data_8XZY
# 
_entry.id   8XZY 
# 
_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   8XZY         pdb_00008xzy 10.2210/pdb8xzy/pdb 
WWPDB D_1300044476 ?            ?                   
# 
_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                        8XZY 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              guoreyting@hubu.edu.cn 
_pdbx_contact_author.name_first         Rey-Ting 
_pdbx_contact_author.name_last          Guo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2942-7246 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xiang, W.L.'  1 ? 
'Huang, J.-W.' 2 ? 
'Yang, Y.'     3 ? 
'Chen, C.-C.'  4 ? 
'Guo, R.-T.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J.Agric.Food Chem.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5118 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            72 
_citation.language                  ? 
_citation.page_first                18201 
_citation.page_last                 18213 
_citation.title                     
'Unleashing the Power of Evolution in Xylanase Engineering: Investigating the Role of Distal Mutation Regulation.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jafc.4c03245 
_citation.pdbx_database_id_PubMed   39082219 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, Y.'      1  ?                   
primary 'Yang, Y.'    2  ?                   
primary 'Lu, G.'      3  ?                   
primary 'Xiang, W.L.' 4  ?                   
primary 'Sun, T.Y.'   5  0000-0002-7746-479X 
primary 'Chen, K.W.'  6  ?                   
primary 'Lv, X.'      7  ?                   
primary 'Gui, Y.F.'   8  ?                   
primary 'Zeng, R.Q.'  9  ?                   
primary 'Du, Y.K.'    10 ?                   
primary 'Fu, C.H.'    11 ?                   
primary 'Huang, J.W.' 12 ?                   
primary 'Chen, C.C.'  13 ?                   
primary 'Guo, R.T.'   14 0000-0003-2942-7246 
primary 'Yu, L.J.'    15 0000-0003-2517-2266 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Endo-1,4-beta-xylanase 21502.773 4   3.2.1.8 E176A,D31P,A34Q,K118Q,A168H ? ? 
2 non-polymer syn 'ZINC ION'             65.409    7   ?       ?                           ? ? 
3 water       nat water                  18.015    697 ?       ?                           ? ? 
# 
_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 
2 'ZINC ION' ZN  
3 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 (strain NIH 2624 / FGSC A1156)' 
_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_
_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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -11 ?   ?   ?   A . n 
A 1 2   ALA 2   -10 ?   ?   ?   A . n 
A 1 3   GLY 3   -9  ?   ?   ?   A . n 
A 1 4   ALA 4   -8  ?   ?   ?   A . n 
A 1 5   GLY 5   -7  ?   ?   ?   A . n 
A 1 6   ALA 6   -6  ?   ?   ?   A . n 
A 1 7   GLY 7   -5  ?   ?   ?   A . n 
A 1 8   ALA 8   -4  ?   ?   ?   A . n 
A 1 9   GLY 9   -3  ?   ?   ?   A . n 
A 1 10  ALA 10  -2  ?   ?   ?   A . n 
A 1 11  GLY 11  -1  ?   ?   ?   A . n 
A 1 12  MET 12  0   ?   ?   ?   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_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN  1   200 200 ZN  ZN  A . 
F 2 ZN  1   201 201 ZN  ZN  A . 
G 2 ZN  1   200 200 ZN  ZN  B . 
H 2 ZN  1   201 201 ZN  ZN  B . 
I 2 ZN  1   200 200 ZN  ZN  C . 
J 2 ZN  1   200 200 ZN  ZN  D . 
K 2 ZN  1   201 201 ZN  ZN  D . 
L 3 HOH 1   301 330 HOH HOH A . 
L 3 HOH 2   302 8   HOH HOH A . 
L 3 HOH 3   303 352 HOH HOH A . 
L 3 HOH 4   304 626 HOH HOH A . 
L 3 HOH 5   305 586 HOH HOH A . 
L 3 HOH 6   306 630 HOH HOH A . 
L 3 HOH 7   307 639 HOH HOH A . 
L 3 HOH 8   308 454 HOH HOH A . 
L 3 HOH 9   309 627 HOH HOH A . 
L 3 HOH 10  310 332 HOH HOH A . 
L 3 HOH 11  311 550 HOH HOH A . 
L 3 HOH 12  312 572 HOH HOH A . 
L 3 HOH 13  313 81  HOH HOH A . 
L 3 HOH 14  314 380 HOH HOH A . 
L 3 HOH 15  315 142 HOH HOH A . 
L 3 HOH 16  316 7   HOH HOH A . 
L 3 HOH 17  317 621 HOH HOH A . 
L 3 HOH 18  318 662 HOH HOH A . 
L 3 HOH 19  319 66  HOH HOH A . 
L 3 HOH 20  320 530 HOH HOH A . 
L 3 HOH 21  321 469 HOH HOH A . 
L 3 HOH 22  322 375 HOH HOH A . 
L 3 HOH 23  323 159 HOH HOH A . 
L 3 HOH 24  324 457 HOH HOH A . 
L 3 HOH 25  325 528 HOH HOH A . 
L 3 HOH 26  326 490 HOH HOH A . 
L 3 HOH 27  327 2   HOH HOH A . 
L 3 HOH 28  328 360 HOH HOH A . 
L 3 HOH 29  329 170 HOH HOH A . 
L 3 HOH 30  330 232 HOH HOH A . 
L 3 HOH 31  331 394 HOH HOH A . 
L 3 HOH 32  332 194 HOH HOH A . 
L 3 HOH 33  333 43  HOH HOH A . 
L 3 HOH 34  334 37  HOH HOH A . 
L 3 HOH 35  335 193 HOH HOH A . 
L 3 HOH 36  336 176 HOH HOH A . 
L 3 HOH 37  337 247 HOH HOH A . 
L 3 HOH 38  338 112 HOH HOH A . 
L 3 HOH 39  339 235 HOH HOH A . 
L 3 HOH 40  340 284 HOH HOH A . 
L 3 HOH 41  341 486 HOH HOH A . 
L 3 HOH 42  342 86  HOH HOH A . 
L 3 HOH 43  343 94  HOH HOH A . 
L 3 HOH 44  344 302 HOH HOH A . 
L 3 HOH 45  345 539 HOH HOH A . 
L 3 HOH 46  346 222 HOH HOH A . 
L 3 HOH 47  347 164 HOH HOH A . 
L 3 HOH 48  348 87  HOH HOH A . 
L 3 HOH 49  349 166 HOH HOH A . 
L 3 HOH 50  350 140 HOH HOH A . 
L 3 HOH 51  351 110 HOH HOH A . 
L 3 HOH 52  352 59  HOH HOH A . 
L 3 HOH 53  353 213 HOH HOH A . 
L 3 HOH 54  354 299 HOH HOH A . 
L 3 HOH 55  355 3   HOH HOH A . 
L 3 HOH 56  356 121 HOH HOH A . 
L 3 HOH 57  357 20  HOH HOH A . 
L 3 HOH 58  358 465 HOH HOH A . 
L 3 HOH 59  359 217 HOH HOH A . 
L 3 HOH 60  360 304 HOH HOH A . 
L 3 HOH 61  361 253 HOH HOH A . 
L 3 HOH 62  362 378 HOH HOH A . 
L 3 HOH 63  363 205 HOH HOH A . 
L 3 HOH 64  364 241 HOH HOH A . 
L 3 HOH 65  365 175 HOH HOH A . 
L 3 HOH 66  366 157 HOH HOH A . 
L 3 HOH 67  367 177 HOH HOH A . 
L 3 HOH 68  368 618 HOH HOH A . 
L 3 HOH 69  369 441 HOH HOH A . 
L 3 HOH 70  370 174 HOH HOH A . 
L 3 HOH 71  371 393 HOH HOH A . 
L 3 HOH 72  372 71  HOH HOH A . 
L 3 HOH 73  373 212 HOH HOH A . 
L 3 HOH 74  374 482 HOH HOH A . 
L 3 HOH 75  375 242 HOH HOH A . 
L 3 HOH 76  376 329 HOH HOH A . 
L 3 HOH 77  377 481 HOH HOH A . 
L 3 HOH 78  378 325 HOH HOH A . 
L 3 HOH 79  379 206 HOH HOH A . 
L 3 HOH 80  380 456 HOH HOH A . 
L 3 HOH 81  381 136 HOH HOH A . 
L 3 HOH 82  382 192 HOH HOH A . 
L 3 HOH 83  383 615 HOH HOH A . 
L 3 HOH 84  384 79  HOH HOH A . 
L 3 HOH 85  385 50  HOH HOH A . 
L 3 HOH 86  386 447 HOH HOH A . 
L 3 HOH 87  387 385 HOH HOH A . 
L 3 HOH 88  388 366 HOH HOH A . 
L 3 HOH 89  389 141 HOH HOH A . 
L 3 HOH 90  390 210 HOH HOH A . 
L 3 HOH 91  391 35  HOH HOH A . 
L 3 HOH 92  392 63  HOH HOH A . 
L 3 HOH 93  393 578 HOH HOH A . 
L 3 HOH 94  394 91  HOH HOH A . 
L 3 HOH 95  395 76  HOH HOH A . 
L 3 HOH 96  396 220 HOH HOH A . 
L 3 HOH 97  397 551 HOH HOH A . 
L 3 HOH 98  398 275 HOH HOH A . 
L 3 HOH 99  399 425 HOH HOH A . 
L 3 HOH 100 400 357 HOH HOH A . 
L 3 HOH 101 401 240 HOH HOH A . 
L 3 HOH 102 402 221 HOH HOH A . 
L 3 HOH 103 403 358 HOH HOH A . 
L 3 HOH 104 404 105 HOH HOH A . 
L 3 HOH 105 405 158 HOH HOH A . 
L 3 HOH 106 406 293 HOH HOH A . 
L 3 HOH 107 407 268 HOH HOH A . 
L 3 HOH 108 408 653 HOH HOH A . 
L 3 HOH 109 409 648 HOH HOH A . 
L 3 HOH 110 410 265 HOH HOH A . 
L 3 HOH 111 411 69  HOH HOH A . 
L 3 HOH 112 412 617 HOH HOH A . 
L 3 HOH 113 413 179 HOH HOH A . 
L 3 HOH 114 414 574 HOH HOH A . 
L 3 HOH 115 415 168 HOH HOH A . 
L 3 HOH 116 416 300 HOH HOH A . 
L 3 HOH 117 417 442 HOH HOH A . 
L 3 HOH 118 418 472 HOH HOH A . 
L 3 HOH 119 419 704 HOH HOH A . 
L 3 HOH 120 420 343 HOH HOH A . 
L 3 HOH 121 421 236 HOH HOH A . 
L 3 HOH 122 422 334 HOH HOH A . 
L 3 HOH 123 423 690 HOH HOH A . 
L 3 HOH 124 424 36  HOH HOH A . 
L 3 HOH 125 425 496 HOH HOH A . 
L 3 HOH 126 426 237 HOH HOH A . 
L 3 HOH 127 427 151 HOH HOH A . 
L 3 HOH 128 428 51  HOH HOH A . 
L 3 HOH 129 429 435 HOH HOH A . 
L 3 HOH 130 430 494 HOH HOH A . 
L 3 HOH 131 431 323 HOH HOH A . 
L 3 HOH 132 432 29  HOH HOH A . 
L 3 HOH 133 433 480 HOH HOH A . 
L 3 HOH 134 434 495 HOH HOH A . 
L 3 HOH 135 435 616 HOH HOH A . 
L 3 HOH 136 436 678 HOH HOH A . 
L 3 HOH 137 437 421 HOH HOH A . 
L 3 HOH 138 438 195 HOH HOH A . 
L 3 HOH 139 439 289 HOH HOH A . 
L 3 HOH 140 440 432 HOH HOH A . 
L 3 HOH 141 441 322 HOH HOH A . 
L 3 HOH 142 442 638 HOH HOH A . 
L 3 HOH 143 443 491 HOH HOH A . 
L 3 HOH 144 444 700 HOH HOH A . 
L 3 HOH 145 445 249 HOH HOH A . 
L 3 HOH 146 446 555 HOH HOH A . 
L 3 HOH 147 447 487 HOH HOH A . 
L 3 HOH 148 448 547 HOH HOH A . 
L 3 HOH 149 449 525 HOH HOH A . 
L 3 HOH 150 450 691 HOH HOH A . 
L 3 HOH 151 451 520 HOH HOH A . 
L 3 HOH 152 452 710 HOH HOH A . 
L 3 HOH 153 453 512 HOH HOH A . 
L 3 HOH 154 454 422 HOH HOH A . 
L 3 HOH 155 455 196 HOH HOH A . 
L 3 HOH 156 456 652 HOH HOH A . 
L 3 HOH 157 457 517 HOH HOH A . 
L 3 HOH 158 458 569 HOH HOH A . 
L 3 HOH 159 459 156 HOH HOH A . 
L 3 HOH 160 460 694 HOH HOH A . 
L 3 HOH 161 461 413 HOH HOH A . 
L 3 HOH 162 462 354 HOH HOH A . 
L 3 HOH 163 463 479 HOH HOH A . 
L 3 HOH 164 464 565 HOH HOH A . 
L 3 HOH 165 465 403 HOH HOH A . 
L 3 HOH 166 466 685 HOH HOH A . 
L 3 HOH 167 467 610 HOH HOH A . 
L 3 HOH 168 468 313 HOH HOH A . 
L 3 HOH 169 469 661 HOH HOH A . 
L 3 HOH 170 470 697 HOH HOH A . 
L 3 HOH 171 471 513 HOH HOH A . 
L 3 HOH 172 472 585 HOH HOH A . 
L 3 HOH 173 473 363 HOH HOH A . 
L 3 HOH 174 474 546 HOH HOH A . 
L 3 HOH 175 475 406 HOH HOH A . 
L 3 HOH 176 476 251 HOH HOH A . 
L 3 HOH 177 477 651 HOH HOH A . 
L 3 HOH 178 478 327 HOH HOH A . 
L 3 HOH 179 479 384 HOH HOH A . 
L 3 HOH 180 480 252 HOH HOH A . 
L 3 HOH 181 481 416 HOH HOH A . 
L 3 HOH 182 482 419 HOH HOH A . 
L 3 HOH 183 483 693 HOH HOH A . 
L 3 HOH 184 484 431 HOH HOH A . 
L 3 HOH 185 485 420 HOH HOH A . 
L 3 HOH 186 486 628 HOH HOH A . 
L 3 HOH 187 487 623 HOH HOH A . 
L 3 HOH 188 488 602 HOH HOH A . 
M 3 HOH 1   301 587 HOH HOH B . 
M 3 HOH 2   302 706 HOH HOH B . 
M 3 HOH 3   303 711 HOH HOH B . 
M 3 HOH 4   304 705 HOH HOH B . 
M 3 HOH 5   305 663 HOH HOH B . 
M 3 HOH 6   306 207 HOH HOH B . 
M 3 HOH 7   307 488 HOH HOH B . 
M 3 HOH 8   308 292 HOH HOH B . 
M 3 HOH 9   309 664 HOH HOH B . 
M 3 HOH 10  310 499 HOH HOH B . 
M 3 HOH 11  311 609 HOH HOH B . 
M 3 HOH 12  312 256 HOH HOH B . 
M 3 HOH 13  313 458 HOH HOH B . 
M 3 HOH 14  314 9   HOH HOH B . 
M 3 HOH 15  315 336 HOH HOH B . 
M 3 HOH 16  316 552 HOH HOH B . 
M 3 HOH 17  317 167 HOH HOH B . 
M 3 HOH 18  318 502 HOH HOH B . 
M 3 HOH 19  319 531 HOH HOH B . 
M 3 HOH 20  320 613 HOH HOH B . 
M 3 HOH 21  321 644 HOH HOH B . 
M 3 HOH 22  322 554 HOH HOH B . 
M 3 HOH 23  323 474 HOH HOH B . 
M 3 HOH 24  324 173 HOH HOH B . 
M 3 HOH 25  325 464 HOH HOH B . 
M 3 HOH 26  326 676 HOH HOH B . 
M 3 HOH 27  327 120 HOH HOH B . 
M 3 HOH 28  328 377 HOH HOH B . 
M 3 HOH 29  329 455 HOH HOH B . 
M 3 HOH 30  330 631 HOH HOH B . 
M 3 HOH 31  331 666 HOH HOH B . 
M 3 HOH 32  332 283 HOH HOH B . 
M 3 HOH 33  333 106 HOH HOH B . 
M 3 HOH 34  334 145 HOH HOH B . 
M 3 HOH 35  335 436 HOH HOH B . 
M 3 HOH 36  336 381 HOH HOH B . 
M 3 HOH 37  337 306 HOH HOH B . 
M 3 HOH 38  338 287 HOH HOH B . 
M 3 HOH 39  339 571 HOH HOH B . 
M 3 HOH 40  340 146 HOH HOH B . 
M 3 HOH 41  341 309 HOH HOH B . 
M 3 HOH 42  342 131 HOH HOH B . 
M 3 HOH 43  343 1   HOH HOH B . 
M 3 HOH 44  344 68  HOH HOH B . 
M 3 HOH 45  345 92  HOH HOH B . 
M 3 HOH 46  346 65  HOH HOH B . 
M 3 HOH 47  347 257 HOH HOH B . 
M 3 HOH 48  348 348 HOH HOH B . 
M 3 HOH 49  349 449 HOH HOH B . 
M 3 HOH 50  350 42  HOH HOH B . 
M 3 HOH 51  351 48  HOH HOH B . 
M 3 HOH 52  352 32  HOH HOH B . 
M 3 HOH 53  353 246 HOH HOH B . 
M 3 HOH 54  354 114 HOH HOH B . 
M 3 HOH 55  355 107 HOH HOH B . 
M 3 HOH 56  356 117 HOH HOH B . 
M 3 HOH 57  357 186 HOH HOH B . 
M 3 HOH 58  358 483 HOH HOH B . 
M 3 HOH 59  359 510 HOH HOH B . 
M 3 HOH 60  360 261 HOH HOH B . 
M 3 HOH 61  361 277 HOH HOH B . 
M 3 HOH 62  362 31  HOH HOH B . 
M 3 HOH 63  363 620 HOH HOH B . 
M 3 HOH 64  364 150 HOH HOH B . 
M 3 HOH 65  365 344 HOH HOH B . 
M 3 HOH 66  366 450 HOH HOH B . 
M 3 HOH 67  367 70  HOH HOH B . 
M 3 HOH 68  368 370 HOH HOH B . 
M 3 HOH 69  369 88  HOH HOH B . 
M 3 HOH 70  370 340 HOH HOH B . 
M 3 HOH 71  371 119 HOH HOH B . 
M 3 HOH 72  372 503 HOH HOH B . 
M 3 HOH 73  373 108 HOH HOH B . 
M 3 HOH 74  374 97  HOH HOH B . 
M 3 HOH 75  375 258 HOH HOH B . 
M 3 HOH 76  376 634 HOH HOH B . 
M 3 HOH 77  377 15  HOH HOH B . 
M 3 HOH 78  378 471 HOH HOH B . 
M 3 HOH 79  379 234 HOH HOH B . 
M 3 HOH 80  380 185 HOH HOH B . 
M 3 HOH 81  381 274 HOH HOH B . 
M 3 HOH 82  382 238 HOH HOH B . 
M 3 HOH 83  383 577 HOH HOH B . 
M 3 HOH 84  384 67  HOH HOH B . 
M 3 HOH 85  385 434 HOH HOH B . 
M 3 HOH 86  386 445 HOH HOH B . 
M 3 HOH 87  387 227 HOH HOH B . 
M 3 HOH 88  388 61  HOH HOH B . 
M 3 HOH 89  389 260 HOH HOH B . 
M 3 HOH 90  390 109 HOH HOH B . 
M 3 HOH 91  391 501 HOH HOH B . 
M 3 HOH 92  392 362 HOH HOH B . 
M 3 HOH 93  393 439 HOH HOH B . 
M 3 HOH 94  394 118 HOH HOH B . 
M 3 HOH 95  395 96  HOH HOH B . 
M 3 HOH 96  396 46  HOH HOH B . 
M 3 HOH 97  397 62  HOH HOH B . 
M 3 HOH 98  398 200 HOH HOH B . 
M 3 HOH 99  399 203 HOH HOH B . 
M 3 HOH 100 400 21  HOH HOH B . 
M 3 HOH 101 401 26  HOH HOH B . 
M 3 HOH 102 402 338 HOH HOH B . 
M 3 HOH 103 403 372 HOH HOH B . 
M 3 HOH 104 404 16  HOH HOH B . 
M 3 HOH 105 405 55  HOH HOH B . 
M 3 HOH 106 406 53  HOH HOH B . 
M 3 HOH 107 407 359 HOH HOH B . 
M 3 HOH 108 408 230 HOH HOH B . 
M 3 HOH 109 409 180 HOH HOH B . 
M 3 HOH 110 410 709 HOH HOH B . 
M 3 HOH 111 411 152 HOH HOH B . 
M 3 HOH 112 412 307 HOH HOH B . 
M 3 HOH 113 413 95  HOH HOH B . 
M 3 HOH 114 414 11  HOH HOH B . 
M 3 HOH 115 415 123 HOH HOH B . 
M 3 HOH 116 416 529 HOH HOH B . 
M 3 HOH 117 417 126 HOH HOH B . 
M 3 HOH 118 418 498 HOH HOH B . 
M 3 HOH 119 419 557 HOH HOH B . 
M 3 HOH 120 420 459 HOH HOH B . 
M 3 HOH 121 421 99  HOH HOH B . 
M 3 HOH 122 422 18  HOH HOH B . 
M 3 HOH 123 423 438 HOH HOH B . 
M 3 HOH 124 424 599 HOH HOH B . 
M 3 HOH 125 425 296 HOH HOH B . 
M 3 HOH 126 426 612 HOH HOH B . 
M 3 HOH 127 427 34  HOH HOH B . 
M 3 HOH 128 428 314 HOH HOH B . 
M 3 HOH 129 429 124 HOH HOH B . 
M 3 HOH 130 430 444 HOH HOH B . 
M 3 HOH 131 431 350 HOH HOH B . 
M 3 HOH 132 432 169 HOH HOH B . 
M 3 HOH 133 433 654 HOH HOH B . 
M 3 HOH 134 434 243 HOH HOH B . 
M 3 HOH 135 435 231 HOH HOH B . 
M 3 HOH 136 436 113 HOH HOH B . 
M 3 HOH 137 437 558 HOH HOH B . 
M 3 HOH 138 438 440 HOH HOH B . 
M 3 HOH 139 439 349 HOH HOH B . 
M 3 HOH 140 440 374 HOH HOH B . 
M 3 HOH 141 441 521 HOH HOH B . 
M 3 HOH 142 442 595 HOH HOH B . 
M 3 HOH 143 443 541 HOH HOH B . 
M 3 HOH 144 444 588 HOH HOH B . 
M 3 HOH 145 445 24  HOH HOH B . 
M 3 HOH 146 446 562 HOH HOH B . 
M 3 HOH 147 447 201 HOH HOH B . 
M 3 HOH 148 448 659 HOH HOH B . 
M 3 HOH 149 449 695 HOH HOH B . 
M 3 HOH 150 450 708 HOH HOH B . 
M 3 HOH 151 451 665 HOH HOH B . 
M 3 HOH 152 452 522 HOH HOH B . 
M 3 HOH 153 453 576 HOH HOH B . 
M 3 HOH 154 454 476 HOH HOH B . 
M 3 HOH 155 455 163 HOH HOH B . 
M 3 HOH 156 456 596 HOH HOH B . 
M 3 HOH 157 457 497 HOH HOH B . 
M 3 HOH 158 458 38  HOH HOH B . 
M 3 HOH 159 459 341 HOH HOH B . 
M 3 HOH 160 460 427 HOH HOH B . 
M 3 HOH 161 461 409 HOH HOH B . 
M 3 HOH 162 462 614 HOH HOH B . 
M 3 HOH 163 463 567 HOH HOH B . 
M 3 HOH 164 464 645 HOH HOH B . 
M 3 HOH 165 465 538 HOH HOH B . 
M 3 HOH 166 466 632 HOH HOH B . 
M 3 HOH 167 467 523 HOH HOH B . 
M 3 HOH 168 468 566 HOH HOH B . 
M 3 HOH 169 469 629 HOH HOH B . 
M 3 HOH 170 470 692 HOH HOH B . 
M 3 HOH 171 471 544 HOH HOH B . 
M 3 HOH 172 472 134 HOH HOH B . 
M 3 HOH 173 473 594 HOH HOH B . 
M 3 HOH 174 474 575 HOH HOH B . 
M 3 HOH 175 475 543 HOH HOH B . 
M 3 HOH 176 476 516 HOH HOH B . 
M 3 HOH 177 477 633 HOH HOH B . 
M 3 HOH 178 478 414 HOH HOH B . 
M 3 HOH 179 479 672 HOH HOH B . 
M 3 HOH 180 480 506 HOH HOH B . 
M 3 HOH 181 481 135 HOH HOH B . 
M 3 HOH 182 482 295 HOH HOH B . 
M 3 HOH 183 483 714 HOH HOH B . 
M 3 HOH 184 484 423 HOH HOH B . 
M 3 HOH 185 485 703 HOH HOH B . 
M 3 HOH 186 486 518 HOH HOH B . 
M 3 HOH 187 487 524 HOH HOH B . 
N 3 HOH 1   301 650 HOH HOH C . 
N 3 HOH 2   302 606 HOH HOH C . 
N 3 HOH 3   303 622 HOH HOH C . 
N 3 HOH 4   304 484 HOH HOH C . 
N 3 HOH 5   305 689 HOH HOH C . 
N 3 HOH 6   306 580 HOH HOH C . 
N 3 HOH 7   307 389 HOH HOH C . 
N 3 HOH 8   308 254 HOH HOH C . 
N 3 HOH 9   309 273 HOH HOH C . 
N 3 HOH 10  310 353 HOH HOH C . 
N 3 HOH 11  311 137 HOH HOH C . 
N 3 HOH 12  312 102 HOH HOH C . 
N 3 HOH 13  313 473 HOH HOH C . 
N 3 HOH 14  314 5   HOH HOH C . 
N 3 HOH 15  315 138 HOH HOH C . 
N 3 HOH 16  316 171 HOH HOH C . 
N 3 HOH 17  317 316 HOH HOH C . 
N 3 HOH 18  318 540 HOH HOH C . 
N 3 HOH 19  319 154 HOH HOH C . 
N 3 HOH 20  320 371 HOH HOH C . 
N 3 HOH 21  321 54  HOH HOH C . 
N 3 HOH 22  322 553 HOH HOH C . 
N 3 HOH 23  323 267 HOH HOH C . 
N 3 HOH 24  324 183 HOH HOH C . 
N 3 HOH 25  325 139 HOH HOH C . 
N 3 HOH 26  326 25  HOH HOH C . 
N 3 HOH 27  327 6   HOH HOH C . 
N 3 HOH 28  328 468 HOH HOH C . 
N 3 HOH 29  329 90  HOH HOH C . 
N 3 HOH 30  330 233 HOH HOH C . 
N 3 HOH 31  331 570 HOH HOH C . 
N 3 HOH 32  332 52  HOH HOH C . 
N 3 HOH 33  333 23  HOH HOH C . 
N 3 HOH 34  334 668 HOH HOH C . 
N 3 HOH 35  335 165 HOH HOH C . 
N 3 HOH 36  336 443 HOH HOH C . 
N 3 HOH 37  337 28  HOH HOH C . 
N 3 HOH 38  338 73  HOH HOH C . 
N 3 HOH 39  339 229 HOH HOH C . 
N 3 HOH 40  340 492 HOH HOH C . 
N 3 HOH 41  341 400 HOH HOH C . 
N 3 HOH 42  342 294 HOH HOH C . 
N 3 HOH 43  343 276 HOH HOH C . 
N 3 HOH 44  344 298 HOH HOH C . 
N 3 HOH 45  345 45  HOH HOH C . 
N 3 HOH 46  346 74  HOH HOH C . 
N 3 HOH 47  347 204 HOH HOH C . 
N 3 HOH 48  348 60  HOH HOH C . 
N 3 HOH 49  349 589 HOH HOH C . 
N 3 HOH 50  350 527 HOH HOH C . 
N 3 HOH 51  351 288 HOH HOH C . 
N 3 HOH 52  352 144 HOH HOH C . 
N 3 HOH 53  353 331 HOH HOH C . 
N 3 HOH 54  354 339 HOH HOH C . 
N 3 HOH 55  355 368 HOH HOH C . 
N 3 HOH 56  356 147 HOH HOH C . 
N 3 HOH 57  357 244 HOH HOH C . 
N 3 HOH 58  358 85  HOH HOH C . 
N 3 HOH 59  359 369 HOH HOH C . 
N 3 HOH 60  360 319 HOH HOH C . 
N 3 HOH 61  361 127 HOH HOH C . 
N 3 HOH 62  362 4   HOH HOH C . 
N 3 HOH 63  363 189 HOH HOH C . 
N 3 HOH 64  364 286 HOH HOH C . 
N 3 HOH 65  365 116 HOH HOH C . 
N 3 HOH 66  366 466 HOH HOH C . 
N 3 HOH 67  367 579 HOH HOH C . 
N 3 HOH 68  368 214 HOH HOH C . 
N 3 HOH 69  369 33  HOH HOH C . 
N 3 HOH 70  370 129 HOH HOH C . 
N 3 HOH 71  371 93  HOH HOH C . 
N 3 HOH 72  372 78  HOH HOH C . 
N 3 HOH 73  373 181 HOH HOH C . 
N 3 HOH 74  374 89  HOH HOH C . 
N 3 HOH 75  375 280 HOH HOH C . 
N 3 HOH 76  376 153 HOH HOH C . 
N 3 HOH 77  377 184 HOH HOH C . 
N 3 HOH 78  378 84  HOH HOH C . 
N 3 HOH 79  379 535 HOH HOH C . 
N 3 HOH 80  380 342 HOH HOH C . 
N 3 HOH 81  381 58  HOH HOH C . 
N 3 HOH 82  382 128 HOH HOH C . 
N 3 HOH 83  383 39  HOH HOH C . 
N 3 HOH 84  384 49  HOH HOH C . 
N 3 HOH 85  385 301 HOH HOH C . 
N 3 HOH 86  386 462 HOH HOH C . 
N 3 HOH 87  387 216 HOH HOH C . 
N 3 HOH 88  388 397 HOH HOH C . 
N 3 HOH 89  389 361 HOH HOH C . 
N 3 HOH 90  390 199 HOH HOH C . 
N 3 HOH 91  391 75  HOH HOH C . 
N 3 HOH 92  392 30  HOH HOH C . 
N 3 HOH 93  393 346 HOH HOH C . 
N 3 HOH 94  394 12  HOH HOH C . 
N 3 HOH 95  395 22  HOH HOH C . 
N 3 HOH 96  396 10  HOH HOH C . 
N 3 HOH 97  397 208 HOH HOH C . 
N 3 HOH 98  398 100 HOH HOH C . 
N 3 HOH 99  399 13  HOH HOH C . 
N 3 HOH 100 400 245 HOH HOH C . 
N 3 HOH 101 401 437 HOH HOH C . 
N 3 HOH 102 402 228 HOH HOH C . 
N 3 HOH 103 403 335 HOH HOH C . 
N 3 HOH 104 404 282 HOH HOH C . 
N 3 HOH 105 405 198 HOH HOH C . 
N 3 HOH 106 406 19  HOH HOH C . 
N 3 HOH 107 407 271 HOH HOH C . 
N 3 HOH 108 408 133 HOH HOH C . 
N 3 HOH 109 409 182 HOH HOH C . 
N 3 HOH 110 410 583 HOH HOH C . 
N 3 HOH 111 411 263 HOH HOH C . 
N 3 HOH 112 412 453 HOH HOH C . 
N 3 HOH 113 413 379 HOH HOH C . 
N 3 HOH 114 414 160 HOH HOH C . 
N 3 HOH 115 415 641 HOH HOH C . 
N 3 HOH 116 416 684 HOH HOH C . 
N 3 HOH 117 417 345 HOH HOH C . 
N 3 HOH 118 418 428 HOH HOH C . 
N 3 HOH 119 419 382 HOH HOH C . 
N 3 HOH 120 420 670 HOH HOH C . 
N 3 HOH 121 421 563 HOH HOH C . 
N 3 HOH 122 422 215 HOH HOH C . 
N 3 HOH 123 423 259 HOH HOH C . 
N 3 HOH 124 424 312 HOH HOH C . 
N 3 HOH 125 425 507 HOH HOH C . 
N 3 HOH 126 426 218 HOH HOH C . 
N 3 HOH 127 427 625 HOH HOH C . 
N 3 HOH 128 428 712 HOH HOH C . 
N 3 HOH 129 429 545 HOH HOH C . 
N 3 HOH 130 430 401 HOH HOH C . 
N 3 HOH 131 431 537 HOH HOH C . 
N 3 HOH 132 432 701 HOH HOH C . 
N 3 HOH 133 433 646 HOH HOH C . 
N 3 HOH 134 434 573 HOH HOH C . 
N 3 HOH 135 435 477 HOH HOH C . 
N 3 HOH 136 436 608 HOH HOH C . 
N 3 HOH 137 437 568 HOH HOH C . 
N 3 HOH 138 438 584 HOH HOH C . 
N 3 HOH 139 439 508 HOH HOH C . 
N 3 HOH 140 440 392 HOH HOH C . 
N 3 HOH 141 441 417 HOH HOH C . 
N 3 HOH 142 442 429 HOH HOH C . 
N 3 HOH 143 443 407 HOH HOH C . 
N 3 HOH 144 444 426 HOH HOH C . 
N 3 HOH 145 445 285 HOH HOH C . 
N 3 HOH 146 446 291 HOH HOH C . 
N 3 HOH 147 447 560 HOH HOH C . 
N 3 HOH 148 448 415 HOH HOH C . 
N 3 HOH 149 449 515 HOH HOH C . 
N 3 HOH 150 450 411 HOH HOH C . 
N 3 HOH 151 451 405 HOH HOH C . 
N 3 HOH 152 452 582 HOH HOH C . 
N 3 HOH 153 453 549 HOH HOH C . 
N 3 HOH 154 454 636 HOH HOH C . 
N 3 HOH 155 455 581 HOH HOH C . 
N 3 HOH 156 456 673 HOH HOH C . 
N 3 HOH 157 457 430 HOH HOH C . 
O 3 HOH 1   301 713 HOH HOH D . 
O 3 HOH 2   302 591 HOH HOH D . 
O 3 HOH 3   303 649 HOH HOH D . 
O 3 HOH 4   304 590 HOH HOH D . 
O 3 HOH 5   305 642 HOH HOH D . 
O 3 HOH 6   306 103 HOH HOH D . 
O 3 HOH 7   307 702 HOH HOH D . 
O 3 HOH 8   308 671 HOH HOH D . 
O 3 HOH 9   309 148 HOH HOH D . 
O 3 HOH 10  310 115 HOH HOH D . 
O 3 HOH 11  311 80  HOH HOH D . 
O 3 HOH 12  312 390 HOH HOH D . 
O 3 HOH 13  313 82  HOH HOH D . 
O 3 HOH 14  314 607 HOH HOH D . 
O 3 HOH 15  315 367 HOH HOH D . 
O 3 HOH 16  316 448 HOH HOH D . 
O 3 HOH 17  317 315 HOH HOH D . 
O 3 HOH 18  318 57  HOH HOH D . 
O 3 HOH 19  319 387 HOH HOH D . 
O 3 HOH 20  320 364 HOH HOH D . 
O 3 HOH 21  321 398 HOH HOH D . 
O 3 HOH 22  322 41  HOH HOH D . 
O 3 HOH 23  323 347 HOH HOH D . 
O 3 HOH 24  324 467 HOH HOH D . 
O 3 HOH 25  325 386 HOH HOH D . 
O 3 HOH 26  326 433 HOH HOH D . 
O 3 HOH 27  327 202 HOH HOH D . 
O 3 HOH 28  328 493 HOH HOH D . 
O 3 HOH 29  329 122 HOH HOH D . 
O 3 HOH 30  330 489 HOH HOH D . 
O 3 HOH 31  331 40  HOH HOH D . 
O 3 HOH 32  332 279 HOH HOH D . 
O 3 HOH 33  333 356 HOH HOH D . 
O 3 HOH 34  334 451 HOH HOH D . 
O 3 HOH 35  335 461 HOH HOH D . 
O 3 HOH 36  336 365 HOH HOH D . 
O 3 HOH 37  337 255 HOH HOH D . 
O 3 HOH 38  338 526 HOH HOH D . 
O 3 HOH 39  339 556 HOH HOH D . 
O 3 HOH 40  340 266 HOH HOH D . 
O 3 HOH 41  341 272 HOH HOH D . 
O 3 HOH 42  342 44  HOH HOH D . 
O 3 HOH 43  343 308 HOH HOH D . 
O 3 HOH 44  344 101 HOH HOH D . 
O 3 HOH 45  345 303 HOH HOH D . 
O 3 HOH 46  346 478 HOH HOH D . 
O 3 HOH 47  347 47  HOH HOH D . 
O 3 HOH 48  348 211 HOH HOH D . 
O 3 HOH 49  349 162 HOH HOH D . 
O 3 HOH 50  350 83  HOH HOH D . 
O 3 HOH 51  351 226 HOH HOH D . 
O 3 HOH 52  352 500 HOH HOH D . 
O 3 HOH 53  353 337 HOH HOH D . 
O 3 HOH 54  354 388 HOH HOH D . 
O 3 HOH 55  355 533 HOH HOH D . 
O 3 HOH 56  356 225 HOH HOH D . 
O 3 HOH 57  357 77  HOH HOH D . 
O 3 HOH 58  358 155 HOH HOH D . 
O 3 HOH 59  359 320 HOH HOH D . 
O 3 HOH 60  360 485 HOH HOH D . 
O 3 HOH 61  361 376 HOH HOH D . 
O 3 HOH 62  362 281 HOH HOH D . 
O 3 HOH 63  363 98  HOH HOH D . 
O 3 HOH 64  364 269 HOH HOH D . 
O 3 HOH 65  365 111 HOH HOH D . 
O 3 HOH 66  366 17  HOH HOH D . 
O 3 HOH 67  367 130 HOH HOH D . 
O 3 HOH 68  368 660 HOH HOH D . 
O 3 HOH 69  369 318 HOH HOH D . 
O 3 HOH 70  370 311 HOH HOH D . 
O 3 HOH 71  371 224 HOH HOH D . 
O 3 HOH 72  372 328 HOH HOH D . 
O 3 HOH 73  373 27  HOH HOH D . 
O 3 HOH 74  374 190 HOH HOH D . 
O 3 HOH 75  375 262 HOH HOH D . 
O 3 HOH 76  376 56  HOH HOH D . 
O 3 HOH 77  377 373 HOH HOH D . 
O 3 HOH 78  378 270 HOH HOH D . 
O 3 HOH 79  379 604 HOH HOH D . 
O 3 HOH 80  380 72  HOH HOH D . 
O 3 HOH 81  381 191 HOH HOH D . 
O 3 HOH 82  382 532 HOH HOH D . 
O 3 HOH 83  383 536 HOH HOH D . 
O 3 HOH 84  384 297 HOH HOH D . 
O 3 HOH 85  385 383 HOH HOH D . 
O 3 HOH 86  386 188 HOH HOH D . 
O 3 HOH 87  387 104 HOH HOH D . 
O 3 HOH 88  388 707 HOH HOH D . 
O 3 HOH 89  389 333 HOH HOH D . 
O 3 HOH 90  390 125 HOH HOH D . 
O 3 HOH 91  391 463 HOH HOH D . 
O 3 HOH 92  392 310 HOH HOH D . 
O 3 HOH 93  393 305 HOH HOH D . 
O 3 HOH 94  394 64  HOH HOH D . 
O 3 HOH 95  395 351 HOH HOH D . 
O 3 HOH 96  396 321 HOH HOH D . 
O 3 HOH 97  397 161 HOH HOH D . 
O 3 HOH 98  398 187 HOH HOH D . 
O 3 HOH 99  399 223 HOH HOH D . 
O 3 HOH 100 400 172 HOH HOH D . 
O 3 HOH 101 401 317 HOH HOH D . 
O 3 HOH 102 402 149 HOH HOH D . 
O 3 HOH 103 403 132 HOH HOH D . 
O 3 HOH 104 404 391 HOH HOH D . 
O 3 HOH 105 405 326 HOH HOH D . 
O 3 HOH 106 406 143 HOH HOH D . 
O 3 HOH 107 407 534 HOH HOH D . 
O 3 HOH 108 408 178 HOH HOH D . 
O 3 HOH 109 409 446 HOH HOH D . 
O 3 HOH 110 410 395 HOH HOH D . 
O 3 HOH 111 411 219 HOH HOH D . 
O 3 HOH 112 412 688 HOH HOH D . 
O 3 HOH 113 413 605 HOH HOH D . 
O 3 HOH 114 414 603 HOH HOH D . 
O 3 HOH 115 415 264 HOH HOH D . 
O 3 HOH 116 416 355 HOH HOH D . 
O 3 HOH 117 417 505 HOH HOH D . 
O 3 HOH 118 418 278 HOH HOH D . 
O 3 HOH 119 419 324 HOH HOH D . 
O 3 HOH 120 420 197 HOH HOH D . 
O 3 HOH 121 421 475 HOH HOH D . 
O 3 HOH 122 422 597 HOH HOH D . 
O 3 HOH 123 423 209 HOH HOH D . 
O 3 HOH 124 424 239 HOH HOH D . 
O 3 HOH 125 425 699 HOH HOH D . 
O 3 HOH 126 426 683 HOH HOH D . 
O 3 HOH 127 427 682 HOH HOH D . 
O 3 HOH 128 428 504 HOH HOH D . 
O 3 HOH 129 429 452 HOH HOH D . 
O 3 HOH 130 430 592 HOH HOH D . 
O 3 HOH 131 431 290 HOH HOH D . 
O 3 HOH 132 432 564 HOH HOH D . 
O 3 HOH 133 433 248 HOH HOH D . 
O 3 HOH 134 434 404 HOH HOH D . 
O 3 HOH 135 435 460 HOH HOH D . 
O 3 HOH 136 436 598 HOH HOH D . 
O 3 HOH 137 437 698 HOH HOH D . 
O 3 HOH 138 438 470 HOH HOH D . 
O 3 HOH 139 439 396 HOH HOH D . 
O 3 HOH 140 440 593 HOH HOH D . 
O 3 HOH 141 441 559 HOH HOH D . 
O 3 HOH 142 442 611 HOH HOH D . 
O 3 HOH 143 443 680 HOH HOH D . 
O 3 HOH 144 444 675 HOH HOH D . 
O 3 HOH 145 445 14  HOH HOH D . 
O 3 HOH 146 446 669 HOH HOH D . 
O 3 HOH 147 447 511 HOH HOH D . 
O 3 HOH 148 448 561 HOH HOH D . 
O 3 HOH 149 449 686 HOH HOH D . 
O 3 HOH 150 450 399 HOH HOH D . 
O 3 HOH 151 451 600 HOH HOH D . 
O 3 HOH 152 452 635 HOH HOH D . 
O 3 HOH 153 453 601 HOH HOH D . 
O 3 HOH 154 454 408 HOH HOH D . 
O 3 HOH 155 455 687 HOH HOH D . 
O 3 HOH 156 456 250 HOH HOH D . 
O 3 HOH 157 457 509 HOH HOH D . 
O 3 HOH 158 458 410 HOH HOH D . 
O 3 HOH 159 459 657 HOH HOH D . 
O 3 HOH 160 460 548 HOH HOH D . 
O 3 HOH 161 461 667 HOH HOH D . 
O 3 HOH 162 462 514 HOH HOH D . 
O 3 HOH 163 463 640 HOH HOH D . 
O 3 HOH 164 464 619 HOH HOH D . 
O 3 HOH 165 465 716 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? 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                   97.66 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XZY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.231 
_cell.length_a_esd                 ? 
_cell.length_b                     137.536 
_cell.length_b_esd                 ? 
_cell.length_c                     52.857 
_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                         8XZY 
_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                   8XZY 
_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          43.77 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '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         2023-09-29 
_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                                       8XZY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_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                                     70638 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          26.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.363 
_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                                0.050 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       266971 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.042 
_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 
1.75 1.81  ? ? ? ? ? ? 6664 ? ? ? ? ? ? ? ? ? ? ? 4.1 1.380 ? ? 0.140 0.065 ? 1  1 0.988 0.997 ? 90.4 ? 0.123 ? ? ? ? ? ? ? ? ? 
1.81 1.89  ? ? ? ? ? ? 6773 ? ? ? ? ? ? ? ? ? ? ? 4.0 1.422 ? ? 0.114 0.054 ? 2  1 0.992 0.998 ? 92.2 ? 0.099 ? ? ? ? ? ? ? ? ? 
1.89 1.97  ? ? ? ? ? ? 6926 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.476 ? ? 0.088 0.043 ? 3  1 0.995 0.999 ? 94.4 ? 0.076 ? ? ? ? ? ? ? ? ? 
1.97 2.07  ? ? ? ? ? ? 7020 ? ? ? ? ? ? ? ? ? ? ? 3.6 1.360 ? ? 0.071 0.036 ? 4  1 0.995 0.999 ? 95.3 ? 0.061 ? ? ? ? ? ? ? ? ? 
2.07 2.20  ? ? ? ? ? ? 7142 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.382 ? ? 0.062 0.031 ? 5  1 0.996 0.999 ? 97.0 ? 0.053 ? ? ? ? ? ? ? ? ? 
2.20 2.37  ? ? ? ? ? ? 7223 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.337 ? ? 0.057 0.029 ? 6  1 0.996 0.999 ? 98.0 ? 0.049 ? ? ? ? ? ? ? ? ? 
2.37 2.61  ? ? ? ? ? ? 7309 ? ? ? ? ? ? ? ? ? ? ? 4.1 1.295 ? ? 0.055 0.026 ? 7  1 0.997 0.999 ? 99.1 ? 0.048 ? ? ? ? ? ? ? ? ? 
2.61 2.99  ? ? ? ? ? ? 7305 ? ? ? ? ? ? ? ? ? ? ? 4.0 1.342 ? ? 0.049 0.024 ? 8  1 0.997 0.999 ? 99.1 ? 0.043 ? ? ? ? ? ? ? ? ? 
2.99 3.77  ? ? ? ? ? ? 7181 ? ? ? ? ? ? ? ? ? ? ? 3.5 1.357 ? ? 0.043 0.022 ? 9  1 0.997 0.999 ? 96.9 ? 0.036 ? ? ? ? ? ? ? ? ? 
3.77 25.00 ? ? ? ? ? ? 7095 ? ? ? ? ? ? ? ? ? ? ? 3.1 1.265 ? ? 0.044 0.025 ? 10 1 0.996 0.999 ? 95.2 ? 0.036 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            1.11 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.44 
_refine.aniso_B[2][2]                            -0.05 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.91 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.855 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.914 
_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                                 8XZY 
_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                            1.75 
_refine.ls_d_res_low                             23.29 
_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                     67221 
_refine.ls_number_reflns_R_free                  3368 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.44 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18301 
_refine.ls_R_factor_R_free                       0.22800 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18071 
_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                       0.131 
_refine.pdbx_overall_ESU_R_Free                  0.129 
_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                             2.227 
_refine.overall_SU_ML                            0.074 
_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                       1.75 
_refine_hist.d_res_low                        23.29 
_refine_hist.number_atoms_solvent             716 
_refine_hist.number_atoms_total               6575 
_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        5852 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         7 
_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  6024  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  4768  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.734  1.650  8248  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.553  1.562  11132 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.380  5.000  752   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 39.725 24.557 316   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.875 15.000 800   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.850 15.000 12    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.084  0.200  788   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  7036  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1336  ? 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' ? 1.899  1.919  3020  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.895  1.919  3019  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.637  2.869  3768  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.637  2.870  3769  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.981  2.231  3004  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.980  2.229  3002  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.438  3.239  4480  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.049  23.826 7053  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.918  23.161 6887  ? 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                       1.752 
_refine_ls_shell.d_res_low                        1.798 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             212 
_refine_ls_shell.number_reflns_R_work             4525 
_refine_ls_shell.percent_reflns_obs               86.69 
_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                  0.167 
_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                  0.237 
# 
_struct.entry_id                     8XZY 
_struct.title                        'Structure of a xylanase Xyl-1 M4 mutant E175A' 
_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        8XZY 
_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 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
# 
_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 8XZY A 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
2 1 8XZY B 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
3 1 8XZY C 14 ? 201 ? Q0CMZ1 33 ? 220 ? 2 189 
4 1 8XZY 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 8XZY GLY A 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 1  
1 8XZY ALA A 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 2  
1 8XZY GLY A 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  3  
1 8XZY ALA A 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  4  
1 8XZY GLY A 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  5  
1 8XZY ALA A 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  6  
1 8XZY GLY A 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  7  
1 8XZY ALA A 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  8  
1 8XZY GLY A 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  9  
1 8XZY ALA A 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  10 
1 8XZY GLY A 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  11 
1 8XZY MET A 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   12 
1 8XZY GLU A 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   13 
1 8XZY PRO A 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  14 
1 8XZY GLN A 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  15 
1 8XZY GLN A 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 16 
1 8XZY HIS A 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 17 
1 8XZY ALA A 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 18 
2 8XZY GLY B 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 19 
2 8XZY ALA B 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 20 
2 8XZY GLY B 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  21 
2 8XZY ALA B 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  22 
2 8XZY GLY B 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  23 
2 8XZY ALA B 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  24 
2 8XZY GLY B 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  25 
2 8XZY ALA B 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  26 
2 8XZY GLY B 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  27 
2 8XZY ALA B 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  28 
2 8XZY GLY B 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  29 
2 8XZY MET B 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   30 
2 8XZY GLU B 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   31 
2 8XZY PRO B 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  32 
2 8XZY GLN B 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  33 
2 8XZY GLN B 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 34 
2 8XZY HIS B 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 35 
2 8XZY ALA B 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 36 
3 8XZY GLY C 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 37 
3 8XZY ALA C 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 38 
3 8XZY GLY C 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  39 
3 8XZY ALA C 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  40 
3 8XZY GLY C 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  41 
3 8XZY ALA C 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  42 
3 8XZY GLY C 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  43 
3 8XZY ALA C 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  44 
3 8XZY GLY C 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  45 
3 8XZY ALA C 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  46 
3 8XZY GLY C 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  47 
3 8XZY MET C 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   48 
3 8XZY GLU C 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   49 
3 8XZY PRO C 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  50 
3 8XZY GLN C 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  51 
3 8XZY GLN C 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 52 
3 8XZY HIS C 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 53 
3 8XZY ALA C 188 ? UNP Q0CMZ1 GLU 207 'engineered mutation' 176 54 
4 8XZY GLY D 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 55 
4 8XZY ALA D 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 56 
4 8XZY GLY D 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  57 
4 8XZY ALA D 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  58 
4 8XZY GLY D 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  59 
4 8XZY ALA D 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  60 
4 8XZY GLY D 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  61 
4 8XZY ALA D 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  62 
4 8XZY GLY D 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  63 
4 8XZY ALA D 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  64 
4 8XZY GLY D 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  65 
4 8XZY MET D 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   66 
4 8XZY GLU D 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      1   67 
4 8XZY PRO D 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 31  68 
4 8XZY GLN D 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 34  69 
4 8XZY GLN D 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 118 70 
4 8XZY HIS D 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 168 71 
4 8XZY 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         -27  ? 
1 'SSA (A^2)'  8180 ? 
2 'ABSA (A^2)' 90   ? 
2 MORE         -24  ? 
2 'SSA (A^2)'  8110 ? 
3 'ABSA (A^2)' 90   ? 
3 MORE         -23  ? 
3 'SSA (A^2)'  8180 ? 
4 'ABSA (A^2)' 90   ? 
4 MORE         -26  ? 
4 'SSA (A^2)'  8250 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,L 
2 1 B,G,H,M 
3 1 C,I,N   
4 1 D,J,K,O 
# 
_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 THR A 163 ? ALA A 173 ? THR A 151 ALA A 161 1 ? 11 
HELX_P HELX_P2 AA2 THR B 163 ? ALA B 173 ? THR B 151 ALA B 161 1 ? 11 
HELX_P HELX_P3 AA3 THR C 163 ? ALA C 173 ? THR C 151 ALA C 161 1 ? 11 
HELX_P HELX_P4 AA4 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 
metalc1  metalc ? ? A PHE 104 O   ? ? ? 1_555 F ZN  . ZN ? ? A PHE 92  A ZN  201 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc2  metalc ? ? A ASP 154 OD1 ? ? ? 1_555 E ZN  . ZN ? ? A ASP 142 A ZN  200 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc3  metalc ? ? A ASP 154 OD2 ? ? ? 1_555 E ZN  . ZN ? ? A ASP 142 A ZN  200 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc4  metalc ? ? A HIS 155 ND1 ? ? ? 1_555 F ZN  . ZN ? ? A HIS 143 A ZN  201 1_555 ? ? ? ? ? ? ? 1.904 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 L HOH . O  ? ? A ZN  200 A HOH 419 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc6  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? A ZN  200 B HOH 320 1_554 ? ? ? ? ? ? ? 2.200 ? ? 
metalc7  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? A ZN  200 B HOH 331 1_554 ? ? ? ? ? ? ? 1.954 ? ? 
metalc8  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? A ZN  200 B HOH 448 1_554 ? ? ? ? ? ? ? 2.354 ? ? 
metalc9  metalc ? ? F ZN  .   ZN  ? ? ? 1_555 L HOH . O  ? ? A ZN  201 A HOH 368 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc10 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 L HOH . O  ? ? A ZN  201 A HOH 412 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc11 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 L HOH . O  ? ? A ZN  201 A HOH 435 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc12 metalc ? ? B ASP 154 OD1 ? ? ? 1_555 G ZN  . ZN ? ? B ASP 142 B ZN  200 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc13 metalc ? ? B ASP 154 OD2 ? ? ? 1_555 G ZN  . ZN ? ? B ASP 142 B ZN  200 1_555 ? ? ? ? ? ? ? 2.251 ? ? 
metalc14 metalc ? ? B HIS 155 ND1 ? ? ? 1_555 H ZN  . ZN ? ? B HIS 143 B ZN  201 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc15 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? B ZN  200 B HOH 304 1_555 ? ? ? ? ? ? ? 1.846 ? ? 
metalc16 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? B ZN  200 B HOH 318 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc17 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? B ZN  200 B HOH 450 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc18 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? B ZN  201 B HOH 410 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc19 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? B ZN  201 B HOH 442 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc20 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 M HOH . O  ? ? B ZN  201 B HOH 456 1_555 ? ? ? ? ? ? ? 2.223 ? ? 
metalc21 metalc ? ? C HIS 155 ND1 ? ? ? 1_555 I ZN  . ZN ? ? C HIS 143 C ZN  200 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc22 metalc ? ? I ZN  .   ZN  ? ? ? 1_555 N HOH . O  ? ? C ZN  200 C HOH 428 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc23 metalc ? ? D PHE 104 O   ? ? ? 1_555 K ZN  . ZN ? ? D PHE 92  D ZN  201 1_555 ? ? ? ? ? ? ? 2.492 ? ? 
metalc24 metalc ? ? D ASP 154 OD1 ? ? ? 1_555 J ZN  . ZN ? ? D ASP 142 D ZN  200 1_555 ? ? ? ? ? ? ? 2.232 ? ? 
metalc25 metalc ? ? D ASP 154 OD2 ? ? ? 1_555 J ZN  . ZN ? ? D ASP 142 D ZN  200 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc26 metalc ? ? D HIS 155 ND1 ? ? ? 1_555 K ZN  . ZN ? ? D HIS 143 D ZN  201 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
metalc27 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 O HOH . O  ? ? D ZN  200 D HOH 314 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc28 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 O HOH . O  ? ? D ZN  200 D HOH 388 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc29 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 O HOH . O  ? ? D ZN  200 D HOH 426 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc30 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 O HOH . O  ? ? D ZN  201 D HOH 379 1_555 ? ? ? ? ? ? ? 1.916 ? ? 
metalc31 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 O HOH . O  ? ? D ZN  201 D HOH 414 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 155 ? A HIS 143 ? 1_555 89.7  ? 
2  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 368 ? 1_555 80.3  ? 
3  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 368 ? 1_555 110.0 ? 
4  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 412 ? 1_555 172.3 ? 
5  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 412 ? 1_555 97.5  ? 
6  O   ? L HOH .   ? A HOH 368 ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 412 ? 1_555 94.7  ? 
7  O   ? A PHE 104 ? A PHE 92  ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 435 ? 1_555 85.7  ? 
8  ND1 ? A HIS 155 ? A HIS 143 ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 435 ? 1_555 116.4 ? 
9  O   ? L HOH .   ? A HOH 368 ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 435 ? 1_555 131.2 ? 
10 O   ? L HOH .   ? A HOH 412 ? 1_555 ZN ? F ZN . ? A ZN 201 ? 1_555 O   ? L HOH .   ? A HOH 435 ? 1_555 93.4  ? 
11 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 54.9  ? 
12 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? L HOH .   ? A HOH 419 ? 1_555 87.0  ? 
13 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? L HOH .   ? A HOH 419 ? 1_555 79.9  ? 
14 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 320 ? 1_554 96.4  ? 
15 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 320 ? 1_554 104.8 ? 
16 O   ? L HOH .   ? A HOH 419 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 320 ? 1_554 175.3 ? 
17 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 331 ? 1_554 129.0 ? 
18 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 331 ? 1_554 77.9  ? 
19 O   ? L HOH .   ? A HOH 419 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 331 ? 1_554 104.0 ? 
20 O   ? M HOH .   ? B HOH 320 ? 1_554 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 331 ? 1_554 76.4  ? 
21 OD1 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_554 123.8 ? 
22 OD2 ? A ASP 154 ? A ASP 142 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_554 164.8 ? 
23 O   ? L HOH .   ? A HOH 419 ? 1_555 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_554 85.0  ? 
24 O   ? M HOH .   ? B HOH 320 ? 1_554 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_554 90.4  ? 
25 O   ? M HOH .   ? B HOH 331 ? 1_554 ZN ? E ZN . ? A ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_554 106.9 ? 
26 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 56.7  ? 
27 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 304 ? 1_555 117.0 ? 
28 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 304 ? 1_555 63.2  ? 
29 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 318 ? 1_555 94.9  ? 
30 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 318 ? 1_555 96.8  ? 
31 O   ? M HOH .   ? B HOH 304 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 318 ? 1_555 74.5  ? 
32 OD1 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 450 ? 1_555 131.1 ? 
33 OD2 ? B ASP 154 ? B ASP 142 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 450 ? 1_555 95.0  ? 
34 O   ? M HOH .   ? B HOH 304 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 450 ? 1_555 68.5  ? 
35 O   ? M HOH .   ? B HOH 318 ? 1_555 ZN ? G ZN . ? B ZN 200 ? 1_555 O   ? M HOH .   ? B HOH 450 ? 1_555 130.3 ? 
36 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? M HOH .   ? B HOH 410 ? 1_555 112.2 ? 
37 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? M HOH .   ? B HOH 442 ? 1_555 109.6 ? 
38 O   ? M HOH .   ? B HOH 410 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? M HOH .   ? B HOH 442 ? 1_555 119.8 ? 
39 ND1 ? B HIS 155 ? B HIS 143 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? M HOH .   ? B HOH 456 ? 1_555 109.1 ? 
40 O   ? M HOH .   ? B HOH 410 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? M HOH .   ? B HOH 456 ? 1_555 105.9 ? 
41 O   ? M HOH .   ? B HOH 442 ? 1_555 ZN ? H ZN . ? B ZN 201 ? 1_555 O   ? M HOH .   ? B HOH 456 ? 1_555 98.9  ? 
42 ND1 ? C HIS 155 ? C HIS 143 ? 1_555 ZN ? I ZN . ? C ZN 200 ? 1_555 O   ? N HOH .   ? C HOH 428 ? 1_555 105.2 ? 
43 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? K ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 91.1  ? 
44 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? K ZN . ? D ZN 201 ? 1_555 O   ? O HOH .   ? D HOH 379 ? 1_555 173.8 ? 
45 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 ZN ? K ZN . ? D ZN 201 ? 1_555 O   ? O HOH .   ? D HOH 379 ? 1_555 94.7  ? 
46 O   ? D PHE 104 ? D PHE 92  ? 1_555 ZN ? K ZN . ? D ZN 201 ? 1_555 O   ? O HOH .   ? D HOH 414 ? 1_555 83.2  ? 
47 ND1 ? D HIS 155 ? D HIS 143 ? 1_555 ZN ? K ZN . ? D ZN 201 ? 1_555 O   ? O HOH .   ? D HOH 414 ? 1_555 117.2 ? 
48 O   ? O HOH .   ? D HOH 379 ? 1_555 ZN ? K ZN . ? D ZN 201 ? 1_555 O   ? O HOH .   ? D HOH 414 ? 1_555 92.4  ? 
49 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 OD2 ? D ASP 154 ? D ASP 142 ? 1_555 58.4  ? 
50 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 314 ? 1_555 86.9  ? 
51 OD2 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 314 ? 1_555 95.5  ? 
52 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 388 ? 1_555 138.8 ? 
53 OD2 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 388 ? 1_555 84.9  ? 
54 O   ? O HOH .   ? D HOH 314 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 388 ? 1_555 77.9  ? 
55 OD1 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 426 ? 1_555 96.0  ? 
56 OD2 ? D ASP 154 ? D ASP 142 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 426 ? 1_555 91.2  ? 
57 O   ? O HOH .   ? D HOH 314 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 426 ? 1_555 173.3 ? 
58 O   ? O HOH .   ? D HOH 388 ? 1_555 ZN ? J ZN . ? D ZN 200 ? 1_555 O   ? O HOH .   ? D HOH 426 ? 1_555 103.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 64 A . ? ASN 52 A PRO 65 A ? PRO 53 A 1 2.69  
2 ASN 93 A . ? ASN 81 A PRO 94 A ? PRO 82 A 1 5.82  
3 ASN 64 B . ? ASN 52 B PRO 65 B ? PRO 53 B 1 -4.77 
4 ASN 93 B . ? ASN 81 B PRO 94 B ? PRO 82 B 1 2.88  
5 ASN 64 C . ? ASN 52 C PRO 65 C ? PRO 53 C 1 -4.42 
6 ASN 93 C . ? ASN 81 C PRO 94 C ? PRO 82 C 1 0.08  
7 ASN 64 D . ? ASN 52 D PRO 65 D ? PRO 53 D 1 -0.65 
8 ASN 93 D . ? ASN 81 D PRO 94 D ? PRO 82 D 1 3.03  
# 
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  ? SER B 105 ? VAL B 84  SER B 93  
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 GLN C 114 ? THR C 121 ? GLN C 102 THR C 109 
AA6 1 GLN C 36  ? ASN C 41  ? GLN C 24  ASN C 29  
AA6 2 GLN C 46  ? SER C 52  ? GLN C 34  SER C 40  
AA6 3 SER C 193 ? VAL C 200 ? SER C 181 VAL C 188 
AA6 4 THR C 70  ? ASN C 80  ? THR C 58  ASN C 68  
AA6 5 GLY C 159 ? THR C 162 ? GLY C 147 THR C 150 
AA7 1 GLU D 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  ? PHE D 104 ? VAL D 84  PHE D 92  
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 ? GLN D 201 ? SER D 181 GLN D 189 
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 TRP A 30  ? N TRP A 18  O VAL A 58  ? O VAL A 46  
AA1 3 4 N ALA A 59  ? N ALA A 47  O THR A 187 ? O THR A 175 
AA1 4 5 O ALA A 186 ? O ALA A 174 N SER A 86  ? N SER A 74  
AA1 5 6 N VAL A 87  ? N VAL A 75  O ILE A 100 ? O ILE A 88  
AA1 6 7 N VAL A 101 ? N VAL A 89  O SER A 150 ? O SER A 138 
AA1 7 8 O ALA A 143 ? O ALA A 131 N ALA A 136 ? N ALA A 124 
AA1 8 9 O ILE A 128 ? O ILE A 116 N GLY A 117 ? N GLY A 105 
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 TYR B 26  ? N TYR B 14  O GLY B 62  ? O GLY B 50  
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 TYR B 126 ? O TYR B 114 N VAL B 119 ? N VAL B 107 
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 GLN C 147 ? O GLN C 135 N THR C 131 ? N THR C 119 
AA5 8 9 O ILE C 128 ? O ILE C 116 N LEU C 116 ? N LEU C 104 
AA6 1 2 N THR C 38  ? N THR C 26  O GLU C 50  ? O GLU C 38  
AA6 2 3 N TRP C 51  ? N TRP C 39  O GLY C 194 ? O GLY C 182 
AA6 3 4 O SER C 193 ? O SER C 181 N ASN C 80  ? N ASN C 68  
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 TYR D 26  ? N TYR D 14  O GLY D 62  ? O GLY D 50  
AA7 3 4 N ALA D 59  ? N ALA D 47  O THR D 187 ? O THR D 175 
AA7 4 5 O ALA D 186 ? O ALA D 174 N SER D 86  ? N SER D 74  
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 GLN D 147 ? O GLN D 135 N THR D 131 ? N THR D 119 
AA7 8 9 O ILE D 128 ? O ILE D 116 N LEU D 116 ? N LEU D 104 
AA8 1 2 N THR D 38  ? N THR D 26  O GLU D 50  ? O GLU D 38  
AA8 2 3 N TYR D 47  ? N TYR D 35  O ILE D 198 ? O ILE D 186 
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                   8XZY 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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  B ZN  200 ? ? O B HOH 302 ? ? 1.42 
2  1 ZN  A ZN  200 ? ? O A HOH 303 ? ? 1.43 
3  1 O   B HOH 367 ? ? O B HOH 420 ? ? 1.46 
4  1 OE1 A GLU 128 ? ? O A HOH 301 ? ? 1.61 
5  1 OD1 D ASP 142 ? ? O D HOH 301 ? ? 1.61 
6  1 O   C HOH 313 ? ? O C HOH 360 ? ? 1.61 
7  1 ZN  D ZN  200 ? ? O D HOH 301 ? ? 1.65 
8  1 O   B HOH 322 ? ? O B HOH 430 ? ? 1.70 
9  1 O   A SER 55  ? ? O A HOH 302 ? ? 1.72 
10 1 O   D HOH 362 ? ? O D HOH 382 ? ? 1.84 
11 1 O   D HOH 328 ? ? O D HOH 416 ? ? 1.87 
12 1 O   A HOH 432 ? ? O A HOH 453 ? ? 1.89 
13 1 O   B HOH 420 ? ? O D HOH 356 ? ? 1.94 
14 1 O   D GLY 12  ? ? O D HOH 302 ? ? 1.95 
15 1 O   C HOH 326 ? ? O D HOH 427 ? ? 1.96 
16 1 O   B HOH 325 ? ? O B HOH 355 ? ? 1.96 
17 1 OE1 C GLU 164 ? ? O C HOH 301 ? ? 1.96 
18 1 OE2 D GLU 64  ? ? O D HOH 303 ? ? 1.98 
19 1 O   B HOH 366 ? ? O B HOH 445 ? ? 1.98 
20 1 OE1 C GLU 128 ? ? O C HOH 302 ? ? 1.98 
21 1 O   B HOH 322 ? ? O B HOH 427 ? ? 1.99 
22 1 OG  D SER 98  ? ? O D HOH 304 ? ? 2.01 
23 1 OD1 A ASP 142 ? ? O A HOH 303 ? ? 2.01 
24 1 OE2 B GLU 38  ? ? O B HOH 301 ? ? 2.04 
25 1 O   D HOH 412 ? ? O D HOH 442 ? ? 2.05 
26 1 O   B HOH 437 ? ? O B HOH 486 ? ? 2.05 
27 1 NE2 D GLN 189 ? ? O D HOH 305 ? ? 2.09 
28 1 O   C HOH 323 ? ? O C HOH 437 ? ? 2.10 
29 1 OE1 A GLN 80  ? ? O A HOH 304 ? ? 2.10 
30 1 O   C HOH 437 ? ? O C HOH 451 ? ? 2.11 
31 1 OD1 B ASP 142 ? ? O B HOH 302 ? ? 2.11 
32 1 O   D HOH 384 ? ? O D HOH 428 ? ? 2.12 
33 1 OE1 A GLU 1   ? ? O A HOH 305 ? ? 2.12 
34 1 O   B HOH 309 ? ? O B HOH 386 ? ? 2.12 
35 1 O   B SER 93  ? ? O B HOH 303 ? ? 2.14 
36 1 OE1 D GLN 34  ? ? O D HOH 306 ? ? 2.14 
37 1 OE2 A GLU 64  ? ? O A HOH 306 ? ? 2.16 
38 1 O   C HOH 410 ? ? O C HOH 438 ? ? 2.17 
39 1 OD2 B ASP 142 ? ? O B HOH 304 ? ? 2.17 
40 1 OE2 B GLU 64  ? ? O B HOH 305 ? ? 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 A HOH 317 ? ? 1_555 O B HOH 305 ? ? 1_655 1.87 
2 1 O C HOH 301 ? ? 1_555 O D HOH 303 ? ? 1_554 2.03 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_1              87 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_2              87 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_3              87 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.33 
_pdbx_validate_rmsd_angle.angle_target_value         121.00 
_pdbx_validate_rmsd_angle.angle_deviation            -3.67 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 32  ? ? 50.63   -124.77 
2  1 SER A 55  ? ? -93.16  -144.88 
3  1 SER A 93  ? ? -97.20  -89.45  
4  1 ASN A 169 ? ? -98.03  -144.37 
5  1 ALA B 32  ? ? 49.06   -127.08 
6  1 THR B 94  ? ? 73.47   -25.53  
7  1 ASN B 169 ? ? -100.36 -141.31 
8  1 ALA C 32  ? ? 48.36   -126.52 
9  1 SER C 93  ? ? -100.24 -96.32  
10 1 ASN C 169 ? ? -102.00 -142.24 
11 1 ALA D 32  ? ? 43.41   -122.67 
12 1 SER D 55  ? ? -111.56 -157.26 
13 1 SER D 56  ? ? -97.79  46.22   
14 1 SER D 93  ? ? -97.27  -92.23  
15 1 ASN D 169 ? ? -99.82  -144.84 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -11 ? A GLY 1  
2  1 Y 1 A ALA -10 ? A ALA 2  
3  1 Y 1 A GLY -9  ? A GLY 3  
4  1 Y 1 A ALA -8  ? A ALA 4  
5  1 Y 1 A GLY -7  ? A GLY 5  
6  1 Y 1 A ALA -6  ? A ALA 6  
7  1 Y 1 A GLY -5  ? A GLY 7  
8  1 Y 1 A ALA -4  ? A ALA 8  
9  1 Y 1 A GLY -3  ? A GLY 9  
10 1 Y 1 A ALA -2  ? A ALA 10 
11 1 Y 1 A GLY -1  ? A GLY 11 
12 1 Y 1 A MET 0   ? A MET 12 
13 1 Y 1 B GLY -11 ? B GLY 1  
14 1 Y 1 B ALA -10 ? B ALA 2  
15 1 Y 1 B GLY -9  ? B GLY 3  
16 1 Y 1 B ALA -8  ? B ALA 4  
17 1 Y 1 B GLY -7  ? B GLY 5  
18 1 Y 1 B ALA -6  ? B ALA 6  
19 1 Y 1 B GLY -5  ? B GLY 7  
20 1 Y 1 B ALA -4  ? B ALA 8  
21 1 Y 1 B GLY -3  ? B GLY 9  
22 1 Y 1 B ALA -2  ? B ALA 10 
23 1 Y 1 B GLY -1  ? B GLY 11 
24 1 Y 1 B MET 0   ? B MET 12 
25 1 Y 1 C GLY -11 ? C GLY 1  
26 1 Y 1 C ALA -10 ? C ALA 2  
27 1 Y 1 C GLY -9  ? C GLY 3  
28 1 Y 1 C ALA -8  ? C ALA 4  
29 1 Y 1 C GLY -7  ? C GLY 5  
30 1 Y 1 C ALA -6  ? C ALA 6  
31 1 Y 1 C GLY -5  ? C GLY 7  
32 1 Y 1 C ALA -4  ? C ALA 8  
33 1 Y 1 C GLY -3  ? C GLY 9  
34 1 Y 1 C ALA -2  ? C ALA 10 
35 1 Y 1 C GLY -1  ? C GLY 11 
36 1 Y 1 C MET 0   ? C MET 12 
37 1 Y 1 D GLY -11 ? D GLY 1  
38 1 Y 1 D ALA -10 ? D ALA 2  
39 1 Y 1 D GLY -9  ? D GLY 3  
40 1 Y 1 D ALA -8  ? D ALA 4  
41 1 Y 1 D GLY -7  ? D GLY 5  
42 1 Y 1 D ALA -6  ? D ALA 6  
43 1 Y 1 D GLY -5  ? D GLY 7  
44 1 Y 1 D ALA -4  ? D ALA 8  
45 1 Y 1 D GLY -3  ? D GLY 9  
46 1 Y 1 D ALA -2  ? D ALA 10 
47 1 Y 1 D GLY -1  ? D GLY 11 
48 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 
ZN  ZN   ZN N N 377 
# 
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 
# 
_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 
# 
_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                    8XZY 
_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]   0.019146 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002576 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007271 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.019089 
_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   . GLU A 1 13  ? 11.632  -20.515 18.764  1.00 39.27 ? 1   GLU A N   1 
ATOM   2    C  CA  . GLU A 1 13  ? 12.962  -21.179 18.742  1.00 33.31 ? 1   GLU A CA  1 
ATOM   3    C  C   . GLU A 1 13  ? 13.666  -20.886 20.073  1.00 30.48 ? 1   GLU A C   1 
ATOM   4    O  O   . GLU A 1 13  ? 13.929  -21.868 20.786  1.00 26.99 ? 1   GLU A O   1 
ATOM   5    C  CB  . GLU A 1 13  ? 13.769  -20.784 17.499  1.00 41.50 ? 1   GLU A CB  1 
ATOM   6    C  CG  . GLU A 1 13  ? 15.117  -21.465 17.365  1.00 35.87 ? 1   GLU A CG  1 
ATOM   7    C  CD  . GLU A 1 13  ? 15.165  -22.881 16.786  1.00 40.59 ? 1   GLU A CD  1 
ATOM   8    O  OE1 . GLU A 1 13  ? 14.791  -23.075 15.606  1.00 38.12 ? 1   GLU A OE1 1 
ATOM   9    O  OE2 . GLU A 1 13  ? 15.711  -23.762 17.476  1.00 33.97 ? 1   GLU A OE2 1 
ATOM   10   N  N   . ILE A 1 14  ? 13.988  -19.629 20.415  1.00 25.87 ? 2   ILE A N   1 
ATOM   11   C  CA  . ILE A 1 14  ? 14.638  -19.349 21.727  1.00 26.57 ? 2   ILE A CA  1 
ATOM   12   C  C   . ILE A 1 14  ? 13.831  -18.321 22.518  1.00 25.26 ? 2   ILE A C   1 
ATOM   13   O  O   . ILE A 1 14  ? 13.174  -17.444 21.902  1.00 22.14 ? 2   ILE A O   1 
ATOM   14   C  CB  . ILE A 1 14  ? 16.103  -18.934 21.591  1.00 27.81 ? 2   ILE A CB  1 
ATOM   15   C  CG1 . ILE A 1 14  ? 16.271  -17.649 20.796  1.00 25.16 ? 2   ILE A CG1 1 
ATOM   16   C  CG2 . ILE A 1 14  ? 16.963  -20.064 21.024  1.00 30.34 ? 2   ILE A CG2 1 
ATOM   17   C  CD1 . ILE A 1 14  ? 17.584  -16.983 21.072  1.00 27.67 ? 2   ILE A CD1 1 
ATOM   18   N  N   . THR A 1 15  ? 13.903  -18.428 23.847  1.00 24.12 ? 3   THR A N   1 
ATOM   19   C  CA  . THR A 1 15  ? 13.078  -17.615 24.770  1.00 22.61 ? 3   THR A CA  1 
ATOM   20   C  C   . THR A 1 15  ? 13.931  -16.899 25.823  1.00 21.40 ? 3   THR A C   1 
ATOM   21   O  O   . THR A 1 15  ? 13.342  -16.221 26.688  1.00 20.62 ? 3   THR A O   1 
ATOM   22   C  CB  . THR A 1 15  ? 12.024  -18.489 25.451  1.00 26.92 ? 3   THR A CB  1 
ATOM   23   O  OG1 . THR A 1 15  ? 12.717  -19.479 26.217  1.00 28.11 ? 3   THR A OG1 1 
ATOM   24   C  CG2 . THR A 1 15  ? 11.086  -19.143 24.462  1.00 30.38 ? 3   THR A CG2 1 
ATOM   25   N  N   . SER A 1 16  ? 15.249  -17.033 25.765  1.00 19.75 ? 4   SER A N   1 
ATOM   26   C  CA  . SER A 1 16  ? 16.198  -16.395 26.705  1.00 22.17 ? 4   SER A CA  1 
ATOM   27   C  C   . SER A 1 16  ? 17.378  -15.866 25.913  1.00 18.89 ? 4   SER A C   1 
ATOM   28   O  O   . SER A 1 16  ? 17.585  -16.343 24.786  1.00 18.22 ? 4   SER A O   1 
ATOM   29   C  CB  . SER A 1 16  ? 16.638  -17.343 27.812  1.00 23.89 ? 4   SER A CB  1 
ATOM   30   O  OG  . SER A 1 16  ? 16.850  -18.635 27.302  1.00 29.15 ? 4   SER A OG  1 
ATOM   31   N  N   . SER A 1 17  ? 18.074  -14.905 26.500  1.00 18.12 ? 5   SER A N   1 
ATOM   32   C  CA  . SER A 1 17  ? 19.075  -14.041 25.844  1.00 18.49 ? 5   SER A CA  1 
ATOM   33   C  C   . SER A 1 17  ? 20.163  -14.918 25.222  1.00 19.45 ? 5   SER A C   1 
ATOM   34   O  O   . SER A 1 17  ? 20.569  -15.905 25.836  1.00 18.58 ? 5   SER A O   1 
ATOM   35   C  CB  . SER A 1 17  ? 19.641  -13.063 26.811  1.00 20.11 ? 5   SER A CB  1 
ATOM   36   O  OG  . SER A 1 17  ? 18.612  -12.213 27.303  1.00 18.30 ? 5   SER A OG  1 
ATOM   37   N  N   . GLU A 1 18  ? 20.564  -14.576 24.012  1.00 17.89 ? 6   GLU A N   1 
ATOM   38   C  CA  . GLU A 1 18  ? 21.624  -15.295 23.291  1.00 18.77 ? 6   GLU A CA  1 
ATOM   39   C  C   . GLU A 1 18  ? 22.167  -14.384 22.197  1.00 16.69 ? 6   GLU A C   1 
ATOM   40   O  O   . GLU A 1 18  ? 21.427  -13.649 21.627  1.00 16.19 ? 6   GLU A O   1 
ATOM   41   C  CB  . GLU A 1 18  ? 21.023  -16.573 22.699  1.00 21.40 ? 6   GLU A CB  1 
ATOM   42   C  CG  . GLU A 1 18  ? 21.989  -17.418 21.880  1.00 24.91 ? 6   GLU A CG  1 
ATOM   43   C  CD  . GLU A 1 18  ? 21.295  -18.616 21.259  1.00 29.50 ? 6   GLU A CD  1 
ATOM   44   O  OE1 . GLU A 1 18  ? 21.310  -18.724 20.019  1.00 31.89 ? 6   GLU A OE1 1 
ATOM   45   O  OE2 . GLU A 1 18  ? 20.686  -19.418 22.019  1.00 36.47 ? 6   GLU A OE2 1 
ATOM   46   N  N   . THR A 1 19  ? 23.433  -14.534 21.874  1.00 16.38 ? 7   THR A N   1 
ATOM   47   C  CA  . THR A 1 19  ? 24.048  -13.913 20.690  1.00 15.06 ? 7   THR A CA  1 
ATOM   48   C  C   . THR A 1 19  ? 24.783  -15.010 19.912  1.00 15.68 ? 7   THR A C   1 
ATOM   49   O  O   . THR A 1 19  ? 24.975  -16.161 20.429  1.00 16.22 ? 7   THR A O   1 
ATOM   50   C  CB  . THR A 1 19  ? 24.968  -12.753 21.073  1.00 17.26 ? 7   THR A CB  1 
ATOM   51   O  OG1 . THR A 1 19  ? 26.117  -13.355 21.699  1.00 19.32 ? 7   THR A OG1 1 
ATOM   52   C  CG2 . THR A 1 19  ? 24.295  -11.719 21.959  1.00 17.17 ? 7   THR A CG2 1 
ATOM   53   N  N   . GLY A 1 20  ? 25.011  -14.727 18.651  1.00 15.78 ? 8   GLY A N   1 
ATOM   54   C  CA  . GLY A 1 20  ? 25.750  -15.655 17.789  1.00 14.73 ? 8   GLY A CA  1 
ATOM   55   C  C   . GLY A 1 20  ? 25.860  -15.104 16.410  1.00 15.41 ? 8   GLY A C   1 
ATOM   56   O  O   . GLY A 1 20  ? 25.602  -13.925 16.201  1.00 15.71 ? 8   GLY A O   1 
ATOM   57   N  N   . THR A 1 21  ? 26.293  -15.929 15.481  1.00 16.75 ? 9   THR A N   1 
ATOM   58   C  CA  . THR A 1 21  ? 26.326  -15.599 14.052  1.00 16.50 ? 9   THR A CA  1 
ATOM   59   C  C   . THR A 1 21  ? 25.541  -16.705 13.359  1.00 17.59 ? 9   THR A C   1 
ATOM   60   O  O   . THR A 1 21  ? 25.727  -17.885 13.746  1.00 21.21 ? 9   THR A O   1 
ATOM   61   C  CB  . THR A 1 21  ? 27.783  -15.515 13.569  1.00 18.60 ? 9   THR A CB  1 
ATOM   62   O  OG1 . THR A 1 21  ? 28.458  -14.505 14.302  1.00 21.32 ? 9   THR A OG1 1 
ATOM   63   C  CG2 . THR A 1 21  ? 27.865  -15.156 12.103  1.00 19.70 ? 9   THR A CG2 1 
ATOM   64   N  N   . ASN A 1 22  ? 24.640  -16.350 12.451  1.00 13.66 ? 10  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 22  ? 23.705  -17.262 11.754  1.00 14.15 ? 10  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 22  ? 23.618  -16.821 10.284  1.00 15.00 ? 10  ASN A C   1 
ATOM   67   O  O   . ASN A 1 22  ? 23.355  -15.635 10.031  1.00 13.97 ? 10  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 22  ? 22.327  -17.205 12.422  1.00 14.70 ? 10  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 22  ? 21.272  -17.977 11.660  1.00 15.17 ? 10  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 22  ? 20.532  -17.401 10.863  1.00 18.88 ? 10  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 22  ? 21.151  -19.264 11.951  1.00 17.95 ? 10  ASN A ND2 1 
ATOM   72   N  N   . ASN A 1 23  ? 23.941  -17.701 9.343   1.00 16.02 ? 11  ASN A N   1 
ATOM   73   C  CA  . ASN A 1 23  ? 23.916  -17.382 7.897   1.00 17.53 ? 11  ASN A CA  1 
ATOM   74   C  C   . ASN A 1 23  ? 24.768  -16.132 7.617   1.00 17.85 ? 11  ASN A C   1 
ATOM   75   O  O   . ASN A 1 23  ? 24.412  -15.337 6.708   1.00 18.90 ? 11  ASN A O   1 
ATOM   76   C  CB  . ASN A 1 23  ? 22.455  -17.263 7.437   1.00 18.37 ? 11  ASN A CB  1 
ATOM   77   C  CG  . ASN A 1 23  ? 21.765  -18.601 7.474   1.00 21.92 ? 11  ASN A CG  1 
ATOM   78   O  OD1 . ASN A 1 23  ? 22.249  -19.544 6.878   1.00 24.21 ? 11  ASN A OD1 1 
ATOM   79   N  ND2 . ASN A 1 23  ? 20.675  -18.717 8.201   1.00 20.42 ? 11  ASN A ND2 1 
ATOM   80   N  N   . GLY A 1 24  ? 25.885  -15.942 8.331   1.00 15.97 ? 12  GLY A N   1 
ATOM   81   C  CA  . GLY A 1 24  ? 26.821  -14.836 8.093   1.00 15.78 ? 12  GLY A CA  1 
ATOM   82   C  C   . GLY A 1 24  ? 26.457  -13.504 8.740   1.00 14.52 ? 12  GLY A C   1 
ATOM   83   O  O   . GLY A 1 24  ? 27.228  -12.561 8.630   1.00 14.80 ? 12  GLY A O   1 
ATOM   84   N  N   . TYR A 1 25  ? 25.343  -13.450 9.484   1.00 13.98 ? 13  TYR A N   1 
ATOM   85   C  CA  . TYR A 1 25  ? 24.907  -12.254 10.239  1.00 13.84 ? 13  TYR A CA  1 
ATOM   86   C  C   . TYR A 1 25  ? 24.998  -12.510 11.731  1.00 13.08 ? 13  TYR A C   1 
ATOM   87   O  O   . TYR A 1 25  ? 24.528  -13.596 12.227  1.00 14.71 ? 13  TYR A O   1 
ATOM   88   C  CB  . TYR A 1 25  ? 23.438  -11.939 9.933   1.00 14.00 ? 13  TYR A CB  1 
ATOM   89   C  CG  . TYR A 1 25  ? 23.281  -11.479 8.522   1.00 16.01 ? 13  TYR A CG  1 
ATOM   90   C  CD1 . TYR A 1 25  ? 23.410  -10.141 8.227   1.00 17.47 ? 13  TYR A CD1 1 
ATOM   91   C  CD2 . TYR A 1 25  ? 23.051  -12.374 7.488   1.00 16.34 ? 13  TYR A CD2 1 
ATOM   92   C  CE1 . TYR A 1 25  ? 23.309  -9.684  6.918   1.00 21.90 ? 13  TYR A CE1 1 
ATOM   93   C  CE2 . TYR A 1 25  ? 22.918  -11.932 6.179   1.00 19.45 ? 13  TYR A CE2 1 
ATOM   94   C  CZ  . TYR A 1 25  ? 23.066  -10.582 5.897   1.00 22.17 ? 13  TYR A CZ  1 
ATOM   95   O  OH  . TYR A 1 25  ? 22.984  -10.104 4.624   1.00 26.21 ? 13  TYR A OH  1 
ATOM   96   N  N   . TYR A 1 26  ? 25.590  -11.528 12.407  1.00 14.33 ? 14  TYR A N   1 
ATOM   97   C  CA  . TYR A 1 26  ? 25.562  -11.421 13.871  1.00 13.68 ? 14  TYR A CA  1 
ATOM   98   C  C   . TYR A 1 26  ? 24.092  -11.381 14.284  1.00 13.57 ? 14  TYR A C   1 
ATOM   99   O  O   . TYR A 1 26  ? 23.329  -10.682 13.591  1.00 13.94 ? 14  TYR A O   1 
ATOM   100  C  CB  . TYR A 1 26  ? 26.279  -10.177 14.348  1.00 14.90 ? 14  TYR A CB  1 
ATOM   101  C  CG  . TYR A 1 26  ? 26.264  -10.045 15.839  1.00 15.79 ? 14  TYR A CG  1 
ATOM   102  C  CD1 . TYR A 1 26  ? 27.007  -10.918 16.628  1.00 15.48 ? 14  TYR A CD1 1 
ATOM   103  C  CD2 . TYR A 1 26  ? 25.490  -9.076  16.482  1.00 15.20 ? 14  TYR A CD2 1 
ATOM   104  C  CE1 . TYR A 1 26  ? 27.000  -10.809 18.002  1.00 16.78 ? 14  TYR A CE1 1 
ATOM   105  C  CE2 . TYR A 1 26  ? 25.484  -8.974  17.862  1.00 16.41 ? 14  TYR A CE2 1 
ATOM   106  C  CZ  . TYR A 1 26  ? 26.248  -9.837  18.618  1.00 17.83 ? 14  TYR A CZ  1 
ATOM   107  O  OH  . TYR A 1 26  ? 26.285  -9.777  19.978  1.00 22.30 ? 14  TYR A OH  1 
ATOM   108  N  N   . TYR A 1 27  ? 23.729  -12.012 15.376  1.00 12.22 ? 15  TYR A N   1 
ATOM   109  C  CA  . TYR A 1 27  ? 22.377  -11.759 15.935  1.00 12.74 ? 15  TYR A CA  1 
ATOM   110  C  C   . TYR A 1 27  ? 22.511  -11.535 17.419  1.00 14.70 ? 15  TYR A C   1 
ATOM   111  O  O   . TYR A 1 27  ? 23.403  -12.103 18.069  1.00 13.38 ? 15  TYR A O   1 
ATOM   112  C  CB  . TYR A 1 27  ? 21.365  -12.854 15.620  1.00 13.16 ? 15  TYR A CB  1 
ATOM   113  C  CG  . TYR A 1 27  ? 21.660  -14.192 16.256  1.00 12.81 ? 15  TYR A CG  1 
ATOM   114  C  CD1 . TYR A 1 27  ? 22.499  -15.113 15.635  1.00 13.19 ? 15  TYR A CD1 1 
ATOM   115  C  CD2 . TYR A 1 27  ? 21.130  -14.530 17.479  1.00 15.02 ? 15  TYR A CD2 1 
ATOM   116  C  CE1 . TYR A 1 27  ? 22.797  -16.327 16.224  1.00 16.17 ? 15  TYR A CE1 1 
ATOM   117  C  CE2 . TYR A 1 27  ? 21.403  -15.755 18.069  1.00 15.64 ? 15  TYR A CE2 1 
ATOM   118  C  CZ  . TYR A 1 27  ? 22.234  -16.653 17.431  1.00 15.94 ? 15  TYR A CZ  1 
ATOM   119  O  OH  . TYR A 1 27  ? 22.544  -17.835 18.014  1.00 20.75 ? 15  TYR A OH  1 
ATOM   120  N  N   . SER A 1 28  ? 21.632  -10.681 17.927  1.00 15.10 ? 16  SER A N   1 
ATOM   121  C  CA  . SER A 1 28  ? 21.545  -10.435 19.375  1.00 14.01 ? 16  SER A CA  1 
ATOM   122  C  C   . SER A 1 28  ? 20.086  -10.558 19.774  1.00 14.63 ? 16  SER A C   1 
ATOM   123  O  O   . SER A 1 28  ? 19.255  -9.893  19.171  1.00 13.91 ? 16  SER A O   1 
ATOM   124  C  CB  . SER A 1 28  ? 22.178  -9.119  19.751  1.00 14.80 ? 16  SER A CB  1 
ATOM   125  O  OG  . SER A 1 28  ? 22.075  -8.890  21.147  1.00 16.99 ? 16  SER A OG  1 
ATOM   126  N  N   . PHE A 1 29  ? 19.799  -11.390 20.770  1.00 13.96 ? 17  PHE A N   1 
ATOM   127  C  CA  . PHE A 1 29  ? 18.436  -11.477 21.336  1.00 15.83 ? 17  PHE A CA  1 
ATOM   128  C  C   . PHE A 1 29  ? 18.601  -11.238 22.820  1.00 16.97 ? 17  PHE A C   1 
ATOM   129  O  O   . PHE A 1 29  ? 19.298  -12.022 23.507  1.00 16.46 ? 17  PHE A O   1 
ATOM   130  C  CB  . PHE A 1 29  ? 17.765  -12.809 21.015  1.00 16.43 ? 17  PHE A CB  1 
ATOM   131  C  CG  . PHE A 1 29  ? 16.477  -13.019 21.772  1.00 16.86 ? 17  PHE A CG  1 
ATOM   132  C  CD1 . PHE A 1 29  ? 15.454  -12.094 21.631  1.00 18.35 ? 17  PHE A CD1 1 
ATOM   133  C  CD2 . PHE A 1 29  ? 16.311  -14.060 22.666  1.00 17.87 ? 17  PHE A CD2 1 
ATOM   134  C  CE1 . PHE A 1 29  ? 14.277  -12.236 22.337  1.00 15.79 ? 17  PHE A CE1 1 
ATOM   135  C  CE2 . PHE A 1 29  ? 15.100  -14.244 23.330  1.00 18.54 ? 17  PHE A CE2 1 
ATOM   136  C  CZ  . PHE A 1 29  ? 14.101  -13.317 23.176  1.00 16.40 ? 17  PHE A CZ  1 
ATOM   137  N  N   . TRP A 1 30  ? 18.062  -10.127 23.313  1.00 16.33 ? 18  TRP A N   1 
ATOM   138  C  CA  . TRP A 1 30  ? 18.185  -9.844  24.760  1.00 18.26 ? 18  TRP A CA  1 
ATOM   139  C  C   . TRP A 1 30  ? 16.774  -9.731  25.323  1.00 17.15 ? 18  TRP A C   1 
ATOM   140  O  O   . TRP A 1 30  ? 15.971  -9.025  24.691  1.00 18.31 ? 18  TRP A O   1 
ATOM   141  C  CB  . TRP A 1 30  ? 19.004  -8.586  25.010  1.00 20.58 ? 18  TRP A CB  1 
ATOM   142  C  CG  . TRP A 1 30  ? 19.121  -8.239  26.455  1.00 23.92 ? 18  TRP A CG  1 
ATOM   143  C  CD1 . TRP A 1 30  ? 20.005  -8.759  27.363  1.00 28.71 ? 18  TRP A CD1 1 
ATOM   144  C  CD2 . TRP A 1 30  ? 18.269  -7.340  27.183  1.00 27.24 ? 18  TRP A CD2 1 
ATOM   145  N  NE1 . TRP A 1 30  ? 19.779  -8.216  28.604  1.00 30.52 ? 18  TRP A NE1 1 
ATOM   146  C  CE2 . TRP A 1 30  ? 18.730  -7.336  28.520  1.00 30.50 ? 18  TRP A CE2 1 
ATOM   147  C  CE3 . TRP A 1 30  ? 17.193  -6.521  26.824  1.00 29.72 ? 18  TRP A CE3 1 
ATOM   148  C  CZ2 . TRP A 1 30  ? 18.107  -6.564  29.504  1.00 32.85 ? 18  TRP A CZ2 1 
ATOM   149  C  CZ3 . TRP A 1 30  ? 16.600  -5.732  27.791  1.00 33.80 ? 18  TRP A CZ3 1 
ATOM   150  C  CH2 . TRP A 1 30  ? 17.049  -5.773  29.116  1.00 30.80 ? 18  TRP A CH2 1 
ATOM   151  N  N   . THR A 1 31  ? 16.472  -10.441 26.403  1.00 17.05 ? 19  THR A N   1 
ATOM   152  C  CA  . THR A 1 31  ? 15.202  -10.228 27.141  1.00 18.02 ? 19  THR A CA  1 
ATOM   153  C  C   . THR A 1 31  ? 15.496  -10.211 28.641  1.00 22.73 ? 19  THR A C   1 
ATOM   154  O  O   . THR A 1 31  ? 16.355  -11.022 29.087  1.00 20.34 ? 19  THR A O   1 
ATOM   155  C  CB  . THR A 1 31  ? 14.112  -11.211 26.717  1.00 20.10 ? 19  THR A CB  1 
ATOM   156  O  OG1 . THR A 1 31  ? 12.984  -10.831 27.512  1.00 21.18 ? 19  THR A OG1 1 
ATOM   157  C  CG2 . THR A 1 31  ? 14.470  -12.683 26.847  1.00 19.43 ? 19  THR A CG2 1 
ATOM   158  N  N   . ASP A 1 32  ? 14.791  -9.333  29.369  1.00 22.01 ? 20  ASP A N   1 
ATOM   159  C  CA  . ASP A 1 32  ? 14.841  -9.285  30.857  1.00 23.87 ? 20  ASP A CA  1 
ATOM   160  C  C   . ASP A 1 32  ? 14.031  -10.452 31.450  1.00 23.71 ? 20  ASP A C   1 
ATOM   161  O  O   . ASP A 1 32  ? 14.048  -10.565 32.690  1.00 28.44 ? 20  ASP A O   1 
ATOM   162  C  CB  . ASP A 1 32  ? 14.452  -7.895  31.367  1.00 22.64 ? 20  ASP A CB  1 
ATOM   163  C  CG  . ASP A 1 32  ? 12.964  -7.595  31.202  1.00 22.63 ? 20  ASP A CG  1 
ATOM   164  O  OD1 . ASP A 1 32  ? 12.259  -8.527  30.794  1.00 20.90 ? 20  ASP A OD1 1 
ATOM   165  O  OD2 . ASP A 1 32  ? 12.532  -6.405  31.480  1.00 25.04 ? 20  ASP A OD2 1 
ATOM   166  N  N   . GLY A 1 33  ? 13.375  -11.303 30.637  1.00 22.85 ? 21  GLY A N   1 
ATOM   167  C  CA  . GLY A 1 33  ? 12.624  -12.487 31.099  1.00 25.31 ? 21  GLY A CA  1 
ATOM   168  C  C   . GLY A 1 33  ? 11.137  -12.227 31.344  1.00 24.55 ? 21  GLY A C   1 
ATOM   169  O  O   . GLY A 1 33  ? 10.427  -13.211 31.602  1.00 28.77 ? 21  GLY A O   1 
ATOM   170  N  N   . GLY A 1 34  ? 10.673  -10.970 31.277  1.00 23.41 ? 22  GLY A N   1 
ATOM   171  C  CA  . GLY A 1 34  ? 9.245   -10.601 31.399  1.00 23.62 ? 22  GLY A CA  1 
ATOM   172  C  C   . GLY A 1 34  ? 8.372   -11.254 30.341  1.00 21.14 ? 22  GLY A C   1 
ATOM   173  O  O   . GLY A 1 34  ? 8.812   -11.373 29.167  1.00 22.30 ? 22  GLY A O   1 
ATOM   174  N  N   . GLY A 1 35  ? 7.184   -11.713 30.738  1.00 21.36 ? 23  GLY A N   1 
ATOM   175  C  CA  . GLY A 1 35  ? 6.189   -12.329 29.847  1.00 22.77 ? 23  GLY A CA  1 
ATOM   176  C  C   . GLY A 1 35  ? 6.782   -13.412 28.965  1.00 24.61 ? 23  GLY A C   1 
ATOM   177  O  O   . GLY A 1 35  ? 7.568   -14.239 29.469  1.00 22.56 ? 23  GLY A O   1 
ATOM   178  N  N   . GLN A 1 36  ? 6.391   -13.461 27.689  1.00 20.87 ? 24  GLN A N   1 
ATOM   179  C  CA  . GLN A 1 36  ? 6.936   -14.467 26.764  1.00 22.02 ? 24  GLN A CA  1 
ATOM   180  C  C   . GLN A 1 36  ? 7.504   -13.725 25.566  1.00 20.42 ? 24  GLN A C   1 
ATOM   181  O  O   . GLN A 1 36  ? 6.777   -12.939 24.945  1.00 18.14 ? 24  GLN A O   1 
ATOM   182  C  CB  . GLN A 1 36  ? 5.898   -15.502 26.308  1.00 25.72 ? 24  GLN A CB  1 
ATOM   183  C  CG  . GLN A 1 36  ? 5.059   -16.096 27.433  1.00 31.44 ? 24  GLN A CG  1 
ATOM   184  C  CD  . GLN A 1 36  ? 3.613   -15.661 27.383  1.00 38.75 ? 24  GLN A CD  1 
ATOM   185  O  OE1 . GLN A 1 36  ? 3.193   -14.749 28.097  1.00 48.07 ? 24  GLN A OE1 1 
ATOM   186  N  NE2 . GLN A 1 36  ? 2.833   -16.310 26.529  1.00 43.17 ? 24  GLN A NE2 1 
ATOM   187  N  N   . VAL A 1 37  ? 8.758   -13.982 25.226  1.00 18.96 ? 25  VAL A N   1 
ATOM   188  C  CA  . VAL A 1 37  ? 9.337   -13.358 24.004  1.00 17.14 ? 25  VAL A CA  1 
ATOM   189  C  C   . VAL A 1 37  ? 10.038  -14.490 23.280  1.00 17.42 ? 25  VAL A C   1 
ATOM   190  O  O   . VAL A 1 37  ? 10.763  -15.216 23.982  1.00 18.07 ? 25  VAL A O   1 
ATOM   191  C  CB  . VAL A 1 37  ? 10.333  -12.229 24.325  1.00 18.11 ? 25  VAL A CB  1 
ATOM   192  C  CG1 . VAL A 1 37  ? 10.933  -11.618 23.061  1.00 17.61 ? 25  VAL A CG1 1 
ATOM   193  C  CG2 . VAL A 1 37  ? 9.745   -11.143 25.193  1.00 17.48 ? 25  VAL A CG2 1 
ATOM   194  N  N   . THR A 1 38  ? 9.705   -14.730 22.014  1.00 16.51 ? 26  THR A N   1 
ATOM   195  C  CA  . THR A 1 38  ? 10.220  -15.894 21.249  1.00 16.11 ? 26  THR A CA  1 
ATOM   196  C  C   . THR A 1 38  ? 10.923  -15.388 19.995  1.00 15.17 ? 26  THR A C   1 
ATOM   197  O  O   . THR A 1 38  ? 10.248  -14.764 19.168  1.00 15.20 ? 26  THR A O   1 
ATOM   198  C  CB  . THR A 1 38  ? 9.088   -16.845 20.867  1.00 19.63 ? 26  THR A CB  1 
ATOM   199  O  OG1 . THR A 1 38  ? 8.433   -17.290 22.061  1.00 22.46 ? 26  THR A OG1 1 
ATOM   200  C  CG2 . THR A 1 38  ? 9.564   -18.063 20.117  1.00 22.89 ? 26  THR A CG2 1 
ATOM   201  N  N   . TYR A 1 39  ? 12.187  -15.746 19.813  1.00 14.48 ? 27  TYR A N   1 
ATOM   202  C  CA  . TYR A 1 39  ? 13.002  -15.281 18.682  1.00 13.89 ? 27  TYR A CA  1 
ATOM   203  C  C   . TYR A 1 39  ? 13.340  -16.469 17.783  1.00 15.68 ? 27  TYR A C   1 
ATOM   204  O  O   . TYR A 1 39  ? 13.597  -17.573 18.291  1.00 14.36 ? 27  TYR A O   1 
ATOM   205  C  CB  . TYR A 1 39  ? 14.234  -14.596 19.262  1.00 12.08 ? 27  TYR A CB  1 
ATOM   206  C  CG  . TYR A 1 39  ? 15.264  -14.240 18.234  1.00 12.46 ? 27  TYR A CG  1 
ATOM   207  C  CD1 . TYR A 1 39  ? 16.257  -15.129 17.852  1.00 13.68 ? 27  TYR A CD1 1 
ATOM   208  C  CD2 . TYR A 1 39  ? 15.221  -13.011 17.614  1.00 12.09 ? 27  TYR A CD2 1 
ATOM   209  C  CE1 . TYR A 1 39  ? 17.202  -14.759 16.903  1.00 13.62 ? 27  TYR A CE1 1 
ATOM   210  C  CE2 . TYR A 1 39  ? 16.174  -12.627 16.692  1.00 13.38 ? 27  TYR A CE2 1 
ATOM   211  C  CZ  . TYR A 1 39  ? 17.167  -13.500 16.341  1.00 13.22 ? 27  TYR A CZ  1 
ATOM   212  O  OH  . TYR A 1 39  ? 18.030  -13.044 15.395  1.00 13.88 ? 27  TYR A OH  1 
ATOM   213  N  N   . THR A 1 40  ? 13.354  -16.282 16.470  1.00 14.68 ? 28  THR A N   1 
ATOM   214  C  CA  . THR A 1 40  ? 13.848  -17.324 15.552  1.00 16.09 ? 28  THR A CA  1 
ATOM   215  C  C   . THR A 1 40  ? 14.772  -16.673 14.525  1.00 14.88 ? 28  THR A C   1 
ATOM   216  O  O   . THR A 1 40  ? 14.437  -15.625 13.969  1.00 15.60 ? 28  THR A O   1 
ATOM   217  C  CB  . THR A 1 40  ? 12.708  -18.141 14.915  1.00 19.82 ? 28  THR A CB  1 
ATOM   218  O  OG1 . THR A 1 40  ? 11.938  -17.248 14.136  1.00 21.30 ? 28  THR A OG1 1 
ATOM   219  C  CG2 . THR A 1 40  ? 11.726  -18.734 15.898  1.00 19.68 ? 28  THR A CG2 1 
ATOM   220  N  N   . ASN A 1 41  ? 15.872  -17.335 14.206  1.00 13.65 ? 29  ASN A N   1 
ATOM   221  C  CA  . ASN A 1 41  ? 16.648  -16.979 12.982  1.00 14.53 ? 29  ASN A CA  1 
ATOM   222  C  C   . ASN A 1 41  ? 16.050  -17.673 11.761  1.00 16.48 ? 29  ASN A C   1 
ATOM   223  O  O   . ASN A 1 41  ? 15.695  -18.873 11.855  1.00 19.24 ? 29  ASN A O   1 
ATOM   224  C  CB  . ASN A 1 41  ? 18.128  -17.330 13.134  1.00 15.01 ? 29  ASN A CB  1 
ATOM   225  C  CG  . ASN A 1 41  ? 18.852  -16.449 14.117  1.00 14.65 ? 29  ASN A CG  1 
ATOM   226  O  OD1 . ASN A 1 41  ? 18.824  -15.238 13.979  1.00 17.83 ? 29  ASN A OD1 1 
ATOM   227  N  ND2 . ASN A 1 41  ? 19.600  -17.056 15.027  1.00 17.71 ? 29  ASN A ND2 1 
ATOM   228  N  N   . GLY A 1 42  ? 16.000  -16.933 10.654  1.00 14.50 ? 30  GLY A N   1 
ATOM   229  C  CA  . GLY A 1 42  ? 15.616  -17.421 9.336   1.00 15.86 ? 30  GLY A CA  1 
ATOM   230  C  C   . GLY A 1 42  ? 16.827  -17.485 8.422   1.00 16.32 ? 30  GLY A C   1 
ATOM   231  O  O   . GLY A 1 42  ? 17.946  -17.183 8.812   1.00 17.31 ? 30  GLY A O   1 
ATOM   232  N  N   . PRO A 1 43  ? 16.596  -17.812 7.139   1.00 18.91 ? 31  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 43  ? 17.646  -17.785 6.123   1.00 19.94 ? 31  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 43  ? 18.252  -16.386 5.952   1.00 19.37 ? 31  PRO A C   1 
ATOM   235  O  O   . PRO A 1 43  ? 17.544  -15.434 6.203   1.00 17.84 ? 31  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 43  ? 16.917  -18.178 4.824   1.00 21.68 ? 31  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 43  ? 15.573  -18.735 5.250   1.00 23.51 ? 31  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 43  ? 15.262  -18.139 6.609   1.00 21.32 ? 31  PRO A CD  1 
ATOM   239  N  N   . ALA A 1 44  ? 19.528  -16.292 5.533   1.00 16.94 ? 32  ALA A N   1 
ATOM   240  C  CA  . ALA A 1 44  ? 20.246  -15.049 5.208   1.00 17.07 ? 32  ALA A CA  1 
ATOM   241  C  C   . ALA A 1 44  ? 20.078  -14.060 6.374   1.00 16.52 ? 32  ALA A C   1 
ATOM   242  O  O   . ALA A 1 44  ? 20.323  -14.469 7.528   1.00 16.72 ? 32  ALA A O   1 
ATOM   243  C  CB  . ALA A 1 44  ? 19.786  -14.485 3.855   1.00 18.07 ? 32  ALA A CB  1 
ATOM   244  N  N   . GLY A 1 45  ? 19.580  -12.852 6.096   1.00 14.09 ? 33  GLY A N   1 
ATOM   245  C  CA  . GLY A 1 45  ? 19.515  -11.786 7.113   1.00 14.24 ? 33  GLY A CA  1 
ATOM   246  C  C   . GLY A 1 45  ? 18.176  -11.765 7.823   1.00 12.33 ? 33  GLY A C   1 
ATOM   247  O  O   . GLY A 1 45  ? 17.906  -10.735 8.424   1.00 11.90 ? 33  GLY A O   1 
ATOM   248  N  N   . GLN A 1 46  ? 17.391  -12.832 7.806   1.00 13.61 ? 34  GLN A N   1 
ATOM   249  C  CA  . GLN A 1 46  ? 15.983  -12.785 8.333   1.00 12.94 ? 34  GLN A CA  1 
ATOM   250  C  C   . GLN A 1 46  ? 15.935  -13.176 9.808   1.00 12.35 ? 34  GLN A C   1 
ATOM   251  O  O   . GLN A 1 46  ? 16.616  -14.152 10.227  1.00 11.91 ? 34  GLN A O   1 
ATOM   252  C  CB  . GLN A 1 46  ? 15.052  -13.694 7.534   1.00 15.40 ? 34  GLN A CB  1 
ATOM   253  C  CG  . GLN A 1 46  ? 13.557  -13.489 7.764   1.00 17.45 ? 34  GLN A CG  1 
ATOM   254  C  CD  . GLN A 1 46  ? 12.891  -14.182 8.936   1.00 17.72 ? 34  GLN A CD  1 
ATOM   255  O  OE1 . GLN A 1 46  ? 11.697  -13.979 9.225   1.00 22.06 ? 34  GLN A OE1 1 
ATOM   256  N  NE2 . GLN A 1 46  ? 13.594  -15.074 9.584   1.00 17.38 ? 34  GLN A NE2 1 
ATOM   257  N  N   . TYR A 1 47  ? 15.079  -12.500 10.581  1.00 12.21 ? 35  TYR A N   1 
ATOM   258  C  CA  . TYR A 1 47  ? 14.714  -12.999 11.922  1.00 11.95 ? 35  TYR A CA  1 
ATOM   259  C  C   . TYR A 1 47  ? 13.236  -12.697 12.139  1.00 10.38 ? 35  TYR A C   1 
ATOM   260  O  O   . TYR A 1 47  ? 12.672  -11.802 11.494  1.00 12.04 ? 35  TYR A O   1 
ATOM   261  C  CB  . TYR A 1 47  ? 15.593  -12.376 13.012  1.00 11.57 ? 35  TYR A CB  1 
ATOM   262  C  CG  . TYR A 1 47  ? 15.369  -10.894 13.249  1.00 11.84 ? 35  TYR A CG  1 
ATOM   263  C  CD1 . TYR A 1 47  ? 16.047  -9.928  12.530  1.00 10.32 ? 35  TYR A CD1 1 
ATOM   264  C  CD2 . TYR A 1 47  ? 14.428  -10.460 14.186  1.00 11.63 ? 35  TYR A CD2 1 
ATOM   265  C  CE1 . TYR A 1 47  ? 15.792  -8.572  12.711  1.00 10.98 ? 35  TYR A CE1 1 
ATOM   266  C  CE2 . TYR A 1 47  ? 14.210  -9.110  14.420  1.00 10.68 ? 35  TYR A CE2 1 
ATOM   267  C  CZ  . TYR A 1 47  ? 14.890  -8.159  13.685  1.00 11.11 ? 35  TYR A CZ  1 
ATOM   268  O  OH  . TYR A 1 47  ? 14.688  -6.834  13.930  1.00 12.71 ? 35  TYR A OH  1 
ATOM   269  N  N   . SER A 1 48  ? 12.654  -13.425 13.053  1.00 12.09 ? 36  SER A N   1 
ATOM   270  C  CA  . SER A 1 48  ? 11.279  -13.176 13.533  1.00 13.12 ? 36  SER A CA  1 
ATOM   271  C  C   . SER A 1 48  ? 11.320  -13.090 15.036  1.00 13.14 ? 36  SER A C   1 
ATOM   272  O  O   . SER A 1 48  ? 12.120  -13.811 15.685  1.00 13.88 ? 36  SER A O   1 
ATOM   273  C  CB  . SER A 1 48  ? 10.296  -14.242 13.060  1.00 15.32 ? 36  SER A CB  1 
ATOM   274  O  OG  . SER A 1 48  ? 10.157  -14.236 11.631  1.00 20.81 ? 36  SER A OG  1 
ATOM   275  N  N   . VAL A 1 49  ? 10.452  -12.257 15.596  1.00 12.42 ? 37  VAL A N   1 
ATOM   276  C  CA  . VAL A 1 49  ? 10.240  -12.240 17.040  1.00 14.01 ? 37  VAL A CA  1 
ATOM   277  C  C   . VAL A 1 49  ? 8.734   -12.129 17.292  1.00 14.20 ? 37  VAL A C   1 
ATOM   278  O  O   . VAL A 1 49  ? 8.044   -11.428 16.554  1.00 14.86 ? 37  VAL A O   1 
ATOM   279  C  CB  . VAL A 1 49  ? 11.054  -11.141 17.729  1.00 15.66 ? 37  VAL A CB  1 
ATOM   280  C  CG1 . VAL A 1 49  ? 10.769  -9.722  17.264  1.00 17.98 ? 37  VAL A CG1 1 
ATOM   281  C  CG2 . VAL A 1 49  ? 10.998  -11.275 19.232  1.00 16.18 ? 37  VAL A CG2 1 
ATOM   282  N  N   . GLU A 1 50  ? 8.256   -12.822 18.313  1.00 14.18 ? 38  GLU A N   1 
ATOM   283  C  CA  . GLU A 1 50  ? 6.823   -12.773 18.719  1.00 17.10 ? 38  GLU A CA  1 
ATOM   284  C  C   . GLU A 1 50  ? 6.824   -12.516 20.225  1.00 16.52 ? 38  GLU A C   1 
ATOM   285  O  O   . GLU A 1 50  ? 7.653   -13.125 20.929  1.00 16.34 ? 38  GLU A O   1 
ATOM   286  C  CB  . GLU A 1 50  ? 6.056   -14.054 18.351  1.00 23.23 ? 38  GLU A CB  1 
ATOM   287  C  CG  . GLU A 1 50  ? 6.201   -14.500 16.900  1.00 27.78 ? 38  GLU A CG  1 
ATOM   288  C  CD  . GLU A 1 50  ? 5.043   -15.237 16.240  1.00 36.26 ? 38  GLU A CD  1 
ATOM   289  O  OE1 . GLU A 1 50  ? 5.241   -15.754 15.103  1.00 39.45 ? 38  GLU A OE1 1 
ATOM   290  O  OE2 . GLU A 1 50  ? 3.942   -15.265 16.834  1.00 44.53 ? 38  GLU A OE2 1 
ATOM   291  N  N   . TRP A 1 51  ? 5.971   -11.644 20.734  1.00 15.07 ? 39  TRP A N   1 
ATOM   292  C  CA  . TRP A 1 51  ? 6.079   -11.319 22.179  1.00 14.53 ? 39  TRP A CA  1 
ATOM   293  C  C   . TRP A 1 51  ? 4.703   -11.066 22.754  1.00 14.84 ? 39  TRP A C   1 
ATOM   294  O  O   . TRP A 1 51  ? 3.799   -10.693 22.015  1.00 14.15 ? 39  TRP A O   1 
ATOM   295  C  CB  . TRP A 1 51  ? 7.038   -10.204 22.459  1.00 13.84 ? 39  TRP A CB  1 
ATOM   296  C  CG  . TRP A 1 51  ? 6.665   -8.827  21.992  1.00 13.71 ? 39  TRP A CG  1 
ATOM   297  C  CD1 . TRP A 1 51  ? 6.132   -7.831  22.757  1.00 14.51 ? 39  TRP A CD1 1 
ATOM   298  C  CD2 . TRP A 1 51  ? 6.865   -8.263  20.673  1.00 13.65 ? 39  TRP A CD2 1 
ATOM   299  N  NE1 . TRP A 1 51  ? 6.033   -6.683  22.036  1.00 14.31 ? 39  TRP A NE1 1 
ATOM   300  C  CE2 . TRP A 1 51  ? 6.416   -6.922  20.739  1.00 14.71 ? 39  TRP A CE2 1 
ATOM   301  C  CE3 . TRP A 1 51  ? 7.353   -8.767  19.455  1.00 13.37 ? 39  TRP A CE3 1 
ATOM   302  C  CZ2 . TRP A 1 51  ? 6.510   -6.049  19.651  1.00 15.12 ? 39  TRP A CZ2 1 
ATOM   303  C  CZ3 . TRP A 1 51  ? 7.386   -7.925  18.367  1.00 12.58 ? 39  TRP A CZ3 1 
ATOM   304  C  CH2 . TRP A 1 51  ? 6.976   -6.593  18.462  1.00 14.17 ? 39  TRP A CH2 1 
ATOM   305  N  N   . SER A 1 52  ? 4.558   -11.421 24.021  1.00 14.39 ? 40  SER A N   1 
ATOM   306  C  CA  . SER A 1 52  ? 3.257   -11.342 24.718  1.00 16.55 ? 40  SER A CA  1 
ATOM   307  C  C   . SER A 1 52  ? 3.521   -10.813 26.134  1.00 16.97 ? 40  SER A C   1 
ATOM   308  O  O   . SER A 1 52  ? 4.265   -11.482 26.876  1.00 17.43 ? 40  SER A O   1 
ATOM   309  C  CB  . SER A 1 52  ? 2.586   -12.687 24.700  1.00 20.41 ? 40  SER A CB  1 
ATOM   310  O  OG  . SER A 1 52  ? 1.381   -12.649 25.472  1.00 27.33 ? 40  SER A OG  1 
ATOM   311  N  N   . ASN A 1 53  ? 2.944   -9.659  26.476  1.00 16.27 ? 41  ASN A N   1 
ATOM   312  C  CA  . ASN A 1 53  ? 3.036   -9.008  27.805  1.00 17.05 ? 41  ASN A CA  1 
ATOM   313  C  C   . ASN A 1 53  ? 4.483   -8.956  28.264  1.00 15.50 ? 41  ASN A C   1 
ATOM   314  O  O   . ASN A 1 53  ? 4.797   -9.463  29.377  1.00 16.24 ? 41  ASN A O   1 
ATOM   315  C  CB  . ASN A 1 53  ? 2.161   -9.742  28.828  1.00 18.46 ? 41  ASN A CB  1 
ATOM   316  C  CG  . ASN A 1 53  ? 0.704   -9.565  28.515  1.00 18.34 ? 41  ASN A CG  1 
ATOM   317  O  OD1 . ASN A 1 53  ? 0.258   -8.436  28.389  1.00 19.44 ? 41  ASN A OD1 1 
ATOM   318  N  ND2 . ASN A 1 53  ? -0.018  -10.672 28.394  1.00 19.96 ? 41  ASN A ND2 1 
ATOM   319  N  N   . SER A 1 54  ? 5.360   -8.470  27.394  1.00 14.92 ? 42  SER A N   1 
ATOM   320  C  CA  . SER A 1 54  ? 6.826   -8.596  27.554  1.00 15.43 ? 42  SER A CA  1 
ATOM   321  C  C   . SER A 1 54  ? 7.351   -7.701  28.657  1.00 15.50 ? 42  SER A C   1 
ATOM   322  O  O   . SER A 1 54  ? 6.698   -6.713  29.008  1.00 15.41 ? 42  SER A O   1 
ATOM   323  C  CB  . SER A 1 54  ? 7.543   -8.239  26.264  1.00 14.41 ? 42  SER A CB  1 
ATOM   324  O  OG  . SER A 1 54  ? 7.359   -6.880  25.910  1.00 16.45 ? 42  SER A OG  1 
ATOM   325  N  N   . GLY A 1 55  ? 8.529   -8.018  29.189  1.00 15.55 ? 43  GLY A N   1 
ATOM   326  C  CA  . GLY A 1 55  ? 9.313   -6.966  29.829  1.00 16.13 ? 43  GLY A CA  1 
ATOM   327  C  C   . GLY A 1 55  ? 10.007  -6.202  28.736  1.00 18.26 ? 43  GLY A C   1 
ATOM   328  O  O   . GLY A 1 55  ? 9.410   -5.957  27.664  1.00 21.37 ? 43  GLY A O   1 
ATOM   329  N  N   . ASN A 1 56  ? 11.267  -5.906  28.953  1.00 16.32 ? 44  ASN A N   1 
ATOM   330  C  CA  . ASN A 1 56  ? 12.102  -5.196  27.967  1.00 17.85 ? 44  ASN A CA  1 
ATOM   331  C  C   . ASN A 1 56  ? 12.823  -6.252  27.136  1.00 17.71 ? 44  ASN A C   1 
ATOM   332  O  O   . ASN A 1 56  ? 13.363  -7.193  27.726  1.00 16.89 ? 44  ASN A O   1 
ATOM   333  C  CB  . ASN A 1 56  ? 13.156  -4.330  28.654  1.00 21.43 ? 44  ASN A CB  1 
ATOM   334  C  CG  . ASN A 1 56  ? 12.672  -2.932  28.893  1.00 29.16 ? 44  ASN A CG  1 
ATOM   335  O  OD1 . ASN A 1 56  ? 12.399  -2.203  27.932  1.00 39.44 ? 44  ASN A OD1 1 
ATOM   336  N  ND2 . ASN A 1 56  ? 12.538  -2.576  30.158  1.00 37.38 ? 44  ASN A ND2 1 
ATOM   337  N  N   . PHE A 1 57  ? 12.863  -6.092  25.819  1.00 14.50 ? 45  PHE A N   1 
ATOM   338  C  CA  . PHE A 1 57  ? 13.648  -6.995  24.962  1.00 13.74 ? 45  PHE A CA  1 
ATOM   339  C  C   . PHE A 1 57  ? 14.177  -6.171  23.794  1.00 14.43 ? 45  PHE A C   1 
ATOM   340  O  O   . PHE A 1 57  ? 13.536  -5.164  23.376  1.00 12.60 ? 45  PHE A O   1 
ATOM   341  C  CB  . PHE A 1 57  ? 12.818  -8.204  24.508  1.00 14.53 ? 45  PHE A CB  1 
ATOM   342  C  CG  . PHE A 1 57  ? 11.839  -7.894  23.405  1.00 14.91 ? 45  PHE A CG  1 
ATOM   343  C  CD1 . PHE A 1 57  ? 12.208  -7.958  22.072  1.00 15.29 ? 45  PHE A CD1 1 
ATOM   344  C  CD2 . PHE A 1 57  ? 10.553  -7.485  23.720  1.00 15.60 ? 45  PHE A CD2 1 
ATOM   345  C  CE1 . PHE A 1 57  ? 11.289  -7.683  21.074  1.00 17.75 ? 45  PHE A CE1 1 
ATOM   346  C  CE2 . PHE A 1 57  ? 9.632   -7.225  22.725  1.00 16.59 ? 45  PHE A CE2 1 
ATOM   347  C  CZ  . PHE A 1 57  ? 10.015  -7.284  21.407  1.00 17.94 ? 45  PHE A CZ  1 
ATOM   348  N  N   . VAL A 1 58  ? 15.281  -6.646  23.198  1.00 12.82 ? 46  VAL A N   1 
ATOM   349  C  CA  . VAL A 1 58  ? 15.817  -6.062  21.947  1.00 14.39 ? 46  VAL A CA  1 
ATOM   350  C  C   . VAL A 1 58  ? 16.309  -7.240  21.120  1.00 15.37 ? 46  VAL A C   1 
ATOM   351  O  O   . VAL A 1 58  ? 17.022  -8.103  21.685  1.00 16.42 ? 46  VAL A O   1 
ATOM   352  C  CB  . VAL A 1 58  ? 16.999  -5.103  22.195  1.00 18.34 ? 46  VAL A CB  1 
ATOM   353  C  CG1 . VAL A 1 58  ? 17.498  -4.523  20.886  1.00 19.08 ? 46  VAL A CG1 1 
ATOM   354  C  CG2 . VAL A 1 58  ? 16.681  -3.995  23.191  1.00 19.97 ? 46  VAL A CG2 1 
ATOM   355  N  N   . ALA A 1 59  ? 15.922  -7.317  19.862  1.00 12.86 ? 47  ALA A N   1 
ATOM   356  C  CA  . ALA A 1 59  ? 16.243  -8.511  19.039  1.00 13.53 ? 47  ALA A CA  1 
ATOM   357  C  C   . ALA A 1 59  ? 16.595  -8.076  17.630  1.00 12.08 ? 47  ALA A C   1 
ATOM   358  O  O   . ALA A 1 59  ? 15.840  -7.283  17.023  1.00 11.47 ? 47  ALA A O   1 
ATOM   359  C  CB  . ALA A 1 59  ? 15.077  -9.418  19.030  1.00 15.85 ? 47  ALA A CB  1 
ATOM   360  N  N   . GLY A 1 60  ? 17.658  -8.619  17.074  1.00 11.56 ? 48  GLY A N   1 
ATOM   361  C  CA  . GLY A 1 60  ? 17.869  -8.399  15.646  1.00 9.93  ? 48  GLY A CA  1 
ATOM   362  C  C   . GLY A 1 60  ? 19.129  -8.991  15.097  1.00 10.53 ? 48  GLY A C   1 
ATOM   363  O  O   . GLY A 1 60  ? 19.921  -9.629  15.859  1.00 12.39 ? 48  GLY A O   1 
ATOM   364  N  N   . LYS A 1 61  ? 19.325  -8.743  13.820  1.00 10.96 ? 49  LYS A N   1 
ATOM   365  C  CA  . LYS A 1 61  ? 20.482  -9.238  13.031  1.00 11.13 ? 49  LYS A CA  1 
ATOM   366  C  C   . LYS A 1 61  ? 21.247  -8.087  12.431  1.00 11.63 ? 49  LYS A C   1 
ATOM   367  O  O   . LYS A 1 61  ? 20.685  -7.033  12.142  1.00 9.85  ? 49  LYS A O   1 
ATOM   368  C  CB  . LYS A 1 61  ? 20.079  -10.137 11.852  1.00 11.34 ? 49  LYS A CB  1 
ATOM   369  C  CG  . LYS A 1 61  ? 20.105  -11.624 12.127  1.00 11.73 ? 49  LYS A CG  1 
ATOM   370  C  CD  . LYS A 1 61  ? 19.666  -12.507 10.977  1.00 12.25 ? 49  LYS A CD  1 
ATOM   371  C  CE  . LYS A 1 61  ? 19.866  -13.992 11.226  1.00 13.22 ? 49  LYS A CE  1 
ATOM   372  N  NZ  . LYS A 1 61  ? 19.430  -14.866 10.117  1.00 13.99 ? 49  LYS A NZ  1 
ATOM   373  N  N   . GLY A 1 62  ? 22.544  -8.323  12.242  1.00 11.96 ? 50  GLY A N   1 
ATOM   374  C  CA  . GLY A 1 62  ? 23.405  -7.355  11.569  1.00 11.67 ? 50  GLY A CA  1 
ATOM   375  C  C   . GLY A 1 62  ? 24.862  -7.793  11.603  1.00 13.21 ? 50  GLY A C   1 
ATOM   376  O  O   . GLY A 1 62  ? 25.157  -8.937  11.200  1.00 13.57 ? 50  GLY A O   1 
ATOM   377  N  N   . TRP A 1 63  ? 25.722  -6.954  12.153  1.00 13.80 ? 51  TRP A N   1 
ATOM   378  C  CA  . TRP A 1 63  ? 27.199  -7.100  12.072  1.00 14.40 ? 51  TRP A CA  1 
ATOM   379  C  C   . TRP A 1 63  ? 27.837  -6.935  13.448  1.00 15.16 ? 51  TRP A C   1 
ATOM   380  O  O   . TRP A 1 63  ? 27.404  -6.093  14.260  1.00 14.65 ? 51  TRP A O   1 
ATOM   381  C  CB  . TRP A 1 63  ? 27.797  -6.090  11.094  1.00 15.33 ? 51  TRP A CB  1 
ATOM   382  C  CG  . TRP A 1 63  ? 27.178  -6.200  9.747   1.00 17.18 ? 51  TRP A CG  1 
ATOM   383  C  CD1 . TRP A 1 63  ? 27.635  -6.954  8.699   1.00 21.99 ? 51  TRP A CD1 1 
ATOM   384  C  CD2 . TRP A 1 63  ? 25.955  -5.589  9.311   1.00 16.41 ? 51  TRP A CD2 1 
ATOM   385  N  NE1 . TRP A 1 63  ? 26.775  -6.843  7.635   1.00 22.10 ? 51  TRP A NE1 1 
ATOM   386  C  CE2 . TRP A 1 63  ? 25.730  -6.041  7.991   1.00 20.28 ? 51  TRP A CE2 1 
ATOM   387  C  CE3 . TRP A 1 63  ? 25.018  -4.739  9.910   1.00 17.58 ? 51  TRP A CE3 1 
ATOM   388  C  CZ2 . TRP A 1 63  ? 24.651  -5.604  7.227   1.00 20.79 ? 51  TRP A CZ2 1 
ATOM   389  C  CZ3 . TRP A 1 63  ? 23.937  -4.330  9.160   1.00 21.10 ? 51  TRP A CZ3 1 
ATOM   390  C  CH2 . TRP A 1 63  ? 23.757  -4.763  7.840   1.00 20.69 ? 51  TRP A CH2 1 
ATOM   391  N  N   . ASN A 1 64  ? 28.956  -7.625  13.636  1.00 16.38 ? 52  ASN A N   1 
ATOM   392  C  CA  . ASN A 1 64  ? 29.793  -7.408  14.834  1.00 16.79 ? 52  ASN A CA  1 
ATOM   393  C  C   . ASN A 1 64  ? 31.270  -7.593  14.462  1.00 19.38 ? 52  ASN A C   1 
ATOM   394  O  O   . ASN A 1 64  ? 31.711  -8.714  14.267  1.00 21.55 ? 52  ASN A O   1 
ATOM   395  C  CB  . ASN A 1 64  ? 29.361  -8.307  15.968  1.00 18.61 ? 52  ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 64  ? 30.075  -7.962  17.257  1.00 21.17 ? 52  ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 64  ? 30.538  -6.835  17.426  1.00 20.02 ? 52  ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 64  ? 30.168  -8.934  18.152  1.00 25.57 ? 52  ASN A ND2 1 
ATOM   399  N  N   . PRO A 1 65  ? 32.036  -6.492  14.393  1.00 19.92 ? 53  PRO A N   1 
ATOM   400  C  CA  . PRO A 1 65  ? 31.512  -5.163  14.716  1.00 19.04 ? 53  PRO A CA  1 
ATOM   401  C  C   . PRO A 1 65  ? 30.775  -4.489  13.562  1.00 18.34 ? 53  PRO A C   1 
ATOM   402  O  O   . PRO A 1 65  ? 30.978  -4.876  12.421  1.00 19.35 ? 53  PRO A O   1 
ATOM   403  C  CB  . PRO A 1 65  ? 32.787  -4.359  14.969  1.00 21.85 ? 53  PRO A CB  1 
ATOM   404  C  CG  . PRO A 1 65  ? 33.749  -4.957  13.987  1.00 22.79 ? 53  PRO A CG  1 
ATOM   405  C  CD  . PRO A 1 65  ? 33.480  -6.442  14.032  1.00 22.51 ? 53  PRO A CD  1 
ATOM   406  N  N   . GLY A 1 66  ? 30.011  -3.444  13.889  1.00 16.86 ? 54  GLY A N   1 
ATOM   407  C  CA  . GLY A 1 66  ? 29.496  -2.503  12.901  1.00 19.10 ? 54  GLY A CA  1 
ATOM   408  C  C   . GLY A 1 66  ? 30.643  -1.773  12.224  1.00 20.98 ? 54  GLY A C   1 
ATOM   409  O  O   . GLY A 1 66  ? 31.676  -1.473  12.870  1.00 17.19 ? 54  GLY A O   1 
ATOM   410  N  N   . SER A 1 67  ? 30.495  -1.537  10.934  1.00 22.42 ? 55  SER A N   1 
ATOM   411  C  CA  . SER A 1 67  ? 31.238  -0.445  10.292  1.00 30.01 ? 55  SER A CA  1 
ATOM   412  C  C   . SER A 1 67  ? 30.239  0.695   10.388  1.00 34.89 ? 55  SER A C   1 
ATOM   413  O  O   . SER A 1 67  ? 29.490  0.770   11.379  1.00 46.61 ? 55  SER A O   1 
ATOM   414  C  CB  . SER A 1 67  ? 31.678  -0.773  8.899   1.00 35.91 ? 55  SER A CB  1 
ATOM   415  O  OG  . SER A 1 67  ? 32.031  -2.135  8.800   1.00 30.29 ? 55  SER A OG  1 
ATOM   416  N  N   . SER A 1 68  ? 30.220  1.527   9.401   1.00 37.97 ? 56  SER A N   1 
ATOM   417  C  CA  . SER A 1 68  ? 29.248  2.617   9.284   1.00 29.80 ? 56  SER A CA  1 
ATOM   418  C  C   . SER A 1 68  ? 28.587  2.389   7.931   1.00 26.95 ? 56  SER A C   1 
ATOM   419  O  O   . SER A 1 68  ? 28.513  3.312   7.139   1.00 31.48 ? 56  SER A O   1 
ATOM   420  C  CB  . SER A 1 68  ? 30.003  3.898   9.446   1.00 29.13 ? 56  SER A CB  1 
ATOM   421  O  OG  . SER A 1 68  ? 30.557  3.966   10.762  1.00 31.04 ? 56  SER A OG  1 
ATOM   422  N  N   . GLN A 1 69  ? 28.145  1.157   7.717   1.00 25.97 ? 57  GLN A N   1 
ATOM   423  C  CA  . GLN A 1 69  ? 27.639  0.714   6.398   1.00 25.08 ? 57  GLN A CA  1 
ATOM   424  C  C   . GLN A 1 69  ? 26.206  1.189   6.186   1.00 21.08 ? 57  GLN A C   1 
ATOM   425  O  O   . GLN A 1 69  ? 25.450  1.483   7.145   1.00 17.81 ? 57  GLN A O   1 
ATOM   426  C  CB  . GLN A 1 69  ? 27.766  -0.789  6.183   1.00 25.02 ? 57  GLN A CB  1 
ATOM   427  C  CG  . GLN A 1 69  ? 27.017  -1.670  7.165   1.00 25.34 ? 57  GLN A CG  1 
ATOM   428  C  CD  . GLN A 1 69  ? 27.965  -2.361  8.126   1.00 25.86 ? 57  GLN A CD  1 
ATOM   429  O  OE1 . GLN A 1 69  ? 28.368  -3.511  7.945   1.00 32.36 ? 57  GLN A OE1 1 
ATOM   430  N  NE2 . GLN A 1 69  ? 28.332  -1.644  9.166   1.00 21.01 ? 57  GLN A NE2 1 
ATOM   431  N  N   . THR A 1 70  ? 25.861  1.228   4.916   1.00 21.82 ? 58  THR A N   1 
ATOM   432  C  CA  . THR A 1 70  ? 24.512  1.563   4.433   1.00 20.82 ? 58  THR A CA  1 
ATOM   433  C  C   . THR A 1 70  ? 23.680  0.287   4.549   1.00 20.09 ? 58  THR A C   1 
ATOM   434  O  O   . THR A 1 70  ? 23.990  -0.700  3.879   1.00 25.53 ? 58  THR A O   1 
ATOM   435  C  CB  . THR A 1 70  ? 24.631  2.208   3.053   1.00 21.61 ? 58  THR A CB  1 
ATOM   436  O  OG1 . THR A 1 70  ? 25.366  3.414   3.278   1.00 22.56 ? 58  THR A OG1 1 
ATOM   437  C  CG2 . THR A 1 70  ? 23.287  2.521   2.423   1.00 21.39 ? 58  THR A CG2 1 
ATOM   438  N  N   . ILE A 1 71  ? 22.649  0.311   5.380   1.00 18.09 ? 59  ILE A N   1 
ATOM   439  C  CA  . ILE A 1 71  ? 21.832  -0.884  5.707   1.00 18.17 ? 59  ILE A CA  1 
ATOM   440  C  C   . ILE A 1 71  ? 20.612  -0.809  4.789   1.00 17.42 ? 59  ILE A C   1 
ATOM   441  O  O   . ILE A 1 71  ? 20.103  0.327   4.576   1.00 18.67 ? 59  ILE A O   1 
ATOM   442  C  CB  . ILE A 1 71  ? 21.419  -0.887  7.187   1.00 18.11 ? 59  ILE A CB  1 
ATOM   443  C  CG1 . ILE A 1 71  ? 22.651  -0.970  8.100   1.00 19.07 ? 59  ILE A CG1 1 
ATOM   444  C  CG2 . ILE A 1 71  ? 20.418  -2.014  7.470   1.00 20.40 ? 59  ILE A CG2 1 
ATOM   445  C  CD1 . ILE A 1 71  ? 22.337  -0.869  9.571   1.00 18.14 ? 59  ILE A CD1 1 
ATOM   446  N  N   . THR A 1 72  ? 20.215  -1.943  4.249   1.00 15.28 ? 60  THR A N   1 
ATOM   447  C  CA  . THR A 1 72  ? 18.890  -2.097  3.608   1.00 17.31 ? 60  THR A CA  1 
ATOM   448  C  C   . THR A 1 72  ? 18.140  -3.144  4.399   1.00 16.51 ? 60  THR A C   1 
ATOM   449  O  O   . THR A 1 72  ? 18.755  -4.149  4.742   1.00 19.24 ? 60  THR A O   1 
ATOM   450  C  CB  . THR A 1 72  ? 19.071  -2.424  2.133   1.00 19.86 ? 60  THR A CB  1 
ATOM   451  O  OG1 . THR A 1 72  ? 19.944  -3.543  1.983   1.00 29.46 ? 60  THR A OG1 1 
ATOM   452  C  CG2 . THR A 1 72  ? 19.598  -1.244  1.358   1.00 19.50 ? 60  THR A CG2 1 
ATOM   453  N  N   . TYR A 1 73  ? 16.872  -2.903  4.701   1.00 15.48 ? 61  TYR A N   1 
ATOM   454  C  CA  . TYR A 1 73  ? 16.102  -3.920  5.453   1.00 15.62 ? 61  TYR A CA  1 
ATOM   455  C  C   . TYR A 1 73  ? 14.692  -3.919  4.888   1.00 13.48 ? 61  TYR A C   1 
ATOM   456  O  O   . TYR A 1 73  ? 14.251  -2.861  4.355   1.00 13.40 ? 61  TYR A O   1 
ATOM   457  C  CB  . TYR A 1 73  ? 16.167  -3.662  6.961   1.00 16.18 ? 61  TYR A CB  1 
ATOM   458  C  CG  . TYR A 1 73  ? 15.358  -2.477  7.401   1.00 16.34 ? 61  TYR A CG  1 
ATOM   459  C  CD1 . TYR A 1 73  ? 15.814  -1.188  7.225   1.00 15.95 ? 61  TYR A CD1 1 
ATOM   460  C  CD2 . TYR A 1 73  ? 14.112  -2.648  7.971   1.00 17.25 ? 61  TYR A CD2 1 
ATOM   461  C  CE1 . TYR A 1 73  ? 15.026  -0.086  7.516   1.00 18.35 ? 61  TYR A CE1 1 
ATOM   462  C  CE2 . TYR A 1 73  ? 13.369  -1.575  8.374   1.00 15.39 ? 61  TYR A CE2 1 
ATOM   463  C  CZ  . TYR A 1 73  ? 13.793  -0.291  8.121   1.00 17.65 ? 61  TYR A CZ  1 
ATOM   464  O  OH  . TYR A 1 73  ? 13.012  0.766   8.463   1.00 18.90 ? 61  TYR A OH  1 
ATOM   465  N  N   . SER A 1 74  ? 14.019  -5.030  5.090   1.00 14.00 ? 62  SER A N   1 
ATOM   466  C  CA  . SER A 1 74  ? 12.631  -5.251  4.597   1.00 14.37 ? 62  SER A CA  1 
ATOM   467  C  C   . SER A 1 74  ? 11.865  -6.025  5.670   1.00 14.02 ? 62  SER A C   1 
ATOM   468  O  O   . SER A 1 74  ? 12.491  -6.592  6.596   1.00 13.60 ? 62  SER A O   1 
ATOM   469  C  CB  . SER A 1 74  ? 12.665  -5.970  3.276   1.00 17.14 ? 62  SER A CB  1 
ATOM   470  O  OG  . SER A 1 74  ? 13.166  -7.302  3.437   1.00 21.01 ? 62  SER A OG  1 
ATOM   471  N  N   . GLY A 1 75  ? 10.553  -6.021  5.534   1.00 12.34 ? 63  GLY A N   1 
ATOM   472  C  CA  . GLY A 1 75  ? 9.693   -6.945  6.271   1.00 13.00 ? 63  GLY A CA  1 
ATOM   473  C  C   . GLY A 1 75  ? 8.496   -6.244  6.848   1.00 11.84 ? 63  GLY A C   1 
ATOM   474  O  O   . GLY A 1 75  ? 7.973   -5.290  6.243   1.00 12.13 ? 63  GLY A O   1 
ATOM   475  N  N   . GLU A 1 76  ? 8.081   -6.756  7.995   1.00 11.60 ? 64  GLU A N   1 
ATOM   476  C  CA  . GLU A 1 76  ? 6.850   -6.272  8.654   1.00 14.03 ? 64  GLU A CA  1 
ATOM   477  C  C   . GLU A 1 76  ? 7.084   -6.234  10.162  1.00 13.65 ? 64  GLU A C   1 
ATOM   478  O  O   . GLU A 1 76  ? 7.885   -7.035  10.688  1.00 13.65 ? 64  GLU A O   1 
ATOM   479  C  CB  . GLU A 1 76  ? 5.683   -7.127  8.238   1.00 15.78 ? 64  GLU A CB  1 
ATOM   480  C  CG  . GLU A 1 76  ? 5.739   -8.538  8.707   1.00 18.90 ? 64  GLU A CG  1 
ATOM   481  C  CD  . GLU A 1 76  ? 4.608   -9.371  8.132   1.00 23.88 ? 64  GLU A CD  1 
ATOM   482  O  OE1 . GLU A 1 76  ? 3.655   -8.776  7.579   1.00 28.65 ? 64  GLU A OE1 1 
ATOM   483  O  OE2 . GLU A 1 76  ? 4.734   -10.585 8.206   1.00 31.62 ? 64  GLU A OE2 1 
ATOM   484  N  N   . TRP A 1 77  ? 6.394   -5.312  10.811  1.00 12.44 ? 65  TRP A N   1 
ATOM   485  C  CA  . TRP A 1 77  ? 6.568   -4.974  12.235  1.00 13.95 ? 65  TRP A CA  1 
ATOM   486  C  C   . TRP A 1 77  ? 5.163   -4.664  12.737  1.00 13.22 ? 65  TRP A C   1 
ATOM   487  O  O   . TRP A 1 77  ? 4.612   -3.662  12.291  1.00 14.48 ? 65  TRP A O   1 
ATOM   488  C  CB  . TRP A 1 77  ? 7.538   -3.811  12.322  1.00 13.99 ? 65  TRP A CB  1 
ATOM   489  C  CG  . TRP A 1 77  ? 7.675   -3.164  13.665  1.00 14.75 ? 65  TRP A CG  1 
ATOM   490  C  CD1 . TRP A 1 77  ? 8.323   -3.649  14.762  1.00 17.12 ? 65  TRP A CD1 1 
ATOM   491  C  CD2 . TRP A 1 77  ? 7.182   -1.867  14.033  1.00 14.49 ? 65  TRP A CD2 1 
ATOM   492  N  NE1 . TRP A 1 77  ? 8.278   -2.728  15.777  1.00 17.30 ? 65  TRP A NE1 1 
ATOM   493  C  CE2 . TRP A 1 77  ? 7.576   -1.635  15.365  1.00 17.22 ? 65  TRP A CE2 1 
ATOM   494  C  CE3 . TRP A 1 77  ? 6.451   -0.889  13.359  1.00 15.63 ? 65  TRP A CE3 1 
ATOM   495  C  CZ2 . TRP A 1 77  ? 7.289   -0.449  16.036  1.00 16.95 ? 65  TRP A CZ2 1 
ATOM   496  C  CZ3 . TRP A 1 77  ? 6.106   0.247   14.043  1.00 16.37 ? 65  TRP A CZ3 1 
ATOM   497  C  CH2 . TRP A 1 77  ? 6.526   0.464   15.359  1.00 16.29 ? 65  TRP A CH2 1 
ATOM   498  N  N   . ASN A 1 78  ? 4.630   -5.507  13.615  1.00 12.79 ? 66  ASN A N   1 
ATOM   499  C  CA  . ASN A 1 78  ? 3.200   -5.472  13.991  1.00 14.56 ? 66  ASN A CA  1 
ATOM   500  C  C   . ASN A 1 78  ? 3.080   -5.424  15.502  1.00 13.06 ? 66  ASN A C   1 
ATOM   501  O  O   . ASN A 1 78  ? 2.626   -6.401  16.073  1.00 14.47 ? 66  ASN A O   1 
ATOM   502  C  CB  . ASN A 1 78  ? 2.454   -6.648  13.372  1.00 17.84 ? 66  ASN A CB  1 
ATOM   503  C  CG  . ASN A 1 78  ? 2.486   -6.592  11.855  1.00 19.13 ? 66  ASN A CG  1 
ATOM   504  O  OD1 . ASN A 1 78  ? 1.876   -5.714  11.263  1.00 25.41 ? 66  ASN A OD1 1 
ATOM   505  N  ND2 . ASN A 1 78  ? 3.140   -7.551  11.228  1.00 25.39 ? 66  ASN A ND2 1 
ATOM   506  N  N   . PRO A 1 79  ? 3.469   -4.303  16.158  1.00 15.91 ? 67  PRO A N   1 
ATOM   507  C  CA  . PRO A 1 79  ? 3.365   -4.178  17.614  1.00 13.49 ? 67  PRO A CA  1 
ATOM   508  C  C   . PRO A 1 79  ? 1.911   -3.928  18.018  1.00 16.46 ? 67  PRO A C   1 
ATOM   509  O  O   . PRO A 1 79  ? 1.171   -3.349  17.259  1.00 17.75 ? 67  PRO A O   1 
ATOM   510  C  CB  . PRO A 1 79  ? 4.208   -2.964  17.958  1.00 15.96 ? 67  PRO A CB  1 
ATOM   511  C  CG  . PRO A 1 79  ? 4.166   -2.119  16.705  1.00 17.24 ? 67  PRO A CG  1 
ATOM   512  C  CD  . PRO A 1 79  ? 3.998   -3.085  15.543  1.00 16.23 ? 67  PRO A CD  1 
ATOM   513  N  N   . ASN A 1 80  ? 1.533   -4.451  19.166  1.00 16.28 ? 68  ASN A N   1 
ATOM   514  C  CA  . ASN A 1 80  ? 0.360   -3.953  19.921  1.00 19.81 ? 68  ASN A CA  1 
ATOM   515  C  C   . ASN A 1 80  ? 0.834   -3.350  21.252  1.00 16.33 ? 68  ASN A C   1 
ATOM   516  O  O   . ASN A 1 80  ? 0.922   -4.105  22.230  1.00 16.19 ? 68  ASN A O   1 
ATOM   517  C  CB  . ASN A 1 80  ? -0.640  -5.077  20.095  1.00 22.01 ? 68  ASN A CB  1 
ATOM   518  C  CG  . ASN A 1 80  ? -1.871  -4.556  20.801  1.00 26.33 ? 68  ASN A CG  1 
ATOM   519  O  OD1 . ASN A 1 80  ? -2.343  -3.474  20.465  1.00 31.40 ? 68  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A 1 80  ? -2.374  -5.317  21.762  1.00 29.63 ? 68  ASN A ND2 1 
ATOM   521  N  N   . GLY A 1 81  ? 1.107   -2.054  21.279  1.00 16.43 ? 69  GLY A N   1 
ATOM   522  C  CA  . GLY A 1 81  ? 1.778   -1.359  22.396  1.00 17.48 ? 69  GLY A CA  1 
ATOM   523  C  C   . GLY A 1 81  ? 3.227   -1.020  22.094  1.00 18.05 ? 69  GLY A C   1 
ATOM   524  O  O   . GLY A 1 81  ? 3.649   -1.107  20.919  1.00 18.45 ? 69  GLY A O   1 
ATOM   525  N  N   . ASN A 1 82  ? 3.975   -0.657  23.136  1.00 16.43 ? 70  ASN A N   1 
ATOM   526  C  CA  . ASN A 1 82  ? 5.254   0.065   23.053  1.00 16.07 ? 70  ASN A CA  1 
ATOM   527  C  C   . ASN A 1 82  ? 6.305   -0.806  22.353  1.00 14.72 ? 70  ASN A C   1 
ATOM   528  O  O   . ASN A 1 82  ? 6.667   -1.852  22.916  1.00 15.56 ? 70  ASN A O   1 
ATOM   529  C  CB  . ASN A 1 82  ? 5.708   0.489   24.451  1.00 17.46 ? 70  ASN A CB  1 
ATOM   530  C  CG  . ASN A 1 82  ? 7.033   1.202   24.481  1.00 18.91 ? 70  ASN A CG  1 
ATOM   531  O  OD1 . ASN A 1 82  ? 7.569   1.577   23.452  1.00 21.55 ? 70  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A 1 82  ? 7.530   1.503   25.676  1.00 22.71 ? 70  ASN A ND2 1 
ATOM   533  N  N   . SER A 1 83  ? 6.796   -0.344  21.214  1.00 13.28 ? 71  SER A N   1 
ATOM   534  C  CA  . SER A 1 83  ? 7.797   -1.072  20.412  1.00 12.95 ? 71  SER A CA  1 
ATOM   535  C  C   . SER A 1 83  ? 8.527   -0.052  19.536  1.00 14.11 ? 71  SER A C   1 
ATOM   536  O  O   . SER A 1 83  ? 7.888   0.936   19.088  1.00 13.59 ? 71  SER A O   1 
ATOM   537  C  CB  . SER A 1 83  ? 7.168   -2.181  19.590  1.00 13.40 ? 71  SER A CB  1 
ATOM   538  O  OG  . SER A 1 83  ? 8.137   -2.971  18.849  1.00 14.11 ? 71  SER A OG  1 
ATOM   539  N  N   . TYR A 1 84  ? 9.793   -0.331  19.236  1.00 13.46 ? 72  TYR A N   1 
ATOM   540  C  CA  . TYR A 1 84  ? 10.613  0.517   18.320  1.00 15.24 ? 72  TYR A CA  1 
ATOM   541  C  C   . TYR A 1 84  ? 11.206  -0.415  17.257  1.00 12.87 ? 72  TYR A C   1 
ATOM   542  O  O   . TYR A 1 84  ? 11.446  -1.585  17.564  1.00 11.04 ? 72  TYR A O   1 
ATOM   543  C  CB  . TYR A 1 84  ? 11.850  1.179   18.982  1.00 19.08 ? 72  TYR A CB  1 
ATOM   544  C  CG  . TYR A 1 84  ? 11.793  1.767   20.368  1.00 22.80 ? 72  TYR A CG  1 
ATOM   545  C  CD1 . TYR A 1 84  ? 10.674  2.417   20.847  1.00 25.67 ? 72  TYR A CD1 1 
ATOM   546  C  CD2 . TYR A 1 84  ? 12.912  1.724   21.206  1.00 27.16 ? 72  TYR A CD2 1 
ATOM   547  C  CE1 . TYR A 1 84  ? 10.650  3.009   22.102  1.00 28.34 ? 72  TYR A CE1 1 
ATOM   548  C  CE2 . TYR A 1 84  ? 12.901  2.295   22.475  1.00 29.39 ? 72  TYR A CE2 1 
ATOM   549  C  CZ  . TYR A 1 84  ? 11.756  2.940   22.936  1.00 33.64 ? 72  TYR A CZ  1 
ATOM   550  O  OH  . TYR A 1 84  ? 11.654  3.514   24.193  1.00 29.55 ? 72  TYR A OH  1 
ATOM   551  N  N   . LEU A 1 85  ? 11.330  0.055   16.026  1.00 12.40 ? 73  LEU A N   1 
ATOM   552  C  CA  . LEU A 1 85  ? 12.101  -0.617  14.959  1.00 12.00 ? 73  LEU A CA  1 
ATOM   553  C  C   . LEU A 1 85  ? 13.275  0.320   14.679  1.00 11.95 ? 73  LEU A C   1 
ATOM   554  O  O   . LEU A 1 85  ? 13.028  1.441   14.287  1.00 10.60 ? 73  LEU A O   1 
ATOM   555  C  CB  . LEU A 1 85  ? 11.187  -0.809  13.736  1.00 12.69 ? 73  LEU A CB  1 
ATOM   556  C  CG  . LEU A 1 85  ? 11.834  -1.465  12.516  1.00 13.74 ? 73  LEU A CG  1 
ATOM   557  C  CD1 . LEU A 1 85  ? 12.359  -2.838  12.863  1.00 15.91 ? 73  LEU A CD1 1 
ATOM   558  C  CD2 . LEU A 1 85  ? 10.847  -1.547  11.374  1.00 16.53 ? 73  LEU A CD2 1 
ATOM   559  N  N   . SER A 1 86  ? 14.536  -0.117  14.854  1.00 12.37 ? 74  SER A N   1 
ATOM   560  C  CA  . SER A 1 86  ? 15.684  0.805   14.866  1.00 12.53 ? 74  SER A CA  1 
ATOM   561  C  C   . SER A 1 86  ? 16.934  0.108   14.342  1.00 12.13 ? 74  SER A C   1 
ATOM   562  O  O   . SER A 1 86  ? 17.050  -1.126  14.572  1.00 14.83 ? 74  SER A O   1 
ATOM   563  C  CB  . SER A 1 86  ? 15.986  1.361   16.276  1.00 15.62 ? 74  SER A CB  1 
ATOM   564  O  OG  . SER A 1 86  ? 14.797  1.530   17.033  1.00 21.97 ? 74  SER A OG  1 
ATOM   565  N  N   . VAL A 1 87  ? 17.824  0.873   13.708  1.00 11.45 ? 75  VAL A N   1 
ATOM   566  C  CA  . VAL A 1 87  ? 19.249  0.481   13.645  1.00 11.94 ? 75  VAL A CA  1 
ATOM   567  C  C   . VAL A 1 87  ? 19.783  0.738   15.056  1.00 13.24 ? 75  VAL A C   1 
ATOM   568  O  O   . VAL A 1 87  ? 19.610  1.881   15.592  1.00 16.14 ? 75  VAL A O   1 
ATOM   569  C  CB  . VAL A 1 87  ? 20.018  1.215   12.548  1.00 13.36 ? 75  VAL A CB  1 
ATOM   570  C  CG1 . VAL A 1 87  ? 21.511  0.842   12.645  1.00 13.61 ? 75  VAL A CG1 1 
ATOM   571  C  CG2 . VAL A 1 87  ? 19.453  0.923   11.181  1.00 13.80 ? 75  VAL A CG2 1 
ATOM   572  N  N   . TYR A 1 88  ? 20.283  -0.309  15.698  1.00 12.22 ? 76  TYR A N   1 
ATOM   573  C  CA  . TYR A 1 88  ? 20.666  -0.287  17.122  1.00 14.11 ? 76  TYR A CA  1 
ATOM   574  C  C   . TYR A 1 88  ? 22.094  -0.794  17.286  1.00 12.61 ? 76  TYR A C   1 
ATOM   575  O  O   . TYR A 1 88  ? 22.429  -1.786  16.679  1.00 12.11 ? 76  TYR A O   1 
ATOM   576  C  CB  . TYR A 1 88  ? 19.627  -1.122  17.861  1.00 14.40 ? 76  TYR A CB  1 
ATOM   577  C  CG  . TYR A 1 88  ? 19.978  -1.462  19.273  1.00 14.52 ? 76  TYR A CG  1 
ATOM   578  C  CD1 . TYR A 1 88  ? 19.822  -0.511  20.270  1.00 14.89 ? 76  TYR A CD1 1 
ATOM   579  C  CD2 . TYR A 1 88  ? 20.510  -2.690  19.615  1.00 13.32 ? 76  TYR A CD2 1 
ATOM   580  C  CE1 . TYR A 1 88  ? 20.154  -0.794  21.580  1.00 14.39 ? 76  TYR A CE1 1 
ATOM   581  C  CE2 . TYR A 1 88  ? 20.832  -2.992  20.920  1.00 14.74 ? 76  TYR A CE2 1 
ATOM   582  C  CZ  . TYR A 1 88  ? 20.660  -2.032  21.904  1.00 13.85 ? 76  TYR A CZ  1 
ATOM   583  O  OH  . TYR A 1 88  ? 20.971  -2.331  23.194  1.00 16.75 ? 76  TYR A OH  1 
ATOM   584  N  N   . GLY A 1 89  ? 22.894  -0.146  18.128  1.00 12.16 ? 77  GLY A N   1 
ATOM   585  C  CA  . GLY A 1 89  ? 24.232  -0.686  18.373  1.00 11.35 ? 77  GLY A CA  1 
ATOM   586  C  C   . GLY A 1 89  ? 24.896  -0.043  19.553  1.00 11.23 ? 77  GLY A C   1 
ATOM   587  O  O   . GLY A 1 89  ? 24.271  0.735   20.296  1.00 10.66 ? 77  GLY A O   1 
ATOM   588  N  N   . TRP A 1 90  ? 26.161  -0.386  19.688  1.00 11.56 ? 78  TRP A N   1 
ATOM   589  C  CA  . TRP A 1 90  ? 27.010  0.038   20.822  1.00 12.93 ? 78  TRP A CA  1 
ATOM   590  C  C   . TRP A 1 90  ? 28.336  0.548   20.262  1.00 12.25 ? 78  TRP A C   1 
ATOM   591  O  O   . TRP A 1 90  ? 28.841  -0.012  19.270  1.00 11.57 ? 78  TRP A O   1 
ATOM   592  C  CB  . TRP A 1 90  ? 27.241  -1.119  21.797  1.00 13.12 ? 78  TRP A CB  1 
ATOM   593  C  CG  . TRP A 1 90  ? 26.014  -1.538  22.549  1.00 14.31 ? 78  TRP A CG  1 
ATOM   594  C  CD1 . TRP A 1 90  ? 25.030  -2.380  22.127  1.00 14.70 ? 78  TRP A CD1 1 
ATOM   595  C  CD2 . TRP A 1 90  ? 25.605  -1.074  23.846  1.00 14.00 ? 78  TRP A CD2 1 
ATOM   596  N  NE1 . TRP A 1 90  ? 24.069  -2.519  23.093  1.00 15.19 ? 78  TRP A NE1 1 
ATOM   597  C  CE2 . TRP A 1 90  ? 24.383  -1.702  24.140  1.00 15.47 ? 78  TRP A CE2 1 
ATOM   598  C  CE3 . TRP A 1 90  ? 26.158  -0.198  24.785  1.00 15.02 ? 78  TRP A CE3 1 
ATOM   599  C  CZ2 . TRP A 1 90  ? 23.735  -1.522  25.356  1.00 16.00 ? 78  TRP A CZ2 1 
ATOM   600  C  CZ3 . TRP A 1 90  ? 25.502  0.007   25.972  1.00 16.05 ? 78  TRP A CZ3 1 
ATOM   601  C  CH2 . TRP A 1 90  ? 24.302  -0.657  26.252  1.00 16.50 ? 78  TRP A CH2 1 
ATOM   602  N  N   . THR A 1 91  ? 28.913  1.499   20.988  1.00 13.51 ? 79  THR A N   1 
ATOM   603  C  CA  . THR A 1 91  ? 30.369  1.777   20.938  1.00 14.27 ? 79  THR A CA  1 
ATOM   604  C  C   . THR A 1 91  ? 30.945  1.530   22.328  1.00 13.53 ? 79  THR A C   1 
ATOM   605  O  O   . THR A 1 91  ? 30.198  1.512   23.339  1.00 13.46 ? 79  THR A O   1 
ATOM   606  C  CB  . THR A 1 91  ? 30.750  3.164   20.425  1.00 14.97 ? 79  THR A CB  1 
ATOM   607  O  OG1 . THR A 1 91  ? 30.477  4.171   21.407  1.00 16.17 ? 79  THR A OG1 1 
ATOM   608  C  CG2 . THR A 1 91  ? 30.058  3.455   19.109  1.00 16.39 ? 79  THR A CG2 1 
ATOM   609  N  N   . GLN A 1 92  ? 32.234  1.290   22.323  1.00 14.43 ? 80  GLN A N   1 
ATOM   610  C  CA  . GLN A 1 92  ? 33.018  1.133   23.569  1.00 15.34 ? 80  GLN A CA  1 
ATOM   611  C  C   . GLN A 1 92  ? 34.045  2.275   23.701  1.00 14.05 ? 80  GLN A C   1 
ATOM   612  O  O   . GLN A 1 92  ? 34.588  2.747   22.705  1.00 13.46 ? 80  GLN A O   1 
ATOM   613  C  CB  . GLN A 1 92  ? 33.645  -0.259  23.557  1.00 17.04 ? 80  GLN A CB  1 
ATOM   614  C  CG  . GLN A 1 92  ? 32.681  -1.416  23.788  1.00 20.63 ? 80  GLN A CG  1 
ATOM   615  C  CD  . GLN A 1 92  ? 33.304  -2.717  23.322  1.00 25.40 ? 80  GLN A CD  1 
ATOM   616  O  OE1 . GLN A 1 92  ? 33.588  -2.893  22.138  1.00 33.62 ? 80  GLN A OE1 1 
ATOM   617  N  NE2 . GLN A 1 92  ? 33.491  -3.656  24.231  1.00 26.37 ? 80  GLN A NE2 1 
ATOM   618  N  N   . ASN A 1 93  ? 34.315  2.702   24.925  1.00 13.87 ? 81  ASN A N   1 
ATOM   619  C  CA  . ASN A 1 93  ? 35.432  3.650   25.204  1.00 14.68 ? 81  ASN A CA  1 
ATOM   620  C  C   . ASN A 1 93  ? 35.344  4.907   24.327  1.00 15.81 ? 81  ASN A C   1 
ATOM   621  O  O   . ASN A 1 93  ? 36.213  5.165   23.481  1.00 14.83 ? 81  ASN A O   1 
ATOM   622  C  CB  . ASN A 1 93  ? 36.716  2.858   24.984  1.00 16.75 ? 81  ASN A CB  1 
ATOM   623  C  CG  . ASN A 1 93  ? 37.941  3.652   25.346  1.00 16.38 ? 81  ASN A CG  1 
ATOM   624  O  OD1 . ASN A 1 93  ? 39.049  3.422   24.801  1.00 22.06 ? 81  ASN A OD1 1 
ATOM   625  N  ND2 . ASN A 1 93  ? 37.752  4.618   26.218  1.00 13.16 ? 81  ASN A ND2 1 
ATOM   626  N  N   . PRO A 1 94  ? 34.296  5.755   24.457  1.00 15.46 ? 82  PRO A N   1 
ATOM   627  C  CA  . PRO A 1 94  ? 33.277  5.606   25.492  1.00 15.23 ? 82  PRO A CA  1 
ATOM   628  C  C   . PRO A 1 94  ? 32.109  4.661   25.153  1.00 15.82 ? 82  PRO A C   1 
ATOM   629  O  O   . PRO A 1 94  ? 31.787  4.446   23.960  1.00 14.23 ? 82  PRO A O   1 
ATOM   630  C  CB  . PRO A 1 94  ? 32.705  7.018   25.621  1.00 16.48 ? 82  PRO A CB  1 
ATOM   631  C  CG  . PRO A 1 94  ? 32.849  7.590   24.268  1.00 17.97 ? 82  PRO A CG  1 
ATOM   632  C  CD  . PRO A 1 94  ? 34.138  7.011   23.718  1.00 17.59 ? 82  PRO A CD  1 
ATOM   633  N  N   . LEU A 1 95  ? 31.564  4.074   26.218  1.00 14.81 ? 83  LEU A N   1 
ATOM   634  C  CA  . LEU A 1 95  ? 30.388  3.196   26.155  1.00 15.23 ? 83  LEU A CA  1 
ATOM   635  C  C   . LEU A 1 95  ? 29.182  4.044   25.753  1.00 14.81 ? 83  LEU A C   1 
ATOM   636  O  O   . LEU A 1 95  ? 28.825  5.045   26.434  1.00 14.95 ? 83  LEU A O   1 
ATOM   637  C  CB  . LEU A 1 95  ? 30.208  2.496   27.498  1.00 15.45 ? 83  LEU A CB  1 
ATOM   638  C  CG  . LEU A 1 95  ? 29.121  1.429   27.520  1.00 16.57 ? 83  LEU A CG  1 
ATOM   639  C  CD1 . LEU A 1 95  ? 29.416  0.293   26.542  1.00 16.40 ? 83  LEU A CD1 1 
ATOM   640  C  CD2 . LEU A 1 95  ? 28.887  0.901   28.925  1.00 19.97 ? 83  LEU A CD2 1 
ATOM   641  N  N   . VAL A 1 96  ? 28.604  3.705   24.601  1.00 13.66 ? 84  VAL A N   1 
ATOM   642  C  CA  . VAL A 1 96  ? 27.423  4.402   24.031  1.00 13.64 ? 84  VAL A CA  1 
ATOM   643  C  C   . VAL A 1 96  ? 26.458  3.342   23.475  1.00 12.90 ? 84  VAL A C   1 
ATOM   644  O  O   . VAL A 1 96  ? 26.885  2.469   22.749  1.00 11.57 ? 84  VAL A O   1 
ATOM   645  C  CB  . VAL A 1 96  ? 27.827  5.402   22.938  1.00 12.55 ? 84  VAL A CB  1 
ATOM   646  C  CG1 . VAL A 1 96  ? 26.581  5.917   22.241  1.00 13.75 ? 84  VAL A CG1 1 
ATOM   647  C  CG2 . VAL A 1 96  ? 28.717  6.518   23.484  1.00 13.89 ? 84  VAL A CG2 1 
ATOM   648  N  N   . GLU A 1 97  ? 25.168  3.462   23.806  1.00 12.64 ? 85  GLU A N   1 
ATOM   649  C  CA  . GLU A 1 97  ? 24.065  2.745   23.147  1.00 13.20 ? 85  GLU A CA  1 
ATOM   650  C  C   . GLU A 1 97  ? 23.428  3.754   22.175  1.00 12.50 ? 85  GLU A C   1 
ATOM   651  O  O   . GLU A 1 97  ? 23.070  4.869   22.618  1.00 12.26 ? 85  GLU A O   1 
ATOM   652  C  CB  . GLU A 1 97  ? 23.080  2.253   24.211  1.00 14.09 ? 85  GLU A CB  1 
ATOM   653  C  CG  . GLU A 1 97  ? 22.075  1.210   23.738  1.00 15.10 ? 85  GLU A CG  1 
ATOM   654  C  CD  . GLU A 1 97  ? 21.056  0.802   24.810  1.00 16.75 ? 85  GLU A CD  1 
ATOM   655  O  OE1 . GLU A 1 97  ? 20.676  -0.395  24.856  1.00 17.49 ? 85  GLU A OE1 1 
ATOM   656  O  OE2 . GLU A 1 97  ? 20.698  1.660   25.650  1.00 18.62 ? 85  GLU A OE2 1 
ATOM   657  N  N   . TYR A 1 98  ? 23.210  3.373   20.934  1.00 11.52 ? 86  TYR A N   1 
ATOM   658  C  CA  . TYR A 1 98  ? 22.602  4.301   19.967  1.00 13.73 ? 86  TYR A CA  1 
ATOM   659  C  C   . TYR A 1 98  ? 21.492  3.605   19.187  1.00 13.16 ? 86  TYR A C   1 
ATOM   660  O  O   . TYR A 1 98  ? 21.483  2.378   19.014  1.00 11.97 ? 86  TYR A O   1 
ATOM   661  C  CB  . TYR A 1 98  ? 23.649  4.872   19.031  1.00 13.11 ? 86  TYR A CB  1 
ATOM   662  C  CG  . TYR A 1 98  ? 24.276  3.852   18.113  1.00 13.86 ? 86  TYR A CG  1 
ATOM   663  C  CD1 . TYR A 1 98  ? 23.665  3.481   16.933  1.00 13.53 ? 86  TYR A CD1 1 
ATOM   664  C  CD2 . TYR A 1 98  ? 25.493  3.286   18.399  1.00 13.53 ? 86  TYR A CD2 1 
ATOM   665  C  CE1 . TYR A 1 98  ? 24.232  2.580   16.065  1.00 13.53 ? 86  TYR A CE1 1 
ATOM   666  C  CE2 . TYR A 1 98  ? 26.093  2.379   17.537  1.00 13.03 ? 86  TYR A CE2 1 
ATOM   667  C  CZ  . TYR A 1 98  ? 25.457  2.022   16.356  1.00 13.97 ? 86  TYR A CZ  1 
ATOM   668  O  OH  . TYR A 1 98  ? 26.015  1.098   15.524  1.00 16.08 ? 86  TYR A OH  1 
ATOM   669  N  N   . TYR A 1 99  ? 20.570  4.455   18.758  1.00 13.46 ? 87  TYR A N   1 
ATOM   670  C  CA  . TYR A 1 99  ? 19.331  4.069   18.075  1.00 13.84 ? 87  TYR A CA  1 
ATOM   671  C  C   . TYR A 1 99  ? 19.108  5.003   16.893  1.00 14.18 ? 87  TYR A C   1 
ATOM   672  O  O   . TYR A 1 99  ? 19.169  6.227   17.093  1.00 15.08 ? 87  TYR A O   1 
ATOM   673  C  CB  . TYR A 1 99  ? 18.120  4.236   18.994  1.00 14.33 ? 87  TYR A CB  1 
ATOM   674  C  CG  . TYR A 1 99  ? 18.128  3.442   20.259  1.00 19.03 ? 87  TYR A CG  1 
ATOM   675  C  CD1 . TYR A 1 99  ? 18.928  3.836   21.329  1.00 20.18 ? 87  TYR A CD1 1 
ATOM   676  C  CD2 . TYR A 1 99  ? 17.343  2.327   20.390  1.00 19.27 ? 87  TYR A CD2 1 
ATOM   677  C  CE1 . TYR A 1 99  ? 18.917  3.116   22.510  1.00 22.18 ? 87  TYR A CE1 1 
ATOM   678  C  CE2 . TYR A 1 99  ? 17.315  1.615   21.577  1.00 22.54 ? 87  TYR A CE2 1 
ATOM   679  C  CZ  . TYR A 1 99  ? 18.118  2.004   22.625  1.00 21.44 ? 87  TYR A CZ  1 
ATOM   680  O  OH  . TYR A 1 99  ? 18.080  1.281   23.784  1.00 27.30 ? 87  TYR A OH  1 
ATOM   681  N  N   . ILE A 1 100 ? 18.829  4.447   15.712  1.00 13.50 ? 88  ILE A N   1 
ATOM   682  C  CA  . ILE A 1 100 ? 18.315  5.213   14.552  1.00 12.63 ? 88  ILE A CA  1 
ATOM   683  C  C   . ILE A 1 100 ? 16.898  4.665   14.349  1.00 12.23 ? 88  ILE A C   1 
ATOM   684  O  O   . ILE A 1 100 ? 16.751  3.534   13.850  1.00 13.93 ? 88  ILE A O   1 
ATOM   685  C  CB  . ILE A 1 100 ? 19.232  5.065   13.323  1.00 12.80 ? 88  ILE A CB  1 
ATOM   686  C  CG1 . ILE A 1 100 ? 20.664  5.551   13.598  1.00 14.20 ? 88  ILE A CG1 1 
ATOM   687  C  CG2 . ILE A 1 100 ? 18.642  5.786   12.113  1.00 15.10 ? 88  ILE A CG2 1 
ATOM   688  C  CD1 . ILE A 1 100 ? 21.642  5.130   12.529  1.00 14.18 ? 88  ILE A CD1 1 
ATOM   689  N  N   . VAL A 1 101 ? 15.919  5.364   14.941  1.00 11.49 ? 89  VAL A N   1 
ATOM   690  C  CA  . VAL A 1 101 ? 14.549  4.851   15.086  1.00 11.45 ? 89  VAL A CA  1 
ATOM   691  C  C   . VAL A 1 101 ? 13.783  5.119   13.795  1.00 11.88 ? 89  VAL A C   1 
ATOM   692  O  O   . VAL A 1 101 ? 13.529  6.298   13.529  1.00 12.92 ? 89  VAL A O   1 
ATOM   693  C  CB  . VAL A 1 101 ? 13.885  5.466   16.336  1.00 11.14 ? 89  VAL A CB  1 
ATOM   694  C  CG1 . VAL A 1 101 ? 12.466  4.935   16.496  1.00 13.11 ? 89  VAL A CG1 1 
ATOM   695  C  CG2 . VAL A 1 101 ? 14.685  5.132   17.564  1.00 11.88 ? 89  VAL A CG2 1 
ATOM   696  N  N   . GLU A 1 102 ? 13.366  4.058   13.116  1.00 12.91 ? 90  GLU A N   1 
ATOM   697  C  CA  . GLU A 1 102 ? 12.602  4.105   11.844  1.00 12.38 ? 90  GLU A CA  1 
ATOM   698  C  C   . GLU A 1 102 ? 11.110  4.233   12.144  1.00 12.84 ? 90  GLU A C   1 
ATOM   699  O  O   . GLU A 1 102 ? 10.415  4.931   11.381  1.00 13.07 ? 90  GLU A O   1 
ATOM   700  C  CB  . GLU A 1 102 ? 12.906  2.863   11.023  1.00 13.63 ? 90  GLU A CB  1 
ATOM   701  C  CG  . GLU A 1 102 ? 14.337  2.819   10.550  1.00 15.78 ? 90  GLU A CG  1 
ATOM   702  C  CD  . GLU A 1 102 ? 14.590  3.807   9.458   1.00 18.07 ? 90  GLU A CD  1 
ATOM   703  O  OE1 . GLU A 1 102 ? 15.046  4.880   9.795   1.00 18.48 ? 90  GLU A OE1 1 
ATOM   704  O  OE2 . GLU A 1 102 ? 14.257  3.508   8.286   1.00 19.60 ? 90  GLU A OE2 1 
ATOM   705  N  N   . SER A 1 103 ? 10.631  3.549   13.187  1.00 12.54 ? 91  SER A N   1 
ATOM   706  C  CA  . SER A 1 103 ? 9.228   3.623   13.667  1.00 13.61 ? 91  SER A CA  1 
ATOM   707  C  C   . SER A 1 103 ? 9.230   3.414   15.163  1.00 14.42 ? 91  SER A C   1 
ATOM   708  O  O   . SER A 1 103 ? 10.024  2.606   15.681  1.00 11.57 ? 91  SER A O   1 
ATOM   709  C  CB  . SER A 1 103 ? 8.317   2.583   13.090  1.00 16.59 ? 91  SER A CB  1 
ATOM   710  O  OG  . SER A 1 103 ? 8.080   2.746   11.728  1.00 18.65 ? 91  SER A OG  1 
ATOM   711  N  N   . PHE A 1 104 ? 8.323   4.090   15.844  1.00 13.68 ? 92  PHE A N   1 
ATOM   712  C  CA  . PHE A 1 104 ? 7.885   3.678   17.180  1.00 13.97 ? 92  PHE A CA  1 
ATOM   713  C  C   . PHE A 1 104 ? 6.373   3.728   17.197  1.00 16.73 ? 92  PHE A C   1 
ATOM   714  O  O   . PHE A 1 104 ? 5.769   4.348   16.303  1.00 17.13 ? 92  PHE A O   1 
ATOM   715  C  CB  . PHE A 1 104 ? 8.520   4.562   18.238  1.00 14.85 ? 92  PHE A CB  1 
ATOM   716  C  CG  . PHE A 1 104 ? 8.092   6.003   18.229  1.00 15.06 ? 92  PHE A CG  1 
ATOM   717  C  CD1 . PHE A 1 104 ? 6.852   6.352   18.751  1.00 17.32 ? 92  PHE A CD1 1 
ATOM   718  C  CD2 . PHE A 1 104 ? 8.929   7.009   17.777  1.00 15.31 ? 92  PHE A CD2 1 
ATOM   719  C  CE1 . PHE A 1 104 ? 6.497   7.687   18.816  1.00 16.20 ? 92  PHE A CE1 1 
ATOM   720  C  CE2 . PHE A 1 104 ? 8.553   8.343   17.806  1.00 16.00 ? 92  PHE A CE2 1 
ATOM   721  C  CZ  . PHE A 1 104 ? 7.319   8.672   18.331  1.00 16.99 ? 92  PHE A CZ  1 
ATOM   722  N  N   . SER A 1 105 ? 5.781   3.031   18.139  1.00 16.62 ? 93  SER A N   1 
ATOM   723  C  CA  . SER A 1 105 ? 4.317   2.805   18.142  1.00 17.54 ? 93  SER A CA  1 
ATOM   724  C  C   . SER A 1 105 ? 3.704   3.856   19.082  1.00 20.06 ? 93  SER A C   1 
ATOM   725  O  O   . SER A 1 105 ? 3.496   5.023   18.650  1.00 24.67 ? 93  SER A O   1 
ATOM   726  C  CB  . SER A 1 105 ? 4.054   1.406   18.542  1.00 18.18 ? 93  SER A CB  1 
ATOM   727  O  OG  . SER A 1 105 ? 4.770   1.099   19.731  1.00 19.57 ? 93  SER A OG  1 
ATOM   728  N  N   . THR A 1 106 ? 3.597   3.518   20.350  1.00 19.84 ? 94  THR A N   1 
ATOM   729  C  CA  . THR A 1 106 ? 2.770   4.242   21.353  1.00 17.76 ? 94  THR A CA  1 
ATOM   730  C  C   . THR A 1 106 ? 3.600   5.093   22.322  1.00 18.89 ? 94  THR A C   1 
ATOM   731  O  O   . THR A 1 106 ? 2.985   5.746   23.217  1.00 20.58 ? 94  THR A O   1 
ATOM   732  C  CB  . THR A 1 106 ? 1.901   3.237   22.114  1.00 17.14 ? 94  THR A CB  1 
ATOM   733  O  OG1 . THR A 1 106 ? 2.790   2.383   22.818  1.00 19.22 ? 94  THR A OG1 1 
ATOM   734  C  CG2 . THR A 1 106 ? 0.960   2.454   21.231  1.00 18.47 ? 94  THR A CG2 1 
ATOM   735  N  N   . TYR A 1 107 ? 4.925   5.145   22.191  1.00 17.03 ? 95  TYR A N   1 
ATOM   736  C  CA  . TYR A 1 107 ? 5.814   5.852   23.144  1.00 18.38 ? 95  TYR A CA  1 
ATOM   737  C  C   . TYR A 1 107 ? 7.038   6.366   22.388  1.00 17.65 ? 95  TYR A C   1 
ATOM   738  O  O   . TYR A 1 107 ? 7.719   5.549   21.728  1.00 18.00 ? 95  TYR A O   1 
ATOM   739  C  CB  . TYR A 1 107 ? 6.317   4.962   24.292  1.00 18.25 ? 95  TYR A CB  1 
ATOM   740  C  CG  . TYR A 1 107 ? 7.198   5.672   25.298  1.00 17.70 ? 95  TYR A CG  1 
ATOM   741  C  CD1 . TYR A 1 107 ? 6.642   6.555   26.212  1.00 19.04 ? 95  TYR A CD1 1 
ATOM   742  C  CD2 . TYR A 1 107 ? 8.570   5.445   25.379  1.00 17.92 ? 95  TYR A CD2 1 
ATOM   743  C  CE1 . TYR A 1 107 ? 7.410   7.170   27.183  1.00 20.43 ? 95  TYR A CE1 1 
ATOM   744  C  CE2 . TYR A 1 107 ? 9.364   6.100   26.304  1.00 20.04 ? 95  TYR A CE2 1 
ATOM   745  C  CZ  . TYR A 1 107 ? 8.777   6.952   27.229  1.00 20.97 ? 95  TYR A CZ  1 
ATOM   746  O  OH  . TYR A 1 107 ? 9.509   7.616   28.160  1.00 23.82 ? 95  TYR A OH  1 
ATOM   747  N  N   . ASP A 1 108 ? 7.301   7.649   22.483  1.00 17.20 ? 96  ASP A N   1 
ATOM   748  C  CA  . ASP A 1 108 ? 8.483   8.286   21.845  1.00 20.38 ? 96  ASP A CA  1 
ATOM   749  C  C   . ASP A 1 108 ? 9.678   8.188   22.794  1.00 23.42 ? 96  ASP A C   1 
ATOM   750  O  O   . ASP A 1 108 ? 9.753   8.958   23.754  1.00 22.96 ? 96  ASP A O   1 
ATOM   751  C  CB  . ASP A 1 108 ? 8.220   9.743   21.491  1.00 20.00 ? 96  ASP A CB  1 
ATOM   752  C  CG  . ASP A 1 108 ? 9.322   10.385  20.660  1.00 22.04 ? 96  ASP A CG  1 
ATOM   753  O  OD1 . ASP A 1 108 ? 10.445  9.825   20.651  1.00 24.35 ? 96  ASP A OD1 1 
ATOM   754  O  OD2 . ASP A 1 108 ? 9.037   11.434  20.064  1.00 23.66 ? 96  ASP A OD2 1 
ATOM   755  N  N   . PRO A 1 109 ? 10.700  7.360   22.445  1.00 31.07 ? 97  PRO A N   1 
ATOM   756  C  CA  . PRO A 1 109 ? 11.948  7.224   23.222  1.00 32.67 ? 97  PRO A CA  1 
ATOM   757  C  C   . PRO A 1 109 ? 12.733  8.477   23.641  1.00 39.19 ? 97  PRO A C   1 
ATOM   758  O  O   . PRO A 1 109 ? 13.504  8.370   24.582  1.00 42.04 ? 97  PRO A O   1 
ATOM   759  C  CB  . PRO A 1 109 ? 12.907  6.474   22.284  1.00 37.83 ? 97  PRO A CB  1 
ATOM   760  C  CG  . PRO A 1 109 ? 12.245  6.472   20.926  1.00 32.77 ? 97  PRO A CG  1 
ATOM   761  C  CD  . PRO A 1 109 ? 10.753  6.592   21.198  1.00 28.92 ? 97  PRO A CD  1 
ATOM   762  N  N   . SER A 1 110 ? 12.560  9.609   22.950  1.00 38.61 ? 98  SER A N   1 
ATOM   763  C  CA  . SER A 1 110 ? 13.269  10.893  23.197  1.00 36.57 ? 98  SER A CA  1 
ATOM   764  C  C   . SER A 1 110 ? 12.538  11.738  24.247  1.00 35.36 ? 98  SER A C   1 
ATOM   765  O  O   . SER A 1 110 ? 12.947  12.926  24.504  1.00 36.33 ? 98  SER A O   1 
ATOM   766  C  CB  . SER A 1 110 ? 13.408  11.650  21.902  1.00 33.41 ? 98  SER A CB  1 
ATOM   767  O  OG  . SER A 1 110 ? 12.130  11.910  21.338  1.00 35.45 ? 98  SER A OG  1 
ATOM   768  N  N   . THR A 1 111 ? 11.421  11.221  24.766  1.00 28.78 ? 99  THR A N   1 
ATOM   769  C  CA  . THR A 1 111 ? 10.651  11.890  25.814  1.00 27.35 ? 99  THR A CA  1 
ATOM   770  C  C   . THR A 1 111 ? 11.626  12.280  26.936  1.00 29.25 ? 99  THR A C   1 
ATOM   771  O  O   . THR A 1 111 ? 12.257  11.372  27.447  1.00 29.39 ? 99  THR A O   1 
ATOM   772  C  CB  . THR A 1 111 ? 9.528   10.956  26.273  1.00 28.61 ? 99  THR A CB  1 
ATOM   773  O  OG1 . THR A 1 111 ? 8.762   10.663  25.091  1.00 24.97 ? 99  THR A OG1 1 
ATOM   774  C  CG2 . THR A 1 111 ? 8.707   11.573  27.380  1.00 30.47 ? 99  THR A CG2 1 
ATOM   775  N  N   . GLY A 1 112 ? 11.706  13.562  27.285  1.00 33.82 ? 100 GLY A N   1 
ATOM   776  C  CA  . GLY A 1 112 ? 12.553  14.043  28.396  1.00 37.15 ? 100 GLY A CA  1 
ATOM   777  C  C   . GLY A 1 112 ? 13.997  14.169  27.939  1.00 39.74 ? 100 GLY A C   1 
ATOM   778  O  O   . GLY A 1 112 ? 14.930  13.694  28.664  1.00 38.86 ? 100 GLY A O   1 
ATOM   779  N  N   . ALA A 1 113 ? 14.180  14.759  26.753  1.00 37.39 ? 101 ALA A N   1 
ATOM   780  C  CA  . ALA A 1 113 ? 15.516  15.056  26.192  1.00 33.04 ? 101 ALA A CA  1 
ATOM   781  C  C   . ALA A 1 113 ? 15.490  16.341  25.364  1.00 36.77 ? 101 ALA A C   1 
ATOM   782  O  O   . ALA A 1 113 ? 14.579  16.532  24.536  1.00 33.05 ? 101 ALA A O   1 
ATOM   783  C  CB  . ALA A 1 113 ? 16.004  13.924  25.370  1.00 32.21 ? 101 ALA A CB  1 
ATOM   784  N  N   . GLN A 1 114 ? 16.512  17.165  25.573  1.00 33.43 ? 102 GLN A N   1 
ATOM   785  C  CA  . GLN A 1 114 ? 16.901  18.267  24.660  1.00 39.75 ? 102 GLN A CA  1 
ATOM   786  C  C   . GLN A 1 114 ? 17.098  17.678  23.257  1.00 36.58 ? 102 GLN A C   1 
ATOM   787  O  O   . GLN A 1 114 ? 17.976  16.813  23.078  1.00 39.70 ? 102 GLN A O   1 
ATOM   788  C  CB  . GLN A 1 114 ? 18.181  18.921  25.196  1.00 39.70 ? 102 GLN A CB  1 
ATOM   789  C  CG  . GLN A 1 114 ? 18.578  20.229  24.528  1.00 43.24 ? 102 GLN A CG  1 
ATOM   790  C  CD  . GLN A 1 114 ? 19.951  20.681  24.974  1.00 44.53 ? 102 GLN A CD  1 
ATOM   791  O  OE1 . GLN A 1 114 ? 20.658  19.990  25.710  1.00 48.66 ? 102 GLN A OE1 1 
ATOM   792  N  NE2 . GLN A 1 114 ? 20.347  21.858  24.515  1.00 48.60 ? 102 GLN A NE2 1 
ATOM   793  N  N   . GLU A 1 115 ? 16.308  18.151  22.299  1.00 40.50 ? 103 GLU A N   1 
ATOM   794  C  CA  . GLU A 1 115 ? 16.614  18.027  20.857  1.00 36.36 ? 103 GLU A CA  1 
ATOM   795  C  C   . GLU A 1 115 ? 17.891  18.831  20.599  1.00 34.49 ? 103 GLU A C   1 
ATOM   796  O  O   . GLU A 1 115 ? 17.956  20.008  21.044  1.00 35.22 ? 103 GLU A O   1 
ATOM   797  C  CB  . GLU A 1 115 ? 15.402  18.480  20.042  1.00 37.90 ? 103 GLU A CB  1 
ATOM   798  C  CG  . GLU A 1 115 ? 15.686  18.613  18.565  1.00 40.45 ? 103 GLU A CG  1 
ATOM   799  C  CD  . GLU A 1 115 ? 14.453  18.720  17.682  1.00 41.83 ? 103 GLU A CD  1 
ATOM   800  O  OE1 . GLU A 1 115 ? 14.649  18.879  16.471  1.00 40.97 ? 103 GLU A OE1 1 
ATOM   801  O  OE2 . GLU A 1 115 ? 13.303  18.612  18.211  1.00 38.71 ? 103 GLU A OE2 1 
ATOM   802  N  N   . LEU A 1 116 ? 18.880  18.210  19.953  1.00 28.04 ? 104 LEU A N   1 
ATOM   803  C  CA  . LEU A 1 116 ? 20.224  18.773  19.685  1.00 30.05 ? 104 LEU A CA  1 
ATOM   804  C  C   . LEU A 1 116 ? 20.348  19.173  18.221  1.00 30.81 ? 104 LEU A C   1 
ATOM   805  O  O   . LEU A 1 116 ? 21.409  19.719  17.852  1.00 33.18 ? 104 LEU A O   1 
ATOM   806  C  CB  . LEU A 1 116 ? 21.277  17.722  20.037  1.00 28.22 ? 104 LEU A CB  1 
ATOM   807  C  CG  . LEU A 1 116 ? 21.378  17.361  21.510  1.00 30.43 ? 104 LEU A CG  1 
ATOM   808  C  CD1 . LEU A 1 116 ? 22.493  16.359  21.735  1.00 31.46 ? 104 LEU A CD1 1 
ATOM   809  C  CD2 . LEU A 1 116 ? 21.604  18.597  22.375  1.00 30.55 ? 104 LEU A CD2 1 
ATOM   810  N  N   . GLY A 1 117 ? 19.321  18.886  17.417  1.00 30.37 ? 105 GLY A N   1 
ATOM   811  C  CA  . GLY A 1 117 ? 19.339  19.162  15.970  1.00 30.65 ? 105 GLY A CA  1 
ATOM   812  C  C   . GLY A 1 117 ? 18.517  18.159  15.176  1.00 29.05 ? 105 GLY A C   1 
ATOM   813  O  O   . GLY A 1 117 ? 17.746  17.353  15.772  1.00 27.02 ? 105 GLY A O   1 
ATOM   814  N  N   . THR A 1 118 ? 18.661  18.231  13.866  1.00 26.30 ? 106 THR A N   1 
ATOM   815  C  CA  . THR A 1 118 ? 18.034  17.294  12.902  1.00 26.05 ? 106 THR A CA  1 
ATOM   816  C  C   . THR A 1 118 ? 19.074  16.912  11.871  1.00 25.39 ? 106 THR A C   1 
ATOM   817  O  O   . THR A 1 118 ? 20.067  17.651  11.711  1.00 26.73 ? 106 THR A O   1 
ATOM   818  C  CB  . THR A 1 118 ? 16.816  17.857  12.157  1.00 28.36 ? 106 THR A CB  1 
ATOM   819  O  OG1 . THR A 1 118 ? 17.259  18.976  11.386  1.00 31.35 ? 106 THR A OG1 1 
ATOM   820  C  CG2 . THR A 1 118 ? 15.663  18.199  13.073  1.00 32.17 ? 106 THR A CG2 1 
ATOM   821  N  N   . VAL A 1 119 ? 18.866  15.763  11.235  1.00 22.51 ? 107 VAL A N   1 
ATOM   822  C  CA  . VAL A 1 119 ? 19.676  15.287  10.089  1.00 20.55 ? 107 VAL A CA  1 
ATOM   823  C  C   . VAL A 1 119 ? 18.683  14.807  9.015   1.00 21.78 ? 107 VAL A C   1 
ATOM   824  O  O   . VAL A 1 119 ? 17.655  14.171  9.372   1.00 20.63 ? 107 VAL A O   1 
ATOM   825  C  CB  . VAL A 1 119 ? 20.684  14.222  10.530  1.00 21.29 ? 107 VAL A CB  1 
ATOM   826  C  CG1 . VAL A 1 119 ? 20.029  12.996  11.156  1.00 23.28 ? 107 VAL A CG1 1 
ATOM   827  C  CG2 . VAL A 1 119 ? 21.642  13.868  9.389   1.00 22.00 ? 107 VAL A CG2 1 
ATOM   828  N  N   . GLU A 1 120 ? 18.940  15.184  7.767   1.00 20.26 ? 108 GLU A N   1 
ATOM   829  C  CA  . GLU A 1 120 ? 18.128  14.789  6.598   1.00 23.17 ? 108 GLU A CA  1 
ATOM   830  C  C   . GLU A 1 120 ? 18.910  13.717  5.872   1.00 22.30 ? 108 GLU A C   1 
ATOM   831  O  O   . GLU A 1 120 ? 20.081  13.974  5.507   1.00 22.54 ? 108 GLU A O   1 
ATOM   832  C  CB  . GLU A 1 120 ? 17.857  15.987  5.692   1.00 28.22 ? 108 GLU A CB  1 
ATOM   833  C  CG  . GLU A 1 120 ? 16.851  16.945  6.272   1.00 31.84 ? 108 GLU A CG  1 
ATOM   834  C  CD  . GLU A 1 120 ? 16.334  17.916  5.229   1.00 39.76 ? 108 GLU A CD  1 
ATOM   835  O  OE1 . GLU A 1 120 ? 15.639  17.467  4.286   1.00 50.30 ? 108 GLU A OE1 1 
ATOM   836  O  OE2 . GLU A 1 120 ? 16.657  19.100  5.343   1.00 43.46 ? 108 GLU A OE2 1 
ATOM   837  N  N   . THR A 1 121 ? 18.331  12.531  5.727   1.00 21.17 ? 109 THR A N   1 
ATOM   838  C  CA  . THR A 1 121 ? 19.007  11.363  5.108   1.00 21.40 ? 109 THR A CA  1 
ATOM   839  C  C   . THR A 1 121 ? 17.941  10.328  4.785   1.00 19.89 ? 109 THR A C   1 
ATOM   840  O  O   . THR A 1 121 ? 16.923  10.312  5.518   1.00 18.75 ? 109 THR A O   1 
ATOM   841  C  CB  . THR A 1 121 ? 20.101  10.780  6.012   1.00 22.34 ? 109 THR A CB  1 
ATOM   842  O  OG1 . THR A 1 121 ? 20.776  9.767   5.289   1.00 25.57 ? 109 THR A OG1 1 
ATOM   843  C  CG2 . THR A 1 121 ? 19.586  10.182  7.299   1.00 23.86 ? 109 THR A CG2 1 
ATOM   844  N  N   . ASP A 1 122 ? 18.127  9.604   3.683   1.00 20.32 ? 110 ASP A N   1 
ATOM   845  C  CA  . ASP A 1 122 ? 17.296  8.441   3.254   1.00 20.52 ? 110 ASP A CA  1 
ATOM   846  C  C   . ASP A 1 122 ? 15.836  8.901   3.157   1.00 19.72 ? 110 ASP A C   1 
ATOM   847  O  O   . ASP A 1 122 ? 14.924  8.238   3.709   1.00 18.22 ? 110 ASP A O   1 
ATOM   848  C  CB  . ASP A 1 122 ? 17.592  7.233   4.144   1.00 18.36 ? 110 ASP A CB  1 
ATOM   849  C  CG  . ASP A 1 122 ? 19.092  6.974   4.300   1.00 19.24 ? 110 ASP A CG  1 
ATOM   850  O  OD1 . ASP A 1 122 ? 19.737  6.577   3.302   1.00 20.22 ? 110 ASP A OD1 1 
ATOM   851  O  OD2 . ASP A 1 122 ? 19.610  7.175   5.436   1.00 20.20 ? 110 ASP A OD2 1 
ATOM   852  N  N   . ASP A 1 123 ? 15.640  10.057  2.522   1.00 20.99 ? 111 ASP A N   1 
ATOM   853  C  CA  . ASP A 1 123 ? 14.315  10.635  2.179   1.00 24.81 ? 111 ASP A CA  1 
ATOM   854  C  C   . ASP A 1 123 ? 13.496  10.900  3.449   1.00 23.78 ? 111 ASP A C   1 
ATOM   855  O  O   . ASP A 1 123 ? 12.267  10.972  3.377   1.00 23.06 ? 111 ASP A O   1 
ATOM   856  C  CB  . ASP A 1 123 ? 13.621  9.744   1.150   1.00 28.90 ? 111 ASP A CB  1 
ATOM   857  C  CG  . ASP A 1 123 ? 14.351  9.797   -0.178  1.00 35.33 ? 111 ASP A CG  1 
ATOM   858  O  OD1 . ASP A 1 123 ? 14.398  10.898  -0.755  1.00 43.20 ? 111 ASP A OD1 1 
ATOM   859  O  OD2 . ASP A 1 123 ? 14.919  8.756   -0.597  1.00 39.91 ? 111 ASP A OD2 1 
ATOM   860  N  N   . GLY A 1 124 ? 14.159  11.158  4.573   1.00 21.05 ? 112 GLY A N   1 
ATOM   861  C  CA  . GLY A 1 124 ? 13.469  11.519  5.821   1.00 20.00 ? 112 GLY A CA  1 
ATOM   862  C  C   . GLY A 1 124 ? 14.229  12.575  6.588   1.00 19.03 ? 112 GLY A C   1 
ATOM   863  O  O   . GLY A 1 124 ? 15.332  12.987  6.120   1.00 22.10 ? 112 GLY A O   1 
ATOM   864  N  N   . THR A 1 125 ? 13.622  13.022  7.668   1.00 19.12 ? 113 THR A N   1 
ATOM   865  C  CA  . THR A 1 125 ? 14.204  13.946  8.668   1.00 18.70 ? 113 THR A CA  1 
ATOM   866  C  C   . THR A 1 125 ? 14.238  13.206  9.995   1.00 17.79 ? 113 THR A C   1 
ATOM   867  O  O   . THR A 1 125 ? 13.217  12.559  10.309  1.00 17.29 ? 113 THR A O   1 
ATOM   868  C  CB  . THR A 1 125 ? 13.351  15.202  8.783   1.00 21.40 ? 113 THR A CB  1 
ATOM   869  O  OG1 . THR A 1 125 ? 13.473  15.779  7.486   1.00 22.76 ? 113 THR A OG1 1 
ATOM   870  C  CG2 . THR A 1 125 ? 13.798  16.152  9.869   1.00 23.64 ? 113 THR A CG2 1 
ATOM   871  N  N   . TYR A 1 126 ? 15.355  13.300  10.721  1.00 15.89 ? 114 TYR A N   1 
ATOM   872  C  CA  . TYR A 1 126 ? 15.523  12.654  12.040  1.00 17.01 ? 114 TYR A CA  1 
ATOM   873  C  C   . TYR A 1 126 ? 15.849  13.753  13.058  1.00 17.05 ? 114 TYR A C   1 
ATOM   874  O  O   . TYR A 1 126 ? 16.716  14.541  12.787  1.00 19.00 ? 114 TYR A O   1 
ATOM   875  C  CB  . TYR A 1 126 ? 16.623  11.589  11.979  1.00 16.42 ? 114 TYR A CB  1 
ATOM   876  C  CG  . TYR A 1 126 ? 16.370  10.412  11.081  1.00 14.91 ? 114 TYR A CG  1 
ATOM   877  C  CD1 . TYR A 1 126 ? 16.466  10.518  9.699   1.00 14.48 ? 114 TYR A CD1 1 
ATOM   878  C  CD2 . TYR A 1 126 ? 16.044  9.170   11.600  1.00 14.10 ? 114 TYR A CD2 1 
ATOM   879  C  CE1 . TYR A 1 126 ? 16.230  9.437   8.862   1.00 14.05 ? 114 TYR A CE1 1 
ATOM   880  C  CE2 . TYR A 1 126 ? 15.796  8.082   10.769  1.00 14.05 ? 114 TYR A CE2 1 
ATOM   881  C  CZ  . TYR A 1 126 ? 15.892  8.199   9.396   1.00 12.79 ? 114 TYR A CZ  1 
ATOM   882  O  OH  . TYR A 1 126 ? 15.717  7.095   8.581   1.00 14.82 ? 114 TYR A OH  1 
ATOM   883  N  N   . LYS A 1 127 ? 15.148  13.752  14.188  1.00 18.27 ? 115 LYS A N   1 
ATOM   884  C  CA  . LYS A 1 127 ? 15.428  14.582  15.366  1.00 20.99 ? 115 LYS A CA  1 
ATOM   885  C  C   . LYS A 1 127 ? 16.515  13.855  16.165  1.00 19.41 ? 115 LYS A C   1 
ATOM   886  O  O   . LYS A 1 127 ? 16.409  12.609  16.328  1.00 17.84 ? 115 LYS A O   1 
ATOM   887  C  CB  . LYS A 1 127 ? 14.099  14.752  16.104  1.00 23.41 ? 115 LYS A CB  1 
ATOM   888  C  CG  . LYS A 1 127 ? 13.052  15.504  15.281  1.00 26.22 ? 115 LYS A CG  1 
ATOM   889  C  CD  . LYS A 1 127 ? 11.874  15.961  16.118  1.00 29.12 ? 115 LYS A CD  1 
ATOM   890  C  CE  . LYS A 1 127 ? 10.853  16.716  15.286  1.00 31.39 ? 115 LYS A CE  1 
ATOM   891  N  NZ  . LYS A 1 127 ? 9.628   17.003  16.072  1.00 37.50 ? 115 LYS A NZ  1 
ATOM   892  N  N   . ILE A 1 128 ? 17.531  14.594  16.606  1.00 18.12 ? 116 ILE A N   1 
ATOM   893  C  CA  . ILE A 1 128 ? 18.711  14.058  17.345  1.00 18.62 ? 116 ILE A CA  1 
ATOM   894  C  C   . ILE A 1 128 ? 18.552  14.362  18.826  1.00 16.76 ? 116 ILE A C   1 
ATOM   895  O  O   . ILE A 1 128 ? 18.209  15.488  19.142  1.00 19.70 ? 116 ILE A O   1 
ATOM   896  C  CB  . ILE A 1 128 ? 19.998  14.675  16.775  1.00 18.40 ? 116 ILE A CB  1 
ATOM   897  C  CG1 . ILE A 1 128 ? 20.198  14.244  15.323  1.00 19.05 ? 116 ILE A CG1 1 
ATOM   898  C  CG2 . ILE A 1 128 ? 21.201  14.325  17.612  1.00 17.74 ? 116 ILE A CG2 1 
ATOM   899  C  CD1 . ILE A 1 128 ? 21.252  15.053  14.593  1.00 20.65 ? 116 ILE A CD1 1 
ATOM   900  N  N   . TYR A 1 129 ? 18.808  13.379  19.706  1.00 16.14 ? 117 TYR A N   1 
ATOM   901  C  CA  . TYR A 1 129 ? 18.710  13.555  21.172  1.00 15.69 ? 117 TYR A CA  1 
ATOM   902  C  C   . TYR A 1 129 ? 19.833  12.794  21.876  1.00 16.63 ? 117 TYR A C   1 
ATOM   903  O  O   . TYR A 1 129 ? 20.369  11.850  21.308  1.00 15.15 ? 117 TYR A O   1 
ATOM   904  C  CB  . TYR A 1 129 ? 17.410  12.967  21.711  1.00 17.14 ? 117 TYR A CB  1 
ATOM   905  C  CG  . TYR A 1 129 ? 16.171  13.483  21.027  1.00 19.46 ? 117 TYR A CG  1 
ATOM   906  C  CD1 . TYR A 1 129 ? 15.689  12.904  19.870  1.00 19.28 ? 117 TYR A CD1 1 
ATOM   907  C  CD2 . TYR A 1 129 ? 15.426  14.504  21.606  1.00 23.37 ? 117 TYR A CD2 1 
ATOM   908  C  CE1 . TYR A 1 129 ? 14.535  13.363  19.257  1.00 21.12 ? 117 TYR A CE1 1 
ATOM   909  C  CE2 . TYR A 1 129 ? 14.268  14.982  20.999  1.00 25.39 ? 117 TYR A CE2 1 
ATOM   910  C  CZ  . TYR A 1 129 ? 13.800  14.381  19.843  1.00 25.62 ? 117 TYR A CZ  1 
ATOM   911  O  OH  . TYR A 1 129 ? 12.663  14.844  19.222  1.00 25.64 ? 117 TYR A OH  1 
ATOM   912  N  N   . GLN A 1 130 ? 20.186  13.204  23.088  1.00 16.23 ? 118 GLN A N   1 
ATOM   913  C  CA  . GLN A 1 130 ? 21.115  12.447  23.957  1.00 17.60 ? 118 GLN A CA  1 
ATOM   914  C  C   . GLN A 1 130 ? 20.453  12.263  25.318  1.00 20.79 ? 118 GLN A C   1 
ATOM   915  O  O   . GLN A 1 130 ? 19.868  13.232  25.842  1.00 19.09 ? 118 GLN A O   1 
ATOM   916  C  CB  . GLN A 1 130 ? 22.487  13.110  24.135  1.00 20.79 ? 118 GLN A CB  1 
ATOM   917  C  CG  . GLN A 1 130 ? 23.352  12.284  25.072  1.00 23.97 ? 118 GLN A CG  1 
ATOM   918  C  CD  . GLN A 1 130 ? 24.647  12.922  25.510  1.00 29.82 ? 118 GLN A CD  1 
ATOM   919  O  OE1 . GLN A 1 130 ? 25.584  12.216  25.849  1.00 35.07 ? 118 GLN A OE1 1 
ATOM   920  N  NE2 . GLN A 1 130 ? 24.695  14.250  25.541  1.00 33.80 ? 118 GLN A NE2 1 
ATOM   921  N  N   . THR A 1 131 ? 20.503  11.034  25.823  1.00 23.57 ? 119 THR A N   1 
ATOM   922  C  CA  . THR A 1 131 ? 20.028  10.638  27.175  1.00 28.45 ? 119 THR A CA  1 
ATOM   923  C  C   . THR A 1 131 ? 21.211  9.974   27.897  1.00 28.16 ? 119 THR A C   1 
ATOM   924  O  O   . THR A 1 131 ? 22.268  9.737   27.255  1.00 25.62 ? 119 THR A O   1 
ATOM   925  C  CB  . THR A 1 131 ? 18.744  9.793   27.112  1.00 31.03 ? 119 THR A CB  1 
ATOM   926  O  OG1 . THR A 1 131 ? 18.968  8.598   26.374  1.00 34.12 ? 119 THR A OG1 1 
ATOM   927  C  CG2 . THR A 1 131 ? 17.571  10.484  26.448  1.00 34.72 ? 119 THR A CG2 1 
ATOM   928  N  N   . THR A 1 132 ? 21.086  9.799   29.208  1.00 31.96 ? 120 THR A N   1 
ATOM   929  C  CA  . THR A 1 132 ? 22.002  9.006   30.064  1.00 33.33 ? 120 THR A CA  1 
ATOM   930  C  C   . THR A 1 132 ? 21.214  7.848   30.680  1.00 30.05 ? 120 THR A C   1 
ATOM   931  O  O   . THR A 1 132 ? 20.043  8.053   31.031  1.00 31.39 ? 120 THR A O   1 
ATOM   932  C  CB  . THR A 1 132 ? 22.644  9.886   31.144  1.00 35.93 ? 120 THR A CB  1 
ATOM   933  O  OG1 . THR A 1 132 ? 23.618  10.705  30.497  1.00 43.76 ? 120 THR A OG1 1 
ATOM   934  C  CG2 . THR A 1 132 ? 23.322  9.086   32.231  1.00 39.38 ? 120 THR A CG2 1 
ATOM   935  N  N   . ARG A 1 133 ? 21.845  6.689   30.837  1.00 25.12 ? 121 ARG A N   1 
ATOM   936  C  CA  . ARG A 1 133 ? 21.320  5.554   31.626  1.00 26.74 ? 121 ARG A CA  1 
ATOM   937  C  C   . ARG A 1 133 ? 22.297  5.305   32.776  1.00 26.65 ? 121 ARG A C   1 
ATOM   938  O  O   . ARG A 1 133 ? 23.534  5.291   32.515  1.00 25.08 ? 121 ARG A O   1 
ATOM   939  C  CB  . ARG A 1 133 ? 21.172  4.285   30.782  1.00 29.54 ? 121 ARG A CB  1 
ATOM   940  C  CG  . ARG A 1 133 ? 20.409  4.483   29.478  1.00 32.69 ? 121 ARG A CG  1 
ATOM   941  C  CD  . ARG A 1 133 ? 18.902  4.388   29.615  1.00 38.66 ? 121 ARG A CD  1 
ATOM   942  N  NE  . ARG A 1 133 ? 18.494  3.037   29.964  1.00 38.72 ? 121 ARG A NE  1 
ATOM   943  C  CZ  . ARG A 1 133 ? 18.068  2.663   31.163  1.00 42.36 ? 121 ARG A CZ  1 
ATOM   944  N  NH1 . ARG A 1 133 ? 17.994  3.542   32.147  1.00 43.74 ? 121 ARG A NH1 1 
ATOM   945  N  NH2 . ARG A 1 133 ? 17.735  1.402   31.378  1.00 41.63 ? 121 ARG A NH2 1 
ATOM   946  N  N   . GLU A 1 134 ? 21.763  5.115   33.980  1.00 30.03 ? 122 GLU A N   1 
ATOM   947  C  CA  . GLU A 1 134 ? 22.559  4.925   35.226  1.00 33.55 ? 122 GLU A CA  1 
ATOM   948  C  C   . GLU A 1 134 ? 22.352  3.489   35.719  1.00 34.51 ? 122 GLU A C   1 
ATOM   949  O  O   . GLU A 1 134 ? 21.183  3.077   35.829  1.00 28.83 ? 122 GLU A O   1 
ATOM   950  C  CB  . GLU A 1 134 ? 22.120  5.921   36.305  1.00 40.28 ? 122 GLU A CB  1 
ATOM   951  C  CG  . GLU A 1 134 ? 22.501  7.366   36.028  1.00 46.13 ? 122 GLU A CG  1 
ATOM   952  C  CD  . GLU A 1 134 ? 22.262  8.325   37.190  1.00 53.41 ? 122 GLU A CD  1 
ATOM   953  O  OE1 . GLU A 1 134 ? 22.725  8.018   38.315  1.00 54.80 ? 122 GLU A OE1 1 
ATOM   954  O  OE2 . GLU A 1 134 ? 21.614  9.381   36.975  1.00 55.85 ? 122 GLU A OE2 1 
ATOM   955  N  N   . ASN A 1 135 ? 23.441  2.763   35.989  1.00 31.96 ? 123 ASN A N   1 
ATOM   956  C  CA  . ASN A 1 135 ? 23.399  1.420   36.624  1.00 35.52 ? 123 ASN A CA  1 
ATOM   957  C  C   . ASN A 1 135 ? 22.436  0.540   35.811  1.00 32.00 ? 123 ASN A C   1 
ATOM   958  O  O   . ASN A 1 135 ? 21.483  -0.029  36.369  1.00 28.84 ? 123 ASN A O   1 
ATOM   959  C  CB  . ASN A 1 135 ? 23.045  1.562   38.110  1.00 40.42 ? 123 ASN A CB  1 
ATOM   960  C  CG  . ASN A 1 135 ? 23.974  2.504   38.854  1.00 39.62 ? 123 ASN A CG  1 
ATOM   961  O  OD1 . ASN A 1 135 ? 23.529  3.456   39.485  1.00 46.62 ? 123 ASN A OD1 1 
ATOM   962  N  ND2 . ASN A 1 135 ? 25.266  2.242   38.807  1.00 34.81 ? 123 ASN A ND2 1 
ATOM   963  N  N   . ALA A 1 136 ? 22.662  0.484   34.505  1.00 26.89 ? 124 ALA A N   1 
ATOM   964  C  CA  . ALA A 1 136 ? 21.756  -0.140  33.516  1.00 27.87 ? 124 ALA A CA  1 
ATOM   965  C  C   . ALA A 1 136 ? 22.491  -1.310  32.880  1.00 27.26 ? 124 ALA A C   1 
ATOM   966  O  O   . ALA A 1 136 ? 23.715  -1.244  32.779  1.00 23.70 ? 124 ALA A O   1 
ATOM   967  C  CB  . ALA A 1 136 ? 21.377  0.894   32.496  1.00 28.15 ? 124 ALA A CB  1 
ATOM   968  N  N   . PRO A 1 137 ? 21.787  -2.376  32.429  1.00 23.58 ? 125 PRO A N   1 
ATOM   969  C  CA  . PRO A 1 137 ? 22.384  -3.413  31.596  1.00 25.61 ? 125 PRO A CA  1 
ATOM   970  C  C   . PRO A 1 137 ? 23.081  -2.818  30.367  1.00 23.89 ? 125 PRO A C   1 
ATOM   971  O  O   . PRO A 1 137 ? 22.563  -1.870  29.746  1.00 22.48 ? 125 PRO A O   1 
ATOM   972  C  CB  . PRO A 1 137 ? 21.238  -4.328  31.151  1.00 26.22 ? 125 PRO A CB  1 
ATOM   973  C  CG  . PRO A 1 137 ? 20.068  -3.970  32.035  1.00 27.57 ? 125 PRO A CG  1 
ATOM   974  C  CD  . PRO A 1 137 ? 20.388  -2.694  32.785  1.00 28.36 ? 125 PRO A CD  1 
ATOM   975  N  N   . SER A 1 138 ? 24.263  -3.344  30.082  1.00 23.16 ? 126 SER A N   1 
ATOM   976  C  CA  . SER A 1 138 ? 25.070  -2.978  28.897  1.00 22.73 ? 126 SER A CA  1 
ATOM   977  C  C   . SER A 1 138 ? 25.819  -4.201  28.381  1.00 22.12 ? 126 SER A C   1 
ATOM   978  O  O   . SER A 1 138 ? 25.878  -5.225  29.080  1.00 23.12 ? 126 SER A O   1 
ATOM   979  C  CB  . SER A 1 138 ? 26.032  -1.866  29.211  1.00 23.97 ? 126 SER A CB  1 
ATOM   980  O  OG  . SER A 1 138 ? 27.187  -2.384  29.835  1.00 21.47 ? 126 SER A OG  1 
ATOM   981  N  N   . ILE A 1 139 ? 26.497  -4.031  27.253  1.00 21.08 ? 127 ILE A N   1 
ATOM   982  C  CA  . ILE A 1 139 ? 27.388  -5.065  26.665  1.00 22.91 ? 127 ILE A CA  1 
ATOM   983  C  C   . ILE A 1 139 ? 28.584  -5.274  27.599  1.00 24.56 ? 127 ILE A C   1 
ATOM   984  O  O   . ILE A 1 139 ? 29.291  -6.271  27.382  1.00 26.67 ? 127 ILE A O   1 
ATOM   985  C  CB  . ILE A 1 139 ? 27.850  -4.704  25.245  1.00 21.88 ? 127 ILE A CB  1 
ATOM   986  C  CG1 . ILE A 1 139 ? 28.550  -3.342  25.192  1.00 21.00 ? 127 ILE A CG1 1 
ATOM   987  C  CG2 . ILE A 1 139 ? 26.694  -4.792  24.275  1.00 23.28 ? 127 ILE A CG2 1 
ATOM   988  C  CD1 . ILE A 1 139 ? 29.399  -3.141  23.964  1.00 23.86 ? 127 ILE A CD1 1 
ATOM   989  N  N   . GLU A 1 140 ? 28.802  -4.378  28.562  1.00 23.98 ? 128 GLU A N   1 
ATOM   990  C  CA  . GLU A 1 140 ? 29.930  -4.486  29.541  1.00 25.83 ? 128 GLU A CA  1 
ATOM   991  C  C   . GLU A 1 140 ? 29.442  -4.878  30.938  1.00 26.08 ? 128 GLU A C   1 
ATOM   992  O  O   . GLU A 1 140 ? 30.314  -4.899  31.861  1.00 27.13 ? 128 GLU A O   1 
ATOM   993  C  CB  . GLU A 1 140 ? 30.698  -3.168  29.611  1.00 31.35 ? 128 GLU A CB  1 
ATOM   994  C  CG  . GLU A 1 140 ? 31.508  -2.923  28.351  1.00 35.63 ? 128 GLU A CG  1 
ATOM   995  C  CD  . GLU A 1 140 ? 32.494  -1.770  28.401  1.00 47.34 ? 128 GLU A CD  1 
ATOM   996  O  OE1 . GLU A 1 140 ? 33.286  -1.662  27.444  1.00 48.47 ? 128 GLU A OE1 1 
ATOM   997  O  OE2 . GLU A 1 140 ? 32.489  -0.993  29.398  1.00 53.22 ? 128 GLU A OE2 1 
ATOM   998  N  N   . GLY A 1 141 ? 28.148  -5.181  31.103  1.00 23.40 ? 129 GLY A N   1 
ATOM   999  C  CA  . GLY A 1 141 ? 27.528  -5.384  32.431  1.00 24.96 ? 129 GLY A CA  1 
ATOM   1000 C  C   . GLY A 1 141 ? 26.842  -4.134  32.968  1.00 22.92 ? 129 GLY A C   1 
ATOM   1001 O  O   . GLY A 1 141 ? 26.683  -3.141  32.205  1.00 22.50 ? 129 GLY A O   1 
ATOM   1002 N  N   . THR A 1 142 ? 26.451  -4.121  34.244  1.00 20.81 ? 130 THR A N   1 
ATOM   1003 C  CA  . THR A 1 142 ? 25.805  -2.934  34.859  1.00 23.42 ? 130 THR A CA  1 
ATOM   1004 C  C   . THR A 1 142 ? 26.692  -1.698  34.679  1.00 24.02 ? 130 THR A C   1 
ATOM   1005 O  O   . THR A 1 142 ? 27.854  -1.747  35.071  1.00 20.60 ? 130 THR A O   1 
ATOM   1006 C  CB  . THR A 1 142 ? 25.470  -3.165  36.333  1.00 26.13 ? 130 THR A CB  1 
ATOM   1007 O  OG1 . THR A 1 142 ? 24.721  -4.377  36.332  1.00 28.51 ? 130 THR A OG1 1 
ATOM   1008 C  CG2 . THR A 1 142 ? 24.689  -2.038  36.970  1.00 27.22 ? 130 THR A CG2 1 
ATOM   1009 N  N   . ALA A 1 143 ? 26.179  -0.625  34.086  1.00 21.64 ? 131 ALA A N   1 
ATOM   1010 C  CA  . ALA A 1 143 ? 27.018  0.538   33.729  1.00 20.81 ? 131 ALA A CA  1 
ATOM   1011 C  C   . ALA A 1 143 ? 26.205  1.815   33.592  1.00 24.43 ? 131 ALA A C   1 
ATOM   1012 O  O   . ALA A 1 143 ? 24.957  1.735   33.428  1.00 24.21 ? 131 ALA A O   1 
ATOM   1013 C  CB  . ALA A 1 143 ? 27.781  0.226   32.480  1.00 20.08 ? 131 ALA A CB  1 
ATOM   1014 N  N   . THR A 1 144 ? 26.937  2.936   33.614  1.00 22.30 ? 132 THR A N   1 
ATOM   1015 C  CA  . THR A 1 144 ? 26.475  4.302   33.282  1.00 22.77 ? 132 THR A CA  1 
ATOM   1016 C  C   . THR A 1 144 ? 26.995  4.677   31.889  1.00 24.06 ? 132 THR A C   1 
ATOM   1017 O  O   . THR A 1 144 ? 28.179  4.497   31.571  1.00 24.76 ? 132 THR A O   1 
ATOM   1018 C  CB  . THR A 1 144 ? 26.856  5.294   34.383  1.00 24.20 ? 132 THR A CB  1 
ATOM   1019 O  OG1 . THR A 1 144 ? 26.144  4.814   35.523  1.00 26.51 ? 132 THR A OG1 1 
ATOM   1020 C  CG2 . THR A 1 144 ? 26.483  6.716   34.029  1.00 28.22 ? 132 THR A CG2 1 
ATOM   1021 N  N   . PHE A 1 145 ? 26.101  5.105   31.011  1.00 20.74 ? 133 PHE A N   1 
ATOM   1022 C  CA  . PHE A 1 145 ? 26.512  5.329   29.604  1.00 19.83 ? 133 PHE A CA  1 
ATOM   1023 C  C   . PHE A 1 145 ? 25.526  6.294   28.973  1.00 16.85 ? 133 PHE A C   1 
ATOM   1024 O  O   . PHE A 1 145 ? 24.417  6.445   29.482  1.00 20.15 ? 133 PHE A O   1 
ATOM   1025 C  CB  . PHE A 1 145 ? 26.617  4.006   28.841  1.00 19.13 ? 133 PHE A CB  1 
ATOM   1026 C  CG  . PHE A 1 145 ? 25.359  3.167   28.868  1.00 19.34 ? 133 PHE A CG  1 
ATOM   1027 C  CD1 . PHE A 1 145 ? 24.347  3.345   27.933  1.00 19.85 ? 133 PHE A CD1 1 
ATOM   1028 C  CD2 . PHE A 1 145 ? 25.169  2.223   29.863  1.00 19.74 ? 133 PHE A CD2 1 
ATOM   1029 C  CE1 . PHE A 1 145 ? 23.192  2.582   27.988  1.00 20.26 ? 133 PHE A CE1 1 
ATOM   1030 C  CE2 . PHE A 1 145 ? 24.006  1.472   29.925  1.00 20.76 ? 133 PHE A CE2 1 
ATOM   1031 C  CZ  . PHE A 1 145 ? 23.026  1.640   28.976  1.00 19.85 ? 133 PHE A CZ  1 
ATOM   1032 N  N   . ASN A 1 146 ? 25.964  6.915   27.895  1.00 17.48 ? 134 ASN A N   1 
ATOM   1033 C  CA  . ASN A 1 146 ? 25.086  7.840   27.149  1.00 20.32 ? 134 ASN A CA  1 
ATOM   1034 C  C   . ASN A 1 146 ? 24.351  7.024   26.101  1.00 18.41 ? 134 ASN A C   1 
ATOM   1035 O  O   . ASN A 1 146 ? 24.865  5.948   25.693  1.00 15.19 ? 134 ASN A O   1 
ATOM   1036 C  CB  . ASN A 1 146 ? 25.835  9.031   26.596  1.00 23.97 ? 134 ASN A CB  1 
ATOM   1037 C  CG  . ASN A 1 146 ? 26.293  9.958   27.713  1.00 27.16 ? 134 ASN A CG  1 
ATOM   1038 O  OD1 . ASN A 1 146 ? 25.591  10.165  28.705  1.00 31.96 ? 134 ASN A OD1 1 
ATOM   1039 N  ND2 . ASN A 1 146 ? 27.451  10.534  27.525  1.00 27.63 ? 134 ASN A ND2 1 
ATOM   1040 N  N   . GLN A 1 147 ? 23.164  7.522   25.745  1.00 16.52 ? 135 GLN A N   1 
ATOM   1041 C  CA  . GLN A 1 147 ? 22.346  6.968   24.657  1.00 17.25 ? 135 GLN A CA  1 
ATOM   1042 C  C   . GLN A 1 147 ? 22.173  8.076   23.636  1.00 15.26 ? 135 GLN A C   1 
ATOM   1043 O  O   . GLN A 1 147 ? 21.835  9.216   24.054  1.00 17.04 ? 135 GLN A O   1 
ATOM   1044 C  CB  . GLN A 1 147 ? 20.933  6.600   25.098  1.00 20.71 ? 135 GLN A CB  1 
ATOM   1045 C  CG  . GLN A 1 147 ? 20.792  5.310   25.820  1.00 22.79 ? 135 GLN A CG  1 
ATOM   1046 C  CD  . GLN A 1 147 ? 19.331  5.159   26.166  1.00 23.88 ? 135 GLN A CD  1 
ATOM   1047 O  OE1 . GLN A 1 147 ? 18.652  6.107   26.564  1.00 24.51 ? 135 GLN A OE1 1 
ATOM   1048 N  NE2 . GLN A 1 147 ? 18.852  3.943   26.047  1.00 21.95 ? 135 GLN A NE2 1 
ATOM   1049 N  N   . TYR A 1 148 ? 22.432  7.806   22.367  1.00 13.93 ? 136 TYR A N   1 
ATOM   1050 C  CA  . TYR A 1 148 ? 22.180  8.773   21.291  1.00 14.15 ? 136 TYR A CA  1 
ATOM   1051 C  C   . TYR A 1 148 ? 21.021  8.255   20.456  1.00 15.76 ? 136 TYR A C   1 
ATOM   1052 O  O   . TYR A 1 148 ? 20.879  7.028   20.308  1.00 15.23 ? 136 TYR A O   1 
ATOM   1053 C  CB  . TYR A 1 148 ? 23.393  8.948   20.395  1.00 15.32 ? 136 TYR A CB  1 
ATOM   1054 C  CG  . TYR A 1 148 ? 24.647  9.283   21.144  1.00 15.83 ? 136 TYR A CG  1 
ATOM   1055 C  CD1 . TYR A 1 148 ? 24.617  9.928   22.376  1.00 16.74 ? 136 TYR A CD1 1 
ATOM   1056 C  CD2 . TYR A 1 148 ? 25.861  9.044   20.554  1.00 16.18 ? 136 TYR A CD2 1 
ATOM   1057 C  CE1 . TYR A 1 148 ? 25.785  10.252  23.047  1.00 18.56 ? 136 TYR A CE1 1 
ATOM   1058 C  CE2 . TYR A 1 148 ? 27.038  9.381   21.201  1.00 19.05 ? 136 TYR A CE2 1 
ATOM   1059 C  CZ  . TYR A 1 148 ? 26.996  9.984   22.443  1.00 18.85 ? 136 TYR A CZ  1 
ATOM   1060 O  OH  . TYR A 1 148 ? 28.180  10.269  23.078  1.00 26.82 ? 136 TYR A OH  1 
ATOM   1061 N  N   . TRP A 1 149 ? 20.190  9.181   20.013  1.00 14.53 ? 137 TRP A N   1 
ATOM   1062 C  CA  . TRP A 1 149 ? 18.948  8.885   19.289  1.00 14.97 ? 137 TRP A CA  1 
ATOM   1063 C  C   . TRP A 1 149 ? 18.909  9.722   18.015  1.00 14.93 ? 137 TRP A C   1 
ATOM   1064 O  O   . TRP A 1 149 ? 19.147  10.929  18.061  1.00 15.27 ? 137 TRP A O   1 
ATOM   1065 C  CB  . TRP A 1 149 ? 17.709  9.214   20.125  1.00 14.72 ? 137 TRP A CB  1 
ATOM   1066 C  CG  . TRP A 1 149 ? 17.586  8.483   21.416  1.00 15.72 ? 137 TRP A CG  1 
ATOM   1067 C  CD1 . TRP A 1 149 ? 18.161  8.857   22.594  1.00 17.28 ? 137 TRP A CD1 1 
ATOM   1068 C  CD2 . TRP A 1 149 ? 16.909  7.242   21.661  1.00 14.34 ? 137 TRP A CD2 1 
ATOM   1069 N  NE1 . TRP A 1 149 ? 17.787  7.991   23.582  1.00 16.12 ? 137 TRP A NE1 1 
ATOM   1070 C  CE2 . TRP A 1 149 ? 17.082  6.956   23.028  1.00 16.58 ? 137 TRP A CE2 1 
ATOM   1071 C  CE3 . TRP A 1 149 ? 16.150  6.363   20.875  1.00 15.05 ? 137 TRP A CE3 1 
ATOM   1072 C  CZ2 . TRP A 1 149 ? 16.524  5.829   23.613  1.00 16.23 ? 137 TRP A CZ2 1 
ATOM   1073 C  CZ3 . TRP A 1 149 ? 15.621  5.239   21.449  1.00 16.41 ? 137 TRP A CZ3 1 
ATOM   1074 C  CH2 . TRP A 1 149 ? 15.839  4.959   22.797  1.00 16.66 ? 137 TRP A CH2 1 
ATOM   1075 N  N   . SER A 1 150 ? 18.549  9.080   16.919  1.00 15.73 ? 138 SER A N   1 
ATOM   1076 C  CA  . SER A 1 150 ? 18.046  9.725   15.692  1.00 14.41 ? 138 SER A CA  1 
ATOM   1077 C  C   . SER A 1 150 ? 16.627  9.208   15.519  1.00 14.83 ? 138 SER A C   1 
ATOM   1078 O  O   . SER A 1 150 ? 16.524  7.987   15.377  1.00 14.89 ? 138 SER A O   1 
ATOM   1079 C  CB  . SER A 1 150 ? 18.841  9.307   14.495  1.00 17.21 ? 138 SER A CB  1 
ATOM   1080 O  OG  . SER A 1 150 ? 19.843  10.216  14.186  1.00 19.76 ? 138 SER A OG  1 
ATOM   1081 N  N   . VAL A 1 151 ? 15.585  10.054  15.562  1.00 13.95 ? 139 VAL A N   1 
ATOM   1082 C  CA  . VAL A 1 151 ? 14.176  9.551   15.514  1.00 15.11 ? 139 VAL A CA  1 
ATOM   1083 C  C   . VAL A 1 151 ? 13.515  10.124  14.257  1.00 16.52 ? 139 VAL A C   1 
ATOM   1084 O  O   . VAL A 1 151 ? 13.365  11.353  14.179  1.00 16.35 ? 139 VAL A O   1 
ATOM   1085 C  CB  . VAL A 1 151 ? 13.390  9.929   16.794  1.00 15.68 ? 139 VAL A CB  1 
ATOM   1086 C  CG1 . VAL A 1 151 ? 11.982  9.320   16.760  1.00 16.16 ? 139 VAL A CG1 1 
ATOM   1087 C  CG2 . VAL A 1 151 ? 14.145  9.521   18.067  1.00 15.81 ? 139 VAL A CG2 1 
ATOM   1088 N  N   . ARG A 1 152 ? 13.172  9.268   13.309  1.00 13.72 ? 140 ARG A N   1 
ATOM   1089 C  CA  . ARG A 1 152 ? 12.555  9.665   12.021  1.00 14.79 ? 140 ARG A CA  1 
ATOM   1090 C  C   . ARG A 1 152 ? 11.237  10.359  12.346  1.00 16.81 ? 140 ARG A C   1 
ATOM   1091 O  O   . ARG A 1 152 ? 10.489  9.808   13.191  1.00 14.54 ? 140 ARG A O   1 
ATOM   1092 C  CB  . ARG A 1 152 ? 12.354  8.439   11.136  1.00 15.17 ? 140 ARG A CB  1 
ATOM   1093 C  CG  . ARG A 1 152 ? 12.242  8.745   9.652   1.00 15.88 ? 140 ARG A CG  1 
ATOM   1094 C  CD  . ARG A 1 152 ? 12.099  7.473   8.826   1.00 15.82 ? 140 ARG A CD  1 
ATOM   1095 N  NE  . ARG A 1 152 ? 11.741  7.739   7.436   1.00 17.72 ? 140 ARG A NE  1 
ATOM   1096 C  CZ  . ARG A 1 152 ? 12.584  7.935   6.422   1.00 17.94 ? 140 ARG A CZ  1 
ATOM   1097 N  NH1 . ARG A 1 152 ? 13.888  7.989   6.585   1.00 19.03 ? 140 ARG A NH1 1 
ATOM   1098 N  NH2 . ARG A 1 152 ? 12.089  8.127   5.212   1.00 21.94 ? 140 ARG A NH2 1 
ATOM   1099 N  N   . THR A 1 153 ? 10.956  11.481  11.674  1.00 17.15 ? 141 THR A N   1 
ATOM   1100 C  CA  . THR A 1 153 ? 9.684   12.237  11.853  1.00 18.29 ? 141 THR A CA  1 
ATOM   1101 C  C   . THR A 1 153 ? 8.523   11.517  11.167  1.00 18.56 ? 141 THR A C   1 
ATOM   1102 O  O   . THR A 1 153 ? 7.400   11.699  11.642  1.00 21.40 ? 141 THR A O   1 
ATOM   1103 C  CB  . THR A 1 153 ? 9.797   13.688  11.347  1.00 20.85 ? 141 THR A CB  1 
ATOM   1104 O  OG1 . THR A 1 153 ? 10.095  13.689  9.953   1.00 20.79 ? 141 THR A OG1 1 
ATOM   1105 C  CG2 . THR A 1 153 ? 10.856  14.485  12.081  1.00 23.18 ? 141 THR A CG2 1 
ATOM   1106 N  N   . ASP A 1 154 ? 8.756   10.871  10.022  1.00 18.40 ? 142 ASP A N   1 
ATOM   1107 C  CA  . ASP A 1 154 ? 7.741   10.083  9.262   1.00 21.63 ? 142 ASP A CA  1 
ATOM   1108 C  C   . ASP A 1 154 ? 8.066   8.595   9.425   1.00 18.01 ? 142 ASP A C   1 
ATOM   1109 O  O   . ASP A 1 154 ? 8.974   8.073   8.726   1.00 19.55 ? 142 ASP A O   1 
ATOM   1110 C  CB  . ASP A 1 154 ? 7.690   10.449  7.782   1.00 23.51 ? 142 ASP A CB  1 
ATOM   1111 C  CG  . ASP A 1 154 ? 6.627   9.653   7.025   1.00 26.48 ? 142 ASP A CG  1 
ATOM   1112 O  OD1 . ASP A 1 154 ? 5.688   9.200   7.664   1.00 32.08 ? 142 ASP A OD1 1 
ATOM   1113 O  OD2 . ASP A 1 154 ? 6.762   9.481   5.820   1.00 32.60 ? 142 ASP A OD2 1 
ATOM   1114 N  N   . HIS A 1 155 ? 7.334   7.911   10.292  1.00 18.22 ? 143 HIS A N   1 
ATOM   1115 C  CA  . HIS A 1 155 ? 7.626   6.488   10.632  1.00 16.40 ? 143 HIS A CA  1 
ATOM   1116 C  C   . HIS A 1 155 ? 7.511   5.597   9.391   1.00 16.83 ? 143 HIS A C   1 
ATOM   1117 O  O   . HIS A 1 155 ? 6.555   5.737   8.591   1.00 14.95 ? 143 HIS A O   1 
ATOM   1118 C  CB  . HIS A 1 155 ? 6.686   6.026   11.741  1.00 18.35 ? 143 HIS A CB  1 
ATOM   1119 C  CG  . HIS A 1 155 ? 6.923   6.743   13.022  1.00 20.00 ? 143 HIS A CG  1 
ATOM   1120 N  ND1 . HIS A 1 155 ? 6.212   6.458   14.171  1.00 18.86 ? 143 HIS A ND1 1 
ATOM   1121 C  CD2 . HIS A 1 155 ? 7.798   7.707   13.341  1.00 19.81 ? 143 HIS A CD2 1 
ATOM   1122 C  CE1 . HIS A 1 155 ? 6.618   7.253   15.138  1.00 20.12 ? 143 HIS A CE1 1 
ATOM   1123 N  NE2 . HIS A 1 155 ? 7.593   8.031   14.667  1.00 19.68 ? 143 HIS A NE2 1 
ATOM   1124 N  N   . ARG A 1 156 ? 8.404   4.640   9.261   1.00 13.10 ? 144 ARG A N   1 
ATOM   1125 C  CA  . ARG A 1 156 ? 8.374   3.676   8.125   1.00 12.77 ? 144 ARG A CA  1 
ATOM   1126 C  C   . ARG A 1 156 ? 8.891   2.324   8.562   1.00 13.85 ? 144 ARG A C   1 
ATOM   1127 O  O   . ARG A 1 156 ? 9.560   2.224   9.615   1.00 14.89 ? 144 ARG A O   1 
ATOM   1128 C  CB  . ARG A 1 156 ? 9.189   4.182   6.946   1.00 12.68 ? 144 ARG A CB  1 
ATOM   1129 C  CG  . ARG A 1 156 ? 10.682  4.272   7.199   1.00 13.93 ? 144 ARG A CG  1 
ATOM   1130 C  CD  . ARG A 1 156 ? 11.387  4.579   5.899   1.00 14.03 ? 144 ARG A CD  1 
ATOM   1131 N  NE  . ARG A 1 156 ? 12.793  4.627   6.236   1.00 15.83 ? 144 ARG A NE  1 
ATOM   1132 C  CZ  . ARG A 1 156 ? 13.792  4.798   5.381   1.00 16.28 ? 144 ARG A CZ  1 
ATOM   1133 N  NH1 . ARG A 1 156 ? 13.579  5.006   4.093   1.00 16.07 ? 144 ARG A NH1 1 
ATOM   1134 N  NH2 . ARG A 1 156 ? 15.024  4.738   5.846   1.00 17.56 ? 144 ARG A NH2 1 
ATOM   1135 N  N   . VAL A 1 157 ? 8.511   1.324   7.780   1.00 13.87 ? 145 VAL A N   1 
ATOM   1136 C  CA  . VAL A 1 157 ? 8.979   -0.065  7.910   1.00 14.37 ? 145 VAL A CA  1 
ATOM   1137 C  C   . VAL A 1 157 ? 9.654   -0.435  6.592   1.00 15.56 ? 145 VAL A C   1 
ATOM   1138 O  O   . VAL A 1 157 ? 8.943   -0.764  5.592   1.00 15.60 ? 145 VAL A O   1 
ATOM   1139 C  CB  . VAL A 1 157 ? 7.840   -1.025  8.292   1.00 15.46 ? 145 VAL A CB  1 
ATOM   1140 C  CG1 . VAL A 1 157 ? 8.415   -2.413  8.456   1.00 15.76 ? 145 VAL A CG1 1 
ATOM   1141 C  CG2 . VAL A 1 157 ? 7.110   -0.585  9.557   1.00 18.12 ? 145 VAL A CG2 1 
ATOM   1142 N  N   . GLY A 1 158 ? 10.973  -0.320  6.554   1.00 16.42 ? 146 GLY A N   1 
ATOM   1143 C  CA  . GLY A 1 158 ? 11.741  -0.700  5.359   1.00 16.60 ? 146 GLY A CA  1 
ATOM   1144 C  C   . GLY A 1 158 ? 12.429  0.490   4.759   1.00 19.28 ? 146 GLY A C   1 
ATOM   1145 O  O   . GLY A 1 158 ? 12.020  1.617   5.025   1.00 23.39 ? 146 GLY A O   1 
ATOM   1146 N  N   . GLY A 1 159 ? 13.425  0.243   3.925   1.00 18.76 ? 147 GLY A N   1 
ATOM   1147 C  CA  . GLY A 1 159 ? 14.169  1.331   3.293   1.00 18.81 ? 147 GLY A CA  1 
ATOM   1148 C  C   . GLY A 1 159 ? 15.643  1.181   3.556   1.00 18.32 ? 147 GLY A C   1 
ATOM   1149 O  O   . GLY A 1 159 ? 16.077  0.112   3.957   1.00 20.77 ? 147 GLY A O   1 
ATOM   1150 N  N   . THR A 1 160 ? 16.366  2.278   3.344   1.00 17.02 ? 148 THR A N   1 
ATOM   1151 C  CA  . THR A 1 160 ? 17.835  2.354   3.414   1.00 16.90 ? 148 THR A CA  1 
ATOM   1152 C  C   . THR A 1 160 ? 18.177  3.247   4.601   1.00 15.27 ? 148 THR A C   1 
ATOM   1153 O  O   . THR A 1 160 ? 17.543  4.270   4.790   1.00 17.10 ? 148 THR A O   1 
ATOM   1154 C  CB  . THR A 1 160 ? 18.353  2.902   2.073   1.00 17.50 ? 148 THR A CB  1 
ATOM   1155 O  OG1 . THR A 1 160 ? 17.882  1.997   1.055   1.00 21.10 ? 148 THR A OG1 1 
ATOM   1156 C  CG2 . THR A 1 160 ? 19.849  3.078   2.032   1.00 18.20 ? 148 THR A CG2 1 
ATOM   1157 N  N   . VAL A 1 161 ? 19.129  2.847   5.422   1.00 14.07 ? 149 VAL A N   1 
ATOM   1158 C  CA  . VAL A 1 161 ? 19.693  3.716   6.491   1.00 13.18 ? 149 VAL A CA  1 
ATOM   1159 C  C   . VAL A 1 161 ? 21.172  3.916   6.164   1.00 13.28 ? 149 VAL A C   1 
ATOM   1160 O  O   . VAL A 1 161 ? 21.913  2.933   6.294   1.00 14.19 ? 149 VAL A O   1 
ATOM   1161 C  CB  . VAL A 1 161 ? 19.536  3.097   7.885   1.00 13.52 ? 149 VAL A CB  1 
ATOM   1162 C  CG1 . VAL A 1 161 ? 20.145  4.001   8.951   1.00 13.92 ? 149 VAL A CG1 1 
ATOM   1163 C  CG2 . VAL A 1 161 ? 18.072  2.813   8.203   1.00 13.65 ? 149 VAL A CG2 1 
ATOM   1164 N  N   . THR A 1 162 ? 21.553  5.157   5.840   1.00 13.90 ? 150 THR A N   1 
ATOM   1165 C  CA  . THR A 1 162 ? 22.974  5.528   5.630   1.00 14.97 ? 150 THR A CA  1 
ATOM   1166 C  C   . THR A 1 162 ? 23.533  5.875   7.018   1.00 13.46 ? 150 THR A C   1 
ATOM   1167 O  O   . THR A 1 162 ? 23.555  7.077   7.400   1.00 14.30 ? 150 THR A O   1 
ATOM   1168 C  CB  . THR A 1 162 ? 23.122  6.586   4.543   1.00 18.28 ? 150 THR A CB  1 
ATOM   1169 O  OG1 . THR A 1 162 ? 22.393  6.122   3.407   1.00 19.11 ? 150 THR A OG1 1 
ATOM   1170 C  CG2 . THR A 1 162 ? 24.575  6.828   4.181   1.00 18.11 ? 150 THR A CG2 1 
ATOM   1171 N  N   . THR A 1 163 ? 24.021  4.855   7.724   1.00 13.84 ? 151 THR A N   1 
ATOM   1172 C  CA  . THR A 1 163 ? 24.414  4.993   9.153   1.00 14.59 ? 151 THR A CA  1 
ATOM   1173 C  C   . THR A 1 163 ? 25.467  6.090   9.319   1.00 15.88 ? 151 THR A C   1 
ATOM   1174 O  O   . THR A 1 163 ? 25.436  6.778   10.351  1.00 13.66 ? 151 THR A O   1 
ATOM   1175 C  CB  . THR A 1 163 ? 24.835  3.681   9.820   1.00 15.00 ? 151 THR A CB  1 
ATOM   1176 O  OG1 . THR A 1 163 ? 26.026  3.124   9.260   1.00 15.72 ? 151 THR A OG1 1 
ATOM   1177 C  CG2 . THR A 1 163 ? 23.762  2.619   9.782   1.00 14.92 ? 151 THR A CG2 1 
ATOM   1178 N  N   . GLN A 1 164 ? 26.382  6.214   8.359   1.00 15.27 ? 152 GLN A N   1 
ATOM   1179 C  CA  . GLN A 1 164 ? 27.457  7.232   8.463   1.00 19.71 ? 152 GLN A CA  1 
ATOM   1180 C  C   . GLN A 1 164 ? 26.868  8.629   8.560   1.00 17.13 ? 152 GLN A C   1 
ATOM   1181 O  O   . GLN A 1 164 ? 27.362  9.390   9.345   1.00 16.98 ? 152 GLN A O   1 
ATOM   1182 C  CB  . GLN A 1 164 ? 28.441  7.194   7.296   1.00 22.53 ? 152 GLN A CB  1 
ATOM   1183 C  CG  . GLN A 1 164 ? 29.673  8.065   7.562   1.00 25.87 ? 152 GLN A CG  1 
ATOM   1184 C  CD  . GLN A 1 164 ? 30.471  7.591   8.758   1.00 30.17 ? 152 GLN A CD  1 
ATOM   1185 O  OE1 . GLN A 1 164 ? 30.954  6.459   8.804   1.00 33.66 ? 152 GLN A OE1 1 
ATOM   1186 N  NE2 . GLN A 1 164 ? 30.621  8.447   9.754   1.00 33.45 ? 152 GLN A NE2 1 
ATOM   1187 N  N   . ASN A 1 165 ? 25.780  8.954   7.850   1.00 17.23 ? 153 ASN A N   1 
ATOM   1188 C  CA  . ASN A 1 165 ? 25.150  10.302  7.951   1.00 18.18 ? 153 ASN A CA  1 
ATOM   1189 C  C   . ASN A 1 165 ? 24.667  10.566  9.381   1.00 15.82 ? 153 ASN A C   1 
ATOM   1190 O  O   . ASN A 1 165 ? 24.694  11.752  9.847   1.00 18.89 ? 153 ASN A O   1 
ATOM   1191 C  CB  . ASN A 1 165 ? 24.005  10.451  6.952   1.00 19.64 ? 153 ASN A CB  1 
ATOM   1192 C  CG  . ASN A 1 165 ? 24.473  10.447  5.517   1.00 23.20 ? 153 ASN A CG  1 
ATOM   1193 O  OD1 . ASN A 1 165 ? 25.667  10.625  5.245   1.00 22.75 ? 153 ASN A OD1 1 
ATOM   1194 N  ND2 . ASN A 1 165 ? 23.547  10.186  4.598   1.00 23.57 ? 153 ASN A ND2 1 
ATOM   1195 N  N   . HIS A 1 166 ? 24.171  9.536   10.072  1.00 15.05 ? 154 HIS A N   1 
ATOM   1196 C  CA  . HIS A 1 166 ? 23.709  9.698   11.468  1.00 13.30 ? 154 HIS A CA  1 
ATOM   1197 C  C   . HIS A 1 166 ? 24.912  9.873   12.402  1.00 14.91 ? 154 HIS A C   1 
ATOM   1198 O  O   . HIS A 1 166 ? 24.875  10.753  13.253  1.00 14.33 ? 154 HIS A O   1 
ATOM   1199 C  CB  . HIS A 1 166 ? 22.854  8.520   11.925  1.00 14.08 ? 154 HIS A CB  1 
ATOM   1200 C  CG  . HIS A 1 166 ? 21.583  8.423   11.136  1.00 11.70 ? 154 HIS A CG  1 
ATOM   1201 N  ND1 . HIS A 1 166 ? 20.450  9.054   11.533  1.00 13.72 ? 154 HIS A ND1 1 
ATOM   1202 C  CD2 . HIS A 1 166 ? 21.295  7.798   9.975   1.00 13.23 ? 154 HIS A CD2 1 
ATOM   1203 C  CE1 . HIS A 1 166 ? 19.478  8.831   10.651  1.00 12.11 ? 154 HIS A CE1 1 
ATOM   1204 N  NE2 . HIS A 1 166 ? 19.975  8.040   9.682   1.00 11.91 ? 154 HIS A NE2 1 
ATOM   1205 N  N   . PHE A 1 167 ? 25.936  9.057   12.228  1.00 16.21 ? 155 PHE A N   1 
ATOM   1206 C  CA  . PHE A 1 167 ? 27.156  9.126   13.069  1.00 16.23 ? 155 PHE A CA  1 
ATOM   1207 C  C   . PHE A 1 167 ? 27.771  10.525  12.919  1.00 18.87 ? 155 PHE A C   1 
ATOM   1208 O  O   . PHE A 1 167 ? 28.182  11.081  13.936  1.00 19.06 ? 155 PHE A O   1 
ATOM   1209 C  CB  . PHE A 1 167 ? 28.098  7.967   12.769  1.00 18.71 ? 155 PHE A CB  1 
ATOM   1210 C  CG  . PHE A 1 167 ? 27.550  6.586   13.007  1.00 18.00 ? 155 PHE A CG  1 
ATOM   1211 C  CD1 . PHE A 1 167 ? 26.451  6.364   13.819  1.00 18.54 ? 155 PHE A CD1 1 
ATOM   1212 C  CD2 . PHE A 1 167 ? 28.073  5.516   12.310  1.00 20.20 ? 155 PHE A CD2 1 
ATOM   1213 C  CE1 . PHE A 1 167 ? 25.938  5.081   13.979  1.00 19.96 ? 155 PHE A CE1 1 
ATOM   1214 C  CE2 . PHE A 1 167 ? 27.569  4.230   12.480  1.00 19.67 ? 155 PHE A CE2 1 
ATOM   1215 C  CZ  . PHE A 1 167 ? 26.516  4.018   13.333  1.00 19.43 ? 155 PHE A CZ  1 
ATOM   1216 N  N   . ASP A 1 168 ? 27.846  11.053  11.700  1.00 17.76 ? 156 ASP A N   1 
ATOM   1217 C  CA  . ASP A 1 168 ? 28.446  12.388  11.407  1.00 20.85 ? 156 ASP A CA  1 
ATOM   1218 C  C   . ASP A 1 168 ? 27.598  13.487  12.060  1.00 19.80 ? 156 ASP A C   1 
ATOM   1219 O  O   . ASP A 1 168 ? 28.176  14.403  12.664  1.00 18.60 ? 156 ASP A O   1 
ATOM   1220 C  CB  . ASP A 1 168 ? 28.559  12.625  9.904   1.00 20.59 ? 156 ASP A CB  1 
ATOM   1221 C  CG  . ASP A 1 168 ? 29.646  11.840  9.184   1.00 25.50 ? 156 ASP A CG  1 
ATOM   1222 O  OD1 . ASP A 1 168 ? 30.593  11.374  9.848   1.00 29.65 ? 156 ASP A OD1 1 
ATOM   1223 O  OD2 . ASP A 1 168 ? 29.529  11.702  7.933   1.00 29.27 ? 156 ASP A OD2 1 
ATOM   1224 N  N   . ALA A 1 169 ? 26.265  13.382  12.005  1.00 19.89 ? 157 ALA A N   1 
ATOM   1225 C  CA  . ALA A 1 169 ? 25.352  14.364  12.625  1.00 18.77 ? 157 ALA A CA  1 
ATOM   1226 C  C   . ALA A 1 169 ? 25.514  14.359  14.147  1.00 17.29 ? 157 ALA A C   1 
ATOM   1227 O  O   . ALA A 1 169 ? 25.516  15.439  14.757  1.00 18.42 ? 157 ALA A O   1 
ATOM   1228 C  CB  . ALA A 1 169 ? 23.921  14.104  12.204  1.00 19.29 ? 157 ALA A CB  1 
ATOM   1229 N  N   . TRP A 1 170 ? 25.596  13.185  14.764  1.00 15.54 ? 158 TRP A N   1 
ATOM   1230 C  CA  . TRP A 1 170 ? 25.805  13.091  16.216  1.00 17.00 ? 158 TRP A CA  1 
ATOM   1231 C  C   . TRP A 1 170 ? 27.144  13.740  16.575  1.00 16.31 ? 158 TRP A C   1 
ATOM   1232 O  O   . TRP A 1 170 ? 27.138  14.521  17.529  1.00 16.02 ? 158 TRP A O   1 
ATOM   1233 C  CB  . TRP A 1 170 ? 25.753  11.650  16.698  1.00 17.47 ? 158 TRP A CB  1 
ATOM   1234 C  CG  . TRP A 1 170 ? 24.414  11.024  16.493  1.00 19.26 ? 158 TRP A CG  1 
ATOM   1235 C  CD1 . TRP A 1 170 ? 23.217  11.655  16.272  1.00 22.77 ? 158 TRP A CD1 1 
ATOM   1236 C  CD2 . TRP A 1 170 ? 24.147  9.618   16.492  1.00 19.14 ? 158 TRP A CD2 1 
ATOM   1237 N  NE1 . TRP A 1 170 ? 22.220  10.728  16.101  1.00 22.43 ? 158 TRP A NE1 1 
ATOM   1238 C  CE2 . TRP A 1 170 ? 22.760  9.472   16.266  1.00 20.79 ? 158 TRP A CE2 1 
ATOM   1239 C  CE3 . TRP A 1 170 ? 24.934  8.469   16.664  1.00 18.17 ? 158 TRP A CE3 1 
ATOM   1240 C  CZ2 . TRP A 1 170 ? 22.153  8.213   16.266  1.00 18.58 ? 158 TRP A CZ2 1 
ATOM   1241 C  CZ3 . TRP A 1 170 ? 24.343  7.232   16.599  1.00 17.59 ? 158 TRP A CZ3 1 
ATOM   1242 C  CH2 . TRP A 1 170 ? 22.967  7.105   16.376  1.00 16.85 ? 158 TRP A CH2 1 
ATOM   1243 N  N   . LYS A 1 171 ? 28.204  13.419  15.839  1.00 17.55 ? 159 LYS A N   1 
ATOM   1244 C  CA  . LYS A 1 171 ? 29.546  14.016  16.115  1.00 19.23 ? 159 LYS A CA  1 
ATOM   1245 C  C   . LYS A 1 171 ? 29.452  15.534  15.911  1.00 20.64 ? 159 LYS A C   1 
ATOM   1246 O  O   . LYS A 1 171 ? 29.992  16.272  16.763  1.00 19.87 ? 159 LYS A O   1 
ATOM   1247 C  CB  . LYS A 1 171 ? 30.618  13.367  15.236  1.00 22.13 ? 159 LYS A CB  1 
ATOM   1248 C  CG  . LYS A 1 171 ? 32.024  13.926  15.413  1.00 27.92 ? 159 LYS A CG  1 
ATOM   1249 C  CD  . LYS A 1 171 ? 33.008  13.250  14.471  1.00 33.57 ? 159 LYS A CD  1 
ATOM   1250 C  CE  . LYS A 1 171 ? 34.445  13.383  14.921  1.00 38.66 ? 159 LYS A CE  1 
ATOM   1251 N  NZ  . LYS A 1 171 ? 35.360  12.684  13.991  1.00 43.00 ? 159 LYS A NZ  1 
ATOM   1252 N  N   . ASN A 1 172 ? 28.768  15.995  14.859  1.00 21.97 ? 160 ASN A N   1 
ATOM   1253 C  CA  . ASN A 1 172 ? 28.602  17.450  14.587  1.00 25.38 ? 160 ASN A CA  1 
ATOM   1254 C  C   . ASN A 1 172 ? 27.952  18.114  15.802  1.00 24.88 ? 160 ASN A C   1 
ATOM   1255 O  O   . ASN A 1 172 ? 28.307  19.272  16.134  1.00 27.97 ? 160 ASN A O   1 
ATOM   1256 C  CB  . ASN A 1 172 ? 27.791  17.701  13.313  1.00 30.49 ? 160 ASN A CB  1 
ATOM   1257 C  CG  . ASN A 1 172 ? 28.544  17.380  12.039  1.00 38.53 ? 160 ASN A CG  1 
ATOM   1258 O  OD1 . ASN A 1 172 ? 29.770  17.250  12.043  1.00 50.29 ? 160 ASN A OD1 1 
ATOM   1259 N  ND2 . ASN A 1 172 ? 27.818  17.257  10.935  1.00 42.44 ? 160 ASN A ND2 1 
ATOM   1260 N  N   . ALA A 1 173 ? 27.008  17.431  16.442  1.00 21.73 ? 161 ALA A N   1 
ATOM   1261 C  CA  . ALA A 1 173 ? 26.212  17.944  17.570  1.00 22.95 ? 161 ALA A CA  1 
ATOM   1262 C  C   . ALA A 1 173 ? 27.005  17.872  18.882  1.00 23.54 ? 161 ALA A C   1 
ATOM   1263 O  O   . ALA A 1 173 ? 26.422  18.196  19.909  1.00 28.18 ? 161 ALA A O   1 
ATOM   1264 C  CB  . ALA A 1 173 ? 24.906  17.191  17.660  1.00 22.55 ? 161 ALA A CB  1 
ATOM   1265 N  N   . GLY A 1 174 ? 28.273  17.434  18.846  1.00 24.72 ? 162 GLY A N   1 
ATOM   1266 C  CA  . GLY A 1 174 ? 29.130  17.260  20.037  1.00 26.72 ? 162 GLY A CA  1 
ATOM   1267 C  C   . GLY A 1 174 ? 28.947  15.932  20.762  1.00 27.26 ? 162 GLY A C   1 
ATOM   1268 O  O   . GLY A 1 174 ? 29.357  15.869  21.948  1.00 32.38 ? 162 GLY A O   1 
ATOM   1269 N  N   . LEU A 1 175 ? 28.372  14.899  20.130  1.00 22.54 ? 163 LEU A N   1 
ATOM   1270 C  CA  . LEU A 1 175 ? 28.179  13.556  20.753  1.00 25.31 ? 163 LEU A CA  1 
ATOM   1271 C  C   . LEU A 1 175 ? 29.291  12.601  20.286  1.00 26.75 ? 163 LEU A C   1 
ATOM   1272 O  O   . LEU A 1 175 ? 29.190  12.092  19.145  1.00 25.43 ? 163 LEU A O   1 
ATOM   1273 C  CB  . LEU A 1 175 ? 26.814  13.002  20.350  1.00 24.70 ? 163 LEU A CB  1 
ATOM   1274 C  CG  . LEU A 1 175 ? 25.622  13.910  20.653  1.00 25.32 ? 163 LEU A CG  1 
ATOM   1275 C  CD1 . LEU A 1 175 ? 24.341  13.237  20.200  1.00 26.32 ? 163 LEU A CD1 1 
ATOM   1276 C  CD2 . LEU A 1 175 ? 25.568  14.253  22.139  1.00 25.38 ? 163 LEU A CD2 1 
ATOM   1277 N  N   . GLU A 1 176 ? 30.191  12.257  21.212  1.00 27.72 ? 164 GLU A N   1 
ATOM   1278 C  CA  . GLU A 1 176 ? 31.410  11.444  20.979  1.00 28.45 ? 164 GLU A CA  1 
ATOM   1279 C  C   . GLU A 1 176 ? 31.021  9.967   20.831  1.00 22.69 ? 164 GLU A C   1 
ATOM   1280 O  O   . GLU A 1 176 ? 30.328  9.441   21.700  1.00 23.08 ? 164 GLU A O   1 
ATOM   1281 C  CB  . GLU A 1 176 ? 32.367  11.655  22.158  1.00 31.14 ? 164 GLU A CB  1 
ATOM   1282 C  CG  . GLU A 1 176 ? 32.911  13.080  22.255  1.00 37.70 ? 164 GLU A CG  1 
ATOM   1283 C  CD  . GLU A 1 176 ? 34.346  13.267  21.781  1.00 43.99 ? 164 GLU A CD  1 
ATOM   1284 O  OE1 . GLU A 1 176 ? 34.640  14.289  21.092  1.00 51.71 ? 164 GLU A OE1 1 
ATOM   1285 O  OE2 . GLU A 1 176 ? 35.184  12.409  22.124  1.00 45.98 ? 164 GLU A OE2 1 
ATOM   1286 N  N   . MET A 1 177 ? 31.513  9.328   19.788  1.00 23.97 ? 165 MET A N   1 
ATOM   1287 C  CA  . MET A 1 177 ? 31.344  7.876   19.539  1.00 23.83 ? 165 MET A CA  1 
ATOM   1288 C  C   . MET A 1 177 ? 32.662  7.174   19.848  1.00 23.27 ? 165 MET A C   1 
ATOM   1289 O  O   . MET A 1 177 ? 33.717  7.727   19.518  1.00 23.55 ? 165 MET A O   1 
ATOM   1290 C  CB  . MET A 1 177 ? 30.939  7.615   18.087  1.00 28.82 ? 165 MET A CB  1 
ATOM   1291 C  CG  . MET A 1 177 ? 29.605  8.293   17.757  1.00 33.05 ? 165 MET A CG  1 
ATOM   1292 S  SD  . MET A 1 177 ? 28.242  7.164   18.062  1.00 42.85 ? 165 MET A SD  1 
ATOM   1293 C  CE  . MET A 1 177 ? 28.421  6.072   16.655  1.00 33.57 ? 165 MET A CE  1 
ATOM   1294 N  N   . GLY A 1 178 ? 32.573  5.980   20.397  1.00 20.20 ? 166 GLY A N   1 
ATOM   1295 C  CA  . GLY A 1 178 ? 33.726  5.126   20.702  1.00 21.29 ? 166 GLY A CA  1 
ATOM   1296 C  C   . GLY A 1 178 ? 34.043  4.193   19.549  1.00 21.35 ? 166 GLY A C   1 
ATOM   1297 O  O   . GLY A 1 178 ? 33.608  4.461   18.399  1.00 20.86 ? 166 GLY A O   1 
ATOM   1298 N  N   . THR A 1 179 ? 34.807  3.150   19.846  1.00 19.45 ? 167 THR A N   1 
ATOM   1299 C  CA  . THR A 1 179 ? 35.082  2.005   18.955  1.00 21.17 ? 167 THR A CA  1 
ATOM   1300 C  C   . THR A 1 179 ? 33.791  1.213   18.750  1.00 18.46 ? 167 THR A C   1 
ATOM   1301 O  O   . THR A 1 179 ? 33.113  0.927   19.711  1.00 18.17 ? 167 THR A O   1 
ATOM   1302 C  CB  . THR A 1 179 ? 36.129  1.057   19.545  1.00 23.84 ? 167 THR A CB  1 
ATOM   1303 O  OG1 . THR A 1 179 ? 37.297  1.852   19.755  1.00 25.89 ? 167 THR A OG1 1 
ATOM   1304 C  CG2 . THR A 1 179 ? 36.406  -0.105  18.621  1.00 25.61 ? 167 THR A CG2 1 
ATOM   1305 N  N   . HIS A 1 180 ? 33.453  0.947   17.509  1.00 18.96 ? 168 HIS A N   1 
ATOM   1306 C  CA  . HIS A 1 180 ? 32.159  0.300   17.176  1.00 18.82 ? 168 HIS A CA  1 
ATOM   1307 C  C   . HIS A 1 180 ? 32.173  -1.150  17.651  1.00 18.23 ? 168 HIS A C   1 
ATOM   1308 O  O   . HIS A 1 180 ? 33.152  -1.900  17.371  1.00 20.41 ? 168 HIS A O   1 
ATOM   1309 C  CB  . HIS A 1 180 ? 31.909  0.408   15.675  1.00 20.89 ? 168 HIS A CB  1 
ATOM   1310 C  CG  . HIS A 1 180 ? 31.295  1.703   15.288  1.00 24.82 ? 168 HIS A CG  1 
ATOM   1311 N  ND1 . HIS A 1 180 ? 31.945  2.918   15.392  1.00 30.28 ? 168 HIS A ND1 1 
ATOM   1312 C  CD2 . HIS A 1 180 ? 30.046  1.990   14.884  1.00 25.80 ? 168 HIS A CD2 1 
ATOM   1313 C  CE1 . HIS A 1 180 ? 31.126  3.880   15.004  1.00 26.67 ? 168 HIS A CE1 1 
ATOM   1314 N  NE2 . HIS A 1 180 ? 29.960  3.334   14.709  1.00 30.60 ? 168 HIS A NE2 1 
ATOM   1315 N  N   . ASN A 1 181 ? 31.145  -1.525  18.404  1.00 14.86 ? 169 ASN A N   1 
ATOM   1316 C  CA  . ASN A 1 181 ? 30.782  -2.924  18.685  1.00 14.92 ? 169 ASN A CA  1 
ATOM   1317 C  C   . ASN A 1 181 ? 29.660  -3.303  17.713  1.00 13.54 ? 169 ASN A C   1 
ATOM   1318 O  O   . ASN A 1 181 ? 29.699  -2.840  16.569  1.00 16.61 ? 169 ASN A O   1 
ATOM   1319 C  CB  . ASN A 1 181 ? 30.399  -3.111  20.155  1.00 17.01 ? 169 ASN A CB  1 
ATOM   1320 C  CG  . ASN A 1 181 ? 30.452  -4.555  20.600  1.00 21.41 ? 169 ASN A CG  1 
ATOM   1321 O  OD1 . ASN A 1 181 ? 29.449  -5.263  20.552  1.00 19.88 ? 169 ASN A OD1 1 
ATOM   1322 N  ND2 . ASN A 1 181 ? 31.598  -5.005  21.110  1.00 24.28 ? 169 ASN A ND2 1 
ATOM   1323 N  N   . TYR A 1 182 ? 28.707  -4.111  18.122  1.00 13.46 ? 170 TYR A N   1 
ATOM   1324 C  CA  . TYR A 1 182 ? 27.706  -4.603  17.130  1.00 12.54 ? 170 TYR A CA  1 
ATOM   1325 C  C   . TYR A 1 182 ? 26.787  -3.471  16.693  1.00 12.50 ? 170 TYR A C   1 
ATOM   1326 O  O   . TYR A 1 182 ? 26.597  -2.415  17.351  1.00 11.75 ? 170 TYR A O   1 
ATOM   1327 C  CB  . TYR A 1 182 ? 26.916  -5.783  17.661  1.00 13.26 ? 170 TYR A CB  1 
ATOM   1328 C  CG  . TYR A 1 182 ? 25.975  -5.557  18.794  1.00 13.92 ? 170 TYR A CG  1 
ATOM   1329 C  CD1 . TYR A 1 182 ? 24.717  -5.070  18.548  1.00 14.49 ? 170 TYR A CD1 1 
ATOM   1330 C  CD2 . TYR A 1 182 ? 26.246  -6.038  20.068  1.00 14.80 ? 170 TYR A CD2 1 
ATOM   1331 C  CE1 . TYR A 1 182 ? 23.775  -5.005  19.537  1.00 14.00 ? 170 TYR A CE1 1 
ATOM   1332 C  CE2 . TYR A 1 182 ? 25.316  -5.956  21.080  1.00 15.30 ? 170 TYR A CE2 1 
ATOM   1333 C  CZ  . TYR A 1 182 ? 24.062  -5.457  20.802  1.00 15.36 ? 170 TYR A CZ  1 
ATOM   1334 O  OH  . TYR A 1 182 ? 23.145  -5.377  21.796  1.00 17.23 ? 170 TYR A OH  1 
ATOM   1335 N  N   . MET A 1 183 ? 26.168  -3.740  15.553  1.00 12.67 ? 171 MET A N   1 
ATOM   1336 C  CA  . MET A 1 183 ? 25.150  -2.883  14.936  1.00 11.95 ? 171 MET A CA  1 
ATOM   1337 C  C   . MET A 1 183 ? 24.120  -3.827  14.300  1.00 11.54 ? 171 MET A C   1 
ATOM   1338 O  O   . MET A 1 183 ? 24.487  -4.680  13.451  1.00 10.95 ? 171 MET A O   1 
ATOM   1339 C  CB  . MET A 1 183 ? 25.758  -1.946  13.899  1.00 14.15 ? 171 MET A CB  1 
ATOM   1340 C  CG  . MET A 1 183 ? 24.726  -1.027  13.335  1.00 15.39 ? 171 MET A CG  1 
ATOM   1341 S  SD  . MET A 1 183 ? 25.366  0.283   12.244  1.00 17.60 ? 171 MET A SD  1 
ATOM   1342 C  CE  . MET A 1 183 ? 25.927  -0.642  10.837  1.00 17.47 ? 171 MET A CE  1 
ATOM   1343 N  N   . ILE A 1 184 ? 22.858  -3.686  14.666  1.00 11.24 ? 172 ILE A N   1 
ATOM   1344 C  CA  . ILE A 1 184 ? 21.817  -4.635  14.198  1.00 11.39 ? 172 ILE A CA  1 
ATOM   1345 C  C   . ILE A 1 184 ? 20.577  -3.847  13.778  1.00 10.76 ? 172 ILE A C   1 
ATOM   1346 O  O   . ILE A 1 184 ? 20.411  -2.698  14.227  1.00 10.82 ? 172 ILE A O   1 
ATOM   1347 C  CB  . ILE A 1 184 ? 21.463  -5.686  15.275  1.00 12.37 ? 172 ILE A CB  1 
ATOM   1348 C  CG1 . ILE A 1 184 ? 20.979  -5.047  16.590  1.00 11.17 ? 172 ILE A CG1 1 
ATOM   1349 C  CG2 . ILE A 1 184 ? 22.597  -6.679  15.519  1.00 12.47 ? 172 ILE A CG2 1 
ATOM   1350 C  CD1 . ILE A 1 184 ? 20.445  -6.082  17.572  1.00 13.24 ? 172 ILE A CD1 1 
ATOM   1351 N  N   . VAL A 1 185 ? 19.714  -4.448  12.974  1.00 10.22 ? 173 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 185 ? 18.352  -3.882  12.740  1.00 10.55 ? 173 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 185 ? 17.489  -4.551  13.786  1.00 9.97  ? 173 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 185 ? 17.206  -5.771  13.647  1.00 11.65 ? 173 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 185 ? 17.840  -4.105  11.305  1.00 10.40 ? 173 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 185 ? 16.398  -3.586  11.121  1.00 10.82 ? 173 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 185 ? 18.768  -3.462  10.315  1.00 12.70 ? 173 VAL A CG2 1 
ATOM   1358 N  N   . ALA A 1 186 ? 17.073  -3.805  14.802  1.00 10.63 ? 174 ALA A N   1 
ATOM   1359 C  CA  . ALA A 1 186 ? 16.435  -4.391  15.963  1.00 10.89 ? 174 ALA A CA  1 
ATOM   1360 C  C   . ALA A 1 186 ? 14.968  -4.042  16.059  1.00 10.78 ? 174 ALA A C   1 
ATOM   1361 O  O   . ALA A 1 186 ? 14.576  -2.931  15.768  1.00 13.54 ? 174 ALA A O   1 
ATOM   1362 C  CB  . ALA A 1 186 ? 17.148  -3.990  17.204  1.00 12.63 ? 174 ALA A CB  1 
ATOM   1363 N  N   . THR A 1 187 ? 14.240  -5.002  16.569  1.00 10.68 ? 175 THR A N   1 
ATOM   1364 C  CA  . THR A 1 187 ? 12.895  -4.847  17.114  1.00 11.19 ? 175 THR A CA  1 
ATOM   1365 C  C   . THR A 1 187 ? 13.021  -4.814  18.622  1.00 10.91 ? 175 THR A C   1 
ATOM   1366 O  O   . THR A 1 187 ? 13.623  -5.765  19.181  1.00 11.18 ? 175 THR A O   1 
ATOM   1367 C  CB  . THR A 1 187 ? 12.025  -6.000  16.655  1.00 11.57 ? 175 THR A CB  1 
ATOM   1368 O  OG1 . THR A 1 187 ? 12.053  -5.977  15.239  1.00 12.82 ? 175 THR A OG1 1 
ATOM   1369 C  CG2 . THR A 1 187 ? 10.607  -5.908  17.159  1.00 12.07 ? 175 THR A CG2 1 
ATOM   1370 N  N   . ALA A 1 188 ? 12.466  -3.763  19.253  1.00 11.01 ? 176 ALA A N   1 
ATOM   1371 C  CA  . ALA A 1 188 ? 12.499  -3.591  20.720  1.00 11.53 ? 176 ALA A CA  1 
ATOM   1372 C  C   . ALA A 1 188 ? 11.074  -3.489  21.218  1.00 13.19 ? 176 ALA A C   1 
ATOM   1373 O  O   . ALA A 1 188 ? 10.205  -3.069  20.456  1.00 13.24 ? 176 ALA A O   1 
ATOM   1374 C  CB  . ALA A 1 188 ? 13.279  -2.380  21.135  1.00 12.16 ? 176 ALA A CB  1 
ATOM   1375 N  N   . GLY A 1 189 ? 10.825  -4.025  22.405  1.00 13.41 ? 177 GLY A N   1 
ATOM   1376 C  CA  . GLY A 1 189 ? 9.492   -3.862  22.993  1.00 14.88 ? 177 GLY A CA  1 
ATOM   1377 C  C   . GLY A 1 189 ? 9.604   -3.612  24.472  1.00 16.18 ? 177 GLY A C   1 
ATOM   1378 O  O   . GLY A 1 189 ? 10.620  -4.031  25.110  1.00 14.99 ? 177 GLY A O   1 
ATOM   1379 N  N   . TYR A 1 190 ? 8.536   -3.079  25.050  1.00 17.24 ? 178 TYR A N   1 
ATOM   1380 C  CA  . TYR A 1 190 ? 8.457   -3.026  26.520  1.00 18.13 ? 178 TYR A CA  1 
ATOM   1381 C  C   . TYR A 1 190 ? 7.011   -3.045  26.970  1.00 16.89 ? 178 TYR A C   1 
ATOM   1382 O  O   . TYR A 1 190 ? 6.292   -2.173  26.471  1.00 16.08 ? 178 TYR A O   1 
ATOM   1383 C  CB  . TYR A 1 190 ? 9.073   -1.755  27.082  1.00 20.38 ? 178 TYR A CB  1 
ATOM   1384 C  CG  . TYR A 1 190 ? 8.963   -1.759  28.584  1.00 24.29 ? 178 TYR A CG  1 
ATOM   1385 C  CD1 . TYR A 1 190 ? 9.708   -2.636  29.354  1.00 26.23 ? 178 TYR A CD1 1 
ATOM   1386 C  CD2 . TYR A 1 190 ? 8.017   -0.976  29.227  1.00 24.59 ? 178 TYR A CD2 1 
ATOM   1387 C  CE1 . TYR A 1 190 ? 9.594   -2.670  30.737  1.00 29.98 ? 178 TYR A CE1 1 
ATOM   1388 C  CE2 . TYR A 1 190 ? 7.920   -0.972  30.603  1.00 28.68 ? 178 TYR A CE2 1 
ATOM   1389 C  CZ  . TYR A 1 190 ? 8.699   -1.821  31.367  1.00 35.11 ? 178 TYR A CZ  1 
ATOM   1390 O  OH  . TYR A 1 190 ? 8.552   -1.796  32.728  1.00 38.52 ? 178 TYR A OH  1 
ATOM   1391 N  N   . GLN A 1 191 ? 6.639   -3.999  27.816  1.00 16.83 ? 179 GLN A N   1 
ATOM   1392 C  CA  . GLN A 1 191 ? 5.250   -4.165  28.338  1.00 17.23 ? 179 GLN A CA  1 
ATOM   1393 C  C   . GLN A 1 191 ? 4.247   -4.044  27.202  1.00 16.67 ? 179 GLN A C   1 
ATOM   1394 O  O   . GLN A 1 191 ? 3.357   -3.191  27.237  1.00 14.92 ? 179 GLN A O   1 
ATOM   1395 C  CB  . GLN A 1 191 ? 5.013   -3.132  29.441  1.00 20.57 ? 179 GLN A CB  1 
ATOM   1396 C  CG  . GLN A 1 191 ? 5.738   -3.559  30.708  1.00 22.48 ? 179 GLN A CG  1 
ATOM   1397 C  CD  . GLN A 1 191 ? 5.313   -2.817  31.955  1.00 26.81 ? 179 GLN A CD  1 
ATOM   1398 O  OE1 . GLN A 1 191 ? 4.671   -1.770  31.886  1.00 27.09 ? 179 GLN A OE1 1 
ATOM   1399 N  NE2 . GLN A 1 191 ? 5.665   -3.376  33.106  1.00 28.91 ? 179 GLN A NE2 1 
ATOM   1400 N  N   . SER A 1 192 ? 4.398   -4.886  26.204  1.00 15.37 ? 180 SER A N   1 
ATOM   1401 C  CA  . SER A 1 192 ? 3.570   -4.850  24.990  1.00 13.73 ? 180 SER A CA  1 
ATOM   1402 C  C   . SER A 1 192 ? 3.456   -6.262  24.419  1.00 13.76 ? 180 SER A C   1 
ATOM   1403 O  O   . SER A 1 192 ? 3.976   -7.247  25.023  1.00 13.41 ? 180 SER A O   1 
ATOM   1404 C  CB  . SER A 1 192 ? 4.135   -3.871  24.021  1.00 14.62 ? 180 SER A CB  1 
ATOM   1405 O  OG  . SER A 1 192 ? 5.414   -4.310  23.543  1.00 13.86 ? 180 SER A OG  1 
ATOM   1406 N  N   . SER A 1 193 ? 2.766   -6.407  23.299  1.00 12.80 ? 181 SER A N   1 
ATOM   1407 C  CA  . SER A 1 193 ? 2.658   -7.699  22.587  1.00 14.57 ? 181 SER A CA  1 
ATOM   1408 C  C   . SER A 1 193 ? 2.948   -7.351  21.127  1.00 14.36 ? 181 SER A C   1 
ATOM   1409 O  O   . SER A 1 193 ? 2.817   -6.157  20.769  1.00 15.87 ? 181 SER A O   1 
ATOM   1410 C  CB  . SER A 1 193 ? 1.307   -8.368  22.768  1.00 18.32 ? 181 SER A CB  1 
ATOM   1411 O  OG  . SER A 1 193 ? 1.092   -8.898  24.103  1.00 20.19 ? 181 SER A OG  1 
ATOM   1412 N  N   . GLY A 1 194 ? 3.256   -8.349  20.325  1.00 13.45 ? 182 GLY A N   1 
ATOM   1413 C  CA  . GLY A 1 194 ? 3.476   -8.078  18.911  1.00 12.39 ? 182 GLY A CA  1 
ATOM   1414 C  C   . GLY A 1 194 ? 4.158   -9.199  18.196  1.00 13.30 ? 182 GLY A C   1 
ATOM   1415 O  O   . GLY A 1 194 ? 4.448   -10.296 18.750  1.00 12.35 ? 182 GLY A O   1 
ATOM   1416 N  N   . SER A 1 195 ? 4.424   -8.913  16.936  1.00 13.63 ? 183 SER A N   1 
ATOM   1417 C  CA  . SER A 1 195 ? 5.249   -9.801  16.112  1.00 13.24 ? 183 SER A CA  1 
ATOM   1418 C  C   . SER A 1 195 ? 6.026   -8.950  15.126  1.00 13.23 ? 183 SER A C   1 
ATOM   1419 O  O   . SER A 1 195 ? 5.574   -7.861  14.770  1.00 12.47 ? 183 SER A O   1 
ATOM   1420 C  CB  . SER A 1 195 ? 4.438   -10.860 15.422  1.00 15.72 ? 183 SER A CB  1 
ATOM   1421 O  OG  . SER A 1 195 ? 3.580   -10.335 14.456  1.00 19.04 ? 183 SER A OG  1 
ATOM   1422 N  N   . ALA A 1 196 ? 7.114   -9.500  14.634  1.00 12.20 ? 184 ALA A N   1 
ATOM   1423 C  CA  . ALA A 1 196 ? 7.865   -8.837  13.556  1.00 11.56 ? 184 ALA A CA  1 
ATOM   1424 C  C   . ALA A 1 196 ? 8.657   -9.898  12.812  1.00 13.18 ? 184 ALA A C   1 
ATOM   1425 O  O   . ALA A 1 196 ? 9.034   -10.944 13.363  1.00 12.95 ? 184 ALA A O   1 
ATOM   1426 C  CB  . ALA A 1 196 ? 8.772   -7.755  14.088  1.00 13.35 ? 184 ALA A CB  1 
ATOM   1427 N  N   . SER A 1 197 ? 8.882   -9.619  11.536  1.00 12.96 ? 185 SER A N   1 
ATOM   1428 C  CA  . SER A 1 197 ? 9.682   -10.513 10.670  1.00 14.30 ? 185 SER A CA  1 
ATOM   1429 C  C   . SER A 1 197 ? 10.517  -9.597  9.807   1.00 12.38 ? 185 SER A C   1 
ATOM   1430 O  O   . SER A 1 197 ? 9.946   -8.908  8.948   1.00 12.55 ? 185 SER A O   1 
ATOM   1431 C  CB  . SER A 1 197 ? 8.828   -11.441 9.820   1.00 17.63 ? 185 SER A CB  1 
ATOM   1432 O  OG  . SER A 1 197 ? 8.192   -12.430 10.631  1.00 21.35 ? 185 SER A OG  1 
ATOM   1433 N  N   . ILE A 1 198 ? 11.801  -9.517  10.072  1.00 13.69 ? 186 ILE A N   1 
ATOM   1434 C  CA  . ILE A 1 198 ? 12.652  -8.477  9.444   1.00 12.20 ? 186 ILE A CA  1 
ATOM   1435 C  C   . ILE A 1 198 ? 13.791  -9.172  8.716   1.00 13.36 ? 186 ILE A C   1 
ATOM   1436 O  O   . ILE A 1 198 ? 14.395  -10.075 9.283   1.00 12.66 ? 186 ILE A O   1 
ATOM   1437 C  CB  . ILE A 1 198 ? 13.177  -7.481  10.506  1.00 13.01 ? 186 ILE A CB  1 
ATOM   1438 C  CG1 . ILE A 1 198 ? 12.023  -6.679  11.112  1.00 13.35 ? 186 ILE A CG1 1 
ATOM   1439 C  CG2 . ILE A 1 198 ? 14.228  -6.530  9.959   1.00 14.20 ? 186 ILE A CG2 1 
ATOM   1440 C  CD1 . ILE A 1 198 ? 11.395  -5.729  10.102  1.00 14.90 ? 186 ILE A CD1 1 
ATOM   1441 N  N   . THR A 1 199 ? 14.100  -8.707  7.523   1.00 14.27 ? 187 THR A N   1 
ATOM   1442 C  CA  . THR A 1 199 ? 15.277  -9.201  6.790   1.00 14.80 ? 187 THR A CA  1 
ATOM   1443 C  C   . THR A 1 199 ? 16.281  -8.077  6.593   1.00 15.81 ? 187 THR A C   1 
ATOM   1444 O  O   . THR A 1 199 ? 15.942  -7.076  5.968   1.00 13.34 ? 187 THR A O   1 
ATOM   1445 C  CB  . THR A 1 199 ? 14.884  -9.873  5.469   1.00 16.90 ? 187 THR A CB  1 
ATOM   1446 O  OG1 . THR A 1 199 ? 13.928  -10.893 5.705   1.00 18.97 ? 187 THR A OG1 1 
ATOM   1447 C  CG2 . THR A 1 199 ? 16.103  -10.458 4.777   1.00 17.20 ? 187 THR A CG2 1 
ATOM   1448 N  N   . VAL A 1 200 ? 17.538  -8.321  6.978   1.00 14.77 ? 188 VAL A N   1 
ATOM   1449 C  CA  . VAL A 1 200 ? 18.649  -7.371  6.729   1.00 18.65 ? 188 VAL A CA  1 
ATOM   1450 C  C   . VAL A 1 200 ? 19.251  -7.820  5.391   1.00 22.31 ? 188 VAL A C   1 
ATOM   1451 O  O   . VAL A 1 200 ? 19.571  -8.986  5.320   1.00 18.33 ? 188 VAL A O   1 
ATOM   1452 C  CB  . VAL A 1 200 ? 19.623  -7.426  7.920   1.00 19.18 ? 188 VAL A CB  1 
ATOM   1453 C  CG1 . VAL A 1 200 ? 20.788  -6.478  7.720   1.00 21.78 ? 188 VAL A CG1 1 
ATOM   1454 C  CG2 . VAL A 1 200 ? 18.911  -7.121  9.219   1.00 21.59 ? 188 VAL A CG2 1 
ATOM   1455 N  N   . GLN A 1 201 ? 19.173  -7.005  4.334   1.00 29.07 ? 189 GLN A N   1 
ATOM   1456 C  CA  . GLN A 1 201 ? 19.523  -7.437  2.945   1.00 37.21 ? 189 GLN A CA  1 
ATOM   1457 C  C   . GLN A 1 201 ? 21.019  -7.219  2.722   1.00 40.82 ? 189 GLN A C   1 
ATOM   1458 O  O   . GLN A 1 201 ? 21.579  -7.798  1.779   1.00 51.35 ? 189 GLN A O   1 
ATOM   1459 C  CB  . GLN A 1 201 ? 18.689  -6.709  1.881   1.00 43.83 ? 189 GLN A CB  1 
ATOM   1460 C  CG  . GLN A 1 201 ? 17.458  -7.489  1.411   1.00 47.27 ? 189 GLN A CG  1 
ATOM   1461 C  CD  . GLN A 1 201 ? 16.250  -7.280  2.292   1.00 48.42 ? 189 GLN A CD  1 
ATOM   1462 O  OE1 . GLN A 1 201 ? 16.070  -6.227  2.896   1.00 53.53 ? 189 GLN A OE1 1 
ATOM   1463 N  NE2 . GLN A 1 201 ? 15.385  -8.278  2.340   1.00 53.16 ? 189 GLN A NE2 1 
ATOM   1464 N  N   . GLU B 1 13  ? -5.305  21.462  34.325  1.00 34.77 ? 1   GLU B N   1 
ATOM   1465 C  CA  . GLU B 1 13  ? -5.350  22.131  35.657  1.00 31.63 ? 1   GLU B CA  1 
ATOM   1466 C  C   . GLU B 1 13  ? -4.265  21.593  36.608  1.00 29.73 ? 1   GLU B C   1 
ATOM   1467 O  O   . GLU B 1 13  ? -3.599  22.443  37.175  1.00 28.29 ? 1   GLU B O   1 
ATOM   1468 C  CB  . GLU B 1 13  ? -6.732  22.046  36.292  1.00 37.62 ? 1   GLU B CB  1 
ATOM   1469 C  CG  . GLU B 1 13  ? -6.916  22.972  37.469  1.00 37.35 ? 1   GLU B CG  1 
ATOM   1470 C  CD  . GLU B 1 13  ? -7.809  24.172  37.195  1.00 38.33 ? 1   GLU B CD  1 
ATOM   1471 O  OE1 . GLU B 1 13  ? -7.358  25.138  36.520  1.00 39.42 ? 1   GLU B OE1 1 
ATOM   1472 O  OE2 . GLU B 1 13  ? -8.975  24.121  37.632  1.00 42.83 ? 1   GLU B OE2 1 
ATOM   1473 N  N   . ILE B 1 14  ? -4.130  20.281  36.855  1.00 21.87 ? 2   ILE B N   1 
ATOM   1474 C  CA  . ILE B 1 14  ? -3.124  19.670  37.802  1.00 24.38 ? 2   ILE B CA  1 
ATOM   1475 C  C   . ILE B 1 14  ? -2.093  18.891  36.952  1.00 24.95 ? 2   ILE B C   1 
ATOM   1476 O  O   . ILE B 1 14  ? -2.549  18.087  36.088  1.00 21.11 ? 2   ILE B O   1 
ATOM   1477 C  CB  . ILE B 1 14  ? -3.884  18.770  38.816  1.00 24.65 ? 2   ILE B CB  1 
ATOM   1478 C  CG1 . ILE B 1 14  ? -5.045  19.514  39.489  1.00 27.68 ? 2   ILE B CG1 1 
ATOM   1479 C  CG2 . ILE B 1 14  ? -3.003  18.141  39.877  1.00 26.69 ? 2   ILE B CG2 1 
ATOM   1480 C  CD1 . ILE B 1 14  ? -5.826  18.694  40.518  1.00 28.36 ? 2   ILE B CD1 1 
ATOM   1481 N  N   . THR B 1 15  ? -0.775  19.046  37.178  1.00 22.21 ? 3   THR B N   1 
ATOM   1482 C  CA  . THR B 1 15  ? 0.301   18.365  36.392  1.00 22.96 ? 3   THR B CA  1 
ATOM   1483 C  C   . THR B 1 15  ? 1.293   17.602  37.299  1.00 21.74 ? 3   THR B C   1 
ATOM   1484 O  O   . THR B 1 15  ? 2.165   16.862  36.757  1.00 21.12 ? 3   THR B O   1 
ATOM   1485 C  CB  . THR B 1 15  ? 0.965   19.383  35.461  1.00 29.21 ? 3   THR B CB  1 
ATOM   1486 O  OG1 . THR B 1 15  ? 1.673   20.325  36.271  1.00 29.84 ? 3   THR B OG1 1 
ATOM   1487 C  CG2 . THR B 1 15  ? -0.054  20.093  34.596  1.00 32.74 ? 3   THR B CG2 1 
ATOM   1488 N  N   . SER B 1 16  ? 1.115   17.682  38.622  1.00 18.77 ? 4   SER B N   1 
ATOM   1489 C  CA  . SER B 1 16  ? 1.954   17.035  39.644  1.00 19.31 ? 4   SER B CA  1 
ATOM   1490 C  C   . SER B 1 16  ? 1.042   16.423  40.690  1.00 17.69 ? 4   SER B C   1 
ATOM   1491 O  O   . SER B 1 16  ? -0.122  16.933  40.852  1.00 18.38 ? 4   SER B O   1 
ATOM   1492 C  CB  . SER B 1 16  ? 2.929   18.031  40.246  1.00 22.90 ? 4   SER B CB  1 
ATOM   1493 O  OG  . SER B 1 16  ? 3.900   18.385  39.264  1.00 28.44 ? 4   SER B OG  1 
ATOM   1494 N  N   . SER B 1 17  ? 1.540   15.401  41.373  1.00 16.45 ? 5   SER B N   1 
ATOM   1495 C  CA  . SER B 1 17  ? 0.765   14.554  42.307  1.00 15.69 ? 5   SER B CA  1 
ATOM   1496 C  C   . SER B 1 17  ? 0.082   15.432  43.344  1.00 17.52 ? 5   SER B C   1 
ATOM   1497 O  O   . SER B 1 17  ? 0.746   16.314  43.935  1.00 16.62 ? 5   SER B O   1 
ATOM   1498 C  CB  . SER B 1 17  ? 1.569   13.478  42.945  1.00 16.44 ? 5   SER B CB  1 
ATOM   1499 O  OG  . SER B 1 17  ? 2.134   12.618  41.954  1.00 20.64 ? 5   SER B OG  1 
ATOM   1500 N  N   . GLU B 1 18  ? -1.188  15.147  43.595  1.00 15.29 ? 6   GLU B N   1 
ATOM   1501 C  CA  . GLU B 1 18  ? -2.018  15.909  44.554  1.00 16.04 ? 6   GLU B CA  1 
ATOM   1502 C  C   . GLU B 1 18  ? -3.172  15.004  44.988  1.00 15.76 ? 6   GLU B C   1 
ATOM   1503 O  O   . GLU B 1 18  ? -3.668  14.268  44.162  1.00 16.16 ? 6   GLU B O   1 
ATOM   1504 C  CB  . GLU B 1 18  ? -2.522  17.180  43.857  1.00 18.39 ? 6   GLU B CB  1 
ATOM   1505 C  CG  . GLU B 1 18  ? -3.493  18.053  44.640  1.00 23.36 ? 6   GLU B CG  1 
ATOM   1506 C  CD  . GLU B 1 18  ? -3.884  19.325  43.897  1.00 24.41 ? 6   GLU B CD  1 
ATOM   1507 O  OE1 . GLU B 1 18  ? -5.099  19.555  43.711  1.00 26.03 ? 6   GLU B OE1 1 
ATOM   1508 O  OE2 . GLU B 1 18  ? -2.962  20.034  43.401  1.00 25.27 ? 6   GLU B OE2 1 
ATOM   1509 N  N   . THR B 1 19  ? -3.663  15.198  46.208  1.00 14.28 ? 7   THR B N   1 
ATOM   1510 C  CA  . THR B 1 19  ? -4.883  14.522  46.666  1.00 13.51 ? 7   THR B CA  1 
ATOM   1511 C  C   . THR B 1 19  ? -5.730  15.610  47.277  1.00 13.64 ? 7   THR B C   1 
ATOM   1512 O  O   . THR B 1 19  ? -5.128  16.595  47.763  1.00 14.01 ? 7   THR B O   1 
ATOM   1513 C  CB  . THR B 1 19  ? -4.632  13.373  47.653  1.00 14.80 ? 7   THR B CB  1 
ATOM   1514 O  OG1 . THR B 1 19  ? -4.062  13.875  48.869  1.00 15.55 ? 7   THR B OG1 1 
ATOM   1515 C  CG2 . THR B 1 19  ? -3.756  12.275  47.068  1.00 14.50 ? 7   THR B CG2 1 
ATOM   1516 N  N   . GLY B 1 20  ? -7.031  15.387  47.282  1.00 14.24 ? 8   GLY B N   1 
ATOM   1517 C  CA  . GLY B 1 20  ? -7.935  16.314  47.964  1.00 13.73 ? 8   GLY B CA  1 
ATOM   1518 C  C   . GLY B 1 20  ? -9.380  15.910  47.882  1.00 14.04 ? 8   GLY B C   1 
ATOM   1519 O  O   . GLY B 1 20  ? -9.700  14.709  47.671  1.00 12.93 ? 8   GLY B O   1 
ATOM   1520 N  N   . THR B 1 21  ? -10.240 16.882  48.168  1.00 12.71 ? 9   THR B N   1 
ATOM   1521 C  CA  . THR B 1 21  ? -11.702 16.748  48.039  1.00 12.67 ? 9   THR B CA  1 
ATOM   1522 C  C   . THR B 1 21  ? -12.141 17.645  46.897  1.00 12.22 ? 9   THR B C   1 
ATOM   1523 O  O   . THR B 1 21  ? -11.647 18.787  46.833  1.00 11.32 ? 9   THR B O   1 
ATOM   1524 C  CB  . THR B 1 21  ? -12.409 17.177  49.330  1.00 13.11 ? 9   THR B CB  1 
ATOM   1525 O  OG1 . THR B 1 21  ? -11.811 16.488  50.418  1.00 15.95 ? 9   THR B OG1 1 
ATOM   1526 C  CG2 . THR B 1 21  ? -13.880 16.852  49.289  1.00 14.36 ? 9   THR B CG2 1 
ATOM   1527 N  N   . ASN B 1 22  ? -13.042 17.169  46.038  1.00 11.18 ? 10  ASN B N   1 
ATOM   1528 C  CA  . ASN B 1 22  ? -13.598 17.999  44.964  1.00 11.95 ? 10  ASN B CA  1 
ATOM   1529 C  C   . ASN B 1 22  ? -15.058 17.636  44.791  1.00 12.49 ? 10  ASN B C   1 
ATOM   1530 O  O   . ASN B 1 22  ? -15.371 16.479  44.475  1.00 13.18 ? 10  ASN B O   1 
ATOM   1531 C  CB  . ASN B 1 22  ? -12.791 17.892  43.674  1.00 12.38 ? 10  ASN B CB  1 
ATOM   1532 C  CG  . ASN B 1 22  ? -13.368 18.733  42.568  1.00 13.79 ? 10  ASN B CG  1 
ATOM   1533 O  OD1 . ASN B 1 22  ? -14.110 18.213  41.725  1.00 15.41 ? 10  ASN B OD1 1 
ATOM   1534 N  ND2 . ASN B 1 22  ? -13.086 20.037  42.576  1.00 14.34 ? 10  ASN B ND2 1 
ATOM   1535 N  N   . ASN B 1 23  ? -15.939 18.580  45.131  1.00 12.77 ? 11  ASN B N   1 
ATOM   1536 C  CA  . ASN B 1 23  ? -17.383 18.422  44.873  1.00 14.36 ? 11  ASN B CA  1 
ATOM   1537 C  C   . ASN B 1 23  ? -17.888 17.166  45.597  1.00 14.45 ? 11  ASN B C   1 
ATOM   1538 O  O   . ASN B 1 23  ? -18.753 16.440  45.057  1.00 16.85 ? 11  ASN B O   1 
ATOM   1539 C  CB  . ASN B 1 23  ? -17.605 18.490  43.363  1.00 15.31 ? 11  ASN B CB  1 
ATOM   1540 C  CG  . ASN B 1 23  ? -17.266 19.837  42.787  1.00 17.53 ? 11  ASN B CG  1 
ATOM   1541 O  OD1 . ASN B 1 23  ? -17.626 20.847  43.381  1.00 20.24 ? 11  ASN B OD1 1 
ATOM   1542 N  ND2 . ASN B 1 23  ? -16.571 19.883  41.656  1.00 20.68 ? 11  ASN B ND2 1 
ATOM   1543 N  N   . GLY B 1 24  ? -17.373 16.898  46.796  1.00 12.74 ? 12  GLY B N   1 
ATOM   1544 C  CA  . GLY B 1 24  ? -17.848 15.797  47.643  1.00 14.80 ? 12  GLY B CA  1 
ATOM   1545 C  C   . GLY B 1 24  ? -17.232 14.442  47.331  1.00 13.52 ? 12  GLY B C   1 
ATOM   1546 O  O   . GLY B 1 24  ? -17.642 13.482  47.957  1.00 16.17 ? 12  GLY B O   1 
ATOM   1547 N  N   . TYR B 1 25  ? -16.221 14.409  46.473  1.00 12.15 ? 13  TYR B N   1 
ATOM   1548 C  CA  . TYR B 1 25  ? -15.466 13.206  46.083  1.00 12.02 ? 13  TYR B CA  1 
ATOM   1549 C  C   . TYR B 1 25  ? -14.033 13.369  46.549  1.00 12.01 ? 13  TYR B C   1 
ATOM   1550 O  O   . TYR B 1 25  ? -13.439 14.446  46.388  1.00 12.38 ? 13  TYR B O   1 
ATOM   1551 C  CB  . TYR B 1 25  ? -15.531 12.984  44.569  1.00 13.51 ? 13  TYR B CB  1 
ATOM   1552 C  CG  . TYR B 1 25  ? -16.893 12.490  44.169  1.00 14.43 ? 13  TYR B CG  1 
ATOM   1553 C  CD1 . TYR B 1 25  ? -17.167 11.141  44.195  1.00 16.47 ? 13  TYR B CD1 1 
ATOM   1554 C  CD2 . TYR B 1 25  ? -17.923 13.373  43.864  1.00 15.68 ? 13  TYR B CD2 1 
ATOM   1555 C  CE1 . TYR B 1 25  ? -18.441 10.649  43.917  1.00 21.13 ? 13  TYR B CE1 1 
ATOM   1556 C  CE2 . TYR B 1 25  ? -19.190 12.898  43.554  1.00 19.58 ? 13  TYR B CE2 1 
ATOM   1557 C  CZ  . TYR B 1 25  ? -19.449 11.535  43.580  1.00 21.28 ? 13  TYR B CZ  1 
ATOM   1558 O  OH  . TYR B 1 25  ? -20.693 11.025  43.313  1.00 26.08 ? 13  TYR B OH  1 
ATOM   1559 N  N   . TYR B 1 26  ? -13.486 12.301  47.099  1.00 10.05 ? 14  TYR B N   1 
ATOM   1560 C  CA  . TYR B 1 26  ? -12.025 12.135  47.227  1.00 10.44 ? 14  TYR B CA  1 
ATOM   1561 C  C   . TYR B 1 26  ? -11.461 12.126  45.815  1.00 10.82 ? 14  TYR B C   1 
ATOM   1562 O  O   . TYR B 1 26  ? -12.060 11.449  44.939  1.00 11.21 ? 14  TYR B O   1 
ATOM   1563 C  CB  . TYR B 1 26  ? -11.680 10.853  47.972  1.00 11.73 ? 14  TYR B CB  1 
ATOM   1564 C  CG  . TYR B 1 26  ? -10.196 10.613  48.062  1.00 12.12 ? 14  TYR B CG  1 
ATOM   1565 C  CD1 . TYR B 1 26  ? -9.397  11.210  49.020  1.00 13.29 ? 14  TYR B CD1 1 
ATOM   1566 C  CD2 . TYR B 1 26  ? -9.598  9.798   47.110  1.00 13.54 ? 14  TYR B CD2 1 
ATOM   1567 C  CE1 . TYR B 1 26  ? -8.035  10.964  49.068  1.00 13.70 ? 14  TYR B CE1 1 
ATOM   1568 C  CE2 . TYR B 1 26  ? -8.242  9.581   47.126  1.00 14.22 ? 14  TYR B CE2 1 
ATOM   1569 C  CZ  . TYR B 1 26  ? -7.465  10.130  48.120  1.00 12.25 ? 14  TYR B CZ  1 
ATOM   1570 O  OH  . TYR B 1 26  ? -6.127  9.878   48.140  1.00 13.30 ? 14  TYR B OH  1 
ATOM   1571 N  N   . TYR B 1 27  ? -10.301 12.722  45.635  1.00 10.32 ? 15  TYR B N   1 
ATOM   1572 C  CA  . TYR B 1 27  ? -9.537  12.516  44.377  1.00 10.85 ? 15  TYR B CA  1 
ATOM   1573 C  C   . TYR B 1 27  ? -8.083  12.325  44.704  1.00 11.31 ? 15  TYR B C   1 
ATOM   1574 O  O   . TYR B 1 27  ? -7.598  12.785  45.720  1.00 11.44 ? 15  TYR B O   1 
ATOM   1575 C  CB  . TYR B 1 27  ? -9.723  13.628  43.341  1.00 11.67 ? 15  TYR B CB  1 
ATOM   1576 C  CG  . TYR B 1 27  ? -9.028  14.924  43.660  1.00 11.91 ? 15  TYR B CG  1 
ATOM   1577 C  CD1 . TYR B 1 27  ? -9.650  15.892  44.430  1.00 12.25 ? 15  TYR B CD1 1 
ATOM   1578 C  CD2 . TYR B 1 27  ? -7.749  15.192  43.206  1.00 12.92 ? 15  TYR B CD2 1 
ATOM   1579 C  CE1 . TYR B 1 27  ? -9.013  17.069  44.770  1.00 14.69 ? 15  TYR B CE1 1 
ATOM   1580 C  CE2 . TYR B 1 27  ? -7.112  16.383  43.499  1.00 14.67 ? 15  TYR B CE2 1 
ATOM   1581 C  CZ  . TYR B 1 27  ? -7.738  17.337  44.287  1.00 15.24 ? 15  TYR B CZ  1 
ATOM   1582 O  OH  . TYR B 1 27  ? -7.070  18.510  44.588  1.00 18.27 ? 15  TYR B OH  1 
ATOM   1583 N  N   . SER B 1 28  ? -7.441  11.512  43.867  1.00 11.53 ? 16  SER B N   1 
ATOM   1584 C  CA  . SER B 1 28  ? -5.993  11.281  43.927  1.00 13.15 ? 16  SER B CA  1 
ATOM   1585 C  C   . SER B 1 28  ? -5.471  11.349  42.509  1.00 12.04 ? 16  SER B C   1 
ATOM   1586 O  O   . SER B 1 28  ? -6.021  10.651  41.607  1.00 12.53 ? 16  SER B O   1 
ATOM   1587 C  CB  . SER B 1 28  ? -5.631  9.980   44.582  1.00 14.19 ? 16  SER B CB  1 
ATOM   1588 O  OG  . SER B 1 28  ? -4.199  9.775   44.504  1.00 14.83 ? 16  SER B OG  1 
ATOM   1589 N  N   . PHE B 1 29  ? -4.457  12.177  42.314  1.00 11.61 ? 17  PHE B N   1 
ATOM   1590 C  CA  . PHE B 1 29  ? -3.707  12.238  41.047  1.00 12.61 ? 17  PHE B CA  1 
ATOM   1591 C  C   . PHE B 1 29  ? -2.261  11.947  41.426  1.00 14.05 ? 17  PHE B C   1 
ATOM   1592 O  O   . PHE B 1 29  ? -1.699  12.682  42.240  1.00 14.69 ? 17  PHE B O   1 
ATOM   1593 C  CB  . PHE B 1 29  ? -3.843  13.590  40.375  1.00 13.46 ? 17  PHE B CB  1 
ATOM   1594 C  CG  . PHE B 1 29  ? -2.960  13.758  39.166  1.00 14.30 ? 17  PHE B CG  1 
ATOM   1595 C  CD1 . PHE B 1 29  ? -2.954  12.815  38.144  1.00 16.31 ? 17  PHE B CD1 1 
ATOM   1596 C  CD2 . PHE B 1 29  ? -2.111  14.847  39.055  1.00 18.86 ? 17  PHE B CD2 1 
ATOM   1597 C  CE1 . PHE B 1 29  ? -2.110  12.956  37.054  1.00 17.67 ? 17  PHE B CE1 1 
ATOM   1598 C  CE2 . PHE B 1 29  ? -1.280  14.997  37.948  1.00 18.74 ? 17  PHE B CE2 1 
ATOM   1599 C  CZ  . PHE B 1 29  ? -1.282  14.062  36.941  1.00 17.23 ? 17  PHE B CZ  1 
ATOM   1600 N  N   . TRP B 1 30  ? -1.695  10.873  40.886  1.00 14.02 ? 18  TRP B N   1 
ATOM   1601 C  CA  . TRP B 1 30  ? -0.303  10.495  41.204  1.00 14.76 ? 18  TRP B CA  1 
ATOM   1602 C  C   . TRP B 1 30  ? 0.421   10.350  39.877  1.00 15.36 ? 18  TRP B C   1 
ATOM   1603 O  O   . TRP B 1 30  ? -0.117  9.675   38.984  1.00 14.24 ? 18  TRP B O   1 
ATOM   1604 C  CB  . TRP B 1 30  ? -0.270  9.208   42.034  1.00 17.39 ? 18  TRP B CB  1 
ATOM   1605 C  CG  . TRP B 1 30  ? 1.121   8.776   42.354  1.00 21.00 ? 18  TRP B CG  1 
ATOM   1606 C  CD1 . TRP B 1 30  ? 1.894   9.185   43.399  1.00 25.05 ? 18  TRP B CD1 1 
ATOM   1607 C  CD2 . TRP B 1 30  ? 1.968   7.976   41.510  1.00 25.02 ? 18  TRP B CD2 1 
ATOM   1608 N  NE1 . TRP B 1 30  ? 3.154   8.642   43.291  1.00 26.69 ? 18  TRP B NE1 1 
ATOM   1609 C  CE2 . TRP B 1 30  ? 3.227   7.898   42.145  1.00 28.21 ? 18  TRP B CE2 1 
ATOM   1610 C  CE3 . TRP B 1 30  ? 1.764   7.276   40.318  1.00 27.80 ? 18  TRP B CE3 1 
ATOM   1611 C  CZ2 . TRP B 1 30  ? 4.285   7.154   41.607  1.00 28.11 ? 18  TRP B CZ2 1 
ATOM   1612 C  CZ3 . TRP B 1 30  ? 2.801   6.533   39.793  1.00 28.01 ? 18  TRP B CZ3 1 
ATOM   1613 C  CH2 . TRP B 1 30  ? 4.044   6.490   40.425  1.00 27.45 ? 18  TRP B CH2 1 
ATOM   1614 N  N   . THR B 1 31  ? 1.572   10.972  39.751  1.00 14.76 ? 19  THR B N   1 
ATOM   1615 C  CA  . THR B 1 31  ? 2.372   10.806  38.519  1.00 14.73 ? 19  THR B CA  1 
ATOM   1616 C  C   . THR B 1 31  ? 3.830   10.761  38.953  1.00 18.21 ? 19  THR B C   1 
ATOM   1617 O  O   . THR B 1 31  ? 4.206   11.489  39.905  1.00 16.10 ? 19  THR B O   1 
ATOM   1618 C  CB  . THR B 1 31  ? 2.101   11.881  37.463  1.00 16.70 ? 19  THR B CB  1 
ATOM   1619 O  OG1 . THR B 1 31  ? 2.986   11.655  36.354  1.00 20.26 ? 19  THR B OG1 1 
ATOM   1620 C  CG2 . THR B 1 31  ? 2.282   13.313  37.919  1.00 16.35 ? 19  THR B CG2 1 
ATOM   1621 N  N   . ASP B 1 32  ? 4.628   9.972   38.246  1.00 18.09 ? 20  ASP B N   1 
ATOM   1622 C  CA  . ASP B 1 32  ? 6.083   9.928   38.571  1.00 22.31 ? 20  ASP B CA  1 
ATOM   1623 C  C   . ASP B 1 32  ? 6.800   11.120  37.931  1.00 23.52 ? 20  ASP B C   1 
ATOM   1624 O  O   . ASP B 1 32  ? 8.037   11.180  38.100  1.00 23.76 ? 20  ASP B O   1 
ATOM   1625 C  CB  . ASP B 1 32  ? 6.704   8.591   38.181  1.00 21.18 ? 20  ASP B CB  1 
ATOM   1626 C  CG  . ASP B 1 32  ? 6.700   8.312   36.686  1.00 20.18 ? 20  ASP B CG  1 
ATOM   1627 O  OD1 . ASP B 1 32  ? 6.360   9.236   35.907  1.00 23.28 ? 20  ASP B OD1 1 
ATOM   1628 O  OD2 . ASP B 1 32  ? 6.988   7.159   36.329  1.00 23.90 ? 20  ASP B OD2 1 
ATOM   1629 N  N   . GLY B 1 33  ? 6.093   11.954  37.153  1.00 23.03 ? 21  GLY B N   1 
ATOM   1630 C  CA  . GLY B 1 33  ? 6.603   13.174  36.487  1.00 25.57 ? 21  GLY B CA  1 
ATOM   1631 C  C   . GLY B 1 33  ? 7.096   12.971  35.054  1.00 25.22 ? 21  GLY B C   1 
ATOM   1632 O  O   . GLY B 1 33  ? 7.570   13.949  34.452  1.00 26.62 ? 21  GLY B O   1 
ATOM   1633 N  N   . GLY B 1 34  ? 6.980   11.768  34.495  1.00 25.55 ? 22  GLY B N   1 
ATOM   1634 C  CA  . GLY B 1 34  ? 7.414   11.461  33.122  1.00 26.13 ? 22  GLY B CA  1 
ATOM   1635 C  C   . GLY B 1 34  ? 6.429   12.000  32.113  1.00 24.94 ? 22  GLY B C   1 
ATOM   1636 O  O   . GLY B 1 34  ? 5.214   11.988  32.421  1.00 24.11 ? 22  GLY B O   1 
ATOM   1637 N  N   . GLY B 1 35  ? 6.937   12.539  30.998  1.00 23.03 ? 23  GLY B N   1 
ATOM   1638 C  CA  . GLY B 1 35  ? 6.139   13.113  29.901  1.00 20.93 ? 23  GLY B CA  1 
ATOM   1639 C  C   . GLY B 1 35  ? 5.156   14.151  30.385  1.00 23.16 ? 23  GLY B C   1 
ATOM   1640 O  O   . GLY B 1 35  ? 5.509   14.975  31.253  1.00 21.00 ? 23  GLY B O   1 
ATOM   1641 N  N   . GLN B 1 36  ? 3.969   14.181  29.791  1.00 19.08 ? 24  GLN B N   1 
ATOM   1642 C  CA  . GLN B 1 36  ? 2.977   15.200  30.133  1.00 22.09 ? 24  GLN B CA  1 
ATOM   1643 C  C   . GLN B 1 36  ? 1.737   14.455  30.591  1.00 17.96 ? 24  GLN B C   1 
ATOM   1644 O  O   . GLN B 1 36  ? 1.222   13.612  29.848  1.00 16.04 ? 24  GLN B O   1 
ATOM   1645 C  CB  . GLN B 1 36  ? 2.692   16.136  28.961  1.00 26.54 ? 24  GLN B CB  1 
ATOM   1646 C  CG  . GLN B 1 36  ? 1.546   17.106  29.215  1.00 34.11 ? 24  GLN B CG  1 
ATOM   1647 C  CD  . GLN B 1 36  ? 1.968   18.475  29.690  1.00 43.50 ? 24  GLN B CD  1 
ATOM   1648 O  OE1 . GLN B 1 36  ? 3.014   18.654  30.316  1.00 50.63 ? 24  GLN B OE1 1 
ATOM   1649 N  NE2 . GLN B 1 36  ? 1.133   19.458  29.382  1.00 46.77 ? 24  GLN B NE2 1 
ATOM   1650 N  N   . VAL B 1 37  ? 1.291   14.776  31.782  1.00 18.34 ? 25  VAL B N   1 
ATOM   1651 C  CA  . VAL B 1 37  ? 0.041   14.159  32.303  1.00 15.97 ? 25  VAL B CA  1 
ATOM   1652 C  C   . VAL B 1 37  ? -0.725  15.289  32.951  1.00 15.14 ? 25  VAL B C   1 
ATOM   1653 O  O   . VAL B 1 37  ? -0.126  15.940  33.828  1.00 17.46 ? 25  VAL B O   1 
ATOM   1654 C  CB  . VAL B 1 37  ? 0.288   12.990  33.271  1.00 16.75 ? 25  VAL B CB  1 
ATOM   1655 C  CG1 . VAL B 1 37  ? -1.046  12.419  33.737  1.00 17.18 ? 25  VAL B CG1 1 
ATOM   1656 C  CG2 . VAL B 1 37  ? 1.160   11.891  32.667  1.00 18.28 ? 25  VAL B CG2 1 
ATOM   1657 N  N   . THR B 1 38  ? -1.968  15.522  32.515  1.00 14.29 ? 26  THR B N   1 
ATOM   1658 C  CA  . THR B 1 38  ? -2.761  16.684  32.962  1.00 15.06 ? 26  THR B CA  1 
ATOM   1659 C  C   . THR B 1 38  ? -4.078  16.150  33.508  1.00 14.97 ? 26  THR B C   1 
ATOM   1660 O  O   . THR B 1 38  ? -4.831  15.607  32.734  1.00 15.37 ? 26  THR B O   1 
ATOM   1661 C  CB  . THR B 1 38  ? -2.973  17.728  31.865  1.00 19.82 ? 26  THR B CB  1 
ATOM   1662 O  OG1 . THR B 1 38  ? -1.693  18.169  31.384  1.00 21.33 ? 26  THR B OG1 1 
ATOM   1663 C  CG2 . THR B 1 38  ? -3.730  18.950  32.346  1.00 22.34 ? 26  THR B CG2 1 
ATOM   1664 N  N   . TYR B 1 39  ? -4.355  16.452  34.754  1.00 13.80 ? 27  TYR B N   1 
ATOM   1665 C  CA  . TYR B 1 39  ? -5.596  16.033  35.433  1.00 13.97 ? 27  TYR B CA  1 
ATOM   1666 C  C   . TYR B 1 39  ? -6.485  17.265  35.641  1.00 14.88 ? 27  TYR B C   1 
ATOM   1667 O  O   . TYR B 1 39  ? -5.996  18.327  36.122  1.00 14.70 ? 27  TYR B O   1 
ATOM   1668 C  CB  . TYR B 1 39  ? -5.194  15.259  36.690  1.00 14.09 ? 27  TYR B CB  1 
ATOM   1669 C  CG  . TYR B 1 39  ? -6.361  14.884  37.555  1.00 13.17 ? 27  TYR B CG  1 
ATOM   1670 C  CD1 . TYR B 1 39  ? -6.854  15.754  38.495  1.00 13.23 ? 27  TYR B CD1 1 
ATOM   1671 C  CD2 . TYR B 1 39  ? -7.000  13.676  37.417  1.00 12.45 ? 27  TYR B CD2 1 
ATOM   1672 C  CE1 . TYR B 1 39  ? -7.932  15.444  39.304  1.00 14.57 ? 27  TYR B CE1 1 
ATOM   1673 C  CE2 . TYR B 1 39  ? -8.070  13.330  38.228  1.00 13.59 ? 27  TYR B CE2 1 
ATOM   1674 C  CZ  . TYR B 1 39  ? -8.538  14.218  39.173  1.00 14.33 ? 27  TYR B CZ  1 
ATOM   1675 O  OH  . TYR B 1 39  ? -9.623  13.871  39.916  1.00 13.56 ? 27  TYR B OH  1 
ATOM   1676 N  N   . THR B 1 40  ? -7.794  17.097  35.382  1.00 15.82 ? 28  THR B N   1 
ATOM   1677 C  CA  . THR B 1 40  ? -8.811  18.147  35.593  1.00 16.16 ? 28  THR B CA  1 
ATOM   1678 C  C   . THR B 1 40  ? -9.977  17.598  36.408  1.00 15.83 ? 28  THR B C   1 
ATOM   1679 O  O   . THR B 1 40  ? -10.577 16.646  35.964  1.00 17.83 ? 28  THR B O   1 
ATOM   1680 C  CB  . THR B 1 40  ? -9.245  18.695  34.236  1.00 19.46 ? 28  THR B CB  1 
ATOM   1681 O  OG1 . THR B 1 40  ? -8.058  19.156  33.559  1.00 22.26 ? 28  THR B OG1 1 
ATOM   1682 C  CG2 . THR B 1 40  ? -10.220 19.828  34.393  1.00 21.95 ? 28  THR B CG2 1 
ATOM   1683 N  N   . ASN B 1 41  ? -10.304 18.197  37.555  1.00 15.53 ? 29  ASN B N   1 
ATOM   1684 C  CA  . ASN B 1 41  ? -11.562 17.872  38.266  1.00 15.20 ? 29  ASN B CA  1 
ATOM   1685 C  C   . ASN B 1 41  ? -12.727 18.583  37.586  1.00 16.78 ? 29  ASN B C   1 
ATOM   1686 O  O   . ASN B 1 41  ? -12.630 19.823  37.308  1.00 18.17 ? 29  ASN B O   1 
ATOM   1687 C  CB  . ASN B 1 41  ? -11.508 18.253  39.742  1.00 15.21 ? 29  ASN B CB  1 
ATOM   1688 C  CG  . ASN B 1 41  ? -10.747 17.256  40.591  1.00 14.64 ? 29  ASN B CG  1 
ATOM   1689 O  OD1 . ASN B 1 41  ? -10.885 16.048  40.400  1.00 16.81 ? 29  ASN B OD1 1 
ATOM   1690 N  ND2 . ASN B 1 41  ? -9.902  17.771  41.486  1.00 15.96 ? 29  ASN B ND2 1 
ATOM   1691 N  N   . GLY B 1 42  ? -13.790 17.844  37.345  1.00 14.49 ? 30  GLY B N   1 
ATOM   1692 C  CA  . GLY B 1 42  ? -15.049 18.374  36.816  1.00 15.28 ? 30  GLY B CA  1 
ATOM   1693 C  C   . GLY B 1 42  ? -16.111 18.410  37.902  1.00 16.89 ? 30  GLY B C   1 
ATOM   1694 O  O   . GLY B 1 42  ? -15.864 18.089  39.070  1.00 14.99 ? 30  GLY B O   1 
ATOM   1695 N  N   . PRO B 1 43  ? -17.334 18.820  37.543  1.00 20.12 ? 31  PRO B N   1 
ATOM   1696 C  CA  . PRO B 1 43  ? -18.427 18.841  38.514  1.00 20.75 ? 31  PRO B CA  1 
ATOM   1697 C  C   . PRO B 1 43  ? -18.758 17.457  39.072  1.00 18.57 ? 31  PRO B C   1 
ATOM   1698 O  O   . PRO B 1 43  ? -18.594 16.396  38.374  1.00 16.61 ? 31  PRO B O   1 
ATOM   1699 C  CB  . PRO B 1 43  ? -19.597 19.420  37.707  1.00 23.50 ? 31  PRO B CB  1 
ATOM   1700 C  CG  . PRO B 1 43  ? -18.943 20.167  36.563  1.00 26.13 ? 31  PRO B CG  1 
ATOM   1701 C  CD  . PRO B 1 43  ? -17.722 19.348  36.217  1.00 22.89 ? 31  PRO B CD  1 
ATOM   1702 N  N   . ALA B 1 44  ? -19.272 17.424  40.302  1.00 17.78 ? 32  ALA B N   1 
ATOM   1703 C  CA  . ALA B 1 44  ? -19.732 16.190  40.968  1.00 16.90 ? 32  ALA B CA  1 
ATOM   1704 C  C   . ALA B 1 44  ? -18.631 15.121  40.834  1.00 16.81 ? 32  ALA B C   1 
ATOM   1705 O  O   . ALA B 1 44  ? -17.497 15.413  41.264  1.00 15.90 ? 32  ALA B O   1 
ATOM   1706 C  CB  . ALA B 1 44  ? -21.079 15.786  40.425  1.00 17.36 ? 32  ALA B CB  1 
ATOM   1707 N  N   . GLY B 1 45  ? -18.937 13.927  40.337  1.00 14.61 ? 33  GLY B N   1 
ATOM   1708 C  CA  . GLY B 1 45  ? -17.956 12.835  40.329  1.00 14.03 ? 33  GLY B CA  1 
ATOM   1709 C  C   . GLY B 1 45  ? -17.088 12.794  39.080  1.00 13.32 ? 33  GLY B C   1 
ATOM   1710 O  O   . GLY B 1 45  ? -16.498 11.709  38.826  1.00 13.77 ? 33  GLY B O   1 
ATOM   1711 N  N   . GLN B 1 46  ? -17.004 13.879  38.319  1.00 14.05 ? 34  GLN B N   1 
ATOM   1712 C  CA  . GLN B 1 46  ? -16.282 13.865  37.010  1.00 15.10 ? 34  GLN B CA  1 
ATOM   1713 C  C   . GLN B 1 46  ? -14.802 14.185  37.191  1.00 12.15 ? 34  GLN B C   1 
ATOM   1714 O  O   . GLN B 1 46  ? -14.428 15.065  37.981  1.00 12.35 ? 34  GLN B O   1 
ATOM   1715 C  CB  . GLN B 1 46  ? -16.910 14.864  36.013  1.00 16.90 ? 34  GLN B CB  1 
ATOM   1716 C  CG  . GLN B 1 46  ? -16.537 14.590  34.559  1.00 19.69 ? 34  GLN B CG  1 
ATOM   1717 C  CD  . GLN B 1 46  ? -15.301 15.275  34.030  1.00 21.77 ? 34  GLN B CD  1 
ATOM   1718 O  OE1 . GLN B 1 46  ? -14.904 15.099  32.862  1.00 27.17 ? 34  GLN B OE1 1 
ATOM   1719 N  NE2 . GLN B 1 46  ? -14.660 16.084  34.848  1.00 23.14 ? 34  GLN B NE2 1 
ATOM   1720 N  N   . TYR B 1 47  ? -13.959 13.534  36.392  1.00 11.36 ? 35  TYR B N   1 
ATOM   1721 C  CA  . TYR B 1 47  ? -12.587 13.984  36.163  1.00 11.38 ? 35  TYR B CA  1 
ATOM   1722 C  C   . TYR B 1 47  ? -12.188 13.624  34.750  1.00 11.42 ? 35  TYR B C   1 
ATOM   1723 O  O   . TYR B 1 47  ? -12.806 12.787  34.110  1.00 11.70 ? 35  TYR B O   1 
ATOM   1724 C  CB  . TYR B 1 47  ? -11.625 13.340  37.162  1.00 12.33 ? 35  TYR B CB  1 
ATOM   1725 C  CG  . TYR B 1 47  ? -11.406 11.860  36.959  1.00 11.53 ? 35  TYR B CG  1 
ATOM   1726 C  CD1 . TYR B 1 47  ? -12.198 10.900  37.574  1.00 10.81 ? 35  TYR B CD1 1 
ATOM   1727 C  CD2 . TYR B 1 47  ? -10.344 11.393  36.185  1.00 11.36 ? 35  TYR B CD2 1 
ATOM   1728 C  CE1 . TYR B 1 47  ? -12.008 9.538   37.347  1.00 11.65 ? 35  TYR B CE1 1 
ATOM   1729 C  CE2 . TYR B 1 47  ? -10.102 10.031  36.011  1.00 12.09 ? 35  TYR B CE2 1 
ATOM   1730 C  CZ  . TYR B 1 47  ? -10.908 9.097   36.627  1.00 11.95 ? 35  TYR B CZ  1 
ATOM   1731 O  OH  . TYR B 1 47  ? -10.704 7.754   36.445  1.00 12.93 ? 35  TYR B OH  1 
ATOM   1732 N  N   . SER B 1 48  ? -11.156 14.295  34.297  1.00 12.06 ? 36  SER B N   1 
ATOM   1733 C  CA  . SER B 1 48  ? -10.554 14.070  32.974  1.00 12.96 ? 36  SER B CA  1 
ATOM   1734 C  C   . SER B 1 48  ? -9.064  13.938  33.153  1.00 12.54 ? 36  SER B C   1 
ATOM   1735 O  O   . SER B 1 48  ? -8.509  14.542  34.066  1.00 13.52 ? 36  SER B O   1 
ATOM   1736 C  CB  . SER B 1 48  ? -10.846 15.204  32.052  1.00 15.91 ? 36  SER B CB  1 
ATOM   1737 O  OG  . SER B 1 48  ? -12.240 15.230  31.776  1.00 22.57 ? 36  SER B OG  1 
ATOM   1738 N  N   . VAL B 1 49  ? -8.417  13.189  32.279  1.00 12.44 ? 37  VAL B N   1 
ATOM   1739 C  CA  . VAL B 1 49  ? -6.939  13.142  32.303  1.00 15.26 ? 37  VAL B CA  1 
ATOM   1740 C  C   . VAL B 1 49  ? -6.515  13.007  30.860  1.00 17.34 ? 37  VAL B C   1 
ATOM   1741 O  O   . VAL B 1 49  ? -7.249  12.361  30.041  1.00 15.52 ? 37  VAL B O   1 
ATOM   1742 C  CB  . VAL B 1 49  ? -6.367  12.057  33.243  1.00 16.96 ? 37  VAL B CB  1 
ATOM   1743 C  CG1 . VAL B 1 49  ? -6.943  10.671  33.042  1.00 18.47 ? 37  VAL B CG1 1 
ATOM   1744 C  CG2 . VAL B 1 49  ? -4.845  12.041  33.225  1.00 18.19 ? 37  VAL B CG2 1 
ATOM   1745 N  N   . GLU B 1 50  ? -5.452  13.728  30.533  1.00 16.45 ? 38  GLU B N   1 
ATOM   1746 C  CA  . GLU B 1 50  ? -4.926  13.781  29.165  1.00 18.92 ? 38  GLU B CA  1 
ATOM   1747 C  C   . GLU B 1 50  ? -3.464  13.465  29.327  1.00 17.52 ? 38  GLU B C   1 
ATOM   1748 O  O   . GLU B 1 50  ? -2.873  14.131  30.181  1.00 16.66 ? 38  GLU B O   1 
ATOM   1749 C  CB  . GLU B 1 50  ? -5.169  15.172  28.584  1.00 24.09 ? 38  GLU B CB  1 
ATOM   1750 C  CG  . GLU B 1 50  ? -6.448  15.304  27.798  1.00 34.60 ? 38  GLU B CG  1 
ATOM   1751 C  CD  . GLU B 1 50  ? -6.143  15.841  26.413  1.00 39.39 ? 38  GLU B CD  1 
ATOM   1752 O  OE1 . GLU B 1 50  ? -6.873  15.481  25.461  1.00 48.48 ? 38  GLU B OE1 1 
ATOM   1753 O  OE2 . GLU B 1 50  ? -5.140  16.609  26.293  1.00 36.39 ? 38  GLU B OE2 1 
ATOM   1754 N  N   . TRP B 1 51  ? -2.890  12.519  28.570  1.00 14.21 ? 39  TRP B N   1 
ATOM   1755 C  CA  . TRP B 1 51  ? -1.447  12.264  28.754  1.00 14.04 ? 39  TRP B CA  1 
ATOM   1756 C  C   . TRP B 1 51  ? -0.739  12.003  27.435  1.00 13.96 ? 39  TRP B C   1 
ATOM   1757 O  O   . TRP B 1 51  ? -1.400  11.619  26.472  1.00 13.54 ? 39  TRP B O   1 
ATOM   1758 C  CB  . TRP B 1 51  ? -1.224  11.128  29.725  1.00 14.28 ? 39  TRP B CB  1 
ATOM   1759 C  CG  . TRP B 1 51  ? -1.720  9.765   29.326  1.00 13.75 ? 39  TRP B CG  1 
ATOM   1760 C  CD1 . TRP B 1 51  ? -0.909  8.750   28.907  1.00 14.78 ? 39  TRP B CD1 1 
ATOM   1761 C  CD2 . TRP B 1 51  ? -3.051  9.200   29.411  1.00 14.31 ? 39  TRP B CD2 1 
ATOM   1762 N  NE1 . TRP B 1 51  ? -1.629  7.609   28.712  1.00 13.36 ? 39  TRP B NE1 1 
ATOM   1763 C  CE2 . TRP B 1 51  ? -2.936  7.845   29.020  1.00 15.21 ? 39  TRP B CE2 1 
ATOM   1764 C  CE3 . TRP B 1 51  ? -4.314  9.677   29.802  1.00 14.44 ? 39  TRP B CE3 1 
ATOM   1765 C  CZ2 . TRP B 1 51  ? -4.013  6.963   29.017  1.00 14.73 ? 39  TRP B CZ2 1 
ATOM   1766 C  CZ3 . TRP B 1 51  ? -5.387  8.808   29.777  1.00 13.88 ? 39  TRP B CZ3 1 
ATOM   1767 C  CH2 . TRP B 1 51  ? -5.242  7.477   29.370  1.00 14.58 ? 39  TRP B CH2 1 
ATOM   1768 N  N   . SER B 1 52  ? 0.565   12.262  27.433  1.00 15.94 ? 40  SER B N   1 
ATOM   1769 C  CA  . SER B 1 52  ? 1.415   12.194  26.211  1.00 16.94 ? 40  SER B CA  1 
ATOM   1770 C  C   . SER B 1 52  ? 2.775   11.672  26.665  1.00 15.69 ? 40  SER B C   1 
ATOM   1771 O  O   . SER B 1 52  ? 3.397   12.311  27.521  1.00 18.34 ? 40  SER B O   1 
ATOM   1772 C  CB  . SER B 1 52  ? 1.458   13.549  25.505  1.00 20.06 ? 40  SER B CB  1 
ATOM   1773 O  OG  . SER B 1 52  ? 2.375   13.525  24.427  1.00 27.86 ? 40  SER B OG  1 
ATOM   1774 N  N   . ASN B 1 53  ? 3.165   10.486  26.197  1.00 15.63 ? 41  ASN B N   1 
ATOM   1775 C  CA  . ASN B 1 53  ? 4.503   9.925   26.499  1.00 17.42 ? 41  ASN B CA  1 
ATOM   1776 C  C   . ASN B 1 53  ? 4.754   9.905   28.003  1.00 16.32 ? 41  ASN B C   1 
ATOM   1777 O  O   . ASN B 1 53  ? 5.854   10.272  28.471  1.00 17.34 ? 41  ASN B O   1 
ATOM   1778 C  CB  . ASN B 1 53  ? 5.545   10.721  25.723  1.00 18.72 ? 41  ASN B CB  1 
ATOM   1779 C  CG  . ASN B 1 53  ? 5.390   10.525  24.241  1.00 17.94 ? 41  ASN B CG  1 
ATOM   1780 O  OD1 . ASN B 1 53  ? 5.358   9.383   23.784  1.00 17.62 ? 41  ASN B OD1 1 
ATOM   1781 N  ND2 . ASN B 1 53  ? 5.297   11.626  23.508  1.00 20.64 ? 41  ASN B ND2 1 
ATOM   1782 N  N   . SER B 1 54  ? 3.784   9.402   28.751  1.00 16.93 ? 42  SER B N   1 
ATOM   1783 C  CA  . SER B 1 54  ? 3.753   9.419   30.230  1.00 16.74 ? 42  SER B CA  1 
ATOM   1784 C  C   . SER B 1 54  ? 4.817   8.497   30.820  1.00 17.43 ? 42  SER B C   1 
ATOM   1785 O  O   . SER B 1 54  ? 5.194   7.475   30.203  1.00 17.54 ? 42  SER B O   1 
ATOM   1786 C  CB  . SER B 1 54  ? 2.379   9.018   30.732  1.00 15.60 ? 42  SER B CB  1 
ATOM   1787 O  OG  . SER B 1 54  ? 2.144   7.614   30.579  1.00 17.90 ? 42  SER B OG  1 
ATOM   1788 N  N   . GLY B 1 55  ? 5.229   8.783   32.054  1.00 16.60 ? 43  GLY B N   1 
ATOM   1789 C  CA  . GLY B 1 55  ? 5.767   7.749   32.935  1.00 17.25 ? 43  GLY B CA  1 
ATOM   1790 C  C   . GLY B 1 55  ? 4.594   6.983   33.513  1.00 20.23 ? 43  GLY B C   1 
ATOM   1791 O  O   . GLY B 1 55  ? 3.565   6.842   32.774  1.00 21.13 ? 43  GLY B O   1 
ATOM   1792 N  N   . ASN B 1 56  ? 4.666   6.601   34.779  1.00 18.09 ? 44  ASN B N   1 
ATOM   1793 C  CA  . ASN B 1 56  ? 3.547   5.910   35.469  1.00 17.27 ? 44  ASN B CA  1 
ATOM   1794 C  C   . ASN B 1 56  ? 2.614   6.992   36.048  1.00 14.52 ? 44  ASN B C   1 
ATOM   1795 O  O   . ASN B 1 56  ? 3.094   7.954   36.634  1.00 14.63 ? 44  ASN B O   1 
ATOM   1796 C  CB  . ASN B 1 56  ? 4.011   4.980   36.603  1.00 20.38 ? 44  ASN B CB  1 
ATOM   1797 C  CG  . ASN B 1 56  ? 4.315   3.547   36.210  1.00 29.89 ? 44  ASN B CG  1 
ATOM   1798 O  OD1 . ASN B 1 56  ? 5.428   3.061   36.443  1.00 34.98 ? 44  ASN B OD1 1 
ATOM   1799 N  ND2 . ASN B 1 56  ? 3.327   2.852   35.664  1.00 35.61 ? 44  ASN B ND2 1 
ATOM   1800 N  N   . PHE B 1 57  ? 1.298   6.842   35.909  1.00 12.24 ? 45  PHE B N   1 
ATOM   1801 C  CA  . PHE B 1 57  ? 0.378   7.706   36.670  1.00 12.84 ? 45  PHE B CA  1 
ATOM   1802 C  C   . PHE B 1 57  ? -0.831  6.871   37.041  1.00 12.26 ? 45  PHE B C   1 
ATOM   1803 O  O   . PHE B 1 57  ? -1.175  5.931   36.334  1.00 11.23 ? 45  PHE B O   1 
ATOM   1804 C  CB  . PHE B 1 57  ? -0.045  8.942   35.869  1.00 12.88 ? 45  PHE B CB  1 
ATOM   1805 C  CG  . PHE B 1 57  ? -0.994  8.642   34.736  1.00 13.76 ? 45  PHE B CG  1 
ATOM   1806 C  CD1 . PHE B 1 57  ? -0.503  8.244   33.504  1.00 14.19 ? 45  PHE B CD1 1 
ATOM   1807 C  CD2 . PHE B 1 57  ? -2.367  8.682   34.920  1.00 14.79 ? 45  PHE B CD2 1 
ATOM   1808 C  CE1 . PHE B 1 57  ? -1.368  7.956   32.454  1.00 16.76 ? 45  PHE B CE1 1 
ATOM   1809 C  CE2 . PHE B 1 57  ? -3.231  8.338   33.892  1.00 14.45 ? 45  PHE B CE2 1 
ATOM   1810 C  CZ  . PHE B 1 57  ? -2.725  8.038   32.647  1.00 14.79 ? 45  PHE B CZ  1 
ATOM   1811 N  N   . VAL B 1 58  ? -1.558  7.355   38.048  1.00 12.29 ? 46  VAL B N   1 
ATOM   1812 C  CA  . VAL B 1 58  ? -2.834  6.759   38.480  1.00 13.81 ? 46  VAL B CA  1 
ATOM   1813 C  C   . VAL B 1 58  ? -3.689  7.941   38.927  1.00 12.78 ? 46  VAL B C   1 
ATOM   1814 O  O   . VAL B 1 58  ? -3.216  8.742   39.771  1.00 14.50 ? 46  VAL B O   1 
ATOM   1815 C  CB  . VAL B 1 58  ? -2.660  5.738   39.626  1.00 15.50 ? 46  VAL B CB  1 
ATOM   1816 C  CG1 . VAL B 1 58  ? -4.001  5.125   40.019  1.00 16.93 ? 46  VAL B CG1 1 
ATOM   1817 C  CG2 . VAL B 1 58  ? -1.673  4.639   39.285  1.00 17.06 ? 46  VAL B CG2 1 
ATOM   1818 N  N   . ALA B 1 59  ? -4.923  8.036   38.440  1.00 11.95 ? 47  ALA B N   1 
ATOM   1819 C  CA  . ALA B 1 59  ? -5.769  9.221   38.673  1.00 12.51 ? 47  ALA B CA  1 
ATOM   1820 C  C   . ALA B 1 59  ? -7.231  8.857   38.804  1.00 11.04 ? 47  ALA B C   1 
ATOM   1821 O  O   . ALA B 1 59  ? -7.734  8.065   38.003  1.00 10.64 ? 47  ALA B O   1 
ATOM   1822 C  CB  . ALA B 1 59  ? -5.634  10.197  37.556  1.00 13.55 ? 47  ALA B CB  1 
ATOM   1823 N  N   . GLY B 1 60  ? -7.908  9.446   39.771  1.00 10.01 ? 48  GLY B N   1 
ATOM   1824 C  CA  . GLY B 1 60  ? -9.350  9.228   39.796  1.00 9.88  ? 48  GLY B CA  1 
ATOM   1825 C  C   . GLY B 1 60  ? -10.063 9.771   41.020  1.00 10.06 ? 48  GLY B C   1 
ATOM   1826 O  O   . GLY B 1 60  ? -9.437  10.390  41.901  1.00 10.19 ? 48  GLY B O   1 
ATOM   1827 N  N   . LYS B 1 61  ? -11.359 9.540   41.022  1.00 10.95 ? 49  LYS B N   1 
ATOM   1828 C  CA  . LYS B 1 61  ? -12.301 10.084  42.040  1.00 10.76 ? 49  LYS B CA  1 
ATOM   1829 C  C   . LYS B 1 61  ? -13.025 8.929   42.712  1.00 9.93  ? 49  LYS B C   1 
ATOM   1830 O  O   . LYS B 1 61  ? -13.259 7.857   42.086  1.00 10.69 ? 49  LYS B O   1 
ATOM   1831 C  CB  . LYS B 1 61  ? -13.374 11.027  41.467  1.00 10.73 ? 49  LYS B CB  1 
ATOM   1832 C  CG  . LYS B 1 61  ? -13.028 12.500  41.465  1.00 11.91 ? 49  LYS B CG  1 
ATOM   1833 C  CD  . LYS B 1 61  ? -14.133 13.397  40.984  1.00 12.70 ? 49  LYS B CD  1 
ATOM   1834 C  CE  . LYS B 1 61  ? -13.867 14.867  41.290  1.00 13.31 ? 49  LYS B CE  1 
ATOM   1835 N  NZ  . LYS B 1 61  ? -14.823 15.759  40.608  1.00 14.36 ? 49  LYS B NZ  1 
ATOM   1836 N  N   . GLY B 1 62  ? -13.393 9.156   43.969  1.00 10.52 ? 50  GLY B N   1 
ATOM   1837 C  CA  . GLY B 1 62  ? -14.206 8.213   44.711  1.00 9.99  ? 50  GLY B CA  1 
ATOM   1838 C  C   . GLY B 1 62  ? -14.424 8.641   46.142  1.00 11.00 ? 50  GLY B C   1 
ATOM   1839 O  O   . GLY B 1 62  ? -14.903 9.758   46.389  1.00 10.93 ? 50  GLY B O   1 
ATOM   1840 N  N   . TRP B 1 63  ? -14.052 7.749   47.064  1.00 12.19 ? 51  TRP B N   1 
ATOM   1841 C  CA  . TRP B 1 63  ? -14.492 7.796   48.480  1.00 13.04 ? 51  TRP B CA  1 
ATOM   1842 C  C   . TRP B 1 63  ? -13.294 7.617   49.403  1.00 12.43 ? 51  TRP B C   1 
ATOM   1843 O  O   . TRP B 1 63  ? -12.384 6.843   49.094  1.00 12.58 ? 51  TRP B O   1 
ATOM   1844 C  CB  . TRP B 1 63  ? -15.529 6.717   48.746  1.00 15.29 ? 51  TRP B CB  1 
ATOM   1845 C  CG  . TRP B 1 63  ? -16.695 6.851   47.817  1.00 16.86 ? 51  TRP B CG  1 
ATOM   1846 C  CD1 . TRP B 1 63  ? -17.808 7.631   47.981  1.00 20.58 ? 51  TRP B CD1 1 
ATOM   1847 C  CD2 . TRP B 1 63  ? -16.761 6.324   46.489  1.00 18.93 ? 51  TRP B CD2 1 
ATOM   1848 N  NE1 . TRP B 1 63  ? -18.611 7.533   46.873  1.00 20.73 ? 51  TRP B NE1 1 
ATOM   1849 C  CE2 . TRP B 1 63  ? -17.970 6.787   45.920  1.00 22.17 ? 51  TRP B CE2 1 
ATOM   1850 C  CE3 . TRP B 1 63  ? -15.936 5.476   45.745  1.00 19.39 ? 51  TRP B CE3 1 
ATOM   1851 C  CZ2 . TRP B 1 63  ? -18.363 6.409   44.629  1.00 22.84 ? 51  TRP B CZ2 1 
ATOM   1852 C  CZ3 . TRP B 1 63  ? -16.301 5.135   44.461  1.00 21.21 ? 51  TRP B CZ3 1 
ATOM   1853 C  CH2 . TRP B 1 63  ? -17.513 5.579   43.926  1.00 21.39 ? 51  TRP B CH2 1 
ATOM   1854 N  N   . ASN B 1 64  ? -13.349 8.277   50.544  1.00 12.19 ? 52  ASN B N   1 
ATOM   1855 C  CA  . ASN B 1 64  ? -12.463 7.942   51.661  1.00 12.85 ? 52  ASN B CA  1 
ATOM   1856 C  C   . ASN B 1 64  ? -13.216 8.046   52.977  1.00 13.76 ? 52  ASN B C   1 
ATOM   1857 O  O   . ASN B 1 64  ? -13.684 9.138   53.309  1.00 14.25 ? 52  ASN B O   1 
ATOM   1858 C  CB  . ASN B 1 64  ? -11.249 8.849   51.667  1.00 13.41 ? 52  ASN B CB  1 
ATOM   1859 C  CG  . ASN B 1 64  ? -10.127 8.264   52.486  1.00 13.75 ? 52  ASN B CG  1 
ATOM   1860 O  OD1 . ASN B 1 64  ? -10.198 7.093   52.909  1.00 14.40 ? 52  ASN B OD1 1 
ATOM   1861 N  ND2 . ASN B 1 64  ? -9.069  9.056   52.640  1.00 16.78 ? 52  ASN B ND2 1 
ATOM   1862 N  N   . PRO B 1 65  ? -13.328 6.961   53.770  1.00 14.69 ? 53  PRO B N   1 
ATOM   1863 C  CA  . PRO B 1 65  ? -12.855 5.625   53.418  1.00 14.96 ? 53  PRO B CA  1 
ATOM   1864 C  C   . PRO B 1 65  ? -13.766 4.964   52.364  1.00 15.44 ? 53  PRO B C   1 
ATOM   1865 O  O   . PRO B 1 65  ? -14.961 5.309   52.235  1.00 13.25 ? 53  PRO B O   1 
ATOM   1866 C  CB  . PRO B 1 65  ? -12.877 4.890   54.766  1.00 16.59 ? 53  PRO B CB  1 
ATOM   1867 C  CG  . PRO B 1 65  ? -14.020 5.518   55.501  1.00 17.95 ? 53  PRO B CG  1 
ATOM   1868 C  CD  . PRO B 1 65  ? -13.974 6.981   55.108  1.00 16.62 ? 53  PRO B CD  1 
ATOM   1869 N  N   . GLY B 1 66  ? -13.224 3.996   51.609  1.00 15.46 ? 54  GLY B N   1 
ATOM   1870 C  CA  . GLY B 1 66  ? -14.064 3.004   50.910  1.00 16.47 ? 54  GLY B CA  1 
ATOM   1871 C  C   . GLY B 1 66  ? -14.839 2.173   51.932  1.00 19.59 ? 54  GLY B C   1 
ATOM   1872 O  O   . GLY B 1 66  ? -14.358 1.948   53.016  1.00 22.67 ? 54  GLY B O   1 
ATOM   1873 N  N   . SER B 1 67  ? -16.078 1.844   51.648  1.00 23.26 ? 55  SER B N   1 
ATOM   1874 C  CA  . SER B 1 67  ? -16.915 0.993   52.542  1.00 24.07 ? 55  SER B CA  1 
ATOM   1875 C  C   . SER B 1 67  ? -17.563 -0.114  51.716  1.00 26.30 ? 55  SER B C   1 
ATOM   1876 O  O   . SER B 1 67  ? -18.725 -0.463  51.991  1.00 25.00 ? 55  SER B O   1 
ATOM   1877 C  CB  . SER B 1 67  ? -17.932 1.806   53.288  1.00 27.91 ? 55  SER B CB  1 
ATOM   1878 O  OG  . SER B 1 67  ? -18.769 2.475   52.368  1.00 30.95 ? 55  SER B OG  1 
ATOM   1879 N  N   . SER B 1 68  ? -16.831 -0.660  50.743  1.00 22.04 ? 56  SER B N   1 
ATOM   1880 C  CA  . SER B 1 68  ? -17.276 -1.844  49.965  1.00 23.87 ? 56  SER B CA  1 
ATOM   1881 C  C   . SER B 1 68  ? -18.585 -1.523  49.236  1.00 24.36 ? 56  SER B C   1 
ATOM   1882 O  O   . SER B 1 68  ? -19.444 -2.400  49.115  1.00 25.50 ? 56  SER B O   1 
ATOM   1883 C  CB  . SER B 1 68  ? -17.422 -3.053  50.836  1.00 26.33 ? 56  SER B CB  1 
ATOM   1884 O  OG  . SER B 1 68  ? -16.202 -3.331  51.524  1.00 26.62 ? 56  SER B OG  1 
ATOM   1885 N  N   . GLN B 1 69  ? -18.716 -0.300  48.732  1.00 24.08 ? 57  GLN B N   1 
ATOM   1886 C  CA  . GLN B 1 69  ? -19.979 0.112   48.096  1.00 26.41 ? 57  GLN B CA  1 
ATOM   1887 C  C   . GLN B 1 69  ? -20.040 -0.470  46.697  1.00 22.67 ? 57  GLN B C   1 
ATOM   1888 O  O   . GLN B 1 69  ? -18.984 -0.774  46.091  1.00 21.07 ? 57  GLN B O   1 
ATOM   1889 C  CB  . GLN B 1 69  ? -20.179 1.626   48.047  1.00 30.51 ? 57  GLN B CB  1 
ATOM   1890 C  CG  . GLN B 1 69  ? -18.991 2.430   47.572  1.00 31.04 ? 57  GLN B CG  1 
ATOM   1891 C  CD  . GLN B 1 69  ? -18.350 3.103   48.758  1.00 33.72 ? 57  GLN B CD  1 
ATOM   1892 O  OE1 . GLN B 1 69  ? -18.661 4.248   49.109  1.00 34.44 ? 57  GLN B OE1 1 
ATOM   1893 N  NE2 . GLN B 1 69  ? -17.503 2.343   49.428  1.00 26.20 ? 57  GLN B NE2 1 
ATOM   1894 N  N   . THR B 1 70  ? -21.253 -0.550  46.179  1.00 19.07 ? 58  THR B N   1 
ATOM   1895 C  CA  . THR B 1 70  ? -21.499 -0.852  44.766  1.00 20.29 ? 58  THR B CA  1 
ATOM   1896 C  C   . THR B 1 70  ? -21.321 0.455   43.973  1.00 21.30 ? 58  THR B C   1 
ATOM   1897 O  O   . THR B 1 70  ? -22.071 1.406   44.199  1.00 26.49 ? 58  THR B O   1 
ATOM   1898 C  CB  . THR B 1 70  ? -22.868 -1.529  44.606  1.00 22.65 ? 58  THR B CB  1 
ATOM   1899 O  OG1 . THR B 1 70  ? -22.821 -2.797  45.262  1.00 21.33 ? 58  THR B OG1 1 
ATOM   1900 C  CG2 . THR B 1 70  ? -23.203 -1.777  43.158  1.00 23.47 ? 58  THR B CG2 1 
ATOM   1901 N  N   . ILE B 1 71  ? -20.348 0.490   43.075  1.00 20.19 ? 59  ILE B N   1 
ATOM   1902 C  CA  . ILE B 1 71  ? -19.923 1.705   42.318  1.00 19.81 ? 59  ILE B CA  1 
ATOM   1903 C  C   . ILE B 1 71  ? -20.634 1.684   40.985  1.00 21.89 ? 59  ILE B C   1 
ATOM   1904 O  O   . ILE B 1 71  ? -20.659 0.612   40.367  1.00 20.13 ? 59  ILE B O   1 
ATOM   1905 C  CB  . ILE B 1 71  ? -18.392 1.653   42.083  1.00 22.89 ? 59  ILE B CB  1 
ATOM   1906 C  CG1 . ILE B 1 71  ? -17.650 1.567   43.406  1.00 26.28 ? 59  ILE B CG1 1 
ATOM   1907 C  CG2 . ILE B 1 71  ? -17.874 2.786   41.206  1.00 24.01 ? 59  ILE B CG2 1 
ATOM   1908 C  CD1 . ILE B 1 71  ? -18.305 2.355   44.490  1.00 28.21 ? 59  ILE B CD1 1 
ATOM   1909 N  N   . THR B 1 72  ? -21.097 2.842   40.527  1.00 20.93 ? 60  THR B N   1 
ATOM   1910 C  CA  . THR B 1 72  ? -21.495 3.018   39.124  1.00 22.08 ? 60  THR B CA  1 
ATOM   1911 C  C   . THR B 1 72  ? -20.666 4.164   38.568  1.00 17.73 ? 60  THR B C   1 
ATOM   1912 O  O   . THR B 1 72  ? -20.375 5.093   39.297  1.00 18.84 ? 60  THR B O   1 
ATOM   1913 C  CB  . THR B 1 72  ? -23.012 3.183   39.003  1.00 25.64 ? 60  THR B CB  1 
ATOM   1914 O  OG1 . THR B 1 72  ? -23.380 4.275   39.837  1.00 33.74 ? 60  THR B OG1 1 
ATOM   1915 C  CG2 . THR B 1 72  ? -23.759 1.946   39.432  1.00 28.18 ? 60  THR B CG2 1 
ATOM   1916 N  N   . TYR B 1 73  ? -20.262 4.049   37.324  1.00 16.66 ? 61  TYR B N   1 
ATOM   1917 C  CA  . TYR B 1 73  ? -19.486 5.090   36.641  1.00 17.50 ? 61  TYR B CA  1 
ATOM   1918 C  C   . TYR B 1 73  ? -19.798 5.016   35.152  1.00 17.29 ? 61  TYR B C   1 
ATOM   1919 O  O   . TYR B 1 73  ? -20.300 3.977   34.644  1.00 18.25 ? 61  TYR B O   1 
ATOM   1920 C  CB  . TYR B 1 73  ? -17.999 4.904   36.996  1.00 18.91 ? 61  TYR B CB  1 
ATOM   1921 C  CG  . TYR B 1 73  ? -17.334 3.791   36.238  1.00 18.68 ? 61  TYR B CG  1 
ATOM   1922 C  CD1 . TYR B 1 73  ? -17.372 2.481   36.673  1.00 20.58 ? 61  TYR B CD1 1 
ATOM   1923 C  CD2 . TYR B 1 73  ? -16.740 4.048   35.013  1.00 20.92 ? 61  TYR B CD2 1 
ATOM   1924 C  CE1 . TYR B 1 73  ? -16.857 1.442   35.923  1.00 22.58 ? 61  TYR B CE1 1 
ATOM   1925 C  CE2 . TYR B 1 73  ? -16.172 3.032   34.275  1.00 20.62 ? 61  TYR B CE2 1 
ATOM   1926 C  CZ  . TYR B 1 73  ? -16.237 1.729   34.721  1.00 20.91 ? 61  TYR B CZ  1 
ATOM   1927 O  OH  . TYR B 1 73  ? -15.684 0.730   34.004  1.00 22.09 ? 61  TYR B OH  1 
ATOM   1928 N  N   . SER B 1 74  ? -19.541 6.132   34.483  1.00 18.65 ? 62  SER B N   1 
ATOM   1929 C  CA  . SER B 1 74  ? -19.795 6.308   33.042  1.00 18.16 ? 62  SER B CA  1 
ATOM   1930 C  C   . SER B 1 74  ? -18.606 7.051   32.462  1.00 16.18 ? 62  SER B C   1 
ATOM   1931 O  O   . SER B 1 74  ? -17.706 7.500   33.227  1.00 13.77 ? 62  SER B O   1 
ATOM   1932 C  CB  . SER B 1 74  ? -21.083 7.034   32.789  1.00 20.38 ? 62  SER B CB  1 
ATOM   1933 O  OG  . SER B 1 74  ? -21.078 8.339   33.357  1.00 24.40 ? 62  SER B OG  1 
ATOM   1934 N  N   . GLY B 1 75  ? -18.602 7.151   31.152  1.00 14.94 ? 63  GLY B N   1 
ATOM   1935 C  CA  . GLY B 1 75  ? -17.666 8.020   30.443  1.00 14.29 ? 63  GLY B CA  1 
ATOM   1936 C  C   . GLY B 1 75  ? -16.925 7.263   29.357  1.00 13.83 ? 63  GLY B C   1 
ATOM   1937 O  O   . GLY B 1 75  ? -17.452 6.296   28.746  1.00 14.57 ? 63  GLY B O   1 
ATOM   1938 N  N   . GLU B 1 76  ? -15.729 7.740   29.089  1.00 13.43 ? 64  GLU B N   1 
ATOM   1939 C  CA  . GLU B 1 76  ? -14.950 7.306   27.897  1.00 16.29 ? 64  GLU B CA  1 
ATOM   1940 C  C   . GLU B 1 76  ? -13.496 7.187   28.335  1.00 15.67 ? 64  GLU B C   1 
ATOM   1941 O  O   . GLU B 1 76  ? -13.056 7.990   29.205  1.00 14.55 ? 64  GLU B O   1 
ATOM   1942 C  CB  . GLU B 1 76  ? -15.026 8.336   26.765  1.00 22.61 ? 64  GLU B CB  1 
ATOM   1943 C  CG  . GLU B 1 76  ? -16.431 8.832   26.461  1.00 30.97 ? 64  GLU B CG  1 
ATOM   1944 C  CD  . GLU B 1 76  ? -16.526 9.920   25.399  1.00 35.05 ? 64  GLU B CD  1 
ATOM   1945 O  OE1 . GLU B 1 76  ? -17.425 10.788  25.523  1.00 41.38 ? 64  GLU B OE1 1 
ATOM   1946 O  OE2 . GLU B 1 76  ? -15.725 9.884   24.448  1.00 39.67 ? 64  GLU B OE2 1 
ATOM   1947 N  N   . TRP B 1 77  ? -12.765 6.277   27.698  1.00 13.82 ? 65  TRP B N   1 
ATOM   1948 C  CA  . TRP B 1 77  ? -11.340 5.993   28.048  1.00 13.73 ? 65  TRP B CA  1 
ATOM   1949 C  C   . TRP B 1 77  ? -10.643 5.603   26.749  1.00 13.58 ? 65  TRP B C   1 
ATOM   1950 O  O   . TRP B 1 77  ? -10.976 4.537   26.189  1.00 15.35 ? 65  TRP B O   1 
ATOM   1951 C  CB  . TRP B 1 77  ? -11.264 4.921   29.116  1.00 14.50 ? 65  TRP B CB  1 
ATOM   1952 C  CG  . TRP B 1 77  ? -9.958  4.180   29.268  1.00 15.36 ? 65  TRP B CG  1 
ATOM   1953 C  CD1 . TRP B 1 77  ? -8.878  4.599   29.994  1.00 18.65 ? 65  TRP B CD1 1 
ATOM   1954 C  CD2 . TRP B 1 77  ? -9.651  2.846   28.815  1.00 15.84 ? 65  TRP B CD2 1 
ATOM   1955 N  NE1 . TRP B 1 77  ? -7.898  3.631   29.980  1.00 17.96 ? 65  TRP B NE1 1 
ATOM   1956 C  CE2 . TRP B 1 77  ? -8.339  2.545   29.278  1.00 17.06 ? 65  TRP B CE2 1 
ATOM   1957 C  CE3 . TRP B 1 77  ? -10.314 1.894   28.022  1.00 16.91 ? 65  TRP B CE3 1 
ATOM   1958 C  CZ2 . TRP B 1 77  ? -7.706  1.344   28.973  1.00 17.09 ? 65  TRP B CZ2 1 
ATOM   1959 C  CZ3 . TRP B 1 77  ? -9.688  0.700   27.727  1.00 18.31 ? 65  TRP B CZ3 1 
ATOM   1960 C  CH2 . TRP B 1 77  ? -8.401  0.416   28.227  1.00 17.34 ? 65  TRP B CH2 1 
ATOM   1961 N  N   . ASN B 1 78  ? -9.735  6.451   26.288  1.00 13.59 ? 66  ASN B N   1 
ATOM   1962 C  CA  . ASN B 1 78  ? -9.191  6.436   24.921  1.00 14.36 ? 66  ASN B CA  1 
ATOM   1963 C  C   . ASN B 1 78  ? -7.673  6.383   25.007  1.00 13.60 ? 66  ASN B C   1 
ATOM   1964 O  O   . ASN B 1 78  ? -7.008  7.381   24.705  1.00 14.14 ? 66  ASN B O   1 
ATOM   1965 C  CB  . ASN B 1 78  ? -9.690  7.643   24.146  1.00 15.50 ? 66  ASN B CB  1 
ATOM   1966 C  CG  . ASN B 1 78  ? -11.203 7.629   24.055  1.00 19.72 ? 66  ASN B CG  1 
ATOM   1967 O  OD1 . ASN B 1 78  ? -11.768 6.659   23.568  1.00 27.80 ? 66  ASN B OD1 1 
ATOM   1968 N  ND2 . ASN B 1 78  ? -11.845 8.690   24.496  1.00 25.07 ? 66  ASN B ND2 1 
ATOM   1969 N  N   . PRO B 1 79  ? -7.106  5.226   25.365  1.00 15.21 ? 67  PRO B N   1 
ATOM   1970 C  CA  . PRO B 1 79  ? -5.653  5.100   25.409  1.00 15.39 ? 67  PRO B CA  1 
ATOM   1971 C  C   . PRO B 1 79  ? -5.048  4.756   24.044  1.00 15.29 ? 67  PRO B C   1 
ATOM   1972 O  O   . PRO B 1 79  ? -5.721  4.209   23.171  1.00 16.44 ? 67  PRO B O   1 
ATOM   1973 C  CB  . PRO B 1 79  ? -5.442  3.924   26.368  1.00 16.16 ? 67  PRO B CB  1 
ATOM   1974 C  CG  . PRO B 1 79  ? -6.622  3.035   26.040  1.00 15.30 ? 67  PRO B CG  1 
ATOM   1975 C  CD  . PRO B 1 79  ? -7.772  4.012   25.852  1.00 16.45 ? 67  PRO B CD  1 
ATOM   1976 N  N   . ASN B 1 80  ? -3.793  5.141   23.914  1.00 16.05 ? 68  ASN B N   1 
ATOM   1977 C  CA  . ASN B 1 80  ? -2.878  4.781   22.805  1.00 17.07 ? 68  ASN B CA  1 
ATOM   1978 C  C   . ASN B 1 80  ? -1.654  4.187   23.491  1.00 17.07 ? 68  ASN B C   1 
ATOM   1979 O  O   . ASN B 1 80  ? -0.678  4.918   23.758  1.00 16.41 ? 68  ASN B O   1 
ATOM   1980 C  CB  . ASN B 1 80  ? -2.595  5.979   21.898  1.00 20.85 ? 68  ASN B CB  1 
ATOM   1981 C  CG  . ASN B 1 80  ? -1.568  5.676   20.821  1.00 23.47 ? 68  ASN B CG  1 
ATOM   1982 O  OD1 . ASN B 1 80  ? -1.451  4.537   20.394  1.00 30.55 ? 68  ASN B OD1 1 
ATOM   1983 N  ND2 . ASN B 1 80  ? -0.853  6.694   20.364  1.00 25.72 ? 68  ASN B ND2 1 
ATOM   1984 N  N   . GLY B 1 81  ? -1.752  2.903   23.811  1.00 16.29 ? 69  GLY B N   1 
ATOM   1985 C  CA  . GLY B 1 81  ? -0.717  2.158   24.538  1.00 14.99 ? 69  GLY B CA  1 
ATOM   1986 C  C   . GLY B 1 81  ? -1.180  1.858   25.932  1.00 15.68 ? 69  GLY B C   1 
ATOM   1987 O  O   . GLY B 1 81  ? -2.439  1.817   26.175  1.00 15.59 ? 69  GLY B O   1 
ATOM   1988 N  N   . ASN B 1 82  ? -0.218  1.555   26.787  1.00 15.25 ? 70  ASN B N   1 
ATOM   1989 C  CA  . ASN B 1 82  ? -0.434  0.828   28.046  1.00 15.39 ? 70  ASN B CA  1 
ATOM   1990 C  C   . ASN B 1 82  ? -1.284  1.721   28.970  1.00 14.38 ? 70  ASN B C   1 
ATOM   1991 O  O   . ASN B 1 82  ? -0.780  2.744   29.448  1.00 14.44 ? 70  ASN B O   1 
ATOM   1992 C  CB  . ASN B 1 82  ? 0.915   0.509   28.671  1.00 15.92 ? 70  ASN B CB  1 
ATOM   1993 C  CG  . ASN B 1 82  ? 0.841   -0.306  29.938  1.00 18.18 ? 70  ASN B CG  1 
ATOM   1994 O  OD1 . ASN B 1 82  ? -0.218  -0.635  30.469  1.00 21.46 ? 70  ASN B OD1 1 
ATOM   1995 N  ND2 . ASN B 1 82  ? 2.016   -0.687  30.403  1.00 21.31 ? 70  ASN B ND2 1 
ATOM   1996 N  N   . SER B 1 83  ? -2.464  1.248   29.298  1.00 13.14 ? 71  SER B N   1 
ATOM   1997 C  CA  . SER B 1 83  ? -3.411  1.965   30.176  1.00 12.74 ? 71  SER B CA  1 
ATOM   1998 C  C   . SER B 1 83  ? -4.405  0.937   30.717  1.00 12.44 ? 71  SER B C   1 
ATOM   1999 O  O   . SER B 1 83  ? -4.646  -0.107  30.040  1.00 12.70 ? 71  SER B O   1 
ATOM   2000 C  CB  . SER B 1 83  ? -4.084  3.090   29.421  1.00 13.46 ? 71  SER B CB  1 
ATOM   2001 O  OG  . SER B 1 83  ? -4.961  3.853   30.275  1.00 13.32 ? 71  SER B OG  1 
ATOM   2002 N  N   . TYR B 1 84  ? -4.993  1.217   31.874  1.00 12.03 ? 72  TYR B N   1 
ATOM   2003 C  CA  . TYR B 1 84  ? -6.109  0.425   32.402  1.00 12.64 ? 72  TYR B CA  1 
ATOM   2004 C  C   . TYR B 1 84  ? -7.039  1.298   33.216  1.00 11.78 ? 72  TYR B C   1 
ATOM   2005 O  O   . TYR B 1 84  ? -6.659  2.436   33.666  1.00 11.30 ? 72  TYR B O   1 
ATOM   2006 C  CB  . TYR B 1 84  ? -5.669  -0.850  33.134  1.00 13.45 ? 72  TYR B CB  1 
ATOM   2007 C  CG  . TYR B 1 84  ? -4.671  -0.671  34.242  1.00 16.76 ? 72  TYR B CG  1 
ATOM   2008 C  CD1 . TYR B 1 84  ? -3.307  -0.632  34.044  1.00 24.83 ? 72  TYR B CD1 1 
ATOM   2009 C  CD2 . TYR B 1 84  ? -5.148  -0.518  35.525  1.00 21.54 ? 72  TYR B CD2 1 
ATOM   2010 C  CE1 . TYR B 1 84  ? -2.440  -0.462  35.125  1.00 25.83 ? 72  TYR B CE1 1 
ATOM   2011 C  CE2 . TYR B 1 84  ? -4.310  -0.315  36.596  1.00 23.11 ? 72  TYR B CE2 1 
ATOM   2012 C  CZ  . TYR B 1 84  ? -2.951  -0.326  36.404  1.00 25.56 ? 72  TYR B CZ  1 
ATOM   2013 O  OH  . TYR B 1 84  ? -2.202  -0.099  37.526  1.00 31.58 ? 72  TYR B OH  1 
ATOM   2014 N  N   . LEU B 1 85  ? -8.273  0.836   33.258  1.00 11.38 ? 73  LEU B N   1 
ATOM   2015 C  CA  . LEU B 1 85  ? -9.385  1.478   33.972  1.00 11.66 ? 73  LEU B CA  1 
ATOM   2016 C  C   . LEU B 1 85  ? -9.840  0.553   35.088  1.00 11.91 ? 73  LEU B C   1 
ATOM   2017 O  O   . LEU B 1 85  ? -10.199 -0.637  34.827  1.00 11.49 ? 73  LEU B O   1 
ATOM   2018 C  CB  . LEU B 1 85  ? -10.511 1.760   32.974  1.00 14.29 ? 73  LEU B CB  1 
ATOM   2019 C  CG  . LEU B 1 85  ? -11.750 2.441   33.550  1.00 16.11 ? 73  LEU B CG  1 
ATOM   2020 C  CD1 . LEU B 1 85  ? -11.471 3.887   33.971  1.00 17.39 ? 73  LEU B CD1 1 
ATOM   2021 C  CD2 . LEU B 1 85  ? -12.807 2.403   32.438  1.00 18.20 ? 73  LEU B CD2 1 
ATOM   2022 N  N   . SER B 1 86  ? -9.826  1.026   36.335  1.00 11.96 ? 74  SER B N   1 
ATOM   2023 C  CA  . SER B 1 86  ? -9.992  0.075   37.459  1.00 12.80 ? 74  SER B CA  1 
ATOM   2024 C  C   . SER B 1 86  ? -10.682 0.772   38.604  1.00 11.56 ? 74  SER B C   1 
ATOM   2025 O  O   . SER B 1 86  ? -10.652 2.010   38.688  1.00 12.62 ? 74  SER B O   1 
ATOM   2026 C  CB  . SER B 1 86  ? -8.627  -0.445  37.979  1.00 15.54 ? 74  SER B CB  1 
ATOM   2027 O  OG  . SER B 1 86  ? -7.819  -0.919  36.912  1.00 23.14 ? 74  SER B OG  1 
ATOM   2028 N  N   . VAL B 1 87  ? -11.261 -0.024  39.466  1.00 11.62 ? 75  VAL B N   1 
ATOM   2029 C  CA  . VAL B 1 87  ? -11.528 0.424   40.832  1.00 11.27 ? 75  VAL B CA  1 
ATOM   2030 C  C   . VAL B 1 87  ? -10.215 0.167   41.558  1.00 11.58 ? 75  VAL B C   1 
ATOM   2031 O  O   . VAL B 1 87  ? -9.755  -0.963  41.531  1.00 14.63 ? 75  VAL B O   1 
ATOM   2032 C  CB  . VAL B 1 87  ? -12.729 -0.277  41.447  1.00 13.43 ? 75  VAL B CB  1 
ATOM   2033 C  CG1 . VAL B 1 87  ? -12.879 0.103   42.905  1.00 13.72 ? 75  VAL B CG1 1 
ATOM   2034 C  CG2 . VAL B 1 87  ? -13.970 0.054   40.654  1.00 15.96 ? 75  VAL B CG2 1 
ATOM   2035 N  N   . TYR B 1 88  ? -9.740  1.171   42.251  1.00 9.51  ? 76  TYR B N   1 
ATOM   2036 C  CA  . TYR B 1 88  ? -8.393  1.143   42.859  1.00 10.05 ? 76  TYR B CA  1 
ATOM   2037 C  C   . TYR B 1 88  ? -8.470  1.656   44.286  1.00 9.92  ? 76  TYR B C   1 
ATOM   2038 O  O   . TYR B 1 88  ? -9.080  2.656   44.527  1.00 11.12 ? 76  TYR B O   1 
ATOM   2039 C  CB  . TYR B 1 88  ? -7.450  1.959   41.998  1.00 11.75 ? 76  TYR B CB  1 
ATOM   2040 C  CG  . TYR B 1 88  ? -6.127  2.312   42.601  1.00 12.20 ? 76  TYR B CG  1 
ATOM   2041 C  CD1 . TYR B 1 88  ? -5.101  1.376   42.580  1.00 14.44 ? 76  TYR B CD1 1 
ATOM   2042 C  CD2 . TYR B 1 88  ? -5.863  3.558   43.138  1.00 13.45 ? 76  TYR B CD2 1 
ATOM   2043 C  CE1 . TYR B 1 88  ? -3.855  1.657   43.110  1.00 14.91 ? 76  TYR B CE1 1 
ATOM   2044 C  CE2 . TYR B 1 88  ? -4.615  3.844   43.691  1.00 14.30 ? 76  TYR B CE2 1 
ATOM   2045 C  CZ  . TYR B 1 88  ? -3.588  2.907   43.627  1.00 14.09 ? 76  TYR B CZ  1 
ATOM   2046 O  OH  . TYR B 1 88  ? -2.353  3.162   44.176  1.00 16.36 ? 76  TYR B OH  1 
ATOM   2047 N  N   . GLY B 1 89  ? -7.815  0.957   45.193  1.00 10.45 ? 77  GLY B N   1 
ATOM   2048 C  CA  . GLY B 1 89  ? -7.853  1.410   46.591  1.00 9.89  ? 77  GLY B CA  1 
ATOM   2049 C  C   . GLY B 1 89  ? -6.775  0.807   47.449  1.00 9.52  ? 77  GLY B C   1 
ATOM   2050 O  O   . GLY B 1 89  ? -5.932  0.030   46.925  1.00 11.58 ? 77  GLY B O   1 
ATOM   2051 N  N   . TRP B 1 90  ? -6.831  1.178   48.732  1.00 9.71  ? 78  TRP B N   1 
ATOM   2052 C  CA  . TRP B 1 90  ? -5.871  0.701   49.753  1.00 10.23 ? 78  TRP B CA  1 
ATOM   2053 C  C   . TRP B 1 90  ? -6.592  0.198   50.974  1.00 9.78  ? 78  TRP B C   1 
ATOM   2054 O  O   . TRP B 1 90  ? -7.643  0.735   51.289  1.00 10.46 ? 78  TRP B O   1 
ATOM   2055 C  CB  . TRP B 1 90  ? -4.939  1.819   50.132  1.00 11.13 ? 78  TRP B CB  1 
ATOM   2056 C  CG  . TRP B 1 90  ? -4.034  2.230   49.025  1.00 11.73 ? 78  TRP B CG  1 
ATOM   2057 C  CD1 . TRP B 1 90  ? -4.320  3.117   48.035  1.00 12.54 ? 78  TRP B CD1 1 
ATOM   2058 C  CD2 . TRP B 1 90  ? -2.665  1.846   48.836  1.00 11.87 ? 78  TRP B CD2 1 
ATOM   2059 N  NE1 . TRP B 1 90  ? -3.218  3.282   47.228  1.00 13.77 ? 78  TRP B NE1 1 
ATOM   2060 C  CE2 . TRP B 1 90  ? -2.206  2.511   47.676  1.00 13.08 ? 78  TRP B CE2 1 
ATOM   2061 C  CE3 . TRP B 1 90  ? -1.796  0.968   49.470  1.00 12.22 ? 78  TRP B CE3 1 
ATOM   2062 C  CZ2 . TRP B 1 90  ? -0.908  2.369   47.187  1.00 12.70 ? 78  TRP B CZ2 1 
ATOM   2063 C  CZ3 . TRP B 1 90  ? -0.529  0.802   48.964  1.00 13.22 ? 78  TRP B CZ3 1 
ATOM   2064 C  CH2 . TRP B 1 90  ? -0.101  1.501   47.840  1.00 12.13 ? 78  TRP B CH2 1 
ATOM   2065 N  N   . THR B 1 91  ? -5.961  -0.719  51.653  1.00 10.20 ? 79  THR B N   1 
ATOM   2066 C  CA  . THR B 1 91  ? -6.219  -0.967  53.081  1.00 11.18 ? 79  THR B CA  1 
ATOM   2067 C  C   . THR B 1 91  ? -4.938  -0.684  53.851  1.00 11.92 ? 79  THR B C   1 
ATOM   2068 O  O   . THR B 1 91  ? -3.853  -0.643  53.261  1.00 11.71 ? 79  THR B O   1 
ATOM   2069 C  CB  . THR B 1 91  ? -6.723  -2.369  53.400  1.00 13.54 ? 79  THR B CB  1 
ATOM   2070 O  OG1 . THR B 1 91  ? -5.694  -3.370  53.288  1.00 14.99 ? 79  THR B OG1 1 
ATOM   2071 C  CG2 . THR B 1 91  ? -7.917  -2.721  52.540  1.00 14.07 ? 79  THR B CG2 1 
ATOM   2072 N  N   . GLN B 1 92  ? -5.093  -0.567  55.147  1.00 12.09 ? 80  GLN B N   1 
ATOM   2073 C  CA  . GLN B 1 92  ? -3.979  -0.378  56.080  1.00 13.08 ? 80  GLN B CA  1 
ATOM   2074 C  C   . GLN B 1 92  ? -4.031  -1.493  57.127  1.00 11.86 ? 80  GLN B C   1 
ATOM   2075 O  O   . GLN B 1 92  ? -5.113  -1.933  57.510  1.00 11.77 ? 80  GLN B O   1 
ATOM   2076 C  CB  . GLN B 1 92  ? -4.065  0.989   56.758  1.00 15.14 ? 80  GLN B CB  1 
ATOM   2077 C  CG  . GLN B 1 92  ? -3.712  2.144   55.841  1.00 17.14 ? 80  GLN B CG  1 
ATOM   2078 C  CD  . GLN B 1 92  ? -4.232  3.472   56.333  1.00 20.67 ? 80  GLN B CD  1 
ATOM   2079 O  OE1 . GLN B 1 92  ? -5.435  3.707   56.398  1.00 23.66 ? 80  GLN B OE1 1 
ATOM   2080 N  NE2 . GLN B 1 92  ? -3.309  4.384   56.593  1.00 22.70 ? 80  GLN B NE2 1 
ATOM   2081 N  N   . ASN B 1 93  ? -2.853  -1.865  57.635  1.00 11.29 ? 81  ASN B N   1 
ATOM   2082 C  CA  . ASN B 1 93  ? -2.761  -2.793  58.780  1.00 12.68 ? 81  ASN B CA  1 
ATOM   2083 C  C   . ASN B 1 93  ? -3.549  -4.081  58.543  1.00 12.76 ? 81  ASN B C   1 
ATOM   2084 O  O   . ASN B 1 93  ? -4.496  -4.393  59.289  1.00 14.41 ? 81  ASN B O   1 
ATOM   2085 C  CB  . ASN B 1 93  ? -3.263  -2.076  60.020  1.00 13.29 ? 81  ASN B CB  1 
ATOM   2086 C  CG  . ASN B 1 93  ? -2.914  -2.814  61.289  1.00 14.16 ? 81  ASN B CG  1 
ATOM   2087 O  OD1 . ASN B 1 93  ? -3.597  -2.614  62.327  1.00 18.46 ? 81  ASN B OD1 1 
ATOM   2088 N  ND2 . ASN B 1 93  ? -1.868  -3.620  61.216  1.00 10.55 ? 81  ASN B ND2 1 
ATOM   2089 N  N   . PRO B 1 94  ? -3.206  -4.918  57.538  1.00 11.98 ? 82  PRO B N   1 
ATOM   2090 C  CA  . PRO B 1 94  ? -2.053  -4.703  56.660  1.00 12.97 ? 82  PRO B CA  1 
ATOM   2091 C  C   . PRO B 1 94  ? -2.289  -3.730  55.493  1.00 12.68 ? 82  PRO B C   1 
ATOM   2092 O  O   . PRO B 1 94  ? -3.414  -3.604  54.979  1.00 11.50 ? 82  PRO B O   1 
ATOM   2093 C  CB  . PRO B 1 94  ? -1.806  -6.121  56.081  1.00 13.73 ? 82  PRO B CB  1 
ATOM   2094 C  CG  . PRO B 1 94  ? -3.134  -6.723  56.057  1.00 14.52 ? 82  PRO B CG  1 
ATOM   2095 C  CD  . PRO B 1 94  ? -3.835  -6.226  57.295  1.00 13.62 ? 82  PRO B CD  1 
ATOM   2096 N  N   . LEU B 1 95  ? -1.188  -3.157  55.066  1.00 12.80 ? 83  LEU B N   1 
ATOM   2097 C  CA  . LEU B 1 95  ? -1.079  -2.337  53.848  1.00 13.34 ? 83  LEU B CA  1 
ATOM   2098 C  C   . LEU B 1 95  ? -1.271  -3.234  52.618  1.00 13.40 ? 83  LEU B C   1 
ATOM   2099 O  O   . LEU B 1 95  ? -0.490  -4.178  52.373  1.00 13.83 ? 83  LEU B O   1 
ATOM   2100 C  CB  . LEU B 1 95  ? 0.276   -1.637  53.842  1.00 13.52 ? 83  LEU B CB  1 
ATOM   2101 C  CG  . LEU B 1 95  ? 0.433   -0.498  52.840  1.00 14.70 ? 83  LEU B CG  1 
ATOM   2102 C  CD1 . LEU B 1 95  ? -0.510  0.669   53.132  1.00 13.82 ? 83  LEU B CD1 1 
ATOM   2103 C  CD2 . LEU B 1 95  ? 1.869   0.025   52.831  1.00 16.16 ? 83  LEU B CD2 1 
ATOM   2104 N  N   . VAL B 1 96  ? -2.302  -2.905  51.834  1.00 12.24 ? 84  VAL B N   1 
ATOM   2105 C  CA  . VAL B 1 96  ? -2.676  -3.640  50.606  1.00 11.90 ? 84  VAL B CA  1 
ATOM   2106 C  C   . VAL B 1 96  ? -3.100  -2.586  49.564  1.00 10.87 ? 84  VAL B C   1 
ATOM   2107 O  O   . VAL B 1 96  ? -3.821  -1.657  49.898  1.00 11.19 ? 84  VAL B O   1 
ATOM   2108 C  CB  . VAL B 1 96  ? -3.826  -4.632  50.816  1.00 12.76 ? 84  VAL B CB  1 
ATOM   2109 C  CG1 . VAL B 1 96  ? -4.289  -5.180  49.474  1.00 13.50 ? 84  VAL B CG1 1 
ATOM   2110 C  CG2 . VAL B 1 96  ? -3.520  -5.728  51.821  1.00 11.71 ? 84  VAL B CG2 1 
ATOM   2111 N  N   . GLU B 1 97  ? -2.578  -2.712  48.361  1.00 10.11 ? 85  GLU B N   1 
ATOM   2112 C  CA  . GLU B 1 97  ? -2.984  -1.957  47.164  1.00 10.81 ? 85  GLU B CA  1 
ATOM   2113 C  C   . GLU B 1 97  ? -3.826  -2.911  46.332  1.00 10.48 ? 85  GLU B C   1 
ATOM   2114 O  O   . GLU B 1 97  ? -3.412  -4.084  46.145  1.00 11.91 ? 85  GLU B O   1 
ATOM   2115 C  CB  . GLU B 1 97  ? -1.736  -1.511  46.405  1.00 11.05 ? 85  GLU B CB  1 
ATOM   2116 C  CG  . GLU B 1 97  ? -2.016  -0.684  45.192  1.00 14.07 ? 85  GLU B CG  1 
ATOM   2117 C  CD  . GLU B 1 97  ? -0.789  -0.211  44.425  1.00 15.44 ? 85  GLU B CD  1 
ATOM   2118 O  OE1 . GLU B 1 97  ? -0.683  1.035   44.146  1.00 18.15 ? 85  GLU B OE1 1 
ATOM   2119 O  OE2 . GLU B 1 97  ? 0.093   -1.075  44.174  1.00 18.04 ? 85  GLU B OE2 1 
ATOM   2120 N  N   . TYR B 1 98  ? -5.011  -2.512  45.888  1.00 11.78 ? 86  TYR B N   1 
ATOM   2121 C  CA  . TYR B 1 98  ? -5.848  -3.472  45.128  1.00 12.28 ? 86  TYR B CA  1 
ATOM   2122 C  C   . TYR B 1 98  ? -6.391  -2.800  43.872  1.00 11.83 ? 86  TYR B C   1 
ATOM   2123 O  O   . TYR B 1 98  ? -6.588  -1.551  43.816  1.00 11.15 ? 86  TYR B O   1 
ATOM   2124 C  CB  . TYR B 1 98  ? -6.948  -4.091  45.969  1.00 11.97 ? 86  TYR B CB  1 
ATOM   2125 C  CG  . TYR B 1 98  ? -7.971  -3.102  46.453  1.00 12.45 ? 86  TYR B CG  1 
ATOM   2126 C  CD1 . TYR B 1 98  ? -8.992  -2.666  45.610  1.00 13.56 ? 86  TYR B CD1 1 
ATOM   2127 C  CD2 . TYR B 1 98  ? -7.902  -2.553  47.728  1.00 13.35 ? 86  TYR B CD2 1 
ATOM   2128 C  CE1 . TYR B 1 98  ? -9.938  -1.764  46.041  1.00 12.05 ? 86  TYR B CE1 1 
ATOM   2129 C  CE2 . TYR B 1 98  ? -8.843  -1.648  48.162  1.00 13.28 ? 86  TYR B CE2 1 
ATOM   2130 C  CZ  . TYR B 1 98  ? -9.869  -1.251  47.315  1.00 13.86 ? 86  TYR B CZ  1 
ATOM   2131 O  OH  . TYR B 1 98  ? -10.764 -0.324  47.797  1.00 16.39 ? 86  TYR B OH  1 
ATOM   2132 N  N   . TYR B 1 99  ? -6.663  -3.628  42.861  1.00 13.28 ? 87  TYR B N   1 
ATOM   2133 C  CA  . TYR B 1 99  ? -7.240  -3.126  41.582  1.00 14.14 ? 87  TYR B CA  1 
ATOM   2134 C  C   . TYR B 1 99  ? -8.283  -4.106  41.095  1.00 15.10 ? 87  TYR B C   1 
ATOM   2135 O  O   . TYR B 1 99  ? -7.979  -5.330  41.061  1.00 15.71 ? 87  TYR B O   1 
ATOM   2136 C  CB  . TYR B 1 99  ? -6.256  -3.119  40.413  1.00 17.62 ? 87  TYR B CB  1 
ATOM   2137 C  CG  . TYR B 1 99  ? -5.032  -2.308  40.620  1.00 19.81 ? 87  TYR B CG  1 
ATOM   2138 C  CD1 . TYR B 1 99  ? -4.102  -2.784  41.519  1.00 23.54 ? 87  TYR B CD1 1 
ATOM   2139 C  CD2 . TYR B 1 99  ? -4.800  -1.119  39.954  1.00 22.60 ? 87  TYR B CD2 1 
ATOM   2140 C  CE1 . TYR B 1 99  ? -2.926  -2.120  41.724  1.00 24.94 ? 87  TYR B CE1 1 
ATOM   2141 C  CE2 . TYR B 1 99  ? -3.600  -0.438  40.163  1.00 26.82 ? 87  TYR B CE2 1 
ATOM   2142 C  CZ  . TYR B 1 99  ? -2.680  -0.957  41.052  1.00 23.04 ? 87  TYR B CZ  1 
ATOM   2143 O  OH  . TYR B 1 99  ? -1.450  -0.456  41.368  1.00 31.67 ? 87  TYR B OH  1 
ATOM   2144 N  N   . ILE B 1 100 ? -9.445  -3.575  40.766  1.00 13.21 ? 88  ILE B N   1 
ATOM   2145 C  CA  . ILE B 1 100 ? -10.492 -4.311  40.034  1.00 12.67 ? 88  ILE B CA  1 
ATOM   2146 C  C   . ILE B 1 100 ? -10.494 -3.733  38.628  1.00 11.77 ? 88  ILE B C   1 
ATOM   2147 O  O   . ILE B 1 100 ? -10.992 -2.628  38.397  1.00 13.41 ? 88  ILE B O   1 
ATOM   2148 C  CB  . ILE B 1 100 ? -11.834 -4.209  40.772  1.00 12.92 ? 88  ILE B CB  1 
ATOM   2149 C  CG1 . ILE B 1 100 ? -11.759 -4.793  42.173  1.00 13.59 ? 88  ILE B CG1 1 
ATOM   2150 C  CG2 . ILE B 1 100 ? -12.968 -4.863  39.965  1.00 13.77 ? 88  ILE B CG2 1 
ATOM   2151 C  CD1 . ILE B 1 100 ? -12.839 -4.267  43.064  1.00 13.20 ? 88  ILE B CD1 1 
ATOM   2152 N  N   . VAL B 1 101 ? -9.857  -4.438  37.710  1.00 10.76 ? 89  VAL B N   1 
ATOM   2153 C  CA  . VAL B 1 101 ? -9.564  -3.920  36.367  1.00 10.42 ? 89  VAL B CA  1 
ATOM   2154 C  C   . VAL B 1 101 ? -10.753 -4.268  35.464  1.00 10.99 ? 89  VAL B C   1 
ATOM   2155 O  O   . VAL B 1 101 ? -11.009 -5.470  35.237  1.00 11.12 ? 89  VAL B O   1 
ATOM   2156 C  CB  . VAL B 1 101 ? -8.265  -4.492  35.813  1.00 11.13 ? 89  VAL B CB  1 
ATOM   2157 C  CG1 . VAL B 1 101 ? -7.966  -3.971  34.437  1.00 11.48 ? 89  VAL B CG1 1 
ATOM   2158 C  CG2 . VAL B 1 101 ? -7.122  -4.248  36.765  1.00 10.41 ? 89  VAL B CG2 1 
ATOM   2159 N  N   . GLU B 1 102 ? -11.342 -3.224  34.922  1.00 12.04 ? 90  GLU B N   1 
ATOM   2160 C  CA  . GLU B 1 102 ? -12.524 -3.288  34.025  1.00 12.87 ? 90  GLU B CA  1 
ATOM   2161 C  C   . GLU B 1 102 ? -12.092 -3.393  32.553  1.00 12.96 ? 90  GLU B C   1 
ATOM   2162 O  O   . GLU B 1 102 ? -12.794 -4.096  31.754  1.00 13.37 ? 90  GLU B O   1 
ATOM   2163 C  CB  . GLU B 1 102 ? -13.413 -2.086  34.295  1.00 15.11 ? 90  GLU B CB  1 
ATOM   2164 C  CG  . GLU B 1 102 ? -14.070 -2.176  35.658  1.00 16.80 ? 90  GLU B CG  1 
ATOM   2165 C  CD  . GLU B 1 102 ? -14.998 -3.354  35.800  1.00 19.42 ? 90  GLU B CD  1 
ATOM   2166 O  OE1 . GLU B 1 102 ? -14.604 -4.271  36.477  1.00 23.69 ? 90  GLU B OE1 1 
ATOM   2167 O  OE2 . GLU B 1 102 ? -16.145 -3.314  35.293  1.00 22.66 ? 90  GLU B OE2 1 
ATOM   2168 N  N   . SER B 1 103 ? -11.043 -2.688  32.191  1.00 12.50 ? 91  SER B N   1 
ATOM   2169 C  CA  . SER B 1 103 ? -10.404 -2.717  30.856  1.00 11.71 ? 91  SER B CA  1 
ATOM   2170 C  C   . SER B 1 103 ? -8.910  -2.510  31.012  1.00 11.98 ? 91  SER B C   1 
ATOM   2171 O  O   . SER B 1 103 ? -8.503  -1.715  31.847  1.00 11.99 ? 91  SER B O   1 
ATOM   2172 C  CB  . SER B 1 103 ? -10.905 -1.642  29.931  1.00 13.62 ? 91  SER B CB  1 
ATOM   2173 O  OG  . SER B 1 103 ? -12.266 -1.772  29.590  1.00 17.64 ? 91  SER B OG  1 
ATOM   2174 N  N   . PHE B 1 104 ? -8.146  -3.107  30.123  1.00 11.42 ? 92  PHE B N   1 
ATOM   2175 C  CA  . PHE B 1 104 ? -6.724  -2.739  29.889  1.00 11.74 ? 92  PHE B CA  1 
ATOM   2176 C  C   . PHE B 1 104 ? -6.447  -2.737  28.396  1.00 14.02 ? 92  PHE B C   1 
ATOM   2177 O  O   . PHE B 1 104 ? -7.174  -3.435  27.635  1.00 13.88 ? 92  PHE B O   1 
ATOM   2178 C  CB  . PHE B 1 104 ? -5.799  -3.666  30.675  1.00 13.65 ? 92  PHE B CB  1 
ATOM   2179 C  CG  . PHE B 1 104 ? -5.757  -5.101  30.213  1.00 13.60 ? 92  PHE B CG  1 
ATOM   2180 C  CD1 . PHE B 1 104 ? -5.059  -5.463  29.053  1.00 13.97 ? 92  PHE B CD1 1 
ATOM   2181 C  CD2 . PHE B 1 104 ? -6.346  -6.099  30.981  1.00 13.47 ? 92  PHE B CD2 1 
ATOM   2182 C  CE1 . PHE B 1 104 ? -5.008  -6.803  28.676  1.00 16.59 ? 92  PHE B CE1 1 
ATOM   2183 C  CE2 . PHE B 1 104 ? -6.281  -7.433  30.602  1.00 14.63 ? 92  PHE B CE2 1 
ATOM   2184 C  CZ  . PHE B 1 104 ? -5.605  -7.782  29.440  1.00 15.85 ? 92  PHE B CZ  1 
ATOM   2185 N  N   . SER B 1 105 ? -5.390  -2.026  28.016  1.00 13.80 ? 93  SER B N   1 
ATOM   2186 C  CA  . SER B 1 105 ? -4.941  -1.774  26.639  1.00 17.48 ? 93  SER B CA  1 
ATOM   2187 C  C   . SER B 1 105 ? -3.455  -2.182  26.546  1.00 20.01 ? 93  SER B C   1 
ATOM   2188 O  O   . SER B 1 105 ? -2.596  -1.643  27.267  1.00 27.24 ? 93  SER B O   1 
ATOM   2189 C  CB  . SER B 1 105 ? -5.058  -0.359  26.291  1.00 17.48 ? 93  SER B CB  1 
ATOM   2190 O  OG  . SER B 1 105 ? -4.829  -0.135  24.906  1.00 24.71 ? 93  SER B OG  1 
ATOM   2191 N  N   . THR B 1 106 ? -3.192  -3.079  25.668  1.00 20.22 ? 94  THR B N   1 
ATOM   2192 C  CA  . THR B 1 106 ? -1.863  -3.480  25.185  1.00 16.05 ? 94  THR B CA  1 
ATOM   2193 C  C   . THR B 1 106 ? -1.086  -4.307  26.214  1.00 18.61 ? 94  THR B C   1 
ATOM   2194 O  O   . THR B 1 106 ? -0.176  -4.992  25.776  1.00 18.89 ? 94  THR B O   1 
ATOM   2195 C  CB  . THR B 1 106 ? -1.007  -2.324  24.639  1.00 19.53 ? 94  THR B CB  1 
ATOM   2196 O  OG1 . THR B 1 106 ? -0.495  -1.459  25.642  1.00 18.57 ? 94  THR B OG1 1 
ATOM   2197 C  CG2 . THR B 1 106 ? -1.728  -1.515  23.589  1.00 18.91 ? 94  THR B CG2 1 
ATOM   2198 N  N   . TYR B 1 107 ? -1.326  -4.203  27.522  1.00 15.40 ? 95  TYR B N   1 
ATOM   2199 C  CA  . TYR B 1 107 ? -0.508  -4.920  28.527  1.00 14.38 ? 95  TYR B CA  1 
ATOM   2200 C  C   . TYR B 1 107 ? -1.407  -5.334  29.693  1.00 15.14 ? 95  TYR B C   1 
ATOM   2201 O  O   . TYR B 1 107 ? -2.079  -4.430  30.260  1.00 15.00 ? 95  TYR B O   1 
ATOM   2202 C  CB  . TYR B 1 107 ? 0.626   -4.028  29.043  1.00 15.57 ? 95  TYR B CB  1 
ATOM   2203 C  CG  . TYR B 1 107 ? 1.523   -4.710  30.043  1.00 16.78 ? 95  TYR B CG  1 
ATOM   2204 C  CD1 . TYR B 1 107 ? 2.486   -5.605  29.627  1.00 17.11 ? 95  TYR B CD1 1 
ATOM   2205 C  CD2 . TYR B 1 107 ? 1.498   -4.396  31.395  1.00 18.14 ? 95  TYR B CD2 1 
ATOM   2206 C  CE1 . TYR B 1 107 ? 3.299   -6.267  30.535  1.00 16.82 ? 95  TYR B CE1 1 
ATOM   2207 C  CE2 . TYR B 1 107 ? 2.300   -5.038  32.315  1.00 16.18 ? 95  TYR B CE2 1 
ATOM   2208 C  CZ  . TYR B 1 107 ? 3.212   -5.987  31.887  1.00 17.75 ? 95  TYR B CZ  1 
ATOM   2209 O  OH  . TYR B 1 107 ? 4.078   -6.592  32.739  1.00 18.20 ? 95  TYR B OH  1 
ATOM   2210 N  N   . ASP B 1 108 ? -1.429  -6.616  30.011  1.00 15.07 ? 96  ASP B N   1 
ATOM   2211 C  CA  . ASP B 1 108 ? -2.240  -7.148  31.143  1.00 16.18 ? 96  ASP B CA  1 
ATOM   2212 C  C   . ASP B 1 108 ? -1.483  -6.743  32.406  1.00 17.53 ? 96  ASP B C   1 
ATOM   2213 O  O   . ASP B 1 108 ? -0.370  -7.219  32.589  1.00 18.42 ? 96  ASP B O   1 
ATOM   2214 C  CB  . ASP B 1 108 ? -2.445  -8.656  30.985  1.00 17.23 ? 96  ASP B CB  1 
ATOM   2215 C  CG  . ASP B 1 108 ? -3.352  -9.223  32.069  1.00 18.24 ? 96  ASP B CG  1 
ATOM   2216 O  OD1 . ASP B 1 108 ? -3.446  -8.604  33.142  1.00 19.23 ? 96  ASP B OD1 1 
ATOM   2217 O  OD2 . ASP B 1 108 ? -3.923  -10.258 31.836  1.00 20.20 ? 96  ASP B OD2 1 
ATOM   2218 N  N   . PRO B 1 109 ? -1.986  -5.790  33.243  1.00 18.10 ? 97  PRO B N   1 
ATOM   2219 C  CA  . PRO B 1 109 ? -1.209  -5.267  34.369  1.00 18.02 ? 97  PRO B CA  1 
ATOM   2220 C  C   . PRO B 1 109 ? -1.007  -6.323  35.464  1.00 18.56 ? 97  PRO B C   1 
ATOM   2221 O  O   . PRO B 1 109 ? -0.180  -6.084  36.350  1.00 17.75 ? 97  PRO B O   1 
ATOM   2222 C  CB  . PRO B 1 109 ? -2.015  -4.053  34.867  1.00 17.96 ? 97  PRO B CB  1 
ATOM   2223 C  CG  . PRO B 1 109 ? -3.452  -4.403  34.502  1.00 18.04 ? 97  PRO B CG  1 
ATOM   2224 C  CD  . PRO B 1 109 ? -3.343  -5.196  33.203  1.00 17.93 ? 97  PRO B CD  1 
ATOM   2225 N  N   . SER B 1 110 ? -1.673  -7.481  35.352  1.00 19.51 ? 98  SER B N   1 
ATOM   2226 C  CA  . SER B 1 110 ? -1.509  -8.638  36.284  1.00 21.24 ? 98  SER B CA  1 
ATOM   2227 C  C   . SER B 1 110 ? -0.333  -9.531  35.881  1.00 21.29 ? 98  SER B C   1 
ATOM   2228 O  O   . SER B 1 110 ? -0.001  -10.469 36.655  1.00 21.12 ? 98  SER B O   1 
ATOM   2229 C  CB  . SER B 1 110 ? -2.769  -9.454  36.428  1.00 22.35 ? 98  SER B CB  1 
ATOM   2230 O  OG  . SER B 1 110 ? -3.004  -10.215 35.261  1.00 21.38 ? 98  SER B OG  1 
ATOM   2231 N  N   . THR B 1 111 ? 0.304   -9.257  34.738  1.00 19.56 ? 99  THR B N   1 
ATOM   2232 C  CA  . THR B 1 111 ? 1.485   -10.023 34.282  1.00 17.21 ? 99  THR B CA  1 
ATOM   2233 C  C   . THR B 1 111 ? 2.535   -10.064 35.407  1.00 16.24 ? 99  THR B C   1 
ATOM   2234 O  O   . THR B 1 111 ? 2.823   -9.008  36.016  1.00 20.42 ? 99  THR B O   1 
ATOM   2235 C  CB  . THR B 1 111 ? 2.128   -9.432  33.023  1.00 18.21 ? 99  THR B CB  1 
ATOM   2236 O  OG1 . THR B 1 111 ? 1.113   -9.364  32.033  1.00 18.39 ? 99  THR B OG1 1 
ATOM   2237 C  CG2 . THR B 1 111 ? 3.244   -10.302 32.485  1.00 18.90 ? 99  THR B CG2 1 
ATOM   2238 N  N   . GLY B 1 112 ? 3.012   -11.246 35.725  1.00 17.43 ? 100 GLY B N   1 
ATOM   2239 C  CA  . GLY B 1 112 ? 4.052   -11.430 36.759  1.00 20.70 ? 100 GLY B CA  1 
ATOM   2240 C  C   . GLY B 1 112 ? 3.429   -11.635 38.137  1.00 21.79 ? 100 GLY B C   1 
ATOM   2241 O  O   . GLY B 1 112 ? 4.165   -11.986 39.054  1.00 24.83 ? 100 GLY B O   1 
ATOM   2242 N  N   . ALA B 1 113 ? 2.106   -11.512 38.279  1.00 20.48 ? 101 ALA B N   1 
ATOM   2243 C  CA  . ALA B 1 113 ? 1.422   -11.885 39.544  1.00 20.91 ? 101 ALA B CA  1 
ATOM   2244 C  C   . ALA B 1 113 ? 0.977   -13.353 39.519  1.00 20.83 ? 101 ALA B C   1 
ATOM   2245 O  O   . ALA B 1 113 ? 0.870   -13.936 38.425  1.00 21.73 ? 101 ALA B O   1 
ATOM   2246 C  CB  . ALA B 1 113 ? 0.277   -10.940 39.836  1.00 20.15 ? 101 ALA B CB  1 
ATOM   2247 N  N   . GLN B 1 114 ? 0.715   -13.921 40.711  1.00 22.09 ? 102 GLN B N   1 
ATOM   2248 C  CA  . GLN B 1 114 ? 0.329   -15.339 40.906  1.00 23.29 ? 102 GLN B CA  1 
ATOM   2249 C  C   . GLN B 1 114 ? -1.189  -15.422 40.797  1.00 22.71 ? 102 GLN B C   1 
ATOM   2250 O  O   . GLN B 1 114 ? -1.879  -14.699 41.562  1.00 17.48 ? 102 GLN B O   1 
ATOM   2251 C  CB  . GLN B 1 114 ? 0.722   -15.938 42.260  1.00 27.83 ? 102 GLN B CB  1 
ATOM   2252 C  CG  . GLN B 1 114 ? 1.531   -15.042 43.178  1.00 31.55 ? 102 GLN B CG  1 
ATOM   2253 C  CD  . GLN B 1 114 ? 3.013   -15.146 42.918  1.00 33.39 ? 102 GLN B CD  1 
ATOM   2254 O  OE1 . GLN B 1 114 ? 3.793   -15.436 43.828  1.00 43.99 ? 102 GLN B OE1 1 
ATOM   2255 N  NE2 . GLN B 1 114 ? 3.417   -14.878 41.686  1.00 33.64 ? 102 GLN B NE2 1 
ATOM   2256 N  N   . GLU B 1 115 ? -1.672  -16.248 39.859  1.00 21.07 ? 103 GLU B N   1 
ATOM   2257 C  CA  . GLU B 1 115 ? -3.109  -16.480 39.618  1.00 24.33 ? 103 GLU B CA  1 
ATOM   2258 C  C   . GLU B 1 115 ? -3.637  -17.385 40.735  1.00 27.01 ? 103 GLU B C   1 
ATOM   2259 O  O   . GLU B 1 115 ? -2.873  -18.292 41.163  1.00 26.28 ? 103 GLU B O   1 
ATOM   2260 C  CB  . GLU B 1 115 ? -3.275  -17.078 38.225  1.00 24.25 ? 103 GLU B CB  1 
ATOM   2261 C  CG  . GLU B 1 115 ? -4.675  -16.915 37.691  1.00 26.39 ? 103 GLU B CG  1 
ATOM   2262 C  CD  . GLU B 1 115 ? -4.785  -17.244 36.207  1.00 28.03 ? 103 GLU B CD  1 
ATOM   2263 O  OE1 . GLU B 1 115 ? -5.918  -17.401 35.740  1.00 32.03 ? 103 GLU B OE1 1 
ATOM   2264 O  OE2 . GLU B 1 115 ? -3.726  -17.352 35.535  1.00 35.53 ? 103 GLU B OE2 1 
ATOM   2265 N  N   . LEU B 1 116 ? -4.869  -17.130 41.195  1.00 23.42 ? 104 LEU B N   1 
ATOM   2266 C  CA  . LEU B 1 116 ? -5.449  -17.684 42.443  1.00 27.36 ? 104 LEU B CA  1 
ATOM   2267 C  C   . LEU B 1 116 ? -6.765  -18.385 42.176  1.00 28.82 ? 104 LEU B C   1 
ATOM   2268 O  O   . LEU B 1 116 ? -7.098  -19.272 42.966  1.00 34.89 ? 104 LEU B O   1 
ATOM   2269 C  CB  . LEU B 1 116 ? -5.741  -16.570 43.453  1.00 32.19 ? 104 LEU B CB  1 
ATOM   2270 C  CG  . LEU B 1 116 ? -4.655  -16.297 44.478  1.00 35.73 ? 104 LEU B CG  1 
ATOM   2271 C  CD1 . LEU B 1 116 ? -4.241  -14.853 44.401  1.00 32.42 ? 104 LEU B CD1 1 
ATOM   2272 C  CD2 . LEU B 1 116 ? -5.121  -16.660 45.884  1.00 36.43 ? 104 LEU B CD2 1 
ATOM   2273 N  N   . GLY B 1 117 ? -7.527  -17.937 41.190  1.00 25.02 ? 105 GLY B N   1 
ATOM   2274 C  CA  . GLY B 1 117 ? -8.940  -18.326 41.025  1.00 24.53 ? 105 GLY B CA  1 
ATOM   2275 C  C   . GLY B 1 117 ? -9.685  -17.306 40.188  1.00 22.55 ? 105 GLY B C   1 
ATOM   2276 O  O   . GLY B 1 117 ? -9.029  -16.512 39.460  1.00 20.61 ? 105 GLY B O   1 
ATOM   2277 N  N   . THR B 1 118 ? -11.012 -17.330 40.266  1.00 22.68 ? 106 THR B N   1 
ATOM   2278 C  CA  . THR B 1 118 ? -11.910 -16.429 39.492  1.00 22.73 ? 106 THR B CA  1 
ATOM   2279 C  C   . THR B 1 118 ? -13.086 -16.065 40.386  1.00 21.44 ? 106 THR B C   1 
ATOM   2280 O  O   . THR B 1 118 ? -13.347 -16.739 41.398  1.00 23.56 ? 106 THR B O   1 
ATOM   2281 C  CB  . THR B 1 118 ? -12.411 -17.063 38.176  1.00 26.41 ? 106 THR B CB  1 
ATOM   2282 O  OG1 . THR B 1 118 ? -13.174 -18.233 38.461  1.00 27.19 ? 106 THR B OG1 1 
ATOM   2283 C  CG2 . THR B 1 118 ? -11.314 -17.430 37.202  1.00 29.62 ? 106 THR B CG2 1 
ATOM   2284 N  N   . VAL B 1 119 ? -13.772 -15.003 40.032  1.00 20.58 ? 107 VAL B N   1 
ATOM   2285 C  CA  . VAL B 1 119 ? -15.032 -14.586 40.686  1.00 20.03 ? 107 VAL B CA  1 
ATOM   2286 C  C   . VAL B 1 119 ? -15.952 -14.083 39.572  1.00 20.51 ? 107 VAL B C   1 
ATOM   2287 O  O   . VAL B 1 119 ? -15.440 -13.475 38.598  1.00 20.17 ? 107 VAL B O   1 
ATOM   2288 C  CB  . VAL B 1 119 ? -14.767 -13.520 41.760  1.00 19.81 ? 107 VAL B CB  1 
ATOM   2289 C  CG1 . VAL B 1 119 ? -13.991 -12.357 41.185  1.00 19.68 ? 107 VAL B CG1 1 
ATOM   2290 C  CG2 . VAL B 1 119 ? -16.057 -13.069 42.426  1.00 19.22 ? 107 VAL B CG2 1 
ATOM   2291 N  N   . GLU B 1 120 ? -17.207 -14.503 39.623  1.00 19.85 ? 108 GLU B N   1 
ATOM   2292 C  CA  . GLU B 1 120 ? -18.259 -14.084 38.678  1.00 22.95 ? 108 GLU B CA  1 
ATOM   2293 C  C   . GLU B 1 120 ? -19.087 -12.984 39.347  1.00 20.42 ? 108 GLU B C   1 
ATOM   2294 O  O   . GLU B 1 120 ? -19.660 -13.205 40.439  1.00 20.47 ? 108 GLU B O   1 
ATOM   2295 C  CB  . GLU B 1 120 ? -19.098 -15.290 38.246  1.00 28.11 ? 108 GLU B CB  1 
ATOM   2296 C  CG  . GLU B 1 120 ? -18.563 -15.970 36.990  1.00 37.18 ? 108 GLU B CG  1 
ATOM   2297 C  CD  . GLU B 1 120 ? -19.539 -16.927 36.315  1.00 44.22 ? 108 GLU B CD  1 
ATOM   2298 O  OE1 . GLU B 1 120 ? -19.076 -17.938 35.774  1.00 45.31 ? 108 GLU B OE1 1 
ATOM   2299 O  OE2 . GLU B 1 120 ? -20.761 -16.660 36.336  1.00 51.48 ? 108 GLU B OE2 1 
ATOM   2300 N  N   . THR B 1 121 ? -19.165 -11.810 38.726  1.00 21.79 ? 109 THR B N   1 
ATOM   2301 C  CA  . THR B 1 121 ? -19.850 -10.644 39.325  1.00 22.45 ? 109 THR B CA  1 
ATOM   2302 C  C   . THR B 1 121 ? -20.125 -9.621  38.223  1.00 19.46 ? 109 THR B C   1 
ATOM   2303 O  O   . THR B 1 121 ? -19.366 -9.564  37.230  1.00 18.46 ? 109 THR B O   1 
ATOM   2304 C  CB  . THR B 1 121 ? -19.069 -10.054 40.520  1.00 24.75 ? 109 THR B CB  1 
ATOM   2305 O  OG1 . THR B 1 121 ? -19.750 -8.923  41.077  1.00 26.16 ? 109 THR B OG1 1 
ATOM   2306 C  CG2 . THR B 1 121 ? -17.672 -9.610  40.161  1.00 23.17 ? 109 THR B CG2 1 
ATOM   2307 N  N   . ASP B 1 122 ? -21.235 -8.923  38.357  1.00 19.17 ? 110 ASP B N   1 
ATOM   2308 C  CA  . ASP B 1 122 ? -21.608 -7.806  37.445  1.00 19.86 ? 110 ASP B CA  1 
ATOM   2309 C  C   . ASP B 1 122 ? -21.497 -8.267  35.977  1.00 21.80 ? 110 ASP B C   1 
ATOM   2310 O  O   . ASP B 1 122 ? -20.840 -7.571  35.176  1.00 21.17 ? 110 ASP B O   1 
ATOM   2311 C  CB  . ASP B 1 122 ? -20.744 -6.591  37.802  1.00 19.76 ? 110 ASP B CB  1 
ATOM   2312 C  CG  . ASP B 1 122 ? -20.793 -6.218  39.279  1.00 20.60 ? 110 ASP B CG  1 
ATOM   2313 O  OD1 . ASP B 1 122 ? -21.901 -5.849  39.755  1.00 20.70 ? 110 ASP B OD1 1 
ATOM   2314 O  OD2 . ASP B 1 122 ? -19.731 -6.330  39.974  1.00 20.64 ? 110 ASP B OD2 1 
ATOM   2315 N  N   . ASP B 1 123 ? -22.071 -9.436  35.653  1.00 22.43 ? 111 ASP B N   1 
ATOM   2316 C  CA  . ASP B 1 123 ? -22.217 -9.943  34.259  1.00 25.40 ? 111 ASP B CA  1 
ATOM   2317 C  C   . ASP B 1 123 ? -20.858 -10.296 33.640  1.00 24.84 ? 111 ASP B C   1 
ATOM   2318 O  O   . ASP B 1 123 ? -20.799 -10.525 32.430  1.00 23.12 ? 111 ASP B O   1 
ATOM   2319 C  CB  . ASP B 1 123 ? -23.041 -8.950  33.440  1.00 26.92 ? 111 ASP B CB  1 
ATOM   2320 C  CG  . ASP B 1 123 ? -24.452 -8.847  33.999  1.00 36.46 ? 111 ASP B CG  1 
ATOM   2321 O  OD1 . ASP B 1 123 ? -24.632 -8.132  35.004  1.00 42.47 ? 111 ASP B OD1 1 
ATOM   2322 O  OD2 . ASP B 1 123 ? -25.352 -9.546  33.468  1.00 45.09 ? 111 ASP B OD2 1 
ATOM   2323 N  N   . GLY B 1 124 ? -19.815 -10.454 34.454  1.00 21.66 ? 112 GLY B N   1 
ATOM   2324 C  CA  . GLY B 1 124 ? -18.456 -10.743 33.976  1.00 20.43 ? 112 GLY B CA  1 
ATOM   2325 C  C   . GLY B 1 124 ? -17.798 -11.850 34.783  1.00 19.75 ? 112 GLY B C   1 
ATOM   2326 O  O   . GLY B 1 124 ? -18.324 -12.263 35.847  1.00 19.58 ? 112 GLY B O   1 
ATOM   2327 N  N   . THR B 1 125 ? -16.636 -12.278 34.316  1.00 18.15 ? 113 THR B N   1 
ATOM   2328 C  CA  . THR B 1 125 ? -15.747 -13.208 35.028  1.00 19.16 ? 113 THR B CA  1 
ATOM   2329 C  C   . THR B 1 125 ? -14.440 -12.453 35.250  1.00 17.00 ? 113 THR B C   1 
ATOM   2330 O  O   . THR B 1 125 ? -13.972 -11.785 34.291  1.00 16.87 ? 113 THR B O   1 
ATOM   2331 C  CB  . THR B 1 125 ? -15.538 -14.497 34.209  1.00 21.22 ? 113 THR B CB  1 
ATOM   2332 O  OG1 . THR B 1 125 ? -16.833 -15.062 34.001  1.00 26.03 ? 113 THR B OG1 1 
ATOM   2333 C  CG2 . THR B 1 125 ? -14.642 -15.494 34.888  1.00 23.87 ? 113 THR B CG2 1 
ATOM   2334 N  N   . TYR B 1 126 ? -13.896 -12.546 36.456  1.00 17.14 ? 114 TYR B N   1 
ATOM   2335 C  CA  . TYR B 1 126 ? -12.607 -11.923 36.809  1.00 16.62 ? 114 TYR B CA  1 
ATOM   2336 C  C   . TYR B 1 126 ? -11.633 -13.009 37.258  1.00 16.38 ? 114 TYR B C   1 
ATOM   2337 O  O   . TYR B 1 126 ? -11.980 -13.817 38.090  1.00 20.42 ? 114 TYR B O   1 
ATOM   2338 C  CB  . TYR B 1 126 ? -12.788 -10.863 37.907  1.00 15.95 ? 114 TYR B CB  1 
ATOM   2339 C  CG  . TYR B 1 126 ? -13.666 -9.691  37.558  1.00 14.69 ? 114 TYR B CG  1 
ATOM   2340 C  CD1 . TYR B 1 126 ? -15.060 -9.813  37.483  1.00 14.50 ? 114 TYR B CD1 1 
ATOM   2341 C  CD2 . TYR B 1 126 ? -13.118 -8.442  37.318  1.00 14.30 ? 114 TYR B CD2 1 
ATOM   2342 C  CE1 . TYR B 1 126 ? -15.851 -8.723  37.149  1.00 13.73 ? 114 TYR B CE1 1 
ATOM   2343 C  CE2 . TYR B 1 126 ? -13.903 -7.355  36.995  1.00 13.50 ? 114 TYR B CE2 1 
ATOM   2344 C  CZ  . TYR B 1 126 ? -15.278 -7.485  36.931  1.00 12.84 ? 114 TYR B CZ  1 
ATOM   2345 O  OH  . TYR B 1 126 ? -16.044 -6.401  36.620  1.00 16.38 ? 114 TYR B OH  1 
ATOM   2346 N  N   . LYS B 1 127 ? -10.427 -12.967 36.715  1.00 16.07 ? 115 LYS B N   1 
ATOM   2347 C  CA  . LYS B 1 127 ? -9.263  -13.709 37.213  1.00 15.82 ? 115 LYS B CA  1 
ATOM   2348 C  C   . LYS B 1 127 ? -8.647  -12.939 38.398  1.00 15.25 ? 115 LYS B C   1 
ATOM   2349 O  O   . LYS B 1 127 ? -8.441  -11.715 38.291  1.00 14.53 ? 115 LYS B O   1 
ATOM   2350 C  CB  . LYS B 1 127 ? -8.291  -13.934 36.054  1.00 17.78 ? 115 LYS B CB  1 
ATOM   2351 C  CG  . LYS B 1 127 ? -8.802  -14.964 35.039  1.00 19.52 ? 115 LYS B CG  1 
ATOM   2352 C  CD  . LYS B 1 127 ? -7.832  -15.206 33.921  1.00 22.39 ? 115 LYS B CD  1 
ATOM   2353 C  CE  . LYS B 1 127 ? -8.234  -16.360 33.025  1.00 24.27 ? 115 LYS B CE  1 
ATOM   2354 N  NZ  . LYS B 1 127 ? -7.294  -16.501 31.895  1.00 28.91 ? 115 LYS B NZ  1 
ATOM   2355 N  N   . ILE B 1 128 ? -8.338  -13.675 39.469  1.00 16.52 ? 116 ILE B N   1 
ATOM   2356 C  CA  . ILE B 1 128 ? -7.812  -13.139 40.750  1.00 16.82 ? 116 ILE B CA  1 
ATOM   2357 C  C   . ILE B 1 128 ? -6.307  -13.419 40.817  1.00 15.91 ? 116 ILE B C   1 
ATOM   2358 O  O   . ILE B 1 128 ? -5.887  -14.541 40.514  1.00 15.15 ? 116 ILE B O   1 
ATOM   2359 C  CB  . ILE B 1 128 ? -8.550  -13.757 41.951  1.00 17.25 ? 116 ILE B CB  1 
ATOM   2360 C  CG1 . ILE B 1 128 ? -10.040 -13.447 41.932  1.00 19.47 ? 116 ILE B CG1 1 
ATOM   2361 C  CG2 . ILE B 1 128 ? -7.908  -13.295 43.249  1.00 20.42 ? 116 ILE B CG2 1 
ATOM   2362 C  CD1 . ILE B 1 128 ? -10.850 -14.359 42.851  1.00 20.68 ? 116 ILE B CD1 1 
ATOM   2363 N  N   . TYR B 1 129 ? -5.512  -12.432 41.234  1.00 14.08 ? 117 TYR B N   1 
ATOM   2364 C  CA  . TYR B 1 129 ? -4.041  -12.584 41.305  1.00 13.75 ? 117 TYR B CA  1 
ATOM   2365 C  C   . TYR B 1 129 ? -3.559  -11.924 42.582  1.00 14.34 ? 117 TYR B C   1 
ATOM   2366 O  O   . TYR B 1 129 ? -4.224  -10.980 43.072  1.00 13.08 ? 117 TYR B O   1 
ATOM   2367 C  CB  . TYR B 1 129 ? -3.329  -11.913 40.127  1.00 14.16 ? 117 TYR B CB  1 
ATOM   2368 C  CG  . TYR B 1 129 ? -3.754  -12.365 38.753  1.00 15.49 ? 117 TYR B CG  1 
ATOM   2369 C  CD1 . TYR B 1 129 ? -4.900  -11.853 38.154  1.00 15.28 ? 117 TYR B CD1 1 
ATOM   2370 C  CD2 . TYR B 1 129 ? -2.954  -13.221 38.001  1.00 18.43 ? 117 TYR B CD2 1 
ATOM   2371 C  CE1 . TYR B 1 129 ? -5.281  -12.263 36.888  1.00 17.35 ? 117 TYR B CE1 1 
ATOM   2372 C  CE2 . TYR B 1 129 ? -3.339  -13.640 36.733  1.00 19.93 ? 117 TYR B CE2 1 
ATOM   2373 C  CZ  . TYR B 1 129 ? -4.497  -13.145 36.171  1.00 17.77 ? 117 TYR B CZ  1 
ATOM   2374 O  OH  . TYR B 1 129 ? -4.916  -13.552 34.928  1.00 19.79 ? 117 TYR B OH  1 
ATOM   2375 N  N   . GLN B 1 130 ? -2.371  -12.316 43.047  1.00 12.46 ? 118 GLN B N   1 
ATOM   2376 C  CA  . GLN B 1 130 ? -1.684  -11.588 44.109  1.00 15.31 ? 118 GLN B CA  1 
ATOM   2377 C  C   . GLN B 1 130 ? -0.226  -11.421 43.722  1.00 15.60 ? 118 GLN B C   1 
ATOM   2378 O  O   . GLN B 1 130 ? 0.307   -12.273 43.067  1.00 15.72 ? 118 GLN B O   1 
ATOM   2379 C  CB  . GLN B 1 130 ? -1.864  -12.231 45.487  1.00 17.68 ? 118 GLN B CB  1 
ATOM   2380 C  CG  . GLN B 1 130 ? -1.152  -13.558 45.745  1.00 20.74 ? 118 GLN B CG  1 
ATOM   2381 C  CD  . GLN B 1 130 ? -1.127  -13.839 47.236  1.00 21.40 ? 118 GLN B CD  1 
ATOM   2382 O  OE1 . GLN B 1 130 ? -1.081  -12.919 48.045  1.00 24.61 ? 118 GLN B OE1 1 
ATOM   2383 N  NE2 . GLN B 1 130 ? -1.218  -15.103 47.618  1.00 25.20 ? 118 GLN B NE2 1 
ATOM   2384 N  N   . THR B 1 131 ? 0.398   -10.359 44.189  1.00 17.32 ? 119 THR B N   1 
ATOM   2385 C  CA  . THR B 1 131 ? 1.872   -10.198 44.129  1.00 19.15 ? 119 THR B CA  1 
ATOM   2386 C  C   . THR B 1 131 ? 2.301   -9.325  45.295  1.00 20.11 ? 119 THR B C   1 
ATOM   2387 O  O   . THR B 1 131 ? 1.459   -9.028  46.168  1.00 17.85 ? 119 THR B O   1 
ATOM   2388 C  CB  . THR B 1 131 ? 2.305   -9.719  42.746  1.00 21.14 ? 119 THR B CB  1 
ATOM   2389 O  OG1 . THR B 1 131 ? 3.736   -9.768  42.688  1.00 24.20 ? 119 THR B OG1 1 
ATOM   2390 C  CG2 . THR B 1 131 ? 1.814   -8.327  42.415  1.00 22.20 ? 119 THR B CG2 1 
ATOM   2391 N  N   . THR B 1 132 ? 3.608   -9.125  45.428  1.00 22.21 ? 120 THR B N   1 
ATOM   2392 C  CA  . THR B 1 132 ? 4.220   -8.220  46.426  1.00 24.77 ? 120 THR B CA  1 
ATOM   2393 C  C   . THR B 1 132 ? 4.887   -7.075  45.658  1.00 24.59 ? 120 THR B C   1 
ATOM   2394 O  O   . THR B 1 132 ? 5.421   -7.285  44.512  1.00 25.47 ? 120 THR B O   1 
ATOM   2395 C  CB  . THR B 1 132 ? 5.185   -8.970  47.350  1.00 30.50 ? 120 THR B CB  1 
ATOM   2396 O  OG1 . THR B 1 132 ? 4.468   -10.055 47.938  1.00 34.63 ? 120 THR B OG1 1 
ATOM   2397 C  CG2 . THR B 1 132 ? 5.764   -8.102  48.452  1.00 32.84 ? 120 THR B CG2 1 
ATOM   2398 N  N   . ARG B 1 133 ? 4.790   -5.885  46.215  1.00 19.43 ? 121 ARG B N   1 
ATOM   2399 C  CA  . ARG B 1 133 ? 5.565   -4.714  45.768  1.00 21.93 ? 121 ARG B CA  1 
ATOM   2400 C  C   . ARG B 1 133 ? 6.612   -4.470  46.850  1.00 23.16 ? 121 ARG B C   1 
ATOM   2401 O  O   . ARG B 1 133 ? 6.238   -4.438  48.028  1.00 20.20 ? 121 ARG B O   1 
ATOM   2402 C  CB  . ARG B 1 133 ? 4.678   -3.493  45.543  1.00 24.30 ? 121 ARG B CB  1 
ATOM   2403 C  CG  . ARG B 1 133 ? 3.536   -3.750  44.566  1.00 29.24 ? 121 ARG B CG  1 
ATOM   2404 C  CD  . ARG B 1 133 ? 3.988   -3.590  43.132  1.00 34.88 ? 121 ARG B CD  1 
ATOM   2405 N  NE  . ARG B 1 133 ? 4.125   -2.178  42.838  1.00 34.51 ? 121 ARG B NE  1 
ATOM   2406 C  CZ  . ARG B 1 133 ? 5.252   -1.555  42.498  1.00 39.89 ? 121 ARG B CZ  1 
ATOM   2407 N  NH1 . ARG B 1 133 ? 6.398   -2.216  42.398  1.00 41.14 ? 121 ARG B NH1 1 
ATOM   2408 N  NH2 . ARG B 1 133 ? 5.217   -0.255  42.255  1.00 42.67 ? 121 ARG B NH2 1 
ATOM   2409 N  N   . GLU B 1 134 ? 7.873   -4.328  46.445  1.00 25.34 ? 122 GLU B N   1 
ATOM   2410 C  CA  . GLU B 1 134 ? 9.006   -4.163  47.393  1.00 25.57 ? 122 GLU B CA  1 
ATOM   2411 C  C   . GLU B 1 134 ? 9.514   -2.735  47.248  1.00 25.75 ? 122 GLU B C   1 
ATOM   2412 O  O   . GLU B 1 134 ? 9.661   -2.290  46.101  1.00 25.93 ? 122 GLU B O   1 
ATOM   2413 C  CB  . GLU B 1 134 ? 10.119  -5.177  47.092  1.00 31.17 ? 122 GLU B CB  1 
ATOM   2414 C  CG  . GLU B 1 134 ? 9.641   -6.614  47.019  1.00 37.27 ? 122 GLU B CG  1 
ATOM   2415 C  CD  . GLU B 1 134 ? 10.111  -7.374  45.783  1.00 49.01 ? 122 GLU B CD  1 
ATOM   2416 O  OE1 . GLU B 1 134 ? 10.763  -8.441  45.949  1.00 50.56 ? 122 GLU B OE1 1 
ATOM   2417 O  OE2 . GLU B 1 134 ? 9.824   -6.904  44.652  1.00 55.97 ? 122 GLU B OE2 1 
ATOM   2418 N  N   . ASN B 1 135 ? 9.691   -2.014  48.365  1.00 25.39 ? 123 ASN B N   1 
ATOM   2419 C  CA  . ASN B 1 135 ? 10.356  -0.690  48.390  1.00 26.22 ? 123 ASN B CA  1 
ATOM   2420 C  C   . ASN B 1 135 ? 9.671   0.223   47.364  1.00 27.95 ? 123 ASN B C   1 
ATOM   2421 O  O   . ASN B 1 135 ? 10.355  0.784   46.473  1.00 26.30 ? 123 ASN B O   1 
ATOM   2422 C  CB  . ASN B 1 135 ? 11.875  -0.881  48.209  1.00 32.25 ? 123 ASN B CB  1 
ATOM   2423 C  CG  . ASN B 1 135 ? 12.460  -1.836  49.235  1.00 33.08 ? 123 ASN B CG  1 
ATOM   2424 O  OD1 . ASN B 1 135 ? 12.405  -1.583  50.436  1.00 34.24 ? 123 ASN B OD1 1 
ATOM   2425 N  ND2 . ASN B 1 135 ? 12.993  -2.962  48.792  1.00 34.55 ? 123 ASN B ND2 1 
ATOM   2426 N  N   . ALA B 1 136 ? 8.346   0.345   47.450  1.00 22.14 ? 124 ALA B N   1 
ATOM   2427 C  CA  . ALA B 1 136 ? 7.513   0.983   46.414  1.00 21.92 ? 124 ALA B CA  1 
ATOM   2428 C  C   . ALA B 1 136 ? 6.726   2.126   47.025  1.00 21.95 ? 124 ALA B C   1 
ATOM   2429 O  O   . ALA B 1 136 ? 6.455   2.123   48.232  1.00 19.70 ? 124 ALA B O   1 
ATOM   2430 C  CB  . ALA B 1 136 ? 6.572   -0.023  45.799  1.00 20.55 ? 124 ALA B CB  1 
ATOM   2431 N  N   . PRO B 1 137 ? 6.248   3.082   46.190  1.00 23.95 ? 125 PRO B N   1 
ATOM   2432 C  CA  . PRO B 1 137 ? 5.462   4.201   46.686  1.00 23.22 ? 125 PRO B CA  1 
ATOM   2433 C  C   . PRO B 1 137 ? 4.155   3.603   47.214  1.00 23.25 ? 125 PRO B C   1 
ATOM   2434 O  O   . PRO B 1 137 ? 3.696   2.639   46.630  1.00 24.70 ? 125 PRO B O   1 
ATOM   2435 C  CB  . PRO B 1 137 ? 5.257   5.111   45.463  1.00 27.23 ? 125 PRO B CB  1 
ATOM   2436 C  CG  . PRO B 1 137 ? 6.228   4.576   44.412  1.00 28.17 ? 125 PRO B CG  1 
ATOM   2437 C  CD  . PRO B 1 137 ? 6.367   3.102   44.718  1.00 28.54 ? 125 PRO B CD  1 
ATOM   2438 N  N   . SER B 1 138 ? 3.649   4.139   48.317  1.00 22.01 ? 126 SER B N   1 
ATOM   2439 C  CA  . SER B 1 138 ? 2.411   3.691   49.002  1.00 21.01 ? 126 SER B CA  1 
ATOM   2440 C  C   . SER B 1 138 ? 1.793   4.898   49.680  1.00 20.68 ? 126 SER B C   1 
ATOM   2441 O  O   . SER B 1 138 ? 2.468   5.947   49.783  1.00 20.32 ? 126 SER B O   1 
ATOM   2442 C  CB  . SER B 1 138 ? 2.708   2.585   49.990  1.00 20.90 ? 126 SER B CB  1 
ATOM   2443 O  OG  . SER B 1 138 ? 3.056   3.147   51.241  1.00 19.16 ? 126 SER B OG  1 
ATOM   2444 N  N   . ILE B 1 139 ? 0.607   4.740   50.242  1.00 19.84 ? 127 ILE B N   1 
ATOM   2445 C  CA  . ILE B 1 139 ? -0.043  5.841   50.994  1.00 20.89 ? 127 ILE B CA  1 
ATOM   2446 C  C   . ILE B 1 139 ? 0.710   6.077   52.309  1.00 21.73 ? 127 ILE B C   1 
ATOM   2447 O  O   . ILE B 1 139 ? 0.384   7.063   52.962  1.00 23.69 ? 127 ILE B O   1 
ATOM   2448 C  CB  . ILE B 1 139 ? -1.537  5.574   51.242  1.00 22.02 ? 127 ILE B CB  1 
ATOM   2449 C  CG1 . ILE B 1 139 ? -1.770  4.220   51.923  1.00 20.46 ? 127 ILE B CG1 1 
ATOM   2450 C  CG2 . ILE B 1 139 ? -2.334  5.745   49.956  1.00 23.37 ? 127 ILE B CG2 1 
ATOM   2451 C  CD1 . ILE B 1 139 ? -3.148  4.054   52.566  1.00 20.99 ? 127 ILE B CD1 1 
ATOM   2452 N  N   . GLU B 1 140 ? 1.623   5.191   52.717  1.00 22.93 ? 128 GLU B N   1 
ATOM   2453 C  CA  . GLU B 1 140 ? 2.380   5.344   53.991  1.00 22.11 ? 128 GLU B CA  1 
ATOM   2454 C  C   . GLU B 1 140 ? 3.850   5.690   53.730  1.00 23.08 ? 128 GLU B C   1 
ATOM   2455 O  O   . GLU B 1 140 ? 4.610   5.717   54.720  1.00 23.31 ? 128 GLU B O   1 
ATOM   2456 C  CB  . GLU B 1 140 ? 2.283   4.055   54.803  1.00 25.62 ? 128 GLU B CB  1 
ATOM   2457 C  CG  . GLU B 1 140 ? 0.883   3.743   55.302  1.00 28.16 ? 128 GLU B CG  1 
ATOM   2458 C  CD  . GLU B 1 140 ? 0.264   4.791   56.202  1.00 34.85 ? 128 GLU B CD  1 
ATOM   2459 O  OE1 . GLU B 1 140 ? -0.780  4.492   56.835  1.00 36.84 ? 128 GLU B OE1 1 
ATOM   2460 O  OE2 . GLU B 1 140 ? 0.850   5.901   56.306  1.00 42.07 ? 128 GLU B OE2 1 
ATOM   2461 N  N   . GLY B 1 141 ? 4.209   6.013   52.484  1.00 19.86 ? 129 GLY B N   1 
ATOM   2462 C  CA  . GLY B 1 141 ? 5.601   6.212   52.025  1.00 20.51 ? 129 GLY B CA  1 
ATOM   2463 C  C   . GLY B 1 141 ? 6.191   4.956   51.394  1.00 21.31 ? 129 GLY B C   1 
ATOM   2464 O  O   . GLY B 1 141 ? 5.437   3.977   51.125  1.00 19.92 ? 129 GLY B O   1 
ATOM   2465 N  N   . THR B 1 142 ? 7.503   4.952   51.129  1.00 17.30 ? 130 THR B N   1 
ATOM   2466 C  CA  . THR B 1 142 ? 8.178   3.773   50.578  1.00 18.07 ? 130 THR B CA  1 
ATOM   2467 C  C   . THR B 1 142 ? 7.904   2.573   51.474  1.00 18.98 ? 130 THR B C   1 
ATOM   2468 O  O   . THR B 1 142 ? 8.160   2.642   52.693  1.00 19.58 ? 130 THR B O   1 
ATOM   2469 C  CB  . THR B 1 142 ? 9.685   3.982   50.409  1.00 20.57 ? 130 THR B CB  1 
ATOM   2470 O  OG1 . THR B 1 142 ? 9.762   5.188   49.655  1.00 21.88 ? 130 THR B OG1 1 
ATOM   2471 C  CG2 . THR B 1 142 ? 10.331  2.804   49.734  1.00 21.95 ? 130 THR B CG2 1 
ATOM   2472 N  N   . ALA B 1 143 ? 7.343   1.517   50.897  1.00 16.07 ? 131 ALA B N   1 
ATOM   2473 C  CA  . ALA B 1 143 ? 6.933   0.356   51.699  1.00 15.86 ? 131 ALA B CA  1 
ATOM   2474 C  C   . ALA B 1 143 ? 6.929   -0.949  50.880  1.00 15.96 ? 131 ALA B C   1 
ATOM   2475 O  O   . ALA B 1 143 ? 7.008   -0.931  49.656  1.00 17.83 ? 131 ALA B O   1 
ATOM   2476 C  CB  . ALA B 1 143 ? 5.557   0.696   52.278  1.00 13.91 ? 131 ALA B CB  1 
ATOM   2477 N  N   . THR B 1 144 ? 6.793   -2.066  51.580  1.00 16.37 ? 132 THR B N   1 
ATOM   2478 C  CA  . THR B 1 144 ? 6.614   -3.415  50.992  1.00 18.11 ? 132 THR B CA  1 
ATOM   2479 C  C   . THR B 1 144 ? 5.215   -3.896  51.351  1.00 18.69 ? 132 THR B C   1 
ATOM   2480 O  O   . THR B 1 144 ? 4.826   -3.778  52.530  1.00 20.79 ? 132 THR B O   1 
ATOM   2481 C  CB  . THR B 1 144 ? 7.732   -4.344  51.469  1.00 20.15 ? 132 THR B CB  1 
ATOM   2482 O  OG1 . THR B 1 144 ? 8.941   -3.867  50.853  1.00 20.08 ? 132 THR B OG1 1 
ATOM   2483 C  CG2 . THR B 1 144 ? 7.423   -5.782  51.150  1.00 20.12 ? 132 THR B CG2 1 
ATOM   2484 N  N   . PHE B 1 145 ? 4.426   -4.289  50.362  1.00 16.04 ? 133 PHE B N   1 
ATOM   2485 C  CA  . PHE B 1 145 ? 2.982   -4.507  50.618  1.00 15.60 ? 133 PHE B CA  1 
ATOM   2486 C  C   . PHE B 1 145 ? 2.450   -5.479  49.578  1.00 14.98 ? 133 PHE B C   1 
ATOM   2487 O  O   . PHE B 1 145 ? 3.067   -5.661  48.524  1.00 15.41 ? 133 PHE B O   1 
ATOM   2488 C  CB  . PHE B 1 145 ? 2.213   -3.181  50.625  1.00 16.77 ? 133 PHE B CB  1 
ATOM   2489 C  CG  . PHE B 1 145 ? 2.429   -2.325  49.398  1.00 15.19 ? 133 PHE B CG  1 
ATOM   2490 C  CD1 . PHE B 1 145 ? 1.637   -2.492  48.274  1.00 14.83 ? 133 PHE B CD1 1 
ATOM   2491 C  CD2 . PHE B 1 145 ? 3.437   -1.382  49.353  1.00 15.17 ? 133 PHE B CD2 1 
ATOM   2492 C  CE1 . PHE B 1 145 ? 1.840   -1.732  47.141  1.00 15.61 ? 133 PHE B CE1 1 
ATOM   2493 C  CE2 . PHE B 1 145 ? 3.629   -0.598  48.228  1.00 15.37 ? 133 PHE B CE2 1 
ATOM   2494 C  CZ  . PHE B 1 145 ? 2.845   -0.794  47.108  1.00 15.22 ? 133 PHE B CZ  1 
ATOM   2495 N  N   . ASN B 1 146 ? 1.353   -6.139  49.924  1.00 15.54 ? 134 ASN B N   1 
ATOM   2496 C  CA  . ASN B 1 146 ? 0.690   -7.069  48.986  1.00 16.15 ? 134 ASN B CA  1 
ATOM   2497 C  C   . ASN B 1 146 ? -0.122  -6.231  47.983  1.00 14.40 ? 134 ASN B C   1 
ATOM   2498 O  O   . ASN B 1 146 ? -0.659  -5.180  48.351  1.00 12.90 ? 134 ASN B O   1 
ATOM   2499 C  CB  . ASN B 1 146 ? -0.237  -8.033  49.725  1.00 21.16 ? 134 ASN B CB  1 
ATOM   2500 C  CG  . ASN B 1 146 ? 0.452   -9.150  50.500  1.00 24.85 ? 134 ASN B CG  1 
ATOM   2501 O  OD1 . ASN B 1 146 ? 1.619   -9.473  50.268  1.00 28.93 ? 134 ASN B OD1 1 
ATOM   2502 N  ND2 . ASN B 1 146 ? -0.319  -9.796  51.361  1.00 27.33 ? 134 ASN B ND2 1 
ATOM   2503 N  N   . GLN B 1 147 ? -0.245  -6.726  46.754  1.00 13.25 ? 135 GLN B N   1 
ATOM   2504 C  CA  . GLN B 1 147 ? -1.056  -6.130  45.693  1.00 13.69 ? 135 GLN B CA  1 
ATOM   2505 C  C   . GLN B 1 147 ? -2.009  -7.199  45.180  1.00 13.82 ? 135 GLN B C   1 
ATOM   2506 O  O   . GLN B 1 147 ? -1.545  -8.304  44.841  1.00 15.10 ? 135 GLN B O   1 
ATOM   2507 C  CB  . GLN B 1 147 ? -0.082  -5.602  44.641  1.00 14.32 ? 135 GLN B CB  1 
ATOM   2508 C  CG  . GLN B 1 147 ? -0.740  -4.719  43.616  1.00 14.74 ? 135 GLN B CG  1 
ATOM   2509 C  CD  . GLN B 1 147 ? 0.248   -4.365  42.536  1.00 16.52 ? 135 GLN B CD  1 
ATOM   2510 O  OE1 . GLN B 1 147 ? 0.780   -5.265  41.918  1.00 17.05 ? 135 GLN B OE1 1 
ATOM   2511 N  NE2 . GLN B 1 147 ? 0.463   -3.073  42.264  1.00 17.10 ? 135 GLN B NE2 1 
ATOM   2512 N  N   . TYR B 1 148 ? -3.313  -6.922  45.159  1.00 12.74 ? 136 TYR B N   1 
ATOM   2513 C  CA  . TYR B 1 148 ? -4.327  -7.898  44.744  1.00 12.10 ? 136 TYR B CA  1 
ATOM   2514 C  C   . TYR B 1 148 ? -5.014  -7.350  43.498  1.00 13.61 ? 136 TYR B C   1 
ATOM   2515 O  O   . TYR B 1 148 ? -5.156  -6.116  43.329  1.00 12.08 ? 136 TYR B O   1 
ATOM   2516 C  CB  . TYR B 1 148 ? -5.396  -8.151  45.796  1.00 12.37 ? 136 TYR B CB  1 
ATOM   2517 C  CG  . TYR B 1 148 ? -4.903  -8.576  47.154  1.00 12.64 ? 136 TYR B CG  1 
ATOM   2518 C  CD1 . TYR B 1 148 ? -3.694  -9.230  47.312  1.00 14.15 ? 136 TYR B CD1 1 
ATOM   2519 C  CD2 . TYR B 1 148 ? -5.683  -8.384  48.276  1.00 13.94 ? 136 TYR B CD2 1 
ATOM   2520 C  CE1 . TYR B 1 148 ? -3.232  -9.594  48.567  1.00 15.23 ? 136 TYR B CE1 1 
ATOM   2521 C  CE2 . TYR B 1 148 ? -5.224  -8.725  49.544  1.00 15.72 ? 136 TYR B CE2 1 
ATOM   2522 C  CZ  . TYR B 1 148 ? -3.998  -9.342  49.687  1.00 15.96 ? 136 TYR B CZ  1 
ATOM   2523 O  OH  . TYR B 1 148 ? -3.517  -9.713  50.923  1.00 18.03 ? 136 TYR B OH  1 
ATOM   2524 N  N   . TRP B 1 149 ? -5.321  -8.269  42.612  1.00 13.53 ? 137 TRP B N   1 
ATOM   2525 C  CA  . TRP B 1 149 ? -5.930  -7.951  41.302  1.00 14.07 ? 137 TRP B CA  1 
ATOM   2526 C  C   . TRP B 1 149 ? -7.195  -8.768  41.085  1.00 14.72 ? 137 TRP B C   1 
ATOM   2527 O  O   . TRP B 1 149 ? -7.151  -10.013 41.272  1.00 14.34 ? 137 TRP B O   1 
ATOM   2528 C  CB  . TRP B 1 149 ? -4.916  -8.266  40.199  1.00 13.13 ? 137 TRP B CB  1 
ATOM   2529 C  CG  . TRP B 1 149 ? -3.670  -7.458  40.243  1.00 13.69 ? 137 TRP B CG  1 
ATOM   2530 C  CD1 . TRP B 1 149 ? -2.553  -7.734  40.983  1.00 13.46 ? 137 TRP B CD1 1 
ATOM   2531 C  CD2 . TRP B 1 149 ? -3.377  -6.266  39.504  1.00 13.12 ? 137 TRP B CD2 1 
ATOM   2532 N  NE1 . TRP B 1 149 ? -1.604  -6.794  40.742  1.00 14.94 ? 137 TRP B NE1 1 
ATOM   2533 C  CE2 . TRP B 1 149 ? -2.078  -5.868  39.857  1.00 12.82 ? 137 TRP B CE2 1 
ATOM   2534 C  CE3 . TRP B 1 149 ? -4.105  -5.470  38.623  1.00 13.59 ? 137 TRP B CE3 1 
ATOM   2535 C  CZ2 . TRP B 1 149 ? -1.485  -4.720  39.345  1.00 13.42 ? 137 TRP B CZ2 1 
ATOM   2536 C  CZ3 . TRP B 1 149 ? -3.516  -4.340  38.106  1.00 15.11 ? 137 TRP B CZ3 1 
ATOM   2537 C  CH2 . TRP B 1 149 ? -2.214  -3.967  38.463  1.00 13.72 ? 137 TRP B CH2 1 
ATOM   2538 N  N   . SER B 1 150 ? -8.237  -8.127  40.529  1.00 13.21 ? 138 SER B N   1 
ATOM   2539 C  CA  . SER B 1 150 ? -9.365  -8.825  39.866  1.00 12.99 ? 138 SER B CA  1 
ATOM   2540 C  C   . SER B 1 150 ? -9.370  -8.319  38.440  1.00 12.26 ? 138 SER B C   1 
ATOM   2541 O  O   . SER B 1 150 ? -9.434  -7.103  38.301  1.00 11.22 ? 138 SER B O   1 
ATOM   2542 C  CB  . SER B 1 150 ? -10.674 -8.526  40.470  1.00 13.11 ? 138 SER B CB  1 
ATOM   2543 O  OG  . SER B 1 150 ? -10.991 -9.403  41.482  1.00 17.94 ? 138 SER B OG  1 
ATOM   2544 N  N   . VAL B 1 151 ? -9.196  -9.183  37.423  1.00 12.58 ? 139 VAL B N   1 
ATOM   2545 C  CA  . VAL B 1 151 ? -9.055  -8.688  36.028  1.00 11.98 ? 139 VAL B CA  1 
ATOM   2546 C  C   . VAL B 1 151 ? -10.205 -9.244  35.179  1.00 13.48 ? 139 VAL B C   1 
ATOM   2547 O  O   . VAL B 1 151 ? -10.236 -10.477 35.007  1.00 13.11 ? 139 VAL B O   1 
ATOM   2548 C  CB  . VAL B 1 151 ? -7.680  -9.000  35.412  1.00 11.60 ? 139 VAL B CB  1 
ATOM   2549 C  CG1 . VAL B 1 151 ? -7.574  -8.357  34.062  1.00 12.24 ? 139 VAL B CG1 1 
ATOM   2550 C  CG2 . VAL B 1 151 ? -6.527  -8.531  36.296  1.00 11.95 ? 139 VAL B CG2 1 
ATOM   2551 N  N   . ARG B 1 152 ? -11.067 -8.368  34.652  1.00 12.37 ? 140 ARG B N   1 
ATOM   2552 C  CA  . ARG B 1 152 ? -12.275 -8.765  33.870  1.00 14.49 ? 140 ARG B CA  1 
ATOM   2553 C  C   . ARG B 1 152 ? -11.810 -9.438  32.574  1.00 15.63 ? 140 ARG B C   1 
ATOM   2554 O  O   . ARG B 1 152 ? -10.952 -8.881  31.894  1.00 16.13 ? 140 ARG B O   1 
ATOM   2555 C  CB  . ARG B 1 152 ? -13.163 -7.563  33.583  1.00 14.61 ? 140 ARG B CB  1 
ATOM   2556 C  CG  . ARG B 1 152 ? -14.598 -7.938  33.205  1.00 15.85 ? 140 ARG B CG  1 
ATOM   2557 C  CD  . ARG B 1 152 ? -15.482 -6.723  33.097  1.00 16.08 ? 140 ARG B CD  1 
ATOM   2558 N  NE  . ARG B 1 152 ? -16.807 -7.063  32.577  1.00 16.95 ? 140 ARG B NE  1 
ATOM   2559 C  CZ  . ARG B 1 152 ? -17.907 -7.266  33.296  1.00 17.93 ? 140 ARG B CZ  1 
ATOM   2560 N  NH1 . ARG B 1 152 ? -17.956 -7.093  34.605  1.00 16.85 ? 140 ARG B NH1 1 
ATOM   2561 N  NH2 . ARG B 1 152 ? -19.034 -7.549  32.656  1.00 17.84 ? 140 ARG B NH2 1 
ATOM   2562 N  N   . THR B 1 153 ? -12.448 -10.542 32.188  1.00 17.27 ? 141 THR B N   1 
ATOM   2563 C  CA  . THR B 1 153 ? -12.062 -11.303 30.977  1.00 19.97 ? 141 THR B CA  1 
ATOM   2564 C  C   . THR B 1 153 ? -12.678 -10.593 29.751  1.00 21.47 ? 141 THR B C   1 
ATOM   2565 O  O   . THR B 1 153 ? -12.046 -10.629 28.667  1.00 25.20 ? 141 THR B O   1 
ATOM   2566 C  CB  . THR B 1 153 ? -12.395 -12.785 31.171  1.00 22.49 ? 141 THR B CB  1 
ATOM   2567 O  OG1 . THR B 1 153 ? -13.815 -12.882 31.214  1.00 23.82 ? 141 THR B OG1 1 
ATOM   2568 C  CG2 . THR B 1 153 ? -11.794 -13.413 32.403  1.00 24.77 ? 141 THR B CG2 1 
ATOM   2569 N  N   . ASP B 1 154 ? -13.842 -9.957  29.895  1.00 20.86 ? 142 ASP B N   1 
ATOM   2570 C  CA  . ASP B 1 154 ? -14.484 -9.177  28.794  1.00 22.38 ? 142 ASP B CA  1 
ATOM   2571 C  C   . ASP B 1 154 ? -14.416 -7.691  29.140  1.00 21.29 ? 142 ASP B C   1 
ATOM   2572 O  O   . ASP B 1 154 ? -15.223 -7.218  29.975  1.00 20.17 ? 142 ASP B O   1 
ATOM   2573 C  CB  . ASP B 1 154 ? -15.935 -9.567  28.544  1.00 25.44 ? 142 ASP B CB  1 
ATOM   2574 C  CG  . ASP B 1 154 ? -16.566 -8.714  27.449  1.00 25.29 ? 142 ASP B CG  1 
ATOM   2575 O  OD1 . ASP B 1 154 ? -15.822 -8.237  26.579  1.00 29.20 ? 142 ASP B OD1 1 
ATOM   2576 O  OD2 . ASP B 1 154 ? -17.769 -8.492  27.512  1.00 32.66 ? 142 ASP B OD2 1 
ATOM   2577 N  N   . HIS B 1 155 ? -13.519 -6.969  28.473  1.00 20.08 ? 143 HIS B N   1 
ATOM   2578 C  CA  . HIS B 1 155 ? -13.243 -5.564  28.836  1.00 20.16 ? 143 HIS B CA  1 
ATOM   2579 C  C   . HIS B 1 155 ? -14.465 -4.687  28.630  1.00 20.19 ? 143 HIS B C   1 
ATOM   2580 O  O   . HIS B 1 155 ? -15.238 -4.882  27.658  1.00 17.13 ? 143 HIS B O   1 
ATOM   2581 C  CB  . HIS B 1 155 ? -12.037 -5.061  28.072  1.00 19.91 ? 143 HIS B CB  1 
ATOM   2582 C  CG  . HIS B 1 155 ? -10.820 -5.789  28.481  1.00 21.33 ? 143 HIS B CG  1 
ATOM   2583 N  ND1 . HIS B 1 155 ? -9.630  -5.584  27.880  1.00 20.20 ? 143 HIS B ND1 1 
ATOM   2584 C  CD2 . HIS B 1 155 ? -10.623 -6.729  29.423  1.00 19.49 ? 143 HIS B CD2 1 
ATOM   2585 C  CE1 . HIS B 1 155 ? -8.734  -6.374  28.402  1.00 20.99 ? 143 HIS B CE1 1 
ATOM   2586 N  NE2 . HIS B 1 155 ? -9.323  -7.095  29.347  1.00 23.06 ? 143 HIS B NE2 1 
ATOM   2587 N  N   . ARG B 1 156 ? -14.627 -3.705  29.504  1.00 15.82 ? 144 ARG B N   1 
ATOM   2588 C  CA  . ARG B 1 156 ? -15.764 -2.771  29.396  1.00 17.40 ? 144 ARG B CA  1 
ATOM   2589 C  C   . ARG B 1 156 ? -15.412 -1.413  29.982  1.00 17.29 ? 144 ARG B C   1 
ATOM   2590 O  O   . ARG B 1 156 ? -14.471 -1.303  30.796  1.00 17.91 ? 144 ARG B O   1 
ATOM   2591 C  CB  . ARG B 1 156 ? -17.002 -3.353  30.068  1.00 17.86 ? 144 ARG B CB  1 
ATOM   2592 C  CG  . ARG B 1 156 ? -16.964 -3.386  31.569  1.00 17.53 ? 144 ARG B CG  1 
ATOM   2593 C  CD  . ARG B 1 156 ? -18.291 -3.848  32.153  1.00 18.22 ? 144 ARG B CD  1 
ATOM   2594 N  NE  . ARG B 1 156 ? -18.095 -3.844  33.574  1.00 17.35 ? 144 ARG B NE  1 
ATOM   2595 C  CZ  . ARG B 1 156 ? -19.051 -3.973  34.485  1.00 19.49 ? 144 ARG B CZ  1 
ATOM   2596 N  NH1 . ARG B 1 156 ? -20.312 -4.161  34.122  1.00 19.93 ? 144 ARG B NH1 1 
ATOM   2597 N  NH2 . ARG B 1 156 ? -18.734 -3.870  35.756  1.00 18.84 ? 144 ARG B NH2 1 
ATOM   2598 N  N   . VAL B 1 157 ? -16.149 -0.409  29.525  1.00 17.35 ? 145 VAL B N   1 
ATOM   2599 C  CA  . VAL B 1 157 ? -16.043 0.958   30.063  1.00 14.88 ? 145 VAL B CA  1 
ATOM   2600 C  C   . VAL B 1 157 ? -17.423 1.346   30.568  1.00 16.92 ? 145 VAL B C   1 
ATOM   2601 O  O   . VAL B 1 157 ? -18.293 1.660   29.741  1.00 20.76 ? 145 VAL B O   1 
ATOM   2602 C  CB  . VAL B 1 157 ? -15.496 1.937   29.035  1.00 14.65 ? 145 VAL B CB  1 
ATOM   2603 C  CG1 . VAL B 1 157 ? -15.449 3.341   29.632  1.00 14.24 ? 145 VAL B CG1 1 
ATOM   2604 C  CG2 . VAL B 1 157 ? -14.123 1.461   28.537  1.00 15.45 ? 145 VAL B CG2 1 
ATOM   2605 N  N   . GLY B 1 158 ? -17.588 1.339   31.872  1.00 19.84 ? 146 GLY B N   1 
ATOM   2606 C  CA  . GLY B 1 158 ? -18.852 1.722   32.515  1.00 21.27 ? 146 GLY B CA  1 
ATOM   2607 C  C   . GLY B 1 158 ? -19.574 0.502   33.021  1.00 22.78 ? 146 GLY B C   1 
ATOM   2608 O  O   . GLY B 1 158 ? -19.060 -0.631  32.896  1.00 23.88 ? 146 GLY B O   1 
ATOM   2609 N  N   . GLY B 1 159 ? -20.701 0.718   33.679  1.00 26.05 ? 147 GLY B N   1 
ATOM   2610 C  CA  . GLY B 1 159 ? -21.382 -0.369  34.389  1.00 24.90 ? 147 GLY B CA  1 
ATOM   2611 C  C   . GLY B 1 159 ? -21.222 -0.254  35.888  1.00 22.28 ? 147 GLY B C   1 
ATOM   2612 O  O   . GLY B 1 159 ? -20.887 0.820   36.410  1.00 23.56 ? 147 GLY B O   1 
ATOM   2613 N  N   . THR B 1 160 ? -21.483 -1.354  36.568  1.00 18.83 ? 148 THR B N   1 
ATOM   2614 C  CA  . THR B 1 160 ? -21.576 -1.410  38.042  1.00 19.02 ? 148 THR B CA  1 
ATOM   2615 C  C   . THR B 1 160 ? -20.524 -2.386  38.521  1.00 15.52 ? 148 THR B C   1 
ATOM   2616 O  O   . THR B 1 160 ? -20.330 -3.407  37.874  1.00 16.28 ? 148 THR B O   1 
ATOM   2617 C  CB  . THR B 1 160 ? -22.941 -1.948  38.499  1.00 21.56 ? 148 THR B CB  1 
ATOM   2618 O  OG1 . THR B 1 160 ? -23.891 -1.044  37.938  1.00 23.29 ? 148 THR B OG1 1 
ATOM   2619 C  CG2 . THR B 1 160 ? -23.070 -1.999  39.997  1.00 22.53 ? 148 THR B CG2 1 
ATOM   2620 N  N   . VAL B 1 161 ? -19.847 -2.033  39.592  1.00 14.14 ? 149 VAL B N   1 
ATOM   2621 C  CA  . VAL B 1 161 ? -18.839 -2.905  40.226  1.00 13.51 ? 149 VAL B CA  1 
ATOM   2622 C  C   . VAL B 1 161 ? -19.273 -3.086  41.669  1.00 14.06 ? 149 VAL B C   1 
ATOM   2623 O  O   . VAL B 1 161 ? -19.335 -2.055  42.407  1.00 14.41 ? 149 VAL B O   1 
ATOM   2624 C  CB  . VAL B 1 161 ? -17.418 -2.323  40.167  1.00 15.13 ? 149 VAL B CB  1 
ATOM   2625 C  CG1 . VAL B 1 161 ? -16.460 -3.161  40.975  1.00 16.81 ? 149 VAL B CG1 1 
ATOM   2626 C  CG2 . VAL B 1 161 ? -16.941 -2.118  38.740  1.00 17.91 ? 149 VAL B CG2 1 
ATOM   2627 N  N   . THR B 1 162 ? -19.686 -4.307  41.983  1.00 13.71 ? 150 THR B N   1 
ATOM   2628 C  CA  . THR B 1 162 ? -20.107 -4.698  43.334  1.00 15.45 ? 150 THR B CA  1 
ATOM   2629 C  C   . THR B 1 162 ? -18.831 -5.079  44.081  1.00 14.82 ? 150 THR B C   1 
ATOM   2630 O  O   . THR B 1 162 ? -18.454 -6.281  44.037  1.00 16.18 ? 150 THR B O   1 
ATOM   2631 C  CB  . THR B 1 162 ? -21.135 -5.823  43.290  1.00 18.55 ? 150 THR B CB  1 
ATOM   2632 O  OG1 . THR B 1 162 ? -22.153 -5.403  42.367  1.00 21.17 ? 150 THR B OG1 1 
ATOM   2633 C  CG2 . THR B 1 162 ? -21.677 -6.121  44.679  1.00 18.77 ? 150 THR B CG2 1 
ATOM   2634 N  N   . THR B 1 163 ? -18.191 -4.098  44.705  1.00 16.56 ? 151 THR B N   1 
ATOM   2635 C  CA  . THR B 1 163 ? -16.826 -4.268  45.268  1.00 15.26 ? 151 THR B CA  1 
ATOM   2636 C  C   . THR B 1 163 ? -16.859 -5.400  46.305  1.00 15.99 ? 151 THR B C   1 
ATOM   2637 O  O   . THR B 1 163 ? -15.856 -6.131  46.436  1.00 15.16 ? 151 THR B O   1 
ATOM   2638 C  CB  . THR B 1 163 ? -16.230 -2.948  45.781  1.00 17.04 ? 151 THR B CB  1 
ATOM   2639 O  OG1 . THR B 1 163 ? -17.044 -2.457  46.850  1.00 16.11 ? 151 THR B OG1 1 
ATOM   2640 C  CG2 . THR B 1 163 ? -16.075 -1.893  44.686  1.00 15.54 ? 151 THR B CG2 1 
ATOM   2641 N  N   . GLN B 1 164 ? -17.934 -5.507  47.088  1.00 15.75 ? 152 GLN B N   1 
ATOM   2642 C  CA  . GLN B 1 164 ? -17.984 -6.519  48.165  1.00 19.21 ? 152 GLN B CA  1 
ATOM   2643 C  C   . GLN B 1 164 ? -17.757 -7.922  47.587  1.00 17.53 ? 152 GLN B C   1 
ATOM   2644 O  O   . GLN B 1 164 ? -17.139 -8.739  48.274  1.00 16.81 ? 152 GLN B O   1 
ATOM   2645 C  CB  . GLN B 1 164 ? -19.300 -6.426  48.929  1.00 22.11 ? 152 GLN B CB  1 
ATOM   2646 C  CG  . GLN B 1 164 ? -19.349 -7.355  50.125  1.00 28.40 ? 152 GLN B CG  1 
ATOM   2647 C  CD  . GLN B 1 164 ? -18.194 -7.128  51.066  1.00 33.70 ? 152 GLN B CD  1 
ATOM   2648 O  OE1 . GLN B 1 164 ? -17.723 -6.007  51.256  1.00 44.03 ? 152 GLN B OE1 1 
ATOM   2649 N  NE2 . GLN B 1 164 ? -17.707 -8.203  51.662  1.00 42.68 ? 152 GLN B NE2 1 
ATOM   2650 N  N   . ASN B 1 165 ? -18.244 -8.216  46.372  1.00 16.69 ? 153 ASN B N   1 
ATOM   2651 C  CA  . ASN B 1 165 ? -18.070 -9.521  45.696  1.00 16.39 ? 153 ASN B CA  1 
ATOM   2652 C  C   . ASN B 1 165 ? -16.570 -9.781  45.445  1.00 17.71 ? 153 ASN B C   1 
ATOM   2653 O  O   . ASN B 1 165 ? -16.162 -10.957 45.607  1.00 17.05 ? 153 ASN B O   1 
ATOM   2654 C  CB  . ASN B 1 165 ? -18.877 -9.657  44.400  1.00 16.45 ? 153 ASN B CB  1 
ATOM   2655 C  CG  . ASN B 1 165 ? -20.361 -9.765  44.675  1.00 19.05 ? 153 ASN B CG  1 
ATOM   2656 O  OD1 . ASN B 1 165 ? -20.744 -10.058 45.809  1.00 22.80 ? 153 ASN B OD1 1 
ATOM   2657 N  ND2 . ASN B 1 165 ? -21.196 -9.545  43.667  1.00 19.54 ? 153 ASN B ND2 1 
ATOM   2658 N  N   . HIS B 1 166 ? -15.774 -8.770  45.065  1.00 15.64 ? 154 HIS B N   1 
ATOM   2659 C  CA  . HIS B 1 166 ? -14.310 -8.928  44.872  1.00 15.51 ? 154 HIS B CA  1 
ATOM   2660 C  C   . HIS B 1 166 ? -13.611 -9.173  46.208  1.00 16.04 ? 154 HIS B C   1 
ATOM   2661 O  O   . HIS B 1 166 ? -12.788 -10.126 46.305  1.00 16.66 ? 154 HIS B O   1 
ATOM   2662 C  CB  . HIS B 1 166 ? -13.741 -7.702  44.132  1.00 15.59 ? 154 HIS B CB  1 
ATOM   2663 C  CG  . HIS B 1 166 ? -14.294 -7.615  42.763  1.00 14.29 ? 154 HIS B CG  1 
ATOM   2664 N  ND1 . HIS B 1 166 ? -13.712 -8.284  41.715  1.00 14.13 ? 154 HIS B ND1 1 
ATOM   2665 C  CD2 . HIS B 1 166 ? -15.408 -7.023  42.290  1.00 16.65 ? 154 HIS B CD2 1 
ATOM   2666 C  CE1 . HIS B 1 166 ? -14.409 -8.049  40.621  1.00 15.26 ? 154 HIS B CE1 1 
ATOM   2667 N  NE2 . HIS B 1 166 ? -15.457 -7.274  40.932  1.00 15.41 ? 154 HIS B NE2 1 
ATOM   2668 N  N   . PHE B 1 167 ? -13.924 -8.365  47.217  1.00 16.11 ? 155 PHE B N   1 
ATOM   2669 C  CA  . PHE B 1 167 ? -13.271 -8.455  48.544  1.00 16.48 ? 155 PHE B CA  1 
ATOM   2670 C  C   . PHE B 1 167 ? -13.543 -9.842  49.172  1.00 16.41 ? 155 PHE B C   1 
ATOM   2671 O  O   . PHE B 1 167 ? -12.587 -10.463 49.744  1.00 16.54 ? 155 PHE B O   1 
ATOM   2672 C  CB  . PHE B 1 167 ? -13.695 -7.303  49.446  1.00 15.54 ? 155 PHE B CB  1 
ATOM   2673 C  CG  . PHE B 1 167 ? -13.412 -5.903  48.930  1.00 15.51 ? 155 PHE B CG  1 
ATOM   2674 C  CD1 . PHE B 1 167 ? -12.342 -5.624  48.086  1.00 16.33 ? 155 PHE B CD1 1 
ATOM   2675 C  CD2 . PHE B 1 167 ? -14.248 -4.869  49.273  1.00 17.17 ? 155 PHE B CD2 1 
ATOM   2676 C  CE1 . PHE B 1 167 ? -12.100 -4.339  47.628  1.00 17.96 ? 155 PHE B CE1 1 
ATOM   2677 C  CE2 . PHE B 1 167 ? -14.019 -3.590  48.786  1.00 17.59 ? 155 PHE B CE2 1 
ATOM   2678 C  CZ  . PHE B 1 167 ? -12.915 -3.312  48.003  1.00 18.53 ? 155 PHE B CZ  1 
ATOM   2679 N  N   . ASP B 1 168 ? -14.809 -10.292 49.116  1.00 17.94 ? 156 ASP B N   1 
ATOM   2680 C  CA  . ASP B 1 168 ? -15.270 -11.613 49.620  1.00 22.04 ? 156 ASP B CA  1 
ATOM   2681 C  C   . ASP B 1 168 ? -14.455 -12.705 48.922  1.00 21.06 ? 156 ASP B C   1 
ATOM   2682 O  O   . ASP B 1 168 ? -13.978 -13.608 49.621  1.00 20.07 ? 156 ASP B O   1 
ATOM   2683 C  CB  . ASP B 1 168 ? -16.774 -11.819 49.421  1.00 24.05 ? 156 ASP B CB  1 
ATOM   2684 C  CG  . ASP B 1 168 ? -17.606 -10.958 50.365  1.00 29.02 ? 156 ASP B CG  1 
ATOM   2685 O  OD1 . ASP B 1 168 ? -17.015 -10.388 51.306  1.00 33.04 ? 156 ASP B OD1 1 
ATOM   2686 O  OD2 . ASP B 1 168 ? -18.831 -10.856 50.143  1.00 34.96 ? 156 ASP B OD2 1 
ATOM   2687 N  N   . ALA B 1 169 ? -14.286 -12.595 47.606  1.00 20.58 ? 157 ALA B N   1 
ATOM   2688 C  CA  . ALA B 1 169 ? -13.617 -13.600 46.758  1.00 21.18 ? 157 ALA B CA  1 
ATOM   2689 C  C   . ALA B 1 169 ? -12.128 -13.639 47.128  1.00 19.89 ? 157 ALA B C   1 
ATOM   2690 O  O   . ALA B 1 169 ? -11.575 -14.752 47.318  1.00 22.56 ? 157 ALA B O   1 
ATOM   2691 C  CB  . ALA B 1 169 ? -13.811 -13.266 45.302  1.00 20.52 ? 157 ALA B CB  1 
ATOM   2692 N  N   . TRP B 1 170 ? -11.519 -12.464 47.329  1.00 15.91 ? 158 TRP B N   1 
ATOM   2693 C  CA  . TRP B 1 170 ? -10.095 -12.356 47.732  1.00 15.12 ? 158 TRP B CA  1 
ATOM   2694 C  C   . TRP B 1 170 ? -9.909  -12.998 49.100  1.00 16.22 ? 158 TRP B C   1 
ATOM   2695 O  O   . TRP B 1 170 ? -8.914  -13.713 49.305  1.00 18.32 ? 158 TRP B O   1 
ATOM   2696 C  CB  . TRP B 1 170 ? -9.628  -10.904 47.768  1.00 16.45 ? 158 TRP B CB  1 
ATOM   2697 C  CG  . TRP B 1 170 ? -9.632  -10.275 46.409  1.00 17.02 ? 158 TRP B CG  1 
ATOM   2698 C  CD1 . TRP B 1 170 ? -9.783  -10.897 45.199  1.00 19.40 ? 158 TRP B CD1 1 
ATOM   2699 C  CD2 . TRP B 1 170 ? -9.571  -8.880  46.134  1.00 15.86 ? 158 TRP B CD2 1 
ATOM   2700 N  NE1 . TRP B 1 170 ? -9.770  -9.974  44.184  1.00 21.02 ? 158 TRP B NE1 1 
ATOM   2701 C  CE2 . TRP B 1 170 ? -9.658  -8.724  44.735  1.00 17.08 ? 158 TRP B CE2 1 
ATOM   2702 C  CE3 . TRP B 1 170 ? -9.476  -7.745  46.936  1.00 16.13 ? 158 TRP B CE3 1 
ATOM   2703 C  CZ2 . TRP B 1 170 ? -9.556  -7.491  44.123  1.00 15.48 ? 158 TRP B CZ2 1 
ATOM   2704 C  CZ3 . TRP B 1 170 ? -9.445  -6.514  46.318  1.00 15.88 ? 158 TRP B CZ3 1 
ATOM   2705 C  CH2 . TRP B 1 170 ? -9.518  -6.390  44.941  1.00 15.38 ? 158 TRP B CH2 1 
ATOM   2706 N  N   . LYS B 1 171 ? -10.790 -12.675 50.027  1.00 16.99 ? 159 LYS B N   1 
ATOM   2707 C  CA  . LYS B 1 171 ? -10.666 -13.152 51.424  1.00 19.70 ? 159 LYS B CA  1 
ATOM   2708 C  C   . LYS B 1 171 ? -10.898 -14.667 51.446  1.00 20.52 ? 159 LYS B C   1 
ATOM   2709 O  O   . LYS B 1 171 ? -10.177 -15.364 52.176  1.00 20.34 ? 159 LYS B O   1 
ATOM   2710 C  CB  . LYS B 1 171 ? -11.685 -12.435 52.309  1.00 21.55 ? 159 LYS B CB  1 
ATOM   2711 C  CG  . LYS B 1 171 ? -11.323 -11.006 52.694  1.00 27.12 ? 159 LYS B CG  1 
ATOM   2712 C  CD  . LYS B 1 171 ? -12.576 -10.300 53.200  1.00 31.39 ? 159 LYS B CD  1 
ATOM   2713 C  CE  . LYS B 1 171 ? -12.389 -9.387  54.376  1.00 36.38 ? 159 LYS B CE  1 
ATOM   2714 N  NZ  . LYS B 1 171 ? -13.720 -9.089  54.966  1.00 36.96 ? 159 LYS B NZ  1 
ATOM   2715 N  N   . ASN B 1 172 ? -11.839 -15.133 50.628  1.00 20.75 ? 160 ASN B N   1 
ATOM   2716 C  CA  . ASN B 1 172 ? -12.211 -16.569 50.565  1.00 26.31 ? 160 ASN B CA  1 
ATOM   2717 C  C   . ASN B 1 172 ? -10.989 -17.329 50.046  1.00 23.69 ? 160 ASN B C   1 
ATOM   2718 O  O   . ASN B 1 172 ? -10.728 -18.440 50.569  1.00 25.29 ? 160 ASN B O   1 
ATOM   2719 C  CB  . ASN B 1 172 ? -13.486 -16.787 49.752  1.00 28.74 ? 160 ASN B CB  1 
ATOM   2720 C  CG  . ASN B 1 172 ? -14.742 -16.352 50.477  1.00 35.60 ? 160 ASN B CG  1 
ATOM   2721 O  OD1 . ASN B 1 172 ? -14.742 -16.196 51.695  1.00 40.21 ? 160 ASN B OD1 1 
ATOM   2722 N  ND2 . ASN B 1 172 ? -15.816 -16.136 49.734  1.00 42.36 ? 160 ASN B ND2 1 
ATOM   2723 N  N   . ALA B 1 173 ? -10.212 -16.715 49.147  1.00 21.31 ? 161 ALA B N   1 
ATOM   2724 C  CA  . ALA B 1 173 ? -8.969  -17.269 48.538  1.00 21.52 ? 161 ALA B CA  1 
ATOM   2725 C  C   . ALA B 1 173 ? -7.748  -17.150 49.477  1.00 21.14 ? 161 ALA B C   1 
ATOM   2726 O  O   . ALA B 1 173 ? -6.616  -17.569 49.078  1.00 23.05 ? 161 ALA B O   1 
ATOM   2727 C  CB  . ALA B 1 173 ? -8.698  -16.575 47.225  1.00 23.26 ? 161 ALA B CB  1 
ATOM   2728 N  N   . GLY B 1 174 ? -7.901  -16.585 50.666  1.00 19.48 ? 162 GLY B N   1 
ATOM   2729 C  CA  . GLY B 1 174 ? -6.814  -16.488 51.652  1.00 20.28 ? 162 GLY B CA  1 
ATOM   2730 C  C   . GLY B 1 174 ? -6.056  -15.164 51.626  1.00 23.52 ? 162 GLY B C   1 
ATOM   2731 O  O   . GLY B 1 174 ? -5.038  -15.053 52.340  1.00 25.11 ? 162 GLY B O   1 
ATOM   2732 N  N   . LEU B 1 175 ? -6.507  -14.167 50.861  1.00 20.00 ? 163 LEU B N   1 
ATOM   2733 C  CA  . LEU B 1 175 ? -5.827  -12.860 50.777  1.00 20.08 ? 163 LEU B CA  1 
ATOM   2734 C  C   . LEU B 1 175 ? -6.321  -11.972 51.921  1.00 24.20 ? 163 LEU B C   1 
ATOM   2735 O  O   . LEU B 1 175 ? -7.523  -11.645 51.899  1.00 31.14 ? 163 LEU B O   1 
ATOM   2736 C  CB  . LEU B 1 175 ? -6.142  -12.260 49.409  1.00 20.93 ? 163 LEU B CB  1 
ATOM   2737 C  CG  . LEU B 1 175 ? -5.760  -13.138 48.222  1.00 23.09 ? 163 LEU B CG  1 
ATOM   2738 C  CD1 . LEU B 1 175 ? -6.002  -12.431 46.897  1.00 26.53 ? 163 LEU B CD1 1 
ATOM   2739 C  CD2 . LEU B 1 175 ? -4.320  -13.594 48.355  1.00 26.48 ? 163 LEU B CD2 1 
ATOM   2740 N  N   . GLU B 1 176 ? -5.441  -11.584 52.857  1.00 22.25 ? 164 GLU B N   1 
ATOM   2741 C  CA  . GLU B 1 176 ? -5.831  -10.777 54.047  1.00 22.57 ? 164 GLU B CA  1 
ATOM   2742 C  C   . GLU B 1 176 ? -6.015  -9.309  53.631  1.00 20.42 ? 164 GLU B C   1 
ATOM   2743 O  O   . GLU B 1 176 ? -5.183  -8.808  52.889  1.00 18.23 ? 164 GLU B O   1 
ATOM   2744 C  CB  . GLU B 1 176 ? -4.738  -10.789 55.122  1.00 30.24 ? 164 GLU B CB  1 
ATOM   2745 C  CG  . GLU B 1 176 ? -4.812  -11.924 56.132  1.00 39.66 ? 164 GLU B CG  1 
ATOM   2746 C  CD  . GLU B 1 176 ? -4.370  -11.482 57.527  1.00 42.30 ? 164 GLU B CD  1 
ATOM   2747 O  OE1 . GLU B 1 176 ? -5.002  -10.561 58.090  1.00 45.67 ? 164 GLU B OE1 1 
ATOM   2748 O  OE2 . GLU B 1 176 ? -3.392  -12.039 58.049  1.00 55.95 ? 164 GLU B OE2 1 
ATOM   2749 N  N   . MET B 1 177 ? -7.054  -8.648  54.116  1.00 18.50 ? 165 MET B N   1 
ATOM   2750 C  CA  . MET B 1 177 ? -7.285  -7.206  53.864  1.00 20.07 ? 165 MET B CA  1 
ATOM   2751 C  C   . MET B 1 177 ? -7.299  -6.501  55.218  1.00 17.59 ? 165 MET B C   1 
ATOM   2752 O  O   . MET B 1 177 ? -7.777  -7.092  56.201  1.00 17.03 ? 165 MET B O   1 
ATOM   2753 C  CB  . MET B 1 177 ? -8.632  -6.952  53.188  1.00 23.08 ? 165 MET B CB  1 
ATOM   2754 C  CG  . MET B 1 177 ? -8.812  -7.677  51.877  1.00 30.95 ? 165 MET B CG  1 
ATOM   2755 S  SD  . MET B 1 177 ? -8.319  -6.615  50.506  1.00 37.91 ? 165 MET B SD  1 
ATOM   2756 C  CE  . MET B 1 177 ? -9.702  -5.488  50.395  1.00 31.80 ? 165 MET B CE  1 
ATOM   2757 N  N   . GLY B 1 178 ? -6.869  -5.255  55.243  1.00 15.31 ? 166 GLY B N   1 
ATOM   2758 C  CA  . GLY B 1 178 ? -6.866  -4.444  56.461  1.00 14.18 ? 166 GLY B CA  1 
ATOM   2759 C  C   . GLY B 1 178 ? -8.061  -3.513  56.497  1.00 14.82 ? 166 GLY B C   1 
ATOM   2760 O  O   . GLY B 1 178 ? -9.152  -3.855  55.914  1.00 17.85 ? 166 GLY B O   1 
ATOM   2761 N  N   . THR B 1 179 ? -7.920  -2.423  57.245  1.00 15.36 ? 167 THR B N   1 
ATOM   2762 C  CA  . THR B 1 179 ? -8.898  -1.325  57.355  1.00 16.23 ? 167 THR B CA  1 
ATOM   2763 C  C   . THR B 1 179 ? -8.906  -0.544  56.036  1.00 14.17 ? 167 THR B C   1 
ATOM   2764 O  O   . THR B 1 179 ? -7.852  -0.110  55.561  1.00 13.38 ? 167 THR B O   1 
ATOM   2765 C  CB  . THR B 1 179 ? -8.571  -0.449  58.572  1.00 19.60 ? 167 THR B CB  1 
ATOM   2766 O  OG1 . THR B 1 179 ? -8.634  -1.328  59.704  1.00 24.20 ? 167 THR B OG1 1 
ATOM   2767 C  CG2 . THR B 1 179 ? -9.572  0.671   58.714  1.00 20.80 ? 167 THR B CG2 1 
ATOM   2768 N  N   . HIS B 1 180 ? -10.075 -0.351  55.443  1.00 15.05 ? 168 HIS B N   1 
ATOM   2769 C  CA  . HIS B 1 180 ? -10.171 0.394   54.163  1.00 14.85 ? 168 HIS B CA  1 
ATOM   2770 C  C   . HIS B 1 180 ? -9.716  1.851   54.313  1.00 14.37 ? 168 HIS B C   1 
ATOM   2771 O  O   . HIS B 1 180 ? -10.200 2.561   55.189  1.00 15.47 ? 168 HIS B O   1 
ATOM   2772 C  CB  . HIS B 1 180 ? -11.590 0.302   53.560  1.00 17.13 ? 168 HIS B CB  1 
ATOM   2773 C  CG  . HIS B 1 180 ? -11.791 -0.981  52.818  1.00 20.94 ? 168 HIS B CG  1 
ATOM   2774 N  ND1 . HIS B 1 180 ? -12.064 -2.176  53.449  1.00 28.31 ? 168 HIS B ND1 1 
ATOM   2775 C  CD2 . HIS B 1 180 ? -11.553 -1.287  51.524  1.00 23.79 ? 168 HIS B CD2 1 
ATOM   2776 C  CE1 . HIS B 1 180 ? -12.081 -3.149  52.554  1.00 25.69 ? 168 HIS B CE1 1 
ATOM   2777 N  NE2 . HIS B 1 180 ? -11.750 -2.631  51.366  1.00 28.31 ? 168 HIS B NE2 1 
ATOM   2778 N  N   . ASN B 1 181 ? -8.837  2.271   53.411  1.00 12.77 ? 169 ASN B N   1 
ATOM   2779 C  CA  . ASN B 1 181 ? -8.541  3.683   53.135  1.00 13.22 ? 169 ASN B CA  1 
ATOM   2780 C  C   . ASN B 1 181 ? -9.325  4.020   51.871  1.00 12.27 ? 169 ASN B C   1 
ATOM   2781 O  O   . ASN B 1 181 ? -10.484 3.550   51.722  1.00 12.03 ? 169 ASN B O   1 
ATOM   2782 C  CB  . ASN B 1 181 ? -7.020  3.907   53.091  1.00 14.05 ? 169 ASN B CB  1 
ATOM   2783 C  CG  . ASN B 1 181 ? -6.652  5.362   53.308  1.00 16.90 ? 169 ASN B CG  1 
ATOM   2784 O  OD1 . ASN B 1 181 ? -6.574  6.136   52.359  1.00 17.37 ? 169 ASN B OD1 1 
ATOM   2785 N  ND2 . ASN B 1 181 ? -6.448  5.773   54.561  1.00 20.02 ? 169 ASN B ND2 1 
ATOM   2786 N  N   . TYR B 1 182 ? -8.755  4.803   50.991  1.00 12.66 ? 170 TYR B N   1 
ATOM   2787 C  CA  . TYR B 1 182 ? -9.575  5.360   49.891  1.00 11.34 ? 170 TYR B CA  1 
ATOM   2788 C  C   . TYR B 1 182 ? -9.883  4.265   48.875  1.00 12.11 ? 170 TYR B C   1 
ATOM   2789 O  O   . TYR B 1 182 ? -9.187  3.225   48.780  1.00 11.83 ? 170 TYR B O   1 
ATOM   2790 C  CB  . TYR B 1 182 ? -8.906  6.566   49.265  1.00 11.28 ? 170 TYR B CB  1 
ATOM   2791 C  CG  . TYR B 1 182 ? -7.630  6.397   48.489  1.00 11.29 ? 170 TYR B CG  1 
ATOM   2792 C  CD1 . TYR B 1 182 ? -7.645  5.865   47.219  1.00 12.57 ? 170 TYR B CD1 1 
ATOM   2793 C  CD2 . TYR B 1 182 ? -6.415  6.822   48.982  1.00 13.05 ? 170 TYR B CD2 1 
ATOM   2794 C  CE1 . TYR B 1 182 ? -6.494  5.777   46.457  1.00 12.51 ? 170 TYR B CE1 1 
ATOM   2795 C  CE2 . TYR B 1 182 ? -5.251  6.742   48.226  1.00 12.66 ? 170 TYR B CE2 1 
ATOM   2796 C  CZ  . TYR B 1 182 ? -5.294  6.221   46.942  1.00 14.00 ? 170 TYR B CZ  1 
ATOM   2797 O  OH  . TYR B 1 182 ? -4.184  6.093   46.126  1.00 15.68 ? 170 TYR B OH  1 
ATOM   2798 N  N   . MET B 1 183 ? -10.923 4.521   48.071  1.00 11.38 ? 171 MET B N   1 
ATOM   2799 C  CA  . MET B 1 183 ? -11.281 3.683   46.902  1.00 12.60 ? 171 MET B CA  1 
ATOM   2800 C  C   . MET B 1 183 ? -11.696 4.657   45.787  1.00 11.92 ? 171 MET B C   1 
ATOM   2801 O  O   . MET B 1 183 ? -12.547 5.474   46.041  1.00 12.36 ? 171 MET B O   1 
ATOM   2802 C  CB  . MET B 1 183 ? -12.417 2.723   47.214  1.00 13.40 ? 171 MET B CB  1 
ATOM   2803 C  CG  . MET B 1 183 ? -12.741 1.788   46.087  1.00 15.31 ? 171 MET B CG  1 
ATOM   2804 S  SD  . MET B 1 183 ? -13.933 0.526   46.661  1.00 18.32 ? 171 MET B SD  1 
ATOM   2805 C  CE  . MET B 1 183 ? -15.444 1.448   46.779  1.00 17.94 ? 171 MET B CE  1 
ATOM   2806 N  N   . ILE B 1 184 ? -11.114 4.554   44.591  1.00 10.99 ? 172 ILE B N   1 
ATOM   2807 C  CA  . ILE B 1 184 ? -11.384 5.495   43.477  1.00 11.44 ? 172 ILE B CA  1 
ATOM   2808 C  C   . ILE B 1 184 ? -11.660 4.683   42.212  1.00 11.61 ? 172 ILE B C   1 
ATOM   2809 O  O   . ILE B 1 184 ? -11.233 3.523   42.134  1.00 10.42 ? 172 ILE B O   1 
ATOM   2810 C  CB  . ILE B 1 184 ? -10.272 6.532   43.207  1.00 11.91 ? 172 ILE B CB  1 
ATOM   2811 C  CG1 . ILE B 1 184 ? -8.932  5.868   42.872  1.00 11.59 ? 172 ILE B CG1 1 
ATOM   2812 C  CG2 . ILE B 1 184 ? -10.150 7.518   44.355  1.00 11.72 ? 172 ILE B CG2 1 
ATOM   2813 C  CD1 . ILE B 1 184 ? -7.844  6.851   42.510  1.00 12.32 ? 172 ILE B CD1 1 
ATOM   2814 N  N   . VAL B 1 185 ? -12.353 5.294   41.257  1.00 10.81 ? 173 VAL B N   1 
ATOM   2815 C  CA  . VAL B 1 185 ? -12.400 4.786   39.876  1.00 11.30 ? 173 VAL B CA  1 
ATOM   2816 C  C   . VAL B 1 185 ? -11.239 5.455   39.146  1.00 12.02 ? 173 VAL B C   1 
ATOM   2817 O  O   . VAL B 1 185 ? -11.286 6.677   38.930  1.00 11.28 ? 173 VAL B O   1 
ATOM   2818 C  CB  . VAL B 1 185 ? -13.757 5.013   39.193  1.00 11.85 ? 173 VAL B CB  1 
ATOM   2819 C  CG1 . VAL B 1 185 ? -13.676 4.476   37.788  1.00 13.73 ? 173 VAL B CG1 1 
ATOM   2820 C  CG2 . VAL B 1 185 ? -14.898 4.415   39.997  1.00 12.85 ? 173 VAL B CG2 1 
ATOM   2821 N  N   . ALA B 1 186 ? -10.220 4.669   38.826  1.00 10.93 ? 174 ALA B N   1 
ATOM   2822 C  CA  . ALA B 1 186 ? -8.897  5.151   38.400  1.00 11.60 ? 174 ALA B CA  1 
ATOM   2823 C  C   . ALA B 1 186 ? -8.598  4.833   36.937  1.00 12.43 ? 174 ALA B C   1 
ATOM   2824 O  O   . ALA B 1 186 ? -8.852  3.716   36.480  1.00 14.16 ? 174 ALA B O   1 
ATOM   2825 C  CB  . ALA B 1 186 ? -7.846  4.542   39.272  1.00 13.36 ? 174 ALA B CB  1 
ATOM   2826 N  N   . THR B 1 187 ? -8.071  5.834   36.239  1.00 11.99 ? 175 THR B N   1 
ATOM   2827 C  CA  . THR B 1 187 ? -7.354  5.684   34.971  1.00 11.59 ? 175 THR B CA  1 
ATOM   2828 C  C   . THR B 1 187 ? -5.860  5.607   35.287  1.00 11.71 ? 175 THR B C   1 
ATOM   2829 O  O   . THR B 1 187 ? -5.332  6.508   36.002  1.00 11.38 ? 175 THR B O   1 
ATOM   2830 C  CB  . THR B 1 187 ? -7.686  6.847   34.044  1.00 12.44 ? 175 THR B CB  1 
ATOM   2831 O  OG1 . THR B 1 187 ? -9.114  6.895   33.873  1.00 13.64 ? 175 THR B OG1 1 
ATOM   2832 C  CG2 . THR B 1 187 ? -6.989  6.704   32.697  1.00 12.98 ? 175 THR B CG2 1 
ATOM   2833 N  N   . ALA B 1 188 ? -5.167  4.596   34.739  1.00 11.18 ? 176 ALA B N   1 
ATOM   2834 C  CA  . ALA B 1 188 ? -3.733  4.437   34.998  1.00 12.90 ? 176 ALA B CA  1 
ATOM   2835 C  C   . ALA B 1 188 ? -3.039  4.288   33.651  1.00 13.62 ? 176 ALA B C   1 
ATOM   2836 O  O   . ALA B 1 188 ? -3.668  3.785   32.728  1.00 12.76 ? 176 ALA B O   1 
ATOM   2837 C  CB  . ALA B 1 188 ? -3.496  3.244   35.867  1.00 13.89 ? 176 ALA B CB  1 
ATOM   2838 N  N   . GLY B 1 189 ? -1.795  4.719   33.555  1.00 13.05 ? 177 GLY B N   1 
ATOM   2839 C  CA  . GLY B 1 189 ? -1.055  4.528   32.296  1.00 13.40 ? 177 GLY B CA  1 
ATOM   2840 C  C   . GLY B 1 189 ? 0.425   4.511   32.523  1.00 14.79 ? 177 GLY B C   1 
ATOM   2841 O  O   . GLY B 1 189 ? 0.890   4.949   33.603  1.00 14.84 ? 177 GLY B O   1 
ATOM   2842 N  N   . TYR B 1 190 ? 1.165   3.968   31.569  1.00 14.95 ? 178 TYR B N   1 
ATOM   2843 C  CA  . TYR B 1 190 ? 2.639   3.884   31.650  1.00 15.94 ? 178 TYR B CA  1 
ATOM   2844 C  C   . TYR B 1 190 ? 3.160   3.905   30.223  1.00 15.24 ? 178 TYR B C   1 
ATOM   2845 O  O   . TYR B 1 190 ? 2.773   3.002   29.435  1.00 14.69 ? 178 TYR B O   1 
ATOM   2846 C  CB  . TYR B 1 190 ? 3.117   2.603   32.337  1.00 19.94 ? 178 TYR B CB  1 
ATOM   2847 C  CG  . TYR B 1 190 ? 4.628   2.513   32.469  1.00 23.49 ? 178 TYR B CG  1 
ATOM   2848 C  CD1 . TYR B 1 190 ? 5.329   3.363   33.307  1.00 26.52 ? 178 TYR B CD1 1 
ATOM   2849 C  CD2 . TYR B 1 190 ? 5.377   1.657   31.675  1.00 25.66 ? 178 TYR B CD2 1 
ATOM   2850 C  CE1 . TYR B 1 190 ? 6.713   3.301   33.419  1.00 28.70 ? 178 TYR B CE1 1 
ATOM   2851 C  CE2 . TYR B 1 190 ? 6.750   1.590   31.764  1.00 29.49 ? 178 TYR B CE2 1 
ATOM   2852 C  CZ  . TYR B 1 190 ? 7.432   2.396   32.662  1.00 31.75 ? 178 TYR B CZ  1 
ATOM   2853 O  OH  . TYR B 1 190 ? 8.801   2.306   32.753  1.00 31.97 ? 178 TYR B OH  1 
ATOM   2854 N  N   . GLN B 1 191 ? 4.044   4.828   29.918  1.00 16.84 ? 179 GLN B N   1 
ATOM   2855 C  CA  . GLN B 1 191 ? 4.751   4.881   28.603  1.00 17.41 ? 179 GLN B CA  1 
ATOM   2856 C  C   . GLN B 1 191 ? 3.716   4.854   27.485  1.00 16.88 ? 179 GLN B C   1 
ATOM   2857 O  O   . GLN B 1 191 ? 3.837   4.083   26.579  1.00 16.03 ? 179 GLN B O   1 
ATOM   2858 C  CB  . GLN B 1 191 ? 5.797   3.767   28.576  1.00 19.83 ? 179 GLN B CB  1 
ATOM   2859 C  CG  . GLN B 1 191 ? 6.894   4.076   29.595  1.00 24.39 ? 179 GLN B CG  1 
ATOM   2860 C  CD  . GLN B 1 191 ? 8.255   3.549   29.214  1.00 27.89 ? 179 GLN B CD  1 
ATOM   2861 O  OE1 . GLN B 1 191 ? 8.367   2.541   28.525  1.00 34.60 ? 179 GLN B OE1 1 
ATOM   2862 N  NE2 . GLN B 1 191 ? 9.294   4.229   29.679  1.00 29.43 ? 179 GLN B NE2 1 
ATOM   2863 N  N   . SER B 1 192 ? 2.696   5.684   27.591  1.00 15.98 ? 180 SER B N   1 
ATOM   2864 C  CA  . SER B 1 192 ? 1.578   5.732   26.627  1.00 15.02 ? 180 SER B CA  1 
ATOM   2865 C  C   . SER B 1 192 ? 1.050   7.155   26.497  1.00 14.54 ? 180 SER B C   1 
ATOM   2866 O  O   . SER B 1 192 ? 1.564   8.106   27.158  1.00 14.44 ? 180 SER B O   1 
ATOM   2867 C  CB  . SER B 1 192 ? 0.520   4.770   27.042  1.00 16.15 ? 180 SER B CB  1 
ATOM   2868 O  OG  . SER B 1 192 ? -0.099  5.208   28.239  1.00 13.81 ? 180 SER B OG  1 
ATOM   2869 N  N   . SER B 1 193 ? 0.041   7.316   25.647  1.00 13.89 ? 181 SER B N   1 
ATOM   2870 C  CA  . SER B 1 193 ? -0.660  8.603   25.473  1.00 14.83 ? 181 SER B CA  1 
ATOM   2871 C  C   . SER B 1 193 ? -2.148  8.267   25.588  1.00 14.38 ? 181 SER B C   1 
ATOM   2872 O  O   . SER B 1 193 ? -2.535  7.073   25.469  1.00 13.92 ? 181 SER B O   1 
ATOM   2873 C  CB  . SER B 1 193 ? -0.366  9.313   24.161  1.00 16.79 ? 181 SER B CB  1 
ATOM   2874 O  OG  . SER B 1 193 ? 1.020   9.650   24.051  1.00 17.71 ? 181 SER B OG  1 
ATOM   2875 N  N   . GLY B 1 194 ? -2.964  9.276   25.767  1.00 13.66 ? 182 GLY B N   1 
ATOM   2876 C  CA  . GLY B 1 194 ? -4.400  9.004   25.830  1.00 13.83 ? 182 GLY B CA  1 
ATOM   2877 C  C   . GLY B 1 194 ? -5.174  10.106  26.483  1.00 13.46 ? 182 GLY B C   1 
ATOM   2878 O  O   . GLY B 1 194 ? -4.647  11.258  26.782  1.00 15.36 ? 182 GLY B O   1 
ATOM   2879 N  N   . SER B 1 195 ? -6.468  9.858   26.520  1.00 12.91 ? 183 SER B N   1 
ATOM   2880 C  CA  . SER B 1 195 ? -7.362  10.746  27.276  1.00 13.90 ? 183 SER B CA  1 
ATOM   2881 C  C   . SER B 1 195 ? -8.463  9.898   27.882  1.00 12.61 ? 183 SER B C   1 
ATOM   2882 O  O   . SER B 1 195 ? -8.766  8.857   27.355  1.00 13.58 ? 183 SER B O   1 
ATOM   2883 C  CB  . SER B 1 195 ? -7.909  11.843  26.423  1.00 15.45 ? 183 SER B CB  1 
ATOM   2884 O  OG  . SER B 1 195 ? -8.789  11.322  25.477  1.00 17.04 ? 183 SER B OG  1 
ATOM   2885 N  N   . ALA B 1 196 ? -9.028  10.370  28.964  1.00 12.29 ? 184 ALA B N   1 
ATOM   2886 C  CA  . ALA B 1 196 ? -10.197 9.741   29.583  1.00 11.17 ? 184 ALA B CA  1 
ATOM   2887 C  C   . ALA B 1 196 ? -11.048 10.833  30.229  1.00 13.15 ? 184 ALA B C   1 
ATOM   2888 O  O   . ALA B 1 196 ? -10.504 11.824  30.668  1.00 14.16 ? 184 ALA B O   1 
ATOM   2889 C  CB  . ALA B 1 196 ? -9.781  8.709   30.602  1.00 12.12 ? 184 ALA B CB  1 
ATOM   2890 N  N   . SER B 1 197 ? -12.347 10.585  30.303  1.00 12.73 ? 185 SER B N   1 
ATOM   2891 C  CA  . SER B 1 197 ? -13.306 11.464  30.990  1.00 14.42 ? 185 SER B CA  1 
ATOM   2892 C  C   . SER B 1 197 ? -14.306 10.539  31.680  1.00 13.73 ? 185 SER B C   1 
ATOM   2893 O  O   . SER B 1 197 ? -15.070 9.850   30.987  1.00 13.65 ? 185 SER B O   1 
ATOM   2894 C  CB  . SER B 1 197 ? -13.925 12.446  30.017  1.00 17.23 ? 185 SER B CB  1 
ATOM   2895 O  OG  . SER B 1 197 ? -15.078 13.057  30.585  1.00 21.07 ? 185 SER B OG  1 
ATOM   2896 N  N   . ILE B 1 198 ? -14.224 10.443  32.992  1.00 13.79 ? 186 ILE B N   1 
ATOM   2897 C  CA  . ILE B 1 198 ? -14.940 9.435   33.785  1.00 13.14 ? 186 ILE B CA  1 
ATOM   2898 C  C   . ILE B 1 198 ? -15.803 10.174  34.794  1.00 14.17 ? 186 ILE B C   1 
ATOM   2899 O  O   . ILE B 1 198 ? -15.303 11.107  35.437  1.00 13.97 ? 186 ILE B O   1 
ATOM   2900 C  CB  . ILE B 1 198 ? -13.901 8.488   34.436  1.00 14.30 ? 186 ILE B CB  1 
ATOM   2901 C  CG1 . ILE B 1 198 ? -13.090 7.757   33.356  1.00 14.99 ? 186 ILE B CG1 1 
ATOM   2902 C  CG2 . ILE B 1 198 ? -14.536 7.550   35.442  1.00 15.22 ? 186 ILE B CG2 1 
ATOM   2903 C  CD1 . ILE B 1 198 ? -13.874 6.707   32.571  1.00 16.85 ? 186 ILE B CD1 1 
ATOM   2904 N  N   . THR B 1 199 ? -17.049 9.752   34.934  1.00 13.53 ? 187 THR B N   1 
ATOM   2905 C  CA  . THR B 1 199 ? -17.943 10.329  35.978  1.00 15.24 ? 187 THR B CA  1 
ATOM   2906 C  C   . THR B 1 199 ? -18.334 9.216   36.933  1.00 16.04 ? 187 THR B C   1 
ATOM   2907 O  O   . THR B 1 199 ? -18.951 8.310   36.504  1.00 15.92 ? 187 THR B O   1 
ATOM   2908 C  CB  . THR B 1 199 ? -19.183 11.001  35.364  1.00 17.17 ? 187 THR B CB  1 
ATOM   2909 O  OG1 . THR B 1 199 ? -18.727 12.032  34.508  1.00 21.24 ? 187 THR B OG1 1 
ATOM   2910 C  CG2 . THR B 1 199 ? -20.088 11.618  36.412  1.00 18.06 ? 187 THR B CG2 1 
ATOM   2911 N  N   . VAL B 1 200 ? -17.930 9.302   38.198  1.00 14.75 ? 188 VAL B N   1 
ATOM   2912 C  CA  . VAL B 1 200 ? -18.334 8.373   39.267  1.00 17.17 ? 188 VAL B CA  1 
ATOM   2913 C  C   . VAL B 1 200 ? -19.695 8.854   39.764  1.00 19.35 ? 188 VAL B C   1 
ATOM   2914 O  O   . VAL B 1 200 ? -19.826 10.086  39.886  1.00 18.05 ? 188 VAL B O   1 
ATOM   2915 C  CB  . VAL B 1 200 ? -17.274 8.363   40.376  1.00 17.92 ? 188 VAL B CB  1 
ATOM   2916 C  CG1 . VAL B 1 200 ? -17.648 7.368   41.450  1.00 20.72 ? 188 VAL B CG1 1 
ATOM   2917 C  CG2 . VAL B 1 200 ? -15.909 8.074   39.778  1.00 18.15 ? 188 VAL B CG2 1 
ATOM   2918 N  N   . GLN B 1 201 ? -20.649 7.940   39.931  1.00 23.72 ? 189 GLN B N   1 
ATOM   2919 C  CA  . GLN B 1 201 ? -22.030 8.237   40.431  1.00 29.73 ? 189 GLN B CA  1 
ATOM   2920 C  C   . GLN B 1 201 ? -22.350 7.364   41.643  1.00 33.63 ? 189 GLN B C   1 
ATOM   2921 O  O   . GLN B 1 201 ? -21.531 7.323   42.583  1.00 45.45 ? 189 GLN B O   1 
ATOM   2922 C  CB  . GLN B 1 201 ? -23.049 7.992   39.323  1.00 34.83 ? 189 GLN B CB  1 
ATOM   2923 C  CG  . GLN B 1 201 ? -22.954 9.012   38.198  1.00 42.12 ? 189 GLN B CG  1 
ATOM   2924 C  CD  . GLN B 1 201 ? -22.847 8.327   36.861  1.00 46.07 ? 189 GLN B CD  1 
ATOM   2925 O  OE1 . GLN B 1 201 ? -23.749 7.601   36.446  1.00 60.91 ? 189 GLN B OE1 1 
ATOM   2926 N  NE2 . GLN B 1 201 ? -21.722 8.528   36.193  1.00 45.69 ? 189 GLN B NE2 1 
ATOM   2927 N  N   . GLU C 1 13  ? -1.083  10.285  15.530  1.00 34.22 ? 1   GLU C N   1 
ATOM   2928 C  CA  . GLU C 1 13  ? -0.729  9.677   14.230  1.00 35.74 ? 1   GLU C CA  1 
ATOM   2929 C  C   . GLU C 1 13  ? 0.275   10.565  13.488  1.00 34.02 ? 1   GLU C C   1 
ATOM   2930 O  O   . GLU C 1 13  ? 1.206   9.982   12.992  1.00 26.98 ? 1   GLU C O   1 
ATOM   2931 C  CB  . GLU C 1 13  ? -1.957  9.331   13.385  1.00 41.29 ? 1   GLU C CB  1 
ATOM   2932 C  CG  . GLU C 1 13  ? -1.636  8.495   12.154  1.00 40.23 ? 1   GLU C CG  1 
ATOM   2933 C  CD  . GLU C 1 13  ? -2.023  7.011   12.197  1.00 43.12 ? 1   GLU C CD  1 
ATOM   2934 O  OE1 . GLU C 1 13  ? -2.975  6.629   11.472  1.00 46.38 ? 1   GLU C OE1 1 
ATOM   2935 O  OE2 . GLU C 1 13  ? -1.366  6.220   12.921  1.00 38.52 ? 1   GLU C OE2 1 
ATOM   2936 N  N   . ILE C 1 14  ? 0.166   11.900  13.432  1.00 27.76 ? 2   ILE C N   1 
ATOM   2937 C  CA  . ILE C 1 14  ? 1.272   12.695  12.819  1.00 30.62 ? 2   ILE C CA  1 
ATOM   2938 C  C   . ILE C 1 14  ? 1.650   13.901  13.703  1.00 26.48 ? 2   ILE C C   1 
ATOM   2939 O  O   . ILE C 1 14  ? 0.770   14.534  14.304  1.00 21.89 ? 2   ILE C O   1 
ATOM   2940 C  CB  . ILE C 1 14  ? 0.990   13.047  11.340  1.00 34.45 ? 2   ILE C CB  1 
ATOM   2941 C  CG1 . ILE C 1 14  ? 0.356   14.414  11.135  1.00 32.84 ? 2   ILE C CG1 1 
ATOM   2942 C  CG2 . ILE C 1 14  ? 0.186   11.974  10.614  1.00 35.17 ? 2   ILE C CG2 1 
ATOM   2943 C  CD1 . ILE C 1 14  ? 0.729   15.015  9.829   1.00 33.41 ? 2   ILE C CD1 1 
ATOM   2944 N  N   . THR C 1 15  ? 2.954   14.135  13.847  1.00 26.00 ? 3   THR C N   1 
ATOM   2945 C  CA  . THR C 1 15  ? 3.530   15.091  14.827  1.00 26.03 ? 3   THR C CA  1 
ATOM   2946 C  C   . THR C 1 15  ? 4.510   16.042  14.141  1.00 24.38 ? 3   THR C C   1 
ATOM   2947 O  O   . THR C 1 15  ? 5.004   16.929  14.823  1.00 23.79 ? 3   THR C O   1 
ATOM   2948 C  CB  . THR C 1 15  ? 4.192   14.360  16.003  1.00 33.23 ? 3   THR C CB  1 
ATOM   2949 O  OG1 . THR C 1 15  ? 5.179   13.476  15.469  1.00 30.74 ? 3   THR C OG1 1 
ATOM   2950 C  CG2 . THR C 1 15  ? 3.206   13.581  16.845  1.00 31.97 ? 3   THR C CG2 1 
ATOM   2951 N  N   . SER C 1 16  ? 4.798   15.847  12.852  1.00 21.17 ? 4   SER C N   1 
ATOM   2952 C  CA  . SER C 1 16  ? 5.670   16.726  12.054  1.00 22.87 ? 4   SER C CA  1 
ATOM   2953 C  C   . SER C 1 16  ? 4.909   17.147  10.807  1.00 18.09 ? 4   SER C C   1 
ATOM   2954 O  O   . SER C 1 16  ? 3.953   16.396  10.434  1.00 17.92 ? 4   SER C O   1 
ATOM   2955 C  CB  . SER C 1 16  ? 6.974   16.056  11.763  1.00 23.82 ? 4   SER C CB  1 
ATOM   2956 O  OG  . SER C 1 16  ? 7.824   16.215  12.888  1.00 28.43 ? 4   SER C OG  1 
ATOM   2957 N  N   . SER C 1 17  ? 5.259   18.316  10.240  1.00 18.06 ? 5   SER C N   1 
ATOM   2958 C  CA  . SER C 1 17  ? 4.515   18.960  9.115   1.00 18.04 ? 5   SER C CA  1 
ATOM   2959 C  C   . SER C 1 17  ? 4.370   17.991  7.940   1.00 19.28 ? 5   SER C C   1 
ATOM   2960 O  O   . SER C 1 17  ? 5.383   17.343  7.538   1.00 16.72 ? 5   SER C O   1 
ATOM   2961 C  CB  . SER C 1 17  ? 5.180   20.248  8.678   1.00 20.70 ? 5   SER C CB  1 
ATOM   2962 O  OG  . SER C 1 17  ? 5.274   21.177  9.744   1.00 18.34 ? 5   SER C OG  1 
ATOM   2963 N  N   . GLU C 1 18  ? 3.170   17.900  7.361   1.00 17.38 ? 6   GLU C N   1 
ATOM   2964 C  CA  . GLU C 1 18  ? 2.881   16.982  6.234   1.00 18.60 ? 6   GLU C CA  1 
ATOM   2965 C  C   . GLU C 1 18  ? 1.697   17.568  5.473   1.00 17.78 ? 6   GLU C C   1 
ATOM   2966 O  O   . GLU C 1 18  ? 0.773   18.165  6.105   1.00 18.68 ? 6   GLU C O   1 
ATOM   2967 C  CB  . GLU C 1 18  ? 2.619   15.586  6.806   1.00 20.09 ? 6   GLU C CB  1 
ATOM   2968 C  CG  . GLU C 1 18  ? 2.140   14.533  5.821   1.00 26.31 ? 6   GLU C CG  1 
ATOM   2969 C  CD  . GLU C 1 18  ? 1.984   13.183  6.492   1.00 27.94 ? 6   GLU C CD  1 
ATOM   2970 O  OE1 . GLU C 1 18  ? 0.841   12.669  6.529   1.00 26.83 ? 6   GLU C OE1 1 
ATOM   2971 O  OE2 . GLU C 1 18  ? 2.990   12.712  7.070   1.00 28.89 ? 6   GLU C OE2 1 
ATOM   2972 N  N   . THR C 1 19  ? 1.666   17.346  4.178   1.00 16.19 ? 7   THR C N   1 
ATOM   2973 C  CA  . THR C 1 19  ? 0.437   17.601  3.388   1.00 15.08 ? 7   THR C CA  1 
ATOM   2974 C  C   . THR C 1 19  ? 0.165   16.354  2.571   1.00 15.59 ? 7   THR C C   1 
ATOM   2975 O  O   . THR C 1 19  ? 1.101   15.564  2.319   1.00 13.65 ? 7   THR C O   1 
ATOM   2976 C  CB  . THR C 1 19  ? 0.557   18.815  2.459   1.00 18.42 ? 7   THR C CB  1 
ATOM   2977 O  OG1 . THR C 1 19  ? 1.463   18.521  1.372   1.00 19.23 ? 7   THR C OG1 1 
ATOM   2978 C  CG2 . THR C 1 19  ? 0.982   20.080  3.183   1.00 20.49 ? 7   THR C CG2 1 
ATOM   2979 N  N   . GLY C 1 20  ? -1.080  16.166  2.193   1.00 13.45 ? 8   GLY C N   1 
ATOM   2980 C  CA  . GLY C 1 20  ? -1.437  15.026  1.338   1.00 14.17 ? 8   GLY C CA  1 
ATOM   2981 C  C   . GLY C 1 20  ? -2.921  15.017  1.063   1.00 13.79 ? 8   GLY C C   1 
ATOM   2982 O  O   . GLY C 1 20  ? -3.564  16.110  1.104   1.00 13.71 ? 8   GLY C O   1 
ATOM   2983 N  N   . THR C 1 21  ? -3.407  13.894  0.551   1.00 13.13 ? 9   THR C N   1 
ATOM   2984 C  CA  . THR C 1 21  ? -4.870  13.695  0.387   1.00 13.66 ? 9   THR C CA  1 
ATOM   2985 C  C   . THR C 1 21  ? -5.269  12.567  1.320   1.00 13.44 ? 9   THR C C   1 
ATOM   2986 O  O   . THR C 1 21  ? -4.511  11.614  1.508   1.00 12.50 ? 9   THR C O   1 
ATOM   2987 C  CB  . THR C 1 21  ? -5.368  13.667  -1.060  1.00 20.05 ? 9   THR C CB  1 
ATOM   2988 O  OG1 . THR C 1 21  ? -6.341  12.667  -1.391  1.00 23.80 ? 9   THR C OG1 1 
ATOM   2989 C  CG2 . THR C 1 21  ? -4.248  13.903  -2.042  1.00 14.65 ? 9   THR C CG2 1 
ATOM   2990 N  N   . ASN C 1 22  ? -6.415  12.765  1.955   1.00 13.10 ? 10  ASN C N   1 
ATOM   2991 C  CA  . ASN C 1 22  ? -6.999  11.766  2.862   1.00 13.46 ? 10  ASN C CA  1 
ATOM   2992 C  C   . ASN C 1 22  ? -8.515  11.700  2.558   1.00 12.49 ? 10  ASN C C   1 
ATOM   2993 O  O   . ASN C 1 22  ? -9.200  12.680  2.721   1.00 12.30 ? 10  ASN C O   1 
ATOM   2994 C  CB  . ASN C 1 22  ? -6.642  12.036  4.315   1.00 13.97 ? 10  ASN C CB  1 
ATOM   2995 C  CG  . ASN C 1 22  ? -7.214  10.951  5.195   1.00 14.65 ? 10  ASN C CG  1 
ATOM   2996 O  OD1 . ASN C 1 22  ? -8.245  11.169  5.834   1.00 17.74 ? 10  ASN C OD1 1 
ATOM   2997 N  ND2 . ASN C 1 22  ? -6.561  9.792   5.203   1.00 14.86 ? 10  ASN C ND2 1 
ATOM   2998 N  N   . ASN C 1 23  ? -8.976  10.582  2.006   1.00 13.03 ? 11  ASN C N   1 
ATOM   2999 C  CA  . ASN C 1 23  ? -10.427 10.315  1.840   1.00 13.86 ? 11  ASN C CA  1 
ATOM   3000 C  C   . ASN C 1 23  ? -11.069 11.413  0.997   1.00 14.71 ? 11  ASN C C   1 
ATOM   3001 O  O   . ASN C 1 23  ? -12.229 11.844  1.320   1.00 15.71 ? 11  ASN C O   1 
ATOM   3002 C  CB  . ASN C 1 23  ? -11.056 10.112  3.220   1.00 15.05 ? 11  ASN C CB  1 
ATOM   3003 C  CG  . ASN C 1 23  ? -10.473 8.944   3.963   1.00 17.81 ? 11  ASN C CG  1 
ATOM   3004 O  OD1 . ASN C 1 23  ? -10.358 7.885   3.391   1.00 19.27 ? 11  ASN C OD1 1 
ATOM   3005 N  ND2 . ASN C 1 23  ? -10.147 9.088   5.242   1.00 19.18 ? 11  ASN C ND2 1 
ATOM   3006 N  N   . GLY C 1 24  ? -10.410 11.831  -0.084  1.00 13.62 ? 12  GLY C N   1 
ATOM   3007 C  CA  . GLY C 1 24  ? -10.929 12.804  -1.073  1.00 14.31 ? 12  GLY C CA  1 
ATOM   3008 C  C   . GLY C 1 24  ? -10.736 14.257  -0.679  1.00 12.48 ? 12  GLY C C   1 
ATOM   3009 O  O   . GLY C 1 24  ? -11.249 15.127  -1.388  1.00 15.15 ? 12  GLY C O   1 
ATOM   3010 N  N   . TYR C 1 25  ? -10.072 14.533  0.443   1.00 11.83 ? 13  TYR C N   1 
ATOM   3011 C  CA  . TYR C 1 25  ? -9.799  15.911  0.951   1.00 10.82 ? 13  TYR C CA  1 
ATOM   3012 C  C   . TYR C 1 25  ? -8.300  16.169  0.911   1.00 10.87 ? 13  TYR C C   1 
ATOM   3013 O  O   . TYR C 1 25  ? -7.504  15.280  1.291   1.00 10.73 ? 13  TYR C O   1 
ATOM   3014 C  CB  . TYR C 1 25  ? -10.312 16.061  2.379   1.00 11.84 ? 13  TYR C CB  1 
ATOM   3015 C  CG  . TYR C 1 25  ? -11.809 16.066  2.375   1.00 13.09 ? 13  TYR C CG  1 
ATOM   3016 C  CD1 . TYR C 1 25  ? -12.486 17.245  2.160   1.00 16.59 ? 13  TYR C CD1 1 
ATOM   3017 C  CD2 . TYR C 1 25  ? -12.544 14.894  2.474   1.00 16.59 ? 13  TYR C CD2 1 
ATOM   3018 C  CE1 . TYR C 1 25  ? -13.867 17.272  2.074   1.00 19.65 ? 13  TYR C CE1 1 
ATOM   3019 C  CE2 . TYR C 1 25  ? -13.923 14.905  2.407   1.00 17.02 ? 13  TYR C CE2 1 
ATOM   3020 C  CZ  . TYR C 1 25  ? -14.581 16.105  2.222   1.00 18.90 ? 13  TYR C CZ  1 
ATOM   3021 O  OH  . TYR C 1 25  ? -15.942 16.213  2.150   1.00 25.87 ? 13  TYR C OH  1 
ATOM   3022 N  N   . TYR C 1 26  ? -7.952  17.410  0.592   1.00 11.57 ? 14  TYR C N   1 
ATOM   3023 C  CA  . TYR C 1 26  ? -6.596  17.951  0.782   1.00 11.79 ? 14  TYR C CA  1 
ATOM   3024 C  C   . TYR C 1 26  ? -6.409  18.068  2.280   1.00 11.59 ? 14  TYR C C   1 
ATOM   3025 O  O   . TYR C 1 26  ? -7.382  18.519  2.968   1.00 11.28 ? 14  TYR C O   1 
ATOM   3026 C  CB  . TYR C 1 26  ? -6.475  19.303  0.095   1.00 13.86 ? 14  TYR C CB  1 
ATOM   3027 C  CG  . TYR C 1 26  ? -5.189  19.985  0.407   1.00 13.37 ? 14  TYR C CG  1 
ATOM   3028 C  CD1 . TYR C 1 26  ? -4.035  19.675  -0.297  1.00 15.17 ? 14  TYR C CD1 1 
ATOM   3029 C  CD2 . TYR C 1 26  ? -5.100  20.867  1.475   1.00 14.51 ? 14  TYR C CD2 1 
ATOM   3030 C  CE1 . TYR C 1 26  ? -2.841  20.296  0.008   1.00 14.92 ? 14  TYR C CE1 1 
ATOM   3031 C  CE2 . TYR C 1 26  ? -3.898  21.463  1.815   1.00 13.83 ? 14  TYR C CE2 1 
ATOM   3032 C  CZ  . TYR C 1 26  ? -2.771  21.207  1.052   1.00 14.89 ? 14  TYR C CZ  1 
ATOM   3033 O  OH  . TYR C 1 26  ? -1.559  21.745  1.381   1.00 15.43 ? 14  TYR C OH  1 
ATOM   3034 N  N   . TYR C 1 27  ? -5.262  17.722  2.811   1.00 12.24 ? 15  TYR C N   1 
ATOM   3035 C  CA  . TYR C 1 27  ? -4.984  18.079  4.221   1.00 12.54 ? 15  TYR C CA  1 
ATOM   3036 C  C   . TYR C 1 27  ? -3.614  18.695  4.323   1.00 13.41 ? 15  TYR C C   1 
ATOM   3037 O  O   . TYR C 1 27  ? -2.707  18.420  3.531   1.00 13.40 ? 15  TYR C O   1 
ATOM   3038 C  CB  . TYR C 1 27  ? -5.149  16.913  5.209   1.00 13.33 ? 15  TYR C CB  1 
ATOM   3039 C  CG  . TYR C 1 27  ? -4.057  15.891  5.136   1.00 13.52 ? 15  TYR C CG  1 
ATOM   3040 C  CD1 . TYR C 1 27  ? -4.129  14.832  4.256   1.00 12.52 ? 15  TYR C CD1 1 
ATOM   3041 C  CD2 . TYR C 1 27  ? -2.936  15.999  5.940   1.00 13.90 ? 15  TYR C CD2 1 
ATOM   3042 C  CE1 . TYR C 1 27  ? -3.128  13.880  4.181   1.00 13.58 ? 15  TYR C CE1 1 
ATOM   3043 C  CE2 . TYR C 1 27  ? -1.958  15.045  5.904   1.00 15.62 ? 15  TYR C CE2 1 
ATOM   3044 C  CZ  . TYR C 1 27  ? -2.018  14.013  4.991   1.00 15.05 ? 15  TYR C CZ  1 
ATOM   3045 O  OH  . TYR C 1 27  ? -0.991  13.114  4.966   1.00 18.72 ? 15  TYR C OH  1 
ATOM   3046 N  N   . SER C 1 28  ? -3.501  19.591  5.302   1.00 13.30 ? 16  SER C N   1 
ATOM   3047 C  CA  . SER C 1 28  ? -2.200  20.219  5.603   1.00 14.27 ? 16  SER C CA  1 
ATOM   3048 C  C   . SER C 1 28  ? -2.070  20.249  7.109   1.00 14.25 ? 16  SER C C   1 
ATOM   3049 O  O   . SER C 1 28  ? -3.014  20.785  7.790   1.00 14.20 ? 16  SER C O   1 
ATOM   3050 C  CB  . SER C 1 28  ? -2.082  21.593  4.991   1.00 15.30 ? 16  SER C CB  1 
ATOM   3051 O  OG  . SER C 1 28  ? -0.911  22.247  5.468   1.00 17.37 ? 16  SER C OG  1 
ATOM   3052 N  N   . PHE C 1 29  ? -0.943  19.753  7.616   1.00 13.83 ? 17  PHE C N   1 
ATOM   3053 C  CA  . PHE C 1 29  ? -0.590  19.893  9.039   1.00 14.46 ? 17  PHE C CA  1 
ATOM   3054 C  C   . PHE C 1 29  ? 0.749   20.626  9.054   1.00 14.11 ? 17  PHE C C   1 
ATOM   3055 O  O   . PHE C 1 29  ? 1.734   20.083  8.463   1.00 15.98 ? 17  PHE C O   1 
ATOM   3056 C  CB  . PHE C 1 29  ? -0.542  18.523  9.697   1.00 15.45 ? 17  PHE C CB  1 
ATOM   3057 C  CG  . PHE C 1 29  ? 0.005   18.577  11.084  1.00 15.82 ? 17  PHE C CG  1 
ATOM   3058 C  CD1 . PHE C 1 29  ? -0.573  19.401  12.030  1.00 15.97 ? 17  PHE C CD1 1 
ATOM   3059 C  CD2 . PHE C 1 29  ? 1.153   17.883  11.427  1.00 17.72 ? 17  PHE C CD2 1 
ATOM   3060 C  CE1 . PHE C 1 29  ? -0.046  19.487  13.309  1.00 17.08 ? 17  PHE C CE1 1 
ATOM   3061 C  CE2 . PHE C 1 29  ? 1.656   17.947  12.720  1.00 19.43 ? 17  PHE C CE2 1 
ATOM   3062 C  CZ  . PHE C 1 29  ? 1.077   18.775  13.657  1.00 17.29 ? 17  PHE C CZ  1 
ATOM   3063 N  N   . TRP C 1 30  ? 0.803   21.809  9.654   1.00 14.23 ? 18  TRP C N   1 
ATOM   3064 C  CA  . TRP C 1 30  ? 2.079   22.570  9.743   1.00 15.31 ? 18  TRP C CA  1 
ATOM   3065 C  C   . TRP C 1 30  ? 2.369   22.855  11.217  1.00 16.89 ? 18  TRP C C   1 
ATOM   3066 O  O   . TRP C 1 30  ? 1.447   23.336  11.924  1.00 15.01 ? 18  TRP C O   1 
ATOM   3067 C  CB  . TRP C 1 30  ? 2.040   23.819  8.874   1.00 19.38 ? 18  TRP C CB  1 
ATOM   3068 C  CG  . TRP C 1 30  ? 3.308   24.600  8.985   1.00 22.99 ? 18  TRP C CG  1 
ATOM   3069 C  CD1 . TRP C 1 30  ? 4.458   24.450  8.253   1.00 31.61 ? 18  TRP C CD1 1 
ATOM   3070 C  CD2 . TRP C 1 30  ? 3.584   25.618  9.966   1.00 27.11 ? 18  TRP C CD2 1 
ATOM   3071 N  NE1 . TRP C 1 30  ? 5.421   25.323  8.702   1.00 30.20 ? 18  TRP C NE1 1 
ATOM   3072 C  CE2 . TRP C 1 30  ? 4.912   26.045  9.751   1.00 30.46 ? 18  TRP C CE2 1 
ATOM   3073 C  CE3 . TRP C 1 30  ? 2.836   26.210  10.984  1.00 28.46 ? 18  TRP C CE3 1 
ATOM   3074 C  CZ2 . TRP C 1 30  ? 5.496   27.040  10.535  1.00 32.18 ? 18  TRP C CZ2 1 
ATOM   3075 C  CZ3 . TRP C 1 30  ? 3.420   27.189  11.761  1.00 32.83 ? 18  TRP C CZ3 1 
ATOM   3076 C  CH2 . TRP C 1 30  ? 4.745   27.580  11.546  1.00 30.01 ? 18  TRP C CH2 1 
ATOM   3077 N  N   . THR C 1 31  ? 3.561   22.520  11.707  1.00 17.33 ? 19  THR C N   1 
ATOM   3078 C  CA  . THR C 1 31  ? 3.968   22.903  13.087  1.00 17.54 ? 19  THR C CA  1 
ATOM   3079 C  C   . THR C 1 31  ? 5.403   23.430  13.008  1.00 20.25 ? 19  THR C C   1 
ATOM   3080 O  O   . THR C 1 31  ? 6.220   22.897  12.189  1.00 21.93 ? 19  THR C O   1 
ATOM   3081 C  CB  . THR C 1 31  ? 3.723   21.762  14.088  1.00 18.90 ? 19  THR C CB  1 
ATOM   3082 O  OG1 . THR C 1 31  ? 4.115   22.217  15.392  1.00 20.79 ? 19  THR C OG1 1 
ATOM   3083 C  CG2 . THR C 1 31  ? 4.446   20.472  13.749  1.00 18.27 ? 19  THR C CG2 1 
ATOM   3084 N  N   . ASP C 1 32  ? 5.728   24.432  13.814  1.00 20.72 ? 20  ASP C N   1 
ATOM   3085 C  CA  . ASP C 1 32  ? 7.146   24.875  13.941  1.00 26.13 ? 20  ASP C CA  1 
ATOM   3086 C  C   . ASP C 1 32  ? 7.937   23.895  14.832  1.00 27.86 ? 20  ASP C C   1 
ATOM   3087 O  O   . ASP C 1 32  ? 9.153   24.115  14.996  1.00 31.57 ? 20  ASP C O   1 
ATOM   3088 C  CB  . ASP C 1 32  ? 7.214   26.331  14.402  1.00 28.43 ? 20  ASP C CB  1 
ATOM   3089 C  CG  . ASP C 1 32  ? 6.665   26.555  15.794  1.00 27.93 ? 20  ASP C CG  1 
ATOM   3090 O  OD1 . ASP C 1 32  ? 6.395   25.559  16.479  1.00 30.35 ? 20  ASP C OD1 1 
ATOM   3091 O  OD2 . ASP C 1 32  ? 6.512   27.718  16.164  1.00 29.71 ? 20  ASP C OD2 1 
ATOM   3092 N  N   . GLY C 1 33  ? 7.314   22.854  15.395  1.00 26.55 ? 21  GLY C N   1 
ATOM   3093 C  CA  . GLY C 1 33  ? 8.006   21.823  16.213  1.00 29.25 ? 21  GLY C CA  1 
ATOM   3094 C  C   . GLY C 1 33  ? 7.920   22.045  17.720  1.00 29.47 ? 21  GLY C C   1 
ATOM   3095 O  O   . GLY C 1 33  ? 8.250   21.086  18.485  1.00 34.92 ? 21  GLY C O   1 
ATOM   3096 N  N   . GLY C 1 34  ? 7.459   23.220  18.161  1.00 27.09 ? 22  GLY C N   1 
ATOM   3097 C  CA  . GLY C 1 34  ? 7.287   23.577  19.583  1.00 27.42 ? 22  GLY C CA  1 
ATOM   3098 C  C   . GLY C 1 34  ? 6.302   22.674  20.309  1.00 27.12 ? 22  GLY C C   1 
ATOM   3099 O  O   . GLY C 1 34  ? 5.225   22.345  19.725  1.00 25.70 ? 22  GLY C O   1 
ATOM   3100 N  N   . GLY C 1 35  ? 6.636   22.278  21.544  1.00 25.61 ? 23  GLY C N   1 
ATOM   3101 C  CA  . GLY C 1 35  ? 5.773   21.475  22.434  1.00 25.39 ? 23  GLY C CA  1 
ATOM   3102 C  C   . GLY C 1 35  ? 5.312   20.179  21.777  1.00 26.09 ? 23  GLY C C   1 
ATOM   3103 O  O   . GLY C 1 35  ? 6.110   19.598  21.007  1.00 22.03 ? 23  GLY C O   1 
ATOM   3104 N  N   . GLN C 1 36  ? 4.062   19.771  22.020  1.00 24.20 ? 24  GLN C N   1 
ATOM   3105 C  CA  . GLN C 1 36  ? 3.444   18.531  21.479  1.00 26.05 ? 24  GLN C CA  1 
ATOM   3106 C  C   . GLN C 1 36  ? 2.222   18.952  20.659  1.00 22.17 ? 24  GLN C C   1 
ATOM   3107 O  O   . GLN C 1 36  ? 1.297   19.562  21.225  1.00 19.31 ? 24  GLN C O   1 
ATOM   3108 C  CB  . GLN C 1 36  ? 3.112   17.559  22.613  1.00 33.14 ? 24  GLN C CB  1 
ATOM   3109 C  CG  . GLN C 1 36  ? 2.591   16.203  22.156  1.00 40.52 ? 24  GLN C CG  1 
ATOM   3110 C  CD  . GLN C 1 36  ? 3.670   15.204  21.797  1.00 48.13 ? 24  GLN C CD  1 
ATOM   3111 O  OE1 . GLN C 1 36  ? 4.696   15.529  21.191  1.00 48.87 ? 24  GLN C OE1 1 
ATOM   3112 N  NE2 . GLN C 1 36  ? 3.424   13.952  22.153  1.00 48.10 ? 24  GLN C NE2 1 
ATOM   3113 N  N   . VAL C 1 37  ? 2.225   18.649  19.371  1.00 20.32 ? 25  VAL C N   1 
ATOM   3114 C  CA  . VAL C 1 37  ? 1.003   18.796  18.540  1.00 18.43 ? 25  VAL C CA  1 
ATOM   3115 C  C   . VAL C 1 37  ? 0.783   17.491  17.784  1.00 18.82 ? 25  VAL C C   1 
ATOM   3116 O  O   . VAL C 1 37  ? 1.698   17.090  17.021  1.00 22.20 ? 25  VAL C O   1 
ATOM   3117 C  CB  . VAL C 1 37  ? 1.081   19.994  17.579  1.00 17.15 ? 25  VAL C CB  1 
ATOM   3118 C  CG1 . VAL C 1 37  ? -0.227  20.192  16.852  1.00 18.40 ? 25  VAL C CG1 1 
ATOM   3119 C  CG2 . VAL C 1 37  ? 1.505   21.283  18.261  1.00 19.73 ? 25  VAL C CG2 1 
ATOM   3120 N  N   . THR C 1 38  ? -0.374  16.875  17.965  1.00 17.85 ? 26  THR C N   1 
ATOM   3121 C  CA  . THR C 1 38  ? -0.712  15.564  17.327  1.00 18.76 ? 26  THR C CA  1 
ATOM   3122 C  C   . THR C 1 38  ? -1.949  15.775  16.450  1.00 18.01 ? 26  THR C C   1 
ATOM   3123 O  O   . THR C 1 38  ? -3.038  16.076  16.976  1.00 16.90 ? 26  THR C O   1 
ATOM   3124 C  CB  . THR C 1 38  ? -0.872  14.423  18.336  1.00 22.91 ? 26  THR C CB  1 
ATOM   3125 O  OG1 . THR C 1 38  ? 0.301   14.367  19.151  1.00 27.69 ? 26  THR C OG1 1 
ATOM   3126 C  CG2 . THR C 1 38  ? -1.079  13.076  17.675  1.00 26.35 ? 26  THR C CG2 1 
ATOM   3127 N  N   . TYR C 1 39  ? -1.792  15.442  15.172  1.00 16.57 ? 27  TYR C N   1 
ATOM   3128 C  CA  . TYR C 1 39  ? -2.827  15.556  14.123  1.00 15.90 ? 27  TYR C CA  1 
ATOM   3129 C  C   . TYR C 1 39  ? -3.244  14.147  13.684  1.00 16.47 ? 27  TYR C C   1 
ATOM   3130 O  O   . TYR C 1 39  ? -2.373  13.259  13.486  1.00 17.83 ? 27  TYR C O   1 
ATOM   3131 C  CB  . TYR C 1 39  ? -2.283  16.441  12.991  1.00 15.10 ? 27  TYR C CB  1 
ATOM   3132 C  CG  . TYR C 1 39  ? -3.205  16.491  11.807  1.00 15.12 ? 27  TYR C CG  1 
ATOM   3133 C  CD1 . TYR C 1 39  ? -3.164  15.505  10.845  1.00 15.71 ? 27  TYR C CD1 1 
ATOM   3134 C  CD2 . TYR C 1 39  ? -4.134  17.497  11.648  1.00 13.64 ? 27  TYR C CD2 1 
ATOM   3135 C  CE1 . TYR C 1 39  ? -4.019  15.524  9.756   1.00 16.72 ? 27  TYR C CE1 1 
ATOM   3136 C  CE2 . TYR C 1 39  ? -4.995  17.535  10.570  1.00 14.55 ? 27  TYR C CE2 1 
ATOM   3137 C  CZ  . TYR C 1 39  ? -4.928  16.545  9.605   1.00 14.10 ? 27  TYR C CZ  1 
ATOM   3138 O  OH  . TYR C 1 39  ? -5.781  16.525  8.547   1.00 14.94 ? 27  TYR C OH  1 
ATOM   3139 N  N   . THR C 1 40  ? -4.549  13.932  13.535  1.00 14.94 ? 28  THR C N   1 
ATOM   3140 C  CA  . THR C 1 40  ? -5.101  12.638  13.087  1.00 17.58 ? 28  THR C CA  1 
ATOM   3141 C  C   . THR C 1 40  ? -6.111  12.897  11.973  1.00 15.81 ? 28  THR C C   1 
ATOM   3142 O  O   . THR C 1 40  ? -7.034  13.686  12.173  1.00 16.56 ? 28  THR C O   1 
ATOM   3143 C  CB  . THR C 1 40  ? -5.683  11.811  14.252  1.00 22.37 ? 28  THR C CB  1 
ATOM   3144 O  OG1 . THR C 1 40  ? -4.671  11.681  15.259  1.00 27.84 ? 28  THR C OG1 1 
ATOM   3145 C  CG2 . THR C 1 40  ? -6.148  10.446  13.790  1.00 24.05 ? 28  THR C CG2 1 
ATOM   3146 N  N   . ASN C 1 41  ? -5.944  12.256  10.811  1.00 14.76 ? 29  ASN C N   1 
ATOM   3147 C  CA  . ASN C 1 41  ? -7.023  12.206  9.788   1.00 14.81 ? 29  ASN C CA  1 
ATOM   3148 C  C   . ASN C 1 41  ? -8.056  11.148  10.152  1.00 17.35 ? 29  ASN C C   1 
ATOM   3149 O  O   . ASN C 1 41  ? -7.674  9.973   10.542  1.00 17.70 ? 29  ASN C O   1 
ATOM   3150 C  CB  . ASN C 1 41  ? -6.474  11.856  8.403   1.00 15.18 ? 29  ASN C CB  1 
ATOM   3151 C  CG  . ASN C 1 41  ? -5.786  13.045  7.763   1.00 14.92 ? 29  ASN C CG  1 
ATOM   3152 O  OD1 . ASN C 1 41  ? -6.333  14.158  7.761   1.00 17.98 ? 29  ASN C OD1 1 
ATOM   3153 N  ND2 . ASN C 1 41  ? -4.589  12.826  7.233   1.00 15.56 ? 29  ASN C ND2 1 
ATOM   3154 N  N   . GLY C 1 42  ? -9.313  11.537  10.036  1.00 16.84 ? 30  GLY C N   1 
ATOM   3155 C  CA  . GLY C 1 42  ? -10.457 10.639  10.214  1.00 17.24 ? 30  GLY C CA  1 
ATOM   3156 C  C   . GLY C 1 42  ? -11.121 10.319  8.892   1.00 18.00 ? 30  GLY C C   1 
ATOM   3157 O  O   . GLY C 1 42  ? -10.617 10.638  7.799   1.00 18.20 ? 30  GLY C O   1 
ATOM   3158 N  N   . PRO C 1 43  ? -12.279 9.642   8.954   1.00 19.36 ? 31  PRO C N   1 
ATOM   3159 C  CA  . PRO C 1 43  ? -13.041 9.351   7.747   1.00 20.21 ? 31  PRO C CA  1 
ATOM   3160 C  C   . PRO C 1 43  ? -13.576 10.614  7.068   1.00 19.61 ? 31  PRO C C   1 
ATOM   3161 O  O   . PRO C 1 43  ? -13.887 11.597  7.810   1.00 18.76 ? 31  PRO C O   1 
ATOM   3162 C  CB  . PRO C 1 43  ? -14.212 8.494   8.260   1.00 21.16 ? 31  PRO C CB  1 
ATOM   3163 C  CG  . PRO C 1 43  ? -13.768 7.957   9.590   1.00 23.33 ? 31  PRO C CG  1 
ATOM   3164 C  CD  . PRO C 1 43  ? -12.833 8.998   10.167  1.00 23.10 ? 31  PRO C CD  1 
ATOM   3165 N  N   . ALA C 1 44  ? -13.733 10.543  5.746   1.00 16.37 ? 32  ALA C N   1 
ATOM   3166 C  CA  . ALA C 1 44  ? -14.313 11.593  4.877   1.00 15.09 ? 32  ALA C CA  1 
ATOM   3167 C  C   . ALA C 1 44  ? -13.606 12.901  5.278   1.00 16.66 ? 32  ALA C C   1 
ATOM   3168 O  O   . ALA C 1 44  ? -12.333 12.878  5.311   1.00 15.82 ? 32  ALA C O   1 
ATOM   3169 C  CB  . ALA C 1 44  ? -15.813 11.658  5.074   1.00 15.56 ? 32  ALA C CB  1 
ATOM   3170 N  N   . GLY C 1 45  ? -14.340 13.964  5.615   1.00 14.34 ? 33  GLY C N   1 
ATOM   3171 C  CA  . GLY C 1 45  ? -13.698 15.283  5.824   1.00 13.78 ? 33  GLY C CA  1 
ATOM   3172 C  C   . GLY C 1 45  ? -13.278 15.523  7.267   1.00 13.55 ? 33  GLY C C   1 
ATOM   3173 O  O   . GLY C 1 45  ? -13.119 16.719  7.619   1.00 13.89 ? 33  GLY C O   1 
ATOM   3174 N  N   . GLN C 1 46  ? -13.083 14.477  8.080   1.00 14.80 ? 34  GLN C N   1 
ATOM   3175 C  CA  . GLN C 1 46  ? -12.817 14.625  9.531   1.00 15.42 ? 34  GLN C CA  1 
ATOM   3176 C  C   . GLN C 1 46  ? -11.321 14.720  9.809   1.00 12.81 ? 34  GLN C C   1 
ATOM   3177 O  O   . GLN C 1 46  ? -10.522 13.953  9.218   1.00 13.63 ? 34  GLN C O   1 
ATOM   3178 C  CB  . GLN C 1 46  ? -13.417 13.501  10.376  1.00 18.45 ? 34  GLN C CB  1 
ATOM   3179 C  CG  . GLN C 1 46  ? -13.559 13.898  11.829  1.00 21.46 ? 34  GLN C CG  1 
ATOM   3180 C  CD  . GLN C 1 46  ? -12.402 13.487  12.702  1.00 27.13 ? 34  GLN C CD  1 
ATOM   3181 O  OE1 . GLN C 1 46  ? -11.457 12.809  12.279  1.00 34.15 ? 34  GLN C OE1 1 
ATOM   3182 N  NE2 . GLN C 1 46  ? -12.458 13.906  13.957  1.00 28.36 ? 34  GLN C NE2 1 
ATOM   3183 N  N   . TYR C 1 47  ? -10.944 15.608  10.717  1.00 12.07 ? 35  TYR C N   1 
ATOM   3184 C  CA  . TYR C 1 47  ? -9.602  15.598  11.327  1.00 11.75 ? 35  TYR C CA  1 
ATOM   3185 C  C   . TYR C 1 47  ? -9.723  15.992  12.790  1.00 12.31 ? 35  TYR C C   1 
ATOM   3186 O  O   . TYR C 1 47  ? -10.733 16.612  13.199  1.00 13.31 ? 35  TYR C O   1 
ATOM   3187 C  CB  . TYR C 1 47  ? -8.635  16.518  10.576  1.00 12.07 ? 35  TYR C CB  1 
ATOM   3188 C  CG  . TYR C 1 47  ? -8.871  17.997  10.776  1.00 11.85 ? 35  TYR C CG  1 
ATOM   3189 C  CD1 . TYR C 1 47  ? -8.277  18.683  11.832  1.00 11.97 ? 35  TYR C CD1 1 
ATOM   3190 C  CD2 . TYR C 1 47  ? -9.729  18.715  9.953   1.00 11.95 ? 35  TYR C CD2 1 
ATOM   3191 C  CE1 . TYR C 1 47  ? -8.480  20.053  11.997  1.00 12.45 ? 35  TYR C CE1 1 
ATOM   3192 C  CE2 . TYR C 1 47  ? -9.990  20.061  10.149  1.00 12.77 ? 35  TYR C CE2 1 
ATOM   3193 C  CZ  . TYR C 1 47  ? -9.349  20.740  11.169  1.00 12.62 ? 35  TYR C CZ  1 
ATOM   3194 O  OH  . TYR C 1 47  ? -9.545  22.095  11.310  1.00 13.14 ? 35  TYR C OH  1 
ATOM   3195 N  N   . SER C 1 48  ? -8.714  15.593  13.528  1.00 13.70 ? 36  SER C N   1 
ATOM   3196 C  CA  . SER C 1 48  ? -8.552  15.899  14.973  1.00 16.40 ? 36  SER C CA  1 
ATOM   3197 C  C   . SER C 1 48  ? -7.190  16.497  15.204  1.00 15.61 ? 36  SER C C   1 
ATOM   3198 O  O   . SER C 1 48  ? -6.259  16.117  14.479  1.00 16.36 ? 36  SER C O   1 
ATOM   3199 C  CB  . SER C 1 48  ? -8.724  14.643  15.808  1.00 19.80 ? 36  SER C CB  1 
ATOM   3200 O  OG  . SER C 1 48  ? -10.086 14.247  15.770  1.00 26.17 ? 36  SER C OG  1 
ATOM   3201 N  N   . VAL C 1 49  ? -7.063  17.386  16.199  1.00 15.18 ? 37  VAL C N   1 
ATOM   3202 C  CA  . VAL C 1 49  ? -5.722  17.866  16.628  1.00 15.71 ? 37  VAL C CA  1 
ATOM   3203 C  C   . VAL C 1 49  ? -5.747  18.058  18.144  1.00 17.79 ? 37  VAL C C   1 
ATOM   3204 O  O   . VAL C 1 49  ? -6.784  18.475  18.677  1.00 17.02 ? 37  VAL C O   1 
ATOM   3205 C  CB  . VAL C 1 49  ? -5.231  19.107  15.843  1.00 17.84 ? 37  VAL C CB  1 
ATOM   3206 C  CG1 . VAL C 1 49  ? -6.214  20.252  15.828  1.00 20.10 ? 37  VAL C CG1 1 
ATOM   3207 C  CG2 . VAL C 1 49  ? -3.841  19.577  16.295  1.00 17.62 ? 37  VAL C CG2 1 
ATOM   3208 N  N   . GLU C 1 50  ? -4.688  17.602  18.809  1.00 17.47 ? 38  GLU C N   1 
ATOM   3209 C  CA  . GLU C 1 50  ? -4.500  17.656  20.296  1.00 20.68 ? 38  GLU C CA  1 
ATOM   3210 C  C   . GLU C 1 50  ? -3.182  18.356  20.464  1.00 18.67 ? 38  GLU C C   1 
ATOM   3211 O  O   . GLU C 1 50  ? -2.236  17.929  19.783  1.00 17.27 ? 38  GLU C O   1 
ATOM   3212 C  CB  . GLU C 1 50  ? -4.389  16.283  20.986  1.00 25.68 ? 38  GLU C CB  1 
ATOM   3213 C  CG  . GLU C 1 50  ? -3.274  16.120  22.047  1.00 36.07 ? 38  GLU C CG  1 
ATOM   3214 C  CD  . GLU C 1 50  ? -2.007  15.282  21.762  1.00 37.53 ? 38  GLU C CD  1 
ATOM   3215 O  OE1 . GLU C 1 50  ? -2.109  14.000  21.630  1.00 42.27 ? 38  GLU C OE1 1 
ATOM   3216 O  OE2 . GLU C 1 50  ? -0.879  15.871  21.742  1.00 38.31 ? 38  GLU C OE2 1 
ATOM   3217 N  N   . TRP C 1 51  ? -3.118  19.412  21.281  1.00 18.60 ? 39  TRP C N   1 
ATOM   3218 C  CA  . TRP C 1 51  ? -1.841  20.113  21.479  1.00 16.52 ? 39  TRP C CA  1 
ATOM   3219 C  C   . TRP C 1 51  ? -1.649  20.525  22.942  1.00 17.38 ? 39  TRP C C   1 
ATOM   3220 O  O   . TRP C 1 51  ? -2.636  20.697  23.679  1.00 18.02 ? 39  TRP C O   1 
ATOM   3221 C  CB  . TRP C 1 51  ? -1.738  21.278  20.495  1.00 16.68 ? 39  TRP C CB  1 
ATOM   3222 C  CG  . TRP C 1 51  ? -2.660  22.440  20.722  1.00 14.73 ? 39  TRP C CG  1 
ATOM   3223 C  CD1 . TRP C 1 51  ? -2.315  23.625  21.310  1.00 15.54 ? 39  TRP C CD1 1 
ATOM   3224 C  CD2 . TRP C 1 51  ? -4.035  22.590  20.289  1.00 15.61 ? 39  TRP C CD2 1 
ATOM   3225 N  NE1 . TRP C 1 51  ? -3.360  24.495  21.243  1.00 16.35 ? 39  TRP C NE1 1 
ATOM   3226 C  CE2 . TRP C 1 51  ? -4.435  23.894  20.651  1.00 14.92 ? 39  TRP C CE2 1 
ATOM   3227 C  CE3 . TRP C 1 51  ? -4.950  21.787  19.598  1.00 14.95 ? 39  TRP C CE3 1 
ATOM   3228 C  CZ2 . TRP C 1 51  ? -5.700  24.405  20.340  1.00 14.32 ? 39  TRP C CZ2 1 
ATOM   3229 C  CZ3 . TRP C 1 51  ? -6.224  22.255  19.356  1.00 14.49 ? 39  TRP C CZ3 1 
ATOM   3230 C  CH2 . TRP C 1 51  ? -6.587  23.572  19.694  1.00 13.88 ? 39  TRP C CH2 1 
ATOM   3231 N  N   . SER C 1 52  ? -0.377  20.613  23.323  1.00 20.25 ? 40  SER C N   1 
ATOM   3232 C  CA  . SER C 1 52  ? 0.080   20.946  24.689  1.00 21.51 ? 40  SER C CA  1 
ATOM   3233 C  C   . SER C 1 52  ? 1.332   21.802  24.572  1.00 20.25 ? 40  SER C C   1 
ATOM   3234 O  O   . SER C 1 52  ? 2.310   21.365  23.906  1.00 21.15 ? 40  SER C O   1 
ATOM   3235 C  CB  . SER C 1 52  ? 0.350   19.699  25.502  1.00 26.02 ? 40  SER C CB  1 
ATOM   3236 O  OG  . SER C 1 52  ? 0.556   20.068  26.862  1.00 36.57 ? 40  SER C OG  1 
ATOM   3237 N  N   . ASN C 1 53  ? 1.295   22.990  25.180  1.00 20.62 ? 41  ASN C N   1 
ATOM   3238 C  CA  . ASN C 1 53  ? 2.424   23.946  25.233  1.00 21.83 ? 41  ASN C CA  1 
ATOM   3239 C  C   . ASN C 1 53  ? 3.007   24.114  23.825  1.00 23.29 ? 41  ASN C C   1 
ATOM   3240 O  O   . ASN C 1 53  ? 4.222   24.027  23.656  1.00 23.21 ? 41  ASN C O   1 
ATOM   3241 C  CB  . ASN C 1 53  ? 3.448   23.505  26.281  1.00 23.94 ? 41  ASN C CB  1 
ATOM   3242 C  CG  . ASN C 1 53  ? 2.837   23.533  27.661  1.00 25.88 ? 41  ASN C CG  1 
ATOM   3243 O  OD1 . ASN C 1 53  ? 2.238   24.541  28.050  1.00 25.29 ? 41  ASN C OD1 1 
ATOM   3244 N  ND2 . ASN C 1 53  ? 2.895   22.399  28.341  1.00 27.81 ? 41  ASN C ND2 1 
ATOM   3245 N  N   . SER C 1 54  ? 2.156   24.368  22.832  1.00 22.09 ? 42  SER C N   1 
ATOM   3246 C  CA  . SER C 1 54  ? 2.540   24.344  21.404  1.00 22.14 ? 42  SER C CA  1 
ATOM   3247 C  C   . SER C 1 54  ? 3.415   25.528  21.033  1.00 20.64 ? 42  SER C C   1 
ATOM   3248 O  O   . SER C 1 54  ? 3.350   26.611  21.661  1.00 20.68 ? 42  SER C O   1 
ATOM   3249 C  CB  . SER C 1 54  ? 1.315   24.354  20.506  1.00 21.52 ? 42  SER C CB  1 
ATOM   3250 O  OG  . SER C 1 54  ? 0.661   25.636  20.558  1.00 22.48 ? 42  SER C OG  1 
ATOM   3251 N  N   . GLY C 1 55  ? 4.192   25.352  19.975  1.00 20.85 ? 43  GLY C N   1 
ATOM   3252 C  CA  . GLY C 1 55  ? 4.620   26.496  19.176  1.00 23.15 ? 43  GLY C CA  1 
ATOM   3253 C  C   . GLY C 1 55  ? 3.467   26.903  18.288  1.00 23.84 ? 43  GLY C C   1 
ATOM   3254 O  O   . GLY C 1 55  ? 2.283   26.751  18.726  1.00 24.80 ? 43  GLY C O   1 
ATOM   3255 N  N   . ASN C 1 56  ? 3.789   27.391  17.095  1.00 19.62 ? 44  ASN C N   1 
ATOM   3256 C  CA  . ASN C 1 56  ? 2.792   27.778  16.075  1.00 21.39 ? 44  ASN C CA  1 
ATOM   3257 C  C   . ASN C 1 56  ? 2.389   26.489  15.344  1.00 19.47 ? 44  ASN C C   1 
ATOM   3258 O  O   . ASN C 1 56  ? 3.291   25.691  14.988  1.00 18.25 ? 44  ASN C O   1 
ATOM   3259 C  CB  . ASN C 1 56  ? 3.344   28.846  15.131  1.00 25.51 ? 44  ASN C CB  1 
ATOM   3260 C  CG  . ASN C 1 56  ? 2.327   29.907  14.762  1.00 34.87 ? 44  ASN C CG  1 
ATOM   3261 O  OD1 . ASN C 1 56  ? 2.049   30.813  15.553  1.00 42.83 ? 44  ASN C OD1 1 
ATOM   3262 N  ND2 . ASN C 1 56  ? 1.788   29.829  13.556  1.00 42.33 ? 44  ASN C ND2 1 
ATOM   3263 N  N   . PHE C 1 57  ? 1.089   26.289  15.101  1.00 16.89 ? 45  PHE C N   1 
ATOM   3264 C  CA  . PHE C 1 57  ? 0.662   25.201  14.178  1.00 14.74 ? 45  PHE C CA  1 
ATOM   3265 C  C   . PHE C 1 57  ? -0.602  25.664  13.477  1.00 15.24 ? 45  PHE C C   1 
ATOM   3266 O  O   . PHE C 1 57  ? -1.318  26.526  14.003  1.00 12.89 ? 45  PHE C O   1 
ATOM   3267 C  CB  . PHE C 1 57  ? 0.430   23.886  14.909  1.00 15.51 ? 45  PHE C CB  1 
ATOM   3268 C  CG  . PHE C 1 57  ? -0.837  23.874  15.728  1.00 15.43 ? 45  PHE C CG  1 
ATOM   3269 C  CD1 . PHE C 1 57  ? -0.823  24.332  17.022  1.00 15.97 ? 45  PHE C CD1 1 
ATOM   3270 C  CD2 . PHE C 1 57  ? -2.029  23.426  15.188  1.00 15.01 ? 45  PHE C CD2 1 
ATOM   3271 C  CE1 . PHE C 1 57  ? -1.973  24.299  17.790  1.00 17.05 ? 45  PHE C CE1 1 
ATOM   3272 C  CE2 . PHE C 1 57  ? -3.197  23.441  15.939  1.00 16.11 ? 45  PHE C CE2 1 
ATOM   3273 C  CZ  . PHE C 1 57  ? -3.166  23.905  17.232  1.00 17.27 ? 45  PHE C CZ  1 
ATOM   3274 N  N   . VAL C 1 58  ? -0.869  25.048  12.326  1.00 13.30 ? 46  VAL C N   1 
ATOM   3275 C  CA  . VAL C 1 58  ? -2.084  25.307  11.522  1.00 14.53 ? 46  VAL C CA  1 
ATOM   3276 C  C   . VAL C 1 58  ? -2.408  23.965  10.894  1.00 14.75 ? 46  VAL C C   1 
ATOM   3277 O  O   . VAL C 1 58  ? -1.502  23.417  10.244  1.00 16.62 ? 46  VAL C O   1 
ATOM   3278 C  CB  . VAL C 1 58  ? -1.888  26.406  10.444  1.00 16.85 ? 46  VAL C CB  1 
ATOM   3279 C  CG1 . VAL C 1 58  ? -3.220  26.646  9.723   1.00 17.83 ? 46  VAL C CG1 1 
ATOM   3280 C  CG2 . VAL C 1 58  ? -1.353  27.725  11.002  1.00 19.37 ? 46  VAL C CG2 1 
ATOM   3281 N  N   . ALA C 1 59  ? -3.643  23.460  11.031  1.00 12.72 ? 47  ALA C N   1 
ATOM   3282 C  CA  . ALA C 1 59  ? -3.985  22.093  10.582  1.00 12.15 ? 47  ALA C CA  1 
ATOM   3283 C  C   . ALA C 1 59  ? -5.410  22.039  10.074  1.00 11.53 ? 47  ALA C C   1 
ATOM   3284 O  O   . ALA C 1 59  ? -6.281  22.666  10.676  1.00 11.13 ? 47  ALA C O   1 
ATOM   3285 C  CB  . ALA C 1 59  ? -3.816  21.124  11.703  1.00 13.81 ? 47  ALA C CB  1 
ATOM   3286 N  N   . GLY C 1 60  ? -5.624  21.354  8.962   1.00 9.92  ? 48  GLY C N   1 
ATOM   3287 C  CA  . GLY C 1 60  ? -6.996  21.167  8.528   1.00 11.08 ? 48  GLY C CA  1 
ATOM   3288 C  C   . GLY C 1 60  ? -7.144  20.423  7.214   1.00 11.68 ? 48  GLY C C   1 
ATOM   3289 O  O   . GLY C 1 60  ? -6.125  20.056  6.533   1.00 11.66 ? 48  GLY C O   1 
ATOM   3290 N  N   . LYS C 1 61  ? -8.400  20.211  6.873   1.00 12.60 ? 49  LYS C N   1 
ATOM   3291 C  CA  . LYS C 1 61  ? -8.798  19.529  5.640   1.00 12.96 ? 49  LYS C CA  1 
ATOM   3292 C  C   . LYS C 1 61  ? -9.563  20.496  4.751   1.00 11.41 ? 49  LYS C C   1 
ATOM   3293 O  O   . LYS C 1 61  ? -10.258 21.421  5.224   1.00 11.97 ? 49  LYS C O   1 
ATOM   3294 C  CB  . LYS C 1 61  ? -9.686  18.306  5.912   1.00 12.91 ? 49  LYS C CB  1 
ATOM   3295 C  CG  . LYS C 1 61  ? -8.947  16.996  6.106   1.00 12.71 ? 49  LYS C CG  1 
ATOM   3296 C  CD  . LYS C 1 61  ? -9.859  15.845  6.321   1.00 13.07 ? 49  LYS C CD  1 
ATOM   3297 C  CE  . LYS C 1 61  ? -9.157  14.528  6.161   1.00 14.55 ? 49  LYS C CE  1 
ATOM   3298 N  NZ  . LYS C 1 61  ? -9.996  13.361  6.487   1.00 13.54 ? 49  LYS C NZ  1 
ATOM   3299 N  N   . GLY C 1 62  ? -9.535  20.195  3.465   1.00 11.59 ? 50  GLY C N   1 
ATOM   3300 C  CA  . GLY C 1 62  ? -10.292 20.956  2.470   1.00 12.30 ? 50  GLY C CA  1 
ATOM   3301 C  C   . GLY C 1 62  ? -9.991  20.545  1.037   1.00 11.96 ? 50  GLY C C   1 
ATOM   3302 O  O   . GLY C 1 62  ? -10.130 19.346  0.685   1.00 13.73 ? 50  GLY C O   1 
ATOM   3303 N  N   . TRP C 1 63  ? -9.726  21.554  0.224   1.00 12.55 ? 51  TRP C N   1 
ATOM   3304 C  CA  . TRP C 1 63  ? -9.785  21.421  -1.243  1.00 13.28 ? 51  TRP C CA  1 
ATOM   3305 C  C   . TRP C 1 63  ? -8.514  21.957  -1.861  1.00 11.54 ? 51  TRP C C   1 
ATOM   3306 O  O   . TRP C 1 63  ? -7.959  22.891  -1.357  1.00 11.75 ? 51  TRP C O   1 
ATOM   3307 C  CB  . TRP C 1 63  ? -11.021 22.149  -1.751  1.00 14.83 ? 51  TRP C CB  1 
ATOM   3308 C  CG  . TRP C 1 63  ? -12.268 21.701  -1.063  1.00 16.92 ? 51  TRP C CG  1 
ATOM   3309 C  CD1 . TRP C 1 63  ? -13.101 20.685  -1.431  1.00 19.72 ? 51  TRP C CD1 1 
ATOM   3310 C  CD2 . TRP C 1 63  ? -12.768 22.211  0.181   1.00 18.07 ? 51  TRP C CD2 1 
ATOM   3311 N  NE1 . TRP C 1 63  ? -14.103 20.550  -0.505  1.00 22.20 ? 51  TRP C NE1 1 
ATOM   3312 C  CE2 . TRP C 1 63  ? -13.901 21.444  0.511   1.00 20.56 ? 51  TRP C CE2 1 
ATOM   3313 C  CE3 . TRP C 1 63  ? -12.322 23.183  1.078   1.00 16.72 ? 51  TRP C CE3 1 
ATOM   3314 C  CZ2 . TRP C 1 63  ? -14.648 21.711  1.660   1.00 21.37 ? 51  TRP C CZ2 1 
ATOM   3315 C  CZ3 . TRP C 1 63  ? -13.042 23.409  2.227   1.00 19.15 ? 51  TRP C CZ3 1 
ATOM   3316 C  CH2 . TRP C 1 63  ? -14.182 22.679  2.509   1.00 19.51 ? 51  TRP C CH2 1 
ATOM   3317 N  N   . ASN C 1 64  ? -8.091  21.378  -2.956  1.00 12.19 ? 52  ASN C N   1 
ATOM   3318 C  CA  . ASN C 1 64  ? -7.028  22.008  -3.761  1.00 12.81 ? 52  ASN C CA  1 
ATOM   3319 C  C   . ASN C 1 64  ? -7.330  21.742  -5.227  1.00 14.36 ? 52  ASN C C   1 
ATOM   3320 O  O   . ASN C 1 64  ? -7.430  20.583  -5.604  1.00 14.57 ? 52  ASN C O   1 
ATOM   3321 C  CB  . ASN C 1 64  ? -5.655  21.537  -3.342  1.00 13.66 ? 52  ASN C CB  1 
ATOM   3322 C  CG  . ASN C 1 64  ? -4.543  22.380  -3.931  1.00 14.84 ? 52  ASN C CG  1 
ATOM   3323 O  OD1 . ASN C 1 64  ? -4.770  23.510  -4.352  1.00 14.62 ? 52  ASN C OD1 1 
ATOM   3324 N  ND2 . ASN C 1 64  ? -3.324  21.868  -3.858  1.00 15.88 ? 52  ASN C ND2 1 
ATOM   3325 N  N   . PRO C 1 65  ? -7.509  22.777  -6.067  1.00 15.63 ? 53  PRO C N   1 
ATOM   3326 C  CA  . PRO C 1 65  ? -7.520  24.168  -5.620  1.00 16.86 ? 53  PRO C CA  1 
ATOM   3327 C  C   . PRO C 1 65  ? -8.841  24.542  -4.927  1.00 17.01 ? 53  PRO C C   1 
ATOM   3328 O  O   . PRO C 1 65  ? -9.849  23.917  -5.161  1.00 17.69 ? 53  PRO C O   1 
ATOM   3329 C  CB  . PRO C 1 65  ? -7.364  24.940  -6.935  1.00 17.16 ? 53  PRO C CB  1 
ATOM   3330 C  CG  . PRO C 1 65  ? -8.124  24.082  -7.928  1.00 18.84 ? 53  PRO C CG  1 
ATOM   3331 C  CD  . PRO C 1 65  ? -7.799  22.657  -7.517  1.00 19.68 ? 53  PRO C CD  1 
ATOM   3332 N  N   . GLY C 1 66  ? -8.816  25.570  -4.092  1.00 17.76 ? 54  GLY C N   1 
ATOM   3333 C  CA  . GLY C 1 66  ? -10.051 26.240  -3.675  1.00 19.17 ? 54  GLY C CA  1 
ATOM   3334 C  C   . GLY C 1 66  ? -10.688 26.830  -4.921  1.00 19.24 ? 54  GLY C C   1 
ATOM   3335 O  O   . GLY C 1 66  ? -9.979  27.214  -5.855  1.00 23.51 ? 54  GLY C O   1 
ATOM   3336 N  N   . SER C 1 67  ? -11.994 26.801  -4.974  1.00 22.18 ? 55  SER C N   1 
ATOM   3337 C  CA  . SER C 1 67  ? -12.778 27.323  -6.107  1.00 25.48 ? 55  SER C CA  1 
ATOM   3338 C  C   . SER C 1 67  ? -13.840 28.264  -5.547  1.00 27.53 ? 55  SER C C   1 
ATOM   3339 O  O   . SER C 1 67  ? -14.938 28.329  -6.124  1.00 28.60 ? 55  SER C O   1 
ATOM   3340 C  CB  . SER C 1 67  ? -13.347 26.155  -6.876  1.00 28.01 ? 55  SER C CB  1 
ATOM   3341 O  OG  . SER C 1 67  ? -12.289 25.274  -7.232  1.00 37.71 ? 55  SER C OG  1 
ATOM   3342 N  N   . SER C 1 68  ? -13.539 28.937  -4.437  1.00 23.90 ? 56  SER C N   1 
ATOM   3343 C  CA  . SER C 1 68  ? -14.440 29.957  -3.839  1.00 26.64 ? 56  SER C CA  1 
ATOM   3344 C  C   . SER C 1 68  ? -15.800 29.310  -3.555  1.00 25.70 ? 56  SER C C   1 
ATOM   3345 O  O   . SER C 1 68  ? -16.848 30.011  -3.656  1.00 29.25 ? 56  SER C O   1 
ATOM   3346 C  CB  . SER C 1 68  ? -14.569 31.170  -4.749  1.00 26.23 ? 56  SER C CB  1 
ATOM   3347 O  OG  . SER C 1 68  ? -13.292 31.563  -5.245  1.00 26.74 ? 56  SER C OG  1 
ATOM   3348 N  N   . GLN C 1 69  ? -15.804 28.031  -3.157  1.00 27.26 ? 57  GLN C N   1 
ATOM   3349 C  CA  . GLN C 1 69  ? -17.084 27.305  -2.984  1.00 28.64 ? 57  GLN C CA  1 
ATOM   3350 C  C   . GLN C 1 69  ? -17.658 27.692  -1.624  1.00 24.01 ? 57  GLN C C   1 
ATOM   3351 O  O   . GLN C 1 69  ? -16.910 28.206  -0.755  1.00 23.62 ? 57  GLN C O   1 
ATOM   3352 C  CB  . GLN C 1 69  ? -16.939 25.786  -3.160  1.00 33.04 ? 57  GLN C CB  1 
ATOM   3353 C  CG  . GLN C 1 69  ? -16.001 25.127  -2.159  1.00 34.67 ? 57  GLN C CG  1 
ATOM   3354 C  CD  . GLN C 1 69  ? -14.753 24.595  -2.817  1.00 40.95 ? 57  GLN C CD  1 
ATOM   3355 O  OE1 . GLN C 1 69  ? -14.755 23.503  -3.389  1.00 48.66 ? 57  GLN C OE1 1 
ATOM   3356 N  NE2 . GLN C 1 69  ? -13.680 25.371  -2.754  1.00 42.28 ? 57  GLN C NE2 1 
ATOM   3357 N  N   . THR C 1 70  ? -18.962 27.512  -1.466  1.00 22.96 ? 58  THR C N   1 
ATOM   3358 C  CA  . THR C 1 70  ? -19.693 27.592  -0.183  1.00 21.60 ? 58  THR C CA  1 
ATOM   3359 C  C   . THR C 1 70  ? -19.377 26.321  0.606   1.00 21.49 ? 58  THR C C   1 
ATOM   3360 O  O   . THR C 1 70  ? -19.668 25.220  0.065   1.00 24.55 ? 58  THR C O   1 
ATOM   3361 C  CB  . THR C 1 70  ? -21.196 27.788  -0.454  1.00 20.76 ? 58  THR C CB  1 
ATOM   3362 O  OG1 . THR C 1 70  ? -21.274 28.971  -1.246  1.00 22.47 ? 58  THR C OG1 1 
ATOM   3363 C  CG2 . THR C 1 70  ? -22.021 27.938  0.801   1.00 23.79 ? 58  THR C CG2 1 
ATOM   3364 N  N   . ILE C 1 71  ? -18.750 26.488  1.775   1.00 20.48 ? 59  ILE C N   1 
ATOM   3365 C  CA  . ILE C 1 71  ? -18.196 25.436  2.671   1.00 22.34 ? 59  ILE C CA  1 
ATOM   3366 C  C   . ILE C 1 71  ? -19.209 25.182  3.793   1.00 19.52 ? 59  ILE C C   1 
ATOM   3367 O  O   . ILE C 1 71  ? -19.709 26.152  4.339   1.00 20.99 ? 59  ILE C O   1 
ATOM   3368 C  CB  . ILE C 1 71  ? -16.863 25.996  3.244   1.00 24.75 ? 59  ILE C CB  1 
ATOM   3369 C  CG1 . ILE C 1 71  ? -15.682 25.762  2.310   1.00 31.86 ? 59  ILE C CG1 1 
ATOM   3370 C  CG2 . ILE C 1 71  ? -16.588 25.496  4.638   1.00 26.41 ? 59  ILE C CG2 1 
ATOM   3371 C  CD1 . ILE C 1 71  ? -16.037 25.213  0.959   1.00 29.13 ? 59  ILE C CD1 1 
ATOM   3372 N  N   . THR C 1 72  ? -19.432 23.933  4.191   1.00 17.55 ? 60  THR C N   1 
ATOM   3373 C  CA  . THR C 1 72  ? -20.136 23.618  5.462   1.00 20.16 ? 60  THR C CA  1 
ATOM   3374 C  C   . THR C 1 72  ? -19.201 22.756  6.308   1.00 18.01 ? 60  THR C C   1 
ATOM   3375 O  O   . THR C 1 72  ? -18.474 21.898  5.764   1.00 18.66 ? 60  THR C O   1 
ATOM   3376 C  CB  . THR C 1 72  ? -21.515 23.008  5.194   1.00 22.45 ? 60  THR C CB  1 
ATOM   3377 O  OG1 . THR C 1 72  ? -22.168 23.888  4.281   1.00 24.98 ? 60  THR C OG1 1 
ATOM   3378 C  CG2 . THR C 1 72  ? -22.361 22.849  6.443   1.00 22.71 ? 60  THR C CG2 1 
ATOM   3379 N  N   . TYR C 1 73  ? -19.080 23.070  7.581   1.00 16.99 ? 61  TYR C N   1 
ATOM   3380 C  CA  . TYR C 1 73  ? -18.268 22.242  8.497   1.00 18.06 ? 61  TYR C CA  1 
ATOM   3381 C  C   . TYR C 1 73  ? -18.990 22.200  9.832   1.00 17.15 ? 61  TYR C C   1 
ATOM   3382 O  O   . TYR C 1 73  ? -19.911 22.995  10.071  1.00 17.42 ? 61  TYR C O   1 
ATOM   3383 C  CB  . TYR C 1 73  ? -16.840 22.793  8.607   1.00 17.35 ? 61  TYR C CB  1 
ATOM   3384 C  CG  . TYR C 1 73  ? -16.809 24.062  9.409   1.00 17.33 ? 61  TYR C CG  1 
ATOM   3385 C  CD1 . TYR C 1 73  ? -17.244 25.270  8.884   1.00 19.69 ? 61  TYR C CD1 1 
ATOM   3386 C  CD2 . TYR C 1 73  ? -16.504 24.013  10.754  1.00 19.88 ? 61  TYR C CD2 1 
ATOM   3387 C  CE1 . TYR C 1 73  ? -17.335 26.411  9.662   1.00 20.08 ? 61  TYR C CE1 1 
ATOM   3388 C  CE2 . TYR C 1 73  ? -16.536 25.155  11.530  1.00 21.65 ? 61  TYR C CE2 1 
ATOM   3389 C  CZ  . TYR C 1 73  ? -16.978 26.347  10.998  1.00 22.85 ? 61  TYR C CZ  1 
ATOM   3390 O  OH  . TYR C 1 73  ? -17.061 27.439  11.816  1.00 28.56 ? 61  TYR C OH  1 
ATOM   3391 N  N   . SER C 1 74  ? -18.570 21.277  10.674  1.00 18.27 ? 62  SER C N   1 
ATOM   3392 C  CA  . SER C 1 74  ? -19.089 21.145  12.048  1.00 19.48 ? 62  SER C CA  1 
ATOM   3393 C  C   . SER C 1 74  ? -17.987 20.575  12.915  1.00 19.13 ? 62  SER C C   1 
ATOM   3394 O  O   . SER C 1 74  ? -16.930 20.137  12.375  1.00 18.52 ? 62  SER C O   1 
ATOM   3395 C  CB  . SER C 1 74  ? -20.328 20.302  12.095  1.00 22.67 ? 62  SER C CB  1 
ATOM   3396 O  OG  . SER C 1 74  ? -20.025 18.971  11.743  1.00 26.42 ? 62  SER C OG  1 
ATOM   3397 N  N   . GLY C 1 75  ? -18.202 20.567  14.219  1.00 18.21 ? 63  GLY C N   1 
ATOM   3398 C  CA  . GLY C 1 75  ? -17.283 19.862  15.123  1.00 20.73 ? 63  GLY C CA  1 
ATOM   3399 C  C   . GLY C 1 75  ? -17.187 20.571  16.447  1.00 18.34 ? 63  GLY C C   1 
ATOM   3400 O  O   . GLY C 1 75  ? -18.107 21.348  16.772  1.00 19.46 ? 63  GLY C O   1 
ATOM   3401 N  N   . GLU C 1 76  ? -16.078 20.341  17.124  1.00 17.64 ? 64  GLU C N   1 
ATOM   3402 C  CA  . GLU C 1 76  ? -15.813 20.745  18.519  1.00 20.19 ? 64  GLU C CA  1 
ATOM   3403 C  C   . GLU C 1 76  ? -14.445 21.410  18.548  1.00 20.60 ? 64  GLU C C   1 
ATOM   3404 O  O   . GLU C 1 76  ? -13.506 20.928  17.889  1.00 16.86 ? 64  GLU C O   1 
ATOM   3405 C  CB  . GLU C 1 76  ? -15.856 19.521  19.434  1.00 25.86 ? 64  GLU C CB  1 
ATOM   3406 C  CG  . GLU C 1 76  ? -17.257 19.000  19.716  1.00 32.44 ? 64  GLU C CG  1 
ATOM   3407 C  CD  . GLU C 1 76  ? -17.224 17.977  20.843  1.00 38.45 ? 64  GLU C CD  1 
ATOM   3408 O  OE1 . GLU C 1 76  ? -18.256 17.797  21.548  1.00 44.63 ? 64  GLU C OE1 1 
ATOM   3409 O  OE2 . GLU C 1 76  ? -16.146 17.361  21.013  1.00 45.06 ? 64  GLU C OE2 1 
ATOM   3410 N  N   . TRP C 1 77  ? -14.352 22.541  19.242  1.00 18.67 ? 65  TRP C N   1 
ATOM   3411 C  CA  . TRP C 1 77  ? -13.089 23.304  19.296  1.00 19.93 ? 65  TRP C CA  1 
ATOM   3412 C  C   . TRP C 1 77  ? -12.936 23.790  20.732  1.00 20.51 ? 65  TRP C C   1 
ATOM   3413 O  O   . TRP C 1 77  ? -13.757 24.651  21.132  1.00 20.77 ? 65  TRP C O   1 
ATOM   3414 C  CB  . TRP C 1 77  ? -13.125 24.425  18.262  1.00 20.49 ? 65  TRP C CB  1 
ATOM   3415 C  CG  . TRP C 1 77  ? -12.037 25.446  18.416  1.00 20.40 ? 65  TRP C CG  1 
ATOM   3416 C  CD1 . TRP C 1 77  ? -10.730 25.308  18.033  1.00 20.05 ? 65  TRP C CD1 1 
ATOM   3417 C  CD2 . TRP C 1 77  ? -12.176 26.788  18.922  1.00 18.96 ? 65  TRP C CD2 1 
ATOM   3418 N  NE1 . TRP C 1 77  ? -10.053 26.482  18.261  1.00 22.15 ? 65  TRP C NE1 1 
ATOM   3419 C  CE2 . TRP C 1 77  ? -10.899 27.387  18.847  1.00 20.70 ? 65  TRP C CE2 1 
ATOM   3420 C  CE3 . TRP C 1 77  ? -13.231 27.533  19.460  1.00 18.59 ? 65  TRP C CE3 1 
ATOM   3421 C  CZ2 . TRP C 1 77  ? -10.669 28.707  19.241  1.00 18.09 ? 65  TRP C CZ2 1 
ATOM   3422 C  CZ3 . TRP C 1 77  ? -13.000 28.834  19.857  1.00 19.26 ? 65  TRP C CZ3 1 
ATOM   3423 C  CH2 . TRP C 1 77  ? -11.723 29.400  19.784  1.00 17.76 ? 65  TRP C CH2 1 
ATOM   3424 N  N   . ASN C 1 78  ? -11.963 23.210  21.455  1.00 18.04 ? 66  ASN C N   1 
ATOM   3425 C  CA  . ASN C 1 78  ? -11.800 23.306  22.920  1.00 19.81 ? 66  ASN C CA  1 
ATOM   3426 C  C   . ASN C 1 78  ? -10.393 23.784  23.224  1.00 17.54 ? 66  ASN C C   1 
ATOM   3427 O  O   . ASN C 1 78  ? -9.551  23.008  23.663  1.00 16.69 ? 66  ASN C O   1 
ATOM   3428 C  CB  . ASN C 1 78  ? -12.051 21.968  23.600  1.00 22.63 ? 66  ASN C CB  1 
ATOM   3429 C  CG  . ASN C 1 78  ? -13.470 21.511  23.374  1.00 26.64 ? 66  ASN C CG  1 
ATOM   3430 O  OD1 . ASN C 1 78  ? -14.404 22.220  23.729  1.00 29.93 ? 66  ASN C OD1 1 
ATOM   3431 N  ND2 . ASN C 1 78  ? -13.620 20.336  22.791  1.00 28.86 ? 66  ASN C ND2 1 
ATOM   3432 N  N   . PRO C 1 79  ? -10.113 25.088  23.030  1.00 18.40 ? 67  PRO C N   1 
ATOM   3433 C  CA  . PRO C 1 79  ? -8.793  25.636  23.338  1.00 19.31 ? 67  PRO C CA  1 
ATOM   3434 C  C   . PRO C 1 79  ? -8.637  25.959  24.824  1.00 21.90 ? 67  PRO C C   1 
ATOM   3435 O  O   . PRO C 1 79  ? -9.636  26.273  25.463  1.00 20.65 ? 67  PRO C O   1 
ATOM   3436 C  CB  . PRO C 1 79  ? -8.747  26.963  22.564  1.00 19.03 ? 67  PRO C CB  1 
ATOM   3437 C  CG  . PRO C 1 79  ? -10.188 27.382  22.497  1.00 20.45 ? 67  PRO C CG  1 
ATOM   3438 C  CD  . PRO C 1 79  ? -11.024 26.106  22.495  1.00 20.08 ? 67  PRO C CD  1 
ATOM   3439 N  N   . ASN C 1 80  ? -7.392  25.887  25.294  1.00 20.19 ? 68  ASN C N   1 
ATOM   3440 C  CA  . ASN C 1 80  ? -6.939  26.523  26.564  1.00 22.50 ? 68  ASN C CA  1 
ATOM   3441 C  C   . ASN C 1 80  ? -5.820  27.502  26.213  1.00 20.20 ? 68  ASN C C   1 
ATOM   3442 O  O   . ASN C 1 80  ? -4.635  27.105  26.233  1.00 20.68 ? 68  ASN C O   1 
ATOM   3443 C  CB  . ASN C 1 80  ? -6.502  25.494  27.603  1.00 26.44 ? 68  ASN C CB  1 
ATOM   3444 C  CG  . ASN C 1 80  ? -6.072  26.169  28.892  1.00 31.07 ? 68  ASN C CG  1 
ATOM   3445 O  OD1 . ASN C 1 80  ? -6.565  27.249  29.225  1.00 35.15 ? 68  ASN C OD1 1 
ATOM   3446 N  ND2 . ASN C 1 80  ? -5.134  25.567  29.596  1.00 34.99 ? 68  ASN C ND2 1 
ATOM   3447 N  N   . GLY C 1 81  ? -6.183  28.705  25.771  1.00 20.16 ? 69  GLY C N   1 
ATOM   3448 C  CA  . GLY C 1 81  ? -5.214  29.714  25.330  1.00 19.25 ? 69  GLY C CA  1 
ATOM   3449 C  C   . GLY C 1 81  ? -5.385  30.045  23.856  1.00 18.29 ? 69  GLY C C   1 
ATOM   3450 O  O   . GLY C 1 81  ? -6.423  29.696  23.256  1.00 18.88 ? 69  GLY C O   1 
ATOM   3451 N  N   . ASN C 1 82  ? -4.345  30.640  23.270  1.00 17.80 ? 70  ASN C N   1 
ATOM   3452 C  CA  . ASN C 1 82  ? -4.397  31.305  21.958  1.00 17.69 ? 70  ASN C CA  1 
ATOM   3453 C  C   . ASN C 1 82  ? -4.652  30.251  20.857  1.00 17.15 ? 70  ASN C C   1 
ATOM   3454 O  O   . ASN C 1 82  ? -3.799  29.338  20.666  1.00 16.76 ? 70  ASN C O   1 
ATOM   3455 C  CB  . ASN C 1 82  ? -3.068  32.013  21.734  1.00 19.81 ? 70  ASN C CB  1 
ATOM   3456 C  CG  . ASN C 1 82  ? -2.994  32.689  20.395  1.00 23.00 ? 70  ASN C CG  1 
ATOM   3457 O  OD1 . ASN C 1 82  ? -3.968  32.684  19.644  1.00 24.02 ? 70  ASN C OD1 1 
ATOM   3458 N  ND2 . ASN C 1 82  ? -1.864  33.326  20.137  1.00 24.20 ? 70  ASN C ND2 1 
ATOM   3459 N  N   . SER C 1 83  ? -5.801  30.341  20.199  1.00 15.68 ? 71  SER C N   1 
ATOM   3460 C  CA  . SER C 1 83  ? -6.190  29.383  19.136  1.00 15.71 ? 71  SER C CA  1 
ATOM   3461 C  C   . SER C 1 83  ? -7.244  30.075  18.282  1.00 14.73 ? 71  SER C C   1 
ATOM   3462 O  O   . SER C 1 83  ? -7.971  30.939  18.789  1.00 13.53 ? 71  SER C O   1 
ATOM   3463 C  CB  . SER C 1 83  ? -6.727  28.114  19.736  1.00 15.58 ? 71  SER C CB  1 
ATOM   3464 O  OG  . SER C 1 83  ? -7.176  27.203  18.760  1.00 16.24 ? 71  SER C OG  1 
ATOM   3465 N  N   . TYR C 1 84  ? -7.369  29.708  17.026  1.00 14.06 ? 72  TYR C N   1 
ATOM   3466 C  CA  . TYR C 1 84  ? -8.544  30.166  16.256  1.00 14.69 ? 72  TYR C CA  1 
ATOM   3467 C  C   . TYR C 1 84  ? -8.944  29.100  15.245  1.00 13.36 ? 72  TYR C C   1 
ATOM   3468 O  O   . TYR C 1 84  ? -8.120  28.235  14.886  1.00 12.88 ? 72  TYR C O   1 
ATOM   3469 C  CB  . TYR C 1 84  ? -8.293  31.531  15.606  1.00 15.70 ? 72  TYR C CB  1 
ATOM   3470 C  CG  . TYR C 1 84  ? -7.003  31.656  14.852  1.00 19.28 ? 72  TYR C CG  1 
ATOM   3471 C  CD1 . TYR C 1 84  ? -6.972  31.280  13.528  1.00 22.60 ? 72  TYR C CD1 1 
ATOM   3472 C  CD2 . TYR C 1 84  ? -5.831  32.113  15.445  1.00 23.03 ? 72  TYR C CD2 1 
ATOM   3473 C  CE1 . TYR C 1 84  ? -5.810  31.381  12.779  1.00 27.41 ? 72  TYR C CE1 1 
ATOM   3474 C  CE2 . TYR C 1 84  ? -4.654  32.223  14.702  1.00 25.75 ? 72  TYR C CE2 1 
ATOM   3475 C  CZ  . TYR C 1 84  ? -4.656  31.881  13.361  1.00 27.79 ? 72  TYR C CZ  1 
ATOM   3476 O  OH  . TYR C 1 84  ? -3.533  31.888  12.567  1.00 32.37 ? 72  TYR C OH  1 
ATOM   3477 N  N   . LEU C 1 85  ? -10.188 29.197  14.791  1.00 12.65 ? 73  LEU C N   1 
ATOM   3478 C  CA  . LEU C 1 85  ? -10.811 28.272  13.834  1.00 13.06 ? 73  LEU C CA  1 
ATOM   3479 C  C   . LEU C 1 85  ? -11.188 29.130  12.622  1.00 14.68 ? 73  LEU C C   1 
ATOM   3480 O  O   . LEU C 1 85  ? -11.866 30.151  12.796  1.00 12.44 ? 73  LEU C O   1 
ATOM   3481 C  CB  . LEU C 1 85  ? -12.057 27.611  14.456  1.00 15.81 ? 73  LEU C CB  1 
ATOM   3482 C  CG  . LEU C 1 85  ? -12.741 26.585  13.568  1.00 17.83 ? 73  LEU C CG  1 
ATOM   3483 C  CD1 . LEU C 1 85  ? -11.854 25.388  13.331  1.00 20.37 ? 73  LEU C CD1 1 
ATOM   3484 C  CD2 . LEU C 1 85  ? -14.065 26.111  14.165  1.00 22.25 ? 73  LEU C CD2 1 
ATOM   3485 N  N   . SER C 1 86  ? -10.654 28.793  11.443  1.00 14.19 ? 74  SER C N   1 
ATOM   3486 C  CA  . SER C 1 86  ? -10.768 29.690  10.280  1.00 14.22 ? 74  SER C CA  1 
ATOM   3487 C  C   . SER C 1 86  ? -10.865 28.882  8.997   1.00 15.77 ? 74  SER C C   1 
ATOM   3488 O  O   . SER C 1 86  ? -10.341 27.758  8.959   1.00 17.14 ? 74  SER C O   1 
ATOM   3489 C  CB  . SER C 1 86  ? -9.552  30.592  10.222  1.00 17.50 ? 74  SER C CB  1 
ATOM   3490 O  OG  . SER C 1 86  ? -8.422  29.831  9.802   1.00 25.65 ? 74  SER C OG  1 
ATOM   3491 N  N   . VAL C 1 87  ? -11.478 29.444  7.964   1.00 13.58 ? 75  VAL C N   1 
ATOM   3492 C  CA  . VAL C 1 87  ? -11.194 28.988  6.579   1.00 13.01 ? 75  VAL C CA  1 
ATOM   3493 C  C   . VAL C 1 87  ? -9.885  29.663  6.187   1.00 13.52 ? 75  VAL C C   1 
ATOM   3494 O  O   . VAL C 1 87  ? -9.757  30.886  6.385   1.00 17.50 ? 75  VAL C O   1 
ATOM   3495 C  CB  . VAL C 1 87  ? -12.322 29.354  5.612   1.00 13.22 ? 75  VAL C CB  1 
ATOM   3496 C  CG1 . VAL C 1 87  ? -11.972 28.894  4.207   1.00 14.50 ? 75  VAL C CG1 1 
ATOM   3497 C  CG2 . VAL C 1 87  ? -13.648 28.792  6.047   1.00 13.68 ? 75  VAL C CG2 1 
ATOM   3498 N  N   . TYR C 1 88  ? -8.914  28.898  5.726   1.00 11.91 ? 76  TYR C N   1 
ATOM   3499 C  CA  . TYR C 1 88  ? -7.526  29.353  5.591   1.00 11.68 ? 76  TYR C CA  1 
ATOM   3500 C  C   . TYR C 1 88  ? -7.040  28.925  4.211   1.00 12.21 ? 76  TYR C C   1 
ATOM   3501 O  O   . TYR C 1 88  ? -7.290  27.788  3.844   1.00 11.74 ? 76  TYR C O   1 
ATOM   3502 C  CB  . TYR C 1 88  ? -6.688  28.706  6.677   1.00 14.00 ? 76  TYR C CB  1 
ATOM   3503 C  CG  . TYR C 1 88  ? -5.209  28.823  6.473   1.00 16.12 ? 76  TYR C CG  1 
ATOM   3504 C  CD1 . TYR C 1 88  ? -4.577  30.054  6.607   1.00 15.99 ? 76  TYR C CD1 1 
ATOM   3505 C  CD2 . TYR C 1 88  ? -4.456  27.741  6.041   1.00 15.69 ? 76  TYR C CD2 1 
ATOM   3506 C  CE1 . TYR C 1 88  ? -3.209  30.171  6.442   1.00 15.75 ? 76  TYR C CE1 1 
ATOM   3507 C  CE2 . TYR C 1 88  ? -3.074  27.855  5.886   1.00 16.12 ? 76  TYR C CE2 1 
ATOM   3508 C  CZ  . TYR C 1 88  ? -2.463  29.080  6.040   1.00 16.32 ? 76  TYR C CZ  1 
ATOM   3509 O  OH  . TYR C 1 88  ? -1.108  29.224  5.893   1.00 18.27 ? 76  TYR C OH  1 
ATOM   3510 N  N   . GLY C 1 89  ? -6.422  29.822  3.452   1.00 11.44 ? 77  GLY C N   1 
ATOM   3511 C  CA  . GLY C 1 89  ? -5.941  29.359  2.136   1.00 11.29 ? 77  GLY C CA  1 
ATOM   3512 C  C   . GLY C 1 89  ? -4.957  30.309  1.518   1.00 11.19 ? 77  GLY C C   1 
ATOM   3513 O  O   . GLY C 1 89  ? -4.624  31.333  2.163   1.00 11.78 ? 77  GLY C O   1 
ATOM   3514 N  N   . TRP C 1 90  ? -4.543  29.978  0.292   1.00 12.41 ? 78  TRP C N   1 
ATOM   3515 C  CA  . TRP C 1 90  ? -3.500  30.738  -0.441  1.00 13.41 ? 78  TRP C CA  1 
ATOM   3516 C  C   . TRP C 1 90  ? -3.951  31.117  -1.845  1.00 12.63 ? 78  TRP C C   1 
ATOM   3517 O  O   . TRP C 1 90  ? -4.638  30.282  -2.471  1.00 12.49 ? 78  TRP C O   1 
ATOM   3518 C  CB  . TRP C 1 90  ? -2.213  29.927  -0.519  1.00 13.66 ? 78  TRP C CB  1 
ATOM   3519 C  CG  . TRP C 1 90  ? -1.501  29.796  0.783   1.00 14.69 ? 78  TRP C CG  1 
ATOM   3520 C  CD1 . TRP C 1 90  ? -1.740  28.855  1.738   1.00 14.55 ? 78  TRP C CD1 1 
ATOM   3521 C  CD2 . TRP C 1 90  ? -0.456  30.629  1.294   1.00 16.50 ? 78  TRP C CD2 1 
ATOM   3522 N  NE1 . TRP C 1 90  ? -0.911  29.036  2.800   1.00 17.08 ? 78  TRP C NE1 1 
ATOM   3523 C  CE2 . TRP C 1 90  ? -0.126  30.125  2.578   1.00 16.82 ? 78  TRP C CE2 1 
ATOM   3524 C  CE3 . TRP C 1 90  ? 0.226   31.752  0.813   1.00 16.69 ? 78  TRP C CE3 1 
ATOM   3525 C  CZ2 . TRP C 1 90  ? 0.852   30.708  3.383   1.00 16.58 ? 78  TRP C CZ2 1 
ATOM   3526 C  CZ3 . TRP C 1 90  ? 1.213   32.309  1.603   1.00 16.83 ? 78  TRP C CZ3 1 
ATOM   3527 C  CH2 . TRP C 1 90  ? 1.534   31.777  2.851   1.00 17.72 ? 78  TRP C CH2 1 
ATOM   3528 N  N   . THR C 1 91  ? -3.493  32.284  -2.328  1.00 13.12 ? 79  THR C N   1 
ATOM   3529 C  CA  . THR C 1 91  ? -3.388  32.506  -3.793  1.00 13.26 ? 79  THR C CA  1 
ATOM   3530 C  C   . THR C 1 91  ? -1.931  32.690  -4.178  1.00 15.26 ? 79  THR C C   1 
ATOM   3531 O  O   . THR C 1 91  ? -1.112  32.977  -3.303  1.00 13.68 ? 79  THR C O   1 
ATOM   3532 C  CB  . THR C 1 91  ? -4.241  33.669  -4.304  1.00 16.08 ? 79  THR C CB  1 
ATOM   3533 O  OG1 . THR C 1 91  ? -3.677  34.950  -3.977  1.00 17.01 ? 79  THR C OG1 1 
ATOM   3534 C  CG2 . THR C 1 91  ? -5.657  33.612  -3.774  1.00 14.08 ? 79  THR C CG2 1 
ATOM   3535 N  N   . GLN C 1 92  ? -1.659  32.449  -5.452  1.00 14.84 ? 80  GLN C N   1 
ATOM   3536 C  CA  . GLN C 1 92  ? -0.326  32.716  -6.051  1.00 15.55 ? 80  GLN C CA  1 
ATOM   3537 C  C   . GLN C 1 92  ? -0.458  33.764  -7.163  1.00 15.52 ? 80  GLN C C   1 
ATOM   3538 O  O   . GLN C 1 92  ? -1.486  33.895  -7.779  1.00 13.29 ? 80  GLN C O   1 
ATOM   3539 C  CB  . GLN C 1 92  ? 0.248   31.434  -6.636  1.00 20.84 ? 80  GLN C CB  1 
ATOM   3540 C  CG  . GLN C 1 92  ? 0.569   30.380  -5.584  1.00 24.14 ? 80  GLN C CG  1 
ATOM   3541 C  CD  . GLN C 1 92  ? 0.490   28.997  -6.173  1.00 27.67 ? 80  GLN C CD  1 
ATOM   3542 O  OE1 . GLN C 1 92  ? -0.569  28.563  -6.632  1.00 35.86 ? 80  GLN C OE1 1 
ATOM   3543 N  NE2 . GLN C 1 92  ? 1.605   28.282  -6.155  1.00 28.54 ? 80  GLN C NE2 1 
ATOM   3544 N  N   . ASN C 1 93  ? 0.593   34.541  -7.321  1.00 15.29 ? 81  ASN C N   1 
ATOM   3545 C  CA  . ASN C 1 93  ? 0.690   35.512  -8.440  1.00 16.86 ? 81  ASN C CA  1 
ATOM   3546 C  C   . ASN C 1 93  ? -0.507  36.454  -8.513  1.00 16.38 ? 81  ASN C C   1 
ATOM   3547 O  O   . ASN C 1 93  ? -1.238  36.483  -9.523  1.00 18.00 ? 81  ASN C O   1 
ATOM   3548 C  CB  . ASN C 1 93  ? 0.937   34.685  -9.701  1.00 18.03 ? 81  ASN C CB  1 
ATOM   3549 C  CG  . ASN C 1 93  ? 1.279   35.569  -10.886 1.00 19.97 ? 81  ASN C CG  1 
ATOM   3550 O  OD1 . ASN C 1 93  ? 0.967   35.224  -12.039 1.00 25.31 ? 81  ASN C OD1 1 
ATOM   3551 N  ND2 . ASN C 1 93  ? 1.753   36.764  -10.602 1.00 16.20 ? 81  ASN C ND2 1 
ATOM   3552 N  N   . PRO C 1 94  ? -0.755  37.339  -7.509  1.00 16.94 ? 82  PRO C N   1 
ATOM   3553 C  CA  . PRO C 1 94  ? 0.090   37.450  -6.315  1.00 17.74 ? 82  PRO C CA  1 
ATOM   3554 C  C   . PRO C 1 94  ? -0.117  36.432  -5.180  1.00 19.42 ? 82  PRO C C   1 
ATOM   3555 O  O   . PRO C 1 94  ? -1.210  35.894  -5.014  1.00 17.08 ? 82  PRO C O   1 
ATOM   3556 C  CB  . PRO C 1 94  ? -0.271  38.856  -5.799  1.00 17.82 ? 82  PRO C CB  1 
ATOM   3557 C  CG  . PRO C 1 94  ? -1.713  39.036  -6.196  1.00 18.34 ? 82  PRO C CG  1 
ATOM   3558 C  CD  . PRO C 1 94  ? -1.747  38.416  -7.582  1.00 18.03 ? 82  PRO C CD  1 
ATOM   3559 N  N   . LEU C 1 95  ? 0.966   36.255  -4.419  1.00 18.23 ? 83  LEU C N   1 
ATOM   3560 C  CA  . LEU C 1 95  ? 1.021   35.403  -3.219  1.00 16.84 ? 83  LEU C CA  1 
ATOM   3561 C  C   . LEU C 1 95  ? 0.226   36.085  -2.098  1.00 16.22 ? 83  LEU C C   1 
ATOM   3562 O  O   . LEU C 1 95  ? 0.554   37.213  -1.630  1.00 15.27 ? 83  LEU C O   1 
ATOM   3563 C  CB  . LEU C 1 95  ? 2.485   35.141  -2.859  1.00 18.25 ? 83  LEU C CB  1 
ATOM   3564 C  CG  . LEU C 1 95  ? 2.696   34.060  -1.813  1.00 18.83 ? 83  LEU C CG  1 
ATOM   3565 C  CD1 . LEU C 1 95  ? 2.207   32.693  -2.291  1.00 20.32 ? 83  LEU C CD1 1 
ATOM   3566 C  CD2 . LEU C 1 95  ? 4.173   33.947  -1.410  1.00 21.79 ? 83  LEU C CD2 1 
ATOM   3567 N  N   . VAL C 1 96  ? -0.846  35.431  -1.662  1.00 14.03 ? 84  VAL C N   1 
ATOM   3568 C  CA  . VAL C 1 96  ? -1.739  35.957  -0.602  1.00 13.84 ? 84  VAL C CA  1 
ATOM   3569 C  C   . VAL C 1 96  ? -2.025  34.781  0.346   1.00 13.43 ? 84  VAL C C   1 
ATOM   3570 O  O   . VAL C 1 96  ? -2.273  33.647  -0.142  1.00 14.38 ? 84  VAL C O   1 
ATOM   3571 C  CB  . VAL C 1 96  ? -3.044  36.506  -1.168  1.00 15.17 ? 84  VAL C CB  1 
ATOM   3572 C  CG1 . VAL C 1 96  ? -3.999  36.862  -0.004  1.00 14.09 ? 84  VAL C CG1 1 
ATOM   3573 C  CG2 . VAL C 1 96  ? -2.789  37.705  -2.084  1.00 15.30 ? 84  VAL C CG2 1 
ATOM   3574 N  N   . GLU C 1 97  ? -1.964  35.044  1.638   1.00 14.23 ? 85  GLU C N   1 
ATOM   3575 C  CA  . GLU C 1 97  ? -2.421  34.106  2.692   1.00 13.79 ? 85  GLU C CA  1 
ATOM   3576 C  C   . GLU C 1 97  ? -3.689  34.734  3.270   1.00 13.07 ? 85  GLU C C   1 
ATOM   3577 O  O   . GLU C 1 97  ? -3.680  35.968  3.566   1.00 12.28 ? 85  GLU C O   1 
ATOM   3578 C  CB  . GLU C 1 97  ? -1.349  33.973  3.771   1.00 15.24 ? 85  GLU C CB  1 
ATOM   3579 C  CG  . GLU C 1 97  ? -1.664  32.929  4.832   1.00 16.34 ? 85  GLU C CG  1 
ATOM   3580 C  CD  . GLU C 1 97  ? -0.605  32.854  5.935   1.00 17.40 ? 85  GLU C CD  1 
ATOM   3581 O  OE1 . GLU C 1 97  ? -0.227  31.731  6.341   1.00 19.06 ? 85  GLU C OE1 1 
ATOM   3582 O  OE2 . GLU C 1 97  ? -0.169  33.921  6.384   1.00 19.35 ? 85  GLU C OE2 1 
ATOM   3583 N  N   . TYR C 1 98  ? -4.774  33.981  3.396   1.00 13.61 ? 86  TYR C N   1 
ATOM   3584 C  CA  . TYR C 1 98  ? -6.043  34.589  3.852   1.00 13.27 ? 86  TYR C CA  1 
ATOM   3585 C  C   . TYR C 1 98  ? -6.715  33.703  4.900   1.00 14.50 ? 86  TYR C C   1 
ATOM   3586 O  O   . TYR C 1 98  ? -6.502  32.501  4.949   1.00 14.34 ? 86  TYR C O   1 
ATOM   3587 C  CB  . TYR C 1 98  ? -7.003  34.864  2.694   1.00 14.07 ? 86  TYR C CB  1 
ATOM   3588 C  CG  . TYR C 1 98  ? -7.489  33.616  1.982   1.00 13.96 ? 86  TYR C CG  1 
ATOM   3589 C  CD1 . TYR C 1 98  ? -8.535  32.865  2.493   1.00 14.49 ? 86  TYR C CD1 1 
ATOM   3590 C  CD2 . TYR C 1 98  ? -6.932  33.208  0.780   1.00 14.74 ? 86  TYR C CD2 1 
ATOM   3591 C  CE1 . TYR C 1 98  ? -9.013  31.749  1.832   1.00 14.23 ? 86  TYR C CE1 1 
ATOM   3592 C  CE2 . TYR C 1 98  ? -7.393  32.080  0.126   1.00 15.74 ? 86  TYR C CE2 1 
ATOM   3593 C  CZ  . TYR C 1 98  ? -8.428  31.341  0.659   1.00 14.77 ? 86  TYR C CZ  1 
ATOM   3594 O  OH  . TYR C 1 98  ? -8.894  30.218  0.041   1.00 18.42 ? 86  TYR C OH  1 
ATOM   3595 N  N   . TYR C 1 99  ? -7.513  34.355  5.748   1.00 15.23 ? 87  TYR C N   1 
ATOM   3596 C  CA  . TYR C 1 99  ? -8.130  33.749  6.955   1.00 14.08 ? 87  TYR C CA  1 
ATOM   3597 C  C   . TYR C 1 99  ? -9.549  34.277  7.037   1.00 14.85 ? 87  TYR C C   1 
ATOM   3598 O  O   . TYR C 1 99  ? -9.710  35.509  7.067   1.00 15.38 ? 87  TYR C O   1 
ATOM   3599 C  CB  . TYR C 1 99  ? -7.431  34.164  8.252   1.00 16.64 ? 87  TYR C CB  1 
ATOM   3600 C  CG  . TYR C 1 99  ? -6.123  33.481  8.543   1.00 18.07 ? 87  TYR C CG  1 
ATOM   3601 C  CD1 . TYR C 1 99  ? -6.087  32.281  9.222   1.00 23.97 ? 87  TYR C CD1 1 
ATOM   3602 C  CD2 . TYR C 1 99  ? -4.924  34.004  8.079   1.00 25.29 ? 87  TYR C CD2 1 
ATOM   3603 C  CE1 . TYR C 1 99  ? -4.893  31.639  9.497   1.00 30.66 ? 87  TYR C CE1 1 
ATOM   3604 C  CE2 . TYR C 1 99  ? -3.717  33.397  8.376   1.00 26.82 ? 87  TYR C CE2 1 
ATOM   3605 C  CZ  . TYR C 1 99  ? -3.709  32.199  9.067   1.00 29.39 ? 87  TYR C CZ  1 
ATOM   3606 O  OH  . TYR C 1 99  ? -2.552  31.523  9.336   1.00 40.85 ? 87  TYR C OH  1 
ATOM   3607 N  N   . ILE C 1 100 ? -10.530 33.393  7.105   1.00 13.41 ? 88  ILE C N   1 
ATOM   3608 C  CA  . ILE C 1 100 ? -11.921 33.773  7.459   1.00 13.48 ? 88  ILE C CA  1 
ATOM   3609 C  C   . ILE C 1 100 ? -12.132 33.174  8.844   1.00 12.83 ? 88  ILE C C   1 
ATOM   3610 O  O   . ILE C 1 100 ? -12.306 31.970  8.964   1.00 13.78 ? 88  ILE C O   1 
ATOM   3611 C  CB  . ILE C 1 100 ? -12.963 33.323  6.411   1.00 14.41 ? 88  ILE C CB  1 
ATOM   3612 C  CG1 . ILE C 1 100 ? -12.672 33.907  5.028   1.00 15.04 ? 88  ILE C CG1 1 
ATOM   3613 C  CG2 . ILE C 1 100 ? -14.378 33.703  6.858   1.00 14.17 ? 88  ILE C CG2 1 
ATOM   3614 C  CD1 . ILE C 1 100 ? -13.209 33.074  3.885   1.00 14.86 ? 88  ILE C CD1 1 
ATOM   3615 N  N   . VAL C 1 101 ? -11.980 34.010  9.876   1.00 13.51 ? 89  VAL C N   1 
ATOM   3616 C  CA  . VAL C 1 101 ? -11.933 33.538  11.279  1.00 12.50 ? 89  VAL C CA  1 
ATOM   3617 C  C   . VAL C 1 101 ? -13.363 33.446  11.825  1.00 14.22 ? 89  VAL C C   1 
ATOM   3618 O  O   . VAL C 1 101 ? -14.034 34.446  11.849  1.00 13.62 ? 89  VAL C O   1 
ATOM   3619 C  CB  . VAL C 1 101 ? -11.038 34.438  12.146  1.00 13.59 ? 89  VAL C CB  1 
ATOM   3620 C  CG1 . VAL C 1 101 ? -10.946 33.812  13.523  1.00 13.43 ? 89  VAL C CG1 1 
ATOM   3621 C  CG2 . VAL C 1 101 ? -9.658  34.628  11.523  1.00 13.75 ? 89  VAL C CG2 1 
ATOM   3622 N  N   . GLU C 1 102 ? -13.757 32.239  12.239  1.00 13.98 ? 90  GLU C N   1 
ATOM   3623 C  CA  . GLU C 1 102 ? -15.097 31.896  12.783  1.00 14.67 ? 90  GLU C CA  1 
ATOM   3624 C  C   . GLU C 1 102 ? -15.089 32.054  14.311  1.00 14.22 ? 90  GLU C C   1 
ATOM   3625 O  O   . GLU C 1 102 ? -16.131 32.387  14.857  1.00 12.86 ? 90  GLU C O   1 
ATOM   3626 C  CB  . GLU C 1 102 ? -15.479 30.492  12.353  1.00 17.69 ? 90  GLU C CB  1 
ATOM   3627 C  CG  . GLU C 1 102 ? -15.636 30.346  10.846  1.00 20.52 ? 90  GLU C CG  1 
ATOM   3628 C  CD  . GLU C 1 102 ? -16.885 31.040  10.349  1.00 24.84 ? 90  GLU C CD  1 
ATOM   3629 O  OE1 . GLU C 1 102 ? -16.757 32.179  9.906   1.00 24.70 ? 90  GLU C OE1 1 
ATOM   3630 O  OE2 . GLU C 1 102 ? -17.960 30.449  10.453  1.00 29.21 ? 90  GLU C OE2 1 
ATOM   3631 N  N   . SER C 1 103 ? -13.993 31.682  14.959  1.00 14.61 ? 91  SER C N   1 
ATOM   3632 C  CA  . SER C 1 103 ? -13.765 31.753  16.424  1.00 15.20 ? 91  SER C CA  1 
ATOM   3633 C  C   . SER C 1 103 ? -12.301 32.064  16.688  1.00 14.80 ? 91  SER C C   1 
ATOM   3634 O  O   . SER C 1 103 ? -11.439 31.522  16.017  1.00 14.46 ? 91  SER C O   1 
ATOM   3635 C  CB  . SER C 1 103 ? -14.112 30.454  17.089  1.00 18.58 ? 91  SER C CB  1 
ATOM   3636 O  OG  . SER C 1 103 ? -15.506 30.289  17.195  1.00 20.19 ? 91  SER C OG  1 
ATOM   3637 N  N   . PHE C 1 104 ? -12.030 32.839  17.709  1.00 14.76 ? 92  PHE C N   1 
ATOM   3638 C  CA  . PHE C 1 104 ? -10.694 32.887  18.338  1.00 14.95 ? 92  PHE C CA  1 
ATOM   3639 C  C   . PHE C 1 104 ? -10.892 32.941  19.843  1.00 15.85 ? 92  PHE C C   1 
ATOM   3640 O  O   . PHE C 1 104 ? -12.022 33.262  20.329  1.00 13.27 ? 92  PHE C O   1 
ATOM   3641 C  CB  . PHE C 1 104 ? -9.909  34.069  17.759  1.00 14.80 ? 92  PHE C CB  1 
ATOM   3642 C  CG  . PHE C 1 104 ? -10.453 35.426  18.136  1.00 15.54 ? 92  PHE C CG  1 
ATOM   3643 C  CD1 . PHE C 1 104 ? -10.208 35.961  19.396  1.00 14.55 ? 92  PHE C CD1 1 
ATOM   3644 C  CD2 . PHE C 1 104 ? -11.121 36.206  17.204  1.00 15.27 ? 92  PHE C CD2 1 
ATOM   3645 C  CE1 . PHE C 1 104 ? -10.664 37.229  19.722  1.00 16.18 ? 92  PHE C CE1 1 
ATOM   3646 C  CE2 . PHE C 1 104 ? -11.553 37.487  17.533  1.00 17.35 ? 92  PHE C CE2 1 
ATOM   3647 C  CZ  . PHE C 1 104 ? -11.340 37.979  18.803  1.00 16.55 ? 92  PHE C CZ  1 
ATOM   3648 N  N   . SER C 1 105 ? -9.824  32.652  20.578  1.00 16.89 ? 93  SER C N   1 
ATOM   3649 C  CA  . SER C 1 105 ? -9.916  32.505  22.044  1.00 21.14 ? 93  SER C CA  1 
ATOM   3650 C  C   . SER C 1 105 ? -9.427  33.795  22.731  1.00 25.20 ? 93  SER C C   1 
ATOM   3651 O  O   . SER C 1 105 ? -10.210 34.749  22.858  1.00 34.93 ? 93  SER C O   1 
ATOM   3652 C  CB  . SER C 1 105 ? -9.202  31.247  22.465  1.00 21.91 ? 93  SER C CB  1 
ATOM   3653 O  OG  . SER C 1 105 ? -9.620  30.869  23.756  1.00 25.82 ? 93  SER C OG  1 
ATOM   3654 N  N   . THR C 1 106 ? -8.179  33.819  23.138  1.00 22.77 ? 94  THR C N   1 
ATOM   3655 C  CA  . THR C 1 106 ? -7.541  34.810  24.038  1.00 21.20 ? 94  THR C CA  1 
ATOM   3656 C  C   . THR C 1 106 ? -6.786  35.893  23.268  1.00 20.73 ? 94  THR C C   1 
ATOM   3657 O  O   . THR C 1 106 ? -6.177  36.798  23.924  1.00 20.59 ? 94  THR C O   1 
ATOM   3658 C  CB  . THR C 1 106 ? -6.613  34.017  24.960  1.00 22.18 ? 94  THR C CB  1 
ATOM   3659 O  OG1 . THR C 1 106 ? -5.642  33.358  24.147  1.00 23.93 ? 94  THR C OG1 1 
ATOM   3660 C  CG2 . THR C 1 106 ? -7.411  33.015  25.749  1.00 21.10 ? 94  THR C CG2 1 
ATOM   3661 N  N   . TYR C 1 107 ? -6.678  35.766  21.948  1.00 16.92 ? 95  TYR C N   1 
ATOM   3662 C  CA  . TYR C 1 107 ? -5.882  36.721  21.148  1.00 16.74 ? 95  TYR C CA  1 
ATOM   3663 C  C   . TYR C 1 107 ? -6.571  36.927  19.812  1.00 16.17 ? 95  TYR C C   1 
ATOM   3664 O  O   . TYR C 1 107 ? -6.745  35.941  19.101  1.00 16.73 ? 95  TYR C O   1 
ATOM   3665 C  CB  . TYR C 1 107 ? -4.448  36.243  20.984  1.00 17.47 ? 95  TYR C CB  1 
ATOM   3666 C  CG  . TYR C 1 107 ? -3.567  37.219  20.259  1.00 17.35 ? 95  TYR C CG  1 
ATOM   3667 C  CD1 . TYR C 1 107 ? -3.119  38.374  20.878  1.00 18.20 ? 95  TYR C CD1 1 
ATOM   3668 C  CD2 . TYR C 1 107 ? -3.183  36.985  18.950  1.00 19.83 ? 95  TYR C CD2 1 
ATOM   3669 C  CE1 . TYR C 1 107 ? -2.285  39.277  20.224  1.00 18.87 ? 95  TYR C CE1 1 
ATOM   3670 C  CE2 . TYR C 1 107 ? -2.380  37.890  18.268  1.00 17.99 ? 95  TYR C CE2 1 
ATOM   3671 C  CZ  . TYR C 1 107 ? -1.941  39.051  18.905  1.00 19.72 ? 95  TYR C CZ  1 
ATOM   3672 O  OH  . TYR C 1 107 ? -1.123  39.948  18.274  1.00 20.85 ? 95  TYR C OH  1 
ATOM   3673 N  N   . ASP C 1 108 ? -6.949  38.150  19.495  1.00 16.74 ? 96  ASP C N   1 
ATOM   3674 C  CA  . ASP C 1 108 ? -7.536  38.456  18.162  1.00 17.50 ? 96  ASP C CA  1 
ATOM   3675 C  C   . ASP C 1 108 ? -6.390  38.363  17.157  1.00 17.27 ? 96  ASP C C   1 
ATOM   3676 O  O   . ASP C 1 108 ? -5.474  39.173  17.207  1.00 18.77 ? 96  ASP C O   1 
ATOM   3677 C  CB  . ASP C 1 108 ? -8.278  39.792  18.186  1.00 19.25 ? 96  ASP C CB  1 
ATOM   3678 C  CG  . ASP C 1 108 ? -8.952  40.144  16.866  1.00 19.70 ? 96  ASP C CG  1 
ATOM   3679 O  OD1 . ASP C 1 108 ? -8.567  39.578  15.826  1.00 19.71 ? 96  ASP C OD1 1 
ATOM   3680 O  OD2 . ASP C 1 108 ? -9.902  40.926  16.902  1.00 23.93 ? 96  ASP C OD2 1 
ATOM   3681 N  N   . PRO C 1 109 ? -6.402  37.368  16.230  1.00 16.94 ? 97  PRO C N   1 
ATOM   3682 C  CA  . PRO C 1 109 ? -5.270  37.114  15.334  1.00 17.78 ? 97  PRO C CA  1 
ATOM   3683 C  C   . PRO C 1 109 ? -5.115  38.199  14.272  1.00 17.62 ? 97  PRO C C   1 
ATOM   3684 O  O   . PRO C 1 109 ? -4.003  38.263  13.675  1.00 19.09 ? 97  PRO C O   1 
ATOM   3685 C  CB  . PRO C 1 109 ? -5.598  35.749  14.704  1.00 18.19 ? 97  PRO C CB  1 
ATOM   3686 C  CG  . PRO C 1 109 ? -7.089  35.666  14.731  1.00 18.73 ? 97  PRO C CG  1 
ATOM   3687 C  CD  . PRO C 1 109 ? -7.514  36.439  15.968  1.00 18.79 ? 97  PRO C CD  1 
ATOM   3688 N  N   . SER C 1 110 ? -6.112  39.088  14.153  1.00 18.33 ? 98  SER C N   1 
ATOM   3689 C  CA  . SER C 1 110 ? -6.074  40.298  13.280  1.00 20.14 ? 98  SER C CA  1 
ATOM   3690 C  C   . SER C 1 110 ? -5.308  41.456  13.946  1.00 20.42 ? 98  SER C C   1 
ATOM   3691 O  O   . SER C 1 110 ? -5.127  42.530  13.291  1.00 22.44 ? 98  SER C O   1 
ATOM   3692 C  CB  . SER C 1 110 ? -7.467  40.734  12.861  1.00 20.33 ? 98  SER C CB  1 
ATOM   3693 O  OG  . SER C 1 110 ? -8.173  41.350  13.953  1.00 19.05 ? 98  SER C OG  1 
ATOM   3694 N  N   . THR C 1 111 ? -4.824  41.286  15.180  1.00 17.74 ? 99  THR C N   1 
ATOM   3695 C  CA  . THR C 1 111 ? -4.125  42.359  15.925  1.00 17.55 ? 99  THR C CA  1 
ATOM   3696 C  C   . THR C 1 111 ? -2.880  42.786  15.122  1.00 18.12 ? 99  THR C C   1 
ATOM   3697 O  O   . THR C 1 111 ? -2.139  41.902  14.702  1.00 20.99 ? 99  THR C O   1 
ATOM   3698 C  CB  . THR C 1 111 ? -3.717  41.951  17.347  1.00 16.79 ? 99  THR C CB  1 
ATOM   3699 O  OG1 . THR C 1 111 ? -4.880  41.613  18.091  1.00 17.87 ? 99  THR C OG1 1 
ATOM   3700 C  CG2 . THR C 1 111 ? -3.025  43.087  18.058  1.00 19.22 ? 99  THR C CG2 1 
ATOM   3701 N  N   . GLY C 1 112 ? -2.685  44.094  14.930  1.00 20.95 ? 100 GLY C N   1 
ATOM   3702 C  CA  . GLY C 1 112 ? -1.561  44.616  14.124  1.00 21.53 ? 100 GLY C CA  1 
ATOM   3703 C  C   . GLY C 1 112 ? -1.970  44.866  12.676  1.00 23.69 ? 100 GLY C C   1 
ATOM   3704 O  O   . GLY C 1 112 ? -1.252  45.603  11.955  1.00 24.53 ? 100 GLY C O   1 
ATOM   3705 N  N   . ALA C 1 113 ? -3.114  44.343  12.234  1.00 21.05 ? 101 ALA C N   1 
ATOM   3706 C  CA  . ALA C 1 113 ? -3.540  44.491  10.826  1.00 19.79 ? 101 ALA C CA  1 
ATOM   3707 C  C   . ALA C 1 113 ? -4.434  45.725  10.657  1.00 19.98 ? 101 ALA C C   1 
ATOM   3708 O  O   . ALA C 1 113 ? -5.138  46.133  11.598  1.00 18.62 ? 101 ALA C O   1 
ATOM   3709 C  CB  . ALA C 1 113 ? -4.179  43.220  10.329  1.00 20.92 ? 101 ALA C CB  1 
ATOM   3710 N  N   . GLN C 1 114 ? -4.405  46.330  9.473   1.00 19.87 ? 102 GLN C N   1 
ATOM   3711 C  CA  . GLN C 1 114 ? -5.206  47.549  9.215   1.00 21.05 ? 102 GLN C CA  1 
ATOM   3712 C  C   . GLN C 1 114 ? -6.656  47.144  8.954   1.00 20.50 ? 102 GLN C C   1 
ATOM   3713 O  O   . GLN C 1 114 ? -6.900  46.362  8.020   1.00 19.10 ? 102 GLN C O   1 
ATOM   3714 C  CB  . GLN C 1 114 ? -4.700  48.334  8.014   1.00 23.60 ? 102 GLN C CB  1 
ATOM   3715 C  CG  . GLN C 1 114 ? -5.511  49.616  7.796   1.00 23.65 ? 102 GLN C CG  1 
ATOM   3716 C  CD  . GLN C 1 114 ? -5.084  50.381  6.565   1.00 27.82 ? 102 GLN C CD  1 
ATOM   3717 O  OE1 . GLN C 1 114 ? -4.208  49.961  5.792   1.00 30.55 ? 102 GLN C OE1 1 
ATOM   3718 N  NE2 . GLN C 1 114 ? -5.721  51.529  6.382   1.00 29.86 ? 102 GLN C NE2 1 
ATOM   3719 N  N   . GLU C 1 115 ? -7.594  47.716  9.699   1.00 18.87 ? 103 GLU C N   1 
ATOM   3720 C  CA  . GLU C 1 115 ? -9.046  47.498  9.502   1.00 21.45 ? 103 GLU C CA  1 
ATOM   3721 C  C   . GLU C 1 115 ? -9.529  48.274  8.266   1.00 22.20 ? 103 GLU C C   1 
ATOM   3722 O  O   . GLU C 1 115 ? -9.294  49.516  8.191   1.00 21.39 ? 103 GLU C O   1 
ATOM   3723 C  CB  . GLU C 1 115 ? -9.807  47.903  10.758  1.00 23.06 ? 103 GLU C CB  1 
ATOM   3724 C  CG  . GLU C 1 115 ? -11.191 47.300  10.892  1.00 25.55 ? 103 GLU C CG  1 
ATOM   3725 C  CD  . GLU C 1 115 ? -11.783 47.509  12.283  1.00 31.10 ? 103 GLU C CD  1 
ATOM   3726 O  OE1 . GLU C 1 115 ? -10.986 47.809  13.209  1.00 34.60 ? 103 GLU C OE1 1 
ATOM   3727 O  OE2 . GLU C 1 115 ? -13.021 47.352  12.455  1.00 32.46 ? 103 GLU C OE2 1 
ATOM   3728 N  N   . LEU C 1 116 ? -10.278 47.601  7.378   1.00 20.23 ? 104 LEU C N   1 
ATOM   3729 C  CA  . LEU C 1 116 ? -10.669 48.139  6.049   1.00 23.25 ? 104 LEU C CA  1 
ATOM   3730 C  C   . LEU C 1 116 ? -12.185 48.228  5.912   1.00 27.20 ? 104 LEU C C   1 
ATOM   3731 O  O   . LEU C 1 116 ? -12.639 48.858  4.941   1.00 31.50 ? 104 LEU C O   1 
ATOM   3732 C  CB  . LEU C 1 116 ? -10.056 47.284  4.934   1.00 24.92 ? 104 LEU C CB  1 
ATOM   3733 C  CG  . LEU C 1 116 ? -8.540  47.401  4.796   1.00 25.36 ? 104 LEU C CG  1 
ATOM   3734 C  CD1 . LEU C 1 116 ? -8.039  46.574  3.619   1.00 29.43 ? 104 LEU C CD1 1 
ATOM   3735 C  CD2 . LEU C 1 116 ? -8.098  48.859  4.633   1.00 26.29 ? 104 LEU C CD2 1 
ATOM   3736 N  N   . GLY C 1 117 ? -12.956 47.674  6.835   1.00 25.97 ? 105 GLY C N   1 
ATOM   3737 C  CA  . GLY C 1 117 ? -14.423 47.703  6.722   1.00 26.17 ? 105 GLY C CA  1 
ATOM   3738 C  C   . GLY C 1 117 ? -15.041 46.406  7.209   1.00 26.53 ? 105 GLY C C   1 
ATOM   3739 O  O   . GLY C 1 117 ? -14.438 45.754  8.053   1.00 23.98 ? 105 GLY C O   1 
ATOM   3740 N  N   . THR C 1 118 ? -16.234 46.078  6.730   1.00 25.55 ? 106 THR C N   1 
ATOM   3741 C  CA  . THR C 1 118 ? -17.001 44.906  7.238   1.00 25.03 ? 106 THR C CA  1 
ATOM   3742 C  C   . THR C 1 118 ? -17.743 44.225  6.090   1.00 25.49 ? 106 THR C C   1 
ATOM   3743 O  O   . THR C 1 118 ? -17.971 44.844  5.037   1.00 28.11 ? 106 THR C O   1 
ATOM   3744 C  CB  . THR C 1 118 ? -18.036 45.280  8.313   1.00 28.10 ? 106 THR C CB  1 
ATOM   3745 O  OG1 . THR C 1 118 ? -19.023 46.072  7.650   1.00 31.03 ? 106 THR C OG1 1 
ATOM   3746 C  CG2 . THR C 1 118 ? -17.483 46.011  9.509   1.00 28.96 ? 106 THR C CG2 1 
ATOM   3747 N  N   . VAL C 1 119 ? -18.142 42.987  6.292   1.00 24.18 ? 107 VAL C N   1 
ATOM   3748 C  CA  . VAL C 1 119 ? -18.964 42.233  5.307   1.00 21.55 ? 107 VAL C CA  1 
ATOM   3749 C  C   . VAL C 1 119 ? -19.989 41.476  6.132   1.00 22.72 ? 107 VAL C C   1 
ATOM   3750 O  O   . VAL C 1 119 ? -19.609 40.958  7.200   1.00 20.39 ? 107 VAL C O   1 
ATOM   3751 C  CB  . VAL C 1 119 ? -18.079 41.344  4.410   1.00 22.58 ? 107 VAL C CB  1 
ATOM   3752 C  CG1 . VAL C 1 119 ? -17.232 40.406  5.249   1.00 19.85 ? 107 VAL C CG1 1 
ATOM   3753 C  CG2 . VAL C 1 119 ? -18.884 40.564  3.382   1.00 22.77 ? 107 VAL C CG2 1 
ATOM   3754 N  N   . GLU C 1 120 ? -21.258 41.534  5.715   1.00 22.96 ? 108 GLU C N   1 
ATOM   3755 C  CA  . GLU C 1 120 ? -22.386 40.781  6.316   1.00 28.02 ? 108 GLU C CA  1 
ATOM   3756 C  C   . GLU C 1 120 ? -22.533 39.498  5.508   1.00 24.35 ? 108 GLU C C   1 
ATOM   3757 O  O   . GLU C 1 120 ? -22.694 39.622  4.300   1.00 25.55 ? 108 GLU C O   1 
ATOM   3758 C  CB  . GLU C 1 120 ? -23.670 41.620  6.247   1.00 32.49 ? 108 GLU C CB  1 
ATOM   3759 C  CG  . GLU C 1 120 ? -24.111 42.199  7.574   1.00 42.12 ? 108 GLU C CG  1 
ATOM   3760 C  CD  . GLU C 1 120 ? -25.614 42.450  7.663   1.00 50.00 ? 108 GLU C CD  1 
ATOM   3761 O  OE1 . GLU C 1 120 ? -26.243 41.962  8.644   1.00 51.66 ? 108 GLU C OE1 1 
ATOM   3762 O  OE2 . GLU C 1 120 ? -26.167 43.112  6.734   1.00 53.63 ? 108 GLU C OE2 1 
ATOM   3763 N  N   . THR C 1 121 ? -22.435 38.318  6.122   1.00 26.21 ? 109 THR C N   1 
ATOM   3764 C  CA  . THR C 1 121 ? -22.542 37.016  5.395   1.00 25.40 ? 109 THR C CA  1 
ATOM   3765 C  C   . THR C 1 121 ? -22.786 35.890  6.402   1.00 23.56 ? 109 THR C C   1 
ATOM   3766 O  O   . THR C 1 121 ? -22.280 35.963  7.542   1.00 24.30 ? 109 THR C O   1 
ATOM   3767 C  CB  . THR C 1 121 ? -21.346 36.792  4.456   1.00 27.32 ? 109 THR C CB  1 
ATOM   3768 O  OG1 . THR C 1 121 ? -21.436 35.540  3.780   1.00 27.58 ? 109 THR C OG1 1 
ATOM   3769 C  CG2 . THR C 1 121 ? -20.001 36.844  5.147   1.00 29.95 ? 109 THR C CG2 1 
ATOM   3770 N  N   . ASP C 1 122 ? -23.565 34.894  5.990   1.00 23.49 ? 110 ASP C N   1 
ATOM   3771 C  CA  . ASP C 1 122 ? -23.806 33.668  6.790   1.00 24.01 ? 110 ASP C CA  1 
ATOM   3772 C  C   . ASP C 1 122 ? -24.267 34.080  8.186   1.00 24.66 ? 110 ASP C C   1 
ATOM   3773 O  O   . ASP C 1 122 ? -23.717 33.557  9.163   1.00 22.39 ? 110 ASP C O   1 
ATOM   3774 C  CB  . ASP C 1 122 ? -22.516 32.848  6.752   1.00 22.35 ? 110 ASP C CB  1 
ATOM   3775 C  CG  . ASP C 1 122 ? -22.149 32.544  5.297   1.00 21.83 ? 110 ASP C CG  1 
ATOM   3776 O  OD1 . ASP C 1 122 ? -22.976 31.909  4.590   1.00 21.36 ? 110 ASP C OD1 1 
ATOM   3777 O  OD2 . ASP C 1 122 ? -21.060 32.976  4.851   1.00 23.02 ? 110 ASP C OD2 1 
ATOM   3778 N  N   . ASP C 1 123 ? -25.177 35.052  8.267   1.00 25.82 ? 111 ASP C N   1 
ATOM   3779 C  CA  . ASP C 1 123 ? -25.901 35.424  9.510   1.00 28.35 ? 111 ASP C CA  1 
ATOM   3780 C  C   . ASP C 1 123 ? -24.976 36.119  10.513  1.00 28.90 ? 111 ASP C C   1 
ATOM   3781 O  O   . ASP C 1 123 ? -25.297 36.108  11.719  1.00 28.34 ? 111 ASP C O   1 
ATOM   3782 C  CB  . ASP C 1 123 ? -26.554 34.190  10.141  1.00 30.73 ? 111 ASP C CB  1 
ATOM   3783 C  CG  . ASP C 1 123 ? -27.579 33.528  9.231   1.00 36.29 ? 111 ASP C CG  1 
ATOM   3784 O  OD1 . ASP C 1 123 ? -28.182 34.247  8.410   1.00 39.98 ? 111 ASP C OD1 1 
ATOM   3785 O  OD2 . ASP C 1 123 ? -27.776 32.296  9.358   1.00 43.54 ? 111 ASP C OD2 1 
ATOM   3786 N  N   . GLY C 1 124 ? -23.857 36.657  10.036  1.00 24.04 ? 112 GLY C N   1 
ATOM   3787 C  CA  . GLY C 1 124 ? -22.797 37.223  10.882  1.00 25.60 ? 112 GLY C CA  1 
ATOM   3788 C  C   . GLY C 1 124 ? -22.309 38.496  10.245  1.00 23.28 ? 112 GLY C C   1 
ATOM   3789 O  O   . GLY C 1 124 ? -22.742 38.782  9.101   1.00 25.64 ? 112 GLY C O   1 
ATOM   3790 N  N   . THR C 1 125 ? -21.558 39.273  11.009  1.00 23.77 ? 113 THR C N   1 
ATOM   3791 C  CA  . THR C 1 125 ? -20.775 40.421  10.530  1.00 23.45 ? 113 THR C CA  1 
ATOM   3792 C  C   . THR C 1 125 ? -19.297 40.091  10.725  1.00 20.33 ? 113 THR C C   1 
ATOM   3793 O  O   . THR C 1 125 ? -18.927 39.591  11.802  1.00 20.19 ? 113 THR C O   1 
ATOM   3794 C  CB  . THR C 1 125 ? -21.183 41.679  11.295  1.00 27.43 ? 113 THR C CB  1 
ATOM   3795 O  OG1 . THR C 1 125 ? -22.568 41.825  10.984  1.00 29.20 ? 113 THR C OG1 1 
ATOM   3796 C  CG2 . THR C 1 125 ? -20.363 42.889  10.916  1.00 26.69 ? 113 THR C CG2 1 
ATOM   3797 N  N   . TYR C 1 126 ? -18.505 40.336  9.703   1.00 17.36 ? 114 TYR C N   1 
ATOM   3798 C  CA  . TYR C 1 126 ? -17.046 40.136  9.745   1.00 18.11 ? 114 TYR C CA  1 
ATOM   3799 C  C   . TYR C 1 126 ? -16.356 41.465  9.523   1.00 16.96 ? 114 TYR C C   1 
ATOM   3800 O  O   . TYR C 1 126 ? -16.692 42.200  8.579   1.00 19.09 ? 114 TYR C O   1 
ATOM   3801 C  CB  . TYR C 1 126 ? -16.551 39.125  8.698   1.00 17.06 ? 114 TYR C CB  1 
ATOM   3802 C  CG  . TYR C 1 126 ? -17.101 37.735  8.836   1.00 16.46 ? 114 TYR C CG  1 
ATOM   3803 C  CD1 . TYR C 1 126 ? -18.444 37.440  8.587   1.00 14.83 ? 114 TYR C CD1 1 
ATOM   3804 C  CD2 . TYR C 1 126 ? -16.270 36.691  9.206   1.00 14.61 ? 114 TYR C CD2 1 
ATOM   3805 C  CE1 . TYR C 1 126 ? -18.927 36.139  8.686   1.00 15.85 ? 114 TYR C CE1 1 
ATOM   3806 C  CE2 . TYR C 1 126 ? -16.751 35.402  9.335   1.00 15.64 ? 114 TYR C CE2 1 
ATOM   3807 C  CZ  . TYR C 1 126 ? -18.068 35.112  9.053   1.00 15.20 ? 114 TYR C CZ  1 
ATOM   3808 O  OH  . TYR C 1 126 ? -18.572 33.857  9.210   1.00 16.36 ? 114 TYR C OH  1 
ATOM   3809 N  N   . LYS C 1 127 ? -15.333 41.713  10.330  1.00 17.38 ? 115 LYS C N   1 
ATOM   3810 C  CA  . LYS C 1 127 ? -14.420 42.842  10.130  1.00 17.91 ? 115 LYS C CA  1 
ATOM   3811 C  C   . LYS C 1 127 ? -13.313 42.356  9.196   1.00 16.94 ? 115 LYS C C   1 
ATOM   3812 O  O   . LYS C 1 127 ? -12.813 41.278  9.445   1.00 15.54 ? 115 LYS C O   1 
ATOM   3813 C  CB  . LYS C 1 127 ? -13.909 43.287  11.502  1.00 20.52 ? 115 LYS C CB  1 
ATOM   3814 C  CG  . LYS C 1 127 ? -15.005 43.738  12.462  1.00 24.14 ? 115 LYS C CG  1 
ATOM   3815 C  CD  . LYS C 1 127 ? -14.440 44.560  13.613  1.00 26.66 ? 115 LYS C CD  1 
ATOM   3816 C  CE  . LYS C 1 127 ? -15.476 45.168  14.544  1.00 29.24 ? 115 LYS C CE  1 
ATOM   3817 N  NZ  . LYS C 1 127 ? -14.824 45.728  15.754  1.00 30.22 ? 115 LYS C NZ  1 
ATOM   3818 N  N   . ILE C 1 128 ? -12.963 43.165  8.208   1.00 17.28 ? 116 ILE C N   1 
ATOM   3819 C  CA  . ILE C 1 128 ? -11.940 42.891  7.169   1.00 18.39 ? 116 ILE C CA  1 
ATOM   3820 C  C   . ILE C 1 128 ? -10.664 43.657  7.493   1.00 17.12 ? 116 ILE C C   1 
ATOM   3821 O  O   . ILE C 1 128 ? -10.724 44.876  7.854   1.00 17.02 ? 116 ILE C O   1 
ATOM   3822 C  CB  . ILE C 1 128 ? -12.481 43.311  5.794   1.00 21.78 ? 116 ILE C CB  1 
ATOM   3823 C  CG1 . ILE C 1 128 ? -13.725 42.508  5.409   1.00 26.20 ? 116 ILE C CG1 1 
ATOM   3824 C  CG2 . ILE C 1 128 ? -11.398 43.267  4.728   1.00 25.46 ? 116 ILE C CG2 1 
ATOM   3825 C  CD1 . ILE C 1 128 ? -13.749 41.069  5.843   1.00 26.04 ? 116 ILE C CD1 1 
ATOM   3826 N  N   . TYR C 1 129 ? -9.527  43.004  7.294   1.00 15.15 ? 117 TYR C N   1 
ATOM   3827 C  CA  . TYR C 1 129 ? -8.193  43.571  7.587   1.00 15.67 ? 117 TYR C CA  1 
ATOM   3828 C  C   . TYR C 1 129 ? -7.202  43.120  6.525   1.00 16.58 ? 117 TYR C C   1 
ATOM   3829 O  O   . TYR C 1 129 ? -7.353  42.066  5.920   1.00 17.03 ? 117 TYR C O   1 
ATOM   3830 C  CB  . TYR C 1 129 ? -7.632  43.132  8.937   1.00 16.20 ? 117 TYR C CB  1 
ATOM   3831 C  CG  . TYR C 1 129 ? -8.507  43.344  10.153  1.00 18.26 ? 117 TYR C CG  1 
ATOM   3832 C  CD1 . TYR C 1 129 ? -9.538  42.458  10.446  1.00 17.48 ? 117 TYR C CD1 1 
ATOM   3833 C  CD2 . TYR C 1 129 ? -8.287  44.397  11.028  1.00 19.41 ? 117 TYR C CD2 1 
ATOM   3834 C  CE1 . TYR C 1 129 ? -10.354 42.636  11.546  1.00 17.95 ? 117 TYR C CE1 1 
ATOM   3835 C  CE2 . TYR C 1 129 ? -9.092  44.578  12.142  1.00 20.26 ? 117 TYR C CE2 1 
ATOM   3836 C  CZ  . TYR C 1 129 ? -10.121 43.694  12.406  1.00 19.03 ? 117 TYR C CZ  1 
ATOM   3837 O  OH  . TYR C 1 129 ? -10.910 43.840  13.517  1.00 20.95 ? 117 TYR C OH  1 
ATOM   3838 N  N   . GLN C 1 130 ? -6.136  43.906  6.392   1.00 18.13 ? 118 GLN C N   1 
ATOM   3839 C  CA  . GLN C 1 130 ? -4.964  43.545  5.583   1.00 18.98 ? 118 GLN C CA  1 
ATOM   3840 C  C   . GLN C 1 130 ? -3.697  43.886  6.364   1.00 17.89 ? 118 GLN C C   1 
ATOM   3841 O  O   . GLN C 1 130 ? -3.644  44.926  7.056   1.00 18.70 ? 118 GLN C O   1 
ATOM   3842 C  CB  . GLN C 1 130 ? -5.021  44.248  4.225   1.00 23.54 ? 118 GLN C CB  1 
ATOM   3843 C  CG  . GLN C 1 130 ? -4.693  45.743  4.269   1.00 29.40 ? 118 GLN C CG  1 
ATOM   3844 C  CD  . GLN C 1 130 ? -3.225  46.055  4.119   1.00 29.86 ? 118 GLN C CD  1 
ATOM   3845 O  OE1 . GLN C 1 130 ? -2.483  45.340  3.447   1.00 41.03 ? 118 GLN C OE1 1 
ATOM   3846 N  NE2 . GLN C 1 130 ? -2.785  47.109  4.783   1.00 37.85 ? 118 GLN C NE2 1 
ATOM   3847 N  N   . THR C 1 131 ? -2.692  43.034  6.207   1.00 19.97 ? 119 THR C N   1 
ATOM   3848 C  CA  . THR C 1 131 ? -1.290  43.318  6.587   1.00 22.79 ? 119 THR C CA  1 
ATOM   3849 C  C   . THR C 1 131 ? -0.349  42.642  5.601   1.00 22.66 ? 119 THR C C   1 
ATOM   3850 O  O   . THR C 1 131 ? -0.814  42.029  4.628   1.00 21.01 ? 119 THR C O   1 
ATOM   3851 C  CB  . THR C 1 131 ? -0.809  42.838  7.964   1.00 28.00 ? 119 THR C CB  1 
ATOM   3852 O  OG1 . THR C 1 131 ? -1.290  41.521  8.214   1.00 31.29 ? 119 THR C OG1 1 
ATOM   3853 C  CG2 . THR C 1 131 ? -1.119  43.801  9.079   1.00 35.37 ? 119 THR C CG2 1 
ATOM   3854 N  N   . THR C 1 132 ? 0.947   42.851  5.799   1.00 25.30 ? 120 THR C N   1 
ATOM   3855 C  CA  . THR C 1 132 ? 2.019   42.198  5.001   1.00 30.45 ? 120 THR C CA  1 
ATOM   3856 C  C   . THR C 1 132 ? 2.822   41.324  5.958   1.00 28.53 ? 120 THR C C   1 
ATOM   3857 O  O   . THR C 1 132 ? 2.940   41.720  7.144   1.00 32.34 ? 120 THR C O   1 
ATOM   3858 C  CB  . THR C 1 132 ? 2.877   43.246  4.277   1.00 33.59 ? 120 THR C CB  1 
ATOM   3859 O  OG1 . THR C 1 132 ? 2.023   43.944  3.371   1.00 37.95 ? 120 THR C OG1 1 
ATOM   3860 C  CG2 . THR C 1 132 ? 4.029   42.651  3.496   1.00 36.87 ? 120 THR C CG2 1 
ATOM   3861 N  N   . ARG C 1 133 ? 3.300   40.170  5.496   1.00 25.31 ? 121 ARG C N   1 
ATOM   3862 C  CA  . ARG C 1 133 ? 4.266   39.312  6.230   1.00 27.01 ? 121 ARG C CA  1 
ATOM   3863 C  C   . ARG C 1 133 ? 5.585   39.380  5.469   1.00 28.02 ? 121 ARG C C   1 
ATOM   3864 O  O   . ARG C 1 133 ? 5.532   39.246  4.229   1.00 25.27 ? 121 ARG C O   1 
ATOM   3865 C  CB  . ARG C 1 133 ? 3.777   37.870  6.334   1.00 28.93 ? 121 ARG C CB  1 
ATOM   3866 C  CG  . ARG C 1 133 ? 2.485   37.722  7.124   1.00 32.74 ? 121 ARG C CG  1 
ATOM   3867 C  CD  . ARG C 1 133 ? 2.750   37.684  8.617   1.00 37.96 ? 121 ARG C CD  1 
ATOM   3868 N  NE  . ARG C 1 133 ? 3.316   36.393  8.979   1.00 41.86 ? 121 ARG C NE  1 
ATOM   3869 C  CZ  . ARG C 1 133 ? 4.451   36.194  9.655   1.00 43.06 ? 121 ARG C CZ  1 
ATOM   3870 N  NH1 . ARG C 1 133 ? 5.167   37.209  10.110  1.00 43.90 ? 121 ARG C NH1 1 
ATOM   3871 N  NH2 . ARG C 1 133 ? 4.851   34.957  9.899   1.00 45.17 ? 121 ARG C NH2 1 
ATOM   3872 N  N   . GLU C 1 134 ? 6.688   39.564  6.207   1.00 29.23 ? 122 GLU C N   1 
ATOM   3873 C  CA  . GLU C 1 134 ? 8.058   39.786  5.667   1.00 33.84 ? 122 GLU C CA  1 
ATOM   3874 C  C   . GLU C 1 134 ? 8.878   38.516  5.848   1.00 31.08 ? 122 GLU C C   1 
ATOM   3875 O  O   . GLU C 1 134 ? 8.906   37.996  6.980   1.00 30.84 ? 122 GLU C O   1 
ATOM   3876 C  CB  . GLU C 1 134 ? 8.770   40.924  6.416   1.00 38.81 ? 122 GLU C CB  1 
ATOM   3877 C  CG  . GLU C 1 134 ? 8.479   42.316  5.874   1.00 43.88 ? 122 GLU C CG  1 
ATOM   3878 C  CD  . GLU C 1 134 ? 9.190   43.428  6.644   1.00 51.53 ? 122 GLU C CD  1 
ATOM   3879 O  OE1 . GLU C 1 134 ? 10.182  43.978  6.112   1.00 52.87 ? 122 GLU C OE1 1 
ATOM   3880 O  OE2 . GLU C 1 134 ? 8.769   43.734  7.790   1.00 52.88 ? 122 GLU C OE2 1 
ATOM   3881 N  N   . ASN C 1 135 ? 9.523   38.021  4.787   1.00 33.27 ? 123 ASN C N   1 
ATOM   3882 C  CA  . ASN C 1 135 ? 10.449  36.868  4.892   1.00 34.94 ? 123 ASN C CA  1 
ATOM   3883 C  C   . ASN C 1 135 ? 9.857   35.812  5.836   1.00 34.27 ? 123 ASN C C   1 
ATOM   3884 O  O   . ASN C 1 135 ? 10.526  35.447  6.811   1.00 31.26 ? 123 ASN C O   1 
ATOM   3885 C  CB  . ASN C 1 135 ? 11.819  37.316  5.416   1.00 41.23 ? 123 ASN C CB  1 
ATOM   3886 C  CG  . ASN C 1 135 ? 12.328  38.565  4.735   1.00 42.39 ? 123 ASN C CG  1 
ATOM   3887 O  OD1 . ASN C 1 135 ? 12.446  38.600  3.515   1.00 41.90 ? 123 ASN C OD1 1 
ATOM   3888 N  ND2 . ASN C 1 135 ? 12.642  39.586  5.516   1.00 46.86 ? 123 ASN C ND2 1 
ATOM   3889 N  N   . ALA C 1 136 ? 8.641   35.353  5.555   1.00 26.59 ? 124 ALA C N   1 
ATOM   3890 C  CA  . ALA C 1 136 ? 7.872   34.393  6.379   1.00 28.65 ? 124 ALA C CA  1 
ATOM   3891 C  C   . ALA C 1 136 ? 7.682   33.091  5.597   1.00 28.14 ? 124 ALA C C   1 
ATOM   3892 O  O   . ALA C 1 136 ? 7.727   33.098  4.366   1.00 24.99 ? 124 ALA C O   1 
ATOM   3893 C  CB  . ALA C 1 136 ? 6.546   35.023  6.777   1.00 26.96 ? 124 ALA C CB  1 
ATOM   3894 N  N   . PRO C 1 137 ? 7.411   31.952  6.272   1.00 26.67 ? 125 PRO C N   1 
ATOM   3895 C  CA  . PRO C 1 137 ? 7.118   30.690  5.599   1.00 27.97 ? 125 PRO C CA  1 
ATOM   3896 C  C   . PRO C 1 137 ? 5.868   30.874  4.731   1.00 23.92 ? 125 PRO C C   1 
ATOM   3897 O  O   . PRO C 1 137 ? 4.918   31.610  5.161   1.00 25.12 ? 125 PRO C O   1 
ATOM   3898 C  CB  . PRO C 1 137 ? 6.846   29.670  6.723   1.00 31.12 ? 125 PRO C CB  1 
ATOM   3899 C  CG  . PRO C 1 137 ? 6.553   30.535  7.938   1.00 33.12 ? 125 PRO C CG  1 
ATOM   3900 C  CD  . PRO C 1 137 ? 7.343   31.814  7.740   1.00 34.30 ? 125 PRO C CD  1 
ATOM   3901 N  N   . SER C 1 138 ? 5.870   30.212  3.587   1.00 23.05 ? 126 SER C N   1 
ATOM   3902 C  CA  . SER C 1 138 ? 4.762   30.240  2.605   1.00 22.28 ? 126 SER C CA  1 
ATOM   3903 C  C   . SER C 1 138 ? 4.745   28.944  1.800   1.00 23.78 ? 126 SER C C   1 
ATOM   3904 O  O   . SER C 1 138 ? 5.749   28.190  1.791   1.00 25.71 ? 126 SER C O   1 
ATOM   3905 C  CB  . SER C 1 138 ? 4.896   31.462  1.708   1.00 23.22 ? 126 SER C CB  1 
ATOM   3906 O  OG  . SER C 1 138 ? 5.785   31.184  0.637   1.00 21.12 ? 126 SER C OG  1 
ATOM   3907 N  N   . ILE C 1 139 ? 3.670   28.734  1.051   1.00 24.09 ? 127 ILE C N   1 
ATOM   3908 C  CA  . ILE C 1 139 ? 3.568   27.590  0.120   1.00 26.79 ? 127 ILE C CA  1 
ATOM   3909 C  C   . ILE C 1 139 ? 4.723   27.648  -0.892  1.00 26.83 ? 127 ILE C C   1 
ATOM   3910 O  O   . ILE C 1 139 ? 4.953   26.616  -1.519  1.00 26.89 ? 127 ILE C O   1 
ATOM   3911 C  CB  . ILE C 1 139 ? 2.183   27.541  -0.545  1.00 24.21 ? 127 ILE C CB  1 
ATOM   3912 C  CG1 . ILE C 1 139 ? 1.846   28.808  -1.342  1.00 25.22 ? 127 ILE C CG1 1 
ATOM   3913 C  CG2 . ILE C 1 139 ? 1.138   27.234  0.520   1.00 27.36 ? 127 ILE C CG2 1 
ATOM   3914 C  CD1 . ILE C 1 139 ? 0.810   28.556  -2.433  1.00 24.01 ? 127 ILE C CD1 1 
ATOM   3915 N  N   . GLU C 1 140 ? 5.414   28.781  -1.051  1.00 28.10 ? 128 GLU C N   1 
ATOM   3916 C  CA  . GLU C 1 140 ? 6.501   28.889  -2.060  1.00 27.82 ? 128 GLU C CA  1 
ATOM   3917 C  C   . GLU C 1 140 ? 7.866   28.949  -1.364  1.00 29.58 ? 128 GLU C C   1 
ATOM   3918 O  O   . GLU C 1 140 ? 8.880   29.138  -2.070  1.00 29.04 ? 128 GLU C O   1 
ATOM   3919 C  CB  . GLU C 1 140 ? 6.316   30.141  -2.915  1.00 34.11 ? 128 GLU C CB  1 
ATOM   3920 C  CG  . GLU C 1 140 ? 5.047   30.161  -3.739  1.00 37.03 ? 128 GLU C CG  1 
ATOM   3921 C  CD  . GLU C 1 140 ? 4.999   31.304  -4.731  1.00 44.89 ? 128 GLU C CD  1 
ATOM   3922 O  OE1 . GLU C 1 140 ? 3.930   31.509  -5.355  1.00 52.28 ? 128 GLU C OE1 1 
ATOM   3923 O  OE2 . GLU C 1 140 ? 6.044   31.976  -4.908  1.00 47.23 ? 128 GLU C OE2 1 
ATOM   3924 N  N   . GLY C 1 141 ? 7.902   28.816  -0.040  1.00 24.68 ? 129 GLY C N   1 
ATOM   3925 C  CA  . GLY C 1 141 ? 9.147   28.971  0.739   1.00 27.07 ? 129 GLY C CA  1 
ATOM   3926 C  C   . GLY C 1 141 ? 9.189   30.323  1.393   1.00 22.26 ? 129 GLY C C   1 
ATOM   3927 O  O   . GLY C 1 141 ? 8.170   31.013  1.381   1.00 25.76 ? 129 GLY C O   1 
ATOM   3928 N  N   . THR C 1 142 ? 10.327  30.721  1.940   1.00 23.31 ? 130 THR C N   1 
ATOM   3929 C  CA  . THR C 1 142 ? 10.448  32.019  2.634   1.00 22.39 ? 130 THR C CA  1 
ATOM   3930 C  C   . THR C 1 142 ? 10.068  33.132  1.650   1.00 23.49 ? 130 THR C C   1 
ATOM   3931 O  O   . THR C 1 142 ? 10.666  33.221  0.574   1.00 25.31 ? 130 THR C O   1 
ATOM   3932 C  CB  . THR C 1 142 ? 11.831  32.193  3.254   1.00 24.23 ? 130 THR C CB  1 
ATOM   3933 O  OG1 . THR C 1 142 ? 12.082  31.049  4.079   1.00 27.16 ? 130 THR C OG1 1 
ATOM   3934 C  CG2 . THR C 1 142 ? 11.915  33.484  4.028   1.00 23.61 ? 130 THR C CG2 1 
ATOM   3935 N  N   . ALA C 1 143 ? 9.099   33.960  1.991   1.00 22.35 ? 131 ALA C N   1 
ATOM   3936 C  CA  . ALA C 1 143 ? 8.589   34.988  1.062   1.00 22.05 ? 131 ALA C CA  1 
ATOM   3937 C  C   . ALA C 1 143 ? 7.955   36.175  1.785   1.00 24.37 ? 131 ALA C C   1 
ATOM   3938 O  O   . ALA C 1 143 ? 7.588   36.082  2.999   1.00 25.18 ? 131 ALA C O   1 
ATOM   3939 C  CB  . ALA C 1 143 ? 7.608   34.357  0.094   1.00 20.45 ? 131 ALA C CB  1 
ATOM   3940 N  N   . THR C 1 144 ? 7.742   37.237  1.022   1.00 22.10 ? 132 THR C N   1 
ATOM   3941 C  CA  . THR C 1 144 ? 6.955   38.403  1.462   1.00 22.42 ? 132 THR C CA  1 
ATOM   3942 C  C   . THR C 1 144 ? 5.602   38.344  0.756   1.00 21.82 ? 132 THR C C   1 
ATOM   3943 O  O   . THR C 1 144 ? 5.583   38.128  -0.441  1.00 19.90 ? 132 THR C O   1 
ATOM   3944 C  CB  . THR C 1 144 ? 7.758   39.681  1.191   1.00 25.54 ? 132 THR C CB  1 
ATOM   3945 O  OG1 . THR C 1 144 ? 8.865   39.596  2.089   1.00 25.24 ? 132 THR C OG1 1 
ATOM   3946 C  CG2 . THR C 1 144 ? 6.948   40.939  1.398   1.00 25.57 ? 132 THR C CG2 1 
ATOM   3947 N  N   . PHE C 1 145 ? 4.511   38.565  1.471   1.00 20.93 ? 133 PHE C N   1 
ATOM   3948 C  CA  . PHE C 1 145 ? 3.150   38.395  0.903   1.00 19.84 ? 133 PHE C CA  1 
ATOM   3949 C  C   . PHE C 1 145 ? 2.127   39.178  1.719   1.00 18.73 ? 133 PHE C C   1 
ATOM   3950 O  O   . PHE C 1 145 ? 2.360   39.531  2.874   1.00 18.85 ? 133 PHE C O   1 
ATOM   3951 C  CB  . PHE C 1 145 ? 2.825   36.910  0.805   1.00 21.98 ? 133 PHE C CB  1 
ATOM   3952 C  CG  . PHE C 1 145 ? 2.996   36.126  2.074   1.00 20.54 ? 133 PHE C CG  1 
ATOM   3953 C  CD1 . PHE C 1 145 ? 1.942   35.940  2.949   1.00 21.85 ? 133 PHE C CD1 1 
ATOM   3954 C  CD2 . PHE C 1 145 ? 4.197   35.503  2.356   1.00 21.84 ? 133 PHE C CD2 1 
ATOM   3955 C  CE1 . PHE C 1 145 ? 2.097   35.167  4.085   1.00 22.07 ? 133 PHE C CE1 1 
ATOM   3956 C  CE2 . PHE C 1 145 ? 4.366   34.764  3.512   1.00 21.93 ? 133 PHE C CE2 1 
ATOM   3957 C  CZ  . PHE C 1 145 ? 3.316   34.598  4.383   1.00 22.28 ? 133 PHE C CZ  1 
ATOM   3958 N  N   . ASN C 1 146 ? 0.991   39.459  1.089   1.00 18.37 ? 134 ASN C N   1 
ATOM   3959 C  CA  . ASN C 1 146 ? -0.160  40.112  1.728   1.00 18.45 ? 134 ASN C CA  1 
ATOM   3960 C  C   . ASN C 1 146 ? -0.903  39.055  2.528   1.00 16.09 ? 134 ASN C C   1 
ATOM   3961 O  O   . ASN C 1 146 ? -0.919  37.878  2.115   1.00 15.71 ? 134 ASN C O   1 
ATOM   3962 C  CB  . ASN C 1 146 ? -1.047  40.814  0.700   1.00 22.27 ? 134 ASN C CB  1 
ATOM   3963 C  CG  . ASN C 1 146 ? -0.345  42.025  0.113   1.00 28.78 ? 134 ASN C CG  1 
ATOM   3964 O  OD1 . ASN C 1 146 ? 0.409   42.690  0.812   1.00 38.27 ? 134 ASN C OD1 1 
ATOM   3965 N  ND2 . ASN C 1 146 ? -0.556  42.308  -1.161  1.00 31.59 ? 134 ASN C ND2 1 
ATOM   3966 N  N   . GLN C 1 147 ? -1.474  39.481  3.638   1.00 15.50 ? 135 GLN C N   1 
ATOM   3967 C  CA  . GLN C 1 147 ? -2.288  38.552  4.464   1.00 17.20 ? 135 GLN C CA  1 
ATOM   3968 C  C   . GLN C 1 147 ? -3.623  39.251  4.690   1.00 17.14 ? 135 GLN C C   1 
ATOM   3969 O  O   . GLN C 1 147 ? -3.605  40.425  5.102   1.00 16.01 ? 135 GLN C O   1 
ATOM   3970 C  CB  . GLN C 1 147 ? -1.481  38.186  5.717   1.00 18.00 ? 135 GLN C CB  1 
ATOM   3971 C  CG  . GLN C 1 147 ? -2.185  37.249  6.674   1.00 19.38 ? 135 GLN C CG  1 
ATOM   3972 C  CD  . GLN C 1 147 ? -1.433  37.219  7.981   1.00 21.94 ? 135 GLN C CD  1 
ATOM   3973 O  OE1 . GLN C 1 147 ? -1.423  38.220  8.716   1.00 26.10 ? 135 GLN C OE1 1 
ATOM   3974 N  NE2 . GLN C 1 147 ? -0.760  36.112  8.255   1.00 21.90 ? 135 GLN C NE2 1 
ATOM   3975 N  N   . TYR C 1 148 ? -4.735  38.621  4.321   1.00 15.41 ? 136 TYR C N   1 
ATOM   3976 C  CA  . TYR C 1 148 ? -6.081  39.222  4.435   1.00 14.70 ? 136 TYR C CA  1 
ATOM   3977 C  C   . TYR C 1 148 ? -6.836  38.468  5.518   1.00 15.24 ? 136 TYR C C   1 
ATOM   3978 O  O   . TYR C 1 148 ? -6.691  37.244  5.599   1.00 15.76 ? 136 TYR C O   1 
ATOM   3979 C  CB  . TYR C 1 148 ? -6.879  39.235  3.120   1.00 17.13 ? 136 TYR C CB  1 
ATOM   3980 C  CG  . TYR C 1 148 ? -6.179  39.839  1.924   1.00 16.36 ? 136 TYR C CG  1 
ATOM   3981 C  CD1 . TYR C 1 148 ? -5.173  40.788  2.056   1.00 19.69 ? 136 TYR C CD1 1 
ATOM   3982 C  CD2 . TYR C 1 148 ? -6.512  39.406  0.651   1.00 19.51 ? 136 TYR C CD2 1 
ATOM   3983 C  CE1 . TYR C 1 148 ? -4.535  41.307  0.936   1.00 20.05 ? 136 TYR C CE1 1 
ATOM   3984 C  CE2 . TYR C 1 148 ? -5.884  39.908  -0.478  1.00 20.04 ? 136 TYR C CE2 1 
ATOM   3985 C  CZ  . TYR C 1 148 ? -4.904  40.870  -0.335  1.00 19.47 ? 136 TYR C CZ  1 
ATOM   3986 O  OH  . TYR C 1 148 ? -4.304  41.354  -1.464  1.00 21.91 ? 136 TYR C OH  1 
ATOM   3987 N  N   . TRP C 1 149 ? -7.675  39.184  6.262   1.00 12.86 ? 137 TRP C N   1 
ATOM   3988 C  CA  . TRP C 1 149 ? -8.479  38.656  7.396   1.00 14.57 ? 137 TRP C CA  1 
ATOM   3989 C  C   . TRP C 1 149 ? -9.924  39.079  7.207   1.00 15.33 ? 137 TRP C C   1 
ATOM   3990 O  O   . TRP C 1 149 ? -10.171 40.276  6.885   1.00 15.72 ? 137 TRP C O   1 
ATOM   3991 C  CB  . TRP C 1 149 ? -7.971  39.213  8.728   1.00 15.20 ? 137 TRP C CB  1 
ATOM   3992 C  CG  . TRP C 1 149 ? -6.560  38.838  9.046   1.00 15.36 ? 137 TRP C CG  1 
ATOM   3993 C  CD1 . TRP C 1 149 ? -5.428  39.468  8.642   1.00 16.77 ? 137 TRP C CD1 1 
ATOM   3994 C  CD2 . TRP C 1 149 ? -6.127  37.695  9.798   1.00 14.93 ? 137 TRP C CD2 1 
ATOM   3995 N  NE1 . TRP C 1 149 ? -4.325  38.804  9.093   1.00 16.82 ? 137 TRP C NE1 1 
ATOM   3996 C  CE2 . TRP C 1 149 ? -4.719  37.728  9.839   1.00 16.90 ? 137 TRP C CE2 1 
ATOM   3997 C  CE3 . TRP C 1 149 ? -6.786  36.659  10.475  1.00 15.30 ? 137 TRP C CE3 1 
ATOM   3998 C  CZ2 . TRP C 1 149 ? -3.961  36.753  10.476  1.00 16.69 ? 137 TRP C CZ2 1 
ATOM   3999 C  CZ3 . TRP C 1 149 ? -6.037  35.697  11.102  1.00 15.31 ? 137 TRP C CZ3 1 
ATOM   4000 C  CH2 . TRP C 1 149 ? -4.644  35.749  11.122  1.00 16.57 ? 137 TRP C CH2 1 
ATOM   4001 N  N   . SER C 1 150 ? -10.839 38.176  7.525   1.00 15.09 ? 138 SER C N   1 
ATOM   4002 C  CA  . SER C 1 150 ? -12.259 38.471  7.833   1.00 15.58 ? 138 SER C CA  1 
ATOM   4003 C  C   . SER C 1 150 ? -12.549 37.862  9.182   1.00 16.08 ? 138 SER C C   1 
ATOM   4004 O  O   . SER C 1 150 ? -12.308 36.659  9.317   1.00 16.72 ? 138 SER C O   1 
ATOM   4005 C  CB  . SER C 1 150 ? -13.236 37.913  6.843   1.00 19.81 ? 138 SER C CB  1 
ATOM   4006 O  OG  . SER C 1 150 ? -13.140 38.537  5.609   1.00 28.20 ? 138 SER C OG  1 
ATOM   4007 N  N   . VAL C 1 151 ? -12.985 38.636  10.178  1.00 15.10 ? 139 VAL C N   1 
ATOM   4008 C  CA  . VAL C 1 151 ? -13.067 38.051  11.546  1.00 15.93 ? 139 VAL C CA  1 
ATOM   4009 C  C   . VAL C 1 151 ? -14.492 38.207  12.054  1.00 17.11 ? 139 VAL C C   1 
ATOM   4010 O  O   . VAL C 1 151 ? -14.978 39.352  12.148  1.00 15.64 ? 139 VAL C O   1 
ATOM   4011 C  CB  . VAL C 1 151 ? -12.038 38.664  12.496  1.00 16.86 ? 139 VAL C CB  1 
ATOM   4012 C  CG1 . VAL C 1 151 ? -12.144 38.112  13.907  1.00 18.19 ? 139 VAL C CG1 1 
ATOM   4013 C  CG2 . VAL C 1 151 ? -10.611 38.529  11.942  1.00 18.84 ? 139 VAL C CG2 1 
ATOM   4014 N  N   . ARG C 1 152 ? -15.137 37.091  12.377  1.00 15.31 ? 140 ARG C N   1 
ATOM   4015 C  CA  . ARG C 1 152 ? -16.578 37.120  12.707  1.00 15.69 ? 140 ARG C CA  1 
ATOM   4016 C  C   . ARG C 1 152 ? -16.721 37.852  14.042  1.00 16.81 ? 140 ARG C C   1 
ATOM   4017 O  O   . ARG C 1 152 ? -15.945 37.564  14.957  1.00 18.28 ? 140 ARG C O   1 
ATOM   4018 C  CB  . ARG C 1 152 ? -17.125 35.703  12.779  1.00 16.59 ? 140 ARG C CB  1 
ATOM   4019 C  CG  . ARG C 1 152 ? -18.631 35.619  12.589  1.00 17.64 ? 140 ARG C CG  1 
ATOM   4020 C  CD  . ARG C 1 152 ? -19.103 34.204  12.707  1.00 18.34 ? 140 ARG C CD  1 
ATOM   4021 N  NE  . ARG C 1 152 ? -20.561 34.120  12.812  1.00 20.04 ? 140 ARG C NE  1 
ATOM   4022 C  CZ  . ARG C 1 152 ? -21.419 34.017  11.799  1.00 19.96 ? 140 ARG C CZ  1 
ATOM   4023 N  NH1 . ARG C 1 152 ? -21.009 33.939  10.545  1.00 20.00 ? 140 ARG C NH1 1 
ATOM   4024 N  NH2 . ARG C 1 152 ? -22.715 33.953  12.071  1.00 21.42 ? 140 ARG C NH2 1 
ATOM   4025 N  N   . THR C 1 153 ? -17.722 38.718  14.175  1.00 18.43 ? 141 THR C N   1 
ATOM   4026 C  CA  . THR C 1 153 ? -17.881 39.525  15.418  1.00 22.94 ? 141 THR C CA  1 
ATOM   4027 C  C   . THR C 1 153 ? -18.507 38.643  16.500  1.00 24.31 ? 141 THR C C   1 
ATOM   4028 O  O   . THR C 1 153 ? -18.123 38.805  17.666  1.00 27.49 ? 141 THR C O   1 
ATOM   4029 C  CB  . THR C 1 153 ? -18.690 40.804  15.171  1.00 21.80 ? 141 THR C CB  1 
ATOM   4030 O  OG1 . THR C 1 153 ? -19.976 40.464  14.678  1.00 27.21 ? 141 THR C OG1 1 
ATOM   4031 C  CG2 . THR C 1 153 ? -18.024 41.739  14.194  1.00 21.05 ? 141 THR C CG2 1 
ATOM   4032 N  N   . ASP C 1 154 ? -19.421 37.755  16.111  1.00 23.78 ? 142 ASP C N   1 
ATOM   4033 C  CA  . ASP C 1 154 ? -20.089 36.772  16.998  1.00 26.62 ? 142 ASP C CA  1 
ATOM   4034 C  C   . ASP C 1 154 ? -19.513 35.380  16.714  1.00 21.47 ? 142 ASP C C   1 
ATOM   4035 O  O   . ASP C 1 154 ? -19.887 34.786  15.691  1.00 24.32 ? 142 ASP C O   1 
ATOM   4036 C  CB  . ASP C 1 154 ? -21.601 36.800  16.766  1.00 31.87 ? 142 ASP C CB  1 
ATOM   4037 C  CG  . ASP C 1 154 ? -22.334 37.944  17.432  1.00 37.63 ? 142 ASP C CG  1 
ATOM   4038 O  OD1 . ASP C 1 154 ? -21.791 38.511  18.409  1.00 38.51 ? 142 ASP C OD1 1 
ATOM   4039 O  OD2 . ASP C 1 154 ? -23.474 38.220  16.998  1.00 45.68 ? 142 ASP C OD2 1 
ATOM   4040 N  N   . HIS C 1 155 ? -18.637 34.882  17.581  1.00 23.12 ? 143 HIS C N   1 
ATOM   4041 C  CA  . HIS C 1 155 ? -17.891 33.610  17.349  1.00 21.54 ? 143 HIS C CA  1 
ATOM   4042 C  C   . HIS C 1 155 ? -18.846 32.427  17.197  1.00 21.52 ? 143 HIS C C   1 
ATOM   4043 O  O   . HIS C 1 155 ? -19.882 32.354  17.925  1.00 20.36 ? 143 HIS C O   1 
ATOM   4044 C  CB  . HIS C 1 155 ? -16.878 33.421  18.457  1.00 22.15 ? 143 HIS C CB  1 
ATOM   4045 C  CG  . HIS C 1 155 ? -15.883 34.522  18.430  1.00 24.13 ? 143 HIS C CG  1 
ATOM   4046 N  ND1 . HIS C 1 155 ? -14.806 34.553  19.262  1.00 24.63 ? 143 HIS C ND1 1 
ATOM   4047 C  CD2 . HIS C 1 155 ? -15.761 35.585  17.598  1.00 24.15 ? 143 HIS C CD2 1 
ATOM   4048 C  CE1 . HIS C 1 155 ? -14.087 35.621  19.014  1.00 25.83 ? 143 HIS C CE1 1 
ATOM   4049 N  NE2 . HIS C 1 155 ? -14.657 36.276  18.005  1.00 28.31 ? 143 HIS C NE2 1 
ATOM   4050 N  N   . ARG C 1 156 ? -18.518 31.522  16.281  1.00 18.35 ? 144 ARG C N   1 
ATOM   4051 C  CA  . ARG C 1 156 ? -19.240 30.236  16.163  1.00 20.15 ? 144 ARG C CA  1 
ATOM   4052 C  C   . ARG C 1 156 ? -18.270 29.118  15.823  1.00 18.39 ? 144 ARG C C   1 
ATOM   4053 O  O   . ARG C 1 156 ? -17.160 29.380  15.352  1.00 17.71 ? 144 ARG C O   1 
ATOM   4054 C  CB  . ARG C 1 156 ? -20.392 30.305  15.163  1.00 21.30 ? 144 ARG C CB  1 
ATOM   4055 C  CG  . ARG C 1 156 ? -19.950 30.591  13.746  1.00 25.47 ? 144 ARG C CG  1 
ATOM   4056 C  CD  . ARG C 1 156 ? -21.087 30.738  12.741  1.00 25.16 ? 144 ARG C CD  1 
ATOM   4057 N  NE  . ARG C 1 156 ? -20.476 30.697  11.427  1.00 24.85 ? 144 ARG C NE  1 
ATOM   4058 C  CZ  . ARG C 1 156 ? -21.140 30.514  10.283  1.00 27.51 ? 144 ARG C CZ  1 
ATOM   4059 N  NH1 . ARG C 1 156 ? -22.457 30.385  10.289  1.00 25.99 ? 144 ARG C NH1 1 
ATOM   4060 N  NH2 . ARG C 1 156 ? -20.478 30.469  9.141   1.00 29.35 ? 144 ARG C NH2 1 
ATOM   4061 N  N   . VAL C 1 157 ? -18.716 27.912  16.115  1.00 18.19 ? 145 VAL C N   1 
ATOM   4062 C  CA  . VAL C 1 157 ? -18.038 26.653  15.715  1.00 18.51 ? 145 VAL C CA  1 
ATOM   4063 C  C   . VAL C 1 157 ? -19.039 25.851  14.885  1.00 20.54 ? 145 VAL C C   1 
ATOM   4064 O  O   . VAL C 1 157 ? -19.950 25.195  15.452  1.00 22.92 ? 145 VAL C O   1 
ATOM   4065 C  CB  . VAL C 1 157 ? -17.554 25.886  16.953  1.00 18.16 ? 145 VAL C CB  1 
ATOM   4066 C  CG1 . VAL C 1 157 ? -16.875 24.596  16.574  1.00 18.67 ? 145 VAL C CG1 1 
ATOM   4067 C  CG2 . VAL C 1 157 ? -16.677 26.762  17.850  1.00 20.80 ? 145 VAL C CG2 1 
ATOM   4068 N  N   . GLY C 1 158 ? -18.904 25.921  13.572  1.00 19.99 ? 146 GLY C N   1 
ATOM   4069 C  CA  . GLY C 1 158 ? -19.730 25.153  12.636  1.00 20.35 ? 146 GLY C CA  1 
ATOM   4070 C  C   . GLY C 1 158 ? -20.710 26.049  11.910  1.00 19.67 ? 146 GLY C C   1 
ATOM   4071 O  O   . GLY C 1 158 ? -21.247 27.026  12.502  1.00 23.07 ? 146 GLY C O   1 
ATOM   4072 N  N   . GLY C 1 159 ? -21.039 25.668  10.689  1.00 20.03 ? 147 GLY C N   1 
ATOM   4073 C  CA  . GLY C 1 159 ? -22.046 26.344  9.869   1.00 20.60 ? 147 GLY C CA  1 
ATOM   4074 C  C   . GLY C 1 159 ? -21.561 26.448  8.444   1.00 21.01 ? 147 GLY C C   1 
ATOM   4075 O  O   . GLY C 1 159 ? -20.646 25.703  8.047   1.00 19.15 ? 147 GLY C O   1 
ATOM   4076 N  N   . THR C 1 160 ? -22.158 27.357  7.680   1.00 20.47 ? 148 THR C N   1 
ATOM   4077 C  CA  . THR C 1 160 ? -21.803 27.545  6.264   1.00 20.28 ? 148 THR C CA  1 
ATOM   4078 C  C   . THR C 1 160 ? -20.984 28.832  6.120   1.00 19.71 ? 148 THR C C   1 
ATOM   4079 O  O   . THR C 1 160 ? -21.337 29.870  6.747   1.00 18.77 ? 148 THR C O   1 
ATOM   4080 C  CB  . THR C 1 160 ? -23.076 27.515  5.407   1.00 21.40 ? 148 THR C CB  1 
ATOM   4081 O  OG1 . THR C 1 160 ? -23.628 26.199  5.549   1.00 24.53 ? 148 THR C OG1 1 
ATOM   4082 C  CG2 . THR C 1 160 ? -22.772 27.822  3.958   1.00 21.88 ? 148 THR C CG2 1 
ATOM   4083 N  N   . VAL C 1 161 ? -19.913 28.773  5.325   1.00 17.50 ? 149 VAL C N   1 
ATOM   4084 C  CA  . VAL C 1 161 ? -19.088 29.962  4.981   1.00 17.14 ? 149 VAL C CA  1 
ATOM   4085 C  C   . VAL C 1 161 ? -19.172 30.134  3.469   1.00 17.73 ? 149 VAL C C   1 
ATOM   4086 O  O   . VAL C 1 161 ? -18.692 29.269  2.722   1.00 18.62 ? 149 VAL C O   1 
ATOM   4087 C  CB  . VAL C 1 161 ? -17.617 29.799  5.441   1.00 17.17 ? 149 VAL C CB  1 
ATOM   4088 C  CG1 . VAL C 1 161 ? -16.773 30.943  4.966   1.00 17.15 ? 149 VAL C CG1 1 
ATOM   4089 C  CG2 . VAL C 1 161 ? -17.488 29.608  6.934   1.00 18.82 ? 149 VAL C CG2 1 
ATOM   4090 N  N   . THR C 1 162 ? -19.781 31.222  3.030   1.00 19.08 ? 150 THR C N   1 
ATOM   4091 C  CA  . THR C 1 162 ? -19.959 31.511  1.598   1.00 19.04 ? 150 THR C CA  1 
ATOM   4092 C  C   . THR C 1 162 ? -18.699 32.254  1.190   1.00 16.49 ? 150 THR C C   1 
ATOM   4093 O  O   . THR C 1 162 ? -18.701 33.496  1.345   1.00 18.43 ? 150 THR C O   1 
ATOM   4094 C  CB  . THR C 1 162 ? -21.226 32.318  1.329   1.00 20.19 ? 150 THR C CB  1 
ATOM   4095 O  OG1 . THR C 1 162 ? -22.329 31.579  1.867   1.00 21.93 ? 150 THR C OG1 1 
ATOM   4096 C  CG2 . THR C 1 162 ? -21.390 32.598  -0.143  1.00 21.53 ? 150 THR C CG2 1 
ATOM   4097 N  N   . THR C 1 163 ? -17.654 31.528  0.787   1.00 17.09 ? 151 THR C N   1 
ATOM   4098 C  CA  . THR C 1 163 ? -16.295 32.118  0.696   1.00 17.27 ? 151 THR C CA  1 
ATOM   4099 C  C   . THR C 1 163 ? -16.297 33.252  -0.342  1.00 17.44 ? 151 THR C C   1 
ATOM   4100 O  O   . THR C 1 163 ? -15.575 34.233  -0.127  1.00 15.40 ? 151 THR C O   1 
ATOM   4101 C  CB  . THR C 1 163 ? -15.201 31.083  0.417   1.00 17.70 ? 151 THR C CB  1 
ATOM   4102 O  OG1 . THR C 1 163 ? -15.418 30.473  -0.857  1.00 19.43 ? 151 THR C OG1 1 
ATOM   4103 C  CG2 . THR C 1 163 ? -15.155 30.041  1.504   1.00 18.32 ? 151 THR C CG2 1 
ATOM   4104 N  N   . GLN C 1 164 ? -17.090 33.144  -1.409  1.00 17.86 ? 152 GLN C N   1 
ATOM   4105 C  CA  . GLN C 1 164 ? -17.124 34.207  -2.460  1.00 21.38 ? 152 GLN C CA  1 
ATOM   4106 C  C   . GLN C 1 164 ? -17.489 35.565  -1.833  1.00 19.26 ? 152 GLN C C   1 
ATOM   4107 O  O   . GLN C 1 164 ? -17.003 36.566  -2.344  1.00 19.74 ? 152 GLN C O   1 
ATOM   4108 C  CB  . GLN C 1 164 ? -18.052 33.815  -3.616  1.00 24.06 ? 152 GLN C CB  1 
ATOM   4109 C  CG  . GLN C 1 164 ? -17.949 34.714  -4.835  1.00 29.18 ? 152 GLN C CG  1 
ATOM   4110 C  CD  . GLN C 1 164 ? -16.575 34.767  -5.457  1.00 33.81 ? 152 GLN C CD  1 
ATOM   4111 O  OE1 . GLN C 1 164 ? -16.073 33.782  -5.996  1.00 43.75 ? 152 GLN C OE1 1 
ATOM   4112 N  NE2 . GLN C 1 164 ? -15.965 35.938  -5.432  1.00 37.03 ? 152 GLN C NE2 1 
ATOM   4113 N  N   . ASN C 1 165 ? -18.326 35.617  -0.782  1.00 18.85 ? 153 ASN C N   1 
ATOM   4114 C  CA  . ASN C 1 165 ? -18.768 36.893  -0.171  1.00 18.07 ? 153 ASN C CA  1 
ATOM   4115 C  C   . ASN C 1 165 ? -17.574 37.577  0.486   1.00 20.02 ? 153 ASN C C   1 
ATOM   4116 O  O   . ASN C 1 165 ? -17.520 38.817  0.505   1.00 19.09 ? 153 ASN C O   1 
ATOM   4117 C  CB  . ASN C 1 165 ? -19.943 36.698  0.798   1.00 18.87 ? 153 ASN C CB  1 
ATOM   4118 C  CG  . ASN C 1 165 ? -21.266 36.403  0.126   1.00 20.00 ? 153 ASN C CG  1 
ATOM   4119 O  OD1 . ASN C 1 165 ? -21.464 36.626  -1.079  1.00 22.68 ? 153 ASN C OD1 1 
ATOM   4120 N  ND2 . ASN C 1 165 ? -22.200 35.908  0.922   1.00 21.50 ? 153 ASN C ND2 1 
ATOM   4121 N  N   . HIS C 1 166 ? -16.641 36.785  1.041   1.00 17.72 ? 154 HIS C N   1 
ATOM   4122 C  CA  . HIS C 1 166 ? -15.414 37.321  1.670   1.00 16.66 ? 154 HIS C CA  1 
ATOM   4123 C  C   . HIS C 1 166 ? -14.478 37.826  0.567   1.00 17.93 ? 154 HIS C C   1 
ATOM   4124 O  O   . HIS C 1 166 ? -13.952 38.941  0.691   1.00 18.20 ? 154 HIS C O   1 
ATOM   4125 C  CB  . HIS C 1 166 ? -14.785 36.217  2.534   1.00 15.98 ? 154 HIS C CB  1 
ATOM   4126 C  CG  . HIS C 1 166 ? -15.630 35.892  3.710   1.00 14.74 ? 154 HIS C CG  1 
ATOM   4127 N  ND1 . HIS C 1 166 ? -15.582 36.636  4.896   1.00 15.81 ? 154 HIS C ND1 1 
ATOM   4128 C  CD2 . HIS C 1 166 ? -16.603 34.972  3.888   1.00 17.15 ? 154 HIS C CD2 1 
ATOM   4129 C  CE1 . HIS C 1 166 ? -16.479 36.151  5.730   1.00 14.53 ? 154 HIS C CE1 1 
ATOM   4130 N  NE2 . HIS C 1 166 ? -17.136 35.183  5.143   1.00 15.40 ? 154 HIS C NE2 1 
ATOM   4131 N  N   . PHE C 1 167 ? -14.221 36.993  -0.429  1.00 16.74 ? 155 PHE C N   1 
ATOM   4132 C  CA  . PHE C 1 167 ? -13.353 37.317  -1.586  1.00 17.84 ? 155 PHE C CA  1 
ATOM   4133 C  C   . PHE C 1 167 ? -13.853 38.612  -2.248  1.00 18.49 ? 155 PHE C C   1 
ATOM   4134 O  O   . PHE C 1 167 ? -13.012 39.510  -2.467  1.00 19.62 ? 155 PHE C O   1 
ATOM   4135 C  CB  . PHE C 1 167 ? -13.277 36.137  -2.546  1.00 17.55 ? 155 PHE C CB  1 
ATOM   4136 C  CG  . PHE C 1 167 ? -12.676 34.881  -1.973  1.00 16.79 ? 155 PHE C CG  1 
ATOM   4137 C  CD1 . PHE C 1 167 ? -11.897 34.896  -0.818  1.00 21.03 ? 155 PHE C CD1 1 
ATOM   4138 C  CD2 . PHE C 1 167 ? -12.964 33.667  -2.560  1.00 19.39 ? 155 PHE C CD2 1 
ATOM   4139 C  CE1 . PHE C 1 167 ? -11.357 33.713  -0.311  1.00 22.23 ? 155 PHE C CE1 1 
ATOM   4140 C  CE2 . PHE C 1 167 ? -12.459 32.484  -2.029  1.00 20.33 ? 155 PHE C CE2 1 
ATOM   4141 C  CZ  . PHE C 1 167 ? -11.642 32.507  -0.922  1.00 20.15 ? 155 PHE C CZ  1 
ATOM   4142 N  N   . ASP C 1 168 ? -15.165 38.756  -2.425  1.00 21.08 ? 156 ASP C N   1 
ATOM   4143 C  CA  . ASP C 1 168 ? -15.787 39.961  -3.053  1.00 22.19 ? 156 ASP C CA  1 
ATOM   4144 C  C   . ASP C 1 168 ? -15.631 41.182  -2.150  1.00 21.67 ? 156 ASP C C   1 
ATOM   4145 O  O   . ASP C 1 168 ? -15.366 42.294  -2.722  1.00 23.01 ? 156 ASP C O   1 
ATOM   4146 C  CB  . ASP C 1 168 ? -17.257 39.754  -3.409  1.00 25.08 ? 156 ASP C CB  1 
ATOM   4147 C  CG  . ASP C 1 168 ? -17.442 38.798  -4.573  1.00 29.53 ? 156 ASP C CG  1 
ATOM   4148 O  OD1 . ASP C 1 168 ? -16.448 38.526  -5.272  1.00 32.19 ? 156 ASP C OD1 1 
ATOM   4149 O  OD2 . ASP C 1 168 ? -18.580 38.330  -4.771  1.00 36.73 ? 156 ASP C OD2 1 
ATOM   4150 N  N   . ALA C 1 169 ? -15.795 41.038  -0.824  1.00 18.60 ? 157 ALA C N   1 
ATOM   4151 C  CA  . ALA C 1 169 ? -15.564 42.130  0.157   1.00 20.27 ? 157 ALA C CA  1 
ATOM   4152 C  C   . ALA C 1 169 ? -14.106 42.601  0.079   1.00 19.69 ? 157 ALA C C   1 
ATOM   4153 O  O   . ALA C 1 169 ? -13.859 43.825  0.029   1.00 20.68 ? 157 ALA C O   1 
ATOM   4154 C  CB  . ALA C 1 169 ? -15.937 41.693  1.548   1.00 20.55 ? 157 ALA C CB  1 
ATOM   4155 N  N   . TRP C 1 170 ? -13.146 41.672  0.034   1.00 21.05 ? 158 TRP C N   1 
ATOM   4156 C  CA  . TRP C 1 170 ? -11.707 42.027  -0.058  1.00 19.90 ? 158 TRP C CA  1 
ATOM   4157 C  C   . TRP C 1 170 ? -11.444 42.762  -1.388  1.00 21.59 ? 158 TRP C C   1 
ATOM   4158 O  O   . TRP C 1 170 ? -10.781 43.802  -1.365  1.00 21.15 ? 158 TRP C O   1 
ATOM   4159 C  CB  . TRP C 1 170 ? -10.842 40.785  0.072   1.00 21.91 ? 158 TRP C CB  1 
ATOM   4160 C  CG  . TRP C 1 170 ? -10.971 40.130  1.414   1.00 21.63 ? 158 TRP C CG  1 
ATOM   4161 C  CD1 . TRP C 1 170 ? -11.398 40.700  2.574   1.00 26.85 ? 158 TRP C CD1 1 
ATOM   4162 C  CD2 . TRP C 1 170 ? -10.664 38.768  1.737   1.00 20.64 ? 158 TRP C CD2 1 
ATOM   4163 N  NE1 . TRP C 1 170 ? -11.369 39.790  3.601   1.00 26.93 ? 158 TRP C NE1 1 
ATOM   4164 C  CE2 . TRP C 1 170 ? -10.924 38.593  3.115   1.00 23.31 ? 158 TRP C CE2 1 
ATOM   4165 C  CE3 . TRP C 1 170 ? -10.201 37.689  0.995   1.00 20.85 ? 158 TRP C CE3 1 
ATOM   4166 C  CZ2 . TRP C 1 170 ? -10.715 37.377  3.773   1.00 21.22 ? 158 TRP C CZ2 1 
ATOM   4167 C  CZ3 . TRP C 1 170 ? -10.026 36.481  1.630   1.00 20.53 ? 158 TRP C CZ3 1 
ATOM   4168 C  CH2 . TRP C 1 170 ? -10.262 36.340  2.996   1.00 21.67 ? 158 TRP C CH2 1 
ATOM   4169 N  N   . LYS C 1 171 ? -12.017 42.272  -2.487  1.00 21.37 ? 159 LYS C N   1 
ATOM   4170 C  CA  . LYS C 1 171 ? -11.794 42.879  -3.835  1.00 24.38 ? 159 LYS C CA  1 
ATOM   4171 C  C   . LYS C 1 171 ? -12.341 44.318  -3.805  1.00 22.49 ? 159 LYS C C   1 
ATOM   4172 O  O   . LYS C 1 171 ? -11.715 45.221  -4.378  1.00 21.14 ? 159 LYS C O   1 
ATOM   4173 C  CB  . LYS C 1 171 ? -12.517 42.061  -4.900  1.00 26.72 ? 159 LYS C CB  1 
ATOM   4174 C  CG  . LYS C 1 171 ? -12.000 42.194  -6.324  1.00 34.20 ? 159 LYS C CG  1 
ATOM   4175 C  CD  . LYS C 1 171 ? -12.748 41.262  -7.265  1.00 36.01 ? 159 LYS C CD  1 
ATOM   4176 C  CE  . LYS C 1 171 ? -11.976 40.937  -8.525  1.00 43.83 ? 159 LYS C CE  1 
ATOM   4177 N  NZ  . LYS C 1 171 ? -12.518 39.732  -9.186  1.00 44.28 ? 159 LYS C NZ  1 
ATOM   4178 N  N   . ASN C 1 172 ? -13.489 44.498  -3.154  1.00 23.78 ? 160 ASN C N   1 
ATOM   4179 C  CA  . ASN C 1 172 ? -14.263 45.756  -3.089  1.00 26.26 ? 160 ASN C CA  1 
ATOM   4180 C  C   . ASN C 1 172 ? -13.475 46.771  -2.263  1.00 25.34 ? 160 ASN C C   1 
ATOM   4181 O  O   . ASN C 1 172 ? -13.509 47.963  -2.617  1.00 26.11 ? 160 ASN C O   1 
ATOM   4182 C  CB  . ASN C 1 172 ? -15.707 45.498  -2.662  1.00 29.90 ? 160 ASN C CB  1 
ATOM   4183 C  CG  . ASN C 1 172 ? -16.541 44.975  -3.817  1.00 39.56 ? 160 ASN C CG  1 
ATOM   4184 O  OD1 . ASN C 1 172 ? -16.274 45.289  -4.985  1.00 44.27 ? 160 ASN C OD1 1 
ATOM   4185 N  ND2 . ASN C 1 172 ? -17.575 44.205  -3.511  1.00 43.46 ? 160 ASN C ND2 1 
ATOM   4186 N  N   . ALA C 1 173 ? -12.697 46.319  -1.284  1.00 19.52 ? 161 ALA C N   1 
ATOM   4187 C  CA  . ALA C 1 173 ? -11.845 47.183  -0.453  1.00 23.32 ? 161 ALA C CA  1 
ATOM   4188 C  C   . ALA C 1 173 ? -10.545 47.442  -1.217  1.00 24.08 ? 161 ALA C C   1 
ATOM   4189 O  O   . ALA C 1 173 ? -9.677  48.082  -0.677  1.00 30.08 ? 161 ALA C O   1 
ATOM   4190 C  CB  . ALA C 1 173 ? -11.600 46.526  0.885   1.00 24.97 ? 161 ALA C CB  1 
ATOM   4191 N  N   . GLY C 1 174 ? -10.389 46.846  -2.401  1.00 24.33 ? 162 GLY C N   1 
ATOM   4192 C  CA  . GLY C 1 174 ? -9.268  47.128  -3.309  1.00 24.69 ? 162 GLY C CA  1 
ATOM   4193 C  C   . GLY C 1 174 ? -8.137  46.117  -3.220  1.00 28.45 ? 162 GLY C C   1 
ATOM   4194 O  O   . GLY C 1 174 ? -7.108  46.361  -3.898  1.00 29.75 ? 162 GLY C O   1 
ATOM   4195 N  N   . LEU C 1 175 ? -8.330  44.991  -2.496  1.00 25.29 ? 163 LEU C N   1 
ATOM   4196 C  CA  . LEU C 1 175 ? -7.291  43.953  -2.259  1.00 24.07 ? 163 LEU C CA  1 
ATOM   4197 C  C   . LEU C 1 175 ? -7.260  42.995  -3.459  1.00 24.93 ? 163 LEU C C   1 
ATOM   4198 O  O   . LEU C 1 175 ? -8.329  42.479  -3.890  1.00 26.28 ? 163 LEU C O   1 
ATOM   4199 C  CB  . LEU C 1 175 ? -7.580  43.195  -0.952  1.00 24.45 ? 163 LEU C CB  1 
ATOM   4200 C  CG  . LEU C 1 175 ? -7.757  44.087  0.277   1.00 24.39 ? 163 LEU C CG  1 
ATOM   4201 C  CD1 . LEU C 1 175 ? -8.183  43.293  1.513   1.00 24.82 ? 163 LEU C CD1 1 
ATOM   4202 C  CD2 . LEU C 1 175 ? -6.484  44.847  0.566   1.00 24.80 ? 163 LEU C CD2 1 
ATOM   4203 N  N   . GLU C 1 176 ? -6.063  42.752  -3.947  1.00 24.54 ? 164 GLU C N   1 
ATOM   4204 C  CA  . GLU C 1 176 ? -5.783  41.885  -5.116  1.00 27.60 ? 164 GLU C CA  1 
ATOM   4205 C  C   . GLU C 1 176 ? -5.660  40.433  -4.641  1.00 25.33 ? 164 GLU C C   1 
ATOM   4206 O  O   . GLU C 1 176 ? -4.982  40.223  -3.643  1.00 25.45 ? 164 GLU C O   1 
ATOM   4207 C  CB  . GLU C 1 176 ? -4.482  42.347  -5.762  1.00 32.64 ? 164 GLU C CB  1 
ATOM   4208 C  CG  . GLU C 1 176 ? -4.591  43.739  -6.359  1.00 39.71 ? 164 GLU C CG  1 
ATOM   4209 C  CD  . GLU C 1 176 ? -4.719  43.738  -7.869  1.00 45.95 ? 164 GLU C CD  1 
ATOM   4210 O  OE1 . GLU C 1 176 ? -3.840  43.128  -8.509  1.00 50.59 ? 164 GLU C OE1 1 
ATOM   4211 O  OE2 . GLU C 1 176 ? -5.699  44.330  -8.397  1.00 49.18 ? 164 GLU C OE2 1 
ATOM   4212 N  N   . MET C 1 177 ? -6.325  39.504  -5.328  1.00 23.91 ? 165 MET C N   1 
ATOM   4213 C  CA  . MET C 1 177 ? -6.204  38.039  -5.093  1.00 26.11 ? 165 MET C CA  1 
ATOM   4214 C  C   . MET C 1 177 ? -5.596  37.424  -6.359  1.00 24.66 ? 165 MET C C   1 
ATOM   4215 O  O   . MET C 1 177 ? -5.882  37.925  -7.450  1.00 24.65 ? 165 MET C O   1 
ATOM   4216 C  CB  . MET C 1 177 ? -7.560  37.380  -4.822  1.00 28.59 ? 165 MET C CB  1 
ATOM   4217 C  CG  . MET C 1 177 ? -8.282  37.909  -3.614  1.00 32.95 ? 165 MET C CG  1 
ATOM   4218 S  SD  . MET C 1 177 ? -7.671  37.143  -2.118  1.00 41.53 ? 165 MET C SD  1 
ATOM   4219 C  CE  . MET C 1 177 ? -8.482  35.547  -2.124  1.00 36.38 ? 165 MET C CE  1 
ATOM   4220 N  N   . GLY C 1 178 ? -4.787  36.384  -6.202  1.00 20.77 ? 166 GLY C N   1 
ATOM   4221 C  CA  . GLY C 1 178 ? -4.162  35.636  -7.300  1.00 19.81 ? 166 GLY C CA  1 
ATOM   4222 C  C   . GLY C 1 178 ? -4.955  34.384  -7.653  1.00 18.57 ? 166 GLY C C   1 
ATOM   4223 O  O   . GLY C 1 178 ? -6.196  34.349  -7.395  1.00 20.24 ? 166 GLY C O   1 
ATOM   4224 N  N   . THR C 1 179 ? -4.297  33.430  -8.295  1.00 17.96 ? 167 THR C N   1 
ATOM   4225 C  CA  . THR C 1 179 ? -4.842  32.104  -8.642  1.00 18.64 ? 167 THR C CA  1 
ATOM   4226 C  C   . THR C 1 179 ? -4.965  31.305  -7.350  1.00 16.39 ? 167 THR C C   1 
ATOM   4227 O  O   . THR C 1 179 ? -3.991  31.246  -6.586  1.00 14.94 ? 167 THR C O   1 
ATOM   4228 C  CB  . THR C 1 179 ? -3.966  31.404  -9.695  1.00 21.05 ? 167 THR C CB  1 
ATOM   4229 O  OG1 . THR C 1 179 ? -3.855  32.326  -10.777 1.00 23.64 ? 167 THR C OG1 1 
ATOM   4230 C  CG2 . THR C 1 179 ? -4.557  30.100  -10.186 1.00 23.06 ? 167 THR C CG2 1 
ATOM   4231 N  N   . HIS C 1 180 ? -6.118  30.680  -7.126  1.00 17.96 ? 168 HIS C N   1 
ATOM   4232 C  CA  . HIS C 1 180 ? -6.356  29.958  -5.856  1.00 18.13 ? 168 HIS C CA  1 
ATOM   4233 C  C   . HIS C 1 180 ? -5.509  28.701  -5.811  1.00 16.46 ? 168 HIS C C   1 
ATOM   4234 O  O   . HIS C 1 180 ? -5.523  27.897  -6.826  1.00 16.52 ? 168 HIS C O   1 
ATOM   4235 C  CB  . HIS C 1 180 ? -7.865  29.701  -5.656  1.00 20.03 ? 168 HIS C CB  1 
ATOM   4236 C  CG  . HIS C 1 180 ? -8.534  30.858  -4.998  1.00 24.79 ? 168 HIS C CG  1 
ATOM   4237 N  ND1 . HIS C 1 180 ? -9.086  31.909  -5.715  1.00 30.56 ? 168 HIS C ND1 1 
ATOM   4238 C  CD2 . HIS C 1 180 ? -8.700  31.161  -3.696  1.00 25.59 ? 168 HIS C CD2 1 
ATOM   4239 C  CE1 . HIS C 1 180 ? -9.600  32.787  -4.882  1.00 29.30 ? 168 HIS C CE1 1 
ATOM   4240 N  NE2 . HIS C 1 180 ? -9.390  32.340  -3.633  1.00 34.20 ? 168 HIS C NE2 1 
ATOM   4241 N  N   . ASN C 1 181 ? -4.820  28.516  -4.689  1.00 14.19 ? 169 ASN C N   1 
ATOM   4242 C  CA  . ASN C 1 181 ? -4.193  27.227  -4.321  1.00 14.74 ? 169 ASN C CA  1 
ATOM   4243 C  C   . ASN C 1 181 ? -5.141  26.617  -3.281  1.00 14.14 ? 169 ASN C C   1 
ATOM   4244 O  O   . ASN C 1 181 ? -6.366  26.751  -3.452  1.00 16.27 ? 169 ASN C O   1 
ATOM   4245 C  CB  . ASN C 1 181 ? -2.743  27.456  -3.867  1.00 16.14 ? 169 ASN C CB  1 
ATOM   4246 C  CG  . ASN C 1 181 ? -1.917  26.190  -3.883  1.00 18.93 ? 169 ASN C CG  1 
ATOM   4247 O  OD1 . ASN C 1 181 ? -1.995  25.400  -2.940  1.00 19.42 ? 169 ASN C OD1 1 
ATOM   4248 N  ND2 . ASN C 1 181 ? -1.187  25.939  -4.976  1.00 20.20 ? 169 ASN C ND2 1 
ATOM   4249 N  N   . TYR C 1 182 ? -4.627  25.956  -2.255  1.00 13.03 ? 170 TYR C N   1 
ATOM   4250 C  CA  . TYR C 1 182 ? -5.525  25.168  -1.381  1.00 11.98 ? 170 TYR C CA  1 
ATOM   4251 C  C   . TYR C 1 182 ? -6.365  26.098  -0.508  1.00 12.53 ? 170 TYR C C   1 
ATOM   4252 O  O   . TYR C 1 182 ? -6.077  27.282  -0.308  1.00 12.59 ? 170 TYR C O   1 
ATOM   4253 C  CB  . TYR C 1 182 ? -4.771  24.181  -0.502  1.00 12.58 ? 170 TYR C CB  1 
ATOM   4254 C  CG  . TYR C 1 182 ? -3.842  24.705  0.566   1.00 13.32 ? 170 TYR C CG  1 
ATOM   4255 C  CD1 . TYR C 1 182 ? -4.343  25.184  1.756   1.00 13.69 ? 170 TYR C CD1 1 
ATOM   4256 C  CD2 . TYR C 1 182 ? -2.455  24.691  0.396   1.00 14.89 ? 170 TYR C CD2 1 
ATOM   4257 C  CE1 . TYR C 1 182 ? -3.489  25.583  2.770   1.00 14.67 ? 170 TYR C CE1 1 
ATOM   4258 C  CE2 . TYR C 1 182 ? -1.597  25.051  1.422   1.00 16.21 ? 170 TYR C CE2 1 
ATOM   4259 C  CZ  . TYR C 1 182 ? -2.121  25.539  2.603   1.00 16.91 ? 170 TYR C CZ  1 
ATOM   4260 O  OH  . TYR C 1 182 ? -1.331  25.929  3.654   1.00 17.83 ? 170 TYR C OH  1 
ATOM   4261 N  N   . MET C 1 183 ? -7.424  25.510  0.041   1.00 12.03 ? 171 MET C N   1 
ATOM   4262 C  CA  . MET C 1 183 ? -8.325  26.205  0.992   1.00 12.98 ? 171 MET C CA  1 
ATOM   4263 C  C   . MET C 1 183 ? -8.764  25.131  1.976   1.00 11.35 ? 171 MET C C   1 
ATOM   4264 O  O   . MET C 1 183 ? -9.211  24.062  1.497   1.00 12.19 ? 171 MET C O   1 
ATOM   4265 C  CB  . MET C 1 183 ? -9.554  26.790  0.293   1.00 13.86 ? 171 MET C CB  1 
ATOM   4266 C  CG  . MET C 1 183 ? -10.504 27.530  1.222   1.00 16.50 ? 171 MET C CG  1 
ATOM   4267 S  SD  . MET C 1 183 ? -11.833 28.413  0.381   1.00 20.38 ? 171 MET C SD  1 
ATOM   4268 C  CE  . MET C 1 183 ? -12.740 27.028  -0.289  1.00 21.40 ? 171 MET C CE  1 
ATOM   4269 N  N   . ILE C 1 184 ? -8.584  25.353  3.270   1.00 10.97 ? 172 ILE C N   1 
ATOM   4270 C  CA  . ILE C 1 184 ? -8.907  24.321  4.292   1.00 11.56 ? 172 ILE C CA  1 
ATOM   4271 C  C   . ILE C 1 184 ? -9.748  24.956  5.394   1.00 11.32 ? 172 ILE C C   1 
ATOM   4272 O  O   . ILE C 1 184 ? -9.734  26.211  5.530   1.00 11.90 ? 172 ILE C O   1 
ATOM   4273 C  CB  . ILE C 1 184 ? -7.642  23.666  4.891   1.00 12.59 ? 172 ILE C CB  1 
ATOM   4274 C  CG1 . ILE C 1 184 ? -6.685  24.644  5.552   1.00 13.58 ? 172 ILE C CG1 1 
ATOM   4275 C  CG2 . ILE C 1 184 ? -6.925  22.835  3.865   1.00 11.63 ? 172 ILE C CG2 1 
ATOM   4276 C  CD1 . ILE C 1 184 ? -5.535  23.975  6.245   1.00 14.90 ? 172 ILE C CD1 1 
ATOM   4277 N  N   . VAL C 1 185 ? -10.458 24.113  6.161   1.00 10.66 ? 173 VAL C N   1 
ATOM   4278 C  CA  . VAL C 1 185 ? -11.008 24.574  7.454   1.00 11.20 ? 173 VAL C CA  1 
ATOM   4279 C  C   . VAL C 1 185 ? -9.977  24.243  8.518   1.00 11.65 ? 173 VAL C C   1 
ATOM   4280 O  O   . VAL C 1 185 ? -9.773  23.051  8.790   1.00 12.32 ? 173 VAL C O   1 
ATOM   4281 C  CB  . VAL C 1 185 ? -12.397 24.012  7.760   1.00 12.02 ? 173 VAL C CB  1 
ATOM   4282 C  CG1 . VAL C 1 185 ? -12.901 24.610  9.052   1.00 13.07 ? 173 VAL C CG1 1 
ATOM   4283 C  CG2 . VAL C 1 185 ? -13.345 24.245  6.581   1.00 13.81 ? 173 VAL C CG2 1 
ATOM   4284 N  N   . ALA C 1 186 ? -9.311  25.262  9.039   1.00 11.35 ? 174 ALA C N   1 
ATOM   4285 C  CA  . ALA C 1 186 ? -8.090  25.093  9.838   1.00 11.28 ? 174 ALA C CA  1 
ATOM   4286 C  C   . ALA C 1 186 ? -8.328  25.370  11.323  1.00 11.65 ? 174 ALA C C   1 
ATOM   4287 O  O   . ALA C 1 186 ? -9.007  26.334  11.688  1.00 14.12 ? 174 ALA C O   1 
ATOM   4288 C  CB  . ALA C 1 186 ? -6.989  25.943  9.321   1.00 12.13 ? 174 ALA C CB  1 
ATOM   4289 N  N   . THR C 1 187 ? -7.631  24.597  12.142  1.00 12.43 ? 175 THR C N   1 
ATOM   4290 C  CA  . THR C 1 187 ? -7.412  24.862  13.569  1.00 12.61 ? 175 THR C CA  1 
ATOM   4291 C  C   . THR C 1 187 ? -5.973  25.351  13.723  1.00 12.09 ? 175 THR C C   1 
ATOM   4292 O  O   . THR C 1 187 ? -5.086  24.715  13.197  1.00 11.86 ? 175 THR C O   1 
ATOM   4293 C  CB  . THR C 1 187 ? -7.682  23.599  14.384  1.00 13.73 ? 175 THR C CB  1 
ATOM   4294 O  OG1 . THR C 1 187 ? -9.035  23.176  14.181  1.00 13.68 ? 175 THR C OG1 1 
ATOM   4295 C  CG2 . THR C 1 187 ? -7.479  23.824  15.862  1.00 14.43 ? 175 THR C CG2 1 
ATOM   4296 N  N   . ALA C 1 188 ? -5.773  26.490  14.369  1.00 12.01 ? 176 ALA C N   1 
ATOM   4297 C  CA  . ALA C 1 188 ? -4.429  27.066  14.574  1.00 12.50 ? 176 ALA C CA  1 
ATOM   4298 C  C   . ALA C 1 188 ? -4.255  27.299  16.072  1.00 13.30 ? 176 ALA C C   1 
ATOM   4299 O  O   . ALA C 1 188 ? -5.238  27.596  16.799  1.00 13.68 ? 176 ALA C O   1 
ATOM   4300 C  CB  . ALA C 1 188 ? -4.315  28.352  13.804  1.00 12.51 ? 176 ALA C CB  1 
ATOM   4301 N  N   . GLY C 1 189 ? -3.016  27.295  16.512  1.00 14.59 ? 177 GLY C N   1 
ATOM   4302 C  CA  . GLY C 1 189 ? -2.726  27.526  17.932  1.00 15.59 ? 177 GLY C CA  1 
ATOM   4303 C  C   . GLY C 1 189 ? -1.340  28.077  18.066  1.00 16.92 ? 177 GLY C C   1 
ATOM   4304 O  O   . GLY C 1 189 ? -0.506  27.841  17.148  1.00 17.65 ? 177 GLY C O   1 
ATOM   4305 N  N   . TYR C 1 190 ? -1.093  28.844  19.120  1.00 17.12 ? 178 TYR C N   1 
ATOM   4306 C  CA  . TYR C 1 190 ? 0.275   29.327  19.424  1.00 18.06 ? 178 TYR C CA  1 
ATOM   4307 C  C   . TYR C 1 190 ? 0.393   29.415  20.934  1.00 19.86 ? 178 TYR C C   1 
ATOM   4308 O  O   . TYR C 1 190 ? -0.484  30.089  21.550  1.00 18.35 ? 178 TYR C O   1 
ATOM   4309 C  CB  . TYR C 1 190 ? 0.615   30.663  18.777  1.00 22.91 ? 178 TYR C CB  1 
ATOM   4310 C  CG  . TYR C 1 190 ? 2.022   31.131  19.088  1.00 29.18 ? 178 TYR C CG  1 
ATOM   4311 C  CD1 . TYR C 1 190 ? 3.125   30.670  18.381  1.00 30.65 ? 178 TYR C CD1 1 
ATOM   4312 C  CD2 . TYR C 1 190 ? 2.265   31.984  20.153  1.00 27.18 ? 178 TYR C CD2 1 
ATOM   4313 C  CE1 . TYR C 1 190 ? 4.417   31.092  18.682  1.00 32.49 ? 178 TYR C CE1 1 
ATOM   4314 C  CE2 . TYR C 1 190 ? 3.540   32.412  20.469  1.00 31.88 ? 178 TYR C CE2 1 
ATOM   4315 C  CZ  . TYR C 1 190 ? 4.623   31.985  19.721  1.00 33.00 ? 178 TYR C CZ  1 
ATOM   4316 O  OH  . TYR C 1 190 ? 5.871   32.429  20.065  1.00 36.39 ? 178 TYR C OH  1 
ATOM   4317 N  N   . GLN C 1 191 ? 1.424   28.768  21.479  1.00 19.30 ? 179 GLN C N   1 
ATOM   4318 C  CA  . GLN C 1 191 ? 1.788   28.790  22.924  1.00 19.92 ? 179 GLN C CA  1 
ATOM   4319 C  C   . GLN C 1 191 ? 0.509   28.584  23.731  1.00 19.51 ? 179 GLN C C   1 
ATOM   4320 O  O   . GLN C 1 191 ? 0.148   29.413  24.596  1.00 18.49 ? 179 GLN C O   1 
ATOM   4321 C  CB  . GLN C 1 191 ? 2.607   30.044  23.239  1.00 22.96 ? 179 GLN C CB  1 
ATOM   4322 C  CG  . GLN C 1 191 ? 4.019   29.937  22.679  1.00 25.94 ? 179 GLN C CG  1 
ATOM   4323 C  CD  . GLN C 1 191 ? 5.020   30.942  23.207  1.00 31.01 ? 179 GLN C CD  1 
ATOM   4324 O  OE1 . GLN C 1 191 ? 4.672   31.949  23.821  1.00 34.27 ? 179 GLN C OE1 1 
ATOM   4325 N  NE2 . GLN C 1 191 ? 6.285   30.692  22.914  1.00 35.65 ? 179 GLN C NE2 1 
ATOM   4326 N  N   . SER C 1 192 ? -0.165  27.479  23.445  1.00 17.79 ? 180 SER C N   1 
ATOM   4327 C  CA  . SER C 1 192 ? -1.440  27.094  24.094  1.00 17.44 ? 180 SER C CA  1 
ATOM   4328 C  C   . SER C 1 192 ? -1.558  25.557  24.193  1.00 18.02 ? 180 SER C C   1 
ATOM   4329 O  O   . SER C 1 192 ? -0.647  24.832  23.767  1.00 18.11 ? 180 SER C O   1 
ATOM   4330 C  CB  . SER C 1 192 ? -2.582  27.733  23.379  1.00 18.00 ? 180 SER C CB  1 
ATOM   4331 O  OG  . SER C 1 192 ? -2.712  27.194  22.061  1.00 15.43 ? 180 SER C OG  1 
ATOM   4332 N  N   . SER C 1 193 ? -2.670  25.084  24.731  1.00 17.70 ? 181 SER C N   1 
ATOM   4333 C  CA  . SER C 1 193 ? -3.082  23.662  24.756  1.00 18.09 ? 181 SER C CA  1 
ATOM   4334 C  C   . SER C 1 193 ? -4.513  23.613  24.246  1.00 17.21 ? 181 SER C C   1 
ATOM   4335 O  O   . SER C 1 193 ? -5.179  24.666  24.185  1.00 16.52 ? 181 SER C O   1 
ATOM   4336 C  CB  . SER C 1 193 ? -2.986  23.105  26.161  1.00 21.07 ? 181 SER C CB  1 
ATOM   4337 O  OG  . SER C 1 193 ? -1.634  23.223  26.615  1.00 23.98 ? 181 SER C OG  1 
ATOM   4338 N  N   . GLY C 1 194 ? -4.964  22.442  23.831  1.00 16.41 ? 182 GLY C N   1 
ATOM   4339 C  CA  . GLY C 1 194 ? -6.310  22.352  23.281  1.00 15.31 ? 182 GLY C CA  1 
ATOM   4340 C  C   . GLY C 1 194 ? -6.541  21.034  22.616  1.00 15.72 ? 182 GLY C C   1 
ATOM   4341 O  O   . GLY C 1 194 ? -5.591  20.227  22.476  1.00 16.56 ? 182 GLY C O   1 
ATOM   4342 N  N   . SER C 1 195 ? -7.775  20.886  22.166  1.00 16.85 ? 183 SER C N   1 
ATOM   4343 C  CA  . SER C 1 195 ? -8.179  19.803  21.249  1.00 17.52 ? 183 SER C CA  1 
ATOM   4344 C  C   . SER C 1 195 ? -9.252  20.365  20.313  1.00 18.28 ? 183 SER C C   1 
ATOM   4345 O  O   . SER C 1 195 ? -9.970  21.343  20.656  1.00 17.89 ? 183 SER C O   1 
ATOM   4346 C  CB  . SER C 1 195 ? -8.660  18.593  22.020  1.00 18.36 ? 183 SER C CB  1 
ATOM   4347 O  OG  . SER C 1 195 ? -9.868  18.891  22.690  1.00 18.69 ? 183 SER C OG  1 
ATOM   4348 N  N   . ALA C 1 196 ? -9.344  19.785  19.137  1.00 16.40 ? 184 ALA C N   1 
ATOM   4349 C  CA  . ALA C 1 196 ? -10.432 20.089  18.205  1.00 15.01 ? 184 ALA C CA  1 
ATOM   4350 C  C   . ALA C 1 196 ? -10.660 18.835  17.383  1.00 15.71 ? 184 ALA C C   1 
ATOM   4351 O  O   . ALA C 1 196 ? -9.741  18.027  17.164  1.00 15.47 ? 184 ALA C O   1 
ATOM   4352 C  CB  . ALA C 1 196 ? -10.129 21.294  17.335  1.00 15.77 ? 184 ALA C CB  1 
ATOM   4353 N  N   . SER C 1 197 ? -11.894 18.677  16.991  1.00 15.35 ? 185 SER C N   1 
ATOM   4354 C  CA  . SER C 1 197 ? -12.310 17.623  16.050  1.00 18.66 ? 185 SER C CA  1 
ATOM   4355 C  C   . SER C 1 197 ? -13.272 18.273  15.062  1.00 16.75 ? 185 SER C C   1 
ATOM   4356 O  O   . SER C 1 197 ? -14.420 18.717  15.476  1.00 16.74 ? 185 SER C O   1 
ATOM   4357 C  CB  . SER C 1 197 ? -12.903 16.450  16.789  1.00 22.20 ? 185 SER C CB  1 
ATOM   4358 O  OG  . SER C 1 197 ? -13.159 15.383  15.882  1.00 30.34 ? 185 SER C OG  1 
ATOM   4359 N  N   . ILE C 1 198 ? -12.855 18.386  13.811  1.00 14.86 ? 186 ILE C N   1 
ATOM   4360 C  CA  . ILE C 1 198 ? -13.609 19.145  12.782  1.00 15.38 ? 186 ILE C CA  1 
ATOM   4361 C  C   . ILE C 1 198 ? -13.943 18.252  11.597  1.00 16.70 ? 186 ILE C C   1 
ATOM   4362 O  O   . ILE C 1 198 ? -13.048 17.540  11.134  1.00 16.02 ? 186 ILE C O   1 
ATOM   4363 C  CB  . ILE C 1 198 ? -12.738 20.352  12.372  1.00 16.24 ? 186 ILE C CB  1 
ATOM   4364 C  CG1 . ILE C 1 198 ? -12.514 21.289  13.570  1.00 18.40 ? 186 ILE C CG1 1 
ATOM   4365 C  CG2 . ILE C 1 198 ? -13.362 21.061  11.191  1.00 17.13 ? 186 ILE C CG2 1 
ATOM   4366 C  CD1 . ILE C 1 198 ? -13.787 21.905  14.098  1.00 20.88 ? 186 ILE C CD1 1 
ATOM   4367 N  N   . THR C 1 199 ? -15.181 18.294  11.095  1.00 17.41 ? 187 THR C N   1 
ATOM   4368 C  CA  . THR C 1 199 ? -15.594 17.557  9.876   1.00 18.98 ? 187 THR C CA  1 
ATOM   4369 C  C   . THR C 1 199 ? -16.041 18.562  8.815   1.00 18.13 ? 187 THR C C   1 
ATOM   4370 O  O   . THR C 1 199 ? -16.952 19.363  9.059   1.00 16.83 ? 187 THR C O   1 
ATOM   4371 C  CB  . THR C 1 199 ? -16.693 16.529  10.179  1.00 20.50 ? 187 THR C CB  1 
ATOM   4372 O  OG1 . THR C 1 199 ? -16.190 15.657  11.198  1.00 20.86 ? 187 THR C OG1 1 
ATOM   4373 C  CG2 . THR C 1 199 ? -17.094 15.754  8.940   1.00 21.52 ? 187 THR C CG2 1 
ATOM   4374 N  N   . VAL C 1 200 ? -15.349 18.569  7.682   1.00 16.19 ? 188 VAL C N   1 
ATOM   4375 C  CA  . VAL C 1 200 ? -15.668 19.446  6.539   1.00 18.18 ? 188 VAL C CA  1 
ATOM   4376 C  C   . VAL C 1 200 ? -16.591 18.615  5.645   1.00 21.19 ? 188 VAL C C   1 
ATOM   4377 O  O   . VAL C 1 200 ? -16.406 17.396  5.610   1.00 20.72 ? 188 VAL C O   1 
ATOM   4378 C  CB  . VAL C 1 200 ? -14.369 19.887  5.865   1.00 20.50 ? 188 VAL C CB  1 
ATOM   4379 C  CG1 . VAL C 1 200 ? -14.621 20.679  4.626   1.00 23.80 ? 188 VAL C CG1 1 
ATOM   4380 C  CG2 . VAL C 1 200 ? -13.496 20.679  6.841   1.00 23.29 ? 188 VAL C CG2 1 
ATOM   4381 N  N   . GLN C 1 201 ? -17.582 19.230  5.021   1.00 26.23 ? 189 GLN C N   1 
ATOM   4382 C  CA  . GLN C 1 201 ? -18.475 18.524  4.064   1.00 29.64 ? 189 GLN C CA  1 
ATOM   4383 C  C   . GLN C 1 201 ? -17.866 18.629  2.664   1.00 32.47 ? 189 GLN C C   1 
ATOM   4384 O  O   . GLN C 1 201 ? -17.445 19.640  2.107   1.00 35.61 ? 189 GLN C O   1 
ATOM   4385 C  CB  . GLN C 1 201 ? -19.897 19.058  4.226   1.00 32.29 ? 189 GLN C CB  1 
ATOM   4386 C  CG  . GLN C 1 201 ? -20.486 18.623  5.559   1.00 36.08 ? 189 GLN C CG  1 
ATOM   4387 C  CD  . GLN C 1 201 ? -21.519 19.556  6.153   1.00 42.43 ? 189 GLN C CD  1 
ATOM   4388 O  OE1 . GLN C 1 201 ? -22.500 19.929  5.508   1.00 46.34 ? 189 GLN C OE1 1 
ATOM   4389 N  NE2 . GLN C 1 201 ? -21.327 19.900  7.418   1.00 45.71 ? 189 GLN C NE2 1 
ATOM   4390 N  N   . GLU D 1 13  ? -0.952  54.786  33.557  1.00 43.52 ? 1   GLU D N   1 
ATOM   4391 C  CA  . GLU D 1 13  ? 0.083   55.819  33.778  1.00 37.89 ? 1   GLU D CA  1 
ATOM   4392 C  C   . GLU D 1 13  ? 1.063   55.816  32.591  1.00 34.25 ? 1   GLU D C   1 
ATOM   4393 O  O   . GLU D 1 13  ? 1.194   56.880  31.954  1.00 32.64 ? 1   GLU D O   1 
ATOM   4394 C  CB  . GLU D 1 13  ? 0.769   55.621  35.136  1.00 42.64 ? 1   GLU D CB  1 
ATOM   4395 C  CG  . GLU D 1 13  ? 1.433   56.869  35.670  1.00 44.70 ? 1   GLU D CG  1 
ATOM   4396 C  CD  . GLU D 1 13  ? 0.561   57.815  36.483  1.00 47.48 ? 1   GLU D CD  1 
ATOM   4397 O  OE1 . GLU D 1 13  ? 0.119   57.430  37.607  1.00 46.98 ? 1   GLU D OE1 1 
ATOM   4398 O  OE2 . GLU D 1 13  ? 0.348   58.947  36.007  1.00 50.01 ? 1   GLU D OE2 1 
ATOM   4399 N  N   . ILE D 1 14  ? 1.720   54.702  32.257  1.00 31.05 ? 2   ILE D N   1 
ATOM   4400 C  CA  . ILE D 1 14  ? 2.711   54.683  31.134  1.00 31.10 ? 2   ILE D CA  1 
ATOM   4401 C  C   . ILE D 1 14  ? 2.502   53.463  30.227  1.00 29.91 ? 2   ILE D C   1 
ATOM   4402 O  O   . ILE D 1 14  ? 2.118   52.374  30.748  1.00 25.88 ? 2   ILE D O   1 
ATOM   4403 C  CB  . ILE D 1 14  ? 4.153   54.738  31.661  1.00 30.47 ? 2   ILE D CB  1 
ATOM   4404 C  CG1 . ILE D 1 14  ? 4.529   53.464  32.417  1.00 29.09 ? 2   ILE D CG1 1 
ATOM   4405 C  CG2 . ILE D 1 14  ? 4.391   55.989  32.497  1.00 33.76 ? 2   ILE D CG2 1 
ATOM   4406 C  CD1 . ILE D 1 14  ? 6.011   53.281  32.570  1.00 29.51 ? 2   ILE D CD1 1 
ATOM   4407 N  N   . THR D 1 15  ? 2.793   53.623  28.928  1.00 25.99 ? 3   THR D N   1 
ATOM   4408 C  CA  . THR D 1 15  ? 2.459   52.639  27.872  1.00 27.95 ? 3   THR D CA  1 
ATOM   4409 C  C   . THR D 1 15  ? 3.703   52.279  27.053  1.00 24.55 ? 3   THR D C   1 
ATOM   4410 O  O   . THR D 1 15  ? 3.591   51.453  26.132  1.00 29.52 ? 3   THR D O   1 
ATOM   4411 C  CB  . THR D 1 15  ? 1.302   53.153  27.005  1.00 30.74 ? 3   THR D CB  1 
ATOM   4412 O  OG1 . THR D 1 15  ? 1.633   54.455  26.501  1.00 32.86 ? 3   THR D OG1 1 
ATOM   4413 C  CG2 . THR D 1 15  ? 0.007   53.236  27.789  1.00 31.80 ? 3   THR D CG2 1 
ATOM   4414 N  N   . SER D 1 16  ? 4.849   52.872  27.374  1.00 24.34 ? 4   SER D N   1 
ATOM   4415 C  CA  . SER D 1 16  ? 6.164   52.507  26.806  1.00 24.45 ? 4   SER D CA  1 
ATOM   4416 C  C   . SER D 1 16  ? 7.156   52.236  27.930  1.00 22.93 ? 4   SER D C   1 
ATOM   4417 O  O   . SER D 1 16  ? 6.954   52.760  29.044  1.00 24.75 ? 4   SER D O   1 
ATOM   4418 C  CB  . SER D 1 16  ? 6.667   53.565  25.852  1.00 29.50 ? 4   SER D CB  1 
ATOM   4419 O  OG  . SER D 1 16  ? 6.327   54.862  26.326  1.00 32.14 ? 4   SER D OG  1 
ATOM   4420 N  N   . SER D 1 17  ? 8.184   51.473  27.590  1.00 22.24 ? 5   SER D N   1 
ATOM   4421 C  CA  . SER D 1 17  ? 9.228   50.890  28.479  1.00 21.22 ? 5   SER D CA  1 
ATOM   4422 C  C   . SER D 1 17  ? 9.902   51.992  29.297  1.00 23.74 ? 5   SER D C   1 
ATOM   4423 O  O   . SER D 1 17  ? 10.278  53.054  28.716  1.00 24.74 ? 5   SER D O   1 
ATOM   4424 C  CB  . SER D 1 17  ? 10.267  50.113  27.727  1.00 22.05 ? 5   SER D CB  1 
ATOM   4425 O  OG  . SER D 1 17  ? 9.737   49.144  26.848  1.00 22.27 ? 5   SER D OG  1 
ATOM   4426 N  N   . GLU D 1 18  ? 10.157  51.703  30.568  1.00 21.09 ? 6   GLU D N   1 
ATOM   4427 C  CA  . GLU D 1 18  ? 10.683  52.679  31.543  1.00 24.80 ? 6   GLU D CA  1 
ATOM   4428 C  C   . GLU D 1 18  ? 11.226  51.903  32.750  1.00 24.66 ? 6   GLU D C   1 
ATOM   4429 O  O   . GLU D 1 18  ? 10.618  50.901  33.135  1.00 19.21 ? 6   GLU D O   1 
ATOM   4430 C  CB  . GLU D 1 18  ? 9.557   53.624  31.945  1.00 27.41 ? 6   GLU D CB  1 
ATOM   4431 C  CG  . GLU D 1 18  ? 9.976   54.754  32.855  1.00 32.74 ? 6   GLU D CG  1 
ATOM   4432 C  CD  . GLU D 1 18  ? 8.803   55.649  33.193  1.00 34.75 ? 6   GLU D CD  1 
ATOM   4433 O  OE1 . GLU D 1 18  ? 8.579   55.901  34.388  1.00 38.58 ? 6   GLU D OE1 1 
ATOM   4434 O  OE2 . GLU D 1 18  ? 8.111   56.083  32.244  1.00 40.42 ? 6   GLU D OE2 1 
ATOM   4435 N  N   . THR D 1 19  ? 12.320  52.379  33.339  1.00 18.80 ? 7   THR D N   1 
ATOM   4436 C  CA  . THR D 1 19  ? 12.813  51.894  34.643  1.00 18.95 ? 7   THR D CA  1 
ATOM   4437 C  C   . THR D 1 19  ? 13.048  53.111  35.523  1.00 18.71 ? 7   THR D C   1 
ATOM   4438 O  O   . THR D 1 19  ? 13.163  54.243  34.985  1.00 19.02 ? 7   THR D O   1 
ATOM   4439 C  CB  . THR D 1 19  ? 14.091  51.052  34.570  1.00 19.07 ? 7   THR D CB  1 
ATOM   4440 O  OG1 . THR D 1 19  ? 15.147  51.907  34.143  1.00 22.87 ? 7   THR D OG1 1 
ATOM   4441 C  CG2 . THR D 1 19  ? 13.990  49.892  33.612  1.00 18.49 ? 7   THR D CG2 1 
ATOM   4442 N  N   . GLY D 1 20  ? 13.101  52.871  36.820  1.00 17.57 ? 8   GLY D N   1 
ATOM   4443 C  CA  . GLY D 1 20  ? 13.253  53.955  37.793  1.00 17.43 ? 8   GLY D CA  1 
ATOM   4444 C  C   . GLY D 1 20  ? 13.159  53.444  39.198  1.00 18.94 ? 8   GLY D C   1 
ATOM   4445 O  O   . GLY D 1 20  ? 13.317  52.230  39.432  1.00 15.48 ? 8   GLY D O   1 
ATOM   4446 N  N   . THR D 1 21  ? 12.959  54.372  40.119  1.00 18.39 ? 9   THR D N   1 
ATOM   4447 C  CA  . THR D 1 21  ? 12.698  54.079  41.536  1.00 20.86 ? 9   THR D CA  1 
ATOM   4448 C  C   . THR D 1 21  ? 11.378  54.759  41.861  1.00 23.08 ? 9   THR D C   1 
ATOM   4449 O  O   . THR D 1 21  ? 11.142  55.896  41.355  1.00 22.50 ? 9   THR D O   1 
ATOM   4450 C  CB  . THR D 1 21  ? 13.848  54.571  42.428  1.00 27.93 ? 9   THR D CB  1 
ATOM   4451 O  OG1 . THR D 1 21  ? 13.514  54.284  43.785  1.00 33.81 ? 9   THR D OG1 1 
ATOM   4452 C  CG2 . THR D 1 21  ? 14.108  56.044  42.281  1.00 29.38 ? 9   THR D CG2 1 
ATOM   4453 N  N   . ASN D 1 22  ? 10.587  54.095  42.686  1.00 19.90 ? 10  ASN D N   1 
ATOM   4454 C  CA  . ASN D 1 22  ? 9.238   54.567  43.034  1.00 23.38 ? 10  ASN D CA  1 
ATOM   4455 C  C   . ASN D 1 22  ? 8.936   54.102  44.448  1.00 22.77 ? 10  ASN D C   1 
ATOM   4456 O  O   . ASN D 1 22  ? 9.038   52.902  44.706  1.00 21.47 ? 10  ASN D O   1 
ATOM   4457 C  CB  . ASN D 1 22  ? 8.195   54.098  42.021  1.00 22.56 ? 10  ASN D CB  1 
ATOM   4458 C  CG  . ASN D 1 22  ? 6.820   54.600  42.377  1.00 23.59 ? 10  ASN D CG  1 
ATOM   4459 O  OD1 . ASN D 1 22  ? 6.072   53.883  43.043  1.00 21.29 ? 10  ASN D OD1 1 
ATOM   4460 N  ND2 . ASN D 1 22  ? 6.505   55.823  41.964  1.00 26.20 ? 10  ASN D ND2 1 
ATOM   4461 N  N   . ASN D 1 23  ? 8.695   55.051  45.355  1.00 25.00 ? 11  ASN D N   1 
ATOM   4462 C  CA  . ASN D 1 23  ? 8.299   54.772  46.758  1.00 26.56 ? 11  ASN D CA  1 
ATOM   4463 C  C   . ASN D 1 23  ? 9.288   53.781  47.379  1.00 23.20 ? 11  ASN D C   1 
ATOM   4464 O  O   . ASN D 1 23  ? 8.870   52.969  48.225  1.00 26.00 ? 11  ASN D O   1 
ATOM   4465 C  CB  . ASN D 1 23  ? 6.817   54.375  46.788  1.00 27.48 ? 11  ASN D CB  1 
ATOM   4466 C  CG  . ASN D 1 23  ? 5.907   55.486  46.309  1.00 32.29 ? 11  ASN D CG  1 
ATOM   4467 O  OD1 . ASN D 1 23  ? 6.036   56.619  46.763  1.00 33.20 ? 11  ASN D OD1 1 
ATOM   4468 N  ND2 . ASN D 1 23  ? 4.996   55.201  45.389  1.00 28.58 ? 11  ASN D ND2 1 
ATOM   4469 N  N   . GLY D 1 24  ? 10.580  53.881  47.035  1.00 23.22 ? 12  GLY D N   1 
ATOM   4470 C  CA  . GLY D 1 24  ? 11.678  53.135  47.679  1.00 23.75 ? 12  GLY D CA  1 
ATOM   4471 C  C   . GLY D 1 24  ? 12.076  51.870  46.932  1.00 22.85 ? 12  GLY D C   1 
ATOM   4472 O  O   . GLY D 1 24  ? 13.018  51.180  47.339  1.00 26.65 ? 12  GLY D O   1 
ATOM   4473 N  N   . TYR D 1 25  ? 11.352  51.530  45.880  1.00 19.89 ? 13  TYR D N   1 
ATOM   4474 C  CA  . TYR D 1 25  ? 11.510  50.272  45.120  1.00 17.94 ? 13  TYR D CA  1 
ATOM   4475 C  C   . TYR D 1 25  ? 11.940  50.566  43.692  1.00 16.79 ? 13  TYR D C   1 
ATOM   4476 O  O   . TYR D 1 25  ? 11.378  51.442  43.052  1.00 18.80 ? 13  TYR D O   1 
ATOM   4477 C  CB  . TYR D 1 25  ? 10.159  49.559  45.073  1.00 17.66 ? 13  TYR D CB  1 
ATOM   4478 C  CG  . TYR D 1 25  ? 9.829   48.922  46.396  1.00 19.11 ? 13  TYR D CG  1 
ATOM   4479 C  CD1 . TYR D 1 25  ? 10.254  47.644  46.678  1.00 21.57 ? 13  TYR D CD1 1 
ATOM   4480 C  CD2 . TYR D 1 25  ? 9.097   49.598  47.359  1.00 21.20 ? 13  TYR D CD2 1 
ATOM   4481 C  CE1 . TYR D 1 25  ? 9.991   47.061  47.904  1.00 24.57 ? 13  TYR D CE1 1 
ATOM   4482 C  CE2 . TYR D 1 25  ? 8.796   49.017  48.576  1.00 22.94 ? 13  TYR D CE2 1 
ATOM   4483 C  CZ  . TYR D 1 25  ? 9.252   47.740  48.850  1.00 24.22 ? 13  TYR D CZ  1 
ATOM   4484 O  OH  . TYR D 1 25  ? 9.002   47.102  50.032  1.00 29.13 ? 13  TYR D OH  1 
ATOM   4485 N  N   . TYR D 1 26  ? 12.863  49.758  43.191  1.00 17.04 ? 14  TYR D N   1 
ATOM   4486 C  CA  . TYR D 1 26  ? 13.241  49.734  41.765  1.00 14.60 ? 14  TYR D CA  1 
ATOM   4487 C  C   . TYR D 1 26  ? 12.018  49.249  40.981  1.00 15.56 ? 14  TYR D C   1 
ATOM   4488 O  O   . TYR D 1 26  ? 11.336  48.322  41.492  1.00 14.11 ? 14  TYR D O   1 
ATOM   4489 C  CB  . TYR D 1 26  ? 14.389  48.779  41.513  1.00 15.03 ? 14  TYR D CB  1 
ATOM   4490 C  CG  . TYR D 1 26  ? 14.803  48.668  40.068  1.00 16.09 ? 14  TYR D CG  1 
ATOM   4491 C  CD1 . TYR D 1 26  ? 15.488  49.698  39.438  1.00 17.55 ? 14  TYR D CD1 1 
ATOM   4492 C  CD2 . TYR D 1 26  ? 14.507  47.539  39.314  1.00 16.18 ? 14  TYR D CD2 1 
ATOM   4493 C  CE1 . TYR D 1 26  ? 15.892  49.596  38.116  1.00 17.97 ? 14  TYR D CE1 1 
ATOM   4494 C  CE2 . TYR D 1 26  ? 14.897  47.429  38.000  1.00 17.02 ? 14  TYR D CE2 1 
ATOM   4495 C  CZ  . TYR D 1 26  ? 15.611  48.449  37.398  1.00 17.39 ? 14  TYR D CZ  1 
ATOM   4496 O  OH  . TYR D 1 26  ? 16.004  48.374  36.092  1.00 20.70 ? 14  TYR D OH  1 
ATOM   4497 N  N   . TYR D 1 27  ? 11.768  49.817  39.819  1.00 13.91 ? 15  TYR D N   1 
ATOM   4498 C  CA  . TYR D 1 27  ? 10.687  49.321  38.930  1.00 14.98 ? 15  TYR D CA  1 
ATOM   4499 C  C   . TYR D 1 27  ? 11.222  49.230  37.527  1.00 17.36 ? 15  TYR D C   1 
ATOM   4500 O  O   . TYR D 1 27  ? 12.110  50.021  37.124  1.00 16.32 ? 15  TYR D O   1 
ATOM   4501 C  CB  . TYR D 1 27  ? 9.376   50.102  38.999  1.00 15.77 ? 15  TYR D CB  1 
ATOM   4502 C  CG  . TYR D 1 27  ? 9.392   51.446  38.302  1.00 15.21 ? 15  TYR D CG  1 
ATOM   4503 C  CD1 . TYR D 1 27  ? 9.873   52.562  38.974  1.00 15.60 ? 15  TYR D CD1 1 
ATOM   4504 C  CD2 . TYR D 1 27  ? 9.011   51.584  36.980  1.00 16.15 ? 15  TYR D CD2 1 
ATOM   4505 C  CE1 . TYR D 1 27  ? 9.950   53.796  38.362  1.00 16.58 ? 15  TYR D CE1 1 
ATOM   4506 C  CE2 . TYR D 1 27  ? 9.068   52.829  36.356  1.00 19.48 ? 15  TYR D CE2 1 
ATOM   4507 C  CZ  . TYR D 1 27  ? 9.548   53.931  37.045  1.00 18.82 ? 15  TYR D CZ  1 
ATOM   4508 O  OH  . TYR D 1 27  ? 9.625   55.173  36.479  1.00 20.73 ? 15  TYR D OH  1 
ATOM   4509 N  N   . SER D 1 28  ? 10.713  48.221  36.824  1.00 15.59 ? 16  SER D N   1 
ATOM   4510 C  CA  . SER D 1 28  ? 11.065  47.929  35.427  1.00 16.02 ? 16  SER D CA  1 
ATOM   4511 C  C   . SER D 1 28  ? 9.788   47.582  34.655  1.00 15.45 ? 16  SER D C   1 
ATOM   4512 O  O   . SER D 1 28  ? 9.045   46.694  35.087  1.00 17.19 ? 16  SER D O   1 
ATOM   4513 C  CB  . SER D 1 28  ? 12.039  46.842  35.329  1.00 17.02 ? 16  SER D CB  1 
ATOM   4514 O  OG  . SER D 1 28  ? 12.405  46.689  33.988  1.00 19.37 ? 16  SER D OG  1 
ATOM   4515 N  N   . PHE D 1 29  ? 9.538   48.336  33.610  1.00 14.24 ? 17  PHE D N   1 
ATOM   4516 C  CA  . PHE D 1 29  ? 8.437   48.078  32.669  1.00 15.84 ? 17  PHE D CA  1 
ATOM   4517 C  C   . PHE D 1 29  ? 9.061   47.992  31.297  1.00 17.76 ? 17  PHE D C   1 
ATOM   4518 O  O   . PHE D 1 29  ? 9.631   48.998  30.820  1.00 16.23 ? 17  PHE D O   1 
ATOM   4519 C  CB  . PHE D 1 29  ? 7.370   49.159  32.771  1.00 16.40 ? 17  PHE D CB  1 
ATOM   4520 C  CG  . PHE D 1 29  ? 6.288   49.030  31.731  1.00 17.46 ? 17  PHE D CG  1 
ATOM   4521 C  CD1 . PHE D 1 29  ? 5.581   47.844  31.613  1.00 16.12 ? 17  PHE D CD1 1 
ATOM   4522 C  CD2 . PHE D 1 29  ? 6.000   50.053  30.840  1.00 18.66 ? 17  PHE D CD2 1 
ATOM   4523 C  CE1 . PHE D 1 29  ? 4.569   47.704  30.670  1.00 15.61 ? 17  PHE D CE1 1 
ATOM   4524 C  CE2 . PHE D 1 29  ? 4.987   49.913  29.906  1.00 18.05 ? 17  PHE D CE2 1 
ATOM   4525 C  CZ  . PHE D 1 29  ? 4.280   48.730  29.806  1.00 17.23 ? 17  PHE D CZ  1 
ATOM   4526 N  N   . TRP D 1 30  ? 8.886   46.842  30.655  1.00 16.57 ? 18  TRP D N   1 
ATOM   4527 C  CA  . TRP D 1 30  ? 9.357   46.663  29.263  1.00 18.76 ? 18  TRP D CA  1 
ATOM   4528 C  C   . TRP D 1 30  ? 8.174   46.178  28.435  1.00 19.31 ? 18  TRP D C   1 
ATOM   4529 O  O   . TRP D 1 30  ? 7.530   45.229  28.866  1.00 15.95 ? 18  TRP D O   1 
ATOM   4530 C  CB  . TRP D 1 30  ? 10.519  45.680  29.231  1.00 23.49 ? 18  TRP D CB  1 
ATOM   4531 C  CG  . TRP D 1 30  ? 10.895  45.384  27.819  1.00 28.52 ? 18  TRP D CG  1 
ATOM   4532 C  CD1 . TRP D 1 30  ? 11.554  46.218  26.960  1.00 32.74 ? 18  TRP D CD1 1 
ATOM   4533 C  CD2 . TRP D 1 30  ? 10.514  44.223  27.063  1.00 28.25 ? 18  TRP D CD2 1 
ATOM   4534 N  NE1 . TRP D 1 30  ? 11.648  45.635  25.725  1.00 32.38 ? 18  TRP D NE1 1 
ATOM   4535 C  CE2 . TRP D 1 30  ? 11.034  44.403  25.762  1.00 33.45 ? 18  TRP D CE2 1 
ATOM   4536 C  CE3 . TRP D 1 30  ? 9.818   43.051  27.368  1.00 31.06 ? 18  TRP D CE3 1 
ATOM   4537 C  CZ2 . TRP D 1 30  ? 10.855  43.447  24.762  1.00 31.45 ? 18  TRP D CZ2 1 
ATOM   4538 C  CZ3 . TRP D 1 30  ? 9.657   42.099  26.382  1.00 34.32 ? 18  TRP D CZ3 1 
ATOM   4539 C  CH2 . TRP D 1 30  ? 10.165  42.305  25.094  1.00 31.81 ? 18  TRP D CH2 1 
ATOM   4540 N  N   . THR D 1 31  ? 7.905   46.803  27.300  1.00 18.61 ? 19  THR D N   1 
ATOM   4541 C  CA  . THR D 1 31  ? 6.945   46.277  26.305  1.00 19.92 ? 19  THR D CA  1 
ATOM   4542 C  C   . THR D 1 31  ? 7.550   46.428  24.911  1.00 21.31 ? 19  THR D C   1 
ATOM   4543 O  O   . THR D 1 31  ? 8.278   47.435  24.696  1.00 22.39 ? 19  THR D O   1 
ATOM   4544 C  CB  . THR D 1 31  ? 5.575   46.934  26.446  1.00 21.59 ? 19  THR D CB  1 
ATOM   4545 O  OG1 . THR D 1 31  ? 4.784   46.327  25.419  1.00 22.98 ? 19  THR D OG1 1 
ATOM   4546 C  CG2 . THR D 1 31  ? 5.623   48.441  26.293  1.00 21.81 ? 19  THR D CG2 1 
ATOM   4547 N  N   . ASP D 1 32  ? 7.304   45.445  24.049  1.00 23.44 ? 20  ASP D N   1 
ATOM   4548 C  CA  . ASP D 1 32  ? 7.743   45.439  22.627  1.00 25.40 ? 20  ASP D CA  1 
ATOM   4549 C  C   . ASP D 1 32  ? 6.834   46.359  21.784  1.00 28.98 ? 20  ASP D C   1 
ATOM   4550 O  O   . ASP D 1 32  ? 7.185   46.584  20.609  1.00 30.40 ? 20  ASP D O   1 
ATOM   4551 C  CB  . ASP D 1 32  ? 7.863   44.021  22.072  1.00 26.54 ? 20  ASP D CB  1 
ATOM   4552 C  CG  . ASP D 1 32  ? 6.550   43.265  21.915  1.00 24.70 ? 20  ASP D CG  1 
ATOM   4553 O  OD1 . ASP D 1 32  ? 5.479   43.886  22.176  1.00 27.53 ? 20  ASP D OD1 1 
ATOM   4554 O  OD2 . ASP D 1 32  ? 6.619   42.058  21.535  1.00 24.30 ? 20  ASP D OD2 1 
ATOM   4555 N  N   . GLY D 1 33  ? 5.729   46.883  22.341  1.00 24.52 ? 21  GLY D N   1 
ATOM   4556 C  CA  . GLY D 1 33  ? 4.851   47.860  21.665  1.00 25.33 ? 21  GLY D CA  1 
ATOM   4557 C  C   . GLY D 1 33  ? 3.576   47.250  21.109  1.00 25.38 ? 21  GLY D C   1 
ATOM   4558 O  O   . GLY D 1 33  ? 2.687   48.019  20.697  1.00 27.26 ? 21  GLY D O   1 
ATOM   4559 N  N   . GLY D 1 34  ? 3.447   45.918  21.114  1.00 23.68 ? 22  GLY D N   1 
ATOM   4560 C  CA  . GLY D 1 34  ? 2.261   45.216  20.593  1.00 23.46 ? 22  GLY D CA  1 
ATOM   4561 C  C   . GLY D 1 34  ? 1.030   45.507  21.424  1.00 22.25 ? 22  GLY D C   1 
ATOM   4562 O  O   . GLY D 1 34  ? 1.167   45.668  22.633  1.00 22.75 ? 22  GLY D O   1 
ATOM   4563 N  N   . GLY D 1 35  ? -0.142  45.559  20.799  1.00 22.18 ? 23  GLY D N   1 
ATOM   4564 C  CA  . GLY D 1 35  ? -1.420  45.793  21.500  1.00 22.83 ? 23  GLY D CA  1 
ATOM   4565 C  C   . GLY D 1 35  ? -1.338  47.010  22.395  1.00 24.21 ? 23  GLY D C   1 
ATOM   4566 O  O   . GLY D 1 35  ? -0.714  48.010  21.972  1.00 21.86 ? 23  GLY D O   1 
ATOM   4567 N  N   . GLN D 1 36  ? -1.959  46.939  23.590  1.00 20.73 ? 24  GLN D N   1 
ATOM   4568 C  CA  . GLN D 1 36  ? -1.987  48.018  24.599  1.00 22.44 ? 24  GLN D CA  1 
ATOM   4569 C  C   . GLN D 1 36  ? -1.553  47.376  25.918  1.00 19.53 ? 24  GLN D C   1 
ATOM   4570 O  O   . GLN D 1 36  ? -2.104  46.343  26.271  1.00 19.59 ? 24  GLN D O   1 
ATOM   4571 C  CB  . GLN D 1 36  ? -3.369  48.673  24.692  1.00 26.70 ? 24  GLN D CB  1 
ATOM   4572 C  CG  . GLN D 1 36  ? -3.436  49.820  25.704  1.00 35.73 ? 24  GLN D CG  1 
ATOM   4573 C  CD  . GLN D 1 36  ? -4.218  51.036  25.250  1.00 41.52 ? 24  GLN D CD  1 
ATOM   4574 O  OE1 . GLN D 1 36  ? -4.847  51.054  24.189  1.00 48.93 ? 24  GLN D OE1 1 
ATOM   4575 N  NE2 . GLN D 1 36  ? -4.176  52.087  26.059  1.00 48.60 ? 24  GLN D NE2 1 
ATOM   4576 N  N   . VAL D 1 37  ? -0.498  47.901  26.502  1.00 18.94 ? 25  VAL D N   1 
ATOM   4577 C  CA  . VAL D 1 37  ? 0.022   47.487  27.833  1.00 19.22 ? 25  VAL D CA  1 
ATOM   4578 C  C   . VAL D 1 37  ? 0.195   48.775  28.626  1.00 19.61 ? 25  VAL D C   1 
ATOM   4579 O  O   . VAL D 1 37  ? 0.930   49.654  28.151  1.00 21.31 ? 25  VAL D O   1 
ATOM   4580 C  CB  . VAL D 1 37  ? 1.331   46.692  27.720  1.00 18.94 ? 25  VAL D CB  1 
ATOM   4581 C  CG1 . VAL D 1 37  ? 1.802   46.142  29.059  1.00 19.09 ? 25  VAL D CG1 1 
ATOM   4582 C  CG2 . VAL D 1 37  ? 1.196   45.548  26.728  1.00 20.27 ? 25  VAL D CG2 1 
ATOM   4583 N  N   . THR D 1 38  ? -0.525  48.908  29.742  1.00 18.26 ? 26  THR D N   1 
ATOM   4584 C  CA  . THR D 1 38  ? -0.503  50.116  30.597  1.00 18.41 ? 26  THR D CA  1 
ATOM   4585 C  C   . THR D 1 38  ? -0.001  49.741  31.990  1.00 20.14 ? 26  THR D C   1 
ATOM   4586 O  O   . THR D 1 38  ? -0.560  48.851  32.602  1.00 18.61 ? 26  THR D O   1 
ATOM   4587 C  CB  . THR D 1 38  ? -1.882  50.796  30.619  1.00 23.35 ? 26  THR D CB  1 
ATOM   4588 O  OG1 . THR D 1 38  ? -2.346  51.050  29.281  1.00 22.07 ? 26  THR D OG1 1 
ATOM   4589 C  CG2 . THR D 1 38  ? -1.855  52.081  31.408  1.00 24.27 ? 26  THR D CG2 1 
ATOM   4590 N  N   . TYR D 1 39  ? 1.082   50.365  32.422  1.00 18.06 ? 27  TYR D N   1 
ATOM   4591 C  CA  . TYR D 1 39  ? 1.744   50.107  33.703  1.00 17.07 ? 27  TYR D CA  1 
ATOM   4592 C  C   . TYR D 1 39  ? 1.480   51.300  34.613  1.00 18.31 ? 27  TYR D C   1 
ATOM   4593 O  O   . TYR D 1 39  ? 1.571   52.472  34.153  1.00 19.51 ? 27  TYR D O   1 
ATOM   4594 C  CB  . TYR D 1 39  ? 3.223   49.821  33.451  1.00 15.60 ? 27  TYR D CB  1 
ATOM   4595 C  CG  . TYR D 1 39  ? 4.033   49.703  34.708  1.00 15.57 ? 27  TYR D CG  1 
ATOM   4596 C  CD1 . TYR D 1 39  ? 4.479   50.817  35.381  1.00 15.14 ? 27  TYR D CD1 1 
ATOM   4597 C  CD2 . TYR D 1 39  ? 4.196   48.474  35.320  1.00 14.16 ? 27  TYR D CD2 1 
ATOM   4598 C  CE1 . TYR D 1 39  ? 5.199   50.705  36.569  1.00 15.23 ? 27  TYR D CE1 1 
ATOM   4599 C  CE2 . TYR D 1 39  ? 4.932   48.339  36.483  1.00 15.90 ? 27  TYR D CE2 1 
ATOM   4600 C  CZ  . TYR D 1 39  ? 5.402   49.461  37.140  1.00 15.37 ? 27  TYR D CZ  1 
ATOM   4601 O  OH  . TYR D 1 39  ? 6.147   49.288  38.262  1.00 15.68 ? 27  TYR D OH  1 
ATOM   4602 N  N   . THR D 1 40  ? 1.183   51.038  35.883  1.00 17.74 ? 28  THR D N   1 
ATOM   4603 C  CA  . THR D 1 40  ? 0.989   52.106  36.875  1.00 19.05 ? 28  THR D CA  1 
ATOM   4604 C  C   . THR D 1 40  ? 1.770   51.771  38.144  1.00 18.53 ? 28  THR D C   1 
ATOM   4605 O  O   . THR D 1 40  ? 1.551   50.692  38.729  1.00 19.05 ? 28  THR D O   1 
ATOM   4606 C  CB  . THR D 1 40  ? -0.502  52.329  37.177  1.00 24.38 ? 28  THR D CB  1 
ATOM   4607 O  OG1 . THR D 1 40  ? -1.163  52.681  35.958  1.00 24.11 ? 28  THR D OG1 1 
ATOM   4608 C  CG2 . THR D 1 40  ? -0.703  53.407  38.218  1.00 27.30 ? 28  THR D CG2 1 
ATOM   4609 N  N   . ASN D 1 41  ? 2.539   52.735  38.643  1.00 18.07 ? 29  ASN D N   1 
ATOM   4610 C  CA  . ASN D 1 41  ? 3.199   52.615  39.955  1.00 18.68 ? 29  ASN D CA  1 
ATOM   4611 C  C   . ASN D 1 41  ? 2.167   52.992  41.006  1.00 20.39 ? 29  ASN D C   1 
ATOM   4612 O  O   . ASN D 1 41  ? 1.413   53.957  40.771  1.00 24.68 ? 29  ASN D O   1 
ATOM   4613 C  CB  . ASN D 1 41  ? 4.451   53.483  40.047  1.00 19.46 ? 29  ASN D CB  1 
ATOM   4614 C  CG  . ASN D 1 41  ? 5.670   52.807  39.470  1.00 18.33 ? 29  ASN D CG  1 
ATOM   4615 O  OD1 . ASN D 1 41  ? 5.838   51.615  39.696  1.00 19.15 ? 29  ASN D OD1 1 
ATOM   4616 N  ND2 . ASN D 1 41  ? 6.519   53.554  38.766  1.00 20.91 ? 29  ASN D ND2 1 
ATOM   4617 N  N   . GLY D 1 42  ? 2.136   52.220  42.081  1.00 19.98 ? 30  GLY D N   1 
ATOM   4618 C  CA  . GLY D 1 42  ? 1.287   52.451  43.263  1.00 21.66 ? 30  GLY D CA  1 
ATOM   4619 C  C   . GLY D 1 42  ? 2.135   52.781  44.481  1.00 22.37 ? 30  GLY D C   1 
ATOM   4620 O  O   . GLY D 1 42  ? 3.374   52.782  44.424  1.00 21.02 ? 30  GLY D O   1 
ATOM   4621 N  N   . PRO D 1 43  ? 1.488   52.987  45.647  1.00 23.13 ? 31  PRO D N   1 
ATOM   4622 C  CA  . PRO D 1 43  ? 2.221   53.268  46.883  1.00 26.02 ? 31  PRO D CA  1 
ATOM   4623 C  C   . PRO D 1 43  ? 3.135   52.105  47.307  1.00 26.15 ? 31  PRO D C   1 
ATOM   4624 O  O   . PRO D 1 43  ? 2.840   50.932  47.002  1.00 24.34 ? 31  PRO D O   1 
ATOM   4625 C  CB  . PRO D 1 43  ? 1.102   53.551  47.902  1.00 28.37 ? 31  PRO D CB  1 
ATOM   4626 C  CG  . PRO D 1 43  ? -0.133  52.889  47.335  1.00 28.37 ? 31  PRO D CG  1 
ATOM   4627 C  CD  . PRO D 1 43  ? 0.032   52.934  45.829  1.00 27.30 ? 31  PRO D CD  1 
ATOM   4628 N  N   . ALA D 1 44  ? 4.226   52.461  47.986  1.00 25.30 ? 32  ALA D N   1 
ATOM   4629 C  CA  . ALA D 1 44  ? 5.287   51.553  48.462  1.00 23.18 ? 32  ALA D CA  1 
ATOM   4630 C  C   . ALA D 1 44  ? 5.633   50.541  47.348  1.00 21.48 ? 32  ALA D C   1 
ATOM   4631 O  O   . ALA D 1 44  ? 5.929   50.993  46.238  1.00 21.43 ? 32  ALA D O   1 
ATOM   4632 C  CB  . ALA D 1 44  ? 4.841   50.930  49.767  1.00 26.02 ? 32  ALA D CB  1 
ATOM   4633 N  N   . GLY D 1 45  ? 5.527   49.234  47.601  1.00 21.51 ? 33  GLY D N   1 
ATOM   4634 C  CA  . GLY D 1 45  ? 5.951   48.169  46.655  1.00 19.08 ? 33  GLY D CA  1 
ATOM   4635 C  C   . GLY D 1 45  ? 4.898   47.771  45.622  1.00 19.11 ? 33  GLY D C   1 
ATOM   4636 O  O   . GLY D 1 45  ? 5.042   46.693  45.020  1.00 17.39 ? 33  GLY D O   1 
ATOM   4637 N  N   . GLN D 1 46  ? 3.878   48.588  45.379  1.00 17.75 ? 34  GLN D N   1 
ATOM   4638 C  CA  . GLN D 1 46  ? 2.692   48.160  44.594  1.00 16.80 ? 34  GLN D CA  1 
ATOM   4639 C  C   . GLN D 1 46  ? 2.858   48.583  43.145  1.00 16.75 ? 34  GLN D C   1 
ATOM   4640 O  O   . GLN D 1 46  ? 3.316   49.697  42.879  1.00 15.07 ? 34  GLN D O   1 
ATOM   4641 C  CB  . GLN D 1 46  ? 1.394   48.708  45.181  1.00 20.67 ? 34  GLN D CB  1 
ATOM   4642 C  CG  . GLN D 1 46  ? 0.169   48.091  44.509  1.00 25.90 ? 34  GLN D CG  1 
ATOM   4643 C  CD  . GLN D 1 46  ? -0.636  49.144  43.795  1.00 38.00 ? 34  GLN D CD  1 
ATOM   4644 O  OE1 . GLN D 1 46  ? -0.453  49.406  42.601  1.00 37.30 ? 34  GLN D OE1 1 
ATOM   4645 N  NE2 . GLN D 1 46  ? -1.516  49.786  44.559  1.00 39.71 ? 34  GLN D NE2 1 
ATOM   4646 N  N   . TYR D 1 47  ? 2.421   47.737  42.206  1.00 15.92 ? 35  TYR D N   1 
ATOM   4647 C  CA  . TYR D 1 47  ? 2.330   48.136  40.794  1.00 15.24 ? 35  TYR D CA  1 
ATOM   4648 C  C   . TYR D 1 47  ? 1.104   47.464  40.196  1.00 15.91 ? 35  TYR D C   1 
ATOM   4649 O  O   . TYR D 1 47  ? 0.631   46.442  40.769  1.00 15.10 ? 35  TYR D O   1 
ATOM   4650 C  CB  . TYR D 1 47  ? 3.622   47.836  40.032  1.00 15.65 ? 35  TYR D CB  1 
ATOM   4651 C  CG  . TYR D 1 47  ? 3.850   46.388  39.733  1.00 15.19 ? 35  TYR D CG  1 
ATOM   4652 C  CD1 . TYR D 1 47  ? 3.257   45.769  38.639  1.00 14.46 ? 35  TYR D CD1 1 
ATOM   4653 C  CD2 . TYR D 1 47  ? 4.524   45.588  40.638  1.00 14.67 ? 35  TYR D CD2 1 
ATOM   4654 C  CE1 . TYR D 1 47  ? 3.458   44.419  38.385  1.00 14.06 ? 35  TYR D CE1 1 
ATOM   4655 C  CE2 . TYR D 1 47  ? 4.692   44.235  40.416  1.00 14.10 ? 35  TYR D CE2 1 
ATOM   4656 C  CZ  . TYR D 1 47  ? 4.199   43.650  39.258  1.00 14.02 ? 35  TYR D CZ  1 
ATOM   4657 O  OH  . TYR D 1 47  ? 4.414   42.297  39.082  1.00 15.11 ? 35  TYR D OH  1 
ATOM   4658 N  N   . SER D 1 48  ? 0.626   48.035  39.096  1.00 16.11 ? 36  SER D N   1 
ATOM   4659 C  CA  . SER D 1 48  ? -0.509  47.497  38.321  1.00 17.73 ? 36  SER D CA  1 
ATOM   4660 C  C   . SER D 1 48  ? -0.159  47.489  36.844  1.00 17.11 ? 36  SER D C   1 
ATOM   4661 O  O   . SER D 1 48  ? 0.545   48.363  36.366  1.00 19.15 ? 36  SER D O   1 
ATOM   4662 C  CB  . SER D 1 48  ? -1.781  48.253  38.520  1.00 20.29 ? 36  SER D CB  1 
ATOM   4663 O  OG  . SER D 1 48  ? -2.143  48.261  39.901  1.00 25.70 ? 36  SER D OG  1 
ATOM   4664 N  N   . VAL D 1 49  ? -0.698  46.516  36.154  1.00 17.86 ? 37  VAL D N   1 
ATOM   4665 C  CA  . VAL D 1 49  ? -0.519  46.389  34.692  1.00 18.35 ? 37  VAL D CA  1 
ATOM   4666 C  C   . VAL D 1 49  ? -1.848  45.900  34.134  1.00 20.08 ? 37  VAL D C   1 
ATOM   4667 O  O   . VAL D 1 49  ? -2.483  45.019  34.754  1.00 17.23 ? 37  VAL D O   1 
ATOM   4668 C  CB  . VAL D 1 49  ? 0.700   45.523  34.347  1.00 18.57 ? 37  VAL D CB  1 
ATOM   4669 C  CG1 . VAL D 1 49  ? 0.648   44.113  34.925  1.00 18.81 ? 37  VAL D CG1 1 
ATOM   4670 C  CG2 . VAL D 1 49  ? 0.950   45.526  32.859  1.00 19.77 ? 37  VAL D CG2 1 
ATOM   4671 N  N   . GLU D 1 50  ? -2.285  46.523  33.046  1.00 18.89 ? 38  GLU D N   1 
ATOM   4672 C  CA  . GLU D 1 50  ? -3.490  46.097  32.306  1.00 20.68 ? 38  GLU D CA  1 
ATOM   4673 C  C   . GLU D 1 50  ? -3.080  45.963  30.840  1.00 18.62 ? 38  GLU D C   1 
ATOM   4674 O  O   . GLU D 1 50  ? -2.326  46.837  30.378  1.00 17.89 ? 38  GLU D O   1 
ATOM   4675 C  CB  . GLU D 1 50  ? -4.637  47.092  32.495  1.00 25.37 ? 38  GLU D CB  1 
ATOM   4676 C  CG  . GLU D 1 50  ? -5.475  46.859  33.747  1.00 31.20 ? 38  GLU D CG  1 
ATOM   4677 C  CD  . GLU D 1 50  ? -6.983  46.734  33.533  1.00 37.79 ? 38  GLU D CD  1 
ATOM   4678 O  OE1 . GLU D 1 50  ? -7.714  46.601  34.540  1.00 47.00 ? 38  GLU D OE1 1 
ATOM   4679 O  OE2 . GLU D 1 50  ? -7.429  46.719  32.364  1.00 48.08 ? 38  GLU D OE2 1 
ATOM   4680 N  N   . TRP D 1 51  ? -3.477  44.887  30.194  1.00 17.70 ? 39  TRP D N   1 
ATOM   4681 C  CA  . TRP D 1 51  ? -3.029  44.612  28.805  1.00 16.44 ? 39  TRP D CA  1 
ATOM   4682 C  C   . TRP D 1 51  ? -4.161  44.039  27.954  1.00 17.31 ? 39  TRP D C   1 
ATOM   4683 O  O   . TRP D 1 51  ? -5.099  43.385  28.449  1.00 15.83 ? 39  TRP D O   1 
ATOM   4684 C  CB  . TRP D 1 51  ? -1.747  43.783  28.800  1.00 15.46 ? 39  TRP D CB  1 
ATOM   4685 C  CG  . TRP D 1 51  ? -1.808  42.366  29.290  1.00 16.03 ? 39  TRP D CG  1 
ATOM   4686 C  CD1 . TRP D 1 51  ? -1.821  41.283  28.467  1.00 15.85 ? 39  TRP D CD1 1 
ATOM   4687 C  CD2 . TRP D 1 51  ? -1.771  41.838  30.637  1.00 16.30 ? 39  TRP D CD2 1 
ATOM   4688 N  NE1 . TRP D 1 51  ? -1.780  40.132  29.184  1.00 16.44 ? 39  TRP D NE1 1 
ATOM   4689 C  CE2 . TRP D 1 51  ? -1.787  40.431  30.516  1.00 16.67 ? 39  TRP D CE2 1 
ATOM   4690 C  CE3 . TRP D 1 51  ? -1.694  42.398  31.918  1.00 17.71 ? 39  TRP D CE3 1 
ATOM   4691 C  CZ2 . TRP D 1 51  ? -1.711  39.567  31.616  1.00 16.46 ? 39  TRP D CZ2 1 
ATOM   4692 C  CZ3 . TRP D 1 51  ? -1.697  41.553  33.015  1.00 15.89 ? 39  TRP D CZ3 1 
ATOM   4693 C  CH2 . TRP D 1 51  ? -1.666  40.162  32.861  1.00 14.85 ? 39  TRP D CH2 1 
ATOM   4694 N  N   . SER D 1 52  ? -4.089  44.340  26.668  1.00 18.58 ? 40  SER D N   1 
ATOM   4695 C  CA  . SER D 1 52  ? -5.110  43.969  25.677  1.00 19.76 ? 40  SER D CA  1 
ATOM   4696 C  C   . SER D 1 52  ? -4.367  43.539  24.407  1.00 19.19 ? 40  SER D C   1 
ATOM   4697 O  O   . SER D 1 52  ? -3.672  44.396  23.831  1.00 18.79 ? 40  SER D O   1 
ATOM   4698 C  CB  . SER D 1 52  ? -6.044  45.117  25.433  1.00 23.93 ? 40  SER D CB  1 
ATOM   4699 O  OG  . SER D 1 52  ? -7.143  44.679  24.641  1.00 30.59 ? 40  SER D OG  1 
ATOM   4700 N  N   . ASN D 1 53  ? -4.497  42.276  24.004  1.00 18.06 ? 41  ASN D N   1 
ATOM   4701 C  CA  . ASN D 1 53  ? -3.865  41.708  22.783  1.00 19.68 ? 41  ASN D CA  1 
ATOM   4702 C  C   . ASN D 1 53  ? -2.396  42.122  22.690  1.00 16.97 ? 41  ASN D C   1 
ATOM   4703 O  O   . ASN D 1 53  ? -1.958  42.622  21.611  1.00 17.68 ? 41  ASN D O   1 
ATOM   4704 C  CB  . ASN D 1 53  ? -4.645  42.169  21.561  1.00 20.14 ? 41  ASN D CB  1 
ATOM   4705 C  CG  . ASN D 1 53  ? -6.020  41.547  21.491  1.00 21.95 ? 41  ASN D CG  1 
ATOM   4706 O  OD1 . ASN D 1 53  ? -6.139  40.319  21.527  1.00 21.16 ? 41  ASN D OD1 1 
ATOM   4707 N  ND2 . ASN D 1 53  ? -7.043  42.381  21.367  1.00 25.07 ? 41  ASN D ND2 1 
ATOM   4708 N  N   . SER D 1 54  ? -1.640  41.869  23.754  1.00 17.39 ? 42  SER D N   1 
ATOM   4709 C  CA  . SER D 1 54  ? -0.259  42.373  23.920  1.00 18.17 ? 42  SER D CA  1 
ATOM   4710 C  C   . SER D 1 54  ? 0.709   41.659  22.980  1.00 19.09 ? 42  SER D C   1 
ATOM   4711 O  O   . SER D 1 54  ? 0.461   40.527  22.549  1.00 19.86 ? 42  SER D O   1 
ATOM   4712 C  CB  . SER D 1 54  ? 0.210   42.187  25.331  1.00 17.19 ? 42  SER D CB  1 
ATOM   4713 O  OG  . SER D 1 54  ? 0.380   40.791  25.557  1.00 18.85 ? 42  SER D OG  1 
ATOM   4714 N  N   . GLY D 1 55  ? 1.830   42.300  22.716  1.00 17.84 ? 43  GLY D N   1 
ATOM   4715 C  CA  . GLY D 1 55  ? 3.039   41.571  22.366  1.00 21.02 ? 43  GLY D CA  1 
ATOM   4716 C  C   . GLY D 1 55  ? 3.663   41.048  23.642  1.00 22.74 ? 43  GLY D C   1 
ATOM   4717 O  O   . GLY D 1 55  ? 2.921   40.733  24.638  1.00 25.26 ? 43  GLY D O   1 
ATOM   4718 N  N   . ASN D 1 56  ? 4.972   41.026  23.675  1.00 20.67 ? 44  ASN D N   1 
ATOM   4719 C  CA  . ASN D 1 56  ? 5.729   40.602  24.866  1.00 20.69 ? 44  ASN D CA  1 
ATOM   4720 C  C   . ASN D 1 56  ? 5.837   41.801  25.812  1.00 18.57 ? 44  ASN D C   1 
ATOM   4721 O  O   . ASN D 1 56  ? 6.146   42.899  25.375  1.00 17.20 ? 44  ASN D O   1 
ATOM   4722 C  CB  . ASN D 1 56  ? 7.110   40.074  24.472  1.00 25.98 ? 44  ASN D CB  1 
ATOM   4723 C  CG  . ASN D 1 56  ? 7.090   38.665  23.933  1.00 31.64 ? 44  ASN D CG  1 
ATOM   4724 O  OD1 . ASN D 1 56  ? 7.533   38.414  22.815  1.00 40.29 ? 44  ASN D OD1 1 
ATOM   4725 N  ND2 . ASN D 1 56  ? 6.601   37.736  24.740  1.00 40.58 ? 44  ASN D ND2 1 
ATOM   4726 N  N   . PHE D 1 57  ? 5.601   41.595  27.105  1.00 16.81 ? 45  PHE D N   1 
ATOM   4727 C  CA  . PHE D 1 57  ? 5.875   42.611  28.143  1.00 14.42 ? 45  PHE D CA  1 
ATOM   4728 C  C   . PHE D 1 57  ? 6.316   41.917  29.428  1.00 14.41 ? 45  PHE D C   1 
ATOM   4729 O  O   . PHE D 1 57  ? 6.027   40.734  29.693  1.00 13.89 ? 45  PHE D O   1 
ATOM   4730 C  CB  . PHE D 1 57  ? 4.690   43.538  28.387  1.00 14.34 ? 45  PHE D CB  1 
ATOM   4731 C  CG  . PHE D 1 57  ? 3.564   42.909  29.172  1.00 14.83 ? 45  PHE D CG  1 
ATOM   4732 C  CD1 . PHE D 1 57  ? 2.589   42.165  28.531  1.00 16.58 ? 45  PHE D CD1 1 
ATOM   4733 C  CD2 . PHE D 1 57  ? 3.556   42.976  30.548  1.00 16.38 ? 45  PHE D CD2 1 
ATOM   4734 C  CE1 . PHE D 1 57  ? 1.549   41.589  29.268  1.00 15.84 ? 45  PHE D CE1 1 
ATOM   4735 C  CE2 . PHE D 1 57  ? 2.525   42.385  31.286  1.00 16.38 ? 45  PHE D CE2 1 
ATOM   4736 C  CZ  . PHE D 1 57  ? 1.536   41.685  30.639  1.00 18.21 ? 45  PHE D CZ  1 
ATOM   4737 N  N   . VAL D 1 58  ? 7.079   42.656  30.217  1.00 15.12 ? 46  VAL D N   1 
ATOM   4738 C  CA  . VAL D 1 58  ? 7.505   42.225  31.573  1.00 16.45 ? 46  VAL D CA  1 
ATOM   4739 C  C   . VAL D 1 58  ? 7.394   43.466  32.451  1.00 17.11 ? 46  VAL D C   1 
ATOM   4740 O  O   . VAL D 1 58  ? 7.920   44.521  32.062  1.00 17.75 ? 46  VAL D O   1 
ATOM   4741 C  CB  . VAL D 1 58  ? 8.927   41.628  31.600  1.00 18.48 ? 46  VAL D CB  1 
ATOM   4742 C  CG1 . VAL D 1 58  ? 9.308   41.197  33.030  1.00 21.61 ? 46  VAL D CG1 1 
ATOM   4743 C  CG2 . VAL D 1 58  ? 9.084   40.455  30.636  1.00 21.00 ? 46  VAL D CG2 1 
ATOM   4744 N  N   . ALA D 1 59  ? 6.734   43.367  33.605  1.00 14.81 ? 47  ALA D N   1 
ATOM   4745 C  CA  . ALA D 1 59  ? 6.485   44.521  34.490  1.00 13.72 ? 47  ALA D CA  1 
ATOM   4746 C  C   . ALA D 1 59  ? 6.704   44.115  35.941  1.00 13.20 ? 47  ALA D C   1 
ATOM   4747 O  O   . ALA D 1 59  ? 6.137   43.095  36.341  1.00 14.40 ? 47  ALA D O   1 
ATOM   4748 C  CB  . ALA D 1 59  ? 5.087   45.014  34.307  1.00 16.25 ? 47  ALA D CB  1 
ATOM   4749 N  N   . GLY D 1 60  ? 7.394   44.927  36.747  1.00 12.44 ? 48  GLY D N   1 
ATOM   4750 C  CA  . GLY D 1 60  ? 7.375   44.687  38.182  1.00 13.24 ? 48  GLY D CA  1 
ATOM   4751 C  C   . GLY D 1 60  ? 8.289   45.581  38.989  1.00 13.54 ? 48  GLY D C   1 
ATOM   4752 O  O   . GLY D 1 60  ? 8.950   46.471  38.441  1.00 14.92 ? 48  GLY D O   1 
ATOM   4753 N  N   . LYS D 1 61  ? 8.252   45.358  40.284  1.00 12.97 ? 49  LYS D N   1 
ATOM   4754 C  CA  . LYS D 1 61  ? 8.984   46.142  41.301  1.00 13.20 ? 49  LYS D CA  1 
ATOM   4755 C  C   . LYS D 1 61  ? 9.917   45.197  42.033  1.00 12.67 ? 49  LYS D C   1 
ATOM   4756 O  O   . LYS D 1 61  ? 9.615   43.993  42.198  1.00 13.33 ? 49  LYS D O   1 
ATOM   4757 C  CB  . LYS D 1 61  ? 8.043   46.789  42.327  1.00 13.39 ? 49  LYS D CB  1 
ATOM   4758 C  CG  . LYS D 1 61  ? 7.690   48.230  41.983  1.00 15.37 ? 49  LYS D CG  1 
ATOM   4759 C  CD  . LYS D 1 61  ? 6.736   48.907  42.961  1.00 16.71 ? 49  LYS D CD  1 
ATOM   4760 C  CE  . LYS D 1 61  ? 6.640   50.389  42.676  1.00 19.09 ? 49  LYS D CE  1 
ATOM   4761 N  NZ  . LYS D 1 61  ? 5.708   51.082  43.592  1.00 19.42 ? 49  LYS D NZ  1 
ATOM   4762 N  N   . GLY D 1 62  ? 11.064  45.715  42.445  1.00 12.60 ? 50  GLY D N   1 
ATOM   4763 C  CA  . GLY D 1 62  ? 11.973  45.015  43.349  1.00 12.66 ? 50  GLY D CA  1 
ATOM   4764 C  C   . GLY D 1 62  ? 13.200  45.857  43.623  1.00 13.75 ? 50  GLY D C   1 
ATOM   4765 O  O   . GLY D 1 62  ? 13.066  46.929  44.229  1.00 13.87 ? 50  GLY D O   1 
ATOM   4766 N  N   . TRP D 1 63  ? 14.358  45.341  43.238  1.00 15.87 ? 51  TRP D N   1 
ATOM   4767 C  CA  . TRP D 1 63  ? 15.663  45.838  43.704  1.00 16.02 ? 51  TRP D CA  1 
ATOM   4768 C  C   . TRP D 1 63  ? 16.609  45.890  42.518  1.00 17.47 ? 51  TRP D C   1 
ATOM   4769 O  O   . TRP D 1 63  ? 16.534  45.006  41.641  1.00 15.27 ? 51  TRP D O   1 
ATOM   4770 C  CB  . TRP D 1 63  ? 16.232  44.980  44.845  1.00 18.01 ? 51  TRP D CB  1 
ATOM   4771 C  CG  . TRP D 1 63  ? 15.294  44.929  46.005  1.00 19.52 ? 51  TRP D CG  1 
ATOM   4772 C  CD1 . TRP D 1 63  ? 15.195  45.828  47.025  1.00 22.05 ? 51  TRP D CD1 1 
ATOM   4773 C  CD2 . TRP D 1 63  ? 14.186  44.030  46.146  1.00 19.99 ? 51  TRP D CD2 1 
ATOM   4774 N  NE1 . TRP D 1 63  ? 14.146  45.500  47.834  1.00 22.01 ? 51  TRP D NE1 1 
ATOM   4775 C  CE2 . TRP D 1 63  ? 13.502  44.409  47.318  1.00 21.67 ? 51  TRP D CE2 1 
ATOM   4776 C  CE3 . TRP D 1 63  ? 13.737  42.925  45.420  1.00 20.05 ? 51  TRP D CE3 1 
ATOM   4777 C  CZ2 . TRP D 1 63  ? 12.401  43.686  47.790  1.00 23.26 ? 51  TRP D CZ2 1 
ATOM   4778 C  CZ3 . TRP D 1 63  ? 12.607  42.261  45.844  1.00 21.67 ? 51  TRP D CZ3 1 
ATOM   4779 C  CH2 . TRP D 1 63  ? 11.957  42.629  47.021  1.00 22.30 ? 51  TRP D CH2 1 
ATOM   4780 N  N   . ASN D 1 64  ? 17.493  46.898  42.482  1.00 15.74 ? 52  ASN D N   1 
ATOM   4781 C  CA  . ASN D 1 64  ? 18.584  46.852  41.494  1.00 16.47 ? 52  ASN D CA  1 
ATOM   4782 C  C   . ASN D 1 64  ? 19.805  47.488  42.134  1.00 17.41 ? 52  ASN D C   1 
ATOM   4783 O  O   . ASN D 1 64  ? 19.817  48.705  42.308  1.00 16.03 ? 52  ASN D O   1 
ATOM   4784 C  CB  . ASN D 1 64  ? 18.219  47.541  40.178  1.00 17.84 ? 52  ASN D CB  1 
ATOM   4785 C  CG  . ASN D 1 64  ? 19.256  47.303  39.107  1.00 20.73 ? 52  ASN D CG  1 
ATOM   4786 O  OD1 . ASN D 1 64  ? 20.088  46.410  39.208  1.00 20.01 ? 52  ASN D OD1 1 
ATOM   4787 N  ND2 . ASN D 1 64  ? 19.170  48.072  38.045  1.00 25.01 ? 52  ASN D ND2 1 
ATOM   4788 N  N   . PRO D 1 65  ? 20.851  46.716  42.482  1.00 18.11 ? 53  PRO D N   1 
ATOM   4789 C  CA  . PRO D 1 65  ? 20.892  45.260  42.294  1.00 19.06 ? 53  PRO D CA  1 
ATOM   4790 C  C   . PRO D 1 65  ? 20.075  44.476  43.324  1.00 19.26 ? 53  PRO D C   1 
ATOM   4791 O  O   . PRO D 1 65  ? 19.891  44.943  44.429  1.00 20.82 ? 53  PRO D O   1 
ATOM   4792 C  CB  . PRO D 1 65  ? 22.364  44.922  42.572  1.00 21.22 ? 53  PRO D CB  1 
ATOM   4793 C  CG  . PRO D 1 65  ? 22.824  45.992  43.506  1.00 22.38 ? 53  PRO D CG  1 
ATOM   4794 C  CD  . PRO D 1 65  ? 22.087  47.244  43.079  1.00 21.31 ? 53  PRO D CD  1 
ATOM   4795 N  N   . GLY D 1 66  ? 19.685  43.263  42.987  1.00 19.80 ? 54  GLY D N   1 
ATOM   4796 C  CA  . GLY D 1 66  ? 19.095  42.357  43.982  1.00 20.32 ? 54  GLY D CA  1 
ATOM   4797 C  C   . GLY D 1 66  ? 20.149  41.795  44.910  1.00 22.75 ? 54  GLY D C   1 
ATOM   4798 O  O   . GLY D 1 66  ? 21.341  41.799  44.561  1.00 21.14 ? 54  GLY D O   1 
ATOM   4799 N  N   . SER D 1 67  ? 19.720  41.353  46.076  1.00 23.28 ? 55  SER D N   1 
ATOM   4800 C  CA  . SER D 1 67  ? 20.495  40.447  46.952  1.00 30.16 ? 55  SER D CA  1 
ATOM   4801 C  C   . SER D 1 67  ? 19.773  39.098  46.967  1.00 31.87 ? 55  SER D C   1 
ATOM   4802 O  O   . SER D 1 67  ? 18.996  38.810  46.051  1.00 40.02 ? 55  SER D O   1 
ATOM   4803 C  CB  . SER D 1 67  ? 20.645  40.996  48.341  1.00 35.41 ? 55  SER D CB  1 
ATOM   4804 O  OG  . SER D 1 67  ? 20.838  42.391  48.337  1.00 34.93 ? 55  SER D OG  1 
ATOM   4805 N  N   . SER D 1 68  ? 19.987  38.301  47.986  1.00 39.02 ? 56  SER D N   1 
ATOM   4806 C  CA  . SER D 1 68  ? 19.273  37.015  48.092  1.00 37.69 ? 56  SER D CA  1 
ATOM   4807 C  C   . SER D 1 68  ? 18.090  37.247  49.027  1.00 32.54 ? 56  SER D C   1 
ATOM   4808 O  O   . SER D 1 68  ? 17.906  36.421  49.923  1.00 34.88 ? 56  SER D O   1 
ATOM   4809 C  CB  . SER D 1 68  ? 20.209  35.943  48.563  1.00 42.99 ? 56  SER D CB  1 
ATOM   4810 O  OG  . SER D 1 68  ? 21.003  36.395  49.660  1.00 44.09 ? 56  SER D OG  1 
ATOM   4811 N  N   . GLN D 1 69  ? 17.335  38.334  48.842  1.00 34.25 ? 57  GLN D N   1 
ATOM   4812 C  CA  . GLN D 1 69  ? 16.334  38.710  49.885  1.00 36.16 ? 57  GLN D CA  1 
ATOM   4813 C  C   . GLN D 1 69  ? 15.162  37.722  49.831  1.00 29.15 ? 57  GLN D C   1 
ATOM   4814 O  O   . GLN D 1 69  ? 14.912  37.072  48.791  1.00 23.83 ? 57  GLN D O   1 
ATOM   4815 C  CB  . GLN D 1 69  ? 15.923  40.193  49.917  1.00 38.41 ? 57  GLN D CB  1 
ATOM   4816 C  CG  . GLN D 1 69  ? 15.473  40.854  48.619  1.00 35.65 ? 57  GLN D CG  1 
ATOM   4817 C  CD  . GLN D 1 69  ? 16.576  41.683  47.996  1.00 34.00 ? 57  GLN D CD  1 
ATOM   4818 O  OE1 . GLN D 1 69  ? 17.288  41.197  47.125  1.00 30.96 ? 57  GLN D OE1 1 
ATOM   4819 N  NE2 . GLN D 1 69  ? 16.735  42.933  48.431  1.00 32.40 ? 57  GLN D NE2 1 
ATOM   4820 N  N   . THR D 1 70  ? 14.556  37.519  50.992  1.00 26.16 ? 58  THR D N   1 
ATOM   4821 C  CA  . THR D 1 70  ? 13.312  36.748  51.163  1.00 25.26 ? 58  THR D CA  1 
ATOM   4822 C  C   . THR D 1 70  ? 12.183  37.700  50.825  1.00 24.94 ? 58  THR D C   1 
ATOM   4823 O  O   . THR D 1 70  ? 12.067  38.751  51.503  1.00 23.31 ? 58  THR D O   1 
ATOM   4824 C  CB  . THR D 1 70  ? 13.200  36.195  52.584  1.00 25.84 ? 58  THR D CB  1 
ATOM   4825 O  OG1 . THR D 1 70  ? 14.278  35.272  52.716  1.00 25.81 ? 58  THR D OG1 1 
ATOM   4826 C  CG2 . THR D 1 70  ? 11.876  35.521  52.827  1.00 24.70 ? 58  THR D CG2 1 
ATOM   4827 N  N   . ILE D 1 71  ? 11.489  37.408  49.736  1.00 19.31 ? 59  ILE D N   1 
ATOM   4828 C  CA  . ILE D 1 71  ? 10.504  38.341  49.144  1.00 21.38 ? 59  ILE D CA  1 
ATOM   4829 C  C   . ILE D 1 71  ? 9.150   37.960  49.714  1.00 18.86 ? 59  ILE D C   1 
ATOM   4830 O  O   . ILE D 1 71  ? 8.851   36.769  49.767  1.00 20.58 ? 59  ILE D O   1 
ATOM   4831 C  CB  . ILE D 1 71  ? 10.520  38.260  47.607  1.00 22.26 ? 59  ILE D CB  1 
ATOM   4832 C  CG1 . ILE D 1 71  ? 11.878  38.656  47.015  1.00 21.92 ? 59  ILE D CG1 1 
ATOM   4833 C  CG2 . ILE D 1 71  ? 9.370   39.060  47.004  1.00 21.91 ? 59  ILE D CG2 1 
ATOM   4834 C  CD1 . ILE D 1 71  ? 11.864  38.635  45.500  1.00 24.78 ? 59  ILE D CD1 1 
ATOM   4835 N  N   . THR D 1 72  ? 8.371   38.949  50.119  1.00 19.47 ? 60  THR D N   1 
ATOM   4836 C  CA  . THR D 1 72  ? 6.926   38.754  50.396  1.00 20.28 ? 60  THR D CA  1 
ATOM   4837 C  C   . THR D 1 72  ? 6.123   39.563  49.379  1.00 19.17 ? 60  THR D C   1 
ATOM   4838 O  O   . THR D 1 72  ? 6.539   40.694  49.026  1.00 19.31 ? 60  THR D O   1 
ATOM   4839 C  CB  . THR D 1 72  ? 6.632   39.057  51.858  1.00 23.75 ? 60  THR D CB  1 
ATOM   4840 O  OG1 . THR D 1 72  ? 7.078   40.393  52.094  1.00 32.90 ? 60  THR D OG1 1 
ATOM   4841 C  CG2 . THR D 1 72  ? 7.341   38.096  52.781  1.00 24.65 ? 60  THR D CG2 1 
ATOM   4842 N  N   . TYR D 1 73  ? 5.090   38.955  48.803  1.00 19.00 ? 61  TYR D N   1 
ATOM   4843 C  CA  . TYR D 1 73  ? 4.286   39.655  47.772  1.00 19.06 ? 61  TYR D CA  1 
ATOM   4844 C  C   . TYR D 1 73  ? 2.821   39.227  47.939  1.00 19.43 ? 61  TYR D C   1 
ATOM   4845 O  O   . TYR D 1 73  ? 2.549   38.172  48.498  1.00 18.47 ? 61  TYR D O   1 
ATOM   4846 C  CB  . TYR D 1 73  ? 4.921   39.429  46.387  1.00 19.02 ? 61  TYR D CB  1 
ATOM   4847 C  CG  . TYR D 1 73  ? 4.590   38.078  45.798  1.00 17.76 ? 61  TYR D CG  1 
ATOM   4848 C  CD1 . TYR D 1 73  ? 5.258   36.932  46.209  1.00 19.07 ? 61  TYR D CD1 1 
ATOM   4849 C  CD2 . TYR D 1 73  ? 3.527   37.926  44.919  1.00 20.29 ? 61  TYR D CD2 1 
ATOM   4850 C  CE1 . TYR D 1 73  ? 4.888   35.674  45.771  1.00 19.14 ? 61  TYR D CE1 1 
ATOM   4851 C  CE2 . TYR D 1 73  ? 3.160   36.677  44.450  1.00 18.80 ? 61  TYR D CE2 1 
ATOM   4852 C  CZ  . TYR D 1 73  ? 3.842   35.553  44.870  1.00 21.09 ? 61  TYR D CZ  1 
ATOM   4853 O  OH  . TYR D 1 73  ? 3.459   34.313  44.475  1.00 20.87 ? 61  TYR D OH  1 
ATOM   4854 N  N   . SER D 1 74  ? 1.899   40.038  47.447  1.00 18.78 ? 62  SER D N   1 
ATOM   4855 C  CA  . SER D 1 74  ? 0.443   39.800  47.552  1.00 19.02 ? 62  SER D CA  1 
ATOM   4856 C  C   . SER D 1 74  ? -0.228  40.453  46.349  1.00 18.41 ? 62  SER D C   1 
ATOM   4857 O  O   . SER D 1 74  ? 0.453   41.232  45.682  1.00 19.00 ? 62  SER D O   1 
ATOM   4858 C  CB  . SER D 1 74  ? -0.083  40.337  48.842  1.00 20.28 ? 62  SER D CB  1 
ATOM   4859 O  OG  . SER D 1 74  ? 0.081   41.724  48.908  1.00 21.91 ? 62  SER D OG  1 
ATOM   4860 N  N   . GLY D 1 75  ? -1.514  40.187  46.145  1.00 16.72 ? 63  GLY D N   1 
ATOM   4861 C  CA  . GLY D 1 75  ? -2.421  40.972  45.294  1.00 16.94 ? 63  GLY D CA  1 
ATOM   4862 C  C   . GLY D 1 75  ? -3.205  40.028  44.394  1.00 20.02 ? 63  GLY D C   1 
ATOM   4863 O  O   . GLY D 1 75  ? -3.611  38.918  44.846  1.00 16.81 ? 63  GLY D O   1 
ATOM   4864 N  N   . GLU D 1 76  ? -3.380  40.442  43.144  1.00 18.57 ? 64  GLU D N   1 
ATOM   4865 C  CA  . GLU D 1 76  ? -4.320  39.815  42.194  1.00 20.57 ? 64  GLU D CA  1 
ATOM   4866 C  C   . GLU D 1 76  ? -3.629  39.720  40.829  1.00 19.09 ? 64  GLU D C   1 
ATOM   4867 O  O   . GLU D 1 76  ? -2.978  40.674  40.434  1.00 18.96 ? 64  GLU D O   1 
ATOM   4868 C  CB  . GLU D 1 76  ? -5.562  40.677  42.014  1.00 26.85 ? 64  GLU D CB  1 
ATOM   4869 C  CG  . GLU D 1 76  ? -6.174  41.129  43.325  1.00 33.72 ? 64  GLU D CG  1 
ATOM   4870 C  CD  . GLU D 1 76  ? -7.561  41.689  43.122  1.00 37.56 ? 64  GLU D CD  1 
ATOM   4871 O  OE1 . GLU D 1 76  ? -8.227  42.007  44.139  1.00 48.93 ? 64  GLU D OE1 1 
ATOM   4872 O  OE2 . GLU D 1 76  ? -7.973  41.795  41.943  1.00 41.26 ? 64  GLU D OE2 1 
ATOM   4873 N  N   . TRP D 1 77  ? -3.841  38.623  40.145  1.00 17.60 ? 65  TRP D N   1 
ATOM   4874 C  CA  . TRP D 1 77  ? -3.257  38.350  38.808  1.00 17.94 ? 65  TRP D CA  1 
ATOM   4875 C  C   . TRP D 1 77  ? -4.289  37.594  37.984  1.00 19.14 ? 65  TRP D C   1 
ATOM   4876 O  O   . TRP D 1 77  ? -4.546  36.397  38.286  1.00 17.92 ? 65  TRP D O   1 
ATOM   4877 C  CB  . TRP D 1 77  ? -1.948  37.616  38.984  1.00 17.89 ? 65  TRP D CB  1 
ATOM   4878 C  CG  . TRP D 1 77  ? -1.329  37.066  37.739  1.00 20.24 ? 65  TRP D CG  1 
ATOM   4879 C  CD1 . TRP D 1 77  ? -0.497  37.718  36.867  1.00 21.63 ? 65  TRP D CD1 1 
ATOM   4880 C  CD2 . TRP D 1 77  ? -1.354  35.683  37.331  1.00 18.96 ? 65  TRP D CD2 1 
ATOM   4881 N  NE1 . TRP D 1 77  ? -0.072  36.849  35.894  1.00 21.22 ? 65  TRP D NE1 1 
ATOM   4882 C  CE2 . TRP D 1 77  ? -0.568  35.586  36.165  1.00 20.20 ? 65  TRP D CE2 1 
ATOM   4883 C  CE3 . TRP D 1 77  ? -1.961  34.528  37.843  1.00 19.73 ? 65  TRP D CE3 1 
ATOM   4884 C  CZ2 . TRP D 1 77  ? -0.381  34.377  35.497  1.00 20.48 ? 65  TRP D CZ2 1 
ATOM   4885 C  CZ3 . TRP D 1 77  ? -1.819  33.345  37.152  1.00 20.27 ? 65  TRP D CZ3 1 
ATOM   4886 C  CH2 . TRP D 1 77  ? -0.994  33.258  36.024  1.00 19.67 ? 65  TRP D CH2 1 
ATOM   4887 N  N   . ASN D 1 78  ? -4.854  38.320  37.025  1.00 17.74 ? 66  ASN D N   1 
ATOM   4888 C  CA  . ASN D 1 78  ? -6.092  38.001  36.281  1.00 21.29 ? 66  ASN D CA  1 
ATOM   4889 C  C   . ASN D 1 78  ? -5.784  37.929  34.780  1.00 19.25 ? 66  ASN D C   1 
ATOM   4890 O  O   . ASN D 1 78  ? -6.288  38.768  34.026  1.00 17.11 ? 66  ASN D O   1 
ATOM   4891 C  CB  . ASN D 1 78  ? -7.173  39.043  36.570  1.00 23.86 ? 66  ASN D CB  1 
ATOM   4892 C  CG  . ASN D 1 78  ? -7.467  39.154  38.059  1.00 31.79 ? 66  ASN D CG  1 
ATOM   4893 O  OD1 . ASN D 1 78  ? -7.800  38.161  38.684  1.00 29.12 ? 66  ASN D OD1 1 
ATOM   4894 N  ND2 . ASN D 1 78  ? -7.332  40.343  38.629  1.00 30.37 ? 66  ASN D ND2 1 
ATOM   4895 N  N   . PRO D 1 79  ? -4.982  36.957  34.300  1.00 20.68 ? 67  PRO D N   1 
ATOM   4896 C  CA  . PRO D 1 79  ? -4.721  36.829  32.865  1.00 19.98 ? 67  PRO D CA  1 
ATOM   4897 C  C   . PRO D 1 79  ? -5.888  36.183  32.120  1.00 22.82 ? 67  PRO D C   1 
ATOM   4898 O  O   . PRO D 1 79  ? -6.649  35.398  32.708  1.00 21.58 ? 67  PRO D O   1 
ATOM   4899 C  CB  . PRO D 1 79  ? -3.490  35.944  32.803  1.00 23.44 ? 67  PRO D CB  1 
ATOM   4900 C  CG  . PRO D 1 79  ? -3.661  35.027  33.989  1.00 23.11 ? 67  PRO D CG  1 
ATOM   4901 C  CD  . PRO D 1 79  ? -4.244  35.927  35.067  1.00 22.88 ? 67  PRO D CD  1 
ATOM   4902 N  N   . ASN D 1 80  ? -6.034  36.591  30.865  1.00 20.36 ? 68  ASN D N   1 
ATOM   4903 C  CA  . ASN D 1 80  ? -6.843  35.902  29.837  1.00 21.44 ? 68  ASN D CA  1 
ATOM   4904 C  C   . ASN D 1 80  ? -5.882  35.514  28.707  1.00 20.97 ? 68  ASN D C   1 
ATOM   4905 O  O   . ASN D 1 80  ? -5.773  36.280  27.761  1.00 18.42 ? 68  ASN D O   1 
ATOM   4906 C  CB  . ASN D 1 80  ? -7.995  36.793  29.388  1.00 26.57 ? 68  ASN D CB  1 
ATOM   4907 C  CG  . ASN D 1 80  ? -9.010  36.018  28.578  1.00 31.03 ? 68  ASN D CG  1 
ATOM   4908 O  OD1 . ASN D 1 80  ? -8.970  34.792  28.557  1.00 35.82 ? 68  ASN D OD1 1 
ATOM   4909 N  ND2 . ASN D 1 80  ? -9.904  36.722  27.906  1.00 39.92 ? 68  ASN D ND2 1 
ATOM   4910 N  N   . GLY D 1 81  ? -5.259  34.346  28.831  1.00 19.76 ? 69  GLY D N   1 
ATOM   4911 C  CA  . GLY D 1 81  ? -4.192  33.789  27.981  1.00 19.34 ? 69  GLY D CA  1 
ATOM   4912 C  C   . GLY D 1 81  ? -2.830  33.800  28.662  1.00 19.39 ? 69  GLY D C   1 
ATOM   4913 O  O   . GLY D 1 81  ? -2.754  33.943  29.906  1.00 20.38 ? 69  GLY D O   1 
ATOM   4914 N  N   . ASN D 1 82  ? -1.793  33.698  27.845  1.00 18.40 ? 70  ASN D N   1 
ATOM   4915 C  CA  . ASN D 1 82  ? -0.379  33.439  28.221  1.00 17.64 ? 70  ASN D CA  1 
ATOM   4916 C  C   . ASN D 1 82  ? 0.164   34.557  29.131  1.00 16.95 ? 70  ASN D C   1 
ATOM   4917 O  O   . ASN D 1 82  ? 0.344   35.693  28.678  1.00 15.70 ? 70  ASN D O   1 
ATOM   4918 C  CB  . ASN D 1 82  ? 0.507   33.280  26.972  1.00 18.88 ? 70  ASN D CB  1 
ATOM   4919 C  CG  . ASN D 1 82  ? 1.921   32.830  27.288  1.00 21.23 ? 70  ASN D CG  1 
ATOM   4920 O  OD1 . ASN D 1 82  ? 2.294   32.734  28.444  1.00 26.34 ? 70  ASN D OD1 1 
ATOM   4921 N  ND2 . ASN D 1 82  ? 2.744   32.559  26.289  1.00 24.84 ? 70  ASN D ND2 1 
ATOM   4922 N  N   . SER D 1 83  ? 0.476   34.221  30.380  1.00 15.19 ? 71  SER D N   1 
ATOM   4923 C  CA  . SER D 1 83  ? 1.023   35.162  31.385  1.00 15.90 ? 71  SER D CA  1 
ATOM   4924 C  C   . SER D 1 83  ? 1.739   34.348  32.458  1.00 17.29 ? 71  SER D C   1 
ATOM   4925 O  O   . SER D 1 83  ? 1.372   33.154  32.691  1.00 16.58 ? 71  SER D O   1 
ATOM   4926 C  CB  . SER D 1 83  ? -0.077  36.058  31.940  1.00 15.48 ? 71  SER D CB  1 
ATOM   4927 O  OG  . SER D 1 83  ? 0.410   36.987  32.896  1.00 17.74 ? 71  SER D OG  1 
ATOM   4928 N  N   . TYR D 1 84  ? 2.769   34.923  33.069  1.00 18.10 ? 72  TYR D N   1 
ATOM   4929 C  CA  . TYR D 1 84  ? 3.548   34.261  34.145  1.00 20.01 ? 72  TYR D CA  1 
ATOM   4930 C  C   . TYR D 1 84  ? 3.623   35.285  35.279  1.00 17.75 ? 72  TYR D C   1 
ATOM   4931 O  O   . TYR D 1 84  ? 3.591   36.481  34.969  1.00 15.67 ? 72  TYR D O   1 
ATOM   4932 C  CB  . TYR D 1 84  ? 4.989   33.899  33.744  1.00 22.96 ? 72  TYR D CB  1 
ATOM   4933 C  CG  . TYR D 1 84  ? 5.357   33.565  32.314  1.00 29.39 ? 72  TYR D CG  1 
ATOM   4934 C  CD1 . TYR D 1 84  ? 4.630   32.667  31.554  1.00 35.61 ? 72  TYR D CD1 1 
ATOM   4935 C  CD2 . TYR D 1 84  ? 6.552   34.029  31.772  1.00 36.22 ? 72  TYR D CD2 1 
ATOM   4936 C  CE1 . TYR D 1 84  ? 5.023   32.301  30.272  1.00 41.22 ? 72  TYR D CE1 1 
ATOM   4937 C  CE2 . TYR D 1 84  ? 6.967   33.674  30.498  1.00 38.85 ? 72  TYR D CE2 1 
ATOM   4938 C  CZ  . TYR D 1 84  ? 6.194   32.815  29.734  1.00 42.72 ? 72  TYR D CZ  1 
ATOM   4939 O  OH  . TYR D 1 84  ? 6.592   32.457  28.473  1.00 46.86 ? 72  TYR D OH  1 
ATOM   4940 N  N   . LEU D 1 85  ? 3.609   34.831  36.532  1.00 14.88 ? 73  LEU D N   1 
ATOM   4941 C  CA  . LEU D 1 85  ? 3.937   35.665  37.719  1.00 14.27 ? 73  LEU D CA  1 
ATOM   4942 C  C   . LEU D 1 85  ? 5.202   35.042  38.328  1.00 14.41 ? 73  LEU D C   1 
ATOM   4943 O  O   . LEU D 1 85  ? 5.230   33.837  38.610  1.00 12.79 ? 73  LEU D O   1 
ATOM   4944 C  CB  . LEU D 1 85  ? 2.736   35.661  38.672  1.00 14.66 ? 73  LEU D CB  1 
ATOM   4945 C  CG  . LEU D 1 85  ? 2.876   36.452  39.966  1.00 15.66 ? 73  LEU D CG  1 
ATOM   4946 C  CD1 . LEU D 1 85  ? 3.004   37.933  39.687  1.00 16.58 ? 73  LEU D CD1 1 
ATOM   4947 C  CD2 . LEU D 1 85  ? 1.660   36.197  40.855  1.00 17.86 ? 73  LEU D CD2 1 
ATOM   4948 N  N   . SER D 1 86  ? 6.315   35.758  38.351  1.00 15.11 ? 74  SER D N   1 
ATOM   4949 C  CA  . SER D 1 86  ? 7.616   35.168  38.732  1.00 16.37 ? 74  SER D CA  1 
ATOM   4950 C  C   . SER D 1 86  ? 8.451   36.193  39.491  1.00 16.50 ? 74  SER D C   1 
ATOM   4951 O  O   . SER D 1 86  ? 8.260   37.409  39.308  1.00 16.50 ? 74  SER D O   1 
ATOM   4952 C  CB  . SER D 1 86  ? 8.419   34.634  37.541  1.00 19.62 ? 74  SER D CB  1 
ATOM   4953 O  OG  . SER D 1 86  ? 8.892   35.706  36.739  1.00 29.73 ? 74  SER D OG  1 
ATOM   4954 N  N   . VAL D 1 87  ? 9.360   35.711  40.323  1.00 14.03 ? 75  VAL D N   1 
ATOM   4955 C  CA  . VAL D 1 87  ? 10.542  36.527  40.667  1.00 14.22 ? 75  VAL D CA  1 
ATOM   4956 C  C   . VAL D 1 87  ? 11.474  36.404  39.462  1.00 16.09 ? 75  VAL D C   1 
ATOM   4957 O  O   . VAL D 1 87  ? 11.687  35.254  39.010  1.00 18.00 ? 75  VAL D O   1 
ATOM   4958 C  CB  . VAL D 1 87  ? 11.189  36.045  41.957  1.00 15.84 ? 75  VAL D CB  1 
ATOM   4959 C  CG1 . VAL D 1 87  ? 12.459  36.834  42.257  1.00 16.47 ? 75  VAL D CG1 1 
ATOM   4960 C  CG2 . VAL D 1 87  ? 10.195  36.138  43.096  1.00 15.61 ? 75  VAL D CG2 1 
ATOM   4961 N  N   . TYR D 1 88  ? 11.953  37.520  38.937  1.00 13.00 ? 76  TYR D N   1 
ATOM   4962 C  CA  . TYR D 1 88  ? 12.635  37.580  37.624  1.00 13.27 ? 76  TYR D CA  1 
ATOM   4963 C  C   . TYR D 1 88  ? 13.880  38.441  37.802  1.00 14.14 ? 76  TYR D C   1 
ATOM   4964 O  O   . TYR D 1 88  ? 13.771  39.535  38.353  1.00 12.54 ? 76  TYR D O   1 
ATOM   4965 C  CB  . TYR D 1 88  ? 11.673  38.110  36.562  1.00 16.44 ? 76  TYR D CB  1 
ATOM   4966 C  CG  . TYR D 1 88  ? 12.328  38.430  35.243  1.00 17.57 ? 76  TYR D CG  1 
ATOM   4967 C  CD1 . TYR D 1 88  ? 12.777  37.426  34.398  1.00 20.51 ? 76  TYR D CD1 1 
ATOM   4968 C  CD2 . TYR D 1 88  ? 12.477  39.735  34.820  1.00 18.77 ? 76  TYR D CD2 1 
ATOM   4969 C  CE1 . TYR D 1 88  ? 13.387  37.712  33.179  1.00 21.01 ? 76  TYR D CE1 1 
ATOM   4970 C  CE2 . TYR D 1 88  ? 13.107  40.030  33.614  1.00 22.11 ? 76  TYR D CE2 1 
ATOM   4971 C  CZ  . TYR D 1 88  ? 13.563  39.023  32.789  1.00 21.42 ? 76  TYR D CZ  1 
ATOM   4972 O  OH  . TYR D 1 88  ? 14.175  39.335  31.592  1.00 23.15 ? 76  TYR D OH  1 
ATOM   4973 N  N   . GLY D 1 89  ? 15.010  38.003  37.286  1.00 13.22 ? 77  GLY D N   1 
ATOM   4974 C  CA  . GLY D 1 89  ? 16.215  38.824  37.477  1.00 14.89 ? 77  GLY D CA  1 
ATOM   4975 C  C   . GLY D 1 89  ? 17.369  38.369  36.617  1.00 16.64 ? 77  GLY D C   1 
ATOM   4976 O  O   . GLY D 1 89  ? 17.231  37.400  35.842  1.00 13.55 ? 77  GLY D O   1 
ATOM   4977 N  N   . TRP D 1 90  ? 18.487  39.066  36.767  1.00 16.80 ? 78  TRP D N   1 
ATOM   4978 C  CA  . TRP D 1 90  ? 19.699  38.787  35.969  1.00 18.59 ? 78  TRP D CA  1 
ATOM   4979 C  C   . TRP D 1 90  ? 20.914  38.678  36.893  1.00 19.58 ? 78  TRP D C   1 
ATOM   4980 O  O   . TRP D 1 90  ? 20.978  39.374  37.900  1.00 21.29 ? 78  TRP D O   1 
ATOM   4981 C  CB  . TRP D 1 90  ? 19.930  39.892  34.935  1.00 18.26 ? 78  TRP D CB  1 
ATOM   4982 C  CG  . TRP D 1 90  ? 18.973  39.856  33.793  1.00 20.49 ? 78  TRP D CG  1 
ATOM   4983 C  CD1 . TRP D 1 90  ? 17.699  40.340  33.789  1.00 21.80 ? 78  TRP D CD1 1 
ATOM   4984 C  CD2 . TRP D 1 90  ? 19.174  39.230  32.514  1.00 23.01 ? 78  TRP D CD2 1 
ATOM   4985 N  NE1 . TRP D 1 90  ? 17.105  40.083  32.582  1.00 24.55 ? 78  TRP D NE1 1 
ATOM   4986 C  CE2 . TRP D 1 90  ? 17.991  39.422  31.774  1.00 21.93 ? 78  TRP D CE2 1 
ATOM   4987 C  CE3 . TRP D 1 90  ? 20.257  38.599  31.889  1.00 23.80 ? 78  TRP D CE3 1 
ATOM   4988 C  CZ2 . TRP D 1 90  ? 17.865  39.016  30.447  1.00 24.94 ? 78  TRP D CZ2 1 
ATOM   4989 C  CZ3 . TRP D 1 90  ? 20.111  38.138  30.600  1.00 25.00 ? 78  TRP D CZ3 1 
ATOM   4990 C  CH2 . TRP D 1 90  ? 18.928  38.350  29.884  1.00 25.55 ? 78  TRP D CH2 1 
ATOM   4991 N  N   . THR D 1 91  ? 21.929  37.957  36.426  1.00 21.45 ? 79  THR D N   1 
ATOM   4992 C  CA  . THR D 1 91  ? 23.301  38.067  36.957  1.00 21.47 ? 79  THR D CA  1 
ATOM   4993 C  C   . THR D 1 91  ? 24.233  38.295  35.777  1.00 22.33 ? 79  THR D C   1 
ATOM   4994 O  O   . THR D 1 91  ? 23.820  38.040  34.630  1.00 22.86 ? 79  THR D O   1 
ATOM   4995 C  CB  . THR D 1 91  ? 23.734  36.830  37.765  1.00 24.42 ? 79  THR D CB  1 
ATOM   4996 O  OG1 . THR D 1 91  ? 24.075  35.725  36.919  1.00 23.80 ? 79  THR D OG1 1 
ATOM   4997 C  CG2 . THR D 1 91  ? 22.665  36.414  38.757  1.00 23.88 ? 79  THR D CG2 1 
ATOM   4998 N  N   . GLN D 1 92  ? 25.436  38.755  36.103  1.00 23.87 ? 80  GLN D N   1 
ATOM   4999 C  CA  . GLN D 1 92  ? 26.525  39.016  35.120  1.00 27.24 ? 80  GLN D CA  1 
ATOM   5000 C  C   . GLN D 1 92  ? 27.778  38.249  35.576  1.00 25.93 ? 80  GLN D C   1 
ATOM   5001 O  O   . GLN D 1 92  ? 27.982  38.074  36.795  1.00 25.17 ? 80  GLN D O   1 
ATOM   5002 C  CB  . GLN D 1 92  ? 26.738  40.535  34.989  1.00 28.04 ? 80  GLN D CB  1 
ATOM   5003 C  CG  . GLN D 1 92  ? 25.588  41.249  34.294  1.00 30.20 ? 80  GLN D CG  1 
ATOM   5004 C  CD  . GLN D 1 92  ? 25.749  42.750  34.334  1.00 30.68 ? 80  GLN D CD  1 
ATOM   5005 O  OE1 . GLN D 1 92  ? 25.429  43.395  35.329  1.00 30.85 ? 80  GLN D OE1 1 
ATOM   5006 N  NE2 . GLN D 1 92  ? 26.266  43.310  33.250  1.00 32.86 ? 80  GLN D NE2 1 
ATOM   5007 N  N   . ASN D 1 93  ? 28.601  37.810  34.625  1.00 29.91 ? 81  ASN D N   1 
ATOM   5008 C  CA  . ASN D 1 93  ? 29.921  37.190  34.913  1.00 31.41 ? 81  ASN D CA  1 
ATOM   5009 C  C   . ASN D 1 93  ? 29.726  35.970  35.806  1.00 29.07 ? 81  ASN D C   1 
ATOM   5010 O  O   . ASN D 1 93  ? 30.249  35.912  36.918  1.00 32.59 ? 81  ASN D O   1 
ATOM   5011 C  CB  . ASN D 1 93  ? 30.875  38.244  35.491  1.00 34.84 ? 81  ASN D CB  1 
ATOM   5012 C  CG  . ASN D 1 93  ? 31.245  39.289  34.460  1.00 37.15 ? 81  ASN D CG  1 
ATOM   5013 O  OD1 . ASN D 1 93  ? 30.951  39.132  33.278  1.00 43.51 ? 81  ASN D OD1 1 
ATOM   5014 N  ND2 . ASN D 1 93  ? 31.861  40.376  34.895  1.00 43.25 ? 81  ASN D ND2 1 
ATOM   5015 N  N   . PRO D 1 94  ? 28.962  34.949  35.351  1.00 31.08 ? 82  PRO D N   1 
ATOM   5016 C  CA  . PRO D 1 94  ? 28.364  34.930  34.014  1.00 27.09 ? 82  PRO D CA  1 
ATOM   5017 C  C   . PRO D 1 94  ? 26.954  35.529  33.865  1.00 28.80 ? 82  PRO D C   1 
ATOM   5018 O  O   . PRO D 1 94  ? 26.250  35.722  34.889  1.00 25.58 ? 82  PRO D O   1 
ATOM   5019 C  CB  . PRO D 1 94  ? 28.264  33.411  33.807  1.00 32.53 ? 82  PRO D CB  1 
ATOM   5020 C  CG  . PRO D 1 94  ? 27.808  32.930  35.141  1.00 30.77 ? 82  PRO D CG  1 
ATOM   5021 C  CD  . PRO D 1 94  ? 28.665  33.718  36.106  1.00 31.90 ? 82  PRO D CD  1 
ATOM   5022 N  N   . LEU D 1 95  ? 26.575  35.791  32.607  1.00 27.17 ? 83  LEU D N   1 
ATOM   5023 C  CA  . LEU D 1 95  ? 25.279  36.388  32.223  1.00 26.41 ? 83  LEU D CA  1 
ATOM   5024 C  C   . LEU D 1 95  ? 24.203  35.310  32.394  1.00 25.06 ? 83  LEU D C   1 
ATOM   5025 O  O   . LEU D 1 95  ? 24.267  34.284  31.710  1.00 24.37 ? 83  LEU D O   1 
ATOM   5026 C  CB  . LEU D 1 95  ? 25.355  36.927  30.790  1.00 26.55 ? 83  LEU D CB  1 
ATOM   5027 C  CG  . LEU D 1 95  ? 24.135  37.707  30.294  1.00 26.77 ? 83  LEU D CG  1 
ATOM   5028 C  CD1 . LEU D 1 95  ? 23.841  38.912  31.176  1.00 25.28 ? 83  LEU D CD1 1 
ATOM   5029 C  CD2 . LEU D 1 95  ? 24.260  38.146  28.841  1.00 29.27 ? 83  LEU D CD2 1 
ATOM   5030 N  N   . VAL D 1 96  ? 23.199  35.554  33.228  1.00 22.22 ? 84  VAL D N   1 
ATOM   5031 C  CA  . VAL D 1 96  ? 22.139  34.544  33.513  1.00 23.05 ? 84  VAL D CA  1 
ATOM   5032 C  C   . VAL D 1 96  ? 20.829  35.308  33.671  1.00 22.58 ? 84  VAL D C   1 
ATOM   5033 O  O   . VAL D 1 96  ? 20.856  36.328  34.357  1.00 19.65 ? 84  VAL D O   1 
ATOM   5034 C  CB  . VAL D 1 96  ? 22.431  33.714  34.776  1.00 25.46 ? 84  VAL D CB  1 
ATOM   5035 C  CG1 . VAL D 1 96  ? 21.238  32.836  35.166  1.00 25.04 ? 84  VAL D CG1 1 
ATOM   5036 C  CG2 . VAL D 1 96  ? 23.686  32.877  34.652  1.00 26.31 ? 84  VAL D CG2 1 
ATOM   5037 N  N   . GLU D 1 97  ? 19.780  34.860  32.976  1.00 21.21 ? 85  GLU D N   1 
ATOM   5038 C  CA  . GLU D 1 97  ? 18.373  35.296  33.176  1.00 21.13 ? 85  GLU D CA  1 
ATOM   5039 C  C   . GLU D 1 97  ? 17.690  34.205  34.006  1.00 18.65 ? 85  GLU D C   1 
ATOM   5040 O  O   . GLU D 1 97  ? 17.857  33.012  33.684  1.00 20.49 ? 85  GLU D O   1 
ATOM   5041 C  CB  . GLU D 1 97  ? 17.714  35.495  31.817  1.00 21.61 ? 85  GLU D CB  1 
ATOM   5042 C  CG  . GLU D 1 97  ? 16.287  35.980  31.897  1.00 23.52 ? 85  GLU D CG  1 
ATOM   5043 C  CD  . GLU D 1 97  ? 15.626  36.178  30.550  1.00 24.83 ? 85  GLU D CD  1 
ATOM   5044 O  OE1 . GLU D 1 97  ? 14.961  37.216  30.355  1.00 26.57 ? 85  GLU D OE1 1 
ATOM   5045 O  OE2 . GLU D 1 97  ? 15.807  35.290  29.700  1.00 29.90 ? 85  GLU D OE2 1 
ATOM   5046 N  N   . TYR D 1 98  ? 17.024  34.544  35.103  1.00 16.51 ? 86  TYR D N   1 
ATOM   5047 C  CA  . TYR D 1 98  ? 16.453  33.496  35.972  1.00 15.61 ? 86  TYR D CA  1 
ATOM   5048 C  C   . TYR D 1 98  ? 15.012  33.886  36.303  1.00 14.53 ? 86  TYR D C   1 
ATOM   5049 O  O   . TYR D 1 98  ? 14.638  35.082  36.345  1.00 12.81 ? 86  TYR D O   1 
ATOM   5050 C  CB  . TYR D 1 98  ? 17.309  33.251  37.207  1.00 16.36 ? 86  TYR D CB  1 
ATOM   5051 C  CG  . TYR D 1 98  ? 17.389  34.416  38.167  1.00 16.70 ? 86  TYR D CG  1 
ATOM   5052 C  CD1 . TYR D 1 98  ? 16.371  34.668  39.077  1.00 18.50 ? 86  TYR D CD1 1 
ATOM   5053 C  CD2 . TYR D 1 98  ? 18.465  35.287  38.165  1.00 18.45 ? 86  TYR D CD2 1 
ATOM   5054 C  CE1 . TYR D 1 98  ? 16.407  35.744  39.938  1.00 17.60 ? 86  TYR D CE1 1 
ATOM   5055 C  CE2 . TYR D 1 98  ? 18.529  36.359  39.046  1.00 17.52 ? 86  TYR D CE2 1 
ATOM   5056 C  CZ  . TYR D 1 98  ? 17.497  36.596  39.926  1.00 19.43 ? 86  TYR D CZ  1 
ATOM   5057 O  OH  . TYR D 1 98  ? 17.557  37.632  40.806  1.00 18.95 ? 86  TYR D OH  1 
ATOM   5058 N  N   . TYR D 1 99  ? 14.242  32.846  36.585  1.00 14.36 ? 87  TYR D N   1 
ATOM   5059 C  CA  . TYR D 1 99  ? 12.801  32.946  36.883  1.00 15.22 ? 87  TYR D CA  1 
ATOM   5060 C  C   . TYR D 1 99  ? 12.458  31.989  38.010  1.00 15.68 ? 87  TYR D C   1 
ATOM   5061 O  O   . TYR D 1 99  ? 12.810  30.817  37.871  1.00 16.87 ? 87  TYR D O   1 
ATOM   5062 C  CB  . TYR D 1 99  ? 11.958  32.459  35.723  1.00 16.63 ? 87  TYR D CB  1 
ATOM   5063 C  CG  . TYR D 1 99  ? 12.095  33.209  34.442  1.00 17.51 ? 87  TYR D CG  1 
ATOM   5064 C  CD1 . TYR D 1 99  ? 13.195  33.014  33.615  1.00 17.97 ? 87  TYR D CD1 1 
ATOM   5065 C  CD2 . TYR D 1 99  ? 11.107  34.085  34.053  1.00 19.79 ? 87  TYR D CD2 1 
ATOM   5066 C  CE1 . TYR D 1 99  ? 13.303  33.709  32.425  1.00 19.92 ? 87  TYR D CE1 1 
ATOM   5067 C  CE2 . TYR D 1 99  ? 11.171  34.729  32.830  1.00 23.21 ? 87  TYR D CE2 1 
ATOM   5068 C  CZ  . TYR D 1 99  ? 12.286  34.550  32.034  1.00 22.28 ? 87  TYR D CZ  1 
ATOM   5069 O  OH  . TYR D 1 99  ? 12.378  35.167  30.829  1.00 30.65 ? 87  TYR D OH  1 
ATOM   5070 N  N   . ILE D 1 100 ? 11.777  32.484  39.035  1.00 14.28 ? 88  ILE D N   1 
ATOM   5071 C  CA  . ILE D 1 100 ? 11.088  31.660  40.056  1.00 13.85 ? 88  ILE D CA  1 
ATOM   5072 C  C   . ILE D 1 100 ? 9.593   31.868  39.825  1.00 12.74 ? 88  ILE D C   1 
ATOM   5073 O  O   . ILE D 1 100 ? 9.037   32.905  40.245  1.00 13.35 ? 88  ILE D O   1 
ATOM   5074 C  CB  . ILE D 1 100 ? 11.528  32.027  41.472  1.00 15.37 ? 88  ILE D CB  1 
ATOM   5075 C  CG1 . ILE D 1 100 ? 13.034  31.901  41.634  1.00 15.87 ? 88  ILE D CG1 1 
ATOM   5076 C  CG2 . ILE D 1 100 ? 10.802  31.176  42.503  1.00 14.89 ? 88  ILE D CG2 1 
ATOM   5077 C  CD1 . ILE D 1 100 ? 13.591  32.633  42.864  1.00 16.98 ? 88  ILE D CD1 1 
ATOM   5078 N  N   . VAL D 1 101 ? 8.997   30.936  39.062  1.00 14.62 ? 89  VAL D N   1 
ATOM   5079 C  CA  . VAL D 1 101 ? 7.627   31.088  38.511  1.00 14.50 ? 89  VAL D CA  1 
ATOM   5080 C  C   . VAL D 1 101 ? 6.625   30.599  39.564  1.00 14.77 ? 89  VAL D C   1 
ATOM   5081 O  O   . VAL D 1 101 ? 6.676   29.395  39.925  1.00 17.43 ? 89  VAL D O   1 
ATOM   5082 C  CB  . VAL D 1 101 ? 7.448   30.322  37.193  1.00 14.58 ? 89  VAL D CB  1 
ATOM   5083 C  CG1 . VAL D 1 101 ? 6.040   30.584  36.649  1.00 14.26 ? 89  VAL D CG1 1 
ATOM   5084 C  CG2 . VAL D 1 101 ? 8.535   30.660  36.172  1.00 14.45 ? 89  VAL D CG2 1 
ATOM   5085 N  N   . GLU D 1 102 ? 5.776   31.489  40.014  1.00 14.73 ? 90  GLU D N   1 
ATOM   5086 C  CA  . GLU D 1 102 ? 4.789   31.229  41.087  1.00 14.84 ? 90  GLU D CA  1 
ATOM   5087 C  C   . GLU D 1 102 ? 3.503   30.714  40.417  1.00 15.63 ? 90  GLU D C   1 
ATOM   5088 O  O   . GLU D 1 102 ? 2.771   29.910  41.005  1.00 15.28 ? 90  GLU D O   1 
ATOM   5089 C  CB  . GLU D 1 102 ? 4.529   32.497  41.890  1.00 16.14 ? 90  GLU D CB  1 
ATOM   5090 C  CG  . GLU D 1 102 ? 5.711   32.953  42.728  1.00 17.30 ? 90  GLU D CG  1 
ATOM   5091 C  CD  . GLU D 1 102 ? 5.923   32.042  43.910  1.00 18.50 ? 90  GLU D CD  1 
ATOM   5092 O  OE1 . GLU D 1 102 ? 6.731   31.143  43.773  1.00 20.84 ? 90  GLU D OE1 1 
ATOM   5093 O  OE2 . GLU D 1 102 ? 5.207   32.213  44.937  1.00 22.47 ? 90  GLU D OE2 1 
ATOM   5094 N  N   . SER D 1 103 ? 3.163   31.297  39.277  1.00 17.09 ? 91  SER D N   1 
ATOM   5095 C  CA  . SER D 1 103 ? 1.971   30.916  38.490  1.00 17.38 ? 91  SER D CA  1 
ATOM   5096 C  C   . SER D 1 103 ? 2.295   31.108  37.019  1.00 17.08 ? 91  SER D C   1 
ATOM   5097 O  O   . SER D 1 103 ? 3.022   32.011  36.695  1.00 15.07 ? 91  SER D O   1 
ATOM   5098 C  CB  . SER D 1 103 ? 0.723   31.694  38.809  1.00 20.75 ? 91  SER D CB  1 
ATOM   5099 O  OG  . SER D 1 103 ? 0.222   31.454  40.119  1.00 23.09 ? 91  SER D OG  1 
ATOM   5100 N  N   . PHE D 1 104 ? 1.663   30.302  36.181  1.00 17.07 ? 92  PHE D N   1 
ATOM   5101 C  CA  . PHE D 1 104 ? 1.555   30.534  34.727  1.00 16.87 ? 92  PHE D CA  1 
ATOM   5102 C  C   . PHE D 1 104 ? 0.146   30.120  34.285  1.00 18.32 ? 92  PHE D C   1 
ATOM   5103 O  O   . PHE D 1 104 ? -0.551  29.394  35.008  1.00 17.68 ? 92  PHE D O   1 
ATOM   5104 C  CB  . PHE D 1 104 ? 2.707   29.872  33.982  1.00 17.10 ? 92  PHE D CB  1 
ATOM   5105 C  CG  . PHE D 1 104 ? 2.658   28.371  33.915  1.00 16.43 ? 92  PHE D CG  1 
ATOM   5106 C  CD1 . PHE D 1 104 ? 1.683   27.728  33.155  1.00 18.33 ? 92  PHE D CD1 1 
ATOM   5107 C  CD2 . PHE D 1 104 ? 3.557   27.609  34.630  1.00 19.03 ? 92  PHE D CD2 1 
ATOM   5108 C  CE1 . PHE D 1 104 ? 1.644   26.347  33.116  1.00 18.58 ? 92  PHE D CE1 1 
ATOM   5109 C  CE2 . PHE D 1 104 ? 3.534   26.225  34.563  1.00 20.80 ? 92  PHE D CE2 1 
ATOM   5110 C  CZ  . PHE D 1 104 ? 2.567   25.605  33.809  1.00 19.99 ? 92  PHE D CZ  1 
ATOM   5111 N  N   . SER D 1 105 ? -0.316  30.632  33.157  1.00 17.42 ? 93  SER D N   1 
ATOM   5112 C  CA  . SER D 1 105 ? -1.743  30.491  32.783  1.00 17.38 ? 93  SER D CA  1 
ATOM   5113 C  C   . SER D 1 105 ? -1.830  29.296  31.824  1.00 21.45 ? 93  SER D C   1 
ATOM   5114 O  O   . SER D 1 105 ? -1.760  28.141  32.297  1.00 25.30 ? 93  SER D O   1 
ATOM   5115 C  CB  . SER D 1 105 ? -2.293  31.783  32.250  1.00 19.85 ? 93  SER D CB  1 
ATOM   5116 O  OG  . SER D 1 105 ? -1.473  32.225  31.175  1.00 24.48 ? 93  SER D OG  1 
ATOM   5117 N  N   . THR D 1 106 ? -1.741  29.558  30.538  1.00 21.11 ? 94  THR D N   1 
ATOM   5118 C  CA  . THR D 1 106 ? -2.040  28.621  29.434  1.00 19.49 ? 94  THR D CA  1 
ATOM   5119 C  C   . THR D 1 106 ? -0.766  28.082  28.776  1.00 21.16 ? 94  THR D C   1 
ATOM   5120 O  O   . THR D 1 106 ? -0.859  27.248  27.852  1.00 22.21 ? 94  THR D O   1 
ATOM   5121 C  CB  . THR D 1 106 ? -2.943  29.365  28.452  1.00 21.31 ? 94  THR D CB  1 
ATOM   5122 O  OG1 . THR D 1 106 ? -2.175  30.475  27.993  1.00 22.92 ? 94  THR D OG1 1 
ATOM   5123 C  CG2 . THR D 1 106 ? -4.241  29.825  29.076  1.00 20.20 ? 94  THR D CG2 1 
ATOM   5124 N  N   . TYR D 1 107 ? 0.415   28.485  29.217  1.00 17.43 ? 95  TYR D N   1 
ATOM   5125 C  CA  . TYR D 1 107 ? 1.653   28.039  28.581  1.00 17.18 ? 95  TYR D CA  1 
ATOM   5126 C  C   . TYR D 1 107 ? 2.751   27.912  29.631  1.00 19.36 ? 95  TYR D C   1 
ATOM   5127 O  O   . TYR D 1 107 ? 3.015   28.911  30.306  1.00 23.63 ? 95  TYR D O   1 
ATOM   5128 C  CB  . TYR D 1 107 ? 2.096   29.032  27.517  1.00 17.55 ? 95  TYR D CB  1 
ATOM   5129 C  CG  . TYR D 1 107 ? 3.331   28.610  26.793  1.00 17.68 ? 95  TYR D CG  1 
ATOM   5130 C  CD1 . TYR D 1 107 ? 3.309   27.628  25.822  1.00 20.15 ? 95  TYR D CD1 1 
ATOM   5131 C  CD2 . TYR D 1 107 ? 4.546   29.204  27.082  1.00 21.37 ? 95  TYR D CD2 1 
ATOM   5132 C  CE1 . TYR D 1 107 ? 4.459   27.270  25.147  1.00 22.88 ? 95  TYR D CE1 1 
ATOM   5133 C  CE2 . TYR D 1 107 ? 5.694   28.879  26.401  1.00 23.02 ? 95  TYR D CE2 1 
ATOM   5134 C  CZ  . TYR D 1 107 ? 5.661   27.885  25.440  1.00 22.72 ? 95  TYR D CZ  1 
ATOM   5135 O  OH  . TYR D 1 107 ? 6.804   27.545  24.793  1.00 23.58 ? 95  TYR D OH  1 
ATOM   5136 N  N   . ASP D 1 108 ? 3.376   26.760  29.711  1.00 22.00 ? 96  ASP D N   1 
ATOM   5137 C  CA  . ASP D 1 108 ? 4.441   26.509  30.713  1.00 23.32 ? 96  ASP D CA  1 
ATOM   5138 C  C   . ASP D 1 108 ? 5.712   27.127  30.146  1.00 25.27 ? 96  ASP D C   1 
ATOM   5139 O  O   . ASP D 1 108 ? 6.233   26.607  29.168  1.00 25.76 ? 96  ASP D O   1 
ATOM   5140 C  CB  . ASP D 1 108 ? 4.590   25.022  31.005  1.00 25.84 ? 96  ASP D CB  1 
ATOM   5141 C  CG  . ASP D 1 108 ? 5.609   24.737  32.092  1.00 28.25 ? 96  ASP D CG  1 
ATOM   5142 O  OD1 . ASP D 1 108 ? 6.374   25.671  32.411  1.00 28.48 ? 96  ASP D OD1 1 
ATOM   5143 O  OD2 . ASP D 1 108 ? 5.607   23.593  32.603  1.00 32.54 ? 96  ASP D OD2 1 
ATOM   5144 N  N   . PRO D 1 109 ? 6.179   28.270  30.699  1.00 28.97 ? 97  PRO D N   1 
ATOM   5145 C  CA  . PRO D 1 109 ? 7.284   29.023  30.102  1.00 33.18 ? 97  PRO D CA  1 
ATOM   5146 C  C   . PRO D 1 109 ? 8.590   28.231  30.144  1.00 34.36 ? 97  PRO D C   1 
ATOM   5147 O  O   . PRO D 1 109 ? 9.548   28.637  29.504  1.00 37.75 ? 97  PRO D O   1 
ATOM   5148 C  CB  . PRO D 1 109 ? 7.423   30.293  30.947  1.00 30.80 ? 97  PRO D CB  1 
ATOM   5149 C  CG  . PRO D 1 109 ? 6.653   30.027  32.223  1.00 32.71 ? 97  PRO D CG  1 
ATOM   5150 C  CD  . PRO D 1 109 ? 5.681   28.897  31.931  1.00 28.66 ? 97  PRO D CD  1 
ATOM   5151 N  N   . SER D 1 110 ? 8.590   27.150  30.919  1.00 34.13 ? 98  SER D N   1 
ATOM   5152 C  CA  . SER D 1 110 ? 9.709   26.196  31.037  1.00 36.33 ? 98  SER D CA  1 
ATOM   5153 C  C   . SER D 1 110 ? 9.752   25.241  29.836  1.00 33.80 ? 98  SER D C   1 
ATOM   5154 O  O   . SER D 1 110 ? 10.801  24.651  29.648  1.00 34.06 ? 98  SER D O   1 
ATOM   5155 C  CB  . SER D 1 110 ? 9.652   25.440  32.338  1.00 37.76 ? 98  SER D CB  1 
ATOM   5156 O  OG  . SER D 1 110 ? 9.454   24.057  32.105  1.00 40.45 ? 98  SER D OG  1 
ATOM   5157 N  N   . THR D 1 111 ? 8.673   25.110  29.046  1.00 34.95 ? 99  THR D N   1 
ATOM   5158 C  CA  . THR D 1 111 ? 8.628   24.283  27.808  1.00 32.19 ? 99  THR D CA  1 
ATOM   5159 C  C   . THR D 1 111 ? 9.893   24.557  26.973  1.00 33.27 ? 99  THR D C   1 
ATOM   5160 O  O   . THR D 1 111 ? 10.231  25.743  26.786  1.00 31.76 ? 99  THR D O   1 
ATOM   5161 C  CB  . THR D 1 111 ? 7.369   24.542  26.957  1.00 29.88 ? 99  THR D CB  1 
ATOM   5162 O  OG1 . THR D 1 111 ? 6.197   24.540  27.784  1.00 27.56 ? 99  THR D OG1 1 
ATOM   5163 C  CG2 . THR D 1 111 ? 7.165   23.482  25.896  1.00 32.58 ? 99  THR D CG2 1 
ATOM   5164 N  N   . GLY D 1 112 ? 10.569  23.492  26.527  1.00 31.60 ? 100 GLY D N   1 
ATOM   5165 C  CA  . GLY D 1 112 ? 11.825  23.554  25.744  1.00 36.42 ? 100 GLY D CA  1 
ATOM   5166 C  C   . GLY D 1 112 ? 13.085  23.561  26.609  1.00 35.25 ? 100 GLY D C   1 
ATOM   5167 O  O   . GLY D 1 112 ? 14.201  23.493  26.028  1.00 35.19 ? 100 GLY D O   1 
ATOM   5168 N  N   . ALA D 1 113 ? 12.956  23.664  27.939  1.00 35.64 ? 101 ALA D N   1 
ATOM   5169 C  CA  . ALA D 1 113 ? 14.092  23.658  28.902  1.00 34.13 ? 101 ALA D CA  1 
ATOM   5170 C  C   . ALA D 1 113 ? 14.258  22.257  29.496  1.00 33.93 ? 101 ALA D C   1 
ATOM   5171 O  O   . ALA D 1 113 ? 13.243  21.528  29.567  1.00 38.43 ? 101 ALA D O   1 
ATOM   5172 C  CB  . ALA D 1 113 ? 13.859  24.680  29.999  1.00 35.31 ? 101 ALA D CB  1 
ATOM   5173 N  N   . GLN D 1 114 ? 15.463  21.917  29.978  1.00 35.75 ? 102 GLN D N   1 
ATOM   5174 C  CA  . GLN D 1 114 ? 15.826  20.562  30.498  1.00 39.23 ? 102 GLN D CA  1 
ATOM   5175 C  C   . GLN D 1 114 ? 15.537  20.469  32.002  1.00 34.19 ? 102 GLN D C   1 
ATOM   5176 O  O   . GLN D 1 114 ? 16.037  21.333  32.752  1.00 29.88 ? 102 GLN D O   1 
ATOM   5177 C  CB  . GLN D 1 114 ? 17.308  20.244  30.259  1.00 44.83 ? 102 GLN D CB  1 
ATOM   5178 C  CG  . GLN D 1 114 ? 17.656  18.776  30.521  1.00 45.67 ? 102 GLN D CG  1 
ATOM   5179 C  CD  . GLN D 1 114 ? 19.130  18.473  30.663  1.00 47.48 ? 102 GLN D CD  1 
ATOM   5180 O  OE1 . GLN D 1 114 ? 19.570  17.347  30.436  1.00 52.17 ? 102 GLN D OE1 1 
ATOM   5181 N  NE2 . GLN D 1 114 ? 19.914  19.457  31.067  1.00 47.34 ? 102 GLN D NE2 1 
ATOM   5182 N  N   . GLU D 1 115 ? 14.798  19.441  32.427  1.00 33.03 ? 103 GLU D N   1 
ATOM   5183 C  CA  . GLU D 1 115 ? 14.393  19.227  33.849  1.00 32.71 ? 103 GLU D CA  1 
ATOM   5184 C  C   . GLU D 1 115 ? 15.572  18.652  34.646  1.00 31.18 ? 103 GLU D C   1 
ATOM   5185 O  O   . GLU D 1 115 ? 16.074  17.576  34.281  1.00 30.35 ? 103 GLU D O   1 
ATOM   5186 C  CB  . GLU D 1 115 ? 13.158  18.333  33.923  1.00 34.20 ? 103 GLU D CB  1 
ATOM   5187 C  CG  . GLU D 1 115 ? 12.594  18.225  35.327  1.00 38.65 ? 103 GLU D CG  1 
ATOM   5188 C  CD  . GLU D 1 115 ? 11.158  17.731  35.420  1.00 38.38 ? 103 GLU D CD  1 
ATOM   5189 O  OE1 . GLU D 1 115 ? 10.762  17.344  36.527  1.00 41.72 ? 103 GLU D OE1 1 
ATOM   5190 O  OE2 . GLU D 1 115 ? 10.439  17.771  34.395  1.00 41.21 ? 103 GLU D OE2 1 
ATOM   5191 N  N   . LEU D 1 116 ? 16.019  19.353  35.696  1.00 28.19 ? 104 LEU D N   1 
ATOM   5192 C  CA  . LEU D 1 116 ? 17.314  19.073  36.386  1.00 32.23 ? 104 LEU D CA  1 
ATOM   5193 C  C   . LEU D 1 116 ? 17.101  18.548  37.813  1.00 34.10 ? 104 LEU D C   1 
ATOM   5194 O  O   . LEU D 1 116 ? 18.114  18.087  38.409  1.00 38.42 ? 104 LEU D O   1 
ATOM   5195 C  CB  . LEU D 1 116 ? 18.143  20.361  36.390  1.00 32.31 ? 104 LEU D CB  1 
ATOM   5196 C  CG  . LEU D 1 116 ? 19.318  20.481  35.413  1.00 35.37 ? 104 LEU D CG  1 
ATOM   5197 C  CD1 . LEU D 1 116 ? 19.195  19.579  34.188  1.00 37.11 ? 104 LEU D CD1 1 
ATOM   5198 C  CD2 . LEU D 1 116 ? 19.521  21.925  34.966  1.00 35.85 ? 104 LEU D CD2 1 
ATOM   5199 N  N   . GLY D 1 117 ? 15.886  18.638  38.362  1.00 32.24 ? 105 GLY D N   1 
ATOM   5200 C  CA  . GLY D 1 117 ? 15.571  18.248  39.753  1.00 32.31 ? 105 GLY D CA  1 
ATOM   5201 C  C   . GLY D 1 117 ? 14.423  19.068  40.316  1.00 31.70 ? 105 GLY D C   1 
ATOM   5202 O  O   . GLY D 1 117 ? 13.695  19.697  39.507  1.00 28.45 ? 105 GLY D O   1 
ATOM   5203 N  N   . THR D 1 118 ? 14.231  19.028  41.641  1.00 30.30 ? 106 THR D N   1 
ATOM   5204 C  CA  . THR D 1 118 ? 13.240  19.854  42.380  1.00 30.67 ? 106 THR D CA  1 
ATOM   5205 C  C   . THR D 1 118 ? 13.886  20.526  43.594  1.00 28.88 ? 106 THR D C   1 
ATOM   5206 O  O   . THR D 1 118 ? 14.953  20.068  44.040  1.00 30.98 ? 106 THR D O   1 
ATOM   5207 C  CB  . THR D 1 118 ? 12.012  19.080  42.881  1.00 33.39 ? 106 THR D CB  1 
ATOM   5208 O  OG1 . THR D 1 118 ? 12.417  18.136  43.877  1.00 38.62 ? 106 THR D OG1 1 
ATOM   5209 C  CG2 . THR D 1 118 ? 11.266  18.394  41.761  1.00 32.91 ? 106 THR D CG2 1 
ATOM   5210 N  N   . VAL D 1 119 ? 13.220  21.563  44.108  1.00 27.30 ? 107 VAL D N   1 
ATOM   5211 C  CA  . VAL D 1 119 ? 13.548  22.238  45.391  1.00 26.61 ? 107 VAL D CA  1 
ATOM   5212 C  C   . VAL D 1 119 ? 12.243  22.383  46.181  1.00 27.45 ? 107 VAL D C   1 
ATOM   5213 O  O   . VAL D 1 119 ? 11.225  22.790  45.601  1.00 22.33 ? 107 VAL D O   1 
ATOM   5214 C  CB  . VAL D 1 119 ? 14.277  23.576  45.159  1.00 27.83 ? 107 VAL D CB  1 
ATOM   5215 C  CG1 . VAL D 1 119 ? 13.457  24.597  44.356  1.00 25.91 ? 107 VAL D CG1 1 
ATOM   5216 C  CG2 . VAL D 1 119 ? 14.730  24.177  46.471  1.00 27.43 ? 107 VAL D CG2 1 
ATOM   5217 N  N   . GLU D 1 120 ? 12.253  22.007  47.457  1.00 26.98 ? 108 GLU D N   1 
ATOM   5218 C  CA  . GLU D 1 120 ? 11.109  22.256  48.365  1.00 29.62 ? 108 GLU D CA  1 
ATOM   5219 C  C   . GLU D 1 120 ? 11.398  23.543  49.141  1.00 27.26 ? 108 GLU D C   1 
ATOM   5220 O  O   . GLU D 1 120 ? 12.442  23.613  49.807  1.00 28.13 ? 108 GLU D O   1 
ATOM   5221 C  CB  . GLU D 1 120 ? 10.907  21.074  49.319  1.00 34.39 ? 108 GLU D CB  1 
ATOM   5222 C  CG  . GLU D 1 120 ? 10.549  19.785  48.604  1.00 40.71 ? 108 GLU D CG  1 
ATOM   5223 C  CD  . GLU D 1 120 ? 9.973   18.701  49.500  1.00 44.86 ? 108 GLU D CD  1 
ATOM   5224 O  OE1 . GLU D 1 120 ? 9.267   17.815  48.968  1.00 53.72 ? 108 GLU D OE1 1 
ATOM   5225 O  OE2 . GLU D 1 120 ? 10.225  18.743  50.725  1.00 51.43 ? 108 GLU D OE2 1 
ATOM   5226 N  N   . THR D 1 121 ? 10.513  24.532  49.060  1.00 26.72 ? 109 THR D N   1 
ATOM   5227 C  CA  . THR D 1 121 ? 10.678  25.821  49.772  1.00 25.05 ? 109 THR D CA  1 
ATOM   5228 C  C   . THR D 1 121 ? 9.354   26.571  49.795  1.00 24.84 ? 109 THR D C   1 
ATOM   5229 O  O   . THR D 1 121 ? 8.554   26.395  48.847  1.00 22.79 ? 109 THR D O   1 
ATOM   5230 C  CB  . THR D 1 121 ? 11.812  26.643  49.142  1.00 28.20 ? 109 THR D CB  1 
ATOM   5231 O  OG1 . THR D 1 121 ? 11.919  27.835  49.916  1.00 27.99 ? 109 THR D OG1 1 
ATOM   5232 C  CG2 . THR D 1 121 ? 11.571  26.974  47.693  1.00 27.58 ? 109 THR D CG2 1 
ATOM   5233 N  N   . ASP D 1 122 ? 9.115   27.341  50.859  1.00 23.34 ? 110 ASP D N   1 
ATOM   5234 C  CA  . ASP D 1 122 ? 7.912   28.184  50.969  1.00 22.71 ? 110 ASP D CA  1 
ATOM   5235 C  C   . ASP D 1 122 ? 6.663   27.312  50.738  1.00 23.12 ? 110 ASP D C   1 
ATOM   5236 O  O   . ASP D 1 122 ? 5.781   27.723  49.945  1.00 22.83 ? 110 ASP D O   1 
ATOM   5237 C  CB  . ASP D 1 122 ? 8.094   29.359  50.002  1.00 20.31 ? 110 ASP D CB  1 
ATOM   5238 C  CG  . ASP D 1 122 ? 9.412   30.092  50.254  1.00 21.95 ? 110 ASP D CG  1 
ATOM   5239 O  OD1 . ASP D 1 122 ? 9.562   30.649  51.383  1.00 22.50 ? 110 ASP D OD1 1 
ATOM   5240 O  OD2 . ASP D 1 122 ? 10.300  30.116  49.324  1.00 20.01 ? 110 ASP D OD2 1 
ATOM   5241 N  N   . ASP D 1 123 ? 6.613   26.122  51.352  1.00 24.47 ? 111 ASP D N   1 
ATOM   5242 C  CA  . ASP D 1 123 ? 5.411   25.234  51.404  1.00 26.65 ? 111 ASP D CA  1 
ATOM   5243 C  C   . ASP D 1 123 ? 5.021   24.755  49.996  1.00 26.21 ? 111 ASP D C   1 
ATOM   5244 O  O   . ASP D 1 123 ? 3.843   24.393  49.759  1.00 25.64 ? 111 ASP D O   1 
ATOM   5245 C  CB  . ASP D 1 123 ? 4.294   25.938  52.171  1.00 30.17 ? 111 ASP D CB  1 
ATOM   5246 C  CG  . ASP D 1 123 ? 4.521   25.924  53.681  1.00 36.70 ? 111 ASP D CG  1 
ATOM   5247 O  OD1 . ASP D 1 123 ? 4.302   24.854  54.284  1.00 43.96 ? 111 ASP D OD1 1 
ATOM   5248 O  OD2 . ASP D 1 123 ? 4.906   26.983  54.250  1.00 37.76 ? 111 ASP D OD2 1 
ATOM   5249 N  N   . GLY D 1 124 ? 6.007   24.684  49.106  1.00 24.60 ? 112 GLY D N   1 
ATOM   5250 C  CA  . GLY D 1 124 ? 5.831   24.368  47.687  1.00 24.11 ? 112 GLY D CA  1 
ATOM   5251 C  C   . GLY D 1 124 ? 6.937   23.479  47.199  1.00 21.53 ? 112 GLY D C   1 
ATOM   5252 O  O   . GLY D 1 124 ? 8.000   23.359  47.863  1.00 24.74 ? 112 GLY D O   1 
ATOM   5253 N  N   . THR D 1 125 ? 6.697   22.854  46.067  1.00 22.74 ? 113 THR D N   1 
ATOM   5254 C  CA  . THR D 1 125 ? 7.731   22.153  45.296  1.00 20.82 ? 113 THR D CA  1 
ATOM   5255 C  C   . THR D 1 125 ? 7.918   22.910  43.989  1.00 20.80 ? 113 THR D C   1 
ATOM   5256 O  O   . THR D 1 125 ? 6.896   23.327  43.391  1.00 19.51 ? 113 THR D O   1 
ATOM   5257 C  CB  . THR D 1 125 ? 7.319   20.691  45.083  1.00 26.84 ? 113 THR D CB  1 
ATOM   5258 O  OG1 . THR D 1 125 ? 7.007   20.198  46.387  1.00 27.15 ? 113 THR D OG1 1 
ATOM   5259 C  CG2 . THR D 1 125 ? 8.378   19.871  44.384  1.00 27.38 ? 113 THR D CG2 1 
ATOM   5260 N  N   . TYR D 1 126 ? 9.165   23.040  43.554  1.00 19.61 ? 114 TYR D N   1 
ATOM   5261 C  CA  . TYR D 1 126 ? 9.526   23.772  42.318  1.00 20.15 ? 114 TYR D CA  1 
ATOM   5262 C  C   . TYR D 1 126 ? 10.389  22.868  41.447  1.00 20.55 ? 114 TYR D C   1 
ATOM   5263 O  O   . TYR D 1 126 ? 11.391  22.286  41.923  1.00 23.93 ? 114 TYR D O   1 
ATOM   5264 C  CB  . TYR D 1 126 ? 10.287  25.076  42.610  1.00 18.56 ? 114 TYR D CB  1 
ATOM   5265 C  CG  . TYR D 1 126 ? 9.519   26.142  43.334  1.00 16.99 ? 114 TYR D CG  1 
ATOM   5266 C  CD1 . TYR D 1 126 ? 9.245   26.057  44.690  1.00 15.04 ? 114 TYR D CD1 1 
ATOM   5267 C  CD2 . TYR D 1 126 ? 9.087   27.276  42.660  1.00 16.84 ? 114 TYR D CD2 1 
ATOM   5268 C  CE1 . TYR D 1 126 ? 8.560   27.048  45.373  1.00 15.30 ? 114 TYR D CE1 1 
ATOM   5269 C  CE2 . TYR D 1 126 ? 8.407   28.273  43.327  1.00 16.30 ? 114 TYR D CE2 1 
ATOM   5270 C  CZ  . TYR D 1 126 ? 8.144   28.173  44.683  1.00 15.33 ? 114 TYR D CZ  1 
ATOM   5271 O  OH  . TYR D 1 126 ? 7.470   29.181  45.289  1.00 16.02 ? 114 TYR D OH  1 
ATOM   5272 N  N   . LYS D 1 127 ? 10.003  22.727  40.184  1.00 21.13 ? 115 LYS D N   1 
ATOM   5273 C  CA  . LYS D 1 127 ? 10.802  21.976  39.187  1.00 21.93 ? 115 LYS D CA  1 
ATOM   5274 C  C   . LYS D 1 127 ? 11.879  22.903  38.634  1.00 23.11 ? 115 LYS D C   1 
ATOM   5275 O  O   . LYS D 1 127 ? 11.532  24.053  38.331  1.00 23.14 ? 115 LYS D O   1 
ATOM   5276 C  CB  . LYS D 1 127 ? 9.868   21.458  38.095  1.00 22.44 ? 115 LYS D CB  1 
ATOM   5277 C  CG  . LYS D 1 127 ? 8.881   20.408  38.579  1.00 25.62 ? 115 LYS D CG  1 
ATOM   5278 C  CD  . LYS D 1 127 ? 8.159   19.744  37.424  1.00 27.48 ? 115 LYS D CD  1 
ATOM   5279 C  CE  . LYS D 1 127 ? 7.332   18.546  37.818  1.00 32.81 ? 115 LYS D CE  1 
ATOM   5280 N  NZ  . LYS D 1 127 ? 6.459   18.121  36.692  1.00 35.43 ? 115 LYS D NZ  1 
ATOM   5281 N  N   . ILE D 1 128 ? 13.121  22.419  38.566  1.00 21.23 ? 116 ILE D N   1 
ATOM   5282 C  CA  . ILE D 1 128 ? 14.310  23.168  38.110  1.00 22.94 ? 116 ILE D CA  1 
ATOM   5283 C  C   . ILE D 1 128 ? 14.614  22.844  36.657  1.00 23.72 ? 116 ILE D C   1 
ATOM   5284 O  O   . ILE D 1 128 ? 14.684  21.643  36.293  1.00 25.02 ? 116 ILE D O   1 
ATOM   5285 C  CB  . ILE D 1 128 ? 15.537  22.873  38.993  1.00 24.77 ? 116 ILE D CB  1 
ATOM   5286 C  CG1 . ILE D 1 128 ? 15.268  23.264  40.451  1.00 26.70 ? 116 ILE D CG1 1 
ATOM   5287 C  CG2 . ILE D 1 128 ? 16.758  23.553  38.395  1.00 24.14 ? 116 ILE D CG2 1 
ATOM   5288 C  CD1 . ILE D 1 128 ? 16.253  22.669  41.439  1.00 27.04 ? 116 ILE D CD1 1 
ATOM   5289 N  N   . TYR D 1 129 ? 14.846  23.880  35.854  1.00 20.95 ? 117 TYR D N   1 
ATOM   5290 C  CA  . TYR D 1 129 ? 15.243  23.710  34.444  1.00 22.30 ? 117 TYR D CA  1 
ATOM   5291 C  C   . TYR D 1 129 ? 16.365  24.665  34.086  1.00 24.06 ? 117 TYR D C   1 
ATOM   5292 O  O   . TYR D 1 129 ? 16.451  25.831  34.599  1.00 23.98 ? 117 TYR D O   1 
ATOM   5293 C  CB  . TYR D 1 129 ? 14.084  23.943  33.472  1.00 22.24 ? 117 TYR D CB  1 
ATOM   5294 C  CG  . TYR D 1 129 ? 12.794  23.227  33.791  1.00 21.45 ? 117 TYR D CG  1 
ATOM   5295 C  CD1 . TYR D 1 129 ? 11.947  23.689  34.780  1.00 22.30 ? 117 TYR D CD1 1 
ATOM   5296 C  CD2 . TYR D 1 129 ? 12.407  22.105  33.065  1.00 25.46 ? 117 TYR D CD2 1 
ATOM   5297 C  CE1 . TYR D 1 129 ? 10.752  23.046  35.072  1.00 23.90 ? 117 TYR D CE1 1 
ATOM   5298 C  CE2 . TYR D 1 129 ? 11.213  21.459  33.331  1.00 23.82 ? 117 TYR D CE2 1 
ATOM   5299 C  CZ  . TYR D 1 129 ? 10.381  21.936  34.330  1.00 26.57 ? 117 TYR D CZ  1 
ATOM   5300 O  OH  . TYR D 1 129 ? 9.179   21.339  34.580  1.00 29.50 ? 117 TYR D OH  1 
ATOM   5301 N  N   . GLN D 1 130 ? 17.187  24.236  33.142  1.00 23.19 ? 118 GLN D N   1 
ATOM   5302 C  CA  . GLN D 1 130 ? 18.096  25.185  32.482  1.00 29.03 ? 118 GLN D CA  1 
ATOM   5303 C  C   . GLN D 1 130 ? 17.826  25.171  30.991  1.00 30.31 ? 118 GLN D C   1 
ATOM   5304 O  O   . GLN D 1 130 ? 17.513  24.069  30.436  1.00 28.50 ? 118 GLN D O   1 
ATOM   5305 C  CB  . GLN D 1 130 ? 19.580  24.890  32.715  1.00 33.05 ? 118 GLN D CB  1 
ATOM   5306 C  CG  . GLN D 1 130 ? 20.436  25.796  31.838  1.00 36.34 ? 118 GLN D CG  1 
ATOM   5307 C  CD  . GLN D 1 130 ? 21.929  25.595  31.910  1.00 42.98 ? 118 GLN D CD  1 
ATOM   5308 O  OE1 . GLN D 1 130 ? 22.426  24.483  32.100  1.00 48.35 ? 118 GLN D OE1 1 
ATOM   5309 N  NE2 . GLN D 1 130 ? 22.653  26.679  31.686  1.00 39.28 ? 118 GLN D NE2 1 
ATOM   5310 N  N   . THR D 1 131 ? 18.030  26.332  30.369  1.00 31.67 ? 119 THR D N   1 
ATOM   5311 C  CA  . THR D 1 131 ? 18.107  26.461  28.900  1.00 37.93 ? 119 THR D CA  1 
ATOM   5312 C  C   . THR D 1 131 ? 19.144  27.518  28.506  1.00 39.23 ? 119 THR D C   1 
ATOM   5313 O  O   . THR D 1 131 ? 19.736  28.166  29.389  1.00 32.65 ? 119 THR D O   1 
ATOM   5314 C  CB  . THR D 1 131 ? 16.730  26.725  28.295  1.00 40.27 ? 119 THR D CB  1 
ATOM   5315 O  OG1 . THR D 1 131 ? 16.952  26.655  26.888  1.00 49.09 ? 119 THR D OG1 1 
ATOM   5316 C  CG2 . THR D 1 131 ? 16.129  28.049  28.702  1.00 44.00 ? 119 THR D CG2 1 
ATOM   5317 N  N   . THR D 1 132 ? 19.411  27.593  27.206  1.00 44.17 ? 120 THR D N   1 
ATOM   5318 C  CA  . THR D 1 132 ? 20.514  28.380  26.612  1.00 42.70 ? 120 THR D CA  1 
ATOM   5319 C  C   . THR D 1 132 ? 19.881  29.227  25.521  1.00 44.49 ? 120 THR D C   1 
ATOM   5320 O  O   . THR D 1 132 ? 19.383  28.624  24.564  1.00 44.22 ? 120 THR D O   1 
ATOM   5321 C  CB  . THR D 1 132 ? 21.650  27.458  26.162  1.00 47.47 ? 120 THR D CB  1 
ATOM   5322 O  OG1 . THR D 1 132 ? 22.204  26.928  27.366  1.00 55.05 ? 120 THR D OG1 1 
ATOM   5323 C  CG2 . THR D 1 132 ? 22.735  28.152  25.368  1.00 54.24 ? 120 THR D CG2 1 
ATOM   5324 N  N   . ARG D 1 133 ? 19.818  30.545  25.755  1.00 41.22 ? 121 ARG D N   1 
ATOM   5325 C  CA  . ARG D 1 133 ? 19.450  31.603  24.779  1.00 44.24 ? 121 ARG D CA  1 
ATOM   5326 C  C   . ARG D 1 133 ? 20.727  31.984  24.016  1.00 43.96 ? 121 ARG D C   1 
ATOM   5327 O  O   . ARG D 1 133 ? 21.754  32.247  24.675  1.00 36.38 ? 121 ARG D O   1 
ATOM   5328 C  CB  . ARG D 1 133 ? 18.831  32.812  25.494  1.00 45.55 ? 121 ARG D CB  1 
ATOM   5329 C  CG  . ARG D 1 133 ? 17.487  32.537  26.160  1.00 50.67 ? 121 ARG D CG  1 
ATOM   5330 C  CD  . ARG D 1 133 ? 16.291  33.185  25.476  1.00 50.82 ? 121 ARG D CD  1 
ATOM   5331 N  NE  . ARG D 1 133 ? 16.256  32.937  24.041  1.00 55.89 ? 121 ARG D NE  1 
ATOM   5332 C  CZ  . ARG D 1 133 ? 15.372  33.459  23.192  1.00 57.54 ? 121 ARG D CZ  1 
ATOM   5333 N  NH1 . ARG D 1 133 ? 14.430  34.286  23.621  1.00 58.97 ? 121 ARG D NH1 1 
ATOM   5334 N  NH2 . ARG D 1 133 ? 15.447  33.160  21.907  1.00 60.04 ? 121 ARG D NH2 1 
ATOM   5335 N  N   . GLU D 1 134 ? 20.670  31.973  22.681  1.00 49.72 ? 122 GLU D N   1 
ATOM   5336 C  CA  . GLU D 1 134 ? 21.820  32.317  21.796  1.00 51.95 ? 122 GLU D CA  1 
ATOM   5337 C  C   . GLU D 1 134 ? 21.399  33.475  20.882  1.00 52.17 ? 122 GLU D C   1 
ATOM   5338 O  O   . GLU D 1 134 ? 20.239  33.442  20.404  1.00 47.92 ? 122 GLU D O   1 
ATOM   5339 C  CB  . GLU D 1 134 ? 22.335  31.078  21.051  1.00 59.43 ? 122 GLU D CB  1 
ATOM   5340 C  CG  . GLU D 1 134 ? 21.273  30.053  20.659  1.00 62.43 ? 122 GLU D CG  1 
ATOM   5341 C  CD  . GLU D 1 134 ? 21.547  28.636  21.148  1.00 63.75 ? 122 GLU D CD  1 
ATOM   5342 O  OE1 . GLU D 1 134 ? 20.602  27.993  21.653  1.00 62.57 ? 122 GLU D OE1 1 
ATOM   5343 O  OE2 . GLU D 1 134 ? 22.710  28.183  21.038  1.00 61.02 ? 122 GLU D OE2 1 
ATOM   5344 N  N   . ASN D 1 135 ? 22.288  34.475  20.715  1.00 54.17 ? 123 ASN D N   1 
ATOM   5345 C  CA  . ASN D 1 135 ? 22.095  35.713  19.901  1.00 52.60 ? 123 ASN D CA  1 
ATOM   5346 C  C   . ASN D 1 135 ? 20.721  36.299  20.251  1.00 50.22 ? 123 ASN D C   1 
ATOM   5347 O  O   . ASN D 1 135 ? 19.930  36.578  19.324  1.00 46.84 ? 123 ASN D O   1 
ATOM   5348 C  CB  . ASN D 1 135 ? 22.293  35.426  18.401  1.00 56.05 ? 123 ASN D CB  1 
ATOM   5349 C  CG  . ASN D 1 135 ? 22.291  36.651  17.503  1.00 55.46 ? 123 ASN D CG  1 
ATOM   5350 O  OD1 . ASN D 1 135 ? 23.030  36.715  16.518  1.00 51.07 ? 123 ASN D OD1 1 
ATOM   5351 N  ND2 . ASN D 1 135 ? 21.441  37.618  17.803  1.00 53.55 ? 123 ASN D ND2 1 
ATOM   5352 N  N   . ALA D 1 136 ? 20.426  36.436  21.549  1.00 46.63 ? 124 ALA D N   1 
ATOM   5353 C  CA  . ALA D 1 136 ? 19.090  36.839  22.051  1.00 46.47 ? 124 ALA D CA  1 
ATOM   5354 C  C   . ALA D 1 136 ? 19.204  38.129  22.855  1.00 44.91 ? 124 ALA D C   1 
ATOM   5355 O  O   . ALA D 1 136 ? 20.261  38.424  23.410  1.00 43.42 ? 124 ALA D O   1 
ATOM   5356 C  CB  . ALA D 1 136 ? 18.477  35.736  22.875  1.00 45.75 ? 124 ALA D CB  1 
ATOM   5357 N  N   . PRO D 1 137 ? 18.115  38.930  22.927  1.00 43.83 ? 125 PRO D N   1 
ATOM   5358 C  CA  . PRO D 1 137 ? 18.111  40.164  23.709  1.00 43.29 ? 125 PRO D CA  1 
ATOM   5359 C  C   . PRO D 1 137 ? 18.480  39.862  25.170  1.00 42.99 ? 125 PRO D C   1 
ATOM   5360 O  O   . PRO D 1 137 ? 18.106  38.816  25.688  1.00 48.24 ? 125 PRO D O   1 
ATOM   5361 C  CB  . PRO D 1 137 ? 16.675  40.691  23.562  1.00 44.44 ? 125 PRO D CB  1 
ATOM   5362 C  CG  . PRO D 1 137 ? 16.185  40.069  22.268  1.00 42.99 ? 125 PRO D CG  1 
ATOM   5363 C  CD  . PRO D 1 137 ? 16.836  38.704  22.228  1.00 44.82 ? 125 PRO D CD  1 
ATOM   5364 N  N   . SER D 1 138 ? 19.292  40.728  25.771  1.00 40.86 ? 126 SER D N   1 
ATOM   5365 C  CA  . SER D 1 138 ? 19.753  40.585  27.175  1.00 38.21 ? 126 SER D CA  1 
ATOM   5366 C  C   . SER D 1 138 ? 20.024  41.979  27.731  1.00 38.21 ? 126 SER D C   1 
ATOM   5367 O  O   . SER D 1 138 ? 19.831  42.958  26.982  1.00 41.95 ? 126 SER D O   1 
ATOM   5368 C  CB  . SER D 1 138 ? 20.966  39.684  27.250  1.00 37.31 ? 126 SER D CB  1 
ATOM   5369 O  OG  . SER D 1 138 ? 22.169  40.430  27.215  1.00 35.58 ? 126 SER D OG  1 
ATOM   5370 N  N   . ILE D 1 139 ? 20.459  42.057  28.987  1.00 33.74 ? 127 ILE D N   1 
ATOM   5371 C  CA  . ILE D 1 139 ? 20.813  43.329  29.677  1.00 30.39 ? 127 ILE D CA  1 
ATOM   5372 C  C   . ILE D 1 139 ? 22.193  43.789  29.173  1.00 33.93 ? 127 ILE D C   1 
ATOM   5373 O  O   . ILE D 1 139 ? 22.570  44.972  29.445  1.00 37.31 ? 127 ILE D O   1 
ATOM   5374 C  CB  . ILE D 1 139 ? 20.732  43.167  31.209  1.00 27.32 ? 127 ILE D CB  1 
ATOM   5375 C  CG1 . ILE D 1 139 ? 21.722  42.143  31.761  1.00 26.60 ? 127 ILE D CG1 1 
ATOM   5376 C  CG2 . ILE D 1 139 ? 19.302  42.831  31.621  1.00 27.78 ? 127 ILE D CG2 1 
ATOM   5377 C  CD1 . ILE D 1 139 ? 22.172  42.440  33.179  1.00 27.96 ? 127 ILE D CD1 1 
ATOM   5378 N  N   . GLU D 1 140 ? 22.901  42.915  28.455  1.00 34.33 ? 128 GLU D N   1 
ATOM   5379 C  CA  . GLU D 1 140 ? 24.209  43.226  27.806  1.00 37.64 ? 128 GLU D CA  1 
ATOM   5380 C  C   . GLU D 1 140 ? 24.032  43.321  26.280  1.00 41.94 ? 128 GLU D C   1 
ATOM   5381 O  O   . GLU D 1 140 ? 25.038  43.219  25.569  1.00 44.16 ? 128 GLU D O   1 
ATOM   5382 C  CB  . GLU D 1 140 ? 25.247  42.166  28.191  1.00 37.51 ? 128 GLU D CB  1 
ATOM   5383 C  CG  . GLU D 1 140 ? 25.841  42.369  29.584  1.00 39.38 ? 128 GLU D CG  1 
ATOM   5384 C  CD  . GLU D 1 140 ? 26.758  41.253  30.071  1.00 42.73 ? 128 GLU D CD  1 
ATOM   5385 O  OE1 . GLU D 1 140 ? 27.189  41.324  31.248  1.00 35.87 ? 128 GLU D OE1 1 
ATOM   5386 O  OE2 . GLU D 1 140 ? 27.051  40.306  29.268  1.00 46.05 ? 128 GLU D OE2 1 
ATOM   5387 N  N   . GLY D 1 141 ? 22.806  43.534  25.795  1.00 43.27 ? 129 GLY D N   1 
ATOM   5388 C  CA  . GLY D 1 141 ? 22.466  43.475  24.360  1.00 46.82 ? 129 GLY D CA  1 
ATOM   5389 C  C   . GLY D 1 141 ? 22.396  42.044  23.848  1.00 49.12 ? 129 GLY D C   1 
ATOM   5390 O  O   . GLY D 1 141 ? 22.254  41.113  24.682  1.00 47.17 ? 129 GLY D O   1 
ATOM   5391 N  N   . THR D 1 142 ? 22.492  41.866  22.525  1.00 45.96 ? 130 THR D N   1 
ATOM   5392 C  CA  . THR D 1 142 ? 22.509  40.545  21.842  1.00 48.77 ? 130 THR D CA  1 
ATOM   5393 C  C   . THR D 1 142 ? 23.600  39.694  22.496  1.00 46.78 ? 130 THR D C   1 
ATOM   5394 O  O   . THR D 1 142 ? 24.763  40.116  22.463  1.00 44.17 ? 130 THR D O   1 
ATOM   5395 C  CB  . THR D 1 142 ? 22.694  40.709  20.325  1.00 51.45 ? 130 THR D CB  1 
ATOM   5396 O  OG1 . THR D 1 142 ? 21.428  41.077  19.775  1.00 52.67 ? 130 THR D OG1 1 
ATOM   5397 C  CG2 . THR D 1 142 ? 23.199  39.457  19.640  1.00 53.52 ? 130 THR D CG2 1 
ATOM   5398 N  N   . ALA D 1 143 ? 23.236  38.568  23.116  1.00 45.25 ? 131 ALA D N   1 
ATOM   5399 C  CA  . ALA D 1 143 ? 24.192  37.723  23.874  1.00 45.55 ? 131 ALA D CA  1 
ATOM   5400 C  C   . ALA D 1 143 ? 23.774  36.254  23.851  1.00 44.09 ? 131 ALA D C   1 
ATOM   5401 O  O   . ALA D 1 143 ? 22.673  35.930  23.372  1.00 44.35 ? 131 ALA D O   1 
ATOM   5402 C  CB  . ALA D 1 143 ? 24.327  38.233  25.292  1.00 45.34 ? 131 ALA D CB  1 
ATOM   5403 N  N   . THR D 1 144 ? 24.685  35.409  24.327  1.00 44.88 ? 132 THR D N   1 
ATOM   5404 C  CA  . THR D 1 144 ? 24.498  33.956  24.520  1.00 44.18 ? 132 THR D CA  1 
ATOM   5405 C  C   . THR D 1 144 ? 24.605  33.693  26.016  1.00 42.24 ? 132 THR D C   1 
ATOM   5406 O  O   . THR D 1 144 ? 25.656  34.020  26.622  1.00 42.92 ? 132 THR D O   1 
ATOM   5407 C  CB  . THR D 1 144 ? 25.506  33.162  23.688  1.00 46.55 ? 132 THR D CB  1 
ATOM   5408 O  OG1 . THR D 1 144 ? 25.127  33.453  22.343  1.00 43.03 ? 132 THR D OG1 1 
ATOM   5409 C  CG2 . THR D 1 144 ? 25.476  31.675  23.974  1.00 50.29 ? 132 THR D CG2 1 
ATOM   5410 N  N   . PHE D 1 145 ? 23.542  33.162  26.601  1.00 33.70 ? 133 PHE D N   1 
ATOM   5411 C  CA  . PHE D 1 145 ? 23.421  33.117  28.073  1.00 31.44 ? 133 PHE D CA  1 
ATOM   5412 C  C   . PHE D 1 145 ? 22.445  32.029  28.502  1.00 30.67 ? 133 PHE D C   1 
ATOM   5413 O  O   . PHE D 1 145 ? 21.502  31.689  27.752  1.00 32.21 ? 133 PHE D O   1 
ATOM   5414 C  CB  . PHE D 1 145 ? 23.031  34.503  28.579  1.00 29.28 ? 133 PHE D CB  1 
ATOM   5415 C  CG  . PHE D 1 145 ? 21.689  34.984  28.120  1.00 27.09 ? 133 PHE D CG  1 
ATOM   5416 C  CD1 . PHE D 1 145 ? 20.527  34.530  28.738  1.00 27.99 ? 133 PHE D CD1 1 
ATOM   5417 C  CD2 . PHE D 1 145 ? 21.580  35.923  27.108  1.00 26.81 ? 133 PHE D CD2 1 
ATOM   5418 C  CE1 . PHE D 1 145 ? 19.290  34.991  28.331  1.00 25.91 ? 133 PHE D CE1 1 
ATOM   5419 C  CE2 . PHE D 1 145 ? 20.342  36.407  26.726  1.00 26.71 ? 133 PHE D CE2 1 
ATOM   5420 C  CZ  . PHE D 1 145 ? 19.196  35.935  27.337  1.00 30.22 ? 133 PHE D CZ  1 
ATOM   5421 N  N   . ASN D 1 146 ? 22.721  31.529  29.702  1.00 31.54 ? 134 ASN D N   1 
ATOM   5422 C  CA  . ASN D 1 146 ? 21.947  30.511  30.442  1.00 29.77 ? 134 ASN D CA  1 
ATOM   5423 C  C   . ASN D 1 146 ? 20.659  31.159  30.968  1.00 27.35 ? 134 ASN D C   1 
ATOM   5424 O  O   . ASN D 1 146 ? 20.718  32.305  31.438  1.00 23.92 ? 134 ASN D O   1 
ATOM   5425 C  CB  . ASN D 1 146 ? 22.787  29.959  31.588  1.00 32.96 ? 134 ASN D CB  1 
ATOM   5426 C  CG  . ASN D 1 146 ? 24.074  29.316  31.106  1.00 39.63 ? 134 ASN D CG  1 
ATOM   5427 O  OD1 . ASN D 1 146 ? 24.098  28.713  30.025  1.00 36.37 ? 134 ASN D OD1 1 
ATOM   5428 N  ND2 . ASN D 1 146 ? 25.117  29.415  31.918  1.00 40.79 ? 134 ASN D ND2 1 
ATOM   5429 N  N   . GLN D 1 147 ? 19.544  30.440  30.884  1.00 25.10 ? 135 GLN D N   1 
ATOM   5430 C  CA  . GLN D 1 147 ? 18.279  30.816  31.572  1.00 24.25 ? 135 GLN D CA  1 
ATOM   5431 C  C   . GLN D 1 147 ? 18.022  29.737  32.604  1.00 22.79 ? 135 GLN D C   1 
ATOM   5432 O  O   . GLN D 1 147 ? 18.100  28.534  32.266  1.00 19.88 ? 135 GLN D O   1 
ATOM   5433 C  CB  . GLN D 1 147 ? 17.053  30.779  30.661  1.00 27.57 ? 135 GLN D CB  1 
ATOM   5434 C  CG  . GLN D 1 147 ? 16.683  32.051  29.931  1.00 30.66 ? 135 GLN D CG  1 
ATOM   5435 C  CD  . GLN D 1 147 ? 15.299  31.882  29.339  1.00 31.48 ? 135 GLN D CD  1 
ATOM   5436 O  OE1 . GLN D 1 147 ? 14.798  30.762  29.194  1.00 31.98 ? 135 GLN D OE1 1 
ATOM   5437 N  NE2 . GLN D 1 147 ? 14.664  32.995  28.996  1.00 29.45 ? 135 GLN D NE2 1 
ATOM   5438 N  N   . TYR D 1 148 ? 17.703  30.115  33.835  1.00 19.72 ? 136 TYR D N   1 
ATOM   5439 C  CA  . TYR D 1 148 ? 17.476  29.121  34.897  1.00 18.80 ? 136 TYR D CA  1 
ATOM   5440 C  C   . TYR D 1 148 ? 16.042  29.327  35.353  1.00 18.94 ? 136 TYR D C   1 
ATOM   5441 O  O   . TYR D 1 148 ? 15.670  30.506  35.458  1.00 16.86 ? 136 TYR D O   1 
ATOM   5442 C  CB  . TYR D 1 148 ? 18.384  29.321  36.104  1.00 20.95 ? 136 TYR D CB  1 
ATOM   5443 C  CG  . TYR D 1 148 ? 19.867  29.267  35.830  1.00 22.72 ? 136 TYR D CG  1 
ATOM   5444 C  CD1 . TYR D 1 148 ? 20.391  28.610  34.721  1.00 24.52 ? 136 TYR D CD1 1 
ATOM   5445 C  CD2 . TYR D 1 148 ? 20.750  29.828  36.724  1.00 24.74 ? 136 TYR D CD2 1 
ATOM   5446 C  CE1 . TYR D 1 148 ? 21.762  28.527  34.520  1.00 26.73 ? 136 TYR D CE1 1 
ATOM   5447 C  CE2 . TYR D 1 148 ? 22.115  29.789  36.516  1.00 25.58 ? 136 TYR D CE2 1 
ATOM   5448 C  CZ  . TYR D 1 148 ? 22.628  29.112  35.422  1.00 27.73 ? 136 TYR D CZ  1 
ATOM   5449 O  OH  . TYR D 1 148 ? 23.982  29.052  35.224  1.00 29.92 ? 136 TYR D OH  1 
ATOM   5450 N  N   . TRP D 1 149 ? 15.341  28.226  35.621  1.00 16.59 ? 137 TRP D N   1 
ATOM   5451 C  CA  . TRP D 1 149 ? 13.921  28.215  36.033  1.00 17.45 ? 137 TRP D CA  1 
ATOM   5452 C  C   . TRP D 1 149 ? 13.741  27.375  37.288  1.00 18.39 ? 137 TRP D C   1 
ATOM   5453 O  O   . TRP D 1 149 ? 14.335  26.268  37.385  1.00 19.10 ? 137 TRP D O   1 
ATOM   5454 C  CB  . TRP D 1 149 ? 13.061  27.643  34.908  1.00 18.20 ? 137 TRP D CB  1 
ATOM   5455 C  CG  . TRP D 1 149 ? 13.188  28.324  33.588  1.00 18.19 ? 137 TRP D CG  1 
ATOM   5456 C  CD1 . TRP D 1 149 ? 14.115  28.083  32.609  1.00 19.06 ? 137 TRP D CD1 1 
ATOM   5457 C  CD2 . TRP D 1 149 ? 12.264  29.270  33.043  1.00 18.00 ? 137 TRP D CD2 1 
ATOM   5458 N  NE1 . TRP D 1 149 ? 13.860  28.872  31.526  1.00 20.15 ? 137 TRP D NE1 1 
ATOM   5459 C  CE2 . TRP D 1 149 ? 12.734  29.616  31.764  1.00 20.72 ? 137 TRP D CE2 1 
ATOM   5460 C  CE3 . TRP D 1 149 ? 11.112  29.897  33.539  1.00 17.58 ? 137 TRP D CE3 1 
ATOM   5461 C  CZ2 . TRP D 1 149 ? 12.110  30.593  30.985  1.00 20.73 ? 137 TRP D CZ2 1 
ATOM   5462 C  CZ3 . TRP D 1 149 ? 10.492  30.837  32.751  1.00 18.47 ? 137 TRP D CZ3 1 
ATOM   5463 C  CH2 . TRP D 1 149 ? 10.964  31.155  31.488  1.00 18.35 ? 137 TRP D CH2 1 
ATOM   5464 N  N   . SER D 1 150 ? 12.940  27.892  38.208  1.00 17.01 ? 138 SER D N   1 
ATOM   5465 C  CA  . SER D 1 150 ? 12.208  27.170  39.260  1.00 18.24 ? 138 SER D CA  1 
ATOM   5466 C  C   . SER D 1 150 ? 10.737  27.398  38.988  1.00 18.52 ? 138 SER D C   1 
ATOM   5467 O  O   . SER D 1 150 ? 10.306  28.557  39.037  1.00 17.61 ? 138 SER D O   1 
ATOM   5468 C  CB  . SER D 1 150 ? 12.510  27.658  40.637  1.00 21.00 ? 138 SER D CB  1 
ATOM   5469 O  OG  . SER D 1 150 ? 13.695  27.097  41.100  1.00 20.47 ? 138 SER D OG  1 
ATOM   5470 N  N   . VAL D 1 151 ? 9.981   26.333  38.765  1.00 16.82 ? 139 VAL D N   1 
ATOM   5471 C  CA  . VAL D 1 151 ? 8.547   26.451  38.395  1.00 16.62 ? 139 VAL D CA  1 
ATOM   5472 C  C   . VAL D 1 151 ? 7.711   25.756  39.469  1.00 16.76 ? 139 VAL D C   1 
ATOM   5473 O  O   . VAL D 1 151 ? 7.856   24.507  39.607  1.00 20.98 ? 139 VAL D O   1 
ATOM   5474 C  CB  . VAL D 1 151 ? 8.315   25.849  36.996  1.00 17.73 ? 139 VAL D CB  1 
ATOM   5475 C  CG1 . VAL D 1 151 ? 6.867   26.009  36.581  1.00 17.89 ? 139 VAL D CG1 1 
ATOM   5476 C  CG2 . VAL D 1 151 ? 9.234   26.477  35.959  1.00 20.04 ? 139 VAL D CG2 1 
ATOM   5477 N  N   . ARG D 1 152 ? 6.879   26.505  40.180  1.00 16.30 ? 140 ARG D N   1 
ATOM   5478 C  CA  . ARG D 1 152 ? 6.061   25.985  41.297  1.00 17.76 ? 140 ARG D CA  1 
ATOM   5479 C  C   . ARG D 1 152 ? 5.053   24.968  40.723  1.00 20.34 ? 140 ARG D C   1 
ATOM   5480 O  O   . ARG D 1 152 ? 4.494   25.212  39.623  1.00 20.45 ? 140 ARG D O   1 
ATOM   5481 C  CB  . ARG D 1 152 ? 5.407   27.130  42.059  1.00 19.29 ? 140 ARG D CB  1 
ATOM   5482 C  CG  . ARG D 1 152 ? 4.896   26.718  43.424  1.00 18.47 ? 140 ARG D CG  1 
ATOM   5483 C  CD  . ARG D 1 152 ? 4.330   27.845  44.217  1.00 20.03 ? 140 ARG D CD  1 
ATOM   5484 N  NE  . ARG D 1 152 ? 3.718   27.398  45.453  1.00 22.21 ? 140 ARG D NE  1 
ATOM   5485 C  CZ  . ARG D 1 152 ? 4.258   27.434  46.677  1.00 22.24 ? 140 ARG D CZ  1 
ATOM   5486 N  NH1 . ARG D 1 152 ? 5.484   27.895  46.907  1.00 21.03 ? 140 ARG D NH1 1 
ATOM   5487 N  NH2 . ARG D 1 152 ? 3.523   27.001  47.686  1.00 24.61 ? 140 ARG D NH2 1 
ATOM   5488 N  N   . THR D 1 153 ? 4.901   23.810  41.378  1.00 21.35 ? 141 THR D N   1 
ATOM   5489 C  CA  . THR D 1 153 ? 3.955   22.731  40.930  1.00 22.19 ? 141 THR D CA  1 
ATOM   5490 C  C   . THR D 1 153 ? 2.499   23.102  41.243  1.00 21.53 ? 141 THR D C   1 
ATOM   5491 O  O   . THR D 1 153 ? 1.610   22.712  40.456  1.00 27.11 ? 141 THR D O   1 
ATOM   5492 C  CB  . THR D 1 153 ? 4.361   21.381  41.540  1.00 22.85 ? 141 THR D CB  1 
ATOM   5493 O  OG1 . THR D 1 153 ? 4.117   21.512  42.938  1.00 25.80 ? 141 THR D OG1 1 
ATOM   5494 C  CG2 . THR D 1 153 ? 5.786   21.006  41.218  1.00 22.78 ? 141 THR D CG2 1 
ATOM   5495 N  N   . ASP D 1 154 ? 2.224   23.762  42.367  1.00 20.95 ? 142 ASP D N   1 
ATOM   5496 C  CA  . ASP D 1 154 ? 0.873   24.232  42.766  1.00 25.94 ? 142 ASP D CA  1 
ATOM   5497 C  C   . ASP D 1 154 ? 0.880   25.752  42.623  1.00 22.28 ? 142 ASP D C   1 
ATOM   5498 O  O   . ASP D 1 154 ? 1.420   26.465  43.516  1.00 19.50 ? 142 ASP D O   1 
ATOM   5499 C  CB  . ASP D 1 154 ? 0.500   23.752  44.167  1.00 26.72 ? 142 ASP D CB  1 
ATOM   5500 C  CG  . ASP D 1 154 ? -0.757  24.408  44.711  1.00 30.44 ? 142 ASP D CG  1 
ATOM   5501 O  OD1 . ASP D 1 154 ? -1.661  24.704  43.890  1.00 30.54 ? 142 ASP D OD1 1 
ATOM   5502 O  OD2 . ASP D 1 154 ? -0.835  24.600  45.948  1.00 34.77 ? 142 ASP D OD2 1 
ATOM   5503 N  N   . HIS D 1 155 ? 0.348   26.236  41.498  1.00 21.84 ? 143 HIS D N   1 
ATOM   5504 C  CA  . HIS D 1 155 ? 0.359   27.683  41.185  1.00 21.15 ? 143 HIS D CA  1 
ATOM   5505 C  C   . HIS D 1 155 ? -0.272  28.450  42.340  1.00 21.80 ? 143 HIS D C   1 
ATOM   5506 O  O   . HIS D 1 155 ? -1.343  28.043  42.881  1.00 20.08 ? 143 HIS D O   1 
ATOM   5507 C  CB  . HIS D 1 155 ? -0.322  27.948  39.837  1.00 22.49 ? 143 HIS D CB  1 
ATOM   5508 C  CG  . HIS D 1 155 ? 0.412   27.309  38.708  1.00 23.06 ? 143 HIS D CG  1 
ATOM   5509 N  ND1 . HIS D 1 155 ? -0.034  27.323  37.393  1.00 20.20 ? 143 HIS D ND1 1 
ATOM   5510 C  CD2 . HIS D 1 155 ? 1.556   26.583  38.709  1.00 23.26 ? 143 HIS D CD2 1 
ATOM   5511 C  CE1 . HIS D 1 155 ? 0.828   26.682  36.635  1.00 21.87 ? 143 HIS D CE1 1 
ATOM   5512 N  NE2 . HIS D 1 155 ? 1.800   26.199  37.424  1.00 24.60 ? 143 HIS D NE2 1 
ATOM   5513 N  N   . ARG D 1 156 ? 0.311   29.585  42.679  1.00 17.31 ? 144 ARG D N   1 
ATOM   5514 C  CA  . ARG D 1 156 ? -0.329  30.503  43.634  1.00 17.23 ? 144 ARG D CA  1 
ATOM   5515 C  C   . ARG D 1 156 ? -0.059  31.949  43.239  1.00 18.22 ? 144 ARG D C   1 
ATOM   5516 O  O   . ARG D 1 156 ? 0.886   32.215  42.443  1.00 18.42 ? 144 ARG D O   1 
ATOM   5517 C  CB  . ARG D 1 156 ? 0.170   30.215  45.048  1.00 18.14 ? 144 ARG D CB  1 
ATOM   5518 C  CG  . ARG D 1 156 ? 1.639   30.568  45.216  1.00 18.36 ? 144 ARG D CG  1 
ATOM   5519 C  CD  . ARG D 1 156 ? 2.174   30.292  46.598  1.00 19.32 ? 144 ARG D CD  1 
ATOM   5520 N  NE  . ARG D 1 156 ? 3.567   30.740  46.620  1.00 20.10 ? 144 ARG D NE  1 
ATOM   5521 C  CZ  . ARG D 1 156 ? 4.304   30.851  47.714  1.00 18.83 ? 144 ARG D CZ  1 
ATOM   5522 N  NH1 . ARG D 1 156 ? 3.827   30.482  48.889  1.00 18.72 ? 144 ARG D NH1 1 
ATOM   5523 N  NH2 . ARG D 1 156 ? 5.561   31.269  47.623  1.00 21.95 ? 144 ARG D NH2 1 
ATOM   5524 N  N   . VAL D 1 157 ? -0.820  32.846  43.844  1.00 18.04 ? 145 VAL D N   1 
ATOM   5525 C  CA  . VAL D 1 157 ? -0.660  34.320  43.769  1.00 17.95 ? 145 VAL D CA  1 
ATOM   5526 C  C   . VAL D 1 157 ? -0.548  34.836  45.197  1.00 20.40 ? 145 VAL D C   1 
ATOM   5527 O  O   . VAL D 1 157 ? -1.607  35.040  45.862  1.00 21.74 ? 145 VAL D O   1 
ATOM   5528 C  CB  . VAL D 1 157 ? -1.817  35.021  43.052  1.00 17.50 ? 145 VAL D CB  1 
ATOM   5529 C  CG1 . VAL D 1 157 ? -1.549  36.500  42.961  1.00 17.99 ? 145 VAL D CG1 1 
ATOM   5530 C  CG2 . VAL D 1 157 ? -2.121  34.429  41.677  1.00 21.58 ? 145 VAL D CG2 1 
ATOM   5531 N  N   . GLY D 1 158 ? 0.691   34.964  45.654  1.00 20.79 ? 146 GLY D N   1 
ATOM   5532 C  CA  . GLY D 1 158 ? 1.011   35.539  46.960  1.00 18.83 ? 146 GLY D CA  1 
ATOM   5533 C  C   . GLY D 1 158 ? 1.858   34.601  47.779  1.00 20.69 ? 146 GLY D C   1 
ATOM   5534 O  O   . GLY D 1 158 ? 1.871   33.394  47.532  1.00 24.03 ? 146 GLY D O   1 
ATOM   5535 N  N   . GLY D 1 159 ? 2.490   35.124  48.800  1.00 19.60 ? 147 GLY D N   1 
ATOM   5536 C  CA  . GLY D 1 159 ? 3.263   34.284  49.709  1.00 19.14 ? 147 GLY D CA  1 
ATOM   5537 C  C   . GLY D 1 159 ? 4.677   34.814  49.806  1.00 19.67 ? 147 GLY D C   1 
ATOM   5538 O  O   . GLY D 1 159 ? 4.887   35.990  49.537  1.00 19.16 ? 147 GLY D O   1 
ATOM   5539 N  N   . THR D 1 160 ? 5.568   33.945  50.242  1.00 17.98 ? 148 THR D N   1 
ATOM   5540 C  CA  . THR D 1 160 ? 6.983   34.237  50.564  1.00 19.25 ? 148 THR D CA  1 
ATOM   5541 C  C   . THR D 1 160 ? 7.789   33.462  49.542  1.00 17.87 ? 148 THR D C   1 
ATOM   5542 O  O   . THR D 1 160 ? 7.443   32.314  49.302  1.00 18.77 ? 148 THR D O   1 
ATOM   5543 C  CB  . THR D 1 160 ? 7.289   33.812  52.001  1.00 20.60 ? 148 THR D CB  1 
ATOM   5544 O  OG1 . THR D 1 160 ? 6.413   34.492  52.904  1.00 23.74 ? 148 THR D OG1 1 
ATOM   5545 C  CG2 . THR D 1 160 ? 8.724   34.078  52.397  1.00 23.68 ? 148 THR D CG2 1 
ATOM   5546 N  N   . VAL D 1 161 ? 8.810   34.084  48.963  1.00 17.19 ? 149 VAL D N   1 
ATOM   5547 C  CA  . VAL D 1 161 ? 9.838   33.449  48.100  1.00 16.47 ? 149 VAL D CA  1 
ATOM   5548 C  C   . VAL D 1 161 ? 11.196  33.688  48.775  1.00 16.66 ? 149 VAL D C   1 
ATOM   5549 O  O   . VAL D 1 161 ? 11.645  34.896  48.861  1.00 17.08 ? 149 VAL D O   1 
ATOM   5550 C  CB  . VAL D 1 161 ? 9.836   34.032  46.684  1.00 16.86 ? 149 VAL D CB  1 
ATOM   5551 C  CG1 . VAL D 1 161 ? 10.947  33.462  45.820  1.00 18.23 ? 149 VAL D CG1 1 
ATOM   5552 C  CG2 . VAL D 1 161 ? 8.480   33.832  46.019  1.00 17.85 ? 149 VAL D CG2 1 
ATOM   5553 N  N   . THR D 1 162 ? 11.752  32.599  49.292  1.00 15.69 ? 150 THR D N   1 
ATOM   5554 C  CA  . THR D 1 162 ? 13.081  32.555  49.931  1.00 18.97 ? 150 THR D CA  1 
ATOM   5555 C  C   . THR D 1 162 ? 14.062  32.357  48.779  1.00 16.84 ? 150 THR D C   1 
ATOM   5556 O  O   . THR D 1 162 ? 14.377  31.206  48.469  1.00 19.26 ? 150 THR D O   1 
ATOM   5557 C  CB  . THR D 1 162 ? 13.150  31.492  51.030  1.00 20.98 ? 150 THR D CB  1 
ATOM   5558 O  OG1 . THR D 1 162 ? 12.068  31.701  51.944  1.00 22.13 ? 150 THR D OG1 1 
ATOM   5559 C  CG2 . THR D 1 162 ? 14.480  31.564  51.758  1.00 22.24 ? 150 THR D CG2 1 
ATOM   5560 N  N   . THR D 1 163 ? 14.442  33.438  48.101  1.00 19.01 ? 151 THR D N   1 
ATOM   5561 C  CA  . THR D 1 163 ? 15.251  33.374  46.855  1.00 18.88 ? 151 THR D CA  1 
ATOM   5562 C  C   . THR D 1 163 ? 16.535  32.569  47.105  1.00 20.42 ? 151 THR D C   1 
ATOM   5563 O  O   . THR D 1 163 ? 16.918  31.779  46.253  1.00 18.08 ? 151 THR D O   1 
ATOM   5564 C  CB  . THR D 1 163 ? 15.516  34.767  46.245  1.00 22.24 ? 151 THR D CB  1 
ATOM   5565 O  OG1 . THR D 1 163 ? 16.220  35.590  47.169  1.00 21.67 ? 151 THR D OG1 1 
ATOM   5566 C  CG2 . THR D 1 163 ? 14.260  35.505  45.845  1.00 21.12 ? 151 THR D CG2 1 
ATOM   5567 N  N   . GLN D 1 164 ? 17.194  32.744  48.250  1.00 19.84 ? 152 GLN D N   1 
ATOM   5568 C  CA  . GLN D 1 164 ? 18.428  31.990  48.571  1.00 22.33 ? 152 GLN D CA  1 
ATOM   5569 C  C   . GLN D 1 164 ? 18.195  30.477  48.452  1.00 22.73 ? 152 GLN D C   1 
ATOM   5570 O  O   . GLN D 1 164 ? 19.154  29.767  48.075  1.00 20.96 ? 152 GLN D O   1 
ATOM   5571 C  CB  . GLN D 1 164 ? 18.955  32.377  49.959  1.00 23.30 ? 152 GLN D CB  1 
ATOM   5572 C  CG  . GLN D 1 164 ? 20.344  31.821  50.232  1.00 26.69 ? 152 GLN D CG  1 
ATOM   5573 C  CD  . GLN D 1 164 ? 21.392  32.451  49.351  1.00 29.82 ? 152 GLN D CD  1 
ATOM   5574 O  OE1 . GLN D 1 164 ? 21.676  33.654  49.438  1.00 34.30 ? 152 GLN D OE1 1 
ATOM   5575 N  NE2 . GLN D 1 164 ? 21.977  31.646  48.485  1.00 32.90 ? 152 GLN D NE2 1 
ATOM   5576 N  N   . ASN D 1 165 ? 16.997  29.959  48.747  1.00 20.07 ? 153 ASN D N   1 
ATOM   5577 C  CA  . ASN D 1 165 ? 16.772  28.483  48.667  1.00 19.24 ? 153 ASN D CA  1 
ATOM   5578 C  C   . ASN D 1 165 ? 16.832  28.058  47.195  1.00 21.44 ? 153 ASN D C   1 
ATOM   5579 O  O   . ASN D 1 165 ? 17.357  26.956  46.905  1.00 21.43 ? 153 ASN D O   1 
ATOM   5580 C  CB  . ASN D 1 165 ? 15.461  28.044  49.298  1.00 22.56 ? 153 ASN D CB  1 
ATOM   5581 C  CG  . ASN D 1 165 ? 15.477  28.072  50.811  1.00 24.96 ? 153 ASN D CG  1 
ATOM   5582 O  OD1 . ASN D 1 165 ? 16.518  27.846  51.423  1.00 29.76 ? 153 ASN D OD1 1 
ATOM   5583 N  ND2 . ASN D 1 165 ? 14.315  28.214  51.415  1.00 26.89 ? 153 ASN D ND2 1 
ATOM   5584 N  N   . HIS D 1 166 ? 16.305  28.894  46.278  1.00 20.15 ? 154 HIS D N   1 
ATOM   5585 C  CA  . HIS D 1 166 ? 16.367  28.656  44.819  1.00 19.07 ? 154 HIS D CA  1 
ATOM   5586 C  C   . HIS D 1 166 ? 17.810  28.756  44.312  1.00 20.27 ? 154 HIS D C   1 
ATOM   5587 O  O   . HIS D 1 166 ? 18.274  27.871  43.569  1.00 17.88 ? 154 HIS D O   1 
ATOM   5588 C  CB  . HIS D 1 166 ? 15.424  29.591  44.059  1.00 16.61 ? 154 HIS D CB  1 
ATOM   5589 C  CG  . HIS D 1 166 ? 13.997  29.367  44.394  1.00 15.92 ? 154 HIS D CG  1 
ATOM   5590 N  ND1 . HIS D 1 166 ? 13.212  28.412  43.729  1.00 15.59 ? 154 HIS D ND1 1 
ATOM   5591 C  CD2 . HIS D 1 166 ? 13.232  29.876  45.365  1.00 16.08 ? 154 HIS D CD2 1 
ATOM   5592 C  CE1 . HIS D 1 166 ? 12.020  28.406  44.264  1.00 16.26 ? 154 HIS D CE1 1 
ATOM   5593 N  NE2 . HIS D 1 166 ? 11.978  29.305  45.237  1.00 16.24 ? 154 HIS D NE2 1 
ATOM   5594 N  N   . PHE D 1 167 ? 18.531  29.793  44.697  1.00 20.07 ? 155 PHE D N   1 
ATOM   5595 C  CA  . PHE D 1 167 ? 19.919  29.986  44.219  1.00 22.57 ? 155 PHE D CA  1 
ATOM   5596 C  C   . PHE D 1 167 ? 20.796  28.816  44.716  1.00 21.58 ? 155 PHE D C   1 
ATOM   5597 O  O   . PHE D 1 167 ? 21.619  28.342  43.912  1.00 20.95 ? 155 PHE D O   1 
ATOM   5598 C  CB  . PHE D 1 167 ? 20.448  31.367  44.609  1.00 23.20 ? 155 PHE D CB  1 
ATOM   5599 C  CG  . PHE D 1 167 ? 19.624  32.548  44.160  1.00 21.90 ? 155 PHE D CG  1 
ATOM   5600 C  CD1 . PHE D 1 167 ? 18.797  32.494  43.049  1.00 20.53 ? 155 PHE D CD1 1 
ATOM   5601 C  CD2 . PHE D 1 167 ? 19.686  33.737  44.873  1.00 22.90 ? 155 PHE D CD2 1 
ATOM   5602 C  CE1 . PHE D 1 167 ? 18.030  33.584  42.671  1.00 22.19 ? 155 PHE D CE1 1 
ATOM   5603 C  CE2 . PHE D 1 167 ? 18.905  34.819  44.505  1.00 23.13 ? 155 PHE D CE2 1 
ATOM   5604 C  CZ  . PHE D 1 167 ? 18.121  34.767  43.381  1.00 21.95 ? 155 PHE D CZ  1 
ATOM   5605 N  N   . ASP D 1 168 ? 20.591  28.346  45.952  1.00 23.67 ? 156 ASP D N   1 
ATOM   5606 C  CA  . ASP D 1 168 ? 21.308  27.177  46.556  1.00 25.32 ? 156 ASP D CA  1 
ATOM   5607 C  C   . ASP D 1 168 ? 20.988  25.891  45.772  1.00 27.32 ? 156 ASP D C   1 
ATOM   5608 O  O   . ASP D 1 168 ? 21.924  25.134  45.468  1.00 24.29 ? 156 ASP D O   1 
ATOM   5609 C  CB  . ASP D 1 168 ? 20.920  26.942  48.019  1.00 29.40 ? 156 ASP D CB  1 
ATOM   5610 C  CG  . ASP D 1 168 ? 21.482  27.930  49.040  1.00 34.15 ? 156 ASP D CG  1 
ATOM   5611 O  OD1 . ASP D 1 168 ? 22.205  28.848  48.645  1.00 35.89 ? 156 ASP D OD1 1 
ATOM   5612 O  OD2 . ASP D 1 168 ? 21.167  27.777  50.240  1.00 44.21 ? 156 ASP D OD2 1 
ATOM   5613 N  N   . ALA D 1 169 ? 19.701  25.653  45.475  1.00 25.29 ? 157 ALA D N   1 
ATOM   5614 C  CA  . ALA D 1 169 ? 19.203  24.505  44.684  1.00 23.31 ? 157 ALA D CA  1 
ATOM   5615 C  C   . ALA D 1 169 ? 19.800  24.532  43.272  1.00 23.15 ? 157 ALA D C   1 
ATOM   5616 O  O   . ALA D 1 169 ? 20.251  23.470  42.827  1.00 24.57 ? 157 ALA D O   1 
ATOM   5617 C  CB  . ALA D 1 169 ? 17.700  24.497  44.656  1.00 23.73 ? 157 ALA D CB  1 
ATOM   5618 N  N   . TRP D 1 170 ? 19.855  25.690  42.592  1.00 23.87 ? 158 TRP D N   1 
ATOM   5619 C  CA  . TRP D 1 170 ? 20.472  25.816  41.250  1.00 23.57 ? 158 TRP D CA  1 
ATOM   5620 C  C   . TRP D 1 170 ? 21.987  25.589  41.350  1.00 26.03 ? 158 TRP D C   1 
ATOM   5621 O  O   . TRP D 1 170 ? 22.526  24.895  40.468  1.00 27.17 ? 158 TRP D O   1 
ATOM   5622 C  CB  . TRP D 1 170 ? 20.172  27.148  40.556  1.00 24.96 ? 158 TRP D CB  1 
ATOM   5623 C  CG  . TRP D 1 170 ? 18.717  27.460  40.404  1.00 22.21 ? 158 TRP D CG  1 
ATOM   5624 C  CD1 . TRP D 1 170 ? 17.674  26.581  40.387  1.00 26.25 ? 158 TRP D CD1 1 
ATOM   5625 C  CD2 . TRP D 1 170 ? 18.145  28.774  40.227  1.00 21.82 ? 158 TRP D CD2 1 
ATOM   5626 N  NE1 . TRP D 1 170 ? 16.491  27.253  40.215  1.00 25.86 ? 158 TRP D NE1 1 
ATOM   5627 C  CE2 . TRP D 1 170 ? 16.753  28.604  40.115  1.00 23.72 ? 158 TRP D CE2 1 
ATOM   5628 C  CE3 . TRP D 1 170 ? 18.675  30.065  40.141  1.00 20.99 ? 158 TRP D CE3 1 
ATOM   5629 C  CZ2 . TRP D 1 170 ? 15.885  29.679  39.886  1.00 22.30 ? 158 TRP D CZ2 1 
ATOM   5630 C  CZ3 . TRP D 1 170 ? 17.816  31.137  39.971  1.00 19.57 ? 158 TRP D CZ3 1 
ATOM   5631 C  CH2 . TRP D 1 170 ? 16.428  30.947  39.865  1.00 21.68 ? 158 TRP D CH2 1 
ATOM   5632 N  N   . LYS D 1 171 ? 22.663  26.155  42.354  1.00 26.37 ? 159 LYS D N   1 
ATOM   5633 C  CA  . LYS D 1 171 ? 24.111  25.852  42.558  1.00 29.23 ? 159 LYS D CA  1 
ATOM   5634 C  C   . LYS D 1 171 ? 24.296  24.333  42.681  1.00 30.75 ? 159 LYS D C   1 
ATOM   5635 O  O   . LYS D 1 171 ? 25.202  23.775  41.999  1.00 31.57 ? 159 LYS D O   1 
ATOM   5636 C  CB  . LYS D 1 171 ? 24.679  26.488  43.822  1.00 31.36 ? 159 LYS D CB  1 
ATOM   5637 C  CG  . LYS D 1 171 ? 26.135  26.117  44.082  1.00 34.90 ? 159 LYS D CG  1 
ATOM   5638 C  CD  . LYS D 1 171 ? 26.646  26.619  45.405  1.00 39.13 ? 159 LYS D CD  1 
ATOM   5639 C  CE  . LYS D 1 171 ? 28.151  26.733  45.436  1.00 43.60 ? 159 LYS D CE  1 
ATOM   5640 N  NZ  . LYS D 1 171 ? 28.619  27.889  44.632  1.00 44.51 ? 159 LYS D NZ  1 
ATOM   5641 N  N   . ASN D 1 172 ? 23.478  23.695  43.522  1.00 33.71 ? 160 ASN D N   1 
ATOM   5642 C  CA  . ASN D 1 172 ? 23.524  22.237  43.800  1.00 35.83 ? 160 ASN D CA  1 
ATOM   5643 C  C   . ASN D 1 172 ? 23.364  21.478  42.470  1.00 37.67 ? 160 ASN D C   1 
ATOM   5644 O  O   . ASN D 1 172 ? 24.092  20.481  42.281  1.00 40.38 ? 160 ASN D O   1 
ATOM   5645 C  CB  . ASN D 1 172 ? 22.512  21.862  44.891  1.00 37.93 ? 160 ASN D CB  1 
ATOM   5646 C  CG  . ASN D 1 172 ? 22.960  22.232  46.292  1.00 42.31 ? 160 ASN D CG  1 
ATOM   5647 O  OD1 . ASN D 1 172 ? 24.128  22.550  46.518  1.00 44.97 ? 160 ASN D OD1 1 
ATOM   5648 N  ND2 . ASN D 1 172 ? 22.047  22.171  47.250  1.00 44.93 ? 160 ASN D ND2 1 
ATOM   5649 N  N   . ALA D 1 173 ? 22.489  21.932  41.564  1.00 29.59 ? 161 ALA D N   1 
ATOM   5650 C  CA  . ALA D 1 173 ? 22.231  21.294  40.248  1.00 31.58 ? 161 ALA D CA  1 
ATOM   5651 C  C   . ALA D 1 173 ? 23.331  21.595  39.211  1.00 31.26 ? 161 ALA D C   1 
ATOM   5652 O  O   . ALA D 1 173 ? 23.168  21.153  38.056  1.00 34.15 ? 161 ALA D O   1 
ATOM   5653 C  CB  . ALA D 1 173 ? 20.869  21.704  39.728  1.00 32.23 ? 161 ALA D CB  1 
ATOM   5654 N  N   . GLY D 1 174 ? 24.381  22.353  39.555  1.00 33.57 ? 162 GLY D N   1 
ATOM   5655 C  CA  . GLY D 1 174 ? 25.486  22.716  38.637  1.00 33.33 ? 162 GLY D CA  1 
ATOM   5656 C  C   . GLY D 1 174 ? 25.294  24.013  37.838  1.00 34.07 ? 162 GLY D C   1 
ATOM   5657 O  O   . GLY D 1 174 ? 26.060  24.208  36.881  1.00 35.34 ? 162 GLY D O   1 
ATOM   5658 N  N   . LEU D 1 175 ? 24.374  24.905  38.231  1.00 32.06 ? 163 LEU D N   1 
ATOM   5659 C  CA  . LEU D 1 175 ? 24.022  26.149  37.479  1.00 34.11 ? 163 LEU D CA  1 
ATOM   5660 C  C   . LEU D 1 175 ? 24.698  27.381  38.109  1.00 33.82 ? 163 LEU D C   1 
ATOM   5661 O  O   . LEU D 1 175 ? 24.174  27.892  39.132  1.00 36.54 ? 163 LEU D O   1 
ATOM   5662 C  CB  . LEU D 1 175 ? 22.498  26.310  37.484  1.00 34.41 ? 163 LEU D CB  1 
ATOM   5663 C  CG  . LEU D 1 175 ? 21.708  25.104  36.986  1.00 34.15 ? 163 LEU D CG  1 
ATOM   5664 C  CD1 . LEU D 1 175 ? 20.222  25.440  36.840  1.00 33.95 ? 163 LEU D CD1 1 
ATOM   5665 C  CD2 . LEU D 1 175 ? 22.288  24.589  35.679  1.00 35.42 ? 163 LEU D CD2 1 
ATOM   5666 N  N   . GLU D 1 176 ? 25.741  27.911  37.461  1.00 28.69 ? 164 GLU D N   1 
ATOM   5667 C  CA  . GLU D 1 176 ? 26.577  29.005  38.027  1.00 34.38 ? 164 GLU D CA  1 
ATOM   5668 C  C   . GLU D 1 176 ? 25.822  30.347  37.951  1.00 28.46 ? 164 GLU D C   1 
ATOM   5669 O  O   . GLU D 1 176 ? 25.312  30.704  36.888  1.00 30.30 ? 164 GLU D O   1 
ATOM   5670 C  CB  . GLU D 1 176 ? 27.923  29.092  37.308  1.00 37.41 ? 164 GLU D CB  1 
ATOM   5671 C  CG  . GLU D 1 176 ? 28.940  29.992  38.004  1.00 41.36 ? 164 GLU D CG  1 
ATOM   5672 C  CD  . GLU D 1 176 ? 30.232  30.186  37.224  1.00 44.14 ? 164 GLU D CD  1 
ATOM   5673 O  OE1 . GLU D 1 176 ? 30.261  29.801  36.038  1.00 44.72 ? 164 GLU D OE1 1 
ATOM   5674 O  OE2 . GLU D 1 176 ? 31.194  30.739  37.791  1.00 45.44 ? 164 GLU D OE2 1 
ATOM   5675 N  N   . MET D 1 177 ? 25.816  31.088  39.051  1.00 29.66 ? 165 MET D N   1 
ATOM   5676 C  CA  . MET D 1 177 ? 25.230  32.457  39.120  1.00 30.14 ? 165 MET D CA  1 
ATOM   5677 C  C   . MET D 1 177 ? 26.359  33.491  39.222  1.00 27.58 ? 165 MET D C   1 
ATOM   5678 O  O   . MET D 1 177 ? 27.310  33.259  39.983  1.00 32.85 ? 165 MET D O   1 
ATOM   5679 C  CB  . MET D 1 177 ? 24.323  32.569  40.350  1.00 33.23 ? 165 MET D CB  1 
ATOM   5680 C  CG  . MET D 1 177 ? 23.093  31.670  40.257  1.00 38.38 ? 165 MET D CG  1 
ATOM   5681 S  SD  . MET D 1 177 ? 21.837  32.397  39.177  1.00 41.33 ? 165 MET D SD  1 
ATOM   5682 C  CE  . MET D 1 177 ? 21.044  33.509  40.338  1.00 36.57 ? 165 MET D CE  1 
ATOM   5683 N  N   . GLY D 1 178 ? 26.202  34.618  38.546  1.00 26.05 ? 166 GLY D N   1 
ATOM   5684 C  CA  . GLY D 1 178 ? 27.158  35.742  38.569  1.00 27.04 ? 166 GLY D CA  1 
ATOM   5685 C  C   . GLY D 1 178 ? 26.817  36.793  39.607  1.00 25.58 ? 166 GLY D C   1 
ATOM   5686 O  O   . GLY D 1 178 ? 26.113  36.502  40.598  1.00 27.93 ? 166 GLY D O   1 
ATOM   5687 N  N   . THR D 1 179 ? 27.314  38.004  39.397  1.00 28.72 ? 167 THR D N   1 
ATOM   5688 C  CA  . THR D 1 179 ? 27.022  39.178  40.263  1.00 27.53 ? 167 THR D CA  1 
ATOM   5689 C  C   . THR D 1 179 ? 25.604  39.654  39.946  1.00 23.71 ? 167 THR D C   1 
ATOM   5690 O  O   . THR D 1 179 ? 25.291  39.820  38.768  1.00 22.31 ? 167 THR D O   1 
ATOM   5691 C  CB  . THR D 1 179 ? 28.080  40.261  40.046  1.00 33.61 ? 167 THR D CB  1 
ATOM   5692 O  OG1 . THR D 1 179 ? 27.970  40.759  38.713  1.00 42.87 ? 167 THR D OG1 1 
ATOM   5693 C  CG2 . THR D 1 179 ? 29.475  39.727  40.236  1.00 30.88 ? 167 THR D CG2 1 
ATOM   5694 N  N   . HIS D 1 180 ? 24.765  39.835  40.960  1.00 23.73 ? 168 HIS D N   1 
ATOM   5695 C  CA  . HIS D 1 180 ? 23.329  40.162  40.744  1.00 22.75 ? 168 HIS D CA  1 
ATOM   5696 C  C   . HIS D 1 180 ? 23.183  41.518  40.052  1.00 21.92 ? 168 HIS D C   1 
ATOM   5697 O  O   . HIS D 1 180 ? 23.892  42.485  40.439  1.00 24.98 ? 168 HIS D O   1 
ATOM   5698 C  CB  . HIS D 1 180 ? 22.562  40.129  42.067  1.00 23.23 ? 168 HIS D CB  1 
ATOM   5699 C  CG  . HIS D 1 180 ? 22.316  38.746  42.550  1.00 29.51 ? 168 HIS D CG  1 
ATOM   5700 N  ND1 . HIS D 1 180 ? 23.258  38.035  43.278  1.00 38.00 ? 168 HIS D ND1 1 
ATOM   5701 C  CD2 . HIS D 1 180 ? 21.288  37.899  42.339  1.00 29.74 ? 168 HIS D CD2 1 
ATOM   5702 C  CE1 . HIS D 1 180 ? 22.786  36.828  43.518  1.00 33.33 ? 168 HIS D CE1 1 
ATOM   5703 N  NE2 . HIS D 1 180 ? 21.597  36.722  42.973  1.00 33.36 ? 168 HIS D NE2 1 
ATOM   5704 N  N   . ASN D 1 181 ? 22.340  41.570  39.021  1.00 18.94 ? 169 ASN D N   1 
ATOM   5705 C  CA  . ASN D 1 181 ? 21.744  42.806  38.485  1.00 17.69 ? 169 ASN D CA  1 
ATOM   5706 C  C   . ASN D 1 181 ? 20.328  42.843  39.092  1.00 15.32 ? 169 ASN D C   1 
ATOM   5707 O  O   . ASN D 1 181 ? 20.159  42.354  40.238  1.00 15.76 ? 169 ASN D O   1 
ATOM   5708 C  CB  . ASN D 1 181 ? 21.877  42.830  36.962  1.00 20.42 ? 169 ASN D CB  1 
ATOM   5709 C  CG  . ASN D 1 181 ? 21.710  44.191  36.312  1.00 21.98 ? 169 ASN D CG  1 
ATOM   5710 O  OD1 . ASN D 1 181 ? 20.633  44.789  36.298  1.00 21.80 ? 169 ASN D OD1 1 
ATOM   5711 N  ND2 . ASN D 1 181 ? 22.775  44.645  35.650  1.00 24.99 ? 169 ASN D ND2 1 
ATOM   5712 N  N   . TYR D 1 182 ? 19.340  43.331  38.370  1.00 14.59 ? 170 TYR D N   1 
ATOM   5713 C  CA  . TYR D 1 182 ? 18.017  43.620  39.004  1.00 15.66 ? 170 TYR D CA  1 
ATOM   5714 C  C   . TYR D 1 182 ? 17.301  42.324  39.390  1.00 16.09 ? 170 TYR D C   1 
ATOM   5715 O  O   . TYR D 1 182 ? 17.544  41.234  38.840  1.00 14.98 ? 170 TYR D O   1 
ATOM   5716 C  CB  . TYR D 1 182 ? 17.155  44.531  38.130  1.00 17.15 ? 170 TYR D CB  1 
ATOM   5717 C  CG  . TYR D 1 182 ? 16.616  43.972  36.832  1.00 19.18 ? 170 TYR D CG  1 
ATOM   5718 C  CD1 . TYR D 1 182 ? 15.487  43.156  36.778  1.00 19.07 ? 170 TYR D CD1 1 
ATOM   5719 C  CD2 . TYR D 1 182 ? 17.175  44.356  35.633  1.00 22.83 ? 170 TYR D CD2 1 
ATOM   5720 C  CE1 . TYR D 1 182 ? 14.954  42.720  35.570  1.00 19.95 ? 170 TYR D CE1 1 
ATOM   5721 C  CE2 . TYR D 1 182 ? 16.682  43.908  34.423  1.00 22.65 ? 170 TYR D CE2 1 
ATOM   5722 C  CZ  . TYR D 1 182 ? 15.563  43.098  34.383  1.00 23.66 ? 170 TYR D CZ  1 
ATOM   5723 O  OH  . TYR D 1 182 ? 15.127  42.716  33.146  1.00 24.50 ? 170 TYR D OH  1 
ATOM   5724 N  N   . MET D 1 183 ? 16.396  42.441  40.353  1.00 15.41 ? 171 MET D N   1 
ATOM   5725 C  CA  . MET D 1 183 ? 15.480  41.344  40.696  1.00 15.68 ? 171 MET D CA  1 
ATOM   5726 C  C   . MET D 1 183 ? 14.148  41.971  41.007  1.00 15.09 ? 171 MET D C   1 
ATOM   5727 O  O   . MET D 1 183 ? 14.114  42.784  41.877  1.00 14.56 ? 171 MET D O   1 
ATOM   5728 C  CB  . MET D 1 183 ? 15.962  40.525  41.895  1.00 16.71 ? 171 MET D CB  1 
ATOM   5729 C  CG  . MET D 1 183 ? 15.064  39.347  42.178  1.00 16.77 ? 171 MET D CG  1 
ATOM   5730 S  SD  . MET D 1 183 ? 15.749  38.357  43.545  1.00 18.84 ? 171 MET D SD  1 
ATOM   5731 C  CE  . MET D 1 183 ? 15.528  39.501  44.897  1.00 19.62 ? 171 MET D CE  1 
ATOM   5732 N  N   . ILE D 1 184 ? 13.098  41.525  40.334  1.00 14.96 ? 172 ILE D N   1 
ATOM   5733 C  CA  . ILE D 1 184 ? 11.744  42.095  40.503  1.00 13.25 ? 172 ILE D CA  1 
ATOM   5734 C  C   . ILE D 1 184 ? 10.728  40.948  40.626  1.00 14.57 ? 172 ILE D C   1 
ATOM   5735 O  O   . ILE D 1 184 ? 10.962  39.856  40.135  1.00 15.54 ? 172 ILE D O   1 
ATOM   5736 C  CB  . ILE D 1 184 ? 11.386  43.047  39.351  1.00 14.36 ? 172 ILE D CB  1 
ATOM   5737 C  CG1 . ILE D 1 184 ? 11.374  42.291  38.015  1.00 14.59 ? 172 ILE D CG1 1 
ATOM   5738 C  CG2 . ILE D 1 184 ? 12.311  44.290  39.333  1.00 15.65 ? 172 ILE D CG2 1 
ATOM   5739 C  CD1 . ILE D 1 184 ? 10.810  43.086  36.850  1.00 15.43 ? 172 ILE D CD1 1 
ATOM   5740 N  N   . VAL D 1 185 ? 9.583   41.287  41.190  1.00 14.43 ? 173 VAL D N   1 
ATOM   5741 C  CA  . VAL D 1 185 ? 8.393   40.417  41.173  1.00 14.19 ? 173 VAL D CA  1 
ATOM   5742 C  C   . VAL D 1 185 ? 7.586   40.815  39.956  1.00 13.08 ? 173 VAL D C   1 
ATOM   5743 O  O   . VAL D 1 185 ? 6.970   41.870  39.957  1.00 14.00 ? 173 VAL D O   1 
ATOM   5744 C  CB  . VAL D 1 185 ? 7.592   40.526  42.472  1.00 15.85 ? 173 VAL D CB  1 
ATOM   5745 C  CG1 . VAL D 1 185 ? 6.389   39.622  42.440  1.00 18.10 ? 173 VAL D CG1 1 
ATOM   5746 C  CG2 . VAL D 1 185 ? 8.500   40.216  43.633  1.00 16.27 ? 173 VAL D CG2 1 
ATOM   5747 N  N   . ALA D 1 186 ? 7.629   39.976  38.934  1.00 13.87 ? 174 ALA D N   1 
ATOM   5748 C  CA  . ALA D 1 186 ? 7.270   40.398  37.582  1.00 14.05 ? 174 ALA D CA  1 
ATOM   5749 C  C   . ALA D 1 186 ? 5.966   39.728  37.173  1.00 14.40 ? 174 ALA D C   1 
ATOM   5750 O  O   . ALA D 1 186 ? 5.817   38.508  37.406  1.00 16.30 ? 174 ALA D O   1 
ATOM   5751 C  CB  . ALA D 1 186 ? 8.371   40.047  36.619  1.00 16.43 ? 174 ALA D CB  1 
ATOM   5752 N  N   . THR D 1 187 ? 5.148   40.523  36.496  1.00 13.77 ? 175 THR D N   1 
ATOM   5753 C  CA  . THR D 1 187 ? 4.032   40.069  35.657  1.00 12.96 ? 175 THR D CA  1 
ATOM   5754 C  C   . THR D 1 187 ? 4.520   40.118  34.214  1.00 12.33 ? 175 THR D C   1 
ATOM   5755 O  O   . THR D 1 187 ? 4.938   41.208  33.765  1.00 12.88 ? 175 THR D O   1 
ATOM   5756 C  CB  . THR D 1 187 ? 2.783   40.913  35.873  1.00 13.77 ? 175 THR D CB  1 
ATOM   5757 O  OG1 . THR D 1 187 ? 2.463   40.803  37.258  1.00 16.98 ? 175 THR D OG1 1 
ATOM   5758 C  CG2 . THR D 1 187 ? 1.630   40.462  35.004  1.00 14.60 ? 175 THR D CG2 1 
ATOM   5759 N  N   . ALA D 1 188 ? 4.469   38.985  33.522  1.00 13.54 ? 176 ALA D N   1 
ATOM   5760 C  CA  . ALA D 1 188 ? 4.849   38.898  32.086  1.00 13.98 ? 176 ALA D CA  1 
ATOM   5761 C  C   . ALA D 1 188 ? 3.667   38.383  31.274  1.00 17.16 ? 176 ALA D C   1 
ATOM   5762 O  O   . ALA D 1 188 ? 2.858   37.598  31.798  1.00 16.12 ? 176 ALA D O   1 
ATOM   5763 C  CB  . ALA D 1 188 ? 6.059   38.059  31.875  1.00 13.98 ? 176 ALA D CB  1 
ATOM   5764 N  N   . GLY D 1 189 ? 3.581   38.820  30.026  1.00 16.51 ? 177 GLY D N   1 
ATOM   5765 C  CA  . GLY D 1 189 ? 2.489   38.402  29.135  1.00 18.61 ? 177 GLY D CA  1 
ATOM   5766 C  C   . GLY D 1 189 ? 2.993   38.312  27.719  1.00 19.20 ? 177 GLY D C   1 
ATOM   5767 O  O   . GLY D 1 189 ? 4.043   38.947  27.380  1.00 16.73 ? 177 GLY D O   1 
ATOM   5768 N  N   . TYR D 1 190 ? 2.282   37.544  26.912  1.00 18.49 ? 178 TYR D N   1 
ATOM   5769 C  CA  . TYR D 1 190 ? 2.513   37.504  25.443  1.00 19.46 ? 178 TYR D CA  1 
ATOM   5770 C  C   . TYR D 1 190 ? 1.221   37.090  24.756  1.00 17.18 ? 178 TYR D C   1 
ATOM   5771 O  O   . TYR D 1 190 ? 0.723   35.950  25.056  1.00 17.45 ? 178 TYR D O   1 
ATOM   5772 C  CB  . TYR D 1 190 ? 3.615   36.521  25.060  1.00 23.27 ? 178 TYR D CB  1 
ATOM   5773 C  CG  . TYR D 1 190 ? 3.924   36.472  23.574  1.00 27.25 ? 178 TYR D CG  1 
ATOM   5774 C  CD1 . TYR D 1 190 ? 4.521   37.542  22.926  1.00 33.82 ? 178 TYR D CD1 1 
ATOM   5775 C  CD2 . TYR D 1 190 ? 3.543   35.389  22.789  1.00 29.51 ? 178 TYR D CD2 1 
ATOM   5776 C  CE1 . TYR D 1 190 ? 4.789   37.516  21.564  1.00 32.96 ? 178 TYR D CE1 1 
ATOM   5777 C  CE2 . TYR D 1 190 ? 3.815   35.343  21.431  1.00 34.81 ? 178 TYR D CE2 1 
ATOM   5778 C  CZ  . TYR D 1 190 ? 4.456   36.401  20.815  1.00 37.35 ? 178 TYR D CZ  1 
ATOM   5779 O  OH  . TYR D 1 190 ? 4.709   36.365  19.472  1.00 40.71 ? 178 TYR D OH  1 
ATOM   5780 N  N   . GLN D 1 191 ? 0.793   37.896  23.784  1.00 17.31 ? 179 GLN D N   1 
ATOM   5781 C  CA  . GLN D 1 191 ? -0.364  37.613  22.894  1.00 17.21 ? 179 GLN D CA  1 
ATOM   5782 C  C   . GLN D 1 191 ? -1.560  37.227  23.758  1.00 15.22 ? 179 GLN D C   1 
ATOM   5783 O  O   . GLN D 1 191 ? -2.168  36.175  23.541  1.00 15.67 ? 179 GLN D O   1 
ATOM   5784 C  CB  . GLN D 1 191 ? -0.007  36.578  21.838  1.00 19.06 ? 179 GLN D CB  1 
ATOM   5785 C  CG  . GLN D 1 191 ? 0.948   37.142  20.793  1.00 23.38 ? 179 GLN D CG  1 
ATOM   5786 C  CD  . GLN D 1 191 ? 0.965   36.422  19.462  1.00 26.01 ? 179 GLN D CD  1 
ATOM   5787 O  OE1 . GLN D 1 191 ? 0.796   35.216  19.372  1.00 30.44 ? 179 GLN D OE1 1 
ATOM   5788 N  NE2 . GLN D 1 191 ? 1.187   37.176  18.393  1.00 31.33 ? 179 GLN D NE2 1 
ATOM   5789 N  N   . SER D 1 192 ? -1.812  38.021  24.782  1.00 15.90 ? 180 SER D N   1 
ATOM   5790 C  CA  . SER D 1 192 ? -2.922  37.796  25.737  1.00 15.97 ? 180 SER D CA  1 
ATOM   5791 C  C   . SER D 1 192 ? -3.530  39.121  26.173  1.00 16.70 ? 180 SER D C   1 
ATOM   5792 O  O   . SER D 1 192 ? -3.091  40.181  25.732  1.00 16.64 ? 180 SER D O   1 
ATOM   5793 C  CB  . SER D 1 192 ? -2.456  37.003  26.916  1.00 16.89 ? 180 SER D CB  1 
ATOM   5794 O  OG  . SER D 1 192 ? -1.404  37.638  27.613  1.00 15.38 ? 180 SER D OG  1 
ATOM   5795 N  N   . SER D 1 193 ? -4.462  39.062  27.121  1.00 16.80 ? 181 SER D N   1 
ATOM   5796 C  CA  . SER D 1 193 ? -5.073  40.244  27.751  1.00 16.06 ? 181 SER D CA  1 
ATOM   5797 C  C   . SER D 1 193 ? -5.117  39.954  29.241  1.00 16.20 ? 181 SER D C   1 
ATOM   5798 O  O   . SER D 1 193 ? -5.006  38.780  29.604  1.00 18.17 ? 181 SER D O   1 
ATOM   5799 C  CB  . SER D 1 193 ? -6.441  40.552  27.232  1.00 17.70 ? 181 SER D CB  1 
ATOM   5800 O  OG  . SER D 1 193 ? -6.421  40.809  25.845  1.00 18.97 ? 181 SER D OG  1 
ATOM   5801 N  N   . GLY D 1 194 ? -5.277  40.990  30.042  1.00 18.36 ? 182 GLY D N   1 
ATOM   5802 C  CA  . GLY D 1 194 ? -5.402  40.740  31.481  1.00 18.13 ? 182 GLY D CA  1 
ATOM   5803 C  C   . GLY D 1 194 ? -5.155  41.968  32.308  1.00 16.27 ? 182 GLY D C   1 
ATOM   5804 O  O   . GLY D 1 194 ? -5.062  43.116  31.804  1.00 16.02 ? 182 GLY D O   1 
ATOM   5805 N  N   . SER D 1 195 ? -5.159  41.726  33.604  1.00 16.02 ? 183 SER D N   1 
ATOM   5806 C  CA  . SER D 1 195 ? -4.871  42.749  34.621  1.00 18.07 ? 183 SER D CA  1 
ATOM   5807 C  C   . SER D 1 195 ? -4.138  42.055  35.774  1.00 16.47 ? 183 SER D C   1 
ATOM   5808 O  O   . SER D 1 195 ? -4.258  40.856  35.942  1.00 16.87 ? 183 SER D O   1 
ATOM   5809 C  CB  . SER D 1 195 ? -6.153  43.451  35.046  1.00 21.65 ? 183 SER D CB  1 
ATOM   5810 O  OG  . SER D 1 195 ? -6.974  42.581  35.829  1.00 24.30 ? 183 SER D OG  1 
ATOM   5811 N  N   . ALA D 1 196 ? -3.322  42.804  36.484  1.00 15.22 ? 184 ALA D N   1 
ATOM   5812 C  CA  . ALA D 1 196 ? -2.632  42.343  37.697  1.00 14.78 ? 184 ALA D CA  1 
ATOM   5813 C  C   . ALA D 1 196 ? -2.381  43.558  38.576  1.00 15.09 ? 184 ALA D C   1 
ATOM   5814 O  O   . ALA D 1 196 ? -2.156  44.655  38.077  1.00 13.49 ? 184 ALA D O   1 
ATOM   5815 C  CB  . ALA D 1 196 ? -1.349  41.631  37.395  1.00 14.73 ? 184 ALA D CB  1 
ATOM   5816 N  N   . SER D 1 197 ? -2.429  43.335  39.874  1.00 14.78 ? 185 SER D N   1 
ATOM   5817 C  CA  . SER D 1 197 ? -2.072  44.368  40.863  1.00 16.23 ? 185 SER D CA  1 
ATOM   5818 C  C   . SER D 1 197 ? -1.285  43.666  41.963  1.00 15.85 ? 185 SER D C   1 
ATOM   5819 O  O   . SER D 1 197 ? -1.873  42.889  42.729  1.00 18.68 ? 185 SER D O   1 
ATOM   5820 C  CB  . SER D 1 197 ? -3.300  45.083  41.344  1.00 18.86 ? 185 SER D CB  1 
ATOM   5821 O  OG  . SER D 1 197 ? -2.950  45.986  42.342  1.00 27.47 ? 185 SER D OG  1 
ATOM   5822 N  N   . ILE D 1 198 ? 0.029   43.868  41.982  1.00 15.59 ? 186 ILE D N   1 
ATOM   5823 C  CA  . ILE D 1 198 ? 0.951   43.119  42.864  1.00 16.88 ? 186 ILE D CA  1 
ATOM   5824 C  C   . ILE D 1 198 ? 1.641   44.104  43.813  1.00 17.60 ? 186 ILE D C   1 
ATOM   5825 O  O   . ILE D 1 198 ? 2.027   45.192  43.360  1.00 17.56 ? 186 ILE D O   1 
ATOM   5826 C  CB  . ILE D 1 198 ? 1.963   42.334  42.015  1.00 17.23 ? 186 ILE D CB  1 
ATOM   5827 C  CG1 . ILE D 1 198 ? 1.295   41.276  41.138  1.00 17.12 ? 186 ILE D CG1 1 
ATOM   5828 C  CG2 . ILE D 1 198 ? 3.032   41.765  42.899  1.00 15.46 ? 186 ILE D CG2 1 
ATOM   5829 C  CD1 . ILE D 1 198 ? 0.506   40.266  41.900  1.00 18.08 ? 186 ILE D CD1 1 
ATOM   5830 N  N   . THR D 1 199 ? 1.745   43.729  45.075  1.00 15.05 ? 187 THR D N   1 
ATOM   5831 C  CA  . THR D 1 199 ? 2.504   44.498  46.079  1.00 18.89 ? 187 THR D CA  1 
ATOM   5832 C  C   . THR D 1 199 ? 3.707   43.690  46.538  1.00 17.03 ? 187 THR D C   1 
ATOM   5833 O  O   . THR D 1 199 ? 3.540   42.613  47.124  1.00 15.79 ? 187 THR D O   1 
ATOM   5834 C  CB  . THR D 1 199 ? 1.641   44.958  47.257  1.00 21.57 ? 187 THR D CB  1 
ATOM   5835 O  OG1 . THR D 1 199 ? 0.644   45.855  46.768  1.00 22.25 ? 187 THR D OG1 1 
ATOM   5836 C  CG2 . THR D 1 199 ? 2.465   45.665  48.315  1.00 23.87 ? 187 THR D CG2 1 
ATOM   5837 N  N   . VAL D 1 200 ? 4.881   44.305  46.444  1.00 17.24 ? 188 VAL D N   1 
ATOM   5838 C  CA  . VAL D 1 200 ? 6.160   43.692  46.910  1.00 21.11 ? 188 VAL D CA  1 
ATOM   5839 C  C   . VAL D 1 200 ? 6.547   44.253  48.276  1.00 26.05 ? 188 VAL D C   1 
ATOM   5840 O  O   . VAL D 1 200 ? 6.299   45.461  48.480  1.00 25.01 ? 188 VAL D O   1 
ATOM   5841 C  CB  . VAL D 1 200 ? 7.274   44.004  45.899  1.00 21.59 ? 188 VAL D CB  1 
ATOM   5842 C  CG1 . VAL D 1 200 ? 8.621   43.514  46.370  1.00 24.95 ? 188 VAL D CG1 1 
ATOM   5843 C  CG2 . VAL D 1 200 ? 6.920   43.451  44.530  1.00 21.19 ? 188 VAL D CG2 1 
ATOM   5844 N  N   . GLN D 1 201 ? 7.187   43.415  49.107  1.00 33.64 ? 189 GLN D N   1 
ATOM   5845 C  CA  . GLN D 1 201 ? 8.143   43.800  50.197  1.00 36.78 ? 189 GLN D CA  1 
ATOM   5846 C  C   . GLN D 1 201 ? 9.401   42.915  50.146  1.00 39.51 ? 189 GLN D C   1 
ATOM   5847 O  O   . GLN D 1 201 ? 9.519   41.712  49.792  1.00 32.88 ? 189 GLN D O   1 
ATOM   5848 C  CB  . GLN D 1 201 ? 7.502   43.669  51.580  1.00 40.30 ? 189 GLN D CB  1 
ATOM   5849 C  CG  . GLN D 1 201 ? 6.107   44.257  51.663  1.00 46.65 ? 189 GLN D CG  1 
ATOM   5850 C  CD  . GLN D 1 201 ? 5.039   43.235  51.371  1.00 50.48 ? 189 GLN D CD  1 
ATOM   5851 O  OE1 . GLN D 1 201 ? 4.840   42.287  52.127  1.00 50.89 ? 189 GLN D OE1 1 
ATOM   5852 N  NE2 . GLN D 1 201 ? 4.342   43.425  50.262  1.00 55.40 ? 189 GLN D NE2 1 
HETATM 5853 ZN ZN  . ZN  E 2 .   ? 4.928   8.100   5.710   1.00 37.26 ? 200 ZN  A ZN  1 
HETATM 5854 ZN ZN  . ZN  F 2 .   ? 4.630   5.470   14.555  1.00 24.72 ? 201 ZN  A ZN  1 
HETATM 5855 ZN ZN  . ZN  G 2 .   ? -17.710 -7.283  25.614  1.00 40.35 ? 200 ZN  B ZN  1 
HETATM 5856 ZN ZN  . ZN  H 2 .   ? -9.234  -4.696  26.169  1.00 37.55 ? 201 ZN  B ZN  1 
HETATM 5857 ZN ZN  . ZN  I 2 .   ? -14.929 33.732  21.171  1.00 71.97 ? 200 ZN  C ZN  1 
HETATM 5858 ZN ZN  . ZN  J 2 .   ? -3.002  25.319  45.565  1.00 38.83 ? 200 ZN  D ZN  1 
HETATM 5859 ZN ZN  . ZN  K 2 .   ? -1.732  27.857  36.574  1.00 31.44 ? 201 ZN  D ZN  1 
HETATM 5860 O  O   . HOH L 3 .   ? 34.803  -1.372  26.984  1.00 20.76 ? 301 HOH A O   1 
HETATM 5861 O  O   . HOH L 3 .   ? 28.527  0.653   12.802  1.00 19.86 ? 302 HOH A O   1 
HETATM 5862 O  O   . HOH L 3 .   ? 4.065   8.355   6.821   1.00 23.07 ? 303 HOH A O   1 
HETATM 5863 O  O   . HOH L 3 .   ? 34.354  -1.925  20.440  1.00 43.02 ? 304 HOH A O   1 
HETATM 5864 O  O   . HOH L 3 .   ? 13.428  -21.912 14.474  1.00 33.46 ? 305 HOH A O   1 
HETATM 5865 O  O   . HOH L 3 .   ? 2.703   -11.244 7.913   1.00 24.98 ? 306 HOH A O   1 
HETATM 5866 O  O   . HOH L 3 .   ? 19.753  15.656  24.087  1.00 31.41 ? 307 HOH A O   1 
HETATM 5867 O  O   . HOH L 3 .   ? -0.991  -6.211  23.437  1.00 35.45 ? 308 HOH A O   1 
HETATM 5868 O  O   . HOH L 3 .   ? 10.990  13.643  22.472  1.00 32.71 ? 309 HOH A O   1 
HETATM 5869 O  O   . HOH L 3 .   ? 5.852   -12.002 6.626   1.00 41.63 ? 310 HOH A O   1 
HETATM 5870 O  O   . HOH L 3 .   ? 28.686  7.245   27.388  1.00 26.67 ? 311 HOH A O   1 
HETATM 5871 O  O   . HOH L 3 .   ? 13.737  3.929   25.395  1.00 38.02 ? 312 HOH A O   1 
HETATM 5872 O  O   . HOH L 3 .   ? 26.844  4.491   5.795   1.00 17.72 ? 313 HOH A O   1 
HETATM 5873 O  O   . HOH L 3 .   ? 11.919  7.158   28.276  1.00 36.60 ? 314 HOH A O   1 
HETATM 5874 O  O   . HOH L 3 .   ? 16.221  6.839   0.257   1.00 28.56 ? 315 HOH A O   1 
HETATM 5875 O  O   . HOH L 3 .   ? 28.184  -0.001  16.107  1.00 19.59 ? 316 HOH A O   1 
HETATM 5876 O  O   . HOH L 3 .   ? 36.412  12.509  24.312  1.00 30.47 ? 317 HOH A O   1 
HETATM 5877 O  O   . HOH L 3 .   ? 20.031  -16.964 28.052  1.00 35.12 ? 318 HOH A O   1 
HETATM 5878 O  O   . HOH L 3 .   ? 19.473  1.055   27.764  1.00 27.13 ? 319 HOH A O   1 
HETATM 5879 O  O   . HOH L 3 .   ? 26.028  16.197  9.466   1.00 46.45 ? 320 HOH A O   1 
HETATM 5880 O  O   . HOH L 3 .   ? 0.478   -3.558  14.817  1.00 34.16 ? 321 HOH A O   1 
HETATM 5881 O  O   . HOH L 3 .   ? -0.648  -10.665 24.694  1.00 42.81 ? 322 HOH A O   1 
HETATM 5882 O  O   . HOH L 3 .   ? 22.419  -3.745  1.403   1.00 37.90 ? 323 HOH A O   1 
HETATM 5883 O  O   . HOH L 3 .   ? 38.748  2.815   17.887  1.00 42.83 ? 324 HOH A O   1 
HETATM 5884 O  O   . HOH L 3 .   ? 0.952   -7.301  26.099  1.00 30.79 ? 325 HOH A O   1 
HETATM 5885 O  O   . HOH L 3 .   ? 18.221  -1.018  25.275  1.00 36.78 ? 326 HOH A O   1 
HETATM 5886 O  O   . HOH L 3 .   ? 18.420  6.766   7.686   1.00 17.04 ? 327 HOH A O   1 
HETATM 5887 O  O   . HOH L 3 .   ? 32.902  -6.391  18.364  1.00 36.79 ? 328 HOH A O   1 
HETATM 5888 O  O   . HOH L 3 .   ? 34.265  -1.626  12.834  1.00 26.82 ? 329 HOH A O   1 
HETATM 5889 O  O   . HOH L 3 .   ? 10.471  -5.843  32.965  1.00 33.39 ? 330 HOH A O   1 
HETATM 5890 O  O   . HOH L 3 .   ? 23.403  -8.704  23.377  1.00 29.55 ? 331 HOH A O   1 
HETATM 5891 O  O   . HOH L 3 .   ? 12.153  -10.991 34.430  1.00 38.01 ? 332 HOH A O   1 
HETATM 5892 O  O   . HOH L 3 .   ? 10.952  12.038  8.107   1.00 19.42 ? 333 HOH A O   1 
HETATM 5893 O  O   . HOH L 3 .   ? 25.055  13.809  8.254   1.00 23.21 ? 334 HOH A O   1 
HETATM 5894 O  O   . HOH L 3 .   ? 15.644  -10.523 34.790  1.00 43.01 ? 335 HOH A O   1 
HETATM 5895 O  O   . HOH L 3 .   ? 29.380  -12.085 13.784  1.00 28.88 ? 336 HOH A O   1 
HETATM 5896 O  O   . HOH L 3 .   ? 22.952  21.581  18.926  1.00 38.75 ? 337 HOH A O   1 
HETATM 5897 O  O   . HOH L 3 .   ? 8.262   -3.385  4.425   1.00 20.36 ? 338 HOH A O   1 
HETATM 5898 O  O   . HOH L 3 .   ? 5.626   2.811   10.732  1.00 24.71 ? 339 HOH A O   1 
HETATM 5899 O  O   . HOH L 3 .   ? 19.753  -11.561 29.609  1.00 33.55 ? 340 HOH A O   1 
HETATM 5900 O  O   . HOH L 3 .   ? 18.096  -10.754 31.090  1.00 39.87 ? 341 HOH A O   1 
HETATM 5901 O  O   . HOH L 3 .   ? 18.816  5.233   34.044  1.00 32.84 ? 342 HOH A O   1 
HETATM 5902 O  O   . HOH L 3 .   ? 11.081  -12.581 28.184  1.00 26.57 ? 343 HOH A O   1 
HETATM 5903 O  O   . HOH L 3 .   ? 22.717  17.446  11.417  1.00 33.05 ? 344 HOH A O   1 
HETATM 5904 O  O   . HOH L 3 .   ? 23.148  -6.226  24.335  1.00 39.28 ? 345 HOH A O   1 
HETATM 5905 O  O   . HOH L 3 .   ? 17.560  10.980  0.896   1.00 37.63 ? 346 HOH A O   1 
HETATM 5906 O  O   . HOH L 3 .   ? 6.485   -0.210  4.677   1.00 14.03 ? 347 HOH A O   1 
HETATM 5907 O  O   . HOH L 3 .   ? 18.848  6.342   0.783   1.00 27.93 ? 348 HOH A O   1 
HETATM 5908 O  O   . HOH L 3 .   ? 10.926  -9.248  28.185  1.00 21.06 ? 349 HOH A O   1 
HETATM 5909 O  O   . HOH L 3 .   ? 4.671   -9.692  12.085  1.00 32.21 ? 350 HOH A O   1 
HETATM 5910 O  O   . HOH L 3 .   ? 10.843  12.477  18.354  1.00 28.00 ? 351 HOH A O   1 
HETATM 5911 O  O   . HOH L 3 .   ? 12.445  -16.813 11.299  1.00 23.02 ? 352 HOH A O   1 
HETATM 5912 O  O   . HOH L 3 .   ? 37.557  4.095   21.396  1.00 26.75 ? 353 HOH A O   1 
HETATM 5913 O  O   . HOH L 3 .   ? 13.540  -12.965 4.013   1.00 25.19 ? 354 HOH A O   1 
HETATM 5914 O  O   . HOH L 3 .   ? 6.876   3.051   21.126  1.00 20.61 ? 355 HOH A O   1 
HETATM 5915 O  O   . HOH L 3 .   ? 35.171  -1.668  15.586  1.00 27.16 ? 356 HOH A O   1 
HETATM 5916 O  O   . HOH L 3 .   ? 9.594   -16.632 10.508  1.00 28.66 ? 357 HOH A O   1 
HETATM 5917 O  O   . HOH L 3 .   ? 23.268  6.081   0.845   1.00 35.82 ? 358 HOH A O   1 
HETATM 5918 O  O   . HOH L 3 .   ? 21.904  -11.568 2.617   1.00 30.79 ? 359 HOH A O   1 
HETATM 5919 O  O   . HOH L 3 .   ? 25.137  17.342  11.367  1.00 39.70 ? 360 HOH A O   1 
HETATM 5920 O  O   . HOH L 3 .   ? 13.849  -15.352 29.213  1.00 37.72 ? 361 HOH A O   1 
HETATM 5921 O  O   . HOH L 3 .   ? 29.153  9.424   25.477  1.00 27.94 ? 362 HOH A O   1 
HETATM 5922 O  O   . HOH L 3 .   ? 16.599  -19.627 15.503  1.00 25.22 ? 363 HOH A O   1 
HETATM 5923 O  O   . HOH L 3 .   ? 19.980  -7.176  21.541  1.00 19.76 ? 364 HOH A O   1 
HETATM 5924 O  O   . HOH L 3 .   ? 16.190  6.504   27.690  1.00 28.94 ? 365 HOH A O   1 
HETATM 5925 O  O   . HOH L 3 .   ? 27.628  0.055   3.180   1.00 32.45 ? 366 HOH A O   1 
HETATM 5926 O  O   . HOH L 3 .   ? 32.158  11.069  7.478   1.00 39.61 ? 367 HOH A O   1 
HETATM 5927 O  O   . HOH L 3 .   ? 3.633   6.316   16.232  1.00 24.69 ? 368 HOH A O   1 
HETATM 5928 O  O   . HOH L 3 .   ? 23.438  -15.533 4.139   1.00 35.22 ? 369 HOH A O   1 
HETATM 5929 O  O   . HOH L 3 .   ? 10.059  11.003  5.027   1.00 35.53 ? 370 HOH A O   1 
HETATM 5930 O  O   . HOH L 3 .   ? 30.896  20.231  16.095  1.00 39.02 ? 371 HOH A O   1 
HETATM 5931 O  O   . HOH L 3 .   ? 33.372  1.200   27.051  1.00 17.59 ? 372 HOH A O   1 
HETATM 5932 O  O   . HOH L 3 .   ? 16.201  -23.441 21.028  1.00 42.74 ? 373 HOH A O   1 
HETATM 5933 O  O   . HOH L 3 .   ? 22.930  -17.376 25.825  1.00 38.60 ? 374 HOH A O   1 
HETATM 5934 O  O   . HOH L 3 .   ? 19.429  -11.255 3.696   1.00 20.50 ? 375 HOH A O   1 
HETATM 5935 O  O   . HOH L 3 .   ? 9.021   7.853   5.574   1.00 30.67 ? 376 HOH A O   1 
HETATM 5936 O  O   . HOH L 3 .   ? 11.255  -9.287  3.917   1.00 34.42 ? 377 HOH A O   1 
HETATM 5937 O  O   . HOH L 3 .   ? 20.678  -18.450 4.171   1.00 35.53 ? 378 HOH A O   1 
HETATM 5938 O  O   . HOH L 3 .   ? 21.837  -11.254 24.402  1.00 27.96 ? 379 HOH A O   1 
HETATM 5939 O  O   . HOH L 3 .   ? 23.552  20.052  16.078  1.00 40.54 ? 380 HOH A O   1 
HETATM 5940 O  O   . HOH L 3 .   ? 29.626  -9.771  11.962  1.00 22.59 ? 381 HOH A O   1 
HETATM 5941 O  O   . HOH L 3 .   ? 24.340  17.843  13.917  1.00 24.94 ? 382 HOH A O   1 
HETATM 5942 O  O   . HOH L 3 .   ? 8.137   9.386   29.851  1.00 26.54 ? 383 HOH A O   1 
HETATM 5943 O  O   . HOH L 3 .   ? 29.484  -3.982  35.569  1.00 23.92 ? 384 HOH A O   1 
HETATM 5944 O  O   . HOH L 3 .   ? 11.289  -10.256 6.436   1.00 22.21 ? 385 HOH A O   1 
HETATM 5945 O  O   . HOH L 3 .   ? 28.191  -14.189 19.984  1.00 28.46 ? 386 HOH A O   1 
HETATM 5946 O  O   . HOH L 3 .   ? 4.763   12.691  11.778  1.00 34.27 ? 387 HOH A O   1 
HETATM 5947 O  O   . HOH L 3 .   ? 35.178  1.742   15.420  1.00 27.57 ? 388 HOH A O   1 
HETATM 5948 O  O   . HOH L 3 .   ? 32.115  -7.169  11.220  1.00 34.76 ? 389 HOH A O   1 
HETATM 5949 O  O   . HOH L 3 .   ? 27.721  -10.040 9.817   1.00 26.82 ? 390 HOH A O   1 
HETATM 5950 O  O   . HOH L 3 .   ? 28.878  -14.286 17.093  1.00 20.29 ? 391 HOH A O   1 
HETATM 5951 O  O   . HOH L 3 .   ? 7.520   14.129  8.840   1.00 38.08 ? 392 HOH A O   1 
HETATM 5952 O  O   . HOH L 3 .   ? 2.451   -1.063  25.500  1.00 19.68 ? 393 HOH A O   1 
HETATM 5953 O  O   . HOH L 3 .   ? 14.649  -1.111  18.088  1.00 23.10 ? 394 HOH A O   1 
HETATM 5954 O  O   . HOH L 3 .   ? 21.035  17.093  7.466   1.00 29.59 ? 395 HOH A O   1 
HETATM 5955 O  O   . HOH L 3 .   ? 4.860   9.044   11.154  1.00 24.67 ? 396 HOH A O   1 
HETATM 5956 O  O   . HOH L 3 .   ? 18.222  17.470  3.043   1.00 47.88 ? 397 HOH A O   1 
HETATM 5957 O  O   . HOH L 3 .   ? 15.217  -26.339 16.316  1.00 42.20 ? 398 HOH A O   1 
HETATM 5958 O  O   . HOH L 3 .   ? 32.222  17.943  16.033  1.00 32.70 ? 399 HOH A O   1 
HETATM 5959 O  O   . HOH L 3 .   ? 23.847  10.362  1.736   1.00 40.48 ? 400 HOH A O   1 
HETATM 5960 O  O   . HOH L 3 .   ? 10.638  -15.279 27.035  1.00 24.45 ? 401 HOH A O   1 
HETATM 5961 O  O   . HOH L 3 .   ? 8.641   13.113  23.567  1.00 28.90 ? 402 HOH A O   1 
HETATM 5962 O  O   . HOH L 3 .   ? 2.772   7.651   19.630  1.00 29.33 ? 403 HOH A O   1 
HETATM 5963 O  O   . HOH L 3 .   ? 15.621  -14.824 4.111   1.00 32.72 ? 404 HOH A O   1 
HETATM 5964 O  O   . HOH L 3 .   ? 8.467   10.732  15.324  1.00 22.42 ? 405 HOH A O   1 
HETATM 5965 O  O   . HOH L 3 .   ? 33.769  6.395   16.220  1.00 35.35 ? 406 HOH A O   1 
HETATM 5966 O  O   . HOH L 3 .   ? 15.707  13.839  3.337   1.00 26.94 ? 407 HOH A O   1 
HETATM 5967 O  O   . HOH L 3 .   ? 20.461  -5.168  23.772  1.00 28.08 ? 408 HOH A O   1 
HETATM 5968 O  O   . HOH L 3 .   ? 18.791  16.552  27.329  1.00 33.43 ? 409 HOH A O   1 
HETATM 5969 O  O   . HOH L 3 .   ? 28.416  -11.588 21.188  1.00 40.68 ? 410 HOH A O   1 
HETATM 5970 O  O   . HOH L 3 .   ? 20.452  10.199  1.976   1.00 36.42 ? 411 HOH A O   1 
HETATM 5971 O  O   . HOH L 3 .   ? 3.431   6.350   13.188  1.00 24.30 ? 412 HOH A O   1 
HETATM 5972 O  O   . HOH L 3 .   ? 22.929  13.162  5.680   1.00 34.37 ? 413 HOH A O   1 
HETATM 5973 O  O   . HOH L 3 .   ? 11.625  0.642   28.370  1.00 43.34 ? 414 HOH A O   1 
HETATM 5974 O  O   . HOH L 3 .   ? 22.020  -4.300  4.538   1.00 22.65 ? 415 HOH A O   1 
HETATM 5975 O  O   . HOH L 3 .   ? 0.686   -0.616  18.697  1.00 25.10 ? 416 HOH A O   1 
HETATM 5976 O  O   . HOH L 3 .   ? 16.145  -20.208 24.702  1.00 36.38 ? 417 HOH A O   1 
HETATM 5977 O  O   . HOH L 3 .   ? 26.901  -8.584  5.210   1.00 42.84 ? 418 HOH A O   1 
HETATM 5978 O  O   . HOH L 3 .   ? 3.940   10.154  5.087   1.00 33.78 ? 419 HOH A O   1 
HETATM 5979 O  O   . HOH L 3 .   ? 11.321  -16.017 31.046  1.00 37.42 ? 420 HOH A O   1 
HETATM 5980 O  O   . HOH L 3 .   ? 24.478  -6.107  31.580  1.00 32.19 ? 421 HOH A O   1 
HETATM 5981 O  O   . HOH L 3 .   ? 24.835  -16.147 23.979  1.00 29.25 ? 422 HOH A O   1 
HETATM 5982 O  O   . HOH L 3 .   ? 18.830  -21.064 7.881   1.00 32.66 ? 423 HOH A O   1 
HETATM 5983 O  O   . HOH L 3 .   ? 26.680  21.778  16.493  1.00 39.63 ? 424 HOH A O   1 
HETATM 5984 O  O   . HOH L 3 .   ? 6.260   -15.207 22.612  1.00 33.05 ? 425 HOH A O   1 
HETATM 5985 O  O   . HOH L 3 .   ? 19.581  -20.017 15.630  1.00 27.57 ? 426 HOH A O   1 
HETATM 5986 O  O   . HOH L 3 .   ? 16.930  -13.994 29.190  1.00 24.44 ? 427 HOH A O   1 
HETATM 5987 O  O   . HOH L 3 .   ? 18.751  -19.192 24.369  1.00 30.78 ? 428 HOH A O   1 
HETATM 5988 O  O   . HOH L 3 .   ? 16.098  2.609   25.989  1.00 39.39 ? 429 HOH A O   1 
HETATM 5989 O  O   . HOH L 3 .   ? 10.062  -4.334  3.023   1.00 32.26 ? 430 HOH A O   1 
HETATM 5990 O  O   . HOH L 3 .   ? 34.347  -4.063  19.187  1.00 35.37 ? 431 HOH A O   1 
HETATM 5991 O  O   . HOH L 3 .   ? 6.347   -11.726 33.691  1.00 31.71 ? 432 HOH A O   1 
HETATM 5992 O  O   . HOH L 3 .   ? 15.142  19.556  9.239   1.00 40.64 ? 433 HOH A O   1 
HETATM 5993 O  O   . HOH L 3 .   ? 33.722  10.647  18.067  1.00 37.44 ? 434 HOH A O   1 
HETATM 5994 O  O   . HOH L 3 .   ? 4.461   3.478   13.612  1.00 18.68 ? 435 HOH A O   1 
HETATM 5995 O  O   . HOH L 3 .   ? 27.360  13.506  6.599   1.00 40.45 ? 436 HOH A O   1 
HETATM 5996 O  O   . HOH L 3 .   ? 22.150  -19.641 24.777  1.00 41.84 ? 437 HOH A O   1 
HETATM 5997 O  O   . HOH L 3 .   ? 28.828  20.414  13.257  1.00 42.74 ? 438 HOH A O   1 
HETATM 5998 O  O   . HOH L 3 .   ? 10.798  12.532  15.567  1.00 22.20 ? 439 HOH A O   1 
HETATM 5999 O  O   . HOH L 3 .   ? 18.281  13.646  28.564  1.00 48.14 ? 440 HOH A O   1 
HETATM 6000 O  O   . HOH L 3 .   ? 17.152  -0.922  33.528  1.00 45.28 ? 441 HOH A O   1 
HETATM 6001 O  O   . HOH L 3 .   ? 20.550  20.643  12.818  1.00 32.64 ? 442 HOH A O   1 
HETATM 6002 O  O   . HOH L 3 .   ? 24.760  -3.860  4.255   1.00 34.89 ? 443 HOH A O   1 
HETATM 6003 O  O   . HOH L 3 .   ? 18.474  -20.348 10.369  1.00 49.04 ? 444 HOH A O   1 
HETATM 6004 O  O   . HOH L 3 .   ? 8.515   -21.536 19.341  1.00 37.03 ? 445 HOH A O   1 
HETATM 6005 O  O   . HOH L 3 .   ? 15.752  -13.462 33.068  1.00 39.19 ? 446 HOH A O   1 
HETATM 6006 O  O   . HOH L 3 .   ? 15.911  -24.888 12.966  1.00 40.12 ? 447 HOH A O   1 
HETATM 6007 O  O   . HOH L 3 .   ? -2.143  -12.344 26.216  1.00 42.87 ? 448 HOH A O   1 
HETATM 6008 O  O   . HOH L 3 .   ? 9.946   -16.783 29.199  1.00 42.12 ? 449 HOH A O   1 
HETATM 6009 O  O   . HOH L 3 .   ? 16.642  -20.838 8.884   1.00 45.15 ? 450 HOH A O   1 
HETATM 6010 O  O   . HOH L 3 .   ? 23.287  -5.967  26.796  1.00 39.39 ? 451 HOH A O   1 
HETATM 6011 O  O   . HOH L 3 .   ? -5.703  -6.595  21.734  1.00 51.56 ? 452 HOH A O   1 
HETATM 6012 O  O   . HOH L 3 .   ? 6.504   -9.842  33.706  1.00 37.55 ? 453 HOH A O   1 
HETATM 6013 O  O   . HOH L 3 .   ? 9.309   14.999  29.551  1.00 37.96 ? 454 HOH A O   1 
HETATM 6014 O  O   . HOH L 3 .   ? 9.680   -16.544 7.605   1.00 34.09 ? 455 HOH A O   1 
HETATM 6015 O  O   . HOH L 3 .   ? 20.384  -4.124  26.375  1.00 52.30 ? 456 HOH A O   1 
HETATM 6016 O  O   . HOH L 3 .   ? 33.435  -8.190  20.379  1.00 45.43 ? 457 HOH A O   1 
HETATM 6017 O  O   . HOH L 3 .   ? 11.162  -19.980 11.663  1.00 42.55 ? 458 HOH A O   1 
HETATM 6018 O  O   . HOH L 3 .   ? 4.059   -14.928 22.726  1.00 42.87 ? 459 HOH A O   1 
HETATM 6019 O  O   . HOH L 3 .   ? 11.669  -17.847 7.899   1.00 40.46 ? 460 HOH A O   1 
HETATM 6020 O  O   . HOH L 3 .   ? 19.192  -9.896  -0.406  1.00 36.03 ? 461 HOH A O   1 
HETATM 6021 O  O   . HOH L 3 .   ? 28.327  5.889   3.902   1.00 31.19 ? 462 HOH A O   1 
HETATM 6022 O  O   . HOH L 3 .   ? 11.735  18.249  22.365  1.00 43.34 ? 463 HOH A O   1 
HETATM 6023 O  O   . HOH L 3 .   ? 15.455  -14.665 31.034  1.00 34.87 ? 464 HOH A O   1 
HETATM 6024 O  O   . HOH L 3 .   ? 35.114  5.068   14.318  1.00 40.53 ? 465 HOH A O   1 
HETATM 6025 O  O   . HOH L 3 .   ? 14.453  -0.363  24.186  1.00 28.28 ? 466 HOH A O   1 
HETATM 6026 O  O   . HOH L 3 .   ? 26.248  -4.417  40.052  1.00 33.21 ? 467 HOH A O   1 
HETATM 6027 O  O   . HOH L 3 .   ? 4.572   2.271   8.000   1.00 28.51 ? 468 HOH A O   1 
HETATM 6028 O  O   . HOH L 3 .   ? 8.586   -8.705  3.227   1.00 41.05 ? 469 HOH A O   1 
HETATM 6029 O  O   . HOH L 3 .   ? 6.924   -9.226  4.975   1.00 41.14 ? 470 HOH A O   1 
HETATM 6030 O  O   . HOH L 3 .   ? 34.478  1.614   12.472  1.00 49.66 ? 471 HOH A O   1 
HETATM 6031 O  O   . HOH L 3 .   ? 14.323  -21.101 8.708   1.00 32.33 ? 472 HOH A O   1 
HETATM 6032 O  O   . HOH L 3 .   ? 23.589  -12.407 25.794  1.00 38.00 ? 473 HOH A O   1 
HETATM 6033 O  O   . HOH L 3 .   ? 4.003   9.498   16.179  1.00 35.06 ? 474 HOH A O   1 
HETATM 6034 O  O   . HOH L 3 .   ? 17.577  -1.470  35.658  1.00 38.64 ? 475 HOH A O   1 
HETATM 6035 O  O   . HOH L 3 .   ? 30.214  -9.569  8.111   1.00 37.28 ? 476 HOH A O   1 
HETATM 6036 O  O   . HOH L 3 .   ? 13.070  -22.653 11.613  1.00 30.20 ? 477 HOH A O   1 
HETATM 6037 O  O   . HOH L 3 .   ? 22.996  -13.773 2.142   1.00 43.65 ? 478 HOH A O   1 
HETATM 6038 O  O   . HOH L 3 .   ? 35.014  -5.752  10.680  1.00 37.35 ? 479 HOH A O   1 
HETATM 6039 O  O   . HOH L 3 .   ? 17.459  -12.231 1.862   1.00 36.95 ? 480 HOH A O   1 
HETATM 6040 O  O   . HOH L 3 .   ? 12.649  19.592  11.290  1.00 43.64 ? 481 HOH A O   1 
HETATM 6041 O  O   . HOH L 3 .   ? 25.336  18.158  7.063   1.00 47.25 ? 482 HOH A O   1 
HETATM 6042 O  O   . HOH L 3 .   ? 2.334   1.282   15.269  1.00 35.16 ? 483 HOH A O   1 
HETATM 6043 O  O   . HOH L 3 .   ? 32.227  -9.705  22.380  1.00 35.31 ? 484 HOH A O   1 
HETATM 6044 O  O   . HOH L 3 .   ? 6.034   -21.100 19.990  1.00 48.27 ? 485 HOH A O   1 
HETATM 6045 O  O   . HOH L 3 .   ? 16.031  23.277  2.746   1.00 44.17 ? 486 HOH A O   1 
HETATM 6046 O  O   . HOH L 3 .   ? -0.583  -14.905 20.036  1.00 20.23 ? 487 HOH A O   1 
HETATM 6047 O  O   . HOH L 3 .   ? 7.679   13.737  1.639   1.00 46.67 ? 488 HOH A O   1 
HETATM 6048 O  O   . HOH M 3 .   ? -5.795  18.019  24.973  1.00 28.69 ? 301 HOH B O   1 
HETATM 6049 O  O   . HOH M 3 .   ? -16.582 -7.450  24.769  1.00 24.14 ? 302 HOH B O   1 
HETATM 6050 O  O   . HOH M 3 .   ? -2.639  -2.080  29.360  1.00 28.72 ? 303 HOH B O   1 
HETATM 6051 O  O   . HOH M 3 .   ? -19.181 -7.049  26.704  1.00 36.43 ? 304 HOH B O   1 
HETATM 6052 O  O   . HOH M 3 .   ? -14.935 11.397  23.094  1.00 29.05 ? 305 HOH B O   1 
HETATM 6053 O  O   . HOH M 3 .   ? -2.946  2.975   19.886  1.00 43.82 ? 306 HOH B O   1 
HETATM 6054 O  O   . HOH M 3 .   ? -16.413 -15.817 47.607  1.00 46.24 ? 307 HOH B O   1 
HETATM 6055 O  O   . HOH M 3 .   ? -24.547 -6.128  36.057  1.00 29.23 ? 308 HOH B O   1 
HETATM 6056 O  O   . HOH M 3 .   ? -17.277 13.490  31.062  1.00 33.05 ? 309 HOH B O   1 
HETATM 6057 O  O   . HOH M 3 .   ? -2.243  9.379   45.850  1.00 36.08 ? 310 HOH B O   1 
HETATM 6058 O  O   . HOH M 3 .   ? -7.949  -17.793 36.982  1.00 38.48 ? 311 HOH B O   1 
HETATM 6059 O  O   . HOH M 3 .   ? 2.965   8.224   23.935  1.00 32.78 ? 312 HOH B O   1 
HETATM 6060 O  O   . HOH M 3 .   ? -18.881 -14.906 32.680  1.00 46.29 ? 313 HOH B O   1 
HETATM 6061 O  O   . HOH M 3 .   ? -10.554 0.736   49.995  1.00 17.97 ? 314 HOH B O   1 
HETATM 6062 O  O   . HOH M 3 .   ? -25.108 -3.646  45.492  1.00 28.92 ? 315 HOH B O   1 
HETATM 6063 O  O   . HOH M 3 .   ? -15.087 -13.881 52.463  1.00 41.09 ? 316 HOH B O   1 
HETATM 6064 O  O   . HOH M 3 .   ? -17.391 5.217   51.796  1.00 29.77 ? 317 HOH B O   1 
HETATM 6065 O  O   . HOH M 3 .   ? -17.427 -5.282  26.582  1.00 29.16 ? 318 HOH B O   1 
HETATM 6066 O  O   . HOH M 3 .   ? -3.074  -14.303 33.459  1.00 34.93 ? 319 HOH B O   1 
HETATM 6067 O  O   . HOH M 3 .   ? -1.351  6.106   58.622  1.00 25.26 ? 320 HOH B O   1 
HETATM 6068 O  O   . HOH M 3 .   ? -12.814 17.462  33.922  1.00 29.20 ? 321 HOH B O   1 
HETATM 6069 O  O   . HOH M 3 .   ? 7.105   16.050  32.834  1.00 40.70 ? 322 HOH B O   1 
HETATM 6070 O  O   . HOH M 3 .   ? -21.308 4.832   42.564  1.00 30.36 ? 323 HOH B O   1 
HETATM 6071 O  O   . HOH M 3 .   ? -0.024  1.597   41.480  1.00 31.88 ? 324 HOH B O   1 
HETATM 6072 O  O   . HOH M 3 .   ? -7.768  4.686   56.625  1.00 49.06 ? 325 HOH B O   1 
HETATM 6073 O  O   . HOH M 3 .   ? 3.207   16.955  43.981  1.00 30.25 ? 326 HOH B O   1 
HETATM 6074 O  O   . HOH M 3 .   ? 7.626   5.474   38.128  1.00 33.65 ? 327 HOH B O   1 
HETATM 6075 O  O   . HOH M 3 .   ? -21.168 16.041  44.336  1.00 38.98 ? 328 HOH B O   1 
HETATM 6076 O  O   . HOH M 3 .   ? -11.174 11.020  26.343  1.00 31.09 ? 329 HOH B O   1 
HETATM 6077 O  O   . HOH M 3 .   ? -10.979 -5.593  55.449  1.00 32.37 ? 330 HOH B O   1 
HETATM 6078 O  O   . HOH M 3 .   ? -1.105  7.563   56.513  1.00 41.84 ? 331 HOH B O   1 
HETATM 6079 O  O   . HOH M 3 .   ? -1.398  16.662  29.317  1.00 39.96 ? 332 HOH B O   1 
HETATM 6080 O  O   . HOH M 3 .   ? 2.390   -0.305  43.192  1.00 29.39 ? 333 HOH B O   1 
HETATM 6081 O  O   . HOH M 3 .   ? -7.995  4.730   22.070  1.00 33.86 ? 334 HOH B O   1 
HETATM 6082 O  O   . HOH M 3 .   ? -6.783  21.043  42.431  1.00 46.76 ? 335 HOH B O   1 
HETATM 6083 O  O   . HOH M 3 .   ? 1.283   -7.149  38.202  1.00 35.76 ? 336 HOH B O   1 
HETATM 6084 O  O   . HOH M 3 .   ? -14.922 1.709   55.536  1.00 26.55 ? 337 HOH B O   1 
HETATM 6085 O  O   . HOH M 3 .   ? -4.126  1.511   23.025  1.00 24.94 ? 338 HOH B O   1 
HETATM 6086 O  O   . HOH M 3 .   ? -1.869  -8.553  53.055  1.00 33.25 ? 339 HOH B O   1 
HETATM 6087 O  O   . HOH M 3 .   ? 12.562  0.379   45.128  1.00 39.82 ? 340 HOH B O   1 
HETATM 6088 O  O   . HOH M 3 .   ? -4.954  8.189   52.246  1.00 39.23 ? 341 HOH B O   1 
HETATM 6089 O  O   . HOH M 3 .   ? 3.953   13.272  34.509  1.00 22.07 ? 342 HOH B O   1 
HETATM 6090 O  O   . HOH M 3 .   ? -17.258 -6.082  39.078  1.00 17.37 ? 343 HOH B O   1 
HETATM 6091 O  O   . HOH M 3 .   ? -9.846  7.292   55.528  1.00 24.40 ? 344 HOH B O   1 
HETATM 6092 O  O   . HOH M 3 .   ? -5.872  -11.442 33.191  1.00 21.46 ? 345 HOH B O   1 
HETATM 6093 O  O   . HOH M 3 .   ? -4.774  10.407  50.360  1.00 21.22 ? 346 HOH B O   1 
HETATM 6094 O  O   . HOH M 3 .   ? 3.849   -6.528  35.382  1.00 28.21 ? 347 HOH B O   1 
HETATM 6095 O  O   . HOH M 3 .   ? -20.540 15.556  36.776  1.00 30.81 ? 348 HOH B O   1 
HETATM 6096 O  O   . HOH M 3 .   ? -3.963  -17.641 49.133  1.00 29.74 ? 349 HOH B O   1 
HETATM 6097 O  O   . HOH M 3 .   ? 2.658   -5.738  40.091  1.00 25.38 ? 350 HOH B O   1 
HETATM 6098 O  O   . HOH M 3 .   ? -22.049 2.926   32.933  1.00 31.13 ? 351 HOH B O   1 
HETATM 6099 O  O   . HOH M 3 .   ? -3.653  8.028   42.568  1.00 18.54 ? 352 HOH B O   1 
HETATM 6100 O  O   . HOH M 3 .   ? -20.328 14.102  33.974  1.00 26.61 ? 353 HOH B O   1 
HETATM 6101 O  O   . HOH M 3 .   ? -24.202 -5.362  38.477  1.00 31.88 ? 354 HOH B O   1 
HETATM 6102 O  O   . HOH M 3 .   ? -9.702  4.563   56.915  1.00 31.99 ? 355 HOH B O   1 
HETATM 6103 O  O   . HOH M 3 .   ? 8.737   6.509   34.386  1.00 33.21 ? 356 HOH B O   1 
HETATM 6104 O  O   . HOH M 3 .   ? 5.699   -2.254  54.579  1.00 32.14 ? 357 HOH B O   1 
HETATM 6105 O  O   . HOH M 3 .   ? -17.639 -13.217 45.672  1.00 28.20 ? 358 HOH B O   1 
HETATM 6106 O  O   . HOH M 3 .   ? -6.792  -3.305  60.216  1.00 22.17 ? 359 HOH B O   1 
HETATM 6107 O  O   . HOH M 3 .   ? -8.968  20.393  38.403  1.00 29.00 ? 360 HOH B O   1 
HETATM 6108 O  O   . HOH M 3 .   ? -20.274 12.953  48.356  1.00 32.20 ? 361 HOH B O   1 
HETATM 6109 O  O   . HOH M 3 .   ? 7.736   -7.025  42.921  1.00 43.84 ? 362 HOH B O   1 
HETATM 6110 O  O   . HOH M 3 .   ? -16.400 9.563   21.833  1.00 44.24 ? 363 HOH B O   1 
HETATM 6111 O  O   . HOH M 3 .   ? -20.267 10.217  31.559  1.00 37.13 ? 364 HOH B O   1 
HETATM 6112 O  O   . HOH M 3 .   ? 12.363  5.895   49.259  1.00 35.31 ? 365 HOH B O   1 
HETATM 6113 O  O   . HOH M 3 .   ? -2.832  12.861  24.505  1.00 33.28 ? 366 HOH B O   1 
HETATM 6114 O  O   . HOH M 3 .   ? -0.693  19.744  41.895  1.00 29.48 ? 367 HOH B O   1 
HETATM 6115 O  O   . HOH M 3 .   ? 0.292   -13.548 35.776  1.00 35.54 ? 368 HOH B O   1 
HETATM 6116 O  O   . HOH M 3 .   ? 5.977   -8.328  31.798  1.00 22.43 ? 369 HOH B O   1 
HETATM 6117 O  O   . HOH M 3 .   ? 3.970   9.985   34.417  1.00 23.82 ? 370 HOH B O   1 
HETATM 6118 O  O   . HOH M 3 .   ? -0.720  2.256   58.421  1.00 19.28 ? 371 HOH B O   1 
HETATM 6119 O  O   . HOH M 3 .   ? 0.029   -6.855  52.663  1.00 29.14 ? 372 HOH B O   1 
HETATM 6120 O  O   . HOH M 3 .   ? -19.196 4.174   28.800  1.00 24.45 ? 373 HOH B O   1 
HETATM 6121 O  O   . HOH M 3 .   ? -12.484 -17.066 46.136  1.00 28.69 ? 374 HOH B O   1 
HETATM 6122 O  O   . HOH M 3 .   ? 1.704   2.280   44.722  1.00 30.65 ? 375 HOH B O   1 
HETATM 6123 O  O   . HOH M 3 .   ? -5.177  -6.673  60.675  1.00 20.28 ? 376 HOH B O   1 
HETATM 6124 O  O   . HOH M 3 .   ? -6.672  2.069   36.826  1.00 20.65 ? 377 HOH B O   1 
HETATM 6125 O  O   . HOH M 3 .   ? -0.534  9.340   51.700  1.00 46.82 ? 378 HOH B O   1 
HETATM 6126 O  O   . HOH M 3 .   ? -23.878 -10.531 37.435  1.00 33.79 ? 379 HOH B O   1 
HETATM 6127 O  O   . HOH M 3 .   ? -14.291 -16.639 43.994  1.00 30.81 ? 380 HOH B O   1 
HETATM 6128 O  O   . HOH M 3 .   ? -20.396 19.771  41.239  1.00 22.87 ? 381 HOH B O   1 
HETATM 6129 O  O   . HOH M 3 .   ? -0.337  -19.272 40.622  1.00 24.28 ? 382 HOH B O   1 
HETATM 6130 O  O   . HOH M 3 .   ? 2.459   1.904   25.553  1.00 21.27 ? 383 HOH B O   1 
HETATM 6131 O  O   . HOH M 3 .   ? 8.431   4.790   54.429  1.00 20.28 ? 384 HOH B O   1 
HETATM 6132 O  O   . HOH M 3 .   ? 8.467   -4.760  43.505  1.00 32.56 ? 385 HOH B O   1 
HETATM 6133 O  O   . HOH M 3 .   ? -17.622 11.612  31.983  1.00 24.04 ? 386 HOH B O   1 
HETATM 6134 O  O   . HOH M 3 .   ? -12.295 2.053   56.959  1.00 26.22 ? 387 HOH B O   1 
HETATM 6135 O  O   . HOH M 3 .   ? -17.994 -16.329 41.582  1.00 28.06 ? 388 HOH B O   1 
HETATM 6136 O  O   . HOH M 3 .   ? 3.724   1.742   43.983  1.00 41.17 ? 389 HOH B O   1 
HETATM 6137 O  O   . HOH M 3 .   ? -21.411 12.398  39.770  1.00 19.32 ? 390 HOH B O   1 
HETATM 6138 O  O   . HOH M 3 .   ? -6.705  -19.746 47.309  1.00 33.24 ? 391 HOH B O   1 
HETATM 6139 O  O   . HOH M 3 .   ? -21.003 -13.094 36.028  1.00 32.75 ? 392 HOH B O   1 
HETATM 6140 O  O   . HOH M 3 .   ? 1.442   -2.330  39.733  1.00 36.52 ? 393 HOH B O   1 
HETATM 6141 O  O   . HOH M 3 .   ? -12.725 -1.719  26.812  1.00 25.14 ? 394 HOH B O   1 
HETATM 6142 O  O   . HOH M 3 .   ? -1.301  11.412  44.722  1.00 21.10 ? 395 HOH B O   1 
HETATM 6143 O  O   . HOH M 3 .   ? -16.795 10.833  48.406  1.00 16.78 ? 396 HOH B O   1 
HETATM 6144 O  O   . HOH M 3 .   ? -9.488  20.374  42.490  1.00 27.32 ? 397 HOH B O   1 
HETATM 6145 O  O   . HOH M 3 .   ? 2.775   15.929  34.152  1.00 28.53 ? 398 HOH B O   1 
HETATM 6146 O  O   . HOH M 3 .   ? -7.110  17.031  31.829  1.00 26.02 ? 399 HOH B O   1 
HETATM 6147 O  O   . HOH M 3 .   ? -20.572 -3.885  46.973  1.00 16.82 ? 400 HOH B O   1 
HETATM 6148 O  O   . HOH M 3 .   ? -8.488  14.162  50.185  1.00 21.62 ? 401 HOH B O   1 
HETATM 6149 O  O   . HOH M 3 .   ? -18.503 -6.968  29.922  1.00 27.65 ? 402 HOH B O   1 
HETATM 6150 O  O   . HOH M 3 .   ? -19.673 -12.830 43.260  1.00 30.87 ? 403 HOH B O   1 
HETATM 6151 O  O   . HOH M 3 .   ? -11.208 20.775  44.838  1.00 17.02 ? 404 HOH B O   1 
HETATM 6152 O  O   . HOH M 3 .   ? -15.991 -11.093 31.650  1.00 20.25 ? 405 HOH B O   1 
HETATM 6153 O  O   . HOH M 3 .   ? -8.894  19.276  48.933  1.00 18.02 ? 406 HOH B O   1 
HETATM 6154 O  O   . HOH M 3 .   ? -12.159 -8.116  26.241  1.00 32.47 ? 407 HOH B O   1 
HETATM 6155 O  O   . HOH M 3 .   ? 4.379   11.894  43.577  1.00 33.22 ? 408 HOH B O   1 
HETATM 6156 O  O   . HOH M 3 .   ? -24.985 -5.286  42.833  1.00 35.92 ? 409 HOH B O   1 
HETATM 6157 O  O   . HOH M 3 .   ? -7.151  -5.221  25.385  1.00 29.81 ? 410 HOH B O   1 
HETATM 6158 O  O   . HOH M 3 .   ? -14.444 7.526   22.980  1.00 24.10 ? 411 HOH B O   1 
HETATM 6159 O  O   . HOH M 3 .   ? 9.741   13.113  30.692  1.00 34.56 ? 412 HOH B O   1 
HETATM 6160 O  O   . HOH M 3 .   ? -1.679  5.858   43.422  1.00 21.49 ? 413 HOH B O   1 
HETATM 6161 O  O   . HOH M 3 .   ? -9.837  -6.098  32.004  1.00 37.39 ? 414 HOH B O   1 
HETATM 6162 O  O   . HOH M 3 .   ? -8.642  -11.592 32.872  1.00 24.24 ? 415 HOH B O   1 
HETATM 6163 O  O   . HOH M 3 .   ? -24.020 2.600   42.419  1.00 41.12 ? 416 HOH B O   1 
HETATM 6164 O  O   . HOH M 3 .   ? -0.296  -11.877 31.725  1.00 23.99 ? 417 HOH B O   1 
HETATM 6165 O  O   . HOH M 3 .   ? 10.344  3.622   45.849  1.00 44.48 ? 418 HOH B O   1 
HETATM 6166 O  O   . HOH M 3 .   ? -2.201  8.393   52.912  1.00 47.10 ? 419 HOH B O   1 
HETATM 6167 O  O   . HOH M 3 .   ? 0.449   19.186  42.610  1.00 35.23 ? 420 HOH B O   1 
HETATM 6168 O  O   . HOH M 3 .   ? -8.625  -9.798  30.196  1.00 21.99 ? 421 HOH B O   1 
HETATM 6169 O  O   . HOH M 3 .   ? -16.804 19.094  48.647  1.00 13.50 ? 422 HOH B O   1 
HETATM 6170 O  O   . HOH M 3 .   ? -1.476  -12.432 34.105  1.00 26.21 ? 423 HOH B O   1 
HETATM 6171 O  O   . HOH M 3 .   ? -8.901  -10.120 55.873  1.00 25.80 ? 424 HOH B O   1 
HETATM 6172 O  O   . HOH M 3 .   ? 4.219   14.509  40.540  1.00 26.12 ? 425 HOH B O   1 
HETATM 6173 O  O   . HOH M 3 .   ? -12.588 -1.144  56.803  1.00 25.78 ? 426 HOH B O   1 
HETATM 6174 O  O   . HOH M 3 .   ? 5.436   16.356  33.882  1.00 39.50 ? 427 HOH B O   1 
HETATM 6175 O  O   . HOH M 3 .   ? -5.873  -21.797 44.011  1.00 37.11 ? 428 HOH B O   1 
HETATM 6176 O  O   . HOH M 3 .   ? 5.052   7.075   48.709  1.00 29.09 ? 429 HOH B O   1 
HETATM 6177 O  O   . HOH M 3 .   ? 8.412   15.531  31.879  1.00 39.01 ? 430 HOH B O   1 
HETATM 6178 O  O   . HOH M 3 .   ? -23.289 -9.280  40.545  1.00 33.35 ? 431 HOH B O   1 
HETATM 6179 O  O   . HOH M 3 .   ? -1.809  16.835  47.948  1.00 25.36 ? 432 HOH B O   1 
HETATM 6180 O  O   . HOH M 3 .   ? -9.277  26.072  34.350  1.00 43.66 ? 433 HOH B O   1 
HETATM 6181 O  O   . HOH M 3 .   ? -9.826  13.893  28.535  1.00 29.21 ? 434 HOH B O   1 
HETATM 6182 O  O   . HOH M 3 .   ? -7.369  8.737   55.168  1.00 34.78 ? 435 HOH B O   1 
HETATM 6183 O  O   . HOH M 3 .   ? -13.967 -0.036  49.840  1.00 19.10 ? 436 HOH B O   1 
HETATM 6184 O  O   . HOH M 3 .   ? -21.215 -14.872 33.876  1.00 49.55 ? 437 HOH B O   1 
HETATM 6185 O  O   . HOH M 3 .   ? -11.900 -19.714 42.043  1.00 39.64 ? 438 HOH B O   1 
HETATM 6186 O  O   . HOH M 3 .   ? -18.389 -10.599 30.446  1.00 35.87 ? 439 HOH B O   1 
HETATM 6187 O  O   . HOH M 3 .   ? -14.421 21.365  39.898  1.00 35.01 ? 440 HOH B O   1 
HETATM 6188 O  O   . HOH M 3 .   ? 4.016   18.457  33.296  1.00 45.84 ? 441 HOH B O   1 
HETATM 6189 O  O   . HOH M 3 .   ? -9.897  -2.500  26.270  1.00 18.25 ? 442 HOH B O   1 
HETATM 6190 O  O   . HOH M 3 .   ? 12.255  4.559   28.540  1.00 49.07 ? 443 HOH B O   1 
HETATM 6191 O  O   . HOH M 3 .   ? -8.430  17.979  26.748  1.00 17.14 ? 444 HOH B O   1 
HETATM 6192 O  O   . HOH M 3 .   ? -4.754  13.194  24.195  1.00 25.29 ? 445 HOH B O   1 
HETATM 6193 O  O   . HOH M 3 .   ? 6.080   -14.174 37.614  1.00 41.97 ? 446 HOH B O   1 
HETATM 6194 O  O   . HOH M 3 .   ? -21.039 5.198   30.271  1.00 31.05 ? 447 HOH B O   1 
HETATM 6195 O  O   . HOH M 3 .   ? -4.287  7.219   57.849  1.00 38.59 ? 448 HOH B O   1 
HETATM 6196 O  O   . HOH M 3 .   ? -12.624 10.448  21.788  1.00 56.55 ? 449 HOH B O   1 
HETATM 6197 O  O   . HOH M 3 .   ? -19.566 -8.228  24.720  1.00 34.98 ? 450 HOH B O   1 
HETATM 6198 O  O   . HOH M 3 .   ? -4.477  -13.817 60.665  1.00 42.81 ? 451 HOH B O   1 
HETATM 6199 O  O   . HOH M 3 .   ? -3.394  19.006  27.842  1.00 40.02 ? 452 HOH B O   1 
HETATM 6200 O  O   . HOH M 3 .   ? 4.301   0.468   27.808  1.00 28.84 ? 453 HOH B O   1 
HETATM 6201 O  O   . HOH M 3 .   ? -8.388  -13.438 30.909  1.00 43.19 ? 454 HOH B O   1 
HETATM 6202 O  O   . HOH M 3 .   ? 2.744   8.931   54.577  1.00 37.12 ? 455 HOH B O   1 
HETATM 6203 O  O   . HOH M 3 .   ? -10.665 -5.416  24.627  1.00 33.62 ? 456 HOH B O   1 
HETATM 6204 O  O   . HOH M 3 .   ? -14.375 -19.949 41.970  1.00 40.65 ? 457 HOH B O   1 
HETATM 6205 O  O   . HOH M 3 .   ? -21.350 6.348   48.723  1.00 39.01 ? 458 HOH B O   1 
HETATM 6206 O  O   . HOH M 3 .   ? -0.671  15.473  27.316  1.00 36.22 ? 459 HOH B O   1 
HETATM 6207 O  O   . HOH M 3 .   ? -20.785 10.852  26.454  1.00 35.05 ? 460 HOH B O   1 
HETATM 6208 O  O   . HOH M 3 .   ? -6.742  24.106  32.426  1.00 33.09 ? 461 HOH B O   1 
HETATM 6209 O  O   . HOH M 3 .   ? 8.867   7.163   31.663  1.00 33.98 ? 462 HOH B O   1 
HETATM 6210 O  O   . HOH M 3 .   ? 4.703   11.355  19.968  1.00 39.24 ? 463 HOH B O   1 
HETATM 6211 O  O   . HOH M 3 .   ? -27.136 -11.675 35.817  1.00 44.14 ? 464 HOH B O   1 
HETATM 6212 O  O   . HOH M 3 .   ? -1.306  10.270  53.616  1.00 45.13 ? 465 HOH B O   1 
HETATM 6213 O  O   . HOH M 3 .   ? -12.445 -6.343  52.865  1.00 24.22 ? 466 HOH B O   1 
HETATM 6214 O  O   . HOH M 3 .   ? 7.147   1.228   39.392  1.00 39.89 ? 467 HOH B O   1 
HETATM 6215 O  O   . HOH M 3 .   ? -19.289 20.090  47.470  1.00 38.84 ? 468 HOH B O   1 
HETATM 6216 O  O   . HOH M 3 .   ? -0.785  -9.569  55.147  1.00 32.69 ? 469 HOH B O   1 
HETATM 6217 O  O   . HOH M 3 .   ? -14.457 8.846   20.976  1.00 43.79 ? 470 HOH B O   1 
HETATM 6218 O  O   . HOH M 3 .   ? 7.273   -12.622 47.303  1.00 42.06 ? 471 HOH B O   1 
HETATM 6219 O  O   . HOH M 3 .   ? -22.725 -5.189  48.289  1.00 36.18 ? 472 HOH B O   1 
HETATM 6220 O  O   . HOH M 3 .   ? -23.762 -11.099 29.946  1.00 43.10 ? 473 HOH B O   1 
HETATM 6221 O  O   . HOH M 3 .   ? -23.182 -1.914  50.490  1.00 44.27 ? 474 HOH B O   1 
HETATM 6222 O  O   . HOH M 3 .   ? -23.406 -13.459 33.544  1.00 50.87 ? 475 HOH B O   1 
HETATM 6223 O  O   . HOH M 3 .   ? 13.035  3.830   47.040  1.00 45.66 ? 476 HOH B O   1 
HETATM 6224 O  O   . HOH M 3 .   ? -7.290  -7.272  60.394  1.00 22.84 ? 477 HOH B O   1 
HETATM 6225 O  O   . HOH M 3 .   ? -7.588  -8.760  25.914  1.00 53.73 ? 478 HOH B O   1 
HETATM 6226 O  O   . HOH M 3 .   ? 4.820   15.235  44.209  1.00 50.65 ? 479 HOH B O   1 
HETATM 6227 O  O   . HOH M 3 .   ? -6.906  12.633  21.836  1.00 19.53 ? 480 HOH B O   1 
HETATM 6228 O  O   . HOH M 3 .   ? 13.589  5.011   51.638  1.00 36.48 ? 481 HOH B O   1 
HETATM 6229 O  O   . HOH M 3 .   ? 2.959   12.070  46.156  1.00 43.79 ? 482 HOH B O   1 
HETATM 6230 O  O   . HOH M 3 .   ? -0.405  23.628  34.317  1.00 41.73 ? 483 HOH B O   1 
HETATM 6231 O  O   . HOH M 3 .   ? -5.238  1.347   60.401  1.00 32.39 ? 484 HOH B O   1 
HETATM 6232 O  O   . HOH M 3 .   ? 12.266  3.560   35.234  1.00 36.37 ? 485 HOH B O   1 
HETATM 6233 O  O   . HOH M 3 .   ? -21.276 -15.424 31.902  1.00 42.94 ? 486 HOH B O   1 
HETATM 6234 O  O   . HOH M 3 .   ? -9.927  19.997  28.905  1.00 47.41 ? 487 HOH B O   1 
HETATM 6235 O  O   . HOH N 3 .   ? -3.422  41.296  -9.080  1.00 43.36 ? 301 HOH C O   1 
HETATM 6236 O  O   . HOH N 3 .   ? 3.916   31.239  -7.317  1.00 24.18 ? 302 HOH C O   1 
HETATM 6237 O  O   . HOH N 3 .   ? -9.599  12.099  13.601  1.00 27.74 ? 303 HOH C O   1 
HETATM 6238 O  O   . HOH N 3 .   ? -10.828 41.835  18.936  1.00 31.40 ? 304 HOH C O   1 
HETATM 6239 O  O   . HOH N 3 .   ? -1.350  20.612  28.248  1.00 42.89 ? 305 HOH C O   1 
HETATM 6240 O  O   . HOH N 3 .   ? 5.501   32.812  25.970  1.00 38.66 ? 306 HOH C O   1 
HETATM 6241 O  O   . HOH N 3 .   ? -12.285 18.967  21.199  1.00 36.55 ? 307 HOH C O   1 
HETATM 6242 O  O   . HOH N 3 .   ? -18.494 21.907  2.262   1.00 32.16 ? 308 HOH C O   1 
HETATM 6243 O  O   . HOH N 3 .   ? -22.440 23.026  10.223  1.00 34.43 ? 309 HOH C O   1 
HETATM 6244 O  O   . HOH N 3 .   ? 4.965   20.811  17.331  1.00 23.27 ? 310 HOH C O   1 
HETATM 6245 O  O   . HOH N 3 .   ? 3.094   33.771  -6.158  1.00 22.61 ? 311 HOH C O   1 
HETATM 6246 O  O   . HOH N 3 .   ? -12.405 30.572  -7.421  1.00 34.15 ? 312 HOH C O   1 
HETATM 6247 O  O   . HOH N 3 .   ? 0.217   24.497  -2.036  1.00 31.38 ? 313 HOH C O   1 
HETATM 6248 O  O   . HOH N 3 .   ? -7.709  29.273  -2.027  1.00 21.92 ? 314 HOH C O   1 
HETATM 6249 O  O   . HOH N 3 .   ? -0.501  38.950  11.000  1.00 27.37 ? 315 HOH C O   1 
HETATM 6250 O  O   . HOH N 3 .   ? -9.029  29.509  25.861  1.00 24.47 ? 316 HOH C O   1 
HETATM 6251 O  O   . HOH N 3 .   ? 7.262   18.018  15.435  1.00 29.83 ? 317 HOH C O   1 
HETATM 6252 O  O   . HOH N 3 .   ? -9.836  27.412  -8.430  1.00 26.80 ? 318 HOH C O   1 
HETATM 6253 O  O   . HOH N 3 .   ? -1.360  23.970  7.362   1.00 21.62 ? 319 HOH C O   1 
HETATM 6254 O  O   . HOH N 3 .   ? -15.126 49.710  -1.572  1.00 44.14 ? 320 HOH C O   1 
HETATM 6255 O  O   . HOH N 3 .   ? -7.257  28.861  11.915  1.00 23.84 ? 321 HOH C O   1 
HETATM 6256 O  O   . HOH N 3 .   ? -19.747 18.376  8.829   1.00 30.17 ? 322 HOH C O   1 
HETATM 6257 O  O   . HOH N 3 .   ? -0.590  39.992  15.718  1.00 34.70 ? 323 HOH C O   1 
HETATM 6258 O  O   . HOH N 3 .   ? -1.936  36.665  14.018  1.00 35.26 ? 324 HOH C O   1 
HETATM 6259 O  O   . HOH N 3 .   ? 1.912   33.900  8.003   1.00 35.42 ? 325 HOH C O   1 
HETATM 6260 O  O   . HOH N 3 .   ? 0.469   24.579  30.006  1.00 38.78 ? 326 HOH C O   1 
HETATM 6261 O  O   . HOH N 3 .   ? -3.852  23.602  -6.825  1.00 22.93 ? 327 HOH C O   1 
HETATM 6262 O  O   . HOH N 3 .   ? -4.780  26.984  31.805  1.00 47.01 ? 328 HOH C O   1 
HETATM 6263 O  O   . HOH N 3 .   ? 4.061   23.909  17.429  1.00 21.32 ? 329 HOH C O   1 
HETATM 6264 O  O   . HOH N 3 .   ? 7.918   17.549  8.292   1.00 33.15 ? 330 HOH C O   1 
HETATM 6265 O  O   . HOH N 3 .   ? -8.293  51.913  6.940   1.00 29.73 ? 331 HOH C O   1 
HETATM 6266 O  O   . HOH N 3 .   ? -18.970 33.286  6.476   1.00 20.90 ? 332 HOH C O   1 
HETATM 6267 O  O   . HOH N 3 .   ? -11.633 41.539  14.967  1.00 23.69 ? 333 HOH C O   1 
HETATM 6268 O  O   . HOH N 3 .   ? -6.962  33.382  19.856  1.00 34.60 ? 334 HOH C O   1 
HETATM 6269 O  O   . HOH N 3 .   ? -8.623  35.485  -7.455  1.00 33.83 ? 335 HOH C O   1 
HETATM 6270 O  O   . HOH N 3 .   ? -14.629 26.617  22.733  1.00 30.86 ? 336 HOH C O   1 
HETATM 6271 O  O   . HOH N 3 .   ? -21.121 38.204  13.800  1.00 21.03 ? 337 HOH C O   1 
HETATM 6272 O  O   . HOH N 3 .   ? -2.147  38.195  -11.387 1.00 29.38 ? 338 HOH C O   1 
HETATM 6273 O  O   . HOH N 3 .   ? -2.860  34.822  -10.969 1.00 25.25 ? 339 HOH C O   1 
HETATM 6274 O  O   . HOH N 3 .   ? -3.678  18.784  25.265  1.00 35.65 ? 340 HOH C O   1 
HETATM 6275 O  O   . HOH N 3 .   ? -7.581  43.614  15.293  1.00 26.20 ? 341 HOH C O   1 
HETATM 6276 O  O   . HOH N 3 .   ? -10.020 45.117  15.729  1.00 39.09 ? 342 HOH C O   1 
HETATM 6277 O  O   . HOH N 3 .   ? -7.597  37.671  26.055  1.00 34.11 ? 343 HOH C O   1 
HETATM 6278 O  O   . HOH N 3 .   ? -7.201  27.714  -8.945  1.00 27.16 ? 344 HOH C O   1 
HETATM 6279 O  O   . HOH N 3 .   ? -19.489 40.527  -0.229  1.00 22.60 ? 345 HOH C O   1 
HETATM 6280 O  O   . HOH N 3 .   ? 0.370   21.846  -0.525  1.00 24.77 ? 346 HOH C O   1 
HETATM 6281 O  O   . HOH N 3 .   ? 1.954   12.330  19.859  1.00 27.74 ? 347 HOH C O   1 
HETATM 6282 O  O   . HOH N 3 .   ? 7.419   28.176  18.698  1.00 37.78 ? 348 HOH C O   1 
HETATM 6283 O  O   . HOH N 3 .   ? -12.793 35.504  22.305  1.00 39.12 ? 349 HOH C O   1 
HETATM 6284 O  O   . HOH N 3 .   ? -2.034  31.018  25.062  1.00 19.66 ? 350 HOH C O   1 
HETATM 6285 O  O   . HOH N 3 .   ? -16.022 16.505  13.814  1.00 31.97 ? 351 HOH C O   1 
HETATM 6286 O  O   . HOH N 3 .   ? 6.904   36.949  -2.552  1.00 22.76 ? 352 HOH C O   1 
HETATM 6287 O  O   . HOH N 3 .   ? 2.585   30.949  6.477   1.00 31.17 ? 353 HOH C O   1 
HETATM 6288 O  O   . HOH N 3 .   ? 0.718   17.155  -0.910  1.00 34.64 ? 354 HOH C O   1 
HETATM 6289 O  O   . HOH N 3 .   ? 2.331   21.311  6.059   1.00 32.17 ? 355 HOH C O   1 
HETATM 6290 O  O   . HOH N 3 .   ? -24.263 29.308  8.489   1.00 29.74 ? 356 HOH C O   1 
HETATM 6291 O  O   . HOH N 3 .   ? -15.568 45.729  1.090   1.00 27.13 ? 357 HOH C O   1 
HETATM 6292 O  O   . HOH N 3 .   ? -22.755 27.186  14.821  1.00 25.88 ? 358 HOH C O   1 
HETATM 6293 O  O   . HOH N 3 .   ? -17.889 44.822  2.262   1.00 32.09 ? 359 HOH C O   1 
HETATM 6294 O  O   . HOH N 3 .   ? -0.340  23.169  -2.767  1.00 30.11 ? 360 HOH C O   1 
HETATM 6295 O  O   . HOH N 3 .   ? -6.885  43.546  17.948  1.00 25.10 ? 361 HOH C O   1 
HETATM 6296 O  O   . HOH N 3 .   ? -3.811  10.485  10.501  1.00 23.29 ? 362 HOH C O   1 
HETATM 6297 O  O   . HOH N 3 .   ? 9.664   37.641  -0.975  1.00 25.62 ? 363 HOH C O   1 
HETATM 6298 O  O   . HOH N 3 .   ? -20.274 33.723  20.338  1.00 43.17 ? 364 HOH C O   1 
HETATM 6299 O  O   . HOH N 3 .   ? -3.271  10.428  6.612   1.00 30.85 ? 365 HOH C O   1 
HETATM 6300 O  O   . HOH N 3 .   ? 1.921   12.888  2.526   1.00 35.72 ? 366 HOH C O   1 
HETATM 6301 O  O   . HOH N 3 .   ? -0.562  4.165   14.659  1.00 41.83 ? 367 HOH C O   1 
HETATM 6302 O  O   . HOH N 3 .   ? -16.194 11.461  9.424   1.00 29.95 ? 368 HOH C O   1 
HETATM 6303 O  O   . HOH N 3 .   ? -19.070 30.811  -2.113  1.00 20.21 ? 369 HOH C O   1 
HETATM 6304 O  O   . HOH N 3 .   ? -21.979 42.976  3.392   1.00 29.36 ? 370 HOH C O   1 
HETATM 6305 O  O   . HOH N 3 .   ? 7.592   22.504  8.814   1.00 28.31 ? 371 HOH C O   1 
HETATM 6306 O  O   . HOH N 3 .   ? -5.014  13.965  16.892  1.00 25.41 ? 372 HOH C O   1 
HETATM 6307 O  O   . HOH N 3 .   ? -17.105 14.579  5.429   1.00 19.24 ? 373 HOH C O   1 
HETATM 6308 O  O   . HOH N 3 .   ? -22.815 34.028  14.908  1.00 37.51 ? 374 HOH C O   1 
HETATM 6309 O  O   . HOH N 3 .   ? -16.838 29.871  19.672  1.00 24.53 ? 375 HOH C O   1 
HETATM 6310 O  O   . HOH N 3 .   ? -26.531 41.713  4.279   1.00 45.19 ? 376 HOH C O   1 
HETATM 6311 O  O   . HOH N 3 .   ? -19.252 22.716  19.000  1.00 25.98 ? 377 HOH C O   1 
HETATM 6312 O  O   . HOH N 3 .   ? -4.167  9.723   3.620   1.00 15.82 ? 378 HOH C O   1 
HETATM 6313 O  O   . HOH N 3 .   ? 10.433  25.907  13.169  1.00 44.31 ? 379 HOH C O   1 
HETATM 6314 O  O   . HOH N 3 .   ? 6.215   15.873  5.221   1.00 38.44 ? 380 HOH C O   1 
HETATM 6315 O  O   . HOH N 3 .   ? -2.071  17.173  -1.107  1.00 22.14 ? 381 HOH C O   1 
HETATM 6316 O  O   . HOH N 3 .   ? -21.063 27.665  17.759  1.00 26.91 ? 382 HOH C O   1 
HETATM 6317 O  O   . HOH N 3 .   ? -11.146 17.993  -1.643  1.00 16.20 ? 383 HOH C O   1 
HETATM 6318 O  O   . HOH N 3 .   ? -8.250  30.848  -9.053  1.00 24.33 ? 384 HOH C O   1 
HETATM 6319 O  O   . HOH N 3 .   ? -5.976  45.458  14.269  1.00 30.66 ? 385 HOH C O   1 
HETATM 6320 O  O   . HOH N 3 .   ? -9.934  19.582  25.487  1.00 43.29 ? 386 HOH C O   1 
HETATM 6321 O  O   . HOH N 3 .   ? -14.434 39.060  17.269  1.00 26.09 ? 387 HOH C O   1 
HETATM 6322 O  O   . HOH N 3 .   ? -21.909 39.501  1.514   1.00 28.38 ? 388 HOH C O   1 
HETATM 6323 O  O   . HOH N 3 .   ? -0.258  11.520  2.660   1.00 31.58 ? 389 HOH C O   1 
HETATM 6324 O  O   . HOH N 3 .   ? 7.425   19.858  11.400  1.00 30.16 ? 390 HOH C O   1 
HETATM 6325 O  O   . HOH N 3 .   ? -16.840 23.558  20.338  1.00 24.00 ? 391 HOH C O   1 
HETATM 6326 O  O   . HOH N 3 .   ? -8.726  9.942   -1.530  1.00 12.07 ? 392 HOH C O   1 
HETATM 6327 O  O   . HOH N 3 .   ? 8.379   23.930  10.524  1.00 36.30 ? 393 HOH C O   1 
HETATM 6328 O  O   . HOH N 3 .   ? -1.252  11.909  0.377   1.00 17.74 ? 394 HOH C O   1 
HETATM 6329 O  O   . HOH N 3 .   ? -20.562 22.381  14.881  1.00 22.36 ? 395 HOH C O   1 
HETATM 6330 O  O   . HOH N 3 .   ? -9.091  21.496  26.158  1.00 38.16 ? 396 HOH C O   1 
HETATM 6331 O  O   . HOH N 3 .   ? 4.508   17.715  17.738  1.00 28.87 ? 397 HOH C O   1 
HETATM 6332 O  O   . HOH N 3 .   ? -24.459 30.562  12.465  1.00 34.68 ? 398 HOH C O   1 
HETATM 6333 O  O   . HOH N 3 .   ? -25.055 34.857  3.430   1.00 33.90 ? 399 HOH C O   1 
HETATM 6334 O  O   . HOH N 3 .   ? -2.466  40.327  12.133  1.00 31.46 ? 400 HOH C O   1 
HETATM 6335 O  O   . HOH N 3 .   ? 0.156   26.749  7.030   1.00 24.00 ? 401 HOH C O   1 
HETATM 6336 O  O   . HOH N 3 .   ? 4.290   16.195  3.269   1.00 28.42 ? 402 HOH C O   1 
HETATM 6337 O  O   . HOH N 3 .   ? -17.418 48.036  4.770   1.00 37.26 ? 403 HOH C O   1 
HETATM 6338 O  O   . HOH N 3 .   ? -12.771 41.116  17.852  1.00 46.97 ? 404 HOH C O   1 
HETATM 6339 O  O   . HOH N 3 .   ? -18.284 36.206  20.283  1.00 36.36 ? 405 HOH C O   1 
HETATM 6340 O  O   . HOH N 3 .   ? -10.961 29.278  -2.877  1.00 21.28 ? 406 HOH C O   1 
HETATM 6341 O  O   . HOH N 3 .   ? -7.946  40.459  -7.707  1.00 32.82 ? 407 HOH C O   1 
HETATM 6342 O  O   . HOH N 3 .   ? 4.801   13.632  9.499   1.00 33.02 ? 408 HOH C O   1 
HETATM 6343 O  O   . HOH N 3 .   ? -13.816 7.825   4.378   1.00 24.22 ? 409 HOH C O   1 
HETATM 6344 O  O   . HOH N 3 .   ? -11.185 46.666  -7.019  1.00 28.69 ? 410 HOH C O   1 
HETATM 6345 O  O   . HOH N 3 .   ? -9.591  37.676  23.496  1.00 36.69 ? 411 HOH C O   1 
HETATM 6346 O  O   . HOH N 3 .   ? 9.360   22.139  22.957  1.00 42.29 ? 412 HOH C O   1 
HETATM 6347 O  O   . HOH N 3 .   ? 8.186   28.029  3.672   1.00 37.10 ? 413 HOH C O   1 
HETATM 6348 O  O   . HOH N 3 .   ? -14.241 40.917  14.773  1.00 24.75 ? 414 HOH C O   1 
HETATM 6349 O  O   . HOH N 3 .   ? -24.925 33.362  1.414   1.00 37.04 ? 415 HOH C O   1 
HETATM 6350 O  O   . HOH N 3 .   ? -6.934  49.163  0.605   1.00 43.57 ? 416 HOH C O   1 
HETATM 6351 O  O   . HOH N 3 .   ? -13.235 31.277  22.549  1.00 44.12 ? 417 HOH C O   1 
HETATM 6352 O  O   . HOH N 3 .   ? 3.447   16.223  0.097   1.00 50.55 ? 418 HOH C O   1 
HETATM 6353 O  O   . HOH N 3 .   ? 6.945   27.829  21.403  1.00 43.91 ? 419 HOH C O   1 
HETATM 6354 O  O   . HOH N 3 .   ? -0.515  32.237  -12.079 1.00 40.47 ? 420 HOH C O   1 
HETATM 6355 O  O   . HOH N 3 .   ? 3.799   18.925  25.694  1.00 36.92 ? 421 HOH C O   1 
HETATM 6356 O  O   . HOH N 3 .   ? 5.154   25.368  3.560   1.00 51.49 ? 422 HOH C O   1 
HETATM 6357 O  O   . HOH N 3 .   ? 2.456   24.528  -2.574  1.00 40.47 ? 423 HOH C O   1 
HETATM 6358 O  O   . HOH N 3 .   ? 8.932   19.385  13.636  1.00 39.57 ? 424 HOH C O   1 
HETATM 6359 O  O   . HOH N 3 .   ? 5.930   18.505  24.686  1.00 32.57 ? 425 HOH C O   1 
HETATM 6360 O  O   . HOH N 3 .   ? -9.507  43.603  19.111  1.00 43.61 ? 426 HOH C O   1 
HETATM 6361 O  O   . HOH N 3 .   ? -9.935  7.014   9.254   1.00 31.65 ? 427 HOH C O   1 
HETATM 6362 O  O   . HOH N 3 .   ? -16.912 34.640  22.112  1.00 40.38 ? 428 HOH C O   1 
HETATM 6363 O  O   . HOH N 3 .   ? -25.221 41.139  2.276   1.00 47.13 ? 429 HOH C O   1 
HETATM 6364 O  O   . HOH N 3 .   ? 2.367   28.433  6.210   1.00 45.06 ? 430 HOH C O   1 
HETATM 6365 O  O   . HOH N 3 .   ? -12.882 32.113  24.784  1.00 51.87 ? 431 HOH C O   1 
HETATM 6366 O  O   . HOH N 3 .   ? -29.501 36.849  10.769  1.00 42.33 ? 432 HOH C O   1 
HETATM 6367 O  O   . HOH N 3 .   ? 15.559  32.363  3.414   1.00 40.78 ? 433 HOH C O   1 
HETATM 6368 O  O   . HOH N 3 .   ? -20.555 40.866  -2.777  1.00 44.36 ? 434 HOH C O   1 
HETATM 6369 O  O   . HOH N 3 .   ? -7.017  22.519  30.870  1.00 39.13 ? 435 HOH C O   1 
HETATM 6370 O  O   . HOH N 3 .   ? 1.967   23.208  1.420   1.00 40.81 ? 436 HOH C O   1 
HETATM 6371 O  O   . HOH N 3 .   ? 1.149   39.947  14.545  1.00 47.47 ? 437 HOH C O   1 
HETATM 6372 O  O   . HOH N 3 .   ? -11.164 44.858  -8.210  1.00 37.06 ? 438 HOH C O   1 
HETATM 6373 O  O   . HOH N 3 .   ? -10.772 8.030   -0.901  1.00 37.25 ? 439 HOH C O   1 
HETATM 6374 O  O   . HOH N 3 .   ? -4.149  8.548   8.047   1.00 48.97 ? 440 HOH C O   1 
HETATM 6375 O  O   . HOH N 3 .   ? -7.305  34.184  -11.542 1.00 42.59 ? 441 HOH C O   1 
HETATM 6376 O  O   . HOH N 3 .   ? -18.726 21.196  23.810  1.00 39.03 ? 442 HOH C O   1 
HETATM 6377 O  O   . HOH N 3 .   ? -10.604 35.745  -5.622  1.00 34.88 ? 443 HOH C O   1 
HETATM 6378 O  O   . HOH N 3 .   ? -6.308  26.283  -10.565 1.00 50.54 ? 444 HOH C O   1 
HETATM 6379 O  O   . HOH N 3 .   ? -2.456  34.777  16.279  1.00 33.14 ? 445 HOH C O   1 
HETATM 6380 O  O   . HOH N 3 .   ? -22.540 22.665  13.390  1.00 42.25 ? 446 HOH C O   1 
HETATM 6381 O  O   . HOH N 3 .   ? -6.845  48.367  14.858  1.00 49.71 ? 447 HOH C O   1 
HETATM 6382 O  O   . HOH N 3 .   ? -22.764 34.455  20.384  1.00 37.13 ? 448 HOH C O   1 
HETATM 6383 O  O   . HOH N 3 .   ? -13.017 44.487  19.540  1.00 49.77 ? 449 HOH C O   1 
HETATM 6384 O  O   . HOH N 3 .   ? -16.278 6.994   5.245   1.00 46.09 ? 450 HOH C O   1 
HETATM 6385 O  O   . HOH N 3 .   ? 2.134   41.435  15.675  1.00 49.90 ? 451 HOH C O   1 
HETATM 6386 O  O   . HOH N 3 .   ? -8.724  47.787  -8.636  1.00 33.72 ? 452 HOH C O   1 
HETATM 6387 O  O   . HOH N 3 .   ? -2.874  46.583  -1.143  1.00 44.92 ? 453 HOH C O   1 
HETATM 6388 O  O   . HOH N 3 .   ? -16.871 28.466  21.504  1.00 44.39 ? 454 HOH C O   1 
HETATM 6389 O  O   . HOH N 3 .   ? -8.262  50.066  -7.441  1.00 41.54 ? 455 HOH C O   1 
HETATM 6390 O  O   . HOH N 3 .   ? -28.771 27.138  10.560  1.00 48.27 ? 456 HOH C O   1 
HETATM 6391 O  O   . HOH N 3 .   ? -21.401 21.986  23.580  1.00 52.36 ? 457 HOH C O   1 
HETATM 6392 O  O   . HOH O 3 .   ? -3.266  24.745  44.036  1.00 27.15 ? 301 HOH D O   1 
HETATM 6393 O  O   . HOH O 3 .   ? 13.577  49.392  47.884  1.00 41.78 ? 302 HOH D O   1 
HETATM 6394 O  O   . HOH O 3 .   ? -9.835  42.423  41.745  1.00 24.72 ? 303 HOH D O   1 
HETATM 6395 O  O   . HOH O 3 .   ? 8.470   22.564  31.191  1.00 30.31 ? 304 HOH D O   1 
HETATM 6396 O  O   . HOH O 3 .   ? 2.296   42.979  50.233  1.00 43.11 ? 305 HOH D O   1 
HETATM 6397 O  O   . HOH O 3 .   ? -0.720  50.538  40.801  1.00 32.61 ? 306 HOH D O   1 
HETATM 6398 O  O   . HOH O 3 .   ? 19.022  38.977  43.851  1.00 21.89 ? 307 HOH D O   1 
HETATM 6399 O  O   . HOH O 3 .   ? 2.524   23.541  54.936  1.00 44.28 ? 308 HOH D O   1 
HETATM 6400 O  O   . HOH O 3 .   ? 4.206   23.179  44.639  1.00 21.96 ? 309 HOH D O   1 
HETATM 6401 O  O   . HOH O 3 .   ? 16.335  34.597  50.524  1.00 26.71 ? 310 HOH D O   1 
HETATM 6402 O  O   . HOH O 3 .   ? 11.395  27.797  28.063  1.00 45.21 ? 311 HOH D O   1 
HETATM 6403 O  O   . HOH O 3 .   ? 8.915   46.216  18.850  1.00 45.30 ? 312 HOH D O   1 
HETATM 6404 O  O   . HOH O 3 .   ? 8.097   52.609  50.584  1.00 38.21 ? 313 HOH D O   1 
HETATM 6405 O  O   . HOH O 3 .   ? -2.434  27.466  45.070  1.00 30.13 ? 314 HOH D O   1 
HETATM 6406 O  O   . HOH O 3 .   ? 23.597  42.697  45.212  1.00 34.07 ? 315 HOH D O   1 
HETATM 6407 O  O   . HOH O 3 .   ? 12.147  48.983  30.647  1.00 32.75 ? 316 HOH D O   1 
HETATM 6408 O  O   . HOH O 3 .   ? 10.332  57.337  37.609  1.00 41.33 ? 317 HOH D O   1 
HETATM 6409 O  O   . HOH O 3 .   ? -5.650  39.327  23.922  1.00 26.16 ? 318 HOH D O   1 
HETATM 6410 O  O   . HOH O 3 .   ? -7.305  44.036  29.580  1.00 40.53 ? 319 HOH D O   1 
HETATM 6411 O  O   . HOH O 3 .   ? 7.185   47.895  51.660  1.00 45.72 ? 320 HOH D O   1 
HETATM 6412 O  O   . HOH O 3 .   ? 12.155  32.118  54.476  1.00 40.56 ? 321 HOH D O   1 
HETATM 6413 O  O   . HOH O 3 .   ? 1.317   30.852  30.531  1.00 27.86 ? 322 HOH D O   1 
HETATM 6414 O  O   . HOH O 3 .   ? 4.757   51.338  23.818  1.00 41.06 ? 323 HOH D O   1 
HETATM 6415 O  O   . HOH O 3 .   ? 20.679  35.061  51.876  1.00 27.18 ? 324 HOH D O   1 
HETATM 6416 O  O   . HOH O 3 .   ? 17.632  24.901  48.512  1.00 38.81 ? 325 HOH D O   1 
HETATM 6417 O  O   . HOH O 3 .   ? 19.437  39.408  40.341  1.00 21.07 ? 326 HOH D O   1 
HETATM 6418 O  O   . HOH O 3 .   ? 23.743  35.160  48.790  1.00 44.32 ? 327 HOH D O   1 
HETATM 6419 O  O   . HOH O 3 .   ? 25.976  43.549  41.659  1.00 45.47 ? 328 HOH D O   1 
HETATM 6420 O  O   . HOH O 3 .   ? 8.177   30.567  53.628  1.00 28.91 ? 329 HOH D O   1 
HETATM 6421 O  O   . HOH O 3 .   ? 11.516  49.269  24.898  1.00 32.42 ? 330 HOH D O   1 
HETATM 6422 O  O   . HOH O 3 .   ? 9.604   30.121  46.773  1.00 22.02 ? 331 HOH D O   1 
HETATM 6423 O  O   . HOH O 3 .   ? -8.505  41.346  34.055  1.00 35.69 ? 332 HOH D O   1 
HETATM 6424 O  O   . HOH O 3 .   ? 10.992  44.640  33.028  1.00 25.56 ? 333 HOH D O   1 
HETATM 6425 O  O   . HOH O 3 .   ? 28.128  39.039  32.255  1.00 38.04 ? 334 HOH D O   1 
HETATM 6426 O  O   . HOH O 3 .   ? -6.215  42.874  38.370  1.00 41.81 ? 335 HOH D O   1 
HETATM 6427 O  O   . HOH O 3 .   ? 11.157  45.899  51.056  1.00 49.24 ? 336 HOH D O   1 
HETATM 6428 O  O   . HOH O 3 .   ? 4.822   21.414  31.269  1.00 41.11 ? 337 HOH D O   1 
HETATM 6429 O  O   . HOH O 3 .   ? -8.140  35.124  34.910  1.00 42.08 ? 338 HOH D O   1 
HETATM 6430 O  O   . HOH O 3 .   ? 24.612  27.779  48.183  1.00 39.86 ? 339 HOH D O   1 
HETATM 6431 O  O   . HOH O 3 .   ? 25.550  34.724  42.519  1.00 45.31 ? 340 HOH D O   1 
HETATM 6432 O  O   . HOH O 3 .   ? 2.073   24.020  47.778  1.00 44.35 ? 341 HOH D O   1 
HETATM 6433 O  O   . HOH O 3 .   ? 2.704   47.386  24.090  1.00 24.93 ? 342 HOH D O   1 
HETATM 6434 O  O   . HOH O 3 .   ? 8.940   40.711  21.252  1.00 33.42 ? 343 HOH D O   1 
HETATM 6435 O  O   . HOH O 3 .   ? 5.872   45.822  18.376  1.00 51.23 ? 344 HOH D O   1 
HETATM 6436 O  O   . HOH O 3 .   ? 19.315  44.463  47.024  1.00 26.34 ? 345 HOH D O   1 
HETATM 6437 O  O   . HOH O 3 .   ? -7.492  51.652  24.143  1.00 43.96 ? 346 HOH D O   1 
HETATM 6438 O  O   . HOH O 3 .   ? 1.271   49.739  48.867  1.00 32.29 ? 347 HOH D O   1 
HETATM 6439 O  O   . HOH O 3 .   ? 6.602   25.580  22.930  1.00 26.33 ? 348 HOH D O   1 
HETATM 6440 O  O   . HOH O 3 .   ? 5.197   47.449  49.977  1.00 24.50 ? 349 HOH D O   1 
HETATM 6441 O  O   . HOH O 3 .   ? 5.830   29.382  53.354  1.00 25.04 ? 350 HOH D O   1 
HETATM 6442 O  O   . HOH O 3 .   ? 7.042   36.840  35.086  1.00 27.83 ? 351 HOH D O   1 
HETATM 6443 O  O   . HOH O 3 .   ? -8.708  38.968  32.772  1.00 34.20 ? 352 HOH D O   1 
HETATM 6444 O  O   . HOH O 3 .   ? -1.174  24.433  40.109  1.00 31.88 ? 353 HOH D O   1 
HETATM 6445 O  O   . HOH O 3 .   ? -3.915  27.605  42.048  1.00 49.22 ? 354 HOH D O   1 
HETATM 6446 O  O   . HOH O 3 .   ? 14.175  24.822  23.633  1.00 48.42 ? 355 HOH D O   1 
HETATM 6447 O  O   . HOH O 3 .   ? 1.774   20.232  43.576  1.00 31.32 ? 356 HOH D O   1 
HETATM 6448 O  O   . HOH O 3 .   ? 3.628   44.075  24.349  1.00 23.09 ? 357 HOH D O   1 
HETATM 6449 O  O   . HOH O 3 .   ? 16.270  43.477  30.759  1.00 37.62 ? 358 HOH D O   1 
HETATM 6450 O  O   . HOH O 3 .   ? 5.100   41.399  19.332  1.00 31.10 ? 359 HOH D O   1 
HETATM 6451 O  O   . HOH O 3 .   ? 4.808   16.000  37.314  1.00 30.86 ? 360 HOH D O   1 
HETATM 6452 O  O   . HOH O 3 .   ? -0.259  21.003  39.350  1.00 34.03 ? 361 HOH D O   1 
HETATM 6453 O  O   . HOH O 3 .   ? -3.587  36.817  46.658  1.00 31.45 ? 362 HOH D O   1 
HETATM 6454 O  O   . HOH O 3 .   ? 3.275   55.136  37.421  1.00 33.23 ? 363 HOH D O   1 
HETATM 6455 O  O   . HOH O 3 .   ? -0.012  42.176  19.652  1.00 22.27 ? 364 HOH D O   1 
HETATM 6456 O  O   . HOH O 3 .   ? 22.883  46.396  39.094  1.00 34.32 ? 365 HOH D O   1 
HETATM 6457 O  O   . HOH O 3 .   ? -2.575  33.838  25.026  1.00 20.31 ? 366 HOH D O   1 
HETATM 6458 O  O   . HOH O 3 .   ? 15.100  24.397  50.203  1.00 41.29 ? 367 HOH D O   1 
HETATM 6459 O  O   . HOH O 3 .   ? 3.927   24.376  57.017  1.00 48.51 ? 368 HOH D O   1 
HETATM 6460 O  O   . HOH O 3 .   ? 13.429  46.234  50.445  1.00 43.03 ? 369 HOH D O   1 
HETATM 6461 O  O   . HOH O 3 .   ? 5.886   38.690  18.433  1.00 36.66 ? 370 HOH D O   1 
HETATM 6462 O  O   . HOH O 3 .   ? 19.300  20.890  43.392  1.00 34.67 ? 371 HOH D O   1 
HETATM 6463 O  O   . HOH O 3 .   ? 8.106   19.406  32.845  1.00 37.31 ? 372 HOH D O   1 
HETATM 6464 O  O   . HOH O 3 .   ? 4.903   31.151  51.405  1.00 22.14 ? 373 HOH D O   1 
HETATM 6465 O  O   . HOH O 3 .   ? 27.350  24.960  40.606  1.00 40.26 ? 374 HOH D O   1 
HETATM 6466 O  O   . HOH O 3 .   ? 30.594  37.094  39.461  1.00 40.04 ? 375 HOH D O   1 
HETATM 6467 O  O   . HOH O 3 .   ? 18.011  50.882  42.325  1.00 15.68 ? 376 HOH D O   1 
HETATM 6468 O  O   . HOH O 3 .   ? 0.783   26.775  46.757  1.00 35.15 ? 377 HOH D O   1 
HETATM 6469 O  O   . HOH O 3 .   ? 14.690  48.864  45.543  1.00 21.24 ? 378 HOH D O   1 
HETATM 6470 O  O   . HOH O 3 .   ? -2.812  26.780  37.734  1.00 25.02 ? 379 HOH D O   1 
HETATM 6471 O  O   . HOH O 3 .   ? -2.519  30.808  40.568  1.00 25.80 ? 380 HOH D O   1 
HETATM 6472 O  O   . HOH O 3 .   ? 8.142   50.388  24.827  1.00 23.54 ? 381 HOH D O   1 
HETATM 6473 O  O   . HOH O 3 .   ? -3.918  38.345  47.637  1.00 29.23 ? 382 HOH D O   1 
HETATM 6474 O  O   . HOH O 3 .   ? 2.598   36.625  15.960  1.00 46.00 ? 383 HOH D O   1 
HETATM 6475 O  O   . HOH O 3 .   ? 10.378  21.586  29.466  1.00 36.55 ? 384 HOH D O   1 
HETATM 6476 O  O   . HOH O 3 .   ? 8.919   57.804  44.570  1.00 36.67 ? 385 HOH D O   1 
HETATM 6477 O  O   . HOH O 3 .   ? 17.914  50.390  35.359  1.00 23.08 ? 386 HOH D O   1 
HETATM 6478 O  O   . HOH O 3 .   ? 17.140  48.831  44.602  1.00 20.44 ? 387 HOH D O   1 
HETATM 6479 O  O   . HOH O 3 .   ? -2.863  26.129  47.347  1.00 43.35 ? 388 HOH D O   1 
HETATM 6480 O  O   . HOH O 3 .   ? 28.301  34.944  30.433  1.00 33.50 ? 389 HOH D O   1 
HETATM 6481 O  O   . HOH O 3 .   ? 26.866  46.149  33.188  1.00 33.83 ? 390 HOH D O   1 
HETATM 6482 O  O   . HOH O 3 .   ? 9.353   31.652  28.054  1.00 37.52 ? 391 HOH D O   1 
HETATM 6483 O  O   . HOH O 3 .   ? -1.874  43.441  47.601  1.00 35.95 ? 392 HOH D O   1 
HETATM 6484 O  O   . HOH O 3 .   ? -2.144  49.901  34.817  1.00 28.08 ? 393 HOH D O   1 
HETATM 6485 O  O   . HOH O 3 .   ? 4.310   55.094  49.248  1.00 31.08 ? 394 HOH D O   1 
HETATM 6486 O  O   . HOH O 3 .   ? 1.390   49.811  25.095  1.00 30.30 ? 395 HOH D O   1 
HETATM 6487 O  O   . HOH O 3 .   ? -1.631  44.585  45.415  1.00 27.72 ? 396 HOH D O   1 
HETATM 6488 O  O   . HOH O 3 .   ? 12.504  57.021  38.930  1.00 25.77 ? 397 HOH D O   1 
HETATM 6489 O  O   . HOH O 3 .   ? 19.475  47.650  45.525  1.00 42.56 ? 398 HOH D O   1 
HETATM 6490 O  O   . HOH O 3 .   ? 7.836   22.451  50.668  1.00 41.41 ? 399 HOH D O   1 
HETATM 6491 O  O   . HOH O 3 .   ? 5.741   56.279  37.920  1.00 29.66 ? 400 HOH D O   1 
HETATM 6492 O  O   . HOH O 3 .   ? 3.114   56.492  28.231  1.00 36.71 ? 401 HOH D O   1 
HETATM 6493 O  O   . HOH O 3 .   ? 12.228  41.797  51.007  1.00 30.86 ? 402 HOH D O   1 
HETATM 6494 O  O   . HOH O 3 .   ? -1.784  37.701  47.779  1.00 34.89 ? 403 HOH D O   1 
HETATM 6495 O  O   . HOH O 3 .   ? 11.937  57.002  35.915  1.00 36.88 ? 404 HOH D O   1 
HETATM 6496 O  O   . HOH O 3 .   ? -5.668  32.437  31.113  1.00 39.15 ? 405 HOH D O   1 
HETATM 6497 O  O   . HOH O 3 .   ? -4.487  28.960  33.252  1.00 40.26 ? 406 HOH D O   1 
HETATM 6498 O  O   . HOH O 3 .   ? 27.587  32.916  42.957  1.00 47.75 ? 407 HOH D O   1 
HETATM 6499 O  O   . HOH O 3 .   ? 3.627   23.826  37.018  1.00 27.08 ? 408 HOH D O   1 
HETATM 6500 O  O   . HOH O 3 .   ? 13.988  54.234  31.627  1.00 30.27 ? 409 HOH D O   1 
HETATM 6501 O  O   . HOH O 3 .   ? 25.870  39.855  43.791  1.00 32.51 ? 410 HOH D O   1 
HETATM 6502 O  O   . HOH O 3 .   ? 6.168   21.770  29.086  1.00 31.48 ? 411 HOH D O   1 
HETATM 6503 O  O   . HOH O 3 .   ? 24.375  35.360  44.264  1.00 24.96 ? 412 HOH D O   1 
HETATM 6504 O  O   . HOH O 3 .   ? -8.645  35.684  37.077  1.00 48.10 ? 413 HOH D O   1 
HETATM 6505 O  O   . HOH O 3 .   ? -2.621  29.655  37.270  1.00 25.36 ? 414 HOH D O   1 
HETATM 6506 O  O   . HOH O 3 .   ? 24.952  43.384  21.448  1.00 45.85 ? 415 HOH D O   1 
HETATM 6507 O  O   . HOH O 3 .   ? 25.147  42.950  43.224  1.00 34.54 ? 416 HOH D O   1 
HETATM 6508 O  O   . HOH O 3 .   ? 3.026   21.871  32.801  1.00 39.09 ? 417 HOH D O   1 
HETATM 6509 O  O   . HOH O 3 .   ? 13.437  28.910  27.098  1.00 35.53 ? 418 HOH D O   1 
HETATM 6510 O  O   . HOH O 3 .   ? -4.028  54.627  33.098  1.00 45.17 ? 419 HOH D O   1 
HETATM 6511 O  O   . HOH O 3 .   ? 0.318   44.411  17.930  1.00 43.10 ? 420 HOH D O   1 
HETATM 6512 O  O   . HOH O 3 .   ? 14.542  46.080  24.631  1.00 51.70 ? 421 HOH D O   1 
HETATM 6513 O  O   . HOH O 3 .   ? 15.473  51.846  43.880  1.00 31.63 ? 422 HOH D O   1 
HETATM 6514 O  O   . HOH O 3 .   ? 6.106   22.666  37.770  1.00 29.28 ? 423 HOH D O   1 
HETATM 6515 O  O   . HOH O 3 .   ? 12.686  43.097  31.214  1.00 35.45 ? 424 HOH D O   1 
HETATM 6516 O  O   . HOH O 3 .   ? 14.100  30.320  21.574  1.00 46.16 ? 425 HOH D O   1 
HETATM 6517 O  O   . HOH O 3 .   ? -3.778  23.340  45.972  1.00 34.28 ? 426 HOH D O   1 
HETATM 6518 O  O   . HOH O 3 .   ? -1.136  25.390  30.782  1.00 35.01 ? 427 HOH D O   1 
HETATM 6519 O  O   . HOH O 3 .   ? 10.726  19.540  29.877  1.00 45.27 ? 428 HOH D O   1 
HETATM 6520 O  O   . HOH O 3 .   ? 9.790   37.163  30.767  1.00 31.39 ? 429 HOH D O   1 
HETATM 6521 O  O   . HOH O 3 .   ? 0.061   33.177  23.339  1.00 32.79 ? 430 HOH D O   1 
HETATM 6522 O  O   . HOH O 3 .   ? -5.059  49.863  39.436  1.00 49.43 ? 431 HOH D O   1 
HETATM 6523 O  O   . HOH O 3 .   ? 26.554  46.134  26.633  1.00 48.58 ? 432 HOH D O   1 
HETATM 6524 O  O   . HOH O 3 .   ? 10.352  48.640  22.187  1.00 48.16 ? 433 HOH D O   1 
HETATM 6525 O  O   . HOH O 3 .   ? 6.737   36.311  27.968  1.00 40.30 ? 434 HOH D O   1 
HETATM 6526 O  O   . HOH O 3 .   ? 13.639  51.323  29.830  1.00 32.08 ? 435 HOH D O   1 
HETATM 6527 O  O   . HOH O 3 .   ? 1.685   56.630  45.064  1.00 42.86 ? 436 HOH D O   1 
HETATM 6528 O  O   . HOH O 3 .   ? -8.800  40.072  29.803  1.00 41.92 ? 437 HOH D O   1 
HETATM 6529 O  O   . HOH O 3 .   ? -3.948  51.511  38.020  1.00 43.14 ? 438 HOH D O   1 
HETATM 6530 O  O   . HOH O 3 .   ? 10.750  45.646  20.560  1.00 40.92 ? 439 HOH D O   1 
HETATM 6531 O  O   . HOH O 3 .   ? 6.525   49.449  18.341  1.00 36.27 ? 440 HOH D O   1 
HETATM 6532 O  O   . HOH O 3 .   ? -4.321  40.845  48.555  1.00 32.71 ? 441 HOH D O   1 
HETATM 6533 O  O   . HOH O 3 .   ? 23.486  33.570  43.808  1.00 41.67 ? 442 HOH D O   1 
HETATM 6534 O  O   . HOH O 3 .   ? 24.275  17.542  39.902  1.00 47.60 ? 443 HOH D O   1 
HETATM 6535 O  O   . HOH O 3 .   ? 11.083  39.741  22.720  1.00 49.96 ? 444 HOH D O   1 
HETATM 6536 O  O   . HOH O 3 .   ? -8.285  49.829  30.148  1.00 42.55 ? 445 HOH D O   1 
HETATM 6537 O  O   . HOH O 3 .   ? 31.338  34.959  32.184  1.00 47.83 ? 446 HOH D O   1 
HETATM 6538 O  O   . HOH O 3 .   ? 26.420  19.967  36.005  1.00 43.67 ? 447 HOH D O   1 
HETATM 6539 O  O   . HOH O 3 .   ? -11.142 45.548  36.511  1.00 46.68 ? 448 HOH D O   1 
HETATM 6540 O  O   . HOH O 3 .   ? 33.597  43.906  33.761  1.00 34.70 ? 449 HOH D O   1 
HETATM 6541 O  O   . HOH O 3 .   ? -4.328  31.064  42.698  1.00 29.69 ? 450 HOH D O   1 
HETATM 6542 O  O   . HOH O 3 .   ? 3.590   57.825  39.780  1.00 48.39 ? 451 HOH D O   1 
HETATM 6543 O  O   . HOH O 3 .   ? 26.398  27.925  19.225  1.00 42.29 ? 452 HOH D O   1 
HETATM 6544 O  O   . HOH O 3 .   ? 3.655   59.832  38.316  1.00 49.18 ? 453 HOH D O   1 
HETATM 6545 O  O   . HOH O 3 .   ? -2.957  43.423  51.260  1.00 52.28 ? 454 HOH D O   1 
HETATM 6546 O  O   . HOH O 3 .   ? 22.335  45.930  21.365  1.00 39.96 ? 455 HOH D O   1 
HETATM 6547 O  O   . HOH O 3 .   ? -9.570  30.593  28.665  1.00 45.92 ? 456 HOH D O   1 
HETATM 6548 O  O   . HOH O 3 .   ? 28.207  38.404  25.610  1.00 50.68 ? 457 HOH D O   1 
HETATM 6549 O  O   . HOH O 3 .   ? 7.037   47.614  53.969  1.00 44.89 ? 458 HOH D O   1 
HETATM 6550 O  O   . HOH O 3 .   ? 17.008  25.293  21.601  1.00 46.08 ? 459 HOH D O   1 
HETATM 6551 O  O   . HOH O 3 .   ? 7.075   20.133  27.443  1.00 39.32 ? 460 HOH D O   1 
HETATM 6552 O  O   . HOH O 3 .   ? -3.018  21.701  48.762  1.00 46.13 ? 461 HOH D O   1 
HETATM 6553 O  O   . HOH O 3 .   ? 19.467  48.246  28.068  1.00 38.91 ? 462 HOH D O   1 
HETATM 6554 O  O   . HOH O 3 .   ? 24.994  22.784  27.687  1.00 42.74 ? 463 HOH D O   1 
HETATM 6555 O  O   . HOH O 3 .   ? -4.714  52.795  40.026  1.00 43.47 ? 464 HOH D O   1 
HETATM 6556 O  O   . HOH O 3 .   ? 15.197  42.485  19.782  1.00 52.92 ? 465 HOH D O   1 
# 
