data_8Y00
# 
_entry.id   8Y00 
# 
_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   8Y00         pdb_00008y00 10.2210/pdb8y00/pdb 
WWPDB D_1300044547 ?            ?                   
# 
_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                        8Y00 
_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 ? 'The GenBank ID is MZ569606.1' 
2 branched    syn 'beta-D-xylopyranose-(1-4)-beta-D-xylopyranose'                           282.245   2   ?       ? ? ? 
3 branched    syn 'beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose' 414.360   2   ?       ? ? ? 
4 non-polymer syn 'ZINC ION'                                                                65.409    6   ?       ? ? ? 
5 non-polymer syn beta-D-xylopyranose                                                       150.130   2   ?       ? ? ? 
6 water       nat water                                                                     18.015    700 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        xylotriose 
# 
_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 
4 'ZINC ION'          ZN  
5 beta-D-xylopyranose XYP 
6 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                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 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   ?     
4 3 DXylpb1-4DXylpb1-4DXylpb1-ROH                          'Glycam Condensed Sequence' GMML       1.0   
5 3 'WURCS=2.0/1,3,2/[a212h-1b_1-5]/1-1-1/a4-b1_b4-c1'     WURCS                       PDB2Glycan 1.1.0 
6 3 '[][b-D-Xylp]{[(4+1)][b-D-Xylp]{[(4+1)][b-D-Xylp]{}}}' LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 XYP C1 O1 1 XYP O4 HO4 sing ? 
2 3 2 XYP C1 O1 1 XYP O4 HO4 sing ? 
3 3 3 XYP C1 O1 2 XYP O4 HO4 sing ? 
# 
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  -7  GLY GLY 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   ?   ?   ?   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   ?   ?   ?   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 3  n 
F 3 XYP 1 F XYP 1 E XYP 6  n 
F 3 XYP 2 F XYP 2 E XYP 5  n 
F 3 XYP 3 F XYP 3 E XYP 4  n 
G 3 XYP 1 G XYP 1 E XYP 9  n 
G 3 XYP 2 G XYP 2 E XYP 8  n 
G 3 XYP 3 G XYP 3 E XYP 7  n 
H 2 XYP 1 H XYP 1 E XYP 11 n 
H 2 XYP 2 H XYP 2 E XYP 12 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 
I 4 ZN  1   201 300 ZN  ZN  A . 
J 4 ZN  1   202 301 ZN  ZN  A . 
K 5 XYP 1   203 1   XYP XYP A . 
L 4 ZN  1   300 300 ZN  ZN  B . 
M 4 ZN  1   301 301 ZN  ZN  B . 
N 4 ZN  1   300 300 ZN  ZN  C . 
O 4 ZN  1   301 301 ZN  ZN  C . 
P 5 XYP 1   201 10  XYP XYP D . 
Q 6 HOH 1   301 348 HOH HOH A . 
Q 6 HOH 2   302 581 HOH HOH A . 
Q 6 HOH 3   303 656 HOH HOH A . 
Q 6 HOH 4   304 616 HOH HOH A . 
Q 6 HOH 5   305 683 HOH HOH A . 
Q 6 HOH 6   306 345 HOH HOH A . 
Q 6 HOH 7   307 537 HOH HOH A . 
Q 6 HOH 8   308 178 HOH HOH A . 
Q 6 HOH 9   309 127 HOH HOH A . 
Q 6 HOH 10  310 373 HOH HOH A . 
Q 6 HOH 11  311 148 HOH HOH A . 
Q 6 HOH 12  312 52  HOH HOH A . 
Q 6 HOH 13  313 307 HOH HOH A . 
Q 6 HOH 14  314 646 HOH HOH A . 
Q 6 HOH 15  315 438 HOH HOH A . 
Q 6 HOH 16  316 446 HOH HOH A . 
Q 6 HOH 17  317 287 HOH HOH A . 
Q 6 HOH 18  318 476 HOH HOH A . 
Q 6 HOH 19  319 6   HOH HOH A . 
Q 6 HOH 20  320 282 HOH HOH A . 
Q 6 HOH 21  321 209 HOH HOH A . 
Q 6 HOH 22  322 328 HOH HOH A . 
Q 6 HOH 23  323 562 HOH HOH A . 
Q 6 HOH 24  324 275 HOH HOH A . 
Q 6 HOH 25  325 448 HOH HOH A . 
Q 6 HOH 26  326 116 HOH HOH A . 
Q 6 HOH 27  327 223 HOH HOH A . 
Q 6 HOH 28  328 79  HOH HOH A . 
Q 6 HOH 29  329 608 HOH HOH A . 
Q 6 HOH 30  330 707 HOH HOH A . 
Q 6 HOH 31  331 254 HOH HOH A . 
Q 6 HOH 32  332 50  HOH HOH A . 
Q 6 HOH 33  333 666 HOH HOH A . 
Q 6 HOH 34  334 119 HOH HOH A . 
Q 6 HOH 35  335 349 HOH HOH A . 
Q 6 HOH 36  336 49  HOH HOH A . 
Q 6 HOH 37  337 318 HOH HOH A . 
Q 6 HOH 38  338 95  HOH HOH A . 
Q 6 HOH 39  339 229 HOH HOH A . 
Q 6 HOH 40  340 149 HOH HOH A . 
Q 6 HOH 41  341 201 HOH HOH A . 
Q 6 HOH 42  342 145 HOH HOH A . 
Q 6 HOH 43  343 146 HOH HOH A . 
Q 6 HOH 44  344 375 HOH HOH A . 
Q 6 HOH 45  345 304 HOH HOH A . 
Q 6 HOH 46  346 474 HOH HOH A . 
Q 6 HOH 47  347 162 HOH HOH A . 
Q 6 HOH 48  348 268 HOH HOH A . 
Q 6 HOH 49  349 8   HOH HOH A . 
Q 6 HOH 50  350 216 HOH HOH A . 
Q 6 HOH 51  351 341 HOH HOH A . 
Q 6 HOH 52  352 245 HOH HOH A . 
Q 6 HOH 53  353 504 HOH HOH A . 
Q 6 HOH 54  354 46  HOH HOH A . 
Q 6 HOH 55  355 171 HOH HOH A . 
Q 6 HOH 56  356 121 HOH HOH A . 
Q 6 HOH 57  357 239 HOH HOH A . 
Q 6 HOH 58  358 2   HOH HOH A . 
Q 6 HOH 59  359 542 HOH HOH A . 
Q 6 HOH 60  360 233 HOH HOH A . 
Q 6 HOH 61  361 107 HOH HOH A . 
Q 6 HOH 62  362 189 HOH HOH A . 
Q 6 HOH 63  363 465 HOH HOH A . 
Q 6 HOH 64  364 20  HOH HOH A . 
Q 6 HOH 65  365 473 HOH HOH A . 
Q 6 HOH 66  366 202 HOH HOH A . 
Q 6 HOH 67  367 23  HOH HOH A . 
Q 6 HOH 68  368 263 HOH HOH A . 
Q 6 HOH 69  369 495 HOH HOH A . 
Q 6 HOH 70  370 155 HOH HOH A . 
Q 6 HOH 71  371 196 HOH HOH A . 
Q 6 HOH 72  372 65  HOH HOH A . 
Q 6 HOH 73  373 40  HOH HOH A . 
Q 6 HOH 74  374 59  HOH HOH A . 
Q 6 HOH 75  375 525 HOH HOH A . 
Q 6 HOH 76  376 238 HOH HOH A . 
Q 6 HOH 77  377 160 HOH HOH A . 
Q 6 HOH 78  378 154 HOH HOH A . 
Q 6 HOH 79  379 180 HOH HOH A . 
Q 6 HOH 80  380 701 HOH HOH A . 
Q 6 HOH 81  381 306 HOH HOH A . 
Q 6 HOH 82  382 94  HOH HOH A . 
Q 6 HOH 83  383 408 HOH HOH A . 
Q 6 HOH 84  384 607 HOH HOH A . 
Q 6 HOH 85  385 450 HOH HOH A . 
Q 6 HOH 86  386 647 HOH HOH A . 
Q 6 HOH 87  387 136 HOH HOH A . 
Q 6 HOH 88  388 80  HOH HOH A . 
Q 6 HOH 89  389 342 HOH HOH A . 
Q 6 HOH 90  390 132 HOH HOH A . 
Q 6 HOH 91  391 115 HOH HOH A . 
Q 6 HOH 92  392 334 HOH HOH A . 
Q 6 HOH 93  393 361 HOH HOH A . 
Q 6 HOH 94  394 190 HOH HOH A . 
Q 6 HOH 95  395 385 HOH HOH A . 
Q 6 HOH 96  396 198 HOH HOH A . 
Q 6 HOH 97  397 441 HOH HOH A . 
Q 6 HOH 98  398 234 HOH HOH A . 
Q 6 HOH 99  399 601 HOH HOH A . 
Q 6 HOH 100 400 67  HOH HOH A . 
Q 6 HOH 101 401 203 HOH HOH A . 
Q 6 HOH 102 402 488 HOH HOH A . 
Q 6 HOH 103 403 105 HOH HOH A . 
Q 6 HOH 104 404 133 HOH HOH A . 
Q 6 HOH 105 405 331 HOH HOH A . 
Q 6 HOH 106 406 501 HOH HOH A . 
Q 6 HOH 107 407 45  HOH HOH A . 
Q 6 HOH 108 408 464 HOH HOH A . 
Q 6 HOH 109 409 164 HOH HOH A . 
Q 6 HOH 110 410 456 HOH HOH A . 
Q 6 HOH 111 411 483 HOH HOH A . 
Q 6 HOH 112 412 680 HOH HOH A . 
Q 6 HOH 113 413 82  HOH HOH A . 
Q 6 HOH 114 414 528 HOH HOH A . 
Q 6 HOH 115 415 195 HOH HOH A . 
Q 6 HOH 116 416 62  HOH HOH A . 
Q 6 HOH 117 417 61  HOH HOH A . 
Q 6 HOH 118 418 66  HOH HOH A . 
Q 6 HOH 119 419 500 HOH HOH A . 
Q 6 HOH 120 420 359 HOH HOH A . 
Q 6 HOH 121 421 130 HOH HOH A . 
Q 6 HOH 122 422 329 HOH HOH A . 
Q 6 HOH 123 423 682 HOH HOH A . 
Q 6 HOH 124 424 141 HOH HOH A . 
Q 6 HOH 125 425 602 HOH HOH A . 
Q 6 HOH 126 426 200 HOH HOH A . 
Q 6 HOH 127 427 708 HOH HOH A . 
Q 6 HOH 128 428 103 HOH HOH A . 
Q 6 HOH 129 429 619 HOH HOH A . 
Q 6 HOH 130 430 140 HOH HOH A . 
Q 6 HOH 131 431 39  HOH HOH A . 
Q 6 HOH 132 432 526 HOH HOH A . 
Q 6 HOH 133 433 603 HOH HOH A . 
Q 6 HOH 134 434 629 HOH HOH A . 
Q 6 HOH 135 435 19  HOH HOH A . 
Q 6 HOH 136 436 231 HOH HOH A . 
Q 6 HOH 137 437 22  HOH HOH A . 
Q 6 HOH 138 438 527 HOH HOH A . 
Q 6 HOH 139 439 551 HOH HOH A . 
Q 6 HOH 140 440 695 HOH HOH A . 
Q 6 HOH 141 441 458 HOH HOH A . 
Q 6 HOH 142 442 186 HOH HOH A . 
Q 6 HOH 143 443 516 HOH HOH A . 
Q 6 HOH 144 444 481 HOH HOH A . 
Q 6 HOH 145 445 709 HOH HOH A . 
Q 6 HOH 146 446 649 HOH HOH A . 
Q 6 HOH 147 447 365 HOH HOH A . 
Q 6 HOH 148 448 210 HOH HOH A . 
Q 6 HOH 149 449 605 HOH HOH A . 
Q 6 HOH 150 450 518 HOH HOH A . 
Q 6 HOH 151 451 291 HOH HOH A . 
Q 6 HOH 152 452 246 HOH HOH A . 
Q 6 HOH 153 453 299 HOH HOH A . 
Q 6 HOH 154 454 610 HOH HOH A . 
Q 6 HOH 155 455 648 HOH HOH A . 
Q 6 HOH 156 456 400 HOH HOH A . 
Q 6 HOH 157 457 622 HOH HOH A . 
Q 6 HOH 158 458 655 HOH HOH A . 
Q 6 HOH 159 459 570 HOH HOH A . 
Q 6 HOH 160 460 424 HOH HOH A . 
Q 6 HOH 161 461 506 HOH HOH A . 
Q 6 HOH 162 462 78  HOH HOH A . 
Q 6 HOH 163 463 524 HOH HOH A . 
Q 6 HOH 164 464 691 HOH HOH A . 
Q 6 HOH 165 465 493 HOH HOH A . 
Q 6 HOH 166 466 414 HOH HOH A . 
Q 6 HOH 167 467 60  HOH HOH A . 
Q 6 HOH 168 468 372 HOH HOH A . 
Q 6 HOH 169 469 599 HOH HOH A . 
Q 6 HOH 170 470 420 HOH HOH A . 
Q 6 HOH 171 471 409 HOH HOH A . 
Q 6 HOH 172 472 265 HOH HOH A . 
Q 6 HOH 173 473 618 HOH HOH A . 
Q 6 HOH 174 474 512 HOH HOH A . 
Q 6 HOH 175 475 377 HOH HOH A . 
Q 6 HOH 176 476 93  HOH HOH A . 
Q 6 HOH 177 477 406 HOH HOH A . 
Q 6 HOH 178 478 117 HOH HOH A . 
Q 6 HOH 179 479 260 HOH HOH A . 
Q 6 HOH 180 480 215 HOH HOH A . 
Q 6 HOH 181 481 511 HOH HOH A . 
Q 6 HOH 182 482 410 HOH HOH A . 
Q 6 HOH 183 483 494 HOH HOH A . 
Q 6 HOH 184 484 705 HOH HOH A . 
Q 6 HOH 185 485 266 HOH HOH A . 
Q 6 HOH 186 486 514 HOH HOH A . 
Q 6 HOH 187 487 426 HOH HOH A . 
Q 6 HOH 188 488 425 HOH HOH A . 
Q 6 HOH 189 489 430 HOH HOH A . 
Q 6 HOH 190 490 565 HOH HOH A . 
Q 6 HOH 191 491 674 HOH HOH A . 
R 6 HOH 1   401 582 HOH HOH B . 
R 6 HOH 2   402 624 HOH HOH B . 
R 6 HOH 3   403 661 HOH HOH B . 
R 6 HOH 4   404 652 HOH HOH B . 
R 6 HOH 5   405 658 HOH HOH B . 
R 6 HOH 6   406 612 HOH HOH B . 
R 6 HOH 7   407 311 HOH HOH B . 
R 6 HOH 8   408 700 HOH HOH B . 
R 6 HOH 9   409 177 HOH HOH B . 
R 6 HOH 10  410 586 HOH HOH B . 
R 6 HOH 11  411 529 HOH HOH B . 
R 6 HOH 12  412 440 HOH HOH B . 
R 6 HOH 13  413 83  HOH HOH B . 
R 6 HOH 14  414 357 HOH HOH B . 
R 6 HOH 15  415 347 HOH HOH B . 
R 6 HOH 16  416 442 HOH HOH B . 
R 6 HOH 17  417 611 HOH HOH B . 
R 6 HOH 18  418 391 HOH HOH B . 
R 6 HOH 19  419 255 HOH HOH B . 
R 6 HOH 20  420 184 HOH HOH B . 
R 6 HOH 21  421 466 HOH HOH B . 
R 6 HOH 22  422 615 HOH HOH B . 
R 6 HOH 23  423 435 HOH HOH B . 
R 6 HOH 24  424 122 HOH HOH B . 
R 6 HOH 25  425 220 HOH HOH B . 
R 6 HOH 26  426 124 HOH HOH B . 
R 6 HOH 27  427 477 HOH HOH B . 
R 6 HOH 28  428 660 HOH HOH B . 
R 6 HOH 29  429 55  HOH HOH B . 
R 6 HOH 30  430 91  HOH HOH B . 
R 6 HOH 31  431 460 HOH HOH B . 
R 6 HOH 32  432 32  HOH HOH B . 
R 6 HOH 33  433 257 HOH HOH B . 
R 6 HOH 34  434 478 HOH HOH B . 
R 6 HOH 35  435 118 HOH HOH B . 
R 6 HOH 36  436 165 HOH HOH B . 
R 6 HOH 37  437 139 HOH HOH B . 
R 6 HOH 38  438 261 HOH HOH B . 
R 6 HOH 39  439 379 HOH HOH B . 
R 6 HOH 40  440 432 HOH HOH B . 
R 6 HOH 41  441 643 HOH HOH B . 
R 6 HOH 42  442 4   HOH HOH B . 
R 6 HOH 43  443 168 HOH HOH B . 
R 6 HOH 44  444 218 HOH HOH B . 
R 6 HOH 45  445 3   HOH HOH B . 
R 6 HOH 46  446 169 HOH HOH B . 
R 6 HOH 47  447 126 HOH HOH B . 
R 6 HOH 48  448 580 HOH HOH B . 
R 6 HOH 49  449 437 HOH HOH B . 
R 6 HOH 50  450 235 HOH HOH B . 
R 6 HOH 51  451 469 HOH HOH B . 
R 6 HOH 52  452 161 HOH HOH B . 
R 6 HOH 53  453 96  HOH HOH B . 
R 6 HOH 54  454 35  HOH HOH B . 
R 6 HOH 55  455 11  HOH HOH B . 
R 6 HOH 56  456 461 HOH HOH B . 
R 6 HOH 57  457 332 HOH HOH B . 
R 6 HOH 58  458 43  HOH HOH B . 
R 6 HOH 59  459 26  HOH HOH B . 
R 6 HOH 60  460 199 HOH HOH B . 
R 6 HOH 61  461 470 HOH HOH B . 
R 6 HOH 62  462 75  HOH HOH B . 
R 6 HOH 63  463 48  HOH HOH B . 
R 6 HOH 64  464 300 HOH HOH B . 
R 6 HOH 65  465 696 HOH HOH B . 
R 6 HOH 66  466 588 HOH HOH B . 
R 6 HOH 67  467 53  HOH HOH B . 
R 6 HOH 68  468 703 HOH HOH B . 
R 6 HOH 69  469 272 HOH HOH B . 
R 6 HOH 70  470 316 HOH HOH B . 
R 6 HOH 71  471 101 HOH HOH B . 
R 6 HOH 72  472 221 HOH HOH B . 
R 6 HOH 73  473 301 HOH HOH B . 
R 6 HOH 74  474 447 HOH HOH B . 
R 6 HOH 75  475 97  HOH HOH B . 
R 6 HOH 76  476 346 HOH HOH B . 
R 6 HOH 77  477 667 HOH HOH B . 
R 6 HOH 78  478 212 HOH HOH B . 
R 6 HOH 79  479 324 HOH HOH B . 
R 6 HOH 80  480 58  HOH HOH B . 
R 6 HOH 81  481 614 HOH HOH B . 
R 6 HOH 82  482 69  HOH HOH B . 
R 6 HOH 83  483 63  HOH HOH B . 
R 6 HOH 84  484 10  HOH HOH B . 
R 6 HOH 85  485 24  HOH HOH B . 
R 6 HOH 86  486 259 HOH HOH B . 
R 6 HOH 87  487 207 HOH HOH B . 
R 6 HOH 88  488 204 HOH HOH B . 
R 6 HOH 89  489 225 HOH HOH B . 
R 6 HOH 90  490 600 HOH HOH B . 
R 6 HOH 91  491 463 HOH HOH B . 
R 6 HOH 92  492 248 HOH HOH B . 
R 6 HOH 93  493 392 HOH HOH B . 
R 6 HOH 94  494 443 HOH HOH B . 
R 6 HOH 95  495 166 HOH HOH B . 
R 6 HOH 96  496 13  HOH HOH B . 
R 6 HOH 97  497 70  HOH HOH B . 
R 6 HOH 98  498 106 HOH HOH B . 
R 6 HOH 99  499 421 HOH HOH B . 
R 6 HOH 100 500 224 HOH HOH B . 
R 6 HOH 101 501 176 HOH HOH B . 
R 6 HOH 102 502 561 HOH HOH B . 
R 6 HOH 103 503 380 HOH HOH B . 
R 6 HOH 104 504 137 HOH HOH B . 
R 6 HOH 105 505 174 HOH HOH B . 
R 6 HOH 106 506 104 HOH HOH B . 
R 6 HOH 107 507 490 HOH HOH B . 
R 6 HOH 108 508 64  HOH HOH B . 
R 6 HOH 109 509 34  HOH HOH B . 
R 6 HOH 110 510 393 HOH HOH B . 
R 6 HOH 111 511 445 HOH HOH B . 
R 6 HOH 112 512 147 HOH HOH B . 
R 6 HOH 113 513 175 HOH HOH B . 
R 6 HOH 114 514 283 HOH HOH B . 
R 6 HOH 115 515 153 HOH HOH B . 
R 6 HOH 116 516 81  HOH HOH B . 
R 6 HOH 117 517 47  HOH HOH B . 
R 6 HOH 118 518 314 HOH HOH B . 
R 6 HOH 119 519 241 HOH HOH B . 
R 6 HOH 120 520 269 HOH HOH B . 
R 6 HOH 121 521 151 HOH HOH B . 
R 6 HOH 122 522 574 HOH HOH B . 
R 6 HOH 123 523 288 HOH HOH B . 
R 6 HOH 124 524 270 HOH HOH B . 
R 6 HOH 125 525 556 HOH HOH B . 
R 6 HOH 126 526 519 HOH HOH B . 
R 6 HOH 127 527 626 HOH HOH B . 
R 6 HOH 128 528 563 HOH HOH B . 
R 6 HOH 129 529 659 HOH HOH B . 
R 6 HOH 130 530 487 HOH HOH B . 
R 6 HOH 131 531 355 HOH HOH B . 
R 6 HOH 132 532 135 HOH HOH B . 
R 6 HOH 133 533 427 HOH HOH B . 
R 6 HOH 134 534 353 HOH HOH B . 
R 6 HOH 135 535 57  HOH HOH B . 
R 6 HOH 136 536 376 HOH HOH B . 
R 6 HOH 137 537 557 HOH HOH B . 
R 6 HOH 138 538 625 HOH HOH B . 
R 6 HOH 139 539 125 HOH HOH B . 
R 6 HOH 140 540 172 HOH HOH B . 
R 6 HOH 141 541 595 HOH HOH B . 
R 6 HOH 142 542 457 HOH HOH B . 
R 6 HOH 143 543 604 HOH HOH B . 
R 6 HOH 144 544 25  HOH HOH B . 
R 6 HOH 145 545 585 HOH HOH B . 
R 6 HOH 146 546 710 HOH HOH B . 
R 6 HOH 147 547 322 HOH HOH B . 
R 6 HOH 148 548 279 HOH HOH B . 
R 6 HOH 149 549 664 HOH HOH B . 
R 6 HOH 150 550 498 HOH HOH B . 
R 6 HOH 151 551 668 HOH HOH B . 
R 6 HOH 152 552 657 HOH HOH B . 
R 6 HOH 153 553 428 HOH HOH B . 
R 6 HOH 154 554 403 HOH HOH B . 
R 6 HOH 155 555 575 HOH HOH B . 
R 6 HOH 156 556 471 HOH HOH B . 
R 6 HOH 157 557 539 HOH HOH B . 
R 6 HOH 158 558 553 HOH HOH B . 
R 6 HOH 159 559 549 HOH HOH B . 
R 6 HOH 160 560 503 HOH HOH B . 
R 6 HOH 161 561 407 HOH HOH B . 
R 6 HOH 162 562 418 HOH HOH B . 
R 6 HOH 163 563 381 HOH HOH B . 
R 6 HOH 164 564 564 HOH HOH B . 
R 6 HOH 165 565 258 HOH HOH B . 
R 6 HOH 166 566 613 HOH HOH B . 
R 6 HOH 167 567 587 HOH HOH B . 
R 6 HOH 168 568 513 HOH HOH B . 
R 6 HOH 169 569 567 HOH HOH B . 
R 6 HOH 170 570 697 HOH HOH B . 
R 6 HOH 171 571 515 HOH HOH B . 
R 6 HOH 172 572 681 HOH HOH B . 
R 6 HOH 173 573 583 HOH HOH B . 
R 6 HOH 174 574 310 HOH HOH B . 
R 6 HOH 175 575 692 HOH HOH B . 
R 6 HOH 176 576 262 HOH HOH B . 
R 6 HOH 177 577 627 HOH HOH B . 
R 6 HOH 178 578 350 HOH HOH B . 
R 6 HOH 179 579 247 HOH HOH B . 
R 6 HOH 180 580 584 HOH HOH B . 
R 6 HOH 181 581 193 HOH HOH B . 
R 6 HOH 182 582 558 HOH HOH B . 
R 6 HOH 183 583 521 HOH HOH B . 
R 6 HOH 184 584 569 HOH HOH B . 
R 6 HOH 185 585 227 HOH HOH B . 
R 6 HOH 186 586 398 HOH HOH B . 
R 6 HOH 187 587 315 HOH HOH B . 
R 6 HOH 188 588 423 HOH HOH B . 
R 6 HOH 189 589 289 HOH HOH B . 
R 6 HOH 190 590 662 HOH HOH B . 
R 6 HOH 191 591 336 HOH HOH B . 
R 6 HOH 192 592 554 HOH HOH B . 
R 6 HOH 193 593 571 HOH HOH B . 
R 6 HOH 194 594 566 HOH HOH B . 
R 6 HOH 195 595 706 HOH HOH B . 
S 6 HOH 1   401 636 HOH HOH C . 
S 6 HOH 2   402 589 HOH HOH C . 
S 6 HOH 3   403 312 HOH HOH C . 
S 6 HOH 4   404 37  HOH HOH C . 
S 6 HOH 5   405 638 HOH HOH C . 
S 6 HOH 6   406 156 HOH HOH C . 
S 6 HOH 7   407 628 HOH HOH C . 
S 6 HOH 8   408 15  HOH HOH C . 
S 6 HOH 9   409 475 HOH HOH C . 
S 6 HOH 10  410 340 HOH HOH C . 
S 6 HOH 11  411 635 HOH HOH C . 
S 6 HOH 12  412 633 HOH HOH C . 
S 6 HOH 13  413 482 HOH HOH C . 
S 6 HOH 14  414 21  HOH HOH C . 
S 6 HOH 15  415 690 HOH HOH C . 
S 6 HOH 16  416 675 HOH HOH C . 
S 6 HOH 17  417 323 HOH HOH C . 
S 6 HOH 18  418 645 HOH HOH C . 
S 6 HOH 19  419 321 HOH HOH C . 
S 6 HOH 20  420 454 HOH HOH C . 
S 6 HOH 21  421 71  HOH HOH C . 
S 6 HOH 22  422 541 HOH HOH C . 
S 6 HOH 23  423 534 HOH HOH C . 
S 6 HOH 24  424 308 HOH HOH C . 
S 6 HOH 25  425 327 HOH HOH C . 
S 6 HOH 26  426 313 HOH HOH C . 
S 6 HOH 27  427 144 HOH HOH C . 
S 6 HOH 28  428 351 HOH HOH C . 
S 6 HOH 29  429 284 HOH HOH C . 
S 6 HOH 30  430 544 HOH HOH C . 
S 6 HOH 31  431 77  HOH HOH C . 
S 6 HOH 32  432 390 HOH HOH C . 
S 6 HOH 33  433 548 HOH HOH C . 
S 6 HOH 34  434 598 HOH HOH C . 
S 6 HOH 35  435 676 HOH HOH C . 
S 6 HOH 36  436 597 HOH HOH C . 
S 6 HOH 37  437 290 HOH HOH C . 
S 6 HOH 38  438 688 HOH HOH C . 
S 6 HOH 39  439 244 HOH HOH C . 
S 6 HOH 40  440 54  HOH HOH C . 
S 6 HOH 41  441 277 HOH HOH C . 
S 6 HOH 42  442 496 HOH HOH C . 
S 6 HOH 43  443 90  HOH HOH C . 
S 6 HOH 44  444 36  HOH HOH C . 
S 6 HOH 45  445 228 HOH HOH C . 
S 6 HOH 46  446 12  HOH HOH C . 
S 6 HOH 47  447 128 HOH HOH C . 
S 6 HOH 48  448 468 HOH HOH C . 
S 6 HOH 49  449 185 HOH HOH C . 
S 6 HOH 50  450 9   HOH HOH C . 
S 6 HOH 51  451 100 HOH HOH C . 
S 6 HOH 52  452 28  HOH HOH C . 
S 6 HOH 53  453 208 HOH HOH C . 
S 6 HOH 54  454 173 HOH HOH C . 
S 6 HOH 55  455 594 HOH HOH C . 
S 6 HOH 56  456 302 HOH HOH C . 
S 6 HOH 57  457 371 HOH HOH C . 
S 6 HOH 58  458 123 HOH HOH C . 
S 6 HOH 59  459 205 HOH HOH C . 
S 6 HOH 60  460 253 HOH HOH C . 
S 6 HOH 61  461 436 HOH HOH C . 
S 6 HOH 62  462 596 HOH HOH C . 
S 6 HOH 63  463 480 HOH HOH C . 
S 6 HOH 64  464 280 HOH HOH C . 
S 6 HOH 65  465 382 HOH HOH C . 
S 6 HOH 66  466 264 HOH HOH C . 
S 6 HOH 67  467 296 HOH HOH C . 
S 6 HOH 68  468 540 HOH HOH C . 
S 6 HOH 69  469 591 HOH HOH C . 
S 6 HOH 70  470 206 HOH HOH C . 
S 6 HOH 71  471 276 HOH HOH C . 
S 6 HOH 72  472 157 HOH HOH C . 
S 6 HOH 73  473 394 HOH HOH C . 
S 6 HOH 74  474 389 HOH HOH C . 
S 6 HOH 75  475 325 HOH HOH C . 
S 6 HOH 76  476 250 HOH HOH C . 
S 6 HOH 77  477 243 HOH HOH C . 
S 6 HOH 78  478 374 HOH HOH C . 
S 6 HOH 79  479 182 HOH HOH C . 
S 6 HOH 80  480 38  HOH HOH C . 
S 6 HOH 81  481 5   HOH HOH C . 
S 6 HOH 82  482 360 HOH HOH C . 
S 6 HOH 83  483 89  HOH HOH C . 
S 6 HOH 84  484 572 HOH HOH C . 
S 6 HOH 85  485 396 HOH HOH C . 
S 6 HOH 86  486 72  HOH HOH C . 
S 6 HOH 87  487 295 HOH HOH C . 
S 6 HOH 88  488 491 HOH HOH C . 
S 6 HOH 89  489 358 HOH HOH C . 
S 6 HOH 90  490 383 HOH HOH C . 
S 6 HOH 91  491 363 HOH HOH C . 
S 6 HOH 92  492 134 HOH HOH C . 
S 6 HOH 93  493 434 HOH HOH C . 
S 6 HOH 94  494 592 HOH HOH C . 
S 6 HOH 95  495 634 HOH HOH C . 
S 6 HOH 96  496 143 HOH HOH C . 
S 6 HOH 97  497 188 HOH HOH C . 
S 6 HOH 98  498 546 HOH HOH C . 
S 6 HOH 99  499 102 HOH HOH C . 
S 6 HOH 100 500 179 HOH HOH C . 
S 6 HOH 101 501 7   HOH HOH C . 
S 6 HOH 102 502 545 HOH HOH C . 
S 6 HOH 103 503 214 HOH HOH C . 
S 6 HOH 104 504 367 HOH HOH C . 
S 6 HOH 105 505 191 HOH HOH C . 
S 6 HOH 106 506 333 HOH HOH C . 
S 6 HOH 107 507 114 HOH HOH C . 
S 6 HOH 108 508 479 HOH HOH C . 
S 6 HOH 109 509 99  HOH HOH C . 
S 6 HOH 110 510 459 HOH HOH C . 
S 6 HOH 111 511 131 HOH HOH C . 
S 6 HOH 112 512 192 HOH HOH C . 
S 6 HOH 113 513 387 HOH HOH C . 
S 6 HOH 114 514 278 HOH HOH C . 
S 6 HOH 115 515 685 HOH HOH C . 
S 6 HOH 116 516 281 HOH HOH C . 
S 6 HOH 117 517 319 HOH HOH C . 
S 6 HOH 118 518 462 HOH HOH C . 
S 6 HOH 119 519 593 HOH HOH C . 
S 6 HOH 120 520 606 HOH HOH C . 
S 6 HOH 121 521 41  HOH HOH C . 
S 6 HOH 122 522 522 HOH HOH C . 
S 6 HOH 123 523 309 HOH HOH C . 
S 6 HOH 124 524 560 HOH HOH C . 
S 6 HOH 125 525 401 HOH HOH C . 
S 6 HOH 126 526 343 HOH HOH C . 
S 6 HOH 127 527 415 HOH HOH C . 
S 6 HOH 128 528 236 HOH HOH C . 
S 6 HOH 129 529 404 HOH HOH C . 
S 6 HOH 130 530 620 HOH HOH C . 
S 6 HOH 131 531 665 HOH HOH C . 
S 6 HOH 132 532 484 HOH HOH C . 
S 6 HOH 133 533 671 HOH HOH C . 
S 6 HOH 134 534 237 HOH HOH C . 
S 6 HOH 135 535 486 HOH HOH C . 
S 6 HOH 136 536 405 HOH HOH C . 
S 6 HOH 137 537 654 HOH HOH C . 
S 6 HOH 138 538 568 HOH HOH C . 
S 6 HOH 139 539 413 HOH HOH C . 
S 6 HOH 140 540 698 HOH HOH C . 
S 6 HOH 141 541 402 HOH HOH C . 
S 6 HOH 142 542 669 HOH HOH C . 
S 6 HOH 143 543 219 HOH HOH C . 
S 6 HOH 144 544 256 HOH HOH C . 
S 6 HOH 145 545 578 HOH HOH C . 
S 6 HOH 146 546 252 HOH HOH C . 
S 6 HOH 147 547 111 HOH HOH C . 
S 6 HOH 148 548 416 HOH HOH C . 
S 6 HOH 149 549 555 HOH HOH C . 
S 6 HOH 150 550 650 HOH HOH C . 
S 6 HOH 151 551 397 HOH HOH C . 
S 6 HOH 152 552 508 HOH HOH C . 
S 6 HOH 153 553 523 HOH HOH C . 
S 6 HOH 154 554 417 HOH HOH C . 
S 6 HOH 155 555 576 HOH HOH C . 
S 6 HOH 156 556 670 HOH HOH C . 
S 6 HOH 157 557 509 HOH HOH C . 
S 6 HOH 158 558 684 HOH HOH C . 
S 6 HOH 159 559 577 HOH HOH C . 
S 6 HOH 160 560 702 HOH HOH C . 
T 6 HOH 1   301 183 HOH HOH D . 
T 6 HOH 2   302 499 HOH HOH D . 
T 6 HOH 3   303 677 HOH HOH D . 
T 6 HOH 4   304 678 HOH HOH D . 
T 6 HOH 5   305 590 HOH HOH D . 
T 6 HOH 6   306 573 HOH HOH D . 
T 6 HOH 7   307 533 HOH HOH D . 
T 6 HOH 8   308 632 HOH HOH D . 
T 6 HOH 9   309 686 HOH HOH D . 
T 6 HOH 10  310 110 HOH HOH D . 
T 6 HOH 11  311 538 HOH HOH D . 
T 6 HOH 12  312 485 HOH HOH D . 
T 6 HOH 13  313 251 HOH HOH D . 
T 6 HOH 14  314 344 HOH HOH D . 
T 6 HOH 15  315 449 HOH HOH D . 
T 6 HOH 16  316 452 HOH HOH D . 
T 6 HOH 17  317 87  HOH HOH D . 
T 6 HOH 18  318 444 HOH HOH D . 
T 6 HOH 19  319 29  HOH HOH D . 
T 6 HOH 20  320 337 HOH HOH D . 
T 6 HOH 21  321 159 HOH HOH D . 
T 6 HOH 22  322 1   HOH HOH D . 
T 6 HOH 23  323 120 HOH HOH D . 
T 6 HOH 24  324 240 HOH HOH D . 
T 6 HOH 25  325 17  HOH HOH D . 
T 6 HOH 26  326 217 HOH HOH D . 
T 6 HOH 27  327 292 HOH HOH D . 
T 6 HOH 28  328 335 HOH HOH D . 
T 6 HOH 29  329 18  HOH HOH D . 
T 6 HOH 30  330 14  HOH HOH D . 
T 6 HOH 31  331 112 HOH HOH D . 
T 6 HOH 32  332 694 HOH HOH D . 
T 6 HOH 33  333 85  HOH HOH D . 
T 6 HOH 34  334 535 HOH HOH D . 
T 6 HOH 35  335 33  HOH HOH D . 
T 6 HOH 36  336 167 HOH HOH D . 
T 6 HOH 37  337 211 HOH HOH D . 
T 6 HOH 38  338 338 HOH HOH D . 
T 6 HOH 39  339 42  HOH HOH D . 
T 6 HOH 40  340 317 HOH HOH D . 
T 6 HOH 41  341 364 HOH HOH D . 
T 6 HOH 42  342 623 HOH HOH D . 
T 6 HOH 43  343 27  HOH HOH D . 
T 6 HOH 44  344 439 HOH HOH D . 
T 6 HOH 45  345 158 HOH HOH D . 
T 6 HOH 46  346 271 HOH HOH D . 
T 6 HOH 47  347 30  HOH HOH D . 
T 6 HOH 48  348 44  HOH HOH D . 
T 6 HOH 49  349 84  HOH HOH D . 
T 6 HOH 50  350 679 HOH HOH D . 
T 6 HOH 51  351 467 HOH HOH D . 
T 6 HOH 52  352 543 HOH HOH D . 
T 6 HOH 53  353 386 HOH HOH D . 
T 6 HOH 54  354 108 HOH HOH D . 
T 6 HOH 55  355 76  HOH HOH D . 
T 6 HOH 56  356 56  HOH HOH D . 
T 6 HOH 57  357 453 HOH HOH D . 
T 6 HOH 58  358 249 HOH HOH D . 
T 6 HOH 59  359 226 HOH HOH D . 
T 6 HOH 60  360 356 HOH HOH D . 
T 6 HOH 61  361 631 HOH HOH D . 
T 6 HOH 62  362 559 HOH HOH D . 
T 6 HOH 63  363 497 HOH HOH D . 
T 6 HOH 64  364 31  HOH HOH D . 
T 6 HOH 65  365 502 HOH HOH D . 
T 6 HOH 66  366 536 HOH HOH D . 
T 6 HOH 67  367 152 HOH HOH D . 
T 6 HOH 68  368 197 HOH HOH D . 
T 6 HOH 69  369 505 HOH HOH D . 
T 6 HOH 70  370 492 HOH HOH D . 
T 6 HOH 71  371 129 HOH HOH D . 
T 6 HOH 72  372 109 HOH HOH D . 
T 6 HOH 73  373 73  HOH HOH D . 
T 6 HOH 74  374 320 HOH HOH D . 
T 6 HOH 75  375 274 HOH HOH D . 
T 6 HOH 76  376 86  HOH HOH D . 
T 6 HOH 77  377 489 HOH HOH D . 
T 6 HOH 78  378 532 HOH HOH D . 
T 6 HOH 79  379 366 HOH HOH D . 
T 6 HOH 80  380 187 HOH HOH D . 
T 6 HOH 81  381 222 HOH HOH D . 
T 6 HOH 82  382 326 HOH HOH D . 
T 6 HOH 83  383 294 HOH HOH D . 
T 6 HOH 84  384 98  HOH HOH D . 
T 6 HOH 85  385 150 HOH HOH D . 
T 6 HOH 86  386 431 HOH HOH D . 
T 6 HOH 87  387 242 HOH HOH D . 
T 6 HOH 88  388 88  HOH HOH D . 
T 6 HOH 89  389 354 HOH HOH D . 
T 6 HOH 90  390 368 HOH HOH D . 
T 6 HOH 91  391 74  HOH HOH D . 
T 6 HOH 92  392 273 HOH HOH D . 
T 6 HOH 93  393 689 HOH HOH D . 
T 6 HOH 94  394 297 HOH HOH D . 
T 6 HOH 95  395 422 HOH HOH D . 
T 6 HOH 96  396 369 HOH HOH D . 
T 6 HOH 97  397 51  HOH HOH D . 
T 6 HOH 98  398 232 HOH HOH D . 
T 6 HOH 99  399 142 HOH HOH D . 
T 6 HOH 100 400 451 HOH HOH D . 
T 6 HOH 101 401 547 HOH HOH D . 
T 6 HOH 102 402 68  HOH HOH D . 
T 6 HOH 103 403 92  HOH HOH D . 
T 6 HOH 104 404 213 HOH HOH D . 
T 6 HOH 105 405 113 HOH HOH D . 
T 6 HOH 106 406 507 HOH HOH D . 
T 6 HOH 107 407 384 HOH HOH D . 
T 6 HOH 108 408 370 HOH HOH D . 
T 6 HOH 109 409 303 HOH HOH D . 
T 6 HOH 110 410 411 HOH HOH D . 
T 6 HOH 111 411 378 HOH HOH D . 
T 6 HOH 112 412 388 HOH HOH D . 
T 6 HOH 113 413 531 HOH HOH D . 
T 6 HOH 114 414 530 HOH HOH D . 
T 6 HOH 115 415 181 HOH HOH D . 
T 6 HOH 116 416 16  HOH HOH D . 
T 6 HOH 117 417 704 HOH HOH D . 
T 6 HOH 118 418 711 HOH HOH D . 
T 6 HOH 119 419 230 HOH HOH D . 
T 6 HOH 120 420 672 HOH HOH D . 
T 6 HOH 121 421 163 HOH HOH D . 
T 6 HOH 122 422 395 HOH HOH D . 
T 6 HOH 123 423 305 HOH HOH D . 
T 6 HOH 124 424 330 HOH HOH D . 
T 6 HOH 125 425 579 HOH HOH D . 
T 6 HOH 126 426 138 HOH HOH D . 
T 6 HOH 127 427 641 HOH HOH D . 
T 6 HOH 128 428 693 HOH HOH D . 
T 6 HOH 129 429 352 HOH HOH D . 
T 6 HOH 130 430 472 HOH HOH D . 
T 6 HOH 131 431 520 HOH HOH D . 
T 6 HOH 132 432 293 HOH HOH D . 
T 6 HOH 133 433 550 HOH HOH D . 
T 6 HOH 134 434 267 HOH HOH D . 
T 6 HOH 135 435 455 HOH HOH D . 
T 6 HOH 136 436 433 HOH HOH D . 
T 6 HOH 137 437 285 HOH HOH D . 
T 6 HOH 138 438 510 HOH HOH D . 
T 6 HOH 139 439 419 HOH HOH D . 
T 6 HOH 140 440 673 HOH HOH D . 
T 6 HOH 141 441 617 HOH HOH D . 
T 6 HOH 142 442 412 HOH HOH D . 
T 6 HOH 143 443 339 HOH HOH D . 
T 6 HOH 144 444 399 HOH HOH D . 
T 6 HOH 145 445 170 HOH HOH D . 
T 6 HOH 146 446 362 HOH HOH D . 
T 6 HOH 147 447 194 HOH HOH D . 
T 6 HOH 148 448 298 HOH HOH D . 
T 6 HOH 149 449 621 HOH HOH D . 
T 6 HOH 150 450 552 HOH HOH D . 
T 6 HOH 151 451 637 HOH HOH D . 
T 6 HOH 152 452 286 HOH HOH D . 
T 6 HOH 153 453 517 HOH HOH D . 
T 6 HOH 154 454 639 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A XYP 203 ? O4 ? K XYP 1 O4 
2 1 N 1 D XYP 201 ? O4 ? P XYP 1 O4 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.85 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y00 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.192 
_cell.length_a_esd                 ? 
_cell.length_b                     137.834 
_cell.length_b_esd                 ? 
_cell.length_c                     52.822 
_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                         8Y00 
_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                   8Y00 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.79 
_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 6.5, 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                                       8Y00 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.71 
_reflns.d_resolution_low                               25.00 
_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                                     76502 
_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                           96.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.424 
_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                                0.067 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.061 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
1.72 1.78  ? ? ? ? ? ? 7424 ? ? ? ? ? ? ? ? ? ? ? 5.9 1.148 ? ? 0.285 0.116 ? 1  1 0.973 0.993 ? 93.9 ? 0.259 ? ? ? ? ? ? ? ? ? 
1.78 1.85  ? ? ? ? ? ? 7654 ? ? ? ? ? ? ? ? ? ? ? 6.6 1.424 ? ? 0.217 0.084 ? 2  1 0.984 0.996 ? 97.1 ? 0.200 ? ? ? ? ? ? ? ? ? 
1.85 1.94  ? ? ? ? ? ? 7757 ? ? ? ? ? ? ? ? ? ? ? 7.2 1.538 ? ? 0.167 0.062 ? 3  1 0.989 0.997 ? 97.9 ? 0.154 ? ? ? ? ? ? ? ? ? 
1.94 2.04  ? ? ? ? ? ? 7678 ? ? ? ? ? ? ? ? ? ? ? 7.0 1.523 ? ? 0.130 0.049 ? 4  1 0.993 0.998 ? 97.2 ? 0.120 ? ? ? ? ? ? ? ? ? 
2.04 2.17  ? ? ? ? ? ? 7639 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.469 ? ? 0.106 0.041 ? 5  1 0.994 0.998 ? 96.9 ? 0.097 ? ? ? ? ? ? ? ? ? 
2.17 2.33  ? ? ? ? ? ? 7550 ? ? ? ? ? ? ? ? ? ? ? 6.3 1.465 ? ? 0.088 0.035 ? 6  1 0.995 0.999 ? 95.6 ? 0.081 ? ? ? ? ? ? ? ? ? 
2.33 2.57  ? ? ? ? ? ? 7610 ? ? ? ? ? ? ? ? ? ? ? 6.5 1.519 ? ? 0.083 0.032 ? 7  1 0.995 0.999 ? 96.0 ? 0.076 ? ? ? ? ? ? ? ? ? 
2.57 2.94  ? ? ? ? ? ? 7589 ? ? ? ? ? ? ? ? ? ? ? 6.4 1.445 ? ? 0.071 0.028 ? 8  1 0.996 0.999 ? 95.7 ? 0.065 ? ? ? ? ? ? ? ? ? 
2.94 3.70  ? ? ? ? ? ? 7709 ? ? ? ? ? ? ? ? ? ? ? 6.1 1.343 ? ? 0.059 0.024 ? 9  1 0.997 0.999 ? 97.0 ? 0.054 ? ? ? ? ? ? ? ? ? 
3.70 25.00 ? ? ? ? ? ? 7892 ? ? ? ? ? ? ? ? ? ? ? 5.1 1.267 ? ? 0.050 0.022 ? 10 1 0.997 0.999 ? 98.6 ? 0.045 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.88 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.80 
_refine.aniso_B[2][2]                            0.70 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.31 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.741 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.922 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8Y00 
_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                            1.71 
_refine.ls_d_res_low                             24.47 
_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                     72686 
_refine.ls_number_reflns_R_free                  3773 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.06 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18455 
_refine.ls_R_factor_R_free                       0.22895 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18220 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.123 
_refine.pdbx_overall_ESU_R_Free                  0.123 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.506 
_refine.overall_SU_ML                            0.083 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.71 
_refine_hist.d_res_low                        24.47 
_refine_hist.number_atoms_solvent             711 
_refine_hist.number_atoms_total               6720 
_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        5891 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         118 
_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' ? 0.011  0.012  6175  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  4884  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.739  1.653  8451  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.531  1.564  11418 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.354  5.000  760   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 39.790 24.557 316   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.426 15.000 803   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.106 15.000 12    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  832   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  7092  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1344  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.765  2.064  3052  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.763  2.063  3051  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.457  3.091  3808  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.457  3.091  3809  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.841  2.318  3123  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.841  2.318  3124  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.165  3.388  4644  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.449  25.261 7223  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.449  25.263 7224  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.710 
_refine_ls_shell.d_res_low                        1.754 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             219 
_refine_ls_shell.number_reflns_R_work             4926 
_refine_ls_shell.percent_reflns_obs               87.40 
_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                  0.218 
_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   20 
_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                  0.292 
# 
_struct.entry_id                     8Y00 
_struct.title                        'Structure of a xylanase Xyl-1 M4 mutant E175A in complex with xylotriose' 
_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        8Y00 
_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 2 ? 
I N N 4 ? 
J N N 4 ? 
K N N 5 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 5 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 6 ? 
T N N 6 ? 
# 
_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 8Y00 A 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
2 1 8Y00 B 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
3 1 8Y00 C 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
4 1 8Y00 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 8Y00 GLY A 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 1  
1 8Y00 ALA A 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 2  
1 8Y00 GLY A 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  3  
1 8Y00 ALA A 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  4  
1 8Y00 GLY A 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  5  
1 8Y00 ALA A 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  6  
1 8Y00 GLY A 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  7  
1 8Y00 ALA A 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  8  
1 8Y00 GLY A 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  9  
1 8Y00 ALA A 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  10 
1 8Y00 GLY A 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  11 
1 8Y00 MET A 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   12 
1 8Y00 GLU A 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   13 
1 8Y00 PRO A 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  14 
1 8Y00 GLN A 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  15 
1 8Y00 GLN A 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 16 
1 8Y00 HIS A 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 17 
1 8Y00 ALA A 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 18 
2 8Y00 GLY B 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 19 
2 8Y00 ALA B 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 20 
2 8Y00 GLY B 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  21 
2 8Y00 ALA B 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  22 
2 8Y00 GLY B 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  23 
2 8Y00 ALA B 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  24 
2 8Y00 GLY B 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  25 
2 8Y00 ALA B 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  26 
2 8Y00 GLY B 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  27 
2 8Y00 ALA B 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  28 
2 8Y00 GLY B 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  29 
2 8Y00 MET B 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   30 
2 8Y00 GLU B 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   31 
2 8Y00 PRO B 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  32 
2 8Y00 GLN B 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  33 
2 8Y00 GLN B 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 34 
2 8Y00 HIS B 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 35 
2 8Y00 ALA B 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 36 
3 8Y00 GLY C 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 37 
3 8Y00 ALA C 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 38 
3 8Y00 GLY C 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  39 
3 8Y00 ALA C 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  40 
3 8Y00 GLY C 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  41 
3 8Y00 ALA C 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  42 
3 8Y00 GLY C 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  43 
3 8Y00 ALA C 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  44 
3 8Y00 GLY C 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  45 
3 8Y00 ALA C 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  46 
3 8Y00 GLY C 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  47 
3 8Y00 MET C 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   48 
3 8Y00 GLU C 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   49 
3 8Y00 PRO C 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  50 
3 8Y00 GLN C 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  51 
3 8Y00 GLN C 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 52 
3 8Y00 HIS C 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 53 
3 8Y00 ALA C 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 54 
4 8Y00 GLY D 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 55 
4 8Y00 ALA D 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 56 
4 8Y00 GLY D 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  57 
4 8Y00 ALA D 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  58 
4 8Y00 GLY D 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  59 
4 8Y00 ALA D 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  60 
4 8Y00 GLY D 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  61 
4 8Y00 ALA D 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  62 
4 8Y00 GLY D 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  63 
4 8Y00 ALA D 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  64 
4 8Y00 GLY D 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  65 
4 8Y00 MET D 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   66 
4 8Y00 GLU D 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   67 
4 8Y00 PRO D 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  68 
4 8Y00 GLN D 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  69 
4 8Y00 GLN D 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 70 
4 8Y00 HIS D 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 71 
4 8Y00 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_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 90   ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  8520 ? 
2 'ABSA (A^2)' 90   ? 
2 MORE         -26  ? 
2 'SSA (A^2)'  8190 ? 
3 'ABSA (A^2)' 90   ? 
3 MORE         -26  ? 
3 'SSA (A^2)'  8220 ? 
4 'ABSA (A^2)' 0    ? 
4 MORE         0    ? 
4 'SSA (A^2)'  8230 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,I,J,K,Q 
2 1 B,F,L,M,R   
3 1 C,G,N,O,S   
4 1 D,H,P,T     
# 
_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 ? E XYP .   O4  ? ? ? 1_555 E XYP . C1 ? ? E XYP 1   E XYP 2   1_555 ? ? ? ? ? ? ? 1.384 ? ? 
covale2  covale both ? F XYP .   O4  ? ? ? 1_555 F XYP . C1 ? ? F XYP 1   F XYP 2   1_555 ? ? ? ? ? ? ? 1.510 ? ? 
covale3  covale both ? F XYP .   O4  ? ? ? 1_555 F XYP . C1 ? ? F XYP 2   F XYP 3   1_555 ? ? ? ? ? ? ? 1.478 ? ? 
covale4  covale both ? G XYP .   O4  ? ? ? 1_555 G XYP . C1 ? ? G XYP 1   G XYP 2   1_555 ? ? ? ? ? ? ? 1.485 ? ? 
covale5  covale both ? G XYP .   O4  ? ? ? 1_555 G XYP . C1 ? ? G XYP 2   G XYP 3   1_555 ? ? ? ? ? ? ? 1.548 ? ? 
covale6  covale both ? H XYP .   O4  ? ? ? 1_555 H XYP . C1 ? ? H XYP 1   H XYP 2   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
metalc1  metalc ?    ? A PHE 104 O   ? ? ? 1_555 J ZN  . ZN ? ? A PHE 92  A ZN  202 1_555 ? ? ? ? ? ? ? 2.429 ? ? 
metalc2  metalc ?    ? A ASP 154 OD1 ? ? ? 1_555 I ZN  . ZN ? ? A ASP 142 A ZN  201 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc3  metalc ?    ? A ASP 154 OD2 ? ? ? 1_555 I ZN  . ZN ? ? A ASP 142 A ZN  201 1_555 ? ? ? ? ? ? ? 2.698 ? ? 
metalc4  metalc ?    ? A HIS 155 ND1 ? ? ? 1_555 J ZN  . ZN ? ? A HIS 143 A ZN  202 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc5  metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  201 A HOH 304 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc6  metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  201 B HOH 422 1_554 ? ? ? ? ? ? ? 2.196 ? ? 
metalc7  metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  201 B HOH 481 1_554 ? ? ? ? ? ? ? 2.043 ? ? 
metalc8  metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? A ZN  201 B HOH 546 1_554 ? ? ? ? ? ? ? 2.614 ? ? 
metalc9  metalc ?    ? J ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  202 A HOH 330 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc10 metalc ?    ? J ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  202 A HOH 427 1_555 ? ? ? ? ? ? ? 2.152 ? ? 
metalc11 metalc ?    ? J ZN  .   ZN  ? ? ? 1_555 Q HOH . O  ? ? A ZN  202 A HOH 433 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc12 metalc ?    ? Q HOH .   O   ? ? ? 1_455 L ZN  . ZN ? ? A HOH 445 B ZN  300 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc13 metalc ?    ? Q HOH .   O   ? ? ? 1_455 L ZN  . ZN ? ? A HOH 454 B ZN  300 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc14 metalc ?    ? B PHE 104 O   ? ? ? 1_555 M ZN  . ZN ? ? B PHE 92  B ZN  301 1_555 ? ? ? ? ? ? ? 2.645 ? ? 
metalc15 metalc ?    ? B ASP 154 OD1 ? ? ? 1_555 L ZN  . ZN ? ? B ASP 142 B ZN  300 1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc16 metalc ?    ? B HIS 155 ND1 ? ? ? 1_555 M ZN  . ZN ? ? B HIS 143 B ZN  301 1_555 ? ? ? ? ? ? ? 1.918 ? ? 
metalc17 metalc ?    ? L ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? B ZN  300 B HOH 417 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
metalc18 metalc ?    ? M ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? B ZN  301 B HOH 470 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc19 metalc ?    ? M ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? B ZN  301 B HOH 529 1_555 ? ? ? ? ? ? ? 1.816 ? ? 
metalc20 metalc ?    ? M ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? B ZN  301 B HOH 541 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc21 metalc ?    ? M ZN  .   ZN  ? ? ? 1_555 R HOH . O  ? ? B ZN  301 B HOH 575 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc22 metalc ?    ? C PHE 104 O   ? ? ? 1_555 O ZN  . ZN ? ? C PHE 92  C ZN  301 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc23 metalc ?    ? C ASP 154 OD1 ? ? ? 1_555 N ZN  . ZN ? ? C ASP 142 C ZN  300 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc24 metalc ?    ? C ASP 154 OD2 ? ? ? 1_555 N ZN  . ZN ? ? C ASP 142 C ZN  300 1_555 ? ? ? ? ? ? ? 2.483 ? ? 
metalc25 metalc ?    ? C HIS 155 ND1 ? ? ? 1_555 O ZN  . ZN ? ? C HIS 143 C ZN  301 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc26 metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? C ZN  300 C HOH 469 1_555 ? ? ? ? ? ? ? 1.833 ? ? 
metalc27 metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 T HOH . O  ? ? C ZN  300 D HOH 305 1_556 ? ? ? ? ? ? ? 2.176 ? ? 
metalc28 metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 T HOH . O  ? ? C ZN  300 D HOH 418 1_556 ? ? ? ? ? ? ? 2.218 ? ? 
metalc29 metalc ?    ? O ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? C ZN  301 C HOH 455 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc30 metalc ?    ? O ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? C ZN  301 C HOH 494 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc31 metalc ?    ? O ZN  .   ZN  ? ? ? 1_555 S HOH . O  ? ? C ZN  301 C HOH 519 1_555 ? ? ? ? ? ? ? 1.977 ? ? 
# 
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 ? J ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 155 ? A HIS 143 ? 1_555 90.3  ? 
2  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 330 ? 1_555 77.1  ? 
3  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 330 ? 1_555 113.8 ? 
4  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 427 ? 1_555 81.2  ? 
5  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 427 ? 1_555 116.3 ? 
6  O   ? Q HOH .   ? A HOH 330 ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 427 ? 1_555 125.0 ? 
7  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 433 ? 1_555 172.8 ? 
8  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 433 ? 1_555 96.9  ? 
9  O   ? Q HOH .   ? A HOH 330 ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 433 ? 1_555 100.3 ? 
10 O   ? Q HOH .   ? A HOH 427 ? 1_555 ZN ? J ZN . ? A ZN 202 ? 1_555 O   ? Q HOH .   ? A HOH 433 ? 1_555 95.1  ? 
11 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 51.4  ? 
12 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? Q HOH .   ? A HOH 304 ? 1_555 98.2  ? 
13 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? Q HOH .   ? A HOH 304 ? 1_555 52.3  ? 
14 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 422 ? 1_554 84.8  ? 
15 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 422 ? 1_554 128.2 ? 
16 O   ? Q HOH .   ? A HOH 304 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 422 ? 1_554 174.4 ? 
17 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 481 ? 1_554 107.2 ? 
18 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 481 ? 1_554 82.8  ? 
19 O   ? Q HOH .   ? A HOH 304 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 481 ? 1_554 88.2  ? 
20 O   ? R HOH .   ? B HOH 422 ? 1_554 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 481 ? 1_554 86.5  ? 
21 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 546 ? 1_554 117.2 ? 
22 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 546 ? 1_554 140.4 ? 
23 O   ? Q HOH .   ? A HOH 304 ? 1_555 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 546 ? 1_554 103.0 ? 
24 O   ? R HOH .   ? B HOH 422 ? 1_554 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 546 ? 1_554 79.6  ? 
25 O   ? R HOH .   ? B HOH 481 ? 1_554 ZN ? I ZN . ? A ZN 201 ? 1_555 O   ? R HOH .   ? B HOH 546 ? 1_554 131.6 ? 
26 O   ? Q HOH .   ? A HOH 445 ? 1_455 ZN ? L ZN . ? B ZN 300 ? 1_555 O   ? Q HOH .   ? A HOH 454 ? 1_455 69.9  ? 
27 O   ? Q HOH .   ? A HOH 445 ? 1_455 ZN ? L ZN . ? B ZN 300 ? 1_555 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 110.5 ? 
28 O   ? Q HOH .   ? A HOH 454 ? 1_455 ZN ? L ZN . ? B ZN 300 ? 1_555 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 168.4 ? 
29 O   ? Q HOH .   ? A HOH 445 ? 1_455 ZN ? L ZN . ? B ZN 300 ? 1_555 O   ? R HOH .   ? B HOH 417 ? 1_555 76.0  ? 
30 O   ? Q HOH .   ? A HOH 454 ? 1_455 ZN ? L ZN . ? B ZN 300 ? 1_555 O   ? R HOH .   ? B HOH 417 ? 1_555 106.6 ? 
31 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? L ZN . ? B ZN 300 ? 1_555 O   ? R HOH .   ? B HOH 417 ? 1_555 84.4  ? 
32 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 85.0  ? 
33 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 470 ? 1_555 72.0  ? 
34 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 470 ? 1_555 110.0 ? 
35 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 529 ? 1_555 168.4 ? 
36 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 529 ? 1_555 106.5 ? 
37 O   ? R HOH .   ? B HOH 470 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 529 ? 1_555 104.8 ? 
38 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 541 ? 1_555 79.2  ? 
39 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 541 ? 1_555 111.9 ? 
40 O   ? R HOH .   ? B HOH 470 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 541 ? 1_555 125.9 ? 
41 O   ? R HOH .   ? B HOH 529 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 541 ? 1_555 94.5  ? 
42 O   ? B PHE 104 ? B PHE 92  ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 575 ? 1_555 112.6 ? 
43 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 575 ? 1_555 142.1 ? 
44 O   ? R HOH .   ? B HOH 470 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 575 ? 1_555 51.5  ? 
45 O   ? R HOH .   ? B HOH 529 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 575 ? 1_555 59.2  ? 
46 O   ? R HOH .   ? B HOH 541 ? 1_555 ZN ? M ZN . ? B ZN 301 ? 1_555 O   ? R HOH .   ? B HOH 575 ? 1_555 104.4 ? 
47 O   ? C PHE 104 ? C PHE 92  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 155 ? C HIS 143 ? 1_555 91.3  ? 
48 O   ? C PHE 104 ? C PHE 92  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 455 ? 1_555 78.7  ? 
49 ND1 ? C HIS 155 ? C HIS 143 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 455 ? 1_555 106.1 ? 
50 O   ? C PHE 104 ? C PHE 92  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 494 ? 1_555 80.9  ? 
51 ND1 ? C HIS 155 ? C HIS 143 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 494 ? 1_555 119.0 ? 
52 O   ? S HOH .   ? C HOH 455 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 494 ? 1_555 130.5 ? 
53 O   ? C PHE 104 ? C PHE 92  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 519 ? 1_555 165.4 ? 
54 ND1 ? C HIS 155 ? C HIS 143 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 519 ? 1_555 99.5  ? 
55 O   ? S HOH .   ? C HOH 455 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 519 ? 1_555 107.4 ? 
56 O   ? S HOH .   ? C HOH 494 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 O   ? S HOH .   ? C HOH 519 ? 1_555 85.3  ? 
57 OD1 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 OD2 ? C ASP 154 ? C ASP 142 ? 1_555 56.1  ? 
58 OD1 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? S HOH .   ? C HOH 469 ? 1_555 135.7 ? 
59 OD2 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? S HOH .   ? C HOH 469 ? 1_555 79.7  ? 
60 OD1 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 305 ? 1_556 94.9  ? 
61 OD2 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 305 ? 1_556 99.8  ? 
62 O   ? S HOH .   ? C HOH 469 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 305 ? 1_556 95.2  ? 
63 OD1 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 418 ? 1_556 128.1 ? 
64 OD2 ? C ASP 154 ? C ASP 142 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 418 ? 1_556 173.0 ? 
65 O   ? S HOH .   ? C HOH 469 ? 1_555 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 418 ? 1_556 95.6  ? 
66 O   ? T HOH .   ? D HOH 305 ? 1_556 ZN ? N ZN . ? C ZN 300 ? 1_555 O   ? T HOH .   ? D HOH 418 ? 1_556 85.8  ? 
# 
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 5.20  
2 ASN 93 A . ? ASN 81 A PRO 94 A ? PRO 82 A 1 5.66  
3 ASN 64 B . ? ASN 52 B PRO 65 B ? PRO 53 B 1 -5.58 
4 ASN 93 B . ? ASN 81 B PRO 94 B ? PRO 82 B 1 4.33  
5 ASN 64 C . ? ASN 52 C PRO 65 C ? PRO 53 C 1 -0.14 
6 ASN 93 C . ? ASN 81 C PRO 94 C ? PRO 82 C 1 4.96  
7 ASN 64 D . ? ASN 52 D PRO 65 D ? PRO 53 D 1 -2.71 
8 ASN 93 D . ? ASN 81 D PRO 94 D ? PRO 82 D 1 0.25  
# 
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 ? 9 ? 
AA8 ? 5 ? 
# 
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 
AA7 6 7 ? parallel      
AA7 7 8 ? anti-parallel 
AA7 8 9 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? 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 ASN C 56  ? TRP C 63  ? ASN C 44  TRP C 51  
AA5 4 THR C 179 ? TYR C 190 ? THR C 167 TYR C 178 
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 GLU C 115 ? THR C 121 ? GLU C 103 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 18  ? ASN D 22  ? GLU D 6   ASN D 10  
AA7 2 TYR D 25  ? THR D 31  ? TYR D 13  THR D 19  
AA7 3 PHE D 57  ? TRP D 63  ? PHE D 45  TRP D 51  
AA7 4 THR D 179 ? GLY D 189 ? THR D 167 GLY D 177 
AA7 5 SER D 83  ? GLN D 92  ? SER D 71  GLN D 80  
AA7 6 VAL D 96  ? SER D 105 ? VAL D 84  SER D 93  
AA7 7 ALA D 143 ? ARG D 152 ? ALA D 131 ARG D 140 
AA7 8 GLY D 124 ? ALA D 136 ? GLY D 112 ALA D 124 
AA7 9 GLN D 114 ? THR D 121 ? GLN D 102 THR D 109 
AA8 1 GLN D 36  ? ASN D 41  ? GLN D 24  ASN D 29  
AA8 2 GLN D 46  ? SER D 52  ? GLN D 34  SER D 40  
AA8 3 SER D 193 ? VAL D 200 ? SER D 181 VAL D 188 
AA8 4 THR D 70  ? ASN D 80  ? THR D 58  ASN D 68  
AA8 5 GLY D 159 ? THR D 162 ? GLY D 147 THR D 150 
# 
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 SER A 28  ? N SER A 16  O GLY A 60  ? O GLY A 48  
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 TYR A 126 ? O TYR A 114 N VAL A 119 ? N VAL A 107 
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 ASN B 22  ? N ASN B 10  O TYR B 25  ? O TYR B 13  
AA3 2 3 N SER B 28  ? N SER B 16  O GLY B 60  ? O GLY B 48  
AA3 3 4 N LYS B 61  ? N LYS B 49  O VAL B 185 ? O VAL B 173 
AA3 4 5 O ALA B 186 ? O ALA B 174 N SER B 86  ? N SER B 74  
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 GLY B 117 ? N GLY B 105 
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 195 ? O SER B 183 N ASN B 78  ? N ASN B 66  
AA4 4 5 N ILE B 71  ? N ILE B 59  O VAL B 161 ? O VAL B 149 
AA5 1 2 N GLU C 18  ? N GLU C 6   O PHE C 29  ? O PHE C 17  
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 ALA C 186 ? O ALA C 174 N SER C 86  ? N SER C 74  
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 PHE C 145 ? O PHE C 133 N ARG C 133 ? N ARG C 121 
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 40  ? N THR C 28  O SER C 48  ? O SER C 36  
AA6 2 3 N TYR C 47  ? N TYR C 35  O ILE C 198 ? O ILE C 186 
AA6 3 4 O SER C 195 ? O SER C 183 N ASN C 78  ? N ASN C 66  
AA6 4 5 N ILE C 71  ? N ILE C 59  O VAL C 161 ? O VAL C 149 
AA7 1 2 N ASN D 22  ? N ASN D 10  O TYR D 25  ? O TYR D 13  
AA7 2 3 N SER D 28  ? N SER D 16  O GLY D 60  ? O GLY D 48  
AA7 3 4 N LYS D 61  ? N LYS D 49  O VAL D 185 ? O VAL D 173 
AA7 4 5 O ILE D 184 ? O ILE D 172 N TYR D 88  ? N TYR D 76  
AA7 5 6 N VAL D 87  ? N VAL D 75  O ILE D 100 ? O ILE D 88  
AA7 6 7 N VAL D 101 ? N VAL D 89  O SER D 150 ? O SER D 138 
AA7 7 8 O ALA D 143 ? O ALA D 131 N ALA D 136 ? N ALA D 124 
AA7 8 9 O TYR D 126 ? O TYR D 114 N VAL D 119 ? N VAL D 107 
AA8 1 2 N THR D 38  ? N THR D 26  O GLU D 50  ? O GLU D 38  
AA8 2 3 N TRP D 51  ? N TRP D 39  O GLY D 194 ? O GLY D 182 
AA8 3 4 O SER D 193 ? O SER D 181 N ASN D 80  ? N ASN D 68  
AA8 4 5 N ILE D 71  ? N ILE D 59  O VAL D 161 ? O VAL D 149 
# 
_pdbx_entry_details.entry_id                   8Y00 
_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  201 ? ? O   A HOH 303 ? ? 1.57 
2  1 O1  E XYP 1   ? ? C4  A XYP 203 ? ? 1.58 
3  1 O1  H XYP 1   ? ? C4  D XYP 201 ? ? 1.60 
4  1 OE1 A GLU 128 ? ? O   A HOH 301 ? ? 1.61 
5  1 ZN  B ZN  300 ? ? O   B HOH 428 ? ? 1.64 
6  1 ZN  C ZN  300 ? ? O   C HOH 402 ? ? 1.69 
7  1 O   D HOH 369 ? ? O   D HOH 398 ? ? 1.79 
8  1 O   B HOH 543 ? ? O   B HOH 580 ? ? 1.84 
9  1 O   A HOH 302 ? ? O   A HOH 333 ? ? 1.85 
10 1 OE2 A GLU 64  ? ? O   A HOH 302 ? ? 1.87 
11 1 O   C HOH 433 ? ? O   D HOH 315 ? ? 1.91 
12 1 O   C HOH 401 ? ? O   C HOH 495 ? ? 1.92 
13 1 O   C HOH 401 ? ? O   C HOH 412 ? ? 1.92 
14 1 O   A HOH 463 ? ? O   A HOH 470 ? ? 1.94 
15 1 O   B HOH 470 ? ? O   B HOH 575 ? ? 1.97 
16 1 OH  D TYR 87  ? ? O1  D XYP 201 ? ? 1.99 
17 1 OE2 B GLU 164 ? ? O   B HOH 401 ? ? 2.01 
18 1 OE2 C GLU 64  ? ? O   C HOH 401 ? ? 2.03 
19 1 O   A HOH 329 ? ? O   A HOH 384 ? ? 2.03 
20 1 OD1 C ASP 142 ? ? O   C HOH 402 ? ? 2.08 
21 1 NZ  B LYS 159 ? ? O   B HOH 402 ? ? 2.10 
22 1 NE2 D GLN 118 ? ? O   D HOH 301 ? ? 2.11 
23 1 OE1 D GLU 108 ? ? OG1 D THR 113 ? ? 2.11 
24 1 O   B HOH 529 ? ? O   B HOH 575 ? ? 2.11 
25 1 O   C HOH 501 ? ? O   C HOH 549 ? ? 2.12 
26 1 O   D HOH 444 ? ? O   D HOH 450 ? ? 2.13 
27 1 OE1 B GLU 103 ? ? O   B HOH 403 ? ? 2.16 
28 1 OE2 B GLU 122 ? ? O   B HOH 404 ? ? 2.16 
29 1 O   A HOH 318 ? ? O   A HOH 468 ? ? 2.18 
# 
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   B HOH 494 ? ? 1_555 O D HOH 444 ? ? 1_556 1.78 
2 1 O   A HOH 303 ? ? 1_555 O B HOH 546 ? ? 1_554 2.04 
3 1 O   C HOH 402 ? ? 1_555 O D HOH 418 ? ? 1_556 2.10 
4 1 O   A HOH 423 ? ? 1_555 O B HOH 406 ? ? 1_655 2.15 
5 1 OE2 B GLU 164 ? ? 1_555 O A HOH 302 ? ? 1_556 2.16 
# 
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  ? ? 50.90   -128.39 
2  1 SER A 93  ? ? -102.11 -90.70  
3  1 ASN A 169 ? ? -99.77  -138.13 
4  1 ALA B 32  ? ? 52.56   -127.60 
5  1 SER B 93  ? ? -99.57  -89.14  
6  1 ASN B 169 ? ? -101.13 -134.15 
7  1 ALA C 32  ? ? 50.75   -120.30 
8  1 SER C 55  ? ? -105.42 -161.73 
9  1 SER C 56  ? ? -107.31 46.23   
10 1 SER C 93  ? ? -106.17 -96.45  
11 1 ASN C 169 ? ? -99.08  -136.24 
12 1 ALA D 32  ? ? 50.67   -122.54 
13 1 THR D 94  ? ? 72.81   -30.79  
14 1 ASN D 169 ? ? -101.91 -138.21 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   C 
_pdbx_validate_peptide_omega.auth_seq_id_1    42 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   C 
_pdbx_validate_peptide_omega.auth_seq_id_2    43 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.44 
# 
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 B GLY -11 ? B GLY 1  
6  1 Y 1 B ALA -10 ? B ALA 2  
7  1 Y 1 B GLY -9  ? B GLY 3  
8  1 Y 1 B ALA -8  ? B ALA 4  
9  1 Y 1 B GLY -7  ? B GLY 5  
10 1 Y 1 B ALA -6  ? B ALA 6  
11 1 Y 1 B GLY -5  ? B GLY 7  
12 1 Y 1 B ALA -4  ? B ALA 8  
13 1 Y 1 B GLY -3  ? B GLY 9  
14 1 Y 1 B ALA -2  ? B ALA 10 
15 1 Y 1 B GLY -1  ? B GLY 11 
16 1 Y 1 B MET 0   ? B MET 12 
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 
40 1 Y 1 D MET 0   ? D MET 12 
# 
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 
3 XYP 1 n 
3 XYP 2 n 
3 XYP 3 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                    8Y00 
_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]   0.019160 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002640 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007255 
_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]   0.019110 
_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   . GLY A 1 5   ? 6.384   -14.824 7.741   1.00 37.88 ? -7  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 5   ? 7.880   -14.654 7.714   1.00 35.79 ? -7  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 5   ? 8.557   -15.690 6.825   1.00 37.19 ? -7  GLY A C   1 
ATOM   4    O  O   . GLY A 1 5   ? 8.154   -15.788 5.632   1.00 32.79 ? -7  GLY A O   1 
ATOM   5    N  N   . ALA A 1 6   ? 9.531   -16.431 7.383   1.00 32.43 ? -6  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 6   ? 10.360  -17.462 6.703   1.00 33.72 ? -6  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 6   ? 9.630   -18.816 6.637   1.00 34.34 ? -6  ALA A C   1 
ATOM   8    O  O   . ALA A 1 6   ? 10.244  -19.795 6.119   1.00 31.04 ? -6  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 6   ? 11.681  -17.616 7.435   1.00 30.86 ? -6  ALA A CB  1 
ATOM   10   N  N   . GLY A 1 7   ? 8.400   -18.890 7.171   1.00 32.83 ? -5  GLY A N   1 
ATOM   11   C  CA  . GLY A 1 7   ? 7.557   -20.100 7.168   1.00 33.30 ? -5  GLY A CA  1 
ATOM   12   C  C   . GLY A 1 7   ? 8.310   -21.271 7.762   1.00 32.40 ? -5  GLY A C   1 
ATOM   13   O  O   . GLY A 1 7   ? 8.905   -21.098 8.863   1.00 34.80 ? -5  GLY A O   1 
ATOM   14   N  N   . ALA A 1 8   ? 8.394   -22.383 7.021   1.00 30.77 ? -4  ALA A N   1 
ATOM   15   C  CA  . ALA A 1 8   ? 9.134   -23.603 7.441   1.00 33.95 ? -4  ALA A CA  1 
ATOM   16   C  C   . ALA A 1 8   ? 10.628  -23.296 7.636   1.00 31.85 ? -4  ALA A C   1 
ATOM   17   O  O   . ALA A 1 8   ? 11.299  -24.107 8.292   1.00 34.46 ? -4  ALA A O   1 
ATOM   18   C  CB  . ALA A 1 8   ? 8.942   -24.732 6.449   1.00 31.87 ? -4  ALA A CB  1 
ATOM   19   N  N   . GLY A 1 9   ? 11.135  -22.189 7.077   1.00 30.31 ? -3  GLY A N   1 
ATOM   20   C  CA  . GLY A 1 9   ? 12.575  -21.863 7.073   1.00 29.95 ? -3  GLY A CA  1 
ATOM   21   C  C   . GLY A 1 9   ? 13.082  -21.340 8.409   1.00 29.82 ? -3  GLY A C   1 
ATOM   22   O  O   . GLY A 1 9   ? 14.305  -21.155 8.528   1.00 31.20 ? -3  GLY A O   1 
ATOM   23   N  N   . ALA A 1 10  ? 12.194  -21.016 9.357   1.00 31.12 ? -2  ALA A N   1 
ATOM   24   C  CA  . ALA A 1 10  ? 12.569  -20.417 10.661  1.00 31.15 ? -2  ALA A CA  1 
ATOM   25   C  C   . ALA A 1 10  ? 13.463  -21.417 11.391  1.00 33.96 ? -2  ALA A C   1 
ATOM   26   O  O   . ALA A 1 10  ? 13.122  -22.625 11.327  1.00 34.06 ? -2  ALA A O   1 
ATOM   27   C  CB  . ALA A 1 10  ? 11.325  -20.064 11.451  1.00 32.90 ? -2  ALA A CB  1 
ATOM   28   N  N   . GLY A 1 11  ? 14.563  -20.959 12.018  1.00 32.17 ? -1  GLY A N   1 
ATOM   29   C  CA  . GLY A 1 11  ? 15.447  -21.792 12.862  1.00 31.51 ? -1  GLY A CA  1 
ATOM   30   C  C   . GLY A 1 11  ? 14.800  -22.146 14.200  1.00 32.48 ? -1  GLY A C   1 
ATOM   31   O  O   . GLY A 1 11  ? 13.603  -21.849 14.366  1.00 28.54 ? -1  GLY A O   1 
ATOM   32   N  N   . MET A 1 12  ? 15.551  -22.795 15.108  1.00 32.45 ? 0   MET A N   1 
ATOM   33   C  CA  . MET A 1 12  ? 15.056  -23.227 16.448  1.00 33.03 ? 0   MET A CA  1 
ATOM   34   C  C   . MET A 1 12  ? 14.569  -21.999 17.220  1.00 31.25 ? 0   MET A C   1 
ATOM   35   O  O   . MET A 1 12  ? 15.242  -20.946 17.139  1.00 28.87 ? 0   MET A O   1 
ATOM   36   C  CB  . MET A 1 12  ? 16.146  -23.937 17.264  1.00 42.52 ? 0   MET A CB  1 
ATOM   37   C  CG  . MET A 1 12  ? 17.299  -23.054 17.749  1.00 49.83 ? 0   MET A CG  1 
ATOM   38   S  SD  . MET A 1 12  ? 17.346  -22.716 19.559  1.00 67.11 ? 0   MET A SD  1 
ATOM   39   C  CE  . MET A 1 12  ? 16.920  -24.316 20.248  1.00 65.08 ? 0   MET A CE  1 
ATOM   40   N  N   . GLU A 1 13  ? 13.494  -22.131 18.000  1.00 28.41 ? 1   GLU A N   1 
ATOM   41   C  CA  . GLU A 1 13  ? 12.979  -20.973 18.787  1.00 26.58 ? 1   GLU A CA  1 
ATOM   42   C  C   . GLU A 1 13  ? 13.954  -20.669 19.929  1.00 25.49 ? 1   GLU A C   1 
ATOM   43   O  O   . GLU A 1 13  ? 14.385  -21.581 20.624  1.00 23.93 ? 1   GLU A O   1 
ATOM   44   C  CB  . GLU A 1 13  ? 11.571  -21.212 19.327  1.00 30.27 ? 1   GLU A CB  1 
ATOM   45   C  CG  . GLU A 1 13  ? 10.509  -21.321 18.246  1.00 33.37 ? 1   GLU A CG  1 
ATOM   46   C  CD  . GLU A 1 13  ? 9.092   -21.346 18.798  1.00 38.68 ? 1   GLU A CD  1 
ATOM   47   O  OE1 . GLU A 1 13  ? 8.947   -21.496 20.030  1.00 45.22 ? 1   GLU A OE1 1 
ATOM   48   O  OE2 . GLU A 1 13  ? 8.140   -21.213 18.004  1.00 40.97 ? 1   GLU A OE2 1 
ATOM   49   N  N   . ILE A 1 14  ? 14.319  -19.407 20.071  1.00 21.60 ? 2   ILE A N   1 
ATOM   50   C  CA  . ILE A 1 14  ? 15.229  -18.877 21.127  1.00 21.97 ? 2   ILE A CA  1 
ATOM   51   C  C   . ILE A 1 14  ? 14.347  -18.041 22.065  1.00 21.69 ? 2   ILE A C   1 
ATOM   52   O  O   . ILE A 1 14  ? 13.654  -17.145 21.548  1.00 22.24 ? 2   ILE A O   1 
ATOM   53   C  CB  . ILE A 1 14  ? 16.368  -18.058 20.480  1.00 23.98 ? 2   ILE A CB  1 
ATOM   54   C  CG1 . ILE A 1 14  ? 17.303  -18.940 19.630  1.00 26.67 ? 2   ILE A CG1 1 
ATOM   55   C  CG2 . ILE A 1 14  ? 17.127  -17.266 21.531  1.00 26.20 ? 2   ILE A CG2 1 
ATOM   56   C  CD1 . ILE A 1 14  ? 18.307  -18.165 18.762  1.00 28.16 ? 2   ILE A CD1 1 
ATOM   57   N  N   . THR A 1 15  ? 14.407  -18.271 23.386  1.00 21.37 ? 3   THR A N   1 
ATOM   58   C  CA  . THR A 1 15  ? 13.514  -17.591 24.367  1.00 22.53 ? 3   THR A CA  1 
ATOM   59   C  C   . THR A 1 15  ? 14.304  -16.903 25.481  1.00 21.32 ? 3   THR A C   1 
ATOM   60   O  O   . THR A 1 15  ? 13.673  -16.315 26.361  1.00 23.33 ? 3   THR A O   1 
ATOM   61   C  CB  . THR A 1 15  ? 12.506  -18.607 24.904  1.00 24.94 ? 3   THR A CB  1 
ATOM   62   O  OG1 . THR A 1 15  ? 13.263  -19.646 25.532  1.00 25.72 ? 3   THR A OG1 1 
ATOM   63   C  CG2 . THR A 1 15  ? 11.626  -19.147 23.801  1.00 26.87 ? 3   THR A CG2 1 
ATOM   64   N  N   . SER A 1 16  ? 15.624  -17.018 25.481  1.00 19.04 ? 4   SER A N   1 
ATOM   65   C  CA  . SER A 1 16  ? 16.517  -16.387 26.485  1.00 20.92 ? 4   SER A CA  1 
ATOM   66   C  C   . SER A 1 16  ? 17.715  -15.814 25.739  1.00 19.45 ? 4   SER A C   1 
ATOM   67   O  O   . SER A 1 16  ? 17.978  -16.297 24.613  1.00 18.08 ? 4   SER A O   1 
ATOM   68   C  CB  . SER A 1 16  ? 16.872  -17.323 27.629  1.00 24.79 ? 4   SER A CB  1 
ATOM   69   O  OG  . SER A 1 16  ? 17.621  -18.432 27.195  1.00 29.08 ? 4   SER A OG  1 
ATOM   70   N  N   . SER A 1 17  ? 18.300  -14.755 26.303  1.00 19.18 ? 5   SER A N   1 
ATOM   71   C  CA  . SER A 1 17  ? 19.347  -13.889 25.701  1.00 19.01 ? 5   SER A CA  1 
ATOM   72   C  C   . SER A 1 17  ? 20.463  -14.729 25.089  1.00 19.72 ? 5   SER A C   1 
ATOM   73   O  O   . SER A 1 17  ? 20.939  -15.712 25.751  1.00 20.27 ? 5   SER A O   1 
ATOM   74   C  CB  . SER A 1 17  ? 19.860  -12.929 26.717  1.00 21.74 ? 5   SER A CB  1 
ATOM   75   O  OG  . SER A 1 17  ? 18.808  -12.087 27.158  1.00 19.34 ? 5   SER A OG  1 
ATOM   76   N  N   . GLU A 1 18  ? 20.852  -14.405 23.860  1.00 17.46 ? 6   GLU A N   1 
ATOM   77   C  CA  . GLU A 1 18  ? 22.047  -15.019 23.274  1.00 19.53 ? 6   GLU A CA  1 
ATOM   78   C  C   . GLU A 1 18  ? 22.444  -14.273 22.035  1.00 16.89 ? 6   GLU A C   1 
ATOM   79   O  O   . GLU A 1 18  ? 21.619  -13.606 21.444  1.00 18.19 ? 6   GLU A O   1 
ATOM   80   C  CB  . GLU A 1 18  ? 21.842  -16.509 22.930  1.00 22.15 ? 6   GLU A CB  1 
ATOM   81   C  CG  . GLU A 1 18  ? 20.866  -16.782 21.815  1.00 22.43 ? 6   GLU A CG  1 
ATOM   82   C  CD  . GLU A 1 18  ? 20.904  -18.226 21.296  1.00 28.15 ? 6   GLU A CD  1 
ATOM   83   O  OE1 . GLU A 1 18  ? 21.257  -18.431 20.101  1.00 29.00 ? 6   GLU A OE1 1 
ATOM   84   O  OE2 . GLU A 1 18  ? 20.606  -19.147 22.087  1.00 28.01 ? 6   GLU A OE2 1 
ATOM   85   N  N   . THR A 1 19  ? 23.681  -14.497 21.637  1.00 17.88 ? 7   THR A N   1 
ATOM   86   C  CA  . THR A 1 19  ? 24.256  -13.887 20.443  1.00 16.64 ? 7   THR A CA  1 
ATOM   87   C  C   . THR A 1 19  ? 24.956  -14.970 19.637  1.00 16.90 ? 7   THR A C   1 
ATOM   88   O  O   . THR A 1 19  ? 25.257  -16.059 20.156  1.00 18.64 ? 7   THR A O   1 
ATOM   89   C  CB  . THR A 1 19  ? 25.196  -12.721 20.758  1.00 17.65 ? 7   THR A CB  1 
ATOM   90   O  OG1 . THR A 1 19  ? 26.425  -13.227 21.317  1.00 17.97 ? 7   THR A OG1 1 
ATOM   91   C  CG2 . THR A 1 19  ? 24.532  -11.649 21.608  1.00 18.89 ? 7   THR A CG2 1 
ATOM   92   N  N   . GLY A 1 20  ? 25.176  -14.676 18.379  1.00 17.15 ? 8   GLY A N   1 
ATOM   93   C  CA  . GLY A 1 20  ? 25.927  -15.576 17.496  1.00 15.53 ? 8   GLY A CA  1 
ATOM   94   C  C   . GLY A 1 20  ? 26.008  -15.017 16.100  1.00 16.88 ? 8   GLY A C   1 
ATOM   95   O  O   . GLY A 1 20  ? 25.806  -13.806 15.904  1.00 18.25 ? 8   GLY A O   1 
ATOM   96   N  N   . THR A 1 21  ? 26.434  -15.856 15.176  1.00 16.46 ? 9   THR A N   1 
ATOM   97   C  CA  . THR A 1 21  ? 26.467  -15.556 13.739  1.00 18.17 ? 9   THR A CA  1 
ATOM   98   C  C   . THR A 1 21  ? 25.723  -16.674 13.011  1.00 19.38 ? 9   THR A C   1 
ATOM   99   O  O   . THR A 1 21  ? 26.008  -17.853 13.242  1.00 21.20 ? 9   THR A O   1 
ATOM   100  C  CB  . THR A 1 21  ? 27.927  -15.361 13.283  1.00 19.79 ? 9   THR A CB  1 
ATOM   101  O  OG1 . THR A 1 21  ? 28.527  -14.220 13.926  1.00 19.74 ? 9   THR A OG1 1 
ATOM   102  C  CG2 . THR A 1 21  ? 27.990  -15.102 11.795  1.00 22.56 ? 9   THR A CG2 1 
ATOM   103  N  N   . ASN A 1 22  ? 24.761  -16.305 12.180  1.00 17.53 ? 10  ASN A N   1 
ATOM   104  C  CA  . ASN A 1 22  ? 23.817  -17.227 11.505  1.00 18.29 ? 10  ASN A CA  1 
ATOM   105  C  C   . ASN A 1 22  ? 23.743  -16.746 10.051  1.00 17.53 ? 10  ASN A C   1 
ATOM   106  O  O   . ASN A 1 22  ? 23.489  -15.544 9.821   1.00 15.98 ? 10  ASN A O   1 
ATOM   107  C  CB  . ASN A 1 22  ? 22.452  -17.230 12.203  1.00 18.65 ? 10  ASN A CB  1 
ATOM   108  C  CG  . ASN A 1 22  ? 21.378  -17.945 11.424  1.00 18.18 ? 10  ASN A CG  1 
ATOM   109  O  OD1 . ASN A 1 22  ? 20.687  -17.329 10.630  1.00 18.13 ? 10  ASN A OD1 1 
ATOM   110  N  ND2 . ASN A 1 22  ? 21.283  -19.277 11.567  1.00 17.54 ? 10  ASN A ND2 1 
ATOM   111  N  N   . ASN A 1 23  ? 24.119  -17.601 9.104   1.00 17.80 ? 11  ASN A N   1 
ATOM   112  C  CA  . ASN A 1 23  ? 24.019  -17.306 7.652   1.00 17.19 ? 11  ASN A CA  1 
ATOM   113  C  C   . ASN A 1 23  ? 24.845  -16.042 7.322   1.00 18.88 ? 11  ASN A C   1 
ATOM   114  O  O   . ASN A 1 23  ? 24.431  -15.293 6.419   1.00 22.09 ? 11  ASN A O   1 
ATOM   115  C  CB  . ASN A 1 23  ? 22.545  -17.250 7.217   1.00 18.96 ? 11  ASN A CB  1 
ATOM   116  C  CG  . ASN A 1 23  ? 21.862  -18.607 7.191   1.00 20.01 ? 11  ASN A CG  1 
ATOM   117  O  OD1 . ASN A 1 23  ? 22.363  -19.533 6.562   1.00 21.50 ? 11  ASN A OD1 1 
ATOM   118  N  ND2 . ASN A 1 23  ? 20.774  -18.783 7.924   1.00 19.27 ? 11  ASN A ND2 1 
ATOM   119  N  N   . GLY A 1 24  ? 25.986  -15.826 7.997   1.00 19.61 ? 12  GLY A N   1 
ATOM   120  C  CA  . GLY A 1 24  ? 26.922  -14.713 7.752   1.00 17.52 ? 12  GLY A CA  1 
ATOM   121  C  C   . GLY A 1 24  ? 26.528  -13.403 8.439   1.00 16.87 ? 12  GLY A C   1 
ATOM   122  O  O   . GLY A 1 24  ? 27.293  -12.434 8.378   1.00 17.74 ? 12  GLY A O   1 
ATOM   123  N  N   . TYR A 1 25  ? 25.412  -13.380 9.162   1.00 16.98 ? 13  TYR A N   1 
ATOM   124  C  CA  . TYR A 1 25  ? 24.969  -12.207 9.942   1.00 15.94 ? 13  TYR A CA  1 
ATOM   125  C  C   . TYR A 1 25  ? 25.128  -12.446 11.442  1.00 15.72 ? 13  TYR A C   1 
ATOM   126  O  O   . TYR A 1 25  ? 24.658  -13.493 12.001  1.00 17.88 ? 13  TYR A O   1 
ATOM   127  C  CB  . TYR A 1 25  ? 23.500  -11.905 9.653   1.00 16.35 ? 13  TYR A CB  1 
ATOM   128  C  CG  . TYR A 1 25  ? 23.332  -11.374 8.260   1.00 16.87 ? 13  TYR A CG  1 
ATOM   129  C  CD1 . TYR A 1 25  ? 23.436  -10.006 8.034   1.00 18.69 ? 13  TYR A CD1 1 
ATOM   130  C  CD2 . TYR A 1 25  ? 23.171  -12.200 7.174   1.00 19.68 ? 13  TYR A CD2 1 
ATOM   131  C  CE1 . TYR A 1 25  ? 23.338  -9.490  6.747   1.00 21.59 ? 13  TYR A CE1 1 
ATOM   132  C  CE2 . TYR A 1 25  ? 23.066  -11.701 5.882   1.00 20.48 ? 13  TYR A CE2 1 
ATOM   133  C  CZ  . TYR A 1 25  ? 23.155  -10.335 5.666   1.00 23.26 ? 13  TYR A CZ  1 
ATOM   134  O  OH  . TYR A 1 25  ? 23.103  -9.780  4.406   1.00 27.05 ? 13  TYR A OH  1 
ATOM   135  N  N   . TYR A 1 26  ? 25.659  -11.424 12.099  1.00 15.82 ? 14  TYR A N   1 
ATOM   136  C  CA  . TYR A 1 26  ? 25.649  -11.343 13.571  1.00 15.43 ? 14  TYR A CA  1 
ATOM   137  C  C   . TYR A 1 26  ? 24.183  -11.263 14.003  1.00 15.97 ? 14  TYR A C   1 
ATOM   138  O  O   . TYR A 1 26  ? 23.395  -10.643 13.301  1.00 16.79 ? 14  TYR A O   1 
ATOM   139  C  CB  . TYR A 1 26  ? 26.436  -10.142 14.072  1.00 16.83 ? 14  TYR A CB  1 
ATOM   140  C  CG  . TYR A 1 26  ? 26.445  -10.024 15.565  1.00 17.91 ? 14  TYR A CG  1 
ATOM   141  C  CD1 . TYR A 1 26  ? 27.220  -10.869 16.339  1.00 17.53 ? 14  TYR A CD1 1 
ATOM   142  C  CD2 . TYR A 1 26  ? 25.690  -9.046  16.201  1.00 15.90 ? 14  TYR A CD2 1 
ATOM   143  C  CE1 . TYR A 1 26  ? 27.241  -10.760 17.718  1.00 19.25 ? 14  TYR A CE1 1 
ATOM   144  C  CE2 . TYR A 1 26  ? 25.687  -8.950  17.584  1.00 18.30 ? 14  TYR A CE2 1 
ATOM   145  C  CZ  . TYR A 1 26  ? 26.500  -9.764  18.333  1.00 19.89 ? 14  TYR A CZ  1 
ATOM   146  O  OH  . TYR A 1 26  ? 26.526  -9.635  19.681  1.00 20.64 ? 14  TYR A OH  1 
ATOM   147  N  N   . TYR A 1 27  ? 23.824  -11.882 15.114  1.00 15.29 ? 15  TYR A N   1 
ATOM   148  C  CA  . TYR A 1 27  ? 22.476  -11.681 15.702  1.00 14.90 ? 15  TYR A CA  1 
ATOM   149  C  C   . TYR A 1 27  ? 22.634  -11.496 17.185  1.00 16.72 ? 15  TYR A C   1 
ATOM   150  O  O   . TYR A 1 27  ? 23.554  -12.098 17.771  1.00 14.54 ? 15  TYR A O   1 
ATOM   151  C  CB  . TYR A 1 27  ? 21.495  -12.802 15.428  1.00 15.84 ? 15  TYR A CB  1 
ATOM   152  C  CG  . TYR A 1 27  ? 21.787  -14.137 16.060  1.00 16.07 ? 15  TYR A CG  1 
ATOM   153  C  CD1 . TYR A 1 27  ? 22.638  -15.037 15.447  1.00 16.00 ? 15  TYR A CD1 1 
ATOM   154  C  CD2 . TYR A 1 27  ? 21.316  -14.445 17.325  1.00 17.24 ? 15  TYR A CD2 1 
ATOM   155  C  CE1 . TYR A 1 27  ? 22.930  -16.262 16.025  1.00 18.87 ? 15  TYR A CE1 1 
ATOM   156  C  CE2 . TYR A 1 27  ? 21.562  -15.690 17.906  1.00 18.05 ? 15  TYR A CE2 1 
ATOM   157  C  CZ  . TYR A 1 27  ? 22.419  -16.569 17.278  1.00 18.99 ? 15  TYR A CZ  1 
ATOM   158  O  OH  . TYR A 1 27  ? 22.683  -17.774 17.857  1.00 21.95 ? 15  TYR A OH  1 
ATOM   159  N  N   . SER A 1 28  ? 21.843  -10.563 17.726  1.00 16.64 ? 16  SER A N   1 
ATOM   160  C  CA  . SER A 1 28  ? 21.750  -10.353 19.180  1.00 15.60 ? 16  SER A CA  1 
ATOM   161  C  C   . SER A 1 28  ? 20.284  -10.521 19.555  1.00 15.87 ? 16  SER A C   1 
ATOM   162  O  O   . SER A 1 28  ? 19.438  -9.870  18.920  1.00 16.37 ? 16  SER A O   1 
ATOM   163  C  CB  . SER A 1 28  ? 22.281  -8.975  19.563  1.00 14.07 ? 16  SER A CB  1 
ATOM   164  O  OG  . SER A 1 28  ? 22.169  -8.789  20.976  1.00 15.25 ? 16  SER A OG  1 
ATOM   165  N  N   . PHE A 1 29  ? 20.003  -11.367 20.535  1.00 14.76 ? 17  PHE A N   1 
ATOM   166  C  CA  . PHE A 1 29  ? 18.657  -11.502 21.129  1.00 15.99 ? 17  PHE A CA  1 
ATOM   167  C  C   . PHE A 1 29  ? 18.854  -11.197 22.604  1.00 15.66 ? 17  PHE A C   1 
ATOM   168  O  O   . PHE A 1 29  ? 19.604  -11.943 23.280  1.00 16.16 ? 17  PHE A O   1 
ATOM   169  C  CB  . PHE A 1 29  ? 18.077  -12.899 20.945  1.00 17.18 ? 17  PHE A CB  1 
ATOM   170  C  CG  . PHE A 1 29  ? 16.741  -13.038 21.632  1.00 17.06 ? 17  PHE A CG  1 
ATOM   171  C  CD1 . PHE A 1 29  ? 15.696  -12.193 21.320  1.00 18.61 ? 17  PHE A CD1 1 
ATOM   172  C  CD2 . PHE A 1 29  ? 16.588  -13.899 22.698  1.00 18.36 ? 17  PHE A CD2 1 
ATOM   173  C  CE1 . PHE A 1 29  ? 14.484  -12.290 21.987  1.00 19.20 ? 17  PHE A CE1 1 
ATOM   174  C  CE2 . PHE A 1 29  ? 15.376  -14.005 23.362  1.00 20.68 ? 17  PHE A CE2 1 
ATOM   175  C  CZ  . PHE A 1 29  ? 14.324  -13.215 23.001  1.00 18.50 ? 17  PHE A CZ  1 
ATOM   176  N  N   . TRP A 1 30  ? 18.313  -10.063 23.072  1.00 15.83 ? 18  TRP A N   1 
ATOM   177  C  CA  . TRP A 1 30  ? 18.390  -9.758  24.524  1.00 16.43 ? 18  TRP A CA  1 
ATOM   178  C  C   . TRP A 1 30  ? 16.982  -9.626  25.082  1.00 16.13 ? 18  TRP A C   1 
ATOM   179  O  O   . TRP A 1 30  ? 16.155  -8.942  24.477  1.00 16.05 ? 18  TRP A O   1 
ATOM   180  C  CB  . TRP A 1 30  ? 19.230  -8.510  24.807  1.00 16.94 ? 18  TRP A CB  1 
ATOM   181  C  CG  . TRP A 1 30  ? 19.240  -8.188  26.266  1.00 17.26 ? 18  TRP A CG  1 
ATOM   182  C  CD1 . TRP A 1 30  ? 20.048  -8.717  27.232  1.00 18.07 ? 18  TRP A CD1 1 
ATOM   183  C  CD2 . TRP A 1 30  ? 18.392  -7.237  26.931  1.00 20.64 ? 18  TRP A CD2 1 
ATOM   184  N  NE1 . TRP A 1 30  ? 19.728  -8.192  28.468  1.00 18.12 ? 18  TRP A NE1 1 
ATOM   185  C  CE2 . TRP A 1 30  ? 18.762  -7.245  28.302  1.00 20.45 ? 18  TRP A CE2 1 
ATOM   186  C  CE3 . TRP A 1 30  ? 17.400  -6.345  26.498  1.00 20.67 ? 18  TRP A CE3 1 
ATOM   187  C  CZ2 . TRP A 1 30  ? 18.120  -6.426  29.240  1.00 20.61 ? 18  TRP A CZ2 1 
ATOM   188  C  CZ3 . TRP A 1 30  ? 16.748  -5.563  27.434  1.00 22.29 ? 18  TRP A CZ3 1 
ATOM   189  C  CH2 . TRP A 1 30  ? 17.128  -5.591  28.778  1.00 20.63 ? 18  TRP A CH2 1 
ATOM   190  N  N   . THR A 1 31  ? 16.684  -10.317 26.162  1.00 15.79 ? 19  THR A N   1 
ATOM   191  C  CA  . THR A 1 31  ? 15.406  -10.090 26.885  1.00 16.67 ? 19  THR A CA  1 
ATOM   192  C  C   . THR A 1 31  ? 15.692  -10.019 28.383  1.00 20.06 ? 19  THR A C   1 
ATOM   193  O  O   . THR A 1 31  ? 16.548  -10.829 28.859  1.00 21.04 ? 19  THR A O   1 
ATOM   194  C  CB  . THR A 1 31  ? 14.354  -11.139 26.527  1.00 18.72 ? 19  THR A CB  1 
ATOM   195  O  OG1 . THR A 1 31  ? 13.193  -10.809 27.317  1.00 17.90 ? 19  THR A OG1 1 
ATOM   196  C  CG2 . THR A 1 31  ? 14.815  -12.568 26.782  1.00 17.82 ? 19  THR A CG2 1 
ATOM   197  N  N   . ASP A 1 32  ? 14.943  -9.189  29.126  1.00 19.92 ? 20  ASP A N   1 
ATOM   198  C  CA  . ASP A 1 32  ? 15.034  -9.166  30.611  1.00 22.10 ? 20  ASP A CA  1 
ATOM   199  C  C   . ASP A 1 32  ? 14.300  -10.376 31.214  1.00 23.22 ? 20  ASP A C   1 
ATOM   200  O  O   . ASP A 1 32  ? 14.371  -10.515 32.448  1.00 24.36 ? 20  ASP A O   1 
ATOM   201  C  CB  . ASP A 1 32  ? 14.600  -7.815  31.172  1.00 23.05 ? 20  ASP A CB  1 
ATOM   202  C  CG  . ASP A 1 32  ? 13.124  -7.498  30.969  1.00 22.49 ? 20  ASP A CG  1 
ATOM   203  O  OD1 . ASP A 1 32  ? 12.396  -8.436  30.633  1.00 20.04 ? 20  ASP A OD1 1 
ATOM   204  O  OD2 . ASP A 1 32  ? 12.715  -6.309  31.202  1.00 23.92 ? 20  ASP A OD2 1 
ATOM   205  N  N   . GLY A 1 33  ? 13.607  -11.193 30.397  1.00 21.26 ? 21  GLY A N   1 
ATOM   206  C  CA  . GLY A 1 33  ? 12.916  -12.426 30.819  1.00 22.70 ? 21  GLY A CA  1 
ATOM   207  C  C   . GLY A 1 33  ? 11.439  -12.211 31.162  1.00 23.42 ? 21  GLY A C   1 
ATOM   208  O  O   . GLY A 1 33  ? 10.777  -13.176 31.549  1.00 25.16 ? 21  GLY A O   1 
ATOM   209  N  N   . GLY A 1 34  ? 10.895  -11.022 30.954  1.00 21.68 ? 22  GLY A N   1 
ATOM   210  C  CA  . GLY A 1 34  ? 9.459   -10.759 31.173  1.00 23.15 ? 22  GLY A CA  1 
ATOM   211  C  C   . GLY A 1 34  ? 8.571   -11.360 30.088  1.00 22.08 ? 22  GLY A C   1 
ATOM   212  O  O   . GLY A 1 34  ? 8.969   -11.433 28.895  1.00 20.47 ? 22  GLY A O   1 
ATOM   213  N  N   . GLY A 1 35  ? 7.355   -11.739 30.454  1.00 21.46 ? 23  GLY A N   1 
ATOM   214  C  CA  . GLY A 1 35  ? 6.375   -12.275 29.500  1.00 23.18 ? 23  GLY A CA  1 
ATOM   215  C  C   . GLY A 1 35  ? 6.958   -13.416 28.693  1.00 24.32 ? 23  GLY A C   1 
ATOM   216  O  O   . GLY A 1 35  ? 7.798   -14.167 29.248  1.00 21.02 ? 23  GLY A O   1 
ATOM   217  N  N   . GLN A 1 36  ? 6.602   -13.492 27.410  1.00 20.59 ? 24  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 36  ? 7.131   -14.497 26.471  1.00 22.84 ? 24  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 36  ? 7.714   -13.764 25.269  1.00 20.01 ? 24  GLN A C   1 
ATOM   220  O  O   . GLN A 1 36  ? 6.998   -12.951 24.668  1.00 19.79 ? 24  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 36  ? 6.047   -15.480 26.031  1.00 25.80 ? 24  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 36  ? 5.651   -16.472 27.118  1.00 33.15 ? 24  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 36  ? 4.199   -16.884 27.043  1.00 38.17 ? 24  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 36  ? 3.575   -17.164 28.069  1.00 44.06 ? 24  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 36  ? 3.640   -16.926 25.836  1.00 39.10 ? 24  GLN A NE2 1 
ATOM   226  N  N   . VAL A 1 37  ? 8.996   -13.966 24.997  1.00 17.91 ? 25  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 37  ? 9.626   -13.383 23.783  1.00 18.29 ? 25  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 37  ? 10.292  -14.530 23.030  1.00 19.43 ? 25  VAL A C   1 
ATOM   229  O  O   . VAL A 1 37  ? 11.123  -15.253 23.641  1.00 20.63 ? 25  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 37  ? 10.576  -12.213 24.107  1.00 17.82 ? 25  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 37  ? 11.144  -11.582 22.833  1.00 17.02 ? 25  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 37  ? 9.929   -11.164 24.988  1.00 17.10 ? 25  VAL A CG2 1 
ATOM   233  N  N   . THR A 1 38  ? 9.890   -14.756 21.783  1.00 17.51 ? 26  THR A N   1 
ATOM   234  C  CA  . THR A 1 38  ? 10.400  -15.902 20.992  1.00 17.68 ? 26  THR A CA  1 
ATOM   235  C  C   . THR A 1 38  ? 11.069  -15.369 19.727  1.00 17.15 ? 26  THR A C   1 
ATOM   236  O  O   . THR A 1 38  ? 10.393  -14.774 18.917  1.00 19.40 ? 26  THR A O   1 
ATOM   237  C  CB  . THR A 1 38  ? 9.290   -16.903 20.680  1.00 21.78 ? 26  THR A CB  1 
ATOM   238  O  OG1 . THR A 1 38  ? 8.723   -17.382 21.906  1.00 24.48 ? 26  THR A OG1 1 
ATOM   239  C  CG2 . THR A 1 38  ? 9.815   -18.066 19.876  1.00 22.78 ? 26  THR A CG2 1 
ATOM   240  N  N   . TYR A 1 39  ? 12.343  -15.653 19.554  1.00 15.80 ? 27  TYR A N   1 
ATOM   241  C  CA  . TYR A 1 39  ? 13.154  -15.205 18.404  1.00 14.29 ? 27  TYR A CA  1 
ATOM   242  C  C   . TYR A 1 39  ? 13.549  -16.403 17.533  1.00 16.35 ? 27  TYR A C   1 
ATOM   243  O  O   . TYR A 1 39  ? 13.872  -17.457 18.064  1.00 16.50 ? 27  TYR A O   1 
ATOM   244  C  CB  . TYR A 1 39  ? 14.384  -14.537 18.976  1.00 14.30 ? 27  TYR A CB  1 
ATOM   245  C  CG  . TYR A 1 39  ? 15.390  -14.134 17.925  1.00 13.63 ? 27  TYR A CG  1 
ATOM   246  C  CD1 . TYR A 1 39  ? 15.391  -12.852 17.433  1.00 12.82 ? 27  TYR A CD1 1 
ATOM   247  C  CD2 . TYR A 1 39  ? 16.428  -14.948 17.551  1.00 15.45 ? 27  TYR A CD2 1 
ATOM   248  C  CE1 . TYR A 1 39  ? 16.314  -12.431 16.484  1.00 14.71 ? 27  TYR A CE1 1 
ATOM   249  C  CE2 . TYR A 1 39  ? 17.361  -14.560 16.595  1.00 15.15 ? 27  TYR A CE2 1 
ATOM   250  C  CZ  . TYR A 1 39  ? 17.314  -13.276 16.065  1.00 15.68 ? 27  TYR A CZ  1 
ATOM   251  O  OH  . TYR A 1 39  ? 18.233  -12.880 15.126  1.00 15.33 ? 27  TYR A OH  1 
ATOM   252  N  N   . THR A 1 40  ? 13.577  -16.225 16.212  1.00 16.45 ? 28  THR A N   1 
ATOM   253  C  CA  . THR A 1 40  ? 14.093  -17.245 15.270  1.00 17.35 ? 28  THR A CA  1 
ATOM   254  C  C   . THR A 1 40  ? 14.969  -16.582 14.209  1.00 17.23 ? 28  THR A C   1 
ATOM   255  O  O   . THR A 1 40  ? 14.620  -15.481 13.690  1.00 17.28 ? 28  THR A O   1 
ATOM   256  C  CB  . THR A 1 40  ? 12.995  -18.089 14.604  1.00 20.29 ? 28  THR A CB  1 
ATOM   257  O  OG1 . THR A 1 40  ? 12.094  -17.238 13.894  1.00 21.67 ? 28  THR A OG1 1 
ATOM   258  C  CG2 . THR A 1 40  ? 12.205  -18.911 15.594  1.00 22.33 ? 28  THR A CG2 1 
ATOM   259  N  N   . ASN A 1 41  ? 16.068  -17.254 13.884  1.00 15.59 ? 29  ASN A N   1 
ATOM   260  C  CA  . ASN A 1 41  ? 16.895  -16.905 12.703  1.00 15.89 ? 29  ASN A CA  1 
ATOM   261  C  C   . ASN A 1 41  ? 16.312  -17.587 11.462  1.00 17.97 ? 29  ASN A C   1 
ATOM   262  O  O   . ASN A 1 41  ? 16.089  -18.853 11.502  1.00 21.38 ? 29  ASN A O   1 
ATOM   263  C  CB  . ASN A 1 41  ? 18.354  -17.286 12.914  1.00 16.13 ? 29  ASN A CB  1 
ATOM   264  C  CG  . ASN A 1 41  ? 19.077  -16.367 13.865  1.00 17.71 ? 29  ASN A CG  1 
ATOM   265  O  OD1 . ASN A 1 41  ? 18.978  -15.144 13.767  1.00 17.18 ? 29  ASN A OD1 1 
ATOM   266  N  ND2 . ASN A 1 41  ? 19.821  -16.948 14.785  1.00 18.56 ? 29  ASN A ND2 1 
ATOM   267  N  N   . GLY A 1 42  ? 16.177  -16.811 10.397  1.00 15.99 ? 30  GLY A N   1 
ATOM   268  C  CA  . GLY A 1 42  ? 15.801  -17.280 9.068   1.00 17.36 ? 30  GLY A CA  1 
ATOM   269  C  C   . GLY A 1 42  ? 16.998  -17.361 8.146   1.00 16.88 ? 30  GLY A C   1 
ATOM   270  O  O   . GLY A 1 42  ? 18.135  -17.107 8.549   1.00 17.89 ? 30  GLY A O   1 
ATOM   271  N  N   . PRO A 1 43  ? 16.730  -17.683 6.863   1.00 17.54 ? 31  PRO A N   1 
ATOM   272  C  CA  . PRO A 1 43  ? 17.785  -17.715 5.858   1.00 18.59 ? 31  PRO A CA  1 
ATOM   273  C  C   . PRO A 1 43  ? 18.371  -16.309 5.701   1.00 20.42 ? 31  PRO A C   1 
ATOM   274  O  O   . PRO A 1 43  ? 17.651  -15.356 5.935   1.00 20.24 ? 31  PRO A O   1 
ATOM   275  C  CB  . PRO A 1 43  ? 17.099  -18.189 4.582   1.00 20.58 ? 31  PRO A CB  1 
ATOM   276  C  CG  . PRO A 1 43  ? 15.605  -18.146 4.848   1.00 21.64 ? 31  PRO A CG  1 
ATOM   277  C  CD  . PRO A 1 43  ? 15.393  -17.976 6.337   1.00 20.26 ? 31  PRO A CD  1 
ATOM   278  N  N   . ALA A 1 44  ? 19.642  -16.225 5.298   1.00 19.97 ? 32  ALA A N   1 
ATOM   279  C  CA  . ALA A 1 44  ? 20.356  -14.977 4.964   1.00 20.33 ? 32  ALA A CA  1 
ATOM   280  C  C   . ALA A 1 44  ? 20.164  -13.993 6.125   1.00 20.48 ? 32  ALA A C   1 
ATOM   281  O  O   . ALA A 1 44  ? 20.432  -14.381 7.274   1.00 18.14 ? 32  ALA A O   1 
ATOM   282  C  CB  . ALA A 1 44  ? 19.918  -14.481 3.601   1.00 21.88 ? 32  ALA A CB  1 
ATOM   283  N  N   . GLY A 1 45  ? 19.728  -12.762 5.874   1.00 18.84 ? 33  GLY A N   1 
ATOM   284  C  CA  . GLY A 1 45  ? 19.668  -11.753 6.944   1.00 15.89 ? 33  GLY A CA  1 
ATOM   285  C  C   . GLY A 1 45  ? 18.309  -11.714 7.630   1.00 13.44 ? 33  GLY A C   1 
ATOM   286  O  O   . GLY A 1 45  ? 17.992  -10.674 8.206   1.00 15.05 ? 33  GLY A O   1 
ATOM   287  N  N   . GLN A 1 46  ? 17.512  -12.775 7.556   1.00 15.51 ? 34  GLN A N   1 
ATOM   288  C  CA  . GLN A 1 46  ? 16.107  -12.770 8.079   1.00 15.56 ? 34  GLN A CA  1 
ATOM   289  C  C   . GLN A 1 46  ? 16.139  -13.130 9.567   1.00 14.78 ? 34  GLN A C   1 
ATOM   290  O  O   . GLN A 1 46  ? 16.812  -14.136 9.956   1.00 14.89 ? 34  GLN A O   1 
ATOM   291  C  CB  . GLN A 1 46  ? 15.212  -13.728 7.303   1.00 17.84 ? 34  GLN A CB  1 
ATOM   292  C  CG  . GLN A 1 46  ? 13.706  -13.562 7.505   1.00 19.54 ? 34  GLN A CG  1 
ATOM   293  C  CD  . GLN A 1 46  ? 13.092  -14.250 8.708   1.00 19.34 ? 34  GLN A CD  1 
ATOM   294  O  OE1 . GLN A 1 46  ? 13.726  -14.988 9.450   1.00 20.64 ? 34  GLN A OE1 1 
ATOM   295  N  NE2 . GLN A 1 46  ? 11.824  -13.966 8.948   1.00 20.67 ? 34  GLN A NE2 1 
ATOM   296  N  N   . TYR A 1 47  ? 15.274  -12.470 10.338  1.00 14.42 ? 35  TYR A N   1 
ATOM   297  C  CA  . TYR A 1 47  ? 14.863  -12.929 11.677  1.00 14.14 ? 35  TYR A CA  1 
ATOM   298  C  C   . TYR A 1 47  ? 13.385  -12.644 11.896  1.00 14.21 ? 35  TYR A C   1 
ATOM   299  O  O   . TYR A 1 47  ? 12.805  -11.736 11.272  1.00 15.40 ? 35  TYR A O   1 
ATOM   300  C  CB  . TYR A 1 47  ? 15.749  -12.303 12.740  1.00 13.62 ? 35  TYR A CB  1 
ATOM   301  C  CG  . TYR A 1 47  ? 15.478  -10.854 13.012  1.00 13.15 ? 35  TYR A CG  1 
ATOM   302  C  CD1 . TYR A 1 47  ? 16.131  -9.880  12.288  1.00 12.06 ? 35  TYR A CD1 1 
ATOM   303  C  CD2 . TYR A 1 47  ? 14.531  -10.468 13.946  1.00 12.65 ? 35  TYR A CD2 1 
ATOM   304  C  CE1 . TYR A 1 47  ? 15.863  -8.539  12.502  1.00 12.55 ? 35  TYR A CE1 1 
ATOM   305  C  CE2 . TYR A 1 47  ? 14.275  -9.133  14.188  1.00 12.12 ? 35  TYR A CE2 1 
ATOM   306  C  CZ  . TYR A 1 47  ? 14.939  -8.173  13.461  1.00 12.99 ? 35  TYR A CZ  1 
ATOM   307  O  OH  . TYR A 1 47  ? 14.725  -6.868  13.710  1.00 13.60 ? 35  TYR A OH  1 
ATOM   308  N  N   . SER A 1 48  ? 12.810  -13.406 12.808  1.00 15.48 ? 36  SER A N   1 
ATOM   309  C  CA  . SER A 1 48  ? 11.428  -13.234 13.314  1.00 15.72 ? 36  SER A CA  1 
ATOM   310  C  C   . SER A 1 48  ? 11.426  -13.139 14.830  1.00 15.65 ? 36  SER A C   1 
ATOM   311  O  O   . SER A 1 48  ? 12.292  -13.725 15.496  1.00 14.10 ? 36  SER A O   1 
ATOM   312  C  CB  . SER A 1 48  ? 10.570  -14.363 12.837  1.00 19.09 ? 36  SER A CB  1 
ATOM   313  O  OG  . SER A 1 48  ? 10.161  -14.144 11.489  1.00 22.13 ? 36  SER A OG  1 
ATOM   314  N  N   . VAL A 1 49  ? 10.561  -12.282 15.358  1.00 15.94 ? 37  VAL A N   1 
ATOM   315  C  CA  . VAL A 1 49  ? 10.382  -12.193 16.811  1.00 14.98 ? 37  VAL A CA  1 
ATOM   316  C  C   . VAL A 1 49  ? 8.878   -12.117 17.058  1.00 16.57 ? 37  VAL A C   1 
ATOM   317  O  O   . VAL A 1 49  ? 8.160   -11.429 16.286  1.00 16.64 ? 37  VAL A O   1 
ATOM   318  C  CB  . VAL A 1 49  ? 11.223  -11.072 17.453  1.00 16.08 ? 37  VAL A CB  1 
ATOM   319  C  CG1 . VAL A 1 49  ? 10.896  -9.684  16.936  1.00 16.21 ? 37  VAL A CG1 1 
ATOM   320  C  CG2 . VAL A 1 49  ? 11.103  -11.082 18.982  1.00 15.74 ? 37  VAL A CG2 1 
ATOM   321  N  N   . GLU A 1 50  ? 8.408   -12.837 18.073  1.00 17.11 ? 38  GLU A N   1 
ATOM   322  C  CA  . GLU A 1 50  ? 6.973   -12.863 18.477  1.00 18.98 ? 38  GLU A CA  1 
ATOM   323  C  C   . GLU A 1 50  ? 6.976   -12.595 19.977  1.00 18.15 ? 38  GLU A C   1 
ATOM   324  O  O   . GLU A 1 50  ? 7.798   -13.237 20.672  1.00 17.14 ? 38  GLU A O   1 
ATOM   325  C  CB  . GLU A 1 50  ? 6.273   -14.220 18.258  1.00 25.23 ? 38  GLU A CB  1 
ATOM   326  C  CG  . GLU A 1 50  ? 6.370   -14.802 16.865  1.00 28.98 ? 38  GLU A CG  1 
ATOM   327  C  CD  . GLU A 1 50  ? 5.076   -15.376 16.297  1.00 35.75 ? 38  GLU A CD  1 
ATOM   328  O  OE1 . GLU A 1 50  ? 5.026   -15.570 15.064  1.00 44.25 ? 38  GLU A OE1 1 
ATOM   329  O  OE2 . GLU A 1 50  ? 4.115   -15.611 17.081  1.00 40.83 ? 38  GLU A OE2 1 
ATOM   330  N  N   . TRP A 1 51  ? 6.202   -11.637 20.476  1.00 15.72 ? 39  TRP A N   1 
ATOM   331  C  CA  . TRP A 1 51  ? 6.211   -11.369 21.936  1.00 13.41 ? 39  TRP A CA  1 
ATOM   332  C  C   . TRP A 1 51  ? 4.813   -11.177 22.501  1.00 14.16 ? 39  TRP A C   1 
ATOM   333  O  O   . TRP A 1 51  ? 3.871   -10.858 21.768  1.00 14.86 ? 39  TRP A O   1 
ATOM   334  C  CB  . TRP A 1 51  ? 7.151   -10.246 22.269  1.00 15.02 ? 39  TRP A CB  1 
ATOM   335  C  CG  . TRP A 1 51  ? 6.761   -8.890  21.785  1.00 14.28 ? 39  TRP A CG  1 
ATOM   336  C  CD1 . TRP A 1 51  ? 6.267   -7.882  22.554  1.00 15.65 ? 39  TRP A CD1 1 
ATOM   337  C  CD2 . TRP A 1 51  ? 6.958   -8.327  20.467  1.00 14.58 ? 39  TRP A CD2 1 
ATOM   338  N  NE1 . TRP A 1 51  ? 6.140   -6.733  21.830  1.00 15.53 ? 39  TRP A NE1 1 
ATOM   339  C  CE2 . TRP A 1 51  ? 6.567   -6.972  20.548  1.00 14.95 ? 39  TRP A CE2 1 
ATOM   340  C  CE3 . TRP A 1 51  ? 7.490   -8.808  19.257  1.00 14.89 ? 39  TRP A CE3 1 
ATOM   341  C  CZ2 . TRP A 1 51  ? 6.587   -6.136  19.432  1.00 15.78 ? 39  TRP A CZ2 1 
ATOM   342  C  CZ3 . TRP A 1 51  ? 7.520   -7.978  18.161  1.00 15.57 ? 39  TRP A CZ3 1 
ATOM   343  C  CH2 . TRP A 1 51  ? 7.135   -6.631  18.268  1.00 15.69 ? 39  TRP A CH2 1 
ATOM   344  N  N   . SER A 1 52  ? 4.706   -11.443 23.792  1.00 15.58 ? 40  SER A N   1 
ATOM   345  C  CA  . SER A 1 52  ? 3.412   -11.435 24.513  1.00 16.33 ? 40  SER A CA  1 
ATOM   346  C  C   . SER A 1 52  ? 3.652   -10.891 25.919  1.00 15.55 ? 40  SER A C   1 
ATOM   347  O  O   . SER A 1 52  ? 4.420   -11.508 26.643  1.00 17.33 ? 40  SER A O   1 
ATOM   348  C  CB  . SER A 1 52  ? 2.841   -12.842 24.542  1.00 18.58 ? 40  SER A CB  1 
ATOM   349  O  OG  . SER A 1 52  ? 1.678   -12.866 25.351  1.00 26.29 ? 40  SER A OG  1 
ATOM   350  N  N   . ASN A 1 53  ? 3.060   -9.736  26.261  1.00 16.65 ? 41  ASN A N   1 
ATOM   351  C  CA  . ASN A 1 53  ? 3.166   -9.086  27.594  1.00 16.74 ? 41  ASN A CA  1 
ATOM   352  C  C   . ASN A 1 53  ? 4.619   -9.034  28.042  1.00 14.37 ? 41  ASN A C   1 
ATOM   353  O  O   . ASN A 1 53  ? 4.944   -9.396  29.172  1.00 16.70 ? 41  ASN A O   1 
ATOM   354  C  CB  . ASN A 1 53  ? 2.281   -9.806  28.610  1.00 18.63 ? 41  ASN A CB  1 
ATOM   355  C  CG  . ASN A 1 53  ? 0.817   -9.693  28.263  1.00 20.95 ? 41  ASN A CG  1 
ATOM   356  O  OD1 . ASN A 1 53  ? 0.319   -8.590  28.091  1.00 18.76 ? 41  ASN A OD1 1 
ATOM   357  N  ND2 . ASN A 1 53  ? 0.118   -10.813 28.194  1.00 20.70 ? 41  ASN A ND2 1 
ATOM   358  N  N   . SER A 1 54  ? 5.510   -8.672  27.137  1.00 13.39 ? 42  SER A N   1 
ATOM   359  C  CA  . SER A 1 54  ? 6.960   -8.727  27.341  1.00 13.19 ? 42  SER A CA  1 
ATOM   360  C  C   . SER A 1 54  ? 7.409   -7.798  28.458  1.00 14.24 ? 42  SER A C   1 
ATOM   361  O  O   . SER A 1 54  ? 6.738   -6.764  28.732  1.00 14.70 ? 42  SER A O   1 
ATOM   362  C  CB  . SER A 1 54  ? 7.674   -8.359  26.047  1.00 12.56 ? 42  SER A CB  1 
ATOM   363  O  OG  . SER A 1 54  ? 7.532   -6.964  25.759  1.00 13.86 ? 42  SER A OG  1 
ATOM   364  N  N   . GLY A 1 55  ? 8.599   -8.054  28.970  1.00 16.06 ? 43  GLY A N   1 
ATOM   365  C  CA  . GLY A 1 55  ? 9.378   -6.987  29.604  1.00 17.03 ? 43  GLY A CA  1 
ATOM   366  C  C   . GLY A 1 55  ? 10.098  -6.160  28.544  1.00 19.87 ? 43  GLY A C   1 
ATOM   367  O  O   . GLY A 1 55  ? 9.518   -5.867  27.475  1.00 19.58 ? 43  GLY A O   1 
ATOM   368  N  N   . ASN A 1 56  ? 11.356  -5.826  28.802  1.00 16.56 ? 44  ASN A N   1 
ATOM   369  C  CA  . ASN A 1 56  ? 12.234  -5.174  27.803  1.00 18.87 ? 44  ASN A CA  1 
ATOM   370  C  C   . ASN A 1 56  ? 12.929  -6.235  26.944  1.00 17.97 ? 44  ASN A C   1 
ATOM   371  O  O   . ASN A 1 56  ? 13.485  -7.212  27.482  1.00 15.96 ? 44  ASN A O   1 
ATOM   372  C  CB  . ASN A 1 56  ? 13.275  -4.271  28.476  1.00 21.44 ? 44  ASN A CB  1 
ATOM   373  C  CG  . ASN A 1 56  ? 12.733  -2.924  28.908  1.00 29.11 ? 44  ASN A CG  1 
ATOM   374  O  OD1 . ASN A 1 56  ? 12.613  -2.652  30.103  1.00 38.63 ? 44  ASN A OD1 1 
ATOM   375  N  ND2 . ASN A 1 56  ? 12.408  -2.069  27.951  1.00 33.50 ? 44  ASN A ND2 1 
ATOM   376  N  N   . PHE A 1 57  ? 12.966  -6.044  25.638  1.00 15.24 ? 45  PHE A N   1 
ATOM   377  C  CA  . PHE A 1 57  ? 13.768  -6.920  24.776  1.00 14.66 ? 45  PHE A CA  1 
ATOM   378  C  C   . PHE A 1 57  ? 14.246  -6.086  23.597  1.00 15.37 ? 45  PHE A C   1 
ATOM   379  O  O   . PHE A 1 57  ? 13.605  -5.091  23.198  1.00 14.41 ? 45  PHE A O   1 
ATOM   380  C  CB  . PHE A 1 57  ? 12.991  -8.143  24.276  1.00 14.49 ? 45  PHE A CB  1 
ATOM   381  C  CG  . PHE A 1 57  ? 11.995  -7.883  23.186  1.00 12.69 ? 45  PHE A CG  1 
ATOM   382  C  CD1 . PHE A 1 57  ? 12.380  -7.905  21.848  1.00 12.76 ? 45  PHE A CD1 1 
ATOM   383  C  CD2 . PHE A 1 57  ? 10.688  -7.600  23.497  1.00 13.75 ? 45  PHE A CD2 1 
ATOM   384  C  CE1 . PHE A 1 57  ? 11.440  -7.745  20.853  1.00 13.90 ? 45  PHE A CE1 1 
ATOM   385  C  CE2 . PHE A 1 57  ? 9.752   -7.443  22.500  1.00 15.23 ? 45  PHE A CE2 1 
ATOM   386  C  CZ  . PHE A 1 57  ? 10.146  -7.463  21.184  1.00 15.54 ? 45  PHE A CZ  1 
ATOM   387  N  N   . VAL A 1 58  ? 15.331  -6.551  22.990  1.00 15.38 ? 46  VAL A N   1 
ATOM   388  C  CA  . VAL A 1 58  ? 15.895  -5.923  21.769  1.00 16.20 ? 46  VAL A CA  1 
ATOM   389  C  C   . VAL A 1 58  ? 16.506  -7.057  20.969  1.00 18.10 ? 46  VAL A C   1 
ATOM   390  O  O   . VAL A 1 58  ? 17.339  -7.785  21.554  1.00 16.47 ? 46  VAL A O   1 
ATOM   391  C  CB  . VAL A 1 58  ? 16.958  -4.851  22.068  1.00 19.33 ? 46  VAL A CB  1 
ATOM   392  C  CG1 . VAL A 1 58  ? 17.528  -4.324  20.762  1.00 19.15 ? 46  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A 1 58  ? 16.438  -3.737  22.943  1.00 21.15 ? 46  VAL A CG2 1 
ATOM   394  N  N   . ALA A 1 59  ? 16.131  -7.209  19.695  1.00 14.92 ? 47  ALA A N   1 
ATOM   395  C  CA  . ALA A 1 59  ? 16.609  -8.363  18.925  1.00 14.78 ? 47  ALA A CA  1 
ATOM   396  C  C   . ALA A 1 59  ? 16.802  -8.031  17.462  1.00 14.89 ? 47  ALA A C   1 
ATOM   397  O  O   . ALA A 1 59  ? 15.964  -7.226  16.919  1.00 14.57 ? 47  ALA A O   1 
ATOM   398  C  CB  . ALA A 1 59  ? 15.625  -9.434  19.057  1.00 14.76 ? 47  ALA A CB  1 
ATOM   399  N  N   . GLY A 1 60  ? 17.816  -8.641  16.866  1.00 12.84 ? 48  GLY A N   1 
ATOM   400  C  CA  . GLY A 1 60  ? 17.950  -8.600  15.402  1.00 12.35 ? 48  GLY A CA  1 
ATOM   401  C  C   . GLY A 1 60  ? 19.307  -8.995  14.886  1.00 11.60 ? 48  GLY A C   1 
ATOM   402  O  O   . GLY A 1 60  ? 20.163  -9.348  15.691  1.00 13.64 ? 48  GLY A O   1 
ATOM   403  N  N   . LYS A 1 61  ? 19.460  -8.831  13.589  1.00 12.53 ? 49  LYS A N   1 
ATOM   404  C  CA  . LYS A 1 61  ? 20.637  -9.208  12.759  1.00 13.36 ? 49  LYS A CA  1 
ATOM   405  C  C   . LYS A 1 61  ? 21.358  -7.979  12.172  1.00 13.83 ? 49  LYS A C   1 
ATOM   406  O  O   . LYS A 1 61  ? 20.758  -6.903  11.908  1.00 13.00 ? 49  LYS A O   1 
ATOM   407  C  CB  . LYS A 1 61  ? 20.234  -10.152 11.615  1.00 13.47 ? 49  LYS A CB  1 
ATOM   408  C  CG  . LYS A 1 61  ? 20.168  -11.655 11.914  1.00 14.25 ? 49  LYS A CG  1 
ATOM   409  C  CD  . LYS A 1 61  ? 19.758  -12.467 10.739  1.00 14.81 ? 49  LYS A CD  1 
ATOM   410  C  CE  . LYS A 1 61  ? 20.106  -13.930 10.908  1.00 15.57 ? 49  LYS A CE  1 
ATOM   411  N  NZ  . LYS A 1 61  ? 19.627  -14.708 9.750   1.00 15.96 ? 49  LYS A NZ  1 
ATOM   412  N  N   . GLY A 1 62  ? 22.663  -8.150  11.952  1.00 14.82 ? 50  GLY A N   1 
ATOM   413  C  CA  . GLY A 1 62  ? 23.516  -7.139  11.340  1.00 14.90 ? 50  GLY A CA  1 
ATOM   414  C  C   . GLY A 1 62  ? 24.962  -7.586  11.357  1.00 15.11 ? 50  GLY A C   1 
ATOM   415  O  O   . GLY A 1 62  ? 25.223  -8.750  10.918  1.00 15.39 ? 50  GLY A O   1 
ATOM   416  N  N   . TRP A 1 63  ? 25.813  -6.814  11.999  1.00 16.17 ? 51  TRP A N   1 
ATOM   417  C  CA  . TRP A 1 63  ? 27.289  -6.975  11.922  1.00 18.20 ? 51  TRP A CA  1 
ATOM   418  C  C   . TRP A 1 63  ? 27.922  -6.769  13.288  1.00 18.30 ? 51  TRP A C   1 
ATOM   419  O  O   . TRP A 1 63  ? 27.382  -6.016  14.106  1.00 16.76 ? 51  TRP A O   1 
ATOM   420  C  CB  . TRP A 1 63  ? 27.897  -6.005  10.906  1.00 18.77 ? 51  TRP A CB  1 
ATOM   421  C  CG  . TRP A 1 63  ? 27.282  -6.138  9.557   1.00 21.13 ? 51  TRP A CG  1 
ATOM   422  C  CD1 . TRP A 1 63  ? 27.756  -6.835  8.491   1.00 25.22 ? 51  TRP A CD1 1 
ATOM   423  C  CD2 . TRP A 1 63  ? 26.039  -5.560  9.138   1.00 22.13 ? 51  TRP A CD2 1 
ATOM   424  N  NE1 . TRP A 1 63  ? 26.877  -6.755  7.449   1.00 25.67 ? 51  TRP A NE1 1 
ATOM   425  C  CE2 . TRP A 1 63  ? 25.836  -5.954  7.805   1.00 24.63 ? 51  TRP A CE2 1 
ATOM   426  C  CE3 . TRP A 1 63  ? 25.116  -4.706  9.746   1.00 21.86 ? 51  TRP A CE3 1 
ATOM   427  C  CZ2 . TRP A 1 63  ? 24.715  -5.568  7.078   1.00 25.00 ? 51  TRP A CZ2 1 
ATOM   428  C  CZ3 . TRP A 1 63  ? 24.009  -4.316  9.023   1.00 22.77 ? 51  TRP A CZ3 1 
ATOM   429  C  CH2 . TRP A 1 63  ? 23.827  -4.724  7.702   1.00 24.27 ? 51  TRP A CH2 1 
ATOM   430  N  N   . ASN A 1 64  ? 29.063  -7.412  13.517  1.00 17.60 ? 52  ASN A N   1 
ATOM   431  C  CA  . ASN A 1 64  ? 29.828  -7.194  14.763  1.00 18.49 ? 52  ASN A CA  1 
ATOM   432  C  C   . ASN A 1 64  ? 31.304  -7.396  14.411  1.00 17.70 ? 52  ASN A C   1 
ATOM   433  O  O   . ASN A 1 64  ? 31.741  -8.530  14.248  1.00 19.58 ? 52  ASN A O   1 
ATOM   434  C  CB  . ASN A 1 64  ? 29.395  -8.119  15.910  1.00 19.08 ? 52  ASN A CB  1 
ATOM   435  C  CG  . ASN A 1 64  ? 30.032  -7.677  17.214  1.00 20.92 ? 52  ASN A CG  1 
ATOM   436  O  OD1 . ASN A 1 64  ? 30.675  -6.631  17.253  1.00 20.13 ? 52  ASN A OD1 1 
ATOM   437  N  ND2 . ASN A 1 64  ? 29.888  -8.447  18.280  1.00 25.18 ? 52  ASN A ND2 1 
ATOM   438  N  N   . PRO A 1 65  ? 32.090  -6.329  14.289  1.00 18.96 ? 53  PRO A N   1 
ATOM   439  C  CA  . PRO A 1 65  ? 31.619  -4.980  14.588  1.00 17.71 ? 53  PRO A CA  1 
ATOM   440  C  C   . PRO A 1 65  ? 30.858  -4.359  13.414  1.00 19.29 ? 53  PRO A C   1 
ATOM   441  O  O   . PRO A 1 65  ? 31.080  -4.774  12.264  1.00 18.36 ? 53  PRO A O   1 
ATOM   442  C  CB  . PRO A 1 65  ? 32.945  -4.264  14.857  1.00 20.76 ? 53  PRO A CB  1 
ATOM   443  C  CG  . PRO A 1 65  ? 33.864  -4.858  13.852  1.00 20.00 ? 53  PRO A CG  1 
ATOM   444  C  CD  . PRO A 1 65  ? 33.521  -6.345  13.901  1.00 20.69 ? 53  PRO A CD  1 
ATOM   445  N  N   . GLY A 1 66  ? 30.093  -3.302  13.696  1.00 19.52 ? 54  GLY A N   1 
ATOM   446  C  CA  . GLY A 1 66  ? 29.526  -2.425  12.676  1.00 20.19 ? 54  GLY A CA  1 
ATOM   447  C  C   . GLY A 1 66  ? 30.627  -1.602  12.017  1.00 19.76 ? 54  GLY A C   1 
ATOM   448  O  O   . GLY A 1 66  ? 31.684  -1.346  12.667  1.00 18.32 ? 54  GLY A O   1 
ATOM   449  N  N   . SER A 1 67  ? 30.478  -1.304  10.732  1.00 19.47 ? 55  SER A N   1 
ATOM   450  C  CA  . SER A 1 67  ? 31.460  -0.424  10.053  1.00 23.67 ? 55  SER A CA  1 
ATOM   451  C  C   . SER A 1 67  ? 30.765  0.676   9.255   1.00 22.53 ? 55  SER A C   1 
ATOM   452  O  O   . SER A 1 67  ? 31.231  0.976   8.151   1.00 25.78 ? 55  SER A O   1 
ATOM   453  C  CB  . SER A 1 67  ? 32.426  -1.209  9.227   1.00 25.46 ? 55  SER A CB  1 
ATOM   454  O  OG  . SER A 1 67  ? 31.774  -1.967  8.250   1.00 29.17 ? 55  SER A OG  1 
ATOM   455  N  N   . SER A 1 68  ? 29.734  1.284   9.823   1.00 22.08 ? 56  SER A N   1 
ATOM   456  C  CA  . SER A 1 68  ? 29.088  2.515   9.298   1.00 23.78 ? 56  SER A CA  1 
ATOM   457  C  C   . SER A 1 68  ? 28.554  2.271   7.887   1.00 24.50 ? 56  SER A C   1 
ATOM   458  O  O   . SER A 1 68  ? 28.604  3.169   7.070   1.00 27.59 ? 56  SER A O   1 
ATOM   459  C  CB  . SER A 1 68  ? 30.016  3.711   9.324   1.00 24.58 ? 56  SER A CB  1 
ATOM   460  O  OG  . SER A 1 68  ? 30.502  3.952   10.626  1.00 25.93 ? 56  SER A OG  1 
ATOM   461  N  N   . GLN A 1 69  ? 28.046  1.084   7.630   1.00 24.35 ? 57  GLN A N   1 
ATOM   462  C  CA  . GLN A 1 69  ? 27.612  0.755   6.258   1.00 24.74 ? 57  GLN A CA  1 
ATOM   463  C  C   . GLN A 1 69  ? 26.219  1.336   6.020   1.00 21.19 ? 57  GLN A C   1 
ATOM   464  O  O   . GLN A 1 69  ? 25.463  1.613   6.964   1.00 20.79 ? 57  GLN A O   1 
ATOM   465  C  CB  . GLN A 1 69  ? 27.696  -0.735  5.965   1.00 25.05 ? 57  GLN A CB  1 
ATOM   466  C  CG  . GLN A 1 69  ? 27.025  -1.646  6.971   1.00 24.85 ? 57  GLN A CG  1 
ATOM   467  C  CD  . GLN A 1 69  ? 28.032  -2.353  7.847   1.00 26.85 ? 57  GLN A CD  1 
ATOM   468  O  OE1 . GLN A 1 69  ? 28.446  -3.499  7.610   1.00 31.12 ? 57  GLN A OE1 1 
ATOM   469  N  NE2 . GLN A 1 69  ? 28.420  -1.666  8.903   1.00 21.82 ? 57  GLN A NE2 1 
ATOM   470  N  N   . THR A 1 70  ? 25.904  1.488   4.755   1.00 21.52 ? 58  THR A N   1 
ATOM   471  C  CA  . THR A 1 70  ? 24.526  1.747   4.301   1.00 19.93 ? 58  THR A CA  1 
ATOM   472  C  C   . THR A 1 70  ? 23.713  0.457   4.385   1.00 21.01 ? 58  THR A C   1 
ATOM   473  O  O   . THR A 1 70  ? 24.099  -0.547  3.771   1.00 23.33 ? 58  THR A O   1 
ATOM   474  C  CB  . THR A 1 70  ? 24.563  2.394   2.923   1.00 24.07 ? 58  THR A CB  1 
ATOM   475  O  OG1 . THR A 1 70  ? 25.339  3.584   3.115   1.00 23.58 ? 58  THR A OG1 1 
ATOM   476  C  CG2 . THR A 1 70  ? 23.173  2.664   2.401   1.00 21.16 ? 58  THR A CG2 1 
ATOM   477  N  N   . ILE A 1 71  ? 22.645  0.482   5.178   1.00 20.07 ? 59  ILE A N   1 
ATOM   478  C  CA  . ILE A 1 71  ? 21.853  -0.747  5.445   1.00 19.43 ? 59  ILE A CA  1 
ATOM   479  C  C   . ILE A 1 71  ? 20.616  -0.664  4.554   1.00 17.54 ? 59  ILE A C   1 
ATOM   480  O  O   . ILE A 1 71  ? 20.063  0.440   4.414   1.00 20.50 ? 59  ILE A O   1 
ATOM   481  C  CB  . ILE A 1 71  ? 21.473  -0.846  6.928   1.00 18.44 ? 59  ILE A CB  1 
ATOM   482  C  CG1 . ILE A 1 71  ? 22.709  -0.941  7.825   1.00 20.15 ? 59  ILE A CG1 1 
ATOM   483  C  CG2 . ILE A 1 71  ? 20.522  -2.022  7.142   1.00 22.04 ? 59  ILE A CG2 1 
ATOM   484  C  CD1 . ILE A 1 71  ? 22.347  -0.951  9.307   1.00 21.72 ? 59  ILE A CD1 1 
ATOM   485  N  N   . THR A 1 72  ? 20.219  -1.803  4.015   1.00 16.56 ? 60  THR A N   1 
ATOM   486  C  CA  . THR A 1 72  ? 18.905  -1.986  3.344   1.00 18.40 ? 60  THR A CA  1 
ATOM   487  C  C   . THR A 1 72  ? 18.149  -3.039  4.134   1.00 18.58 ? 60  THR A C   1 
ATOM   488  O  O   . THR A 1 72  ? 18.753  -4.058  4.458   1.00 20.81 ? 60  THR A O   1 
ATOM   489  C  CB  . THR A 1 72  ? 19.099  -2.338  1.863   1.00 22.18 ? 60  THR A CB  1 
ATOM   490  O  OG1 . THR A 1 72  ? 19.843  -3.556  1.798   1.00 33.59 ? 60  THR A OG1 1 
ATOM   491  C  CG2 . THR A 1 72  ? 19.787  -1.238  1.095   1.00 23.03 ? 60  THR A CG2 1 
ATOM   492  N  N   . TYR A 1 73  ? 16.893  -2.811  4.472   1.00 18.84 ? 61  TYR A N   1 
ATOM   493  C  CA  . TYR A 1 73  ? 16.131  -3.845  5.208   1.00 19.14 ? 61  TYR A CA  1 
ATOM   494  C  C   . TYR A 1 73  ? 14.718  -3.837  4.659   1.00 17.55 ? 61  TYR A C   1 
ATOM   495  O  O   . TYR A 1 73  ? 14.282  -2.782  4.178   1.00 16.47 ? 61  TYR A O   1 
ATOM   496  C  CB  . TYR A 1 73  ? 16.216  -3.615  6.720   1.00 20.19 ? 61  TYR A CB  1 
ATOM   497  C  CG  . TYR A 1 73  ? 15.419  -2.448  7.221   1.00 19.49 ? 61  TYR A CG  1 
ATOM   498  C  CD1 . TYR A 1 73  ? 15.825  -1.155  6.989   1.00 19.39 ? 61  TYR A CD1 1 
ATOM   499  C  CD2 . TYR A 1 73  ? 14.157  -2.634  7.778   1.00 21.50 ? 61  TYR A CD2 1 
ATOM   500  C  CE1 . TYR A 1 73  ? 15.058  -0.074  7.391   1.00 20.86 ? 61  TYR A CE1 1 
ATOM   501  C  CE2 . TYR A 1 73  ? 13.404  -1.574  8.236   1.00 20.88 ? 61  TYR A CE2 1 
ATOM   502  C  CZ  . TYR A 1 73  ? 13.818  -0.285  7.981   1.00 22.10 ? 61  TYR A CZ  1 
ATOM   503  O  OH  . TYR A 1 73  ? 13.040  0.785   8.329   1.00 25.11 ? 61  TYR A OH  1 
ATOM   504  N  N   . SER A 1 74  ? 14.060  -4.968  4.814   1.00 18.85 ? 62  SER A N   1 
ATOM   505  C  CA  . SER A 1 74  ? 12.676  -5.194  4.320   1.00 18.50 ? 62  SER A CA  1 
ATOM   506  C  C   . SER A 1 74  ? 11.929  -6.005  5.371   1.00 17.22 ? 62  SER A C   1 
ATOM   507  O  O   . SER A 1 74  ? 12.567  -6.492  6.350   1.00 15.81 ? 62  SER A O   1 
ATOM   508  C  CB  . SER A 1 74  ? 12.688  -5.866  3.005   1.00 20.49 ? 62  SER A CB  1 
ATOM   509  O  OG  . SER A 1 74  ? 13.655  -5.303  2.147   1.00 30.87 ? 62  SER A OG  1 
ATOM   510  N  N   . GLY A 1 75  ? 10.607  -6.042  5.234   1.00 15.22 ? 63  GLY A N   1 
ATOM   511  C  CA  . GLY A 1 75  ? 9.776   -6.937  6.039   1.00 17.71 ? 63  GLY A CA  1 
ATOM   512  C  C   . GLY A 1 75  ? 8.584   -6.239  6.645   1.00 15.21 ? 63  GLY A C   1 
ATOM   513  O  O   . GLY A 1 75  ? 8.026   -5.286  6.052   1.00 15.31 ? 63  GLY A O   1 
ATOM   514  N  N   . GLU A 1 76  ? 8.178   -6.727  7.797   1.00 15.09 ? 64  GLU A N   1 
ATOM   515  C  CA  . GLU A 1 76  ? 6.926   -6.282  8.448   1.00 15.59 ? 64  GLU A CA  1 
ATOM   516  C  C   . GLU A 1 76  ? 7.175   -6.249  9.952   1.00 15.11 ? 64  GLU A C   1 
ATOM   517  O  O   . GLU A 1 76  ? 8.006   -6.990  10.472  1.00 14.19 ? 64  GLU A O   1 
ATOM   518  C  CB  . GLU A 1 76  ? 5.715   -7.131  8.089   1.00 18.14 ? 64  GLU A CB  1 
ATOM   519  C  CG  . GLU A 1 76  ? 5.786   -8.559  8.559   1.00 19.79 ? 64  GLU A CG  1 
ATOM   520  C  CD  . GLU A 1 76  ? 4.660   -9.462  8.068   1.00 23.96 ? 64  GLU A CD  1 
ATOM   521  O  OE1 . GLU A 1 76  ? 3.700   -8.937  7.499   1.00 26.29 ? 64  GLU A OE1 1 
ATOM   522  O  OE2 . GLU A 1 76  ? 4.780   -10.713 8.242   1.00 32.42 ? 64  GLU A OE2 1 
ATOM   523  N  N   . TRP A 1 77  ? 6.525   -5.308  10.583  1.00 14.24 ? 65  TRP A N   1 
ATOM   524  C  CA  . TRP A 1 77  ? 6.628   -5.020  12.030  1.00 15.33 ? 65  TRP A CA  1 
ATOM   525  C  C   . TRP A 1 77  ? 5.204   -4.692  12.469  1.00 15.64 ? 65  TRP A C   1 
ATOM   526  O  O   . TRP A 1 77  ? 4.687   -3.590  12.103  1.00 16.11 ? 65  TRP A O   1 
ATOM   527  C  CB  . TRP A 1 77  ? 7.613   -3.872  12.166  1.00 16.13 ? 65  TRP A CB  1 
ATOM   528  C  CG  . TRP A 1 77  ? 7.710   -3.212  13.508  1.00 15.95 ? 65  TRP A CG  1 
ATOM   529  C  CD1 . TRP A 1 77  ? 8.389   -3.664  14.604  1.00 18.79 ? 65  TRP A CD1 1 
ATOM   530  C  CD2 . TRP A 1 77  ? 7.210   -1.911  13.855  1.00 16.87 ? 65  TRP A CD2 1 
ATOM   531  N  NE1 . TRP A 1 77  ? 8.307   -2.738  15.611  1.00 20.12 ? 65  TRP A NE1 1 
ATOM   532  C  CE2 . TRP A 1 77  ? 7.574   -1.669  15.198  1.00 18.28 ? 65  TRP A CE2 1 
ATOM   533  C  CE3 . TRP A 1 77  ? 6.398   -0.995  13.203  1.00 16.63 ? 65  TRP A CE3 1 
ATOM   534  C  CZ2 . TRP A 1 77  ? 7.241   -0.472  15.853  1.00 19.72 ? 65  TRP A CZ2 1 
ATOM   535  C  CZ3 . TRP A 1 77  ? 6.096   0.192   13.822  1.00 17.63 ? 65  TRP A CZ3 1 
ATOM   536  C  CH2 . TRP A 1 77  ? 6.457   0.418   15.157  1.00 20.23 ? 65  TRP A CH2 1 
ATOM   537  N  N   . ASN A 1 78  ? 4.673   -5.546  13.325  1.00 15.47 ? 66  ASN A N   1 
ATOM   538  C  CA  . ASN A 1 78  ? 3.248   -5.602  13.737  1.00 16.23 ? 66  ASN A CA  1 
ATOM   539  C  C   . ASN A 1 78  ? 3.169   -5.547  15.264  1.00 14.77 ? 66  ASN A C   1 
ATOM   540  O  O   . ASN A 1 78  ? 2.764   -6.518  15.874  1.00 15.02 ? 66  ASN A O   1 
ATOM   541  C  CB  . ASN A 1 78  ? 2.597   -6.873  13.171  1.00 18.90 ? 66  ASN A CB  1 
ATOM   542  C  CG  . ASN A 1 78  ? 2.609   -6.862  11.653  1.00 22.21 ? 66  ASN A CG  1 
ATOM   543  O  OD1 . ASN A 1 78  ? 2.045   -5.957  11.062  1.00 28.59 ? 66  ASN A OD1 1 
ATOM   544  N  ND2 . ASN A 1 78  ? 3.287   -7.802  11.037  1.00 28.02 ? 66  ASN A ND2 1 
ATOM   545  N  N   . PRO A 1 79  ? 3.466   -4.411  15.929  1.00 16.99 ? 67  PRO A N   1 
ATOM   546  C  CA  . PRO A 1 79  ? 3.341   -4.306  17.383  1.00 16.14 ? 67  PRO A CA  1 
ATOM   547  C  C   . PRO A 1 79  ? 1.869   -4.132  17.768  1.00 17.82 ? 67  PRO A C   1 
ATOM   548  O  O   . PRO A 1 79  ? 1.098   -3.607  16.994  1.00 21.38 ? 67  PRO A O   1 
ATOM   549  C  CB  . PRO A 1 79  ? 4.091   -3.019  17.722  1.00 18.91 ? 67  PRO A CB  1 
ATOM   550  C  CG  . PRO A 1 79  ? 3.924   -2.182  16.499  1.00 18.74 ? 67  PRO A CG  1 
ATOM   551  C  CD  . PRO A 1 79  ? 3.989   -3.167  15.346  1.00 19.07 ? 67  PRO A CD  1 
ATOM   552  N  N   . ASN A 1 80  ? 1.553   -4.518  18.974  1.00 15.83 ? 68  ASN A N   1 
ATOM   553  C  CA  . ASN A 1 80  ? 0.330   -4.162  19.735  1.00 19.20 ? 68  ASN A CA  1 
ATOM   554  C  C   . ASN A 1 80  ? 0.837   -3.545  21.034  1.00 18.75 ? 68  ASN A C   1 
ATOM   555  O  O   . ASN A 1 80  ? 1.009   -4.296  22.007  1.00 19.34 ? 68  ASN A O   1 
ATOM   556  C  CB  . ASN A 1 80  ? -0.537  -5.386  19.968  1.00 21.67 ? 68  ASN A CB  1 
ATOM   557  C  CG  . ASN A 1 80  ? -1.900  -5.046  20.537  1.00 28.60 ? 68  ASN A CG  1 
ATOM   558  O  OD1 . ASN A 1 80  ? -2.717  -5.935  20.766  1.00 40.33 ? 68  ASN A OD1 1 
ATOM   559  N  ND2 . ASN A 1 80  ? -2.171  -3.765  20.711  1.00 26.44 ? 68  ASN A ND2 1 
ATOM   560  N  N   . GLY A 1 81  ? 1.157   -2.248  20.989  1.00 17.51 ? 69  GLY A N   1 
ATOM   561  C  CA  . GLY A 1 81  ? 1.804   -1.522  22.085  1.00 18.23 ? 69  GLY A CA  1 
ATOM   562  C  C   . GLY A 1 81  ? 3.238   -1.123  21.775  1.00 17.15 ? 69  GLY A C   1 
ATOM   563  O  O   . GLY A 1 81  ? 3.669   -1.126  20.616  1.00 19.24 ? 69  GLY A O   1 
ATOM   564  N  N   . ASN A 1 82  ? 3.939   -0.773  22.828  1.00 17.04 ? 70  ASN A N   1 
ATOM   565  C  CA  . ASN A 1 82  ? 5.227   -0.066  22.806  1.00 16.15 ? 70  ASN A CA  1 
ATOM   566  C  C   . ASN A 1 82  ? 6.293   -0.912  22.123  1.00 14.76 ? 70  ASN A C   1 
ATOM   567  O  O   . ASN A 1 82  ? 6.631   -1.976  22.669  1.00 15.68 ? 70  ASN A O   1 
ATOM   568  C  CB  . ASN A 1 82  ? 5.639   0.276   24.223  1.00 17.92 ? 70  ASN A CB  1 
ATOM   569  C  CG  . ASN A 1 82  ? 6.869   1.138   24.309  1.00 17.68 ? 70  ASN A CG  1 
ATOM   570  O  OD1 . ASN A 1 82  ? 7.558   1.415   23.312  1.00 18.81 ? 70  ASN A OD1 1 
ATOM   571  N  ND2 . ASN A 1 82  ? 7.245   1.467   25.530  1.00 20.56 ? 70  ASN A ND2 1 
ATOM   572  N  N   . SER A 1 83  ? 6.774   -0.465  20.971  1.00 14.89 ? 71  SER A N   1 
ATOM   573  C  CA  . SER A 1 83  ? 7.792   -1.144  20.164  1.00 14.94 ? 71  SER A CA  1 
ATOM   574  C  C   . SER A 1 83  ? 8.510   -0.133  19.281  1.00 17.12 ? 71  SER A C   1 
ATOM   575  O  O   . SER A 1 83  ? 7.908   0.918   18.948  1.00 14.81 ? 71  SER A O   1 
ATOM   576  C  CB  . SER A 1 83  ? 7.173   -2.281  19.375  1.00 16.32 ? 71  SER A CB  1 
ATOM   577  O  OG  . SER A 1 83  ? 8.140   -2.952  18.577  1.00 16.00 ? 71  SER A OG  1 
ATOM   578  N  N   . TYR A 1 84  ? 9.772   -0.395  18.967  1.00 15.28 ? 72  TYR A N   1 
ATOM   579  C  CA  . TYR A 1 84  ? 10.608  0.482   18.103  1.00 17.01 ? 72  TYR A CA  1 
ATOM   580  C  C   . TYR A 1 84  ? 11.265  -0.446  17.071  1.00 14.82 ? 72  TYR A C   1 
ATOM   581  O  O   . TYR A 1 84  ? 11.548  -1.630  17.380  1.00 14.24 ? 72  TYR A O   1 
ATOM   582  C  CB  . TYR A 1 84  ? 11.755  1.235   18.839  1.00 19.39 ? 72  TYR A CB  1 
ATOM   583  C  CG  . TYR A 1 84  ? 11.634  1.713   20.262  1.00 20.90 ? 72  TYR A CG  1 
ATOM   584  C  CD1 . TYR A 1 84  ? 10.438  2.138   20.808  1.00 24.99 ? 72  TYR A CD1 1 
ATOM   585  C  CD2 . TYR A 1 84  ? 12.755  1.741   21.106  1.00 26.14 ? 72  TYR A CD2 1 
ATOM   586  C  CE1 . TYR A 1 84  ? 10.353  2.609   22.121  1.00 32.30 ? 72  TYR A CE1 1 
ATOM   587  C  CE2 . TYR A 1 84  ? 12.676  2.184   22.425  1.00 30.77 ? 72  TYR A CE2 1 
ATOM   588  C  CZ  . TYR A 1 84  ? 11.468  2.633   22.948  1.00 35.66 ? 72  TYR A CZ  1 
ATOM   589  O  OH  . TYR A 1 84  ? 11.353  3.115   24.257  1.00 32.79 ? 72  TYR A OH  1 
ATOM   590  N  N   . LEU A 1 85  ? 11.350  -0.000  15.829  1.00 14.27 ? 73  LEU A N   1 
ATOM   591  C  CA  . LEU A 1 85  ? 12.116  -0.641  14.744  1.00 13.48 ? 73  LEU A CA  1 
ATOM   592  C  C   . LEU A 1 85  ? 13.263  0.293   14.398  1.00 14.76 ? 73  LEU A C   1 
ATOM   593  O  O   . LEU A 1 85  ? 12.981  1.447   14.071  1.00 13.62 ? 73  LEU A O   1 
ATOM   594  C  CB  . LEU A 1 85  ? 11.193  -0.877  13.538  1.00 14.65 ? 73  LEU A CB  1 
ATOM   595  C  CG  . LEU A 1 85  ? 11.864  -1.522  12.336  1.00 14.56 ? 73  LEU A CG  1 
ATOM   596  C  CD1 . LEU A 1 85  ? 12.344  -2.933  12.673  1.00 16.93 ? 73  LEU A CD1 1 
ATOM   597  C  CD2 . LEU A 1 85  ? 10.870  -1.561  11.158  1.00 14.68 ? 73  LEU A CD2 1 
ATOM   598  N  N   . SER A 1 86  ? 14.525  -0.114  14.569  1.00 15.66 ? 74  SER A N   1 
ATOM   599  C  CA  . SER A 1 86  ? 15.637  0.864   14.576  1.00 15.80 ? 74  SER A CA  1 
ATOM   600  C  C   . SER A 1 86  ? 16.899  0.246   13.996  1.00 14.90 ? 74  SER A C   1 
ATOM   601  O  O   . SER A 1 86  ? 17.013  -0.982  13.976  1.00 14.15 ? 74  SER A O   1 
ATOM   602  C  CB  . SER A 1 86  ? 15.925  1.305   15.982  1.00 18.38 ? 74  SER A CB  1 
ATOM   603  O  OG  . SER A 1 86  ? 16.468  0.191   16.661  1.00 25.95 ? 74  SER A OG  1 
ATOM   604  N  N   . VAL A 1 87  ? 17.791  1.068   13.498  1.00 12.90 ? 75  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 87  ? 19.206  0.620   13.407  1.00 13.19 ? 75  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 87  ? 19.806  0.877   14.782  1.00 13.94 ? 75  VAL A C   1 
ATOM   607  O  O   . VAL A 1 87  ? 19.645  1.995   15.273  1.00 17.28 ? 75  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 87  ? 19.989  1.240   12.254  1.00 13.21 ? 75  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 87  ? 21.451  0.874   12.335  1.00 13.68 ? 75  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 87  ? 19.441  0.857   10.921  1.00 14.08 ? 75  VAL A CG2 1 
ATOM   611  N  N   . TYR A 1 88  ? 20.357  -0.165  15.390  1.00 12.67 ? 76  TYR A N   1 
ATOM   612  C  CA  . TYR A 1 88  ? 20.680  -0.166  16.824  1.00 13.22 ? 76  TYR A CA  1 
ATOM   613  C  C   . TYR A 1 88  ? 22.090  -0.683  16.974  1.00 12.24 ? 76  TYR A C   1 
ATOM   614  O  O   . TYR A 1 88  ? 22.422  -1.722  16.396  1.00 13.78 ? 76  TYR A O   1 
ATOM   615  C  CB  . TYR A 1 88  ? 19.657  -1.020  17.572  1.00 13.44 ? 76  TYR A CB  1 
ATOM   616  C  CG  . TYR A 1 88  ? 20.029  -1.335  18.997  1.00 14.44 ? 76  TYR A CG  1 
ATOM   617  C  CD1 . TYR A 1 88  ? 19.829  -0.400  20.004  1.00 15.40 ? 76  TYR A CD1 1 
ATOM   618  C  CD2 . TYR A 1 88  ? 20.494  -2.592  19.362  1.00 13.88 ? 76  TYR A CD2 1 
ATOM   619  C  CE1 . TYR A 1 88  ? 20.199  -0.672  21.315  1.00 15.21 ? 76  TYR A CE1 1 
ATOM   620  C  CE2 . TYR A 1 88  ? 20.828  -2.890  20.665  1.00 14.62 ? 76  TYR A CE2 1 
ATOM   621  C  CZ  . TYR A 1 88  ? 20.616  -1.956  21.660  1.00 13.80 ? 76  TYR A CZ  1 
ATOM   622  O  OH  . TYR A 1 88  ? 20.962  -2.236  22.952  1.00 15.30 ? 76  TYR A OH  1 
ATOM   623  N  N   . GLY A 1 89  ? 22.879  -0.011  17.807  1.00 12.77 ? 77  GLY A N   1 
ATOM   624  C  CA  . GLY A 1 89  ? 24.234  -0.506  18.055  1.00 12.90 ? 77  GLY A CA  1 
ATOM   625  C  C   . GLY A 1 89  ? 24.882  0.100   19.261  1.00 13.13 ? 77  GLY A C   1 
ATOM   626  O  O   . GLY A 1 89  ? 24.229  0.907   20.015  1.00 13.52 ? 77  GLY A O   1 
ATOM   627  N  N   . TRP A 1 90  ? 26.161  -0.237  19.389  1.00 12.96 ? 78  TRP A N   1 
ATOM   628  C  CA  . TRP A 1 90  ? 27.004  0.163   20.547  1.00 13.27 ? 78  TRP A CA  1 
ATOM   629  C  C   . TRP A 1 90  ? 28.353  0.646   20.065  1.00 13.51 ? 78  TRP A C   1 
ATOM   630  O  O   . TRP A 1 90  ? 28.822  0.081   19.046  1.00 13.43 ? 78  TRP A O   1 
ATOM   631  C  CB  . TRP A 1 90  ? 27.208  -1.010  21.506  1.00 14.25 ? 78  TRP A CB  1 
ATOM   632  C  CG  . TRP A 1 90  ? 25.968  -1.343  22.285  1.00 14.96 ? 78  TRP A CG  1 
ATOM   633  C  CD1 . TRP A 1 90  ? 24.942  -2.092  21.808  1.00 14.98 ? 78  TRP A CD1 1 
ATOM   634  C  CD2 . TRP A 1 90  ? 25.581  -0.912  23.598  1.00 16.59 ? 78  TRP A CD2 1 
ATOM   635  N  NE1 . TRP A 1 90  ? 23.971  -2.217  22.758  1.00 14.76 ? 78  TRP A NE1 1 
ATOM   636  C  CE2 . TRP A 1 90  ? 24.322  -1.490  23.858  1.00 15.66 ? 78  TRP A CE2 1 
ATOM   637  C  CE3 . TRP A 1 90  ? 26.146  -0.090  24.592  1.00 15.56 ? 78  TRP A CE3 1 
ATOM   638  C  CZ2 . TRP A 1 90  ? 23.647  -1.313  25.069  1.00 16.15 ? 78  TRP A CZ2 1 
ATOM   639  C  CZ3 . TRP A 1 90  ? 25.477  0.080   25.789  1.00 15.02 ? 78  TRP A CZ3 1 
ATOM   640  C  CH2 . TRP A 1 90  ? 24.216  -0.471  25.993  1.00 16.39 ? 78  TRP A CH2 1 
ATOM   641  N  N   . THR A 1 91  ? 28.914  1.663   20.760  1.00 13.13 ? 79  THR A N   1 
ATOM   642  C  CA  . THR A 1 91  ? 30.375  1.919   20.715  1.00 12.31 ? 79  THR A CA  1 
ATOM   643  C  C   . THR A 1 91  ? 30.932  1.630   22.093  1.00 11.98 ? 79  THR A C   1 
ATOM   644  O  O   . THR A 1 91  ? 30.206  1.531   23.104  1.00 11.82 ? 79  THR A O   1 
ATOM   645  C  CB  . THR A 1 91  ? 30.799  3.318   20.198  1.00 14.07 ? 79  THR A CB  1 
ATOM   646  O  OG1 . THR A 1 91  ? 30.478  4.186   21.271  1.00 15.64 ? 79  THR A OG1 1 
ATOM   647  C  CG2 . THR A 1 91  ? 30.130  3.682   18.900  1.00 14.92 ? 79  THR A CG2 1 
ATOM   648  N  N   . GLN A 1 92  ? 32.222  1.403   22.102  1.00 13.98 ? 80  GLN A N   1 
ATOM   649  C  CA  . GLN A 1 92  ? 33.002  1.222   23.355  1.00 15.77 ? 80  GLN A CA  1 
ATOM   650  C  C   . GLN A 1 92  ? 34.046  2.336   23.447  1.00 15.74 ? 80  GLN A C   1 
ATOM   651  O  O   . GLN A 1 92  ? 34.604  2.732   22.418  1.00 14.31 ? 80  GLN A O   1 
ATOM   652  C  CB  . GLN A 1 92  ? 33.629  -0.166  23.367  1.00 18.19 ? 80  GLN A CB  1 
ATOM   653  C  CG  . GLN A 1 92  ? 32.609  -1.266  23.572  1.00 20.38 ? 80  GLN A CG  1 
ATOM   654  C  CD  . GLN A 1 92  ? 33.149  -2.612  23.140  1.00 21.81 ? 80  GLN A CD  1 
ATOM   655  O  OE1 . GLN A 1 92  ? 33.457  -2.830  21.967  1.00 28.68 ? 80  GLN A OE1 1 
ATOM   656  N  NE2 . GLN A 1 92  ? 33.260  -3.527  24.073  1.00 27.02 ? 80  GLN A NE2 1 
ATOM   657  N  N   . ASN A 1 93  ? 34.347  2.766   24.668  1.00 15.32 ? 81  ASN A N   1 
ATOM   658  C  CA  . ASN A 1 93  ? 35.493  3.654   24.966  1.00 17.92 ? 81  ASN A CA  1 
ATOM   659  C  C   . ASN A 1 93  ? 35.417  4.941   24.139  1.00 16.25 ? 81  ASN A C   1 
ATOM   660  O  O   . ASN A 1 93  ? 36.269  5.252   23.279  1.00 16.37 ? 81  ASN A O   1 
ATOM   661  C  CB  . ASN A 1 93  ? 36.790  2.903   24.740  1.00 17.75 ? 81  ASN A CB  1 
ATOM   662  C  CG  . ASN A 1 93  ? 37.965  3.697   25.228  1.00 17.63 ? 81  ASN A CG  1 
ATOM   663  O  OD1 . ASN A 1 93  ? 37.792  4.560   26.080  1.00 17.38 ? 81  ASN A OD1 1 
ATOM   664  N  ND2 . ASN A 1 93  ? 39.122  3.496   24.610  1.00 20.99 ? 81  ASN A ND2 1 
ATOM   665  N  N   . PRO A 1 94  ? 34.371  5.754   24.329  1.00 17.52 ? 82  PRO A N   1 
ATOM   666  C  CA  . PRO A 1 94  ? 33.356  5.545   25.366  1.00 18.88 ? 82  PRO A CA  1 
ATOM   667  C  C   . PRO A 1 94  ? 32.176  4.648   24.991  1.00 17.63 ? 82  PRO A C   1 
ATOM   668  O  O   . PRO A 1 94  ? 31.806  4.553   23.795  1.00 14.59 ? 82  PRO A O   1 
ATOM   669  C  CB  . PRO A 1 94  ? 32.733  6.941   25.541  1.00 18.43 ? 82  PRO A CB  1 
ATOM   670  C  CG  . PRO A 1 94  ? 32.862  7.558   24.193  1.00 19.80 ? 82  PRO A CG  1 
ATOM   671  C  CD  . PRO A 1 94  ? 34.155  7.026   23.618  1.00 17.75 ? 82  PRO A CD  1 
ATOM   672  N  N   . LEU A 1 95  ? 31.602  4.081   26.035  1.00 16.86 ? 83  LEU A N   1 
ATOM   673  C  CA  . LEU A 1 95  ? 30.394  3.223   25.933  1.00 18.83 ? 83  LEU A CA  1 
ATOM   674  C  C   . LEU A 1 95  ? 29.211  4.108   25.543  1.00 15.62 ? 83  LEU A C   1 
ATOM   675  O  O   . LEU A 1 95  ? 28.879  5.111   26.233  1.00 17.24 ? 83  LEU A O   1 
ATOM   676  C  CB  . LEU A 1 95  ? 30.185  2.497   27.262  1.00 18.51 ? 83  LEU A CB  1 
ATOM   677  C  CG  . LEU A 1 95  ? 29.095  1.429   27.293  1.00 18.58 ? 83  LEU A CG  1 
ATOM   678  C  CD1 . LEU A 1 95  ? 29.404  0.274   26.348  1.00 18.57 ? 83  LEU A CD1 1 
ATOM   679  C  CD2 . LEU A 1 95  ? 28.880  0.900   28.708  1.00 19.29 ? 83  LEU A CD2 1 
ATOM   680  N  N   . VAL A 1 96  ? 28.569  3.755   24.434  1.00 15.18 ? 84  VAL A N   1 
ATOM   681  C  CA  . VAL A 1 96  ? 27.427  4.489   23.843  1.00 16.28 ? 84  VAL A CA  1 
ATOM   682  C  C   . VAL A 1 96  ? 26.448  3.450   23.298  1.00 14.06 ? 84  VAL A C   1 
ATOM   683  O  O   . VAL A 1 96  ? 26.875  2.525   22.571  1.00 14.06 ? 84  VAL A O   1 
ATOM   684  C  CB  . VAL A 1 96  ? 27.853  5.433   22.710  1.00 15.90 ? 84  VAL A CB  1 
ATOM   685  C  CG1 . VAL A 1 96  ? 26.640  5.971   21.956  1.00 19.26 ? 84  VAL A CG1 1 
ATOM   686  C  CG2 . VAL A 1 96  ? 28.752  6.547   23.213  1.00 17.96 ? 84  VAL A CG2 1 
ATOM   687  N  N   . GLU A 1 97  ? 25.171  3.649   23.590  1.00 14.42 ? 85  GLU A N   1 
ATOM   688  C  CA  . GLU A 1 97  ? 24.066  2.901   22.947  1.00 15.34 ? 85  GLU A CA  1 
ATOM   689  C  C   . GLU A 1 97  ? 23.407  3.846   21.962  1.00 15.57 ? 85  GLU A C   1 
ATOM   690  O  O   . GLU A 1 97  ? 23.151  4.987   22.337  1.00 14.67 ? 85  GLU A O   1 
ATOM   691  C  CB  . GLU A 1 97  ? 23.059  2.444   24.005  1.00 15.03 ? 85  GLU A CB  1 
ATOM   692  C  CG  . GLU A 1 97  ? 22.043  1.453   23.482  1.00 17.08 ? 85  GLU A CG  1 
ATOM   693  C  CD  . GLU A 1 97  ? 20.973  1.073   24.496  1.00 17.29 ? 85  GLU A CD  1 
ATOM   694  O  OE1 . GLU A 1 97  ? 20.487  -0.051  24.434  1.00 18.87 ? 85  GLU A OE1 1 
ATOM   695  O  OE2 . GLU A 1 97  ? 20.692  1.844   25.373  1.00 20.04 ? 85  GLU A OE2 1 
ATOM   696  N  N   . TYR A 1 98  ? 23.135  3.425   20.731  1.00 15.33 ? 86  TYR A N   1 
ATOM   697  C  CA  . TYR A 1 98  ? 22.515  4.379   19.787  1.00 15.81 ? 86  TYR A CA  1 
ATOM   698  C  C   . TYR A 1 98  ? 21.400  3.690   19.006  1.00 14.38 ? 86  TYR A C   1 
ATOM   699  O  O   . TYR A 1 98  ? 21.377  2.440   18.820  1.00 13.55 ? 86  TYR A O   1 
ATOM   700  C  CB  . TYR A 1 98  ? 23.542  4.999   18.851  1.00 16.80 ? 86  TYR A CB  1 
ATOM   701  C  CG  . TYR A 1 98  ? 24.175  3.999   17.925  1.00 15.64 ? 86  TYR A CG  1 
ATOM   702  C  CD1 . TYR A 1 98  ? 23.527  3.621   16.767  1.00 16.38 ? 86  TYR A CD1 1 
ATOM   703  C  CD2 . TYR A 1 98  ? 25.418  3.456   18.173  1.00 16.72 ? 86  TYR A CD2 1 
ATOM   704  C  CE1 . TYR A 1 98  ? 24.065  2.686   15.906  1.00 16.64 ? 86  TYR A CE1 1 
ATOM   705  C  CE2 . TYR A 1 98  ? 25.984  2.531   17.307  1.00 17.21 ? 86  TYR A CE2 1 
ATOM   706  C  CZ  . TYR A 1 98  ? 25.303  2.145   16.170  1.00 17.22 ? 86  TYR A CZ  1 
ATOM   707  O  OH  . TYR A 1 98  ? 25.833  1.261   15.285  1.00 21.20 ? 86  TYR A OH  1 
ATOM   708  N  N   . TYR A 1 99  ? 20.468  4.526   18.588  1.00 14.24 ? 87  TYR A N   1 
ATOM   709  C  CA  . TYR A 1 99  ? 19.211  4.125   17.931  1.00 14.98 ? 87  TYR A CA  1 
ATOM   710  C  C   . TYR A 1 99  ? 18.956  5.079   16.783  1.00 15.89 ? 87  TYR A C   1 
ATOM   711  O  O   . TYR A 1 99  ? 18.882  6.321   17.015  1.00 15.40 ? 87  TYR A O   1 
ATOM   712  C  CB  . TYR A 1 99  ? 18.022  4.184   18.898  1.00 16.41 ? 87  TYR A CB  1 
ATOM   713  C  CG  . TYR A 1 99  ? 17.806  3.059   19.891  1.00 20.04 ? 87  TYR A CG  1 
ATOM   714  C  CD1 . TYR A 1 99  ? 17.054  1.953   19.551  1.00 25.73 ? 87  TYR A CD1 1 
ATOM   715  C  CD2 . TYR A 1 99  ? 18.262  3.132   21.205  1.00 25.19 ? 87  TYR A CD2 1 
ATOM   716  C  CE1 . TYR A 1 99  ? 16.791  0.924   20.442  1.00 28.27 ? 87  TYR A CE1 1 
ATOM   717  C  CE2 . TYR A 1 99  ? 18.007  2.109   22.113  1.00 25.40 ? 87  TYR A CE2 1 
ATOM   718  C  CZ  . TYR A 1 99  ? 17.271  0.999   21.732  1.00 29.05 ? 87  TYR A CZ  1 
ATOM   719  O  OH  . TYR A 1 99  ? 16.969  -0.045  22.583  1.00 37.90 ? 87  TYR A OH  1 
ATOM   720  N  N   . ILE A 1 100 ? 18.798  4.530   15.587  1.00 14.97 ? 88  ILE A N   1 
ATOM   721  C  CA  . ILE A 1 100 ? 18.238  5.215   14.410  1.00 13.84 ? 88  ILE A CA  1 
ATOM   722  C  C   . ILE A 1 100 ? 16.828  4.655   14.224  1.00 13.57 ? 88  ILE A C   1 
ATOM   723  O  O   . ILE A 1 100 ? 16.675  3.528   13.671  1.00 15.38 ? 88  ILE A O   1 
ATOM   724  C  CB  . ILE A 1 100 ? 19.133  5.017   13.178  1.00 12.77 ? 88  ILE A CB  1 
ATOM   725  C  CG1 . ILE A 1 100 ? 20.530  5.548   13.447  1.00 13.58 ? 88  ILE A CG1 1 
ATOM   726  C  CG2 . ILE A 1 100 ? 18.516  5.650   11.954  1.00 15.06 ? 88  ILE A CG2 1 
ATOM   727  C  CD1 . ILE A 1 100 ? 21.568  5.135   12.442  1.00 13.20 ? 88  ILE A CD1 1 
ATOM   728  N  N   . VAL A 1 101 ? 15.876  5.353   14.826  1.00 13.07 ? 89  VAL A N   1 
ATOM   729  C  CA  . VAL A 1 101 ? 14.496  4.879   14.965  1.00 13.28 ? 89  VAL A CA  1 
ATOM   730  C  C   . VAL A 1 101 ? 13.749  5.128   13.655  1.00 12.83 ? 89  VAL A C   1 
ATOM   731  O  O   . VAL A 1 101 ? 13.477  6.296   13.339  1.00 15.77 ? 89  VAL A O   1 
ATOM   732  C  CB  . VAL A 1 101 ? 13.809  5.481   16.191  1.00 13.76 ? 89  VAL A CB  1 
ATOM   733  C  CG1 . VAL A 1 101 ? 12.393  4.967   16.296  1.00 14.92 ? 89  VAL A CG1 1 
ATOM   734  C  CG2 . VAL A 1 101 ? 14.583  5.193   17.462  1.00 15.41 ? 89  VAL A CG2 1 
ATOM   735  N  N   . GLU A 1 102 ? 13.357  4.037   12.997  1.00 13.25 ? 90  GLU A N   1 
ATOM   736  C  CA  . GLU A 1 102 ? 12.608  4.047   11.719  1.00 14.15 ? 90  GLU A CA  1 
ATOM   737  C  C   . GLU A 1 102 ? 11.095  4.171   11.980  1.00 16.25 ? 90  GLU A C   1 
ATOM   738  O  O   . GLU A 1 102 ? 10.386  4.910   11.246  1.00 14.15 ? 90  GLU A O   1 
ATOM   739  C  CB  . GLU A 1 102 ? 12.943  2.802   10.924  1.00 16.28 ? 90  GLU A CB  1 
ATOM   740  C  CG  . GLU A 1 102 ? 14.380  2.805   10.440  1.00 18.37 ? 90  GLU A CG  1 
ATOM   741  C  CD  . GLU A 1 102 ? 14.584  3.827   9.352   1.00 20.28 ? 90  GLU A CD  1 
ATOM   742  O  OE1 . GLU A 1 102 ? 14.971  4.979   9.683   1.00 21.61 ? 90  GLU A OE1 1 
ATOM   743  O  OE2 . GLU A 1 102 ? 14.296  3.498   8.192   1.00 23.32 ? 90  GLU A OE2 1 
ATOM   744  N  N   . SER A 1 103 ? 10.611  3.499   13.015  1.00 15.65 ? 91  SER A N   1 
ATOM   745  C  CA  . SER A 1 103 ? 9.202   3.588   13.468  1.00 16.47 ? 91  SER A CA  1 
ATOM   746  C  C   . SER A 1 103 ? 9.194   3.387   14.975  1.00 15.46 ? 91  SER A C   1 
ATOM   747  O  O   . SER A 1 103 ? 10.016  2.613   15.532  1.00 15.34 ? 91  SER A O   1 
ATOM   748  C  CB  . SER A 1 103 ? 8.278   2.591   12.828  1.00 17.17 ? 91  SER A CB  1 
ATOM   749  O  OG  . SER A 1 103 ? 8.155   2.697   11.416  1.00 19.15 ? 91  SER A OG  1 
ATOM   750  N  N   . PHE A 1 104 ? 8.293   4.050   15.658  1.00 14.54 ? 92  PHE A N   1 
ATOM   751  C  CA  . PHE A 1 104 ? 7.890   3.655   17.028  1.00 16.21 ? 92  PHE A CA  1 
ATOM   752  C  C   . PHE A 1 104 ? 6.375   3.610   17.037  1.00 16.75 ? 92  PHE A C   1 
ATOM   753  O  O   . PHE A 1 104 ? 5.744   4.168   16.142  1.00 18.79 ? 92  PHE A O   1 
ATOM   754  C  CB  . PHE A 1 104 ? 8.476   4.554   18.102  1.00 17.57 ? 92  PHE A CB  1 
ATOM   755  C  CG  . PHE A 1 104 ? 8.053   6.000   18.066  1.00 16.34 ? 92  PHE A CG  1 
ATOM   756  C  CD1 . PHE A 1 104 ? 6.811   6.389   18.577  1.00 16.42 ? 92  PHE A CD1 1 
ATOM   757  C  CD2 . PHE A 1 104 ? 8.906   6.976   17.592  1.00 16.65 ? 92  PHE A CD2 1 
ATOM   758  C  CE1 . PHE A 1 104 ? 6.470   7.738   18.639  1.00 16.48 ? 92  PHE A CE1 1 
ATOM   759  C  CE2 . PHE A 1 104 ? 8.533   8.317   17.615  1.00 16.34 ? 92  PHE A CE2 1 
ATOM   760  C  CZ  . PHE A 1 104 ? 7.300   8.686   18.110  1.00 19.08 ? 92  PHE A CZ  1 
ATOM   761  N  N   . SER A 1 105 ? 5.783   2.962   18.032  1.00 15.97 ? 93  SER A N   1 
ATOM   762  C  CA  . SER A 1 105 ? 4.322   2.735   18.025  1.00 16.38 ? 93  SER A CA  1 
ATOM   763  C  C   . SER A 1 105 ? 3.699   3.748   18.974  1.00 20.70 ? 93  SER A C   1 
ATOM   764  O  O   . SER A 1 105 ? 3.561   4.951   18.567  1.00 25.74 ? 93  SER A O   1 
ATOM   765  C  CB  . SER A 1 105 ? 4.014   1.294   18.330  1.00 17.19 ? 93  SER A CB  1 
ATOM   766  O  OG  . SER A 1 105 ? 4.634   0.957   19.547  1.00 17.13 ? 93  SER A OG  1 
ATOM   767  N  N   . THR A 1 106 ? 3.553   3.378   20.244  1.00 22.20 ? 94  THR A N   1 
ATOM   768  C  CA  . THR A 1 106 ? 2.750   4.149   21.231  1.00 20.82 ? 94  THR A CA  1 
ATOM   769  C  C   . THR A 1 106 ? 3.587   5.049   22.155  1.00 20.50 ? 94  THR A C   1 
ATOM   770  O  O   . THR A 1 106 ? 2.989   5.712   23.063  1.00 20.82 ? 94  THR A O   1 
ATOM   771  C  CB  . THR A 1 106 ? 1.917   3.150   22.032  1.00 22.61 ? 94  THR A CB  1 
ATOM   772  O  OG1 . THR A 1 106 ? 2.826   2.292   22.699  1.00 23.57 ? 94  THR A OG1 1 
ATOM   773  C  CG2 . THR A 1 106 ? 1.001   2.337   21.157  1.00 22.93 ? 94  THR A CG2 1 
ATOM   774  N  N   . TYR A 1 107 ? 4.912   5.053   22.054  1.00 16.56 ? 95  TYR A N   1 
ATOM   775  C  CA  . TYR A 1 107 ? 5.804   5.751   23.004  1.00 17.46 ? 95  TYR A CA  1 
ATOM   776  C  C   . TYR A 1 107 ? 7.021   6.267   22.240  1.00 17.78 ? 95  TYR A C   1 
ATOM   777  O  O   . TYR A 1 107 ? 7.684   5.474   21.608  1.00 16.34 ? 95  TYR A O   1 
ATOM   778  C  CB  . TYR A 1 107 ? 6.271   4.881   24.168  1.00 18.58 ? 95  TYR A CB  1 
ATOM   779  C  CG  . TYR A 1 107 ? 7.144   5.606   25.164  1.00 18.80 ? 95  TYR A CG  1 
ATOM   780  C  CD1 . TYR A 1 107 ? 6.606   6.564   26.015  1.00 21.23 ? 95  TYR A CD1 1 
ATOM   781  C  CD2 . TYR A 1 107 ? 8.509   5.374   25.251  1.00 20.66 ? 95  TYR A CD2 1 
ATOM   782  C  CE1 . TYR A 1 107 ? 7.375   7.261   26.929  1.00 21.52 ? 95  TYR A CE1 1 
ATOM   783  C  CE2 . TYR A 1 107 ? 9.303   6.073   26.146  1.00 21.87 ? 95  TYR A CE2 1 
ATOM   784  C  CZ  . TYR A 1 107 ? 8.734   7.004   27.006  1.00 23.31 ? 95  TYR A CZ  1 
ATOM   785  O  OH  . TYR A 1 107 ? 9.451   7.710   27.911  1.00 22.70 ? 95  TYR A OH  1 
ATOM   786  N  N   . ASP A 1 108 ? 7.228   7.573   22.245  1.00 18.19 ? 96  ASP A N   1 
ATOM   787  C  CA  . ASP A 1 108 ? 8.404   8.203   21.600  1.00 20.28 ? 96  ASP A CA  1 
ATOM   788  C  C   . ASP A 1 108 ? 9.602   7.976   22.521  1.00 22.67 ? 96  ASP A C   1 
ATOM   789  O  O   . ASP A 1 108 ? 9.654   8.556   23.609  1.00 22.17 ? 96  ASP A O   1 
ATOM   790  C  CB  . ASP A 1 108 ? 8.194   9.706   21.356  1.00 19.10 ? 96  ASP A CB  1 
ATOM   791  C  CG  . ASP A 1 108 ? 9.306   10.337  20.518  1.00 24.08 ? 96  ASP A CG  1 
ATOM   792  O  OD1 . ASP A 1 108 ? 10.409  9.743   20.448  1.00 26.47 ? 96  ASP A OD1 1 
ATOM   793  O  OD2 . ASP A 1 108 ? 9.048   11.407  19.911  1.00 25.76 ? 96  ASP A OD2 1 
ATOM   794  N  N   . PRO A 1 109 ? 10.570  7.116   22.130  1.00 25.79 ? 97  PRO A N   1 
ATOM   795  C  CA  . PRO A 1 109 ? 11.647  6.702   23.029  1.00 30.44 ? 97  PRO A CA  1 
ATOM   796  C  C   . PRO A 1 109 ? 12.658  7.813   23.285  1.00 34.78 ? 97  PRO A C   1 
ATOM   797  O  O   . PRO A 1 109 ? 13.504  7.614   24.149  1.00 40.70 ? 97  PRO A O   1 
ATOM   798  C  CB  . PRO A 1 109 ? 12.283  5.548   22.245  1.00 33.11 ? 97  PRO A CB  1 
ATOM   799  C  CG  . PRO A 1 109 ? 12.201  6.057   20.830  1.00 30.49 ? 97  PRO A CG  1 
ATOM   800  C  CD  . PRO A 1 109 ? 10.776  6.574   20.780  1.00 26.71 ? 97  PRO A CD  1 
ATOM   801  N  N   . SER A 1 110 ? 12.531  8.929   22.550  1.00 36.95 ? 98  SER A N   1 
ATOM   802  C  CA  . SER A 1 110 ? 13.302  10.182  22.728  1.00 34.26 ? 98  SER A CA  1 
ATOM   803  C  C   . SER A 1 110 ? 12.726  10.972  23.898  1.00 34.79 ? 98  SER A C   1 
ATOM   804  O  O   . SER A 1 110 ? 13.336  11.975  24.264  1.00 37.62 ? 98  SER A O   1 
ATOM   805  C  CB  . SER A 1 110 ? 13.354  11.024  21.459  1.00 35.36 ? 98  SER A CB  1 
ATOM   806  O  OG  . SER A 1 110 ? 12.232  11.889  21.324  1.00 30.49 ? 98  SER A OG  1 
ATOM   807  N  N   . THR A 1 111 ? 11.571  10.565  24.444  1.00 27.91 ? 99  THR A N   1 
ATOM   808  C  CA  . THR A 1 111 ? 10.978  11.229  25.615  1.00 24.91 ? 99  THR A CA  1 
ATOM   809  C  C   . THR A 1 111 ? 12.024  11.325  26.746  1.00 25.66 ? 99  THR A C   1 
ATOM   810  O  O   . THR A 1 111 ? 12.640  10.280  27.100  1.00 29.69 ? 99  THR A O   1 
ATOM   811  C  CB  . THR A 1 111 ? 9.687   10.539  26.063  1.00 23.05 ? 99  THR A CB  1 
ATOM   812  O  OG1 . THR A 1 111 ? 8.742   10.685  25.003  1.00 22.56 ? 99  THR A OG1 1 
ATOM   813  C  CG2 . THR A 1 111 ? 9.126   11.117  27.347  1.00 25.42 ? 99  THR A CG2 1 
ATOM   814  N  N   . GLY A 1 112 ? 12.179  12.560  27.232  1.00 27.51 ? 100 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 112 ? 13.035  13.016  28.353  1.00 35.56 ? 100 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 112 ? 14.347  13.644  27.889  1.00 38.32 ? 100 GLY A C   1 
ATOM   817  O  O   . GLY A 1 112 ? 15.342  13.465  28.613  1.00 36.91 ? 100 GLY A O   1 
ATOM   818  N  N   . ALA A 1 113 ? 14.346  14.400  26.770  1.00 47.21 ? 101 ALA A N   1 
ATOM   819  C  CA  . ALA A 1 113 ? 15.569  14.944  26.114  1.00 40.67 ? 101 ALA A CA  1 
ATOM   820  C  C   . ALA A 1 113 ? 15.342  16.294  25.421  1.00 45.13 ? 101 ALA A C   1 
ATOM   821  O  O   . ALA A 1 113 ? 14.288  16.486  24.788  1.00 44.64 ? 101 ALA A O   1 
ATOM   822  C  CB  . ALA A 1 113 ? 16.086  13.961  25.120  1.00 38.83 ? 101 ALA A CB  1 
ATOM   823  N  N   . GLN A 1 114 ? 16.359  17.165  25.472  1.00 40.95 ? 102 GLN A N   1 
ATOM   824  C  CA  . GLN A 1 114 ? 16.455  18.371  24.613  1.00 43.79 ? 102 GLN A CA  1 
ATOM   825  C  C   . GLN A 1 114 ? 16.845  17.895  23.213  1.00 37.94 ? 102 GLN A C   1 
ATOM   826  O  O   . GLN A 1 114 ? 17.812  17.148  23.089  1.00 38.54 ? 102 GLN A O   1 
ATOM   827  C  CB  . GLN A 1 114 ? 17.471  19.381  25.161  1.00 44.95 ? 102 GLN A CB  1 
ATOM   828  C  CG  . GLN A 1 114 ? 17.558  20.667  24.341  1.00 52.06 ? 102 GLN A CG  1 
ATOM   829  C  CD  . GLN A 1 114 ? 17.678  21.911  25.194  1.00 57.63 ? 102 GLN A CD  1 
ATOM   830  O  OE1 . GLN A 1 114 ? 18.698  22.599  25.186  1.00 61.75 ? 102 GLN A OE1 1 
ATOM   831  N  NE2 . GLN A 1 114 ? 16.629  22.211  25.946  1.00 57.37 ? 102 GLN A NE2 1 
ATOM   832  N  N   . GLU A 1 115 ? 16.088  18.298  22.203  1.00 38.83 ? 103 GLU A N   1 
ATOM   833  C  CA  . GLU A 1 115 ? 16.458  18.047  20.798  1.00 37.44 ? 103 GLU A CA  1 
ATOM   834  C  C   . GLU A 1 115 ? 17.721  18.870  20.509  1.00 38.57 ? 103 GLU A C   1 
ATOM   835  O  O   . GLU A 1 115 ? 17.753  20.087  20.868  1.00 40.89 ? 103 GLU A O   1 
ATOM   836  C  CB  . GLU A 1 115 ? 15.261  18.370  19.904  1.00 38.26 ? 103 GLU A CB  1 
ATOM   837  C  CG  . GLU A 1 115 ? 15.414  17.903  18.478  1.00 40.80 ? 103 GLU A CG  1 
ATOM   838  C  CD  . GLU A 1 115 ? 14.377  18.501  17.546  1.00 43.27 ? 103 GLU A CD  1 
ATOM   839  O  OE1 . GLU A 1 115 ? 14.732  18.833  16.381  1.00 39.68 ? 103 GLU A OE1 1 
ATOM   840  O  OE2 . GLU A 1 115 ? 13.211  18.637  18.001  1.00 40.67 ? 103 GLU A OE2 1 
ATOM   841  N  N   . LEU A 1 116 ? 18.706  18.249  19.860  1.00 29.93 ? 104 LEU A N   1 
ATOM   842  C  CA  . LEU A 1 116 ? 20.028  18.858  19.548  1.00 33.22 ? 104 LEU A CA  1 
ATOM   843  C  C   . LEU A 1 116 ? 20.083  19.359  18.103  1.00 33.84 ? 104 LEU A C   1 
ATOM   844  O  O   . LEU A 1 116 ? 21.069  20.055  17.755  1.00 36.47 ? 104 LEU A O   1 
ATOM   845  C  CB  . LEU A 1 116 ? 21.113  17.814  19.801  1.00 30.97 ? 104 LEU A CB  1 
ATOM   846  C  CG  . LEU A 1 116 ? 21.257  17.373  21.249  1.00 33.71 ? 104 LEU A CG  1 
ATOM   847  C  CD1 . LEU A 1 116 ? 22.323  16.296  21.378  1.00 33.74 ? 104 LEU A CD1 1 
ATOM   848  C  CD2 . LEU A 1 116 ? 21.562  18.554  22.156  1.00 34.17 ? 104 LEU A CD2 1 
ATOM   849  N  N   . GLY A 1 117 ? 19.078  19.026  17.294  1.00 30.42 ? 105 GLY A N   1 
ATOM   850  C  CA  . GLY A 1 117 ? 19.026  19.378  15.865  1.00 31.94 ? 105 GLY A CA  1 
ATOM   851  C  C   . GLY A 1 117 ? 18.343  18.290  15.050  1.00 28.22 ? 105 GLY A C   1 
ATOM   852  O  O   . GLY A 1 117 ? 17.607  17.438  15.641  1.00 24.67 ? 105 GLY A O   1 
ATOM   853  N  N   . THR A 1 118 ? 18.576  18.313  13.740  1.00 28.56 ? 106 THR A N   1 
ATOM   854  C  CA  . THR A 1 118 ? 17.951  17.400  12.759  1.00 27.21 ? 106 THR A CA  1 
ATOM   855  C  C   . THR A 1 118 ? 18.996  16.945  11.748  1.00 26.27 ? 106 THR A C   1 
ATOM   856  O  O   . THR A 1 118 ? 19.993  17.659  11.542  1.00 26.36 ? 106 THR A O   1 
ATOM   857  C  CB  . THR A 1 118 ? 16.784  18.065  12.026  1.00 31.73 ? 106 THR A CB  1 
ATOM   858  O  OG1 . THR A 1 118 ? 17.335  19.210  11.362  1.00 33.07 ? 106 THR A OG1 1 
ATOM   859  C  CG2 . THR A 1 118 ? 15.644  18.420  12.955  1.00 30.96 ? 106 THR A CG2 1 
ATOM   860  N  N   . VAL A 1 119 ? 18.808  15.752  11.185  1.00 24.12 ? 107 VAL A N   1 
ATOM   861  C  CA  . VAL A 1 119 ? 19.565  15.296  9.996   1.00 23.26 ? 107 VAL A CA  1 
ATOM   862  C  C   . VAL A 1 119 ? 18.561  14.876  8.913   1.00 24.37 ? 107 VAL A C   1 
ATOM   863  O  O   . VAL A 1 119 ? 17.520  14.261  9.240   1.00 21.45 ? 107 VAL A O   1 
ATOM   864  C  CB  . VAL A 1 119 ? 20.552  14.177  10.351  1.00 23.73 ? 107 VAL A CB  1 
ATOM   865  C  CG1 . VAL A 1 119 ? 19.860  12.940  10.869  1.00 25.08 ? 107 VAL A CG1 1 
ATOM   866  C  CG2 . VAL A 1 119 ? 21.478  13.840  9.198   1.00 24.33 ? 107 VAL A CG2 1 
ATOM   867  N  N   . GLU A 1 120 ? 18.843  15.254  7.671   1.00 24.99 ? 108 GLU A N   1 
ATOM   868  C  CA  . GLU A 1 120 ? 18.013  14.875  6.503   1.00 25.89 ? 108 GLU A CA  1 
ATOM   869  C  C   . GLU A 1 120 ? 18.802  13.796  5.765   1.00 24.06 ? 108 GLU A C   1 
ATOM   870  O  O   . GLU A 1 120 ? 19.942  14.048  5.369   1.00 25.05 ? 108 GLU A O   1 
ATOM   871  C  CB  . GLU A 1 120 ? 17.651  16.120  5.679   1.00 31.01 ? 108 GLU A CB  1 
ATOM   872  C  CG  . GLU A 1 120 ? 18.331  16.207  4.321   1.00 38.32 ? 108 GLU A CG  1 
ATOM   873  C  CD  . GLU A 1 120 ? 17.885  17.353  3.427   1.00 46.32 ? 108 GLU A CD  1 
ATOM   874  O  OE1 . GLU A 1 120 ? 18.739  17.875  2.674   1.00 51.46 ? 108 GLU A OE1 1 
ATOM   875  O  OE2 . GLU A 1 120 ? 16.687  17.724  3.483   1.00 56.46 ? 108 GLU A OE2 1 
ATOM   876  N  N   . THR A 1 121 ? 18.250  12.600  5.649   1.00 21.02 ? 109 THR A N   1 
ATOM   877  C  CA  . THR A 1 121 ? 18.901  11.432  5.026   1.00 21.99 ? 109 THR A CA  1 
ATOM   878  C  C   . THR A 1 121 ? 17.835  10.389  4.657   1.00 19.93 ? 109 THR A C   1 
ATOM   879  O  O   . THR A 1 121 ? 16.819  10.291  5.382   1.00 20.17 ? 109 THR A O   1 
ATOM   880  C  CB  . THR A 1 121 ? 20.023  10.894  5.925   1.00 24.44 ? 109 THR A CB  1 
ATOM   881  O  OG1 . THR A 1 121 ? 20.593  9.727   5.347   1.00 25.79 ? 109 THR A OG1 1 
ATOM   882  C  CG2 . THR A 1 121 ? 19.567  10.561  7.332   1.00 25.31 ? 109 THR A CG2 1 
ATOM   883  N  N   . ASP A 1 122 ? 18.037  9.693   3.542   1.00 19.93 ? 110 ASP A N   1 
ATOM   884  C  CA  . ASP A 1 122 ? 17.237  8.516   3.122   1.00 20.73 ? 110 ASP A CA  1 
ATOM   885  C  C   . ASP A 1 122 ? 15.768  8.937   2.994   1.00 21.50 ? 110 ASP A C   1 
ATOM   886  O  O   . ASP A 1 122 ? 14.892  8.264   3.569   1.00 21.28 ? 110 ASP A O   1 
ATOM   887  C  CB  . ASP A 1 122 ? 17.526  7.372   4.095   1.00 19.83 ? 110 ASP A CB  1 
ATOM   888  C  CG  . ASP A 1 122 ? 19.013  7.064   4.213   1.00 17.46 ? 110 ASP A CG  1 
ATOM   889  O  OD1 . ASP A 1 122 ? 19.658  6.743   3.160   1.00 18.57 ? 110 ASP A OD1 1 
ATOM   890  O  OD2 . ASP A 1 122 ? 19.531  7.205   5.323   1.00 18.14 ? 110 ASP A OD2 1 
ATOM   891  N  N   . ASP A 1 123 ? 15.534  10.091  2.353   1.00 22.31 ? 111 ASP A N   1 
ATOM   892  C  CA  . ASP A 1 123 ? 14.191  10.657  2.012   1.00 23.08 ? 111 ASP A CA  1 
ATOM   893  C  C   . ASP A 1 123 ? 13.378  10.996  3.265   1.00 22.00 ? 111 ASP A C   1 
ATOM   894  O  O   . ASP A 1 123 ? 12.159  11.138  3.188   1.00 21.76 ? 111 ASP A O   1 
ATOM   895  C  CB  . ASP A 1 123 ? 13.477  9.774   1.000   1.00 25.88 ? 111 ASP A CB  1 
ATOM   896  C  CG  . ASP A 1 123 ? 13.992  10.040  -0.408  1.00 33.32 ? 111 ASP A CG  1 
ATOM   897  O  OD1 . ASP A 1 123 ? 15.242  10.023  -0.607  1.00 42.02 ? 111 ASP A OD1 1 
ATOM   898  O  OD2 . ASP A 1 123 ? 13.147  10.320  -1.298  1.00 42.57 ? 111 ASP A OD2 1 
ATOM   899  N  N   . GLY A 1 124 ? 14.047  11.263  4.373   1.00 21.55 ? 112 GLY A N   1 
ATOM   900  C  CA  . GLY A 1 124 ? 13.348  11.657  5.592   1.00 22.23 ? 112 GLY A CA  1 
ATOM   901  C  C   . GLY A 1 124 ? 14.158  12.616  6.420   1.00 21.65 ? 112 GLY A C   1 
ATOM   902  O  O   . GLY A 1 124 ? 15.283  13.006  5.997   1.00 22.72 ? 112 GLY A O   1 
ATOM   903  N  N   . THR A 1 125 ? 13.536  13.028  7.506   1.00 20.91 ? 113 THR A N   1 
ATOM   904  C  CA  . THR A 1 125 ? 14.087  13.958  8.514   1.00 22.83 ? 113 THR A CA  1 
ATOM   905  C  C   . THR A 1 125 ? 14.142  13.213  9.830   1.00 20.00 ? 113 THR A C   1 
ATOM   906  O  O   . THR A 1 125 ? 13.129  12.598  10.190  1.00 19.40 ? 113 THR A O   1 
ATOM   907  C  CB  . THR A 1 125 ? 13.236  15.228  8.600   1.00 24.07 ? 113 THR A CB  1 
ATOM   908  O  OG1 . THR A 1 125 ? 13.248  15.786  7.290   1.00 24.23 ? 113 THR A OG1 1 
ATOM   909  C  CG2 . THR A 1 125 ? 13.765  16.228  9.598   1.00 26.04 ? 113 THR A CG2 1 
ATOM   910  N  N   . TYR A 1 126 ? 15.259  13.305  10.549  1.00 19.72 ? 114 TYR A N   1 
ATOM   911  C  CA  . TYR A 1 126 ? 15.411  12.688  11.884  1.00 20.58 ? 114 TYR A CA  1 
ATOM   912  C  C   . TYR A 1 126 ? 15.762  13.800  12.878  1.00 18.84 ? 114 TYR A C   1 
ATOM   913  O  O   . TYR A 1 126 ? 16.619  14.620  12.577  1.00 22.88 ? 114 TYR A O   1 
ATOM   914  C  CB  . TYR A 1 126 ? 16.492  11.606  11.856  1.00 20.63 ? 114 TYR A CB  1 
ATOM   915  C  CG  . TYR A 1 126 ? 16.249  10.432  10.939  1.00 17.64 ? 114 TYR A CG  1 
ATOM   916  C  CD1 . TYR A 1 126 ? 16.370  10.540  9.558   1.00 17.72 ? 114 TYR A CD1 1 
ATOM   917  C  CD2 . TYR A 1 126 ? 15.962  9.180   11.460  1.00 17.14 ? 114 TYR A CD2 1 
ATOM   918  C  CE1 . TYR A 1 126 ? 16.170  9.458   8.726   1.00 16.67 ? 114 TYR A CE1 1 
ATOM   919  C  CE2 . TYR A 1 126 ? 15.813  8.083   10.642  1.00 17.04 ? 114 TYR A CE2 1 
ATOM   920  C  CZ  . TYR A 1 126 ? 15.872  8.228   9.268   1.00 17.07 ? 114 TYR A CZ  1 
ATOM   921  O  OH  . TYR A 1 126 ? 15.679  7.153   8.460   1.00 17.63 ? 114 TYR A OH  1 
ATOM   922  N  N   . LYS A 1 127 ? 15.077  13.826  14.025  1.00 20.81 ? 115 LYS A N   1 
ATOM   923  C  CA  . LYS A 1 127 ? 15.414  14.652  15.210  1.00 20.04 ? 115 LYS A CA  1 
ATOM   924  C  C   . LYS A 1 127 ? 16.481  13.944  16.036  1.00 20.05 ? 115 LYS A C   1 
ATOM   925  O  O   . LYS A 1 127 ? 16.347  12.692  16.249  1.00 17.84 ? 115 LYS A O   1 
ATOM   926  C  CB  . LYS A 1 127 ? 14.135  14.873  16.022  1.00 23.39 ? 115 LYS A CB  1 
ATOM   927  C  CG  . LYS A 1 127 ? 13.105  15.724  15.283  1.00 26.34 ? 115 LYS A CG  1 
ATOM   928  C  CD  . LYS A 1 127 ? 11.890  16.048  16.119  1.00 28.27 ? 115 LYS A CD  1 
ATOM   929  C  CE  . LYS A 1 127 ? 10.830  16.842  15.390  1.00 29.04 ? 115 LYS A CE  1 
ATOM   930  N  NZ  . LYS A 1 127 ? 9.533   16.745  16.105  1.00 31.72 ? 115 LYS A NZ  1 
ATOM   931  N  N   . ILE A 1 128 ? 17.483  14.691  16.486  1.00 17.32 ? 116 ILE A N   1 
ATOM   932  C  CA  . ILE A 1 128 ? 18.654  14.164  17.237  1.00 18.75 ? 116 ILE A CA  1 
ATOM   933  C  C   . ILE A 1 128 ? 18.476  14.467  18.728  1.00 18.89 ? 116 ILE A C   1 
ATOM   934  O  O   . ILE A 1 128 ? 18.120  15.631  19.084  1.00 19.14 ? 116 ILE A O   1 
ATOM   935  C  CB  . ILE A 1 128 ? 19.958  14.754  16.650  1.00 19.44 ? 116 ILE A CB  1 
ATOM   936  C  CG1 . ILE A 1 128 ? 20.163  14.296  15.208  1.00 20.07 ? 116 ILE A CG1 1 
ATOM   937  C  CG2 . ILE A 1 128 ? 21.131  14.423  17.544  1.00 19.22 ? 116 ILE A CG2 1 
ATOM   938  C  CD1 . ILE A 1 128 ? 21.187  15.095  14.430  1.00 21.59 ? 116 ILE A CD1 1 
ATOM   939  N  N   . TYR A 1 129 ? 18.686  13.459  19.570  1.00 16.86 ? 117 TYR A N   1 
ATOM   940  C  CA  . TYR A 1 129 ? 18.638  13.598  21.043  1.00 17.80 ? 117 TYR A CA  1 
ATOM   941  C  C   . TYR A 1 129 ? 19.807  12.876  21.697  1.00 18.06 ? 117 TYR A C   1 
ATOM   942  O  O   . TYR A 1 129 ? 20.334  11.846  21.168  1.00 18.32 ? 117 TYR A O   1 
ATOM   943  C  CB  . TYR A 1 129 ? 17.335  13.058  21.620  1.00 17.30 ? 117 TYR A CB  1 
ATOM   944  C  CG  . TYR A 1 129 ? 16.074  13.509  20.934  1.00 18.28 ? 117 TYR A CG  1 
ATOM   945  C  CD1 . TYR A 1 129 ? 15.614  12.892  19.788  1.00 21.18 ? 117 TYR A CD1 1 
ATOM   946  C  CD2 . TYR A 1 129 ? 15.346  14.582  21.451  1.00 22.67 ? 117 TYR A CD2 1 
ATOM   947  C  CE1 . TYR A 1 129 ? 14.424  13.287  19.188  1.00 21.97 ? 117 TYR A CE1 1 
ATOM   948  C  CE2 . TYR A 1 129 ? 14.177  15.012  20.835  1.00 22.70 ? 117 TYR A CE2 1 
ATOM   949  C  CZ  . TYR A 1 129 ? 13.738  14.389  19.686  1.00 24.32 ? 117 TYR A CZ  1 
ATOM   950  O  OH  . TYR A 1 129 ? 12.566  14.812  19.109  1.00 21.73 ? 117 TYR A OH  1 
ATOM   951  N  N   . GLN A 1 130 ? 20.138  13.320  22.900  1.00 16.66 ? 118 GLN A N   1 
ATOM   952  C  CA  . GLN A 1 130 ? 21.059  12.569  23.766  1.00 20.72 ? 118 GLN A CA  1 
ATOM   953  C  C   . GLN A 1 130 ? 20.413  12.396  25.134  1.00 22.78 ? 118 GLN A C   1 
ATOM   954  O  O   . GLN A 1 130 ? 19.770  13.313  25.636  1.00 20.45 ? 118 GLN A O   1 
ATOM   955  C  CB  . GLN A 1 130 ? 22.453  13.164  23.922  1.00 22.38 ? 118 GLN A CB  1 
ATOM   956  C  CG  . GLN A 1 130 ? 23.222  12.383  24.970  1.00 28.03 ? 118 GLN A CG  1 
ATOM   957  C  CD  . GLN A 1 130 ? 24.497  13.044  25.405  1.00 33.74 ? 118 GLN A CD  1 
ATOM   958  O  OE1 . GLN A 1 130 ? 24.687  14.254  25.258  1.00 37.45 ? 118 GLN A OE1 1 
ATOM   959  N  NE2 . GLN A 1 130 ? 25.369  12.222  25.946  1.00 32.91 ? 118 GLN A NE2 1 
ATOM   960  N  N   . THR A 1 131 ? 20.561  11.205  25.699  1.00 23.07 ? 119 THR A N   1 
ATOM   961  C  CA  . THR A 1 131 ? 20.169  10.943  27.101  1.00 27.39 ? 119 THR A CA  1 
ATOM   962  C  C   . THR A 1 131 ? 21.283  10.142  27.785  1.00 27.13 ? 119 THR A C   1 
ATOM   963  O  O   . THR A 1 131 ? 22.364  9.919   27.165  1.00 25.21 ? 119 THR A O   1 
ATOM   964  C  CB  . THR A 1 131 ? 18.784  10.287  27.192  1.00 30.58 ? 119 THR A CB  1 
ATOM   965  O  OG1 . THR A 1 131 ? 18.824  8.981   26.604  1.00 29.14 ? 119 THR A OG1 1 
ATOM   966  C  CG2 . THR A 1 131 ? 17.685  11.098  26.541  1.00 34.30 ? 119 THR A CG2 1 
ATOM   967  N  N   . THR A 1 132 ? 21.042  9.804   29.048  1.00 30.27 ? 120 THR A N   1 
ATOM   968  C  CA  . THR A 1 132 ? 21.945  8.985   29.896  1.00 32.89 ? 120 THR A CA  1 
ATOM   969  C  C   . THR A 1 132 ? 21.170  7.807   30.493  1.00 29.52 ? 120 THR A C   1 
ATOM   970  O  O   . THR A 1 132 ? 20.023  7.986   30.884  1.00 35.25 ? 120 THR A O   1 
ATOM   971  C  CB  . THR A 1 132 ? 22.604  9.841   30.987  1.00 35.73 ? 120 THR A CB  1 
ATOM   972  O  OG1 . THR A 1 132 ? 23.616  10.594  30.327  1.00 40.88 ? 120 THR A OG1 1 
ATOM   973  C  CG2 . THR A 1 132 ? 23.228  9.019   32.093  1.00 39.24 ? 120 THR A CG2 1 
ATOM   974  N  N   . ARG A 1 133 ? 21.808  6.644   30.566  1.00 24.95 ? 121 ARG A N   1 
ATOM   975  C  CA  . ARG A 1 133 ? 21.323  5.434   31.262  1.00 23.42 ? 121 ARG A CA  1 
ATOM   976  C  C   . ARG A 1 133 ? 22.246  5.194   32.452  1.00 22.45 ? 121 ARG A C   1 
ATOM   977  O  O   . ARG A 1 133 ? 23.460  5.183   32.245  1.00 21.41 ? 121 ARG A O   1 
ATOM   978  C  CB  . ARG A 1 133 ? 21.329  4.255   30.282  1.00 23.75 ? 121 ARG A CB  1 
ATOM   979  C  CG  . ARG A 1 133 ? 20.267  4.370   29.195  1.00 24.45 ? 121 ARG A CG  1 
ATOM   980  C  CD  . ARG A 1 133 ? 18.913  3.951   29.719  1.00 25.60 ? 121 ARG A CD  1 
ATOM   981  N  NE  . ARG A 1 133 ? 18.834  2.493   29.767  1.00 27.67 ? 121 ARG A NE  1 
ATOM   982  C  CZ  . ARG A 1 133 ? 18.245  1.753   30.701  1.00 26.63 ? 121 ARG A CZ  1 
ATOM   983  N  NH1 . ARG A 1 133 ? 17.648  2.294   31.745  1.00 29.36 ? 121 ARG A NH1 1 
ATOM   984  N  NH2 . ARG A 1 133 ? 18.271  0.443   30.596  1.00 30.53 ? 121 ARG A NH2 1 
ATOM   985  N  N   . GLU A 1 134 ? 21.697  5.127   33.654  1.00 23.14 ? 122 GLU A N   1 
ATOM   986  C  CA  . GLU A 1 134 ? 22.530  4.946   34.867  1.00 27.61 ? 122 GLU A CA  1 
ATOM   987  C  C   . GLU A 1 134 ? 22.289  3.539   35.412  1.00 24.38 ? 122 GLU A C   1 
ATOM   988  O  O   . GLU A 1 134 ? 21.132  3.151   35.549  1.00 24.84 ? 122 GLU A O   1 
ATOM   989  C  CB  . GLU A 1 134 ? 22.295  6.087   35.851  1.00 31.90 ? 122 GLU A CB  1 
ATOM   990  C  CG  . GLU A 1 134 ? 22.710  7.426   35.254  1.00 36.84 ? 122 GLU A CG  1 
ATOM   991  C  CD  . GLU A 1 134 ? 22.233  8.660   35.997  1.00 46.52 ? 122 GLU A CD  1 
ATOM   992  O  OE1 . GLU A 1 134 ? 22.785  8.947   37.082  1.00 51.77 ? 122 GLU A OE1 1 
ATOM   993  O  OE2 . GLU A 1 134 ? 21.288  9.313   35.499  1.00 53.26 ? 122 GLU A OE2 1 
ATOM   994  N  N   . ASN A 1 135 ? 23.377  2.845   35.719  1.00 25.39 ? 123 ASN A N   1 
ATOM   995  C  CA  . ASN A 1 135 ? 23.364  1.527   36.402  1.00 27.16 ? 123 ASN A CA  1 
ATOM   996  C  C   . ASN A 1 135 ? 22.481  0.579   35.570  1.00 25.22 ? 123 ASN A C   1 
ATOM   997  O  O   . ASN A 1 135 ? 21.601  -0.068  36.143  1.00 23.82 ? 123 ASN A O   1 
ATOM   998  C  CB  . ASN A 1 135 ? 22.929  1.744   37.860  1.00 29.48 ? 123 ASN A CB  1 
ATOM   999  C  CG  . ASN A 1 135 ? 24.067  1.914   38.849  1.00 34.32 ? 123 ASN A CG  1 
ATOM   1000 O  OD1 . ASN A 1 135 ? 25.238  2.060   38.488  1.00 28.95 ? 123 ASN A OD1 1 
ATOM   1001 N  ND2 . ASN A 1 135 ? 23.730  1.833   40.128  1.00 39.66 ? 123 ASN A ND2 1 
ATOM   1002 N  N   . ALA A 1 136 ? 22.693  0.559   34.253  1.00 21.59 ? 124 ALA A N   1 
ATOM   1003 C  CA  . ALA A 1 136 ? 21.786  -0.054  33.240  1.00 22.02 ? 124 ALA A CA  1 
ATOM   1004 C  C   . ALA A 1 136 ? 22.462  -1.261  32.585  1.00 20.69 ? 124 ALA A C   1 
ATOM   1005 O  O   . ALA A 1 136 ? 23.693  -1.319  32.498  1.00 22.68 ? 124 ALA A O   1 
ATOM   1006 C  CB  . ALA A 1 136 ? 21.421  0.997   32.226  1.00 22.60 ? 124 ALA A CB  1 
ATOM   1007 N  N   . PRO A 1 137 ? 21.710  -2.267  32.075  1.00 18.03 ? 125 PRO A N   1 
ATOM   1008 C  CA  . PRO A 1 137 ? 22.311  -3.351  31.307  1.00 18.23 ? 125 PRO A CA  1 
ATOM   1009 C  C   . PRO A 1 137 ? 23.041  -2.799  30.081  1.00 20.13 ? 125 PRO A C   1 
ATOM   1010 O  O   . PRO A 1 137 ? 22.646  -1.771  29.509  1.00 17.52 ? 125 PRO A O   1 
ATOM   1011 C  CB  . PRO A 1 137 ? 21.150  -4.209  30.832  1.00 19.70 ? 125 PRO A CB  1 
ATOM   1012 C  CG  . PRO A 1 137 ? 20.072  -3.939  31.854  1.00 20.25 ? 125 PRO A CG  1 
ATOM   1013 C  CD  . PRO A 1 137 ? 20.262  -2.482  32.242  1.00 19.19 ? 125 PRO A CD  1 
ATOM   1014 N  N   . SER A 1 138 ? 24.146  -3.440  29.767  1.00 16.77 ? 126 SER A N   1 
ATOM   1015 C  CA  . SER A 1 138 ? 24.954  -3.030  28.594  1.00 16.67 ? 126 SER A CA  1 
ATOM   1016 C  C   . SER A 1 138 ? 25.796  -4.185  28.092  1.00 15.36 ? 126 SER A C   1 
ATOM   1017 O  O   . SER A 1 138 ? 25.810  -5.250  28.712  1.00 18.19 ? 126 SER A O   1 
ATOM   1018 C  CB  . SER A 1 138 ? 25.814  -1.816  28.880  1.00 15.71 ? 126 SER A CB  1 
ATOM   1019 O  OG  . SER A 1 138 ? 27.046  -2.164  29.543  1.00 17.32 ? 126 SER A OG  1 
ATOM   1020 N  N   . ILE A 1 139 ? 26.483  -3.971  26.971  1.00 15.16 ? 127 ILE A N   1 
ATOM   1021 C  CA  . ILE A 1 139 ? 27.367  -4.997  26.353  1.00 17.33 ? 127 ILE A CA  1 
ATOM   1022 C  C   . ILE A 1 139 ? 28.592  -5.175  27.270  1.00 18.22 ? 127 ILE A C   1 
ATOM   1023 O  O   . ILE A 1 139 ? 29.367  -6.132  27.053  1.00 20.12 ? 127 ILE A O   1 
ATOM   1024 C  CB  . ILE A 1 139 ? 27.781  -4.631  24.912  1.00 15.79 ? 127 ILE A CB  1 
ATOM   1025 C  CG1 . ILE A 1 139 ? 28.471  -3.257  24.857  1.00 15.71 ? 127 ILE A CG1 1 
ATOM   1026 C  CG2 . ILE A 1 139 ? 26.588  -4.717  23.960  1.00 15.77 ? 127 ILE A CG2 1 
ATOM   1027 C  CD1 . ILE A 1 139 ? 29.317  -2.972  23.600  1.00 16.53 ? 127 ILE A CD1 1 
ATOM   1028 N  N   . GLU A 1 140 ? 28.713  -4.338  28.292  1.00 19.49 ? 128 GLU A N   1 
ATOM   1029 C  CA  . GLU A 1 140 ? 29.851  -4.428  29.262  1.00 22.22 ? 128 GLU A CA  1 
ATOM   1030 C  C   . GLU A 1 140 ? 29.340  -4.873  30.634  1.00 23.43 ? 128 GLU A C   1 
ATOM   1031 O  O   . GLU A 1 140 ? 30.158  -4.861  31.610  1.00 23.46 ? 128 GLU A O   1 
ATOM   1032 C  CB  . GLU A 1 140 ? 30.560  -3.070  29.384  1.00 24.06 ? 128 GLU A CB  1 
ATOM   1033 C  CG  . GLU A 1 140 ? 31.276  -2.637  28.115  1.00 26.07 ? 128 GLU A CG  1 
ATOM   1034 C  CD  . GLU A 1 140 ? 32.554  -1.844  28.319  1.00 38.64 ? 128 GLU A CD  1 
ATOM   1035 O  OE1 . GLU A 1 140 ? 33.383  -1.774  27.352  1.00 44.13 ? 128 GLU A OE1 1 
ATOM   1036 O  OE2 . GLU A 1 140 ? 32.742  -1.301  29.441  1.00 50.80 ? 128 GLU A OE2 1 
ATOM   1037 N  N   . GLY A 1 141 ? 28.050  -5.214  30.751  1.00 19.62 ? 129 GLY A N   1 
ATOM   1038 C  CA  . GLY A 1 141 ? 27.433  -5.486  32.060  1.00 20.55 ? 129 GLY A CA  1 
ATOM   1039 C  C   . GLY A 1 141 ? 26.811  -4.242  32.651  1.00 20.83 ? 129 GLY A C   1 
ATOM   1040 O  O   . GLY A 1 141 ? 26.661  -3.272  31.909  1.00 21.99 ? 129 GLY A O   1 
ATOM   1041 N  N   . THR A 1 142 ? 26.473  -4.221  33.948  1.00 21.78 ? 130 THR A N   1 
ATOM   1042 C  CA  . THR A 1 142 ? 25.796  -3.051  34.546  1.00 20.70 ? 130 THR A CA  1 
ATOM   1043 C  C   . THR A 1 142 ? 26.677  -1.812  34.380  1.00 22.01 ? 130 THR A C   1 
ATOM   1044 O  O   . THR A 1 142 ? 27.833  -1.894  34.793  1.00 23.09 ? 130 THR A O   1 
ATOM   1045 C  CB  . THR A 1 142 ? 25.476  -3.268  36.018  1.00 22.26 ? 130 THR A CB  1 
ATOM   1046 O  OG1 . THR A 1 142 ? 24.701  -4.457  35.966  1.00 22.80 ? 130 THR A OG1 1 
ATOM   1047 C  CG2 . THR A 1 142 ? 24.751  -2.096  36.616  1.00 21.91 ? 130 THR A CG2 1 
ATOM   1048 N  N   . ALA A 1 143 ? 26.160  -0.728  33.804  1.00 21.77 ? 131 ALA A N   1 
ATOM   1049 C  CA  . ALA A 1 143 ? 26.986  0.439   33.416  1.00 23.04 ? 131 ALA A CA  1 
ATOM   1050 C  C   . ALA A 1 143 ? 26.160  1.722   33.306  1.00 24.42 ? 131 ALA A C   1 
ATOM   1051 O  O   . ALA A 1 143 ? 24.902  1.660   33.198  1.00 24.26 ? 131 ALA A O   1 
ATOM   1052 C  CB  . ALA A 1 143 ? 27.733  0.160   32.138  1.00 21.36 ? 131 ALA A CB  1 
ATOM   1053 N  N   . THR A 1 144 ? 26.886  2.843   33.305  1.00 22.81 ? 132 THR A N   1 
ATOM   1054 C  CA  . THR A 1 144 ? 26.414  4.224   33.020  1.00 22.85 ? 132 THR A CA  1 
ATOM   1055 C  C   . THR A 1 144 ? 26.932  4.622   31.632  1.00 22.43 ? 132 THR A C   1 
ATOM   1056 O  O   . THR A 1 144 ? 28.104  4.438   31.311  1.00 22.56 ? 132 THR A O   1 
ATOM   1057 C  CB  . THR A 1 144 ? 26.774  5.199   34.152  1.00 23.58 ? 132 THR A CB  1 
ATOM   1058 O  OG1 . THR A 1 144 ? 26.069  4.809   35.330  1.00 26.03 ? 132 THR A OG1 1 
ATOM   1059 C  CG2 . THR A 1 144 ? 26.382  6.626   33.834  1.00 27.47 ? 132 THR A CG2 1 
ATOM   1060 N  N   . PHE A 1 145 ? 26.040  5.035   30.737  1.00 22.44 ? 133 PHE A N   1 
ATOM   1061 C  CA  . PHE A 1 145 ? 26.478  5.309   29.348  1.00 22.66 ? 133 PHE A CA  1 
ATOM   1062 C  C   . PHE A 1 145 ? 25.534  6.318   28.711  1.00 19.47 ? 133 PHE A C   1 
ATOM   1063 O  O   . PHE A 1 145 ? 24.388  6.452   29.193  1.00 21.02 ? 133 PHE A O   1 
ATOM   1064 C  CB  . PHE A 1 145 ? 26.581  3.996   28.565  1.00 22.83 ? 133 PHE A CB  1 
ATOM   1065 C  CG  . PHE A 1 145 ? 25.334  3.160   28.611  1.00 20.61 ? 133 PHE A CG  1 
ATOM   1066 C  CD1 . PHE A 1 145 ? 24.297  3.335   27.690  1.00 20.17 ? 133 PHE A CD1 1 
ATOM   1067 C  CD2 . PHE A 1 145 ? 25.179  2.204   29.599  1.00 21.39 ? 133 PHE A CD2 1 
ATOM   1068 C  CE1 . PHE A 1 145 ? 23.152  2.568   27.773  1.00 19.53 ? 133 PHE A CE1 1 
ATOM   1069 C  CE2 . PHE A 1 145 ? 24.035  1.421   29.654  1.00 21.88 ? 133 PHE A CE2 1 
ATOM   1070 C  CZ  . PHE A 1 145 ? 23.038  1.584   28.716  1.00 19.17 ? 133 PHE A CZ  1 
ATOM   1071 N  N   . ASN A 1 146 ? 26.050  6.958   27.667  1.00 20.55 ? 134 ASN A N   1 
ATOM   1072 C  CA  . ASN A 1 146 ? 25.331  7.926   26.804  1.00 22.63 ? 134 ASN A CA  1 
ATOM   1073 C  C   . ASN A 1 146 ? 24.437  7.091   25.863  1.00 19.85 ? 134 ASN A C   1 
ATOM   1074 O  O   . ASN A 1 146 ? 24.833  5.969   25.412  1.00 16.63 ? 134 ASN A O   1 
ATOM   1075 C  CB  . ASN A 1 146 ? 26.277  8.823   25.980  1.00 24.47 ? 134 ASN A CB  1 
ATOM   1076 C  CG  . ASN A 1 146 ? 27.176  9.755   26.773  1.00 31.65 ? 134 ASN A CG  1 
ATOM   1077 O  OD1 . ASN A 1 146 ? 26.786  10.280  27.813  1.00 30.64 ? 134 ASN A OD1 1 
ATOM   1078 N  ND2 . ASN A 1 146 ? 28.353  10.027  26.222  1.00 34.80 ? 134 ASN A ND2 1 
ATOM   1079 N  N   . GLN A 1 147 ? 23.237  7.598   25.605  1.00 17.89 ? 135 GLN A N   1 
ATOM   1080 C  CA  . GLN A 1 147 ? 22.334  7.067   24.551  1.00 18.42 ? 135 GLN A CA  1 
ATOM   1081 C  C   . GLN A 1 147 ? 22.109  8.141   23.517  1.00 17.25 ? 135 GLN A C   1 
ATOM   1082 O  O   . GLN A 1 147 ? 21.697  9.269   23.922  1.00 18.89 ? 135 GLN A O   1 
ATOM   1083 C  CB  . GLN A 1 147 ? 20.953  6.810   25.161  1.00 21.11 ? 135 GLN A CB  1 
ATOM   1084 C  CG  . GLN A 1 147 ? 20.588  5.366   25.293  1.00 22.65 ? 135 GLN A CG  1 
ATOM   1085 C  CD  . GLN A 1 147 ? 19.190  5.212   25.859  1.00 21.99 ? 135 GLN A CD  1 
ATOM   1086 O  OE1 . GLN A 1 147 ? 18.547  6.194   26.253  1.00 28.27 ? 135 GLN A OE1 1 
ATOM   1087 N  NE2 . GLN A 1 147 ? 18.730  3.980   25.948  1.00 19.76 ? 135 GLN A NE2 1 
ATOM   1088 N  N   . TYR A 1 148 ? 22.319  7.862   22.233  1.00 16.88 ? 136 TYR A N   1 
ATOM   1089 C  CA  . TYR A 1 148 ? 22.079  8.852   21.161  1.00 16.04 ? 136 TYR A CA  1 
ATOM   1090 C  C   . TYR A 1 148 ? 20.879  8.362   20.360  1.00 16.05 ? 136 TYR A C   1 
ATOM   1091 O  O   . TYR A 1 148 ? 20.738  7.094   20.208  1.00 15.31 ? 136 TYR A O   1 
ATOM   1092 C  CB  . TYR A 1 148 ? 23.305  9.022   20.263  1.00 15.12 ? 136 TYR A CB  1 
ATOM   1093 C  CG  . TYR A 1 148 ? 24.572  9.404   20.996  1.00 17.15 ? 136 TYR A CG  1 
ATOM   1094 C  CD1 . TYR A 1 148 ? 24.557  9.976   22.263  1.00 17.36 ? 136 TYR A CD1 1 
ATOM   1095 C  CD2 . TYR A 1 148 ? 25.785  9.255   20.372  1.00 15.31 ? 136 TYR A CD2 1 
ATOM   1096 C  CE1 . TYR A 1 148 ? 25.732  10.328  22.912  1.00 17.50 ? 136 TYR A CE1 1 
ATOM   1097 C  CE2 . TYR A 1 148 ? 26.975  9.585   21.009  1.00 18.03 ? 136 TYR A CE2 1 
ATOM   1098 C  CZ  . TYR A 1 148 ? 26.949  10.122  22.281  1.00 19.75 ? 136 TYR A CZ  1 
ATOM   1099 O  OH  . TYR A 1 148 ? 28.109  10.479  22.912  1.00 21.22 ? 136 TYR A OH  1 
ATOM   1100 N  N   . TRP A 1 149 ? 20.030  9.283   19.946  1.00 15.49 ? 137 TRP A N   1 
ATOM   1101 C  CA  . TRP A 1 149 ? 18.806  8.995   19.165  1.00 15.92 ? 137 TRP A CA  1 
ATOM   1102 C  C   . TRP A 1 149 ? 18.822  9.783   17.853  1.00 16.40 ? 137 TRP A C   1 
ATOM   1103 O  O   . TRP A 1 149 ? 19.130  10.991  17.878  1.00 17.06 ? 137 TRP A O   1 
ATOM   1104 C  CB  . TRP A 1 149 ? 17.589  9.319   20.009  1.00 16.08 ? 137 TRP A CB  1 
ATOM   1105 C  CG  . TRP A 1 149 ? 17.505  8.576   21.297  1.00 18.60 ? 137 TRP A CG  1 
ATOM   1106 C  CD1 . TRP A 1 149 ? 18.029  8.940   22.509  1.00 19.34 ? 137 TRP A CD1 1 
ATOM   1107 C  CD2 . TRP A 1 149 ? 16.854  7.314   21.494  1.00 17.87 ? 137 TRP A CD2 1 
ATOM   1108 N  NE1 . TRP A 1 149 ? 17.720  7.998   23.454  1.00 18.99 ? 137 TRP A NE1 1 
ATOM   1109 C  CE2 . TRP A 1 149 ? 16.990  7.001   22.862  1.00 19.86 ? 137 TRP A CE2 1 
ATOM   1110 C  CE3 . TRP A 1 149 ? 16.095  6.464   20.673  1.00 17.23 ? 137 TRP A CE3 1 
ATOM   1111 C  CZ2 . TRP A 1 149 ? 16.427  5.849   23.403  1.00 20.49 ? 137 TRP A CZ2 1 
ATOM   1112 C  CZ3 . TRP A 1 149 ? 15.581  5.306   21.200  1.00 18.74 ? 137 TRP A CZ3 1 
ATOM   1113 C  CH2 . TRP A 1 149 ? 15.736  5.020   22.559  1.00 19.25 ? 137 TRP A CH2 1 
ATOM   1114 N  N   . SER A 1 150 ? 18.443  9.135   16.747  1.00 18.18 ? 138 SER A N   1 
ATOM   1115 C  CA  . SER A 1 150 ? 17.918  9.782   15.515  1.00 17.45 ? 138 SER A CA  1 
ATOM   1116 C  C   . SER A 1 150 ? 16.530  9.199   15.318  1.00 15.98 ? 138 SER A C   1 
ATOM   1117 O  O   . SER A 1 150 ? 16.438  7.953   15.209  1.00 16.74 ? 138 SER A O   1 
ATOM   1118 C  CB  . SER A 1 150 ? 18.710  9.549   14.239  1.00 18.80 ? 138 SER A CB  1 
ATOM   1119 O  OG  . SER A 1 150 ? 19.843  10.332  14.174  1.00 26.08 ? 138 SER A OG  1 
ATOM   1120 N  N   . VAL A 1 151 ? 15.497  10.047  15.357  1.00 15.39 ? 139 VAL A N   1 
ATOM   1121 C  CA  . VAL A 1 151 ? 14.080  9.591   15.354  1.00 16.56 ? 139 VAL A CA  1 
ATOM   1122 C  C   . VAL A 1 151 ? 13.415  10.160  14.103  1.00 16.37 ? 139 VAL A C   1 
ATOM   1123 O  O   . VAL A 1 151 ? 13.275  11.417  13.965  1.00 17.24 ? 139 VAL A O   1 
ATOM   1124 C  CB  . VAL A 1 151 ? 13.334  9.960   16.647  1.00 16.13 ? 139 VAL A CB  1 
ATOM   1125 C  CG1 . VAL A 1 151 ? 11.918  9.400   16.669  1.00 17.39 ? 139 VAL A CG1 1 
ATOM   1126 C  CG2 . VAL A 1 151 ? 14.136  9.551   17.891  1.00 17.76 ? 139 VAL A CG2 1 
ATOM   1127 N  N   . ARG A 1 152 ? 13.075  9.286   13.206  1.00 15.31 ? 140 ARG A N   1 
ATOM   1128 C  CA  . ARG A 1 152 ? 12.462  9.645   11.902  1.00 17.01 ? 140 ARG A CA  1 
ATOM   1129 C  C   . ARG A 1 152 ? 11.114  10.297  12.171  1.00 18.13 ? 140 ARG A C   1 
ATOM   1130 O  O   . ARG A 1 152 ? 10.361  9.778   13.023  1.00 16.78 ? 140 ARG A O   1 
ATOM   1131 C  CB  . ARG A 1 152 ? 12.296  8.417   11.019  1.00 17.29 ? 140 ARG A CB  1 
ATOM   1132 C  CG  . ARG A 1 152 ? 12.186  8.766   9.546   1.00 17.84 ? 140 ARG A CG  1 
ATOM   1133 C  CD  . ARG A 1 152 ? 12.076  7.558   8.667   1.00 16.71 ? 140 ARG A CD  1 
ATOM   1134 N  NE  . ARG A 1 152 ? 11.692  7.870   7.290   1.00 18.23 ? 140 ARG A NE  1 
ATOM   1135 C  CZ  . ARG A 1 152 ? 12.516  8.061   6.271   1.00 16.07 ? 140 ARG A CZ  1 
ATOM   1136 N  NH1 . ARG A 1 152 ? 13.832  8.007   6.408   1.00 18.30 ? 140 ARG A NH1 1 
ATOM   1137 N  NH2 . ARG A 1 152 ? 12.013  8.267   5.069   1.00 18.64 ? 140 ARG A NH2 1 
ATOM   1138 N  N   . THR A 1 153 ? 10.866  11.466  11.555  1.00 18.51 ? 141 THR A N   1 
ATOM   1139 C  CA  . THR A 1 153 ? 9.593   12.193  11.743  1.00 19.64 ? 141 THR A CA  1 
ATOM   1140 C  C   . THR A 1 153 ? 8.438   11.504  11.006  1.00 19.63 ? 141 THR A C   1 
ATOM   1141 O  O   . THR A 1 153 ? 7.304   11.710  11.451  1.00 22.86 ? 141 THR A O   1 
ATOM   1142 C  CB  . THR A 1 153 ? 9.750   13.678  11.375  1.00 20.15 ? 141 THR A CB  1 
ATOM   1143 O  OG1 . THR A 1 153 ? 9.891   13.793  9.959   1.00 20.29 ? 141 THR A OG1 1 
ATOM   1144 C  CG2 . THR A 1 153 ? 10.928  14.299  12.088  1.00 21.44 ? 141 THR A CG2 1 
ATOM   1145 N  N   . ASP A 1 154 ? 8.692   10.794  9.898   1.00 21.04 ? 142 ASP A N   1 
ATOM   1146 C  CA  . ASP A 1 154 ? 7.685   10.072  9.067   1.00 21.15 ? 142 ASP A CA  1 
ATOM   1147 C  C   . ASP A 1 154 ? 8.012   8.586   9.198   1.00 18.32 ? 142 ASP A C   1 
ATOM   1148 O  O   . ASP A 1 154 ? 8.918   8.077   8.512   1.00 21.09 ? 142 ASP A O   1 
ATOM   1149 C  CB  . ASP A 1 154 ? 7.692   10.501  7.595   1.00 24.52 ? 142 ASP A CB  1 
ATOM   1150 C  CG  . ASP A 1 154 ? 6.597   9.889   6.709   1.00 27.43 ? 142 ASP A CG  1 
ATOM   1151 O  OD1 . ASP A 1 154 ? 6.139   8.778   6.988   1.00 30.65 ? 142 ASP A OD1 1 
ATOM   1152 O  OD2 . ASP A 1 154 ? 6.281   10.492  5.676   1.00 33.86 ? 142 ASP A OD2 1 
ATOM   1153 N  N   . HIS A 1 155 ? 7.306   7.923   10.088  1.00 18.85 ? 143 HIS A N   1 
ATOM   1154 C  CA  . HIS A 1 155 ? 7.614   6.508   10.419  1.00 17.80 ? 143 HIS A CA  1 
ATOM   1155 C  C   . HIS A 1 155 ? 7.519   5.648   9.175   1.00 17.92 ? 143 HIS A C   1 
ATOM   1156 O  O   . HIS A 1 155 ? 6.601   5.857   8.342   1.00 16.85 ? 143 HIS A O   1 
ATOM   1157 C  CB  . HIS A 1 155 ? 6.714   6.008   11.541  1.00 19.51 ? 143 HIS A CB  1 
ATOM   1158 C  CG  . HIS A 1 155 ? 6.973   6.696   12.839  1.00 21.21 ? 143 HIS A CG  1 
ATOM   1159 N  ND1 . HIS A 1 155 ? 6.249   6.410   13.976  1.00 21.01 ? 143 HIS A ND1 1 
ATOM   1160 C  CD2 . HIS A 1 155 ? 7.832   7.680   13.173  1.00 21.49 ? 143 HIS A CD2 1 
ATOM   1161 C  CE1 . HIS A 1 155 ? 6.643   7.179   14.966  1.00 21.47 ? 143 HIS A CE1 1 
ATOM   1162 N  NE2 . HIS A 1 155 ? 7.616   7.996   14.497  1.00 23.80 ? 143 HIS A NE2 1 
ATOM   1163 N  N   . ARG A 1 156 ? 8.390   4.650   9.073   1.00 16.84 ? 144 ARG A N   1 
ATOM   1164 C  CA  . ARG A 1 156 ? 8.379   3.702   7.942   1.00 14.92 ? 144 ARG A CA  1 
ATOM   1165 C  C   . ARG A 1 156 ? 8.904   2.349   8.397   1.00 15.13 ? 144 ARG A C   1 
ATOM   1166 O  O   . ARG A 1 156 ? 9.557   2.273   9.484   1.00 16.57 ? 144 ARG A O   1 
ATOM   1167 C  CB  . ARG A 1 156 ? 9.184   4.202   6.741   1.00 14.22 ? 144 ARG A CB  1 
ATOM   1168 C  CG  . ARG A 1 156 ? 10.657  4.336   7.042   1.00 14.97 ? 144 ARG A CG  1 
ATOM   1169 C  CD  . ARG A 1 156 ? 11.427  4.625   5.762   1.00 15.20 ? 144 ARG A CD  1 
ATOM   1170 N  NE  . ARG A 1 156 ? 12.829  4.668   6.129   1.00 15.26 ? 144 ARG A NE  1 
ATOM   1171 C  CZ  . ARG A 1 156 ? 13.829  4.818   5.269   1.00 17.74 ? 144 ARG A CZ  1 
ATOM   1172 N  NH1 . ARG A 1 156 ? 13.601  5.113   3.992   1.00 20.41 ? 144 ARG A NH1 1 
ATOM   1173 N  NH2 . ARG A 1 156 ? 15.056  4.732   5.740   1.00 18.85 ? 144 ARG A NH2 1 
ATOM   1174 N  N   . VAL A 1 157 ? 8.591   1.340   7.586   1.00 15.59 ? 145 VAL A N   1 
ATOM   1175 C  CA  . VAL A 1 157 ? 9.055   -0.079  7.684   1.00 15.00 ? 145 VAL A CA  1 
ATOM   1176 C  C   . VAL A 1 157 ? 9.705   -0.470  6.364   1.00 16.67 ? 145 VAL A C   1 
ATOM   1177 O  O   . VAL A 1 157 ? 9.000   -0.779  5.389   1.00 18.23 ? 145 VAL A O   1 
ATOM   1178 C  CB  . VAL A 1 157 ? 7.935   -1.049  8.067   1.00 18.34 ? 145 VAL A CB  1 
ATOM   1179 C  CG1 . VAL A 1 157 ? 8.514   -2.455  8.222   1.00 17.44 ? 145 VAL A CG1 1 
ATOM   1180 C  CG2 . VAL A 1 157 ? 7.197   -0.583  9.311   1.00 18.90 ? 145 VAL A CG2 1 
ATOM   1181 N  N   . GLY A 1 158 ? 11.028  -0.416  6.353   1.00 17.22 ? 146 GLY A N   1 
ATOM   1182 C  CA  . GLY A 1 158 ? 11.850  -0.727  5.190   1.00 18.01 ? 146 GLY A CA  1 
ATOM   1183 C  C   . GLY A 1 158 ? 12.499  0.503   4.623   1.00 20.81 ? 146 GLY A C   1 
ATOM   1184 O  O   . GLY A 1 158 ? 12.160  1.603   5.029   1.00 25.02 ? 146 GLY A O   1 
ATOM   1185 N  N   . GLY A 1 159 ? 13.426  0.276   3.719   1.00 21.86 ? 147 GLY A N   1 
ATOM   1186 C  CA  . GLY A 1 159 ? 14.162  1.325   3.002   1.00 19.50 ? 147 GLY A CA  1 
ATOM   1187 C  C   . GLY A 1 159 ? 15.640  1.220   3.315   1.00 19.25 ? 147 GLY A C   1 
ATOM   1188 O  O   . GLY A 1 159 ? 16.113  0.118   3.662   1.00 19.86 ? 147 GLY A O   1 
ATOM   1189 N  N   . THR A 1 160 ? 16.340  2.341   3.126   1.00 17.95 ? 148 THR A N   1 
ATOM   1190 C  CA  . THR A 1 160 ? 17.805  2.444   3.229   1.00 18.24 ? 148 THR A CA  1 
ATOM   1191 C  C   . THR A 1 160 ? 18.114  3.328   4.436   1.00 16.01 ? 148 THR A C   1 
ATOM   1192 O  O   . THR A 1 160 ? 17.504  4.395   4.611   1.00 17.04 ? 148 THR A O   1 
ATOM   1193 C  CB  . THR A 1 160 ? 18.412  2.983   1.922   1.00 19.55 ? 148 THR A CB  1 
ATOM   1194 O  OG1 . THR A 1 160 ? 18.017  2.112   0.855   1.00 23.91 ? 148 THR A OG1 1 
ATOM   1195 C  CG2 . THR A 1 160 ? 19.918  3.090   1.984   1.00 20.13 ? 148 THR A CG2 1 
ATOM   1196 N  N   . VAL A 1 161 ? 19.082  2.928   5.248   1.00 15.30 ? 149 VAL A N   1 
ATOM   1197 C  CA  . VAL A 1 161 ? 19.666  3.787   6.299   1.00 16.14 ? 149 VAL A CA  1 
ATOM   1198 C  C   . VAL A 1 161 ? 21.153  4.008   6.014   1.00 16.15 ? 149 VAL A C   1 
ATOM   1199 O  O   . VAL A 1 161 ? 21.909  3.062   6.079   1.00 15.84 ? 149 VAL A O   1 
ATOM   1200 C  CB  . VAL A 1 161 ? 19.442  3.179   7.686   1.00 15.81 ? 149 VAL A CB  1 
ATOM   1201 C  CG1 . VAL A 1 161 ? 20.029  4.065   8.777   1.00 15.07 ? 149 VAL A CG1 1 
ATOM   1202 C  CG2 . VAL A 1 161 ? 17.962  2.866   7.896   1.00 17.49 ? 149 VAL A CG2 1 
ATOM   1203 N  N   . THR A 1 162 ? 21.518  5.260   5.718   1.00 15.27 ? 150 THR A N   1 
ATOM   1204 C  CA  . THR A 1 162 ? 22.925  5.654   5.487   1.00 16.66 ? 150 THR A CA  1 
ATOM   1205 C  C   . THR A 1 162 ? 23.496  5.986   6.857   1.00 16.65 ? 150 THR A C   1 
ATOM   1206 O  O   . THR A 1 162 ? 23.405  7.157   7.287   1.00 18.28 ? 150 THR A O   1 
ATOM   1207 C  CB  . THR A 1 162 ? 23.082  6.764   4.448   1.00 20.48 ? 150 THR A CB  1 
ATOM   1208 O  OG1 . THR A 1 162 ? 22.339  6.372   3.293   1.00 19.63 ? 150 THR A OG1 1 
ATOM   1209 C  CG2 . THR A 1 162 ? 24.540  6.950   4.074   1.00 19.71 ? 150 THR A CG2 1 
ATOM   1210 N  N   . THR A 1 163 ? 23.996  4.977   7.550   1.00 16.49 ? 151 THR A N   1 
ATOM   1211 C  CA  . THR A 1 163 ? 24.344  5.130   8.993   1.00 18.29 ? 151 THR A CA  1 
ATOM   1212 C  C   . THR A 1 163 ? 25.410  6.207   9.164   1.00 18.87 ? 151 THR A C   1 
ATOM   1213 O  O   . THR A 1 163 ? 25.364  6.938   10.146  1.00 17.22 ? 151 THR A O   1 
ATOM   1214 C  CB  . THR A 1 163 ? 24.768  3.837   9.689   1.00 18.75 ? 151 THR A CB  1 
ATOM   1215 O  OG1 . THR A 1 163 ? 25.945  3.287   9.089   1.00 18.20 ? 151 THR A OG1 1 
ATOM   1216 C  CG2 . THR A 1 163 ? 23.645  2.821   9.684   1.00 17.61 ? 151 THR A CG2 1 
ATOM   1217 N  N   . GLN A 1 164 ? 26.320  6.347   8.211   1.00 18.93 ? 152 GLN A N   1 
ATOM   1218 C  CA  . GLN A 1 164 ? 27.373  7.372   8.346   1.00 20.54 ? 152 GLN A CA  1 
ATOM   1219 C  C   . GLN A 1 164 ? 26.774  8.774   8.452   1.00 19.74 ? 152 GLN A C   1 
ATOM   1220 O  O   . GLN A 1 164 ? 27.356  9.535   9.173   1.00 18.66 ? 152 GLN A O   1 
ATOM   1221 C  CB  . GLN A 1 164 ? 28.368  7.312   7.198   1.00 22.32 ? 152 GLN A CB  1 
ATOM   1222 C  CG  . GLN A 1 164 ? 29.604  8.175   7.444   1.00 23.49 ? 152 GLN A CG  1 
ATOM   1223 C  CD  . GLN A 1 164 ? 30.416  7.722   8.638   1.00 29.38 ? 152 GLN A CD  1 
ATOM   1224 O  OE1 . GLN A 1 164 ? 30.857  6.567   8.730   1.00 32.65 ? 152 GLN A OE1 1 
ATOM   1225 N  NE2 . GLN A 1 164 ? 30.622  8.630   9.580   1.00 32.01 ? 152 GLN A NE2 1 
ATOM   1226 N  N   . ASN A 1 165 ? 25.653  9.110   7.778   1.00 18.70 ? 153 ASN A N   1 
ATOM   1227 C  CA  . ASN A 1 165 ? 25.047  10.471  7.869   1.00 18.76 ? 153 ASN A CA  1 
ATOM   1228 C  C   . ASN A 1 165 ? 24.557  10.735  9.308   1.00 17.09 ? 153 ASN A C   1 
ATOM   1229 O  O   . ASN A 1 165 ? 24.540  11.886  9.762   1.00 18.76 ? 153 ASN A O   1 
ATOM   1230 C  CB  . ASN A 1 165 ? 23.899  10.636  6.868   1.00 16.96 ? 153 ASN A CB  1 
ATOM   1231 C  CG  . ASN A 1 165 ? 24.355  10.620  5.427   1.00 21.46 ? 153 ASN A CG  1 
ATOM   1232 O  OD1 . ASN A 1 165 ? 25.551  10.762  5.144   1.00 21.06 ? 153 ASN A OD1 1 
ATOM   1233 N  ND2 . ASN A 1 165 ? 23.414  10.430  4.505   1.00 20.62 ? 153 ASN A ND2 1 
ATOM   1234 N  N   . HIS A 1 166 ? 24.058  9.706   9.975   1.00 15.78 ? 154 HIS A N   1 
ATOM   1235 C  CA  . HIS A 1 166 ? 23.604  9.821   11.378  1.00 14.40 ? 154 HIS A CA  1 
ATOM   1236 C  C   . HIS A 1 166 ? 24.835  10.053  12.265  1.00 15.42 ? 154 HIS A C   1 
ATOM   1237 O  O   . HIS A 1 166 ? 24.813  10.955  13.115  1.00 18.24 ? 154 HIS A O   1 
ATOM   1238 C  CB  . HIS A 1 166 ? 22.775  8.603   11.812  1.00 14.80 ? 154 HIS A CB  1 
ATOM   1239 C  CG  . HIS A 1 166 ? 21.500  8.497   11.050  1.00 13.66 ? 154 HIS A CG  1 
ATOM   1240 N  ND1 . HIS A 1 166 ? 20.347  9.124   11.467  1.00 14.84 ? 154 HIS A ND1 1 
ATOM   1241 C  CD2 . HIS A 1 166 ? 21.216  7.868   9.893   1.00 14.69 ? 154 HIS A CD2 1 
ATOM   1242 C  CE1 . HIS A 1 166 ? 19.394  8.861   10.589  1.00 14.79 ? 154 HIS A CE1 1 
ATOM   1243 N  NE2 . HIS A 1 166 ? 19.893  8.081   9.623   1.00 14.61 ? 154 HIS A NE2 1 
ATOM   1244 N  N   . PHE A 1 167 ? 25.825  9.193   12.144  1.00 17.74 ? 155 PHE A N   1 
ATOM   1245 C  CA  . PHE A 1 167 ? 27.059  9.254   12.968  1.00 17.35 ? 155 PHE A CA  1 
ATOM   1246 C  C   . PHE A 1 167 ? 27.643  10.675  12.814  1.00 19.02 ? 155 PHE A C   1 
ATOM   1247 O  O   . PHE A 1 167 ? 28.052  11.261  13.833  1.00 18.69 ? 155 PHE A O   1 
ATOM   1248 C  CB  . PHE A 1 167 ? 28.014  8.125   12.623  1.00 18.53 ? 155 PHE A CB  1 
ATOM   1249 C  CG  . PHE A 1 167 ? 27.479  6.724   12.858  1.00 17.03 ? 155 PHE A CG  1 
ATOM   1250 C  CD1 . PHE A 1 167 ? 26.387  6.482   13.679  1.00 19.69 ? 155 PHE A CD1 1 
ATOM   1251 C  CD2 . PHE A 1 167 ? 28.022  5.671   12.188  1.00 18.19 ? 155 PHE A CD2 1 
ATOM   1252 C  CE1 . PHE A 1 167 ? 25.894  5.193   13.853  1.00 20.43 ? 155 PHE A CE1 1 
ATOM   1253 C  CE2 . PHE A 1 167 ? 27.533  4.375   12.347  1.00 18.92 ? 155 PHE A CE2 1 
ATOM   1254 C  CZ  . PHE A 1 167 ? 26.489  4.145   13.208  1.00 19.12 ? 155 PHE A CZ  1 
ATOM   1255 N  N   . ASP A 1 168 ? 27.713  11.176  11.578  1.00 19.87 ? 156 ASP A N   1 
ATOM   1256 C  CA  . ASP A 1 168 ? 28.260  12.527  11.251  1.00 22.75 ? 156 ASP A CA  1 
ATOM   1257 C  C   . ASP A 1 168 ? 27.422  13.598  11.945  1.00 23.76 ? 156 ASP A C   1 
ATOM   1258 O  O   . ASP A 1 168 ? 28.010  14.564  12.492  1.00 24.62 ? 156 ASP A O   1 
ATOM   1259 C  CB  . ASP A 1 168 ? 28.325  12.790  9.741   1.00 24.15 ? 156 ASP A CB  1 
ATOM   1260 C  CG  . ASP A 1 168 ? 29.396  12.007  9.001   1.00 28.24 ? 156 ASP A CG  1 
ATOM   1261 O  OD1 . ASP A 1 168 ? 30.281  11.433  9.685   1.00 29.03 ? 156 ASP A OD1 1 
ATOM   1262 O  OD2 . ASP A 1 168 ? 29.356  11.994  7.727   1.00 30.05 ? 156 ASP A OD2 1 
ATOM   1263 N  N   . ALA A 1 169 ? 26.093  13.502  11.903  1.00 20.91 ? 157 ALA A N   1 
ATOM   1264 C  CA  . ALA A 1 169 ? 25.214  14.524  12.497  1.00 20.46 ? 157 ALA A CA  1 
ATOM   1265 C  C   . ALA A 1 169 ? 25.401  14.523  14.015  1.00 17.89 ? 157 ALA A C   1 
ATOM   1266 O  O   . ALA A 1 169 ? 25.404  15.568  14.645  1.00 20.27 ? 157 ALA A O   1 
ATOM   1267 C  CB  . ALA A 1 169 ? 23.784  14.259  12.129  1.00 20.44 ? 157 ALA A CB  1 
ATOM   1268 N  N   . TRP A 1 170 ? 25.526  13.352  14.603  1.00 17.50 ? 158 TRP A N   1 
ATOM   1269 C  CA  . TRP A 1 170 ? 25.756  13.209  16.055  1.00 17.04 ? 158 TRP A CA  1 
ATOM   1270 C  C   . TRP A 1 170 ? 27.096  13.836  16.435  1.00 16.47 ? 158 TRP A C   1 
ATOM   1271 O  O   . TRP A 1 170 ? 27.087  14.639  17.367  1.00 20.17 ? 158 TRP A O   1 
ATOM   1272 C  CB  . TRP A 1 170 ? 25.736  11.735  16.451  1.00 17.80 ? 158 TRP A CB  1 
ATOM   1273 C  CG  . TRP A 1 170 ? 24.394  11.112  16.254  1.00 18.25 ? 158 TRP A CG  1 
ATOM   1274 C  CD1 . TRP A 1 170 ? 23.193  11.729  16.061  1.00 22.29 ? 158 TRP A CD1 1 
ATOM   1275 C  CD2 . TRP A 1 170 ? 24.132  9.701   16.244  1.00 19.22 ? 158 TRP A CD2 1 
ATOM   1276 N  NE1 . TRP A 1 170 ? 22.209  10.799  15.864  1.00 24.45 ? 158 TRP A NE1 1 
ATOM   1277 C  CE2 . TRP A 1 170 ? 22.749  9.546   16.015  1.00 21.54 ? 158 TRP A CE2 1 
ATOM   1278 C  CE3 . TRP A 1 170 ? 24.928  8.573   16.396  1.00 18.49 ? 158 TRP A CE3 1 
ATOM   1279 C  CZ2 . TRP A 1 170 ? 22.156  8.292   15.953  1.00 21.61 ? 158 TRP A CZ2 1 
ATOM   1280 C  CZ3 . TRP A 1 170 ? 24.355  7.335   16.280  1.00 18.80 ? 158 TRP A CZ3 1 
ATOM   1281 C  CH2 . TRP A 1 170 ? 22.983  7.203   16.051  1.00 18.48 ? 158 TRP A CH2 1 
ATOM   1282 N  N   . LYS A 1 171 ? 28.141  13.576  15.654  1.00 17.38 ? 159 LYS A N   1 
ATOM   1283 C  CA  . LYS A 1 171 ? 29.497  14.153  15.935  1.00 18.42 ? 159 LYS A CA  1 
ATOM   1284 C  C   . LYS A 1 171 ? 29.398  15.679  15.800  1.00 19.99 ? 159 LYS A C   1 
ATOM   1285 O  O   . LYS A 1 171 ? 29.970  16.403  16.647  1.00 20.79 ? 159 LYS A O   1 
ATOM   1286 C  CB  . LYS A 1 171 ? 30.534  13.637  14.940  1.00 20.01 ? 159 LYS A CB  1 
ATOM   1287 C  CG  . LYS A 1 171 ? 31.975  13.964  15.302  1.00 24.35 ? 159 LYS A CG  1 
ATOM   1288 C  CD  . LYS A 1 171 ? 32.927  13.759  14.131  1.00 29.82 ? 159 LYS A CD  1 
ATOM   1289 C  CE  . LYS A 1 171 ? 34.001  14.823  14.006  1.00 34.81 ? 159 LYS A CE  1 
ATOM   1290 N  NZ  . LYS A 1 171 ? 34.195  15.231  12.588  1.00 40.89 ? 159 LYS A NZ  1 
ATOM   1291 N  N   . ASN A 1 172 ? 28.658  16.155  14.798  1.00 22.69 ? 160 ASN A N   1 
ATOM   1292 C  CA  . ASN A 1 172 ? 28.444  17.609  14.525  1.00 25.20 ? 160 ASN A CA  1 
ATOM   1293 C  C   . ASN A 1 172 ? 27.719  18.287  15.692  1.00 26.04 ? 160 ASN A C   1 
ATOM   1294 O  O   . ASN A 1 172 ? 28.060  19.481  16.000  1.00 27.30 ? 160 ASN A O   1 
ATOM   1295 C  CB  . ASN A 1 172 ? 27.703  17.809  13.202  1.00 28.19 ? 160 ASN A CB  1 
ATOM   1296 C  CG  . ASN A 1 172 ? 28.564  17.470  12.007  1.00 33.52 ? 160 ASN A CG  1 
ATOM   1297 O  OD1 . ASN A 1 172 ? 29.779  17.339  12.133  1.00 41.75 ? 160 ASN A OD1 1 
ATOM   1298 N  ND2 . ASN A 1 172 ? 27.955  17.335  10.840  1.00 39.73 ? 160 ASN A ND2 1 
ATOM   1299 N  N   . ALA A 1 173 ? 26.809  17.588  16.373  1.00 22.29 ? 161 ALA A N   1 
ATOM   1300 C  CA  . ALA A 1 173 ? 26.042  18.104  17.527  1.00 24.15 ? 161 ALA A CA  1 
ATOM   1301 C  C   . ALA A 1 173 ? 26.873  18.000  18.812  1.00 25.55 ? 161 ALA A C   1 
ATOM   1302 O  O   . ALA A 1 173 ? 26.327  18.339  19.889  1.00 27.29 ? 161 ALA A O   1 
ATOM   1303 C  CB  . ALA A 1 173 ? 24.728  17.364  17.640  1.00 24.54 ? 161 ALA A CB  1 
ATOM   1304 N  N   . GLY A 1 174 ? 28.118  17.518  18.729  1.00 25.82 ? 162 GLY A N   1 
ATOM   1305 C  CA  . GLY A 1 174 ? 29.023  17.385  19.889  1.00 27.49 ? 162 GLY A CA  1 
ATOM   1306 C  C   . GLY A 1 174 ? 28.934  16.027  20.594  1.00 29.39 ? 162 GLY A C   1 
ATOM   1307 O  O   . GLY A 1 174 ? 29.491  15.912  21.724  1.00 32.21 ? 162 GLY A O   1 
ATOM   1308 N  N   . LEU A 1 175 ? 28.297  15.021  19.982  1.00 26.12 ? 163 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 175 ? 28.106  13.651  20.560  1.00 25.55 ? 163 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 175 ? 29.269  12.749  20.132  1.00 30.96 ? 163 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 175 ? 29.291  12.340  18.939  1.00 31.41 ? 163 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 175 ? 26.776  13.069  20.073  1.00 25.36 ? 163 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 175 ? 25.574  14.006  20.239  1.00 25.62 ? 163 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 175 ? 24.267  13.301  19.865  1.00 25.23 ? 163 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 175 ? 25.529  14.562  21.661  1.00 26.40 ? 163 LEU A CD2 1 
ATOM   1316 N  N   . GLU A 1 176 ? 30.132  12.391  21.086  1.00 30.33 ? 164 GLU A N   1 
ATOM   1317 C  CA  . GLU A 1 176 ? 31.329  11.551  20.817  1.00 30.83 ? 164 GLU A CA  1 
ATOM   1318 C  C   . GLU A 1 176 ? 30.938  10.067  20.705  1.00 25.81 ? 164 GLU A C   1 
ATOM   1319 O  O   . GLU A 1 176 ? 30.117  9.606   21.483  1.00 22.47 ? 164 GLU A O   1 
ATOM   1320 C  CB  . GLU A 1 176 ? 32.372  11.800  21.905  1.00 37.75 ? 164 GLU A CB  1 
ATOM   1321 C  CG  . GLU A 1 176 ? 32.939  13.208  21.843  1.00 43.58 ? 164 GLU A CG  1 
ATOM   1322 C  CD  . GLU A 1 176 ? 34.456  13.272  21.859  1.00 51.18 ? 164 GLU A CD  1 
ATOM   1323 O  OE1 . GLU A 1 176 ? 35.030  14.102  21.096  1.00 52.34 ? 164 GLU A OE1 1 
ATOM   1324 O  OE2 . GLU A 1 176 ? 35.060  12.483  22.630  1.00 51.15 ? 164 GLU A OE2 1 
ATOM   1325 N  N   . MET A 1 177 ? 31.494  9.392   19.716  1.00 23.21 ? 165 MET A N   1 
ATOM   1326 C  CA  . MET A 1 177 ? 31.341  7.931   19.479  1.00 23.75 ? 165 MET A CA  1 
ATOM   1327 C  C   . MET A 1 177 ? 32.691  7.264   19.746  1.00 22.33 ? 165 MET A C   1 
ATOM   1328 O  O   . MET A 1 177 ? 33.699  7.808   19.309  1.00 22.63 ? 165 MET A O   1 
ATOM   1329 C  CB  . MET A 1 177 ? 30.935  7.616   18.033  1.00 27.20 ? 165 MET A CB  1 
ATOM   1330 C  CG  . MET A 1 177 ? 29.816  8.494   17.497  1.00 33.36 ? 165 MET A CG  1 
ATOM   1331 S  SD  . MET A 1 177 ? 28.515  7.472   16.801  1.00 39.32 ? 165 MET A SD  1 
ATOM   1332 C  CE  . MET A 1 177 ? 27.854  7.007   18.397  1.00 33.35 ? 165 MET A CE  1 
ATOM   1333 N  N   . GLY A 1 178 ? 32.677  6.020   20.235  1.00 18.81 ? 166 GLY A N   1 
ATOM   1334 C  CA  . GLY A 1 178 ? 33.882  5.218   20.444  1.00 20.36 ? 166 GLY A CA  1 
ATOM   1335 C  C   . GLY A 1 178 ? 34.116  4.282   19.283  1.00 21.09 ? 166 GLY A C   1 
ATOM   1336 O  O   . GLY A 1 178 ? 33.601  4.576   18.159  1.00 24.34 ? 166 GLY A O   1 
ATOM   1337 N  N   . THR A 1 179 ? 34.788  3.184   19.591  1.00 18.58 ? 167 THR A N   1 
ATOM   1338 C  CA  . THR A 1 179 ? 35.082  2.009   18.737  1.00 20.51 ? 167 THR A CA  1 
ATOM   1339 C  C   . THR A 1 179 ? 33.783  1.245   18.549  1.00 17.93 ? 167 THR A C   1 
ATOM   1340 O  O   . THR A 1 179 ? 33.101  1.008   19.535  1.00 16.31 ? 167 THR A O   1 
ATOM   1341 C  CB  . THR A 1 179 ? 36.176  1.129   19.346  1.00 23.01 ? 167 THR A CB  1 
ATOM   1342 O  OG1 . THR A 1 179 ? 37.339  1.941   19.410  1.00 26.12 ? 167 THR A OG1 1 
ATOM   1343 C  CG2 . THR A 1 179 ? 36.469  -0.134  18.567  1.00 23.16 ? 167 THR A CG2 1 
ATOM   1344 N  N   . HIS A 1 180 ? 33.414  0.987   17.304  1.00 18.48 ? 168 HIS A N   1 
ATOM   1345 C  CA  . HIS A 1 180 ? 32.107  0.362   17.023  1.00 18.14 ? 168 HIS A CA  1 
ATOM   1346 C  C   . HIS A 1 180 ? 32.155  -1.084  17.505  1.00 16.79 ? 168 HIS A C   1 
ATOM   1347 O  O   . HIS A 1 180 ? 33.180  -1.756  17.304  1.00 19.58 ? 168 HIS A O   1 
ATOM   1348 C  CB  . HIS A 1 180 ? 31.775  0.453   15.537  1.00 19.36 ? 168 HIS A CB  1 
ATOM   1349 C  CG  . HIS A 1 180 ? 31.098  1.710   15.162  1.00 23.23 ? 168 HIS A CG  1 
ATOM   1350 N  ND1 . HIS A 1 180 ? 31.777  2.880   14.945  1.00 30.79 ? 168 HIS A ND1 1 
ATOM   1351 C  CD2 . HIS A 1 180 ? 29.792  2.002   15.039  1.00 26.49 ? 168 HIS A CD2 1 
ATOM   1352 C  CE1 . HIS A 1 180 ? 30.924  3.826   14.647  1.00 27.86 ? 168 HIS A CE1 1 
ATOM   1353 N  NE2 . HIS A 1 180 ? 29.694  3.324   14.729  1.00 32.03 ? 168 HIS A NE2 1 
ATOM   1354 N  N   . ASN A 1 181 ? 31.134  -1.477  18.249  1.00 14.60 ? 169 ASN A N   1 
ATOM   1355 C  CA  . ASN A 1 181 ? 30.761  -2.882  18.541  1.00 14.54 ? 169 ASN A CA  1 
ATOM   1356 C  C   . ASN A 1 181 ? 29.610  -3.233  17.589  1.00 15.05 ? 169 ASN A C   1 
ATOM   1357 O  O   . ASN A 1 181 ? 29.657  -2.835  16.414  1.00 15.33 ? 169 ASN A O   1 
ATOM   1358 C  CB  . ASN A 1 181 ? 30.394  -3.030  20.023  1.00 16.90 ? 169 ASN A CB  1 
ATOM   1359 C  CG  . ASN A 1 181 ? 30.399  -4.484  20.448  1.00 18.27 ? 169 ASN A CG  1 
ATOM   1360 O  OD1 . ASN A 1 181 ? 29.356  -5.114  20.525  1.00 20.38 ? 169 ASN A OD1 1 
ATOM   1361 N  ND2 . ASN A 1 181 ? 31.561  -4.995  20.841  1.00 21.08 ? 169 ASN A ND2 1 
ATOM   1362 N  N   . TYR A 1 182 ? 28.584  -3.925  18.041  1.00 16.18 ? 170 TYR A N   1 
ATOM   1363 C  CA  . TYR A 1 182 ? 27.621  -4.492  17.047  1.00 15.06 ? 170 TYR A CA  1 
ATOM   1364 C  C   . TYR A 1 182 ? 26.727  -3.397  16.521  1.00 14.34 ? 170 TYR A C   1 
ATOM   1365 O  O   . TYR A 1 182 ? 26.546  -2.358  17.182  1.00 15.73 ? 170 TYR A O   1 
ATOM   1366 C  CB  . TYR A 1 182 ? 26.837  -5.697  17.540  1.00 14.50 ? 170 TYR A CB  1 
ATOM   1367 C  CG  . TYR A 1 182 ? 25.841  -5.465  18.637  1.00 12.53 ? 170 TYR A CG  1 
ATOM   1368 C  CD1 . TYR A 1 182 ? 24.602  -4.944  18.364  1.00 12.41 ? 170 TYR A CD1 1 
ATOM   1369 C  CD2 . TYR A 1 182 ? 26.116  -5.856  19.923  1.00 13.01 ? 170 TYR A CD2 1 
ATOM   1370 C  CE1 . TYR A 1 182 ? 23.629  -4.846  19.353  1.00 12.62 ? 170 TYR A CE1 1 
ATOM   1371 C  CE2 . TYR A 1 182 ? 25.176  -5.744  20.929  1.00 13.02 ? 170 TYR A CE2 1 
ATOM   1372 C  CZ  . TYR A 1 182 ? 23.920  -5.265  20.630  1.00 12.52 ? 170 TYR A CZ  1 
ATOM   1373 O  OH  . TYR A 1 182 ? 23.018  -5.097  21.629  1.00 14.80 ? 170 TYR A OH  1 
ATOM   1374 N  N   . MET A 1 183 ? 26.146  -3.662  15.349  1.00 14.16 ? 171 MET A N   1 
ATOM   1375 C  CA  . MET A 1 183 ? 25.142  -2.783  14.732  1.00 15.56 ? 171 MET A CA  1 
ATOM   1376 C  C   . MET A 1 183 ? 24.144  -3.718  14.066  1.00 15.11 ? 171 MET A C   1 
ATOM   1377 O  O   . MET A 1 183 ? 24.553  -4.521  13.196  1.00 14.18 ? 171 MET A O   1 
ATOM   1378 C  CB  . MET A 1 183 ? 25.753  -1.766  13.758  1.00 16.36 ? 171 MET A CB  1 
ATOM   1379 C  CG  . MET A 1 183 ? 24.725  -0.948  13.019  1.00 17.38 ? 171 MET A CG  1 
ATOM   1380 S  SD  . MET A 1 183 ? 25.410  0.415   12.032  1.00 17.48 ? 171 MET A SD  1 
ATOM   1381 C  CE  . MET A 1 183 ? 26.038  -0.448  10.612  1.00 19.00 ? 171 MET A CE  1 
ATOM   1382 N  N   . ILE A 1 184 ? 22.865  -3.646  14.452  1.00 13.70 ? 172 ILE A N   1 
ATOM   1383 C  CA  . ILE A 1 184 ? 21.824  -4.566  13.935  1.00 12.82 ? 172 ILE A CA  1 
ATOM   1384 C  C   . ILE A 1 184 ? 20.561  -3.793  13.561  1.00 12.09 ? 172 ILE A C   1 
ATOM   1385 O  O   . ILE A 1 184 ? 20.437  -2.570  13.914  1.00 12.05 ? 172 ILE A O   1 
ATOM   1386 C  CB  . ILE A 1 184 ? 21.492  -5.651  14.989  1.00 13.68 ? 172 ILE A CB  1 
ATOM   1387 C  CG1 . ILE A 1 184 ? 21.009  -5.024  16.288  1.00 12.99 ? 172 ILE A CG1 1 
ATOM   1388 C  CG2 . ILE A 1 184 ? 22.653  -6.606  15.217  1.00 14.39 ? 172 ILE A CG2 1 
ATOM   1389 C  CD1 . ILE A 1 184 ? 20.498  -5.996  17.303  1.00 13.46 ? 172 ILE A CD1 1 
ATOM   1390 N  N   . VAL A 1 185 ? 19.713  -4.434  12.754  1.00 12.70 ? 173 VAL A N   1 
ATOM   1391 C  CA  . VAL A 1 185 ? 18.354  -3.911  12.489  1.00 13.26 ? 173 VAL A CA  1 
ATOM   1392 C  C   . VAL A 1 185 ? 17.478  -4.573  13.536  1.00 12.42 ? 173 VAL A C   1 
ATOM   1393 O  O   . VAL A 1 185 ? 17.299  -5.815  13.456  1.00 15.38 ? 173 VAL A O   1 
ATOM   1394 C  CB  . VAL A 1 185 ? 17.820  -4.133  11.074  1.00 14.16 ? 173 VAL A CB  1 
ATOM   1395 C  CG1 . VAL A 1 185 ? 16.434  -3.521  10.981  1.00 16.05 ? 173 VAL A CG1 1 
ATOM   1396 C  CG2 . VAL A 1 185 ? 18.761  -3.562  10.018  1.00 16.21 ? 173 VAL A CG2 1 
ATOM   1397 N  N   . ALA A 1 186 ? 17.125  -3.799  14.540  1.00 12.99 ? 174 ALA A N   1 
ATOM   1398 C  CA  . ALA A 1 186 ? 16.538  -4.293  15.786  1.00 13.33 ? 174 ALA A CA  1 
ATOM   1399 C  C   . ALA A 1 186 ? 15.048  -4.011  15.844  1.00 12.68 ? 174 ALA A C   1 
ATOM   1400 O  O   . ALA A 1 186 ? 14.617  -2.859  15.611  1.00 15.26 ? 174 ALA A O   1 
ATOM   1401 C  CB  . ALA A 1 186 ? 17.222  -3.702  16.957  1.00 14.00 ? 174 ALA A CB  1 
ATOM   1402 N  N   . THR A 1 187 ? 14.371  -5.015  16.345  1.00 12.24 ? 175 THR A N   1 
ATOM   1403 C  CA  . THR A 1 187 ? 13.020  -4.907  16.942  1.00 12.69 ? 175 THR A CA  1 
ATOM   1404 C  C   . THR A 1 187 ? 13.138  -4.858  18.456  1.00 12.75 ? 175 THR A C   1 
ATOM   1405 O  O   . THR A 1 187 ? 13.719  -5.741  19.034  1.00 14.42 ? 175 THR A O   1 
ATOM   1406 C  CB  . THR A 1 187 ? 12.124  -6.034  16.465  1.00 11.82 ? 175 THR A CB  1 
ATOM   1407 O  OG1 . THR A 1 187 ? 12.067  -6.010  15.038  1.00 13.66 ? 175 THR A OG1 1 
ATOM   1408 C  CG2 . THR A 1 187 ? 10.710  -5.921  16.948  1.00 12.72 ? 175 THR A CG2 1 
ATOM   1409 N  N   . ALA A 1 188 ? 12.559  -3.823  19.078  1.00 12.91 ? 176 ALA A N   1 
ATOM   1410 C  CA  . ALA A 1 188 ? 12.597  -3.610  20.544  1.00 11.66 ? 176 ALA A CA  1 
ATOM   1411 C  C   . ALA A 1 188 ? 11.160  -3.525  21.019  1.00 12.42 ? 176 ALA A C   1 
ATOM   1412 O  O   . ALA A 1 188 ? 10.254  -3.116  20.236  1.00 14.61 ? 176 ALA A O   1 
ATOM   1413 C  CB  . ALA A 1 188 ? 13.338  -2.333  20.922  1.00 12.71 ? 176 ALA A CB  1 
ATOM   1414 N  N   . GLY A 1 189 ? 10.934  -3.883  22.264  1.00 12.83 ? 177 GLY A N   1 
ATOM   1415 C  CA  . GLY A 1 189 ? 9.576   -3.815  22.811  1.00 13.26 ? 177 GLY A CA  1 
ATOM   1416 C  C   . GLY A 1 189 ? 9.644   -3.709  24.298  1.00 14.55 ? 177 GLY A C   1 
ATOM   1417 O  O   . GLY A 1 189 ? 10.686  -4.088  24.888  1.00 16.75 ? 177 GLY A O   1 
ATOM   1418 N  N   . TYR A 1 190 ? 8.613   -3.132  24.899  1.00 16.28 ? 178 TYR A N   1 
ATOM   1419 C  CA  . TYR A 1 190 ? 8.498   -3.065  26.368  1.00 16.99 ? 178 TYR A CA  1 
ATOM   1420 C  C   . TYR A 1 190 ? 7.019   -3.134  26.748  1.00 16.45 ? 178 TYR A C   1 
ATOM   1421 O  O   . TYR A 1 190 ? 6.270   -2.282  26.249  1.00 15.86 ? 178 TYR A O   1 
ATOM   1422 C  CB  . TYR A 1 190 ? 9.102   -1.772  26.911  1.00 18.18 ? 178 TYR A CB  1 
ATOM   1423 C  CG  . TYR A 1 190 ? 9.016   -1.707  28.419  1.00 22.12 ? 178 TYR A CG  1 
ATOM   1424 C  CD1 . TYR A 1 190 ? 9.724   -2.577  29.242  1.00 25.53 ? 178 TYR A CD1 1 
ATOM   1425 C  CD2 . TYR A 1 190 ? 8.147   -0.829  29.027  1.00 24.73 ? 178 TYR A CD2 1 
ATOM   1426 C  CE1 . TYR A 1 190 ? 9.614   -2.526  30.624  1.00 27.89 ? 178 TYR A CE1 1 
ATOM   1427 C  CE2 . TYR A 1 190 ? 8.068   -0.722  30.400  1.00 27.39 ? 178 TYR A CE2 1 
ATOM   1428 C  CZ  . TYR A 1 190 ? 8.818   -1.555  31.212  1.00 28.03 ? 178 TYR A CZ  1 
ATOM   1429 O  OH  . TYR A 1 190 ? 8.696   -1.476  32.574  1.00 29.45 ? 178 TYR A OH  1 
ATOM   1430 N  N   . GLN A 1 191 ? 6.644   -4.068  27.620  1.00 16.45 ? 179 GLN A N   1 
ATOM   1431 C  CA  . GLN A 1 191 ? 5.259   -4.219  28.154  1.00 16.71 ? 179 GLN A CA  1 
ATOM   1432 C  C   . GLN A 1 191 ? 4.271   -4.145  26.990  1.00 17.36 ? 179 GLN A C   1 
ATOM   1433 O  O   . GLN A 1 191 ? 3.362   -3.318  26.985  1.00 16.52 ? 179 GLN A O   1 
ATOM   1434 C  CB  . GLN A 1 191 ? 5.026   -3.208  29.269  1.00 18.53 ? 179 GLN A CB  1 
ATOM   1435 C  CG  . GLN A 1 191 ? 5.879   -3.582  30.450  1.00 19.58 ? 179 GLN A CG  1 
ATOM   1436 C  CD  . GLN A 1 191 ? 5.476   -2.937  31.749  1.00 23.97 ? 179 GLN A CD  1 
ATOM   1437 O  OE1 . GLN A 1 191 ? 4.954   -1.833  31.764  1.00 27.67 ? 179 GLN A OE1 1 
ATOM   1438 N  NE2 . GLN A 1 191 ? 5.816   -3.587  32.844  1.00 26.42 ? 179 GLN A NE2 1 
ATOM   1439 N  N   . SER A 1 192 ? 4.451   -5.022  26.017  1.00 17.14 ? 180 SER A N   1 
ATOM   1440 C  CA  . SER A 1 192 ? 3.646   -4.979  24.768  1.00 16.14 ? 180 SER A CA  1 
ATOM   1441 C  C   . SER A 1 192 ? 3.565   -6.385  24.206  1.00 15.91 ? 180 SER A C   1 
ATOM   1442 O  O   . SER A 1 192 ? 4.159   -7.300  24.800  1.00 14.57 ? 180 SER A O   1 
ATOM   1443 C  CB  . SER A 1 192 ? 4.157   -3.957  23.776  1.00 15.53 ? 180 SER A CB  1 
ATOM   1444 O  OG  . SER A 1 192 ? 5.468   -4.263  23.306  1.00 15.33 ? 180 SER A OG  1 
ATOM   1445 N  N   . SER A 1 193 ? 2.808   -6.563  23.119  1.00 16.21 ? 181 SER A N   1 
ATOM   1446 C  CA  . SER A 1 193 ? 2.781   -7.833  22.355  1.00 16.20 ? 181 SER A CA  1 
ATOM   1447 C  C   . SER A 1 193 ? 2.997   -7.432  20.898  1.00 15.37 ? 181 SER A C   1 
ATOM   1448 O  O   . SER A 1 193 ? 2.945   -6.203  20.578  1.00 15.58 ? 181 SER A O   1 
ATOM   1449 C  CB  . SER A 1 193 ? 1.507   -8.586  22.530  1.00 15.95 ? 181 SER A CB  1 
ATOM   1450 O  OG  . SER A 1 193 ? 1.223   -8.836  23.909  1.00 19.56 ? 181 SER A OG  1 
ATOM   1451 N  N   . GLY A 1 194 ? 3.431   -8.372  20.112  1.00 14.98 ? 182 GLY A N   1 
ATOM   1452 C  CA  . GLY A 1 194 ? 3.467   -8.205  18.662  1.00 14.07 ? 182 GLY A CA  1 
ATOM   1453 C  C   . GLY A 1 194 ? 4.254   -9.277  17.952  1.00 16.38 ? 182 GLY A C   1 
ATOM   1454 O  O   . GLY A 1 194 ? 4.585   -10.332 18.538  1.00 16.24 ? 182 GLY A O   1 
ATOM   1455 N  N   . SER A 1 195 ? 4.578   -8.971  16.709  1.00 15.81 ? 183 SER A N   1 
ATOM   1456 C  CA  . SER A 1 195 ? 5.408   -9.873  15.885  1.00 15.83 ? 183 SER A CA  1 
ATOM   1457 C  C   . SER A 1 195 ? 6.130   -9.034  14.873  1.00 15.02 ? 183 SER A C   1 
ATOM   1458 O  O   . SER A 1 195 ? 5.649   -7.927  14.570  1.00 14.19 ? 183 SER A O   1 
ATOM   1459 C  CB  . SER A 1 195 ? 4.631   -10.981 15.231  1.00 18.35 ? 183 SER A CB  1 
ATOM   1460 O  OG  . SER A 1 195 ? 3.736   -10.472 14.290  1.00 20.86 ? 183 SER A OG  1 
ATOM   1461 N  N   . ALA A 1 196 ? 7.271   -9.507  14.408  1.00 14.35 ? 184 ALA A N   1 
ATOM   1462 C  CA  . ALA A 1 196 ? 8.004   -8.808  13.342  1.00 14.85 ? 184 ALA A CA  1 
ATOM   1463 C  C   . ALA A 1 196 ? 8.792   -9.870  12.599  1.00 15.14 ? 184 ALA A C   1 
ATOM   1464 O  O   . ALA A 1 196 ? 9.190   -10.912 13.193  1.00 16.65 ? 184 ALA A O   1 
ATOM   1465 C  CB  . ALA A 1 196 ? 8.922   -7.711  13.861  1.00 14.01 ? 184 ALA A CB  1 
ATOM   1466 N  N   . SER A 1 197 ? 9.029   -9.590  11.316  1.00 16.04 ? 185 SER A N   1 
ATOM   1467 C  CA  . SER A 1 197 ? 9.790   -10.484 10.413  1.00 16.76 ? 185 SER A CA  1 
ATOM   1468 C  C   . SER A 1 197 ? 10.604  -9.563  9.540   1.00 16.43 ? 185 SER A C   1 
ATOM   1469 O  O   . SER A 1 197 ? 10.002  -8.873  8.685   1.00 16.35 ? 185 SER A O   1 
ATOM   1470 C  CB  . SER A 1 197 ? 8.890   -11.379 9.581   1.00 20.51 ? 185 SER A CB  1 
ATOM   1471 O  OG  . SER A 1 197 ? 8.318   -12.433 10.357  1.00 21.93 ? 185 SER A OG  1 
ATOM   1472 N  N   . ILE A 1 198 ? 11.900  -9.481  9.809   1.00 15.32 ? 186 ILE A N   1 
ATOM   1473 C  CA  . ILE A 1 198 ? 12.755  -8.435  9.205   1.00 16.45 ? 186 ILE A CA  1 
ATOM   1474 C  C   . ILE A 1 198 ? 13.907  -9.100  8.479   1.00 17.43 ? 186 ILE A C   1 
ATOM   1475 O  O   . ILE A 1 198 ? 14.456  -10.053 9.032   1.00 18.06 ? 186 ILE A O   1 
ATOM   1476 C  CB  . ILE A 1 198 ? 13.259  -7.456  10.280  1.00 16.82 ? 186 ILE A CB  1 
ATOM   1477 C  CG1 . ILE A 1 198 ? 12.114  -6.684  10.934  1.00 18.51 ? 186 ILE A CG1 1 
ATOM   1478 C  CG2 . ILE A 1 198 ? 14.334  -6.504  9.716   1.00 17.70 ? 186 ILE A CG2 1 
ATOM   1479 C  CD1 . ILE A 1 198 ? 11.437  -5.699  10.025  1.00 18.88 ? 186 ILE A CD1 1 
ATOM   1480 N  N   . THR A 1 199 ? 14.223  -8.609  7.285   1.00 14.92 ? 187 THR A N   1 
ATOM   1481 C  CA  . THR A 1 199 ? 15.349  -9.124  6.487   1.00 17.46 ? 187 THR A CA  1 
ATOM   1482 C  C   . THR A 1 199 ? 16.363  -8.025  6.264   1.00 17.30 ? 187 THR A C   1 
ATOM   1483 O  O   . THR A 1 199 ? 16.015  -6.954  5.738   1.00 16.57 ? 187 THR A O   1 
ATOM   1484 C  CB  . THR A 1 199 ? 14.922  -9.797  5.175   1.00 19.56 ? 187 THR A CB  1 
ATOM   1485 O  OG1 . THR A 1 199 ? 14.029  -10.860 5.469   1.00 20.78 ? 187 THR A OG1 1 
ATOM   1486 C  CG2 . THR A 1 199 ? 16.112  -10.346 4.403   1.00 19.60 ? 187 THR A CG2 1 
ATOM   1487 N  N   . VAL A 1 200 ? 17.588  -8.246  6.744   1.00 16.86 ? 188 VAL A N   1 
ATOM   1488 C  CA  . VAL A 1 200 ? 18.700  -7.305  6.502   1.00 18.99 ? 188 VAL A CA  1 
ATOM   1489 C  C   . VAL A 1 200 ? 19.318  -7.738  5.172   1.00 22.22 ? 188 VAL A C   1 
ATOM   1490 O  O   . VAL A 1 200 ? 19.617  -8.921  5.085   1.00 21.14 ? 188 VAL A O   1 
ATOM   1491 C  CB  . VAL A 1 200 ? 19.731  -7.355  7.643   1.00 19.25 ? 188 VAL A CB  1 
ATOM   1492 C  CG1 . VAL A 1 200 ? 20.793  -6.294  7.430   1.00 21.40 ? 188 VAL A CG1 1 
ATOM   1493 C  CG2 . VAL A 1 200 ? 19.040  -7.165  8.972   1.00 19.89 ? 188 VAL A CG2 1 
ATOM   1494 N  N   . GLN A 1 201 ? 19.379  -6.880  4.155   1.00 27.15 ? 189 GLN A N   1 
ATOM   1495 C  CA  . GLN A 1 201 ? 19.964  -7.303  2.838   1.00 30.29 ? 189 GLN A CA  1 
ATOM   1496 C  C   . GLN A 1 201 ? 21.317  -6.606  2.668   1.00 34.26 ? 189 GLN A C   1 
ATOM   1497 O  O   . GLN A 1 201 ? 22.102  -6.562  3.638   1.00 43.71 ? 189 GLN A O   1 
ATOM   1498 C  CB  . GLN A 1 201 ? 19.054  -7.017  1.643   1.00 37.05 ? 189 GLN A CB  1 
ATOM   1499 C  CG  . GLN A 1 201 ? 17.735  -7.780  1.656   1.00 41.51 ? 189 GLN A CG  1 
ATOM   1500 C  CD  . GLN A 1 201 ? 16.573  -6.948  2.141   1.00 44.14 ? 189 GLN A CD  1 
ATOM   1501 O  OE1 . GLN A 1 201 ? 16.671  -5.725  2.316   1.00 42.44 ? 189 GLN A OE1 1 
ATOM   1502 N  NE2 . GLN A 1 201 ? 15.441  -7.612  2.313   1.00 44.35 ? 189 GLN A NE2 1 
ATOM   1503 N  N   . GLU B 1 13  ? -5.264  21.172  34.288  1.00 38.68 ? 1   GLU B N   1 
ATOM   1504 C  CA  . GLU B 1 13  ? -5.236  22.032  35.507  1.00 32.58 ? 1   GLU B CA  1 
ATOM   1505 C  C   . GLU B 1 13  ? -4.296  21.471  36.590  1.00 28.98 ? 1   GLU B C   1 
ATOM   1506 O  O   . GLU B 1 13  ? -3.719  22.290  37.262  1.00 23.42 ? 1   GLU B O   1 
ATOM   1507 C  CB  . GLU B 1 13  ? -6.645  22.305  36.015  1.00 36.89 ? 1   GLU B CB  1 
ATOM   1508 C  CG  . GLU B 1 13  ? -6.703  23.234  37.196  1.00 38.90 ? 1   GLU B CG  1 
ATOM   1509 C  CD  . GLU B 1 13  ? -7.713  24.350  37.011  1.00 39.78 ? 1   GLU B CD  1 
ATOM   1510 O  OE1 . GLU B 1 13  ? -7.368  25.361  36.347  1.00 36.96 ? 1   GLU B OE1 1 
ATOM   1511 O  OE2 . GLU B 1 13  ? -8.858  24.178  37.496  1.00 41.31 ? 1   GLU B OE2 1 
ATOM   1512 N  N   . ILE B 1 14  ? -4.111  20.158  36.742  1.00 22.50 ? 2   ILE B N   1 
ATOM   1513 C  CA  . ILE B 1 14  ? -3.163  19.534  37.731  1.00 26.41 ? 2   ILE B CA  1 
ATOM   1514 C  C   . ILE B 1 14  ? -2.113  18.719  36.943  1.00 26.74 ? 2   ILE B C   1 
ATOM   1515 O  O   . ILE B 1 14  ? -2.534  17.812  36.220  1.00 24.40 ? 2   ILE B O   1 
ATOM   1516 C  CB  . ILE B 1 14  ? -3.987  18.671  38.724  1.00 27.53 ? 2   ILE B CB  1 
ATOM   1517 C  CG1 . ILE B 1 14  ? -5.124  19.485  39.344  1.00 30.06 ? 2   ILE B CG1 1 
ATOM   1518 C  CG2 . ILE B 1 14  ? -3.153  18.042  39.825  1.00 30.11 ? 2   ILE B CG2 1 
ATOM   1519 C  CD1 . ILE B 1 14  ? -5.853  18.774  40.465  1.00 34.02 ? 2   ILE B CD1 1 
ATOM   1520 N  N   . THR B 1 15  ? -0.804  18.996  37.066  1.00 24.79 ? 3   THR B N   1 
ATOM   1521 C  CA  . THR B 1 15  ? 0.267   18.260  36.317  1.00 24.61 ? 3   THR B CA  1 
ATOM   1522 C  C   . THR B 1 15  ? 1.281   17.562  37.246  1.00 23.73 ? 3   THR B C   1 
ATOM   1523 O  O   . THR B 1 15  ? 2.133   16.790  36.727  1.00 21.79 ? 3   THR B O   1 
ATOM   1524 C  CB  . THR B 1 15  ? 0.970   19.175  35.321  1.00 30.23 ? 3   THR B CB  1 
ATOM   1525 O  OG1 . THR B 1 15  ? 1.624   20.191  36.093  1.00 30.67 ? 3   THR B OG1 1 
ATOM   1526 C  CG2 . THR B 1 15  ? -0.012  19.720  34.305  1.00 31.03 ? 3   THR B CG2 1 
ATOM   1527 N  N   . SER B 1 16  ? 1.147   17.718  38.564  1.00 21.15 ? 4   SER B N   1 
ATOM   1528 C  CA  . SER B 1 16  ? 1.956   17.022  39.586  1.00 21.31 ? 4   SER B CA  1 
ATOM   1529 C  C   . SER B 1 16  ? 1.008   16.422  40.610  1.00 19.36 ? 4   SER B C   1 
ATOM   1530 O  O   . SER B 1 16  ? -0.137  16.919  40.714  1.00 20.58 ? 4   SER B O   1 
ATOM   1531 C  CB  . SER B 1 16  ? 2.989   17.924  40.241  1.00 25.59 ? 4   SER B CB  1 
ATOM   1532 O  OG  . SER B 1 16  ? 4.000   18.298  39.295  1.00 29.66 ? 4   SER B OG  1 
ATOM   1533 N  N   . SER B 1 17  ? 1.470   15.380  41.289  1.00 19.08 ? 5   SER B N   1 
ATOM   1534 C  CA  . SER B 1 17  ? 0.689   14.569  42.244  1.00 17.59 ? 5   SER B CA  1 
ATOM   1535 C  C   . SER B 1 17  ? -0.007  15.439  43.292  1.00 20.37 ? 5   SER B C   1 
ATOM   1536 O  O   . SER B 1 17  ? 0.637   16.327  43.891  1.00 18.86 ? 5   SER B O   1 
ATOM   1537 C  CB  . SER B 1 17  ? 1.537   13.540  42.876  1.00 19.32 ? 5   SER B CB  1 
ATOM   1538 O  OG  . SER B 1 17  ? 2.135   12.766  41.863  1.00 19.35 ? 5   SER B OG  1 
ATOM   1539 N  N   . GLU B 1 18  ? -1.269  15.140  43.538  1.00 19.37 ? 6   GLU B N   1 
ATOM   1540 C  CA  . GLU B 1 18  ? -2.032  15.817  44.596  1.00 20.41 ? 6   GLU B CA  1 
ATOM   1541 C  C   . GLU B 1 18  ? -3.272  14.983  44.890  1.00 18.25 ? 6   GLU B C   1 
ATOM   1542 O  O   . GLU B 1 18  ? -3.755  14.277  43.987  1.00 17.59 ? 6   GLU B O   1 
ATOM   1543 C  CB  . GLU B 1 18  ? -2.226  17.286  44.182  1.00 24.96 ? 6   GLU B CB  1 
ATOM   1544 C  CG  . GLU B 1 18  ? -3.520  17.696  43.508  1.00 27.88 ? 6   GLU B CG  1 
ATOM   1545 C  CD  . GLU B 1 18  ? -3.772  19.208  43.431  1.00 31.98 ? 6   GLU B CD  1 
ATOM   1546 O  OE1 . GLU B 1 18  ? -4.937  19.620  43.610  1.00 27.96 ? 6   GLU B OE1 1 
ATOM   1547 O  OE2 . GLU B 1 18  ? -2.823  19.987  43.113  1.00 27.24 ? 6   GLU B OE2 1 
ATOM   1548 N  N   . THR B 1 19  ? -3.817  15.177  46.084  1.00 16.80 ? 7   THR B N   1 
ATOM   1549 C  CA  . THR B 1 19  ? -5.062  14.570  46.529  1.00 15.98 ? 7   THR B CA  1 
ATOM   1550 C  C   . THR B 1 19  ? -5.895  15.658  47.160  1.00 17.32 ? 7   THR B C   1 
ATOM   1551 O  O   . THR B 1 19  ? -5.351  16.719  47.545  1.00 17.97 ? 7   THR B O   1 
ATOM   1552 C  CB  . THR B 1 19  ? -4.848  13.419  47.528  1.00 18.41 ? 7   THR B CB  1 
ATOM   1553 O  OG1 . THR B 1 19  ? -4.223  13.876  48.736  1.00 19.56 ? 7   THR B OG1 1 
ATOM   1554 C  CG2 . THR B 1 19  ? -4.010  12.319  46.907  1.00 19.02 ? 7   THR B CG2 1 
ATOM   1555 N  N   . GLY B 1 20  ? -7.185  15.452  47.132  1.00 16.64 ? 8   GLY B N   1 
ATOM   1556 C  CA  . GLY B 1 20  ? -8.078  16.403  47.811  1.00 17.09 ? 8   GLY B CA  1 
ATOM   1557 C  C   . GLY B 1 20  ? -9.493  15.953  47.661  1.00 16.25 ? 8   GLY B C   1 
ATOM   1558 O  O   . GLY B 1 20  ? -9.718  14.763  47.423  1.00 15.25 ? 8   GLY B O   1 
ATOM   1559 N  N   . THR B 1 21  ? -10.400 16.822  48.026  1.00 15.70 ? 9   THR B N   1 
ATOM   1560 C  CA  . THR B 1 21  ? -11.851 16.702  47.789  1.00 15.75 ? 9   THR B CA  1 
ATOM   1561 C  C   . THR B 1 21  ? -12.211 17.650  46.658  1.00 15.49 ? 9   THR B C   1 
ATOM   1562 O  O   . THR B 1 21  ? -11.733 18.803  46.642  1.00 15.05 ? 9   THR B O   1 
ATOM   1563 C  CB  . THR B 1 21  ? -12.616 17.119  49.045  1.00 17.02 ? 9   THR B CB  1 
ATOM   1564 O  OG1 . THR B 1 21  ? -12.034 16.437  50.156  1.00 16.99 ? 9   THR B OG1 1 
ATOM   1565 C  CG2 . THR B 1 21  ? -14.093 16.860  48.945  1.00 17.76 ? 9   THR B CG2 1 
ATOM   1566 N  N   . ASN B 1 22  ? -13.149 17.239  45.825  1.00 15.36 ? 10  ASN B N   1 
ATOM   1567 C  CA  . ASN B 1 22  ? -13.644 18.056  44.712  1.00 14.65 ? 10  ASN B CA  1 
ATOM   1568 C  C   . ASN B 1 22  ? -15.116 17.707  44.525  1.00 14.71 ? 10  ASN B C   1 
ATOM   1569 O  O   . ASN B 1 22  ? -15.435 16.546  44.234  1.00 15.87 ? 10  ASN B O   1 
ATOM   1570 C  CB  . ASN B 1 22  ? -12.858 17.867  43.404  1.00 15.22 ? 10  ASN B CB  1 
ATOM   1571 C  CG  . ASN B 1 22  ? -13.473 18.719  42.319  1.00 15.76 ? 10  ASN B CG  1 
ATOM   1572 O  OD1 . ASN B 1 22  ? -14.229 18.220  41.488  1.00 16.50 ? 10  ASN B OD1 1 
ATOM   1573 N  ND2 . ASN B 1 22  ? -13.235 20.047  42.355  1.00 15.67 ? 10  ASN B ND2 1 
ATOM   1574 N  N   . ASN B 1 23  ? -15.997 18.610  44.908  1.00 15.57 ? 11  ASN B N   1 
ATOM   1575 C  CA  . ASN B 1 23  ? -17.448 18.427  44.643  1.00 15.92 ? 11  ASN B CA  1 
ATOM   1576 C  C   . ASN B 1 23  ? -17.954 17.142  45.315  1.00 17.65 ? 11  ASN B C   1 
ATOM   1577 O  O   . ASN B 1 23  ? -18.807 16.454  44.709  1.00 18.47 ? 11  ASN B O   1 
ATOM   1578 C  CB  . ASN B 1 23  ? -17.664 18.456  43.132  1.00 16.05 ? 11  ASN B CB  1 
ATOM   1579 C  CG  . ASN B 1 23  ? -17.358 19.809  42.535  1.00 18.32 ? 11  ASN B CG  1 
ATOM   1580 O  OD1 . ASN B 1 23  ? -17.747 20.807  43.111  1.00 22.40 ? 11  ASN B OD1 1 
ATOM   1581 N  ND2 . ASN B 1 23  ? -16.683 19.856  41.387  1.00 18.76 ? 11  ASN B ND2 1 
ATOM   1582 N  N   . GLY B 1 24  ? -17.508 16.887  46.555  1.00 17.12 ? 12  GLY B N   1 
ATOM   1583 C  CA  . GLY B 1 24  ? -17.972 15.805  47.430  1.00 19.19 ? 12  GLY B CA  1 
ATOM   1584 C  C   . GLY B 1 24  ? -17.367 14.461  47.080  1.00 17.36 ? 12  GLY B C   1 
ATOM   1585 O  O   . GLY B 1 24  ? -17.805 13.461  47.610  1.00 22.34 ? 12  GLY B O   1 
ATOM   1586 N  N   . TYR B 1 25  ? -16.373 14.430  46.192  1.00 16.11 ? 13  TYR B N   1 
ATOM   1587 C  CA  . TYR B 1 25  ? -15.622 13.195  45.870  1.00 14.38 ? 13  TYR B CA  1 
ATOM   1588 C  C   . TYR B 1 25  ? -14.189 13.364  46.354  1.00 14.33 ? 13  TYR B C   1 
ATOM   1589 O  O   . TYR B 1 25  ? -13.625 14.442  46.160  1.00 15.35 ? 13  TYR B O   1 
ATOM   1590 C  CB  . TYR B 1 25  ? -15.626 12.920  44.363  1.00 15.23 ? 13  TYR B CB  1 
ATOM   1591 C  CG  . TYR B 1 25  ? -16.984 12.446  43.927  1.00 17.02 ? 13  TYR B CG  1 
ATOM   1592 C  CD1 . TYR B 1 25  ? -17.977 13.331  43.553  1.00 18.49 ? 13  TYR B CD1 1 
ATOM   1593 C  CD2 . TYR B 1 25  ? -17.276 11.094  43.977  1.00 18.79 ? 13  TYR B CD2 1 
ATOM   1594 C  CE1 . TYR B 1 25  ? -19.249 12.873  43.228  1.00 20.99 ? 13  TYR B CE1 1 
ATOM   1595 C  CE2 . TYR B 1 25  ? -18.542 10.623  43.672  1.00 22.20 ? 13  TYR B CE2 1 
ATOM   1596 C  CZ  . TYR B 1 25  ? -19.530 11.518  43.295  1.00 23.02 ? 13  TYR B CZ  1 
ATOM   1597 O  OH  . TYR B 1 25  ? -20.777 11.040  42.986  1.00 29.31 ? 13  TYR B OH  1 
ATOM   1598 N  N   . TYR B 1 26  ? -13.626 12.299  46.900  1.00 13.08 ? 14  TYR B N   1 
ATOM   1599 C  CA  . TYR B 1 26  ? -12.160 12.145  47.064  1.00 13.04 ? 14  TYR B CA  1 
ATOM   1600 C  C   . TYR B 1 26  ? -11.576 12.154  45.656  1.00 13.22 ? 14  TYR B C   1 
ATOM   1601 O  O   . TYR B 1 26  ? -12.186 11.533  44.750  1.00 14.65 ? 14  TYR B O   1 
ATOM   1602 C  CB  . TYR B 1 26  ? -11.865 10.836  47.808  1.00 13.52 ? 14  TYR B CB  1 
ATOM   1603 C  CG  . TYR B 1 26  ? -10.393 10.557  47.848  1.00 14.74 ? 14  TYR B CG  1 
ATOM   1604 C  CD1 . TYR B 1 26  ? -9.596  11.125  48.815  1.00 15.52 ? 14  TYR B CD1 1 
ATOM   1605 C  CD2 . TYR B 1 26  ? -9.793  9.759   46.891  1.00 16.13 ? 14  TYR B CD2 1 
ATOM   1606 C  CE1 . TYR B 1 26  ? -8.231  10.920  48.827  1.00 15.75 ? 14  TYR B CE1 1 
ATOM   1607 C  CE2 . TYR B 1 26  ? -8.423  9.573   46.873  1.00 14.94 ? 14  TYR B CE2 1 
ATOM   1608 C  CZ  . TYR B 1 26  ? -7.647  10.111  47.873  1.00 15.72 ? 14  TYR B CZ  1 
ATOM   1609 O  OH  . TYR B 1 26  ? -6.294  9.941   47.892  1.00 18.47 ? 14  TYR B OH  1 
ATOM   1610 N  N   . TYR B 1 27  ? -10.410 12.717  45.462  1.00 14.18 ? 15  TYR B N   1 
ATOM   1611 C  CA  . TYR B 1 27  ? -9.658  12.522  44.194  1.00 13.87 ? 15  TYR B CA  1 
ATOM   1612 C  C   . TYR B 1 27  ? -8.215  12.270  44.542  1.00 15.72 ? 15  TYR B C   1 
ATOM   1613 O  O   . TYR B 1 27  ? -7.727  12.819  45.518  1.00 14.32 ? 15  TYR B O   1 
ATOM   1614 C  CB  . TYR B 1 27  ? -9.806  13.660  43.177  1.00 14.54 ? 15  TYR B CB  1 
ATOM   1615 C  CG  . TYR B 1 27  ? -9.124  14.960  43.518  1.00 16.05 ? 15  TYR B CG  1 
ATOM   1616 C  CD1 . TYR B 1 27  ? -9.760  15.929  44.277  1.00 15.62 ? 15  TYR B CD1 1 
ATOM   1617 C  CD2 . TYR B 1 27  ? -7.837  15.230  43.066  1.00 16.04 ? 15  TYR B CD2 1 
ATOM   1618 C  CE1 . TYR B 1 27  ? -9.141  17.125  44.592  1.00 16.36 ? 15  TYR B CE1 1 
ATOM   1619 C  CE2 . TYR B 1 27  ? -7.221  16.442  43.352  1.00 18.30 ? 15  TYR B CE2 1 
ATOM   1620 C  CZ  . TYR B 1 27  ? -7.846  17.368  44.163  1.00 18.18 ? 15  TYR B CZ  1 
ATOM   1621 O  OH  . TYR B 1 27  ? -7.209  18.559  44.455  1.00 18.64 ? 15  TYR B OH  1 
ATOM   1622 N  N   . SER B 1 28  ? -7.582  11.421  43.723  1.00 15.94 ? 16  SER B N   1 
ATOM   1623 C  CA  . SER B 1 28  ? -6.128  11.209  43.768  1.00 15.44 ? 16  SER B CA  1 
ATOM   1624 C  C   . SER B 1 28  ? -5.590  11.335  42.356  1.00 15.85 ? 16  SER B C   1 
ATOM   1625 O  O   . SER B 1 28  ? -6.140  10.686  41.447  1.00 15.57 ? 16  SER B O   1 
ATOM   1626 C  CB  . SER B 1 28  ? -5.762  9.883   44.379  1.00 15.21 ? 16  SER B CB  1 
ATOM   1627 O  OG  . SER B 1 28  ? -4.341  9.730   44.384  1.00 15.56 ? 16  SER B OG  1 
ATOM   1628 N  N   . PHE B 1 29  ? -4.531  12.129  42.207  1.00 14.91 ? 17  PHE B N   1 
ATOM   1629 C  CA  . PHE B 1 29  ? -3.743  12.215  40.955  1.00 14.68 ? 17  PHE B CA  1 
ATOM   1630 C  C   . PHE B 1 29  ? -2.309  11.909  41.348  1.00 15.22 ? 17  PHE B C   1 
ATOM   1631 O  O   . PHE B 1 29  ? -1.756  12.666  42.160  1.00 16.28 ? 17  PHE B O   1 
ATOM   1632 C  CB  . PHE B 1 29  ? -3.783  13.617  40.348  1.00 15.47 ? 17  PHE B CB  1 
ATOM   1633 C  CG  . PHE B 1 29  ? -2.897  13.732  39.132  1.00 16.46 ? 17  PHE B CG  1 
ATOM   1634 C  CD1 . PHE B 1 29  ? -2.945  12.770  38.122  1.00 18.82 ? 17  PHE B CD1 1 
ATOM   1635 C  CD2 . PHE B 1 29  ? -1.984  14.776  39.024  1.00 19.97 ? 17  PHE B CD2 1 
ATOM   1636 C  CE1 . PHE B 1 29  ? -2.099  12.867  37.025  1.00 18.87 ? 17  PHE B CE1 1 
ATOM   1637 C  CE2 . PHE B 1 29  ? -1.152  14.874  37.916  1.00 18.56 ? 17  PHE B CE2 1 
ATOM   1638 C  CZ  . PHE B 1 29  ? -1.220  13.941  36.914  1.00 19.16 ? 17  PHE B CZ  1 
ATOM   1639 N  N   . TRP B 1 30  ? -1.800  10.751  40.927  1.00 14.70 ? 18  TRP B N   1 
ATOM   1640 C  CA  . TRP B 1 30  ? -0.396  10.373  41.220  1.00 14.89 ? 18  TRP B CA  1 
ATOM   1641 C  C   . TRP B 1 30  ? 0.333   10.225  39.890  1.00 14.99 ? 18  TRP B C   1 
ATOM   1642 O  O   . TRP B 1 30  ? -0.128  9.408   39.081  1.00 16.34 ? 18  TRP B O   1 
ATOM   1643 C  CB  . TRP B 1 30  ? -0.313  9.094   42.051  1.00 14.88 ? 18  TRP B CB  1 
ATOM   1644 C  CG  . TRP B 1 30  ? 1.108   8.756   42.361  1.00 17.81 ? 18  TRP B CG  1 
ATOM   1645 C  CD1 . TRP B 1 30  ? 1.882   9.256   43.363  1.00 19.48 ? 18  TRP B CD1 1 
ATOM   1646 C  CD2 . TRP B 1 30  ? 1.922   7.830   41.635  1.00 21.44 ? 18  TRP B CD2 1 
ATOM   1647 N  NE1 . TRP B 1 30  ? 3.146   8.732   43.296  1.00 21.81 ? 18  TRP B NE1 1 
ATOM   1648 C  CE2 . TRP B 1 30  ? 3.193   7.832   42.261  1.00 21.74 ? 18  TRP B CE2 1 
ATOM   1649 C  CE3 . TRP B 1 30  ? 1.682   6.984   40.545  1.00 19.86 ? 18  TRP B CE3 1 
ATOM   1650 C  CZ2 . TRP B 1 30  ? 4.233   7.036   41.789  1.00 21.79 ? 18  TRP B CZ2 1 
ATOM   1651 C  CZ3 . TRP B 1 30  ? 2.718   6.225   40.060  1.00 23.57 ? 18  TRP B CZ3 1 
ATOM   1652 C  CH2 . TRP B 1 30  ? 3.981   6.259   40.681  1.00 21.74 ? 18  TRP B CH2 1 
ATOM   1653 N  N   . THR B 1 31  ? 1.479   10.878  39.731  1.00 13.84 ? 19  THR B N   1 
ATOM   1654 C  CA  . THR B 1 31  ? 2.346   10.677  38.548  1.00 15.34 ? 19  THR B CA  1 
ATOM   1655 C  C   . THR B 1 31  ? 3.798   10.591  39.022  1.00 17.54 ? 19  THR B C   1 
ATOM   1656 O  O   . THR B 1 31  ? 4.120   11.273  40.037  1.00 19.74 ? 19  THR B O   1 
ATOM   1657 C  CB  . THR B 1 31  ? 2.108   11.743  37.488  1.00 17.54 ? 19  THR B CB  1 
ATOM   1658 O  OG1 . THR B 1 31  ? 3.021   11.429  36.440  1.00 19.74 ? 19  THR B OG1 1 
ATOM   1659 C  CG2 . THR B 1 31  ? 2.288   13.174  37.980  1.00 16.76 ? 19  THR B CG2 1 
ATOM   1660 N  N   . ASP B 1 32  ? 4.589   9.703   38.414  1.00 19.48 ? 20  ASP B N   1 
ATOM   1661 C  CA  . ASP B 1 32  ? 6.061   9.670   38.690  1.00 21.43 ? 20  ASP B CA  1 
ATOM   1662 C  C   . ASP B 1 32  ? 6.720   10.897  38.023  1.00 23.69 ? 20  ASP B C   1 
ATOM   1663 O  O   . ASP B 1 32  ? 7.928   11.077  38.215  1.00 22.66 ? 20  ASP B O   1 
ATOM   1664 C  CB  . ASP B 1 32  ? 6.685   8.342   38.292  1.00 23.05 ? 20  ASP B CB  1 
ATOM   1665 C  CG  . ASP B 1 32  ? 6.669   8.046   36.796  1.00 22.54 ? 20  ASP B CG  1 
ATOM   1666 O  OD1 . ASP B 1 32  ? 6.298   8.940   36.042  1.00 22.72 ? 20  ASP B OD1 1 
ATOM   1667 O  OD2 . ASP B 1 32  ? 6.959   6.895   36.416  1.00 24.84 ? 20  ASP B OD2 1 
ATOM   1668 N  N   . GLY B 1 33  ? 5.982   11.656  37.204  1.00 23.60 ? 21  GLY B N   1 
ATOM   1669 C  CA  . GLY B 1 33  ? 6.459   12.910  36.590  1.00 25.23 ? 21  GLY B CA  1 
ATOM   1670 C  C   . GLY B 1 33  ? 7.025   12.725  35.190  1.00 24.20 ? 21  GLY B C   1 
ATOM   1671 O  O   . GLY B 1 33  ? 7.426   13.728  34.569  1.00 28.10 ? 21  GLY B O   1 
ATOM   1672 N  N   . GLY B 1 34  ? 6.995   11.519  34.639  1.00 23.75 ? 22  GLY B N   1 
ATOM   1673 C  CA  . GLY B 1 34  ? 7.424   11.291  33.241  1.00 25.44 ? 22  GLY B CA  1 
ATOM   1674 C  C   . GLY B 1 34  ? 6.445   11.871  32.240  1.00 24.05 ? 22  GLY B C   1 
ATOM   1675 O  O   . GLY B 1 34  ? 5.226   11.831  32.507  1.00 23.13 ? 22  GLY B O   1 
ATOM   1676 N  N   . GLY B 1 35  ? 6.963   12.428  31.131  1.00 23.51 ? 23  GLY B N   1 
ATOM   1677 C  CA  . GLY B 1 35  ? 6.151   12.916  30.003  1.00 22.34 ? 23  GLY B CA  1 
ATOM   1678 C  C   . GLY B 1 35  ? 5.223   14.030  30.426  1.00 25.09 ? 23  GLY B C   1 
ATOM   1679 O  O   . GLY B 1 35  ? 5.610   14.882  31.249  1.00 23.78 ? 23  GLY B O   1 
ATOM   1680 N  N   . GLN B 1 36  ? 4.031   14.071  29.850  1.00 22.54 ? 24  GLN B N   1 
ATOM   1681 C  CA  . GLN B 1 36  ? 3.031   15.094  30.171  1.00 24.34 ? 24  GLN B CA  1 
ATOM   1682 C  C   . GLN B 1 36  ? 1.768   14.373  30.619  1.00 20.74 ? 24  GLN B C   1 
ATOM   1683 O  O   . GLN B 1 36  ? 1.219   13.634  29.822  1.00 18.74 ? 24  GLN B O   1 
ATOM   1684 C  CB  . GLN B 1 36  ? 2.684   15.927  28.945  1.00 27.75 ? 24  GLN B CB  1 
ATOM   1685 C  CG  . GLN B 1 36  ? 3.661   17.044  28.623  1.00 35.59 ? 24  GLN B CG  1 
ATOM   1686 C  CD  . GLN B 1 36  ? 2.964   18.032  27.723  1.00 40.31 ? 24  GLN B CD  1 
ATOM   1687 O  OE1 . GLN B 1 36  ? 3.553   18.623  26.819  1.00 53.66 ? 24  GLN B OE1 1 
ATOM   1688 N  NE2 . GLN B 1 36  ? 1.666   18.173  27.932  1.00 48.69 ? 24  GLN B NE2 1 
ATOM   1689 N  N   . VAL B 1 37  ? 1.305   14.636  31.819  1.00 20.91 ? 25  VAL B N   1 
ATOM   1690 C  CA  . VAL B 1 37  ? 0.021   14.071  32.305  1.00 20.27 ? 25  VAL B CA  1 
ATOM   1691 C  C   . VAL B 1 37  ? -0.746  15.235  32.913  1.00 17.91 ? 25  VAL B C   1 
ATOM   1692 O  O   . VAL B 1 37  ? -0.220  15.815  33.881  1.00 17.36 ? 25  VAL B O   1 
ATOM   1693 C  CB  . VAL B 1 37  ? 0.209   12.926  33.318  1.00 20.20 ? 25  VAL B CB  1 
ATOM   1694 C  CG1 . VAL B 1 37  ? -1.122  12.314  33.723  1.00 19.88 ? 25  VAL B CG1 1 
ATOM   1695 C  CG2 . VAL B 1 37  ? 1.152   11.837  32.828  1.00 21.40 ? 25  VAL B CG2 1 
ATOM   1696 N  N   . THR B 1 38  ? -1.935  15.512  32.382  1.00 15.63 ? 26  THR B N   1 
ATOM   1697 C  CA  . THR B 1 38  ? -2.761  16.653  32.848  1.00 20.12 ? 26  THR B CA  1 
ATOM   1698 C  C   . THR B 1 38  ? -4.083  16.105  33.359  1.00 17.67 ? 26  THR B C   1 
ATOM   1699 O  O   . THR B 1 38  ? -4.853  15.598  32.563  1.00 17.13 ? 26  THR B O   1 
ATOM   1700 C  CB  . THR B 1 38  ? -2.929  17.730  31.779  1.00 23.13 ? 26  THR B CB  1 
ATOM   1701 O  OG1 . THR B 1 38  ? -1.616  18.051  31.299  1.00 26.60 ? 26  THR B OG1 1 
ATOM   1702 C  CG2 . THR B 1 38  ? -3.656  18.943  32.324  1.00 24.62 ? 26  THR B CG2 1 
ATOM   1703 N  N   . TYR B 1 39  ? -4.371  16.369  34.626  1.00 16.18 ? 27  TYR B N   1 
ATOM   1704 C  CA  . TYR B 1 39  ? -5.617  15.934  35.302  1.00 16.54 ? 27  TYR B CA  1 
ATOM   1705 C  C   . TYR B 1 39  ? -6.533  17.148  35.529  1.00 16.52 ? 27  TYR B C   1 
ATOM   1706 O  O   . TYR B 1 39  ? -6.051  18.217  35.913  1.00 15.74 ? 27  TYR B O   1 
ATOM   1707 C  CB  . TYR B 1 39  ? -5.208  15.148  36.552  1.00 16.47 ? 27  TYR B CB  1 
ATOM   1708 C  CG  . TYR B 1 39  ? -6.359  14.802  37.454  1.00 16.14 ? 27  TYR B CG  1 
ATOM   1709 C  CD1 . TYR B 1 39  ? -6.867  15.714  38.352  1.00 18.12 ? 27  TYR B CD1 1 
ATOM   1710 C  CD2 . TYR B 1 39  ? -6.968  13.569  37.357  1.00 15.40 ? 27  TYR B CD2 1 
ATOM   1711 C  CE1 . TYR B 1 39  ? -7.953  15.394  39.159  1.00 18.46 ? 27  TYR B CE1 1 
ATOM   1712 C  CE2 . TYR B 1 39  ? -8.033  13.222  38.158  1.00 16.66 ? 27  TYR B CE2 1 
ATOM   1713 C  CZ  . TYR B 1 39  ? -8.549  14.144  39.038  1.00 15.96 ? 27  TYR B CZ  1 
ATOM   1714 O  OH  . TYR B 1 39  ? -9.614  13.800  39.797  1.00 15.33 ? 27  TYR B OH  1 
ATOM   1715 N  N   . THR B 1 40  ? -7.833  17.010  35.251  1.00 17.18 ? 28  THR B N   1 
ATOM   1716 C  CA  . THR B 1 40  ? -8.793  18.133  35.489  1.00 19.72 ? 28  THR B CA  1 
ATOM   1717 C  C   . THR B 1 40  ? -9.988  17.597  36.259  1.00 18.71 ? 28  THR B C   1 
ATOM   1718 O  O   . THR B 1 40  ? -10.574 16.619  35.794  1.00 19.25 ? 28  THR B O   1 
ATOM   1719 C  CB  . THR B 1 40  ? -9.217  18.834  34.192  1.00 22.92 ? 28  THR B CB  1 
ATOM   1720 O  OG1 . THR B 1 40  ? -8.086  19.191  33.390  1.00 27.01 ? 28  THR B OG1 1 
ATOM   1721 C  CG2 . THR B 1 40  ? -9.902  20.157  34.471  1.00 25.89 ? 28  THR B CG2 1 
ATOM   1722 N  N   . ASN B 1 41  ? -10.303 18.154  37.432  1.00 18.13 ? 29  ASN B N   1 
ATOM   1723 C  CA  . ASN B 1 41  ? -11.611 17.885  38.077  1.00 17.98 ? 29  ASN B CA  1 
ATOM   1724 C  C   . ASN B 1 41  ? -12.722 18.626  37.331  1.00 19.04 ? 29  ASN B C   1 
ATOM   1725 O  O   . ASN B 1 41  ? -12.542 19.833  36.997  1.00 20.60 ? 29  ASN B O   1 
ATOM   1726 C  CB  . ASN B 1 41  ? -11.583 18.236  39.554  1.00 17.08 ? 29  ASN B CB  1 
ATOM   1727 C  CG  . ASN B 1 41  ? -10.783 17.296  40.408  1.00 18.04 ? 29  ASN B CG  1 
ATOM   1728 O  OD1 . ASN B 1 41  ? -10.926 16.080  40.281  1.00 17.45 ? 29  ASN B OD1 1 
ATOM   1729 N  ND2 . ASN B 1 41  ? -10.028 17.837  41.358  1.00 19.01 ? 29  ASN B ND2 1 
ATOM   1730 N  N   . GLY B 1 42  ? -13.830 17.934  37.114  1.00 17.77 ? 30  GLY B N   1 
ATOM   1731 C  CA  . GLY B 1 42  ? -15.096 18.437  36.574  1.00 19.06 ? 30  GLY B CA  1 
ATOM   1732 C  C   . GLY B 1 42  ? -16.160 18.448  37.662  1.00 19.36 ? 30  GLY B C   1 
ATOM   1733 O  O   . GLY B 1 42  ? -15.905 18.077  38.813  1.00 21.05 ? 30  GLY B O   1 
ATOM   1734 N  N   . PRO B 1 43  ? -17.413 18.784  37.300  1.00 21.17 ? 31  PRO B N   1 
ATOM   1735 C  CA  . PRO B 1 43  ? -18.510 18.836  38.263  1.00 21.28 ? 31  PRO B CA  1 
ATOM   1736 C  C   . PRO B 1 43  ? -18.839 17.463  38.855  1.00 21.12 ? 31  PRO B C   1 
ATOM   1737 O  O   . PRO B 1 43  ? -18.601 16.447  38.149  1.00 19.91 ? 31  PRO B O   1 
ATOM   1738 C  CB  . PRO B 1 43  ? -19.680 19.357  37.417  1.00 23.67 ? 31  PRO B CB  1 
ATOM   1739 C  CG  . PRO B 1 43  ? -19.037 20.057  36.271  1.00 23.81 ? 31  PRO B CG  1 
ATOM   1740 C  CD  . PRO B 1 43  ? -17.837 19.188  35.946  1.00 24.38 ? 31  PRO B CD  1 
ATOM   1741 N  N   . ALA B 1 44  ? -19.337 17.419  40.099  1.00 18.40 ? 32  ALA B N   1 
ATOM   1742 C  CA  . ALA B 1 44  ? -19.815 16.168  40.717  1.00 18.39 ? 32  ALA B CA  1 
ATOM   1743 C  C   . ALA B 1 44  ? -18.689 15.138  40.585  1.00 16.94 ? 32  ALA B C   1 
ATOM   1744 O  O   . ALA B 1 44  ? -17.552 15.444  41.006  1.00 18.49 ? 32  ALA B O   1 
ATOM   1745 C  CB  . ALA B 1 44  ? -21.099 15.730  40.053  1.00 18.30 ? 32  ALA B CB  1 
ATOM   1746 N  N   . GLY B 1 45  ? -18.969 13.945  40.043  1.00 18.38 ? 33  GLY B N   1 
ATOM   1747 C  CA  . GLY B 1 45  ? -18.000 12.829  40.055  1.00 17.93 ? 33  GLY B CA  1 
ATOM   1748 C  C   . GLY B 1 45  ? -17.081 12.817  38.833  1.00 16.72 ? 33  GLY B C   1 
ATOM   1749 O  O   . GLY B 1 45  ? -16.473 11.766  38.593  1.00 15.79 ? 33  GLY B O   1 
ATOM   1750 N  N   . GLN B 1 46  ? -17.031 13.899  38.052  1.00 17.09 ? 34  GLN B N   1 
ATOM   1751 C  CA  . GLN B 1 46  ? -16.334 13.902  36.729  1.00 17.27 ? 34  GLN B CA  1 
ATOM   1752 C  C   . GLN B 1 46  ? -14.849 14.182  36.938  1.00 16.25 ? 34  GLN B C   1 
ATOM   1753 O  O   . GLN B 1 46  ? -14.483 15.067  37.711  1.00 16.99 ? 34  GLN B O   1 
ATOM   1754 C  CB  . GLN B 1 46  ? -16.991 14.839  35.706  1.00 19.38 ? 34  GLN B CB  1 
ATOM   1755 C  CG  . GLN B 1 46  ? -16.564 14.591  34.253  1.00 20.54 ? 34  GLN B CG  1 
ATOM   1756 C  CD  . GLN B 1 46  ? -15.261 15.223  33.848  1.00 21.64 ? 34  GLN B CD  1 
ATOM   1757 O  OE1 . GLN B 1 46  ? -14.582 15.852  34.640  1.00 27.83 ? 34  GLN B OE1 1 
ATOM   1758 N  NE2 . GLN B 1 46  ? -14.857 15.027  32.602  1.00 27.09 ? 34  GLN B NE2 1 
ATOM   1759 N  N   . TYR B 1 47  ? -14.007 13.483  36.188  1.00 14.57 ? 35  TYR B N   1 
ATOM   1760 C  CA  . TYR B 1 47  ? -12.595 13.887  36.017  1.00 13.83 ? 35  TYR B CA  1 
ATOM   1761 C  C   . TYR B 1 47  ? -12.192 13.554  34.596  1.00 14.45 ? 35  TYR B C   1 
ATOM   1762 O  O   . TYR B 1 47  ? -12.841 12.748  33.955  1.00 14.39 ? 35  TYR B O   1 
ATOM   1763 C  CB  . TYR B 1 47  ? -11.645 13.245  37.032  1.00 13.47 ? 35  TYR B CB  1 
ATOM   1764 C  CG  . TYR B 1 47  ? -11.412 11.760  36.836  1.00 12.64 ? 35  TYR B CG  1 
ATOM   1765 C  CD1 . TYR B 1 47  ? -12.260 10.822  37.392  1.00 12.60 ? 35  TYR B CD1 1 
ATOM   1766 C  CD2 . TYR B 1 47  ? -10.347 11.300  36.074  1.00 11.93 ? 35  TYR B CD2 1 
ATOM   1767 C  CE1 . TYR B 1 47  ? -12.051 9.459   37.210  1.00 12.38 ? 35  TYR B CE1 1 
ATOM   1768 C  CE2 . TYR B 1 47  ? -10.109 9.943   35.909  1.00 12.86 ? 35  TYR B CE2 1 
ATOM   1769 C  CZ  . TYR B 1 47  ? -10.954 9.031   36.463  1.00 12.07 ? 35  TYR B CZ  1 
ATOM   1770 O  OH  . TYR B 1 47  ? -10.721 7.703   36.258  1.00 12.67 ? 35  TYR B OH  1 
ATOM   1771 N  N   . SER B 1 48  ? -11.140 14.218  34.148  1.00 15.56 ? 36  SER B N   1 
ATOM   1772 C  CA  . SER B 1 48  ? -10.540 13.932  32.828  1.00 17.05 ? 36  SER B CA  1 
ATOM   1773 C  C   . SER B 1 48  ? -9.036  13.873  32.993  1.00 15.74 ? 36  SER B C   1 
ATOM   1774 O  O   . SER B 1 48  ? -8.490  14.441  33.926  1.00 17.13 ? 36  SER B O   1 
ATOM   1775 C  CB  . SER B 1 48  ? -11.037 14.839  31.748  1.00 21.87 ? 36  SER B CB  1 
ATOM   1776 O  OG  . SER B 1 48  ? -10.623 16.165  31.948  1.00 29.04 ? 36  SER B OG  1 
ATOM   1777 N  N   . VAL B 1 49  ? -8.390  13.060  32.167  1.00 16.43 ? 37  VAL B N   1 
ATOM   1778 C  CA  . VAL B 1 49  ? -6.909  13.056  32.139  1.00 16.85 ? 37  VAL B CA  1 
ATOM   1779 C  C   . VAL B 1 49  ? -6.493  12.952  30.685  1.00 17.59 ? 37  VAL B C   1 
ATOM   1780 O  O   . VAL B 1 49  ? -7.249  12.375  29.867  1.00 17.58 ? 37  VAL B O   1 
ATOM   1781 C  CB  . VAL B 1 49  ? -6.304  11.996  33.071  1.00 19.67 ? 37  VAL B CB  1 
ATOM   1782 C  CG1 . VAL B 1 49  ? -6.817  10.590  32.811  1.00 22.26 ? 37  VAL B CG1 1 
ATOM   1783 C  CG2 . VAL B 1 49  ? -4.786  12.061  33.114  1.00 20.14 ? 37  VAL B CG2 1 
ATOM   1784 N  N   . GLU B 1 50  ? -5.425  13.660  30.361  1.00 16.88 ? 38  GLU B N   1 
ATOM   1785 C  CA  . GLU B 1 50  ? -4.860  13.715  28.991  1.00 18.91 ? 38  GLU B CA  1 
ATOM   1786 C  C   . GLU B 1 50  ? -3.376  13.476  29.160  1.00 18.35 ? 38  GLU B C   1 
ATOM   1787 O  O   . GLU B 1 50  ? -2.800  14.021  30.105  1.00 18.31 ? 38  GLU B O   1 
ATOM   1788 C  CB  . GLU B 1 50  ? -5.108  15.062  28.297  1.00 24.16 ? 38  GLU B CB  1 
ATOM   1789 C  CG  . GLU B 1 50  ? -6.536  15.309  27.826  1.00 33.72 ? 38  GLU B CG  1 
ATOM   1790 C  CD  . GLU B 1 50  ? -6.638  16.556  26.959  1.00 40.10 ? 38  GLU B CD  1 
ATOM   1791 O  OE1 . GLU B 1 50  ? -7.675  17.280  27.023  1.00 47.00 ? 38  GLU B OE1 1 
ATOM   1792 O  OE2 . GLU B 1 50  ? -5.651  16.822  26.220  1.00 50.47 ? 38  GLU B OE2 1 
ATOM   1793 N  N   . TRP B 1 51  ? -2.802  12.535  28.427  1.00 17.48 ? 39  TRP B N   1 
ATOM   1794 C  CA  . TRP B 1 51  ? -1.385  12.216  28.692  1.00 16.66 ? 39  TRP B CA  1 
ATOM   1795 C  C   . TRP B 1 51  ? -0.675  11.982  27.378  1.00 15.29 ? 39  TRP B C   1 
ATOM   1796 O  O   . TRP B 1 51  ? -1.335  11.629  26.389  1.00 16.37 ? 39  TRP B O   1 
ATOM   1797 C  CB  . TRP B 1 51  ? -1.206  11.067  29.664  1.00 16.71 ? 39  TRP B CB  1 
ATOM   1798 C  CG  . TRP B 1 51  ? -1.705  9.717   29.254  1.00 15.58 ? 39  TRP B CG  1 
ATOM   1799 C  CD1 . TRP B 1 51  ? -0.899  8.681   28.884  1.00 15.34 ? 39  TRP B CD1 1 
ATOM   1800 C  CD2 . TRP B 1 51  ? -3.044  9.163   29.298  1.00 15.76 ? 39  TRP B CD2 1 
ATOM   1801 N  NE1 . TRP B 1 51  ? -1.622  7.546   28.675  1.00 15.40 ? 39  TRP B NE1 1 
ATOM   1802 C  CE2 . TRP B 1 51  ? -2.935  7.807   28.900  1.00 16.61 ? 39  TRP B CE2 1 
ATOM   1803 C  CE3 . TRP B 1 51  ? -4.315  9.641   29.649  1.00 16.70 ? 39  TRP B CE3 1 
ATOM   1804 C  CZ2 . TRP B 1 51  ? -4.022  6.941   28.858  1.00 14.95 ? 39  TRP B CZ2 1 
ATOM   1805 C  CZ3 . TRP B 1 51  ? -5.395  8.796   29.566  1.00 15.15 ? 39  TRP B CZ3 1 
ATOM   1806 C  CH2 . TRP B 1 51  ? -5.242  7.447   29.215  1.00 15.35 ? 39  TRP B CH2 1 
ATOM   1807 N  N   . SER B 1 52  ? 0.618   12.230  27.424  1.00 16.28 ? 40  SER B N   1 
ATOM   1808 C  CA  . SER B 1 52  ? 1.494   12.191  26.235  1.00 17.81 ? 40  SER B CA  1 
ATOM   1809 C  C   . SER B 1 52  ? 2.853   11.643  26.688  1.00 18.01 ? 40  SER B C   1 
ATOM   1810 O  O   . SER B 1 52  ? 3.510   12.267  27.541  1.00 18.40 ? 40  SER B O   1 
ATOM   1811 C  CB  . SER B 1 52  ? 1.546   13.584  25.606  1.00 21.83 ? 40  SER B CB  1 
ATOM   1812 O  OG  . SER B 1 52  ? 2.465   13.602  24.516  1.00 27.46 ? 40  SER B OG  1 
ATOM   1813 N  N   . ASN B 1 53  ? 3.217   10.428  26.236  1.00 17.86 ? 41  ASN B N   1 
ATOM   1814 C  CA  . ASN B 1 53  ? 4.542   9.831   26.522  1.00 18.25 ? 41  ASN B CA  1 
ATOM   1815 C  C   . ASN B 1 53  ? 4.790   9.833   28.024  1.00 16.09 ? 41  ASN B C   1 
ATOM   1816 O  O   . ASN B 1 53  ? 5.922   10.080  28.478  1.00 16.84 ? 41  ASN B O   1 
ATOM   1817 C  CB  . ASN B 1 53  ? 5.641   10.535  25.742  1.00 19.22 ? 41  ASN B CB  1 
ATOM   1818 C  CG  . ASN B 1 53  ? 5.442   10.450  24.247  1.00 19.50 ? 41  ASN B CG  1 
ATOM   1819 O  OD1 . ASN B 1 53  ? 5.369   9.358   23.695  1.00 18.77 ? 41  ASN B OD1 1 
ATOM   1820 N  ND2 . ASN B 1 53  ? 5.357   11.599  23.585  1.00 22.00 ? 41  ASN B ND2 1 
ATOM   1821 N  N   . SER B 1 54  ? 3.768   9.448   28.774  1.00 17.69 ? 42  SER B N   1 
ATOM   1822 C  CA  . SER B 1 54  ? 3.746   9.406   30.246  1.00 17.66 ? 42  SER B CA  1 
ATOM   1823 C  C   . SER B 1 54  ? 4.823   8.468   30.802  1.00 18.61 ? 42  SER B C   1 
ATOM   1824 O  O   . SER B 1 54  ? 5.201   7.464   30.165  1.00 16.34 ? 42  SER B O   1 
ATOM   1825 C  CB  . SER B 1 54  ? 2.370   9.014   30.698  1.00 15.82 ? 42  SER B CB  1 
ATOM   1826 O  OG  . SER B 1 54  ? 2.150   7.586   30.563  1.00 17.42 ? 42  SER B OG  1 
ATOM   1827 N  N   . GLY B 1 55  ? 5.232   8.727   32.039  1.00 18.53 ? 43  GLY B N   1 
ATOM   1828 C  CA  . GLY B 1 55  ? 5.747   7.668   32.899  1.00 19.37 ? 43  GLY B CA  1 
ATOM   1829 C  C   . GLY B 1 55  ? 4.579   6.934   33.515  1.00 20.31 ? 43  GLY B C   1 
ATOM   1830 O  O   . GLY B 1 55  ? 3.558   6.747   32.797  1.00 20.43 ? 43  GLY B O   1 
ATOM   1831 N  N   . ASN B 1 56  ? 4.657   6.610   34.790  1.00 18.51 ? 44  ASN B N   1 
ATOM   1832 C  CA  . ASN B 1 56  ? 3.551   5.881   35.479  1.00 20.77 ? 44  ASN B CA  1 
ATOM   1833 C  C   . ASN B 1 56  ? 2.599   6.929   36.054  1.00 17.02 ? 44  ASN B C   1 
ATOM   1834 O  O   . ASN B 1 56  ? 3.070   7.799   36.717  1.00 17.15 ? 44  ASN B O   1 
ATOM   1835 C  CB  . ASN B 1 56  ? 4.065   4.910   36.555  1.00 23.55 ? 44  ASN B CB  1 
ATOM   1836 C  CG  . ASN B 1 56  ? 5.133   3.971   36.022  1.00 30.64 ? 44  ASN B CG  1 
ATOM   1837 O  OD1 . ASN B 1 56  ? 5.878   4.346   35.125  1.00 36.99 ? 44  ASN B OD1 1 
ATOM   1838 N  ND2 . ASN B 1 56  ? 5.224   2.753   36.539  1.00 34.82 ? 44  ASN B ND2 1 
ATOM   1839 N  N   . PHE B 1 57  ? 1.285   6.808   35.842  1.00 14.42 ? 45  PHE B N   1 
ATOM   1840 C  CA  . PHE B 1 57  ? 0.318   7.610   36.613  1.00 14.22 ? 45  PHE B CA  1 
ATOM   1841 C  C   . PHE B 1 57  ? -0.904  6.773   36.924  1.00 14.05 ? 45  PHE B C   1 
ATOM   1842 O  O   . PHE B 1 57  ? -1.217  5.794   36.214  1.00 13.65 ? 45  PHE B O   1 
ATOM   1843 C  CB  . PHE B 1 57  ? -0.056  8.902   35.871  1.00 14.32 ? 45  PHE B CB  1 
ATOM   1844 C  CG  . PHE B 1 57  ? -1.006  8.704   34.705  1.00 12.52 ? 45  PHE B CG  1 
ATOM   1845 C  CD1 . PHE B 1 57  ? -2.370  8.696   34.894  1.00 12.74 ? 45  PHE B CD1 1 
ATOM   1846 C  CD2 . PHE B 1 57  ? -0.536  8.401   33.438  1.00 14.17 ? 45  PHE B CD2 1 
ATOM   1847 C  CE1 . PHE B 1 57  ? -3.236  8.443   33.837  1.00 13.21 ? 45  PHE B CE1 1 
ATOM   1848 C  CE2 . PHE B 1 57  ? -1.403  8.232   32.368  1.00 15.23 ? 45  PHE B CE2 1 
ATOM   1849 C  CZ  . PHE B 1 57  ? -2.761  8.248   32.573  1.00 14.06 ? 45  PHE B CZ  1 
ATOM   1850 N  N   . VAL B 1 58  ? -1.626  7.219   37.949  1.00 15.13 ? 46  VAL B N   1 
ATOM   1851 C  CA  . VAL B 1 58  ? -2.921  6.610   38.356  1.00 17.54 ? 46  VAL B CA  1 
ATOM   1852 C  C   . VAL B 1 58  ? -3.748  7.751   38.934  1.00 17.14 ? 46  VAL B C   1 
ATOM   1853 O  O   . VAL B 1 58  ? -3.257  8.435   39.799  1.00 16.62 ? 46  VAL B O   1 
ATOM   1854 C  CB  . VAL B 1 58  ? -2.802  5.450   39.372  1.00 21.06 ? 46  VAL B CB  1 
ATOM   1855 C  CG1 . VAL B 1 58  ? -4.156  4.758   39.511  1.00 21.63 ? 46  VAL B CG1 1 
ATOM   1856 C  CG2 . VAL B 1 58  ? -1.709  4.445   39.045  1.00 25.68 ? 46  VAL B CG2 1 
ATOM   1857 N  N   . ALA B 1 59  ? -4.978  7.952   38.459  1.00 15.35 ? 47  ALA B N   1 
ATOM   1858 C  CA  . ALA B 1 59  ? -5.750  9.117   38.862  1.00 15.96 ? 47  ALA B CA  1 
ATOM   1859 C  C   . ALA B 1 59  ? -7.232  8.808   38.811  1.00 13.95 ? 47  ALA B C   1 
ATOM   1860 O  O   . ALA B 1 59  ? -7.651  8.061   37.901  1.00 13.83 ? 47  ALA B O   1 
ATOM   1861 C  CB  . ALA B 1 59  ? -5.408  10.271  37.964  1.00 16.52 ? 47  ALA B CB  1 
ATOM   1862 N  N   . GLY B 1 60  ? -7.991  9.449   39.706  1.00 13.04 ? 48  GLY B N   1 
ATOM   1863 C  CA  . GLY B 1 60  ? -9.448  9.396   39.572  1.00 12.41 ? 48  GLY B CA  1 
ATOM   1864 C  C   . GLY B 1 60  ? -10.171 9.777   40.831  1.00 12.20 ? 48  GLY B C   1 
ATOM   1865 O  O   . GLY B 1 60  ? -9.523  10.290  41.774  1.00 13.10 ? 48  GLY B O   1 
ATOM   1866 N  N   . LYS B 1 61  ? -11.488 9.597   40.792  1.00 12.09 ? 49  LYS B N   1 
ATOM   1867 C  CA  . LYS B 1 61  ? -12.426 10.078  41.843  1.00 14.04 ? 49  LYS B CA  1 
ATOM   1868 C  C   . LYS B 1 61  ? -13.122 8.910   42.519  1.00 13.55 ? 49  LYS B C   1 
ATOM   1869 O  O   . LYS B 1 61  ? -13.332 7.814   41.907  1.00 13.19 ? 49  LYS B O   1 
ATOM   1870 C  CB  . LYS B 1 61  ? -13.484 11.030  41.269  1.00 13.36 ? 49  LYS B CB  1 
ATOM   1871 C  CG  . LYS B 1 61  ? -13.124 12.499  41.291  1.00 13.69 ? 49  LYS B CG  1 
ATOM   1872 C  CD  . LYS B 1 61  ? -14.208 13.370  40.782  1.00 15.01 ? 49  LYS B CD  1 
ATOM   1873 C  CE  . LYS B 1 61  ? -13.874 14.824  41.052  1.00 15.19 ? 49  LYS B CE  1 
ATOM   1874 N  NZ  . LYS B 1 61  ? -14.818 15.747  40.395  1.00 16.54 ? 49  LYS B NZ  1 
ATOM   1875 N  N   . GLY B 1 62  ? -13.498 9.136   43.781  1.00 14.00 ? 50  GLY B N   1 
ATOM   1876 C  CA  . GLY B 1 62  ? -14.325 8.190   44.511  1.00 14.83 ? 50  GLY B CA  1 
ATOM   1877 C  C   . GLY B 1 62  ? -14.513 8.601   45.948  1.00 14.93 ? 50  GLY B C   1 
ATOM   1878 O  O   . GLY B 1 62  ? -14.954 9.734   46.186  1.00 15.55 ? 50  GLY B O   1 
ATOM   1879 N  N   . TRP B 1 63  ? -14.084 7.739   46.854  1.00 14.51 ? 51  TRP B N   1 
ATOM   1880 C  CA  . TRP B 1 63  ? -14.489 7.773   48.281  1.00 15.65 ? 51  TRP B CA  1 
ATOM   1881 C  C   . TRP B 1 63  ? -13.279 7.560   49.189  1.00 16.62 ? 51  TRP B C   1 
ATOM   1882 O  O   . TRP B 1 63  ? -12.335 6.859   48.853  1.00 14.95 ? 51  TRP B O   1 
ATOM   1883 C  CB  . TRP B 1 63  ? -15.564 6.739   48.544  1.00 16.85 ? 51  TRP B CB  1 
ATOM   1884 C  CG  . TRP B 1 63  ? -16.748 6.888   47.654  1.00 18.43 ? 51  TRP B CG  1 
ATOM   1885 C  CD1 . TRP B 1 63  ? -17.903 7.579   47.882  1.00 22.28 ? 51  TRP B CD1 1 
ATOM   1886 C  CD2 . TRP B 1 63  ? -16.850 6.341   46.340  1.00 21.69 ? 51  TRP B CD2 1 
ATOM   1887 N  NE1 . TRP B 1 63  ? -18.728 7.477   46.795  1.00 24.16 ? 51  TRP B NE1 1 
ATOM   1888 C  CE2 . TRP B 1 63  ? -18.116 6.714   45.837  1.00 24.04 ? 51  TRP B CE2 1 
ATOM   1889 C  CE3 . TRP B 1 63  ? -16.041 5.476   45.597  1.00 20.91 ? 51  TRP B CE3 1 
ATOM   1890 C  CZ2 . TRP B 1 63  ? -18.553 6.301   44.571  1.00 25.68 ? 51  TRP B CZ2 1 
ATOM   1891 C  CZ3 . TRP B 1 63  ? -16.439 5.133   44.327  1.00 23.94 ? 51  TRP B CZ3 1 
ATOM   1892 C  CH2 . TRP B 1 63  ? -17.691 5.521   43.838  1.00 24.44 ? 51  TRP B CH2 1 
ATOM   1893 N  N   . ASN B 1 64  ? -13.320 8.189   50.342  1.00 16.76 ? 52  ASN B N   1 
ATOM   1894 C  CA  . ASN B 1 64  ? -12.367 7.939   51.428  1.00 18.72 ? 52  ASN B CA  1 
ATOM   1895 C  C   . ASN B 1 64  ? -13.181 8.049   52.709  1.00 18.79 ? 52  ASN B C   1 
ATOM   1896 O  O   . ASN B 1 64  ? -13.741 9.112   52.963  1.00 17.59 ? 52  ASN B O   1 
ATOM   1897 C  CB  . ASN B 1 64  ? -11.203 8.916   51.408  1.00 20.72 ? 52  ASN B CB  1 
ATOM   1898 C  CG  . ASN B 1 64  ? -10.003 8.312   52.092  1.00 23.58 ? 52  ASN B CG  1 
ATOM   1899 O  OD1 . ASN B 1 64  ? -10.060 7.141   52.479  1.00 24.07 ? 52  ASN B OD1 1 
ATOM   1900 N  ND2 . ASN B 1 64  ? -8.945  9.095   52.251  1.00 23.38 ? 52  ASN B ND2 1 
ATOM   1901 N  N   . PRO B 1 65  ? -13.335 6.961   53.489  1.00 18.83 ? 53  PRO B N   1 
ATOM   1902 C  CA  . PRO B 1 65  ? -12.856 5.620   53.118  1.00 19.00 ? 53  PRO B CA  1 
ATOM   1903 C  C   . PRO B 1 65  ? -13.762 4.913   52.110  1.00 18.26 ? 53  PRO B C   1 
ATOM   1904 O  O   . PRO B 1 65  ? -14.958 5.221   52.052  1.00 17.10 ? 53  PRO B O   1 
ATOM   1905 C  CB  . PRO B 1 65  ? -12.956 4.863   54.456  1.00 20.67 ? 53  PRO B CB  1 
ATOM   1906 C  CG  . PRO B 1 65  ? -14.152 5.481   55.108  1.00 21.87 ? 53  PRO B CG  1 
ATOM   1907 C  CD  . PRO B 1 65  ? -14.098 6.962   54.753  1.00 20.62 ? 53  PRO B CD  1 
ATOM   1908 N  N   . GLY B 1 66  ? -13.204 3.998   51.301  1.00 18.63 ? 54  GLY B N   1 
ATOM   1909 C  CA  . GLY B 1 66  ? -14.048 3.013   50.589  1.00 20.29 ? 54  GLY B CA  1 
ATOM   1910 C  C   . GLY B 1 66  ? -14.903 2.244   51.589  1.00 20.71 ? 54  GLY B C   1 
ATOM   1911 O  O   . GLY B 1 66  ? -14.428 1.988   52.693  1.00 20.83 ? 54  GLY B O   1 
ATOM   1912 N  N   . SER B 1 67  ? -16.156 1.958   51.275  1.00 23.40 ? 55  SER B N   1 
ATOM   1913 C  CA  . SER B 1 67  ? -17.025 1.113   52.149  1.00 25.56 ? 55  SER B CA  1 
ATOM   1914 C  C   . SER B 1 67  ? -17.606 -0.080  51.383  1.00 26.07 ? 55  SER B C   1 
ATOM   1915 O  O   . SER B 1 67  ? -18.741 -0.484  51.691  1.00 25.54 ? 55  SER B O   1 
ATOM   1916 C  CB  . SER B 1 67  ? -18.099 1.927   52.804  1.00 27.54 ? 55  SER B CB  1 
ATOM   1917 O  OG  . SER B 1 67  ? -18.706 2.790   51.869  1.00 31.53 ? 55  SER B OG  1 
ATOM   1918 N  N   . SER B 1 68  ? -16.865 -0.631  50.431  1.00 22.87 ? 56  SER B N   1 
ATOM   1919 C  CA  . SER B 1 68  ? -17.281 -1.854  49.707  1.00 24.39 ? 56  SER B CA  1 
ATOM   1920 C  C   . SER B 1 68  ? -18.607 -1.573  48.991  1.00 25.42 ? 56  SER B C   1 
ATOM   1921 O  O   . SER B 1 68  ? -19.469 -2.457  48.932  1.00 29.04 ? 56  SER B O   1 
ATOM   1922 C  CB  . SER B 1 68  ? -17.376 -3.064  50.619  1.00 23.91 ? 56  SER B CB  1 
ATOM   1923 O  OG  . SER B 1 68  ? -16.168 -3.306  51.319  1.00 25.74 ? 56  SER B OG  1 
ATOM   1924 N  N   . GLN B 1 69  ? -18.777 -0.365  48.458  1.00 24.64 ? 57  GLN B N   1 
ATOM   1925 C  CA  . GLN B 1 69  ? -20.061 -0.022  47.798  1.00 25.79 ? 57  GLN B CA  1 
ATOM   1926 C  C   . GLN B 1 69  ? -20.084 -0.554  46.368  1.00 20.75 ? 57  GLN B C   1 
ATOM   1927 O  O   . GLN B 1 69  ? -19.041 -0.765  45.767  1.00 19.97 ? 57  GLN B O   1 
ATOM   1928 C  CB  . GLN B 1 69  ? -20.344 1.479   47.842  1.00 29.56 ? 57  GLN B CB  1 
ATOM   1929 C  CG  . GLN B 1 69  ? -19.205 2.351   47.355  1.00 29.32 ? 57  GLN B CG  1 
ATOM   1930 C  CD  . GLN B 1 69  ? -18.444 2.992   48.493  1.00 31.25 ? 57  GLN B CD  1 
ATOM   1931 O  OE1 . GLN B 1 69  ? -17.598 2.367   49.134  1.00 27.02 ? 57  GLN B OE1 1 
ATOM   1932 N  NE2 . GLN B 1 69  ? -18.694 4.277   48.722  1.00 31.03 ? 57  GLN B NE2 1 
ATOM   1933 N  N   . THR B 1 70  ? -21.283 -0.698  45.837  1.00 20.14 ? 58  THR B N   1 
ATOM   1934 C  CA  . THR B 1 70  ? -21.546 -0.938  44.407  1.00 20.11 ? 58  THR B CA  1 
ATOM   1935 C  C   . THR B 1 70  ? -21.351 0.386   43.672  1.00 22.15 ? 58  THR B C   1 
ATOM   1936 O  O   . THR B 1 70  ? -22.016 1.392   44.010  1.00 24.35 ? 58  THR B O   1 
ATOM   1937 C  CB  . THR B 1 70  ? -22.914 -1.592  44.218  1.00 22.91 ? 58  THR B CB  1 
ATOM   1938 O  OG1 . THR B 1 70  ? -22.859 -2.869  44.864  1.00 23.22 ? 58  THR B OG1 1 
ATOM   1939 C  CG2 . THR B 1 70  ? -23.300 -1.771  42.773  1.00 24.35 ? 58  THR B CG2 1 
ATOM   1940 N  N   . ILE B 1 71  ? -20.430 0.384   42.712  1.00 19.26 ? 59  ILE B N   1 
ATOM   1941 C  CA  . ILE B 1 71  ? -19.976 1.575   41.947  1.00 20.36 ? 59  ILE B CA  1 
ATOM   1942 C  C   . ILE B 1 71  ? -20.638 1.581   40.574  1.00 21.51 ? 59  ILE B C   1 
ATOM   1943 O  O   . ILE B 1 71  ? -20.621 0.551   39.938  1.00 22.54 ? 59  ILE B O   1 
ATOM   1944 C  CB  . ILE B 1 71  ? -18.448 1.511   41.776  1.00 21.07 ? 59  ILE B CB  1 
ATOM   1945 C  CG1 . ILE B 1 71  ? -17.778 1.610   43.147  1.00 22.45 ? 59  ILE B CG1 1 
ATOM   1946 C  CG2 . ILE B 1 71  ? -17.982 2.561   40.779  1.00 24.78 ? 59  ILE B CG2 1 
ATOM   1947 C  CD1 . ILE B 1 71  ? -16.277 1.619   43.084  1.00 23.11 ? 59  ILE B CD1 1 
ATOM   1948 N  N   . THR B 1 72  ? -21.150 2.719   40.144  1.00 21.18 ? 60  THR B N   1 
ATOM   1949 C  CA  . THR B 1 72  ? -21.578 2.915   38.747  1.00 24.00 ? 60  THR B CA  1 
ATOM   1950 C  C   . THR B 1 72  ? -20.797 4.122   38.237  1.00 21.60 ? 60  THR B C   1 
ATOM   1951 O  O   . THR B 1 72  ? -20.501 5.019   39.000  1.00 21.55 ? 60  THR B O   1 
ATOM   1952 C  CB  . THR B 1 72  ? -23.102 3.029   38.627  1.00 28.78 ? 60  THR B CB  1 
ATOM   1953 O  OG1 . THR B 1 72  ? -23.538 4.141   39.396  1.00 35.23 ? 60  THR B OG1 1 
ATOM   1954 C  CG2 . THR B 1 72  ? -23.834 1.808   39.130  1.00 32.45 ? 60  THR B CG2 1 
ATOM   1955 N  N   . TYR B 1 73  ? -20.370 4.066   37.000  1.00 20.93 ? 61  TYR B N   1 
ATOM   1956 C  CA  . TYR B 1 73  ? -19.622 5.179   36.413  1.00 20.59 ? 61  TYR B CA  1 
ATOM   1957 C  C   . TYR B 1 73  ? -19.902 5.150   34.915  1.00 22.13 ? 61  TYR B C   1 
ATOM   1958 O  O   . TYR B 1 73  ? -20.355 4.128   34.414  1.00 21.62 ? 61  TYR B O   1 
ATOM   1959 C  CB  . TYR B 1 73  ? -18.132 5.059   36.784  1.00 22.39 ? 61  TYR B CB  1 
ATOM   1960 C  CG  . TYR B 1 73  ? -17.418 3.993   36.020  1.00 21.97 ? 61  TYR B CG  1 
ATOM   1961 C  CD1 . TYR B 1 73  ? -17.500 2.670   36.403  1.00 22.38 ? 61  TYR B CD1 1 
ATOM   1962 C  CD2 . TYR B 1 73  ? -16.791 4.289   34.824  1.00 22.76 ? 61  TYR B CD2 1 
ATOM   1963 C  CE1 . TYR B 1 73  ? -16.922 1.668   35.652  1.00 28.10 ? 61  TYR B CE1 1 
ATOM   1964 C  CE2 . TYR B 1 73  ? -16.183 3.307   34.068  1.00 22.99 ? 61  TYR B CE2 1 
ATOM   1965 C  CZ  . TYR B 1 73  ? -16.260 1.993   34.481  1.00 23.42 ? 61  TYR B CZ  1 
ATOM   1966 O  OH  . TYR B 1 73  ? -15.724 1.002   33.731  1.00 26.00 ? 61  TYR B OH  1 
ATOM   1967 N  N   . SER B 1 74  ? -19.630 6.257   34.245  1.00 21.16 ? 62  SER B N   1 
ATOM   1968 C  CA  . SER B 1 74  ? -19.823 6.376   32.777  1.00 21.17 ? 62  SER B CA  1 
ATOM   1969 C  C   . SER B 1 74  ? -18.644 7.131   32.188  1.00 19.00 ? 62  SER B C   1 
ATOM   1970 O  O   . SER B 1 74  ? -17.783 7.586   32.939  1.00 17.40 ? 62  SER B O   1 
ATOM   1971 C  CB  . SER B 1 74  ? -21.127 7.032   32.451  1.00 22.76 ? 62  SER B CB  1 
ATOM   1972 O  OG  . SER B 1 74  ? -21.169 8.360   32.935  1.00 24.79 ? 62  SER B OG  1 
ATOM   1973 N  N   . GLY B 1 75  ? -18.568 7.143   30.868  1.00 17.93 ? 63  GLY B N   1 
ATOM   1974 C  CA  . GLY B 1 75  ? -17.665 8.046   30.150  1.00 17.91 ? 63  GLY B CA  1 
ATOM   1975 C  C   . GLY B 1 75  ? -16.883 7.297   29.094  1.00 15.95 ? 63  GLY B C   1 
ATOM   1976 O  O   . GLY B 1 75  ? -17.422 6.316   28.499  1.00 17.12 ? 63  GLY B O   1 
ATOM   1977 N  N   . GLU B 1 76  ? -15.641 7.734   28.871  1.00 16.05 ? 64  GLU B N   1 
ATOM   1978 C  CA  . GLU B 1 76  ? -14.837 7.418   27.661  1.00 17.98 ? 64  GLU B CA  1 
ATOM   1979 C  C   . GLU B 1 76  ? -13.406 7.185   28.137  1.00 17.06 ? 64  GLU B C   1 
ATOM   1980 O  O   . GLU B 1 76  ? -13.005 7.928   29.038  1.00 16.08 ? 64  GLU B O   1 
ATOM   1981 C  CB  . GLU B 1 76  ? -14.755 8.641   26.726  1.00 24.38 ? 64  GLU B CB  1 
ATOM   1982 C  CG  . GLU B 1 76  ? -16.073 9.192   26.242  1.00 33.77 ? 64  GLU B CG  1 
ATOM   1983 C  CD  . GLU B 1 76  ? -15.976 9.802   24.853  1.00 33.79 ? 64  GLU B CD  1 
ATOM   1984 O  OE1 . GLU B 1 76  ? -17.025 10.215  24.307  1.00 45.87 ? 64  GLU B OE1 1 
ATOM   1985 O  OE2 . GLU B 1 76  ? -14.845 9.831   24.307  1.00 41.82 ? 64  GLU B OE2 1 
ATOM   1986 N  N   . TRP B 1 77  ? -12.720 6.171   27.610  1.00 15.23 ? 65  TRP B N   1 
ATOM   1987 C  CA  . TRP B 1 77  ? -11.288 5.910   27.902  1.00 15.50 ? 65  TRP B CA  1 
ATOM   1988 C  C   . TRP B 1 77  ? -10.595 5.556   26.577  1.00 15.44 ? 65  TRP B C   1 
ATOM   1989 O  O   . TRP B 1 77  ? -10.903 4.497   26.024  1.00 17.14 ? 65  TRP B O   1 
ATOM   1990 C  CB  . TRP B 1 77  ? -11.244 4.795   28.923  1.00 16.08 ? 65  TRP B CB  1 
ATOM   1991 C  CG  . TRP B 1 77  ? -9.923  4.123   29.097  1.00 15.94 ? 65  TRP B CG  1 
ATOM   1992 C  CD1 . TRP B 1 77  ? -8.849  4.564   29.815  1.00 17.90 ? 65  TRP B CD1 1 
ATOM   1993 C  CD2 . TRP B 1 77  ? -9.600  2.804   28.622  1.00 15.57 ? 65  TRP B CD2 1 
ATOM   1994 N  NE1 . TRP B 1 77  ? -7.865  3.614   29.794  1.00 19.39 ? 65  TRP B NE1 1 
ATOM   1995 C  CE2 . TRP B 1 77  ? -8.282  2.527   29.062  1.00 18.05 ? 65  TRP B CE2 1 
ATOM   1996 C  CE3 . TRP B 1 77  ? -10.248 1.871   27.811  1.00 16.45 ? 65  TRP B CE3 1 
ATOM   1997 C  CZ2 . TRP B 1 77  ? -7.661  1.317   28.763  1.00 18.86 ? 65  TRP B CZ2 1 
ATOM   1998 C  CZ3 . TRP B 1 77  ? -9.629  0.682   27.497  1.00 17.98 ? 65  TRP B CZ3 1 
ATOM   1999 C  CH2 . TRP B 1 77  ? -8.329  0.420   27.955  1.00 18.11 ? 65  TRP B CH2 1 
ATOM   2000 N  N   . ASN B 1 78  ? -9.704  6.432   26.118  1.00 16.21 ? 66  ASN B N   1 
ATOM   2001 C  CA  . ASN B 1 78  ? -9.141  6.429   24.752  1.00 18.56 ? 66  ASN B CA  1 
ATOM   2002 C  C   . ASN B 1 78  ? -7.625  6.355   24.857  1.00 18.19 ? 66  ASN B C   1 
ATOM   2003 O  O   . ASN B 1 78  ? -6.948  7.330   24.539  1.00 16.22 ? 66  ASN B O   1 
ATOM   2004 C  CB  . ASN B 1 78  ? -9.618  7.650   23.977  1.00 19.50 ? 66  ASN B CB  1 
ATOM   2005 C  CG  . ASN B 1 78  ? -11.128 7.618   23.815  1.00 22.21 ? 66  ASN B CG  1 
ATOM   2006 O  OD1 . ASN B 1 78  ? -11.636 6.673   23.233  1.00 29.43 ? 66  ASN B OD1 1 
ATOM   2007 N  ND2 . ASN B 1 78  ? -11.832 8.582   24.380  1.00 26.89 ? 66  ASN B ND2 1 
ATOM   2008 N  N   . PRO B 1 79  ? -7.042  5.199   25.235  1.00 18.78 ? 67  PRO B N   1 
ATOM   2009 C  CA  . PRO B 1 79  ? -5.578  5.098   25.289  1.00 18.31 ? 67  PRO B CA  1 
ATOM   2010 C  C   . PRO B 1 79  ? -4.964  4.803   23.916  1.00 19.38 ? 67  PRO B C   1 
ATOM   2011 O  O   . PRO B 1 79  ? -5.620  4.314   23.018  1.00 22.14 ? 67  PRO B O   1 
ATOM   2012 C  CB  . PRO B 1 79  ? -5.328  3.893   26.188  1.00 20.03 ? 67  PRO B CB  1 
ATOM   2013 C  CG  . PRO B 1 79  ? -6.520  3.017   25.921  1.00 20.07 ? 67  PRO B CG  1 
ATOM   2014 C  CD  . PRO B 1 79  ? -7.694  3.954   25.660  1.00 20.90 ? 67  PRO B CD  1 
ATOM   2015 N  N   . ASN B 1 80  ? -3.706  5.167   23.802  1.00 17.89 ? 68  ASN B N   1 
ATOM   2016 C  CA  . ASN B 1 80  ? -2.779  4.783   22.722  1.00 19.49 ? 68  ASN B CA  1 
ATOM   2017 C  C   . ASN B 1 80  ? -1.549  4.225   23.434  1.00 19.04 ? 68  ASN B C   1 
ATOM   2018 O  O   . ASN B 1 80  ? -0.658  4.996   23.738  1.00 19.25 ? 68  ASN B O   1 
ATOM   2019 C  CB  . ASN B 1 80  ? -2.460  5.947   21.778  1.00 24.29 ? 68  ASN B CB  1 
ATOM   2020 C  CG  . ASN B 1 80  ? -1.538  5.491   20.668  1.00 29.45 ? 68  ASN B CG  1 
ATOM   2021 O  OD1 . ASN B 1 80  ? -1.440  4.291   20.419  1.00 35.14 ? 68  ASN B OD1 1 
ATOM   2022 N  ND2 . ASN B 1 80  ? -0.886  6.424   19.993  1.00 37.63 ? 68  ASN B ND2 1 
ATOM   2023 N  N   . GLY B 1 81  ? -1.568  2.905   23.682  1.00 17.80 ? 69  GLY B N   1 
ATOM   2024 C  CA  . GLY B 1 81  ? -0.569  2.154   24.451  1.00 17.26 ? 69  GLY B CA  1 
ATOM   2025 C  C   . GLY B 1 81  ? -1.081  1.799   25.831  1.00 16.24 ? 69  GLY B C   1 
ATOM   2026 O  O   . GLY B 1 81  ? -2.309  1.779   26.040  1.00 18.02 ? 69  GLY B O   1 
ATOM   2027 N  N   . ASN B 1 82  ? -0.163  1.493   26.723  1.00 16.81 ? 70  ASN B N   1 
ATOM   2028 C  CA  . ASN B 1 82  ? -0.435  0.771   27.977  1.00 17.11 ? 70  ASN B CA  1 
ATOM   2029 C  C   . ASN B 1 82  ? -1.268  1.648   28.904  1.00 16.35 ? 70  ASN B C   1 
ATOM   2030 O  O   . ASN B 1 82  ? -0.835  2.763   29.274  1.00 16.45 ? 70  ASN B O   1 
ATOM   2031 C  CB  . ASN B 1 82  ? 0.869   0.248   28.572  1.00 19.13 ? 70  ASN B CB  1 
ATOM   2032 C  CG  . ASN B 1 82  ? 0.752   -0.439  29.900  1.00 18.19 ? 70  ASN B CG  1 
ATOM   2033 O  OD1 . ASN B 1 82  ? -0.322  -0.756  30.397  1.00 22.11 ? 70  ASN B OD1 1 
ATOM   2034 N  ND2 . ASN B 1 82  ? 1.909   -0.658  30.502  1.00 21.83 ? 70  ASN B ND2 1 
ATOM   2035 N  N   . SER B 1 83  ? -2.476  1.195   29.161  1.00 14.53 ? 71  SER B N   1 
ATOM   2036 C  CA  . SER B 1 83  ? -3.403  1.914   30.053  1.00 14.55 ? 71  SER B CA  1 
ATOM   2037 C  C   . SER B 1 83  ? -4.436  0.946   30.590  1.00 14.48 ? 71  SER B C   1 
ATOM   2038 O  O   . SER B 1 83  ? -4.703  -0.076  29.916  1.00 13.97 ? 71  SER B O   1 
ATOM   2039 C  CB  . SER B 1 83  ? -4.019  3.055   29.301  1.00 13.89 ? 71  SER B CB  1 
ATOM   2040 O  OG  . SER B 1 83  ? -5.004  3.708   30.097  1.00 14.94 ? 71  SER B OG  1 
ATOM   2041 N  N   . TYR B 1 84  ? -4.978  1.200   31.783  1.00 12.91 ? 72  TYR B N   1 
ATOM   2042 C  CA  . TYR B 1 84  ? -6.129  0.421   32.249  1.00 13.94 ? 72  TYR B CA  1 
ATOM   2043 C  C   . TYR B 1 84  ? -7.051  1.299   33.062  1.00 14.13 ? 72  TYR B C   1 
ATOM   2044 O  O   . TYR B 1 84  ? -6.676  2.443   33.504  1.00 13.48 ? 72  TYR B O   1 
ATOM   2045 C  CB  . TYR B 1 84  ? -5.793  -0.863  33.011  1.00 15.69 ? 72  TYR B CB  1 
ATOM   2046 C  CG  . TYR B 1 84  ? -4.537  -0.875  33.825  1.00 17.29 ? 72  TYR B CG  1 
ATOM   2047 C  CD1 . TYR B 1 84  ? -3.334  -1.058  33.160  1.00 19.87 ? 72  TYR B CD1 1 
ATOM   2048 C  CD2 . TYR B 1 84  ? -4.550  -0.808  35.203  1.00 24.84 ? 72  TYR B CD2 1 
ATOM   2049 C  CE1 . TYR B 1 84  ? -2.145  -1.146  33.851  1.00 24.95 ? 72  TYR B CE1 1 
ATOM   2050 C  CE2 . TYR B 1 84  ? -3.360  -0.868  35.903  1.00 25.33 ? 72  TYR B CE2 1 
ATOM   2051 C  CZ  . TYR B 1 84  ? -2.164  -1.033  35.223  1.00 26.73 ? 72  TYR B CZ  1 
ATOM   2052 O  OH  . TYR B 1 84  ? -0.955  -1.162  35.859  1.00 30.76 ? 72  TYR B OH  1 
ATOM   2053 N  N   . LEU B 1 85  ? -8.289  0.834   33.057  1.00 13.13 ? 73  LEU B N   1 
ATOM   2054 C  CA  . LEU B 1 85  ? -9.444  1.443   33.719  1.00 14.19 ? 73  LEU B CA  1 
ATOM   2055 C  C   . LEU B 1 85  ? -9.914  0.485   34.780  1.00 13.76 ? 73  LEU B C   1 
ATOM   2056 O  O   . LEU B 1 85  ? -10.130 -0.733  34.458  1.00 14.66 ? 73  LEU B O   1 
ATOM   2057 C  CB  . LEU B 1 85  ? -10.540 1.734   32.689  1.00 16.08 ? 73  LEU B CB  1 
ATOM   2058 C  CG  . LEU B 1 85  ? -11.745 2.459   33.270  1.00 17.83 ? 73  LEU B CG  1 
ATOM   2059 C  CD1 . LEU B 1 85  ? -11.427 3.856   33.784  1.00 18.30 ? 73  LEU B CD1 1 
ATOM   2060 C  CD2 . LEU B 1 85  ? -12.840 2.573   32.196  1.00 18.57 ? 73  LEU B CD2 1 
ATOM   2061 N  N   . SER B 1 86  ? -9.969  0.941   36.038  1.00 14.31 ? 74  SER B N   1 
ATOM   2062 C  CA  . SER B 1 86  ? -10.142 0.006   37.172  1.00 14.44 ? 74  SER B CA  1 
ATOM   2063 C  C   . SER B 1 86  ? -10.847 0.701   38.328  1.00 14.13 ? 74  SER B C   1 
ATOM   2064 O  O   . SER B 1 86  ? -10.824 1.984   38.390  1.00 15.23 ? 74  SER B O   1 
ATOM   2065 C  CB  . SER B 1 86  ? -8.782  -0.517  37.611  1.00 17.72 ? 74  SER B CB  1 
ATOM   2066 O  OG  . SER B 1 86  ? -8.123  0.451   38.388  1.00 24.68 ? 74  SER B OG  1 
ATOM   2067 N  N   . VAL B 1 87  ? -11.461 -0.096  39.195  1.00 11.82 ? 75  VAL B N   1 
ATOM   2068 C  CA  . VAL B 1 87  ? -11.703 0.308   40.592  1.00 12.23 ? 75  VAL B CA  1 
ATOM   2069 C  C   . VAL B 1 87  ? -10.406 0.040   41.334  1.00 12.50 ? 75  VAL B C   1 
ATOM   2070 O  O   . VAL B 1 87  ? -9.884  -1.075  41.264  1.00 14.52 ? 75  VAL B O   1 
ATOM   2071 C  CB  . VAL B 1 87  ? -12.905 -0.387  41.216  1.00 12.49 ? 75  VAL B CB  1 
ATOM   2072 C  CG1 . VAL B 1 87  ? -13.033 -0.022  42.673  1.00 13.24 ? 75  VAL B CG1 1 
ATOM   2073 C  CG2 . VAL B 1 87  ? -14.175 -0.040  40.452  1.00 12.87 ? 75  VAL B CG2 1 
ATOM   2074 N  N   . TYR B 1 88  ? -9.914  1.049   42.006  1.00 11.87 ? 76  TYR B N   1 
ATOM   2075 C  CA  . TYR B 1 88  ? -8.537  1.030   42.540  1.00 12.08 ? 76  TYR B CA  1 
ATOM   2076 C  C   . TYR B 1 88  ? -8.617  1.499   43.980  1.00 12.42 ? 76  TYR B C   1 
ATOM   2077 O  O   . TYR B 1 88  ? -9.269  2.550   44.250  1.00 13.73 ? 76  TYR B O   1 
ATOM   2078 C  CB  . TYR B 1 88  ? -7.654  1.906   41.660  1.00 13.31 ? 76  TYR B CB  1 
ATOM   2079 C  CG  . TYR B 1 88  ? -6.320  2.269   42.242  1.00 13.92 ? 76  TYR B CG  1 
ATOM   2080 C  CD1 . TYR B 1 88  ? -5.308  1.331   42.261  1.00 15.16 ? 76  TYR B CD1 1 
ATOM   2081 C  CD2 . TYR B 1 88  ? -6.031  3.573   42.637  1.00 13.98 ? 76  TYR B CD2 1 
ATOM   2082 C  CE1 . TYR B 1 88  ? -4.075  1.629   42.839  1.00 15.29 ? 76  TYR B CE1 1 
ATOM   2083 C  CE2 . TYR B 1 88  ? -4.787  3.893   43.171  1.00 14.70 ? 76  TYR B CE2 1 
ATOM   2084 C  CZ  . TYR B 1 88  ? -3.791  2.926   43.237  1.00 14.94 ? 76  TYR B CZ  1 
ATOM   2085 O  OH  . TYR B 1 88  ? -2.522  3.150   43.767  1.00 15.60 ? 76  TYR B OH  1 
ATOM   2086 N  N   . GLY B 1 89  ? -7.826  0.887   44.840  1.00 12.72 ? 77  GLY B N   1 
ATOM   2087 C  CA  . GLY B 1 89  ? -7.929  1.278   46.253  1.00 12.28 ? 77  GLY B CA  1 
ATOM   2088 C  C   . GLY B 1 89  ? -6.815  0.722   47.117  1.00 12.29 ? 77  GLY B C   1 
ATOM   2089 O  O   . GLY B 1 89  ? -5.959  -0.011  46.612  1.00 14.16 ? 77  GLY B O   1 
ATOM   2090 N  N   . TRP B 1 90  ? -6.911  1.040   48.396  1.00 12.51 ? 78  TRP B N   1 
ATOM   2091 C  CA  . TRP B 1 90  ? -5.901  0.655   49.405  1.00 13.60 ? 78  TRP B CA  1 
ATOM   2092 C  C   . TRP B 1 90  ? -6.622  0.160   50.636  1.00 13.65 ? 78  TRP B C   1 
ATOM   2093 O  O   . TRP B 1 90  ? -7.664  0.741   50.972  1.00 14.45 ? 78  TRP B O   1 
ATOM   2094 C  CB  . TRP B 1 90  ? -5.019  1.845   49.728  1.00 14.63 ? 78  TRP B CB  1 
ATOM   2095 C  CG  . TRP B 1 90  ? -4.065  2.174   48.615  1.00 13.43 ? 78  TRP B CG  1 
ATOM   2096 C  CD1 . TRP B 1 90  ? -4.363  2.933   47.533  1.00 14.24 ? 78  TRP B CD1 1 
ATOM   2097 C  CD2 . TRP B 1 90  ? -2.693  1.767   48.466  1.00 14.54 ? 78  TRP B CD2 1 
ATOM   2098 N  NE1 . TRP B 1 90  ? -3.277  3.044   46.716  1.00 15.28 ? 78  TRP B NE1 1 
ATOM   2099 C  CE2 . TRP B 1 90  ? -2.241  2.326   47.246  1.00 14.65 ? 78  TRP B CE2 1 
ATOM   2100 C  CE3 . TRP B 1 90  ? -1.807  0.951   49.179  1.00 14.98 ? 78  TRP B CE3 1 
ATOM   2101 C  CZ2 . TRP B 1 90  ? -0.927  2.211   46.798  1.00 16.22 ? 78  TRP B CZ2 1 
ATOM   2102 C  CZ3 . TRP B 1 90  ? -0.519  0.815   48.727  1.00 15.25 ? 78  TRP B CZ3 1 
ATOM   2103 C  CH2 . TRP B 1 90  ? -0.096  1.390   47.520  1.00 16.06 ? 78  TRP B CH2 1 
ATOM   2104 N  N   . THR B 1 91  ? -5.976  -0.778  51.339  1.00 13.83 ? 79  THR B N   1 
ATOM   2105 C  CA  . THR B 1 91  ? -6.266  -0.999  52.770  1.00 13.56 ? 79  THR B CA  1 
ATOM   2106 C  C   . THR B 1 91  ? -4.999  -0.697  53.546  1.00 12.83 ? 79  THR B C   1 
ATOM   2107 O  O   . THR B 1 91  ? -3.908  -0.680  52.975  1.00 13.91 ? 79  THR B O   1 
ATOM   2108 C  CB  . THR B 1 91  ? -6.796  -2.405  53.064  1.00 14.13 ? 79  THR B CB  1 
ATOM   2109 O  OG1 . THR B 1 91  ? -5.741  -3.357  52.990  1.00 15.71 ? 79  THR B OG1 1 
ATOM   2110 C  CG2 . THR B 1 91  ? -7.932  -2.812  52.158  1.00 14.14 ? 79  THR B CG2 1 
ATOM   2111 N  N   . GLN B 1 92  ? -5.181  -0.560  54.830  1.00 14.06 ? 80  GLN B N   1 
ATOM   2112 C  CA  . GLN B 1 92  ? -4.059  -0.398  55.771  1.00 15.25 ? 80  GLN B CA  1 
ATOM   2113 C  C   . GLN B 1 92  ? -4.121  -1.502  56.821  1.00 14.69 ? 80  GLN B C   1 
ATOM   2114 O  O   . GLN B 1 92  ? -5.193  -1.886  57.236  1.00 15.26 ? 80  GLN B O   1 
ATOM   2115 C  CB  . GLN B 1 92  ? -4.116  0.982   56.412  1.00 16.54 ? 80  GLN B CB  1 
ATOM   2116 C  CG  . GLN B 1 92  ? -3.794  2.123   55.468  1.00 19.45 ? 80  GLN B CG  1 
ATOM   2117 C  CD  . GLN B 1 92  ? -4.373  3.457   55.884  1.00 22.32 ? 80  GLN B CD  1 
ATOM   2118 O  OE1 . GLN B 1 92  ? -5.590  3.669   55.942  1.00 24.04 ? 80  GLN B OE1 1 
ATOM   2119 N  NE2 . GLN B 1 92  ? -3.479  4.376   56.178  1.00 26.43 ? 80  GLN B NE2 1 
ATOM   2120 N  N   . ASN B 1 93  ? -2.957  -1.831  57.363  1.00 15.18 ? 81  ASN B N   1 
ATOM   2121 C  CA  . ASN B 1 93  ? -2.844  -2.756  58.507  1.00 15.56 ? 81  ASN B CA  1 
ATOM   2122 C  C   . ASN B 1 93  ? -3.631  -4.062  58.279  1.00 14.61 ? 81  ASN B C   1 
ATOM   2123 O  O   . ASN B 1 93  ? -4.579  -4.419  59.010  1.00 14.63 ? 81  ASN B O   1 
ATOM   2124 C  CB  . ASN B 1 93  ? -3.258  -2.030  59.777  1.00 15.09 ? 81  ASN B CB  1 
ATOM   2125 C  CG  . ASN B 1 93  ? -2.945  -2.839  61.011  1.00 15.95 ? 81  ASN B CG  1 
ATOM   2126 O  OD1 . ASN B 1 93  ? -2.012  -3.641  60.974  1.00 14.96 ? 81  ASN B OD1 1 
ATOM   2127 N  ND2 . ASN B 1 93  ? -3.739  -2.658  62.076  1.00 17.96 ? 81  ASN B ND2 1 
ATOM   2128 N  N   . PRO B 1 94  ? -3.277  -4.883  57.295  1.00 14.45 ? 82  PRO B N   1 
ATOM   2129 C  CA  . PRO B 1 94  ? -2.106  -4.687  56.433  1.00 15.36 ? 82  PRO B CA  1 
ATOM   2130 C  C   . PRO B 1 94  ? -2.306  -3.763  55.222  1.00 16.57 ? 82  PRO B C   1 
ATOM   2131 O  O   . PRO B 1 94  ? -3.440  -3.623  54.704  1.00 14.96 ? 82  PRO B O   1 
ATOM   2132 C  CB  . PRO B 1 94  ? -1.867  -6.122  55.947  1.00 16.70 ? 82  PRO B CB  1 
ATOM   2133 C  CG  . PRO B 1 94  ? -3.216  -6.688  55.833  1.00 16.91 ? 82  PRO B CG  1 
ATOM   2134 C  CD  . PRO B 1 94  ? -3.839  -6.235  57.126  1.00 15.79 ? 82  PRO B CD  1 
ATOM   2135 N  N   . LEU B 1 95  ? -1.185  -3.198  54.795  1.00 16.06 ? 83  LEU B N   1 
ATOM   2136 C  CA  . LEU B 1 95  ? -1.095  -2.374  53.562  1.00 17.32 ? 83  LEU B CA  1 
ATOM   2137 C  C   . LEU B 1 95  ? -1.280  -3.265  52.332  1.00 15.79 ? 83  LEU B C   1 
ATOM   2138 O  O   . LEU B 1 95  ? -0.446  -4.147  52.081  1.00 15.70 ? 83  LEU B O   1 
ATOM   2139 C  CB  . LEU B 1 95  ? 0.261   -1.667  53.560  1.00 16.54 ? 83  LEU B CB  1 
ATOM   2140 C  CG  . LEU B 1 95  ? 0.420   -0.574  52.512  1.00 17.23 ? 83  LEU B CG  1 
ATOM   2141 C  CD1 . LEU B 1 95  ? -0.552  0.594   52.774  1.00 16.65 ? 83  LEU B CD1 1 
ATOM   2142 C  CD2 . LEU B 1 95  ? 1.865   -0.102  52.516  1.00 18.49 ? 83  LEU B CD2 1 
ATOM   2143 N  N   . VAL B 1 96  ? -2.345  -2.998  51.575  1.00 16.24 ? 84  VAL B N   1 
ATOM   2144 C  CA  . VAL B 1 96  ? -2.724  -3.694  50.329  1.00 14.70 ? 84  VAL B CA  1 
ATOM   2145 C  C   . VAL B 1 96  ? -3.128  -2.645  49.300  1.00 13.75 ? 84  VAL B C   1 
ATOM   2146 O  O   . VAL B 1 96  ? -3.853  -1.698  49.648  1.00 13.85 ? 84  VAL B O   1 
ATOM   2147 C  CB  . VAL B 1 96  ? -3.885  -4.681  50.557  1.00 17.37 ? 84  VAL B CB  1 
ATOM   2148 C  CG1 . VAL B 1 96  ? -4.352  -5.282  49.225  1.00 18.33 ? 84  VAL B CG1 1 
ATOM   2149 C  CG2 . VAL B 1 96  ? -3.562  -5.762  51.600  1.00 16.16 ? 84  VAL B CG2 1 
ATOM   2150 N  N   . GLU B 1 97  ? -2.609  -2.791  48.087  1.00 14.65 ? 85  GLU B N   1 
ATOM   2151 C  CA  . GLU B 1 97  ? -3.036  -2.050  46.885  1.00 14.26 ? 85  GLU B CA  1 
ATOM   2152 C  C   . GLU B 1 97  ? -3.893  -3.009  46.047  1.00 14.25 ? 85  GLU B C   1 
ATOM   2153 O  O   . GLU B 1 97  ? -3.498  -4.219  45.864  1.00 13.49 ? 85  GLU B O   1 
ATOM   2154 C  CB  . GLU B 1 97  ? -1.829  -1.573  46.079  1.00 15.56 ? 85  GLU B CB  1 
ATOM   2155 C  CG  . GLU B 1 97  ? -2.217  -0.726  44.882  1.00 16.11 ? 85  GLU B CG  1 
ATOM   2156 C  CD  . GLU B 1 97  ? -1.097  -0.248  43.988  1.00 16.11 ? 85  GLU B CD  1 
ATOM   2157 O  OE1 . GLU B 1 97  ? -1.120  0.949   43.563  1.00 19.07 ? 85  GLU B OE1 1 
ATOM   2158 O  OE2 . GLU B 1 97  ? -0.208  -1.025  43.736  1.00 19.62 ? 85  GLU B OE2 1 
ATOM   2159 N  N   . TYR B 1 98  ? -5.039  -2.586  45.555  1.00 14.28 ? 86  TYR B N   1 
ATOM   2160 C  CA  . TYR B 1 98  ? -5.890  -3.520  44.783  1.00 15.66 ? 86  TYR B CA  1 
ATOM   2161 C  C   . TYR B 1 98  ? -6.462  -2.839  43.546  1.00 14.70 ? 86  TYR B C   1 
ATOM   2162 O  O   . TYR B 1 98  ? -6.640  -1.586  43.498  1.00 13.73 ? 86  TYR B O   1 
ATOM   2163 C  CB  . TYR B 1 98  ? -6.986  -4.136  45.646  1.00 14.50 ? 86  TYR B CB  1 
ATOM   2164 C  CG  . TYR B 1 98  ? -8.020  -3.152  46.111  1.00 15.59 ? 86  TYR B CG  1 
ATOM   2165 C  CD1 . TYR B 1 98  ? -9.064  -2.774  45.267  1.00 14.71 ? 86  TYR B CD1 1 
ATOM   2166 C  CD2 . TYR B 1 98  ? -7.979  -2.600  47.374  1.00 14.94 ? 86  TYR B CD2 1 
ATOM   2167 C  CE1 . TYR B 1 98  ? -10.000 -1.829  45.668  1.00 16.21 ? 86  TYR B CE1 1 
ATOM   2168 C  CE2 . TYR B 1 98  ? -8.917  -1.676  47.794  1.00 16.89 ? 86  TYR B CE2 1 
ATOM   2169 C  CZ  . TYR B 1 98  ? -9.961  -1.327  46.958  1.00 17.36 ? 86  TYR B CZ  1 
ATOM   2170 O  OH  . TYR B 1 98  ? -10.870 -0.387  47.363  1.00 18.84 ? 86  TYR B OH  1 
ATOM   2171 N  N   . TYR B 1 99  ? -6.687  -3.663  42.536  1.00 15.60 ? 87  TYR B N   1 
ATOM   2172 C  CA  . TYR B 1 99  ? -7.212  -3.234  41.215  1.00 15.12 ? 87  TYR B CA  1 
ATOM   2173 C  C   . TYR B 1 99  ? -8.299  -4.211  40.796  1.00 15.32 ? 87  TYR B C   1 
ATOM   2174 O  O   . TYR B 1 99  ? -8.052  -5.446  40.745  1.00 15.65 ? 87  TYR B O   1 
ATOM   2175 C  CB  . TYR B 1 99  ? -6.135  -3.215  40.126  1.00 16.82 ? 87  TYR B CB  1 
ATOM   2176 C  CG  . TYR B 1 99  ? -5.114  -2.095  40.115  1.00 18.64 ? 87  TYR B CG  1 
ATOM   2177 C  CD1 . TYR B 1 99  ? -5.355  -0.916  39.444  1.00 21.90 ? 87  TYR B CD1 1 
ATOM   2178 C  CD2 . TYR B 1 99  ? -3.882  -2.221  40.752  1.00 21.83 ? 87  TYR B CD2 1 
ATOM   2179 C  CE1 . TYR B 1 99  ? -4.415  0.096   39.351  1.00 26.13 ? 87  TYR B CE1 1 
ATOM   2180 C  CE2 . TYR B 1 99  ? -2.952  -1.197  40.719  1.00 21.08 ? 87  TYR B CE2 1 
ATOM   2181 C  CZ  . TYR B 1 99  ? -3.207  -0.038  40.004  1.00 25.39 ? 87  TYR B CZ  1 
ATOM   2182 O  OH  . TYR B 1 99  ? -2.329  1.003   39.865  1.00 28.56 ? 87  TYR B OH  1 
ATOM   2183 N  N   . ILE B 1 100 ? -9.472  -3.670  40.470  1.00 15.24 ? 88  ILE B N   1 
ATOM   2184 C  CA  . ILE B 1 100 ? -10.529 -4.389  39.720  1.00 14.70 ? 88  ILE B CA  1 
ATOM   2185 C  C   . ILE B 1 100 ? -10.525 -3.841  38.297  1.00 14.50 ? 88  ILE B C   1 
ATOM   2186 O  O   . ILE B 1 100 ? -11.016 -2.700  38.069  1.00 15.52 ? 88  ILE B O   1 
ATOM   2187 C  CB  . ILE B 1 100 ? -11.897 -4.215  40.405  1.00 15.03 ? 88  ILE B CB  1 
ATOM   2188 C  CG1 . ILE B 1 100 ? -11.834 -4.684  41.855  1.00 15.40 ? 88  ILE B CG1 1 
ATOM   2189 C  CG2 . ILE B 1 100 ? -12.991 -4.880  39.570  1.00 16.00 ? 88  ILE B CG2 1 
ATOM   2190 C  CD1 . ILE B 1 100 ? -12.915 -4.150  42.754  1.00 14.25 ? 88  ILE B CD1 1 
ATOM   2191 N  N   . VAL B 1 101 ? -9.874  -4.568  37.398  1.00 12.55 ? 89  VAL B N   1 
ATOM   2192 C  CA  . VAL B 1 101 ? -9.536  -4.049  36.066  1.00 12.79 ? 89  VAL B CA  1 
ATOM   2193 C  C   . VAL B 1 101 ? -10.721 -4.315  35.131  1.00 13.14 ? 89  VAL B C   1 
ATOM   2194 O  O   . VAL B 1 101 ? -11.043 -5.493  34.929  1.00 12.99 ? 89  VAL B O   1 
ATOM   2195 C  CB  . VAL B 1 101 ? -8.232  -4.619  35.544  1.00 12.54 ? 89  VAL B CB  1 
ATOM   2196 C  CG1 . VAL B 1 101 ? -7.977  -4.088  34.144  1.00 12.70 ? 89  VAL B CG1 1 
ATOM   2197 C  CG2 . VAL B 1 101 ? -7.070  -4.367  36.507  1.00 12.27 ? 89  VAL B CG2 1 
ATOM   2198 N  N   . GLU B 1 102 ? -11.330 -3.247  34.646  1.00 12.66 ? 90  GLU B N   1 
ATOM   2199 C  CA  . GLU B 1 102 ? -12.514 -3.300  33.748  1.00 13.16 ? 90  GLU B CA  1 
ATOM   2200 C  C   . GLU B 1 102 ? -12.061 -3.347  32.286  1.00 14.18 ? 90  GLU B C   1 
ATOM   2201 O  O   . GLU B 1 102 ? -12.756 -3.989  31.460  1.00 14.75 ? 90  GLU B O   1 
ATOM   2202 C  CB  . GLU B 1 102 ? -13.435 -2.113  34.009  1.00 15.21 ? 90  GLU B CB  1 
ATOM   2203 C  CG  . GLU B 1 102 ? -14.049 -2.215  35.395  1.00 16.12 ? 90  GLU B CG  1 
ATOM   2204 C  CD  . GLU B 1 102 ? -14.993 -3.395  35.507  1.00 20.09 ? 90  GLU B CD  1 
ATOM   2205 O  OE1 . GLU B 1 102 ? -14.596 -4.376  36.131  1.00 24.61 ? 90  GLU B OE1 1 
ATOM   2206 O  OE2 . GLU B 1 102 ? -16.114 -3.353  34.914  1.00 24.30 ? 90  GLU B OE2 1 
ATOM   2207 N  N   . SER B 1 103 ? -10.973 -2.667  31.958  1.00 15.51 ? 91  SER B N   1 
ATOM   2208 C  CA  . SER B 1 103 ? -10.372 -2.677  30.606  1.00 15.60 ? 91  SER B CA  1 
ATOM   2209 C  C   . SER B 1 103 ? -8.880  -2.517  30.772  1.00 15.17 ? 91  SER B C   1 
ATOM   2210 O  O   . SER B 1 103 ? -8.490  -1.701  31.555  1.00 14.56 ? 91  SER B O   1 
ATOM   2211 C  CB  . SER B 1 103 ? -10.842 -1.579  29.703  1.00 16.21 ? 91  SER B CB  1 
ATOM   2212 O  OG  . SER B 1 103 ? -12.228 -1.680  29.334  1.00 18.45 ? 91  SER B OG  1 
ATOM   2213 N  N   . PHE B 1 104 ? -8.108  -3.145  29.896  1.00 15.63 ? 92  PHE B N   1 
ATOM   2214 C  CA  . PHE B 1 104 ? -6.685  -2.798  29.697  1.00 15.43 ? 92  PHE B CA  1 
ATOM   2215 C  C   . PHE B 1 104 ? -6.433  -2.801  28.206  1.00 15.35 ? 92  PHE B C   1 
ATOM   2216 O  O   . PHE B 1 104 ? -7.254  -3.318  27.442  1.00 15.71 ? 92  PHE B O   1 
ATOM   2217 C  CB  . PHE B 1 104 ? -5.726  -3.720  30.432  1.00 14.28 ? 92  PHE B CB  1 
ATOM   2218 C  CG  . PHE B 1 104 ? -5.694  -5.160  29.969  1.00 14.13 ? 92  PHE B CG  1 
ATOM   2219 C  CD1 . PHE B 1 104 ? -5.053  -5.538  28.788  1.00 13.78 ? 92  PHE B CD1 1 
ATOM   2220 C  CD2 . PHE B 1 104 ? -6.330  -6.113  30.719  1.00 15.36 ? 92  PHE B CD2 1 
ATOM   2221 C  CE1 . PHE B 1 104 ? -5.011  -6.883  28.408  1.00 15.88 ? 92  PHE B CE1 1 
ATOM   2222 C  CE2 . PHE B 1 104 ? -6.271  -7.452  30.351  1.00 15.36 ? 92  PHE B CE2 1 
ATOM   2223 C  CZ  . PHE B 1 104 ? -5.614  -7.827  29.195  1.00 15.77 ? 92  PHE B CZ  1 
ATOM   2224 N  N   . SER B 1 105 ? -5.378  -2.148  27.779  1.00 17.22 ? 93  SER B N   1 
ATOM   2225 C  CA  . SER B 1 105 ? -5.171  -1.911  26.338  1.00 18.34 ? 93  SER B CA  1 
ATOM   2226 C  C   . SER B 1 105 ? -4.175  -2.949  25.817  1.00 23.46 ? 93  SER B C   1 
ATOM   2227 O  O   . SER B 1 105 ? -4.588  -4.099  25.450  1.00 30.95 ? 93  SER B O   1 
ATOM   2228 C  CB  . SER B 1 105 ? -4.803  -0.453  26.125  1.00 20.86 ? 93  SER B CB  1 
ATOM   2229 O  OG  . SER B 1 105 ? -4.587  -0.182  24.759  1.00 26.96 ? 93  SER B OG  1 
ATOM   2230 N  N   . THR B 1 106 ? -2.905  -2.632  25.878  1.00 21.57 ? 94  THR B N   1 
ATOM   2231 C  CA  . THR B 1 106 ? -1.875  -3.381  25.131  1.00 20.27 ? 94  THR B CA  1 
ATOM   2232 C  C   . THR B 1 106 ? -1.033  -4.267  26.049  1.00 19.76 ? 94  THR B C   1 
ATOM   2233 O  O   . THR B 1 106 ? -0.098  -4.923  25.550  1.00 20.95 ? 94  THR B O   1 
ATOM   2234 C  CB  . THR B 1 106 ? -0.987  -2.369  24.403  1.00 20.72 ? 94  THR B CB  1 
ATOM   2235 O  OG1 . THR B 1 106 ? -0.443  -1.431  25.319  1.00 21.39 ? 94  THR B OG1 1 
ATOM   2236 C  CG2 . THR B 1 106 ? -1.739  -1.545  23.396  1.00 18.71 ? 94  THR B CG2 1 
ATOM   2237 N  N   . TYR B 1 107 ? -1.279  -4.231  27.348  1.00 15.78 ? 95  TYR B N   1 
ATOM   2238 C  CA  . TYR B 1 107 ? -0.487  -4.970  28.333  1.00 15.40 ? 95  TYR B CA  1 
ATOM   2239 C  C   . TYR B 1 107 ? -1.404  -5.427  29.458  1.00 16.28 ? 95  TYR B C   1 
ATOM   2240 O  O   . TYR B 1 107 ? -2.060  -4.576  30.029  1.00 17.20 ? 95  TYR B O   1 
ATOM   2241 C  CB  . TYR B 1 107 ? 0.643   -4.120  28.883  1.00 16.49 ? 95  TYR B CB  1 
ATOM   2242 C  CG  . TYR B 1 107 ? 1.554   -4.836  29.840  1.00 17.06 ? 95  TYR B CG  1 
ATOM   2243 C  CD1 . TYR B 1 107 ? 2.505   -5.747  29.407  1.00 17.85 ? 95  TYR B CD1 1 
ATOM   2244 C  CD2 . TYR B 1 107 ? 1.469   -4.615  31.204  1.00 19.36 ? 95  TYR B CD2 1 
ATOM   2245 C  CE1 . TYR B 1 107 ? 3.372   -6.375  30.288  1.00 20.28 ? 95  TYR B CE1 1 
ATOM   2246 C  CE2 . TYR B 1 107 ? 2.305   -5.259  32.099  1.00 19.22 ? 95  TYR B CE2 1 
ATOM   2247 C  CZ  . TYR B 1 107 ? 3.283   -6.116  31.647  1.00 19.18 ? 95  TYR B CZ  1 
ATOM   2248 O  OH  . TYR B 1 107 ? 4.085   -6.722  32.572  1.00 19.08 ? 95  TYR B OH  1 
ATOM   2249 N  N   . ASP B 1 108 ? -1.429  -6.727  29.726  1.00 15.40 ? 96  ASP B N   1 
ATOM   2250 C  CA  . ASP B 1 108 ? -2.214  -7.282  30.857  1.00 15.82 ? 96  ASP B CA  1 
ATOM   2251 C  C   . ASP B 1 108 ? -1.501  -6.917  32.160  1.00 17.28 ? 96  ASP B C   1 
ATOM   2252 O  O   . ASP B 1 108 ? -0.405  -7.415  32.391  1.00 18.62 ? 96  ASP B O   1 
ATOM   2253 C  CB  . ASP B 1 108 ? -2.437  -8.782  30.632  1.00 16.74 ? 96  ASP B CB  1 
ATOM   2254 C  CG  . ASP B 1 108 ? -3.378  -9.373  31.659  1.00 18.22 ? 96  ASP B CG  1 
ATOM   2255 O  OD1 . ASP B 1 108 ? -3.454  -8.794  32.736  1.00 20.00 ? 96  ASP B OD1 1 
ATOM   2256 O  OD2 . ASP B 1 108 ? -3.945  -10.454 31.399  1.00 22.58 ? 96  ASP B OD2 1 
ATOM   2257 N  N   . PRO B 1 109 ? -1.998  -5.953  32.993  1.00 19.47 ? 97  PRO B N   1 
ATOM   2258 C  CA  . PRO B 1 109 ? -1.251  -5.528  34.184  1.00 20.89 ? 97  PRO B CA  1 
ATOM   2259 C  C   . PRO B 1 109 ? -1.045  -6.615  35.250  1.00 20.09 ? 97  PRO B C   1 
ATOM   2260 O  O   . PRO B 1 109 ? -0.225  -6.383  36.162  1.00 19.37 ? 97  PRO B O   1 
ATOM   2261 C  CB  . PRO B 1 109 ? -2.114  -4.395  34.746  1.00 22.51 ? 97  PRO B CB  1 
ATOM   2262 C  CG  . PRO B 1 109 ? -3.513  -4.742  34.309  1.00 20.94 ? 97  PRO B CG  1 
ATOM   2263 C  CD  . PRO B 1 109 ? -3.300  -5.270  32.900  1.00 18.91 ? 97  PRO B CD  1 
ATOM   2264 N  N   . SER B 1 110 ? -1.748  -7.751  35.122  1.00 21.02 ? 98  SER B N   1 
ATOM   2265 C  CA  . SER B 1 110 ? -1.642  -8.975  35.960  1.00 23.21 ? 98  SER B CA  1 
ATOM   2266 C  C   . SER B 1 110 ? -0.384  -9.778  35.596  1.00 23.28 ? 98  SER B C   1 
ATOM   2267 O  O   . SER B 1 110 ? -0.003  -10.653 36.369  1.00 24.65 ? 98  SER B O   1 
ATOM   2268 C  CB  . SER B 1 110 ? -2.896  -9.854  35.858  1.00 21.33 ? 98  SER B CB  1 
ATOM   2269 O  OG  . SER B 1 110 ? -2.909  -10.648 34.684  1.00 22.65 ? 98  SER B OG  1 
ATOM   2270 N  N   . THR B 1 111 ? 0.269   -9.463  34.476  1.00 22.35 ? 99  THR B N   1 
ATOM   2271 C  CA  . THR B 1 111 ? 1.436   -10.230 34.001  1.00 20.10 ? 99  THR B CA  1 
ATOM   2272 C  C   . THR B 1 111 ? 2.460   -10.262 35.143  1.00 19.64 ? 99  THR B C   1 
ATOM   2273 O  O   . THR B 1 111 ? 2.717   -9.190  35.730  1.00 22.05 ? 99  THR B O   1 
ATOM   2274 C  CB  . THR B 1 111 ? 2.038   -9.630  32.731  1.00 18.30 ? 99  THR B CB  1 
ATOM   2275 O  OG1 . THR B 1 111 ? 1.023   -9.571  31.729  1.00 18.97 ? 99  THR B OG1 1 
ATOM   2276 C  CG2 . THR B 1 111 ? 3.222   -10.427 32.234  1.00 19.38 ? 99  THR B CG2 1 
ATOM   2277 N  N   . GLY B 1 112 ? 2.954   -11.448 35.481  1.00 19.78 ? 100 GLY B N   1 
ATOM   2278 C  CA  . GLY B 1 112 ? 3.973   -11.613 36.533  1.00 20.58 ? 100 GLY B CA  1 
ATOM   2279 C  C   . GLY B 1 112 ? 3.349   -11.808 37.903  1.00 20.29 ? 100 GLY B C   1 
ATOM   2280 O  O   . GLY B 1 112 ? 4.109   -12.088 38.856  1.00 23.47 ? 100 GLY B O   1 
ATOM   2281 N  N   . ALA B 1 113 ? 2.025   -11.738 38.022  1.00 17.60 ? 101 ALA B N   1 
ATOM   2282 C  CA  . ALA B 1 113 ? 1.322   -12.042 39.292  1.00 17.87 ? 101 ALA B CA  1 
ATOM   2283 C  C   . ALA B 1 113 ? 0.899   -13.522 39.285  1.00 20.43 ? 101 ALA B C   1 
ATOM   2284 O  O   . ALA B 1 113 ? 0.789   -14.143 38.200  1.00 25.63 ? 101 ALA B O   1 
ATOM   2285 C  CB  . ALA B 1 113 ? 0.135   -11.150 39.501  1.00 19.19 ? 101 ALA B CB  1 
ATOM   2286 N  N   . GLN B 1 114 ? 0.617   -14.054 40.464  1.00 21.16 ? 102 GLN B N   1 
ATOM   2287 C  CA  . GLN B 1 114 ? 0.264   -15.471 40.667  1.00 23.10 ? 102 GLN B CA  1 
ATOM   2288 C  C   . GLN B 1 114 ? -1.270  -15.606 40.587  1.00 24.22 ? 102 GLN B C   1 
ATOM   2289 O  O   . GLN B 1 114 ? -2.001  -14.888 41.317  1.00 21.29 ? 102 GLN B O   1 
ATOM   2290 C  CB  . GLN B 1 114 ? 0.908   -15.963 41.963  1.00 26.36 ? 102 GLN B CB  1 
ATOM   2291 C  CG  . GLN B 1 114 ? 2.437   -15.775 42.058  1.00 31.07 ? 102 GLN B CG  1 
ATOM   2292 C  CD  . GLN B 1 114 ? 3.240   -15.414 40.823  1.00 37.38 ? 102 GLN B CD  1 
ATOM   2293 O  OE1 . GLN B 1 114 ? 3.016   -14.393 40.180  1.00 48.63 ? 102 GLN B OE1 1 
ATOM   2294 N  NE2 . GLN B 1 114 ? 4.260   -16.198 40.514  1.00 41.58 ? 102 GLN B NE2 1 
ATOM   2295 N  N   . GLU B 1 115 ? -1.746  -16.460 39.676  1.00 22.17 ? 103 GLU B N   1 
ATOM   2296 C  CA  . GLU B 1 115 ? -3.191  -16.622 39.403  1.00 24.72 ? 103 GLU B CA  1 
ATOM   2297 C  C   . GLU B 1 115 ? -3.741  -17.534 40.493  1.00 25.79 ? 103 GLU B C   1 
ATOM   2298 O  O   . GLU B 1 115 ? -3.041  -18.513 40.823  1.00 26.94 ? 103 GLU B O   1 
ATOM   2299 C  CB  . GLU B 1 115 ? -3.412  -17.132 37.981  1.00 24.35 ? 103 GLU B CB  1 
ATOM   2300 C  CG  . GLU B 1 115 ? -4.855  -17.040 37.539  1.00 25.64 ? 103 GLU B CG  1 
ATOM   2301 C  CD  . GLU B 1 115 ? -5.101  -17.391 36.081  1.00 28.51 ? 103 GLU B CD  1 
ATOM   2302 O  OE1 . GLU B 1 115 ? -6.277  -17.481 35.694  1.00 34.98 ? 103 GLU B OE1 1 
ATOM   2303 O  OE2 . GLU B 1 115 ? -4.127  -17.619 35.349  1.00 35.43 ? 103 GLU B OE2 1 
ATOM   2304 N  N   . LEU B 1 116 ? -4.930  -17.210 41.019  1.00 26.23 ? 104 LEU B N   1 
ATOM   2305 C  CA  . LEU B 1 116 ? -5.530  -17.808 42.244  1.00 28.85 ? 104 LEU B CA  1 
ATOM   2306 C  C   . LEU B 1 116 ? -6.870  -18.466 41.932  1.00 31.39 ? 104 LEU B C   1 
ATOM   2307 O  O   . LEU B 1 116 ? -7.258  -19.363 42.700  1.00 36.79 ? 104 LEU B O   1 
ATOM   2308 C  CB  . LEU B 1 116 ? -5.780  -16.708 43.285  1.00 33.23 ? 104 LEU B CB  1 
ATOM   2309 C  CG  . LEU B 1 116 ? -4.632  -16.342 44.218  1.00 34.03 ? 104 LEU B CG  1 
ATOM   2310 C  CD1 . LEU B 1 116 ? -4.387  -14.855 44.172  1.00 31.52 ? 104 LEU B CD1 1 
ATOM   2311 C  CD2 . LEU B 1 116 ? -4.939  -16.762 45.653  1.00 36.10 ? 104 LEU B CD2 1 
ATOM   2312 N  N   . GLY B 1 117 ? -7.571  -18.016 40.891  1.00 26.32 ? 105 GLY B N   1 
ATOM   2313 C  CA  . GLY B 1 117 ? -8.942  -18.455 40.571  1.00 26.40 ? 105 GLY B CA  1 
ATOM   2314 C  C   . GLY B 1 117 ? -9.738  -17.347 39.893  1.00 24.43 ? 105 GLY B C   1 
ATOM   2315 O  O   . GLY B 1 117 ? -9.132  -16.499 39.228  1.00 24.18 ? 105 GLY B O   1 
ATOM   2316 N  N   . THR B 1 118 ? -11.067 -17.378 40.020  1.00 24.26 ? 106 THR B N   1 
ATOM   2317 C  CA  . THR B 1 118 ? -11.995 -16.517 39.237  1.00 24.24 ? 106 THR B CA  1 
ATOM   2318 C  C   . THR B 1 118 ? -13.174 -16.095 40.115  1.00 24.81 ? 106 THR B C   1 
ATOM   2319 O  O   . THR B 1 118 ? -13.461 -16.755 41.140  1.00 25.29 ? 106 THR B O   1 
ATOM   2320 C  CB  . THR B 1 118 ? -12.513 -17.192 37.951  1.00 27.87 ? 106 THR B CB  1 
ATOM   2321 O  OG1 . THR B 1 118 ? -13.349 -18.302 38.278  1.00 25.26 ? 106 THR B OG1 1 
ATOM   2322 C  CG2 . THR B 1 118 ? -11.414 -17.703 37.049  1.00 26.65 ? 106 THR B CG2 1 
ATOM   2323 N  N   . VAL B 1 119 ? -13.824 -15.004 39.739  1.00 22.76 ? 107 VAL B N   1 
ATOM   2324 C  CA  . VAL B 1 119 ? -15.105 -14.581 40.356  1.00 23.37 ? 107 VAL B CA  1 
ATOM   2325 C  C   . VAL B 1 119 ? -16.043 -14.127 39.232  1.00 22.62 ? 107 VAL B C   1 
ATOM   2326 O  O   . VAL B 1 119 ? -15.571 -13.480 38.272  1.00 23.16 ? 107 VAL B O   1 
ATOM   2327 C  CB  . VAL B 1 119 ? -14.864 -13.502 41.432  1.00 22.87 ? 107 VAL B CB  1 
ATOM   2328 C  CG1 . VAL B 1 119 ? -14.045 -12.321 40.930  1.00 20.59 ? 107 VAL B CG1 1 
ATOM   2329 C  CG2 . VAL B 1 119 ? -16.161 -13.044 42.088  1.00 23.71 ? 107 VAL B CG2 1 
ATOM   2330 N  N   . GLU B 1 120 ? -17.301 -14.542 39.317  1.00 23.38 ? 108 GLU B N   1 
ATOM   2331 C  CA  . GLU B 1 120 ? -18.369 -14.132 38.370  1.00 24.27 ? 108 GLU B CA  1 
ATOM   2332 C  C   . GLU B 1 120 ? -19.161 -13.016 39.031  1.00 21.17 ? 108 GLU B C   1 
ATOM   2333 O  O   . GLU B 1 120 ? -19.693 -13.249 40.125  1.00 20.61 ? 108 GLU B O   1 
ATOM   2334 C  CB  . GLU B 1 120 ? -19.308 -15.296 38.050  1.00 27.11 ? 108 GLU B CB  1 
ATOM   2335 C  CG  . GLU B 1 120 ? -18.593 -16.548 37.605  1.00 31.72 ? 108 GLU B CG  1 
ATOM   2336 C  CD  . GLU B 1 120 ? -17.652 -16.364 36.432  1.00 37.20 ? 108 GLU B CD  1 
ATOM   2337 O  OE1 . GLU B 1 120 ? -16.622 -17.091 36.377  1.00 49.64 ? 108 GLU B OE1 1 
ATOM   2338 O  OE2 . GLU B 1 120 ? -17.937 -15.504 35.578  1.00 46.09 ? 108 GLU B OE2 1 
ATOM   2339 N  N   . THR B 1 121 ? -19.217 -11.837 38.421  1.00 20.60 ? 109 THR B N   1 
ATOM   2340 C  CA  . THR B 1 121 ? -19.906 -10.669 39.000  1.00 20.37 ? 109 THR B CA  1 
ATOM   2341 C  C   . THR B 1 121 ? -20.155 -9.644  37.901  1.00 18.53 ? 109 THR B C   1 
ATOM   2342 O  O   . THR B 1 121 ? -19.342 -9.570  36.938  1.00 16.76 ? 109 THR B O   1 
ATOM   2343 C  CB  . THR B 1 121 ? -19.153 -10.114 40.223  1.00 22.62 ? 109 THR B CB  1 
ATOM   2344 O  OG1 . THR B 1 121 ? -19.855 -8.997  40.769  1.00 24.36 ? 109 THR B OG1 1 
ATOM   2345 C  CG2 . THR B 1 121 ? -17.739 -9.701  39.893  1.00 20.05 ? 109 THR B CG2 1 
ATOM   2346 N  N   . ASP B 1 122 ? -21.302 -8.969  37.984  1.00 19.44 ? 110 ASP B N   1 
ATOM   2347 C  CA  . ASP B 1 122 ? -21.632 -7.811  37.108  1.00 18.71 ? 110 ASP B CA  1 
ATOM   2348 C  C   . ASP B 1 122 ? -21.537 -8.285  35.642  1.00 19.94 ? 110 ASP B C   1 
ATOM   2349 O  O   . ASP B 1 122 ? -20.841 -7.650  34.834  1.00 18.76 ? 110 ASP B O   1 
ATOM   2350 C  CB  . ASP B 1 122 ? -20.764 -6.591  37.490  1.00 18.52 ? 110 ASP B CB  1 
ATOM   2351 C  CG  . ASP B 1 122 ? -20.803 -6.277  38.978  1.00 16.40 ? 110 ASP B CG  1 
ATOM   2352 O  OD1 . ASP B 1 122 ? -21.907 -6.017  39.464  1.00 18.61 ? 110 ASP B OD1 1 
ATOM   2353 O  OD2 . ASP B 1 122 ? -19.732 -6.332  39.661  1.00 17.72 ? 110 ASP B OD2 1 
ATOM   2354 N  N   . ASP B 1 123 ? -22.123 -9.450  35.351  1.00 21.81 ? 111 ASP B N   1 
ATOM   2355 C  CA  . ASP B 1 123 ? -22.267 -9.958  33.972  1.00 23.45 ? 111 ASP B CA  1 
ATOM   2356 C  C   . ASP B 1 123 ? -20.892 -10.221 33.348  1.00 22.87 ? 111 ASP B C   1 
ATOM   2357 O  O   . ASP B 1 123 ? -20.826 -10.323 32.089  1.00 25.02 ? 111 ASP B O   1 
ATOM   2358 C  CB  . ASP B 1 123 ? -23.094 -8.987  33.124  1.00 27.86 ? 111 ASP B CB  1 
ATOM   2359 C  CG  . ASP B 1 123 ? -23.698 -9.610  31.876  1.00 36.28 ? 111 ASP B CG  1 
ATOM   2360 O  OD1 . ASP B 1 123 ? -23.873 -10.875 31.848  1.00 40.71 ? 111 ASP B OD1 1 
ATOM   2361 O  OD2 . ASP B 1 123 ? -23.976 -8.844  30.925  1.00 38.11 ? 111 ASP B OD2 1 
ATOM   2362 N  N   . GLY B 1 124 ? -19.847 -10.390 34.167  1.00 21.70 ? 112 GLY B N   1 
ATOM   2363 C  CA  . GLY B 1 124 ? -18.496 -10.731 33.680  1.00 25.57 ? 112 GLY B CA  1 
ATOM   2364 C  C   . GLY B 1 124 ? -17.830 -11.843 34.470  1.00 21.84 ? 112 GLY B C   1 
ATOM   2365 O  O   . GLY B 1 124 ? -18.359 -12.315 35.493  1.00 23.06 ? 112 GLY B O   1 
ATOM   2366 N  N   . THR B 1 125 ? -16.671 -12.248 33.976  1.00 19.79 ? 113 THR B N   1 
ATOM   2367 C  CA  . THR B 1 125 ? -15.749 -13.176 34.632  1.00 20.12 ? 113 THR B CA  1 
ATOM   2368 C  C   . THR B 1 125 ? -14.441 -12.422 34.853  1.00 18.71 ? 113 THR B C   1 
ATOM   2369 O  O   . THR B 1 125 ? -13.983 -11.738 33.927  1.00 19.24 ? 113 THR B O   1 
ATOM   2370 C  CB  . THR B 1 125 ? -15.590 -14.455 33.800  1.00 21.80 ? 113 THR B CB  1 
ATOM   2371 O  OG1 . THR B 1 125 ? -16.902 -14.998 33.611  1.00 22.96 ? 113 THR B OG1 1 
ATOM   2372 C  CG2 . THR B 1 125 ? -14.633 -15.403 34.460  1.00 24.71 ? 113 THR B CG2 1 
ATOM   2373 N  N   . TYR B 1 126 ? -13.904 -12.555 36.057  1.00 18.02 ? 114 TYR B N   1 
ATOM   2374 C  CA  . TYR B 1 126 ? -12.632 -11.922 36.461  1.00 18.47 ? 114 TYR B CA  1 
ATOM   2375 C  C   . TYR B 1 126 ? -11.683 -13.013 36.927  1.00 17.81 ? 114 TYR B C   1 
ATOM   2376 O  O   . TYR B 1 126 ? -12.041 -13.886 37.720  1.00 19.42 ? 114 TYR B O   1 
ATOM   2377 C  CB  . TYR B 1 126 ? -12.818 -10.900 37.592  1.00 17.50 ? 114 TYR B CB  1 
ATOM   2378 C  CG  . TYR B 1 126 ? -13.671 -9.710  37.258  1.00 17.34 ? 114 TYR B CG  1 
ATOM   2379 C  CD1 . TYR B 1 126 ? -15.053 -9.830  37.103  1.00 17.06 ? 114 TYR B CD1 1 
ATOM   2380 C  CD2 . TYR B 1 126 ? -13.109 -8.451  37.066  1.00 16.22 ? 114 TYR B CD2 1 
ATOM   2381 C  CE1 . TYR B 1 126 ? -15.835 -8.726  36.789  1.00 16.74 ? 114 TYR B CE1 1 
ATOM   2382 C  CE2 . TYR B 1 126 ? -13.882 -7.338  36.778  1.00 15.18 ? 114 TYR B CE2 1 
ATOM   2383 C  CZ  . TYR B 1 126 ? -15.258 -7.489  36.613  1.00 14.43 ? 114 TYR B CZ  1 
ATOM   2384 O  OH  . TYR B 1 126 ? -16.036 -6.412  36.310  1.00 16.66 ? 114 TYR B OH  1 
ATOM   2385 N  N   . LYS B 1 127 ? -10.462 -12.940 36.442  1.00 16.52 ? 115 LYS B N   1 
ATOM   2386 C  CA  . LYS B 1 127 ? -9.322  -13.738 36.917  1.00 16.89 ? 115 LYS B CA  1 
ATOM   2387 C  C   . LYS B 1 127 ? -8.721  -13.026 38.116  1.00 17.22 ? 115 LYS B C   1 
ATOM   2388 O  O   . LYS B 1 127 ? -8.513  -11.792 38.022  1.00 18.48 ? 115 LYS B O   1 
ATOM   2389 C  CB  . LYS B 1 127 ? -8.298  -13.945 35.782  1.00 18.13 ? 115 LYS B CB  1 
ATOM   2390 C  CG  . LYS B 1 127 ? -8.754  -15.004 34.775  1.00 22.02 ? 115 LYS B CG  1 
ATOM   2391 C  CD  . LYS B 1 127 ? -7.933  -15.112 33.532  1.00 25.63 ? 115 LYS B CD  1 
ATOM   2392 C  CE  . LYS B 1 127 ? -8.362  -16.287 32.672  1.00 27.96 ? 115 LYS B CE  1 
ATOM   2393 N  NZ  . LYS B 1 127 ? -7.410  -16.521 31.565  1.00 28.87 ? 115 LYS B NZ  1 
ATOM   2394 N  N   . ILE B 1 128 ? -8.427  -13.781 39.170  1.00 16.95 ? 116 ILE B N   1 
ATOM   2395 C  CA  . ILE B 1 128 ? -7.853  -13.251 40.426  1.00 17.49 ? 116 ILE B CA  1 
ATOM   2396 C  C   . ILE B 1 128 ? -6.360  -13.533 40.491  1.00 17.04 ? 116 ILE B C   1 
ATOM   2397 O  O   . ILE B 1 128 ? -5.968  -14.667 40.256  1.00 17.67 ? 116 ILE B O   1 
ATOM   2398 C  CB  . ILE B 1 128 ? -8.580  -13.865 41.631  1.00 18.43 ? 116 ILE B CB  1 
ATOM   2399 C  CG1 . ILE B 1 128 ? -10.039 -13.431 41.646  1.00 21.42 ? 116 ILE B CG1 1 
ATOM   2400 C  CG2 . ILE B 1 128 ? -7.868  -13.523 42.920  1.00 21.52 ? 116 ILE B CG2 1 
ATOM   2401 C  CD1 . ILE B 1 128 ? -10.890 -14.274 42.587  1.00 23.42 ? 116 ILE B CD1 1 
ATOM   2402 N  N   . TYR B 1 129 ? -5.571  -12.529 40.898  1.00 15.13 ? 117 TYR B N   1 
ATOM   2403 C  CA  . TYR B 1 129 ? -4.107  -12.677 41.053  1.00 15.82 ? 117 TYR B CA  1 
ATOM   2404 C  C   . TYR B 1 129 ? -3.626  -11.999 42.322  1.00 16.77 ? 117 TYR B C   1 
ATOM   2405 O  O   . TYR B 1 129 ? -4.254  -11.040 42.793  1.00 15.89 ? 117 TYR B O   1 
ATOM   2406 C  CB  . TYR B 1 129 ? -3.339  -12.067 39.886  1.00 16.07 ? 117 TYR B CB  1 
ATOM   2407 C  CG  . TYR B 1 129 ? -3.766  -12.495 38.513  1.00 17.65 ? 117 TYR B CG  1 
ATOM   2408 C  CD1 . TYR B 1 129 ? -4.922  -11.980 37.946  1.00 16.64 ? 117 TYR B CD1 1 
ATOM   2409 C  CD2 . TYR B 1 129 ? -3.010  -13.400 37.769  1.00 19.08 ? 117 TYR B CD2 1 
ATOM   2410 C  CE1 . TYR B 1 129 ? -5.332  -12.362 36.683  1.00 18.60 ? 117 TYR B CE1 1 
ATOM   2411 C  CE2 . TYR B 1 129 ? -3.394  -13.752 36.482  1.00 19.00 ? 117 TYR B CE2 1 
ATOM   2412 C  CZ  . TYR B 1 129 ? -4.573  -13.259 35.957  1.00 17.76 ? 117 TYR B CZ  1 
ATOM   2413 O  OH  . TYR B 1 129 ? -4.981  -13.574 34.697  1.00 19.17 ? 117 TYR B OH  1 
ATOM   2414 N  N   . GLN B 1 130 ? -2.453  -12.420 42.801  1.00 17.97 ? 118 GLN B N   1 
ATOM   2415 C  CA  . GLN B 1 130 ? -1.765  -11.710 43.882  1.00 19.58 ? 118 GLN B CA  1 
ATOM   2416 C  C   . GLN B 1 130 ? -0.297  -11.582 43.515  1.00 20.48 ? 118 GLN B C   1 
ATOM   2417 O  O   . GLN B 1 130 ? 0.248   -12.485 42.871  1.00 18.85 ? 118 GLN B O   1 
ATOM   2418 C  CB  . GLN B 1 130 ? -1.967  -12.342 45.267  1.00 19.98 ? 118 GLN B CB  1 
ATOM   2419 C  CG  . GLN B 1 130 ? -1.325  -13.710 45.463  1.00 25.57 ? 118 GLN B CG  1 
ATOM   2420 C  CD  . GLN B 1 130 ? -1.303  -14.064 46.940  1.00 27.20 ? 118 GLN B CD  1 
ATOM   2421 O  OE1 . GLN B 1 130 ? -1.498  -15.212 47.330  1.00 32.07 ? 118 GLN B OE1 1 
ATOM   2422 N  NE2 . GLN B 1 130 ? -1.095  -13.067 47.789  1.00 26.77 ? 118 GLN B NE2 1 
ATOM   2423 N  N   . THR B 1 131 ? 0.282   -10.431 43.854  1.00 18.78 ? 119 THR B N   1 
ATOM   2424 C  CA  . THR B 1 131 ? 1.746   -10.254 43.818  1.00 20.17 ? 119 THR B CA  1 
ATOM   2425 C  C   . THR B 1 131 ? 2.189   -9.335  44.954  1.00 18.73 ? 119 THR B C   1 
ATOM   2426 O  O   . THR B 1 131 ? 1.384   -9.023  45.867  1.00 18.40 ? 119 THR B O   1 
ATOM   2427 C  CB  . THR B 1 131 ? 2.197   -9.794  42.432  1.00 20.28 ? 119 THR B CB  1 
ATOM   2428 O  OG1 . THR B 1 131 ? 3.636   -9.837  42.435  1.00 24.02 ? 119 THR B OG1 1 
ATOM   2429 C  CG2 . THR B 1 131 ? 1.689   -8.405  42.097  1.00 22.19 ? 119 THR B CG2 1 
ATOM   2430 N  N   . THR B 1 132 ? 3.482   -9.071  45.004  1.00 21.44 ? 120 THR B N   1 
ATOM   2431 C  CA  . THR B 1 132 ? 4.055   -8.142  46.005  1.00 24.71 ? 120 THR B CA  1 
ATOM   2432 C  C   . THR B 1 132 ? 4.732   -6.989  45.263  1.00 25.45 ? 120 THR B C   1 
ATOM   2433 O  O   . THR B 1 132 ? 5.266   -7.242  44.135  1.00 25.48 ? 120 THR B O   1 
ATOM   2434 C  CB  . THR B 1 132 ? 5.022   -8.876  46.932  1.00 27.30 ? 120 THR B CB  1 
ATOM   2435 O  OG1 . THR B 1 132 ? 6.052   -9.390  46.086  1.00 32.06 ? 120 THR B OG1 1 
ATOM   2436 C  CG2 . THR B 1 132 ? 4.363   -9.989  47.709  1.00 27.48 ? 120 THR B CG2 1 
ATOM   2437 N  N   . ARG B 1 133 ? 4.698   -5.795  45.867  1.00 20.35 ? 121 ARG B N   1 
ATOM   2438 C  CA  . ARG B 1 133 ? 5.474   -4.597  45.458  1.00 20.55 ? 121 ARG B CA  1 
ATOM   2439 C  C   . ARG B 1 133 ? 6.507   -4.290  46.553  1.00 19.96 ? 121 ARG B C   1 
ATOM   2440 O  O   . ARG B 1 133 ? 6.141   -4.321  47.726  1.00 18.28 ? 121 ARG B O   1 
ATOM   2441 C  CB  . ARG B 1 133 ? 4.585   -3.373  45.233  1.00 21.59 ? 121 ARG B CB  1 
ATOM   2442 C  CG  . ARG B 1 133 ? 3.594   -3.552  44.088  1.00 23.73 ? 121 ARG B CG  1 
ATOM   2443 C  CD  . ARG B 1 133 ? 4.187   -3.211  42.736  1.00 23.32 ? 121 ARG B CD  1 
ATOM   2444 N  NE  . ARG B 1 133 ? 4.304   -1.769  42.613  1.00 24.41 ? 121 ARG B NE  1 
ATOM   2445 C  CZ  . ARG B 1 133 ? 5.397   -1.091  42.276  1.00 24.41 ? 121 ARG B CZ  1 
ATOM   2446 N  NH1 . ARG B 1 133 ? 6.524   -1.707  41.960  1.00 25.05 ? 121 ARG B NH1 1 
ATOM   2447 N  NH2 . ARG B 1 133 ? 5.355   0.226   42.265  1.00 25.69 ? 121 ARG B NH2 1 
ATOM   2448 N  N   . GLU B 1 134 ? 7.773   -4.173  46.162  1.00 20.86 ? 122 GLU B N   1 
ATOM   2449 C  CA  . GLU B 1 134 ? 8.914   -4.024  47.093  1.00 22.42 ? 122 GLU B CA  1 
ATOM   2450 C  C   . GLU B 1 134 ? 9.429   -2.587  47.002  1.00 22.17 ? 122 GLU B C   1 
ATOM   2451 O  O   . GLU B 1 134 ? 9.617   -2.086  45.869  1.00 23.25 ? 122 GLU B O   1 
ATOM   2452 C  CB  . GLU B 1 134 ? 10.018  -5.023  46.750  1.00 27.89 ? 122 GLU B CB  1 
ATOM   2453 C  CG  . GLU B 1 134 ? 9.630   -6.466  47.039  1.00 33.70 ? 122 GLU B CG  1 
ATOM   2454 C  CD  . GLU B 1 134 ? 10.771  -7.468  46.986  1.00 43.16 ? 122 GLU B CD  1 
ATOM   2455 O  OE1 . GLU B 1 134 ? 10.484  -8.688  47.013  1.00 49.10 ? 122 GLU B OE1 1 
ATOM   2456 O  OE2 . GLU B 1 134 ? 11.942  -7.032  46.918  1.00 48.82 ? 122 GLU B OE2 1 
ATOM   2457 N  N   . ASN B 1 135 ? 9.641   -1.947  48.151  1.00 22.85 ? 123 ASN B N   1 
ATOM   2458 C  CA  . ASN B 1 135 ? 10.280  -0.599  48.230  1.00 24.38 ? 123 ASN B CA  1 
ATOM   2459 C  C   . ASN B 1 135 ? 9.626   0.320   47.179  1.00 24.96 ? 123 ASN B C   1 
ATOM   2460 O  O   . ASN B 1 135 ? 10.324  0.935   46.354  1.00 22.34 ? 123 ASN B O   1 
ATOM   2461 C  CB  . ASN B 1 135 ? 11.801  -0.734  48.062  1.00 27.59 ? 123 ASN B CB  1 
ATOM   2462 C  CG  . ASN B 1 135 ? 12.386  -1.795  48.973  1.00 30.97 ? 123 ASN B CG  1 
ATOM   2463 O  OD1 . ASN B 1 135 ? 12.345  -1.654  50.203  1.00 32.74 ? 123 ASN B OD1 1 
ATOM   2464 N  ND2 . ASN B 1 135 ? 12.928  -2.856  48.385  1.00 29.38 ? 123 ASN B ND2 1 
ATOM   2465 N  N   . ALA B 1 136 ? 8.301   0.389   47.189  1.00 21.48 ? 124 ALA B N   1 
ATOM   2466 C  CA  . ALA B 1 136 ? 7.499   1.016   46.118  1.00 20.12 ? 124 ALA B CA  1 
ATOM   2467 C  C   . ALA B 1 136 ? 6.723   2.178   46.712  1.00 21.52 ? 124 ALA B C   1 
ATOM   2468 O  O   . ALA B 1 136 ? 6.417   2.183   47.915  1.00 19.35 ? 124 ALA B O   1 
ATOM   2469 C  CB  . ALA B 1 136 ? 6.554   0.000   45.520  1.00 20.27 ? 124 ALA B CB  1 
ATOM   2470 N  N   . PRO B 1 137 ? 6.259   3.132   45.880  1.00 21.05 ? 125 PRO B N   1 
ATOM   2471 C  CA  . PRO B 1 137 ? 5.424   4.207   46.379  1.00 20.72 ? 125 PRO B CA  1 
ATOM   2472 C  C   . PRO B 1 137 ? 4.128   3.615   46.938  1.00 19.24 ? 125 PRO B C   1 
ATOM   2473 O  O   . PRO B 1 137 ? 3.637   2.659   46.406  1.00 17.92 ? 125 PRO B O   1 
ATOM   2474 C  CB  . PRO B 1 137 ? 5.150   5.093   45.159  1.00 22.37 ? 125 PRO B CB  1 
ATOM   2475 C  CG  . PRO B 1 137 ? 6.246   4.721   44.177  1.00 23.21 ? 125 PRO B CG  1 
ATOM   2476 C  CD  . PRO B 1 137 ? 6.501   3.252   44.428  1.00 22.96 ? 125 PRO B CD  1 
ATOM   2477 N  N   . SER B 1 138 ? 3.625   4.221   47.998  1.00 19.21 ? 126 SER B N   1 
ATOM   2478 C  CA  . SER B 1 138 ? 2.371   3.782   48.645  1.00 18.99 ? 126 SER B CA  1 
ATOM   2479 C  C   . SER B 1 138 ? 1.722   4.955   49.350  1.00 17.86 ? 126 SER B C   1 
ATOM   2480 O  O   . SER B 1 138 ? 2.346   6.018   49.516  1.00 16.99 ? 126 SER B O   1 
ATOM   2481 C  CB  . SER B 1 138 ? 2.650   2.617   49.578  1.00 20.77 ? 126 SER B CB  1 
ATOM   2482 O  OG  . SER B 1 138 ? 3.024   3.077   50.877  1.00 18.30 ? 126 SER B OG  1 
ATOM   2483 N  N   . ILE B 1 139 ? 0.505   4.749   49.838  1.00 16.61 ? 127 ILE B N   1 
ATOM   2484 C  CA  . ILE B 1 139 ? -0.178  5.752   50.691  1.00 19.15 ? 127 ILE B CA  1 
ATOM   2485 C  C   . ILE B 1 139 ? 0.569   5.925   52.031  1.00 19.65 ? 127 ILE B C   1 
ATOM   2486 O  O   . ILE B 1 139 ? 0.220   6.849   52.738  1.00 20.78 ? 127 ILE B O   1 
ATOM   2487 C  CB  . ILE B 1 139 ? -1.653  5.400   50.917  1.00 20.08 ? 127 ILE B CB  1 
ATOM   2488 C  CG1 . ILE B 1 139 ? -1.854  3.992   51.485  1.00 19.31 ? 127 ILE B CG1 1 
ATOM   2489 C  CG2 . ILE B 1 139 ? -2.434  5.630   49.637  1.00 20.35 ? 127 ILE B CG2 1 
ATOM   2490 C  CD1 . ILE B 1 139 ? -3.195  3.821   52.184  1.00 21.04 ? 127 ILE B CD1 1 
ATOM   2491 N  N   . GLU B 1 140 ? 1.530   5.070   52.363  1.00 20.07 ? 128 GLU B N   1 
ATOM   2492 C  CA  . GLU B 1 140 ? 2.332   5.226   53.616  1.00 20.42 ? 128 GLU B CA  1 
ATOM   2493 C  C   . GLU B 1 140 ? 3.781   5.617   53.319  1.00 21.28 ? 128 GLU B C   1 
ATOM   2494 O  O   . GLU B 1 140 ? 4.602   5.557   54.277  1.00 23.94 ? 128 GLU B O   1 
ATOM   2495 C  CB  . GLU B 1 140 ? 2.299   3.921   54.409  1.00 22.58 ? 128 GLU B CB  1 
ATOM   2496 C  CG  . GLU B 1 140 ? 0.915   3.596   54.926  1.00 23.25 ? 128 GLU B CG  1 
ATOM   2497 C  CD  . GLU B 1 140 ? 0.299   4.621   55.861  1.00 27.45 ? 128 GLU B CD  1 
ATOM   2498 O  OE1 . GLU B 1 140 ? -0.725  4.312   56.464  1.00 28.09 ? 128 GLU B OE1 1 
ATOM   2499 O  OE2 . GLU B 1 140 ? 0.868   5.734   56.019  1.00 30.52 ? 128 GLU B OE2 1 
ATOM   2500 N  N   . GLY B 1 141 ? 4.087   6.023   52.079  1.00 19.81 ? 129 GLY B N   1 
ATOM   2501 C  CA  . GLY B 1 141 ? 5.456   6.243   51.572  1.00 19.82 ? 129 GLY B CA  1 
ATOM   2502 C  C   . GLY B 1 141 ? 6.078   4.965   51.043  1.00 20.41 ? 129 GLY B C   1 
ATOM   2503 O  O   . GLY B 1 141 ? 5.369   3.983   50.783  1.00 21.89 ? 129 GLY B O   1 
ATOM   2504 N  N   . THR B 1 142 ? 7.400   4.959   50.888  1.00 19.57 ? 130 THR B N   1 
ATOM   2505 C  CA  . THR B 1 142 ? 8.123   3.823   50.318  1.00 17.64 ? 130 THR B CA  1 
ATOM   2506 C  C   . THR B 1 142 ? 7.842   2.596   51.188  1.00 19.60 ? 130 THR B C   1 
ATOM   2507 O  O   . THR B 1 142 ? 8.083   2.654   52.399  1.00 17.58 ? 130 THR B O   1 
ATOM   2508 C  CB  . THR B 1 142 ? 9.629   4.095   50.195  1.00 18.38 ? 130 THR B CB  1 
ATOM   2509 O  OG1 . THR B 1 142 ? 9.760   5.291   49.435  1.00 19.98 ? 130 THR B OG1 1 
ATOM   2510 C  CG2 . THR B 1 142 ? 10.327  2.964   49.498  1.00 19.41 ? 130 THR B CG2 1 
ATOM   2511 N  N   . ALA B 1 143 ? 7.300   1.543   50.591  1.00 18.28 ? 131 ALA B N   1 
ATOM   2512 C  CA  . ALA B 1 143 ? 6.826   0.395   51.378  1.00 18.67 ? 131 ALA B CA  1 
ATOM   2513 C  C   . ALA B 1 143 ? 6.825   -0.869  50.541  1.00 19.89 ? 131 ALA B C   1 
ATOM   2514 O  O   . ALA B 1 143 ? 6.935   -0.809  49.265  1.00 19.01 ? 131 ALA B O   1 
ATOM   2515 C  CB  . ALA B 1 143 ? 5.454   0.677   51.959  1.00 18.54 ? 131 ALA B CB  1 
ATOM   2516 N  N   . THR B 1 144 ? 6.671   -1.976  51.256  1.00 18.38 ? 132 THR B N   1 
ATOM   2517 C  CA  . THR B 1 144 ? 6.516   -3.349  50.702  1.00 19.24 ? 132 THR B CA  1 
ATOM   2518 C  C   . THR B 1 144 ? 5.119   -3.850  51.035  1.00 20.05 ? 132 THR B C   1 
ATOM   2519 O  O   . THR B 1 144 ? 4.754   -3.846  52.222  1.00 22.26 ? 132 THR B O   1 
ATOM   2520 C  CB  . THR B 1 144 ? 7.612   -4.292  51.179  1.00 22.35 ? 132 THR B CB  1 
ATOM   2521 O  OG1 . THR B 1 144 ? 8.819   -3.957  50.495  1.00 20.79 ? 132 THR B OG1 1 
ATOM   2522 C  CG2 . THR B 1 144 ? 7.276   -5.735  50.869  1.00 23.60 ? 132 THR B CG2 1 
ATOM   2523 N  N   . PHE B 1 145 ? 4.318   -4.157  50.015  1.00 16.40 ? 133 PHE B N   1 
ATOM   2524 C  CA  . PHE B 1 145 ? 2.884   -4.412  50.250  1.00 17.48 ? 133 PHE B CA  1 
ATOM   2525 C  C   . PHE B 1 145 ? 2.367   -5.428  49.228  1.00 17.61 ? 133 PHE B C   1 
ATOM   2526 O  O   . PHE B 1 145 ? 2.993   -5.641  48.170  1.00 17.67 ? 133 PHE B O   1 
ATOM   2527 C  CB  . PHE B 1 145 ? 2.099   -3.098  50.239  1.00 18.53 ? 133 PHE B CB  1 
ATOM   2528 C  CG  . PHE B 1 145 ? 2.308   -2.279  49.000  1.00 16.89 ? 133 PHE B CG  1 
ATOM   2529 C  CD1 . PHE B 1 145 ? 1.557   -2.500  47.855  1.00 15.94 ? 133 PHE B CD1 1 
ATOM   2530 C  CD2 . PHE B 1 145 ? 3.295   -1.305  48.979  1.00 17.15 ? 133 PHE B CD2 1 
ATOM   2531 C  CE1 . PHE B 1 145 ? 1.795   -1.748  46.720  1.00 18.15 ? 133 PHE B CE1 1 
ATOM   2532 C  CE2 . PHE B 1 145 ? 3.515   -0.528  47.859  1.00 16.44 ? 133 PHE B CE2 1 
ATOM   2533 C  CZ  . PHE B 1 145 ? 2.761   -0.751  46.720  1.00 17.26 ? 133 PHE B CZ  1 
ATOM   2534 N  N   . ASN B 1 146 ? 1.269   -6.071  49.599  1.00 17.44 ? 134 ASN B N   1 
ATOM   2535 C  CA  . ASN B 1 146 ? 0.544   -7.078  48.782  1.00 18.37 ? 134 ASN B CA  1 
ATOM   2536 C  C   . ASN B 1 146 ? -0.239  -6.280  47.734  1.00 16.60 ? 134 ASN B C   1 
ATOM   2537 O  O   . ASN B 1 146 ? -0.711  -5.141  48.030  1.00 15.49 ? 134 ASN B O   1 
ATOM   2538 C  CB  . ASN B 1 146 ? -0.362  -7.964  49.632  1.00 21.55 ? 134 ASN B CB  1 
ATOM   2539 C  CG  . ASN B 1 146 ? 0.341   -9.096  50.379  1.00 27.21 ? 134 ASN B CG  1 
ATOM   2540 O  OD1 . ASN B 1 146 ? 1.540   -9.342  50.218  1.00 29.12 ? 134 ASN B OD1 1 
ATOM   2541 N  ND2 . ASN B 1 146 ? -0.412  -9.818  51.194  1.00 27.26 ? 134 ASN B ND2 1 
ATOM   2542 N  N   . GLN B 1 147 ? -0.324  -6.821  46.533  1.00 15.54 ? 135 GLN B N   1 
ATOM   2543 C  CA  . GLN B 1 147 ? -1.076  -6.209  45.424  1.00 17.29 ? 135 GLN B CA  1 
ATOM   2544 C  C   . GLN B 1 147 ? -2.023  -7.254  44.847  1.00 18.74 ? 135 GLN B C   1 
ATOM   2545 O  O   . GLN B 1 147 ? -1.574  -8.373  44.488  1.00 18.46 ? 135 GLN B O   1 
ATOM   2546 C  CB  . GLN B 1 147 ? -0.095  -5.601  44.418  1.00 18.21 ? 135 GLN B CB  1 
ATOM   2547 C  CG  . GLN B 1 147 ? -0.778  -4.867  43.291  1.00 17.95 ? 135 GLN B CG  1 
ATOM   2548 C  CD  . GLN B 1 147 ? 0.237   -4.517  42.228  1.00 18.85 ? 135 GLN B CD  1 
ATOM   2549 O  OE1 . GLN B 1 147 ? 0.804   -5.409  41.618  1.00 17.26 ? 135 GLN B OE1 1 
ATOM   2550 N  NE2 . GLN B 1 147 ? 0.473   -3.220  42.019  1.00 16.31 ? 135 GLN B NE2 1 
ATOM   2551 N  N   . TYR B 1 148 ? -3.313  -6.939  44.830  1.00 16.27 ? 136 TYR B N   1 
ATOM   2552 C  CA  . TYR B 1 148 ? -4.361  -7.906  44.446  1.00 15.41 ? 136 TYR B CA  1 
ATOM   2553 C  C   . TYR B 1 148 ? -5.040  -7.382  43.181  1.00 16.12 ? 136 TYR B C   1 
ATOM   2554 O  O   . TYR B 1 148 ? -5.242  -6.142  43.012  1.00 15.23 ? 136 TYR B O   1 
ATOM   2555 C  CB  . TYR B 1 148 ? -5.436  -8.136  45.505  1.00 15.16 ? 136 TYR B CB  1 
ATOM   2556 C  CG  . TYR B 1 148 ? -4.929  -8.567  46.849  1.00 15.78 ? 136 TYR B CG  1 
ATOM   2557 C  CD1 . TYR B 1 148 ? -3.729  -9.247  47.005  1.00 16.67 ? 136 TYR B CD1 1 
ATOM   2558 C  CD2 . TYR B 1 148 ? -5.696  -8.368  47.979  1.00 16.07 ? 136 TYR B CD2 1 
ATOM   2559 C  CE1 . TYR B 1 148 ? -3.286  -9.672  48.250  1.00 17.22 ? 136 TYR B CE1 1 
ATOM   2560 C  CE2 . TYR B 1 148 ? -5.248  -8.737  49.236  1.00 18.72 ? 136 TYR B CE2 1 
ATOM   2561 C  CZ  . TYR B 1 148 ? -4.051  -9.414  49.373  1.00 18.84 ? 136 TYR B CZ  1 
ATOM   2562 O  OH  . TYR B 1 148 ? -3.565  -9.783  50.593  1.00 19.28 ? 136 TYR B OH  1 
ATOM   2563 N  N   . TRP B 1 149 ? -5.316  -8.318  42.291  1.00 13.90 ? 137 TRP B N   1 
ATOM   2564 C  CA  . TRP B 1 149 ? -5.942  -8.054  40.980  1.00 13.82 ? 137 TRP B CA  1 
ATOM   2565 C  C   . TRP B 1 149 ? -7.208  -8.869  40.799  1.00 14.03 ? 137 TRP B C   1 
ATOM   2566 O  O   . TRP B 1 149 ? -7.187  -10.147 41.024  1.00 14.46 ? 137 TRP B O   1 
ATOM   2567 C  CB  . TRP B 1 149 ? -4.950  -8.320  39.853  1.00 13.98 ? 137 TRP B CB  1 
ATOM   2568 C  CG  . TRP B 1 149 ? -3.668  -7.559  39.898  1.00 15.55 ? 137 TRP B CG  1 
ATOM   2569 C  CD1 . TRP B 1 149 ? -2.551  -7.878  40.617  1.00 16.24 ? 137 TRP B CD1 1 
ATOM   2570 C  CD2 . TRP B 1 149 ? -3.370  -6.322  39.233  1.00 15.75 ? 137 TRP B CD2 1 
ATOM   2571 N  NE1 . TRP B 1 149 ? -1.581  -6.944  40.410  1.00 16.62 ? 137 TRP B NE1 1 
ATOM   2572 C  CE2 . TRP B 1 149 ? -2.055  -5.958  39.591  1.00 15.88 ? 137 TRP B CE2 1 
ATOM   2573 C  CE3 . TRP B 1 149 ? -4.085  -5.481  38.383  1.00 14.46 ? 137 TRP B CE3 1 
ATOM   2574 C  CZ2 . TRP B 1 149 ? -1.444  -4.809  39.087  1.00 14.94 ? 137 TRP B CZ2 1 
ATOM   2575 C  CZ3 . TRP B 1 149 ? -3.509  -4.328  37.927  1.00 14.55 ? 137 TRP B CZ3 1 
ATOM   2576 C  CH2 . TRP B 1 149 ? -2.186  -4.006  38.259  1.00 16.03 ? 137 TRP B CH2 1 
ATOM   2577 N  N   . SER B 1 150 ? -8.232  -8.216  40.233  1.00 14.73 ? 138 SER B N   1 
ATOM   2578 C  CA  . SER B 1 150 ? -9.383  -8.845  39.549  1.00 16.85 ? 138 SER B CA  1 
ATOM   2579 C  C   . SER B 1 150 ? -9.384  -8.302  38.125  1.00 15.58 ? 138 SER B C   1 
ATOM   2580 O  O   . SER B 1 150 ? -9.462  -7.083  37.975  1.00 16.18 ? 138 SER B O   1 
ATOM   2581 C  CB  . SER B 1 150 ? -10.663 -8.549  40.234  1.00 18.01 ? 138 SER B CB  1 
ATOM   2582 O  OG  . SER B 1 150 ? -11.007 -9.539  41.141  1.00 23.05 ? 138 SER B OG  1 
ATOM   2583 N  N   . VAL B 1 151 ? -9.221  -9.144  37.109  1.00 14.45 ? 139 VAL B N   1 
ATOM   2584 C  CA  . VAL B 1 151 ? -9.102  -8.665  35.707  1.00 13.75 ? 139 VAL B CA  1 
ATOM   2585 C  C   . VAL B 1 151 ? -10.218 -9.263  34.843  1.00 14.88 ? 139 VAL B C   1 
ATOM   2586 O  O   . VAL B 1 151 ? -10.282 -10.519 34.657  1.00 15.04 ? 139 VAL B O   1 
ATOM   2587 C  CB  . VAL B 1 151 ? -7.717  -8.938  35.111  1.00 13.42 ? 139 VAL B CB  1 
ATOM   2588 C  CG1 . VAL B 1 151 ? -7.647  -8.497  33.683  1.00 13.80 ? 139 VAL B CG1 1 
ATOM   2589 C  CG2 . VAL B 1 151 ? -6.570  -8.410  35.960  1.00 14.50 ? 139 VAL B CG2 1 
ATOM   2590 N  N   . ARG B 1 152 ? -11.082 -8.395  34.348  1.00 15.03 ? 140 ARG B N   1 
ATOM   2591 C  CA  . ARG B 1 152 ? -12.277 -8.815  33.584  1.00 16.27 ? 140 ARG B CA  1 
ATOM   2592 C  C   . ARG B 1 152 ? -11.818 -9.477  32.287  1.00 16.97 ? 140 ARG B C   1 
ATOM   2593 O  O   . ARG B 1 152 ? -10.868 -8.983  31.636  1.00 18.17 ? 140 ARG B O   1 
ATOM   2594 C  CB  . ARG B 1 152 ? -13.180 -7.619  33.352  1.00 16.32 ? 140 ARG B CB  1 
ATOM   2595 C  CG  . ARG B 1 152 ? -14.620 -8.008  33.044  1.00 16.51 ? 140 ARG B CG  1 
ATOM   2596 C  CD  . ARG B 1 152 ? -15.474 -6.806  32.823  1.00 17.28 ? 140 ARG B CD  1 
ATOM   2597 N  NE  . ARG B 1 152 ? -16.787 -7.126  32.275  1.00 16.98 ? 140 ARG B NE  1 
ATOM   2598 C  CZ  . ARG B 1 152 ? -17.906 -7.289  32.982  1.00 17.73 ? 140 ARG B CZ  1 
ATOM   2599 N  NH1 . ARG B 1 152 ? -17.933 -7.291  34.310  1.00 19.01 ? 140 ARG B NH1 1 
ATOM   2600 N  NH2 . ARG B 1 152 ? -19.020 -7.531  32.324  1.00 19.16 ? 140 ARG B NH2 1 
ATOM   2601 N  N   . THR B 1 153 ? -12.440 -10.601 31.921  1.00 19.80 ? 141 THR B N   1 
ATOM   2602 C  CA  . THR B 1 153 ? -12.064 -11.345 30.685  1.00 20.50 ? 141 THR B CA  1 
ATOM   2603 C  C   . THR B 1 153 ? -12.656 -10.671 29.434  1.00 21.16 ? 141 THR B C   1 
ATOM   2604 O  O   . THR B 1 153 ? -12.060 -10.866 28.364  1.00 22.97 ? 141 THR B O   1 
ATOM   2605 C  CB  . THR B 1 153 ? -12.401 -12.840 30.790  1.00 20.63 ? 141 THR B CB  1 
ATOM   2606 O  OG1 . THR B 1 153 ? -13.814 -12.985 30.831  1.00 21.86 ? 141 THR B OG1 1 
ATOM   2607 C  CG2 . THR B 1 153 ? -11.774 -13.524 31.980  1.00 21.52 ? 141 THR B CG2 1 
ATOM   2608 N  N   . ASP B 1 154 ? -13.783 -9.970  29.544  1.00 22.74 ? 142 ASP B N   1 
ATOM   2609 C  CA  . ASP B 1 154 ? -14.463 -9.197  28.469  1.00 25.92 ? 142 ASP B CA  1 
ATOM   2610 C  C   . ASP B 1 154 ? -14.391 -7.714  28.841  1.00 23.54 ? 142 ASP B C   1 
ATOM   2611 O  O   . ASP B 1 154 ? -15.198 -7.268  29.692  1.00 24.59 ? 142 ASP B O   1 
ATOM   2612 C  CB  . ASP B 1 154 ? -15.908 -9.667  28.284  1.00 27.98 ? 142 ASP B CB  1 
ATOM   2613 C  CG  . ASP B 1 154 ? -16.655 -8.976  27.149  1.00 33.24 ? 142 ASP B CG  1 
ATOM   2614 O  OD1 . ASP B 1 154 ? -16.125 -7.987  26.615  1.00 38.68 ? 142 ASP B OD1 1 
ATOM   2615 O  OD2 . ASP B 1 154 ? -17.769 -9.432  26.811  1.00 40.68 ? 142 ASP B OD2 1 
ATOM   2616 N  N   . HIS B 1 155 ? -13.465 -6.984  28.222  1.00 20.59 ? 143 HIS B N   1 
ATOM   2617 C  CA  . HIS B 1 155 ? -13.193 -5.557  28.554  1.00 21.06 ? 143 HIS B CA  1 
ATOM   2618 C  C   . HIS B 1 155 ? -14.448 -4.707  28.411  1.00 19.89 ? 143 HIS B C   1 
ATOM   2619 O  O   . HIS B 1 155 ? -15.215 -4.865  27.420  1.00 19.26 ? 143 HIS B O   1 
ATOM   2620 C  CB  . HIS B 1 155 ? -12.001 -5.033  27.765  1.00 21.45 ? 143 HIS B CB  1 
ATOM   2621 C  CG  . HIS B 1 155 ? -10.750 -5.710  28.200  1.00 22.67 ? 143 HIS B CG  1 
ATOM   2622 N  ND1 . HIS B 1 155 ? -9.524  -5.462  27.640  1.00 24.67 ? 143 HIS B ND1 1 
ATOM   2623 C  CD2 . HIS B 1 155 ? -10.564 -6.726  29.071  1.00 22.53 ? 143 HIS B CD2 1 
ATOM   2624 C  CE1 . HIS B 1 155 ? -8.637  -6.305  28.121  1.00 25.04 ? 143 HIS B CE1 1 
ATOM   2625 N  NE2 . HIS B 1 155 ? -9.234  -7.047  29.041  1.00 27.13 ? 143 HIS B NE2 1 
ATOM   2626 N  N   . ARG B 1 156 ? -14.617 -3.753  29.309  1.00 16.37 ? 144 ARG B N   1 
ATOM   2627 C  CA  . ARG B 1 156 ? -15.688 -2.773  29.145  1.00 17.95 ? 144 ARG B CA  1 
ATOM   2628 C  C   . ARG B 1 156 ? -15.321 -1.415  29.737  1.00 17.49 ? 144 ARG B C   1 
ATOM   2629 O  O   . ARG B 1 156 ? -14.430 -1.312  30.611  1.00 17.79 ? 144 ARG B O   1 
ATOM   2630 C  CB  . ARG B 1 156 ? -16.969 -3.357  29.726  1.00 18.75 ? 144 ARG B CB  1 
ATOM   2631 C  CG  . ARG B 1 156 ? -17.018 -3.322  31.233  1.00 17.50 ? 144 ARG B CG  1 
ATOM   2632 C  CD  . ARG B 1 156 ? -18.315 -3.890  31.797  1.00 19.28 ? 144 ARG B CD  1 
ATOM   2633 N  NE  . ARG B 1 156 ? -18.153 -3.956  33.233  1.00 18.75 ? 144 ARG B NE  1 
ATOM   2634 C  CZ  . ARG B 1 156 ? -19.124 -4.159  34.139  1.00 17.57 ? 144 ARG B CZ  1 
ATOM   2635 N  NH1 . ARG B 1 156 ? -20.384 -4.333  33.775  1.00 16.86 ? 144 ARG B NH1 1 
ATOM   2636 N  NH2 . ARG B 1 156 ? -18.816 -4.111  35.420  1.00 19.06 ? 144 ARG B NH2 1 
ATOM   2637 N  N   . VAL B 1 157 ? -16.088 -0.437  29.323  1.00 16.35 ? 145 VAL B N   1 
ATOM   2638 C  CA  . VAL B 1 157 ? -16.026 0.967   29.818  1.00 16.31 ? 145 VAL B CA  1 
ATOM   2639 C  C   . VAL B 1 157 ? -17.407 1.375   30.301  1.00 17.51 ? 145 VAL B C   1 
ATOM   2640 O  O   . VAL B 1 157 ? -18.264 1.659   29.457  1.00 17.97 ? 145 VAL B O   1 
ATOM   2641 C  CB  . VAL B 1 157 ? -15.476 1.921   28.787  1.00 16.28 ? 145 VAL B CB  1 
ATOM   2642 C  CG1 . VAL B 1 157 ? -15.453 3.313   29.390  1.00 16.31 ? 145 VAL B CG1 1 
ATOM   2643 C  CG2 . VAL B 1 157 ? -14.123 1.470   28.301  1.00 16.81 ? 145 VAL B CG2 1 
ATOM   2644 N  N   . GLY B 1 158 ? -17.583 1.306   31.611  1.00 19.80 ? 146 GLY B N   1 
ATOM   2645 C  CA  . GLY B 1 158 ? -18.849 1.625   32.277  1.00 20.50 ? 146 GLY B CA  1 
ATOM   2646 C  C   . GLY B 1 158 ? -19.544 0.396   32.805  1.00 23.04 ? 146 GLY B C   1 
ATOM   2647 O  O   . GLY B 1 158 ? -19.011 -0.722  32.739  1.00 24.08 ? 146 GLY B O   1 
ATOM   2648 N  N   . GLY B 1 159 ? -20.745 0.590   33.301  1.00 25.79 ? 147 GLY B N   1 
ATOM   2649 C  CA  . GLY B 1 159 ? -21.475 -0.487  33.973  1.00 22.72 ? 147 GLY B CA  1 
ATOM   2650 C  C   . GLY B 1 159 ? -21.330 -0.336  35.467  1.00 21.47 ? 147 GLY B C   1 
ATOM   2651 O  O   . GLY B 1 159 ? -21.043 0.766   35.939  1.00 22.39 ? 147 GLY B O   1 
ATOM   2652 N  N   . THR B 1 160 ? -21.514 -1.432  36.184  1.00 17.94 ? 148 THR B N   1 
ATOM   2653 C  CA  . THR B 1 160 ? -21.599 -1.476  37.651  1.00 18.92 ? 148 THR B CA  1 
ATOM   2654 C  C   . THR B 1 160 ? -20.540 -2.436  38.142  1.00 16.82 ? 148 THR B C   1 
ATOM   2655 O  O   . THR B 1 160 ? -20.382 -3.503  37.533  1.00 17.61 ? 148 THR B O   1 
ATOM   2656 C  CB  . THR B 1 160 ? -22.974 -1.986  38.092  1.00 22.29 ? 148 THR B CB  1 
ATOM   2657 O  OG1 . THR B 1 160 ? -23.851 -1.072  37.456  1.00 23.69 ? 148 THR B OG1 1 
ATOM   2658 C  CG2 . THR B 1 160 ? -23.144 -2.036  39.594  1.00 23.55 ? 148 THR B CG2 1 
ATOM   2659 N  N   . VAL B 1 161 ? -19.865 -2.064  39.219  1.00 16.19 ? 149 VAL B N   1 
ATOM   2660 C  CA  . VAL B 1 161 ? -18.856 -2.901  39.889  1.00 16.90 ? 149 VAL B CA  1 
ATOM   2661 C  C   . VAL B 1 161 ? -19.343 -3.111  41.314  1.00 15.49 ? 149 VAL B C   1 
ATOM   2662 O  O   . VAL B 1 161 ? -19.431 -2.133  42.060  1.00 16.58 ? 149 VAL B O   1 
ATOM   2663 C  CB  . VAL B 1 161 ? -17.435 -2.335  39.821  1.00 17.32 ? 149 VAL B CB  1 
ATOM   2664 C  CG1 . VAL B 1 161 ? -16.480 -3.140  40.668  1.00 18.58 ? 149 VAL B CG1 1 
ATOM   2665 C  CG2 . VAL B 1 161 ? -16.917 -2.268  38.391  1.00 18.73 ? 149 VAL B CG2 1 
ATOM   2666 N  N   . THR B 1 162 ? -19.720 -4.349  41.610  1.00 15.26 ? 150 THR B N   1 
ATOM   2667 C  CA  . THR B 1 162 ? -20.144 -4.765  42.977  1.00 15.88 ? 150 THR B CA  1 
ATOM   2668 C  C   . THR B 1 162 ? -18.852 -5.119  43.714  1.00 15.36 ? 150 THR B C   1 
ATOM   2669 O  O   . THR B 1 162 ? -18.450 -6.304  43.711  1.00 15.64 ? 150 THR B O   1 
ATOM   2670 C  CB  . THR B 1 162 ? -21.185 -5.884  42.937  1.00 18.44 ? 150 THR B CB  1 
ATOM   2671 O  OG1 . THR B 1 162 ? -22.237 -5.576  42.019  1.00 17.52 ? 150 THR B OG1 1 
ATOM   2672 C  CG2 . THR B 1 162 ? -21.734 -6.162  44.325  1.00 18.74 ? 150 THR B CG2 1 
ATOM   2673 N  N   . THR B 1 163 ? -18.200 -4.135  44.304  1.00 16.00 ? 151 THR B N   1 
ATOM   2674 C  CA  . THR B 1 163 ? -16.843 -4.313  44.897  1.00 16.23 ? 151 THR B CA  1 
ATOM   2675 C  C   . THR B 1 163 ? -16.867 -5.426  45.945  1.00 16.78 ? 151 THR B C   1 
ATOM   2676 O  O   . THR B 1 163 ? -15.843 -6.106  46.087  1.00 16.35 ? 151 THR B O   1 
ATOM   2677 C  CB  . THR B 1 163 ? -16.246 -2.995  45.432  1.00 18.16 ? 151 THR B CB  1 
ATOM   2678 O  OG1 . THR B 1 163 ? -17.032 -2.528  46.532  1.00 17.47 ? 151 THR B OG1 1 
ATOM   2679 C  CG2 . THR B 1 163 ? -16.136 -1.915  44.383  1.00 19.19 ? 151 THR B CG2 1 
ATOM   2680 N  N   . GLN B 1 164 ? -17.960 -5.585  46.702  1.00 17.21 ? 152 GLN B N   1 
ATOM   2681 C  CA  . GLN B 1 164 ? -18.013 -6.552  47.817  1.00 18.48 ? 152 GLN B CA  1 
ATOM   2682 C  C   . GLN B 1 164 ? -17.840 -7.979  47.260  1.00 17.12 ? 152 GLN B C   1 
ATOM   2683 O  O   . GLN B 1 164 ? -17.174 -8.783  47.911  1.00 18.43 ? 152 GLN B O   1 
ATOM   2684 C  CB  . GLN B 1 164 ? -19.294 -6.380  48.629  1.00 22.26 ? 152 GLN B CB  1 
ATOM   2685 C  CG  . GLN B 1 164 ? -19.371 -7.307  49.838  1.00 27.41 ? 152 GLN B CG  1 
ATOM   2686 C  CD  . GLN B 1 164 ? -18.269 -7.023  50.838  1.00 31.53 ? 152 GLN B CD  1 
ATOM   2687 O  OE1 . GLN B 1 164 ? -18.037 -5.883  51.226  1.00 39.25 ? 152 GLN B OE1 1 
ATOM   2688 N  NE2 . GLN B 1 164 ? -17.558 -8.049  51.267  1.00 38.27 ? 152 GLN B NE2 1 
ATOM   2689 N  N   . ASN B 1 165 ? -18.261 -8.249  46.023  1.00 16.09 ? 153 ASN B N   1 
ATOM   2690 C  CA  . ASN B 1 165 ? -18.082 -9.603  45.424  1.00 16.83 ? 153 ASN B CA  1 
ATOM   2691 C  C   . ASN B 1 165 ? -16.584 -9.877  45.152  1.00 18.01 ? 153 ASN B C   1 
ATOM   2692 O  O   . ASN B 1 165 ? -16.132 -11.047 45.304  1.00 18.79 ? 153 ASN B O   1 
ATOM   2693 C  CB  . ASN B 1 165 ? -18.902 -9.770  44.146  1.00 18.51 ? 153 ASN B CB  1 
ATOM   2694 C  CG  . ASN B 1 165 ? -20.386 -9.879  44.388  1.00 21.44 ? 153 ASN B CG  1 
ATOM   2695 O  OD1 . ASN B 1 165 ? -20.828 -10.086 45.514  1.00 23.19 ? 153 ASN B OD1 1 
ATOM   2696 N  ND2 . ASN B 1 165 ? -21.171 -9.699  43.326  1.00 21.58 ? 153 ASN B ND2 1 
ATOM   2697 N  N   . HIS B 1 166 ? -15.813 -8.864  44.742  1.00 17.26 ? 154 HIS B N   1 
ATOM   2698 C  CA  . HIS B 1 166 ? -14.352 -9.007  44.536  1.00 17.81 ? 154 HIS B CA  1 
ATOM   2699 C  C   . HIS B 1 166 ? -13.653 -9.209  45.875  1.00 17.95 ? 154 HIS B C   1 
ATOM   2700 O  O   . HIS B 1 166 ? -12.878 -10.161 46.021  1.00 17.93 ? 154 HIS B O   1 
ATOM   2701 C  CB  . HIS B 1 166 ? -13.789 -7.789  43.820  1.00 15.72 ? 154 HIS B CB  1 
ATOM   2702 C  CG  . HIS B 1 166 ? -14.314 -7.706  42.435  1.00 14.76 ? 154 HIS B CG  1 
ATOM   2703 N  ND1 . HIS B 1 166 ? -13.715 -8.353  41.381  1.00 16.20 ? 154 HIS B ND1 1 
ATOM   2704 C  CD2 . HIS B 1 166 ? -15.419 -7.124  41.951  1.00 16.48 ? 154 HIS B CD2 1 
ATOM   2705 C  CE1 . HIS B 1 166 ? -14.418 -8.131  40.281  1.00 16.27 ? 154 HIS B CE1 1 
ATOM   2706 N  NE2 . HIS B 1 166 ? -15.476 -7.375  40.592  1.00 15.13 ? 154 HIS B NE2 1 
ATOM   2707 N  N   . PHE B 1 167 ? -13.964 -8.364  46.847  1.00 17.12 ? 155 PHE B N   1 
ATOM   2708 C  CA  . PHE B 1 167 ? -13.311 -8.471  48.183  1.00 16.97 ? 155 PHE B CA  1 
ATOM   2709 C  C   . PHE B 1 167 ? -13.589 -9.865  48.769  1.00 19.07 ? 155 PHE B C   1 
ATOM   2710 O  O   . PHE B 1 167 ? -12.658 -10.472 49.373  1.00 18.79 ? 155 PHE B O   1 
ATOM   2711 C  CB  . PHE B 1 167 ? -13.750 -7.362  49.130  1.00 18.48 ? 155 PHE B CB  1 
ATOM   2712 C  CG  . PHE B 1 167 ? -13.486 -5.971  48.611  1.00 17.22 ? 155 PHE B CG  1 
ATOM   2713 C  CD1 . PHE B 1 167 ? -12.419 -5.730  47.756  1.00 18.57 ? 155 PHE B CD1 1 
ATOM   2714 C  CD2 . PHE B 1 167 ? -14.311 -4.918  48.929  1.00 18.60 ? 155 PHE B CD2 1 
ATOM   2715 C  CE1 . PHE B 1 167 ? -12.146 -4.456  47.291  1.00 19.76 ? 155 PHE B CE1 1 
ATOM   2716 C  CE2 . PHE B 1 167 ? -14.061 -3.652  48.428  1.00 19.10 ? 155 PHE B CE2 1 
ATOM   2717 C  CZ  . PHE B 1 167 ? -12.975 -3.420  47.620  1.00 20.94 ? 155 PHE B CZ  1 
ATOM   2718 N  N   . ASP B 1 168 ? -14.851 -10.300 48.683  1.00 19.24 ? 156 ASP B N   1 
ATOM   2719 C  CA  . ASP B 1 168 ? -15.279 -11.627 49.187  1.00 22.76 ? 156 ASP B CA  1 
ATOM   2720 C  C   . ASP B 1 168 ? -14.433 -12.702 48.495  1.00 21.25 ? 156 ASP B C   1 
ATOM   2721 O  O   . ASP B 1 168 ? -13.981 -13.677 49.189  1.00 20.76 ? 156 ASP B O   1 
ATOM   2722 C  CB  . ASP B 1 168 ? -16.779 -11.829 48.979  1.00 25.58 ? 156 ASP B CB  1 
ATOM   2723 C  CG  . ASP B 1 168 ? -17.651 -11.092 49.976  1.00 26.85 ? 156 ASP B CG  1 
ATOM   2724 O  OD1 . ASP B 1 168 ? -17.106 -10.567 50.963  1.00 30.84 ? 156 ASP B OD1 1 
ATOM   2725 O  OD2 . ASP B 1 168 ? -18.855 -11.009 49.728  1.00 33.33 ? 156 ASP B OD2 1 
ATOM   2726 N  N   . ALA B 1 169 ? -14.308 -12.644 47.159  1.00 21.09 ? 157 ALA B N   1 
ATOM   2727 C  CA  . ALA B 1 169 ? -13.609 -13.676 46.372  1.00 20.61 ? 157 ALA B CA  1 
ATOM   2728 C  C   . ALA B 1 169 ? -12.135 -13.680 46.764  1.00 20.61 ? 157 ALA B C   1 
ATOM   2729 O  O   . ALA B 1 169 ? -11.565 -14.756 46.961  1.00 21.57 ? 157 ALA B O   1 
ATOM   2730 C  CB  . ALA B 1 169 ? -13.796 -13.487 44.891  1.00 21.06 ? 157 ALA B CB  1 
ATOM   2731 N  N   . TRP B 1 170 ? -11.551 -12.508 46.968  1.00 17.32 ? 158 TRP B N   1 
ATOM   2732 C  CA  . TRP B 1 170 ? -10.136 -12.413 47.409  1.00 18.32 ? 158 TRP B CA  1 
ATOM   2733 C  C   . TRP B 1 170 ? -9.971  -13.035 48.800  1.00 17.15 ? 158 TRP B C   1 
ATOM   2734 O  O   . TRP B 1 170 ? -9.034  -13.811 48.985  1.00 20.98 ? 158 TRP B O   1 
ATOM   2735 C  CB  . TRP B 1 170 ? -9.682  -10.945 47.406  1.00 19.41 ? 158 TRP B CB  1 
ATOM   2736 C  CG  . TRP B 1 170 ? -9.697  -10.305 46.051  1.00 19.73 ? 158 TRP B CG  1 
ATOM   2737 C  CD1 . TRP B 1 170 ? -9.870  -10.894 44.830  1.00 21.13 ? 158 TRP B CD1 1 
ATOM   2738 C  CD2 . TRP B 1 170 ? -9.580  -8.893  45.802  1.00 17.72 ? 158 TRP B CD2 1 
ATOM   2739 N  NE1 . TRP B 1 170 ? -9.854  -9.947  43.831  1.00 21.55 ? 158 TRP B NE1 1 
ATOM   2740 C  CE2 . TRP B 1 170 ? -9.659  -8.713  44.402  1.00 18.80 ? 158 TRP B CE2 1 
ATOM   2741 C  CE3 . TRP B 1 170 ? -9.478  -7.775  46.627  1.00 19.20 ? 158 TRP B CE3 1 
ATOM   2742 C  CZ2 . TRP B 1 170 ? -9.584  -7.456  43.811  1.00 19.53 ? 158 TRP B CZ2 1 
ATOM   2743 C  CZ3 . TRP B 1 170 ? -9.435  -6.530  46.038  1.00 18.12 ? 158 TRP B CZ3 1 
ATOM   2744 C  CH2 . TRP B 1 170 ? -9.536  -6.371  44.654  1.00 17.58 ? 158 TRP B CH2 1 
ATOM   2745 N  N   . LYS B 1 171 ? -10.846 -12.717 49.750  1.00 19.59 ? 159 LYS B N   1 
ATOM   2746 C  CA  . LYS B 1 171 ? -10.721 -13.170 51.150  1.00 21.65 ? 159 LYS B CA  1 
ATOM   2747 C  C   . LYS B 1 171 ? -10.922 -14.689 51.199  1.00 23.12 ? 159 LYS B C   1 
ATOM   2748 O  O   . LYS B 1 171 ? -10.233 -15.372 51.973  1.00 21.77 ? 159 LYS B O   1 
ATOM   2749 C  CB  . LYS B 1 171 ? -11.791 -12.509 52.014  1.00 24.72 ? 159 LYS B CB  1 
ATOM   2750 C  CG  . LYS B 1 171 ? -11.737 -12.847 53.486  1.00 31.50 ? 159 LYS B CG  1 
ATOM   2751 C  CD  . LYS B 1 171 ? -13.109 -12.844 54.096  1.00 35.27 ? 159 LYS B CD  1 
ATOM   2752 C  CE  . LYS B 1 171 ? -13.079 -12.612 55.586  1.00 37.73 ? 159 LYS B CE  1 
ATOM   2753 N  NZ  . LYS B 1 171 ? -14.421 -12.241 56.078  1.00 41.64 ? 159 LYS B NZ  1 
ATOM   2754 N  N   . ASN B 1 172 ? -11.905 -15.141 50.426  1.00 24.31 ? 160 ASN B N   1 
ATOM   2755 C  CA  . ASN B 1 172 ? -12.279 -16.570 50.285  1.00 28.80 ? 160 ASN B CA  1 
ATOM   2756 C  C   . ASN B 1 172 ? -11.086 -17.355 49.751  1.00 27.02 ? 160 ASN B C   1 
ATOM   2757 O  O   . ASN B 1 172 ? -10.945 -18.560 50.145  1.00 28.01 ? 160 ASN B O   1 
ATOM   2758 C  CB  . ASN B 1 172 ? -13.556 -16.667 49.454  1.00 31.57 ? 160 ASN B CB  1 
ATOM   2759 C  CG  . ASN B 1 172 ? -14.775 -16.301 50.274  1.00 34.86 ? 160 ASN B CG  1 
ATOM   2760 O  OD1 . ASN B 1 172 ? -14.665 -16.039 51.472  1.00 41.66 ? 160 ASN B OD1 1 
ATOM   2761 N  ND2 . ASN B 1 172 ? -15.938 -16.255 49.640  1.00 40.93 ? 160 ASN B ND2 1 
ATOM   2762 N  N   . ALA B 1 173 ? -10.269 -16.733 48.890  1.00 23.34 ? 161 ALA B N   1 
ATOM   2763 C  CA  . ALA B 1 173 ? -9.045  -17.292 48.262  1.00 24.32 ? 161 ALA B CA  1 
ATOM   2764 C  C   . ALA B 1 173 ? -7.820  -17.173 49.184  1.00 24.53 ? 161 ALA B C   1 
ATOM   2765 O  O   . ALA B 1 173 ? -6.697  -17.563 48.740  1.00 25.60 ? 161 ALA B O   1 
ATOM   2766 C  CB  . ALA B 1 173 ? -8.763  -16.611 46.962  1.00 26.59 ? 161 ALA B CB  1 
ATOM   2767 N  N   . GLY B 1 174 ? -8.000  -16.632 50.389  1.00 21.49 ? 162 GLY B N   1 
ATOM   2768 C  CA  . GLY B 1 174 ? -6.940  -16.525 51.401  1.00 22.85 ? 162 GLY B CA  1 
ATOM   2769 C  C   . GLY B 1 174 ? -6.155  -15.232 51.360  1.00 24.81 ? 162 GLY B C   1 
ATOM   2770 O  O   . GLY B 1 174 ? -5.112  -15.168 52.080  1.00 30.11 ? 162 GLY B O   1 
ATOM   2771 N  N   . LEU B 1 175 ? -6.616  -14.224 50.604  1.00 20.87 ? 163 LEU B N   1 
ATOM   2772 C  CA  . LEU B 1 175 ? -5.928  -12.914 50.480  1.00 22.21 ? 163 LEU B CA  1 
ATOM   2773 C  C   . LEU B 1 175 ? -6.418  -11.990 51.588  1.00 24.86 ? 163 LEU B C   1 
ATOM   2774 O  O   . LEU B 1 175 ? -7.560  -11.552 51.513  1.00 29.27 ? 163 LEU B O   1 
ATOM   2775 C  CB  . LEU B 1 175 ? -6.239  -12.316 49.113  1.00 21.79 ? 163 LEU B CB  1 
ATOM   2776 C  CG  . LEU B 1 175 ? -5.858  -13.206 47.933  1.00 21.94 ? 163 LEU B CG  1 
ATOM   2777 C  CD1 . LEU B 1 175 ? -6.125  -12.502 46.608  1.00 24.29 ? 163 LEU B CD1 1 
ATOM   2778 C  CD2 . LEU B 1 175 ? -4.397  -13.611 48.045  1.00 24.06 ? 163 LEU B CD2 1 
ATOM   2779 N  N   . GLU B 1 176 ? -5.524  -11.591 52.487  1.00 23.68 ? 164 GLU B N   1 
ATOM   2780 C  CA  . GLU B 1 176 ? -5.911  -10.802 53.669  1.00 23.04 ? 164 GLU B CA  1 
ATOM   2781 C  C   . GLU B 1 176 ? -6.014  -9.314  53.301  1.00 20.89 ? 164 GLU B C   1 
ATOM   2782 O  O   . GLU B 1 176 ? -5.154  -8.837  52.567  1.00 21.28 ? 164 GLU B O   1 
ATOM   2783 C  CB  . GLU B 1 176 ? -4.891  -11.069 54.763  1.00 27.48 ? 164 GLU B CB  1 
ATOM   2784 C  CG  . GLU B 1 176 ? -4.881  -12.527 55.177  1.00 33.64 ? 164 GLU B CG  1 
ATOM   2785 C  CD  . GLU B 1 176 ? -4.200  -12.793 56.499  1.00 37.93 ? 164 GLU B CD  1 
ATOM   2786 O  OE1 . GLU B 1 176 ? -3.750  -13.936 56.696  1.00 45.37 ? 164 GLU B OE1 1 
ATOM   2787 O  OE2 . GLU B 1 176 ? -4.136  -11.859 57.336  1.00 43.96 ? 164 GLU B OE2 1 
ATOM   2788 N  N   . MET B 1 177 ? -7.066  -8.669  53.782  1.00 20.08 ? 165 MET B N   1 
ATOM   2789 C  CA  . MET B 1 177 ? -7.338  -7.224  53.573  1.00 21.35 ? 165 MET B CA  1 
ATOM   2790 C  C   . MET B 1 177 ? -7.347  -6.566  54.939  1.00 20.67 ? 165 MET B C   1 
ATOM   2791 O  O   . MET B 1 177 ? -7.813  -7.206  55.923  1.00 20.61 ? 165 MET B O   1 
ATOM   2792 C  CB  . MET B 1 177 ? -8.689  -6.945  52.905  1.00 23.90 ? 165 MET B CB  1 
ATOM   2793 C  CG  . MET B 1 177 ? -8.922  -7.667  51.592  1.00 31.71 ? 165 MET B CG  1 
ATOM   2794 S  SD  . MET B 1 177 ? -8.335  -6.720  50.177  1.00 37.36 ? 165 MET B SD  1 
ATOM   2795 C  CE  . MET B 1 177 ? -9.548  -5.410  49.999  1.00 34.78 ? 165 MET B CE  1 
ATOM   2796 N  N   . GLY B 1 178 ? -6.935  -5.299  54.978  1.00 19.06 ? 166 GLY B N   1 
ATOM   2797 C  CA  . GLY B 1 178 ? -6.984  -4.476  56.197  1.00 18.96 ? 166 GLY B CA  1 
ATOM   2798 C  C   . GLY B 1 178 ? -8.139  -3.506  56.203  1.00 18.60 ? 166 GLY B C   1 
ATOM   2799 O  O   . GLY B 1 178 ? -9.180  -3.758  55.527  1.00 18.30 ? 166 GLY B O   1 
ATOM   2800 N  N   . THR B 1 179 ? -7.997  -2.439  56.975  1.00 19.82 ? 167 THR B N   1 
ATOM   2801 C  CA  . THR B 1 179 ? -8.943  -1.301  57.053  1.00 20.67 ? 167 THR B CA  1 
ATOM   2802 C  C   . THR B 1 179 ? -8.927  -0.519  55.732  1.00 16.73 ? 167 THR B C   1 
ATOM   2803 O  O   . THR B 1 179 ? -7.881  -0.110  55.302  1.00 16.35 ? 167 THR B O   1 
ATOM   2804 C  CB  . THR B 1 179 ? -8.596  -0.428  58.262  1.00 23.54 ? 167 THR B CB  1 
ATOM   2805 O  OG1 . THR B 1 179 ? -8.721  -1.344  59.360  1.00 24.62 ? 167 THR B OG1 1 
ATOM   2806 C  CG2 . THR B 1 179 ? -9.483  0.791   58.357  1.00 24.23 ? 167 THR B CG2 1 
ATOM   2807 N  N   . HIS B 1 180 ? -10.092 -0.263  55.136  1.00 16.94 ? 168 HIS B N   1 
ATOM   2808 C  CA  . HIS B 1 180 ? -10.167 0.430   53.828  1.00 15.29 ? 168 HIS B CA  1 
ATOM   2809 C  C   . HIS B 1 180 ? -9.719  1.903   53.969  1.00 15.40 ? 168 HIS B C   1 
ATOM   2810 O  O   . HIS B 1 180 ? -10.124 2.620   54.878  1.00 15.85 ? 168 HIS B O   1 
ATOM   2811 C  CB  . HIS B 1 180 ? -11.582 0.271   53.239  1.00 16.72 ? 168 HIS B CB  1 
ATOM   2812 C  CG  . HIS B 1 180 ? -11.822 -1.048  52.569  1.00 20.79 ? 168 HIS B CG  1 
ATOM   2813 N  ND1 . HIS B 1 180 ? -12.223 -2.185  53.259  1.00 28.31 ? 168 HIS B ND1 1 
ATOM   2814 C  CD2 . HIS B 1 180 ? -11.656 -1.453  51.282  1.00 22.52 ? 168 HIS B CD2 1 
ATOM   2815 C  CE1 . HIS B 1 180 ? -12.317 -3.206  52.431  1.00 25.26 ? 168 HIS B CE1 1 
ATOM   2816 N  NE2 . HIS B 1 180 ? -11.964 -2.798  51.222  1.00 29.06 ? 168 HIS B NE2 1 
ATOM   2817 N  N   . ASN B 1 181 ? -8.834  2.303   53.082  1.00 13.93 ? 169 ASN B N   1 
ATOM   2818 C  CA  . ASN B 1 181 ? -8.500  3.721   52.837  1.00 14.93 ? 169 ASN B CA  1 
ATOM   2819 C  C   . ASN B 1 181 ? -9.268  4.088   51.562  1.00 14.95 ? 169 ASN B C   1 
ATOM   2820 O  O   . ASN B 1 181 ? -10.424 3.712   51.425  1.00 15.35 ? 169 ASN B O   1 
ATOM   2821 C  CB  . ASN B 1 181 ? -6.986  3.898   52.789  1.00 15.94 ? 169 ASN B CB  1 
ATOM   2822 C  CG  . ASN B 1 181 ? -6.581  5.349   52.940  1.00 20.39 ? 169 ASN B CG  1 
ATOM   2823 O  OD1 . ASN B 1 181 ? -6.412  6.043   51.944  1.00 21.36 ? 169 ASN B OD1 1 
ATOM   2824 N  ND2 . ASN B 1 181 ? -6.516  5.826   54.183  1.00 20.10 ? 169 ASN B ND2 1 
ATOM   2825 N  N   . TYR B 1 182 ? -8.643  4.754   50.616  1.00 14.88 ? 170 TYR B N   1 
ATOM   2826 C  CA  . TYR B 1 182 ? -9.433  5.311   49.496  1.00 14.65 ? 170 TYR B CA  1 
ATOM   2827 C  C   . TYR B 1 182 ? -9.802  4.227   48.494  1.00 14.47 ? 170 TYR B C   1 
ATOM   2828 O  O   . TYR B 1 182 ? -9.164  3.181   48.420  1.00 13.95 ? 170 TYR B O   1 
ATOM   2829 C  CB  . TYR B 1 182 ? -8.705  6.490   48.850  1.00 14.23 ? 170 TYR B CB  1 
ATOM   2830 C  CG  . TYR B 1 182 ? -7.482  6.229   48.014  1.00 12.24 ? 170 TYR B CG  1 
ATOM   2831 C  CD1 . TYR B 1 182 ? -7.575  5.763   46.732  1.00 13.09 ? 170 TYR B CD1 1 
ATOM   2832 C  CD2 . TYR B 1 182 ? -6.229  6.638   48.432  1.00 13.78 ? 170 TYR B CD2 1 
ATOM   2833 C  CE1 . TYR B 1 182 ? -6.475  5.699   45.891  1.00 12.99 ? 170 TYR B CE1 1 
ATOM   2834 C  CE2 . TYR B 1 182 ? -5.105  6.522   47.637  1.00 13.91 ? 170 TYR B CE2 1 
ATOM   2835 C  CZ  . TYR B 1 182 ? -5.218  6.050   46.353  1.00 12.95 ? 170 TYR B CZ  1 
ATOM   2836 O  OH  . TYR B 1 182 ? -4.121  5.920   45.550  1.00 14.76 ? 170 TYR B OH  1 
ATOM   2837 N  N   . MET B 1 183 ? -10.829 4.540   47.704  1.00 14.07 ? 171 MET B N   1 
ATOM   2838 C  CA  . MET B 1 183 ? -11.301 3.687   46.597  1.00 16.32 ? 171 MET B CA  1 
ATOM   2839 C  C   . MET B 1 183 ? -11.800 4.626   45.485  1.00 14.67 ? 171 MET B C   1 
ATOM   2840 O  O   . MET B 1 183 ? -12.636 5.459   45.753  1.00 15.21 ? 171 MET B O   1 
ATOM   2841 C  CB  . MET B 1 183 ? -12.398 2.714   47.052  1.00 15.49 ? 171 MET B CB  1 
ATOM   2842 C  CG  . MET B 1 183 ? -12.901 1.847   45.916  1.00 17.42 ? 171 MET B CG  1 
ATOM   2843 S  SD  . MET B 1 183 ? -13.973 0.494   46.448  1.00 20.63 ? 171 MET B SD  1 
ATOM   2844 C  CE  . MET B 1 183 ? -15.468 1.415   46.764  1.00 20.65 ? 171 MET B CE  1 
ATOM   2845 N  N   . ILE B 1 184 ? -11.213 4.528   44.291  1.00 14.32 ? 172 ILE B N   1 
ATOM   2846 C  CA  . ILE B 1 184 ? -11.505 5.453   43.167  1.00 14.04 ? 172 ILE B CA  1 
ATOM   2847 C  C   . ILE B 1 184 ? -11.756 4.662   41.907  1.00 14.36 ? 172 ILE B C   1 
ATOM   2848 O  O   . ILE B 1 184 ? -11.371 3.448   41.820  1.00 12.27 ? 172 ILE B O   1 
ATOM   2849 C  CB  . ILE B 1 184 ? -10.392 6.505   42.992  1.00 15.69 ? 172 ILE B CB  1 
ATOM   2850 C  CG1 . ILE B 1 184 ? -9.055  5.864   42.614  1.00 16.07 ? 172 ILE B CG1 1 
ATOM   2851 C  CG2 . ILE B 1 184 ? -10.258 7.389   44.207  1.00 15.92 ? 172 ILE B CG2 1 
ATOM   2852 C  CD1 . ILE B 1 184 ? -7.963  6.875   42.265  1.00 16.19 ? 172 ILE B CD1 1 
ATOM   2853 N  N   . VAL B 1 185 ? -12.445 5.291   40.973  1.00 13.27 ? 173 VAL B N   1 
ATOM   2854 C  CA  . VAL B 1 185 ? -12.486 4.756   39.594  1.00 14.51 ? 173 VAL B CA  1 
ATOM   2855 C  C   . VAL B 1 185 ? -11.316 5.404   38.883  1.00 13.31 ? 173 VAL B C   1 
ATOM   2856 O  O   . VAL B 1 185 ? -11.332 6.627   38.695  1.00 13.54 ? 173 VAL B O   1 
ATOM   2857 C  CB  . VAL B 1 185 ? -13.833 5.008   38.903  1.00 16.60 ? 173 VAL B CB  1 
ATOM   2858 C  CG1 . VAL B 1 185 ? -13.801 4.503   37.483  1.00 17.87 ? 173 VAL B CG1 1 
ATOM   2859 C  CG2 . VAL B 1 185 ? -14.961 4.386   39.706  1.00 17.15 ? 173 VAL B CG2 1 
ATOM   2860 N  N   . ALA B 1 186 ? -10.306 4.624   38.578  1.00 12.31 ? 174 ALA B N   1 
ATOM   2861 C  CA  . ALA B 1 186 ? -8.999  5.164   38.206  1.00 13.81 ? 174 ALA B CA  1 
ATOM   2862 C  C   . ALA B 1 186 ? -8.683  4.847   36.759  1.00 14.09 ? 174 ALA B C   1 
ATOM   2863 O  O   . ALA B 1 186 ? -8.877  3.674   36.301  1.00 14.12 ? 174 ALA B O   1 
ATOM   2864 C  CB  . ALA B 1 186 ? -7.925  4.612   39.090  1.00 15.05 ? 174 ALA B CB  1 
ATOM   2865 N  N   . THR B 1 187 ? -8.093  5.834   36.128  1.00 12.25 ? 175 THR B N   1 
ATOM   2866 C  CA  . THR B 1 187 ? -7.342  5.740   34.869  1.00 12.17 ? 175 THR B CA  1 
ATOM   2867 C  C   . THR B 1 187 ? -5.849  5.611   35.173  1.00 13.11 ? 175 THR B C   1 
ATOM   2868 O  O   . THR B 1 187 ? -5.312  6.456   35.870  1.00 13.41 ? 175 THR B O   1 
ATOM   2869 C  CB  . THR B 1 187 ? -7.668  6.908   33.956  1.00 13.58 ? 175 THR B CB  1 
ATOM   2870 O  OG1 . THR B 1 187 ? -9.090  6.905   33.758  1.00 15.07 ? 175 THR B OG1 1 
ATOM   2871 C  CG2 . THR B 1 187 ? -6.971  6.780   32.625  1.00 13.40 ? 175 THR B CG2 1 
ATOM   2872 N  N   . ALA B 1 188 ? -5.189  4.594   34.621  1.00 12.76 ? 176 ALA B N   1 
ATOM   2873 C  CA  . ALA B 1 188 ? -3.734  4.418   34.839  1.00 14.04 ? 176 ALA B CA  1 
ATOM   2874 C  C   . ALA B 1 188 ? -3.071  4.395   33.464  1.00 14.50 ? 176 ALA B C   1 
ATOM   2875 O  O   . ALA B 1 188 ? -3.662  3.843   32.523  1.00 16.06 ? 176 ALA B O   1 
ATOM   2876 C  CB  . ALA B 1 188 ? -3.433  3.158   35.588  1.00 13.75 ? 176 ALA B CB  1 
ATOM   2877 N  N   . GLY B 1 189 ? -1.816  4.782   33.409  1.00 13.91 ? 177 GLY B N   1 
ATOM   2878 C  CA  . GLY B 1 189 ? -1.087  4.678   32.143  1.00 14.65 ? 177 GLY B CA  1 
ATOM   2879 C  C   . GLY B 1 189 ? 0.370   4.538   32.413  1.00 16.34 ? 177 GLY B C   1 
ATOM   2880 O  O   . GLY B 1 189 ? 0.802   4.885   33.517  1.00 17.42 ? 177 GLY B O   1 
ATOM   2881 N  N   . TYR B 1 190 ? 1.099   3.992   31.447  1.00 17.42 ? 178 TYR B N   1 
ATOM   2882 C  CA  . TYR B 1 190 ? 2.567   3.835   31.573  1.00 18.21 ? 178 TYR B CA  1 
ATOM   2883 C  C   . TYR B 1 190 ? 3.133   3.809   30.155  1.00 17.16 ? 178 TYR B C   1 
ATOM   2884 O  O   . TYR B 1 190 ? 2.702   2.968   29.311  1.00 17.54 ? 178 TYR B O   1 
ATOM   2885 C  CB  . TYR B 1 190 ? 2.973   2.568   32.334  1.00 22.73 ? 178 TYR B CB  1 
ATOM   2886 C  CG  . TYR B 1 190 ? 4.474   2.459   32.551  1.00 28.83 ? 178 TYR B CG  1 
ATOM   2887 C  CD1 . TYR B 1 190 ? 5.261   3.578   32.818  1.00 33.27 ? 178 TYR B CD1 1 
ATOM   2888 C  CD2 . TYR B 1 190 ? 5.112   1.228   32.515  1.00 37.40 ? 178 TYR B CD2 1 
ATOM   2889 C  CE1 . TYR B 1 190 ? 6.639   3.481   32.990  1.00 33.76 ? 178 TYR B CE1 1 
ATOM   2890 C  CE2 . TYR B 1 190 ? 6.482   1.108   32.725  1.00 38.87 ? 178 TYR B CE2 1 
ATOM   2891 C  CZ  . TYR B 1 190 ? 7.251   2.234   32.961  1.00 40.25 ? 178 TYR B CZ  1 
ATOM   2892 O  OH  . TYR B 1 190 ? 8.605   2.089   33.145  1.00 42.21 ? 178 TYR B OH  1 
ATOM   2893 N  N   . GLN B 1 191 ? 4.042   4.730   29.873  1.00 17.87 ? 179 GLN B N   1 
ATOM   2894 C  CA  . GLN B 1 191 ? 4.756   4.823   28.566  1.00 19.00 ? 179 GLN B CA  1 
ATOM   2895 C  C   . GLN B 1 191 ? 3.717   4.782   27.427  1.00 19.75 ? 179 GLN B C   1 
ATOM   2896 O  O   . GLN B 1 191 ? 3.850   3.951   26.502  1.00 17.24 ? 179 GLN B O   1 
ATOM   2897 C  CB  . GLN B 1 191 ? 5.801   3.710   28.485  1.00 21.15 ? 179 GLN B CB  1 
ATOM   2898 C  CG  . GLN B 1 191 ? 6.837   3.792   29.612  1.00 22.93 ? 179 GLN B CG  1 
ATOM   2899 C  CD  . GLN B 1 191 ? 8.244   3.378   29.237  1.00 27.83 ? 179 GLN B CD  1 
ATOM   2900 O  OE1 . GLN B 1 191 ? 8.459   2.278   28.726  1.00 32.67 ? 179 GLN B OE1 1 
ATOM   2901 N  NE2 . GLN B 1 191 ? 9.227   4.211   29.570  1.00 30.97 ? 179 GLN B NE2 1 
ATOM   2902 N  N   . SER B 1 192 ? 2.721   5.661   27.509  1.00 17.58 ? 180 SER B N   1 
ATOM   2903 C  CA  . SER B 1 192 ? 1.590   5.734   26.552  1.00 16.59 ? 180 SER B CA  1 
ATOM   2904 C  C   . SER B 1 192 ? 1.097   7.171   26.423  1.00 15.73 ? 180 SER B C   1 
ATOM   2905 O  O   . SER B 1 192 ? 1.632   8.060   27.085  1.00 16.38 ? 180 SER B O   1 
ATOM   2906 C  CB  . SER B 1 192 ? 0.476   4.805   26.951  1.00 16.76 ? 180 SER B CB  1 
ATOM   2907 O  OG  . SER B 1 192 ? -0.040  5.131   28.232  1.00 15.70 ? 180 SER B OG  1 
ATOM   2908 N  N   . SER B 1 193 ? 0.087   7.366   25.584  1.00 15.17 ? 181 SER B N   1 
ATOM   2909 C  CA  . SER B 1 193 ? -0.612  8.647   25.411  1.00 17.00 ? 181 SER B CA  1 
ATOM   2910 C  C   . SER B 1 193 ? -2.089  8.304   25.489  1.00 16.78 ? 181 SER B C   1 
ATOM   2911 O  O   . SER B 1 193 ? -2.451  7.105   25.344  1.00 16.78 ? 181 SER B O   1 
ATOM   2912 C  CB  . SER B 1 193 ? -0.254  9.280   24.116  1.00 17.42 ? 181 SER B CB  1 
ATOM   2913 O  OG  . SER B 1 193 ? 1.114   9.655   24.101  1.00 17.71 ? 181 SER B OG  1 
ATOM   2914 N  N   . GLY B 1 194 ? -2.901  9.303   25.727  1.00 15.54 ? 182 GLY B N   1 
ATOM   2915 C  CA  . GLY B 1 194 ? -4.343  9.104   25.590  1.00 17.18 ? 182 GLY B CA  1 
ATOM   2916 C  C   . GLY B 1 194 ? -5.132  10.130  26.330  1.00 17.45 ? 182 GLY B C   1 
ATOM   2917 O  O   . GLY B 1 194 ? -4.606  11.210  26.736  1.00 17.14 ? 182 GLY B O   1 
ATOM   2918 N  N   . SER B 1 195 ? -6.428  9.874   26.352  1.00 15.68 ? 183 SER B N   1 
ATOM   2919 C  CA  . SER B 1 195 ? -7.334  10.754  27.104  1.00 17.60 ? 183 SER B CA  1 
ATOM   2920 C  C   . SER B 1 195 ? -8.444  9.911   27.674  1.00 15.83 ? 183 SER B C   1 
ATOM   2921 O  O   . SER B 1 195 ? -8.709  8.801   27.150  1.00 16.66 ? 183 SER B O   1 
ATOM   2922 C  CB  . SER B 1 195 ? -7.876  11.860  26.265  1.00 18.74 ? 183 SER B CB  1 
ATOM   2923 O  OG  . SER B 1 195 ? -8.646  11.347  25.211  1.00 19.84 ? 183 SER B OG  1 
ATOM   2924 N  N   . ALA B 1 196 ? -9.047  10.432  28.729  1.00 16.49 ? 184 ALA B N   1 
ATOM   2925 C  CA  . ALA B 1 196 ? -10.183 9.768   29.376  1.00 16.23 ? 184 ALA B CA  1 
ATOM   2926 C  C   . ALA B 1 196 ? -11.035 10.825  30.048  1.00 15.65 ? 184 ALA B C   1 
ATOM   2927 O  O   . ALA B 1 196 ? -10.512 11.832  30.489  1.00 17.48 ? 184 ALA B O   1 
ATOM   2928 C  CB  . ALA B 1 196 ? -9.727  8.726   30.357  1.00 16.48 ? 184 ALA B CB  1 
ATOM   2929 N  N   . SER B 1 197 ? -12.321 10.566  30.111  1.00 15.01 ? 185 SER B N   1 
ATOM   2930 C  CA  . SER B 1 197 ? -13.268 11.466  30.776  1.00 18.24 ? 185 SER B CA  1 
ATOM   2931 C  C   . SER B 1 197 ? -14.284 10.570  31.444  1.00 16.62 ? 185 SER B C   1 
ATOM   2932 O  O   . SER B 1 197 ? -15.033 9.909   30.718  1.00 16.72 ? 185 SER B O   1 
ATOM   2933 C  CB  . SER B 1 197 ? -13.901 12.447  29.816  1.00 22.63 ? 185 SER B CB  1 
ATOM   2934 O  OG  . SER B 1 197 ? -14.782 13.336  30.490  1.00 25.21 ? 185 SER B OG  1 
ATOM   2935 N  N   . ILE B 1 198 ? -14.255 10.509  32.761  1.00 15.40 ? 186 ILE B N   1 
ATOM   2936 C  CA  . ILE B 1 198 ? -14.957 9.463   33.552  1.00 16.32 ? 186 ILE B CA  1 
ATOM   2937 C  C   . ILE B 1 198 ? -15.813 10.193  34.577  1.00 16.73 ? 186 ILE B C   1 
ATOM   2938 O  O   . ILE B 1 198 ? -15.317 11.105  35.206  1.00 17.39 ? 186 ILE B O   1 
ATOM   2939 C  CB  . ILE B 1 198 ? -13.957 8.502   34.246  1.00 19.35 ? 186 ILE B CB  1 
ATOM   2940 C  CG1 . ILE B 1 198 ? -13.155 7.661   33.247  1.00 20.45 ? 186 ILE B CG1 1 
ATOM   2941 C  CG2 . ILE B 1 198 ? -14.620 7.599   35.276  1.00 18.44 ? 186 ILE B CG2 1 
ATOM   2942 C  CD1 . ILE B 1 198 ? -13.998 6.733   32.398  1.00 19.39 ? 186 ILE B CD1 1 
ATOM   2943 N  N   . THR B 1 199 ? -17.052 9.781   34.715  1.00 16.01 ? 187 THR B N   1 
ATOM   2944 C  CA  . THR B 1 199 ? -17.982 10.352  35.721  1.00 17.21 ? 187 THR B CA  1 
ATOM   2945 C  C   . THR B 1 199 ? -18.395 9.244   36.679  1.00 17.91 ? 187 THR B C   1 
ATOM   2946 O  O   . THR B 1 199 ? -19.045 8.286   36.235  1.00 19.18 ? 187 THR B O   1 
ATOM   2947 C  CB  . THR B 1 199 ? -19.200 10.999  35.051  1.00 20.21 ? 187 THR B CB  1 
ATOM   2948 O  OG1 . THR B 1 199 ? -18.736 12.060  34.225  1.00 23.74 ? 187 THR B OG1 1 
ATOM   2949 C  CG2 . THR B 1 199 ? -20.182 11.528  36.081  1.00 20.49 ? 187 THR B CG2 1 
ATOM   2950 N  N   . VAL B 1 200 ? -18.014 9.364   37.959  1.00 17.30 ? 188 VAL B N   1 
ATOM   2951 C  CA  . VAL B 1 200 ? -18.445 8.399   38.990  1.00 18.65 ? 188 VAL B CA  1 
ATOM   2952 C  C   . VAL B 1 200 ? -19.828 8.893   39.445  1.00 21.99 ? 188 VAL B C   1 
ATOM   2953 O  O   . VAL B 1 200 ? -19.964 10.125  39.604  1.00 20.10 ? 188 VAL B O   1 
ATOM   2954 C  CB  . VAL B 1 200 ? -17.419 8.350   40.137  1.00 19.18 ? 188 VAL B CB  1 
ATOM   2955 C  CG1 . VAL B 1 200 ? -17.854 7.416   41.225  1.00 22.41 ? 188 VAL B CG1 1 
ATOM   2956 C  CG2 . VAL B 1 200 ? -16.040 8.010   39.606  1.00 19.79 ? 188 VAL B CG2 1 
ATOM   2957 N  N   . GLN B 1 201 ? -20.798 8.002   39.566  1.00 24.42 ? 189 GLN B N   1 
ATOM   2958 C  CA  . GLN B 1 201 ? -22.191 8.328   40.007  1.00 31.64 ? 189 GLN B CA  1 
ATOM   2959 C  C   . GLN B 1 201 ? -22.467 7.655   41.358  1.00 34.12 ? 189 GLN B C   1 
ATOM   2960 O  O   . GLN B 1 201 ? -21.555 7.540   42.193  1.00 37.61 ? 189 GLN B O   1 
ATOM   2961 C  CB  . GLN B 1 201 ? -23.227 7.847   38.995  1.00 35.80 ? 189 GLN B CB  1 
ATOM   2962 C  CG  . GLN B 1 201 ? -23.205 8.598   37.673  1.00 45.26 ? 189 GLN B CG  1 
ATOM   2963 C  CD  . GLN B 1 201 ? -22.621 7.802   36.532  1.00 47.43 ? 189 GLN B CD  1 
ATOM   2964 O  OE1 . GLN B 1 201 ? -22.806 6.590   36.429  1.00 55.59 ? 189 GLN B OE1 1 
ATOM   2965 N  NE2 . GLN B 1 201 ? -21.933 8.493   35.637  1.00 48.73 ? 189 GLN B NE2 1 
ATOM   2966 N  N   . GLU C 1 13  ? -0.228  54.456  34.075  1.00 49.19 ? 1   GLU C N   1 
ATOM   2967 C  CA  . GLU C 1 13  ? -0.209  55.715  33.285  1.00 42.73 ? 1   GLU C CA  1 
ATOM   2968 C  C   . GLU C 1 13  ? 1.037   55.770  32.398  1.00 38.51 ? 1   GLU C C   1 
ATOM   2969 O  O   . GLU C 1 13  ? 1.348   56.865  31.903  1.00 38.02 ? 1   GLU C O   1 
ATOM   2970 C  CB  . GLU C 1 13  ? -0.287  56.944  34.195  1.00 40.52 ? 1   GLU C CB  1 
ATOM   2971 C  CG  . GLU C 1 13  ? 0.795   57.030  35.254  1.00 42.72 ? 1   GLU C CG  1 
ATOM   2972 C  CD  . GLU C 1 13  ? 0.536   58.144  36.263  1.00 46.98 ? 1   GLU C CD  1 
ATOM   2973 O  OE1 . GLU C 1 13  ? 0.338   57.831  37.461  1.00 47.62 ? 1   GLU C OE1 1 
ATOM   2974 O  OE2 . GLU C 1 13  ? 0.525   59.324  35.850  1.00 48.42 ? 1   GLU C OE2 1 
ATOM   2975 N  N   . ILE C 1 14  ? 1.735   54.653  32.193  1.00 30.12 ? 2   ILE C N   1 
ATOM   2976 C  CA  . ILE C 1 14  ? 2.894   54.610  31.259  1.00 30.10 ? 2   ILE C CA  1 
ATOM   2977 C  C   . ILE C 1 14  ? 2.685   53.425  30.323  1.00 29.04 ? 2   ILE C C   1 
ATOM   2978 O  O   . ILE C 1 14  ? 2.198   52.366  30.810  1.00 25.15 ? 2   ILE C O   1 
ATOM   2979 C  CB  . ILE C 1 14  ? 4.230   54.574  32.019  1.00 35.11 ? 2   ILE C CB  1 
ATOM   2980 C  CG1 . ILE C 1 14  ? 4.632   53.168  32.453  1.00 37.30 ? 2   ILE C CG1 1 
ATOM   2981 C  CG2 . ILE C 1 14  ? 4.220   55.531  33.203  1.00 39.50 ? 2   ILE C CG2 1 
ATOM   2982 C  CD1 . ILE C 1 14  ? 6.095   53.042  32.735  1.00 39.14 ? 2   ILE C CD1 1 
ATOM   2983 N  N   . THR C 1 15  ? 2.979   53.616  29.033  1.00 25.67 ? 3   THR C N   1 
ATOM   2984 C  CA  . THR C 1 15  ? 2.642   52.640  27.959  1.00 25.59 ? 3   THR C CA  1 
ATOM   2985 C  C   . THR C 1 15  ? 3.870   52.297  27.108  1.00 24.95 ? 3   THR C C   1 
ATOM   2986 O  O   . THR C 1 15  ? 3.731   51.444  26.200  1.00 25.46 ? 3   THR C O   1 
ATOM   2987 C  CB  . THR C 1 15  ? 1.452   53.147  27.134  1.00 28.34 ? 3   THR C CB  1 
ATOM   2988 O  OG1 . THR C 1 15  ? 1.820   54.458  26.699  1.00 33.94 ? 3   THR C OG1 1 
ATOM   2989 C  CG2 . THR C 1 15  ? 0.164   53.204  27.929  1.00 30.65 ? 3   THR C CG2 1 
ATOM   2990 N  N   . SER C 1 16  ? 5.044   52.828  27.440  1.00 23.75 ? 4   SER C N   1 
ATOM   2991 C  CA  . SER C 1 16  ? 6.333   52.412  26.837  1.00 27.51 ? 4   SER C CA  1 
ATOM   2992 C  C   . SER C 1 16  ? 7.355   52.156  27.950  1.00 23.89 ? 4   SER C C   1 
ATOM   2993 O  O   . SER C 1 16  ? 7.182   52.690  29.073  1.00 23.50 ? 4   SER C O   1 
ATOM   2994 C  CB  . SER C 1 16  ? 6.820   53.419  25.841  1.00 31.36 ? 4   SER C CB  1 
ATOM   2995 O  OG  . SER C 1 16  ? 6.741   54.733  26.381  1.00 36.72 ? 4   SER C OG  1 
ATOM   2996 N  N   . SER C 1 17  ? 8.402   51.415  27.615  1.00 23.92 ? 5   SER C N   1 
ATOM   2997 C  CA  . SER C 1 17  ? 9.386   50.863  28.583  1.00 23.06 ? 5   SER C CA  1 
ATOM   2998 C  C   . SER C 1 17  ? 10.001  51.981  29.425  1.00 25.11 ? 5   SER C C   1 
ATOM   2999 O  O   . SER C 1 17  ? 10.353  53.043  28.879  1.00 23.85 ? 5   SER C O   1 
ATOM   3000 C  CB  . SER C 1 17  ? 10.436  50.066  27.899  1.00 22.81 ? 5   SER C CB  1 
ATOM   3001 O  OG  . SER C 1 17  ? 9.853   49.091  27.059  1.00 21.48 ? 5   SER C OG  1 
ATOM   3002 N  N   . GLU C 1 18  ? 10.145  51.735  30.720  1.00 22.13 ? 6   GLU C N   1 
ATOM   3003 C  CA  . GLU C 1 18  ? 10.685  52.733  31.672  1.00 25.19 ? 6   GLU C CA  1 
ATOM   3004 C  C   . GLU C 1 18  ? 11.199  51.967  32.889  1.00 23.43 ? 6   GLU C C   1 
ATOM   3005 O  O   . GLU C 1 18  ? 10.606  50.947  33.235  1.00 21.25 ? 6   GLU C O   1 
ATOM   3006 C  CB  . GLU C 1 18  ? 9.562   53.679  32.072  1.00 28.33 ? 6   GLU C CB  1 
ATOM   3007 C  CG  . GLU C 1 18  ? 9.968   54.895  32.860  1.00 32.91 ? 6   GLU C CG  1 
ATOM   3008 C  CD  . GLU C 1 18  ? 8.735   55.693  33.222  1.00 32.73 ? 6   GLU C CD  1 
ATOM   3009 O  OE1 . GLU C 1 18  ? 8.325   55.630  34.411  1.00 33.35 ? 6   GLU C OE1 1 
ATOM   3010 O  OE2 . GLU C 1 18  ? 8.140   56.325  32.296  1.00 35.05 ? 6   GLU C OE2 1 
ATOM   3011 N  N   . THR C 1 19  ? 12.249  52.483  33.517  1.00 23.88 ? 7   THR C N   1 
ATOM   3012 C  CA  . THR C 1 19  ? 12.677  52.049  34.865  1.00 20.78 ? 7   THR C CA  1 
ATOM   3013 C  C   . THR C 1 19  ? 12.759  53.282  35.757  1.00 21.10 ? 7   THR C C   1 
ATOM   3014 O  O   . THR C 1 19  ? 12.754  54.418  35.258  1.00 19.33 ? 7   THR C O   1 
ATOM   3015 C  CB  . THR C 1 19  ? 13.992  51.260  34.843  1.00 22.31 ? 7   THR C CB  1 
ATOM   3016 O  OG1 . THR C 1 19  ? 15.028  52.148  34.432  1.00 20.70 ? 7   THR C OG1 1 
ATOM   3017 C  CG2 . THR C 1 19  ? 13.957  50.065  33.915  1.00 22.06 ? 7   THR C CG2 1 
ATOM   3018 N  N   . GLY C 1 20  ? 12.808  53.051  37.059  1.00 19.29 ? 8   GLY C N   1 
ATOM   3019 C  CA  . GLY C 1 20  ? 12.973  54.138  38.025  1.00 18.75 ? 8   GLY C CA  1 
ATOM   3020 C  C   . GLY C 1 20  ? 12.836  53.630  39.433  1.00 17.96 ? 8   GLY C C   1 
ATOM   3021 O  O   . GLY C 1 20  ? 12.892  52.393  39.666  1.00 17.27 ? 8   GLY C O   1 
ATOM   3022 N  N   . THR C 1 21  ? 12.591  54.550  40.340  1.00 20.10 ? 9   THR C N   1 
ATOM   3023 C  CA  . THR C 1 21  ? 12.264  54.228  41.744  1.00 21.65 ? 9   THR C CA  1 
ATOM   3024 C  C   . THR C 1 21  ? 10.929  54.886  42.044  1.00 21.90 ? 9   THR C C   1 
ATOM   3025 O  O   . THR C 1 21  ? 10.686  56.037  41.579  1.00 23.63 ? 9   THR C O   1 
ATOM   3026 C  CB  . THR C 1 21  ? 13.462  54.569  42.650  1.00 27.38 ? 9   THR C CB  1 
ATOM   3027 O  OG1 . THR C 1 21  ? 13.071  54.473  44.020  1.00 33.00 ? 9   THR C OG1 1 
ATOM   3028 C  CG2 . THR C 1 21  ? 13.988  55.957  42.407  1.00 29.23 ? 9   THR C CG2 1 
ATOM   3029 N  N   . ASN C 1 22  ? 10.108  54.207  42.832  1.00 21.12 ? 10  ASN C N   1 
ATOM   3030 C  CA  . ASN C 1 22  ? 8.759   54.689  43.155  1.00 20.95 ? 10  ASN C CA  1 
ATOM   3031 C  C   . ASN C 1 22  ? 8.397   54.238  44.563  1.00 21.20 ? 10  ASN C C   1 
ATOM   3032 O  O   . ASN C 1 22  ? 8.386   53.023  44.812  1.00 21.64 ? 10  ASN C O   1 
ATOM   3033 C  CB  . ASN C 1 22  ? 7.736   54.282  42.102  1.00 21.49 ? 10  ASN C CB  1 
ATOM   3034 C  CG  . ASN C 1 22  ? 6.342   54.715  42.467  1.00 23.34 ? 10  ASN C CG  1 
ATOM   3035 O  OD1 . ASN C 1 22  ? 5.608   53.941  43.073  1.00 23.14 ? 10  ASN C OD1 1 
ATOM   3036 N  ND2 . ASN C 1 22  ? 5.966   55.935  42.084  1.00 24.55 ? 10  ASN C ND2 1 
ATOM   3037 N  N   . ASN C 1 23  ? 8.160   55.190  45.453  1.00 25.68 ? 11  ASN C N   1 
ATOM   3038 C  CA  . ASN C 1 23  ? 7.758   54.905  46.855  1.00 28.08 ? 11  ASN C CA  1 
ATOM   3039 C  C   . ASN C 1 23  ? 8.724   53.911  47.513  1.00 26.93 ? 11  ASN C C   1 
ATOM   3040 O  O   . ASN C 1 23  ? 8.257   53.076  48.292  1.00 28.80 ? 11  ASN C O   1 
ATOM   3041 C  CB  . ASN C 1 23  ? 6.303   54.438  46.866  1.00 27.91 ? 11  ASN C CB  1 
ATOM   3042 C  CG  . ASN C 1 23  ? 5.348   55.549  46.510  1.00 30.43 ? 11  ASN C CG  1 
ATOM   3043 O  OD1 . ASN C 1 23  ? 5.500   56.642  47.031  1.00 34.29 ? 11  ASN C OD1 1 
ATOM   3044 N  ND2 . ASN C 1 23  ? 4.385   55.310  45.630  1.00 29.62 ? 11  ASN C ND2 1 
ATOM   3045 N  N   . GLY C 1 24  ? 10.025  54.012  47.229  1.00 25.33 ? 12  GLY C N   1 
ATOM   3046 C  CA  . GLY C 1 24  ? 11.091  53.286  47.925  1.00 25.24 ? 12  GLY C CA  1 
ATOM   3047 C  C   . GLY C 1 24  ? 11.480  52.008  47.219  1.00 24.51 ? 12  GLY C C   1 
ATOM   3048 O  O   . GLY C 1 24  ? 12.381  51.352  47.689  1.00 28.87 ? 12  GLY C O   1 
ATOM   3049 N  N   . TYR C 1 25  ? 10.828  51.691  46.096  1.00 21.54 ? 13  TYR C N   1 
ATOM   3050 C  CA  . TYR C 1 25  ? 11.038  50.439  45.322  1.00 19.95 ? 13  TYR C CA  1 
ATOM   3051 C  C   . TYR C 1 25  ? 11.526  50.763  43.905  1.00 18.09 ? 13  TYR C C   1 
ATOM   3052 O  O   . TYR C 1 25  ? 10.951  51.620  43.230  1.00 20.55 ? 13  TYR C O   1 
ATOM   3053 C  CB  . TYR C 1 25  ? 9.728   49.671  45.201  1.00 21.03 ? 13  TYR C CB  1 
ATOM   3054 C  CG  . TYR C 1 25  ? 9.341   49.008  46.495  1.00 21.36 ? 13  TYR C CG  1 
ATOM   3055 C  CD1 . TYR C 1 25  ? 8.649   49.694  47.471  1.00 22.07 ? 13  TYR C CD1 1 
ATOM   3056 C  CD2 . TYR C 1 25  ? 9.735   47.706  46.760  1.00 22.66 ? 13  TYR C CD2 1 
ATOM   3057 C  CE1 . TYR C 1 25  ? 8.346   49.100  48.686  1.00 25.22 ? 13  TYR C CE1 1 
ATOM   3058 C  CE2 . TYR C 1 25  ? 9.449   47.097  47.964  1.00 26.76 ? 13  TYR C CE2 1 
ATOM   3059 C  CZ  . TYR C 1 25  ? 8.729   47.786  48.918  1.00 27.12 ? 13  TYR C CZ  1 
ATOM   3060 O  OH  . TYR C 1 25  ? 8.454   47.135  50.080  1.00 31.17 ? 13  TYR C OH  1 
ATOM   3061 N  N   . TYR C 1 26  ? 12.481  49.971  43.445  1.00 18.37 ? 14  TYR C N   1 
ATOM   3062 C  CA  . TYR C 1 26  ? 12.885  49.911  42.024  1.00 16.16 ? 14  TYR C CA  1 
ATOM   3063 C  C   . TYR C 1 26  ? 11.682  49.427  41.219  1.00 16.93 ? 14  TYR C C   1 
ATOM   3064 O  O   . TYR C 1 26  ? 10.990  48.504  41.681  1.00 16.67 ? 14  TYR C O   1 
ATOM   3065 C  CB  . TYR C 1 26  ? 14.038  48.949  41.811  1.00 17.29 ? 14  TYR C CB  1 
ATOM   3066 C  CG  . TYR C 1 26  ? 14.474  48.858  40.371  1.00 17.68 ? 14  TYR C CG  1 
ATOM   3067 C  CD1 . TYR C 1 26  ? 15.104  49.923  39.758  1.00 18.69 ? 14  TYR C CD1 1 
ATOM   3068 C  CD2 . TYR C 1 26  ? 14.269  47.708  39.626  1.00 19.71 ? 14  TYR C CD2 1 
ATOM   3069 C  CE1 . TYR C 1 26  ? 15.560  49.832  38.459  1.00 18.21 ? 14  TYR C CE1 1 
ATOM   3070 C  CE2 . TYR C 1 26  ? 14.660  47.629  38.300  1.00 18.88 ? 14  TYR C CE2 1 
ATOM   3071 C  CZ  . TYR C 1 26  ? 15.354  48.681  37.729  1.00 19.53 ? 14  TYR C CZ  1 
ATOM   3072 O  OH  . TYR C 1 26  ? 15.764  48.626  36.425  1.00 20.04 ? 14  TYR C OH  1 
ATOM   3073 N  N   . TYR C 1 27  ? 11.454  49.968  40.030  1.00 16.59 ? 15  TYR C N   1 
ATOM   3074 C  CA  . TYR C 1 27  ? 10.427  49.394  39.112  1.00 16.74 ? 15  TYR C CA  1 
ATOM   3075 C  C   . TYR C 1 27  ? 11.038  49.256  37.735  1.00 18.13 ? 15  TYR C C   1 
ATOM   3076 O  O   . TYR C 1 27  ? 11.905  50.084  37.369  1.00 17.52 ? 15  TYR C O   1 
ATOM   3077 C  CB  . TYR C 1 27  ? 9.107   50.159  39.068  1.00 17.37 ? 15  TYR C CB  1 
ATOM   3078 C  CG  . TYR C 1 27  ? 9.128   51.516  38.405  1.00 16.64 ? 15  TYR C CG  1 
ATOM   3079 C  CD1 . TYR C 1 27  ? 9.537   52.618  39.117  1.00 18.23 ? 15  TYR C CD1 1 
ATOM   3080 C  CD2 . TYR C 1 27  ? 8.815   51.688  37.058  1.00 18.96 ? 15  TYR C CD2 1 
ATOM   3081 C  CE1 . TYR C 1 27  ? 9.617   53.877  38.528  1.00 18.28 ? 15  TYR C CE1 1 
ATOM   3082 C  CE2 . TYR C 1 27  ? 8.841   52.949  36.471  1.00 20.56 ? 15  TYR C CE2 1 
ATOM   3083 C  CZ  . TYR C 1 27  ? 9.247   54.044  37.205  1.00 20.18 ? 15  TYR C CZ  1 
ATOM   3084 O  OH  . TYR C 1 27  ? 9.328   55.287  36.624  1.00 23.46 ? 15  TYR C OH  1 
ATOM   3085 N  N   . SER C 1 28  ? 10.653  48.185  37.038  1.00 15.89 ? 16  SER C N   1 
ATOM   3086 C  CA  . SER C 1 28  ? 11.015  47.977  35.621  1.00 16.31 ? 16  SER C CA  1 
ATOM   3087 C  C   . SER C 1 28  ? 9.735   47.696  34.844  1.00 18.24 ? 16  SER C C   1 
ATOM   3088 O  O   . SER C 1 28  ? 9.019   46.729  35.198  1.00 18.57 ? 16  SER C O   1 
ATOM   3089 C  CB  . SER C 1 28  ? 11.993  46.881  35.420  1.00 18.08 ? 16  SER C CB  1 
ATOM   3090 O  OG  . SER C 1 28  ? 12.355  46.755  34.033  1.00 17.62 ? 16  SER C OG  1 
ATOM   3091 N  N   . PHE C 1 29  ? 9.495   48.459  33.791  1.00 17.54 ? 17  PHE C N   1 
ATOM   3092 C  CA  . PHE C 1 29  ? 8.412   48.179  32.828  1.00 16.97 ? 17  PHE C CA  1 
ATOM   3093 C  C   . PHE C 1 29  ? 9.056   48.095  31.452  1.00 17.96 ? 17  PHE C C   1 
ATOM   3094 O  O   . PHE C 1 29  ? 9.687   49.069  31.010  1.00 18.29 ? 17  PHE C O   1 
ATOM   3095 C  CB  . PHE C 1 29  ? 7.283   49.193  32.929  1.00 17.77 ? 17  PHE C CB  1 
ATOM   3096 C  CG  . PHE C 1 29  ? 6.260   49.060  31.828  1.00 19.79 ? 17  PHE C CG  1 
ATOM   3097 C  CD1 . PHE C 1 29  ? 5.552   47.881  31.679  1.00 19.35 ? 17  PHE C CD1 1 
ATOM   3098 C  CD2 . PHE C 1 29  ? 6.045   50.070  30.903  1.00 21.32 ? 17  PHE C CD2 1 
ATOM   3099 C  CE1 . PHE C 1 29  ? 4.611   47.727  30.675  1.00 20.87 ? 17  PHE C CE1 1 
ATOM   3100 C  CE2 . PHE C 1 29  ? 5.112   49.909  29.884  1.00 21.49 ? 17  PHE C CE2 1 
ATOM   3101 C  CZ  . PHE C 1 29  ? 4.389   48.741  29.775  1.00 22.24 ? 17  PHE C CZ  1 
ATOM   3102 N  N   . TRP C 1 30  ? 8.981   46.917  30.851  1.00 18.89 ? 18  TRP C N   1 
ATOM   3103 C  CA  . TRP C 1 30  ? 9.485   46.704  29.476  1.00 18.38 ? 18  TRP C CA  1 
ATOM   3104 C  C   . TRP C 1 30  ? 8.328   46.172  28.633  1.00 19.68 ? 18  TRP C C   1 
ATOM   3105 O  O   . TRP C 1 30  ? 7.692   45.182  29.028  1.00 16.69 ? 18  TRP C O   1 
ATOM   3106 C  CB  . TRP C 1 30  ? 10.693  45.780  29.506  1.00 20.84 ? 18  TRP C CB  1 
ATOM   3107 C  CG  . TRP C 1 30  ? 11.210  45.529  28.130  1.00 23.08 ? 18  TRP C CG  1 
ATOM   3108 C  CD1 . TRP C 1 30  ? 12.011  46.359  27.405  1.00 22.73 ? 18  TRP C CD1 1 
ATOM   3109 C  CD2 . TRP C 1 30  ? 10.852  44.432  27.272  1.00 21.00 ? 18  TRP C CD2 1 
ATOM   3110 N  NE1 . TRP C 1 30  ? 12.215  45.830  26.159  1.00 24.59 ? 18  TRP C NE1 1 
ATOM   3111 C  CE2 . TRP C 1 30  ? 11.524  44.648  26.046  1.00 23.28 ? 18  TRP C CE2 1 
ATOM   3112 C  CE3 . TRP C 1 30  ? 10.063  43.286  27.426  1.00 23.96 ? 18  TRP C CE3 1 
ATOM   3113 C  CZ2 . TRP C 1 30  ? 11.378  43.778  24.963  1.00 24.41 ? 18  TRP C CZ2 1 
ATOM   3114 C  CZ3 . TRP C 1 30  ? 9.970   42.397  26.380  1.00 26.47 ? 18  TRP C CZ3 1 
ATOM   3115 C  CH2 . TRP C 1 30  ? 10.624  42.642  25.165  1.00 26.00 ? 18  TRP C CH2 1 
ATOM   3116 N  N   . THR C 1 31  ? 8.124   46.743  27.461  1.00 17.94 ? 19  THR C N   1 
ATOM   3117 C  CA  . THR C 1 31  ? 7.191   46.167  26.470  1.00 18.00 ? 19  THR C CA  1 
ATOM   3118 C  C   . THR C 1 31  ? 7.824   46.333  25.103  1.00 20.10 ? 19  THR C C   1 
ATOM   3119 O  O   . THR C 1 31  ? 8.496   47.379  24.885  1.00 22.49 ? 19  THR C O   1 
ATOM   3120 C  CB  . THR C 1 31  ? 5.806   46.800  26.546  1.00 18.44 ? 19  THR C CB  1 
ATOM   3121 O  OG1 . THR C 1 31  ? 5.047   46.339  25.423  1.00 19.94 ? 19  THR C OG1 1 
ATOM   3122 C  CG2 . THR C 1 31  ? 5.819   48.311  26.512  1.00 19.19 ? 19  THR C CG2 1 
ATOM   3123 N  N   . ASP C 1 32  ? 7.621   45.356  24.244  1.00 20.99 ? 20  ASP C N   1 
ATOM   3124 C  CA  . ASP C 1 32  ? 8.102   45.408  22.837  1.00 22.98 ? 20  ASP C CA  1 
ATOM   3125 C  C   . ASP C 1 32  ? 7.204   46.336  21.998  1.00 24.37 ? 20  ASP C C   1 
ATOM   3126 O  O   . ASP C 1 32  ? 7.560   46.528  20.828  1.00 26.00 ? 20  ASP C O   1 
ATOM   3127 C  CB  . ASP C 1 32  ? 8.233   43.990  22.261  1.00 22.85 ? 20  ASP C CB  1 
ATOM   3128 C  CG  . ASP C 1 32  ? 6.906   43.275  22.044  1.00 24.80 ? 20  ASP C CG  1 
ATOM   3129 O  OD1 . ASP C 1 32  ? 5.853   43.888  22.268  1.00 25.87 ? 20  ASP C OD1 1 
ATOM   3130 O  OD2 . ASP C 1 32  ? 6.932   42.115  21.642  1.00 27.60 ? 20  ASP C OD2 1 
ATOM   3131 N  N   . GLY C 1 33  ? 6.065   46.821  22.526  1.00 22.74 ? 21  GLY C N   1 
ATOM   3132 C  CA  . GLY C 1 33  ? 5.190   47.837  21.901  1.00 22.41 ? 21  GLY C CA  1 
ATOM   3133 C  C   . GLY C 1 33  ? 3.975   47.254  21.192  1.00 24.51 ? 21  GLY C C   1 
ATOM   3134 O  O   . GLY C 1 33  ? 3.132   48.037  20.711  1.00 26.05 ? 21  GLY C O   1 
ATOM   3135 N  N   . GLY C 1 34  ? 3.789   45.929  21.215  1.00 23.36 ? 22  GLY C N   1 
ATOM   3136 C  CA  . GLY C 1 34  ? 2.591   45.309  20.620  1.00 23.36 ? 22  GLY C CA  1 
ATOM   3137 C  C   . GLY C 1 34  ? 1.353   45.515  21.474  1.00 21.73 ? 22  GLY C C   1 
ATOM   3138 O  O   . GLY C 1 34  ? 1.489   45.603  22.699  1.00 23.30 ? 22  GLY C O   1 
ATOM   3139 N  N   . GLY C 1 35  ? 0.183   45.577  20.848  1.00 22.34 ? 23  GLY C N   1 
ATOM   3140 C  CA  . GLY C 1 35  ? -1.111  45.767  21.540  1.00 22.70 ? 23  GLY C CA  1 
ATOM   3141 C  C   . GLY C 1 35  ? -1.148  47.017  22.401  1.00 24.19 ? 23  GLY C C   1 
ATOM   3142 O  O   . GLY C 1 35  ? -0.510  48.032  22.056  1.00 23.42 ? 23  GLY C O   1 
ATOM   3143 N  N   . GLN C 1 36  ? -1.855  46.948  23.529  1.00 25.05 ? 24  GLN C N   1 
ATOM   3144 C  CA  . GLN C 1 36  ? -1.823  48.012  24.563  1.00 27.06 ? 24  GLN C CA  1 
ATOM   3145 C  C   . GLN C 1 36  ? -1.458  47.340  25.884  1.00 23.84 ? 24  GLN C C   1 
ATOM   3146 O  O   . GLN C 1 36  ? -2.022  46.267  26.168  1.00 25.23 ? 24  GLN C O   1 
ATOM   3147 C  CB  . GLN C 1 36  ? -3.135  48.798  24.628  1.00 34.74 ? 24  GLN C CB  1 
ATOM   3148 C  CG  . GLN C 1 36  ? -2.997  50.119  25.377  1.00 43.77 ? 24  GLN C CG  1 
ATOM   3149 C  CD  . GLN C 1 36  ? -3.687  51.272  24.682  1.00 49.19 ? 24  GLN C CD  1 
ATOM   3150 O  OE1 . GLN C 1 36  ? -3.159  51.860  23.737  1.00 55.98 ? 24  GLN C OE1 1 
ATOM   3151 N  NE2 . GLN C 1 36  ? -4.884  51.600  25.144  1.00 51.52 ? 24  GLN C NE2 1 
ATOM   3152 N  N   . VAL C 1 37  ? -0.425  47.865  26.528  1.00 21.00 ? 25  VAL C N   1 
ATOM   3153 C  CA  . VAL C 1 37  ? 0.085   47.461  27.866  1.00 21.24 ? 25  VAL C CA  1 
ATOM   3154 C  C   . VAL C 1 37  ? 0.226   48.776  28.643  1.00 22.71 ? 25  VAL C C   1 
ATOM   3155 O  O   . VAL C 1 37  ? 0.953   49.652  28.157  1.00 23.71 ? 25  VAL C O   1 
ATOM   3156 C  CB  . VAL C 1 37  ? 1.418   46.691  27.756  1.00 21.38 ? 25  VAL C CB  1 
ATOM   3157 C  CG1 . VAL C 1 37  ? 1.934   46.262  29.126  1.00 22.33 ? 25  VAL C CG1 1 
ATOM   3158 C  CG2 . VAL C 1 37  ? 1.326   45.459  26.866  1.00 21.76 ? 25  VAL C CG2 1 
ATOM   3159 N  N   . THR C 1 38  ? -0.491  48.927  29.759  1.00 20.89 ? 26  THR C N   1 
ATOM   3160 C  CA  . THR C 1 38  ? -0.570  50.160  30.563  1.00 20.72 ? 26  THR C CA  1 
ATOM   3161 C  C   . THR C 1 38  ? -0.111  49.792  31.970  1.00 20.55 ? 26  THR C C   1 
ATOM   3162 O  O   . THR C 1 38  ? -0.765  48.976  32.568  1.00 21.06 ? 26  THR C O   1 
ATOM   3163 C  CB  . THR C 1 38  ? -1.996  50.742  30.555  1.00 24.54 ? 26  THR C CB  1 
ATOM   3164 O  OG1 . THR C 1 38  ? -2.389  51.018  29.201  1.00 24.64 ? 26  THR C OG1 1 
ATOM   3165 C  CG2 . THR C 1 38  ? -2.127  52.024  31.356  1.00 27.12 ? 26  THR C CG2 1 
ATOM   3166 N  N   . TYR C 1 39  ? 1.017   50.325  32.406  1.00 18.28 ? 27  TYR C N   1 
ATOM   3167 C  CA  . TYR C 1 39  ? 1.630   50.096  33.733  1.00 17.21 ? 27  TYR C CA  1 
ATOM   3168 C  C   . TYR C 1 39  ? 1.345   51.285  34.638  1.00 20.76 ? 27  TYR C C   1 
ATOM   3169 O  O   . TYR C 1 39  ? 1.511   52.423  34.176  1.00 19.43 ? 27  TYR C O   1 
ATOM   3170 C  CB  . TYR C 1 39  ? 3.135   49.941  33.543  1.00 17.17 ? 27  TYR C CB  1 
ATOM   3171 C  CG  . TYR C 1 39  ? 3.900   49.804  34.838  1.00 18.55 ? 27  TYR C CG  1 
ATOM   3172 C  CD1 . TYR C 1 39  ? 4.061   48.565  35.412  1.00 15.43 ? 27  TYR C CD1 1 
ATOM   3173 C  CD2 . TYR C 1 39  ? 4.404   50.894  35.515  1.00 18.32 ? 27  TYR C CD2 1 
ATOM   3174 C  CE1 . TYR C 1 39  ? 4.761   48.388  36.590  1.00 18.85 ? 27  TYR C CE1 1 
ATOM   3175 C  CE2 . TYR C 1 39  ? 5.071   50.747  36.726  1.00 18.87 ? 27  TYR C CE2 1 
ATOM   3176 C  CZ  . TYR C 1 39  ? 5.294   49.472  37.246  1.00 17.94 ? 27  TYR C CZ  1 
ATOM   3177 O  OH  . TYR C 1 39  ? 5.949   49.278  38.431  1.00 19.39 ? 27  TYR C OH  1 
ATOM   3178 N  N   . THR C 1 40  ? 1.000   51.040  35.901  1.00 20.82 ? 28  THR C N   1 
ATOM   3179 C  CA  . THR C 1 40  ? 0.766   52.117  36.889  1.00 22.48 ? 28  THR C CA  1 
ATOM   3180 C  C   . THR C 1 40  ? 1.512   51.768  38.174  1.00 22.16 ? 28  THR C C   1 
ATOM   3181 O  O   . THR C 1 40  ? 1.285   50.661  38.674  1.00 25.27 ? 28  THR C O   1 
ATOM   3182 C  CB  . THR C 1 40  ? -0.733  52.327  37.157  1.00 26.90 ? 28  THR C CB  1 
ATOM   3183 O  OG1 . THR C 1 40  ? -1.446  52.454  35.926  1.00 30.13 ? 28  THR C OG1 1 
ATOM   3184 C  CG2 . THR C 1 40  ? -1.004  53.572  37.966  1.00 29.96 ? 28  THR C CG2 1 
ATOM   3185 N  N   . ASN C 1 41  ? 2.325   52.693  38.685  1.00 21.01 ? 29  ASN C N   1 
ATOM   3186 C  CA  . ASN C 1 41  ? 2.879   52.621  40.060  1.00 20.72 ? 29  ASN C CA  1 
ATOM   3187 C  C   . ASN C 1 41  ? 1.802   53.005  41.070  1.00 23.04 ? 29  ASN C C   1 
ATOM   3188 O  O   . ASN C 1 41  ? 1.059   53.997  40.838  1.00 27.16 ? 29  ASN C O   1 
ATOM   3189 C  CB  . ASN C 1 41  ? 4.140   53.452  40.263  1.00 20.46 ? 29  ASN C CB  1 
ATOM   3190 C  CG  . ASN C 1 41  ? 5.355   52.803  39.632  1.00 19.36 ? 29  ASN C CG  1 
ATOM   3191 O  OD1 . ASN C 1 41  ? 5.540   51.592  39.771  1.00 19.76 ? 29  ASN C OD1 1 
ATOM   3192 N  ND2 . ASN C 1 41  ? 6.185   53.579  38.971  1.00 21.48 ? 29  ASN C ND2 1 
ATOM   3193 N  N   . GLY C 1 42  ? 1.773   52.247  42.151  1.00 21.85 ? 30  GLY C N   1 
ATOM   3194 C  CA  . GLY C 1 42  ? 0.887   52.498  43.292  1.00 24.05 ? 30  GLY C CA  1 
ATOM   3195 C  C   . GLY C 1 42  ? 1.682   52.787  44.545  1.00 23.10 ? 30  GLY C C   1 
ATOM   3196 O  O   . GLY C 1 42  ? 2.911   52.812  44.559  1.00 24.87 ? 30  GLY C O   1 
ATOM   3197 N  N   . PRO C 1 43  ? 0.959   52.919  45.666  1.00 23.72 ? 31  PRO C N   1 
ATOM   3198 C  CA  . PRO C 1 43  ? 1.587   53.170  46.961  1.00 25.96 ? 31  PRO C CA  1 
ATOM   3199 C  C   . PRO C 1 43  ? 2.537   52.042  47.392  1.00 26.03 ? 31  PRO C C   1 
ATOM   3200 O  O   . PRO C 1 43  ? 2.234   50.892  47.092  1.00 23.04 ? 31  PRO C O   1 
ATOM   3201 C  CB  . PRO C 1 43  ? 0.381   53.265  47.919  1.00 25.77 ? 31  PRO C CB  1 
ATOM   3202 C  CG  . PRO C 1 43  ? -0.826  53.453  47.052  1.00 26.63 ? 31  PRO C CG  1 
ATOM   3203 C  CD  . PRO C 1 43  ? -0.510  52.841  45.709  1.00 26.22 ? 31  PRO C CD  1 
ATOM   3204 N  N   . ALA C 1 44  ? 3.665   52.404  48.021  1.00 26.83 ? 32  ALA C N   1 
ATOM   3205 C  CA  . ALA C 1 44  ? 4.715   51.499  48.558  1.00 25.94 ? 32  ALA C CA  1 
ATOM   3206 C  C   . ALA C 1 44  ? 5.131   50.503  47.468  1.00 22.85 ? 32  ALA C C   1 
ATOM   3207 O  O   . ALA C 1 44  ? 5.562   50.955  46.401  1.00 21.40 ? 32  ALA C O   1 
ATOM   3208 C  CB  . ALA C 1 44  ? 4.248   50.833  49.832  1.00 29.07 ? 32  ALA C CB  1 
ATOM   3209 N  N   . GLY C 1 45  ? 4.982   49.192  47.686  1.00 24.81 ? 33  GLY C N   1 
ATOM   3210 C  CA  . GLY C 1 45  ? 5.486   48.186  46.732  1.00 20.14 ? 33  GLY C CA  1 
ATOM   3211 C  C   . GLY C 1 45  ? 4.440   47.800  45.693  1.00 21.33 ? 33  GLY C C   1 
ATOM   3212 O  O   . GLY C 1 45  ? 4.599   46.732  45.118  1.00 18.63 ? 33  GLY C O   1 
ATOM   3213 N  N   . GLN C 1 46  ? 3.392   48.599  45.481  1.00 19.45 ? 34  GLN C N   1 
ATOM   3214 C  CA  . GLN C 1 46  ? 2.262   48.187  44.616  1.00 19.47 ? 34  GLN C CA  1 
ATOM   3215 C  C   . GLN C 1 46  ? 2.503   48.627  43.181  1.00 19.43 ? 34  GLN C C   1 
ATOM   3216 O  O   . GLN C 1 46  ? 2.861   49.803  42.933  1.00 17.44 ? 34  GLN C O   1 
ATOM   3217 C  CB  . GLN C 1 46  ? 0.929   48.750  45.105  1.00 21.10 ? 34  GLN C CB  1 
ATOM   3218 C  CG  . GLN C 1 46  ? -0.298  48.087  44.473  1.00 24.24 ? 34  GLN C CG  1 
ATOM   3219 C  CD  . GLN C 1 46  ? -0.817  48.693  43.192  1.00 30.07 ? 34  GLN C CD  1 
ATOM   3220 O  OE1 . GLN C 1 46  ? -0.380  49.750  42.739  1.00 36.18 ? 34  GLN C OE1 1 
ATOM   3221 N  NE2 . GLN C 1 46  ? -1.774  48.013  42.580  1.00 35.32 ? 34  GLN C NE2 1 
ATOM   3222 N  N   . TYR C 1 47  ? 2.144   47.775  42.234  1.00 17.47 ? 35  TYR C N   1 
ATOM   3223 C  CA  . TYR C 1 47  ? 1.986   48.198  40.834  1.00 16.66 ? 35  TYR C CA  1 
ATOM   3224 C  C   . TYR C 1 47  ? 0.784   47.475  40.254  1.00 17.79 ? 35  TYR C C   1 
ATOM   3225 O  O   . TYR C 1 47  ? 0.361   46.410  40.752  1.00 17.10 ? 35  TYR C O   1 
ATOM   3226 C  CB  . TYR C 1 47  ? 3.267   47.924  40.040  1.00 16.11 ? 35  TYR C CB  1 
ATOM   3227 C  CG  . TYR C 1 47  ? 3.501   46.460  39.785  1.00 15.24 ? 35  TYR C CG  1 
ATOM   3228 C  CD1 . TYR C 1 47  ? 4.150   45.676  40.719  1.00 13.78 ? 35  TYR C CD1 1 
ATOM   3229 C  CD2 . TYR C 1 47  ? 3.060   45.848  38.620  1.00 15.19 ? 35  TYR C CD2 1 
ATOM   3230 C  CE1 . TYR C 1 47  ? 4.354   44.317  40.488  1.00 13.72 ? 35  TYR C CE1 1 
ATOM   3231 C  CE2 . TYR C 1 47  ? 3.263   44.494  38.378  1.00 15.12 ? 35  TYR C CE2 1 
ATOM   3232 C  CZ  . TYR C 1 47  ? 3.936   43.730  39.302  1.00 14.66 ? 35  TYR C CZ  1 
ATOM   3233 O  OH  . TYR C 1 47  ? 4.151   42.366  39.123  1.00 15.77 ? 35  TYR C OH  1 
ATOM   3234 N  N   . SER C 1 48  ? 0.280   48.018  39.164  1.00 19.68 ? 36  SER C N   1 
ATOM   3235 C  CA  . SER C 1 48  ? -0.744  47.378  38.329  1.00 21.21 ? 36  SER C CA  1 
ATOM   3236 C  C   . SER C 1 48  ? -0.318  47.434  36.862  1.00 19.64 ? 36  SER C C   1 
ATOM   3237 O  O   . SER C 1 48  ? 0.381   48.381  36.424  1.00 21.09 ? 36  SER C O   1 
ATOM   3238 C  CB  . SER C 1 48  ? -2.120  47.963  38.554  1.00 26.12 ? 36  SER C CB  1 
ATOM   3239 O  OG  . SER C 1 48  ? -2.164  49.318  38.129  1.00 34.26 ? 36  SER C OG  1 
ATOM   3240 N  N   . VAL C 1 49  ? -0.800  46.474  36.111  1.00 20.99 ? 37  VAL C N   1 
ATOM   3241 C  CA  . VAL C 1 49  ? -0.650  46.477  34.641  1.00 20.86 ? 37  VAL C CA  1 
ATOM   3242 C  C   . VAL C 1 49  ? -1.952  45.967  34.032  1.00 21.81 ? 37  VAL C C   1 
ATOM   3243 O  O   . VAL C 1 49  ? -2.587  45.042  34.598  1.00 20.94 ? 37  VAL C O   1 
ATOM   3244 C  CB  . VAL C 1 49  ? 0.608   45.703  34.237  1.00 24.59 ? 37  VAL C CB  1 
ATOM   3245 C  CG1 . VAL C 1 49  ? 0.636   44.300  34.824  1.00 22.63 ? 37  VAL C CG1 1 
ATOM   3246 C  CG2 . VAL C 1 49  ? 0.791   45.713  32.734  1.00 24.71 ? 37  VAL C CG2 1 
ATOM   3247 N  N   . GLU C 1 50  ? -2.377  46.618  32.956  1.00 19.82 ? 38  GLU C N   1 
ATOM   3248 C  CA  . GLU C 1 50  ? -3.611  46.263  32.225  1.00 23.52 ? 38  GLU C CA  1 
ATOM   3249 C  C   . GLU C 1 50  ? -3.152  46.050  30.789  1.00 21.31 ? 38  GLU C C   1 
ATOM   3250 O  O   . GLU C 1 50  ? -2.361  46.894  30.331  1.00 19.95 ? 38  GLU C O   1 
ATOM   3251 C  CB  . GLU C 1 50  ? -4.658  47.359  32.416  1.00 26.08 ? 38  GLU C CB  1 
ATOM   3252 C  CG  . GLU C 1 50  ? -5.951  47.102  31.671  1.00 33.35 ? 38  GLU C CG  1 
ATOM   3253 C  CD  . GLU C 1 50  ? -7.228  47.474  32.412  1.00 40.19 ? 38  GLU C CD  1 
ATOM   3254 O  OE1 . GLU C 1 50  ? -7.317  47.233  33.652  1.00 44.49 ? 38  GLU C OE1 1 
ATOM   3255 O  OE2 . GLU C 1 50  ? -8.150  47.977  31.744  1.00 49.06 ? 38  GLU C OE2 1 
ATOM   3256 N  N   . TRP C 1 51  ? -3.471  44.909  30.172  1.00 19.25 ? 39  TRP C N   1 
ATOM   3257 C  CA  . TRP C 1 51  ? -2.991  44.664  28.787  1.00 19.14 ? 39  TRP C CA  1 
ATOM   3258 C  C   . TRP C 1 51  ? -4.088  44.080  27.895  1.00 20.81 ? 39  TRP C C   1 
ATOM   3259 O  O   . TRP C 1 51  ? -5.003  43.377  28.375  1.00 20.35 ? 39  TRP C O   1 
ATOM   3260 C  CB  . TRP C 1 51  ? -1.705  43.835  28.751  1.00 17.93 ? 39  TRP C CB  1 
ATOM   3261 C  CG  . TRP C 1 51  ? -1.777  42.418  29.205  1.00 17.14 ? 39  TRP C CG  1 
ATOM   3262 C  CD1 . TRP C 1 51  ? -1.766  41.326  28.403  1.00 18.21 ? 39  TRP C CD1 1 
ATOM   3263 C  CD2 . TRP C 1 51  ? -1.761  41.920  30.558  1.00 17.90 ? 39  TRP C CD2 1 
ATOM   3264 N  NE1 . TRP C 1 51  ? -1.761  40.182  29.153  1.00 17.69 ? 39  TRP C NE1 1 
ATOM   3265 C  CE2 . TRP C 1 51  ? -1.796  40.514  30.477  1.00 17.20 ? 39  TRP C CE2 1 
ATOM   3266 C  CE3 . TRP C 1 51  ? -1.730  42.522  31.822  1.00 17.34 ? 39  TRP C CE3 1 
ATOM   3267 C  CZ2 . TRP C 1 51  ? -1.736  39.695  31.607  1.00 19.13 ? 39  TRP C CZ2 1 
ATOM   3268 C  CZ3 . TRP C 1 51  ? -1.760  41.718  32.943  1.00 18.16 ? 39  TRP C CZ3 1 
ATOM   3269 C  CH2 . TRP C 1 51  ? -1.715  40.321  32.839  1.00 17.13 ? 39  TRP C CH2 1 
ATOM   3270 N  N   . SER C 1 52  ? -3.967  44.356  26.603  1.00 20.65 ? 40  SER C N   1 
ATOM   3271 C  CA  . SER C 1 52  ? -4.960  43.947  25.592  1.00 21.39 ? 40  SER C CA  1 
ATOM   3272 C  C   . SER C 1 52  ? -4.203  43.562  24.325  1.00 22.15 ? 40  SER C C   1 
ATOM   3273 O  O   . SER C 1 52  ? -3.541  44.424  23.764  1.00 20.34 ? 40  SER C O   1 
ATOM   3274 C  CB  . SER C 1 52  ? -5.960  45.042  25.333  1.00 23.59 ? 40  SER C CB  1 
ATOM   3275 O  OG  . SER C 1 52  ? -6.905  44.621  24.370  1.00 27.68 ? 40  SER C OG  1 
ATOM   3276 N  N   . ASN C 1 53  ? -4.282  42.295  23.920  1.00 18.98 ? 41  ASN C N   1 
ATOM   3277 C  CA  . ASN C 1 53  ? -3.694  41.813  22.640  1.00 19.41 ? 41  ASN C CA  1 
ATOM   3278 C  C   . ASN C 1 53  ? -2.230  42.210  22.574  1.00 17.06 ? 41  ASN C C   1 
ATOM   3279 O  O   . ASN C 1 53  ? -1.753  42.644  21.465  1.00 17.97 ? 41  ASN C O   1 
ATOM   3280 C  CB  . ASN C 1 53  ? -4.501  42.329  21.449  1.00 20.46 ? 41  ASN C CB  1 
ATOM   3281 C  CG  . ASN C 1 53  ? -5.873  41.705  21.398  1.00 24.51 ? 41  ASN C CG  1 
ATOM   3282 O  OD1 . ASN C 1 53  ? -6.005  40.500  21.560  1.00 22.85 ? 41  ASN C OD1 1 
ATOM   3283 N  ND2 . ASN C 1 53  ? -6.880  42.491  21.078  1.00 27.59 ? 41  ASN C ND2 1 
ATOM   3284 N  N   . SER C 1 54  ? -1.533  42.024  23.690  1.00 16.96 ? 42  SER C N   1 
ATOM   3285 C  CA  . SER C 1 54  ? -0.123  42.427  23.881  1.00 17.72 ? 42  SER C CA  1 
ATOM   3286 C  C   . SER C 1 54  ? 0.839   41.722  22.913  1.00 16.79 ? 42  SER C C   1 
ATOM   3287 O  O   . SER C 1 54  ? 0.605   40.546  22.484  1.00 17.85 ? 42  SER C O   1 
ATOM   3288 C  CB  . SER C 1 54  ? 0.305   42.235  25.330  1.00 17.58 ? 42  SER C CB  1 
ATOM   3289 O  OG  . SER C 1 54  ? 0.540   40.874  25.625  1.00 17.64 ? 42  SER C OG  1 
ATOM   3290 N  N   . GLY C 1 55  ? 1.995   42.349  22.695  1.00 18.34 ? 43  GLY C N   1 
ATOM   3291 C  CA  . GLY C 1 55  ? 3.233   41.637  22.389  1.00 18.62 ? 43  GLY C CA  1 
ATOM   3292 C  C   . GLY C 1 55  ? 3.839   41.084  23.654  1.00 19.93 ? 43  GLY C C   1 
ATOM   3293 O  O   . GLY C 1 55  ? 3.083   40.741  24.577  1.00 20.61 ? 43  GLY C O   1 
ATOM   3294 N  N   . ASN C 1 56  ? 5.156   41.051  23.717  1.00 19.81 ? 44  ASN C N   1 
ATOM   3295 C  CA  . ASN C 1 56  ? 5.907   40.670  24.930  1.00 22.06 ? 44  ASN C CA  1 
ATOM   3296 C  C   . ASN C 1 56  ? 5.961   41.857  25.900  1.00 19.51 ? 44  ASN C C   1 
ATOM   3297 O  O   . ASN C 1 56  ? 6.283   42.968  25.475  1.00 18.28 ? 44  ASN C O   1 
ATOM   3298 C  CB  . ASN C 1 56  ? 7.332   40.274  24.572  1.00 24.48 ? 44  ASN C CB  1 
ATOM   3299 C  CG  . ASN C 1 56  ? 7.454   38.854  24.057  1.00 32.05 ? 44  ASN C CG  1 
ATOM   3300 O  OD1 . ASN C 1 56  ? 7.836   38.647  22.902  1.00 36.03 ? 44  ASN C OD1 1 
ATOM   3301 N  ND2 . ASN C 1 56  ? 7.195   37.883  24.918  1.00 37.02 ? 44  ASN C ND2 1 
ATOM   3302 N  N   . PHE C 1 57  ? 5.719   41.627  27.196  1.00 19.79 ? 45  PHE C N   1 
ATOM   3303 C  CA  . PHE C 1 57  ? 5.980   42.656  28.229  1.00 17.55 ? 45  PHE C CA  1 
ATOM   3304 C  C   . PHE C 1 57  ? 6.365   41.975  29.542  1.00 16.69 ? 45  PHE C C   1 
ATOM   3305 O  O   . PHE C 1 57  ? 6.031   40.797  29.739  1.00 14.89 ? 45  PHE C O   1 
ATOM   3306 C  CB  . PHE C 1 57  ? 4.798   43.603  28.412  1.00 17.29 ? 45  PHE C CB  1 
ATOM   3307 C  CG  . PHE C 1 57  ? 3.655   42.975  29.160  1.00 18.13 ? 45  PHE C CG  1 
ATOM   3308 C  CD1 . PHE C 1 57  ? 3.629   43.007  30.553  1.00 17.51 ? 45  PHE C CD1 1 
ATOM   3309 C  CD2 . PHE C 1 57  ? 2.639   42.316  28.477  1.00 17.67 ? 45  PHE C CD2 1 
ATOM   3310 C  CE1 . PHE C 1 57  ? 2.565   42.435  31.241  1.00 18.27 ? 45  PHE C CE1 1 
ATOM   3311 C  CE2 . PHE C 1 57  ? 1.586   41.747  29.172  1.00 18.72 ? 45  PHE C CE2 1 
ATOM   3312 C  CZ  . PHE C 1 57  ? 1.561   41.795  30.550  1.00 18.31 ? 45  PHE C CZ  1 
ATOM   3313 N  N   . VAL C 1 58  ? 7.143   42.664  30.363  1.00 16.13 ? 46  VAL C N   1 
ATOM   3314 C  CA  . VAL C 1 58  ? 7.511   42.220  31.736  1.00 17.99 ? 46  VAL C CA  1 
ATOM   3315 C  C   . VAL C 1 58  ? 7.506   43.470  32.604  1.00 20.31 ? 46  VAL C C   1 
ATOM   3316 O  O   . VAL C 1 58  ? 8.155   44.439  32.220  1.00 21.47 ? 46  VAL C O   1 
ATOM   3317 C  CB  . VAL C 1 58  ? 8.905   41.562  31.760  1.00 22.29 ? 46  VAL C CB  1 
ATOM   3318 C  CG1 . VAL C 1 58  ? 9.265   41.063  33.151  1.00 23.82 ? 46  VAL C CG1 1 
ATOM   3319 C  CG2 . VAL C 1 58  ? 9.039   40.468  30.725  1.00 24.14 ? 46  VAL C CG2 1 
ATOM   3320 N  N   . ALA C 1 59  ? 6.800   43.462  33.733  1.00 16.83 ? 47  ALA C N   1 
ATOM   3321 C  CA  . ALA C 1 59  ? 6.654   44.675  34.563  1.00 18.77 ? 47  ALA C CA  1 
ATOM   3322 C  C   . ALA C 1 59  ? 6.661   44.239  36.016  1.00 16.77 ? 47  ALA C C   1 
ATOM   3323 O  O   . ALA C 1 59  ? 5.981   43.227  36.319  1.00 17.56 ? 47  ALA C O   1 
ATOM   3324 C  CB  . ALA C 1 59  ? 5.356   45.372  34.300  1.00 20.23 ? 47  ALA C CB  1 
ATOM   3325 N  N   . GLY C 1 60  ? 7.323   45.011  36.861  1.00 15.32 ? 48  GLY C N   1 
ATOM   3326 C  CA  . GLY C 1 60  ? 7.096   44.899  38.304  1.00 15.72 ? 48  GLY C CA  1 
ATOM   3327 C  C   . GLY C 1 60  ? 7.999   45.765  39.157  1.00 16.37 ? 48  GLY C C   1 
ATOM   3328 O  O   . GLY C 1 60  ? 8.783   46.536  38.625  1.00 16.16 ? 48  GLY C O   1 
ATOM   3329 N  N   . LYS C 1 61  ? 7.855   45.608  40.467  1.00 16.01 ? 49  LYS C N   1 
ATOM   3330 C  CA  . LYS C 1 61  ? 8.651   46.289  41.512  1.00 16.78 ? 49  LYS C CA  1 
ATOM   3331 C  C   . LYS C 1 61  ? 9.581   45.338  42.256  1.00 16.07 ? 49  LYS C C   1 
ATOM   3332 O  O   . LYS C 1 61  ? 9.300   44.131  42.397  1.00 15.02 ? 49  LYS C O   1 
ATOM   3333 C  CB  . LYS C 1 61  ? 7.753   46.987  42.532  1.00 17.00 ? 49  LYS C CB  1 
ATOM   3334 C  CG  . LYS C 1 61  ? 7.244   48.337  42.071  1.00 17.94 ? 49  LYS C CG  1 
ATOM   3335 C  CD  . LYS C 1 61  ? 6.372   49.024  43.075  1.00 17.52 ? 49  LYS C CD  1 
ATOM   3336 C  CE  . LYS C 1 61  ? 6.323   50.524  42.827  1.00 17.54 ? 49  LYS C CE  1 
ATOM   3337 N  NZ  . LYS C 1 61  ? 5.299   51.202  43.676  1.00 19.61 ? 49  LYS C NZ  1 
ATOM   3338 N  N   . GLY C 1 62  ? 10.689  45.887  42.749  1.00 16.48 ? 50  GLY C N   1 
ATOM   3339 C  CA  . GLY C 1 62  ? 11.616  45.177  43.644  1.00 16.82 ? 50  GLY C CA  1 
ATOM   3340 C  C   . GLY C 1 62  ? 12.850  46.023  43.898  1.00 17.47 ? 50  GLY C C   1 
ATOM   3341 O  O   . GLY C 1 62  ? 12.696  47.142  44.480  1.00 16.72 ? 50  GLY C O   1 
ATOM   3342 N  N   . TRP C 1 63  ? 14.003  45.548  43.426  1.00 17.11 ? 51  TRP C N   1 
ATOM   3343 C  CA  . TRP C 1 63  ? 15.323  46.064  43.868  1.00 18.26 ? 51  TRP C CA  1 
ATOM   3344 C  C   . TRP C 1 63  ? 16.288  46.095  42.712  1.00 19.69 ? 51  TRP C C   1 
ATOM   3345 O  O   . TRP C 1 63  ? 16.261  45.171  41.909  1.00 17.56 ? 51  TRP C O   1 
ATOM   3346 C  CB  . TRP C 1 63  ? 15.914  45.257  45.008  1.00 20.17 ? 51  TRP C CB  1 
ATOM   3347 C  CG  . TRP C 1 63  ? 14.960  45.172  46.151  1.00 22.45 ? 51  TRP C CG  1 
ATOM   3348 C  CD1 . TRP C 1 63  ? 14.879  46.034  47.200  1.00 22.31 ? 51  TRP C CD1 1 
ATOM   3349 C  CD2 . TRP C 1 63  ? 13.890  44.217  46.326  1.00 20.96 ? 51  TRP C CD2 1 
ATOM   3350 N  NE1 . TRP C 1 63  ? 13.833  45.697  48.003  1.00 21.99 ? 51  TRP C NE1 1 
ATOM   3351 C  CE2 . TRP C 1 63  ? 13.233  44.566  47.525  1.00 22.52 ? 51  TRP C CE2 1 
ATOM   3352 C  CE3 . TRP C 1 63  ? 13.451  43.093  45.617  1.00 21.95 ? 51  TRP C CE3 1 
ATOM   3353 C  CZ2 . TRP C 1 63  ? 12.139  43.848  48.023  1.00 24.17 ? 51  TRP C CZ2 1 
ATOM   3354 C  CZ3 . TRP C 1 63  ? 12.371  42.400  46.100  1.00 20.42 ? 51  TRP C CZ3 1 
ATOM   3355 C  CH2 . TRP C 1 63  ? 11.719  42.763  47.282  1.00 20.33 ? 51  TRP C CH2 1 
ATOM   3356 N  N   . ASN C 1 64  ? 17.163  47.103  42.692  1.00 16.24 ? 52  ASN C N   1 
ATOM   3357 C  CA  . ASN C 1 64  ? 18.278  47.053  41.733  1.00 16.50 ? 52  ASN C CA  1 
ATOM   3358 C  C   . ASN C 1 64  ? 19.504  47.692  42.361  1.00 17.88 ? 52  ASN C C   1 
ATOM   3359 O  O   . ASN C 1 64  ? 19.523  48.920  42.538  1.00 17.70 ? 52  ASN C O   1 
ATOM   3360 C  CB  . ASN C 1 64  ? 17.929  47.722  40.429  1.00 16.51 ? 52  ASN C CB  1 
ATOM   3361 C  CG  . ASN C 1 64  ? 18.995  47.472  39.399  1.00 17.05 ? 52  ASN C CG  1 
ATOM   3362 O  OD1 . ASN C 1 64  ? 19.850  46.607  39.580  1.00 19.17 ? 52  ASN C OD1 1 
ATOM   3363 N  ND2 . ASN C 1 64  ? 18.931  48.199  38.295  1.00 25.55 ? 52  ASN C ND2 1 
ATOM   3364 N  N   . PRO C 1 65  ? 20.546  46.922  42.718  1.00 19.95 ? 53  PRO C N   1 
ATOM   3365 C  CA  . PRO C 1 65  ? 20.600  45.472  42.550  1.00 19.75 ? 53  PRO C CA  1 
ATOM   3366 C  C   . PRO C 1 65  ? 19.761  44.650  43.522  1.00 20.54 ? 53  PRO C C   1 
ATOM   3367 O  O   . PRO C 1 65  ? 19.520  45.104  44.621  1.00 21.67 ? 53  PRO C O   1 
ATOM   3368 C  CB  . PRO C 1 65  ? 22.066  45.098  42.835  1.00 21.84 ? 53  PRO C CB  1 
ATOM   3369 C  CG  . PRO C 1 65  ? 22.674  46.281  43.542  1.00 24.19 ? 53  PRO C CG  1 
ATOM   3370 C  CD  . PRO C 1 65  ? 21.757  47.453  43.365  1.00 21.70 ? 53  PRO C CD  1 
ATOM   3371 N  N   . GLY C 1 66  ? 19.371  43.448  43.080  1.00 21.22 ? 54  GLY C N   1 
ATOM   3372 C  CA  . GLY C 1 66  ? 18.772  42.425  43.940  1.00 21.14 ? 54  GLY C CA  1 
ATOM   3373 C  C   . GLY C 1 66  ? 19.809  41.851  44.886  1.00 22.27 ? 54  GLY C C   1 
ATOM   3374 O  O   . GLY C 1 66  ? 20.994  41.825  44.562  1.00 23.91 ? 54  GLY C O   1 
ATOM   3375 N  N   . SER C 1 67  ? 19.366  41.501  46.069  1.00 23.80 ? 55  SER C N   1 
ATOM   3376 C  CA  . SER C 1 67  ? 20.118  40.695  47.045  1.00 29.10 ? 55  SER C CA  1 
ATOM   3377 C  C   . SER C 1 67  ? 19.472  39.307  47.005  1.00 29.22 ? 55  SER C C   1 
ATOM   3378 O  O   . SER C 1 67  ? 18.759  39.016  46.061  1.00 33.10 ? 55  SER C O   1 
ATOM   3379 C  CB  . SER C 1 67  ? 20.075  41.336  48.401  1.00 33.83 ? 55  SER C CB  1 
ATOM   3380 O  OG  . SER C 1 67  ? 20.446  42.711  48.338  1.00 34.09 ? 55  SER C OG  1 
ATOM   3381 N  N   . SER C 1 68  ? 19.682  38.490  48.006  1.00 34.73 ? 56  SER C N   1 
ATOM   3382 C  CA  . SER C 1 68  ? 19.072  37.144  48.015  1.00 33.72 ? 56  SER C CA  1 
ATOM   3383 C  C   . SER C 1 68  ? 17.964  37.192  49.055  1.00 31.39 ? 56  SER C C   1 
ATOM   3384 O  O   . SER C 1 68  ? 17.915  36.304  49.907  1.00 37.85 ? 56  SER C O   1 
ATOM   3385 C  CB  . SER C 1 68  ? 20.113  36.104  48.269  1.00 37.42 ? 56  SER C CB  1 
ATOM   3386 O  OG  . SER C 1 68  ? 20.980  36.519  49.324  1.00 42.25 ? 56  SER C OG  1 
ATOM   3387 N  N   . GLN C 1 69  ? 17.163  38.257  48.997  1.00 36.93 ? 57  GLN C N   1 
ATOM   3388 C  CA  . GLN C 1 69  ? 16.217  38.620  50.083  1.00 37.96 ? 57  GLN C CA  1 
ATOM   3389 C  C   . GLN C 1 69  ? 14.992  37.705  49.951  1.00 30.33 ? 57  GLN C C   1 
ATOM   3390 O  O   . GLN C 1 69  ? 14.626  37.310  48.835  1.00 27.82 ? 57  GLN C O   1 
ATOM   3391 C  CB  . GLN C 1 69  ? 15.894  40.128  50.116  1.00 40.41 ? 57  GLN C CB  1 
ATOM   3392 C  CG  . GLN C 1 69  ? 15.349  40.741  48.827  1.00 39.63 ? 57  GLN C CG  1 
ATOM   3393 C  CD  . GLN C 1 69  ? 16.297  41.715  48.150  1.00 42.35 ? 57  GLN C CD  1 
ATOM   3394 O  OE1 . GLN C 1 69  ? 16.323  42.926  48.406  1.00 41.99 ? 57  GLN C OE1 1 
ATOM   3395 N  NE2 . GLN C 1 69  ? 17.080  41.201  47.227  1.00 34.00 ? 57  GLN C NE2 1 
ATOM   3396 N  N   . THR C 1 70  ? 14.422  37.327  51.080  1.00 28.78 ? 58  THR C N   1 
ATOM   3397 C  CA  . THR C 1 70  ? 13.095  36.667  51.140  1.00 28.43 ? 58  THR C CA  1 
ATOM   3398 C  C   . THR C 1 70  ? 12.028  37.691  50.768  1.00 24.93 ? 58  THR C C   1 
ATOM   3399 O  O   . THR C 1 70  ? 11.978  38.801  51.382  1.00 27.34 ? 58  THR C O   1 
ATOM   3400 C  CB  . THR C 1 70  ? 12.870  36.026  52.509  1.00 29.30 ? 58  THR C CB  1 
ATOM   3401 O  OG1 . THR C 1 70  ? 13.944  35.102  52.635  1.00 29.51 ? 58  THR C OG1 1 
ATOM   3402 C  CG2 . THR C 1 70  ? 11.551  35.308  52.609  1.00 29.65 ? 58  THR C CG2 1 
ATOM   3403 N  N   . ILE C 1 71  ? 11.237  37.381  49.747  1.00 22.32 ? 59  ILE C N   1 
ATOM   3404 C  CA  . ILE C 1 71  ? 10.234  38.343  49.219  1.00 22.06 ? 59  ILE C CA  1 
ATOM   3405 C  C   . ILE C 1 71  ? 8.879   37.875  49.714  1.00 22.30 ? 59  ILE C C   1 
ATOM   3406 O  O   . ILE C 1 71  ? 8.634   36.628  49.735  1.00 22.77 ? 59  ILE C O   1 
ATOM   3407 C  CB  . ILE C 1 71  ? 10.282  38.353  47.685  1.00 22.07 ? 59  ILE C CB  1 
ATOM   3408 C  CG1 . ILE C 1 71  ? 11.646  38.838  47.182  1.00 20.93 ? 59  ILE C CG1 1 
ATOM   3409 C  CG2 . ILE C 1 71  ? 9.076   39.072  47.103  1.00 24.31 ? 59  ILE C CG2 1 
ATOM   3410 C  CD1 . ILE C 1 71  ? 11.799  38.683  45.699  1.00 21.85 ? 59  ILE C CD1 1 
ATOM   3411 N  N   . THR C 1 72  ? 8.040   38.831  50.051  1.00 20.95 ? 60  THR C N   1 
ATOM   3412 C  CA  . THR C 1 72  ? 6.613   38.610  50.361  1.00 21.28 ? 60  THR C CA  1 
ATOM   3413 C  C   . THR C 1 72  ? 5.808   39.453  49.382  1.00 21.23 ? 60  THR C C   1 
ATOM   3414 O  O   . THR C 1 72  ? 6.131   40.670  49.208  1.00 22.15 ? 60  THR C O   1 
ATOM   3415 C  CB  . THR C 1 72  ? 6.315   38.917  51.831  1.00 25.85 ? 60  THR C CB  1 
ATOM   3416 O  OG1 . THR C 1 72  ? 6.654   40.279  52.095  1.00 37.53 ? 60  THR C OG1 1 
ATOM   3417 C  CG2 . THR C 1 72  ? 7.105   38.062  52.787  1.00 26.06 ? 60  THR C CG2 1 
ATOM   3418 N  N   . TYR C 1 73  ? 4.818   38.847  48.730  1.00 20.10 ? 61  TYR C N   1 
ATOM   3419 C  CA  . TYR C 1 73  ? 3.993   39.585  47.747  1.00 20.53 ? 61  TYR C CA  1 
ATOM   3420 C  C   . TYR C 1 73  ? 2.548   39.107  47.920  1.00 21.20 ? 61  TYR C C   1 
ATOM   3421 O  O   . TYR C 1 73  ? 2.300   37.960  48.385  1.00 21.13 ? 61  TYR C O   1 
ATOM   3422 C  CB  . TYR C 1 73  ? 4.543   39.415  46.323  1.00 21.80 ? 61  TYR C CB  1 
ATOM   3423 C  CG  . TYR C 1 73  ? 4.265   38.059  45.721  1.00 19.90 ? 61  TYR C CG  1 
ATOM   3424 C  CD1 . TYR C 1 73  ? 4.948   36.947  46.133  1.00 20.79 ? 61  TYR C CD1 1 
ATOM   3425 C  CD2 . TYR C 1 73  ? 3.216   37.882  44.833  1.00 21.11 ? 61  TYR C CD2 1 
ATOM   3426 C  CE1 . TYR C 1 73  ? 4.654   35.683  45.659  1.00 22.46 ? 61  TYR C CE1 1 
ATOM   3427 C  CE2 . TYR C 1 73  ? 2.906   36.633  44.333  1.00 22.05 ? 61  TYR C CE2 1 
ATOM   3428 C  CZ  . TYR C 1 73  ? 3.632   35.530  44.731  1.00 24.02 ? 61  TYR C CZ  1 
ATOM   3429 O  OH  . TYR C 1 73  ? 3.309   34.292  44.277  1.00 24.42 ? 61  TYR C OH  1 
ATOM   3430 N  N   . SER C 1 74  ? 1.641   39.942  47.471  1.00 21.47 ? 62  SER C N   1 
ATOM   3431 C  CA  . SER C 1 74  ? 0.191   39.668  47.492  1.00 21.57 ? 62  SER C CA  1 
ATOM   3432 C  C   . SER C 1 74  ? -0.464  40.378  46.318  1.00 22.15 ? 62  SER C C   1 
ATOM   3433 O  O   . SER C 1 74  ? 0.224   41.167  45.636  1.00 20.64 ? 62  SER C O   1 
ATOM   3434 C  CB  . SER C 1 74  ? -0.392  40.096  48.797  1.00 23.45 ? 62  SER C CB  1 
ATOM   3435 O  OG  . SER C 1 74  ? -0.324  41.499  48.921  1.00 25.73 ? 62  SER C OG  1 
ATOM   3436 N  N   . GLY C 1 75  ? -1.753  40.129  46.148  1.00 20.78 ? 63  GLY C N   1 
ATOM   3437 C  CA  . GLY C 1 75  ? -2.641  40.817  45.208  1.00 21.66 ? 63  GLY C CA  1 
ATOM   3438 C  C   . GLY C 1 75  ? -3.390  39.858  44.311  1.00 22.00 ? 63  GLY C C   1 
ATOM   3439 O  O   . GLY C 1 75  ? -3.765  38.716  44.757  1.00 19.91 ? 63  GLY C O   1 
ATOM   3440 N  N   . GLU C 1 76  ? -3.580  40.295  43.066  1.00 19.98 ? 64  GLU C N   1 
ATOM   3441 C  CA  . GLU C 1 76  ? -4.466  39.672  42.065  1.00 22.27 ? 64  GLU C CA  1 
ATOM   3442 C  C   . GLU C 1 76  ? -3.730  39.616  40.732  1.00 21.55 ? 64  GLU C C   1 
ATOM   3443 O  O   . GLU C 1 76  ? -3.045  40.608  40.385  1.00 20.61 ? 64  GLU C O   1 
ATOM   3444 C  CB  . GLU C 1 76  ? -5.736  40.488  41.832  1.00 26.11 ? 64  GLU C CB  1 
ATOM   3445 C  CG  . GLU C 1 76  ? -6.461  40.916  43.090  1.00 33.08 ? 64  GLU C CG  1 
ATOM   3446 C  CD  . GLU C 1 76  ? -7.822  41.517  42.775  1.00 37.85 ? 64  GLU C CD  1 
ATOM   3447 O  OE1 . GLU C 1 76  ? -8.670  41.564  43.693  1.00 46.62 ? 64  GLU C OE1 1 
ATOM   3448 O  OE2 . GLU C 1 76  ? -8.037  41.923  41.600  1.00 41.82 ? 64  GLU C OE2 1 
ATOM   3449 N  N   . TRP C 1 77  ? -3.989  38.547  39.998  1.00 19.00 ? 65  TRP C N   1 
ATOM   3450 C  CA  . TRP C 1 77  ? -3.394  38.283  38.667  1.00 19.54 ? 65  TRP C CA  1 
ATOM   3451 C  C   . TRP C 1 77  ? -4.445  37.572  37.828  1.00 21.26 ? 65  TRP C C   1 
ATOM   3452 O  O   . TRP C 1 77  ? -4.786  36.366  38.118  1.00 19.01 ? 65  TRP C O   1 
ATOM   3453 C  CB  . TRP C 1 77  ? -2.080  37.544  38.847  1.00 18.94 ? 65  TRP C CB  1 
ATOM   3454 C  CG  . TRP C 1 77  ? -1.418  37.009  37.614  1.00 20.15 ? 65  TRP C CG  1 
ATOM   3455 C  CD1 . TRP C 1 77  ? -0.628  37.690  36.735  1.00 21.74 ? 65  TRP C CD1 1 
ATOM   3456 C  CD2 . TRP C 1 77  ? -1.410  35.633  37.203  1.00 18.63 ? 65  TRP C CD2 1 
ATOM   3457 N  NE1 . TRP C 1 77  ? -0.159  36.834  35.771  1.00 21.69 ? 65  TRP C NE1 1 
ATOM   3458 C  CE2 . TRP C 1 77  ? -0.631  35.562  36.028  1.00 20.10 ? 65  TRP C CE2 1 
ATOM   3459 C  CE3 . TRP C 1 77  ? -2.001  34.464  37.698  1.00 20.72 ? 65  TRP C CE3 1 
ATOM   3460 C  CZ2 . TRP C 1 77  ? -0.427  34.364  35.358  1.00 20.70 ? 65  TRP C CZ2 1 
ATOM   3461 C  CZ3 . TRP C 1 77  ? -1.835  33.288  37.011  1.00 18.96 ? 65  TRP C CZ3 1 
ATOM   3462 C  CH2 . TRP C 1 77  ? -1.023  33.236  35.872  1.00 21.39 ? 65  TRP C CH2 1 
ATOM   3463 N  N   . ASN C 1 78  ? -4.986  38.327  36.876  1.00 19.40 ? 66  ASN C N   1 
ATOM   3464 C  CA  . ASN C 1 78  ? -6.181  37.947  36.090  1.00 20.81 ? 66  ASN C CA  1 
ATOM   3465 C  C   . ASN C 1 78  ? -5.828  37.954  34.602  1.00 20.22 ? 66  ASN C C   1 
ATOM   3466 O  O   . ASN C 1 78  ? -6.400  38.745  33.852  1.00 18.95 ? 66  ASN C O   1 
ATOM   3467 C  CB  . ASN C 1 78  ? -7.373  38.844  36.411  1.00 22.98 ? 66  ASN C CB  1 
ATOM   3468 C  CG  . ASN C 1 78  ? -7.572  39.060  37.902  1.00 29.89 ? 66  ASN C CG  1 
ATOM   3469 O  OD1 . ASN C 1 78  ? -7.768  38.110  38.644  1.00 31.07 ? 66  ASN C OD1 1 
ATOM   3470 N  ND2 . ASN C 1 78  ? -7.530  40.307  38.355  1.00 30.32 ? 66  ASN C ND2 1 
ATOM   3471 N  N   . PRO C 1 79  ? -4.997  36.999  34.127  1.00 22.01 ? 67  PRO C N   1 
ATOM   3472 C  CA  . PRO C 1 79  ? -4.731  36.875  32.692  1.00 21.23 ? 67  PRO C CA  1 
ATOM   3473 C  C   . PRO C 1 79  ? -5.867  36.198  31.909  1.00 25.19 ? 67  PRO C C   1 
ATOM   3474 O  O   . PRO C 1 79  ? -6.552  35.336  32.435  1.00 23.42 ? 67  PRO C O   1 
ATOM   3475 C  CB  . PRO C 1 79  ? -3.453  36.039  32.699  1.00 23.20 ? 67  PRO C CB  1 
ATOM   3476 C  CG  . PRO C 1 79  ? -3.674  35.062  33.855  1.00 22.96 ? 67  PRO C CG  1 
ATOM   3477 C  CD  . PRO C 1 79  ? -4.339  35.925  34.908  1.00 23.98 ? 67  PRO C CD  1 
ATOM   3478 N  N   . ASN C 1 80  ? -6.058  36.639  30.667  1.00 23.32 ? 68  ASN C N   1 
ATOM   3479 C  CA  . ASN C 1 80  ? -6.838  35.920  29.626  1.00 25.14 ? 68  ASN C CA  1 
ATOM   3480 C  C   . ASN C 1 80  ? -5.866  35.519  28.512  1.00 25.40 ? 68  ASN C C   1 
ATOM   3481 O  O   . ASN C 1 80  ? -5.732  36.281  27.539  1.00 22.58 ? 68  ASN C O   1 
ATOM   3482 C  CB  . ASN C 1 80  ? -7.988  36.773  29.097  1.00 28.31 ? 68  ASN C CB  1 
ATOM   3483 C  CG  . ASN C 1 80  ? -8.915  35.990  28.192  1.00 35.38 ? 68  ASN C CG  1 
ATOM   3484 O  OD1 . ASN C 1 80  ? -9.006  34.769  28.299  1.00 40.02 ? 68  ASN C OD1 1 
ATOM   3485 N  ND2 . ASN C 1 80  ? -9.624  36.684  27.317  1.00 40.11 ? 68  ASN C ND2 1 
ATOM   3486 N  N   . GLY C 1 81  ? -5.221  34.354  28.657  1.00 20.81 ? 69  GLY C N   1 
ATOM   3487 C  CA  . GLY C 1 81  ? -4.114  33.907  27.803  1.00 21.08 ? 69  GLY C CA  1 
ATOM   3488 C  C   . GLY C 1 81  ? -2.771  33.923  28.514  1.00 18.71 ? 69  GLY C C   1 
ATOM   3489 O  O   . GLY C 1 81  ? -2.713  34.081  29.738  1.00 20.20 ? 69  GLY C O   1 
ATOM   3490 N  N   . ASN C 1 82  ? -1.721  33.795  27.720  1.00 17.84 ? 70  ASN C N   1 
ATOM   3491 C  CA  . ASN C 1 82  ? -0.320  33.543  28.120  1.00 18.15 ? 70  ASN C CA  1 
ATOM   3492 C  C   . ASN C 1 82  ? 0.189   34.618  29.072  1.00 18.42 ? 70  ASN C C   1 
ATOM   3493 O  O   . ASN C 1 82  ? 0.378   35.787  28.645  1.00 16.63 ? 70  ASN C O   1 
ATOM   3494 C  CB  . ASN C 1 82  ? 0.582   33.419  26.898  1.00 18.73 ? 70  ASN C CB  1 
ATOM   3495 C  CG  . ASN C 1 82  ? 1.993   32.989  27.217  1.00 23.14 ? 70  ASN C CG  1 
ATOM   3496 O  OD1 . ASN C 1 82  ? 2.364   32.745  28.385  1.00 23.60 ? 70  ASN C OD1 1 
ATOM   3497 N  ND2 . ASN C 1 82  ? 2.791   32.854  26.163  1.00 23.99 ? 70  ASN C ND2 1 
ATOM   3498 N  N   . SER C 1 83  ? 0.451   34.245  30.322  1.00 17.30 ? 71  SER C N   1 
ATOM   3499 C  CA  . SER C 1 83  ? 0.973   35.180  31.345  1.00 18.33 ? 71  SER C CA  1 
ATOM   3500 C  C   . SER C 1 83  ? 1.691   34.380  32.430  1.00 19.28 ? 71  SER C C   1 
ATOM   3501 O  O   . SER C 1 83  ? 1.404   33.142  32.617  1.00 19.20 ? 71  SER C O   1 
ATOM   3502 C  CB  . SER C 1 83  ? -0.119  36.070  31.894  1.00 17.93 ? 71  SER C CB  1 
ATOM   3503 O  OG  . SER C 1 83  ? 0.378   37.031  32.830  1.00 18.63 ? 71  SER C OG  1 
ATOM   3504 N  N   . TYR C 1 84  ? 2.722   34.984  32.989  1.00 19.69 ? 72  TYR C N   1 
ATOM   3505 C  CA  . TYR C 1 84  ? 3.517   34.386  34.092  1.00 21.80 ? 72  TYR C CA  1 
ATOM   3506 C  C   . TYR C 1 84  ? 3.548   35.416  35.207  1.00 18.07 ? 72  TYR C C   1 
ATOM   3507 O  O   . TYR C 1 84  ? 3.564   36.648  34.969  1.00 15.38 ? 72  TYR C O   1 
ATOM   3508 C  CB  . TYR C 1 84  ? 4.983   34.061  33.744  1.00 24.34 ? 72  TYR C CB  1 
ATOM   3509 C  CG  . TYR C 1 84  ? 5.373   33.547  32.381  1.00 27.09 ? 72  TYR C CG  1 
ATOM   3510 C  CD1 . TYR C 1 84  ? 4.611   32.619  31.683  1.00 30.24 ? 72  TYR C CD1 1 
ATOM   3511 C  CD2 . TYR C 1 84  ? 6.597   33.915  31.824  1.00 30.72 ? 72  TYR C CD2 1 
ATOM   3512 C  CE1 . TYR C 1 84  ? 5.027   32.103  30.462  1.00 34.07 ? 72  TYR C CE1 1 
ATOM   3513 C  CE2 . TYR C 1 84  ? 7.006   33.436  30.589  1.00 31.93 ? 72  TYR C CE2 1 
ATOM   3514 C  CZ  . TYR C 1 84  ? 6.229   32.513  29.911  1.00 34.41 ? 72  TYR C CZ  1 
ATOM   3515 O  OH  . TYR C 1 84  ? 6.650   32.003  28.701  1.00 35.25 ? 72  TYR C OH  1 
ATOM   3516 N  N   . LEU C 1 85  ? 3.470   34.930  36.436  1.00 18.49 ? 73  LEU C N   1 
ATOM   3517 C  CA  . LEU C 1 85  ? 3.719   35.725  37.652  1.00 17.07 ? 73  LEU C CA  1 
ATOM   3518 C  C   . LEU C 1 85  ? 4.957   35.118  38.313  1.00 17.04 ? 73  LEU C C   1 
ATOM   3519 O  O   . LEU C 1 85  ? 4.991   33.889  38.585  1.00 15.93 ? 73  LEU C O   1 
ATOM   3520 C  CB  . LEU C 1 85  ? 2.482   35.662  38.550  1.00 18.04 ? 73  LEU C CB  1 
ATOM   3521 C  CG  . LEU C 1 85  ? 2.611   36.397  39.871  1.00 19.21 ? 73  LEU C CG  1 
ATOM   3522 C  CD1 . LEU C 1 85  ? 2.762   37.900  39.628  1.00 20.53 ? 73  LEU C CD1 1 
ATOM   3523 C  CD2 . LEU C 1 85  ? 1.402   36.114  40.769  1.00 20.10 ? 73  LEU C CD2 1 
ATOM   3524 N  N   . SER C 1 86  ? 6.003   35.898  38.510  1.00 17.32 ? 74  SER C N   1 
ATOM   3525 C  CA  . SER C 1 86  ? 7.318   35.333  38.863  1.00 18.51 ? 74  SER C CA  1 
ATOM   3526 C  C   . SER C 1 86  ? 8.136   36.319  39.665  1.00 17.60 ? 74  SER C C   1 
ATOM   3527 O  O   . SER C 1 86  ? 7.956   37.549  39.500  1.00 18.21 ? 74  SER C O   1 
ATOM   3528 C  CB  . SER C 1 86  ? 8.084   34.957  37.615  1.00 21.67 ? 74  SER C CB  1 
ATOM   3529 O  OG  . SER C 1 86  ? 8.391   36.166  36.942  1.00 28.03 ? 74  SER C OG  1 
ATOM   3530 N  N   . VAL C 1 87  ? 9.057   35.782  40.446  1.00 15.81 ? 75  VAL C N   1 
ATOM   3531 C  CA  . VAL C 1 87  ? 10.220  36.586  40.875  1.00 15.00 ? 75  VAL C CA  1 
ATOM   3532 C  C   . VAL C 1 87  ? 11.204  36.517  39.715  1.00 16.25 ? 75  VAL C C   1 
ATOM   3533 O  O   . VAL C 1 87  ? 11.477  35.403  39.196  1.00 18.04 ? 75  VAL C O   1 
ATOM   3534 C  CB  . VAL C 1 87  ? 10.806  36.147  42.215  1.00 15.54 ? 75  VAL C CB  1 
ATOM   3535 C  CG1 . VAL C 1 87  ? 12.121  36.835  42.468  1.00 16.58 ? 75  VAL C CG1 1 
ATOM   3536 C  CG2 . VAL C 1 87  ? 9.837   36.361  43.356  1.00 15.78 ? 75  VAL C CG2 1 
ATOM   3537 N  N   . TYR C 1 88  ? 11.617  37.690  39.253  1.00 14.48 ? 76  TYR C N   1 
ATOM   3538 C  CA  . TYR C 1 88  ? 12.252  37.833  37.917  1.00 15.10 ? 76  TYR C CA  1 
ATOM   3539 C  C   . TYR C 1 88  ? 13.492  38.681  38.054  1.00 15.44 ? 76  TYR C C   1 
ATOM   3540 O  O   . TYR C 1 88  ? 13.415  39.736  38.652  1.00 14.64 ? 76  TYR C O   1 
ATOM   3541 C  CB  . TYR C 1 88  ? 11.252  38.372  36.902  1.00 15.74 ? 76  TYR C CB  1 
ATOM   3542 C  CG  . TYR C 1 88  ? 11.859  38.731  35.579  1.00 16.43 ? 76  TYR C CG  1 
ATOM   3543 C  CD1 . TYR C 1 88  ? 12.243  37.780  34.657  1.00 17.03 ? 76  TYR C CD1 1 
ATOM   3544 C  CD2 . TYR C 1 88  ? 12.035  40.055  35.254  1.00 15.19 ? 76  TYR C CD2 1 
ATOM   3545 C  CE1 . TYR C 1 88  ? 12.786  38.147  33.432  1.00 17.36 ? 76  TYR C CE1 1 
ATOM   3546 C  CE2 . TYR C 1 88  ? 12.579  40.448  34.039  1.00 16.87 ? 76  TYR C CE2 1 
ATOM   3547 C  CZ  . TYR C 1 88  ? 12.975  39.491  33.127  1.00 14.59 ? 76  TYR C CZ  1 
ATOM   3548 O  OH  . TYR C 1 88  ? 13.507  39.872  31.911  1.00 17.55 ? 76  TYR C OH  1 
ATOM   3549 N  N   . GLY C 1 89  ? 14.584  38.291  37.394  1.00 16.51 ? 77  GLY C N   1 
ATOM   3550 C  CA  . GLY C 1 89  ? 15.790  39.102  37.572  1.00 17.22 ? 77  GLY C CA  1 
ATOM   3551 C  C   . GLY C 1 89  ? 16.908  38.733  36.637  1.00 17.59 ? 77  GLY C C   1 
ATOM   3552 O  O   . GLY C 1 89  ? 16.733  37.801  35.829  1.00 17.29 ? 77  GLY C O   1 
ATOM   3553 N  N   . TRP C 1 90  ? 18.027  39.435  36.794  1.00 16.74 ? 78  TRP C N   1 
ATOM   3554 C  CA  . TRP C 1 90  ? 19.194  39.323  35.900  1.00 16.66 ? 78  TRP C CA  1 
ATOM   3555 C  C   . TRP C 1 90  ? 20.441  39.296  36.770  1.00 18.17 ? 78  TRP C C   1 
ATOM   3556 O  O   . TRP C 1 90  ? 20.449  39.898  37.847  1.00 19.85 ? 78  TRP C O   1 
ATOM   3557 C  CB  . TRP C 1 90  ? 19.265  40.478  34.901  1.00 17.68 ? 78  TRP C CB  1 
ATOM   3558 C  CG  . TRP C 1 90  ? 18.174  40.523  33.891  1.00 17.82 ? 78  TRP C CG  1 
ATOM   3559 C  CD1 . TRP C 1 90  ? 16.915  40.996  34.069  1.00 19.13 ? 78  TRP C CD1 1 
ATOM   3560 C  CD2 . TRP C 1 90  ? 18.235  40.053  32.540  1.00 17.49 ? 78  TRP C CD2 1 
ATOM   3561 N  NE1 . TRP C 1 90  ? 16.192  40.853  32.925  1.00 20.39 ? 78  TRP C NE1 1 
ATOM   3562 C  CE2 . TRP C 1 90  ? 16.982  40.279  31.966  1.00 17.57 ? 78  TRP C CE2 1 
ATOM   3563 C  CE3 . TRP C 1 90  ? 19.240  39.492  31.750  1.00 18.81 ? 78  TRP C CE3 1 
ATOM   3564 C  CZ2 . TRP C 1 90  ? 16.698  39.956  30.652  1.00 17.84 ? 78  TRP C CZ2 1 
ATOM   3565 C  CZ3 . TRP C 1 90  ? 18.957  39.178  30.441  1.00 19.98 ? 78  TRP C CZ3 1 
ATOM   3566 C  CH2 . TRP C 1 90  ? 17.697  39.398  29.903  1.00 19.31 ? 78  TRP C CH2 1 
ATOM   3567 N  N   . THR C 1 91  ? 21.456  38.641  36.248  1.00 20.26 ? 79  THR C N   1 
ATOM   3568 C  CA  . THR C 1 91  ? 22.852  38.698  36.723  1.00 20.43 ? 79  THR C CA  1 
ATOM   3569 C  C   . THR C 1 91  ? 23.709  39.009  35.508  1.00 19.97 ? 79  THR C C   1 
ATOM   3570 O  O   . THR C 1 91  ? 23.235  38.906  34.347  1.00 20.55 ? 79  THR C O   1 
ATOM   3571 C  CB  . THR C 1 91  ? 23.359  37.408  37.387  1.00 24.29 ? 79  THR C CB  1 
ATOM   3572 O  OG1 . THR C 1 91  ? 23.746  36.430  36.415  1.00 22.24 ? 79  THR C OG1 1 
ATOM   3573 C  CG2 . THR C 1 91  ? 22.382  36.744  38.335  1.00 23.19 ? 79  THR C CG2 1 
ATOM   3574 N  N   . GLN C 1 92  ? 24.950  39.401  35.774  1.00 21.79 ? 80  GLN C N   1 
ATOM   3575 C  CA  . GLN C 1 92  ? 25.920  39.790  34.713  1.00 23.62 ? 80  GLN C CA  1 
ATOM   3576 C  C   . GLN C 1 92  ? 27.253  39.118  35.048  1.00 24.57 ? 80  GLN C C   1 
ATOM   3577 O  O   . GLN C 1 92  ? 27.450  38.818  36.218  1.00 25.81 ? 80  GLN C O   1 
ATOM   3578 C  CB  . GLN C 1 92  ? 26.062  41.318  34.648  1.00 24.05 ? 80  GLN C CB  1 
ATOM   3579 C  CG  . GLN C 1 92  ? 24.840  42.024  34.088  1.00 23.82 ? 80  GLN C CG  1 
ATOM   3580 C  CD  . GLN C 1 92  ? 24.935  43.532  34.188  1.00 25.61 ? 80  GLN C CD  1 
ATOM   3581 O  OE1 . GLN C 1 92  ? 24.738  44.109  35.243  1.00 25.78 ? 80  GLN C OE1 1 
ATOM   3582 N  NE2 . GLN C 1 92  ? 25.206  44.182  33.069  1.00 28.28 ? 80  GLN C NE2 1 
ATOM   3583 N  N   . ASN C 1 93  ? 28.081  38.845  34.038  1.00 30.83 ? 81  ASN C N   1 
ATOM   3584 C  CA  . ASN C 1 93  ? 29.372  38.117  34.190  1.00 31.25 ? 81  ASN C CA  1 
ATOM   3585 C  C   . ASN C 1 93  ? 29.183  36.848  35.020  1.00 30.00 ? 81  ASN C C   1 
ATOM   3586 O  O   . ASN C 1 93  ? 29.751  36.731  36.111  1.00 27.12 ? 81  ASN C O   1 
ATOM   3587 C  CB  . ASN C 1 93  ? 30.441  39.019  34.809  1.00 37.03 ? 81  ASN C CB  1 
ATOM   3588 C  CG  . ASN C 1 93  ? 30.592  40.327  34.065  1.00 43.36 ? 81  ASN C CG  1 
ATOM   3589 O  OD1 . ASN C 1 93  ? 30.444  40.370  32.843  1.00 49.06 ? 81  ASN C OD1 1 
ATOM   3590 N  ND2 . ASN C 1 93  ? 30.879  41.399  34.791  1.00 49.78 ? 81  ASN C ND2 1 
ATOM   3591 N  N   . PRO C 1 94  ? 28.378  35.860  34.556  1.00 25.63 ? 82  PRO C N   1 
ATOM   3592 C  CA  . PRO C 1 94  ? 27.749  35.893  33.236  1.00 24.57 ? 82  PRO C CA  1 
ATOM   3593 C  C   . PRO C 1 94  ? 26.355  36.528  33.184  1.00 23.55 ? 82  PRO C C   1 
ATOM   3594 O  O   . PRO C 1 94  ? 25.719  36.656  34.249  1.00 21.61 ? 82  PRO C O   1 
ATOM   3595 C  CB  . PRO C 1 94  ? 27.580  34.396  32.948  1.00 25.38 ? 82  PRO C CB  1 
ATOM   3596 C  CG  . PRO C 1 94  ? 27.253  33.811  34.285  1.00 27.34 ? 82  PRO C CG  1 
ATOM   3597 C  CD  . PRO C 1 94  ? 28.091  34.600  35.270  1.00 28.00 ? 82  PRO C CD  1 
ATOM   3598 N  N   . LEU C 1 95  ? 25.886  36.768  31.965  1.00 23.73 ? 83  LEU C N   1 
ATOM   3599 C  CA  . LEU C 1 95  ? 24.550  37.352  31.700  1.00 25.28 ? 83  LEU C CA  1 
ATOM   3600 C  C   . LEU C 1 95  ? 23.535  36.218  31.827  1.00 24.33 ? 83  LEU C C   1 
ATOM   3601 O  O   . LEU C 1 95  ? 23.599  35.263  31.057  1.00 25.70 ? 83  LEU C O   1 
ATOM   3602 C  CB  . LEU C 1 95  ? 24.511  38.034  30.322  1.00 26.18 ? 83  LEU C CB  1 
ATOM   3603 C  CG  . LEU C 1 95  ? 23.217  38.797  30.004  1.00 25.53 ? 83  LEU C CG  1 
ATOM   3604 C  CD1 . LEU C 1 95  ? 23.005  39.965  30.947  1.00 26.41 ? 83  LEU C CD1 1 
ATOM   3605 C  CD2 . LEU C 1 95  ? 23.145  39.259  28.552  1.00 25.48 ? 83  LEU C CD2 1 
ATOM   3606 N  N   . VAL C 1 96  ? 22.628  36.334  32.793  1.00 23.58 ? 84  VAL C N   1 
ATOM   3607 C  CA  . VAL C 1 96  ? 21.566  35.330  33.020  1.00 21.82 ? 84  VAL C CA  1 
ATOM   3608 C  C   . VAL C 1 96  ? 20.246  36.042  33.251  1.00 19.55 ? 84  VAL C C   1 
ATOM   3609 O  O   . VAL C 1 96  ? 20.225  36.996  34.004  1.00 18.25 ? 84  VAL C O   1 
ATOM   3610 C  CB  . VAL C 1 96  ? 21.908  34.452  34.230  1.00 23.54 ? 84  VAL C CB  1 
ATOM   3611 C  CG1 . VAL C 1 96  ? 20.757  33.518  34.594  1.00 21.30 ? 84  VAL C CG1 1 
ATOM   3612 C  CG2 . VAL C 1 96  ? 23.216  33.703  34.008  1.00 24.06 ? 84  VAL C CG2 1 
ATOM   3613 N  N   . GLU C 1 97  ? 19.197  35.575  32.601  1.00 19.72 ? 85  GLU C N   1 
ATOM   3614 C  CA  . GLU C 1 97  ? 17.802  35.939  32.955  1.00 19.10 ? 85  GLU C CA  1 
ATOM   3615 C  C   . GLU C 1 97  ? 17.207  34.809  33.799  1.00 17.53 ? 85  GLU C C   1 
ATOM   3616 O  O   . GLU C 1 97  ? 17.320  33.631  33.384  1.00 20.49 ? 85  GLU C O   1 
ATOM   3617 C  CB  . GLU C 1 97  ? 16.999  36.146  31.684  1.00 18.96 ? 85  GLU C CB  1 
ATOM   3618 C  CG  . GLU C 1 97  ? 15.648  36.776  31.903  1.00 21.70 ? 85  GLU C CG  1 
ATOM   3619 C  CD  . GLU C 1 97  ? 14.845  36.887  30.613  1.00 23.52 ? 85  GLU C CD  1 
ATOM   3620 O  OE1 . GLU C 1 97  ? 14.061  37.820  30.497  1.00 21.21 ? 85  GLU C OE1 1 
ATOM   3621 O  OE2 . GLU C 1 97  ? 14.986  35.998  29.741  1.00 23.94 ? 85  GLU C OE2 1 
ATOM   3622 N  N   . TYR C 1 98  ? 16.608  35.107  34.946  1.00 18.58 ? 86  TYR C N   1 
ATOM   3623 C  CA  . TYR C 1 98  ? 16.097  34.007  35.801  1.00 17.83 ? 86  TYR C CA  1 
ATOM   3624 C  C   . TYR C 1 98  ? 14.649  34.273  36.184  1.00 17.37 ? 86  TYR C C   1 
ATOM   3625 O  O   . TYR C 1 98  ? 14.183  35.430  36.305  1.00 15.74 ? 86  TYR C O   1 
ATOM   3626 C  CB  . TYR C 1 98  ? 17.002  33.743  37.010  1.00 19.45 ? 86  TYR C CB  1 
ATOM   3627 C  CG  . TYR C 1 98  ? 17.076  34.860  38.011  1.00 20.40 ? 86  TYR C CG  1 
ATOM   3628 C  CD1 . TYR C 1 98  ? 16.064  35.059  38.935  1.00 20.44 ? 86  TYR C CD1 1 
ATOM   3629 C  CD2 . TYR C 1 98  ? 18.168  35.716  38.055  1.00 22.62 ? 86  TYR C CD2 1 
ATOM   3630 C  CE1 . TYR C 1 98  ? 16.125  36.090  39.851  1.00 21.14 ? 86  TYR C CE1 1 
ATOM   3631 C  CE2 . TYR C 1 98  ? 18.251  36.745  38.985  1.00 20.73 ? 86  TYR C CE2 1 
ATOM   3632 C  CZ  . TYR C 1 98  ? 17.214  36.932  39.885  1.00 22.26 ? 86  TYR C CZ  1 
ATOM   3633 O  OH  . TYR C 1 98  ? 17.257  37.930  40.822  1.00 27.10 ? 86  TYR C OH  1 
ATOM   3634 N  N   . TYR C 1 99  ? 13.934  33.175  36.394  1.00 17.93 ? 87  TYR C N   1 
ATOM   3635 C  CA  . TYR C 1 99  ? 12.507  33.215  36.759  1.00 19.23 ? 87  TYR C CA  1 
ATOM   3636 C  C   . TYR C 1 99  ? 12.212  32.196  37.832  1.00 18.38 ? 87  TYR C C   1 
ATOM   3637 O  O   . TYR C 1 99  ? 12.550  30.993  37.673  1.00 22.32 ? 87  TYR C O   1 
ATOM   3638 C  CB  . TYR C 1 99  ? 11.588  32.798  35.629  1.00 21.30 ? 87  TYR C CB  1 
ATOM   3639 C  CG  . TYR C 1 99  ? 11.700  33.562  34.355  1.00 24.54 ? 87  TYR C CG  1 
ATOM   3640 C  CD1 . TYR C 1 99  ? 12.781  33.356  33.516  1.00 23.82 ? 87  TYR C CD1 1 
ATOM   3641 C  CD2 . TYR C 1 99  ? 10.706  34.438  33.981  1.00 27.14 ? 87  TYR C CD2 1 
ATOM   3642 C  CE1 . TYR C 1 99  ? 12.854  33.997  32.301  1.00 27.64 ? 87  TYR C CE1 1 
ATOM   3643 C  CE2 . TYR C 1 99  ? 10.781  35.115  32.777  1.00 28.74 ? 87  TYR C CE2 1 
ATOM   3644 C  CZ  . TYR C 1 99  ? 11.849  34.876  31.943  1.00 28.51 ? 87  TYR C CZ  1 
ATOM   3645 O  OH  . TYR C 1 99  ? 11.925  35.485  30.736  1.00 35.61 ? 87  TYR C OH  1 
ATOM   3646 N  N   . ILE C 1 100 ? 11.623  32.665  38.912  1.00 17.63 ? 88  ILE C N   1 
ATOM   3647 C  CA  . ILE C 1 100 ? 10.946  31.815  39.927  1.00 18.08 ? 88  ILE C CA  1 
ATOM   3648 C  C   . ILE C 1 100 ? 9.452   31.984  39.688  1.00 16.21 ? 88  ILE C C   1 
ATOM   3649 O  O   . ILE C 1 100 ? 8.873   33.025  40.063  1.00 17.53 ? 88  ILE C O   1 
ATOM   3650 C  CB  . ILE C 1 100 ? 11.393  32.178  41.348  1.00 18.34 ? 88  ILE C CB  1 
ATOM   3651 C  CG1 . ILE C 1 100 ? 12.903  32.048  41.486  1.00 18.55 ? 88  ILE C CG1 1 
ATOM   3652 C  CG2 . ILE C 1 100 ? 10.668  31.321  42.391  1.00 19.55 ? 88  ILE C CG2 1 
ATOM   3653 C  CD1 . ILE C 1 100 ? 13.458  32.767  42.710  1.00 19.80 ? 88  ILE C CD1 1 
ATOM   3654 N  N   . VAL C 1 101 ? 8.893   31.039  38.942  1.00 17.18 ? 89  VAL C N   1 
ATOM   3655 C  CA  . VAL C 1 101 ? 7.518   31.187  38.396  1.00 17.25 ? 89  VAL C CA  1 
ATOM   3656 C  C   . VAL C 1 101 ? 6.527   30.669  39.443  1.00 17.03 ? 89  VAL C C   1 
ATOM   3657 O  O   . VAL C 1 101 ? 6.558   29.432  39.703  1.00 18.85 ? 89  VAL C O   1 
ATOM   3658 C  CB  . VAL C 1 101 ? 7.326   30.444  37.078  1.00 16.52 ? 89  VAL C CB  1 
ATOM   3659 C  CG1 . VAL C 1 101 ? 5.936   30.710  36.522  1.00 15.19 ? 89  VAL C CG1 1 
ATOM   3660 C  CG2 . VAL C 1 101 ? 8.411   30.780  36.059  1.00 16.92 ? 89  VAL C CG2 1 
ATOM   3661 N  N   . GLU C 1 102 ? 5.688   31.558  39.943  1.00 17.41 ? 90  GLU C N   1 
ATOM   3662 C  CA  . GLU C 1 102 ? 4.647   31.269  40.967  1.00 18.62 ? 90  GLU C CA  1 
ATOM   3663 C  C   . GLU C 1 102 ? 3.370   30.762  40.276  1.00 19.90 ? 90  GLU C C   1 
ATOM   3664 O  O   . GLU C 1 102 ? 2.709   29.861  40.820  1.00 18.20 ? 90  GLU C O   1 
ATOM   3665 C  CB  . GLU C 1 102 ? 4.342   32.518  41.782  1.00 18.52 ? 90  GLU C CB  1 
ATOM   3666 C  CG  . GLU C 1 102 ? 5.529   32.959  42.637  1.00 20.88 ? 90  GLU C CG  1 
ATOM   3667 C  CD  . GLU C 1 102 ? 5.759   31.996  43.784  1.00 20.36 ? 90  GLU C CD  1 
ATOM   3668 O  OE1 . GLU C 1 102 ? 6.580   31.097  43.621  1.00 22.98 ? 90  GLU C OE1 1 
ATOM   3669 O  OE2 . GLU C 1 102 ? 5.037   32.108  44.811  1.00 26.40 ? 90  GLU C OE2 1 
ATOM   3670 N  N   . SER C 1 103 ? 2.961   31.418  39.198  1.00 18.46 ? 91  SER C N   1 
ATOM   3671 C  CA  . SER C 1 103 ? 1.846   30.977  38.320  1.00 19.30 ? 91  SER C CA  1 
ATOM   3672 C  C   . SER C 1 103 ? 2.249   31.154  36.867  1.00 18.41 ? 91  SER C C   1 
ATOM   3673 O  O   . SER C 1 103 ? 2.953   32.115  36.565  1.00 19.63 ? 91  SER C O   1 
ATOM   3674 C  CB  . SER C 1 103 ? 0.574   31.682  38.544  1.00 19.97 ? 91  SER C CB  1 
ATOM   3675 O  OG  . SER C 1 103 ? 0.014   31.413  39.819  1.00 21.25 ? 91  SER C OG  1 
ATOM   3676 N  N   . PHE C 1 104 ? 1.727   30.294  35.998  1.00 18.67 ? 92  PHE C N   1 
ATOM   3677 C  CA  . PHE C 1 104 ? 1.602   30.558  34.547  1.00 18.58 ? 92  PHE C CA  1 
ATOM   3678 C  C   . PHE C 1 104 ? 0.187   30.148  34.156  1.00 19.98 ? 92  PHE C C   1 
ATOM   3679 O  O   . PHE C 1 104 ? -0.522  29.440  34.911  1.00 22.43 ? 92  PHE C O   1 
ATOM   3680 C  CB  . PHE C 1 104 ? 2.717   29.928  33.723  1.00 18.51 ? 92  PHE C CB  1 
ATOM   3681 C  CG  . PHE C 1 104 ? 2.732   28.415  33.694  1.00 20.16 ? 92  PHE C CG  1 
ATOM   3682 C  CD1 . PHE C 1 104 ? 1.806   27.723  32.939  1.00 20.80 ? 92  PHE C CD1 1 
ATOM   3683 C  CD2 . PHE C 1 104 ? 3.656   27.692  34.426  1.00 20.97 ? 92  PHE C CD2 1 
ATOM   3684 C  CE1 . PHE C 1 104 ? 1.817   26.338  32.904  1.00 21.25 ? 92  PHE C CE1 1 
ATOM   3685 C  CE2 . PHE C 1 104 ? 3.673   26.302  34.377  1.00 23.01 ? 92  PHE C CE2 1 
ATOM   3686 C  CZ  . PHE C 1 104 ? 2.764   25.634  33.598  1.00 21.01 ? 92  PHE C CZ  1 
ATOM   3687 N  N   . SER C 1 105 ? -0.270  30.598  33.007  1.00 18.94 ? 93  SER C N   1 
ATOM   3688 C  CA  . SER C 1 105 ? -1.685  30.392  32.623  1.00 19.14 ? 93  SER C CA  1 
ATOM   3689 C  C   . SER C 1 105 ? -1.685  29.314  31.550  1.00 21.41 ? 93  SER C C   1 
ATOM   3690 O  O   . SER C 1 105 ? -1.508  28.126  31.909  1.00 22.76 ? 93  SER C O   1 
ATOM   3691 C  CB  . SER C 1 105 ? -2.345  31.689  32.207  1.00 21.99 ? 93  SER C CB  1 
ATOM   3692 O  OG  . SER C 1 105 ? -1.590  32.246  31.160  1.00 22.55 ? 93  SER C OG  1 
ATOM   3693 N  N   . THR C 1 106 ? -1.712  29.690  30.278  1.00 22.31 ? 94  THR C N   1 
ATOM   3694 C  CA  . THR C 1 106 ? -2.003  28.774  29.149  1.00 22.78 ? 94  THR C CA  1 
ATOM   3695 C  C   . THR C 1 106 ? -0.740  28.198  28.496  1.00 23.18 ? 94  THR C C   1 
ATOM   3696 O  O   . THR C 1 106 ? -0.895  27.269  27.674  1.00 28.02 ? 94  THR C O   1 
ATOM   3697 C  CB  . THR C 1 106 ? -2.921  29.500  28.164  1.00 22.58 ? 94  THR C CB  1 
ATOM   3698 O  OG1 . THR C 1 106 ? -2.238  30.680  27.752  1.00 23.00 ? 94  THR C OG1 1 
ATOM   3699 C  CG2 . THR C 1 106 ? -4.239  29.849  28.800  1.00 21.91 ? 94  THR C CG2 1 
ATOM   3700 N  N   . TYR C 1 107 ? 0.470   28.629  28.875  1.00 20.69 ? 95  TYR C N   1 
ATOM   3701 C  CA  . TYR C 1 107 ? 1.728   28.162  28.244  1.00 21.52 ? 95  TYR C CA  1 
ATOM   3702 C  C   . TYR C 1 107 ? 2.800   27.928  29.322  1.00 21.20 ? 95  TYR C C   1 
ATOM   3703 O  O   . TYR C 1 107 ? 3.017   28.845  30.103  1.00 22.71 ? 95  TYR C O   1 
ATOM   3704 C  CB  . TYR C 1 107 ? 2.181   29.135  27.163  1.00 20.54 ? 95  TYR C CB  1 
ATOM   3705 C  CG  . TYR C 1 107 ? 3.428   28.705  26.453  1.00 21.52 ? 95  TYR C CG  1 
ATOM   3706 C  CD1 . TYR C 1 107 ? 3.385   27.726  25.473  1.00 19.50 ? 95  TYR C CD1 1 
ATOM   3707 C  CD2 . TYR C 1 107 ? 4.667   29.201  26.816  1.00 21.64 ? 95  TYR C CD2 1 
ATOM   3708 C  CE1 . TYR C 1 107 ? 4.521   27.333  24.806  1.00 22.36 ? 95  TYR C CE1 1 
ATOM   3709 C  CE2 . TYR C 1 107 ? 5.824   28.783  26.195  1.00 23.21 ? 95  TYR C CE2 1 
ATOM   3710 C  CZ  . TYR C 1 107 ? 5.751   27.835  25.186  1.00 22.43 ? 95  TYR C CZ  1 
ATOM   3711 O  OH  . TYR C 1 107 ? 6.873   27.404  24.589  1.00 26.21 ? 95  TYR C OH  1 
ATOM   3712 N  N   . ASP C 1 108 ? 3.337   26.717  29.392  1.00 22.02 ? 96  ASP C N   1 
ATOM   3713 C  CA  . ASP C 1 108 ? 4.449   26.330  30.310  1.00 23.78 ? 96  ASP C CA  1 
ATOM   3714 C  C   . ASP C 1 108 ? 5.775   26.804  29.711  1.00 25.50 ? 96  ASP C C   1 
ATOM   3715 O  O   . ASP C 1 108 ? 6.211   26.307  28.686  1.00 23.35 ? 96  ASP C O   1 
ATOM   3716 C  CB  . ASP C 1 108 ? 4.505   24.809  30.550  1.00 24.23 ? 96  ASP C CB  1 
ATOM   3717 C  CG  . ASP C 1 108 ? 5.531   24.405  31.610  1.00 26.30 ? 96  ASP C CG  1 
ATOM   3718 O  OD1 . ASP C 1 108 ? 6.438   25.204  31.882  1.00 28.26 ? 96  ASP C OD1 1 
ATOM   3719 O  OD2 . ASP C 1 108 ? 5.399   23.305  32.188  1.00 28.99 ? 96  ASP C OD2 1 
ATOM   3720 N  N   . PRO C 1 109 ? 6.466   27.766  30.355  1.00 29.47 ? 97  PRO C N   1 
ATOM   3721 C  CA  . PRO C 1 109 ? 7.787   28.235  29.909  1.00 33.45 ? 97  PRO C CA  1 
ATOM   3722 C  C   . PRO C 1 109 ? 8.927   27.228  29.710  1.00 37.64 ? 97  PRO C C   1 
ATOM   3723 O  O   . PRO C 1 109 ? 9.852   27.546  28.982  1.00 39.92 ? 97  PRO C O   1 
ATOM   3724 C  CB  . PRO C 1 109 ? 8.267   29.102  31.086  1.00 33.39 ? 97  PRO C CB  1 
ATOM   3725 C  CG  . PRO C 1 109 ? 7.326   28.782  32.239  1.00 32.82 ? 97  PRO C CG  1 
ATOM   3726 C  CD  . PRO C 1 109 ? 6.013   28.441  31.574  1.00 29.33 ? 97  PRO C CD  1 
ATOM   3727 N  N   . SER C 1 110 ? 8.885   26.096  30.413  1.00 35.79 ? 98  SER C N   1 
ATOM   3728 C  CA  . SER C 1 110 ? 9.949   25.060  30.408  1.00 37.30 ? 98  SER C CA  1 
ATOM   3729 C  C   . SER C 1 110 ? 9.754   24.075  29.253  1.00 36.10 ? 98  SER C C   1 
ATOM   3730 O  O   . SER C 1 110 ? 10.500  23.057  29.216  1.00 38.62 ? 98  SER C O   1 
ATOM   3731 C  CB  . SER C 1 110 ? 9.975   24.330  31.720  1.00 34.84 ? 98  SER C CB  1 
ATOM   3732 O  OG  . SER C 1 110 ? 8.726   23.685  31.972  1.00 37.98 ? 98  SER C OG  1 
ATOM   3733 N  N   . THR C 1 111 ? 8.758   24.288  28.381  1.00 32.92 ? 99  THR C N   1 
ATOM   3734 C  CA  . THR C 1 111 ? 8.476   23.351  27.262  1.00 33.74 ? 99  THR C CA  1 
ATOM   3735 C  C   . THR C 1 111 ? 9.764   23.151  26.439  1.00 32.95 ? 99  THR C C   1 
ATOM   3736 O  O   . THR C 1 111 ? 10.382  24.152  26.060  1.00 33.21 ? 99  THR C O   1 
ATOM   3737 C  CB  . THR C 1 111 ? 7.292   23.855  26.422  1.00 30.61 ? 99  THR C CB  1 
ATOM   3738 O  OG1 . THR C 1 111 ? 6.199   24.080  27.324  1.00 27.93 ? 99  THR C OG1 1 
ATOM   3739 C  CG2 . THR C 1 111 ? 6.930   22.888  25.314  1.00 29.73 ? 99  THR C CG2 1 
ATOM   3740 N  N   . GLY C 1 112 ? 10.184  21.899  26.227  1.00 35.14 ? 100 GLY C N   1 
ATOM   3741 C  CA  . GLY C 1 112 ? 11.330  21.553  25.358  1.00 38.10 ? 100 GLY C CA  1 
ATOM   3742 C  C   . GLY C 1 112 ? 12.658  21.504  26.107  1.00 37.76 ? 100 GLY C C   1 
ATOM   3743 O  O   . GLY C 1 112 ? 13.684  21.156  25.462  1.00 36.44 ? 100 GLY C O   1 
ATOM   3744 N  N   . ALA C 1 113 ? 12.671  21.862  27.395  1.00 34.84 ? 101 ALA C N   1 
ATOM   3745 C  CA  . ALA C 1 113 ? 13.906  21.903  28.224  1.00 34.95 ? 101 ALA C CA  1 
ATOM   3746 C  C   . ALA C 1 113 ? 14.021  20.665  29.119  1.00 35.67 ? 101 ALA C C   1 
ATOM   3747 O  O   . ALA C 1 113 ? 12.987  20.210  29.675  1.00 34.67 ? 101 ALA C O   1 
ATOM   3748 C  CB  . ALA C 1 113 ? 13.943  23.156  29.052  1.00 30.95 ? 101 ALA C CB  1 
ATOM   3749 N  N   . GLN C 1 114 ? 15.257  20.187  29.300  1.00 37.53 ? 102 GLN C N   1 
ATOM   3750 C  CA  . GLN C 1 114 ? 15.597  19.057  30.208  1.00 38.99 ? 102 GLN C CA  1 
ATOM   3751 C  C   . GLN C 1 114 ? 15.340  19.508  31.649  1.00 35.88 ? 102 GLN C C   1 
ATOM   3752 O  O   . GLN C 1 114 ? 15.817  20.595  32.046  1.00 32.54 ? 102 GLN C O   1 
ATOM   3753 C  CB  . GLN C 1 114 ? 17.053  18.607  30.030  1.00 41.25 ? 102 GLN C CB  1 
ATOM   3754 C  CG  . GLN C 1 114 ? 17.328  17.216  30.597  1.00 46.48 ? 102 GLN C CG  1 
ATOM   3755 C  CD  . GLN C 1 114 ? 18.791  16.955  30.868  1.00 47.74 ? 102 GLN C CD  1 
ATOM   3756 O  OE1 . GLN C 1 114 ? 19.671  17.628  30.332  1.00 51.88 ? 102 GLN C OE1 1 
ATOM   3757 N  NE2 . GLN C 1 114 ? 19.057  15.959  31.703  1.00 44.95 ? 102 GLN C NE2 1 
ATOM   3758 N  N   . GLU C 1 115 ? 14.581  18.721  32.402  1.00 34.21 ? 103 GLU C N   1 
ATOM   3759 C  CA  . GLU C 1 115 ? 14.422  18.963  33.852  1.00 33.62 ? 103 GLU C CA  1 
ATOM   3760 C  C   . GLU C 1 115 ? 15.762  18.647  34.504  1.00 31.38 ? 103 GLU C C   1 
ATOM   3761 O  O   . GLU C 1 115 ? 16.334  17.606  34.174  1.00 34.22 ? 103 GLU C O   1 
ATOM   3762 C  CB  . GLU C 1 115 ? 13.264  18.144  34.403  1.00 35.15 ? 103 GLU C CB  1 
ATOM   3763 C  CG  . GLU C 1 115 ? 13.059  18.313  35.894  1.00 38.03 ? 103 GLU C CG  1 
ATOM   3764 C  CD  . GLU C 1 115 ? 11.768  17.670  36.380  1.00 41.77 ? 103 GLU C CD  1 
ATOM   3765 O  OE1 . GLU C 1 115 ? 11.646  17.451  37.605  1.00 44.58 ? 103 GLU C OE1 1 
ATOM   3766 O  OE2 . GLU C 1 115 ? 10.877  17.429  35.530  1.00 39.14 ? 103 GLU C OE2 1 
ATOM   3767 N  N   . LEU C 1 116 ? 16.244  19.510  35.397  1.00 28.78 ? 104 LEU C N   1 
ATOM   3768 C  CA  . LEU C 1 116 ? 17.587  19.366  36.027  1.00 30.04 ? 104 LEU C CA  1 
ATOM   3769 C  C   . LEU C 1 116 ? 17.469  18.989  37.508  1.00 34.96 ? 104 LEU C C   1 
ATOM   3770 O  O   . LEU C 1 116 ? 18.525  18.751  38.113  1.00 39.26 ? 104 LEU C O   1 
ATOM   3771 C  CB  . LEU C 1 116 ? 18.363  20.675  35.865  1.00 30.30 ? 104 LEU C CB  1 
ATOM   3772 C  CG  . LEU C 1 116 ? 18.733  21.059  34.434  1.00 32.69 ? 104 LEU C CG  1 
ATOM   3773 C  CD1 . LEU C 1 116 ? 19.545  22.336  34.407  1.00 31.76 ? 104 LEU C CD1 1 
ATOM   3774 C  CD2 . LEU C 1 116 ? 19.498  19.950  33.730  1.00 30.84 ? 104 LEU C CD2 1 
ATOM   3775 N  N   . GLY C 1 117 ? 16.260  18.920  38.073  1.00 33.77 ? 105 GLY C N   1 
ATOM   3776 C  CA  . GLY C 1 117 ? 16.063  18.705  39.521  1.00 32.30 ? 105 GLY C CA  1 
ATOM   3777 C  C   . GLY C 1 117 ? 14.817  19.399  40.034  1.00 33.36 ? 105 GLY C C   1 
ATOM   3778 O  O   . GLY C 1 117 ? 14.026  19.928  39.196  1.00 28.90 ? 105 GLY C O   1 
ATOM   3779 N  N   . THR C 1 118 ? 14.623  19.384  41.357  1.00 32.14 ? 106 THR C N   1 
ATOM   3780 C  CA  . THR C 1 118 ? 13.497  20.070  42.051  1.00 32.36 ? 106 THR C CA  1 
ATOM   3781 C  C   . THR C 1 118 ? 14.033  20.755  43.300  1.00 29.53 ? 106 THR C C   1 
ATOM   3782 O  O   . THR C 1 118 ? 15.105  20.300  43.794  1.00 33.00 ? 106 THR C O   1 
ATOM   3783 C  CB  . THR C 1 118 ? 12.372  19.132  42.500  1.00 36.59 ? 106 THR C CB  1 
ATOM   3784 O  OG1 . THR C 1 118 ? 13.037  18.115  43.245  1.00 39.26 ? 106 THR C OG1 1 
ATOM   3785 C  CG2 . THR C 1 118 ? 11.555  18.569  41.359  1.00 36.48 ? 106 THR C CG2 1 
ATOM   3786 N  N   . VAL C 1 119 ? 13.361  21.828  43.747  1.00 27.44 ? 107 VAL C N   1 
ATOM   3787 C  CA  . VAL C 1 119 ? 13.606  22.454  45.073  1.00 27.31 ? 107 VAL C CA  1 
ATOM   3788 C  C   . VAL C 1 119 ? 12.269  22.523  45.831  1.00 27.02 ? 107 VAL C C   1 
ATOM   3789 O  O   . VAL C 1 119 ? 11.214  22.835  45.220  1.00 24.03 ? 107 VAL C O   1 
ATOM   3790 C  CB  . VAL C 1 119 ? 14.302  23.827  44.929  1.00 31.30 ? 107 VAL C CB  1 
ATOM   3791 C  CG1 . VAL C 1 119 ? 13.600  24.768  43.959  1.00 29.67 ? 107 VAL C CG1 1 
ATOM   3792 C  CG2 . VAL C 1 119 ? 14.506  24.518  46.266  1.00 31.69 ? 107 VAL C CG2 1 
ATOM   3793 N  N   . GLU C 1 120 ? 12.302  22.175  47.108  1.00 28.07 ? 108 GLU C N   1 
ATOM   3794 C  CA  . GLU C 1 120 ? 11.157  22.270  48.040  1.00 29.18 ? 108 GLU C CA  1 
ATOM   3795 C  C   . GLU C 1 120 ? 11.390  23.528  48.876  1.00 27.34 ? 108 GLU C C   1 
ATOM   3796 O  O   . GLU C 1 120 ? 12.448  23.620  49.510  1.00 24.05 ? 108 GLU C O   1 
ATOM   3797 C  CB  . GLU C 1 120 ? 11.072  21.037  48.946  1.00 34.54 ? 108 GLU C CB  1 
ATOM   3798 C  CG  . GLU C 1 120 ? 11.343  19.709  48.247  1.00 40.76 ? 108 GLU C CG  1 
ATOM   3799 C  CD  . GLU C 1 120 ? 10.423  19.318  47.098  1.00 45.11 ? 108 GLU C CD  1 
ATOM   3800 O  OE1 . GLU C 1 120 ? 9.205   19.097  47.342  1.00 46.20 ? 108 GLU C OE1 1 
ATOM   3801 O  OE2 . GLU C 1 120 ? 10.928  19.206  45.955  1.00 55.57 ? 108 GLU C OE2 1 
ATOM   3802 N  N   . THR C 1 121 ? 10.490  24.493  48.802  1.00 26.12 ? 109 THR C N   1 
ATOM   3803 C  CA  . THR C 1 121 ? 10.626  25.796  49.484  1.00 26.71 ? 109 THR C CA  1 
ATOM   3804 C  C   . THR C 1 121 ? 9.249   26.463  49.529  1.00 25.69 ? 109 THR C C   1 
ATOM   3805 O  O   . THR C 1 121 ? 8.441   26.281  48.569  1.00 24.43 ? 109 THR C O   1 
ATOM   3806 C  CB  . THR C 1 121 ? 11.754  26.617  48.842  1.00 27.87 ? 109 THR C CB  1 
ATOM   3807 O  OG1 . THR C 1 121 ? 11.918  27.826  49.582  1.00 27.39 ? 109 THR C OG1 1 
ATOM   3808 C  CG2 . THR C 1 121 ? 11.483  26.965  47.399  1.00 28.06 ? 109 THR C CG2 1 
ATOM   3809 N  N   . ASP C 1 122 ? 8.986   27.199  50.615  1.00 27.68 ? 110 ASP C N   1 
ATOM   3810 C  CA  . ASP C 1 122 ? 7.784   28.058  50.761  1.00 24.89 ? 110 ASP C CA  1 
ATOM   3811 C  C   . ASP C 1 122 ? 6.535   27.197  50.487  1.00 26.81 ? 110 ASP C C   1 
ATOM   3812 O  O   . ASP C 1 122 ? 5.670   27.621  49.698  1.00 24.32 ? 110 ASP C O   1 
ATOM   3813 C  CB  . ASP C 1 122 ? 7.942   29.315  49.893  1.00 24.82 ? 110 ASP C CB  1 
ATOM   3814 C  CG  . ASP C 1 122 ? 9.266   30.040  50.149  1.00 23.99 ? 110 ASP C CG  1 
ATOM   3815 O  OD1 . ASP C 1 122 ? 9.428   30.541  51.282  1.00 25.46 ? 110 ASP C OD1 1 
ATOM   3816 O  OD2 . ASP C 1 122 ? 10.154  30.058  49.236  1.00 22.25 ? 110 ASP C OD2 1 
ATOM   3817 N  N   . ASP C 1 123 ? 6.475   26.012  51.122  1.00 28.28 ? 111 ASP C N   1 
ATOM   3818 C  CA  . ASP C 1 123 ? 5.354   25.020  51.101  1.00 30.20 ? 111 ASP C CA  1 
ATOM   3819 C  C   . ASP C 1 123 ? 4.999   24.634  49.658  1.00 28.63 ? 111 ASP C C   1 
ATOM   3820 O  O   . ASP C 1 123 ? 3.801   24.346  49.350  1.00 26.48 ? 111 ASP C O   1 
ATOM   3821 C  CB  . ASP C 1 123 ? 4.150   25.510  51.914  1.00 37.84 ? 111 ASP C CB  1 
ATOM   3822 C  CG  . ASP C 1 123 ? 4.061   24.844  53.282  1.00 44.87 ? 111 ASP C CG  1 
ATOM   3823 O  OD1 . ASP C 1 123 ? 5.113   24.773  53.979  1.00 51.68 ? 111 ASP C OD1 1 
ATOM   3824 O  OD2 . ASP C 1 123 ? 2.956   24.372  53.635  1.00 53.94 ? 111 ASP C OD2 1 
ATOM   3825 N  N   . GLY C 1 124 ? 6.012   24.581  48.792  1.00 28.12 ? 112 GLY C N   1 
ATOM   3826 C  CA  . GLY C 1 124 ? 5.845   24.196  47.387  1.00 25.48 ? 112 GLY C CA  1 
ATOM   3827 C  C   . GLY C 1 124 ? 7.014   23.375  46.886  1.00 25.38 ? 112 GLY C C   1 
ATOM   3828 O  O   . GLY C 1 124 ? 8.074   23.298  47.565  1.00 27.65 ? 112 GLY C O   1 
ATOM   3829 N  N   . THR C 1 125 ? 6.835   22.826  45.699  1.00 23.61 ? 113 THR C N   1 
ATOM   3830 C  CA  . THR C 1 125 ? 7.881   22.204  44.889  1.00 23.27 ? 113 THR C CA  1 
ATOM   3831 C  C   . THR C 1 125 ? 8.028   22.964  43.582  1.00 21.53 ? 113 THR C C   1 
ATOM   3832 O  O   . THR C 1 125 ? 7.003   23.294  42.942  1.00 20.15 ? 113 THR C O   1 
ATOM   3833 C  CB  . THR C 1 125 ? 7.548   20.730  44.622  1.00 26.01 ? 113 THR C CB  1 
ATOM   3834 O  OG1 . THR C 1 125 ? 7.289   20.215  45.925  1.00 25.83 ? 113 THR C OG1 1 
ATOM   3835 C  CG2 . THR C 1 125 ? 8.653   20.002  43.891  1.00 26.47 ? 113 THR C CG2 1 
ATOM   3836 N  N   . TYR C 1 126 ? 9.267   23.128  43.161  1.00 21.98 ? 114 TYR C N   1 
ATOM   3837 C  CA  . TYR C 1 126 ? 9.632   23.843  41.918  1.00 23.22 ? 114 TYR C CA  1 
ATOM   3838 C  C   . TYR C 1 126 ? 10.581  22.969  41.104  1.00 21.84 ? 114 TYR C C   1 
ATOM   3839 O  O   . TYR C 1 126 ? 11.572  22.464  41.648  1.00 23.90 ? 114 TYR C O   1 
ATOM   3840 C  CB  . TYR C 1 126 ? 10.294  25.200  42.210  1.00 22.98 ? 114 TYR C CB  1 
ATOM   3841 C  CG  . TYR C 1 126 ? 9.490   26.221  42.971  1.00 20.32 ? 114 TYR C CG  1 
ATOM   3842 C  CD1 . TYR C 1 126 ? 9.273   26.113  44.329  1.00 19.76 ? 114 TYR C CD1 1 
ATOM   3843 C  CD2 . TYR C 1 126 ? 9.029   27.365  42.346  1.00 20.24 ? 114 TYR C CD2 1 
ATOM   3844 C  CE1 . TYR C 1 126 ? 8.535   27.053  45.016  1.00 18.82 ? 114 TYR C CE1 1 
ATOM   3845 C  CE2 . TYR C 1 126 ? 8.316   28.353  43.032  1.00 20.51 ? 114 TYR C CE2 1 
ATOM   3846 C  CZ  . TYR C 1 126 ? 8.084   28.195  44.384  1.00 18.63 ? 114 TYR C CZ  1 
ATOM   3847 O  OH  . TYR C 1 126 ? 7.368   29.100  45.084  1.00 19.44 ? 114 TYR C OH  1 
ATOM   3848 N  N   . LYS C 1 127 ? 10.251  22.785  39.828  1.00 22.21 ? 115 LYS C N   1 
ATOM   3849 C  CA  . LYS C 1 127 ? 11.078  22.066  38.831  1.00 23.88 ? 115 LYS C CA  1 
ATOM   3850 C  C   . LYS C 1 127 ? 12.078  23.061  38.246  1.00 23.65 ? 115 LYS C C   1 
ATOM   3851 O  O   . LYS C 1 127 ? 11.658  24.171  37.927  1.00 23.53 ? 115 LYS C O   1 
ATOM   3852 C  CB  . LYS C 1 127 ? 10.184  21.454  37.750  1.00 25.28 ? 115 LYS C CB  1 
ATOM   3853 C  CG  . LYS C 1 127 ? 9.204   20.411  38.283  1.00 30.47 ? 115 LYS C CG  1 
ATOM   3854 C  CD  . LYS C 1 127 ? 8.418   19.717  37.178  1.00 32.38 ? 115 LYS C CD  1 
ATOM   3855 C  CE  . LYS C 1 127 ? 7.478   18.646  37.680  1.00 35.66 ? 115 LYS C CE  1 
ATOM   3856 N  NZ  . LYS C 1 127 ? 6.367   18.446  36.723  1.00 36.55 ? 115 LYS C NZ  1 
ATOM   3857 N  N   . ILE C 1 128 ? 13.334  22.656  38.090  1.00 21.91 ? 116 ILE C N   1 
ATOM   3858 C  CA  . ILE C 1 128 ? 14.469  23.488  37.620  1.00 22.90 ? 116 ILE C CA  1 
ATOM   3859 C  C   . ILE C 1 128 ? 14.764  23.185  36.153  1.00 22.35 ? 116 ILE C C   1 
ATOM   3860 O  O   . ILE C 1 128 ? 14.841  21.980  35.759  1.00 24.85 ? 116 ILE C O   1 
ATOM   3861 C  CB  . ILE C 1 128 ? 15.712  23.239  38.485  1.00 23.38 ? 116 ILE C CB  1 
ATOM   3862 C  CG1 . ILE C 1 128 ? 15.429  23.635  39.935  1.00 25.37 ? 116 ILE C CG1 1 
ATOM   3863 C  CG2 . ILE C 1 128 ? 16.923  23.920  37.885  1.00 24.49 ? 116 ILE C CG2 1 
ATOM   3864 C  CD1 . ILE C 1 128 ? 16.375  23.042  40.917  1.00 25.37 ? 116 ILE C CD1 1 
ATOM   3865 N  N   . TYR C 1 129 ? 14.950  24.240  35.371  1.00 20.62 ? 117 TYR C N   1 
ATOM   3866 C  CA  . TYR C 1 129 ? 15.269  24.150  33.930  1.00 21.69 ? 117 TYR C CA  1 
ATOM   3867 C  C   . TYR C 1 129 ? 16.228  25.259  33.544  1.00 23.85 ? 117 TYR C C   1 
ATOM   3868 O  O   . TYR C 1 129 ? 16.276  26.347  34.184  1.00 23.72 ? 117 TYR C O   1 
ATOM   3869 C  CB  . TYR C 1 129 ? 14.046  24.301  33.022  1.00 22.85 ? 117 TYR C CB  1 
ATOM   3870 C  CG  . TYR C 1 129 ? 12.869  23.442  33.376  1.00 22.91 ? 117 TYR C CG  1 
ATOM   3871 C  CD1 . TYR C 1 129 ? 11.974  23.839  34.349  1.00 23.74 ? 117 TYR C CD1 1 
ATOM   3872 C  CD2 . TYR C 1 129 ? 12.702  22.200  32.784  1.00 26.67 ? 117 TYR C CD2 1 
ATOM   3873 C  CE1 . TYR C 1 129 ? 10.878  23.064  34.675  1.00 26.93 ? 117 TYR C CE1 1 
ATOM   3874 C  CE2 . TYR C 1 129 ? 11.613  21.401  33.109  1.00 26.33 ? 117 TYR C CE2 1 
ATOM   3875 C  CZ  . TYR C 1 129 ? 10.716  21.829  34.070  1.00 28.01 ? 117 TYR C CZ  1 
ATOM   3876 O  OH  . TYR C 1 129 ? 9.634   21.064  34.391  1.00 30.76 ? 117 TYR C OH  1 
ATOM   3877 N  N   . GLN C 1 130 ? 16.937  24.983  32.463  1.00 24.80 ? 118 GLN C N   1 
ATOM   3878 C  CA  . GLN C 1 130 ? 17.799  25.966  31.781  1.00 25.69 ? 118 GLN C CA  1 
ATOM   3879 C  C   . GLN C 1 130 ? 17.460  25.918  30.301  1.00 26.11 ? 118 GLN C C   1 
ATOM   3880 O  O   . GLN C 1 130 ? 17.347  24.778  29.747  1.00 28.87 ? 118 GLN C O   1 
ATOM   3881 C  CB  . GLN C 1 130 ? 19.284  25.710  32.035  1.00 28.37 ? 118 GLN C CB  1 
ATOM   3882 C  CG  . GLN C 1 130 ? 20.146  26.194  30.885  1.00 33.89 ? 118 GLN C CG  1 
ATOM   3883 C  CD  . GLN C 1 130 ? 21.608  25.990  31.167  1.00 38.33 ? 118 GLN C CD  1 
ATOM   3884 O  OE1 . GLN C 1 130 ? 22.056  24.874  31.414  1.00 43.82 ? 118 GLN C OE1 1 
ATOM   3885 N  NE2 . GLN C 1 130 ? 22.354  27.077  31.152  1.00 36.50 ? 118 GLN C NE2 1 
ATOM   3886 N  N   . THR C 1 131 ? 17.290  27.107  29.728  1.00 25.79 ? 119 THR C N   1 
ATOM   3887 C  CA  . THR C 1 131 ? 17.074  27.371  28.282  1.00 27.57 ? 119 THR C CA  1 
ATOM   3888 C  C   . THR C 1 131 ? 18.085  28.444  27.834  1.00 29.05 ? 119 THR C C   1 
ATOM   3889 O  O   . THR C 1 131 ? 18.886  28.927  28.676  1.00 26.52 ? 119 THR C O   1 
ATOM   3890 C  CB  . THR C 1 131 ? 15.616  27.782  28.011  1.00 29.79 ? 119 THR C CB  1 
ATOM   3891 O  OG1 . THR C 1 131 ? 15.279  28.994  28.700  1.00 27.87 ? 119 THR C OG1 1 
ATOM   3892 C  CG2 . THR C 1 131 ? 14.612  26.709  28.382  1.00 32.24 ? 119 THR C CG2 1 
ATOM   3893 N  N   . THR C 1 132 ? 18.061  28.772  26.544  1.00 30.99 ? 120 THR C N   1 
ATOM   3894 C  CA  . THR C 1 132 ? 19.031  29.676  25.879  1.00 35.31 ? 120 THR C CA  1 
ATOM   3895 C  C   . THR C 1 132 ? 18.236  30.680  25.057  1.00 35.02 ? 120 THR C C   1 
ATOM   3896 O  O   . THR C 1 132 ? 17.269  30.255  24.398  1.00 39.10 ? 120 THR C O   1 
ATOM   3897 C  CB  . THR C 1 132 ? 20.046  28.874  25.049  1.00 35.87 ? 120 THR C CB  1 
ATOM   3898 O  OG1 . THR C 1 132 ? 20.948  28.308  25.998  1.00 37.01 ? 120 THR C OG1 1 
ATOM   3899 C  CG2 . THR C 1 132 ? 20.842  29.700  24.065  1.00 42.00 ? 120 THR C CG2 1 
ATOM   3900 N  N   . ARG C 1 133 ? 18.642  31.951  25.112  1.00 33.29 ? 121 ARG C N   1 
ATOM   3901 C  CA  . ARG C 1 133 ? 18.079  33.071  24.316  1.00 31.73 ? 121 ARG C CA  1 
ATOM   3902 C  C   . ARG C 1 133 ? 19.183  33.613  23.398  1.00 30.31 ? 121 ARG C C   1 
ATOM   3903 O  O   . ARG C 1 133 ? 20.262  33.948  23.901  1.00 32.76 ? 121 ARG C O   1 
ATOM   3904 C  CB  . ARG C 1 133 ? 17.498  34.124  25.260  1.00 30.63 ? 121 ARG C CB  1 
ATOM   3905 C  CG  . ARG C 1 133 ? 16.230  33.676  25.980  1.00 30.60 ? 121 ARG C CG  1 
ATOM   3906 C  CD  . ARG C 1 133 ? 14.974  33.824  25.125  1.00 28.66 ? 121 ARG C CD  1 
ATOM   3907 N  NE  . ARG C 1 133 ? 14.610  35.239  25.008  1.00 30.43 ? 121 ARG C NE  1 
ATOM   3908 C  CZ  . ARG C 1 133 ? 13.981  35.789  23.967  1.00 33.66 ? 121 ARG C CZ  1 
ATOM   3909 N  NH1 . ARG C 1 133 ? 13.658  35.064  22.904  1.00 37.30 ? 121 ARG C NH1 1 
ATOM   3910 N  NH2 . ARG C 1 133 ? 13.749  37.092  23.960  1.00 36.01 ? 121 ARG C NH2 1 
ATOM   3911 N  N   . GLU C 1 134 ? 18.922  33.656  22.093  1.00 32.51 ? 122 GLU C N   1 
ATOM   3912 C  CA  . GLU C 1 134 ? 19.885  34.108  21.045  1.00 33.40 ? 122 GLU C CA  1 
ATOM   3913 C  C   . GLU C 1 134 ? 19.411  35.436  20.436  1.00 31.34 ? 122 GLU C C   1 
ATOM   3914 O  O   . GLU C 1 134 ? 18.229  35.519  20.073  1.00 30.69 ? 122 GLU C O   1 
ATOM   3915 C  CB  . GLU C 1 134 ? 20.008  33.050  19.950  1.00 38.06 ? 122 GLU C CB  1 
ATOM   3916 C  CG  . GLU C 1 134 ? 20.146  31.631  20.468  1.00 42.48 ? 122 GLU C CG  1 
ATOM   3917 C  CD  . GLU C 1 134 ? 20.863  30.710  19.500  1.00 48.12 ? 122 GLU C CD  1 
ATOM   3918 O  OE1 . GLU C 1 134 ? 22.002  30.305  19.822  1.00 51.56 ? 122 GLU C OE1 1 
ATOM   3919 O  OE2 . GLU C 1 134 ? 20.292  30.419  18.419  1.00 51.50 ? 122 GLU C OE2 1 
ATOM   3920 N  N   . ASN C 1 135 ? 20.311  36.419  20.289  1.00 34.42 ? 123 ASN C N   1 
ATOM   3921 C  CA  . ASN C 1 135 ? 20.032  37.747  19.669  1.00 33.69 ? 123 ASN C CA  1 
ATOM   3922 C  C   . ASN C 1 135 ? 18.684  38.261  20.182  1.00 31.56 ? 123 ASN C C   1 
ATOM   3923 O  O   . ASN C 1 135 ? 17.799  38.599  19.372  1.00 30.48 ? 123 ASN C O   1 
ATOM   3924 C  CB  . ASN C 1 135 ? 20.119  37.680  18.139  1.00 36.34 ? 123 ASN C CB  1 
ATOM   3925 C  CG  . ASN C 1 135 ? 21.551  37.498  17.683  1.00 39.20 ? 123 ASN C CG  1 
ATOM   3926 O  OD1 . ASN C 1 135 ? 22.446  37.316  18.506  1.00 42.98 ? 123 ASN C OD1 1 
ATOM   3927 N  ND2 . ASN C 1 135 ? 21.784  37.548  16.386  1.00 44.22 ? 123 ASN C ND2 1 
ATOM   3928 N  N   . ALA C 1 136 ? 18.558  38.341  21.506  1.00 29.42 ? 124 ALA C N   1 
ATOM   3929 C  CA  . ALA C 1 136 ? 17.307  38.695  22.214  1.00 27.96 ? 124 ALA C CA  1 
ATOM   3930 C  C   . ALA C 1 136 ? 17.512  39.971  23.032  1.00 27.09 ? 124 ALA C C   1 
ATOM   3931 O  O   . ALA C 1 136 ? 18.632  40.306  23.423  1.00 27.81 ? 124 ALA C O   1 
ATOM   3932 C  CB  . ALA C 1 136 ? 16.878  37.536  23.083  1.00 25.73 ? 124 ALA C CB  1 
ATOM   3933 N  N   . PRO C 1 137 ? 16.424  40.728  23.302  1.00 27.16 ? 125 PRO C N   1 
ATOM   3934 C  CA  . PRO C 1 137 ? 16.482  41.848  24.228  1.00 29.27 ? 125 PRO C CA  1 
ATOM   3935 C  C   . PRO C 1 137 ? 17.078  41.406  25.565  1.00 27.56 ? 125 PRO C C   1 
ATOM   3936 O  O   . PRO C 1 137 ? 16.832  40.313  26.033  1.00 24.90 ? 125 PRO C O   1 
ATOM   3937 C  CB  . PRO C 1 137 ? 15.027  42.277  24.421  1.00 29.86 ? 125 PRO C CB  1 
ATOM   3938 C  CG  . PRO C 1 137 ? 14.312  41.758  23.188  1.00 30.79 ? 125 PRO C CG  1 
ATOM   3939 C  CD  . PRO C 1 137 ? 15.070  40.529  22.749  1.00 31.53 ? 125 PRO C CD  1 
ATOM   3940 N  N   . SER C 1 138 ? 17.859  42.283  26.174  1.00 24.09 ? 126 SER C N   1 
ATOM   3941 C  CA  . SER C 1 138 ? 18.389  42.023  27.530  1.00 23.19 ? 126 SER C CA  1 
ATOM   3942 C  C   . SER C 1 138 ? 18.718  43.357  28.191  1.00 20.70 ? 126 SER C C   1 
ATOM   3943 O  O   . SER C 1 138 ? 18.489  44.430  27.549  1.00 23.13 ? 126 SER C O   1 
ATOM   3944 C  CB  . SER C 1 138 ? 19.572  41.087  27.521  1.00 23.60 ? 126 SER C CB  1 
ATOM   3945 O  OG  . SER C 1 138 ? 20.778  41.734  27.109  1.00 26.54 ? 126 SER C OG  1 
ATOM   3946 N  N   . ILE C 1 139 ? 19.211  43.291  29.428  1.00 20.77 ? 127 ILE C N   1 
ATOM   3947 C  CA  . ILE C 1 139 ? 19.702  44.475  30.192  1.00 24.73 ? 127 ILE C CA  1 
ATOM   3948 C  C   . ILE C 1 139 ? 21.021  44.983  29.596  1.00 26.40 ? 127 ILE C C   1 
ATOM   3949 O  O   . ILE C 1 139 ? 21.426  46.092  29.975  1.00 26.94 ? 127 ILE C O   1 
ATOM   3950 C  CB  . ILE C 1 139 ? 19.839  44.165  31.694  1.00 23.45 ? 127 ILE C CB  1 
ATOM   3951 C  CG1 . ILE C 1 139 ? 20.714  42.937  31.965  1.00 22.86 ? 127 ILE C CG1 1 
ATOM   3952 C  CG2 . ILE C 1 139 ? 18.423  44.063  32.275  1.00 23.36 ? 127 ILE C CG2 1 
ATOM   3953 C  CD1 . ILE C 1 139 ? 21.354  42.875  33.325  1.00 24.22 ? 127 ILE C CD1 1 
ATOM   3954 N  N   . GLU C 1 140 ? 21.637  44.225  28.693  1.00 27.04 ? 128 GLU C N   1 
ATOM   3955 C  CA  . GLU C 1 140 ? 22.881  44.658  27.990  1.00 28.61 ? 128 GLU C CA  1 
ATOM   3956 C  C   . GLU C 1 140 ? 22.573  44.978  26.518  1.00 28.29 ? 128 GLU C C   1 
ATOM   3957 O  O   . GLU C 1 140 ? 23.533  45.160  25.746  1.00 32.80 ? 128 GLU C O   1 
ATOM   3958 C  CB  . GLU C 1 140 ? 23.948  43.570  28.150  1.00 29.86 ? 128 GLU C CB  1 
ATOM   3959 C  CG  . GLU C 1 140 ? 24.451  43.424  29.577  1.00 32.32 ? 128 GLU C CG  1 
ATOM   3960 C  CD  . GLU C 1 140 ? 25.640  42.490  29.756  1.00 33.23 ? 128 GLU C CD  1 
ATOM   3961 O  OE1 . GLU C 1 140 ? 26.099  42.316  30.905  1.00 34.08 ? 128 GLU C OE1 1 
ATOM   3962 O  OE2 . GLU C 1 140 ? 26.134  41.968  28.734  1.00 37.83 ? 128 GLU C OE2 1 
ATOM   3963 N  N   . GLY C 1 141 ? 21.304  45.013  26.122  1.00 24.79 ? 129 GLY C N   1 
ATOM   3964 C  CA  . GLY C 1 141 ? 20.867  45.154  24.719  1.00 26.51 ? 129 GLY C CA  1 
ATOM   3965 C  C   . GLY C 1 141 ? 20.834  43.806  24.032  1.00 29.47 ? 129 GLY C C   1 
ATOM   3966 O  O   . GLY C 1 141 ? 20.875  42.788  24.742  1.00 26.07 ? 129 GLY C O   1 
ATOM   3967 N  N   . THR C 1 142 ? 20.802  43.774  22.695  1.00 28.01 ? 130 THR C N   1 
ATOM   3968 C  CA  . THR C 1 142 ? 20.660  42.506  21.936  1.00 30.37 ? 130 THR C CA  1 
ATOM   3969 C  C   . THR C 1 142 ? 21.798  41.581  22.349  1.00 31.48 ? 130 THR C C   1 
ATOM   3970 O  O   . THR C 1 142 ? 22.969  42.016  22.250  1.00 30.73 ? 130 THR C O   1 
ATOM   3971 C  CB  . THR C 1 142 ? 20.618  42.754  20.426  1.00 31.92 ? 130 THR C CB  1 
ATOM   3972 O  OG1 . THR C 1 142 ? 19.711  43.850  20.271  1.00 34.59 ? 130 THR C OG1 1 
ATOM   3973 C  CG2 . THR C 1 142 ? 20.175  41.533  19.649  1.00 33.75 ? 130 THR C CG2 1 
ATOM   3974 N  N   . ALA C 1 143 ? 21.480  40.366  22.812  1.00 28.64 ? 131 ALA C N   1 
ATOM   3975 C  CA  . ALA C 1 143 ? 22.449  39.508  23.518  1.00 28.57 ? 131 ALA C CA  1 
ATOM   3976 C  C   . ALA C 1 143 ? 22.050  38.039  23.415  1.00 25.91 ? 131 ALA C C   1 
ATOM   3977 O  O   . ALA C 1 143 ? 20.887  37.750  23.131  1.00 27.72 ? 131 ALA C O   1 
ATOM   3978 C  CB  . ALA C 1 143 ? 22.563  39.925  24.964  1.00 31.32 ? 131 ALA C CB  1 
ATOM   3979 N  N   . THR C 1 144 ? 23.008  37.167  23.682  1.00 29.46 ? 132 THR C N   1 
ATOM   3980 C  CA  . THR C 1 144 ? 22.807  35.704  23.817  1.00 28.88 ? 132 THR C CA  1 
ATOM   3981 C  C   . THR C 1 144 ? 23.104  35.339  25.273  1.00 30.13 ? 132 THR C C   1 
ATOM   3982 O  O   . THR C 1 144 ? 24.167  35.727  25.776  1.00 32.37 ? 132 THR C O   1 
ATOM   3983 C  CB  . THR C 1 144 ? 23.627  34.969  22.752  1.00 32.53 ? 132 THR C CB  1 
ATOM   3984 O  OG1 . THR C 1 144 ? 23.049  35.379  21.510  1.00 31.78 ? 132 THR C OG1 1 
ATOM   3985 C  CG2 . THR C 1 144 ? 23.590  33.462  22.891  1.00 35.07 ? 132 THR C CG2 1 
ATOM   3986 N  N   . PHE C 1 145 ? 22.171  34.656  25.944  1.00 29.57 ? 133 PHE C N   1 
ATOM   3987 C  CA  . PHE C 1 145 ? 22.272  34.409  27.404  1.00 26.84 ? 133 PHE C CA  1 
ATOM   3988 C  C   . PHE C 1 145 ? 21.440  33.185  27.787  1.00 26.55 ? 133 PHE C C   1 
ATOM   3989 O  O   . PHE C 1 145 ? 20.562  32.755  27.014  1.00 29.27 ? 133 PHE C O   1 
ATOM   3990 C  CB  . PHE C 1 145 ? 21.860  35.653  28.190  1.00 26.12 ? 133 PHE C CB  1 
ATOM   3991 C  CG  . PHE C 1 145 ? 20.490  36.174  27.847  1.00 24.56 ? 133 PHE C CG  1 
ATOM   3992 C  CD1 . PHE C 1 145 ? 19.358  35.698  28.500  1.00 24.67 ? 133 PHE C CD1 1 
ATOM   3993 C  CD2 . PHE C 1 145 ? 20.327  37.139  26.872  1.00 22.85 ? 133 PHE C CD2 1 
ATOM   3994 C  CE1 . PHE C 1 145 ? 18.100  36.159  28.155  1.00 23.85 ? 133 PHE C CE1 1 
ATOM   3995 C  CE2 . PHE C 1 145 ? 19.063  37.575  26.515  1.00 23.51 ? 133 PHE C CE2 1 
ATOM   3996 C  CZ  . PHE C 1 145 ? 17.952  37.115  27.185  1.00 23.95 ? 133 PHE C CZ  1 
ATOM   3997 N  N   . ASN C 1 146 ? 21.771  32.631  28.942  1.00 25.51 ? 134 ASN C N   1 
ATOM   3998 C  CA  . ASN C 1 146 ? 21.054  31.466  29.509  1.00 25.21 ? 134 ASN C CA  1 
ATOM   3999 C  C   . ASN C 1 146 ? 19.910  32.015  30.351  1.00 23.78 ? 134 ASN C C   1 
ATOM   4000 O  O   . ASN C 1 146 ? 20.002  33.158  30.849  1.00 21.26 ? 134 ASN C O   1 
ATOM   4001 C  CB  . ASN C 1 146 ? 22.006  30.522  30.234  1.00 28.87 ? 134 ASN C CB  1 
ATOM   4002 C  CG  . ASN C 1 146 ? 22.891  29.813  29.228  1.00 29.18 ? 134 ASN C CG  1 
ATOM   4003 O  OD1 . ASN C 1 146 ? 22.490  29.632  28.083  1.00 31.23 ? 134 ASN C OD1 1 
ATOM   4004 N  ND2 . ASN C 1 146 ? 24.104  29.498  29.619  1.00 29.18 ? 134 ASN C ND2 1 
ATOM   4005 N  N   . GLN C 1 147 ? 18.856  31.224  30.416  1.00 22.54 ? 135 GLN C N   1 
ATOM   4006 C  CA  . GLN C 1 147 ? 17.644  31.519  31.196  1.00 23.14 ? 135 GLN C CA  1 
ATOM   4007 C  C   . GLN C 1 147 ? 17.539  30.422  32.226  1.00 22.17 ? 135 GLN C C   1 
ATOM   4008 O  O   . GLN C 1 147 ? 17.632  29.214  31.832  1.00 23.58 ? 135 GLN C O   1 
ATOM   4009 C  CB  . GLN C 1 147 ? 16.388  31.484  30.336  1.00 25.95 ? 135 GLN C CB  1 
ATOM   4010 C  CG  . GLN C 1 147 ? 16.207  32.649  29.381  1.00 28.66 ? 135 GLN C CG  1 
ATOM   4011 C  CD  . GLN C 1 147 ? 14.871  32.494  28.677  1.00 28.04 ? 135 GLN C CD  1 
ATOM   4012 O  OE1 . GLN C 1 147 ? 14.562  31.431  28.135  1.00 24.68 ? 135 GLN C OE1 1 
ATOM   4013 N  NE2 . GLN C 1 147 ? 14.054  33.536  28.684  1.00 23.13 ? 135 GLN C NE2 1 
ATOM   4014 N  N   . TYR C 1 148 ? 17.417  30.776  33.505  1.00 20.65 ? 136 TYR C N   1 
ATOM   4015 C  CA  . TYR C 1 148 ? 17.236  29.744  34.552  1.00 21.54 ? 136 TYR C CA  1 
ATOM   4016 C  C   . TYR C 1 148 ? 15.805  29.824  35.055  1.00 21.37 ? 136 TYR C C   1 
ATOM   4017 O  O   . TYR C 1 148 ? 15.289  30.936  35.219  1.00 21.59 ? 136 TYR C O   1 
ATOM   4018 C  CB  . TYR C 1 148 ? 18.201  29.862  35.736  1.00 21.58 ? 136 TYR C CB  1 
ATOM   4019 C  CG  . TYR C 1 148 ? 19.659  29.949  35.392  1.00 21.89 ? 136 TYR C CG  1 
ATOM   4020 C  CD1 . TYR C 1 148 ? 20.152  29.500  34.176  1.00 24.25 ? 136 TYR C CD1 1 
ATOM   4021 C  CD2 . TYR C 1 148 ? 20.570  30.413  36.325  1.00 23.56 ? 136 TYR C CD2 1 
ATOM   4022 C  CE1 . TYR C 1 148 ? 21.499  29.572  33.880  1.00 23.86 ? 136 TYR C CE1 1 
ATOM   4023 C  CE2 . TYR C 1 148 ? 21.923  30.491  36.040  1.00 24.20 ? 136 TYR C CE2 1 
ATOM   4024 C  CZ  . TYR C 1 148 ? 22.387  30.085  34.804  1.00 24.63 ? 136 TYR C CZ  1 
ATOM   4025 O  OH  . TYR C 1 148 ? 23.711  30.161  34.474  1.00 27.97 ? 136 TYR C OH  1 
ATOM   4026 N  N   . TRP C 1 149 ? 15.198  28.665  35.297  1.00 20.18 ? 137 TRP C N   1 
ATOM   4027 C  CA  . TRP C 1 149 ? 13.775  28.579  35.697  1.00 20.61 ? 137 TRP C CA  1 
ATOM   4028 C  C   . TRP C 1 149 ? 13.633  27.705  36.938  1.00 21.36 ? 137 TRP C C   1 
ATOM   4029 O  O   . TRP C 1 149 ? 14.222  26.572  36.973  1.00 21.61 ? 137 TRP C O   1 
ATOM   4030 C  CB  . TRP C 1 149 ? 12.907  28.011  34.563  1.00 21.49 ? 137 TRP C CB  1 
ATOM   4031 C  CG  . TRP C 1 149 ? 13.015  28.679  33.231  1.00 23.12 ? 137 TRP C CG  1 
ATOM   4032 C  CD1 . TRP C 1 149 ? 13.938  28.494  32.238  1.00 22.74 ? 137 TRP C CD1 1 
ATOM   4033 C  CD2 . TRP C 1 149 ? 12.081  29.638  32.730  1.00 21.16 ? 137 TRP C CD2 1 
ATOM   4034 N  NE1 . TRP C 1 149 ? 13.641  29.308  31.168  1.00 21.81 ? 137 TRP C NE1 1 
ATOM   4035 C  CE2 . TRP C 1 149 ? 12.518  30.026  31.442  1.00 21.35 ? 137 TRP C CE2 1 
ATOM   4036 C  CE3 . TRP C 1 149 ? 10.941  30.237  33.266  1.00 20.72 ? 137 TRP C CE3 1 
ATOM   4037 C  CZ2 . TRP C 1 149 ? 11.839  30.984  30.690  1.00 20.79 ? 137 TRP C CZ2 1 
ATOM   4038 C  CZ3 . TRP C 1 149 ? 10.277  31.187  32.519  1.00 19.92 ? 137 TRP C CZ3 1 
ATOM   4039 C  CH2 . TRP C 1 149 ? 10.710  31.533  31.242  1.00 21.48 ? 137 TRP C CH2 1 
ATOM   4040 N  N   . SER C 1 150 ? 12.825  28.178  37.879  1.00 19.87 ? 138 SER C N   1 
ATOM   4041 C  CA  . SER C 1 150 ? 12.177  27.394  38.950  1.00 20.86 ? 138 SER C CA  1 
ATOM   4042 C  C   . SER C 1 150 ? 10.693  27.508  38.715  1.00 21.50 ? 138 SER C C   1 
ATOM   4043 O  O   . SER C 1 150 ? 10.188  28.620  38.797  1.00 21.51 ? 138 SER C O   1 
ATOM   4044 C  CB  . SER C 1 150 ? 12.467  27.894  40.313  1.00 22.21 ? 138 SER C CB  1 
ATOM   4045 O  OG  . SER C 1 150 ? 13.669  27.409  40.773  1.00 24.78 ? 138 SER C OG  1 
ATOM   4046 N  N   . VAL C 1 151 ? 10.014  26.407  38.408  1.00 20.59 ? 139 VAL C N   1 
ATOM   4047 C  CA  . VAL C 1 151 ? 8.567   26.470  38.080  1.00 20.54 ? 139 VAL C CA  1 
ATOM   4048 C  C   . VAL C 1 151 ? 7.747   25.740  39.156  1.00 19.36 ? 139 VAL C C   1 
ATOM   4049 O  O   . VAL C 1 151 ? 7.919   24.518  39.314  1.00 21.60 ? 139 VAL C O   1 
ATOM   4050 C  CB  . VAL C 1 151 ? 8.318   25.938  36.657  1.00 21.72 ? 139 VAL C CB  1 
ATOM   4051 C  CG1 . VAL C 1 151 ? 6.837   26.045  36.312  1.00 21.75 ? 139 VAL C CG1 1 
ATOM   4052 C  CG2 . VAL C 1 151 ? 9.180   26.648  35.614  1.00 24.30 ? 139 VAL C CG2 1 
ATOM   4053 N  N   . ARG C 1 152 ? 6.953   26.482  39.916  1.00 19.00 ? 140 ARG C N   1 
ATOM   4054 C  CA  . ARG C 1 152 ? 6.100   25.944  41.013  1.00 18.92 ? 140 ARG C CA  1 
ATOM   4055 C  C   . ARG C 1 152 ? 5.148   24.885  40.433  1.00 20.06 ? 140 ARG C C   1 
ATOM   4056 O  O   . ARG C 1 152 ? 4.559   25.124  39.345  1.00 21.14 ? 140 ARG C O   1 
ATOM   4057 C  CB  . ARG C 1 152 ? 5.334   27.043  41.728  1.00 20.05 ? 140 ARG C CB  1 
ATOM   4058 C  CG  . ARG C 1 152 ? 4.910   26.633  43.133  1.00 20.36 ? 140 ARG C CG  1 
ATOM   4059 C  CD  . ARG C 1 152 ? 4.272   27.712  43.961  1.00 21.36 ? 140 ARG C CD  1 
ATOM   4060 N  NE  . ARG C 1 152 ? 3.656   27.292  45.217  1.00 22.85 ? 140 ARG C NE  1 
ATOM   4061 C  CZ  . ARG C 1 152 ? 4.199   27.408  46.424  1.00 25.20 ? 140 ARG C CZ  1 
ATOM   4062 N  NH1 . ARG C 1 152 ? 5.420   27.896  46.572  1.00 25.73 ? 140 ARG C NH1 1 
ATOM   4063 N  NH2 . ARG C 1 152 ? 3.538   27.000  47.496  1.00 25.56 ? 140 ARG C NH2 1 
ATOM   4064 N  N   . THR C 1 153 ? 5.047   23.716  41.068  1.00 22.90 ? 141 THR C N   1 
ATOM   4065 C  CA  . THR C 1 153 ? 4.156   22.633  40.563  1.00 23.78 ? 141 THR C CA  1 
ATOM   4066 C  C   . THR C 1 153 ? 2.696   22.985  40.904  1.00 25.02 ? 141 THR C C   1 
ATOM   4067 O  O   . THR C 1 153 ? 1.824   22.611  40.093  1.00 29.96 ? 141 THR C O   1 
ATOM   4068 C  CB  . THR C 1 153 ? 4.622   21.252  41.051  1.00 25.32 ? 141 THR C CB  1 
ATOM   4069 O  OG1 . THR C 1 153 ? 4.399   21.200  42.452  1.00 28.38 ? 141 THR C OG1 1 
ATOM   4070 C  CG2 . THR C 1 153 ? 6.057   20.929  40.696  1.00 26.34 ? 141 THR C CG2 1 
ATOM   4071 N  N   . ASP C 1 154 ? 2.418   23.684  42.021  1.00 26.37 ? 142 ASP C N   1 
ATOM   4072 C  CA  . ASP C 1 154 ? 1.058   24.128  42.466  1.00 26.44 ? 142 ASP C CA  1 
ATOM   4073 C  C   . ASP C 1 154 ? 0.969   25.652  42.314  1.00 24.94 ? 142 ASP C C   1 
ATOM   4074 O  O   . ASP C 1 154 ? 1.474   26.388  43.198  1.00 23.92 ? 142 ASP C O   1 
ATOM   4075 C  CB  . ASP C 1 154 ? 0.739   23.766  43.930  1.00 30.28 ? 142 ASP C CB  1 
ATOM   4076 C  CG  . ASP C 1 154 ? -0.559  24.349  44.514  1.00 28.72 ? 142 ASP C CG  1 
ATOM   4077 O  OD1 . ASP C 1 154 ? -1.533  24.520  43.769  1.00 29.40 ? 142 ASP C OD1 1 
ATOM   4078 O  OD2 . ASP C 1 154 ? -0.622  24.581  45.766  1.00 35.12 ? 142 ASP C OD2 1 
ATOM   4079 N  N   . HIS C 1 155 ? 0.362   26.123  41.229  1.00 20.32 ? 143 HIS C N   1 
ATOM   4080 C  CA  . HIS C 1 155 ? 0.370   27.584  40.907  1.00 19.98 ? 143 HIS C CA  1 
ATOM   4081 C  C   . HIS C 1 155 ? -0.291  28.333  42.055  1.00 19.01 ? 143 HIS C C   1 
ATOM   4082 O  O   . HIS C 1 155 ? -1.317  27.816  42.605  1.00 22.42 ? 143 HIS C O   1 
ATOM   4083 C  CB  . HIS C 1 155 ? -0.288  27.792  39.541  1.00 19.96 ? 143 HIS C CB  1 
ATOM   4084 C  CG  . HIS C 1 155 ? 0.501   27.199  38.414  1.00 21.15 ? 143 HIS C CG  1 
ATOM   4085 N  ND1 . HIS C 1 155 ? 0.087   27.242  37.099  1.00 21.68 ? 143 HIS C ND1 1 
ATOM   4086 C  CD2 . HIS C 1 155 ? 1.692   26.568  38.398  1.00 23.74 ? 143 HIS C CD2 1 
ATOM   4087 C  CE1 . HIS C 1 155 ? 0.991   26.651  36.332  1.00 22.51 ? 143 HIS C CE1 1 
ATOM   4088 N  NE2 . HIS C 1 155 ? 1.995   26.233  37.105  1.00 23.29 ? 143 HIS C NE2 1 
ATOM   4089 N  N   . ARG C 1 156 ? 0.149   29.564  42.356  1.00 18.93 ? 144 ARG C N   1 
ATOM   4090 C  CA  . ARG C 1 156 ? -0.485  30.415  43.387  1.00 17.33 ? 144 ARG C CA  1 
ATOM   4091 C  C   . ARG C 1 156 ? -0.197  31.877  43.065  1.00 17.66 ? 144 ARG C C   1 
ATOM   4092 O  O   . ARG C 1 156 ? 0.715   32.164  42.265  1.00 18.53 ? 144 ARG C O   1 
ATOM   4093 C  CB  . ARG C 1 156 ? 0.041   30.140  44.795  1.00 18.18 ? 144 ARG C CB  1 
ATOM   4094 C  CG  . ARG C 1 156 ? 1.499   30.516  44.998  1.00 17.50 ? 144 ARG C CG  1 
ATOM   4095 C  CD  . ARG C 1 156 ? 1.988   30.337  46.424  1.00 17.99 ? 144 ARG C CD  1 
ATOM   4096 N  NE  . ARG C 1 156 ? 3.396   30.702  46.457  1.00 18.40 ? 144 ARG C NE  1 
ATOM   4097 C  CZ  . ARG C 1 156 ? 4.150   30.758  47.543  1.00 19.87 ? 144 ARG C CZ  1 
ATOM   4098 N  NH1 . ARG C 1 156 ? 3.671   30.400  48.729  1.00 21.19 ? 144 ARG C NH1 1 
ATOM   4099 N  NH2 . ARG C 1 156 ? 5.413   31.131  47.419  1.00 23.69 ? 144 ARG C NH2 1 
ATOM   4100 N  N   . VAL C 1 157 ? -0.938  32.715  43.741  1.00 16.40 ? 145 VAL C N   1 
ATOM   4101 C  CA  . VAL C 1 157 ? -0.864  34.201  43.692  1.00 15.95 ? 145 VAL C CA  1 
ATOM   4102 C  C   . VAL C 1 157 ? -0.775  34.676  45.123  1.00 19.14 ? 145 VAL C C   1 
ATOM   4103 O  O   . VAL C 1 157 ? -1.799  34.794  45.775  1.00 21.69 ? 145 VAL C O   1 
ATOM   4104 C  CB  . VAL C 1 157 ? -2.061  34.805  42.962  1.00 17.83 ? 145 VAL C CB  1 
ATOM   4105 C  CG1 . VAL C 1 157 ? -1.936  36.318  42.898  1.00 18.33 ? 145 VAL C CG1 1 
ATOM   4106 C  CG2 . VAL C 1 157 ? -2.258  34.182  41.583  1.00 20.83 ? 145 VAL C CG2 1 
ATOM   4107 N  N   . GLY C 1 158 ? 0.449   34.895  45.568  1.00 22.14 ? 146 GLY C N   1 
ATOM   4108 C  CA  . GLY C 1 158 ? 0.723   35.417  46.903  1.00 22.58 ? 146 GLY C CA  1 
ATOM   4109 C  C   . GLY C 1 158 ? 1.598   34.463  47.648  1.00 23.31 ? 146 GLY C C   1 
ATOM   4110 O  O   . GLY C 1 158 ? 1.616   33.267  47.327  1.00 26.52 ? 146 GLY C O   1 
ATOM   4111 N  N   . GLY C 1 159 ? 2.302   34.990  48.620  1.00 23.92 ? 147 GLY C N   1 
ATOM   4112 C  CA  . GLY C 1 159 ? 3.029   34.155  49.569  1.00 23.57 ? 147 GLY C CA  1 
ATOM   4113 C  C   . GLY C 1 159 ? 4.427   34.687  49.715  1.00 22.01 ? 147 GLY C C   1 
ATOM   4114 O  O   . GLY C 1 159 ? 4.631   35.910  49.546  1.00 24.14 ? 147 GLY C O   1 
ATOM   4115 N  N   . THR C 1 160 ? 5.315   33.799  50.118  1.00 19.53 ? 148 THR C N   1 
ATOM   4116 C  CA  . THR C 1 160 ? 6.735   34.064  50.426  1.00 19.07 ? 148 THR C CA  1 
ATOM   4117 C  C   . THR C 1 160 ? 7.573   33.328  49.397  1.00 18.63 ? 148 THR C C   1 
ATOM   4118 O  O   . THR C 1 160 ? 7.376   32.114  49.234  1.00 19.73 ? 148 THR C O   1 
ATOM   4119 C  CB  . THR C 1 160 ? 7.067   33.576  51.834  1.00 19.97 ? 148 THR C CB  1 
ATOM   4120 O  OG1 . THR C 1 160 ? 6.175   34.181  52.771  1.00 25.43 ? 148 THR C OG1 1 
ATOM   4121 C  CG2 . THR C 1 160 ? 8.518   33.766  52.208  1.00 22.63 ? 148 THR C CG2 1 
ATOM   4122 N  N   . VAL C 1 161 ? 8.595   33.991  48.875  1.00 17.27 ? 149 VAL C N   1 
ATOM   4123 C  CA  . VAL C 1 161 ? 9.646   33.382  48.027  1.00 16.69 ? 149 VAL C CA  1 
ATOM   4124 C  C   . VAL C 1 161 ? 11.005  33.643  48.705  1.00 17.20 ? 149 VAL C C   1 
ATOM   4125 O  O   . VAL C 1 161 ? 11.452  34.846  48.777  1.00 19.73 ? 149 VAL C O   1 
ATOM   4126 C  CB  . VAL C 1 161 ? 9.605   33.900  46.589  1.00 17.02 ? 149 VAL C CB  1 
ATOM   4127 C  CG1 . VAL C 1 161 ? 10.757  33.406  45.771  1.00 17.94 ? 149 VAL C CG1 1 
ATOM   4128 C  CG2 . VAL C 1 161 ? 8.266   33.605  45.946  1.00 17.71 ? 149 VAL C CG2 1 
ATOM   4129 N  N   . THR C 1 162 ? 11.592  32.566  49.200  1.00 18.20 ? 150 THR C N   1 
ATOM   4130 C  CA  . THR C 1 162 ? 12.955  32.495  49.794  1.00 19.48 ? 150 THR C CA  1 
ATOM   4131 C  C   . THR C 1 162 ? 13.930  32.297  48.629  1.00 19.01 ? 150 THR C C   1 
ATOM   4132 O  O   . THR C 1 162 ? 14.220  31.159  48.257  1.00 22.68 ? 150 THR C O   1 
ATOM   4133 C  CB  . THR C 1 162 ? 13.082  31.427  50.880  1.00 21.38 ? 150 THR C CB  1 
ATOM   4134 O  OG1 . THR C 1 162 ? 12.025  31.551  51.837  1.00 20.67 ? 150 THR C OG1 1 
ATOM   4135 C  CG2 . THR C 1 162 ? 14.403  31.560  51.601  1.00 21.01 ? 150 THR C CG2 1 
ATOM   4136 N  N   . THR C 1 163 ? 14.323  33.384  47.996  1.00 20.40 ? 151 THR C N   1 
ATOM   4137 C  CA  . THR C 1 163 ? 15.079  33.369  46.718  1.00 20.49 ? 151 THR C CA  1 
ATOM   4138 C  C   . THR C 1 163 ? 16.405  32.631  46.906  1.00 22.07 ? 151 THR C C   1 
ATOM   4139 O  O   . THR C 1 163 ? 16.801  31.910  45.988  1.00 23.68 ? 151 THR C O   1 
ATOM   4140 C  CB  . THR C 1 163 ? 15.324  34.786  46.154  1.00 24.94 ? 151 THR C CB  1 
ATOM   4141 O  OG1 . THR C 1 163 ? 16.037  35.533  47.133  1.00 23.47 ? 151 THR C OG1 1 
ATOM   4142 C  CG2 . THR C 1 163 ? 14.053  35.503  45.779  1.00 24.72 ? 151 THR C CG2 1 
ATOM   4143 N  N   . GLN C 1 164 ? 17.045  32.717  48.074  1.00 23.09 ? 152 GLN C N   1 
ATOM   4144 C  CA  . GLN C 1 164 ? 18.314  31.981  48.313  1.00 23.10 ? 152 GLN C CA  1 
ATOM   4145 C  C   . GLN C 1 164 ? 18.132  30.477  48.092  1.00 24.28 ? 152 GLN C C   1 
ATOM   4146 O  O   . GLN C 1 164 ? 19.099  29.844  47.616  1.00 25.54 ? 152 GLN C O   1 
ATOM   4147 C  CB  . GLN C 1 164 ? 18.867  32.185  49.726  1.00 23.31 ? 152 GLN C CB  1 
ATOM   4148 C  CG  . GLN C 1 164 ? 20.301  31.689  49.853  1.00 25.47 ? 152 GLN C CG  1 
ATOM   4149 C  CD  . GLN C 1 164 ? 21.255  32.487  49.000  1.00 25.48 ? 152 GLN C CD  1 
ATOM   4150 O  OE1 . GLN C 1 164 ? 21.392  33.691  49.163  1.00 31.41 ? 152 GLN C OE1 1 
ATOM   4151 N  NE2 . GLN C 1 164 ? 21.926  31.836  48.063  1.00 31.86 ? 152 GLN C NE2 1 
ATOM   4152 N  N   . ASN C 1 165 ? 16.972  29.894  48.435  1.00 22.29 ? 153 ASN C N   1 
ATOM   4153 C  CA  . ASN C 1 165 ? 16.785  28.425  48.249  1.00 20.76 ? 153 ASN C CA  1 
ATOM   4154 C  C   . ASN C 1 165 ? 16.828  28.101  46.756  1.00 22.17 ? 153 ASN C C   1 
ATOM   4155 O  O   . ASN C 1 165 ? 17.332  27.001  46.402  1.00 23.62 ? 153 ASN C O   1 
ATOM   4156 C  CB  . ASN C 1 165 ? 15.520  27.917  48.936  1.00 22.59 ? 153 ASN C CB  1 
ATOM   4157 C  CG  . ASN C 1 165 ? 15.606  27.983  50.437  1.00 25.66 ? 153 ASN C CG  1 
ATOM   4158 O  OD1 . ASN C 1 165 ? 16.695  27.952  51.022  1.00 30.79 ? 153 ASN C OD1 1 
ATOM   4159 N  ND2 . ASN C 1 165 ? 14.447  27.995  51.068  1.00 25.51 ? 153 ASN C ND2 1 
ATOM   4160 N  N   . HIS C 1 166 ? 16.287  28.981  45.909  1.00 20.60 ? 154 HIS C N   1 
ATOM   4161 C  CA  . HIS C 1 166 ? 16.301  28.813  44.443  1.00 21.31 ? 154 HIS C CA  1 
ATOM   4162 C  C   . HIS C 1 166 ? 17.742  28.976  43.947  1.00 21.92 ? 154 HIS C C   1 
ATOM   4163 O  O   . HIS C 1 166 ? 18.184  28.179  43.136  1.00 22.45 ? 154 HIS C O   1 
ATOM   4164 C  CB  . HIS C 1 166 ? 15.327  29.798  43.783  1.00 19.81 ? 154 HIS C CB  1 
ATOM   4165 C  CG  . HIS C 1 166 ? 13.907  29.534  44.146  1.00 19.20 ? 154 HIS C CG  1 
ATOM   4166 N  ND1 . HIS C 1 166 ? 13.158  28.525  43.544  1.00 19.48 ? 154 HIS C ND1 1 
ATOM   4167 C  CD2 . HIS C 1 166 ? 13.121  30.080  45.094  1.00 20.34 ? 154 HIS C CD2 1 
ATOM   4168 C  CE1 . HIS C 1 166 ? 11.967  28.489  44.099  1.00 18.40 ? 154 HIS C CE1 1 
ATOM   4169 N  NE2 . HIS C 1 166 ? 11.898  29.445  45.038  1.00 19.79 ? 154 HIS C NE2 1 
ATOM   4170 N  N   . PHE C 1 167 ? 18.420  30.040  44.359  1.00 23.69 ? 155 PHE C N   1 
ATOM   4171 C  CA  . PHE C 1 167 ? 19.787  30.329  43.864  1.00 25.00 ? 155 PHE C CA  1 
ATOM   4172 C  C   . PHE C 1 167 ? 20.694  29.137  44.210  1.00 23.45 ? 155 PHE C C   1 
ATOM   4173 O  O   . PHE C 1 167 ? 21.514  28.757  43.358  1.00 22.16 ? 155 PHE C O   1 
ATOM   4174 C  CB  . PHE C 1 167 ? 20.329  31.642  44.430  1.00 24.77 ? 155 PHE C CB  1 
ATOM   4175 C  CG  . PHE C 1 167 ? 19.547  32.873  44.069  1.00 23.80 ? 155 PHE C CG  1 
ATOM   4176 C  CD1 . PHE C 1 167 ? 18.652  32.888  43.003  1.00 23.21 ? 155 PHE C CD1 1 
ATOM   4177 C  CD2 . PHE C 1 167 ? 19.729  34.033  44.802  1.00 27.94 ? 155 PHE C CD2 1 
ATOM   4178 C  CE1 . PHE C 1 167 ? 17.953  34.035  42.682  1.00 27.75 ? 155 PHE C CE1 1 
ATOM   4179 C  CE2 . PHE C 1 167 ? 19.003  35.172  44.498  1.00 30.43 ? 155 PHE C CE2 1 
ATOM   4180 C  CZ  . PHE C 1 167 ? 18.131  35.179  43.428  1.00 28.03 ? 155 PHE C CZ  1 
ATOM   4181 N  N   . ASP C 1 168 ? 20.552  28.606  45.418  1.00 24.51 ? 156 ASP C N   1 
ATOM   4182 C  CA  . ASP C 1 168 ? 21.336  27.453  45.946  1.00 26.97 ? 156 ASP C CA  1 
ATOM   4183 C  C   . ASP C 1 168 ? 21.020  26.199  45.113  1.00 29.40 ? 156 ASP C C   1 
ATOM   4184 O  O   . ASP C 1 168 ? 21.961  25.508  44.676  1.00 27.66 ? 156 ASP C O   1 
ATOM   4185 C  CB  . ASP C 1 168 ? 21.086  27.284  47.448  1.00 28.83 ? 156 ASP C CB  1 
ATOM   4186 C  CG  . ASP C 1 168 ? 21.721  28.366  48.325  1.00 32.02 ? 156 ASP C CG  1 
ATOM   4187 O  OD1 . ASP C 1 168 ? 22.676  29.029  47.868  1.00 38.67 ? 156 ASP C OD1 1 
ATOM   4188 O  OD2 . ASP C 1 168 ? 21.261  28.536  49.469  1.00 37.01 ? 156 ASP C OD2 1 
ATOM   4189 N  N   . ALA C 1 169 ? 19.743  25.928  44.833  1.00 28.37 ? 157 ALA C N   1 
ATOM   4190 C  CA  . ALA C 1 169 ? 19.307  24.797  43.991  1.00 27.01 ? 157 ALA C CA  1 
ATOM   4191 C  C   . ALA C 1 169 ? 19.878  24.949  42.576  1.00 25.19 ? 157 ALA C C   1 
ATOM   4192 O  O   . ALA C 1 169 ? 20.317  23.966  42.030  1.00 26.92 ? 157 ALA C O   1 
ATOM   4193 C  CB  . ALA C 1 169 ? 17.803  24.719  43.965  1.00 27.95 ? 157 ALA C CB  1 
ATOM   4194 N  N   . TRP C 1 170 ? 19.883  26.151  42.000  1.00 22.13 ? 158 TRP C N   1 
ATOM   4195 C  CA  . TRP C 1 170 ? 20.436  26.352  40.639  1.00 22.76 ? 158 TRP C CA  1 
ATOM   4196 C  C   . TRP C 1 170 ? 21.941  26.087  40.701  1.00 23.57 ? 158 TRP C C   1 
ATOM   4197 O  O   . TRP C 1 170 ? 22.455  25.465  39.761  1.00 23.97 ? 158 TRP C O   1 
ATOM   4198 C  CB  . TRP C 1 170 ? 20.161  27.743  40.088  1.00 24.37 ? 158 TRP C CB  1 
ATOM   4199 C  CG  . TRP C 1 170 ? 18.701  28.009  39.910  1.00 22.85 ? 158 TRP C CG  1 
ATOM   4200 C  CD1 . TRP C 1 170 ? 17.708  27.080  39.862  1.00 23.82 ? 158 TRP C CD1 1 
ATOM   4201 C  CD2 . TRP C 1 170 ? 18.064  29.300  39.806  1.00 20.32 ? 158 TRP C CD2 1 
ATOM   4202 N  NE1 . TRP C 1 170 ? 16.491  27.689  39.708  1.00 23.89 ? 158 TRP C NE1 1 
ATOM   4203 C  CE2 . TRP C 1 170 ? 16.685  29.052  39.666  1.00 20.24 ? 158 TRP C CE2 1 
ATOM   4204 C  CE3 . TRP C 1 170 ? 18.502  30.633  39.820  1.00 22.62 ? 158 TRP C CE3 1 
ATOM   4205 C  CZ2 . TRP C 1 170 ? 15.752  30.072  39.530  1.00 21.69 ? 158 TRP C CZ2 1 
ATOM   4206 C  CZ3 . TRP C 1 170 ? 17.574  31.638  39.720  1.00 19.13 ? 158 TRP C CZ3 1 
ATOM   4207 C  CH2 . TRP C 1 170 ? 16.217  31.367  39.533  1.00 19.32 ? 158 TRP C CH2 1 
ATOM   4208 N  N   . LYS C 1 171 ? 22.606  26.578  41.752  1.00 26.02 ? 159 LYS C N   1 
ATOM   4209 C  CA  . LYS C 1 171 ? 24.072  26.373  41.885  1.00 26.22 ? 159 LYS C CA  1 
ATOM   4210 C  C   . LYS C 1 171 ? 24.334  24.866  41.881  1.00 28.78 ? 159 LYS C C   1 
ATOM   4211 O  O   . LYS C 1 171 ? 25.222  24.428  41.135  1.00 27.15 ? 159 LYS C O   1 
ATOM   4212 C  CB  . LYS C 1 171 ? 24.639  26.994  43.158  1.00 29.38 ? 159 LYS C CB  1 
ATOM   4213 C  CG  . LYS C 1 171 ? 26.150  26.803  43.316  1.00 33.68 ? 159 LYS C CG  1 
ATOM   4214 C  CD  . LYS C 1 171 ? 26.878  28.060  43.716  1.00 39.11 ? 159 LYS C CD  1 
ATOM   4215 C  CE  . LYS C 1 171 ? 26.459  28.544  45.084  1.00 42.02 ? 159 LYS C CE  1 
ATOM   4216 N  NZ  . LYS C 1 171 ? 27.556  29.281  45.750  1.00 42.83 ? 159 LYS C NZ  1 
ATOM   4217 N  N   . ASN C 1 172 ? 23.590  24.118  42.692  1.00 30.81 ? 160 ASN C N   1 
ATOM   4218 C  CA  . ASN C 1 172 ? 23.776  22.643  42.861  1.00 32.95 ? 160 ASN C CA  1 
ATOM   4219 C  C   . ASN C 1 172 ? 23.449  21.893  41.563  1.00 33.90 ? 160 ASN C C   1 
ATOM   4220 O  O   . ASN C 1 172 ? 24.007  20.763  41.362  1.00 31.67 ? 160 ASN C O   1 
ATOM   4221 C  CB  . ASN C 1 172 ? 22.962  22.116  44.041  1.00 38.45 ? 160 ASN C CB  1 
ATOM   4222 C  CG  . ASN C 1 172 ? 23.360  22.793  45.333  1.00 43.34 ? 160 ASN C CG  1 
ATOM   4223 O  OD1 . ASN C 1 172 ? 24.429  23.400  45.410  1.00 47.85 ? 160 ASN C OD1 1 
ATOM   4224 N  ND2 . ASN C 1 172 ? 22.496  22.739  46.333  1.00 47.93 ? 160 ASN C ND2 1 
ATOM   4225 N  N   . ALA C 1 173 ? 22.614  22.460  40.685  1.00 29.91 ? 161 ALA C N   1 
ATOM   4226 C  CA  . ALA C 1 173 ? 22.309  21.896  39.346  1.00 33.10 ? 161 ALA C CA  1 
ATOM   4227 C  C   . ALA C 1 173 ? 23.357  22.306  38.301  1.00 33.57 ? 161 ALA C C   1 
ATOM   4228 O  O   . ALA C 1 173 ? 23.108  22.084  37.118  1.00 34.64 ? 161 ALA C O   1 
ATOM   4229 C  CB  . ALA C 1 173 ? 20.917  22.311  38.913  1.00 31.69 ? 161 ALA C CB  1 
ATOM   4230 N  N   . GLY C 1 174 ? 24.471  22.922  38.699  1.00 34.75 ? 162 GLY C N   1 
ATOM   4231 C  CA  . GLY C 1 174 ? 25.538  23.368  37.777  1.00 34.95 ? 162 GLY C CA  1 
ATOM   4232 C  C   . GLY C 1 174 ? 25.215  24.667  37.048  1.00 33.62 ? 162 GLY C C   1 
ATOM   4233 O  O   . GLY C 1 174 ? 25.855  24.929  36.017  1.00 35.24 ? 162 GLY C O   1 
ATOM   4234 N  N   . LEU C 1 175 ? 24.267  25.474  37.540  1.00 32.46 ? 163 LEU C N   1 
ATOM   4235 C  CA  . LEU C 1 175 ? 23.885  26.760  36.880  1.00 32.21 ? 163 LEU C CA  1 
ATOM   4236 C  C   . LEU C 1 175 ? 24.530  27.930  37.635  1.00 29.86 ? 163 LEU C C   1 
ATOM   4237 O  O   . LEU C 1 175 ? 24.053  28.262  38.733  1.00 28.91 ? 163 LEU C O   1 
ATOM   4238 C  CB  . LEU C 1 175 ? 22.357  26.894  36.847  1.00 31.15 ? 163 LEU C CB  1 
ATOM   4239 C  CG  . LEU C 1 175 ? 21.613  25.739  36.184  1.00 33.73 ? 163 LEU C CG  1 
ATOM   4240 C  CD1 . LEU C 1 175 ? 20.113  26.003  36.189  1.00 34.50 ? 163 LEU C CD1 1 
ATOM   4241 C  CD2 . LEU C 1 175 ? 22.123  25.509  34.765  1.00 32.05 ? 163 LEU C CD2 1 
ATOM   4242 N  N   . GLU C 1 176 ? 25.515  28.559  37.005  1.00 30.55 ? 164 GLU C N   1 
ATOM   4243 C  CA  . GLU C 1 176 ? 26.354  29.653  37.561  1.00 34.19 ? 164 GLU C CA  1 
ATOM   4244 C  C   . GLU C 1 176 ? 25.570  30.966  37.529  1.00 30.44 ? 164 GLU C C   1 
ATOM   4245 O  O   . GLU C 1 176 ? 25.022  31.295  36.463  1.00 28.44 ? 164 GLU C O   1 
ATOM   4246 C  CB  . GLU C 1 176 ? 27.634  29.800  36.734  1.00 38.71 ? 164 GLU C CB  1 
ATOM   4247 C  CG  . GLU C 1 176 ? 28.392  28.484  36.516  1.00 41.85 ? 164 GLU C CG  1 
ATOM   4248 C  CD  . GLU C 1 176 ? 29.246  28.460  35.254  1.00 47.22 ? 164 GLU C CD  1 
ATOM   4249 O  OE1 . GLU C 1 176 ? 30.482  28.340  35.379  1.00 53.84 ? 164 GLU C OE1 1 
ATOM   4250 O  OE2 . GLU C 1 176 ? 28.678  28.595  34.145  1.00 49.65 ? 164 GLU C OE2 1 
ATOM   4251 N  N   . MET C 1 177 ? 25.567  31.704  38.641  1.00 28.31 ? 165 MET C N   1 
ATOM   4252 C  CA  . MET C 1 177 ? 24.950  33.053  38.756  1.00 31.03 ? 165 MET C CA  1 
ATOM   4253 C  C   . MET C 1 177 ? 26.066  34.091  38.716  1.00 28.30 ? 165 MET C C   1 
ATOM   4254 O  O   . MET C 1 177 ? 27.111  33.837  39.314  1.00 27.66 ? 165 MET C O   1 
ATOM   4255 C  CB  . MET C 1 177 ? 24.185  33.195  40.074  1.00 34.69 ? 165 MET C CB  1 
ATOM   4256 C  CG  . MET C 1 177 ? 23.061  32.197  40.183  1.00 39.19 ? 165 MET C CG  1 
ATOM   4257 S  SD  . MET C 1 177 ? 21.713  32.673  39.106  1.00 44.26 ? 165 MET C SD  1 
ATOM   4258 C  CE  . MET C 1 177 ? 20.810  33.726  40.239  1.00 43.25 ? 165 MET C CE  1 
ATOM   4259 N  N   . GLY C 1 178 ? 25.837  35.236  38.085  1.00 27.54 ? 166 GLY C N   1 
ATOM   4260 C  CA  . GLY C 1 178 ? 26.820  36.334  38.111  1.00 27.33 ? 166 GLY C CA  1 
ATOM   4261 C  C   . GLY C 1 178 ? 26.508  37.364  39.173  1.00 27.01 ? 166 GLY C C   1 
ATOM   4262 O  O   . GLY C 1 178 ? 25.861  37.036  40.179  1.00 28.43 ? 166 GLY C O   1 
ATOM   4263 N  N   . THR C 1 179 ? 26.958  38.587  38.920  1.00 27.11 ? 167 THR C N   1 
ATOM   4264 C  CA  . THR C 1 179 ? 26.698  39.813  39.708  1.00 25.37 ? 167 THR C CA  1 
ATOM   4265 C  C   . THR C 1 179 ? 25.237  40.224  39.520  1.00 22.25 ? 167 THR C C   1 
ATOM   4266 O  O   . THR C 1 179 ? 24.824  40.370  38.373  1.00 21.98 ? 167 THR C O   1 
ATOM   4267 C  CB  . THR C 1 179 ? 27.654  40.920  39.249  1.00 28.15 ? 167 THR C CB  1 
ATOM   4268 O  OG1 . THR C 1 179 ? 28.982  40.442  39.504  1.00 28.51 ? 167 THR C OG1 1 
ATOM   4269 C  CG2 . THR C 1 179 ? 27.418  42.244  39.942  1.00 30.57 ? 167 THR C CG2 1 
ATOM   4270 N  N   . HIS C 1 180 ? 24.497  40.358  40.613  1.00 23.58 ? 168 HIS C N   1 
ATOM   4271 C  CA  . HIS C 1 180 ? 23.044  40.649  40.562  1.00 21.52 ? 168 HIS C CA  1 
ATOM   4272 C  C   . HIS C 1 180 ? 22.846  42.018  39.913  1.00 22.58 ? 168 HIS C C   1 
ATOM   4273 O  O   . HIS C 1 180 ? 23.520  42.998  40.327  1.00 23.65 ? 168 HIS C O   1 
ATOM   4274 C  CB  . HIS C 1 180 ? 22.431  40.518  41.961  1.00 23.37 ? 168 HIS C CB  1 
ATOM   4275 C  CG  . HIS C 1 180 ? 22.103  39.098  42.267  1.00 26.22 ? 168 HIS C CG  1 
ATOM   4276 N  ND1 . HIS C 1 180 ? 23.066  38.146  42.553  1.00 36.54 ? 168 HIS C ND1 1 
ATOM   4277 C  CD2 . HIS C 1 180 ? 20.943  38.432  42.190  1.00 28.30 ? 168 HIS C CD2 1 
ATOM   4278 C  CE1 . HIS C 1 180 ? 22.482  36.960  42.679  1.00 28.82 ? 168 HIS C CE1 1 
ATOM   4279 N  NE2 . HIS C 1 180 ? 21.195  37.105  42.446  1.00 30.61 ? 168 HIS C NE2 1 
ATOM   4280 N  N   . ASN C 1 181 ? 21.947  42.093  38.928  1.00 20.52 ? 169 ASN C N   1 
ATOM   4281 C  CA  . ASN C 1 181 ? 21.296  43.355  38.504  1.00 20.37 ? 169 ASN C CA  1 
ATOM   4282 C  C   . ASN C 1 181 ? 19.918  43.373  39.179  1.00 20.23 ? 169 ASN C C   1 
ATOM   4283 O  O   . ASN C 1 181 ? 19.818  42.932  40.321  1.00 18.99 ? 169 ASN C O   1 
ATOM   4284 C  CB  . ASN C 1 181 ? 21.228  43.437  36.977  1.00 21.17 ? 169 ASN C CB  1 
ATOM   4285 C  CG  . ASN C 1 181 ? 20.980  44.850  36.490  1.00 22.76 ? 169 ASN C CG  1 
ATOM   4286 O  OD1 . ASN C 1 181 ? 19.832  45.292  36.346  1.00 22.25 ? 169 ASN C OD1 1 
ATOM   4287 N  ND2 . ASN C 1 181 ? 22.063  45.527  36.148  1.00 26.42 ? 169 ASN C ND2 1 
ATOM   4288 N  N   . TYR C 1 182 ? 18.852  43.743  38.480  1.00 18.00 ? 170 TYR C N   1 
ATOM   4289 C  CA  . TYR C 1 182 ? 17.549  43.934  39.173  1.00 15.80 ? 170 TYR C CA  1 
ATOM   4290 C  C   . TYR C 1 182 ? 16.909  42.598  39.524  1.00 17.13 ? 170 TYR C C   1 
ATOM   4291 O  O   . TYR C 1 182 ? 17.205  41.546  38.959  1.00 16.01 ? 170 TYR C O   1 
ATOM   4292 C  CB  . TYR C 1 182 ? 16.626  44.897  38.420  1.00 16.78 ? 170 TYR C CB  1 
ATOM   4293 C  CG  . TYR C 1 182 ? 15.980  44.418  37.139  1.00 16.86 ? 170 TYR C CG  1 
ATOM   4294 C  CD1 . TYR C 1 182 ? 15.010  43.432  37.144  1.00 18.50 ? 170 TYR C CD1 1 
ATOM   4295 C  CD2 . TYR C 1 182 ? 16.319  44.985  35.924  1.00 16.86 ? 170 TYR C CD2 1 
ATOM   4296 C  CE1 . TYR C 1 182 ? 14.398  43.012  35.971  1.00 17.90 ? 170 TYR C CE1 1 
ATOM   4297 C  CE2 . TYR C 1 182 ? 15.688  44.628  34.747  1.00 18.27 ? 170 TYR C CE2 1 
ATOM   4298 C  CZ  . TYR C 1 182 ? 14.735  43.615  34.768  1.00 18.76 ? 170 TYR C CZ  1 
ATOM   4299 O  OH  . TYR C 1 182 ? 14.137  43.239  33.602  1.00 17.81 ? 170 TYR C OH  1 
ATOM   4300 N  N   . MET C 1 183 ? 16.076  42.657  40.551  1.00 16.47 ? 171 MET C N   1 
ATOM   4301 C  CA  . MET C 1 183 ? 15.168  41.561  40.924  1.00 17.80 ? 171 MET C CA  1 
ATOM   4302 C  C   . MET C 1 183 ? 13.818  42.174  41.271  1.00 17.18 ? 171 MET C C   1 
ATOM   4303 O  O   . MET C 1 183 ? 13.755  43.041  42.140  1.00 18.28 ? 171 MET C O   1 
ATOM   4304 C  CB  . MET C 1 183 ? 15.703  40.730  42.094  1.00 18.31 ? 171 MET C CB  1 
ATOM   4305 C  CG  . MET C 1 183 ? 14.812  39.503  42.384  1.00 18.97 ? 171 MET C CG  1 
ATOM   4306 S  SD  . MET C 1 183 ? 15.538  38.473  43.656  1.00 20.38 ? 171 MET C SD  1 
ATOM   4307 C  CE  . MET C 1 183 ? 15.461  39.597  45.042  1.00 22.86 ? 171 MET C CE  1 
ATOM   4308 N  N   . ILE C 1 184 ? 12.765  41.713  40.599  1.00 16.56 ? 172 ILE C N   1 
ATOM   4309 C  CA  . ILE C 1 184 ? 11.388  42.243  40.760  1.00 16.41 ? 172 ILE C CA  1 
ATOM   4310 C  C   . ILE C 1 184 ? 10.382  41.096  40.902  1.00 17.87 ? 172 ILE C C   1 
ATOM   4311 O  O   . ILE C 1 184 ? 10.685  39.946  40.475  1.00 15.83 ? 172 ILE C O   1 
ATOM   4312 C  CB  . ILE C 1 184 ? 11.022  43.158  39.578  1.00 17.28 ? 172 ILE C CB  1 
ATOM   4313 C  CG1 . ILE C 1 184 ? 11.054  42.436  38.222  1.00 17.15 ? 172 ILE C CG1 1 
ATOM   4314 C  CG2 . ILE C 1 184 ? 11.884  44.411  39.559  1.00 17.18 ? 172 ILE C CG2 1 
ATOM   4315 C  CD1 . ILE C 1 184 ? 10.616  43.302  37.095  1.00 18.66 ? 172 ILE C CD1 1 
ATOM   4316 N  N   . VAL C 1 185 ? 9.222   41.421  41.477  1.00 17.72 ? 173 VAL C N   1 
ATOM   4317 C  CA  . VAL C 1 185 ? 8.045   40.511  41.381  1.00 16.86 ? 173 VAL C CA  1 
ATOM   4318 C  C   . VAL C 1 185 ? 7.296   40.936  40.125  1.00 15.44 ? 173 VAL C C   1 
ATOM   4319 O  O   . VAL C 1 185 ? 6.753   42.056  40.102  1.00 17.38 ? 173 VAL C O   1 
ATOM   4320 C  CB  . VAL C 1 185 ? 7.141   40.497  42.620  1.00 17.99 ? 173 VAL C CB  1 
ATOM   4321 C  CG1 . VAL C 1 185 ? 6.040   39.473  42.427  1.00 20.03 ? 173 VAL C CG1 1 
ATOM   4322 C  CG2 . VAL C 1 185 ? 7.938   40.196  43.865  1.00 18.14 ? 173 VAL C CG2 1 
ATOM   4323 N  N   . ALA C 1 186 ? 7.369   40.118  39.089  1.00 14.57 ? 174 ALA C N   1 
ATOM   4324 C  CA  . ALA C 1 186 ? 7.018   40.550  37.727  1.00 15.13 ? 174 ALA C CA  1 
ATOM   4325 C  C   . ALA C 1 186 ? 5.762   39.853  37.223  1.00 16.01 ? 174 ALA C C   1 
ATOM   4326 O  O   . ALA C 1 186 ? 5.619   38.595  37.376  1.00 16.47 ? 174 ALA C O   1 
ATOM   4327 C  CB  . ALA C 1 186 ? 8.154   40.328  36.753  1.00 15.90 ? 174 ALA C CB  1 
ATOM   4328 N  N   . THR C 1 187 ? 4.961   40.637  36.521  1.00 13.90 ? 175 THR C N   1 
ATOM   4329 C  CA  . THR C 1 187 ? 3.859   40.162  35.668  1.00 14.96 ? 175 THR C CA  1 
ATOM   4330 C  C   . THR C 1 187 ? 4.367   40.191  34.224  1.00 15.51 ? 175 THR C C   1 
ATOM   4331 O  O   . THR C 1 187 ? 4.880   41.243  33.802  1.00 16.31 ? 175 THR C O   1 
ATOM   4332 C  CB  . THR C 1 187 ? 2.614   41.016  35.854  1.00 15.85 ? 175 THR C CB  1 
ATOM   4333 O  OG1 . THR C 1 187 ? 2.238   40.947  37.235  1.00 18.27 ? 175 THR C OG1 1 
ATOM   4334 C  CG2 . THR C 1 187 ? 1.468   40.547  34.985  1.00 15.83 ? 175 THR C CG2 1 
ATOM   4335 N  N   . ALA C 1 188 ? 4.300   39.058  33.532  1.00 15.05 ? 176 ALA C N   1 
ATOM   4336 C  CA  . ALA C 1 188 ? 4.736   38.986  32.121  1.00 16.39 ? 176 ALA C CA  1 
ATOM   4337 C  C   . ALA C 1 188 ? 3.581   38.465  31.284  1.00 17.82 ? 176 ALA C C   1 
ATOM   4338 O  O   . ALA C 1 188 ? 2.745   37.653  31.756  1.00 19.15 ? 176 ALA C O   1 
ATOM   4339 C  CB  . ALA C 1 188 ? 5.912   38.090  31.967  1.00 15.57 ? 176 ALA C CB  1 
ATOM   4340 N  N   . GLY C 1 189 ? 3.571   38.876  30.037  1.00 17.88 ? 177 GLY C N   1 
ATOM   4341 C  CA  . GLY C 1 189 ? 2.521   38.429  29.112  1.00 18.75 ? 177 GLY C CA  1 
ATOM   4342 C  C   . GLY C 1 189 ? 3.058   38.368  27.707  1.00 19.52 ? 177 GLY C C   1 
ATOM   4343 O  O   . GLY C 1 189 ? 4.093   39.037  27.418  1.00 19.44 ? 177 GLY C O   1 
ATOM   4344 N  N   . TYR C 1 190 ? 2.371   37.620  26.852  1.00 19.22 ? 178 TYR C N   1 
ATOM   4345 C  CA  . TYR C 1 190 ? 2.664   37.585  25.395  1.00 20.64 ? 178 TYR C CA  1 
ATOM   4346 C  C   . TYR C 1 190 ? 1.394   37.218  24.639  1.00 18.69 ? 178 TYR C C   1 
ATOM   4347 O  O   . TYR C 1 190 ? 0.866   36.129  24.916  1.00 18.10 ? 178 TYR C O   1 
ATOM   4348 C  CB  . TYR C 1 190 ? 3.746   36.564  25.076  1.00 24.69 ? 178 TYR C CB  1 
ATOM   4349 C  CG  . TYR C 1 190 ? 4.136   36.562  23.619  1.00 28.22 ? 178 TYR C CG  1 
ATOM   4350 C  CD1 . TYR C 1 190 ? 4.569   37.719  23.000  1.00 32.18 ? 178 TYR C CD1 1 
ATOM   4351 C  CD2 . TYR C 1 190 ? 4.009   35.420  22.844  1.00 35.91 ? 178 TYR C CD2 1 
ATOM   4352 C  CE1 . TYR C 1 190 ? 4.914   37.740  21.659  1.00 34.67 ? 178 TYR C CE1 1 
ATOM   4353 C  CE2 . TYR C 1 190 ? 4.363   35.423  21.505  1.00 35.92 ? 178 TYR C CE2 1 
ATOM   4354 C  CZ  . TYR C 1 190 ? 4.822   36.583  20.911  1.00 37.62 ? 178 TYR C CZ  1 
ATOM   4355 O  OH  . TYR C 1 190 ? 5.154   36.589  19.587  1.00 41.87 ? 178 TYR C OH  1 
ATOM   4356 N  N   . GLN C 1 191 ? 0.979   38.055  23.687  1.00 17.43 ? 179 GLN C N   1 
ATOM   4357 C  CA  . GLN C 1 191 ? -0.202  37.807  22.809  1.00 19.87 ? 179 GLN C CA  1 
ATOM   4358 C  C   . GLN C 1 191 ? -1.376  37.378  23.689  1.00 20.15 ? 179 GLN C C   1 
ATOM   4359 O  O   . GLN C 1 191 ? -2.011  36.305  23.462  1.00 17.91 ? 179 GLN C O   1 
ATOM   4360 C  CB  . GLN C 1 191 ? 0.171   36.792  21.729  1.00 23.04 ? 179 GLN C CB  1 
ATOM   4361 C  CG  . GLN C 1 191 ? 1.033   37.440  20.655  1.00 25.69 ? 179 GLN C CG  1 
ATOM   4362 C  CD  . GLN C 1 191 ? 1.139   36.631  19.389  1.00 28.24 ? 179 GLN C CD  1 
ATOM   4363 O  OE1 . GLN C 1 191 ? 0.835   35.444  19.370  1.00 31.17 ? 179 GLN C OE1 1 
ATOM   4364 N  NE2 . GLN C 1 191 ? 1.595   37.271  18.327  1.00 33.50 ? 179 GLN C NE2 1 
ATOM   4365 N  N   . SER C 1 192 ? -1.645  38.190  24.690  1.00 18.51 ? 180 SER C N   1 
ATOM   4366 C  CA  . SER C 1 192 ? -2.759  37.934  25.626  1.00 18.22 ? 180 SER C CA  1 
ATOM   4367 C  C   . SER C 1 192 ? -3.360  39.249  26.098  1.00 19.39 ? 180 SER C C   1 
ATOM   4368 O  O   . SER C 1 192 ? -2.947  40.284  25.653  1.00 18.76 ? 180 SER C O   1 
ATOM   4369 C  CB  . SER C 1 192 ? -2.300  37.076  26.774  1.00 20.08 ? 180 SER C CB  1 
ATOM   4370 O  OG  . SER C 1 192 ? -1.310  37.727  27.569  1.00 18.62 ? 180 SER C OG  1 
ATOM   4371 N  N   . SER C 1 193 ? -4.348  39.164  26.987  1.00 19.70 ? 181 SER C N   1 
ATOM   4372 C  CA  . SER C 1 193 ? -4.991  40.324  27.623  1.00 18.46 ? 181 SER C CA  1 
ATOM   4373 C  C   . SER C 1 193 ? -5.044  39.980  29.107  1.00 18.09 ? 181 SER C C   1 
ATOM   4374 O  O   . SER C 1 193 ? -4.875  38.818  29.446  1.00 18.40 ? 181 SER C O   1 
ATOM   4375 C  CB  . SER C 1 193 ? -6.384  40.575  27.089  1.00 20.09 ? 181 SER C CB  1 
ATOM   4376 O  OG  . SER C 1 193 ? -6.360  40.804  25.675  1.00 21.19 ? 181 SER C OG  1 
ATOM   4377 N  N   . GLY C 1 194 ? -5.202  40.971  29.928  1.00 19.91 ? 182 GLY C N   1 
ATOM   4378 C  CA  . GLY C 1 194 ? -5.340  40.693  31.362  1.00 19.90 ? 182 GLY C CA  1 
ATOM   4379 C  C   . GLY C 1 194 ? -5.214  41.922  32.197  1.00 20.84 ? 182 GLY C C   1 
ATOM   4380 O  O   . GLY C 1 194 ? -5.147  43.058  31.674  1.00 20.00 ? 182 GLY C O   1 
ATOM   4381 N  N   . SER C 1 195 ? -5.230  41.689  33.511  1.00 20.29 ? 183 SER C N   1 
ATOM   4382 C  CA  . SER C 1 195 ? -4.972  42.737  34.510  1.00 20.96 ? 183 SER C CA  1 
ATOM   4383 C  C   . SER C 1 195 ? -4.270  42.064  35.682  1.00 18.13 ? 183 SER C C   1 
ATOM   4384 O  O   . SER C 1 195 ? -4.378  40.817  35.856  1.00 19.82 ? 183 SER C O   1 
ATOM   4385 C  CB  . SER C 1 195 ? -6.250  43.427  34.919  1.00 25.74 ? 183 SER C CB  1 
ATOM   4386 O  OG  . SER C 1 195 ? -7.094  42.474  35.547  1.00 29.97 ? 183 SER C OG  1 
ATOM   4387 N  N   . ALA C 1 196 ? -3.442  42.828  36.356  1.00 18.65 ? 184 ALA C N   1 
ATOM   4388 C  CA  . ALA C 1 196 ? -2.779  42.401  37.595  1.00 19.07 ? 184 ALA C CA  1 
ATOM   4389 C  C   . ALA C 1 196 ? -2.550  43.603  38.499  1.00 18.99 ? 184 ALA C C   1 
ATOM   4390 O  O   . ALA C 1 196 ? -2.304  44.709  38.026  1.00 19.73 ? 184 ALA C O   1 
ATOM   4391 C  CB  . ALA C 1 196 ? -1.514  41.681  37.287  1.00 18.93 ? 184 ALA C CB  1 
ATOM   4392 N  N   . SER C 1 197 ? -2.685  43.365  39.795  1.00 18.99 ? 185 SER C N   1 
ATOM   4393 C  CA  . SER C 1 197 ? -2.372  44.369  40.832  1.00 20.56 ? 185 SER C CA  1 
ATOM   4394 C  C   . SER C 1 197 ? -1.581  43.641  41.921  1.00 21.33 ? 185 SER C C   1 
ATOM   4395 O  O   . SER C 1 197 ? -2.176  42.803  42.652  1.00 21.60 ? 185 SER C O   1 
ATOM   4396 C  CB  . SER C 1 197 ? -3.643  45.026  41.303  1.00 24.50 ? 185 SER C CB  1 
ATOM   4397 O  OG  . SER C 1 197 ? -3.380  45.959  42.324  1.00 33.64 ? 185 SER C OG  1 
ATOM   4398 N  N   . ILE C 1 198 ? -0.273  43.879  41.970  1.00 19.21 ? 186 ILE C N   1 
ATOM   4399 C  CA  . ILE C 1 198 ? 0.674   43.134  42.839  1.00 19.71 ? 186 ILE C CA  1 
ATOM   4400 C  C   . ILE C 1 198 ? 1.375   44.092  43.791  1.00 20.91 ? 186 ILE C C   1 
ATOM   4401 O  O   . ILE C 1 198 ? 1.679   45.288  43.409  1.00 19.27 ? 186 ILE C O   1 
ATOM   4402 C  CB  . ILE C 1 198 ? 1.667   42.316  41.982  1.00 19.55 ? 186 ILE C CB  1 
ATOM   4403 C  CG1 . ILE C 1 198 ? 0.954   41.290  41.114  1.00 20.39 ? 186 ILE C CG1 1 
ATOM   4404 C  CG2 . ILE C 1 198 ? 2.777   41.700  42.804  1.00 18.78 ? 186 ILE C CG2 1 
ATOM   4405 C  CD1 . ILE C 1 198 ? 0.223   40.225  41.879  1.00 21.69 ? 186 ILE C CD1 1 
ATOM   4406 N  N   . THR C 1 199 ? 1.499   43.651  45.046  1.00 20.06 ? 187 THR C N   1 
ATOM   4407 C  CA  . THR C 1 199 ? 2.145   44.454  46.110  1.00 20.86 ? 187 THR C CA  1 
ATOM   4408 C  C   . THR C 1 199 ? 3.360   43.692  46.616  1.00 21.46 ? 187 THR C C   1 
ATOM   4409 O  O   . THR C 1 199 ? 3.194   42.597  47.140  1.00 19.71 ? 187 THR C O   1 
ATOM   4410 C  CB  . THR C 1 199 ? 1.179   44.781  47.261  1.00 23.99 ? 187 THR C CB  1 
ATOM   4411 O  OG1 . THR C 1 199 ? 0.122   45.584  46.733  1.00 23.46 ? 187 THR C OG1 1 
ATOM   4412 C  CG2 . THR C 1 199 ? 1.886   45.482  48.399  1.00 24.06 ? 187 THR C CG2 1 
ATOM   4413 N  N   . VAL C 1 200 ? 4.552   44.258  46.482  1.00 21.07 ? 188 VAL C N   1 
ATOM   4414 C  CA  . VAL C 1 200 ? 5.769   43.669  47.111  1.00 23.81 ? 188 VAL C CA  1 
ATOM   4415 C  C   . VAL C 1 200 ? 5.810   44.266  48.523  1.00 28.02 ? 188 VAL C C   1 
ATOM   4416 O  O   . VAL C 1 200 ? 5.810   45.494  48.611  1.00 27.09 ? 188 VAL C O   1 
ATOM   4417 C  CB  . VAL C 1 200 ? 7.030   43.968  46.267  1.00 24.69 ? 188 VAL C CB  1 
ATOM   4418 C  CG1 . VAL C 1 200 ? 8.265   43.308  46.830  1.00 28.44 ? 188 VAL C CG1 1 
ATOM   4419 C  CG2 . VAL C 1 200 ? 6.827   43.598  44.811  1.00 23.75 ? 188 VAL C CG2 1 
ATOM   4420 N  N   . GLN C 1 201 ? 5.659   43.446  49.566  1.00 33.79 ? 189 GLN C N   1 
ATOM   4421 C  CA  . GLN C 1 201 ? 5.683   43.898  50.989  1.00 37.76 ? 189 GLN C CA  1 
ATOM   4422 C  C   . GLN C 1 201 ? 7.097   43.669  51.531  1.00 39.55 ? 189 GLN C C   1 
ATOM   4423 O  O   . GLN C 1 201 ? 8.044   43.686  50.729  1.00 48.21 ? 189 GLN C O   1 
ATOM   4424 C  CB  . GLN C 1 201 ? 4.644   43.172  51.845  1.00 43.00 ? 189 GLN C CB  1 
ATOM   4425 C  CG  . GLN C 1 201 ? 3.405   44.002  52.188  1.00 44.52 ? 189 GLN C CG  1 
ATOM   4426 C  CD  . GLN C 1 201 ? 2.163   43.670  51.394  1.00 47.40 ? 189 GLN C CD  1 
ATOM   4427 O  OE1 . GLN C 1 201 ? 1.119   44.292  51.571  1.00 44.67 ? 189 GLN C OE1 1 
ATOM   4428 N  NE2 . GLN C 1 201 ? 2.249   42.673  50.523  1.00 50.40 ? 189 GLN C NE2 1 
ATOM   4429 N  N   . GLU D 1 13  ? -1.218  8.805   13.026  1.00 34.23 ? 1   GLU D N   1 
ATOM   4430 C  CA  . GLU D 1 13  ? -0.893  10.096  13.745  1.00 35.74 ? 1   GLU D CA  1 
ATOM   4431 C  C   . GLU D 1 13  ? 0.301   10.808  13.091  1.00 34.06 ? 1   GLU D C   1 
ATOM   4432 O  O   . GLU D 1 13  ? 1.313   10.154  12.807  1.00 35.19 ? 1   GLU D O   1 
ATOM   4433 C  CB  . GLU D 1 13  ? -0.599  9.849   15.224  1.00 39.89 ? 1   GLU D CB  1 
ATOM   4434 C  CG  . GLU D 1 13  ? -1.850  9.580   16.026  1.00 43.57 ? 1   GLU D CG  1 
ATOM   4435 C  CD  . GLU D 1 13  ? -1.636  8.645   17.195  1.00 51.48 ? 1   GLU D CD  1 
ATOM   4436 O  OE1 . GLU D 1 13  ? -0.920  9.046   18.137  1.00 57.11 ? 1   GLU D OE1 1 
ATOM   4437 O  OE2 . GLU D 1 13  ? -2.165  7.509   17.143  1.00 53.83 ? 1   GLU D OE2 1 
ATOM   4438 N  N   . ILE D 1 14  ? 0.198   12.130  12.947  1.00 28.05 ? 2   ILE D N   1 
ATOM   4439 C  CA  . ILE D 1 14  ? 1.119   13.019  12.180  1.00 29.11 ? 2   ILE D CA  1 
ATOM   4440 C  C   . ILE D 1 14  ? 1.618   14.062  13.195  1.00 30.07 ? 2   ILE D C   1 
ATOM   4441 O  O   . ILE D 1 14  ? 0.764   14.638  13.887  1.00 27.41 ? 2   ILE D O   1 
ATOM   4442 C  CB  . ILE D 1 14  ? 0.372   13.632  10.960  1.00 27.01 ? 2   ILE D CB  1 
ATOM   4443 C  CG1 . ILE D 1 14  ? 0.015   12.575  9.905   1.00 27.53 ? 2   ILE D CG1 1 
ATOM   4444 C  CG2 . ILE D 1 14  ? 1.127   14.781  10.321  1.00 28.81 ? 2   ILE D CG2 1 
ATOM   4445 C  CD1 . ILE D 1 14  ? -1.223  12.884  9.076   1.00 26.45 ? 2   ILE D CD1 1 
ATOM   4446 N  N   . THR D 1 15  ? 2.934   14.199  13.402  1.00 28.64 ? 3   THR D N   1 
ATOM   4447 C  CA  . THR D 1 15  ? 3.470   15.118  14.450  1.00 28.72 ? 3   THR D CA  1 
ATOM   4448 C  C   . THR D 1 15  ? 4.487   16.110  13.863  1.00 26.49 ? 3   THR D C   1 
ATOM   4449 O  O   . THR D 1 15  ? 4.956   16.978  14.614  1.00 26.44 ? 3   THR D O   1 
ATOM   4450 C  CB  . THR D 1 15  ? 4.039   14.325  15.633  1.00 31.44 ? 3   THR D CB  1 
ATOM   4451 O  OG1 . THR D 1 15  ? 5.156   13.592  15.134  1.00 30.20 ? 3   THR D OG1 1 
ATOM   4452 C  CG2 . THR D 1 15  ? 3.031   13.388  16.265  1.00 31.88 ? 3   THR D CG2 1 
ATOM   4453 N  N   . SER D 1 16  ? 4.811   16.003  12.575  1.00 25.44 ? 4   SER D N   1 
ATOM   4454 C  CA  . SER D 1 16  ? 5.677   16.962  11.846  1.00 25.18 ? 4   SER D CA  1 
ATOM   4455 C  C   . SER D 1 16  ? 4.956   17.380  10.561  1.00 24.21 ? 4   SER D C   1 
ATOM   4456 O  O   . SER D 1 16  ? 4.016   16.679  10.171  1.00 25.53 ? 4   SER D O   1 
ATOM   4457 C  CB  . SER D 1 16  ? 7.043   16.381  11.580  1.00 27.20 ? 4   SER D CB  1 
ATOM   4458 O  OG  . SER D 1 16  ? 7.717   16.149  12.819  1.00 31.76 ? 4   SER D OG  1 
ATOM   4459 N  N   . SER D 1 17  ? 5.321   18.518  9.975   1.00 21.64 ? 5   SER D N   1 
ATOM   4460 C  CA  . SER D 1 17  ? 4.565   19.062  8.805   1.00 21.90 ? 5   SER D CA  1 
ATOM   4461 C  C   . SER D 1 17  ? 4.448   18.042  7.665   1.00 22.57 ? 5   SER D C   1 
ATOM   4462 O  O   . SER D 1 17  ? 5.481   17.515  7.236   1.00 20.02 ? 5   SER D O   1 
ATOM   4463 C  CB  . SER D 1 17  ? 5.179   20.320  8.325   1.00 24.89 ? 5   SER D CB  1 
ATOM   4464 O  OG  . SER D 1 17  ? 5.240   21.253  9.385   1.00 20.99 ? 5   SER D OG  1 
ATOM   4465 N  N   . GLU D 1 18  ? 3.270   17.973  7.037   1.00 20.13 ? 6   GLU D N   1 
ATOM   4466 C  CA  . GLU D 1 18  ? 2.992   17.060  5.910   1.00 22.76 ? 6   GLU D CA  1 
ATOM   4467 C  C   . GLU D 1 18  ? 1.772   17.588  5.167   1.00 22.33 ? 6   GLU D C   1 
ATOM   4468 O  O   . GLU D 1 18  ? 0.872   18.182  5.815   1.00 22.07 ? 6   GLU D O   1 
ATOM   4469 C  CB  . GLU D 1 18  ? 2.699   15.682  6.514   1.00 25.18 ? 6   GLU D CB  1 
ATOM   4470 C  CG  . GLU D 1 18  ? 2.512   14.546  5.546   1.00 29.33 ? 6   GLU D CG  1 
ATOM   4471 C  CD  . GLU D 1 18  ? 2.193   13.297  6.345   1.00 29.88 ? 6   GLU D CD  1 
ATOM   4472 O  OE1 . GLU D 1 18  ? 1.022   12.897  6.331   1.00 28.77 ? 6   GLU D OE1 1 
ATOM   4473 O  OE2 . GLU D 1 18  ? 3.107   12.817  7.085   1.00 33.59 ? 6   GLU D OE2 1 
ATOM   4474 N  N   . THR D 1 19  ? 1.699   17.319  3.873   1.00 19.59 ? 7   THR D N   1 
ATOM   4475 C  CA  . THR D 1 19  ? 0.428   17.518  3.133   1.00 19.16 ? 7   THR D CA  1 
ATOM   4476 C  C   . THR D 1 19  ? 0.146   16.216  2.391   1.00 21.28 ? 7   THR D C   1 
ATOM   4477 O  O   . THR D 1 19  ? 1.077   15.420  2.180   1.00 19.10 ? 7   THR D O   1 
ATOM   4478 C  CB  . THR D 1 19  ? 0.479   18.694  2.157   1.00 19.93 ? 7   THR D CB  1 
ATOM   4479 O  OG1 . THR D 1 19  ? 1.459   18.364  1.151   1.00 21.36 ? 7   THR D OG1 1 
ATOM   4480 C  CG2 . THR D 1 19  ? 0.823   19.999  2.842   1.00 22.71 ? 7   THR D CG2 1 
ATOM   4481 N  N   . GLY D 1 20  ? -1.091  16.036  1.987   1.00 19.22 ? 8   GLY D N   1 
ATOM   4482 C  CA  . GLY D 1 20  ? -1.424  14.999  1.014   1.00 20.10 ? 8   GLY D CA  1 
ATOM   4483 C  C   . GLY D 1 20  ? -2.898  14.997  0.736   1.00 18.57 ? 8   GLY D C   1 
ATOM   4484 O  O   . GLY D 1 20  ? -3.565  16.063  0.841   1.00 19.50 ? 8   GLY D O   1 
ATOM   4485 N  N   . THR D 1 21  ? -3.378  13.860  0.290   1.00 18.40 ? 9   THR D N   1 
ATOM   4486 C  CA  . THR D 1 21  ? -4.805  13.590  0.063   1.00 18.12 ? 9   THR D CA  1 
ATOM   4487 C  C   . THR D 1 21  ? -5.223  12.539  1.072   1.00 19.13 ? 9   THR D C   1 
ATOM   4488 O  O   . THR D 1 21  ? -4.455  11.566  1.298   1.00 18.76 ? 9   THR D O   1 
ATOM   4489 C  CB  . THR D 1 21  ? -5.048  13.069  -1.360  1.00 20.33 ? 9   THR D CB  1 
ATOM   4490 O  OG1 . THR D 1 21  ? -4.397  13.966  -2.270  1.00 22.12 ? 9   THR D OG1 1 
ATOM   4491 C  CG2 . THR D 1 21  ? -6.530  12.947  -1.636  1.00 20.29 ? 9   THR D CG2 1 
ATOM   4492 N  N   . ASN D 1 22  ? -6.360  12.731  1.720   1.00 19.92 ? 10  ASN D N   1 
ATOM   4493 C  CA  . ASN D 1 22  ? -6.907  11.686  2.618   1.00 19.71 ? 10  ASN D CA  1 
ATOM   4494 C  C   . ASN D 1 22  ? -8.404  11.614  2.355   1.00 18.22 ? 10  ASN D C   1 
ATOM   4495 O  O   . ASN D 1 22  ? -9.075  12.599  2.594   1.00 17.80 ? 10  ASN D O   1 
ATOM   4496 C  CB  . ASN D 1 22  ? -6.654  11.975  4.095   1.00 18.92 ? 10  ASN D CB  1 
ATOM   4497 C  CG  . ASN D 1 22  ? -7.230  10.885  4.961   1.00 20.34 ? 10  ASN D CG  1 
ATOM   4498 O  OD1 . ASN D 1 22  ? -8.267  11.091  5.590   1.00 19.97 ? 10  ASN D OD1 1 
ATOM   4499 N  ND2 . ASN D 1 22  ? -6.585  9.723   4.955   1.00 22.07 ? 10  ASN D ND2 1 
ATOM   4500 N  N   . ASN D 1 23  ? -8.895  10.515  1.786   1.00 16.28 ? 11  ASN D N   1 
ATOM   4501 C  CA  . ASN D 1 23  ? -10.359 10.304  1.624   1.00 17.65 ? 11  ASN D CA  1 
ATOM   4502 C  C   . ASN D 1 23  ? -11.014 11.384  0.750   1.00 20.11 ? 11  ASN D C   1 
ATOM   4503 O  O   . ASN D 1 23  ? -12.169 11.760  1.034   1.00 19.63 ? 11  ASN D O   1 
ATOM   4504 C  CB  . ASN D 1 23  ? -10.990 10.113  3.010   1.00 18.75 ? 11  ASN D CB  1 
ATOM   4505 C  CG  . ASN D 1 23  ? -10.445 8.883   3.711   1.00 22.09 ? 11  ASN D CG  1 
ATOM   4506 O  OD1 . ASN D 1 23  ? -10.330 7.816   3.111   1.00 26.92 ? 11  ASN D OD1 1 
ATOM   4507 N  ND2 . ASN D 1 23  ? -10.075 9.017   4.976   1.00 22.38 ? 11  ASN D ND2 1 
ATOM   4508 N  N   . GLY D 1 24  ? -10.346 11.803  -0.326  1.00 17.87 ? 12  GLY D N   1 
ATOM   4509 C  CA  . GLY D 1 24  ? -10.865 12.751  -1.321  1.00 20.52 ? 12  GLY D CA  1 
ATOM   4510 C  C   . GLY D 1 24  ? -10.752 14.198  -0.863  1.00 18.70 ? 12  GLY D C   1 
ATOM   4511 O  O   . GLY D 1 24  ? -11.329 15.055  -1.539  1.00 21.00 ? 12  GLY D O   1 
ATOM   4512 N  N   . TYR D 1 25  ? -10.097 14.458  0.277   1.00 18.33 ? 13  TYR D N   1 
ATOM   4513 C  CA  . TYR D 1 25  ? -9.825  15.845  0.755   1.00 18.74 ? 13  TYR D CA  1 
ATOM   4514 C  C   . TYR D 1 25  ? -8.332  16.126  0.687   1.00 16.41 ? 13  TYR D C   1 
ATOM   4515 O  O   . TYR D 1 25  ? -7.520  15.290  1.084   1.00 16.97 ? 13  TYR D O   1 
ATOM   4516 C  CB  . TYR D 1 25  ? -10.342 16.083  2.178   1.00 19.23 ? 13  TYR D CB  1 
ATOM   4517 C  CG  . TYR D 1 25  ? -11.845 16.035  2.205   1.00 20.93 ? 13  TYR D CG  1 
ATOM   4518 C  CD1 . TYR D 1 25  ? -12.516 14.818  2.283   1.00 23.68 ? 13  TYR D CD1 1 
ATOM   4519 C  CD2 . TYR D 1 25  ? -12.568 17.181  1.954   1.00 24.14 ? 13  TYR D CD2 1 
ATOM   4520 C  CE1 . TYR D 1 25  ? -13.904 14.774  2.234   1.00 24.67 ? 13  TYR D CE1 1 
ATOM   4521 C  CE2 . TYR D 1 25  ? -13.946 17.152  1.889   1.00 27.87 ? 13  TYR D CE2 1 
ATOM   4522 C  CZ  . TYR D 1 25  ? -14.610 15.946  2.040   1.00 27.89 ? 13  TYR D CZ  1 
ATOM   4523 O  OH  . TYR D 1 25  ? -15.970 15.960  1.985   1.00 35.14 ? 13  TYR D OH  1 
ATOM   4524 N  N   . TYR D 1 26  ? -8.012  17.372  0.303   1.00 16.86 ? 14  TYR D N   1 
ATOM   4525 C  CA  . TYR D 1 26  ? -6.673  17.953  0.483   1.00 15.88 ? 14  TYR D CA  1 
ATOM   4526 C  C   . TYR D 1 26  ? -6.486  18.017  1.999   1.00 15.76 ? 14  TYR D C   1 
ATOM   4527 O  O   . TYR D 1 26  ? -7.457  18.399  2.678   1.00 16.07 ? 14  TYR D O   1 
ATOM   4528 C  CB  . TYR D 1 26  ? -6.569  19.333  -0.188  1.00 18.04 ? 14  TYR D CB  1 
ATOM   4529 C  CG  . TYR D 1 26  ? -5.279  20.013  0.153   1.00 16.98 ? 14  TYR D CG  1 
ATOM   4530 C  CD1 . TYR D 1 26  ? -4.111  19.722  -0.533  1.00 17.00 ? 14  TYR D CD1 1 
ATOM   4531 C  CD2 . TYR D 1 26  ? -5.206  20.905  1.213   1.00 18.12 ? 14  TYR D CD2 1 
ATOM   4532 C  CE1 . TYR D 1 26  ? -2.899  20.283  -0.169  1.00 17.48 ? 14  TYR D CE1 1 
ATOM   4533 C  CE2 . TYR D 1 26  ? -4.004  21.462  1.598   1.00 17.79 ? 14  TYR D CE2 1 
ATOM   4534 C  CZ  . TYR D 1 26  ? -2.848  21.162  0.902   1.00 18.33 ? 14  TYR D CZ  1 
ATOM   4535 O  OH  . TYR D 1 26  ? -1.677  21.729  1.286   1.00 19.02 ? 14  TYR D OH  1 
ATOM   4536 N  N   . TYR D 1 27  ? -5.306  17.736  2.526   1.00 16.02 ? 15  TYR D N   1 
ATOM   4537 C  CA  . TYR D 1 27  ? -5.012  18.082  3.939   1.00 16.82 ? 15  TYR D CA  1 
ATOM   4538 C  C   . TYR D 1 27  ? -3.651  18.741  4.017   1.00 17.64 ? 15  TYR D C   1 
ATOM   4539 O  O   . TYR D 1 27  ? -2.692  18.372  3.320   1.00 16.74 ? 15  TYR D O   1 
ATOM   4540 C  CB  . TYR D 1 27  ? -5.183  16.910  4.926   1.00 17.70 ? 15  TYR D CB  1 
ATOM   4541 C  CG  . TYR D 1 27  ? -4.075  15.891  4.892   1.00 18.56 ? 15  TYR D CG  1 
ATOM   4542 C  CD1 . TYR D 1 27  ? -4.142  14.796  4.048   1.00 19.67 ? 15  TYR D CD1 1 
ATOM   4543 C  CD2 . TYR D 1 27  ? -2.940  16.019  5.683   1.00 17.31 ? 15  TYR D CD2 1 
ATOM   4544 C  CE1 . TYR D 1 27  ? -3.116  13.877  3.981   1.00 19.71 ? 15  TYR D CE1 1 
ATOM   4545 C  CE2 . TYR D 1 27  ? -1.916  15.089  5.646   1.00 20.72 ? 15  TYR D CE2 1 
ATOM   4546 C  CZ  . TYR D 1 27  ? -2.002  14.013  4.786   1.00 22.73 ? 15  TYR D CZ  1 
ATOM   4547 O  OH  . TYR D 1 27  ? -0.994  13.110  4.716   1.00 23.08 ? 15  TYR D OH  1 
ATOM   4548 N  N   . SER D 1 28  ? -3.580  19.760  4.891   1.00 16.30 ? 16  SER D N   1 
ATOM   4549 C  CA  . SER D 1 28  ? -2.309  20.379  5.270   1.00 15.52 ? 16  SER D CA  1 
ATOM   4550 C  C   . SER D 1 28  ? -2.163  20.312  6.790   1.00 15.09 ? 16  SER D C   1 
ATOM   4551 O  O   . SER D 1 28  ? -3.108  20.668  7.507   1.00 17.09 ? 16  SER D O   1 
ATOM   4552 C  CB  . SER D 1 28  ? -2.244  21.804  4.756   1.00 16.25 ? 16  SER D CB  1 
ATOM   4553 O  OG  . SER D 1 28  ? -0.986  22.393  5.107   1.00 18.80 ? 16  SER D OG  1 
ATOM   4554 N  N   . PHE D 1 29  ? -0.978  19.964  7.244   1.00 16.80 ? 17  PHE D N   1 
ATOM   4555 C  CA  . PHE D 1 29  ? -0.575  20.033  8.672   1.00 18.36 ? 17  PHE D CA  1 
ATOM   4556 C  C   . PHE D 1 29  ? 0.782   20.698  8.675   1.00 17.71 ? 17  PHE D C   1 
ATOM   4557 O  O   . PHE D 1 29  ? 1.721   20.201  8.038   1.00 17.53 ? 17  PHE D O   1 
ATOM   4558 C  CB  . PHE D 1 29  ? -0.542  18.675  9.377   1.00 20.17 ? 17  PHE D CB  1 
ATOM   4559 C  CG  . PHE D 1 29  ? 0.055   18.747  10.762  1.00 22.21 ? 17  PHE D CG  1 
ATOM   4560 C  CD1 . PHE D 1 29  ? -0.624  19.378  11.792  1.00 20.48 ? 17  PHE D CD1 1 
ATOM   4561 C  CD2 . PHE D 1 29  ? 1.303   18.234  11.038  1.00 23.91 ? 17  PHE D CD2 1 
ATOM   4562 C  CE1 . PHE D 1 29  ? -0.081  19.480  13.056  1.00 23.39 ? 17  PHE D CE1 1 
ATOM   4563 C  CE2 . PHE D 1 29  ? 1.845   18.332  12.312  1.00 26.63 ? 17  PHE D CE2 1 
ATOM   4564 C  CZ  . PHE D 1 29  ? 1.143   18.938  13.327  1.00 24.55 ? 17  PHE D CZ  1 
ATOM   4565 N  N   . TRP D 1 30  ? 0.824   21.887  9.268   1.00 17.63 ? 18  TRP D N   1 
ATOM   4566 C  CA  . TRP D 1 30  ? 2.067   22.682  9.366   1.00 18.40 ? 18  TRP D CA  1 
ATOM   4567 C  C   . TRP D 1 30  ? 2.293   23.037  10.830  1.00 18.66 ? 18  TRP D C   1 
ATOM   4568 O  O   . TRP D 1 30  ? 1.357   23.509  11.473  1.00 18.10 ? 18  TRP D O   1 
ATOM   4569 C  CB  . TRP D 1 30  ? 2.031   23.899  8.435   1.00 20.83 ? 18  TRP D CB  1 
ATOM   4570 C  CG  . TRP D 1 30  ? 3.309   24.674  8.544   1.00 22.68 ? 18  TRP D CG  1 
ATOM   4571 C  CD1 . TRP D 1 30  ? 4.449   24.463  7.821   1.00 24.25 ? 18  TRP D CD1 1 
ATOM   4572 C  CD2 . TRP D 1 30  ? 3.584   25.780  9.414   1.00 24.47 ? 18  TRP D CD2 1 
ATOM   4573 N  NE1 . TRP D 1 30  ? 5.424   25.344  8.200   1.00 25.28 ? 18  TRP D NE1 1 
ATOM   4574 C  CE2 . TRP D 1 30  ? 4.924   26.165  9.170   1.00 25.70 ? 18  TRP D CE2 1 
ATOM   4575 C  CE3 . TRP D 1 30  ? 2.844   26.462  10.388  1.00 23.14 ? 18  TRP D CE3 1 
ATOM   4576 C  CZ2 . TRP D 1 30  ? 5.533   27.203  9.865   1.00 25.43 ? 18  TRP D CZ2 1 
ATOM   4577 C  CZ3 . TRP D 1 30  ? 3.463   27.467  11.088  1.00 26.67 ? 18  TRP D CZ3 1 
ATOM   4578 C  CH2 . TRP D 1 30  ? 4.784   27.824  10.826  1.00 23.69 ? 18  TRP D CH2 1 
ATOM   4579 N  N   . THR D 1 31  ? 3.494   22.774  11.328  1.00 20.06 ? 19  THR D N   1 
ATOM   4580 C  CA  . THR D 1 31  ? 3.906   23.162  12.697  1.00 20.25 ? 19  THR D CA  1 
ATOM   4581 C  C   . THR D 1 31  ? 5.343   23.661  12.605  1.00 24.32 ? 19  THR D C   1 
ATOM   4582 O  O   . THR D 1 31  ? 6.131   23.068  11.829  1.00 22.35 ? 19  THR D O   1 
ATOM   4583 C  CB  . THR D 1 31  ? 3.732   22.020  13.705  1.00 22.29 ? 19  THR D CB  1 
ATOM   4584 O  OG1 . THR D 1 31  ? 4.185   22.533  14.960  1.00 23.60 ? 19  THR D OG1 1 
ATOM   4585 C  CG2 . THR D 1 31  ? 4.534   20.779  13.369  1.00 24.60 ? 19  THR D CG2 1 
ATOM   4586 N  N   . ASP D 1 32  ? 5.653   24.750  13.316  1.00 23.90 ? 20  ASP D N   1 
ATOM   4587 C  CA  . ASP D 1 32  ? 7.053   25.221  13.520  1.00 24.82 ? 20  ASP D CA  1 
ATOM   4588 C  C   . ASP D 1 32  ? 7.826   24.227  14.411  1.00 26.91 ? 20  ASP D C   1 
ATOM   4589 O  O   . ASP D 1 32  ? 9.060   24.395  14.534  1.00 31.52 ? 20  ASP D O   1 
ATOM   4590 C  CB  . ASP D 1 32  ? 7.051   26.662  14.050  1.00 26.14 ? 20  ASP D CB  1 
ATOM   4591 C  CG  . ASP D 1 32  ? 6.499   26.820  15.463  1.00 26.13 ? 20  ASP D CG  1 
ATOM   4592 O  OD1 . ASP D 1 32  ? 6.276   25.791  16.151  1.00 28.44 ? 20  ASP D OD1 1 
ATOM   4593 O  OD2 . ASP D 1 32  ? 6.299   27.958  15.867  1.00 27.79 ? 20  ASP D OD2 1 
ATOM   4594 N  N   . GLY D 1 33  ? 7.168   23.211  14.987  1.00 28.18 ? 21  GLY D N   1 
ATOM   4595 C  CA  . GLY D 1 33  ? 7.801   22.055  15.663  1.00 30.38 ? 21  GLY D CA  1 
ATOM   4596 C  C   . GLY D 1 33  ? 7.860   22.219  17.179  1.00 30.07 ? 21  GLY D C   1 
ATOM   4597 O  O   . GLY D 1 33  ? 8.325   21.307  17.878  1.00 31.70 ? 21  GLY D O   1 
ATOM   4598 N  N   . GLY D 1 34  ? 7.323   23.309  17.710  1.00 26.43 ? 22  GLY D N   1 
ATOM   4599 C  CA  . GLY D 1 34  ? 7.341   23.575  19.158  1.00 25.92 ? 22  GLY D CA  1 
ATOM   4600 C  C   . GLY D 1 34  ? 6.287   22.770  19.892  1.00 26.14 ? 22  GLY D C   1 
ATOM   4601 O  O   . GLY D 1 34  ? 5.203   22.518  19.328  1.00 24.43 ? 22  GLY D O   1 
ATOM   4602 N  N   . GLY D 1 35  ? 6.574   22.391  21.140  1.00 28.17 ? 23  GLY D N   1 
ATOM   4603 C  CA  . GLY D 1 35  ? 5.640   21.640  21.996  1.00 25.97 ? 23  GLY D CA  1 
ATOM   4604 C  C   . GLY D 1 35  ? 5.275   20.303  21.372  1.00 27.42 ? 23  GLY D C   1 
ATOM   4605 O  O   . GLY D 1 35  ? 6.087   19.782  20.581  1.00 27.04 ? 23  GLY D O   1 
ATOM   4606 N  N   . GLN D 1 36  ? 4.068   19.824  21.654  1.00 25.02 ? 24  GLN D N   1 
ATOM   4607 C  CA  . GLN D 1 36  ? 3.486   18.586  21.075  1.00 28.47 ? 24  GLN D CA  1 
ATOM   4608 C  C   . GLN D 1 36  ? 2.222   18.987  20.315  1.00 24.03 ? 24  GLN D C   1 
ATOM   4609 O  O   . GLN D 1 36  ? 1.323   19.594  20.918  1.00 25.68 ? 24  GLN D O   1 
ATOM   4610 C  CB  . GLN D 1 36  ? 3.201   17.562  22.166  1.00 32.10 ? 24  GLN D CB  1 
ATOM   4611 C  CG  . GLN D 1 36  ? 2.851   16.173  21.646  1.00 39.80 ? 24  GLN D CG  1 
ATOM   4612 C  CD  . GLN D 1 36  ? 4.003   15.196  21.704  1.00 43.66 ? 24  GLN D CD  1 
ATOM   4613 O  OE1 . GLN D 1 36  ? 5.158   15.524  21.421  1.00 45.79 ? 24  GLN D OE1 1 
ATOM   4614 N  NE2 . GLN D 1 36  ? 3.675   13.956  22.039  1.00 53.56 ? 24  GLN D NE2 1 
ATOM   4615 N  N   . VAL D 1 37  ? 2.218   18.751  19.015  1.00 21.86 ? 25  VAL D N   1 
ATOM   4616 C  CA  . VAL D 1 37  ? 0.999   18.884  18.175  1.00 21.51 ? 25  VAL D CA  1 
ATOM   4617 C  C   . VAL D 1 37  ? 0.789   17.574  17.440  1.00 21.80 ? 25  VAL D C   1 
ATOM   4618 O  O   . VAL D 1 37  ? 1.700   17.207  16.658  1.00 25.15 ? 25  VAL D O   1 
ATOM   4619 C  CB  . VAL D 1 37  ? 1.093   20.042  17.170  1.00 20.89 ? 25  VAL D CB  1 
ATOM   4620 C  CG1 . VAL D 1 37  ? -0.228  20.229  16.437  1.00 18.61 ? 25  VAL D CG1 1 
ATOM   4621 C  CG2 . VAL D 1 37  ? 1.507   21.329  17.839  1.00 20.93 ? 25  VAL D CG2 1 
ATOM   4622 N  N   . THR D 1 38  ? -0.375  16.949  17.630  1.00 22.44 ? 26  THR D N   1 
ATOM   4623 C  CA  . THR D 1 38  ? -0.718  15.618  17.029  1.00 23.08 ? 26  THR D CA  1 
ATOM   4624 C  C   . THR D 1 38  ? -1.977  15.770  16.152  1.00 22.11 ? 26  THR D C   1 
ATOM   4625 O  O   . THR D 1 38  ? -3.071  16.017  16.699  1.00 22.46 ? 26  THR D O   1 
ATOM   4626 C  CB  . THR D 1 38  ? -0.862  14.538  18.100  1.00 25.14 ? 26  THR D CB  1 
ATOM   4627 O  OG1 . THR D 1 38  ? 0.314   14.517  18.908  1.00 28.12 ? 26  THR D OG1 1 
ATOM   4628 C  CG2 . THR D 1 38  ? -1.088  13.163  17.502  1.00 28.65 ? 26  THR D CG2 1 
ATOM   4629 N  N   . TYR D 1 39  ? -1.812  15.541  14.849  1.00 18.90 ? 27  TYR D N   1 
ATOM   4630 C  CA  . TYR D 1 39  ? -2.849  15.683  13.795  1.00 19.53 ? 27  TYR D CA  1 
ATOM   4631 C  C   . TYR D 1 39  ? -3.237  14.268  13.343  1.00 18.46 ? 27  TYR D C   1 
ATOM   4632 O  O   . TYR D 1 39  ? -2.339  13.417  13.113  1.00 22.29 ? 27  TYR D O   1 
ATOM   4633 C  CB  . TYR D 1 39  ? -2.346  16.553  12.634  1.00 19.59 ? 27  TYR D CB  1 
ATOM   4634 C  CG  . TYR D 1 39  ? -3.300  16.606  11.464  1.00 20.80 ? 27  TYR D CG  1 
ATOM   4635 C  CD1 . TYR D 1 39  ? -3.252  15.637  10.471  1.00 22.13 ? 27  TYR D CD1 1 
ATOM   4636 C  CD2 . TYR D 1 39  ? -4.234  17.623  11.338  1.00 19.64 ? 27  TYR D CD2 1 
ATOM   4637 C  CE1 . TYR D 1 39  ? -4.159  15.631  9.424   1.00 21.82 ? 27  TYR D CE1 1 
ATOM   4638 C  CE2 . TYR D 1 39  ? -5.134  17.654  10.279  1.00 21.45 ? 27  TYR D CE2 1 
ATOM   4639 C  CZ  . TYR D 1 39  ? -5.075  16.660  9.304   1.00 21.67 ? 27  TYR D CZ  1 
ATOM   4640 O  OH  . TYR D 1 39  ? -5.959  16.645  8.269   1.00 21.03 ? 27  TYR D OH  1 
ATOM   4641 N  N   . THR D 1 40  ? -4.532  14.050  13.222  1.00 17.54 ? 28  THR D N   1 
ATOM   4642 C  CA  . THR D 1 40  ? -5.100  12.735  12.840  1.00 21.82 ? 28  THR D CA  1 
ATOM   4643 C  C   . THR D 1 40  ? -6.140  12.928  11.732  1.00 22.41 ? 28  THR D C   1 
ATOM   4644 O  O   . THR D 1 40  ? -7.137  13.651  11.958  1.00 22.77 ? 28  THR D O   1 
ATOM   4645 C  CB  . THR D 1 40  ? -5.669  12.012  14.069  1.00 24.32 ? 28  THR D CB  1 
ATOM   4646 O  OG1 . THR D 1 40  ? -4.618  11.895  15.039  1.00 27.73 ? 28  THR D OG1 1 
ATOM   4647 C  CG2 . THR D 1 40  ? -6.210  10.645  13.711  1.00 28.50 ? 28  THR D CG2 1 
ATOM   4648 N  N   . ASN D 1 41  ? -5.984  12.193  10.624  1.00 19.99 ? 29  ASN D N   1 
ATOM   4649 C  CA  . ASN D 1 41  ? -7.003  12.188  9.543   1.00 20.48 ? 29  ASN D CA  1 
ATOM   4650 C  C   . ASN D 1 41  ? -8.054  11.161  9.907   1.00 23.03 ? 29  ASN D C   1 
ATOM   4651 O  O   . ASN D 1 41  ? -7.657  9.993   10.212  1.00 24.61 ? 29  ASN D O   1 
ATOM   4652 C  CB  . ASN D 1 41  ? -6.421  11.853  8.164   1.00 20.25 ? 29  ASN D CB  1 
ATOM   4653 C  CG  . ASN D 1 41  ? -5.777  13.043  7.487   1.00 20.30 ? 29  ASN D CG  1 
ATOM   4654 O  OD1 . ASN D 1 41  ? -6.327  14.141  7.510   1.00 23.48 ? 29  ASN D OD1 1 
ATOM   4655 N  ND2 . ASN D 1 41  ? -4.579  12.841  6.940   1.00 22.17 ? 29  ASN D ND2 1 
ATOM   4656 N  N   . GLY D 1 42  ? -9.324  11.551  9.835   1.00 22.87 ? 30  GLY D N   1 
ATOM   4657 C  CA  . GLY D 1 42  ? -10.412 10.571  10.014  1.00 25.17 ? 30  GLY D CA  1 
ATOM   4658 C  C   . GLY D 1 42  ? -11.066 10.216  8.688   1.00 25.15 ? 30  GLY D C   1 
ATOM   4659 O  O   . GLY D 1 42  ? -10.614 10.597  7.604   1.00 25.99 ? 30  GLY D O   1 
ATOM   4660 N  N   . PRO D 1 43  ? -12.247 9.585   8.758   1.00 22.81 ? 31  PRO D N   1 
ATOM   4661 C  CA  . PRO D 1 43  ? -13.014 9.285   7.553   1.00 23.04 ? 31  PRO D CA  1 
ATOM   4662 C  C   . PRO D 1 43  ? -13.519 10.552  6.861   1.00 23.36 ? 31  PRO D C   1 
ATOM   4663 O  O   . PRO D 1 43  ? -13.797 11.509  7.565   1.00 23.54 ? 31  PRO D O   1 
ATOM   4664 C  CB  . PRO D 1 43  ? -14.190 8.447   8.064   1.00 25.61 ? 31  PRO D CB  1 
ATOM   4665 C  CG  . PRO D 1 43  ? -14.282 8.719   9.555   1.00 27.89 ? 31  PRO D CG  1 
ATOM   4666 C  CD  . PRO D 1 43  ? -12.902 9.157   10.014  1.00 25.30 ? 31  PRO D CD  1 
ATOM   4667 N  N   . ALA D 1 44  ? -13.702 10.483  5.537   1.00 24.82 ? 32  ALA D N   1 
ATOM   4668 C  CA  . ALA D 1 44  ? -14.307 11.526  4.684   1.00 22.73 ? 32  ALA D CA  1 
ATOM   4669 C  C   . ALA D 1 44  ? -13.596 12.854  4.995   1.00 21.36 ? 32  ALA D C   1 
ATOM   4670 O  O   . ALA D 1 44  ? -12.362 12.877  4.912   1.00 21.67 ? 32  ALA D O   1 
ATOM   4671 C  CB  . ALA D 1 44  ? -15.811 11.575  4.919   1.00 23.36 ? 32  ALA D CB  1 
ATOM   4672 N  N   . GLY D 1 45  ? -14.328 13.882  5.404   1.00 19.25 ? 33  GLY D N   1 
ATOM   4673 C  CA  . GLY D 1 45  ? -13.733 15.228  5.582   1.00 19.48 ? 33  GLY D CA  1 
ATOM   4674 C  C   . GLY D 1 45  ? -13.273 15.498  7.000   1.00 17.85 ? 33  GLY D C   1 
ATOM   4675 O  O   . GLY D 1 45  ? -13.160 16.703  7.346   1.00 20.72 ? 33  GLY D O   1 
ATOM   4676 N  N   . GLN D 1 46  ? -13.069 14.485  7.831   1.00 20.11 ? 34  GLN D N   1 
ATOM   4677 C  CA  . GLN D 1 46  ? -12.824 14.690  9.273   1.00 20.88 ? 34  GLN D CA  1 
ATOM   4678 C  C   . GLN D 1 46  ? -11.329 14.757  9.546   1.00 19.02 ? 34  GLN D C   1 
ATOM   4679 O  O   . GLN D 1 46  ? -10.540 14.001  8.924   1.00 20.90 ? 34  GLN D O   1 
ATOM   4680 C  CB  . GLN D 1 46  ? -13.476 13.607  10.130  1.00 25.79 ? 34  GLN D CB  1 
ATOM   4681 C  CG  . GLN D 1 46  ? -13.436 13.928  11.619  1.00 28.61 ? 34  GLN D CG  1 
ATOM   4682 C  CD  . GLN D 1 46  ? -12.811 12.792  12.371  1.00 34.41 ? 34  GLN D CD  1 
ATOM   4683 O  OE1 . GLN D 1 46  ? -13.487 11.823  12.712  1.00 41.72 ? 34  GLN D OE1 1 
ATOM   4684 N  NE2 . GLN D 1 46  ? -11.505 12.878  12.570  1.00 36.17 ? 34  GLN D NE2 1 
ATOM   4685 N  N   . TYR D 1 47  ? -10.951 15.637  10.470  1.00 17.78 ? 35  TYR D N   1 
ATOM   4686 C  CA  . TYR D 1 47  ? -9.617  15.622  11.093  1.00 17.47 ? 35  TYR D CA  1 
ATOM   4687 C  C   . TYR D 1 47  ? -9.747  16.016  12.550  1.00 17.49 ? 35  TYR D C   1 
ATOM   4688 O  O   . TYR D 1 47  ? -10.719 16.674  12.949  1.00 18.05 ? 35  TYR D O   1 
ATOM   4689 C  CB  . TYR D 1 47  ? -8.645  16.511  10.330  1.00 17.04 ? 35  TYR D CB  1 
ATOM   4690 C  CG  . TYR D 1 47  ? -8.903  17.996  10.495  1.00 17.85 ? 35  TYR D CG  1 
ATOM   4691 C  CD1 . TYR D 1 47  ? -8.303  18.686  11.531  1.00 17.39 ? 35  TYR D CD1 1 
ATOM   4692 C  CD2 . TYR D 1 47  ? -9.777  18.686  9.657   1.00 18.78 ? 35  TYR D CD2 1 
ATOM   4693 C  CE1 . TYR D 1 47  ? -8.526  20.037  11.703  1.00 17.49 ? 35  TYR D CE1 1 
ATOM   4694 C  CE2 . TYR D 1 47  ? -10.037 20.041  9.847   1.00 18.02 ? 35  TYR D CE2 1 
ATOM   4695 C  CZ  . TYR D 1 47  ? -9.425  20.708  10.893  1.00 17.00 ? 35  TYR D CZ  1 
ATOM   4696 O  OH  . TYR D 1 47  ? -9.576  22.065  11.054  1.00 16.04 ? 35  TYR D OH  1 
ATOM   4697 N  N   . SER D 1 48  ? -8.718  15.672  13.296  1.00 19.61 ? 36  SER D N   1 
ATOM   4698 C  CA  . SER D 1 48  ? -8.634  16.050  14.717  1.00 22.26 ? 36  SER D CA  1 
ATOM   4699 C  C   . SER D 1 48  ? -7.244  16.611  14.957  1.00 20.65 ? 36  SER D C   1 
ATOM   4700 O  O   . SER D 1 48  ? -6.268  16.218  14.273  1.00 20.26 ? 36  SER D O   1 
ATOM   4701 C  CB  . SER D 1 48  ? -9.003  14.878  15.601  1.00 25.87 ? 36  SER D CB  1 
ATOM   4702 O  OG  . SER D 1 48  ? -8.038  13.857  15.493  1.00 33.44 ? 36  SER D OG  1 
ATOM   4703 N  N   . VAL D 1 49  ? -7.134  17.553  15.878  1.00 21.79 ? 37  VAL D N   1 
ATOM   4704 C  CA  . VAL D 1 49  ? -5.791  17.978  16.346  1.00 20.92 ? 37  VAL D CA  1 
ATOM   4705 C  C   . VAL D 1 49  ? -5.852  18.071  17.863  1.00 21.58 ? 37  VAL D C   1 
ATOM   4706 O  O   . VAL D 1 49  ? -6.903  18.391  18.377  1.00 20.35 ? 37  VAL D O   1 
ATOM   4707 C  CB  . VAL D 1 49  ? -5.341  19.269  15.627  1.00 24.74 ? 37  VAL D CB  1 
ATOM   4708 C  CG1 . VAL D 1 49  ? -6.273  20.433  15.838  1.00 27.30 ? 37  VAL D CG1 1 
ATOM   4709 C  CG2 . VAL D 1 49  ? -3.904  19.646  15.958  1.00 25.45 ? 37  VAL D CG2 1 
ATOM   4710 N  N   . GLU D 1 50  ? -4.774  17.670  18.513  1.00 21.59 ? 38  GLU D N   1 
ATOM   4711 C  CA  . GLU D 1 50  ? -4.579  17.742  19.987  1.00 26.13 ? 38  GLU D CA  1 
ATOM   4712 C  C   . GLU D 1 50  ? -3.236  18.420  20.147  1.00 23.20 ? 38  GLU D C   1 
ATOM   4713 O  O   . GLU D 1 50  ? -2.273  17.993  19.461  1.00 22.38 ? 38  GLU D O   1 
ATOM   4714 C  CB  . GLU D 1 50  ? -4.431  16.391  20.702  1.00 31.87 ? 38  GLU D CB  1 
ATOM   4715 C  CG  . GLU D 1 50  ? -5.557  15.389  20.486  1.00 42.85 ? 38  GLU D CG  1 
ATOM   4716 C  CD  . GLU D 1 50  ? -5.302  14.010  21.093  1.00 46.92 ? 38  GLU D CD  1 
ATOM   4717 O  OE1 . GLU D 1 50  ? -4.168  13.474  20.917  1.00 49.25 ? 38  GLU D OE1 1 
ATOM   4718 O  OE2 . GLU D 1 50  ? -6.239  13.454  21.742  1.00 55.72 ? 38  GLU D OE2 1 
ATOM   4719 N  N   . TRP D 1 51  ? -3.154  19.466  20.964  1.00 23.21 ? 39  TRP D N   1 
ATOM   4720 C  CA  . TRP D 1 51  ? -1.861  20.158  21.109  1.00 21.44 ? 39  TRP D CA  1 
ATOM   4721 C  C   . TRP D 1 51  ? -1.632  20.494  22.578  1.00 19.62 ? 39  TRP D C   1 
ATOM   4722 O  O   . TRP D 1 51  ? -2.614  20.661  23.343  1.00 22.24 ? 39  TRP D O   1 
ATOM   4723 C  CB  . TRP D 1 51  ? -1.751  21.361  20.148  1.00 21.00 ? 39  TRP D CB  1 
ATOM   4724 C  CG  . TRP D 1 51  ? -2.660  22.527  20.395  1.00 19.91 ? 39  TRP D CG  1 
ATOM   4725 C  CD1 . TRP D 1 51  ? -2.325  23.692  21.022  1.00 20.82 ? 39  TRP D CD1 1 
ATOM   4726 C  CD2 . TRP D 1 51  ? -4.033  22.693  19.978  1.00 20.29 ? 39  TRP D CD2 1 
ATOM   4727 N  NE1 . TRP D 1 51  ? -3.372  24.558  21.026  1.00 19.81 ? 39  TRP D NE1 1 
ATOM   4728 C  CE2 . TRP D 1 51  ? -4.426  23.992  20.376  1.00 20.45 ? 39  TRP D CE2 1 
ATOM   4729 C  CE3 . TRP D 1 51  ? -4.965  21.901  19.296  1.00 19.40 ? 39  TRP D CE3 1 
ATOM   4730 C  CZ2 . TRP D 1 51  ? -5.712  24.479  20.178  1.00 20.34 ? 39  TRP D CZ2 1 
ATOM   4731 C  CZ3 . TRP D 1 51  ? -6.239  22.393  19.086  1.00 19.03 ? 39  TRP D CZ3 1 
ATOM   4732 C  CH2 . TRP D 1 51  ? -6.593  23.689  19.493  1.00 18.76 ? 39  TRP D CH2 1 
ATOM   4733 N  N   . SER D 1 52  ? -0.369  20.528  22.951  1.00 20.20 ? 40  SER D N   1 
ATOM   4734 C  CA  . SER D 1 52  ? 0.082   20.880  24.315  1.00 21.95 ? 40  SER D CA  1 
ATOM   4735 C  C   . SER D 1 52  ? 1.301   21.790  24.215  1.00 21.33 ? 40  SER D C   1 
ATOM   4736 O  O   . SER D 1 52  ? 2.310   21.350  23.652  1.00 22.71 ? 40  SER D O   1 
ATOM   4737 C  CB  . SER D 1 52  ? 0.404   19.645  25.122  1.00 25.58 ? 40  SER D CB  1 
ATOM   4738 O  OG  . SER D 1 52  ? 1.032   20.062  26.330  1.00 34.88 ? 40  SER D OG  1 
ATOM   4739 N  N   . ASN D 1 53  ? 1.188   23.032  24.725  1.00 20.78 ? 41  ASN D N   1 
ATOM   4740 C  CA  . ASN D 1 53  ? 2.305   24.002  24.795  1.00 21.51 ? 41  ASN D CA  1 
ATOM   4741 C  C   . ASN D 1 53  ? 2.936   24.148  23.418  1.00 21.38 ? 41  ASN D C   1 
ATOM   4742 O  O   . ASN D 1 53  ? 4.148   24.098  23.327  1.00 20.91 ? 41  ASN D O   1 
ATOM   4743 C  CB  . ASN D 1 53  ? 3.375   23.594  25.803  1.00 24.43 ? 41  ASN D CB  1 
ATOM   4744 C  CG  . ASN D 1 53  ? 2.811   23.579  27.206  1.00 25.39 ? 41  ASN D CG  1 
ATOM   4745 O  OD1 . ASN D 1 53  ? 2.282   24.590  27.660  1.00 23.53 ? 41  ASN D OD1 1 
ATOM   4746 N  ND2 . ASN D 1 53  ? 2.880   22.431  27.862  1.00 25.99 ? 41  ASN D ND2 1 
ATOM   4747 N  N   . SER D 1 54  ? 2.108   24.350  22.404  1.00 20.84 ? 42  SER D N   1 
ATOM   4748 C  CA  . SER D 1 54  ? 2.515   24.331  20.988  1.00 21.66 ? 42  SER D CA  1 
ATOM   4749 C  C   . SER D 1 54  ? 3.394   25.533  20.659  1.00 22.19 ? 42  SER D C   1 
ATOM   4750 O  O   . SER D 1 54  ? 3.301   26.573  21.314  1.00 21.72 ? 42  SER D O   1 
ATOM   4751 C  CB  . SER D 1 54  ? 1.261   24.349  20.122  1.00 22.62 ? 42  SER D CB  1 
ATOM   4752 O  OG  . SER D 1 54  ? 0.643   25.629  20.183  1.00 23.76 ? 42  SER D OG  1 
ATOM   4753 N  N   . GLY D 1 55  ? 4.169   25.435  19.588  1.00 21.85 ? 43  GLY D N   1 
ATOM   4754 C  CA  . GLY D 1 55  ? 4.533   26.634  18.833  1.00 20.75 ? 43  GLY D CA  1 
ATOM   4755 C  C   . GLY D 1 55  ? 3.386   27.015  17.913  1.00 22.04 ? 43  GLY D C   1 
ATOM   4756 O  O   . GLY D 1 55  ? 2.188   26.834  18.310  1.00 21.04 ? 43  GLY D O   1 
ATOM   4757 N  N   . ASN D 1 56  ? 3.716   27.580  16.758  1.00 21.00 ? 44  ASN D N   1 
ATOM   4758 C  CA  . ASN D 1 56  ? 2.739   27.920  15.693  1.00 21.26 ? 44  ASN D CA  1 
ATOM   4759 C  C   . ASN D 1 56  ? 2.368   26.612  14.991  1.00 18.62 ? 44  ASN D C   1 
ATOM   4760 O  O   . ASN D 1 56  ? 3.303   25.897  14.555  1.00 17.37 ? 44  ASN D O   1 
ATOM   4761 C  CB  . ASN D 1 56  ? 3.296   28.936  14.694  1.00 25.69 ? 44  ASN D CB  1 
ATOM   4762 C  CG  . ASN D 1 56  ? 3.391   30.332  15.268  1.00 31.73 ? 44  ASN D CG  1 
ATOM   4763 O  OD1 . ASN D 1 56  ? 4.479   30.893  15.364  1.00 42.78 ? 44  ASN D OD1 1 
ATOM   4764 N  ND2 . ASN D 1 56  ? 2.266   30.907  15.656  1.00 32.69 ? 44  ASN D ND2 1 
ATOM   4765 N  N   . PHE D 1 57  ? 1.071   26.383  14.788  1.00 17.64 ? 45  PHE D N   1 
ATOM   4766 C  CA  . PHE D 1 57  ? 0.589   25.372  13.833  1.00 16.46 ? 45  PHE D CA  1 
ATOM   4767 C  C   . PHE D 1 57  ? -0.696  25.860  13.178  1.00 16.50 ? 45  PHE D C   1 
ATOM   4768 O  O   . PHE D 1 57  ? -1.460  26.673  13.739  1.00 15.94 ? 45  PHE D O   1 
ATOM   4769 C  CB  . PHE D 1 57  ? 0.465   24.004  14.530  1.00 15.82 ? 45  PHE D CB  1 
ATOM   4770 C  CG  . PHE D 1 57  ? -0.788  23.876  15.356  1.00 15.44 ? 45  PHE D CG  1 
ATOM   4771 C  CD1 . PHE D 1 57  ? -1.995  23.567  14.761  1.00 14.71 ? 45  PHE D CD1 1 
ATOM   4772 C  CD2 . PHE D 1 57  ? -0.778  24.211  16.703  1.00 16.58 ? 45  PHE D CD2 1 
ATOM   4773 C  CE1 . PHE D 1 57  ? -3.157  23.515  15.512  1.00 15.32 ? 45  PHE D CE1 1 
ATOM   4774 C  CE2 . PHE D 1 57  ? -1.940  24.166  17.454  1.00 16.98 ? 45  PHE D CE2 1 
ATOM   4775 C  CZ  . PHE D 1 57  ? -3.131  23.834  16.854  1.00 17.51 ? 45  PHE D CZ  1 
ATOM   4776 N  N   . VAL D 1 58  ? -0.953  25.295  12.003  1.00 16.85 ? 46  VAL D N   1 
ATOM   4777 C  CA  . VAL D 1 58  ? -2.204  25.491  11.227  1.00 18.47 ? 46  VAL D CA  1 
ATOM   4778 C  C   . VAL D 1 58  ? -2.450  24.165  10.527  1.00 17.96 ? 46  VAL D C   1 
ATOM   4779 O  O   . VAL D 1 58  ? -1.540  23.716  9.819   1.00 17.63 ? 46  VAL D O   1 
ATOM   4780 C  CB  . VAL D 1 58  ? -2.148  26.638  10.196  1.00 21.67 ? 46  VAL D CB  1 
ATOM   4781 C  CG1 . VAL D 1 58  ? -3.544  26.883  9.600   1.00 21.31 ? 46  VAL D CG1 1 
ATOM   4782 C  CG2 . VAL D 1 58  ? -1.588  27.923  10.750  1.00 26.19 ? 46  VAL D CG2 1 
ATOM   4783 N  N   . ALA D 1 59  ? -3.662  23.633  10.610  1.00 16.56 ? 47  ALA D N   1 
ATOM   4784 C  CA  . ALA D 1 59  ? -3.951  22.260  10.123  1.00 16.79 ? 47  ALA D CA  1 
ATOM   4785 C  C   . ALA D 1 59  ? -5.413  22.076  9.731   1.00 15.13 ? 47  ALA D C   1 
ATOM   4786 O  O   . ALA D 1 59  ? -6.305  22.639  10.378  1.00 15.41 ? 47  ALA D O   1 
ATOM   4787 C  CB  . ALA D 1 59  ? -3.583  21.315  11.192  1.00 17.55 ? 47  ALA D CB  1 
ATOM   4788 N  N   . GLY D 1 60  ? -5.651  21.333  8.665   1.00 15.81 ? 48  GLY D N   1 
ATOM   4789 C  CA  . GLY D 1 60  ? -7.008  20.852  8.386   1.00 15.13 ? 48  GLY D CA  1 
ATOM   4790 C  C   . GLY D 1 60  ? -7.205  20.386  6.977   1.00 14.27 ? 48  GLY D C   1 
ATOM   4791 O  O   . GLY D 1 60  ? -6.194  20.169  6.264   1.00 14.21 ? 48  GLY D O   1 
ATOM   4792 N  N   . LYS D 1 61  ? -8.473  20.228  6.617   1.00 15.95 ? 49  LYS D N   1 
ATOM   4793 C  CA  . LYS D 1 61  ? -8.912  19.573  5.367   1.00 17.47 ? 49  LYS D CA  1 
ATOM   4794 C  C   . LYS D 1 61  ? -9.736  20.518  4.501   1.00 16.77 ? 49  LYS D C   1 
ATOM   4795 O  O   . LYS D 1 61  ? -10.421 21.490  4.999   1.00 16.22 ? 49  LYS D O   1 
ATOM   4796 C  CB  . LYS D 1 61  ? -9.771  18.313  5.609   1.00 18.45 ? 49  LYS D CB  1 
ATOM   4797 C  CG  . LYS D 1 61  ? -9.025  17.011  5.850   1.00 18.65 ? 49  LYS D CG  1 
ATOM   4798 C  CD  . LYS D 1 61  ? -9.932  15.821  6.044   1.00 19.24 ? 49  LYS D CD  1 
ATOM   4799 C  CE  . LYS D 1 61  ? -9.207  14.517  5.828   1.00 20.70 ? 49  LYS D CE  1 
ATOM   4800 N  NZ  . LYS D 1 61  ? -9.980  13.348  6.293   1.00 20.07 ? 49  LYS D NZ  1 
ATOM   4801 N  N   . GLY D 1 62  ? -9.690  20.244  3.198   1.00 16.98 ? 50  GLY D N   1 
ATOM   4802 C  CA  . GLY D 1 62  ? -10.436 21.024  2.208   1.00 18.02 ? 50  GLY D CA  1 
ATOM   4803 C  C   . GLY D 1 62  ? -10.082 20.597  0.803   1.00 19.40 ? 50  GLY D C   1 
ATOM   4804 O  O   . GLY D 1 62  ? -10.151 19.346  0.492   1.00 17.76 ? 50  GLY D O   1 
ATOM   4805 N  N   . TRP D 1 63  ? -9.668  21.571  0.006   1.00 16.56 ? 51  TRP D N   1 
ATOM   4806 C  CA  . TRP D 1 63  ? -9.680  21.464  -1.464  1.00 18.37 ? 51  TRP D CA  1 
ATOM   4807 C  C   . TRP D 1 63  ? -8.419  22.040  -2.060  1.00 16.21 ? 51  TRP D C   1 
ATOM   4808 O  O   . TRP D 1 63  ? -7.908  23.029  -1.564  1.00 18.21 ? 51  TRP D O   1 
ATOM   4809 C  CB  . TRP D 1 63  ? -10.898 22.150  -2.051  1.00 18.43 ? 51  TRP D CB  1 
ATOM   4810 C  CG  . TRP D 1 63  ? -12.160 21.673  -1.431  1.00 21.30 ? 51  TRP D CG  1 
ATOM   4811 C  CD1 . TRP D 1 63  ? -12.939 20.633  -1.862  1.00 24.76 ? 51  TRP D CD1 1 
ATOM   4812 C  CD2 . TRP D 1 63  ? -12.762 22.167  -0.231  1.00 22.73 ? 51  TRP D CD2 1 
ATOM   4813 N  NE1 . TRP D 1 63  ? -14.019 20.486  -1.033  1.00 27.33 ? 51  TRP D NE1 1 
ATOM   4814 C  CE2 . TRP D 1 63  ? -13.912 21.382  -0.003  1.00 26.03 ? 51  TRP D CE2 1 
ATOM   4815 C  CE3 . TRP D 1 63  ? -12.428 23.168  0.686   1.00 21.94 ? 51  TRP D CE3 1 
ATOM   4816 C  CZ2 . TRP D 1 63  ? -14.746 21.604  1.093   1.00 28.21 ? 51  TRP D CZ2 1 
ATOM   4817 C  CZ3 . TRP D 1 63  ? -13.230 23.358  1.784   1.00 25.45 ? 51  TRP D CZ3 1 
ATOM   4818 C  CH2 . TRP D 1 63  ? -14.397 22.612  1.957   1.00 24.88 ? 51  TRP D CH2 1 
ATOM   4819 N  N   . ASN D 1 64  ? -7.996  21.460  -3.164  1.00 16.28 ? 52  ASN D N   1 
ATOM   4820 C  CA  . ASN D 1 64  ? -6.907  22.038  -3.967  1.00 16.90 ? 52  ASN D CA  1 
ATOM   4821 C  C   . ASN D 1 64  ? -7.226  21.767  -5.429  1.00 18.23 ? 52  ASN D C   1 
ATOM   4822 O  O   . ASN D 1 64  ? -7.400  20.617  -5.831  1.00 17.54 ? 52  ASN D O   1 
ATOM   4823 C  CB  . ASN D 1 64  ? -5.548  21.539  -3.509  1.00 17.84 ? 52  ASN D CB  1 
ATOM   4824 C  CG  . ASN D 1 64  ? -4.426  22.411  -4.025  1.00 20.08 ? 52  ASN D CG  1 
ATOM   4825 O  OD1 . ASN D 1 64  ? -4.630  23.558  -4.451  1.00 18.28 ? 52  ASN D OD1 1 
ATOM   4826 N  ND2 . ASN D 1 64  ? -3.227  21.851  -4.007  1.00 19.99 ? 52  ASN D ND2 1 
ATOM   4827 N  N   . PRO D 1 65  ? -7.449  22.818  -6.230  1.00 16.99 ? 53  PRO D N   1 
ATOM   4828 C  CA  . PRO D 1 65  ? -7.456  24.196  -5.753  1.00 18.11 ? 53  PRO D CA  1 
ATOM   4829 C  C   . PRO D 1 65  ? -8.786  24.580  -5.091  1.00 18.37 ? 53  PRO D C   1 
ATOM   4830 O  O   . PRO D 1 65  ? -9.786  23.910  -5.313  1.00 19.74 ? 53  PRO D O   1 
ATOM   4831 C  CB  . PRO D 1 65  ? -7.209  24.985  -7.050  1.00 18.41 ? 53  PRO D CB  1 
ATOM   4832 C  CG  . PRO D 1 65  ? -7.938  24.187  -8.093  1.00 20.26 ? 53  PRO D CG  1 
ATOM   4833 C  CD  . PRO D 1 65  ? -7.723  22.735  -7.687  1.00 19.37 ? 53  PRO D CD  1 
ATOM   4834 N  N   . GLY D 1 66  ? -8.768  25.654  -4.306  1.00 18.49 ? 54  GLY D N   1 
ATOM   4835 C  CA  . GLY D 1 66  ? -9.985  26.341  -3.870  1.00 21.01 ? 54  GLY D CA  1 
ATOM   4836 C  C   . GLY D 1 66  ? -10.692 26.867  -5.101  1.00 20.19 ? 54  GLY D C   1 
ATOM   4837 O  O   . GLY D 1 66  ? -10.006 27.229  -6.072  1.00 22.32 ? 54  GLY D O   1 
ATOM   4838 N  N   . SER D 1 67  ? -12.013 26.854  -5.122  1.00 24.59 ? 55  SER D N   1 
ATOM   4839 C  CA  . SER D 1 67  ? -12.752 27.434  -6.275  1.00 26.81 ? 55  SER D CA  1 
ATOM   4840 C  C   . SER D 1 67  ? -13.858 28.339  -5.742  1.00 26.71 ? 55  SER D C   1 
ATOM   4841 O  O   . SER D 1 67  ? -14.912 28.474  -6.391  1.00 27.23 ? 55  SER D O   1 
ATOM   4842 C  CB  . SER D 1 67  ? -13.244 26.369  -7.212  1.00 27.11 ? 55  SER D CB  1 
ATOM   4843 O  OG  . SER D 1 67  ? -14.099 25.497  -6.526  1.00 29.38 ? 55  SER D OG  1 
ATOM   4844 N  N   . SER D 1 68  ? -13.576 29.009  -4.629  1.00 22.13 ? 56  SER D N   1 
ATOM   4845 C  CA  . SER D 1 68  ? -14.471 30.054  -4.037  1.00 25.99 ? 56  SER D CA  1 
ATOM   4846 C  C   . SER D 1 68  ? -15.845 29.451  -3.760  1.00 26.29 ? 56  SER D C   1 
ATOM   4847 O  O   . SER D 1 68  ? -16.888 30.181  -3.889  1.00 28.80 ? 56  SER D O   1 
ATOM   4848 C  CB  . SER D 1 68  ? -14.590 31.262  -4.905  1.00 24.03 ? 56  SER D CB  1 
ATOM   4849 O  OG  . SER D 1 68  ? -13.312 31.763  -5.258  1.00 26.74 ? 56  SER D OG  1 
ATOM   4850 N  N   . GLN D 1 69  ? -15.855 28.180  -3.370  1.00 27.09 ? 57  GLN D N   1 
ATOM   4851 C  CA  . GLN D 1 69  ? -17.117 27.439  -3.165  1.00 30.77 ? 57  GLN D CA  1 
ATOM   4852 C  C   . GLN D 1 69  ? -17.703 27.830  -1.808  1.00 25.32 ? 57  GLN D C   1 
ATOM   4853 O  O   . GLN D 1 69  ? -16.991 28.326  -0.908  1.00 23.32 ? 57  GLN D O   1 
ATOM   4854 C  CB  . GLN D 1 69  ? -16.925 25.920  -3.346  1.00 33.25 ? 57  GLN D CB  1 
ATOM   4855 C  CG  . GLN D 1 69  ? -15.915 25.277  -2.404  1.00 32.80 ? 57  GLN D CG  1 
ATOM   4856 C  CD  . GLN D 1 69  ? -14.548 25.072  -3.021  1.00 34.60 ? 57  GLN D CD  1 
ATOM   4857 O  OE1 . GLN D 1 69  ? -13.791 26.018  -3.213  1.00 34.11 ? 57  GLN D OE1 1 
ATOM   4858 N  NE2 . GLN D 1 69  ? -14.197 23.829  -3.323  1.00 34.91 ? 57  GLN D NE2 1 
ATOM   4859 N  N   . THR D 1 70  ? -18.996 27.603  -1.674  1.00 27.59 ? 58  THR D N   1 
ATOM   4860 C  CA  . THR D 1 70  ? -19.739 27.659  -0.400  1.00 24.79 ? 58  THR D CA  1 
ATOM   4861 C  C   . THR D 1 70  ? -19.420 26.381  0.381   1.00 29.09 ? 58  THR D C   1 
ATOM   4862 O  O   . THR D 1 70  ? -19.697 25.275  -0.141  1.00 32.62 ? 58  THR D O   1 
ATOM   4863 C  CB  . THR D 1 70  ? -21.220 27.889  -0.710  1.00 25.68 ? 58  THR D CB  1 
ATOM   4864 O  OG1 . THR D 1 70  ? -21.259 29.044  -1.549  1.00 25.20 ? 58  THR D OG1 1 
ATOM   4865 C  CG2 . THR D 1 70  ? -22.071 28.096  0.521   1.00 25.32 ? 58  THR D CG2 1 
ATOM   4866 N  N   . ILE D 1 71  ? -18.827 26.549  1.564   1.00 26.33 ? 59  ILE D N   1 
ATOM   4867 C  CA  . ILE D 1 71  ? -18.251 25.506  2.463   1.00 27.13 ? 59  ILE D CA  1 
ATOM   4868 C  C   . ILE D 1 71  ? -19.275 25.262  3.567   1.00 24.73 ? 59  ILE D C   1 
ATOM   4869 O  O   . ILE D 1 71  ? -19.771 26.250  4.076   1.00 24.63 ? 59  ILE D O   1 
ATOM   4870 C  CB  . ILE D 1 71  ? -16.926 26.028  3.080   1.00 26.60 ? 59  ILE D CB  1 
ATOM   4871 C  CG1 . ILE D 1 71  ? -15.734 25.857  2.147   1.00 29.68 ? 59  ILE D CG1 1 
ATOM   4872 C  CG2 . ILE D 1 71  ? -16.633 25.435  4.445   1.00 27.59 ? 59  ILE D CG2 1 
ATOM   4873 C  CD1 . ILE D 1 71  ? -16.071 25.336  0.777   1.00 29.12 ? 59  ILE D CD1 1 
ATOM   4874 N  N   . THR D 1 72  ? -19.504 24.019  3.986   1.00 22.08 ? 60  THR D N   1 
ATOM   4875 C  CA  . THR D 1 72  ? -20.125 23.805  5.320   1.00 24.15 ? 60  THR D CA  1 
ATOM   4876 C  C   . THR D 1 72  ? -19.289 22.794  6.096   1.00 24.49 ? 60  THR D C   1 
ATOM   4877 O  O   . THR D 1 72  ? -18.707 21.870  5.508   1.00 24.76 ? 60  THR D O   1 
ATOM   4878 C  CB  . THR D 1 72  ? -21.652 23.665  5.246   1.00 27.98 ? 60  THR D CB  1 
ATOM   4879 O  OG1 . THR D 1 72  ? -22.090 22.487  5.928   1.00 35.29 ? 60  THR D OG1 1 
ATOM   4880 C  CG2 . THR D 1 72  ? -22.190 23.708  3.837   1.00 27.49 ? 60  THR D CG2 1 
ATOM   4881 N  N   . TYR D 1 73  ? -19.142 23.077  7.376   1.00 24.62 ? 61  TYR D N   1 
ATOM   4882 C  CA  . TYR D 1 73  ? -18.312 22.282  8.294   1.00 23.71 ? 61  TYR D CA  1 
ATOM   4883 C  C   . TYR D 1 73  ? -19.072 22.232  9.619   1.00 23.40 ? 61  TYR D C   1 
ATOM   4884 O  O   . TYR D 1 73  ? -19.949 23.064  9.897   1.00 22.55 ? 61  TYR D O   1 
ATOM   4885 C  CB  . TYR D 1 73  ? -16.903 22.864  8.444   1.00 23.05 ? 61  TYR D CB  1 
ATOM   4886 C  CG  . TYR D 1 73  ? -16.897 24.115  9.267   1.00 24.07 ? 61  TYR D CG  1 
ATOM   4887 C  CD1 . TYR D 1 73  ? -17.394 25.289  8.730   1.00 25.36 ? 61  TYR D CD1 1 
ATOM   4888 C  CD2 . TYR D 1 73  ? -16.502 24.106  10.606  1.00 23.41 ? 61  TYR D CD2 1 
ATOM   4889 C  CE1 . TYR D 1 73  ? -17.499 26.435  9.488   1.00 25.99 ? 61  TYR D CE1 1 
ATOM   4890 C  CE2 . TYR D 1 73  ? -16.545 25.268  11.359  1.00 26.07 ? 61  TYR D CE2 1 
ATOM   4891 C  CZ  . TYR D 1 73  ? -17.081 26.418  10.812  1.00 27.27 ? 61  TYR D CZ  1 
ATOM   4892 O  OH  . TYR D 1 73  ? -17.186 27.570  11.539  1.00 31.87 ? 61  TYR D OH  1 
ATOM   4893 N  N   . SER D 1 74  ? -18.712 21.254  10.415  1.00 23.15 ? 62  SER D N   1 
ATOM   4894 C  CA  . SER D 1 74  ? -19.194 21.153  11.812  1.00 24.22 ? 62  SER D CA  1 
ATOM   4895 C  C   . SER D 1 74  ? -18.061 20.590  12.649  1.00 23.43 ? 62  SER D C   1 
ATOM   4896 O  O   . SER D 1 74  ? -17.039 20.203  12.082  1.00 24.88 ? 62  SER D O   1 
ATOM   4897 C  CB  . SER D 1 74  ? -20.434 20.347  11.893  1.00 24.94 ? 62  SER D CB  1 
ATOM   4898 O  OG  . SER D 1 74  ? -20.178 19.046  11.437  1.00 27.05 ? 62  SER D OG  1 
ATOM   4899 N  N   . GLY D 1 75  ? -18.230 20.538  13.957  1.00 22.14 ? 63  GLY D N   1 
ATOM   4900 C  CA  . GLY D 1 75  ? -17.176 19.986  14.818  1.00 24.00 ? 63  GLY D CA  1 
ATOM   4901 C  C   . GLY D 1 75  ? -17.216 20.565  16.208  1.00 21.06 ? 63  GLY D C   1 
ATOM   4902 O  O   . GLY D 1 75  ? -18.203 21.202  16.563  1.00 24.70 ? 63  GLY D O   1 
ATOM   4903 N  N   . GLU D 1 76  ? -16.106 20.396  16.914  1.00 22.02 ? 64  GLU D N   1 
ATOM   4904 C  CA  . GLU D 1 76  ? -15.878 20.812  18.317  1.00 23.76 ? 64  GLU D CA  1 
ATOM   4905 C  C   . GLU D 1 76  ? -14.506 21.484  18.331  1.00 24.14 ? 64  GLU D C   1 
ATOM   4906 O  O   . GLU D 1 76  ? -13.618 21.018  17.607  1.00 24.08 ? 64  GLU D O   1 
ATOM   4907 C  CB  . GLU D 1 76  ? -15.977 19.587  19.232  1.00 29.88 ? 64  GLU D CB  1 
ATOM   4908 C  CG  . GLU D 1 76  ? -17.367 18.953  19.231  1.00 37.75 ? 64  GLU D CG  1 
ATOM   4909 C  CD  . GLU D 1 76  ? -18.183 19.090  20.517  1.00 43.82 ? 64  GLU D CD  1 
ATOM   4910 O  OE1 . GLU D 1 76  ? -17.568 19.275  21.605  1.00 53.18 ? 64  GLU D OE1 1 
ATOM   4911 O  OE2 . GLU D 1 76  ? -19.438 19.002  20.439  1.00 49.69 ? 64  GLU D OE2 1 
ATOM   4912 N  N   . TRP D 1 77  ? -14.394 22.641  18.979  1.00 23.84 ? 65  TRP D N   1 
ATOM   4913 C  CA  . TRP D 1 77  ? -13.106 23.366  19.078  1.00 22.39 ? 65  TRP D CA  1 
ATOM   4914 C  C   . TRP D 1 77  ? -12.949 23.790  20.537  1.00 24.04 ? 65  TRP D C   1 
ATOM   4915 O  O   . TRP D 1 77  ? -13.808 24.540  21.021  1.00 25.57 ? 65  TRP D O   1 
ATOM   4916 C  CB  . TRP D 1 77  ? -13.127 24.507  18.056  1.00 26.01 ? 65  TRP D CB  1 
ATOM   4917 C  CG  . TRP D 1 77  ? -12.059 25.542  18.197  1.00 23.02 ? 65  TRP D CG  1 
ATOM   4918 C  CD1 . TRP D 1 77  ? -10.771 25.470  17.760  1.00 25.04 ? 65  TRP D CD1 1 
ATOM   4919 C  CD2 . TRP D 1 77  ? -12.228 26.858  18.743  1.00 23.32 ? 65  TRP D CD2 1 
ATOM   4920 N  NE1 . TRP D 1 77  ? -10.124 26.649  18.001  1.00 26.87 ? 65  TRP D NE1 1 
ATOM   4921 C  CE2 . TRP D 1 77  ? -10.987 27.514  18.617  1.00 23.63 ? 65  TRP D CE2 1 
ATOM   4922 C  CE3 . TRP D 1 77  ? -13.302 27.538  19.319  1.00 21.80 ? 65  TRP D CE3 1 
ATOM   4923 C  CZ2 . TRP D 1 77  ? -10.797 28.827  19.049  1.00 25.18 ? 65  TRP D CZ2 1 
ATOM   4924 C  CZ3 . TRP D 1 77  ? -13.115 28.830  19.741  1.00 22.49 ? 65  TRP D CZ3 1 
ATOM   4925 C  CH2 . TRP D 1 77  ? -11.869 29.446  19.648  1.00 23.12 ? 65  TRP D CH2 1 
ATOM   4926 N  N   . ASN D 1 78  ? -11.945 23.236  21.225  1.00 22.20 ? 66  ASN D N   1 
ATOM   4927 C  CA  . ASN D 1 78  ? -11.794 23.327  22.700  1.00 24.63 ? 66  ASN D CA  1 
ATOM   4928 C  C   . ASN D 1 78  ? -10.376 23.787  23.004  1.00 21.97 ? 66  ASN D C   1 
ATOM   4929 O  O   . ASN D 1 78  ? -9.533  23.005  23.423  1.00 21.03 ? 66  ASN D O   1 
ATOM   4930 C  CB  . ASN D 1 78  ? -12.116 21.990  23.367  1.00 26.20 ? 66  ASN D CB  1 
ATOM   4931 C  CG  . ASN D 1 78  ? -13.586 21.653  23.277  1.00 30.57 ? 66  ASN D CG  1 
ATOM   4932 O  OD1 . ASN D 1 78  ? -14.439 22.424  23.724  1.00 34.09 ? 66  ASN D OD1 1 
ATOM   4933 N  ND2 . ASN D 1 78  ? -13.882 20.481  22.740  1.00 35.22 ? 66  ASN D ND2 1 
ATOM   4934 N  N   . PRO D 1 79  ? -10.091 25.089  22.783  1.00 22.62 ? 67  PRO D N   1 
ATOM   4935 C  CA  . PRO D 1 79  ? -8.774  25.650  23.054  1.00 23.12 ? 67  PRO D CA  1 
ATOM   4936 C  C   . PRO D 1 79  ? -8.606  25.985  24.537  1.00 24.11 ? 67  PRO D C   1 
ATOM   4937 O  O   . PRO D 1 79  ? -9.584  26.310  25.193  1.00 25.71 ? 67  PRO D O   1 
ATOM   4938 C  CB  . PRO D 1 79  ? -8.774  26.963  22.255  1.00 23.71 ? 67  PRO D CB  1 
ATOM   4939 C  CG  . PRO D 1 79  ? -10.211 27.354  22.202  1.00 23.86 ? 67  PRO D CG  1 
ATOM   4940 C  CD  . PRO D 1 79  ? -11.012 26.059  22.204  1.00 23.76 ? 67  PRO D CD  1 
ATOM   4941 N  N   . ASN D 1 80  ? -7.381  25.863  25.020  1.00 21.37 ? 68  ASN D N   1 
ATOM   4942 C  CA  . ASN D 1 80  ? -6.916  26.523  26.265  1.00 24.84 ? 68  ASN D CA  1 
ATOM   4943 C  C   . ASN D 1 80  ? -5.810  27.520  25.901  1.00 20.34 ? 68  ASN D C   1 
ATOM   4944 O  O   . ASN D 1 80  ? -4.614  27.156  25.967  1.00 21.15 ? 68  ASN D O   1 
ATOM   4945 C  CB  . ASN D 1 80  ? -6.465  25.517  27.311  1.00 25.50 ? 68  ASN D CB  1 
ATOM   4946 C  CG  . ASN D 1 80  ? -6.200  26.219  28.628  1.00 28.26 ? 68  ASN D CG  1 
ATOM   4947 O  OD1 . ASN D 1 80  ? -6.915  27.141  28.979  1.00 35.66 ? 68  ASN D OD1 1 
ATOM   4948 N  ND2 . ASN D 1 80  ? -5.130  25.868  29.315  1.00 36.49 ? 68  ASN D ND2 1 
ATOM   4949 N  N   . GLY D 1 81  ? -6.190  28.740  25.513  1.00 22.51 ? 69  GLY D N   1 
ATOM   4950 C  CA  . GLY D 1 81  ? -5.248  29.790  25.097  1.00 22.64 ? 69  GLY D CA  1 
ATOM   4951 C  C   . GLY D 1 81  ? -5.410  30.104  23.625  1.00 20.14 ? 69  GLY D C   1 
ATOM   4952 O  O   . GLY D 1 81  ? -6.484  29.839  23.050  1.00 20.22 ? 69  GLY D O   1 
ATOM   4953 N  N   . ASN D 1 82  ? -4.368  30.665  23.025  1.00 19.30 ? 70  ASN D N   1 
ATOM   4954 C  CA  . ASN D 1 82  ? -4.426  31.310  21.698  1.00 21.77 ? 70  ASN D CA  1 
ATOM   4955 C  C   . ASN D 1 82  ? -4.719  30.261  20.623  1.00 19.31 ? 70  ASN D C   1 
ATOM   4956 O  O   . ASN D 1 82  ? -3.887  29.371  20.411  1.00 19.93 ? 70  ASN D O   1 
ATOM   4957 C  CB  . ASN D 1 82  ? -3.117  32.046  21.461  1.00 21.98 ? 70  ASN D CB  1 
ATOM   4958 C  CG  . ASN D 1 82  ? -3.045  32.762  20.137  1.00 24.58 ? 70  ASN D CG  1 
ATOM   4959 O  OD1 . ASN D 1 82  ? -4.020  32.826  19.388  1.00 28.49 ? 70  ASN D OD1 1 
ATOM   4960 N  ND2 . ASN D 1 82  ? -1.874  33.299  19.840  1.00 30.16 ? 70  ASN D ND2 1 
ATOM   4961 N  N   . SER D 1 83  ? -5.847  30.391  19.939  1.00 18.13 ? 71  SER D N   1 
ATOM   4962 C  CA  . SER D 1 83  ? -6.227  29.446  18.862  1.00 16.66 ? 71  SER D CA  1 
ATOM   4963 C  C   . SER D 1 83  ? -7.334  30.090  18.055  1.00 16.98 ? 71  SER D C   1 
ATOM   4964 O  O   . SER D 1 83  ? -8.003  31.015  18.583  1.00 15.64 ? 71  SER D O   1 
ATOM   4965 C  CB  . SER D 1 83  ? -6.618  28.107  19.486  1.00 17.42 ? 71  SER D CB  1 
ATOM   4966 O  OG  . SER D 1 83  ? -7.283  27.292  18.566  1.00 17.23 ? 71  SER D OG  1 
ATOM   4967 N  N   . TYR D 1 84  ? -7.445  29.757  16.772  1.00 15.55 ? 72  TYR D N   1 
ATOM   4968 C  CA  . TYR D 1 84  ? -8.582  30.253  15.958  1.00 16.82 ? 72  TYR D CA  1 
ATOM   4969 C  C   . TYR D 1 84  ? -8.973  29.187  14.958  1.00 17.10 ? 72  TYR D C   1 
ATOM   4970 O  O   . TYR D 1 84  ? -8.132  28.309  14.688  1.00 16.43 ? 72  TYR D O   1 
ATOM   4971 C  CB  . TYR D 1 84  ? -8.333  31.629  15.312  1.00 16.92 ? 72  TYR D CB  1 
ATOM   4972 C  CG  . TYR D 1 84  ? -7.045  31.780  14.534  1.00 18.37 ? 72  TYR D CG  1 
ATOM   4973 C  CD1 . TYR D 1 84  ? -5.840  32.052  15.158  1.00 21.94 ? 72  TYR D CD1 1 
ATOM   4974 C  CD2 . TYR D 1 84  ? -7.029  31.599  13.161  1.00 23.04 ? 72  TYR D CD2 1 
ATOM   4975 C  CE1 . TYR D 1 84  ? -4.658  32.193  14.439  1.00 22.27 ? 72  TYR D CE1 1 
ATOM   4976 C  CE2 . TYR D 1 84  ? -5.860  31.742  12.430  1.00 22.69 ? 72  TYR D CE2 1 
ATOM   4977 C  CZ  . TYR D 1 84  ? -4.677  32.056  13.066  1.00 22.06 ? 72  TYR D CZ  1 
ATOM   4978 O  OH  . TYR D 1 84  ? -3.526  32.085  12.318  1.00 29.38 ? 72  TYR D OH  1 
ATOM   4979 N  N   . LEU D 1 85  ? -10.222 29.258  14.511  1.00 17.10 ? 73  LEU D N   1 
ATOM   4980 C  CA  . LEU D 1 85  ? -10.868 28.298  13.590  1.00 19.49 ? 73  LEU D CA  1 
ATOM   4981 C  C   . LEU D 1 85  ? -11.291 29.140  12.394  1.00 17.30 ? 73  LEU D C   1 
ATOM   4982 O  O   . LEU D 1 85  ? -11.887 30.189  12.589  1.00 16.42 ? 73  LEU D O   1 
ATOM   4983 C  CB  . LEU D 1 85  ? -12.028 27.569  14.282  1.00 20.87 ? 73  LEU D CB  1 
ATOM   4984 C  CG  . LEU D 1 85  ? -12.846 26.602  13.434  1.00 22.98 ? 73  LEU D CG  1 
ATOM   4985 C  CD1 . LEU D 1 85  ? -12.062 25.368  13.114  1.00 25.79 ? 73  LEU D CD1 1 
ATOM   4986 C  CD2 . LEU D 1 85  ? -14.155 26.213  14.148  1.00 24.13 ? 73  LEU D CD2 1 
ATOM   4987 N  N   . SER D 1 86  ? -10.832 28.787  11.209  1.00 18.28 ? 74  SER D N   1 
ATOM   4988 C  CA  . SER D 1 86  ? -10.951 29.694  10.055  1.00 17.99 ? 74  SER D CA  1 
ATOM   4989 C  C   . SER D 1 86  ? -11.119 28.890  8.775   1.00 18.81 ? 74  SER D C   1 
ATOM   4990 O  O   . SER D 1 86  ? -10.745 27.683  8.750   1.00 18.73 ? 74  SER D O   1 
ATOM   4991 C  CB  . SER D 1 86  ? -9.716  30.541  9.986   1.00 21.55 ? 74  SER D CB  1 
ATOM   4992 O  OG  . SER D 1 86  ? -8.624  29.763  9.526   1.00 24.95 ? 74  SER D OG  1 
ATOM   4993 N  N   . VAL D 1 87  ? -11.646 29.526  7.752   1.00 16.06 ? 75  VAL D N   1 
ATOM   4994 C  CA  . VAL D 1 87  ? -11.377 29.044  6.371   1.00 15.86 ? 75  VAL D CA  1 
ATOM   4995 C  C   . VAL D 1 87  ? -10.072 29.697  5.956   1.00 15.91 ? 75  VAL D C   1 
ATOM   4996 O  O   . VAL D 1 87  ? -9.947  30.931  6.108   1.00 18.32 ? 75  VAL D O   1 
ATOM   4997 C  CB  . VAL D 1 87  ? -12.532 29.340  5.405   1.00 17.45 ? 75  VAL D CB  1 
ATOM   4998 C  CG1 . VAL D 1 87  ? -12.220 28.844  4.007   1.00 17.94 ? 75  VAL D CG1 1 
ATOM   4999 C  CG2 . VAL D 1 87  ? -13.809 28.724  5.897   1.00 18.22 ? 75  VAL D CG2 1 
ATOM   5000 N  N   . TYR D 1 88  ? -9.152  28.889  5.474   1.00 14.64 ? 76  TYR D N   1 
ATOM   5001 C  CA  . TYR D 1 88  ? -7.746  29.306  5.354   1.00 15.57 ? 76  TYR D CA  1 
ATOM   5002 C  C   . TYR D 1 88  ? -7.236  28.888  3.990   1.00 14.17 ? 76  TYR D C   1 
ATOM   5003 O  O   . TYR D 1 88  ? -7.401  27.721  3.611   1.00 14.34 ? 76  TYR D O   1 
ATOM   5004 C  CB  . TYR D 1 88  ? -6.928  28.686  6.464   1.00 15.56 ? 76  TYR D CB  1 
ATOM   5005 C  CG  . TYR D 1 88  ? -5.439  28.813  6.287   1.00 15.76 ? 76  TYR D CG  1 
ATOM   5006 C  CD1 . TYR D 1 88  ? -4.832  30.050  6.326   1.00 17.56 ? 76  TYR D CD1 1 
ATOM   5007 C  CD2 . TYR D 1 88  ? -4.648  27.701  6.078   1.00 16.72 ? 76  TYR D CD2 1 
ATOM   5008 C  CE1 . TYR D 1 88  ? -3.464  30.180  6.243   1.00 16.94 ? 76  TYR D CE1 1 
ATOM   5009 C  CE2 . TYR D 1 88  ? -3.266  27.819  5.966   1.00 16.64 ? 76  TYR D CE2 1 
ATOM   5010 C  CZ  . TYR D 1 88  ? -2.685  29.067  5.986   1.00 16.50 ? 76  TYR D CZ  1 
ATOM   5011 O  OH  . TYR D 1 88  ? -1.331  29.217  5.928   1.00 18.17 ? 76  TYR D OH  1 
ATOM   5012 N  N   . GLY D 1 89  ? -6.571  29.783  3.299   1.00 13.32 ? 77  GLY D N   1 
ATOM   5013 C  CA  . GLY D 1 89  ? -6.009  29.360  2.001   1.00 13.04 ? 77  GLY D CA  1 
ATOM   5014 C  C   . GLY D 1 89  ? -4.972  30.272  1.419   1.00 13.62 ? 77  GLY D C   1 
ATOM   5015 O  O   . GLY D 1 89  ? -4.622  31.349  2.017   1.00 13.69 ? 77  GLY D O   1 
ATOM   5016 N  N   . TRP D 1 90  ? -4.571  29.928  0.197   1.00 14.25 ? 78  TRP D N   1 
ATOM   5017 C  CA  . TRP D 1 90  ? -3.542  30.738  -0.508  1.00 15.89 ? 78  TRP D CA  1 
ATOM   5018 C  C   . TRP D 1 90  ? -3.977  31.105  -1.906  1.00 16.83 ? 78  TRP D C   1 
ATOM   5019 O  O   . TRP D 1 90  ? -4.636  30.292  -2.500  1.00 14.94 ? 78  TRP D O   1 
ATOM   5020 C  CB  . TRP D 1 90  ? -2.241  29.971  -0.596  1.00 16.49 ? 78  TRP D CB  1 
ATOM   5021 C  CG  . TRP D 1 90  ? -1.597  29.817  0.734   1.00 16.95 ? 78  TRP D CG  1 
ATOM   5022 C  CD1 . TRP D 1 90  ? -1.907  28.898  1.684   1.00 16.10 ? 78  TRP D CD1 1 
ATOM   5023 C  CD2 . TRP D 1 90  ? -0.537  30.632  1.271   1.00 17.93 ? 78  TRP D CD2 1 
ATOM   5024 N  NE1 . TRP D 1 90  ? -1.087  29.046  2.773   1.00 17.52 ? 78  TRP D NE1 1 
ATOM   5025 C  CE2 . TRP D 1 90  ? -0.258  30.128  2.562   1.00 16.80 ? 78  TRP D CE2 1 
ATOM   5026 C  CE3 . TRP D 1 90  ? 0.189   31.738  0.801   1.00 16.22 ? 78  TRP D CE3 1 
ATOM   5027 C  CZ2 . TRP D 1 90  ? 0.773   30.637  3.345   1.00 17.54 ? 78  TRP D CZ2 1 
ATOM   5028 C  CZ3 . TRP D 1 90  ? 1.201   32.242  1.589   1.00 17.19 ? 78  TRP D CZ3 1 
ATOM   5029 C  CH2 . TRP D 1 90  ? 1.436   31.751  2.868   1.00 18.05 ? 78  TRP D CH2 1 
ATOM   5030 N  N   . THR D 1 91  ? -3.516  32.255  -2.409  1.00 15.43 ? 79  THR D N   1 
ATOM   5031 C  CA  . THR D 1 91  ? -3.402  32.457  -3.883  1.00 14.77 ? 79  THR D CA  1 
ATOM   5032 C  C   . THR D 1 91  ? -1.939  32.630  -4.266  1.00 15.19 ? 79  THR D C   1 
ATOM   5033 O  O   . THR D 1 91  ? -1.064  32.847  -3.411  1.00 15.51 ? 79  THR D O   1 
ATOM   5034 C  CB  . THR D 1 91  ? -4.196  33.663  -4.394  1.00 17.39 ? 79  THR D CB  1 
ATOM   5035 O  OG1 . THR D 1 91  ? -3.547  34.872  -4.013  1.00 18.49 ? 79  THR D OG1 1 
ATOM   5036 C  CG2 . THR D 1 91  ? -5.629  33.677  -3.928  1.00 17.04 ? 79  THR D CG2 1 
ATOM   5037 N  N   . GLN D 1 92  ? -1.691  32.485  -5.543  1.00 17.40 ? 80  GLN D N   1 
ATOM   5038 C  CA  . GLN D 1 92  ? -0.331  32.655  -6.133  1.00 16.83 ? 80  GLN D CA  1 
ATOM   5039 C  C   . GLN D 1 92  ? -0.433  33.658  -7.272  1.00 18.51 ? 80  GLN D C   1 
ATOM   5040 O  O   . GLN D 1 92  ? -1.484  33.771  -7.897  1.00 16.42 ? 80  GLN D O   1 
ATOM   5041 C  CB  . GLN D 1 92  ? 0.173   31.336  -6.696  1.00 19.90 ? 80  GLN D CB  1 
ATOM   5042 C  CG  . GLN D 1 92  ? 0.523   30.323  -5.629  1.00 22.12 ? 80  GLN D CG  1 
ATOM   5043 C  CD  . GLN D 1 92  ? 0.467   28.929  -6.200  1.00 24.79 ? 80  GLN D CD  1 
ATOM   5044 O  OE1 . GLN D 1 92  ? -0.543  28.532  -6.788  1.00 24.74 ? 80  GLN D OE1 1 
ATOM   5045 N  NE2 . GLN D 1 92  ? 1.589   28.228  -6.129  1.00 27.85 ? 80  GLN D NE2 1 
ATOM   5046 N  N   . ASN D 1 93  ? 0.626   34.427  -7.428  1.00 18.34 ? 81  ASN D N   1 
ATOM   5047 C  CA  . ASN D 1 93  ? 0.758   35.404  -8.541  1.00 20.24 ? 81  ASN D CA  1 
ATOM   5048 C  C   . ASN D 1 93  ? -0.424  36.374  -8.589  1.00 17.38 ? 81  ASN D C   1 
ATOM   5049 O  O   . ASN D 1 93  ? -1.160  36.417  -9.593  1.00 18.63 ? 81  ASN D O   1 
ATOM   5050 C  CB  . ASN D 1 93  ? 1.007   34.605  -9.820  1.00 18.79 ? 81  ASN D CB  1 
ATOM   5051 C  CG  . ASN D 1 93  ? 1.362   35.528  -10.966 1.00 21.36 ? 81  ASN D CG  1 
ATOM   5052 O  OD1 . ASN D 1 93  ? 1.910   36.597  -10.718 1.00 20.39 ? 81  ASN D OD1 1 
ATOM   5053 N  ND2 . ASN D 1 93  ? 0.931   35.195  -12.170 1.00 23.58 ? 81  ASN D ND2 1 
ATOM   5054 N  N   . PRO D 1 94  ? -0.622  37.268  -7.584  1.00 19.69 ? 82  PRO D N   1 
ATOM   5055 C  CA  . PRO D 1 94  ? 0.257   37.381  -6.404  1.00 20.49 ? 82  PRO D CA  1 
ATOM   5056 C  C   . PRO D 1 94  ? 0.036   36.377  -5.266  1.00 21.85 ? 82  PRO D C   1 
ATOM   5057 O  O   . PRO D 1 94  ? -1.063  35.819  -5.145  1.00 19.94 ? 82  PRO D O   1 
ATOM   5058 C  CB  . PRO D 1 94  ? -0.099  38.763  -5.835  1.00 21.33 ? 82  PRO D CB  1 
ATOM   5059 C  CG  . PRO D 1 94  ? -1.529  38.955  -6.225  1.00 21.15 ? 82  PRO D CG  1 
ATOM   5060 C  CD  . PRO D 1 94  ? -1.633  38.338  -7.605  1.00 19.92 ? 82  PRO D CD  1 
ATOM   5061 N  N   . LEU D 1 95  ? 1.098   36.199  -4.466  1.00 20.04 ? 83  LEU D N   1 
ATOM   5062 C  CA  . LEU D 1 95  ? 1.102   35.306  -3.285  1.00 20.50 ? 83  LEU D CA  1 
ATOM   5063 C  C   . LEU D 1 95  ? 0.307   35.998  -2.188  1.00 18.83 ? 83  LEU D C   1 
ATOM   5064 O  O   . LEU D 1 95  ? 0.665   37.099  -1.750  1.00 16.88 ? 83  LEU D O   1 
ATOM   5065 C  CB  . LEU D 1 95  ? 2.541   35.022  -2.860  1.00 20.28 ? 83  LEU D CB  1 
ATOM   5066 C  CG  . LEU D 1 95  ? 2.717   33.958  -1.784  1.00 19.99 ? 83  LEU D CG  1 
ATOM   5067 C  CD1 . LEU D 1 95  ? 2.151   32.594  -2.186  1.00 18.16 ? 83  LEU D CD1 1 
ATOM   5068 C  CD2 . LEU D 1 95  ? 4.204   33.820  -1.418  1.00 22.42 ? 83  LEU D CD2 1 
ATOM   5069 N  N   . VAL D 1 96  ? -0.772  35.364  -1.750  1.00 18.52 ? 84  VAL D N   1 
ATOM   5070 C  CA  . VAL D 1 96  ? -1.666  35.918  -0.711  1.00 17.93 ? 84  VAL D CA  1 
ATOM   5071 C  C   . VAL D 1 96  ? -1.968  34.776  0.237   1.00 17.27 ? 84  VAL D C   1 
ATOM   5072 O  O   . VAL D 1 96  ? -2.229  33.663  -0.251  1.00 16.08 ? 84  VAL D O   1 
ATOM   5073 C  CB  . VAL D 1 96  ? -2.960  36.465  -1.316  1.00 17.95 ? 84  VAL D CB  1 
ATOM   5074 C  CG1 . VAL D 1 96  ? -3.945  36.850  -0.220  1.00 20.57 ? 84  VAL D CG1 1 
ATOM   5075 C  CG2 . VAL D 1 96  ? -2.662  37.633  -2.259  1.00 19.12 ? 84  VAL D CG2 1 
ATOM   5076 N  N   . GLU D 1 97  ? -1.957  35.069  1.522   1.00 16.88 ? 85  GLU D N   1 
ATOM   5077 C  CA  . GLU D 1 97  ? -2.456  34.155  2.581   1.00 16.96 ? 85  GLU D CA  1 
ATOM   5078 C  C   . GLU D 1 97  ? -3.743  34.792  3.115   1.00 15.48 ? 85  GLU D C   1 
ATOM   5079 O  O   . GLU D 1 97  ? -3.733  36.036  3.397   1.00 16.12 ? 85  GLU D O   1 
ATOM   5080 C  CB  . GLU D 1 97  ? -1.445  34.013  3.713   1.00 16.15 ? 85  GLU D CB  1 
ATOM   5081 C  CG  . GLU D 1 97  ? -1.763  32.847  4.650   1.00 17.82 ? 85  GLU D CG  1 
ATOM   5082 C  CD  . GLU D 1 97  ? -0.839  32.762  5.874   1.00 16.39 ? 85  GLU D CD  1 
ATOM   5083 O  OE1 . GLU D 1 97  ? -0.584  31.631  6.323   1.00 16.52 ? 85  GLU D OE1 1 
ATOM   5084 O  OE2 . GLU D 1 97  ? -0.355  33.838  6.329   1.00 18.36 ? 85  GLU D OE2 1 
ATOM   5085 N  N   . TYR D 1 98  ? -4.811  34.015  3.295   1.00 16.80 ? 86  TYR D N   1 
ATOM   5086 C  CA  . TYR D 1 98  ? -6.093  34.592  3.761   1.00 16.38 ? 86  TYR D CA  1 
ATOM   5087 C  C   . TYR D 1 98  ? -6.744  33.675  4.785   1.00 16.98 ? 86  TYR D C   1 
ATOM   5088 O  O   . TYR D 1 98  ? -6.574  32.469  4.732   1.00 16.39 ? 86  TYR D O   1 
ATOM   5089 C  CB  . TYR D 1 98  ? -7.015  34.919  2.581   1.00 17.36 ? 86  TYR D CB  1 
ATOM   5090 C  CG  . TYR D 1 98  ? -7.526  33.675  1.899   1.00 15.84 ? 86  TYR D CG  1 
ATOM   5091 C  CD1 . TYR D 1 98  ? -8.649  33.018  2.362   1.00 16.43 ? 86  TYR D CD1 1 
ATOM   5092 C  CD2 . TYR D 1 98  ? -6.970  33.244  0.710   1.00 16.83 ? 86  TYR D CD2 1 
ATOM   5093 C  CE1 . TYR D 1 98  ? -9.086  31.846  1.770   1.00 18.76 ? 86  TYR D CE1 1 
ATOM   5094 C  CE2 . TYR D 1 98  ? -7.402  32.085  0.101   1.00 17.42 ? 86  TYR D CE2 1 
ATOM   5095 C  CZ  . TYR D 1 98  ? -8.478  31.389  0.610   1.00 18.54 ? 86  TYR D CZ  1 
ATOM   5096 O  OH  . TYR D 1 98  ? -8.927  30.266  -0.026  1.00 19.27 ? 86  TYR D OH  1 
ATOM   5097 N  N   . TYR D 1 99  ? -7.459  34.322  5.700   1.00 19.40 ? 87  TYR D N   1 
ATOM   5098 C  CA  . TYR D 1 99  ? -8.209  33.711  6.814   1.00 18.04 ? 87  TYR D CA  1 
ATOM   5099 C  C   . TYR D 1 99  ? -9.606  34.312  6.833   1.00 16.70 ? 87  TYR D C   1 
ATOM   5100 O  O   . TYR D 1 99  ? -9.767  35.565  6.838   1.00 17.83 ? 87  TYR D O   1 
ATOM   5101 C  CB  . TYR D 1 99  ? -7.554  34.017  8.151   1.00 19.81 ? 87  TYR D CB  1 
ATOM   5102 C  CG  . TYR D 1 99  ? -6.172  33.468  8.304   1.00 22.81 ? 87  TYR D CG  1 
ATOM   5103 C  CD1 . TYR D 1 99  ? -5.109  34.211  7.826   1.00 25.84 ? 87  TYR D CD1 1 
ATOM   5104 C  CD2 . TYR D 1 99  ? -5.926  32.252  8.919   1.00 26.84 ? 87  TYR D CD2 1 
ATOM   5105 C  CE1 . TYR D 1 99  ? -3.813  33.761  7.962   1.00 31.47 ? 87  TYR D CE1 1 
ATOM   5106 C  CE2 . TYR D 1 99  ? -4.624  31.800  9.084   1.00 31.14 ? 87  TYR D CE2 1 
ATOM   5107 C  CZ  . TYR D 1 99  ? -3.579  32.551  8.575   1.00 28.21 ? 87  TYR D CZ  1 
ATOM   5108 O  OH  . TYR D 1 99  ? -2.278  32.174  8.680   1.00 38.48 ? 87  TYR D OH  1 
ATOM   5109 N  N   . ILE D 1 100 ? -10.590 33.440  6.926   1.00 17.30 ? 88  ILE D N   1 
ATOM   5110 C  CA  . ILE D 1 100 ? -11.982 33.827  7.272   1.00 16.71 ? 88  ILE D CA  1 
ATOM   5111 C  C   . ILE D 1 100 ? -12.218 33.262  8.660   1.00 17.47 ? 88  ILE D C   1 
ATOM   5112 O  O   . ILE D 1 100 ? -12.371 32.034  8.781   1.00 16.90 ? 88  ILE D O   1 
ATOM   5113 C  CB  . ILE D 1 100 ? -12.981 33.346  6.219   1.00 16.52 ? 88  ILE D CB  1 
ATOM   5114 C  CG1 . ILE D 1 100 ? -12.666 33.931  4.843   1.00 17.75 ? 88  ILE D CG1 1 
ATOM   5115 C  CG2 . ILE D 1 100 ? -14.407 33.666  6.669   1.00 16.72 ? 88  ILE D CG2 1 
ATOM   5116 C  CD1 . ILE D 1 100 ? -13.228 33.121  3.718   1.00 16.89 ? 88  ILE D CD1 1 
ATOM   5117 N  N   . VAL D 1 101 ? -12.098 34.117  9.666   1.00 18.43 ? 89  VAL D N   1 
ATOM   5118 C  CA  . VAL D 1 101 ? -11.992 33.632  11.069  1.00 18.44 ? 89  VAL D CA  1 
ATOM   5119 C  C   . VAL D 1 101 ? -13.408 33.492  11.632  1.00 18.83 ? 89  VAL D C   1 
ATOM   5120 O  O   . VAL D 1 101 ? -14.100 34.471  11.682  1.00 17.34 ? 89  VAL D O   1 
ATOM   5121 C  CB  . VAL D 1 101 ? -11.069 34.510  11.912  1.00 17.09 ? 89  VAL D CB  1 
ATOM   5122 C  CG1 . VAL D 1 101 ? -11.056 34.018  13.354  1.00 19.14 ? 89  VAL D CG1 1 
ATOM   5123 C  CG2 . VAL D 1 101 ? -9.663  34.532  11.318  1.00 17.61 ? 89  VAL D CG2 1 
ATOM   5124 N  N   . GLU D 1 102 ? -13.790 32.272  12.020  1.00 17.72 ? 90  GLU D N   1 
ATOM   5125 C  CA  . GLU D 1 102 ? -15.143 31.918  12.540  1.00 18.66 ? 90  GLU D CA  1 
ATOM   5126 C  C   . GLU D 1 102 ? -15.164 32.047  14.072  1.00 19.06 ? 90  GLU D C   1 
ATOM   5127 O  O   . GLU D 1 102 ? -16.226 32.381  14.651  1.00 20.35 ? 90  GLU D O   1 
ATOM   5128 C  CB  . GLU D 1 102 ? -15.461 30.479  12.126  1.00 22.43 ? 90  GLU D CB  1 
ATOM   5129 C  CG  . GLU D 1 102 ? -15.655 30.303  10.634  1.00 23.58 ? 90  GLU D CG  1 
ATOM   5130 C  CD  . GLU D 1 102 ? -16.912 31.003  10.157  1.00 26.88 ? 90  GLU D CD  1 
ATOM   5131 O  OE1 . GLU D 1 102 ? -16.801 32.169  9.762   1.00 25.81 ? 90  GLU D OE1 1 
ATOM   5132 O  OE2 . GLU D 1 102 ? -18.004 30.394  10.219  1.00 28.12 ? 90  GLU D OE2 1 
ATOM   5133 N  N   . SER D 1 103 ? -14.037 31.752  14.709  1.00 19.12 ? 91  SER D N   1 
ATOM   5134 C  CA  . SER D 1 103 ? -13.870 31.765  16.179  1.00 19.37 ? 91  SER D CA  1 
ATOM   5135 C  C   . SER D 1 103 ? -12.415 32.056  16.490  1.00 18.34 ? 91  SER D C   1 
ATOM   5136 O  O   . SER D 1 103 ? -11.518 31.583  15.766  1.00 18.37 ? 91  SER D O   1 
ATOM   5137 C  CB  . SER D 1 103 ? -14.260 30.428  16.830  1.00 21.80 ? 91  SER D CB  1 
ATOM   5138 O  OG  . SER D 1 103 ? -15.662 30.248  16.924  1.00 23.97 ? 91  SER D OG  1 
ATOM   5139 N  N   . PHE D 1 104 ? -12.174 32.797  17.552  1.00 17.35 ? 92  PHE D N   1 
ATOM   5140 C  CA  . PHE D 1 104 ? -10.821 32.882  18.146  1.00 18.16 ? 92  PHE D CA  1 
ATOM   5141 C  C   . PHE D 1 104 ? -10.977 32.975  19.650  1.00 19.61 ? 92  PHE D C   1 
ATOM   5142 O  O   . PHE D 1 104 ? -12.039 33.350  20.143  1.00 20.13 ? 92  PHE D O   1 
ATOM   5143 C  CB  . PHE D 1 104 ? -9.983  34.027  17.577  1.00 18.75 ? 92  PHE D CB  1 
ATOM   5144 C  CG  . PHE D 1 104 ? -10.430 35.425  17.934  1.00 19.20 ? 92  PHE D CG  1 
ATOM   5145 C  CD1 . PHE D 1 104 ? -10.129 36.000  19.163  1.00 19.85 ? 92  PHE D CD1 1 
ATOM   5146 C  CD2 . PHE D 1 104 ? -11.188 36.156  17.035  1.00 17.64 ? 92  PHE D CD2 1 
ATOM   5147 C  CE1 . PHE D 1 104 ? -10.511 37.314  19.451  1.00 18.62 ? 92  PHE D CE1 1 
ATOM   5148 C  CE2 . PHE D 1 104 ? -11.547 37.466  17.327  1.00 18.85 ? 92  PHE D CE2 1 
ATOM   5149 C  CZ  . PHE D 1 104 ? -11.267 38.003  18.563  1.00 18.71 ? 92  PHE D CZ  1 
ATOM   5150 N  N   . SER D 1 105 ? -9.872  32.688  20.313  1.00 19.76 ? 93  SER D N   1 
ATOM   5151 C  CA  . SER D 1 105 ? -9.759  32.560  21.783  1.00 21.87 ? 93  SER D CA  1 
ATOM   5152 C  C   . SER D 1 105 ? -8.484  33.281  22.181  1.00 25.90 ? 93  SER D C   1 
ATOM   5153 O  O   . SER D 1 105 ? -7.431  33.046  21.502  1.00 32.26 ? 93  SER D O   1 
ATOM   5154 C  CB  . SER D 1 105 ? -9.614  31.155  22.167  1.00 23.97 ? 93  SER D CB  1 
ATOM   5155 O  OG  . SER D 1 105 ? -8.283  30.781  21.816  1.00 31.24 ? 93  SER D OG  1 
ATOM   5156 N  N   . THR D 1 106 ? -8.620  34.185  23.143  1.00 27.52 ? 94  THR D N   1 
ATOM   5157 C  CA  . THR D 1 106 ? -7.573  34.879  23.952  1.00 25.47 ? 94  THR D CA  1 
ATOM   5158 C  C   . THR D 1 106 ? -6.785  35.942  23.170  1.00 25.29 ? 94  THR D C   1 
ATOM   5159 O  O   . THR D 1 106 ? -6.321  36.897  23.842  1.00 28.39 ? 94  THR D O   1 
ATOM   5160 C  CB  . THR D 1 106 ? -6.676  33.919  24.748  1.00 27.35 ? 94  THR D CB  1 
ATOM   5161 O  OG1 . THR D 1 106 ? -5.609  33.314  24.016  1.00 31.80 ? 94  THR D OG1 1 
ATOM   5162 C  CG2 . THR D 1 106 ? -7.516  32.865  25.429  1.00 27.64 ? 94  THR D CG2 1 
ATOM   5163 N  N   . TYR D 1 107 ? -6.587  35.786  21.859  1.00 20.08 ? 95  TYR D N   1 
ATOM   5164 C  CA  . TYR D 1 107 ? -5.825  36.751  21.038  1.00 19.95 ? 95  TYR D CA  1 
ATOM   5165 C  C   . TYR D 1 107 ? -6.506  36.920  19.680  1.00 19.07 ? 95  TYR D C   1 
ATOM   5166 O  O   . TYR D 1 107 ? -6.640  35.956  18.950  1.00 18.63 ? 95  TYR D O   1 
ATOM   5167 C  CB  . TYR D 1 107 ? -4.372  36.316  20.908  1.00 19.72 ? 95  TYR D CB  1 
ATOM   5168 C  CG  . TYR D 1 107 ? -3.497  37.313  20.192  1.00 20.45 ? 95  TYR D CG  1 
ATOM   5169 C  CD1 . TYR D 1 107 ? -3.068  38.472  20.815  1.00 22.31 ? 95  TYR D CD1 1 
ATOM   5170 C  CD2 . TYR D 1 107 ? -3.091  37.105  18.883  1.00 22.14 ? 95  TYR D CD2 1 
ATOM   5171 C  CE1 . TYR D 1 107 ? -2.224  39.384  20.175  1.00 22.26 ? 95  TYR D CE1 1 
ATOM   5172 C  CE2 . TYR D 1 107 ? -2.269  38.003  18.222  1.00 20.85 ? 95  TYR D CE2 1 
ATOM   5173 C  CZ  . TYR D 1 107 ? -1.837  39.155  18.867  1.00 22.33 ? 95  TYR D CZ  1 
ATOM   5174 O  OH  . TYR D 1 107 ? -1.019  40.027  18.192  1.00 23.91 ? 95  TYR D OH  1 
ATOM   5175 N  N   . ASP D 1 108 ? -6.911  38.152  19.374  1.00 20.61 ? 96  ASP D N   1 
ATOM   5176 C  CA  . ASP D 1 108 ? -7.496  38.499  18.056  1.00 20.60 ? 96  ASP D CA  1 
ATOM   5177 C  C   . ASP D 1 108 ? -6.370  38.409  17.023  1.00 20.89 ? 96  ASP D C   1 
ATOM   5178 O  O   . ASP D 1 108 ? -5.448  39.219  17.035  1.00 21.14 ? 96  ASP D O   1 
ATOM   5179 C  CB  . ASP D 1 108 ? -8.180  39.869  18.084  1.00 20.59 ? 96  ASP D CB  1 
ATOM   5180 C  CG  . ASP D 1 108 ? -8.882  40.180  16.771  1.00 23.65 ? 96  ASP D CG  1 
ATOM   5181 O  OD1 . ASP D 1 108 ? -8.527  39.531  15.753  1.00 26.43 ? 96  ASP D OD1 1 
ATOM   5182 O  OD2 . ASP D 1 108 ? -9.773  41.065  16.756  1.00 23.96 ? 96  ASP D OD2 1 
ATOM   5183 N  N   . PRO D 1 109 ? -6.382  37.403  16.120  1.00 20.02 ? 97  PRO D N   1 
ATOM   5184 C  CA  . PRO D 1 109 ? -5.266  37.204  15.195  1.00 22.00 ? 97  PRO D CA  1 
ATOM   5185 C  C   . PRO D 1 109 ? -5.134  38.300  14.126  1.00 21.59 ? 97  PRO D C   1 
ATOM   5186 O  O   . PRO D 1 109 ? -4.120  38.326  13.418  1.00 21.53 ? 97  PRO D O   1 
ATOM   5187 C  CB  . PRO D 1 109 ? -5.601  35.842  14.568  1.00 21.55 ? 97  PRO D CB  1 
ATOM   5188 C  CG  . PRO D 1 109 ? -7.095  35.792  14.558  1.00 21.62 ? 97  PRO D CG  1 
ATOM   5189 C  CD  . PRO D 1 109 ? -7.476  36.448  15.878  1.00 22.40 ? 97  PRO D CD  1 
ATOM   5190 N  N   . SER D 1 110 ? -6.118  39.196  14.035  1.00 24.39 ? 98  SER D N   1 
ATOM   5191 C  CA  . SER D 1 110 ? -6.064  40.389  13.146  1.00 23.78 ? 98  SER D CA  1 
ATOM   5192 C  C   . SER D 1 110 ? -5.304  41.538  13.827  1.00 25.81 ? 98  SER D C   1 
ATOM   5193 O  O   . SER D 1 110 ? -4.957  42.521  13.105  1.00 24.58 ? 98  SER D O   1 
ATOM   5194 C  CB  . SER D 1 110 ? -7.435  40.807  12.718  1.00 22.89 ? 98  SER D CB  1 
ATOM   5195 O  OG  . SER D 1 110 ? -8.127  41.360  13.810  1.00 22.58 ? 98  SER D OG  1 
ATOM   5196 N  N   . THR D 1 111 ? -4.964  41.417  15.123  1.00 22.53 ? 99  THR D N   1 
ATOM   5197 C  CA  . THR D 1 111 ? -4.146  42.422  15.845  1.00 23.61 ? 99  THR D CA  1 
ATOM   5198 C  C   . THR D 1 111 ? -2.930  42.841  14.991  1.00 23.79 ? 99  THR D C   1 
ATOM   5199 O  O   . THR D 1 111 ? -2.122  41.951  14.594  1.00 23.44 ? 99  THR D O   1 
ATOM   5200 C  CB  . THR D 1 111 ? -3.721  41.923  17.235  1.00 23.45 ? 99  THR D CB  1 
ATOM   5201 O  OG1 . THR D 1 111 ? -4.921  41.583  17.937  1.00 22.02 ? 99  THR D OG1 1 
ATOM   5202 C  CG2 . THR D 1 111 ? -2.943  42.970  18.000  1.00 26.39 ? 99  THR D CG2 1 
ATOM   5203 N  N   . GLY D 1 112 ? -2.793  44.156  14.757  1.00 23.68 ? 100 GLY D N   1 
ATOM   5204 C  CA  . GLY D 1 112 ? -1.645  44.723  14.028  1.00 24.50 ? 100 GLY D CA  1 
ATOM   5205 C  C   . GLY D 1 112 ? -1.897  44.759  12.541  1.00 24.95 ? 100 GLY D C   1 
ATOM   5206 O  O   . GLY D 1 112 ? -0.984  45.155  11.803  1.00 30.35 ? 100 GLY D O   1 
ATOM   5207 N  N   . ALA D 1 113 ? -3.106  44.427  12.096  1.00 22.64 ? 101 ALA D N   1 
ATOM   5208 C  CA  . ALA D 1 113 ? -3.507  44.567  10.676  1.00 21.03 ? 101 ALA D CA  1 
ATOM   5209 C  C   . ALA D 1 113 ? -4.406  45.798  10.516  1.00 21.31 ? 101 ALA D C   1 
ATOM   5210 O  O   . ALA D 1 113 ? -5.074  46.200  11.481  1.00 22.85 ? 101 ALA D O   1 
ATOM   5211 C  CB  . ALA D 1 113 ? -4.185  43.307  10.204  1.00 22.86 ? 101 ALA D CB  1 
ATOM   5212 N  N   . GLN D 1 114 ? -4.486  46.328  9.312   1.00 21.57 ? 102 GLN D N   1 
ATOM   5213 C  CA  . GLN D 1 114 ? -5.282  47.555  9.047   1.00 24.05 ? 102 GLN D CA  1 
ATOM   5214 C  C   . GLN D 1 114 ? -6.734  47.165  8.789   1.00 23.08 ? 102 GLN D C   1 
ATOM   5215 O  O   . GLN D 1 114 ? -6.988  46.359  7.881   1.00 23.21 ? 102 GLN D O   1 
ATOM   5216 C  CB  . GLN D 1 114 ? -4.748  48.348  7.861   1.00 26.09 ? 102 GLN D CB  1 
ATOM   5217 C  CG  . GLN D 1 114 ? -5.437  49.710  7.746   1.00 26.51 ? 102 GLN D CG  1 
ATOM   5218 C  CD  . GLN D 1 114 ? -5.215  50.354  6.397   1.00 31.12 ? 102 GLN D CD  1 
ATOM   5219 O  OE1 . GLN D 1 114 ? -4.416  49.900  5.576   1.00 33.49 ? 102 GLN D OE1 1 
ATOM   5220 N  NE2 . GLN D 1 114 ? -5.907  51.461  6.174   1.00 30.97 ? 102 GLN D NE2 1 
ATOM   5221 N  N   . GLU D 1 115 ? -7.642  47.709  9.603   1.00 20.39 ? 103 GLU D N   1 
ATOM   5222 C  CA  . GLU D 1 115 ? -9.101  47.542  9.458   1.00 22.47 ? 103 GLU D CA  1 
ATOM   5223 C  C   . GLU D 1 115 ? -9.556  48.333  8.218   1.00 23.35 ? 103 GLU D C   1 
ATOM   5224 O  O   . GLU D 1 115 ? -9.270  49.595  8.129   1.00 23.56 ? 103 GLU D O   1 
ATOM   5225 C  CB  . GLU D 1 115 ? -9.749  47.881  10.802  1.00 21.72 ? 103 GLU D CB  1 
ATOM   5226 C  CG  . GLU D 1 115 ? -11.203 47.500  10.908  1.00 25.30 ? 103 GLU D CG  1 
ATOM   5227 C  CD  . GLU D 1 115 ? -11.826 47.602  12.303  1.00 26.25 ? 103 GLU D CD  1 
ATOM   5228 O  OE1 . GLU D 1 115 ? -13.076 47.527  12.395  1.00 31.77 ? 103 GLU D OE1 1 
ATOM   5229 O  OE2 . GLU D 1 115 ? -11.069 47.718  13.300  1.00 37.06 ? 103 GLU D OE2 1 
ATOM   5230 N  N   . LEU D 1 116 ? -10.291 47.673  7.311   1.00 23.97 ? 104 LEU D N   1 
ATOM   5231 C  CA  . LEU D 1 116 ? -10.692 48.266  6.002   1.00 26.26 ? 104 LEU D CA  1 
ATOM   5232 C  C   . LEU D 1 116 ? -12.201 48.487  5.919   1.00 31.12 ? 104 LEU D C   1 
ATOM   5233 O  O   . LEU D 1 116 ? -12.590 49.419  5.201   1.00 32.94 ? 104 LEU D O   1 
ATOM   5234 C  CB  . LEU D 1 116 ? -10.231 47.358  4.863   1.00 27.59 ? 104 LEU D CB  1 
ATOM   5235 C  CG  . LEU D 1 116 ? -8.718  47.177  4.731   1.00 30.34 ? 104 LEU D CG  1 
ATOM   5236 C  CD1 . LEU D 1 116 ? -8.429  46.341  3.501   1.00 30.36 ? 104 LEU D CD1 1 
ATOM   5237 C  CD2 . LEU D 1 116 ? -7.995  48.513  4.634   1.00 32.65 ? 104 LEU D CD2 1 
ATOM   5238 N  N   . GLY D 1 117 ? -12.996 47.700  6.647   1.00 29.11 ? 105 GLY D N   1 
ATOM   5239 C  CA  . GLY D 1 117 ? -14.471 47.742  6.618   1.00 28.25 ? 105 GLY D CA  1 
ATOM   5240 C  C   . GLY D 1 117 ? -15.059 46.401  7.021   1.00 28.59 ? 105 GLY D C   1 
ATOM   5241 O  O   . GLY D 1 117 ? -14.403 45.678  7.800   1.00 25.59 ? 105 GLY D O   1 
ATOM   5242 N  N   . THR D 1 118 ? -16.276 46.100  6.571   1.00 25.39 ? 106 THR D N   1 
ATOM   5243 C  CA  . THR D 1 118 ? -17.018 44.904  7.038   1.00 28.34 ? 106 THR D CA  1 
ATOM   5244 C  C   . THR D 1 118 ? -17.722 44.228  5.863   1.00 29.48 ? 106 THR D C   1 
ATOM   5245 O  O   . THR D 1 118 ? -17.959 44.863  4.819   1.00 30.11 ? 106 THR D O   1 
ATOM   5246 C  CB  . THR D 1 118 ? -18.100 45.184  8.094   1.00 30.16 ? 106 THR D CB  1 
ATOM   5247 O  OG1 . THR D 1 118 ? -19.140 45.888  7.407   1.00 33.56 ? 106 THR D OG1 1 
ATOM   5248 C  CG2 . THR D 1 118 ? -17.597 45.903  9.318   1.00 31.49 ? 106 THR D CG2 1 
ATOM   5249 N  N   . VAL D 1 119 ? -18.114 42.984  6.085   1.00 28.35 ? 107 VAL D N   1 
ATOM   5250 C  CA  . VAL D 1 119 ? -18.984 42.232  5.151   1.00 28.04 ? 107 VAL D CA  1 
ATOM   5251 C  C   . VAL D 1 119 ? -20.013 41.480  5.987   1.00 27.84 ? 107 VAL D C   1 
ATOM   5252 O  O   . VAL D 1 119 ? -19.685 41.023  7.121   1.00 25.43 ? 107 VAL D O   1 
ATOM   5253 C  CB  . VAL D 1 119 ? -18.167 41.311  4.230   1.00 25.45 ? 107 VAL D CB  1 
ATOM   5254 C  CG1 . VAL D 1 119 ? -17.385 40.288  5.022   1.00 24.96 ? 107 VAL D CG1 1 
ATOM   5255 C  CG2 . VAL D 1 119 ? -19.022 40.660  3.162   1.00 25.80 ? 107 VAL D CG2 1 
ATOM   5256 N  N   . GLU D 1 120 ? -21.247 41.492  5.487   1.00 28.42 ? 108 GLU D N   1 
ATOM   5257 C  CA  . GLU D 1 120 ? -22.389 40.766  6.075   1.00 31.92 ? 108 GLU D CA  1 
ATOM   5258 C  C   . GLU D 1 120 ? -22.553 39.498  5.242   1.00 28.27 ? 108 GLU D C   1 
ATOM   5259 O  O   . GLU D 1 120 ? -22.840 39.618  4.038   1.00 27.59 ? 108 GLU D O   1 
ATOM   5260 C  CB  . GLU D 1 120 ? -23.643 41.644  6.046   1.00 33.78 ? 108 GLU D CB  1 
ATOM   5261 C  CG  . GLU D 1 120 ? -23.562 42.861  6.943   1.00 38.75 ? 108 GLU D CG  1 
ATOM   5262 C  CD  . GLU D 1 120 ? -23.778 42.562  8.417   1.00 44.19 ? 108 GLU D CD  1 
ATOM   5263 O  OE1 . GLU D 1 120 ? -22.809 42.690  9.187   1.00 44.39 ? 108 GLU D OE1 1 
ATOM   5264 O  OE2 . GLU D 1 120 ? -24.921 42.217  8.799   1.00 55.45 ? 108 GLU D OE2 1 
ATOM   5265 N  N   . THR D 1 121 ? -22.353 38.333  5.837   1.00 26.73 ? 109 THR D N   1 
ATOM   5266 C  CA  . THR D 1 121 ? -22.512 37.048  5.113   1.00 26.47 ? 109 THR D CA  1 
ATOM   5267 C  C   . THR D 1 121 ? -22.773 35.937  6.134   1.00 26.39 ? 109 THR D C   1 
ATOM   5268 O  O   . THR D 1 121 ? -22.295 36.035  7.283   1.00 24.32 ? 109 THR D O   1 
ATOM   5269 C  CB  . THR D 1 121 ? -21.357 36.865  4.113   1.00 26.14 ? 109 THR D CB  1 
ATOM   5270 O  OG1 . THR D 1 121 ? -21.610 35.639  3.425   1.00 29.12 ? 109 THR D OG1 1 
ATOM   5271 C  CG2 . THR D 1 121 ? -19.977 36.874  4.734   1.00 25.19 ? 109 THR D CG2 1 
ATOM   5272 N  N   . ASP D 1 122 ? -23.571 34.949  5.742   1.00 26.22 ? 110 ASP D N   1 
ATOM   5273 C  CA  . ASP D 1 122 ? -23.830 33.731  6.549   1.00 27.38 ? 110 ASP D CA  1 
ATOM   5274 C  C   . ASP D 1 122 ? -24.292 34.139  7.959   1.00 28.08 ? 110 ASP D C   1 
ATOM   5275 O  O   . ASP D 1 122 ? -23.753 33.627  8.944   1.00 26.06 ? 110 ASP D O   1 
ATOM   5276 C  CB  . ASP D 1 122 ? -22.590 32.830  6.493   1.00 27.18 ? 110 ASP D CB  1 
ATOM   5277 C  CG  . ASP D 1 122 ? -22.150 32.573  5.057   1.00 28.33 ? 110 ASP D CG  1 
ATOM   5278 O  OD1 . ASP D 1 122 ? -22.946 31.895  4.291   1.00 24.92 ? 110 ASP D OD1 1 
ATOM   5279 O  OD2 . ASP D 1 122 ? -21.056 33.091  4.674   1.00 26.98 ? 110 ASP D OD2 1 
ATOM   5280 N  N   . ASP D 1 123 ? -25.245 35.074  8.037   1.00 33.86 ? 111 ASP D N   1 
ATOM   5281 C  CA  . ASP D 1 123 ? -25.928 35.494  9.297   1.00 33.70 ? 111 ASP D CA  1 
ATOM   5282 C  C   . ASP D 1 123 ? -24.938 36.077  10.306  1.00 31.93 ? 111 ASP D C   1 
ATOM   5283 O  O   . ASP D 1 123 ? -25.206 35.993  11.534  1.00 32.75 ? 111 ASP D O   1 
ATOM   5284 C  CB  . ASP D 1 123 ? -26.694 34.319  9.894   1.00 34.70 ? 111 ASP D CB  1 
ATOM   5285 C  CG  . ASP D 1 123 ? -27.715 33.775  8.915   1.00 42.52 ? 111 ASP D CG  1 
ATOM   5286 O  OD1 . ASP D 1 123 ? -28.394 34.605  8.274   1.00 43.24 ? 111 ASP D OD1 1 
ATOM   5287 O  OD2 . ASP D 1 123 ? -27.801 32.525  8.784   1.00 48.32 ? 111 ASP D OD2 1 
ATOM   5288 N  N   . GLY D 1 124 ? -23.859 36.676  9.808   1.00 27.81 ? 112 GLY D N   1 
ATOM   5289 C  CA  . GLY D 1 124 ? -22.796 37.259  10.633  1.00 26.79 ? 112 GLY D CA  1 
ATOM   5290 C  C   . GLY D 1 124 ? -22.291 38.554  10.023  1.00 26.74 ? 112 GLY D C   1 
ATOM   5291 O  O   . GLY D 1 124 ? -22.627 38.851  8.872   1.00 28.59 ? 112 GLY D O   1 
ATOM   5292 N  N   . THR D 1 125 ? -21.519 39.287  10.802  1.00 27.68 ? 113 THR D N   1 
ATOM   5293 C  CA  . THR D 1 125 ? -20.759 40.476  10.379  1.00 29.22 ? 113 THR D CA  1 
ATOM   5294 C  C   . THR D 1 125 ? -19.288 40.113  10.538  1.00 27.46 ? 113 THR D C   1 
ATOM   5295 O  O   . THR D 1 125 ? -18.931 39.557  11.599  1.00 27.69 ? 113 THR D O   1 
ATOM   5296 C  CB  . THR D 1 125 ? -21.146 41.696  11.217  1.00 33.03 ? 113 THR D CB  1 
ATOM   5297 O  OG1 . THR D 1 125 ? -22.564 41.815  11.088  1.00 37.06 ? 113 THR D OG1 1 
ATOM   5298 C  CG2 . THR D 1 125 ? -20.445 42.957  10.765  1.00 32.52 ? 113 THR D CG2 1 
ATOM   5299 N  N   . TYR D 1 126 ? -18.498 40.356  9.502   1.00 25.01 ? 114 TYR D N   1 
ATOM   5300 C  CA  . TYR D 1 126 ? -17.030 40.138  9.541   1.00 24.87 ? 114 TYR D CA  1 
ATOM   5301 C  C   . TYR D 1 126 ? -16.327 41.475  9.360   1.00 22.26 ? 114 TYR D C   1 
ATOM   5302 O  O   . TYR D 1 126 ? -16.673 42.242  8.437   1.00 24.48 ? 114 TYR D O   1 
ATOM   5303 C  CB  . TYR D 1 126 ? -16.583 39.168  8.449   1.00 23.25 ? 114 TYR D CB  1 
ATOM   5304 C  CG  . TYR D 1 126 ? -17.132 37.777  8.604   1.00 22.01 ? 114 TYR D CG  1 
ATOM   5305 C  CD1 . TYR D 1 126 ? -18.460 37.477  8.309   1.00 20.88 ? 114 TYR D CD1 1 
ATOM   5306 C  CD2 . TYR D 1 126 ? -16.314 36.739  9.014   1.00 21.00 ? 114 TYR D CD2 1 
ATOM   5307 C  CE1 . TYR D 1 126 ? -18.956 36.186  8.440   1.00 19.22 ? 114 TYR D CE1 1 
ATOM   5308 C  CE2 . TYR D 1 126 ? -16.795 35.455  9.146   1.00 20.10 ? 114 TYR D CE2 1 
ATOM   5309 C  CZ  . TYR D 1 126 ? -18.123 35.174  8.854   1.00 18.47 ? 114 TYR D CZ  1 
ATOM   5310 O  OH  . TYR D 1 126 ? -18.586 33.895  9.009   1.00 19.08 ? 114 TYR D OH  1 
ATOM   5311 N  N   . LYS D 1 127 ? -15.312 41.733  10.171  1.00 20.54 ? 115 LYS D N   1 
ATOM   5312 C  CA  . LYS D 1 127 ? -14.421 42.891  9.932   1.00 21.61 ? 115 LYS D CA  1 
ATOM   5313 C  C   . LYS D 1 127 ? -13.297 42.413  9.014   1.00 21.48 ? 115 LYS D C   1 
ATOM   5314 O  O   . LYS D 1 127 ? -12.800 41.306  9.252   1.00 19.76 ? 115 LYS D O   1 
ATOM   5315 C  CB  . LYS D 1 127 ? -13.909 43.445  11.255  1.00 24.66 ? 115 LYS D CB  1 
ATOM   5316 C  CG  . LYS D 1 127 ? -15.014 44.018  12.122  1.00 25.74 ? 115 LYS D CG  1 
ATOM   5317 C  CD  . LYS D 1 127 ? -14.491 44.540  13.426  1.00 28.27 ? 115 LYS D CD  1 
ATOM   5318 C  CE  . LYS D 1 127 ? -15.601 44.985  14.351  1.00 31.85 ? 115 LYS D CE  1 
ATOM   5319 N  NZ  . LYS D 1 127 ? -15.033 45.399  15.649  1.00 30.90 ? 115 LYS D NZ  1 
ATOM   5320 N  N   . ILE D 1 128 ? -12.965 43.222  8.005   1.00 23.17 ? 116 ILE D N   1 
ATOM   5321 C  CA  . ILE D 1 128 ? -11.938 42.913  6.968   1.00 23.26 ? 116 ILE D CA  1 
ATOM   5322 C  C   . ILE D 1 128 ? -10.663 43.626  7.362   1.00 21.01 ? 116 ILE D C   1 
ATOM   5323 O  O   . ILE D 1 128 ? -10.746 44.823  7.701   1.00 20.65 ? 116 ILE D O   1 
ATOM   5324 C  CB  . ILE D 1 128 ? -12.408 43.375  5.578   1.00 25.48 ? 116 ILE D CB  1 
ATOM   5325 C  CG1 . ILE D 1 128 ? -13.679 42.644  5.160   1.00 31.32 ? 116 ILE D CG1 1 
ATOM   5326 C  CG2 . ILE D 1 128 ? -11.300 43.247  4.542   1.00 29.66 ? 116 ILE D CG2 1 
ATOM   5327 C  CD1 . ILE D 1 128 ? -14.389 43.334  3.998   1.00 33.46 ? 116 ILE D CD1 1 
ATOM   5328 N  N   . TYR D 1 129 ? -9.520  42.983  7.205   1.00 21.18 ? 117 TYR D N   1 
ATOM   5329 C  CA  . TYR D 1 129 ? -8.211  43.606  7.486   1.00 21.13 ? 117 TYR D CA  1 
ATOM   5330 C  C   . TYR D 1 129 ? -7.197  43.176  6.434   1.00 21.37 ? 117 TYR D C   1 
ATOM   5331 O  O   . TYR D 1 129 ? -7.331  42.108  5.830   1.00 20.70 ? 117 TYR D O   1 
ATOM   5332 C  CB  . TYR D 1 129 ? -7.633  43.182  8.836   1.00 22.68 ? 117 TYR D CB  1 
ATOM   5333 C  CG  . TYR D 1 129 ? -8.535  43.347  10.032  1.00 23.59 ? 117 TYR D CG  1 
ATOM   5334 C  CD1 . TYR D 1 129 ? -9.568  42.452  10.265  1.00 23.69 ? 117 TYR D CD1 1 
ATOM   5335 C  CD2 . TYR D 1 129 ? -8.340  44.378  10.945  1.00 24.59 ? 117 TYR D CD2 1 
ATOM   5336 C  CE1 . TYR D 1 129 ? -10.404 42.589  11.359  1.00 21.80 ? 117 TYR D CE1 1 
ATOM   5337 C  CE2 . TYR D 1 129 ? -9.155  44.513  12.058  1.00 24.05 ? 117 TYR D CE2 1 
ATOM   5338 C  CZ  . TYR D 1 129 ? -10.173 43.606  12.272  1.00 23.16 ? 117 TYR D CZ  1 
ATOM   5339 O  OH  . TYR D 1 129 ? -10.955 43.767  13.375  1.00 22.56 ? 117 TYR D OH  1 
ATOM   5340 N  N   . GLN D 1 130 ? -6.143  43.965  6.309   1.00 21.06 ? 118 GLN D N   1 
ATOM   5341 C  CA  . GLN D 1 130 ? -4.987  43.622  5.455   1.00 23.57 ? 118 GLN D CA  1 
ATOM   5342 C  C   . GLN D 1 130 ? -3.707  43.886  6.240   1.00 23.61 ? 118 GLN D C   1 
ATOM   5343 O  O   . GLN D 1 130 ? -3.633  44.837  7.021   1.00 23.59 ? 118 GLN D O   1 
ATOM   5344 C  CB  . GLN D 1 130 ? -5.068  44.330  4.103   1.00 25.80 ? 118 GLN D CB  1 
ATOM   5345 C  CG  . GLN D 1 130 ? -4.769  45.830  4.159   1.00 31.57 ? 118 GLN D CG  1 
ATOM   5346 C  CD  . GLN D 1 130 ? -3.440  46.162  3.528   1.00 35.50 ? 118 GLN D CD  1 
ATOM   5347 O  OE1 . GLN D 1 130 ? -3.256  46.028  2.314   1.00 43.26 ? 118 GLN D OE1 1 
ATOM   5348 N  NE2 . GLN D 1 130 ? -2.497  46.584  4.350   1.00 38.41 ? 118 GLN D NE2 1 
ATOM   5349 N  N   . THR D 1 131 ? -2.715  43.032  6.033   1.00 22.41 ? 119 THR D N   1 
ATOM   5350 C  CA  . THR D 1 131 ? -1.345  43.210  6.548   1.00 21.96 ? 119 THR D CA  1 
ATOM   5351 C  C   . THR D 1 131 ? -0.380  42.501  5.601   1.00 20.14 ? 119 THR D C   1 
ATOM   5352 O  O   . THR D 1 131 ? -0.814  42.052  4.541   1.00 21.17 ? 119 THR D O   1 
ATOM   5353 C  CB  . THR D 1 131 ? -1.233  42.769  8.010   1.00 20.05 ? 119 THR D CB  1 
ATOM   5354 O  OG1 . THR D 1 131 ? 0.031   43.193  8.511   1.00 23.00 ? 119 THR D OG1 1 
ATOM   5355 C  CG2 . THR D 1 131 ? -1.358  41.267  8.187   1.00 18.86 ? 119 THR D CG2 1 
ATOM   5356 N  N   . THR D 1 132 ? 0.894   42.503  5.949   1.00 22.26 ? 120 THR D N   1 
ATOM   5357 C  CA  . THR D 1 132 ? 1.991   41.881  5.162   1.00 26.57 ? 120 THR D CA  1 
ATOM   5358 C  C   . THR D 1 132 ? 2.777   40.985  6.101   1.00 25.40 ? 120 THR D C   1 
ATOM   5359 O  O   . THR D 1 132 ? 2.749   41.265  7.322   1.00 28.70 ? 120 THR D O   1 
ATOM   5360 C  CB  . THR D 1 132 ? 2.863   42.927  4.463   1.00 31.66 ? 120 THR D CB  1 
ATOM   5361 O  OG1 . THR D 1 132 ? 2.051   43.518  3.450   1.00 37.88 ? 120 THR D OG1 1 
ATOM   5362 C  CG2 . THR D 1 132 ? 4.097   42.350  3.796   1.00 35.43 ? 120 THR D CG2 1 
ATOM   5363 N  N   . ARG D 1 133 ? 3.307   39.880  5.564   1.00 23.30 ? 121 ARG D N   1 
ATOM   5364 C  CA  . ARG D 1 133 ? 4.242   38.949  6.235   1.00 22.02 ? 121 ARG D CA  1 
ATOM   5365 C  C   . ARG D 1 133 ? 5.548   39.024  5.444   1.00 23.97 ? 121 ARG D C   1 
ATOM   5366 O  O   . ARG D 1 133 ? 5.492   38.895  4.193   1.00 23.24 ? 121 ARG D O   1 
ATOM   5367 C  CB  . ARG D 1 133 ? 3.692   37.507  6.273   1.00 22.07 ? 121 ARG D CB  1 
ATOM   5368 C  CG  . ARG D 1 133 ? 2.378   37.346  7.037   1.00 24.91 ? 121 ARG D CG  1 
ATOM   5369 C  CD  . ARG D 1 133 ? 2.561   37.066  8.530   1.00 25.37 ? 121 ARG D CD  1 
ATOM   5370 N  NE  . ARG D 1 133 ? 3.183   35.750  8.670   1.00 29.48 ? 121 ARG D NE  1 
ATOM   5371 C  CZ  . ARG D 1 133 ? 4.315   35.467  9.323   1.00 30.18 ? 121 ARG D CZ  1 
ATOM   5372 N  NH1 . ARG D 1 133 ? 4.965   36.401  10.001  1.00 32.24 ? 121 ARG D NH1 1 
ATOM   5373 N  NH2 . ARG D 1 133 ? 4.774   34.227  9.342   1.00 28.14 ? 121 ARG D NH2 1 
ATOM   5374 N  N   . GLU D 1 134 ? 6.674   39.255  6.127   1.00 23.93 ? 122 GLU D N   1 
ATOM   5375 C  CA  . GLU D 1 134 ? 7.993   39.516  5.497   1.00 25.51 ? 122 GLU D CA  1 
ATOM   5376 C  C   . GLU D 1 134 ? 8.887   38.319  5.806   1.00 24.75 ? 122 GLU D C   1 
ATOM   5377 O  O   . GLU D 1 134 ? 8.933   37.917  6.969   1.00 25.73 ? 122 GLU D O   1 
ATOM   5378 C  CB  . GLU D 1 134 ? 8.601   40.836  6.013   1.00 30.15 ? 122 GLU D CB  1 
ATOM   5379 C  CG  . GLU D 1 134 ? 7.998   42.091  5.386   1.00 35.06 ? 122 GLU D CG  1 
ATOM   5380 C  CD  . GLU D 1 134 ? 8.463   43.423  5.975   1.00 42.11 ? 122 GLU D CD  1 
ATOM   5381 O  OE1 . GLU D 1 134 ? 7.657   44.074  6.663   1.00 47.49 ? 122 GLU D OE1 1 
ATOM   5382 O  OE2 . GLU D 1 134 ? 9.627   43.808  5.756   1.00 46.65 ? 122 GLU D OE2 1 
ATOM   5383 N  N   . ASN D 1 135 ? 9.511   37.726  4.788   1.00 26.98 ? 123 ASN D N   1 
ATOM   5384 C  CA  . ASN D 1 135 ? 10.550  36.688  4.974   1.00 28.02 ? 123 ASN D CA  1 
ATOM   5385 C  C   . ASN D 1 135 ? 9.948   35.551  5.800   1.00 26.63 ? 123 ASN D C   1 
ATOM   5386 O  O   . ASN D 1 135 ? 10.574  35.121  6.772   1.00 28.66 ? 123 ASN D O   1 
ATOM   5387 C  CB  . ASN D 1 135 ? 11.785  37.315  5.615   1.00 31.53 ? 123 ASN D CB  1 
ATOM   5388 C  CG  . ASN D 1 135 ? 12.280  38.472  4.774   1.00 34.15 ? 123 ASN D CG  1 
ATOM   5389 O  OD1 . ASN D 1 135 ? 12.600  38.297  3.593   1.00 35.41 ? 123 ASN D OD1 1 
ATOM   5390 N  ND2 . ASN D 1 135 ? 12.289  39.653  5.357   1.00 36.50 ? 123 ASN D ND2 1 
ATOM   5391 N  N   . ALA D 1 136 ? 8.743   35.126  5.424   1.00 23.41 ? 124 ALA D N   1 
ATOM   5392 C  CA  . ALA D 1 136 ? 7.878   34.267  6.253   1.00 21.36 ? 124 ALA D CA  1 
ATOM   5393 C  C   . ALA D 1 136 ? 7.699   32.921  5.557   1.00 21.50 ? 124 ALA D C   1 
ATOM   5394 O  O   . ALA D 1 136 ? 7.762   32.821  4.325   1.00 21.95 ? 124 ALA D O   1 
ATOM   5395 C  CB  . ALA D 1 136 ? 6.554   34.927  6.486   1.00 22.01 ? 124 ALA D CB  1 
ATOM   5396 N  N   . PRO D 1 137 ? 7.342   31.869  6.304   1.00 19.85 ? 125 PRO D N   1 
ATOM   5397 C  CA  . PRO D 1 137 ? 7.010   30.576  5.682   1.00 19.89 ? 125 PRO D CA  1 
ATOM   5398 C  C   . PRO D 1 137 ? 5.786   30.741  4.764   1.00 18.49 ? 125 PRO D C   1 
ATOM   5399 O  O   . PRO D 1 137 ? 4.883   31.541  5.089   1.00 22.12 ? 125 PRO D O   1 
ATOM   5400 C  CB  . PRO D 1 137 ? 6.729   29.672  6.895   1.00 22.62 ? 125 PRO D CB  1 
ATOM   5401 C  CG  . PRO D 1 137 ? 7.462   30.351  8.009   1.00 21.77 ? 125 PRO D CG  1 
ATOM   5402 C  CD  . PRO D 1 137 ? 7.243   31.836  7.770   1.00 22.74 ? 125 PRO D CD  1 
ATOM   5403 N  N   . SER D 1 138 ? 5.832   30.130  3.596   1.00 18.92 ? 126 SER D N   1 
ATOM   5404 C  CA  . SER D 1 138 ? 4.713   30.133  2.618   1.00 17.90 ? 126 SER D CA  1 
ATOM   5405 C  C   . SER D 1 138 ? 4.677   28.821  1.806   1.00 18.73 ? 126 SER D C   1 
ATOM   5406 O  O   . SER D 1 138 ? 5.642   28.010  1.871   1.00 19.32 ? 126 SER D O   1 
ATOM   5407 C  CB  . SER D 1 138 ? 4.831   31.328  1.755   1.00 19.54 ? 126 SER D CB  1 
ATOM   5408 O  OG  . SER D 1 138 ? 5.686   31.055  0.674   1.00 18.78 ? 126 SER D OG  1 
ATOM   5409 N  N   . ILE D 1 139 ? 3.636   28.650  0.975   1.00 18.04 ? 127 ILE D N   1 
ATOM   5410 C  CA  . ILE D 1 139 ? 3.554   27.526  0.005   1.00 19.75 ? 127 ILE D CA  1 
ATOM   5411 C  C   . ILE D 1 139 ? 4.663   27.658  -1.051  1.00 20.72 ? 127 ILE D C   1 
ATOM   5412 O  O   . ILE D 1 139 ? 4.849   26.679  -1.820  1.00 21.58 ? 127 ILE D O   1 
ATOM   5413 C  CB  . ILE D 1 139 ? 2.156   27.444  -0.638  1.00 19.02 ? 127 ILE D CB  1 
ATOM   5414 C  CG1 . ILE D 1 139 ? 1.760   28.720  -1.378  1.00 21.73 ? 127 ILE D CG1 1 
ATOM   5415 C  CG2 . ILE D 1 139 ? 1.144   27.042  0.446   1.00 19.82 ? 127 ILE D CG2 1 
ATOM   5416 C  CD1 . ILE D 1 139 ? 0.594   28.485  -2.337  1.00 20.85 ? 127 ILE D CD1 1 
ATOM   5417 N  N   . GLU D 1 140 ? 5.364   28.793  -1.102  1.00 20.65 ? 128 GLU D N   1 
ATOM   5418 C  CA  . GLU D 1 140 ? 6.444   28.995  -2.093  1.00 21.73 ? 128 GLU D CA  1 
ATOM   5419 C  C   . GLU D 1 140 ? 7.814   28.998  -1.410  1.00 21.93 ? 128 GLU D C   1 
ATOM   5420 O  O   . GLU D 1 140 ? 8.826   29.170  -2.137  1.00 25.19 ? 128 GLU D O   1 
ATOM   5421 C  CB  . GLU D 1 140 ? 6.211   30.270  -2.905  1.00 25.99 ? 128 GLU D CB  1 
ATOM   5422 C  CG  . GLU D 1 140 ? 5.063   30.151  -3.913  1.00 26.08 ? 128 GLU D CG  1 
ATOM   5423 C  CD  . GLU D 1 140 ? 5.179   29.004  -4.908  1.00 27.65 ? 128 GLU D CD  1 
ATOM   5424 O  OE1 . GLU D 1 140 ? 4.364   28.928  -5.840  1.00 32.58 ? 128 GLU D OE1 1 
ATOM   5425 O  OE2 . GLU D 1 140 ? 6.080   28.183  -4.756  1.00 32.20 ? 128 GLU D OE2 1 
ATOM   5426 N  N   . GLY D 1 141 ? 7.868   28.735  -0.107  1.00 18.81 ? 129 GLY D N   1 
ATOM   5427 C  CA  . GLY D 1 141 ? 9.097   28.839  0.694   1.00 21.27 ? 129 GLY D CA  1 
ATOM   5428 C  C   . GLY D 1 141 ? 9.162   30.193  1.358   1.00 20.19 ? 129 GLY D C   1 
ATOM   5429 O  O   . GLY D 1 141 ? 8.130   30.860  1.422   1.00 21.46 ? 129 GLY D O   1 
ATOM   5430 N  N   . THR D 1 142 ? 10.313  30.559  1.898   1.00 20.45 ? 130 THR D N   1 
ATOM   5431 C  CA  . THR D 1 142 ? 10.487  31.866  2.554   1.00 20.86 ? 130 THR D CA  1 
ATOM   5432 C  C   . THR D 1 142 ? 10.075  32.971  1.572   1.00 21.27 ? 130 THR D C   1 
ATOM   5433 O  O   . THR D 1 142 ? 10.647  33.086  0.473   1.00 21.47 ? 130 THR D O   1 
ATOM   5434 C  CB  . THR D 1 142 ? 11.906  32.026  3.107   1.00 22.09 ? 130 THR D CB  1 
ATOM   5435 O  OG1 . THR D 1 142 ? 12.180  30.876  3.913   1.00 24.42 ? 130 THR D OG1 1 
ATOM   5436 C  CG2 . THR D 1 142 ? 12.065  33.322  3.860   1.00 23.27 ? 130 THR D CG2 1 
ATOM   5437 N  N   . ALA D 1 143 ? 9.094   33.761  1.941   1.00 19.71 ? 131 ALA D N   1 
ATOM   5438 C  CA  . ALA D 1 143 ? 8.533   34.755  1.012   1.00 22.13 ? 131 ALA D CA  1 
ATOM   5439 C  C   . ALA D 1 143 ? 7.927   35.939  1.752   1.00 21.93 ? 131 ALA D C   1 
ATOM   5440 O  O   . ALA D 1 143 ? 7.604   35.820  2.968   1.00 22.42 ? 131 ALA D O   1 
ATOM   5441 C  CB  . ALA D 1 143 ? 7.542   34.077  0.093   1.00 21.02 ? 131 ALA D CB  1 
ATOM   5442 N  N   . THR D 1 144 ? 7.744   37.036  1.016   1.00 20.64 ? 132 THR D N   1 
ATOM   5443 C  CA  . THR D 1 144 ? 6.969   38.225  1.432   1.00 20.27 ? 132 THR D CA  1 
ATOM   5444 C  C   . THR D 1 144 ? 5.625   38.228  0.685   1.00 21.22 ? 132 THR D C   1 
ATOM   5445 O  O   . THR D 1 144 ? 5.606   38.095  -0.545  1.00 22.50 ? 132 THR D O   1 
ATOM   5446 C  CB  . THR D 1 144 ? 7.827   39.494  1.267   1.00 21.43 ? 132 THR D CB  1 
ATOM   5447 O  OG1 . THR D 1 144 ? 8.910   39.447  2.202   1.00 23.45 ? 132 THR D OG1 1 
ATOM   5448 C  CG2 . THR D 1 144 ? 7.046   40.773  1.502   1.00 21.33 ? 132 THR D CG2 1 
ATOM   5449 N  N   . PHE D 1 145 ? 4.515   38.352  1.400   1.00 19.78 ? 133 PHE D N   1 
ATOM   5450 C  CA  . PHE D 1 145 ? 3.151   38.159  0.835   1.00 19.77 ? 133 PHE D CA  1 
ATOM   5451 C  C   . PHE D 1 145 ? 2.153   39.007  1.627   1.00 19.28 ? 133 PHE D C   1 
ATOM   5452 O  O   . PHE D 1 145 ? 2.363   39.326  2.813   1.00 20.84 ? 133 PHE D O   1 
ATOM   5453 C  CB  . PHE D 1 145 ? 2.779   36.660  0.781   1.00 20.25 ? 133 PHE D CB  1 
ATOM   5454 C  CG  . PHE D 1 145 ? 2.963   35.871  2.061   1.00 20.50 ? 133 PHE D CG  1 
ATOM   5455 C  CD1 . PHE D 1 145 ? 4.179   35.282  2.369   1.00 18.86 ? 133 PHE D CD1 1 
ATOM   5456 C  CD2 . PHE D 1 145 ? 1.926   35.725  2.977   1.00 20.71 ? 133 PHE D CD2 1 
ATOM   5457 C  CE1 . PHE D 1 145 ? 4.353   34.579  3.550   1.00 20.42 ? 133 PHE D CE1 1 
ATOM   5458 C  CE2 . PHE D 1 145 ? 2.107   35.045  4.171   1.00 20.74 ? 133 PHE D CE2 1 
ATOM   5459 C  CZ  . PHE D 1 145 ? 3.323   34.466  4.456   1.00 20.41 ? 133 PHE D CZ  1 
ATOM   5460 N  N   . ASN D 1 146 ? 1.082   39.393  0.960   1.00 21.10 ? 134 ASN D N   1 
ATOM   5461 C  CA  . ASN D 1 146 ? -0.090  40.012  1.607   1.00 21.59 ? 134 ASN D CA  1 
ATOM   5462 C  C   . ASN D 1 146 ? -0.849  38.946  2.405   1.00 16.83 ? 134 ASN D C   1 
ATOM   5463 O  O   . ASN D 1 146 ? -0.820  37.709  2.062   1.00 17.49 ? 134 ASN D O   1 
ATOM   5464 C  CB  . ASN D 1 146 ? -0.955  40.729  0.575   1.00 23.11 ? 134 ASN D CB  1 
ATOM   5465 C  CG  . ASN D 1 146 ? -0.275  41.964  0.010   1.00 29.14 ? 134 ASN D CG  1 
ATOM   5466 O  OD1 . ASN D 1 146 ? 0.700   42.452  0.570   1.00 32.98 ? 134 ASN D OD1 1 
ATOM   5467 N  ND2 . ASN D 1 146 ? -0.779  42.458  -1.104  1.00 33.27 ? 134 ASN D ND2 1 
ATOM   5468 N  N   . GLN D 1 147 ? -1.426  39.377  3.523   1.00 19.22 ? 135 GLN D N   1 
ATOM   5469 C  CA  . GLN D 1 147 ? -2.253  38.505  4.404   1.00 17.71 ? 135 GLN D CA  1 
ATOM   5470 C  C   . GLN D 1 147 ? -3.597  39.206  4.614   1.00 16.68 ? 135 GLN D C   1 
ATOM   5471 O  O   . GLN D 1 147 ? -3.597  40.413  5.020   1.00 19.28 ? 135 GLN D O   1 
ATOM   5472 C  CB  . GLN D 1 147 ? -1.502  38.234  5.713   1.00 18.68 ? 135 GLN D CB  1 
ATOM   5473 C  CG  . GLN D 1 147 ? -2.182  37.208  6.602   1.00 18.84 ? 135 GLN D CG  1 
ATOM   5474 C  CD  . GLN D 1 147 ? -1.425  37.138  7.908   1.00 18.82 ? 135 GLN D CD  1 
ATOM   5475 O  OE1 . GLN D 1 147 ? -1.280  38.152  8.588   1.00 23.19 ? 135 GLN D OE1 1 
ATOM   5476 N  NE2 . GLN D 1 147 ? -0.902  35.964  8.246   1.00 17.29 ? 135 GLN D NE2 1 
ATOM   5477 N  N   . TYR D 1 148 ? -4.704  38.593  4.217   1.00 15.71 ? 136 TYR D N   1 
ATOM   5478 C  CA  . TYR D 1 148 ? -6.058  39.176  4.337   1.00 16.54 ? 136 TYR D CA  1 
ATOM   5479 C  C   . TYR D 1 148 ? -6.825  38.419  5.414   1.00 16.74 ? 136 TYR D C   1 
ATOM   5480 O  O   . TYR D 1 148 ? -6.743  37.179  5.471   1.00 19.00 ? 136 TYR D O   1 
ATOM   5481 C  CB  . TYR D 1 148 ? -6.865  39.183  3.038   1.00 17.69 ? 136 TYR D CB  1 
ATOM   5482 C  CG  . TYR D 1 148 ? -6.163  39.793  1.844   1.00 18.95 ? 136 TYR D CG  1 
ATOM   5483 C  CD1 . TYR D 1 148 ? -5.182  40.759  1.982   1.00 21.21 ? 136 TYR D CD1 1 
ATOM   5484 C  CD2 . TYR D 1 148 ? -6.516  39.425  0.559   1.00 21.52 ? 136 TYR D CD2 1 
ATOM   5485 C  CE1 . TYR D 1 148 ? -4.501  41.246  0.885   1.00 22.07 ? 136 TYR D CE1 1 
ATOM   5486 C  CE2 . TYR D 1 148 ? -5.871  39.939  -0.554  1.00 22.81 ? 136 TYR D CE2 1 
ATOM   5487 C  CZ  . TYR D 1 148 ? -4.849  40.843  -0.392  1.00 22.59 ? 136 TYR D CZ  1 
ATOM   5488 O  OH  . TYR D 1 148 ? -4.212  41.370  -1.490  1.00 23.91 ? 136 TYR D OH  1 
ATOM   5489 N  N   . TRP D 1 149 ? -7.621  39.165  6.166   1.00 17.29 ? 137 TRP D N   1 
ATOM   5490 C  CA  . TRP D 1 149 ? -8.482  38.676  7.266   1.00 17.34 ? 137 TRP D CA  1 
ATOM   5491 C  C   . TRP D 1 149 ? -9.921  39.135  7.043   1.00 16.41 ? 137 TRP D C   1 
ATOM   5492 O  O   . TRP D 1 149 ? -10.187 40.373  6.747   1.00 20.30 ? 137 TRP D O   1 
ATOM   5493 C  CB  . TRP D 1 149 ? -7.996  39.120  8.645   1.00 17.72 ? 137 TRP D CB  1 
ATOM   5494 C  CG  . TRP D 1 149 ? -6.579  38.760  8.958   1.00 17.47 ? 137 TRP D CG  1 
ATOM   5495 C  CD1 . TRP D 1 149 ? -5.459  39.425  8.562   1.00 19.77 ? 137 TRP D CD1 1 
ATOM   5496 C  CD2 . TRP D 1 149 ? -6.120  37.617  9.695   1.00 18.16 ? 137 TRP D CD2 1 
ATOM   5497 N  NE1 . TRP D 1 149 ? -4.342  38.818  9.055   1.00 19.36 ? 137 TRP D NE1 1 
ATOM   5498 C  CE2 . TRP D 1 149 ? -4.710  37.685  9.732   1.00 20.07 ? 137 TRP D CE2 1 
ATOM   5499 C  CE3 . TRP D 1 149 ? -6.768  36.579  10.379  1.00 17.00 ? 137 TRP D CE3 1 
ATOM   5500 C  CZ2 . TRP D 1 149 ? -3.929  36.722  10.363  1.00 19.59 ? 137 TRP D CZ2 1 
ATOM   5501 C  CZ3 . TRP D 1 149 ? -5.989  35.628  11.010  1.00 17.09 ? 137 TRP D CZ3 1 
ATOM   5502 C  CH2 . TRP D 1 149 ? -4.592  35.699  11.004  1.00 18.08 ? 137 TRP D CH2 1 
ATOM   5503 N  N   . SER D 1 150 ? -10.815 38.206  7.316   1.00 20.36 ? 138 SER D N   1 
ATOM   5504 C  CA  . SER D 1 150 ? -12.234 38.459  7.623   1.00 19.93 ? 138 SER D CA  1 
ATOM   5505 C  C   . SER D 1 150 ? -12.501 37.852  8.986   1.00 19.33 ? 138 SER D C   1 
ATOM   5506 O  O   . SER D 1 150 ? -12.261 36.643  9.134   1.00 19.61 ? 138 SER D O   1 
ATOM   5507 C  CB  . SER D 1 150 ? -13.123 37.824  6.593   1.00 23.32 ? 138 SER D CB  1 
ATOM   5508 O  OG  . SER D 1 150 ? -13.581 38.795  5.688   1.00 32.44 ? 138 SER D OG  1 
ATOM   5509 N  N   . VAL D 1 151 ? -12.950 38.633  9.966   1.00 18.50 ? 139 VAL D N   1 
ATOM   5510 C  CA  . VAL D 1 151 ? -13.063 38.066  11.333  1.00 18.57 ? 139 VAL D CA  1 
ATOM   5511 C  C   . VAL D 1 151 ? -14.517 38.215  11.805  1.00 18.88 ? 139 VAL D C   1 
ATOM   5512 O  O   . VAL D 1 151 ? -15.018 39.360  11.898  1.00 18.92 ? 139 VAL D O   1 
ATOM   5513 C  CB  . VAL D 1 151 ? -12.043 38.699  12.290  1.00 18.80 ? 139 VAL D CB  1 
ATOM   5514 C  CG1 . VAL D 1 151 ? -12.226 38.195  13.712  1.00 20.67 ? 139 VAL D CG1 1 
ATOM   5515 C  CG2 . VAL D 1 151 ? -10.594 38.535  11.797  1.00 19.61 ? 139 VAL D CG2 1 
ATOM   5516 N  N   . ARG D 1 152 ? -15.182 37.104  12.112  1.00 20.04 ? 140 ARG D N   1 
ATOM   5517 C  CA  . ARG D 1 152 ? -16.620 37.148  12.499  1.00 20.57 ? 140 ARG D CA  1 
ATOM   5518 C  C   . ARG D 1 152 ? -16.791 37.859  13.852  1.00 22.33 ? 140 ARG D C   1 
ATOM   5519 O  O   . ARG D 1 152 ? -16.003 37.604  14.763  1.00 21.89 ? 140 ARG D O   1 
ATOM   5520 C  CB  . ARG D 1 152 ? -17.166 35.726  12.581  1.00 20.58 ? 140 ARG D CB  1 
ATOM   5521 C  CG  . ARG D 1 152 ? -18.671 35.662  12.405  1.00 21.17 ? 140 ARG D CG  1 
ATOM   5522 C  CD  . ARG D 1 152 ? -19.152 34.230  12.505  1.00 20.82 ? 140 ARG D CD  1 
ATOM   5523 N  NE  . ARG D 1 152 ? -20.607 34.111  12.608  1.00 21.44 ? 140 ARG D NE  1 
ATOM   5524 C  CZ  . ARG D 1 152 ? -21.465 33.990  11.618  1.00 21.55 ? 140 ARG D CZ  1 
ATOM   5525 N  NH1 . ARG D 1 152 ? -21.057 33.935  10.364  1.00 22.65 ? 140 ARG D NH1 1 
ATOM   5526 N  NH2 . ARG D 1 152 ? -22.757 33.885  11.901  1.00 23.16 ? 140 ARG D NH2 1 
ATOM   5527 N  N   . THR D 1 153 ? -17.748 38.774  13.976  1.00 24.35 ? 141 THR D N   1 
ATOM   5528 C  CA  . THR D 1 153 ? -17.914 39.562  15.237  1.00 27.99 ? 141 THR D CA  1 
ATOM   5529 C  C   . THR D 1 153 ? -18.551 38.674  16.310  1.00 28.77 ? 141 THR D C   1 
ATOM   5530 O  O   . THR D 1 153 ? -18.189 38.826  17.503  1.00 30.65 ? 141 THR D O   1 
ATOM   5531 C  CB  . THR D 1 153 ? -18.699 40.858  15.006  1.00 29.62 ? 141 THR D CB  1 
ATOM   5532 O  OG1 . THR D 1 153 ? -20.009 40.560  14.530  1.00 32.67 ? 141 THR D OG1 1 
ATOM   5533 C  CG2 . THR D 1 153 ? -18.002 41.749  14.011  1.00 26.06 ? 141 THR D CG2 1 
ATOM   5534 N  N   . ASP D 1 154 ? -19.466 37.802  15.903  1.00 28.40 ? 142 ASP D N   1 
ATOM   5535 C  CA  . ASP D 1 154 ? -20.136 36.817  16.785  1.00 31.65 ? 142 ASP D CA  1 
ATOM   5536 C  C   . ASP D 1 154 ? -19.618 35.417  16.425  1.00 28.22 ? 142 ASP D C   1 
ATOM   5537 O  O   . ASP D 1 154 ? -20.020 34.892  15.360  1.00 29.98 ? 142 ASP D O   1 
ATOM   5538 C  CB  . ASP D 1 154 ? -21.655 36.863  16.630  1.00 34.61 ? 142 ASP D CB  1 
ATOM   5539 C  CG  . ASP D 1 154 ? -22.322 38.132  17.117  1.00 39.87 ? 142 ASP D CG  1 
ATOM   5540 O  OD1 . ASP D 1 154 ? -21.902 38.654  18.178  1.00 42.78 ? 142 ASP D OD1 1 
ATOM   5541 O  OD2 . ASP D 1 154 ? -23.291 38.546  16.454  1.00 43.96 ? 142 ASP D OD2 1 
ATOM   5542 N  N   . HIS D 1 155 ? -18.777 34.860  17.297  1.00 27.48 ? 143 HIS D N   1 
ATOM   5543 C  CA  . HIS D 1 155 ? -18.014 33.606  17.075  1.00 27.62 ? 143 HIS D CA  1 
ATOM   5544 C  C   . HIS D 1 155 ? -18.967 32.421  16.996  1.00 28.03 ? 143 HIS D C   1 
ATOM   5545 O  O   . HIS D 1 155 ? -19.979 32.391  17.728  1.00 25.49 ? 143 HIS D O   1 
ATOM   5546 C  CB  . HIS D 1 155 ? -16.983 33.418  18.187  1.00 26.03 ? 143 HIS D CB  1 
ATOM   5547 C  CG  . HIS D 1 155 ? -15.950 34.488  18.170  1.00 27.13 ? 143 HIS D CG  1 
ATOM   5548 N  ND1 . HIS D 1 155 ? -14.889 34.499  19.033  1.00 28.23 ? 143 HIS D ND1 1 
ATOM   5549 C  CD2 . HIS D 1 155 ? -15.804 35.557  17.357  1.00 26.86 ? 143 HIS D CD2 1 
ATOM   5550 C  CE1 . HIS D 1 155 ? -14.128 35.542  18.779  1.00 26.78 ? 143 HIS D CE1 1 
ATOM   5551 N  NE2 . HIS D 1 155 ? -14.668 36.206  17.749  1.00 26.85 ? 143 HIS D NE2 1 
ATOM   5552 N  N   . ARG D 1 156 ? -18.630 31.481  16.135  1.00 23.99 ? 144 ARG D N   1 
ATOM   5553 C  CA  . ARG D 1 156 ? -19.340 30.196  16.011  1.00 25.88 ? 144 ARG D CA  1 
ATOM   5554 C  C   . ARG D 1 156 ? -18.339 29.110  15.635  1.00 24.81 ? 144 ARG D C   1 
ATOM   5555 O  O   . ARG D 1 156 ? -17.237 29.431  15.133  1.00 22.27 ? 144 ARG D O   1 
ATOM   5556 C  CB  . ARG D 1 156 ? -20.447 30.295  14.961  1.00 27.22 ? 144 ARG D CB  1 
ATOM   5557 C  CG  . ARG D 1 156 ? -19.954 30.500  13.539  1.00 26.52 ? 144 ARG D CG  1 
ATOM   5558 C  CD  . ARG D 1 156 ? -21.095 30.456  12.549  1.00 26.34 ? 144 ARG D CD  1 
ATOM   5559 N  NE  . ARG D 1 156 ? -20.534 30.519  11.211  1.00 26.10 ? 144 ARG D NE  1 
ATOM   5560 C  CZ  . ARG D 1 156 ? -21.215 30.414  10.084  1.00 24.50 ? 144 ARG D CZ  1 
ATOM   5561 N  NH1 . ARG D 1 156 ? -22.527 30.311  10.101  1.00 27.69 ? 144 ARG D NH1 1 
ATOM   5562 N  NH2 . ARG D 1 156 ? -20.565 30.450  8.937   1.00 26.97 ? 144 ARG D NH2 1 
ATOM   5563 N  N   . VAL D 1 157 ? -18.753 27.879  15.887  1.00 23.07 ? 145 VAL D N   1 
ATOM   5564 C  CA  . VAL D 1 157 ? -18.063 26.626  15.496  1.00 23.69 ? 145 VAL D CA  1 
ATOM   5565 C  C   . VAL D 1 157 ? -19.080 25.876  14.646  1.00 25.26 ? 145 VAL D C   1 
ATOM   5566 O  O   . VAL D 1 157 ? -20.082 25.375  15.216  1.00 28.86 ? 145 VAL D O   1 
ATOM   5567 C  CB  . VAL D 1 157 ? -17.603 25.817  16.719  1.00 22.27 ? 145 VAL D CB  1 
ATOM   5568 C  CG1 . VAL D 1 157 ? -16.939 24.493  16.328  1.00 22.91 ? 145 VAL D CG1 1 
ATOM   5569 C  CG2 . VAL D 1 157 ? -16.696 26.614  17.633  1.00 22.44 ? 145 VAL D CG2 1 
ATOM   5570 N  N   . GLY D 1 158 ? -18.910 25.919  13.332  1.00 25.71 ? 146 GLY D N   1 
ATOM   5571 C  CA  . GLY D 1 158 ? -19.730 25.153  12.380  1.00 26.60 ? 146 GLY D CA  1 
ATOM   5572 C  C   . GLY D 1 158 ? -20.726 26.053  11.680  1.00 30.82 ? 146 GLY D C   1 
ATOM   5573 O  O   . GLY D 1 158 ? -21.156 27.070  12.267  1.00 32.40 ? 146 GLY D O   1 
ATOM   5574 N  N   . GLY D 1 159 ? -21.123 25.648  10.481  1.00 26.99 ? 147 GLY D N   1 
ATOM   5575 C  CA  . GLY D 1 159 ? -22.140 26.330  9.678   1.00 26.65 ? 147 GLY D CA  1 
ATOM   5576 C  C   . GLY D 1 159 ? -21.608 26.458  8.274   1.00 24.89 ? 147 GLY D C   1 
ATOM   5577 O  O   . GLY D 1 159 ? -20.697 25.695  7.929   1.00 24.56 ? 147 GLY D O   1 
ATOM   5578 N  N   . THR D 1 160 ? -22.142 27.400  7.513   1.00 22.74 ? 148 THR D N   1 
ATOM   5579 C  CA  . THR D 1 160 ? -21.835 27.554  6.075   1.00 22.56 ? 148 THR D CA  1 
ATOM   5580 C  C   . THR D 1 160 ? -21.038 28.835  5.903   1.00 22.83 ? 148 THR D C   1 
ATOM   5581 O  O   . THR D 1 160 ? -21.417 29.803  6.495   1.00 22.62 ? 148 THR D O   1 
ATOM   5582 C  CB  . THR D 1 160 ? -23.140 27.580  5.266   1.00 25.67 ? 148 THR D CB  1 
ATOM   5583 O  OG1 . THR D 1 160 ? -23.677 26.255  5.294   1.00 26.13 ? 148 THR D OG1 1 
ATOM   5584 C  CG2 . THR D 1 160 ? -22.930 28.037  3.841   1.00 29.31 ? 148 THR D CG2 1 
ATOM   5585 N  N   . VAL D 1 161 ? -19.991 28.812  5.084   1.00 21.84 ? 149 VAL D N   1 
ATOM   5586 C  CA  . VAL D 1 161 ? -19.164 29.999  4.771   1.00 19.32 ? 149 VAL D CA  1 
ATOM   5587 C  C   . VAL D 1 161 ? -19.194 30.212  3.259   1.00 20.79 ? 149 VAL D C   1 
ATOM   5588 O  O   . VAL D 1 161 ? -18.734 29.313  2.537   1.00 20.66 ? 149 VAL D O   1 
ATOM   5589 C  CB  . VAL D 1 161 ? -17.713 29.831  5.260   1.00 20.19 ? 149 VAL D CB  1 
ATOM   5590 C  CG1 . VAL D 1 161 ? -16.877 31.004  4.770   1.00 20.68 ? 149 VAL D CG1 1 
ATOM   5591 C  CG2 . VAL D 1 161 ? -17.639 29.701  6.772   1.00 19.76 ? 149 VAL D CG2 1 
ATOM   5592 N  N   . THR D 1 162 ? -19.770 31.336  2.809   1.00 20.79 ? 150 THR D N   1 
ATOM   5593 C  CA  . THR D 1 162 ? -19.947 31.647  1.372   1.00 20.31 ? 150 THR D CA  1 
ATOM   5594 C  C   . THR D 1 162 ? -18.663 32.359  0.974   1.00 19.57 ? 150 THR D C   1 
ATOM   5595 O  O   . THR D 1 162 ? -18.615 33.622  1.131   1.00 19.28 ? 150 THR D O   1 
ATOM   5596 C  CB  . THR D 1 162 ? -21.222 32.456  1.100   1.00 24.02 ? 150 THR D CB  1 
ATOM   5597 O  OG1 . THR D 1 162 ? -22.314 31.738  1.685   1.00 24.13 ? 150 THR D OG1 1 
ATOM   5598 C  CG2 . THR D 1 162 ? -21.457 32.687  -0.379  1.00 23.55 ? 150 THR D CG2 1 
ATOM   5599 N  N   . THR D 1 163 ? -17.624 31.605  0.617   1.00 20.37 ? 151 THR D N   1 
ATOM   5600 C  CA  . THR D 1 163 ? -16.262 32.191  0.515   1.00 19.52 ? 151 THR D CA  1 
ATOM   5601 C  C   . THR D 1 163 ? -16.251 33.319  -0.528  1.00 20.10 ? 151 THR D C   1 
ATOM   5602 O  O   . THR D 1 163 ? -15.568 34.318  -0.297  1.00 19.39 ? 151 THR D O   1 
ATOM   5603 C  CB  . THR D 1 163 ? -15.164 31.154  0.244   1.00 20.12 ? 151 THR D CB  1 
ATOM   5604 O  OG1 . THR D 1 163 ? -15.378 30.551  -1.026  1.00 19.48 ? 151 THR D OG1 1 
ATOM   5605 C  CG2 . THR D 1 163 ? -15.074 30.135  1.346   1.00 20.93 ? 151 THR D CG2 1 
ATOM   5606 N  N   . GLN D 1 164 ? -17.029 33.222  -1.604  1.00 22.25 ? 152 GLN D N   1 
ATOM   5607 C  CA  . GLN D 1 164 ? -17.061 34.274  -2.654  1.00 24.42 ? 152 GLN D CA  1 
ATOM   5608 C  C   . GLN D 1 164 ? -17.444 35.624  -2.040  1.00 22.56 ? 152 GLN D C   1 
ATOM   5609 O  O   . GLN D 1 164 ? -16.937 36.612  -2.491  1.00 24.92 ? 152 GLN D O   1 
ATOM   5610 C  CB  . GLN D 1 164 ? -17.993 33.881  -3.803  1.00 26.63 ? 152 GLN D CB  1 
ATOM   5611 C  CG  . GLN D 1 164 ? -17.846 34.751  -5.042  1.00 28.08 ? 152 GLN D CG  1 
ATOM   5612 C  CD  . GLN D 1 164 ? -16.427 34.815  -5.552  1.00 31.15 ? 152 GLN D CD  1 
ATOM   5613 O  OE1 . GLN D 1 164 ? -15.873 33.816  -5.985  1.00 35.07 ? 152 GLN D OE1 1 
ATOM   5614 N  NE2 . GLN D 1 164 ? -15.830 35.997  -5.506  1.00 32.66 ? 152 GLN D NE2 1 
ATOM   5615 N  N   . ASN D 1 165 ? -18.315 35.678  -1.034  1.00 22.52 ? 153 ASN D N   1 
ATOM   5616 C  CA  . ASN D 1 165 ? -18.725 36.964  -0.414  1.00 22.02 ? 153 ASN D CA  1 
ATOM   5617 C  C   . ASN D 1 165 ? -17.508 37.633  0.244   1.00 21.55 ? 153 ASN D C   1 
ATOM   5618 O  O   . ASN D 1 165 ? -17.458 38.876  0.259   1.00 21.89 ? 153 ASN D O   1 
ATOM   5619 C  CB  . ASN D 1 165 ? -19.888 36.760  0.569   1.00 22.37 ? 153 ASN D CB  1 
ATOM   5620 C  CG  . ASN D 1 165 ? -21.225 36.467  -0.094  1.00 23.35 ? 153 ASN D CG  1 
ATOM   5621 O  OD1 . ASN D 1 165 ? -21.451 36.771  -1.271  1.00 25.93 ? 153 ASN D OD1 1 
ATOM   5622 N  ND2 . ASN D 1 165 ? -22.135 35.897  0.682   1.00 24.55 ? 153 ASN D ND2 1 
ATOM   5623 N  N   . HIS D 1 166 ? -16.570 36.864  0.824   1.00 19.62 ? 154 HIS D N   1 
ATOM   5624 C  CA  . HIS D 1 166 ? -15.346 37.391  1.485   1.00 19.94 ? 154 HIS D CA  1 
ATOM   5625 C  C   . HIS D 1 166 ? -14.396 37.897  0.396   1.00 19.56 ? 154 HIS D C   1 
ATOM   5626 O  O   . HIS D 1 166 ? -13.897 39.062  0.502   1.00 21.23 ? 154 HIS D O   1 
ATOM   5627 C  CB  . HIS D 1 166 ? -14.738 36.296  2.383   1.00 17.88 ? 154 HIS D CB  1 
ATOM   5628 C  CG  . HIS D 1 166 ? -15.615 35.991  3.552   1.00 17.48 ? 154 HIS D CG  1 
ATOM   5629 N  ND1 . HIS D 1 166 ? -15.615 36.777  4.694   1.00 19.11 ? 154 HIS D ND1 1 
ATOM   5630 C  CD2 . HIS D 1 166 ? -16.549 35.045  3.741   1.00 20.02 ? 154 HIS D CD2 1 
ATOM   5631 C  CE1 . HIS D 1 166 ? -16.519 36.320  5.525   1.00 18.28 ? 154 HIS D CE1 1 
ATOM   5632 N  NE2 . HIS D 1 166 ? -17.104 35.247  4.987   1.00 17.46 ? 154 HIS D NE2 1 
ATOM   5633 N  N   . PHE D 1 167 ? -14.165 37.062  -0.617  1.00 20.55 ? 155 PHE D N   1 
ATOM   5634 C  CA  . PHE D 1 167 ? -13.276 37.404  -1.752  1.00 20.34 ? 155 PHE D CA  1 
ATOM   5635 C  C   . PHE D 1 167 ? -13.787 38.696  -2.416  1.00 22.15 ? 155 PHE D C   1 
ATOM   5636 O  O   . PHE D 1 167 ? -12.945 39.582  -2.708  1.00 22.91 ? 155 PHE D O   1 
ATOM   5637 C  CB  . PHE D 1 167 ? -13.177 36.238  -2.740  1.00 19.55 ? 155 PHE D CB  1 
ATOM   5638 C  CG  . PHE D 1 167 ? -12.606 34.975  -2.166  1.00 20.75 ? 155 PHE D CG  1 
ATOM   5639 C  CD1 . PHE D 1 167 ? -11.728 34.984  -1.088  1.00 23.67 ? 155 PHE D CD1 1 
ATOM   5640 C  CD2 . PHE D 1 167 ? -12.990 33.751  -2.667  1.00 20.95 ? 155 PHE D CD2 1 
ATOM   5641 C  CE1 . PHE D 1 167 ? -11.236 33.796  -0.556  1.00 25.47 ? 155 PHE D CE1 1 
ATOM   5642 C  CE2 . PHE D 1 167 ? -12.500 32.565  -2.135  1.00 22.45 ? 155 PHE D CE2 1 
ATOM   5643 C  CZ  . PHE D 1 167 ? -11.592 32.582  -1.099  1.00 21.67 ? 155 PHE D CZ  1 
ATOM   5644 N  N   . ASP D 1 168 ? -15.107 38.806  -2.630  1.00 24.66 ? 156 ASP D N   1 
ATOM   5645 C  CA  . ASP D 1 168 ? -15.764 40.009  -3.215  1.00 24.18 ? 156 ASP D CA  1 
ATOM   5646 C  C   . ASP D 1 168 ? -15.583 41.219  -2.304  1.00 25.15 ? 156 ASP D C   1 
ATOM   5647 O  O   . ASP D 1 168 ? -15.316 42.313  -2.848  1.00 22.97 ? 156 ASP D O   1 
ATOM   5648 C  CB  . ASP D 1 168 ? -17.254 39.801  -3.465  1.00 27.43 ? 156 ASP D CB  1 
ATOM   5649 C  CG  . ASP D 1 168 ? -17.575 38.904  -4.644  1.00 30.60 ? 156 ASP D CG  1 
ATOM   5650 O  OD1 . ASP D 1 168 ? -16.659 38.606  -5.433  1.00 34.17 ? 156 ASP D OD1 1 
ATOM   5651 O  OD2 . ASP D 1 168 ? -18.752 38.533  -4.762  1.00 36.52 ? 156 ASP D OD2 1 
ATOM   5652 N  N   . ALA D 1 169 ? -15.709 41.052  -0.984  1.00 22.95 ? 157 ALA D N   1 
ATOM   5653 C  CA  . ALA D 1 169 ? -15.493 42.132  0.006   1.00 23.99 ? 157 ALA D CA  1 
ATOM   5654 C  C   . ALA D 1 169 ? -14.037 42.610  -0.067  1.00 24.50 ? 157 ALA D C   1 
ATOM   5655 O  O   . ALA D 1 169 ? -13.804 43.820  -0.107  1.00 21.86 ? 157 ALA D O   1 
ATOM   5656 C  CB  . ALA D 1 169 ? -15.869 41.692  1.389   1.00 25.97 ? 157 ALA D CB  1 
ATOM   5657 N  N   . TRP D 1 170 ? -13.068 41.698  -0.089  1.00 22.36 ? 158 TRP D N   1 
ATOM   5658 C  CA  . TRP D 1 170 ? -11.636 42.082  -0.174  1.00 22.48 ? 158 TRP D CA  1 
ATOM   5659 C  C   . TRP D 1 170 ? -11.367 42.824  -1.501  1.00 22.41 ? 158 TRP D C   1 
ATOM   5660 O  O   . TRP D 1 170 ? -10.715 43.883  -1.440  1.00 23.25 ? 158 TRP D O   1 
ATOM   5661 C  CB  . TRP D 1 170 ? -10.704 40.878  -0.025  1.00 23.01 ? 158 TRP D CB  1 
ATOM   5662 C  CG  . TRP D 1 170 ? -10.776 40.222  1.318   1.00 24.68 ? 158 TRP D CG  1 
ATOM   5663 C  CD1 . TRP D 1 170 ? -11.062 40.817  2.507   1.00 30.22 ? 158 TRP D CD1 1 
ATOM   5664 C  CD2 . TRP D 1 170 ? -10.559 38.834  1.610   1.00 23.27 ? 158 TRP D CD2 1 
ATOM   5665 N  NE1 . TRP D 1 170 ? -11.032 39.908  3.529   1.00 31.46 ? 158 TRP D NE1 1 
ATOM   5666 C  CE2 . TRP D 1 170 ? -10.764 38.669  3.000   1.00 24.94 ? 158 TRP D CE2 1 
ATOM   5667 C  CE3 . TRP D 1 170 ? -10.239 37.724  0.832   1.00 22.88 ? 158 TRP D CE3 1 
ATOM   5668 C  CZ2 . TRP D 1 170 ? -10.594 37.444  3.631   1.00 24.40 ? 158 TRP D CZ2 1 
ATOM   5669 C  CZ3 . TRP D 1 170 ? -10.088 36.509  1.457   1.00 23.39 ? 158 TRP D CZ3 1 
ATOM   5670 C  CH2 . TRP D 1 170 ? -10.296 36.376  2.832   1.00 21.42 ? 158 TRP D CH2 1 
ATOM   5671 N  N   . LYS D 1 171 ? -11.894 42.317  -2.620  1.00 23.45 ? 159 LYS D N   1 
ATOM   5672 C  CA  . LYS D 1 171 ? -11.774 42.950  -3.965  1.00 26.77 ? 159 LYS D CA  1 
ATOM   5673 C  C   . LYS D 1 171 ? -12.341 44.380  -3.894  1.00 27.00 ? 159 LYS D C   1 
ATOM   5674 O  O   . LYS D 1 171 ? -11.661 45.288  -4.351  1.00 27.92 ? 159 LYS D O   1 
ATOM   5675 C  CB  . LYS D 1 171 ? -12.492 42.141  -5.048  1.00 30.09 ? 159 LYS D CB  1 
ATOM   5676 C  CG  . LYS D 1 171 ? -12.268 42.640  -6.474  1.00 36.12 ? 159 LYS D CG  1 
ATOM   5677 C  CD  . LYS D 1 171 ? -12.791 41.739  -7.590  1.00 38.99 ? 159 LYS D CD  1 
ATOM   5678 C  CE  . LYS D 1 171 ? -12.647 42.391  -8.956  1.00 43.58 ? 159 LYS D CE  1 
ATOM   5679 N  NZ  . LYS D 1 171 ? -13.153 41.550  -10.069 1.00 45.36 ? 159 LYS D NZ  1 
ATOM   5680 N  N   . ASN D 1 172 ? -13.533 44.556  -3.315  1.00 27.70 ? 160 ASN D N   1 
ATOM   5681 C  CA  . ASN D 1 172 ? -14.258 45.854  -3.181  1.00 28.82 ? 160 ASN D CA  1 
ATOM   5682 C  C   . ASN D 1 172 ? -13.416 46.875  -2.402  1.00 29.56 ? 160 ASN D C   1 
ATOM   5683 O  O   . ASN D 1 172 ? -13.416 48.066  -2.764  1.00 31.49 ? 160 ASN D O   1 
ATOM   5684 C  CB  . ASN D 1 172 ? -15.623 45.588  -2.545  1.00 32.77 ? 160 ASN D CB  1 
ATOM   5685 C  CG  . ASN D 1 172 ? -16.558 46.768  -2.579  1.00 36.52 ? 160 ASN D CG  1 
ATOM   5686 O  OD1 . ASN D 1 172 ? -16.922 47.289  -1.533  1.00 44.34 ? 160 ASN D OD1 1 
ATOM   5687 N  ND2 . ASN D 1 172 ? -16.984 47.153  -3.770  1.00 37.64 ? 160 ASN D ND2 1 
ATOM   5688 N  N   . ALA D 1 173 ? -12.685 46.429  -1.383  1.00 27.75 ? 161 ALA D N   1 
ATOM   5689 C  CA  . ALA D 1 173 ? -11.772 47.259  -0.573  1.00 29.73 ? 161 ALA D CA  1 
ATOM   5690 C  C   . ALA D 1 173 ? -10.428 47.436  -1.300  1.00 27.48 ? 161 ALA D C   1 
ATOM   5691 O  O   . ALA D 1 173 ? -9.521  48.057  -0.715  1.00 33.15 ? 161 ALA D O   1 
ATOM   5692 C  CB  . ALA D 1 173 ? -11.591 46.610  0.774   1.00 29.86 ? 161 ALA D CB  1 
ATOM   5693 N  N   . GLY D 1 174 ? -10.288 46.873  -2.510  1.00 27.08 ? 162 GLY D N   1 
ATOM   5694 C  CA  . GLY D 1 174 ? -9.161  47.133  -3.423  1.00 27.55 ? 162 GLY D CA  1 
ATOM   5695 C  C   . GLY D 1 174 ? -8.072  46.077  -3.356  1.00 29.83 ? 162 GLY D C   1 
ATOM   5696 O  O   . GLY D 1 174 ? -7.043  46.254  -4.054  1.00 32.82 ? 162 GLY D O   1 
ATOM   5697 N  N   . LEU D 1 175 ? -8.284  45.015  -2.566  1.00 27.31 ? 163 LEU D N   1 
ATOM   5698 C  CA  . LEU D 1 175 ? -7.288  43.940  -2.291  1.00 27.63 ? 163 LEU D CA  1 
ATOM   5699 C  C   . LEU D 1 175 ? -7.214  42.972  -3.477  1.00 27.13 ? 163 LEU D C   1 
ATOM   5700 O  O   . LEU D 1 175 ? -8.244  42.387  -3.864  1.00 27.32 ? 163 LEU D O   1 
ATOM   5701 C  CB  . LEU D 1 175 ? -7.672  43.222  -0.991  1.00 25.86 ? 163 LEU D CB  1 
ATOM   5702 C  CG  . LEU D 1 175 ? -7.704  44.132  0.239   1.00 28.09 ? 163 LEU D CG  1 
ATOM   5703 C  CD1 . LEU D 1 175 ? -8.110  43.372  1.504   1.00 28.57 ? 163 LEU D CD1 1 
ATOM   5704 C  CD2 . LEU D 1 175 ? -6.359  44.830  0.421   1.00 26.16 ? 163 LEU D CD2 1 
ATOM   5705 N  N   . GLU D 1 176 ? -6.012  42.806  -4.015  1.00 27.24 ? 164 GLU D N   1 
ATOM   5706 C  CA  . GLU D 1 176 ? -5.724  41.917  -5.167  1.00 28.39 ? 164 GLU D CA  1 
ATOM   5707 C  C   . GLU D 1 176 ? -5.575  40.482  -4.679  1.00 27.95 ? 164 GLU D C   1 
ATOM   5708 O  O   . GLU D 1 176 ? -4.889  40.290  -3.653  1.00 32.91 ? 164 GLU D O   1 
ATOM   5709 C  CB  . GLU D 1 176 ? -4.403  42.324  -5.811  1.00 31.22 ? 164 GLU D CB  1 
ATOM   5710 C  CG  . GLU D 1 176 ? -4.420  43.740  -6.336  1.00 35.34 ? 164 GLU D CG  1 
ATOM   5711 C  CD  . GLU D 1 176 ? -4.394  43.782  -7.846  1.00 40.55 ? 164 GLU D CD  1 
ATOM   5712 O  OE1 . GLU D 1 176 ? -5.494  43.834  -8.452  1.00 43.20 ? 164 GLU D OE1 1 
ATOM   5713 O  OE2 . GLU D 1 176 ? -3.272  43.724  -8.406  1.00 49.84 ? 164 GLU D OE2 1 
ATOM   5714 N  N   . MET D 1 177 ? -6.144  39.537  -5.430  1.00 25.25 ? 165 MET D N   1 
ATOM   5715 C  CA  . MET D 1 177 ? -5.994  38.065  -5.226  1.00 26.46 ? 165 MET D CA  1 
ATOM   5716 C  C   . MET D 1 177 ? -5.413  37.434  -6.493  1.00 25.18 ? 165 MET D C   1 
ATOM   5717 O  O   . MET D 1 177 ? -5.772  37.861  -7.594  1.00 22.25 ? 165 MET D O   1 
ATOM   5718 C  CB  . MET D 1 177 ? -7.333  37.383  -4.945  1.00 27.63 ? 165 MET D CB  1 
ATOM   5719 C  CG  . MET D 1 177 ? -8.138  38.037  -3.860  1.00 33.01 ? 165 MET D CG  1 
ATOM   5720 S  SD  . MET D 1 177 ? -7.876  37.313  -2.242  1.00 43.07 ? 165 MET D SD  1 
ATOM   5721 C  CE  . MET D 1 177 ? -8.478  35.637  -2.450  1.00 40.06 ? 165 MET D CE  1 
ATOM   5722 N  N   . GLY D 1 178 ? -4.624  36.384  -6.325  1.00 22.07 ? 166 GLY D N   1 
ATOM   5723 C  CA  . GLY D 1 178 ? -4.019  35.639  -7.438  1.00 22.43 ? 166 GLY D CA  1 
ATOM   5724 C  C   . GLY D 1 178 ? -4.847  34.412  -7.776  1.00 20.87 ? 166 GLY D C   1 
ATOM   5725 O  O   . GLY D 1 178 ? -6.054  34.384  -7.445  1.00 20.51 ? 166 GLY D O   1 
ATOM   5726 N  N   . THR D 1 179 ? -4.219  33.437  -8.410  1.00 19.85 ? 167 THR D N   1 
ATOM   5727 C  CA  . THR D 1 179 ? -4.814  32.145  -8.764  1.00 20.76 ? 167 THR D CA  1 
ATOM   5728 C  C   . THR D 1 179 ? -4.932  31.331  -7.484  1.00 17.84 ? 167 THR D C   1 
ATOM   5729 O  O   . THR D 1 179 ? -3.946  31.236  -6.771  1.00 15.82 ? 167 THR D O   1 
ATOM   5730 C  CB  . THR D 1 179 ? -3.964  31.434  -9.823  1.00 23.50 ? 167 THR D CB  1 
ATOM   5731 O  OG1 . THR D 1 179 ? -3.860  32.342  -10.930 1.00 24.82 ? 167 THR D OG1 1 
ATOM   5732 C  CG2 . THR D 1 179 ? -4.574  30.117  -10.227 1.00 23.09 ? 167 THR D CG2 1 
ATOM   5733 N  N   . HIS D 1 180 ? -6.090  30.732  -7.220  1.00 20.30 ? 168 HIS D N   1 
ATOM   5734 C  CA  . HIS D 1 180 ? -6.310  29.974  -5.962  1.00 19.48 ? 168 HIS D CA  1 
ATOM   5735 C  C   . HIS D 1 180 ? -5.443  28.722  -5.900  1.00 19.65 ? 168 HIS D C   1 
ATOM   5736 O  O   . HIS D 1 180 ? -5.433  27.919  -6.885  1.00 17.78 ? 168 HIS D O   1 
ATOM   5737 C  CB  . HIS D 1 180 ? -7.792  29.619  -5.783  1.00 20.55 ? 168 HIS D CB  1 
ATOM   5738 C  CG  . HIS D 1 180 ? -8.547  30.760  -5.205  1.00 28.42 ? 168 HIS D CG  1 
ATOM   5739 N  ND1 . HIS D 1 180 ? -9.114  31.744  -5.992  1.00 31.06 ? 168 HIS D ND1 1 
ATOM   5740 C  CD2 . HIS D 1 180 ? -8.731  31.140  -3.923  1.00 29.90 ? 168 HIS D CD2 1 
ATOM   5741 C  CE1 . HIS D 1 180 ? -9.660  32.651  -5.207  1.00 31.64 ? 168 HIS D CE1 1 
ATOM   5742 N  NE2 . HIS D 1 180 ? -9.462  32.287  -3.940  1.00 35.91 ? 168 HIS D NE2 1 
ATOM   5743 N  N   . ASN D 1 181 ? -4.764  28.560  -4.759  1.00 15.59 ? 169 ASN D N   1 
ATOM   5744 C  CA  . ASN D 1 181 ? -4.141  27.275  -4.381  1.00 17.19 ? 169 ASN D CA  1 
ATOM   5745 C  C   . ASN D 1 181 ? -5.088  26.646  -3.344  1.00 15.94 ? 169 ASN D C   1 
ATOM   5746 O  O   . ASN D 1 181 ? -6.328  26.706  -3.542  1.00 15.58 ? 169 ASN D O   1 
ATOM   5747 C  CB  . ASN D 1 181 ? -2.709  27.540  -3.910  1.00 18.46 ? 169 ASN D CB  1 
ATOM   5748 C  CG  . ASN D 1 181 ? -1.880  26.274  -3.901  1.00 21.48 ? 169 ASN D CG  1 
ATOM   5749 O  OD1 . ASN D 1 181 ? -1.918  25.534  -2.937  1.00 20.22 ? 169 ASN D OD1 1 
ATOM   5750 N  ND2 . ASN D 1 181 ? -1.143  25.984  -4.969  1.00 24.73 ? 169 ASN D ND2 1 
ATOM   5751 N  N   . TYR D 1 182 ? -4.554  26.060  -2.283  1.00 15.53 ? 170 TYR D N   1 
ATOM   5752 C  CA  . TYR D 1 182 ? -5.436  25.254  -1.396  1.00 14.68 ? 170 TYR D CA  1 
ATOM   5753 C  C   . TYR D 1 182 ? -6.328  26.164  -0.566  1.00 15.76 ? 170 TYR D C   1 
ATOM   5754 O  O   . TYR D 1 182 ? -6.070  27.365  -0.360  1.00 14.70 ? 170 TYR D O   1 
ATOM   5755 C  CB  . TYR D 1 182 ? -4.668  24.262  -0.537  1.00 16.21 ? 170 TYR D CB  1 
ATOM   5756 C  CG  . TYR D 1 182 ? -3.818  24.797  0.587   1.00 14.87 ? 170 TYR D CG  1 
ATOM   5757 C  CD1 . TYR D 1 182 ? -4.371  25.198  1.787   1.00 14.63 ? 170 TYR D CD1 1 
ATOM   5758 C  CD2 . TYR D 1 182 ? -2.436  24.793  0.500   1.00 14.57 ? 170 TYR D CD2 1 
ATOM   5759 C  CE1 . TYR D 1 182 ? -3.571  25.571  2.853   1.00 16.44 ? 170 TYR D CE1 1 
ATOM   5760 C  CE2 . TYR D 1 182 ? -1.633  25.143  1.555   1.00 15.34 ? 170 TYR D CE2 1 
ATOM   5761 C  CZ  . TYR D 1 182 ? -2.196  25.547  2.750   1.00 15.90 ? 170 TYR D CZ  1 
ATOM   5762 O  OH  . TYR D 1 182 ? -1.397  25.933  3.805   1.00 16.18 ? 170 TYR D OH  1 
ATOM   5763 N  N   . MET D 1 183 ? -7.424  25.567  -0.122  1.00 16.34 ? 171 MET D N   1 
ATOM   5764 C  CA  . MET D 1 183 ? -8.383  26.214  0.801   1.00 16.23 ? 171 MET D CA  1 
ATOM   5765 C  C   . MET D 1 183 ? -8.869  25.130  1.761   1.00 15.53 ? 171 MET D C   1 
ATOM   5766 O  O   . MET D 1 183 ? -9.286  24.032  1.282   1.00 14.97 ? 171 MET D O   1 
ATOM   5767 C  CB  . MET D 1 183 ? -9.580  26.801  0.056   1.00 16.84 ? 171 MET D CB  1 
ATOM   5768 C  CG  . MET D 1 183 ? -10.434 27.708  0.966   1.00 18.87 ? 171 MET D CG  1 
ATOM   5769 S  SD  . MET D 1 183 ? -11.827 28.480  0.134   1.00 21.32 ? 171 MET D SD  1 
ATOM   5770 C  CE  . MET D 1 183 ? -12.754 26.998  -0.265  1.00 22.44 ? 171 MET D CE  1 
ATOM   5771 N  N   . ILE D 1 184 ? -8.696  25.354  3.066   1.00 15.16 ? 172 ILE D N   1 
ATOM   5772 C  CA  . ILE D 1 184 ? -9.013  24.311  4.084   1.00 15.37 ? 172 ILE D CA  1 
ATOM   5773 C  C   . ILE D 1 184 ? -9.855  24.944  5.179   1.00 14.18 ? 172 ILE D C   1 
ATOM   5774 O  O   . ILE D 1 184 ? -9.833  26.230  5.333   1.00 14.47 ? 172 ILE D O   1 
ATOM   5775 C  CB  . ILE D 1 184 ? -7.729  23.664  4.664   1.00 15.69 ? 172 ILE D CB  1 
ATOM   5776 C  CG1 . ILE D 1 184 ? -6.812  24.678  5.343   1.00 16.25 ? 172 ILE D CG1 1 
ATOM   5777 C  CG2 . ILE D 1 184 ? -7.016  22.845  3.610   1.00 15.28 ? 172 ILE D CG2 1 
ATOM   5778 C  CD1 . ILE D 1 184 ? -5.641  24.087  6.112   1.00 16.95 ? 172 ILE D CD1 1 
ATOM   5779 N  N   . VAL D 1 185 ? -10.540 24.087  5.939   1.00 13.56 ? 173 VAL D N   1 
ATOM   5780 C  CA  . VAL D 1 185 ? -11.123 24.488  7.233   1.00 15.33 ? 173 VAL D CA  1 
ATOM   5781 C  C   . VAL D 1 185 ? -10.073 24.166  8.295   1.00 15.49 ? 173 VAL D C   1 
ATOM   5782 O  O   . VAL D 1 185 ? -9.821  22.953  8.573   1.00 17.46 ? 173 VAL D O   1 
ATOM   5783 C  CB  . VAL D 1 185 ? -12.492 23.873  7.499   1.00 16.72 ? 173 VAL D CB  1 
ATOM   5784 C  CG1 . VAL D 1 185 ? -13.021 24.307  8.858   1.00 18.58 ? 173 VAL D CG1 1 
ATOM   5785 C  CG2 . VAL D 1 185 ? -13.442 24.225  6.384   1.00 17.91 ? 173 VAL D CG2 1 
ATOM   5786 N  N   . ALA D 1 186 ? -9.448  25.231  8.814   1.00 14.80 ? 174 ALA D N   1 
ATOM   5787 C  CA  . ALA D 1 186 ? -8.211  25.090  9.608   1.00 16.01 ? 174 ALA D CA  1 
ATOM   5788 C  C   . ALA D 1 186 ? -8.445  25.377  11.097  1.00 15.56 ? 174 ALA D C   1 
ATOM   5789 O  O   . ALA D 1 186 ? -9.128  26.360  11.440  1.00 17.10 ? 174 ALA D O   1 
ATOM   5790 C  CB  . ALA D 1 186 ? -7.127  25.963  9.073   1.00 17.05 ? 174 ALA D CB  1 
ATOM   5791 N  N   . THR D 1 187 ? -7.659  24.686  11.890  1.00 15.15 ? 175 THR D N   1 
ATOM   5792 C  CA  . THR D 1 187 ? -7.483  24.849  13.344  1.00 16.15 ? 175 THR D CA  1 
ATOM   5793 C  C   . THR D 1 187 ? -6.063  25.378  13.516  1.00 16.60 ? 175 THR D C   1 
ATOM   5794 O  O   . THR D 1 187 ? -5.175  24.817  12.957  1.00 15.14 ? 175 THR D O   1 
ATOM   5795 C  CB  . THR D 1 187 ? -7.701  23.526  14.086  1.00 17.32 ? 175 THR D CB  1 
ATOM   5796 O  OG1 . THR D 1 187 ? -9.058  23.151  13.883  1.00 16.78 ? 175 THR D OG1 1 
ATOM   5797 C  CG2 . THR D 1 187 ? -7.434  23.678  15.563  1.00 18.37 ? 175 THR D CG2 1 
ATOM   5798 N  N   . ALA D 1 188 ? -5.900  26.549  14.114  1.00 15.06 ? 176 ALA D N   1 
ATOM   5799 C  CA  . ALA D 1 188 ? -4.564  27.144  14.332  1.00 15.98 ? 176 ALA D CA  1 
ATOM   5800 C  C   . ALA D 1 188 ? -4.345  27.320  15.831  1.00 14.92 ? 176 ALA D C   1 
ATOM   5801 O  O   . ALA D 1 188 ? -5.328  27.480  16.563  1.00 15.65 ? 176 ALA D O   1 
ATOM   5802 C  CB  . ALA D 1 188 ? -4.507  28.442  13.569  1.00 16.62 ? 176 ALA D CB  1 
ATOM   5803 N  N   . GLY D 1 189 ? -3.084  27.316  16.258  1.00 15.91 ? 177 GLY D N   1 
ATOM   5804 C  CA  . GLY D 1 189 ? -2.766  27.527  17.681  1.00 18.30 ? 177 GLY D CA  1 
ATOM   5805 C  C   . GLY D 1 189 ? -1.362  28.035  17.828  1.00 20.19 ? 177 GLY D C   1 
ATOM   5806 O  O   . GLY D 1 189 ? -0.543  27.794  16.934  1.00 21.13 ? 177 GLY D O   1 
ATOM   5807 N  N   . TYR D 1 190 ? -1.103  28.829  18.882  1.00 22.69 ? 178 TYR D N   1 
ATOM   5808 C  CA  . TYR D 1 190 ? 0.248   29.364  19.170  1.00 22.34 ? 178 TYR D CA  1 
ATOM   5809 C  C   . TYR D 1 190 ? 0.365   29.435  20.683  1.00 20.62 ? 178 TYR D C   1 
ATOM   5810 O  O   . TYR D 1 190 ? -0.553  29.992  21.285  1.00 19.57 ? 178 TYR D O   1 
ATOM   5811 C  CB  . TYR D 1 190 ? 0.478   30.730  18.521  1.00 27.25 ? 178 TYR D CB  1 
ATOM   5812 C  CG  . TYR D 1 190 ? 1.868   31.268  18.769  1.00 31.44 ? 178 TYR D CG  1 
ATOM   5813 C  CD1 . TYR D 1 190 ? 2.998   30.609  18.305  1.00 32.82 ? 178 TYR D CD1 1 
ATOM   5814 C  CD2 . TYR D 1 190 ? 2.067   32.387  19.556  1.00 31.52 ? 178 TYR D CD2 1 
ATOM   5815 C  CE1 . TYR D 1 190 ? 4.276   31.098  18.541  1.00 35.14 ? 178 TYR D CE1 1 
ATOM   5816 C  CE2 . TYR D 1 190 ? 3.329   32.902  19.779  1.00 34.93 ? 178 TYR D CE2 1 
ATOM   5817 C  CZ  . TYR D 1 190 ? 4.446   32.266  19.263  1.00 35.35 ? 178 TYR D CZ  1 
ATOM   5818 O  OH  . TYR D 1 190 ? 5.698   32.760  19.533  1.00 36.57 ? 178 TYR D OH  1 
ATOM   5819 N  N   . GLN D 1 191 ? 1.432   28.855  21.240  1.00 21.95 ? 179 GLN D N   1 
ATOM   5820 C  CA  . GLN D 1 191 ? 1.783   28.865  22.681  1.00 21.79 ? 179 GLN D CA  1 
ATOM   5821 C  C   . GLN D 1 191 ? 0.513   28.599  23.503  1.00 22.14 ? 179 GLN D C   1 
ATOM   5822 O  O   . GLN D 1 191 ? 0.135   29.396  24.391  1.00 20.81 ? 179 GLN D O   1 
ATOM   5823 C  CB  . GLN D 1 191 ? 2.584   30.139  22.975  1.00 25.39 ? 179 GLN D CB  1 
ATOM   5824 C  CG  . GLN D 1 191 ? 3.921   30.162  22.223  1.00 29.38 ? 179 GLN D CG  1 
ATOM   5825 C  CD  . GLN D 1 191 ? 4.990   30.986  22.914  1.00 33.25 ? 179 GLN D CD  1 
ATOM   5826 O  OE1 . GLN D 1 191 ? 4.689   31.851  23.731  1.00 38.10 ? 179 GLN D OE1 1 
ATOM   5827 N  NE2 . GLN D 1 191 ? 6.254   30.742  22.579  1.00 31.62 ? 179 GLN D NE2 1 
ATOM   5828 N  N   . SER D 1 192 ? -0.150  27.483  23.190  1.00 20.72 ? 180 SER D N   1 
ATOM   5829 C  CA  . SER D 1 192 ? -1.420  27.112  23.834  1.00 19.69 ? 180 SER D CA  1 
ATOM   5830 C  C   . SER D 1 192 ? -1.527  25.588  23.885  1.00 17.30 ? 180 SER D C   1 
ATOM   5831 O  O   . SER D 1 192 ? -0.572  24.899  23.466  1.00 16.96 ? 180 SER D O   1 
ATOM   5832 C  CB  . SER D 1 192 ? -2.588  27.759  23.151  1.00 20.51 ? 180 SER D CB  1 
ATOM   5833 O  OG  . SER D 1 192 ? -2.762  27.237  21.843  1.00 19.28 ? 180 SER D OG  1 
ATOM   5834 N  N   . SER D 1 193 ? -2.649  25.140  24.421  1.00 18.96 ? 181 SER D N   1 
ATOM   5835 C  CA  . SER D 1 193 ? -3.082  23.720  24.458  1.00 19.75 ? 181 SER D CA  1 
ATOM   5836 C  C   . SER D 1 193 ? -4.519  23.692  23.942  1.00 19.26 ? 181 SER D C   1 
ATOM   5837 O  O   . SER D 1 193 ? -5.188  24.750  23.911  1.00 21.59 ? 181 SER D O   1 
ATOM   5838 C  CB  . SER D 1 193 ? -2.952  23.153  25.836  1.00 22.01 ? 181 SER D CB  1 
ATOM   5839 O  OG  . SER D 1 193 ? -1.589  23.194  26.261  1.00 23.68 ? 181 SER D OG  1 
ATOM   5840 N  N   . GLY D 1 194 ? -5.006  22.517  23.562  1.00 20.08 ? 182 GLY D N   1 
ATOM   5841 C  CA  . GLY D 1 194 ? -6.374  22.406  23.068  1.00 18.82 ? 182 GLY D CA  1 
ATOM   5842 C  C   . GLY D 1 194 ? -6.612  21.081  22.387  1.00 20.37 ? 182 GLY D C   1 
ATOM   5843 O  O   . GLY D 1 194 ? -5.675  20.317  22.200  1.00 19.47 ? 182 GLY D O   1 
ATOM   5844 N  N   . SER D 1 195 ? -7.848  20.896  21.958  1.00 21.52 ? 183 SER D N   1 
ATOM   5845 C  CA  . SER D 1 195 ? -8.227  19.834  21.021  1.00 21.93 ? 183 SER D CA  1 
ATOM   5846 C  C   . SER D 1 195 ? -9.324  20.380  20.129  1.00 21.03 ? 183 SER D C   1 
ATOM   5847 O  O   . SER D 1 195 ? -9.981  21.366  20.487  1.00 23.02 ? 183 SER D O   1 
ATOM   5848 C  CB  . SER D 1 195 ? -8.646  18.589  21.754  1.00 22.34 ? 183 SER D CB  1 
ATOM   5849 O  OG  . SER D 1 195 ? -9.799  18.842  22.509  1.00 25.34 ? 183 SER D OG  1 
ATOM   5850 N  N   . ALA D 1 196 ? -9.393  19.862  18.919  1.00 20.68 ? 184 ALA D N   1 
ATOM   5851 C  CA  . ALA D 1 196 ? -10.495 20.155  17.990  1.00 19.31 ? 184 ALA D CA  1 
ATOM   5852 C  C   . ALA D 1 196 ? -10.707 18.922  17.127  1.00 20.69 ? 184 ALA D C   1 
ATOM   5853 O  O   . ALA D 1 196 ? -9.768  18.148  16.878  1.00 22.38 ? 184 ALA D O   1 
ATOM   5854 C  CB  . ALA D 1 196 ? -10.195 21.382  17.146  1.00 21.20 ? 184 ALA D CB  1 
ATOM   5855 N  N   . SER D 1 197 ? -11.943 18.751  16.715  1.00 21.54 ? 185 SER D N   1 
ATOM   5856 C  CA  . SER D 1 197 ? -12.333 17.695  15.776  1.00 22.53 ? 185 SER D CA  1 
ATOM   5857 C  C   . SER D 1 197 ? -13.305 18.353  14.812  1.00 21.26 ? 185 SER D C   1 
ATOM   5858 O  O   . SER D 1 197 ? -14.365 18.824  15.260  1.00 20.38 ? 185 SER D O   1 
ATOM   5859 C  CB  . SER D 1 197 ? -12.901 16.495  16.528  1.00 27.08 ? 185 SER D CB  1 
ATOM   5860 O  OG  . SER D 1 197 ? -13.194 15.434  15.635  1.00 33.29 ? 185 SER D OG  1 
ATOM   5861 N  N   . ILE D 1 198 ? -12.930 18.414  13.538  1.00 21.12 ? 186 ILE D N   1 
ATOM   5862 C  CA  . ILE D 1 198 ? -13.685 19.149  12.496  1.00 20.80 ? 186 ILE D CA  1 
ATOM   5863 C  C   . ILE D 1 198 ? -13.987 18.237  11.320  1.00 20.48 ? 186 ILE D C   1 
ATOM   5864 O  O   . ILE D 1 198 ? -13.081 17.508  10.910  1.00 22.29 ? 186 ILE D O   1 
ATOM   5865 C  CB  . ILE D 1 198 ? -12.856 20.371  12.052  1.00 21.47 ? 186 ILE D CB  1 
ATOM   5866 C  CG1 . ILE D 1 198 ? -12.605 21.321  13.228  1.00 24.54 ? 186 ILE D CG1 1 
ATOM   5867 C  CG2 . ILE D 1 198 ? -13.513 21.025  10.865  1.00 20.85 ? 186 ILE D CG2 1 
ATOM   5868 C  CD1 . ILE D 1 198 ? -13.869 21.929  13.812  1.00 26.39 ? 186 ILE D CD1 1 
ATOM   5869 N  N   . THR D 1 199 ? -15.206 18.323  10.795  1.00 21.06 ? 187 THR D N   1 
ATOM   5870 C  CA  . THR D 1 199 ? -15.662 17.608  9.576   1.00 23.98 ? 187 THR D CA  1 
ATOM   5871 C  C   . THR D 1 199 ? -16.077 18.642  8.542   1.00 22.71 ? 187 THR D C   1 
ATOM   5872 O  O   . THR D 1 199 ? -16.943 19.435  8.819   1.00 22.12 ? 187 THR D O   1 
ATOM   5873 C  CB  . THR D 1 199 ? -16.775 16.596  9.863   1.00 25.36 ? 187 THR D CB  1 
ATOM   5874 O  OG1 . THR D 1 199 ? -16.300 15.722  10.887  1.00 25.85 ? 187 THR D OG1 1 
ATOM   5875 C  CG2 . THR D 1 199 ? -17.159 15.801  8.636   1.00 26.06 ? 187 THR D CG2 1 
ATOM   5876 N  N   . VAL D 1 200 ? -15.344 18.664  7.440   1.00 21.38 ? 188 VAL D N   1 
ATOM   5877 C  CA  . VAL D 1 200 ? -15.666 19.375  6.181   1.00 23.48 ? 188 VAL D CA  1 
ATOM   5878 C  C   . VAL D 1 200 ? -16.607 18.489  5.345   1.00 23.71 ? 188 VAL D C   1 
ATOM   5879 O  O   . VAL D 1 200 ? -16.390 17.252  5.282   1.00 24.26 ? 188 VAL D O   1 
ATOM   5880 C  CB  . VAL D 1 200 ? -14.335 19.691  5.481   1.00 25.74 ? 188 VAL D CB  1 
ATOM   5881 C  CG1 . VAL D 1 200 ? -14.509 20.248  4.094   1.00 31.11 ? 188 VAL D CG1 1 
ATOM   5882 C  CG2 . VAL D 1 200 ? -13.472 20.615  6.336   1.00 27.57 ? 188 VAL D CG2 1 
ATOM   5883 N  N   . GLN D 1 201 ? -17.610 19.088  4.720   1.00 28.82 ? 189 GLN D N   1 
ATOM   5884 C  CA  . GLN D 1 201 ? -18.554 18.397  3.796   1.00 31.55 ? 189 GLN D CA  1 
ATOM   5885 C  C   . GLN D 1 201 ? -18.139 18.605  2.337   1.00 35.97 ? 189 GLN D C   1 
ATOM   5886 O  O   . GLN D 1 201 ? -17.072 19.121  2.009   1.00 37.40 ? 189 GLN D O   1 
ATOM   5887 C  CB  . GLN D 1 201 ? -19.960 18.927  4.034   1.00 34.86 ? 189 GLN D CB  1 
ATOM   5888 C  CG  . GLN D 1 201 ? -20.401 18.716  5.468   1.00 37.41 ? 189 GLN D CG  1 
ATOM   5889 C  CD  . GLN D 1 201 ? -21.885 18.870  5.669   1.00 43.88 ? 189 GLN D CD  1 
ATOM   5890 O  OE1 . GLN D 1 201 ? -22.637 19.177  4.739   1.00 50.61 ? 189 GLN D OE1 1 
ATOM   5891 N  NE2 . GLN D 1 201 ? -22.317 18.650  6.903   1.00 48.37 ? 189 GLN D NE2 1 
HETATM 5892 O  O1  . XYP E 2 .   ? 20.881  -3.054  26.255  1.00 16.41 ? 1   XYP E O1  1 
HETATM 5893 C  C1  . XYP E 2 .   ? 21.203  -4.407  26.320  1.00 14.46 ? 1   XYP E C1  1 
HETATM 5894 C  C2  . XYP E 2 .   ? 21.846  -4.833  25.000  1.00 14.52 ? 1   XYP E C2  1 
HETATM 5895 C  C3  . XYP E 2 .   ? 22.442  -6.243  25.090  1.00 14.30 ? 1   XYP E C3  1 
HETATM 5896 C  C4  . XYP E 2 .   ? 23.286  -6.352  26.358  1.00 14.47 ? 1   XYP E C4  1 
HETATM 5897 C  C5  . XYP E 2 .   ? 22.505  -5.895  27.575  1.00 14.53 ? 1   XYP E C5  1 
HETATM 5898 O  O2  . XYP E 2 .   ? 20.909  -4.699  23.926  1.00 14.30 ? 1   XYP E O2  1 
HETATM 5899 O  O3  . XYP E 2 .   ? 23.276  -6.520  23.944  1.00 14.97 ? 1   XYP E O3  1 
HETATM 5900 O  O4  . XYP E 2 .   ? 23.548  -7.872  26.480  1.00 17.96 ? 1   XYP E O4  1 
HETATM 5901 O  O5  . XYP E 2 .   ? 22.149  -4.533  27.405  1.00 15.68 ? 1   XYP E O5  1 
HETATM 5902 C  C1  . XYP E 2 .   ? 24.674  -8.152  27.235  1.00 20.47 ? 2   XYP E C1  1 
HETATM 5903 C  C2  . XYP E 2 .   ? 24.406  -9.565  27.745  1.00 23.74 ? 2   XYP E C2  1 
HETATM 5904 C  C3  . XYP E 2 .   ? 25.594  -10.085 28.520  1.00 28.91 ? 2   XYP E C3  1 
HETATM 5905 C  C4  . XYP E 2 .   ? 26.833  -9.961  27.650  1.00 30.13 ? 2   XYP E C4  1 
HETATM 5906 C  C5  . XYP E 2 .   ? 27.001  -8.510  27.219  1.00 26.50 ? 2   XYP E C5  1 
HETATM 5907 O  O2  . XYP E 2 .   ? 23.264  -9.586  28.596  1.00 25.91 ? 2   XYP E O2  1 
HETATM 5908 O  O3  . XYP E 2 .   ? 25.353  -11.444 28.869  1.00 34.28 ? 2   XYP E O3  1 
HETATM 5909 O  O4  . XYP E 2 .   ? 27.971  -10.393 28.405  1.00 35.34 ? 2   XYP E O4  1 
HETATM 5910 O  O5  . XYP E 2 .   ? 25.858  -8.084  26.461  1.00 22.64 ? 2   XYP E O5  1 
HETATM 5911 O  O1  . XYP F 3 .   ? -0.221  0.802   40.891  1.00 28.28 ? 1   XYP F O1  1 
HETATM 5912 C  C1  . XYP F 3 .   ? 0.628   1.642   41.477  1.00 24.79 ? 1   XYP F C1  1 
HETATM 5913 C  C2  . XYP F 3 .   ? 1.925   1.154   42.058  1.00 20.82 ? 1   XYP F C2  1 
HETATM 5914 C  C3  . XYP F 3 .   ? 2.016   2.005   43.294  1.00 19.35 ? 1   XYP F C3  1 
HETATM 5915 C  C4  . XYP F 3 .   ? 1.661   3.488   43.037  1.00 17.97 ? 1   XYP F C4  1 
HETATM 5916 C  C5  . XYP F 3 .   ? 0.866   3.815   41.766  1.00 21.44 ? 1   XYP F C5  1 
HETATM 5917 O  O2  . XYP F 3 .   ? 1.939   -0.253  42.327  1.00 20.27 ? 1   XYP F O2  1 
HETATM 5918 O  O3  . XYP F 3 .   ? 3.330   1.888   43.853  1.00 18.46 ? 1   XYP F O3  1 
HETATM 5919 O  O4  . XYP F 3 .   ? 0.833   3.866   44.137  1.00 17.64 ? 1   XYP F O4  1 
HETATM 5920 O  O5  . XYP F 3 .   ? 0.945   2.791   40.778  1.00 22.22 ? 1   XYP F O5  1 
HETATM 5921 C  C1  . XYP F 3 .   ? 0.732   5.320   44.531  1.00 15.98 ? 2   XYP F C1  1 
HETATM 5922 C  C2  . XYP F 3 .   ? -0.639  5.688   44.985  1.00 14.43 ? 2   XYP F C2  1 
HETATM 5923 C  C3  . XYP F 3 .   ? -0.647  7.102   45.559  1.00 16.29 ? 2   XYP F C3  1 
HETATM 5924 C  C4  . XYP F 3 .   ? 0.460   7.253   46.588  1.00 16.08 ? 2   XYP F C4  1 
HETATM 5925 C  C5  . XYP F 3 .   ? 1.776   6.767   46.024  1.00 15.98 ? 2   XYP F C5  1 
HETATM 5926 O  O2  . XYP F 3 .   ? -1.510  5.630   43.855  1.00 14.71 ? 2   XYP F O2  1 
HETATM 5927 O  O3  . XYP F 3 .   ? -1.890  7.401   46.164  1.00 15.14 ? 2   XYP F O3  1 
HETATM 5928 O  O4  . XYP F 3 .   ? 0.599   8.632   46.909  1.00 18.16 ? 2   XYP F O4  1 
HETATM 5929 O  O5  . XYP F 3 .   ? 1.667   5.400   45.632  1.00 16.60 ? 2   XYP F O5  1 
HETATM 5930 C  C1  . XYP F 3 .   ? 1.384   8.979   48.112  1.00 24.34 ? 3   XYP F C1  1 
HETATM 5931 C  C2  . XYP F 3 .   ? 1.798   10.441  47.913  1.00 27.37 ? 3   XYP F C2  1 
HETATM 5932 C  C3  . XYP F 3 .   ? 2.402   10.976  49.196  1.00 28.77 ? 3   XYP F C3  1 
HETATM 5933 C  C4  . XYP F 3 .   ? 1.447   10.726  50.352  1.00 25.99 ? 3   XYP F C4  1 
HETATM 5934 C  C5  . XYP F 3 .   ? 0.973   9.278   50.387  1.00 24.91 ? 3   XYP F C5  1 
HETATM 5935 O  O2  . XYP F 3 .   ? 2.748   10.547  46.864  1.00 30.46 ? 3   XYP F O2  1 
HETATM 5936 O  O3  . XYP F 3 .   ? 2.638   12.384  49.069  1.00 32.12 ? 3   XYP F O3  1 
HETATM 5937 O  O4  . XYP F 3 .   ? 2.120   11.038  51.571  1.00 29.57 ? 3   XYP F O4  1 
HETATM 5938 O  O5  . XYP F 3 .   ? 0.382   8.923   49.133  1.00 23.17 ? 3   XYP F O5  1 
HETATM 5939 O  O1  . XYP G 3 .   ? 10.733  36.930  27.576  1.00 34.72 ? 1   XYP G O1  1 
HETATM 5940 C  C1  . XYP G 3 .   ? 11.610  37.840  28.139  1.00 30.96 ? 1   XYP G C1  1 
HETATM 5941 C  C2  . XYP G 3 .   ? 12.819  37.769  27.273  1.00 28.46 ? 1   XYP G C2  1 
HETATM 5942 C  C3  . XYP G 3 .   ? 13.817  38.897  27.457  1.00 23.74 ? 1   XYP G C3  1 
HETATM 5943 C  C4  . XYP G 3 .   ? 13.179  40.248  27.784  1.00 24.31 ? 1   XYP G C4  1 
HETATM 5944 C  C5  . XYP G 3 .   ? 11.889  40.142  28.577  1.00 27.39 ? 1   XYP G C5  1 
HETATM 5945 O  O2  . XYP G 3 .   ? 13.528  36.566  27.517  1.00 25.81 ? 1   XYP G O2  1 
HETATM 5946 O  O3  . XYP G 3 .   ? 14.556  38.964  26.232  1.00 24.89 ? 1   XYP G O3  1 
HETATM 5947 O  O4  . XYP G 3 .   ? 14.109  40.944  28.598  1.00 21.31 ? 1   XYP G O4  1 
HETATM 5948 O  O5  . XYP G 3 .   ? 11.035  39.117  28.061  1.00 29.05 ? 1   XYP G O5  1 
HETATM 5949 C  C1  . XYP G 3 .   ? 13.958  42.421  28.621  1.00 18.62 ? 2   XYP G C1  1 
HETATM 5950 C  C2  . XYP G 3 .   ? 14.113  42.871  30.033  1.00 18.98 ? 2   XYP G C2  1 
HETATM 5951 C  C3  . XYP G 3 .   ? 14.232  44.390  30.064  1.00 16.85 ? 2   XYP G C3  1 
HETATM 5952 C  C4  . XYP G 3 .   ? 15.280  44.854  29.066  1.00 17.58 ? 2   XYP G C4  1 
HETATM 5953 C  C5  . XYP G 3 .   ? 15.106  44.222  27.705  1.00 18.07 ? 2   XYP G C5  1 
HETATM 5954 O  O2  . XYP G 3 .   ? 13.002  42.467  30.820  1.00 20.15 ? 2   XYP G O2  1 
HETATM 5955 O  O3  . XYP G 3 .   ? 14.651  44.783  31.364  1.00 17.57 ? 2   XYP G O3  1 
HETATM 5956 O  O4  . XYP G 3 .   ? 15.206  46.278  28.966  1.00 19.61 ? 2   XYP G O4  1 
HETATM 5957 O  O5  . XYP G 3 .   ? 15.092  42.796  27.843  1.00 18.28 ? 2   XYP G O5  1 
HETATM 5958 C  C1  . XYP G 3 .   ? 16.586  46.910  28.664  1.00 27.43 ? 3   XYP G C1  1 
HETATM 5959 C  C2  . XYP G 3 .   ? 16.112  48.299  28.287  1.00 28.87 ? 3   XYP G C2  1 
HETATM 5960 C  C3  . XYP G 3 .   ? 17.296  49.257  28.191  1.00 32.71 ? 3   XYP G C3  1 
HETATM 5961 C  C4  . XYP G 3 .   ? 18.127  49.203  29.471  1.00 32.80 ? 3   XYP G C4  1 
HETATM 5962 C  C5  . XYP G 3 .   ? 18.492  47.754  29.740  1.00 30.52 ? 3   XYP G C5  1 
HETATM 5963 O  O2  . XYP G 3 .   ? 15.375  48.190  27.073  1.00 29.37 ? 3   XYP G O2  1 
HETATM 5964 O  O3  . XYP G 3 .   ? 16.781  50.567  27.960  1.00 35.53 ? 3   XYP G O3  1 
HETATM 5965 O  O4  . XYP G 3 .   ? 19.340  49.966  29.381  1.00 32.53 ? 3   XYP G O4  1 
HETATM 5966 O  O5  . XYP G 3 .   ? 17.310  46.956  29.862  1.00 29.49 ? 3   XYP G O5  1 
HETATM 5967 O  O1  . XYP H 2 .   ? 2.114   29.367  6.484   1.00 19.66 ? 1   XYP H O1  1 
HETATM 5968 C  C1  . XYP H 2 .   ? 2.587   28.129  6.153   1.00 19.94 ? 1   XYP H C1  1 
HETATM 5969 C  C2  . XYP H 2 .   ? 1.518   27.295  5.406   1.00 20.87 ? 1   XYP H C2  1 
HETATM 5970 C  C3  . XYP H 2 .   ? 2.081   26.003  4.830   1.00 19.95 ? 1   XYP H C3  1 
HETATM 5971 C  C4  . XYP H 2 .   ? 3.400   26.275  4.121   1.00 20.85 ? 1   XYP H C4  1 
HETATM 5972 C  C5  . XYP H 2 .   ? 4.319   27.016  5.065   1.00 20.77 ? 1   XYP H C5  1 
HETATM 5973 O  O2  . XYP H 2 .   ? 0.405   26.950  6.245   1.00 20.41 ? 1   XYP H O2  1 
HETATM 5974 O  O3  . XYP H 2 .   ? 1.175   25.421  3.899   1.00 21.66 ? 1   XYP H O3  1 
HETATM 5975 O  O4  . XYP H 2 .   ? 3.962   24.900  3.884   1.00 20.85 ? 1   XYP H O4  1 
HETATM 5976 O  O5  . XYP H 2 .   ? 3.759   28.298  5.356   1.00 19.13 ? 1   XYP H O5  1 
HETATM 5977 C  C1  . XYP H 2 .   ? 5.029   24.840  2.987   1.00 25.40 ? 2   XYP H C1  1 
HETATM 5978 C  C2  . XYP H 2 .   ? 5.868   23.645  3.396   1.00 28.54 ? 2   XYP H C2  1 
HETATM 5979 C  C3  . XYP H 2 .   ? 6.909   23.275  2.349   1.00 34.21 ? 2   XYP H C3  1 
HETATM 5980 C  C4  . XYP H 2 .   ? 6.297   23.269  0.955   1.00 31.98 ? 2   XYP H C4  1 
HETATM 5981 C  C5  . XYP H 2 .   ? 5.531   24.556  0.700   1.00 31.36 ? 2   XYP H C5  1 
HETATM 5982 O  O2  . XYP H 2 .   ? 6.526   23.911  4.629   1.00 32.97 ? 2   XYP H O2  1 
HETATM 5983 O  O3  . XYP H 2 .   ? 7.414   21.973  2.660   1.00 34.10 ? 2   XYP H O3  1 
HETATM 5984 O  O4  . XYP H 2 .   ? 7.321   23.146  -0.029  1.00 38.14 ? 2   XYP H O4  1 
HETATM 5985 O  O5  . XYP H 2 .   ? 4.492   24.714  1.676   1.00 26.96 ? 2   XYP H O5  1 
HETATM 5986 ZN ZN  . ZN  I 4 .   ? 5.105   8.110   5.207   1.00 32.62 ? 201 ZN  A ZN  1 
HETATM 5987 ZN ZN  . ZN  J 4 .   ? 4.569   5.412   14.418  1.00 28.10 ? 202 ZN  A ZN  1 
HETATM 5988 O  O1  . XYP K 5 .   ? 17.599  0.069   24.903  1.00 30.21 ? 203 XYP A O1  1 
HETATM 5989 C  C1  . XYP K 5 .   ? 18.203  -0.753  25.766  1.00 25.90 ? 203 XYP A C1  1 
HETATM 5990 C  C2  . XYP K 5 .   ? 18.601  -0.319  27.141  1.00 21.49 ? 203 XYP A C2  1 
HETATM 5991 C  C3  . XYP K 5 .   ? 19.835  -1.162  27.392  1.00 20.02 ? 203 XYP A C3  1 
HETATM 5992 C  C4  . XYP K 5 .   ? 19.603  -2.661  27.102  1.00 20.44 ? 203 XYP A C4  1 
HETATM 5993 C  C5  . XYP K 5 .   ? 18.687  -2.936  25.910  1.00 22.98 ? 203 XYP A C5  1 
HETATM 5994 O  O2  . XYP K 5 .   ? 18.793  1.104   27.239  1.00 21.49 ? 203 XYP A O2  1 
HETATM 5995 O  O3  . XYP K 5 .   ? 20.215  -1.056  28.759  1.00 21.22 ? 203 XYP A O3  1 
HETATM 5996 O  O5  . XYP K 5 .   ? 17.591  -2.039  25.923  1.00 26.70 ? 203 XYP A O5  1 
HETATM 5997 ZN ZN  . ZN  L 4 .   ? -17.717 -7.216  25.221  1.00 39.05 ? 300 ZN  B ZN  1 
HETATM 5998 ZN ZN  . ZN  M 4 .   ? -9.046  -4.611  25.989  1.00 40.69 ? 301 ZN  B ZN  1 
HETATM 5999 ZN ZN  . ZN  N 4 .   ? -2.984  25.125  45.227  1.00 36.68 ? 300 ZN  C ZN  1 
HETATM 6000 ZN ZN  . ZN  O 4 .   ? -1.657  27.827  36.235  1.00 28.72 ? 301 ZN  C ZN  1 
HETATM 6001 O  O1  . XYP P 5 .   ? -0.497  32.275  9.563   1.00 34.25 ? 201 XYP D O1  1 
HETATM 6002 C  C1  . XYP P 5 .   ? 0.514   31.492  9.073   1.00 27.92 ? 201 XYP D C1  1 
HETATM 6003 C  C2  . XYP P 5 .   ? 1.781   32.197  8.718   1.00 22.90 ? 201 XYP D C2  1 
HETATM 6004 C  C3  . XYP P 5 .   ? 2.399   31.389  7.590   1.00 23.61 ? 201 XYP D C3  1 
HETATM 6005 C  C4  . XYP P 5 .   ? 2.453   29.902  7.957   1.00 21.98 ? 201 XYP D C4  1 
HETATM 6006 C  C5  . XYP P 5 .   ? 1.254   29.392  8.754   1.00 22.35 ? 201 XYP D C5  1 
HETATM 6007 O  O2  . XYP P 5 .   ? 1.495   33.566  8.417   1.00 23.81 ? 201 XYP D O2  1 
HETATM 6008 O  O3  . XYP P 5 .   ? 3.725   31.839  7.325   1.00 24.96 ? 201 XYP D O3  1 
HETATM 6009 O  O5  . XYP P 5 .   ? 0.900   30.322  9.774   1.00 25.68 ? 201 XYP D O5  1 
HETATM 6010 O  O   . HOH Q 6 .   ? 34.817  -1.374  26.741  1.00 23.67 ? 301 HOH A O   1 
HETATM 6011 O  O   . HOH Q 6 .   ? 3.583   -11.587 7.096   1.00 24.52 ? 302 HOH A O   1 
HETATM 6012 O  O   . HOH Q 6 .   ? 4.097   8.220   6.401   1.00 24.59 ? 303 HOH A O   1 
HETATM 6013 O  O   . HOH Q 6 .   ? 4.507   10.086  4.433   1.00 28.30 ? 304 HOH A O   1 
HETATM 6014 O  O   . HOH Q 6 .   ? 6.063   -17.073 8.257   1.00 32.19 ? 305 HOH A O   1 
HETATM 6015 O  O   . HOH Q 6 .   ? 3.090   7.794   24.266  1.00 30.77 ? 306 HOH A O   1 
HETATM 6016 O  O   . HOH Q 6 .   ? 26.569  18.459  22.326  1.00 40.53 ? 307 HOH A O   1 
HETATM 6017 O  O   . HOH Q 6 .   ? 21.995  -4.175  4.350   1.00 25.98 ? 308 HOH A O   1 
HETATM 6018 O  O   . HOH Q 6 .   ? 0.870   -7.294  25.838  1.00 36.61 ? 309 HOH A O   1 
HETATM 6019 O  O   . HOH Q 6 .   ? 0.978   -13.203 27.726  1.00 40.28 ? 310 HOH A O   1 
HETATM 6020 O  O   . HOH Q 6 .   ? 4.785   -9.583  11.999  1.00 26.31 ? 311 HOH A O   1 
HETATM 6021 O  O   . HOH Q 6 .   ? 14.594  -1.018  17.843  1.00 24.23 ? 312 HOH A O   1 
HETATM 6022 O  O   . HOH Q 6 .   ? 33.627  6.210   16.235  1.00 34.35 ? 313 HOH A O   1 
HETATM 6023 O  O   . HOH Q 6 .   ? 16.645  -20.569 9.298   1.00 50.75 ? 314 HOH A O   1 
HETATM 6024 O  O   . HOH Q 6 .   ? 23.545  -8.901  23.111  1.00 15.24 ? 315 HOH A O   1 
HETATM 6025 O  O   . HOH Q 6 .   ? 17.910  -11.085 30.997  1.00 36.72 ? 316 HOH A O   1 
HETATM 6026 O  O   . HOH Q 6 .   ? 20.233  -16.961 27.868  1.00 33.05 ? 317 HOH A O   1 
HETATM 6027 O  O   . HOH Q 6 .   ? 26.509  -14.225 23.685  1.00 35.84 ? 318 HOH A O   1 
HETATM 6028 O  O   . HOH Q 6 .   ? 18.314  6.913   7.574   1.00 17.44 ? 319 HOH A O   1 
HETATM 6029 O  O   . HOH Q 6 .   ? 34.265  -1.231  12.705  1.00 27.83 ? 320 HOH A O   1 
HETATM 6030 O  O   . HOH Q 6 .   ? 7.643   14.127  8.720   1.00 39.31 ? 321 HOH A O   1 
HETATM 6031 O  O   . HOH Q 6 .   ? 27.704  -10.264 9.730   1.00 28.03 ? 322 HOH A O   1 
HETATM 6032 O  O   . HOH Q 6 .   ? 14.139  -4.550  32.461  1.00 38.31 ? 323 HOH A O   1 
HETATM 6033 O  O   . HOH Q 6 .   ? 32.876  2.956   10.918  1.00 34.00 ? 324 HOH A O   1 
HETATM 6034 O  O   . HOH Q 6 .   ? 4.504   0.016   29.997  1.00 26.60 ? 325 HOH A O   1 
HETATM 6035 O  O   . HOH Q 6 .   ? 5.706   -11.621 10.495  1.00 35.56 ? 326 HOH A O   1 
HETATM 6036 O  O   . HOH Q 6 .   ? 22.586  17.479  11.325  1.00 29.84 ? 327 HOH A O   1 
HETATM 6037 O  O   . HOH Q 6 .   ? 35.111  -1.343  15.574  1.00 29.78 ? 328 HOH A O   1 
HETATM 6038 O  O   . HOH Q 6 .   ? 29.407  -11.893 13.082  1.00 29.51 ? 329 HOH A O   1 
HETATM 6039 O  O   . HOH Q 6 .   ? 3.638   6.062   16.178  1.00 26.60 ? 330 HOH A O   1 
HETATM 6040 O  O   . HOH Q 6 .   ? 10.139  2.222   26.423  1.00 38.14 ? 331 HOH A O   1 
HETATM 6041 O  O   . HOH Q 6 .   ? 8.177   8.984   29.842  1.00 27.41 ? 332 HOH A O   1 
HETATM 6042 O  O   . HOH Q 6 .   ? 2.320   -11.659 8.444   1.00 37.82 ? 333 HOH A O   1 
HETATM 6043 O  O   . HOH Q 6 .   ? 19.119  -18.975 24.272  1.00 28.53 ? 334 HOH A O   1 
HETATM 6044 O  O   . HOH Q 6 .   ? 24.724  -18.653 20.330  1.00 32.59 ? 335 HOH A O   1 
HETATM 6045 O  O   . HOH Q 6 .   ? 8.346   -3.306  4.314   1.00 21.34 ? 336 HOH A O   1 
HETATM 6046 O  O   . HOH Q 6 .   ? 11.883  16.248  23.684  1.00 36.05 ? 337 HOH A O   1 
HETATM 6047 O  O   . HOH Q 6 .   ? 9.943   11.165  4.655   1.00 28.69 ? 338 HOH A O   1 
HETATM 6048 O  O   . HOH Q 6 .   ? 16.240  6.570   27.519  1.00 24.94 ? 339 HOH A O   1 
HETATM 6049 O  O   . HOH Q 6 .   ? 37.474  4.340   21.084  1.00 28.48 ? 340 HOH A O   1 
HETATM 6050 O  O   . HOH Q 6 .   ? 33.143  -6.432  18.241  1.00 29.89 ? 341 HOH A O   1 
HETATM 6051 O  O   . HOH Q 6 .   ? 18.877  6.320   0.645   1.00 23.76 ? 342 HOH A O   1 
HETATM 6052 O  O   . HOH Q 6 .   ? 9.480   -17.691 14.203  1.00 32.14 ? 343 HOH A O   1 
HETATM 6053 O  O   . HOH Q 6 .   ? 8.644   14.918  17.852  1.00 37.03 ? 344 HOH A O   1 
HETATM 6054 O  O   . HOH Q 6 .   ? 23.601  -15.303 3.871   1.00 34.62 ? 345 HOH A O   1 
HETATM 6055 O  O   . HOH Q 6 .   ? 22.767  21.562  19.181  1.00 40.73 ? 346 HOH A O   1 
HETATM 6056 O  O   . HOH Q 6 .   ? 24.962  14.080  8.271   1.00 29.34 ? 347 HOH A O   1 
HETATM 6057 O  O   . HOH Q 6 .   ? 30.692  20.005  16.149  1.00 44.57 ? 348 HOH A O   1 
HETATM 6058 O  O   . HOH Q 6 .   ? 6.770   3.022   20.988  1.00 18.83 ? 349 HOH A O   1 
HETATM 6059 O  O   . HOH Q 6 .   ? 17.468  21.802  28.470  1.00 35.21 ? 350 HOH A O   1 
HETATM 6060 O  O   . HOH Q 6 .   ? 28.393  -11.416 21.012  1.00 33.08 ? 351 HOH A O   1 
HETATM 6061 O  O   . HOH Q 6 .   ? 13.368  5.632   25.969  1.00 37.24 ? 352 HOH A O   1 
HETATM 6062 O  O   . HOH Q 6 .   ? 29.781  13.172  23.645  1.00 40.66 ? 353 HOH A O   1 
HETATM 6063 O  O   . HOH Q 6 .   ? 12.631  -16.853 11.065  1.00 22.47 ? 354 HOH A O   1 
HETATM 6064 O  O   . HOH Q 6 .   ? 28.855  -6.989  22.404  1.00 26.57 ? 355 HOH A O   1 
HETATM 6065 O  O   . HOH Q 6 .   ? 6.546   -0.314  4.349   1.00 17.09 ? 356 HOH A O   1 
HETATM 6066 O  O   . HOH Q 6 .   ? 11.062  -9.229  27.851  1.00 21.72 ? 357 HOH A O   1 
HETATM 6067 O  O   . HOH Q 6 .   ? 28.096  -0.050  16.018  1.00 23.13 ? 358 HOH A O   1 
HETATM 6068 O  O   . HOH Q 6 .   ? 32.217  -6.953  11.099  1.00 33.04 ? 359 HOH A O   1 
HETATM 6069 O  O   . HOH Q 6 .   ? 16.699  -19.667 15.231  1.00 25.24 ? 360 HOH A O   1 
HETATM 6070 O  O   . HOH Q 6 .   ? 23.140  6.069   0.707   1.00 36.18 ? 361 HOH A O   1 
HETATM 6071 O  O   . HOH Q 6 .   ? 12.910  -1.995  1.949   1.00 33.49 ? 362 HOH A O   1 
HETATM 6072 O  O   . HOH Q 6 .   ? 13.781  -15.560 28.988  1.00 32.02 ? 363 HOH A O   1 
HETATM 6073 O  O   . HOH Q 6 .   ? 20.301  -6.927  21.708  1.00 16.67 ? 364 HOH A O   1 
HETATM 6074 O  O   . HOH Q 6 .   ? 30.961  -8.768  20.779  1.00 41.79 ? 365 HOH A O   1 
HETATM 6075 O  O   . HOH Q 6 .   ? 19.667  -11.072 3.390   1.00 21.25 ? 366 HOH A O   1 
HETATM 6076 O  O   . HOH Q 6 .   ? 11.375  -12.777 27.891  1.00 23.60 ? 367 HOH A O   1 
HETATM 6077 O  O   . HOH Q 6 .   ? 30.999  -4.471  9.542   1.00 28.54 ? 368 HOH A O   1 
HETATM 6078 O  O   . HOH Q 6 .   ? 15.448  13.967  3.432   1.00 32.04 ? 369 HOH A O   1 
HETATM 6079 O  O   . HOH Q 6 .   ? 25.352  4.847   0.659   1.00 39.38 ? 370 HOH A O   1 
HETATM 6080 O  O   . HOH Q 6 .   ? 20.734  -18.325 3.861   1.00 23.94 ? 371 HOH A O   1 
HETATM 6081 O  O   . HOH Q 6 .   ? 19.788  -11.531 29.688  1.00 31.10 ? 372 HOH A O   1 
HETATM 6082 O  O   . HOH Q 6 .   ? 26.769  4.710   5.681   1.00 18.41 ? 373 HOH A O   1 
HETATM 6083 O  O   . HOH Q 6 .   ? 24.186  17.931  13.865  1.00 28.28 ? 374 HOH A O   1 
HETATM 6084 O  O   . HOH Q 6 .   ? 30.999  -0.610  5.883   1.00 38.12 ? 375 HOH A O   1 
HETATM 6085 O  O   . HOH Q 6 .   ? 15.325  4.942   1.817   1.00 22.32 ? 376 HOH A O   1 
HETATM 6086 O  O   . HOH Q 6 .   ? 11.411  -10.260 6.196   1.00 22.75 ? 377 HOH A O   1 
HETATM 6087 O  O   . HOH Q 6 .   ? 32.909  4.184   28.490  1.00 24.20 ? 378 HOH A O   1 
HETATM 6088 O  O   . HOH Q 6 .   ? 10.425  -6.038  32.781  1.00 28.99 ? 379 HOH A O   1 
HETATM 6089 O  O   . HOH Q 6 .   ? 4.086   7.054   8.593   1.00 39.58 ? 380 HOH A O   1 
HETATM 6090 O  O   . HOH Q 6 .   ? 22.008  -11.195 2.252   1.00 36.25 ? 381 HOH A O   1 
HETATM 6091 O  O   . HOH Q 6 .   ? 6.101   -8.474  31.550  1.00 19.84 ? 382 HOH A O   1 
HETATM 6092 O  O   . HOH Q 6 .   ? 10.586  -23.748 11.718  1.00 34.98 ? 383 HOH A O   1 
HETATM 6093 O  O   . HOH Q 6 .   ? 30.848  -11.201 14.341  1.00 42.87 ? 384 HOH A O   1 
HETATM 6094 O  O   . HOH Q 6 .   ? 4.198   9.750   8.788   1.00 53.12 ? 385 HOH A O   1 
HETATM 6095 O  O   . HOH Q 6 .   ? 10.909  -22.705 14.349  1.00 39.57 ? 386 HOH A O   1 
HETATM 6096 O  O   . HOH Q 6 .   ? 13.719  -13.101 3.758   1.00 25.28 ? 387 HOH A O   1 
HETATM 6097 O  O   . HOH Q 6 .   ? 28.454  -14.180 19.572  1.00 36.60 ? 388 HOH A O   1 
HETATM 6098 O  O   . HOH Q 6 .   ? 9.939   -16.066 16.427  1.00 29.85 ? 389 HOH A O   1 
HETATM 6099 O  O   . HOH Q 6 .   ? 8.413   10.639  15.204  1.00 22.19 ? 390 HOH A O   1 
HETATM 6100 O  O   . HOH Q 6 .   ? 5.519   2.747   10.334  1.00 23.55 ? 391 HOH A O   1 
HETATM 6101 O  O   . HOH Q 6 .   ? 20.513  -4.426  -0.834  1.00 31.73 ? 392 HOH A O   1 
HETATM 6102 O  O   . HOH Q 6 .   ? 22.740  13.604  5.742   1.00 34.69 ? 393 HOH A O   1 
HETATM 6103 O  O   . HOH Q 6 .   ? 4.634   12.750  11.550  1.00 31.12 ? 394 HOH A O   1 
HETATM 6104 O  O   . HOH Q 6 .   ? -0.516  -11.116 23.918  1.00 37.61 ? 395 HOH A O   1 
HETATM 6105 O  O   . HOH Q 6 .   ? 23.578  -16.818 25.945  1.00 28.69 ? 396 HOH A O   1 
HETATM 6106 O  O   . HOH Q 6 .   ? 27.546  9.225   3.760   1.00 54.90 ? 397 HOH A O   1 
HETATM 6107 O  O   . HOH Q 6 .   ? 4.960   8.818   11.487  1.00 34.02 ? 398 HOH A O   1 
HETATM 6108 O  O   . HOH Q 6 .   ? 2.500   -1.134  25.322  1.00 21.29 ? 399 HOH A O   1 
HETATM 6109 O  O   . HOH Q 6 .   ? 10.821  11.973  7.932   1.00 17.79 ? 400 HOH A O   1 
HETATM 6110 O  O   . HOH Q 6 .   ? 16.176  3.128   26.971  1.00 35.20 ? 401 HOH A O   1 
HETATM 6111 O  O   . HOH Q 6 .   ? 10.959  12.534  18.067  1.00 28.87 ? 402 HOH A O   1 
HETATM 6112 O  O   . HOH Q 6 .   ? 10.982  -15.352 26.760  1.00 22.93 ? 403 HOH A O   1 
HETATM 6113 O  O   . HOH Q 6 .   ? 8.510   13.148  23.510  1.00 25.98 ? 404 HOH A O   1 
HETATM 6114 O  O   . HOH Q 6 .   ? 24.426  -19.678 16.534  1.00 38.27 ? 405 HOH A O   1 
HETATM 6115 O  O   . HOH Q 6 .   ? 24.750  -3.374  3.871   1.00 36.18 ? 406 HOH A O   1 
HETATM 6116 O  O   . HOH Q 6 .   ? 22.085  -11.002 24.485  1.00 18.02 ? 407 HOH A O   1 
HETATM 6117 O  O   . HOH Q 6 .   ? 18.866  -20.977 7.717   1.00 31.87 ? 408 HOH A O   1 
HETATM 6118 O  O   . HOH Q 6 .   ? 16.579  -20.032 24.250  1.00 27.26 ? 409 HOH A O   1 
HETATM 6119 O  O   . HOH Q 6 .   ? 18.856  16.621  26.901  1.00 36.23 ? 410 HOH A O   1 
HETATM 6120 O  O   . HOH Q 6 .   ? 11.617  -15.835 30.639  1.00 39.16 ? 411 HOH A O   1 
HETATM 6121 O  O   . HOH Q 6 .   ? 9.778   -16.814 10.335  1.00 31.66 ? 412 HOH A O   1 
HETATM 6122 O  O   . HOH Q 6 .   ? 20.945  17.281  7.386   1.00 29.30 ? 413 HOH A O   1 
HETATM 6123 O  O   . HOH Q 6 .   ? 22.674  -20.157 23.924  1.00 43.41 ? 414 HOH A O   1 
HETATM 6124 O  O   . HOH Q 6 .   ? 29.570  -9.704  11.726  1.00 23.04 ? 415 HOH A O   1 
HETATM 6125 O  O   . HOH Q 6 .   ? 0.648   -0.621  18.578  1.00 26.10 ? 416 HOH A O   1 
HETATM 6126 O  O   . HOH Q 6 .   ? 17.096  -14.136 28.934  1.00 27.80 ? 417 HOH A O   1 
HETATM 6127 O  O   . HOH Q 6 .   ? 18.754  5.415   33.815  1.00 32.32 ? 418 HOH A O   1 
HETATM 6128 O  O   . HOH Q 6 .   ? 30.473  -7.065  24.464  1.00 32.24 ? 419 HOH A O   1 
HETATM 6129 O  O   . HOH Q 6 .   ? 10.890  12.465  15.385  1.00 25.98 ? 420 HOH A O   1 
HETATM 6130 O  O   . HOH Q 6 .   ? 16.164  -14.299 3.592   1.00 33.88 ? 421 HOH A O   1 
HETATM 6131 O  O   . HOH Q 6 .   ? 35.046  1.958   15.012  1.00 26.58 ? 422 HOH A O   1 
HETATM 6132 O  O   . HOH Q 6 .   ? 37.733  13.794  22.629  1.00 51.97 ? 423 HOH A O   1 
HETATM 6133 O  O   . HOH Q 6 .   ? 25.299  -16.253 23.421  1.00 28.42 ? 424 HOH A O   1 
HETATM 6134 O  O   . HOH Q 6 .   ? 4.679   -0.087  27.489  1.00 28.02 ? 425 HOH A O   1 
HETATM 6135 O  O   . HOH Q 6 .   ? 17.555  11.923  1.146   1.00 38.73 ? 426 HOH A O   1 
HETATM 6136 O  O   . HOH Q 6 .   ? 4.387   3.437   13.583  1.00 19.40 ? 427 HOH A O   1 
HETATM 6137 O  O   . HOH Q 6 .   ? 33.476  10.930  18.093  1.00 35.25 ? 428 HOH A O   1 
HETATM 6138 O  O   . HOH Q 6 .   ? 27.662  -6.406  35.611  1.00 28.42 ? 429 HOH A O   1 
HETATM 6139 O  O   . HOH Q 6 .   ? 20.350  10.450  1.768   1.00 26.17 ? 430 HOH A O   1 
HETATM 6140 O  O   . HOH Q 6 .   ? 6.521   -11.236 33.315  1.00 32.17 ? 431 HOH A O   1 
HETATM 6141 O  O   . HOH Q 6 .   ? 28.600  0.694   12.577  1.00 21.53 ? 432 HOH A O   1 
HETATM 6142 O  O   . HOH Q 6 .   ? 3.368   6.316   13.012  1.00 29.56 ? 433 HOH A O   1 
HETATM 6143 O  O   . HOH Q 6 .   ? 18.741  -19.982 10.051  1.00 40.47 ? 434 HOH A O   1 
HETATM 6144 O  O   . HOH Q 6 .   ? 20.562  20.505  12.987  1.00 31.24 ? 435 HOH A O   1 
HETATM 6145 O  O   . HOH Q 6 .   ? 27.064  13.633  6.539   1.00 38.84 ? 436 HOH A O   1 
HETATM 6146 O  O   . HOH Q 6 .   ? 6.230   -15.446 22.132  1.00 36.14 ? 437 HOH A O   1 
HETATM 6147 O  O   . HOH Q 6 .   ? 24.275  -6.153  31.272  1.00 25.34 ? 438 HOH A O   1 
HETATM 6148 O  O   . HOH Q 6 .   ? 16.536  -2.174  30.763  1.00 38.68 ? 439 HOH A O   1 
HETATM 6149 O  O   . HOH Q 6 .   ? 28.686  20.192  12.996  1.00 36.00 ? 440 HOH A O   1 
HETATM 6150 O  O   . HOH Q 6 .   ? 14.286  -0.388  24.200  1.00 31.90 ? 441 HOH A O   1 
HETATM 6151 O  O   . HOH Q 6 .   ? 16.863  5.355   31.878  1.00 40.55 ? 442 HOH A O   1 
HETATM 6152 O  O   . HOH Q 6 .   ? 9.789   -16.469 28.230  1.00 43.70 ? 443 HOH A O   1 
HETATM 6153 O  O   . HOH Q 6 .   ? 7.008   -13.272 13.620  1.00 36.53 ? 444 HOH A O   1 
HETATM 6154 O  O   . HOH Q 6 .   ? 32.476  -6.797  26.399  1.00 50.15 ? 445 HOH A O   1 
HETATM 6155 O  O   . HOH Q 6 .   ? 26.830  -9.549  5.797   1.00 40.34 ? 446 HOH A O   1 
HETATM 6156 O  O   . HOH Q 6 .   ? 10.016  -4.336  2.536   1.00 26.85 ? 447 HOH A O   1 
HETATM 6157 O  O   . HOH Q 6 .   ? 7.654   -6.199  32.257  1.00 29.72 ? 448 HOH A O   1 
HETATM 6158 O  O   . HOH Q 6 .   ? 19.401  -20.166 15.277  1.00 31.43 ? 449 HOH A O   1 
HETATM 6159 O  O   . HOH Q 6 .   ? 31.619  10.503  26.306  1.00 39.44 ? 450 HOH A O   1 
HETATM 6160 O  O   . HOH Q 6 .   ? 15.208  19.508  8.841   1.00 44.84 ? 451 HOH A O   1 
HETATM 6161 O  O   . HOH Q 6 .   ? 10.177  -12.643 6.341   1.00 25.60 ? 452 HOH A O   1 
HETATM 6162 O  O   . HOH Q 6 .   ? 3.105   -14.642 8.635   1.00 40.15 ? 453 HOH A O   1 
HETATM 6163 O  O   . HOH Q 6 .   ? 32.815  -6.891  23.806  1.00 32.45 ? 454 HOH A O   1 
HETATM 6164 O  O   . HOH Q 6 .   ? 26.815  -11.700 5.072   1.00 41.24 ? 455 HOH A O   1 
HETATM 6165 O  O   . HOH Q 6 .   ? 27.949  8.288   30.377  1.00 32.50 ? 456 HOH A O   1 
HETATM 6166 O  O   . HOH Q 6 .   ? 12.146  0.958   29.587  1.00 40.60 ? 457 HOH A O   1 
HETATM 6167 O  O   . HOH Q 6 .   ? 32.495  -5.199  28.221  1.00 32.35 ? 458 HOH A O   1 
HETATM 6168 O  O   . HOH Q 6 .   ? 22.070  16.512  25.563  1.00 38.66 ? 459 HOH A O   1 
HETATM 6169 O  O   . HOH Q 6 .   ? 27.342  -18.759 19.250  1.00 30.85 ? 460 HOH A O   1 
HETATM 6170 O  O   . HOH Q 6 .   ? 8.658   -7.645  2.645   1.00 32.87 ? 461 HOH A O   1 
HETATM 6171 O  O   . HOH Q 6 .   ? 23.695  -12.952 25.584  1.00 25.92 ? 462 HOH A O   1 
HETATM 6172 O  O   . HOH Q 6 .   ? -1.767  -0.138  20.558  1.00 34.60 ? 463 HOH A O   1 
HETATM 6173 O  O   . HOH Q 6 .   ? 33.010  -9.557  19.855  1.00 47.88 ? 464 HOH A O   1 
HETATM 6174 O  O   . HOH Q 6 .   ? 11.254  -9.324  3.534   1.00 34.47 ? 465 HOH A O   1 
HETATM 6175 O  O   . HOH Q 6 .   ? -2.035  -12.315 25.506  1.00 36.22 ? 466 HOH A O   1 
HETATM 6176 O  O   . HOH Q 6 .   ? 22.886  20.484  14.458  1.00 43.10 ? 467 HOH A O   1 
HETATM 6177 O  O   . HOH Q 6 .   ? 26.366  -12.549 25.075  1.00 35.13 ? 468 HOH A O   1 
HETATM 6178 O  O   . HOH Q 6 .   ? 20.986  2.286   -1.602  1.00 31.23 ? 469 HOH A O   1 
HETATM 6179 O  O   . HOH Q 6 .   ? -3.699  -0.154  20.746  1.00 37.57 ? 470 HOH A O   1 
HETATM 6180 O  O   . HOH Q 6 .   ? 11.933  18.363  22.238  1.00 41.66 ? 471 HOH A O   1 
HETATM 6181 O  O   . HOH Q 6 .   ? 20.741  4.402   39.670  1.00 36.99 ? 472 HOH A O   1 
HETATM 6182 O  O   . HOH Q 6 .   ? 26.091  -4.223  39.686  1.00 31.45 ? 473 HOH A O   1 
HETATM 6183 O  O   . HOH Q 6 .   ? 36.840  -1.413  25.405  1.00 25.92 ? 474 HOH A O   1 
HETATM 6184 O  O   . HOH Q 6 .   ? -1.100  -6.440  14.895  1.00 43.04 ? 475 HOH A O   1 
HETATM 6185 O  O   . HOH Q 6 .   ? 19.685  -14.786 30.106  1.00 51.00 ? 476 HOH A O   1 
HETATM 6186 O  O   . HOH Q 6 .   ? 3.851   -3.921  36.383  1.00 35.42 ? 477 HOH A O   1 
HETATM 6187 O  O   . HOH Q 6 .   ? 4.552   2.108   7.751   1.00 28.27 ? 478 HOH A O   1 
HETATM 6188 O  O   . HOH Q 6 .   ? 28.299  6.420   3.732   1.00 30.56 ? 479 HOH A O   1 
HETATM 6189 O  O   . HOH Q 6 .   ? 15.535  -14.898 30.357  1.00 34.26 ? 480 HOH A O   1 
HETATM 6190 O  O   . HOH Q 6 .   ? 37.426  -0.520  22.796  1.00 41.35 ? 481 HOH A O   1 
HETATM 6191 O  O   . HOH Q 6 .   ? 31.295  7.244   14.363  1.00 31.63 ? 482 HOH A O   1 
HETATM 6192 O  O   . HOH Q 6 .   ? 26.007  -8.882  23.942  1.00 36.57 ? 483 HOH A O   1 
HETATM 6193 O  O   . HOH Q 6 .   ? 14.802  -7.077  35.282  1.00 40.66 ? 484 HOH A O   1 
HETATM 6194 O  O   . HOH Q 6 .   ? 17.712  -11.454 1.694   1.00 42.69 ? 485 HOH A O   1 
HETATM 6195 O  O   . HOH Q 6 .   ? 26.920  8.638   1.287   1.00 48.26 ? 486 HOH A O   1 
HETATM 6196 O  O   . HOH Q 6 .   ? 35.932  -8.580  12.004  1.00 44.70 ? 487 HOH A O   1 
HETATM 6197 O  O   . HOH Q 6 .   ? 20.243  -6.057  34.947  1.00 39.98 ? 488 HOH A O   1 
HETATM 6198 O  O   . HOH Q 6 .   ? 18.321  -6.940  32.966  1.00 38.29 ? 489 HOH A O   1 
HETATM 6199 O  O   . HOH Q 6 .   ? 11.587  20.274  9.544   1.00 49.59 ? 490 HOH A O   1 
HETATM 6200 O  O   . HOH Q 6 .   ? 18.363  11.949  39.091  1.00 43.24 ? 491 HOH A O   1 
HETATM 6201 O  O   . HOH R 6 .   ? -4.802  -10.127 58.108  1.00 39.28 ? 401 HOH B O   1 
HETATM 6202 O  O   . HOH R 6 .   ? -16.448 -11.945 56.522  1.00 40.31 ? 402 HOH B O   1 
HETATM 6203 O  O   . HOH R 6 .   ? -8.130  -17.906 36.715  1.00 36.63 ? 403 HOH B O   1 
HETATM 6204 O  O   . HOH R 6 .   ? 13.171  -6.587  45.200  1.00 40.94 ? 404 HOH B O   1 
HETATM 6205 O  O   . HOH R 6 .   ? -6.233  17.652  24.259  1.00 48.15 ? 405 HOH B O   1 
HETATM 6206 O  O   . HOH R 6 .   ? -14.964 11.742  23.049  1.00 27.95 ? 406 HOH B O   1 
HETATM 6207 O  O   . HOH R 6 .   ? -2.034  13.424  49.292  1.00 35.59 ? 407 HOH B O   1 
HETATM 6208 O  O   . HOH R 6 .   ? -20.156 -15.113 34.900  1.00 47.64 ? 408 HOH B O   1 
HETATM 6209 O  O   . HOH R 6 .   ? -3.103  22.312  42.678  1.00 35.70 ? 409 HOH B O   1 
HETATM 6210 O  O   . HOH R 6 .   ? -15.315 -13.799 52.059  1.00 33.44 ? 410 HOH B O   1 
HETATM 6211 O  O   . HOH R 6 .   ? -6.417  27.318  35.209  1.00 44.22 ? 411 HOH B O   1 
HETATM 6212 O  O   . HOH R 6 .   ? -16.962 -1.107  34.264  1.00 26.01 ? 412 HOH B O   1 
HETATM 6213 O  O   . HOH R 6 .   ? 3.761   20.199  37.705  1.00 34.90 ? 413 HOH B O   1 
HETATM 6214 O  O   . HOH R 6 .   ? -25.204 -3.679  45.145  1.00 37.05 ? 414 HOH B O   1 
HETATM 6215 O  O   . HOH R 6 .   ? 10.931  -5.247  50.831  1.00 36.45 ? 415 HOH B O   1 
HETATM 6216 O  O   . HOH R 6 .   ? -7.795  3.677   21.921  1.00 43.56 ? 416 HOH B O   1 
HETATM 6217 O  O   . HOH R 6 .   ? -17.363 -5.338  26.194  1.00 25.92 ? 417 HOH B O   1 
HETATM 6218 O  O   . HOH R 6 .   ? -8.065  20.300  46.065  1.00 34.47 ? 418 HOH B O   1 
HETATM 6219 O  O   . HOH R 6 .   ? -14.427 15.767  29.907  1.00 39.13 ? 419 HOH B O   1 
HETATM 6220 O  O   . HOH R 6 .   ? 3.831   -6.609  35.089  1.00 29.68 ? 420 HOH B O   1 
HETATM 6221 O  O   . HOH R 6 .   ? -0.043  -6.635  52.390  1.00 35.16 ? 421 HOH B O   1 
HETATM 6222 O  O   . HOH R 6 .   ? -1.413  6.112   58.120  1.00 27.10 ? 422 HOH B O   1 
HETATM 6223 O  O   . HOH R 6 .   ? -10.074 -6.571  31.756  1.00 39.89 ? 423 HOH B O   1 
HETATM 6224 O  O   . HOH R 6 .   ? -4.675  7.905   51.841  1.00 29.68 ? 424 HOH B O   1 
HETATM 6225 O  O   . HOH R 6 .   ? -21.165 16.098  43.783  1.00 38.90 ? 425 HOH B O   1 
HETATM 6226 O  O   . HOH R 6 .   ? -22.295 2.959   33.208  1.00 26.68 ? 426 HOH B O   1 
HETATM 6227 O  O   . HOH R 6 .   ? -2.440  13.123  24.618  1.00 40.58 ? 427 HOH B O   1 
HETATM 6228 O  O   . HOH R 6 .   ? -16.459 -7.251  24.169  1.00 25.86 ? 428 HOH B O   1 
HETATM 6229 O  O   . HOH R 6 .   ? -14.451 7.657   22.970  1.00 25.28 ? 429 HOH B O   1 
HETATM 6230 O  O   . HOH R 6 .   ? -2.399  9.775   46.087  1.00 19.19 ? 430 HOH B O   1 
HETATM 6231 O  O   . HOH R 6 .   ? -18.571 -14.045 31.881  1.00 36.23 ? 431 HOH B O   1 
HETATM 6232 O  O   . HOH R 6 .   ? -2.606  -2.248  29.026  1.00 20.19 ? 432 HOH B O   1 
HETATM 6233 O  O   . HOH R 6 .   ? -15.754 -5.721  52.453  1.00 39.56 ? 433 HOH B O   1 
HETATM 6234 O  O   . HOH R 6 .   ? -24.807 -5.566  42.406  1.00 35.37 ? 434 HOH B O   1 
HETATM 6235 O  O   . HOH R 6 .   ? -24.217 -5.631  38.328  1.00 30.47 ? 435 HOH B O   1 
HETATM 6236 O  O   . HOH R 6 .   ? -1.534  -12.729 33.918  1.00 29.74 ? 436 HOH B O   1 
HETATM 6237 O  O   . HOH R 6 .   ? -4.906  10.210  50.088  1.00 23.36 ? 437 HOH B O   1 
HETATM 6238 O  O   . HOH R 6 .   ? -21.211 4.951   42.120  1.00 27.27 ? 438 HOH B O   1 
HETATM 6239 O  O   . HOH R 6 .   ? -3.975  1.535   22.881  1.00 35.45 ? 439 HOH B O   1 
HETATM 6240 O  O   . HOH R 6 .   ? -12.790 17.625  33.901  1.00 31.59 ? 440 HOH B O   1 
HETATM 6241 O  O   . HOH R 6 .   ? -20.245 14.154  33.669  1.00 29.75 ? 441 HOH B O   1 
HETATM 6242 O  O   . HOH R 6 .   ? -17.258 -6.184  38.713  1.00 18.27 ? 442 HOH B O   1 
HETATM 6243 O  O   . HOH R 6 .   ? -0.053  -11.989 31.525  1.00 29.65 ? 443 HOH B O   1 
HETATM 6244 O  O   . HOH R 6 .   ? 3.168   17.142  43.848  1.00 30.84 ? 444 HOH B O   1 
HETATM 6245 O  O   . HOH R 6 .   ? -10.563 0.807   49.722  1.00 20.29 ? 445 HOH B O   1 
HETATM 6246 O  O   . HOH R 6 .   ? -0.458  19.562  41.929  1.00 29.16 ? 446 HOH B O   1 
HETATM 6247 O  O   . HOH R 6 .   ? -5.841  -11.445 33.019  1.00 23.39 ? 447 HOH B O   1 
HETATM 6248 O  O   . HOH R 6 .   ? -6.898  -3.216  59.976  1.00 23.25 ? 448 HOH B O   1 
HETATM 6249 O  O   . HOH R 6 .   ? 3.861   13.161  34.568  1.00 22.05 ? 449 HOH B O   1 
HETATM 6250 O  O   . HOH R 6 .   ? -14.358 -16.661 43.673  1.00 30.87 ? 450 HOH B O   1 
HETATM 6251 O  O   . HOH R 6 .   ? -3.223  -15.201 33.469  1.00 36.14 ? 451 HOH B O   1 
HETATM 6252 O  O   . HOH R 6 .   ? -9.067  20.449  38.112  1.00 26.65 ? 452 HOH B O   1 
HETATM 6253 O  O   . HOH R 6 .   ? -17.614 -13.305 45.317  1.00 24.49 ? 453 HOH B O   1 
HETATM 6254 O  O   . HOH R 6 .   ? -8.455  11.755  52.321  1.00 19.46 ? 454 HOH B O   1 
HETATM 6255 O  O   . HOH R 6 .   ? -3.514  7.698   42.793  1.00 18.93 ? 455 HOH B O   1 
HETATM 6256 O  O   . HOH R 6 .   ? 4.717   16.098  37.179  1.00 30.62 ? 456 HOH B O   1 
HETATM 6257 O  O   . HOH R 6 .   ? 1.516   -4.306  36.288  1.00 31.12 ? 457 HOH B O   1 
HETATM 6258 O  O   . HOH R 6 .   ? 2.692   -5.902  39.725  1.00 25.79 ? 458 HOH B O   1 
HETATM 6259 O  O   . HOH R 6 .   ? -18.834 1.116   26.853  1.00 17.21 ? 459 HOH B O   1 
HETATM 6260 O  O   . HOH R 6 .   ? -14.875 1.555   55.343  1.00 29.01 ? 460 HOH B O   1 
HETATM 6261 O  O   . HOH R 6 .   ? -2.215  8.062   52.968  1.00 35.30 ? 461 HOH B O   1 
HETATM 6262 O  O   . HOH R 6 .   ? -20.457 13.251  48.233  1.00 37.86 ? 462 HOH B O   1 
HETATM 6263 O  O   . HOH R 6 .   ? -22.734 -4.150  35.162  1.00 22.33 ? 463 HOH B O   1 
HETATM 6264 O  O   . HOH R 6 .   ? 3.809   9.730   34.446  1.00 21.48 ? 464 HOH B O   1 
HETATM 6265 O  O   . HOH R 6 .   ? -0.428  -19.313 40.690  1.00 24.73 ? 465 HOH B O   1 
HETATM 6266 O  O   . HOH R 6 .   ? -12.364 -17.078 45.750  1.00 26.40 ? 466 HOH B O   1 
HETATM 6267 O  O   . HOH R 6 .   ? -11.269 20.658  44.677  1.00 21.68 ? 467 HOH B O   1 
HETATM 6268 O  O   . HOH R 6 .   ? -16.159 -2.153  53.807  1.00 37.04 ? 468 HOH B O   1 
HETATM 6269 O  O   . HOH R 6 .   ? -22.777 12.456  41.754  1.00 30.83 ? 469 HOH B O   1 
HETATM 6270 O  O   . HOH R 6 .   ? -7.071  -5.266  25.361  1.00 27.32 ? 470 HOH B O   1 
HETATM 6271 O  O   . HOH R 6 .   ? -0.889  2.162   58.165  1.00 19.41 ? 471 HOH B O   1 
HETATM 6272 O  O   . HOH R 6 .   ? -12.217 2.079   56.573  1.00 33.10 ? 472 HOH B O   1 
HETATM 6273 O  O   . HOH R 6 .   ? -24.025 -10.744 36.866  1.00 35.92 ? 473 HOH B O   1 
HETATM 6274 O  O   . HOH R 6 .   ? -3.957  -17.571 49.023  1.00 26.98 ? 474 HOH B O   1 
HETATM 6275 O  O   . HOH R 6 .   ? -23.271 -9.273  39.898  1.00 31.63 ? 475 HOH B O   1 
HETATM 6276 O  O   . HOH R 6 .   ? -17.572 11.555  31.766  1.00 25.96 ? 476 HOH B O   1 
HETATM 6277 O  O   . HOH R 6 .   ? -5.297  -6.645  60.492  1.00 22.40 ? 477 HOH B O   1 
HETATM 6278 O  O   . HOH R 6 .   ? -18.071 -16.101 41.472  1.00 29.89 ? 478 HOH B O   1 
HETATM 6279 O  O   . HOH R 6 .   ? 3.731   2.397   38.848  1.00 41.86 ? 479 HOH B O   1 
HETATM 6280 O  O   . HOH R 6 .   ? -21.499 12.436  39.598  1.00 20.90 ? 480 HOH B O   1 
HETATM 6281 O  O   . HOH R 6 .   ? -0.728  8.013   56.032  1.00 31.33 ? 481 HOH B O   1 
HETATM 6282 O  O   . HOH R 6 .   ? 5.014   17.009  32.948  1.00 33.80 ? 482 HOH B O   1 
HETATM 6283 O  O   . HOH R 6 .   ? -18.846 -10.253 30.129  1.00 35.05 ? 483 HOH B O   1 
HETATM 6284 O  O   . HOH R 6 .   ? -6.680  1.957   36.513  1.00 21.80 ? 484 HOH B O   1 
HETATM 6285 O  O   . HOH R 6 .   ? -8.763  14.188  49.994  1.00 24.77 ? 485 HOH B O   1 
HETATM 6286 O  O   . HOH R 6 .   ? -1.281  16.753  28.835  1.00 32.73 ? 486 HOH B O   1 
HETATM 6287 O  O   . HOH R 6 .   ? 0.173   -13.774 35.487  1.00 29.76 ? 487 HOH B O   1 
HETATM 6288 O  O   . HOH R 6 .   ? -7.113  17.041  31.721  1.00 24.42 ? 488 HOH B O   1 
HETATM 6289 O  O   . HOH R 6 .   ? -9.607  20.453  42.300  1.00 30.56 ? 489 HOH B O   1 
HETATM 6290 O  O   . HOH R 6 .   ? 2.437   1.709   25.557  1.00 23.14 ? 490 HOH B O   1 
HETATM 6291 O  O   . HOH R 6 .   ? -8.469  4.310   56.433  1.00 44.31 ? 491 HOH B O   1 
HETATM 6292 O  O   . HOH R 6 .   ? -20.504 19.798  41.103  1.00 25.64 ? 492 HOH B O   1 
HETATM 6293 O  O   . HOH R 6 .   ? 12.527  5.690   48.954  1.00 33.95 ? 493 HOH B O   1 
HETATM 6294 O  O   . HOH R 6 .   ? -16.434 7.645   51.963  1.00 27.30 ? 494 HOH B O   1 
HETATM 6295 O  O   . HOH R 6 .   ? 1.774   7.823   57.731  1.00 30.69 ? 495 HOH B O   1 
HETATM 6296 O  O   . HOH R 6 .   ? -20.681 15.583  36.401  1.00 27.37 ? 496 HOH B O   1 
HETATM 6297 O  O   . HOH R 6 .   ? -20.520 -3.927  46.725  1.00 21.25 ? 497 HOH B O   1 
HETATM 6298 O  O   . HOH R 6 .   ? 5.179   14.263  26.368  1.00 39.16 ? 498 HOH B O   1 
HETATM 6299 O  O   . HOH R 6 .   ? 0.867   -2.284  33.970  1.00 31.35 ? 499 HOH B O   1 
HETATM 6300 O  O   . HOH R 6 .   ? 1.883   -2.163  39.754  1.00 29.54 ? 500 HOH B O   1 
HETATM 6301 O  O   . HOH R 6 .   ? -10.079 7.220   55.349  1.00 26.15 ? 501 HOH B O   1 
HETATM 6302 O  O   . HOH R 6 .   ? -0.752  20.741  30.777  1.00 36.35 ? 502 HOH B O   1 
HETATM 6303 O  O   . HOH R 6 .   ? 8.064   6.517   47.466  1.00 39.64 ? 503 HOH B O   1 
HETATM 6304 O  O   . HOH R 6 .   ? -8.687  -11.502 32.475  1.00 23.19 ? 504 HOH B O   1 
HETATM 6305 O  O   . HOH R 6 .   ? 2.854   15.774  34.129  1.00 24.79 ? 505 HOH B O   1 
HETATM 6306 O  O   . HOH R 6 .   ? -16.855 10.794  48.166  1.00 23.02 ? 506 HOH B O   1 
HETATM 6307 O  O   . HOH R 6 .   ? 1.292   11.712  22.074  1.00 43.44 ? 507 HOH B O   1 
HETATM 6308 O  O   . HOH R 6 .   ? -16.893 19.146  48.267  1.00 18.67 ? 508 HOH B O   1 
HETATM 6309 O  O   . HOH R 6 .   ? -16.067 -11.112 31.374  1.00 18.94 ? 509 HOH B O   1 
HETATM 6310 O  O   . HOH R 6 .   ? -6.300  14.780  50.553  1.00 34.36 ? 510 HOH B O   1 
HETATM 6311 O  O   . HOH R 6 .   ? 8.677   6.574   31.188  1.00 36.46 ? 511 HOH B O   1 
HETATM 6312 O  O   . HOH R 6 .   ? -8.616  -9.785  29.965  1.00 24.83 ? 512 HOH B O   1 
HETATM 6313 O  O   . HOH R 6 .   ? -12.942 -1.630  26.503  1.00 28.96 ? 513 HOH B O   1 
HETATM 6314 O  O   . HOH R 6 .   ? -1.071  -6.443  23.248  1.00 33.38 ? 514 HOH B O   1 
HETATM 6315 O  O   . HOH R 6 .   ? -11.958 -8.042  25.947  1.00 29.59 ? 515 HOH B O   1 
HETATM 6316 O  O   . HOH R 6 .   ? -9.028  19.286  48.827  1.00 20.60 ? 516 HOH B O   1 
HETATM 6317 O  O   . HOH R 6 .   ? 8.955   6.957   52.401  1.00 24.92 ? 517 HOH B O   1 
HETATM 6318 O  O   . HOH R 6 .   ? 4.515   12.243  43.528  1.00 35.68 ? 518 HOH B O   1 
HETATM 6319 O  O   . HOH R 6 .   ? -0.972  11.715  44.846  1.00 23.73 ? 519 HOH B O   1 
HETATM 6320 O  O   . HOH R 6 .   ? -0.022  -17.373 37.454  1.00 29.96 ? 520 HOH B O   1 
HETATM 6321 O  O   . HOH R 6 .   ? 4.183   14.535  40.469  1.00 27.97 ? 521 HOH B O   1 
HETATM 6322 O  O   . HOH R 6 .   ? -21.545 -0.738  52.607  1.00 46.35 ? 522 HOH B O   1 
HETATM 6323 O  O   . HOH R 6 .   ? 9.821   12.994  30.588  1.00 30.38 ? 523 HOH B O   1 
HETATM 6324 O  O   . HOH R 6 .   ? -19.653 -12.848 43.063  1.00 29.13 ? 524 HOH B O   1 
HETATM 6325 O  O   . HOH R 6 .   ? 9.969   10.861  36.065  1.00 47.36 ? 525 HOH B O   1 
HETATM 6326 O  O   . HOH R 6 .   ? -2.252  -8.714  53.254  1.00 27.31 ? 526 HOH B O   1 
HETATM 6327 O  O   . HOH R 6 .   ? -8.944  -10.230 55.489  1.00 28.17 ? 527 HOH B O   1 
HETATM 6328 O  O   . HOH R 6 .   ? -6.536  9.358   22.390  1.00 37.21 ? 528 HOH B O   1 
HETATM 6329 O  O   . HOH R 6 .   ? -10.175 -5.264  24.726  1.00 33.73 ? 529 HOH B O   1 
HETATM 6330 O  O   . HOH R 6 .   ? -3.383  -6.815  25.076  1.00 43.23 ? 530 HOH B O   1 
HETATM 6331 O  O   . HOH R 6 .   ? -23.562 0.430   47.428  1.00 35.10 ? 531 HOH B O   1 
HETATM 6332 O  O   . HOH R 6 .   ? -1.904  16.714  47.823  1.00 25.42 ? 532 HOH B O   1 
HETATM 6333 O  O   . HOH R 6 .   ? -8.996  -19.647 45.152  1.00 36.99 ? 533 HOH B O   1 
HETATM 6334 O  O   . HOH R 6 .   ? -18.313 -6.821  29.460  1.00 34.60 ? 534 HOH B O   1 
HETATM 6335 O  O   . HOH R 6 .   ? 8.758   6.472   33.998  1.00 43.69 ? 535 HOH B O   1 
HETATM 6336 O  O   . HOH R 6 .   ? -11.911 -19.637 41.889  1.00 35.06 ? 536 HOH B O   1 
HETATM 6337 O  O   . HOH R 6 .   ? 8.470   -4.932  43.282  1.00 33.06 ? 537 HOH B O   1 
HETATM 6338 O  O   . HOH R 6 .   ? -12.614 -1.213  56.588  1.00 28.49 ? 538 HOH B O   1 
HETATM 6339 O  O   . HOH R 6 .   ? -24.180 2.597   42.190  1.00 34.55 ? 539 HOH B O   1 
HETATM 6340 O  O   . HOH R 6 .   ? -11.398 11.330  26.591  1.00 36.98 ? 540 HOH B O   1 
HETATM 6341 O  O   . HOH R 6 .   ? -9.805  -2.600  25.872  1.00 27.70 ? 541 HOH B O   1 
HETATM 6342 O  O   . HOH R 6 .   ? -18.248 10.025  27.154  1.00 38.92 ? 542 HOH B O   1 
HETATM 6343 O  O   . HOH R 6 .   ? -12.198 -4.472  55.833  1.00 41.26 ? 543 HOH B O   1 
HETATM 6344 O  O   . HOH R 6 .   ? -13.905 0.029   49.636  1.00 23.17 ? 544 HOH B O   1 
HETATM 6345 O  O   . HOH R 6 .   ? -10.766 -8.173  56.515  1.00 33.98 ? 545 HOH B O   1 
HETATM 6346 O  O   . HOH R 6 .   ? -4.399  6.893   57.869  1.00 51.02 ? 546 HOH B O   1 
HETATM 6347 O  O   . HOH R 6 .   ? -2.292  -12.543 29.672  1.00 34.83 ? 547 HOH B O   1 
HETATM 6348 O  O   . HOH R 6 .   ? 3.648   -7.413  51.602  1.00 36.78 ? 548 HOH B O   1 
HETATM 6349 O  O   . HOH R 6 .   ? -14.056 -19.061 49.692  1.00 35.02 ? 549 HOH B O   1 
HETATM 6350 O  O   . HOH R 6 .   ? -26.424 5.186   40.266  1.00 40.29 ? 550 HOH B O   1 
HETATM 6351 O  O   . HOH R 6 .   ? -9.974  18.628  28.896  1.00 47.18 ? 551 HOH B O   1 
HETATM 6352 O  O   . HOH R 6 .   ? -9.490  14.501  28.824  1.00 38.11 ? 552 HOH B O   1 
HETATM 6353 O  O   . HOH R 6 .   ? -5.005  24.452  34.200  1.00 38.82 ? 553 HOH B O   1 
HETATM 6354 O  O   . HOH R 6 .   ? 5.237   7.134   48.169  1.00 24.63 ? 554 HOH B O   1 
HETATM 6355 O  O   . HOH R 6 .   ? 6.066   18.831  24.625  1.00 51.57 ? 555 HOH B O   1 
HETATM 6356 O  O   . HOH R 6 .   ? 5.920   -14.490 37.382  1.00 42.15 ? 556 HOH B O   1 
HETATM 6357 O  O   . HOH R 6 .   ? 2.553   8.754   54.255  1.00 40.63 ? 557 HOH B O   1 
HETATM 6358 O  O   . HOH R 6 .   ? -15.955 21.854  37.648  1.00 38.25 ? 558 HOH B O   1 
HETATM 6359 O  O   . HOH R 6 .   ? -16.155 -18.721 40.395  1.00 41.59 ? 559 HOH B O   1 
HETATM 6360 O  O   . HOH R 6 .   ? -3.411  18.935  27.716  1.00 40.21 ? 560 HOH B O   1 
HETATM 6361 O  O   . HOH R 6 .   ? 0.131   13.888  46.432  1.00 27.41 ? 561 HOH B O   1 
HETATM 6362 O  O   . HOH R 6 .   ? 4.788   9.207   46.343  1.00 40.35 ? 562 HOH B O   1 
HETATM 6363 O  O   . HOH R 6 .   ? -20.649 9.008   28.753  1.00 35.84 ? 563 HOH B O   1 
HETATM 6364 O  O   . HOH R 6 .   ? -8.110  8.082   56.383  1.00 41.71 ? 564 HOH B O   1 
HETATM 6365 O  O   . HOH R 6 .   ? 6.201   15.521  38.907  1.00 36.64 ? 565 HOH B O   1 
HETATM 6366 O  O   . HOH R 6 .   ? -14.335 8.991   20.872  1.00 39.73 ? 566 HOH B O   1 
HETATM 6367 O  O   . HOH R 6 .   ? -17.067 -18.935 51.730  1.00 38.37 ? 567 HOH B O   1 
HETATM 6368 O  O   . HOH R 6 .   ? 4.742   -6.219  40.738  1.00 38.61 ? 568 HOH B O   1 
HETATM 6369 O  O   . HOH R 6 .   ? -3.395  9.242   22.162  1.00 36.27 ? 569 HOH B O   1 
HETATM 6370 O  O   . HOH R 6 .   ? -22.996 -12.167 41.090  1.00 44.00 ? 570 HOH B O   1 
HETATM 6371 O  O   . HOH R 6 .   ? -0.697  -9.694  54.944  1.00 34.59 ? 571 HOH B O   1 
HETATM 6372 O  O   . HOH R 6 .   ? -3.711  0.749   63.730  1.00 40.64 ? 572 HOH B O   1 
HETATM 6373 O  O   . HOH R 6 .   ? -12.346 -6.289  52.687  1.00 27.54 ? 573 HOH B O   1 
HETATM 6374 O  O   . HOH R 6 .   ? -22.809 19.278  39.717  1.00 37.23 ? 574 HOH B O   1 
HETATM 6375 O  O   . HOH R 6 .   ? -8.278  -5.077  23.811  1.00 32.95 ? 575 HOH B O   1 
HETATM 6376 O  O   . HOH R 6 .   ? 8.239   14.758  39.977  1.00 47.68 ? 576 HOH B O   1 
HETATM 6377 O  O   . HOH R 6 .   ? -7.487  -7.209  60.010  1.00 17.62 ? 577 HOH B O   1 
HETATM 6378 O  O   . HOH R 6 .   ? -5.774  11.990  52.064  1.00 35.42 ? 578 HOH B O   1 
HETATM 6379 O  O   . HOH R 6 .   ? -2.196  10.084  48.810  1.00 24.35 ? 579 HOH B O   1 
HETATM 6380 O  O   . HOH R 6 .   ? -12.907 -4.066  57.478  1.00 45.86 ? 580 HOH B O   1 
HETATM 6381 O  O   . HOH R 6 .   ? 13.641  4.906   51.067  1.00 33.33 ? 581 HOH B O   1 
HETATM 6382 O  O   . HOH R 6 .   ? -25.926 -11.290 35.546  1.00 49.73 ? 582 HOH B O   1 
HETATM 6383 O  O   . HOH R 6 .   ? 0.668   20.377  45.499  1.00 35.75 ? 583 HOH B O   1 
HETATM 6384 O  O   . HOH R 6 .   ? -0.390  23.682  34.438  1.00 40.55 ? 584 HOH B O   1 
HETATM 6385 O  O   . HOH R 6 .   ? -5.251  1.457   60.037  1.00 31.45 ? 585 HOH B O   1 
HETATM 6386 O  O   . HOH R 6 .   ? -0.906  -20.062 37.092  1.00 40.99 ? 586 HOH B O   1 
HETATM 6387 O  O   . HOH R 6 .   ? 1.482   -14.026 31.626  1.00 33.45 ? 587 HOH B O   1 
HETATM 6388 O  O   . HOH R 6 .   ? 9.019   6.852   45.168  1.00 42.72 ? 588 HOH B O   1 
HETATM 6389 O  O   . HOH R 6 .   ? -22.698 13.600  37.311  1.00 35.15 ? 589 HOH B O   1 
HETATM 6390 O  O   . HOH R 6 .   ? -21.899 -17.173 38.885  1.00 56.23 ? 590 HOH B O   1 
HETATM 6391 O  O   . HOH R 6 .   ? -16.808 3.198   56.637  1.00 36.22 ? 591 HOH B O   1 
HETATM 6392 O  O   . HOH R 6 .   ? 7.758   7.562   42.326  1.00 39.17 ? 592 HOH B O   1 
HETATM 6393 O  O   . HOH R 6 .   ? -19.928 -9.923  22.478  1.00 31.42 ? 593 HOH B O   1 
HETATM 6394 O  O   . HOH R 6 .   ? -19.709 1.817   56.724  1.00 54.63 ? 594 HOH B O   1 
HETATM 6395 O  O   . HOH R 6 .   ? 12.623  -10.071 42.090  1.00 48.82 ? 595 HOH B O   1 
HETATM 6396 O  O   . HOH S 6 .   ? -9.982  42.401  41.254  1.00 28.39 ? 401 HOH C O   1 
HETATM 6397 O  O   . HOH S 6 .   ? -3.588  24.853  43.677  1.00 30.82 ? 402 HOH C O   1 
HETATM 6398 O  O   . HOH S 6 .   ? -8.262  42.814  24.941  1.00 35.15 ? 403 HOH C O   1 
HETATM 6399 O  O   . HOH S 6 .   ? 18.805  39.154  43.698  1.00 25.39 ? 404 HOH C O   1 
HETATM 6400 O  O   . HOH S 6 .   ? 24.339  43.113  24.869  1.00 44.32 ? 405 HOH C O   1 
HETATM 6401 O  O   . HOH S 6 .   ? 24.587  26.777  31.990  1.00 46.63 ? 406 HOH C O   1 
HETATM 6402 O  O   . HOH S 6 .   ? -1.296  50.706  40.667  1.00 29.07 ? 407 HOH C O   1 
HETATM 6403 O  O   . HOH S 6 .   ? 6.745   36.893  35.256  1.00 29.77 ? 408 HOH C O   1 
HETATM 6404 O  O   . HOH S 6 .   ? 24.188  33.038  30.144  1.00 27.22 ? 409 HOH C O   1 
HETATM 6405 O  O   . HOH S 6 .   ? 2.162   24.085  47.503  1.00 41.73 ? 410 HOH C O   1 
HETATM 6406 O  O   . HOH S 6 .   ? 9.195   41.627  49.943  1.00 28.28 ? 411 HOH C O   1 
HETATM 6407 O  O   . HOH S 6 .   ? -10.935 41.462  42.638  1.00 44.49 ? 412 HOH C O   1 
HETATM 6408 O  O   . HOH S 6 .   ? 3.378   22.356  33.330  1.00 38.62 ? 413 HOH C O   1 
HETATM 6409 O  O   . HOH S 6 .   ? 3.057   47.345  24.269  1.00 25.09 ? 414 HOH C O   1 
HETATM 6410 O  O   . HOH S 6 .   ? 8.446   16.734  35.462  1.00 42.45 ? 415 HOH C O   1 
HETATM 6411 O  O   . HOH S 6 .   ? 17.350  22.301  30.967  1.00 30.09 ? 416 HOH C O   1 
HETATM 6412 O  O   . HOH S 6 .   ? 10.423  29.515  27.491  1.00 33.63 ? 417 HOH C O   1 
HETATM 6413 O  O   . HOH S 6 .   ? 19.495  21.645  42.666  1.00 38.28 ? 418 HOH C O   1 
HETATM 6414 O  O   . HOH S 6 .   ? 27.390  39.853  28.050  1.00 39.47 ? 419 HOH C O   1 
HETATM 6415 O  O   . HOH S 6 .   ? 4.181   21.605  30.711  1.00 39.63 ? 420 HOH C O   1 
HETATM 6416 O  O   . HOH S 6 .   ? 16.234  34.448  50.457  1.00 25.36 ? 421 HOH C O   1 
HETATM 6417 O  O   . HOH S 6 .   ? 9.486   45.974  19.228  1.00 45.81 ? 422 HOH C O   1 
HETATM 6418 O  O   . HOH S 6 .   ? 12.039  32.290  54.296  1.00 37.45 ? 423 HOH C O   1 
HETATM 6419 O  O   . HOH S 6 .   ? 7.979   30.435  53.409  1.00 30.31 ? 424 HOH C O   1 
HETATM 6420 O  O   . HOH S 6 .   ? 0.752   26.681  46.364  1.00 36.18 ? 425 HOH C O   1 
HETATM 6421 O  O   . HOH S 6 .   ? 7.402   55.224  29.547  1.00 39.45 ? 426 HOH C O   1 
HETATM 6422 O  O   . HOH S 6 .   ? 10.403  20.026  29.674  1.00 38.15 ? 427 HOH C O   1 
HETATM 6423 O  O   . HOH S 6 .   ? 17.398  21.376  44.372  1.00 44.08 ? 428 HOH C O   1 
HETATM 6424 O  O   . HOH S 6 .   ? -3.427  36.657  46.593  1.00 27.46 ? 429 HOH C O   1 
HETATM 6425 O  O   . HOH S 6 .   ? 23.505  41.506  45.186  1.00 35.83 ? 430 HOH C O   1 
HETATM 6426 O  O   . HOH S 6 .   ? 14.179  47.169  32.213  1.00 22.07 ? 431 HOH C O   1 
HETATM 6427 O  O   . HOH S 6 .   ? -8.692  39.272  32.714  1.00 37.84 ? 432 HOH C O   1 
HETATM 6428 O  O   . HOH S 6 .   ? 5.560   32.711  26.427  1.00 39.44 ? 433 HOH C O   1 
HETATM 6429 O  O   . HOH S 6 .   ? 9.135   31.726  27.914  1.00 40.59 ? 434 HOH C O   1 
HETATM 6430 O  O   . HOH S 6 .   ? 19.382  28.664  51.311  1.00 35.00 ? 435 HOH C O   1 
HETATM 6431 O  O   . HOH S 6 .   ? 0.670   33.775  23.748  1.00 32.54 ? 436 HOH C O   1 
HETATM 6432 O  O   . HOH S 6 .   ? 27.431  40.079  31.344  1.00 36.50 ? 437 HOH C O   1 
HETATM 6433 O  O   . HOH S 6 .   ? -8.157  35.497  34.549  1.00 39.03 ? 438 HOH C O   1 
HETATM 6434 O  O   . HOH S 6 .   ? 22.393  47.348  39.345  1.00 28.92 ? 439 HOH C O   1 
HETATM 6435 O  O   . HOH S 6 .   ? -4.160  33.668  46.269  1.00 20.89 ? 440 HOH C O   1 
HETATM 6436 O  O   . HOH S 6 .   ? 24.965  43.199  42.555  1.00 34.38 ? 441 HOH C O   1 
HETATM 6437 O  O   . HOH S 6 .   ? 26.167  27.697  34.160  1.00 39.91 ? 442 HOH C O   1 
HETATM 6438 O  O   . HOH S 6 .   ? 8.009   25.080  53.100  1.00 40.15 ? 443 HOH C O   1 
HETATM 6439 O  O   . HOH S 6 .   ? 1.458   31.003  30.452  1.00 23.25 ? 444 HOH C O   1 
HETATM 6440 O  O   . HOH S 6 .   ? 4.723   47.487  50.074  1.00 27.08 ? 445 HOH C O   1 
HETATM 6441 O  O   . HOH S 6 .   ? 9.477   30.015  46.612  1.00 25.50 ? 446 HOH C O   1 
HETATM 6442 O  O   . HOH S 6 .   ? 17.451  50.594  35.624  1.00 24.38 ? 447 HOH C O   1 
HETATM 6443 O  O   . HOH S 6 .   ? 12.484  30.768  26.517  1.00 38.65 ? 448 HOH C O   1 
HETATM 6444 O  O   . HOH S 6 .   ? -1.888  44.479  45.270  1.00 28.64 ? 449 HOH C O   1 
HETATM 6445 O  O   . HOH S 6 .   ? 19.120  39.843  40.285  1.00 26.81 ? 450 HOH C O   1 
HETATM 6446 O  O   . HOH S 6 .   ? 0.124   42.204  19.530  1.00 22.60 ? 451 HOH C O   1 
HETATM 6447 O  O   . HOH S 6 .   ? 11.198  44.513  32.981  1.00 19.22 ? 452 HOH C O   1 
HETATM 6448 O  O   . HOH S 6 .   ? 20.472  34.887  51.458  1.00 32.05 ? 453 HOH C O   1 
HETATM 6449 O  O   . HOH S 6 .   ? 11.572  48.941  24.935  1.00 33.12 ? 454 HOH C O   1 
HETATM 6450 O  O   . HOH S 6 .   ? -1.704  26.925  34.362  1.00 24.84 ? 455 HOH C O   1 
HETATM 6451 O  O   . HOH S 6 .   ? 2.706   55.141  37.476  1.00 31.63 ? 456 HOH C O   1 
HETATM 6452 O  O   . HOH S 6 .   ? 10.756  53.696  26.230  1.00 33.13 ? 457 HOH C O   1 
HETATM 6453 O  O   . HOH S 6 .   ? 0.475   49.548  48.740  1.00 36.95 ? 458 HOH C O   1 
HETATM 6454 O  O   . HOH S 6 .   ? 19.196  46.852  34.143  1.00 25.63 ? 459 HOH C O   1 
HETATM 6455 O  O   . HOH S 6 .   ? 27.494  36.461  29.724  1.00 30.57 ? 460 HOH C O   1 
HETATM 6456 O  O   . HOH S 6 .   ? 24.937  30.856  32.079  1.00 32.81 ? 461 HOH C O   1 
HETATM 6457 O  O   . HOH S 6 .   ? -2.236  33.920  24.872  1.00 26.71 ? 462 HOH C O   1 
HETATM 6458 O  O   . HOH S 6 .   ? -1.221  24.493  39.619  1.00 38.16 ? 463 HOH C O   1 
HETATM 6459 O  O   . HOH S 6 .   ? 12.139  41.518  50.793  1.00 31.26 ? 464 HOH C O   1 
HETATM 6460 O  O   . HOH S 6 .   ? 5.030   50.545  23.901  1.00 33.57 ? 465 HOH C O   1 
HETATM 6461 O  O   . HOH S 6 .   ? 14.197  49.028  45.892  1.00 27.39 ? 466 HOH C O   1 
HETATM 6462 O  O   . HOH S 6 .   ? 8.384   57.929  44.904  1.00 38.16 ? 467 HOH C O   1 
HETATM 6463 O  O   . HOH S 6 .   ? 13.831  20.675  22.705  1.00 38.39 ? 468 HOH C O   1 
HETATM 6464 O  O   . HOH S 6 .   ? -3.012  25.314  47.050  1.00 45.03 ? 469 HOH C O   1 
HETATM 6465 O  O   . HOH S 6 .   ? -2.652  30.671  40.366  1.00 28.37 ? 470 HOH C O   1 
HETATM 6466 O  O   . HOH S 6 .   ? 10.773  27.016  52.792  1.00 31.28 ? 471 HOH C O   1 
HETATM 6467 O  O   . HOH S 6 .   ? -0.247  20.797  39.457  1.00 25.62 ? 472 HOH C O   1 
HETATM 6468 O  O   . HOH S 6 .   ? 22.378  22.089  31.779  1.00 46.31 ? 473 HOH C O   1 
HETATM 6469 O  O   . HOH S 6 .   ? 5.919   57.435  26.544  1.00 40.55 ? 474 HOH C O   1 
HETATM 6470 O  O   . HOH S 6 .   ? 17.956  24.807  48.079  1.00 35.18 ? 475 HOH C O   1 
HETATM 6471 O  O   . HOH S 6 .   ? -1.378  25.490  30.883  1.00 31.81 ? 476 HOH C O   1 
HETATM 6472 O  O   . HOH S 6 .   ? -2.260  49.733  34.855  1.00 28.84 ? 477 HOH C O   1 
HETATM 6473 O  O   . HOH S 6 .   ? 16.223  40.959  19.496  1.00 42.36 ? 478 HOH C O   1 
HETATM 6474 O  O   . HOH S 6 .   ? 6.428   25.588  22.448  1.00 26.05 ? 479 HOH C O   1 
HETATM 6475 O  O   . HOH S 6 .   ? 3.616   44.091  24.415  1.00 24.52 ? 480 HOH C O   1 
HETATM 6476 O  O   . HOH S 6 .   ? -2.163  31.052  24.927  1.00 22.12 ? 481 HOH C O   1 
HETATM 6477 O  O   . HOH S 6 .   ? 20.945  47.729  32.261  1.00 31.09 ? 482 HOH C O   1 
HETATM 6478 O  O   . HOH S 6 .   ? 4.235   23.245  44.442  1.00 21.89 ? 483 HOH C O   1 
HETATM 6479 O  O   . HOH S 6 .   ? -9.845  50.121  30.908  1.00 45.18 ? 484 HOH C O   1 
HETATM 6480 O  O   . HOH S 6 .   ? 15.983  54.616  35.547  1.00 18.80 ? 485 HOH C O   1 
HETATM 6481 O  O   . HOH S 6 .   ? 19.216  47.665  45.884  1.00 36.99 ? 486 HOH C O   1 
HETATM 6482 O  O   . HOH S 6 .   ? 6.023   21.850  29.129  1.00 32.82 ? 487 HOH C O   1 
HETATM 6483 O  O   . HOH S 6 .   ? 4.789   20.358  47.352  1.00 39.99 ? 488 HOH C O   1 
HETATM 6484 O  O   . HOH S 6 .   ? 25.876  40.498  43.158  1.00 34.27 ? 489 HOH C O   1 
HETATM 6485 O  O   . HOH S 6 .   ? 10.687  45.622  51.162  1.00 46.70 ? 490 HOH C O   1 
HETATM 6486 O  O   . HOH S 6 .   ? -6.214  45.406  21.657  1.00 42.54 ? 491 HOH C O   1 
HETATM 6487 O  O   . HOH S 6 .   ? 12.565  48.850  30.599  1.00 19.55 ? 492 HOH C O   1 
HETATM 6488 O  O   . HOH S 6 .   ? 29.862  31.191  35.313  1.00 37.13 ? 493 HOH C O   1 
HETATM 6489 O  O   . HOH S 6 .   ? -2.614  29.572  36.942  1.00 22.92 ? 494 HOH C O   1 
HETATM 6490 O  O   . HOH S 6 .   ? -10.140 41.356  39.656  1.00 53.07 ? 495 HOH C O   1 
HETATM 6491 O  O   . HOH S 6 .   ? 8.166   50.524  24.842  1.00 23.24 ? 496 HOH C O   1 
HETATM 6492 O  O   . HOH S 6 .   ? 17.578  51.099  42.668  1.00 18.82 ? 497 HOH C O   1 
HETATM 6493 O  O   . HOH S 6 .   ? -5.760  32.578  30.917  1.00 28.23 ? 498 HOH C O   1 
HETATM 6494 O  O   . HOH S 6 .   ? 16.831  49.114  44.791  1.00 20.91 ? 499 HOH C O   1 
HETATM 6495 O  O   . HOH S 6 .   ? 7.789   22.201  50.266  1.00 33.57 ? 500 HOH C O   1 
HETATM 6496 O  O   . HOH S 6 .   ? 24.263  35.924  44.067  1.00 21.95 ? 501 HOH C O   1 
HETATM 6497 O  O   . HOH S 6 .   ? 0.741   33.467  21.553  1.00 50.36 ? 502 HOH C O   1 
HETATM 6498 O  O   . HOH S 6 .   ? 12.136  57.203  39.137  1.00 29.82 ? 503 HOH C O   1 
HETATM 6499 O  O   . HOH S 6 .   ? 16.819  17.971  42.765  1.00 40.45 ? 504 HOH C O   1 
HETATM 6500 O  O   . HOH S 6 .   ? 3.758   55.100  49.274  1.00 34.29 ? 505 HOH C O   1 
HETATM 6501 O  O   . HOH S 6 .   ? 8.186   57.421  40.749  1.00 34.99 ? 506 HOH C O   1 
HETATM 6502 O  O   . HOH S 6 .   ? 3.634   23.757  36.767  1.00 23.27 ? 507 HOH C O   1 
HETATM 6503 O  O   . HOH S 6 .   ? 13.932  46.108  23.719  1.00 38.85 ? 508 HOH C O   1 
HETATM 6504 O  O   . HOH S 6 .   ? 16.221  32.573  21.373  1.00 45.46 ? 509 HOH C O   1 
HETATM 6505 O  O   . HOH S 6 .   ? 17.638  44.866  24.668  1.00 35.53 ? 510 HOH C O   1 
HETATM 6506 O  O   . HOH S 6 .   ? 5.154   41.104  19.446  1.00 29.70 ? 511 HOH C O   1 
HETATM 6507 O  O   . HOH S 6 .   ? -1.814  54.867  40.930  1.00 46.13 ? 512 HOH C O   1 
HETATM 6508 O  O   . HOH S 6 .   ? 1.644   49.591  25.039  1.00 29.47 ? 513 HOH C O   1 
HETATM 6509 O  O   . HOH S 6 .   ? 4.772   56.053  28.881  1.00 36.45 ? 514 HOH C O   1 
HETATM 6510 O  O   . HOH S 6 .   ? 25.857  38.207  23.630  1.00 47.61 ? 515 HOH C O   1 
HETATM 6511 O  O   . HOH S 6 .   ? 0.243   44.631  17.966  1.00 31.09 ? 516 HOH C O   1 
HETATM 6512 O  O   . HOH S 6 .   ? 14.815  20.829  48.163  1.00 34.11 ? 517 HOH C O   1 
HETATM 6513 O  O   . HOH S 6 .   ? 9.517   37.355  30.957  1.00 32.87 ? 518 HOH C O   1 
HETATM 6514 O  O   . HOH S 6 .   ? -2.934  26.856  37.390  1.00 28.03 ? 519 HOH C O   1 
HETATM 6515 O  O   . HOH S 6 .   ? 14.302  57.031  35.808  1.00 32.53 ? 520 HOH C O   1 
HETATM 6516 O  O   . HOH S 6 .   ? 13.605  54.817  32.002  1.00 27.46 ? 521 HOH C O   1 
HETATM 6517 O  O   . HOH S 6 .   ? 15.278  44.621  50.795  1.00 37.94 ? 522 HOH C O   1 
HETATM 6518 O  O   . HOH S 6 .   ? -4.135  48.597  28.240  1.00 44.08 ? 523 HOH C O   1 
HETATM 6519 O  O   . HOH S 6 .   ? 26.488  28.201  28.030  1.00 43.44 ? 524 HOH C O   1 
HETATM 6520 O  O   . HOH S 6 .   ? 5.296   56.513  38.176  1.00 32.88 ? 525 HOH C O   1 
HETATM 6521 O  O   . HOH S 6 .   ? 6.210   41.481  55.103  1.00 42.70 ? 526 HOH C O   1 
HETATM 6522 O  O   . HOH S 6 .   ? -8.482  40.901  29.943  1.00 37.62 ? 527 HOH C O   1 
HETATM 6523 O  O   . HOH S 6 .   ? 15.266  52.002  44.064  1.00 34.86 ? 528 HOH C O   1 
HETATM 6524 O  O   . HOH S 6 .   ? 5.817   36.311  28.161  1.00 34.85 ? 529 HOH C O   1 
HETATM 6525 O  O   . HOH S 6 .   ? 20.311  22.282  30.276  1.00 38.72 ? 530 HOH C O   1 
HETATM 6526 O  O   . HOH S 6 .   ? 0.967   44.917  54.879  1.00 51.23 ? 531 HOH C O   1 
HETATM 6527 O  O   . HOH S 6 .   ? 10.807  17.941  30.933  1.00 35.27 ? 532 HOH C O   1 
HETATM 6528 O  O   . HOH S 6 .   ? 30.573  35.554  31.946  1.00 44.81 ? 533 HOH C O   1 
HETATM 6529 O  O   . HOH S 6 .   ? 2.511   40.559  19.119  1.00 35.61 ? 534 HOH C O   1 
HETATM 6530 O  O   . HOH S 6 .   ? 0.102   37.252  15.147  1.00 36.28 ? 535 HOH C O   1 
HETATM 6531 O  O   . HOH S 6 .   ? 13.652  51.380  29.956  1.00 24.91 ? 536 HOH C O   1 
HETATM 6532 O  O   . HOH S 6 .   ? 10.529  56.357  49.966  1.00 43.30 ? 537 HOH C O   1 
HETATM 6533 O  O   . HOH S 6 .   ? 23.534  44.494  47.320  1.00 37.66 ? 538 HOH C O   1 
HETATM 6534 O  O   . HOH S 6 .   ? 17.296  17.847  45.628  1.00 44.02 ? 539 HOH C O   1 
HETATM 6535 O  O   . HOH S 6 .   ? 3.467   57.774  39.916  1.00 45.65 ? 540 HOH C O   1 
HETATM 6536 O  O   . HOH S 6 .   ? 11.171  49.943  51.029  1.00 45.64 ? 541 HOH C O   1 
HETATM 6537 O  O   . HOH S 6 .   ? -10.256 43.236  23.153  1.00 47.17 ? 542 HOH C O   1 
HETATM 6538 O  O   . HOH S 6 .   ? 16.743  47.804  32.726  1.00 31.67 ? 543 HOH C O   1 
HETATM 6539 O  O   . HOH S 6 .   ? 13.679  50.197  26.437  1.00 35.74 ? 544 HOH C O   1 
HETATM 6540 O  O   . HOH S 6 .   ? -4.408  30.980  42.599  1.00 30.84 ? 545 HOH C O   1 
HETATM 6541 O  O   . HOH S 6 .   ? 10.543  51.766  24.049  1.00 36.40 ? 546 HOH C O   1 
HETATM 6542 O  O   . HOH S 6 .   ? 8.248   37.032  28.781  1.00 39.10 ? 547 HOH C O   1 
HETATM 6543 O  O   . HOH S 6 .   ? 6.471   49.928  18.784  1.00 35.02 ? 548 HOH C O   1 
HETATM 6544 O  O   . HOH S 6 .   ? 23.528  33.952  43.782  1.00 41.79 ? 549 HOH C O   1 
HETATM 6545 O  O   . HOH S 6 .   ? 15.443  49.098  49.901  1.00 49.20 ? 550 HOH C O   1 
HETATM 6546 O  O   . HOH S 6 .   ? 23.989  21.951  29.044  1.00 42.65 ? 551 HOH C O   1 
HETATM 6547 O  O   . HOH S 6 .   ? -4.131  27.988  39.393  1.00 41.63 ? 552 HOH C O   1 
HETATM 6548 O  O   . HOH S 6 .   ? 11.177  41.591  21.304  1.00 36.07 ? 553 HOH C O   1 
HETATM 6549 O  O   . HOH S 6 .   ? -12.436 39.488  29.366  1.00 41.75 ? 554 HOH C O   1 
HETATM 6550 O  O   . HOH S 6 .   ? 11.185  52.612  51.879  1.00 50.51 ? 555 HOH C O   1 
HETATM 6551 O  O   . HOH S 6 .   ? -11.160 36.321  32.424  1.00 39.63 ? 556 HOH C O   1 
HETATM 6552 O  O   . HOH S 6 .   ? 6.964   51.163  52.432  1.00 32.52 ? 557 HOH C O   1 
HETATM 6553 O  O   . HOH S 6 .   ? 12.415  16.216  49.848  1.00 49.62 ? 558 HOH C O   1 
HETATM 6554 O  O   . HOH S 6 .   ? 16.048  29.960  55.832  1.00 35.45 ? 559 HOH C O   1 
HETATM 6555 O  O   . HOH S 6 .   ? 27.148  28.653  19.549  1.00 40.94 ? 560 HOH C O   1 
HETATM 6556 O  O   . HOH T 6 .   ? -2.275  47.888  5.990   1.00 41.52 ? 301 HOH D O   1 
HETATM 6557 O  O   . HOH T 6 .   ? -14.459 11.213  1.033   1.00 35.13 ? 302 HOH D O   1 
HETATM 6558 O  O   . HOH T 6 .   ? -9.482  11.995  13.392  1.00 33.75 ? 303 HOH D O   1 
HETATM 6559 O  O   . HOH T 6 .   ? -5.472  39.106  23.881  1.00 31.17 ? 304 HOH D O   1 
HETATM 6560 O  O   . HOH T 6 .   ? 4.427   27.252  -7.516  1.00 23.66 ? 305 HOH D O   1 
HETATM 6561 O  O   . HOH T 6 .   ? -0.785  20.760  27.755  1.00 39.67 ? 306 HOH D O   1 
HETATM 6562 O  O   . HOH T 6 .   ? -16.205 39.216  18.891  1.00 46.64 ? 307 HOH D O   1 
HETATM 6563 O  O   . HOH T 6 .   ? -9.759  27.619  -8.483  1.00 28.41 ? 308 HOH D O   1 
HETATM 6564 O  O   . HOH T 6 .   ? -13.485 47.206  14.998  1.00 46.55 ? 309 HOH D O   1 
HETATM 6565 O  O   . HOH T 6 .   ? -2.622  34.493  -11.150 1.00 26.41 ? 310 HOH D O   1 
HETATM 6566 O  O   . HOH T 6 .   ? 7.202   13.666  13.685  1.00 37.37 ? 311 HOH D O   1 
HETATM 6567 O  O   . HOH T 6 .   ? 10.650  30.252  5.822   1.00 35.63 ? 312 HOH D O   1 
HETATM 6568 O  O   . HOH T 6 .   ? -0.624  39.816  15.699  1.00 32.58 ? 313 HOH D O   1 
HETATM 6569 O  O   . HOH T 6 .   ? -25.098 30.876  5.176   1.00 34.50 ? 314 HOH D O   1 
HETATM 6570 O  O   . HOH T 6 .   ? 6.131   33.654  24.868  1.00 43.80 ? 315 HOH D O   1 
HETATM 6571 O  O   . HOH T 6 .   ? -3.119  25.877  27.695  1.00 34.37 ? 316 HOH D O   1 
HETATM 6572 O  O   . HOH T 6 .   ? -0.273  38.896  10.852  1.00 27.61 ? 317 HOH D O   1 
HETATM 6573 O  O   . HOH T 6 .   ? 9.207   43.916  8.731   1.00 46.59 ? 318 HOH D O   1 
HETATM 6574 O  O   . HOH T 6 .   ? -18.915 30.928  -2.457  1.00 21.30 ? 319 HOH D O   1 
HETATM 6575 O  O   . HOH T 6 .   ? 7.099   37.049  -2.388  1.00 33.37 ? 320 HOH D O   1 
HETATM 6576 O  O   . HOH T 6 .   ? -24.210 29.659  8.225   1.00 32.24 ? 321 HOH D O   1 
HETATM 6577 O  O   . HOH T 6 .   ? -7.681  29.261  -2.084  1.00 25.31 ? 322 HOH D O   1 
HETATM 6578 O  O   . HOH T 6 .   ? 0.237   21.854  -0.485  1.00 28.69 ? 323 HOH D O   1 
HETATM 6579 O  O   . HOH T 6 .   ? -1.934  37.057  14.097  1.00 36.82 ? 324 HOH D O   1 
HETATM 6580 O  O   . HOH T 6 .   ? -1.256  24.360  6.828   1.00 24.49 ? 325 HOH D O   1 
HETATM 6581 O  O   . HOH T 6 .   ? 14.534  30.598  5.064   1.00 32.22 ? 326 HOH D O   1 
HETATM 6582 O  O   . HOH T 6 .   ? -4.700  26.594  31.820  1.00 37.63 ? 327 HOH D O   1 
HETATM 6583 O  O   . HOH T 6 .   ? -10.146 45.187  15.465  1.00 32.57 ? 328 HOH D O   1 
HETATM 6584 O  O   . HOH T 6 .   ? -3.852  23.662  -6.987  1.00 23.83 ? 329 HOH D O   1 
HETATM 6585 O  O   . HOH T 6 .   ? 3.836   24.197  17.004  1.00 27.45 ? 330 HOH D O   1 
HETATM 6586 O  O   . HOH T 6 .   ? 1.369   22.885  3.969   1.00 18.60 ? 331 HOH D O   1 
HETATM 6587 O  O   . HOH T 6 .   ? -1.494  6.249   12.328  1.00 39.47 ? 332 HOH D O   1 
HETATM 6588 O  O   . HOH T 6 .   ? -18.851 33.379  6.166   1.00 25.18 ? 333 HOH D O   1 
HETATM 6589 O  O   . HOH T 6 .   ? 1.660   12.276  19.529  1.00 44.02 ? 334 HOH D O   1 
HETATM 6590 O  O   . HOH T 6 .   ? -11.604 41.568  14.847  1.00 27.07 ? 335 HOH D O   1 
HETATM 6591 O  O   . HOH T 6 .   ? 0.443   17.314  -1.111  1.00 33.29 ? 336 HOH D O   1 
HETATM 6592 O  O   . HOH T 6 .   ? 7.659   22.345  8.912   1.00 30.72 ? 337 HOH D O   1 
HETATM 6593 O  O   . HOH T 6 .   ? -22.644 23.075  9.812   1.00 40.68 ? 338 HOH D O   1 
HETATM 6594 O  O   . HOH T 6 .   ? -1.935  38.371  -11.283 1.00 23.18 ? 339 HOH D O   1 
HETATM 6595 O  O   . HOH T 6 .   ? 9.497   37.359  -1.011  1.00 31.90 ? 340 HOH D O   1 
HETATM 6596 O  O   . HOH T 6 .   ? 4.923   20.883  16.968  1.00 24.07 ? 341 HOH D O   1 
HETATM 6597 O  O   . HOH T 6 .   ? -15.229 32.287  20.554  1.00 32.96 ? 342 HOH D O   1 
HETATM 6598 O  O   . HOH T 6 .   ? -7.571  43.655  15.140  1.00 25.42 ? 343 HOH D O   1 
HETATM 6599 O  O   . HOH T 6 .   ? -19.495 40.544  -0.404  1.00 28.02 ? 344 HOH D O   1 
HETATM 6600 O  O   . HOH T 6 .   ? -3.342  10.436  7.207   1.00 35.63 ? 345 HOH D O   1 
HETATM 6601 O  O   . HOH T 6 .   ? -7.071  27.963  -9.061  1.00 28.11 ? 346 HOH D O   1 
HETATM 6602 O  O   . HOH T 6 .   ? -2.140  16.954  -1.306  1.00 25.56 ? 347 HOH D O   1 
HETATM 6603 O  O   . HOH T 6 .   ? -16.719 23.369  20.207  1.00 24.96 ? 348 HOH D O   1 
HETATM 6604 O  O   . HOH T 6 .   ? 11.851  31.114  -0.979  1.00 23.83 ? 349 HOH D O   1 
HETATM 6605 O  O   . HOH T 6 .   ? -3.015  45.690  -0.386  1.00 40.99 ? 350 HOH D O   1 
HETATM 6606 O  O   . HOH T 6 .   ? -16.914 22.617  22.583  1.00 44.78 ? 351 HOH D O   1 
HETATM 6607 O  O   . HOH T 6 .   ? -20.815 24.458  17.688  1.00 40.80 ? 352 HOH D O   1 
HETATM 6608 O  O   . HOH T 6 .   ? -8.542  35.496  -7.695  1.00 31.71 ? 353 HOH D O   1 
HETATM 6609 O  O   . HOH T 6 .   ? -6.951  48.791  -0.126  1.00 41.32 ? 354 HOH D O   1 
HETATM 6610 O  O   . HOH T 6 .   ? 0.544   29.657  12.409  1.00 41.70 ? 355 HOH D O   1 
HETATM 6611 O  O   . HOH T 6 .   ? -21.110 38.291  13.449  1.00 25.94 ? 356 HOH D O   1 
HETATM 6612 O  O   . HOH T 6 .   ? -4.959  14.027  16.805  1.00 30.00 ? 357 HOH D O   1 
HETATM 6613 O  O   . HOH T 6 .   ? -14.696 26.584  22.624  1.00 31.42 ? 358 HOH D O   1 
HETATM 6614 O  O   . HOH T 6 .   ? -17.148 14.614  5.090   1.00 24.65 ? 359 HOH D O   1 
HETATM 6615 O  O   . HOH T 6 .   ? -17.792 44.827  2.071   1.00 27.19 ? 360 HOH D O   1 
HETATM 6616 O  O   . HOH T 6 .   ? -3.712  10.725  10.100  1.00 30.44 ? 361 HOH D O   1 
HETATM 6617 O  O   . HOH T 6 .   ? -16.144 21.895  -3.576  1.00 44.25 ? 362 HOH D O   1 
HETATM 6618 O  O   . HOH T 6 .   ? 7.326   18.341  15.035  1.00 35.44 ? 363 HOH D O   1 
HETATM 6619 O  O   . HOH T 6 .   ? -7.440  28.780  11.842  1.00 23.70 ? 364 HOH D O   1 
HETATM 6620 O  O   . HOH T 6 .   ? -3.766  18.660  24.896  1.00 37.78 ? 365 HOH D O   1 
HETATM 6621 O  O   . HOH T 6 .   ? -1.883  43.320  2.296   1.00 36.10 ? 366 HOH D O   1 
HETATM 6622 O  O   . HOH T 6 .   ? -4.785  13.134  24.104  1.00 41.63 ? 367 HOH D O   1 
HETATM 6623 O  O   . HOH T 6 .   ? 4.547   18.028  17.169  1.00 25.89 ? 368 HOH D O   1 
HETATM 6624 O  O   . HOH T 6 .   ? -0.441  23.149  -2.851  1.00 40.86 ? 369 HOH D O   1 
HETATM 6625 O  O   . HOH T 6 .   ? -3.795  44.172  -2.955  1.00 37.53 ? 370 HOH D O   1 
HETATM 6626 O  O   . HOH T 6 .   ? -4.043  9.797   3.450   1.00 20.14 ? 371 HOH D O   1 
HETATM 6627 O  O   . HOH T 6 .   ? -21.449 23.587  1.295   1.00 40.68 ? 372 HOH D O   1 
HETATM 6628 O  O   . HOH T 6 .   ? 3.893   31.164  -7.509  1.00 20.08 ? 373 HOH D O   1 
HETATM 6629 O  O   . HOH T 6 .   ? -16.679 30.125  19.570  1.00 27.62 ? 374 HOH D O   1 
HETATM 6630 O  O   . HOH T 6 .   ? 2.975   24.814  -2.850  1.00 28.48 ? 375 HOH D O   1 
HETATM 6631 O  O   . HOH T 6 .   ? 3.010   21.288  5.752   1.00 24.17 ? 376 HOH D O   1 
HETATM 6632 O  O   . HOH T 6 .   ? -19.174 22.754  18.747  1.00 31.87 ? 377 HOH D O   1 
HETATM 6633 O  O   . HOH T 6 .   ? 3.431   41.815  0.049   1.00 42.82 ? 378 HOH D O   1 
HETATM 6634 O  O   . HOH T 6 .   ? 4.750   14.105  9.029   1.00 33.05 ? 379 HOH D O   1 
HETATM 6635 O  O   . HOH T 6 .   ? -22.684 34.063  14.753  1.00 51.21 ? 380 HOH D O   1 
HETATM 6636 O  O   . HOH T 6 .   ? -2.482  40.256  12.082  1.00 26.78 ? 381 HOH D O   1 
HETATM 6637 O  O   . HOH T 6 .   ? -8.751  22.118  26.033  1.00 41.42 ? 382 HOH D O   1 
HETATM 6638 O  O   . HOH T 6 .   ? -17.201 48.027  4.651   1.00 31.80 ? 383 HOH D O   1 
HETATM 6639 O  O   . HOH T 6 .   ? -8.287  30.893  -9.087  1.00 26.93 ? 384 HOH D O   1 
HETATM 6640 O  O   . HOH T 6 .   ? -24.469 30.491  12.233  1.00 37.79 ? 385 HOH D O   1 
HETATM 6641 O  O   . HOH T 6 .   ? -15.443 45.922  1.011   1.00 28.42 ? 386 HOH D O   1 
HETATM 6642 O  O   . HOH T 6 .   ? 0.146   35.340  10.876  1.00 35.86 ? 387 HOH D O   1 
HETATM 6643 O  O   . HOH T 6 .   ? -8.636  9.920   -1.734  1.00 16.95 ? 388 HOH D O   1 
HETATM 6644 O  O   . HOH T 6 .   ? -14.550 39.053  17.169  1.00 27.45 ? 389 HOH D O   1 
HETATM 6645 O  O   . HOH T 6 .   ? -1.874  40.929  -3.336  1.00 32.86 ? 390 HOH D O   1 
HETATM 6646 O  O   . HOH T 6 .   ? -21.375 27.621  17.148  1.00 35.28 ? 391 HOH D O   1 
HETATM 6647 O  O   . HOH T 6 .   ? -7.039  43.609  17.838  1.00 24.54 ? 392 HOH D O   1 
HETATM 6648 O  O   . HOH T 6 .   ? -24.621 39.865  11.842  1.00 41.33 ? 393 HOH D O   1 
HETATM 6649 O  O   . HOH T 6 .   ? 4.366   16.544  2.914   1.00 27.95 ? 394 HOH D O   1 
HETATM 6650 O  O   . HOH T 6 .   ? -19.677 30.451  19.918  1.00 41.01 ? 395 HOH D O   1 
HETATM 6651 O  O   . HOH T 6 .   ? 3.716   20.210  0.750   1.00 32.05 ? 396 HOH D O   1 
HETATM 6652 O  O   . HOH T 6 .   ? -11.113 17.990  -1.937  1.00 18.66 ? 397 HOH D O   1 
HETATM 6653 O  O   . HOH T 6 .   ? 0.578   24.320  -1.952  1.00 27.89 ? 398 HOH D O   1 
HETATM 6654 O  O   . HOH T 6 .   ? -19.778 18.435  8.387   1.00 37.18 ? 399 HOH D O   1 
HETATM 6655 O  O   . HOH T 6 .   ? -6.378  45.648  14.076  1.00 32.30 ? 400 HOH D O   1 
HETATM 6656 O  O   . HOH T 6 .   ? -18.514 36.235  19.908  1.00 37.85 ? 401 HOH D O   1 
HETATM 6657 O  O   . HOH T 6 .   ? -16.427 11.693  8.930   1.00 35.44 ? 402 HOH D O   1 
HETATM 6658 O  O   . HOH T 6 .   ? -13.751 7.777   4.316   1.00 29.82 ? 403 HOH D O   1 
HETATM 6659 O  O   . HOH T 6 .   ? -9.101  29.324  25.582  1.00 29.08 ? 404 HOH D O   1 
HETATM 6660 O  O   . HOH T 6 .   ? -20.594 22.477  14.704  1.00 26.23 ? 405 HOH D O   1 
HETATM 6661 O  O   . HOH T 6 .   ? 12.932  29.532  0.890   1.00 29.63 ? 406 HOH D O   1 
HETATM 6662 O  O   . HOH T 6 .   ? 7.461   20.211  11.224  1.00 33.98 ? 407 HOH D O   1 
HETATM 6663 O  O   . HOH T 6 .   ? 9.287   23.197  22.142  1.00 41.06 ? 408 HOH D O   1 
HETATM 6664 O  O   . HOH T 6 .   ? -21.987 43.121  3.058   1.00 35.64 ? 409 HOH D O   1 
HETATM 6665 O  O   . HOH T 6 .   ? 4.554   39.292  10.763  1.00 44.79 ? 410 HOH D O   1 
HETATM 6666 O  O   . HOH T 6 .   ? 6.411   39.901  9.072   1.00 35.12 ? 411 HOH D O   1 
HETATM 6667 O  O   . HOH T 6 .   ? -18.350 22.003  2.023   1.00 32.94 ? 412 HOH D O   1 
HETATM 6668 O  O   . HOH T 6 .   ? -25.251 34.887  3.194   1.00 34.18 ? 413 HOH D O   1 
HETATM 6669 O  O   . HOH T 6 .   ? -12.537 50.082  8.503   1.00 45.69 ? 414 HOH D O   1 
HETATM 6670 O  O   . HOH T 6 .   ? -14.409 40.922  14.462  1.00 38.94 ? 415 HOH D O   1 
HETATM 6671 O  O   . HOH T 6 .   ? -11.015 29.315  -2.975  1.00 23.11 ? 416 HOH D O   1 
HETATM 6672 O  O   . HOH T 6 .   ? -13.170 31.372  22.233  1.00 39.22 ? 417 HOH D O   1 
HETATM 6673 O  O   . HOH T 6 .   ? 2.053   25.438  -7.385  1.00 39.64 ? 418 HOH D O   1 
HETATM 6674 O  O   . HOH T 6 .   ? -7.967  40.488  -7.749  1.00 33.70 ? 419 HOH D O   1 
HETATM 6675 O  O   . HOH T 6 .   ? -19.881 33.518  20.615  1.00 54.04 ? 420 HOH D O   1 
HETATM 6676 O  O   . HOH T 6 .   ? 8.109   27.749  3.795   1.00 25.41 ? 421 HOH D O   1 
HETATM 6677 O  O   . HOH T 6 .   ? -0.648  22.815  -5.532  1.00 37.77 ? 422 HOH D O   1 
HETATM 6678 O  O   . HOH T 6 .   ? 8.368   24.381  10.017  1.00 38.65 ? 423 HOH D O   1 
HETATM 6679 O  O   . HOH T 6 .   ? 6.594   27.856  21.274  1.00 47.89 ? 424 HOH D O   1 
HETATM 6680 O  O   . HOH T 6 .   ? 7.951   26.035  6.238   1.00 36.10 ? 425 HOH D O   1 
HETATM 6681 O  O   . HOH T 6 .   ? -0.618  32.291  -12.259 1.00 36.11 ? 426 HOH D O   1 
HETATM 6682 O  O   . HOH T 6 .   ? 14.832  40.620  7.247   1.00 46.02 ? 427 HOH D O   1 
HETATM 6683 O  O   . HOH T 6 .   ? -12.951 43.789  17.811  1.00 48.12 ? 428 HOH D O   1 
HETATM 6684 O  O   . HOH T 6 .   ? -9.380  43.617  18.997  1.00 37.12 ? 429 HOH D O   1 
HETATM 6685 O  O   . HOH T 6 .   ? -27.277 44.553  9.726   1.00 38.62 ? 430 HOH D O   1 
HETATM 6686 O  O   . HOH T 6 .   ? -16.580 19.568  -3.165  1.00 41.80 ? 431 HOH D O   1 
HETATM 6687 O  O   . HOH T 6 .   ? -1.033  13.385  22.415  1.00 37.36 ? 432 HOH D O   1 
HETATM 6688 O  O   . HOH T 6 .   ? -6.223  21.837  26.772  1.00 39.32 ? 433 HOH D O   1 
HETATM 6689 O  O   . HOH T 6 .   ? -13.421 7.416   1.473   1.00 50.95 ? 434 HOH D O   1 
HETATM 6690 O  O   . HOH T 6 .   ? -26.002 38.816  5.382   1.00 47.16 ? 435 HOH D O   1 
HETATM 6691 O  O   . HOH T 6 .   ? 11.022  40.261  8.821   1.00 51.20 ? 436 HOH D O   1 
HETATM 6692 O  O   . HOH T 6 .   ? -19.602 44.898  -2.288  1.00 46.53 ? 437 HOH D O   1 
HETATM 6693 O  O   . HOH T 6 .   ? 4.633   11.047  19.981  1.00 45.17 ? 438 HOH D O   1 
HETATM 6694 O  O   . HOH T 6 .   ? -9.770  6.829   9.154   1.00 42.28 ? 439 HOH D O   1 
HETATM 6695 O  O   . HOH T 6 .   ? -13.983 36.453  22.104  1.00 49.33 ? 440 HOH D O   1 
HETATM 6696 O  O   . HOH T 6 .   ? -6.826  34.638  -11.428 1.00 51.14 ? 441 HOH D O   1 
HETATM 6697 O  O   . HOH T 6 .   ? 1.458   41.595  15.797  1.00 47.14 ? 442 HOH D O   1 
HETATM 6698 O  O   . HOH T 6 .   ? -10.418 35.555  -5.665  1.00 28.93 ? 443 HOH D O   1 
HETATM 6699 O  O   . HOH T 6 .   ? -10.837 7.991   -1.013  1.00 32.66 ? 444 HOH D O   1 
HETATM 6700 O  O   . HOH T 6 .   ? 2.198   22.778  1.460   1.00 27.50 ? 445 HOH D O   1 
HETATM 6701 O  O   . HOH T 6 .   ? -2.582  34.819  16.095  1.00 30.12 ? 446 HOH D O   1 
HETATM 6702 O  O   . HOH T 6 .   ? -22.828 22.642  12.883  1.00 38.80 ? 447 HOH D O   1 
HETATM 6703 O  O   . HOH T 6 .   ? -16.122 7.109   5.124   1.00 46.63 ? 448 HOH D O   1 
HETATM 6704 O  O   . HOH T 6 .   ? -0.327  46.253  -6.693  1.00 46.86 ? 449 HOH D O   1 
HETATM 6705 O  O   . HOH T 6 .   ? -12.905 8.329   -1.390  1.00 39.10 ? 450 HOH D O   1 
HETATM 6706 O  O   . HOH T 6 .   ? -14.133 18.856  -5.002  1.00 45.82 ? 451 HOH D O   1 
HETATM 6707 O  O   . HOH T 6 .   ? -16.555 27.889  21.586  1.00 32.07 ? 452 HOH D O   1 
HETATM 6708 O  O   . HOH T 6 .   ? 17.206  37.031  3.138   1.00 38.29 ? 453 HOH D O   1 
HETATM 6709 O  O   . HOH T 6 .   ? 8.936   28.020  10.787  1.00 45.12 ? 454 HOH D O   1 
# 
