.98  ? 90  GLU A N   1 
ATOM   732  C  CA  . GLU A 1 102 ? 12.477  4.182   11.909  1.00 9.46  ? 90  GLU A CA  1 
ATOM   733  C  C   . GLU A 1 102 ? 10.983  4.306   12.175  1.00 10.14 ? 90  GLU A C   1 
ATOM   734  O  O   . GLU A 1 102 ? 10.278  5.022   11.455  1.00 9.82  ? 90  GLU A O   1 
ATOM   735  C  CB  . GLU A 1 102 ? 12.754  2.938   11.072  1.00 10.02 ? 90  GLU A CB  1 
ATOM   736  C  CG  . GLU A 1 102 ? 14.187  2.878   10.599  1.00 12.15 ? 90  GLU A CG  1 
ATOM   737  C  CD  . GLU A 1 102 ? 14.432  3.870   9.493   1.00 15.06 ? 90  GLU A CD  1 
ATOM   738  O  OE1 . GLU A 1 102 ? 14.895  4.989   9.795   1.00 15.27 ? 90  GLU A OE1 1 
ATOM   739  O  OE2 . GLU A 1 102 ? 14.140  3.535   8.326   1.00 17.51 ? 90  GLU A OE2 1 
ATOM   740  N  N   . SER A 1 103 ? 10.509  3.600   13.204  1.00 10.12 ? 91  SER A N   1 
ATOM   741  C  CA  . SER A 1 103 ? 9.131   3.653   13.669  1.00 11.38 ? 91  SER A CA  1 
ATOM   742  C  C   . SER A 1 103 ? 9.120   3.450   15.175  1.00 10.87 ? 91  SER A C   1 
ATOM   743  O  O   . SER A 1 103 ? 9.915   2.669   15.705  1.00 9.99  ? 91  SER A O   1 
ATOM   744  C  CB  . SER A 1 103 ? 8.276   2.558   13.025  1.00 13.20 ? 91  SER A CB  1 
ATOM   745  O  OG  . SER A 1 103 ? 7.981   2.823   11.675  1.00 14.84 ? 91  SER A OG  1 
ATOM   746  N  N   . PHE A 1 104 ? 8.220   4.143   15.866  1.00 10.12 ? 92  PHE A N   1 
ATOM   747  C  CA  . PHE A 1 104 ? 7.804   3.717   17.195  1.00 12.71 ? 92  PHE A CA  1 
ATOM   748  C  C   . PHE A 1 104 ? 6.286   3.723   17.229  1.00 14.13 ? 92  PHE A C   1 
ATOM   749  O  O   . PHE A 1 104 ? 5.629   4.330   16.380  1.00 13.34 ? 92  PHE A O   1 
ATOM   750  C  CB  . PHE A 1 104 ? 8.397   4.580   18.327  1.00 10.95 ? 92  PHE A CB  1 
ATOM   751  C  CG  . PHE A 1 104 ? 7.989   6.031   18.295  1.00 13.19 ? 92  PHE A CG  1 
ATOM   752  C  CD1 . PHE A 1 104 ? 6.769   6.436   18.829  1.00 15.26 ? 92  PHE A CD1 1 
ATOM   753  C  CD2 . PHE A 1 104 ? 8.840   6.996   17.769  1.00 11.90 ? 92  PHE A CD2 1 
ATOM   754  C  CE1 . PHE A 1 104 ? 6.407   7.769   18.832  1.00 15.03 ? 92  PHE A CE1 1 
ATOM   755  C  CE2 . PHE A 1 104 ? 8.472   8.334   17.754  1.00 14.70 ? 92  PHE A CE2 1 
ATOM   756  C  CZ  . PHE A 1 104 ? 7.246   8.714   18.290  1.00 13.23 ? 92  PHE A CZ  1 
ATOM   757  N  N   . SER A 1 105 ? 5.723   2.996   18.187  1.00 11.15 ? 93  SER A N   1 
ATOM   758  C  CA  . SER A 1 105 ? 4.276   2.845   18.193  1.00 11.86 ? 93  SER A CA  1 
ATOM   759  C  C   . SER A 1 105 ? 3.650   3.817   19.192  1.00 16.76 ? 93  SER A C   1 
ATOM   760  O  O   . SER A 1 105 ? 3.279   4.935   18.823  1.00 23.98 ? 93  SER A O   1 
ATOM   761  C  CB  . SER A 1 105 ? 3.913   1.389   18.484  1.00 13.66 ? 93  SER A CB  1 
ATOM   762  O  OG  . SER A 1 105 ? 4.519   0.950   19.687  1.00 15.68 ? 93  SER A OG  1 
ATOM   763  N  N   . THR A 1 106 ? 3.578   3.444   20.463  1.00 17.59 ? 94  THR A N   1 
ATOM   764  C  CA  . THR A 1 106 ? 2.769   4.188   21.420  1.00 11.94 ? 94  THR A CA  1 
ATOM   765  C  C   . THR A 1 106 ? 3.574   5.071   22.369  1.00 15.05 ? 94  THR A C   1 
ATOM   766  O  O   . THR A 1 106 ? 2.979   5.741   23.227  1.00 15.85 ? 94  THR A O   1 
ATOM   767  C  CB  . THR A 1 106 ? 1.925   3.207   22.232  1.00 15.55 ? 94  THR A CB  1 
ATOM   768  O  OG1 . THR A 1 106 ? 2.799   2.298   22.902  1.00 18.32 ? 94  THR A OG1 1 
ATOM   769  C  CG2 . THR A 1 106 ? 0.998   2.414   21.325  1.00 17.45 ? 94  THR A CG2 1 
ATOM   770  N  N   . TYR A 1 107 ? 4.899   5.086   22.260  1.00 13.51 ? 95  TYR A N   1 
ATOM   771  C  CA  . TYR A 1 107 ? 5.714   5.860   23.188  1.00 13.74 ? 95  TYR A CA  1 
ATOM   772  C  C   . TYR A 1 107 ? 6.930   6.374   22.439  1.00 15.08 ? 95  TYR A C   1 
ATOM   773  O  O   . TYR A 1 107 ? 7.642   5.584   21.809  1.00 14.00 ? 95  TYR A O   1 
ATOM   774  C  CB  . TYR A 1 107 ? 6.154   5.011   24.389  1.00 13.87 ? 95  TYR A CB  1 
ATOM   775  C  CG  . TYR A 1 107 ? 7.043   5.715   25.399  1.00 14.97 ? 95  TYR A CG  1 
ATOM   776  C  CD1 . TYR A 1 107 ? 6.509   6.612   26.315  1.00 14.93 ? 95  TYR A CD1 1 
ATOM   777  C  CD2 . TYR A 1 107 ? 8.416   5.460   25.457  1.00 15.05 ? 95  TYR A CD2 1 
ATOM   778  C  CE1 . TYR A 1 107 ? 7.301   7.242   27.256  1.00 16.68 ? 95  TYR A CE1 1 
ATOM   779  C  CE2 . TYR A 1 107 ? 9.220   6.097   26.393  1.00 17.25 ? 95  TYR A CE2 1 
ATOM   780  C  CZ  . TYR A 1 107 ? 8.656   6.988   27.287  1.00 18.02 ? 95  TYR A CZ  1 
ATOM   781  O  OH  . TYR A 1 107 ? 9.433   7.629   28.214  1.00 18.83 ? 95  TYR A OH  1 
ATOM   782  N  N   . ASP A 1 108 ? 7.148   7.685   22.502  1.00 13.34 ? 96  ASP A N   1 
ATOM   783  C  CA  . ASP A 1 108 ? 8.311   8.331   21.895  1.00 16.46 ? 96  ASP A CA  1 
ATOM   784  C  C   . ASP A 1 108 ? 9.512   8.198   22.819  1.00 17.05 ? 96  ASP A C   1 
ATOM   785  O  O   . ASP A 1 108 ? 9.547   8.827   23.885  1.00 16.84 ? 96  ASP A O   1 
ATOM   786  C  CB  . ASP A 1 108 ? 8.025   9.812   21.614  1.00 16.24 ? 96  ASP A CB  1 
ATOM   787  C  CG  . ASP A 1 108 ? 9.112   10.484  20.778  1.00 19.47 ? 96  ASP A CG  1 
ATOM   788  O  OD1 . ASP A 1 108 ? 10.265  10.000  20.767  1.00 18.40 ? 96  ASP A OD1 1 
ATOM   789  O  OD2 . ASP A 1 108 ? 8.809   11.508  20.134  1.00 20.10 ? 96  ASP A OD2 1 
ATOM   790  N  N   . PRO A 1 109 ? 10.525  7.418   22.429  1.00 20.50 ? 97  PRO A N   1 
ATOM   791  C  CA  . PRO A 1 109 ? 11.679  7.187   23.319  1.00 23.48 ? 97  PRO A CA  1 
ATOM   792  C  C   . PRO A 1 109 ? 12.533  8.418   23.602  1.00 27.16 ? 97  PRO A C   1 
ATOM   793  O  O   . PRO A 1 109 ? 13.418  8.336   24.468  1.00 26.75 ? 97  PRO A O   1 
ATOM   794  C  CB  . PRO A 1 109 ? 12.484  6.126   22.571  1.00 24.27 ? 97  PRO A CB  1 
ATOM   795  C  CG  . PRO A 1 109 ? 12.101  6.308   21.127  1.00 20.26 ? 97  PRO A CG  1 
ATOM   796  C  CD  . PRO A 1 109 ? 10.635  6.647   21.179  1.00 16.94 ? 97  PRO A CD  1 
ATOM   797  N  N   . SER A 1 110 ? 12.302  9.546   22.937  1.00 25.88 ? 98  SER A N   1 
ATOM   798  C  CA  . SER A 1 110 ? 13.056  10.766  23.199  1.00 25.38 ? 98  SER A CA  1 
ATOM   799  C  C   . SER A 1 110 ? 12.408  11.666  24.248  1.00 27.46 ? 98  SER A C   1 
ATOM   800  O  O   . SER A 1 110 ? 12.910  12.769  24.496  1.00 27.33 ? 98  SER A O   1 
ATOM   801  C  CB  . SER A 1 110 ? 13.234  11.548  21.894  1.00 23.37 ? 98  SER A CB  1 
ATOM   802  O  OG  . SER A 1 110 ? 11.992  12.007  21.379  1.00 24.82 ? 98  SER A OG  1 
ATOM   803  N  N   . THR A 1 111 ? 11.316  11.224  24.871  1.00 18.24 ? 99  THR A N   1 
ATOM   804  C  CA  . THR A 1 111 ? 10.539  12.087  25.749  1.00 20.71 ? 99  THR A CA  1 
ATOM   805  C  C   . THR A 1 111 ? 11.383  12.645  26.894  1.00 21.99 ? 99  THR A C   1 
ATOM   806  O  O   . THR A 1 111 ? 12.134  11.912  27.537  1.00 21.85 ? 99  THR A O   1 
ATOM   807  C  CB  . THR A 1 111 ? 9.360   11.283  26.285  1.00 23.12 ? 99  THR A CB  1 
ATOM   808  O  OG1 . THR A 1 111 ? 8.554   10.885  25.162  1.00 18.94 ? 99  THR A OG1 1 
ATOM   809  C  CG2 . THR A 1 111 ? 8.543   12.109  27.270  1.00 20.99 ? 99  THR A CG2 1 
ATOM   810  N  N   . GLY A 1 112 ? 11.262  13.955  27.132  1.00 28.13 ? 100 GLY A N   1 
ATOM   811  C  CA  . GLY A 1 112 ? 11.962  14.616  28.215  1.00 26.12 ? 100 GLY A CA  1 
ATOM   812  C  C   . GLY A 1 112 ? 13.359  15.098  27.887  1.00 31.05 ? 100 GLY A C   1 
ATOM   813  O  O   . GLY A 1 112 ? 14.000  15.723  28.748  1.00 29.68 ? 100 GLY A O   1 
ATOM   814  N  N   . ALA A 1 113 ? 13.851  14.834  26.678  1.00 24.49 ? 101 ALA A N   1 
ATOM   815  C  CA  . ALA A 1 113 ? 15.202  15.197  26.278  1.00 23.09 ? 101 ALA A CA  1 
ATOM   816  C  C   . ALA A 1 113 ? 15.198  16.457  25.422  1.00 28.60 ? 101 ALA A C   1 
ATOM   817  O  O   . ALA A 1 113 ? 14.248  16.731  24.683  1.00 28.41 ? 101 ALA A O   1 
ATOM   818  C  CB  . ALA A 1 113 ? 15.867  14.063  25.501  1.00 19.90 ? 101 ALA A CB  1 
ATOM   819  N  N   . GLN A 1 114 ? 16.280  17.223  25.528  1.00 25.42 ? 102 GLN A N   1 
ATOM   820  C  CA  . GLN A 1 114 ? 16.447  18.387  24.671  1.00 26.79 ? 102 GLN A CA  1 
ATOM   821  C  C   . GLN A 1 114 ? 16.766  17.935  23.250  1.00 23.30 ? 102 GLN A C   1 
ATOM   822  O  O   . GLN A 1 114 ? 17.681  17.138  23.032  1.00 24.76 ? 102 GLN A O   1 
ATOM   823  C  CB  . GLN A 1 114 ? 17.563  19.284  25.212  1.00 28.89 ? 102 GLN A CB  1 
ATOM   824  C  CG  . GLN A 1 114 ? 17.802  20.561  24.421  1.00 28.07 ? 102 GLN A CG  1 
ATOM   825  C  CD  . GLN A 1 114 ? 19.185  21.141  24.671  1.00 42.76 ? 102 GLN A CD  1 
ATOM   826  O  OE1 . GLN A 1 114 ? 19.992  20.563  25.407  1.00 44.61 ? 102 GLN A OE1 1 
ATOM   827  N  NE2 . GLN A 1 114 ? 19.467  22.290  24.059  1.00 47.47 ? 102 GLN A NE2 1 
ATOM   828  N  N   . GLU A 1 115 ? 16.007  18.436  22.281  1.00 29.28 ? 103 GLU A N   1 
ATOM   829  C  CA  . GLU A 1 115 ? 16.358  18.185  20.892  1.00 24.29 ? 103 GLU A CA  1 
ATOM   830  C  C   . GLU A 1 115 ? 17.638  18.941  20.554  1.00 27.71 ? 103 GLU A C   1 
ATOM   831  O  O   . GLU A 1 115 ? 17.760  20.137  20.839  1.00 29.64 ? 103 GLU A O   1 
ATOM   832  C  CB  . GLU A 1 115 ? 15.215  18.599  19.963  1.00 23.23 ? 103 GLU A CB  1 
ATOM   833  C  CG  . GLU A 1 115 ? 15.534  18.417  18.499  1.00 26.40 ? 103 GLU A CG  1 
ATOM   834  C  CD  . GLU A 1 115 ? 14.406  18.869  17.590  1.00 35.15 ? 103 GLU A CD  1 
ATOM   835  O  OE1 . GLU A 1 115 ? 14.712  19.328  16.463  1.00 33.36 ? 103 GLU A OE1 1 
ATOM   836  O  OE2 . GLU A 1 115 ? 13.222  18.756  17.998  1.00 31.68 ? 103 GLU A OE2 1 
ATOM   837  N  N   . LEU A 1 116 ? 18.602  18.238  19.958  1.00 22.19 ? 104 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 116 ? 19.911  18.804  19.645  1.00 22.52 ? 104 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 116 ? 20.061  19.217  18.189  1.00 27.99 ? 104 LEU A C   1 
ATOM   840  O  O   . LEU A 1 116 ? 21.108  19.761  17.817  1.00 29.85 ? 104 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 116 ? 21.014  17.802  19.997  1.00 21.60 ? 104 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 116 ? 21.106  17.416  21.469  1.00 24.97 ? 104 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 116 ? 22.175  16.356  21.666  1.00 23.89 ? 104 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 116 ? 21.393  18.638  22.321  1.00 25.60 ? 104 LEU A CD2 1 
ATOM   845  N  N   . GLY A 1 117 ? 19.062  18.974  17.361  1.00 22.99 ? 105 GLY A N   1 
ATOM   846  C  CA  . GLY A 1 117 ? 19.141  19.297  15.958  1.00 24.08 ? 105 GLY A CA  1 
ATOM   847  C  C   . GLY A 1 117 ? 18.389  18.268  15.148  1.00 22.40 ? 105 GLY A C   1 
ATOM   848  O  O   . GLY A 1 117 ? 17.662  17.436  15.687  1.00 17.12 ? 105 GLY A O   1 
ATOM   849  N  N   . THR A 1 118 ? 18.559  18.343  13.830  1.00 22.80 ? 106 THR A N   1 
ATOM   850  C  CA  . THR A 1 118 ? 17.922  17.414  12.911  1.00 18.17 ? 106 THR A CA  1 
ATOM   851  C  C   . THR A 1 118 ? 18.945  16.989  11.870  1.00 22.29 ? 106 THR A C   1 
ATOM   852  O  O   . THR A 1 118 ? 19.953  17.668  11.645  1.00 22.20 ? 106 THR A O   1 
ATOM   853  C  CB  . THR A 1 118 ? 16.690  18.016  12.203  1.00 25.54 ? 106 THR A CB  1 
ATOM   854  O  OG1 . THR A 1 118 ? 17.093  19.108  11.367  1.00 27.75 ? 106 THR A OG1 1 
ATOM   855  C  CG2 . THR A 1 118 ? 15.656  18.509  13.208  1.00 22.07 ? 106 THR A CG2 1 
ATOM   856  N  N   . VAL A 1 119 ? 18.683  15.852  11.236  1.00 16.41 ? 107 VAL A N   1 
ATOM   857  C  CA  . VAL A 1 119 ? 19.457  15.400  10.089  1.00 16.59 ? 107 VAL A CA  1 
ATOM   858  C  C   . VAL A 1 119 ? 18.481  14.966  9.005   1.00 19.41 ? 107 VAL A C   1 
ATOM   859  O  O   . VAL A 1 119 ? 17.467  14.316  9.290   1.00 16.72 ? 107 VAL A O   1 
ATOM   860  C  CB  . VAL A 1 119 ? 20.439  14.262  10.460  1.00 15.60 ? 107 VAL A CB  1 
ATOM   861  C  CG1 . VAL A 1 119 ? 19.711  13.062  11.031  1.00 17.96 ? 107 VAL A CG1 1 
ATOM   862  C  CG2 . VAL A 1 119 ? 21.295  13.867  9.260   1.00 19.55 ? 107 VAL A CG2 1 
ATOM   863  N  N   . GLU A 1 120 ? 18.757  15.370  7.771   1.00 19.62 ? 108 GLU A N   1 
ATOM   864  C  CA  . GLU A 1 120 ? 17.958  14.959  6.626   1.00 17.09 ? 108 GLU A CA  1 
ATOM   865  C  C   . GLU A 1 120 ? 18.729  13.883  5.877   1.00 17.80 ? 108 GLU A C   1 
ATOM   866  O  O   . GLU A 1 120 ? 19.848  14.123  5.414   1.00 19.28 ? 108 GLU A O   1 
ATOM   867  C  CB  . GLU A 1 120 ? 17.651  16.148  5.716   1.00 20.84 ? 108 GLU A CB  1 
ATOM   868  C  CG  . GLU A 1 120 ? 17.117  17.367  6.456   1.00 28.50 ? 108 GLU A CG  1 
ATOM   869  C  CD  . GLU A 1 120 ? 15.624  17.297  6.725   1.00 33.40 ? 108 GLU A CD  1 
ATOM   870  O  OE1 . GLU A 1 120 ? 14.931  16.497  6.055   1.00 41.45 ? 108 GLU A OE1 1 
ATOM   871  O  OE2 . GLU A 1 120 ? 15.138  18.044  7.604   1.00 40.56 ? 108 GLU A OE2 1 
ATOM   872  N  N   . THR A 1 121 ? 18.142  12.694  5.774   1.00 15.42 ? 109 THR A N   1 
ATOM   873  C  CA  . THR A 1 121 ? 18.815  11.600  5.098   1.00 16.51 ? 109 THR A CA  1 
ATOM   874  C  C   . THR A 1 121 ? 17.776  10.553  4.733   1.00 15.73 ? 109 THR A C   1 
ATOM   875  O  O   . THR A 1 121 ? 16.740  10.427  5.394   1.00 14.93 ? 109 THR A O   1 
ATOM   876  C  CB  . THR A 1 121 ? 19.941  11.016  5.975   1.00 19.37 ? 109 THR A CB  1 
ATOM   877  O  OG1 . THR A 1 121 ? 20.571  9.904   5.324   1.00 18.77 ? 109 THR A OG1 1 
ATOM   878  C  CG2 . THR A 1 121 ? 19.417  10.584  7.343   1.00 19.62 ? 109 THR A CG2 1 
ATOM   879  N  N   . ASP A 1 122 ? 18.060  9.830   3.655   1.00 16.68 ? 110 ASP A N   1 
ATOM   880  C  CA  . ASP A 1 122 ? 17.232  8.715   3.197   1.00 17.01 ? 110 ASP A CA  1 
ATOM   881  C  C   . ASP A 1 122 ? 15.762  9.120   3.097   1.00 16.22 ? 110 ASP A C   1 
ATOM   882  O  O   . ASP A 1 122 ? 14.854  8.425   3.564   1.00 15.62 ? 110 ASP A O   1 
ATOM   883  C  CB  . ASP A 1 122 ? 17.436  7.507   4.105   1.00 15.06 ? 110 ASP A CB  1 
ATOM   884  C  CG  . ASP A 1 122 ? 18.913  7.157   4.264   1.00 16.00 ? 110 ASP A CG  1 
ATOM   885  O  OD1 . ASP A 1 122 ? 19.550  6.758   3.261   1.00 16.55 ? 110 ASP A OD1 1 
ATOM   886  O  OD2 . ASP A 1 122 ? 19.444  7.306   5.386   1.00 14.97 ? 110 ASP A OD2 1 
ATOM   887  N  N   . ASP A 1 123 ? 15.543  10.285  2.484   1.00 19.19 ? 111 ASP A N   1 
ATOM   888  C  CA  . ASP A 1 123 ? 14.217  10.816  2.169   1.00 23.71 ? 111 ASP A CA  1 
ATOM   889  C  C   . ASP A 1 123 ? 13.375  11.093  3.412   1.00 22.84 ? 111 ASP A C   1 
ATOM   890  O  O   . ASP A 1 123 ? 12.149  11.172  3.331   1.00 21.77 ? 111 ASP A O   1 
ATOM   891  C  CB  . ASP A 1 123 ? 13.475  9.881   1.207   1.00 22.18 ? 111 ASP A CB  1 
ATOM   892  C  CG  . ASP A 1 123 ? 14.081  9.894   -0.189  1.00 32.22 ? 111 ASP A CG  1 
ATOM   893  O  OD1 . ASP A 1 123 ? 13.783  10.834  -0.959  1.00 39.91 ? 111 ASP A OD1 1 
ATOM   894  O  OD2 . ASP A 1 123 ? 14.868  8.974   -0.517  1.00 34.12 ? 111 ASP A OD2 1 
ATOM   895  N  N   . GLY A 1 124 ? 14.003  11.266  4.577   1.00 16.75 ? 112 GLY A N   1 
ATOM   896  C  CA  . GLY A 1 124 ? 13.280  11.623  5.776   1.00 16.06 ? 112 GLY A CA  1 
ATOM   897  C  C   . GLY A 1 124 ? 14.025  12.675  6.576   1.00 14.82 ? 112 GLY A C   1 
ATOM   898  O  O   . GLY A 1 124 ? 15.097  13.141  6.182   1.00 18.18 ? 112 GLY A O   1 
ATOM   899  N  N   . THR A 1 125 ? 13.413  13.059  7.692   1.00 15.55 ? 113 THR A N   1 
ATOM   900  C  CA  . THR A 1 125 ? 13.995  13.976  8.665   1.00 14.03 ? 113 THR A CA  1 
ATOM   901  C  C   . THR A 1 125 ? 14.028  13.275  10.012  1.00 13.35 ? 113 THR A C   1 
ATOM   902  O  O   . THR A 1 125 ? 13.040  12.652  10.406  1.00 14.45 ? 113 THR A O   1 
ATOM   903  C  CB  . THR A 1 125 ? 13.178  15.266  8.771   1.00 17.19 ? 113 THR A CB  1 
ATOM   904  O  OG1 . THR A 1 125 ? 13.160  15.918  7.501   1.00 21.16 ? 113 THR A OG1 1 
ATOM   905  C  CG2 . THR A 1 125 ? 13.781  16.205  9.808   1.00 21.96 ? 113 THR A CG2 1 
ATOM   906  N  N   . TYR A 1 126 ? 15.157  13.370  10.713  1.00 12.10 ? 114 TYR A N   1 
ATOM   907  C  CA  . TYR A 1 126 ? 15.324  12.739  12.014  1.00 12.72 ? 114 TYR A CA  1 
ATOM   908  C  C   . TYR A 1 126 ? 15.670  13.812  13.036  1.00 13.68 ? 114 TYR A C   1 
ATOM   909  O  O   . TYR A 1 126 ? 16.528  14.662  12.776  1.00 15.60 ? 114 TYR A O   1 
ATOM   910  C  CB  . TYR A 1 126 ? 16.441  11.686  11.993  1.00 12.66 ? 114 TYR A CB  1 
ATOM   911  C  CG  . TYR A 1 126 ? 16.189  10.509  11.087  1.00 12.31 ? 114 TYR A CG  1 
ATOM   912  C  CD1 . TYR A 1 126 ? 16.288  10.634  9.696   1.00 11.54 ? 114 TYR A CD1 1 
ATOM   913  C  CD2 . TYR A 1 126 ? 15.867  9.266   11.617  1.00 11.24 ? 114 TYR A CD2 1 
ATOM   914  C  CE1 . TYR A 1 126 ? 16.045  9.562   8.862   1.00 11.04 ? 114 TYR A CE1 1 
ATOM   915  C  CE2 . TYR A 1 126 ? 15.636  8.184   10.791  1.00 10.72 ? 114 TYR A CE2 1 
ATOM   916  C  CZ  . TYR A 1 126 ? 15.727  8.335   9.418   1.00 11.59 ? 114 TYR A CZ  1 
ATOM   917  O  OH  . TYR A 1 126 ? 15.493  7.256   8.602   1.00 12.37 ? 114 TYR A OH  1 
ATOM   918  N  N   . LYS A 1 127 ? 15.015  13.767  14.190  1.00 12.20 ? 115 LYS A N   1 
ATOM   919  C  CA  . LYS A 1 127 ? 15.370  14.630  15.308  1.00 14.88 ? 115 LYS A CA  1 
ATOM   920  C  C   . LYS A 1 127 ? 16.386  13.916  16.188  1.00 13.35 ? 115 LYS A C   1 
ATOM   921  O  O   . LYS A 1 127 ? 16.297  12.699  16.395  1.00 12.80 ? 115 LYS A O   1 
ATOM   922  C  CB  . LYS A 1 127 ? 14.124  15.007  16.116  1.00 16.85 ? 115 LYS A CB  1 
ATOM   923  C  CG  . LYS A 1 127 ? 13.152  15.877  15.314  1.00 20.13 ? 115 LYS A CG  1 
ATOM   924  C  CD  . LYS A 1 127 ? 11.932  16.291  16.118  1.00 22.58 ? 115 LYS A CD  1 
ATOM   925  C  CE  . LYS A 1 127 ? 11.076  17.261  15.288  1.00 29.12 ? 115 LYS A CE  1 
ATOM   926  N  NZ  . LYS A 1 127 ? 9.667   17.385  15.766  1.00 33.13 ? 115 LYS A NZ  1 
ATOM   927  N  N   . ILE A 1 128 ? 17.354  14.680  16.697  1.00 12.25 ? 116 ILE A N   1 
ATOM   928  C  CA  . ILE A 1 128 ? 18.520  14.150  17.401  1.00 13.60 ? 116 ILE A CA  1 
ATOM   929  C  C   . ILE A 1 128 ? 18.387  14.476  18.882  1.00 13.32 ? 116 ILE A C   1 
ATOM   930  O  O   . ILE A 1 128 ? 18.044  15.610  19.246  1.00 13.57 ? 116 ILE A O   1 
ATOM   931  C  CB  . ILE A 1 128 ? 19.818  14.733  16.809  1.00 14.18 ? 116 ILE A CB  1 
ATOM   932  C  CG1 . ILE A 1 128 ? 19.996  14.250  15.370  1.00 14.86 ? 116 ILE A CG1 1 
ATOM   933  C  CG2 . ILE A 1 128 ? 21.039  14.404  17.658  1.00 14.73 ? 116 ILE A CG2 1 
ATOM   934  C  CD1 . ILE A 1 128 ? 21.084  15.006  14.613  1.00 17.60 ? 116 ILE A CD1 1 
ATOM   935  N  N   . TYR A 1 129 ? 18.640  13.475  19.731  1.00 11.84 ? 117 TYR A N   1 
ATOM   936  C  CA  . TYR A 1 129 ? 18.554  13.612  21.178  1.00 12.64 ? 117 TYR A CA  1 
ATOM   937  C  C   . TYR A 1 129 ? 19.684  12.834  21.838  1.00 12.50 ? 117 TYR A C   1 
ATOM   938  O  O   . TYR A 1 129 ? 20.240  11.886  21.270  1.00 12.71 ? 117 TYR A O   1 
ATOM   939  C  CB  . TYR A 1 129 ? 17.233  13.077  21.750  1.00 11.47 ? 117 TYR A CB  1 
ATOM   940  C  CG  . TYR A 1 129 ? 15.987  13.589  21.066  1.00 14.72 ? 117 TYR A CG  1 
ATOM   941  C  CD1 . TYR A 1 129 ? 15.532  13.003  19.897  1.00 14.98 ? 117 TYR A CD1 1 
ATOM   942  C  CD2 . TYR A 1 129 ? 15.251  14.645  21.611  1.00 17.65 ? 117 TYR A CD2 1 
ATOM   943  C  CE1 . TYR A 1 129 ? 14.374  13.455  19.268  1.00 16.09 ? 117 TYR A CE1 1 
ATOM   944  C  CE2 . TYR A 1 129 ? 14.100  15.107  20.980  1.00 19.55 ? 117 TYR A CE2 1 
ATOM   945  C  CZ  . TYR A 1 129 ? 13.670  14.508  19.816  1.00 22.42 ? 117 TYR A CZ  1 
ATOM   946  O  OH  . TYR A 1 129 ? 12.520  14.956  19.186  1.00 18.49 ? 117 TYR A OH  1 
ATOM   947  N  N   . GLN A 1 130 ? 20.009  13.234  23.064  1.00 10.66 ? 118 GLN A N   1 
ATOM   948  C  CA  . GLN A 1 130 ? 20.889  12.443  23.910  1.00 13.27 ? 118 GLN A CA  1 
ATOM   949  C  C   . GLN A 1 130 ? 20.233  12.256  25.265  1.00 16.76 ? 118 GLN A C   1 
ATOM   950  O  O   . GLN A 1 130 ? 19.645  13.196  25.814  1.00 17.63 ? 118 GLN A O   1 
ATOM   951  C  CB  . GLN A 1 130 ? 22.266  13.089  24.110  1.00 15.41 ? 118 GLN A CB  1 
ATOM   952  C  CG  . GLN A 1 130 ? 23.096  12.321  25.123  1.00 21.90 ? 118 GLN A CG  1 
ATOM   953  C  CD  . GLN A 1 130 ? 24.319  13.076  25.580  1.00 27.26 ? 118 GLN A CD  1 
ATOM   954  O  OE1 . GLN A 1 130 ? 24.356  14.310  25.550  1.00 32.91 ? 118 GLN A OE1 1 
ATOM   955  N  NE2 . GLN A 1 130 ? 25.335  12.338  26.001  1.00 29.13 ? 118 GLN A NE2 1 
ATOM   956  N  N   . THR A 1 131 ? 20.319  11.036  25.792  1.00 16.62 ? 119 THR A N   1 
ATOM   957  C  CA  . THR A 1 131 ? 19.882  10.728  27.144  1.00 22.19 ? 119 THR A CA  1 
ATOM   958  C  C   . THR A 1 131 ? 20.997  9.969   27.860  1.00 18.38 ? 119 THR A C   1 
ATOM   959  O  O   . THR A 1 131 ? 22.092  9.757   27.320  1.00 19.86 ? 119 THR A O   1 
ATOM   960  C  CB  . THR A 1 131 ? 18.572  9.924   27.150  1.00 24.22 ? 119 THR A CB  1 
ATOM   961  O  OG1 . THR A 1 131 ? 18.732  8.727   26.384  1.00 25.44 ? 119 THR A OG1 1 
ATOM   962  C  CG2 . THR A 1 131 ? 17.418  10.740  26.563  1.00 28.87 ? 119 THR A CG2 1 
ATOM   963  N  N   . THR A 1 132 ? 20.720  9.589   29.104  1.00 24.82 ? 120 THR A N   1 
ATOM   964  C  CA  . THR A 1 132 ? 21.655  8.854   29.939  1.00 20.79 ? 120 THR A CA  1 
ATOM   965  C  C   . THR A 1 132 ? 20.923  7.701   30.607  1.00 20.43 ? 120 THR A C   1 
ATOM   966  O  O   . THR A 1 132 ? 19.766  7.838   31.008  1.00 25.81 ? 120 THR A O   1 
ATOM   967  C  CB  . THR A 1 132 ? 22.287  9.755   31.020  1.00 28.33 ? 120 THR A CB  1 
ATOM   968  O  OG1 . THR A 1 132 ? 22.901  10.891  30.401  1.00 36.62 ? 120 THR A OG1 1 
ATOM   969  C  CG2 . THR A 1 132 ? 23.338  8.989   31.804  1.00 28.94 ? 120 THR A CG2 1 
ATOM   970  N  N   . ARG A 1 133 ? 21.601  6.566   30.721  1.00 16.53 ? 121 ARG A N   1 
ATOM   971  C  CA  . ARG A 1 133 ? 21.127  5.429   31.492  1.00 16.21 ? 121 ARG A CA  1 
ATOM   972  C  C   . ARG A 1 133 ? 22.092  5.217   32.646  1.00 18.01 ? 121 ARG A C   1 
ATOM   973  O  O   . ARG A 1 133 ? 23.310  5.253   32.448  1.00 20.30 ? 121 ARG A O   1 
ATOM   974  C  CB  . ARG A 1 133 ? 21.042  4.169   30.631  1.00 18.88 ? 121 ARG A CB  1 
ATOM   975  C  CG  . ARG A 1 133 ? 20.120  4.340   29.420  1.00 18.54 ? 121 ARG A CG  1 
ATOM   976  C  CD  . ARG A 1 133 ? 18.698  3.975   29.790  1.00 23.47 ? 121 ARG A CD  1 
ATOM   977  N  NE  . ARG A 1 133 ? 18.520  2.528   29.819  1.00 24.63 ? 121 ARG A NE  1 
ATOM   978  C  CZ  . ARG A 1 133 ? 18.005  1.847   30.837  1.00 25.79 ? 121 ARG A CZ  1 
ATOM   979  N  NH1 . ARG A 1 133 ? 17.609  2.476   31.935  1.00 26.71 ? 121 ARG A NH1 1 
ATOM   980  N  NH2 . ARG A 1 133 ? 17.892  0.527   30.756  1.00 25.34 ? 121 ARG A NH2 1 
ATOM   981  N  N   . GLU A 1 134 ? 21.557  5.001   33.840  1.00 20.91 ? 122 GLU A N   1 
ATOM   982  C  CA  . GLU A 1 134 ? 22.378  4.829   35.032  1.00 25.80 ? 122 GLU A CA  1 
ATOM   983  C  C   . GLU A 1 134 ? 22.126  3.451   35.620  1.00 22.15 ? 122 GLU A C   1 
ATOM   984  O  O   . GLU A 1 134 ? 20.972  3.063   35.828  1.00 23.68 ? 122 GLU A O   1 
ATOM   985  C  CB  . GLU A 1 134 ? 22.086  5.919   36.073  1.00 33.76 ? 122 GLU A CB  1 
ATOM   986  C  CG  . GLU A 1 134 ? 22.912  7.189   35.886  1.00 40.16 ? 122 GLU A CG  1 
ATOM   987  C  CD  . GLU A 1 134 ? 22.542  8.276   36.882  1.00 54.26 ? 122 GLU A CD  1 
ATOM   988  O  OE1 . GLU A 1 134 ? 23.173  9.356   36.852  1.00 58.46 ? 122 GLU A OE1 1 
ATOM   989  O  OE2 . GLU A 1 134 ? 21.619  8.047   37.695  1.00 55.84 ? 122 GLU A OE2 1 
ATOM   990  N  N   . ASN A 1 135 ? 23.211  2.713   35.866  1.00 19.79 ? 123 ASN A N   1 
ATOM   991  C  CA  . ASN A 1 135 ? 23.158  1.382   36.473  1.00 25.37 ? 123 ASN A CA  1 
ATOM   992  C  C   . ASN A 1 135 ? 22.229  0.457   35.689  1.00 20.89 ? 123 ASN A C   1 
ATOM   993  O  O   . ASN A 1 135 ? 21.349  -0.203  36.248  1.00 20.78 ? 123 ASN A O   1 
ATOM   994  C  CB  . ASN A 1 135 ? 22.736  1.470   37.941  1.00 25.79 ? 123 ASN A CB  1 
ATOM   995  C  CG  . ASN A 1 135 ? 23.651  2.366   38.755  1.00 33.49 ? 123 ASN A CG  1 
ATOM   996  O  OD1 . ASN A 1 135 ? 24.876  2.219   38.721  1.00 31.68 ? 123 ASN A OD1 1 
ATOM   997  N  ND2 . ASN A 1 135 ? 23.059  3.306   39.488  1.00 33.88 ? 123 ASN A ND2 1 
ATOM   998  N  N   . ALA A 1 136 ? 22.438  0.413   34.380  1.00 20.88 ? 124 ALA A N   1 
ATOM   999  C  CA  . ALA A 1 136 ? 21.541  -0.237  33.438  1.00 18.60 ? 124 ALA A CA  1 
ATOM   1000 C  C   . ALA A 1 136 ? 22.252  -1.375  32.718  1.00 14.92 ? 124 ALA A C   1 
ATOM   1001 O  O   . ALA A 1 136 ? 23.484  -1.380  32.614  1.00 16.52 ? 124 ALA A O   1 
ATOM   1002 C  CB  . ALA A 1 136 ? 21.027  0.780   32.411  1.00 17.68 ? 124 ALA A CB  1 
ATOM   1003 N  N   . PRO A 1 137 ? 21.509  -2.355  32.196  1.00 14.03 ? 125 PRO A N   1 
ATOM   1004 C  CA  . PRO A 1 137 ? 22.151  -3.411  31.410  1.00 14.86 ? 125 PRO A CA  1 
ATOM   1005 C  C   . PRO A 1 137 ? 22.860  -2.827  30.202  1.00 14.23 ? 125 PRO A C   1 
ATOM   1006 O  O   . PRO A 1 137 ? 22.431  -1.826  29.622  1.00 14.16 ? 125 PRO A O   1 
ATOM   1007 C  CB  . PRO A 1 137 ? 20.983  -4.311  30.990  1.00 17.46 ? 125 PRO A CB  1 
ATOM   1008 C  CG  . PRO A 1 137 ? 19.907  -4.021  31.962  1.00 20.53 ? 125 PRO A CG  1 
ATOM   1009 C  CD  . PRO A 1 137 ? 20.061  -2.574  32.326  1.00 20.10 ? 125 PRO A CD  1 
ATOM   1010 N  N   . SER A 1 138 ? 23.964  -3.466  29.832  1.00 13.04 ? 126 SER A N   1 
ATOM   1011 C  CA  . SER A 1 138 ? 24.788  -3.009  28.722  1.00 13.31 ? 126 SER A CA  1 
ATOM   1012 C  C   . SER A 1 138 ? 25.566  -4.200  28.185  1.00 13.58 ? 126 SER A C   1 
ATOM   1013 O  O   . SER A 1 138 ? 25.590  -5.277  28.788  1.00 14.23 ? 126 SER A O   1 
ATOM   1014 C  CB  . SER A 1 138 ? 25.741  -1.885  29.168  1.00 16.03 ? 126 SER A CB  1 
ATOM   1015 O  OG  . SER A 1 138 ? 26.953  -2.442  29.638  1.00 13.77 ? 126 SER A OG  1 
ATOM   1016 N  N   . ILE A 1 139 ? 26.235  -3.981  27.050  1.00 12.48 ? 127 ILE A N   1 
ATOM   1017 C  CA  . ILE A 1 139 ? 27.120  -5.002  26.502  1.00 14.22 ? 127 ILE A CA  1 
ATOM   1018 C  C   . ILE A 1 139 ? 28.337  -5.228  27.382  1.00 16.65 ? 127 ILE A C   1 
ATOM   1019 O  O   . ILE A 1 139 ? 29.105  -6.167  27.127  1.00 15.76 ? 127 ILE A O   1 
ATOM   1020 C  CB  . ILE A 1 139 ? 27.582  -4.655  25.072  1.00 13.20 ? 127 ILE A CB  1 
ATOM   1021 C  CG1 . ILE A 1 139 ? 28.324  -3.311  25.043  1.00 14.07 ? 127 ILE A CG1 1 
ATOM   1022 C  CG2 . ILE A 1 139 ? 26.374  -4.679  24.108  1.00 14.08 ? 127 ILE A CG2 1 
ATOM   1023 C  CD1 . ILE A 1 139 ? 29.153  -3.071  23.787  1.00 16.02 ? 127 ILE A CD1 1 
ATOM   1024 N  N   . GLU A 1 140 ? 28.534  -4.384  28.398  1.00 14.59 ? 128 GLU A N   1 
ATOM   1025 C  CA  . GLU A 1 140 ? 29.624  -4.538  29.358  1.00 17.66 ? 128 GLU A CA  1 
ATOM   1026 C  C   . GLU A 1 140 ? 29.138  -4.911  30.754  1.00 21.54 ? 128 GLU A C   1 
ATOM   1027 O  O   . GLU A 1 140 ? 29.932  -4.862  31.706  1.00 20.42 ? 128 GLU A O   1 
ATOM   1028 C  CB  . GLU A 1 140 ? 30.460  -3.252  29.435  1.00 15.96 ? 128 GLU A CB  1 
ATOM   1029 C  CG  . GLU A 1 140 ? 31.212  -2.869  28.145  1.00 19.88 ? 128 GLU A CG  1 
ATOM   1030 C  CD  . GLU A 1 140 ? 32.283  -3.869  27.723  1.00 26.24 ? 128 GLU A CD  1 
ATOM   1031 O  OE1 . GLU A 1 140 ? 32.334  -4.999  28.266  1.00 28.52 ? 128 GLU A OE1 1 
ATOM   1032 O  OE2 . GLU A 1 140 ? 33.088  -3.517  26.829  1.00 28.95 ? 128 GLU A OE2 1 
ATOM   1033 N  N   . GLY A 1 141 ? 27.875  -5.307  30.902  1.00 16.01 ? 129 GLY A N   1 
ATOM   1034 C  CA  . GLY A 1 141 ? 27.296  -5.496  32.221  1.00 15.82 ? 129 GLY A CA  1 
ATOM   1035 C  C   . GLY A 1 141 ? 26.602  -4.244  32.722  1.00 19.36 ? 129 GLY A C   1 
ATOM   1036 O  O   . GLY A 1 141 ? 26.415  -3.254  32.000  1.00 16.80 ? 129 GLY A O   1 
ATOM   1037 N  N   . THR A 1 142 ? 26.204  -4.292  33.997  1.00 15.85 ? 130 THR A N   1 
ATOM   1038 C  CA  . THR A 1 142 ? 25.555  -3.133  34.603  1.00 16.81 ? 130 THR A CA  1 
ATOM   1039 C  C   . THR A 1 142 ? 26.459  -1.914  34.490  1.00 21.16 ? 130 THR A C   1 
ATOM   1040 O  O   . THR A 1 142 ? 27.617  -1.958  34.909  1.00 19.65 ? 130 THR A O   1 
ATOM   1041 C  CB  . THR A 1 142 ? 25.235  -3.408  36.066  1.00 18.24 ? 130 THR A CB  1 
ATOM   1042 O  OG1 . THR A 1 142 ? 24.387  -4.561  36.147  1.00 20.46 ? 130 THR A OG1 1 
ATOM   1043 C  CG2 . THR A 1 142 ? 24.515  -2.212  36.677  1.00 20.31 ? 130 THR A CG2 1 
ATOM   1044 N  N   . ALA A 1 143 ? 25.938  -0.826  33.923  1.00 16.98 ? 131 ALA A N   1 
ATOM   1045 C  CA  . ALA A 1 143 ? 26.799  0.299   33.577  1.00 18.39 ? 131 ALA A CA  1 
ATOM   1046 C  C   . ALA A 1 143 ? 25.980  1.577   33.462  1.00 19.34 ? 131 ALA A C   1 
ATOM   1047 O  O   . ALA A 1 143 ? 24.747  1.553   33.384  1.00 19.84 ? 131 ALA A O   1 
ATOM   1048 C  CB  . ALA A 1 143 ? 27.559  0.032   32.276  1.00 18.45 ? 131 ALA A CB  1 
ATOM   1049 N  N   . THR A 1 144 ? 26.704  2.698   33.444  1.00 17.58 ? 132 THR A N   1 
ATOM   1050 C  CA  . THR A 1 144 ? 26.160  4.012   33.126  1.00 17.17 ? 132 THR A CA  1 
ATOM   1051 C  C   . THR A 1 144 ? 26.708  4.451   31.772  1.00 18.70 ? 132 THR A C   1 
ATOM   1052 O  O   . THR A 1 144 ? 27.900  4.288   31.487  1.00 20.62 ? 132 THR A O   1 
ATOM   1053 C  CB  . THR A 1 144 ? 26.518  5.040   34.210  1.00 24.11 ? 132 THR A CB  1 
ATOM   1054 O  OG1 . THR A 1 144 ? 25.842  4.699   35.427  1.00 24.25 ? 132 THR A OG1 1 
ATOM   1055 C  CG2 . THR A 1 144 ? 26.090  6.442   33.793  1.00 26.88 ? 132 THR A CG2 1 
ATOM   1056 N  N   . PHE A 1 145 ? 25.839  4.986   30.925  1.00 18.85 ? 133 PHE A N   1 
ATOM   1057 C  CA  . PHE A 1 145 ? 26.273  5.283   29.572  1.00 17.17 ? 133 PHE A CA  1 
ATOM   1058 C  C   . PHE A 1 145 ? 25.294  6.260   28.953  1.00 13.54 ? 133 PHE A C   1 
ATOM   1059 O  O   . PHE A 1 145 ? 24.168  6.428   29.426  1.00 16.79 ? 133 PHE A O   1 
ATOM   1060 C  CB  . PHE A 1 145 ? 26.375  4.009   28.726  1.00 16.60 ? 133 PHE A CB  1 
ATOM   1061 C  CG  . PHE A 1 145 ? 25.135  3.153   28.768  1.00 12.50 ? 133 PHE A CG  1 
ATOM   1062 C  CD1 . PHE A 1 145 ? 24.967  2.203   29.762  1.00 14.79 ? 133 PHE A CD1 1 
ATOM   1063 C  CD2 . PHE A 1 145 ? 24.121  3.308   27.820  1.00 13.08 ? 133 PHE A CD2 1 
ATOM   1064 C  CE1 . PHE A 1 145 ? 23.825  1.415   29.812  1.00 15.88 ? 133 PHE A CE1 1 
ATOM   1065 C  CE2 . PHE A 1 145 ? 22.979  2.532   27.873  1.00 13.21 ? 133 PHE A CE2 1 
ATOM   1066 C  CZ  . PHE A 1 145 ? 22.829  1.579   28.858  1.00 13.88 ? 133 PHE A CZ  1 
ATOM   1067 N  N   . ASN A 1 146 ? 25.744  6.909   27.895  1.00 14.35 ? 134 ASN A N   1 
ATOM   1068 C  CA  . ASN A 1 146 ? 24.865  7.801   27.170  1.00 16.33 ? 134 ASN A CA  1 
ATOM   1069 C  C   . ASN A 1 146 ? 24.139  7.034   26.079  1.00 13.51 ? 134 ASN A C   1 
ATOM   1070 O  O   . ASN A 1 146 ? 24.628  6.017   25.585  1.00 11.65 ? 134 ASN A O   1 
ATOM   1071 C  CB  . ASN A 1 146 ? 25.652  8.961   26.586  1.00 16.99 ? 134 ASN A CB  1 
ATOM   1072 C  CG  . ASN A 1 146 ? 26.091  9.945   27.671  1.00 21.78 ? 134 ASN A CG  1 
ATOM   1073 O  OD1 . ASN A 1 146 ? 25.334  10.228  28.609  1.00 27.74 ? 134 ASN A OD1 1 
ATOM   1074 N  ND2 . ASN A 1 146 ? 27.304  10.446  27.558  1.00 22.88 ? 134 ASN A ND2 1 
ATOM   1075 N  N   . GLN A 1 147 ? 22.944  7.511   25.744  1.00 12.96 ? 135 GLN A N   1 
ATOM   1076 C  CA  . GLN A 1 147 ? 22.171  6.991   24.625  1.00 12.04 ? 135 GLN A CA  1 
ATOM   1077 C  C   . GLN A 1 147 ? 22.020  8.104   23.609  1.00 11.19 ? 135 GLN A C   1 
ATOM   1078 O  O   . GLN A 1 147 ? 21.655  9.226   23.979  1.00 13.76 ? 135 GLN A O   1 
ATOM   1079 C  CB  . GLN A 1 147 ? 20.769  6.550   25.039  1.00 17.61 ? 135 GLN A CB  1 
ATOM   1080 C  CG  . GLN A 1 147 ? 20.627  5.346   25.905  1.00 21.48 ? 135 GLN A CG  1 
ATOM   1081 C  CD  . GLN A 1 147 ? 19.155  5.111   26.197  1.00 20.58 ? 135 GLN A CD  1 
ATOM   1082 O  OE1 . GLN A 1 147 ? 18.420  6.057   26.489  1.00 23.43 ? 135 GLN A OE1 1 
ATOM   1083 N  NE2 . GLN A 1 147 ? 18.713  3.871   26.095  1.00 16.34 ? 135 GLN A NE2 1 
ATOM   1084 N  N   . TYR A 1 148 ? 22.267  7.802   22.340  1.00 9.91  ? 136 TYR A N   1 
ATOM   1085 C  CA  . TYR A 1 148 ? 22.047  8.769   21.274  1.00 10.94 ? 136 TYR A CA  1 
ATOM   1086 C  C   . TYR A 1 148 ? 20.858  8.322   20.441  1.00 14.16 ? 136 TYR A C   1 
ATOM   1087 O  O   . TYR A 1 148 ? 20.684  7.123   20.198  1.00 12.04 ? 136 TYR A O   1 
ATOM   1088 C  CB  . TYR A 1 148 ? 23.267  8.913   20.376  1.00 10.64 ? 136 TYR A CB  1 
ATOM   1089 C  CG  . TYR A 1 148 ? 24.531  9.307   21.105  1.00 13.64 ? 136 TYR A CG  1 
ATOM   1090 C  CD1 . TYR A 1 148 ? 24.482  9.897   22.365  1.00 13.67 ? 136 TYR A CD1 1 
ATOM   1091 C  CD2 . TYR A 1 148 ? 25.772  9.084   20.526  1.00 13.73 ? 136 TYR A CD2 1 
ATOM   1092 C  CE1 . TYR A 1 148 ? 25.654  10.242  23.037  1.00 14.64 ? 136 TYR A CE1 1 
ATOM   1093 C  CE2 . TYR A 1 148 ? 26.942  9.424   21.178  1.00 16.19 ? 136 TYR A CE2 1 
ATOM   1094 C  CZ  . TYR A 1 148 ? 26.881  9.997   22.427  1.00 16.80 ? 136 TYR A CZ  1 
ATOM   1095 O  OH  . TYR A 1 148 ? 28.069  10.320  23.051  1.00 18.79 ? 136 TYR A OH  1 
ATOM   1096 N  N   . TRP A 1 149 ? 20.035  9.289   20.024  1.00 11.93 ? 137 TRP A N   1 
ATOM   1097 C  CA  . TRP A 1 149 ? 18.809  9.008   19.290  1.00 10.38 ? 137 TRP A CA  1 
ATOM   1098 C  C   . TRP A 1 149 ? 18.741  9.828   18.012  1.00 12.45 ? 137 TRP A C   1 
ATOM   1099 O  O   . TRP A 1 149 ? 19.066  11.020  18.001  1.00 11.40 ? 137 TRP A O   1 
ATOM   1100 C  CB  . TRP A 1 149 ? 17.562  9.318   20.120  1.00 12.23 ? 137 TRP A CB  1 
ATOM   1101 C  CG  . TRP A 1 149 ? 17.457  8.584   21.411  1.00 11.10 ? 137 TRP A CG  1 
ATOM   1102 C  CD1 . TRP A 1 149 ? 17.962  8.977   22.618  1.00 15.63 ? 137 TRP A CD1 1 
ATOM   1103 C  CD2 . TRP A 1 149 ? 16.782  7.342   21.642  1.00 10.37 ? 137 TRP A CD2 1 
ATOM   1104 N  NE1 . TRP A 1 149 ? 17.644  8.057   23.585  1.00 14.07 ? 137 TRP A NE1 1 
ATOM   1105 C  CE2 . TRP A 1 149 ? 16.925  7.040   23.017  1.00 15.15 ? 137 TRP A CE2 1 
ATOM   1106 C  CE3 . TRP A 1 149 ? 16.060  6.459   20.824  1.00 12.99 ? 137 TRP A CE3 1 
ATOM   1107 C  CZ2 . TRP A 1 149 ? 16.387  5.893   23.588  1.00 15.57 ? 137 TRP A CZ2 1 
ATOM   1108 C  CZ3 . TRP A 1 149 ? 15.537  5.315   21.391  1.00 14.82 ? 137 TRP A CZ3 1 
ATOM   1109 C  CH2 . TRP A 1 149 ? 15.708  5.038   22.764  1.00 15.43 ? 137 TRP A CH2 1 
ATOM   1110 N  N   . SER A 1 150 ? 18.329  9.170   16.934  1.00 10.59 ? 138 SER A N   1 
ATOM   1111 C  CA  . SER A 1 150 ? 17.847  9.810   15.713  1.00 12.19 ? 138 SER A CA  1 
ATOM   1112 C  C   . SER A 1 150 ? 16.452  9.268   15.482  1.00 11.31 ? 138 SER A C   1 
ATOM   1113 O  O   . SER A 1 150 ? 16.301  8.067   15.242  1.00 12.53 ? 138 SER A O   1 
ATOM   1114 C  CB  . SER A 1 150 ? 18.718  9.465   14.501  1.00 14.42 ? 138 SER A CB  1 
ATOM   1115 O  OG  . SER A 1 150 ? 19.725  10.417  14.272  1.00 20.63 ? 138 SER A OG  1 
ATOM   1116 N  N   . VAL A 1 151 ? 15.431  10.132  15.542  1.00 9.68  ? 139 VAL A N   1 
ATOM   1117 C  CA  . VAL A 1 151 ? 14.048  9.667   15.537  1.00 10.86 ? 139 VAL A CA  1 
ATOM   1118 C  C   . VAL A 1 151 ? 13.360  10.220  14.297  1.00 11.81 ? 139 VAL A C   1 
ATOM   1119 O  O   . VAL A 1 151 ? 13.171  11.437  14.177  1.00 13.27 ? 139 VAL A O   1 
ATOM   1120 C  CB  . VAL A 1 151 ? 13.304  10.079  16.815  1.00 12.82 ? 139 VAL A CB  1 
ATOM   1121 C  CG1 . VAL A 1 151 ? 11.932  9.448   16.846  1.00 13.06 ? 139 VAL A CG1 1 
ATOM   1122 C  CG2 . VAL A 1 151 ? 14.153  9.693   18.079  1.00 11.88 ? 139 VAL A CG2 1 
ATOM   1123 N  N   . ARG A 1 152 ? 13.005  9.329   13.371  1.00 9.30  ? 140 ARG A N   1 
ATOM   1124 C  CA  . ARG A 1 152 ? 12.406  9.753   12.109  1.00 10.69 ? 140 ARG A CA  1 
ATOM   1125 C  C   . ARG A 1 152 ? 11.068  10.423  12.381  1.00 12.65 ? 140 ARG A C   1 
ATOM   1126 O  O   . ARG A 1 152 ? 10.274  9.937   13.189  1.00 12.44 ? 140 ARG A O   1 
ATOM   1127 C  CB  . ARG A 1 152 ? 12.221  8.553   11.182  1.00 10.65 ? 140 ARG A CB  1 
ATOM   1128 C  CG  . ARG A 1 152 ? 12.029  8.888   9.695   1.00 12.77 ? 140 ARG A CG  1 
ATOM   1129 C  CD  . ARG A 1 152 ? 11.974  7.629   8.826   1.00 11.64 ? 140 ARG A CD  1 
ATOM   1130 N  NE  . ARG A 1 152 ? 11.536  7.930   7.453   1.00 14.68 ? 140 ARG A NE  1 
ATOM   1131 C  CZ  . ARG A 1 152 ? 12.361  8.160   6.438   1.00 13.19 ? 140 ARG A CZ  1 
ATOM   1132 N  NH1 . ARG A 1 152 ? 13.677  8.119   6.621   1.00 13.74 ? 140 ARG A NH1 1 
ATOM   1133 N  NH2 . ARG A 1 152 ? 11.871  8.407   5.225   1.00 16.73 ? 140 ARG A NH2 1 
ATOM   1134 N  N   . THR A 1 153 ? 10.822  11.554  11.704  1.00 11.86 ? 141 THR A N   1 
ATOM   1135 C  CA  . THR A 1 153 ? 9.572   12.280  11.917  1.00 14.21 ? 141 THR A CA  1 
ATOM   1136 C  C   . THR A 1 153 ? 8.387   11.625  11.211  1.00 16.02 ? 141 THR A C   1 
ATOM   1137 O  O   . THR A 1 153 ? 7.244   11.807  11.644  1.00 17.16 ? 141 THR A O   1 
ATOM   1138 C  CB  . THR A 1 153 ? 9.708   13.736  11.454  1.00 14.48 ? 141 THR A CB  1 
ATOM   1139 O  OG1 . THR A 1 153 ? 9.945   13.774  10.045  1.00 17.49 ? 141 THR A OG1 1 
ATOM   1140 C  CG2 . THR A 1 153 ? 10.853  14.431  12.191  1.00 16.97 ? 141 THR A CG2 1 
ATOM   1141 N  N   . ASP A 1 154 ? 8.628   10.870  10.138  1.00 13.73 ? 142 ASP A N   1 
ATOM   1142 C  CA  . ASP A 1 154 ? 7.585   10.163  9.385   1.00 20.24 ? 142 ASP A CA  1 
ATOM   1143 C  C   . ASP A 1 154 ? 7.891   8.668   9.485   1.00 18.43 ? 142 ASP A C   1 
ATOM   1144 O  O   . ASP A 1 154 ? 8.786   8.164   8.802   1.00 19.27 ? 142 ASP A O   1 
ATOM   1145 C  CB  . ASP A 1 154 ? 7.550   10.647  7.932   1.00 18.13 ? 142 ASP A CB  1 
ATOM   1146 C  CG  . ASP A 1 154 ? 6.478   9.964   7.105   1.00 25.87 ? 142 ASP A CG  1 
ATOM   1147 O  OD1 . ASP A 1 154 ? 5.560   9.370   7.701   1.00 29.38 ? 142 ASP A OD1 1 
ATOM   1148 O  OD2 . ASP A 1 154 ? 6.554   10.039  5.860   1.00 31.02 ? 142 ASP A OD2 1 
ATOM   1149 N  N   . HIS A 1 155 ? 7.165   7.958   10.346  1.00 14.89 ? 143 HIS A N   1 
ATOM   1150 C  CA  . HIS A 1 155 ? 7.512   6.573   10.641  1.00 14.45 ? 143 HIS A CA  1 
ATOM   1151 C  C   . HIS A 1 155 ? 7.342   5.696   9.409   1.00 15.78 ? 143 HIS A C   1 
ATOM   1152 O  O   . HIS A 1 155 ? 6.429   5.898   8.606   1.00 15.11 ? 143 HIS A O   1 
ATOM   1153 C  CB  . HIS A 1 155 ? 6.649   6.053   11.789  1.00 15.10 ? 143 HIS A CB  1 
ATOM   1154 C  CG  . HIS A 1 155 ? 6.861   6.794   13.073  1.00 17.00 ? 143 HIS A CG  1 
ATOM   1155 N  ND1 . HIS A 1 155 ? 6.139   6.526   14.214  1.00 14.90 ? 143 HIS A ND1 1 
ATOM   1156 C  CD2 . HIS A 1 155 ? 7.709   7.801   13.393  1.00 16.26 ? 143 HIS A CD2 1 
ATOM   1157 C  CE1 . HIS A 1 155 ? 6.534   7.328   15.187  1.00 14.86 ? 143 HIS A CE1 1 
ATOM   1158 N  NE2 . HIS A 1 155 ? 7.482   8.118   14.713  1.00 19.13 ? 143 HIS A NE2 1 
ATOM   1159 N  N   . ARG A 1 156 ? 8.232   4.720   9.254   1.00 10.63 ? 144 ARG A N   1 
ATOM   1160 C  CA  . ARG A 1 156 ? 8.168   3.799   8.128   1.00 9.99  ? 144 ARG A CA  1 
ATOM   1161 C  C   . ARG A 1 156 ? 8.720   2.442   8.536   1.00 10.78 ? 144 ARG A C   1 
ATOM   1162 O  O   . ARG A 1 156 ? 9.404   2.299   9.558   1.00 11.40 ? 144 ARG A O   1 
ATOM   1163 C  CB  . ARG A 1 156 ? 8.945   4.317   6.919   1.00 10.91 ? 144 ARG A CB  1 
ATOM   1164 C  CG  . ARG A 1 156 ? 10.439  4.365   7.193   1.00 11.77 ? 144 ARG A CG  1 
ATOM   1165 C  CD  . ARG A 1 156 ? 11.240  4.727   5.954   1.00 12.31 ? 144 ARG A CD  1 
ATOM   1166 N  NE  . ARG A 1 156 ? 12.663  4.729   6.296   1.00 11.29 ? 144 ARG A NE  1 
ATOM   1167 C  CZ  . ARG A 1 156 ? 13.646  4.952   5.437   1.00 13.80 ? 144 ARG A CZ  1 
ATOM   1168 N  NH1 . ARG A 1 156 ? 13.385  5.205   4.157   1.00 16.20 ? 144 ARG A NH1 1 
ATOM   1169 N  NH2 . ARG A 1 156 ? 14.897  4.924   5.870   1.00 13.76 ? 144 ARG A NH2 1 
ATOM   1170 N  N   . VAL A 1 157 ? 8.382   1.437   7.727   1.00 11.43 ? 145 VAL A N   1 
ATOM   1171 C  CA  . VAL A 1 157 ? 8.873   0.071   7.882   1.00 8.06  ? 145 VAL A CA  1 
ATOM   1172 C  C   . VAL A 1 157 ? 9.542   -0.296  6.563   1.00 12.37 ? 145 VAL A C   1 
ATOM   1173 O  O   . VAL A 1 157 ? 8.868   -0.634  5.580   1.00 13.55 ? 145 VAL A O   1 
ATOM   1174 C  CB  . VAL A 1 157 ? 7.757   -0.918  8.241   1.00 10.84 ? 145 VAL A CB  1 
ATOM   1175 C  CG1 . VAL A 1 157 ? 8.336   -2.331  8.403   1.00 12.10 ? 145 VAL A CG1 1 
ATOM   1176 C  CG2 . VAL A 1 157 ? 7.031   -0.462  9.518   1.00 15.10 ? 145 VAL A CG2 1 
ATOM   1177 N  N   . GLY A 1 158 ? 10.866  -0.206  6.522   1.00 12.18 ? 146 GLY A N   1 
ATOM   1178 C  CA  . GLY A 1 158 ? 11.591  -0.581  5.330   1.00 12.22 ? 146 GLY A CA  1 
ATOM   1179 C  C   . GLY A 1 158 ? 12.292  0.611   4.727   1.00 15.63 ? 146 GLY A C   1 
ATOM   1180 O  O   . GLY A 1 158 ? 11.971  1.751   5.059   1.00 22.15 ? 146 GLY A O   1 
ATOM   1181 N  N   . GLY A 1 159 ? 13.252  0.363   3.853   1.00 16.82 ? 147 GLY A N   1 
ATOM   1182 C  CA  . GLY A 1 159 ? 13.982  1.450   3.243   1.00 15.97 ? 147 GLY A CA  1 
ATOM   1183 C  C   . GLY A 1 159 ? 15.471  1.333   3.477   1.00 14.99 ? 147 GLY A C   1 
ATOM   1184 O  O   . GLY A 1 159 ? 15.984  0.268   3.835   1.00 16.10 ? 147 GLY A O   1 
ATOM   1185 N  N   . THR A 1 160 ? 16.166  2.444   3.288   1.00 12.93 ? 148 THR A N   1 
ATOM   1186 C  CA  . THR A 1 160 ? 17.616  2.507   3.364   1.00 13.68 ? 148 THR A CA  1 
ATOM   1187 C  C   . THR A 1 160 ? 17.998  3.411   4.524   1.00 10.80 ? 148 THR A C   1 
ATOM   1188 O  O   . THR A 1 160 ? 17.389  4.465   4.726   1.00 12.58 ? 148 THR A O   1 
ATOM   1189 C  CB  . THR A 1 160 ? 18.196  3.049   2.041   1.00 16.65 ? 148 THR A CB  1 
ATOM   1190 O  OG1 . THR A 1 160 ? 17.801  2.199   0.956   1.00 20.09 ? 148 THR A OG1 1 
ATOM   1191 C  CG2 . THR A 1 160 ? 19.702  3.115   2.100   1.00 14.87 ? 148 THR A CG2 1 
ATOM   1192 N  N   . VAL A 1 161 ? 18.997  3.003   5.303   1.00 10.13 ? 149 VAL A N   1 
ATOM   1193 C  CA  . VAL A 1 161 ? 19.523  3.845   6.378   1.00 10.30 ? 149 VAL A CA  1 
ATOM   1194 C  C   . VAL A 1 161 ? 21.008  4.044   6.110   1.00 11.53 ? 149 VAL A C   1 
ATOM   1195 O  O   . VAL A 1 161 ? 21.793  3.092   6.199   1.00 12.64 ? 149 VAL A O   1 
ATOM   1196 C  CB  . VAL A 1 161 ? 19.289  3.240   7.767   1.00 9.69  ? 149 VAL A CB  1 
ATOM   1197 C  CG1 . VAL A 1 161 ? 19.953  4.111   8.840   1.00 10.09 ? 149 VAL A CG1 1 
ATOM   1198 C  CG2 . VAL A 1 161 ? 17.781  3.121   8.040   1.00 11.25 ? 149 VAL A CG2 1 
ATOM   1199 N  N   . THR A 1 162 ? 21.394  5.275   5.775   1.00 10.81 ? 150 THR A N   1 
ATOM   1200 C  CA  . THR A 1 162 ? 22.804  5.627   5.586   1.00 11.67 ? 150 THR A CA  1 
ATOM   1201 C  C   . THR A 1 162 ? 23.355  5.986   6.960   1.00 12.24 ? 150 THR A C   1 
ATOM   1202 O  O   . THR A 1 162 ? 23.296  7.142   7.398   1.00 11.38 ? 150 THR A O   1 
ATOM   1203 C  CB  . THR A 1 162 ? 22.945  6.769   4.586   1.00 15.74 ? 150 THR A CB  1 
ATOM   1204 O  OG1 . THR A 1 162 ? 22.205  6.443   3.406   1.00 15.75 ? 150 THR A OG1 1 
ATOM   1205 C  CG2 . THR A 1 162 ? 24.428  6.976   4.190   1.00 15.41 ? 150 THR A CG2 1 
ATOM   1206 N  N   . THR A 1 163 ? 23.868  4.969   7.671   1.00 10.96 ? 151 THR A N   1 
ATOM   1207 C  CA  . THR A 1 163 ? 24.208  5.177   9.077   1.00 11.83 ? 151 THR A CA  1 
ATOM   1208 C  C   . THR A 1 163 ? 25.275  6.251   9.247   1.00 14.20 ? 151 THR A C   1 
ATOM   1209 O  O   . THR A 1 163 ? 25.254  6.981   10.242  1.00 12.40 ? 151 THR A O   1 
ATOM   1210 C  CB  . THR A 1 163 ? 24.672  3.875   9.748   1.00 12.47 ? 151 THR A CB  1 
ATOM   1211 O  OG1 . THR A 1 163 ? 25.857  3.370   9.114   1.00 12.64 ? 151 THR A OG1 1 
ATOM   1212 C  CG2 . THR A 1 163 ? 23.565  2.801   9.695   1.00 9.30  ? 151 THR A CG2 1 
ATOM   1213 N  N   . GLN A 1 164 ? 26.201  6.382   8.291   1.00 13.75 ? 152 GLN A N   1 
ATOM   1214 C  CA  . GLN A 1 164 ? 27.237  7.398   8.446   1.00 15.07 ? 152 GLN A CA  1 
ATOM   1215 C  C   . GLN A 1 164 ? 26.649  8.795   8.558   1.00 16.71 ? 152 GLN A C   1 
ATOM   1216 O  O   . GLN A 1 164 ? 27.201  9.634   9.273   1.00 15.54 ? 152 GLN A O   1 
ATOM   1217 C  CB  . GLN A 1 164 ? 28.236  7.346   7.291   1.00 17.12 ? 152 GLN A CB  1 
ATOM   1218 C  CG  . GLN A 1 164 ? 29.502  8.205   7.537   1.00 20.57 ? 152 GLN A CG  1 
ATOM   1219 C  CD  . GLN A 1 164 ? 30.224  7.863   8.842   1.00 24.75 ? 152 GLN A CD  1 
ATOM   1220 O  OE1 . GLN A 1 164 ? 30.668  6.730   9.046   1.00 29.09 ? 152 GLN A OE1 1 
ATOM   1221 N  NE2 . GLN A 1 164 ? 30.355  8.852   9.725   1.00 29.20 ? 152 GLN A NE2 1 
ATOM   1222 N  N   . ASN A 1 165 ? 25.534  9.071   7.867   1.00 14.35 ? 153 ASN A N   1 
ATOM   1223 C  CA  . ASN A 1 165 ? 24.930  10.397  7.986   1.00 15.24 ? 153 ASN A CA  1 
ATOM   1224 C  C   . ASN A 1 165 ? 24.448  10.666  9.409   1.00 14.64 ? 153 ASN A C   1 
ATOM   1225 O  O   . ASN A 1 165 ? 24.526  11.801  9.895   1.00 14.15 ? 153 ASN A O   1 
ATOM   1226 C  CB  . ASN A 1 165 ? 23.776  10.550  6.987   1.00 16.60 ? 153 ASN A CB  1 
ATOM   1227 C  CG  . ASN A 1 165 ? 24.244  10.607  5.540   1.00 22.90 ? 153 ASN A CG  1 
ATOM   1228 O  OD1 . ASN A 1 165 ? 25.437  10.767  5.262   1.00 20.15 ? 153 ASN A OD1 1 
ATOM   1229 N  ND2 . ASN A 1 165 ? 23.297  10.474  4.601   1.00 18.99 ? 153 ASN A ND2 1 
ATOM   1230 N  N   . HIS A 1 166 ? 23.958  9.642   10.102  1.00 12.32 ? 154 HIS A N   1 
ATOM   1231 C  CA  . HIS A 1 166 ? 23.523  9.848   11.474  1.00 11.49 ? 154 HIS A CA  1 
ATOM   1232 C  C   . HIS A 1 166 ? 24.719  10.038  12.395  1.00 11.11 ? 154 HIS A C   1 
ATOM   1233 O  O   . HIS A 1 166 ? 24.731  10.942  13.239  1.00 13.15 ? 154 HIS A O   1 
ATOM   1234 C  CB  . HIS A 1 166 ? 22.670  8.669   11.923  1.00 10.77 ? 154 HIS A CB  1 
ATOM   1235 C  CG  . HIS A 1 166 ? 21.384  8.572   11.171  1.00 8.07  ? 154 HIS A CG  1 
ATOM   1236 N  ND1 . HIS A 1 166 ? 20.252  9.259   11.550  1.00 10.17 ? 154 HIS A ND1 1 
ATOM   1237 C  CD2 . HIS A 1 166 ? 21.062  7.908   10.035  1.00 11.43 ? 154 HIS A CD2 1 
ATOM   1238 C  CE1 . HIS A 1 166 ? 19.277  9.002   10.695  1.00 10.47 ? 154 HIS A CE1 1 
ATOM   1239 N  NE2 . HIS A 1 166 ? 19.742  8.185   9.765   1.00 12.22 ? 154 HIS A NE2 1 
ATOM   1240 N  N   . PHE A 1 167 ? 25.734  9.191   12.234  1.00 13.91 ? 155 PHE A N   1 
ATOM   1241 C  CA  . PHE A 1 167 ? 26.931  9.302   13.059  1.00 13.21 ? 155 PHE A CA  1 
ATOM   1242 C  C   . PHE A 1 167 ? 27.594  10.669  12.887  1.00 16.20 ? 155 PHE A C   1 
ATOM   1243 O  O   . PHE A 1 167 ? 28.063  11.264  13.867  1.00 15.47 ? 155 PHE A O   1 
ATOM   1244 C  CB  . PHE A 1 167 ? 27.913  8.179   12.715  1.00 12.28 ? 155 PHE A CB  1 
ATOM   1245 C  CG  . PHE A 1 167 ? 27.361  6.793   12.914  1.00 12.92 ? 155 PHE A CG  1 
ATOM   1246 C  CD1 . PHE A 1 167 ? 26.297  6.564   13.769  1.00 16.63 ? 155 PHE A CD1 1 
ATOM   1247 C  CD2 . PHE A 1 167 ? 27.902  5.723   12.230  1.00 15.62 ? 155 PHE A CD2 1 
ATOM   1248 C  CE1 . PHE A 1 167 ? 25.791  5.274   13.947  1.00 19.11 ? 155 PHE A CE1 1 
ATOM   1249 C  CE2 . PHE A 1 167 ? 27.397  4.436   12.384  1.00 16.64 ? 155 PHE A CE2 1 
ATOM   1250 C  CZ  . PHE A 1 167 ? 26.346  4.210   13.255  1.00 15.30 ? 155 PHE A CZ  1 
ATOM   1251 N  N   . ASP A 1 168 ? 27.637  11.176  11.651  1.00 14.74 ? 156 ASP A N   1 
ATOM   1252 C  CA  . ASP A 1 168 ? 28.182  12.514  11.399  1.00 18.13 ? 156 ASP A CA  1 
ATOM   1253 C  C   . ASP A 1 168 ? 27.350  13.585  12.090  1.00 20.23 ? 156 ASP A C   1 
ATOM   1254 O  O   . ASP A 1 168 ? 27.894  14.535  12.667  1.00 16.89 ? 156 ASP A O   1 
ATOM   1255 C  CB  . ASP A 1 168 ? 28.222  12.815  9.895   1.00 17.54 ? 156 ASP A CB  1 
ATOM   1256 C  CG  . ASP A 1 168 ? 29.280  12.021  9.139   1.00 25.72 ? 156 ASP A CG  1 
ATOM   1257 O  OD1 . ASP A 1 168 ? 30.150  11.385  9.775   1.00 24.88 ? 156 ASP A OD1 1 
ATOM   1258 O  OD2 . ASP A 1 168 ? 29.228  12.042  7.883   1.00 25.87 ? 156 ASP A OD2 1 
ATOM   1259 N  N   . ALA A 1 169 ? 26.022  13.471  12.004  1.00 17.74 ? 157 ALA A N   1 
ATOM   1260 C  CA  . ALA A 1 169 ? 25.152  14.460  12.629  1.00 16.33 ? 157 ALA A CA  1 
ATOM   1261 C  C   . ALA A 1 169 ? 25.305  14.456  14.145  1.00 14.56 ? 157 ALA A C   1 
ATOM   1262 O  O   . ALA A 1 169 ? 25.326  15.520  14.781  1.00 16.38 ? 157 ALA A O   1 
ATOM   1263 C  CB  . ALA A 1 169 ? 23.701  14.193  12.233  1.00 17.11 ? 157 ALA A CB  1 
ATOM   1264 N  N   . TRP A 1 170 ? 25.397  13.270  14.747  1.00 12.97 ? 158 TRP A N   1 
ATOM   1265 C  CA  . TRP A 1 170 ? 25.610  13.202  16.186  1.00 13.34 ? 158 TRP A CA  1 
ATOM   1266 C  C   . TRP A 1 170 ? 26.937  13.845  16.573  1.00 13.63 ? 158 TRP A C   1 
ATOM   1267 O  O   . TRP A 1 170 ? 27.002  14.612  17.541  1.00 14.25 ? 158 TRP A O   1 
ATOM   1268 C  CB  . TRP A 1 170 ? 25.567  11.755  16.670  1.00 14.95 ? 158 TRP A CB  1 
ATOM   1269 C  CG  . TRP A 1 170 ? 24.244  11.106  16.439  1.00 13.59 ? 158 TRP A CG  1 
ATOM   1270 C  CD1 . TRP A 1 170 ? 23.056  11.732  16.176  1.00 18.39 ? 158 TRP A CD1 1 
ATOM   1271 C  CD2 . TRP A 1 170 ? 23.976  9.703   16.428  1.00 14.87 ? 158 TRP A CD2 1 
ATOM   1272 N  NE1 . TRP A 1 170 ? 22.059  10.794  15.995  1.00 17.96 ? 158 TRP A NE1 1 
ATOM   1273 C  CE2 . TRP A 1 170 ? 22.600  9.541   16.150  1.00 15.41 ? 158 TRP A CE2 1 
ATOM   1274 C  CE3 . TRP A 1 170 ? 24.764  8.566   16.621  1.00 12.05 ? 158 TRP A CE3 1 
ATOM   1275 C  CZ2 . TRP A 1 170 ? 21.996  8.284   16.072  1.00 16.47 ? 158 TRP A CZ2 1 
ATOM   1276 C  CZ3 . TRP A 1 170 ? 24.167  7.313   16.523  1.00 12.55 ? 158 TRP A CZ3 1 
ATOM   1277 C  CH2 . TRP A 1 170 ? 22.795  7.184   16.254  1.00 12.35 ? 158 TRP A CH2 1 
ATOM   1278 N  N   . LYS A 1 171 ? 28.003  13.550  15.826  1.00 13.87 ? 159 LYS A N   1 
ATOM   1279 C  CA  . LYS A 1 171 ? 29.301  14.153  16.139  1.00 15.13 ? 159 LYS A CA  1 
ATOM   1280 C  C   . LYS A 1 171 ? 29.257  15.674  15.988  1.00 18.45 ? 159 LYS A C   1 
ATOM   1281 O  O   . LYS A 1 171 ? 29.846  16.406  16.796  1.00 16.82 ? 159 LYS A O   1 
ATOM   1282 C  CB  . LYS A 1 171 ? 30.387  13.555  15.249  1.00 16.82 ? 159 LYS A CB  1 
ATOM   1283 C  CG  . LYS A 1 171 ? 31.797  14.091  15.576  1.00 25.40 ? 159 LYS A CG  1 
ATOM   1284 C  CD  . LYS A 1 171 ? 32.721  13.939  14.378  1.00 29.83 ? 159 LYS A CD  1 
ATOM   1285 C  CE  . LYS A 1 171 ? 33.584  12.711  14.534  1.00 39.06 ? 159 LYS A CE  1 
ATOM   1286 N  NZ  . LYS A 1 171 ? 35.011  12.990  14.190  1.00 36.49 ? 159 LYS A NZ  1 
ATOM   1287 N  N   . ASN A 1 172 ? 28.560  16.171  14.960  1.00 18.64 ? 160 ASN A N   1 
ATOM   1288 C  CA  . ASN A 1 172 ? 28.438  17.616  14.782  1.00 20.72 ? 160 ASN A CA  1 
ATOM   1289 C  C   . ASN A 1 172 ? 27.672  18.255  15.932  1.00 22.42 ? 160 ASN A C   1 
ATOM   1290 O  O   . ASN A 1 172 ? 27.946  19.401  16.304  1.00 22.39 ? 160 ASN A O   1 
ATOM   1291 C  CB  . ASN A 1 172 ? 27.766  17.924  13.442  1.00 22.87 ? 160 ASN A CB  1 
ATOM   1292 C  CG  . ASN A 1 172 ? 27.583  19.410  13.211  1.00 33.59 ? 160 ASN A CG  1 
ATOM   1293 O  OD1 . ASN A 1 172 ? 28.534  20.125  12.886  1.00 36.65 ? 160 ASN A OD1 1 
ATOM   1294 N  ND2 . ASN A 1 172 ? 26.347  19.886  13.371  1.00 33.13 ? 160 ASN A ND2 1 
ATOM   1295 N  N   . ALA A 1 173 ? 26.722  17.531  16.517  1.00 19.88 ? 161 ALA A N   1 
ATOM   1296 C  CA  . ALA A 1 173 ? 25.992  18.006  17.683  1.00 19.85 ? 161 ALA A CA  1 
ATOM   1297 C  C   . ALA A 1 173 ? 26.791  17.876  18.971  1.00 22.25 ? 161 ALA A C   1 
ATOM   1298 O  O   . ALA A 1 173 ? 26.258  18.187  20.042  1.00 26.52 ? 161 ALA A O   1 
ATOM   1299 C  CB  . ALA A 1 173 ? 24.667  17.241  17.820  1.00 19.80 ? 161 ALA A CB  1 
ATOM   1300 N  N   . GLY A 1 174 ? 28.039  17.418  18.896  1.00 18.57 ? 162 GLY A N   1 
ATOM   1301 C  CA  . GLY A 1 174 ? 28.876  17.256  20.064  1.00 21.84 ? 162 GLY A CA  1 
ATOM   1302 C  C   . GLY A 1 174 ? 28.795  15.910  20.743  1.00 24.32 ? 162 GLY A C   1 
ATOM   1303 O  O   . GLY A 1 174 ? 29.272  15.782  21.876  1.00 29.05 ? 162 GLY A O   1 
ATOM   1304 N  N   . LEU A 1 175 ? 28.216  14.898  20.095  1.00 19.53 ? 163 LEU A N   1 
ATOM   1305 C  CA  . LEU A 1 175 ? 28.018  13.583  20.700  1.00 20.87 ? 163 LEU A CA  1 
ATOM   1306 C  C   . LEU A 1 175 ? 29.155  12.660  20.270  1.00 23.73 ? 163 LEU A C   1 
ATOM   1307 O  O   . LEU A 1 175 ? 29.219  12.249  19.105  1.00 25.10 ? 163 LEU A O   1 
ATOM   1308 C  CB  . LEU A 1 175 ? 26.662  13.003  20.299  1.00 17.98 ? 163 LEU A CB  1 
ATOM   1309 C  CG  . LEU A 1 175 ? 25.446  13.886  20.594  1.00 18.49 ? 163 LEU A CG  1 
ATOM   1310 C  CD1 . LEU A 1 175 ? 24.162  13.184  20.157  1.00 17.97 ? 163 LEU A CD1 1 
ATOM   1311 C  CD2 . LEU A 1 175 ? 25.397  14.246  22.077  1.00 21.10 ? 163 LEU A CD2 1 
ATOM   1312 N  N   . GLU A 1 176 ? 30.022  12.306  21.222  1.00 21.49 ? 164 GLU A N   1 
ATOM   1313 C  CA  . GLU A 1 176 ? 31.204  11.505  20.938  1.00 25.18 ? 164 GLU A CA  1 
ATOM   1314 C  C   . GLU A 1 176 ? 30.858  10.027  20.816  1.00 18.46 ? 164 GLU A C   1 
ATOM   1315 O  O   . GLU A 1 176 ? 30.125  9.476   21.636  1.00 17.47 ? 164 GLU A O   1 
ATOM   1316 C  CB  . GLU A 1 176 ? 32.253  11.679  22.040  1.00 25.03 ? 164 GLU A CB  1 
ATOM   1317 C  CG  . GLU A 1 176 ? 32.732  13.107  22.247  1.00 38.31 ? 164 GLU A CG  1 
ATOM   1318 C  CD  . GLU A 1 176 ? 34.200  13.286  21.905  1.00 44.47 ? 164 GLU A CD  1 
ATOM   1319 O  OE1 . GLU A 1 176 ? 35.011  12.394  22.237  1.00 43.63 ? 164 GLU A OE1 1 
ATOM   1320 O  OE2 . GLU A 1 176 ? 34.545  14.317  21.299  1.00 50.04 ? 164 GLU A OE2 1 
ATOM   1321 N  N   . MET A 1 177 ? 31.421  9.381   19.805  1.00 19.06 ? 165 MET A N   1 
ATOM   1322 C  CA  . MET A 1 177 ? 31.247  7.954   19.587  1.00 17.74 ? 165 MET A CA  1 
ATOM   1323 C  C   . MET A 1 177 ? 32.562  7.235   19.847  1.00 15.51 ? 165 MET A C   1 
ATOM   1324 O  O   . MET A 1 177 ? 33.630  7.756   19.523  1.00 18.01 ? 165 MET A O   1 
ATOM   1325 C  CB  . MET A 1 177 ? 30.788  7.673   18.160  1.00 20.27 ? 165 MET A CB  1 
ATOM   1326 C  CG  . MET A 1 177 ? 29.528  8.424   17.794  1.00 29.94 ? 165 MET A CG  1 
ATOM   1327 S  SD  . MET A 1 177 ? 28.136  7.367   18.169  1.00 38.38 ? 165 MET A SD  1 
ATOM   1328 C  CE  . MET A 1 177 ? 28.163  6.291   16.738  1.00 22.72 ? 165 MET A CE  1 
ATOM   1329 N  N   . GLY A 1 178 ? 32.480  6.031   20.396  1.00 12.02 ? 166 GLY A N   1 
ATOM   1330 C  CA  . GLY A 1 178 ? 33.650  5.209   20.626  1.00 12.72 ? 166 GLY A CA  1 
ATOM   1331 C  C   . GLY A 1 178 ? 33.915  4.247   19.488  1.00 14.73 ? 166 GLY A C   1 
ATOM   1332 O  O   . GLY A 1 178 ? 33.509  4.464   18.340  1.00 15.50 ? 166 GLY A O   1 
ATOM   1333 N  N   . THR A 1 179 ? 34.625  3.172   19.823  1.00 13.52 ? 167 THR A N   1 
ATOM   1334 C  CA  . THR A 1 179 ? 34.883  2.082   18.890  1.00 13.87 ? 167 THR A CA  1 
ATOM   1335 C  C   . THR A 1 179 ? 33.613  1.266   18.689  1.00 12.29 ? 167 THR A C   1 
ATOM   1336 O  O   . THR A 1 179 ? 32.952  0.886   19.655  1.00 13.11 ? 167 THR A O   1 
ATOM   1337 C  CB  . THR A 1 179 ? 35.997  1.189   19.441  1.00 19.18 ? 167 THR A CB  1 
ATOM   1338 O  OG1 . THR A 1 179 ? 37.194  1.964   19.589  1.00 24.04 ? 167 THR A OG1 1 
ATOM   1339 C  CG2 . THR A 1 179 ? 36.265  0.021   18.516  1.00 19.39 ? 167 THR A CG2 1 
ATOM   1340 N  N   . HIS A 1 180 ? 33.273  0.985   17.435  1.00 14.55 ? 168 HIS A N   1 
ATOM   1341 C  CA  . HIS A 1 180 ? 31.993  0.341   17.162  1.00 11.80 ? 168 HIS A CA  1 
ATOM   1342 C  C   . HIS A 1 180 ? 31.988  -1.100  17.650  1.00 14.07 ? 168 HIS A C   1 
ATOM   1343 O  O   . HIS A 1 180 ? 32.951  -1.845  17.437  1.00 14.84 ? 168 HIS A O   1 
ATOM   1344 C  CB  . HIS A 1 180 ? 31.685  0.403   15.663  1.00 13.54 ? 168 HIS A CB  1 
ATOM   1345 C  CG  . HIS A 1 180 ? 31.177  1.735   15.223  1.00 19.12 ? 168 HIS A CG  1 
ATOM   1346 N  ND1 . HIS A 1 180 ? 29.845  1.975   14.979  1.00 22.32 ? 168 HIS A ND1 1 
ATOM   1347 C  CD2 . HIS A 1 180 ? 31.812  2.915   15.032  1.00 25.52 ? 168 HIS A CD2 1 
ATOM   1348 C  CE1 . HIS A 1 180 ? 29.682  3.238   14.631  1.00 25.78 ? 168 HIS A CE1 1 
ATOM   1349 N  NE2 . HIS A 1 180 ? 30.860  3.830   14.652  1.00 22.64 ? 168 HIS A NE2 1 
ATOM   1350 N  N   . ASN A 1 181 ? 30.907  -1.475  18.336  1.00 11.01 ? 169 ASN A N   1 
ATOM   1351 C  CA  . ASN A 1 181 ? 30.588  -2.866  18.632  1.00 10.03 ? 169 ASN A CA  1 
ATOM   1352 C  C   . ASN A 1 181 ? 29.472  -3.267  17.670  1.00 9.87  ? 169 ASN A C   1 
ATOM   1353 O  O   . ASN A 1 181 ? 29.508  -2.861  16.505  1.00 10.86 ? 169 ASN A O   1 
ATOM   1354 C  CB  . ASN A 1 181 ? 30.194  -3.033  20.105  1.00 12.07 ? 169 ASN A CB  1 
ATOM   1355 C  CG  . ASN A 1 181 ? 30.196  -4.479  20.554  1.00 14.09 ? 169 ASN A CG  1 
ATOM   1356 O  OD1 . ASN A 1 181 ? 29.167  -5.144  20.525  1.00 15.21 ? 169 ASN A OD1 1 
ATOM   1357 N  ND2 . ASN A 1 181 ? 31.355  -4.966  21.011  1.00 17.06 ? 169 ASN A ND2 1 
ATOM   1358 N  N   . TYR A 1 182 ? 28.465  -4.015  18.109  1.00 8.67  ? 170 TYR A N   1 
ATOM   1359 C  CA  . TYR A 1 182 ? 27.529  -4.502  17.086  1.00 7.58  ? 170 TYR A CA  1 
ATOM   1360 C  C   . TYR A 1 182 ? 26.594  -3.405  16.572  1.00 8.21  ? 170 TYR A C   1 
ATOM   1361 O  O   . TYR A 1 182 ? 26.395  -2.358  17.194  1.00 8.35  ? 170 TYR A O   1 
ATOM   1362 C  CB  . TYR A 1 182 ? 26.723  -5.702  17.595  1.00 8.74  ? 170 TYR A CB  1 
ATOM   1363 C  CG  . TYR A 1 182 ? 25.693  -5.495  18.693  1.00 9.24  ? 170 TYR A CG  1 
ATOM   1364 C  CD1 . TYR A 1 182 ? 24.479  -4.871  18.432  1.00 9.86  ? 170 TYR A CD1 1 
ATOM   1365 C  CD2 . TYR A 1 182 ? 25.900  -6.012  19.963  1.00 10.27 ? 170 TYR A CD2 1 
ATOM   1366 C  CE1 . TYR A 1 182 ? 23.517  -4.729  19.413  1.00 10.90 ? 170 TYR A CE1 1 
ATOM   1367 C  CE2 . TYR A 1 182 ? 24.938  -5.882  20.956  1.00 10.73 ? 170 TYR A CE2 1 
ATOM   1368 C  CZ  . TYR A 1 182 ? 23.750  -5.235  20.673  1.00 11.14 ? 170 TYR A CZ  1 
ATOM   1369 O  OH  . TYR A 1 182 ? 22.809  -5.099  21.661  1.00 11.69 ? 170 TYR A OH  1 
ATOM   1370 N  N   . MET A 1 183 ? 26.035  -3.661  15.388  1.00 9.26  ? 171 MET A N   1 
ATOM   1371 C  CA  . MET A 1 183 ? 25.007  -2.812  14.791  1.00 8.68  ? 171 MET A CA  1 
ATOM   1372 C  C   . MET A 1 183 ? 23.991  -3.730  14.122  1.00 9.44  ? 171 MET A C   1 
ATOM   1373 O  O   . MET A 1 183 ? 24.361  -4.536  13.262  1.00 8.42  ? 171 MET A O   1 
ATOM   1374 C  CB  . MET A 1 183 ? 25.611  -1.828  13.783  1.00 8.11  ? 171 MET A CB  1 
ATOM   1375 C  CG  . MET A 1 183 ? 24.553  -0.877  13.177  1.00 9.58  ? 171 MET A CG  1 
ATOM   1376 S  SD  . MET A 1 183 ? 25.269  0.407   12.105  1.00 13.40 ? 171 MET A SD  1 
ATOM   1377 C  CE  . MET A 1 183 ? 25.819  -0.580  10.740  1.00 14.91 ? 171 MET A CE  1 
ATOM   1378 N  N   . ILE A 1 184 ? 22.717  -3.627  14.512  1.00 8.32  ? 172 ILE A N   1 
ATOM   1379 C  CA  . ILE A 1 184 ? 21.686  -4.541  14.024  1.00 6.00  ? 172 ILE A CA  1 
ATOM   1380 C  C   . ILE A 1 184 ? 20.447  -3.742  13.645  1.00 6.22  ? 172 ILE A C   1 
ATOM   1381 O  O   . ILE A 1 184 ? 20.282  -2.586  14.040  1.00 8.87  ? 172 ILE A O   1 
ATOM   1382 C  CB  . ILE A 1 184 ? 21.308  -5.619  15.076  1.00 8.50  ? 172 ILE A CB  1 
ATOM   1383 C  CG1 . ILE A 1 184 ? 20.832  -4.976  16.389  1.00 7.39  ? 172 ILE A CG1 1 
ATOM   1384 C  CG2 . ILE A 1 184 ? 22.472  -6.594  15.329  1.00 7.51  ? 172 ILE A CG2 1 
ATOM   1385 C  CD1 . ILE A 1 184 ? 20.327  -5.999  17.441  1.00 9.61  ? 172 ILE A CD1 1 
ATOM   1386 N  N   . VAL A 1 185 ? 19.572  -4.363  12.854  1.00 6.59  ? 173 VAL A N   1 
ATOM   1387 C  CA  . VAL A 1 185 ? 18.240  -3.802  12.639  1.00 6.48  ? 173 VAL A CA  1 
ATOM   1388 C  C   . VAL A 1 185 ? 17.352  -4.474  13.676  1.00 8.03  ? 173 VAL A C   1 
ATOM   1389 O  O   . VAL A 1 185 ? 17.071  -5.673  13.583  1.00 9.29  ? 173 VAL A O   1 
ATOM   1390 C  CB  . VAL A 1 185 ? 17.718  -4.018  11.214  1.00 8.12  ? 173 VAL A CB  1 
ATOM   1391 C  CG1 . VAL A 1 185 ? 16.297  -3.410  11.085  1.00 9.67  ? 173 VAL A CG1 1 
ATOM   1392 C  CG2 . VAL A 1 185 ? 18.651  -3.351  10.190  1.00 10.81 ? 173 VAL A CG2 1 
ATOM   1393 N  N   . ALA A 1 186 ? 16.957  -3.716  14.689  1.00 7.56  ? 174 ALA A N   1 
ATOM   1394 C  CA  . ALA A 1 186 ? 16.398  -4.277  15.908  1.00 7.81  ? 174 ALA A CA  1 
ATOM   1395 C  C   . ALA A 1 186 ? 14.918  -3.975  16.053  1.00 8.90  ? 174 ALA A C   1 
ATOM   1396 O  O   . ALA A 1 186 ? 14.474  -2.854  15.803  1.00 11.35 ? 174 ALA A O   1 
ATOM   1397 C  CB  . ALA A 1 186 ? 17.107  -3.732  17.146  1.00 8.66  ? 174 ALA A CB  1 
ATOM   1398 N  N   . THR A 1 187 ? 14.188  -4.974  16.527  1.00 8.75  ? 175 THR A N   1 
ATOM   1399 C  CA  . THR A 1 187 ? 12.841  -4.815  17.042  1.00 7.78  ? 175 THR A CA  1 
ATOM   1400 C  C   . THR A 1 187 ? 12.932  -4.803  18.562  1.00 9.09  ? 175 THR A C   1 
ATOM   1401 O  O   . THR A 1 187 ? 13.478  -5.734  19.157  1.00 9.43  ? 175 THR A O   1 
ATOM   1402 C  CB  . THR A 1 187 ? 11.955  -5.962  16.574  1.00 8.02  ? 175 THR A CB  1 
ATOM   1403 O  OG1 . THR A 1 187 ? 11.926  -5.971  15.146  1.00 10.23 ? 175 THR A OG1 1 
ATOM   1404 C  CG2 . THR A 1 187 ? 10.550  -5.771  17.105  1.00 10.35 ? 175 THR A CG2 1 
ATOM   1405 N  N   . ALA A 1 188 ? 12.413  -3.753  19.185  1.00 7.95  ? 176 ALA A N   1 
ATOM   1406 C  CA  . ALA A 1 188 ? 12.439  -3.624  20.634  1.00 10.05 ? 176 ALA A CA  1 
ATOM   1407 C  C   . ALA A 1 188 ? 11.015  -3.483  21.139  1.00 12.15 ? 176 ALA A C   1 
ATOM   1408 O  O   . ALA A 1 188 ? 10.134  -3.010  20.419  1.00 10.09 ? 176 ALA A O   1 
ATOM   1409 C  CB  . ALA A 1 188 ? 13.280  -2.415  21.068  1.00 10.21 ? 176 ALA A CB  1 
ATOM   1410 N  N   . GLY A 1 189 ? 10.784  -3.923  22.368  1.00 10.17 ? 177 GLY A N   1 
ATOM   1411 C  CA  . GLY A 1 189 ? 9.477   -3.754  22.970  1.00 10.25 ? 177 GLY A CA  1 
ATOM   1412 C  C   . GLY A 1 189 ? 9.582   -3.637  24.473  1.00 11.58 ? 177 GLY A C   1 
ATOM   1413 O  O   . GLY A 1 189 ? 10.599  -3.999  25.084  1.00 11.85 ? 177 GLY A O   1 
ATOM   1414 N  N   . TYR A 1 190 ? 8.510   -3.120  25.067  1.00 12.32 ? 178 TYR A N   1 
ATOM   1415 C  CA  . TYR A 1 190 ? 8.413   -3.072  26.525  1.00 14.05 ? 178 TYR A CA  1 
ATOM   1416 C  C   . TYR A 1 190 ? 6.946   -3.098  26.921  1.00 12.26 ? 178 TYR A C   1 
ATOM   1417 O  O   . TYR A 1 190 ? 6.174   -2.238  26.484  1.00 11.17 ? 178 TYR A O   1 
ATOM   1418 C  CB  . TYR A 1 190 ? 9.078   -1.825  27.086  1.00 12.87 ? 178 TYR A CB  1 
ATOM   1419 C  CG  . TYR A 1 190 ? 8.943   -1.735  28.585  1.00 18.55 ? 178 TYR A CG  1 
ATOM   1420 C  CD1 . TYR A 1 190 ? 9.585   -2.649  29.414  1.00 20.06 ? 178 TYR A CD1 1 
ATOM   1421 C  CD2 . TYR A 1 190 ? 8.143   -0.764  29.173  1.00 18.85 ? 178 TYR A CD2 1 
ATOM   1422 C  CE1 . TYR A 1 190 ? 9.467   -2.575  30.785  1.00 22.17 ? 178 TYR A CE1 1 
ATOM   1423 C  CE2 . TYR A 1 190 ? 8.019   -0.686  30.535  1.00 24.22 ? 178 TYR A CE2 1 
ATOM   1424 C  CZ  . TYR A 1 190 ? 8.683   -1.586  31.341  1.00 25.03 ? 178 TYR A CZ  1 
ATOM   1425 O  OH  . TYR A 1 190 ? 8.547   -1.499  32.708  1.00 31.32 ? 178 TYR A OH  1 
ATOM   1426 N  N   . GLN A 1 191 ? 6.575   -4.070  27.747  1.00 10.45 ? 179 GLN A N   1 
ATOM   1427 C  CA  . GLN A 1 191 ? 5.213   -4.210  28.269  1.00 12.73 ? 179 GLN A CA  1 
ATOM   1428 C  C   . GLN A 1 191 ? 4.174   -4.089  27.150  1.00 13.83 ? 179 GLN A C   1 
ATOM   1429 O  O   . GLN A 1 191 ? 3.263   -3.253  27.172  1.00 11.89 ? 179 GLN A O   1 
ATOM   1430 C  CB  . GLN A 1 191 ? 4.992   -3.203  29.401  1.00 12.70 ? 179 GLN A CB  1 
ATOM   1431 C  CG  . GLN A 1 191 ? 5.882   -3.575  30.600  1.00 17.48 ? 179 GLN A CG  1 
ATOM   1432 C  CD  . GLN A 1 191 ? 5.425   -2.992  31.914  1.00 21.33 ? 179 GLN A CD  1 
ATOM   1433 O  OE1 . GLN A 1 191 ? 4.758   -1.963  31.950  1.00 25.30 ? 179 GLN A OE1 1 
ATOM   1434 N  NE2 . GLN A 1 191 ? 5.800   -3.645  33.012  1.00 23.27 ? 179 GLN A NE2 1 
ATOM   1435 N  N   . SER A 1 192 ? 4.334   -4.961  26.156  1.00 11.76 ? 180 SER A N   1 
ATOM   1436 C  CA  . SER A 1 192 ? 3.468   -4.970  24.982  1.00 10.69 ? 180 SER A CA  1 
ATOM   1437 C  C   . SER A 1 192 ? 3.419   -6.382  24.416  1.00 11.39 ? 180 SER A C   1 
ATOM   1438 O  O   . SER A 1 192 ? 4.024   -7.313  24.956  1.00 10.60 ? 180 SER A O   1 
ATOM   1439 C  CB  . SER A 1 192 ? 3.964   -3.978  23.921  1.00 9.62  ? 180 SER A CB  1 
ATOM   1440 O  OG  . SER A 1 192 ? 5.270   -4.328  23.481  1.00 10.75 ? 180 SER A OG  1 
ATOM   1441 N  N   . SER A 1 193 ? 2.695   -6.533  23.307  1.00 8.93  ? 181 SER A N   1 
ATOM   1442 C  CA  . SER A 1 193 ? 2.681   -7.767  22.534  1.00 10.52 ? 181 SER A CA  1 
ATOM   1443 C  C   . SER A 1 193 ? 2.924   -7.402  21.078  1.00 10.32 ? 181 SER A C   1 
ATOM   1444 O  O   . SER A 1 193 ? 2.842   -6.235  20.703  1.00 12.50 ? 181 SER A O   1 
ATOM   1445 C  CB  . SER A 1 193 ? 1.351   -8.521  22.673  1.00 9.99  ? 181 SER A CB  1 
ATOM   1446 O  OG  . SER A 1 193 ? 1.073   -8.880  24.016  1.00 15.27 ? 181 SER A OG  1 
ATOM   1447 N  N   . GLY A 1 194 ? 3.258   -8.392  20.264  1.00 10.29 ? 182 GLY A N   1 
ATOM   1448 C  CA  . GLY A 1 194 ? 3.316   -8.162  18.836  1.00 8.70  ? 182 GLY A CA  1 
ATOM   1449 C  C   . GLY A 1 194 ? 4.129   -9.220  18.112  1.00 11.10 ? 182 GLY A C   1 
ATOM   1450 O  O   . GLY A 1 194 ? 4.459   -10.277 18.654  1.00 11.16 ? 182 GLY A O   1 
ATOM   1451 N  N   . SER A 1 195 ? 4.411   -8.915  16.851  1.00 10.48 ? 183 SER A N   1 
ATOM   1452 C  CA  . SER A 1 195 ? 5.264   -9.777  16.056  1.00 11.03 ? 183 SER A CA  1 
ATOM   1453 C  C   . SER A 1 195 ? 5.979   -8.914  15.032  1.00 12.30 ? 183 SER A C   1 
ATOM   1454 O  O   . SER A 1 195 ? 5.527   -7.817  14.683  1.00 10.95 ? 183 SER A O   1 
ATOM   1455 C  CB  . SER A 1 195 ? 4.476   -10.899 15.367  1.00 13.64 ? 183 SER A CB  1 
ATOM   1456 O  OG  . SER A 1 195 ? 3.574   -10.380 14.420  1.00 16.50 ? 183 SER A OG  1 
ATOM   1457 N  N   . ALA A 1 196 ? 7.100   -9.428  14.543  1.00 9.25  ? 184 ALA A N   1 
ATOM   1458 C  CA  . ALA A 1 196 ? 7.808   -8.760  13.466  1.00 8.68  ? 184 ALA A CA  1 
ATOM   1459 C  C   . ALA A 1 196 ? 8.602   -9.800  12.698  1.00 12.11 ? 184 ALA A C   1 
ATOM   1460 O  O   . ALA A 1 196 ? 9.031   -10.815 13.258  1.00 11.73 ? 184 ALA A O   1 
ATOM   1461 C  CB  . ALA A 1 196 ? 8.740   -7.652  13.983  1.00 9.88  ? 184 ALA A CB  1 
ATOM   1462 N  N   . SER A 1 197 ? 8.789   -9.536  11.407  1.00 9.40  ? 185 SER A N   1 
ATOM   1463 C  CA  . SER A 1 197 ? 9.589   -10.396 10.538  1.00 9.46  ? 185 SER A CA  1 
ATOM   1464 C  C   . SER A 1 197 ? 10.401  -9.471  9.651   1.00 9.56  ? 185 SER A C   1 
ATOM   1465 O  O   . SER A 1 197 ? 9.843   -8.813  8.768   1.00 10.47 ? 185 SER A O   1 
ATOM   1466 C  CB  . SER A 1 197 ? 8.716   -11.332 9.694   1.00 13.11 ? 185 SER A CB  1 
ATOM   1467 O  OG  . SER A 1 197 ? 8.128   -12.346 10.489  1.00 18.74 ? 185 SER A OG  1 
ATOM   1468 N  N   . ILE A 1 198 ? 11.706  -9.413  9.883   1.00 10.19 ? 186 ILE A N   1 
ATOM   1469 C  CA  . ILE A 1 198 ? 12.560  -8.383  9.298   1.00 8.03  ? 186 ILE A CA  1 
ATOM   1470 C  C   . ILE A 1 198 ? 13.719  -9.061  8.589   1.00 11.76 ? 186 ILE A C   1 
ATOM   1471 O  O   . ILE A 1 198 ? 14.297  -10.022 9.107   1.00 9.87  ? 186 ILE A O   1 
ATOM   1472 C  CB  . ILE A 1 198 ? 13.082  -7.402  10.376  1.00 9.71  ? 186 ILE A CB  1 
ATOM   1473 C  CG1 . ILE A 1 198 ? 11.926  -6.618  11.007  1.00 12.90 ? 186 ILE A CG1 1 
ATOM   1474 C  CG2 . ILE A 1 198 ? 14.153  -6.424  9.808   1.00 9.99  ? 186 ILE A CG2 1 
ATOM   1475 C  CD1 . ILE A 1 198 ? 11.257  -5.615  10.058  1.00 14.65 ? 186 ILE A CD1 1 
ATOM   1476 N  N   . THR A 1 199 ? 14.060  -8.565  7.402   1.00 10.66 ? 187 THR A N   1 
ATOM   1477 C  CA  . THR A 1 199 ? 15.197  -9.092  6.658   1.00 11.01 ? 187 THR A CA  1 
ATOM   1478 C  C   . THR A 1 199 ? 16.206  -7.977  6.434   1.00 12.80 ? 187 THR A C   1 
ATOM   1479 O  O   . THR A 1 199 ? 15.863  -6.931  5.878   1.00 12.56 ? 187 THR A O   1 
ATOM   1480 C  CB  . THR A 1 199 ? 14.762  -9.696  5.323   1.00 14.69 ? 187 THR A CB  1 
ATOM   1481 O  OG1 . THR A 1 199 ? 13.846  -10.767 5.564   1.00 15.79 ? 187 THR A OG1 1 
ATOM   1482 C  CG2 . THR A 1 199 ? 15.987  -10.246 4.580   1.00 15.69 ? 187 THR A CG2 1 
ATOM   1483 N  N   . VAL A 1 200 ? 17.445  -8.203  6.864   1.00 9.79  ? 188 VAL A N   1 
ATOM   1484 C  CA  . VAL A 1 200 ? 18.537  -7.273  6.610   1.00 9.36  ? 188 VAL A CA  1 
ATOM   1485 C  C   . VAL A 1 200 ? 19.194  -7.708  5.304   1.00 18.88 ? 188 VAL A C   1 
ATOM   1486 O  O   . VAL A 1 200 ? 19.610  -8.862  5.170   1.00 19.03 ? 188 VAL A O   1 
ATOM   1487 C  CB  . VAL A 1 200 ? 19.540  -7.267  7.777   1.00 14.64 ? 188 VAL A CB  1 
ATOM   1488 C  CG1 . VAL A 1 200 ? 20.665  -6.287  7.513   1.00 17.35 ? 188 VAL A CG1 1 
ATOM   1489 C  CG2 . VAL A 1 200 ? 18.830  -6.907  9.069   1.00 16.62 ? 188 VAL A CG2 1 
ATOM   1490 N  N   . GLN A 1 201 ? 19.222  -6.809  4.318   1.00 23.97 ? 189 GLN A N   1 
ATOM   1491 C  CA  . GLN A 1 201 ? 19.740  -7.140  2.983   1.00 27.81 ? 189 GLN A CA  1 
ATOM   1492 C  C   . GLN A 1 201 ? 21.173  -6.649  2.821   1.00 28.62 ? 189 GLN A C   1 
ATOM   1493 O  O   . GLN A 1 201 ? 21.888  -6.460  3.815   1.00 33.56 ? 189 GLN A O   1 
ATOM   1494 C  CB  . GLN A 1 201 ? 18.851  -6.534  1.886   1.00 30.79 ? 189 GLN A CB  1 
ATOM   1495 C  CG  . GLN A 1 201 ? 17.564  -7.308  1.607   1.00 36.40 ? 189 GLN A CG  1 
ATOM   1496 C  CD  . GLN A 1 201 ? 16.407  -6.864  2.485   1.00 33.77 ? 189 GLN A CD  1 
ATOM   1497 O  OE1 . GLN A 1 201 ? 16.350  -5.716  2.933   1.00 36.16 ? 189 GLN A OE1 1 
ATOM   1498 N  NE2 . GLN A 1 201 ? 15.478  -7.777  2.740   1.00 37.98 ? 189 GLN A NE2 1 
ATOM   1499 N  N   . MET B 1 12  ? -8.978  24.228  38.097  1.00 42.48 ? 0   MET B N   1 
ATOM   1500 C  CA  . MET B 1 12  ? -8.233  24.083  36.855  1.00 38.10 ? 0   MET B CA  1 
ATOM   1501 C  C   . MET B 1 12  ? -7.236  22.933  36.905  1.00 27.73 ? 0   MET B C   1 
ATOM   1502 O  O   . MET B 1 12  ? -7.238  22.120  37.825  1.00 30.94 ? 0   MET B O   1 
ATOM   1503 C  CB  . MET B 1 12  ? -7.505  25.382  36.510  1.00 35.68 ? 0   MET B CB  1 
ATOM   1504 C  CG  . MET B 1 12  ? -8.400  26.619  36.568  1.00 52.96 ? 0   MET B CG  1 
ATOM   1505 S  SD  . MET B 1 12  ? -7.831  27.943  35.465  1.00 67.05 ? 0   MET B SD  1 
ATOM   1506 C  CE  . MET B 1 12  ? -6.111  27.504  35.273  1.00 42.22 ? 0   MET B CE  1 
ATOM   1507 N  N   . GLU B 1 13  ? -6.361  22.900  35.911  1.00 25.02 ? 1   GLU B N   1 
ATOM   1508 C  CA  . GLU B 1 13  ? -5.622  21.691  35.578  1.00 22.68 ? 1   GLU B CA  1 
ATOM   1509 C  C   . GLU B 1 13  ? -4.509  21.402  36.581  1.00 23.06 ? 1   GLU B C   1 
ATOM   1510 O  O   . GLU B 1 13  ? -3.886  22.308  37.143  1.00 21.81 ? 1   GLU B O   1 
ATOM   1511 C  CB  . GLU B 1 13  ? -5.069  21.804  34.158  1.00 27.53 ? 1   GLU B CB  1 
ATOM   1512 C  CG  . GLU B 1 13  ? -6.146  21.515  33.105  1.00 37.51 ? 1   GLU B CG  1 
ATOM   1513 C  CD  . GLU B 1 13  ? -6.487  22.716  32.218  1.00 49.00 ? 1   GLU B CD  1 
ATOM   1514 O  OE1 . GLU B 1 13  ? -6.583  23.854  32.733  1.00 51.18 ? 1   GLU B OE1 1 
ATOM   1515 O  OE2 . GLU B 1 13  ? -6.675  22.505  31.000  1.00 43.93 ? 1   GLU B OE2 1 
ATOM   1516 N  N   . ILE B 1 14  ? -4.287  20.112  36.812  1.00 15.37 ? 2   ILE B N   1 
ATOM   1517 C  CA  . ILE B 1 14  ? -3.352  19.588  37.805  1.00 21.87 ? 2   ILE B CA  1 
ATOM   1518 C  C   . ILE B 1 14  ? -2.338  18.735  37.053  1.00 20.16 ? 2   ILE B C   1 
ATOM   1519 O  O   . ILE B 1 14  ? -2.731  17.855  36.282  1.00 17.76 ? 2   ILE B O   1 
ATOM   1520 C  CB  . ILE B 1 14  ? -4.112  18.760  38.867  1.00 17.45 ? 2   ILE B CB  1 
ATOM   1521 C  CG1 . ILE B 1 14  ? -5.154  19.640  39.570  1.00 23.36 ? 2   ILE B CG1 1 
ATOM   1522 C  CG2 . ILE B 1 14  ? -3.184  18.111  39.886  1.00 20.95 ? 2   ILE B CG2 1 
ATOM   1523 C  CD1 . ILE B 1 14  ? -6.107  18.872  40.500  1.00 23.66 ? 2   ILE B CD1 1 
ATOM   1524 N  N   . THR B 1 15  ? -1.042  19.015  37.227  1.00 18.19 ? 3   THR B N   1 
ATOM   1525 C  CA  . THR B 1 15  ? -0.021  18.233  36.531  1.00 14.47 ? 3   THR B CA  1 
ATOM   1526 C  C   . THR B 1 15  ? 1.002   17.572  37.452  1.00 16.55 ? 3   THR B C   1 
ATOM   1527 O  O   . THR B 1 15  ? 1.906   16.884  36.954  1.00 18.43 ? 3   THR B O   1 
ATOM   1528 C  CB  . THR B 1 15  ? 0.712   19.091  35.490  1.00 19.95 ? 3   THR B CB  1 
ATOM   1529 O  OG1 . THR B 1 15  ? 1.433   20.137  36.150  1.00 27.94 ? 3   THR B OG1 1 
ATOM   1530 C  CG2 . THR B 1 15  ? -0.276  19.700  34.492  1.00 22.61 ? 3   THR B CG2 1 
ATOM   1531 N  N   . SER B 1 16  ? 0.883   17.741  38.768  1.00 14.81 ? 4   SER B N   1 
ATOM   1532 C  CA  . SER B 1 16  ? 1.706   17.043  39.740  1.00 15.33 ? 4   SER B CA  1 
ATOM   1533 C  C   . SER B 1 16  ? 0.792   16.389  40.762  1.00 14.07 ? 4   SER B C   1 
ATOM   1534 O  O   . SER B 1 16  ? -0.354  16.804  40.950  1.00 15.47 ? 4   SER B O   1 
ATOM   1535 C  CB  . SER B 1 16  ? 2.686   17.994  40.453  1.00 18.95 ? 4   SER B CB  1 
ATOM   1536 O  OG  . SER B 1 16  ? 3.713   18.421  39.574  1.00 28.90 ? 4   SER B OG  1 
ATOM   1537 N  N   . SER B 1 17  ? 1.319   15.372  41.442  1.00 14.03 ? 5   SER B N   1 
ATOM   1538 C  CA  . SER B 1 17  ? 0.499   14.577  42.352  1.00 12.89 ? 5   SER B CA  1 
ATOM   1539 C  C   . SER B 1 17  ? -0.198  15.444  43.390  1.00 18.25 ? 5   SER B C   1 
ATOM   1540 O  O   . SER B 1 17  ? 0.395   16.363  43.966  1.00 16.96 ? 5   SER B O   1 
ATOM   1541 C  CB  . SER B 1 17  ? 1.339   13.529  43.059  1.00 14.34 ? 5   SER B CB  1 
ATOM   1542 O  OG  . SER B 1 17  ? 2.023   12.730  42.131  1.00 16.06 ? 5   SER B OG  1 
ATOM   1543 N  N   . GLU B 1 18  ? -1.462  15.115  43.644  1.00 14.05 ? 6   GLU B N   1 
ATOM   1544 C  CA  . GLU B 1 18  ? -2.314  15.881  44.542  1.00 13.48 ? 6   GLU B CA  1 
ATOM   1545 C  C   . GLU B 1 18  ? -3.496  15.004  44.916  1.00 15.52 ? 6   GLU B C   1 
ATOM   1546 O  O   . GLU B 1 18  ? -3.948  14.191  44.105  1.00 14.58 ? 6   GLU B O   1 
ATOM   1547 C  CB  . GLU B 1 18  ? -2.777  17.169  43.853  1.00 17.59 ? 6   GLU B CB  1 
ATOM   1548 C  CG  . GLU B 1 18  ? -3.630  18.104  44.668  1.00 24.61 ? 6   GLU B CG  1 
ATOM   1549 C  CD  . GLU B 1 18  ? -4.061  19.308  43.849  1.00 26.96 ? 6   GLU B CD  1 
ATOM   1550 O  OE1 . GLU B 1 18  ? -5.276  19.477  43.615  1.00 24.51 ? 6   GLU B OE1 1 
ATOM   1551 O  OE2 . GLU B 1 18  ? -3.173  20.072  43.411  1.00 29.47 ? 6   GLU B OE2 1 
ATOM   1552 N  N   . THR B 1 19  ? -3.991  15.186  46.137  1.00 12.21 ? 7   THR B N   1 
ATOM   1553 C  CA  . THR B 1 19  ? -5.213  14.541  46.592  1.00 10.27 ? 7   THR B CA  1 
ATOM   1554 C  C   . THR B 1 19  ? -6.074  15.586  47.272  1.00 14.53 ? 7   THR B C   1 
ATOM   1555 O  O   . THR B 1 19  ? -5.574  16.607  47.755  1.00 16.62 ? 7   THR B O   1 
ATOM   1556 C  CB  . THR B 1 19  ? -4.956  13.382  47.579  1.00 17.90 ? 7   THR B CB  1 
ATOM   1557 O  OG1 . THR B 1 19  ? -4.313  13.875  48.766  1.00 22.21 ? 7   THR B OG1 1 
ATOM   1558 C  CG2 . THR B 1 19  ? -4.073  12.343  46.960  1.00 19.58 ? 7   THR B CG2 1 
ATOM   1559 N  N   . GLY B 1 20  ? -7.368  15.322  47.320  1.00 13.09 ? 8   GLY B N   1 
ATOM   1560 C  CA  . GLY B 1 20  ? -8.251  16.230  48.019  1.00 15.03 ? 8   GLY B CA  1 
ATOM   1561 C  C   . GLY B 1 20  ? -9.702  15.836  47.891  1.00 12.76 ? 8   GLY B C   1 
ATOM   1562 O  O   . GLY B 1 20  ? -10.039 14.680  47.624  1.00 12.75 ? 8   GLY B O   1 
ATOM   1563 N  N   . THR B 1 21  ? -10.556 16.816  48.150  1.00 11.80 ? 9   THR B N   1 
ATOM   1564 C  CA  . THR B 1 21  ? -11.991 16.714  47.953  1.00 10.83 ? 9   THR B CA  1 
ATOM   1565 C  C   . THR B 1 21  ? -12.374 17.640  46.820  1.00 10.33 ? 9   THR B C   1 
ATOM   1566 O  O   . THR B 1 21  ? -11.872 18.765  46.733  1.00 9.54  ? 9   THR B O   1 
ATOM   1567 C  CB  . THR B 1 21  ? -12.750 17.115  49.219  1.00 11.89 ? 9   THR B CB  1 
ATOM   1568 O  OG1 . THR B 1 21  ? -12.267 16.334  50.315  1.00 13.41 ? 9   THR B OG1 1 
ATOM   1569 C  CG2 . THR B 1 21  ? -14.244 16.886  49.056  1.00 12.15 ? 9   THR B CG2 1 
ATOM   1570 N  N   . ASN B 1 22  ? -13.264 17.169  45.953  1.00 9.28  ? 10  ASN B N   1 
ATOM   1571 C  CA  . ASN B 1 22  ? -13.796 18.011  44.890  1.00 10.87 ? 10  ASN B CA  1 
ATOM   1572 C  C   . ASN B 1 22  ? -15.259 17.652  44.704  1.00 9.85  ? 10  ASN B C   1 
ATOM   1573 O  O   . ASN B 1 22  ? -15.574 16.532  44.299  1.00 11.66 ? 10  ASN B O   1 
ATOM   1574 C  CB  . ASN B 1 22  ? -13.030 17.834  43.576  1.00 11.87 ? 10  ASN B CB  1 
ATOM   1575 C  CG  . ASN B 1 22  ? -13.575 18.734  42.482  1.00 12.14 ? 10  ASN B CG  1 
ATOM   1576 O  OD1 . ASN B 1 22  ? -14.310 18.287  41.592  1.00 12.12 ? 10  ASN B OD1 1 
ATOM   1577 N  ND2 . ASN B 1 22  ? -13.236 20.024  42.555  1.00 11.34 ? 10  ASN B ND2 1 
ATOM   1578 N  N   . ASN B 1 23  ? -16.147 18.593  45.028  1.00 10.13 ? 11  ASN B N   1 
ATOM   1579 C  CA  . ASN B 1 23  ? -17.573 18.436  44.765  1.00 10.91 ? 11  ASN B CA  1 
ATOM   1580 C  C   . ASN B 1 23  ? -18.128 17.182  45.431  1.00 15.47 ? 11  ASN B C   1 
ATOM   1581 O  O   . ASN B 1 23  ? -18.914 16.436  44.846  1.00 14.29 ? 11  ASN B O   1 
ATOM   1582 C  CB  . ASN B 1 23  ? -17.834 18.441  43.260  1.00 13.01 ? 11  ASN B CB  1 
ATOM   1583 C  CG  . ASN B 1 23  ? -17.518 19.778  42.633  1.00 15.80 ? 11  ASN B CG  1 
ATOM   1584 O  OD1 . ASN B 1 23  ? -17.841 20.829  43.200  1.00 18.45 ? 11  ASN B OD1 1 
ATOM   1585 N  ND2 . ASN B 1 23  ? -16.876 19.759  41.467  1.00 15.32 ? 11  ASN B ND2 1 
ATOM   1586 N  N   . GLY B 1 24  ? -17.699 16.941  46.668  1.00 13.25 ? 12  GLY B N   1 
ATOM   1587 C  CA  . GLY B 1 24  ? -18.189 15.829  47.447  1.00 16.12 ? 12  GLY B CA  1 
ATOM   1588 C  C   . GLY B 1 24  ? -17.535 14.499  47.166  1.00 13.69 ? 12  GLY B C   1 
ATOM   1589 O  O   . GLY B 1 24  ? -17.956 13.488  47.745  1.00 17.27 ? 12  GLY B O   1 
ATOM   1590 N  N   . TYR B 1 25  ? -16.537 14.454  46.295  1.00 11.48 ? 13  TYR B N   1 
ATOM   1591 C  CA  . TYR B 1 25  ? -15.834 13.221  45.982  1.00 10.88 ? 13  TYR B CA  1 
ATOM   1592 C  C   . TYR B 1 25  ? -14.391 13.327  46.435  1.00 10.26 ? 13  TYR B C   1 
ATOM   1593 O  O   . TYR B 1 25  ? -13.767 14.378  46.290  1.00 11.75 ? 13  TYR B O   1 
ATOM   1594 C  CB  . TYR B 1 25  ? -15.883 12.918  44.481  1.00 11.19 ? 13  TYR B CB  1 
ATOM   1595 C  CG  . TYR B 1 25  ? -17.237 12.400  44.088  1.00 11.73 ? 13  TYR B CG  1 
ATOM   1596 C  CD1 . TYR B 1 25  ? -18.271 13.277  43.793  1.00 12.35 ? 13  TYR B CD1 1 
ATOM   1597 C  CD2 . TYR B 1 25  ? -17.499 11.041  44.088  1.00 12.33 ? 13  TYR B CD2 1 
ATOM   1598 C  CE1 . TYR B 1 25  ? -19.522 12.807  43.472  1.00 14.51 ? 13  TYR B CE1 1 
ATOM   1599 C  CE2 . TYR B 1 25  ? -18.744 10.563  43.768  1.00 15.05 ? 13  TYR B CE2 1 
ATOM   1600 C  CZ  . TYR B 1 25  ? -19.753 11.452  43.463  1.00 18.91 ? 13  TYR B CZ  1 
ATOM   1601 O  OH  . TYR B 1 25  ? -21.001 10.974  43.145  1.00 20.02 ? 13  TYR B OH  1 
ATOM   1602 N  N   . TYR B 1 26  ? -13.870 12.244  47.003  1.00 8.44  ? 14  TYR B N   1 
ATOM   1603 C  CA  . TYR B 1 26  ? -12.424 12.113  47.130  1.00 7.56  ? 14  TYR B CA  1 
ATOM   1604 C  C   . TYR B 1 26  ? -11.803 12.047  45.738  1.00 10.03 ? 14  TYR B C   1 
ATOM   1605 O  O   . TYR B 1 26  ? -12.350 11.405  44.836  1.00 10.07 ? 14  TYR B O   1 
ATOM   1606 C  CB  . TYR B 1 26  ? -12.072 10.847  47.933  1.00 7.77  ? 14  TYR B CB  1 
ATOM   1607 C  CG  . TYR B 1 26  ? -10.583 10.559  47.976  1.00 10.21 ? 14  TYR B CG  1 
ATOM   1608 C  CD1 . TYR B 1 26  ? -9.760  11.162  48.927  1.00 11.05 ? 14  TYR B CD1 1 
ATOM   1609 C  CD2 . TYR B 1 26  ? -9.996  9.706   47.050  1.00 11.32 ? 14  TYR B CD2 1 
ATOM   1610 C  CE1 . TYR B 1 26  ? -8.390  10.903  48.954  1.00 12.87 ? 14  TYR B CE1 1 
ATOM   1611 C  CE2 . TYR B 1 26  ? -8.643  9.460   47.061  1.00 12.38 ? 14  TYR B CE2 1 
ATOM   1612 C  CZ  . TYR B 1 26  ? -7.846  10.051  48.013  1.00 12.77 ? 14  TYR B CZ  1 
ATOM   1613 O  OH  . TYR B 1 26  ? -6.496  9.794   48.010  1.00 14.52 ? 14  TYR B OH  1 
ATOM   1614 N  N   . TYR B 1 27  ? -10.656 12.714  45.545  1.00 10.13 ? 15  TYR B N   1 
ATOM   1615 C  CA  . TYR B 1 27  ? -9.873  12.487  44.330  1.00 9.63  ? 15  TYR B CA  1 
ATOM   1616 C  C   . TYR B 1 27  ? -8.406  12.273  44.675  1.00 10.37 ? 15  TYR B C   1 
ATOM   1617 O  O   . TYR B 1 27  ? -7.887  12.810  45.662  1.00 10.41 ? 15  TYR B O   1 
ATOM   1618 C  CB  . TYR B 1 27  ? -10.011 13.641  43.279  1.00 6.90  ? 15  TYR B CB  1 
ATOM   1619 C  CG  . TYR B 1 27  ? -9.292  14.927  43.638  1.00 9.74  ? 15  TYR B CG  1 
ATOM   1620 C  CD1 . TYR B 1 27  ? -9.916  15.899  44.423  1.00 11.71 ? 15  TYR B CD1 1 
ATOM   1621 C  CD2 . TYR B 1 27  ? -8.007  15.180  43.171  1.00 11.18 ? 15  TYR B CD2 1 
ATOM   1622 C  CE1 . TYR B 1 27  ? -9.270  17.069  44.757  1.00 12.50 ? 15  TYR B CE1 1 
ATOM   1623 C  CE2 . TYR B 1 27  ? -7.343  16.357  43.506  1.00 12.52 ? 15  TYR B CE2 1 
ATOM   1624 C  CZ  . TYR B 1 27  ? -7.985  17.298  44.295  1.00 14.61 ? 15  TYR B CZ  1 
ATOM   1625 O  OH  . TYR B 1 27  ? -7.344  18.480  44.622  1.00 15.53 ? 15  TYR B OH  1 
ATOM   1626 N  N   . SER B 1 28  ? -7.747  11.441  43.864  1.00 8.45  ? 16  SER B N   1 
ATOM   1627 C  CA  . SER B 1 28  ? -6.303  11.254  43.939  1.00 10.22 ? 16  SER B CA  1 
ATOM   1628 C  C   . SER B 1 28  ? -5.741  11.323  42.530  1.00 10.56 ? 16  SER B C   1 
ATOM   1629 O  O   . SER B 1 28  ? -6.247  10.657  41.622  1.00 9.87  ? 16  SER B O   1 
ATOM   1630 C  CB  . SER B 1 28  ? -5.935  9.914   44.601  1.00 13.00 ? 16  SER B CB  1 
ATOM   1631 O  OG  . SER B 1 28  ? -4.524  9.681   44.563  1.00 13.37 ? 16  SER B OG  1 
ATOM   1632 N  N   . PHE B 1 29  ? -4.728  12.160  42.341  1.00 8.87  ? 17  PHE B N   1 
ATOM   1633 C  CA  . PHE B 1 29  ? -3.935  12.185  41.124  1.00 8.80  ? 17  PHE B CA  1 
ATOM   1634 C  C   . PHE B 1 29  ? -2.501  11.881  41.523  1.00 10.38 ? 17  PHE B C   1 
ATOM   1635 O  O   . PHE B 1 29  ? -1.913  12.617  42.324  1.00 12.78 ? 17  PHE B O   1 
ATOM   1636 C  CB  . PHE B 1 29  ? -4.011  13.548  40.435  1.00 12.57 ? 17  PHE B CB  1 
ATOM   1637 C  CG  . PHE B 1 29  ? -3.102  13.673  39.249  1.00 12.29 ? 17  PHE B CG  1 
ATOM   1638 C  CD1 . PHE B 1 29  ? -3.209  12.783  38.180  1.00 13.16 ? 17  PHE B CD1 1 
ATOM   1639 C  CD2 . PHE B 1 29  ? -2.134  14.672  39.191  1.00 14.14 ? 17  PHE B CD2 1 
ATOM   1640 C  CE1 . PHE B 1 29  ? -2.364  12.886  37.085  1.00 13.47 ? 17  PHE B CE1 1 
ATOM   1641 C  CE2 . PHE B 1 29  ? -1.284  14.786  38.090  1.00 14.71 ? 17  PHE B CE2 1 
ATOM   1642 C  CZ  . PHE B 1 29  ? -1.398  13.903  37.036  1.00 12.73 ? 17  PHE B CZ  1 
ATOM   1643 N  N   . TRP B 1 30  ? -1.953  10.787  41.004  1.00 8.86  ? 18  TRP B N   1 
ATOM   1644 C  CA  . TRP B 1 30  ? -0.568  10.428  41.296  1.00 11.56 ? 18  TRP B CA  1 
ATOM   1645 C  C   . TRP B 1 30  ? 0.176   10.233  39.988  1.00 12.79 ? 18  TRP B C   1 
ATOM   1646 O  O   . TRP B 1 30  ? -0.279  9.482   39.118  1.00 10.78 ? 18  TRP B O   1 
ATOM   1647 C  CB  . TRP B 1 30  ? -0.462  9.157   42.137  1.00 11.96 ? 18  TRP B CB  1 
ATOM   1648 C  CG  . TRP B 1 30  ? 0.985   8.793   42.417  1.00 13.30 ? 18  TRP B CG  1 
ATOM   1649 C  CD1 . TRP B 1 30  ? 1.789   9.314   43.388  1.00 18.12 ? 18  TRP B CD1 1 
ATOM   1650 C  CD2 . TRP B 1 30  ? 1.802   7.891   41.661  1.00 17.04 ? 18  TRP B CD2 1 
ATOM   1651 N  NE1 . TRP B 1 30  ? 3.053   8.764   43.307  1.00 18.01 ? 18  TRP B NE1 1 
ATOM   1652 C  CE2 . TRP B 1 30  ? 3.083   7.886   42.255  1.00 18.97 ? 18  TRP B CE2 1 
ATOM   1653 C  CE3 . TRP B 1 30  ? 1.566   7.068   40.557  1.00 15.57 ? 18  TRP B CE3 1 
ATOM   1654 C  CZ2 . TRP B 1 30  ? 4.128   7.098   41.771  1.00 20.61 ? 18  TRP B CZ2 1 
ATOM   1655 C  CZ3 . TRP B 1 30  ? 2.602   6.285   40.073  1.00 18.74 ? 18  TRP B CZ3 1 
ATOM   1656 C  CH2 . TRP B 1 30  ? 3.872   6.310   40.680  1.00 20.06 ? 18  TRP B CH2 1 
ATOM   1657 N  N   . THR B 1 31  ? 1.323   10.894  39.851  1.00 11.88 ? 19  THR B N   1 
ATOM   1658 C  CA  . THR B 1 31  ? 2.154   10.675  38.683  1.00 9.78  ? 19  THR B CA  1 
ATOM   1659 C  C   . THR B 1 31  ? 3.605   10.633  39.137  1.00 15.83 ? 19  THR B C   1 
ATOM   1660 O  O   . THR B 1 31  ? 3.986   11.322  40.086  1.00 14.58 ? 19  THR B O   1 
ATOM   1661 C  CB  . THR B 1 31  ? 1.941   11.763  37.613  1.00 12.73 ? 19  THR B CB  1 
ATOM   1662 O  OG1 . THR B 1 31  ? 2.833   11.542  36.514  1.00 16.40 ? 19  THR B OG1 1 
ATOM   1663 C  CG2 . THR B 1 31  ? 2.175   13.168  38.174  1.00 16.75 ? 19  THR B CG2 1 
ATOM   1664 N  N   . ASP B 1 32  ? 4.404   9.797   38.478  1.00 15.43 ? 20  ASP B N   1 
ATOM   1665 C  CA  . ASP B 1 32  ? 5.835   9.805   38.770  1.00 16.88 ? 20  ASP B CA  1 
ATOM   1666 C  C   . ASP B 1 32  ? 6.553   10.956  38.076  1.00 20.27 ? 20  ASP B C   1 
ATOM   1667 O  O   . ASP B 1 32  ? 7.776   11.076  38.203  1.00 20.19 ? 20  ASP B O   1 
ATOM   1668 C  CB  . ASP B 1 32  ? 6.482   8.460   38.399  1.00 15.61 ? 20  ASP B CB  1 
ATOM   1669 C  CG  . ASP B 1 32  ? 6.491   8.181   36.894  1.00 18.80 ? 20  ASP B CG  1 
ATOM   1670 O  OD1 . ASP B 1 32  ? 6.145   9.070   36.094  1.00 18.10 ? 20  ASP B OD1 1 
ATOM   1671 O  OD2 . ASP B 1 32  ? 6.849   7.042   36.511  1.00 21.09 ? 20  ASP B OD2 1 
ATOM   1672 N  N   . GLY B 1 33  ? 5.822   11.799  37.354  1.00 13.94 ? 21  GLY B N   1 
ATOM   1673 C  CA  . GLY B 1 33  ? 6.384   12.973  36.727  1.00 19.68 ? 21  GLY B CA  1 
ATOM   1674 C  C   . GLY B 1 33  ? 6.854   12.799  35.297  1.00 20.97 ? 21  GLY B C   1 
ATOM   1675 O  O   . GLY B 1 33  ? 7.280   13.785  34.678  1.00 26.12 ? 21  GLY B O   1 
ATOM   1676 N  N   . GLY B 1 34  ? 6.792   11.591  34.745  1.00 18.09 ? 22  GLY B N   1 
ATOM   1677 C  CA  . GLY B 1 34  ? 7.227   11.389  33.374  1.00 16.85 ? 22  GLY B CA  1 
ATOM   1678 C  C   . GLY B 1 34  ? 6.224   11.914  32.365  1.00 19.55 ? 22  GLY B C   1 
ATOM   1679 O  O   . GLY B 1 34  ? 5.014   11.884  32.583  1.00 18.50 ? 22  GLY B O   1 
ATOM   1680 N  N   . GLY B 1 35  ? 6.749   12.417  31.244  1.00 16.58 ? 23  GLY B N   1 
ATOM   1681 C  CA  . GLY B 1 35  ? 5.951   12.953  30.144  1.00 15.35 ? 23  GLY B CA  1 
ATOM   1682 C  C   . GLY B 1 35  ? 5.034   14.072  30.598  1.00 21.96 ? 23  GLY B C   1 
ATOM   1683 O  O   . GLY B 1 35  ? 5.343   14.847  31.511  1.00 18.42 ? 23  GLY B O   1 
ATOM   1684 N  N   . GLN B 1 36  ? 3.873   14.157  29.959  1.00 16.51 ? 24  GLN B N   1 
ATOM   1685 C  CA  . GLN B 1 36  ? 2.866   15.142  30.323  1.00 18.63 ? 24  GLN B CA  1 
ATOM   1686 C  C   . GLN B 1 36  ? 1.595   14.400  30.698  1.00 18.81 ? 24  GLN B C   1 
ATOM   1687 O  O   . GLN B 1 36  ? 1.079   13.611  29.905  1.00 16.03 ? 24  GLN B O   1 
ATOM   1688 C  CB  . GLN B 1 36  ? 2.603   16.136  29.187  1.00 19.24 ? 24  GLN B CB  1 
ATOM   1689 C  CG  . GLN B 1 36  ? 3.853   16.888  28.739  1.00 33.55 ? 24  GLN B CG  1 
ATOM   1690 C  CD  . GLN B 1 36  ? 3.588   18.337  28.355  1.00 41.23 ? 24  GLN B CD  1 
ATOM   1691 O  OE1 . GLN B 1 36  ? 4.005   19.265  29.063  1.00 49.38 ? 24  GLN B OE1 1 
ATOM   1692 N  NE2 . GLN B 1 36  ? 2.919   18.540  27.221  1.00 37.02 ? 24  GLN B NE2 1 
ATOM   1693 N  N   . VAL B 1 37  ? 1.120   14.628  31.917  1.00 18.18 ? 25  VAL B N   1 
ATOM   1694 C  CA  . VAL B 1 37  ? -0.149  14.092  32.397  1.00 16.75 ? 25  VAL B CA  1 
ATOM   1695 C  C   . VAL B 1 37  ? -0.917  15.256  32.998  1.00 15.34 ? 25  VAL B C   1 
ATOM   1696 O  O   . VAL B 1 37  ? -0.419  15.907  33.925  1.00 13.80 ? 25  VAL B O   1 
ATOM   1697 C  CB  . VAL B 1 37  ? 0.047   12.987  33.449  1.00 14.60 ? 25  VAL B CB  1 
ATOM   1698 C  CG1 . VAL B 1 37  ? -1.293  12.342  33.806  1.00 13.32 ? 25  VAL B CG1 1 
ATOM   1699 C  CG2 . VAL B 1 37  ? 1.078   11.956  32.998  1.00 16.16 ? 25  VAL B CG2 1 
ATOM   1700 N  N   . THR B 1 38  ? -2.121  15.517  32.486  1.00 12.20 ? 26  THR B N   1 
ATOM   1701 C  CA  . THR B 1 38  ? -2.921  16.653  32.930  1.00 15.30 ? 26  THR B CA  1 
ATOM   1702 C  C   . THR B 1 38  ? -4.264  16.148  33.438  1.00 11.44 ? 26  THR B C   1 
ATOM   1703 O  O   . THR B 1 38  ? -5.018  15.518  32.690  1.00 12.79 ? 26  THR B O   1 
ATOM   1704 C  CB  . THR B 1 38  ? -3.113  17.670  31.803  1.00 18.08 ? 26  THR B CB  1 
ATOM   1705 O  OG1 . THR B 1 38  ? -1.829  18.108  31.331  1.00 19.82 ? 26  THR B OG1 1 
ATOM   1706 C  CG2 . THR B 1 38  ? -3.888  18.878  32.305  1.00 21.43 ? 26  THR B CG2 1 
ATOM   1707 N  N   . TYR B 1 39  ? -4.556  16.436  34.700  1.00 10.38 ? 27  TYR B N   1 
ATOM   1708 C  CA  . TYR B 1 39  ? -5.760  15.972  35.373  1.00 11.29 ? 27  TYR B CA  1 
ATOM   1709 C  C   . TYR B 1 39  ? -6.665  17.165  35.645  1.00 11.14 ? 27  TYR B C   1 
ATOM   1710 O  O   . TYR B 1 39  ? -6.191  18.224  36.064  1.00 12.11 ? 27  TYR B O   1 
ATOM   1711 C  CB  . TYR B 1 39  ? -5.389  15.251  36.680  1.00 9.27  ? 27  TYR B CB  1 
ATOM   1712 C  CG  . TYR B 1 39  ? -6.560  14.856  37.544  1.00 12.61 ? 27  TYR B CG  1 
ATOM   1713 C  CD1 . TYR B 1 39  ? -7.077  15.734  38.503  1.00 10.29 ? 27  TYR B CD1 1 
ATOM   1714 C  CD2 . TYR B 1 39  ? -7.161  13.618  37.399  1.00 9.40  ? 27  TYR B CD2 1 
ATOM   1715 C  CE1 . TYR B 1 39  ? -8.147  15.380  39.287  1.00 9.96  ? 27  TYR B CE1 1 
ATOM   1716 C  CE2 . TYR B 1 39  ? -8.225  13.249  38.195  1.00 12.50 ? 27  TYR B CE2 1 
ATOM   1717 C  CZ  . TYR B 1 39  ? -8.720  14.140  39.130  1.00 9.72  ? 27  TYR B CZ  1 
ATOM   1718 O  OH  . TYR B 1 39  ? -9.779  13.771  39.904  1.00 11.18 ? 27  TYR B OH  1 
ATOM   1719 N  N   . THR B 1 40  ? -7.966  16.998  35.390  1.00 10.41 ? 28  THR B N   1 
ATOM   1720 C  CA  . THR B 1 40  ? -8.943  18.063  35.608  1.00 13.32 ? 28  THR B CA  1 
ATOM   1721 C  C   . THR B 1 40  ? -10.126 17.518  36.396  1.00 14.72 ? 28  THR B C   1 
ATOM   1722 O  O   . THR B 1 40  ? -10.719 16.511  36.006  1.00 14.24 ? 28  THR B O   1 
ATOM   1723 C  CB  . THR B 1 40  ? -9.420  18.646  34.273  1.00 17.06 ? 28  THR B CB  1 
ATOM   1724 O  OG1 . THR B 1 40  ? -8.292  19.112  33.520  1.00 21.41 ? 28  THR B OG1 1 
ATOM   1725 C  CG2 . THR B 1 40  ? -10.380 19.809  34.500  1.00 23.88 ? 28  THR B CG2 1 
ATOM   1726 N  N   . ASN B 1 41  ? -10.478 18.182  37.495  1.00 11.38 ? 29  ASN B N   1 
ATOM   1727 C  CA  . ASN B 1 41  ? -11.719 17.857  38.182  1.00 11.05 ? 29  ASN B CA  1 
ATOM   1728 C  C   . ASN B 1 41  ? -12.875 18.571  37.504  1.00 15.03 ? 29  ASN B C   1 
ATOM   1729 O  O   . ASN B 1 41  ? -12.775 19.761  37.194  1.00 16.44 ? 29  ASN B O   1 
ATOM   1730 C  CB  . ASN B 1 41  ? -11.651 18.277  39.650  1.00 12.34 ? 29  ASN B CB  1 
ATOM   1731 C  CG  . ASN B 1 41  ? -10.912 17.286  40.503  1.00 12.79 ? 29  ASN B CG  1 
ATOM   1732 O  OD1 . ASN B 1 41  ? -11.069 16.074  40.345  1.00 11.87 ? 29  ASN B OD1 1 
ATOM   1733 N  ND2 . ASN B 1 41  ? -10.098 17.795  41.426  1.00 11.29 ? 29  ASN B ND2 1 
ATOM   1734 N  N   . GLY B 1 42  ? -13.967 17.845  37.278  1.00 12.84 ? 30  GLY B N   1 
ATOM   1735 C  CA  . GLY B 1 42  ? -15.190 18.433  36.790  1.00 15.42 ? 30  GLY B CA  1 
ATOM   1736 C  C   . GLY B 1 42  ? -16.295 18.386  37.827  1.00 16.50 ? 30  GLY B C   1 
ATOM   1737 O  O   . GLY B 1 42  ? -16.086 18.022  38.991  1.00 14.88 ? 30  GLY B O   1 
ATOM   1738 N  N   . PRO B 1 43  ? -17.511 18.743  37.413  1.00 16.39 ? 31  PRO B N   1 
ATOM   1739 C  CA  . PRO B 1 43  ? -18.634 18.764  38.359  1.00 14.87 ? 31  PRO B CA  1 
ATOM   1740 C  C   . PRO B 1 43  ? -18.957 17.382  38.912  1.00 17.50 ? 31  PRO B C   1 
ATOM   1741 O  O   . PRO B 1 43  ? -18.781 16.359  38.241  1.00 14.33 ? 31  PRO B O   1 
ATOM   1742 C  CB  . PRO B 1 43  ? -19.801 19.296  37.515  1.00 22.18 ? 31  PRO B CB  1 
ATOM   1743 C  CG  . PRO B 1 43  ? -19.172 19.917  36.303  1.00 23.14 ? 31  PRO B CG  1 
ATOM   1744 C  CD  . PRO B 1 43  ? -17.894 19.185  36.060  1.00 18.67 ? 31  PRO B CD  1 
ATOM   1745 N  N   . ALA B 1 44  ? -19.472 17.366  40.144  1.00 15.32 ? 32  ALA B N   1 
ATOM   1746 C  CA  . ALA B 1 44  ? -19.986 16.144  40.790  1.00 13.50 ? 32  ALA B CA  1 
ATOM   1747 C  C   . ALA B 1 44  ? -18.877 15.092  40.724  1.00 14.04 ? 32  ALA B C   1 
ATOM   1748 O  O   . ALA B 1 44  ? -17.738 15.396  41.096  1.00 13.76 ? 32  ALA B O   1 
ATOM   1749 C  CB  . ALA B 1 44  ? -21.310 15.744  40.155  1.00 14.62 ? 32  ALA B CB  1 
ATOM   1750 N  N   . GLY B 1 45  ? -19.143 13.881  40.241  1.00 13.35 ? 33  GLY B N   1 
ATOM   1751 C  CA  . GLY B 1 45  ? -18.108 12.860  40.257  1.00 13.10 ? 33  GLY B CA  1 
ATOM   1752 C  C   . GLY B 1 45  ? -17.281 12.764  38.988  1.00 10.99 ? 33  GLY B C   1 
ATOM   1753 O  O   . GLY B 1 45  ? -16.695 11.710  38.709  1.00 10.85 ? 33  GLY B O   1 
ATOM   1754 N  N   . GLN B 1 46  ? -17.204 13.850  38.214  1.00 11.46 ? 34  GLN B N   1 
ATOM   1755 C  CA  . GLN B 1 46  ? -16.484 13.830  36.941  1.00 12.30 ? 34  GLN B CA  1 
ATOM   1756 C  C   . GLN B 1 46  ? -15.004 14.178  37.101  1.00 10.96 ? 34  GLN B C   1 
ATOM   1757 O  O   . GLN B 1 46  ? -14.629 15.040  37.899  1.00 10.69 ? 34  GLN B O   1 
ATOM   1758 C  CB  . GLN B 1 46  ? -17.128 14.798  35.940  1.00 14.19 ? 34  GLN B CB  1 
ATOM   1759 C  CG  . GLN B 1 46  ? -16.754 14.505  34.481  1.00 14.30 ? 34  GLN B CG  1 
ATOM   1760 C  CD  . GLN B 1 46  ? -15.524 15.262  34.006  1.00 20.20 ? 34  GLN B CD  1 
ATOM   1761 O  OE1 . GLN B 1 46  ? -14.934 16.053  34.748  1.00 22.85 ? 34  GLN B OE1 1 
ATOM   1762 N  NE2 . GLN B 1 46  ? -15.130 15.025  32.754  1.00 25.74 ? 34  GLN B NE2 1 
ATOM   1763 N  N   . TYR B 1 47  ? -14.159 13.492  36.334  1.00 9.83  ? 35  TYR B N   1 
ATOM   1764 C  CA  . TYR B 1 47  ? -12.779 13.920  36.173  1.00 8.28  ? 35  TYR B CA  1 
ATOM   1765 C  C   . TYR B 1 47  ? -12.336 13.580  34.761  1.00 12.32 ? 35  TYR B C   1 
ATOM   1766 O  O   . TYR B 1 47  ? -12.921 12.728  34.091  1.00 10.46 ? 35  TYR B O   1 
ATOM   1767 C  CB  . TYR B 1 47  ? -11.835 13.257  37.198  1.00 8.02  ? 35  TYR B CB  1 
ATOM   1768 C  CG  . TYR B 1 47  ? -11.579 11.772  36.961  1.00 9.87  ? 35  TYR B CG  1 
ATOM   1769 C  CD1 . TYR B 1 47  ? -12.424 10.803  37.497  1.00 8.88  ? 35  TYR B CD1 1 
ATOM   1770 C  CD2 . TYR B 1 47  ? -10.480 11.342  36.209  1.00 8.25  ? 35  TYR B CD2 1 
ATOM   1771 C  CE1 . TYR B 1 47  ? -12.186 9.434   37.299  1.00 8.13  ? 35  TYR B CE1 1 
ATOM   1772 C  CE2 . TYR B 1 47  ? -10.235 9.980   36.001  1.00 7.87  ? 35  TYR B CE2 1 
ATOM   1773 C  CZ  . TYR B 1 47  ? -11.093 9.039   36.551  1.00 8.88  ? 35  TYR B CZ  1 
ATOM   1774 O  OH  . TYR B 1 47  ? -10.863 7.696   36.365  1.00 9.30  ? 35  TYR B OH  1 
ATOM   1775 N  N   . SER B 1 48  ? -11.296 14.259  34.305  1.00 10.58 ? 36  SER B N   1 
ATOM   1776 C  CA  . SER B 1 48  ? -10.709 13.896  33.029  1.00 11.72 ? 36  SER B CA  1 
ATOM   1777 C  C   . SER B 1 48  ? -9.200  13.884  33.177  1.00 12.11 ? 36  SER B C   1 
ATOM   1778 O  O   . SER B 1 48  ? -8.637  14.507  34.078  1.00 12.22 ? 36  SER B O   1 
ATOM   1779 C  CB  . SER B 1 48  ? -11.151 14.848  31.904  1.00 19.94 ? 36  SER B CB  1 
ATOM   1780 O  OG  . SER B 1 48  ? -10.609 16.135  32.081  1.00 26.94 ? 36  SER B OG  1 
ATOM   1781 N  N   . VAL B 1 49  ? -8.544  13.130  32.305  1.00 11.42 ? 37  VAL B N   1 
ATOM   1782 C  CA  . VAL B 1 49  ? -7.091  13.103  32.284  1.00 10.75 ? 37  VAL B CA  1 
ATOM   1783 C  C   . VAL B 1 49  ? -6.654  12.985  30.834  1.00 13.84 ? 37  VAL B C   1 
ATOM   1784 O  O   . VAL B 1 49  ? -7.299  12.305  30.026  1.00 13.91 ? 37  VAL B O   1 
ATOM   1785 C  CB  . VAL B 1 49  ? -6.523  11.976  33.188  1.00 15.48 ? 37  VAL B CB  1 
ATOM   1786 C  CG1 . VAL B 1 49  ? -7.126  10.618  32.870  1.00 15.67 ? 37  VAL B CG1 1 
ATOM   1787 C  CG2 . VAL B 1 49  ? -4.990  11.950  33.155  1.00 14.91 ? 37  VAL B CG2 1 
ATOM   1788 N  N   . GLU B 1 50  ? -5.617  13.737  30.481  1.00 12.56 ? 38  GLU B N   1 
ATOM   1789 C  CA  . GLU B 1 50  ? -5.043  13.726  29.143  1.00 16.52 ? 38  GLU B CA  1 
ATOM   1790 C  C   . GLU B 1 50  ? -3.565  13.471  29.339  1.00 15.98 ? 38  GLU B C   1 
ATOM   1791 O  O   . GLU B 1 50  ? -2.944  14.134  30.171  1.00 15.47 ? 38  GLU B O   1 
ATOM   1792 C  CB  . GLU B 1 50  ? -5.238  15.067  28.413  1.00 19.70 ? 38  GLU B CB  1 
ATOM   1793 C  CG  . GLU B 1 50  ? -6.675  15.530  28.245  1.00 28.88 ? 38  GLU B CG  1 
ATOM   1794 C  CD  . GLU B 1 50  ? -7.161  15.401  26.812  1.00 37.98 ? 38  GLU B CD  1 
ATOM   1795 O  OE1 . GLU B 1 50  ? -6.329  15.116  25.917  1.00 40.96 ? 38  GLU B OE1 1 
ATOM   1796 O  OE2 . GLU B 1 50  ? -8.378  15.589  26.578  1.00 47.08 ? 38  GLU B OE2 1 
ATOM   1797 N  N   . TRP B 1 51  ? -2.991  12.521  28.602  1.00 11.45 ? 39  TRP B N   1 
ATOM   1798 C  CA  . TRP B 1 51  ? -1.579  12.261  28.824  1.00 12.88 ? 39  TRP B CA  1 
ATOM   1799 C  C   . TRP B 1 51  ? -0.858  11.990  27.516  1.00 13.04 ? 39  TRP B C   1 
ATOM   1800 O  O   . TRP B 1 51  ? -1.458  11.613  26.509  1.00 11.87 ? 39  TRP B O   1 
ATOM   1801 C  CB  . TRP B 1 51  ? -1.354  11.111  29.819  1.00 12.46 ? 39  TRP B CB  1 
ATOM   1802 C  CG  . TRP B 1 51  ? -1.795  9.717   29.402  1.00 11.98 ? 39  TRP B CG  1 
ATOM   1803 C  CD1 . TRP B 1 51  ? -0.973  8.696   28.980  1.00 10.95 ? 39  TRP B CD1 1 
ATOM   1804 C  CD2 . TRP B 1 51  ? -3.125  9.160   29.446  1.00 11.94 ? 39  TRP B CD2 1 
ATOM   1805 N  NE1 . TRP B 1 51  ? -1.708  7.563   28.743  1.00 11.60 ? 39  TRP B NE1 1 
ATOM   1806 C  CE2 . TRP B 1 51  ? -3.029  7.821   29.009  1.00 12.07 ? 39  TRP B CE2 1 
ATOM   1807 C  CE3 . TRP B 1 51  ? -4.383  9.669   29.800  1.00 11.73 ? 39  TRP B CE3 1 
ATOM   1808 C  CZ2 . TRP B 1 51  ? -4.131  6.980   28.928  1.00 9.79  ? 39  TRP B CZ2 1 
ATOM   1809 C  CZ3 . TRP B 1 51  ? -5.491  8.826   29.706  1.00 10.43 ? 39  TRP B CZ3 1 
ATOM   1810 C  CH2 . TRP B 1 51  ? -5.348  7.494   29.277  1.00 10.54 ? 39  TRP B CH2 1 
ATOM   1811 N  N   . SER B 1 52  ? 0.454   12.227  27.551  1.00 13.77 ? 40  SER B N   1 
ATOM   1812 C  CA  . SER B 1 52  ? 1.292   12.078  26.367  1.00 15.69 ? 40  SER B CA  1 
ATOM   1813 C  C   . SER B 1 52  ? 2.664   11.593  26.814  1.00 14.38 ? 40  SER B C   1 
ATOM   1814 O  O   . SER B 1 52  ? 3.326   12.255  27.622  1.00 16.02 ? 40  SER B O   1 
ATOM   1815 C  CB  . SER B 1 52  ? 1.385   13.401  25.604  1.00 18.49 ? 40  SER B CB  1 
ATOM   1816 O  OG  . SER B 1 52  ? 2.421   13.377  24.640  1.00 29.06 ? 40  SER B OG  1 
ATOM   1817 N  N   . ASN B 1 53  ? 3.067   10.423  26.316  1.00 12.72 ? 41  ASN B N   1 
ATOM   1818 C  CA  . ASN B 1 53  ? 4.372   9.823   26.615  1.00 14.64 ? 41  ASN B CA  1 
ATOM   1819 C  C   . ASN B 1 53  ? 4.644   9.807   28.116  1.00 14.76 ? 41  ASN B C   1 
ATOM   1820 O  O   . ASN B 1 53  ? 5.702   10.231  28.593  1.00 15.03 ? 41  ASN B O   1 
ATOM   1821 C  CB  . ASN B 1 53  ? 5.487   10.553  25.869  1.00 17.18 ? 41  ASN B CB  1 
ATOM   1822 C  CG  . ASN B 1 53  ? 5.333   10.452  24.380  1.00 14.16 ? 41  ASN B CG  1 
ATOM   1823 O  OD1 . ASN B 1 53  ? 5.254   9.351   23.831  1.00 14.87 ? 41  ASN B OD1 1 
ATOM   1824 N  ND2 . ASN B 1 53  ? 5.250   11.601  23.708  1.00 18.93 ? 41  ASN B ND2 1 
ATOM   1825 N  N   . SER B 1 54  ? 3.671   9.296   28.863  1.00 13.40 ? 42  SER B N   1 
ATOM   1826 C  CA  . SER B 1 54  ? 3.683   9.386   30.315  1.00 14.29 ? 42  SER B CA  1 
ATOM   1827 C  C   . SER B 1 54  ? 4.702   8.426   30.918  1.00 15.78 ? 42  SER B C   1 
ATOM   1828 O  O   . SER B 1 54  ? 5.134   7.459   30.288  1.00 15.04 ? 42  SER B O   1 
ATOM   1829 C  CB  . SER B 1 54  ? 2.298   9.058   30.871  1.00 13.69 ? 42  SER B CB  1 
ATOM   1830 O  OG  . SER B 1 54  ? 1.974   7.692   30.614  1.00 14.98 ? 42  SER B OG  1 
ATOM   1831 N  N   . GLY B 1 55  ? 5.083   8.704   32.166  1.00 12.64 ? 43  GLY B N   1 
ATOM   1832 C  CA  . GLY B 1 55  ? 5.595   7.664   33.034  1.00 15.48 ? 43  GLY B CA  1 
ATOM   1833 C  C   . GLY B 1 55  ? 4.425   6.908   33.639  1.00 18.53 ? 43  GLY B C   1 
ATOM   1834 O  O   . GLY B 1 55  ? 3.421   6.680   32.954  1.00 18.09 ? 43  GLY B O   1 
ATOM   1835 N  N   . ASN B 1 56  ? 4.521   6.541   34.915  1.00 14.81 ? 44  ASN B N   1 
ATOM   1836 C  CA  . ASN B 1 56  ? 3.429   5.885   35.636  1.00 14.67 ? 44  ASN B CA  1 
ATOM   1837 C  C   . ASN B 1 56  ? 2.483   6.940   36.193  1.00 14.30 ? 44  ASN B C   1 
ATOM   1838 O  O   . ASN B 1 56  ? 2.936   7.904   36.809  1.00 13.18 ? 44  ASN B O   1 
ATOM   1839 C  CB  . ASN B 1 56  ? 3.969   5.067   36.814  1.00 15.92 ? 44  ASN B CB  1 
ATOM   1840 C  CG  . ASN B 1 56  ? 4.424   3.684   36.424  1.00 28.30 ? 44  ASN B CG  1 
ATOM   1841 O  OD1 . ASN B 1 56  ? 5.589   3.329   36.616  1.00 30.28 ? 44  ASN B OD1 1 
ATOM   1842 N  ND2 . ASN B 1 56  ? 3.505   2.881   35.900  1.00 30.71 ? 44  ASN B ND2 1 
ATOM   1843 N  N   . PHE B 1 57  ? 1.174   6.746   36.016  1.00 10.24 ? 45  PHE B N   1 
ATOM   1844 C  CA  . PHE B 1 57  ? 0.229   7.582   36.750  1.00 10.75 ? 45  PHE B CA  1 
ATOM   1845 C  C   . PHE B 1 57  ? -1.017  6.776   37.061  1.00 10.68 ? 45  PHE B C   1 
ATOM   1846 O  O   . PHE B 1 57  ? -1.334  5.805   36.372  1.00 10.27 ? 45  PHE B O   1 
ATOM   1847 C  CB  . PHE B 1 57  ? -0.159  8.848   35.977  1.00 10.17 ? 45  PHE B CB  1 
ATOM   1848 C  CG  . PHE B 1 57  ? -1.127  8.598   34.846  1.00 10.38 ? 45  PHE B CG  1 
ATOM   1849 C  CD1 . PHE B 1 57  ? -2.503  8.653   35.061  1.00 11.46 ? 45  PHE B CD1 1 
ATOM   1850 C  CD2 . PHE B 1 57  ? -0.661  8.315   33.574  1.00 11.38 ? 45  PHE B CD2 1 
ATOM   1851 C  CE1 . PHE B 1 57  ? -3.401  8.410   34.030  1.00 11.01 ? 45  PHE B CE1 1 
ATOM   1852 C  CE2 . PHE B 1 57  ? -1.556  8.089   32.524  1.00 13.17 ? 45  PHE B CE2 1 
ATOM   1853 C  CZ  . PHE B 1 57  ? -2.922  8.133   32.755  1.00 10.18 ? 45  PHE B CZ  1 
ATOM   1854 N  N   . VAL B 1 58  ? -1.755  7.233   38.073  1.00 8.84  ? 46  VAL B N   1 
ATOM   1855 C  CA  . VAL B 1 58  ? -3.066  6.675   38.397  1.00 9.49  ? 46  VAL B CA  1 
ATOM   1856 C  C   . VAL B 1 58  ? -3.916  7.794   38.986  1.00 10.23 ? 46  VAL B C   1 
ATOM   1857 O  O   . VAL B 1 58  ? -3.460  8.534   39.864  1.00 11.29 ? 46  VAL B O   1 
ATOM   1858 C  CB  . VAL B 1 58  ? -2.955  5.470   39.357  1.00 15.24 ? 46  VAL B CB  1 
ATOM   1859 C  CG1 . VAL B 1 58  ? -2.152  5.814   40.577  1.00 22.09 ? 46  VAL B CG1 1 
ATOM   1860 C  CG2 . VAL B 1 58  ? -4.349  4.962   39.734  1.00 14.63 ? 46  VAL B CG2 1 
ATOM   1861 N  N   . ALA B 1 59  ? -5.147  7.938   38.487  1.00 8.63  ? 47  ALA B N   1 
ATOM   1862 C  CA  . ALA B 1 59  ? -5.942  9.115   38.810  1.00 11.73 ? 47  ALA B CA  1 
ATOM   1863 C  C   . ALA B 1 59  ? -7.422  8.777   38.826  1.00 9.32  ? 47  ALA B C   1 
ATOM   1864 O  O   . ALA B 1 59  ? -7.891  8.007   37.985  1.00 8.25  ? 47  ALA B O   1 
ATOM   1865 C  CB  . ALA B 1 59  ? -5.710  10.230  37.791  1.00 11.73 ? 47  ALA B CB  1 
ATOM   1866 N  N   . GLY B 1 60  ? -8.158  9.372   39.760  1.00 7.35  ? 48  GLY B N   1 
ATOM   1867 C  CA  . GLY B 1 60  ? -9.597  9.194   39.714  1.00 6.85  ? 48  GLY B CA  1 
ATOM   1868 C  C   . GLY B 1 60  ? -10.316 9.766   40.918  1.00 8.23  ? 48  GLY B C   1 
ATOM   1869 O  O   . GLY B 1 60  ? -9.714  10.357  41.832  1.00 8.20  ? 48  GLY B O   1 
ATOM   1870 N  N   . LYS B 1 61  ? -11.635 9.561   40.898  1.00 7.52  ? 49  LYS B N   1 
ATOM   1871 C  CA  . LYS B 1 61  ? -12.544 10.067  41.918  1.00 8.75  ? 49  LYS B CA  1 
ATOM   1872 C  C   . LYS B 1 61  ? -13.263 8.913   42.606  1.00 9.83  ? 49  LYS B C   1 
ATOM   1873 O  O   . LYS B 1 61  ? -13.485 7.849   42.022  1.00 9.30  ? 49  LYS B O   1 
ATOM   1874 C  CB  . LYS B 1 61  ? -13.599 11.017  41.309  1.00 8.66  ? 49  LYS B CB  1 
ATOM   1875 C  CG  . LYS B 1 61  ? -13.218 12.482  41.342  1.00 8.20  ? 49  LYS B CG  1 
ATOM   1876 C  CD  . LYS B 1 61  ? -14.382 13.377  40.891  1.00 9.03  ? 49  LYS B CD  1 
ATOM   1877 C  CE  . LYS B 1 61  ? -14.061 14.855  41.182  1.00 10.83 ? 49  LYS B CE  1 
ATOM   1878 N  NZ  . LYS B 1 61  ? -15.062 15.745  40.521  1.00 10.42 ? 49  LYS B NZ  1 
ATOM   1879 N  N   . GLY B 1 62  ? -13.679 9.154   43.837  1.00 7.63  ? 50  GLY B N   1 
ATOM   1880 C  CA  . GLY B 1 62  ? -14.405 8.154   44.577  1.00 9.13  ? 50  GLY B CA  1 
ATOM   1881 C  C   . GLY B 1 62  ? -14.656 8.573   46.005  1.00 9.01  ? 50  GLY B C   1 
ATOM   1882 O  O   . GLY B 1 62  ? -15.175 9.664   46.257  1.00 9.32  ? 50  GLY B O   1 
ATOM   1883 N  N   . TRP B 1 63  ? -14.258 7.720   46.951  1.00 9.18  ? 51  TRP B N   1 
ATOM   1884 C  CA  . TRP B 1 63  ? -14.695 7.821   48.334  1.00 9.88  ? 51  TRP B CA  1 
ATOM   1885 C  C   . TRP B 1 63  ? -13.523 7.589   49.265  1.00 9.72  ? 51  TRP B C   1 
ATOM   1886 O  O   . TRP B 1 63  ? -12.603 6.826   48.965  1.00 9.40  ? 51  TRP B O   1 
ATOM   1887 C  CB  . TRP B 1 63  ? -15.796 6.793   48.662  1.00 12.49 ? 51  TRP B CB  1 
ATOM   1888 C  CG  . TRP B 1 63  ? -16.936 6.885   47.724  1.00 14.14 ? 51  TRP B CG  1 
ATOM   1889 C  CD1 . TRP B 1 63  ? -18.087 7.603   47.894  1.00 17.82 ? 51  TRP B CD1 1 
ATOM   1890 C  CD2 . TRP B 1 63  ? -17.033 6.260   46.443  1.00 15.20 ? 51  TRP B CD2 1 
ATOM   1891 N  NE1 . TRP B 1 63  ? -18.897 7.459   46.792  1.00 18.07 ? 51  TRP B NE1 1 
ATOM   1892 C  CE2 . TRP B 1 63  ? -18.273 6.636   45.889  1.00 17.26 ? 51  TRP B CE2 1 
ATOM   1893 C  CE3 . TRP B 1 63  ? -16.189 5.418   45.708  1.00 16.15 ? 51  TRP B CE3 1 
ATOM   1894 C  CZ2 . TRP B 1 63  ? -18.694 6.197   44.628  1.00 22.09 ? 51  TRP B CZ2 1 
ATOM   1895 C  CZ3 . TRP B 1 63  ? -16.610 4.985   44.452  1.00 18.73 ? 51  TRP B CZ3 1 
ATOM   1896 C  CH2 . TRP B 1 63  ? -17.852 5.375   43.935  1.00 19.37 ? 51  TRP B CH2 1 
ATOM   1897 N  N   . ASN B 1 64  ? -13.574 8.256   50.410  1.00 10.63 ? 52  ASN B N   1 
ATOM   1898 C  CA  . ASN B 1 64  ? -12.662 7.935   51.493  1.00 10.25 ? 52  ASN B CA  1 
ATOM   1899 C  C   . ASN B 1 64  ? -13.414 8.036   52.816  1.00 13.82 ? 52  ASN B C   1 
ATOM   1900 O  O   . ASN B 1 64  ? -13.966 9.098   53.135  1.00 12.62 ? 52  ASN B O   1 
ATOM   1901 C  CB  . ASN B 1 64  ? -11.451 8.865   51.481  1.00 11.14 ? 52  ASN B CB  1 
ATOM   1902 C  CG  . ASN B 1 64  ? -10.271 8.281   52.227  1.00 15.18 ? 52  ASN B CG  1 
ATOM   1903 O  OD1 . ASN B 1 64  ? -10.323 7.145   52.716  1.00 15.72 ? 52  ASN B OD1 1 
ATOM   1904 N  ND2 . ASN B 1 64  ? -9.193  9.057   52.324  1.00 17.27 ? 52  ASN B ND2 1 
ATOM   1905 N  N   . PRO B 1 65  ? -13.509 6.945   53.590  1.00 14.64 ? 53  PRO B N   1 
ATOM   1906 C  CA  . PRO B 1 65  ? -13.025 5.603   53.243  1.00 13.72 ? 53  PRO B CA  1 
ATOM   1907 C  C   . PRO B 1 65  ? -13.949 4.905   52.252  1.00 14.43 ? 53  PRO B C   1 
ATOM   1908 O  O   . PRO B 1 65  ? -15.134 5.262   52.138  1.00 12.77 ? 53  PRO B O   1 
ATOM   1909 C  CB  . PRO B 1 65  ? -13.048 4.870   54.587  1.00 15.05 ? 53  PRO B CB  1 
ATOM   1910 C  CG  . PRO B 1 65  ? -14.241 5.479   55.287  1.00 18.81 ? 53  PRO B CG  1 
ATOM   1911 C  CD  . PRO B 1 65  ? -14.253 6.950   54.866  1.00 18.42 ? 53  PRO B CD  1 
ATOM   1912 N  N   . GLY B 1 66  ? -13.429 3.922   51.525  1.00 11.21 ? 54  GLY B N   1 
ATOM   1913 C  CA  . GLY B 1 66  ? -14.312 3.005   50.831  1.00 14.48 ? 54  GLY B CA  1 
ATOM   1914 C  C   . GLY B 1 66  ? -15.097 2.163   51.822  1.00 17.21 ? 54  GLY B C   1 
ATOM   1915 O  O   . GLY B 1 66  ? -14.625 1.833   52.904  1.00 16.64 ? 54  GLY B O   1 
ATOM   1916 N  N   . SER B 1 67  ? -16.331 1.831   51.467  1.00 20.19 ? 55  SER B N   1 
ATOM   1917 C  CA  . SER B 1 67  ? -17.141 0.983   52.340  1.00 18.15 ? 55  SER B CA  1 
ATOM   1918 C  C   . SER B 1 67  ? -17.790 -0.123  51.540  1.00 23.95 ? 55  SER B C   1 
ATOM   1919 O  O   . SER B 1 67  ? -18.957 -0.478  51.754  1.00 24.71 ? 55  SER B O   1 
ATOM   1920 C  CB  . SER B 1 67  ? -18.189 1.796   53.096  1.00 24.39 ? 55  SER B CB  1 
ATOM   1921 O  OG  . SER B 1 67  ? -18.971 2.558   52.203  1.00 26.00 ? 55  SER B OG  1 
ATOM   1922 N  N   . SER B 1 68  ? -17.035 -0.673  50.594  1.00 15.63 ? 56  SER B N   1 
ATOM   1923 C  CA  . SER B 1 68  ? -17.465 -1.828  49.812  1.00 18.94 ? 56  SER B CA  1 
ATOM   1924 C  C   . SER B 1 68  ? -18.774 -1.557  49.074  1.00 22.93 ? 56  SER B C   1 
ATOM   1925 O  O   . SER B 1 68  ? -19.606 -2.453  48.902  1.00 25.78 ? 56  SER B O   1 
ATOM   1926 C  CB  . SER B 1 68  ? -17.584 -3.071  50.700  1.00 20.21 ? 56  SER B CB  1 
ATOM   1927 O  OG  . SER B 1 68  ? -16.345 -3.366  51.313  1.00 24.97 ? 56  SER B OG  1 
ATOM   1928 N  N   . GLN B 1 69  ? -18.973 -0.325  48.621  1.00 21.65 ? 57  GLN B N   1 
ATOM   1929 C  CA  . GLN B 1 69  ? -20.234 -0.019  47.969  1.00 23.19 ? 57  GLN B CA  1 
ATOM   1930 C  C   . GLN B 1 69  ? -20.257 -0.553  46.541  1.00 20.10 ? 57  GLN B C   1 
ATOM   1931 O  O   . GLN B 1 69  ? -19.226 -0.906  45.952  1.00 16.82 ? 57  GLN B O   1 
ATOM   1932 C  CB  . GLN B 1 69  ? -20.499 1.487   47.957  1.00 26.10 ? 57  GLN B CB  1 
ATOM   1933 C  CG  . GLN B 1 69  ? -19.345 2.334   47.472  1.00 20.05 ? 57  GLN B CG  1 
ATOM   1934 C  CD  . GLN B 1 69  ? -18.599 2.958   48.625  1.00 25.36 ? 57  GLN B CD  1 
ATOM   1935 O  OE1 . GLN B 1 69  ? -17.762 2.316   49.238  1.00 21.38 ? 57  GLN B OE1 1 
ATOM   1936 N  NE2 . GLN B 1 69  ? -18.913 4.210   48.939  1.00 29.12 ? 57  GLN B NE2 1 
ATOM   1937 N  N   . THR B 1 70  ? -21.463 -0.613  45.989  1.00 16.89 ? 58  THR B N   1 
ATOM   1938 C  CA  . THR B 1 70  ? -21.662 -0.954  44.591  1.00 16.41 ? 58  THR B CA  1 
ATOM   1939 C  C   . THR B 1 70  ? -21.515 0.317   43.757  1.00 19.09 ? 58  THR B C   1 
ATOM   1940 O  O   . THR B 1 70  ? -22.275 1.277   43.934  1.00 21.85 ? 58  THR B O   1 
ATOM   1941 C  CB  . THR B 1 70  ? -23.031 -1.596  44.399  1.00 20.51 ? 58  THR B CB  1 
ATOM   1942 O  OG1 . THR B 1 70  ? -23.069 -2.834  45.120  1.00 18.76 ? 58  THR B OG1 1 
ATOM   1943 C  CG2 . THR B 1 70  ? -23.264 -1.889  42.954  1.00 19.83 ? 58  THR B CG2 1 
ATOM   1944 N  N   . ILE B 1 71  ? -20.537 0.323   42.858  1.00 14.03 ? 59  ILE B N   1 
ATOM   1945 C  CA  . ILE B 1 71  ? -20.116 1.517   42.128  1.00 15.27 ? 59  ILE B CA  1 
ATOM   1946 C  C   . ILE B 1 71  ? -20.766 1.531   40.756  1.00 15.46 ? 59  ILE B C   1 
ATOM   1947 O  O   . ILE B 1 71  ? -20.792 0.510   40.065  1.00 16.33 ? 59  ILE B O   1 
ATOM   1948 C  CB  . ILE B 1 71  ? -18.580 1.531   41.992  1.00 16.84 ? 59  ILE B CB  1 
ATOM   1949 C  CG1 . ILE B 1 71  ? -17.940 1.722   43.359  1.00 16.52 ? 59  ILE B CG1 1 
ATOM   1950 C  CG2 . ILE B 1 71  ? -18.117 2.584   40.978  1.00 17.69 ? 59  ILE B CG2 1 
ATOM   1951 C  CD1 . ILE B 1 71  ? -16.428 1.541   43.324  1.00 21.41 ? 59  ILE B CD1 1 
ATOM   1952 N  N   . THR B 1 72  ? -21.270 2.688   40.341  1.00 14.95 ? 60  THR B N   1 
ATOM   1953 C  CA  . THR B 1 72  ? -21.658 2.882   38.952  1.00 17.86 ? 60  THR B CA  1 
ATOM   1954 C  C   . THR B 1 72  ? -20.899 4.081   38.406  1.00 16.45 ? 60  THR B C   1 
ATOM   1955 O  O   . THR B 1 72  ? -20.682 5.068   39.116  1.00 18.87 ? 60  THR B O   1 
ATOM   1956 C  CB  . THR B 1 72  ? -23.175 3.094   38.781  1.00 21.99 ? 60  THR B CB  1 
ATOM   1957 O  OG1 . THR B 1 72  ? -23.605 4.194   39.583  1.00 30.41 ? 60  THR B OG1 1 
ATOM   1958 C  CG2 . THR B 1 72  ? -23.944 1.849   39.182  1.00 25.72 ? 60  THR B CG2 1 
ATOM   1959 N  N   . TYR B 1 73  ? -20.468 3.983   37.157  1.00 16.53 ? 61  TYR B N   1 
ATOM   1960 C  CA  . TYR B 1 73  ? -19.757 5.088   36.544  1.00 14.45 ? 61  TYR B CA  1 
ATOM   1961 C  C   . TYR B 1 73  ? -20.025 5.046   35.049  1.00 14.53 ? 61  TYR B C   1 
ATOM   1962 O  O   . TYR B 1 73  ? -20.460 4.029   34.498  1.00 14.39 ? 61  TYR B O   1 
ATOM   1963 C  CB  . TYR B 1 73  ? -18.243 5.023   36.839  1.00 17.01 ? 61  TYR B CB  1 
ATOM   1964 C  CG  . TYR B 1 73  ? -17.580 3.917   36.080  1.00 15.32 ? 61  TYR B CG  1 
ATOM   1965 C  CD1 . TYR B 1 73  ? -17.659 2.603   36.520  1.00 16.67 ? 61  TYR B CD1 1 
ATOM   1966 C  CD2 . TYR B 1 73  ? -16.922 4.172   34.883  1.00 14.92 ? 61  TYR B CD2 1 
ATOM   1967 C  CE1 . TYR B 1 73  ? -17.084 1.583   35.809  1.00 17.62 ? 61  TYR B CE1 1 
ATOM   1968 C  CE2 . TYR B 1 73  ? -16.337 3.154   34.163  1.00 17.17 ? 61  TYR B CE2 1 
ATOM   1969 C  CZ  . TYR B 1 73  ? -16.425 1.868   34.621  1.00 15.34 ? 61  TYR B CZ  1 
ATOM   1970 O  OH  . TYR B 1 73  ? -15.848 0.860   33.899  1.00 18.56 ? 61  TYR B OH  1 
ATOM   1971 N  N   . SER B 1 74  ? -19.776 6.169   34.397  1.00 13.47 ? 62  SER B N   1 
ATOM   1972 C  CA  . SER B 1 74  ? -19.959 6.260   32.959  1.00 13.10 ? 62  SER B CA  1 
ATOM   1973 C  C   . SER B 1 74  ? -18.780 7.034   32.390  1.00 12.81 ? 62  SER B C   1 
ATOM   1974 O  O   . SER B 1 74  ? -17.913 7.524   33.127  1.00 13.35 ? 62  SER B O   1 
ATOM   1975 C  CB  . SER B 1 74  ? -21.294 6.926   32.609  1.00 14.92 ? 62  SER B CB  1 
ATOM   1976 O  OG  . SER B 1 74  ? -21.310 8.279   33.026  1.00 19.90 ? 62  SER B OG  1 
ATOM   1977 N  N   . GLY B 1 75  ? -18.744 7.131   31.069  1.00 11.98 ? 63  GLY B N   1 
ATOM   1978 C  CA  . GLY B 1 75  ? -17.739 7.943   30.418  1.00 12.59 ? 63  GLY B CA  1 
ATOM   1979 C  C   . GLY B 1 75  ? -17.003 7.226   29.307  1.00 12.61 ? 63  GLY B C   1 
ATOM   1980 O  O   . GLY B 1 75  ? -17.514 6.273   28.698  1.00 12.35 ? 63  GLY B O   1 
ATOM   1981 N  N   . GLU B 1 76  ? -15.782 7.680   29.045  1.00 10.90 ? 64  GLU B N   1 
ATOM   1982 C  CA  . GLU B 1 76  ? -14.999 7.080   27.985  1.00 12.76 ? 64  GLU B CA  1 
ATOM   1983 C  C   . GLU B 1 76  ? -13.531 7.097   28.369  1.00 13.67 ? 64  GLU B C   1 
ATOM   1984 O  O   . GLU B 1 76  ? -13.076 7.927   29.163  1.00 11.33 ? 64  GLU B O   1 
ATOM   1985 C  CB  . GLU B 1 76  ? -15.206 7.799   26.658  1.00 15.74 ? 64  GLU B CB  1 
ATOM   1986 C  CG  . GLU B 1 76  ? -14.722 9.217   26.635  1.00 16.00 ? 64  GLU B CG  1 
ATOM   1987 C  CD  . GLU B 1 76  ? -14.979 9.851   25.276  1.00 30.62 ? 64  GLU B CD  1 
ATOM   1988 O  OE1 . GLU B 1 76  ? -16.158 9.940   24.879  1.00 33.58 ? 64  GLU B OE1 1 
ATOM   1989 O  OE2 . GLU B 1 76  ? -14.007 10.236  24.595  1.00 35.95 ? 64  GLU B OE2 1 
ATOM   1990 N  N   . TRP B 1 77  ? -12.796 6.174   27.758  1.00 11.44 ? 65  TRP B N   1 
ATOM   1991 C  CA  . TRP B 1 77  ? -11.404 5.903   28.105  1.00 12.16 ? 65  TRP B CA  1 
ATOM   1992 C  C   . TRP B 1 77  ? -10.700 5.544   26.806  1.00 11.56 ? 65  TRP B C   1 
ATOM   1993 O  O   . TRP B 1 77  ? -10.986 4.497   26.218  1.00 12.06 ? 65  TRP B O   1 
ATOM   1994 C  CB  . TRP B 1 77  ? -11.337 4.779   29.128  1.00 11.62 ? 65  TRP B CB  1 
ATOM   1995 C  CG  . TRP B 1 77  ? -10.026 4.066   29.275  1.00 11.65 ? 65  TRP B CG  1 
ATOM   1996 C  CD1 . TRP B 1 77  ? -8.923  4.497   29.962  1.00 14.11 ? 65  TRP B CD1 1 
ATOM   1997 C  CD2 . TRP B 1 77  ? -9.716  2.758   28.788  1.00 11.62 ? 65  TRP B CD2 1 
ATOM   1998 N  NE1 . TRP B 1 77  ? -7.933  3.536   29.914  1.00 13.38 ? 65  TRP B NE1 1 
ATOM   1999 C  CE2 . TRP B 1 77  ? -8.391  2.461   29.197  1.00 13.94 ? 65  TRP B CE2 1 
ATOM   2000 C  CE3 . TRP B 1 77  ? -10.420 1.814   28.028  1.00 13.40 ? 65  TRP B CE3 1 
ATOM   2001 C  CZ2 . TRP B 1 77  ? -7.764  1.265   28.870  1.00 14.80 ? 65  TRP B CZ2 1 
ATOM   2002 C  CZ3 . TRP B 1 77  ? -9.799  0.631   27.704  1.00 13.38 ? 65  TRP B CZ3 1 
ATOM   2003 C  CH2 . TRP B 1 77  ? -8.479  0.362   28.124  1.00 14.77 ? 65  TRP B CH2 1 
ATOM   2004 N  N   . ASN B 1 78  ? -9.806  6.423   26.350  1.00 11.73 ? 66  ASN B N   1 
ATOM   2005 C  CA  . ASN B 1 78  ? -9.256  6.366   24.996  1.00 12.72 ? 66  ASN B CA  1 
ATOM   2006 C  C   . ASN B 1 78  ? -7.736  6.337   25.038  1.00 12.31 ? 66  ASN B C   1 
ATOM   2007 O  O   . ASN B 1 78  ? -7.076  7.338   24.716  1.00 12.68 ? 66  ASN B O   1 
ATOM   2008 C  CB  . ASN B 1 78  ? -9.745  7.554   24.178  1.00 12.44 ? 66  ASN B CB  1 
ATOM   2009 C  CG  . ASN B 1 78  ? -11.240 7.534   23.978  1.00 18.12 ? 66  ASN B CG  1 
ATOM   2010 O  OD1 . ASN B 1 78  ? -11.784 6.585   23.413  1.00 23.28 ? 66  ASN B OD1 1 
ATOM   2011 N  ND2 . ASN B 1 78  ? -11.915 8.584   24.434  1.00 24.84 ? 66  ASN B ND2 1 
ATOM   2012 N  N   . PRO B 1 79  ? -7.148  5.199   25.391  1.00 13.93 ? 67  PRO B N   1 
ATOM   2013 C  CA  . PRO B 1 79  ? -5.688  5.108   25.454  1.00 12.38 ? 67  PRO B CA  1 
ATOM   2014 C  C   . PRO B 1 79  ? -5.071  4.795   24.103  1.00 15.19 ? 67  PRO B C   1 
ATOM   2015 O  O   . PRO B 1 79  ? -5.694  4.209   23.214  1.00 15.23 ? 67  PRO B O   1 
ATOM   2016 C  CB  . PRO B 1 79  ? -5.455  3.943   26.416  1.00 13.62 ? 67  PRO B CB  1 
ATOM   2017 C  CG  . PRO B 1 79  ? -6.617  3.029   26.126  1.00 15.54 ? 67  PRO B CG  1 
ATOM   2018 C  CD  . PRO B 1 79  ? -7.788  3.952   25.856  1.00 14.40 ? 67  PRO B CD  1 
ATOM   2019 N  N   . ASN B 1 80  ? -3.805  5.186   23.983  1.00 13.37 ? 68  ASN B N   1 
ATOM   2020 C  CA  . ASN B 1 80  ? -2.914  4.789   22.897  1.00 15.90 ? 68  ASN B CA  1 
ATOM   2021 C  C   . ASN B 1 80  ? -1.686  4.184   23.576  1.00 15.76 ? 68  ASN B C   1 
ATOM   2022 O  O   . ASN B 1 80  ? -0.720  4.887   23.881  1.00 13.42 ? 68  ASN B O   1 
ATOM   2023 C  CB  . ASN B 1 80  ? -2.547  5.986   21.993  1.00 18.17 ? 68  ASN B CB  1 
ATOM   2024 C  CG  . ASN B 1 80  ? -1.610  5.597   20.859  1.00 24.12 ? 68  ASN B CG  1 
ATOM   2025 O  OD1 . ASN B 1 80  ? -1.546  4.435   20.458  1.00 30.09 ? 68  ASN B OD1 1 
ATOM   2026 N  ND2 . ASN B 1 80  ? -0.879  6.579   20.335  1.00 31.22 ? 68  ASN B ND2 1 
ATOM   2027 N  N   . GLY B 1 81  ? -1.742  2.888   23.848  1.00 13.92 ? 69  GLY B N   1 
ATOM   2028 C  CA  . GLY B 1 81  ? -0.706  2.213   24.598  1.00 14.12 ? 69  GLY B CA  1 
ATOM   2029 C  C   . GLY B 1 81  ? -1.212  1.793   25.968  1.00 14.10 ? 69  GLY B C   1 
ATOM   2030 O  O   . GLY B 1 81  ? -2.415  1.805   26.253  1.00 13.77 ? 69  GLY B O   1 
ATOM   2031 N  N   . ASN B 1 82  ? -0.254  1.471   26.838  1.00 13.57 ? 70  ASN B N   1 
ATOM   2032 C  CA  . ASN B 1 82  ? -0.512  0.766   28.086  1.00 12.56 ? 70  ASN B CA  1 
ATOM   2033 C  C   . ASN B 1 82  ? -1.352  1.628   29.028  1.00 13.66 ? 70  ASN B C   1 
ATOM   2034 O  O   . ASN B 1 82  ? -0.910  2.694   29.463  1.00 13.10 ? 70  ASN B O   1 
ATOM   2035 C  CB  . ASN B 1 82  ? 0.829   0.396   28.723  1.00 12.63 ? 70  ASN B CB  1 
ATOM   2036 C  CG  . ASN B 1 82  ? 0.698   -0.430  29.989  1.00 15.19 ? 70  ASN B CG  1 
ATOM   2037 O  OD1 . ASN B 1 82  ? -0.394  -0.765  30.447  1.00 19.25 ? 70  ASN B OD1 1 
ATOM   2038 N  ND2 . ASN B 1 82  ? 1.848   -0.777  30.565  1.00 18.75 ? 70  ASN B ND2 1 
ATOM   2039 N  N   . SER B 1 83  ? -2.563  1.165   29.334  1.00 10.23 ? 71  SER B N   1 
ATOM   2040 C  CA  . SER B 1 83  ? -3.469  1.883   30.215  1.00 8.53  ? 71  SER B CA  1 
ATOM   2041 C  C   . SER B 1 83  ? -4.519  0.900   30.713  1.00 10.52 ? 71  SER B C   1 
ATOM   2042 O  O   . SER B 1 83  ? -4.804  -0.110  30.056  1.00 10.26 ? 71  SER B O   1 
ATOM   2043 C  CB  . SER B 1 83  ? -4.132  3.060   29.481  1.00 10.37 ? 71  SER B CB  1 
ATOM   2044 O  OG  . SER B 1 83  ? -5.041  3.766   30.304  1.00 10.98 ? 71  SER B OG  1 
ATOM   2045 N  N   . TYR B 1 84  ? -5.078  1.185   31.884  1.00 9.32  ? 72  TYR B N   1 
ATOM   2046 C  CA  . TYR B 1 84  ? -6.234  0.410   32.294  1.00 10.74 ? 72  TYR B CA  1 
ATOM   2047 C  C   . TYR B 1 84  ? -7.172  1.260   33.138  1.00 11.81 ? 72  TYR B C   1 
ATOM   2048 O  O   . TYR B 1 84  ? -6.807  2.316   33.665  1.00 8.86  ? 72  TYR B O   1 
ATOM   2049 C  CB  . TYR B 1 84  ? -5.839  -0.882  33.026  1.00 10.34 ? 72  TYR B CB  1 
ATOM   2050 C  CG  . TYR B 1 84  ? -4.811  -0.731  34.108  1.00 14.01 ? 72  TYR B CG  1 
ATOM   2051 C  CD1 . TYR B 1 84  ? -3.451  -0.777  33.833  1.00 21.14 ? 72  TYR B CD1 1 
ATOM   2052 C  CD2 . TYR B 1 84  ? -5.213  -0.572  35.417  1.00 18.48 ? 72  TYR B CD2 1 
ATOM   2053 C  CE1 . TYR B 1 84  ? -2.513  -0.636  34.867  1.00 22.76 ? 72  TYR B CE1 1 
ATOM   2054 C  CE2 . TYR B 1 84  ? -4.315  -0.439  36.421  1.00 23.66 ? 72  TYR B CE2 1 
ATOM   2055 C  CZ  . TYR B 1 84  ? -2.971  -0.471  36.162  1.00 21.07 ? 72  TYR B CZ  1 
ATOM   2056 O  OH  . TYR B 1 84  ? -2.119  -0.324  37.242  1.00 30.13 ? 72  TYR B OH  1 
ATOM   2057 N  N   . LEU B 1 85  ? -8.408  0.776   33.220  1.00 8.00  ? 73  LEU B N   1 
ATOM   2058 C  CA  . LEU B 1 85  ? -9.519  1.429   33.896  1.00 7.87  ? 73  LEU B CA  1 
ATOM   2059 C  C   . LEU B 1 85  ? -9.990  0.473   34.980  1.00 10.01 ? 73  LEU B C   1 
ATOM   2060 O  O   . LEU B 1 85  ? -10.304 -0.686  34.686  1.00 10.56 ? 73  LEU B O   1 
ATOM   2061 C  CB  . LEU B 1 85  ? -10.632 1.731   32.886  1.00 10.20 ? 73  LEU B CB  1 
ATOM   2062 C  CG  . LEU B 1 85  ? -11.874 2.442   33.411  1.00 13.08 ? 73  LEU B CG  1 
ATOM   2063 C  CD1 . LEU B 1 85  ? -11.528 3.851   33.880  1.00 13.64 ? 73  LEU B CD1 1 
ATOM   2064 C  CD2 . LEU B 1 85  ? -12.931 2.478   32.301  1.00 12.33 ? 73  LEU B CD2 1 
ATOM   2065 N  N   . SER B 1 86  ? -10.020 0.939   36.228  1.00 8.08  ? 74  SER B N   1 
ATOM   2066 C  CA  . SER B 1 86  ? -10.209 0.027   37.346  1.00 7.66  ? 74  SER B CA  1 
ATOM   2067 C  C   . SER B 1 86  ? -10.936 0.718   38.482  1.00 9.48  ? 74  SER B C   1 
ATOM   2068 O  O   . SER B 1 86  ? -10.889 1.941   38.625  1.00 11.79 ? 74  SER B O   1 
ATOM   2069 C  CB  . SER B 1 86  ? -8.865  -0.482  37.909  1.00 11.78 ? 74  SER B CB  1 
ATOM   2070 O  OG  . SER B 1 86  ? -8.003  -0.876  36.870  1.00 19.32 ? 74  SER B OG  1 
ATOM   2071 N  N   . VAL B 1 87  ? -11.593 -0.090  39.306  1.00 8.55  ? 75  VAL B N   1 
ATOM   2072 C  CA  . VAL B 1 87  ? -11.842 0.320   40.681  1.00 6.08  ? 75  VAL B CA  1 
ATOM   2073 C  C   . VAL B 1 87  ? -10.562 0.040   41.452  1.00 8.69  ? 75  VAL B C   1 
ATOM   2074 O  O   . VAL B 1 87  ? -10.004 -1.053  41.353  1.00 10.74 ? 75  VAL B O   1 
ATOM   2075 C  CB  . VAL B 1 87  ? -13.041 -0.432  41.278  1.00 8.37  ? 75  VAL B CB  1 
ATOM   2076 C  CG1 . VAL B 1 87  ? -13.199 -0.051  42.758  1.00 8.43  ? 75  VAL B CG1 1 
ATOM   2077 C  CG2 . VAL B 1 87  ? -14.311 -0.100  40.500  1.00 10.02 ? 75  VAL B CG2 1 
ATOM   2078 N  N   . TYR B 1 88  ? -10.068 1.037   42.180  1.00 7.24  ? 76  TYR B N   1 
ATOM   2079 C  CA  . TYR B 1 88  ? -8.707  0.999   42.710  1.00 6.99  ? 76  TYR B CA  1 
ATOM   2080 C  C   . TYR B 1 88  ? -8.733  1.545   44.124  1.00 6.65  ? 76  TYR B C   1 
ATOM   2081 O  O   . TYR B 1 88  ? -9.428  2.525   44.396  1.00 8.30  ? 76  TYR B O   1 
ATOM   2082 C  CB  . TYR B 1 88  ? -7.784  1.843   41.829  1.00 7.81  ? 76  TYR B CB  1 
ATOM   2083 C  CG  . TYR B 1 88  ? -6.443  2.198   42.412  1.00 8.53  ? 76  TYR B CG  1 
ATOM   2084 C  CD1 . TYR B 1 88  ? -5.445  1.248   42.507  1.00 10.32 ? 76  TYR B CD1 1 
ATOM   2085 C  CD2 . TYR B 1 88  ? -6.159  3.499   42.800  1.00 9.01  ? 76  TYR B CD2 1 
ATOM   2086 C  CE1 . TYR B 1 88  ? -4.196  1.567   43.024  1.00 10.81 ? 76  TYR B CE1 1 
ATOM   2087 C  CE2 . TYR B 1 88  ? -4.920  3.832   43.329  1.00 9.70  ? 76  TYR B CE2 1 
ATOM   2088 C  CZ  . TYR B 1 88  ? -3.938  2.859   43.423  1.00 10.33 ? 76  TYR B CZ  1 
ATOM   2089 O  OH  . TYR B 1 88  ? -2.684  3.166   43.938  1.00 11.08 ? 76  TYR B OH  1 
ATOM   2090 N  N   . GLY B 1 89  ? -7.998  0.918   45.026  1.00 8.17  ? 77  GLY B N   1 
ATOM   2091 C  CA  . GLY B 1 89  ? -8.006  1.439   46.381  1.00 7.95  ? 77  GLY B CA  1 
ATOM   2092 C  C   . GLY B 1 89  ? -6.965  0.785   47.261  1.00 7.79  ? 77  GLY B C   1 
ATOM   2093 O  O   . GLY B 1 89  ? -6.152  -0.022  46.803  1.00 8.69  ? 77  GLY B O   1 
ATOM   2094 N  N   . TRP B 1 90  ? -7.035  1.127   48.556  1.00 7.11  ? 78  TRP B N   1 
ATOM   2095 C  CA  . TRP B 1 90  ? -6.070  0.654   49.540  1.00 8.74  ? 78  TRP B CA  1 
ATOM   2096 C  C   . TRP B 1 90  ? -6.759  0.213   50.822  1.00 7.51  ? 78  TRP B C   1 
ATOM   2097 O  O   . TRP B 1 90  ? -7.810  0.737   51.197  1.00 7.38  ? 78  TRP B O   1 
ATOM   2098 C  CB  . TRP B 1 90  ? -5.067  1.746   49.925  1.00 7.66  ? 78  TRP B CB  1 
ATOM   2099 C  CG  . TRP B 1 90  ? -4.189  2.177   48.821  1.00 7.83  ? 78  TRP B CG  1 
ATOM   2100 C  CD1 . TRP B 1 90  ? -4.517  3.022   47.779  1.00 9.02  ? 78  TRP B CD1 1 
ATOM   2101 C  CD2 . TRP B 1 90  ? -2.826  1.796   48.619  1.00 8.66  ? 78  TRP B CD2 1 
ATOM   2102 N  NE1 . TRP B 1 90  ? -3.424  3.177   46.946  1.00 9.67  ? 78  TRP B NE1 1 
ATOM   2103 C  CE2 . TRP B 1 90  ? -2.381  2.432   47.436  1.00 10.48 ? 78  TRP B CE2 1 
ATOM   2104 C  CE3 . TRP B 1 90  ? -1.940  0.960   49.310  1.00 8.76  ? 78  TRP B CE3 1 
ATOM   2105 C  CZ2 . TRP B 1 90  ? -1.083  2.274   46.944  1.00 11.50 ? 78  TRP B CZ2 1 
ATOM   2106 C  CZ3 . TRP B 1 90  ? -0.653  0.801   48.818  1.00 9.06  ? 78  TRP B CZ3 1 
ATOM   2107 C  CH2 . TRP B 1 90  ? -0.232  1.466   47.653  1.00 10.63 ? 78  TRP B CH2 1 
ATOM   2108 N  N   . THR B 1 91  ? -6.127  -0.718  51.523  1.00 8.04  ? 79  THR B N   1 
ATOM   2109 C  CA  . THR B 1 91  ? -6.411  -0.921  52.935  1.00 8.30  ? 79  THR B CA  1 
ATOM   2110 C  C   . THR B 1 91  ? -5.134  -0.669  53.718  1.00 8.38  ? 79  THR B C   1 
ATOM   2111 O  O   . THR B 1 91  ? -4.037  -0.593  53.154  1.00 8.84  ? 79  THR B O   1 
ATOM   2112 C  CB  . THR B 1 91  ? -6.939  -2.330  53.264  1.00 11.06 ? 79  THR B CB  1 
ATOM   2113 O  OG1 . THR B 1 91  ? -5.877  -3.289  53.187  1.00 11.43 ? 79  THR B OG1 1 
ATOM   2114 C  CG2 . THR B 1 91  ? -8.056  -2.748  52.325  1.00 9.73  ? 79  THR B CG2 1 
ATOM   2115 N  N   . GLN B 1 92  ? -5.308  -0.506  55.030  1.00 9.67  ? 80  GLN B N   1 
ATOM   2116 C  CA  . GLN B 1 92  ? -4.210  -0.327  55.970  1.00 9.59  ? 80  GLN B CA  1 
ATOM   2117 C  C   . GLN B 1 92  ? -4.255  -1.411  57.040  1.00 11.39 ? 80  GLN B C   1 
ATOM   2118 O  O   . GLN B 1 92  ? -5.328  -1.877  57.430  1.00 9.55  ? 80  GLN B O   1 
ATOM   2119 C  CB  . GLN B 1 92  ? -4.286  1.056   56.629  1.00 10.88 ? 80  GLN B CB  1 
ATOM   2120 C  CG  . GLN B 1 92  ? -3.889  2.162   55.691  1.00 12.49 ? 80  GLN B CG  1 
ATOM   2121 C  CD  . GLN B 1 92  ? -4.466  3.505   56.093  1.00 21.64 ? 80  GLN B CD  1 
ATOM   2122 O  OE1 . GLN B 1 92  ? -5.684  3.693   56.126  1.00 21.33 ? 80  GLN B OE1 1 
ATOM   2123 N  NE2 . GLN B 1 92  ? -3.589  4.453   56.388  1.00 21.79 ? 80  GLN B NE2 1 
ATOM   2124 N  N   . ASN B 1 93  ? -3.082  -1.817  57.517  1.00 8.27  ? 81  ASN B N   1 
ATOM   2125 C  CA  . ASN B 1 93  ? -2.979  -2.726  58.652  1.00 9.04  ? 81  ASN B CA  1 
ATOM   2126 C  C   . ASN B 1 93  ? -3.775  -4.028  58.454  1.00 9.03  ? 81  ASN B C   1 
ATOM   2127 O  O   . ASN B 1 93  ? -4.716  -4.303  59.202  1.00 10.78 ? 81  ASN B O   1 
ATOM   2128 C  CB  . ASN B 1 93  ? -3.424  -2.013  59.916  1.00 11.57 ? 81  ASN B CB  1 
ATOM   2129 C  CG  . ASN B 1 93  ? -3.085  -2.783  61.163  1.00 12.62 ? 81  ASN B CG  1 
ATOM   2130 O  OD1 . ASN B 1 93  ? -2.146  -3.579  61.154  1.00 10.16 ? 81  ASN B OD1 1 
ATOM   2131 N  ND2 . ASN B 1 93  ? -3.852  -2.569  62.238  1.00 13.71 ? 81  ASN B ND2 1 
ATOM   2132 N  N   . PRO B 1 94  ? -3.404  -4.863  57.464  1.00 8.63  ? 82  PRO B N   1 
ATOM   2133 C  CA  . PRO B 1 94  ? -2.246  -4.739  56.566  1.00 10.36 ? 82  PRO B CA  1 
ATOM   2134 C  C   . PRO B 1 94  ? -2.438  -3.777  55.387  1.00 10.43 ? 82  PRO B C   1 
ATOM   2135 O  O   . PRO B 1 94  ? -3.546  -3.591  54.882  1.00 9.19  ? 82  PRO B O   1 
ATOM   2136 C  CB  . PRO B 1 94  ? -2.067  -6.164  56.033  1.00 10.31 ? 82  PRO B CB  1 
ATOM   2137 C  CG  . PRO B 1 94  ? -3.435  -6.728  56.065  1.00 12.35 ? 82  PRO B CG  1 
ATOM   2138 C  CD  . PRO B 1 94  ? -4.086  -6.160  57.285  1.00 12.01 ? 82  PRO B CD  1 
ATOM   2139 N  N   . LEU B 1 95  ? -1.322  -3.184  54.984  1.00 10.28 ? 83  LEU B N   1 
ATOM   2140 C  CA  . LEU B 1 95  ? -1.277  -2.346  53.794  1.00 10.63 ? 83  LEU B CA  1 
ATOM   2141 C  C   . LEU B 1 95  ? -1.467  -3.208  52.542  1.00 11.07 ? 83  LEU B C   1 
ATOM   2142 O  O   . LEU B 1 95  ? -0.716  -4.161  52.298  1.00 10.47 ? 83  LEU B O   1 
ATOM   2143 C  CB  . LEU B 1 95  ? 0.048   -1.588  53.759  1.00 10.22 ? 83  LEU B CB  1 
ATOM   2144 C  CG  . LEU B 1 95  ? 0.254   -0.500  52.711  1.00 12.06 ? 83  LEU B CG  1 
ATOM   2145 C  CD1 . LEU B 1 95  ? -0.710  0.657   52.951  1.00 12.70 ? 83  LEU B CD1 1 
ATOM   2146 C  CD2 . LEU B 1 95  ? 1.699   -0.040  52.789  1.00 12.99 ? 83  LEU B CD2 1 
ATOM   2147 N  N   . VAL B 1 96  ? -2.487  -2.877  51.760  1.00 9.35  ? 84  VAL B N   1 
ATOM   2148 C  CA  . VAL B 1 96  ? -2.851  -3.613  50.557  1.00 9.40  ? 84  VAL B CA  1 
ATOM   2149 C  C   . VAL B 1 96  ? -3.257  -2.593  49.507  1.00 8.11  ? 84  VAL B C   1 
ATOM   2150 O  O   . VAL B 1 96  ? -3.986  -1.644  49.810  1.00 9.37  ? 84  VAL B O   1 
ATOM   2151 C  CB  . VAL B 1 96  ? -4.017  -4.594  50.805  1.00 10.67 ? 84  VAL B CB  1 
ATOM   2152 C  CG1 . VAL B 1 96  ? -4.472  -5.212  49.473  1.00 12.33 ? 84  VAL B CG1 1 
ATOM   2153 C  CG2 . VAL B 1 96  ? -3.636  -5.679  51.790  1.00 10.27 ? 84  VAL B CG2 1 
ATOM   2154 N  N   . GLU B 1 97  ? -2.776  -2.782  48.284  1.00 8.24  ? 85  GLU B N   1 
ATOM   2155 C  CA  . GLU B 1 97  ? -3.225  -2.035  47.115  1.00 7.52  ? 85  GLU B CA  1 
ATOM   2156 C  C   . GLU B 1 97  ? -4.025  -2.998  46.250  1.00 6.89  ? 85  GLU B C   1 
ATOM   2157 O  O   . GLU B 1 97  ? -3.576  -4.118  46.003  1.00 9.39  ? 85  GLU B O   1 
ATOM   2158 C  CB  . GLU B 1 97  ? -2.028  -1.476  46.340  1.00 7.93  ? 85  GLU B CB  1 
ATOM   2159 C  CG  . GLU B 1 97  ? -2.402  -0.758  45.041  1.00 11.27 ? 85  GLU B CG  1 
ATOM   2160 C  CD  . GLU B 1 97  ? -1.203  -0.250  44.256  1.00 12.82 ? 85  GLU B CD  1 
ATOM   2161 O  OE1 . GLU B 1 97  ? -1.205  0.945   43.878  1.00 15.29 ? 85  GLU B OE1 1 
ATOM   2162 O  OE2 . GLU B 1 97  ? -0.266  -1.029  43.999  1.00 14.25 ? 85  GLU B OE2 1 
ATOM   2163 N  N   . TYR B 1 98  ? -5.206  -2.587  45.792  1.00 6.50  ? 86  TYR B N   1 
ATOM   2164 C  CA  . TYR B 1 98  ? -6.017  -3.514  45.006  1.00 8.88  ? 86  TYR B CA  1 
ATOM   2165 C  C   . TYR B 1 98  ? -6.573  -2.866  43.745  1.00 9.91  ? 86  TYR B C   1 
ATOM   2166 O  O   . TYR B 1 98  ? -6.800  -1.653  43.686  1.00 8.78  ? 86  TYR B O   1 
ATOM   2167 C  CB  . TYR B 1 98  ? -7.167  -4.119  45.833  1.00 11.21 ? 86  TYR B CB  1 
ATOM   2168 C  CG  . TYR B 1 98  ? -8.210  -3.122  46.287  1.00 8.85  ? 86  TYR B CG  1 
ATOM   2169 C  CD1 . TYR B 1 98  ? -9.218  -2.691  45.419  1.00 8.85  ? 86  TYR B CD1 1 
ATOM   2170 C  CD2 . TYR B 1 98  ? -8.180  -2.599  47.571  1.00 9.20  ? 86  TYR B CD2 1 
ATOM   2171 C  CE1 . TYR B 1 98  ? -10.158 -1.764  45.838  1.00 10.41 ? 86  TYR B CE1 1 
ATOM   2172 C  CE2 . TYR B 1 98  ? -9.113  -1.677  47.997  1.00 9.39  ? 86  TYR B CE2 1 
ATOM   2173 C  CZ  . TYR B 1 98  ? -10.097 -1.266  47.133  1.00 8.88  ? 86  TYR B CZ  1 
ATOM   2174 O  OH  . TYR B 1 98  ? -11.028 -0.342  47.563  1.00 11.31 ? 86  TYR B OH  1 
ATOM   2175 N  N   . TYR B 1 99  ? -6.824  -3.714  42.743  1.00 8.77  ? 87  TYR B N   1 
ATOM   2176 C  CA  . TYR B 1 99  ? -7.332  -3.284  41.441  1.00 9.10  ? 87  TYR B CA  1 
ATOM   2177 C  C   . TYR B 1 99  ? -8.440  -4.230  41.006  1.00 10.01 ? 87  TYR B C   1 
ATOM   2178 O  O   . TYR B 1 99  ? -8.229  -5.446  40.970  1.00 12.14 ? 87  TYR B O   1 
ATOM   2179 C  CB  . TYR B 1 99  ? -6.232  -3.321  40.372  1.00 9.86  ? 87  TYR B CB  1 
ATOM   2180 C  CG  . TYR B 1 99  ? -5.241  -2.169  40.332  1.00 12.18 ? 87  TYR B CG  1 
ATOM   2181 C  CD1 . TYR B 1 99  ? -4.011  -2.244  40.991  1.00 17.89 ? 87  TYR B CD1 1 
ATOM   2182 C  CD2 . TYR B 1 99  ? -5.513  -1.035  39.586  1.00 16.43 ? 87  TYR B CD2 1 
ATOM   2183 C  CE1 . TYR B 1 99  ? -3.092  -1.186  40.915  1.00 13.76 ? 87  TYR B CE1 1 
ATOM   2184 C  CE2 . TYR B 1 99  ? -4.610  0.016   39.516  1.00 18.74 ? 87  TYR B CE2 1 
ATOM   2185 C  CZ  . TYR B 1 99  ? -3.408  -0.066  40.169  1.00 21.91 ? 87  TYR B CZ  1 
ATOM   2186 O  OH  . TYR B 1 99  ? -2.547  1.012   40.052  1.00 27.85 ? 87  TYR B OH  1 
ATOM   2187 N  N   . ILE B 1 100 ? -9.597  -3.679  40.650  1.00 7.84  ? 88  ILE B N   1 
ATOM   2188 C  CA  . ILE B 1 100 ? -10.641 -4.411  39.935  1.00 8.54  ? 88  ILE B CA  1 
ATOM   2189 C  C   . ILE B 1 100 ? -10.633 -3.835  38.527  1.00 8.77  ? 88  ILE B C   1 
ATOM   2190 O  O   . ILE B 1 100 ? -11.187 -2.757  38.275  1.00 8.52  ? 88  ILE B O   1 
ATOM   2191 C  CB  . ILE B 1 100 ? -12.013 -4.278  40.604  1.00 7.73  ? 88  ILE B CB  1 
ATOM   2192 C  CG1 . ILE B 1 100 ? -11.959 -4.828  42.032  1.00 8.91  ? 88  ILE B CG1 1 
ATOM   2193 C  CG2 . ILE B 1 100 ? -13.118 -4.971  39.759  1.00 8.83  ? 88  ILE B CG2 1 
ATOM   2194 C  CD1 . ILE B 1 100 ? -13.107 -4.314  42.914  1.00 10.35 ? 88  ILE B CD1 1 
ATOM   2195 N  N   . VAL B 1 101 ? -9.979  -4.542  37.611  1.00 8.64  ? 89  VAL B N   1 
ATOM   2196 C  CA  . VAL B 1 101 ? -9.672  -4.022  36.283  1.00 6.66  ? 89  VAL B CA  1 
ATOM   2197 C  C   . VAL B 1 101 ? -10.838 -4.313  35.351  1.00 9.32  ? 89  VAL B C   1 
ATOM   2198 O  O   . VAL B 1 101 ? -11.155 -5.476  35.092  1.00 10.50 ? 89  VAL B O   1 
ATOM   2199 C  CB  . VAL B 1 101 ? -8.383  -4.641  35.739  1.00 9.29  ? 89  VAL B CB  1 
ATOM   2200 C  CG1 . VAL B 1 101 ? -8.090  -4.107  34.318  1.00 8.68  ? 89  VAL B CG1 1 
ATOM   2201 C  CG2 . VAL B 1 101 ? -7.219  -4.336  36.712  1.00 7.88  ? 89  VAL B CG2 1 
ATOM   2202 N  N   . GLU B 1 102 ? -11.460 -3.253  34.838  1.00 8.27  ? 90  GLU B N   1 
ATOM   2203 C  CA  . GLU B 1 102 ? -12.586 -3.365  33.912  1.00 8.81  ? 90  GLU B CA  1 
ATOM   2204 C  C   . GLU B 1 102 ? -12.158 -3.427  32.449  1.00 10.45 ? 90  GLU B C   1 
ATOM   2205 O  O   . GLU B 1 102 ? -12.815 -4.107  31.649  1.00 11.00 ? 90  GLU B O   1 
ATOM   2206 C  CB  . GLU B 1 102 ? -13.535 -2.181  34.115  1.00 9.33  ? 90  GLU B CB  1 
ATOM   2207 C  CG  . GLU B 1 102 ? -14.193 -2.205  35.488  1.00 11.43 ? 90  GLU B CG  1 
ATOM   2208 C  CD  . GLU B 1 102 ? -15.130 -3.394  35.630  1.00 14.46 ? 90  GLU B CD  1 
ATOM   2209 O  OE1 . GLU B 1 102 ? -14.750 -4.388  36.278  1.00 19.53 ? 90  GLU B OE1 1 
ATOM   2210 O  OE2 . GLU B 1 102 ? -16.249 -3.341  35.079  1.00 18.65 ? 90  GLU B OE2 1 
ATOM   2211 N  N   . SER B 1 103 ? -11.090 -2.721  32.083  1.00 10.54 ? 91  SER B N   1 
ATOM   2212 C  CA  . SER B 1 103 ? -10.498 -2.773  30.753  1.00 9.07  ? 91  SER B CA  1 
ATOM   2213 C  C   . SER B 1 103 ? -9.005  -2.546  30.901  1.00 12.53 ? 91  SER B C   1 
ATOM   2214 O  O   . SER B 1 103 ? -8.585  -1.767  31.753  1.00 11.29 ? 91  SER B O   1 
ATOM   2215 C  CB  . SER B 1 103 ? -11.038 -1.685  29.824  1.00 12.09 ? 91  SER B CB  1 
ATOM   2216 O  OG  . SER B 1 103 ? -12.385 -1.910  29.457  1.00 15.80 ? 91  SER B OG  1 
ATOM   2217 N  N   . PHE B 1 104 ? -8.217  -3.196  30.057  1.00 10.08 ? 92  PHE B N   1 
ATOM   2218 C  CA  . PHE B 1 104 ? -6.829  -2.806  29.857  1.00 10.94 ? 92  PHE B CA  1 
ATOM   2219 C  C   . PHE B 1 104 ? -6.560  -2.801  28.362  1.00 12.10 ? 92  PHE B C   1 
ATOM   2220 O  O   . PHE B 1 104 ? -7.297  -3.407  27.577  1.00 12.78 ? 92  PHE B O   1 
ATOM   2221 C  CB  . PHE B 1 104 ? -5.832  -3.715  30.612  1.00 11.02 ? 92  PHE B CB  1 
ATOM   2222 C  CG  . PHE B 1 104 ? -5.793  -5.149  30.142  1.00 12.54 ? 92  PHE B CG  1 
ATOM   2223 C  CD1 . PHE B 1 104 ? -5.145  -5.503  28.959  1.00 12.91 ? 92  PHE B CD1 1 
ATOM   2224 C  CD2 . PHE B 1 104 ? -6.346  -6.151  30.920  1.00 13.88 ? 92  PHE B CD2 1 
ATOM   2225 C  CE1 . PHE B 1 104 ? -5.094  -6.828  28.544  1.00 15.06 ? 92  PHE B CE1 1 
ATOM   2226 C  CE2 . PHE B 1 104 ? -6.281  -7.486  30.521  1.00 15.17 ? 92  PHE B CE2 1 
ATOM   2227 C  CZ  . PHE B 1 104 ? -5.660  -7.818  29.318  1.00 13.50 ? 92  PHE B CZ  1 
ATOM   2228 N  N   . SER B 1 105 ? -5.515  -2.089  27.958  1.00 10.04 ? 93  SER B N   1 
ATOM   2229 C  CA  . SER B 1 105 ? -5.324  -1.931  26.525  1.00 12.94 ? 93  SER B CA  1 
ATOM   2230 C  C   . SER B 1 105 ? -4.331  -2.953  25.981  1.00 20.72 ? 93  SER B C   1 
ATOM   2231 O  O   . SER B 1 105 ? -4.719  -4.049  25.560  1.00 27.80 ? 93  SER B O   1 
ATOM   2232 C  CB  . SER B 1 105 ? -4.883  -0.505  26.193  1.00 16.61 ? 93  SER B CB  1 
ATOM   2233 O  OG  . SER B 1 105 ? -3.947  -0.036  27.139  1.00 22.43 ? 93  SER B OG  1 
ATOM   2234 N  N   . THR B 1 106 ? -3.054  -2.619  26.009  1.00 14.85 ? 94  THR B N   1 
ATOM   2235 C  CA  . THR B 1 106 ? -2.019  -3.382  25.324  1.00 11.45 ? 94  THR B CA  1 
ATOM   2236 C  C   . THR B 1 106 ? -1.196  -4.273  26.250  1.00 14.06 ? 94  THR B C   1 
ATOM   2237 O  O   . THR B 1 106 ? -0.330  -5.020  25.766  1.00 14.73 ? 94  THR B O   1 
ATOM   2238 C  CB  . THR B 1 106 ? -1.085  -2.416  24.580  1.00 14.74 ? 94  THR B CB  1 
ATOM   2239 O  OG1 . THR B 1 106 ? -0.523  -1.480  25.506  1.00 16.67 ? 94  THR B OG1 1 
ATOM   2240 C  CG2 . THR B 1 106 ? -1.849  -1.642  23.523  1.00 15.48 ? 94  THR B CG2 1 
ATOM   2241 N  N   . TYR B 1 107 ? -1.435  -4.224  27.557  1.00 11.81 ? 95  TYR B N   1 
ATOM   2242 C  CA  . TYR B 1 107 ? -0.617  -4.962  28.513  1.00 10.21 ? 95  TYR B CA  1 
ATOM   2243 C  C   . TYR B 1 107 ? -1.505  -5.420  29.654  1.00 11.22 ? 95  TYR B C   1 
ATOM   2244 O  O   . TYR B 1 107 ? -2.195  -4.601  30.269  1.00 12.01 ? 95  TYR B O   1 
ATOM   2245 C  CB  . TYR B 1 107 ? 0.527   -4.088  29.065  1.00 11.73 ? 95  TYR B CB  1 
ATOM   2246 C  CG  . TYR B 1 107 ? 1.439   -4.803  30.038  1.00 12.75 ? 95  TYR B CG  1 
ATOM   2247 C  CD1 . TYR B 1 107 ? 2.351   -5.749  29.592  1.00 13.08 ? 95  TYR B CD1 1 
ATOM   2248 C  CD2 . TYR B 1 107 ? 1.396   -4.528  31.405  1.00 14.63 ? 95  TYR B CD2 1 
ATOM   2249 C  CE1 . TYR B 1 107 ? 3.195   -6.413  30.472  1.00 13.58 ? 95  TYR B CE1 1 
ATOM   2250 C  CE2 . TYR B 1 107 ? 2.237   -5.178  32.292  1.00 14.23 ? 95  TYR B CE2 1 
ATOM   2251 C  CZ  . TYR B 1 107 ? 3.137   -6.116  31.823  1.00 13.96 ? 95  TYR B CZ  1 
ATOM   2252 O  OH  . TYR B 1 107 ? 3.974   -6.768  32.697  1.00 16.24 ? 95  TYR B OH  1 
ATOM   2253 N  N   . ASP B 1 108 ? -1.501  -6.717  29.923  1.00 10.53 ? 96  ASP B N   1 
ATOM   2254 C  CA  . ASP B 1 108 ? -2.297  -7.236  31.022  1.00 11.99 ? 96  ASP B CA  1 
ATOM   2255 C  C   . ASP B 1 108 ? -1.548  -6.916  32.310  1.00 14.74 ? 96  ASP B C   1 
ATOM   2256 O  O   . ASP B 1 108 ? -0.475  -7.476  32.548  1.00 14.44 ? 96  ASP B O   1 
ATOM   2257 C  CB  . ASP B 1 108 ? -2.526  -8.739  30.837  1.00 13.40 ? 96  ASP B CB  1 
ATOM   2258 C  CG  . ASP B 1 108 ? -3.425  -9.332  31.896  1.00 16.33 ? 96  ASP B CG  1 
ATOM   2259 O  OD1 . ASP B 1 108 ? -3.537  -8.752  33.004  1.00 17.21 ? 96  ASP B OD1 1 
ATOM   2260 O  OD2 . ASP B 1 108 ? -4.008  -10.394 31.619  1.00 17.80 ? 96  ASP B OD2 1 
ATOM   2261 N  N   . PRO B 1 109 ? -2.065  -6.005  33.142  1.00 14.20 ? 97  PRO B N   1 
ATOM   2262 C  CA  . PRO B 1 109 ? -1.292  -5.552  34.311  1.00 17.86 ? 97  PRO B CA  1 
ATOM   2263 C  C   . PRO B 1 109 ? -1.131  -6.613  35.378  1.00 16.60 ? 97  PRO B C   1 
ATOM   2264 O  O   . PRO B 1 109 ? -0.326  -6.417  36.299  1.00 18.81 ? 97  PRO B O   1 
ATOM   2265 C  CB  . PRO B 1 109 ? -2.100  -4.353  34.825  1.00 17.20 ? 97  PRO B CB  1 
ATOM   2266 C  CG  . PRO B 1 109 ? -3.512  -4.655  34.411  1.00 14.57 ? 97  PRO B CG  1 
ATOM   2267 C  CD  . PRO B 1 109 ? -3.395  -5.362  33.063  1.00 14.24 ? 97  PRO B CD  1 
ATOM   2268 N  N   . SER B 1 110 ? -1.852  -7.730  35.285  1.00 17.28 ? 98  SER B N   1 
ATOM   2269 C  CA  . SER B 1 110 ? -1.636  -8.847  36.194  1.00 18.50 ? 98  SER B CA  1 
ATOM   2270 C  C   . SER B 1 110 ? -0.446  -9.710  35.790  1.00 20.94 ? 98  SER B C   1 
ATOM   2271 O  O   . SER B 1 110 ? -0.127  -10.668 36.506  1.00 17.90 ? 98  SER B O   1 
ATOM   2272 C  CB  . SER B 1 110 ? -2.901  -9.712  36.272  1.00 15.95 ? 98  SER B CB  1 
ATOM   2273 O  OG  . SER B 1 110 ? -3.107  -10.411 35.064  1.00 18.56 ? 98  SER B OG  1 
ATOM   2274 N  N   . THR B 1 111 ? 0.199   -9.410  34.660  1.00 18.40 ? 99  THR B N   1 
ATOM   2275 C  CA  . THR B 1 111 ? 1.366   -10.172 34.237  1.00 16.58 ? 99  THR B CA  1 
ATOM   2276 C  C   . THR B 1 111 ? 2.408   -10.172 35.348  1.00 18.22 ? 99  THR B C   1 
ATOM   2277 O  O   . THR B 1 111 ? 2.714   -9.125  35.926  1.00 19.08 ? 99  THR B O   1 
ATOM   2278 C  CB  . THR B 1 111 ? 1.957   -9.573  32.958  1.00 15.64 ? 99  THR B CB  1 
ATOM   2279 O  OG1 . THR B 1 111 ? 0.951   -9.541  31.938  1.00 14.36 ? 99  THR B OG1 1 
ATOM   2280 C  CG2 . THR B 1 111 ? 3.133   -10.422 32.458  1.00 17.81 ? 99  THR B CG2 1 
ATOM   2281 N  N   . GLY B 1 112 ? 2.932   -11.353 35.657  1.00 16.00 ? 100 GLY B N   1 
ATOM   2282 C  CA  . GLY B 1 112 ? 3.884   -11.506 36.740  1.00 18.49 ? 100 GLY B CA  1 
ATOM   2283 C  C   . GLY B 1 112 ? 3.276   -11.804 38.096  1.00 21.20 ? 100 GLY B C   1 
ATOM   2284 O  O   . GLY B 1 112 ? 4.008   -12.207 39.010  1.00 22.69 ? 100 GLY B O   1 
ATOM   2285 N  N   . ALA B 1 113 ? 1.970   -11.618 38.265  1.00 18.40 ? 101 ALA B N   1 
ATOM   2286 C  CA  . ALA B 1 113 ? 1.312   -11.951 39.521  1.00 13.59 ? 101 ALA B CA  1 
ATOM   2287 C  C   . ALA B 1 113 ? 0.857   -13.410 39.502  1.00 17.30 ? 101 ALA B C   1 
ATOM   2288 O  O   . ALA B 1 113 ? 0.757   -14.037 38.447  1.00 23.57 ? 101 ALA B O   1 
ATOM   2289 C  CB  . ALA B 1 113 ? 0.125   -11.012 39.772  1.00 14.08 ? 101 ALA B CB  1 
ATOM   2290 N  N   . GLN B 1 114 ? 0.598   -13.953 40.695  1.00 18.01 ? 102 GLN B N   1 
ATOM   2291 C  CA  . GLN B 1 114 ? 0.181   -15.345 40.845  1.00 17.59 ? 102 GLN B CA  1 
ATOM   2292 C  C   . GLN B 1 114 ? -1.334  -15.472 40.754  1.00 16.84 ? 102 GLN B C   1 
ATOM   2293 O  O   . GLN B 1 114 ? -2.067  -14.835 41.516  1.00 14.37 ? 102 GLN B O   1 
ATOM   2294 C  CB  . GLN B 1 114 ? 0.657   -15.927 42.177  1.00 24.34 ? 102 GLN B CB  1 
ATOM   2295 C  CG  . GLN B 1 114 ? 2.169   -16.055 42.310  1.00 28.92 ? 102 GLN B CG  1 
ATOM   2296 C  CD  . GLN B 1 114 ? 2.804   -16.914 41.223  1.00 36.50 ? 102 GLN B CD  1 
ATOM   2297 O  OE1 . GLN B 1 114 ? 3.998   -16.786 40.950  1.00 44.08 ? 102 GLN B OE1 1 
ATOM   2298 N  NE2 . GLN B 1 114 ? 2.017   -17.802 40.609  1.00 36.42 ? 102 GLN B NE2 1 
ATOM   2299 N  N   . GLU B 1 115 ? -1.797  -16.318 39.836  1.00 17.41 ? 103 GLU B N   1 
ATOM   2300 C  CA  . GLU B 1 115 ? -3.224  -16.534 39.653  1.00 19.49 ? 103 GLU B CA  1 
ATOM   2301 C  C   . GLU B 1 115 ? -3.779  -17.399 40.777  1.00 19.39 ? 103 GLU B C   1 
ATOM   2302 O  O   . GLU B 1 115 ? -3.136  -18.358 41.213  1.00 25.02 ? 103 GLU B O   1 
ATOM   2303 C  CB  . GLU B 1 115 ? -3.485  -17.196 38.301  1.00 20.39 ? 103 GLU B CB  1 
ATOM   2304 C  CG  . GLU B 1 115 ? -4.910  -17.084 37.833  1.00 23.77 ? 103 GLU B CG  1 
ATOM   2305 C  CD  . GLU B 1 115 ? -5.057  -17.392 36.356  1.00 26.65 ? 103 GLU B CD  1 
ATOM   2306 O  OE1 . GLU B 1 115 ? -6.213  -17.501 35.891  1.00 30.30 ? 103 GLU B OE1 1 
ATOM   2307 O  OE2 . GLU B 1 115 ? -4.022  -17.529 35.664  1.00 33.80 ? 103 GLU B OE2 1 
ATOM   2308 N  N   . LEU B 1 116 ? -4.985  -17.058 41.241  1.00 16.57 ? 104 LEU B N   1 
ATOM   2309 C  CA  . LEU B 1 116 ? -5.600  -17.699 42.397  1.00 20.71 ? 104 LEU B CA  1 
ATOM   2310 C  C   . LEU B 1 116 ? -6.952  -18.340 42.126  1.00 23.20 ? 104 LEU B C   1 
ATOM   2311 O  O   . LEU B 1 116 ? -7.354  -19.219 42.896  1.00 31.47 ? 104 LEU B O   1 
ATOM   2312 C  CB  . LEU B 1 116 ? -5.803  -16.688 43.539  1.00 24.71 ? 104 LEU B CB  1 
ATOM   2313 C  CG  . LEU B 1 116 ? -4.639  -16.099 44.325  1.00 25.84 ? 104 LEU B CG  1 
ATOM   2314 C  CD1 . LEU B 1 116 ? -4.657  -14.606 44.240  1.00 23.85 ? 104 LEU B CD1 1 
ATOM   2315 C  CD2 . LEU B 1 116 ? -4.778  -16.521 45.776  1.00 31.70 ? 104 LEU B CD2 1 
ATOM   2316 N  N   . GLY B 1 117 ? -7.665  -17.930 41.089  1.00 21.40 ? 105 GLY B N   1 
ATOM   2317 C  CA  . GLY B 1 117 ? -9.015  -18.406 40.850  1.00 21.01 ? 105 GLY B CA  1 
ATOM   2318 C  C   . GLY B 1 117 ? -9.801  -17.365 40.071  1.00 19.57 ? 105 GLY B C   1 
ATOM   2319 O  O   . GLY B 1 117 ? -9.217  -16.509 39.413  1.00 17.82 ? 105 GLY B O   1 
ATOM   2320 N  N   . THR B 1 118 ? -11.133 -17.472 40.142  1.00 19.93 ? 106 THR B N   1 
ATOM   2321 C  CA  . THR B 1 118 ? -12.029 -16.569 39.426  1.00 18.66 ? 106 THR B CA  1 
ATOM   2322 C  C   . THR B 1 118 ? -13.200 -16.175 40.315  1.00 20.25 ? 106 THR B C   1 
ATOM   2323 O  O   . THR B 1 118 ? -13.491 -16.818 41.329  1.00 20.43 ? 106 THR B O   1 
ATOM   2324 C  CB  . THR B 1 118 ? -12.605 -17.182 38.129  1.00 22.28 ? 106 THR B CB  1 
ATOM   2325 O  OG1 . THR B 1 118 ? -13.406 -18.325 38.450  1.00 23.35 ? 106 THR B OG1 1 
ATOM   2326 C  CG2 . THR B 1 118 ? -11.506 -17.582 37.146  1.00 20.86 ? 106 THR B CG2 1 
ATOM   2327 N  N   . VAL B 1 119 ? -13.883 -15.108 39.912  1.00 16.07 ? 107 VAL B N   1 
ATOM   2328 C  CA  . VAL B 1 119 ? -15.128 -14.695 40.544  1.00 17.06 ? 107 VAL B CA  1 
ATOM   2329 C  C   . VAL B 1 119 ? -16.071 -14.210 39.449  1.00 17.05 ? 107 VAL B C   1 
ATOM   2330 O  O   . VAL B 1 119 ? -15.653 -13.499 38.529  1.00 16.94 ? 107 VAL B O   1 
ATOM   2331 C  CB  . VAL B 1 119 ? -14.883 -13.613 41.623  1.00 18.37 ? 107 VAL B CB  1 
ATOM   2332 C  CG1 . VAL B 1 119 ? -14.101 -12.436 41.051  1.00 15.31 ? 107 VAL B CG1 1 
ATOM   2333 C  CG2 . VAL B 1 119 ? -16.198 -13.159 42.265  1.00 17.15 ? 107 VAL B CG2 1 
ATOM   2334 N  N   . GLU B 1 120 ? -17.328 -14.636 39.517  1.00 15.04 ? 108 GLU B N   1 
ATOM   2335 C  CA  . GLU B 1 120 ? -18.356 -14.188 38.583  1.00 19.10 ? 108 GLU B CA  1 
ATOM   2336 C  C   . GLU B 1 120 ? -19.204 -13.117 39.258  1.00 19.07 ? 108 GLU B C   1 
ATOM   2337 O  O   . GLU B 1 120 ? -19.800 -13.364 40.312  1.00 19.26 ? 108 GLU B O   1 
ATOM   2338 C  CB  . GLU B 1 120 ? -19.224 -15.361 38.129  1.00 22.27 ? 108 GLU B CB  1 
ATOM   2339 C  CG  . GLU B 1 120 ? -18.445 -16.640 37.900  1.00 25.66 ? 108 GLU B CG  1 
ATOM   2340 C  CD  . GLU B 1 120 ? -18.009 -16.797 36.454  1.00 36.94 ? 108 GLU B CD  1 
ATOM   2341 O  OE1 . GLU B 1 120 ? -17.510 -17.887 36.089  1.00 49.89 ? 108 GLU B OE1 1 
ATOM   2342 O  OE2 . GLU B 1 120 ? -18.168 -15.831 35.678  1.00 41.16 ? 108 GLU B OE2 1 
ATOM   2343 N  N   . THR B 1 121 ? -19.252 -11.933 38.657  1.00 18.47 ? 109 THR B N   1 
ATOM   2344 C  CA  . THR B 1 121 ? -20.009 -10.829 39.226  1.00 17.51 ? 109 THR B CA  1 
ATOM   2345 C  C   . THR B 1 121 ? -20.262 -9.807  38.128  1.00 16.12 ? 109 THR B C   1 
ATOM   2346 O  O   . THR B 1 121 ? -19.459 -9.664  37.202  1.00 14.28 ? 109 THR B O   1 
ATOM   2347 C  CB  . THR B 1 121 ? -19.271 -10.206 40.428  1.00 21.26 ? 109 THR B CB  1 
ATOM   2348 O  OG1 . THR B 1 121 ? -19.999 -9.079  40.940  1.00 20.13 ? 109 THR B OG1 1 
ATOM   2349 C  CG2 . THR B 1 121 ? -17.853 -9.783  40.052  1.00 16.00 ? 109 THR B CG2 1 
ATOM   2350 N  N   . ASP B 1 122 ? -21.400 -9.123  38.230  1.00 16.69 ? 110 ASP B N   1 
ATOM   2351 C  CA  . ASP B 1 122 ? -21.734 -8.012  37.335  1.00 15.55 ? 110 ASP B CA  1 
ATOM   2352 C  C   . ASP B 1 122 ? -21.624 -8.422  35.869  1.00 17.48 ? 110 ASP B C   1 
ATOM   2353 O  O   . ASP B 1 122 ? -21.006 -7.742  35.049  1.00 15.14 ? 110 ASP B O   1 
ATOM   2354 C  CB  . ASP B 1 122 ? -20.856 -6.802  37.648  1.00 15.87 ? 110 ASP B CB  1 
ATOM   2355 C  CG  . ASP B 1 122 ? -20.967 -6.393  39.101  1.00 15.94 ? 110 ASP B CG  1 
ATOM   2356 O  OD1 . ASP B 1 122 ? -22.096 -6.030  39.518  1.00 15.83 ? 110 ASP B OD1 1 
ATOM   2357 O  OD2 . ASP B 1 122 ? -19.949 -6.474  39.831  1.00 16.48 ? 110 ASP B OD2 1 
ATOM   2358 N  N   . ASP B 1 123 ? -22.227 -9.572  35.558  1.00 17.11 ? 111 ASP B N   1 
ATOM   2359 C  CA  . ASP B 1 123 ? -22.358 -10.090 34.200  1.00 19.38 ? 111 ASP B CA  1 
ATOM   2360 C  C   . ASP B 1 123 ? -21.012 -10.376 33.542  1.00 20.85 ? 111 ASP B C   1 
ATOM   2361 O  O   . ASP B 1 123 ? -20.918 -10.433 32.311  1.00 24.25 ? 111 ASP B O   1 
ATOM   2362 C  CB  . ASP B 1 123 ? -23.194 -9.138  33.339  1.00 22.07 ? 111 ASP B CB  1 
ATOM   2363 C  CG  . ASP B 1 123 ? -24.593 -8.946  33.896  1.00 33.92 ? 111 ASP B CG  1 
ATOM   2364 O  OD1 . ASP B 1 123 ? -25.456 -9.825  33.674  1.00 36.41 ? 111 ASP B OD1 1 
ATOM   2365 O  OD2 . ASP B 1 123 ? -24.821 -7.926  34.584  1.00 34.22 ? 111 ASP B OD2 1 
ATOM   2366 N  N   . GLY B 1 124 ? -19.969 -10.593 34.345  1.00 19.23 ? 112 GLY B N   1 
ATOM   2367 C  CA  . GLY B 1 124 ? -18.656 -10.899 33.822  1.00 21.61 ? 112 GLY B CA  1 
ATOM   2368 C  C   . GLY B 1 124 ? -17.949 -11.940 34.668  1.00 17.68 ? 112 GLY B C   1 
ATOM   2369 O  O   . GLY B 1 124 ? -18.460 -12.401 35.690  1.00 19.83 ? 112 GLY B O   1 
ATOM   2370 N  N   . THR B 1 125 ? -16.764 -12.302 34.208  1.00 14.47 ? 113 THR B N   1 
ATOM   2371 C  CA  . THR B 1 125 ? -15.885 -13.234 34.890  1.00 15.00 ? 113 THR B CA  1 
ATOM   2372 C  C   . THR B 1 125 ? -14.565 -12.519 35.113  1.00 13.54 ? 113 THR B C   1 
ATOM   2373 O  O   . THR B 1 125 ? -14.072 -11.824 34.219  1.00 13.90 ? 113 THR B O   1 
ATOM   2374 C  CB  . THR B 1 125 ? -15.668 -14.508 34.059  1.00 20.83 ? 113 THR B CB  1 
ATOM   2375 O  OG1 . THR B 1 125 ? -16.933 -15.151 33.835  1.00 23.73 ? 113 THR B OG1 1 
ATOM   2376 C  CG2 . THR B 1 125 ? -14.733 -15.466 34.768  1.00 22.06 ? 113 THR B CG2 1 
ATOM   2377 N  N   . TYR B 1 126 ? -14.007 -12.663 36.311  1.00 13.37 ? 114 TYR B N   1 
ATOM   2378 C  CA  . TYR B 1 126 ? -12.756 -12.009 36.652  1.00 12.74 ? 114 TYR B CA  1 
ATOM   2379 C  C   . TYR B 1 126 ? -11.758 -13.051 37.123  1.00 13.73 ? 114 TYR B C   1 
ATOM   2380 O  O   . TYR B 1 126 ? -12.095 -13.917 37.933  1.00 15.86 ? 114 TYR B O   1 
ATOM   2381 C  CB  . TYR B 1 126 ? -12.937 -10.970 37.774  1.00 15.13 ? 114 TYR B CB  1 
ATOM   2382 C  CG  . TYR B 1 126 ? -13.798 -9.785  37.434  1.00 13.46 ? 114 TYR B CG  1 
ATOM   2383 C  CD1 . TYR B 1 126 ? -15.181 -9.915  37.306  1.00 11.05 ? 114 TYR B CD1 1 
ATOM   2384 C  CD2 . TYR B 1 126 ? -13.230 -8.529  37.245  1.00 11.16 ? 114 TYR B CD2 1 
ATOM   2385 C  CE1 . TYR B 1 126 ? -15.976 -8.817  36.995  1.00 10.19 ? 114 TYR B CE1 1 
ATOM   2386 C  CE2 . TYR B 1 126 ? -14.012 -7.428  36.955  1.00 9.53  ? 114 TYR B CE2 1 
ATOM   2387 C  CZ  . TYR B 1 126 ? -15.381 -7.581  36.815  1.00 7.62  ? 114 TYR B CZ  1 
ATOM   2388 O  OH  . TYR B 1 126 ? -16.151 -6.471  36.519  1.00 10.34 ? 114 TYR B OH  1 
ATOM   2389 N  N   . LYS B 1 127 ? -10.531 -12.949 36.636  1.00 12.21 ? 115 LYS B N   1 
ATOM   2390 C  CA  . LYS B 1 127 ? -9.437  -13.756 37.148  1.00 10.94 ? 115 LYS B CA  1 
ATOM   2391 C  C   . LYS B 1 127 ? -8.771  -13.014 38.297  1.00 11.70 ? 115 LYS B C   1 
ATOM   2392 O  O   . LYS B 1 127 ? -8.529  -11.804 38.211  1.00 11.75 ? 115 LYS B O   1 
ATOM   2393 C  CB  . LYS B 1 127 ? -8.416  -14.055 36.052  1.00 12.60 ? 115 LYS B CB  1 
ATOM   2394 C  CG  . LYS B 1 127 ? -8.972  -14.956 34.961  1.00 16.63 ? 115 LYS B CG  1 
ATOM   2395 C  CD  . LYS B 1 127 ? -7.931  -15.289 33.942  1.00 18.60 ? 115 LYS B CD  1 
ATOM   2396 C  CE  . LYS B 1 127 ? -8.552  -16.158 32.881  1.00 25.17 ? 115 LYS B CE  1 
ATOM   2397 N  NZ  . LYS B 1 127 ? -7.507  -16.344 31.884  1.00 30.68 ? 115 LYS B NZ  1 
ATOM   2398 N  N   . ILE B 1 128 ? -8.476  -13.748 39.368  1.00 10.47 ? 116 ILE B N   1 
ATOM   2399 C  CA  . ILE B 1 128 ? -7.942  -13.172 40.600  1.00 11.11 ? 116 ILE B CA  1 
ATOM   2400 C  C   . ILE B 1 128 ? -6.459  -13.491 40.701  1.00 13.59 ? 116 ILE B C   1 
ATOM   2401 O  O   . ILE B 1 128 ? -6.045  -14.624 40.434  1.00 12.37 ? 116 ILE B O   1 
ATOM   2402 C  CB  . ILE B 1 128 ? -8.684  -13.701 41.843  1.00 12.19 ? 116 ILE B CB  1 
ATOM   2403 C  CG1 . ILE B 1 128 ? -10.170 -13.349 41.791  1.00 15.68 ? 116 ILE B CG1 1 
ATOM   2404 C  CG2 . ILE B 1 128 ? -8.065  -13.142 43.113  1.00 15.46 ? 116 ILE B CG2 1 
ATOM   2405 C  CD1 . ILE B 1 128 ? -11.001 -14.257 42.682  1.00 19.95 ? 116 ILE B CD1 1 
ATOM   2406 N  N   . TYR B 1 129 ? -5.665  -12.499 41.132  1.00 10.61 ? 117 TYR B N   1 
ATOM   2407 C  CA  . TYR B 1 129 ? -4.220  -12.640 41.262  1.00 9.99  ? 117 TYR B CA  1 
ATOM   2408 C  C   . TYR B 1 129 ? -3.737  -11.915 42.509  1.00 12.98 ? 117 TYR B C   1 
ATOM   2409 O  O   . TYR B 1 129 ? -4.386  -10.998 43.012  1.00 10.27 ? 117 TYR B O   1 
ATOM   2410 C  CB  . TYR B 1 129 ? -3.437  -12.055 40.075  1.00 9.73  ? 117 TYR B CB  1 
ATOM   2411 C  CG  . TYR B 1 129 ? -3.885  -12.484 38.699  1.00 13.35 ? 117 TYR B CG  1 
ATOM   2412 C  CD1 . TYR B 1 129 ? -5.005  -11.909 38.106  1.00 9.46  ? 117 TYR B CD1 1 
ATOM   2413 C  CD2 . TYR B 1 129 ? -3.168  -13.435 37.978  1.00 16.11 ? 117 TYR B CD2 1 
ATOM   2414 C  CE1 . TYR B 1 129 ? -5.411  -12.289 36.843  1.00 14.45 ? 117 TYR B CE1 1 
ATOM   2415 C  CE2 . TYR B 1 129 ? -3.577  -13.821 36.696  1.00 17.54 ? 117 TYR B CE2 1 
ATOM   2416 C  CZ  . TYR B 1 129 ? -4.699  -13.241 36.146  1.00 15.98 ? 117 TYR B CZ  1 
ATOM   2417 O  OH  . TYR B 1 129 ? -5.122  -13.594 34.879  1.00 16.46 ? 117 TYR B OH  1 
ATOM   2418 N  N   . GLN B 1 130 ? -2.561  -12.314 42.985  1.00 11.48 ? 118 GLN B N   1 
ATOM   2419 C  CA  . GLN B 1 130 ? -1.880  -11.561 44.026  1.00 12.54 ? 118 GLN B CA  1 
ATOM   2420 C  C   . GLN B 1 130 ? -0.403  -11.468 43.689  1.00 14.40 ? 118 GLN B C   1 
ATOM   2421 O  O   . GLN B 1 130 ? 0.166   -12.352 43.045  1.00 14.51 ? 118 GLN B O   1 
ATOM   2422 C  CB  . GLN B 1 130 ? -2.078  -12.193 45.415  1.00 15.14 ? 118 GLN B CB  1 
ATOM   2423 C  CG  . GLN B 1 130 ? -1.292  -13.469 45.675  1.00 21.52 ? 118 GLN B CG  1 
ATOM   2424 C  CD  . GLN B 1 130 ? -1.266  -13.843 47.158  1.00 26.68 ? 118 GLN B CD  1 
ATOM   2425 O  OE1 . GLN B 1 130 ? -1.499  -14.999 47.532  1.00 32.65 ? 118 GLN B OE1 1 
ATOM   2426 N  NE2 . GLN B 1 130 ? -1.008  -12.859 48.009  1.00 22.34 ? 118 GLN B NE2 1 
ATOM   2427 N  N   . THR B 1 131 ? 0.212   -10.376 44.120  1.00 14.66 ? 119 THR B N   1 
ATOM   2428 C  CA  . THR B 1 131 ? 1.655   -10.247 44.055  1.00 16.92 ? 119 THR B CA  1 
ATOM   2429 C  C   . THR B 1 131 ? 2.082   -9.327  45.186  1.00 14.71 ? 119 THR B C   1 
ATOM   2430 O  O   . THR B 1 131 ? 1.282   -8.966  46.053  1.00 16.58 ? 119 THR B O   1 
ATOM   2431 C  CB  . THR B 1 131 ? 2.111   -9.745  42.680  1.00 18.50 ? 119 THR B CB  1 
ATOM   2432 O  OG1 . THR B 1 131 ? 3.552   -9.752  42.620  1.00 20.49 ? 119 THR B OG1 1 
ATOM   2433 C  CG2 . THR B 1 131 ? 1.577   -8.326  42.413  1.00 17.80 ? 119 THR B CG2 1 
ATOM   2434 N  N   . THR B 1 132 ? 3.358   -8.969  45.199  1.00 19.18 ? 120 THR B N   1 
ATOM   2435 C  CA  . THR B 1 132 ? 3.887   -8.070  46.207  1.00 20.54 ? 120 THR B CA  1 
ATOM   2436 C  C   . THR B 1 132 ? 4.620   -6.947  45.495  1.00 20.50 ? 120 THR B C   1 
ATOM   2437 O  O   . THR B 1 132 ? 5.187   -7.143  44.418  1.00 22.32 ? 120 THR B O   1 
ATOM   2438 C  CB  . THR B 1 132 ? 4.819   -8.813  47.190  1.00 24.46 ? 120 THR B CB  1 
ATOM   2439 O  OG1 . THR B 1 132 ? 4.059   -9.797  47.904  1.00 32.17 ? 120 THR B OG1 1 
ATOM   2440 C  CG2 . THR B 1 132 ? 5.444   -7.859  48.203  1.00 27.46 ? 120 THR B CG2 1 
ATOM   2441 N  N   . ARG B 1 133 ? 4.552   -5.756  46.073  1.00 14.44 ? 121 ARG B N   1 
ATOM   2442 C  CA  . ARG B 1 133 ? 5.335   -4.616  45.623  1.00 14.70 ? 121 ARG B CA  1 
ATOM   2443 C  C   . ARG B 1 133 ? 6.376   -4.325  46.691  1.00 18.23 ? 121 ARG B C   1 
ATOM   2444 O  O   . ARG B 1 133 ? 6.040   -4.294  47.876  1.00 15.87 ? 121 ARG B O   1 
ATOM   2445 C  CB  . ARG B 1 133 ? 4.435   -3.404  45.382  1.00 15.01 ? 121 ARG B CB  1 
ATOM   2446 C  CG  . ARG B 1 133 ? 3.415   -3.641  44.268  1.00 18.30 ? 121 ARG B CG  1 
ATOM   2447 C  CD  . ARG B 1 133 ? 3.965   -3.246  42.894  1.00 20.54 ? 121 ARG B CD  1 
ATOM   2448 N  NE  . ARG B 1 133 ? 4.066   -1.798  42.750  1.00 18.50 ? 121 ARG B NE  1 
ATOM   2449 C  CZ  . ARG B 1 133 ? 5.194   -1.143  42.498  1.00 21.18 ? 121 ARG B CZ  1 
ATOM   2450 N  NH1 . ARG B 1 133 ? 6.333   -1.807  42.352  1.00 26.15 ? 121 ARG B NH1 1 
ATOM   2451 N  NH2 . ARG B 1 133 ? 5.179   0.180   42.402  1.00 21.50 ? 121 ARG B NH2 1 
ATOM   2452 N  N   . GLU B 1 134 ? 7.634   -4.158  46.283  1.00 17.39 ? 122 GLU B N   1 
ATOM   2453 C  CA  . GLU B 1 134 ? 8.748   -3.993  47.215  1.00 18.10 ? 122 GLU B CA  1 
ATOM   2454 C  C   . GLU B 1 134 ? 9.308   -2.584  47.112  1.00 17.02 ? 122 GLU B C   1 
ATOM   2455 O  O   . GLU B 1 134 ? 9.586   -2.108  46.008  1.00 20.71 ? 122 GLU B O   1 
ATOM   2456 C  CB  . GLU B 1 134 ? 9.859   -5.010  46.932  1.00 22.26 ? 122 GLU B CB  1 
ATOM   2457 C  CG  . GLU B 1 134 ? 9.358   -6.441  46.773  1.00 32.62 ? 122 GLU B CG  1 
ATOM   2458 C  CD  . GLU B 1 134 ? 10.432  -7.466  47.064  1.00 46.76 ? 122 GLU B CD  1 
ATOM   2459 O  OE1 . GLU B 1 134 ? 10.676  -7.748  48.257  1.00 50.33 ? 122 GLU B OE1 1 
ATOM   2460 O  OE2 . GLU B 1 134 ? 11.034  -7.985  46.099  1.00 51.85 ? 122 GLU B OE2 1 
ATOM   2461 N  N   . ASN B 1 135 ? 9.460   -1.920  48.261  1.00 16.66 ? 123 ASN B N   1 
ATOM   2462 C  CA  . ASN B 1 135 ? 10.059  -0.587  48.329  1.00 15.33 ? 123 ASN B CA  1 
ATOM   2463 C  C   . ASN B 1 135 ? 9.424   0.353   47.307  1.00 21.21 ? 123 ASN B C   1 
ATOM   2464 O  O   . ASN B 1 135 ? 10.104  0.983   46.497  1.00 19.42 ? 123 ASN B O   1 
ATOM   2465 C  CB  . ASN B 1 135 ? 11.577  -0.673  48.134  1.00 21.08 ? 123 ASN B CB  1 
ATOM   2466 C  CG  . ASN B 1 135 ? 12.207  -1.720  49.023  1.00 26.48 ? 123 ASN B CG  1 
ATOM   2467 O  OD1 . ASN B 1 135 ? 12.193  -1.587  50.247  1.00 27.84 ? 123 ASN B OD1 1 
ATOM   2468 N  ND2 . ASN B 1 135 ? 12.734  -2.788  48.419  1.00 27.28 ? 123 ASN B ND2 1 
ATOM   2469 N  N   . ALA B 1 136 ? 8.102   0.439   47.351  1.00 15.69 ? 124 ALA B N   1 
ATOM   2470 C  CA  . ALA B 1 136 ? 7.317   1.093   46.320  1.00 15.92 ? 124 ALA B CA  1 
ATOM   2471 C  C   . ALA B 1 136 ? 6.512   2.239   46.907  1.00 18.49 ? 124 ALA B C   1 
ATOM   2472 O  O   . ALA B 1 136 ? 6.236   2.262   48.113  1.00 14.41 ? 124 ALA B O   1 
ATOM   2473 C  CB  . ALA B 1 136 ? 6.366   0.084   45.663  1.00 15.34 ? 124 ALA B CB  1 
ATOM   2474 N  N   . PRO B 1 137 ? 6.097   3.202   46.082  1.00 15.84 ? 125 PRO B N   1 
ATOM   2475 C  CA  . PRO B 1 137 ? 5.211   4.257   46.585  1.00 13.44 ? 125 PRO B CA  1 
ATOM   2476 C  C   . PRO B 1 137 ? 3.921   3.674   47.135  1.00 13.63 ? 125 PRO B C   1 
ATOM   2477 O  O   . PRO B 1 137 ? 3.391   2.690   46.614  1.00 13.90 ? 125 PRO B O   1 
ATOM   2478 C  CB  . PRO B 1 137 ? 4.946   5.124   45.346  1.00 19.44 ? 125 PRO B CB  1 
ATOM   2479 C  CG  . PRO B 1 137 ? 6.087   4.842   44.427  1.00 18.61 ? 125 PRO B CG  1 
ATOM   2480 C  CD  . PRO B 1 137 ? 6.523   3.441   44.691  1.00 19.93 ? 125 PRO B CD  1 
ATOM   2481 N  N   . SER B 1 138 ? 3.417   4.289   48.202  1.00 13.73 ? 126 SER B N   1 
ATOM   2482 C  CA  . SER B 1 138 ? 2.185   3.833   48.836  1.00 12.48 ? 126 SER B CA  1 
ATOM   2483 C  C   . SER B 1 138 ? 1.551   5.003   49.561  1.00 13.26 ? 126 SER B C   1 
ATOM   2484 O  O   . SER B 1 138 ? 2.145   6.078   49.695  1.00 13.06 ? 126 SER B O   1 
ATOM   2485 C  CB  . SER B 1 138 ? 2.436   2.662   49.806  1.00 12.77 ? 126 SER B CB  1 
ATOM   2486 O  OG  . SER B 1 138 ? 2.813   3.145   51.094  1.00 13.78 ? 126 SER B OG  1 
ATOM   2487 N  N   . ILE B 1 139 ? 0.318   4.792   50.030  1.00 12.38 ? 127 ILE B N   1 
ATOM   2488 C  CA  . ILE B 1 139 ? -0.335  5.815   50.837  1.00 13.78 ? 127 ILE B CA  1 
ATOM   2489 C  C   . ILE B 1 139 ? 0.369   6.029   52.171  1.00 15.60 ? 127 ILE B C   1 
ATOM   2490 O  O   . ILE B 1 139 ? 0.059   6.995   52.882  1.00 16.49 ? 127 ILE B O   1 
ATOM   2491 C  CB  . ILE B 1 139 ? -1.827  5.493   51.077  1.00 14.00 ? 127 ILE B CB  1 
ATOM   2492 C  CG1 . ILE B 1 139 ? -2.014  4.113   51.708  1.00 14.25 ? 127 ILE B CG1 1 
ATOM   2493 C  CG2 . ILE B 1 139 ? -2.626  5.612   49.771  1.00 12.96 ? 127 ILE B CG2 1 
ATOM   2494 C  CD1 . ILE B 1 139 ? -3.383  3.929   52.353  1.00 13.22 ? 127 ILE B CD1 1 
ATOM   2495 N  N   . GLU B 1 140 ? 1.324   5.171   52.521  1.00 15.98 ? 128 GLU B N   1 
ATOM   2496 C  CA  . GLU B 1 140 ? 2.096   5.346   53.747  1.00 14.58 ? 128 GLU B CA  1 
ATOM   2497 C  C   . GLU B 1 140 ? 3.551   5.722   53.497  1.00 19.20 ? 128 GLU B C   1 
ATOM   2498 O  O   . GLU B 1 140 ? 4.350   5.710   54.441  1.00 19.31 ? 128 GLU B O   1 
ATOM   2499 C  CB  . GLU B 1 140 ? 2.031   4.078   54.602  1.00 16.98 ? 128 GLU B CB  1 
ATOM   2500 C  CG  . GLU B 1 140 ? 0.639   3.779   55.164  1.00 16.03 ? 128 GLU B CG  1 
ATOM   2501 C  CD  . GLU B 1 140 ? 0.131   4.823   56.156  1.00 24.35 ? 128 GLU B CD  1 
ATOM   2502 O  OE1 . GLU B 1 140 ? -0.905  4.556   56.799  1.00 25.29 ? 128 GLU B OE1 1 
ATOM   2503 O  OE2 . GLU B 1 140 ? 0.749   5.902   56.311  1.00 25.19 ? 128 GLU B OE2 1 
ATOM   2504 N  N   . GLY B 1 141 ? 3.912   6.064   52.270  1.00 16.28 ? 129 GLY B N   1 
ATOM   2505 C  CA  . GLY B 1 141 ? 5.302   6.273   51.914  1.00 18.24 ? 129 GLY B CA  1 
ATOM   2506 C  C   . GLY B 1 141 ? 5.885   5.037   51.264  1.00 16.66 ? 129 GLY B C   1 
ATOM   2507 O  O   . GLY B 1 141 ? 5.184   4.073   50.937  1.00 18.59 ? 129 GLY B O   1 
ATOM   2508 N  N   . THR B 1 142 ? 7.199   5.075   51.058  1.00 12.65 ? 130 THR B N   1 
ATOM   2509 C  CA  . THR B 1 142 ? 7.883   3.933   50.465  1.00 11.31 ? 130 THR B CA  1 
ATOM   2510 C  C   . THR B 1 142 ? 7.655   2.703   51.332  1.00 16.47 ? 130 THR B C   1 
ATOM   2511 O  O   . THR B 1 142 ? 7.915   2.737   52.535  1.00 15.66 ? 130 THR B O   1 
ATOM   2512 C  CB  . THR B 1 142 ? 9.381   4.226   50.337  1.00 16.57 ? 130 THR B CB  1 
ATOM   2513 O  OG1 . THR B 1 142 ? 9.565   5.400   49.545  1.00 18.65 ? 130 THR B OG1 1 
ATOM   2514 C  CG2 . THR B 1 142 ? 10.096  3.066   49.679  1.00 17.65 ? 130 THR B CG2 1 
ATOM   2515 N  N   . ALA B 1 143 ? 7.140   1.627   50.739  1.00 12.31 ? 131 ALA B N   1 
ATOM   2516 C  CA  . ALA B 1 143 ? 6.727   0.497   51.558  1.00 13.21 ? 131 ALA B CA  1 
ATOM   2517 C  C   . ALA B 1 143 ? 6.693   -0.779  50.732  1.00 16.51 ? 131 ALA B C   1 
ATOM   2518 O  O   . ALA B 1 143 ? 6.769   -0.760  49.498  1.00 17.82 ? 131 ALA B O   1 
ATOM   2519 C  CB  . ALA B 1 143 ? 5.352   0.754   52.195  1.00 14.42 ? 131 ALA B CB  1 
ATOM   2520 N  N   . THR B 1 144 ? 6.533   -1.893  51.443  1.00 13.49 ? 132 THR B N   1 
ATOM   2521 C  CA  . THR B 1 144 ? 6.347   -3.211  50.852  1.00 15.37 ? 132 THR B CA  1 
ATOM   2522 C  C   . THR B 1 144 ? 4.970   -3.723  51.241  1.00 17.04 ? 132 THR B C   1 
ATOM   2523 O  O   . THR B 1 144 ? 4.614   -3.721  52.424  1.00 19.73 ? 132 THR B O   1 
ATOM   2524 C  CB  . THR B 1 144 ? 7.446   -4.177  51.318  1.00 19.07 ? 132 THR B CB  1 
ATOM   2525 O  OG1 . THR B 1 144 ? 8.686   -3.786  50.718  1.00 19.73 ? 132 THR B OG1 1 
ATOM   2526 C  CG2 . THR B 1 144 ? 7.110   -5.605  50.917  1.00 20.28 ? 132 THR B CG2 1 
ATOM   2527 N  N   . PHE B 1 145 ? 4.183   -4.138  50.249  1.00 12.21 ? 133 PHE B N   1 
ATOM   2528 C  CA  . PHE B 1 145 ? 2.780   -4.423  50.516  1.00 12.43 ? 133 PHE B CA  1 
ATOM   2529 C  C   . PHE B 1 145 ? 2.255   -5.420  49.492  1.00 12.83 ? 133 PHE B C   1 
ATOM   2530 O  O   . PHE B 1 145 ? 2.826   -5.590  48.414  1.00 14.29 ? 133 PHE B O   1 
ATOM   2531 C  CB  . PHE B 1 145 ? 1.943   -3.133  50.493  1.00 15.21 ? 133 PHE B CB  1 
ATOM   2532 C  CG  . PHE B 1 145 ? 2.159   -2.288  49.264  1.00 12.32 ? 133 PHE B CG  1 
ATOM   2533 C  CD1 . PHE B 1 145 ? 3.155   -1.322  49.233  1.00 12.34 ? 133 PHE B CD1 1 
ATOM   2534 C  CD2 . PHE B 1 145 ? 1.367   -2.460  48.139  1.00 10.92 ? 133 PHE B CD2 1 
ATOM   2535 C  CE1 . PHE B 1 145 ? 3.367   -0.550  48.104  1.00 14.14 ? 133 PHE B CE1 1 
ATOM   2536 C  CE2 . PHE B 1 145 ? 1.565   -1.692  47.004  1.00 12.05 ? 133 PHE B CE2 1 
ATOM   2537 C  CZ  . PHE B 1 145 ? 2.571   -0.729  46.983  1.00 13.60 ? 133 PHE B CZ  1 
ATOM   2538 N  N   . ASN B 1 146 ? 1.154   -6.085  49.852  1.00 12.81 ? 134 ASN B N   1 
ATOM   2539 C  CA  . ASN B 1 146 ? 0.477   -6.985  48.929  1.00 12.98 ? 134 ASN B CA  1 
ATOM   2540 C  C   . ASN B 1 146 ? -0.328  -6.179  47.917  1.00 10.90 ? 134 ASN B C   1 
ATOM   2541 O  O   . ASN B 1 146 ? -0.855  -5.107  48.222  1.00 10.23 ? 134 ASN B O   1 
ATOM   2542 C  CB  . ASN B 1 146 ? -0.479  -7.924  49.666  1.00 15.06 ? 134 ASN B CB  1 
ATOM   2543 C  CG  . ASN B 1 146 ? 0.233   -8.925  50.581  1.00 20.88 ? 134 ASN B CG  1 
ATOM   2544 O  OD1 . ASN B 1 146 ? 1.445   -9.122  50.507  1.00 21.49 ? 134 ASN B OD1 1 
ATOM   2545 N  ND2 . ASN B 1 146 ? -0.543  -9.573  51.441  1.00 22.76 ? 134 ASN B ND2 1 
ATOM   2546 N  N   . GLN B 1 147 ? -0.458  -6.733  46.716  1.00 10.84 ? 135 GLN B N   1 
ATOM   2547 C  CA  . GLN B 1 147 ? -1.243  -6.130  45.650  1.00 10.47 ? 135 GLN B CA  1 
ATOM   2548 C  C   . GLN B 1 147 ? -2.183  -7.196  45.101  1.00 11.25 ? 135 GLN B C   1 
ATOM   2549 O  O   . GLN B 1 147 ? -1.726  -8.271  44.699  1.00 11.58 ? 135 GLN B O   1 
ATOM   2550 C  CB  . GLN B 1 147 ? -0.298  -5.582  44.575  1.00 11.45 ? 135 GLN B CB  1 
ATOM   2551 C  CG  . GLN B 1 147 ? -0.916  -4.696  43.514  1.00 12.63 ? 135 GLN B CG  1 
ATOM   2552 C  CD  . GLN B 1 147 ? 0.096   -4.371  42.427  1.00 14.65 ? 135 GLN B CD  1 
ATOM   2553 O  OE1 . GLN B 1 147 ? 0.668   -5.275  41.823  1.00 15.67 ? 135 GLN B OE1 1 
ATOM   2554 N  NE2 . GLN B 1 147 ? 0.333   -3.084  42.184  1.00 12.75 ? 135 GLN B NE2 1 
ATOM   2555 N  N   . TYR B 1 148 ? -3.491  -6.923  45.125  1.00 9.18  ? 136 TYR B N   1 
ATOM   2556 C  CA  . TYR B 1 148 ? -4.502  -7.867  44.660  1.00 9.43  ? 136 TYR B CA  1 
ATOM   2557 C  C   . TYR B 1 148 ? -5.136  -7.366  43.366  1.00 12.18 ? 136 TYR B C   1 
ATOM   2558 O  O   . TYR B 1 148 ? -5.310  -6.159  43.165  1.00 10.52 ? 136 TYR B O   1 
ATOM   2559 C  CB  . TYR B 1 148 ? -5.605  -8.090  45.709  1.00 10.68 ? 136 TYR B CB  1 
ATOM   2560 C  CG  . TYR B 1 148 ? -5.104  -8.537  47.068  1.00 9.85  ? 136 TYR B CG  1 
ATOM   2561 C  CD1 . TYR B 1 148 ? -3.901  -9.216  47.193  1.00 9.51  ? 136 TYR B CD1 1 
ATOM   2562 C  CD2 . TYR B 1 148 ? -5.841  -8.283  48.216  1.00 9.96  ? 136 TYR B CD2 1 
ATOM   2563 C  CE1 . TYR B 1 148 ? -3.430  -9.622  48.441  1.00 12.97 ? 136 TYR B CE1 1 
ATOM   2564 C  CE2 . TYR B 1 148 ? -5.381  -8.683  49.479  1.00 15.18 ? 136 TYR B CE2 1 
ATOM   2565 C  CZ  . TYR B 1 148 ? -4.173  -9.354  49.575  1.00 13.63 ? 136 TYR B CZ  1 
ATOM   2566 O  OH  . TYR B 1 148 ? -3.707  -9.749  50.811  1.00 14.13 ? 136 TYR B OH  1 
ATOM   2567 N  N   . TRP B 1 149 ? -5.491  -8.317  42.491  1.00 9.43  ? 137 TRP B N   1 
ATOM   2568 C  CA  . TRP B 1 149 ? -6.067  -8.032  41.183  1.00 10.66 ? 137 TRP B CA  1 
ATOM   2569 C  C   . TRP B 1 149 ? -7.313  -8.876  40.959  1.00 9.41  ? 137 TRP B C   1 
ATOM   2570 O  O   . TRP B 1 149 ? -7.297  -10.080 41.233  1.00 10.25 ? 137 TRP B O   1 
ATOM   2571 C  CB  . TRP B 1 149 ? -5.064  -8.335  40.061  1.00 8.45  ? 137 TRP B CB  1 
ATOM   2572 C  CG  . TRP B 1 149 ? -3.803  -7.532  40.108  1.00 10.54 ? 137 TRP B CG  1 
ATOM   2573 C  CD1 . TRP B 1 149 ? -2.670  -7.823  40.825  1.00 12.42 ? 137 TRP B CD1 1 
ATOM   2574 C  CD2 . TRP B 1 149 ? -3.542  -6.304  39.430  1.00 10.69 ? 137 TRP B CD2 1 
ATOM   2575 N  NE1 . TRP B 1 149 ? -1.718  -6.854  40.612  1.00 12.42 ? 137 TRP B NE1 1 
ATOM   2576 C  CE2 . TRP B 1 149 ? -2.225  -5.910  39.763  1.00 10.77 ? 137 TRP B CE2 1 
ATOM   2577 C  CE3 . TRP B 1 149 ? -4.285  -5.502  38.559  1.00 12.35 ? 137 TRP B CE3 1 
ATOM   2578 C  CZ2 . TRP B 1 149 ? -1.647  -4.752  39.269  1.00 12.16 ? 137 TRP B CZ2 1 
ATOM   2579 C  CZ3 . TRP B 1 149 ? -3.710  -4.342  38.080  1.00 12.07 ? 137 TRP B CZ3 1 
ATOM   2580 C  CH2 . TRP B 1 149 ? -2.398  -3.978  38.434  1.00 14.55 ? 137 TRP B CH2 1 
ATOM   2581 N  N   . SER B 1 150 ? -8.385  -8.249  40.456  1.00 8.46  ? 138 SER B N   1 
ATOM   2582 C  CA  . SER B 1 150 ? -9.464  -8.919  39.725  1.00 11.42 ? 138 SER B CA  1 
ATOM   2583 C  C   . SER B 1 150 ? -9.445  -8.336  38.321  1.00 10.94 ? 138 SER B C   1 
ATOM   2584 O  O   . SER B 1 150 ? -9.555  -7.117  38.168  1.00 11.33 ? 138 SER B O   1 
ATOM   2585 C  CB  . SER B 1 150 ? -10.838 -8.663  40.351  1.00 13.84 ? 138 SER B CB  1 
ATOM   2586 O  OG  . SER B 1 150 ? -11.171 -9.590  41.353  1.00 17.60 ? 138 SER B OG  1 
ATOM   2587 N  N   . VAL B 1 151 ? -9.304  -9.182  37.300  1.00 9.87  ? 139 VAL B N   1 
ATOM   2588 C  CA  . VAL B 1 151 ? -9.177  -8.711  35.922  1.00 8.55  ? 139 VAL B CA  1 
ATOM   2589 C  C   . VAL B 1 151 ? -10.319 -9.308  35.101  1.00 11.27 ? 139 VAL B C   1 
ATOM   2590 O  O   . VAL B 1 151 ? -10.428 -10.533 34.973  1.00 11.69 ? 139 VAL B O   1 
ATOM   2591 C  CB  . VAL B 1 151 ? -7.809  -9.070  35.318  1.00 10.81 ? 139 VAL B CB  1 
ATOM   2592 C  CG1 . VAL B 1 151 ? -7.654  -8.465  33.929  1.00 10.60 ? 139 VAL B CG1 1 
ATOM   2593 C  CG2 . VAL B 1 151 ? -6.662  -8.594  36.248  1.00 11.55 ? 139 VAL B CG2 1 
ATOM   2594 N  N   . ARG B 1 152 ? -11.170 -8.442  34.563  1.00 8.77  ? 140 ARG B N   1 
ATOM   2595 C  CA  . ARG B 1 152 ? -12.337 -8.890  33.807  1.00 11.22 ? 140 ARG B CA  1 
ATOM   2596 C  C   . ARG B 1 152 ? -11.906 -9.535  32.492  1.00 14.11 ? 140 ARG B C   1 
ATOM   2597 O  O   . ARG B 1 152 ? -11.044 -9.015  31.783  1.00 12.83 ? 140 ARG B O   1 
ATOM   2598 C  CB  . ARG B 1 152 ? -13.256 -7.702  33.535  1.00 9.35  ? 140 ARG B CB  1 
ATOM   2599 C  CG  . ARG B 1 152 ? -14.694 -8.082  33.127  1.00 11.13 ? 140 ARG B CG  1 
ATOM   2600 C  CD  . ARG B 1 152 ? -15.605 -6.851  33.021  1.00 12.00 ? 140 ARG B CD  1 
ATOM   2601 N  NE  . ARG B 1 152 ? -16.910 -7.188  32.444  1.00 13.13 ? 140 ARG B NE  1 
ATOM   2602 C  CZ  . ARG B 1 152 ? -18.017 -7.403  33.146  1.00 14.48 ? 140 ARG B CZ  1 
ATOM   2603 N  NH1 . ARG B 1 152 ? -18.007 -7.322  34.475  1.00 14.87 ? 140 ARG B NH1 1 
ATOM   2604 N  NH2 . ARG B 1 152 ? -19.149 -7.683  32.515  1.00 16.54 ? 140 ARG B NH2 1 
ATOM   2605 N  N   . THR B 1 153 ? -12.529 -10.670 32.150  1.00 14.23 ? 141 THR B N   1 
ATOM   2606 C  CA  . THR B 1 153 ? -12.162 -11.351 30.911  1.00 17.32 ? 141 THR B CA  1 
ATOM   2607 C  C   . THR B 1 153 ? -12.775 -10.700 29.672  1.00 16.65 ? 141 THR B C   1 
ATOM   2608 O  O   . THR B 1 153 ? -12.228 -10.854 28.574  1.00 19.81 ? 141 THR B O   1 
ATOM   2609 C  CB  . THR B 1 153 ? -12.558 -12.835 30.966  1.00 15.22 ? 141 THR B CB  1 
ATOM   2610 O  OG1 . THR B 1 153 ? -13.982 -12.958 31.064  1.00 20.19 ? 141 THR B OG1 1 
ATOM   2611 C  CG2 . THR B 1 153 ? -11.895 -13.530 32.157  1.00 16.87 ? 141 THR B CG2 1 
ATOM   2612 N  N   . ASP B 1 154 ? -13.880 -9.978  29.817  1.00 15.35 ? 142 ASP B N   1 
ATOM   2613 C  CA  . ASP B 1 154 ? -14.517 -9.266  28.711  1.00 22.30 ? 142 ASP B CA  1 
ATOM   2614 C  C   . ASP B 1 154 ? -14.501 -7.781  29.052  1.00 19.15 ? 142 ASP B C   1 
ATOM   2615 O  O   . ASP B 1 154 ? -15.265 -7.329  29.912  1.00 19.44 ? 142 ASP B O   1 
ATOM   2616 C  CB  . ASP B 1 154 ? -15.939 -9.772  28.482  1.00 23.21 ? 142 ASP B CB  1 
ATOM   2617 C  CG  . ASP B 1 154 ? -16.681 -8.962  27.440  1.00 30.39 ? 142 ASP B CG  1 
ATOM   2618 O  OD1 . ASP B 1 154 ? -17.858 -8.622  27.678  1.00 41.97 ? 142 ASP B OD1 1 
ATOM   2619 O  OD2 . ASP B 1 154 ? -16.076 -8.650  26.397  1.00 35.00 ? 142 ASP B OD2 1 
ATOM   2620 N  N   . HIS B 1 155 ? -13.633 -7.026  28.384  1.00 16.26 ? 143 HIS B N   1 
ATOM   2621 C  CA  . HIS B 1 155 ? -13.355 -5.666  28.820  1.00 19.31 ? 143 HIS B CA  1 
ATOM   2622 C  C   . HIS B 1 155 ? -14.538 -4.744  28.557  1.00 17.20 ? 143 HIS B C   1 
ATOM   2623 O  O   . HIS B 1 155 ? -15.273 -4.885  27.569  1.00 15.52 ? 143 HIS B O   1 
ATOM   2624 C  CB  . HIS B 1 155 ? -12.097 -5.144  28.129  1.00 17.71 ? 143 HIS B CB  1 
ATOM   2625 C  CG  . HIS B 1 155 ? -10.859 -5.911  28.496  1.00 17.10 ? 143 HIS B CG  1 
ATOM   2626 N  ND1 . HIS B 1 155 ? -9.629  -5.660  27.935  1.00 23.01 ? 143 HIS B ND1 1 
ATOM   2627 C  CD2 . HIS B 1 155 ? -10.675 -6.939  29.357  1.00 19.60 ? 143 HIS B CD2 1 
ATOM   2628 C  CE1 . HIS B 1 155 ? -8.738  -6.500  28.431  1.00 20.83 ? 143 HIS B CE1 1 
ATOM   2629 N  NE2 . HIS B 1 155 ? -9.344  -7.283  29.305  1.00 21.92 ? 143 HIS B NE2 1 
ATOM   2630 N  N   . ARG B 1 156 ? -14.737 -3.789  29.461  1.00 12.15 ? 144 ARG B N   1 
ATOM   2631 C  CA  . ARG B 1 156 ? -15.841 -2.856  29.278  1.00 13.64 ? 144 ARG B CA  1 
ATOM   2632 C  C   . ARG B 1 156 ? -15.513 -1.513  29.908  1.00 15.74 ? 144 ARG B C   1 
ATOM   2633 O  O   . ARG B 1 156 ? -14.645 -1.403  30.782  1.00 14.27 ? 144 ARG B O   1 
ATOM   2634 C  CB  . ARG B 1 156 ? -17.150 -3.392  29.866  1.00 16.47 ? 144 ARG B CB  1 
ATOM   2635 C  CG  . ARG B 1 156 ? -17.156 -3.400  31.360  1.00 15.19 ? 144 ARG B CG  1 
ATOM   2636 C  CD  . ARG B 1 156 ? -18.413 -4.021  31.966  1.00 14.60 ? 144 ARG B CD  1 
ATOM   2637 N  NE  . ARG B 1 156 ? -18.258 -4.049  33.421  1.00 14.86 ? 144 ARG B NE  1 
ATOM   2638 C  CZ  . ARG B 1 156 ? -19.251 -4.193  34.296  1.00 15.29 ? 144 ARG B CZ  1 
ATOM   2639 N  NH1 . ARG B 1 156 ? -20.507 -4.338  33.881  1.00 15.61 ? 144 ARG B NH1 1 
ATOM   2640 N  NH2 . ARG B 1 156 ? -18.981 -4.182  35.599  1.00 13.68 ? 144 ARG B NH2 1 
ATOM   2641 N  N   . VAL B 1 157 ? -16.232 -0.491  29.443  1.00 12.75 ? 145 VAL B N   1 
ATOM   2642 C  CA  . VAL B 1 157 ? -16.139 0.867   29.964  1.00 12.01 ? 145 VAL B CA  1 
ATOM   2643 C  C   . VAL B 1 157 ? -17.533 1.264   30.425  1.00 15.48 ? 145 VAL B C   1 
ATOM   2644 O  O   . VAL B 1 157 ? -18.415 1.555   29.604  1.00 15.34 ? 145 VAL B O   1 
ATOM   2645 C  CB  . VAL B 1 157 ? -15.603 1.862   28.932  1.00 13.21 ? 145 VAL B CB  1 
ATOM   2646 C  CG1 . VAL B 1 157 ? -15.525 3.272   29.551  1.00 11.13 ? 145 VAL B CG1 1 
ATOM   2647 C  CG2 . VAL B 1 157 ? -14.239 1.405   28.417  1.00 15.30 ? 145 VAL B CG2 1 
ATOM   2648 N  N   . GLY B 1 158 ? -17.731 1.289   31.724  1.00 17.03 ? 146 GLY B N   1 
ATOM   2649 C  CA  . GLY B 1 158 ? -19.026 1.599   32.285  1.00 17.06 ? 146 GLY B CA  1 
ATOM   2650 C  C   . GLY B 1 158 ? -19.660 0.354   32.873  1.00 16.99 ? 146 GLY B C   1 
ATOM   2651 O  O   . GLY B 1 158 ? -19.103 -0.745  32.846  1.00 19.91 ? 146 GLY B O   1 
ATOM   2652 N  N   . GLY B 1 159 ? -20.839 0.552   33.425  1.00 21.07 ? 147 GLY B N   1 
ATOM   2653 C  CA  . GLY B 1 159 ? -21.497 -0.513  34.123  1.00 20.47 ? 147 GLY B CA  1 
ATOM   2654 C  C   . GLY B 1 159 ? -21.353 -0.378  35.623  1.00 17.11 ? 147 GLY B C   1 
ATOM   2655 O  O   . GLY B 1 159 ? -21.024 0.675   36.172  1.00 19.40 ? 147 GLY B O   1 
ATOM   2656 N  N   . THR B 1 160 ? -21.594 -1.490  36.290  1.00 12.68 ? 148 THR B N   1 
ATOM   2657 C  CA  . THR B 1 160 ? -21.711 -1.527  37.736  1.00 15.81 ? 148 THR B CA  1 
ATOM   2658 C  C   . THR B 1 160 ? -20.682 -2.499  38.272  1.00 13.41 ? 148 THR B C   1 
ATOM   2659 O  O   . THR B 1 160 ? -20.459 -3.556  37.678  1.00 13.57 ? 148 THR B O   1 
ATOM   2660 C  CB  . THR B 1 160 ? -23.132 -1.959  38.130  1.00 17.88 ? 148 THR B CB  1 
ATOM   2661 O  OG1 . THR B 1 160 ? -24.063 -1.011  37.601  1.00 19.75 ? 148 THR B OG1 1 
ATOM   2662 C  CG2 . THR B 1 160 ? -23.281 -1.988  39.626  1.00 18.95 ? 148 THR B CG2 1 
ATOM   2663 N  N   . VAL B 1 161 ? -20.034 -2.129  39.376  1.00 11.34 ? 149 VAL B N   1 
ATOM   2664 C  CA  . VAL B 1 161 ? -19.037 -2.977  40.019  1.00 12.52 ? 149 VAL B CA  1 
ATOM   2665 C  C   . VAL B 1 161 ? -19.493 -3.207  41.452  1.00 12.85 ? 149 VAL B C   1 
ATOM   2666 O  O   . VAL B 1 161 ? -19.532 -2.266  42.255  1.00 11.85 ? 149 VAL B O   1 
ATOM   2667 C  CB  . VAL B 1 161 ? -17.634 -2.354  39.990  1.00 10.54 ? 149 VAL B CB  1 
ATOM   2668 C  CG1 . VAL B 1 161 ? -16.654 -3.217  40.784  1.00 13.86 ? 149 VAL B CG1 1 
ATOM   2669 C  CG2 . VAL B 1 161 ? -17.147 -2.178  38.559  1.00 13.06 ? 149 VAL B CG2 1 
ATOM   2670 N  N   . THR B 1 162 ? -19.861 -4.448  41.774  1.00 10.63 ? 150 THR B N   1 
ATOM   2671 C  CA  . THR B 1 162 ? -20.272 -4.797  43.134  1.00 11.81 ? 150 THR B CA  1 
ATOM   2672 C  C   . THR B 1 162 ? -19.003 -5.168  43.892  1.00 10.46 ? 150 THR B C   1 
ATOM   2673 O  O   . THR B 1 162 ? -18.563 -6.322  43.883  1.00 13.53 ? 150 THR B O   1 
ATOM   2674 C  CB  . THR B 1 162 ? -21.288 -5.932  43.111  1.00 17.75 ? 150 THR B CB  1 
ATOM   2675 O  OG1 . THR B 1 162 ? -22.346 -5.585  42.204  1.00 16.24 ? 150 THR B OG1 1 
ATOM   2676 C  CG2 . THR B 1 162 ? -21.877 -6.164  44.504  1.00 14.01 ? 150 THR B CG2 1 
ATOM   2677 N  N   . THR B 1 163 ? -18.387 -4.174  44.535  1.00 11.87 ? 151 THR B N   1 
ATOM   2678 C  CA  . THR B 1 163 ? -17.041 -4.390  45.070  1.00 12.38 ? 151 THR B CA  1 
ATOM   2679 C  C   . THR B 1 163 ? -17.021 -5.466  46.146  1.00 12.37 ? 151 THR B C   1 
ATOM   2680 O  O   . THR B 1 163 ? -16.023 -6.187  46.280  1.00 12.35 ? 151 THR B O   1 
ATOM   2681 C  CB  . THR B 1 163 ? -16.434 -3.089  45.625  1.00 13.97 ? 151 THR B CB  1 
ATOM   2682 O  OG1 . THR B 1 163 ? -17.242 -2.568  46.690  1.00 15.03 ? 151 THR B OG1 1 
ATOM   2683 C  CG2 . THR B 1 163 ? -16.283 -2.044  44.515  1.00 13.16 ? 151 THR B CG2 1 
ATOM   2684 N  N   . GLN B 1 164 ? -18.101 -5.592  46.920  1.00 14.01 ? 152 GLN B N   1 
ATOM   2685 C  CA  . GLN B 1 164 ? -18.149 -6.602  47.975  1.00 15.46 ? 152 GLN B CA  1 
ATOM   2686 C  C   . GLN B 1 164 ? -17.949 -8.010  47.428  1.00 14.26 ? 152 GLN B C   1 
ATOM   2687 O  O   . GLN B 1 164 ? -17.365 -8.861  48.108  1.00 14.95 ? 152 GLN B O   1 
ATOM   2688 C  CB  . GLN B 1 164 ? -19.481 -6.517  48.727  1.00 18.70 ? 152 GLN B CB  1 
ATOM   2689 C  CG  . GLN B 1 164 ? -19.542 -7.371  49.993  1.00 22.14 ? 152 GLN B CG  1 
ATOM   2690 C  CD  . GLN B 1 164 ? -18.359 -7.122  50.915  1.00 29.73 ? 152 GLN B CD  1 
ATOM   2691 O  OE1 . GLN B 1 164 ? -18.130 -5.999  51.360  1.00 33.66 ? 152 GLN B OE1 1 
ATOM   2692 N  NE2 . GLN B 1 164 ? -17.591 -8.167  51.195  1.00 35.34 ? 152 GLN B NE2 1 
ATOM   2693 N  N   . ASN B 1 165 ? -18.420 -8.275  46.202  1.00 14.47 ? 153 ASN B N   1 
ATOM   2694 C  CA  . ASN B 1 165 ? -18.215 -9.589  45.607  1.00 12.64 ? 153 ASN B CA  1 
ATOM   2695 C  C   . ASN B 1 165 ? -16.739 -9.859  45.336  1.00 18.00 ? 153 ASN B C   1 
ATOM   2696 O  O   . ASN B 1 165 ? -16.286 -11.004 45.462  1.00 16.21 ? 153 ASN B O   1 
ATOM   2697 C  CB  . ASN B 1 165 ? -19.030 -9.705  44.318  1.00 11.04 ? 153 ASN B CB  1 
ATOM   2698 C  CG  . ASN B 1 165 ? -20.532 -9.786  44.573  1.00 18.07 ? 153 ASN B CG  1 
ATOM   2699 O  OD1 . ASN B 1 165 ? -20.982 -10.025 45.696  1.00 18.52 ? 153 ASN B OD1 1 
ATOM   2700 N  ND2 . ASN B 1 165 ? -21.314 -9.595  43.523  1.00 16.05 ? 153 ASN B ND2 1 
ATOM   2701 N  N   . HIS B 1 166 ? -15.970 -8.824  44.990  1.00 11.71 ? 154 HIS B N   1 
ATOM   2702 C  CA  . HIS B 1 166 ? -14.536 -9.001  44.796  1.00 13.20 ? 154 HIS B CA  1 
ATOM   2703 C  C   . HIS B 1 166 ? -13.816 -9.194  46.122  1.00 12.66 ? 154 HIS B C   1 
ATOM   2704 O  O   . HIS B 1 166 ? -12.993 -10.105 46.260  1.00 14.80 ? 154 HIS B O   1 
ATOM   2705 C  CB  . HIS B 1 166 ? -13.966 -7.804  44.044  1.00 14.13 ? 154 HIS B CB  1 
ATOM   2706 C  CG  . HIS B 1 166 ? -14.454 -7.719  42.636  1.00 8.06  ? 154 HIS B CG  1 
ATOM   2707 N  ND1 . HIS B 1 166 ? -13.853 -8.399  41.596  1.00 11.54 ? 154 HIS B ND1 1 
ATOM   2708 C  CD2 . HIS B 1 166 ? -15.527 -7.087  42.104  1.00 10.82 ? 154 HIS B CD2 1 
ATOM   2709 C  CE1 . HIS B 1 166 ? -14.514 -8.164  40.478  1.00 9.65  ? 154 HIS B CE1 1 
ATOM   2710 N  NE2 . HIS B 1 166 ? -15.547 -7.382  40.760  1.00 11.51 ? 154 HIS B NE2 1 
ATOM   2711 N  N   . PHE B 1 167 ? -14.113 -8.342  47.107  1.00 12.56 ? 155 PHE B N   1 
ATOM   2712 C  CA  . PHE B 1 167 ? -13.464 -8.471  48.410  1.00 13.80 ? 155 PHE B CA  1 
ATOM   2713 C  C   . PHE B 1 167 ? -13.763 -9.826  49.047  1.00 16.01 ? 155 PHE B C   1 
ATOM   2714 O  O   . PHE B 1 167 ? -12.867 -10.453 49.630  1.00 15.37 ? 155 PHE B O   1 
ATOM   2715 C  CB  . PHE B 1 167 ? -13.901 -7.336  49.332  1.00 13.54 ? 155 PHE B CB  1 
ATOM   2716 C  CG  . PHE B 1 167 ? -13.603 -5.956  48.797  1.00 13.36 ? 155 PHE B CG  1 
ATOM   2717 C  CD1 . PHE B 1 167 ? -12.504 -5.731  47.986  1.00 16.51 ? 155 PHE B CD1 1 
ATOM   2718 C  CD2 . PHE B 1 167 ? -14.422 -4.888  49.117  1.00 14.35 ? 155 PHE B CD2 1 
ATOM   2719 C  CE1 . PHE B 1 167 ? -12.221 -4.461  47.495  1.00 15.59 ? 155 PHE B CE1 1 
ATOM   2720 C  CE2 . PHE B 1 167 ? -14.146 -3.607  48.626  1.00 13.49 ? 155 PHE B CE2 1 
ATOM   2721 C  CZ  . PHE B 1 167 ? -13.040 -3.400  47.823  1.00 15.47 ? 155 PHE B CZ  1 
ATOM   2722 N  N   . ASP B 1 168 ? -15.017 -10.289 48.949  1.00 15.51 ? 156 ASP B N   1 
ATOM   2723 C  CA  . ASP B 1 168 ? -15.364 -11.616 49.455  1.00 19.45 ? 156 ASP B CA  1 
ATOM   2724 C  C   . ASP B 1 168 ? -14.582 -12.705 48.736  1.00 18.12 ? 156 ASP B C   1 
ATOM   2725 O  O   . ASP B 1 168 ? -14.103 -13.654 49.362  1.00 18.79 ? 156 ASP B O   1 
ATOM   2726 C  CB  . ASP B 1 168 ? -16.873 -11.873 49.318  1.00 18.96 ? 156 ASP B CB  1 
ATOM   2727 C  CG  . ASP B 1 168 ? -17.683 -11.040 50.282  1.00 31.33 ? 156 ASP B CG  1 
ATOM   2728 O  OD1 . ASP B 1 168 ? -18.868 -10.756 49.974  1.00 38.91 ? 156 ASP B OD1 1 
ATOM   2729 O  OD2 . ASP B 1 168 ? -17.127 -10.656 51.335  1.00 30.33 ? 156 ASP B OD2 1 
ATOM   2730 N  N   . ALA B 1 169 ? -14.489 -12.612 47.406  1.00 15.54 ? 157 ALA B N   1 
ATOM   2731 C  CA  . ALA B 1 169 ? -13.751 -13.619 46.650  1.00 16.91 ? 157 ALA B CA  1 
ATOM   2732 C  C   . ALA B 1 169 ? -12.280 -13.641 47.044  1.00 18.24 ? 157 ALA B C   1 
ATOM   2733 O  O   . ALA B 1 169 ? -11.680 -14.715 47.185  1.00 17.15 ? 157 ALA B O   1 
ATOM   2734 C  CB  . ALA B 1 169 ? -13.895 -13.359 45.146  1.00 18.10 ? 157 ALA B CB  1 
ATOM   2735 N  N   . TRP B 1 170 ? -11.681 -12.462 47.220  1.00 13.87 ? 158 TRP B N   1 
ATOM   2736 C  CA  . TRP B 1 170 ? -10.282 -12.394 47.621  1.00 12.71 ? 158 TRP B CA  1 
ATOM   2737 C  C   . TRP B 1 170 ? -10.080 -13.005 48.999  1.00 13.44 ? 158 TRP B C   1 
ATOM   2738 O  O   . TRP B 1 170 ? -9.172  -13.818 49.200  1.00 15.15 ? 158 TRP B O   1 
ATOM   2739 C  CB  . TRP B 1 170 ? -9.807  -10.946 47.622  1.00 16.07 ? 158 TRP B CB  1 
ATOM   2740 C  CG  . TRP B 1 170 ? -9.855  -10.319 46.275  1.00 17.19 ? 158 TRP B CG  1 
ATOM   2741 C  CD1 . TRP B 1 170 ? -10.016 -10.952 45.071  1.00 17.51 ? 158 TRP B CD1 1 
ATOM   2742 C  CD2 . TRP B 1 170 ? -9.755  -8.926  45.989  1.00 13.92 ? 158 TRP B CD2 1 
ATOM   2743 N  NE1 . TRP B 1 170 ? -10.029 -10.027 44.052  1.00 16.80 ? 158 TRP B NE1 1 
ATOM   2744 C  CE2 . TRP B 1 170 ? -9.861  -8.775  44.592  1.00 15.53 ? 158 TRP B CE2 1 
ATOM   2745 C  CE3 . TRP B 1 170 ? -9.598  -7.786  46.781  1.00 14.80 ? 158 TRP B CE3 1 
ATOM   2746 C  CZ2 . TRP B 1 170 ? -9.805  -7.528  43.971  1.00 15.71 ? 158 TRP B CZ2 1 
ATOM   2747 C  CZ3 . TRP B 1 170 ? -9.551  -6.548  46.160  1.00 14.19 ? 158 TRP B CZ3 1 
ATOM   2748 C  CH2 . TRP B 1 170 ? -9.664  -6.429  44.770  1.00 12.25 ? 158 TRP B CH2 1 
ATOM   2749 N  N   . LYS B 1 171 ? -10.924 -12.616 49.959  1.00 16.69 ? 159 LYS B N   1 
ATOM   2750 C  CA  . LYS B 1 171 ? -10.775 -13.119 51.320  1.00 17.86 ? 159 LYS B CA  1 
ATOM   2751 C  C   . LYS B 1 171 ? -11.027 -14.617 51.370  1.00 20.46 ? 159 LYS B C   1 
ATOM   2752 O  O   . LYS B 1 171 ? -10.291 -15.358 52.028  1.00 20.02 ? 159 LYS B O   1 
ATOM   2753 C  CB  . LYS B 1 171 ? -11.714 -12.362 52.268  1.00 18.96 ? 159 LYS B CB  1 
ATOM   2754 C  CG  . LYS B 1 171 ? -11.215 -10.937 52.564  1.00 22.97 ? 159 LYS B CG  1 
ATOM   2755 C  CD  . LYS B 1 171 ? -12.099 -10.209 53.570  1.00 22.51 ? 159 LYS B CD  1 
ATOM   2756 C  CE  . LYS B 1 171 ? -13.513 -10.057 53.026  1.00 30.47 ? 159 LYS B CE  1 
ATOM   2757 N  NZ  . LYS B 1 171 ? -14.280 -8.984  53.718  1.00 38.38 ? 159 LYS B NZ  1 
ATOM   2758 N  N   . ASN B 1 172 ? -12.042 -15.085 50.646  1.00 18.19 ? 160 ASN B N   1 
ATOM   2759 C  CA  . ASN B 1 172 ? -12.303 -16.516 50.579  1.00 24.10 ? 160 ASN B CA  1 
ATOM   2760 C  C   . ASN B 1 172 ? -11.110 -17.273 50.008  1.00 23.61 ? 160 ASN B C   1 
ATOM   2761 O  O   . ASN B 1 172 ? -10.852 -18.414 50.409  1.00 24.07 ? 160 ASN B O   1 
ATOM   2762 C  CB  . ASN B 1 172 ? -13.556 -16.772 49.746  1.00 25.01 ? 160 ASN B CB  1 
ATOM   2763 C  CG  . ASN B 1 172 ? -13.950 -18.233 49.724  1.00 36.05 ? 160 ASN B CG  1 
ATOM   2764 O  OD1 . ASN B 1 172 ? -14.346 -18.796 50.741  1.00 43.22 ? 160 ASN B OD1 1 
ATOM   2765 N  ND2 . ASN B 1 172 ? -13.842 -18.864 48.562  1.00 35.99 ? 160 ASN B ND2 1 
ATOM   2766 N  N   . ALA B 1 173 ? -10.366 -16.658 49.086  1.00 19.95 ? 161 ALA B N   1 
ATOM   2767 C  CA  . ALA B 1 173 ? -9.182  -17.282 48.507  1.00 20.42 ? 161 ALA B CA  1 
ATOM   2768 C  C   . ALA B 1 173 ? -7.952  -17.167 49.397  1.00 21.39 ? 161 ALA B C   1 
ATOM   2769 O  O   . ALA B 1 173 ? -6.869  -17.583 48.976  1.00 24.03 ? 161 ALA B O   1 
ATOM   2770 C  CB  . ALA B 1 173 ? -8.886  -16.667 47.134  1.00 22.53 ? 161 ALA B CB  1 
ATOM   2771 N  N   . GLY B 1 174 ? -8.087  -16.624 50.604  1.00 17.32 ? 162 GLY B N   1 
ATOM   2772 C  CA  . GLY B 1 174 ? -6.983  -16.529 51.526  1.00 18.57 ? 162 GLY B CA  1 
ATOM   2773 C  C   . GLY B 1 174 ? -6.236  -15.220 51.518  1.00 23.10 ? 162 GLY B C   1 
ATOM   2774 O  O   . GLY B 1 174 ? -5.206  -15.115 52.194  1.00 28.29 ? 162 GLY B O   1 
ATOM   2775 N  N   . LEU B 1 175 ? -6.711  -14.220 50.781  1.00 16.39 ? 163 LEU B N   1 
ATOM   2776 C  CA  . LEU B 1 175 ? -6.044  -12.929 50.735  1.00 15.45 ? 163 LEU B CA  1 
ATOM   2777 C  C   . LEU B 1 175 ? -6.553  -12.080 51.894  1.00 21.97 ? 163 LEU B C   1 
ATOM   2778 O  O   . LEU B 1 175 ? -7.765  -11.944 52.089  1.00 26.13 ? 163 LEU B O   1 
ATOM   2779 C  CB  . LEU B 1 175 ? -6.292  -12.244 49.388  1.00 16.41 ? 163 LEU B CB  1 
ATOM   2780 C  CG  . LEU B 1 175 ? -5.912  -13.078 48.156  1.00 17.59 ? 163 LEU B CG  1 
ATOM   2781 C  CD1 . LEU B 1 175 ? -6.136  -12.307 46.864  1.00 19.19 ? 163 LEU B CD1 1 
ATOM   2782 C  CD2 . LEU B 1 175 ? -4.458  -13.528 48.271  1.00 19.88 ? 163 LEU B CD2 1 
ATOM   2783 N  N   . GLU B 1 176 ? -5.623  -11.534 52.670  1.00 19.71 ? 164 GLU B N   1 
ATOM   2784 C  CA  . GLU B 1 176 ? -5.937  -10.736 53.844  1.00 21.09 ? 164 GLU B CA  1 
ATOM   2785 C  C   . GLU B 1 176 ? -6.136  -9.275  53.468  1.00 15.91 ? 164 GLU B C   1 
ATOM   2786 O  O   . GLU B 1 176 ? -5.351  -8.716  52.705  1.00 17.12 ? 164 GLU B O   1 
ATOM   2787 C  CB  . GLU B 1 176 ? -4.788  -10.836 54.842  1.00 25.13 ? 164 GLU B CB  1 
ATOM   2788 C  CG  . GLU B 1 176 ? -4.801  -12.076 55.672  1.00 32.57 ? 164 GLU B CG  1 
ATOM   2789 C  CD  . GLU B 1 176 ? -4.116  -11.836 56.983  1.00 32.60 ? 164 GLU B CD  1 
ATOM   2790 O  OE1 . GLU B 1 176 ? -4.685  -12.218 58.025  1.00 45.90 ? 164 GLU B OE1 1 
ATOM   2791 O  OE2 . GLU B 1 176 ? -3.019  -11.233 56.986  1.00 38.69 ? 164 GLU B OE2 1 
ATOM   2792 N  N   . MET B 1 177 ? -7.170  -8.652  54.024  1.00 17.63 ? 165 MET B N   1 
ATOM   2793 C  CA  . MET B 1 177 ? -7.417  -7.235  53.799  1.00 16.58 ? 165 MET B CA  1 
ATOM   2794 C  C   . MET B 1 177 ? -7.508  -6.505  55.128  1.00 14.38 ? 165 MET B C   1 
ATOM   2795 O  O   . MET B 1 177 ? -7.967  -7.059  56.135  1.00 16.18 ? 165 MET B O   1 
ATOM   2796 C  CB  . MET B 1 177 ? -8.692  -7.012  52.997  1.00 18.57 ? 165 MET B CB  1 
ATOM   2797 C  CG  . MET B 1 177 ? -8.729  -7.861  51.744  1.00 25.47 ? 165 MET B CG  1 
ATOM   2798 S  SD  . MET B 1 177 ? -9.785  -7.132  50.500  1.00 37.31 ? 165 MET B SD  1 
ATOM   2799 C  CE  . MET B 1 177 ? -8.848  -5.674  50.113  1.00 24.33 ? 165 MET B CE  1 
ATOM   2800 N  N   . GLY B 1 178 ? -7.067  -5.255  55.128  1.00 11.22 ? 166 GLY B N   1 
ATOM   2801 C  CA  . GLY B 1 178 ? -7.089  -4.427  56.314  1.00 13.06 ? 166 GLY B CA  1 
ATOM   2802 C  C   . GLY B 1 178 ? -8.285  -3.494  56.361  1.00 11.58 ? 166 GLY B C   1 
ATOM   2803 O  O   . GLY B 1 178 ? -9.346  -3.759  55.781  1.00 15.29 ? 166 GLY B O   1 
ATOM   2804 N  N   . THR B 1 179 ? -8.117  -2.403  57.100  1.00 10.33 ? 167 THR B N   1 
ATOM   2805 C  CA  . THR B 1 179 ? -9.129  -1.354  57.172  1.00 10.49 ? 167 THR B CA  1 
ATOM   2806 C  C   . THR B 1 179 ? -9.115  -0.526  55.893  1.00 11.06 ? 167 THR B C   1 
ATOM   2807 O  O   . THR B 1 179 ? -8.062  -0.070  55.458  1.00 11.77 ? 167 THR B O   1 
ATOM   2808 C  CB  . THR B 1 179 ? -8.849  -0.456  58.376  1.00 16.01 ? 167 THR B CB  1 
ATOM   2809 O  OG1 . THR B 1 179 ? -8.833  -1.260  59.565  1.00 22.11 ? 167 THR B OG1 1 
ATOM   2810 C  CG2 . THR B 1 179 ? -9.907  0.623   58.495  1.00 19.54 ? 167 THR B CG2 1 
ATOM   2811 N  N   . HIS B 1 180 ? -10.291 -0.289  55.314  1.00 13.18 ? 168 HIS B N   1 
ATOM   2812 C  CA  . HIS B 1 180 ? -10.341 0.381   54.023  1.00 12.39 ? 168 HIS B CA  1 
ATOM   2813 C  C   . HIS B 1 180 ? -9.901  1.834   54.124  1.00 13.85 ? 168 HIS B C   1 
ATOM   2814 O  O   . HIS B 1 180 ? -10.344 2.573   55.007  1.00 15.08 ? 168 HIS B O   1 
ATOM   2815 C  CB  . HIS B 1 180 ? -11.751 0.297   53.447  1.00 13.67 ? 168 HIS B CB  1 
ATOM   2816 C  CG  . HIS B 1 180 ? -12.056 -1.034  52.848  1.00 17.75 ? 168 HIS B CG  1 
ATOM   2817 N  ND1 . HIS B 1 180 ? -11.856 -1.305  51.514  1.00 19.68 ? 168 HIS B ND1 1 
ATOM   2818 C  CD2 . HIS B 1 180 ? -12.500 -2.184  53.405  1.00 24.81 ? 168 HIS B CD2 1 
ATOM   2819 C  CE1 . HIS B 1 180 ? -12.178 -2.561  51.269  1.00 24.31 ? 168 HIS B CE1 1 
ATOM   2820 N  NE2 . HIS B 1 180 ? -12.579 -3.115  52.399  1.00 25.06 ? 168 HIS B NE2 1 
ATOM   2821 N  N   . ASN B 1 181 ? -9.012  2.234   53.212  1.00 8.75  ? 169 ASN B N   1 
ATOM   2822 C  CA  . ASN B 1 181 ? -8.730  3.644   52.979  1.00 9.68  ? 169 ASN B CA  1 
ATOM   2823 C  C   . ASN B 1 181 ? -9.502  4.055   51.723  1.00 10.18 ? 169 ASN B C   1 
ATOM   2824 O  O   . ASN B 1 181 ? -10.653 3.658   51.564  1.00 10.89 ? 169 ASN B O   1 
ATOM   2825 C  CB  . ASN B 1 181 ? -7.222  3.880   52.864  1.00 10.40 ? 169 ASN B CB  1 
ATOM   2826 C  CG  . ASN B 1 181 ? -6.834  5.348   53.055  1.00 16.33 ? 169 ASN B CG  1 
ATOM   2827 O  OD1 . ASN B 1 181 ? -6.743  6.102   52.091  1.00 14.55 ? 169 ASN B OD1 1 
ATOM   2828 N  ND2 . ASN B 1 181 ? -6.588  5.752   54.303  1.00 17.29 ? 169 ASN B ND2 1 
ATOM   2829 N  N   . TYR B 1 182 ? -8.911  4.822   50.818  1.00 10.17 ? 170 TYR B N   1 
ATOM   2830 C  CA  . TYR B 1 182 ? -9.742  5.316   49.720  1.00 8.81  ? 170 TYR B CA  1 
ATOM   2831 C  C   . TYR B 1 182 ? -10.064 4.225   48.694  1.00 9.71  ? 170 TYR B C   1 
ATOM   2832 O  O   . TYR B 1 182 ? -9.416  3.181   48.623  1.00 8.57  ? 170 TYR B O   1 
ATOM   2833 C  CB  . TYR B 1 182 ? -9.077  6.519   49.042  1.00 9.32  ? 170 TYR B CB  1 
ATOM   2834 C  CG  . TYR B 1 182 ? -7.831  6.307   48.189  1.00 8.88  ? 170 TYR B CG  1 
ATOM   2835 C  CD1 . TYR B 1 182 ? -7.909  5.725   46.923  1.00 8.57  ? 170 TYR B CD1 1 
ATOM   2836 C  CD2 . TYR B 1 182 ? -6.592  6.782   48.611  1.00 12.72 ? 170 TYR B CD2 1 
ATOM   2837 C  CE1 . TYR B 1 182 ? -6.771  5.582   46.128  1.00 10.43 ? 170 TYR B CE1 1 
ATOM   2838 C  CE2 . TYR B 1 182 ? -5.459  6.651   47.828  1.00 10.36 ? 170 TYR B CE2 1 
ATOM   2839 C  CZ  . TYR B 1 182 ? -5.555  6.054   46.582  1.00 9.86  ? 170 TYR B CZ  1 
ATOM   2840 O  OH  . TYR B 1 182 ? -4.419  5.913   45.813  1.00 10.91 ? 170 TYR B OH  1 
ATOM   2841 N  N   . MET B 1 183 ? -11.106 4.492   47.899  1.00 7.80  ? 171 MET B N   1 
ATOM   2842 C  CA  . MET B 1 183 ? -11.498 3.659   46.761  1.00 6.60  ? 171 MET B CA  1 
ATOM   2843 C  C   . MET B 1 183 ? -11.971 4.598   45.656  1.00 10.03 ? 171 MET B C   1 
ATOM   2844 O  O   . MET B 1 183 ? -12.829 5.448   45.904  1.00 9.53  ? 171 MET B O   1 
ATOM   2845 C  CB  . MET B 1 183 ? -12.607 2.676   47.142  1.00 8.72  ? 171 MET B CB  1 
ATOM   2846 C  CG  . MET B 1 183 ? -13.037 1.752   46.001  1.00 9.97  ? 171 MET B CG  1 
ATOM   2847 S  SD  . MET B 1 183 ? -14.190 0.469   46.564  1.00 13.95 ? 171 MET B SD  1 
ATOM   2848 C  CE  . MET B 1 183 ? -15.639 1.466   46.832  1.00 14.41 ? 171 MET B CE  1 
ATOM   2849 N  N   . ILE B 1 184 ? -11.401 4.471   44.452  1.00 6.80  ? 172 ILE B N   1 
ATOM   2850 C  CA  . ILE B 1 184 ? -11.714 5.384   43.360  1.00 7.00  ? 172 ILE B CA  1 
ATOM   2851 C  C   . ILE B 1 184 ? -11.943 4.579   42.093  1.00 7.80  ? 172 ILE B C   1 
ATOM   2852 O  O   . ILE B 1 184 ? -11.530 3.423   41.977  1.00 7.50  ? 172 ILE B O   1 
ATOM   2853 C  CB  . ILE B 1 184 ? -10.604 6.432   43.120  1.00 8.47  ? 172 ILE B CB  1 
ATOM   2854 C  CG1 . ILE B 1 184 ? -9.252  5.768   42.813  1.00 7.63  ? 172 ILE B CG1 1 
ATOM   2855 C  CG2 . ILE B 1 184 ? -10.471 7.377   44.325  1.00 10.33 ? 172 ILE B CG2 1 
ATOM   2856 C  CD1 . ILE B 1 184 ? -8.173  6.773   42.409  1.00 9.59  ? 172 ILE B CD1 1 
ATOM   2857 N  N   . VAL B 1 185 ? -12.593 5.220   41.125  1.00 8.10  ? 173 VAL B N   1 
ATOM   2858 C  CA  . VAL B 1 185 ? -12.625 4.720   39.753  1.00 7.76  ? 173 VAL B CA  1 
ATOM   2859 C  C   . VAL B 1 185 ? -11.453 5.367   39.032  1.00 9.02  ? 173 VAL B C   1 
ATOM   2860 O  O   . VAL B 1 185 ? -11.476 6.567   38.743  1.00 9.67  ? 173 VAL B O   1 
ATOM   2861 C  CB  . VAL B 1 185 ? -13.953 5.042   39.060  1.00 9.45  ? 173 VAL B CB  1 
ATOM   2862 C  CG1 . VAL B 1 185 ? -13.945 4.501   37.635  1.00 9.90  ? 173 VAL B CG1 1 
ATOM   2863 C  CG2 . VAL B 1 185 ? -15.117 4.432   39.842  1.00 10.64 ? 173 VAL B CG2 1 
ATOM   2864 N  N   . ALA B 1 186 ? -10.420 4.575   38.759  1.00 6.80  ? 174 ALA B N   1 
ATOM   2865 C  CA  . ALA B 1 186 ? -9.107  5.089   38.409  1.00 8.35  ? 174 ALA B CA  1 
ATOM   2866 C  C   . ALA B 1 186 ? -8.772  4.809   36.953  1.00 10.64 ? 174 ALA B C   1 
ATOM   2867 O  O   . ALA B 1 186 ? -9.035  3.715   36.444  1.00 10.94 ? 174 ALA B O   1 
ATOM   2868 C  CB  . ALA B 1 186 ? -8.032  4.462   39.295  1.00 9.70  ? 174 ALA B CB  1 
ATOM   2869 N  N   . THR B 1 187 ? -8.196  5.817   36.301  1.00 9.19  ? 175 THR B N   1 
ATOM   2870 C  CA  . THR B 1 187 ? -7.504  5.683   35.028  1.00 7.27  ? 175 THR B CA  1 
ATOM   2871 C  C   . THR B 1 187 ? -6.009  5.613   35.308  1.00 9.05  ? 175 THR B C   1 
ATOM   2872 O  O   . THR B 1 187 ? -5.470  6.451   36.047  1.00 9.01  ? 175 THR B O   1 
ATOM   2873 C  CB  . THR B 1 187 ? -7.807  6.875   34.118  1.00 10.77 ? 175 THR B CB  1 
ATOM   2874 O  OG1 . THR B 1 187 ? -9.217  6.936   33.870  1.00 10.16 ? 175 THR B OG1 1 
ATOM   2875 C  CG2 . THR B 1 187 ? -7.065  6.734   32.781  1.00 10.28 ? 175 THR B CG2 1 
ATOM   2876 N  N   . ALA B 1 188 ? -5.344  4.609   34.745  1.00 7.45  ? 176 ALA B N   1 
ATOM   2877 C  CA  . ALA B 1 188 ? -3.913  4.428   34.959  1.00 8.30  ? 176 ALA B CA  1 
ATOM   2878 C  C   . ALA B 1 188 ? -3.212  4.290   33.615  1.00 10.58 ? 176 ALA B C   1 
ATOM   2879 O  O   . ALA B 1 188 ? -3.784  3.777   32.655  1.00 9.79  ? 176 ALA B O   1 
ATOM   2880 C  CB  . ALA B 1 188 ? -3.619  3.193   35.815  1.00 10.64 ? 176 ALA B CB  1 
ATOM   2881 N  N   . GLY B 1 189 ? -1.960  4.732   33.549  1.00 9.59  ? 177 GLY B N   1 
ATOM   2882 C  CA  . GLY B 1 189 ? -1.223  4.599   32.304  1.00 11.11 ? 177 GLY B CA  1 
ATOM   2883 C  C   . GLY B 1 189 ? 0.264   4.529   32.562  1.00 13.02 ? 177 GLY B C   1 
ATOM   2884 O  O   . GLY B 1 189 ? 0.760   4.978   33.602  1.00 13.66 ? 177 GLY B O   1 
ATOM   2885 N  N   . TYR B 1 190 ? 0.970   3.936   31.604  1.00 12.39 ? 178 TYR B N   1 
ATOM   2886 C  CA  . TYR B 1 190 ? 2.422   3.878   31.688  1.00 14.62 ? 178 TYR B CA  1 
ATOM   2887 C  C   . TYR B 1 190 ? 2.997   3.857   30.282  1.00 13.01 ? 178 TYR B C   1 
ATOM   2888 O  O   . TYR B 1 190 ? 2.612   3.018   29.460  1.00 12.59 ? 178 TYR B O   1 
ATOM   2889 C  CB  . TYR B 1 190 ? 2.904   2.656   32.467  1.00 16.18 ? 178 TYR B CB  1 
ATOM   2890 C  CG  . TYR B 1 190 ? 4.427   2.611   32.580  1.00 24.07 ? 178 TYR B CG  1 
ATOM   2891 C  CD1 . TYR B 1 190 ? 5.123   3.527   33.354  1.00 26.11 ? 178 TYR B CD1 1 
ATOM   2892 C  CD2 . TYR B 1 190 ? 5.160   1.676   31.884  1.00 25.59 ? 178 TYR B CD2 1 
ATOM   2893 C  CE1 . TYR B 1 190 ? 6.516   3.484   33.447  1.00 28.53 ? 178 TYR B CE1 1 
ATOM   2894 C  CE2 . TYR B 1 190 ? 6.526   1.618   31.969  1.00 33.55 ? 178 TYR B CE2 1 
ATOM   2895 C  CZ  . TYR B 1 190 ? 7.212   2.518   32.749  1.00 36.33 ? 178 TYR B CZ  1 
ATOM   2896 O  OH  . TYR B 1 190 ? 8.596   2.439   32.811  1.00 35.88 ? 178 TYR B OH  1 
ATOM   2897 N  N   . GLN B 1 191 ? 3.921   4.777   30.017  1.00 12.88 ? 179 GLN B N   1 
ATOM   2898 C  CA  . GLN B 1 191 ? 4.603   4.874   28.729  1.00 13.90 ? 179 GLN B CA  1 
ATOM   2899 C  C   . GLN B 1 191 ? 3.594   4.814   27.585  1.00 12.36 ? 179 GLN B C   1 
ATOM   2900 O  O   . GLN B 1 191 ? 3.711   4.021   26.649  1.00 12.51 ? 179 GLN B O   1 
ATOM   2901 C  CB  . GLN B 1 191 ? 5.690   3.804   28.602  1.00 17.89 ? 179 GLN B CB  1 
ATOM   2902 C  CG  . GLN B 1 191 ? 6.773   3.999   29.670  1.00 20.43 ? 179 GLN B CG  1 
ATOM   2903 C  CD  . GLN B 1 191 ? 8.178   3.599   29.234  1.00 29.64 ? 179 GLN B CD  1 
ATOM   2904 O  OE1 . GLN B 1 191 ? 8.374   2.566   28.594  1.00 32.40 ? 179 GLN B OE1 1 
ATOM   2905 N  NE2 . GLN B 1 191 ? 9.171   4.403   29.621  1.00 32.26 ? 179 GLN B NE2 1 
ATOM   2906 N  N   . SER B 1 192 ? 2.599   5.692   27.674  1.00 11.93 ? 180 SER B N   1 
ATOM   2907 C  CA  . SER B 1 192 ? 1.498   5.727   26.724  1.00 12.86 ? 180 SER B CA  1 
ATOM   2908 C  C   . SER B 1 192 ? 0.991   7.159   26.601  1.00 11.48 ? 180 SER B C   1 
ATOM   2909 O  O   . SER B 1 192 ? 1.499   8.083   27.241  1.00 12.34 ? 180 SER B O   1 
ATOM   2910 C  CB  . SER B 1 192 ? 0.381   4.761   27.166  1.00 12.83 ? 180 SER B CB  1 
ATOM   2911 O  OG  . SER B 1 192 ? -0.212  5.208   28.367  1.00 12.23 ? 180 SER B OG  1 
ATOM   2912 N  N   . SER B 1 193 ? 0.003   7.340   25.729  1.00 12.88 ? 181 SER B N   1 
ATOM   2913 C  CA  . SER B 1 193 ? -0.738  8.581   25.601  1.00 12.33 ? 181 SER B CA  1 
ATOM   2914 C  C   . SER B 1 193 ? -2.212  8.224   25.642  1.00 11.72 ? 181 SER B C   1 
ATOM   2915 O  O   . SER B 1 193 ? -2.593  7.054   25.521  1.00 13.10 ? 181 SER B O   1 
ATOM   2916 C  CB  . SER B 1 193 ? -0.406  9.342   24.303  1.00 14.37 ? 181 SER B CB  1 
ATOM   2917 O  OG  . SER B 1 193 ? 0.986   9.589   24.183  1.00 16.23 ? 181 SER B OG  1 
ATOM   2918 N  N   . GLY B 1 194 ? -3.049  9.229   25.838  1.00 10.92 ? 182 GLY B N   1 
ATOM   2919 C  CA  . GLY B 1 194 ? -4.469  8.971   25.796  1.00 12.39 ? 182 GLY B CA  1 
ATOM   2920 C  C   . GLY B 1 194 ? -5.264  10.100  26.414  1.00 12.90 ? 182 GLY B C   1 
ATOM   2921 O  O   . GLY B 1 194 ? -4.736  11.157  26.768  1.00 13.72 ? 182 GLY B O   1 
ATOM   2922 N  N   . SER B 1 195 ? -6.561  9.848   26.508  1.00 11.55 ? 183 SER B N   1 
ATOM   2923 C  CA  . SER B 1 195 ? -7.436  10.738  27.237  1.00 12.68 ? 183 SER B CA  1 
ATOM   2924 C  C   . SER B 1 195 ? -8.560  9.896   27.806  1.00 13.40 ? 183 SER B C   1 
ATOM   2925 O  O   . SER B 1 195 ? -8.898  8.837   27.275  1.00 14.45 ? 183 SER B O   1 
ATOM   2926 C  CB  . SER B 1 195 ? -8.001  11.842  26.345  1.00 16.40 ? 183 SER B CB  1 
ATOM   2927 O  OG  . SER B 1 195 ? -8.862  11.272  25.391  1.00 18.10 ? 183 SER B OG  1 
ATOM   2928 N  N   . ALA B 1 196 ? -9.151  10.396  28.881  1.00 10.84 ? 184 ALA B N   1 
ATOM   2929 C  CA  . ALA B 1 196 ? -10.273 9.724   29.507  1.00 10.05 ? 184 ALA B CA  1 
ATOM   2930 C  C   . ALA B 1 196 ? -11.133 10.780  30.167  1.00 13.47 ? 184 ALA B C   1 
ATOM   2931 O  O   . ALA B 1 196 ? -10.640 11.820  30.604  1.00 12.23 ? 184 ALA B O   1 
ATOM   2932 C  CB  . ALA B 1 196 ? -9.823  8.691   30.543  1.00 11.35 ? 184 ALA B CB  1 
ATOM   2933 N  N   . SER B 1 197 ? -12.425 10.499  30.234  1.00 9.86  ? 185 SER B N   1 
ATOM   2934 C  CA  . SER B 1 197 ? -13.382 11.371  30.905  1.00 10.60 ? 185 SER B CA  1 
ATOM   2935 C  C   . SER B 1 197 ? -14.390 10.456  31.584  1.00 9.48  ? 185 SER B C   1 
ATOM   2936 O  O   . SER B 1 197 ? -15.172 9.790   30.905  1.00 12.00 ? 185 SER B O   1 
ATOM   2937 C  CB  . SER B 1 197 ? -14.067 12.318  29.920  1.00 17.23 ? 185 SER B CB  1 
ATOM   2938 O  OG  . SER B 1 197 ? -15.010 13.133  30.596  1.00 21.28 ? 185 SER B OG  1 
ATOM   2939 N  N   . ILE B 1 198 ? -14.355 10.405  32.912  1.00 9.10  ? 186 ILE B N   1 
ATOM   2940 C  CA  . ILE B 1 198 ? -15.081 9.411   33.693  1.00 11.71 ? 186 ILE B CA  1 
ATOM   2941 C  C   . ILE B 1 198 ? -15.950 10.132  34.714  1.00 11.81 ? 186 ILE B C   1 
ATOM   2942 O  O   . ILE B 1 198 ? -15.498 11.078  35.365  1.00 11.61 ? 186 ILE B O   1 
ATOM   2943 C  CB  . ILE B 1 198 ? -14.105 8.439   34.400  1.00 10.85 ? 186 ILE B CB  1 
ATOM   2944 C  CG1 . ILE B 1 198 ? -13.290 7.647   33.368  1.00 10.56 ? 186 ILE B CG1 1 
ATOM   2945 C  CG2 . ILE B 1 198 ? -14.831 7.514   35.376  1.00 12.73 ? 186 ILE B CG2 1 
ATOM   2946 C  CD1 . ILE B 1 198 ? -14.117 6.636   32.572  1.00 12.59 ? 186 ILE B CD1 1 
ATOM   2947 N  N   . THR B 1 199 ? -17.201 9.699   34.852  1.00 9.95  ? 187 THR B N   1 
ATOM   2948 C  CA  . THR B 1 199 ? -18.092 10.274  35.856  1.00 12.96 ? 187 THR B CA  1 
ATOM   2949 C  C   . THR B 1 199 ? -18.539 9.180   36.814  1.00 14.00 ? 187 THR B C   1 
ATOM   2950 O  O   . THR B 1 199 ? -19.226 8.241   36.408  1.00 15.88 ? 187 THR B O   1 
ATOM   2951 C  CB  . THR B 1 199 ? -19.308 10.943  35.220  1.00 17.45 ? 187 THR B CB  1 
ATOM   2952 O  OG1 . THR B 1 199 ? -18.878 12.051  34.420  1.00 18.97 ? 187 THR B OG1 1 
ATOM   2953 C  CG2 . THR B 1 199 ? -20.237 11.454  36.310  1.00 18.09 ? 187 THR B CG2 1 
ATOM   2954 N  N   . VAL B 1 200 ? -18.138 9.301   38.075  1.00 12.09 ? 188 VAL B N   1 
ATOM   2955 C  CA  . VAL B 1 200 ? -18.590 8.387   39.112  1.00 13.94 ? 188 VAL B CA  1 
ATOM   2956 C  C   . VAL B 1 200 ? -19.949 8.870   39.604  1.00 18.13 ? 188 VAL B C   1 
ATOM   2957 O  O   . VAL B 1 200 ? -20.134 10.065  39.854  1.00 18.32 ? 188 VAL B O   1 
ATOM   2958 C  CB  . VAL B 1 200 ? -17.567 8.333   40.259  1.00 13.73 ? 188 VAL B CB  1 
ATOM   2959 C  CG1 . VAL B 1 200 ? -18.021 7.383   41.316  1.00 18.42 ? 188 VAL B CG1 1 
ATOM   2960 C  CG2 . VAL B 1 200 ? -16.186 7.956   39.726  1.00 14.60 ? 188 VAL B CG2 1 
ATOM   2961 N  N   . GLN B 1 201 ? -20.916 7.957   39.706  1.00 21.33 ? 189 GLN B N   1 
ATOM   2962 C  CA  . GLN B 1 201 ? -22.264 8.331   40.164  1.00 27.01 ? 189 GLN B CA  1 
ATOM   2963 C  C   . GLN B 1 201 ? -22.694 7.545   41.397  1.00 29.09 ? 189 GLN B C   1 
ATOM   2964 O  O   . GLN B 1 201 ? -21.866 7.190   42.241  1.00 32.82 ? 189 GLN B O   1 
ATOM   2965 C  CB  . GLN B 1 201 ? -23.298 8.126   39.058  1.00 28.51 ? 189 GLN B CB  1 
ATOM   2966 C  CG  . GLN B 1 201 ? -23.020 8.891   37.779  1.00 36.36 ? 189 GLN B CG  1 
ATOM   2967 C  CD  . GLN B 1 201 ? -22.544 7.978   36.668  1.00 31.52 ? 189 GLN B CD  1 
ATOM   2968 O  OE1 . GLN B 1 201 ? -22.576 6.754   36.806  1.00 34.68 ? 189 GLN B OE1 1 
ATOM   2969 N  NE2 . GLN B 1 201 ? -22.101 8.566   35.559  1.00 33.09 ? 189 GLN B NE2 1 
ATOM   2970 N  N   . GLU C 1 13  ? -1.122  10.354  15.234  1.00 34.07 ? 1   GLU C N   1 
ATOM   2971 C  CA  . GLU C 1 13  ? -0.714  9.726   13.982  1.00 30.69 ? 1   GLU C CA  1 
ATOM   2972 C  C   . GLU C 1 13  ? 0.276   10.594  13.200  1.00 27.94 ? 1   GLU C C   1 
ATOM   2973 O  O   . GLU C 1 13  ? 1.260   10.078  12.689  1.00 28.82 ? 1   GLU C O   1 
ATOM   2974 C  CB  . GLU C 1 13  ? -1.934  9.406   13.115  1.00 35.21 ? 1   GLU C CB  1 
ATOM   2975 C  CG  . GLU C 1 13  ? -1.638  8.577   11.873  1.00 28.84 ? 1   GLU C CG  1 
ATOM   2976 C  CD  . GLU C 1 13  ? -1.805  7.074   12.106  1.00 40.43 ? 1   GLU C CD  1 
ATOM   2977 O  OE1 . GLU C 1 13  ? -0.925  6.445   12.740  1.00 39.56 ? 1   GLU C OE1 1 
ATOM   2978 O  OE2 . GLU C 1 13  ? -2.830  6.519   11.647  1.00 42.51 ? 1   GLU C OE2 1 
ATOM   2979 N  N   . ILE C 1 14  ? 0.032   11.903  13.108  1.00 17.88 ? 2   ILE C N   1 
ATOM   2980 C  CA  . ILE C 1 14  ? 0.910   12.822  12.386  1.00 17.97 ? 2   ILE C CA  1 
ATOM   2981 C  C   . ILE C 1 14  ? 1.387   13.902  13.358  1.00 21.16 ? 2   ILE C C   1 
ATOM   2982 O  O   . ILE C 1 14  ? 0.570   14.554  14.016  1.00 18.72 ? 2   ILE C O   1 
ATOM   2983 C  CB  . ILE C 1 14  ? 0.200   13.438  11.163  1.00 20.59 ? 2   ILE C CB  1 
ATOM   2984 C  CG1 . ILE C 1 14  ? -0.102  12.352  10.117  1.00 21.03 ? 2   ILE C CG1 1 
ATOM   2985 C  CG2 . ILE C 1 14  ? 1.034   14.533  10.545  1.00 21.82 ? 2   ILE C CG2 1 
ATOM   2986 C  CD1 . ILE C 1 14  ? -1.134  12.763  9.068   1.00 23.59 ? 2   ILE C CD1 1 
ATOM   2987 N  N   . THR C 1 15  ? 2.711   14.075  13.473  1.00 18.91 ? 3   THR C N   1 
ATOM   2988 C  CA  . THR C 1 15  ? 3.254   15.038  14.428  1.00 15.27 ? 3   THR C CA  1 
ATOM   2989 C  C   . THR C 1 15  ? 4.283   15.995  13.831  1.00 20.18 ? 3   THR C C   1 
ATOM   2990 O  O   . THR C 1 15  ? 4.786   16.866  14.555  1.00 17.91 ? 3   THR C O   1 
ATOM   2991 C  CB  . THR C 1 15  ? 3.873   14.316  15.638  1.00 24.51 ? 3   THR C CB  1 
ATOM   2992 O  OG1 . THR C 1 15  ? 4.917   13.441  15.197  1.00 26.29 ? 3   THR C OG1 1 
ATOM   2993 C  CG2 . THR C 1 15  ? 2.815   13.514  16.403  1.00 23.83 ? 3   THR C CG2 1 
ATOM   2994 N  N   . SER C 1 16  ? 4.607   15.858  12.547  1.00 17.28 ? 4   SER C N   1 
ATOM   2995 C  CA  . SER C 1 16  ? 5.431   16.795  11.801  1.00 19.80 ? 4   SER C CA  1 
ATOM   2996 C  C   . SER C 1 16  ? 4.675   17.219  10.552  1.00 17.40 ? 4   SER C C   1 
ATOM   2997 O  O   . SER C 1 16  ? 3.738   16.541  10.122  1.00 18.01 ? 4   SER C O   1 
ATOM   2998 C  CB  . SER C 1 16  ? 6.776   16.171  11.406  1.00 20.85 ? 4   SER C CB  1 
ATOM   2999 O  OG  . SER C 1 16  ? 7.695   16.274  12.475  1.00 29.85 ? 4   SER C OG  1 
ATOM   3000 N  N   . SER C 1 17  ? 5.100   18.340  9.963   1.00 17.84 ? 5   SER C N   1 
ATOM   3001 C  CA  . SER C 1 17  ? 4.361   18.929  8.848   1.00 14.74 ? 5   SER C CA  1 
ATOM   3002 C  C   . SER C 1 17  ? 4.252   17.959  7.679   1.00 20.54 ? 5   SER C C   1 
ATOM   3003 O  O   . SER C 1 17  ? 5.212   17.267  7.324   1.00 16.31 ? 5   SER C O   1 
ATOM   3004 C  CB  . SER C 1 17  ? 5.030   20.228  8.377   1.00 16.40 ? 5   SER C CB  1 
ATOM   3005 O  OG  . SER C 1 17  ? 5.102   21.178  9.428   1.00 15.79 ? 5   SER C OG  1 
ATOM   3006 N  N   . GLU C 1 18  ? 3.071   17.944  7.063   1.00 15.22 ? 6   GLU C N   1 
ATOM   3007 C  CA  . GLU C 1 18  ? 2.723   16.979  6.035   1.00 17.72 ? 6   GLU C CA  1 
ATOM   3008 C  C   . GLU C 1 18  ? 1.508   17.516  5.291   1.00 17.59 ? 6   GLU C C   1 
ATOM   3009 O  O   . GLU C 1 18  ? 0.653   18.173  5.890   1.00 17.44 ? 6   GLU C O   1 
ATOM   3010 C  CB  . GLU C 1 18  ? 2.407   15.616  6.665   1.00 14.82 ? 6   GLU C CB  1 
ATOM   3011 C  CG  . GLU C 1 18  ? 2.239   14.484  5.690   1.00 27.37 ? 6   GLU C CG  1 
ATOM   3012 C  CD  . GLU C 1 18  ? 1.946   13.178  6.396   1.00 30.24 ? 6   GLU C CD  1 
ATOM   3013 O  OE1 . GLU C 1 18  ? 0.810   12.676  6.262   1.00 26.14 ? 6   GLU C OE1 1 
ATOM   3014 O  OE2 . GLU C 1 18  ? 2.850   12.661  7.092   1.00 30.45 ? 6   GLU C OE2 1 
ATOM   3015 N  N   . THR C 1 19  ? 1.448   17.258  3.987   1.00 15.95 ? 7   THR C N   1 
ATOM   3016 C  CA  . THR C 1 19  ? 0.250   17.518  3.201   1.00 13.37 ? 7   THR C CA  1 
ATOM   3017 C  C   . THR C 1 19  ? -0.023  16.296  2.346   1.00 16.85 ? 7   THR C C   1 
ATOM   3018 O  O   . THR C 1 19  ? 0.864   15.475  2.095   1.00 14.56 ? 7   THR C O   1 
ATOM   3019 C  CB  . THR C 1 19  ? 0.372   18.740  2.277   1.00 18.17 ? 7   THR C CB  1 
ATOM   3020 O  OG1 . THR C 1 19  ? 1.343   18.479  1.247   1.00 21.28 ? 7   THR C OG1 1 
ATOM   3021 C  CG2 . THR C 1 19  ? 0.779   19.975  3.061   1.00 18.26 ? 7   THR C CG2 1 
ATOM   3022 N  N   . GLY C 1 20  ? -1.260  16.190  1.884   1.00 14.22 ? 8   GLY C N   1 
ATOM   3023 C  CA  . GLY C 1 20  ? -1.609  15.070  1.035   1.00 16.45 ? 8   GLY C CA  1 
ATOM   3024 C  C   . GLY C 1 20  ? -3.095  15.036  0.765   1.00 15.53 ? 8   GLY C C   1 
ATOM   3025 O  O   . GLY C 1 20  ? -3.798  16.036  0.922   1.00 12.90 ? 8   GLY C O   1 
ATOM   3026 N  N   . THR C 1 21  ? -3.549  13.869  0.337   1.00 11.58 ? 9   THR C N   1 
ATOM   3027 C  CA  . THR C 1 21  ? -4.963  13.593  0.131   1.00 8.93  ? 9   THR C CA  1 
ATOM   3028 C  C   . THR C 1 21  ? -5.400  12.559  1.152   1.00 11.89 ? 9   THR C C   1 
ATOM   3029 O  O   . THR C 1 21  ? -4.679  11.595  1.402   1.00 12.58 ? 9   THR C O   1 
ATOM   3030 C  CB  . THR C 1 21  ? -5.213  13.041  -1.277  1.00 13.30 ? 9   THR C CB  1 
ATOM   3031 O  OG1 . THR C 1 21  ? -4.605  13.903  -2.246  1.00 15.79 ? 9   THR C OG1 1 
ATOM   3032 C  CG2 . THR C 1 21  ? -6.713  12.928  -1.561  1.00 12.28 ? 9   THR C CG2 1 
ATOM   3033 N  N   . ASN C 1 22  ? -6.585  12.743  1.728   1.00 11.28 ? 10  ASN C N   1 
ATOM   3034 C  CA  . ASN C 1 22  ? -7.144  11.733  2.623   1.00 11.74 ? 10  ASN C CA  1 
ATOM   3035 C  C   . ASN C 1 22  ? -8.646  11.651  2.394   1.00 11.38 ? 10  ASN C C   1 
ATOM   3036 O  O   . ASN C 1 22  ? -9.373  12.598  2.696   1.00 12.01 ? 10  ASN C O   1 
ATOM   3037 C  CB  . ASN C 1 22  ? -6.830  12.042  4.082   1.00 10.40 ? 10  ASN C CB  1 
ATOM   3038 C  CG  . ASN C 1 22  ? -7.346  10.971  5.009   1.00 12.47 ? 10  ASN C CG  1 
ATOM   3039 O  OD1 . ASN C 1 22  ? -8.400  11.126  5.612   1.00 12.04 ? 10  ASN C OD1 1 
ATOM   3040 N  ND2 . ASN C 1 22  ? -6.619  9.862   5.101   1.00 13.74 ? 10  ASN C ND2 1 
ATOM   3041 N  N   . ASN C 1 23  ? -9.108  10.520  1.856   1.00 10.76 ? 11  ASN C N   1 
ATOM   3042 C  CA  . ASN C 1 23  ? -10.540 10.257  1.706   1.00 13.10 ? 11  ASN C CA  1 
ATOM   3043 C  C   . ASN C 1 23  ? -11.228 11.344  0.884   1.00 16.47 ? 11  ASN C C   1 
ATOM   3044 O  O   . ASN C 1 23  ? -12.330 11.795  1.206   1.00 16.62 ? 11  ASN C O   1 
ATOM   3045 C  CB  . ASN C 1 23  ? -11.199 10.075  3.080   1.00 17.20 ? 11  ASN C CB  1 
ATOM   3046 C  CG  . ASN C 1 23  ? -10.632 8.878   3.830   1.00 18.53 ? 11  ASN C CG  1 
ATOM   3047 O  OD1 . ASN C 1 23  ? -10.454 7.816   3.250   1.00 20.87 ? 11  ASN C OD1 1 
ATOM   3048 N  ND2 . ASN C 1 23  ? -10.335 9.050   5.118   1.00 18.46 ? 11  ASN C ND2 1 
ATOM   3049 N  N   . GLY C 1 24  ? -10.568 11.765  -0.195  1.00 12.44 ? 12  GLY C N   1 
ATOM   3050 C  CA  . GLY C 1 24  ? -11.124 12.713  -1.135  1.00 15.63 ? 12  GLY C CA  1 
ATOM   3051 C  C   . GLY C 1 24  ? -10.951 14.161  -0.750  1.00 15.35 ? 12  GLY C C   1 
ATOM   3052 O  O   . GLY C 1 24  ? -11.471 15.039  -1.458  1.00 15.74 ? 12  GLY C O   1 
ATOM   3053 N  N   . TYR C 1 25  ? -10.261 14.441  0.352   1.00 11.77 ? 13  TYR C N   1 
ATOM   3054 C  CA  . TYR C 1 25  ? -10.001 15.805  0.786   1.00 11.00 ? 13  TYR C CA  1 
ATOM   3055 C  C   . TYR C 1 25  ? -8.510  16.097  0.754   1.00 11.20 ? 13  TYR C C   1 
ATOM   3056 O  O   . TYR C 1 25  ? -7.682  15.240  1.095   1.00 12.28 ? 13  TYR C O   1 
ATOM   3057 C  CB  . TYR C 1 25  ? -10.553 16.051  2.204   1.00 11.73 ? 13  TYR C CB  1 
ATOM   3058 C  CG  . TYR C 1 25  ? -12.058 16.072  2.192   1.00 11.47 ? 13  TYR C CG  1 
ATOM   3059 C  CD1 . TYR C 1 25  ? -12.787 14.890  2.306   1.00 14.15 ? 13  TYR C CD1 1 
ATOM   3060 C  CD2 . TYR C 1 25  ? -12.747 17.256  1.993   1.00 15.44 ? 13  TYR C CD2 1 
ATOM   3061 C  CE1 . TYR C 1 25  ? -14.163 14.897  2.261   1.00 15.86 ? 13  TYR C CE1 1 
ATOM   3062 C  CE2 . TYR C 1 25  ? -14.125 17.271  1.941   1.00 20.14 ? 13  TYR C CE2 1 
ATOM   3063 C  CZ  . TYR C 1 25  ? -14.824 16.094  2.079   1.00 21.86 ? 13  TYR C CZ  1 
ATOM   3064 O  OH  . TYR C 1 25  ? -16.198 16.127  2.025   1.00 28.27 ? 13  TYR C OH  1 
ATOM   3065 N  N   . TYR C 1 26  ? -8.179  17.316  0.341   1.00 11.60 ? 14  TYR C N   1 
ATOM   3066 C  CA  . TYR C 1 26  ? -6.857  17.850  0.605   1.00 8.25  ? 14  TYR C CA  1 
ATOM   3067 C  C   . TYR C 1 26  ? -6.699  18.043  2.108   1.00 10.84 ? 14  TYR C C   1 
ATOM   3068 O  O   . TYR C 1 26  ? -7.646  18.438  2.791   1.00 9.31  ? 14  TYR C O   1 
ATOM   3069 C  CB  . TYR C 1 26  ? -6.670  19.182  -0.118  1.00 10.90 ? 14  TYR C CB  1 
ATOM   3070 C  CG  . TYR C 1 26  ? -5.379  19.873  0.236   1.00 10.31 ? 14  TYR C CG  1 
ATOM   3071 C  CD1 . TYR C 1 26  ? -4.195  19.547  -0.420  1.00 13.11 ? 14  TYR C CD1 1 
ATOM   3072 C  CD2 . TYR C 1 26  ? -5.336  20.848  1.229   1.00 11.76 ? 14  TYR C CD2 1 
ATOM   3073 C  CE1 . TYR C 1 26  ? -3.002  20.165  -0.089  1.00 13.14 ? 14  TYR C CE1 1 
ATOM   3074 C  CE2 . TYR C 1 26  ? -4.141  21.468  1.573   1.00 12.27 ? 14  TYR C CE2 1 
ATOM   3075 C  CZ  . TYR C 1 26  ? -2.984  21.124  0.907   1.00 15.46 ? 14  TYR C CZ  1 
ATOM   3076 O  OH  . TYR C 1 26  ? -1.801  21.736  1.237   1.00 14.35 ? 14  TYR C OH  1 
ATOM   3077 N  N   . TYR C 1 27  ? -5.509  17.755  2.631   1.00 10.15 ? 15  TYR C N   1 
ATOM   3078 C  CA  . TYR C 1 27  ? -5.215  18.126  4.010   1.00 9.57  ? 15  TYR C CA  1 
ATOM   3079 C  C   . TYR C 1 27  ? -3.833  18.741  4.099   1.00 12.75 ? 15  TYR C C   1 
ATOM   3080 O  O   . TYR C 1 27  ? -2.915  18.394  3.350   1.00 11.86 ? 15  TYR C O   1 
ATOM   3081 C  CB  . TYR C 1 27  ? -5.317  16.939  5.016   1.00 11.59 ? 15  TYR C CB  1 
ATOM   3082 C  CG  . TYR C 1 27  ? -4.194  15.921  4.940   1.00 12.99 ? 15  TYR C CG  1 
ATOM   3083 C  CD1 . TYR C 1 27  ? -4.275  14.841  4.068   1.00 11.61 ? 15  TYR C CD1 1 
ATOM   3084 C  CD2 . TYR C 1 27  ? -3.069  16.021  5.757   1.00 13.19 ? 15  TYR C CD2 1 
ATOM   3085 C  CE1 . TYR C 1 27  ? -3.262  13.902  3.995   1.00 12.67 ? 15  TYR C CE1 1 
ATOM   3086 C  CE2 . TYR C 1 27  ? -2.053  15.077  5.690   1.00 15.50 ? 15  TYR C CE2 1 
ATOM   3087 C  CZ  . TYR C 1 27  ? -2.162  14.017  4.807   1.00 16.91 ? 15  TYR C CZ  1 
ATOM   3088 O  OH  . TYR C 1 27  ? -1.162  13.069  4.715   1.00 18.47 ? 15  TYR C OH  1 
ATOM   3089 N  N   . SER C 1 28  ? -3.699  19.677  5.034   1.00 12.31 ? 16  SER C N   1 
ATOM   3090 C  CA  . SER C 1 28  ? -2.394  20.247  5.317   1.00 11.84 ? 16  SER C CA  1 
ATOM   3091 C  C   . SER C 1 28  ? -2.256  20.314  6.826   1.00 12.24 ? 16  SER C C   1 
ATOM   3092 O  O   . SER C 1 28  ? -3.172  20.773  7.517   1.00 11.84 ? 16  SER C O   1 
ATOM   3093 C  CB  . SER C 1 28  ? -2.223  21.635  4.693   1.00 11.58 ? 16  SER C CB  1 
ATOM   3094 O  OG  . SER C 1 28  ? -1.028  22.259  5.158   1.00 15.54 ? 16  SER C OG  1 
ATOM   3095 N  N   . PHE C 1 29  ? -1.134  19.818  7.330   1.00 13.47 ? 17  PHE C N   1 
ATOM   3096 C  CA  . PHE C 1 29  ? -0.746  19.977  8.722   1.00 11.94 ? 17  PHE C CA  1 
ATOM   3097 C  C   . PHE C 1 29  ? 0.612   20.657  8.724   1.00 13.22 ? 17  PHE C C   1 
ATOM   3098 O  O   . PHE C 1 29  ? 1.566   20.128  8.153   1.00 14.37 ? 17  PHE C O   1 
ATOM   3099 C  CB  . PHE C 1 29  ? -0.695  18.620  9.430   1.00 15.09 ? 17  PHE C CB  1 
ATOM   3100 C  CG  . PHE C 1 29  ? -0.132  18.675  10.823  1.00 14.21 ? 17  PHE C CG  1 
ATOM   3101 C  CD1 . PHE C 1 29  ? -0.751  19.423  11.803  1.00 16.10 ? 17  PHE C CD1 1 
ATOM   3102 C  CD2 . PHE C 1 29  ? 1.030   17.989  11.146  1.00 15.80 ? 17  PHE C CD2 1 
ATOM   3103 C  CE1 . PHE C 1 29  ? -0.235  19.481  13.083  1.00 15.36 ? 17  PHE C CE1 1 
ATOM   3104 C  CE2 . PHE C 1 29  ? 1.544   18.033  12.424  1.00 18.61 ? 17  PHE C CE2 1 
ATOM   3105 C  CZ  . PHE C 1 29  ? 0.917   18.786  13.393  1.00 17.21 ? 17  PHE C CZ  1 
ATOM   3106 N  N   . TRP C 1 30  ? 0.693   21.840  9.322   1.00 11.76 ? 18  TRP C N   1 
ATOM   3107 C  CA  . TRP C 1 30  ? 1.956   22.554  9.421   1.00 12.46 ? 18  TRP C CA  1 
ATOM   3108 C  C   . TRP C 1 30  ? 2.209   22.899  10.878  1.00 15.36 ? 18  TRP C C   1 
ATOM   3109 O  O   . TRP C 1 30  ? 1.323   23.425  11.560  1.00 12.53 ? 18  TRP C O   1 
ATOM   3110 C  CB  . TRP C 1 30  ? 1.951   23.820  8.555   1.00 16.97 ? 18  TRP C CB  1 
ATOM   3111 C  CG  . TRP C 1 30  ? 3.222   24.615  8.696   1.00 18.35 ? 18  TRP C CG  1 
ATOM   3112 C  CD1 . TRP C 1 30  ? 4.381   24.445  7.981   1.00 20.62 ? 18  TRP C CD1 1 
ATOM   3113 C  CD2 . TRP C 1 30  ? 3.473   25.690  9.616   1.00 19.51 ? 18  TRP C CD2 1 
ATOM   3114 N  NE1 . TRP C 1 30  ? 5.329   25.354  8.397   1.00 20.06 ? 18  TRP C NE1 1 
ATOM   3115 C  CE2 . TRP C 1 30  ? 4.802   26.124  9.401   1.00 21.43 ? 18  TRP C CE2 1 
ATOM   3116 C  CE3 . TRP C 1 30  ? 2.707   26.327  10.598  1.00 20.53 ? 18  TRP C CE3 1 
ATOM   3117 C  CZ2 . TRP C 1 30  ? 5.380   27.168  10.131  1.00 23.37 ? 18  TRP C CZ2 1 
ATOM   3118 C  CZ3 . TRP C 1 30  ? 3.285   27.369  11.324  1.00 25.66 ? 18  TRP C CZ3 1 
ATOM   3119 C  CH2 . TRP C 1 30  ? 4.609   27.773  11.085  1.00 25.21 ? 18  TRP C CH2 1 
ATOM   3120 N  N   . THR C 1 31  ? 3.406   22.576  11.361  1.00 14.46 ? 19  THR C N   1 
ATOM   3121 C  CA  . THR C 1 31  ? 3.804   22.969  12.706  1.00 15.27 ? 19  THR C CA  1 
ATOM   3122 C  C   . THR C 1 31  ? 5.241   23.464  12.669  1.00 18.92 ? 19  THR C C   1 
ATOM   3123 O  O   . THR C 1 31  ? 6.064   22.953  11.899  1.00 18.81 ? 19  THR C O   1 
ATOM   3124 C  CB  . THR C 1 31  ? 3.654   21.810  13.702  1.00 15.45 ? 19  THR C CB  1 
ATOM   3125 O  OG1 . THR C 1 31  ? 4.119   22.223  14.996  1.00 20.59 ? 19  THR C OG1 1 
ATOM   3126 C  CG2 . THR C 1 31  ? 4.453   20.596  13.250  1.00 19.48 ? 19  THR C CG2 1 
ATOM   3127 N  N   . ASP C 1 32  ? 5.538   24.484  13.477  1.00 18.73 ? 20  ASP C N   1 
ATOM   3128 C  CA  . ASP C 1 32  ? 6.932   24.903  13.581  1.00 22.08 ? 20  ASP C CA  1 
ATOM   3129 C  C   . ASP C 1 32  ? 7.750   23.973  14.471  1.00 22.55 ? 20  ASP C C   1 
ATOM   3130 O  O   . ASP C 1 32  ? 8.950   24.200  14.641  1.00 26.73 ? 20  ASP C O   1 
ATOM   3131 C  CB  . ASP C 1 32  ? 7.026   26.362  14.065  1.00 20.97 ? 20  ASP C CB  1 
ATOM   3132 C  CG  . ASP C 1 32  ? 6.534   26.563  15.499  1.00 21.06 ? 20  ASP C CG  1 
ATOM   3133 O  OD1 . ASP C 1 32  ? 6.273   25.579  16.210  1.00 23.17 ? 20  ASP C OD1 1 
ATOM   3134 O  OD2 . ASP C 1 32  ? 6.413   27.734  15.921  1.00 24.83 ? 20  ASP C OD2 1 
ATOM   3135 N  N   . GLY C 1 33  ? 7.132   22.939  15.038  1.00 19.63 ? 21  GLY C N   1 
ATOM   3136 C  CA  . GLY C 1 33  ? 7.827   21.926  15.797  1.00 24.76 ? 21  GLY C CA  1 
ATOM   3137 C  C   . GLY C 1 33  ? 7.781   22.091  17.303  1.00 24.20 ? 21  GLY C C   1 
ATOM   3138 O  O   . GLY C 1 33  ? 8.205   21.174  18.018  1.00 25.24 ? 21  GLY C O   1 
ATOM   3139 N  N   . GLY C 1 34  ? 7.269   23.213  17.807  1.00 20.79 ? 22  GLY C N   1 
ATOM   3140 C  CA  . GLY C 1 34  ? 7.255   23.438  19.244  1.00 20.66 ? 22  GLY C CA  1 
ATOM   3141 C  C   . GLY C 1 34  ? 6.195   22.614  19.954  1.00 24.79 ? 22  GLY C C   1 
ATOM   3142 O  O   . GLY C 1 34  ? 5.110   22.360  19.429  1.00 19.81 ? 22  GLY C O   1 
ATOM   3143 N  N   . GLY C 1 35  ? 6.529   22.184  21.172  1.00 22.27 ? 23  GLY C N   1 
ATOM   3144 C  CA  . GLY C 1 35  ? 5.605   21.424  22.005  1.00 18.29 ? 23  GLY C CA  1 
ATOM   3145 C  C   . GLY C 1 35  ? 5.188   20.111  21.370  1.00 22.24 ? 23  GLY C C   1 
ATOM   3146 O  O   . GLY C 1 35  ? 5.933   19.485  20.612  1.00 22.71 ? 23  GLY C O   1 
ATOM   3147 N  N   . GLN C 1 36  ? 3.968   19.688  21.684  1.00 20.60 ? 24  GLN C N   1 
ATOM   3148 C  CA  . GLN C 1 36  ? 3.372   18.486  21.114  1.00 22.48 ? 24  GLN C CA  1 
ATOM   3149 C  C   . GLN C 1 36  ? 2.111   18.887  20.364  1.00 18.05 ? 24  GLN C C   1 
ATOM   3150 O  O   . GLN C 1 36  ? 1.194   19.465  20.954  1.00 17.63 ? 24  GLN C O   1 
ATOM   3151 C  CB  . GLN C 1 36  ? 3.053   17.459  22.200  1.00 25.83 ? 24  GLN C CB  1 
ATOM   3152 C  CG  . GLN C 1 36  ? 2.528   16.127  21.675  1.00 35.50 ? 24  GLN C CG  1 
ATOM   3153 C  CD  . GLN C 1 36  ? 3.639   15.153  21.306  1.00 41.56 ? 24  GLN C CD  1 
ATOM   3154 O  OE1 . GLN C 1 36  ? 4.781   15.554  21.053  1.00 40.17 ? 24  GLN C OE1 1 
ATOM   3155 N  NE2 . GLN C 1 36  ? 3.308   13.863  21.273  1.00 43.65 ? 24  GLN C NE2 1 
ATOM   3156 N  N   . VAL C 1 37  ? 2.087   18.624  19.062  1.00 17.21 ? 25  VAL C N   1 
ATOM   3157 C  CA  . VAL C 1 37  ? 0.888   18.795  18.249  1.00 18.38 ? 25  VAL C CA  1 
ATOM   3158 C  C   . VAL C 1 37  ? 0.664   17.487  17.510  1.00 17.99 ? 25  VAL C C   1 
ATOM   3159 O  O   . VAL C 1 37  ? 1.554   17.029  16.785  1.00 20.91 ? 25  VAL C O   1 
ATOM   3160 C  CB  . VAL C 1 37  ? 1.011   19.964  17.258  1.00 14.85 ? 25  VAL C CB  1 
ATOM   3161 C  CG1 . VAL C 1 37  ? -0.340  20.215  16.560  1.00 14.48 ? 25  VAL C CG1 1 
ATOM   3162 C  CG2 . VAL C 1 37  ? 1.478   21.227  17.967  1.00 15.03 ? 25  VAL C CG2 1 
ATOM   3163 N  N   . THR C 1 38  ? -0.501  16.870  17.712  1.00 14.72 ? 26  THR C N   1 
ATOM   3164 C  CA  . THR C 1 38  ? -0.815  15.588  17.081  1.00 16.51 ? 26  THR C CA  1 
ATOM   3165 C  C   . THR C 1 38  ? -2.068  15.716  16.224  1.00 17.14 ? 26  THR C C   1 
ATOM   3166 O  O   . THR C 1 38  ? -3.152  16.012  16.738  1.00 14.16 ? 26  THR C O   1 
ATOM   3167 C  CB  . THR C 1 38  ? -1.004  14.484  18.118  1.00 21.10 ? 26  THR C CB  1 
ATOM   3168 O  OG1 . THR C 1 38  ? 0.156   14.418  18.961  1.00 22.38 ? 26  THR C OG1 1 
ATOM   3169 C  CG2 . THR C 1 38  ? -1.188  13.139  17.414  1.00 22.44 ? 26  THR C CG2 1 
ATOM   3170 N  N   . TYR C 1 39  ? -1.919  15.436  14.932  1.00 14.47 ? 27  TYR C N   1 
ATOM   3171 C  CA  . TYR C 1 39  ? -2.978  15.557  13.944  1.00 13.54 ? 27  TYR C CA  1 
ATOM   3172 C  C   . TYR C 1 39  ? -3.409  14.167  13.495  1.00 15.50 ? 27  TYR C C   1 
ATOM   3173 O  O   . TYR C 1 39  ? -2.567  13.282  13.308  1.00 16.17 ? 27  TYR C O   1 
ATOM   3174 C  CB  . TYR C 1 39  ? -2.471  16.380  12.752  1.00 13.48 ? 27  TYR C CB  1 
ATOM   3175 C  CG  . TYR C 1 39  ? -3.417  16.475  11.581  1.00 14.02 ? 27  TYR C CG  1 
ATOM   3176 C  CD1 . TYR C 1 39  ? -4.329  17.521  11.486  1.00 12.47 ? 27  TYR C CD1 1 
ATOM   3177 C  CD2 . TYR C 1 39  ? -3.384  15.534  10.560  1.00 14.72 ? 27  TYR C CD2 1 
ATOM   3178 C  CE1 . TYR C 1 39  ? -5.200  17.617  10.401  1.00 13.45 ? 27  TYR C CE1 1 
ATOM   3179 C  CE2 . TYR C 1 39  ? -4.247  15.614  9.483   1.00 14.74 ? 27  TYR C CE2 1 
ATOM   3180 C  CZ  . TYR C 1 39  ? -5.152  16.654  9.411   1.00 13.31 ? 27  TYR C CZ  1 
ATOM   3181 O  OH  . TYR C 1 39  ? -6.002  16.736  8.337   1.00 13.09 ? 27  TYR C OH  1 
ATOM   3182 N  N   . THR C 1 40  ? -4.716  13.980  13.310  1.00 11.92 ? 28  THR C N   1 
ATOM   3183 C  CA  . THR C 1 40  ? -5.266  12.698  12.881  1.00 13.96 ? 28  THR C CA  1 
ATOM   3184 C  C   . THR C 1 40  ? -6.298  12.903  11.783  1.00 12.91 ? 28  THR C C   1 
ATOM   3185 O  O   . THR C 1 40  ? -7.238  13.683  11.948  1.00 16.93 ? 28  THR C O   1 
ATOM   3186 C  CB  . THR C 1 40  ? -5.903  11.961  14.067  1.00 19.48 ? 28  THR C CB  1 
ATOM   3187 O  OG1 . THR C 1 40  ? -4.893  11.673  15.039  1.00 24.08 ? 28  THR C OG1 1 
ATOM   3188 C  CG2 . THR C 1 40  ? -6.530  10.661  13.617  1.00 21.01 ? 28  THR C CG2 1 
ATOM   3189 N  N   . ASN C 1 41  ? -6.125  12.203  10.663  1.00 12.14 ? 29  ASN C N   1 
ATOM   3190 C  CA  . ASN C 1 41  ? -7.148  12.193  9.625   1.00 13.10 ? 29  ASN C CA  1 
ATOM   3191 C  C   . ASN C 1 41  ? -8.208  11.159  9.968   1.00 15.65 ? 29  ASN C C   1 
ATOM   3192 O  O   . ASN C 1 41  ? -7.878  10.021  10.319  1.00 18.28 ? 29  ASN C O   1 
ATOM   3193 C  CB  . ASN C 1 41  ? -6.539  11.860  8.262   1.00 15.22 ? 29  ASN C CB  1 
ATOM   3194 C  CG  . ASN C 1 41  ? -5.920  13.061  7.582   1.00 12.99 ? 29  ASN C CG  1 
ATOM   3195 O  OD1 . ASN C 1 41  ? -6.471  14.163  7.610   1.00 15.59 ? 29  ASN C OD1 1 
ATOM   3196 N  ND2 . ASN C 1 41  ? -4.768  12.851  6.956   1.00 16.26 ? 29  ASN C ND2 1 
ATOM   3197 N  N   . GLY C 1 42  ? -9.475  11.547  9.855   1.00 13.52 ? 30  GLY C N   1 
ATOM   3198 C  CA  . GLY C 1 42  ? -10.567 10.615  10.030  1.00 14.68 ? 30  GLY C CA  1 
ATOM   3199 C  C   . GLY C 1 42  ? -11.295 10.345  8.728   1.00 17.97 ? 30  GLY C C   1 
ATOM   3200 O  O   . GLY C 1 42  ? -10.869 10.756  7.641   1.00 15.42 ? 30  GLY C O   1 
ATOM   3201 N  N   . PRO C 1 43  ? -12.424 9.656   8.818   1.00 16.22 ? 31  PRO C N   1 
ATOM   3202 C  CA  . PRO C 1 43  ? -13.187 9.345   7.606   1.00 14.67 ? 31  PRO C CA  1 
ATOM   3203 C  C   . PRO C 1 43  ? -13.731 10.605  6.955   1.00 18.24 ? 31  PRO C C   1 
ATOM   3204 O  O   . PRO C 1 43  ? -14.027 11.599  7.628   1.00 16.39 ? 31  PRO C O   1 
ATOM   3205 C  CB  . PRO C 1 43  ? -14.330 8.457   8.120   1.00 19.91 ? 31  PRO C CB  1 
ATOM   3206 C  CG  . PRO C 1 43  ? -13.919 8.005   9.468   1.00 21.02 ? 31  PRO C CG  1 
ATOM   3207 C  CD  . PRO C 1 43  ? -13.023 9.069   10.031  1.00 18.97 ? 31  PRO C CD  1 
ATOM   3208 N  N   . ALA C 1 44  ? -13.873 10.537  5.624   1.00 16.50 ? 32  ALA C N   1 
ATOM   3209 C  CA  . ALA C 1 44  ? -14.446 11.595  4.775   1.00 15.51 ? 32  ALA C CA  1 
ATOM   3210 C  C   . ALA C 1 44  ? -13.757 12.912  5.129   1.00 13.77 ? 32  ALA C C   1 
ATOM   3211 O  O   . ALA C 1 44  ? -12.517 12.961  5.143   1.00 13.85 ? 32  ALA C O   1 
ATOM   3212 C  CB  . ALA C 1 44  ? -15.963 11.602  4.905   1.00 16.12 ? 32  ALA C CB  1 
ATOM   3213 N  N   . GLY C 1 45  ? -14.499 13.972  5.439   1.00 14.71 ? 33  GLY C N   1 
ATOM   3214 C  CA  . GLY C 1 45  ? -13.890 15.272  5.662   1.00 12.38 ? 33  GLY C CA  1 
ATOM   3215 C  C   . GLY C 1 45  ? -13.481 15.562  7.092   1.00 13.72 ? 33  GLY C C   1 
ATOM   3216 O  O   . GLY C 1 45  ? -13.315 16.730  7.452   1.00 12.56 ? 33  GLY C O   1 
ATOM   3217 N  N   . GLN C 1 46  ? -13.296 14.531  7.917   1.00 13.09 ? 34  GLN C N   1 
ATOM   3218 C  CA  . GLN C 1 46  ? -13.016 14.724  9.335   1.00 12.19 ? 34  GLN C CA  1 
ATOM   3219 C  C   . GLN C 1 46  ? -11.518 14.766  9.620   1.00 11.15 ? 34  GLN C C   1 
ATOM   3220 O  O   . GLN C 1 46  ? -10.739 14.002  9.044   1.00 12.06 ? 34  GLN C O   1 
ATOM   3221 C  CB  . GLN C 1 46  ? -13.650 13.602  10.161  1.00 14.29 ? 34  GLN C CB  1 
ATOM   3222 C  CG  . GLN C 1 46  ? -13.779 13.935  11.646  1.00 15.37 ? 34  GLN C CG  1 
ATOM   3223 C  CD  . GLN C 1 46  ? -12.569 13.572  12.465  1.00 22.20 ? 34  GLN C CD  1 
ATOM   3224 O  OE1 . GLN C 1 46  ? -11.718 12.782  12.044  1.00 28.07 ? 34  GLN C OE1 1 
ATOM   3225 N  NE2 . GLN C 1 46  ? -12.484 14.142  13.665  1.00 24.56 ? 34  GLN C NE2 1 
ATOM   3226 N  N   . TYR C 1 47  ? -11.120 15.661  10.527  1.00 11.32 ? 35  TYR C N   1 
ATOM   3227 C  CA  . TYR C 1 47  ? -9.797  15.605  11.125  1.00 10.49 ? 35  TYR C CA  1 
ATOM   3228 C  C   . TYR C 1 47  ? -9.897  16.009  12.588  1.00 10.41 ? 35  TYR C C   1 
ATOM   3229 O  O   . TYR C 1 47  ? -10.851 16.673  13.011  1.00 11.70 ? 35  TYR C O   1 
ATOM   3230 C  CB  . TYR C 1 47  ? -8.788  16.513  10.397  1.00 10.29 ? 35  TYR C CB  1 
ATOM   3231 C  CG  . TYR C 1 47  ? -9.029  17.998  10.614  1.00 10.94 ? 35  TYR C CG  1 
ATOM   3232 C  CD1 . TYR C 1 47  ? -9.918  18.709  9.795   1.00 11.94 ? 35  TYR C CD1 1 
ATOM   3233 C  CD2 . TYR C 1 47  ? -8.367  18.690  11.637  1.00 9.69  ? 35  TYR C CD2 1 
ATOM   3234 C  CE1 . TYR C 1 47  ? -10.142 20.061  9.992   1.00 9.90  ? 35  TYR C CE1 1 
ATOM   3235 C  CE2 . TYR C 1 47  ? -8.591  20.042  11.840  1.00 12.17 ? 35  TYR C CE2 1 
ATOM   3236 C  CZ  . TYR C 1 47  ? -9.478  20.720  11.005  1.00 11.02 ? 35  TYR C CZ  1 
ATOM   3237 O  OH  . TYR C 1 47  ? -9.721  22.069  11.175  1.00 10.50 ? 35  TYR C OH  1 
ATOM   3238 N  N   . SER C 1 48  ? -8.890  15.605  13.351  1.00 10.60 ? 36  SER C N   1 
ATOM   3239 C  CA  . SER C 1 48  ? -8.752  15.986  14.752  1.00 12.37 ? 36  SER C CA  1 
ATOM   3240 C  C   . SER C 1 48  ? -7.342  16.496  14.991  1.00 13.24 ? 36  SER C C   1 
ATOM   3241 O  O   . SER C 1 48  ? -6.391  16.048  14.351  1.00 13.45 ? 36  SER C O   1 
ATOM   3242 C  CB  . SER C 1 48  ? -9.015  14.805  15.708  1.00 16.53 ? 36  SER C CB  1 
ATOM   3243 O  OG  . SER C 1 48  ? -10.325 14.284  15.554  1.00 24.24 ? 36  SER C OG  1 
ATOM   3244 N  N   . VAL C 1 49  ? -7.201  17.423  15.933  1.00 13.29 ? 37  VAL C N   1 
ATOM   3245 C  CA  . VAL C 1 49  ? -5.880  17.866  16.352  1.00 14.69 ? 37  VAL C CA  1 
ATOM   3246 C  C   . VAL C 1 49  ? -5.899  18.066  17.858  1.00 16.89 ? 37  VAL C C   1 
ATOM   3247 O  O   . VAL C 1 49  ? -6.883  18.543  18.432  1.00 14.40 ? 37  VAL C O   1 
ATOM   3248 C  CB  . VAL C 1 49  ? -5.420  19.139  15.596  1.00 17.01 ? 37  VAL C CB  1 
ATOM   3249 C  CG1 . VAL C 1 49  ? -6.391  20.275  15.767  1.00 16.61 ? 37  VAL C CG1 1 
ATOM   3250 C  CG2 . VAL C 1 49  ? -4.009  19.557  16.041  1.00 17.13 ? 37  VAL C CG2 1 
ATOM   3251 N  N   . GLU C 1 50  ? -4.828  17.642  18.506  1.00 12.47 ? 38  GLU C N   1 
ATOM   3252 C  CA  . GLU C 1 50  ? -4.694  17.789  19.944  1.00 16.36 ? 38  GLU C CA  1 
ATOM   3253 C  C   . GLU C 1 50  ? -3.317  18.364  20.199  1.00 17.22 ? 38  GLU C C   1 
ATOM   3254 O  O   . GLU C 1 50  ? -2.340  17.917  19.586  1.00 16.62 ? 38  GLU C O   1 
ATOM   3255 C  CB  . GLU C 1 50  ? -4.879  16.449  20.636  1.00 21.76 ? 38  GLU C CB  1 
ATOM   3256 C  CG  . GLU C 1 50  ? -4.567  16.465  22.097  1.00 33.02 ? 38  GLU C CG  1 
ATOM   3257 C  CD  . GLU C 1 50  ? -4.214  15.093  22.590  1.00 39.28 ? 38  GLU C CD  1 
ATOM   3258 O  OE1 . GLU C 1 50  ? -5.064  14.190  22.435  1.00 48.20 ? 38  GLU C OE1 1 
ATOM   3259 O  OE2 . GLU C 1 50  ? -3.092  14.907  23.112  1.00 48.33 ? 38  GLU C OE2 1 
ATOM   3260 N  N   . TRP C 1 51  ? -3.231  19.379  21.059  1.00 15.85 ? 39  TRP C N   1 
ATOM   3261 C  CA  . TRP C 1 51  ? -1.949  20.049  21.193  1.00 14.40 ? 39  TRP C CA  1 
ATOM   3262 C  C   . TRP C 1 51  ? -1.710  20.490  22.629  1.00 13.72 ? 39  TRP C C   1 
ATOM   3263 O  O   . TRP C 1 51  ? -2.645  20.716  23.397  1.00 13.54 ? 39  TRP C O   1 
ATOM   3264 C  CB  . TRP C 1 51  ? -1.845  21.223  20.210  1.00 14.48 ? 39  TRP C CB  1 
ATOM   3265 C  CG  . TRP C 1 51  ? -2.698  22.418  20.471  1.00 12.79 ? 39  TRP C CG  1 
ATOM   3266 C  CD1 . TRP C 1 51  ? -2.308  23.588  21.071  1.00 13.85 ? 39  TRP C CD1 1 
ATOM   3267 C  CD2 . TRP C 1 51  ? -4.066  22.611  20.073  1.00 13.74 ? 39  TRP C CD2 1 
ATOM   3268 N  NE1 . TRP C 1 51  ? -3.355  24.483  21.087  1.00 12.81 ? 39  TRP C NE1 1 
ATOM   3269 C  CE2 . TRP C 1 51  ? -4.446  23.907  20.493  1.00 13.23 ? 39  TRP C CE2 1 
ATOM   3270 C  CE3 . TRP C 1 51  ? -5.008  21.809  19.427  1.00 13.13 ? 39  TRP C CE3 1 
ATOM   3271 C  CZ2 . TRP C 1 51  ? -5.724  24.424  20.271  1.00 13.14 ? 39  TRP C CZ2 1 
ATOM   3272 C  CZ3 . TRP C 1 51  ? -6.283  22.321  19.203  1.00 11.95 ? 39  TRP C CZ3 1 
ATOM   3273 C  CH2 . TRP C 1 51  ? -6.631  23.614  19.628  1.00 13.61 ? 39  TRP C CH2 1 
ATOM   3274 N  N   . SER C 1 52  ? -0.430  20.589  22.971  1.00 14.48 ? 40  SER C N   1 
ATOM   3275 C  CA  . SER C 1 52  ? 0.015   20.873  24.329  1.00 15.24 ? 40  SER C CA  1 
ATOM   3276 C  C   . SER C 1 52  ? 1.260   21.742  24.253  1.00 15.31 ? 40  SER C C   1 
ATOM   3277 O  O   . SER C 1 52  ? 2.265   21.332  23.661  1.00 16.47 ? 40  SER C O   1 
ATOM   3278 C  CB  . SER C 1 52  ? 0.314   19.567  25.080  1.00 17.73 ? 40  SER C CB  1 
ATOM   3279 O  OG  . SER C 1 52  ? 0.353   19.788  26.475  1.00 31.67 ? 40  SER C OG  1 
ATOM   3280 N  N   . ASN C 1 53  ? 1.193   22.937  24.841  1.00 13.27 ? 41  ASN C N   1 
ATOM   3281 C  CA  . ASN C 1 53  ? 2.329   23.863  24.893  1.00 16.37 ? 41  ASN C CA  1 
ATOM   3282 C  C   . ASN C 1 53  ? 2.958   24.050  23.514  1.00 19.23 ? 41  ASN C C   1 
ATOM   3283 O  O   . ASN C 1 53  ? 4.174   23.975  23.333  1.00 17.52 ? 41  ASN C O   1 
ATOM   3284 C  CB  . ASN C 1 53  ? 3.360   23.382  25.909  1.00 20.46 ? 41  ASN C CB  1 
ATOM   3285 C  CG  . ASN C 1 53  ? 2.822   23.413  27.308  1.00 19.38 ? 41  ASN C CG  1 
ATOM   3286 O  OD1 . ASN C 1 53  ? 2.284   24.430  27.748  1.00 17.39 ? 41  ASN C OD1 1 
ATOM   3287 N  ND2 . ASN C 1 53  ? 2.919   22.290  28.008  1.00 21.82 ? 41  ASN C ND2 1 
ATOM   3288 N  N   . SER C 1 54  ? 2.102   24.295  22.532  1.00 14.48 ? 42  SER C N   1 
ATOM   3289 C  CA  . SER C 1 54  ? 2.519   24.243  21.143  1.00 15.50 ? 42  SER C CA  1 
ATOM   3290 C  C   . SER C 1 54  ? 3.344   25.464  20.767  1.00 16.59 ? 42  SER C C   1 
ATOM   3291 O  O   . SER C 1 54  ? 3.335   26.493  21.444  1.00 16.86 ? 42  SER C O   1 
ATOM   3292 C  CB  . SER C 1 54  ? 1.296   24.172  20.228  1.00 15.24 ? 42  SER C CB  1 
ATOM   3293 O  OG  . SER C 1 54  ? 0.567   25.398  20.284  1.00 15.50 ? 42  SER C OG  1 
ATOM   3294 N  N   . GLY C 1 55  ? 4.062   25.339  19.657  1.00 17.00 ? 43  GLY C N   1 
ATOM   3295 C  CA  . GLY C 1 55  ? 4.500   26.509  18.936  1.00 18.79 ? 43  GLY C CA  1 
ATOM   3296 C  C   . GLY C 1 55  ? 3.375   26.945  18.017  1.00 19.55 ? 43  GLY C C   1 
ATOM   3297 O  O   . GLY C 1 55  ? 2.196   26.826  18.376  1.00 19.32 ? 43  GLY C O   1 
ATOM   3298 N  N   . ASN C 1 56  ? 3.721   27.439  16.831  1.00 16.19 ? 44  ASN C N   1 
ATOM   3299 C  CA  . ASN C 1 56  ? 2.734   27.771  15.813  1.00 16.93 ? 44  ASN C CA  1 
ATOM   3300 C  C   . ASN C 1 56  ? 2.344   26.505  15.062  1.00 15.43 ? 44  ASN C C   1 
ATOM   3301 O  O   . ASN C 1 56  ? 3.205   25.697  14.698  1.00 14.68 ? 44  ASN C O   1 
ATOM   3302 C  CB  . ASN C 1 56  ? 3.295   28.778  14.802  1.00 21.60 ? 44  ASN C CB  1 
ATOM   3303 C  CG  . ASN C 1 56  ? 3.325   30.201  15.320  1.00 28.87 ? 44  ASN C CG  1 
ATOM   3304 O  OD1 . ASN C 1 56  ? 2.283   30.824  15.526  1.00 33.06 ? 44  ASN C OD1 1 
ATOM   3305 N  ND2 . ASN C 1 56  ? 4.529   30.735  15.510  1.00 30.69 ? 44  ASN C ND2 1 
ATOM   3306 N  N   . PHE C 1 57  ? 1.047   26.337  14.824  1.00 15.39 ? 45  PHE C N   1 
ATOM   3307 C  CA  . PHE C 1 57  ? 0.591   25.295  13.916  1.00 13.84 ? 45  PHE C CA  1 
ATOM   3308 C  C   . PHE C 1 57  ? -0.708  25.730  13.257  1.00 14.03 ? 45  PHE C C   1 
ATOM   3309 O  O   . PHE C 1 57  ? -1.474  26.530  13.810  1.00 10.13 ? 45  PHE C O   1 
ATOM   3310 C  CB  . PHE C 1 57  ? 0.395   23.957  14.628  1.00 14.51 ? 45  PHE C CB  1 
ATOM   3311 C  CG  . PHE C 1 57  ? -0.850  23.895  15.471  1.00 15.78 ? 45  PHE C CG  1 
ATOM   3312 C  CD1 . PHE C 1 57  ? -2.061  23.464  14.932  1.00 13.49 ? 45  PHE C CD1 1 
ATOM   3313 C  CD2 . PHE C 1 57  ? -0.806  24.281  16.806  1.00 12.72 ? 45  PHE C CD2 1 
ATOM   3314 C  CE1 . PHE C 1 57  ? -3.206  23.416  15.702  1.00 13.78 ? 45  PHE C CE1 1 
ATOM   3315 C  CE2 . PHE C 1 57  ? -1.941  24.229  17.588  1.00 16.38 ? 45  PHE C CE2 1 
ATOM   3316 C  CZ  . PHE C 1 57  ? -3.146  23.801  17.039  1.00 14.13 ? 45  PHE C CZ  1 
ATOM   3317 N  N   . VAL C 1 58  ? -0.944  25.182  12.063  1.00 12.09 ? 46  VAL C N   1 
ATOM   3318 C  CA  . VAL C 1 58  ? -2.195  25.343  11.324  1.00 12.20 ? 46  VAL C CA  1 
ATOM   3319 C  C   . VAL C 1 58  ? -2.485  24.011  10.650  1.00 15.28 ? 46  VAL C C   1 
ATOM   3320 O  O   . VAL C 1 58  ? -1.595  23.438  10.014  1.00 14.72 ? 46  VAL C O   1 
ATOM   3321 C  CB  . VAL C 1 58  ? -2.127  26.460  10.261  1.00 13.91 ? 46  VAL C CB  1 
ATOM   3322 C  CG1 . VAL C 1 58  ? -3.536  26.734  9.689   1.00 13.33 ? 46  VAL C CG1 1 
ATOM   3323 C  CG2 . VAL C 1 58  ? -1.516  27.739  10.819  1.00 20.67 ? 46  VAL C CG2 1 
ATOM   3324 N  N   . ALA C 1 59  ? -3.725  23.526  10.761  1.00 12.32 ? 47  ALA C N   1 
ATOM   3325 C  CA  . ALA C 1 59  ? -4.031  22.192  10.252  1.00 13.13 ? 47  ALA C CA  1 
ATOM   3326 C  C   . ALA C 1 59  ? -5.487  22.087  9.828   1.00 10.46 ? 47  ALA C C   1 
ATOM   3327 O  O   . ALA C 1 59  ? -6.374  22.617  10.502  1.00 9.42  ? 47  ALA C O   1 
ATOM   3328 C  CB  . ALA C 1 59  ? -3.742  21.134  11.316  1.00 15.48 ? 47  ALA C CB  1 
ATOM   3329 N  N   . GLY C 1 60  ? -5.744  21.388  8.726   1.00 9.43  ? 48  GLY C N   1 
ATOM   3330 C  CA  . GLY C 1 60  ? -7.136  21.146  8.396   1.00 8.41  ? 48  GLY C CA  1 
ATOM   3331 C  C   . GLY C 1 60  ? -7.310  20.450  7.063   1.00 10.52 ? 48  GLY C C   1 
ATOM   3332 O  O   . GLY C 1 60  ? -6.343  20.076  6.387   1.00 11.57 ? 48  GLY C O   1 
ATOM   3333 N  N   . LYS C 1 61  ? -8.584  20.259  6.712   1.00 10.11 ? 49  LYS C N   1 
ATOM   3334 C  CA  . LYS C 1 61  ? -8.980  19.579  5.487   1.00 10.21 ? 49  LYS C CA  1 
ATOM   3335 C  C   . LYS C 1 61  ? -9.755  20.512  4.571   1.00 9.67  ? 49  LYS C C   1 
ATOM   3336 O  O   . LYS C 1 61  ? -10.463 21.420  5.017   1.00 10.69 ? 49  LYS C O   1 
ATOM   3337 C  CB  . LYS C 1 61  ? -9.871  18.356  5.764   1.00 11.43 ? 49  LYS C CB  1 
ATOM   3338 C  CG  . LYS C 1 61  ? -9.108  17.039  5.877   1.00 9.92  ? 49  LYS C CG  1 
ATOM   3339 C  CD  . LYS C 1 61  ? -10.063 15.863  6.095   1.00 10.75 ? 49  LYS C CD  1 
ATOM   3340 C  CE  . LYS C 1 61  ? -9.317  14.547  5.926   1.00 9.92  ? 49  LYS C CE  1 
ATOM   3341 N  NZ  . LYS C 1 61  ? -10.117 13.383  6.412   1.00 12.03 ? 49  LYS C NZ  1 
ATOM   3342 N  N   . GLY C 1 62  ? -9.670  20.234  3.281   1.00 8.50  ? 50  GLY C N   1 
ATOM   3343 C  CA  . GLY C 1 62  ? -10.409 21.031  2.337   1.00 10.55 ? 50  GLY C CA  1 
ATOM   3344 C  C   . GLY C 1 62  ? -10.191 20.606  0.904   1.00 11.80 ? 50  GLY C C   1 
ATOM   3345 O  O   . GLY C 1 62  ? -10.346 19.431  0.555   1.00 10.12 ? 50  GLY C O   1 
ATOM   3346 N  N   . TRP C 1 63  ? -9.819  21.570  0.072   1.00 9.76  ? 51  TRP C N   1 
ATOM   3347 C  CA  . TRP C 1 63  ? -9.852  21.415  -1.374  1.00 11.06 ? 51  TRP C CA  1 
ATOM   3348 C  C   . TRP C 1 63  ? -8.585  21.988  -1.979  1.00 8.92  ? 51  TRP C C   1 
ATOM   3349 O  O   . TRP C 1 63  ? -8.014  22.951  -1.470  1.00 10.15 ? 51  TRP C O   1 
ATOM   3350 C  CB  . TRP C 1 63  ? -11.072 22.123  -1.976  1.00 13.21 ? 51  TRP C CB  1 
ATOM   3351 C  CG  . TRP C 1 63  ? -12.305 21.704  -1.302  1.00 14.50 ? 51  TRP C CG  1 
ATOM   3352 C  CD1 . TRP C 1 63  ? -13.156 20.709  -1.688  1.00 19.47 ? 51  TRP C CD1 1 
ATOM   3353 C  CD2 . TRP C 1 63  ? -12.817 22.222  -0.071  1.00 16.80 ? 51  TRP C CD2 1 
ATOM   3354 N  NE1 . TRP C 1 63  ? -14.183 20.592  -0.774  1.00 20.59 ? 51  TRP C NE1 1 
ATOM   3355 C  CE2 . TRP C 1 63  ? -13.987 21.505  0.229   1.00 21.19 ? 51  TRP C CE2 1 
ATOM   3356 C  CE3 . TRP C 1 63  ? -12.398 23.227  0.801   1.00 14.67 ? 51  TRP C CE3 1 
ATOM   3357 C  CZ2 . TRP C 1 63  ? -14.745 21.769  1.359   1.00 23.89 ? 51  TRP C CZ2 1 
ATOM   3358 C  CZ3 . TRP C 1 63  ? -13.136 23.474  1.928   1.00 17.23 ? 51  TRP C CZ3 1 
ATOM   3359 C  CH2 . TRP C 1 63  ? -14.299 22.751  2.197   1.00 20.70 ? 51  TRP C CH2 1 
ATOM   3360 N  N   . ASN C 1 64  ? -8.187  21.426  -3.104  1.00 10.39 ? 52  ASN C N   1 
ATOM   3361 C  CA  . ASN C 1 64  ? -7.104  22.014  -3.876  1.00 11.84 ? 52  ASN C CA  1 
ATOM   3362 C  C   . ASN C 1 64  ? -7.381  21.724  -5.344  1.00 13.34 ? 52  ASN C C   1 
ATOM   3363 O  O   . ASN C 1 64  ? -7.543  20.559  -5.727  1.00 12.74 ? 52  ASN C O   1 
ATOM   3364 C  CB  . ASN C 1 64  ? -5.749  21.462  -3.437  1.00 11.75 ? 52  ASN C CB  1 
ATOM   3365 C  CG  . ASN C 1 64  ? -4.577  22.316  -3.917  1.00 14.52 ? 52  ASN C CG  1 
ATOM   3366 O  OD1 . ASN C 1 64  ? -4.760  23.428  -4.408  1.00 13.33 ? 52  ASN C OD1 1 
ATOM   3367 N  ND2 . ASN C 1 64  ? -3.366  21.792  -3.770  1.00 16.22 ? 52  ASN C ND2 1 
ATOM   3368 N  N   . PRO C 1 65  ? -7.529  22.752  -6.183  1.00 12.20 ? 53  PRO C N   1 
ATOM   3369 C  CA  . PRO C 1 65  ? -7.525  24.160  -5.785  1.00 14.20 ? 53  PRO C CA  1 
ATOM   3370 C  C   . PRO C 1 65  ? -8.829  24.555  -5.112  1.00 12.66 ? 53  PRO C C   1 
ATOM   3371 O  O   . PRO C 1 65  ? -9.865  23.931  -5.329  1.00 15.77 ? 53  PRO C O   1 
ATOM   3372 C  CB  . PRO C 1 65  ? -7.370  24.895  -7.120  1.00 16.90 ? 53  PRO C CB  1 
ATOM   3373 C  CG  . PRO C 1 65  ? -8.107  23.991  -8.089  1.00 16.89 ? 53  PRO C CG  1 
ATOM   3374 C  CD  . PRO C 1 65  ? -7.760  22.585  -7.631  1.00 15.24 ? 53  PRO C CD  1 
ATOM   3375 N  N   . GLY C 1 66  ? -8.771  25.577  -4.271  1.00 14.06 ? 54  GLY C N   1 
ATOM   3376 C  CA  . GLY C 1 66  ? -9.993  26.227  -3.863  1.00 12.98 ? 54  GLY C CA  1 
ATOM   3377 C  C   . GLY C 1 66  ? -10.655 26.879  -5.060  1.00 18.14 ? 54  GLY C C   1 
ATOM   3378 O  O   . GLY C 1 66  ? -9.993  27.343  -5.988  1.00 20.79 ? 54  GLY C O   1 
ATOM   3379 N  N   . SER C 1 67  ? -11.974 26.864  -5.070  1.00 20.53 ? 55  SER C N   1 
ATOM   3380 C  CA  . SER C 1 67  ? -12.704 27.465  -6.181  1.00 18.78 ? 55  SER C CA  1 
ATOM   3381 C  C   . SER C 1 67  ? -13.785 28.385  -5.656  1.00 23.60 ? 55  SER C C   1 
ATOM   3382 O  O   . SER C 1 67  ? -14.877 28.493  -6.227  1.00 29.26 ? 55  SER C O   1 
ATOM   3383 C  CB  . SER C 1 67  ? -13.277 26.394  -7.108  1.00 24.47 ? 55  SER C CB  1 
ATOM   3384 O  OG  . SER C 1 67  ? -14.045 25.448  -6.387  1.00 27.35 ? 55  SER C OG  1 
ATOM   3385 N  N   . SER C 1 68  ? -13.492 29.068  -4.551  1.00 19.28 ? 56  SER C N   1 
ATOM   3386 C  CA  . SER C 1 68  ? -14.415 30.036  -3.959  1.00 19.07 ? 56  SER C CA  1 
ATOM   3387 C  C   . SER C 1 68  ? -15.768 29.400  -3.664  1.00 20.66 ? 56  SER C C   1 
ATOM   3388 O  O   . SER C 1 68  ? -16.821 30.029  -3.792  1.00 21.85 ? 56  SER C O   1 
ATOM   3389 C  CB  . SER C 1 68  ? -14.576 31.257  -4.863  1.00 24.16 ? 56  SER C CB  1 
ATOM   3390 O  OG  . SER C 1 68  ? -13.312 31.756  -5.264  1.00 23.05 ? 56  SER C OG  1 
ATOM   3391 N  N   . GLN C 1 69  ? -15.744 28.133  -3.265  1.00 23.91 ? 57  GLN C N   1 
ATOM   3392 C  CA  . GLN C 1 69  ? -17.008 27.452  -3.071  1.00 26.78 ? 57  GLN C CA  1 
ATOM   3393 C  C   . GLN C 1 69  ? -17.612 27.813  -1.717  1.00 21.10 ? 57  GLN C C   1 
ATOM   3394 O  O   . GLN C 1 69  ? -16.963 28.379  -0.831  1.00 16.63 ? 57  GLN C O   1 
ATOM   3395 C  CB  . GLN C 1 69  ? -16.842 25.936  -3.196  1.00 27.67 ? 57  GLN C CB  1 
ATOM   3396 C  CG  . GLN C 1 69  ? -15.797 25.347  -2.286  1.00 24.96 ? 57  GLN C CG  1 
ATOM   3397 C  CD  . GLN C 1 69  ? -14.503 25.026  -3.010  1.00 29.86 ? 57  GLN C CD  1 
ATOM   3398 O  OE1 . GLN C 1 69  ? -13.662 25.904  -3.212  1.00 30.20 ? 57  GLN C OE1 1 
ATOM   3399 N  NE2 . GLN C 1 69  ? -14.339 23.766  -3.412  1.00 29.68 ? 57  GLN C NE2 1 
ATOM   3400 N  N   . THR C 1 70  ? -18.891 27.490  -1.588  1.00 20.28 ? 58  THR C N   1 
ATOM   3401 C  CA  . THR C 1 70  ? -19.655 27.688  -0.366  1.00 18.93 ? 58  THR C CA  1 
ATOM   3402 C  C   . THR C 1 70  ? -19.443 26.464  0.517   1.00 21.03 ? 58  THR C C   1 
ATOM   3403 O  O   . THR C 1 70  ? -19.887 25.363  0.176   1.00 24.02 ? 58  THR C O   1 
ATOM   3404 C  CB  . THR C 1 70  ? -21.124 27.898  -0.722  1.00 20.85 ? 58  THR C CB  1 
ATOM   3405 O  OG1 . THR C 1 70  ? -21.235 29.079  -1.527  1.00 20.83 ? 58  THR C OG1 1 
ATOM   3406 C  CG2 . THR C 1 70  ? -21.975 28.055  0.511   1.00 21.99 ? 58  THR C CG2 1 
ATOM   3407 N  N   . ILE C 1 71  ? -18.764 26.669  1.649   1.00 16.21 ? 59  ILE C N   1 
ATOM   3408 C  CA  . ILE C 1 71  ? -18.278 25.629  2.554   1.00 19.89 ? 59  ILE C CA  1 
ATOM   3409 C  C   . ILE C 1 71  ? -19.321 25.359  3.626   1.00 17.84 ? 59  ILE C C   1 
ATOM   3410 O  O   . ILE C 1 71  ? -19.948 26.292  4.132   1.00 18.74 ? 59  ILE C O   1 
ATOM   3411 C  CB  . ILE C 1 71  ? -16.945 26.079  3.203   1.00 17.60 ? 59  ILE C CB  1 
ATOM   3412 C  CG1 . ILE C 1 71  ? -15.834 26.120  2.167   1.00 26.76 ? 59  ILE C CG1 1 
ATOM   3413 C  CG2 . ILE C 1 71  ? -16.565 25.211  4.400   1.00 20.50 ? 59  ILE C CG2 1 
ATOM   3414 C  CD1 . ILE C 1 71  ? -16.033 25.124  1.067   1.00 23.28 ? 59  ILE C CD1 1 
ATOM   3415 N  N   . THR C 1 72  ? -19.482 24.091  4.015   1.00 13.72 ? 60  THR C N   1 
ATOM   3416 C  CA  . THR C 1 72  ? -20.188 23.772  5.249   1.00 14.38 ? 60  THR C CA  1 
ATOM   3417 C  C   . THR C 1 72  ? -19.295 22.892  6.114   1.00 15.26 ? 60  THR C C   1 
ATOM   3418 O  O   . THR C 1 72  ? -18.627 21.987  5.607   1.00 17.52 ? 60  THR C O   1 
ATOM   3419 C  CB  . THR C 1 72  ? -21.526 23.094  4.961   1.00 19.96 ? 60  THR C CB  1 
ATOM   3420 O  OG1 . THR C 1 72  ? -22.294 23.965  4.127   1.00 23.09 ? 60  THR C OG1 1 
ATOM   3421 C  CG2 . THR C 1 72  ? -22.298 22.837  6.256   1.00 21.26 ? 60  THR C CG2 1 
ATOM   3422 N  N   . TYR C 1 73  ? -19.239 23.189  7.411   1.00 14.97 ? 61  TYR C N   1 
ATOM   3423 C  CA  . TYR C 1 73  ? -18.422 22.401  8.328   1.00 16.16 ? 61  TYR C CA  1 
ATOM   3424 C  C   . TYR C 1 73  ? -19.121 22.322  9.681   1.00 16.29 ? 61  TYR C C   1 
ATOM   3425 O  O   . TYR C 1 73  ? -19.999 23.121  9.996   1.00 15.62 ? 61  TYR C O   1 
ATOM   3426 C  CB  . TYR C 1 73  ? -17.002 22.987  8.490   1.00 14.86 ? 61  TYR C CB  1 
ATOM   3427 C  CG  . TYR C 1 73  ? -16.999 24.257  9.300   1.00 17.92 ? 61  TYR C CG  1 
ATOM   3428 C  CD1 . TYR C 1 73  ? -17.499 25.441  8.761   1.00 17.70 ? 61  TYR C CD1 1 
ATOM   3429 C  CD2 . TYR C 1 73  ? -16.550 24.269  10.620  1.00 17.91 ? 61  TYR C CD2 1 
ATOM   3430 C  CE1 . TYR C 1 73  ? -17.548 26.595  9.500   1.00 18.72 ? 61  TYR C CE1 1 
ATOM   3431 C  CE2 . TYR C 1 73  ? -16.585 25.432  11.366  1.00 15.72 ? 61  TYR C CE2 1 
ATOM   3432 C  CZ  . TYR C 1 73  ? -17.086 26.586  10.804  1.00 23.91 ? 61  TYR C CZ  1 
ATOM   3433 O  OH  . TYR C 1 73  ? -17.135 27.748  11.539  1.00 29.09 ? 61  TYR C OH  1 
ATOM   3434 N  N   . SER C 1 74  ? -18.717 21.342  10.482  1.00 13.53 ? 62  SER C N   1 
ATOM   3435 C  CA  . SER C 1 74  ? -19.248 21.152  11.824  1.00 15.68 ? 62  SER C CA  1 
ATOM   3436 C  C   . SER C 1 74  ? -18.126 20.608  12.694  1.00 15.81 ? 62  SER C C   1 
ATOM   3437 O  O   . SER C 1 74  ? -17.120 20.104  12.194  1.00 17.81 ? 62  SER C O   1 
ATOM   3438 C  CB  . SER C 1 74  ? -20.451 20.184  11.828  1.00 17.43 ? 62  SER C CB  1 
ATOM   3439 O  OG  . SER C 1 74  ? -20.020 18.882  11.494  1.00 24.46 ? 62  SER C OG  1 
ATOM   3440 N  N   . GLY C 1 75  ? -18.309 20.691  14.002  1.00 18.07 ? 63  GLY C N   1 
ATOM   3441 C  CA  . GLY C 1 75  ? -17.399 20.010  14.899  1.00 19.67 ? 63  GLY C CA  1 
ATOM   3442 C  C   . GLY C 1 75  ? -17.318 20.690  16.254  1.00 15.95 ? 63  GLY C C   1 
ATOM   3443 O  O   . GLY C 1 75  ? -18.221 21.425  16.649  1.00 18.07 ? 63  GLY C O   1 
ATOM   3444 N  N   . GLU C 1 76  ? -16.200 20.405  16.931  1.00 13.33 ? 64  GLU C N   1 
ATOM   3445 C  CA  . GLU C 1 76  ? -15.913 20.844  18.287  1.00 17.08 ? 64  GLU C CA  1 
ATOM   3446 C  C   . GLU C 1 76  ? -14.556 21.527  18.306  1.00 16.99 ? 64  GLU C C   1 
ATOM   3447 O  O   . GLU C 1 76  ? -13.599 21.047  17.692  1.00 16.75 ? 64  GLU C O   1 
ATOM   3448 C  CB  . GLU C 1 76  ? -15.861 19.670  19.278  1.00 20.34 ? 64  GLU C CB  1 
ATOM   3449 C  CG  . GLU C 1 76  ? -17.111 18.845  19.395  1.00 31.02 ? 64  GLU C CG  1 
ATOM   3450 C  CD  . GLU C 1 76  ? -16.959 17.780  20.465  1.00 45.29 ? 64  GLU C CD  1 
ATOM   3451 O  OE1 . GLU C 1 76  ? -16.370 18.074  21.532  1.00 46.63 ? 64  GLU C OE1 1 
ATOM   3452 O  OE2 . GLU C 1 76  ? -17.417 16.645  20.234  1.00 52.13 ? 64  GLU C OE2 1 
ATOM   3453 N  N   . TRP C 1 77  ? -14.453 22.614  19.058  1.00 17.56 ? 65  TRP C N   1 
ATOM   3454 C  CA  . TRP C 1 77  ? -13.207 23.370  19.124  1.00 13.59 ? 65  TRP C CA  1 
ATOM   3455 C  C   . TRP C 1 77  ? -13.042 23.818  20.571  1.00 16.76 ? 65  TRP C C   1 
ATOM   3456 O  O   . TRP C 1 77  ? -13.835 24.626  21.063  1.00 17.59 ? 65  TRP C O   1 
ATOM   3457 C  CB  . TRP C 1 77  ? -13.247 24.545  18.143  1.00 16.93 ? 65  TRP C CB  1 
ATOM   3458 C  CG  . TRP C 1 77  ? -12.132 25.542  18.263  1.00 16.44 ? 65  TRP C CG  1 
ATOM   3459 C  CD1 . TRP C 1 77  ? -10.842 25.394  17.845  1.00 15.61 ? 65  TRP C CD1 1 
ATOM   3460 C  CD2 . TRP C 1 77  ? -12.237 26.865  18.797  1.00 15.18 ? 65  TRP C CD2 1 
ATOM   3461 N  NE1 . TRP C 1 77  ? -10.131 26.548  18.101  1.00 15.76 ? 65  TRP C NE1 1 
ATOM   3462 C  CE2 . TRP C 1 77  ? -10.966 27.462  18.691  1.00 16.66 ? 65  TRP C CE2 1 
ATOM   3463 C  CE3 . TRP C 1 77  ? -13.284 27.598  19.363  1.00 14.86 ? 65  TRP C CE3 1 
ATOM   3464 C  CZ2 . TRP C 1 77  ? -10.712 28.759  19.138  1.00 15.14 ? 65  TRP C CZ2 1 
ATOM   3465 C  CZ3 . TRP C 1 77  ? -13.034 28.876  19.807  1.00 17.46 ? 65  TRP C CZ3 1 
ATOM   3466 C  CH2 . TRP C 1 77  ? -11.755 29.448  19.693  1.00 14.50 ? 65  TRP C CH2 1 
ATOM   3467 N  N   . ASN C 1 78  ? -12.041 23.253  21.260  1.00 14.27 ? 66  ASN C N   1 
ATOM   3468 C  CA  . ASN C 1 78  ? -11.869 23.395  22.710  1.00 17.04 ? 66  ASN C CA  1 
ATOM   3469 C  C   . ASN C 1 78  ? -10.451 23.848  23.027  1.00 12.86 ? 66  ASN C C   1 
ATOM   3470 O  O   . ASN C 1 78  ? -9.612  23.052  23.477  1.00 14.68 ? 66  ASN C O   1 
ATOM   3471 C  CB  . ASN C 1 78  ? -12.173 22.080  23.427  1.00 21.65 ? 66  ASN C CB  1 
ATOM   3472 C  CG  . ASN C 1 78  ? -13.602 21.629  23.228  1.00 26.89 ? 66  ASN C CG  1 
ATOM   3473 O  OD1 . ASN C 1 78  ? -14.546 22.355  23.548  1.00 30.18 ? 66  ASN C OD1 1 
ATOM   3474 N  ND2 . ASN C 1 78  ? -13.771 20.431  22.678  1.00 28.84 ? 66  ASN C ND2 1 
ATOM   3475 N  N   . PRO C 1 79  ? -10.153 25.125  22.827  1.00 14.45 ? 67  PRO C N   1 
ATOM   3476 C  CA  . PRO C 1 79  ? -8.809  25.623  23.118  1.00 14.22 ? 67  PRO C CA  1 
ATOM   3477 C  C   . PRO C 1 79  ? -8.646  25.958  24.592  1.00 18.34 ? 67  PRO C C   1 
ATOM   3478 O  O   . PRO C 1 79  ? -9.606  26.225  25.312  1.00 20.08 ? 67  PRO C O   1 
ATOM   3479 C  CB  . PRO C 1 79  ? -8.720  26.897  22.269  1.00 16.10 ? 67  PRO C CB  1 
ATOM   3480 C  CG  . PRO C 1 79  ? -10.111 27.418  22.291  1.00 17.40 ? 67  PRO C CG  1 
ATOM   3481 C  CD  . PRO C 1 79  ? -11.019 26.184  22.277  1.00 17.76 ? 67  PRO C CD  1 
ATOM   3482 N  N   . ASN C 1 80  ? -7.389  25.949  25.027  1.00 16.48 ? 68  ASN C N   1 
ATOM   3483 C  CA  . ASN C 1 80  ? -6.984  26.517  26.317  1.00 16.73 ? 68  ASN C CA  1 
ATOM   3484 C  C   . ASN C 1 80  ? -5.841  27.476  25.994  1.00 14.56 ? 68  ASN C C   1 
ATOM   3485 O  O   . ASN C 1 80  ? -4.675  27.090  26.025  1.00 13.47 ? 68  ASN C O   1 
ATOM   3486 C  CB  . ASN C 1 80  ? -6.576  25.430  27.302  1.00 19.67 ? 68  ASN C CB  1 
ATOM   3487 C  CG  . ASN C 1 80  ? -6.214  25.987  28.665  1.00 24.84 ? 68  ASN C CG  1 
ATOM   3488 O  OD1 . ASN C 1 80  ? -6.671  27.064  29.048  1.00 29.86 ? 68  ASN C OD1 1 
ATOM   3489 N  ND2 . ASN C 1 80  ? -5.384  25.261  29.400  1.00 34.84 ? 68  ASN C ND2 1 
ATOM   3490 N  N   . GLY C 1 81  ? -6.186  28.703  25.614  1.00 15.39 ? 69  GLY C N   1 
ATOM   3491 C  CA  . GLY C 1 81  ? -5.212  29.682  25.174  1.00 15.54 ? 69  GLY C CA  1 
ATOM   3492 C  C   . GLY C 1 81  ? -5.391  30.053  23.712  1.00 13.07 ? 69  GLY C C   1 
ATOM   3493 O  O   . GLY C 1 81  ? -6.432  29.821  23.102  1.00 15.78 ? 69  GLY C O   1 
ATOM   3494 N  N   . ASN C 1 82  ? -4.326  30.615  23.142  1.00 13.63 ? 70  ASN C N   1 
ATOM   3495 C  CA  . ASN C 1 82  ? -4.356  31.230  21.817  1.00 14.95 ? 70  ASN C CA  1 
ATOM   3496 C  C   . ASN C 1 82  ? -4.678  30.213  20.714  1.00 15.45 ? 70  ASN C C   1 
ATOM   3497 O  O   . ASN C 1 82  ? -3.908  29.282  20.475  1.00 13.85 ? 70  ASN C O   1 
ATOM   3498 C  CB  . ASN C 1 82  ? -2.994  31.873  21.584  1.00 14.77 ? 70  ASN C CB  1 
ATOM   3499 C  CG  . ASN C 1 82  ? -2.932  32.716  20.347  1.00 21.40 ? 70  ASN C CG  1 
ATOM   3500 O  OD1 . ASN C 1 82  ? -3.865  32.752  19.544  1.00 24.22 ? 70  ASN C OD1 1 
ATOM   3501 N  ND2 . ASN C 1 82  ? -1.814  33.414  20.182  1.00 23.72 ? 70  ASN C ND2 1 
ATOM   3502 N  N   . SER C 1 83  ? -5.796  30.415  20.021  1.00 12.07 ? 71  SER C N   1 
ATOM   3503 C  CA  . SER C 1 83  ? -6.233  29.482  18.982  1.00 12.37 ? 71  SER C CA  1 
ATOM   3504 C  C   . SER C 1 83  ? -7.305  30.155  18.141  1.00 12.99 ? 71  SER C C   1 
ATOM   3505 O  O   . SER C 1 83  ? -8.037  31.012  18.634  1.00 10.26 ? 71  SER C O   1 
ATOM   3506 C  CB  . SER C 1 83  ? -6.778  28.187  19.608  1.00 12.54 ? 71  SER C CB  1 
ATOM   3507 O  OG  . SER C 1 83  ? -7.216  27.245  18.645  1.00 13.74 ? 71  SER C OG  1 
ATOM   3508 N  N   . TYR C 1 84  ? -7.407  29.755  16.875  1.00 9.61  ? 72  TYR C N   1 
ATOM   3509 C  CA  . TYR C 1 84  ? -8.565  30.202  16.123  1.00 13.64 ? 72  TYR C CA  1 
ATOM   3510 C  C   . TYR C 1 84  ? -8.961  29.147  15.104  1.00 11.74 ? 72  TYR C C   1 
ATOM   3511 O  O   . TYR C 1 84  ? -8.170  28.273  14.738  1.00 11.17 ? 72  TYR C O   1 
ATOM   3512 C  CB  . TYR C 1 84  ? -8.326  31.553  15.438  1.00 12.41 ? 72  TYR C CB  1 
ATOM   3513 C  CG  . TYR C 1 84  ? -7.053  31.663  14.631  1.00 15.34 ? 72  TYR C CG  1 
ATOM   3514 C  CD1 . TYR C 1 84  ? -5.869  32.098  15.218  1.00 18.95 ? 72  TYR C CD1 1 
ATOM   3515 C  CD2 . TYR C 1 84  ? -7.049  31.355  13.275  1.00 18.49 ? 72  TYR C CD2 1 
ATOM   3516 C  CE1 . TYR C 1 84  ? -4.705  32.212  14.472  1.00 21.73 ? 72  TYR C CE1 1 
ATOM   3517 C  CE2 . TYR C 1 84  ? -5.901  31.460  12.529  1.00 21.77 ? 72  TYR C CE2 1 
ATOM   3518 C  CZ  . TYR C 1 84  ? -4.737  31.895  13.123  1.00 24.04 ? 72  TYR C CZ  1 
ATOM   3519 O  OH  . TYR C 1 84  ? -3.597  31.991  12.355  1.00 29.71 ? 72  TYR C OH  1 
ATOM   3520 N  N   . LEU C 1 85  ? -10.213 29.254  14.666  1.00 9.98  ? 73  LEU C N   1 
ATOM   3521 C  CA  . LEU C 1 85  ? -10.842 28.362  13.704  1.00 10.41 ? 73  LEU C CA  1 
ATOM   3522 C  C   . LEU C 1 85  ? -11.233 29.211  12.504  1.00 11.81 ? 73  LEU C C   1 
ATOM   3523 O  O   . LEU C 1 85  ? -11.897 30.237  12.672  1.00 10.36 ? 73  LEU C O   1 
ATOM   3524 C  CB  . LEU C 1 85  ? -12.072 27.693  14.323  1.00 13.15 ? 73  LEU C CB  1 
ATOM   3525 C  CG  . LEU C 1 85  ? -12.852 26.710  13.456  1.00 15.18 ? 73  LEU C CG  1 
ATOM   3526 C  CD1 . LEU C 1 85  ? -12.034 25.459  13.209  1.00 17.90 ? 73  LEU C CD1 1 
ATOM   3527 C  CD2 . LEU C 1 85  ? -14.183 26.357  14.127  1.00 17.93 ? 73  LEU C CD2 1 
ATOM   3528 N  N   . SER C 1 86  ? -10.815 28.807  11.306  1.00 9.64  ? 74  SER C N   1 
ATOM   3529 C  CA  . SER C 1 86  ? -11.000 29.684  10.156  1.00 9.77  ? 74  SER C CA  1 
ATOM   3530 C  C   . SER C 1 86  ? -11.065 28.879  8.873   1.00 12.90 ? 74  SER C C   1 
ATOM   3531 O  O   . SER C 1 86  ? -10.611 27.735  8.811   1.00 15.61 ? 74  SER C O   1 
ATOM   3532 C  CB  . SER C 1 86  ? -9.851  30.697  10.041  1.00 13.77 ? 74  SER C CB  1 
ATOM   3533 O  OG  . SER C 1 86  ? -8.637  30.046  9.701   1.00 22.48 ? 74  SER C OG  1 
ATOM   3534 N  N   . VAL C 1 87  ? -11.611 29.506  7.840   1.00 9.31  ? 75  VAL C N   1 
ATOM   3535 C  CA  . VAL C 1 87  ? -11.333 29.076  6.474   1.00 11.31 ? 75  VAL C CA  1 
ATOM   3536 C  C   . VAL C 1 87  ? -10.026 29.733  6.051   1.00 12.48 ? 75  VAL C C   1 
ATOM   3537 O  O   . VAL C 1 87  ? -9.849  30.949  6.201   1.00 15.75 ? 75  VAL C O   1 
ATOM   3538 C  CB  . VAL C 1 87  ? -12.485 29.451  5.529   1.00 10.21 ? 75  VAL C CB  1 
ATOM   3539 C  CG1 . VAL C 1 87  ? -12.139 29.065  4.082   1.00 10.73 ? 75  VAL C CG1 1 
ATOM   3540 C  CG2 . VAL C 1 87  ? -13.784 28.764  5.957   1.00 13.18 ? 75  VAL C CG2 1 
ATOM   3541 N  N   . TYR C 1 88  ? -9.097  28.935  5.550   1.00 9.56  ? 76  TYR C N   1 
ATOM   3542 C  CA  . TYR C 1 88  ? -7.715  29.363  5.407   1.00 8.95  ? 76  TYR C CA  1 
ATOM   3543 C  C   . TYR C 1 88  ? -7.193  28.927  4.052   1.00 9.55  ? 76  TYR C C   1 
ATOM   3544 O  O   . TYR C 1 88  ? -7.423  27.790  3.640   1.00 10.15 ? 76  TYR C O   1 
ATOM   3545 C  CB  . TYR C 1 88  ? -6.863  28.731  6.515   1.00 10.40 ? 76  TYR C CB  1 
ATOM   3546 C  CG  . TYR C 1 88  ? -5.372  28.846  6.322   1.00 12.12 ? 76  TYR C CG  1 
ATOM   3547 C  CD1 . TYR C 1 88  ? -4.745  30.077  6.403   1.00 12.93 ? 76  TYR C CD1 1 
ATOM   3548 C  CD2 . TYR C 1 88  ? -4.593  27.725  6.064   1.00 11.48 ? 76  TYR C CD2 1 
ATOM   3549 C  CE1 . TYR C 1 88  ? -3.392  30.201  6.251   1.00 13.31 ? 76  TYR C CE1 1 
ATOM   3550 C  CE2 . TYR C 1 88  ? -3.218  27.835  5.911   1.00 12.59 ? 76  TYR C CE2 1 
ATOM   3551 C  CZ  . TYR C 1 88  ? -2.628  29.080  6.000   1.00 13.82 ? 76  TYR C CZ  1 
ATOM   3552 O  OH  . TYR C 1 88  ? -1.275  29.226  5.846   1.00 12.85 ? 76  TYR C OH  1 
ATOM   3553 N  N   . GLY C 1 89  ? -6.488  29.807  3.355   1.00 7.74  ? 77  GLY C N   1 
ATOM   3554 C  CA  . GLY C 1 89  ? -5.992  29.372  2.061   1.00 8.45  ? 77  GLY C CA  1 
ATOM   3555 C  C   . GLY C 1 89  ? -4.980  30.324  1.464   1.00 8.02  ? 77  GLY C C   1 
ATOM   3556 O  O   . GLY C 1 89  ? -4.589  31.316  2.082   1.00 9.78  ? 77  GLY C O   1 
ATOM   3557 N  N   . TRP C 1 90  ? -4.606  30.025  0.217   1.00 8.97  ? 78  TRP C N   1 
ATOM   3558 C  CA  . TRP C 1 90  ? -3.549  30.753  -0.480  1.00 9.16  ? 78  TRP C CA  1 
ATOM   3559 C  C   . TRP C 1 90  ? -3.964  31.086  -1.903  1.00 11.85 ? 78  TRP C C   1 
ATOM   3560 O  O   . TRP C 1 90  ? -4.708  30.337  -2.529  1.00 9.85  ? 78  TRP C O   1 
ATOM   3561 C  CB  . TRP C 1 90  ? -2.258  29.925  -0.554  1.00 11.22 ? 78  TRP C CB  1 
ATOM   3562 C  CG  . TRP C 1 90  ? -1.578  29.779  0.759   1.00 10.67 ? 78  TRP C CG  1 
ATOM   3563 C  CD1 . TRP C 1 90  ? -1.853  28.857  1.734   1.00 10.37 ? 78  TRP C CD1 1 
ATOM   3564 C  CD2 . TRP C 1 90  ? -0.521  30.591  1.258   1.00 13.29 ? 78  TRP C CD2 1 
ATOM   3565 N  NE1 . TRP C 1 90  ? -1.027  29.049  2.811   1.00 11.77 ? 78  TRP C NE1 1 
ATOM   3566 C  CE2 . TRP C 1 90  ? -0.192  30.105  2.543   1.00 11.94 ? 78  TRP C CE2 1 
ATOM   3567 C  CE3 . TRP C 1 90  ? 0.194   31.677  0.739   1.00 14.77 ? 78  TRP C CE3 1 
ATOM   3568 C  CZ2 . TRP C 1 90  ? 0.823   30.668  3.317   1.00 14.85 ? 78  TRP C CZ2 1 
ATOM   3569 C  CZ3 . TRP C 1 90  ? 1.198   32.243  1.513   1.00 14.01 ? 78  TRP C CZ3 1 
ATOM   3570 C  CH2 . TRP C 1 90  ? 1.502   31.736  2.787   1.00 16.22 ? 78  TRP C CH2 1 
ATOM   3571 N  N   . THR C 1 91  ? -3.431  32.190  -2.428  1.00 10.65 ? 79  THR C N   1 
ATOM   3572 C  CA  . THR C 1 91  ? -3.389  32.385  -3.876  1.00 10.00 ? 79  THR C CA  1 
ATOM   3573 C  C   . THR C 1 91  ? -1.939  32.565  -4.295  1.00 12.40 ? 79  THR C C   1 
ATOM   3574 O  O   . THR C 1 91  ? -1.062  32.826  -3.467  1.00 13.17 ? 79  THR C O   1 
ATOM   3575 C  CB  . THR C 1 91  ? -4.218  33.594  -4.361  1.00 14.16 ? 79  THR C CB  1 
ATOM   3576 O  OG1 . THR C 1 91  ? -3.600  34.831  -3.973  1.00 13.04 ? 79  THR C OG1 1 
ATOM   3577 C  CG2 . THR C 1 91  ? -5.637  33.543  -3.832  1.00 13.49 ? 79  THR C CG2 1 
ATOM   3578 N  N   . GLN C 1 92  ? -1.689  32.383  -5.586  1.00 13.24 ? 80  GLN C N   1 
ATOM   3579 C  CA  . GLN C 1 92  ? -0.364  32.592  -6.151  1.00 12.79 ? 80  GLN C CA  1 
ATOM   3580 C  C   . GLN C 1 92  ? -0.456  33.638  -7.248  1.00 13.59 ? 80  GLN C C   1 
ATOM   3581 O  O   . GLN C 1 92  ? -1.486  33.771  -7.913  1.00 14.44 ? 80  GLN C O   1 
ATOM   3582 C  CB  . GLN C 1 92  ? 0.211   31.296  -6.723  1.00 17.05 ? 80  GLN C CB  1 
ATOM   3583 C  CG  . GLN C 1 92  ? 0.555   30.258  -5.663  1.00 15.21 ? 80  GLN C CG  1 
ATOM   3584 C  CD  . GLN C 1 92  ? 0.525   28.841  -6.208  1.00 24.75 ? 80  GLN C CD  1 
ATOM   3585 O  OE1 . GLN C 1 92  ? -0.516  28.352  -6.655  1.00 26.77 ? 80  GLN C OE1 1 
ATOM   3586 N  NE2 . GLN C 1 92  ? 1.671   28.179  -6.181  1.00 27.65 ? 80  GLN C NE2 1 
ATOM   3587 N  N   . ASN C 1 93  ? 0.617   34.401  -7.409  1.00 14.57 ? 81  ASN C N   1 
ATOM   3588 C  CA  . ASN C 1 93  ? 0.749   35.338  -8.518  1.00 15.11 ? 81  ASN C CA  1 
ATOM   3589 C  C   . ASN C 1 93  ? -0.415  36.325  -8.612  1.00 12.83 ? 81  ASN C C   1 
ATOM   3590 O  O   . ASN C 1 93  ? -1.142  36.350  -9.618  1.00 14.92 ? 81  ASN C O   1 
ATOM   3591 C  CB  . ASN C 1 93  ? 0.919   34.568  -9.821  1.00 15.26 ? 81  ASN C CB  1 
ATOM   3592 C  CG  . ASN C 1 93  ? 1.342   35.458  -10.965 1.00 18.15 ? 81  ASN C CG  1 
ATOM   3593 O  OD1 . ASN C 1 93  ? 2.001   36.476  -10.756 1.00 15.45 ? 81  ASN C OD1 1 
ATOM   3594 N  ND2 . ASN C 1 93  ? 0.956   35.083  -12.186 1.00 17.15 ? 81  ASN C ND2 1 
ATOM   3595 N  N   . PRO C 1 94  ? -0.602  37.196  -7.607  1.00 14.40 ? 82  PRO C N   1 
ATOM   3596 C  CA  . PRO C 1 94  ? 0.258   37.395  -6.429  1.00 15.34 ? 82  PRO C CA  1 
ATOM   3597 C  C   . PRO C 1 94  ? 0.045   36.394  -5.292  1.00 18.60 ? 82  PRO C C   1 
ATOM   3598 O  O   . PRO C 1 94  ? -1.053  35.857  -5.125  1.00 14.90 ? 82  PRO C O   1 
ATOM   3599 C  CB  . PRO C 1 94  ? -0.130  38.795  -5.962  1.00 15.74 ? 82  PRO C CB  1 
ATOM   3600 C  CG  . PRO C 1 94  ? -1.560  38.911  -6.333  1.00 17.60 ? 82  PRO C CG  1 
ATOM   3601 C  CD  . PRO C 1 94  ? -1.669  38.212  -7.673  1.00 14.47 ? 82  PRO C CD  1 
ATOM   3602 N  N   . LEU C 1 95  ? 1.112   36.172  -4.529  1.00 14.92 ? 83  LEU C N   1 
ATOM   3603 C  CA  . LEU C 1 95  ? 1.075   35.298  -3.360  1.00 15.44 ? 83  LEU C CA  1 
ATOM   3604 C  C   . LEU C 1 95  ? 0.303   35.966  -2.222  1.00 14.49 ? 83  LEU C C   1 
ATOM   3605 O  O   . LEU C 1 95  ? 0.687   37.038  -1.736  1.00 12.84 ? 83  LEU C O   1 
ATOM   3606 C  CB  . LEU C 1 95  ? 2.502   34.969  -2.934  1.00 16.30 ? 83  LEU C CB  1 
ATOM   3607 C  CG  . LEU C 1 95  ? 2.707   33.908  -1.864  1.00 15.02 ? 83  LEU C CG  1 
ATOM   3608 C  CD1 . LEU C 1 95  ? 2.230   32.555  -2.390  1.00 13.39 ? 83  LEU C CD1 1 
ATOM   3609 C  CD2 . LEU C 1 95  ? 4.189   33.850  -1.475  1.00 15.94 ? 83  LEU C CD2 1 
ATOM   3610 N  N   . VAL C 1 96  ? -0.789  35.333  -1.793  1.00 11.70 ? 84  VAL C N   1 
ATOM   3611 C  CA  . VAL C 1 96  ? -1.644  35.864  -0.740  1.00 10.88 ? 84  VAL C CA  1 
ATOM   3612 C  C   . VAL C 1 96  ? -1.987  34.728  0.208   1.00 13.51 ? 84  VAL C C   1 
ATOM   3613 O  O   . VAL C 1 96  ? -2.312  33.622  -0.236  1.00 11.80 ? 84  VAL C O   1 
ATOM   3614 C  CB  . VAL C 1 96  ? -2.941  36.473  -1.304  1.00 12.58 ? 84  VAL C CB  1 
ATOM   3615 C  CG1 . VAL C 1 96  ? -3.889  36.868  -0.161  1.00 16.06 ? 84  VAL C CG1 1 
ATOM   3616 C  CG2 . VAL C 1 96  ? -2.639  37.666  -2.208  1.00 13.11 ? 84  VAL C CG2 1 
ATOM   3617 N  N   . GLU C 1 97  ? -1.925  35.006  1.505   1.00 11.76 ? 85  GLU C N   1 
ATOM   3618 C  CA  . GLU C 1 97  ? -2.447  34.131  2.546   1.00 11.71 ? 85  GLU C CA  1 
ATOM   3619 C  C   . GLU C 1 97  ? -3.698  34.783  3.117   1.00 10.53 ? 85  GLU C C   1 
ATOM   3620 O  O   . GLU C 1 97  ? -3.692  35.980  3.412   1.00 13.36 ? 85  GLU C O   1 
ATOM   3621 C  CB  . GLU C 1 97  ? -1.406  33.916  3.645   1.00 12.49 ? 85  GLU C CB  1 
ATOM   3622 C  CG  . GLU C 1 97  ? -1.771  32.814  4.625   1.00 14.21 ? 85  GLU C CG  1 
ATOM   3623 C  CD  . GLU C 1 97  ? -0.824  32.753  5.821   1.00 16.34 ? 85  GLU C CD  1 
ATOM   3624 O  OE1 . GLU C 1 97  ? -0.564  31.639  6.317   1.00 15.23 ? 85  GLU C OE1 1 
ATOM   3625 O  OE2 . GLU C 1 97  ? -0.360  33.816  6.272   1.00 15.31 ? 85  GLU C OE2 1 
ATOM   3626 N  N   . TYR C 1 98  ? -4.772  34.015  3.277   1.00 11.84 ? 86  TYR C N   1 
ATOM   3627 C  CA  . TYR C 1 98  ? -6.005  34.623  3.753   1.00 10.74 ? 86  TYR C CA  1 
ATOM   3628 C  C   . TYR C 1 98  ? -6.678  33.750  4.802   1.00 14.95 ? 86  TYR C C   1 
ATOM   3629 O  O   . TYR C 1 98  ? -6.541  32.523  4.798   1.00 10.51 ? 86  TYR C O   1 
ATOM   3630 C  CB  . TYR C 1 98  ? -6.988  34.905  2.602   1.00 10.47 ? 86  TYR C CB  1 
ATOM   3631 C  CG  . TYR C 1 98  ? -7.506  33.662  1.907   1.00 11.51 ? 86  TYR C CG  1 
ATOM   3632 C  CD1 . TYR C 1 98  ? -8.587  32.946  2.422   1.00 10.98 ? 86  TYR C CD1 1 
ATOM   3633 C  CD2 . TYR C 1 98  ? -6.922  33.213  0.722   1.00 12.96 ? 86  TYR C CD2 1 
ATOM   3634 C  CE1 . TYR C 1 98  ? -9.058  31.808  1.782   1.00 13.09 ? 86  TYR C CE1 1 
ATOM   3635 C  CE2 . TYR C 1 98  ? -7.390  32.080  0.084   1.00 11.14 ? 86  TYR C CE2 1 
ATOM   3636 C  CZ  . TYR C 1 98  ? -8.457  31.385  0.619   1.00 12.71 ? 86  TYR C CZ  1 
ATOM   3637 O  OH  . TYR C 1 98  ? -8.924  30.253  -0.021  1.00 13.32 ? 86  TYR C OH  1 
ATOM   3638 N  N   . TYR C 1 99  ? -7.440  34.415  5.676   1.00 12.42 ? 87  TYR C N   1 
ATOM   3639 C  CA  . TYR C 1 99  ? -8.137  33.806  6.803   1.00 12.44 ? 87  TYR C CA  1 
ATOM   3640 C  C   . TYR C 1 99  ? -9.546  34.363  6.883   1.00 12.31 ? 87  TYR C C   1 
ATOM   3641 O  O   . TYR C 1 99  ? -9.718  35.584  6.911   1.00 13.47 ? 87  TYR C O   1 
ATOM   3642 C  CB  . TYR C 1 99  ? -7.456  34.117  8.131   1.00 13.66 ? 87  TYR C CB  1 
ATOM   3643 C  CG  . TYR C 1 99  ? -6.138  33.460  8.359   1.00 14.57 ? 87  TYR C CG  1 
ATOM   3644 C  CD1 . TYR C 1 99  ? -4.955  34.077  7.972   1.00 19.76 ? 87  TYR C CD1 1 
ATOM   3645 C  CD2 . TYR C 1 99  ? -6.067  32.242  9.014   1.00 18.07 ? 87  TYR C CD2 1 
ATOM   3646 C  CE1 . TYR C 1 99  ? -3.736  33.477  8.217   1.00 19.82 ? 87  TYR C CE1 1 
ATOM   3647 C  CE2 . TYR C 1 99  ? -4.863  31.643  9.259   1.00 24.37 ? 87  TYR C CE2 1 
ATOM   3648 C  CZ  . TYR C 1 99  ? -3.701  32.261  8.854   1.00 22.09 ? 87  TYR C CZ  1 
ATOM   3649 O  OH  . TYR C 1 99  ? -2.491  31.645  9.098   1.00 32.98 ? 87  TYR C OH  1 
ATOM   3650 N  N   . ILE C 1 100 ? -10.536 33.480  6.967   1.00 11.13 ? 88  ILE C N   1 
ATOM   3651 C  CA  . ILE C 1 100 ? -11.903 33.854  7.315   1.00 11.02 ? 88  ILE C CA  1 
ATOM   3652 C  C   . ILE C 1 100 ? -12.145 33.276  8.703   1.00 10.90 ? 88  ILE C C   1 
ATOM   3653 O  O   . ILE C 1 100 ? -12.414 32.080  8.847   1.00 11.55 ? 88  ILE C O   1 
ATOM   3654 C  CB  . ILE C 1 100 ? -12.923 33.345  6.291   1.00 12.73 ? 88  ILE C CB  1 
ATOM   3655 C  CG1 . ILE C 1 100 ? -12.628 33.954  4.912   1.00 12.28 ? 88  ILE C CG1 1 
ATOM   3656 C  CG2 . ILE C 1 100 ? -14.358 33.682  6.731   1.00 11.02 ? 88  ILE C CG2 1 
ATOM   3657 C  CD1 . ILE C 1 100 ? -13.203 33.151  3.762   1.00 13.66 ? 88  ILE C CD1 1 
ATOM   3658 N  N   . VAL C 1 101 ? -12.011 34.104  9.736   1.00 10.45 ? 89  VAL C N   1 
ATOM   3659 C  CA  . VAL C 1 101 ? -11.941 33.614  11.114  1.00 10.86 ? 89  VAL C CA  1 
ATOM   3660 C  C   . VAL C 1 101 ? -13.350 33.505  11.682  1.00 11.96 ? 89  VAL C C   1 
ATOM   3661 O  O   . VAL C 1 101 ? -14.086 34.494  11.746  1.00 12.52 ? 89  VAL C O   1 
ATOM   3662 C  CB  . VAL C 1 101 ? -11.060 34.518  11.986  1.00 10.66 ? 89  VAL C CB  1 
ATOM   3663 C  CG1 . VAL C 1 101 ? -11.029 33.996  13.424  1.00 10.90 ? 89  VAL C CG1 1 
ATOM   3664 C  CG2 . VAL C 1 101 ? -9.641  34.575  11.413  1.00 11.01 ? 89  VAL C CG2 1 
ATOM   3665 N  N   . GLU C 1 102 ? -13.720 32.299  12.106  1.00 10.55 ? 90  GLU C N   1 
ATOM   3666 C  CA  . GLU C 1 102 ? -15.042 32.026  12.658  1.00 12.67 ? 90  GLU C CA  1 
ATOM   3667 C  C   . GLU C 1 102 ? -15.083 32.126  14.175  1.00 15.17 ? 90  GLU C C   1 
ATOM   3668 O  O   . GLU C 1 102 ? -16.113 32.528  14.731  1.00 14.13 ? 90  GLU C O   1 
ATOM   3669 C  CB  . GLU C 1 102 ? -15.498 30.626  12.247  1.00 15.32 ? 90  GLU C CB  1 
ATOM   3670 C  CG  . GLU C 1 102 ? -15.688 30.444  10.755  1.00 15.26 ? 90  GLU C CG  1 
ATOM   3671 C  CD  . GLU C 1 102 ? -16.945 31.119  10.269  1.00 19.38 ? 90  GLU C CD  1 
ATOM   3672 O  OE1 . GLU C 1 102 ? -16.852 32.277  9.836   1.00 20.60 ? 90  GLU C OE1 1 
ATOM   3673 O  OE2 . GLU C 1 102 ? -18.028 30.499  10.338  1.00 24.60 ? 90  GLU C OE2 1 
ATOM   3674 N  N   . SER C 1 103 ? -13.993 31.740  14.840  1.00 12.81 ? 91  SER C N   1 
ATOM   3675 C  CA  . SER C 1 103 ? -13.817 31.880  16.281  1.00 14.63 ? 91  SER C CA  1 
ATOM   3676 C  C   . SER C 1 103 ? -12.345 32.122  16.568  1.00 12.91 ? 91  SER C C   1 
ATOM   3677 O  O   . SER C 1 103 ? -11.472 31.594  15.878  1.00 13.18 ? 91  SER C O   1 
ATOM   3678 C  CB  . SER C 1 103 ? -14.253 30.629  17.053  1.00 14.21 ? 91  SER C CB  1 
ATOM   3679 O  OG  . SER C 1 103 ? -15.653 30.443  17.045  1.00 16.80 ? 91  SER C OG  1 
ATOM   3680 N  N   . PHE C 1 104 ? -12.071 32.907  17.604  1.00 12.09 ? 92  PHE C N   1 
ATOM   3681 C  CA  . PHE C 1 104 ? -10.739 32.928  18.195  1.00 13.26 ? 92  PHE C CA  1 
ATOM   3682 C  C   . PHE C 1 104 ? -10.904 32.988  19.707  1.00 16.31 ? 92  PHE C C   1 
ATOM   3683 O  O   . PHE C 1 104 ? -11.957 33.386  20.207  1.00 15.06 ? 92  PHE C O   1 
ATOM   3684 C  CB  . PHE C 1 104 ? -9.866  34.093  17.663  1.00 13.92 ? 92  PHE C CB  1 
ATOM   3685 C  CG  . PHE C 1 104 ? -10.375 35.475  18.024  1.00 15.08 ? 92  PHE C CG  1 
ATOM   3686 C  CD1 . PHE C 1 104 ? -10.119 36.025  19.271  1.00 16.23 ? 92  PHE C CD1 1 
ATOM   3687 C  CD2 . PHE C 1 104 ? -11.071 36.234  17.096  1.00 14.98 ? 92  PHE C CD2 1 
ATOM   3688 C  CE1 . PHE C 1 104 ? -10.574 37.291  19.598  1.00 16.77 ? 92  PHE C CE1 1 
ATOM   3689 C  CE2 . PHE C 1 104 ? -11.525 37.510  17.414  1.00 14.48 ? 92  PHE C CE2 1 
ATOM   3690 C  CZ  . PHE C 1 104 ? -11.272 38.034  18.677  1.00 14.73 ? 92  PHE C CZ  1 
ATOM   3691 N  N   . SER C 1 105 ? -9.858  32.592  20.444  1.00 11.99 ? 93  SER C N   1 
ATOM   3692 C  CA  . SER C 1 105 ? -10.038 32.538  21.896  1.00 16.38 ? 93  SER C CA  1 
ATOM   3693 C  C   . SER C 1 105 ? -9.453  33.764  22.604  1.00 24.35 ? 93  SER C C   1 
ATOM   3694 O  O   . SER C 1 105 ? -10.166 34.748  22.824  1.00 37.03 ? 93  SER C O   1 
ATOM   3695 C  CB  . SER C 1 105 ? -9.459  31.241  22.478  1.00 18.80 ? 93  SER C CB  1 
ATOM   3696 O  OG  . SER C 1 105 ? -8.286  30.820  21.800  1.00 26.48 ? 93  SER C OG  1 
ATOM   3697 N  N   . THR C 1 106 ? -8.165  33.735  22.941  1.00 22.38 ? 94  THR C N   1 
ATOM   3698 C  CA  . THR C 1 106 ? -7.545  34.711  23.843  1.00 14.87 ? 94  THR C CA  1 
ATOM   3699 C  C   . THR C 1 106 ? -6.757  35.813  23.137  1.00 18.18 ? 94  THR C C   1 
ATOM   3700 O  O   . THR C 1 106 ? -6.240  36.723  23.808  1.00 18.75 ? 94  THR C O   1 
ATOM   3701 C  CB  . THR C 1 106 ? -6.617  33.987  24.815  1.00 19.05 ? 94  THR C CB  1 
ATOM   3702 O  OG1 . THR C 1 106 ? -5.539  33.394  24.082  1.00 21.25 ? 94  THR C OG1 1 
ATOM   3703 C  CG2 . THR C 1 106 ? -7.376  32.902  25.554  1.00 17.89 ? 94  THR C CG2 1 
ATOM   3704 N  N   . TYR C 1 107 ? -6.614  35.745  21.821  1.00 14.34 ? 95  TYR C N   1 
ATOM   3705 C  CA  . TYR C 1 107 ? -5.843  36.740  21.087  1.00 14.78 ? 95  TYR C CA  1 
ATOM   3706 C  C   . TYR C 1 107 ? -6.495  36.889  19.725  1.00 14.86 ? 95  TYR C C   1 
ATOM   3707 O  O   . TYR C 1 107 ? -6.671  35.894  19.014  1.00 13.88 ? 95  TYR C O   1 
ATOM   3708 C  CB  . TYR C 1 107 ? -4.390  36.316  20.949  1.00 11.05 ? 95  TYR C CB  1 
ATOM   3709 C  CG  . TYR C 1 107 ? -3.493  37.278  20.206  1.00 13.89 ? 95  TYR C CG  1 
ATOM   3710 C  CD1 . TYR C 1 107 ? -2.948  38.382  20.844  1.00 17.46 ? 95  TYR C CD1 1 
ATOM   3711 C  CD2 . TYR C 1 107 ? -3.170  37.066  18.864  1.00 17.62 ? 95  TYR C CD2 1 
ATOM   3712 C  CE1 . TYR C 1 107 ? -2.093  39.260  20.166  1.00 15.54 ? 95  TYR C CE1 1 
ATOM   3713 C  CE2 . TYR C 1 107 ? -2.327  37.933  18.179  1.00 15.94 ? 95  TYR C CE2 1 
ATOM   3714 C  CZ  . TYR C 1 107 ? -1.795  39.030  18.835  1.00 17.79 ? 95  TYR C CZ  1 
ATOM   3715 O  OH  . TYR C 1 107 ? -0.960  39.900  18.164  1.00 17.44 ? 95  TYR C OH  1 
ATOM   3716 N  N   . ASP C 1 108 ? -6.867  38.111  19.382  1.00 16.02 ? 96  ASP C N   1 
ATOM   3717 C  CA  . ASP C 1 108 ? -7.437  38.392  18.071  1.00 14.30 ? 96  ASP C CA  1 
ATOM   3718 C  C   . ASP C 1 108 ? -6.320  38.317  17.040  1.00 15.79 ? 96  ASP C C   1 
ATOM   3719 O  O   . ASP C 1 108 ? -5.430  39.178  17.048  1.00 16.07 ? 96  ASP C O   1 
ATOM   3720 C  CB  . ASP C 1 108 ? -8.110  39.777  18.079  1.00 14.72 ? 96  ASP C CB  1 
ATOM   3721 C  CG  . ASP C 1 108 ? -8.858  40.090  16.780  1.00 18.19 ? 96  ASP C CG  1 
ATOM   3722 O  OD1 . ASP C 1 108 ? -8.521  39.514  15.727  1.00 18.54 ? 96  ASP C OD1 1 
ATOM   3723 O  OD2 . ASP C 1 108 ? -9.783  40.942  16.815  1.00 17.08 ? 96  ASP C OD2 1 
ATOM   3724 N  N   . PRO C 1 109 ? -6.325  37.333  16.133  1.00 14.57 ? 97  PRO C N   1 
ATOM   3725 C  CA  . PRO C 1 109 ? -5.197  37.185  15.206  1.00 15.25 ? 97  PRO C CA  1 
ATOM   3726 C  C   . PRO C 1 109 ? -5.112  38.302  14.179  1.00 13.62 ? 97  PRO C C   1 
ATOM   3727 O  O   . PRO C 1 109 ? -4.082  38.399  13.489  1.00 16.51 ? 97  PRO C O   1 
ATOM   3728 C  CB  . PRO C 1 109 ? -5.461  35.827  14.545  1.00 16.69 ? 97  PRO C CB  1 
ATOM   3729 C  CG  . PRO C 1 109 ? -6.957  35.684  14.575  1.00 14.86 ? 97  PRO C CG  1 
ATOM   3730 C  CD  . PRO C 1 109 ? -7.407  36.372  15.862  1.00 15.64 ? 97  PRO C CD  1 
ATOM   3731 N  N   . SER C 1 110 ? -6.134  39.155  14.075  1.00 13.71 ? 98  SER C N   1 
ATOM   3732 C  CA  . SER C 1 110 ? -6.055  40.336  13.225  1.00 16.70 ? 98  SER C CA  1 
ATOM   3733 C  C   . SER C 1 110 ? -5.275  41.483  13.866  1.00 20.00 ? 98  SER C C   1 
ATOM   3734 O  O   . SER C 1 110 ? -5.050  42.501  13.199  1.00 19.63 ? 98  SER C O   1 
ATOM   3735 C  CB  . SER C 1 110 ? -7.477  40.809  12.864  1.00 16.24 ? 98  SER C CB  1 
ATOM   3736 O  OG  . SER C 1 110 ? -8.115  41.489  13.930  1.00 17.22 ? 98  SER C OG  1 
ATOM   3737 N  N   . THR C 1 111 ? -4.837  41.334  15.119  1.00 15.15 ? 99  THR C N   1 
ATOM   3738 C  CA  . THR C 1 111 ? -4.101  42.394  15.805  1.00 15.97 ? 99  THR C CA  1 
ATOM   3739 C  C   . THR C 1 111 ? -2.869  42.800  15.005  1.00 17.79 ? 99  THR C C   1 
ATOM   3740 O  O   . THR C 1 111 ? -2.080  41.953  14.575  1.00 18.49 ? 99  THR C O   1 
ATOM   3741 C  CB  . THR C 1 111 ? -3.674  41.932  17.212  1.00 16.85 ? 99  THR C CB  1 
ATOM   3742 O  OG1 . THR C 1 111 ? -4.832  41.628  17.996  1.00 15.42 ? 99  THR C OG1 1 
ATOM   3743 C  CG2 . THR C 1 111 ? -2.866  43.020  17.924  1.00 18.52 ? 99  THR C CG2 1 
ATOM   3744 N  N   . GLY C 1 112 ? -2.701  44.109  14.823  1.00 19.16 ? 100 GLY C N   1 
ATOM   3745 C  CA  . GLY C 1 112 ? -1.611  44.631  14.034  1.00 19.91 ? 100 GLY C CA  1 
ATOM   3746 C  C   . GLY C 1 112 ? -1.940  44.834  12.574  1.00 22.94 ? 100 GLY C C   1 
ATOM   3747 O  O   . GLY C 1 112 ? -1.150  45.458  11.855  1.00 24.23 ? 100 GLY C O   1 
ATOM   3748 N  N   . ALA C 1 113 ? -3.082  44.343  12.116  1.00 21.57 ? 101 ALA C N   1 
ATOM   3749 C  CA  . ALA C 1 113 ? -3.491  44.516  10.731  1.00 18.30 ? 101 ALA C CA  1 
ATOM   3750 C  C   . ALA C 1 113 ? -4.375  45.751  10.570  1.00 18.81 ? 101 ALA C C   1 
ATOM   3751 O  O   . ALA C 1 113 ? -5.043  46.192  11.506  1.00 18.60 ? 101 ALA C O   1 
ATOM   3752 C  CB  . ALA C 1 113 ? -4.216  43.262  10.241  1.00 15.70 ? 101 ALA C CB  1 
ATOM   3753 N  N   . GLN C 1 114 ? -4.382  46.310  9.355   1.00 17.16 ? 102 GLN C N   1 
ATOM   3754 C  CA  . GLN C 1 114 ? -5.192  47.498  9.097   1.00 18.60 ? 102 GLN C CA  1 
ATOM   3755 C  C   . GLN C 1 114 ? -6.642  47.114  8.822   1.00 17.75 ? 102 GLN C C   1 
ATOM   3756 O  O   . GLN C 1 114 ? -6.929  46.352  7.889   1.00 17.13 ? 102 GLN C O   1 
ATOM   3757 C  CB  . GLN C 1 114 ? -4.645  48.309  7.926   1.00 19.62 ? 102 GLN C CB  1 
ATOM   3758 C  CG  . GLN C 1 114 ? -5.466  49.592  7.710   1.00 20.43 ? 102 GLN C CG  1 
ATOM   3759 C  CD  . GLN C 1 114 ? -5.148  50.321  6.414   1.00 29.30 ? 102 GLN C CD  1 
ATOM   3760 O  OE1 . GLN C 1 114 ? -4.353  49.853  5.594   1.00 30.76 ? 102 GLN C OE1 1 
ATOM   3761 N  NE2 . GLN C 1 114 ? -5.778  51.482  6.222   1.00 28.18 ? 102 GLN C NE2 1 
ATOM   3762 N  N   . GLU C 1 115 ? -7.551  47.681  9.611   1.00 13.99 ? 103 GLU C N   1 
ATOM   3763 C  CA  . GLU C 1 115 ? -8.981  47.474  9.416   1.00 19.51 ? 103 GLU C CA  1 
ATOM   3764 C  C   . GLU C 1 115 ? -9.474  48.279  8.219   1.00 22.03 ? 103 GLU C C   1 
ATOM   3765 O  O   . GLU C 1 115 ? -9.219  49.483  8.121   1.00 19.95 ? 103 GLU C O   1 
ATOM   3766 C  CB  . GLU C 1 115 ? -9.735  47.881  10.679  1.00 18.71 ? 103 GLU C CB  1 
ATOM   3767 C  CG  . GLU C 1 115 ? -11.164 47.376  10.773  1.00 24.58 ? 103 GLU C CG  1 
ATOM   3768 C  CD  . GLU C 1 115 ? -11.745 47.580  12.173  1.00 30.87 ? 103 GLU C CD  1 
ATOM   3769 O  OE1 . GLU C 1 115 ? -12.982 47.484  12.334  1.00 34.58 ? 103 GLU C OE1 1 
ATOM   3770 O  OE2 . GLU C 1 115 ? -10.955 47.830  13.114  1.00 36.53 ? 103 GLU C OE2 1 
ATOM   3771 N  N   . LEU C 1 116 ? -10.204 47.619  7.313   1.00 18.48 ? 104 LEU C N   1 
ATOM   3772 C  CA  . LEU C 1 116 ? -10.633 48.239  6.068   1.00 17.62 ? 104 LEU C CA  1 
ATOM   3773 C  C   . LEU C 1 116 ? -12.137 48.390  5.938   1.00 23.11 ? 104 LEU C C   1 
ATOM   3774 O  O   . LEU C 1 116 ? -12.588 49.194  5.115   1.00 25.44 ? 104 LEU C O   1 
ATOM   3775 C  CB  . LEU C 1 116 ? -10.120 47.433  4.860   1.00 20.68 ? 104 LEU C CB  1 
ATOM   3776 C  CG  . LEU C 1 116 ? -8.597  47.326  4.760   1.00 23.26 ? 104 LEU C CG  1 
ATOM   3777 C  CD1 . LEU C 1 116 ? -8.184  46.446  3.584   1.00 25.01 ? 104 LEU C CD1 1 
ATOM   3778 C  CD2 . LEU C 1 116 ? -7.978  48.718  4.628   1.00 20.97 ? 104 LEU C CD2 1 
ATOM   3779 N  N   . GLY C 1 117 ? -12.920 47.655  6.710   1.00 20.93 ? 105 GLY C N   1 
ATOM   3780 C  CA  . GLY C 1 117 ? -14.360 47.710  6.571   1.00 22.08 ? 105 GLY C CA  1 
ATOM   3781 C  C   . GLY C 1 117 ? -14.978 46.433  7.108   1.00 22.65 ? 105 GLY C C   1 
ATOM   3782 O  O   . GLY C 1 117 ? -14.381 45.741  7.932   1.00 21.45 ? 105 GLY C O   1 
ATOM   3783 N  N   . THR C 1 118 ? -16.187 46.148  6.623   1.00 20.75 ? 106 THR C N   1 
ATOM   3784 C  CA  . THR C 1 118 ? -16.935 44.981  7.071   1.00 22.26 ? 106 THR C CA  1 
ATOM   3785 C  C   . THR C 1 118 ? -17.659 44.347  5.894   1.00 23.10 ? 106 THR C C   1 
ATOM   3786 O  O   . THR C 1 118 ? -17.883 44.974  4.856   1.00 25.07 ? 106 THR C O   1 
ATOM   3787 C  CB  . THR C 1 118 ? -17.993 45.311  8.141   1.00 23.83 ? 106 THR C CB  1 
ATOM   3788 O  OG1 . THR C 1 118 ? -18.948 46.223  7.585   1.00 29.00 ? 106 THR C OG1 1 
ATOM   3789 C  CG2 . THR C 1 118 ? -17.373 45.911  9.401   1.00 25.19 ? 106 THR C CG2 1 
ATOM   3790 N  N   . VAL C 1 119 ? -18.057 43.094  6.091   1.00 21.95 ? 107 VAL C N   1 
ATOM   3791 C  CA  . VAL C 1 119 ? -18.925 42.388  5.159   1.00 20.16 ? 107 VAL C CA  1 
ATOM   3792 C  C   . VAL C 1 119 ? -19.951 41.612  5.973   1.00 23.57 ? 107 VAL C C   1 
ATOM   3793 O  O   . VAL C 1 119 ? -19.635 41.063  7.035   1.00 18.06 ? 107 VAL C O   1 
ATOM   3794 C  CB  . VAL C 1 119 ? -18.112 41.470  4.216   1.00 19.89 ? 107 VAL C CB  1 
ATOM   3795 C  CG1 . VAL C 1 119 ? -17.203 40.545  5.021   1.00 18.47 ? 107 VAL C CG1 1 
ATOM   3796 C  CG2 . VAL C 1 119 ? -19.035 40.680  3.285   1.00 21.01 ? 107 VAL C CG2 1 
ATOM   3797 N  N   . GLU C 1 120 ? -21.193 41.602  5.497   1.00 21.32 ? 108 GLU C N   1 
ATOM   3798 C  CA  . GLU C 1 120 ? -22.256 40.823  6.118   1.00 21.58 ? 108 GLU C CA  1 
ATOM   3799 C  C   . GLU C 1 120 ? -22.502 39.582  5.269   1.00 20.43 ? 108 GLU C C   1 
ATOM   3800 O  O   . GLU C 1 120 ? -22.812 39.692  4.079   1.00 23.21 ? 108 GLU C O   1 
ATOM   3801 C  CB  . GLU C 1 120 ? -23.533 41.654  6.262   1.00 31.25 ? 108 GLU C CB  1 
ATOM   3802 C  CG  . GLU C 1 120 ? -24.004 41.835  7.704   1.00 38.26 ? 108 GLU C CG  1 
ATOM   3803 C  CD  . GLU C 1 120 ? -24.827 40.654  8.208   1.00 42.80 ? 108 GLU C CD  1 
ATOM   3804 O  OE1 . GLU C 1 120 ? -25.100 40.586  9.427   1.00 49.53 ? 108 GLU C OE1 1 
ATOM   3805 O  OE2 . GLU C 1 120 ? -25.184 39.780  7.388   1.00 45.32 ? 108 GLU C OE2 1 
ATOM   3806 N  N   . THR C 1 121 ? -22.336 38.408  5.869   1.00 21.50 ? 109 THR C N   1 
ATOM   3807 C  CA  . THR C 1 121 ? -22.542 37.160  5.151   1.00 20.59 ? 109 THR C CA  1 
ATOM   3808 C  C   . THR C 1 121 ? -22.761 36.053  6.173   1.00 20.92 ? 109 THR C C   1 
ATOM   3809 O  O   . THR C 1 121 ? -22.256 36.118  7.298   1.00 20.03 ? 109 THR C O   1 
ATOM   3810 C  CB  . THR C 1 121 ? -21.360 36.857  4.202   1.00 23.60 ? 109 THR C CB  1 
ATOM   3811 O  OG1 . THR C 1 121 ? -21.548 35.587  3.562   1.00 22.89 ? 109 THR C OG1 1 
ATOM   3812 C  CG2 . THR C 1 121 ? -20.029 36.857  4.947   1.00 20.84 ? 109 THR C CG2 1 
ATOM   3813 N  N   . ASP C 1 122 ? -23.571 35.070  5.786   1.00 20.55 ? 110 ASP C N   1 
ATOM   3814 C  CA  . ASP C 1 122 ? -23.802 33.869  6.586   1.00 20.61 ? 110 ASP C CA  1 
ATOM   3815 C  C   . ASP C 1 122 ? -24.245 34.211  8.009   1.00 21.40 ? 110 ASP C C   1 
ATOM   3816 O  O   . ASP C 1 122 ? -23.728 33.689  9.003   1.00 20.68 ? 110 ASP C O   1 
ATOM   3817 C  CB  . ASP C 1 122 ? -22.556 32.988  6.557   1.00 19.34 ? 110 ASP C CB  1 
ATOM   3818 C  CG  . ASP C 1 122 ? -22.128 32.677  5.130   1.00 18.87 ? 110 ASP C CG  1 
ATOM   3819 O  OD1 . ASP C 1 122 ? -22.907 32.000  4.413   1.00 17.54 ? 110 ASP C OD1 1 
ATOM   3820 O  OD2 . ASP C 1 122 ? -21.047 33.136  4.709   1.00 19.10 ? 110 ASP C OD2 1 
ATOM   3821 N  N   . ASP C 1 123 ? -25.239 35.104  8.097   1.00 24.26 ? 111 ASP C N   1 
ATOM   3822 C  CA  . ASP C 1 123 ? -25.878 35.464  9.365   1.00 23.79 ? 111 ASP C CA  1 
ATOM   3823 C  C   . ASP C 1 123 ? -24.903 36.124  10.329  1.00 27.21 ? 111 ASP C C   1 
ATOM   3824 O  O   . ASP C 1 123 ? -25.091 36.077  11.548  1.00 30.43 ? 111 ASP C O   1 
ATOM   3825 C  CB  . ASP C 1 123 ? -26.526 34.245  10.027  1.00 28.92 ? 111 ASP C CB  1 
ATOM   3826 C  CG  . ASP C 1 123 ? -27.557 33.583  9.138   1.00 36.20 ? 111 ASP C CG  1 
ATOM   3827 O  OD1 . ASP C 1 123 ? -28.438 34.310  8.628   1.00 36.41 ? 111 ASP C OD1 1 
ATOM   3828 O  OD2 . ASP C 1 123 ? -27.484 32.349  8.942   1.00 37.52 ? 111 ASP C OD2 1 
ATOM   3829 N  N   . GLY C 1 124 ? -23.852 36.744  9.798   1.00 22.72 ? 112 GLY C N   1 
ATOM   3830 C  CA  . GLY C 1 124 ? -22.862 37.364  10.652  1.00 24.76 ? 112 GLY C CA  1 
ATOM   3831 C  C   . GLY C 1 124 ? -22.286 38.609  10.016  1.00 22.82 ? 112 GLY C C   1 
ATOM   3832 O  O   . GLY C 1 124 ? -22.531 38.916  8.846   1.00 26.50 ? 112 GLY C O   1 
ATOM   3833 N  N   . THR C 1 125 ? -21.517 39.331  10.824  1.00 22.39 ? 113 THR C N   1 
ATOM   3834 C  CA  . THR C 1 125 ? -20.756 40.491  10.390  1.00 21.53 ? 113 THR C CA  1 
ATOM   3835 C  C   . THR C 1 125 ? -19.281 40.189  10.591  1.00 17.06 ? 113 THR C C   1 
ATOM   3836 O  O   . THR C 1 125 ? -18.888 39.693  11.652  1.00 18.50 ? 113 THR C O   1 
ATOM   3837 C  CB  . THR C 1 125 ? -21.163 41.736  11.176  1.00 25.18 ? 113 THR C CB  1 
ATOM   3838 O  OG1 . THR C 1 125 ? -22.530 42.042  10.873  1.00 27.21 ? 113 THR C OG1 1 
ATOM   3839 C  CG2 . THR C 1 125 ? -20.274 42.925  10.819  1.00 22.34 ? 113 THR C CG2 1 
ATOM   3840 N  N   . TYR C 1 126 ? -18.477 40.468  9.568   1.00 15.29 ? 114 TYR C N   1 
ATOM   3841 C  CA  . TYR C 1 126 ? -17.042 40.210  9.599   1.00 16.34 ? 114 TYR C CA  1 
ATOM   3842 C  C   . TYR C 1 126 ? -16.294 41.516  9.397   1.00 16.51 ? 114 TYR C C   1 
ATOM   3843 O  O   . TYR C 1 126 ? -16.629 42.290  8.500   1.00 19.18 ? 114 TYR C O   1 
ATOM   3844 C  CB  . TYR C 1 126 ? -16.622 39.223  8.504   1.00 16.37 ? 114 TYR C CB  1 
ATOM   3845 C  CG  . TYR C 1 126 ? -17.153 37.822  8.660   1.00 15.62 ? 114 TYR C CG  1 
ATOM   3846 C  CD1 . TYR C 1 126 ? -18.482 37.522  8.371   1.00 14.77 ? 114 TYR C CD1 1 
ATOM   3847 C  CD2 . TYR C 1 126 ? -16.318 36.789  9.069   1.00 14.47 ? 114 TYR C CD2 1 
ATOM   3848 C  CE1 . TYR C 1 126 ? -18.970 36.233  8.503   1.00 16.99 ? 114 TYR C CE1 1 
ATOM   3849 C  CE2 . TYR C 1 126 ? -16.800 35.491  9.202   1.00 14.52 ? 114 TYR C CE2 1 
ATOM   3850 C  CZ  . TYR C 1 126 ? -18.118 35.220  8.924   1.00 16.33 ? 114 TYR C CZ  1 
ATOM   3851 O  OH  . TYR C 1 126 ? -18.602 33.933  9.048   1.00 15.49 ? 114 TYR C OH  1 
ATOM   3852 N  N   . LYS C 1 127 ? -15.291 41.764  10.226  1.00 15.76 ? 115 LYS C N   1 
ATOM   3853 C  CA  . LYS C 1 127 ? -14.381 42.873  9.995   1.00 15.88 ? 115 LYS C CA  1 
ATOM   3854 C  C   . LYS C 1 127 ? -13.238 42.423  9.093   1.00 16.08 ? 115 LYS C C   1 
ATOM   3855 O  O   . LYS C 1 127 ? -12.670 41.344  9.289   1.00 15.50 ? 115 LYS C O   1 
ATOM   3856 C  CB  . LYS C 1 127 ? -13.841 43.404  11.322  1.00 20.79 ? 115 LYS C CB  1 
ATOM   3857 C  CG  . LYS C 1 127 ? -14.921 44.028  12.195  1.00 21.99 ? 115 LYS C CG  1 
ATOM   3858 C  CD  . LYS C 1 127 ? -14.350 44.522  13.510  1.00 24.67 ? 115 LYS C CD  1 
ATOM   3859 C  CE  . LYS C 1 127 ? -15.439 45.147  14.366  1.00 28.82 ? 115 LYS C CE  1 
ATOM   3860 N  NZ  . LYS C 1 127 ? -14.901 45.660  15.664  1.00 29.41 ? 115 LYS C NZ  1 
ATOM   3861 N  N   . ILE C 1 128 ? -12.894 43.273  8.108   1.00 14.31 ? 116 ILE C N   1 
ATOM   3862 C  CA  . ILE C 1 128 ? -11.904 42.970  7.078   1.00 14.06 ? 116 ILE C CA  1 
ATOM   3863 C  C   . ILE C 1 128 ? -10.609 43.699  7.404   1.00 14.27 ? 116 ILE C C   1 
ATOM   3864 O  O   . ILE C 1 128 ? -10.634 44.890  7.741   1.00 17.03 ? 116 ILE C O   1 
ATOM   3865 C  CB  . ILE C 1 128 ? -12.420 43.388  5.686   1.00 15.98 ? 116 ILE C CB  1 
ATOM   3866 C  CG1 . ILE C 1 128 ? -13.671 42.598  5.298   1.00 22.31 ? 116 ILE C CG1 1 
ATOM   3867 C  CG2 . ILE C 1 128 ? -11.334 43.241  4.642   1.00 25.55 ? 116 ILE C CG2 1 
ATOM   3868 C  CD1 . ILE C 1 128 ? -13.656 41.186  5.732   1.00 23.99 ? 116 ILE C CD1 1 
ATOM   3869 N  N   . TYR C 1 129 ? -9.474  43.006  7.252   1.00 14.60 ? 117 TYR C N   1 
ATOM   3870 C  CA  . TYR C 1 129 ? -8.156  43.564  7.526   1.00 15.31 ? 117 TYR C CA  1 
ATOM   3871 C  C   . TYR C 1 129 ? -7.156  43.135  6.458   1.00 17.34 ? 117 TYR C C   1 
ATOM   3872 O  O   . TYR C 1 129 ? -7.329  42.123  5.778   1.00 14.23 ? 117 TYR C O   1 
ATOM   3873 C  CB  . TYR C 1 129 ? -7.588  43.119  8.888   1.00 12.77 ? 117 TYR C CB  1 
ATOM   3874 C  CG  . TYR C 1 129 ? -8.491  43.325  10.088  1.00 15.44 ? 117 TYR C CG  1 
ATOM   3875 C  CD1 . TYR C 1 129 ? -9.548  42.457  10.340  1.00 15.99 ? 117 TYR C CD1 1 
ATOM   3876 C  CD2 . TYR C 1 129 ? -8.265  44.361  10.993  1.00 16.57 ? 117 TYR C CD2 1 
ATOM   3877 C  CE1 . TYR C 1 129 ? -10.369 42.626  11.433  1.00 16.58 ? 117 TYR C CE1 1 
ATOM   3878 C  CE2 . TYR C 1 129 ? -9.083  44.532  12.101  1.00 17.14 ? 117 TYR C CE2 1 
ATOM   3879 C  CZ  . TYR C 1 129 ? -10.139 43.658  12.310  1.00 17.62 ? 117 TYR C CZ  1 
ATOM   3880 O  OH  . TYR C 1 129 ? -10.982 43.792  13.395  1.00 17.95 ? 117 TYR C OH  1 
ATOM   3881 N  N   . GLN C 1 130 ? -6.059  43.889  6.364   1.00 15.35 ? 118 GLN C N   1 
ATOM   3882 C  CA  . GLN C 1 130 ? -4.933  43.512  5.523   1.00 17.84 ? 118 GLN C CA  1 
ATOM   3883 C  C   . GLN C 1 130 ? -3.618  43.792  6.245   1.00 16.68 ? 118 GLN C C   1 
ATOM   3884 O  O   . GLN C 1 130 ? -3.495  44.799  6.951   1.00 20.28 ? 118 GLN C O   1 
ATOM   3885 C  CB  . GLN C 1 130 ? -4.998  44.274  4.183   1.00 20.57 ? 118 GLN C CB  1 
ATOM   3886 C  CG  . GLN C 1 130 ? -3.736  44.181  3.351   1.00 27.33 ? 118 GLN C CG  1 
ATOM   3887 C  CD  . GLN C 1 130 ? -2.745  45.293  3.665   1.00 29.35 ? 118 GLN C CD  1 
ATOM   3888 O  OE1 . GLN C 1 130 ? -3.129  46.393  4.066   1.00 31.20 ? 118 GLN C OE1 1 
ATOM   3889 N  NE2 . GLN C 1 130 ? -1.467  45.008  3.478   1.00 30.87 ? 118 GLN C NE2 1 
ATOM   3890 N  N   . THR C 1 131 ? -2.646  42.886  6.090   1.00 16.09 ? 119 THR C N   1 
ATOM   3891 C  CA  . THR C 1 131 ? -1.253  43.125  6.492   1.00 18.50 ? 119 THR C CA  1 
ATOM   3892 C  C   . THR C 1 131 ? -0.318  42.512  5.467   1.00 20.41 ? 119 THR C C   1 
ATOM   3893 O  O   . THR C 1 131 ? -0.730  42.001  4.424   1.00 17.32 ? 119 THR C O   1 
ATOM   3894 C  CB  . THR C 1 131 ? -0.816  42.529  7.844   1.00 25.52 ? 119 THR C CB  1 
ATOM   3895 O  OG1 . THR C 1 131 ? -1.442  41.262  8.098   1.00 28.35 ? 119 THR C OG1 1 
ATOM   3896 C  CG2 . THR C 1 131 ? -0.941  43.504  8.977   1.00 32.80 ? 119 THR C CG2 1 
ATOM   3897 N  N   . THR C 1 132 ? 0.963   42.535  5.814   1.00 20.69 ? 120 THR C N   1 
ATOM   3898 C  CA  . THR C 1 132 ? 2.007   41.883  5.048   1.00 26.51 ? 120 THR C CA  1 
ATOM   3899 C  C   . THR C 1 132 ? 2.790   40.984  5.985   1.00 21.27 ? 120 THR C C   1 
ATOM   3900 O  O   . THR C 1 132 ? 2.894   41.249  7.187   1.00 26.30 ? 120 THR C O   1 
ATOM   3901 C  CB  . THR C 1 132 ? 2.963   42.887  4.397   1.00 27.46 ? 120 THR C CB  1 
ATOM   3902 O  OG1 . THR C 1 132 ? 3.515   43.739  5.409   1.00 38.91 ? 120 THR C OG1 1 
ATOM   3903 C  CG2 . THR C 1 132 ? 2.236   43.732  3.360   1.00 25.28 ? 120 THR C CG2 1 
ATOM   3904 N  N   . ARG C 1 133 ? 3.324   39.907  5.429   1.00 21.38 ? 121 ARG C N   1 
ATOM   3905 C  CA  . ARG C 1 133 ? 4.247   39.035  6.135   1.00 19.58 ? 121 ARG C CA  1 
ATOM   3906 C  C   . ARG C 1 133 ? 5.563   39.072  5.379   1.00 24.67 ? 121 ARG C C   1 
ATOM   3907 O  O   . ARG C 1 133 ? 5.581   38.875  4.159   1.00 21.56 ? 121 ARG C O   1 
ATOM   3908 C  CB  . ARG C 1 133 ? 3.701   37.606  6.234   1.00 21.48 ? 121 ARG C CB  1 
ATOM   3909 C  CG  . ARG C 1 133 ? 2.397   37.503  7.033   1.00 21.75 ? 121 ARG C CG  1 
ATOM   3910 C  CD  . ARG C 1 133 ? 2.653   37.200  8.518   1.00 22.57 ? 121 ARG C CD  1 
ATOM   3911 N  NE  . ARG C 1 133 ? 3.186   35.852  8.707   1.00 24.64 ? 121 ARG C NE  1 
ATOM   3912 C  CZ  . ARG C 1 133 ? 4.326   35.572  9.332   1.00 28.62 ? 121 ARG C CZ  1 
ATOM   3913 N  NH1 . ARG C 1 133 ? 5.056   36.551  9.847   1.00 29.34 ? 121 ARG C NH1 1 
ATOM   3914 N  NH2 . ARG C 1 133 ? 4.731   34.310  9.447   1.00 27.36 ? 121 ARG C NH2 1 
ATOM   3915 N  N   . GLU C 1 134 ? 6.652   39.350  6.097   1.00 21.78 ? 122 GLU C N   1 
ATOM   3916 C  CA  . GLU C 1 134 ? 7.968   39.561  5.506   1.00 23.86 ? 122 GLU C CA  1 
ATOM   3917 C  C   . GLU C 1 134 ? 8.863   38.369  5.811   1.00 23.83 ? 122 GLU C C   1 
ATOM   3918 O  O   . GLU C 1 134 ? 8.968   37.951  6.968   1.00 23.90 ? 122 GLU C O   1 
ATOM   3919 C  CB  . GLU C 1 134 ? 8.605   40.845  6.047   1.00 30.89 ? 122 GLU C CB  1 
ATOM   3920 C  CG  . GLU C 1 134 ? 8.047   42.126  5.441   1.00 34.55 ? 122 GLU C CG  1 
ATOM   3921 C  CD  . GLU C 1 134 ? 8.573   43.374  6.135   1.00 45.04 ? 122 GLU C CD  1 
ATOM   3922 O  OE1 . GLU C 1 134 ? 9.807   43.570  6.156   1.00 49.16 ? 122 GLU C OE1 1 
ATOM   3923 O  OE2 . GLU C 1 134 ? 7.753   44.158  6.659   1.00 51.25 ? 122 GLU C OE2 1 
ATOM   3924 N  N   . ASN C 1 135 ? 9.496   37.822  4.773   1.00 22.47 ? 123 ASN C N   1 
ATOM   3925 C  CA  . ASN C 1 135 ? 10.446  36.721  4.913   1.00 21.71 ? 123 ASN C CA  1 
ATOM   3926 C  C   . ASN C 1 135 ? 9.885   35.622  5.812   1.00 24.29 ? 123 ASN C C   1 
ATOM   3927 O  O   . ASN C 1 135 ? 10.466  35.249  6.830   1.00 26.20 ? 123 ASN C O   1 
ATOM   3928 C  CB  . ASN C 1 135 ? 11.783  37.238  5.445   1.00 27.59 ? 123 ASN C CB  1 
ATOM   3929 C  CG  . ASN C 1 135 ? 12.336  38.368  4.607   1.00 26.98 ? 123 ASN C CG  1 
ATOM   3930 O  OD1 . ASN C 1 135 ? 12.658  38.180  3.440   1.00 27.77 ? 123 ASN C OD1 1 
ATOM   3931 N  ND2 . ASN C 1 135 ? 12.450  39.548  5.200   1.00 31.11 ? 123 ASN C ND2 1 
ATOM   3932 N  N   . ALA C 1 136 ? 8.718   35.128  5.425   1.00 19.10 ? 124 ALA C N   1 
ATOM   3933 C  CA  . ALA C 1 136 ? 7.918   34.238  6.243   1.00 22.02 ? 124 ALA C CA  1 
ATOM   3934 C  C   . ALA C 1 136 ? 7.717   32.910  5.531   1.00 20.50 ? 124 ALA C C   1 
ATOM   3935 O  O   . ALA C 1 136 ? 7.876   32.823  4.306   1.00 18.50 ? 124 ALA C O   1 
ATOM   3936 C  CB  . ALA C 1 136 ? 6.554   34.877  6.550   1.00 18.79 ? 124 ALA C CB  1 
ATOM   3937 N  N   . PRO C 1 137 ? 7.359   31.854  6.262   1.00 17.94 ? 125 PRO C N   1 
ATOM   3938 C  CA  . PRO C 1 137 ? 7.026   30.589  5.600   1.00 17.98 ? 125 PRO C CA  1 
ATOM   3939 C  C   . PRO C 1 137 ? 5.814   30.757  4.698   1.00 14.81 ? 125 PRO C C   1 
ATOM   3940 O  O   . PRO C 1 137 ? 4.894   31.526  4.992   1.00 17.61 ? 125 PRO C O   1 
ATOM   3941 C  CB  . PRO C 1 137 ? 6.729   29.639  6.767   1.00 22.99 ? 125 PRO C CB  1 
ATOM   3942 C  CG  . PRO C 1 137 ? 7.458   30.222  7.915   1.00 24.03 ? 125 PRO C CG  1 
ATOM   3943 C  CD  . PRO C 1 137 ? 7.382   31.711  7.728   1.00 25.38 ? 125 PRO C CD  1 
ATOM   3944 N  N   . SER C 1 138 ? 5.819   30.013  3.598   1.00 18.94 ? 126 SER C N   1 
ATOM   3945 C  CA  . SER C 1 138 ? 4.779   30.124  2.587   1.00 16.62 ? 126 SER C CA  1 
ATOM   3946 C  C   . SER C 1 138 ? 4.755   28.842  1.764   1.00 16.26 ? 126 SER C C   1 
ATOM   3947 O  O   . SER C 1 138 ? 5.681   28.024  1.816   1.00 17.49 ? 126 SER C O   1 
ATOM   3948 C  CB  . SER C 1 138 ? 5.022   31.362  1.704   1.00 20.00 ? 126 SER C CB  1 
ATOM   3949 O  OG  . SER C 1 138 ? 5.789   31.016  0.567   1.00 16.79 ? 126 SER C OG  1 
ATOM   3950 N  N   . ILE C 1 139 ? 3.683   28.682  0.980   1.00 16.43 ? 127 ILE C N   1 
ATOM   3951 C  CA  . ILE C 1 139 ? 3.590   27.539  0.082   1.00 20.55 ? 127 ILE C CA  1 
ATOM   3952 C  C   . ILE C 1 139 ? 4.657   27.571  -1.002  1.00 20.37 ? 127 ILE C C   1 
ATOM   3953 O  O   . ILE C 1 139 ? 4.811   26.592  -1.741  1.00 21.70 ? 127 ILE C O   1 
ATOM   3954 C  CB  . ILE C 1 139 ? 2.187   27.445  -0.563  1.00 18.08 ? 127 ILE C CB  1 
ATOM   3955 C  CG1 . ILE C 1 139 ? 1.820   28.745  -1.285  1.00 16.24 ? 127 ILE C CG1 1 
ATOM   3956 C  CG2 . ILE C 1 139 ? 1.151   27.068  0.496   1.00 17.79 ? 127 ILE C CG2 1 
ATOM   3957 C  CD1 . ILE C 1 139 ? 0.706   28.556  -2.313  1.00 16.56 ? 127 ILE C CD1 1 
ATOM   3958 N  N   . GLU C 1 140 ? 5.395   28.672  -1.125  1.00 19.57 ? 128 GLU C N   1 
ATOM   3959 C  CA  . GLU C 1 140 ? 6.483   28.751  -2.090  1.00 19.59 ? 128 GLU C CA  1 
ATOM   3960 C  C   . GLU C 1 140 ? 7.856   28.784  -1.429  1.00 20.68 ? 128 GLU C C   1 
ATOM   3961 O  O   . GLU C 1 140 ? 8.860   28.943  -2.129  1.00 24.16 ? 128 GLU C O   1 
ATOM   3962 C  CB  . GLU C 1 140 ? 6.303   29.970  -3.010  1.00 19.66 ? 128 GLU C CB  1 
ATOM   3963 C  CG  . GLU C 1 140 ? 5.066   29.907  -3.930  1.00 21.60 ? 128 GLU C CG  1 
ATOM   3964 C  CD  . GLU C 1 140 ? 5.162   28.824  -5.015  1.00 28.73 ? 128 GLU C CD  1 
ATOM   3965 O  OE1 . GLU C 1 140 ? 4.351   28.856  -5.966  1.00 28.62 ? 128 GLU C OE1 1 
ATOM   3966 O  OE2 . GLU C 1 140 ? 6.043   27.939  -4.933  1.00 32.11 ? 128 GLU C OE2 1 
ATOM   3967 N  N   . GLY C 1 141 ? 7.930   28.606  -0.112  1.00 18.57 ? 129 GLY C N   1 
ATOM   3968 C  CA  . GLY C 1 141 ? 9.166   28.800  0.620   1.00 20.75 ? 129 GLY C CA  1 
ATOM   3969 C  C   . GLY C 1 141 ? 9.169   30.150  1.304   1.00 18.18 ? 129 GLY C C   1 
ATOM   3970 O  O   . GLY C 1 141 ? 8.158   30.851  1.372   1.00 18.76 ? 129 GLY C O   1 
ATOM   3971 N  N   . THR C 1 142 ? 10.335  30.529  1.815   1.00 18.80 ? 130 THR C N   1 
ATOM   3972 C  CA  . THR C 1 142 ? 10.438  31.822  2.479   1.00 15.60 ? 130 THR C CA  1 
ATOM   3973 C  C   . THR C 1 142 ? 10.073  32.938  1.513   1.00 16.20 ? 130 THR C C   1 
ATOM   3974 O  O   . THR C 1 142 ? 10.646  33.043  0.426   1.00 19.80 ? 130 THR C O   1 
ATOM   3975 C  CB  . THR C 1 142 ? 11.850  32.033  3.013   1.00 21.03 ? 130 THR C CB  1 
ATOM   3976 O  OG1 . THR C 1 142 ? 12.191  30.935  3.861   1.00 21.33 ? 130 THR C OG1 1 
ATOM   3977 C  CG2 . THR C 1 142 ? 11.925  33.325  3.808   1.00 19.47 ? 130 THR C CG2 1 
ATOM   3978 N  N   . ALA C 1 143 ? 9.121   33.780  1.905   1.00 14.59 ? 131 ALA C N   1 
ATOM   3979 C  CA  . ALA C 1 143 ? 8.633   34.779  0.967   1.00 17.76 ? 131 ALA C CA  1 
ATOM   3980 C  C   . ALA C 1 143 ? 7.977   35.931  1.709   1.00 19.78 ? 131 ALA C C   1 
ATOM   3981 O  O   . ALA C 1 143 ? 7.695   35.860  2.908   1.00 21.06 ? 131 ALA C O   1 
ATOM   3982 C  CB  . ALA C 1 143 ? 7.651   34.163  -0.040  1.00 17.96 ? 131 ALA C CB  1 
ATOM   3983 N  N   . THR C 1 144 ? 7.742   37.004  0.964   1.00 16.52 ? 132 THR C N   1 
ATOM   3984 C  CA  . THR C 1 144 ? 6.994   38.158  1.432   1.00 15.99 ? 132 THR C CA  1 
ATOM   3985 C  C   . THR C 1 144 ? 5.675   38.205  0.674   1.00 18.73 ? 132 THR C C   1 
ATOM   3986 O  O   . THR C 1 144 ? 5.664   38.111  -0.558  1.00 21.02 ? 132 THR C O   1 
ATOM   3987 C  CB  . THR C 1 144 ? 7.797   39.448  1.219   1.00 23.01 ? 132 THR C CB  1 
ATOM   3988 O  OG1 . THR C 1 144 ? 8.923   39.446  2.101   1.00 23.16 ? 132 THR C OG1 1 
ATOM   3989 C  CG2 . THR C 1 144 ? 6.940   40.691  1.488   1.00 24.21 ? 132 THR C CG2 1 
ATOM   3990 N  N   . PHE C 1 145 ? 4.568   38.325  1.403   1.00 18.35 ? 133 PHE C N   1 
ATOM   3991 C  CA  . PHE C 1 145 ? 3.254   38.196  0.785   1.00 16.78 ? 133 PHE C CA  1 
ATOM   3992 C  C   . PHE C 1 145 ? 2.238   39.009  1.572   1.00 18.28 ? 133 PHE C C   1 
ATOM   3993 O  O   . PHE C 1 145 ? 2.455   39.351  2.736   1.00 17.36 ? 133 PHE C O   1 
ATOM   3994 C  CB  . PHE C 1 145 ? 2.809   36.729  0.701   1.00 15.57 ? 133 PHE C CB  1 
ATOM   3995 C  CG  . PHE C 1 145 ? 2.975   35.948  1.994   1.00 18.20 ? 133 PHE C CG  1 
ATOM   3996 C  CD1 . PHE C 1 145 ? 4.170   35.302  2.281   1.00 16.83 ? 133 PHE C CD1 1 
ATOM   3997 C  CD2 . PHE C 1 145 ? 1.931   35.837  2.899   1.00 19.25 ? 133 PHE C CD2 1 
ATOM   3998 C  CE1 . PHE C 1 145 ? 4.326   34.577  3.457   1.00 19.13 ? 133 PHE C CE1 1 
ATOM   3999 C  CE2 . PHE C 1 145 ? 2.080   35.116  4.080   1.00 17.72 ? 133 PHE C CE2 1 
ATOM   4000 C  CZ  . PHE C 1 145 ? 3.277   34.481  4.356   1.00 16.63 ? 133 PHE C CZ  1 
ATOM   4001 N  N   . ASN C 1 146 ? 1.125   39.322  0.915   1.00 15.67 ? 134 ASN C N   1 
ATOM   4002 C  CA  . ASN C 1 146 ? 0.014   39.967  1.593   1.00 15.54 ? 134 ASN C CA  1 
ATOM   4003 C  C   . ASN C 1 146 ? -0.804  38.935  2.360   1.00 14.38 ? 134 ASN C C   1 
ATOM   4004 O  O   . ASN C 1 146 ? -0.849  37.757  2.005   1.00 14.53 ? 134 ASN C O   1 
ATOM   4005 C  CB  . ASN C 1 146 ? -0.875  40.708  0.596   1.00 17.57 ? 134 ASN C CB  1 
ATOM   4006 C  CG  . ASN C 1 146 ? -0.185  41.928  0.011   1.00 27.07 ? 134 ASN C CG  1 
ATOM   4007 O  OD1 . ASN C 1 146 ? 0.803   42.415  0.564   1.00 29.79 ? 134 ASN C OD1 1 
ATOM   4008 N  ND2 . ASN C 1 146 ? -0.695  42.421  -1.113  1.00 32.83 ? 134 ASN C ND2 1 
ATOM   4009 N  N   . GLN C 1 147 ? -1.428  39.388  3.443   1.00 14.37 ? 135 GLN C N   1 
ATOM   4010 C  CA  . GLN C 1 147 ? -2.241  38.534  4.304   1.00 13.03 ? 135 GLN C CA  1 
ATOM   4011 C  C   . GLN C 1 147 ? -3.564  39.246  4.542   1.00 14.53 ? 135 GLN C C   1 
ATOM   4012 O  O   . GLN C 1 147 ? -3.575  40.383  5.019   1.00 16.82 ? 135 GLN C O   1 
ATOM   4013 C  CB  . GLN C 1 147 ? -1.507  38.255  5.619   1.00 14.90 ? 135 GLN C CB  1 
ATOM   4014 C  CG  . GLN C 1 147 ? -2.119  37.217  6.524   1.00 13.18 ? 135 GLN C CG  1 
ATOM   4015 C  CD  . GLN C 1 147 ? -1.384  37.137  7.858   1.00 16.85 ? 135 GLN C CD  1 
ATOM   4016 O  OE1 . GLN C 1 147 ? -1.380  38.098  8.634   1.00 19.91 ? 135 GLN C OE1 1 
ATOM   4017 N  NE2 . GLN C 1 147 ? -0.753  35.995  8.123   1.00 16.91 ? 135 GLN C NE2 1 
ATOM   4018 N  N   . TYR C 1 148 ? -4.675  38.598  4.193   1.00 12.82 ? 136 TYR C N   1 
ATOM   4019 C  CA  . TYR C 1 148 ? -5.998  39.200  4.306   1.00 11.41 ? 136 TYR C CA  1 
ATOM   4020 C  C   . TYR C 1 148 ? -6.792  38.487  5.392   1.00 14.18 ? 136 TYR C C   1 
ATOM   4021 O  O   . TYR C 1 148 ? -6.670  37.270  5.551   1.00 14.48 ? 136 TYR C O   1 
ATOM   4022 C  CB  . TYR C 1 148 ? -6.777  39.119  2.988   1.00 12.06 ? 136 TYR C CB  1 
ATOM   4023 C  CG  . TYR C 1 148 ? -6.088  39.744  1.792   1.00 14.50 ? 136 TYR C CG  1 
ATOM   4024 C  CD1 . TYR C 1 148 ? -5.081  40.690  1.956   1.00 18.23 ? 136 TYR C CD1 1 
ATOM   4025 C  CD2 . TYR C 1 148 ? -6.456  39.390  0.498   1.00 16.00 ? 136 TYR C CD2 1 
ATOM   4026 C  CE1 . TYR C 1 148 ? -4.455  41.261  0.874   1.00 16.59 ? 136 TYR C CE1 1 
ATOM   4027 C  CE2 . TYR C 1 148 ? -5.822  39.952  -0.603  1.00 19.29 ? 136 TYR C CE2 1 
ATOM   4028 C  CZ  . TYR C 1 148 ? -4.824  40.888  -0.402  1.00 16.53 ? 136 TYR C CZ  1 
ATOM   4029 O  OH  . TYR C 1 148 ? -4.180  41.468  -1.465  1.00 19.54 ? 136 TYR C OH  1 
ATOM   4030 N  N   . TRP C 1 149 ? -7.622  39.247  6.113   1.00 12.90 ? 137 TRP C N   1 
ATOM   4031 C  CA  . TRP C 1 149 ? -8.416  38.744  7.226   1.00 12.82 ? 137 TRP C CA  1 
ATOM   4032 C  C   . TRP C 1 149 ? -9.870  39.168  7.110   1.00 13.96 ? 137 TRP C C   1 
ATOM   4033 O  O   . TRP C 1 149 ? -10.183 40.314  6.762   1.00 13.39 ? 137 TRP C O   1 
ATOM   4034 C  CB  . TRP C 1 149 ? -7.893  39.248  8.582   1.00 11.84 ? 137 TRP C CB  1 
ATOM   4035 C  CG  . TRP C 1 149 ? -6.498  38.837  8.899   1.00 11.59 ? 137 TRP C CG  1 
ATOM   4036 C  CD1 . TRP C 1 149 ? -5.352  39.470  8.526   1.00 14.17 ? 137 TRP C CD1 1 
ATOM   4037 C  CD2 . TRP C 1 149 ? -6.097  37.699  9.675   1.00 12.96 ? 137 TRP C CD2 1 
ATOM   4038 N  NE1 . TRP C 1 149 ? -4.257  38.802  9.021   1.00 15.01 ? 137 TRP C NE1 1 
ATOM   4039 C  CE2 . TRP C 1 149 ? -4.686  37.705  9.724   1.00 15.04 ? 137 TRP C CE2 1 
ATOM   4040 C  CE3 . TRP C 1 149 ? -6.792  36.677  10.334  1.00 12.24 ? 137 TRP C CE3 1 
ATOM   4041 C  CZ2 . TRP C 1 149 ? -3.953  36.724  10.396  1.00 15.20 ? 137 TRP C CZ2 1 
ATOM   4042 C  CZ3 . TRP C 1 149 ? -6.058  35.699  10.998  1.00 12.07 ? 137 TRP C CZ3 1 
ATOM   4043 C  CH2 . TRP C 1 149 ? -4.654  35.732  11.025  1.00 15.40 ? 137 TRP C CH2 1 
ATOM   4044 N  N   . SER C 1 150 ? -10.747 38.235  7.453   1.00 12.56 ? 138 SER C N   1 
ATOM   4045 C  CA  . SER C 1 150 ? -12.158 38.483  7.692   1.00 11.84 ? 138 SER C CA  1 
ATOM   4046 C  C   . SER C 1 150 ? -12.471 37.836  9.033   1.00 12.52 ? 138 SER C C   1 
ATOM   4047 O  O   . SER C 1 150 ? -12.280 36.630  9.182   1.00 15.85 ? 138 SER C O   1 
ATOM   4048 C  CB  . SER C 1 150 ? -12.989 37.874  6.555   1.00 13.96 ? 138 SER C CB  1 
ATOM   4049 O  OG  . SER C 1 150 ? -14.317 38.326  6.567   1.00 24.66 ? 138 SER C OG  1 
ATOM   4050 N  N   . VAL C 1 151 ? -12.891 38.623  10.032  1.00 12.04 ? 139 VAL C N   1 
ATOM   4051 C  CA  . VAL C 1 151 ? -13.016 38.122  11.404  1.00 11.67 ? 139 VAL C CA  1 
ATOM   4052 C  C   . VAL C 1 151 ? -14.459 38.301  11.877  1.00 14.98 ? 139 VAL C C   1 
ATOM   4053 O  O   . VAL C 1 151 ? -14.939 39.431  12.011  1.00 15.33 ? 139 VAL C O   1 
ATOM   4054 C  CB  . VAL C 1 151 ? -12.027 38.819  12.357  1.00 12.17 ? 139 VAL C CB  1 
ATOM   4055 C  CG1 . VAL C 1 151 ? -12.180 38.288  13.773  1.00 13.20 ? 139 VAL C CG1 1 
ATOM   4056 C  CG2 . VAL C 1 151 ? -10.578 38.643  11.858  1.00 15.10 ? 139 VAL C CG2 1 
ATOM   4057 N  N   . ARG C 1 152 ? -15.146 37.186  12.130  1.00 13.52 ? 140 ARG C N   1 
ATOM   4058 C  CA  . ARG C 1 152 ? -16.551 37.245  12.536  1.00 14.98 ? 140 ARG C CA  1 
ATOM   4059 C  C   . ARG C 1 152 ? -16.706 37.953  13.881  1.00 15.89 ? 140 ARG C C   1 
ATOM   4060 O  O   . ARG C 1 152 ? -15.972 37.681  14.831  1.00 18.22 ? 140 ARG C O   1 
ATOM   4061 C  CB  . ARG C 1 152 ? -17.130 35.828  12.629  1.00 14.94 ? 140 ARG C CB  1 
ATOM   4062 C  CG  . ARG C 1 152 ? -18.637 35.770  12.524  1.00 13.39 ? 140 ARG C CG  1 
ATOM   4063 C  CD  . ARG C 1 152 ? -19.125 34.333  12.493  1.00 15.06 ? 140 ARG C CD  1 
ATOM   4064 N  NE  . ARG C 1 152 ? -20.573 34.264  12.673  1.00 15.84 ? 140 ARG C NE  1 
ATOM   4065 C  CZ  . ARG C 1 152 ? -21.452 34.125  11.690  1.00 20.96 ? 140 ARG C CZ  1 
ATOM   4066 N  NH1 . ARG C 1 152 ? -21.047 34.037  10.429  1.00 20.22 ? 140 ARG C NH1 1 
ATOM   4067 N  NH2 . ARG C 1 152 ? -22.747 34.075  11.973  1.00 19.87 ? 140 ARG C NH2 1 
ATOM   4068 N  N   . THR C 1 153 ? -17.705 38.837  13.981  1.00 13.98 ? 141 THR C N   1 
ATOM   4069 C  CA  . THR C 1 153 ? -17.870 39.595  15.220  1.00 19.02 ? 141 THR C CA  1 
ATOM   4070 C  C   . THR C 1 153 ? -18.472 38.740  16.331  1.00 19.76 ? 141 THR C C   1 
ATOM   4071 O  O   . THR C 1 153 ? -18.088 38.884  17.497  1.00 23.28 ? 141 THR C O   1 
ATOM   4072 C  CB  . THR C 1 153 ? -18.726 40.841  14.981  1.00 17.45 ? 141 THR C CB  1 
ATOM   4073 O  OG1 . THR C 1 153 ? -19.978 40.456  14.402  1.00 29.31 ? 141 THR C OG1 1 
ATOM   4074 C  CG2 . THR C 1 153 ? -18.010 41.793  14.049  1.00 17.12 ? 141 THR C CG2 1 
ATOM   4075 N  N   . ASP C 1 154 ? -19.427 37.865  16.001  1.00 20.70 ? 142 ASP C N   1 
ATOM   4076 C  CA  . ASP C 1 154 ? -20.000 36.912  16.955  1.00 23.04 ? 142 ASP C CA  1 
ATOM   4077 C  C   . ASP C 1 154 ? -19.514 35.518  16.579  1.00 19.60 ? 142 ASP C C   1 
ATOM   4078 O  O   . ASP C 1 154 ? -19.923 34.967  15.550  1.00 21.08 ? 142 ASP C O   1 
ATOM   4079 C  CB  . ASP C 1 154 ? -21.527 36.954  16.969  1.00 31.16 ? 142 ASP C CB  1 
ATOM   4080 C  CG  . ASP C 1 154 ? -22.084 38.365  17.107  1.00 40.18 ? 142 ASP C CG  1 
ATOM   4081 O  OD1 . ASP C 1 154 ? -21.637 39.104  18.011  1.00 42.26 ? 142 ASP C OD1 1 
ATOM   4082 O  OD2 . ASP C 1 154 ? -22.993 38.720  16.317  1.00 43.54 ? 142 ASP C OD2 1 
ATOM   4083 N  N   . HIS C 1 155 ? -18.674 34.942  17.431  1.00 20.64 ? 143 HIS C N   1 
ATOM   4084 C  CA  . HIS C 1 155 ? -17.960 33.715  17.104  1.00 18.79 ? 143 HIS C CA  1 
ATOM   4085 C  C   . HIS C 1 155 ? -18.901 32.517  17.037  1.00 19.59 ? 143 HIS C C   1 
ATOM   4086 O  O   . HIS C 1 155 ? -19.902 32.435  17.753  1.00 17.40 ? 143 HIS C O   1 
ATOM   4087 C  CB  . HIS C 1 155 ? -16.871 33.480  18.139  1.00 17.90 ? 143 HIS C CB  1 
ATOM   4088 C  CG  . HIS C 1 155 ? -15.864 34.590  18.202  1.00 20.99 ? 143 HIS C CG  1 
ATOM   4089 N  ND1 . HIS C 1 155 ? -14.759 34.554  19.020  1.00 20.15 ? 143 HIS C ND1 1 
ATOM   4090 C  CD2 . HIS C 1 155 ? -15.791 35.763  17.525  1.00 21.05 ? 143 HIS C CD2 1 
ATOM   4091 C  CE1 . HIS C 1 155 ? -14.052 35.659  18.855  1.00 20.30 ? 143 HIS C CE1 1 
ATOM   4092 N  NE2 . HIS C 1 155 ? -14.661 36.412  17.957  1.00 22.81 ? 143 HIS C NE2 1 
ATOM   4093 N  N   . ARG C 1 156 ? -18.574 31.581  16.155  1.00 16.62 ? 144 ARG C N   1 
ATOM   4094 C  CA  . ARG C 1 156 ? -19.316 30.336  16.085  1.00 15.77 ? 144 ARG C CA  1 
ATOM   4095 C  C   . ARG C 1 156 ? -18.369 29.210  15.709  1.00 16.41 ? 144 ARG C C   1 
ATOM   4096 O  O   . ARG C 1 156 ? -17.258 29.439  15.222  1.00 16.74 ? 144 ARG C O   1 
ATOM   4097 C  CB  . ARG C 1 156 ? -20.460 30.418  15.079  1.00 18.30 ? 144 ARG C CB  1 
ATOM   4098 C  CG  . ARG C 1 156 ? -19.957 30.619  13.687  1.00 18.83 ? 144 ARG C CG  1 
ATOM   4099 C  CD  . ARG C 1 156 ? -21.072 30.758  12.687  1.00 19.28 ? 144 ARG C CD  1 
ATOM   4100 N  NE  . ARG C 1 156 ? -20.511 30.760  11.344  1.00 19.57 ? 144 ARG C NE  1 
ATOM   4101 C  CZ  . ARG C 1 156 ? -21.225 30.658  10.234  1.00 21.54 ? 144 ARG C CZ  1 
ATOM   4102 N  NH1 . ARG C 1 156 ? -22.547 30.549  10.300  1.00 21.28 ? 144 ARG C NH1 1 
ATOM   4103 N  NH2 . ARG C 1 156 ? -20.610 30.674  9.058   1.00 21.92 ? 144 ARG C NH2 1 
ATOM   4104 N  N   . VAL C 1 157 ? -18.828 27.985  15.955  1.00 16.16 ? 145 VAL C N   1 
ATOM   4105 C  CA  . VAL C 1 157 ? -18.125 26.765  15.574  1.00 14.71 ? 145 VAL C CA  1 
ATOM   4106 C  C   . VAL C 1 157 ? -19.100 25.947  14.737  1.00 20.86 ? 145 VAL C C   1 
ATOM   4107 O  O   . VAL C 1 157 ? -19.989 25.273  15.280  1.00 22.38 ? 145 VAL C O   1 
ATOM   4108 C  CB  . VAL C 1 157 ? -17.636 25.969  16.789  1.00 15.74 ? 145 VAL C CB  1 
ATOM   4109 C  CG1 . VAL C 1 157 ? -16.909 24.701  16.339  1.00 17.45 ? 145 VAL C CG1 1 
ATOM   4110 C  CG2 . VAL C 1 157 ? -16.736 26.836  17.672  1.00 18.14 ? 145 VAL C CG2 1 
ATOM   4111 N  N   . GLY C 1 158 ? -18.947 26.002  13.427  1.00 19.31 ? 146 GLY C N   1 
ATOM   4112 C  CA  . GLY C 1 158 ? -19.820 25.258  12.541  1.00 18.62 ? 146 GLY C CA  1 
ATOM   4113 C  C   . GLY C 1 158 ? -20.779 26.169  11.797  1.00 20.04 ? 146 GLY C C   1 
ATOM   4114 O  O   . GLY C 1 158 ? -21.253 27.186  12.319  1.00 24.81 ? 146 GLY C O   1 
ATOM   4115 N  N   . GLY C 1 159 ? -21.072 25.799  10.567  1.00 18.49 ? 147 GLY C N   1 
ATOM   4116 C  CA  . GLY C 1 159 ? -22.030 26.523  9.766   1.00 20.06 ? 147 GLY C CA  1 
ATOM   4117 C  C   . GLY C 1 159 ? -21.601 26.530  8.319   1.00 21.02 ? 147 GLY C C   1 
ATOM   4118 O  O   . GLY C 1 159 ? -20.827 25.681  7.875   1.00 18.47 ? 147 GLY C O   1 
ATOM   4119 N  N   . THR C 1 160 ? -22.118 27.506  7.584   1.00 17.12 ? 148 THR C N   1 
ATOM   4120 C  CA  . THR C 1 160 ? -21.807 27.666  6.176   1.00 16.24 ? 148 THR C CA  1 
ATOM   4121 C  C   . THR C 1 160 ? -21.028 28.957  5.983   1.00 17.87 ? 148 THR C C   1 
ATOM   4122 O  O   . THR C 1 160 ? -21.352 29.983  6.589   1.00 19.97 ? 148 THR C O   1 
ATOM   4123 C  CB  . THR C 1 160 ? -23.088 27.670  5.332   1.00 19.59 ? 148 THR C CB  1 
ATOM   4124 O  OG1 . THR C 1 160 ? -23.706 26.381  5.416   1.00 22.12 ? 148 THR C OG1 1 
ATOM   4125 C  CG2 . THR C 1 160 ? -22.769 27.962  3.884   1.00 21.13 ? 148 THR C CG2 1 
ATOM   4126 N  N   . VAL C 1 161 ? -19.973 28.890  5.179   1.00 14.90 ? 149 VAL C N   1 
ATOM   4127 C  CA  . VAL C 1 161 ? -19.142 30.045  4.863   1.00 14.27 ? 149 VAL C CA  1 
ATOM   4128 C  C   . VAL C 1 161 ? -19.203 30.237  3.356   1.00 13.91 ? 149 VAL C C   1 
ATOM   4129 O  O   . VAL C 1 161 ? -18.717 29.390  2.599   1.00 14.24 ? 149 VAL C O   1 
ATOM   4130 C  CB  . VAL C 1 161 ? -17.689 29.861  5.329   1.00 16.75 ? 149 VAL C CB  1 
ATOM   4131 C  CG1 . VAL C 1 161 ? -16.833 31.011  4.835   1.00 14.61 ? 149 VAL C CG1 1 
ATOM   4132 C  CG2 . VAL C 1 161 ? -17.617 29.733  6.845   1.00 16.86 ? 149 VAL C CG2 1 
ATOM   4133 N  N   . THR C 1 162 ? -19.797 31.343  2.916   1.00 14.34 ? 150 THR C N   1 
ATOM   4134 C  CA  . THR C 1 162 ? -19.904 31.634  1.485   1.00 14.64 ? 150 THR C CA  1 
ATOM   4135 C  C   . THR C 1 162 ? -18.644 32.399  1.110   1.00 15.03 ? 150 THR C C   1 
ATOM   4136 O  O   . THR C 1 162 ? -18.594 33.625  1.198   1.00 16.10 ? 150 THR C O   1 
ATOM   4137 C  CB  . THR C 1 162 ? -21.169 32.427  1.188   1.00 20.52 ? 150 THR C CB  1 
ATOM   4138 O  OG1 . THR C 1 162 ? -22.303 31.710  1.700   1.00 19.29 ? 150 THR C OG1 1 
ATOM   4139 C  CG2 . THR C 1 162 ? -21.335 32.639  -0.320  1.00 20.22 ? 150 THR C CG2 1 
ATOM   4140 N  N   . THR C 1 163 ? -17.592 31.661  0.721   1.00 15.17 ? 151 THR C N   1 
ATOM   4141 C  CA  . THR C 1 163 ? -16.280 32.289  0.602   1.00 13.15 ? 151 THR C CA  1 
ATOM   4142 C  C   . THR C 1 163 ? -16.254 33.366  -0.478  1.00 14.94 ? 151 THR C C   1 
ATOM   4143 O  O   . THR C 1 163 ? -15.529 34.355  -0.337  1.00 15.18 ? 151 THR C O   1 
ATOM   4144 C  CB  . THR C 1 163 ? -15.171 31.248  0.355   1.00 14.08 ? 151 THR C CB  1 
ATOM   4145 O  OG1 . THR C 1 163 ? -15.335 30.600  -0.919  1.00 13.85 ? 151 THR C OG1 1 
ATOM   4146 C  CG2 . THR C 1 163 ? -15.167 30.207  1.457   1.00 13.54 ? 151 THR C CG2 1 
ATOM   4147 N  N   . GLN C 1 164 ? -17.064 33.233  -1.531  1.00 16.96 ? 152 GLN C N   1 
ATOM   4148 C  CA  . GLN C 1 164 ? -17.056 34.274  -2.557  1.00 20.18 ? 152 GLN C CA  1 
ATOM   4149 C  C   . GLN C 1 164 ? -17.435 35.637  -1.985  1.00 18.15 ? 152 GLN C C   1 
ATOM   4150 O  O   . GLN C 1 164 ? -16.938 36.664  -2.461  1.00 19.66 ? 152 GLN C O   1 
ATOM   4151 C  CB  . GLN C 1 164 ? -17.994 33.910  -3.709  1.00 20.39 ? 152 GLN C CB  1 
ATOM   4152 C  CG  . GLN C 1 164 ? -17.861 34.849  -4.895  1.00 23.81 ? 152 GLN C CG  1 
ATOM   4153 C  CD  . GLN C 1 164 ? -16.448 34.877  -5.454  1.00 28.66 ? 152 GLN C CD  1 
ATOM   4154 O  OE1 . GLN C 1 164 ? -15.941 33.860  -5.927  1.00 34.88 ? 152 GLN C OE1 1 
ATOM   4155 N  NE2 . GLN C 1 164 ? -15.805 36.041  -5.403  1.00 28.78 ? 152 GLN C NE2 1 
ATOM   4156 N  N   . ASN C 1 165 ? -18.301 35.672  -0.962  1.00 18.54 ? 153 ASN C N   1 
ATOM   4157 C  CA  . ASN C 1 165 ? -18.676 36.950  -0.362  1.00 15.40 ? 153 ASN C CA  1 
ATOM   4158 C  C   . ASN C 1 165 ? -17.491 37.621  0.317   1.00 20.12 ? 153 ASN C C   1 
ATOM   4159 O  O   . ASN C 1 165 ? -17.396 38.855  0.328   1.00 18.15 ? 153 ASN C O   1 
ATOM   4160 C  CB  . ASN C 1 165 ? -19.809 36.752  0.644   1.00 17.44 ? 153 ASN C CB  1 
ATOM   4161 C  CG  . ASN C 1 165 ? -21.140 36.481  -0.025  1.00 22.26 ? 153 ASN C CG  1 
ATOM   4162 O  OD1 . ASN C 1 165 ? -21.310 36.739  -1.218  1.00 22.00 ? 153 ASN C OD1 1 
ATOM   4163 N  ND2 . ASN C 1 165 ? -22.092 35.956  0.741   1.00 21.92 ? 153 ASN C ND2 1 
ATOM   4164 N  N   . HIS C 1 166 ? -16.579 36.829  0.887   1.00 16.14 ? 154 HIS C N   1 
ATOM   4165 C  CA  . HIS C 1 166 ? -15.388 37.402  1.497   1.00 14.93 ? 154 HIS C CA  1 
ATOM   4166 C  C   . HIS C 1 166 ? -14.400 37.852  0.435   1.00 18.71 ? 154 HIS C C   1 
ATOM   4167 O  O   . HIS C 1 166 ? -13.850 38.955  0.523   1.00 17.62 ? 154 HIS C O   1 
ATOM   4168 C  CB  . HIS C 1 166 ? -14.754 36.386  2.454   1.00 13.99 ? 154 HIS C CB  1 
ATOM   4169 C  CG  . HIS C 1 166 ? -15.650 36.023  3.599   1.00 14.29 ? 154 HIS C CG  1 
ATOM   4170 N  ND1 . HIS C 1 166 ? -15.631 36.702  4.800   1.00 14.92 ? 154 HIS C ND1 1 
ATOM   4171 C  CD2 . HIS C 1 166 ? -16.626 35.088  3.709   1.00 13.99 ? 154 HIS C CD2 1 
ATOM   4172 C  CE1 . HIS C 1 166 ? -16.544 36.189  5.606   1.00 13.97 ? 154 HIS C CE1 1 
ATOM   4173 N  NE2 . HIS C 1 166 ? -17.165 35.211  4.969   1.00 12.63 ? 154 HIS C NE2 1 
ATOM   4174 N  N   . PHE C 1 167 ? -14.174 37.020  -0.588  1.00 17.04 ? 155 PHE C N   1 
ATOM   4175 C  CA  . PHE C 1 167 ? -13.284 37.422  -1.671  1.00 16.55 ? 155 PHE C CA  1 
ATOM   4176 C  C   . PHE C 1 167 ? -13.798 38.687  -2.354  1.00 18.26 ? 155 PHE C C   1 
ATOM   4177 O  O   . PHE C 1 167 ? -13.015 39.595  -2.665  1.00 19.24 ? 155 PHE C O   1 
ATOM   4178 C  CB  . PHE C 1 167 ? -13.130 36.280  -2.680  1.00 17.33 ? 155 PHE C CB  1 
ATOM   4179 C  CG  . PHE C 1 167 ? -12.587 35.001  -2.089  1.00 17.88 ? 155 PHE C CG  1 
ATOM   4180 C  CD1 . PHE C 1 167 ? -11.812 35.020  -0.938  1.00 19.32 ? 155 PHE C CD1 1 
ATOM   4181 C  CD2 . PHE C 1 167 ? -12.875 33.778  -2.673  1.00 19.96 ? 155 PHE C CD2 1 
ATOM   4182 C  CE1 . PHE C 1 167 ? -11.305 33.843  -0.394  1.00 19.17 ? 155 PHE C CE1 1 
ATOM   4183 C  CE2 . PHE C 1 167 ? -12.382 32.590  -2.129  1.00 19.79 ? 155 PHE C CE2 1 
ATOM   4184 C  CZ  . PHE C 1 167 ? -11.598 32.625  -0.986  1.00 16.20 ? 155 PHE C CZ  1 
ATOM   4185 N  N   . ASP C 1 168 ? -15.119 38.776  -2.561  1.00 19.73 ? 156 ASP C N   1 
ATOM   4186 C  CA  . ASP C 1 168 ? -15.713 39.977  -3.154  1.00 18.82 ? 156 ASP C CA  1 
ATOM   4187 C  C   . ASP C 1 168 ? -15.499 41.202  -2.272  1.00 20.69 ? 156 ASP C C   1 
ATOM   4188 O  O   . ASP C 1 168 ? -15.162 42.281  -2.773  1.00 22.00 ? 156 ASP C O   1 
ATOM   4189 C  CB  . ASP C 1 168 ? -17.210 39.764  -3.413  1.00 21.74 ? 156 ASP C CB  1 
ATOM   4190 C  CG  . ASP C 1 168 ? -17.485 38.864  -4.616  1.00 27.45 ? 156 ASP C CG  1 
ATOM   4191 O  OD1 . ASP C 1 168 ? -16.532 38.503  -5.344  1.00 30.14 ? 156 ASP C OD1 1 
ATOM   4192 O  OD2 . ASP C 1 168 ? -18.669 38.533  -4.840  1.00 29.01 ? 156 ASP C OD2 1 
ATOM   4193 N  N   . ALA C 1 169 ? -15.684 41.055  -0.955  1.00 19.11 ? 157 ALA C N   1 
ATOM   4194 C  CA  . ALA C 1 169 ? -15.471 42.172  -0.040  1.00 19.82 ? 157 ALA C CA  1 
ATOM   4195 C  C   . ALA C 1 169 ? -14.020 42.633  -0.059  1.00 18.24 ? 157 ALA C C   1 
ATOM   4196 O  O   . ALA C 1 169 ? -13.743 43.837  -0.094  1.00 18.95 ? 157 ALA C O   1 
ATOM   4197 C  CB  . ALA C 1 169 ? -15.890 41.781  1.378   1.00 20.13 ? 157 ALA C CB  1 
ATOM   4198 N  N   . TRP C 1 170 ? -13.073 41.688  -0.036  1.00 17.18 ? 158 TRP C N   1 
ATOM   4199 C  CA  . TRP C 1 170 ? -11.661 42.058  -0.099  1.00 16.89 ? 158 TRP C CA  1 
ATOM   4200 C  C   . TRP C 1 170 ? -11.353 42.801  -1.393  1.00 18.99 ? 158 TRP C C   1 
ATOM   4201 O  O   . TRP C 1 170 ? -10.673 43.832  -1.397  1.00 19.50 ? 158 TRP C O   1 
ATOM   4202 C  CB  . TRP C 1 170 ? -10.791 40.806  -0.001  1.00 18.30 ? 158 TRP C CB  1 
ATOM   4203 C  CG  . TRP C 1 170 ? -10.877 40.144  1.348   1.00 21.17 ? 158 TRP C CG  1 
ATOM   4204 C  CD1 . TRP C 1 170 ? -11.267 40.716  2.519   1.00 27.83 ? 158 TRP C CD1 1 
ATOM   4205 C  CD2 . TRP C 1 170 ? -10.583 38.780  1.646   1.00 17.03 ? 158 TRP C CD2 1 
ATOM   4206 N  NE1 . TRP C 1 170 ? -11.218 39.795  3.540   1.00 26.26 ? 158 TRP C NE1 1 
ATOM   4207 C  CE2 . TRP C 1 170 ? -10.800 38.596  3.029   1.00 19.61 ? 158 TRP C CE2 1 
ATOM   4208 C  CE3 . TRP C 1 170 ? -10.147 37.697  0.883   1.00 16.84 ? 158 TRP C CE3 1 
ATOM   4209 C  CZ2 . TRP C 1 170 ? -10.592 37.375  3.664   1.00 16.86 ? 158 TRP C CZ2 1 
ATOM   4210 C  CZ3 . TRP C 1 170 ? -9.941  36.481  1.520   1.00 17.15 ? 158 TRP C CZ3 1 
ATOM   4211 C  CH2 . TRP C 1 170 ? -10.171 36.332  2.892   1.00 14.72 ? 158 TRP C CH2 1 
ATOM   4212 N  N   . LYS C 1 171 ? -11.857 42.279  -2.503  1.00 19.99 ? 159 LYS C N   1 
ATOM   4213 C  CA  . LYS C 1 171 ? -11.617 42.892  -3.796  1.00 22.82 ? 159 LYS C CA  1 
ATOM   4214 C  C   . LYS C 1 171 ? -12.273 44.268  -3.882  1.00 22.91 ? 159 LYS C C   1 
ATOM   4215 O  O   . LYS C 1 171 ? -11.706 45.206  -4.461  1.00 20.56 ? 159 LYS C O   1 
ATOM   4216 C  CB  . LYS C 1 171 ? -12.084 41.891  -4.850  1.00 25.31 ? 159 LYS C CB  1 
ATOM   4217 C  CG  . LYS C 1 171 ? -12.494 42.332  -6.146  1.00 33.83 ? 159 LYS C CG  1 
ATOM   4218 C  CD  . LYS C 1 171 ? -13.023 41.053  -6.719  1.00 42.99 ? 159 LYS C CD  1 
ATOM   4219 C  CE  . LYS C 1 171 ? -14.413 40.909  -6.402  1.00 39.96 ? 159 LYS C CE  1 
ATOM   4220 N  NZ  . LYS C 1 171 ? -15.084 42.255  -6.660  1.00 42.72 ? 159 LYS C NZ  1 
ATOM   4221 N  N   . ASN C 1 172 ? -13.457 44.413  -3.279  1.00 21.00 ? 160 ASN C N   1 
ATOM   4222 C  CA  . ASN C 1 172 ? -14.129 45.716  -3.222  1.00 21.68 ? 160 ASN C CA  1 
ATOM   4223 C  C   . ASN C 1 172 ? -13.327 46.744  -2.422  1.00 26.79 ? 160 ASN C C   1 
ATOM   4224 O  O   . ASN C 1 172 ? -13.328 47.936  -2.758  1.00 22.86 ? 160 ASN C O   1 
ATOM   4225 C  CB  . ASN C 1 172 ? -15.536 45.553  -2.623  1.00 23.69 ? 160 ASN C CB  1 
ATOM   4226 C  CG  . ASN C 1 172 ? -16.338 46.827  -2.612  1.00 30.55 ? 160 ASN C CG  1 
ATOM   4227 O  OD1 . ASN C 1 172 ? -16.874 47.242  -3.644  1.00 35.54 ? 160 ASN C OD1 1 
ATOM   4228 N  ND2 . ASN C 1 172 ? -16.440 47.454  -1.444  1.00 35.08 ? 160 ASN C ND2 1 
ATOM   4229 N  N   . ALA C 1 173 ? -12.640 46.308  -1.369  1.00 16.35 ? 161 ALA C N   1 
ATOM   4230 C  CA  . ALA C 1 173 ? -11.727 47.173  -0.640  1.00 20.99 ? 161 ALA C CA  1 
ATOM   4231 C  C   . ALA C 1 173 ? -10.414 47.379  -1.375  1.00 18.05 ? 161 ALA C C   1 
ATOM   4232 O  O   . ALA C 1 173 ? -9.520  48.045  -0.840  1.00 24.19 ? 161 ALA C O   1 
ATOM   4233 C  CB  . ALA C 1 173 ? -11.451 46.607  0.758   1.00 22.17 ? 161 ALA C CB  1 
ATOM   4234 N  N   . GLY C 1 174 ? -10.268 46.824  -2.576  1.00 21.12 ? 162 GLY C N   1 
ATOM   4235 C  CA  . GLY C 1 174 ? -9.091  47.060  -3.383  1.00 22.86 ? 162 GLY C CA  1 
ATOM   4236 C  C   . GLY C 1 174 ? -7.981  46.050  -3.233  1.00 27.83 ? 162 GLY C C   1 
ATOM   4237 O  O   . GLY C 1 174 ? -6.884  46.280  -3.759  1.00 31.67 ? 162 GLY C O   1 
ATOM   4238 N  N   . LEU C 1 175 ? -8.222  44.940  -2.542  1.00 20.97 ? 163 LEU C N   1 
ATOM   4239 C  CA  . LEU C 1 175 ? -7.187  43.944  -2.310  1.00 18.57 ? 163 LEU C CA  1 
ATOM   4240 C  C   . LEU C 1 175 ? -7.134  42.964  -3.479  1.00 23.14 ? 163 LEU C C   1 
ATOM   4241 O  O   . LEU C 1 175 ? -8.163  42.421  -3.894  1.00 24.17 ? 163 LEU C O   1 
ATOM   4242 C  CB  . LEU C 1 175 ? -7.444  43.206  -0.995  1.00 18.99 ? 163 LEU C CB  1 
ATOM   4243 C  CG  . LEU C 1 175 ? -7.524  44.110  0.243   1.00 19.79 ? 163 LEU C CG  1 
ATOM   4244 C  CD1 . LEU C 1 175 ? -7.927  43.309  1.484   1.00 22.11 ? 163 LEU C CD1 1 
ATOM   4245 C  CD2 . LEU C 1 175 ? -6.204  44.828  0.470   1.00 19.58 ? 163 LEU C CD2 1 
ATOM   4246 N  N   . GLU C 1 176 ? -5.932  42.737  -3.995  1.00 25.24 ? 164 GLU C N   1 
ATOM   4247 C  CA  . GLU C 1 176 ? -5.727  41.850  -5.131  1.00 22.15 ? 164 GLU C CA  1 
ATOM   4248 C  C   . GLU C 1 176 ? -5.557  40.410  -4.669  1.00 21.12 ? 164 GLU C C   1 
ATOM   4249 O  O   . GLU C 1 176 ? -4.870  40.143  -3.680  1.00 21.51 ? 164 GLU C O   1 
ATOM   4250 C  CB  . GLU C 1 176 ? -4.485  42.267  -5.917  1.00 24.85 ? 164 GLU C CB  1 
ATOM   4251 C  CG  . GLU C 1 176 ? -4.598  43.580  -6.661  1.00 33.82 ? 164 GLU C CG  1 
ATOM   4252 C  CD  . GLU C 1 176 ? -3.339  43.886  -7.446  1.00 43.87 ? 164 GLU C CD  1 
ATOM   4253 O  OE1 . GLU C 1 176 ? -2.754  44.971  -7.234  1.00 54.53 ? 164 GLU C OE1 1 
ATOM   4254 O  OE2 . GLU C 1 176 ? -2.927  43.032  -8.264  1.00 43.23 ? 164 GLU C OE2 1 
ATOM   4255 N  N   . MET C 1 177 ? -6.162  39.486  -5.413  1.00 21.25 ? 165 MET C N   1 
ATOM   4256 C  CA  . MET C 1 177 ? -5.978  38.055  -5.217  1.00 20.13 ? 165 MET C CA  1 
ATOM   4257 C  C   . MET C 1 177 ? -5.452  37.428  -6.498  1.00 17.72 ? 165 MET C C   1 
ATOM   4258 O  O   . MET C 1 177 ? -5.792  37.862  -7.601  1.00 17.69 ? 165 MET C O   1 
ATOM   4259 C  CB  . MET C 1 177 ? -7.287  37.366  -4.841  1.00 19.71 ? 165 MET C CB  1 
ATOM   4260 C  CG  . MET C 1 177 ? -8.067  38.086  -3.777  1.00 29.08 ? 165 MET C CG  1 
ATOM   4261 S  SD  . MET C 1 177 ? -7.898  37.197  -2.238  1.00 42.28 ? 165 MET C SD  1 
ATOM   4262 C  CE  . MET C 1 177 ? -8.940  35.787  -2.561  1.00 31.13 ? 165 MET C CE  1 
ATOM   4263 N  N   . GLY C 1 178 ? -4.646  36.389  -6.348  1.00 15.63 ? 166 GLY C N   1 
ATOM   4264 C  CA  . GLY C 1 178 ? -4.116  35.649  -7.470  1.00 14.10 ? 166 GLY C CA  1 
ATOM   4265 C  C   . GLY C 1 178 ? -4.912  34.400  -7.778  1.00 14.77 ? 166 GLY C C   1 
ATOM   4266 O  O   . GLY C 1 178 ? -6.116  34.312  -7.507  1.00 17.00 ? 166 GLY C O   1 
ATOM   4267 N  N   . THR C 1 179 ? -4.232  33.429  -8.368  1.00 13.57 ? 167 THR C N   1 
ATOM   4268 C  CA  . THR C 1 179 ? -4.839  32.155  -8.712  1.00 17.29 ? 167 THR C CA  1 
ATOM   4269 C  C   . THR C 1 179 ? -4.919  31.297  -7.461  1.00 13.28 ? 167 THR C C   1 
ATOM   4270 O  O   . THR C 1 179 ? -3.947  31.206  -6.711  1.00 12.41 ? 167 THR C O   1 
ATOM   4271 C  CB  . THR C 1 179 ? -4.009  31.467  -9.796  1.00 20.45 ? 167 THR C CB  1 
ATOM   4272 O  OG1 . THR C 1 179 ? -3.934  32.338  -10.938 1.00 20.42 ? 167 THR C OG1 1 
ATOM   4273 C  CG2 . THR C 1 179 ? -4.649  30.151  -10.208 1.00 20.90 ? 167 THR C CG2 1 
ATOM   4274 N  N   . HIS C 1 180 ? -6.077  30.684  -7.227  1.00 13.61 ? 168 HIS C N   1 
ATOM   4275 C  CA  . HIS C 1 180 ? -6.290  29.982  -5.968  1.00 13.31 ? 168 HIS C CA  1 
ATOM   4276 C  C   . HIS C 1 180 ? -5.477  28.697  -5.904  1.00 14.69 ? 168 HIS C C   1 
ATOM   4277 O  O   . HIS C 1 180 ? -5.441  27.910  -6.861  1.00 16.39 ? 168 HIS C O   1 
ATOM   4278 C  CB  . HIS C 1 180 ? -7.775  29.686  -5.767  1.00 15.68 ? 168 HIS C CB  1 
ATOM   4279 C  CG  . HIS C 1 180 ? -8.527  30.832  -5.168  1.00 21.20 ? 168 HIS C CG  1 
ATOM   4280 N  ND1 . HIS C 1 180 ? -8.697  30.979  -3.809  1.00 22.85 ? 168 HIS C ND1 1 
ATOM   4281 C  CD2 . HIS C 1 180 ? -9.110  31.913  -5.741  1.00 26.55 ? 168 HIS C CD2 1 
ATOM   4282 C  CE1 . HIS C 1 180 ? -9.376  32.087  -3.570  1.00 27.46 ? 168 HIS C CE1 1 
ATOM   4283 N  NE2 . HIS C 1 180 ? -9.640  32.672  -4.726  1.00 24.96 ? 168 HIS C NE2 1 
ATOM   4284 N  N   . ASN C 1 181 ? -4.807  28.508  -4.768  1.00 10.18 ? 169 ASN C N   1 
ATOM   4285 C  CA  . ASN C 1 181 ? -4.195  27.238  -4.403  1.00 11.53 ? 169 ASN C CA  1 
ATOM   4286 C  C   . ASN C 1 181 ? -5.137  26.594  -3.391  1.00 10.81 ? 169 ASN C C   1 
ATOM   4287 O  O   . ASN C 1 181 ? -6.356  26.647  -3.581  1.00 12.33 ? 169 ASN C O   1 
ATOM   4288 C  CB  . ASN C 1 181 ? -2.781  27.452  -3.847  1.00 12.31 ? 169 ASN C CB  1 
ATOM   4289 C  CG  . ASN C 1 181 ? -1.942  26.176  -3.866  1.00 16.51 ? 169 ASN C CG  1 
ATOM   4290 O  OD1 . ASN C 1 181 ? -1.948  25.413  -2.906  1.00 16.92 ? 169 ASN C OD1 1 
ATOM   4291 N  ND2 . ASN C 1 181 ? -1.221  25.941  -4.967  1.00 18.74 ? 169 ASN C ND2 1 
ATOM   4292 N  N   . TYR C 1 182 ? -4.622  26.039  -2.297  1.00 9.36  ? 170 TYR C N   1 
ATOM   4293 C  CA  . TYR C 1 182 ? -5.542  25.267  -1.475  1.00 10.90 ? 170 TYR C CA  1 
ATOM   4294 C  C   . TYR C 1 182 ? -6.413  26.152  -0.584  1.00 10.41 ? 170 TYR C C   1 
ATOM   4295 O  O   . TYR C 1 182 ? -6.144  27.335  -0.359  1.00 9.79  ? 170 TYR C O   1 
ATOM   4296 C  CB  . TYR C 1 182 ? -4.796  24.245  -0.620  1.00 10.68 ? 170 TYR C CB  1 
ATOM   4297 C  CG  . TYR C 1 182 ? -3.911  24.750  0.499   1.00 9.56  ? 170 TYR C CG  1 
ATOM   4298 C  CD1 . TYR C 1 182 ? -4.450  25.166  1.709   1.00 7.89  ? 170 TYR C CD1 1 
ATOM   4299 C  CD2 . TYR C 1 182 ? -2.526  24.711  0.378   1.00 11.39 ? 170 TYR C CD2 1 
ATOM   4300 C  CE1 . TYR C 1 182 ? -3.636  25.587  2.755   1.00 12.08 ? 170 TYR C CE1 1 
ATOM   4301 C  CE2 . TYR C 1 182 ? -1.711  25.111  1.417   1.00 11.75 ? 170 TYR C CE2 1 
ATOM   4302 C  CZ  . TYR C 1 182 ? -2.273  25.552  2.608   1.00 14.35 ? 170 TYR C CZ  1 
ATOM   4303 O  OH  . TYR C 1 182 ? -1.463  25.957  3.660   1.00 15.40 ? 170 TYR C OH  1 
ATOM   4304 N  N   . MET C 1 183 ? -7.482  25.543  -0.078  1.00 9.02  ? 171 MET C N   1 
ATOM   4305 C  CA  . MET C 1 183 ? -8.390  26.193  0.860   1.00 9.35  ? 171 MET C CA  1 
ATOM   4306 C  C   . MET C 1 183 ? -8.875  25.129  1.832   1.00 10.66 ? 171 MET C C   1 
ATOM   4307 O  O   . MET C 1 183 ? -9.402  24.097  1.400   1.00 10.44 ? 171 MET C O   1 
ATOM   4308 C  CB  . MET C 1 183 ? -9.583  26.836  0.132   1.00 9.56  ? 171 MET C CB  1 
ATOM   4309 C  CG  . MET C 1 183 ? -10.496 27.635  1.064   1.00 12.73 ? 171 MET C CG  1 
ATOM   4310 S  SD  . MET C 1 183 ? -11.827 28.489  0.194   1.00 15.36 ? 171 MET C SD  1 
ATOM   4311 C  CE  . MET C 1 183 ? -12.820 27.104  -0.348  1.00 18.76 ? 171 MET C CE  1 
ATOM   4312 N  N   . ILE C 1 184 ? -8.722  25.378  3.133   1.00 7.62  ? 172 ILE C N   1 
ATOM   4313 C  CA  . ILE C 1 184 ? -9.071  24.371  4.126   1.00 8.49  ? 172 ILE C CA  1 
ATOM   4314 C  C   . ILE C 1 184 ? -9.858  25.033  5.246   1.00 8.10  ? 172 ILE C C   1 
ATOM   4315 O  O   . ILE C 1 184 ? -9.839  26.254  5.410   1.00 10.70 ? 172 ILE C O   1 
ATOM   4316 C  CB  . ILE C 1 184 ? -7.817  23.655  4.708   1.00 9.64  ? 172 ILE C CB  1 
ATOM   4317 C  CG1 . ILE C 1 184 ? -6.857  24.658  5.359   1.00 9.56  ? 172 ILE C CG1 1 
ATOM   4318 C  CG2 . ILE C 1 184 ? -7.087  22.848  3.644   1.00 10.49 ? 172 ILE C CG2 1 
ATOM   4319 C  CD1 . ILE C 1 184 ? -5.696  23.989  6.116   1.00 10.94 ? 172 ILE C CD1 1 
ATOM   4320 N  N   . VAL C 1 185 ? -10.557 24.209  6.027   1.00 7.76  ? 173 VAL C N   1 
ATOM   4321 C  CA  . VAL C 1 185 ? -11.135 24.667  7.286   1.00 9.21  ? 173 VAL C CA  1 
ATOM   4322 C  C   . VAL C 1 185 ? -10.124 24.309  8.367   1.00 10.93 ? 173 VAL C C   1 
ATOM   4323 O  O   . VAL C 1 185 ? -9.933  23.130  8.683   1.00 9.97  ? 173 VAL C O   1 
ATOM   4324 C  CB  . VAL C 1 185 ? -12.501 24.025  7.556   1.00 9.61  ? 173 VAL C CB  1 
ATOM   4325 C  CG1 . VAL C 1 185 ? -13.068 24.523  8.874   1.00 13.75 ? 173 VAL C CG1 1 
ATOM   4326 C  CG2 . VAL C 1 185 ? -13.464 24.339  6.415   1.00 11.61 ? 173 VAL C CG2 1 
ATOM   4327 N  N   . ALA C 1 186 ? -9.439  25.311  8.904   1.00 8.08  ? 174 ALA C N   1 
ATOM   4328 C  CA  . ALA C 1 186 ? -8.224  25.065  9.662   1.00 9.59  ? 174 ALA C CA  1 
ATOM   4329 C  C   . ALA C 1 186 ? -8.405  25.403  11.130  1.00 10.12 ? 174 ALA C C   1 
ATOM   4330 O  O   . ALA C 1 186 ? -9.074  26.377  11.484  1.00 10.67 ? 174 ALA C O   1 
ATOM   4331 C  CB  . ALA C 1 186 ? -7.041  25.877  9.117   1.00 10.48 ? 174 ALA C CB  1 
ATOM   4332 N  N   . THR C 1 187 ? -7.767  24.600  11.968  1.00 9.10  ? 175 THR C N   1 
ATOM   4333 C  CA  . THR C 1 187 ? -7.555  24.897  13.375  1.00 8.79  ? 175 THR C CA  1 
ATOM   4334 C  C   . THR C 1 187 ? -6.125  25.397  13.540  1.00 11.02 ? 175 THR C C   1 
ATOM   4335 O  O   . THR C 1 187 ? -5.185  24.760  13.054  1.00 10.23 ? 175 THR C O   1 
ATOM   4336 C  CB  . THR C 1 187 ? -7.780  23.633  14.203  1.00 10.76 ? 175 THR C CB  1 
ATOM   4337 O  OG1 . THR C 1 187 ? -9.123  23.179  14.019  1.00 11.42 ? 175 THR C OG1 1 
ATOM   4338 C  CG2 . THR C 1 187 ? -7.504  23.889  15.686  1.00 13.25 ? 175 THR C CG2 1 
ATOM   4339 N  N   . ALA C 1 188 ? -5.952  26.530  14.223  1.00 9.79  ? 176 ALA C N   1 
ATOM   4340 C  CA  . ALA C 1 188 ? -4.622  27.087  14.436  1.00 11.08 ? 176 ALA C CA  1 
ATOM   4341 C  C   . ALA C 1 188 ? -4.398  27.359  15.913  1.00 9.86  ? 176 ALA C C   1 
ATOM   4342 O  O   . ALA C 1 188 ? -5.341  27.590  16.670  1.00 10.45 ? 176 ALA C O   1 
ATOM   4343 C  CB  . ALA C 1 188 ? -4.408  28.380  13.631  1.00 12.41 ? 176 ALA C CB  1 
ATOM   4344 N  N   . GLY C 1 189 ? -3.135  27.330  16.319  1.00 13.74 ? 177 GLY C N   1 
ATOM   4345 C  CA  . GLY C 1 189 ? -2.812  27.591  17.710  1.00 15.14 ? 177 GLY C CA  1 
ATOM   4346 C  C   . GLY C 1 189 ? -1.396  28.095  17.853  1.00 15.06 ? 177 GLY C C   1 
ATOM   4347 O  O   . GLY C 1 189 ? -0.538  27.858  16.995  1.00 14.81 ? 177 GLY C O   1 
ATOM   4348 N  N   . TYR C 1 190 ? -1.157  28.805  18.953  1.00 13.33 ? 178 TYR C N   1 
ATOM   4349 C  CA  . TYR C 1 190 ? 0.192   29.261  19.252  1.00 16.31 ? 178 TYR C CA  1 
ATOM   4350 C  C   . TYR C 1 190 ? 0.356   29.365  20.758  1.00 16.50 ? 178 TYR C C   1 
ATOM   4351 O  O   . TYR C 1 190 ? -0.454  30.021  21.422  1.00 15.45 ? 178 TYR C O   1 
ATOM   4352 C  CB  . TYR C 1 190 ? 0.493   30.615  18.605  1.00 18.92 ? 178 TYR C CB  1 
ATOM   4353 C  CG  . TYR C 1 190 ? 1.886   31.104  18.936  1.00 25.05 ? 178 TYR C CG  1 
ATOM   4354 C  CD1 . TYR C 1 190 ? 3.006   30.445  18.446  1.00 26.84 ? 178 TYR C CD1 1 
ATOM   4355 C  CD2 . TYR C 1 190 ? 2.084   32.198  19.767  1.00 23.58 ? 178 TYR C CD2 1 
ATOM   4356 C  CE1 . TYR C 1 190 ? 4.281   30.880  18.742  1.00 25.45 ? 178 TYR C CE1 1 
ATOM   4357 C  CE2 . TYR C 1 190 ? 3.350   32.636  20.068  1.00 30.44 ? 178 TYR C CE2 1 
ATOM   4358 C  CZ  . TYR C 1 190 ? 4.448   31.980  19.556  1.00 32.99 ? 178 TYR C CZ  1 
ATOM   4359 O  OH  . TYR C 1 190 ? 5.718   32.421  19.864  1.00 35.15 ? 178 TYR C OH  1 
ATOM   4360 N  N   . GLN C 1 191 ? 1.395   28.716  21.278  1.00 16.86 ? 179 GLN C N   1 
ATOM   4361 C  CA  . GLN C 1 191 ? 1.739   28.714  22.704  1.00 17.61 ? 179 GLN C CA  1 
ATOM   4362 C  C   . GLN C 1 191 ? 0.496   28.496  23.568  1.00 17.46 ? 179 GLN C C   1 
ATOM   4363 O  O   . GLN C 1 191 ? 0.137   29.291  24.439  1.00 14.94 ? 179 GLN C O   1 
ATOM   4364 C  CB  . GLN C 1 191 ? 2.509   29.986  23.071  1.00 17.13 ? 179 GLN C CB  1 
ATOM   4365 C  CG  . GLN C 1 191 ? 3.880   30.012  22.373  1.00 22.99 ? 179 GLN C CG  1 
ATOM   4366 C  CD  . GLN C 1 191 ? 4.891   30.961  23.001  1.00 28.48 ? 179 GLN C CD  1 
ATOM   4367 O  OE1 . GLN C 1 191 ? 4.526   31.966  23.613  1.00 30.73 ? 179 GLN C OE1 1 
ATOM   4368 N  NE2 . GLN C 1 191 ? 6.177   30.648  22.836  1.00 30.28 ? 179 GLN C NE2 1 
ATOM   4369 N  N   . SER C 1 192 ? -0.171  27.375  23.291  1.00 14.54 ? 180 SER C N   1 
ATOM   4370 C  CA  . SER C 1 192 ? -1.414  27.035  23.957  1.00 14.59 ? 180 SER C CA  1 
ATOM   4371 C  C   . SER C 1 192 ? -1.568  25.519  23.984  1.00 13.64 ? 180 SER C C   1 
ATOM   4372 O  O   . SER C 1 192 ? -0.691  24.768  23.540  1.00 13.31 ? 180 SER C O   1 
ATOM   4373 C  CB  . SER C 1 192 ? -2.599  27.702  23.261  1.00 15.39 ? 180 SER C CB  1 
ATOM   4374 O  OG  . SER C 1 192 ? -2.730  27.199  21.942  1.00 14.90 ? 180 SER C OG  1 
ATOM   4375 N  N   . SER C 1 193 ? -2.694  25.080  24.524  1.00 14.06 ? 181 SER C N   1 
ATOM   4376 C  CA  . SER C 1 193 ? -3.109  23.687  24.509  1.00 15.20 ? 181 SER C CA  1 
ATOM   4377 C  C   . SER C 1 193 ? -4.546  23.653  24.018  1.00 13.15 ? 181 SER C C   1 
ATOM   4378 O  O   . SER C 1 193 ? -5.235  24.676  23.987  1.00 15.55 ? 181 SER C O   1 
ATOM   4379 C  CB  . SER C 1 193 ? -2.986  23.051  25.905  1.00 18.90 ? 181 SER C CB  1 
ATOM   4380 O  OG  . SER C 1 193 ? -1.626  23.105  26.335  1.00 17.59 ? 181 SER C OG  1 
ATOM   4381 N  N   . GLY C 1 194 ? -5.013  22.479  23.631  1.00 12.70 ? 182 GLY C N   1 
ATOM   4382 C  CA  . GLY C 1 194 ? -6.391  22.387  23.203  1.00 13.09 ? 182 GLY C CA  1 
ATOM   4383 C  C   . GLY C 1 194 ? -6.638  21.107  22.441  1.00 16.79 ? 182 GLY C C   1 
ATOM   4384 O  O   . GLY C 1 194 ? -5.747  20.270  22.261  1.00 14.20 ? 182 GLY C O   1 
ATOM   4385 N  N   . SER C 1 195 ? -7.881  20.981  21.993  1.00 15.03 ? 183 SER C N   1 
ATOM   4386 C  CA  . SER C 1 195 ? -8.251  19.919  21.073  1.00 15.58 ? 183 SER C CA  1 
ATOM   4387 C  C   . SER C 1 195 ? -9.362  20.418  20.164  1.00 14.62 ? 183 SER C C   1 
ATOM   4388 O  O   . SER C 1 195 ? -10.110 21.338  20.507  1.00 14.41 ? 183 SER C O   1 
ATOM   4389 C  CB  . SER C 1 195 ? -8.693  18.659  21.820  1.00 17.67 ? 183 SER C CB  1 
ATOM   4390 O  OG  . SER C 1 195 ? -9.912  18.893  22.488  1.00 20.09 ? 183 SER C OG  1 
ATOM   4391 N  N   . ALA C 1 196 ? -9.445  19.818  18.985  1.00 13.28 ? 184 ALA C N   1 
ATOM   4392 C  CA  . ALA C 1 196 ? -10.511 20.153  18.058  1.00 13.07 ? 184 ALA C CA  1 
ATOM   4393 C  C   . ALA C 1 196 ? -10.804 18.928  17.211  1.00 14.04 ? 184 ALA C C   1 
ATOM   4394 O  O   . ALA C 1 196 ? -9.915  18.122  16.933  1.00 14.33 ? 184 ALA C O   1 
ATOM   4395 C  CB  . ALA C 1 196 ? -10.134 21.336  17.158  1.00 13.22 ? 184 ALA C CB  1 
ATOM   4396 N  N   . SER C 1 197 ? -12.060 18.796  16.808  1.00 13.78 ? 185 SER C N   1 
ATOM   4397 C  CA  . SER C 1 197 ? -12.466 17.753  15.871  1.00 13.81 ? 185 SER C CA  1 
ATOM   4398 C  C   . SER C 1 197 ? -13.431 18.389  14.892  1.00 14.22 ? 185 SER C C   1 
ATOM   4399 O  O   . SER C 1 197 ? -14.512 18.829  15.296  1.00 16.44 ? 185 SER C O   1 
ATOM   4400 C  CB  . SER C 1 197 ? -13.134 16.577  16.589  1.00 19.64 ? 185 SER C CB  1 
ATOM   4401 O  OG  . SER C 1 197 ? -12.240 15.967  17.501  1.00 29.17 ? 185 SER C OG  1 
ATOM   4402 N  N   . ILE C 1 198 ? -13.054 18.436  13.620  1.00 12.86 ? 186 ILE C N   1 
ATOM   4403 C  CA  . ILE C 1 198 ? -13.780 19.206  12.619  1.00 11.23 ? 186 ILE C CA  1 
ATOM   4404 C  C   . ILE C 1 198 ? -14.116 18.296  11.451  1.00 13.97 ? 186 ILE C C   1 
ATOM   4405 O  O   . ILE C 1 198 ? -13.277 17.499  11.020  1.00 12.82 ? 186 ILE C O   1 
ATOM   4406 C  CB  . ILE C 1 198 ? -12.946 20.413  12.136  1.00 10.85 ? 186 ILE C CB  1 
ATOM   4407 C  CG1 . ILE C 1 198 ? -12.672 21.376  13.302  1.00 16.12 ? 186 ILE C CG1 1 
ATOM   4408 C  CG2 . ILE C 1 198 ? -13.627 21.119  10.957  1.00 11.55 ? 186 ILE C CG2 1 
ATOM   4409 C  CD1 . ILE C 1 198 ? -13.912 22.073  13.844  1.00 15.08 ? 186 ILE C CD1 1 
ATOM   4410 N  N   . THR C 1 199 ? -15.338 18.418  10.933  1.00 13.12 ? 187 THR C N   1 
ATOM   4411 C  CA  . THR C 1 199 ? -15.752 17.681  9.744   1.00 14.53 ? 187 THR C CA  1 
ATOM   4412 C  C   . THR C 1 199 ? -16.150 18.668  8.659   1.00 15.07 ? 187 THR C C   1 
ATOM   4413 O  O   . THR C 1 199 ? -17.077 19.464  8.843   1.00 15.88 ? 187 THR C O   1 
ATOM   4414 C  CB  . THR C 1 199 ? -16.910 16.728  10.050  1.00 16.25 ? 187 THR C CB  1 
ATOM   4415 O  OG1 . THR C 1 199 ? -16.507 15.809  11.071  1.00 20.59 ? 187 THR C OG1 1 
ATOM   4416 C  CG2 . THR C 1 199 ? -17.297 15.952  8.792   1.00 18.53 ? 187 THR C CG2 1 
ATOM   4417 N  N   . VAL C 1 200 ? -15.449 18.615  7.544   1.00 13.12 ? 188 VAL C N   1 
ATOM   4418 C  CA  . VAL C 1 200 ? -15.779 19.410  6.371   1.00 13.91 ? 188 VAL C CA  1 
ATOM   4419 C  C   . VAL C 1 200 ? -16.688 18.586  5.463   1.00 17.65 ? 188 VAL C C   1 
ATOM   4420 O  O   . VAL C 1 200 ? -16.487 17.380  5.299   1.00 17.52 ? 188 VAL C O   1 
ATOM   4421 C  CB  . VAL C 1 200 ? -14.494 19.838  5.649   1.00 16.54 ? 188 VAL C CB  1 
ATOM   4422 C  CG1 . VAL C 1 200 ? -14.839 20.684  4.514   1.00 24.90 ? 188 VAL C CG1 1 
ATOM   4423 C  CG2 . VAL C 1 200 ? -13.582 20.595  6.604   1.00 19.00 ? 188 VAL C CG2 1 
ATOM   4424 N  N   . GLN C 1 201 ? -17.702 19.226  4.889   1.00 19.79 ? 189 GLN C N   1 
ATOM   4425 C  CA  . GLN C 1 201 ? -18.628 18.517  3.998   1.00 27.26 ? 189 GLN C CA  1 
ATOM   4426 C  C   . GLN C 1 201 ? -18.300 18.741  2.524   1.00 29.53 ? 189 GLN C C   1 
ATOM   4427 O  O   . GLN C 1 201 ? -17.493 19.605  2.177   1.00 27.17 ? 189 GLN C O   1 
ATOM   4428 C  CB  . GLN C 1 201 ? -20.068 18.944  4.278   1.00 28.31 ? 189 GLN C CB  1 
ATOM   4429 C  CG  . GLN C 1 201 ? -20.573 18.474  5.628   1.00 31.25 ? 189 GLN C CG  1 
ATOM   4430 C  CD  . GLN C 1 201 ? -21.666 19.359  6.183   1.00 35.52 ? 189 GLN C CD  1 
ATOM   4431 O  OE1 . GLN C 1 201 ? -22.556 19.796  5.449   1.00 41.88 ? 189 GLN C OE1 1 
ATOM   4432 N  NE2 . GLN C 1 201 ? -21.611 19.630  7.490   1.00 34.08 ? 189 GLN C NE2 1 
ATOM   4433 N  N   . MET D 1 12  ? 1.040   59.218  35.436  1.00 44.09 ? 0   MET D N   1 
ATOM   4434 C  CA  . MET D 1 12  ? 0.716   58.021  36.203  1.00 37.00 ? 0   MET D CA  1 
ATOM   4435 C  C   . MET D 1 12  ? 0.785   56.765  35.342  1.00 32.27 ? 0   MET D C   1 
ATOM   4436 O  O   . MET D 1 12  ? 1.593   55.877  35.581  1.00 34.35 ? 0   MET D O   1 
ATOM   4437 C  CB  . MET D 1 12  ? -0.671  58.142  36.823  1.00 43.47 ? 0   MET D CB  1 
ATOM   4438 C  CG  . MET D 1 12  ? -0.829  57.398  38.140  1.00 41.97 ? 0   MET D CG  1 
ATOM   4439 S  SD  . MET D 1 12  ? -0.293  58.376  39.559  1.00 73.73 ? 0   MET D SD  1 
ATOM   4440 C  CE  . MET D 1 12  ? -0.855  60.015  39.076  1.00 52.11 ? 0   MET D CE  1 
ATOM   4441 N  N   . GLU D 1 13  ? -0.078  56.680  34.334  1.00 31.27 ? 1   GLU D N   1 
ATOM   4442 C  CA  . GLU D 1 13  ? -0.101  55.503  33.470  1.00 28.97 ? 1   GLU D CA  1 
ATOM   4443 C  C   . GLU D 1 13  ? 0.974   55.623  32.398  1.00 28.45 ? 1   GLU D C   1 
ATOM   4444 O  O   . GLU D 1 13  ? 1.081   56.658  31.731  1.00 30.92 ? 1   GLU D O   1 
ATOM   4445 C  CB  . GLU D 1 13  ? -1.478  55.338  32.829  1.00 36.32 ? 1   GLU D CB  1 
ATOM   4446 C  CG  . GLU D 1 13  ? -2.516  54.721  33.751  1.00 32.10 ? 1   GLU D CG  1 
ATOM   4447 C  CD  . GLU D 1 13  ? -3.817  54.415  33.033  1.00 45.71 ? 1   GLU D CD  1 
ATOM   4448 O  OE1 . GLU D 1 13  ? -4.676  53.703  33.608  1.00 44.08 ? 1   GLU D OE1 1 
ATOM   4449 O  OE2 . GLU D 1 13  ? -3.979  54.890  31.887  1.00 46.34 ? 1   GLU D OE2 1 
ATOM   4450 N  N   . ILE D 1 14  ? 1.778   54.577  32.237  1.00 21.81 ? 2   ILE D N   1 
ATOM   4451 C  CA  . ILE D 1 14  ? 2.812   54.577  31.212  1.00 23.04 ? 2   ILE D CA  1 
ATOM   4452 C  C   . ILE D 1 14  ? 2.628   53.371  30.298  1.00 23.20 ? 2   ILE D C   1 
ATOM   4453 O  O   . ILE D 1 14  ? 2.215   52.288  30.727  1.00 20.65 ? 2   ILE D O   1 
ATOM   4454 C  CB  . ILE D 1 14  ? 4.226   54.597  31.818  1.00 27.41 ? 2   ILE D CB  1 
ATOM   4455 C  CG1 . ILE D 1 14  ? 4.538   53.273  32.501  1.00 21.26 ? 2   ILE D CG1 1 
ATOM   4456 C  CG2 . ILE D 1 14  ? 4.375   55.765  32.784  1.00 29.33 ? 2   ILE D CG2 1 
ATOM   4457 C  CD1 . ILE D 1 14  ? 6.000   52.991  32.558  1.00 25.93 ? 2   ILE D CD1 1 
ATOM   4458 N  N   . THR D 1 15  ? 2.938   53.577  29.018  1.00 19.82 ? 3   THR D N   1 
ATOM   4459 C  CA  . THR D 1 15  ? 2.666   52.597  27.978  1.00 22.95 ? 3   THR D CA  1 
ATOM   4460 C  C   . THR D 1 15  ? 3.899   52.258  27.152  1.00 21.00 ? 3   THR D C   1 
ATOM   4461 O  O   . THR D 1 15  ? 3.785   51.495  26.183  1.00 20.54 ? 3   THR D O   1 
ATOM   4462 C  CB  . THR D 1 15  ? 1.554   53.103  27.045  1.00 25.64 ? 3   THR D CB  1 
ATOM   4463 O  OG1 . THR D 1 15  ? 1.926   54.388  26.533  1.00 33.64 ? 3   THR D OG1 1 
ATOM   4464 C  CG2 . THR D 1 15  ? 0.232   53.249  27.809  1.00 25.82 ? 3   THR D CG2 1 
ATOM   4465 N  N   . SER D 1 16  ? 5.060   52.806  27.504  1.00 17.77 ? 4   SER D N   1 
ATOM   4466 C  CA  . SER D 1 16  ? 6.337   52.502  26.882  1.00 22.37 ? 4   SER D CA  1 
ATOM   4467 C  C   . SER D 1 16  ? 7.341   52.158  27.975  1.00 18.05 ? 4   SER D C   1 
ATOM   4468 O  O   . SER D 1 16  ? 7.218   52.619  29.112  1.00 19.31 ? 4   SER D O   1 
ATOM   4469 C  CB  . SER D 1 16  ? 6.855   53.690  26.056  1.00 29.36 ? 4   SER D CB  1 
ATOM   4470 O  OG  . SER D 1 16  ? 6.080   53.848  24.876  1.00 30.27 ? 4   SER D OG  1 
ATOM   4471 N  N   . SER D 1 17  ? 8.356   51.381  27.603  1.00 19.02 ? 5   SER D N   1 
ATOM   4472 C  CA  . SER D 1 17  ? 9.313   50.859  28.578  1.00 17.79 ? 5   SER D CA  1 
ATOM   4473 C  C   . SER D 1 17  ? 9.980   51.972  29.382  1.00 21.94 ? 5   SER D C   1 
ATOM   4474 O  O   . SER D 1 17  ? 10.290  53.051  28.863  1.00 19.69 ? 5   SER D O   1 
ATOM   4475 C  CB  . SER D 1 17  ? 10.379  50.010  27.888  1.00 17.96 ? 5   SER D CB  1 
ATOM   4476 O  OG  . SER D 1 17  ? 9.801   49.135  26.936  1.00 18.74 ? 5   SER D OG  1 
ATOM   4477 N  N   . GLU D 1 18  ? 10.210  51.687  30.662  1.00 16.49 ? 6   GLU D N   1 
ATOM   4478 C  CA  . GLU D 1 18  ? 10.699  52.661  31.629  1.00 18.57 ? 6   GLU D CA  1 
ATOM   4479 C  C   . GLU D 1 18  ? 11.199  51.917  32.857  1.00 18.71 ? 6   GLU D C   1 
ATOM   4480 O  O   . GLU D 1 18  ? 10.619  50.901  33.237  1.00 16.81 ? 6   GLU D O   1 
ATOM   4481 C  CB  . GLU D 1 18  ? 9.573   53.622  32.022  1.00 20.35 ? 6   GLU D CB  1 
ATOM   4482 C  CG  . GLU D 1 18  ? 9.964   54.808  32.865  1.00 26.35 ? 6   GLU D CG  1 
ATOM   4483 C  CD  . GLU D 1 18  ? 8.760   55.688  33.156  1.00 32.64 ? 6   GLU D CD  1 
ATOM   4484 O  OE1 . GLU D 1 18  ? 8.251   55.648  34.301  1.00 32.01 ? 6   GLU D OE1 1 
ATOM   4485 O  OE2 . GLU D 1 18  ? 8.301   56.393  32.220  1.00 31.11 ? 6   GLU D OE2 1 
ATOM   4486 N  N   . THR D 1 19  ? 12.259  52.432  33.478  1.00 13.12 ? 7   THR D N   1 
ATOM   4487 C  CA  . THR D 1 19  ? 12.652  51.987  34.806  1.00 14.49 ? 7   THR D CA  1 
ATOM   4488 C  C   . THR D 1 19  ? 12.789  53.201  35.711  1.00 16.40 ? 7   THR D C   1 
ATOM   4489 O  O   . THR D 1 19  ? 12.839  54.344  35.245  1.00 13.98 ? 7   THR D O   1 
ATOM   4490 C  CB  . THR D 1 19  ? 13.968  51.197  34.799  1.00 15.29 ? 7   THR D CB  1 
ATOM   4491 O  OG1 . THR D 1 19  ? 15.053  52.082  34.498  1.00 15.33 ? 7   THR D OG1 1 
ATOM   4492 C  CG2 . THR D 1 19  ? 13.936  50.054  33.767  1.00 13.34 ? 7   THR D CG2 1 
ATOM   4493 N  N   . GLY D 1 20  ? 12.859  52.944  37.013  1.00 11.62 ? 8   GLY D N   1 
ATOM   4494 C  CA  . GLY D 1 20  ? 13.000  54.035  37.957  1.00 13.72 ? 8   GLY D CA  1 
ATOM   4495 C  C   . GLY D 1 20  ? 12.845  53.547  39.381  1.00 14.77 ? 8   GLY D C   1 
ATOM   4496 O  O   . GLY D 1 20  ? 12.961  52.354  39.656  1.00 12.93 ? 8   GLY D O   1 
ATOM   4497 N  N   . THR D 1 21  ? 12.605  54.501  40.281  1.00 17.85 ? 9   THR D N   1 
ATOM   4498 C  CA  . THR D 1 21  ? 12.276  54.240  41.673  1.00 17.23 ? 9   THR D CA  1 
ATOM   4499 C  C   . THR D 1 21  ? 10.921  54.849  41.969  1.00 20.35 ? 9   THR D C   1 
ATOM   4500 O  O   . THR D 1 21  ? 10.635  55.973  41.546  1.00 20.62 ? 9   THR D O   1 
ATOM   4501 C  CB  . THR D 1 21  ? 13.292  54.860  42.650  1.00 22.59 ? 9   THR D CB  1 
ATOM   4502 O  OG1 . THR D 1 21  ? 14.611  54.762  42.116  1.00 28.24 ? 9   THR D OG1 1 
ATOM   4503 C  CG2 . THR D 1 21  ? 13.225  54.168  43.994  1.00 18.77 ? 9   THR D CG2 1 
ATOM   4504 N  N   . ASN D 1 22  ? 10.094  54.121  42.713  1.00 19.85 ? 10  ASN D N   1 
ATOM   4505 C  CA  . ASN D 1 22  ? 8.772   54.616  43.069  1.00 18.57 ? 10  ASN D CA  1 
ATOM   4506 C  C   . ASN D 1 22  ? 8.444   54.165  44.480  1.00 19.89 ? 10  ASN D C   1 
ATOM   4507 O  O   . ASN D 1 22  ? 8.432   52.965  44.763  1.00 18.72 ? 10  ASN D O   1 
ATOM   4508 C  CB  . ASN D 1 22  ? 7.715   54.128  42.077  1.00 17.73 ? 10  ASN D CB  1 
ATOM   4509 C  CG  . ASN D 1 22  ? 6.317   54.572  42.455  1.00 19.88 ? 10  ASN D CG  1 
ATOM   4510 O  OD1 . ASN D 1 22  ? 5.570   53.824  43.075  1.00 20.82 ? 10  ASN D OD1 1 
ATOM   4511 N  ND2 . ASN D 1 22  ? 5.954   55.798  42.074  1.00 23.43 ? 10  ASN D ND2 1 
ATOM   4512 N  N   . ASN D 1 23  ? 8.201   55.133  45.365  1.00 23.86 ? 11  ASN D N   1 
ATOM   4513 C  CA  . ASN D 1 23  ? 7.848   54.869  46.765  1.00 23.31 ? 11  ASN D CA  1 
ATOM   4514 C  C   . ASN D 1 23  ? 8.812   53.887  47.430  1.00 22.34 ? 11  ASN D C   1 
ATOM   4515 O  O   . ASN D 1 23  ? 8.411   53.001  48.191  1.00 23.15 ? 11  ASN D O   1 
ATOM   4516 C  CB  . ASN D 1 23  ? 6.399   54.389  46.864  1.00 24.00 ? 11  ASN D CB  1 
ATOM   4517 C  CG  . ASN D 1 23  ? 5.418   55.467  46.464  1.00 28.10 ? 11  ASN D CG  1 
ATOM   4518 O  OD1 . ASN D 1 23  ? 5.575   56.625  46.853  1.00 30.97 ? 11  ASN D OD1 1 
ATOM   4519 N  ND2 . ASN D 1 23  ? 4.417   55.109  45.664  1.00 26.52 ? 11  ASN D ND2 1 
ATOM   4520 N  N   . GLY D 1 24  ? 10.106  54.049  47.146  1.00 23.50 ? 12  GLY D N   1 
ATOM   4521 C  CA  . GLY D 1 24  ? 11.138  53.259  47.779  1.00 23.30 ? 12  GLY D CA  1 
ATOM   4522 C  C   . GLY D 1 24  ? 11.482  51.957  47.093  1.00 19.51 ? 12  GLY D C   1 
ATOM   4523 O  O   . GLY D 1 24  ? 12.377  51.244  47.568  1.00 25.38 ? 12  GLY D O   1 
ATOM   4524 N  N   . TYR D 1 25  ? 10.803  51.619  46.004  1.00 17.85 ? 13  TYR D N   1 
ATOM   4525 C  CA  . TYR D 1 25  ? 11.042  50.386  45.265  1.00 16.82 ? 13  TYR D CA  1 
ATOM   4526 C  C   . TYR D 1 25  ? 11.516  50.697  43.856  1.00 13.40 ? 13  TYR D C   1 
ATOM   4527 O  O   . TYR D 1 25  ? 10.999  51.611  43.205  1.00 17.27 ? 13  TYR D O   1 
ATOM   4528 C  CB  . TYR D 1 25  ? 9.777   49.541  45.177  1.00 16.34 ? 13  TYR D CB  1 
ATOM   4529 C  CG  . TYR D 1 25  ? 9.442   48.875  46.482  1.00 14.18 ? 13  TYR D CG  1 
ATOM   4530 C  CD1 . TYR D 1 25  ? 9.953   47.623  46.784  1.00 18.51 ? 13  TYR D CD1 1 
ATOM   4531 C  CD2 . TYR D 1 25  ? 8.640   49.510  47.424  1.00 18.42 ? 13  TYR D CD2 1 
ATOM   4532 C  CE1 . TYR D 1 25  ? 9.667   47.007  47.979  1.00 21.90 ? 13  TYR D CE1 1 
ATOM   4533 C  CE2 . TYR D 1 25  ? 8.345   48.896  48.640  1.00 19.25 ? 13  TYR D CE2 1 
ATOM   4534 C  CZ  . TYR D 1 25  ? 8.864   47.645  48.903  1.00 25.12 ? 13  TYR D CZ  1 
ATOM   4535 O  OH  . TYR D 1 25  ? 8.590   47.009  50.087  1.00 29.38 ? 13  TYR D OH  1 
ATOM   4536 N  N   . TYR D 1 26  ? 12.502  49.924  43.403  1.00 11.73 ? 14  TYR D N   1 
ATOM   4537 C  CA  . TYR D 1 26  ? 12.860  49.892  41.994  1.00 11.13 ? 14  TYR D CA  1 
ATOM   4538 C  C   . TYR D 1 26  ? 11.693  49.338  41.194  1.00 13.31 ? 14  TYR D C   1 
ATOM   4539 O  O   . TYR D 1 26  ? 10.971  48.453  41.660  1.00 11.92 ? 14  TYR D O   1 
ATOM   4540 C  CB  . TYR D 1 26  ? 14.096  49.010  41.790  1.00 11.60 ? 14  TYR D CB  1 
ATOM   4541 C  CG  . TYR D 1 26  ? 14.531  48.840  40.348  1.00 12.39 ? 14  TYR D CG  1 
ATOM   4542 C  CD1 . TYR D 1 26  ? 15.277  49.826  39.715  1.00 11.55 ? 14  TYR D CD1 1 
ATOM   4543 C  CD2 . TYR D 1 26  ? 14.216  47.689  39.624  1.00 13.27 ? 14  TYR D CD2 1 
ATOM   4544 C  CE1 . TYR D 1 26  ? 15.691  49.685  38.409  1.00 13.61 ? 14  TYR D CE1 1 
ATOM   4545 C  CE2 . TYR D 1 26  ? 14.626  47.538  38.298  1.00 12.87 ? 14  TYR D CE2 1 
ATOM   4546 C  CZ  . TYR D 1 26  ? 15.374  48.544  37.701  1.00 13.92 ? 14  TYR D CZ  1 
ATOM   4547 O  OH  . TYR D 1 26  ? 15.802  48.439  36.397  1.00 15.31 ? 14  TYR D OH  1 
ATOM   4548 N  N   . TYR D 1 27  ? 11.494  49.863  39.992  1.00 11.73 ? 15  TYR D N   1 
ATOM   4549 C  CA  . TYR D 1 27  ? 10.507  49.271  39.101  1.00 12.46 ? 15  TYR D CA  1 
ATOM   4550 C  C   . TYR D 1 27  ? 11.089  49.166  37.704  1.00 14.84 ? 15  TYR D C   1 
ATOM   4551 O  O   . TYR D 1 27  ? 11.931  49.970  37.291  1.00 12.48 ? 15  TYR D O   1 
ATOM   4552 C  CB  . TYR D 1 27  ? 9.186   50.057  39.085  1.00 10.87 ? 15  TYR D CB  1 
ATOM   4553 C  CG  . TYR D 1 27  ? 9.240   51.410  38.399  1.00 11.96 ? 15  TYR D CG  1 
ATOM   4554 C  CD1 . TYR D 1 27  ? 9.592   52.550  39.108  1.00 14.24 ? 15  TYR D CD1 1 
ATOM   4555 C  CD2 . TYR D 1 27  ? 8.921   51.546  37.053  1.00 12.82 ? 15  TYR D CD2 1 
ATOM   4556 C  CE1 . TYR D 1 27  ? 9.643   53.794  38.488  1.00 14.59 ? 15  TYR D CE1 1 
ATOM   4557 C  CE2 . TYR D 1 27  ? 8.961   52.790  36.430  1.00 18.23 ? 15  TYR D CE2 1 
ATOM   4558 C  CZ  . TYR D 1 27  ? 9.328   53.904  37.156  1.00 17.95 ? 15  TYR D CZ  1 
ATOM   4559 O  OH  . TYR D 1 27  ? 9.382   55.136  36.538  1.00 18.72 ? 15  TYR D OH  1 
ATOM   4560 N  N   . SER D 1 28  ? 10.646  48.141  36.987  1.00 9.98  ? 16  SER D N   1 
ATOM   4561 C  CA  . SER D 1 28  ? 11.032  47.958  35.603  1.00 11.66 ? 16  SER D CA  1 
ATOM   4562 C  C   . SER D 1 28  ? 9.785   47.592  34.828  1.00 12.80 ? 16  SER D C   1 
ATOM   4563 O  O   . SER D 1 28  ? 9.060   46.667  35.210  1.00 12.32 ? 16  SER D O   1 
ATOM   4564 C  CB  . SER D 1 28  ? 12.091  46.859  35.444  1.00 12.45 ? 16  SER D CB  1 
ATOM   4565 O  OG  . SER D 1 28  ? 12.370  46.670  34.065  1.00 13.62 ? 16  SER D OG  1 
ATOM   4566 N  N   . PHE D 1 29  ? 9.521   48.345  33.771  1.00 11.76 ? 17  PHE D N   1 
ATOM   4567 C  CA  . PHE D 1 29  ? 8.447   48.037  32.842  1.00 12.95 ? 17  PHE D CA  1 
ATOM   4568 C  C   . PHE D 1 29  ? 9.074   47.958  31.463  1.00 14.73 ? 17  PHE D C   1 
ATOM   4569 O  O   . PHE D 1 29  ? 9.706   48.919  31.010  1.00 14.53 ? 17  PHE D O   1 
ATOM   4570 C  CB  . PHE D 1 29  ? 7.350   49.105  32.883  1.00 11.14 ? 17  PHE D CB  1 
ATOM   4571 C  CG  . PHE D 1 29  ? 6.318   48.951  31.806  1.00 14.13 ? 17  PHE D CG  1 
ATOM   4572 C  CD1 . PHE D 1 29  ? 5.580   47.788  31.702  1.00 14.76 ? 17  PHE D CD1 1 
ATOM   4573 C  CD2 . PHE D 1 29  ? 6.079   49.975  30.904  1.00 15.30 ? 17  PHE D CD2 1 
ATOM   4574 C  CE1 . PHE D 1 29  ? 4.608   47.648  30.709  1.00 13.04 ? 17  PHE D CE1 1 
ATOM   4575 C  CE2 . PHE D 1 29  ? 5.115   49.849  29.913  1.00 16.59 ? 17  PHE D CE2 1 
ATOM   4576 C  CZ  . PHE D 1 29  ? 4.379   48.676  29.812  1.00 14.76 ? 17  PHE D CZ  1 
ATOM   4577 N  N   . TRP D 1 30  ? 8.933   46.813  30.807  1.00 12.57 ? 18  TRP D N   1 
ATOM   4578 C  CA  . TRP D 1 30  ? 9.421   46.665  29.443  1.00 12.61 ? 18  TRP D CA  1 
ATOM   4579 C  C   . TRP D 1 30  ? 8.299   46.118  28.579  1.00 15.26 ? 18  TRP D C   1 
ATOM   4580 O  O   . TRP D 1 30  ? 7.631   45.155  28.967  1.00 13.31 ? 18  TRP D O   1 
ATOM   4581 C  CB  . TRP D 1 30  ? 10.638  45.736  29.391  1.00 16.82 ? 18  TRP D CB  1 
ATOM   4582 C  CG  . TRP D 1 30  ? 11.076  45.440  27.996  1.00 17.40 ? 18  TRP D CG  1 
ATOM   4583 C  CD1 . TRP D 1 30  ? 11.872  46.221  27.205  1.00 20.96 ? 18  TRP D CD1 1 
ATOM   4584 C  CD2 . TRP D 1 30  ? 10.739  44.287  27.217  1.00 17.51 ? 18  TRP D CD2 1 
ATOM   4585 N  NE1 . TRP D 1 30  ? 12.047  45.622  25.979  1.00 21.19 ? 18  TRP D NE1 1 
ATOM   4586 C  CE2 . TRP D 1 30  ? 11.368  44.433  25.963  1.00 20.35 ? 18  TRP D CE2 1 
ATOM   4587 C  CE3 . TRP D 1 30  ? 9.968   43.143  27.459  1.00 16.50 ? 18  TRP D CE3 1 
ATOM   4588 C  CZ2 . TRP D 1 30  ? 11.239  43.483  24.944  1.00 21.72 ? 18  TRP D CZ2 1 
ATOM   4589 C  CZ3 . TRP D 1 30  ? 9.852   42.191  26.454  1.00 22.40 ? 18  TRP D CZ3 1 
ATOM   4590 C  CH2 . TRP D 1 30  ? 10.482  42.370  25.210  1.00 20.46 ? 18  TRP D CH2 1 
ATOM   4591 N  N   . THR D 1 31  ? 8.080   46.731  27.420  1.00 12.51 ? 19  THR D N   1 
ATOM   4592 C  CA  . THR D 1 31  ? 7.169   46.154  26.436  1.00 13.21 ? 19  THR D CA  1 
ATOM   4593 C  C   . THR D 1 31  ? 7.791   46.291  25.056  1.00 17.18 ? 19  THR D C   1 
ATOM   4594 O  O   . THR D 1 31  ? 8.496   47.265  24.771  1.00 19.76 ? 19  THR D O   1 
ATOM   4595 C  CB  . THR D 1 31  ? 5.771   46.806  26.465  1.00 14.23 ? 19  THR D CB  1 
ATOM   4596 O  OG1 . THR D 1 31  ? 4.997   46.309  25.362  1.00 16.51 ? 19  THR D OG1 1 
ATOM   4597 C  CG2 . THR D 1 31  ? 5.873   48.333  26.365  1.00 17.22 ? 19  THR D CG2 1 
ATOM   4598 N  N   . ASP D 1 32  ? 7.544   45.294  24.201  1.00 16.19 ? 20  ASP D N   1 
ATOM   4599 C  CA  . ASP D 1 32  ? 8.019   45.377  22.827  1.00 19.20 ? 20  ASP D CA  1 
ATOM   4600 C  C   . ASP D 1 32  ? 7.126   46.247  21.946  1.00 19.58 ? 20  ASP D C   1 
ATOM   4601 O  O   . ASP D 1 32  ? 7.400   46.367  20.748  1.00 23.39 ? 20  ASP D O   1 
ATOM   4602 C  CB  . ASP D 1 32  ? 8.175   43.969  22.220  1.00 21.62 ? 20  ASP D CB  1 
ATOM   4603 C  CG  . ASP D 1 32  ? 6.836   43.245  22.014  1.00 21.86 ? 20  ASP D CG  1 
ATOM   4604 O  OD1 . ASP D 1 32  ? 5.773   43.843  22.271  1.00 21.51 ? 20  ASP D OD1 1 
ATOM   4605 O  OD2 . ASP D 1 32  ? 6.849   42.065  21.589  1.00 22.47 ? 20  ASP D OD2 1 
ATOM   4606 N  N   . GLY D 1 33  ? 6.067   46.846  22.504  1.00 19.53 ? 21  GLY D N   1 
ATOM   4607 C  CA  . GLY D 1 33  ? 5.221   47.772  21.777  1.00 21.05 ? 21  GLY D CA  1 
ATOM   4608 C  C   . GLY D 1 33  ? 3.973   47.172  21.157  1.00 21.76 ? 21  GLY D C   1 
ATOM   4609 O  O   . GLY D 1 33  ? 3.139   47.927  20.640  1.00 22.48 ? 21  GLY D O   1 
ATOM   4610 N  N   . GLY D 1 34  ? 3.804   45.851  21.202  1.00 20.51 ? 22  GLY D N   1 
ATOM   4611 C  CA  . GLY D 1 34  ? 2.623   45.241  20.610  1.00 19.99 ? 22  GLY D CA  1 
ATOM   4612 C  C   . GLY D 1 34  ? 1.372   45.452  21.447  1.00 18.64 ? 22  GLY D C   1 
ATOM   4613 O  O   . GLY D 1 34  ? 1.417   45.500  22.676  1.00 19.96 ? 22  GLY D O   1 
ATOM   4614 N  N   . GLY D 1 35  ? 0.236   45.581  20.760  1.00 19.59 ? 23  GLY D N   1 
ATOM   4615 C  CA  . GLY D 1 35  ? -1.048  45.739  21.422  1.00 19.05 ? 23  GLY D CA  1 
ATOM   4616 C  C   . GLY D 1 35  ? -1.069  46.969  22.308  1.00 20.93 ? 23  GLY D C   1 
ATOM   4617 O  O   . GLY D 1 35  ? -0.449  47.996  22.012  1.00 21.23 ? 23  GLY D O   1 
ATOM   4618 N  N   . GLN D 1 36  ? -1.787  46.847  23.428  1.00 17.68 ? 24  GLN D N   1 
ATOM   4619 C  CA  . GLN D 1 36  ? -1.873  47.863  24.468  1.00 19.11 ? 24  GLN D CA  1 
ATOM   4620 C  C   . GLN D 1 36  ? -1.436  47.267  25.797  1.00 18.47 ? 24  GLN D C   1 
ATOM   4621 O  O   . GLN D 1 36  ? -1.983  46.251  26.223  1.00 17.00 ? 24  GLN D O   1 
ATOM   4622 C  CB  . GLN D 1 36  ? -3.293  48.392  24.586  1.00 24.77 ? 24  GLN D CB  1 
ATOM   4623 C  CG  . GLN D 1 36  ? -3.779  48.996  23.300  1.00 33.27 ? 24  GLN D CG  1 
ATOM   4624 C  CD  . GLN D 1 36  ? -2.798  49.928  22.600  1.00 42.20 ? 24  GLN D CD  1 
ATOM   4625 O  OE1 . GLN D 1 36  ? -2.143  50.778  23.289  1.00 46.37 ? 24  GLN D OE1 1 
ATOM   4626 N  NE2 . GLN D 1 36  ? -2.729  49.800  21.266  1.00 37.14 ? 24  GLN D NE2 1 
ATOM   4627 N  N   . VAL D 1 37  ? -0.446  47.887  26.439  1.00 16.64 ? 25  VAL D N   1 
ATOM   4628 C  CA  . VAL D 1 37  ? 0.016   47.462  27.762  1.00 16.04 ? 25  VAL D CA  1 
ATOM   4629 C  C   . VAL D 1 37  ? 0.191   48.718  28.597  1.00 19.02 ? 25  VAL D C   1 
ATOM   4630 O  O   . VAL D 1 37  ? 0.954   49.612  28.217  1.00 18.87 ? 25  VAL D O   1 
ATOM   4631 C  CB  . VAL D 1 37  ? 1.334   46.666  27.716  1.00 13.75 ? 25  VAL D CB  1 
ATOM   4632 C  CG1 . VAL D 1 37  ? 1.709   46.143  29.129  1.00 14.39 ? 25  VAL D CG1 1 
ATOM   4633 C  CG2 . VAL D 1 37  ? 1.241   45.504  26.720  1.00 16.90 ? 25  VAL D CG2 1 
ATOM   4634 N  N   . THR D 1 38  ? -0.509  48.792  29.728  1.00 15.05 ? 26  THR D N   1 
ATOM   4635 C  CA  . THR D 1 38  ? -0.535  49.995  30.547  1.00 15.58 ? 26  THR D CA  1 
ATOM   4636 C  C   . THR D 1 38  ? -0.075  49.641  31.950  1.00 15.12 ? 26  THR D C   1 
ATOM   4637 O  O   . THR D 1 38  ? -0.681  48.791  32.610  1.00 15.99 ? 26  THR D O   1 
ATOM   4638 C  CB  . THR D 1 38  ? -1.933  50.616  30.563  1.00 20.20 ? 26  THR D CB  1 
ATOM   4639 O  OG1 . THR D 1 38  ? -2.343  50.876  29.213  1.00 19.89 ? 26  THR D OG1 1 
ATOM   4640 C  CG2 . THR D 1 38  ? -1.927  51.920  31.339  1.00 24.76 ? 26  THR D CG2 1 
ATOM   4641 N  N   . TYR D 1 39  ? 0.999   50.288  32.391  1.00 15.11 ? 27  TYR D N   1 
ATOM   4642 C  CA  . TYR D 1 39  ? 1.617   50.043  33.681  1.00 12.37 ? 27  TYR D CA  1 
ATOM   4643 C  C   . TYR D 1 39  ? 1.378   51.241  34.588  1.00 16.42 ? 27  TYR D C   1 
ATOM   4644 O  O   . TYR D 1 39  ? 1.511   52.389  34.160  1.00 17.38 ? 27  TYR D O   1 
ATOM   4645 C  CB  . TYR D 1 39  ? 3.123   49.795  33.495  1.00 11.08 ? 27  TYR D CB  1 
ATOM   4646 C  CG  . TYR D 1 39  ? 3.888   49.675  34.785  1.00 12.39 ? 27  TYR D CG  1 
ATOM   4647 C  CD1 . TYR D 1 39  ? 4.439   50.787  35.404  1.00 15.27 ? 27  TYR D CD1 1 
ATOM   4648 C  CD2 . TYR D 1 39  ? 4.034   48.442  35.394  1.00 12.44 ? 27  TYR D CD2 1 
ATOM   4649 C  CE1 . TYR D 1 39  ? 5.133   50.664  36.598  1.00 13.92 ? 27  TYR D CE1 1 
ATOM   4650 C  CE2 . TYR D 1 39  ? 4.721   48.301  36.576  1.00 15.66 ? 27  TYR D CE2 1 
ATOM   4651 C  CZ  . TYR D 1 39  ? 5.272   49.413  37.174  1.00 15.91 ? 27  TYR D CZ  1 
ATOM   4652 O  OH  . TYR D 1 39  ? 5.950   49.261  38.354  1.00 12.87 ? 27  TYR D OH  1 
ATOM   4653 N  N   . THR D 1 40  ? 1.031   50.987  35.846  1.00 13.12 ? 28  THR D N   1 
ATOM   4654 C  CA  . THR D 1 40  ? 0.849   52.076  36.795  1.00 15.51 ? 28  THR D CA  1 
ATOM   4655 C  C   . THR D 1 40  ? 1.500   51.744  38.125  1.00 18.06 ? 28  THR D C   1 
ATOM   4656 O  O   . THR D 1 40  ? 1.265   50.671  38.685  1.00 19.39 ? 28  THR D O   1 
ATOM   4657 C  CB  . THR D 1 40  ? -0.630  52.386  37.007  1.00 24.78 ? 28  THR D CB  1 
ATOM   4658 O  OG1 . THR D 1 40  ? -1.264  52.558  35.734  1.00 29.49 ? 28  THR D OG1 1 
ATOM   4659 C  CG2 . THR D 1 40  ? -0.767  53.668  37.798  1.00 29.33 ? 28  THR D CG2 1 
ATOM   4660 N  N   . ASN D 1 41  ? 2.298   52.677  38.633  1.00 12.95 ? 29  ASN D N   1 
ATOM   4661 C  CA  . ASN D 1 41  ? 2.884   52.534  39.955  1.00 16.06 ? 29  ASN D CA  1 
ATOM   4662 C  C   . ASN D 1 41  ? 1.858   52.903  41.013  1.00 20.81 ? 29  ASN D C   1 
ATOM   4663 O  O   . ASN D 1 41  ? 1.079   53.846  40.841  1.00 22.99 ? 29  ASN D O   1 
ATOM   4664 C  CB  . ASN D 1 41  ? 4.117   53.425  40.077  1.00 19.03 ? 29  ASN D CB  1 
ATOM   4665 C  CG  . ASN D 1 41  ? 5.363   52.765  39.529  1.00 16.16 ? 29  ASN D CG  1 
ATOM   4666 O  OD1 . ASN D 1 41  ? 5.603   51.585  39.776  1.00 15.43 ? 29  ASN D OD1 1 
ATOM   4667 N  ND2 . ASN D 1 41  ? 6.163   53.520  38.775  1.00 20.83 ? 29  ASN D ND2 1 
ATOM   4668 N  N   . GLY D 1 42  ? 1.844   52.139  42.096  1.00 17.17 ? 30  GLY D N   1 
ATOM   4669 C  CA  . GLY D 1 42  ? 0.983   52.430  43.216  1.00 21.76 ? 30  GLY D CA  1 
ATOM   4670 C  C   . GLY D 1 42  ? 1.779   52.718  44.474  1.00 20.11 ? 30  GLY D C   1 
ATOM   4671 O  O   . GLY D 1 42  ? 3.015   52.779  44.459  1.00 20.82 ? 30  GLY D O   1 
ATOM   4672 N  N   . PRO D 1 43  ? 1.083   52.887  45.594  1.00 20.23 ? 31  PRO D N   1 
ATOM   4673 C  CA  . PRO D 1 43  ? 1.777   53.194  46.850  1.00 21.71 ? 31  PRO D CA  1 
ATOM   4674 C  C   . PRO D 1 43  ? 2.643   52.035  47.329  1.00 21.87 ? 31  PRO D C   1 
ATOM   4675 O  O   . PRO D 1 43  ? 2.330   50.861  47.114  1.00 20.53 ? 31  PRO D O   1 
ATOM   4676 C  CB  . PRO D 1 43  ? 0.626   53.479  47.824  1.00 25.04 ? 31  PRO D CB  1 
ATOM   4677 C  CG  . PRO D 1 43  ? -0.535  52.757  47.258  1.00 27.91 ? 31  PRO D CG  1 
ATOM   4678 C  CD  . PRO D 1 43  ? -0.383  52.854  45.763  1.00 25.16 ? 31  PRO D CD  1 
ATOM   4679 N  N   . ALA D 1 44  ? 3.749   52.387  47.994  1.00 22.00 ? 32  ALA D N   1 
ATOM   4680 C  CA  . ALA D 1 44  ? 4.731   51.431  48.554  1.00 23.19 ? 32  ALA D CA  1 
ATOM   4681 C  C   . ALA D 1 44  ? 5.136   50.462  47.438  1.00 19.01 ? 32  ALA D C   1 
ATOM   4682 O  O   . ALA D 1 44  ? 5.523   50.906  46.346  1.00 17.77 ? 32  ALA D O   1 
ATOM   4683 C  CB  . ALA D 1 44  ? 4.160   50.780  49.802  1.00 27.79 ? 32  ALA D CB  1 
ATOM   4684 N  N   . GLY D 1 45  ? 5.056   49.149  47.652  1.00 21.31 ? 33  GLY D N   1 
ATOM   4685 C  CA  . GLY D 1 45  ? 5.540   48.216  46.661  1.00 16.21 ? 33  GLY D CA  1 
ATOM   4686 C  C   . GLY D 1 45  ? 4.508   47.718  45.671  1.00 15.75 ? 33  GLY D C   1 
ATOM   4687 O  O   . GLY D 1 45  ? 4.709   46.663  45.065  1.00 15.10 ? 33  GLY D O   1 
ATOM   4688 N  N   . GLN D 1 46  ? 3.424   48.468  45.474  1.00 15.16 ? 34  GLN D N   1 
ATOM   4689 C  CA  . GLN D 1 46  ? 2.335   48.050  44.597  1.00 14.54 ? 34  GLN D CA  1 
ATOM   4690 C  C   . GLN D 1 46  ? 2.560   48.534  43.175  1.00 15.76 ? 34  GLN D C   1 
ATOM   4691 O  O   . GLN D 1 46  ? 3.039   49.650  42.947  1.00 13.95 ? 34  GLN D O   1 
ATOM   4692 C  CB  . GLN D 1 46  ? 0.993   48.595  45.094  1.00 17.40 ? 34  GLN D CB  1 
ATOM   4693 C  CG  . GLN D 1 46  ? -0.237  47.888  44.494  1.00 18.14 ? 34  GLN D CG  1 
ATOM   4694 C  CD  . GLN D 1 46  ? -0.796  48.547  43.231  1.00 26.39 ? 34  GLN D CD  1 
ATOM   4695 O  OE1 . GLN D 1 46  ? -0.260  49.539  42.736  1.00 29.49 ? 34  GLN D OE1 1 
ATOM   4696 N  NE2 . GLN D 1 46  ? -1.891  47.989  42.705  1.00 29.05 ? 34  GLN D NE2 1 
ATOM   4697 N  N   . TYR D 1 47  ? 2.185   47.693  42.216  1.00 13.28 ? 35  TYR D N   1 
ATOM   4698 C  CA  . TYR D 1 47  ? 2.038   48.127  40.837  1.00 11.51 ? 35  TYR D CA  1 
ATOM   4699 C  C   . TYR D 1 47  ? 0.841   47.409  40.227  1.00 13.95 ? 35  TYR D C   1 
ATOM   4700 O  O   . TYR D 1 47  ? 0.363   46.400  40.750  1.00 12.86 ? 35  TYR D O   1 
ATOM   4701 C  CB  . TYR D 1 47  ? 3.307   47.848  40.018  1.00 12.17 ? 35  TYR D CB  1 
ATOM   4702 C  CG  . TYR D 1 47  ? 3.541   46.372  39.766  1.00 12.40 ? 35  TYR D CG  1 
ATOM   4703 C  CD1 . TYR D 1 47  ? 4.247   45.595  40.668  1.00 10.66 ? 35  TYR D CD1 1 
ATOM   4704 C  CD2 . TYR D 1 47  ? 3.041   45.759  38.622  1.00 11.15 ? 35  TYR D CD2 1 
ATOM   4705 C  CE1 . TYR D 1 47  ? 4.447   44.237  40.442  1.00 9.54  ? 35  TYR D CE1 1 
ATOM   4706 C  CE2 . TYR D 1 47  ? 3.237   44.404  38.386  1.00 12.26 ? 35  TYR D CE2 1 
ATOM   4707 C  CZ  . TYR D 1 47  ? 3.947   43.654  39.291  1.00 10.48 ? 35  TYR D CZ  1 
ATOM   4708 O  OH  . TYR D 1 47  ? 4.163   42.305  39.085  1.00 11.44 ? 35  TYR D OH  1 
ATOM   4709 N  N   . SER D 1 48  ? 0.364   47.935  39.103  1.00 12.16 ? 36  SER D N   1 
ATOM   4710 C  CA  . SER D 1 48  ? -0.689  47.290  38.332  1.00 14.59 ? 36  SER D CA  1 
ATOM   4711 C  C   . SER D 1 48  ? -0.336  47.330  36.857  1.00 14.12 ? 36  SER D C   1 
ATOM   4712 O  O   . SER D 1 48  ? 0.320   48.259  36.382  1.00 16.25 ? 36  SER D O   1 
ATOM   4713 C  CB  . SER D 1 48  ? -2.071  47.962  38.513  1.00 17.00 ? 36  SER D CB  1 
ATOM   4714 O  OG  . SER D 1 48  ? -2.367  48.193  39.876  1.00 25.70 ? 36  SER D OG  1 
ATOM   4715 N  N   . VAL D 1 49  ? -0.804  46.332  36.128  1.00 12.99 ? 37  VAL D N   1 
ATOM   4716 C  CA  . VAL D 1 49  ? -0.633  46.298  34.683  1.00 13.24 ? 37  VAL D CA  1 
ATOM   4717 C  C   . VAL D 1 49  ? -1.919  45.773  34.069  1.00 16.94 ? 37  VAL D C   1 
ATOM   4718 O  O   . VAL D 1 49  ? -2.556  44.861  34.607  1.00 16.27 ? 37  VAL D O   1 
ATOM   4719 C  CB  . VAL D 1 49  ? 0.601   45.464  34.264  1.00 16.62 ? 37  VAL D CB  1 
ATOM   4720 C  CG1 . VAL D 1 49  ? 0.495   44.026  34.743  1.00 17.43 ? 37  VAL D CG1 1 
ATOM   4721 C  CG2 . VAL D 1 49  ? 0.820   45.540  32.755  1.00 13.97 ? 37  VAL D CG2 1 
ATOM   4722 N  N   . GLU D 1 50  ? -2.338  46.402  32.979  1.00 14.49 ? 38  GLU D N   1 
ATOM   4723 C  CA  . GLU D 1 50  ? -3.502  45.981  32.222  1.00 15.26 ? 38  GLU D CA  1 
ATOM   4724 C  C   . GLU D 1 50  ? -3.075  45.878  30.770  1.00 15.03 ? 38  GLU D C   1 
ATOM   4725 O  O   . GLU D 1 50  ? -2.354  46.747  30.269  1.00 16.02 ? 38  GLU D O   1 
ATOM   4726 C  CB  . GLU D 1 50  ? -4.660  46.978  32.378  1.00 16.74 ? 38  GLU D CB  1 
ATOM   4727 C  CG  . GLU D 1 50  ? -6.034  46.435  32.057  1.00 31.84 ? 38  GLU D CG  1 
ATOM   4728 C  CD  . GLU D 1 50  ? -7.105  47.037  32.962  1.00 44.04 ? 38  GLU D CD  1 
ATOM   4729 O  OE1 . GLU D 1 50  ? -7.033  48.258  33.228  1.00 49.77 ? 38  GLU D OE1 1 
ATOM   4730 O  OE2 . GLU D 1 50  ? -7.997  46.291  33.427  1.00 43.79 ? 38  GLU D OE2 1 
ATOM   4731 N  N   . TRP D 1 51  ? -3.492  44.815  30.097  1.00 13.93 ? 39  TRP D N   1 
ATOM   4732 C  CA  . TRP D 1 51  ? -3.014  44.624  28.739  1.00 13.61 ? 39  TRP D CA  1 
ATOM   4733 C  C   . TRP D 1 51  ? -4.092  44.002  27.867  1.00 15.26 ? 39  TRP D C   1 
ATOM   4734 O  O   . TRP D 1 51  ? -5.008  43.325  28.347  1.00 11.84 ? 39  TRP D O   1 
ATOM   4735 C  CB  . TRP D 1 51  ? -1.712  43.790  28.719  1.00 12.61 ? 39  TRP D CB  1 
ATOM   4736 C  CG  . TRP D 1 51  ? -1.785  42.329  29.165  1.00 12.13 ? 39  TRP D CG  1 
ATOM   4737 C  CD1 . TRP D 1 51  ? -1.846  41.235  28.348  1.00 12.68 ? 39  TRP D CD1 1 
ATOM   4738 C  CD2 . TRP D 1 51  ? -1.737  41.822  30.510  1.00 12.88 ? 39  TRP D CD2 1 
ATOM   4739 N  NE1 . TRP D 1 51  ? -1.843  40.079  29.100  1.00 11.87 ? 39  TRP D NE1 1 
ATOM   4740 C  CE2 . TRP D 1 51  ? -1.790  40.413  30.428  1.00 11.13 ? 39  TRP D CE2 1 
ATOM   4741 C  CE3 . TRP D 1 51  ? -1.658  42.424  31.773  1.00 11.83 ? 39  TRP D CE3 1 
ATOM   4742 C  CZ2 . TRP D 1 51  ? -1.757  39.592  31.557  1.00 13.94 ? 39  TRP D CZ2 1 
ATOM   4743 C  CZ3 . TRP D 1 51  ? -1.630  41.598  32.903  1.00 12.37 ? 39  TRP D CZ3 1 
ATOM   4744 C  CH2 . TRP D 1 51  ? -1.689  40.202  32.783  1.00 11.88 ? 39  TRP D CH2 1 
ATOM   4745 N  N   . SER D 1 52  ? -3.975  44.273  26.570  1.00 15.87 ? 40  SER D N   1 
ATOM   4746 C  CA  . SER D 1 52  ? -4.947  43.840  25.575  1.00 17.26 ? 40  SER D CA  1 
ATOM   4747 C  C   . SER D 1 52  ? -4.189  43.465  24.310  1.00 19.48 ? 40  SER D C   1 
ATOM   4748 O  O   . SER D 1 52  ? -3.484  44.309  23.741  1.00 16.44 ? 40  SER D O   1 
ATOM   4749 C  CB  . SER D 1 52  ? -5.970  44.951  25.295  1.00 19.82 ? 40  SER D CB  1 
ATOM   4750 O  OG  . SER D 1 52  ? -6.902  44.548  24.301  1.00 27.67 ? 40  SER D OG  1 
ATOM   4751 N  N   . ASN D 1 53  ? -4.309  42.199  23.896  1.00 16.56 ? 41  ASN D N   1 
ATOM   4752 C  CA  . ASN D 1 53  ? -3.703  41.700  22.657  1.00 16.72 ? 41  ASN D CA  1 
ATOM   4753 C  C   . ASN D 1 53  ? -2.232  42.085  22.559  1.00 15.44 ? 41  ASN D C   1 
ATOM   4754 O  O   . ASN D 1 53  ? -1.766  42.609  21.548  1.00 14.76 ? 41  ASN D O   1 
ATOM   4755 C  CB  . ASN D 1 53  ? -4.463  42.214  21.437  1.00 16.37 ? 41  ASN D CB  1 
ATOM   4756 C  CG  . ASN D 1 53  ? -5.833  41.606  21.323  1.00 19.39 ? 41  ASN D CG  1 
ATOM   4757 O  OD1 . ASN D 1 53  ? -5.981  40.385  21.370  1.00 19.36 ? 41  ASN D OD1 1 
ATOM   4758 N  ND2 . ASN D 1 53  ? -6.842  42.447  21.176  1.00 23.03 ? 41  ASN D ND2 1 
ATOM   4759 N  N   . SER D 1 54  ? -1.497  41.808  23.625  1.00 13.36 ? 42  SER D N   1 
ATOM   4760 C  CA  . SER D 1 54  ? -0.158  42.347  23.794  1.00 15.32 ? 42  SER D CA  1 
ATOM   4761 C  C   . SER D 1 54  ? 0.869   41.649  22.903  1.00 13.80 ? 42  SER D C   1 
ATOM   4762 O  O   . SER D 1 54  ? 0.644   40.566  22.368  1.00 15.97 ? 42  SER D O   1 
ATOM   4763 C  CB  . SER D 1 54  ? 0.273   42.195  25.253  1.00 14.35 ? 42  SER D CB  1 
ATOM   4764 O  OG  . SER D 1 54  ? 0.511   40.821  25.541  1.00 15.27 ? 42  SER D OG  1 
ATOM   4765 N  N   . GLY D 1 55  ? 2.017   42.296  22.750  1.00 14.50 ? 43  GLY D N   1 
ATOM   4766 C  CA  . GLY D 1 55  ? 3.225   41.595  22.354  1.00 15.66 ? 43  GLY D CA  1 
ATOM   4767 C  C   . GLY D 1 55  ? 3.861   40.999  23.596  1.00 18.98 ? 43  GLY D C   1 
ATOM   4768 O  O   . GLY D 1 55  ? 3.143   40.508  24.466  1.00 18.37 ? 43  GLY D O   1 
ATOM   4769 N  N   . ASN D 1 56  ? 5.187   41.040  23.699  1.00 15.16 ? 44  ASN D N   1 
ATOM   4770 C  CA  . ASN D 1 56  ? 5.895   40.624  24.902  1.00 18.15 ? 44  ASN D CA  1 
ATOM   4771 C  C   . ASN D 1 56  ? 5.984   41.801  25.857  1.00 14.78 ? 44  ASN D C   1 
ATOM   4772 O  O   . ASN D 1 56  ? 6.265   42.925  25.433  1.00 13.79 ? 44  ASN D O   1 
ATOM   4773 C  CB  . ASN D 1 56  ? 7.320   40.170  24.576  1.00 20.44 ? 44  ASN D CB  1 
ATOM   4774 C  CG  . ASN D 1 56  ? 7.407   38.730  24.138  1.00 31.11 ? 44  ASN D CG  1 
ATOM   4775 O  OD1 . ASN D 1 56  ? 7.183   37.814  24.928  1.00 35.15 ? 44  ASN D OD1 1 
ATOM   4776 N  ND2 . ASN D 1 56  ? 7.773   38.516  22.878  1.00 29.62 ? 44  ASN D ND2 1 
ATOM   4777 N  N   . PHE D 1 57  ? 5.796   41.535  27.153  1.00 12.83 ? 45  PHE D N   1 
ATOM   4778 C  CA  . PHE D 1 57  ? 6.043   42.561  28.160  1.00 11.27 ? 45  PHE D CA  1 
ATOM   4779 C  C   . PHE D 1 57  ? 6.414   41.894  29.476  1.00 12.50 ? 45  PHE D C   1 
ATOM   4780 O  O   . PHE D 1 57  ? 6.035   40.748  29.732  1.00 11.11 ? 45  PHE D O   1 
ATOM   4781 C  CB  . PHE D 1 57  ? 4.837   43.493  28.346  1.00 11.35 ? 45  PHE D CB  1 
ATOM   4782 C  CG  . PHE D 1 57  ? 3.713   42.890  29.154  1.00 10.82 ? 45  PHE D CG  1 
ATOM   4783 C  CD1 . PHE D 1 57  ? 3.707   43.002  30.542  1.00 12.74 ? 45  PHE D CD1 1 
ATOM   4784 C  CD2 . PHE D 1 57  ? 2.659   42.229  28.520  1.00 11.83 ? 45  PHE D CD2 1 
ATOM   4785 C  CE1 . PHE D 1 57  ? 2.676   42.441  31.303  1.00 15.04 ? 45  PHE D CE1 1 
ATOM   4786 C  CE2 . PHE D 1 57  ? 1.626   41.672  29.268  1.00 14.72 ? 45  PHE D CE2 1 
ATOM   4787 C  CZ  . PHE D 1 57  ? 1.636   41.780  30.661  1.00 12.79 ? 45  PHE D CZ  1 
ATOM   4788 N  N   . VAL D 1 58  ? 7.177   42.619  30.300  1.00 10.53 ? 46  VAL D N   1 
ATOM   4789 C  CA  . VAL D 1 58  ? 7.523   42.207  31.661  1.00 11.33 ? 46  VAL D CA  1 
ATOM   4790 C  C   . VAL D 1 58  ? 7.475   43.454  32.532  1.00 13.96 ? 46  VAL D C   1 
ATOM   4791 O  O   . VAL D 1 58  ? 8.041   44.487  32.160  1.00 16.97 ? 46  VAL D O   1 
ATOM   4792 C  CB  . VAL D 1 58  ? 8.927   41.573  31.755  1.00 13.57 ? 46  VAL D CB  1 
ATOM   4793 C  CG1 . VAL D 1 58  ? 9.204   41.065  33.200  1.00 16.57 ? 46  VAL D CG1 1 
ATOM   4794 C  CG2 . VAL D 1 58  ? 9.100   40.477  30.747  1.00 18.16 ? 46  VAL D CG2 1 
ATOM   4795 N  N   . ALA D 1 59  ? 6.828   43.365  33.692  1.00 10.41 ? 47  ALA D N   1 
ATOM   4796 C  CA  . ALA D 1 59  ? 6.657   44.545  34.532  1.00 12.13 ? 47  ALA D CA  1 
ATOM   4797 C  C   . ALA D 1 59  ? 6.659   44.160  36.000  1.00 10.99 ? 47  ALA D C   1 
ATOM   4798 O  O   . ALA D 1 59  ? 6.046   43.162  36.378  1.00 10.16 ? 47  ALA D O   1 
ATOM   4799 C  CB  . ALA D 1 59  ? 5.346   45.261  34.224  1.00 14.86 ? 47  ALA D CB  1 
ATOM   4800 N  N   . GLY D 1 60  ? 7.308   44.968  36.832  1.00 8.23  ? 48  GLY D N   1 
ATOM   4801 C  CA  . GLY D 1 60  ? 7.150   44.727  38.254  1.00 8.86  ? 48  GLY D CA  1 
ATOM   4802 C  C   . GLY D 1 60  ? 8.023   45.629  39.095  1.00 11.73 ? 48  GLY D C   1 
ATOM   4803 O  O   . GLY D 1 60  ? 8.785   46.463  38.588  1.00 11.59 ? 48  GLY D O   1 
ATOM   4804 N  N   . LYS D 1 61  ? 7.914   45.426  40.401  1.00 10.50 ? 49  LYS D N   1 
ATOM   4805 C  CA  . LYS D 1 61  ? 8.680   46.185  41.381  1.00 10.44 ? 49  LYS D CA  1 
ATOM   4806 C  C   . LYS D 1 61  ? 9.601   45.260  42.150  1.00 11.98 ? 49  LYS D C   1 
ATOM   4807 O  O   . LYS D 1 61  ? 9.321   44.066  42.311  1.00 10.10 ? 49  LYS D O   1 
ATOM   4808 C  CB  . LYS D 1 61  ? 7.772   46.907  42.386  1.00 10.80 ? 49  LYS D CB  1 
ATOM   4809 C  CG  . LYS D 1 61  ? 7.328   48.286  41.921  1.00 10.96 ? 49  LYS D CG  1 
ATOM   4810 C  CD  . LYS D 1 61  ? 6.429   48.936  42.941  1.00 13.57 ? 49  LYS D CD  1 
ATOM   4811 C  CE  . LYS D 1 61  ? 6.344   50.449  42.711  1.00 13.53 ? 49  LYS D CE  1 
ATOM   4812 N  NZ  . LYS D 1 61  ? 5.394   51.097  43.687  1.00 15.39 ? 49  LYS D NZ  1 
ATOM   4813 N  N   . GLY D 1 62  ? 10.703  45.833  42.629  1.00 9.14  ? 50  GLY D N   1 
ATOM   4814 C  CA  . GLY D 1 62  ? 11.640  45.095  43.446  1.00 10.59 ? 50  GLY D CA  1 
ATOM   4815 C  C   . GLY D 1 62  ? 12.870  45.917  43.784  1.00 12.55 ? 50  GLY D C   1 
ATOM   4816 O  O   . GLY D 1 62  ? 12.761  46.988  44.396  1.00 11.35 ? 50  GLY D O   1 
ATOM   4817 N  N   . TRP D 1 63  ? 14.037  45.428  43.373  1.00 13.09 ? 51  TRP D N   1 
ATOM   4818 C  CA  . TRP D 1 63  ? 15.318  45.976  43.801  1.00 12.60 ? 51  TRP D CA  1 
ATOM   4819 C  C   . TRP D 1 63  ? 16.287  45.979  42.634  1.00 14.01 ? 51  TRP D C   1 
ATOM   4820 O  O   . TRP D 1 63  ? 16.234  45.106  41.764  1.00 11.80 ? 51  TRP D O   1 
ATOM   4821 C  CB  . TRP D 1 63  ? 15.932  45.162  44.964  1.00 15.55 ? 51  TRP D CB  1 
ATOM   4822 C  CG  . TRP D 1 63  ? 15.009  45.081  46.120  1.00 16.33 ? 51  TRP D CG  1 
ATOM   4823 C  CD1 . TRP D 1 63  ? 14.963  45.911  47.194  1.00 15.96 ? 51  TRP D CD1 1 
ATOM   4824 C  CD2 . TRP D 1 63  ? 13.947  44.140  46.289  1.00 15.33 ? 51  TRP D CD2 1 
ATOM   4825 N  NE1 . TRP D 1 63  ? 13.942  45.540  48.036  1.00 18.48 ? 51  TRP D NE1 1 
ATOM   4826 C  CE2 . TRP D 1 63  ? 13.300  44.455  47.496  1.00 16.94 ? 51  TRP D CE2 1 
ATOM   4827 C  CE3 . TRP D 1 63  ? 13.482  43.060  45.530  1.00 16.43 ? 51  TRP D CE3 1 
ATOM   4828 C  CZ2 . TRP D 1 63  ? 12.220  43.722  47.975  1.00 22.75 ? 51  TRP D CZ2 1 
ATOM   4829 C  CZ3 . TRP D 1 63  ? 12.405  42.339  46.001  1.00 18.43 ? 51  TRP D CZ3 1 
ATOM   4830 C  CH2 . TRP D 1 63  ? 11.785  42.671  47.213  1.00 17.91 ? 51  TRP D CH2 1 
ATOM   4831 N  N   . ASN D 1 64  ? 17.193  46.967  42.631  1.00 12.61 ? 52  ASN D N   1 
ATOM   4832 C  CA  . ASN D 1 64  ? 18.291  46.939  41.678  1.00 11.16 ? 52  ASN D CA  1 
ATOM   4833 C  C   . ASN D 1 64  ? 19.526  47.575  42.299  1.00 12.44 ? 52  ASN D C   1 
ATOM   4834 O  O   . ASN D 1 64  ? 19.550  48.795  42.501  1.00 12.73 ? 52  ASN D O   1 
ATOM   4835 C  CB  . ASN D 1 64  ? 17.945  47.673  40.381  1.00 12.93 ? 52  ASN D CB  1 
ATOM   4836 C  CG  . ASN D 1 64  ? 18.981  47.438  39.295  1.00 15.60 ? 52  ASN D CG  1 
ATOM   4837 O  OD1 . ASN D 1 64  ? 19.854  46.573  39.427  1.00 14.57 ? 52  ASN D OD1 1 
ATOM   4838 N  ND2 . ASN D 1 64  ? 18.887  48.195  38.212  1.00 20.38 ? 52  ASN D ND2 1 
ATOM   4839 N  N   . PRO D 1 65  ? 20.569  46.796  42.604  1.00 13.41 ? 53  PRO D N   1 
ATOM   4840 C  CA  . PRO D 1 65  ? 20.670  45.346  42.406  1.00 16.15 ? 53  PRO D CA  1 
ATOM   4841 C  C   . PRO D 1 65  ? 19.853  44.513  43.398  1.00 16.71 ? 53  PRO D C   1 
ATOM   4842 O  O   . PRO D 1 65  ? 19.616  44.933  44.534  1.00 15.47 ? 53  PRO D O   1 
ATOM   4843 C  CB  . PRO D 1 65  ? 22.164  45.076  42.615  1.00 16.66 ? 53  PRO D CB  1 
ATOM   4844 C  CG  . PRO D 1 65  ? 22.593  46.142  43.556  1.00 20.85 ? 53  PRO D CG  1 
ATOM   4845 C  CD  . PRO D 1 65  ? 21.803  47.357  43.193  1.00 13.77 ? 53  PRO D CD  1 
ATOM   4846 N  N   . GLY D 1 66  ? 19.419  43.331  42.964  1.00 15.57 ? 54  GLY D N   1 
ATOM   4847 C  CA  . GLY D 1 66  ? 18.844  42.386  43.898  1.00 17.14 ? 54  GLY D CA  1 
ATOM   4848 C  C   . GLY D 1 66  ? 19.890  41.804  44.831  1.00 18.79 ? 54  GLY D C   1 
ATOM   4849 O  O   . GLY D 1 66  ? 21.087  41.774  44.530  1.00 20.60 ? 54  GLY D O   1 
ATOM   4850 N  N   . SER D 1 67  ? 19.430  41.344  45.995  1.00 19.74 ? 55  SER D N   1 
ATOM   4851 C  CA  . SER D 1 67  ? 20.316  40.862  47.052  1.00 24.64 ? 55  SER D CA  1 
ATOM   4852 C  C   . SER D 1 67  ? 19.796  39.568  47.670  1.00 31.33 ? 55  SER D C   1 
ATOM   4853 O  O   . SER D 1 67  ? 19.930  39.350  48.879  1.00 32.21 ? 55  SER D O   1 
ATOM   4854 C  CB  . SER D 1 67  ? 20.496  41.927  48.141  1.00 29.10 ? 55  SER D CB  1 
ATOM   4855 O  OG  . SER D 1 67  ? 19.255  42.540  48.451  1.00 40.74 ? 55  SER D OG  1 
ATOM   4856 N  N   . SER D 1 68  ? 19.202  38.690  46.860  1.00 26.57 ? 56  SER D N   1 
ATOM   4857 C  CA  . SER D 1 68  ? 18.772  37.368  47.335  1.00 30.90 ? 56  SER D CA  1 
ATOM   4858 C  C   . SER D 1 68  ? 17.893  37.456  48.584  1.00 26.69 ? 56  SER D C   1 
ATOM   4859 O  O   . SER D 1 68  ? 17.952  36.603  49.476  1.00 29.29 ? 56  SER D O   1 
ATOM   4860 C  CB  . SER D 1 68  ? 19.978  36.463  47.597  1.00 30.76 ? 56  SER D CB  1 
ATOM   4861 O  OG  . SER D 1 68  ? 20.827  36.381  46.459  1.00 29.05 ? 56  SER D OG  1 
ATOM   4862 N  N   . GLN D 1 69  ? 17.068  38.494  48.657  1.00 25.06 ? 57  GLN D N   1 
ATOM   4863 C  CA  . GLN D 1 69  ? 16.249  38.635  49.849  1.00 29.65 ? 57  GLN D CA  1 
ATOM   4864 C  C   . GLN D 1 69  ? 15.074  37.659  49.807  1.00 22.11 ? 57  GLN D C   1 
ATOM   4865 O  O   . GLN D 1 69  ? 14.737  37.085  48.767  1.00 21.71 ? 57  GLN D O   1 
ATOM   4866 C  CB  . GLN D 1 69  ? 15.753  40.080  50.022  1.00 34.13 ? 57  GLN D CB  1 
ATOM   4867 C  CG  . GLN D 1 69  ? 15.256  40.786  48.756  1.00 27.38 ? 57  GLN D CG  1 
ATOM   4868 C  CD  . GLN D 1 69  ? 16.331  41.646  48.086  1.00 26.66 ? 57  GLN D CD  1 
ATOM   4869 O  OE1 . GLN D 1 69  ? 17.010  41.197  47.169  1.00 27.65 ? 57  GLN D OE1 1 
ATOM   4870 N  NE2 . GLN D 1 69  ? 16.477  42.888  48.540  1.00 29.80 ? 57  GLN D NE2 1 
ATOM   4871 N  N   . THR D 1 70  ? 14.491  37.429  50.977  1.00 20.88 ? 58  THR D N   1 
ATOM   4872 C  CA  . THR D 1 70  ? 13.233  36.703  51.068  1.00 20.25 ? 58  THR D CA  1 
ATOM   4873 C  C   . THR D 1 70  ? 12.104  37.668  50.744  1.00 19.65 ? 58  THR D C   1 
ATOM   4874 O  O   . THR D 1 70  ? 11.959  38.706  51.399  1.00 20.16 ? 58  THR D O   1 
ATOM   4875 C  CB  . THR D 1 70  ? 13.065  36.098  52.459  1.00 21.18 ? 58  THR D CB  1 
ATOM   4876 O  OG1 . THR D 1 70  ? 14.075  35.107  52.654  1.00 22.58 ? 58  THR D OG1 1 
ATOM   4877 C  CG2 . THR D 1 70  ? 11.723  35.429  52.580  1.00 19.20 ? 58  THR D CG2 1 
ATOM   4878 N  N   . ILE D 1 71  ? 11.336  37.355  49.705  1.00 14.40 ? 59  ILE D N   1 
ATOM   4879 C  CA  . ILE D 1 71  ? 10.316  38.256  49.194  1.00 17.36 ? 59  ILE D CA  1 
ATOM   4880 C  C   . ILE D 1 71  ? 8.956   37.805  49.696  1.00 17.80 ? 59  ILE D C   1 
ATOM   4881 O  O   . ILE D 1 71  ? 8.672   36.604  49.761  1.00 17.94 ? 59  ILE D O   1 
ATOM   4882 C  CB  . ILE D 1 71  ? 10.334  38.289  47.653  1.00 16.25 ? 59  ILE D CB  1 
ATOM   4883 C  CG1 . ILE D 1 71  ? 11.694  38.745  47.127  1.00 16.47 ? 59  ILE D CG1 1 
ATOM   4884 C  CG2 . ILE D 1 71  ? 9.195   39.161  47.096  1.00 18.56 ? 59  ILE D CG2 1 
ATOM   4885 C  CD1 . ILE D 1 71  ? 11.782  38.589  45.612  1.00 19.15 ? 59  ILE D CD1 1 
ATOM   4886 N  N   . THR D 1 72  ? 8.110   38.772  50.032  1.00 16.88 ? 60  THR D N   1 
ATOM   4887 C  CA  . THR D 1 72  ? 6.707   38.552  50.334  1.00 17.75 ? 60  THR D CA  1 
ATOM   4888 C  C   . THR D 1 72  ? 5.903   39.385  49.342  1.00 16.14 ? 60  THR D C   1 
ATOM   4889 O  O   . THR D 1 72  ? 6.223   40.551  49.103  1.00 20.54 ? 60  THR D O   1 
ATOM   4890 C  CB  . THR D 1 72  ? 6.389   38.949  51.799  1.00 22.36 ? 60  THR D CB  1 
ATOM   4891 O  OG1 . THR D 1 72  ? 7.068   38.052  52.684  1.00 26.95 ? 60  THR D OG1 1 
ATOM   4892 C  CG2 . THR D 1 72  ? 4.903   38.878  52.079  1.00 27.97 ? 60  THR D CG2 1 
ATOM   4893 N  N   . TYR D 1 73  ? 4.891   38.779  48.722  1.00 15.09 ? 61  TYR D N   1 
ATOM   4894 C  CA  . TYR D 1 73  ? 4.094   39.508  47.746  1.00 17.60 ? 61  TYR D CA  1 
ATOM   4895 C  C   . TYR D 1 73  ? 2.650   39.046  47.866  1.00 16.43 ? 61  TYR D C   1 
ATOM   4896 O  O   . TYR D 1 73  ? 2.373   37.947  48.349  1.00 15.19 ? 61  TYR D O   1 
ATOM   4897 C  CB  . TYR D 1 73  ? 4.620   39.320  46.301  1.00 17.66 ? 61  TYR D CB  1 
ATOM   4898 C  CG  . TYR D 1 73  ? 4.298   37.961  45.719  1.00 15.19 ? 61  TYR D CG  1 
ATOM   4899 C  CD1 . TYR D 1 73  ? 5.016   36.830  46.100  1.00 14.97 ? 61  TYR D CD1 1 
ATOM   4900 C  CD2 . TYR D 1 73  ? 3.246   37.803  44.822  1.00 17.17 ? 61  TYR D CD2 1 
ATOM   4901 C  CE1 . TYR D 1 73  ? 4.700   35.583  45.603  1.00 17.37 ? 61  TYR D CE1 1 
ATOM   4902 C  CE2 . TYR D 1 73  ? 2.933   36.563  44.313  1.00 14.52 ? 61  TYR D CE2 1 
ATOM   4903 C  CZ  . TYR D 1 73  ? 3.653   35.461  44.706  1.00 20.02 ? 61  TYR D CZ  1 
ATOM   4904 O  OH  . TYR D 1 73  ? 3.327   34.224  44.208  1.00 16.99 ? 61  TYR D OH  1 
ATOM   4905 N  N   . SER D 1 74  ? 1.737   39.909  47.429  1.00 14.36 ? 62  SER D N   1 
ATOM   4906 C  CA  . SER D 1 74  ? 0.304   39.643  47.497  1.00 17.53 ? 62  SER D CA  1 
ATOM   4907 C  C   . SER D 1 74  ? -0.379  40.341  46.329  1.00 16.58 ? 62  SER D C   1 
ATOM   4908 O  O   . SER D 1 74  ? 0.232   41.129  45.609  1.00 14.46 ? 62  SER D O   1 
ATOM   4909 C  CB  . SER D 1 74  ? -0.286  40.131  48.822  1.00 21.04 ? 62  SER D CB  1 
ATOM   4910 O  OG  . SER D 1 74  ? -0.153  41.539  48.927  1.00 24.72 ? 62  SER D OG  1 
ATOM   4911 N  N   . GLY D 1 75  ? -1.669  40.056  46.156  1.00 14.17 ? 63  GLY D N   1 
ATOM   4912 C  CA  . GLY D 1 75  ? -2.453  40.770  45.166  1.00 13.61 ? 63  GLY D CA  1 
ATOM   4913 C  C   . GLY D 1 75  ? -3.281  39.844  44.304  1.00 15.47 ? 63  GLY D C   1 
ATOM   4914 O  O   . GLY D 1 75  ? -3.747  38.793  44.762  1.00 14.77 ? 63  GLY D O   1 
ATOM   4915 N  N   . GLU D 1 76  ? -3.489  40.236  43.052  1.00 12.42 ? 64  GLU D N   1 
ATOM   4916 C  CA  . GLU D 1 76  ? -4.296  39.441  42.147  1.00 13.13 ? 64  GLU D CA  1 
ATOM   4917 C  C   . GLU D 1 76  ? -3.705  39.498  40.747  1.00 15.49 ? 64  GLU D C   1 
ATOM   4918 O  O   . GLU D 1 76  ? -3.029  40.463  40.363  1.00 14.53 ? 64  GLU D O   1 
ATOM   4919 C  CB  . GLU D 1 76  ? -5.756  39.898  42.127  1.00 18.84 ? 64  GLU D CB  1 
ATOM   4920 C  CG  . GLU D 1 76  ? -5.958  41.362  41.890  1.00 20.56 ? 64  GLU D CG  1 
ATOM   4921 C  CD  . GLU D 1 76  ? -7.427  41.689  41.685  1.00 31.61 ? 64  GLU D CD  1 
ATOM   4922 O  OE1 . GLU D 1 76  ? -8.225  41.493  42.624  1.00 36.86 ? 64  GLU D OE1 1 
ATOM   4923 O  OE2 . GLU D 1 76  ? -7.798  42.128  40.576  1.00 33.19 ? 64  GLU D OE2 1 
ATOM   4924 N  N   . TRP D 1 77  ? -3.946  38.426  40.005  1.00 13.66 ? 65  TRP D N   1 
ATOM   4925 C  CA  . TRP D 1 77  ? -3.315  38.210  38.708  1.00 14.79 ? 65  TRP D CA  1 
ATOM   4926 C  C   . TRP D 1 77  ? -4.354  37.498  37.857  1.00 16.71 ? 65  TRP D C   1 
ATOM   4927 O  O   . TRP D 1 77  ? -4.696  36.344  38.139  1.00 13.25 ? 65  TRP D O   1 
ATOM   4928 C  CB  . TRP D 1 77  ? -2.035  37.398  38.882  1.00 14.26 ? 65  TRP D CB  1 
ATOM   4929 C  CG  . TRP D 1 77  ? -1.360  36.883  37.652  1.00 15.94 ? 65  TRP D CG  1 
ATOM   4930 C  CD1 . TRP D 1 77  ? -0.569  37.585  36.783  1.00 18.48 ? 65  TRP D CD1 1 
ATOM   4931 C  CD2 . TRP D 1 77  ? -1.363  35.532  37.192  1.00 15.87 ? 65  TRP D CD2 1 
ATOM   4932 N  NE1 . TRP D 1 77  ? -0.094  36.749  35.801  1.00 17.14 ? 65  TRP D NE1 1 
ATOM   4933 C  CE2 . TRP D 1 77  ? -0.573  35.484  36.026  1.00 17.67 ? 65  TRP D CE2 1 
ATOM   4934 C  CE3 . TRP D 1 77  ? -1.969  34.355  37.650  1.00 16.31 ? 65  TRP D CE3 1 
ATOM   4935 C  CZ2 . TRP D 1 77  ? -0.367  34.305  35.309  1.00 15.66 ? 65  TRP D CZ2 1 
ATOM   4936 C  CZ3 . TRP D 1 77  ? -1.780  33.189  36.929  1.00 14.82 ? 65  TRP D CZ3 1 
ATOM   4937 C  CH2 . TRP D 1 77  ? -0.978  33.170  35.779  1.00 16.63 ? 65  TRP D CH2 1 
ATOM   4938 N  N   . ASN D 1 78  ? -4.897  38.206  36.861  1.00 14.09 ? 66  ASN D N   1 
ATOM   4939 C  CA  . ASN D 1 78  ? -6.065  37.760  36.100  1.00 14.19 ? 66  ASN D CA  1 
ATOM   4940 C  C   . ASN D 1 78  ? -5.755  37.764  34.605  1.00 12.62 ? 66  ASN D C   1 
ATOM   4941 O  O   . ASN D 1 78  ? -6.246  38.633  33.868  1.00 13.89 ? 66  ASN D O   1 
ATOM   4942 C  CB  . ASN D 1 78  ? -7.270  38.654  36.390  1.00 16.87 ? 66  ASN D CB  1 
ATOM   4943 C  CG  . ASN D 1 78  ? -7.512  38.843  37.882  1.00 26.11 ? 66  ASN D CG  1 
ATOM   4944 O  OD1 . ASN D 1 78  ? -7.895  37.906  38.572  1.00 27.40 ? 66  ASN D OD1 1 
ATOM   4945 N  ND2 . ASN D 1 78  ? -7.281  40.052  38.380  1.00 27.30 ? 66  ASN D ND2 1 
ATOM   4946 N  N   . PRO D 1 79  ? -4.955  36.811  34.126  1.00 14.67 ? 67  PRO D N   1 
ATOM   4947 C  CA  . PRO D 1 79  ? -4.685  36.720  32.687  1.00 13.80 ? 67  PRO D CA  1 
ATOM   4948 C  C   . PRO D 1 79  ? -5.786  36.017  31.918  1.00 17.63 ? 67  PRO D C   1 
ATOM   4949 O  O   . PRO D 1 79  ? -6.431  35.093  32.412  1.00 17.43 ? 67  PRO D O   1 
ATOM   4950 C  CB  . PRO D 1 79  ? -3.399  35.891  32.629  1.00 15.29 ? 67  PRO D CB  1 
ATOM   4951 C  CG  . PRO D 1 79  ? -3.514  34.988  33.828  1.00 17.97 ? 67  PRO D CG  1 
ATOM   4952 C  CD  . PRO D 1 79  ? -4.140  35.849  34.898  1.00 20.05 ? 67  PRO D CD  1 
ATOM   4953 N  N   . ASN D 1 80  ? -5.979  36.465  30.678  1.00 15.55 ? 68  ASN D N   1 
ATOM   4954 C  CA  . ASN D 1 80  ? -6.756  35.745  29.665  1.00 17.25 ? 68  ASN D CA  1 
ATOM   4955 C  C   . ASN D 1 80  ? -5.778  35.392  28.544  1.00 14.82 ? 68  ASN D C   1 
ATOM   4956 O  O   . ASN D 1 80  ? -5.595  36.168  27.603  1.00 16.59 ? 68  ASN D O   1 
ATOM   4957 C  CB  . ASN D 1 80  ? -7.922  36.587  29.158  1.00 21.49 ? 68  ASN D CB  1 
ATOM   4958 C  CG  . ASN D 1 80  ? -8.821  35.824  28.196  1.00 28.26 ? 68  ASN D CG  1 
ATOM   4959 O  OD1 . ASN D 1 80  ? -9.449  36.416  27.314  1.00 34.29 ? 68  ASN D OD1 1 
ATOM   4960 N  ND2 . ASN D 1 80  ? -8.885  34.508  28.361  1.00 27.08 ? 68  ASN D ND2 1 
ATOM   4961 N  N   . GLY D 1 81  ? -5.149  34.230  28.653  1.00 14.43 ? 69  GLY D N   1 
ATOM   4962 C  CA  . GLY D 1 81  ? -4.082  33.823  27.762  1.00 15.48 ? 69  GLY D CA  1 
ATOM   4963 C  C   . GLY D 1 81  ? -2.737  33.805  28.471  1.00 14.78 ? 69  GLY D C   1 
ATOM   4964 O  O   . GLY D 1 81  ? -2.640  33.894  29.698  1.00 18.30 ? 69  GLY D O   1 
ATOM   4965 N  N   . ASN D 1 82  ? -1.689  33.706  27.658  1.00 13.30 ? 70  ASN D N   1 
ATOM   4966 C  CA  . ASN D 1 82  ? -0.336  33.410  28.125  1.00 14.25 ? 70  ASN D CA  1 
ATOM   4967 C  C   . ASN D 1 82  ? 0.193   34.501  29.057  1.00 13.47 ? 70  ASN D C   1 
ATOM   4968 O  O   . ASN D 1 82  ? 0.336   35.659  28.655  1.00 13.43 ? 70  ASN D O   1 
ATOM   4969 C  CB  . ASN D 1 82  ? 0.580   33.253  26.906  1.00 13.46 ? 70  ASN D CB  1 
ATOM   4970 C  CG  . ASN D 1 82  ? 1.985   32.784  27.263  1.00 18.50 ? 70  ASN D CG  1 
ATOM   4971 O  OD1 . ASN D 1 82  ? 2.332   32.616  28.436  1.00 18.27 ? 70  ASN D OD1 1 
ATOM   4972 N  ND2 . ASN D 1 82  ? 2.808   32.577  26.241  1.00 20.39 ? 70  ASN D ND2 1 
ATOM   4973 N  N   . SER D 1 83  ? 0.528   34.121  30.289  1.00 10.62 ? 71  SER D N   1 
ATOM   4974 C  CA  . SER D 1 83  ? 1.098   35.082  31.221  1.00 12.39 ? 71  SER D CA  1 
ATOM   4975 C  C   . SER D 1 83  ? 1.836   34.307  32.304  1.00 15.40 ? 71  SER D C   1 
ATOM   4976 O  O   . SER D 1 83  ? 1.482   33.163  32.602  1.00 13.89 ? 71  SER D O   1 
ATOM   4977 C  CB  . SER D 1 83  ? -0.002  35.971  31.815  1.00 12.25 ? 71  SER D CB  1 
ATOM   4978 O  OG  . SER D 1 83  ? 0.491   36.856  32.811  1.00 13.75 ? 71  SER D OG  1 
ATOM   4979 N  N   . TYR D 1 84  ? 2.887   34.924  32.860  1.00 12.96 ? 72  TYR D N   1 
ATOM   4980 C  CA  . TYR D 1 84  ? 3.638   34.375  33.986  1.00 15.78 ? 72  TYR D CA  1 
ATOM   4981 C  C   . TYR D 1 84  ? 3.591   35.355  35.155  1.00 13.23 ? 72  TYR D C   1 
ATOM   4982 O  O   . TYR D 1 84  ? 3.587   36.570  34.960  1.00 11.61 ? 72  TYR D O   1 
ATOM   4983 C  CB  . TYR D 1 84  ? 5.136   34.125  33.676  1.00 15.13 ? 72  TYR D CB  1 
ATOM   4984 C  CG  . TYR D 1 84  ? 5.516   33.500  32.357  1.00 18.83 ? 72  TYR D CG  1 
ATOM   4985 C  CD1 . TYR D 1 84  ? 4.722   32.528  31.756  1.00 20.85 ? 72  TYR D CD1 1 
ATOM   4986 C  CD2 . TYR D 1 84  ? 6.716   33.849  31.734  1.00 20.37 ? 72  TYR D CD2 1 
ATOM   4987 C  CE1 . TYR D 1 84  ? 5.094   31.944  30.546  1.00 24.93 ? 72  TYR D CE1 1 
ATOM   4988 C  CE2 . TYR D 1 84  ? 7.095   33.273  30.532  1.00 23.09 ? 72  TYR D CE2 1 
ATOM   4989 C  CZ  . TYR D 1 84  ? 6.286   32.324  29.945  1.00 26.79 ? 72  TYR D CZ  1 
ATOM   4990 O  OH  . TYR D 1 84  ? 6.676   31.759  28.744  1.00 25.63 ? 72  TYR D OH  1 
ATOM   4991 N  N   . LEU D 1 85  ? 3.576   34.822  36.374  1.00 12.64 ? 73  LEU D N   1 
ATOM   4992 C  CA  . LEU D 1 85  ? 3.809   35.604  37.587  1.00 10.18 ? 73  LEU D CA  1 
ATOM   4993 C  C   . LEU D 1 85  ? 5.032   35.003  38.267  1.00 12.02 ? 73  LEU D C   1 
ATOM   4994 O  O   . LEU D 1 85  ? 5.033   33.815  38.594  1.00 10.68 ? 73  LEU D O   1 
ATOM   4995 C  CB  . LEU D 1 85  ? 2.586   35.577  38.506  1.00 12.82 ? 73  LEU D CB  1 
ATOM   4996 C  CG  . LEU D 1 85  ? 2.710   36.328  39.836  1.00 14.49 ? 73  LEU D CG  1 
ATOM   4997 C  CD1 . LEU D 1 85  ? 2.885   37.817  39.588  1.00 15.57 ? 73  LEU D CD1 1 
ATOM   4998 C  CD2 . LEU D 1 85  ? 1.480   36.058  40.704  1.00 15.85 ? 73  LEU D CD2 1 
ATOM   4999 N  N   . SER D 1 86  ? 6.080   35.809  38.459  1.00 10.14 ? 74  SER D N   1 
ATOM   5000 C  CA  . SER D 1 86  ? 7.371   35.247  38.835  1.00 10.53 ? 74  SER D CA  1 
ATOM   5001 C  C   . SER D 1 86  ? 8.198   36.254  39.607  1.00 13.44 ? 74  SER D C   1 
ATOM   5002 O  O   . SER D 1 86  ? 8.058   37.467  39.422  1.00 14.01 ? 74  SER D O   1 
ATOM   5003 C  CB  . SER D 1 86  ? 8.223   34.822  37.623  1.00 13.66 ? 74  SER D CB  1 
ATOM   5004 O  OG  . SER D 1 86  ? 7.433   34.294  36.573  1.00 25.38 ? 74  SER D OG  1 
ATOM   5005 N  N   . VAL D 1 87  ? 9.093   35.735  40.442  1.00 8.24  ? 75  VAL D N   1 
ATOM   5006 C  CA  . VAL D 1 87  ? 10.264  36.510  40.831  1.00 8.70  ? 75  VAL D CA  1 
ATOM   5007 C  C   . VAL D 1 87  ? 11.257  36.409  39.685  1.00 11.82 ? 75  VAL D C   1 
ATOM   5008 O  O   . VAL D 1 87  ? 11.553  35.309  39.202  1.00 16.97 ? 75  VAL D O   1 
ATOM   5009 C  CB  . VAL D 1 87  ? 10.866  36.004  42.147  1.00 11.04 ? 75  VAL D CB  1 
ATOM   5010 C  CG1 . VAL D 1 87  ? 12.172  36.768  42.417  1.00 11.64 ? 75  VAL D CG1 1 
ATOM   5011 C  CG2 . VAL D 1 87  ? 9.892   36.221  43.289  1.00 11.16 ? 75  VAL D CG2 1 
ATOM   5012 N  N   . TYR D 1 88  ? 11.716  37.556  39.201  1.00 10.42 ? 76  TYR D N   1 
ATOM   5013 C  CA  . TYR D 1 88  ? 12.336  37.654  37.892  1.00 8.40  ? 76  TYR D CA  1 
ATOM   5014 C  C   . TYR D 1 88  ? 13.528  38.590  37.980  1.00 9.85  ? 76  TYR D C   1 
ATOM   5015 O  O   . TYR D 1 88  ? 13.428  39.661  38.584  1.00 9.67  ? 76  TYR D O   1 
ATOM   5016 C  CB  . TYR D 1 88  ? 11.324  38.188  36.870  1.00 13.00 ? 76  TYR D CB  1 
ATOM   5017 C  CG  . TYR D 1 88  ? 11.905  38.602  35.552  1.00 12.61 ? 76  TYR D CG  1 
ATOM   5018 C  CD1 . TYR D 1 88  ? 12.239  37.660  34.591  1.00 15.64 ? 76  TYR D CD1 1 
ATOM   5019 C  CD2 . TYR D 1 88  ? 12.100  39.943  35.250  1.00 14.92 ? 76  TYR D CD2 1 
ATOM   5020 C  CE1 . TYR D 1 88  ? 12.761  38.041  33.364  1.00 17.13 ? 76  TYR D CE1 1 
ATOM   5021 C  CE2 . TYR D 1 88  ? 12.626  40.333  34.027  1.00 13.34 ? 76  TYR D CE2 1 
ATOM   5022 C  CZ  . TYR D 1 88  ? 12.955  39.379  33.088  1.00 14.08 ? 76  TYR D CZ  1 
ATOM   5023 O  OH  . TYR D 1 88  ? 13.476  39.763  31.864  1.00 15.31 ? 76  TYR D OH  1 
ATOM   5024 N  N   . GLY D 1 89  ? 14.631  38.209  37.346  1.00 11.62 ? 77  GLY D N   1 
ATOM   5025 C  CA  . GLY D 1 89  ? 15.814  39.045  37.484  1.00 11.50 ? 77  GLY D CA  1 
ATOM   5026 C  C   . GLY D 1 89  ? 16.914  38.661  36.521  1.00 13.48 ? 77  GLY D C   1 
ATOM   5027 O  O   . GLY D 1 89  ? 16.769  37.751  35.699  1.00 13.15 ? 77  GLY D O   1 
ATOM   5028 N  N   . TRP D 1 90  ? 18.029  39.387  36.639  1.00 13.08 ? 78  TRP D N   1 
ATOM   5029 C  CA  . TRP D 1 90  ? 19.180  39.207  35.771  1.00 15.56 ? 78  TRP D CA  1 
ATOM   5030 C  C   . TRP D 1 90  ? 20.455  39.161  36.596  1.00 14.81 ? 78  TRP D C   1 
ATOM   5031 O  O   . TRP D 1 90  ? 20.554  39.795  37.650  1.00 14.83 ? 78  TRP D O   1 
ATOM   5032 C  CB  . TRP D 1 90  ? 19.308  40.346  34.752  1.00 14.08 ? 78  TRP D CB  1 
ATOM   5033 C  CG  . TRP D 1 90  ? 18.213  40.398  33.755  1.00 13.60 ? 78  TRP D CG  1 
ATOM   5034 C  CD1 . TRP D 1 90  ? 16.957  40.917  33.932  1.00 13.69 ? 78  TRP D CD1 1 
ATOM   5035 C  CD2 . TRP D 1 90  ? 18.262  39.910  32.413  1.00 14.60 ? 78  TRP D CD2 1 
ATOM   5036 N  NE1 . TRP D 1 90  ? 16.226  40.780  32.774  1.00 15.33 ? 78  TRP D NE1 1 
ATOM   5037 C  CE2 . TRP D 1 90  ? 17.007  40.173  31.826  1.00 14.81 ? 78  TRP D CE2 1 
ATOM   5038 C  CE3 . TRP D 1 90  ? 19.255  39.293  31.639  1.00 17.98 ? 78  TRP D CE3 1 
ATOM   5039 C  CZ2 . TRP D 1 90  ? 16.714  39.831  30.508  1.00 19.32 ? 78  TRP D CZ2 1 
ATOM   5040 C  CZ3 . TRP D 1 90  ? 18.958  38.956  30.326  1.00 16.82 ? 78  TRP D CZ3 1 
ATOM   5041 C  CH2 . TRP D 1 90  ? 17.699  39.220  29.779  1.00 18.03 ? 78  TRP D CH2 1 
ATOM   5042 N  N   . THR D 1 91  ? 21.438  38.414  36.099  1.00 16.74 ? 79  THR D N   1 
ATOM   5043 C  CA  . THR D 1 91  ? 22.819  38.590  36.531  1.00 15.81 ? 79  THR D CA  1 
ATOM   5044 C  C   . THR D 1 91  ? 23.680  38.913  35.317  1.00 18.93 ? 79  THR D C   1 
ATOM   5045 O  O   . THR D 1 91  ? 23.257  38.779  34.166  1.00 18.26 ? 79  THR D O   1 
ATOM   5046 C  CB  . THR D 1 91  ? 23.375  37.355  37.256  1.00 20.53 ? 79  THR D CB  1 
ATOM   5047 O  OG1 . THR D 1 91  ? 23.715  36.339  36.305  1.00 20.88 ? 79  THR D OG1 1 
ATOM   5048 C  CG2 . THR D 1 91  ? 22.378  36.810  38.269  1.00 21.34 ? 79  THR D CG2 1 
ATOM   5049 N  N   . GLN D 1 92  ? 24.903  39.364  35.593  1.00 19.02 ? 80  GLN D N   1 
ATOM   5050 C  CA  . GLN D 1 92  ? 25.873  39.690  34.559  1.00 23.68 ? 80  GLN D CA  1 
ATOM   5051 C  C   . GLN D 1 92  ? 27.185  38.995  34.887  1.00 21.41 ? 80  GLN D C   1 
ATOM   5052 O  O   . GLN D 1 92  ? 27.486  38.740  36.054  1.00 23.04 ? 80  GLN D O   1 
ATOM   5053 C  CB  . GLN D 1 92  ? 26.072  41.212  34.440  1.00 24.46 ? 80  GLN D CB  1 
ATOM   5054 C  CG  . GLN D 1 92  ? 24.836  41.940  33.905  1.00 23.03 ? 80  GLN D CG  1 
ATOM   5055 C  CD  . GLN D 1 92  ? 24.914  43.452  34.034  1.00 28.29 ? 80  GLN D CD  1 
ATOM   5056 O  OE1 . GLN D 1 92  ? 24.826  44.007  35.134  1.00 27.31 ? 80  GLN D OE1 1 
ATOM   5057 N  NE2 . GLN D 1 92  ? 25.063  44.127  32.902  1.00 31.56 ? 80  GLN D NE2 1 
ATOM   5058 N  N   . ASN D 1 93  ? 27.950  38.670  33.840  1.00 24.96 ? 81  ASN D N   1 
ATOM   5059 C  CA  . ASN D 1 93  ? 29.198  37.909  33.924  1.00 26.63 ? 81  ASN D CA  1 
ATOM   5060 C  C   . ASN D 1 93  ? 29.072  36.667  34.808  1.00 26.82 ? 81  ASN D C   1 
ATOM   5061 O  O   . ASN D 1 93  ? 29.687  36.605  35.879  1.00 27.31 ? 81  ASN D O   1 
ATOM   5062 C  CB  . ASN D 1 93  ? 30.328  38.806  34.435  1.00 32.31 ? 81  ASN D CB  1 
ATOM   5063 C  CG  . ASN D 1 93  ? 30.703  39.891  33.437  1.00 41.77 ? 81  ASN D CG  1 
ATOM   5064 O  OD1 . ASN D 1 93  ? 30.012  40.903  33.313  1.00 48.59 ? 81  ASN D OD1 1 
ATOM   5065 N  ND2 . ASN D 1 93  ? 31.797  39.679  32.713  1.00 46.26 ? 81  ASN D ND2 1 
ATOM   5066 N  N   . PRO D 1 94  ? 28.318  35.637  34.384  1.00 24.77 ? 82  PRO D N   1 
ATOM   5067 C  CA  . PRO D 1 94  ? 27.639  35.548  33.087  1.00 24.30 ? 82  PRO D CA  1 
ATOM   5068 C  C   . PRO D 1 94  ? 26.281  36.256  33.045  1.00 24.24 ? 82  PRO D C   1 
ATOM   5069 O  O   . PRO D 1 94  ? 25.650  36.466  34.086  1.00 22.47 ? 82  PRO D O   1 
ATOM   5070 C  CB  . PRO D 1 94  ? 27.460  34.043  32.899  1.00 26.79 ? 82  PRO D CB  1 
ATOM   5071 C  CG  . PRO D 1 94  ? 27.305  33.524  34.294  1.00 28.23 ? 82  PRO D CG  1 
ATOM   5072 C  CD  . PRO D 1 94  ? 28.165  34.401  35.174  1.00 26.60 ? 82  PRO D CD  1 
ATOM   5073 N  N   . LEU D 1 95  ? 25.877  36.636  31.837  1.00 20.12 ? 83  LEU D N   1 
ATOM   5074 C  CA  . LEU D 1 95  ? 24.551  37.192  31.600  1.00 20.73 ? 83  LEU D CA  1 
ATOM   5075 C  C   . LEU D 1 95  ? 23.514  36.084  31.711  1.00 22.14 ? 83  LEU D C   1 
ATOM   5076 O  O   . LEU D 1 95  ? 23.536  35.131  30.925  1.00 22.51 ? 83  LEU D O   1 
ATOM   5077 C  CB  . LEU D 1 95  ? 24.493  37.835  30.217  1.00 20.58 ? 83  LEU D CB  1 
ATOM   5078 C  CG  . LEU D 1 95  ? 23.184  38.552  29.892  1.00 22.45 ? 83  LEU D CG  1 
ATOM   5079 C  CD1 . LEU D 1 95  ? 22.964  39.684  30.876  1.00 20.02 ? 83  LEU D CD1 1 
ATOM   5080 C  CD2 . LEU D 1 95  ? 23.146  39.060  28.459  1.00 19.33 ? 83  LEU D CD2 1 
ATOM   5081 N  N   . VAL D 1 96  ? 22.612  36.205  32.684  1.00 19.36 ? 84  VAL D N   1 
ATOM   5082 C  CA  . VAL D 1 96  ? 21.585  35.200  32.936  1.00 18.19 ? 84  VAL D CA  1 
ATOM   5083 C  C   . VAL D 1 96  ? 20.261  35.910  33.178  1.00 16.62 ? 84  VAL D C   1 
ATOM   5084 O  O   . VAL D 1 96  ? 20.210  36.885  33.932  1.00 17.18 ? 84  VAL D O   1 
ATOM   5085 C  CB  . VAL D 1 96  ? 21.937  34.322  34.152  1.00 19.67 ? 84  VAL D CB  1 
ATOM   5086 C  CG1 . VAL D 1 96  ? 20.752  33.434  34.543  1.00 17.59 ? 84  VAL D CG1 1 
ATOM   5087 C  CG2 . VAL D 1 96  ? 23.173  33.492  33.876  1.00 21.95 ? 84  VAL D CG2 1 
ATOM   5088 N  N   . GLU D 1 97  ? 19.191  35.411  32.562  1.00 14.33 ? 85  GLU D N   1 
ATOM   5089 C  CA  . GLU D 1 97  ? 17.826  35.794  32.906  1.00 13.86 ? 85  GLU D CA  1 
ATOM   5090 C  C   . GLU D 1 97  ? 17.225  34.654  33.714  1.00 12.34 ? 85  GLU D C   1 
ATOM   5091 O  O   . GLU D 1 97  ? 17.300  33.503  33.284  1.00 16.77 ? 85  GLU D O   1 
ATOM   5092 C  CB  . GLU D 1 97  ? 17.003  36.040  31.638  1.00 14.27 ? 85  GLU D CB  1 
ATOM   5093 C  CG  . GLU D 1 97  ? 15.621  36.607  31.873  1.00 16.03 ? 85  GLU D CG  1 
ATOM   5094 C  CD  . GLU D 1 97  ? 14.848  36.800  30.582  1.00 19.61 ? 85  GLU D CD  1 
ATOM   5095 O  OE1 . GLU D 1 97  ? 14.100  37.794  30.479  1.00 19.77 ? 85  GLU D OE1 1 
ATOM   5096 O  OE2 . GLU D 1 97  ? 14.987  35.956  29.670  1.00 19.96 ? 85  GLU D OE2 1 
ATOM   5097 N  N   . TYR D 1 98  ? 16.667  34.948  34.890  1.00 13.09 ? 86  TYR D N   1 
ATOM   5098 C  CA  . TYR D 1 98  ? 16.151  33.870  35.732  1.00 13.83 ? 86  TYR D CA  1 
ATOM   5099 C  C   . TYR D 1 98  ? 14.712  34.138  36.152  1.00 14.87 ? 86  TYR D C   1 
ATOM   5100 O  O   . TYR D 1 98  ? 14.264  35.288  36.226  1.00 10.91 ? 86  TYR D O   1 
ATOM   5101 C  CB  . TYR D 1 98  ? 17.038  33.626  36.961  1.00 13.80 ? 86  TYR D CB  1 
ATOM   5102 C  CG  . TYR D 1 98  ? 17.127  34.772  37.946  1.00 14.13 ? 86  TYR D CG  1 
ATOM   5103 C  CD1 . TYR D 1 98  ? 16.153  34.954  38.920  1.00 13.54 ? 86  TYR D CD1 1 
ATOM   5104 C  CD2 . TYR D 1 98  ? 18.213  35.649  37.930  1.00 16.89 ? 86  TYR D CD2 1 
ATOM   5105 C  CE1 . TYR D 1 98  ? 16.235  35.994  39.828  1.00 13.18 ? 86  TYR D CE1 1 
ATOM   5106 C  CE2 . TYR D 1 98  ? 18.299  36.685  38.835  1.00 16.53 ? 86  TYR D CE2 1 
ATOM   5107 C  CZ  . TYR D 1 98  ? 17.308  36.849  39.783  1.00 17.34 ? 86  TYR D CZ  1 
ATOM   5108 O  OH  . TYR D 1 98  ? 17.391  37.883  40.686  1.00 17.53 ? 86  TYR D OH  1 
ATOM   5109 N  N   . TYR D 1 99  ? 13.991  33.043  36.420  1.00 14.12 ? 87  TYR D N   1 
ATOM   5110 C  CA  . TYR D 1 99  ? 12.579  33.073  36.780  1.00 12.76 ? 87  TYR D CA  1 
ATOM   5111 C  C   . TYR D 1 99  ? 12.324  32.102  37.916  1.00 13.73 ? 87  TYR D C   1 
ATOM   5112 O  O   . TYR D 1 99  ? 12.714  30.935  37.826  1.00 16.52 ? 87  TYR D O   1 
ATOM   5113 C  CB  . TYR D 1 99  ? 11.678  32.641  35.628  1.00 15.21 ? 87  TYR D CB  1 
ATOM   5114 C  CG  . TYR D 1 99  ? 11.755  33.423  34.361  1.00 15.50 ? 87  TYR D CG  1 
ATOM   5115 C  CD1 . TYR D 1 99  ? 12.811  33.245  33.474  1.00 16.28 ? 87  TYR D CD1 1 
ATOM   5116 C  CD2 . TYR D 1 99  ? 10.748  34.297  34.024  1.00 17.51 ? 87  TYR D CD2 1 
ATOM   5117 C  CE1 . TYR D 1 99  ? 12.857  33.947  32.284  1.00 18.08 ? 87  TYR D CE1 1 
ATOM   5118 C  CE2 . TYR D 1 99  ? 10.783  34.994  32.844  1.00 19.65 ? 87  TYR D CE2 1 
ATOM   5119 C  CZ  . TYR D 1 99  ? 11.835  34.816  31.982  1.00 17.31 ? 87  TYR D CZ  1 
ATOM   5120 O  OH  . TYR D 1 99  ? 11.851  35.523  30.801  1.00 26.48 ? 87  TYR D OH  1 
ATOM   5121 N  N   . ILE D 1 100 ? 11.659  32.571  38.958  1.00 11.52 ? 88  ILE D N   1 
ATOM   5122 C  CA  . ILE D 1 100 ? 11.016  31.702  39.933  1.00 11.19 ? 88  ILE D CA  1 
ATOM   5123 C  C   . ILE D 1 100 ? 9.524   31.847  39.679  1.00 11.86 ? 88  ILE D C   1 
ATOM   5124 O  O   . ILE D 1 100 ? 8.895   32.815  40.123  1.00 12.89 ? 88  ILE D O   1 
ATOM   5125 C  CB  . ILE D 1 100 ? 11.394  32.065  41.370  1.00 12.32 ? 88  ILE D CB  1 
ATOM   5126 C  CG1 . ILE D 1 100 ? 12.911  31.970  41.543  1.00 12.56 ? 88  ILE D CG1 1 
ATOM   5127 C  CG2 . ILE D 1 100 ? 10.657  31.150  42.362  1.00 14.14 ? 88  ILE D CG2 1 
ATOM   5128 C  CD1 . ILE D 1 100 ? 13.425  32.798  42.710  1.00 14.04 ? 88  ILE D CD1 1 
ATOM   5129 N  N   . VAL D 1 101 ? 8.962   30.912  38.915  1.00 11.54 ? 89  VAL D N   1 
ATOM   5130 C  CA  . VAL D 1 101 ? 7.603   31.050  38.400  1.00 12.11 ? 89  VAL D CA  1 
ATOM   5131 C  C   . VAL D 1 101 ? 6.617   30.530  39.440  1.00 13.49 ? 89  VAL D C   1 
ATOM   5132 O  O   . VAL D 1 101 ? 6.638   29.344  39.789  1.00 15.07 ? 89  VAL D O   1 
ATOM   5133 C  CB  . VAL D 1 101 ? 7.434   30.304  37.068  1.00 12.14 ? 89  VAL D CB  1 
ATOM   5134 C  CG1 . VAL D 1 101 ? 6.018   30.511  36.544  1.00 12.52 ? 89  VAL D CG1 1 
ATOM   5135 C  CG2 . VAL D 1 101 ? 8.468   30.786  36.037  1.00 13.86 ? 89  VAL D CG2 1 
ATOM   5136 N  N   . GLU D 1 102 ? 5.755   31.418  39.923  1.00 9.46  ? 90  GLU D N   1 
ATOM   5137 C  CA  . GLU D 1 102 ? 4.723   31.118  40.914  1.00 10.93 ? 90  GLU D CA  1 
ATOM   5138 C  C   . GLU D 1 102 ? 3.427   30.644  40.272  1.00 13.77 ? 90  GLU D C   1 
ATOM   5139 O  O   . GLU D 1 102 ? 2.763   29.744  40.797  1.00 13.37 ? 90  GLU D O   1 
ATOM   5140 C  CB  . GLU D 1 102 ? 4.449   32.360  41.764  1.00 11.58 ? 90  GLU D CB  1 
ATOM   5141 C  CG  . GLU D 1 102 ? 5.664   32.777  42.577  1.00 13.51 ? 90  GLU D CG  1 
ATOM   5142 C  CD  . GLU D 1 102 ? 5.824   31.888  43.786  1.00 14.43 ? 90  GLU D CD  1 
ATOM   5143 O  OE1 . GLU D 1 102 ? 6.651   30.957  43.723  1.00 16.18 ? 90  GLU D OE1 1 
ATOM   5144 O  OE2 . GLU D 1 102 ? 5.073   32.095  44.762  1.00 18.39 ? 90  GLU D OE2 1 
ATOM   5145 N  N   . SER D 1 103 ? 3.041   31.260  39.157  1.00 13.39 ? 91  SER D N   1 
ATOM   5146 C  CA  . SER D 1 103 ? 1.961   30.760  38.317  1.00 13.19 ? 91  SER D CA  1 
ATOM   5147 C  C   . SER D 1 103 ? 2.303   31.005  36.857  1.00 15.27 ? 91  SER D C   1 
ATOM   5148 O  O   . SER D 1 103 ? 3.007   31.956  36.518  1.00 10.19 ? 91  SER D O   1 
ATOM   5149 C  CB  . SER D 1 103 ? 0.611   31.436  38.598  1.00 15.03 ? 91  SER D CB  1 
ATOM   5150 O  OG  . SER D 1 103 ? 0.177   31.324  39.946  1.00 17.55 ? 91  SER D OG  1 
ATOM   5151 N  N   . PHE D 1 104 ? 1.808   30.127  35.991  1.00 12.99 ? 92  PHE D N   1 
ATOM   5152 C  CA  . PHE D 1 104 ? 1.653   30.450  34.579  1.00 14.06 ? 92  PHE D CA  1 
ATOM   5153 C  C   . PHE D 1 104 ? 0.248   30.038  34.176  1.00 15.34 ? 92  PHE D C   1 
ATOM   5154 O  O   . PHE D 1 104 ? -0.418  29.272  34.869  1.00 16.13 ? 92  PHE D O   1 
ATOM   5155 C  CB  . PHE D 1 104 ? 2.713   29.792  33.673  1.00 13.15 ? 92  PHE D CB  1 
ATOM   5156 C  CG  . PHE D 1 104 ? 2.718   28.286  33.694  1.00 16.01 ? 92  PHE D CG  1 
ATOM   5157 C  CD1 . PHE D 1 104 ? 1.807   27.558  32.928  1.00 18.16 ? 92  PHE D CD1 1 
ATOM   5158 C  CD2 . PHE D 1 104 ? 3.677   27.596  34.422  1.00 16.60 ? 92  PHE D CD2 1 
ATOM   5159 C  CE1 . PHE D 1 104 ? 1.824   26.171  32.934  1.00 19.46 ? 92  PHE D CE1 1 
ATOM   5160 C  CE2 . PHE D 1 104 ? 3.702   26.201  34.429  1.00 20.45 ? 92  PHE D CE2 1 
ATOM   5161 C  CZ  . PHE D 1 104 ? 2.770   25.491  33.679  1.00 18.19 ? 92  PHE D CZ  1 
ATOM   5162 N  N   . SER D 1 105 ? -0.218  30.575  33.060  1.00 13.49 ? 93  SER D N   1 
ATOM   5163 C  CA  . SER D 1 105 ? -1.597  30.320  32.679  1.00 13.69 ? 93  SER D CA  1 
ATOM   5164 C  C   . SER D 1 105 ? -1.638  29.198  31.648  1.00 16.37 ? 93  SER D C   1 
ATOM   5165 O  O   . SER D 1 105 ? -1.657  28.018  32.006  1.00 19.40 ? 93  SER D O   1 
ATOM   5166 C  CB  . SER D 1 105 ? -2.238  31.599  32.155  1.00 15.59 ? 93  SER D CB  1 
ATOM   5167 O  OG  . SER D 1 105 ? -1.420  32.166  31.145  1.00 17.99 ? 93  SER D OG  1 
ATOM   5168 N  N   . THR D 1 106 ? -1.587  29.553  30.371  1.00 16.99 ? 94  THR D N   1 
ATOM   5169 C  CA  . THR D 1 106 ? -1.905  28.628  29.288  1.00 13.37 ? 94  THR D CA  1 
ATOM   5170 C  C   . THR D 1 106 ? -0.679  28.038  28.605  1.00 17.49 ? 94  THR D C   1 
ATOM   5171 O  O   . THR D 1 106 ? -0.833  27.201  27.708  1.00 20.10 ? 94  THR D O   1 
ATOM   5172 C  CB  . THR D 1 106 ? -2.768  29.344  28.247  1.00 15.91 ? 94  THR D CB  1 
ATOM   5173 O  OG1 . THR D 1 106 ? -2.077  30.517  27.796  1.00 17.50 ? 94  THR D OG1 1 
ATOM   5174 C  CG2 . THR D 1 106 ? -4.113  29.735  28.848  1.00 16.91 ? 94  THR D CG2 1 
ATOM   5175 N  N   . TYR D 1 107 ? 0.528   28.463  28.975  1.00 14.38 ? 95  TYR D N   1 
ATOM   5176 C  CA  . TYR D 1 107 ? 1.741   27.985  28.334  1.00 14.24 ? 95  TYR D CA  1 
ATOM   5177 C  C   . TYR D 1 107 ? 2.836   27.773  29.369  1.00 16.52 ? 95  TYR D C   1 
ATOM   5178 O  O   . TYR D 1 107 ? 3.180   28.706  30.098  1.00 15.09 ? 95  TYR D O   1 
ATOM   5179 C  CB  . TYR D 1 107 ? 2.228   28.979  27.277  1.00 14.35 ? 95  TYR D CB  1 
ATOM   5180 C  CG  . TYR D 1 107 ? 3.460   28.530  26.554  1.00 17.38 ? 95  TYR D CG  1 
ATOM   5181 C  CD1 . TYR D 1 107 ? 3.391   27.540  25.581  1.00 16.01 ? 95  TYR D CD1 1 
ATOM   5182 C  CD2 . TYR D 1 107 ? 4.700   29.098  26.833  1.00 15.74 ? 95  TYR D CD2 1 
ATOM   5183 C  CE1 . TYR D 1 107 ? 4.514   27.128  24.904  1.00 20.70 ? 95  TYR D CE1 1 
ATOM   5184 C  CE2 . TYR D 1 107 ? 5.838   28.682  26.166  1.00 19.11 ? 95  TYR D CE2 1 
ATOM   5185 C  CZ  . TYR D 1 107 ? 5.735   27.699  25.198  1.00 20.95 ? 95  TYR D CZ  1 
ATOM   5186 O  OH  . TYR D 1 107 ? 6.853   27.279  24.525  1.00 23.98 ? 95  TYR D OH  1 
ATOM   5187 N  N   . ASP D 1 108 ? 3.403   26.568  29.393  1.00 16.75 ? 96  ASP D N   1 
ATOM   5188 C  CA  . ASP D 1 108 ? 4.501   26.240  30.306  1.00 16.25 ? 96  ASP D CA  1 
ATOM   5189 C  C   . ASP D 1 108 ? 5.835   26.681  29.709  1.00 17.78 ? 96  ASP D C   1 
ATOM   5190 O  O   . ASP D 1 108 ? 6.270   26.115  28.702  1.00 18.43 ? 96  ASP D O   1 
ATOM   5191 C  CB  . ASP D 1 108 ? 4.527   24.736  30.580  1.00 15.79 ? 96  ASP D CB  1 
ATOM   5192 C  CG  . ASP D 1 108 ? 5.535   24.332  31.657  1.00 24.17 ? 96  ASP D CG  1 
ATOM   5193 O  OD1 . ASP D 1 108 ? 6.489   25.091  31.938  1.00 22.10 ? 96  ASP D OD1 1 
ATOM   5194 O  OD2 . ASP D 1 108 ? 5.369   23.232  32.223  1.00 25.37 ? 96  ASP D OD2 1 
ATOM   5195 N  N   . PRO D 1 109 ? 6.541   27.625  30.331  1.00 20.74 ? 97  PRO D N   1 
ATOM   5196 C  CA  . PRO D 1 109 ? 7.816   28.100  29.755  1.00 21.26 ? 97  PRO D CA  1 
ATOM   5197 C  C   . PRO D 1 109 ? 8.945   27.071  29.746  1.00 26.24 ? 97  PRO D C   1 
ATOM   5198 O  O   . PRO D 1 109 ? 9.946   27.288  29.049  1.00 27.17 ? 97  PRO D O   1 
ATOM   5199 C  CB  . PRO D 1 109 ? 8.175   29.288  30.649  1.00 23.36 ? 97  PRO D CB  1 
ATOM   5200 C  CG  . PRO D 1 109 ? 7.510   28.951  31.985  1.00 23.19 ? 97  PRO D CG  1 
ATOM   5201 C  CD  . PRO D 1 109 ? 6.195   28.313  31.585  1.00 18.05 ? 97  PRO D CD  1 
ATOM   5202 N  N   . SER D 1 110 ? 8.833   25.972  30.489  1.00 21.14 ? 98  SER D N   1 
ATOM   5203 C  CA  . SER D 1 110 ? 9.875   24.952  30.499  1.00 26.80 ? 98  SER D CA  1 
ATOM   5204 C  C   . SER D 1 110 ? 9.759   23.965  29.346  1.00 27.48 ? 98  SER D C   1 
ATOM   5205 O  O   . SER D 1 110 ? 10.577  23.038  29.258  1.00 28.29 ? 98  SER D O   1 
ATOM   5206 C  CB  . SER D 1 110 ? 9.838   24.187  31.823  1.00 24.02 ? 98  SER D CB  1 
ATOM   5207 O  OG  . SER D 1 110 ? 8.649   23.417  31.931  1.00 26.69 ? 98  SER D OG  1 
ATOM   5208 N  N   . THR D 1 111 ? 8.772   24.140  28.468  1.00 23.71 ? 99  THR D N   1 
ATOM   5209 C  CA  . THR D 1 111 ? 8.509   23.182  27.402  1.00 23.99 ? 99  THR D CA  1 
ATOM   5210 C  C   . THR D 1 111 ? 9.749   22.932  26.549  1.00 23.98 ? 99  THR D C   1 
ATOM   5211 O  O   . THR D 1 111 ? 10.378  23.869  26.051  1.00 21.82 ? 99  THR D O   1 
ATOM   5212 C  CB  . THR D 1 111 ? 7.358   23.713  26.542  1.00 25.00 ? 99  THR D CB  1 
ATOM   5213 O  OG1 . THR D 1 111 ? 6.228   23.959  27.393  1.00 20.23 ? 99  THR D OG1 1 
ATOM   5214 C  CG2 . THR D 1 111 ? 6.992   22.720  25.450  1.00 21.76 ? 99  THR D CG2 1 
ATOM   5215 N  N   . GLY D 1 112 ? 10.101  21.652  26.392  1.00 25.62 ? 100 GLY D N   1 
ATOM   5216 C  CA  . GLY D 1 112 ? 11.225  21.250  25.576  1.00 25.17 ? 100 GLY D CA  1 
ATOM   5217 C  C   . GLY D 1 112 ? 12.570  21.249  26.275  1.00 27.38 ? 100 GLY D C   1 
ATOM   5218 O  O   . GLY D 1 112 ? 13.564  20.813  25.671  1.00 22.99 ? 100 GLY D O   1 
ATOM   5219 N  N   . ALA D 1 113 ? 12.639  21.716  27.517  1.00 26.66 ? 101 ALA D N   1 
ATOM   5220 C  CA  . ALA D 1 113 ? 13.888  21.768  28.263  1.00 25.54 ? 101 ALA D CA  1 
ATOM   5221 C  C   . ALA D 1 113 ? 14.044  20.538  29.150  1.00 25.00 ? 101 ALA D C   1 
ATOM   5222 O  O   . ALA D 1 113 ? 13.066  19.990  29.665  1.00 26.49 ? 101 ALA D O   1 
ATOM   5223 C  CB  . ALA D 1 113 ? 13.957  23.034  29.120  1.00 23.07 ? 101 ALA D CB  1 
ATOM   5224 N  N   . GLN D 1 114 ? 15.293  20.109  29.328  1.00 24.37 ? 102 GLN D N   1 
ATOM   5225 C  CA  . GLN D 1 114 ? 15.566  19.000  30.231  1.00 29.40 ? 102 GLN D CA  1 
ATOM   5226 C  C   . GLN D 1 114 ? 15.368  19.441  31.674  1.00 25.78 ? 102 GLN D C   1 
ATOM   5227 O  O   . GLN D 1 114 ? 15.884  20.481  32.091  1.00 27.32 ? 102 GLN D O   1 
ATOM   5228 C  CB  . GLN D 1 114 ? 16.991  18.481  30.030  1.00 31.36 ? 102 GLN D CB  1 
ATOM   5229 C  CG  . GLN D 1 114 ? 17.252  17.139  30.704  1.00 34.61 ? 102 GLN D CG  1 
ATOM   5230 C  CD  . GLN D 1 114 ? 18.718  16.924  31.002  1.00 37.07 ? 102 GLN D CD  1 
ATOM   5231 O  OE1 . GLN D 1 114 ? 19.569  17.704  30.564  1.00 42.05 ? 102 GLN D OE1 1 
ATOM   5232 N  NE2 . GLN D 1 114 ? 19.027  15.863  31.752  1.00 35.52 ? 102 GLN D NE2 1 
ATOM   5233 N  N   . GLU D 1 115 ? 14.608  18.656  32.434  1.00 23.93 ? 103 GLU D N   1 
ATOM   5234 C  CA  . GLU D 1 115 ? 14.490  18.900  33.866  1.00 25.87 ? 103 GLU D CA  1 
ATOM   5235 C  C   . GLU D 1 115 ? 15.806  18.560  34.546  1.00 28.65 ? 103 GLU D C   1 
ATOM   5236 O  O   . GLU D 1 115 ? 16.374  17.488  34.316  1.00 28.25 ? 103 GLU D O   1 
ATOM   5237 C  CB  . GLU D 1 115 ? 13.352  18.071  34.462  1.00 29.22 ? 103 GLU D CB  1 
ATOM   5238 C  CG  . GLU D 1 115 ? 13.180  18.242  35.970  1.00 32.81 ? 103 GLU D CG  1 
ATOM   5239 C  CD  . GLU D 1 115 ? 11.946  17.530  36.503  1.00 39.51 ? 103 GLU D CD  1 
ATOM   5240 O  OE1 . GLU D 1 115 ? 11.872  17.306  37.734  1.00 36.85 ? 103 GLU D OE1 1 
ATOM   5241 O  OE2 . GLU D 1 115 ? 11.053  17.198  35.689  1.00 36.28 ? 103 GLU D OE2 1 
ATOM   5242 N  N   . LEU D 1 116 ? 16.291  19.474  35.388  1.00 21.19 ? 104 LEU D N   1 
ATOM   5243 C  CA  . LEU D 1 116 ? 17.592  19.328  36.024  1.00 20.90 ? 104 LEU D CA  1 
ATOM   5244 C  C   . LEU D 1 116 ? 17.512  18.980  37.499  1.00 29.89 ? 104 LEU D C   1 
ATOM   5245 O  O   . LEU D 1 116 ? 18.551  18.691  38.106  1.00 31.03 ? 104 LEU D O   1 
ATOM   5246 C  CB  . LEU D 1 116 ? 18.406  20.615  35.856  1.00 19.51 ? 104 LEU D CB  1 
ATOM   5247 C  CG  . LEU D 1 116 ? 18.687  21.042  34.417  1.00 23.09 ? 104 LEU D CG  1 
ATOM   5248 C  CD1 . LEU D 1 116 ? 19.527  22.314  34.395  1.00 21.26 ? 104 LEU D CD1 1 
ATOM   5249 C  CD2 . LEU D 1 116 ? 19.370  19.934  33.629  1.00 25.96 ? 104 LEU D CD2 1 
ATOM   5250 N  N   . GLY D 1 117 ? 16.325  18.978  38.080  1.00 29.13 ? 105 GLY D N   1 
ATOM   5251 C  CA  . GLY D 1 117 ? 16.161  18.695  39.489  1.00 27.69 ? 105 GLY D CA  1 
ATOM   5252 C  C   . GLY D 1 117 ? 14.929  19.402  40.014  1.00 27.18 ? 105 GLY D C   1 
ATOM   5253 O  O   . GLY D 1 117 ? 14.153  19.982  39.259  1.00 23.67 ? 105 GLY D O   1 
ATOM   5254 N  N   . THR D 1 118 ? 14.763  19.333  41.333  1.00 26.43 ? 106 THR D N   1 
ATOM   5255 C  CA  . THR D 1 118 ? 13.653  19.983  42.014  1.00 24.98 ? 106 THR D CA  1 
ATOM   5256 C  C   . THR D 1 118 ? 14.166  20.643  43.284  1.00 22.85 ? 106 THR D C   1 
ATOM   5257 O  O   . THR D 1 118 ? 15.237  20.303  43.790  1.00 28.84 ? 106 THR D O   1 
ATOM   5258 C  CB  . THR D 1 118 ? 12.532  18.993  42.366  1.00 30.53 ? 106 THR D CB  1 
ATOM   5259 O  OG1 . THR D 1 118 ? 13.057  17.976  43.231  1.00 34.59 ? 106 THR D OG1 1 
ATOM   5260 C  CG2 . THR D 1 118 ? 11.959  18.350  41.109  1.00 29.11 ? 106 THR D CG2 1 
ATOM   5261 N  N   . VAL D 1 119 ? 13.389  21.592  43.801  1.00 21.03 ? 107 VAL D N   1 
ATOM   5262 C  CA  . VAL D 1 119 ? 13.690  22.210  45.088  1.00 19.63 ? 107 VAL D CA  1 
ATOM   5263 C  C   . VAL D 1 119 ? 12.390  22.388  45.863  1.00 24.26 ? 107 VAL D C   1 
ATOM   5264 O  O   . VAL D 1 119 ? 11.380  22.834  45.307  1.00 23.00 ? 107 VAL D O   1 
ATOM   5265 C  CB  . VAL D 1 119 ? 14.438  23.551  44.937  1.00 23.16 ? 107 VAL D CB  1 
ATOM   5266 C  CG1 . VAL D 1 119 ? 13.677  24.530  44.043  1.00 20.19 ? 107 VAL D CG1 1 
ATOM   5267 C  CG2 . VAL D 1 119 ? 14.735  24.164  46.312  1.00 25.87 ? 107 VAL D CG2 1 
ATOM   5268 N  N   . GLU D 1 120 ? 12.408  22.006  47.138  1.00 23.84 ? 108 GLU D N   1 
ATOM   5269 C  CA  . GLU D 1 120 ? 11.286  22.189  48.046  1.00 22.97 ? 108 GLU D CA  1 
ATOM   5270 C  C   . GLU D 1 120 ? 11.521  23.459  48.852  1.00 23.62 ? 108 GLU D C   1 
ATOM   5271 O  O   . GLU D 1 120 ? 12.535  23.574  49.550  1.00 23.13 ? 108 GLU D O   1 
ATOM   5272 C  CB  . GLU D 1 120 ? 11.148  20.994  48.990  1.00 29.49 ? 108 GLU D CB  1 
ATOM   5273 C  CG  . GLU D 1 120 ? 10.628  19.716  48.362  1.00 34.48 ? 108 GLU D CG  1 
ATOM   5274 C  CD  . GLU D 1 120 ? 9.969   18.810  49.398  1.00 51.80 ? 108 GLU D CD  1 
ATOM   5275 O  OE1 . GLU D 1 120 ? 10.026  19.146  50.605  1.00 53.15 ? 108 GLU D OE1 1 
ATOM   5276 O  OE2 . GLU D 1 120 ? 9.399   17.766  49.011  1.00 53.87 ? 108 GLU D OE2 1 
ATOM   5277 N  N   . THR D 1 121 ? 10.589  24.402  48.766  1.00 23.13 ? 109 THR D N   1 
ATOM   5278 C  CA  . THR D 1 121 ? 10.734  25.652  49.493  1.00 22.78 ? 109 THR D CA  1 
ATOM   5279 C  C   . THR D 1 121 ? 9.388   26.360  49.525  1.00 21.89 ? 109 THR D C   1 
ATOM   5280 O  O   . THR D 1 121 ? 8.581   26.232  48.596  1.00 21.20 ? 109 THR D O   1 
ATOM   5281 C  CB  . THR D 1 121 ? 11.824  26.547  48.867  1.00 21.98 ? 109 THR D CB  1 
ATOM   5282 O  OG1 . THR D 1 121 ? 11.910  27.790  49.579  1.00 25.49 ? 109 THR D OG1 1 
ATOM   5283 C  CG2 . THR D 1 121 ? 11.538  26.831  47.411  1.00 20.54 ? 109 THR D CG2 1 
ATOM   5284 N  N   . ASP D 1 122 ? 9.150   27.077  50.625  1.00 21.14 ? 110 ASP D N   1 
ATOM   5285 C  CA  . ASP D 1 122 ? 7.967   27.919  50.789  1.00 19.30 ? 110 ASP D CA  1 
ATOM   5286 C  C   . ASP D 1 122 ? 6.688   27.124  50.525  1.00 25.92 ? 110 ASP D C   1 
ATOM   5287 O  O   . ASP D 1 122 ? 5.791   27.546  49.782  1.00 18.90 ? 110 ASP D O   1 
ATOM   5288 C  CB  . ASP D 1 122 ? 8.069   29.154  49.895  1.00 21.06 ? 110 ASP D CB  1 
ATOM   5289 C  CG  . ASP D 1 122 ? 9.371   29.925  50.121  1.00 20.27 ? 110 ASP D CG  1 
ATOM   5290 O  OD1 . ASP D 1 122 ? 9.529   30.494  51.220  1.00 21.76 ? 110 ASP D OD1 1 
ATOM   5291 O  OD2 . ASP D 1 122 ? 10.236  29.964  49.212  1.00 18.54 ? 110 ASP D OD2 1 
ATOM   5292 N  N   . ASP D 1 123 ? 6.634   25.933  51.133  1.00 21.84 ? 111 ASP D N   1 
ATOM   5293 C  CA  . ASP D 1 123 ? 5.458   25.059  51.102  1.00 23.19 ? 111 ASP D CA  1 
ATOM   5294 C  C   . ASP D 1 123 ? 5.102   24.614  49.689  1.00 25.84 ? 111 ASP D C   1 
ATOM   5295 O  O   . ASP D 1 123 ? 3.932   24.343  49.387  1.00 23.35 ? 111 ASP D O   1 
ATOM   5296 C  CB  . ASP D 1 123 ? 4.258   25.735  51.762  1.00 23.23 ? 111 ASP D CB  1 
ATOM   5297 C  CG  . ASP D 1 123 ? 4.246   25.552  53.259  1.00 34.72 ? 111 ASP D CG  1 
ATOM   5298 O  OD1 . ASP D 1 123 ? 4.758   26.448  53.955  1.00 35.75 ? 111 ASP D OD1 1 
ATOM   5299 O  OD2 . ASP D 1 123 ? 3.724   24.515  53.732  1.00 43.49 ? 111 ASP D OD2 1 
ATOM   5300 N  N   . GLY D 1 124 ? 6.103   24.527  48.814  1.00 23.67 ? 112 GLY D N   1 
ATOM   5301 C  CA  . GLY D 1 124 ? 5.876   24.086  47.454  1.00 22.51 ? 112 GLY D CA  1 
ATOM   5302 C  C   . GLY D 1 124 ? 7.073   23.326  46.927  1.00 20.90 ? 112 GLY D C   1 
ATOM   5303 O  O   . GLY D 1 124 ? 8.117   23.230  47.575  1.00 22.38 ? 112 GLY D O   1 
ATOM   5304 N  N   . THR D 1 125 ? 6.901   22.788  45.727  1.00 17.22 ? 113 THR D N   1 
ATOM   5305 C  CA  . THR D 1 125 ? 7.959   22.142  44.970  1.00 17.79 ? 113 THR D CA  1 
ATOM   5306 C  C   . THR D 1 125 ? 8.118   22.848  43.632  1.00 18.95 ? 113 THR D C   1 
ATOM   5307 O  O   . THR D 1 125 ? 7.125   23.191  42.982  1.00 19.03 ? 113 THR D O   1 
ATOM   5308 C  CB  . THR D 1 125 ? 7.651   20.654  44.740  1.00 23.14 ? 113 THR D CB  1 
ATOM   5309 O  OG1 . THR D 1 125 ? 7.455   20.011  46.006  1.00 27.25 ? 113 THR D OG1 1 
ATOM   5310 C  CG2 . THR D 1 125 ? 8.803   19.966  43.998  1.00 21.92 ? 113 THR D CG2 1 
ATOM   5311 N  N   . TYR D 1 126 ? 9.367   23.056  43.225  1.00 19.98 ? 114 TYR D N   1 
ATOM   5312 C  CA  . TYR D 1 126 ? 9.700   23.749  41.985  1.00 18.69 ? 114 TYR D CA  1 
ATOM   5313 C  C   . TYR D 1 126 ? 10.606  22.860  41.138  1.00 18.45 ? 114 TYR D C   1 
ATOM   5314 O  O   . TYR D 1 126 ? 11.573  22.294  41.650  1.00 18.71 ? 114 TYR D O   1 
ATOM   5315 C  CB  . TYR D 1 126 ? 10.407  25.083  42.284  1.00 16.73 ? 114 TYR D CB  1 
ATOM   5316 C  CG  . TYR D 1 126 ? 9.597   26.114  43.047  1.00 14.97 ? 114 TYR D CG  1 
ATOM   5317 C  CD1 . TYR D 1 126 ? 9.365   25.992  44.418  1.00 12.71 ? 114 TYR D CD1 1 
ATOM   5318 C  CD2 . TYR D 1 126 ? 9.084   27.233  42.394  1.00 13.74 ? 114 TYR D CD2 1 
ATOM   5319 C  CE1 . TYR D 1 126 ? 8.622   26.950  45.110  1.00 13.78 ? 114 TYR D CE1 1 
ATOM   5320 C  CE2 . TYR D 1 126 ? 8.350   28.191  43.073  1.00 12.18 ? 114 TYR D CE2 1 
ATOM   5321 C  CZ  . TYR D 1 126 ? 8.127   28.052  44.432  1.00 13.94 ? 114 TYR D CZ  1 
ATOM   5322 O  OH  . TYR D 1 126 ? 7.398   29.019  45.091  1.00 17.06 ? 114 TYR D OH  1 
ATOM   5323 N  N   . LYS D 1 127 ? 10.303  22.733  39.846  1.00 17.11 ? 115 LYS D N   1 
ATOM   5324 C  CA  . LYS D 1 127 ? 11.191  22.013  38.943  1.00 17.86 ? 115 LYS D CA  1 
ATOM   5325 C  C   . LYS D 1 127 ? 12.163  22.982  38.282  1.00 19.80 ? 115 LYS D C   1 
ATOM   5326 O  O   . LYS D 1 127 ? 11.783  24.089  37.893  1.00 17.54 ? 115 LYS D O   1 
ATOM   5327 C  CB  . LYS D 1 127 ? 10.393  21.256  37.878  1.00 20.45 ? 115 LYS D CB  1 
ATOM   5328 C  CG  . LYS D 1 127 ? 9.472   20.166  38.433  1.00 25.65 ? 115 LYS D CG  1 
ATOM   5329 C  CD  . LYS D 1 127 ? 8.508   19.679  37.349  1.00 26.26 ? 115 LYS D CD  1 
ATOM   5330 C  CE  . LYS D 1 127 ? 7.672   18.496  37.802  1.00 28.10 ? 115 LYS D CE  1 
ATOM   5331 N  NZ  . LYS D 1 127 ? 6.650   18.131  36.770  1.00 30.69 ? 115 LYS D NZ  1 
ATOM   5332 N  N   . ILE D 1 128 ? 13.422  22.548  38.143  1.00 17.66 ? 116 ILE D N   1 
ATOM   5333 C  CA  . ILE D 1 128 ? 14.517  23.374  37.638  1.00 16.63 ? 116 ILE D CA  1 
ATOM   5334 C  C   . ILE D 1 128 ? 14.795  23.054  36.176  1.00 20.35 ? 116 ILE D C   1 
ATOM   5335 O  O   . ILE D 1 128 ? 14.856  21.878  35.782  1.00 20.50 ? 116 ILE D O   1 
ATOM   5336 C  CB  . ILE D 1 128 ? 15.787  23.166  38.486  1.00 18.66 ? 116 ILE D CB  1 
ATOM   5337 C  CG1 . ILE D 1 128 ? 15.522  23.583  39.936  1.00 22.31 ? 116 ILE D CG1 1 
ATOM   5338 C  CG2 . ILE D 1 128 ? 16.962  23.911  37.887  1.00 19.98 ? 116 ILE D CG2 1 
ATOM   5339 C  CD1 . ILE D 1 128 ? 16.516  23.022  40.913  1.00 24.26 ? 116 ILE D CD1 1 
ATOM   5340 N  N   . TYR D 1 129 ? 15.004  24.104  35.375  1.00 16.34 ? 117 TYR D N   1 
ATOM   5341 C  CA  . TYR D 1 129 ? 15.320  23.982  33.957  1.00 15.73 ? 117 TYR D CA  1 
ATOM   5342 C  C   . TYR D 1 129 ? 16.301  25.069  33.548  1.00 21.72 ? 117 TYR D C   1 
ATOM   5343 O  O   . TYR D 1 129 ? 16.386  26.128  34.176  1.00 19.02 ? 117 TYR D O   1 
ATOM   5344 C  CB  . TYR D 1 129 ? 14.083  24.126  33.054  1.00 17.16 ? 117 TYR D CB  1 
ATOM   5345 C  CG  . TYR D 1 129 ? 12.915  23.259  33.419  1.00 19.35 ? 117 TYR D CG  1 
ATOM   5346 C  CD1 . TYR D 1 129 ? 12.051  23.624  34.441  1.00 16.86 ? 117 TYR D CD1 1 
ATOM   5347 C  CD2 . TYR D 1 129 ? 12.668  22.079  32.728  1.00 21.09 ? 117 TYR D CD2 1 
ATOM   5348 C  CE1 . TYR D 1 129 ? 10.966  22.828  34.781  1.00 22.43 ? 117 TYR D CE1 1 
ATOM   5349 C  CE2 . TYR D 1 129 ? 11.588  21.280  33.055  1.00 23.61 ? 117 TYR D CE2 1 
ATOM   5350 C  CZ  . TYR D 1 129 ? 10.741  21.661  34.078  1.00 24.41 ? 117 TYR D CZ  1 
ATOM   5351 O  OH  . TYR D 1 129 ? 9.666   20.865  34.404  1.00 28.96 ? 117 TYR D OH  1 
ATOM   5352 N  N   . GLN D 1 130 ? 17.014  24.803  32.456  1.00 20.40 ? 118 GLN D N   1 
ATOM   5353 C  CA  . GLN D 1 130 ? 17.828  25.794  31.771  1.00 21.21 ? 118 GLN D CA  1 
ATOM   5354 C  C   . GLN D 1 130 ? 17.452  25.830  30.297  1.00 26.03 ? 118 GLN D C   1 
ATOM   5355 O  O   . GLN D 1 130 ? 17.327  24.779  29.655  1.00 25.48 ? 118 GLN D O   1 
ATOM   5356 C  CB  . GLN D 1 130 ? 19.325  25.494  31.917  1.00 23.92 ? 118 GLN D CB  1 
ATOM   5357 C  CG  . GLN D 1 130 ? 20.200  26.355  31.017  1.00 27.92 ? 118 GLN D CG  1 
ATOM   5358 C  CD  . GLN D 1 130 ? 21.672  26.109  31.244  1.00 34.16 ? 118 GLN D CD  1 
ATOM   5359 O  OE1 . GLN D 1 130 ? 22.105  24.966  31.396  1.00 40.17 ? 118 GLN D OE1 1 
ATOM   5360 N  NE2 . GLN D 1 130 ? 22.449  27.181  31.286  1.00 30.35 ? 118 GLN D NE2 1 
ATOM   5361 N  N   . THR D 1 131 ? 17.275  27.037  29.766  1.00 20.91 ? 119 THR D N   1 
ATOM   5362 C  CA  . THR D 1 131 ? 17.060  27.266  28.343  1.00 23.93 ? 119 THR D CA  1 
ATOM   5363 C  C   . THR D 1 131 ? 18.045  28.332  27.870  1.00 24.25 ? 119 THR D C   1 
ATOM   5364 O  O   . THR D 1 131 ? 18.856  28.846  28.645  1.00 26.62 ? 119 THR D O   1 
ATOM   5365 C  CB  . THR D 1 131 ? 15.610  27.686  28.054  1.00 27.04 ? 119 THR D CB  1 
ATOM   5366 O  OG1 . THR D 1 131 ? 15.299  28.880  28.784  1.00 24.47 ? 119 THR D OG1 1 
ATOM   5367 C  CG2 . THR D 1 131 ? 14.626  26.578  28.456  1.00 24.60 ? 119 THR D CG2 1 
ATOM   5368 N  N   . THR D 1 132 ? 17.966  28.674  26.585  1.00 26.03 ? 120 THR D N   1 
ATOM   5369 C  CA  . THR D 1 132 ? 18.900  29.605  25.962  1.00 29.15 ? 120 THR D CA  1 
ATOM   5370 C  C   . THR D 1 132 ? 18.133  30.564  25.067  1.00 26.34 ? 120 THR D C   1 
ATOM   5371 O  O   . THR D 1 132 ? 17.143  30.175  24.444  1.00 31.72 ? 120 THR D O   1 
ATOM   5372 C  CB  . THR D 1 132 ? 19.970  28.858  25.144  1.00 27.78 ? 120 THR D CB  1 
ATOM   5373 O  OG1 . THR D 1 132 ? 20.688  27.969  26.006  1.00 36.19 ? 120 THR D OG1 1 
ATOM   5374 C  CG2 . THR D 1 132 ? 20.961  29.831  24.512  1.00 36.44 ? 120 THR D CG2 1 
ATOM   5375 N  N   . ARG D 1 133 ? 18.584  31.815  25.017  1.00 26.48 ? 121 ARG D N   1 
ATOM   5376 C  CA  . ARG D 1 133 ? 18.022  32.830  24.137  1.00 27.46 ? 121 ARG D CA  1 
ATOM   5377 C  C   . ARG D 1 133 ? 19.122  33.378  23.237  1.00 28.67 ? 121 ARG D C   1 
ATOM   5378 O  O   . ARG D 1 133 ? 20.222  33.677  23.710  1.00 31.03 ? 121 ARG D O   1 
ATOM   5379 C  CB  . ARG D 1 133 ? 17.377  33.955  24.943  1.00 27.16 ? 121 ARG D CB  1 
ATOM   5380 C  CG  . ARG D 1 133 ? 16.188  33.500  25.767  1.00 24.38 ? 121 ARG D CG  1 
ATOM   5381 C  CD  . ARG D 1 133 ? 14.913  33.566  24.947  1.00 25.30 ? 121 ARG D CD  1 
ATOM   5382 N  NE  . ARG D 1 133 ? 14.413  34.936  24.867  1.00 30.84 ? 121 ARG D NE  1 
ATOM   5383 C  CZ  . ARG D 1 133 ? 13.859  35.472  23.784  1.00 33.77 ? 121 ARG D CZ  1 
ATOM   5384 N  NH1 . ARG D 1 133 ? 13.733  34.754  22.675  1.00 33.60 ? 121 ARG D NH1 1 
ATOM   5385 N  NH2 . ARG D 1 133 ? 13.437  36.730  23.810  1.00 34.02 ? 121 ARG D NH2 1 
ATOM   5386 N  N   . GLU D 1 134 ? 18.824  33.509  21.946  1.00 30.65 ? 122 GLU D N   1 
ATOM   5387 C  CA  . GLU D 1 134 ? 19.784  33.967  20.948  1.00 35.36 ? 122 GLU D CA  1 
ATOM   5388 C  C   . GLU D 1 134 ? 19.271  35.236  20.281  1.00 33.22 ? 122 GLU D C   1 
ATOM   5389 O  O   . GLU D 1 134 ? 18.118  35.281  19.838  1.00 31.07 ? 122 GLU D O   1 
ATOM   5390 C  CB  . GLU D 1 134 ? 20.029  32.889  19.887  1.00 38.84 ? 122 GLU D CB  1 
ATOM   5391 C  CG  . GLU D 1 134 ? 20.119  31.482  20.442  1.00 41.04 ? 122 GLU D CG  1 
ATOM   5392 C  CD  . GLU D 1 134 ? 21.182  30.656  19.748  1.00 54.11 ? 122 GLU D CD  1 
ATOM   5393 O  OE1 . GLU D 1 134 ? 20.813  29.732  18.992  1.00 58.22 ? 122 GLU D OE1 1 
ATOM   5394 O  OE2 . GLU D 1 134 ? 22.384  30.935  19.957  1.00 55.23 ? 122 GLU D OE2 1 
ATOM   5395 N  N   . ASN D 1 135 ? 20.134  36.253  20.200  1.00 35.37 ? 123 ASN D N   1 
ATOM   5396 C  CA  . ASN D 1 135 ? 19.810  37.519  19.534  1.00 34.86 ? 123 ASN D CA  1 
ATOM   5397 C  C   . ASN D 1 135 ? 18.489  38.087  20.048  1.00 30.96 ? 123 ASN D C   1 
ATOM   5398 O  O   . ASN D 1 135 ? 17.586  38.431  19.281  1.00 28.63 ? 123 ASN D O   1 
ATOM   5399 C  CB  . ASN D 1 135 ? 19.781  37.346  18.013  1.00 37.53 ? 123 ASN D CB  1 
ATOM   5400 C  CG  . ASN D 1 135 ? 21.080  36.773  17.469  1.00 44.33 ? 123 ASN D CG  1 
ATOM   5401 O  OD1 . ASN D 1 135 ? 22.163  37.309  17.720  1.00 41.32 ? 123 ASN D OD1 1 
ATOM   5402 N  ND2 . ASN D 1 135 ? 20.978  35.672  16.729  1.00 44.47 ? 123 ASN D ND2 1 
ATOM   5403 N  N   . ALA D 1 136 ? 18.384  38.182  21.368  1.00 30.38 ? 124 ALA D N   1 
ATOM   5404 C  CA  . ALA D 1 136 ? 17.159  38.545  22.058  1.00 26.58 ? 124 ALA D CA  1 
ATOM   5405 C  C   . ALA D 1 136 ? 17.375  39.787  22.911  1.00 24.61 ? 124 ALA D C   1 
ATOM   5406 O  O   . ALA D 1 136 ? 18.513  40.103  23.280  1.00 26.59 ? 124 ALA D O   1 
ATOM   5407 C  CB  . ALA D 1 136 ? 16.683  37.381  22.941  1.00 25.61 ? 124 ALA D CB  1 
ATOM   5408 N  N   . PRO D 1 137 ? 16.306  40.519  23.241  1.00 23.68 ? 125 PRO D N   1 
ATOM   5409 C  CA  . PRO D 1 137 ? 16.456  41.676  24.135  1.00 24.04 ? 125 PRO D CA  1 
ATOM   5410 C  C   . PRO D 1 137 ? 17.000  41.254  25.493  1.00 23.94 ? 125 PRO D C   1 
ATOM   5411 O  O   . PRO D 1 137 ? 16.724  40.159  25.985  1.00 25.06 ? 125 PRO D O   1 
ATOM   5412 C  CB  . PRO D 1 137 ? 15.027  42.226  24.253  1.00 23.68 ? 125 PRO D CB  1 
ATOM   5413 C  CG  . PRO D 1 137 ? 14.308  41.706  23.045  1.00 24.77 ? 125 PRO D CG  1 
ATOM   5414 C  CD  . PRO D 1 137 ? 14.918  40.369  22.757  1.00 24.51 ? 125 PRO D CD  1 
ATOM   5415 N  N   . SER D 1 138 ? 17.793  42.134  26.096  1.00 21.83 ? 126 SER D N   1 
ATOM   5416 C  CA  . SER D 1 138 ? 18.341  41.871  27.420  1.00 21.00 ? 126 SER D CA  1 
ATOM   5417 C  C   . SER D 1 138 ? 18.680  43.201  28.079  1.00 24.03 ? 126 SER D C   1 
ATOM   5418 O  O   . SER D 1 138 ? 18.517  44.270  27.484  1.00 25.30 ? 126 SER D O   1 
ATOM   5419 C  CB  . SER D 1 138 ? 19.573  40.968  27.346  1.00 23.34 ? 126 SER D CB  1 
ATOM   5420 O  OG  . SER D 1 138 ? 20.717  41.721  26.977  1.00 25.55 ? 126 SER D OG  1 
ATOM   5421 N  N   . ILE D 1 139 ? 19.166  43.123  29.323  1.00 21.16 ? 127 ILE D N   1 
ATOM   5422 C  CA  . ILE D 1 139 ? 19.642  44.314  30.016  1.00 23.43 ? 127 ILE D CA  1 
ATOM   5423 C  C   . ILE D 1 139 ? 20.932  44.848  29.417  1.00 27.80 ? 127 ILE D C   1 
ATOM   5424 O  O   . ILE D 1 139 ? 21.382  45.939  29.797  1.00 27.83 ? 127 ILE D O   1 
ATOM   5425 C  CB  . ILE D 1 139 ? 19.848  44.036  31.521  1.00 21.95 ? 127 ILE D CB  1 
ATOM   5426 C  CG1 . ILE D 1 139 ? 20.827  42.879  31.734  1.00 18.34 ? 127 ILE D CG1 1 
ATOM   5427 C  CG2 . ILE D 1 139 ? 18.515  43.747  32.191  1.00 19.66 ? 127 ILE D CG2 1 
ATOM   5428 C  CD1 . ILE D 1 139 ? 21.424  42.834  33.134  1.00 19.08 ? 127 ILE D CD1 1 
ATOM   5429 N  N   . GLU D 1 140 ? 21.538  44.101  28.492  1.00 23.52 ? 128 GLU D N   1 
ATOM   5430 C  CA  . GLU D 1 140 ? 22.744  44.517  27.784  1.00 25.76 ? 128 GLU D CA  1 
ATOM   5431 C  C   . GLU D 1 140 ? 22.470  44.801  26.308  1.00 29.95 ? 128 GLU D C   1 
ATOM   5432 O  O   . GLU D 1 140 ? 23.405  44.821  25.501  1.00 35.90 ? 128 GLU D O   1 
ATOM   5433 C  CB  . GLU D 1 140 ? 23.832  43.449  27.924  1.00 25.78 ? 128 GLU D CB  1 
ATOM   5434 C  CG  . GLU D 1 140 ? 24.518  43.423  29.282  1.00 28.91 ? 128 GLU D CG  1 
ATOM   5435 C  CD  . GLU D 1 140 ? 25.524  42.294  29.412  1.00 32.79 ? 128 GLU D CD  1 
ATOM   5436 O  OE1 . GLU D 1 140 ? 25.976  42.020  30.545  1.00 28.01 ? 128 GLU D OE1 1 
ATOM   5437 O  OE2 . GLU D 1 140 ? 25.862  41.678  28.376  1.00 35.43 ? 128 GLU D OE2 1 
ATOM   5438 N  N   . GLY D 1 141 ? 21.206  45.020  25.941  1.00 27.42 ? 129 GLY D N   1 
ATOM   5439 C  CA  . GLY D 1 141 ? 20.827  45.095  24.546  1.00 29.98 ? 129 GLY D CA  1 
ATOM   5440 C  C   . GLY D 1 141 ? 20.718  43.705  23.945  1.00 30.78 ? 129 GLY D C   1 
ATOM   5441 O  O   . GLY D 1 141 ? 20.702  42.693  24.653  1.00 29.81 ? 129 GLY D O   1 
ATOM   5442 N  N   . THR D 1 142 ? 20.658  43.660  22.612  1.00 30.54 ? 130 THR D N   1 
ATOM   5443 C  CA  . THR D 1 142 ? 20.556  42.386  21.902  1.00 30.92 ? 130 THR D CA  1 
ATOM   5444 C  C   . THR D 1 142 ? 21.716  41.477  22.284  1.00 32.50 ? 130 THR D C   1 
ATOM   5445 O  O   . THR D 1 142 ? 22.883  41.880  22.235  1.00 29.32 ? 130 THR D O   1 
ATOM   5446 C  CB  . THR D 1 142 ? 20.543  42.616  20.391  1.00 32.47 ? 130 THR D CB  1 
ATOM   5447 O  OG1 . THR D 1 142 ? 19.424  43.438  20.041  1.00 37.38 ? 130 THR D OG1 1 
ATOM   5448 C  CG2 . THR D 1 142 ? 20.429  41.293  19.650  1.00 31.93 ? 130 THR D CG2 1 
ATOM   5449 N  N   . ALA D 1 143 ? 21.399  40.246  22.678  1.00 29.09 ? 131 ALA D N   1 
ATOM   5450 C  CA  . ALA D 1 143 ? 22.422  39.393  23.261  1.00 26.22 ? 131 ALA D CA  1 
ATOM   5451 C  C   . ALA D 1 143 ? 21.956  37.945  23.259  1.00 28.44 ? 131 ALA D C   1 
ATOM   5452 O  O   . ALA D 1 143 ? 20.781  37.640  23.035  1.00 28.51 ? 131 ALA D O   1 
ATOM   5453 C  CB  . ALA D 1 143 ? 22.767  39.841  24.685  1.00 29.07 ? 131 ALA D CB  1 
ATOM   5454 N  N   . THR D 1 144 ? 22.909  37.061  23.530  1.00 26.81 ? 132 THR D N   1 
ATOM   5455 C  CA  . THR D 1 144 ? 22.668  35.637  23.689  1.00 27.49 ? 132 THR D CA  1 
ATOM   5456 C  C   . THR D 1 144 ? 23.010  35.267  25.124  1.00 28.86 ? 132 THR D C   1 
ATOM   5457 O  O   . THR D 1 144 ? 24.063  35.661  25.637  1.00 28.97 ? 132 THR D O   1 
ATOM   5458 C  CB  . THR D 1 144 ? 23.494  34.832  22.677  1.00 34.25 ? 132 THR D CB  1 
ATOM   5459 O  OG1 . THR D 1 144 ? 23.131  35.239  21.349  1.00 35.15 ? 132 THR D OG1 1 
ATOM   5460 C  CG2 . THR D 1 144 ? 23.249  33.337  22.826  1.00 32.85 ? 132 THR D CG2 1 
ATOM   5461 N  N   . PHE D 1 145 ? 22.103  34.552  25.784  1.00 23.30 ? 133 PHE D N   1 
ATOM   5462 C  CA  . PHE D 1 145 ? 22.240  34.299  27.210  1.00 23.07 ? 133 PHE D CA  1 
ATOM   5463 C  C   . PHE D 1 145 ? 21.408  33.083  27.575  1.00 24.40 ? 133 PHE D C   1 
ATOM   5464 O  O   . PHE D 1 145 ? 20.487  32.694  26.850  1.00 24.56 ? 133 PHE D O   1 
ATOM   5465 C  CB  . PHE D 1 145 ? 21.794  35.503  28.046  1.00 20.08 ? 133 PHE D CB  1 
ATOM   5466 C  CG  . PHE D 1 145 ? 20.429  36.021  27.678  1.00 22.82 ? 133 PHE D CG  1 
ATOM   5467 C  CD1 . PHE D 1 145 ? 20.285  36.967  26.685  1.00 20.17 ? 133 PHE D CD1 1 
ATOM   5468 C  CD2 . PHE D 1 145 ? 19.292  35.559  28.331  1.00 19.76 ? 133 PHE D CD2 1 
ATOM   5469 C  CE1 . PHE D 1 145 ? 19.032  37.455  26.339  1.00 23.38 ? 133 PHE D CE1 1 
ATOM   5470 C  CE2 . PHE D 1 145 ? 18.040  36.030  27.993  1.00 21.44 ? 133 PHE D CE2 1 
ATOM   5471 C  CZ  . PHE D 1 145 ? 17.901  36.981  26.997  1.00 24.31 ? 133 PHE D CZ  1 
ATOM   5472 N  N   . ASN D 1 146 ? 21.735  32.507  28.721  1.00 21.81 ? 134 ASN D N   1 
ATOM   5473 C  CA  . ASN D 1 146 ? 20.966  31.408  29.272  1.00 22.49 ? 134 ASN D CA  1 
ATOM   5474 C  C   . ASN D 1 146 ? 19.851  31.936  30.168  1.00 22.44 ? 134 ASN D C   1 
ATOM   5475 O  O   . ASN D 1 146 ? 19.899  33.061  30.669  1.00 19.39 ? 134 ASN D O   1 
ATOM   5476 C  CB  . ASN D 1 146 ? 21.878  30.460  30.046  1.00 25.04 ? 134 ASN D CB  1 
ATOM   5477 C  CG  . ASN D 1 146 ? 22.823  29.699  29.128  1.00 31.56 ? 134 ASN D CG  1 
ATOM   5478 O  OD1 . ASN D 1 146 ? 22.485  29.418  27.974  1.00 29.73 ? 134 ASN D OD1 1 
ATOM   5479 N  ND2 . ASN D 1 146 ? 24.013  29.380  29.628  1.00 33.74 ? 134 ASN D ND2 1 
ATOM   5480 N  N   . GLN D 1 147 ? 18.824  31.109  30.336  1.00 20.54 ? 135 GLN D N   1 
ATOM   5481 C  CA  . GLN D 1 147 ? 17.716  31.375  31.243  1.00 17.52 ? 135 GLN D CA  1 
ATOM   5482 C  C   . GLN D 1 147 ? 17.651  30.258  32.270  1.00 16.91 ? 135 GLN D C   1 
ATOM   5483 O  O   . GLN D 1 147 ? 17.746  29.081  31.912  1.00 18.35 ? 135 GLN D O   1 
ATOM   5484 C  CB  . GLN D 1 147 ? 16.373  31.442  30.502  1.00 16.93 ? 135 GLN D CB  1 
ATOM   5485 C  CG  . GLN D 1 147 ? 16.215  32.530  29.465  1.00 21.97 ? 135 GLN D CG  1 
ATOM   5486 C  CD  . GLN D 1 147 ? 14.884  32.388  28.729  1.00 23.66 ? 135 GLN D CD  1 
ATOM   5487 O  OE1 . GLN D 1 147 ? 14.607  31.346  28.140  1.00 25.99 ? 135 GLN D OE1 1 
ATOM   5488 N  NE2 . GLN D 1 147 ? 14.055  33.428  28.768  1.00 20.04 ? 135 GLN D NE2 1 
ATOM   5489 N  N   . TYR D 1 148 ? 17.488  30.611  33.542  1.00 14.09 ? 136 TYR D N   1 
ATOM   5490 C  CA  . TYR D 1 148 ? 17.286  29.613  34.583  1.00 15.86 ? 136 TYR D CA  1 
ATOM   5491 C  C   . TYR D 1 148 ? 15.853  29.705  35.076  1.00 16.98 ? 136 TYR D C   1 
ATOM   5492 O  O   . TYR D 1 148 ? 15.323  30.804  35.274  1.00 15.22 ? 136 TYR D O   1 
ATOM   5493 C  CB  . TYR D 1 148 ? 18.249  29.789  35.769  1.00 14.66 ? 136 TYR D CB  1 
ATOM   5494 C  CG  . TYR D 1 148 ? 19.723  29.821  35.417  1.00 19.47 ? 136 TYR D CG  1 
ATOM   5495 C  CD1 . TYR D 1 148 ? 20.189  29.321  34.203  1.00 22.54 ? 136 TYR D CD1 1 
ATOM   5496 C  CD2 . TYR D 1 148 ? 20.647  30.346  36.308  1.00 19.26 ? 136 TYR D CD2 1 
ATOM   5497 C  CE1 . TYR D 1 148 ? 21.532  29.361  33.884  1.00 20.25 ? 136 TYR D CE1 1 
ATOM   5498 C  CE2 . TYR D 1 148 ? 21.996  30.391  35.999  1.00 23.13 ? 136 TYR D CE2 1 
ATOM   5499 C  CZ  . TYR D 1 148 ? 22.432  29.899  34.785  1.00 24.47 ? 136 TYR D CZ  1 
ATOM   5500 O  OH  . TYR D 1 148 ? 23.772  29.937  34.474  1.00 26.94 ? 136 TYR D OH  1 
ATOM   5501 N  N   . TRP D 1 149 ? 15.231  28.543  35.261  1.00 15.76 ? 137 TRP D N   1 
ATOM   5502 C  CA  . TRP D 1 149 ? 13.830  28.438  35.638  1.00 15.31 ? 137 TRP D CA  1 
ATOM   5503 C  C   . TRP D 1 149 ? 13.686  27.626  36.916  1.00 16.80 ? 137 TRP D C   1 
ATOM   5504 O  O   . TRP D 1 149 ? 14.336  26.587  37.083  1.00 16.47 ? 137 TRP D O   1 
ATOM   5505 C  CB  . TRP D 1 149 ? 12.995  27.773  34.517  1.00 15.06 ? 137 TRP D CB  1 
ATOM   5506 C  CG  . TRP D 1 149 ? 13.035  28.480  33.199  1.00 15.40 ? 137 TRP D CG  1 
ATOM   5507 C  CD1 . TRP D 1 149 ? 13.945  28.303  32.198  1.00 15.69 ? 137 TRP D CD1 1 
ATOM   5508 C  CD2 . TRP D 1 149 ? 12.115  29.472  32.735  1.00 12.98 ? 137 TRP D CD2 1 
ATOM   5509 N  NE1 . TRP D 1 149 ? 13.650  29.135  31.140  1.00 17.49 ? 137 TRP D NE1 1 
ATOM   5510 C  CE2 . TRP D 1 149 ? 12.534  29.865  31.447  1.00 14.87 ? 137 TRP D CE2 1 
ATOM   5511 C  CE3 . TRP D 1 149 ? 10.988  30.080  33.292  1.00 14.17 ? 137 TRP D CE3 1 
ATOM   5512 C  CZ2 . TRP D 1 149 ? 11.855  30.831  30.699  1.00 15.76 ? 137 TRP D CZ2 1 
ATOM   5513 C  CZ3 . TRP D 1 149 ? 10.316  31.040  32.552  1.00 15.77 ? 137 TRP D CZ3 1 
ATOM   5514 C  CH2 . TRP D 1 149 ? 10.752  31.408  31.269  1.00 15.39 ? 137 TRP D CH2 1 
ATOM   5515 N  N   . SER D 1 150 ? 12.843  28.125  37.816  1.00 14.76 ? 138 SER D N   1 
ATOM   5516 C  CA  . SER D 1 150 ? 12.254  27.366  38.914  1.00 16.02 ? 138 SER D CA  1 
ATOM   5517 C  C   . SER D 1 150 ? 10.749  27.484  38.747  1.00 17.31 ? 138 SER D C   1 
ATOM   5518 O  O   . SER D 1 150 ? 10.200  28.584  38.874  1.00 18.01 ? 138 SER D O   1 
ATOM   5519 C  CB  . SER D 1 150 ? 12.680  27.920  40.271  1.00 17.71 ? 138 SER D CB  1 
ATOM   5520 O  OG  . SER D 1 150 ? 13.813  27.256  40.768  1.00 21.45 ? 138 SER D OG  1 
ATOM   5521 N  N   . VAL D 1 151 ? 10.073  26.373  38.450  1.00 15.82 ? 139 VAL D N   1 
ATOM   5522 C  CA  . VAL D 1 151 ? 8.653   26.413  38.098  1.00 14.27 ? 139 VAL D CA  1 
ATOM   5523 C  C   . VAL D 1 151 ? 7.860   25.659  39.162  1.00 16.52 ? 139 VAL D C   1 
ATOM   5524 O  O   . VAL D 1 151 ? 8.005   24.437  39.305  1.00 16.67 ? 139 VAL D O   1 
ATOM   5525 C  CB  . VAL D 1 151 ? 8.396   25.839  36.699  1.00 15.22 ? 139 VAL D CB  1 
ATOM   5526 C  CG1 . VAL D 1 151 ? 6.930   26.045  36.300  1.00 14.42 ? 139 VAL D CG1 1 
ATOM   5527 C  CG2 . VAL D 1 151 ? 9.342   26.483  35.681  1.00 18.04 ? 139 VAL D CG2 1 
ATOM   5528 N  N   . ARG D 1 152 ? 7.018   26.385  39.899  1.00 14.07 ? 140 ARG D N   1 
ATOM   5529 C  CA  . ARG D 1 152 ? 6.230   25.787  40.977  1.00 15.49 ? 140 ARG D CA  1 
ATOM   5530 C  C   . ARG D 1 152 ? 5.273   24.753  40.400  1.00 18.53 ? 140 ARG D C   1 
ATOM   5531 O  O   . ARG D 1 152 ? 4.641   24.987  39.361  1.00 17.08 ? 140 ARG D O   1 
ATOM   5532 C  CB  . ARG D 1 152 ? 5.454   26.866  41.737  1.00 14.60 ? 140 ARG D CB  1 
ATOM   5533 C  CG  . ARG D 1 152 ? 4.969   26.450  43.129  1.00 16.46 ? 140 ARG D CG  1 
ATOM   5534 C  CD  . ARG D 1 152 ? 4.349   27.624  43.899  1.00 18.19 ? 140 ARG D CD  1 
ATOM   5535 N  NE  . ARG D 1 152 ? 3.668   27.214  45.129  1.00 18.83 ? 140 ARG D NE  1 
ATOM   5536 C  CZ  . ARG D 1 152 ? 4.223   27.234  46.338  1.00 22.05 ? 140 ARG D CZ  1 
ATOM   5537 N  NH1 . ARG D 1 152 ? 5.479   27.655  46.493  1.00 17.99 ? 140 ARG D NH1 1 
ATOM   5538 N  NH2 . ARG D 1 152 ? 3.524   26.840  47.399  1.00 25.90 ? 140 ARG D NH2 1 
ATOM   5539 N  N   . THR D 1 153 ? 5.188   23.590  41.054  1.00 16.08 ? 141 THR D N   1 
ATOM   5540 C  CA  . THR D 1 153 ? 4.313   22.542  40.535  1.00 22.48 ? 141 THR D CA  1 
ATOM   5541 C  C   . THR D 1 153 ? 2.842   22.812  40.826  1.00 22.66 ? 141 THR D C   1 
ATOM   5542 O  O   . THR D 1 153 ? 1.980   22.302  40.099  1.00 24.68 ? 141 THR D O   1 
ATOM   5543 C  CB  . THR D 1 153 ? 4.702   21.174  41.108  1.00 19.47 ? 141 THR D CB  1 
ATOM   5544 O  OG1 . THR D 1 153 ? 4.559   21.190  42.530  1.00 21.71 ? 141 THR D OG1 1 
ATOM   5545 C  CG2 . THR D 1 153 ? 6.126   20.820  40.734  1.00 21.28 ? 141 THR D CG2 1 
ATOM   5546 N  N   . ASP D 1 154 ? 2.544   23.600  41.861  1.00 17.67 ? 142 ASP D N   1 
ATOM   5547 C  CA  . ASP D 1 154 ? 1.185   23.968  42.260  1.00 23.42 ? 142 ASP D CA  1 
ATOM   5548 C  C   . ASP D 1 154 ? 1.082   25.498  42.242  1.00 23.97 ? 142 ASP D C   1 
ATOM   5549 O  O   . ASP D 1 154 ? 1.537   26.180  43.168  1.00 20.93 ? 142 ASP D O   1 
ATOM   5550 C  CB  . ASP D 1 154 ? 0.864   23.376  43.633  1.00 28.49 ? 142 ASP D CB  1 
ATOM   5551 C  CG  . ASP D 1 154 ? -0.409  23.939  44.237  1.00 34.37 ? 142 ASP D CG  1 
ATOM   5552 O  OD1 . ASP D 1 154 ? -1.373  24.165  43.479  1.00 35.94 ? 142 ASP D OD1 1 
ATOM   5553 O  OD2 . ASP D 1 154 ? -0.451  24.149  45.473  1.00 39.01 ? 142 ASP D OD2 1 
ATOM   5554 N  N   . HIS D 1 155 ? 0.481   26.046  41.188  1.00 17.47 ? 143 HIS D N   1 
ATOM   5555 C  CA  . HIS D 1 155 ? 0.505   27.490  40.992  1.00 15.89 ? 143 HIS D CA  1 
ATOM   5556 C  C   . HIS D 1 155 ? -0.253  28.226  42.089  1.00 16.00 ? 143 HIS D C   1 
ATOM   5557 O  O   . HIS D 1 155 ? -1.267  27.753  42.608  1.00 18.00 ? 143 HIS D O   1 
ATOM   5558 C  CB  . HIS D 1 155 ? -0.084  27.845  39.629  1.00 16.21 ? 143 HIS D CB  1 
ATOM   5559 C  CG  . HIS D 1 155 ? 0.608   27.169  38.486  1.00 17.65 ? 143 HIS D CG  1 
ATOM   5560 N  ND1 . HIS D 1 155 ? 0.138   27.223  37.194  1.00 16.75 ? 143 HIS D ND1 1 
ATOM   5561 C  CD2 . HIS D 1 155 ? 1.740   26.427  38.442  1.00 19.49 ? 143 HIS D CD2 1 
ATOM   5562 C  CE1 . HIS D 1 155 ? 0.946   26.543  36.401  1.00 17.21 ? 143 HIS D CE1 1 
ATOM   5563 N  NE2 . HIS D 1 155 ? 1.925   26.045  37.135  1.00 21.82 ? 143 HIS D NE2 1 
ATOM   5564 N  N   . ARG D 1 156 ? 0.252   29.406  42.440  1.00 14.09 ? 144 ARG D N   1 
ATOM   5565 C  CA  . ARG D 1 156 ? -0.391  30.235  43.446  1.00 15.54 ? 144 ARG D CA  1 
ATOM   5566 C  C   . ARG D 1 156 ? -0.152  31.701  43.122  1.00 16.11 ? 144 ARG D C   1 
ATOM   5567 O  O   . ARG D 1 156 ? 0.718   32.048  42.316  1.00 13.93 ? 144 ARG D O   1 
ATOM   5568 C  CB  . ARG D 1 156 ? 0.136   29.918  44.843  1.00 16.23 ? 144 ARG D CB  1 
ATOM   5569 C  CG  . ARG D 1 156 ? 1.602   30.244  44.964  1.00 14.56 ? 144 ARG D CG  1 
ATOM   5570 C  CD  . ARG D 1 156 ? 2.127   30.088  46.381  1.00 14.86 ? 144 ARG D CD  1 
ATOM   5571 N  NE  . ARG D 1 156 ? 3.491   30.604  46.445  1.00 15.31 ? 144 ARG D NE  1 
ATOM   5572 C  CZ  . ARG D 1 156 ? 4.219   30.666  47.554  1.00 17.60 ? 144 ARG D CZ  1 
ATOM   5573 N  NH1 . ARG D 1 156 ? 3.717   30.226  48.705  1.00 16.40 ? 144 ARG D NH1 1 
ATOM   5574 N  NH2 . ARG D 1 156 ? 5.456   31.157  47.506  1.00 16.70 ? 144 ARG D NH2 1 
ATOM   5575 N  N   . VAL D 1 157 ? -0.943  32.559  43.761  1.00 13.80 ? 145 VAL D N   1 
ATOM   5576 C  CA  . VAL D 1 157 ? -0.805  34.006  43.654  1.00 14.77 ? 145 VAL D CA  1 
ATOM   5577 C  C   . VAL D 1 157 ? -0.649  34.538  45.068  1.00 15.18 ? 145 VAL D C   1 
ATOM   5578 O  O   . VAL D 1 157 ? -1.643  34.712  45.785  1.00 16.81 ? 145 VAL D O   1 
ATOM   5579 C  CB  . VAL D 1 157 ? -1.996  34.664  42.961  1.00 13.16 ? 145 VAL D CB  1 
ATOM   5580 C  CG1 . VAL D 1 157 ? -1.779  36.168  42.872  1.00 16.20 ? 145 VAL D CG1 1 
ATOM   5581 C  CG2 . VAL D 1 157 ? -2.213  34.057  41.584  1.00 16.16 ? 145 VAL D CG2 1 
ATOM   5582 N  N   . GLY D 1 158 ? 0.587   34.813  45.467  1.00 15.82 ? 146 GLY D N   1 
ATOM   5583 C  CA  . GLY D 1 158 ? 0.840   35.370  46.778  1.00 17.23 ? 146 GLY D CA  1 
ATOM   5584 C  C   . GLY D 1 158 ? 1.642   34.420  47.630  1.00 19.26 ? 146 GLY D C   1 
ATOM   5585 O  O   . GLY D 1 158 ? 1.647   33.210  47.395  1.00 21.60 ? 146 GLY D O   1 
ATOM   5586 N  N   . GLY D 1 159 ? 2.334   34.956  48.618  1.00 16.31 ? 147 GLY D N   1 
ATOM   5587 C  CA  . GLY D 1 159 ? 3.068   34.113  49.527  1.00 16.43 ? 147 GLY D CA  1 
ATOM   5588 C  C   . GLY D 1 159 ? 4.470   34.643  49.702  1.00 17.34 ? 147 GLY D C   1 
ATOM   5589 O  O   . GLY D 1 159 ? 4.741   35.824  49.458  1.00 17.84 ? 147 GLY D O   1 
ATOM   5590 N  N   . THR D 1 160 ? 5.352   33.747  50.137  1.00 15.84 ? 148 THR D N   1 
ATOM   5591 C  CA  . THR D 1 160 ? 6.745   34.046  50.433  1.00 17.54 ? 148 THR D CA  1 
ATOM   5592 C  C   . THR D 1 160 ? 7.630   33.296  49.454  1.00 17.12 ? 148 THR D C   1 
ATOM   5593 O  O   . THR D 1 160 ? 7.382   32.122  49.161  1.00 16.02 ? 148 THR D O   1 
ATOM   5594 C  CB  . THR D 1 160 ? 7.093   33.627  51.869  1.00 16.45 ? 148 THR D CB  1 
ATOM   5595 O  OG1 . THR D 1 160 ? 6.212   34.288  52.786  1.00 20.25 ? 148 THR D OG1 1 
ATOM   5596 C  CG2 . THR D 1 160 ? 8.519   34.006  52.215  1.00 18.91 ? 148 THR D CG2 1 
ATOM   5597 N  N   . VAL D 1 161 ? 8.662   33.968  48.944  1.00 13.41 ? 149 VAL D N   1 
ATOM   5598 C  CA  . VAL D 1 161 ? 9.656   33.332  48.082  1.00 12.17 ? 149 VAL D CA  1 
ATOM   5599 C  C   . VAL D 1 161 ? 11.022  33.551  48.724  1.00 15.41 ? 149 VAL D C   1 
ATOM   5600 O  O   . VAL D 1 161 ? 11.507  34.688  48.800  1.00 15.84 ? 149 VAL D O   1 
ATOM   5601 C  CB  . VAL D 1 161 ? 9.625   33.879  46.646  1.00 13.27 ? 149 VAL D CB  1 
ATOM   5602 C  CG1 . VAL D 1 161 ? 10.791  33.306  45.850  1.00 12.88 ? 149 VAL D CG1 1 
ATOM   5603 C  CG2 . VAL D 1 161 ? 8.288   33.533  45.969  1.00 15.32 ? 149 VAL D CG2 1 
ATOM   5604 N  N   . THR D 1 162 ? 11.632  32.467  49.200  1.00 14.59 ? 150 THR D N   1 
ATOM   5605 C  CA  . THR D 1 162 ? 12.984  32.499  49.761  1.00 16.06 ? 150 THR D CA  1 
ATOM   5606 C  C   . THR D 1 162 ? 13.955  32.320  48.603  1.00 13.97 ? 150 THR D C   1 
ATOM   5607 O  O   . THR D 1 162 ? 14.339  31.204  48.257  1.00 15.83 ? 150 THR D O   1 
ATOM   5608 C  CB  . THR D 1 162 ? 13.155  31.409  50.813  1.00 19.77 ? 150 THR D CB  1 
ATOM   5609 O  OG1 . THR D 1 162 ? 12.095  31.496  51.771  1.00 17.33 ? 150 THR D OG1 1 
ATOM   5610 C  CG2 . THR D 1 162 ? 14.498  31.557  51.526  1.00 17.00 ? 150 THR D CG2 1 
ATOM   5611 N  N   . THR D 1 163 ? 14.367  33.438  47.992  1.00 15.67 ? 151 THR D N   1 
ATOM   5612 C  CA  . THR D 1 163 ? 15.119  33.344  46.744  1.00 16.18 ? 151 THR D CA  1 
ATOM   5613 C  C   . THR D 1 163 ? 16.434  32.593  46.926  1.00 17.12 ? 151 THR D C   1 
ATOM   5614 O  O   . THR D 1 163 ? 16.876  31.898  46.007  1.00 15.75 ? 151 THR D O   1 
ATOM   5615 C  CB  . THR D 1 163 ? 15.372  34.739  46.159  1.00 20.76 ? 151 THR D CB  1 
ATOM   5616 O  OG1 . THR D 1 163 ? 16.081  35.542  47.111  1.00 20.46 ? 151 THR D OG1 1 
ATOM   5617 C  CG2 . THR D 1 163 ? 14.054  35.426  45.818  1.00 17.22 ? 151 THR D CG2 1 
ATOM   5618 N  N   . GLN D 1 164 ? 17.067  32.695  48.101  1.00 16.16 ? 152 GLN D N   1 
ATOM   5619 C  CA  . GLN D 1 164 ? 18.336  31.995  48.302  1.00 16.41 ? 152 GLN D CA  1 
ATOM   5620 C  C   . GLN D 1 164 ? 18.200  30.489  48.117  1.00 20.54 ? 152 GLN D C   1 
ATOM   5621 O  O   . GLN D 1 164 ? 19.136  29.840  47.633  1.00 20.60 ? 152 GLN D O   1 
ATOM   5622 C  CB  . GLN D 1 164 ? 18.900  32.280  49.694  1.00 19.76 ? 152 GLN D CB  1 
ATOM   5623 C  CG  . GLN D 1 164 ? 20.298  31.716  49.888  1.00 22.91 ? 152 GLN D CG  1 
ATOM   5624 C  CD  . GLN D 1 164 ? 21.331  32.432  49.028  1.00 25.08 ? 152 GLN D CD  1 
ATOM   5625 O  OE1 . GLN D 1 164 ? 21.423  33.659  49.053  1.00 30.21 ? 152 GLN D OE1 1 
ATOM   5626 N  NE2 . GLN D 1 164 ? 22.112  31.668  48.263  1.00 26.90 ? 152 GLN D NE2 1 
ATOM   5627 N  N   . ASN D 1 165 ? 17.051  29.915  48.489  1.00 18.89 ? 153 ASN D N   1 
ATOM   5628 C  CA  . ASN D 1 165 ? 16.864  28.476  48.321  1.00 17.94 ? 153 ASN D CA  1 
ATOM   5629 C  C   . ASN D 1 165 ? 16.857  28.095  46.849  1.00 18.49 ? 153 ASN D C   1 
ATOM   5630 O  O   . ASN D 1 165 ? 17.349  27.024  46.475  1.00 19.72 ? 153 ASN D O   1 
ATOM   5631 C  CB  . ASN D 1 165 ? 15.571  28.030  48.997  1.00 19.96 ? 153 ASN D CB  1 
ATOM   5632 C  CG  . ASN D 1 165 ? 15.658  28.095  50.492  1.00 24.34 ? 153 ASN D CG  1 
ATOM   5633 O  OD1 . ASN D 1 165 ? 16.754  28.116  51.063  1.00 25.64 ? 153 ASN D OD1 1 
ATOM   5634 N  ND2 . ASN D 1 165 ? 14.510  28.117  51.147  1.00 23.14 ? 153 ASN D ND2 1 
ATOM   5635 N  N   . HIS D 1 166 ? 16.307  28.964  45.995  1.00 15.38 ? 154 HIS D N   1 
ATOM   5636 C  CA  . HIS D 1 166 ? 16.352  28.715  44.560  1.00 15.77 ? 154 HIS D CA  1 
ATOM   5637 C  C   . HIS D 1 166 ? 17.759  28.897  44.009  1.00 19.78 ? 154 HIS D C   1 
ATOM   5638 O  O   . HIS D 1 166 ? 18.237  28.073  43.220  1.00 18.19 ? 154 HIS D O   1 
ATOM   5639 C  CB  . HIS D 1 166 ? 15.370  29.637  43.835  1.00 15.91 ? 154 HIS D CB  1 
ATOM   5640 C  CG  . HIS D 1 166 ? 13.947  29.393  44.209  1.00 13.58 ? 154 HIS D CG  1 
ATOM   5641 N  ND1 . HIS D 1 166 ? 13.165  28.459  43.562  1.00 13.59 ? 154 HIS D ND1 1 
ATOM   5642 C  CD2 . HIS D 1 166 ? 13.166  29.942  45.169  1.00 13.00 ? 154 HIS D CD2 1 
ATOM   5643 C  CE1 . HIS D 1 166 ? 11.964  28.440  44.112  1.00 12.64 ? 154 HIS D CE1 1 
ATOM   5644 N  NE2 . HIS D 1 166 ? 11.932  29.339  45.079  1.00 14.75 ? 154 HIS D NE2 1 
ATOM   5645 N  N   . PHE D 1 167 ? 18.433  29.986  44.392  1.00 17.57 ? 155 PHE D N   1 
ATOM   5646 C  CA  . PHE D 1 167 ? 19.779  30.211  43.883  1.00 19.94 ? 155 PHE D CA  1 
ATOM   5647 C  C   . PHE D 1 167 ? 20.694  29.056  44.276  1.00 20.91 ? 155 PHE D C   1 
ATOM   5648 O  O   . PHE D 1 167 ? 21.495  28.587  43.461  1.00 18.14 ? 155 PHE D O   1 
ATOM   5649 C  CB  . PHE D 1 167 ? 20.328  31.547  44.393  1.00 17.74 ? 155 PHE D CB  1 
ATOM   5650 C  CG  . PHE D 1 167 ? 19.517  32.754  43.959  1.00 17.51 ? 155 PHE D CG  1 
ATOM   5651 C  CD1 . PHE D 1 167 ? 18.694  32.699  42.839  1.00 17.14 ? 155 PHE D CD1 1 
ATOM   5652 C  CD2 . PHE D 1 167 ? 19.585  33.941  44.671  1.00 21.94 ? 155 PHE D CD2 1 
ATOM   5653 C  CE1 . PHE D 1 167 ? 17.952  33.810  42.437  1.00 19.90 ? 155 PHE D CE1 1 
ATOM   5654 C  CE2 . PHE D 1 167 ? 18.843  35.052  44.276  1.00 23.60 ? 155 PHE D CE2 1 
ATOM   5655 C  CZ  . PHE D 1 167 ? 18.031  34.989  43.159  1.00 21.31 ? 155 PHE D CZ  1 
ATOM   5656 N  N   . ASP D 1 168 ? 20.532  28.552  45.503  1.00 19.70 ? 156 ASP D N   1 
ATOM   5657 C  CA  . ASP D 1 168 ? 21.299  27.397  45.977  1.00 21.34 ? 156 ASP D CA  1 
ATOM   5658 C  C   . ASP D 1 168 ? 21.027  26.156  45.128  1.00 25.01 ? 156 ASP D C   1 
ATOM   5659 O  O   . ASP D 1 168 ? 21.955  25.420  44.776  1.00 24.94 ? 156 ASP D O   1 
ATOM   5660 C  CB  . ASP D 1 168 ? 20.954  27.102  47.438  1.00 23.43 ? 156 ASP D CB  1 
ATOM   5661 C  CG  . ASP D 1 168 ? 21.592  28.083  48.419  1.00 27.53 ? 156 ASP D CG  1 
ATOM   5662 O  OD1 . ASP D 1 168 ? 22.487  28.854  48.025  1.00 31.11 ? 156 ASP D OD1 1 
ATOM   5663 O  OD2 . ASP D 1 168 ? 21.184  28.079  49.599  1.00 32.75 ? 156 ASP D OD2 1 
ATOM   5664 N  N   . ALA D 1 169 ? 19.753  25.898  44.808  1.00 20.42 ? 157 ALA D N   1 
ATOM   5665 C  CA  . ALA D 1 169 ? 19.402  24.729  44.007  1.00 20.09 ? 157 ALA D CA  1 
ATOM   5666 C  C   . ALA D 1 169 ? 19.925  24.843  42.579  1.00 19.90 ? 157 ALA D C   1 
ATOM   5667 O  O   . ALA D 1 169 ? 20.395  23.852  42.007  1.00 21.40 ? 157 ALA D O   1 
ATOM   5668 C  CB  . ALA D 1 169 ? 17.886  24.529  44.013  1.00 18.99 ? 157 ALA D CB  1 
ATOM   5669 N  N   . TRP D 1 170 ? 19.831  26.034  41.975  1.00 18.45 ? 158 TRP D N   1 
ATOM   5670 C  CA  . TRP D 1 170 ? 20.423  26.236  40.655  1.00 16.20 ? 158 TRP D CA  1 
ATOM   5671 C  C   . TRP D 1 170 ? 21.922  25.994  40.695  1.00 21.11 ? 158 TRP D C   1 
ATOM   5672 O  O   . TRP D 1 170 ? 22.487  25.389  39.779  1.00 19.06 ? 158 TRP D O   1 
ATOM   5673 C  CB  . TRP D 1 170 ? 20.151  27.648  40.144  1.00 17.65 ? 158 TRP D CB  1 
ATOM   5674 C  CG  . TRP D 1 170 ? 18.705  27.918  39.932  1.00 16.41 ? 158 TRP D CG  1 
ATOM   5675 C  CD1 . TRP D 1 170 ? 17.710  26.993  39.809  1.00 24.84 ? 158 TRP D CD1 1 
ATOM   5676 C  CD2 . TRP D 1 170 ? 18.076  29.201  39.840  1.00 17.83 ? 158 TRP D CD2 1 
ATOM   5677 N  NE1 . TRP D 1 170 ? 16.497  27.622  39.639  1.00 24.76 ? 158 TRP D NE1 1 
ATOM   5678 C  CE2 . TRP D 1 170 ? 16.696  28.978  39.654  1.00 20.54 ? 158 TRP D CE2 1 
ATOM   5679 C  CE3 . TRP D 1 170 ? 18.544  30.518  39.895  1.00 19.24 ? 158 TRP D CE3 1 
ATOM   5680 C  CZ2 . TRP D 1 170 ? 15.780  30.023  39.522  1.00 18.98 ? 158 TRP D CZ2 1 
ATOM   5681 C  CZ3 . TRP D 1 170 ? 17.625  31.556  39.762  1.00 15.82 ? 158 TRP D CZ3 1 
ATOM   5682 C  CH2 . TRP D 1 170 ? 16.264  31.300  39.580  1.00 18.03 ? 158 TRP D CH2 1 
ATOM   5683 N  N   . LYS D 1 171 ? 22.584  26.493  41.736  1.00 22.33 ? 159 LYS D N   1 
ATOM   5684 C  CA  . LYS D 1 171 ? 24.011  26.250  41.882  1.00 22.54 ? 159 LYS D CA  1 
ATOM   5685 C  C   . LYS D 1 171 ? 24.307  24.756  41.877  1.00 24.60 ? 159 LYS D C   1 
ATOM   5686 O  O   . LYS D 1 171 ? 25.125  24.274  41.083  1.00 25.94 ? 159 LYS D O   1 
ATOM   5687 C  CB  . LYS D 1 171 ? 24.510  26.901  43.166  1.00 23.81 ? 159 LYS D CB  1 
ATOM   5688 C  CG  . LYS D 1 171 ? 26.000  26.774  43.351  1.00 30.05 ? 159 LYS D CG  1 
ATOM   5689 C  CD  . LYS D 1 171 ? 26.399  27.134  44.759  1.00 33.03 ? 159 LYS D CD  1 
ATOM   5690 C  CE  . LYS D 1 171 ? 27.849  26.792  44.975  1.00 35.17 ? 159 LYS D CE  1 
ATOM   5691 N  NZ  . LYS D 1 171 ? 28.057  25.776  46.044  1.00 37.42 ? 159 LYS D NZ  1 
ATOM   5692 N  N   . ASN D 1 172 ? 23.619  24.003  42.739  1.00 25.61 ? 160 ASN D N   1 
ATOM   5693 C  CA  . ASN D 1 172 ? 23.842  22.562  42.829  1.00 27.70 ? 160 ASN D CA  1 
ATOM   5694 C  C   . ASN D 1 172 ? 23.555  21.853  41.512  1.00 31.19 ? 160 ASN D C   1 
ATOM   5695 O  O   . ASN D 1 172 ? 24.131  20.792  41.245  1.00 32.85 ? 160 ASN D O   1 
ATOM   5696 C  CB  . ASN D 1 172 ? 22.979  21.967  43.940  1.00 27.16 ? 160 ASN D CB  1 
ATOM   5697 C  CG  . ASN D 1 172 ? 23.399  22.437  45.312  1.00 37.99 ? 160 ASN D CG  1 
ATOM   5698 O  OD1 . ASN D 1 172 ? 24.565  22.767  45.537  1.00 39.42 ? 160 ASN D OD1 1 
ATOM   5699 N  ND2 . ASN D 1 172 ? 22.448  22.477  46.241  1.00 36.10 ? 160 ASN D ND2 1 
ATOM   5700 N  N   . ALA D 1 173 ? 22.671  22.406  40.682  1.00 24.60 ? 161 ALA D N   1 
ATOM   5701 C  CA  . ALA D 1 173 ? 22.394  21.817  39.378  1.00 27.04 ? 161 ALA D CA  1 
ATOM   5702 C  C   . ALA D 1 173 ? 23.408  22.220  38.316  1.00 31.23 ? 161 ALA D C   1 
ATOM   5703 O  O   . ALA D 1 173 ? 23.222  21.880  37.144  1.00 33.58 ? 161 ALA D O   1 
ATOM   5704 C  CB  . ALA D 1 173 ? 20.978  22.200  38.913  1.00 24.70 ? 161 ALA D CB  1 
ATOM   5705 N  N   . GLY D 1 174 ? 24.461  22.943  38.686  1.00 30.54 ? 162 GLY D N   1 
ATOM   5706 C  CA  . GLY D 1 174 ? 25.474  23.355  37.733  1.00 25.46 ? 162 GLY D CA  1 
ATOM   5707 C  C   . GLY D 1 174 ? 25.186  24.637  36.989  1.00 29.65 ? 162 GLY D C   1 
ATOM   5708 O  O   . GLY D 1 174 ? 25.816  24.889  35.956  1.00 31.87 ? 162 GLY D O   1 
ATOM   5709 N  N   . LEU D 1 175 ? 24.255  25.459  37.471  1.00 27.41 ? 163 LEU D N   1 
ATOM   5710 C  CA  . LEU D 1 175 ? 23.888  26.709  36.808  1.00 27.44 ? 163 LEU D CA  1 
ATOM   5711 C  C   . LEU D 1 175 ? 24.593  27.864  37.517  1.00 25.20 ? 163 LEU D C   1 
ATOM   5712 O  O   . LEU D 1 175 ? 24.260  28.196  38.658  1.00 28.72 ? 163 LEU D O   1 
ATOM   5713 C  CB  . LEU D 1 175 ? 22.372  26.895  36.819  1.00 26.58 ? 163 LEU D CB  1 
ATOM   5714 C  CG  . LEU D 1 175 ? 21.563  25.707  36.291  1.00 25.54 ? 163 LEU D CG  1 
ATOM   5715 C  CD1 . LEU D 1 175 ? 20.059  26.003  36.323  1.00 23.95 ? 163 LEU D CD1 1 
ATOM   5716 C  CD2 . LEU D 1 175 ? 22.012  25.337  34.887  1.00 28.70 ? 163 LEU D CD2 1 
ATOM   5717 N  N   . GLU D 1 176 ? 25.556  28.480  36.834  1.00 24.65 ? 164 GLU D N   1 
ATOM   5718 C  CA  . GLU D 1 176 ? 26.352  29.552  37.423  1.00 28.22 ? 164 GLU D CA  1 
ATOM   5719 C  C   . GLU D 1 176 ? 25.594  30.875  37.404  1.00 24.86 ? 164 GLU D C   1 
ATOM   5720 O  O   . GLU D 1 176 ? 25.043  31.268  36.374  1.00 27.93 ? 164 GLU D O   1 
ATOM   5721 C  CB  . GLU D 1 176 ? 27.672  29.711  36.671  1.00 31.74 ? 164 GLU D CB  1 
ATOM   5722 C  CG  . GLU D 1 176 ? 28.539  30.838  37.212  1.00 35.99 ? 164 GLU D CG  1 
ATOM   5723 C  CD  . GLU D 1 176 ? 29.732  31.165  36.325  1.00 44.17 ? 164 GLU D CD  1 
ATOM   5724 O  OE1 . GLU D 1 176 ? 30.735  31.691  36.859  1.00 44.65 ? 164 GLU D OE1 1 
ATOM   5725 O  OE2 . GLU D 1 176 ? 29.667  30.905  35.103  1.00 38.72 ? 164 GLU D OE2 1 
ATOM   5726 N  N   . MET D 1 177 ? 25.597  31.575  38.534  1.00 25.15 ? 165 MET D N   1 
ATOM   5727 C  CA  . MET D 1 177 ? 25.003  32.903  38.642  1.00 24.85 ? 165 MET D CA  1 
ATOM   5728 C  C   . MET D 1 177 ? 26.102  33.956  38.673  1.00 26.66 ? 165 MET D C   1 
ATOM   5729 O  O   . MET D 1 177 ? 27.152  33.748  39.286  1.00 26.45 ? 165 MET D O   1 
ATOM   5730 C  CB  . MET D 1 177 ? 24.151  33.019  39.906  1.00 27.98 ? 165 MET D CB  1 
ATOM   5731 C  CG  . MET D 1 177 ? 23.017  32.021  39.977  1.00 34.43 ? 165 MET D CG  1 
ATOM   5732 S  SD  . MET D 1 177 ? 21.619  32.668  39.060  1.00 40.15 ? 165 MET D SD  1 
ATOM   5733 C  CE  . MET D 1 177 ? 21.007  33.881  40.224  1.00 26.47 ? 165 MET D CE  1 
ATOM   5734 N  N   . GLY D 1 178 ? 25.854  35.090  38.028  1.00 20.98 ? 166 GLY D N   1 
ATOM   5735 C  CA  . GLY D 1 178 ? 26.809  36.178  37.972  1.00 23.77 ? 166 GLY D CA  1 
ATOM   5736 C  C   . GLY D 1 178 ? 26.554  37.235  39.028  1.00 23.96 ? 166 GLY D C   1 
ATOM   5737 O  O   . GLY D 1 178 ? 25.956  36.978  40.079  1.00 26.63 ? 166 GLY D O   1 
ATOM   5738 N  N   . THR D 1 179 ? 27.026  38.449  38.743  1.00 21.56 ? 167 THR D N   1 
ATOM   5739 C  CA  . THR D 1 179 ? 26.759  39.591  39.609  1.00 22.16 ? 167 THR D CA  1 
ATOM   5740 C  C   . THR D 1 179 ? 25.318  40.053  39.413  1.00 19.07 ? 167 THR D C   1 
ATOM   5741 O  O   . THR D 1 179 ? 24.872  40.245  38.280  1.00 21.00 ? 167 THR D O   1 
ATOM   5742 C  CB  . THR D 1 179 ? 27.728  40.728  39.286  1.00 27.24 ? 167 THR D CB  1 
ATOM   5743 O  OG1 . THR D 1 179 ? 29.077  40.256  39.409  1.00 29.35 ? 167 THR D OG1 1 
ATOM   5744 C  CG2 . THR D 1 179 ? 27.516  41.897  40.222  1.00 25.32 ? 167 THR D CG2 1 
ATOM   5745 N  N   . HIS D 1 180 ? 24.591  40.235  40.514  1.00 22.99 ? 168 HIS D N   1 
ATOM   5746 C  CA  . HIS D 1 180 ? 23.159  40.504  40.415  1.00 19.68 ? 168 HIS D CA  1 
ATOM   5747 C  C   . HIS D 1 180 ? 22.885  41.886  39.832  1.00 18.68 ? 168 HIS D C   1 
ATOM   5748 O  O   . HIS D 1 180 ? 23.466  42.884  40.273  1.00 20.43 ? 168 HIS D O   1 
ATOM   5749 C  CB  . HIS D 1 180 ? 22.500  40.388  41.788  1.00 20.15 ? 168 HIS D CB  1 
ATOM   5750 C  CG  . HIS D 1 180 ? 22.238  38.978  42.213  1.00 24.28 ? 168 HIS D CG  1 
ATOM   5751 N  ND1 . HIS D 1 180 ? 20.986  38.406  42.164  1.00 27.15 ? 168 HIS D ND1 1 
ATOM   5752 C  CD2 . HIS D 1 180 ? 23.071  38.020  42.685  1.00 32.50 ? 168 HIS D CD2 1 
ATOM   5753 C  CE1 . HIS D 1 180 ? 21.056  37.159  42.595  1.00 30.67 ? 168 HIS D CE1 1 
ATOM   5754 N  NE2 . HIS D 1 180 ? 22.311  36.899  42.917  1.00 29.76 ? 168 HIS D NE2 1 
ATOM   5755 N  N   . ASN D 1 181 ? 22.002  41.934  38.827  1.00 15.19 ? 169 ASN D N   1 
ATOM   5756 C  CA  . ASN D 1 181 ? 21.330  43.166  38.420  1.00 14.77 ? 169 ASN D CA  1 
ATOM   5757 C  C   . ASN D 1 181 ? 19.949  43.184  39.074  1.00 13.06 ? 169 ASN D C   1 
ATOM   5758 O  O   . ASN D 1 181 ? 19.820  42.783  40.231  1.00 15.34 ? 169 ASN D O   1 
ATOM   5759 C  CB  . ASN D 1 181 ? 21.240  43.271  36.890  1.00 16.21 ? 169 ASN D CB  1 
ATOM   5760 C  CG  . ASN D 1 181 ? 21.032  44.707  36.398  1.00 21.30 ? 169 ASN D CG  1 
ATOM   5761 O  OD1 . ASN D 1 181 ? 19.898  45.159  36.203  1.00 18.60 ? 169 ASN D OD1 1 
ATOM   5762 N  ND2 . ASN D 1 181 ? 22.130  45.419  36.171  1.00 28.34 ? 169 ASN D ND2 1 
ATOM   5763 N  N   . TYR D 1 182 ? 18.906  43.610  38.368  1.00 13.23 ? 170 TYR D N   1 
ATOM   5764 C  CA  . TYR D 1 182 ? 17.682  43.822  39.133  1.00 13.38 ? 170 TYR D CA  1 
ATOM   5765 C  C   . TYR D 1 182 ? 16.991  42.503  39.471  1.00 13.71 ? 170 TYR D C   1 
ATOM   5766 O  O   . TYR D 1 182 ? 17.236  41.458  38.861  1.00 13.62 ? 170 TYR D O   1 
ATOM   5767 C  CB  . TYR D 1 182 ? 16.717  44.774  38.405  1.00 13.01 ? 170 TYR D CB  1 
ATOM   5768 C  CG  . TYR D 1 182 ? 16.046  44.311  37.106  1.00 12.31 ? 170 TYR D CG  1 
ATOM   5769 C  CD1 . TYR D 1 182 ? 15.053  43.338  37.111  1.00 13.37 ? 170 TYR D CD1 1 
ATOM   5770 C  CD2 . TYR D 1 182 ? 16.372  44.909  35.892  1.00 14.03 ? 170 TYR D CD2 1 
ATOM   5771 C  CE1 . TYR D 1 182 ? 14.432  42.941  35.923  1.00 13.39 ? 170 TYR D CE1 1 
ATOM   5772 C  CE2 . TYR D 1 182 ? 15.762  44.527  34.713  1.00 16.43 ? 170 TYR D CE2 1 
ATOM   5773 C  CZ  . TYR D 1 182 ? 14.788  43.544  34.735  1.00 14.69 ? 170 TYR D CZ  1 
ATOM   5774 O  OH  . TYR D 1 182 ? 14.176  43.161  33.559  1.00 14.41 ? 170 TYR D OH  1 
ATOM   5775 N  N   . MET D 1 183 ? 16.118  42.573  40.473  1.00 9.98  ? 171 MET D N   1 
ATOM   5776 C  CA  . MET D 1 183 ? 15.219  41.476  40.812  1.00 11.50 ? 171 MET D CA  1 
ATOM   5777 C  C   . MET D 1 183 ? 13.862  42.068  41.165  1.00 11.27 ? 171 MET D C   1 
ATOM   5778 O  O   . MET D 1 183 ? 13.774  42.934  42.040  1.00 11.74 ? 171 MET D O   1 
ATOM   5779 C  CB  . MET D 1 183 ? 15.766  40.644  41.988  1.00 12.10 ? 171 MET D CB  1 
ATOM   5780 C  CG  . MET D 1 183 ? 14.895  39.421  42.303  1.00 13.29 ? 171 MET D CG  1 
ATOM   5781 S  SD  . MET D 1 183 ? 15.594  38.363  43.599  1.00 15.09 ? 171 MET D SD  1 
ATOM   5782 C  CE  . MET D 1 183 ? 15.362  39.389  45.041  1.00 18.48 ? 171 MET D CE  1 
ATOM   5783 N  N   . ILE D 1 184 ? 12.803  41.599  40.497  1.00 10.28 ? 172 ILE D N   1 
ATOM   5784 C  CA  . ILE D 1 184 ? 11.467  42.153  40.681  1.00 9.89  ? 172 ILE D CA  1 
ATOM   5785 C  C   . ILE D 1 184 ? 10.466  41.011  40.793  1.00 9.90  ? 172 ILE D C   1 
ATOM   5786 O  O   . ILE D 1 184 ? 10.731  39.885  40.375  1.00 11.37 ? 172 ILE D O   1 
ATOM   5787 C  CB  . ILE D 1 184 ? 11.051  43.098  39.534  1.00 9.70  ? 172 ILE D CB  1 
ATOM   5788 C  CG1 . ILE D 1 184 ? 11.117  42.365  38.186  1.00 9.96  ? 172 ILE D CG1 1 
ATOM   5789 C  CG2 . ILE D 1 184 ? 11.925  44.368  39.530  1.00 11.70 ? 172 ILE D CG2 1 
ATOM   5790 C  CD1 . ILE D 1 184 ? 10.660  43.213  37.026  1.00 12.26 ? 172 ILE D CD1 1 
ATOM   5791 N  N   . VAL D 1 185 ? 9.310   41.312  41.375  1.00 11.35 ? 173 VAL D N   1 
ATOM   5792 C  CA  . VAL D 1 185 ? 8.151   40.422  41.288  1.00 9.04  ? 173 VAL D CA  1 
ATOM   5793 C  C   . VAL D 1 185 ? 7.388   40.835  40.037  1.00 8.54  ? 173 VAL D C   1 
ATOM   5794 O  O   . VAL D 1 185 ? 6.743   41.885  40.012  1.00 10.98 ? 173 VAL D O   1 
ATOM   5795 C  CB  . VAL D 1 185 ? 7.268   40.491  42.536  1.00 12.17 ? 173 VAL D CB  1 
ATOM   5796 C  CG1 . VAL D 1 185 ? 6.090   39.549  42.381  1.00 14.75 ? 173 VAL D CG1 1 
ATOM   5797 C  CG2 . VAL D 1 185 ? 8.092   40.119  43.774  1.00 12.43 ? 173 VAL D CG2 1 
ATOM   5798 N  N   . ALA D 1 186 ? 7.482   40.026  38.994  1.00 8.26  ? 174 ALA D N   1 
ATOM   5799 C  CA  . ALA D 1 186 ? 7.110   40.463  37.655  1.00 9.27  ? 174 ALA D CA  1 
ATOM   5800 C  C   . ALA D 1 186 ? 5.853   39.770  37.152  1.00 12.02 ? 174 ALA D C   1 
ATOM   5801 O  O   . ALA D 1 186 ? 5.665   38.566  37.350  1.00 12.24 ? 174 ALA D O   1 
ATOM   5802 C  CB  . ALA D 1 186 ? 8.252   40.208  36.665  1.00 11.17 ? 174 ALA D CB  1 
ATOM   5803 N  N   . THR D 1 187 ? 5.010   40.545  36.481  1.00 8.44  ? 175 THR D N   1 
ATOM   5804 C  CA  . THR D 1 187 ? 3.942   40.031  35.641  1.00 9.65  ? 175 THR D CA  1 
ATOM   5805 C  C   . THR D 1 187 ? 4.432   40.082  34.199  1.00 12.32 ? 175 THR D C   1 
ATOM   5806 O  O   . THR D 1 187 ? 4.886   41.134  33.731  1.00 10.65 ? 175 THR D O   1 
ATOM   5807 C  CB  . THR D 1 187 ? 2.670   40.861  35.793  1.00 9.83  ? 175 THR D CB  1 
ATOM   5808 O  OG1 . THR D 1 187 ? 2.222   40.808  37.156  1.00 12.61 ? 175 THR D OG1 1 
ATOM   5809 C  CG2 . THR D 1 187 ? 1.577   40.315  34.875  1.00 10.65 ? 175 THR D CG2 1 
ATOM   5810 N  N   . ALA D 1 188 ? 4.376   38.947  33.509  1.00 10.59 ? 176 ALA D N   1 
ATOM   5811 C  CA  . ALA D 1 188 ? 4.809   38.869  32.122  1.00 11.24 ? 176 ALA D CA  1 
ATOM   5812 C  C   . ALA D 1 188 ? 3.661   38.363  31.270  1.00 11.61 ? 176 ALA D C   1 
ATOM   5813 O  O   . ALA D 1 188 ? 2.799   37.625  31.752  1.00 11.67 ? 176 ALA D O   1 
ATOM   5814 C  CB  . ALA D 1 188 ? 6.012   37.933  31.950  1.00 11.45 ? 176 ALA D CB  1 
ATOM   5815 N  N   . GLY D 1 189 ? 3.659   38.761  30.005  1.00 14.05 ? 177 GLY D N   1 
ATOM   5816 C  CA  . GLY D 1 189 ? 2.605   38.347  29.091  1.00 13.57 ? 177 GLY D CA  1 
ATOM   5817 C  C   . GLY D 1 189 ? 3.104   38.317  27.666  1.00 13.46 ? 177 GLY D C   1 
ATOM   5818 O  O   . GLY D 1 189 ? 4.073   39.001  27.307  1.00 12.33 ? 177 GLY D O   1 
ATOM   5819 N  N   . TYR D 1 190 ? 2.455   37.486  26.852  1.00 14.27 ? 178 TYR D N   1 
ATOM   5820 C  CA  . TYR D 1 190 ? 2.720   37.477  25.419  1.00 14.99 ? 178 TYR D CA  1 
ATOM   5821 C  C   . TYR D 1 190 ? 1.455   37.076  24.686  1.00 12.81 ? 178 TYR D C   1 
ATOM   5822 O  O   . TYR D 1 190 ? 0.851   36.046  25.012  1.00 13.28 ? 178 TYR D O   1 
ATOM   5823 C  CB  . TYR D 1 190 ? 3.844   36.518  25.048  1.00 19.74 ? 178 TYR D CB  1 
ATOM   5824 C  CG  . TYR D 1 190 ? 4.116   36.489  23.554  1.00 26.97 ? 178 TYR D CG  1 
ATOM   5825 C  CD1 . TYR D 1 190 ? 4.800   37.524  22.932  1.00 26.68 ? 178 TYR D CD1 1 
ATOM   5826 C  CD2 . TYR D 1 190 ? 3.674   35.434  22.765  1.00 29.69 ? 178 TYR D CD2 1 
ATOM   5827 C  CE1 . TYR D 1 190 ? 5.062   37.502  21.569  1.00 26.72 ? 178 TYR D CE1 1 
ATOM   5828 C  CE2 . TYR D 1 190 ? 3.932   35.409  21.409  1.00 31.33 ? 178 TYR D CE2 1 
ATOM   5829 C  CZ  . TYR D 1 190 ? 4.630   36.440  20.816  1.00 34.03 ? 178 TYR D CZ  1 
ATOM   5830 O  OH  . TYR D 1 190 ? 4.884   36.410  19.459  1.00 36.75 ? 178 TYR D OH  1 
ATOM   5831 N  N   . GLN D 1 191 ? 1.082   37.886  23.699  1.00 13.69 ? 179 GLN D N   1 
ATOM   5832 C  CA  . GLN D 1 191 ? -0.110  37.682  22.871  1.00 16.57 ? 179 GLN D CA  1 
ATOM   5833 C  C   . GLN D 1 191 ? -1.307  37.244  23.711  1.00 14.08 ? 179 GLN D C   1 
ATOM   5834 O  O   . GLN D 1 191 ? -1.930  36.205  23.479  1.00 15.41 ? 179 GLN D O   1 
ATOM   5835 C  CB  . GLN D 1 191 ? 0.189   36.698  21.734  1.00 18.72 ? 179 GLN D CB  1 
ATOM   5836 C  CG  . GLN D 1 191 ? 1.147   37.320  20.707  1.00 22.75 ? 179 GLN D CG  1 
ATOM   5837 C  CD  . GLN D 1 191 ? 1.264   36.547  19.400  1.00 30.80 ? 179 GLN D CD  1 
ATOM   5838 O  OE1 . GLN D 1 191 ? 0.723   35.451  19.252  1.00 35.94 ? 179 GLN D OE1 1 
ATOM   5839 N  NE2 . GLN D 1 191 ? 1.988   37.123  18.444  1.00 34.86 ? 179 GLN D NE2 1 
ATOM   5840 N  N   . SER D 1 192 ? -1.632  38.080  24.700  1.00 13.67 ? 180 SER D N   1 
ATOM   5841 C  CA  . SER D 1 192 ? -2.734  37.803  25.612  1.00 13.23 ? 180 SER D CA  1 
ATOM   5842 C  C   . SER D 1 192 ? -3.358  39.119  26.066  1.00 15.20 ? 180 SER D C   1 
ATOM   5843 O  O   . SER D 1 192 ? -2.945  40.205  25.652  1.00 13.58 ? 180 SER D O   1 
ATOM   5844 C  CB  . SER D 1 192 ? -2.264  36.967  26.812  1.00 12.79 ? 180 SER D CB  1 
ATOM   5845 O  OG  . SER D 1 192 ? -1.226  37.613  27.540  1.00 12.98 ? 180 SER D OG  1 
ATOM   5846 N  N   . SER D 1 193 ? -4.371  39.010  26.926  1.00 13.77 ? 181 SER D N   1 
ATOM   5847 C  CA  . SER D 1 193 ? -4.962  40.152  27.604  1.00 13.90 ? 181 SER D CA  1 
ATOM   5848 C  C   . SER D 1 193 ? -5.017  39.827  29.088  1.00 11.83 ? 181 SER D C   1 
ATOM   5849 O  O   . SER D 1 193 ? -4.868  38.671  29.487  1.00 17.18 ? 181 SER D O   1 
ATOM   5850 C  CB  . SER D 1 193 ? -6.374  40.462  27.091  1.00 14.84 ? 181 SER D CB  1 
ATOM   5851 O  OG  . SER D 1 193 ? -6.349  40.790  25.709  1.00 17.78 ? 181 SER D OG  1 
ATOM   5852 N  N   . GLY D 1 194 ? -5.216  40.841  29.913  1.00 16.10 ? 182 GLY D N   1 
ATOM   5853 C  CA  . GLY D 1 194 ? -5.358  40.579  31.329  1.00 13.84 ? 182 GLY D CA  1 
ATOM   5854 C  C   . GLY D 1 194 ? -5.179  41.830  32.165  1.00 13.80 ? 182 GLY D C   1 
ATOM   5855 O  O   . GLY D 1 194 ? -5.052  42.940  31.655  1.00 13.73 ? 182 GLY D O   1 
ATOM   5856 N  N   . SER D 1 195 ? -5.192  41.612  33.475  1.00 11.33 ? 183 SER D N   1 
ATOM   5857 C  CA  . SER D 1 195 ? -4.872  42.663  34.424  1.00 12.80 ? 183 SER D CA  1 
ATOM   5858 C  C   . SER D 1 195 ? -4.198  42.010  35.620  1.00 13.43 ? 183 SER D C   1 
ATOM   5859 O  O   . SER D 1 195 ? -4.331  40.806  35.850  1.00 15.84 ? 183 SER D O   1 
ATOM   5860 C  CB  . SER D 1 195 ? -6.116  43.449  34.847  1.00 17.39 ? 183 SER D CB  1 
ATOM   5861 O  OG  . SER D 1 195 ? -7.012  42.629  35.574  1.00 23.41 ? 183 SER D OG  1 
ATOM   5862 N  N   . ALA D 1 196 ? -3.432  42.811  36.351  1.00 13.79 ? 184 ALA D N   1 
ATOM   5863 C  CA  . ALA D 1 196 ? -2.814  42.337  37.584  1.00 12.95 ? 184 ALA D CA  1 
ATOM   5864 C  C   . ALA D 1 196 ? -2.567  43.524  38.500  1.00 14.35 ? 184 ALA D C   1 
ATOM   5865 O  O   . ALA D 1 196 ? -2.320  44.638  38.038  1.00 13.62 ? 184 ALA D O   1 
ATOM   5866 C  CB  . ALA D 1 196 ? -1.503  41.593  37.305  1.00 13.82 ? 184 ALA D CB  1 
ATOM   5867 N  N   . SER D 1 197 ? -2.638  43.273  39.808  1.00 11.36 ? 185 SER D N   1 
ATOM   5868 C  CA  . SER D 1 197 ? -2.281  44.278  40.813  1.00 13.64 ? 185 SER D CA  1 
ATOM   5869 C  C   . SER D 1 197 ? -1.502  43.549  41.887  1.00 13.23 ? 185 SER D C   1 
ATOM   5870 O  O   . SER D 1 197 ? -2.076  42.739  42.617  1.00 14.30 ? 185 SER D O   1 
ATOM   5871 C  CB  . SER D 1 197 ? -3.499  44.977  41.417  1.00 18.44 ? 185 SER D CB  1 
ATOM   5872 O  OG  . SER D 1 197 ? -4.258  45.647  40.430  1.00 28.03 ? 185 SER D OG  1 
ATOM   5873 N  N   . ILE D 1 198 ? -0.206  43.818  41.975  1.00 12.30 ? 186 ILE D N   1 
ATOM   5874 C  CA  . ILE D 1 198 ? 0.696   43.055  42.825  1.00 12.35 ? 186 ILE D CA  1 
ATOM   5875 C  C   . ILE D 1 198 ? 1.382   44.012  43.786  1.00 15.12 ? 186 ILE D C   1 
ATOM   5876 O  O   . ILE D 1 198 ? 1.781   45.113  43.394  1.00 13.62 ? 186 ILE D O   1 
ATOM   5877 C  CB  . ILE D 1 198 ? 1.731   42.290  41.972  1.00 15.30 ? 186 ILE D CB  1 
ATOM   5878 C  CG1 . ILE D 1 198 ? 1.035   41.264  41.071  1.00 13.96 ? 186 ILE D CG1 1 
ATOM   5879 C  CG2 . ILE D 1 198 ? 2.785   41.631  42.841  1.00 11.51 ? 186 ILE D CG2 1 
ATOM   5880 C  CD1 . ILE D 1 198 ? 0.312   40.153  41.830  1.00 13.87 ? 186 ILE D CD1 1 
ATOM   5881 N  N   . THR D 1 199 ? 1.514   43.597  45.047  1.00 12.29 ? 187 THR D N   1 
ATOM   5882 C  CA  . THR D 1 199 ? 2.191   44.397  46.057  1.00 16.09 ? 187 THR D CA  1 
ATOM   5883 C  C   . THR D 1 199 ? 3.386   43.619  46.575  1.00 15.95 ? 187 THR D C   1 
ATOM   5884 O  O   . THR D 1 199 ? 3.229   42.520  47.122  1.00 15.81 ? 187 THR D O   1 
ATOM   5885 C  CB  . THR D 1 199 ? 1.252   44.756  47.213  1.00 21.00 ? 187 THR D CB  1 
ATOM   5886 O  OG1 . THR D 1 199 ? 0.204   45.595  46.723  1.00 20.11 ? 187 THR D OG1 1 
ATOM   5887 C  CG2 . THR D 1 199 ? 2.022   45.510  48.308  1.00 23.03 ? 187 THR D CG2 1 
ATOM   5888 N  N   . VAL D 1 200 ? 4.573   44.189  46.400  1.00 16.25 ? 188 VAL D N   1 
ATOM   5889 C  CA  . VAL D 1 200 ? 5.801   43.631  46.952  1.00 18.16 ? 188 VAL D CA  1 
ATOM   5890 C  C   . VAL D 1 200 ? 5.955   44.213  48.353  1.00 26.62 ? 188 VAL D C   1 
ATOM   5891 O  O   . VAL D 1 200 ? 6.111   45.424  48.513  1.00 21.23 ? 188 VAL D O   1 
ATOM   5892 C  CB  . VAL D 1 200 ? 7.008   43.962  46.063  1.00 15.57 ? 188 VAL D CB  1 
ATOM   5893 C  CG1 . VAL D 1 200 ? 8.285   43.350  46.617  1.00 19.83 ? 188 VAL D CG1 1 
ATOM   5894 C  CG2 . VAL D 1 200 ? 6.754   43.467  44.634  1.00 16.38 ? 188 VAL D CG2 1 
ATOM   5895 N  N   . GLN D 1 201 ? 5.870   43.364  49.373  1.00 31.07 ? 189 GLN D N   1 
ATOM   5896 C  CA  . GLN D 1 201 ? 5.923   43.844  50.755  1.00 33.29 ? 189 GLN D CA  1 
ATOM   5897 C  C   . GLN D 1 201 ? 7.194   43.374  51.445  1.00 27.67 ? 189 GLN D C   1 
ATOM   5898 O  O   . GLN D 1 201 ? 8.279   43.440  50.862  1.00 38.60 ? 189 GLN D O   1 
ATOM   5899 C  CB  . GLN D 1 201 ? 4.687   43.385  51.538  1.00 34.47 ? 189 GLN D CB  1 
ATOM   5900 C  CG  . GLN D 1 201 ? 3.581   44.434  51.603  1.00 38.51 ? 189 GLN D CG  1 
ATOM   5901 C  CD  . GLN D 1 201 ? 2.209   43.844  51.905  1.00 43.50 ? 189 GLN D CD  1 
ATOM   5902 O  OE1 . GLN D 1 201 ? 1.975   42.644  51.722  1.00 53.32 ? 189 GLN D OE1 1 
ATOM   5903 N  NE2 . GLN D 1 201 ? 1.291   44.691  52.359  1.00 43.16 ? 189 GLN D NE2 1 
HETATM 5904 O  O1  . XYP E 2 .   ? 16.277  -0.098  26.451  1.00 37.73 ? 1   XYP E O1  1 
HETATM 5905 C  C1  . XYP E 2 .   ? 17.489  -0.742  26.208  1.00 28.97 ? 1   XYP E C1  1 
HETATM 5906 C  C2  . XYP E 2 .   ? 18.396  -0.480  27.399  1.00 23.25 ? 1   XYP E C2  1 
HETATM 5907 C  C3  . XYP E 2 .   ? 19.664  -1.324  27.407  1.00 18.89 ? 1   XYP E C3  1 
HETATM 5908 C  C4  . XYP E 2 .   ? 19.390  -2.776  27.031  1.00 19.63 ? 1   XYP E C4  1 
HETATM 5909 C  C5  . XYP E 2 .   ? 18.494  -2.843  25.808  1.00 21.83 ? 1   XYP E C5  1 
HETATM 5910 O  O2  . XYP E 2 .   ? 18.730  0.906   27.470  1.00 19.72 ? 1   XYP E O2  1 
HETATM 5911 O  O3  . XYP E 2 .   ? 20.190  -1.264  28.729  1.00 20.43 ? 1   XYP E O3  1 
HETATM 5912 O  O4  . XYP E 2 .   ? 20.484  -3.191  26.307  1.00 15.35 ? 1   XYP E O4  1 
HETATM 5913 O  O5  . XYP E 2 .   ? 17.268  -2.143  26.044  1.00 26.55 ? 1   XYP E O5  1 
HETATM 5914 C  C1  . XYP E 2 .   ? 20.919  -4.517  26.360  1.00 15.61 ? 2   XYP E C1  1 
HETATM 5915 C  C2  . XYP E 2 .   ? 21.610  -4.899  25.056  1.00 12.02 ? 2   XYP E C2  1 
HETATM 5916 C  C3  . XYP E 2 .   ? 22.248  -6.281  25.132  1.00 12.63 ? 2   XYP E C3  1 
HETATM 5917 C  C4  . XYP E 2 .   ? 23.091  -6.428  26.392  1.00 16.11 ? 2   XYP E C4  1 
HETATM 5918 C  C5  . XYP E 2 .   ? 22.268  -6.022  27.600  1.00 14.64 ? 2   XYP E C5  1 
HETATM 5919 O  O2  . XYP E 2 .   ? 20.684  -4.853  23.969  1.00 11.71 ? 2   XYP E O2  1 
HETATM 5920 O  O3  . XYP E 2 .   ? 23.057  -6.494  23.977  1.00 13.23 ? 2   XYP E O3  1 
HETATM 5921 O  O4  . XYP E 2 .   ? 23.520  -7.785  26.544  1.00 17.83 ? 2   XYP E O4  1 
HETATM 5922 O  O5  . XYP E 2 .   ? 21.818  -4.671  27.461  1.00 16.25 ? 2   XYP E O5  1 
HETATM 5923 ZN ZN  . ZN  F 3 .   ? 4.786   8.181   5.584   1.00 35.71 ? 300 ZN  A ZN  1 
HETATM 5924 ZN ZN  . ZN  G 3 .   ? 4.500   5.513   14.594  1.00 21.56 ? 301 ZN  A ZN  1 
HETATM 5925 ZN ZN  . ZN  H 3 .   ? -17.661 -7.313  25.346  1.00 39.71 ? 201 ZN  B ZN  1 
HETATM 5926 ZN ZN  . ZN  I 3 .   ? -9.137  -4.640  26.160  1.00 36.86 ? 202 ZN  B ZN  1 
HETATM 5927 C  C1  . XYP J 4 .   ? 0.520   5.391   44.569  1.00 16.63 ? 203 XYP B C1  1 
HETATM 5928 C  C2  . XYP J 4 .   ? -0.871  5.776   45.039  1.00 13.65 ? 203 XYP B C2  1 
HETATM 5929 C  C3  . XYP J 4 .   ? -0.862  7.153   45.690  1.00 14.38 ? 203 XYP B C3  1 
HETATM 5930 C  C4  . XYP J 4 .   ? 0.230   7.236   46.751  1.00 15.21 ? 203 XYP B C4  1 
HETATM 5931 C  C5  . XYP J 4 .   ? 1.555   6.792   46.164  1.00 17.85 ? 203 XYP B C5  1 
HETATM 5932 O  O2  . XYP J 4 .   ? -1.781  5.722   43.938  1.00 13.39 ? 203 XYP B O2  1 
HETATM 5933 O  O3  . XYP J 4 .   ? -2.137  7.420   46.275  1.00 14.74 ? 203 XYP B O3  1 
HETATM 5934 O  O4  . XYP J 4 .   ? 0.362   8.573   47.244  1.00 17.82 ? 203 XYP B O4  1 
HETATM 5935 O  O5  . XYP J 4 .   ? 1.452   5.461   45.656  1.00 18.23 ? 203 XYP B O5  1 
HETATM 5936 O  O1  . XYP K 4 .   ? 0.344   0.653   40.377  1.00 40.49 ? 204 XYP B O1  1 
HETATM 5937 C  C1  . XYP K 4 .   ? 0.553   1.568   41.398  1.00 26.35 ? 204 XYP B C1  1 
HETATM 5938 C  C2  . XYP K 4 .   ? 1.768   1.236   42.215  1.00 24.43 ? 204 XYP B C2  1 
HETATM 5939 C  C3  . XYP K 4 .   ? 1.800   2.128   43.447  1.00 21.99 ? 204 XYP B C3  1 
HETATM 5940 C  C4  . XYP K 4 .   ? 1.412   3.586   43.180  1.00 19.61 ? 204 XYP B C4  1 
HETATM 5941 C  C5  . XYP K 4 .   ? 0.554   3.826   41.943  1.00 25.43 ? 204 XYP B C5  1 
HETATM 5942 O  O2  . XYP K 4 .   ? 1.773   -0.135  42.611  1.00 21.45 ? 204 XYP B O2  1 
HETATM 5943 O  O3  . XYP K 4 .   ? 3.090   2.051   44.056  1.00 19.30 ? 204 XYP B O3  1 
HETATM 5944 O  O4  . XYP K 4 .   ? 0.666   4.051   44.307  1.00 18.13 ? 204 XYP B O4  1 
HETATM 5945 O  O5  . XYP K 4 .   ? 0.759   2.872   40.898  1.00 24.49 ? 204 XYP B O5  1 
HETATM 5946 O  O1  . XYP L 4 .   ? 0.377   32.349  10.574  1.00 39.38 ? 201 XYP C O1  1 
HETATM 5947 C  C1  . XYP L 4 .   ? 0.674   31.573  9.456   1.00 33.81 ? 201 XYP C C1  1 
HETATM 5948 C  C2  . XYP L 4 .   ? 1.885   32.151  8.758   1.00 26.53 ? 201 XYP C C2  1 
HETATM 5949 C  C3  . XYP L 4 .   ? 2.344   31.312  7.572   1.00 22.71 ? 201 XYP C C3  1 
HETATM 5950 C  C4  . XYP L 4 .   ? 2.274   29.807  7.822   1.00 26.80 ? 201 XYP C C4  1 
HETATM 5951 C  C5  . XYP L 4 .   ? 1.078   29.406  8.670   1.00 26.48 ? 201 XYP C C5  1 
HETATM 5952 O  O2  . XYP L 4 .   ? 1.620   33.485  8.326   1.00 23.42 ? 201 XYP C O2  1 
HETATM 5953 O  O3  . XYP L 4 .   ? 3.678   31.692  7.229   1.00 30.06 ? 201 XYP C O3  1 
HETATM 5954 O  O4  . XYP L 4 .   ? 2.175   29.140  6.559   1.00 23.11 ? 201 XYP C O4  1 
HETATM 5955 O  O5  . XYP L 4 .   ? 0.951   30.231  9.832   1.00 28.40 ? 201 XYP C O5  1 
HETATM 5956 C  C1  . XYP M 4 .   ? 2.509   27.829  6.327   1.00 23.78 ? 202 XYP C C1  1 
HETATM 5957 C  C2  . XYP M 4 .   ? 1.445   27.131  5.503   1.00 20.64 ? 202 XYP C C2  1 
HETATM 5958 C  C3  . XYP M 4 .   ? 2.008   25.876  4.849   1.00 19.72 ? 202 XYP C C3  1 
HETATM 5959 C  C4  . XYP M 4 .   ? 3.310   26.172  4.116   1.00 22.99 ? 202 XYP C C4  1 
HETATM 5960 C  C5  . XYP M 4 .   ? 4.261   26.940  5.013   1.00 21.63 ? 202 XYP C C5  1 
HETATM 5961 O  O2  . XYP M 4 .   ? 0.315   26.820  6.320   1.00 19.23 ? 202 XYP C O2  1 
HETATM 5962 O  O3  . XYP M 4 .   ? 1.054   25.352  3.929   1.00 20.45 ? 202 XYP C O3  1 
HETATM 5963 O  O4  . XYP M 4 .   ? 3.928   24.949  3.707   1.00 20.59 ? 202 XYP C O4  1 
HETATM 5964 O  O5  . XYP M 4 .   ? 3.638   28.132  5.500   1.00 21.25 ? 202 XYP C O5  1 
HETATM 5965 ZN ZN  . ZN  N 3 .   ? -3.019  25.065  45.134  1.00 44.94 ? 201 ZN  D ZN  1 
HETATM 5966 ZN ZN  . ZN  O 3 .   ? -1.571  27.750  36.309  1.00 23.60 ? 202 ZN  D ZN  1 
HETATM 5967 C  C1  . XYP P 4 .   ? 13.781  42.285  28.607  1.00 22.00 ? 203 XYP D C1  1 
HETATM 5968 C  C2  . XYP P 4 .   ? 14.013  42.794  30.023  1.00 18.20 ? 203 XYP D C2  1 
HETATM 5969 C  C3  . XYP P 4 .   ? 14.263  44.297  30.056  1.00 18.26 ? 203 XYP D C3  1 
HETATM 5970 C  C4  . XYP P 4 .   ? 15.331  44.685  29.039  1.00 20.87 ? 203 XYP D C4  1 
HETATM 5971 C  C5  . XYP P 4 .   ? 15.021  44.075  27.683  1.00 21.82 ? 203 XYP D C5  1 
HETATM 5972 O  O2  . XYP P 4 .   ? 12.916  42.444  30.860  1.00 18.15 ? 203 XYP D O2  1 
HETATM 5973 O  O3  . XYP P 4 .   ? 14.677  44.669  31.372  1.00 16.90 ? 203 XYP D O3  1 
HETATM 5974 O  O4  . XYP P 4 .   ? 15.411  46.109  28.913  1.00 25.38 ? 203 XYP D O4  1 
HETATM 5975 O  O5  . XYP P 4 .   ? 14.888  42.652  27.781  1.00 19.63 ? 203 XYP D O5  1 
HETATM 5976 O  O1  . XYP Q 4 .   ? 10.863  36.467  27.311  1.00 37.54 ? 204 XYP D O1  1 
HETATM 5977 C  C1  . XYP Q 4 .   ? 11.686  37.412  27.935  1.00 37.27 ? 204 XYP D C1  1 
HETATM 5978 C  C2  . XYP Q 4 .   ? 12.921  37.570  27.066  1.00 35.79 ? 204 XYP D C2  1 
HETATM 5979 C  C3  . XYP Q 4 .   ? 13.795  38.786  27.366  1.00 29.60 ? 204 XYP D C3  1 
HETATM 5980 C  C4  . XYP Q 4 .   ? 13.008  40.013  27.818  1.00 29.50 ? 204 XYP D C4  1 
HETATM 5981 C  C5  . XYP Q 4 .   ? 11.864  39.616  28.731  1.00 29.23 ? 204 XYP D C5  1 
HETATM 5982 O  O2  . XYP Q 4 .   ? 13.706  36.384  27.154  1.00 29.87 ? 204 XYP D O2  1 
HETATM 5983 O  O3  . XYP Q 4 .   ? 14.530  39.087  26.182  1.00 26.02 ? 204 XYP D O3  1 
HETATM 5984 O  O4  . XYP Q 4 .   ? 13.870  40.915  28.520  1.00 21.75 ? 204 XYP D O4  1 
HETATM 5985 O  O5  . XYP Q 4 .   ? 11.016  38.659  28.092  1.00 36.87 ? 204 XYP D O5  1 
HETATM 5986 O  O   . HOH R 5 .   ? 12.695  9.997   27.143  1.00 29.60 ? 401 HOH A O   1 
HETATM 5987 O  O   . HOH R 5 .   ? 3.842   8.301   6.962   1.00 21.43 ? 402 HOH A O   1 
HETATM 5988 O  O   . HOH R 5 .   ? 36.538  12.469  23.921  1.00 31.32 ? 403 HOH A O   1 
HETATM 5989 O  O   . HOH R 5 .   ? 16.027  7.123   0.217   1.00 18.68 ? 404 HOH A O   1 
HETATM 5990 O  O   . HOH R 5 .   ? 21.873  -4.164  4.356   1.00 21.72 ? 405 HOH A O   1 
HETATM 5991 O  O   . HOH R 5 .   ? 8.154   -15.493 5.875   1.00 33.58 ? 406 HOH A O   1 
HETATM 5992 O  O   . HOH R 5 .   ? 1.979   -9.787  6.271   1.00 33.12 ? 407 HOH A O   1 
HETATM 5993 O  O   . HOH R 5 .   ? 11.809  7.274   28.519  1.00 31.48 ? 408 HOH A O   1 
HETATM 5994 O  O   . HOH R 5 .   ? -1.075  -6.256  23.358  1.00 28.06 ? 409 HOH A O   1 
HETATM 5995 O  O   . HOH R 5 .   ? 23.985  -5.480  38.362  1.00 32.75 ? 410 HOH A O   1 
HETATM 5996 O  O   . HOH R 5 .   ? 34.566  -5.418  26.483  1.00 26.57 ? 411 HOH A O   1 
HETATM 5997 O  O   . HOH R 5 .   ? 32.459  -6.912  26.740  1.00 39.51 ? 412 HOH A O   1 
HETATM 5998 O  O   . HOH R 5 .   ? 22.308  -4.616  34.817  1.00 28.22 ? 413 HOH A O   1 
HETATM 5999 O  O   . HOH R 5 .   ? 16.209  -0.604  23.059  1.00 21.72 ? 414 HOH A O   1 
HETATM 6000 O  O   . HOH R 5 .   ? 24.032  -19.950 5.021   1.00 32.30 ? 415 HOH A O   1 
HETATM 6001 O  O   . HOH R 5 .   ? 34.448  -1.403  26.873  1.00 15.08 ? 416 HOH A O   1 
HETATM 6002 O  O   . HOH R 5 .   ? 10.670  -23.684 11.470  1.00 36.22 ? 417 HOH A O   1 
HETATM 6003 O  O   . HOH R 5 .   ? 26.479  -14.502 23.645  1.00 35.21 ? 418 HOH A O   1 
HETATM 6004 O  O   . HOH R 5 .   ? 0.912   -7.285  25.985  1.00 21.35 ? 419 HOH A O   1 
HETATM 6005 O  O   . HOH R 5 .   ? 22.489  17.517  11.613  1.00 27.37 ? 420 HOH A O   1 
HETATM 6006 O  O   . HOH R 5 .   ? 2.127   -10.873 8.157   1.00 28.72 ? 421 HOH A O   1 
HETATM 6007 O  O   . HOH R 5 .   ? 3.142   -1.249  33.802  1.00 30.87 ? 422 HOH A O   1 
HETATM 6008 O  O   . HOH R 5 .   ? 25.196  4.914   0.944   1.00 38.98 ? 423 HOH A O   1 
HETATM 6009 O  O   . HOH R 5 .   ? 4.077   6.905   8.725   1.00 31.50 ? 424 HOH A O   1 
HETATM 6010 O  O   . HOH R 5 .   ? 13.884  6.554   26.251  1.00 31.66 ? 425 HOH A O   1 
HETATM 6011 O  O   . HOH R 5 .   ? 0.310   -3.267  14.753  1.00 29.53 ? 426 HOH A O   1 
HETATM 6012 O  O   . HOH R 5 .   ? 4.649   -9.617  12.109  1.00 23.73 ? 427 HOH A O   1 
HETATM 6013 O  O   . HOH R 5 .   ? 23.205  20.051  16.354  1.00 35.88 ? 428 HOH A O   1 
HETATM 6014 O  O   . HOH R 5 .   ? 20.159  -7.140  21.732  1.00 13.74 ? 429 HOH A O   1 
HETATM 6015 O  O   . HOH R 5 .   ? 7.254   18.141  15.213  1.00 27.88 ? 430 HOH A O   1 
HETATM 6016 O  O   . HOH R 5 .   ? 32.712  5.638   14.537  1.00 34.84 ? 431 HOH A O   1 
HETATM 6017 O  O   . HOH R 5 .   ? 28.460  7.402   27.080  1.00 24.21 ? 432 HOH A O   1 
HETATM 6018 O  O   . HOH R 5 .   ? 24.441  -19.426 16.832  1.00 30.51 ? 433 HOH A O   1 
HETATM 6019 O  O   . HOH R 5 .   ? 13.408  4.041   25.641  1.00 29.67 ? 434 HOH A O   1 
HETATM 6020 O  O   . HOH R 5 .   ? 10.670  14.023  22.399  1.00 25.34 ? 435 HOH A O   1 
HETATM 6021 O  O   . HOH R 5 .   ? 28.833  9.813   25.505  1.00 24.84 ? 436 HOH A O   1 
HETATM 6022 O  O   . HOH R 5 .   ? 19.665  -11.839 29.676  1.00 26.47 ? 437 HOH A O   1 
HETATM 6023 O  O   . HOH R 5 .   ? 11.806  16.254  23.835  1.00 29.66 ? 438 HOH A O   1 
HETATM 6024 O  O   . HOH R 5 .   ? 34.138  -1.257  12.804  1.00 21.52 ? 439 HOH A O   1 
HETATM 6025 O  O   . HOH R 5 .   ? 8.091   -14.947 31.868  1.00 27.84 ? 440 HOH A O   1 
HETATM 6026 O  O   . HOH R 5 .   ? 31.966  12.919  10.953  1.00 35.10 ? 441 HOH A O   1 
HETATM 6027 O  O   . HOH R 5 .   ? 18.805  6.532   0.718   1.00 21.73 ? 442 HOH A O   1 
HETATM 6028 O  O   . HOH R 5 .   ? 28.021  -0.055  16.084  1.00 16.84 ? 443 HOH A O   1 
HETATM 6029 O  O   . HOH R 5 .   ? 13.690  -12.868 3.917   1.00 22.43 ? 444 HOH A O   1 
HETATM 6030 O  O   . HOH R 5 .   ? 23.513  -8.921  23.230  1.00 14.14 ? 445 HOH A O   1 
HETATM 6031 O  O   . HOH R 5 .   ? 35.735  9.816   22.194  1.00 37.00 ? 446 HOH A O   1 
HETATM 6032 O  O   . HOH R 5 .   ? 29.125  22.716  13.223  1.00 33.93 ? 447 HOH A O   1 
HETATM 6033 O  O   . HOH R 5 .   ? 8.248   -3.217  4.513   1.00 15.72 ? 448 HOH A O   1 
HETATM 6034 O  O   . HOH R 5 .   ? 10.939  -9.271  28.009  1.00 16.21 ? 449 HOH A O   1 
HETATM 6035 O  O   . HOH R 5 .   ? 29.371  -11.846 13.264  1.00 24.26 ? 450 HOH A O   1 
HETATM 6036 O  O   . HOH R 5 .   ? 30.739  -4.404  9.668   1.00 23.29 ? 451 HOH A O   1 
HETATM 6037 O  O   . HOH R 5 .   ? 12.088  -19.019 4.591   1.00 33.83 ? 452 HOH A O   1 
HETATM 6038 O  O   . HOH R 5 .   ? 16.115  6.441   27.836  1.00 25.87 ? 453 HOH A O   1 
HETATM 6039 O  O   . HOH R 5 .   ? 5.460   -11.509 10.810  1.00 27.12 ? 454 HOH A O   1 
HETATM 6040 O  O   . HOH R 5 .   ? 33.037  -6.379  18.126  1.00 24.49 ? 455 HOH A O   1 
HETATM 6041 O  O   . HOH R 5 .   ? 20.207  -17.318 27.908  1.00 30.34 ? 456 HOH A O   1 
HETATM 6042 O  O   . HOH R 5 .   ? 13.889  -15.674 28.997  1.00 31.16 ? 457 HOH A O   1 
HETATM 6043 O  O   . HOH R 5 .   ? 9.328   -17.559 14.227  1.00 33.27 ? 458 HOH A O   1 
HETATM 6044 O  O   . HOH R 5 .   ? 18.186  7.033   7.765   1.00 11.80 ? 459 HOH A O   1 
HETATM 6045 O  O   . HOH R 5 .   ? 37.463  4.069   21.407  1.00 22.92 ? 460 HOH A O   1 
HETATM 6046 O  O   . HOH R 5 .   ? 11.142  -12.778 28.115  1.00 18.67 ? 461 HOH A O   1 
HETATM 6047 O  O   . HOH R 5 .   ? 9.687   -16.524 10.377  1.00 26.62 ? 462 HOH A O   1 
HETATM 6048 O  O   . HOH R 5 .   ? -0.555  -11.052 24.140  1.00 28.76 ? 463 HOH A O   1 
HETATM 6049 O  O   . HOH R 5 .   ? 22.308  -0.817  1.566   1.00 30.02 ? 464 HOH A O   1 
HETATM 6050 O  O   . HOH R 5 .   ? 12.496  -16.681 11.290  1.00 18.31 ? 465 HOH A O   1 
HETATM 6051 O  O   . HOH R 5 .   ? 33.623  6.297   16.334  1.00 27.72 ? 466 HOH A O   1 
HETATM 6052 O  O   . HOH R 5 .   ? 3.554   6.274   16.471  1.00 21.17 ? 467 HOH A O   1 
HETATM 6053 O  O   . HOH R 5 .   ? 11.303  -10.291 6.422   1.00 17.83 ? 468 HOH A O   1 
HETATM 6054 O  O   . HOH R 5 .   ? 26.651  4.752   5.746   1.00 16.23 ? 469 HOH A O   1 
HETATM 6055 O  O   . HOH R 5 .   ? 10.795  12.094  8.070   1.00 17.55 ? 470 HOH A O   1 
HETATM 6056 O  O   . HOH R 5 .   ? 24.934  14.033  8.378   1.00 23.89 ? 471 HOH A O   1 
HETATM 6057 O  O   . HOH R 5 .   ? 10.212  18.883  17.985  1.00 33.27 ? 472 HOH A O   1 
HETATM 6058 O  O   . HOH R 5 .   ? 23.037  6.228   0.808   1.00 32.56 ? 473 HOH A O   1 
HETATM 6059 O  O   . HOH R 5 .   ? 6.353   -0.087  4.644   1.00 12.38 ? 474 HOH A O   1 
HETATM 6060 O  O   . HOH R 5 .   ? 16.531  -19.723 15.239  1.00 20.11 ? 475 HOH A O   1 
HETATM 6061 O  O   . HOH R 5 .   ? 8.090   9.305   29.933  1.00 22.63 ? 476 HOH A O   1 
HETATM 6062 O  O   . HOH R 5 .   ? 14.522  -1.731  1.739   1.00 25.88 ? 477 HOH A O   1 
HETATM 6063 O  O   . HOH R 5 .   ? 27.471  -9.974  9.548   1.00 21.76 ? 478 HOH A O   1 
HETATM 6064 O  O   . HOH R 5 .   ? 15.339  14.119  3.605   1.00 26.17 ? 479 HOH A O   1 
HETATM 6065 O  O   . HOH R 5 .   ? 19.331  -11.053 3.501   1.00 19.77 ? 480 HOH A O   1 
HETATM 6066 O  O   . HOH R 5 .   ? 5.422   2.773   10.577  1.00 18.55 ? 481 HOH A O   1 
HETATM 6067 O  O   . HOH R 5 .   ? 4.861   8.970   11.546  1.00 27.81 ? 482 HOH A O   1 
HETATM 6068 O  O   . HOH R 5 .   ? 28.683  -7.176  22.383  1.00 18.62 ? 483 HOH A O   1 
HETATM 6069 O  O   . HOH R 5 .   ? 37.513  7.448   22.940  1.00 21.42 ? 484 HOH A O   1 
HETATM 6070 O  O   . HOH R 5 .   ? 6.743   3.023   21.133  1.00 14.36 ? 485 HOH A O   1 
HETATM 6071 O  O   . HOH R 5 .   ? 1.790   -6.650  8.226   1.00 17.67 ? 486 HOH A O   1 
HETATM 6072 O  O   . HOH R 5 .   ? 29.177  -4.242  35.360  1.00 18.71 ? 487 HOH A O   1 
HETATM 6073 O  O   . HOH R 5 .   ? 15.130  4.934   1.966   1.00 15.86 ? 488 HOH A O   1 
HETATM 6074 O  O   . HOH R 5 .   ? 10.295  -6.206  33.010  1.00 26.45 ? 489 HOH A O   1 
HETATM 6075 O  O   . HOH R 5 .   ? 29.623  13.099  23.902  1.00 30.98 ? 490 HOH A O   1 
HETATM 6076 O  O   . HOH R 5 .   ? 14.537  -0.924  18.043  1.00 15.63 ? 491 HOH A O   1 
HETATM 6077 O  O   . HOH R 5 .   ? 18.734  5.173   33.956  1.00 32.95 ? 492 HOH A O   1 
HETATM 6078 O  O   . HOH R 5 .   ? 23.266  -17.082 25.862  1.00 34.48 ? 493 HOH A O   1 
HETATM 6079 O  O   . HOH R 5 .   ? 24.058  17.929  13.976  1.00 24.03 ? 494 HOH A O   1 
HETATM 6080 O  O   . HOH R 5 .   ? 1.060   -13.403 28.097  1.00 29.94 ? 495 HOH A O   1 
HETATM 6081 O  O   . HOH R 5 .   ? 18.951  -18.825 24.364  1.00 23.61 ? 496 HOH A O   1 
HETATM 6082 O  O   . HOH R 5 .   ? 4.484   12.520  11.506  1.00 21.18 ? 497 HOH A O   1 
HETATM 6083 O  O   . HOH R 5 .   ? 24.455  -3.269  4.205   1.00 30.31 ? 498 HOH A O   1 
HETATM 6084 O  O   . HOH R 5 .   ? 20.843  17.293  7.405   1.00 24.01 ? 499 HOH A O   1 
HETATM 6085 O  O   . HOH R 5 .   ? 20.530  -4.318  -0.729  1.00 34.45 ? 500 HOH A O   1 
HETATM 6086 O  O   . HOH R 5 .   ? 8.236   13.241  23.566  1.00 22.40 ? 501 HOH A O   1 
HETATM 6087 O  O   . HOH R 5 .   ? 26.396  18.084  22.904  1.00 33.00 ? 502 HOH A O   1 
HETATM 6088 O  O   . HOH R 5 .   ? 28.302  -11.224 20.948  1.00 26.92 ? 503 HOH A O   1 
HETATM 6089 O  O   . HOH R 5 .   ? 22.016  -11.164 24.403  1.00 16.10 ? 504 HOH A O   1 
HETATM 6090 O  O   . HOH R 5 .   ? 10.885  -15.285 26.868  1.00 19.92 ? 505 HOH A O   1 
HETATM 6091 O  O   . HOH R 5 .   ? 18.223  -11.045 31.159  1.00 32.34 ? 506 HOH A O   1 
HETATM 6092 O  O   . HOH R 5 .   ? 8.358   10.808  15.256  1.00 19.39 ? 507 HOH A O   1 
HETATM 6093 O  O   . HOH R 5 .   ? 21.762  -11.287 2.249   1.00 28.84 ? 508 HOH A O   1 
HETATM 6094 O  O   . HOH R 5 .   ? 20.676  -18.376 3.915   1.00 23.96 ? 509 HOH A O   1 
HETATM 6095 O  O   . HOH R 5 .   ? 15.782  -14.384 3.831   1.00 27.07 ? 510 HOH A O   1 
HETATM 6096 O  O   . HOH R 5 .   ? 27.037  13.451  6.611   1.00 30.53 ? 511 HOH A O   1 
HETATM 6097 O  O   . HOH R 5 .   ? 28.254  -14.083 19.558  1.00 26.29 ? 512 HOH A O   1 
HETATM 6098 O  O   . HOH R 5 .   ? 0.528   -0.521  18.808  1.00 21.11 ? 513 HOH A O   1 
HETATM 6099 O  O   . HOH R 5 .   ? 10.825  12.647  18.352  1.00 24.77 ? 514 HOH A O   1 
HETATM 6100 O  O   . HOH R 5 .   ? 32.035  18.233  16.117  1.00 29.79 ? 515 HOH A O   1 
HETATM 6101 O  O   . HOH R 5 .   ? 29.450  -9.648  11.689  1.00 18.27 ? 516 HOH A O   1 
HETATM 6102 O  O   . HOH R 5 .   ? 20.257  10.411  1.797   1.00 24.01 ? 517 HOH A O   1 
HETATM 6103 O  O   . HOH R 5 .   ? 18.545  16.505  27.257  1.00 26.69 ? 518 HOH A O   1 
HETATM 6104 O  O   . HOH R 5 .   ? 13.132  16.279  31.505  1.00 29.04 ? 519 HOH A O   1 
HETATM 6105 O  O   . HOH R 5 .   ? 11.947  -24.697 18.244  1.00 37.99 ? 520 HOH A O   1 
HETATM 6106 O  O   . HOH R 5 .   ? 24.493  -18.875 20.536  1.00 33.96 ? 521 HOH A O   1 
HETATM 6107 O  O   . HOH R 5 .   ? 22.726  13.994  6.061   1.00 25.58 ? 522 HOH A O   1 
HETATM 6108 O  O   . HOH R 5 .   ? 28.493  0.727   12.665  1.00 18.09 ? 523 HOH A O   1 
HETATM 6109 O  O   . HOH R 5 .   ? 34.977  1.868   15.183  1.00 22.98 ? 524 HOH A O   1 
HETATM 6110 O  O   . HOH R 5 .   ? 30.637  15.329  11.853  1.00 31.06 ? 525 HOH A O   1 
HETATM 6111 O  O   . HOH R 5 .   ? 3.339   6.496   13.225  1.00 20.04 ? 526 HOH A O   1 
HETATM 6112 O  O   . HOH R 5 .   ? 16.275  2.658   27.280  1.00 35.53 ? 527 HOH A O   1 
HETATM 6113 O  O   . HOH R 5 .   ? 9.670   -16.056 16.446  1.00 23.42 ? 528 HOH A O   1 
HETATM 6114 O  O   . HOH R 5 .   ? 16.987  -13.973 29.050  1.00 21.42 ? 529 HOH A O   1 
HETATM 6115 O  O   . HOH R 5 .   ? 16.341  -20.238 24.301  1.00 21.75 ? 530 HOH A O   1 
HETATM 6116 O  O   . HOH R 5 .   ? 33.590  11.123  18.722  1.00 35.12 ? 531 HOH A O   1 
HETATM 6117 O  O   . HOH R 5 .   ? 2.540   7.608   19.932  1.00 31.11 ? 532 HOH A O   1 
HETATM 6118 O  O   . HOH R 5 .   ? 35.084  -1.457  15.379  1.00 24.00 ? 533 HOH A O   1 
HETATM 6119 O  O   . HOH R 5 .   ? 4.617   0.065   27.585  1.00 20.68 ? 534 HOH A O   1 
HETATM 6120 O  O   . HOH R 5 .   ? 11.115  -9.210  3.852   1.00 29.44 ? 535 HOH A O   1 
HETATM 6121 O  O   . HOH R 5 .   ? 9.691   11.163  5.056   1.00 31.98 ? 536 HOH A O   1 
HETATM 6122 O  O   . HOH R 5 .   ? 3.608   10.196  5.273   1.00 32.85 ? 537 HOH A O   1 
HETATM 6123 O  O   . HOH R 5 .   ? 17.277  12.685  1.927   1.00 30.57 ? 538 HOH A O   1 
HETATM 6124 O  O   . HOH R 5 .   ? 31.897  6.845   11.797  1.00 36.41 ? 539 HOH A O   1 
HETATM 6125 O  O   . HOH R 5 .   ? 18.659  -20.315 10.480  1.00 24.95 ? 540 HOH A O   1 
HETATM 6126 O  O   . HOH R 5 .   ? 23.778  10.360  1.624   1.00 30.53 ? 541 HOH A O   1 
HETATM 6127 O  O   . HOH R 5 .   ? 18.760  -20.966 7.628   1.00 29.76 ? 542 HOH A O   1 
HETATM 6128 O  O   . HOH R 5 .   ? 10.757  12.684  15.530  1.00 19.70 ? 543 HOH A O   1 
HETATM 6129 O  O   . HOH R 5 .   ? 5.889   -16.987 8.304   1.00 30.70 ? 544 HOH A O   1 
HETATM 6130 O  O   . HOH R 5 .   ? 6.184   -15.488 22.231  1.00 25.64 ? 545 HOH A O   1 
HETATM 6131 O  O   . HOH R 5 .   ? 11.836  -10.576 34.522  1.00 32.29 ? 546 HOH A O   1 
HETATM 6132 O  O   . HOH R 5 .   ? 25.585  -8.263  29.531  1.00 35.89 ? 547 HOH A O   1 
HETATM 6133 O  O   . HOH R 5 .   ? 25.205  -16.305 23.511  1.00 27.83 ? 548 HOH A O   1 
HETATM 6134 O  O   . HOH R 5 .   ? 6.924   -13.079 13.648  1.00 24.51 ? 549 HOH A O   1 
HETATM 6135 O  O   . HOH R 5 .   ? 9.832   -4.194  2.913   1.00 21.95 ? 550 HOH A O   1 
HETATM 6136 O  O   . HOH R 5 .   ? 20.455  20.696  13.013  1.00 30.17 ? 551 HOH A O   1 
HETATM 6137 O  O   . HOH R 5 .   ? 4.281   3.529   13.667  1.00 14.37 ? 552 HOH A O   1 
HETATM 6138 O  O   . HOH R 5 .   ? 7.522   -6.235  32.534  1.00 25.97 ? 553 HOH A O   1 
HETATM 6139 O  O   . HOH R 5 .   ? 21.743  -8.374  30.794  1.00 30.25 ? 554 HOH A O   1 
HETATM 6140 O  O   . HOH R 5 .   ? 24.918  -7.468  3.570   1.00 36.76 ? 555 HOH A O   1 
HETATM 6141 O  O   . HOH R 5 .   ? 6.261   -12.572 33.544  1.00 27.76 ? 556 HOH A O   1 
HETATM 6142 O  O   . HOH R 5 .   ? 23.957  -6.405  31.321  1.00 22.53 ? 557 HOH A O   1 
HETATM 6143 O  O   . HOH R 5 .   ? 27.286  -18.286 19.372  1.00 29.65 ? 558 HOH A O   1 
HETATM 6144 O  O   . HOH R 5 .   ? 19.485  -20.068 15.572  1.00 25.29 ? 559 HOH A O   1 
HETATM 6145 O  O   . HOH R 5 .   ? 10.044  -12.747 6.544   1.00 25.94 ? 560 HOH A O   1 
HETATM 6146 O  O   . HOH R 5 .   ? -3.129  -10.246 27.504  1.00 31.24 ? 561 HOH A O   1 
HETATM 6147 O  O   . HOH R 5 .   ? 8.792   15.074  17.926  1.00 29.07 ? 562 HOH A O   1 
HETATM 6148 O  O   . HOH R 5 .   ? 6.425   -10.539 33.578  1.00 28.70 ? 563 HOH A O   1 
HETATM 6149 O  O   . HOH R 5 .   ? 11.450  0.580   29.456  1.00 34.54 ? 564 HOH A O   1 
HETATM 6150 O  O   . HOH R 5 .   ? 21.935  16.581  25.680  1.00 32.02 ? 565 HOH A O   1 
HETATM 6151 O  O   . HOH R 5 .   ? 31.269  7.127   14.445  1.00 25.46 ? 566 HOH A O   1 
HETATM 6152 O  O   . HOH R 5 .   ? 23.537  -12.955 25.468  1.00 23.88 ? 567 HOH A O   1 
HETATM 6153 O  O   . HOH R 5 .   ? 8.539   -8.102  3.119   1.00 36.37 ? 568 HOH A O   1 
HETATM 6154 O  O   . HOH R 5 .   ? 27.737  8.432   30.709  1.00 31.18 ? 569 HOH A O   1 
HETATM 6155 O  O   . HOH R 5 .   ? 12.582  -2.943  33.796  1.00 36.04 ? 570 HOH A O   1 
HETATM 6156 O  O   . HOH R 5 .   ? 16.201  -2.744  31.226  1.00 33.13 ? 571 HOH A O   1 
HETATM 6157 O  O   . HOH R 5 .   ? 11.248  -14.383 4.751   1.00 26.58 ? 572 HOH A O   1 
HETATM 6158 O  O   . HOH R 5 .   ? 14.333  -0.316  24.322  1.00 30.06 ? 573 HOH A O   1 
HETATM 6159 O  O   . HOH R 5 .   ? 20.794  2.222   -1.498  1.00 28.75 ? 574 HOH A O   1 
HETATM 6160 O  O   . HOH R 5 .   ? 37.201  8.358   18.134  1.00 43.73 ? 575 HOH A O   1 
HETATM 6161 O  O   . HOH R 5 .   ? 29.477  7.559   29.145  1.00 30.83 ? 576 HOH A O   1 
HETATM 6162 O  O   . HOH R 5 .   ? 25.931  -8.315  26.265  1.00 27.99 ? 577 HOH A O   1 
HETATM 6163 O  O   . HOH R 5 .   ? 11.593  18.415  22.309  1.00 32.66 ? 578 HOH A O   1 
HETATM 6164 O  O   . HOH R 5 .   ? 34.517  1.282   12.325  1.00 37.62 ? 579 HOH A O   1 
HETATM 6165 O  O   . HOH R 5 .   ? 4.404   2.064   7.962   1.00 25.40 ? 580 HOH A O   1 
HETATM 6166 O  O   . HOH R 5 .   ? 28.140  6.374   3.818   1.00 24.15 ? 581 HOH A O   1 
HETATM 6167 O  O   . HOH R 5 .   ? 19.288  -15.035 30.313  1.00 33.55 ? 582 HOH A O   1 
HETATM 6168 O  O   . HOH R 5 .   ? 26.250  -19.345 22.458  1.00 42.59 ? 583 HOH A O   1 
HETATM 6169 O  O   . HOH R 5 .   ? 37.213  -0.630  22.895  1.00 27.57 ? 584 HOH A O   1 
HETATM 6170 O  O   . HOH R 5 .   ? 25.840  -4.173  40.093  1.00 27.37 ? 585 HOH A O   1 
HETATM 6171 O  O   . HOH R 5 .   ? 23.103  -13.599 2.167   1.00 36.83 ? 586 HOH A O   1 
HETATM 6172 O  O   . HOH R 5 .   ? 17.707  -2.599  34.960  1.00 39.49 ? 587 HOH A O   1 
HETATM 6173 O  O   . HOH R 5 .   ? 16.561  -4.774  32.838  1.00 33.20 ? 588 HOH A O   1 
HETATM 6174 O  O   . HOH R 5 .   ? 17.478  -12.019 1.811   1.00 31.15 ? 589 HOH A O   1 
HETATM 6175 O  O   . HOH R 5 .   ? 2.367   1.200   14.808  1.00 36.01 ? 590 HOH A O   1 
HETATM 6176 O  O   . HOH R 5 .   ? 36.000  -7.728  12.333  1.00 43.43 ? 591 HOH A O   1 
HETATM 6177 O  O   . HOH R 5 .   ? 4.715   -23.474 22.094  1.00 41.79 ? 592 HOH A O   1 
HETATM 6178 O  O   . HOH R 5 .   ? 18.118  -7.096  33.152  1.00 30.73 ? 593 HOH A O   1 
HETATM 6179 O  O   . HOH R 5 .   ? 24.340  1.879   47.319  1.00 40.84 ? 594 HOH A O   1 
HETATM 6180 O  O   . HOH S 5 .   ? -6.876  -17.384 30.295  1.00 50.54 ? 301 HOH B O   1 
HETATM 6181 O  O   . HOH S 5 .   ? -3.634  -11.919 59.703  1.00 24.10 ? 302 HOH B O   1 
HETATM 6182 O  O   . HOH S 5 .   ? -24.650 -6.301  35.793  1.00 26.23 ? 303 HOH B O   1 
HETATM 6183 O  O   . HOH S 5 .   ? -8.043  -17.831 37.068  1.00 29.26 ? 304 HOH B O   1 
HETATM 6184 O  O   . HOH S 5 .   ? -14.570 11.250  22.696  1.00 27.06 ? 305 HOH B O   1 
HETATM 6185 O  O   . HOH S 5 .   ? -21.393 4.913   42.285  1.00 22.15 ? 306 HOH B O   1 
HETATM 6186 O  O   . HOH S 5 .   ? -2.684  9.694   46.387  1.00 23.06 ? 307 HOH B O   1 
HETATM 6187 O  O   . HOH S 5 .   ? -17.012 -1.145  34.331  1.00 22.98 ? 308 HOH B O   1 
HETATM 6188 O  O   . HOH S 5 .   ? 0.329   -10.907 48.038  1.00 25.54 ? 309 HOH B O   1 
HETATM 6189 O  O   . HOH S 5 .   ? -21.255 15.937  44.616  1.00 29.60 ? 310 HOH B O   1 
HETATM 6190 O  O   . HOH S 5 .   ? -8.565  18.013  26.555  1.00 27.62 ? 311 HOH B O   1 
HETATM 6191 O  O   . HOH S 5 .   ? -1.557  6.215   58.507  1.00 21.15 ? 312 HOH B O   1 
HETATM 6192 O  O   . HOH S 5 .   ? -18.385 -7.206  29.649  1.00 28.38 ? 313 HOH B O   1 
HETATM 6193 O  O   . HOH S 5 .   ? -5.467  -11.181 29.738  1.00 34.85 ? 314 HOH B O   1 
HETATM 6194 O  O   . HOH S 5 .   ? -0.101  -6.588  52.457  1.00 25.14 ? 315 HOH B O   1 
HETATM 6195 O  O   . HOH S 5 .   ? -14.929 -21.088 49.887  1.00 47.31 ? 316 HOH B O   1 
HETATM 6196 O  O   . HOH S 5 .   ? 3.825   -6.632  35.210  1.00 23.49 ? 317 HOH B O   1 
HETATM 6197 O  O   . HOH S 5 .   ? -12.978 17.454  33.981  1.00 21.73 ? 318 HOH B O   1 
HETATM 6198 O  O   . HOH S 5 .   ? 8.487   6.421   34.686  1.00 32.40 ? 319 HOH B O   1 
HETATM 6199 O  O   . HOH S 5 .   ? -9.128  20.495  38.275  1.00 24.59 ? 320 HOH B O   1 
HETATM 6200 O  O   . HOH S 5 .   ? -24.294 -5.459  38.394  1.00 23.01 ? 321 HOH B O   1 
HETATM 6201 O  O   . HOH S 5 .   ? -25.374 -3.902  45.162  1.00 32.35 ? 322 HOH B O   1 
HETATM 6202 O  O   . HOH S 5 .   ? -6.461  8.611   52.445  1.00 30.98 ? 323 HOH B O   1 
HETATM 6203 O  O   . HOH S 5 .   ? -2.139  -8.594  53.179  1.00 24.81 ? 324 HOH B O   1 
HETATM 6204 O  O   . HOH S 5 .   ? -2.733  -2.265  29.380  1.00 17.21 ? 325 HOH B O   1 
HETATM 6205 O  O   . HOH S 5 .   ? -15.076 1.816   55.453  1.00 21.42 ? 326 HOH B O   1 
HETATM 6206 O  O   . HOH S 5 .   ? 2.468   1.899   25.834  1.00 17.71 ? 327 HOH B O   1 
HETATM 6207 O  O   . HOH S 5 .   ? -0.954  7.855   56.142  1.00 35.26 ? 328 HOH B O   1 
HETATM 6208 O  O   . HOH S 5 .   ? 4.303   -0.098  30.032  1.00 23.44 ? 329 HOH B O   1 
HETATM 6209 O  O   . HOH S 5 .   ? 3.519   20.322  37.700  1.00 30.78 ? 330 HOH B O   1 
HETATM 6210 O  O   . HOH S 5 .   ? 0.838   7.206   22.193  1.00 28.74 ? 331 HOH B O   1 
HETATM 6211 O  O   . HOH S 5 .   ? 10.723  -5.411  50.931  1.00 32.39 ? 332 HOH B O   1 
HETATM 6212 O  O   . HOH S 5 .   ? 12.065  6.097   49.194  1.00 31.09 ? 333 HOH B O   1 
HETATM 6213 O  O   . HOH S 5 .   ? -20.438 14.103  33.956  1.00 24.88 ? 334 HOH B O   1 
HETATM 6214 O  O   . HOH S 5 .   ? -17.723 5.220   51.653  1.00 29.84 ? 335 HOH B O   1 
HETATM 6215 O  O   . HOH S 5 .   ? -3.744  7.817   42.871  1.00 15.27 ? 336 HOH B O   1 
HETATM 6216 O  O   . HOH S 5 .   ? -7.014  21.319  42.865  1.00 26.98 ? 337 HOH B O   1 
HETATM 6217 O  O   . HOH S 5 .   ? -10.761 0.837   49.914  1.00 15.31 ? 338 HOH B O   1 
HETATM 6218 O  O   . HOH S 5 .   ? 3.786   13.237  34.712  1.00 17.77 ? 339 HOH B O   1 
HETATM 6219 O  O   . HOH S 5 .   ? -22.067 -12.067 30.565  1.00 40.61 ? 340 HOH B O   1 
HETATM 6220 O  O   . HOH S 5 .   ? -5.844  -11.670 33.200  1.00 17.53 ? 341 HOH B O   1 
HETATM 6221 O  O   . HOH S 5 .   ? -1.801  23.941  37.392  1.00 30.47 ? 342 HOH B O   1 
HETATM 6222 O  O   . HOH S 5 .   ? 2.590   -13.727 34.489  1.00 30.09 ? 343 HOH B O   1 
HETATM 6223 O  O   . HOH S 5 .   ? -8.014  4.893   22.086  1.00 28.45 ? 344 HOH B O   1 
HETATM 6224 O  O   . HOH S 5 .   ? -24.976 -5.315  42.604  1.00 27.06 ? 345 HOH B O   1 
HETATM 6225 O  O   . HOH S 5 .   ? -7.096  -3.207  60.168  1.00 16.77 ? 346 HOH B O   1 
HETATM 6226 O  O   . HOH S 5 .   ? 2.903   17.313  43.943  1.00 25.68 ? 347 HOH B O   1 
HETATM 6227 O  O   . HOH S 5 .   ? -21.547 12.344  39.748  1.00 19.68 ? 348 HOH B O   1 
HETATM 6228 O  O   . HOH S 5 .   ? -24.293 2.013   42.323  1.00 30.90 ? 349 HOH B O   1 
HETATM 6229 O  O   . HOH S 5 .   ? -3.280  -14.953 33.471  1.00 27.45 ? 350 HOH B O   1 
HETATM 6230 O  O   . HOH S 5 .   ? 1.301   -7.538  38.123  1.00 23.77 ? 351 HOH B O   1 
HETATM 6231 O  O   . HOH S 5 .   ? -5.241  19.254  48.095  1.00 30.59 ? 352 HOH B O   1 
HETATM 6232 O  O   . HOH S 5 .   ? -6.787  -19.656 47.260  1.00 31.46 ? 353 HOH B O   1 
HETATM 6233 O  O   . HOH S 5 .   ? -22.904 12.426  41.909  1.00 28.78 ? 354 HOH B O   1 
HETATM 6234 O  O   . HOH S 5 .   ? -8.643  -9.774  30.070  1.00 22.04 ? 355 HOH B O   1 
HETATM 6235 O  O   . HOH S 5 .   ? 1.659   -4.581  36.266  1.00 28.68 ? 356 HOH B O   1 
HETATM 6236 O  O   . HOH S 5 .   ? -11.275 -5.622  55.429  1.00 27.22 ? 357 HOH B O   1 
HETATM 6237 O  O   . HOH S 5 .   ? -11.389 10.648  26.130  1.00 28.48 ? 358 HOH B O   1 
HETATM 6238 O  O   . HOH S 5 .   ? 4.476   -12.242 42.073  1.00 32.97 ? 359 HOH B O   1 
HETATM 6239 O  O   . HOH S 5 .   ? 4.483   16.117  37.313  1.00 26.59 ? 360 HOH B O   1 
HETATM 6240 O  O   . HOH S 5 .   ? -22.286 2.856   32.868  1.00 21.01 ? 361 HOH B O   1 
HETATM 6241 O  O   . HOH S 5 .   ? 5.336   -2.053  54.440  1.00 24.43 ? 362 HOH B O   1 
HETATM 6242 O  O   . HOH S 5 .   ? -9.644  20.357  42.223  1.00 24.02 ? 363 HOH B O   1 
HETATM 6243 O  O   . HOH S 5 .   ? -5.108  10.314  50.293  1.00 18.61 ? 364 HOH B O   1 
HETATM 6244 O  O   . HOH S 5 .   ? -7.901  20.089  46.746  1.00 28.79 ? 365 HOH B O   1 
HETATM 6245 O  O   . HOH S 5 .   ? -9.304  4.482   56.648  1.00 30.11 ? 366 HOH B O   1 
HETATM 6246 O  O   . HOH S 5 .   ? 3.823   9.276   21.513  1.00 28.19 ? 367 HOH B O   1 
HETATM 6247 O  O   . HOH S 5 .   ? 7.588   5.075   38.249  1.00 28.81 ? 368 HOH B O   1 
HETATM 6248 O  O   . HOH S 5 .   ? -10.087 7.369   55.424  1.00 20.49 ? 369 HOH B O   1 
HETATM 6249 O  O   . HOH S 5 .   ? 2.521   -5.738  39.875  1.00 20.78 ? 370 HOH B O   1 
HETATM 6250 O  O   . HOH S 5 .   ? -1.685  -12.549 34.142  1.00 22.75 ? 371 HOH B O   1 
HETATM 6251 O  O   . HOH S 5 .   ? -23.956 -10.886 37.216  1.00 31.67 ? 372 HOH B O   1 
HETATM 6252 O  O   . HOH S 5 .   ? 9.870   2.250   26.327  1.00 29.93 ? 373 HOH B O   1 
HETATM 6253 O  O   . HOH S 5 .   ? -14.669 -15.446 30.157  1.00 30.40 ? 374 HOH B O   1 
HETATM 6254 O  O   . HOH S 5 .   ? -17.363 -6.190  38.956  1.00 13.63 ? 375 HOH B O   1 
HETATM 6255 O  O   . HOH S 5 .   ? 5.930   -8.427  31.714  1.00 18.68 ? 376 HOH B O   1 
HETATM 6256 O  O   . HOH S 5 .   ? 3.742   9.864   34.538  1.00 19.01 ? 377 HOH B O   1 
HETATM 6257 O  O   . HOH S 5 .   ? -18.966 1.022   26.962  1.00 12.59 ? 378 HOH B O   1 
HETATM 6258 O  O   . HOH S 5 .   ? 4.307   12.297  43.610  1.00 23.55 ? 379 HOH B O   1 
HETATM 6259 O  O   . HOH S 5 .   ? 8.222   -4.892  43.693  1.00 28.81 ? 380 HOH B O   1 
HETATM 6260 O  O   . HOH S 5 .   ? -17.822 -13.291 45.530  1.00 23.09 ? 381 HOH B O   1 
HETATM 6261 O  O   . HOH S 5 .   ? -16.074 -11.219 31.560  1.00 17.97 ? 382 HOH B O   1 
HETATM 6262 O  O   . HOH S 5 .   ? -21.018 -13.459 35.670  1.00 28.61 ? 383 HOH B O   1 
HETATM 6263 O  O   . HOH S 5 .   ? -0.120  -14.053 35.820  1.00 26.89 ? 384 HOH B O   1 
HETATM 6264 O  O   . HOH S 5 .   ? -14.546 -16.936 43.891  1.00 28.75 ? 385 HOH B O   1 
HETATM 6265 O  O   . HOH S 5 .   ? -12.581 -17.063 46.010  1.00 23.75 ? 386 HOH B O   1 
HETATM 6266 O  O   . HOH S 5 .   ? -6.929  -8.320  58.385  1.00 34.03 ? 387 HOH B O   1 
HETATM 6267 O  O   . HOH S 5 .   ? -11.393 20.724  44.818  1.00 13.67 ? 388 HOH B O   1 
HETATM 6268 O  O   . HOH S 5 .   ? -4.718  7.976   51.690  1.00 25.18 ? 389 HOH B O   1 
HETATM 6269 O  O   . HOH S 5 .   ? -20.722 -4.006  46.872  1.00 17.07 ? 390 HOH B O   1 
HETATM 6270 O  O   . HOH S 5 .   ? -1.425  16.624  28.991  1.00 29.15 ? 391 HOH B O   1 
HETATM 6271 O  O   . HOH S 5 .   ? -7.057  -5.602  25.527  1.00 27.14 ? 392 HOH B O   1 
HETATM 6272 O  O   . HOH S 5 .   ? -0.380  -12.001 31.678  1.00 20.26 ? 393 HOH B O   1 
HETATM 6273 O  O   . HOH S 5 .   ? -1.119  2.210   58.331  1.00 16.47 ? 394 HOH B O   1 
HETATM 6274 O  O   . HOH S 5 .   ? -4.050  -17.572 49.160  1.00 28.33 ? 395 HOH B O   1 
HETATM 6275 O  O   . HOH S 5 .   ? 2.285   -1.160  25.465  1.00 15.67 ? 396 HOH B O   1 
HETATM 6276 O  O   . HOH S 5 .   ? -19.410 4.101   28.852  1.00 18.03 ? 397 HOH B O   1 
HETATM 6277 O  O   . HOH S 5 .   ? -19.061 -14.225 32.206  1.00 30.30 ? 398 HOH B O   1 
HETATM 6278 O  O   . HOH S 5 .   ? -16.345 -1.981  53.790  1.00 28.68 ? 399 HOH B O   1 
HETATM 6279 O  O   . HOH S 5 .   ? 1.619   7.931   58.096  1.00 23.88 ? 400 HOH B O   1 
HETATM 6280 O  O   . HOH S 5 .   ? -7.314  17.001  31.856  1.00 16.25 ? 401 HOH B O   1 
HETATM 6281 O  O   . HOH S 5 .   ? 0.979   11.927  22.538  1.00 32.37 ? 402 HOH B O   1 
HETATM 6282 O  O   . HOH S 5 .   ? -23.516 -9.639  40.085  1.00 24.18 ? 403 HOH B O   1 
HETATM 6283 O  O   . HOH S 5 .   ? -20.785 13.348  48.165  1.00 33.02 ? 404 HOH B O   1 
HETATM 6284 O  O   . HOH S 5 .   ? -1.214  20.859  30.748  1.00 32.42 ? 405 HOH B O   1 
HETATM 6285 O  O   . HOH S 5 .   ? -12.953 -1.610  26.645  1.00 21.39 ? 406 HOH B O   1 
HETATM 6286 O  O   . HOH S 5 .   ? -17.735 11.442  31.842  1.00 19.90 ? 407 HOH B O   1 
HETATM 6287 O  O   . HOH S 5 .   ? 7.971   15.692  32.374  1.00 28.84 ? 408 HOH B O   1 
HETATM 6288 O  O   . HOH S 5 .   ? -9.914  -6.377  32.144  1.00 26.85 ? 409 HOH B O   1 
HETATM 6289 O  O   . HOH S 5 .   ? 9.894   3.770   45.752  1.00 30.70 ? 410 HOH B O   1 
HETATM 6290 O  O   . HOH S 5 .   ? -17.146 19.186  48.411  1.00 14.40 ? 411 HOH B O   1 
HETATM 6291 O  O   . HOH S 5 .   ? -17.961 -16.327 41.781  1.00 24.36 ? 412 HOH B O   1 
HETATM 6292 O  O   . HOH S 5 .   ? -7.327  10.326  23.121  1.00 32.11 ? 413 HOH B O   1 
HETATM 6293 O  O   . HOH S 5 .   ? -23.649 0.022   47.787  1.00 32.20 ? 414 HOH B O   1 
HETATM 6294 O  O   . HOH S 5 .   ? -1.238  -9.715  55.268  1.00 33.52 ? 415 HOH B O   1 
HETATM 6295 O  O   . HOH S 5 .   ? -9.984  14.252  28.595  1.00 30.49 ? 416 HOH B O   1 
HETATM 6296 O  O   . HOH S 5 .   ? 0.202   17.980  46.381  1.00 32.60 ? 417 HOH B O   1 
HETATM 6297 O  O   . HOH S 5 .   ? 8.562   6.727   31.270  1.00 35.05 ? 418 HOH B O   1 
HETATM 6298 O  O   . HOH S 5 .   ? -17.002 10.785  48.323  1.00 15.56 ? 419 HOH B O   1 
HETATM 6299 O  O   . HOH S 5 .   ? -12.555 1.946   56.823  1.00 25.12 ? 420 HOH B O   1 
HETATM 6300 O  O   . HOH S 5 .   ? -4.080  1.331   23.001  1.00 22.53 ? 421 HOH B O   1 
HETATM 6301 O  O   . HOH S 5 .   ? 4.010   14.384  40.734  1.00 23.87 ? 422 HOH B O   1 
HETATM 6302 O  O   . HOH S 5 .   ? -19.806 -12.884 43.215  1.00 25.45 ? 423 HOH B O   1 
HETATM 6303 O  O   . HOH S 5 .   ? -12.141 -19.615 41.889  1.00 28.65 ? 424 HOH B O   1 
HETATM 6304 O  O   . HOH S 5 .   ? -20.683 19.813  41.252  1.00 19.41 ? 425 HOH B O   1 
HETATM 6305 O  O   . HOH S 5 .   ? 9.647   12.837  30.850  1.00 24.86 ? 426 HOH B O   1 
HETATM 6306 O  O   . HOH S 5 .   ? -9.019  -10.146 55.781  1.00 25.98 ? 427 HOH B O   1 
HETATM 6307 O  O   . HOH S 5 .   ? 1.744   -1.883  39.770  1.00 27.86 ? 428 HOH B O   1 
HETATM 6308 O  O   . HOH S 5 .   ? -6.747  1.855   36.703  1.00 15.72 ? 429 HOH B O   1 
HETATM 6309 O  O   . HOH S 5 .   ? -4.564  7.019   57.499  1.00 35.01 ? 430 HOH B O   1 
HETATM 6310 O  O   . HOH S 5 .   ? -8.583  -14.204 54.157  1.00 27.51 ? 431 HOH B O   1 
HETATM 6311 O  O   . HOH S 5 .   ? 2.656   15.759  34.315  1.00 19.30 ? 432 HOH B O   1 
HETATM 6312 O  O   . HOH S 5 .   ? -14.961 -14.165 52.159  1.00 33.61 ? 433 HOH B O   1 
HETATM 6313 O  O   . HOH S 5 .   ? -1.299  11.593  45.049  1.00 20.79 ? 434 HOH B O   1 
HETATM 6314 O  O   . HOH S 5 .   ? -20.835 15.562  36.231  1.00 24.42 ? 435 HOH B O   1 
HETATM 6315 O  O   . HOH S 5 .   ? -8.740  14.066  50.244  1.00 21.30 ? 436 HOH B O   1 
HETATM 6316 O  O   . HOH S 5 .   ? -12.769 -1.165  56.773  1.00 22.28 ? 437 HOH B O   1 
HETATM 6317 O  O   . HOH S 5 .   ? -18.995 -10.442 29.991  1.00 36.27 ? 438 HOH B O   1 
HETATM 6318 O  O   . HOH S 5 .   ? -0.447  19.634  42.008  1.00 25.89 ? 439 HOH B O   1 
HETATM 6319 O  O   . HOH S 5 .   ? -12.304 -19.856 52.714  1.00 38.66 ? 440 HOH B O   1 
HETATM 6320 O  O   . HOH S 5 .   ? -2.137  16.731  47.975  1.00 19.27 ? 441 HOH B O   1 
HETATM 6321 O  O   . HOH S 5 .   ? -24.280 -9.752  44.221  1.00 37.05 ? 442 HOH B O   1 
HETATM 6322 O  O   . HOH S 5 .   ? -8.951  -19.735 45.454  1.00 31.28 ? 443 HOH B O   1 
HETATM 6323 O  O   . HOH S 5 .   ? -14.103 -0.099  49.812  1.00 17.93 ? 444 HOH B O   1 
HETATM 6324 O  O   . HOH S 5 .   ? -8.699  -11.648 32.693  1.00 18.13 ? 445 HOH B O   1 
HETATM 6325 O  O   . HOH S 5 .   ? -6.249  -0.628  61.749  1.00 26.98 ? 446 HOH B O   1 
HETATM 6326 O  O   . HOH S 5 .   ? -11.910 -8.196  26.015  1.00 28.92 ? 447 HOH B O   1 
HETATM 6327 O  O   . HOH S 5 .   ? -12.675 -6.241  52.841  1.00 23.88 ? 448 HOH B O   1 
HETATM 6328 O  O   . HOH S 5 .   ? -9.962  -2.565  26.081  1.00 20.99 ? 449 HOH B O   1 
HETATM 6329 O  O   . HOH S 5 .   ? -10.530 3.827   22.368  1.00 32.60 ? 450 HOH B O   1 
HETATM 6330 O  O   . HOH S 5 .   ? -10.421 -5.654  24.826  1.00 27.49 ? 451 HOH B O   1 
HETATM 6331 O  O   . HOH S 5 .   ? 3.609   2.413   39.091  1.00 33.03 ? 452 HOH B O   1 
HETATM 6332 O  O   . HOH S 5 .   ? -2.334  -16.085 50.473  1.00 29.01 ? 453 HOH B O   1 
HETATM 6333 O  O   . HOH S 5 .   ? 4.954   7.143   48.468  1.00 22.25 ? 454 HOH B O   1 
HETATM 6334 O  O   . HOH S 5 .   ? -6.077  15.634  50.851  1.00 30.00 ? 455 HOH B O   1 
HETATM 6335 O  O   . HOH S 5 .   ? -2.825  8.459   53.284  1.00 32.95 ? 456 HOH B O   1 
HETATM 6336 O  O   . HOH S 5 .   ? -10.955 -8.237  56.722  1.00 29.24 ? 457 HOH B O   1 
HETATM 6337 O  O   . HOH S 5 .   ? 3.602   -7.174  52.070  1.00 30.63 ? 458 HOH B O   1 
HETATM 6338 O  O   . HOH S 5 .   ? 4.895   9.015   46.055  1.00 34.00 ? 459 HOH B O   1 
HETATM 6339 O  O   . HOH S 5 .   ? -11.241 17.000  25.640  1.00 35.35 ? 460 HOH B O   1 
HETATM 6340 O  O   . HOH S 5 .   ? -21.175 5.021   30.205  1.00 25.83 ? 461 HOH B O   1 
HETATM 6341 O  O   . HOH S 5 .   ? -10.218 1.813   24.382  1.00 27.12 ? 462 HOH B O   1 
HETATM 6342 O  O   . HOH S 5 .   ? -3.630  9.302   22.528  1.00 29.73 ? 463 HOH B O   1 
HETATM 6343 O  O   . HOH S 5 .   ? -0.316  -9.290  57.583  1.00 32.34 ? 464 HOH B O   1 
HETATM 6344 O  O   . HOH S 5 .   ? -6.830  18.400  25.127  1.00 36.94 ? 465 HOH B O   1 
HETATM 6345 O  O   . HOH S 5 .   ? -16.035 21.858  37.615  1.00 32.80 ? 466 HOH B O   1 
HETATM 6346 O  O   . HOH S 5 .   ? -20.726 8.908   28.726  1.00 31.12 ? 467 HOH B O   1 
HETATM 6347 O  O   . HOH S 5 .   ? -7.855  8.948   55.628  1.00 32.85 ? 468 HOH B O   1 
HETATM 6348 O  O   . HOH S 5 .   ? -2.462  9.707   49.330  1.00 28.79 ? 469 HOH B O   1 
HETATM 6349 O  O   . HOH S 5 .   ? -8.353  -5.318  59.402  1.00 31.21 ? 470 HOH B O   1 
HETATM 6350 O  O   . HOH S 5 .   ? -0.338  13.581  46.903  1.00 28.69 ? 471 HOH B O   1 
HETATM 6351 O  O   . HOH S 5 .   ? -0.574  15.816  26.906  1.00 33.36 ? 472 HOH B O   1 
HETATM 6352 O  O   . HOH S 5 .   ? -3.917  0.860   63.863  1.00 33.89 ? 473 HOH B O   1 
HETATM 6353 O  O   . HOH S 5 .   ? -19.541 20.195  47.393  1.00 28.65 ? 474 HOH B O   1 
HETATM 6354 O  O   . HOH S 5 .   ? -21.135 18.460  47.380  1.00 36.09 ? 475 HOH B O   1 
HETATM 6355 O  O   . HOH S 5 .   ? 6.621   15.734  27.779  1.00 34.13 ? 476 HOH B O   1 
HETATM 6356 O  O   . HOH S 5 .   ? -3.436  18.747  27.827  1.00 34.70 ? 477 HOH B O   1 
HETATM 6357 O  O   . HOH S 5 .   ? -8.066  -4.845  23.687  1.00 36.05 ? 478 HOH B O   1 
HETATM 6358 O  O   . HOH S 5 .   ? -9.187  -8.531  59.623  1.00 29.80 ? 479 HOH B O   1 
HETATM 6359 O  O   . HOH S 5 .   ? -6.511  -12.124 61.575  1.00 43.56 ? 480 HOH B O   1 
HETATM 6360 O  O   . HOH S 5 .   ? 0.792   -11.462 58.163  1.00 30.11 ? 481 HOH B O   1 
HETATM 6361 O  O   . HOH S 5 .   ? -11.830 3.949   58.477  1.00 41.42 ? 482 HOH B O   1 
HETATM 6362 O  O   . HOH S 5 .   ? 0.817   -2.379  34.130  1.00 24.41 ? 483 HOH B O   1 
HETATM 6363 O  O   . HOH S 5 .   ? -7.601  -7.244  60.171  1.00 16.81 ? 484 HOH B O   1 
HETATM 6364 O  O   . HOH S 5 .   ? -10.866 -18.591 44.889  1.00 36.76 ? 485 HOH B O   1 
HETATM 6365 O  O   . HOH S 5 .   ? 13.279  5.149   51.253  1.00 29.87 ? 486 HOH B O   1 
HETATM 6366 O  O   . HOH S 5 .   ? -22.812 -5.616  48.145  1.00 29.11 ? 487 HOH B O   1 
HETATM 6367 O  O   . HOH S 5 .   ? -17.964 -12.508 30.096  1.00 32.68 ? 488 HOH B O   1 
HETATM 6368 O  O   . HOH S 5 .   ? -15.358 -1.346  25.437  1.00 23.71 ? 489 HOH B O   1 
HETATM 6369 O  O   . HOH S 5 .   ? -14.349 8.595   20.816  1.00 32.67 ? 490 HOH B O   1 
HETATM 6370 O  O   . HOH S 5 .   ? -7.085  -8.115  25.777  1.00 34.80 ? 491 HOH B O   1 
HETATM 6371 O  O   . HOH S 5 .   ? 1.709   -13.806 31.710  1.00 32.03 ? 492 HOH B O   1 
HETATM 6372 O  O   . HOH S 5 .   ? -5.448  1.345   60.363  1.00 27.43 ? 493 HOH B O   1 
HETATM 6373 O  O   . HOH S 5 .   ? -16.906 3.132   56.641  1.00 33.59 ? 494 HOH B O   1 
HETATM 6374 O  O   . HOH S 5 .   ? -22.917 13.452  37.581  1.00 29.68 ? 495 HOH B O   1 
HETATM 6375 O  O   . HOH S 5 .   ? 7.808   7.692   42.087  1.00 37.03 ? 496 HOH B O   1 
HETATM 6376 O  O   . HOH S 5 .   ? -24.712 15.320  38.870  1.00 36.33 ? 497 HOH B O   1 
HETATM 6377 O  O   . HOH T 5 .   ? -5.071  12.924  24.218  1.00 29.22 ? 301 HOH C O   1 
HETATM 6378 O  O   . HOH T 5 .   ? -7.089  33.119  21.127  1.00 27.74 ? 302 HOH C O   1 
HETATM 6379 O  O   . HOH T 5 .   ? -14.797 34.220  21.229  1.00 35.53 ? 303 HOH C O   1 
HETATM 6380 O  O   . HOH T 5 .   ? 6.876   13.571  13.961  1.00 29.70 ? 304 HOH C O   1 
HETATM 6381 O  O   . HOH T 5 .   ? -10.384 41.994  18.819  1.00 32.30 ? 305 HOH C O   1 
HETATM 6382 O  O   . HOH T 5 .   ? -1.174  20.741  27.991  1.00 32.68 ? 306 HOH C O   1 
HETATM 6383 O  O   . HOH T 5 .   ? 1.183   22.963  3.773   1.00 27.53 ? 307 HOH C O   1 
HETATM 6384 O  O   . HOH T 5 .   ? 4.554   27.200  -7.713  1.00 26.96 ? 308 HOH C O   1 
HETATM 6385 O  O   . HOH T 5 .   ? -19.882 18.394  8.679   1.00 29.46 ? 309 HOH C O   1 
HETATM 6386 O  O   . HOH T 5 .   ? 6.454   29.770  14.363  1.00 38.74 ? 310 HOH C O   1 
HETATM 6387 O  O   . HOH T 5 .   ? -12.446 18.917  21.281  1.00 29.80 ? 311 HOH C O   1 
HETATM 6388 O  O   . HOH T 5 .   ? -2.802  12.987  24.627  1.00 31.24 ? 312 HOH C O   1 
HETATM 6389 O  O   . HOH T 5 .   ? -7.597  43.632  15.077  1.00 19.94 ? 313 HOH C O   1 
HETATM 6390 O  O   . HOH T 5 .   ? -10.216 45.125  15.351  1.00 31.78 ? 314 HOH C O   1 
HETATM 6391 O  O   . HOH T 5 .   ? -5.444  39.093  23.757  1.00 22.53 ? 315 HOH C O   1 
HETATM 6392 O  O   . HOH T 5 .   ? -12.379 23.714  -5.486  1.00 30.09 ? 316 HOH C O   1 
HETATM 6393 O  O   . HOH T 5 .   ? -7.031  12.744  21.738  1.00 30.77 ? 317 HOH C O   1 
HETATM 6394 O  O   . HOH T 5 .   ? -2.244  48.045  5.806   1.00 32.32 ? 318 HOH C O   1 
HETATM 6395 O  O   . HOH T 5 .   ? -16.851 22.302  22.435  1.00 33.97 ? 319 HOH C O   1 
HETATM 6396 O  O   . HOH T 5 .   ? -15.977 21.881  -3.991  1.00 35.63 ? 320 HOH C O   1 
HETATM 6397 O  O   . HOH T 5 .   ? 1.900   13.133  2.243   1.00 31.88 ? 321 HOH C O   1 
HETATM 6398 O  O   . HOH T 5 .   ? -9.758  27.517  -8.539  1.00 25.71 ? 322 HOH C O   1 
HETATM 6399 O  O   . HOH T 5 .   ? -9.668  12.021  13.408  1.00 22.29 ? 323 HOH C O   1 
HETATM 6400 O  O   . HOH T 5 .   ? 6.699   36.804  -2.541  1.00 25.60 ? 324 HOH C O   1 
HETATM 6401 O  O   . HOH T 5 .   ? -3.763  23.433  -6.813  1.00 21.57 ? 325 HOH C O   1 
HETATM 6402 O  O   . HOH T 5 .   ? -8.262  52.029  6.784   1.00 29.40 ? 326 HOH C O   1 
HETATM 6403 O  O   . HOH T 5 .   ? -21.170 38.265  13.595  1.00 21.57 ? 327 HOH C O   1 
HETATM 6404 O  O   . HOH T 5 .   ? -7.707  29.235  -2.116  1.00 17.06 ? 328 HOH C O   1 
HETATM 6405 O  O   . HOH T 5 .   ? 4.892   25.578  -4.847  1.00 40.98 ? 329 HOH C O   1 
HETATM 6406 O  O   . HOH T 5 .   ? 14.746  31.194  4.463   1.00 39.03 ? 330 HOH C O   1 
HETATM 6407 O  O   . HOH T 5 .   ? -24.804 25.601  7.694   1.00 33.86 ? 331 HOH C O   1 
HETATM 6408 O  O   . HOH T 5 .   ? -20.230 17.209  13.536  1.00 31.77 ? 332 HOH C O   1 
HETATM 6409 O  O   . HOH T 5 .   ? -0.271  38.958  10.882  1.00 22.85 ? 333 HOH C O   1 
HETATM 6410 O  O   . HOH T 5 .   ? 4.930   20.704  17.022  1.00 20.79 ? 334 HOH C O   1 
HETATM 6411 O  O   . HOH T 5 .   ? -0.365  23.280  -2.777  1.00 26.85 ? 335 HOH C O   1 
HETATM 6412 O  O   . HOH T 5 .   ? -21.658 43.008  3.277   1.00 27.05 ? 336 HOH C O   1 
HETATM 6413 O  O   . HOH T 5 .   ? -19.163 22.850  18.713  1.00 24.31 ? 337 HOH C O   1 
HETATM 6414 O  O   . HOH T 5 .   ? -18.584 22.053  2.024   1.00 24.20 ? 338 HOH C O   1 
HETATM 6415 O  O   . HOH T 5 .   ? -24.963 30.650  5.493   1.00 25.77 ? 339 HOH C O   1 
HETATM 6416 O  O   . HOH T 5 .   ? -7.511  28.669  11.718  1.00 18.81 ? 340 HOH C O   1 
HETATM 6417 O  O   . HOH T 5 .   ? -18.892 33.536  6.272   1.00 17.25 ? 341 HOH C O   1 
HETATM 6418 O  O   . HOH T 5 .   ? -2.718  34.734  -11.155 1.00 23.48 ? 342 HOH C O   1 
HETATM 6419 O  O   . HOH T 5 .   ? -13.230 43.946  16.906  1.00 44.25 ? 343 HOH C O   1 
HETATM 6420 O  O   . HOH T 5 .   ? -8.505  35.581  -7.599  1.00 25.32 ? 344 HOH C O   1 
HETATM 6421 O  O   . HOH T 5 .   ? -11.649 41.674  14.943  1.00 19.85 ? 345 HOH C O   1 
HETATM 6422 O  O   . HOH T 5 .   ? 0.161   21.753  -0.630  1.00 20.99 ? 346 HOH C O   1 
HETATM 6423 O  O   . HOH T 5 .   ? -6.842  43.424  17.715  1.00 23.13 ? 347 HOH C O   1 
HETATM 6424 O  O   . HOH T 5 .   ? 9.558   37.337  -1.021  1.00 29.02 ? 348 HOH C O   1 
HETATM 6425 O  O   . HOH T 5 .   ? -17.215 13.196  10.910  1.00 28.00 ? 349 HOH C O   1 
HETATM 6426 O  O   . HOH T 5 .   ? -21.946 23.958  1.437   1.00 28.56 ? 350 HOH C O   1 
HETATM 6427 O  O   . HOH T 5 .   ? 1.602   12.225  19.650  1.00 33.95 ? 351 HOH C O   1 
HETATM 6428 O  O   . HOH T 5 .   ? -15.930 16.450  13.648  1.00 27.52 ? 352 HOH C O   1 
HETATM 6429 O  O   . HOH T 5 .   ? -22.722 23.044  10.030  1.00 29.93 ? 353 HOH C O   1 
HETATM 6430 O  O   . HOH T 5 .   ? -17.351 14.796  5.213   1.00 18.85 ? 354 HOH C O   1 
HETATM 6431 O  O   . HOH T 5 .   ? -0.425  39.773  15.491  1.00 29.62 ? 355 HOH C O   1 
HETATM 6432 O  O   . HOH T 5 .   ? 7.522   22.332  8.909   1.00 26.25 ? 356 HOH C O   1 
HETATM 6433 O  O   . HOH T 5 .   ? -19.299 48.147  -4.536  1.00 34.48 ? 357 HOH C O   1 
HETATM 6434 O  O   . HOH T 5 .   ? 7.837   17.271  8.106   1.00 26.79 ? 358 HOH C O   1 
HETATM 6435 O  O   . HOH T 5 .   ? -1.351  24.324  6.933   1.00 22.43 ? 359 HOH C O   1 
HETATM 6436 O  O   . HOH T 5 .   ? -7.149  27.817  -9.005  1.00 23.90 ? 360 HOH C O   1 
HETATM 6437 O  O   . HOH T 5 .   ? -19.398 40.612  -0.327  1.00 23.96 ? 361 HOH C O   1 
HETATM 6438 O  O   . HOH T 5 .   ? -18.906 31.003  -2.267  1.00 18.06 ? 362 HOH C O   1 
HETATM 6439 O  O   . HOH T 5 .   ? -14.834 26.518  22.810  1.00 27.51 ? 363 HOH C O   1 
HETATM 6440 O  O   . HOH T 5 .   ? -1.983  30.976  24.988  1.00 14.84 ? 364 HOH C O   1 
HETATM 6441 O  O   . HOH T 5 .   ? 0.214   17.581  -1.110  1.00 29.80 ? 365 HOH C O   1 
HETATM 6442 O  O   . HOH T 5 .   ? 0.620   39.776  -2.158  1.00 29.67 ? 366 HOH C O   1 
HETATM 6443 O  O   . HOH T 5 .   ? 11.898  31.066  -1.061  1.00 19.60 ? 367 HOH C O   1 
HETATM 6444 O  O   . HOH T 5 .   ? -24.674 30.558  0.835   1.00 29.57 ? 368 HOH C O   1 
HETATM 6445 O  O   . HOH T 5 .   ? -20.975 24.615  17.794  1.00 31.28 ? 369 HOH C O   1 
HETATM 6446 O  O   . HOH T 5 .   ? 0.166   42.063  19.498  1.00 19.22 ? 370 HOH C O   1 
HETATM 6447 O  O   . HOH T 5 .   ? 3.930   23.998  17.140  1.00 20.66 ? 371 HOH C O   1 
HETATM 6448 O  O   . HOH T 5 .   ? -9.823  50.113  1.010   1.00 40.50 ? 372 HOH C O   1 
HETATM 6449 O  O   . HOH T 5 .   ? -24.597 30.752  12.196  1.00 31.80 ? 373 HOH C O   1 
HETATM 6450 O  O   . HOH T 5 .   ? -2.022  36.504  13.657  1.00 27.93 ? 374 HOH C O   1 
HETATM 6451 O  O   . HOH T 5 .   ? -4.225  9.781   3.493   1.00 15.23 ? 375 HOH C O   1 
HETATM 6452 O  O   . HOH T 5 .   ? 3.951   31.146  -7.543  1.00 16.27 ? 376 HOH C O   1 
HETATM 6453 O  O   . HOH T 5 .   ? -10.811 21.298  -5.624  1.00 27.59 ? 377 HOH C O   1 
HETATM 6454 O  O   . HOH T 5 .   ? -6.692  49.489  11.599  1.00 22.36 ? 378 HOH C O   1 
HETATM 6455 O  O   . HOH T 5 .   ? 0.363   24.195  29.805  1.00 32.39 ? 379 HOH C O   1 
HETATM 6456 O  O   . HOH T 5 .   ? -17.692 44.873  2.039   1.00 28.89 ? 380 HOH C O   1 
HETATM 6457 O  O   . HOH T 5 .   ? -17.191 48.165  4.918   1.00 29.52 ? 381 HOH C O   1 
HETATM 6458 O  O   . HOH T 5 .   ? -0.729  15.748  21.298  1.00 32.85 ? 382 HOH C O   1 
HETATM 6459 O  O   . HOH T 5 .   ? -4.000  10.345  10.432  1.00 21.71 ? 383 HOH C O   1 
HETATM 6460 O  O   . HOH T 5 .   ? 7.410   34.074  10.336  1.00 37.05 ? 384 HOH C O   1 
HETATM 6461 O  O   . HOH T 5 .   ? -16.533 11.832  8.931   1.00 29.85 ? 385 HOH C O   1 
HETATM 6462 O  O   . HOH T 5 .   ? -20.586 22.547  14.781  1.00 21.48 ? 386 HOH C O   1 
HETATM 6463 O  O   . HOH T 5 .   ? -3.857  25.896  -8.075  1.00 30.35 ? 387 HOH C O   1 
HETATM 6464 O  O   . HOH T 5 .   ? -16.739 30.052  19.635  1.00 23.48 ? 388 HOH C O   1 
HETATM 6465 O  O   . HOH T 5 .   ? -1.717  41.036  -3.381  1.00 26.84 ? 389 HOH C O   1 
HETATM 6466 O  O   . HOH T 5 .   ? -2.045  19.293  -3.427  1.00 13.21 ? 390 HOH C O   1 
HETATM 6467 O  O   . HOH T 5 .   ? -24.653 40.155  12.217  1.00 41.53 ? 391 HOH C O   1 
HETATM 6468 O  O   . HOH T 5 .   ? -21.297 27.726  17.377  1.00 30.15 ? 392 HOH C O   1 
HETATM 6469 O  O   . HOH T 5 .   ? -1.447  11.936  0.073   1.00 16.16 ? 393 HOH C O   1 
HETATM 6470 O  O   . HOH T 5 .   ? 0.223   35.206  10.774  1.00 31.13 ? 394 HOH C O   1 
HETATM 6471 O  O   . HOH T 5 .   ? -8.931  9.904   -1.641  1.00 11.16 ? 395 HOH C O   1 
HETATM 6472 O  O   . HOH T 5 .   ? -2.383  40.317  12.192  1.00 25.49 ? 396 HOH C O   1 
HETATM 6473 O  O   . HOH T 5 .   ? -12.896 35.352  22.165  1.00 29.24 ? 397 HOH C O   1 
HETATM 6474 O  O   . HOH T 5 .   ? 4.445   17.982  17.180  1.00 22.32 ? 398 HOH C O   1 
HETATM 6475 O  O   . HOH T 5 .   ? -2.204  17.104  -1.220  1.00 22.85 ? 399 HOH C O   1 
HETATM 6476 O  O   . HOH T 5 .   ? -6.139  45.764  14.133  1.00 26.33 ? 400 HOH C O   1 
HETATM 6477 O  O   . HOH T 5 .   ? -24.313 29.564  8.249   1.00 23.70 ? 401 HOH C O   1 
HETATM 6478 O  O   . HOH T 5 .   ? -0.316  11.622  2.368   1.00 29.66 ? 402 HOH C O   1 
HETATM 6479 O  O   . HOH T 5 .   ? -15.414 45.941  0.985   1.00 24.66 ? 403 HOH C O   1 
HETATM 6480 O  O   . HOH T 5 .   ? -5.224  13.975  16.767  1.00 18.72 ? 404 HOH C O   1 
HETATM 6481 O  O   . HOH T 5 .   ? -3.621  44.201  -3.029  1.00 30.89 ? 405 HOH C O   1 
HETATM 6482 O  O   . HOH T 5 .   ? 8.823   19.489  20.346  1.00 38.94 ? 406 HOH C O   1 
HETATM 6483 O  O   . HOH T 5 .   ? -16.592 18.959  -0.680  1.00 34.97 ? 407 HOH C O   1 
HETATM 6484 O  O   . HOH T 5 .   ? 4.642   13.766  9.110   1.00 26.51 ? 408 HOH C O   1 
HETATM 6485 O  O   . HOH T 5 .   ? -3.303  10.596  5.826   1.00 26.09 ? 409 HOH C O   1 
HETATM 6486 O  O   . HOH T 5 .   ? -16.923 23.653  20.219  1.00 22.71 ? 410 HOH C O   1 
HETATM 6487 O  O   . HOH T 5 .   ? -25.154 34.994  3.325   1.00 26.65 ? 411 HOH C O   1 
HETATM 6488 O  O   . HOH T 5 .   ? -18.454 36.160  20.084  1.00 31.44 ? 412 HOH C O   1 
HETATM 6489 O  O   . HOH T 5 .   ? -22.794 27.358  14.809  1.00 31.42 ? 413 HOH C O   1 
HETATM 6490 O  O   . HOH T 5 .   ? -11.026 29.206  -2.951  1.00 16.96 ? 414 HOH C O   1 
HETATM 6491 O  O   . HOH T 5 .   ? -14.144 35.370  14.844  1.00 21.98 ? 415 HOH C O   1 
HETATM 6492 O  O   . HOH T 5 .   ? -20.089 25.459  -3.361  1.00 33.77 ? 416 HOH C O   1 
HETATM 6493 O  O   . HOH T 5 .   ? 9.189   22.485  22.424  1.00 30.22 ? 417 HOH C O   1 
HETATM 6494 O  O   . HOH T 5 .   ? -0.835  32.722  -12.153 1.00 30.79 ? 418 HOH C O   1 
HETATM 6495 O  O   . HOH T 5 .   ? -14.467 39.242  17.090  1.00 27.50 ? 419 HOH C O   1 
HETATM 6496 O  O   . HOH T 5 .   ? 6.227   39.994  8.970   1.00 27.90 ? 420 HOH C O   1 
HETATM 6497 O  O   . HOH T 5 .   ? -11.245 17.998  -1.900  1.00 14.86 ? 421 HOH C O   1 
HETATM 6498 O  O   . HOH T 5 .   ? -8.361  30.990  -9.119  1.00 19.87 ? 422 HOH C O   1 
HETATM 6499 O  O   . HOH T 5 .   ? -9.050  29.524  25.760  1.00 22.35 ? 423 HOH C O   1 
HETATM 6500 O  O   . HOH T 5 .   ? 3.321   41.572  -0.814  1.00 36.28 ? 424 HOH C O   1 
HETATM 6501 O  O   . HOH T 5 .   ? 2.686   21.281  5.624   1.00 23.09 ? 425 HOH C O   1 
HETATM 6502 O  O   . HOH T 5 .   ? -24.489 35.054  -0.816  1.00 27.42 ? 426 HOH C O   1 
HETATM 6503 O  O   . HOH T 5 .   ? -21.818 39.630  1.245   1.00 25.86 ? 427 HOH C O   1 
HETATM 6504 O  O   . HOH T 5 .   ? 12.891  29.351  0.763   1.00 22.38 ? 428 HOH C O   1 
HETATM 6505 O  O   . HOH T 5 .   ? -24.003 36.694  14.337  1.00 37.77 ? 429 HOH C O   1 
HETATM 6506 O  O   . HOH T 5 .   ? -13.903 7.789   4.385   1.00 22.66 ? 430 HOH C O   1 
HETATM 6507 O  O   . HOH T 5 .   ? -14.913 50.137  -1.440  1.00 32.75 ? 431 HOH C O   1 
HETATM 6508 O  O   . HOH T 5 .   ? -10.496 35.368  -5.793  1.00 30.46 ? 432 HOH C O   1 
HETATM 6509 O  O   . HOH T 5 .   ? -7.916  40.485  -7.683  1.00 27.84 ? 433 HOH C O   1 
HETATM 6510 O  O   . HOH T 5 .   ? 4.115   16.181  2.994   1.00 22.29 ? 434 HOH C O   1 
HETATM 6511 O  O   . HOH T 5 .   ? 7.371   20.058  11.143  1.00 27.27 ? 435 HOH C O   1 
HETATM 6512 O  O   . HOH T 5 .   ? 8.145   27.857  3.624   1.00 26.23 ? 436 HOH C O   1 
HETATM 6513 O  O   . HOH T 5 .   ? 6.742   16.756  23.103  1.00 39.67 ? 437 HOH C O   1 
HETATM 6514 O  O   . HOH T 5 .   ? -9.012  21.633  26.187  1.00 33.20 ? 438 HOH C O   1 
HETATM 6515 O  O   . HOH T 5 .   ? 4.613   11.405  19.842  1.00 35.42 ? 439 HOH C O   1 
HETATM 6516 O  O   . HOH T 5 .   ? -14.979 32.099  20.951  1.00 27.46 ? 440 HOH C O   1 
HETATM 6517 O  O   . HOH T 5 .   ? -3.495  10.085  7.695   1.00 29.92 ? 441 HOH C O   1 
HETATM 6518 O  O   . HOH T 5 .   ? 8.547   19.166  13.350  1.00 35.54 ? 442 HOH C O   1 
HETATM 6519 O  O   . HOH T 5 .   ? -14.221 40.892  14.704  1.00 24.46 ? 443 HOH C O   1 
HETATM 6520 O  O   . HOH T 5 .   ? -13.169 31.511  22.441  1.00 34.23 ? 444 HOH C O   1 
HETATM 6521 O  O   . HOH T 5 .   ? -25.750 38.532  4.026   1.00 34.74 ? 445 HOH C O   1 
HETATM 6522 O  O   . HOH T 5 .   ? -17.549 44.077  -5.852  1.00 51.41 ? 446 HOH C O   1 
HETATM 6523 O  O   . HOH T 5 .   ? 7.742   25.466  6.306   1.00 39.00 ? 447 HOH C O   1 
HETATM 6524 O  O   . HOH T 5 .   ? -12.798 34.673  -6.481  1.00 31.36 ? 448 HOH C O   1 
HETATM 6525 O  O   . HOH T 5 .   ? -24.994 33.426  1.159   1.00 33.26 ? 449 HOH C O   1 
HETATM 6526 O  O   . HOH T 5 .   ? -9.029  15.940  19.206  1.00 26.54 ? 450 HOH C O   1 
HETATM 6527 O  O   . HOH T 5 .   ? 6.916   27.861  21.197  1.00 35.23 ? 451 HOH C O   1 
HETATM 6528 O  O   . HOH T 5 .   ? 1.697   25.196  -7.639  1.00 41.26 ? 452 HOH C O   1 
HETATM 6529 O  O   . HOH T 5 .   ? -0.342  16.776  23.149  1.00 33.93 ? 453 HOH C O   1 
HETATM 6530 O  O   . HOH T 5 .   ? -19.368 29.834  19.828  1.00 32.71 ? 454 HOH C O   1 
HETATM 6531 O  O   . HOH T 5 .   ? 0.205   19.509  -1.798  1.00 30.45 ? 455 HOH C O   1 
HETATM 6532 O  O   . HOH T 5 .   ? -9.567  38.089  23.339  1.00 31.35 ? 456 HOH C O   1 
HETATM 6533 O  O   . HOH T 5 .   ? -4.584  8.396   7.556   1.00 34.35 ? 457 HOH C O   1 
HETATM 6534 O  O   . HOH T 5 .   ? 4.512   19.541  4.272   1.00 30.40 ? 458 HOH C O   1 
HETATM 6535 O  O   . HOH T 5 .   ? 2.142   22.998  1.266   1.00 30.28 ? 459 HOH C O   1 
HETATM 6536 O  O   . HOH T 5 .   ? -7.472  47.782  14.180  1.00 34.31 ? 460 HOH C O   1 
HETATM 6537 O  O   . HOH T 5 .   ? 5.820   18.625  24.717  1.00 38.90 ? 461 HOH C O   1 
HETATM 6538 O  O   . HOH T 5 .   ? -6.959  34.923  -11.081 1.00 44.47 ? 462 HOH C O   1 
HETATM 6539 O  O   . HOH T 5 .   ? 1.791   8.208   16.198  1.00 37.25 ? 463 HOH C O   1 
HETATM 6540 O  O   . HOH T 5 .   ? -0.810  34.228  -15.401 1.00 33.85 ? 464 HOH C O   1 
HETATM 6541 O  O   . HOH T 5 .   ? -10.909 8.039   -0.880  1.00 30.25 ? 465 HOH C O   1 
HETATM 6542 O  O   . HOH T 5 .   ? -13.182 9.509   -1.845  1.00 34.72 ? 466 HOH C O   1 
HETATM 6543 O  O   . HOH T 5 .   ? -6.721  21.493  26.957  1.00 39.59 ? 467 HOH C O   1 
HETATM 6544 O  O   . HOH T 5 .   ? 3.955   9.693   16.054  1.00 34.47 ? 468 HOH C O   1 
HETATM 6545 O  O   . HOH T 5 .   ? -20.314 15.494  2.134   1.00 33.28 ? 469 HOH C O   1 
HETATM 6546 O  O   . HOH T 5 .   ? -2.496  34.782  16.115  1.00 28.98 ? 470 HOH C O   1 
HETATM 6547 O  O   . HOH T 5 .   ? -21.270 20.729  19.548  1.00 36.33 ? 471 HOH C O   1 
HETATM 6548 O  O   . HOH T 5 .   ? -16.652 7.260   5.409   1.00 38.75 ? 472 HOH C O   1 
HETATM 6549 O  O   . HOH T 5 .   ? -18.558 13.256  6.861   1.00 32.59 ? 473 HOH C O   1 
HETATM 6550 O  O   . HOH T 5 .   ? -26.002 29.166  2.917   1.00 34.92 ? 474 HOH C O   1 
HETATM 6551 O  O   . HOH T 5 .   ? 0.102   30.620  -10.599 1.00 33.03 ? 475 HOH C O   1 
HETATM 6552 O  O   . HOH T 5 .   ? -16.590 28.080  21.319  1.00 36.26 ? 476 HOH C O   1 
HETATM 6553 O  O   . HOH T 5 .   ? -10.943 25.489  -10.073 1.00 34.43 ? 477 HOH C O   1 
HETATM 6554 O  O   . HOH T 5 .   ? -27.961 24.481  3.978   1.00 43.95 ? 478 HOH C O   1 
HETATM 6555 O  O   . HOH T 5 .   ? 9.327   27.334  10.651  1.00 39.98 ? 479 HOH C O   1 
HETATM 6556 O  O   . HOH U 5 .   ? -3.430  24.693  43.483  1.00 31.59 ? 301 HOH D O   1 
HETATM 6557 O  O   . HOH U 5 .   ? -0.419  34.262  17.883  1.00 33.48 ? 302 HOH D O   1 
HETATM 6558 O  O   . HOH U 5 .   ? 9.827   18.237  34.006  1.00 35.38 ? 303 HOH D O   1 
HETATM 6559 O  O   . HOH U 5 .   ? -6.635  53.732  32.313  1.00 28.31 ? 304 HOH D O   1 
HETATM 6560 O  O   . HOH U 5 .   ? -6.260  42.177  38.278  1.00 29.38 ? 305 HOH D O   1 
HETATM 6561 O  O   . HOH U 5 .   ? -10.082 42.491  41.546  1.00 27.01 ? 306 HOH D O   1 
HETATM 6562 O  O   . HOH U 5 .   ? 2.965   55.067  37.334  1.00 28.29 ? 307 HOH D O   1 
HETATM 6563 O  O   . HOH U 5 .   ? 9.334   41.525  49.945  1.00 24.53 ? 308 HOH D O   1 
HETATM 6564 O  O   . HOH U 5 .   ? 18.861  44.546  47.219  1.00 29.33 ? 309 HOH D O   1 
HETATM 6565 O  O   . HOH U 5 .   ? -1.135  50.675  40.752  1.00 26.65 ? 310 HOH D O   1 
HETATM 6566 O  O   . HOH U 5 .   ? 24.205  35.841  44.116  1.00 20.35 ? 311 HOH D O   1 
HETATM 6567 O  O   . HOH U 5 .   ? -7.758  37.675  25.958  1.00 28.31 ? 312 HOH D O   1 
HETATM 6568 O  O   . HOH U 5 .   ? 3.023   47.436  24.255  1.00 18.20 ? 313 HOH D O   1 
HETATM 6569 O  O   . HOH U 5 .   ? 3.554   55.432  24.901  1.00 34.26 ? 314 HOH D O   1 
HETATM 6570 O  O   . HOH U 5 .   ? -1.660  26.843  34.292  1.00 20.25 ? 315 HOH D O   1 
HETATM 6571 O  O   . HOH U 5 .   ? 8.187   21.207  30.699  1.00 28.13 ? 316 HOH D O   1 
HETATM 6572 O  O   . HOH U 5 .   ? 9.046   31.696  27.746  1.00 28.43 ? 317 HOH D O   1 
HETATM 6573 O  O   . HOH U 5 .   ? 15.566  47.615  26.830  1.00 39.44 ? 318 HOH D O   1 
HETATM 6574 O  O   . HOH U 5 .   ? 0.668   26.388  46.139  1.00 30.28 ? 319 HOH D O   1 
HETATM 6575 O  O   . HOH U 5 .   ? 7.926   52.402  50.667  1.00 36.38 ? 320 HOH D O   1 
HETATM 6576 O  O   . HOH U 5 .   ? 9.800   37.111  30.873  1.00 26.72 ? 321 HOH D O   1 
HETATM 6577 O  O   . HOH U 5 .   ? 17.569  47.215  29.883  1.00 31.07 ? 322 HOH D O   1 
HETATM 6578 O  O   . HOH U 5 .   ? -8.331  42.518  25.128  1.00 31.13 ? 323 HOH D O   1 
HETATM 6579 O  O   . HOH U 5 .   ? 18.876  39.055  43.579  1.00 22.59 ? 324 HOH D O   1 
HETATM 6580 O  O   . HOH U 5 .   ? 23.559  35.125  48.600  1.00 33.49 ? 325 HOH D O   1 
HETATM 6581 O  O   . HOH U 5 .   ? -6.762  45.143  21.740  1.00 34.90 ? 326 HOH D O   1 
HETATM 6582 O  O   . HOH U 5 .   ? 10.464  19.582  29.743  1.00 31.33 ? 327 HOH D O   1 
HETATM 6583 O  O   . HOH U 5 .   ? 17.471  22.308  31.041  1.00 22.70 ? 328 HOH D O   1 
HETATM 6584 O  O   . HOH U 5 .   ? -9.079  38.311  40.901  1.00 24.88 ? 329 HOH D O   1 
HETATM 6585 O  O   . HOH U 5 .   ? 19.259  28.782  51.590  1.00 30.14 ? 330 HOH D O   1 
HETATM 6586 O  O   . HOH U 5 .   ? 10.446  29.390  27.523  1.00 29.33 ? 331 HOH D O   1 
HETATM 6587 O  O   . HOH U 5 .   ? -1.119  47.197  48.363  1.00 34.17 ? 332 HOH D O   1 
HETATM 6588 O  O   . HOH U 5 .   ? 19.221  39.747  40.251  1.00 19.81 ? 333 HOH D O   1 
HETATM 6589 O  O   . HOH U 5 .   ? 6.506   25.479  22.607  1.00 22.92 ? 334 HOH D O   1 
HETATM 6590 O  O   . HOH U 5 .   ? 14.222  47.175  32.118  1.00 19.69 ? 335 HOH D O   1 
HETATM 6591 O  O   . HOH U 5 .   ? 10.032  38.622  53.222  1.00 38.07 ? 336 HOH D O   1 
HETATM 6592 O  O   . HOH U 5 .   ? 12.719  30.442  26.503  1.00 26.53 ? 337 HOH D O   1 
HETATM 6593 O  O   . HOH U 5 .   ? 8.209   30.182  53.506  1.00 26.14 ? 338 HOH D O   1 
HETATM 6594 O  O   . HOH U 5 .   ? 30.130  38.329  37.890  1.00 36.13 ? 339 HOH D O   1 
HETATM 6595 O  O   . HOH U 5 .   ? 12.121  31.880  54.419  1.00 31.70 ? 340 HOH D O   1 
HETATM 6596 O  O   . HOH U 5 .   ? 8.375   57.757  44.810  1.00 29.19 ? 341 HOH D O   1 
HETATM 6597 O  O   . HOH U 5 .   ? 25.247  43.307  42.243  1.00 27.80 ? 342 HOH D O   1 
HETATM 6598 O  O   . HOH U 5 .   ? 24.308  32.643  30.249  1.00 30.05 ? 343 HOH D O   1 
HETATM 6599 O  O   . HOH U 5 .   ? 4.733   51.107  23.694  1.00 32.79 ? 344 HOH D O   1 
HETATM 6600 O  O   . HOH U 5 .   ? -2.969  25.568  27.836  1.00 26.13 ? 345 HOH D O   1 
HETATM 6601 O  O   . HOH U 5 .   ? 5.320   41.612  19.416  1.00 29.82 ? 346 HOH D O   1 
HETATM 6602 O  O   . HOH U 5 .   ? -8.492  39.257  32.509  1.00 30.14 ? 347 HOH D O   1 
HETATM 6603 O  O   . HOH U 5 .   ? 7.490   22.453  34.568  1.00 34.11 ? 348 HOH D O   1 
HETATM 6604 O  O   . HOH U 5 .   ? 9.528   29.916  46.587  1.00 16.93 ? 349 HOH D O   1 
HETATM 6605 O  O   . HOH U 5 .   ? 0.092   48.646  19.421  1.00 31.23 ? 350 HOH D O   1 
HETATM 6606 O  O   . HOH U 5 .   ? 17.844  21.056  44.085  1.00 32.15 ? 351 HOH D O   1 
HETATM 6607 O  O   . HOH U 5 .   ? 17.956  24.978  48.178  1.00 29.39 ? 352 HOH D O   1 
HETATM 6608 O  O   . HOH U 5 .   ? 8.330   57.262  40.835  1.00 31.05 ? 353 HOH D O   1 
HETATM 6609 O  O   . HOH U 5 .   ? 22.455  47.368  39.092  1.00 23.90 ? 354 HOH D O   1 
HETATM 6610 O  O   . HOH U 5 .   ? 11.169  44.464  32.967  1.00 14.80 ? 355 HOH D O   1 
HETATM 6611 O  O   . HOH U 5 .   ? 1.521   30.879  30.399  1.00 16.24 ? 356 HOH D O   1 
HETATM 6612 O  O   . HOH U 5 .   ? 10.664  53.710  26.223  1.00 28.59 ? 357 HOH D O   1 
HETATM 6613 O  O   . HOH U 5 .   ? -0.285  20.821  39.594  1.00 26.77 ? 358 HOH D O   1 
HETATM 6614 O  O   . HOH U 5 .   ? 9.379   28.329  24.865  1.00 33.63 ? 359 HOH D O   1 
HETATM 6615 O  O   . HOH U 5 .   ? 3.699   44.105  24.334  1.00 20.42 ? 360 HOH D O   1 
HETATM 6616 O  O   . HOH U 5 .   ? 15.463  44.128  50.784  1.00 34.44 ? 361 HOH D O   1 
HETATM 6617 O  O   . HOH U 5 .   ? 17.530  50.443  35.613  1.00 19.87 ? 362 HOH D O   1 
HETATM 6618 O  O   . HOH U 5 .   ? -4.106  33.537  46.204  1.00 16.77 ? 363 HOH D O   1 
HETATM 6619 O  O   . HOH U 5 .   ? 19.300  46.882  34.122  1.00 23.33 ? 364 HOH D O   1 
HETATM 6620 O  O   . HOH U 5 .   ? 7.563   55.342  29.478  1.00 28.63 ? 365 HOH D O   1 
HETATM 6621 O  O   . HOH U 5 .   ? 11.605  49.180  24.833  1.00 28.96 ? 366 HOH D O   1 
HETATM 6622 O  O   . HOH U 5 .   ? -3.257  36.892  46.732  1.00 28.73 ? 367 HOH D O   1 
HETATM 6623 O  O   . HOH U 5 .   ? 5.678   32.641  26.282  1.00 36.13 ? 368 HOH D O   1 
HETATM 6624 O  O   . HOH U 5 .   ? -1.766  44.361  45.160  1.00 22.44 ? 369 HOH D O   1 
HETATM 6625 O  O   . HOH U 5 .   ? -8.577  39.704  22.176  1.00 35.60 ? 370 HOH D O   1 
HETATM 6626 O  O   . HOH U 5 .   ? 25.870  40.337  43.010  1.00 28.79 ? 371 HOH D O   1 
HETATM 6627 O  O   . HOH U 5 .   ? 16.296  32.450  21.329  1.00 36.90 ? 372 HOH D O   1 
HETATM 6628 O  O   . HOH U 5 .   ? 5.492   56.157  38.069  1.00 26.46 ? 373 HOH D O   1 
HETATM 6629 O  O   . HOH U 5 .   ? -2.471  26.163  37.286  1.00 25.23 ? 374 HOH D O   1 
HETATM 6630 O  O   . HOH U 5 .   ? 14.774  28.201  53.958  1.00 33.10 ? 375 HOH D O   1 
HETATM 6631 O  O   . HOH U 5 .   ? 15.810  52.277  31.782  1.00 33.21 ? 376 HOH D O   1 
HETATM 6632 O  O   . HOH U 5 .   ? 13.332  46.793  50.496  1.00 32.09 ? 377 HOH D O   1 
HETATM 6633 O  O   . HOH U 5 .   ? -8.273  35.496  34.520  1.00 33.33 ? 378 HOH D O   1 
HETATM 6634 O  O   . HOH U 5 .   ? 27.467  35.926  29.607  1.00 28.14 ? 379 HOH D O   1 
HETATM 6635 O  O   . HOH U 5 .   ? 24.870  30.910  31.853  1.00 31.87 ? 380 HOH D O   1 
HETATM 6636 O  O   . HOH U 5 .   ? 21.027  47.512  32.127  1.00 26.46 ? 381 HOH D O   1 
HETATM 6637 O  O   . HOH U 5 .   ? -8.535  41.029  33.796  1.00 25.25 ? 382 HOH D O   1 
HETATM 6638 O  O   . HOH U 5 .   ? 9.362   40.775  21.288  1.00 35.53 ? 383 HOH D O   1 
HETATM 6639 O  O   . HOH U 5 .   ? 13.768  20.222  22.898  1.00 27.27 ? 384 HOH D O   1 
HETATM 6640 O  O   . HOH U 5 .   ? 25.999  27.185  34.288  1.00 37.07 ? 385 HOH D O   1 
HETATM 6641 O  O   . HOH U 5 .   ? 15.933  54.598  35.493  1.00 17.06 ? 386 HOH D O   1 
HETATM 6642 O  O   . HOH U 5 .   ? 17.435  21.697  28.335  1.00 28.88 ? 387 HOH D O   1 
HETATM 6643 O  O   . HOH U 5 .   ? -2.198  33.695  24.808  1.00 18.55 ? 388 HOH D O   1 
HETATM 6644 O  O   . HOH U 5 .   ? 16.323  34.434  50.372  1.00 19.44 ? 389 HOH D O   1 
HETATM 6645 O  O   . HOH U 5 .   ? 11.942  41.525  50.915  1.00 29.58 ? 390 HOH D O   1 
HETATM 6646 O  O   . HOH U 5 .   ? 4.772   47.421  50.067  1.00 24.94 ? 391 HOH D O   1 
HETATM 6647 O  O   . HOH U 5 .   ? -3.047  25.768  41.563  1.00 33.35 ? 392 HOH D O   1 
HETATM 6648 O  O   . HOH U 5 .   ? -7.432  43.990  29.721  1.00 33.71 ? 393 HOH D O   1 
HETATM 6649 O  O   . HOH U 5 .   ? -3.888  48.593  28.406  1.00 28.35 ? 394 HOH D O   1 
HETATM 6650 O  O   . HOH U 5 .   ? 14.282  48.981  45.799  1.00 21.39 ? 395 HOH D O   1 
HETATM 6651 O  O   . HOH U 5 .   ? 15.146  24.662  50.061  1.00 31.71 ? 396 HOH D O   1 
HETATM 6652 O  O   . HOH U 5 .   ? 14.834  20.864  48.186  1.00 35.67 ? 397 HOH D O   1 
HETATM 6653 O  O   . HOH U 5 .   ? -2.142  43.270  47.771  1.00 28.94 ? 398 HOH D O   1 
HETATM 6654 O  O   . HOH U 5 .   ? 4.271   23.194  44.578  1.00 18.48 ? 399 HOH D O   1 
HETATM 6655 O  O   . HOH U 5 .   ? 4.970   20.280  47.471  1.00 38.45 ? 400 HOH D O   1 
HETATM 6656 O  O   . HOH U 5 .   ? -1.322  24.360  39.663  1.00 26.45 ? 401 HOH D O   1 
HETATM 6657 O  O   . HOH U 5 .   ? -2.165  49.804  34.895  1.00 24.14 ? 402 HOH D O   1 
HETATM 6658 O  O   . HOH U 5 .   ? -5.872  32.421  30.813  1.00 25.50 ? 403 HOH D O   1 
HETATM 6659 O  O   . HOH U 5 .   ? 17.678  51.023  42.567  1.00 15.04 ? 404 HOH D O   1 
HETATM 6660 O  O   . HOH U 5 .   ? 6.960   36.771  35.117  1.00 19.75 ? 405 HOH D O   1 
HETATM 6661 O  O   . HOH U 5 .   ? 16.801  17.707  42.640  1.00 34.71 ? 406 HOH D O   1 
HETATM 6662 O  O   . HOH U 5 .   ? 0.620   49.319  48.904  1.00 31.24 ? 407 HOH D O   1 
HETATM 6663 O  O   . HOH U 5 .   ? 3.750   55.029  49.236  1.00 30.56 ? 408 HOH D O   1 
HETATM 6664 O  O   . HOH U 5 .   ? 12.079  57.080  39.012  1.00 27.77 ? 409 HOH D O   1 
HETATM 6665 O  O   . HOH U 5 .   ? 8.219   50.291  24.763  1.00 23.25 ? 410 HOH D O   1 
HETATM 6666 O  O   . HOH U 5 .   ? 16.430  26.844  24.884  1.00 35.78 ? 411 HOH D O   1 
HETATM 6667 O  O   . HOH U 5 .   ? 12.619  48.819  30.562  1.00 17.21 ? 412 HOH D O   1 
HETATM 6668 O  O   . HOH U 5 .   ? 13.855  45.994  23.669  1.00 37.93 ? 413 HOH D O   1 
HETATM 6669 O  O   . HOH U 5 .   ? -2.612  30.464  40.446  1.00 21.52 ? 414 HOH D O   1 
HETATM 6670 O  O   . HOH U 5 .   ? 6.413   22.653  37.551  1.00 25.39 ? 415 HOH D O   1 
HETATM 6671 O  O   . HOH U 5 .   ? 7.874   22.053  50.289  1.00 31.03 ? 416 HOH D O   1 
HETATM 6672 O  O   . HOH U 5 .   ? -4.388  28.820  32.866  1.00 30.14 ? 417 HOH D O   1 
HETATM 6673 O  O   . HOH U 5 .   ? 1.585   49.758  25.188  1.00 24.37 ? 418 HOH D O   1 
HETATM 6674 O  O   . HOH U 5 .   ? 4.812   55.901  28.863  1.00 31.19 ? 419 HOH D O   1 
HETATM 6675 O  O   . HOH U 5 .   ? 3.143   56.490  42.870  1.00 36.87 ? 420 HOH D O   1 
HETATM 6676 O  O   . HOH U 5 .   ? -4.746  46.257  37.325  1.00 31.14 ? 421 HOH D O   1 
HETATM 6677 O  O   . HOH U 5 .   ? 16.920  48.945  44.874  1.00 17.38 ? 422 HOH D O   1 
HETATM 6678 O  O   . HOH U 5 .   ? 13.686  54.601  31.959  1.00 24.54 ? 423 HOH D O   1 
HETATM 6679 O  O   . HOH U 5 .   ? 17.441  44.743  24.611  1.00 28.70 ? 424 HOH D O   1 
HETATM 6680 O  O   . HOH U 5 .   ? -1.194  25.290  30.789  1.00 25.84 ? 425 HOH D O   1 
HETATM 6681 O  O   . HOH U 5 .   ? 19.106  47.582  45.922  1.00 28.93 ? 426 HOH D O   1 
HETATM 6682 O  O   . HOH U 5 .   ? 3.735   23.628  36.780  1.00 22.07 ? 427 HOH D O   1 
HETATM 6683 O  O   . HOH U 5 .   ? 0.180   44.855  17.799  1.00 28.22 ? 428 HOH D O   1 
HETATM 6684 O  O   . HOH U 5 .   ? 14.465  56.880  35.815  1.00 21.54 ? 429 HOH D O   1 
HETATM 6685 O  O   . HOH U 5 .   ? -2.664  29.484  36.951  1.00 19.30 ? 430 HOH D O   1 
HETATM 6686 O  O   . HOH U 5 .   ? 5.941   19.986  34.407  1.00 37.73 ? 431 HOH D O   1 
HETATM 6687 O  O   . HOH U 5 .   ? -4.833  45.808  21.358  1.00 33.48 ? 432 HOH D O   1 
HETATM 6688 O  O   . HOH U 5 .   ? 2.867   22.052  33.706  1.00 37.31 ? 433 HOH D O   1 
HETATM 6689 O  O   . HOH U 5 .   ? 11.357  27.247  52.867  1.00 29.46 ? 434 HOH D O   1 
HETATM 6690 O  O   . HOH U 5 .   ? 8.345   57.353  38.536  1.00 36.97 ? 435 HOH D O   1 
HETATM 6691 O  O   . HOH U 5 .   ? 27.434  25.981  39.752  1.00 34.51 ? 436 HOH D O   1 
HETATM 6692 O  O   . HOH U 5 .   ? 20.460  22.318  30.761  1.00 30.18 ? 437 HOH D O   1 
HETATM 6693 O  O   . HOH U 5 .   ? 10.812  56.887  45.885  1.00 37.60 ? 438 HOH D O   1 
HETATM 6694 O  O   . HOH U 5 .   ? 2.554   40.211  19.132  1.00 30.87 ? 439 HOH D O   1 
HETATM 6695 O  O   . HOH U 5 .   ? 11.633  59.036  41.262  1.00 34.21 ? 440 HOH D O   1 
HETATM 6696 O  O   . HOH U 5 .   ? -3.433  22.912  45.767  1.00 35.43 ? 441 HOH D O   1 
HETATM 6697 O  O   . HOH U 5 .   ? 7.251   17.901  33.498  1.00 32.89 ? 442 HOH D O   1 
HETATM 6698 O  O   . HOH U 5 .   ? 15.344  51.909  43.757  1.00 30.46 ? 443 HOH D O   1 
HETATM 6699 O  O   . HOH U 5 .   ? 5.353   35.856  27.761  1.00 34.81 ? 444 HOH D O   1 
HETATM 6700 O  O   . HOH U 5 .   ? 2.615   53.542  23.283  1.00 33.49 ? 445 HOH D O   1 
HETATM 6701 O  O   . HOH U 5 .   ? 11.205  50.409  50.779  1.00 37.80 ? 446 HOH D O   1 
HETATM 6702 O  O   . HOH U 5 .   ? 1.836   47.883  50.980  1.00 35.06 ? 447 HOH D O   1 
HETATM 6703 O  O   . HOH U 5 .   ? -6.099  53.606  29.362  1.00 44.53 ? 448 HOH D O   1 
HETATM 6704 O  O   . HOH U 5 .   ? 9.932   55.925  50.152  1.00 36.82 ? 449 HOH D O   1 
HETATM 6705 O  O   . HOH U 5 .   ? 4.394   50.868  19.095  1.00 35.32 ? 450 HOH D O   1 
HETATM 6706 O  O   . HOH U 5 .   ? -8.748  40.432  29.860  1.00 34.12 ? 451 HOH D O   1 
HETATM 6707 O  O   . HOH U 5 .   ? -1.160  46.540  17.633  1.00 33.54 ? 452 HOH D O   1 
HETATM 6708 O  O   . HOH U 5 .   ? 13.673  51.257  29.893  1.00 23.20 ? 453 HOH D O   1 
HETATM 6709 O  O   . HOH U 5 .   ? 9.048   23.557  52.288  1.00 37.01 ? 454 HOH D O   1 
HETATM 6710 O  O   . HOH U 5 .   ? 15.449  52.975  46.911  1.00 37.49 ? 455 HOH D O   1 
HETATM 6711 O  O   . HOH U 5 .   ? 11.210  39.630  22.825  1.00 36.45 ? 456 HOH D O   1 
HETATM 6712 O  O   . HOH U 5 .   ? 2.796   21.956  46.907  1.00 37.31 ? 457 HOH D O   1 
HETATM 6713 O  O   . HOH U 5 .   ? 10.700  17.587  31.142  1.00 32.96 ? 458 HOH D O   1 
HETATM 6714 O  O   . HOH U 5 .   ? -4.430  40.673  48.566  1.00 31.59 ? 459 HOH D O   1 
HETATM 6715 O  O   . HOH U 5 .   ? 16.892  47.844  32.818  1.00 30.66 ? 460 HOH D O   1 
HETATM 6716 O  O   . HOH U 5 .   ? 10.584  51.616  24.146  1.00 32.80 ? 461 HOH D O   1 
HETATM 6717 O  O   . HOH U 5 .   ? 6.064   15.407  39.377  1.00 33.01 ? 462 HOH D O   1 
HETATM 6718 O  O   . HOH U 5 .   ? 9.191   24.658  22.477  1.00 36.98 ? 463 HOH D O   1 
HETATM 6719 O  O   . HOH U 5 .   ? 6.360   49.455  18.599  1.00 36.05 ? 464 HOH D O   1 
HETATM 6720 O  O   . HOH U 5 .   ? -4.265  30.820  42.609  1.00 26.13 ? 465 HOH D O   1 
HETATM 6721 O  O   . HOH U 5 .   ? 9.984   37.160  55.411  1.00 40.06 ? 466 HOH D O   1 
HETATM 6722 O  O   . HOH U 5 .   ? -1.716  24.588  34.246  1.00 37.00 ? 467 HOH D O   1 
HETATM 6723 O  O   . HOH U 5 .   ? 23.598  44.496  46.956  1.00 35.73 ? 468 HOH D O   1 
HETATM 6724 O  O   . HOH U 5 .   ? 9.162   37.856  33.592  1.00 26.35 ? 469 HOH D O   1 
HETATM 6725 O  O   . HOH U 5 .   ? 23.984  43.547  49.281  1.00 41.49 ? 470 HOH D O   1 
# 
