data_8XZX
# 
_entry.id   8XZX 
# 
_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   8XZX         pdb_00008xzx 10.2210/pdb8xzx/pdb 
WWPDB D_1300044557 ?            ?                   
# 
_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                        8XZX 
_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 21560.809 2   3.2.1.8 D30P,A33Q,K117Q,A167H ? ? 
2 water   nat water                  18.015    222 ?       ?                     ? ? 
# 
_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
VTTQNHFDAWKNAGLEMGTHNYMIVATEGYQSSGSASITVQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAGAGAGAGAGMEITSSETGTNNGYYYSFWTDGGGQVTYTNGPAGQYSVEWSNSGNFVAGKGWNPGSSQTITYSGEWNPN
GNSYLSVYGWTQNPLVEYYIVESFSTYDPSTGAQELGTVETDDGTYKIYQTTRENAPSIEGTATFNQYWSVRTDHRVGGT
VTTQNHFDAWKNAGLEMGTHNYMIVATEGYQSSGSASITVQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   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 GLU 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 
# 
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   -12 ?   ?   ?   A . n 
A 1 2   ALA 2   -11 ?   ?   ?   A . n 
A 1 3   GLY 3   -10 ?   ?   ?   A . n 
A 1 4   ALA 4   -9  ?   ?   ?   A . n 
A 1 5   GLY 5   -8  ?   ?   ?   A . n 
A 1 6   ALA 6   -7  ?   ?   ?   A . n 
A 1 7   GLY 7   -6  ?   ?   ?   A . n 
A 1 8   ALA 8   -5  ?   ?   ?   A . n 
A 1 9   GLY 9   -4  -4  GLY GLY A . n 
A 1 10  ALA 10  -3  -3  ALA ALA A . n 
A 1 11  GLY 11  -2  -2  GLY GLY A . n 
A 1 12  MET 12  -1  -1  MET MET A . n 
A 1 13  GLU 13  0   0   GLU GLU A . n 
A 1 14  ILE 14  1   1   ILE ILE A . n 
A 1 15  THR 15  2   2   THR THR A . n 
A 1 16  SER 16  3   3   SER SER A . n 
A 1 17  SER 17  4   4   SER SER A . n 
A 1 18  GLU 18  5   5   GLU GLU A . n 
A 1 19  THR 19  6   6   THR THR A . n 
A 1 20  GLY 20  7   7   GLY GLY A . n 
A 1 21  THR 21  8   8   THR THR A . n 
A 1 22  ASN 22  9   9   ASN ASN A . n 
A 1 23  ASN 23  10  10  ASN ASN A . n 
A 1 24  GLY 24  11  11  GLY GLY A . n 
A 1 25  TYR 25  12  12  TYR TYR A . n 
A 1 26  TYR 26  13  13  TYR TYR A . n 
A 1 27  TYR 27  14  14  TYR TYR A . n 
A 1 28  SER 28  15  15  SER SER A . n 
A 1 29  PHE 29  16  16  PHE PHE A . n 
A 1 30  TRP 30  17  17  TRP TRP A . n 
A 1 31  THR 31  18  18  THR THR A . n 
A 1 32  ASP 32  19  19  ASP ASP A . n 
A 1 33  GLY 33  20  20  GLY GLY A . n 
A 1 34  GLY 34  21  21  GLY GLY A . n 
A 1 35  GLY 35  22  22  GLY GLY A . n 
A 1 36  GLN 36  23  23  GLN GLN A . n 
A 1 37  VAL 37  24  24  VAL VAL A . n 
A 1 38  THR 38  25  25  THR THR A . n 
A 1 39  TYR 39  26  26  TYR TYR A . n 
A 1 40  THR 40  27  27  THR THR A . n 
A 1 41  ASN 41  28  28  ASN ASN A . n 
A 1 42  GLY 42  29  29  GLY GLY A . n 
A 1 43  PRO 43  30  30  PRO PRO A . n 
A 1 44  ALA 44  31  31  ALA ALA A . n 
A 1 45  GLY 45  32  32  GLY GLY A . n 
A 1 46  GLN 46  33  33  GLN GLN A . n 
A 1 47  TYR 47  34  34  TYR TYR A . n 
A 1 48  SER 48  35  35  SER SER A . n 
A 1 49  VAL 49  36  36  VAL VAL A . n 
A 1 50  GLU 50  37  37  GLU GLU A . n 
A 1 51  TRP 51  38  38  TRP TRP A . n 
A 1 52  SER 52  39  39  SER SER A . n 
A 1 53  ASN 53  40  40  ASN ASN A . n 
A 1 54  SER 54  41  41  SER SER A . n 
A 1 55  GLY 55  42  42  GLY GLY A . n 
A 1 56  ASN 56  43  43  ASN ASN A . n 
A 1 57  PHE 57  44  44  PHE PHE A . n 
A 1 58  VAL 58  45  45  VAL VAL A . n 
A 1 59  ALA 59  46  46  ALA ALA A . n 
A 1 60  GLY 60  47  47  GLY GLY A . n 
A 1 61  LYS 61  48  48  LYS LYS A . n 
A 1 62  GLY 62  49  49  GLY GLY A . n 
A 1 63  TRP 63  50  50  TRP TRP A . n 
A 1 64  ASN 64  51  51  ASN ASN A . n 
A 1 65  PRO 65  52  52  PRO PRO A . n 
A 1 66  GLY 66  53  53  GLY GLY A . n 
A 1 67  SER 67  54  54  SER SER A . n 
A 1 68  SER 68  55  55  SER SER A . n 
A 1 69  GLN 69  56  56  GLN GLN A . n 
A 1 70  THR 70  57  57  THR THR A . n 
A 1 71  ILE 71  58  58  ILE ILE A . n 
A 1 72  THR 72  59  59  THR THR A . n 
A 1 73  TYR 73  60  60  TYR TYR A . n 
A 1 74  SER 74  61  61  SER SER A . n 
A 1 75  GLY 75  62  62  GLY GLY A . n 
A 1 76  GLU 76  63  63  GLU GLU A . n 
A 1 77  TRP 77  64  64  TRP TRP A . n 
A 1 78  ASN 78  65  65  ASN ASN A . n 
A 1 79  PRO 79  66  66  PRO PRO A . n 
A 1 80  ASN 80  67  67  ASN ASN A . n 
A 1 81  GLY 81  68  68  GLY GLY A . n 
A 1 82  ASN 82  69  69  ASN ASN A . n 
A 1 83  SER 83  70  70  SER SER A . n 
A 1 84  TYR 84  71  71  TYR TYR A . n 
A 1 85  LEU 85  72  72  LEU LEU A . n 
A 1 86  SER 86  73  73  SER SER A . n 
A 1 87  VAL 87  74  74  VAL VAL A . n 
A 1 88  TYR 88  75  75  TYR TYR A . n 
A 1 89  GLY 89  76  76  GLY GLY A . n 
A 1 90  TRP 90  77  77  TRP TRP A . n 
A 1 91  THR 91  78  78  THR THR A . n 
A 1 92  GLN 92  79  79  GLN GLN A . n 
A 1 93  ASN 93  80  80  ASN ASN A . n 
A 1 94  PRO 94  81  81  PRO PRO A . n 
A 1 95  LEU 95  82  82  LEU LEU A . n 
A 1 96  VAL 96  83  83  VAL VAL A . n 
A 1 97  GLU 97  84  84  GLU GLU A . n 
A 1 98  TYR 98  85  85  TYR TYR A . n 
A 1 99  TYR 99  86  86  TYR TYR A . n 
A 1 100 ILE 100 87  87  ILE ILE A . n 
A 1 101 VAL 101 88  88  VAL VAL A . n 
A 1 102 GLU 102 89  89  GLU GLU A . n 
A 1 103 SER 103 90  90  SER SER A . n 
A 1 104 PHE 104 91  91  PHE PHE A . n 
A 1 105 SER 105 92  92  SER SER A . n 
A 1 106 THR 106 93  93  THR THR A . n 
A 1 107 TYR 107 94  94  TYR TYR A . n 
A 1 108 ASP 108 95  95  ASP ASP A . n 
A 1 109 PRO 109 96  96  PRO PRO A . n 
A 1 110 SER 110 97  97  SER SER A . n 
A 1 111 THR 111 98  98  THR THR A . n 
A 1 112 GLY 112 99  99  GLY GLY A . n 
A 1 113 ALA 113 100 100 ALA ALA A . n 
A 1 114 GLN 114 101 101 GLN GLN A . n 
A 1 115 GLU 115 102 102 GLU GLU A . n 
A 1 116 LEU 116 103 103 LEU LEU A . n 
A 1 117 GLY 117 104 104 GLY GLY A . n 
A 1 118 THR 118 105 105 THR THR A . n 
A 1 119 VAL 119 106 106 VAL VAL A . n 
A 1 120 GLU 120 107 107 GLU GLU A . n 
A 1 121 THR 121 108 108 THR THR A . n 
A 1 122 ASP 122 109 109 ASP ASP A . n 
A 1 123 ASP 123 110 110 ASP ASP A . n 
A 1 124 GLY 124 111 111 GLY GLY A . n 
A 1 125 THR 125 112 112 THR THR A . n 
A 1 126 TYR 126 113 113 TYR TYR A . n 
A 1 127 LYS 127 114 114 LYS LYS A . n 
A 1 128 ILE 128 115 115 ILE ILE A . n 
A 1 129 TYR 129 116 116 TYR TYR A . n 
A 1 130 GLN 130 117 117 GLN GLN A . n 
A 1 131 THR 131 118 118 THR THR A . n 
A 1 132 THR 132 119 119 THR THR A . n 
A 1 133 ARG 133 120 120 ARG ARG A . n 
A 1 134 GLU 134 121 121 GLU GLU A . n 
A 1 135 ASN 135 122 122 ASN ASN A . n 
A 1 136 ALA 136 123 123 ALA ALA A . n 
A 1 137 PRO 137 124 124 PRO PRO A . n 
A 1 138 SER 138 125 125 SER SER A . n 
A 1 139 ILE 139 126 126 ILE ILE A . n 
A 1 140 GLU 140 127 127 GLU GLU A . n 
A 1 141 GLY 141 128 128 GLY GLY A . n 
A 1 142 THR 142 129 129 THR THR A . n 
A 1 143 ALA 143 130 130 ALA ALA A . n 
A 1 144 THR 144 131 131 THR THR A . n 
A 1 145 PHE 145 132 132 PHE PHE A . n 
A 1 146 ASN 146 133 133 ASN ASN A . n 
A 1 147 GLN 147 134 134 GLN GLN A . n 
A 1 148 TYR 148 135 135 TYR TYR A . n 
A 1 149 TRP 149 136 136 TRP TRP A . n 
A 1 150 SER 150 137 137 SER SER A . n 
A 1 151 VAL 151 138 138 VAL VAL A . n 
A 1 152 ARG 152 139 139 ARG ARG A . n 
A 1 153 THR 153 140 140 THR THR A . n 
A 1 154 ASP 154 141 141 ASP ASP A . n 
A 1 155 HIS 155 142 142 HIS HIS A . n 
A 1 156 ARG 156 143 143 ARG ARG A . n 
A 1 157 VAL 157 144 144 VAL VAL A . n 
A 1 158 GLY 158 145 145 GLY GLY A . n 
A 1 159 GLY 159 146 146 GLY GLY A . n 
A 1 160 THR 160 147 147 THR THR A . n 
A 1 161 VAL 161 148 148 VAL VAL A . n 
A 1 162 THR 162 149 149 THR THR A . n 
A 1 163 THR 163 150 150 THR THR A . n 
A 1 164 GLN 164 151 151 GLN GLN A . n 
A 1 165 ASN 165 152 152 ASN ASN A . n 
A 1 166 HIS 166 153 153 HIS HIS A . n 
A 1 167 PHE 167 154 154 PHE PHE A . n 
A 1 168 ASP 168 155 155 ASP ASP A . n 
A 1 169 ALA 169 156 156 ALA ALA A . n 
A 1 170 TRP 170 157 157 TRP TRP A . n 
A 1 171 LYS 171 158 158 LYS LYS A . n 
A 1 172 ASN 172 159 159 ASN ASN A . n 
A 1 173 ALA 173 160 160 ALA ALA A . n 
A 1 174 GLY 174 161 161 GLY GLY A . n 
A 1 175 LEU 175 162 162 LEU LEU A . n 
A 1 176 GLU 176 163 163 GLU GLU A . n 
A 1 177 MET 177 164 164 MET MET A . n 
A 1 178 GLY 178 165 165 GLY GLY A . n 
A 1 179 THR 179 166 166 THR THR A . n 
A 1 180 HIS 180 167 167 HIS HIS A . n 
A 1 181 ASN 181 168 168 ASN ASN A . n 
A 1 182 TYR 182 169 169 TYR TYR A . n 
A 1 183 MET 183 170 170 MET MET A . n 
A 1 184 ILE 184 171 171 ILE ILE A . n 
A 1 185 VAL 185 172 172 VAL VAL A . n 
A 1 186 ALA 186 173 173 ALA ALA A . n 
A 1 187 THR 187 174 174 THR THR A . n 
A 1 188 GLU 188 175 175 GLU GLU A . n 
A 1 189 GLY 189 176 176 GLY GLY A . n 
A 1 190 TYR 190 177 177 TYR TYR A . n 
A 1 191 GLN 191 178 178 GLN GLN A . n 
A 1 192 SER 192 179 179 SER SER A . n 
A 1 193 SER 193 180 180 SER SER A . n 
A 1 194 GLY 194 181 181 GLY GLY A . n 
A 1 195 SER 195 182 182 SER SER A . n 
A 1 196 ALA 196 183 183 ALA ALA A . n 
A 1 197 SER 197 184 184 SER SER A . n 
A 1 198 ILE 198 185 185 ILE ILE A . n 
A 1 199 THR 199 186 186 THR THR A . n 
A 1 200 VAL 200 187 187 VAL VAL A . n 
A 1 201 GLN 201 188 188 GLN GLN A . n 
B 1 1   GLY 1   -12 ?   ?   ?   B . n 
B 1 2   ALA 2   -11 ?   ?   ?   B . n 
B 1 3   GLY 3   -10 ?   ?   ?   B . n 
B 1 4   ALA 4   -9  ?   ?   ?   B . n 
B 1 5   GLY 5   -8  ?   ?   ?   B . n 
B 1 6   ALA 6   -7  ?   ?   ?   B . n 
B 1 7   GLY 7   -6  ?   ?   ?   B . n 
B 1 8   ALA 8   -5  ?   ?   ?   B . n 
B 1 9   GLY 9   -4  ?   ?   ?   B . n 
B 1 10  ALA 10  -3  ?   ?   ?   B . n 
B 1 11  GLY 11  -2  ?   ?   ?   B . n 
B 1 12  MET 12  -1  ?   ?   ?   B . n 
B 1 13  GLU 13  0   0   GLU GLU B . n 
B 1 14  ILE 14  1   1   ILE ILE B . n 
B 1 15  THR 15  2   2   THR THR B . n 
B 1 16  SER 16  3   3   SER SER B . n 
B 1 17  SER 17  4   4   SER SER B . n 
B 1 18  GLU 18  5   5   GLU GLU B . n 
B 1 19  THR 19  6   6   THR THR B . n 
B 1 20  GLY 20  7   7   GLY GLY B . n 
B 1 21  THR 21  8   8   THR THR B . n 
B 1 22  ASN 22  9   9   ASN ASN B . n 
B 1 23  ASN 23  10  10  ASN ASN B . n 
B 1 24  GLY 24  11  11  GLY GLY B . n 
B 1 25  TYR 25  12  12  TYR TYR B . n 
B 1 26  TYR 26  13  13  TYR TYR B . n 
B 1 27  TYR 27  14  14  TYR TYR B . n 
B 1 28  SER 28  15  15  SER SER B . n 
B 1 29  PHE 29  16  16  PHE PHE B . n 
B 1 30  TRP 30  17  17  TRP TRP B . n 
B 1 31  THR 31  18  18  THR THR B . n 
B 1 32  ASP 32  19  19  ASP ASP B . n 
B 1 33  GLY 33  20  20  GLY GLY B . n 
B 1 34  GLY 34  21  21  GLY GLY B . n 
B 1 35  GLY 35  22  22  GLY GLY B . n 
B 1 36  GLN 36  23  23  GLN GLN B . n 
B 1 37  VAL 37  24  24  VAL VAL B . n 
B 1 38  THR 38  25  25  THR THR B . n 
B 1 39  TYR 39  26  26  TYR TYR B . n 
B 1 40  THR 40  27  27  THR THR B . n 
B 1 41  ASN 41  28  28  ASN ASN B . n 
B 1 42  GLY 42  29  29  GLY GLY B . n 
B 1 43  PRO 43  30  30  PRO PRO B . n 
B 1 44  ALA 44  31  31  ALA ALA B . n 
B 1 45  GLY 45  32  32  GLY GLY B . n 
B 1 46  GLN 46  33  33  GLN GLN B . n 
B 1 47  TYR 47  34  34  TYR TYR B . n 
B 1 48  SER 48  35  35  SER SER B . n 
B 1 49  VAL 49  36  36  VAL VAL B . n 
B 1 50  GLU 50  37  37  GLU GLU B . n 
B 1 51  TRP 51  38  38  TRP TRP B . n 
B 1 52  SER 52  39  39  SER SER B . n 
B 1 53  ASN 53  40  40  ASN ASN B . n 
B 1 54  SER 54  41  41  SER SER B . n 
B 1 55  GLY 55  42  42  GLY GLY B . n 
B 1 56  ASN 56  43  43  ASN ASN B . n 
B 1 57  PHE 57  44  44  PHE PHE B . n 
B 1 58  VAL 58  45  45  VAL VAL B . n 
B 1 59  ALA 59  46  46  ALA ALA B . n 
B 1 60  GLY 60  47  47  GLY GLY B . n 
B 1 61  LYS 61  48  48  LYS LYS B . n 
B 1 62  GLY 62  49  49  GLY GLY B . n 
B 1 63  TRP 63  50  50  TRP TRP B . n 
B 1 64  ASN 64  51  51  ASN ASN B . n 
B 1 65  PRO 65  52  52  PRO PRO B . n 
B 1 66  GLY 66  53  53  GLY GLY B . n 
B 1 67  SER 67  54  54  SER SER B . n 
B 1 68  SER 68  55  55  SER SER B . n 
B 1 69  GLN 69  56  56  GLN GLN B . n 
B 1 70  THR 70  57  57  THR THR B . n 
B 1 71  ILE 71  58  58  ILE ILE B . n 
B 1 72  THR 72  59  59  THR THR B . n 
B 1 73  TYR 73  60  60  TYR TYR B . n 
B 1 74  SER 74  61  61  SER SER B . n 
B 1 75  GLY 75  62  62  GLY GLY B . n 
B 1 76  GLU 76  63  63  GLU GLU B . n 
B 1 77  TRP 77  64  64  TRP TRP B . n 
B 1 78  ASN 78  65  65  ASN ASN B . n 
B 1 79  PRO 79  66  66  PRO PRO B . n 
B 1 80  ASN 80  67  67  ASN ASN B . n 
B 1 81  GLY 81  68  68  GLY GLY B . n 
B 1 82  ASN 82  69  69  ASN ASN B . n 
B 1 83  SER 83  70  70  SER SER B . n 
B 1 84  TYR 84  71  71  TYR TYR B . n 
B 1 85  LEU 85  72  72  LEU LEU B . n 
B 1 86  SER 86  73  73  SER SER B . n 
B 1 87  VAL 87  74  74  VAL VAL B . n 
B 1 88  TYR 88  75  75  TYR TYR B . n 
B 1 89  GLY 89  76  76  GLY GLY B . n 
B 1 90  TRP 90  77  77  TRP TRP B . n 
B 1 91  THR 91  78  78  THR THR B . n 
B 1 92  GLN 92  79  79  GLN GLN B . n 
B 1 93  ASN 93  80  80  ASN ASN B . n 
B 1 94  PRO 94  81  81  PRO PRO B . n 
B 1 95  LEU 95  82  82  LEU LEU B . n 
B 1 96  VAL 96  83  83  VAL VAL B . n 
B 1 97  GLU 97  84  84  GLU GLU B . n 
B 1 98  TYR 98  85  85  TYR TYR B . n 
B 1 99  TYR 99  86  86  TYR TYR B . n 
B 1 100 ILE 100 87  87  ILE ILE B . n 
B 1 101 VAL 101 88  88  VAL VAL B . n 
B 1 102 GLU 102 89  89  GLU GLU B . n 
B 1 103 SER 103 90  90  SER SER B . n 
B 1 104 PHE 104 91  91  PHE PHE B . n 
B 1 105 SER 105 92  92  SER SER B . n 
B 1 106 THR 106 93  93  THR THR B . n 
B 1 107 TYR 107 94  94  TYR TYR B . n 
B 1 108 ASP 108 95  95  ASP ASP B . n 
B 1 109 PRO 109 96  96  PRO PRO B . n 
B 1 110 SER 110 97  97  SER SER B . n 
B 1 111 THR 111 98  98  THR THR B . n 
B 1 112 GLY 112 99  99  GLY GLY B . n 
B 1 113 ALA 113 100 100 ALA ALA B . n 
B 1 114 GLN 114 101 101 GLN GLN B . n 
B 1 115 GLU 115 102 102 GLU GLU B . n 
B 1 116 LEU 116 103 103 LEU LEU B . n 
B 1 117 GLY 117 104 104 GLY GLY B . n 
B 1 118 THR 118 105 105 THR THR B . n 
B 1 119 VAL 119 106 106 VAL VAL B . n 
B 1 120 GLU 120 107 107 GLU GLU B . n 
B 1 121 THR 121 108 108 THR THR B . n 
B 1 122 ASP 122 109 109 ASP ASP B . n 
B 1 123 ASP 123 110 110 ASP ASP B . n 
B 1 124 GLY 124 111 111 GLY GLY B . n 
B 1 125 THR 125 112 112 THR THR B . n 
B 1 126 TYR 126 113 113 TYR TYR B . n 
B 1 127 LYS 127 114 114 LYS LYS B . n 
B 1 128 ILE 128 115 115 ILE ILE B . n 
B 1 129 TYR 129 116 116 TYR TYR B . n 
B 1 130 GLN 130 117 117 GLN GLN B . n 
B 1 131 THR 131 118 118 THR THR B . n 
B 1 132 THR 132 119 119 THR THR B . n 
B 1 133 ARG 133 120 120 ARG ARG B . n 
B 1 134 GLU 134 121 121 GLU GLU B . n 
B 1 135 ASN 135 122 122 ASN ASN B . n 
B 1 136 ALA 136 123 123 ALA ALA B . n 
B 1 137 PRO 137 124 124 PRO PRO B . n 
B 1 138 SER 138 125 125 SER SER B . n 
B 1 139 ILE 139 126 126 ILE ILE B . n 
B 1 140 GLU 140 127 127 GLU GLU B . n 
B 1 141 GLY 141 128 128 GLY GLY B . n 
B 1 142 THR 142 129 129 THR THR B . n 
B 1 143 ALA 143 130 130 ALA ALA B . n 
B 1 144 THR 144 131 131 THR THR B . n 
B 1 145 PHE 145 132 132 PHE PHE B . n 
B 1 146 ASN 146 133 133 ASN ASN B . n 
B 1 147 GLN 147 134 134 GLN GLN B . n 
B 1 148 TYR 148 135 135 TYR TYR B . n 
B 1 149 TRP 149 136 136 TRP TRP B . n 
B 1 150 SER 150 137 137 SER SER B . n 
B 1 151 VAL 151 138 138 VAL VAL B . n 
B 1 152 ARG 152 139 139 ARG ARG B . n 
B 1 153 THR 153 140 140 THR THR B . n 
B 1 154 ASP 154 141 141 ASP ASP B . n 
B 1 155 HIS 155 142 142 HIS HIS B . n 
B 1 156 ARG 156 143 143 ARG ARG B . n 
B 1 157 VAL 157 144 144 VAL VAL B . n 
B 1 158 GLY 158 145 145 GLY GLY B . n 
B 1 159 GLY 159 146 146 GLY GLY B . n 
B 1 160 THR 160 147 147 THR THR B . n 
B 1 161 VAL 161 148 148 VAL VAL B . n 
B 1 162 THR 162 149 149 THR THR B . n 
B 1 163 THR 163 150 150 THR THR B . n 
B 1 164 GLN 164 151 151 GLN GLN B . n 
B 1 165 ASN 165 152 152 ASN ASN B . n 
B 1 166 HIS 166 153 153 HIS HIS B . n 
B 1 167 PHE 167 154 154 PHE PHE B . n 
B 1 168 ASP 168 155 155 ASP ASP B . n 
B 1 169 ALA 169 156 156 ALA ALA B . n 
B 1 170 TRP 170 157 157 TRP TRP B . n 
B 1 171 LYS 171 158 158 LYS LYS B . n 
B 1 172 ASN 172 159 159 ASN ASN B . n 
B 1 173 ALA 173 160 160 ALA ALA B . n 
B 1 174 GLY 174 161 161 GLY GLY B . n 
B 1 175 LEU 175 162 162 LEU LEU B . n 
B 1 176 GLU 176 163 163 GLU GLU B . n 
B 1 177 MET 177 164 164 MET MET B . n 
B 1 178 GLY 178 165 165 GLY GLY B . n 
B 1 179 THR 179 166 166 THR THR B . n 
B 1 180 HIS 180 167 167 HIS HIS B . n 
B 1 181 ASN 181 168 168 ASN ASN B . n 
B 1 182 TYR 182 169 169 TYR TYR B . n 
B 1 183 MET 183 170 170 MET MET B . n 
B 1 184 ILE 184 171 171 ILE ILE B . n 
B 1 185 VAL 185 172 172 VAL VAL B . n 
B 1 186 ALA 186 173 173 ALA ALA B . n 
B 1 187 THR 187 174 174 THR THR B . n 
B 1 188 GLU 188 175 175 GLU GLU B . n 
B 1 189 GLY 189 176 176 GLY GLY B . n 
B 1 190 TYR 190 177 177 TYR TYR B . n 
B 1 191 GLN 191 178 178 GLN GLN B . n 
B 1 192 SER 192 179 179 SER SER B . n 
B 1 193 SER 193 180 180 SER SER B . n 
B 1 194 GLY 194 181 181 GLY GLY B . n 
B 1 195 SER 195 182 182 SER SER B . n 
B 1 196 ALA 196 183 183 ALA ALA B . n 
B 1 197 SER 197 184 184 SER SER B . n 
B 1 198 ILE 198 185 185 ILE ILE B . n 
B 1 199 THR 199 186 186 THR THR B . n 
B 1 200 VAL 200 187 187 VAL VAL B . n 
B 1 201 GLN 201 188 188 GLN GLN B . 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 
C 2 HOH 1   201 1   HOH HOH A . 
C 2 HOH 2   202 16  HOH HOH A . 
C 2 HOH 3   203 152 HOH HOH A . 
C 2 HOH 4   204 146 HOH HOH A . 
C 2 HOH 5   205 48  HOH HOH A . 
C 2 HOH 6   206 47  HOH HOH A . 
C 2 HOH 7   207 28  HOH HOH A . 
C 2 HOH 8   208 186 HOH HOH A . 
C 2 HOH 9   209 116 HOH HOH A . 
C 2 HOH 10  210 24  HOH HOH A . 
C 2 HOH 11  211 14  HOH HOH A . 
C 2 HOH 12  212 147 HOH HOH A . 
C 2 HOH 13  213 113 HOH HOH A . 
C 2 HOH 14  214 64  HOH HOH A . 
C 2 HOH 15  215 72  HOH HOH A . 
C 2 HOH 16  216 192 HOH HOH A . 
C 2 HOH 17  217 87  HOH HOH A . 
C 2 HOH 18  218 67  HOH HOH A . 
C 2 HOH 19  219 31  HOH HOH A . 
C 2 HOH 20  220 84  HOH HOH A . 
C 2 HOH 21  221 20  HOH HOH A . 
C 2 HOH 22  222 70  HOH HOH A . 
C 2 HOH 23  223 3   HOH HOH A . 
C 2 HOH 24  224 32  HOH HOH A . 
C 2 HOH 25  225 23  HOH HOH A . 
C 2 HOH 26  226 98  HOH HOH A . 
C 2 HOH 27  227 89  HOH HOH A . 
C 2 HOH 28  228 52  HOH HOH A . 
C 2 HOH 29  229 148 HOH HOH A . 
C 2 HOH 30  230 25  HOH HOH A . 
C 2 HOH 31  231 132 HOH HOH A . 
C 2 HOH 32  232 65  HOH HOH A . 
C 2 HOH 33  233 122 HOH HOH A . 
C 2 HOH 34  234 53  HOH HOH A . 
C 2 HOH 35  235 62  HOH HOH A . 
C 2 HOH 36  236 60  HOH HOH A . 
C 2 HOH 37  237 27  HOH HOH A . 
C 2 HOH 38  238 17  HOH HOH A . 
C 2 HOH 39  239 26  HOH HOH A . 
C 2 HOH 40  240 44  HOH HOH A . 
C 2 HOH 41  241 131 HOH HOH A . 
C 2 HOH 42  242 108 HOH HOH A . 
C 2 HOH 43  243 218 HOH HOH A . 
C 2 HOH 44  244 36  HOH HOH A . 
C 2 HOH 45  245 102 HOH HOH A . 
C 2 HOH 46  246 86  HOH HOH A . 
C 2 HOH 47  247 149 HOH HOH A . 
C 2 HOH 48  248 99  HOH HOH A . 
C 2 HOH 49  249 5   HOH HOH A . 
C 2 HOH 50  250 11  HOH HOH A . 
C 2 HOH 51  251 93  HOH HOH A . 
C 2 HOH 52  252 137 HOH HOH A . 
C 2 HOH 53  253 95  HOH HOH A . 
C 2 HOH 54  254 68  HOH HOH A . 
C 2 HOH 55  255 74  HOH HOH A . 
C 2 HOH 56  256 104 HOH HOH A . 
C 2 HOH 57  257 153 HOH HOH A . 
C 2 HOH 58  258 15  HOH HOH A . 
C 2 HOH 59  259 138 HOH HOH A . 
C 2 HOH 60  260 155 HOH HOH A . 
C 2 HOH 61  261 33  HOH HOH A . 
C 2 HOH 62  262 39  HOH HOH A . 
C 2 HOH 63  263 56  HOH HOH A . 
C 2 HOH 64  264 141 HOH HOH A . 
C 2 HOH 65  265 22  HOH HOH A . 
C 2 HOH 66  266 38  HOH HOH A . 
C 2 HOH 67  267 19  HOH HOH A . 
C 2 HOH 68  268 8   HOH HOH A . 
C 2 HOH 69  269 188 HOH HOH A . 
C 2 HOH 70  270 71  HOH HOH A . 
C 2 HOH 71  271 174 HOH HOH A . 
C 2 HOH 72  272 41  HOH HOH A . 
C 2 HOH 73  273 45  HOH HOH A . 
C 2 HOH 74  274 150 HOH HOH A . 
C 2 HOH 75  275 9   HOH HOH A . 
C 2 HOH 76  276 177 HOH HOH A . 
C 2 HOH 77  277 179 HOH HOH A . 
C 2 HOH 78  278 120 HOH HOH A . 
C 2 HOH 79  279 63  HOH HOH A . 
C 2 HOH 80  280 224 HOH HOH A . 
C 2 HOH 81  281 190 HOH HOH A . 
C 2 HOH 82  282 94  HOH HOH A . 
C 2 HOH 83  283 214 HOH HOH A . 
C 2 HOH 84  284 187 HOH HOH A . 
C 2 HOH 85  285 129 HOH HOH A . 
C 2 HOH 86  286 110 HOH HOH A . 
C 2 HOH 87  287 106 HOH HOH A . 
C 2 HOH 88  288 220 HOH HOH A . 
C 2 HOH 89  289 134 HOH HOH A . 
C 2 HOH 90  290 151 HOH HOH A . 
C 2 HOH 91  291 215 HOH HOH A . 
C 2 HOH 92  292 178 HOH HOH A . 
C 2 HOH 93  293 76  HOH HOH A . 
C 2 HOH 94  294 114 HOH HOH A . 
C 2 HOH 95  295 81  HOH HOH A . 
C 2 HOH 96  296 156 HOH HOH A . 
C 2 HOH 97  297 208 HOH HOH A . 
C 2 HOH 98  298 216 HOH HOH A . 
C 2 HOH 99  299 139 HOH HOH A . 
C 2 HOH 100 300 78  HOH HOH A . 
C 2 HOH 101 301 212 HOH HOH A . 
C 2 HOH 102 302 175 HOH HOH A . 
C 2 HOH 103 303 205 HOH HOH A . 
C 2 HOH 104 304 193 HOH HOH A . 
C 2 HOH 105 305 127 HOH HOH A . 
C 2 HOH 106 306 144 HOH HOH A . 
C 2 HOH 107 307 142 HOH HOH A . 
C 2 HOH 108 308 101 HOH HOH A . 
C 2 HOH 109 309 140 HOH HOH A . 
C 2 HOH 110 310 189 HOH HOH A . 
C 2 HOH 111 311 66  HOH HOH A . 
C 2 HOH 112 312 77  HOH HOH A . 
C 2 HOH 113 313 80  HOH HOH A . 
C 2 HOH 114 314 143 HOH HOH A . 
C 2 HOH 115 315 207 HOH HOH A . 
C 2 HOH 116 316 176 HOH HOH A . 
C 2 HOH 117 317 50  HOH HOH A . 
C 2 HOH 118 318 225 HOH HOH A . 
C 2 HOH 119 319 211 HOH HOH A . 
D 2 HOH 1   201 219 HOH HOH B . 
D 2 HOH 2   202 198 HOH HOH B . 
D 2 HOH 3   203 18  HOH HOH B . 
D 2 HOH 4   204 204 HOH HOH B . 
D 2 HOH 5   205 118 HOH HOH B . 
D 2 HOH 6   206 172 HOH HOH B . 
D 2 HOH 7   207 194 HOH HOH B . 
D 2 HOH 8   208 164 HOH HOH B . 
D 2 HOH 9   209 2   HOH HOH B . 
D 2 HOH 10  210 97  HOH HOH B . 
D 2 HOH 11  211 29  HOH HOH B . 
D 2 HOH 12  212 43  HOH HOH B . 
D 2 HOH 13  213 61  HOH HOH B . 
D 2 HOH 14  214 112 HOH HOH B . 
D 2 HOH 15  215 199 HOH HOH B . 
D 2 HOH 16  216 37  HOH HOH B . 
D 2 HOH 17  217 57  HOH HOH B . 
D 2 HOH 18  218 92  HOH HOH B . 
D 2 HOH 19  219 85  HOH HOH B . 
D 2 HOH 20  220 145 HOH HOH B . 
D 2 HOH 21  221 90  HOH HOH B . 
D 2 HOH 22  222 6   HOH HOH B . 
D 2 HOH 23  223 88  HOH HOH B . 
D 2 HOH 24  224 58  HOH HOH B . 
D 2 HOH 25  225 105 HOH HOH B . 
D 2 HOH 26  226 165 HOH HOH B . 
D 2 HOH 27  227 103 HOH HOH B . 
D 2 HOH 28  228 124 HOH HOH B . 
D 2 HOH 29  229 10  HOH HOH B . 
D 2 HOH 30  230 4   HOH HOH B . 
D 2 HOH 31  231 115 HOH HOH B . 
D 2 HOH 32  232 54  HOH HOH B . 
D 2 HOH 33  233 222 HOH HOH B . 
D 2 HOH 34  234 125 HOH HOH B . 
D 2 HOH 35  235 161 HOH HOH B . 
D 2 HOH 36  236 160 HOH HOH B . 
D 2 HOH 37  237 111 HOH HOH B . 
D 2 HOH 38  238 49  HOH HOH B . 
D 2 HOH 39  239 42  HOH HOH B . 
D 2 HOH 40  240 34  HOH HOH B . 
D 2 HOH 41  241 55  HOH HOH B . 
D 2 HOH 42  242 69  HOH HOH B . 
D 2 HOH 43  243 30  HOH HOH B . 
D 2 HOH 44  244 59  HOH HOH B . 
D 2 HOH 45  245 73  HOH HOH B . 
D 2 HOH 46  246 100 HOH HOH B . 
D 2 HOH 47  247 135 HOH HOH B . 
D 2 HOH 48  248 200 HOH HOH B . 
D 2 HOH 49  249 213 HOH HOH B . 
D 2 HOH 50  250 46  HOH HOH B . 
D 2 HOH 51  251 185 HOH HOH B . 
D 2 HOH 52  252 163 HOH HOH B . 
D 2 HOH 53  253 183 HOH HOH B . 
D 2 HOH 54  254 91  HOH HOH B . 
D 2 HOH 55  255 7   HOH HOH B . 
D 2 HOH 56  256 121 HOH HOH B . 
D 2 HOH 57  257 35  HOH HOH B . 
D 2 HOH 58  258 109 HOH HOH B . 
D 2 HOH 59  259 40  HOH HOH B . 
D 2 HOH 60  260 75  HOH HOH B . 
D 2 HOH 61  261 154 HOH HOH B . 
D 2 HOH 62  262 21  HOH HOH B . 
D 2 HOH 63  263 201 HOH HOH B . 
D 2 HOH 64  264 167 HOH HOH B . 
D 2 HOH 65  265 159 HOH HOH B . 
D 2 HOH 66  266 51  HOH HOH B . 
D 2 HOH 67  267 12  HOH HOH B . 
D 2 HOH 68  268 181 HOH HOH B . 
D 2 HOH 69  269 130 HOH HOH B . 
D 2 HOH 70  270 166 HOH HOH B . 
D 2 HOH 71  271 117 HOH HOH B . 
D 2 HOH 72  272 195 HOH HOH B . 
D 2 HOH 73  273 191 HOH HOH B . 
D 2 HOH 74  274 197 HOH HOH B . 
D 2 HOH 75  275 133 HOH HOH B . 
D 2 HOH 76  276 221 HOH HOH B . 
D 2 HOH 77  277 96  HOH HOH B . 
D 2 HOH 78  278 82  HOH HOH B . 
D 2 HOH 79  279 184 HOH HOH B . 
D 2 HOH 80  280 123 HOH HOH B . 
D 2 HOH 81  281 226 HOH HOH B . 
D 2 HOH 82  282 13  HOH HOH B . 
D 2 HOH 83  283 168 HOH HOH B . 
D 2 HOH 84  284 180 HOH HOH B . 
D 2 HOH 85  285 217 HOH HOH B . 
D 2 HOH 86  286 128 HOH HOH B . 
D 2 HOH 87  287 107 HOH HOH B . 
D 2 HOH 88  288 79  HOH HOH B . 
D 2 HOH 89  289 182 HOH HOH B . 
D 2 HOH 90  290 157 HOH HOH B . 
D 2 HOH 91  291 126 HOH HOH B . 
D 2 HOH 92  292 209 HOH HOH B . 
D 2 HOH 93  293 173 HOH HOH B . 
D 2 HOH 94  294 171 HOH HOH B . 
D 2 HOH 95  295 170 HOH HOH B . 
D 2 HOH 96  296 136 HOH HOH B . 
D 2 HOH 97  297 162 HOH HOH B . 
D 2 HOH 98  298 169 HOH HOH B . 
D 2 HOH 99  299 83  HOH HOH B . 
D 2 HOH 100 300 196 HOH HOH B . 
D 2 HOH 101 301 206 HOH HOH B . 
D 2 HOH 102 302 119 HOH HOH B . 
D 2 HOH 103 303 210 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  96.91 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.49 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  107.51 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XZX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.633 
_cell.length_a_esd                 ? 
_cell.length_b                     52.037 
_cell.length_b_esd                 ? 
_cell.length_c                     52.232 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8XZX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   8XZX 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M sodium formate, 0.1 M Bis-Tris propane 6.5, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   6.5 
_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                         'Bruker PHOTON III' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-01 
_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   1.34138 
_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                      'LIQUID ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER METALJET' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.34138 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XZX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               37.29 
_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                                     18177 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.52 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.59 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0713 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.30 
_reflns_shell.d_res_low                                     2.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.15 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             897 
_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                               3.28 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.2290 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            1.63 
_refine.aniso_B[1][2]                            0.88 
_refine.aniso_B[1][3]                            0.22 
_refine.aniso_B[2][2]                            -0.62 
_refine.aniso_B[2][3]                            -0.55 
_refine.aniso_B[3][3]                            -1.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.916 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.904 
_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                                 8XZX 
_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                            2.30 
_refine.ls_d_res_low                             37.29 
_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                     15202 
_refine.ls_number_reflns_R_free                  730 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.49 
_refine.ls_percent_reflns_R_free                 4.6 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16493 
_refine.ls_R_factor_R_free                       0.23142 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16165 
_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                       0.447 
_refine.pdbx_overall_ESU_R_Free                  0.259 
_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                             7.549 
_refine.overall_SU_ML                            0.178 
_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                       2.30 
_refine_hist.d_res_low                        37.29 
_refine_hist.number_atoms_solvent             226 
_refine_hist.number_atoms_total               3181 
_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        2955 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  0.012  3041 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  2406 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.503  1.650  4161 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.323  1.562  5620 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 9.433  5.000  380  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 41.453 24.625 160  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.485 15.000 407  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.794 15.000 6    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.060  0.200  396  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  3554 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  672  ? 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' ? 1.478  2.410  1526 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.478  2.409  1525 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.277  3.611  1904 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.277  3.612  1905 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.992  2.584  1515 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.985  2.581  1513 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.188  3.803  2257 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.413  27.601 3486 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.363  27.412 3451 ? 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                       2.300 
_refine_ls_shell.d_res_low                        2.360 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             38 
_refine_ls_shell.number_reflns_R_work             646 
_refine_ls_shell.percent_reflns_obs               49.67 
_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                  0.241 
_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                  0.327 
# 
_struct.entry_id                     8XZX 
_struct.title                        'Structure of an engineered xylanase Xyl-1 M4' 
_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        8XZX 
_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 2 ? 
D N N 2 ? 
# 
_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           33 
# 
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 8XZX A 14 ? 201 ? Q0CMZ1 33 ? 220 ? 1 188 
2 1 8XZX B 14 ? 201 ? Q0CMZ1 33 ? 220 ? 1 188 
# 
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 8XZX GLY A 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -12 1  
1 8XZX ALA A 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 2  
1 8XZX GLY A 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 3  
1 8XZX ALA A 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  4  
1 8XZX GLY A 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  5  
1 8XZX ALA A 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  6  
1 8XZX GLY A 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  7  
1 8XZX ALA A 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  8  
1 8XZX GLY A 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  9  
1 8XZX ALA A 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  10 
1 8XZX GLY A 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  11 
1 8XZX MET A 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  12 
1 8XZX GLU A 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   13 
1 8XZX PRO A 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 30  14 
1 8XZX GLN A 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 33  15 
1 8XZX GLN A 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 117 16 
1 8XZX HIS A 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 167 17 
2 8XZX GLY B 1   ? UNP Q0CMZ1 ?   ?   'expression tag'      -12 18 
2 8XZX ALA B 2   ? UNP Q0CMZ1 ?   ?   'expression tag'      -11 19 
2 8XZX GLY B 3   ? UNP Q0CMZ1 ?   ?   'expression tag'      -10 20 
2 8XZX ALA B 4   ? UNP Q0CMZ1 ?   ?   'expression tag'      -9  21 
2 8XZX GLY B 5   ? UNP Q0CMZ1 ?   ?   'expression tag'      -8  22 
2 8XZX ALA B 6   ? UNP Q0CMZ1 ?   ?   'expression tag'      -7  23 
2 8XZX GLY B 7   ? UNP Q0CMZ1 ?   ?   'expression tag'      -6  24 
2 8XZX ALA B 8   ? UNP Q0CMZ1 ?   ?   'expression tag'      -5  25 
2 8XZX GLY B 9   ? UNP Q0CMZ1 ?   ?   'expression tag'      -4  26 
2 8XZX ALA B 10  ? UNP Q0CMZ1 ?   ?   'expression tag'      -3  27 
2 8XZX GLY B 11  ? UNP Q0CMZ1 ?   ?   'expression tag'      -2  28 
2 8XZX MET B 12  ? UNP Q0CMZ1 ?   ?   'expression tag'      -1  29 
2 8XZX GLU B 13  ? UNP Q0CMZ1 ?   ?   'expression tag'      0   30 
2 8XZX PRO B 43  ? UNP Q0CMZ1 ASP 62  'engineered mutation' 30  31 
2 8XZX GLN B 46  ? UNP Q0CMZ1 ALA 65  'engineered mutation' 33  32 
2 8XZX GLN B 130 ? UNP Q0CMZ1 LYS 149 'engineered mutation' 117 33 
2 8XZX HIS B 180 ? UNP Q0CMZ1 ALA 199 'engineered mutation' 167 34 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_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 150 ALA A 160 1 ? 11 
HELX_P HELX_P2 AA2 THR B 163 ? ALA B 173 ? THR B 150 ALA B 160 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 51 A PRO 65 A ? PRO 52 A 1 -0.27 
2 ASN 93 A . ? ASN 80 A PRO 94 A ? PRO 81 A 1 -0.34 
3 ASN 64 B . ? ASN 51 B PRO 65 B ? PRO 52 B 1 -2.14 
4 ASN 93 B . ? ASN 80 B PRO 94 B ? PRO 81 B 1 1.68  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 9 ? 
AA3 ? 9 ? 
AA4 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA2 8 9 ? 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 
# 
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 13  ? ILE A 14  ? GLU A 0   ILE A 1   
AA1 2 GLN A 36  ? ASN A 41  ? GLN A 23  ASN A 28  
AA1 3 GLN A 46  ? SER A 52  ? GLN A 33  SER A 39  
AA1 4 SER A 193 ? VAL A 200 ? SER A 180 VAL A 187 
AA1 5 THR A 70  ? ASN A 80  ? THR A 57  ASN A 67  
AA1 6 GLY A 159 ? THR A 162 ? GLY A 146 THR A 149 
AA2 1 GLU A 18  ? ASN A 22  ? GLU A 5   ASN A 9   
AA2 2 TYR A 25  ? THR A 31  ? TYR A 12  THR A 18  
AA2 3 PHE A 57  ? TRP A 63  ? PHE A 44  TRP A 50  
AA2 4 THR A 179 ? GLY A 189 ? THR A 166 GLY A 176 
AA2 5 SER A 83  ? GLN A 92  ? SER A 70  GLN A 79  
AA2 6 VAL A 96  ? PHE A 104 ? VAL A 83  PHE A 91  
AA2 7 ALA A 143 ? ARG A 152 ? ALA A 130 ARG A 139 
AA2 8 GLY A 124 ? ALA A 136 ? GLY A 111 ALA A 123 
AA2 9 GLN A 114 ? THR A 121 ? GLN A 101 THR A 108 
AA3 1 GLU B 18  ? ASN B 22  ? GLU B 5   ASN B 9   
AA3 2 TYR B 25  ? THR B 31  ? TYR B 12  THR B 18  
AA3 3 PHE B 57  ? TRP B 63  ? PHE B 44  TRP B 50  
AA3 4 THR B 179 ? GLY B 189 ? THR B 166 GLY B 176 
AA3 5 SER B 83  ? GLN B 92  ? SER B 70  GLN B 79  
AA3 6 VAL B 96  ? PHE B 104 ? VAL B 83  PHE B 91  
AA3 7 ALA B 143 ? ARG B 152 ? ALA B 130 ARG B 139 
AA3 8 GLY B 124 ? ALA B 136 ? GLY B 111 ALA B 123 
AA3 9 GLN B 114 ? THR B 121 ? GLN B 101 THR B 108 
AA4 1 GLN B 36  ? ASN B 41  ? GLN B 23  ASN B 28  
AA4 2 GLY B 45  ? SER B 52  ? GLY B 32  SER B 39  
AA4 3 SER B 193 ? GLN B 201 ? SER B 180 GLN B 188 
AA4 4 THR B 70  ? ASN B 80  ? THR B 57  ASN B 67  
AA4 5 GLY B 159 ? THR B 162 ? GLY B 146 THR B 149 
# 
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 ILE A 14  ? N ILE A 1   O TYR A 39  ? O TYR A 26  
AA1 2 3 N THR A 40  ? N THR A 27  O SER A 48  ? O SER A 35  
AA1 3 4 N TRP A 51  ? N TRP A 38  O GLY A 194 ? O GLY A 181 
AA1 4 5 O SER A 197 ? O SER A 184 N GLU A 76  ? N GLU A 63  
AA1 5 6 N ILE A 71  ? N ILE A 58  O VAL A 161 ? O VAL A 148 
AA2 1 2 N GLU A 18  ? N GLU A 5   O PHE A 29  ? O PHE A 16  
AA2 2 3 N TRP A 30  ? N TRP A 17  O VAL A 58  ? O VAL A 45  
AA2 3 4 N ALA A 59  ? N ALA A 46  O THR A 187 ? O THR A 174 
AA2 4 5 O ASN A 181 ? O ASN A 168 N TRP A 90  ? N TRP A 77  
AA2 5 6 N GLY A 89  ? N GLY A 76  O TYR A 98  ? O TYR A 85  
AA2 6 7 N VAL A 101 ? N VAL A 88  O SER A 150 ? O SER A 137 
AA2 7 8 O PHE A 145 ? O PHE A 132 N ARG A 133 ? N ARG A 120 
AA2 8 9 O ILE A 128 ? O ILE A 115 N LEU A 116 ? N LEU A 103 
AA3 1 2 N ASN B 22  ? N ASN B 9   O TYR B 25  ? O TYR B 12  
AA3 2 3 N TRP B 30  ? N TRP B 17  O VAL B 58  ? O VAL B 45  
AA3 3 4 N ALA B 59  ? N ALA B 46  O THR B 187 ? O THR B 174 
AA3 4 5 O ILE B 184 ? O ILE B 171 N TYR B 88  ? N TYR B 75  
AA3 5 6 N LEU B 85  ? N LEU B 72  O SER B 103 ? O SER B 90  
AA3 6 7 N VAL B 101 ? N VAL B 88  O ARG B 152 ? O ARG B 139 
AA3 7 8 O VAL B 151 ? O VAL B 138 N LYS B 127 ? N LYS B 114 
AA3 8 9 O ILE B 128 ? O ILE B 115 N GLY B 117 ? N GLY B 104 
AA4 1 2 N THR B 38  ? N THR B 25  O GLU B 50  ? O GLU B 37  
AA4 2 3 N GLY B 45  ? N GLY B 32  O VAL B 200 ? O VAL B 187 
AA4 3 4 O SER B 195 ? O SER B 182 N ASN B 78  ? N ASN B 65  
AA4 4 5 N ILE B 71  ? N ILE B 58  O VAL B 161 ? O VAL B 148 
# 
_pdbx_entry_details.entry_id                   8XZX 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   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 O   B HOH 234 ? ? O B HOH 243 ? ? 1.86 
2 1 NE2 B GLN 188 ? ? O B HOH 201 ? ? 1.98 
3 1 O   A HOH 238 ? ? O A HOH 286 ? ? 2.00 
# 
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 31  ? ? 60.17   -132.48 
2  1 SER A 54  ? ? -118.83 -150.99 
3  1 ASN A 65  ? ? -111.99 71.41   
4  1 ASN A 80  ? ? 60.36   66.73   
5  1 SER A 92  ? ? -85.58  -87.63  
6  1 ASN A 168 ? ? -85.03  -149.68 
7  1 GLU B 5   ? ? 177.29  129.96  
8  1 ALA B 31  ? ? 56.11   -135.01 
9  1 SER B 54  ? ? -121.27 -155.81 
10 1 SER B 55  ? ? -106.07 50.50   
11 1 ASN B 65  ? ? -111.13 70.24   
12 1 SER B 92  ? ? -92.61  -78.91  
13 1 ALA B 100 ? ? -44.34  157.07  
14 1 ASN B 168 ? ? -87.13  -151.57 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 SER A 41 ? ? GLY A 42 ? ? 147.86  
2 1 GLY A 62 ? ? GLU A 63 ? ? -146.92 
3 1 SER B 73 ? ? VAL B 74 ? ? 149.20  
# 
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 -12 ? A GLY 1  
2  1 Y 1 A ALA -11 ? A ALA 2  
3  1 Y 1 A GLY -10 ? A GLY 3  
4  1 Y 1 A ALA -9  ? A ALA 4  
5  1 Y 1 A GLY -8  ? A GLY 5  
6  1 Y 1 A ALA -7  ? A ALA 6  
7  1 Y 1 A GLY -6  ? A GLY 7  
8  1 Y 1 A ALA -5  ? A ALA 8  
9  1 Y 1 B GLY -12 ? B GLY 1  
10 1 Y 1 B ALA -11 ? B ALA 2  
11 1 Y 1 B GLY -10 ? B GLY 3  
12 1 Y 1 B ALA -9  ? B ALA 4  
13 1 Y 1 B GLY -8  ? B GLY 5  
14 1 Y 1 B ALA -7  ? B ALA 6  
15 1 Y 1 B GLY -6  ? B GLY 7  
16 1 Y 1 B ALA -5  ? B ALA 8  
17 1 Y 1 B GLY -4  ? B GLY 9  
18 1 Y 1 B ALA -3  ? B ALA 10 
19 1 Y 1 B GLY -2  ? B GLY 11 
20 1 Y 1 B MET -1  ? B 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 
# 
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                    8XZX 
_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]   0.023456 
_atom_sites.fract_transf_matrix[1][2]   0.007401 
_atom_sites.fract_transf_matrix[1][3]   0.006804 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020151 
_atom_sites.fract_transf_matrix[2][3]   0.004092 
_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]   0.020009 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 9   ? -21.770 -3.150  -6.780  1.00 43.70 ? -4  GLY A N   1 
ATOM   2    C CA  . GLY A 1 9   ? -20.755 -3.016  -5.720  1.00 46.92 ? -4  GLY A CA  1 
ATOM   3    C C   . GLY A 1 9   ? -21.356 -2.471  -4.433  1.00 47.23 ? -4  GLY A C   1 
ATOM   4    O O   . GLY A 1 9   ? -21.552 -3.277  -3.500  1.00 47.38 ? -4  GLY A O   1 
ATOM   5    N N   . ALA A 1 10  ? -21.646 -1.163  -4.375  1.00 45.05 ? -3  ALA A N   1 
ATOM   6    C CA  . ALA A 1 10  ? -21.917 -0.423  -3.116  1.00 44.93 ? -3  ALA A CA  1 
ATOM   7    C C   . ALA A 1 10  ? -22.835 -1.259  -2.215  1.00 43.07 ? -3  ALA A C   1 
ATOM   8    O O   . ALA A 1 10  ? -23.994 -1.483  -2.604  1.00 49.52 ? -3  ALA A O   1 
ATOM   9    C CB  . ALA A 1 10  ? -22.500 0.939   -3.407  1.00 44.73 ? -3  ALA A CB  1 
ATOM   10   N N   . GLY A 1 11  ? -22.303 -1.753  -1.093  1.00 39.67 ? -2  GLY A N   1 
ATOM   11   C CA  . GLY A 1 11  ? -23.051 -2.462  -0.033  1.00 39.64 ? -2  GLY A CA  1 
ATOM   12   C C   . GLY A 1 11  ? -22.948 -3.987  -0.117  1.00 39.72 ? -2  GLY A C   1 
ATOM   13   O O   . GLY A 1 11  ? -23.331 -4.657  0.863   1.00 37.31 ? -2  GLY A O   1 
ATOM   14   N N   . MET A 1 12  ? -22.479 -4.547  -1.237  1.00 37.74 ? -1  MET A N   1 
ATOM   15   C CA  . MET A 1 12  ? -22.413 -6.020  -1.440  1.00 38.74 ? -1  MET A CA  1 
ATOM   16   C C   . MET A 1 12  ? -21.193 -6.578  -0.689  1.00 36.54 ? -1  MET A C   1 
ATOM   17   O O   . MET A 1 12  ? -20.073 -6.114  -0.973  1.00 29.79 ? -1  MET A O   1 
ATOM   18   C CB  . MET A 1 12  ? -22.297 -6.379  -2.925  1.00 42.81 ? -1  MET A CB  1 
ATOM   19   C CG  . MET A 1 12  ? -23.615 -6.411  -3.677  1.00 45.69 ? -1  MET A CG  1 
ATOM   20   S SD  . MET A 1 12  ? -23.365 -6.663  -5.467  1.00 53.83 ? -1  MET A SD  1 
ATOM   21   C CE  . MET A 1 12  ? -22.183 -8.011  -5.465  1.00 50.53 ? -1  MET A CE  1 
ATOM   22   N N   . GLU A 1 13  ? -21.409 -7.539  0.222   1.00 36.62 ? 0   GLU A N   1 
ATOM   23   C CA  . GLU A 1 13  ? -20.334 -8.262  0.960   1.00 39.97 ? 0   GLU A CA  1 
ATOM   24   C C   . GLU A 1 13  ? -19.615 -9.232  0.015   1.00 37.51 ? 0   GLU A C   1 
ATOM   25   O O   . GLU A 1 13  ? -20.299 -9.924  -0.736  1.00 37.75 ? 0   GLU A O   1 
ATOM   26   C CB  . GLU A 1 13  ? -20.912 -9.033  2.142   1.00 41.23 ? 0   GLU A CB  1 
ATOM   27   C CG  . GLU A 1 13  ? -21.326 -8.131  3.284   1.00 45.27 ? 0   GLU A CG  1 
ATOM   28   C CD  . GLU A 1 13  ? -21.959 -8.894  4.429   1.00 49.20 ? 0   GLU A CD  1 
ATOM   29   O OE1 . GLU A 1 13  ? -23.183 -9.131  4.367   1.00 56.13 ? 0   GLU A OE1 1 
ATOM   30   O OE2 . GLU A 1 13  ? -21.223 -9.283  5.359   1.00 53.85 ? 0   GLU A OE2 1 
ATOM   31   N N   . ILE A 1 14  ? -18.283 -9.261  0.021   1.00 36.60 ? 1   ILE A N   1 
ATOM   32   C CA  . ILE A 1 14  ? -17.507 -10.245 -0.791  1.00 36.84 ? 1   ILE A CA  1 
ATOM   33   C C   . ILE A 1 14  ? -16.465 -10.908 0.115   1.00 35.09 ? 1   ILE A C   1 
ATOM   34   O O   . ILE A 1 14  ? -15.964 -10.225 1.030   1.00 34.14 ? 1   ILE A O   1 
ATOM   35   C CB  . ILE A 1 14  ? -16.893 -9.601  -2.052  1.00 37.85 ? 1   ILE A CB  1 
ATOM   36   C CG1 . ILE A 1 14  ? -15.740 -8.660  -1.718  1.00 38.30 ? 1   ILE A CG1 1 
ATOM   37   C CG2 . ILE A 1 14  ? -17.950 -8.894  -2.893  1.00 38.23 ? 1   ILE A CG2 1 
ATOM   38   C CD1 . ILE A 1 14  ? -14.721 -8.571  -2.816  1.00 38.38 ? 1   ILE A CD1 1 
ATOM   39   N N   . THR A 1 15  ? -16.182 -12.195 -0.130  1.00 33.38 ? 2   THR A N   1 
ATOM   40   C CA  . THR A 1 15  ? -15.387 -13.088 0.758   1.00 31.92 ? 2   THR A CA  1 
ATOM   41   C C   . THR A 1 15  ? -14.250 -13.778 -0.004  1.00 31.03 ? 2   THR A C   1 
ATOM   42   O O   . THR A 1 15  ? -13.447 -14.478 0.670   1.00 28.11 ? 2   THR A O   1 
ATOM   43   C CB  . THR A 1 15  ? -16.295 -14.132 1.411   1.00 31.74 ? 2   THR A CB  1 
ATOM   44   O OG1 . THR A 1 15  ? -16.944 -14.811 0.338   1.00 33.11 ? 2   THR A OG1 1 
ATOM   45   C CG2 . THR A 1 15  ? -17.318 -13.519 2.342   1.00 31.03 ? 2   THR A CG2 1 
ATOM   46   N N   . SER A 1 16  ? -14.150 -13.582 -1.328  1.00 29.44 ? 3   SER A N   1 
ATOM   47   C CA  . SER A 1 16  ? -12.977 -14.042 -2.116  1.00 28.30 ? 3   SER A CA  1 
ATOM   48   C C   . SER A 1 16  ? -12.452 -12.932 -3.027  1.00 26.73 ? 3   SER A C   1 
ATOM   49   O O   . SER A 1 16  ? -13.136 -11.917 -3.240  1.00 27.15 ? 3   SER A O   1 
ATOM   50   C CB  . SER A 1 16  ? -13.271 -15.302 -2.881  1.00 29.59 ? 3   SER A CB  1 
ATOM   51   O OG  . SER A 1 16  ? -14.566 -15.259 -3.422  1.00 29.89 ? 3   SER A OG  1 
ATOM   52   N N   . SER A 1 17  ? -11.233 -13.133 -3.510  1.00 25.63 ? 4   SER A N   1 
ATOM   53   C CA  . SER A 1 17  ? -10.419 -12.110 -4.200  1.00 25.16 ? 4   SER A CA  1 
ATOM   54   C C   . SER A 1 17  ? -11.227 -11.527 -5.358  1.00 25.50 ? 4   SER A C   1 
ATOM   55   O O   . SER A 1 17  ? -11.875 -12.306 -6.087  1.00 26.30 ? 4   SER A O   1 
ATOM   56   C CB  . SER A 1 17  ? -9.108  -12.705 -4.637  1.00 23.82 ? 4   SER A CB  1 
ATOM   57   O OG  . SER A 1 17  ? -8.436  -13.267 -3.512  1.00 21.64 ? 4   SER A OG  1 
ATOM   58   N N   . GLU A 1 18  ? -11.249 -10.204 -5.484  1.00 24.58 ? 5   GLU A N   1 
ATOM   59   C CA  . GLU A 1 18  ? -11.664 -9.555  -6.744  1.00 24.77 ? 5   GLU A CA  1 
ATOM   60   C C   . GLU A 1 18  ? -11.121 -8.132  -6.785  1.00 24.81 ? 5   GLU A C   1 
ATOM   61   O O   . GLU A 1 18  ? -10.783 -7.573  -5.729  1.00 25.21 ? 5   GLU A O   1 
ATOM   62   C CB  . GLU A 1 18  ? -13.177 -9.589  -6.952  1.00 25.93 ? 5   GLU A CB  1 
ATOM   63   C CG  . GLU A 1 18  ? -13.991 -9.083  -5.789  1.00 27.15 ? 5   GLU A CG  1 
ATOM   64   C CD  . GLU A 1 18  ? -15.492 -8.934  -6.049  1.00 27.91 ? 5   GLU A CD  1 
ATOM   65   O OE1 . GLU A 1 18  ? -15.886 -7.831  -6.448  1.00 28.06 ? 5   GLU A OE1 1 
ATOM   66   O OE2 . GLU A 1 18  ? -16.271 -9.903  -5.823  1.00 25.32 ? 5   GLU A OE2 1 
ATOM   67   N N   . THR A 1 19  ? -10.985 -7.635  -8.009  1.00 22.67 ? 6   THR A N   1 
ATOM   68   C CA  . THR A 1 19  ? -10.676 -6.243  -8.367  1.00 22.04 ? 6   THR A CA  1 
ATOM   69   C C   . THR A 1 19  ? -11.823 -5.748  -9.251  1.00 22.66 ? 6   THR A C   1 
ATOM   70   O O   . THR A 1 19  ? -12.461 -6.567  -9.920  1.00 24.76 ? 6   THR A O   1 
ATOM   71   C CB  . THR A 1 19  ? -9.325  -6.171  -9.085  1.00 20.91 ? 6   THR A CB  1 
ATOM   72   O OG1 . THR A 1 19  ? -9.536  -6.642  -10.411 1.00 19.78 ? 6   THR A OG1 1 
ATOM   73   C CG2 . THR A 1 19  ? -8.261  -7.009  -8.423  1.00 21.17 ? 6   THR A CG2 1 
ATOM   74   N N   . GLY A 1 20  ? -12.069 -4.448  -9.245  1.00 23.61 ? 7   GLY A N   1 
ATOM   75   C CA  . GLY A 1 20  ? -13.067 -3.796  -10.107 1.00 22.39 ? 7   GLY A CA  1 
ATOM   76   C C   . GLY A 1 20  ? -13.018 -2.300  -9.882  1.00 22.44 ? 7   GLY A C   1 
ATOM   77   O O   . GLY A 1 20  ? -11.998 -1.797  -9.330  1.00 21.98 ? 7   GLY A O   1 
ATOM   78   N N   . THR A 1 21  ? -14.088 -1.614  -10.257 1.00 20.85 ? 8   THR A N   1 
ATOM   79   C CA  . THR A 1 21  ? -14.285 -0.182  -9.967  1.00 20.93 ? 8   THR A CA  1 
ATOM   80   C C   . THR A 1 21  ? -15.602 -0.033  -9.209  1.00 20.26 ? 8   THR A C   1 
ATOM   81   O O   . THR A 1 21  ? -16.525 -0.786  -9.472  1.00 21.07 ? 8   THR A O   1 
ATOM   82   C CB  . THR A 1 21  ? -14.212 0.645   -11.247 1.00 21.15 ? 8   THR A CB  1 
ATOM   83   O OG1 . THR A 1 21  ? -15.421 0.390   -11.966 1.00 22.30 ? 8   THR A OG1 1 
ATOM   84   C CG2 . THR A 1 21  ? -12.989 0.301   -12.068 1.00 20.83 ? 8   THR A CG2 1 
ATOM   85   N N   . ASN A 1 22  ? -15.649 0.908   -8.280  1.00 20.32 ? 9   ASN A N   1 
ATOM   86   C CA  . ASN A 1 22  ? -16.823 1.179   -7.426  1.00 20.58 ? 9   ASN A CA  1 
ATOM   87   C C   . ASN A 1 22  ? -16.818 2.674   -7.116  1.00 21.14 ? 9   ASN A C   1 
ATOM   88   O O   . ASN A 1 22  ? -15.845 3.127   -6.472  1.00 20.29 ? 9   ASN A O   1 
ATOM   89   C CB  . ASN A 1 22  ? -16.817 0.324   -6.156  1.00 19.33 ? 9   ASN A CB  1 
ATOM   90   C CG  . ASN A 1 22  ? -17.957 0.698   -5.244  1.00 18.88 ? 9   ASN A CG  1 
ATOM   91   O OD1 . ASN A 1 22  ? -17.797 1.533   -4.360  1.00 18.21 ? 9   ASN A OD1 1 
ATOM   92   N ND2 . ASN A 1 22  ? -19.132 0.151   -5.505  1.00 19.33 ? 9   ASN A ND2 1 
ATOM   93   N N   . ASN A 1 23  ? -17.849 3.390   -7.581  1.00 22.11 ? 10  ASN A N   1 
ATOM   94   C CA  . ASN A 1 23  ? -18.111 4.809   -7.234  1.00 23.34 ? 10  ASN A CA  1 
ATOM   95   C C   . ASN A 1 23  ? -16.916 5.667   -7.676  1.00 23.49 ? 10  ASN A C   1 
ATOM   96   O O   . ASN A 1 23  ? -16.585 6.654   -6.981  1.00 24.15 ? 10  ASN A O   1 
ATOM   97   C CB  . ASN A 1 23  ? -18.454 4.932   -5.743  1.00 25.87 ? 10  ASN A CB  1 
ATOM   98   C CG  . ASN A 1 23  ? -19.804 4.324   -5.396  1.00 26.99 ? 10  ASN A CG  1 
ATOM   99   O OD1 . ASN A 1 23  ? -20.751 4.451   -6.164  1.00 28.85 ? 10  ASN A OD1 1 
ATOM   100  N ND2 . ASN A 1 23  ? -19.923 3.695   -4.237  1.00 26.36 ? 10  ASN A ND2 1 
ATOM   101  N N   . GLY A 1 24  ? -16.298 5.320   -8.806  1.00 23.13 ? 11  GLY A N   1 
ATOM   102  C CA  . GLY A 1 24  ? -15.232 6.136   -9.426  1.00 23.17 ? 11  GLY A CA  1 
ATOM   103  C C   . GLY A 1 24  ? -13.846 5.712   -8.961  1.00 23.60 ? 11  GLY A C   1 
ATOM   104  O O   . GLY A 1 24  ? -12.853 6.304   -9.437  1.00 21.23 ? 11  GLY A O   1 
ATOM   105  N N   . TYR A 1 25  ? -13.774 4.710   -8.076  1.00 21.76 ? 12  TYR A N   1 
ATOM   106  C CA  . TYR A 1 25  ? -12.509 4.258   -7.467  1.00 21.84 ? 12  TYR A CA  1 
ATOM   107  C C   . TYR A 1 25  ? -12.225 2.849   -7.958  1.00 21.41 ? 12  TYR A C   1 
ATOM   108  O O   . TYR A 1 25  ? -13.160 2.105   -8.170  1.00 22.29 ? 12  TYR A O   1 
ATOM   109  C CB  . TYR A 1 25  ? -12.585 4.358   -5.945  1.00 22.82 ? 12  TYR A CB  1 
ATOM   110  C CG  . TYR A 1 25  ? -12.492 5.770   -5.425  1.00 22.72 ? 12  TYR A CG  1 
ATOM   111  C CD1 . TYR A 1 25  ? -13.627 6.554   -5.281  1.00 21.82 ? 12  TYR A CD1 1 
ATOM   112  C CD2 . TYR A 1 25  ? -11.268 6.321   -5.075  1.00 23.14 ? 12  TYR A CD2 1 
ATOM   113  C CE1 . TYR A 1 25  ? -13.551 7.855   -4.815  1.00 22.22 ? 12  TYR A CE1 1 
ATOM   114  C CE2 . TYR A 1 25  ? -11.176 7.622   -4.599  1.00 23.60 ? 12  TYR A CE2 1 
ATOM   115  C CZ  . TYR A 1 25  ? -12.322 8.390   -4.477  1.00 22.69 ? 12  TYR A CZ  1 
ATOM   116  O OH  . TYR A 1 25  ? -12.245 9.655   -3.990  1.00 25.01 ? 12  TYR A OH  1 
ATOM   117  N N   . TYR A 1 26  ? -10.960 2.542   -8.197  1.00 20.55 ? 13  TYR A N   1 
ATOM   118  C CA  . TYR A 1 26  ? -10.473 1.153   -8.328  1.00 21.08 ? 13  TYR A CA  1 
ATOM   119  C C   . TYR A 1 26  ? -10.438 0.573   -6.923  1.00 20.52 ? 13  TYR A C   1 
ATOM   120  O O   . TYR A 1 26  ? -10.183 1.350   -5.971  1.00 20.58 ? 13  TYR A O   1 
ATOM   121  C CB  . TYR A 1 26  ? -9.100  1.110   -8.990  1.00 21.87 ? 13  TYR A CB  1 
ATOM   122  C CG  . TYR A 1 26  ? -8.466  -0.252  -9.013  1.00 22.61 ? 13  TYR A CG  1 
ATOM   123  C CD1 . TYR A 1 26  ? -8.790  -1.178  -9.992  1.00 22.76 ? 13  TYR A CD1 1 
ATOM   124  C CD2 . TYR A 1 26  ? -7.527  -0.603  -8.051  1.00 24.27 ? 13  TYR A CD2 1 
ATOM   125  C CE1 . TYR A 1 26  ? -8.177  -2.420  -10.024 1.00 23.82 ? 13  TYR A CE1 1 
ATOM   126  C CE2 . TYR A 1 26  ? -6.929  -1.849  -8.053  1.00 24.12 ? 13  TYR A CE2 1 
ATOM   127  C CZ  . TYR A 1 26  ? -7.247  -2.749  -9.049  1.00 24.43 ? 13  TYR A CZ  1 
ATOM   128  O OH  . TYR A 1 26  ? -6.653  -3.972  -9.027  1.00 29.04 ? 13  TYR A OH  1 
ATOM   129  N N   . TYR A 1 27  ? -10.743 -0.717  -6.796  1.00 20.45 ? 14  TYR A N   1 
ATOM   130  C CA  . TYR A 1 27  ? -10.728 -1.448  -5.503  1.00 20.50 ? 14  TYR A CA  1 
ATOM   131  C C   . TYR A 1 27  ? -10.074 -2.809  -5.749  1.00 20.73 ? 14  TYR A C   1 
ATOM   132  O O   . TYR A 1 27  ? -10.294 -3.400  -6.792  1.00 22.02 ? 14  TYR A O   1 
ATOM   133  C CB  . TYR A 1 27  ? -12.126 -1.517  -4.893  1.00 20.80 ? 14  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 27  ? -13.018 -2.568  -5.497  1.00 23.13 ? 14  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 27  ? -12.903 -3.905  -5.137  1.00 23.82 ? 14  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 27  ? -13.977 -2.229  -6.440  1.00 23.46 ? 14  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 27  ? -13.717 -4.872  -5.708  1.00 24.31 ? 14  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 27  ? -14.793 -3.183  -7.022  1.00 23.64 ? 14  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 27  ? -14.656 -4.507  -6.658  1.00 24.49 ? 14  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 27  ? -15.447 -5.443  -7.245  1.00 27.05 ? 14  TYR A OH  1 
ATOM   141  N N   . SER A 1 28  ? -9.221  -3.245  -4.836  1.00 20.79 ? 15  SER A N   1 
ATOM   142  C CA  . SER A 1 28  ? -8.583  -4.580  -4.880  1.00 21.58 ? 15  SER A CA  1 
ATOM   143  C C   . SER A 1 28  ? -8.812  -5.263  -3.531  1.00 19.71 ? 15  SER A C   1 
ATOM   144  O O   . SER A 1 28  ? -8.416  -4.712  -2.525  1.00 19.89 ? 15  SER A O   1 
ATOM   145  C CB  . SER A 1 28  ? -7.116  -4.486  -5.227  1.00 22.25 ? 15  SER A CB  1 
ATOM   146  O OG  . SER A 1 28  ? -6.585  -5.797  -5.400  1.00 25.41 ? 15  SER A OG  1 
ATOM   147  N N   . PHE A 1 29  ? -9.520  -6.380  -3.526  1.00 19.79 ? 16  PHE A N   1 
ATOM   148  C CA  . PHE A 1 29  ? -9.637  -7.286  -2.361  1.00 19.91 ? 16  PHE A CA  1 
ATOM   149  C C   . PHE A 1 29  ? -8.961  -8.605  -2.737  1.00 19.58 ? 16  PHE A C   1 
ATOM   150  O O   . PHE A 1 29  ? -9.360  -9.232  -3.713  1.00 18.92 ? 16  PHE A O   1 
ATOM   151  C CB  . PHE A 1 29  ? -11.096 -7.467  -1.942  1.00 18.96 ? 16  PHE A CB  1 
ATOM   152  C CG  . PHE A 1 29  ? -11.257 -8.474  -0.838  1.00 19.21 ? 16  PHE A CG  1 
ATOM   153  C CD1 . PHE A 1 29  ? -10.734 -8.226  0.418   1.00 19.47 ? 16  PHE A CD1 1 
ATOM   154  C CD2 . PHE A 1 29  ? -11.899 -9.678  -1.055  1.00 19.83 ? 16  PHE A CD2 1 
ATOM   155  C CE1 . PHE A 1 29  ? -10.833 -9.169  1.427   1.00 19.82 ? 16  PHE A CE1 1 
ATOM   156  C CE2 . PHE A 1 29  ? -12.025 -10.612 -0.036  1.00 20.54 ? 16  PHE A CE2 1 
ATOM   157  C CZ  . PHE A 1 29  ? -11.471 -10.363 1.200   1.00 20.15 ? 16  PHE A CZ  1 
ATOM   158  N N   . TRP A 1 30  ? -7.918  -8.963  -1.999  1.00 21.05 ? 17  TRP A N   1 
ATOM   159  C CA  . TRP A 1 30  ? -7.193  -10.249 -2.139  1.00 22.61 ? 17  TRP A CA  1 
ATOM   160  C C   . TRP A 1 30  ? -7.070  -10.913 -0.767  1.00 21.29 ? 17  TRP A C   1 
ATOM   161  O O   . TRP A 1 30  ? -6.739  -10.224 0.206   1.00 20.11 ? 17  TRP A O   1 
ATOM   162  C CB  . TRP A 1 30  ? -5.819  -10.053 -2.785  1.00 24.57 ? 17  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 30  ? -5.037  -11.328 -2.873  1.00 27.27 ? 17  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 30  ? -5.108  -12.257 -3.867  1.00 28.55 ? 17  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 30  ? -4.087  -11.832 -1.916  1.00 30.40 ? 17  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 30  ? -4.248  -13.289 -3.614  1.00 30.40 ? 17  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 30  ? -3.618  -13.068 -2.415  1.00 31.78 ? 17  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 30  ? -3.585  -11.369 -0.692  1.00 30.75 ? 17  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 30  ? -2.659  -13.831 -1.741  1.00 31.05 ? 17  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 30  ? -2.649  -12.132 -0.023  1.00 33.19 ? 17  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 30  ? -2.185  -13.342 -0.546  1.00 30.92 ? 17  TRP A CH2 1 
ATOM   172  N N   . THR A 1 31  ? -7.351  -12.209 -0.715  1.00 22.44 ? 18  THR A N   1 
ATOM   173  C CA  . THR A 1 31  ? -7.209  -13.072 0.485   1.00 23.73 ? 18  THR A CA  1 
ATOM   174  C C   . THR A 1 31  ? -6.724  -14.438 -0.010  1.00 24.13 ? 18  THR A C   1 
ATOM   175  O O   . THR A 1 31  ? -7.233  -14.885 -1.048  1.00 24.22 ? 18  THR A O   1 
ATOM   176  C CB  . THR A 1 31  ? -8.535  -13.159 1.249   1.00 24.34 ? 18  THR A CB  1 
ATOM   177  O OG1 . THR A 1 31  ? -8.462  -14.107 2.312   1.00 25.67 ? 18  THR A OG1 1 
ATOM   178  C CG2 . THR A 1 31  ? -9.677  -13.586 0.356   1.00 26.32 ? 18  THR A CG2 1 
ATOM   179  N N   . ASP A 1 32  ? -5.771  -15.054 0.689   1.00 23.78 ? 19  ASP A N   1 
ATOM   180  C CA  . ASP A 1 32  ? -5.330  -16.446 0.429   1.00 24.66 ? 19  ASP A CA  1 
ATOM   181  C C   . ASP A 1 32  ? -6.399  -17.435 0.909   1.00 24.47 ? 19  ASP A C   1 
ATOM   182  O O   . ASP A 1 32  ? -6.147  -18.631 0.794   1.00 27.40 ? 19  ASP A O   1 
ATOM   183  C CB  . ASP A 1 32  ? -3.985  -16.733 1.101   1.00 26.39 ? 19  ASP A CB  1 
ATOM   184  C CG  . ASP A 1 32  ? -3.982  -16.557 2.612   1.00 27.43 ? 19  ASP A CG  1 
ATOM   185  O OD1 . ASP A 1 32  ? -5.078  -16.648 3.229   1.00 26.88 ? 19  ASP A OD1 1 
ATOM   186  O OD2 . ASP A 1 32  ? -2.879  -16.339 3.164   1.00 28.48 ? 19  ASP A OD2 1 
ATOM   187  N N   . GLY A 1 33  ? -7.515  -16.967 1.476   1.00 24.55 ? 20  GLY A N   1 
ATOM   188  C CA  . GLY A 1 33  ? -8.656  -17.810 1.878   1.00 24.04 ? 20  GLY A CA  1 
ATOM   189  C C   . GLY A 1 33  ? -8.582  -18.276 3.330   1.00 24.29 ? 20  GLY A C   1 
ATOM   190  O O   . GLY A 1 33  ? -9.550  -18.917 3.782   1.00 24.97 ? 20  GLY A O   1 
ATOM   191  N N   . GLY A 1 34  ? -7.511  -17.952 4.063   1.00 23.16 ? 21  GLY A N   1 
ATOM   192  C CA  . GLY A 1 34  ? -7.383  -18.312 5.489   1.00 23.64 ? 21  GLY A CA  1 
ATOM   193  C C   . GLY A 1 34  ? -8.405  -17.588 6.359   1.00 23.51 ? 21  GLY A C   1 
ATOM   194  O O   . GLY A 1 34  ? -8.658  -16.377 6.115   1.00 22.55 ? 21  GLY A O   1 
ATOM   195  N N   . GLY A 1 35  ? -8.988  -18.297 7.330   1.00 24.01 ? 22  GLY A N   1 
ATOM   196  C CA  . GLY A 1 35  ? -10.051 -17.775 8.218   1.00 25.90 ? 22  GLY A CA  1 
ATOM   197  C C   . GLY A 1 35  ? -11.162 -17.092 7.439   1.00 27.80 ? 22  GLY A C   1 
ATOM   198  O O   . GLY A 1 35  ? -11.430 -17.512 6.291   1.00 28.59 ? 22  GLY A O   1 
ATOM   199  N N   . GLN A 1 36  ? -11.802 -16.080 8.028   1.00 30.03 ? 23  GLN A N   1 
ATOM   200  C CA  . GLN A 1 36  ? -12.891 -15.320 7.362   1.00 33.03 ? 23  GLN A CA  1 
ATOM   201  C C   . GLN A 1 36  ? -12.428 -13.875 7.150   1.00 29.89 ? 23  GLN A C   1 
ATOM   202  O O   . GLN A 1 36  ? -11.910 -13.251 8.099   1.00 28.26 ? 23  GLN A O   1 
ATOM   203  C CB  . GLN A 1 36  ? -14.197 -15.423 8.159   1.00 39.14 ? 23  GLN A CB  1 
ATOM   204  C CG  . GLN A 1 36  ? -15.323 -16.163 7.427   1.00 47.05 ? 23  GLN A CG  1 
ATOM   205  C CD  . GLN A 1 36  ? -16.004 -15.360 6.336   1.00 50.68 ? 23  GLN A CD  1 
ATOM   206  O OE1 . GLN A 1 36  ? -16.837 -15.867 5.583   1.00 52.13 ? 23  GLN A OE1 1 
ATOM   207  N NE2 . GLN A 1 36  ? -15.656 -14.087 6.233   1.00 54.75 ? 23  GLN A NE2 1 
ATOM   208  N N   . VAL A 1 37  ? -12.584 -13.392 5.920   1.00 27.78 ? 24  VAL A N   1 
ATOM   209  C CA  . VAL A 1 37  ? -12.368 -11.975 5.526   1.00 26.26 ? 24  VAL A CA  1 
ATOM   210  C C   . VAL A 1 37  ? -13.532 -11.567 4.625   1.00 26.12 ? 24  VAL A C   1 
ATOM   211  O O   . VAL A 1 37  ? -13.779 -12.261 3.620   1.00 26.33 ? 24  VAL A O   1 
ATOM   212  C CB  . VAL A 1 37  ? -10.999 -11.770 4.856   1.00 25.66 ? 24  VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 37  ? -10.725 -10.306 4.550   1.00 24.92 ? 24  VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 37  ? -9.887  -12.331 5.725   1.00 26.49 ? 24  VAL A CG2 1 
ATOM   215  N N   . THR A 1 38  ? -14.231 -10.499 5.024   1.00 24.91 ? 25  THR A N   1 
ATOM   216  C CA  . THR A 1 38  ? -15.416 -9.924  4.347   1.00 24.38 ? 25  THR A CA  1 
ATOM   217  C C   . THR A 1 38  ? -15.119 -8.469  3.995   1.00 22.99 ? 25  THR A C   1 
ATOM   218  O O   . THR A 1 38  ? -14.833 -7.684  4.904   1.00 22.71 ? 25  THR A O   1 
ATOM   219  C CB  . THR A 1 38  ? -16.656 -10.012 5.239   1.00 24.50 ? 25  THR A CB  1 
ATOM   220  O OG1 . THR A 1 38  ? -16.871 -11.406 5.431   1.00 24.89 ? 25  THR A OG1 1 
ATOM   221  C CG2 . THR A 1 38  ? -17.873 -9.365  4.623   1.00 24.48 ? 25  THR A CG2 1 
ATOM   222  N N   . TYR A 1 39  ? -15.193 -8.148  2.711   1.00 22.39 ? 26  TYR A N   1 
ATOM   223  C CA  . TYR A 1 39  ? -14.930 -6.803  2.161   1.00 22.20 ? 26  TYR A CA  1 
ATOM   224  C C   . TYR A 1 39  ? -16.259 -6.231  1.662   1.00 21.65 ? 26  TYR A C   1 
ATOM   225  O O   . TYR A 1 39  ? -17.101 -6.976  1.138   1.00 21.48 ? 26  TYR A O   1 
ATOM   226  C CB  . TYR A 1 39  ? -13.843 -6.905  1.090   1.00 22.08 ? 26  TYR A CB  1 
ATOM   227  C CG  . TYR A 1 39  ? -13.582 -5.627  0.341   1.00 22.86 ? 26  TYR A CG  1 
ATOM   228  C CD1 . TYR A 1 39  ? -14.327 -5.298  -0.776  1.00 23.46 ? 26  TYR A CD1 1 
ATOM   229  C CD2 . TYR A 1 39  ? -12.604 -4.741  0.743   1.00 22.60 ? 26  TYR A CD2 1 
ATOM   230  C CE1 . TYR A 1 39  ? -14.111 -4.119  -1.467  1.00 22.60 ? 26  TYR A CE1 1 
ATOM   231  C CE2 . TYR A 1 39  ? -12.363 -3.570  0.044   1.00 22.32 ? 26  TYR A CE2 1 
ATOM   232  C CZ  . TYR A 1 39  ? -13.117 -3.256  -1.068  1.00 21.42 ? 26  TYR A CZ  1 
ATOM   233  O OH  . TYR A 1 39  ? -12.909 -2.109  -1.782  1.00 20.82 ? 26  TYR A OH  1 
ATOM   234  N N   . THR A 1 40  ? -16.443 -4.928  1.849   1.00 21.85 ? 27  THR A N   1 
ATOM   235  C CA  . THR A 1 40  ? -17.612 -4.169  1.337   1.00 22.20 ? 27  THR A CA  1 
ATOM   236  C C   . THR A 1 40  ? -17.140 -2.847  0.719   1.00 21.82 ? 27  THR A C   1 
ATOM   237  O O   . THR A 1 40  ? -16.364 -2.125  1.368   1.00 21.86 ? 27  THR A O   1 
ATOM   238  C CB  . THR A 1 40  ? -18.615 -3.925  2.470   1.00 21.47 ? 27  THR A CB  1 
ATOM   239  O OG1 . THR A 1 40  ? -18.976 -5.211  2.970   1.00 20.57 ? 27  THR A OG1 1 
ATOM   240  C CG2 . THR A 1 40  ? -19.835 -3.164  2.011   1.00 22.57 ? 27  THR A CG2 1 
ATOM   241  N N   . ASN A 1 41  ? -17.620 -2.524  -0.476  1.00 21.53 ? 28  ASN A N   1 
ATOM   242  C CA  . ASN A 1 41  ? -17.550 -1.146  -1.025  1.00 20.50 ? 28  ASN A CA  1 
ATOM   243  C C   . ASN A 1 41  ? -18.639 -0.286  -0.379  1.00 21.89 ? 28  ASN A C   1 
ATOM   244  O O   . ASN A 1 41  ? -19.767 -0.773  -0.186  1.00 22.86 ? 28  ASN A O   1 
ATOM   245  C CB  . ASN A 1 41  ? -17.674 -1.165  -2.536  1.00 20.17 ? 28  ASN A CB  1 
ATOM   246  C CG  . ASN A 1 41  ? -16.432 -1.736  -3.165  1.00 19.72 ? 28  ASN A CG  1 
ATOM   247  O OD1 . ASN A 1 41  ? -15.350 -1.214  -2.934  1.00 21.57 ? 28  ASN A OD1 1 
ATOM   248  N ND2 . ASN A 1 41  ? -16.565 -2.809  -3.922  1.00 19.10 ? 28  ASN A ND2 1 
ATOM   249  N N   . GLY A 1 42  ? -18.294 0.942   -0.018  1.00 21.80 ? 29  GLY A N   1 
ATOM   250  C CA  . GLY A 1 42  ? -19.255 1.950   0.445   1.00 20.95 ? 29  GLY A CA  1 
ATOM   251  C C   . GLY A 1 42  ? -19.370 3.058   -0.590  1.00 20.42 ? 29  GLY A C   1 
ATOM   252  O O   . GLY A 1 42  ? -18.869 2.926   -1.696  1.00 18.45 ? 29  GLY A O   1 
ATOM   253  N N   . PRO A 1 43  ? -20.004 4.192   -0.247  1.00 20.20 ? 30  PRO A N   1 
ATOM   254  C CA  . PRO A 1 43  ? -20.133 5.295   -1.182  1.00 20.75 ? 30  PRO A CA  1 
ATOM   255  C C   . PRO A 1 43  ? -18.748 5.904   -1.429  1.00 21.14 ? 30  PRO A C   1 
ATOM   256  O O   . PRO A 1 43  ? -17.935 5.903   -0.501  1.00 19.69 ? 30  PRO A O   1 
ATOM   257  C CB  . PRO A 1 43  ? -21.039 6.313   -0.465  1.00 21.84 ? 30  PRO A CB  1 
ATOM   258  C CG  . PRO A 1 43  ? -21.592 5.565   0.752   1.00 22.02 ? 30  PRO A CG  1 
ATOM   259  C CD  . PRO A 1 43  ? -20.563 4.502   1.075   1.00 21.70 ? 30  PRO A CD  1 
ATOM   260  N N   . ALA A 1 44  ? -18.530 6.447   -2.630  1.00 19.56 ? 31  ALA A N   1 
ATOM   261  C CA  . ALA A 1 44  ? -17.354 7.283   -2.936  1.00 19.15 ? 31  ALA A CA  1 
ATOM   262  C C   . ALA A 1 44  ? -16.086 6.439   -2.705  1.00 19.08 ? 31  ALA A C   1 
ATOM   263  O O   . ALA A 1 44  ? -16.057 5.275   -3.185  1.00 18.68 ? 31  ALA A O   1 
ATOM   264  C CB  . ALA A 1 44  ? -17.430 8.537   -2.096  1.00 18.51 ? 31  ALA A CB  1 
ATOM   265  N N   . GLY A 1 45  ? -15.083 6.963   -2.001  1.00 18.50 ? 32  GLY A N   1 
ATOM   266  C CA  . GLY A 1 45  ? -13.804 6.264   -1.812  1.00 19.70 ? 32  GLY A CA  1 
ATOM   267  C C   . GLY A 1 45  ? -13.786 5.408   -0.560  1.00 20.33 ? 32  GLY A C   1 
ATOM   268  O O   . GLY A 1 45  ? -12.656 5.080   -0.087  1.00 18.03 ? 32  GLY A O   1 
ATOM   269  N N   . GLN A 1 46  ? -14.967 5.025   -0.043  1.00 21.29 ? 33  GLN A N   1 
ATOM   270  C CA  . GLN A 1 46  ? -15.065 4.299   1.251   1.00 22.21 ? 33  GLN A CA  1 
ATOM   271  C C   . GLN A 1 46  ? -15.082 2.776   1.044   1.00 19.71 ? 33  GLN A C   1 
ATOM   272  O O   . GLN A 1 46  ? -15.799 2.288   0.156   1.00 18.85 ? 33  GLN A O   1 
ATOM   273  C CB  . GLN A 1 46  ? -16.293 4.718   2.051   1.00 26.08 ? 33  GLN A CB  1 
ATOM   274  C CG  . GLN A 1 46  ? -16.591 3.704   3.152   1.00 32.03 ? 33  GLN A CG  1 
ATOM   275  C CD  . GLN A 1 46  ? -17.658 4.139   4.117   1.00 36.44 ? 33  GLN A CD  1 
ATOM   276  O OE1 . GLN A 1 46  ? -18.741 4.561   3.722   1.00 39.30 ? 33  GLN A OE1 1 
ATOM   277  N NE2 . GLN A 1 46  ? -17.354 4.002   5.400   1.00 43.95 ? 33  GLN A NE2 1 
ATOM   278  N N   . TYR A 1 47  ? -14.397 2.047   1.916   1.00 17.05 ? 34  TYR A N   1 
ATOM   279  C CA  . TYR A 1 47  ? -14.467 0.569   1.980   1.00 17.03 ? 34  TYR A CA  1 
ATOM   280  C C   . TYR A 1 47  ? -14.488 0.123   3.447   1.00 15.81 ? 34  TYR A C   1 
ATOM   281  O O   . TYR A 1 47  ? -13.990 0.837   4.313   1.00 13.89 ? 34  TYR A O   1 
ATOM   282  C CB  . TYR A 1 47  ? -13.319 -0.043  1.164   1.00 17.81 ? 34  TYR A CB  1 
ATOM   283  C CG  . TYR A 1 47  ? -11.942 0.043   1.783   1.00 17.60 ? 34  TYR A CG  1 
ATOM   284  C CD1 . TYR A 1 47  ? -11.518 -0.925  2.671   1.00 17.97 ? 34  TYR A CD1 1 
ATOM   285  C CD2 . TYR A 1 47  ? -11.046 1.052   1.449   1.00 17.55 ? 34  TYR A CD2 1 
ATOM   286  C CE1 . TYR A 1 47  ? -10.251 -0.889  3.234   1.00 18.53 ? 34  TYR A CE1 1 
ATOM   287  C CE2 . TYR A 1 47  ? -9.782  1.123   2.024   1.00 17.62 ? 34  TYR A CE2 1 
ATOM   288  C CZ  . TYR A 1 47  ? -9.381  0.140   2.918   1.00 18.19 ? 34  TYR A CZ  1 
ATOM   289  O OH  . TYR A 1 47  ? -8.145  0.123   3.495   1.00 17.65 ? 34  TYR A OH  1 
ATOM   290  N N   . SER A 1 48  ? -15.070 -1.046  3.705   1.00 16.12 ? 35  SER A N   1 
ATOM   291  C CA  . SER A 1 48  ? -15.017 -1.739  5.016   1.00 17.39 ? 35  SER A CA  1 
ATOM   292  C C   . SER A 1 48  ? -14.401 -3.111  4.798   1.00 16.56 ? 35  SER A C   1 
ATOM   293  O O   . SER A 1 48  ? -14.625 -3.678  3.723   1.00 17.16 ? 35  SER A O   1 
ATOM   294  C CB  . SER A 1 48  ? -16.369 -1.854  5.667   1.00 18.39 ? 35  SER A CB  1 
ATOM   295  O OG  . SER A 1 48  ? -16.830 -0.564  6.067   1.00 22.09 ? 35  SER A OG  1 
ATOM   296  N N   . VAL A 1 49  ? -13.664 -3.601  5.784   1.00 16.41 ? 36  VAL A N   1 
ATOM   297  C CA  . VAL A 1 49  ? -13.251 -5.028  5.855   1.00 18.65 ? 36  VAL A CA  1 
ATOM   298  C C   . VAL A 1 49  ? -13.335 -5.504  7.313   1.00 19.70 ? 36  VAL A C   1 
ATOM   299  O O   . VAL A 1 49  ? -13.088 -4.704  8.250   1.00 17.18 ? 36  VAL A O   1 
ATOM   300  C CB  . VAL A 1 49  ? -11.857 -5.235  5.237   1.00 19.45 ? 36  VAL A CB  1 
ATOM   301  C CG1 . VAL A 1 49  ? -10.789 -4.404  5.942   1.00 18.78 ? 36  VAL A CG1 1 
ATOM   302  C CG2 . VAL A 1 49  ? -11.489 -6.711  5.207   1.00 19.85 ? 36  VAL A CG2 1 
ATOM   303  N N   . GLU A 1 50  ? -13.749 -6.756  7.484   1.00 21.99 ? 37  GLU A N   1 
ATOM   304  C CA  . GLU A 1 50  ? -13.817 -7.446  8.794   1.00 25.00 ? 37  GLU A CA  1 
ATOM   305  C C   . GLU A 1 50  ? -13.111 -8.774  8.609   1.00 23.13 ? 37  GLU A C   1 
ATOM   306  O O   . GLU A 1 50  ? -13.390 -9.454  7.602   1.00 23.62 ? 37  GLU A O   1 
ATOM   307  C CB  . GLU A 1 50  ? -15.254 -7.721  9.244   1.00 29.94 ? 37  GLU A CB  1 
ATOM   308  C CG  . GLU A 1 50  ? -15.980 -6.501  9.778   1.00 37.62 ? 37  GLU A CG  1 
ATOM   309  C CD  . GLU A 1 50  ? -17.150 -6.775  10.720  1.00 43.84 ? 37  GLU A CD  1 
ATOM   310  O OE1 . GLU A 1 50  ? -18.149 -6.021  10.659  1.00 48.88 ? 37  GLU A OE1 1 
ATOM   311  O OE2 . GLU A 1 50  ? -17.057 -7.722  11.531  1.00 48.92 ? 37  GLU A OE2 1 
ATOM   312  N N   . TRP A 1 51  ? -12.231 -9.132  9.531   1.00 22.38 ? 38  TRP A N   1 
ATOM   313  C CA  . TRP A 1 51  ? -11.517 -10.424 9.433   1.00 21.85 ? 38  TRP A CA  1 
ATOM   314  C C   . TRP A 1 51  ? -11.442 -11.117 10.793  1.00 21.68 ? 38  TRP A C   1 
ATOM   315  O O   . TRP A 1 51  ? -11.578 -10.445 11.847  1.00 21.50 ? 38  TRP A O   1 
ATOM   316  C CB  . TRP A 1 51  ? -10.152 -10.246 8.770   1.00 20.11 ? 38  TRP A CB  1 
ATOM   317  C CG  . TRP A 1 51  ? -9.146  -9.433  9.515   1.00 19.35 ? 38  TRP A CG  1 
ATOM   318  C CD1 . TRP A 1 51  ? -8.072  -9.911  10.203  1.00 18.66 ? 38  TRP A CD1 1 
ATOM   319  C CD2 . TRP A 1 51  ? -9.058  -7.998  9.577   1.00 19.31 ? 38  TRP A CD2 1 
ATOM   320  N NE1 . TRP A 1 51  ? -7.323  -8.879  10.696  1.00 17.99 ? 38  TRP A NE1 1 
ATOM   321  C CE2 . TRP A 1 51  ? -7.890  -7.693  10.312  1.00 19.22 ? 38  TRP A CE2 1 
ATOM   322  C CE3 . TRP A 1 51  ? -9.819  -6.941  9.052   1.00 19.36 ? 38  TRP A CE3 1 
ATOM   323  C CZ2 . TRP A 1 51  ? -7.489  -6.375  10.558  1.00 19.42 ? 38  TRP A CZ2 1 
ATOM   324  C CZ3 . TRP A 1 51  ? -9.424  -5.640  9.300   1.00 19.24 ? 38  TRP A CZ3 1 
ATOM   325  C CH2 . TRP A 1 51  ? -8.271  -5.364  10.039  1.00 19.73 ? 38  TRP A CH2 1 
ATOM   326  N N   . SER A 1 52  ? -11.251 -12.433 10.736  1.00 21.05 ? 39  SER A N   1 
ATOM   327  C CA  . SER A 1 52  ? -11.331 -13.350 11.893  1.00 22.35 ? 39  SER A CA  1 
ATOM   328  C C   . SER A 1 52  ? -10.372 -14.515 11.640  1.00 21.01 ? 39  SER A C   1 
ATOM   329  O O   . SER A 1 52  ? -10.655 -15.304 10.732  1.00 20.33 ? 39  SER A O   1 
ATOM   330  C CB  . SER A 1 52  ? -12.769 -13.789 12.095  1.00 23.18 ? 39  SER A CB  1 
ATOM   331  O OG  . SER A 1 52  ? -12.887 -14.598 13.246  1.00 26.07 ? 39  SER A OG  1 
ATOM   332  N N   . ASN A 1 53  ? -9.250  -14.567 12.367  1.00 20.74 ? 40  ASN A N   1 
ATOM   333  C CA  . ASN A 1 53  ? -8.212  -15.623 12.221  1.00 20.65 ? 40  ASN A CA  1 
ATOM   334  C C   . ASN A 1 53  ? -7.840  -15.762 10.745  1.00 20.67 ? 40  ASN A C   1 
ATOM   335  O O   . ASN A 1 53  ? -7.864  -16.897 10.228  1.00 20.17 ? 40  ASN A O   1 
ATOM   336  C CB  . ASN A 1 53  ? -8.680  -16.962 12.796  1.00 20.35 ? 40  ASN A CB  1 
ATOM   337  C CG  . ASN A 1 53  ? -8.929  -16.871 14.283  1.00 20.29 ? 40  ASN A CG  1 
ATOM   338  O OD1 . ASN A 1 53  ? -8.064  -16.420 15.019  1.00 21.31 ? 40  ASN A OD1 1 
ATOM   339  N ND2 . ASN A 1 53  ? -10.095 -17.296 14.732  1.00 20.83 ? 40  ASN A ND2 1 
ATOM   340  N N   . SER A 1 54  ? -7.504  -14.635 10.115  1.00 21.78 ? 41  SER A N   1 
ATOM   341  C CA  . SER A 1 54  ? -7.132  -14.506 8.679   1.00 21.68 ? 41  SER A CA  1 
ATOM   342  C C   . SER A 1 54  ? -5.802  -15.202 8.381   1.00 21.17 ? 41  SER A C   1 
ATOM   343  O O   . SER A 1 54  ? -4.901  -15.181 9.242   1.00 21.12 ? 41  SER A O   1 
ATOM   344  C CB  . SER A 1 54  ? -7.044  -13.049 8.275   1.00 20.89 ? 41  SER A CB  1 
ATOM   345  O OG  . SER A 1 54  ? -5.963  -12.411 8.947   1.00 20.72 ? 41  SER A OG  1 
ATOM   346  N N   . GLY A 1 55  ? -5.683  -15.726 7.159   1.00 20.41 ? 42  GLY A N   1 
ATOM   347  C CA  . GLY A 1 55  ? -4.411  -15.814 6.422   1.00 20.52 ? 42  GLY A CA  1 
ATOM   348  C C   . GLY A 1 55  ? -3.979  -14.420 6.004   1.00 21.14 ? 42  GLY A C   1 
ATOM   349  O O   . GLY A 1 55  ? -4.356  -13.464 6.700   1.00 23.50 ? 42  GLY A O   1 
ATOM   350  N N   . ASN A 1 56  ? -3.202  -14.289 4.932   1.00 21.51 ? 43  ASN A N   1 
ATOM   351  C CA  . ASN A 1 56  ? -2.771  -12.967 4.401   1.00 21.25 ? 43  ASN A CA  1 
ATOM   352  C C   . ASN A 1 56  ? -3.946  -12.425 3.564   1.00 19.53 ? 43  ASN A C   1 
ATOM   353  O O   . ASN A 1 56  ? -4.592  -13.231 2.859   1.00 20.60 ? 43  ASN A O   1 
ATOM   354  C CB  . ASN A 1 56  ? -1.418  -13.074 3.682   1.00 22.26 ? 43  ASN A CB  1 
ATOM   355  C CG  . ASN A 1 56  ? -0.697  -11.744 3.495   1.00 25.65 ? 43  ASN A CG  1 
ATOM   356  O OD1 . ASN A 1 56  ? -0.786  -10.818 4.317   1.00 25.14 ? 43  ASN A OD1 1 
ATOM   357  N ND2 . ASN A 1 56  ? 0.065   -11.640 2.414   1.00 27.40 ? 43  ASN A ND2 1 
ATOM   358  N N   . PHE A 1 57  ? -4.287  -11.146 3.731   1.00 17.68 ? 44  PHE A N   1 
ATOM   359  C CA  . PHE A 1 57  ? -5.254  -10.402 2.881   1.00 17.50 ? 44  PHE A CA  1 
ATOM   360  C C   . PHE A 1 57  ? -4.833  -8.944  2.720   1.00 17.28 ? 44  PHE A C   1 
ATOM   361  O O   . PHE A 1 57  ? -4.223  -8.329  3.621   1.00 18.25 ? 44  PHE A O   1 
ATOM   362  C CB  . PHE A 1 57  ? -6.669  -10.421 3.465   1.00 17.28 ? 44  PHE A CB  1 
ATOM   363  C CG  . PHE A 1 57  ? -6.937  -9.403  4.545   1.00 16.68 ? 44  PHE A CG  1 
ATOM   364  C CD1 . PHE A 1 57  ? -7.399  -8.143  4.224   1.00 16.30 ? 44  PHE A CD1 1 
ATOM   365  C CD2 . PHE A 1 57  ? -6.792  -9.735  5.887   1.00 17.22 ? 44  PHE A CD2 1 
ATOM   366  C CE1 . PHE A 1 57  ? -7.682  -7.220  5.217   1.00 17.36 ? 44  PHE A CE1 1 
ATOM   367  C CE2 . PHE A 1 57  ? -7.072  -8.813  6.881   1.00 17.62 ? 44  PHE A CE2 1 
ATOM   368  C CZ  . PHE A 1 57  ? -7.513  -7.551  6.545   1.00 17.70 ? 44  PHE A CZ  1 
ATOM   369  N N   . VAL A 1 58  ? -5.209  -8.387  1.582   1.00 17.43 ? 45  VAL A N   1 
ATOM   370  C CA  . VAL A 1 58  ? -5.018  -6.950  1.244   1.00 16.80 ? 45  VAL A CA  1 
ATOM   371  C C   . VAL A 1 58  ? -6.365  -6.459  0.704   1.00 16.00 ? 45  VAL A C   1 
ATOM   372  O O   . VAL A 1 58  ? -7.000  -7.194  -0.089  1.00 16.76 ? 45  VAL A O   1 
ATOM   373  C CB  . VAL A 1 58  ? -3.864  -6.744  0.239   1.00 15.94 ? 45  VAL A CB  1 
ATOM   374  C CG1 . VAL A 1 58  ? -3.632  -5.268  -0.082  1.00 16.13 ? 45  VAL A CG1 1 
ATOM   375  C CG2 . VAL A 1 58  ? -2.572  -7.381  0.718   1.00 15.94 ? 45  VAL A CG2 1 
ATOM   376  N N   . ALA A 1 59  ? -6.778  -5.277  1.133   1.00 14.42 ? 46  ALA A N   1 
ATOM   377  C CA  . ALA A 1 59  ? -8.066  -4.651  0.773   1.00 14.58 ? 46  ALA A CA  1 
ATOM   378  C C   . ALA A 1 59  ? -7.910  -3.123  0.700   1.00 14.08 ? 46  ALA A C   1 
ATOM   379  O O   . ALA A 1 59  ? -7.338  -2.537  1.629   1.00 12.99 ? 46  ALA A O   1 
ATOM   380  C CB  . ALA A 1 59  ? -9.101  -5.068  1.779   1.00 14.64 ? 46  ALA A CB  1 
ATOM   381  N N   . GLY A 1 60  ? -8.386  -2.502  -0.381  1.00 13.75 ? 47  GLY A N   1 
ATOM   382  C CA  . GLY A 1 60  ? -8.626  -1.057  -0.366  1.00 14.47 ? 47  GLY A CA  1 
ATOM   383  C C   . GLY A 1 60  ? -8.940  -0.483  -1.719  1.00 15.20 ? 47  GLY A C   1 
ATOM   384  O O   . GLY A 1 60  ? -8.917  -1.221  -2.731  1.00 16.09 ? 47  GLY A O   1 
ATOM   385  N N   . LYS A 1 61  ? -9.220  0.812   -1.707  1.00 15.75 ? 48  LYS A N   1 
ATOM   386  C CA  . LYS A 1 61  ? -9.657  1.593   -2.880  1.00 16.36 ? 48  LYS A CA  1 
ATOM   387  C C   . LYS A 1 61  ? -8.546  2.548   -3.264  1.00 16.39 ? 48  LYS A C   1 
ATOM   388  O O   . LYS A 1 61  ? -7.691  2.819   -2.426  1.00 17.20 ? 48  LYS A O   1 
ATOM   389  C CB  . LYS A 1 61  ? -10.919 2.389   -2.564  1.00 16.29 ? 48  LYS A CB  1 
ATOM   390  C CG  . LYS A 1 61  ? -12.212 1.660   -2.892  1.00 16.14 ? 48  LYS A CG  1 
ATOM   391  C CD  . LYS A 1 61  ? -13.425 2.505   -2.577  1.00 16.80 ? 48  LYS A CD  1 
ATOM   392  C CE  . LYS A 1 61  ? -14.676 2.048   -3.303  1.00 17.05 ? 48  LYS A CE  1 
ATOM   393  N NZ  . LYS A 1 61  ? -15.868 2.680   -2.695  1.00 17.24 ? 48  LYS A NZ  1 
ATOM   394  N N   . GLY A 1 62  ? -8.601  3.051   -4.483  1.00 16.09 ? 49  GLY A N   1 
ATOM   395  C CA  . GLY A 1 62  ? -7.552  3.918   -5.018  1.00 17.13 ? 49  GLY A CA  1 
ATOM   396  C C   . GLY A 1 62  ? -7.700  4.046   -6.513  1.00 17.96 ? 49  GLY A C   1 
ATOM   397  O O   . GLY A 1 62  ? -8.848  4.215   -6.955  1.00 16.88 ? 49  GLY A O   1 
ATOM   398  N N   . TRP A 1 63  ? -6.585  3.921   -7.239  1.00 19.80 ? 50  TRP A N   1 
ATOM   399  C CA  . TRP A 1 63  ? -6.463  4.232   -8.684  1.00 21.94 ? 50  TRP A CA  1 
ATOM   400  C C   . TRP A 1 63  ? -5.685  3.118   -9.370  1.00 22.35 ? 50  TRP A C   1 
ATOM   401  O O   . TRP A 1 63  ? -4.835  2.511   -8.707  1.00 22.92 ? 50  TRP A O   1 
ATOM   402  C CB  . TRP A 1 63  ? -5.772  5.583   -8.896  1.00 23.77 ? 50  TRP A CB  1 
ATOM   403  C CG  . TRP A 1 63  ? -6.435  6.723   -8.190  1.00 25.79 ? 50  TRP A CG  1 
ATOM   404  C CD1 . TRP A 1 63  ? -7.284  7.639   -8.740  1.00 25.77 ? 50  TRP A CD1 1 
ATOM   405  C CD2 . TRP A 1 63  ? -6.320  7.056   -6.794  1.00 26.02 ? 50  TRP A CD2 1 
ATOM   406  N NE1 . TRP A 1 63  ? -7.685  8.534   -7.788  1.00 28.28 ? 50  TRP A NE1 1 
ATOM   407  C CE2 . TRP A 1 63  ? -7.109  8.208   -6.585  1.00 27.30 ? 50  TRP A CE2 1 
ATOM   408  C CE3 . TRP A 1 63  ? -5.599  6.528   -5.716  1.00 26.86 ? 50  TRP A CE3 1 
ATOM   409  C CZ2 . TRP A 1 63  ? -7.192  8.839   -5.345  1.00 26.26 ? 50  TRP A CZ2 1 
ATOM   410  C CZ3 . TRP A 1 63  ? -5.703  7.136   -4.481  1.00 26.49 ? 50  TRP A CZ3 1 
ATOM   411  C CH2 . TRP A 1 63  ? -6.483  8.278   -4.305  1.00 26.44 ? 50  TRP A CH2 1 
ATOM   412  N N   . ASN A 1 64  ? -6.016  2.882   -10.640 1.00 23.34 ? 51  ASN A N   1 
ATOM   413  C CA  . ASN A 1 64  ? -5.314  1.970   -11.570 1.00 25.94 ? 51  ASN A CA  1 
ATOM   414  C C   . ASN A 1 64  ? -5.343  2.595   -12.962 1.00 26.35 ? 51  ASN A C   1 
ATOM   415  O O   . ASN A 1 64  ? -6.387  2.676   -13.583 1.00 28.69 ? 51  ASN A O   1 
ATOM   416  C CB  . ASN A 1 64  ? -5.915  0.564   -11.573 1.00 26.21 ? 51  ASN A CB  1 
ATOM   417  C CG  . ASN A 1 64  ? -4.931  -0.452  -12.109 1.00 28.93 ? 51  ASN A CG  1 
ATOM   418  O OD1 . ASN A 1 64  ? -3.855  -0.093  -12.592 1.00 28.76 ? 51  ASN A OD1 1 
ATOM   419  N ND2 . ASN A 1 64  ? -5.273  -1.725  -12.010 1.00 32.74 ? 51  ASN A ND2 1 
ATOM   420  N N   . PRO A 1 65  ? -4.213  3.082   -13.506 1.00 27.48 ? 52  PRO A N   1 
ATOM   421  C CA  . PRO A 1 65  ? -2.929  3.046   -12.810 1.00 27.45 ? 52  PRO A CA  1 
ATOM   422  C C   . PRO A 1 65  ? -2.838  4.165   -11.757 1.00 28.17 ? 52  PRO A C   1 
ATOM   423  O O   . PRO A 1 65  ? -3.440  5.227   -11.927 1.00 26.66 ? 52  PRO A O   1 
ATOM   424  C CB  . PRO A 1 65  ? -1.923  3.211   -13.958 1.00 28.07 ? 52  PRO A CB  1 
ATOM   425  C CG  . PRO A 1 65  ? -2.660  4.086   -14.959 1.00 28.96 ? 52  PRO A CG  1 
ATOM   426  C CD  . PRO A 1 65  ? -4.124  3.700   -14.836 1.00 28.35 ? 52  PRO A CD  1 
ATOM   427  N N   . GLY A 1 66  ? -2.128  3.889   -10.662 1.00 27.84 ? 53  GLY A N   1 
ATOM   428  C CA  . GLY A 1 66  ? -1.701  4.928   -9.718  1.00 27.32 ? 53  GLY A CA  1 
ATOM   429  C C   . GLY A 1 66  ? -0.799  5.927   -10.418 1.00 28.76 ? 53  GLY A C   1 
ATOM   430  O O   . GLY A 1 66  ? -0.141  5.535   -11.405 1.00 29.71 ? 53  GLY A O   1 
ATOM   431  N N   . SER A 1 67  ? -0.808  7.172   -9.945  1.00 29.34 ? 54  SER A N   1 
ATOM   432  C CA  . SER A 1 67  ? 0.113   8.274   -10.317 1.00 31.19 ? 54  SER A CA  1 
ATOM   433  C C   . SER A 1 67  ? 0.882   8.722   -9.063  1.00 30.27 ? 54  SER A C   1 
ATOM   434  O O   . SER A 1 67  ? 1.115   7.895   -8.165  1.00 31.87 ? 54  SER A O   1 
ATOM   435  C CB  . SER A 1 67  ? -0.664  9.415   -10.955 1.00 33.62 ? 54  SER A CB  1 
ATOM   436  O OG  . SER A 1 67  ? -0.605  9.343   -12.371 1.00 36.42 ? 54  SER A OG  1 
ATOM   437  N N   . SER A 1 68  ? 1.280   9.986   -9.004  1.00 30.28 ? 55  SER A N   1 
ATOM   438  C CA  . SER A 1 68  ? 1.952   10.588  -7.831  1.00 32.01 ? 55  SER A CA  1 
ATOM   439  C C   . SER A 1 68  ? 0.996   11.603  -7.191  1.00 30.12 ? 55  SER A C   1 
ATOM   440  O O   . SER A 1 68  ? 1.424   12.692  -6.818  1.00 32.45 ? 55  SER A O   1 
ATOM   441  C CB  . SER A 1 68  ? 3.279   11.187  -8.240  1.00 31.60 ? 55  SER A CB  1 
ATOM   442  O OG  . SER A 1 68  ? 3.081   12.284  -9.115  1.00 33.67 ? 55  SER A OG  1 
ATOM   443  N N   . GLN A 1 69  ? -0.264  11.220  -7.033  1.00 31.02 ? 56  GLN A N   1 
ATOM   444  C CA  . GLN A 1 69  ? -1.310  12.097  -6.452  1.00 31.02 ? 56  GLN A CA  1 
ATOM   445  C C   . GLN A 1 69  ? -1.127  12.142  -4.930  1.00 28.34 ? 56  GLN A C   1 
ATOM   446  O O   . GLN A 1 69  ? -0.659  11.143  -4.351  1.00 27.36 ? 56  GLN A O   1 
ATOM   447  C CB  . GLN A 1 69  ? -2.721  11.659  -6.880  1.00 31.59 ? 56  GLN A CB  1 
ATOM   448  C CG  . GLN A 1 69  ? -3.049  10.194  -6.647  1.00 30.92 ? 56  GLN A CG  1 
ATOM   449  C CD  . GLN A 1 69  ? -2.973  9.413   -7.936  1.00 31.11 ? 56  GLN A CD  1 
ATOM   450  O OE1 . GLN A 1 69  ? -2.031  8.674   -8.182  1.00 29.65 ? 56  GLN A OE1 1 
ATOM   451  N NE2 . GLN A 1 69  ? -3.970  9.577   -8.785  1.00 33.18 ? 56  GLN A NE2 1 
ATOM   452  N N   . THR A 1 70  ? -1.459  13.292  -4.340  1.00 26.67 ? 57  THR A N   1 
ATOM   453  C CA  . THR A 1 70  ? -1.446  13.569  -2.883  1.00 25.87 ? 57  THR A CA  1 
ATOM   454  C C   . THR A 1 70  ? -2.771  13.077  -2.322  1.00 23.97 ? 57  THR A C   1 
ATOM   455  O O   . THR A 1 70  ? -3.781  13.689  -2.617  1.00 27.61 ? 57  THR A O   1 
ATOM   456  C CB  . THR A 1 70  ? -1.199  15.061  -2.622  1.00 26.51 ? 57  THR A CB  1 
ATOM   457  O OG1 . THR A 1 70  ? 0.048   15.400  -3.228  1.00 25.78 ? 57  THR A OG1 1 
ATOM   458  C CG2 . THR A 1 70  ? -1.136  15.419  -1.155  1.00 27.13 ? 57  THR A CG2 1 
ATOM   459  N N   . ILE A 1 71  ? -2.752  11.970  -1.594  1.00 24.23 ? 58  ILE A N   1 
ATOM   460  C CA  . ILE A 1 71  ? -3.956  11.214  -1.143  1.00 21.80 ? 58  ILE A CA  1 
ATOM   461  C C   . ILE A 1 71  ? -4.355  11.770  0.218   1.00 21.25 ? 58  ILE A C   1 
ATOM   462  O O   . ILE A 1 71  ? -3.452  11.980  1.036   1.00 20.58 ? 58  ILE A O   1 
ATOM   463  C CB  . ILE A 1 71  ? -3.617  9.719   -1.028  1.00 22.27 ? 58  ILE A CB  1 
ATOM   464  C CG1 . ILE A 1 71  ? -3.121  9.145   -2.352  1.00 23.29 ? 58  ILE A CG1 1 
ATOM   465  C CG2 . ILE A 1 71  ? -4.781  8.921   -0.452  1.00 22.98 ? 58  ILE A CG2 1 
ATOM   466  C CD1 . ILE A 1 71  ? -2.609  7.733   -2.219  1.00 25.08 ? 58  ILE A CD1 1 
ATOM   467  N N   . THR A 1 72  ? -5.641  11.977  0.468   1.00 19.74 ? 59  THR A N   1 
ATOM   468  C CA  . THR A 1 72  ? -6.135  12.196  1.846   1.00 20.24 ? 59  THR A CA  1 
ATOM   469  C C   . THR A 1 72  ? -7.021  10.993  2.140   1.00 19.04 ? 59  THR A C   1 
ATOM   470  O O   . THR A 1 72  ? -7.742  10.545  1.242   1.00 20.96 ? 59  THR A O   1 
ATOM   471  C CB  . THR A 1 72  ? -6.763  13.586  2.047   1.00 20.84 ? 59  THR A CB  1 
ATOM   472  O OG1 . THR A 1 72  ? -8.060  13.635  1.455   1.00 28.46 ? 59  THR A OG1 1 
ATOM   473  C CG2 . THR A 1 72  ? -5.961  14.708  1.432   1.00 20.57 ? 59  THR A CG2 1 
ATOM   474  N N   . TYR A 1 73  ? -6.900  10.428  3.322   1.00 17.44 ? 60  TYR A N   1 
ATOM   475  C CA  . TYR A 1 73  ? -7.675  9.234   3.708   1.00 17.43 ? 60  TYR A CA  1 
ATOM   476  C C   . TYR A 1 73  ? -8.052  9.441   5.157   1.00 17.78 ? 60  TYR A C   1 
ATOM   477  O O   . TYR A 1 73  ? -7.291  10.106  5.886   1.00 18.09 ? 60  TYR A O   1 
ATOM   478  C CB  . TYR A 1 73  ? -6.861  7.952   3.500   1.00 16.55 ? 60  TYR A CB  1 
ATOM   479  C CG  . TYR A 1 73  ? -5.817  7.778   4.564   1.00 16.08 ? 60  TYR A CG  1 
ATOM   480  C CD1 . TYR A 1 73  ? -4.645  8.525   4.528   1.00 15.81 ? 60  TYR A CD1 1 
ATOM   481  C CD2 . TYR A 1 73  ? -6.042  6.968   5.662   1.00 15.43 ? 60  TYR A CD2 1 
ATOM   482  C CE1 . TYR A 1 73  ? -3.684  8.410   5.521   1.00 15.65 ? 60  TYR A CE1 1 
ATOM   483  C CE2 . TYR A 1 73  ? -5.089  6.845   6.661   1.00 15.81 ? 60  TYR A CE2 1 
ATOM   484  C CZ  . TYR A 1 73  ? -3.907  7.568   6.594   1.00 15.60 ? 60  TYR A CZ  1 
ATOM   485  O OH  . TYR A 1 73  ? -2.980  7.489   7.594   1.00 15.52 ? 60  TYR A OH  1 
ATOM   486  N N   . SER A 1 74  ? -9.161  8.844   5.556   1.00 19.94 ? 61  SER A N   1 
ATOM   487  C CA  . SER A 1 74  ? -9.764  9.017   6.896   1.00 20.34 ? 61  SER A CA  1 
ATOM   488  C C   . SER A 1 74  ? -10.402 7.699   7.307   1.00 19.30 ? 61  SER A C   1 
ATOM   489  O O   . SER A 1 74  ? -10.361 6.768   6.499   1.00 20.79 ? 61  SER A O   1 
ATOM   490  C CB  . SER A 1 74  ? -10.767 10.139  6.856   1.00 21.84 ? 61  SER A CB  1 
ATOM   491  O OG  . SER A 1 74  ? -11.837 9.785   5.999   1.00 23.28 ? 61  SER A OG  1 
ATOM   492  N N   . GLY A 1 75  ? -10.960 7.652   8.514   1.00 19.03 ? 62  GLY A N   1 
ATOM   493  C CA  . GLY A 1 75  ? -11.713 6.513   9.052   1.00 18.55 ? 62  GLY A CA  1 
ATOM   494  C C   . GLY A 1 75  ? -11.001 5.907   10.241  1.00 19.57 ? 62  GLY A C   1 
ATOM   495  O O   . GLY A 1 75  ? -10.496 6.650   11.076  1.00 19.50 ? 62  GLY A O   1 
ATOM   496  N N   . GLU A 1 76  ? -10.899 4.587   10.256  1.00 21.69 ? 63  GLU A N   1 
ATOM   497  C CA  . GLU A 1 76  ? -10.916 3.761   11.488  1.00 24.27 ? 63  GLU A CA  1 
ATOM   498  C C   . GLU A 1 76  ? -10.298 2.388   11.192  1.00 21.14 ? 63  GLU A C   1 
ATOM   499  O O   . GLU A 1 76  ? -10.729 1.719   10.244  1.00 19.66 ? 63  GLU A O   1 
ATOM   500  C CB  . GLU A 1 76  ? -12.370 3.582   11.922  1.00 28.81 ? 63  GLU A CB  1 
ATOM   501  C CG  . GLU A 1 76  ? -12.549 3.473   13.410  1.00 34.21 ? 63  GLU A CG  1 
ATOM   502  C CD  . GLU A 1 76  ? -14.012 3.355   13.785  1.00 38.21 ? 63  GLU A CD  1 
ATOM   503  O OE1 . GLU A 1 76  ? -14.355 2.405   14.509  1.00 43.43 ? 63  GLU A OE1 1 
ATOM   504  O OE2 . GLU A 1 76  ? -14.800 4.215   13.343  1.00 45.55 ? 63  GLU A OE2 1 
ATOM   505  N N   . TRP A 1 77  ? -9.352  1.964   12.007  1.00 21.01 ? 64  TRP A N   1 
ATOM   506  C CA  . TRP A 1 77  ? -8.538  0.749   11.748  1.00 22.57 ? 64  TRP A CA  1 
ATOM   507  C C   . TRP A 1 77  ? -8.342  0.049   13.097  1.00 22.10 ? 64  TRP A C   1 
ATOM   508  O O   . TRP A 1 77  ? -7.478  0.509   13.875  1.00 19.82 ? 64  TRP A O   1 
ATOM   509  C CB  . TRP A 1 77  ? -7.251  1.181   11.013  1.00 22.30 ? 64  TRP A CB  1 
ATOM   510  C CG  . TRP A 1 77  ? -6.194  0.141   10.838  1.00 23.03 ? 64  TRP A CG  1 
ATOM   511  C CD1 . TRP A 1 77  ? -6.156  -0.858  9.910   1.00 23.74 ? 64  TRP A CD1 1 
ATOM   512  C CD2 . TRP A 1 77  ? -4.980  0.027   11.598  1.00 23.18 ? 64  TRP A CD2 1 
ATOM   513  N NE1 . TRP A 1 77  ? -5.015  -1.598  10.057  1.00 24.12 ? 64  TRP A NE1 1 
ATOM   514  C CE2 . TRP A 1 77  ? -4.273  -1.083  11.084  1.00 22.88 ? 64  TRP A CE2 1 
ATOM   515  C CE3 . TRP A 1 77  ? -4.426  0.751   12.658  1.00 23.01 ? 64  TRP A CE3 1 
ATOM   516  C CZ2 . TRP A 1 77  ? -3.040  -1.487  11.594  1.00 22.53 ? 64  TRP A CZ2 1 
ATOM   517  C CZ3 . TRP A 1 77  ? -3.212  0.341   13.171  1.00 24.00 ? 64  TRP A CZ3 1 
ATOM   518  C CH2 . TRP A 1 77  ? -2.527  -0.757  12.639  1.00 23.53 ? 64  TRP A CH2 1 
ATOM   519  N N   . ASN A 1 78  ? -9.190  -0.956  13.378  1.00 23.14 ? 65  ASN A N   1 
ATOM   520  C CA  . ASN A 1 78  ? -9.270  -1.693  14.673  1.00 23.99 ? 65  ASN A CA  1 
ATOM   521  C C   . ASN A 1 78  ? -8.803  -3.136  14.498  1.00 23.18 ? 65  ASN A C   1 
ATOM   522  O O   . ASN A 1 78  ? -9.610  -4.057  14.533  1.00 23.23 ? 65  ASN A O   1 
ATOM   523  C CB  . ASN A 1 78  ? -10.682 -1.638  15.257  1.00 26.31 ? 65  ASN A CB  1 
ATOM   524  C CG  . ASN A 1 78  ? -11.227 -0.227  15.252  1.00 30.53 ? 65  ASN A CG  1 
ATOM   525  O OD1 . ASN A 1 78  ? -10.593 0.670   15.798  1.00 32.14 ? 65  ASN A OD1 1 
ATOM   526  N ND2 . ASN A 1 78  ? -12.370 -0.019  14.610  1.00 32.84 ? 65  ASN A ND2 1 
ATOM   527  N N   . PRO A 1 79  ? -7.490  -3.394  14.298  1.00 23.05 ? 66  PRO A N   1 
ATOM   528  C CA  . PRO A 1 79  ? -6.966  -4.758  14.308  1.00 23.33 ? 66  PRO A CA  1 
ATOM   529  C C   . PRO A 1 79  ? -6.704  -5.340  15.704  1.00 23.76 ? 66  PRO A C   1 
ATOM   530  O O   . PRO A 1 79  ? -6.270  -4.605  16.570  1.00 25.69 ? 66  PRO A O   1 
ATOM   531  C CB  . PRO A 1 79  ? -5.617  -4.588  13.594  1.00 23.33 ? 66  PRO A CB  1 
ATOM   532  C CG  . PRO A 1 79  ? -5.160  -3.225  14.054  1.00 23.58 ? 66  PRO A CG  1 
ATOM   533  C CD  . PRO A 1 79  ? -6.440  -2.405  14.007  1.00 23.28 ? 66  PRO A CD  1 
ATOM   534  N N   . ASN A 1 80  ? -6.905  -6.653  15.852  1.00 25.18 ? 67  ASN A N   1 
ATOM   535  C CA  . ASN A 1 80  ? -6.432  -7.486  16.988  1.00 24.69 ? 67  ASN A CA  1 
ATOM   536  C C   . ASN A 1 80  ? -5.367  -8.447  16.446  1.00 24.11 ? 67  ASN A C   1 
ATOM   537  O O   . ASN A 1 80  ? -5.728  -9.571  16.000  1.00 23.14 ? 67  ASN A O   1 
ATOM   538  C CB  . ASN A 1 80  ? -7.589  -8.205  17.695  1.00 27.61 ? 67  ASN A CB  1 
ATOM   539  C CG  . ASN A 1 80  ? -7.264  -8.564  19.135  1.00 31.53 ? 67  ASN A CG  1 
ATOM   540  O OD1 . ASN A 1 80  ? -7.247  -9.737  19.512  1.00 34.90 ? 67  ASN A OD1 1 
ATOM   541  N ND2 . ASN A 1 80  ? -7.006  -7.558  19.958  1.00 33.30 ? 67  ASN A ND2 1 
ATOM   542  N N   . GLY A 1 81  ? -4.102  -8.020  16.504  1.00 22.27 ? 68  GLY A N   1 
ATOM   543  C CA  . GLY A 1 81  ? -2.949  -8.738  15.934  1.00 21.66 ? 68  GLY A CA  1 
ATOM   544  C C   . GLY A 1 81  ? -2.371  -8.033  14.717  1.00 21.15 ? 68  GLY A C   1 
ATOM   545  O O   . GLY A 1 81  ? -2.637  -6.830  14.527  1.00 20.11 ? 68  GLY A O   1 
ATOM   546  N N   . ASN A 1 82  ? -1.596  -8.776  13.927  1.00 22.37 ? 69  ASN A N   1 
ATOM   547  C CA  . ASN A 1 82  ? -0.729  -8.291  12.818  1.00 22.08 ? 69  ASN A CA  1 
ATOM   548  C C   . ASN A 1 82  ? -1.602  -7.688  11.711  1.00 21.31 ? 69  ASN A C   1 
ATOM   549  O O   . ASN A 1 82  ? -2.398  -8.435  11.062  1.00 20.85 ? 69  ASN A O   1 
ATOM   550  C CB  . ASN A 1 82  ? 0.145   -9.434  12.293  1.00 23.27 ? 69  ASN A CB  1 
ATOM   551  C CG  . ASN A 1 82  ? 1.163   -9.016  11.254  1.00 24.46 ? 69  ASN A CG  1 
ATOM   552  O OD1 . ASN A 1 82  ? 1.415   -7.834  11.035  1.00 27.40 ? 69  ASN A OD1 1 
ATOM   553  N ND2 . ASN A 1 82  ? 1.748   -9.993  10.592  1.00 26.05 ? 69  ASN A ND2 1 
ATOM   554  N N   . SER A 1 83  ? -1.456  -6.385  11.505  1.00 19.87 ? 70  SER A N   1 
ATOM   555  C CA  . SER A 1 83  ? -2.157  -5.615  10.449  1.00 19.07 ? 70  SER A CA  1 
ATOM   556  C C   . SER A 1 83  ? -1.365  -4.347  10.174  1.00 17.18 ? 70  SER A C   1 
ATOM   557  O O   . SER A 1 83  ? -0.761  -3.832  11.111  1.00 17.49 ? 70  SER A O   1 
ATOM   558  C CB  . SER A 1 83  ? -3.580  -5.303  10.827  1.00 19.57 ? 70  SER A CB  1 
ATOM   559  O OG  . SER A 1 83  ? -4.227  -4.603  9.772   1.00 20.08 ? 70  SER A OG  1 
ATOM   560  N N   . TYR A 1 84  ? -1.321  -3.922  8.919   1.00 17.69 ? 71  TYR A N   1 
ATOM   561  C CA  . TYR A 1 84  ? -0.776  -2.610  8.498   1.00 19.04 ? 71  TYR A CA  1 
ATOM   562  C C   . TYR A 1 84  ? -1.863  -1.818  7.776   1.00 17.46 ? 71  TYR A C   1 
ATOM   563  O O   . TYR A 1 84  ? -2.737  -2.438  7.130   1.00 15.70 ? 71  TYR A O   1 
ATOM   564  C CB  . TYR A 1 84  ? 0.353   -2.718  7.475   1.00 20.87 ? 71  TYR A CB  1 
ATOM   565  C CG  . TYR A 1 84  ? 1.185   -3.968  7.486   1.00 24.15 ? 71  TYR A CG  1 
ATOM   566  C CD1 . TYR A 1 84  ? 1.834   -4.403  8.637   1.00 26.94 ? 71  TYR A CD1 1 
ATOM   567  C CD2 . TYR A 1 84  ? 1.456   -4.631  6.299   1.00 26.96 ? 71  TYR A CD2 1 
ATOM   568  C CE1 . TYR A 1 84  ? 2.673   -5.512  8.625   1.00 28.23 ? 71  TYR A CE1 1 
ATOM   569  C CE2 . TYR A 1 84  ? 2.285   -5.745  6.270   1.00 29.87 ? 71  TYR A CE2 1 
ATOM   570  C CZ  . TYR A 1 84  ? 2.909   -6.177  7.432   1.00 29.72 ? 71  TYR A CZ  1 
ATOM   571  O OH  . TYR A 1 84  ? 3.730   -7.265  7.382   1.00 31.53 ? 71  TYR A OH  1 
ATOM   572  N N   . LEU A 1 85  ? -1.743  -0.493  7.837   1.00 17.29 ? 72  LEU A N   1 
ATOM   573  C CA  . LEU A 1 85  ? -2.525  0.470   7.023   1.00 17.89 ? 72  LEU A CA  1 
ATOM   574  C C   . LEU A 1 85  ? -1.534  1.307   6.204   1.00 17.02 ? 72  LEU A C   1 
ATOM   575  O O   . LEU A 1 85  ? -0.618  1.918   6.808   1.00 15.54 ? 72  LEU A O   1 
ATOM   576  C CB  . LEU A 1 85  ? -3.391  1.330   7.945   1.00 17.76 ? 72  LEU A CB  1 
ATOM   577  C CG  . LEU A 1 85  ? -4.379  2.233   7.211   1.00 18.53 ? 72  LEU A CG  1 
ATOM   578  C CD1 . LEU A 1 85  ? -5.576  1.429   6.704   1.00 18.18 ? 72  LEU A CD1 1 
ATOM   579  C CD2 . LEU A 1 85  ? -4.835  3.378   8.110   1.00 18.82 ? 72  LEU A CD2 1 
ATOM   580  N N   . SER A 1 86  ? -1.668  1.275   4.875   1.00 16.96 ? 73  SER A N   1 
ATOM   581  C CA  . SER A 1 86  ? -0.609  1.733   3.948   1.00 17.60 ? 73  SER A CA  1 
ATOM   582  C C   . SER A 1 86  ? -1.215  2.318   2.691   1.00 16.68 ? 73  SER A C   1 
ATOM   583  O O   . SER A 1 86  ? -2.289  1.890   2.302   1.00 16.21 ? 73  SER A O   1 
ATOM   584  C CB  . SER A 1 86  ? 0.311   0.611   3.564   1.00 18.80 ? 73  SER A CB  1 
ATOM   585  O OG  . SER A 1 86  ? 0.708   -0.126  4.704   1.00 21.54 ? 73  SER A OG  1 
ATOM   586  N N   . VAL A 1 87  ? -0.482  3.227   2.062   1.00 16.25 ? 74  VAL A N   1 
ATOM   587  C CA  . VAL A 1 87  ? -0.622  3.456   0.608   1.00 15.58 ? 74  VAL A CA  1 
ATOM   588  C C   . VAL A 1 87  ? 0.217   2.359   -0.014  1.00 15.62 ? 74  VAL A C   1 
ATOM   589  O O   . VAL A 1 87  ? 1.415   2.322   0.223   1.00 16.50 ? 74  VAL A O   1 
ATOM   590  C CB  . VAL A 1 87  ? -0.190  4.856   0.168   1.00 15.25 ? 74  VAL A CB  1 
ATOM   591  C CG1 . VAL A 1 87  ? -0.251  4.989   -1.345  1.00 15.32 ? 74  VAL A CG1 1 
ATOM   592  C CG2 . VAL A 1 87  ? -1.031  5.918   0.862   1.00 15.15 ? 74  VAL A CG2 1 
ATOM   593  N N   . TYR A 1 88  ? -0.438  1.481   -0.742  1.00 15.45 ? 75  TYR A N   1 
ATOM   594  C CA  . TYR A 1 88  ? 0.104   0.195   -1.215  1.00 15.69 ? 75  TYR A CA  1 
ATOM   595  C C   . TYR A 1 88  ? -0.071  0.159   -2.731  1.00 16.56 ? 75  TYR A C   1 
ATOM   596  O O   . TYR A 1 88  ? -1.112  0.631   -3.226  1.00 17.24 ? 75  TYR A O   1 
ATOM   597  C CB  . TYR A 1 88  ? -0.626  -0.956  -0.507  1.00 15.18 ? 75  TYR A CB  1 
ATOM   598  C CG  . TYR A 1 88  ? -0.289  -2.312  -1.054  1.00 14.73 ? 75  TYR A CG  1 
ATOM   599  C CD1 . TYR A 1 88  ? 0.904   -2.927  -0.708  1.00 15.40 ? 75  TYR A CD1 1 
ATOM   600  C CD2 . TYR A 1 88  ? -1.125  -2.962  -1.946  1.00 15.12 ? 75  TYR A CD2 1 
ATOM   601  C CE1 . TYR A 1 88  ? 1.266   -4.156  -1.231  1.00 14.86 ? 75  TYR A CE1 1 
ATOM   602  C CE2 . TYR A 1 88  ? -0.768  -4.192  -2.491  1.00 15.44 ? 75  TYR A CE2 1 
ATOM   603  C CZ  . TYR A 1 88  ? 0.433   -4.778  -2.133  1.00 14.68 ? 75  TYR A CZ  1 
ATOM   604  O OH  . TYR A 1 88  ? 0.809   -5.981  -2.623  1.00 16.55 ? 75  TYR A OH  1 
ATOM   605  N N   . GLY A 1 89  ? 0.903   -0.402  -3.441  1.00 17.32 ? 76  GLY A N   1 
ATOM   606  C CA  . GLY A 1 89  ? 0.748   -0.696  -4.875  1.00 17.77 ? 76  GLY A CA  1 
ATOM   607  C C   . GLY A 1 89  ? 2.026   -1.240  -5.489  1.00 17.12 ? 76  GLY A C   1 
ATOM   608  O O   . GLY A 1 89  ? 2.878   -1.759  -4.752  1.00 14.92 ? 76  GLY A O   1 
ATOM   609  N N   . TRP A 1 90  ? 2.112   -1.140  -6.807  1.00 17.45 ? 77  TRP A N   1 
ATOM   610  C CA  . TRP A 1 90  ? 3.020   -1.939  -7.661  1.00 19.01 ? 77  TRP A CA  1 
ATOM   611  C C   . TRP A 1 90  ? 3.464   -1.102  -8.857  1.00 19.66 ? 77  TRP A C   1 
ATOM   612  O O   . TRP A 1 90  ? 2.593   -0.425  -9.469  1.00 22.18 ? 77  TRP A O   1 
ATOM   613  C CB  . TRP A 1 90  ? 2.304   -3.203  -8.163  1.00 19.03 ? 77  TRP A CB  1 
ATOM   614  C CG  . TRP A 1 90  ? 1.951   -4.212  -7.118  1.00 18.45 ? 77  TRP A CG  1 
ATOM   615  C CD1 . TRP A 1 90  ? 0.847   -4.209  -6.314  1.00 18.46 ? 77  TRP A CD1 1 
ATOM   616  C CD2 . TRP A 1 90  ? 2.650   -5.443  -6.839  1.00 18.01 ? 77  TRP A CD2 1 
ATOM   617  N NE1 . TRP A 1 90  ? 0.849   -5.322  -5.511  1.00 18.69 ? 77  TRP A NE1 1 
ATOM   618  C CE2 . TRP A 1 90  ? 1.938   -6.097  -5.811  1.00 17.94 ? 77  TRP A CE2 1 
ATOM   619  C CE3 . TRP A 1 90  ? 3.815   -6.046  -7.332  1.00 17.07 ? 77  TRP A CE3 1 
ATOM   620  C CZ2 . TRP A 1 90  ? 2.357   -7.323  -5.287  1.00 18.55 ? 77  TRP A CZ2 1 
ATOM   621  C CZ3 . TRP A 1 90  ? 4.246   -7.235  -6.791  1.00 16.24 ? 77  TRP A CZ3 1 
ATOM   622  C CH2 . TRP A 1 90  ? 3.522   -7.873  -5.786  1.00 16.75 ? 77  TRP A CH2 1 
ATOM   623  N N   . THR A 1 91  ? 4.743   -1.201  -9.218  1.00 19.82 ? 78  THR A N   1 
ATOM   624  C CA  . THR A 1 91  ? 5.244   -0.868  -10.577 1.00 19.26 ? 78  THR A CA  1 
ATOM   625  C C   . THR A 1 91  ? 5.626   -2.158  -11.303 1.00 18.64 ? 78  THR A C   1 
ATOM   626  O O   . THR A 1 91  ? 5.704   -3.240  -10.667 1.00 17.84 ? 78  THR A O   1 
ATOM   627  C CB  . THR A 1 91  ? 6.449   0.079   -10.561 1.00 20.29 ? 78  THR A CB  1 
ATOM   628  O OG1 . THR A 1 91  ? 7.595   -0.686  -10.188 1.00 20.77 ? 78  THR A OG1 1 
ATOM   629  C CG2 . THR A 1 91  ? 6.282   1.263   -9.628  1.00 20.58 ? 78  THR A CG2 1 
ATOM   630  N N   . GLN A 1 92  ? 5.817   -2.029  -12.609 1.00 19.00 ? 79  GLN A N   1 
ATOM   631  C CA  . GLN A 1 92  ? 6.150   -3.129  -13.544 1.00 19.54 ? 79  GLN A CA  1 
ATOM   632  C C   . GLN A 1 92  ? 7.351   -2.669  -14.367 1.00 19.28 ? 79  GLN A C   1 
ATOM   633  O O   . GLN A 1 92  ? 7.382   -1.477  -14.809 1.00 18.35 ? 79  GLN A O   1 
ATOM   634  C CB  . GLN A 1 92  ? 4.953   -3.459  -14.443 1.00 20.00 ? 79  GLN A CB  1 
ATOM   635  C CG  . GLN A 1 92  ? 3.934   -4.379  -13.794 1.00 20.14 ? 79  GLN A CG  1 
ATOM   636  C CD  . GLN A 1 92  ? 2.680   -4.513  -14.623 1.00 22.09 ? 79  GLN A CD  1 
ATOM   637  O OE1 . GLN A 1 92  ? 1.896   -3.569  -14.747 1.00 23.59 ? 79  GLN A OE1 1 
ATOM   638  N NE2 . GLN A 1 92  ? 2.470   -5.700  -15.174 1.00 20.07 ? 79  GLN A NE2 1 
ATOM   639  N N   . ASN A 1 93  ? 8.303   -3.577  -14.567 1.00 19.69 ? 80  ASN A N   1 
ATOM   640  C CA  . ASN A 1 93  ? 9.475   -3.306  -15.428 1.00 18.62 ? 80  ASN A CA  1 
ATOM   641  C C   . ASN A 1 93  ? 10.247  -2.124  -14.861 1.00 17.97 ? 80  ASN A C   1 
ATOM   642  O O   . ASN A 1 93  ? 10.276  -1.070  -15.473 1.00 19.65 ? 80  ASN A O   1 
ATOM   643  C CB  . ASN A 1 93  ? 9.012   -2.995  -16.850 1.00 17.84 ? 80  ASN A CB  1 
ATOM   644  C CG  . ASN A 1 93  ? 10.149  -2.993  -17.836 1.00 17.93 ? 80  ASN A CG  1 
ATOM   645  O OD1 . ASN A 1 93  ? 9.970   -2.513  -18.944 1.00 19.74 ? 80  ASN A OD1 1 
ATOM   646  N ND2 . ASN A 1 93  ? 11.301  -3.515  -17.447 1.00 15.48 ? 80  ASN A ND2 1 
ATOM   647  N N   . PRO A 1 94  ? 10.873  -2.239  -13.673 1.00 17.23 ? 81  PRO A N   1 
ATOM   648  C CA  . PRO A 1 94  ? 10.843  -3.465  -12.879 1.00 16.62 ? 81  PRO A CA  1 
ATOM   649  C C   . PRO A 1 94  ? 9.547   -3.697  -12.088 1.00 15.96 ? 81  PRO A C   1 
ATOM   650  O O   . PRO A 1 94  ? 8.829   -2.752  -11.765 1.00 14.06 ? 81  PRO A O   1 
ATOM   651  C CB  . PRO A 1 94  ? 11.958  -3.225  -11.870 1.00 16.59 ? 81  PRO A CB  1 
ATOM   652  C CG  . PRO A 1 94  ? 11.868  -1.735  -11.633 1.00 16.87 ? 81  PRO A CG  1 
ATOM   653  C CD  . PRO A 1 94  ? 11.619  -1.165  -13.011 1.00 17.12 ? 81  PRO A CD  1 
ATOM   654  N N   . LEU A 1 95  ? 9.308   -4.966  -11.780 1.00 15.65 ? 82  LEU A N   1 
ATOM   655  C CA  . LEU A 1 95  ? 8.297   -5.409  -10.796 1.00 16.22 ? 82  LEU A CA  1 
ATOM   656  C C   . LEU A 1 95  ? 8.675   -4.903  -9.396  1.00 16.89 ? 82  LEU A C   1 
ATOM   657  O O   . LEU A 1 95  ? 9.743   -5.285  -8.873  1.00 16.35 ? 82  LEU A O   1 
ATOM   658  C CB  . LEU A 1 95  ? 8.208   -6.939  -10.856 1.00 16.63 ? 82  LEU A CB  1 
ATOM   659  C CG  . LEU A 1 95  ? 6.949   -7.541  -10.237 1.00 15.98 ? 82  LEU A CG  1 
ATOM   660  C CD1 . LEU A 1 95  ? 5.702   -7.006  -10.916 1.00 16.08 ? 82  LEU A CD1 1 
ATOM   661  C CD2 . LEU A 1 95  ? 7.001   -9.050  -10.295 1.00 16.61 ? 82  LEU A CD2 1 
ATOM   662  N N   . VAL A 1 96  ? 7.830   -4.047  -8.809  1.00 18.15 ? 83  VAL A N   1 
ATOM   663  C CA  . VAL A 1 96  ? 8.036   -3.486  -7.437  1.00 17.64 ? 83  VAL A CA  1 
ATOM   664  C C   . VAL A 1 96  ? 6.694   -3.459  -6.703  1.00 18.58 ? 83  VAL A C   1 
ATOM   665  O O   . VAL A 1 96  ? 5.744   -2.893  -7.245  1.00 19.57 ? 83  VAL A O   1 
ATOM   666  C CB  . VAL A 1 96  ? 8.666   -2.086  -7.484  1.00 16.39 ? 83  VAL A CB  1 
ATOM   667  C CG1 . VAL A 1 96  ? 8.687   -1.433  -6.107  1.00 16.17 ? 83  VAL A CG1 1 
ATOM   668  C CG2 . VAL A 1 96  ? 10.062  -2.131  -8.085  1.00 15.95 ? 83  VAL A CG2 1 
ATOM   669  N N   . GLU A 1 97  ? 6.641   -4.076  -5.523  1.00 19.13 ? 84  GLU A N   1 
ATOM   670  C CA  . GLU A 1 97  ? 5.546   -3.904  -4.540  1.00 18.51 ? 84  GLU A CA  1 
ATOM   671  C C   . GLU A 1 97  ? 6.005   -2.833  -3.546  1.00 19.36 ? 84  GLU A C   1 
ATOM   672  O O   . GLU A 1 97  ? 7.156   -2.923  -3.064  1.00 17.38 ? 84  GLU A O   1 
ATOM   673  C CB  . GLU A 1 97  ? 5.238   -5.227  -3.852  1.00 18.34 ? 84  GLU A CB  1 
ATOM   674  C CG  . GLU A 1 97  ? 4.189   -5.126  -2.772  1.00 18.25 ? 84  GLU A CG  1 
ATOM   675  C CD  . GLU A 1 97  ? 3.980   -6.449  -2.072  1.00 18.61 ? 84  GLU A CD  1 
ATOM   676  O OE1 . GLU A 1 97  ? 2.803   -6.848  -1.879  1.00 19.41 ? 84  GLU A OE1 1 
ATOM   677  O OE2 . GLU A 1 97  ? 5.002   -7.087  -1.733  1.00 18.23 ? 84  GLU A OE2 1 
ATOM   678  N N   . TYR A 1 98  ? 5.166   -1.829  -3.278  1.00 18.33 ? 85  TYR A N   1 
ATOM   679  C CA  . TYR A 1 98  ? 5.544   -0.691  -2.405  1.00 18.55 ? 85  TYR A CA  1 
ATOM   680  C C   . TYR A 1 98  ? 4.474   -0.415  -1.327  1.00 19.00 ? 85  TYR A C   1 
ATOM   681  O O   . TYR A 1 98  ? 3.235   -0.612  -1.535  1.00 18.49 ? 85  TYR A O   1 
ATOM   682  C CB  . TYR A 1 98  ? 5.950   0.505   -3.274  1.00 18.10 ? 85  TYR A CB  1 
ATOM   683  C CG  . TYR A 1 98  ? 4.860   1.202   -4.043  1.00 17.30 ? 85  TYR A CG  1 
ATOM   684  C CD1 . TYR A 1 98  ? 3.972   2.065   -3.409  1.00 16.74 ? 85  TYR A CD1 1 
ATOM   685  C CD2 . TYR A 1 98  ? 4.776   1.078   -5.423  1.00 17.04 ? 85  TYR A CD2 1 
ATOM   686  C CE1 . TYR A 1 98  ? 2.995   2.735   -4.124  1.00 16.91 ? 85  TYR A CE1 1 
ATOM   687  C CE2 . TYR A 1 98  ? 3.799   1.744   -6.152  1.00 16.82 ? 85  TYR A CE2 1 
ATOM   688  C CZ  . TYR A 1 98  ? 2.898   2.563   -5.495  1.00 17.31 ? 85  TYR A CZ  1 
ATOM   689  O OH  . TYR A 1 98  ? 1.916   3.201   -6.199  1.00 18.74 ? 85  TYR A OH  1 
ATOM   690  N N   . TYR A 1 99  ? 4.983   0.060   -0.188  1.00 18.88 ? 86  TYR A N   1 
ATOM   691  C CA  . TYR A 1 99  ? 4.252   0.358   1.063   1.00 19.64 ? 86  TYR A CA  1 
ATOM   692  C C   . TYR A 1 99  ? 4.677   1.708   1.651   1.00 19.28 ? 86  TYR A C   1 
ATOM   693  O O   . TYR A 1 99  ? 5.879   1.869   1.965   1.00 19.15 ? 86  TYR A O   1 
ATOM   694  C CB  . TYR A 1 99  ? 4.626   -0.669  2.122   1.00 20.32 ? 86  TYR A CB  1 
ATOM   695  C CG  . TYR A 1 99  ? 4.064   -2.050  1.937   1.00 21.40 ? 86  TYR A CG  1 
ATOM   696  C CD1 . TYR A 1 99  ? 4.760   -3.017  1.233   1.00 21.31 ? 86  TYR A CD1 1 
ATOM   697  C CD2 . TYR A 1 99  ? 2.864   -2.406  2.532   1.00 22.88 ? 86  TYR A CD2 1 
ATOM   698  C CE1 . TYR A 1 99  ? 4.269   -4.304  1.109   1.00 21.89 ? 86  TYR A CE1 1 
ATOM   699  C CE2 . TYR A 1 99  ? 2.365   -3.695  2.427   1.00 24.12 ? 86  TYR A CE2 1 
ATOM   700  C CZ  . TYR A 1 99  ? 3.071   -4.643  1.712   1.00 23.27 ? 86  TYR A CZ  1 
ATOM   701  O OH  . TYR A 1 99  ? 2.588   -5.913  1.611   1.00 25.96 ? 86  TYR A OH  1 
ATOM   702  N N   . ILE A 1 100 ? 3.721   2.619   1.839   1.00 18.59 ? 87  ILE A N   1 
ATOM   703  C CA  . ILE A 1 100 ? 3.869   3.837   2.687   1.00 18.72 ? 87  ILE A CA  1 
ATOM   704  C C   . ILE A 1 100 ? 3.045   3.589   3.946   1.00 17.77 ? 87  ILE A C   1 
ATOM   705  O O   . ILE A 1 100 ? 1.820   3.803   3.907   1.00 18.08 ? 87  ILE A O   1 
ATOM   706  C CB  . ILE A 1 100 ? 3.443   5.116   1.941   1.00 20.11 ? 87  ILE A CB  1 
ATOM   707  C CG1 . ILE A 1 100 ? 4.379   5.395   0.765   1.00 21.22 ? 87  ILE A CG1 1 
ATOM   708  C CG2 . ILE A 1 100 ? 3.359   6.312   2.891   1.00 20.29 ? 87  ILE A CG2 1 
ATOM   709  C CD1 . ILE A 1 100 ? 3.773   6.279   -0.308  1.00 23.06 ? 87  ILE A CD1 1 
ATOM   710  N N   . VAL A 1 101 ? 3.687   3.066   4.984   1.00 16.87 ? 88  VAL A N   1 
ATOM   711  C CA  . VAL A 1 101 ? 3.000   2.518   6.185   1.00 17.18 ? 88  VAL A CA  1 
ATOM   712  C C   . VAL A 1 101 ? 2.685   3.679   7.133   1.00 17.07 ? 88  VAL A C   1 
ATOM   713  O O   . VAL A 1 101 ? 3.605   4.304   7.651   1.00 17.15 ? 88  VAL A O   1 
ATOM   714  C CB  . VAL A 1 101 ? 3.824   1.403   6.846   1.00 16.06 ? 88  VAL A CB  1 
ATOM   715  C CG1 . VAL A 1 101 ? 3.172   0.890   8.117   1.00 15.62 ? 88  VAL A CG1 1 
ATOM   716  C CG2 . VAL A 1 101 ? 4.082   0.279   5.851   1.00 16.41 ? 88  VAL A CG2 1 
ATOM   717  N N   . GLU A 1 102 ? 1.400   3.945   7.294   1.00 17.48 ? 89  GLU A N   1 
ATOM   718  C CA  . GLU A 1 102 ? 0.829   4.985   8.179   1.00 18.65 ? 89  GLU A CA  1 
ATOM   719  C C   . GLU A 1 102 ? 0.783   4.454   9.614   1.00 18.74 ? 89  GLU A C   1 
ATOM   720  O O   . GLU A 1 102 ? 1.065   5.221   10.551  1.00 19.89 ? 89  GLU A O   1 
ATOM   721  C CB  . GLU A 1 102 ? -0.543  5.321   7.616   1.00 19.24 ? 89  GLU A CB  1 
ATOM   722  C CG  . GLU A 1 102 ? -0.420  6.032   6.298   1.00 20.07 ? 89  GLU A CG  1 
ATOM   723  C CD  . GLU A 1 102 ? 0.163   7.419   6.500   1.00 21.42 ? 89  GLU A CD  1 
ATOM   724  O OE1 . GLU A 1 102 ? -0.593  8.302   6.959   1.00 20.99 ? 89  GLU A OE1 1 
ATOM   725  O OE2 . GLU A 1 102 ? 1.372   7.596   6.261   1.00 22.46 ? 89  GLU A OE2 1 
ATOM   726  N N   . SER A 1 103 ? 0.478   3.170   9.766   1.00 17.77 ? 90  SER A N   1 
ATOM   727  C CA  . SER A 1 103 ? 0.437   2.480   11.072  1.00 18.42 ? 90  SER A CA  1 
ATOM   728  C C   . SER A 1 103 ? 0.585   0.972   10.875  1.00 17.49 ? 90  SER A C   1 
ATOM   729  O O   . SER A 1 103 ? 0.148   0.472   9.840   1.00 17.17 ? 90  SER A O   1 
ATOM   730  C CB  . SER A 1 103 ? -0.843  2.788   11.809  1.00 18.42 ? 90  SER A CB  1 
ATOM   731  O OG  . SER A 1 103 ? -0.800  2.155   13.075  1.00 19.13 ? 90  SER A OG  1 
ATOM   732  N N   . PHE A 1 104 ? 1.177   0.292   11.854  1.00 18.03 ? 91  PHE A N   1 
ATOM   733  C CA  . PHE A 1 104 ? 1.163   -1.188  11.974  1.00 19.32 ? 91  PHE A CA  1 
ATOM   734  C C   . PHE A 1 104 ? 0.855   -1.540  13.429  1.00 21.28 ? 91  PHE A C   1 
ATOM   735  O O   . PHE A 1 104 ? 1.102   -0.716  14.330  1.00 22.95 ? 91  PHE A O   1 
ATOM   736  C CB  . PHE A 1 104 ? 2.475   -1.801  11.477  1.00 18.63 ? 91  PHE A CB  1 
ATOM   737  C CG  . PHE A 1 104 ? 3.696   -1.380  12.248  1.00 17.74 ? 91  PHE A CG  1 
ATOM   738  C CD1 . PHE A 1 104 ? 3.967   -1.911  13.497  1.00 17.59 ? 91  PHE A CD1 1 
ATOM   739  C CD2 . PHE A 1 104 ? 4.575   -0.446  11.728  1.00 18.06 ? 91  PHE A CD2 1 
ATOM   740  C CE1 . PHE A 1 104 ? 5.092   -1.516  14.207  1.00 17.50 ? 91  PHE A CE1 1 
ATOM   741  C CE2 . PHE A 1 104 ? 5.715   -0.072  12.432  1.00 18.13 ? 91  PHE A CE2 1 
ATOM   742  C CZ  . PHE A 1 104 ? 5.964   -0.600  13.675  1.00 17.17 ? 91  PHE A CZ  1 
ATOM   743  N N   . SER A 1 105 ? 0.308   -2.728  13.649  1.00 23.56 ? 92  SER A N   1 
ATOM   744  C CA  . SER A 1 105 ? -0.181  -3.178  14.973  1.00 25.99 ? 92  SER A CA  1 
ATOM   745  C C   . SER A 1 105 ? 0.974   -3.784  15.783  1.00 26.55 ? 92  SER A C   1 
ATOM   746  O O   . SER A 1 105 ? 1.621   -3.063  16.552  1.00 29.19 ? 92  SER A O   1 
ATOM   747  C CB  . SER A 1 105 ? -1.270  -4.168  14.775  1.00 27.75 ? 92  SER A CB  1 
ATOM   748  O OG  . SER A 1 105 ? -0.762  -5.239  13.980  1.00 31.75 ? 92  SER A OG  1 
ATOM   749  N N   . THR A 1 106 ? 1.216   -5.080  15.612  1.00 26.67 ? 93  THR A N   1 
ATOM   750  C CA  . THR A 1 106 ? 1.984   -5.926  16.565  1.00 27.08 ? 93  THR A CA  1 
ATOM   751  C C   . THR A 1 106 ? 3.312   -6.341  15.922  1.00 25.75 ? 93  THR A C   1 
ATOM   752  O O   . THR A 1 106 ? 4.118   -7.008  16.594  1.00 27.60 ? 93  THR A O   1 
ATOM   753  C CB  . THR A 1 106 ? 1.125   -7.122  17.002  1.00 27.56 ? 93  THR A CB  1 
ATOM   754  O OG1 . THR A 1 106 ? 0.655   -7.843  15.860  1.00 26.68 ? 93  THR A OG1 1 
ATOM   755  C CG2 . THR A 1 106 ? -0.068  -6.686  17.822  1.00 27.65 ? 93  THR A CG2 1 
ATOM   756  N N   . TYR A 1 107 ? 3.554   -5.919  14.683  1.00 24.58 ? 94  TYR A N   1 
ATOM   757  C CA  . TYR A 1 107 ? 4.702   -6.387  13.873  1.00 23.47 ? 94  TYR A CA  1 
ATOM   758  C C   . TYR A 1 107 ? 5.177   -5.274  12.938  1.00 23.61 ? 94  TYR A C   1 
ATOM   759  O O   . TYR A 1 107 ? 4.440   -4.893  11.995  1.00 24.97 ? 94  TYR A O   1 
ATOM   760  C CB  . TYR A 1 107 ? 4.338   -7.647  13.086  1.00 21.66 ? 94  TYR A CB  1 
ATOM   761  C CG  . TYR A 1 107 ? 5.530   -8.196  12.358  1.00 20.47 ? 94  TYR A CG  1 
ATOM   762  C CD1 . TYR A 1 107 ? 6.558   -8.797  13.059  1.00 20.40 ? 94  TYR A CD1 1 
ATOM   763  C CD2 . TYR A 1 107 ? 5.674   -8.025  10.996  1.00 20.30 ? 94  TYR A CD2 1 
ATOM   764  C CE1 . TYR A 1 107 ? 7.683   -9.273  12.413  1.00 21.11 ? 94  TYR A CE1 1 
ATOM   765  C CE2 . TYR A 1 107 ? 6.788   -8.501  10.327  1.00 21.02 ? 94  TYR A CE2 1 
ATOM   766  C CZ  . TYR A 1 107 ? 7.790   -9.133  11.039  1.00 21.25 ? 94  TYR A CZ  1 
ATOM   767  O OH  . TYR A 1 107 ? 8.907   -9.566  10.406  1.00 20.77 ? 94  TYR A OH  1 
ATOM   768  N N   . ASP A 1 108 ? 6.381   -4.771  13.190  1.00 22.69 ? 95  ASP A N   1 
ATOM   769  C CA  . ASP A 1 108 ? 7.047   -3.813  12.278  1.00 25.03 ? 95  ASP A CA  1 
ATOM   770  C C   . ASP A 1 108 ? 7.430   -4.570  11.007  1.00 26.60 ? 95  ASP A C   1 
ATOM   771  O O   . ASP A 1 108 ? 8.308   -5.423  11.046  1.00 27.69 ? 95  ASP A O   1 
ATOM   772  C CB  . ASP A 1 108 ? 8.242   -3.126  12.939  1.00 23.85 ? 95  ASP A CB  1 
ATOM   773  C CG  . ASP A 1 108 ? 8.863   -2.080  12.038  1.00 23.07 ? 95  ASP A CG  1 
ATOM   774  O OD1 . ASP A 1 108 ? 8.662   -2.189  10.814  1.00 24.38 ? 95  ASP A OD1 1 
ATOM   775  O OD2 . ASP A 1 108 ? 9.491   -1.148  12.564  1.00 21.81 ? 95  ASP A OD2 1 
ATOM   776  N N   . PRO A 1 109 ? 6.791   -4.276  9.848   1.00 30.30 ? 96  PRO A N   1 
ATOM   777  C CA  . PRO A 1 109 ? 7.039   -5.027  8.614   1.00 31.76 ? 96  PRO A CA  1 
ATOM   778  C C   . PRO A 1 109 ? 8.423   -4.824  7.978   1.00 32.25 ? 96  PRO A C   1 
ATOM   779  O O   . PRO A 1 109 ? 8.782   -5.627  7.146   1.00 36.05 ? 96  PRO A O   1 
ATOM   780  C CB  . PRO A 1 109 ? 5.984   -4.485  7.643   1.00 33.42 ? 96  PRO A CB  1 
ATOM   781  C CG  . PRO A 1 109 ? 5.685   -3.088  8.152   1.00 32.38 ? 96  PRO A CG  1 
ATOM   782  C CD  . PRO A 1 109 ? 5.808   -3.194  9.657   1.00 30.85 ? 96  PRO A CD  1 
ATOM   783  N N   . SER A 1 110 ? 9.152   -3.783  8.386   1.00 30.85 ? 97  SER A N   1 
ATOM   784  C CA  . SER A 1 110 ? 10.537  -3.464  7.948   1.00 31.33 ? 97  SER A CA  1 
ATOM   785  C C   . SER A 1 110 ? 11.580  -4.265  8.748   1.00 33.10 ? 97  SER A C   1 
ATOM   786  O O   . SER A 1 110 ? 12.800  -3.999  8.582   1.00 39.02 ? 97  SER A O   1 
ATOM   787  C CB  . SER A 1 110 ? 10.790  -1.982  8.098   1.00 30.74 ? 97  SER A CB  1 
ATOM   788  O OG  . SER A 1 110 ? 10.872  -1.615  9.473   1.00 29.03 ? 97  SER A OG  1 
ATOM   789  N N   . THR A 1 111 ? 11.143  -5.139  9.654   1.00 30.72 ? 98  THR A N   1 
ATOM   790  C CA  . THR A 1 111 ? 12.030  -6.077  10.375  1.00 30.57 ? 98  THR A CA  1 
ATOM   791  C C   . THR A 1 111 ? 12.623  -7.039  9.340   1.00 32.21 ? 98  THR A C   1 
ATOM   792  O O   . THR A 1 111 ? 11.834  -7.688  8.614   1.00 30.45 ? 98  THR A O   1 
ATOM   793  C CB  . THR A 1 111 ? 11.287  -6.823  11.493  1.00 30.65 ? 98  THR A CB  1 
ATOM   794  O OG1 . THR A 1 111 ? 10.570  -5.899  12.321  1.00 27.83 ? 98  THR A OG1 1 
ATOM   795  C CG2 . THR A 1 111 ? 12.238  -7.644  12.339  1.00 29.10 ? 98  THR A CG2 1 
ATOM   796  N N   . GLY A 1 112 ? 13.956  -7.126  9.289   1.00 35.48 ? 99  GLY A N   1 
ATOM   797  C CA  . GLY A 1 112 ? 14.703  -8.003  8.364   1.00 39.86 ? 99  GLY A CA  1 
ATOM   798  C C   . GLY A 1 112 ? 14.955  -7.339  7.020   1.00 40.76 ? 99  GLY A C   1 
ATOM   799  O O   . GLY A 1 112 ? 15.466  -8.023  6.100   1.00 41.16 ? 99  GLY A O   1 
ATOM   800  N N   . ALA A 1 113 ? 14.579  -6.060  6.908   1.00 41.24 ? 100 ALA A N   1 
ATOM   801  C CA  . ALA A 1 113 ? 14.822  -5.179  5.745   1.00 37.42 ? 100 ALA A CA  1 
ATOM   802  C C   . ALA A 1 113 ? 15.943  -4.213  6.117   1.00 34.33 ? 100 ALA A C   1 
ATOM   803  O O   . ALA A 1 113 ? 16.223  -4.084  7.316   1.00 33.38 ? 100 ALA A O   1 
ATOM   804  C CB  . ALA A 1 113 ? 13.555  -4.450  5.365   1.00 37.64 ? 100 ALA A CB  1 
ATOM   805  N N   . GLN A 1 114 ? 16.545  -3.561  5.123   1.00 34.11 ? 101 GLN A N   1 
ATOM   806  C CA  . GLN A 1 114 ? 17.747  -2.708  5.317   1.00 35.26 ? 101 GLN A CA  1 
ATOM   807  C C   . GLN A 1 114 ? 17.377  -1.236  5.063   1.00 32.44 ? 101 GLN A C   1 
ATOM   808  O O   . GLN A 1 114 ? 16.866  -0.919  3.963   1.00 28.98 ? 101 GLN A O   1 
ATOM   809  C CB  . GLN A 1 114 ? 18.938  -3.214  4.491   1.00 36.13 ? 101 GLN A CB  1 
ATOM   810  C CG  . GLN A 1 114 ? 18.659  -4.419  3.606   1.00 40.10 ? 101 GLN A CG  1 
ATOM   811  C CD  . GLN A 1 114 ? 18.354  -5.729  4.306   1.00 44.33 ? 101 GLN A CD  1 
ATOM   812  O OE1 . GLN A 1 114 ? 17.753  -6.630  3.718   1.00 48.04 ? 101 GLN A OE1 1 
ATOM   813  N NE2 . GLN A 1 114 ? 18.766  -5.865  5.560   1.00 43.42 ? 101 GLN A NE2 1 
ATOM   814  N N   . GLU A 1 115 ? 17.636  -0.396  6.072   1.00 30.83 ? 102 GLU A N   1 
ATOM   815  C CA  . GLU A 1 115 ? 17.188  1.015   6.176   1.00 32.34 ? 102 GLU A CA  1 
ATOM   816  C C   . GLU A 1 115 ? 18.123  1.893   5.346   1.00 32.20 ? 102 GLU A C   1 
ATOM   817  O O   . GLU A 1 115 ? 19.351  1.887   5.622   1.00 37.02 ? 102 GLU A O   1 
ATOM   818  C CB  . GLU A 1 115 ? 17.164  1.458   7.637   1.00 33.84 ? 102 GLU A CB  1 
ATOM   819  C CG  . GLU A 1 115 ? 17.123  2.963   7.819   1.00 35.81 ? 102 GLU A CG  1 
ATOM   820  C CD  . GLU A 1 115 ? 16.689  3.403   9.204   1.00 40.20 ? 102 GLU A CD  1 
ATOM   821  O OE1 . GLU A 1 115 ? 16.423  4.620   9.381   1.00 44.54 ? 102 GLU A OE1 1 
ATOM   822  O OE2 . GLU A 1 115 ? 16.600  2.528   10.104  1.00 44.88 ? 102 GLU A OE2 1 
ATOM   823  N N   . LEU A 1 116 ? 17.561  2.629   4.391   1.00 28.07 ? 103 LEU A N   1 
ATOM   824  C CA  . LEU A 1 116 ? 18.324  3.389   3.374   1.00 27.52 ? 103 LEU A CA  1 
ATOM   825  C C   . LEU A 1 116 ? 18.246  4.892   3.655   1.00 27.55 ? 103 LEU A C   1 
ATOM   826  O O   . LEU A 1 116 ? 18.792  5.664   2.857   1.00 33.83 ? 103 LEU A O   1 
ATOM   827  C CB  . LEU A 1 116 ? 17.745  3.046   2.001   1.00 25.93 ? 103 LEU A CB  1 
ATOM   828  C CG  . LEU A 1 116 ? 17.850  1.569   1.650   1.00 27.86 ? 103 LEU A CG  1 
ATOM   829  C CD1 . LEU A 1 116 ? 17.286  1.281   0.274   1.00 28.29 ? 103 LEU A CD1 1 
ATOM   830  C CD2 . LEU A 1 116 ? 19.296  1.100   1.739   1.00 29.29 ? 103 LEU A CD2 1 
ATOM   831  N N   . GLY A 1 117 ? 17.567  5.309   4.714   1.00 25.21 ? 104 GLY A N   1 
ATOM   832  C CA  . GLY A 1 117 ? 17.426  6.740   5.017   1.00 26.35 ? 104 GLY A CA  1 
ATOM   833  C C   . GLY A 1 117 ? 16.109  7.033   5.683   1.00 27.51 ? 104 GLY A C   1 
ATOM   834  O O   . GLY A 1 117 ? 15.488  6.081   6.179   1.00 29.67 ? 104 GLY A O   1 
ATOM   835  N N   . THR A 1 118 ? 15.724  8.309   5.712   1.00 26.60 ? 105 THR A N   1 
ATOM   836  C CA  . THR A 1 118 ? 14.394  8.775   6.173   1.00 26.74 ? 105 THR A CA  1 
ATOM   837  C C   . THR A 1 118 ? 13.892  9.869   5.227   1.00 26.39 ? 105 THR A C   1 
ATOM   838  O O   . THR A 1 118 ? 14.715  10.514  4.597   1.00 28.02 ? 105 THR A O   1 
ATOM   839  C CB  . THR A 1 118 ? 14.450  9.264   7.619   1.00 24.99 ? 105 THR A CB  1 
ATOM   840  O OG1 . THR A 1 118 ? 15.174  10.480  7.554   1.00 23.90 ? 105 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 118 ? 15.130  8.297   8.555   1.00 26.19 ? 105 THR A CG2 1 
ATOM   842  N N   . VAL A 1 119 ? 12.579  10.043  5.131   1.00 27.46 ? 106 VAL A N   1 
ATOM   843  C CA  . VAL A 1 119 ? 11.937  11.169  4.397   1.00 27.92 ? 106 VAL A CA  1 
ATOM   844  C C   . VAL A 1 119 ? 10.912  11.839  5.325   1.00 29.79 ? 106 VAL A C   1 
ATOM   845  O O   . VAL A 1 119 ? 10.092  11.105  5.953   1.00 30.00 ? 106 VAL A O   1 
ATOM   846  C CB  . VAL A 1 119 ? 11.309  10.687  3.085   1.00 26.90 ? 106 VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 119 ? 10.397  9.491   3.312   1.00 26.44 ? 106 VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 119 ? 10.584  11.814  2.371   1.00 27.14 ? 106 VAL A CG2 1 
ATOM   849  N N   . GLU A 1 120 ? 11.001  13.168  5.453   1.00 30.39 ? 107 GLU A N   1 
ATOM   850  C CA  . GLU A 1 120 ? 10.063  13.999  6.249   1.00 31.81 ? 107 GLU A CA  1 
ATOM   851  C C   . GLU A 1 120 ? 9.006   14.521  5.276   1.00 28.46 ? 107 GLU A C   1 
ATOM   852  O O   . GLU A 1 120 ? 9.378   15.050  4.212   1.00 27.37 ? 107 GLU A O   1 
ATOM   853  C CB  . GLU A 1 120 ? 10.794  15.134  6.971   1.00 40.17 ? 107 GLU A CB  1 
ATOM   854  C CG  . GLU A 1 120 ? 9.863   16.093  7.713   1.00 48.39 ? 107 GLU A CG  1 
ATOM   855  C CD  . GLU A 1 120 ? 10.049  16.191  9.223   1.00 58.05 ? 107 GLU A CD  1 
ATOM   856  O OE1 . GLU A 1 120 ? 11.228  16.236  9.665   1.00 66.59 ? 107 GLU A OE1 1 
ATOM   857  O OE2 . GLU A 1 120 ? 9.016   16.243  9.960   1.00 57.35 ? 107 GLU A OE2 1 
ATOM   858  N N   . THR A 1 121 ? 7.731   14.308  5.590   1.00 25.11 ? 108 THR A N   1 
ATOM   859  C CA  . THR A 1 121 ? 6.593   14.755  4.750   1.00 23.90 ? 108 THR A CA  1 
ATOM   860  C C   . THR A 1 121 ? 5.301   14.563  5.539   1.00 22.16 ? 108 THR A C   1 
ATOM   861  O O   . THR A 1 121 ? 5.272   13.659  6.386   1.00 21.79 ? 108 THR A O   1 
ATOM   862  C CB  . THR A 1 121 ? 6.586   14.007  3.409   1.00 23.97 ? 108 THR A CB  1 
ATOM   863  O OG1 . THR A 1 121 ? 5.503   14.510  2.631   1.00 22.26 ? 108 THR A OG1 1 
ATOM   864  C CG2 . THR A 1 121 ? 6.465   12.506  3.579   1.00 24.69 ? 108 THR A CG2 1 
ATOM   865  N N   . ASP A 1 122 ? 4.282   15.379  5.265   1.00 21.65 ? 109 ASP A N   1 
ATOM   866  C CA  . ASP A 1 122 ? 2.918   15.211  5.827   1.00 21.61 ? 109 ASP A CA  1 
ATOM   867  C C   . ASP A 1 122 ? 3.015   15.134  7.352   1.00 22.63 ? 109 ASP A C   1 
ATOM   868  O O   . ASP A 1 122 ? 2.330   14.283  7.943   1.00 24.65 ? 109 ASP A O   1 
ATOM   869  C CB  . ASP A 1 122 ? 2.260   13.977  5.229   1.00 20.13 ? 109 ASP A CB  1 
ATOM   870  C CG  . ASP A 1 122 ? 2.329   13.960  3.715   1.00 20.22 ? 109 ASP A CG  1 
ATOM   871  O OD1 . ASP A 1 122 ? 1.726   14.861  3.091   1.00 19.64 ? 109 ASP A OD1 1 
ATOM   872  O OD2 . ASP A 1 122 ? 2.974   13.038  3.166   1.00 20.08 ? 109 ASP A OD2 1 
ATOM   873  N N   . ASP A 1 123 ? 3.872   15.985  7.923   1.00 24.45 ? 110 ASP A N   1 
ATOM   874  C CA  . ASP A 1 123 ? 4.118   16.177  9.376   1.00 28.71 ? 110 ASP A CA  1 
ATOM   875  C C   . ASP A 1 123 ? 4.608   14.866  9.983   1.00 27.52 ? 110 ASP A C   1 
ATOM   876  O O   . ASP A 1 123 ? 4.435   14.689  11.180  1.00 27.87 ? 110 ASP A O   1 
ATOM   877  C CB  . ASP A 1 123 ? 2.892   16.770  10.084  1.00 34.95 ? 110 ASP A CB  1 
ATOM   878  C CG  . ASP A 1 123 ? 2.735   18.261  9.820   1.00 39.48 ? 110 ASP A CG  1 
ATOM   879  O OD1 . ASP A 1 123 ? 3.747   18.990  9.938   1.00 45.46 ? 110 ASP A OD1 1 
ATOM   880  O OD2 . ASP A 1 123 ? 1.622   18.682  9.458   1.00 44.46 ? 110 ASP A OD2 1 
ATOM   881  N N   . GLY A 1 124 ? 5.261   14.029  9.177   1.00 26.23 ? 111 GLY A N   1 
ATOM   882  C CA  . GLY A 1 124 ? 5.825   12.740  9.602   1.00 25.93 ? 111 GLY A CA  1 
ATOM   883  C C   . GLY A 1 124 ? 7.291   12.595  9.223   1.00 25.00 ? 111 GLY A C   1 
ATOM   884  O O   . GLY A 1 124 ? 7.772   13.339  8.332   1.00 22.30 ? 111 GLY A O   1 
ATOM   885  N N   . THR A 1 125 ? 7.963   11.670  9.912   1.00 23.66 ? 112 THR A N   1 
ATOM   886  C CA  . THR A 1 125 ? 9.262   11.066  9.547   1.00 24.81 ? 112 THR A CA  1 
ATOM   887  C C   . THR A 1 125 ? 9.022   9.613   9.170   1.00 23.73 ? 112 THR A C   1 
ATOM   888  O O   . THR A 1 125 ? 8.427   8.905   9.986   1.00 24.57 ? 112 THR A O   1 
ATOM   889  C CB  . THR A 1 125 ? 10.252  11.098  10.712  1.00 25.90 ? 112 THR A CB  1 
ATOM   890  O OG1 . THR A 1 125 ? 10.408  12.478  11.040  1.00 28.94 ? 112 THR A OG1 1 
ATOM   891  C CG2 . THR A 1 125 ? 11.580  10.465  10.362  1.00 26.81 ? 112 THR A CG2 1 
ATOM   892  N N   . TYR A 1 126 ? 9.453   9.209   7.979   1.00 23.28 ? 113 TYR A N   1 
ATOM   893  C CA  . TYR A 1 126 ? 9.270   7.831   7.471   1.00 23.55 ? 113 TYR A CA  1 
ATOM   894  C C   . TYR A 1 126 ? 10.640  7.225   7.202   1.00 22.43 ? 113 TYR A C   1 
ATOM   895  O O   . TYR A 1 126 ? 11.446  7.882   6.541   1.00 21.25 ? 113 TYR A O   1 
ATOM   896  C CB  . TYR A 1 126 ? 8.448   7.799   6.183   1.00 23.37 ? 113 TYR A CB  1 
ATOM   897  C CG  . TYR A 1 126 ? 7.001   8.215   6.282   1.00 22.16 ? 113 TYR A CG  1 
ATOM   898  C CD1 . TYR A 1 126 ? 6.647   9.536   6.477   1.00 21.64 ? 113 TYR A CD1 1 
ATOM   899  C CD2 . TYR A 1 126 ? 5.985   7.308   6.018   1.00 20.79 ? 113 TYR A CD2 1 
ATOM   900  C CE1 . TYR A 1 126 ? 5.315   9.932   6.481   1.00 22.02 ? 113 TYR A CE1 1 
ATOM   901  C CE2 . TYR A 1 126 ? 4.654   7.687   6.007   1.00 20.72 ? 113 TYR A CE2 1 
ATOM   902  C CZ  . TYR A 1 126 ? 4.311   9.007   6.247   1.00 21.28 ? 113 TYR A CZ  1 
ATOM   903  O OH  . TYR A 1 126 ? 2.997   9.401   6.241   1.00 20.21 ? 113 TYR A OH  1 
ATOM   904  N N   . LYS A 1 127 ? 10.878  6.019   7.716   1.00 23.47 ? 114 LYS A N   1 
ATOM   905  C CA  . LYS A 1 127 ? 12.136  5.264   7.499   1.00 24.83 ? 114 LYS A CA  1 
ATOM   906  C C   . LYS A 1 127 ? 11.971  4.426   6.227   1.00 23.30 ? 114 LYS A C   1 
ATOM   907  O O   . LYS A 1 127 ? 10.868  3.869   6.001   1.00 21.03 ? 114 LYS A O   1 
ATOM   908  C CB  . LYS A 1 127 ? 12.481  4.466   8.758   1.00 27.22 ? 114 LYS A CB  1 
ATOM   909  C CG  . LYS A 1 127 ? 12.765  5.348   9.967   1.00 31.29 ? 114 LYS A CG  1 
ATOM   910  C CD  . LYS A 1 127 ? 12.780  4.603   11.295  1.00 35.32 ? 114 LYS A CD  1 
ATOM   911  C CE  . LYS A 1 127 ? 14.159  4.180   11.761  1.00 38.62 ? 114 LYS A CE  1 
ATOM   912  N NZ  . LYS A 1 127 ? 14.204  4.090   13.244  1.00 41.22 ? 114 LYS A NZ  1 
ATOM   913  N N   . ILE A 1 128 ? 13.023  4.382   5.415   1.00 21.93 ? 115 ILE A N   1 
ATOM   914  C CA  . ILE A 1 128 ? 13.004  3.803   4.044   1.00 22.45 ? 115 ILE A CA  1 
ATOM   915  C C   . ILE A 1 128 ? 13.761  2.483   4.107   1.00 22.84 ? 115 ILE A C   1 
ATOM   916  O O   . ILE A 1 128 ? 14.867  2.463   4.699   1.00 23.53 ? 115 ILE A O   1 
ATOM   917  C CB  . ILE A 1 128 ? 13.639  4.785   3.043   1.00 24.07 ? 115 ILE A CB  1 
ATOM   918  C CG1 . ILE A 1 128 ? 12.882  6.108   3.017   1.00 24.86 ? 115 ILE A CG1 1 
ATOM   919  C CG2 . ILE A 1 128 ? 13.731  4.185   1.655   1.00 25.46 ? 115 ILE A CG2 1 
ATOM   920  C CD1 . ILE A 1 128 ? 13.644  7.216   2.359   1.00 26.20 ? 115 ILE A CD1 1 
ATOM   921  N N   . TYR A 1 129 ? 13.191  1.423   3.535   1.00 22.05 ? 116 TYR A N   1 
ATOM   922  C CA  . TYR A 1 129 ? 13.807  0.078   3.502   1.00 20.99 ? 116 TYR A CA  1 
ATOM   923  C C   . TYR A 1 129 ? 13.546  -0.585  2.155   1.00 21.76 ? 116 TYR A C   1 
ATOM   924  O O   . TYR A 1 129 ? 12.542  -0.230  1.506   1.00 21.95 ? 116 TYR A O   1 
ATOM   925  C CB  . TYR A 1 129 ? 13.206  -0.818  4.577   1.00 21.34 ? 116 TYR A CB  1 
ATOM   926  C CG  . TYR A 1 129 ? 13.173  -0.261  5.975   1.00 21.26 ? 116 TYR A CG  1 
ATOM   927  C CD1 . TYR A 1 129 ? 12.145  0.577   6.381   1.00 21.15 ? 116 TYR A CD1 1 
ATOM   928  C CD2 . TYR A 1 129 ? 14.107  -0.656  6.923   1.00 20.53 ? 116 TYR A CD2 1 
ATOM   929  C CE1 . TYR A 1 129 ? 12.074  1.054   7.678   1.00 21.06 ? 116 TYR A CE1 1 
ATOM   930  C CE2 . TYR A 1 129 ? 14.043  -0.198  8.227   1.00 20.59 ? 116 TYR A CE2 1 
ATOM   931  C CZ  . TYR A 1 129 ? 13.029  0.668   8.599   1.00 20.64 ? 116 TYR A CZ  1 
ATOM   932  O OH  . TYR A 1 129 ? 12.953  1.134   9.873   1.00 21.26 ? 116 TYR A OH  1 
ATOM   933  N N   . GLN A 1 130 ? 14.411  -1.523  1.760   1.00 22.14 ? 117 GLN A N   1 
ATOM   934  C CA  . GLN A 1 130 ? 14.126  -2.449  0.643   1.00 23.97 ? 117 GLN A CA  1 
ATOM   935  C C   . GLN A 1 130 ? 14.388  -3.878  1.118   1.00 25.00 ? 117 GLN A C   1 
ATOM   936  O O   . GLN A 1 130 ? 15.294  -4.106  1.955   1.00 24.73 ? 117 GLN A O   1 
ATOM   937  C CB  . GLN A 1 130 ? 14.863  -2.055  -0.641  1.00 25.96 ? 117 GLN A CB  1 
ATOM   938  C CG  . GLN A 1 130 ? 16.199  -2.745  -0.853  1.00 28.56 ? 117 GLN A CG  1 
ATOM   939  C CD  . GLN A 1 130 ? 16.086  -4.140  -1.418  1.00 28.99 ? 117 GLN A CD  1 
ATOM   940  O OE1 . GLN A 1 130 ? 16.708  -5.082  -0.927  1.00 28.15 ? 117 GLN A OE1 1 
ATOM   941  N NE2 . GLN A 1 130 ? 15.294  -4.276  -2.466  1.00 30.98 ? 117 GLN A NE2 1 
ATOM   942  N N   . THR A 1 131 ? 13.531  -4.781  0.651   1.00 28.16 ? 118 THR A N   1 
ATOM   943  C CA  . THR A 1 131 ? 13.690  -6.254  0.689   1.00 29.76 ? 118 THR A CA  1 
ATOM   944  C C   . THR A 1 131 ? 13.490  -6.774  -0.729  1.00 28.85 ? 118 THR A C   1 
ATOM   945  O O   . THR A 1 131 ? 13.023  -6.005  -1.600  1.00 24.39 ? 118 THR A O   1 
ATOM   946  C CB  . THR A 1 131 ? 12.627  -6.969  1.539   1.00 33.04 ? 118 THR A CB  1 
ATOM   947  O OG1 . THR A 1 131 ? 11.709  -6.018  2.087   1.00 32.27 ? 118 THR A OG1 1 
ATOM   948  C CG2 . THR A 1 131 ? 13.241  -7.837  2.617   1.00 33.55 ? 118 THR A CG2 1 
ATOM   949  N N   . THR A 1 132 ? 13.795  -8.053  -0.902  1.00 32.20 ? 119 THR A N   1 
ATOM   950  C CA  . THR A 1 132 ? 13.542  -8.856  -2.115  1.00 33.38 ? 119 THR A CA  1 
ATOM   951  C C   . THR A 1 132 ? 12.611  -9.987  -1.683  1.00 34.71 ? 119 THR A C   1 
ATOM   952  O O   . THR A 1 132 ? 12.967  -10.698 -0.736  1.00 33.79 ? 119 THR A O   1 
ATOM   953  C CB  . THR A 1 132 ? 14.868  -9.336  -2.714  1.00 34.63 ? 119 THR A CB  1 
ATOM   954  O OG1 . THR A 1 132 ? 15.770  -8.224  -2.695  1.00 38.99 ? 119 THR A OG1 1 
ATOM   955  C CG2 . THR A 1 132 ? 14.729  -9.878  -4.121  1.00 35.39 ? 119 THR A CG2 1 
ATOM   956  N N   . ARG A 1 133 ? 11.421  -10.066 -2.276  1.00 34.98 ? 120 ARG A N   1 
ATOM   957  C CA  . ARG A 1 133 ? 10.572  -11.274 -2.217  1.00 33.76 ? 120 ARG A CA  1 
ATOM   958  C C   . ARG A 1 133 ? 11.091  -12.200 -3.318  1.00 33.87 ? 120 ARG A C   1 
ATOM   959  O O   . ARG A 1 133 ? 11.290  -11.694 -4.445  1.00 31.24 ? 120 ARG A O   1 
ATOM   960  C CB  . ARG A 1 133 ? 9.100   -10.909 -2.407  1.00 36.04 ? 120 ARG A CB  1 
ATOM   961  C CG  . ARG A 1 133 ? 8.615   -9.804  -1.485  1.00 37.63 ? 120 ARG A CG  1 
ATOM   962  C CD  . ARG A 1 133 ? 8.277   -10.337 -0.119  1.00 39.91 ? 120 ARG A CD  1 
ATOM   963  N NE  . ARG A 1 133 ? 7.092   -11.190 -0.160  1.00 41.99 ? 120 ARG A NE  1 
ATOM   964  C CZ  . ARG A 1 133 ? 7.096   -12.517 -0.006  1.00 45.88 ? 120 ARG A CZ  1 
ATOM   965  N NH1 . ARG A 1 133 ? 8.233   -13.176 0.186   1.00 45.58 ? 120 ARG A NH1 1 
ATOM   966  N NH2 . ARG A 1 133 ? 5.953   -13.186 -0.049  1.00 44.95 ? 120 ARG A NH2 1 
ATOM   967  N N   . GLU A 1 134 ? 11.352  -13.468 -2.984  1.00 34.19 ? 121 GLU A N   1 
ATOM   968  C CA  . GLU A 1 134 ? 11.846  -14.507 -3.925  1.00 37.11 ? 121 GLU A CA  1 
ATOM   969  C C   . GLU A 1 134 ? 10.715  -15.499 -4.166  1.00 35.53 ? 121 GLU A C   1 
ATOM   970  O O   . GLU A 1 134 ? 10.226  -16.057 -3.187  1.00 32.63 ? 121 GLU A O   1 
ATOM   971  C CB  . GLU A 1 134 ? 13.059  -15.250 -3.369  1.00 40.82 ? 121 GLU A CB  1 
ATOM   972  C CG  . GLU A 1 134 ? 14.250  -14.357 -3.083  1.00 46.52 ? 121 GLU A CG  1 
ATOM   973  C CD  . GLU A 1 134 ? 15.492  -15.111 -2.639  1.00 52.73 ? 121 GLU A CD  1 
ATOM   974  O OE1 . GLU A 1 134 ? 16.198  -14.612 -1.739  1.00 58.06 ? 121 GLU A OE1 1 
ATOM   975  O OE2 . GLU A 1 134 ? 15.756  -16.195 -3.200  1.00 59.35 ? 121 GLU A OE2 1 
ATOM   976  N N   . ASN A 1 135 ? 10.317  -15.693 -5.425  1.00 35.81 ? 122 ASN A N   1 
ATOM   977  C CA  . ASN A 1 135 ? 9.298   -16.704 -5.822  1.00 35.16 ? 122 ASN A CA  1 
ATOM   978  C C   . ASN A 1 135 ? 8.041   -16.513 -4.975  1.00 32.74 ? 122 ASN A C   1 
ATOM   979  O O   . ASN A 1 135 ? 7.584   -17.495 -4.390  1.00 35.75 ? 122 ASN A O   1 
ATOM   980  C CB  . ASN A 1 135 ? 9.859   -18.130 -5.712  1.00 35.36 ? 122 ASN A CB  1 
ATOM   981  C CG  . ASN A 1 135 ? 10.939  -18.400 -6.740  1.00 35.24 ? 122 ASN A CG  1 
ATOM   982  O OD1 . ASN A 1 135 ? 10.690  -18.302 -7.945  1.00 37.63 ? 122 ASN A OD1 1 
ATOM   983  N ND2 . ASN A 1 135 ? 12.137  -18.724 -6.280  1.00 32.37 ? 122 ASN A ND2 1 
ATOM   984  N N   . ALA A 1 136 ? 7.505   -15.289 -4.935  1.00 31.90 ? 123 ALA A N   1 
ATOM   985  C CA  . ALA A 1 136 ? 6.305   -14.906 -4.162  1.00 28.56 ? 123 ALA A CA  1 
ATOM   986  C C   . ALA A 1 136 ? 5.182   -14.523 -5.119  1.00 27.93 ? 123 ALA A C   1 
ATOM   987  O O   . ALA A 1 136 ? 5.425   -14.248 -6.290  1.00 29.66 ? 123 ALA A O   1 
ATOM   988  C CB  . ALA A 1 136 ? 6.650   -13.784 -3.222  1.00 28.62 ? 123 ALA A CB  1 
ATOM   989  N N   . PRO A 1 137 ? 3.912   -14.498 -4.657  1.00 26.67 ? 124 PRO A N   1 
ATOM   990  C CA  . PRO A 1 137 ? 2.811   -14.005 -5.476  1.00 26.55 ? 124 PRO A CA  1 
ATOM   991  C C   . PRO A 1 137 ? 3.050   -12.558 -5.906  1.00 26.27 ? 124 PRO A C   1 
ATOM   992  O O   . PRO A 1 137 ? 3.697   -11.830 -5.170  1.00 26.91 ? 124 PRO A O   1 
ATOM   993  C CB  . PRO A 1 137 ? 1.583   -14.069 -4.554  1.00 25.95 ? 124 PRO A CB  1 
ATOM   994  C CG  . PRO A 1 137 ? 1.952   -15.104 -3.512  1.00 25.48 ? 124 PRO A CG  1 
ATOM   995  C CD  . PRO A 1 137 ? 3.452   -14.981 -3.347  1.00 25.97 ? 124 PRO A CD  1 
ATOM   996  N N   . SER A 1 138 ? 2.528   -12.204 -7.082  1.00 25.04 ? 125 SER A N   1 
ATOM   997  C CA  . SER A 1 138 ? 2.642   -10.863 -7.711  1.00 22.53 ? 125 SER A CA  1 
ATOM   998  C C   . SER A 1 138 ? 1.428   -10.639 -8.607  1.00 21.57 ? 125 SER A C   1 
ATOM   999  O O   . SER A 1 138 ? 0.728   -11.605 -8.941  1.00 20.35 ? 125 SER A O   1 
ATOM   1000 C CB  . SER A 1 138 ? 3.916   -10.723 -8.522  1.00 22.51 ? 125 SER A CB  1 
ATOM   1001 O OG  . SER A 1 138 ? 3.649   -10.879 -9.923  1.00 20.76 ? 125 SER A OG  1 
ATOM   1002 N N   . ILE A 1 139 ? 1.247   -9.395  -9.021  1.00 21.85 ? 126 ILE A N   1 
ATOM   1003 C CA  . ILE A 1 139 ? 0.240   -8.977  -10.033 1.00 22.35 ? 126 ILE A CA  1 
ATOM   1004 C C   . ILE A 1 139 ? 0.532   -9.633  -11.393 1.00 22.92 ? 126 ILE A C   1 
ATOM   1005 O O   . ILE A 1 139 ? -0.366  -9.603  -12.251 1.00 25.34 ? 126 ILE A O   1 
ATOM   1006 C CB  . ILE A 1 139 ? 0.206   -7.440  -10.127 1.00 22.62 ? 126 ILE A CB  1 
ATOM   1007 C CG1 . ILE A 1 139 ? 1.557   -6.856  -10.549 1.00 22.74 ? 126 ILE A CG1 1 
ATOM   1008 C CG2 . ILE A 1 139 ? -0.292  -6.825  -8.822  1.00 21.82 ? 126 ILE A CG2 1 
ATOM   1009 C CD1 . ILE A 1 139 ? 1.435   -5.453  -11.112 1.00 23.46 ? 126 ILE A CD1 1 
ATOM   1010 N N   . GLU A 1 140 ? 1.732   -10.167 -11.638 1.00 23.48 ? 127 GLU A N   1 
ATOM   1011 C CA  . GLU A 1 140 ? 2.035   -10.823 -12.944 1.00 22.93 ? 127 GLU A CA  1 
ATOM   1012 C C   . GLU A 1 140 ? 2.447   -12.281 -12.719 1.00 22.39 ? 127 GLU A C   1 
ATOM   1013 O O   . GLU A 1 140 ? 3.006   -12.855 -13.657 1.00 23.12 ? 127 GLU A O   1 
ATOM   1014 C CB  . GLU A 1 140 ? 3.060   -10.023 -13.758 1.00 23.05 ? 127 GLU A CB  1 
ATOM   1015 C CG  . GLU A 1 140 ? 4.408   -9.793  -13.093 1.00 23.00 ? 127 GLU A CG  1 
ATOM   1016 C CD  . GLU A 1 140 ? 5.307   -8.891  -13.935 1.00 24.57 ? 127 GLU A CD  1 
ATOM   1017 O OE1 . GLU A 1 140 ? 4.818   -7.804  -14.360 1.00 23.69 ? 127 GLU A OE1 1 
ATOM   1018 O OE2 . GLU A 1 140 ? 6.486   -9.285  -14.218 1.00 23.95 ? 127 GLU A OE2 1 
ATOM   1019 N N   . GLY A 1 141 ? 2.141   -12.845 -11.542 1.00 21.76 ? 128 GLY A N   1 
ATOM   1020 C CA  . GLY A 1 141 ? 2.371   -14.262 -11.205 1.00 21.97 ? 128 GLY A CA  1 
ATOM   1021 C C   . GLY A 1 141 ? 3.516   -14.448 -10.229 1.00 22.09 ? 128 GLY A C   1 
ATOM   1022 O O   . GLY A 1 141 ? 4.091   -13.445 -9.788  1.00 23.87 ? 128 GLY A O   1 
ATOM   1023 N N   . THR A 1 142 ? 3.817   -15.694 -9.865  1.00 21.60 ? 129 THR A N   1 
ATOM   1024 C CA  . THR A 1 142 ? 4.967   -16.057 -9.003  1.00 21.79 ? 129 THR A CA  1 
ATOM   1025 C C   . THR A 1 142 ? 6.197   -15.397 -9.604  1.00 23.05 ? 129 THR A C   1 
ATOM   1026 O O   . THR A 1 142 ? 6.449   -15.612 -10.807 1.00 24.56 ? 129 THR A O   1 
ATOM   1027 C CB  . THR A 1 142 ? 5.158   -17.573 -8.918  1.00 22.78 ? 129 THR A CB  1 
ATOM   1028 O OG1 . THR A 1 142 ? 3.948   -18.113 -8.386  1.00 20.94 ? 129 THR A OG1 1 
ATOM   1029 C CG2 . THR A 1 142 ? 6.354   -17.963 -8.080  1.00 23.12 ? 129 THR A CG2 1 
ATOM   1030 N N   . ALA A 1 143 ? 6.898   -14.585 -8.821  1.00 23.54 ? 130 ALA A N   1 
ATOM   1031 C CA  . ALA A 1 143 ? 7.992   -13.719 -9.317  1.00 23.13 ? 130 ALA A CA  1 
ATOM   1032 C C   . ALA A 1 143 ? 8.974   -13.422 -8.182  1.00 22.27 ? 130 ALA A C   1 
ATOM   1033 O O   . ALA A 1 143 ? 8.647   -13.703 -7.010  1.00 22.79 ? 130 ALA A O   1 
ATOM   1034 C CB  . ALA A 1 143 ? 7.416   -12.444 -9.894  1.00 23.43 ? 130 ALA A CB  1 
ATOM   1035 N N   . THR A 1 144 ? 10.124  -12.859 -8.532  1.00 20.72 ? 131 THR A N   1 
ATOM   1036 C CA  . THR A 1 144 ? 11.114  -12.329 -7.575  1.00 21.45 ? 131 THR A CA  1 
ATOM   1037 C C   . THR A 1 144 ? 11.238  -10.828 -7.822  1.00 21.73 ? 131 THR A C   1 
ATOM   1038 O O   . THR A 1 144 ? 11.577  -10.454 -8.928  1.00 22.36 ? 131 THR A O   1 
ATOM   1039 C CB  . THR A 1 144 ? 12.429  -13.102 -7.700  1.00 22.07 ? 131 THR A CB  1 
ATOM   1040 O OG1 . THR A 1 144 ? 12.196  -14.417 -7.187  1.00 22.36 ? 131 THR A OG1 1 
ATOM   1041 C CG2 . THR A 1 144 ? 13.564  -12.441 -6.957  1.00 22.22 ? 131 THR A CG2 1 
ATOM   1042 N N   . PHE A 1 145 ? 10.961  -10.006 -6.811  1.00 23.12 ? 132 PHE A N   1 
ATOM   1043 C CA  . PHE A 1 145 ? 10.871  -8.531  -6.930  1.00 22.89 ? 132 PHE A CA  1 
ATOM   1044 C C   . PHE A 1 145 ? 11.360  -7.874  -5.640  1.00 22.97 ? 132 PHE A C   1 
ATOM   1045 O O   . PHE A 1 145 ? 11.427  -8.552  -4.580  1.00 23.34 ? 132 PHE A O   1 
ATOM   1046 C CB  . PHE A 1 145 ? 9.432   -8.102  -7.219  1.00 23.98 ? 132 PHE A CB  1 
ATOM   1047 C CG  . PHE A 1 145 ? 8.377   -8.782  -6.377  1.00 25.13 ? 132 PHE A CG  1 
ATOM   1048 C CD1 . PHE A 1 145 ? 7.830   -9.997  -6.765  1.00 26.25 ? 132 PHE A CD1 1 
ATOM   1049 C CD2 . PHE A 1 145 ? 7.891   -8.189  -5.227  1.00 26.17 ? 132 PHE A CD2 1 
ATOM   1050 C CE1 . PHE A 1 145 ? 6.827   -10.605 -6.023  1.00 27.14 ? 132 PHE A CE1 1 
ATOM   1051 C CE2 . PHE A 1 145 ? 6.901   -8.805  -4.473  1.00 27.36 ? 132 PHE A CE2 1 
ATOM   1052 C CZ  . PHE A 1 145 ? 6.373   -10.013 -4.870  1.00 27.48 ? 132 PHE A CZ  1 
ATOM   1053 N N   . ASN A 1 146 ? 11.681  -6.583  -5.757  1.00 21.55 ? 133 ASN A N   1 
ATOM   1054 C CA  . ASN A 1 146 ? 11.903  -5.651  -4.629  1.00 21.59 ? 133 ASN A CA  1 
ATOM   1055 C C   . ASN A 1 146 ? 10.542  -5.201  -4.101  1.00 19.99 ? 133 ASN A C   1 
ATOM   1056 O O   . ASN A 1 146 ? 9.633   -4.990  -4.935  1.00 20.19 ? 133 ASN A O   1 
ATOM   1057 C CB  . ASN A 1 146 ? 12.738  -4.442  -5.045  1.00 23.33 ? 133 ASN A CB  1 
ATOM   1058 C CG  . ASN A 1 146 ? 14.082  -4.830  -5.622  1.00 26.11 ? 133 ASN A CG  1 
ATOM   1059 O OD1 . ASN A 1 146 ? 14.867  -5.494  -4.949  1.00 27.82 ? 133 ASN A OD1 1 
ATOM   1060 N ND2 . ASN A 1 146 ? 14.340  -4.444  -6.864  1.00 24.55 ? 133 ASN A ND2 1 
ATOM   1061 N N   . GLN A 1 147 ? 10.407  -5.157  -2.774  1.00 19.35 ? 134 GLN A N   1 
ATOM   1062 C CA  . GLN A 1 147 ? 9.470   -4.292  -2.028  1.00 19.69 ? 134 GLN A CA  1 
ATOM   1063 C C   . GLN A 1 147 ? 10.211  -3.066  -1.526  1.00 19.31 ? 134 GLN A C   1 
ATOM   1064 O O   . GLN A 1 147 ? 11.315  -3.253  -0.975  1.00 19.16 ? 134 GLN A O   1 
ATOM   1065 C CB  . GLN A 1 147 ? 8.931   -4.913  -0.746  1.00 20.33 ? 134 GLN A CB  1 
ATOM   1066 C CG  . GLN A 1 147 ? 8.406   -6.308  -0.912  1.00 22.29 ? 134 GLN A CG  1 
ATOM   1067 C CD  . GLN A 1 147 ? 7.913   -6.820  0.419   1.00 23.16 ? 134 GLN A CD  1 
ATOM   1068 O OE1 . GLN A 1 147 ? 8.648   -6.818  1.418   1.00 23.59 ? 134 GLN A OE1 1 
ATOM   1069 N NE2 . GLN A 1 147 ? 6.668   -7.280  0.422   1.00 21.07 ? 134 GLN A NE2 1 
ATOM   1070 N N   . TYR A 1 148 ? 9.568   -1.895  -1.585  1.00 19.92 ? 135 TYR A N   1 
ATOM   1071 C CA  . TYR A 1 148 ? 10.047  -0.652  -0.922  1.00 19.71 ? 135 TYR A CA  1 
ATOM   1072 C C   . TYR A 1 148 ? 9.089   -0.310  0.221   1.00 20.79 ? 135 TYR A C   1 
ATOM   1073 O O   . TYR A 1 148 ? 7.852   -0.563  0.112   1.00 21.35 ? 135 TYR A O   1 
ATOM   1074 C CB  . TYR A 1 148 ? 10.239  0.495   -1.922  1.00 19.01 ? 135 TYR A CB  1 
ATOM   1075 C CG  . TYR A 1 148 ? 11.030  0.146   -3.162  1.00 19.26 ? 135 TYR A CG  1 
ATOM   1076 C CD1 . TYR A 1 148 ? 12.040  -0.814  -3.146  1.00 19.27 ? 135 TYR A CD1 1 
ATOM   1077 C CD2 . TYR A 1 148 ? 10.788  0.802   -4.357  1.00 18.87 ? 135 TYR A CD2 1 
ATOM   1078 C CE1 . TYR A 1 148 ? 12.750  -1.136  -4.290  1.00 18.27 ? 135 TYR A CE1 1 
ATOM   1079 C CE2 . TYR A 1 148 ? 11.486  0.488   -5.510  1.00 19.04 ? 135 TYR A CE2 1 
ATOM   1080 C CZ  . TYR A 1 148 ? 12.476  -0.482  -5.474  1.00 19.07 ? 135 TYR A CZ  1 
ATOM   1081 O OH  . TYR A 1 148 ? 13.182  -0.789  -6.601  1.00 19.54 ? 135 TYR A OH  1 
ATOM   1082 N N   . TRP A 1 149 ? 9.663   0.237   1.294   1.00 20.75 ? 136 TRP A N   1 
ATOM   1083 C CA  . TRP A 1 149 ? 8.951   0.615   2.538   1.00 21.16 ? 136 TRP A CA  1 
ATOM   1084 C C   . TRP A 1 149 ? 9.288   2.065   2.892   1.00 22.19 ? 136 TRP A C   1 
ATOM   1085 O O   . TRP A 1 149 ? 10.482  2.415   2.863   1.00 23.35 ? 136 TRP A O   1 
ATOM   1086 C CB  . TRP A 1 149 ? 9.324   -0.340  3.673   1.00 21.20 ? 136 TRP A CB  1 
ATOM   1087 C CG  . TRP A 1 149 ? 8.982   -1.778  3.421   1.00 21.07 ? 136 TRP A CG  1 
ATOM   1088 C CD1 . TRP A 1 149 ? 9.773   -2.728  2.841   1.00 21.01 ? 136 TRP A CD1 1 
ATOM   1089 C CD2 . TRP A 1 149 ? 7.752   -2.437  3.766   1.00 21.53 ? 136 TRP A CD2 1 
ATOM   1090 N NE1 . TRP A 1 149 ? 9.117   -3.929  2.793   1.00 21.33 ? 136 TRP A NE1 1 
ATOM   1091 C CE2 . TRP A 1 149 ? 7.883   -3.789  3.376   1.00 21.51 ? 136 TRP A CE2 1 
ATOM   1092 C CE3 . TRP A 1 149 ? 6.555   -2.016  4.358   1.00 21.30 ? 136 TRP A CE3 1 
ATOM   1093 C CZ2 . TRP A 1 149 ? 6.842   -4.711  3.523   1.00 21.16 ? 136 TRP A CZ2 1 
ATOM   1094 C CZ3 . TRP A 1 149 ? 5.542   -2.935  4.535   1.00 21.35 ? 136 TRP A CZ3 1 
ATOM   1095 C CH2 . TRP A 1 149 ? 5.680   -4.261  4.112   1.00 21.42 ? 136 TRP A CH2 1 
ATOM   1096 N N   . SER A 1 150 ? 8.263   2.887   3.131   1.00 21.07 ? 137 SER A N   1 
ATOM   1097 C CA  . SER A 1 150 ? 8.332   4.126   3.942   1.00 20.17 ? 137 SER A CA  1 
ATOM   1098 C C   . SER A 1 150 ? 7.459   3.866   5.156   1.00 19.45 ? 137 SER A C   1 
ATOM   1099 O O   . SER A 1 150 ? 6.268   3.629   4.929   1.00 18.98 ? 137 SER A O   1 
ATOM   1100 C CB  . SER A 1 150 ? 7.811   5.331   3.215   1.00 21.65 ? 137 SER A CB  1 
ATOM   1101 O OG  . SER A 1 150 ? 8.820   5.934   2.454   1.00 21.61 ? 137 SER A OG  1 
ATOM   1102 N N   . VAL A 1 151 ? 8.022   3.880   6.362   1.00 17.29 ? 138 VAL A N   1 
ATOM   1103 C CA  . VAL A 1 151 ? 7.282   3.500   7.593   1.00 17.36 ? 138 VAL A CA  1 
ATOM   1104 C C   . VAL A 1 151 ? 7.261   4.720   8.507   1.00 16.99 ? 138 VAL A C   1 
ATOM   1105 O O   . VAL A 1 151 ? 8.327   5.120   8.958   1.00 17.28 ? 138 VAL A O   1 
ATOM   1106 C CB  . VAL A 1 151 ? 7.916   2.271   8.267   1.00 17.47 ? 138 VAL A CB  1 
ATOM   1107 C CG1 . VAL A 1 151 ? 7.154   1.857   9.516   1.00 17.25 ? 138 VAL A CG1 1 
ATOM   1108 C CG2 . VAL A 1 151 ? 8.048   1.109   7.296   1.00 17.40 ? 138 VAL A CG2 1 
ATOM   1109 N N   . ARG A 1 152 ? 6.087   5.301   8.728   1.00 17.06 ? 139 ARG A N   1 
ATOM   1110 C CA  . ARG A 1 152 ? 5.906   6.470   9.624   1.00 17.11 ? 139 ARG A CA  1 
ATOM   1111 C C   . ARG A 1 152 ? 6.441   6.101   11.004  1.00 17.43 ? 139 ARG A C   1 
ATOM   1112 O O   . ARG A 1 152 ? 6.086   5.025   11.488  1.00 16.36 ? 139 ARG A O   1 
ATOM   1113 C CB  . ARG A 1 152 ? 4.435   6.865   9.704   1.00 17.17 ? 139 ARG A CB  1 
ATOM   1114 C CG  . ARG A 1 152 ? 4.225   8.348   9.951   1.00 18.43 ? 139 ARG A CG  1 
ATOM   1115 C CD  . ARG A 1 152 ? 2.765   8.747   9.839   1.00 18.86 ? 139 ARG A CD  1 
ATOM   1116 N NE  . ARG A 1 152 ? 2.524   10.071  10.405  1.00 20.09 ? 139 ARG A NE  1 
ATOM   1117 C CZ  . ARG A 1 152 ? 2.585   11.222  9.736   1.00 21.96 ? 139 ARG A CZ  1 
ATOM   1118 N NH1 . ARG A 1 152 ? 2.887   11.263  8.445   1.00 21.53 ? 139 ARG A NH1 1 
ATOM   1119 N NH2 . ARG A 1 152 ? 2.346   12.353  10.375  1.00 24.45 ? 139 ARG A NH2 1 
ATOM   1120 N N   . THR A 1 153 ? 7.289   6.943   11.601  1.00 18.91 ? 140 THR A N   1 
ATOM   1121 C CA  . THR A 1 153 ? 7.858   6.676   12.947  1.00 20.79 ? 140 THR A CA  1 
ATOM   1122 C C   . THR A 1 153 ? 6.768   6.877   13.998  1.00 21.48 ? 140 THR A C   1 
ATOM   1123 O O   . THR A 1 153 ? 6.790   6.130   15.004  1.00 21.02 ? 140 THR A O   1 
ATOM   1124 C CB  . THR A 1 153 ? 9.078   7.544   13.268  1.00 21.17 ? 140 THR A CB  1 
ATOM   1125 O OG1 . THR A 1 153 ? 8.718   8.906   13.005  1.00 21.08 ? 140 THR A OG1 1 
ATOM   1126 C CG2 . THR A 1 153 ? 10.298  7.096   12.489  1.00 21.65 ? 140 THR A CG2 1 
ATOM   1127 N N   . ASP A 1 154 ? 5.886   7.851   13.775  1.00 22.34 ? 141 ASP A N   1 
ATOM   1128 C CA  . ASP A 1 154 ? 4.719   8.131   14.655  1.00 25.20 ? 141 ASP A CA  1 
ATOM   1129 C C   . ASP A 1 154 ? 3.436   7.669   13.934  1.00 23.71 ? 141 ASP A C   1 
ATOM   1130 O O   . ASP A 1 154 ? 2.999   8.320   12.955  1.00 20.88 ? 141 ASP A O   1 
ATOM   1131 C CB  . ASP A 1 154 ? 4.660   9.606   15.061  1.00 26.90 ? 141 ASP A CB  1 
ATOM   1132 C CG  . ASP A 1 154 ? 3.674   9.879   16.195  1.00 31.17 ? 141 ASP A CG  1 
ATOM   1133 O OD1 . ASP A 1 154 ? 2.939   8.943   16.593  1.00 32.43 ? 141 ASP A OD1 1 
ATOM   1134 O OD2 . ASP A 1 154 ? 3.647   11.036  16.681  1.00 38.38 ? 141 ASP A OD2 1 
ATOM   1135 N N   . HIS A 1 155 ? 2.861   6.571   14.404  1.00 21.96 ? 142 HIS A N   1 
ATOM   1136 C CA  . HIS A 1 155 ? 1.704   5.907   13.750  1.00 23.26 ? 142 HIS A CA  1 
ATOM   1137 C C   . HIS A 1 155 ? 0.487   6.845   13.773  1.00 21.53 ? 142 HIS A C   1 
ATOM   1138 O O   . HIS A 1 155 ? 0.350   7.630   14.721  1.00 23.91 ? 142 HIS A O   1 
ATOM   1139 C CB  . HIS A 1 155 ? 1.412   4.552   14.411  1.00 23.01 ? 142 HIS A CB  1 
ATOM   1140 C CG  . HIS A 1 155 ? 2.510   3.556   14.265  1.00 23.01 ? 142 HIS A CG  1 
ATOM   1141 N ND1 . HIS A 1 155 ? 2.464   2.322   14.898  1.00 23.53 ? 142 HIS A ND1 1 
ATOM   1142 C CD2 . HIS A 1 155 ? 3.680   3.607   13.588  1.00 22.43 ? 142 HIS A CD2 1 
ATOM   1143 C CE1 . HIS A 1 155 ? 3.575   1.659   14.624  1.00 23.99 ? 142 HIS A CE1 1 
ATOM   1144 N NE2 . HIS A 1 155 ? 4.332   2.421   13.810  1.00 23.09 ? 142 HIS A NE2 1 
ATOM   1145 N N   . ARG A 1 156 ? -0.353  6.772   12.749  1.00 20.88 ? 143 ARG A N   1 
ATOM   1146 C CA  . ARG A 1 156 ? -1.613  7.541   12.672  1.00 20.32 ? 143 ARG A CA  1 
ATOM   1147 C C   . ARG A 1 156 ? -2.607  6.826   11.775  1.00 18.83 ? 143 ARG A C   1 
ATOM   1148 O O   . ARG A 1 156 ? -2.192  6.040   10.921  1.00 19.96 ? 143 ARG A O   1 
ATOM   1149 C CB  . ARG A 1 156 ? -1.332  8.942   12.126  1.00 21.20 ? 143 ARG A CB  1 
ATOM   1150 C CG  . ARG A 1 156 ? -0.886  8.960   10.674  1.00 21.07 ? 143 ARG A CG  1 
ATOM   1151 C CD  . ARG A 1 156 ? -0.746  10.381  10.182  1.00 20.68 ? 143 ARG A CD  1 
ATOM   1152 N NE  . ARG A 1 156 ? -0.488  10.355  8.760   1.00 20.15 ? 143 ARG A NE  1 
ATOM   1153 C CZ  . ARG A 1 156 ? -0.384  11.414  7.984   1.00 19.10 ? 143 ARG A CZ  1 
ATOM   1154 N NH1 . ARG A 1 156 ? -0.470  12.630  8.494   1.00 19.36 ? 143 ARG A NH1 1 
ATOM   1155 N NH2 . ARG A 1 156 ? -0.186  11.238  6.690   1.00 18.99 ? 143 ARG A NH2 1 
ATOM   1156 N N   . VAL A 1 157 ? -3.875  7.162   11.955  1.00 20.55 ? 144 VAL A N   1 
ATOM   1157 C CA  . VAL A 1 157 ? -5.009  6.734   11.089  1.00 19.24 ? 144 VAL A CA  1 
ATOM   1158 C C   . VAL A 1 157 ? -5.727  8.006   10.636  1.00 18.42 ? 144 VAL A C   1 
ATOM   1159 O O   . VAL A 1 157 ? -6.587  8.511   11.360  1.00 17.30 ? 144 VAL A O   1 
ATOM   1160 C CB  . VAL A 1 157 ? -5.922  5.727   11.811  1.00 20.17 ? 144 VAL A CB  1 
ATOM   1161 C CG1 . VAL A 1 157 ? -7.108  5.303   10.953  1.00 20.85 ? 144 VAL A CG1 1 
ATOM   1162 C CG2 . VAL A 1 157 ? -5.139  4.493   12.248  1.00 20.46 ? 144 VAL A CG2 1 
ATOM   1163 N N   . GLY A 1 158 ? -5.303  8.527   9.488   1.00 18.20 ? 145 GLY A N   1 
ATOM   1164 C CA  . GLY A 1 158 ? -5.940  9.660   8.807   1.00 18.40 ? 145 GLY A CA  1 
ATOM   1165 C C   . GLY A 1 158 ? -4.941  10.764  8.534   1.00 18.90 ? 145 GLY A C   1 
ATOM   1166 O O   . GLY A 1 158 ? -4.235  11.178  9.453   1.00 18.93 ? 145 GLY A O   1 
ATOM   1167 N N   . GLY A 1 159 ? -4.880  11.216  7.292   1.00 19.60 ? 146 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 159 ? -4.111  12.407  6.922   1.00 20.69 ? 146 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 159 ? -3.820  12.414  5.440   1.00 21.70 ? 146 GLY A C   1 
ATOM   1170 O O   . GLY A 1 159 ? -4.575  11.779  4.681   1.00 20.73 ? 146 GLY A O   1 
ATOM   1171 N N   . THR A 1 160 ? -2.753  13.121  5.069   1.00 23.35 ? 147 THR A N   1 
ATOM   1172 C CA  . THR A 1 160 ? -2.324  13.394  3.680   1.00 23.80 ? 147 THR A CA  1 
ATOM   1173 C C   . THR A 1 160 ? -1.077  12.546  3.428   1.00 22.82 ? 147 THR A C   1 
ATOM   1174 O O   . THR A 1 160 ? -0.198  12.524  4.298   1.00 20.62 ? 147 THR A O   1 
ATOM   1175 C CB  . THR A 1 160 ? -2.143  14.904  3.473   1.00 25.92 ? 147 THR A CB  1 
ATOM   1176 O OG1 . THR A 1 160 ? -3.429  15.524  3.395   1.00 29.66 ? 147 THR A OG1 1 
ATOM   1177 C CG2 . THR A 1 160 ? -1.407  15.255  2.204   1.00 28.32 ? 147 THR A CG2 1 
ATOM   1178 N N   . VAL A 1 161 ? -1.047  11.821  2.312   1.00 22.19 ? 148 VAL A N   1 
ATOM   1179 C CA  . VAL A 1 161 ? 0.169   11.100  1.844   1.00 22.49 ? 148 VAL A CA  1 
ATOM   1180 C C   . VAL A 1 161 ? 0.579   11.691  0.480   1.00 21.10 ? 148 VAL A C   1 
ATOM   1181 O O   . VAL A 1 161 ? -0.124  11.475  -0.539  1.00 19.91 ? 148 VAL A O   1 
ATOM   1182 C CB  . VAL A 1 161 ? -0.042  9.573   1.830   1.00 21.89 ? 148 VAL A CB  1 
ATOM   1183 C CG1 . VAL A 1 161 ? 1.222   8.861   1.372   1.00 22.11 ? 148 VAL A CG1 1 
ATOM   1184 C CG2 . VAL A 1 161 ? -0.474  9.071   3.197   1.00 21.08 ? 148 VAL A CG2 1 
ATOM   1185 N N   . THR A 1 162 ? 1.650   12.485  0.492   1.00 19.60 ? 149 THR A N   1 
ATOM   1186 C CA  . THR A 1 162 ? 2.233   13.111  -0.715  1.00 19.19 ? 149 THR A CA  1 
ATOM   1187 C C   . THR A 1 162 ? 3.153   12.057  -1.327  1.00 18.79 ? 149 THR A C   1 
ATOM   1188 O O   . THR A 1 162 ? 4.323   11.984  -0.921  1.00 17.20 ? 149 THR A O   1 
ATOM   1189 C CB  . THR A 1 162 ? 2.893   14.445  -0.350  1.00 18.47 ? 149 THR A CB  1 
ATOM   1190 O OG1 . THR A 1 162 ? 1.953   15.186  0.432   1.00 18.03 ? 149 THR A OG1 1 
ATOM   1191 C CG2 . THR A 1 162 ? 3.326   15.231  -1.567  1.00 17.89 ? 149 THR A CG2 1 
ATOM   1192 N N   . THR A 1 163 ? 2.607   11.202  -2.190  1.00 19.83 ? 150 THR A N   1 
ATOM   1193 C CA  . THR A 1 163 ? 3.314   9.973   -2.645  1.00 20.84 ? 150 THR A CA  1 
ATOM   1194 C C   . THR A 1 163 ? 4.570   10.388  -3.421  1.00 22.14 ? 150 THR A C   1 
ATOM   1195 O O   . THR A 1 163 ? 5.596   9.661   -3.305  1.00 22.79 ? 150 THR A O   1 
ATOM   1196 C CB  . THR A 1 163 ? 2.382   9.035   -3.412  1.00 19.65 ? 150 THR A CB  1 
ATOM   1197 O OG1 . THR A 1 163 ? 1.938   9.751   -4.558  1.00 18.86 ? 150 THR A OG1 1 
ATOM   1198 C CG2 . THR A 1 163 ? 1.215   8.559   -2.566  1.00 20.41 ? 150 THR A CG2 1 
ATOM   1199 N N   . GLN A 1 164 ? 4.509   11.520  -4.132  1.00 22.45 ? 151 GLN A N   1 
ATOM   1200 C CA  . GLN A 1 164 ? 5.660   12.080  -4.884  1.00 25.17 ? 151 GLN A CA  1 
ATOM   1201 C C   . GLN A 1 164 ? 6.886   12.149  -3.973  1.00 22.54 ? 151 GLN A C   1 
ATOM   1202 O O   . GLN A 1 164 ? 7.940   11.760  -4.439  1.00 20.63 ? 151 GLN A O   1 
ATOM   1203 C CB  . GLN A 1 164 ? 5.372   13.478  -5.440  1.00 30.04 ? 151 GLN A CB  1 
ATOM   1204 C CG  . GLN A 1 164 ? 6.389   13.923  -6.488  1.00 31.58 ? 151 GLN A CG  1 
ATOM   1205 C CD  . GLN A 1 164 ? 6.426   13.000  -7.685  1.00 33.81 ? 151 GLN A CD  1 
ATOM   1206 O OE1 . GLN A 1 164 ? 7.229   12.067  -7.767  1.00 36.14 ? 151 GLN A OE1 1 
ATOM   1207 N NE2 . GLN A 1 164 ? 5.545   13.257  -8.636  1.00 36.26 ? 151 GLN A NE2 1 
ATOM   1208 N N   . ASN A 1 165 ? 6.719   12.589  -2.720  1.00 22.03 ? 152 ASN A N   1 
ATOM   1209 C CA  . ASN A 1 165 ? 7.801   12.711  -1.710  1.00 22.21 ? 152 ASN A CA  1 
ATOM   1210 C C   . ASN A 1 165 ? 8.365   11.333  -1.355  1.00 22.36 ? 152 ASN A C   1 
ATOM   1211 O O   . ASN A 1 165 ? 9.581   11.263  -1.132  1.00 24.59 ? 152 ASN A O   1 
ATOM   1212 C CB  . ASN A 1 165 ? 7.350   13.441  -0.441  1.00 24.61 ? 152 ASN A CB  1 
ATOM   1213 C CG  . ASN A 1 165 ? 7.160   14.926  -0.657  1.00 26.73 ? 152 ASN A CG  1 
ATOM   1214 O OD1 . ASN A 1 165 ? 7.730   15.478  -1.589  1.00 29.41 ? 152 ASN A OD1 1 
ATOM   1215 N ND2 . ASN A 1 165 ? 6.363   15.582  0.178   1.00 26.74 ? 152 ASN A ND2 1 
ATOM   1216 N N   . HIS A 1 166 ? 7.540   10.281  -1.292  1.00 20.66 ? 153 HIS A N   1 
ATOM   1217 C CA  . HIS A 1 166 ? 8.003   8.897   -1.003  1.00 19.62 ? 153 HIS A CA  1 
ATOM   1218 C C   . HIS A 1 166 ? 8.729   8.297   -2.212  1.00 20.25 ? 153 HIS A C   1 
ATOM   1219 O O   . HIS A 1 166 ? 9.735   7.618   -1.985  1.00 21.56 ? 153 HIS A O   1 
ATOM   1220 C CB  . HIS A 1 166 ? 6.850   8.007   -0.547  1.00 18.59 ? 153 HIS A CB  1 
ATOM   1221 C CG  . HIS A 1 166 ? 6.379   8.375   0.808   1.00 17.87 ? 153 HIS A CG  1 
ATOM   1222 N ND1 . HIS A 1 166 ? 7.093   8.044   1.930   1.00 16.95 ? 153 HIS A ND1 1 
ATOM   1223 C CD2 . HIS A 1 166 ? 5.309   9.093   1.218   1.00 17.52 ? 153 HIS A CD2 1 
ATOM   1224 C CE1 . HIS A 1 166 ? 6.476   8.530   2.984   1.00 17.15 ? 153 HIS A CE1 1 
ATOM   1225 N NE2 . HIS A 1 166 ? 5.375   9.175   2.576   1.00 16.81 ? 153 HIS A NE2 1 
ATOM   1226 N N   . PHE A 1 167 ? 8.235   8.520   -3.432  1.00 20.34 ? 154 PHE A N   1 
ATOM   1227 C CA  . PHE A 1 167 ? 8.827   7.991   -4.693  1.00 20.65 ? 154 PHE A CA  1 
ATOM   1228 C C   . PHE A 1 167 ? 10.196  8.642   -4.958  1.00 21.98 ? 154 PHE A C   1 
ATOM   1229 O O   . PHE A 1 167 ? 11.183  7.921   -5.290  1.00 21.00 ? 154 PHE A O   1 
ATOM   1230 C CB  . PHE A 1 167 ? 7.865   8.199   -5.866  1.00 20.40 ? 154 PHE A CB  1 
ATOM   1231 C CG  . PHE A 1 167 ? 6.508   7.551   -5.709  1.00 20.91 ? 154 PHE A CG  1 
ATOM   1232 C CD1 . PHE A 1 167 ? 6.291   6.537   -4.789  1.00 20.73 ? 154 PHE A CD1 1 
ATOM   1233 C CD2 . PHE A 1 167 ? 5.442   7.946   -6.507  1.00 21.27 ? 154 PHE A CD2 1 
ATOM   1234 C CE1 . PHE A 1 167 ? 5.048   5.932   -4.679  1.00 21.06 ? 154 PHE A CE1 1 
ATOM   1235 C CE2 . PHE A 1 167 ? 4.199   7.347   -6.390  1.00 20.79 ? 154 PHE A CE2 1 
ATOM   1236 C CZ  . PHE A 1 167 ? 4.005   6.340   -5.474  1.00 20.96 ? 154 PHE A CZ  1 
ATOM   1237 N N   . ASP A 1 168 ? 10.270  9.962   -4.794  1.00 22.37 ? 155 ASP A N   1 
ATOM   1238 C CA  . ASP A 1 168 ? 11.525  10.741  -4.916  1.00 24.43 ? 155 ASP A CA  1 
ATOM   1239 C C   . ASP A 1 168 ? 12.560  10.233  -3.908  1.00 23.79 ? 155 ASP A C   1 
ATOM   1240 O O   . ASP A 1 168 ? 13.722  10.062  -4.322  1.00 25.51 ? 155 ASP A O   1 
ATOM   1241 C CB  . ASP A 1 168 ? 11.268  12.242  -4.749  1.00 26.21 ? 155 ASP A CB  1 
ATOM   1242 C CG  . ASP A 1 168 ? 10.694  12.852  -6.007  1.00 28.34 ? 155 ASP A CG  1 
ATOM   1243 O OD1 . ASP A 1 168 ? 10.610  12.111  -7.019  1.00 30.62 ? 155 ASP A OD1 1 
ATOM   1244 O OD2 . ASP A 1 168 ? 10.342  14.049  -5.969  1.00 29.16 ? 155 ASP A OD2 1 
ATOM   1245 N N   . ALA A 1 169 ? 12.182  10.046  -2.640  1.00 23.12 ? 156 ALA A N   1 
ATOM   1246 C CA  . ALA A 1 169 ? 13.088  9.545   -1.580  1.00 21.52 ? 156 ALA A CA  1 
ATOM   1247 C C   . ALA A 1 169 ? 13.547  8.133   -1.967  1.00 22.34 ? 156 ALA A C   1 
ATOM   1248 O O   . ALA A 1 169 ? 14.763  7.873   -1.877  1.00 20.40 ? 156 ALA A O   1 
ATOM   1249 C CB  . ALA A 1 169 ? 12.438  9.590   -0.223  1.00 20.49 ? 156 ALA A CB  1 
ATOM   1250 N N   . TRP A 1 170 ? 12.654  7.268   -2.465  1.00 21.95 ? 157 TRP A N   1 
ATOM   1251 C CA  . TRP A 1 170 ? 13.096  5.910   -2.897  1.00 23.51 ? 157 TRP A CA  1 
ATOM   1252 C C   . TRP A 1 170 ? 14.091  6.039   -4.060  1.00 22.80 ? 157 TRP A C   1 
ATOM   1253 O O   . TRP A 1 170 ? 15.179  5.461   -3.983  1.00 21.21 ? 157 TRP A O   1 
ATOM   1254 C CB  . TRP A 1 170 ? 11.917  4.992   -3.251  1.00 23.77 ? 157 TRP A CB  1 
ATOM   1255 C CG  . TRP A 1 170 ? 10.983  4.731   -2.110  1.00 25.41 ? 157 TRP A CG  1 
ATOM   1256 C CD1 . TRP A 1 170 ? 11.260  4.823   -0.775  1.00 27.57 ? 157 TRP A CD1 1 
ATOM   1257 C CD2 . TRP A 1 170 ? 9.600   4.349   -2.203  1.00 25.44 ? 157 TRP A CD2 1 
ATOM   1258 N NE1 . TRP A 1 170 ? 10.140  4.554   -0.034  1.00 28.83 ? 157 TRP A NE1 1 
ATOM   1259 C CE2 . TRP A 1 170 ? 9.111   4.235   -0.883  1.00 27.22 ? 157 TRP A CE2 1 
ATOM   1260 C CE3 . TRP A 1 170 ? 8.730   4.097   -3.268  1.00 23.77 ? 157 TRP A CE3 1 
ATOM   1261 C CZ2 . TRP A 1 170 ? 7.795   3.872   -0.604  1.00 24.81 ? 157 TRP A CZ2 1 
ATOM   1262 C CZ3 . TRP A 1 170 ? 7.431   3.744   -2.988  1.00 24.11 ? 157 TRP A CZ3 1 
ATOM   1263 C CH2 . TRP A 1 170 ? 6.976   3.621   -1.676  1.00 23.92 ? 157 TRP A CH2 1 
ATOM   1264 N N   . LYS A 1 171 ? 13.713  6.775   -5.098  1.00 25.29 ? 158 LYS A N   1 
ATOM   1265 C CA  . LYS A 1 171 ? 14.551  7.046   -6.297  1.00 28.43 ? 158 LYS A CA  1 
ATOM   1266 C C   . LYS A 1 171 ? 15.883  7.660   -5.855  1.00 28.39 ? 158 LYS A C   1 
ATOM   1267 O O   . LYS A 1 171 ? 16.929  7.247   -6.366  1.00 24.14 ? 158 LYS A O   1 
ATOM   1268 C CB  . LYS A 1 171 ? 13.768  7.929   -7.269  1.00 29.35 ? 158 LYS A CB  1 
ATOM   1269 C CG  . LYS A 1 171 ? 12.683  7.171   -8.022  1.00 32.63 ? 158 LYS A CG  1 
ATOM   1270 C CD  . LYS A 1 171 ? 11.600  8.058   -8.579  1.00 37.73 ? 158 LYS A CD  1 
ATOM   1271 C CE  . LYS A 1 171 ? 12.083  8.908   -9.735  1.00 40.90 ? 158 LYS A CE  1 
ATOM   1272 N NZ  . LYS A 1 171 ? 10.937  9.495   -10.468 1.00 42.48 ? 158 LYS A NZ  1 
ATOM   1273 N N   . ASN A 1 172 ? 15.840  8.563   -4.880  1.00 30.58 ? 159 ASN A N   1 
ATOM   1274 C CA  . ASN A 1 172 ? 17.058  9.170   -4.295  1.00 32.50 ? 159 ASN A CA  1 
ATOM   1275 C C   . ASN A 1 172 ? 18.009  8.086   -3.770  1.00 30.31 ? 159 ASN A C   1 
ATOM   1276 O O   . ASN A 1 172 ? 19.221  8.279   -3.910  1.00 30.51 ? 159 ASN A O   1 
ATOM   1277 C CB  . ASN A 1 172 ? 16.714  10.183  -3.207  1.00 35.15 ? 159 ASN A CB  1 
ATOM   1278 C CG  . ASN A 1 172 ? 17.109  11.568  -3.650  1.00 39.84 ? 159 ASN A CG  1 
ATOM   1279 O OD1 . ASN A 1 172 ? 18.302  11.850  -3.754  1.00 44.55 ? 159 ASN A OD1 1 
ATOM   1280 N ND2 . ASN A 1 172 ? 16.129  12.406  -3.956  1.00 41.45 ? 159 ASN A ND2 1 
ATOM   1281 N N   . ALA A 1 173 ? 17.493  7.021   -3.152  1.00 27.24 ? 160 ALA A N   1 
ATOM   1282 C CA  . ALA A 1 173 ? 18.303  5.980   -2.482  1.00 27.69 ? 160 ALA A CA  1 
ATOM   1283 C C   . ALA A 1 173 ? 18.863  4.976   -3.507  1.00 28.05 ? 160 ALA A C   1 
ATOM   1284 O O   . ALA A 1 173 ? 19.637  4.072   -3.107  1.00 28.52 ? 160 ALA A O   1 
ATOM   1285 C CB  . ALA A 1 173 ? 17.466  5.312   -1.424  1.00 27.74 ? 160 ALA A CB  1 
ATOM   1286 N N   . GLY A 1 174 ? 18.498  5.125   -4.782  1.00 27.19 ? 161 GLY A N   1 
ATOM   1287 C CA  . GLY A 1 174 ? 18.889  4.219   -5.877  1.00 28.61 ? 161 GLY A CA  1 
ATOM   1288 C C   . GLY A 1 174 ? 17.850  3.144   -6.139  1.00 30.63 ? 161 GLY A C   1 
ATOM   1289 O O   . GLY A 1 174 ? 18.199  2.132   -6.788  1.00 30.01 ? 161 GLY A O   1 
ATOM   1290 N N   . LEU A 1 175 ? 16.619  3.331   -5.651  1.00 30.25 ? 162 LEU A N   1 
ATOM   1291 C CA  . LEU A 1 175 ? 15.524  2.344   -5.835  1.00 30.60 ? 162 LEU A CA  1 
ATOM   1292 C C   . LEU A 1 175 ? 14.783  2.671   -7.136  1.00 30.92 ? 162 LEU A C   1 
ATOM   1293 O O   . LEU A 1 175 ? 14.152  3.728   -7.203  1.00 31.36 ? 162 LEU A O   1 
ATOM   1294 C CB  . LEU A 1 175 ? 14.604  2.361   -4.609  1.00 28.04 ? 162 LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 175 ? 15.309  2.095   -3.278  1.00 26.96 ? 162 LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 175 ? 14.335  2.125   -2.108  1.00 26.30 ? 162 LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 175 ? 16.054  0.768   -3.311  1.00 27.49 ? 162 LEU A CD2 1 
ATOM   1298 N N   . GLU A 1 176 ? 14.910  1.785   -8.129  1.00 34.15 ? 163 GLU A N   1 
ATOM   1299 C CA  . GLU A 1 176 ? 14.182  1.802   -9.429  1.00 36.10 ? 163 GLU A CA  1 
ATOM   1300 C C   . GLU A 1 176 ? 12.671  1.722   -9.177  1.00 32.76 ? 163 GLU A C   1 
ATOM   1301 O O   . GLU A 1 176 ? 12.257  0.857   -8.380  1.00 29.76 ? 163 GLU A O   1 
ATOM   1302 C CB  . GLU A 1 176 ? 14.574  0.587   -10.276 1.00 42.07 ? 163 GLU A CB  1 
ATOM   1303 C CG  . GLU A 1 176 ? 16.041  0.528   -10.671 1.00 45.87 ? 163 GLU A CG  1 
ATOM   1304 C CD  . GLU A 1 176 ? 16.350  1.198   -11.997 1.00 49.22 ? 163 GLU A CD  1 
ATOM   1305 O OE1 . GLU A 1 176 ? 17.515  1.602   -12.186 1.00 48.67 ? 163 GLU A OE1 1 
ATOM   1306 O OE2 . GLU A 1 176 ? 15.418  1.308   -12.841 1.00 50.84 ? 163 GLU A OE2 1 
ATOM   1307 N N   . MET A 1 177 ? 11.899  2.589   -9.840  1.00 32.73 ? 164 MET A N   1 
ATOM   1308 C CA  . MET A 1 177 ? 10.421  2.494   -10.008 1.00 31.34 ? 164 MET A CA  1 
ATOM   1309 C C   . MET A 1 177 ? 10.105  2.248   -11.486 1.00 27.70 ? 164 MET A C   1 
ATOM   1310 O O   . MET A 1 177 ? 10.623  2.988   -12.319 1.00 27.98 ? 164 MET A O   1 
ATOM   1311 C CB  . MET A 1 177 ? 9.740   3.792   -9.578  1.00 34.08 ? 164 MET A CB  1 
ATOM   1312 C CG  . MET A 1 177 ? 10.099  4.211   -8.173  1.00 39.16 ? 164 MET A CG  1 
ATOM   1313 S SD  . MET A 1 177 ? 9.076   3.380   -6.963  1.00 44.11 ? 164 MET A SD  1 
ATOM   1314 C CE  . MET A 1 177 ? 7.699   4.524   -6.918  1.00 39.64 ? 164 MET A CE  1 
ATOM   1315 N N   . GLY A 1 178 ? 9.279   1.253   -11.801 1.00 24.33 ? 165 GLY A N   1 
ATOM   1316 C CA  . GLY A 1 178 ? 8.846   0.976   -13.180 1.00 23.38 ? 165 GLY A CA  1 
ATOM   1317 C C   . GLY A 1 178 ? 7.571   1.723   -13.498 1.00 22.89 ? 165 GLY A C   1 
ATOM   1318 O O   . GLY A 1 178 ? 7.347   2.773   -12.873 1.00 22.12 ? 165 GLY A O   1 
ATOM   1319 N N   . THR A 1 179 ? 6.769   1.193   -14.427 1.00 22.12 ? 166 THR A N   1 
ATOM   1320 C CA  . THR A 1 179 ? 5.447   1.739   -14.839 1.00 23.20 ? 166 THR A CA  1 
ATOM   1321 C C   . THR A 1 179 ? 4.391   1.419   -13.768 1.00 22.32 ? 166 THR A C   1 
ATOM   1322 O O   . THR A 1 179 ? 4.252   0.239   -13.387 1.00 20.95 ? 166 THR A O   1 
ATOM   1323 C CB  . THR A 1 179 ? 5.023   1.186   -16.202 1.00 24.22 ? 166 THR A CB  1 
ATOM   1324 O OG1 . THR A 1 179 ? 6.155   1.330   -17.057 1.00 29.22 ? 166 THR A OG1 1 
ATOM   1325 C CG2 . THR A 1 179 ? 3.837   1.917   -16.784 1.00 25.78 ? 166 THR A CG2 1 
ATOM   1326 N N   . HIS A 1 180 ? 3.663   2.435   -13.307 1.00 21.83 ? 167 HIS A N   1 
ATOM   1327 C CA  . HIS A 1 180 ? 2.748   2.316   -12.148 1.00 21.86 ? 167 HIS A CA  1 
ATOM   1328 C C   . HIS A 1 180 ? 1.572   1.435   -12.556 1.00 22.26 ? 167 HIS A C   1 
ATOM   1329 O O   . HIS A 1 180 ? 0.883   1.756   -13.536 1.00 22.75 ? 167 HIS A O   1 
ATOM   1330 C CB  . HIS A 1 180 ? 2.349   3.686   -11.602 1.00 22.19 ? 167 HIS A CB  1 
ATOM   1331 C CG  . HIS A 1 180 ? 3.448   4.350   -10.841 1.00 26.01 ? 167 HIS A CG  1 
ATOM   1332 N ND1 . HIS A 1 180 ? 4.715   4.540   -11.382 1.00 29.22 ? 167 HIS A ND1 1 
ATOM   1333 C CD2 . HIS A 1 180 ? 3.493   4.855   -9.591  1.00 27.13 ? 167 HIS A CD2 1 
ATOM   1334 C CE1 . HIS A 1 180 ? 5.478   5.153   -10.500 1.00 29.46 ? 167 HIS A CE1 1 
ATOM   1335 N NE2 . HIS A 1 180 ? 4.752   5.344   -9.387  1.00 28.98 ? 167 HIS A NE2 1 
ATOM   1336 N N   . ASN A 1 181 ? 1.387   0.336   -11.829 1.00 22.46 ? 168 ASN A N   1 
ATOM   1337 C CA  . ASN A 1 181 ? 0.106   -0.404  -11.794 1.00 21.31 ? 168 ASN A CA  1 
ATOM   1338 C C   . ASN A 1 181 ? -0.769  0.277   -10.740 1.00 19.58 ? 168 ASN A C   1 
ATOM   1339 O O   . ASN A 1 181 ? -0.598  1.496   -10.516 1.00 17.74 ? 168 ASN A O   1 
ATOM   1340 C CB  . ASN A 1 181 ? 0.350   -1.888  -11.551 1.00 22.54 ? 168 ASN A CB  1 
ATOM   1341 C CG  . ASN A 1 181 ? -0.733  -2.753  -12.158 1.00 22.52 ? 168 ASN A CG  1 
ATOM   1342 O OD1 . ASN A 1 181 ? -1.848  -2.825  -11.645 1.00 23.82 ? 168 ASN A OD1 1 
ATOM   1343 N ND2 . ASN A 1 181 ? -0.389  -3.427  -13.238 1.00 22.76 ? 168 ASN A ND2 1 
ATOM   1344 N N   . TYR A 1 182 ? -1.648  -0.466  -10.078 1.00 19.52 ? 169 TYR A N   1 
ATOM   1345 C CA  . TYR A 1 182 ? -2.624  0.133   -9.137  1.00 20.25 ? 169 TYR A CA  1 
ATOM   1346 C C   . TYR A 1 182 ? -1.872  0.725   -7.930  1.00 20.61 ? 169 TYR A C   1 
ATOM   1347 O O   . TYR A 1 182 ? -0.714  0.370   -7.700  1.00 19.24 ? 169 TYR A O   1 
ATOM   1348 C CB  . TYR A 1 182 ? -3.732  -0.871  -8.809  1.00 20.34 ? 169 TYR A CB  1 
ATOM   1349 C CG  . TYR A 1 182 ? -3.335  -2.002  -7.908  1.00 19.91 ? 169 TYR A CG  1 
ATOM   1350 C CD1 . TYR A 1 182 ? -3.233  -1.810  -6.540  1.00 19.93 ? 169 TYR A CD1 1 
ATOM   1351 C CD2 . TYR A 1 182 ? -3.069  -3.260  -8.421  1.00 19.74 ? 169 TYR A CD2 1 
ATOM   1352 C CE1 . TYR A 1 182 ? -2.873  -2.844  -5.695  1.00 20.17 ? 169 TYR A CE1 1 
ATOM   1353 C CE2 . TYR A 1 182 ? -2.721  -4.310  -7.587  1.00 20.63 ? 169 TYR A CE2 1 
ATOM   1354 C CZ  . TYR A 1 182 ? -2.612  -4.096  -6.223  1.00 20.51 ? 169 TYR A CZ  1 
ATOM   1355 O OH  . TYR A 1 182 ? -2.263  -5.115  -5.393  1.00 21.80 ? 169 TYR A OH  1 
ATOM   1356 N N   . MET A 1 183 ? -2.518  1.680   -7.254  1.00 20.51 ? 170 MET A N   1 
ATOM   1357 C CA  . MET A 1 183 ? -2.119  2.262   -5.954  1.00 20.80 ? 170 MET A CA  1 
ATOM   1358 C C   . MET A 1 183 ? -3.395  2.472   -5.126  1.00 21.95 ? 170 MET A C   1 
ATOM   1359 O O   . MET A 1 183 ? -4.293  3.190   -5.610  1.00 23.31 ? 170 MET A O   1 
ATOM   1360 C CB  . MET A 1 183 ? -1.412  3.605   -6.133  1.00 20.34 ? 170 MET A CB  1 
ATOM   1361 C CG  . MET A 1 183 ? -1.037  4.237   -4.818  1.00 21.61 ? 170 MET A CG  1 
ATOM   1362 S SD  . MET A 1 183 ? 0.068   5.651   -5.016  1.00 23.37 ? 170 MET A SD  1 
ATOM   1363 C CE  . MET A 1 183 ? -1.068  6.803   -5.781  1.00 23.69 ? 170 MET A CE  1 
ATOM   1364 N N   . ILE A 1 184 ? -3.474  1.859   -3.941  1.00 21.16 ? 171 ILE A N   1 
ATOM   1365 C CA  . ILE A 1 184 ? -4.678  1.885   -3.060  1.00 20.49 ? 171 ILE A CA  1 
ATOM   1366 C C   . ILE A 1 184 ? -4.251  2.274   -1.645  1.00 18.58 ? 171 ILE A C   1 
ATOM   1367 O O   . ILE A 1 184 ? -3.058  2.215   -1.350  1.00 20.64 ? 171 ILE A O   1 
ATOM   1368 C CB  . ILE A 1 184 ? -5.399  0.525   -3.094  1.00 21.12 ? 171 ILE A CB  1 
ATOM   1369 C CG1 . ILE A 1 184 ? -4.446  -0.635  -2.811  1.00 20.90 ? 171 ILE A CG1 1 
ATOM   1370 C CG2 . ILE A 1 184 ? -6.129  0.316   -4.409  1.00 21.28 ? 171 ILE A CG2 1 
ATOM   1371 C CD1 . ILE A 1 184 ? -5.145  -1.884  -2.333  1.00 20.54 ? 171 ILE A CD1 1 
ATOM   1372 N N   . VAL A 1 185 ? -5.183  2.757   -0.842  1.00 17.14 ? 172 VAL A N   1 
ATOM   1373 C CA  . VAL A 1 185 ? -5.027  2.908   0.636   1.00 17.11 ? 172 VAL A CA  1 
ATOM   1374 C C   . VAL A 1 185 ? -5.518  1.583   1.224   1.00 16.72 ? 172 VAL A C   1 
ATOM   1375 O O   . VAL A 1 185 ? -6.762  1.380   1.254   1.00 17.93 ? 172 VAL A O   1 
ATOM   1376 C CB  . VAL A 1 185 ? -5.827  4.105   1.196   1.00 16.50 ? 172 VAL A CB  1 
ATOM   1377 C CG1 . VAL A 1 185 ? -5.618  4.245   2.697   1.00 16.38 ? 172 VAL A CG1 1 
ATOM   1378 C CG2 . VAL A 1 185 ? -5.524  5.410   0.468   1.00 15.36 ? 172 VAL A CG2 1 
ATOM   1379 N N   . ALA A 1 186 ? -4.594  0.695   1.576   1.00 15.81 ? 173 ALA A N   1 
ATOM   1380 C CA  . ALA A 1 186 ? -4.848  -0.741  1.808   1.00 16.35 ? 173 ALA A CA  1 
ATOM   1381 C C   . ALA A 1 186 ? -4.807  -1.061  3.302   1.00 16.95 ? 173 ALA A C   1 
ATOM   1382 O O   . ALA A 1 186 ? -3.873  -0.613  3.988   1.00 16.93 ? 173 ALA A O   1 
ATOM   1383 C CB  . ALA A 1 186 ? -3.846  -1.579  1.053   1.00 17.45 ? 173 ALA A CB  1 
ATOM   1384 N N   . THR A 1 187 ? -5.809  -1.818  3.762   1.00 17.80 ? 174 THR A N   1 
ATOM   1385 C CA  . THR A 1 187 ? -5.783  -2.604  5.012   1.00 18.17 ? 174 THR A CA  1 
ATOM   1386 C C   . THR A 1 187 ? -5.222  -4.007  4.694   1.00 19.21 ? 174 THR A C   1 
ATOM   1387 O O   . THR A 1 187 ? -5.849  -4.744  3.916   1.00 17.34 ? 174 THR A O   1 
ATOM   1388 C CB  . THR A 1 187 ? -7.181  -2.618  5.632   1.00 18.46 ? 174 THR A CB  1 
ATOM   1389 O OG1 . THR A 1 187 ? -7.578  -1.261  5.872   1.00 16.50 ? 174 THR A OG1 1 
ATOM   1390 C CG2 . THR A 1 187 ? -7.247  -3.446  6.904   1.00 18.85 ? 174 THR A CG2 1 
ATOM   1391 N N   . GLU A 1 188 ? -4.065  -4.354  5.263   1.00 19.96 ? 175 GLU A N   1 
ATOM   1392 C CA  . GLU A 1 188 ? -3.478  -5.717  5.167   1.00 22.00 ? 175 GLU A CA  1 
ATOM   1393 C C   . GLU A 1 188 ? -3.526  -6.398  6.546   1.00 21.85 ? 175 GLU A C   1 
ATOM   1394 O O   . GLU A 1 188 ? -3.429  -5.702  7.576   1.00 20.18 ? 175 GLU A O   1 
ATOM   1395 C CB  . GLU A 1 188 ? -2.049  -5.661  4.610   1.00 22.24 ? 175 GLU A CB  1 
ATOM   1396 C CG  . GLU A 1 188 ? -1.391  -7.026  4.505   1.00 23.57 ? 175 GLU A CG  1 
ATOM   1397 C CD  . GLU A 1 188 ? -0.096  -7.087  3.700   1.00 25.39 ? 175 GLU A CD  1 
ATOM   1398 O OE1 . GLU A 1 188 ? 0.507   -8.192  3.627   1.00 24.53 ? 175 GLU A OE1 1 
ATOM   1399 O OE2 . GLU A 1 188 ? 0.311   -6.039  3.145   1.00 27.53 ? 175 GLU A OE2 1 
ATOM   1400 N N   . GLY A 1 189 ? -3.683  -7.719  6.564   1.00 21.10 ? 176 GLY A N   1 
ATOM   1401 C CA  . GLY A 1 189 ? -3.646  -8.489  7.815   1.00 22.61 ? 176 GLY A CA  1 
ATOM   1402 C C   . GLY A 1 189 ? -2.949  -9.814  7.634   1.00 22.42 ? 176 GLY A C   1 
ATOM   1403 O O   . GLY A 1 189 ? -2.906  -10.295 6.505   1.00 22.54 ? 176 GLY A O   1 
ATOM   1404 N N   . TYR A 1 190 ? -2.423  -10.381 8.714   1.00 24.95 ? 177 TYR A N   1 
ATOM   1405 C CA  . TYR A 1 190 ? -1.866  -11.759 8.722   1.00 27.21 ? 177 TYR A CA  1 
ATOM   1406 C C   . TYR A 1 190 ? -2.083  -12.393 10.096  1.00 25.30 ? 177 TYR A C   1 
ATOM   1407 O O   . TYR A 1 190 ? -1.628  -11.841 11.103  1.00 25.49 ? 177 TYR A O   1 
ATOM   1408 C CB  . TYR A 1 190 ? -0.386  -11.798 8.320   1.00 28.72 ? 177 TYR A CB  1 
ATOM   1409 C CG  . TYR A 1 190 ? 0.093   -13.212 8.112   1.00 31.04 ? 177 TYR A CG  1 
ATOM   1410 C CD1 . TYR A 1 190 ? -0.538  -14.034 7.192   1.00 33.16 ? 177 TYR A CD1 1 
ATOM   1411 C CD2 . TYR A 1 190 ? 1.095   -13.766 8.890   1.00 32.65 ? 177 TYR A CD2 1 
ATOM   1412 C CE1 . TYR A 1 190 ? -0.161  -15.354 7.014   1.00 33.81 ? 177 TYR A CE1 1 
ATOM   1413 C CE2 . TYR A 1 190 ? 1.493   -15.084 8.718   1.00 34.23 ? 177 TYR A CE2 1 
ATOM   1414 C CZ  . TYR A 1 190 ? 0.866   -15.880 7.775   1.00 35.89 ? 177 TYR A CZ  1 
ATOM   1415 O OH  . TYR A 1 190 ? 1.226   -17.189 7.610   1.00 39.67 ? 177 TYR A OH  1 
ATOM   1416 N N   . GLN A 1 191 ? -2.776  -13.529 10.122  1.00 25.38 ? 178 GLN A N   1 
ATOM   1417 C CA  . GLN A 1 191 ? -2.997  -14.325 11.352  1.00 24.65 ? 178 GLN A CA  1 
ATOM   1418 C C   . GLN A 1 191 ? -3.507  -13.382 12.440  1.00 24.06 ? 178 GLN A C   1 
ATOM   1419 O O   . GLN A 1 191 ? -2.874  -13.314 13.512  1.00 23.21 ? 178 GLN A O   1 
ATOM   1420 C CB  . GLN A 1 191 ? -1.705  -14.998 11.794  1.00 24.84 ? 178 GLN A CB  1 
ATOM   1421 C CG  . GLN A 1 191 ? -1.274  -16.137 10.892  1.00 26.36 ? 178 GLN A CG  1 
ATOM   1422 C CD  . GLN A 1 191 ? -0.134  -16.885 11.535  1.00 29.08 ? 178 GLN A CD  1 
ATOM   1423 O OE1 . GLN A 1 191 ? 0.618   -16.324 12.334  1.00 34.67 ? 178 GLN A OE1 1 
ATOM   1424 N NE2 . GLN A 1 191 ? -0.006  -18.156 11.202  1.00 29.80 ? 178 GLN A NE2 1 
ATOM   1425 N N   . SER A 1 192 ? -4.579  -12.654 12.129  1.00 22.49 ? 179 SER A N   1 
ATOM   1426 C CA  . SER A 1 192 ? -5.225  -11.662 13.019  1.00 21.55 ? 179 SER A CA  1 
ATOM   1427 C C   . SER A 1 192 ? -6.729  -11.679 12.753  1.00 21.70 ? 179 SER A C   1 
ATOM   1428 O O   . SER A 1 192 ? -7.164  -12.394 11.830  1.00 21.96 ? 179 SER A O   1 
ATOM   1429 C CB  . SER A 1 192 ? -4.646  -10.278 12.837  1.00 21.63 ? 179 SER A CB  1 
ATOM   1430 O OG  . SER A 1 192 ? -4.657  -9.867  11.469  1.00 22.48 ? 179 SER A OG  1 
ATOM   1431 N N   . SER A 1 193 ? -7.461  -10.962 13.601  1.00 20.67 ? 180 SER A N   1 
ATOM   1432 C CA  . SER A 1 193 ? -8.849  -10.488 13.411  1.00 21.01 ? 180 SER A CA  1 
ATOM   1433 C C   . SER A 1 193 ? -8.840  -8.960  13.465  1.00 20.78 ? 180 SER A C   1 
ATOM   1434 O O   . SER A 1 193 ? -7.837  -8.361  13.901  1.00 20.61 ? 180 SER A O   1 
ATOM   1435 C CB  . SER A 1 193 ? -9.767  -11.041 14.480  1.00 21.19 ? 180 SER A CB  1 
ATOM   1436 O OG  . SER A 1 193 ? -9.649  -12.448 14.563  1.00 21.28 ? 180 SER A OG  1 
ATOM   1437 N N   . GLY A 1 194 ? -9.942  -8.347  13.073  1.00 20.93 ? 181 GLY A N   1 
ATOM   1438 C CA  . GLY A 1 194 ? -10.103 -6.891  13.183  1.00 20.60 ? 181 GLY A CA  1 
ATOM   1439 C C   . GLY A 1 194 ? -11.219 -6.395  12.300  1.00 19.68 ? 181 GLY A C   1 
ATOM   1440 O O   . GLY A 1 194 ? -11.881 -7.198  11.635  1.00 19.21 ? 181 GLY A O   1 
ATOM   1441 N N   . SER A 1 195 ? -11.442 -5.094  12.336  1.00 20.22 ? 182 SER A N   1 
ATOM   1442 C CA  . SER A 1 195 ? -12.254 -4.377  11.334  1.00 20.04 ? 182 SER A CA  1 
ATOM   1443 C C   . SER A 1 195 ? -11.550 -3.057  11.045  1.00 19.75 ? 182 SER A C   1 
ATOM   1444 O O   . SER A 1 195 ? -10.682 -2.643  11.822  1.00 20.59 ? 182 SER A O   1 
ATOM   1445 C CB  . SER A 1 195 ? -13.672 -4.192  11.788  1.00 19.29 ? 182 SER A CB  1 
ATOM   1446 O OG  . SER A 1 195 ? -13.707 -3.395  12.947  1.00 19.81 ? 182 SER A OG  1 
ATOM   1447 N N   . ALA A 1 196 ? -11.858 -2.484  9.905   1.00 19.36 ? 183 ALA A N   1 
ATOM   1448 C CA  . ALA A 1 196 ? -11.320 -1.196  9.455   1.00 20.13 ? 183 ALA A CA  1 
ATOM   1449 C C   . ALA A 1 196 ? -12.395 -0.591  8.573   1.00 19.90 ? 183 ALA A C   1 
ATOM   1450 O O   . ALA A 1 196 ? -13.095 -1.370  7.891   1.00 20.08 ? 183 ALA A O   1 
ATOM   1451 C CB  . ALA A 1 196 ? -10.018 -1.401  8.709   1.00 20.73 ? 183 ALA A CB  1 
ATOM   1452 N N   . SER A 1 197 ? -12.555 0.721   8.618   1.00 19.22 ? 184 SER A N   1 
ATOM   1453 C CA  . SER A 1 197 ? -13.484 1.418   7.703   1.00 20.72 ? 184 SER A CA  1 
ATOM   1454 C C   . SER A 1 197 ? -12.810 2.702   7.259   1.00 20.51 ? 184 SER A C   1 
ATOM   1455 O O   . SER A 1 197 ? -12.631 3.573   8.113   1.00 20.68 ? 184 SER A O   1 
ATOM   1456 C CB  . SER A 1 197 ? -14.818 1.665   8.360   1.00 21.74 ? 184 SER A CB  1 
ATOM   1457 O OG  . SER A 1 197 ? -15.687 2.251   7.415   1.00 25.98 ? 184 SER A OG  1 
ATOM   1458 N N   . ILE A 1 198 ? -12.410 2.769   5.992   1.00 21.99 ? 185 ILE A N   1 
ATOM   1459 C CA  . ILE A 1 198 ? -11.434 3.774   5.475   1.00 22.88 ? 185 ILE A CA  1 
ATOM   1460 C C   . ILE A 1 198 ? -12.072 4.474   4.276   1.00 21.97 ? 185 ILE A C   1 
ATOM   1461 O O   . ILE A 1 198 ? -12.655 3.766   3.433   1.00 22.14 ? 185 ILE A O   1 
ATOM   1462 C CB  . ILE A 1 198 ? -10.091 3.096   5.114   1.00 24.10 ? 185 ILE A CB  1 
ATOM   1463 C CG1 . ILE A 1 198 ? -9.429  2.453   6.329   1.00 24.09 ? 185 ILE A CG1 1 
ATOM   1464 C CG2 . ILE A 1 198 ? -9.148  4.084   4.436   1.00 24.15 ? 185 ILE A CG2 1 
ATOM   1465 C CD1 . ILE A 1 198 ? -8.726  3.457   7.246   1.00 25.23 ? 185 ILE A CD1 1 
ATOM   1466 N N   . THR A 1 199 ? -11.961 5.802   4.208   1.00 19.93 ? 186 THR A N   1 
ATOM   1467 C CA  . THR A 1 199 ? -12.425 6.624   3.060   1.00 19.87 ? 186 THR A CA  1 
ATOM   1468 C C   . THR A 1 199 ? -11.223 7.305   2.400   1.00 20.28 ? 186 THR A C   1 
ATOM   1469 O O   . THR A 1 199 ? -10.574 8.119   3.074   1.00 19.30 ? 186 THR A O   1 
ATOM   1470 C CB  . THR A 1 199 ? -13.432 7.706   3.474   1.00 19.19 ? 186 THR A CB  1 
ATOM   1471 O OG1 . THR A 1 199 ? -14.502 7.064   4.165   1.00 17.82 ? 186 THR A OG1 1 
ATOM   1472 C CG2 . THR A 1 199 ? -13.933 8.506   2.289   1.00 18.26 ? 186 THR A CG2 1 
ATOM   1473 N N   . VAL A 1 200 ? -10.969 6.962   1.133   1.00 21.26 ? 187 VAL A N   1 
ATOM   1474 C CA  . VAL A 1 200 ? -10.096 7.703   0.170   1.00 21.22 ? 187 VAL A CA  1 
ATOM   1475 C C   . VAL A 1 200 ? -10.888 8.923   -0.322  1.00 21.97 ? 187 VAL A C   1 
ATOM   1476 O O   . VAL A 1 200 ? -11.952 8.707   -0.934  1.00 21.85 ? 187 VAL A O   1 
ATOM   1477 C CB  . VAL A 1 200 ? -9.673  6.788   -1.003  1.00 20.55 ? 187 VAL A CB  1 
ATOM   1478 C CG1 . VAL A 1 200 ? -8.558  7.412   -1.816  1.00 20.69 ? 187 VAL A CG1 1 
ATOM   1479 C CG2 . VAL A 1 200 ? -9.256  5.397   -0.544  1.00 20.44 ? 187 VAL A CG2 1 
ATOM   1480 N N   . GLN A 1 201 ? -10.427 10.150  -0.042  1.00 24.54 ? 188 GLN A N   1 
ATOM   1481 C CA  . GLN A 1 201 ? -11.141 11.411  -0.419  1.00 26.68 ? 188 GLN A CA  1 
ATOM   1482 C C   . GLN A 1 201 ? -10.806 11.739  -1.881  1.00 26.10 ? 188 GLN A C   1 
ATOM   1483 O O   . GLN A 1 201 ? -9.900  11.098  -2.422  1.00 23.93 ? 188 GLN A O   1 
ATOM   1484 C CB  . GLN A 1 201 ? -10.782 12.619  0.461   1.00 28.23 ? 188 GLN A CB  1 
ATOM   1485 C CG  . GLN A 1 201 ? -10.694 12.340  1.958   1.00 29.71 ? 188 GLN A CG  1 
ATOM   1486 C CD  . GLN A 1 201 ? -12.002 11.936  2.597   1.00 32.85 ? 188 GLN A CD  1 
ATOM   1487 O OE1 . GLN A 1 201 ? -13.097 12.258  2.121   1.00 32.67 ? 188 GLN A OE1 1 
ATOM   1488 N NE2 . GLN A 1 201 ? -11.887 11.250  3.723   1.00 33.32 ? 188 GLN A NE2 1 
ATOM   1489 N N   . GLU B 1 13  ? 21.275  -15.103 29.755  1.00 47.06 ? 0   GLU B N   1 
ATOM   1490 C CA  . GLU B 1 13  ? 20.547  -14.702 28.517  1.00 46.25 ? 0   GLU B CA  1 
ATOM   1491 C C   . GLU B 1 13  ? 21.199  -15.347 27.289  1.00 44.95 ? 0   GLU B C   1 
ATOM   1492 O O   . GLU B 1 13  ? 22.391  -15.134 27.074  1.00 42.99 ? 0   GLU B O   1 
ATOM   1493 C CB  . GLU B 1 13  ? 20.547  -13.185 28.357  1.00 47.27 ? 0   GLU B CB  1 
ATOM   1494 C CG  . GLU B 1 13  ? 19.965  -12.459 29.550  1.00 52.17 ? 0   GLU B CG  1 
ATOM   1495 C CD  . GLU B 1 13  ? 19.664  -10.989 29.305  1.00 56.17 ? 0   GLU B CD  1 
ATOM   1496 O OE1 . GLU B 1 13  ? 20.279  -10.406 28.392  1.00 57.28 ? 0   GLU B OE1 1 
ATOM   1497 O OE2 . GLU B 1 13  ? 18.809  -10.431 30.024  1.00 61.96 ? 0   GLU B OE2 1 
ATOM   1498 N N   . ILE B 1 14  ? 20.433  -16.103 26.505  1.00 47.76 ? 1   ILE B N   1 
ATOM   1499 C CA  . ILE B 1 14  ? 20.887  -16.652 25.194  1.00 46.91 ? 1   ILE B CA  1 
ATOM   1500 C C   . ILE B 1 14  ? 19.971  -16.100 24.086  1.00 47.22 ? 1   ILE B C   1 
ATOM   1501 O O   . ILE B 1 14  ? 18.785  -15.815 24.363  1.00 43.98 ? 1   ILE B O   1 
ATOM   1502 C CB  . ILE B 1 14  ? 20.962  -18.194 25.236  1.00 46.73 ? 1   ILE B CB  1 
ATOM   1503 C CG1 . ILE B 1 14  ? 19.595  -18.859 25.413  1.00 45.03 ? 1   ILE B CG1 1 
ATOM   1504 C CG2 . ILE B 1 14  ? 21.939  -18.649 26.313  1.00 46.27 ? 1   ILE B CG2 1 
ATOM   1505 C CD1 . ILE B 1 14  ? 19.620  -20.358 25.183  1.00 44.79 ? 1   ILE B CD1 1 
ATOM   1506 N N   . THR B 1 15  ? 20.540  -15.927 22.888  1.00 47.70 ? 2   THR B N   1 
ATOM   1507 C CA  . THR B 1 15  ? 19.970  -15.196 21.723  1.00 43.76 ? 2   THR B CA  1 
ATOM   1508 C C   . THR B 1 15  ? 19.698  -16.173 20.572  1.00 41.42 ? 2   THR B C   1 
ATOM   1509 O O   . THR B 1 15  ? 18.953  -15.776 19.640  1.00 40.73 ? 2   THR B O   1 
ATOM   1510 C CB  . THR B 1 15  ? 20.904  -14.037 21.341  1.00 45.30 ? 2   THR B CB  1 
ATOM   1511 O OG1 . THR B 1 15  ? 20.207  -12.857 21.734  1.00 48.30 ? 2   THR B OG1 1 
ATOM   1512 C CG2 . THR B 1 15  ? 21.270  -13.941 19.873  1.00 47.09 ? 2   THR B CG2 1 
ATOM   1513 N N   . SER B 1 16  ? 20.275  -17.382 20.618  1.00 35.47 ? 3   SER B N   1 
ATOM   1514 C CA  . SER B 1 16  ? 20.090  -18.417 19.568  1.00 35.11 ? 3   SER B CA  1 
ATOM   1515 C C   . SER B 1 16  ? 19.735  -19.768 20.195  1.00 31.49 ? 3   SER B C   1 
ATOM   1516 O O   . SER B 1 16  ? 19.916  -19.945 21.412  1.00 29.16 ? 3   SER B O   1 
ATOM   1517 C CB  . SER B 1 16  ? 21.292  -18.514 18.649  1.00 35.19 ? 3   SER B CB  1 
ATOM   1518 O OG  . SER B 1 16  ? 22.485  -18.673 19.385  1.00 32.53 ? 3   SER B OG  1 
ATOM   1519 N N   . SER B 1 17  ? 19.207  -20.658 19.355  1.00 30.59 ? 4   SER B N   1 
ATOM   1520 C CA  . SER B 1 17  ? 18.638  -21.984 19.702  1.00 28.53 ? 4   SER B CA  1 
ATOM   1521 C C   . SER B 1 17  ? 19.648  -22.785 20.524  1.00 30.20 ? 4   SER B C   1 
ATOM   1522 O O   . SER B 1 17  ? 20.853  -22.608 20.330  1.00 29.56 ? 4   SER B O   1 
ATOM   1523 C CB  . SER B 1 17  ? 18.231  -22.717 18.464  1.00 25.83 ? 4   SER B CB  1 
ATOM   1524 O OG  . SER B 1 17  ? 17.467  -21.866 17.623  1.00 24.43 ? 4   SER B OG  1 
ATOM   1525 N N   . GLU B 1 18  ? 19.142  -23.635 21.408  1.00 32.32 ? 5   GLU B N   1 
ATOM   1526 C CA  . GLU B 1 18  ? 19.930  -24.347 22.436  1.00 33.16 ? 5   GLU B CA  1 
ATOM   1527 C C   . GLU B 1 18  ? 18.938  -25.159 23.268  1.00 31.49 ? 5   GLU B C   1 
ATOM   1528 O O   . GLU B 1 18  ? 17.918  -24.580 23.667  1.00 31.23 ? 5   GLU B O   1 
ATOM   1529 C CB  . GLU B 1 18  ? 20.718  -23.330 23.266  1.00 36.21 ? 5   GLU B CB  1 
ATOM   1530 C CG  . GLU B 1 18  ? 21.198  -23.858 24.604  1.00 39.12 ? 5   GLU B CG  1 
ATOM   1531 C CD  . GLU B 1 18  ? 22.027  -22.896 25.440  1.00 38.69 ? 5   GLU B CD  1 
ATOM   1532 O OE1 . GLU B 1 18  ? 21.954  -22.994 26.685  1.00 37.06 ? 5   GLU B OE1 1 
ATOM   1533 O OE2 . GLU B 1 18  ? 22.752  -22.062 24.852  1.00 38.13 ? 5   GLU B OE2 1 
ATOM   1534 N N   . THR B 1 19  ? 19.220  -26.449 23.461  1.00 28.72 ? 6   THR B N   1 
ATOM   1535 C CA  . THR B 1 19  ? 18.498  -27.377 24.368  1.00 28.23 ? 6   THR B CA  1 
ATOM   1536 C C   . THR B 1 19  ? 19.470  -27.881 25.452  1.00 28.41 ? 6   THR B C   1 
ATOM   1537 O O   . THR B 1 19  ? 20.685  -28.009 25.183  1.00 29.53 ? 6   THR B O   1 
ATOM   1538 C CB  . THR B 1 19  ? 17.908  -28.550 23.581  1.00 27.69 ? 6   THR B CB  1 
ATOM   1539 O OG1 . THR B 1 19  ? 19.017  -29.372 23.232  1.00 26.92 ? 6   THR B OG1 1 
ATOM   1540 C CG2 . THR B 1 19  ? 17.149  -28.136 22.340  1.00 26.89 ? 6   THR B CG2 1 
ATOM   1541 N N   . GLY B 1 20  ? 18.973  -28.161 26.652  1.00 27.36 ? 7   GLY B N   1 
ATOM   1542 C CA  . GLY B 1 20  ? 19.828  -28.623 27.760  1.00 25.67 ? 7   GLY B CA  1 
ATOM   1543 C C   . GLY B 1 20  ? 18.998  -29.017 28.955  1.00 25.04 ? 7   GLY B C   1 
ATOM   1544 O O   . GLY B 1 20  ? 17.778  -29.182 28.799  1.00 25.84 ? 7   GLY B O   1 
ATOM   1545 N N   . THR B 1 21  ? 19.648  -29.164 30.105  1.00 25.20 ? 8   THR B N   1 
ATOM   1546 C CA  . THR B 1 21  ? 19.016  -29.423 31.420  1.00 25.55 ? 8   THR B CA  1 
ATOM   1547 C C   . THR B 1 21  ? 19.419  -28.252 32.316  1.00 25.52 ? 8   THR B C   1 
ATOM   1548 O O   . THR B 1 21  ? 20.529  -27.770 32.153  1.00 29.34 ? 8   THR B O   1 
ATOM   1549 C CB  . THR B 1 21  ? 19.379  -30.829 31.919  1.00 25.91 ? 8   THR B CB  1 
ATOM   1550 O OG1 . THR B 1 21  ? 20.794  -30.941 32.009  1.00 27.04 ? 8   THR B OG1 1 
ATOM   1551 C CG2 . THR B 1 21  ? 18.910  -31.934 30.993  1.00 27.00 ? 8   THR B CG2 1 
ATOM   1552 N N   . ASN B 1 22  ? 18.516  -27.763 33.156  1.00 25.89 ? 9   ASN B N   1 
ATOM   1553 C CA  . ASN B 1 22  ? 18.751  -26.605 34.053  1.00 27.05 ? 9   ASN B CA  1 
ATOM   1554 C C   . ASN B 1 22  ? 17.889  -26.796 35.294  1.00 27.99 ? 9   ASN B C   1 
ATOM   1555 O O   . ASN B 1 22  ? 16.670  -26.842 35.129  1.00 32.76 ? 9   ASN B O   1 
ATOM   1556 C CB  . ASN B 1 22  ? 18.433  -25.291 33.339  1.00 27.08 ? 9   ASN B CB  1 
ATOM   1557 C CG  . ASN B 1 22  ? 18.572  -24.081 34.232  1.00 25.46 ? 9   ASN B CG  1 
ATOM   1558 O OD1 . ASN B 1 22  ? 17.647  -23.728 34.957  1.00 23.58 ? 9   ASN B OD1 1 
ATOM   1559 N ND2 . ASN B 1 22  ? 19.718  -23.430 34.162  1.00 24.57 ? 9   ASN B ND2 1 
ATOM   1560 N N   . ASN B 1 23  ? 18.505  -26.971 36.463  1.00 29.19 ? 10  ASN B N   1 
ATOM   1561 C CA  . ASN B 1 23  ? 17.803  -27.144 37.767  1.00 30.18 ? 10  ASN B CA  1 
ATOM   1562 C C   . ASN B 1 23  ? 16.867  -28.360 37.726  1.00 28.55 ? 10  ASN B C   1 
ATOM   1563 O O   . ASN B 1 23  ? 15.798  -28.309 38.341  1.00 30.16 ? 10  ASN B O   1 
ATOM   1564 C CB  . ASN B 1 23  ? 17.047  -25.872 38.149  1.00 32.41 ? 10  ASN B CB  1 
ATOM   1565 C CG  . ASN B 1 23  ? 17.929  -24.641 38.070  1.00 36.00 ? 10  ASN B CG  1 
ATOM   1566 O OD1 . ASN B 1 23  ? 19.124  -24.701 38.359  1.00 35.95 ? 10  ASN B OD1 1 
ATOM   1567 N ND2 . ASN B 1 23  ? 17.353  -23.517 37.679  1.00 39.25 ? 10  ASN B ND2 1 
ATOM   1568 N N   . GLY B 1 24  ? 17.269  -29.434 37.055  1.00 29.35 ? 11  GLY B N   1 
ATOM   1569 C CA  . GLY B 1 24  ? 16.519  -30.704 37.053  1.00 30.15 ? 11  GLY B CA  1 
ATOM   1570 C C   . GLY B 1 24  ? 15.428  -30.725 35.991  1.00 31.23 ? 11  GLY B C   1 
ATOM   1571 O O   . GLY B 1 24  ? 14.616  -31.663 36.014  1.00 31.51 ? 11  GLY B O   1 
ATOM   1572 N N   . TYR B 1 25  ? 15.402  -29.731 35.096  1.00 29.13 ? 12  TYR B N   1 
ATOM   1573 C CA  . TYR B 1 25  ? 14.387  -29.598 34.024  1.00 27.83 ? 12  TYR B CA  1 
ATOM   1574 C C   . TYR B 1 25  ? 15.108  -29.568 32.684  1.00 25.72 ? 12  TYR B C   1 
ATOM   1575 O O   . TYR B 1 25  ? 16.059  -28.814 32.534  1.00 27.07 ? 12  TYR B O   1 
ATOM   1576 C CB  . TYR B 1 25  ? 13.540  -28.330 34.206  1.00 28.40 ? 12  TYR B CB  1 
ATOM   1577 C CG  . TYR B 1 25  ? 12.610  -28.372 35.391  1.00 28.15 ? 12  TYR B CG  1 
ATOM   1578 C CD1 . TYR B 1 25  ? 13.039  -27.979 36.644  1.00 27.19 ? 12  TYR B CD1 1 
ATOM   1579 C CD2 . TYR B 1 25  ? 11.309  -28.835 35.269  1.00 30.84 ? 12  TYR B CD2 1 
ATOM   1580 C CE1 . TYR B 1 25  ? 12.207  -28.039 37.747  1.00 27.97 ? 12  TYR B CE1 1 
ATOM   1581 C CE2 . TYR B 1 25  ? 10.458  -28.906 36.363  1.00 30.35 ? 12  TYR B CE2 1 
ATOM   1582 C CZ  . TYR B 1 25  ? 10.911  -28.506 37.610  1.00 30.85 ? 12  TYR B CZ  1 
ATOM   1583 O OH  . TYR B 1 25  ? 10.081  -28.551 38.697  1.00 32.85 ? 12  TYR B OH  1 
ATOM   1584 N N   . TYR B 1 26  ? 14.640  -30.356 31.727  1.00 24.71 ? 13  TYR B N   1 
ATOM   1585 C CA  . TYR B 1 26  ? 14.950  -30.137 30.300  1.00 24.02 ? 13  TYR B CA  1 
ATOM   1586 C C   . TYR B 1 26  ? 14.455  -28.738 29.954  1.00 22.78 ? 13  TYR B C   1 
ATOM   1587 O O   . TYR B 1 26  ? 13.419  -28.312 30.486  1.00 23.45 ? 13  TYR B O   1 
ATOM   1588 C CB  . TYR B 1 26  ? 14.276  -31.195 29.431  1.00 25.38 ? 13  TYR B CB  1 
ATOM   1589 C CG  . TYR B 1 26  ? 14.504  -31.032 27.951  1.00 26.06 ? 13  TYR B CG  1 
ATOM   1590 C CD1 . TYR B 1 26  ? 15.755  -31.253 27.382  1.00 25.03 ? 13  TYR B CD1 1 
ATOM   1591 C CD2 . TYR B 1 26  ? 13.447  -30.686 27.120  1.00 26.11 ? 13  TYR B CD2 1 
ATOM   1592 C CE1 . TYR B 1 26  ? 15.944  -31.134 26.012  1.00 26.66 ? 13  TYR B CE1 1 
ATOM   1593 C CE2 . TYR B 1 26  ? 13.625  -30.547 25.754  1.00 27.20 ? 13  TYR B CE2 1 
ATOM   1594 C CZ  . TYR B 1 26  ? 14.874  -30.773 25.202  1.00 28.05 ? 13  TYR B CZ  1 
ATOM   1595 O OH  . TYR B 1 26  ? 15.013  -30.603 23.856  1.00 31.91 ? 13  TYR B OH  1 
ATOM   1596 N N   . TYR B 1 27  ? 15.205  -28.020 29.141  1.00 21.62 ? 14  TYR B N   1 
ATOM   1597 C CA  . TYR B 1 27  ? 14.752  -26.747 28.536  1.00 22.21 ? 14  TYR B CA  1 
ATOM   1598 C C   . TYR B 1 27  ? 15.055  -26.817 27.040  1.00 21.11 ? 14  TYR B C   1 
ATOM   1599 O O   . TYR B 1 27  ? 15.906  -27.612 26.610  1.00 21.49 ? 14  TYR B O   1 
ATOM   1600 C CB  . TYR B 1 27  ? 15.387  -25.542 29.225  1.00 22.91 ? 14  TYR B CB  1 
ATOM   1601 C CG  . TYR B 1 27  ? 16.841  -25.378 28.893  1.00 24.63 ? 14  TYR B CG  1 
ATOM   1602 C CD1 . TYR B 1 27  ? 17.232  -24.738 27.728  1.00 26.12 ? 14  TYR B CD1 1 
ATOM   1603 C CD2 . TYR B 1 27  ? 17.825  -25.908 29.718  1.00 25.45 ? 14  TYR B CD2 1 
ATOM   1604 C CE1 . TYR B 1 27  ? 18.573  -24.606 27.407  1.00 26.83 ? 14  TYR B CE1 1 
ATOM   1605 C CE2 . TYR B 1 27  ? 19.168  -25.778 29.416  1.00 25.25 ? 14  TYR B CE2 1 
ATOM   1606 C CZ  . TYR B 1 27  ? 19.538  -25.127 28.254  1.00 26.31 ? 14  TYR B CZ  1 
ATOM   1607 O OH  . TYR B 1 27  ? 20.854  -25.005 27.932  1.00 28.96 ? 14  TYR B OH  1 
ATOM   1608 N N   . SER B 1 28  ? 14.285  -26.068 26.269  1.00 20.28 ? 15  SER B N   1 
ATOM   1609 C CA  . SER B 1 28  ? 14.363  -25.997 24.794  1.00 20.77 ? 15  SER B CA  1 
ATOM   1610 C C   . SER B 1 28  ? 14.015  -24.564 24.393  1.00 20.55 ? 15  SER B C   1 
ATOM   1611 O O   . SER B 1 28  ? 12.918  -24.105 24.736  1.00 18.73 ? 15  SER B O   1 
ATOM   1612 C CB  . SER B 1 28  ? 13.462  -27.012 24.155  1.00 20.99 ? 15  SER B CB  1 
ATOM   1613 O OG  . SER B 1 28  ? 13.761  -27.161 22.778  1.00 21.93 ? 15  SER B OG  1 
ATOM   1614 N N   . PHE B 1 29  ? 14.989  -23.862 23.818  1.00 21.56 ? 16  PHE B N   1 
ATOM   1615 C CA  . PHE B 1 29  ? 14.824  -22.547 23.157  1.00 21.47 ? 16  PHE B CA  1 
ATOM   1616 C C   . PHE B 1 29  ? 15.184  -22.737 21.685  1.00 21.79 ? 16  PHE B C   1 
ATOM   1617 O O   . PHE B 1 29  ? 16.322  -23.052 21.380  1.00 25.21 ? 16  PHE B O   1 
ATOM   1618 C CB  . PHE B 1 29  ? 15.665  -21.485 23.862  1.00 20.54 ? 16  PHE B CB  1 
ATOM   1619 C CG  . PHE B 1 29  ? 15.714  -20.179 23.123  1.00 21.35 ? 16  PHE B CG  1 
ATOM   1620 C CD1 . PHE B 1 29  ? 14.558  -19.447 22.925  1.00 21.22 ? 16  PHE B CD1 1 
ATOM   1621 C CD2 . PHE B 1 29  ? 16.903  -19.706 22.585  1.00 21.93 ? 16  PHE B CD2 1 
ATOM   1622 C CE1 . PHE B 1 29  ? 14.585  -18.268 22.202  1.00 21.32 ? 16  PHE B CE1 1 
ATOM   1623 C CE2 . PHE B 1 29  ? 16.935  -18.510 21.885  1.00 22.19 ? 16  PHE B CE2 1 
ATOM   1624 C CZ  . PHE B 1 29  ? 15.773  -17.798 21.687  1.00 22.18 ? 16  PHE B CZ  1 
ATOM   1625 N N   . TRP B 1 30  ? 14.196  -22.618 20.817  1.00 23.06 ? 17  TRP B N   1 
ATOM   1626 C CA  . TRP B 1 30  ? 14.349  -22.578 19.345  1.00 24.39 ? 17  TRP B CA  1 
ATOM   1627 C C   . TRP B 1 30  ? 13.825  -21.232 18.838  1.00 24.28 ? 17  TRP B C   1 
ATOM   1628 O O   . TRP B 1 30  ? 12.718  -20.826 19.256  1.00 22.30 ? 17  TRP B O   1 
ATOM   1629 C CB  . TRP B 1 30  ? 13.601  -23.746 18.696  1.00 26.43 ? 17  TRP B CB  1 
ATOM   1630 C CG  . TRP B 1 30  ? 13.646  -23.697 17.202  1.00 30.40 ? 17  TRP B CG  1 
ATOM   1631 C CD1 . TRP B 1 30  ? 14.675  -24.087 16.400  1.00 31.61 ? 17  TRP B CD1 1 
ATOM   1632 C CD2 . TRP B 1 30  ? 12.615  -23.213 16.319  1.00 33.27 ? 17  TRP B CD2 1 
ATOM   1633 N NE1 . TRP B 1 30  ? 14.356  -23.892 15.083  1.00 32.70 ? 17  TRP B NE1 1 
ATOM   1634 C CE2 . TRP B 1 30  ? 13.100  -23.357 14.999  1.00 33.85 ? 17  TRP B CE2 1 
ATOM   1635 C CE3 . TRP B 1 30  ? 11.329  -22.696 16.511  1.00 31.71 ? 17  TRP B CE3 1 
ATOM   1636 C CZ2 . TRP B 1 30  ? 12.349  -22.992 13.880  1.00 33.75 ? 17  TRP B CZ2 1 
ATOM   1637 C CZ3 . TRP B 1 30  ? 10.593  -22.325 15.406  1.00 34.30 ? 17  TRP B CZ3 1 
ATOM   1638 C CH2 . TRP B 1 30  ? 11.096  -22.471 14.109  1.00 33.77 ? 17  TRP B CH2 1 
ATOM   1639 N N   . THR B 1 31  ? 14.594  -20.565 17.977  1.00 24.54 ? 18  THR B N   1 
ATOM   1640 C CA  . THR B 1 31  ? 14.161  -19.354 17.229  1.00 24.95 ? 18  THR B CA  1 
ATOM   1641 C C   . THR B 1 31  ? 14.673  -19.478 15.793  1.00 25.73 ? 18  THR B C   1 
ATOM   1642 O O   . THR B 1 31  ? 15.834  -19.896 15.627  1.00 29.60 ? 18  THR B O   1 
ATOM   1643 C CB  . THR B 1 31  ? 14.655  -18.080 17.920  1.00 25.06 ? 18  THR B CB  1 
ATOM   1644 O OG1 . THR B 1 31  ? 14.340  -16.966 17.090  1.00 26.15 ? 18  THR B OG1 1 
ATOM   1645 C CG2 . THR B 1 31  ? 16.146  -18.077 18.181  1.00 26.46 ? 18  THR B CG2 1 
ATOM   1646 N N   . ASP B 1 32  ? 13.861  -19.139 14.793  1.00 24.19 ? 19  ASP B N   1 
ATOM   1647 C CA  . ASP B 1 32  ? 14.312  -19.129 13.374  1.00 24.31 ? 19  ASP B CA  1 
ATOM   1648 C C   . ASP B 1 32  ? 15.193  -17.895 13.106  1.00 24.38 ? 19  ASP B C   1 
ATOM   1649 O O   . ASP B 1 32  ? 15.484  -17.645 11.942  1.00 23.92 ? 19  ASP B O   1 
ATOM   1650 C CB  . ASP B 1 32  ? 13.128  -19.157 12.407  1.00 22.91 ? 19  ASP B CB  1 
ATOM   1651 C CG  . ASP B 1 32  ? 12.254  -17.920 12.525  1.00 21.83 ? 19  ASP B CG  1 
ATOM   1652 O OD1 . ASP B 1 32  ? 12.735  -16.923 13.132  1.00 22.24 ? 19  ASP B OD1 1 
ATOM   1653 O OD2 . ASP B 1 32  ? 11.111  -17.962 12.024  1.00 19.07 ? 19  ASP B OD2 1 
ATOM   1654 N N   . GLY B 1 33  ? 15.553  -17.113 14.126  1.00 25.34 ? 20  GLY B N   1 
ATOM   1655 C CA  . GLY B 1 33  ? 16.493  -15.979 13.980  1.00 25.28 ? 20  GLY B CA  1 
ATOM   1656 C C   . GLY B 1 33  ? 15.810  -14.662 13.628  1.00 23.61 ? 20  GLY B C   1 
ATOM   1657 O O   . GLY B 1 33  ? 16.490  -13.630 13.693  1.00 23.26 ? 20  GLY B O   1 
ATOM   1658 N N   . GLY B 1 34  ? 14.518  -14.682 13.283  1.00 23.06 ? 21  GLY B N   1 
ATOM   1659 C CA  . GLY B 1 34  ? 13.736  -13.467 12.993  1.00 23.46 ? 21  GLY B CA  1 
ATOM   1660 C C   . GLY B 1 34  ? 13.703  -12.511 14.182  1.00 24.10 ? 21  GLY B C   1 
ATOM   1661 O O   . GLY B 1 34  ? 13.505  -12.973 15.338  1.00 23.22 ? 21  GLY B O   1 
ATOM   1662 N N   . GLY B 1 35  ? 13.850  -11.214 13.924  1.00 24.56 ? 22  GLY B N   1 
ATOM   1663 C CA  . GLY B 1 35  ? 13.839  -10.185 14.981  1.00 26.82 ? 22  GLY B CA  1 
ATOM   1664 C C   . GLY B 1 35  ? 14.794  -10.544 16.103  1.00 28.33 ? 22  GLY B C   1 
ATOM   1665 O O   . GLY B 1 35  ? 15.861  -11.156 15.813  1.00 27.73 ? 22  GLY B O   1 
ATOM   1666 N N   . GLN B 1 36  ? 14.439  -10.198 17.343  1.00 30.72 ? 23  GLN B N   1 
ATOM   1667 C CA  . GLN B 1 36  ? 15.283  -10.520 18.521  1.00 33.28 ? 23  GLN B CA  1 
ATOM   1668 C C   . GLN B 1 36  ? 14.453  -11.258 19.570  1.00 30.10 ? 23  GLN B C   1 
ATOM   1669 O O   . GLN B 1 36  ? 13.450  -10.690 20.064  1.00 29.21 ? 23  GLN B O   1 
ATOM   1670 C CB  . GLN B 1 36  ? 15.976  -9.283  19.101  1.00 38.30 ? 23  GLN B CB  1 
ATOM   1671 C CG  . GLN B 1 36  ? 17.402  -9.620  19.543  1.00 46.79 ? 23  GLN B CG  1 
ATOM   1672 C CD  . GLN B 1 36  ? 18.089  -8.589  20.405  1.00 52.87 ? 23  GLN B CD  1 
ATOM   1673 O OE1 . GLN B 1 36  ? 17.571  -7.500  20.648  1.00 57.35 ? 23  GLN B OE1 1 
ATOM   1674 N NE2 . GLN B 1 36  ? 19.280  -8.937  20.874  1.00 55.97 ? 23  GLN B NE2 1 
ATOM   1675 N N   . VAL B 1 37  ? 14.894  -12.471 19.902  1.00 27.50 ? 24  VAL B N   1 
ATOM   1676 C CA  . VAL B 1 37  ? 14.351  -13.304 21.013  1.00 27.11 ? 24  VAL B CA  1 
ATOM   1677 C C   . VAL B 1 37  ? 15.486  -13.569 22.001  1.00 25.40 ? 24  VAL B C   1 
ATOM   1678 O O   . VAL B 1 37  ? 16.549  -14.021 21.564  1.00 23.76 ? 24  VAL B O   1 
ATOM   1679 C CB  . VAL B 1 37  ? 13.736  -14.611 20.487  1.00 27.93 ? 24  VAL B CB  1 
ATOM   1680 C CG1 . VAL B 1 37  ? 12.942  -15.313 21.573  1.00 30.22 ? 24  VAL B CG1 1 
ATOM   1681 C CG2 . VAL B 1 37  ? 12.860  -14.374 19.265  1.00 27.65 ? 24  VAL B CG2 1 
ATOM   1682 N N   . THR B 1 38  ? 15.273  -13.230 23.275  1.00 25.77 ? 25  THR B N   1 
ATOM   1683 C CA  . THR B 1 38  ? 16.185  -13.540 24.408  1.00 25.87 ? 25  THR B CA  1 
ATOM   1684 C C   . THR B 1 38  ? 15.511  -14.517 25.374  1.00 24.91 ? 25  THR B C   1 
ATOM   1685 O O   . THR B 1 38  ? 14.352  -14.259 25.785  1.00 23.79 ? 25  THR B O   1 
ATOM   1686 C CB  . THR B 1 38  ? 16.598  -12.294 25.195  1.00 26.80 ? 25  THR B CB  1 
ATOM   1687 O OG1 . THR B 1 38  ? 17.007  -11.325 24.232  1.00 27.03 ? 25  THR B OG1 1 
ATOM   1688 C CG2 . THR B 1 38  ? 17.712  -12.592 26.176  1.00 26.97 ? 25  THR B CG2 1 
ATOM   1689 N N   . TYR B 1 39  ? 16.228  -15.582 25.717  1.00 23.53 ? 26  TYR B N   1 
ATOM   1690 C CA  . TYR B 1 39  ? 15.789  -16.652 26.643  1.00 23.83 ? 26  TYR B CA  1 
ATOM   1691 C C   . TYR B 1 39  ? 16.735  -16.664 27.850  1.00 24.62 ? 26  TYR B C   1 
ATOM   1692 O O   . TYR B 1 39  ? 17.973  -16.605 27.653  1.00 25.02 ? 26  TYR B O   1 
ATOM   1693 C CB  . TYR B 1 39  ? 15.743  -17.997 25.915  1.00 22.93 ? 26  TYR B CB  1 
ATOM   1694 C CG  . TYR B 1 39  ? 15.382  -19.175 26.788  1.00 23.86 ? 26  TYR B CG  1 
ATOM   1695 C CD1 . TYR B 1 39  ? 16.353  -19.866 27.494  1.00 23.46 ? 26  TYR B CD1 1 
ATOM   1696 C CD2 . TYR B 1 39  ? 14.073  -19.604 26.919  1.00 23.53 ? 26  TYR B CD2 1 
ATOM   1697 C CE1 . TYR B 1 39  ? 16.039  -20.940 28.308  1.00 22.62 ? 26  TYR B CE1 1 
ATOM   1698 C CE2 . TYR B 1 39  ? 13.742  -20.683 27.727  1.00 23.05 ? 26  TYR B CE2 1 
ATOM   1699 C CZ  . TYR B 1 39  ? 14.728  -21.358 28.429  1.00 22.51 ? 26  TYR B CZ  1 
ATOM   1700 O OH  . TYR B 1 39  ? 14.432  -22.423 29.239  1.00 19.65 ? 26  TYR B OH  1 
ATOM   1701 N N   . THR B 1 40  ? 16.158  -16.728 29.052  1.00 24.25 ? 27  THR B N   1 
ATOM   1702 C CA  . THR B 1 40  ? 16.865  -16.967 30.339  1.00 25.27 ? 27  THR B CA  1 
ATOM   1703 C C   . THR B 1 40  ? 16.269  -18.189 31.060  1.00 23.53 ? 27  THR B C   1 
ATOM   1704 O O   . THR B 1 40  ? 15.046  -18.291 31.208  1.00 21.97 ? 27  THR B O   1 
ATOM   1705 C CB  . THR B 1 40  ? 16.780  -15.719 31.220  1.00 26.96 ? 27  THR B CB  1 
ATOM   1706 O OG1 . THR B 1 40  ? 17.155  -14.640 30.367  1.00 29.74 ? 27  THR B OG1 1 
ATOM   1707 C CG2 . THR B 1 40  ? 17.683  -15.772 32.432  1.00 27.75 ? 27  THR B CG2 1 
ATOM   1708 N N   . ASN B 1 41  ? 17.119  -19.111 31.471  1.00 22.13 ? 28  ASN B N   1 
ATOM   1709 C CA  . ASN B 1 41  ? 16.763  -20.102 32.507  1.00 22.15 ? 28  ASN B CA  1 
ATOM   1710 C C   . ASN B 1 41  ? 16.763  -19.374 33.849  1.00 23.07 ? 28  ASN B C   1 
ATOM   1711 O O   . ASN B 1 41  ? 17.714  -18.615 34.093  1.00 23.90 ? 28  ASN B O   1 
ATOM   1712 C CB  . ASN B 1 41  ? 17.745  -21.266 32.530  1.00 21.35 ? 28  ASN B CB  1 
ATOM   1713 C CG  . ASN B 1 41  ? 17.463  -22.263 31.442  1.00 20.11 ? 28  ASN B CG  1 
ATOM   1714 O OD1 . ASN B 1 41  ? 16.310  -22.559 31.182  1.00 22.09 ? 28  ASN B OD1 1 
ATOM   1715 N ND2 . ASN B 1 41  ? 18.496  -22.797 30.827  1.00 20.61 ? 28  ASN B ND2 1 
ATOM   1716 N N   . GLY B 1 42  ? 15.721  -19.575 34.651  1.00 23.19 ? 29  GLY B N   1 
ATOM   1717 C CA  . GLY B 1 42  ? 15.645  -19.098 36.042  1.00 23.10 ? 29  GLY B CA  1 
ATOM   1718 C C   . GLY B 1 42  ? 15.794  -20.273 37.001  1.00 23.70 ? 29  GLY B C   1 
ATOM   1719 O O   . GLY B 1 42  ? 16.050  -21.392 36.574  1.00 22.46 ? 29  GLY B O   1 
ATOM   1720 N N   . PRO B 1 43  ? 15.646  -20.059 38.323  1.00 25.53 ? 30  PRO B N   1 
ATOM   1721 C CA  . PRO B 1 43  ? 15.732  -21.155 39.286  1.00 27.12 ? 30  PRO B CA  1 
ATOM   1722 C C   . PRO B 1 43  ? 14.609  -22.177 39.075  1.00 27.79 ? 30  PRO B C   1 
ATOM   1723 O O   . PRO B 1 43  ? 13.560  -21.799 38.566  1.00 27.40 ? 30  PRO B O   1 
ATOM   1724 C CB  . PRO B 1 43  ? 15.574  -20.481 40.662  1.00 28.29 ? 30  PRO B CB  1 
ATOM   1725 C CG  . PRO B 1 43  ? 14.946  -19.127 40.358  1.00 28.30 ? 30  PRO B CG  1 
ATOM   1726 C CD  . PRO B 1 43  ? 15.406  -18.758 38.961  1.00 26.91 ? 30  PRO B CD  1 
ATOM   1727 N N   . ALA B 1 44  ? 14.856  -23.432 39.460  1.00 26.13 ? 31  ALA B N   1 
ATOM   1728 C CA  . ALA B 1 44  ? 13.839  -24.506 39.467  1.00 25.06 ? 31  ALA B CA  1 
ATOM   1729 C C   . ALA B 1 44  ? 13.252  -24.620 38.052  1.00 23.60 ? 31  ALA B C   1 
ATOM   1730 O O   . ALA B 1 44  ? 14.048  -24.550 37.069  1.00 22.84 ? 31  ALA B O   1 
ATOM   1731 C CB  . ALA B 1 44  ? 12.800  -24.199 40.534  1.00 24.08 ? 31  ALA B CB  1 
ATOM   1732 N N   . GLY B 1 45  ? 11.928  -24.726 37.933  1.00 22.10 ? 32  GLY B N   1 
ATOM   1733 C CA  . GLY B 1 45  ? 11.239  -24.848 36.633  1.00 24.03 ? 32  GLY B CA  1 
ATOM   1734 C C   . GLY B 1 45  ? 10.888  -23.520 35.969  1.00 23.45 ? 32  GLY B C   1 
ATOM   1735 O O   . GLY B 1 45  ? 10.004  -23.550 35.072  1.00 21.49 ? 32  GLY B O   1 
ATOM   1736 N N   . GLN B 1 46  ? 11.552  -22.409 36.339  1.00 23.86 ? 33  GLN B N   1 
ATOM   1737 C CA  . GLN B 1 46  ? 11.269  -21.062 35.763  1.00 24.09 ? 33  GLN B CA  1 
ATOM   1738 C C   . GLN B 1 46  ? 12.175  -20.810 34.550  1.00 22.93 ? 33  GLN B C   1 
ATOM   1739 O O   . GLN B 1 46  ? 13.405  -21.032 34.640  1.00 24.62 ? 33  GLN B O   1 
ATOM   1740 C CB  . GLN B 1 46  ? 11.442  -19.944 36.793  1.00 25.25 ? 33  GLN B CB  1 
ATOM   1741 C CG  . GLN B 1 46  ? 11.153  -18.550 36.240  1.00 26.25 ? 33  GLN B CG  1 
ATOM   1742 C CD  . GLN B 1 46  ? 11.312  -17.479 37.293  1.00 28.23 ? 33  GLN B CD  1 
ATOM   1743 O OE1 . GLN B 1 46  ? 12.415  -17.163 37.729  1.00 30.35 ? 33  GLN B OE1 1 
ATOM   1744 N NE2 . GLN B 1 46  ? 10.201  -16.892 37.710  1.00 28.37 ? 33  GLN B NE2 1 
ATOM   1745 N N   . TYR B 1 47  ? 11.571  -20.350 33.463  1.00 20.04 ? 34  TYR B N   1 
ATOM   1746 C CA  . TYR B 1 47  ? 12.249  -19.708 32.313  1.00 19.55 ? 34  TYR B CA  1 
ATOM   1747 C C   . TYR B 1 47  ? 11.598  -18.341 32.117  1.00 18.81 ? 34  TYR B C   1 
ATOM   1748 O O   . TYR B 1 47  ? 10.457  -18.100 32.560  1.00 17.34 ? 34  TYR B O   1 
ATOM   1749 C CB  . TYR B 1 47  ? 12.159  -20.567 31.044  1.00 19.43 ? 34  TYR B CB  1 
ATOM   1750 C CG  . TYR B 1 47  ? 10.768  -20.740 30.475  1.00 19.71 ? 34  TYR B CG  1 
ATOM   1751 C CD1 . TYR B 1 47  ? 9.889   -21.718 30.939  1.00 19.84 ? 34  TYR B CD1 1 
ATOM   1752 C CD2 . TYR B 1 47  ? 10.325  -19.934 29.440  1.00 20.33 ? 34  TYR B CD2 1 
ATOM   1753 C CE1 . TYR B 1 47  ? 8.608   -21.868 30.409  1.00 19.12 ? 34  TYR B CE1 1 
ATOM   1754 C CE2 . TYR B 1 47  ? 9.057   -20.085 28.888  1.00 20.08 ? 34  TYR B CE2 1 
ATOM   1755 C CZ  . TYR B 1 47  ? 8.193   -21.046 29.376  1.00 18.83 ? 34  TYR B CZ  1 
ATOM   1756 O OH  . TYR B 1 47  ? 6.966   -21.149 28.795  1.00 18.62 ? 34  TYR B OH  1 
ATOM   1757 N N   . SER B 1 48  ? 12.295  -17.452 31.435  1.00 18.33 ? 35  SER B N   1 
ATOM   1758 C CA  . SER B 1 48  ? 11.659  -16.221 30.940  1.00 20.19 ? 35  SER B CA  1 
ATOM   1759 C C   . SER B 1 48  ? 12.167  -15.969 29.530  1.00 20.82 ? 35  SER B C   1 
ATOM   1760 O O   . SER B 1 48  ? 13.278  -16.382 29.224  1.00 24.35 ? 35  SER B O   1 
ATOM   1761 C CB  . SER B 1 48  ? 11.857  -15.076 31.884  1.00 20.51 ? 35  SER B CB  1 
ATOM   1762 O OG  . SER B 1 48  ? 12.906  -14.256 31.441  1.00 22.17 ? 35  SER B OG  1 
ATOM   1763 N N   . VAL B 1 49  ? 11.319  -15.400 28.691  1.00 21.42 ? 36  VAL B N   1 
ATOM   1764 C CA  . VAL B 1 49  ? 11.644  -15.101 27.273  1.00 21.86 ? 36  VAL B CA  1 
ATOM   1765 C C   . VAL B 1 49  ? 11.083  -13.714 26.964  1.00 22.34 ? 36  VAL B C   1 
ATOM   1766 O O   . VAL B 1 49  ? 10.027  -13.349 27.507  1.00 20.61 ? 36  VAL B O   1 
ATOM   1767 C CB  . VAL B 1 49  ? 11.117  -16.194 26.319  1.00 21.68 ? 36  VAL B CB  1 
ATOM   1768 C CG1 . VAL B 1 49  ? 9.609   -16.361 26.380  1.00 22.19 ? 36  VAL B CG1 1 
ATOM   1769 C CG2 . VAL B 1 49  ? 11.568  -15.968 24.892  1.00 21.02 ? 36  VAL B CG2 1 
ATOM   1770 N N   . GLU B 1 50  ? 11.822  -12.962 26.160  1.00 24.35 ? 37  GLU B N   1 
ATOM   1771 C CA  . GLU B 1 50  ? 11.437  -11.615 25.703  1.00 25.99 ? 37  GLU B CA  1 
ATOM   1772 C C   . GLU B 1 50  ? 11.677  -11.586 24.199  1.00 24.28 ? 37  GLU B C   1 
ATOM   1773 O O   . GLU B 1 50  ? 12.704  -12.120 23.765  1.00 23.38 ? 37  GLU B O   1 
ATOM   1774 C CB  . GLU B 1 50  ? 12.254  -10.593 26.481  1.00 30.38 ? 37  GLU B CB  1 
ATOM   1775 C CG  . GLU B 1 50  ? 11.653  -9.210  26.450  1.00 38.11 ? 37  GLU B CG  1 
ATOM   1776 C CD  . GLU B 1 50  ? 12.122  -8.298  27.572  1.00 44.13 ? 37  GLU B CD  1 
ATOM   1777 O OE1 . GLU B 1 50  ? 12.882  -8.770  28.441  1.00 49.61 ? 37  GLU B OE1 1 
ATOM   1778 O OE2 . GLU B 1 50  ? 11.718  -7.115  27.574  1.00 52.67 ? 37  GLU B OE2 1 
ATOM   1779 N N   . TRP B 1 51  ? 10.725  -11.058 23.429  1.00 23.45 ? 38  TRP B N   1 
ATOM   1780 C CA  . TRP B 1 51  ? 10.840  -10.983 21.954  1.00 22.16 ? 38  TRP B CA  1 
ATOM   1781 C C   . TRP B 1 51  ? 10.355  -9.635  21.432  1.00 22.58 ? 38  TRP B C   1 
ATOM   1782 O O   . TRP B 1 51  ? 9.542   -8.966  22.103  1.00 21.64 ? 38  TRP B O   1 
ATOM   1783 C CB  . TRP B 1 51  ? 10.167  -12.167 21.255  1.00 21.01 ? 38  TRP B CB  1 
ATOM   1784 C CG  . TRP B 1 51  ? 8.692   -12.345 21.430  1.00 20.54 ? 38  TRP B CG  1 
ATOM   1785 C CD1 . TRP B 1 51  ? 7.741   -12.209 20.459  1.00 20.73 ? 38  TRP B CD1 1 
ATOM   1786 C CD2 . TRP B 1 51  ? 7.996   -12.804 22.602  1.00 20.68 ? 38  TRP B CD2 1 
ATOM   1787 N NE1 . TRP B 1 51  ? 6.500   -12.517 20.952  1.00 20.37 ? 38  TRP B NE1 1 
ATOM   1788 C CE2 . TRP B 1 51  ? 6.630   -12.893 22.263  1.00 20.85 ? 38  TRP B CE2 1 
ATOM   1789 C CE3 . TRP B 1 51  ? 8.384   -13.153 23.898  1.00 21.66 ? 38  TRP B CE3 1 
ATOM   1790 C CZ2 . TRP B 1 51  ? 5.662   -13.308 23.177  1.00 21.14 ? 38  TRP B CZ2 1 
ATOM   1791 C CZ3 . TRP B 1 51  ? 7.425   -13.552 24.802  1.00 21.74 ? 38  TRP B CZ3 1 
ATOM   1792 C CH2 . TRP B 1 51  ? 6.083   -13.644 24.439  1.00 20.71 ? 38  TRP B CH2 1 
ATOM   1793 N N   . SER B 1 52  ? 10.889  -9.276  20.267  1.00 23.44 ? 39  SER B N   1 
ATOM   1794 C CA  . SER B 1 52  ? 10.641  -8.007  19.551  1.00 25.46 ? 39  SER B CA  1 
ATOM   1795 C C   . SER B 1 52  ? 10.660  -8.296  18.042  1.00 24.93 ? 39  SER B C   1 
ATOM   1796 O O   . SER B 1 52  ? 11.731  -8.666  17.518  1.00 23.74 ? 39  SER B O   1 
ATOM   1797 C CB  . SER B 1 52  ? 11.664  -6.989  19.981  1.00 27.65 ? 39  SER B CB  1 
ATOM   1798 O OG  . SER B 1 52  ? 11.467  -5.757  19.306  1.00 31.34 ? 39  SER B OG  1 
ATOM   1799 N N   . ASN B 1 53  ? 9.488   -8.224  17.394  1.00 24.02 ? 40  ASN B N   1 
ATOM   1800 C CA  . ASN B 1 53  ? 9.318   -8.405  15.926  1.00 22.21 ? 40  ASN B CA  1 
ATOM   1801 C C   . ASN B 1 53  ? 9.913   -9.758  15.513  1.00 22.72 ? 40  ASN B C   1 
ATOM   1802 O O   . ASN B 1 53  ? 10.630  -9.842  14.479  1.00 21.47 ? 40  ASN B O   1 
ATOM   1803 C CB  . ASN B 1 53  ? 9.898   -7.209  15.170  1.00 21.31 ? 40  ASN B CB  1 
ATOM   1804 C CG  . ASN B 1 53  ? 9.051   -5.973  15.364  1.00 19.64 ? 40  ASN B CG  1 
ATOM   1805 O OD1 . ASN B 1 53  ? 7.903   -5.950  14.944  1.00 20.81 ? 40  ASN B OD1 1 
ATOM   1806 N ND2 . ASN B 1 53  ? 9.595   -4.945  15.977  1.00 17.83 ? 40  ASN B ND2 1 
ATOM   1807 N N   . SER B 1 54  ? 9.568   -10.790 16.285  1.00 23.10 ? 41  SER B N   1 
ATOM   1808 C CA  . SER B 1 54  ? 10.093  -12.172 16.178  1.00 22.00 ? 41  SER B CA  1 
ATOM   1809 C C   . SER B 1 54  ? 9.653   -12.807 14.856  1.00 21.92 ? 41  SER B C   1 
ATOM   1810 O O   . SER B 1 54  ? 8.588   -12.434 14.327  1.00 21.33 ? 41  SER B O   1 
ATOM   1811 C CB  . SER B 1 54  ? 9.640   -12.996 17.362  1.00 21.33 ? 41  SER B CB  1 
ATOM   1812 O OG  . SER B 1 54  ? 8.268   -13.356 17.228  1.00 22.24 ? 41  SER B OG  1 
ATOM   1813 N N   . GLY B 1 55  ? 10.442  -13.765 14.368  1.00 21.90 ? 42  GLY B N   1 
ATOM   1814 C CA  . GLY B 1 55  ? 9.948   -14.853 13.505  1.00 21.99 ? 42  GLY B CA  1 
ATOM   1815 C C   . GLY B 1 55  ? 9.244   -15.889 14.363  1.00 22.34 ? 42  GLY B C   1 
ATOM   1816 O O   . GLY B 1 55  ? 8.663   -15.490 15.396  1.00 23.60 ? 42  GLY B O   1 
ATOM   1817 N N   . ASN B 1 56  ? 9.295   -17.164 13.973  1.00 21.49 ? 43  ASN B N   1 
ATOM   1818 C CA  . ASN B 1 56  ? 8.784   -18.286 14.794  1.00 22.09 ? 43  ASN B CA  1 
ATOM   1819 C C   . ASN B 1 56  ? 9.810   -18.593 15.892  1.00 21.72 ? 43  ASN B C   1 
ATOM   1820 O O   . ASN B 1 56  ? 11.007  -18.684 15.574  1.00 21.09 ? 43  ASN B O   1 
ATOM   1821 C CB  . ASN B 1 56  ? 8.452   -19.509 13.937  1.00 24.67 ? 43  ASN B CB  1 
ATOM   1822 C CG  . ASN B 1 56  ? 7.423   -20.434 14.567  1.00 25.97 ? 43  ASN B CG  1 
ATOM   1823 O OD1 . ASN B 1 56  ? 6.685   -20.059 15.489  1.00 26.43 ? 43  ASN B OD1 1 
ATOM   1824 N ND2 . ASN B 1 56  ? 7.347   -21.650 14.056  1.00 25.69 ? 43  ASN B ND2 1 
ATOM   1825 N N   . PHE B 1 57  ? 9.361   -18.691 17.147  1.00 20.61 ? 44  PHE B N   1 
ATOM   1826 C CA  . PHE B 1 57  ? 10.179  -19.170 18.292  1.00 20.25 ? 44  PHE B CA  1 
ATOM   1827 C C   . PHE B 1 57  ? 9.307   -19.972 19.267  1.00 20.51 ? 44  PHE B C   1 
ATOM   1828 O O   . PHE B 1 57  ? 8.091   -19.710 19.403  1.00 21.40 ? 44  PHE B O   1 
ATOM   1829 C CB  . PHE B 1 57  ? 10.846  -18.011 19.032  1.00 19.61 ? 44  PHE B CB  1 
ATOM   1830 C CG  . PHE B 1 57  ? 9.976   -17.395 20.098  1.00 20.37 ? 44  PHE B CG  1 
ATOM   1831 C CD1 . PHE B 1 57  ? 9.975   -17.895 21.389  1.00 19.50 ? 44  PHE B CD1 1 
ATOM   1832 C CD2 . PHE B 1 57  ? 9.146   -16.319 19.807  1.00 20.58 ? 44  PHE B CD2 1 
ATOM   1833 C CE1 . PHE B 1 57  ? 9.181   -17.318 22.365  1.00 19.43 ? 44  PHE B CE1 1 
ATOM   1834 C CE2 . PHE B 1 57  ? 8.352   -15.748 20.787  1.00 19.81 ? 44  PHE B CE2 1 
ATOM   1835 C CZ  . PHE B 1 57  ? 8.373   -16.250 22.064  1.00 19.25 ? 44  PHE B CZ  1 
ATOM   1836 N N   . VAL B 1 58  ? 9.940   -20.942 19.921  1.00 19.95 ? 45  VAL B N   1 
ATOM   1837 C CA  . VAL B 1 58  ? 9.365   -21.792 20.995  1.00 19.49 ? 45  VAL B CA  1 
ATOM   1838 C C   . VAL B 1 58  ? 10.381  -21.812 22.146  1.00 19.73 ? 45  VAL B C   1 
ATOM   1839 O O   . VAL B 1 58  ? 11.610  -21.965 21.882  1.00 18.95 ? 45  VAL B O   1 
ATOM   1840 C CB  . VAL B 1 58  ? 9.058   -23.206 20.470  1.00 19.76 ? 45  VAL B CB  1 
ATOM   1841 C CG1 . VAL B 1 58  ? 8.291   -24.029 21.495  1.00 20.42 ? 45  VAL B CG1 1 
ATOM   1842 C CG2 . VAL B 1 58  ? 8.303   -23.163 19.151  1.00 20.10 ? 45  VAL B CG2 1 
ATOM   1843 N N   . ALA B 1 59  ? 9.896   -21.647 23.374  1.00 18.25 ? 46  ALA B N   1 
ATOM   1844 C CA  . ALA B 1 59  ? 10.729  -21.600 24.590  1.00 18.83 ? 46  ALA B CA  1 
ATOM   1845 C C   . ALA B 1 59  ? 9.953   -22.219 25.750  1.00 18.86 ? 46  ALA B C   1 
ATOM   1846 O O   . ALA B 1 59  ? 8.806   -21.818 25.961  1.00 17.56 ? 46  ALA B O   1 
ATOM   1847 C CB  . ALA B 1 59  ? 11.117  -20.172 24.882  1.00 19.08 ? 46  ALA B CB  1 
ATOM   1848 N N   . GLY B 1 60  ? 10.564  -23.159 26.474  1.00 20.08 ? 47  GLY B N   1 
ATOM   1849 C CA  . GLY B 1 60  ? 10.044  -23.560 27.792  1.00 21.32 ? 47  GLY B CA  1 
ATOM   1850 C C   . GLY B 1 60  ? 10.822  -24.680 28.433  1.00 22.42 ? 47  GLY B C   1 
ATOM   1851 O O   . GLY B 1 60  ? 11.777  -25.218 27.819  1.00 22.03 ? 47  GLY B O   1 
ATOM   1852 N N   . LYS B 1 61  ? 10.407  -25.013 29.649  1.00 22.38 ? 48  LYS B N   1 
ATOM   1853 C CA  . LYS B 1 61  ? 11.008  -26.089 30.464  1.00 21.23 ? 48  LYS B CA  1 
ATOM   1854 C C   . LYS B 1 61  ? 10.018  -27.240 30.574  1.00 21.23 ? 48  LYS B C   1 
ATOM   1855 O O   . LYS B 1 61  ? 8.796   -27.017 30.429  1.00 21.14 ? 48  LYS B O   1 
ATOM   1856 C CB  . LYS B 1 61  ? 11.407  -25.544 31.834  1.00 21.08 ? 48  LYS B CB  1 
ATOM   1857 C CG  . LYS B 1 61  ? 12.814  -24.963 31.899  1.00 20.36 ? 48  LYS B CG  1 
ATOM   1858 C CD  . LYS B 1 61  ? 13.110  -24.407 33.250  1.00 21.47 ? 48  LYS B CD  1 
ATOM   1859 C CE  . LYS B 1 61  ? 14.577  -24.119 33.473  1.00 22.47 ? 48  LYS B CE  1 
ATOM   1860 N NZ  . LYS B 1 61  ? 14.786  -23.517 34.812  1.00 23.35 ? 48  LYS B NZ  1 
ATOM   1861 N N   . GLY B 1 62  ? 10.546  -28.423 30.839  1.00 20.30 ? 49  GLY B N   1 
ATOM   1862 C CA  . GLY B 1 62  ? 9.739   -29.612 31.142  1.00 21.52 ? 49  GLY B CA  1 
ATOM   1863 C C   . GLY B 1 62  ? 10.631  -30.832 31.233  1.00 22.17 ? 49  GLY B C   1 
ATOM   1864 O O   . GLY B 1 62  ? 11.596  -30.762 32.021  1.00 21.89 ? 49  GLY B O   1 
ATOM   1865 N N   . TRP B 1 63  ? 10.357  -31.861 30.416  1.00 22.98 ? 50  TRP B N   1 
ATOM   1866 C CA  . TRP B 1 63  ? 10.949  -33.227 30.524  1.00 25.21 ? 50  TRP B CA  1 
ATOM   1867 C C   . TRP B 1 63  ? 11.331  -33.765 29.142  1.00 25.66 ? 50  TRP B C   1 
ATOM   1868 O O   . TRP B 1 63  ? 10.596  -33.473 28.161  1.00 24.57 ? 50  TRP B O   1 
ATOM   1869 C CB  . TRP B 1 63  ? 9.975   -34.185 31.221  1.00 26.05 ? 50  TRP B CB  1 
ATOM   1870 C CG  . TRP B 1 63  ? 9.505   -33.701 32.555  1.00 27.08 ? 50  TRP B CG  1 
ATOM   1871 C CD1 . TRP B 1 63  ? 10.000  -34.065 33.770  1.00 26.45 ? 50  TRP B CD1 1 
ATOM   1872 C CD2 . TRP B 1 63  ? 8.476   -32.726 32.811  1.00 26.85 ? 50  TRP B CD2 1 
ATOM   1873 N NE1 . TRP B 1 63  ? 9.324   -33.412 34.763  1.00 27.29 ? 50  TRP B NE1 1 
ATOM   1874 C CE2 . TRP B 1 63  ? 8.383   -32.587 34.212  1.00 27.12 ? 50  TRP B CE2 1 
ATOM   1875 C CE3 . TRP B 1 63  ? 7.611   -31.978 32.003  1.00 27.91 ? 50  TRP B CE3 1 
ATOM   1876 C CZ2 . TRP B 1 63  ? 7.477   -31.719 34.821  1.00 28.05 ? 50  TRP B CZ2 1 
ATOM   1877 C CZ3 . TRP B 1 63  ? 6.707   -31.123 32.603  1.00 29.05 ? 50  TRP B CZ3 1 
ATOM   1878 C CH2 . TRP B 1 63  ? 6.646   -30.994 33.995  1.00 28.65 ? 50  TRP B CH2 1 
ATOM   1879 N N   . ASN B 1 64  ? 12.441  -34.509 29.082  1.00 26.70 ? 51  ASN B N   1 
ATOM   1880 C CA  . ASN B 1 64  ? 12.873  -35.276 27.886  1.00 28.79 ? 51  ASN B CA  1 
ATOM   1881 C C   . ASN B 1 64  ? 13.435  -36.625 28.332  1.00 30.40 ? 51  ASN B C   1 
ATOM   1882 O O   . ASN B 1 64  ? 14.505  -36.685 28.925  1.00 31.88 ? 51  ASN B O   1 
ATOM   1883 C CB  . ASN B 1 64  ? 13.872  -34.518 27.010  1.00 28.37 ? 51  ASN B CB  1 
ATOM   1884 C CG  . ASN B 1 64  ? 14.120  -35.228 25.692  1.00 30.72 ? 51  ASN B CG  1 
ATOM   1885 O OD1 . ASN B 1 64  ? 13.329  -36.063 25.254  1.00 33.82 ? 51  ASN B OD1 1 
ATOM   1886 N ND2 . ASN B 1 64  ? 15.227  -34.924 25.047  1.00 31.04 ? 51  ASN B ND2 1 
ATOM   1887 N N   . PRO B 1 65  ? 12.750  -37.758 28.051  1.00 30.12 ? 52  PRO B N   1 
ATOM   1888 C CA  . PRO B 1 65  ? 11.454  -37.750 27.369  1.00 29.10 ? 52  PRO B CA  1 
ATOM   1889 C C   . PRO B 1 65  ? 10.271  -37.285 28.239  1.00 30.05 ? 52  PRO B C   1 
ATOM   1890 O O   . PRO B 1 65  ? 10.314  -37.456 29.449  1.00 29.86 ? 52  PRO B O   1 
ATOM   1891 C CB  . PRO B 1 65  ? 11.283  -39.229 26.973  1.00 29.61 ? 52  PRO B CB  1 
ATOM   1892 C CG  . PRO B 1 65  ? 12.030  -39.989 28.048  1.00 29.75 ? 52  PRO B CG  1 
ATOM   1893 C CD  . PRO B 1 65  ? 13.237  -39.120 28.337  1.00 30.06 ? 52  PRO B CD  1 
ATOM   1894 N N   . GLY B 1 66  ? 9.220   -36.737 27.613  1.00 30.28 ? 53  GLY B N   1 
ATOM   1895 C CA  . GLY B 1 66  ? 7.918   -36.512 28.279  1.00 30.16 ? 53  GLY B CA  1 
ATOM   1896 C C   . GLY B 1 66  ? 7.250   -37.822 28.697  1.00 30.12 ? 53  GLY B C   1 
ATOM   1897 O O   . GLY B 1 66  ? 7.528   -38.863 28.077  1.00 29.34 ? 53  GLY B O   1 
ATOM   1898 N N   . SER B 1 67  ? 6.415   -37.786 29.733  1.00 31.05 ? 54  SER B N   1 
ATOM   1899 C CA  . SER B 1 67  ? 5.464   -38.870 30.110  1.00 33.60 ? 54  SER B CA  1 
ATOM   1900 C C   . SER B 1 67  ? 4.038   -38.314 30.102  1.00 31.69 ? 54  SER B C   1 
ATOM   1901 O O   . SER B 1 67  ? 3.791   -37.329 29.383  1.00 35.91 ? 54  SER B O   1 
ATOM   1902 C CB  . SER B 1 67  ? 5.808   -39.485 31.446  1.00 33.20 ? 54  SER B CB  1 
ATOM   1903 O OG  . SER B 1 67  ? 7.076   -40.094 31.376  1.00 35.20 ? 54  SER B OG  1 
ATOM   1904 N N   . SER B 1 68  ? 3.140   -38.938 30.856  1.00 32.57 ? 55  SER B N   1 
ATOM   1905 C CA  . SER B 1 68  ? 1.738   -38.498 31.064  1.00 34.38 ? 55  SER B CA  1 
ATOM   1906 C C   . SER B 1 68  ? 1.620   -37.915 32.476  1.00 33.57 ? 55  SER B C   1 
ATOM   1907 O O   . SER B 1 68  ? 0.715   -38.337 33.243  1.00 36.97 ? 55  SER B O   1 
ATOM   1908 C CB  . SER B 1 68  ? 0.771   -39.630 30.842  1.00 34.45 ? 55  SER B CB  1 
ATOM   1909 O OG  . SER B 1 68  ? 0.914   -40.614 31.857  1.00 37.38 ? 55  SER B OG  1 
ATOM   1910 N N   . GLN B 1 69  ? 2.523   -36.997 32.816  1.00 30.20 ? 56  GLN B N   1 
ATOM   1911 C CA  . GLN B 1 69  ? 2.545   -36.373 34.160  1.00 30.31 ? 56  GLN B CA  1 
ATOM   1912 C C   . GLN B 1 69  ? 1.518   -35.236 34.187  1.00 27.13 ? 56  GLN B C   1 
ATOM   1913 O O   . GLN B 1 69  ? 1.255   -34.611 33.135  1.00 24.48 ? 56  GLN B O   1 
ATOM   1914 C CB  . GLN B 1 69  ? 3.949   -35.931 34.597  1.00 31.74 ? 56  GLN B CB  1 
ATOM   1915 C CG  . GLN B 1 69  ? 4.709   -35.068 33.603  1.00 31.71 ? 56  GLN B CG  1 
ATOM   1916 C CD  . GLN B 1 69  ? 5.763   -35.886 32.898  1.00 33.06 ? 56  GLN B CD  1 
ATOM   1917 O OE1 . GLN B 1 69  ? 5.556   -36.372 31.786  1.00 32.18 ? 56  GLN B OE1 1 
ATOM   1918 N NE2 . GLN B 1 69  ? 6.895   -36.072 33.555  1.00 33.12 ? 56  GLN B NE2 1 
ATOM   1919 N N   . THR B 1 70  ? 0.931   -35.054 35.365  1.00 24.26 ? 57  THR B N   1 
ATOM   1920 C CA  . THR B 1 70  ? 0.041   -33.937 35.733  1.00 24.47 ? 57  THR B CA  1 
ATOM   1921 C C   . THR B 1 70  ? 0.944   -32.737 35.996  1.00 23.65 ? 57  THR B C   1 
ATOM   1922 O O   . THR B 1 70  ? 1.641   -32.760 37.001  1.00 26.51 ? 57  THR B O   1 
ATOM   1923 C CB  . THR B 1 70  ? -0.835  -34.367 36.918  1.00 24.60 ? 57  THR B CB  1 
ATOM   1924 O OG1 . THR B 1 70  ? -1.632  -35.449 36.430  1.00 25.04 ? 57  THR B OG1 1 
ATOM   1925 C CG2 . THR B 1 70  ? -1.733  -33.272 37.446  1.00 25.30 ? 57  THR B CG2 1 
ATOM   1926 N N   . ILE B 1 71  ? 0.982   -31.771 35.089  1.00 22.52 ? 58  ILE B N   1 
ATOM   1927 C CA  . ILE B 1 71  ? 1.887   -30.588 35.194  1.00 22.94 ? 58  ILE B CA  1 
ATOM   1928 C C   . ILE B 1 71  ? 1.140   -29.485 35.947  1.00 21.61 ? 58  ILE B C   1 
ATOM   1929 O O   . ILE B 1 71  ? -0.068  -29.296 35.668  1.00 22.88 ? 58  ILE B O   1 
ATOM   1930 C CB  . ILE B 1 71  ? 2.319   -30.115 33.791  1.00 24.06 ? 58  ILE B CB  1 
ATOM   1931 C CG1 . ILE B 1 71  ? 2.925   -31.260 32.973  1.00 24.17 ? 58  ILE B CG1 1 
ATOM   1932 C CG2 . ILE B 1 71  ? 3.242   -28.908 33.890  1.00 23.56 ? 58  ILE B CG2 1 
ATOM   1933 C CD1 . ILE B 1 71  ? 3.028   -30.959 31.492  1.00 25.78 ? 58  ILE B CD1 1 
ATOM   1934 N N   . THR B 1 72  ? 1.799   -28.810 36.886  1.00 19.93 ? 59  THR B N   1 
ATOM   1935 C CA  . THR B 1 72  ? 1.340   -27.494 37.383  1.00 19.81 ? 59  THR B CA  1 
ATOM   1936 C C   . THR B 1 72  ? 2.299   -26.433 36.847  1.00 19.29 ? 59  THR B C   1 
ATOM   1937 O O   . THR B 1 72  ? 3.526   -26.625 36.932  1.00 19.83 ? 59  THR B O   1 
ATOM   1938 C CB  . THR B 1 72  ? 1.210   -27.456 38.905  1.00 21.33 ? 59  THR B CB  1 
ATOM   1939 O OG1 . THR B 1 72  ? 0.275   -28.452 39.306  1.00 22.59 ? 59  THR B OG1 1 
ATOM   1940 C CG2 . THR B 1 72  ? 0.722   -26.114 39.408  1.00 22.68 ? 59  THR B CG2 1 
ATOM   1941 N N   . TYR B 1 73  ? 1.763   -25.357 36.294  1.00 18.21 ? 60  TYR B N   1 
ATOM   1942 C CA  . TYR B 1 73  ? 2.575   -24.210 35.836  1.00 18.48 ? 60  TYR B CA  1 
ATOM   1943 C C   . TYR B 1 73  ? 1.914   -22.932 36.343  1.00 18.19 ? 60  TYR B C   1 
ATOM   1944 O O   . TYR B 1 73  ? 0.667   -22.866 36.542  1.00 17.14 ? 60  TYR B O   1 
ATOM   1945 C CB  . TYR B 1 73  ? 2.731   -24.234 34.309  1.00 19.12 ? 60  TYR B CB  1 
ATOM   1946 C CG  . TYR B 1 73  ? 1.485   -23.788 33.609  1.00 19.01 ? 60  TYR B CG  1 
ATOM   1947 C CD1 . TYR B 1 73  ? 0.402   -24.638 33.522  1.00 19.13 ? 60  TYR B CD1 1 
ATOM   1948 C CD2 . TYR B 1 73  ? 1.340   -22.489 33.153  1.00 19.89 ? 60  TYR B CD2 1 
ATOM   1949 C CE1 . TYR B 1 73  ? -0.784  -24.234 32.940  1.00 20.18 ? 60  TYR B CE1 1 
ATOM   1950 C CE2 . TYR B 1 73  ? 0.155   -22.067 32.566  1.00 19.97 ? 60  TYR B CE2 1 
ATOM   1951 C CZ  . TYR B 1 73  ? -0.913  -22.943 32.466  1.00 20.16 ? 60  TYR B CZ  1 
ATOM   1952 O OH  . TYR B 1 73  ? -2.105  -22.564 31.922  1.00 19.68 ? 60  TYR B OH  1 
ATOM   1953 N N   . SER B 1 74  ? 2.748   -21.916 36.497  1.00 19.09 ? 61  SER B N   1 
ATOM   1954 C CA  . SER B 1 74  ? 2.371   -20.568 36.976  1.00 19.75 ? 61  SER B CA  1 
ATOM   1955 C C   . SER B 1 74  ? 3.232   -19.542 36.251  1.00 18.62 ? 61  SER B C   1 
ATOM   1956 O O   . SER B 1 74  ? 4.088   -19.957 35.454  1.00 16.50 ? 61  SER B O   1 
ATOM   1957 C CB  . SER B 1 74  ? 2.499   -20.469 38.494  1.00 21.20 ? 61  SER B CB  1 
ATOM   1958 O OG  . SER B 1 74  ? 3.850   -20.593 38.907  1.00 21.96 ? 61  SER B OG  1 
ATOM   1959 N N   . GLY B 1 75  ? 2.951   -18.260 36.508  1.00 19.17 ? 62  GLY B N   1 
ATOM   1960 C CA  . GLY B 1 75  ? 3.730   -17.107 36.032  1.00 19.09 ? 62  GLY B CA  1 
ATOM   1961 C C   . GLY B 1 75  ? 2.865   -16.156 35.228  1.00 19.40 ? 62  GLY B C   1 
ATOM   1962 O O   . GLY B 1 75  ? 1.661   -15.998 35.556  1.00 18.91 ? 62  GLY B O   1 
ATOM   1963 N N   . GLU B 1 76  ? 3.454   -15.537 34.210  1.00 19.78 ? 63  GLU B N   1 
ATOM   1964 C CA  . GLU B 1 76  ? 2.767   -14.502 33.407  1.00 22.62 ? 63  GLU B CA  1 
ATOM   1965 C C   . GLU B 1 76  ? 3.293   -14.491 31.978  1.00 21.26 ? 63  GLU B C   1 
ATOM   1966 O O   . GLU B 1 76  ? 4.476   -14.780 31.759  1.00 21.23 ? 63  GLU B O   1 
ATOM   1967 C CB  . GLU B 1 76  ? 2.895   -13.116 34.038  1.00 25.72 ? 63  GLU B CB  1 
ATOM   1968 C CG  . GLU B 1 76  ? 4.289   -12.725 34.463  1.00 27.91 ? 63  GLU B CG  1 
ATOM   1969 C CD  . GLU B 1 76  ? 4.288   -11.309 35.004  1.00 32.40 ? 63  GLU B CD  1 
ATOM   1970 O OE1 . GLU B 1 76  ? 4.318   -11.147 36.244  1.00 41.33 ? 63  GLU B OE1 1 
ATOM   1971 O OE2 . GLU B 1 76  ? 4.197   -10.379 34.192  1.00 33.00 ? 63  GLU B OE2 1 
ATOM   1972 N N   . TRP B 1 77  ? 2.405   -14.124 31.065  1.00 20.91 ? 64  TRP B N   1 
ATOM   1973 C CA  . TRP B 1 77  ? 2.539   -14.291 29.600  1.00 21.58 ? 64  TRP B CA  1 
ATOM   1974 C C   . TRP B 1 77  ? 1.920   -13.037 28.983  1.00 21.17 ? 64  TRP B C   1 
ATOM   1975 O O   . TRP B 1 77  ? 0.679   -12.984 28.914  1.00 20.97 ? 64  TRP B O   1 
ATOM   1976 C CB  . TRP B 1 77  ? 1.862   -15.621 29.210  1.00 21.67 ? 64  TRP B CB  1 
ATOM   1977 C CG  . TRP B 1 77  ? 1.651   -15.895 27.751  1.00 21.59 ? 64  TRP B CG  1 
ATOM   1978 C CD1 . TRP B 1 77  ? 2.562   -16.382 26.855  1.00 21.95 ? 64  TRP B CD1 1 
ATOM   1979 C CD2 . TRP B 1 77  ? 0.415   -15.769 27.026  1.00 20.45 ? 64  TRP B CD2 1 
ATOM   1980 N NE1 . TRP B 1 77  ? 1.987   -16.534 25.619  1.00 21.03 ? 64  TRP B NE1 1 
ATOM   1981 C CE2 . TRP B 1 77  ? 0.675   -16.153 25.689  1.00 20.13 ? 64  TRP B CE2 1 
ATOM   1982 C CE3 . TRP B 1 77  ? -0.871  -15.342 27.369  1.00 20.33 ? 64  TRP B CE3 1 
ATOM   1983 C CZ2 . TRP B 1 77  ? -0.309  -16.143 24.704  1.00 19.94 ? 64  TRP B CZ2 1 
ATOM   1984 C CZ3 . TRP B 1 77  ? -1.849  -15.340 26.396  1.00 21.00 ? 64  TRP B CZ3 1 
ATOM   1985 C CH2 . TRP B 1 77  ? -1.572  -15.744 25.084  1.00 20.90 ? 64  TRP B CH2 1 
ATOM   1986 N N   . ASN B 1 78  ? 2.761   -12.047 28.650  1.00 21.40 ? 65  ASN B N   1 
ATOM   1987 C CA  . ASN B 1 78  ? 2.376   -10.708 28.120  1.00 22.65 ? 65  ASN B CA  1 
ATOM   1988 C C   . ASN B 1 78  ? 2.790   -10.543 26.659  1.00 22.35 ? 65  ASN B C   1 
ATOM   1989 O O   . ASN B 1 78  ? 3.674   -9.755  26.344  1.00 22.40 ? 65  ASN B O   1 
ATOM   1990 C CB  . ASN B 1 78  ? 2.974   -9.600  28.985  1.00 24.04 ? 65  ASN B CB  1 
ATOM   1991 C CG  . ASN B 1 78  ? 2.618   -9.804  30.440  1.00 25.94 ? 65  ASN B CG  1 
ATOM   1992 O OD1 . ASN B 1 78  ? 1.440   -9.753  30.808  1.00 24.93 ? 65  ASN B OD1 1 
ATOM   1993 N ND2 . ASN B 1 78  ? 3.624   -10.094 31.251  1.00 26.21 ? 65  ASN B ND2 1 
ATOM   1994 N N   . PRO B 1 79  ? 2.146   -11.247 25.703  1.00 23.58 ? 66  PRO B N   1 
ATOM   1995 C CA  . PRO B 1 79  ? 2.377   -10.994 24.284  1.00 24.41 ? 66  PRO B CA  1 
ATOM   1996 C C   . PRO B 1 79  ? 1.682   -9.717  23.803  1.00 25.46 ? 66  PRO B C   1 
ATOM   1997 O O   . PRO B 1 79  ? 0.631   -9.398  24.350  1.00 25.13 ? 66  PRO B O   1 
ATOM   1998 C CB  . PRO B 1 79  ? 1.720   -12.202 23.612  1.00 24.80 ? 66  PRO B CB  1 
ATOM   1999 C CG  . PRO B 1 79  ? 0.577   -12.529 24.538  1.00 25.26 ? 66  PRO B CG  1 
ATOM   2000 C CD  . PRO B 1 79  ? 1.174   -12.326 25.916  1.00 24.65 ? 66  PRO B CD  1 
ATOM   2001 N N   . ASN B 1 80  ? 2.278   -9.038  22.813  1.00 25.97 ? 67  ASN B N   1 
ATOM   2002 C CA  . ASN B 1 80  ? 1.579   -8.073  21.924  1.00 24.95 ? 67  ASN B CA  1 
ATOM   2003 C C   . ASN B 1 80  ? 1.591   -8.650  20.504  1.00 23.31 ? 67  ASN B C   1 
ATOM   2004 O O   . ASN B 1 80  ? 2.582   -8.418  19.760  1.00 22.87 ? 67  ASN B O   1 
ATOM   2005 C CB  . ASN B 1 80  ? 2.161   -6.657  22.005  1.00 27.96 ? 67  ASN B CB  1 
ATOM   2006 C CG  . ASN B 1 80  ? 1.253   -5.624  21.360  1.00 31.36 ? 67  ASN B CG  1 
ATOM   2007 O OD1 . ASN B 1 80  ? 0.026   -5.705  21.467  1.00 36.54 ? 67  ASN B OD1 1 
ATOM   2008 N ND2 . ASN B 1 80  ? 1.834   -4.652  20.671  1.00 32.22 ? 67  ASN B ND2 1 
ATOM   2009 N N   . GLY B 1 81  ? 0.529   -9.381  20.149  1.00 20.72 ? 68  GLY B N   1 
ATOM   2010 C CA  . GLY B 1 81  ? 0.432   -10.132 18.883  1.00 20.39 ? 68  GLY B CA  1 
ATOM   2011 C C   . GLY B 1 81  ? 0.455   -11.645 19.077  1.00 19.19 ? 68  GLY B C   1 
ATOM   2012 O O   . GLY B 1 81  ? 0.344   -12.112 20.222  1.00 18.94 ? 68  GLY B O   1 
ATOM   2013 N N   . ASN B 1 82  ? 0.597   -12.380 17.971  1.00 18.50 ? 69  ASN B N   1 
ATOM   2014 C CA  . ASN B 1 82  ? 0.435   -13.856 17.868  1.00 18.03 ? 69  ASN B CA  1 
ATOM   2015 C C   . ASN B 1 82  ? 1.414   -14.578 18.814  1.00 17.86 ? 69  ASN B C   1 
ATOM   2016 O O   . ASN B 1 82  ? 2.662   -14.510 18.613  1.00 17.16 ? 69  ASN B O   1 
ATOM   2017 C CB  . ASN B 1 82  ? 0.551   -14.301 16.409  1.00 18.98 ? 69  ASN B CB  1 
ATOM   2018 C CG  . ASN B 1 82  ? 0.325   -15.783 16.222  1.00 19.41 ? 69  ASN B CG  1 
ATOM   2019 O OD1 . ASN B 1 82  ? -0.138  -16.466 17.129  1.00 23.46 ? 69  ASN B OD1 1 
ATOM   2020 N ND2 . ASN B 1 82  ? 0.660   -16.294 15.054  1.00 20.10 ? 69  ASN B ND2 1 
ATOM   2021 N N   . SER B 1 83  ? 0.858   -15.239 19.833  1.00 17.72 ? 70  SER B N   1 
ATOM   2022 C CA  . SER B 1 83  ? 1.593   -16.089 20.798  1.00 17.52 ? 70  SER B CA  1 
ATOM   2023 C C   . SER B 1 83  ? 0.649   -17.135 21.377  1.00 17.57 ? 70  SER B C   1 
ATOM   2024 O O   . SER B 1 83  ? -0.531  -16.810 21.578  1.00 17.19 ? 70  SER B O   1 
ATOM   2025 C CB  . SER B 1 83  ? 2.219   -15.273 21.885  1.00 17.68 ? 70  SER B CB  1 
ATOM   2026 O OG  . SER B 1 83  ? 3.058   -16.083 22.696  1.00 16.77 ? 70  SER B OG  1 
ATOM   2027 N N   . TYR B 1 84  ? 1.170   -18.336 21.611  1.00 19.22 ? 71  TYR B N   1 
ATOM   2028 C CA  . TYR B 1 84  ? 0.500   -19.423 22.362  1.00 21.49 ? 71  TYR B CA  1 
ATOM   2029 C C   . TYR B 1 84  ? 1.270   -19.677 23.658  1.00 19.45 ? 71  TYR B C   1 
ATOM   2030 O O   . TYR B 1 84  ? 2.489   -19.503 23.673  1.00 17.04 ? 71  TYR B O   1 
ATOM   2031 C CB  . TYR B 1 84  ? 0.457   -20.746 21.586  1.00 24.11 ? 71  TYR B CB  1 
ATOM   2032 C CG  . TYR B 1 84  ? 0.282   -20.641 20.095  1.00 27.21 ? 71  TYR B CG  1 
ATOM   2033 C CD1 . TYR B 1 84  ? -0.654  -19.775 19.543  1.00 29.48 ? 71  TYR B CD1 1 
ATOM   2034 C CD2 . TYR B 1 84  ? 1.003   -21.456 19.231  1.00 30.23 ? 71  TYR B CD2 1 
ATOM   2035 C CE1 . TYR B 1 84  ? -0.844  -19.684 18.172  1.00 30.03 ? 71  TYR B CE1 1 
ATOM   2036 C CE2 . TYR B 1 84  ? 0.816   -21.386 17.854  1.00 33.32 ? 71  TYR B CE2 1 
ATOM   2037 C CZ  . TYR B 1 84  ? -0.115  -20.501 17.327  1.00 32.44 ? 71  TYR B CZ  1 
ATOM   2038 O OH  . TYR B 1 84  ? -0.323  -20.423 15.982  1.00 37.80 ? 71  TYR B OH  1 
ATOM   2039 N N   . LEU B 1 85  ? 0.552   -20.119 24.690  1.00 19.87 ? 72  LEU B N   1 
ATOM   2040 C CA  . LEU B 1 85  ? 1.131   -20.767 25.893  1.00 19.75 ? 72  LEU B CA  1 
ATOM   2041 C C   . LEU B 1 85  ? 0.539   -22.180 25.993  1.00 18.87 ? 72  LEU B C   1 
ATOM   2042 O O   . LEU B 1 85  ? -0.681  -22.292 26.121  1.00 17.82 ? 72  LEU B O   1 
ATOM   2043 C CB  . LEU B 1 85  ? 0.813   -19.901 27.112  1.00 20.25 ? 72  LEU B CB  1 
ATOM   2044 C CG  . LEU B 1 85  ? 1.387   -20.408 28.430  1.00 20.51 ? 72  LEU B CG  1 
ATOM   2045 C CD1 . LEU B 1 85  ? 2.907   -20.343 28.401  1.00 20.30 ? 72  LEU B CD1 1 
ATOM   2046 C CD2 . LEU B 1 85  ? 0.817   -19.602 29.592  1.00 20.60 ? 72  LEU B CD2 1 
ATOM   2047 N N   . SER B 1 86  ? 1.367   -23.223 25.883  1.00 18.55 ? 73  SER B N   1 
ATOM   2048 C CA  . SER B 1 86  ? 0.904   -24.623 25.715  1.00 18.67 ? 73  SER B CA  1 
ATOM   2049 C C   . SER B 1 86  ? 1.756   -25.582 26.527  1.00 17.76 ? 73  SER B C   1 
ATOM   2050 O O   . SER B 1 86  ? 2.923   -25.305 26.735  1.00 18.81 ? 73  SER B O   1 
ATOM   2051 C CB  . SER B 1 86  ? 0.952   -25.039 24.270  1.00 19.14 ? 73  SER B CB  1 
ATOM   2052 O OG  . SER B 1 86  ? 0.333   -24.079 23.442  1.00 19.58 ? 73  SER B OG  1 
ATOM   2053 N N   . VAL B 1 87  ? 1.192   -26.718 26.891  1.00 16.97 ? 74  VAL B N   1 
ATOM   2054 C CA  . VAL B 1 87  ? 2.006   -27.940 27.050  1.00 16.61 ? 74  VAL B CA  1 
ATOM   2055 C C   . VAL B 1 87  ? 2.208   -28.434 25.634  1.00 16.93 ? 74  VAL B C   1 
ATOM   2056 O O   . VAL B 1 87  ? 1.223   -28.697 24.967  1.00 18.26 ? 74  VAL B O   1 
ATOM   2057 C CB  . VAL B 1 87  ? 1.369   -28.984 27.969  1.00 16.89 ? 74  VAL B CB  1 
ATOM   2058 C CG1 . VAL B 1 87  ? 2.265   -30.213 28.065  1.00 17.13 ? 74  VAL B CG1 1 
ATOM   2059 C CG2 . VAL B 1 87  ? 1.074   -28.383 29.345  1.00 16.42 ? 74  VAL B CG2 1 
ATOM   2060 N N   . TYR B 1 88  ? 3.459   -28.437 25.200  1.00 17.41 ? 75  TYR B N   1 
ATOM   2061 C CA  . TYR B 1 88  ? 3.906   -28.643 23.809  1.00 17.85 ? 75  TYR B CA  1 
ATOM   2062 C C   . TYR B 1 88  ? 4.862   -29.819 23.845  1.00 19.83 ? 75  TYR B C   1 
ATOM   2063 O O   . TYR B 1 88  ? 5.618   -29.954 24.834  1.00 21.64 ? 75  TYR B O   1 
ATOM   2064 C CB  . TYR B 1 88  ? 4.587   -27.375 23.279  1.00 17.83 ? 75  TYR B CB  1 
ATOM   2065 C CG  . TYR B 1 88  ? 5.263   -27.500 21.935  1.00 17.09 ? 75  TYR B CG  1 
ATOM   2066 C CD1 . TYR B 1 88  ? 4.533   -27.477 20.763  1.00 17.17 ? 75  TYR B CD1 1 
ATOM   2067 C CD2 . TYR B 1 88  ? 6.635   -27.629 21.828  1.00 17.13 ? 75  TYR B CD2 1 
ATOM   2068 C CE1 . TYR B 1 88  ? 5.138   -27.610 19.527  1.00 16.63 ? 75  TYR B CE1 1 
ATOM   2069 C CE2 . TYR B 1 88  ? 7.258   -27.750 20.597  1.00 16.24 ? 75  TYR B CE2 1 
ATOM   2070 C CZ  . TYR B 1 88  ? 6.506   -27.744 19.446  1.00 16.11 ? 75  TYR B CZ  1 
ATOM   2071 O OH  . TYR B 1 88  ? 7.096   -27.869 18.225  1.00 16.86 ? 75  TYR B OH  1 
ATOM   2072 N N   . GLY B 1 89  ? 4.828   -30.653 22.816  1.00 20.23 ? 76  GLY B N   1 
ATOM   2073 C CA  . GLY B 1 89  ? 5.848   -31.700 22.680  1.00 20.74 ? 76  GLY B CA  1 
ATOM   2074 C C   . GLY B 1 89  ? 5.697   -32.452 21.383  1.00 20.59 ? 76  GLY B C   1 
ATOM   2075 O O   . GLY B 1 89  ? 5.016   -31.926 20.453  1.00 19.00 ? 76  GLY B O   1 
ATOM   2076 N N   . TRP B 1 90  ? 6.338   -33.621 21.345  1.00 20.36 ? 77  TRP B N   1 
ATOM   2077 C CA  . TRP B 1 90  ? 6.546   -34.451 20.134  1.00 20.82 ? 77  TRP B CA  1 
ATOM   2078 C C   . TRP B 1 90  ? 6.489   -35.922 20.529  1.00 20.32 ? 77  TRP B C   1 
ATOM   2079 O O   . TRP B 1 90  ? 7.043   -36.278 21.597  1.00 20.80 ? 77  TRP B O   1 
ATOM   2080 C CB  . TRP B 1 90  ? 7.903   -34.143 19.479  1.00 20.83 ? 77  TRP B CB  1 
ATOM   2081 C CG  . TRP B 1 90  ? 8.023   -32.789 18.864  1.00 20.10 ? 77  TRP B CG  1 
ATOM   2082 C CD1 . TRP B 1 90  ? 8.336   -31.622 19.493  1.00 20.91 ? 77  TRP B CD1 1 
ATOM   2083 C CD2 . TRP B 1 90  ? 7.863   -32.466 17.472  1.00 20.49 ? 77  TRP B CD2 1 
ATOM   2084 N NE1 . TRP B 1 90  ? 8.371   -30.594 18.586  1.00 20.54 ? 77  TRP B NE1 1 
ATOM   2085 C CE2 . TRP B 1 90  ? 8.075   -31.080 17.343  1.00 19.82 ? 77  TRP B CE2 1 
ATOM   2086 C CE3 . TRP B 1 90  ? 7.534   -33.206 16.329  1.00 20.46 ? 77  TRP B CE3 1 
ATOM   2087 C CZ2 . TRP B 1 90  ? 8.001   -30.433 16.112  1.00 20.61 ? 77  TRP B CZ2 1 
ATOM   2088 C CZ3 . TRP B 1 90  ? 7.443   -32.565 15.117  1.00 19.97 ? 77  TRP B CZ3 1 
ATOM   2089 C CH2 . TRP B 1 90  ? 7.661   -31.190 15.013  1.00 20.30 ? 77  TRP B CH2 1 
ATOM   2090 N N   . THR B 1 91  ? 5.877   -36.742 19.676  1.00 20.56 ? 78  THR B N   1 
ATOM   2091 C CA  . THR B 1 91  ? 6.131   -38.204 19.612  1.00 18.83 ? 78  THR B CA  1 
ATOM   2092 C C   . THR B 1 91  ? 6.882   -38.506 18.326  1.00 18.49 ? 78  THR B C   1 
ATOM   2093 O O   . THR B 1 91  ? 6.977   -37.626 17.441  1.00 17.54 ? 78  THR B O   1 
ATOM   2094 C CB  . THR B 1 91  ? 4.866   -39.062 19.702  1.00 18.11 ? 78  THR B CB  1 
ATOM   2095 O OG1 . THR B 1 91  ? 4.125   -38.929 18.492  1.00 17.44 ? 78  THR B OG1 1 
ATOM   2096 C CG2 . THR B 1 91  ? 3.992   -38.695 20.881  1.00 17.71 ? 78  THR B CG2 1 
ATOM   2097 N N   . GLN B 1 92  ? 7.440   -39.711 18.284  1.00 20.21 ? 79  GLN B N   1 
ATOM   2098 C CA  . GLN B 1 92  ? 8.219   -40.262 17.151  1.00 19.33 ? 79  GLN B CA  1 
ATOM   2099 C C   . GLN B 1 92  ? 7.624   -41.629 16.852  1.00 19.22 ? 79  GLN B C   1 
ATOM   2100 O O   . GLN B 1 92  ? 7.203   -42.328 17.828  1.00 16.98 ? 79  GLN B O   1 
ATOM   2101 C CB  . GLN B 1 92  ? 9.707   -40.331 17.493  1.00 19.61 ? 79  GLN B CB  1 
ATOM   2102 C CG  . GLN B 1 92  ? 10.411  -39.001 17.302  1.00 20.84 ? 79  GLN B CG  1 
ATOM   2103 C CD  . GLN B 1 92  ? 11.881  -39.056 17.637  1.00 22.71 ? 79  GLN B CD  1 
ATOM   2104 O OE1 . GLN B 1 92  ? 12.263  -39.445 18.735  1.00 23.83 ? 79  GLN B OE1 1 
ATOM   2105 N NE2 . GLN B 1 92  ? 12.712  -38.638 16.691  1.00 22.86 ? 79  GLN B NE2 1 
ATOM   2106 N N   . ASN B 1 93  ? 7.593   -41.978 15.562  1.00 19.26 ? 80  ASN B N   1 
ATOM   2107 C CA  . ASN B 1 93  ? 7.146   -43.309 15.091  1.00 19.33 ? 80  ASN B CA  1 
ATOM   2108 C C   . ASN B 1 93  ? 5.763   -43.607 15.666  1.00 18.22 ? 80  ASN B C   1 
ATOM   2109 O O   . ASN B 1 93  ? 5.613   -44.497 16.492  1.00 19.48 ? 80  ASN B O   1 
ATOM   2110 C CB  . ASN B 1 93  ? 8.167   -44.370 15.501  1.00 18.60 ? 80  ASN B CB  1 
ATOM   2111 C CG  . ASN B 1 93  ? 7.843   -45.718 14.909  1.00 19.14 ? 80  ASN B CG  1 
ATOM   2112 O OD1 . ASN B 1 93  ? 7.109   -45.807 13.924  1.00 18.77 ? 80  ASN B OD1 1 
ATOM   2113 N ND2 . ASN B 1 93  ? 8.385   -46.762 15.508  1.00 19.23 ? 80  ASN B ND2 1 
ATOM   2114 N N   . PRO B 1 94  ? 4.707   -42.859 15.285  1.00 18.30 ? 81  PRO B N   1 
ATOM   2115 C CA  . PRO B 1 94  ? 4.800   -41.777 14.306  1.00 17.59 ? 81  PRO B CA  1 
ATOM   2116 C C   . PRO B 1 94  ? 5.253   -40.412 14.834  1.00 17.72 ? 81  PRO B C   1 
ATOM   2117 O O   . PRO B 1 94  ? 5.057   -40.084 15.997  1.00 15.63 ? 81  PRO B O   1 
ATOM   2118 C CB  . PRO B 1 94  ? 3.348   -41.567 13.901  1.00 17.67 ? 81  PRO B CB  1 
ATOM   2119 C CG  . PRO B 1 94  ? 2.597   -41.839 15.187  1.00 18.01 ? 81  PRO B CG  1 
ATOM   2120 C CD  . PRO B 1 94  ? 3.340   -43.013 15.804  1.00 18.03 ? 81  PRO B CD  1 
ATOM   2121 N N   . LEU B 1 95  ? 5.790   -39.619 13.916  1.00 18.34 ? 82  LEU B N   1 
ATOM   2122 C CA  . LEU B 1 95  ? 6.211   -38.232 14.191  1.00 19.42 ? 82  LEU B CA  1 
ATOM   2123 C C   . LEU B 1 95  ? 4.948   -37.394 14.417  1.00 19.73 ? 82  LEU B C   1 
ATOM   2124 O O   . LEU B 1 95  ? 4.151   -37.311 13.480  1.00 19.39 ? 82  LEU B O   1 
ATOM   2125 C CB  . LEU B 1 95  ? 7.040   -37.742 13.001  1.00 19.15 ? 82  LEU B CB  1 
ATOM   2126 C CG  . LEU B 1 95  ? 7.740   -36.404 13.186  1.00 18.26 ? 82  LEU B CG  1 
ATOM   2127 C CD1 . LEU B 1 95  ? 8.596   -36.418 14.453  1.00 18.75 ? 82  LEU B CD1 1 
ATOM   2128 C CD2 . LEU B 1 95  ? 8.546   -36.066 11.940  1.00 17.10 ? 82  LEU B CD2 1 
ATOM   2129 N N   . VAL B 1 96  ? 4.789   -36.814 15.616  1.00 20.45 ? 83  VAL B N   1 
ATOM   2130 C CA  . VAL B 1 96  ? 3.621   -35.957 16.008  1.00 20.93 ? 83  VAL B CA  1 
ATOM   2131 C C   . VAL B 1 96  ? 4.124   -34.759 16.812  1.00 20.28 ? 83  VAL B C   1 
ATOM   2132 O O   . VAL B 1 96  ? 4.833   -34.982 17.788  1.00 20.96 ? 83  VAL B O   1 
ATOM   2133 C CB  . VAL B 1 96  ? 2.580   -36.730 16.837  1.00 20.43 ? 83  VAL B CB  1 
ATOM   2134 C CG1 . VAL B 1 96  ? 1.485   -35.813 17.379  1.00 21.34 ? 83  VAL B CG1 1 
ATOM   2135 C CG2 . VAL B 1 96  ? 1.986   -37.880 16.054  1.00 20.26 ? 83  VAL B CG2 1 
ATOM   2136 N N   . GLU B 1 97  ? 3.736   -33.549 16.410  1.00 20.34 ? 84  GLU B N   1 
ATOM   2137 C CA  . GLU B 1 97  ? 3.824   -32.315 17.233  1.00 19.52 ? 84  GLU B CA  1 
ATOM   2138 C C   . GLU B 1 97  ? 2.454   -32.116 17.893  1.00 20.07 ? 84  GLU B C   1 
ATOM   2139 O O   . GLU B 1 97  ? 1.438   -32.126 17.178  1.00 16.69 ? 84  GLU B O   1 
ATOM   2140 C CB  . GLU B 1 97  ? 4.203   -31.139 16.344  1.00 19.54 ? 84  GLU B CB  1 
ATOM   2141 C CG  . GLU B 1 97  ? 4.391   -29.828 17.078  1.00 19.46 ? 84  GLU B CG  1 
ATOM   2142 C CD  . GLU B 1 97  ? 4.773   -28.715 16.123  1.00 19.49 ? 84  GLU B CD  1 
ATOM   2143 O OE1 . GLU B 1 97  ? 5.688   -27.897 16.454  1.00 19.34 ? 84  GLU B OE1 1 
ATOM   2144 O OE2 . GLU B 1 97  ? 4.164   -28.691 15.028  1.00 18.99 ? 84  GLU B OE2 1 
ATOM   2145 N N   . TYR B 1 98  ? 2.412   -32.001 19.221  1.00 19.71 ? 85  TYR B N   1 
ATOM   2146 C CA  . TYR B 1 98  ? 1.141   -31.803 19.950  1.00 19.81 ? 85  TYR B CA  1 
ATOM   2147 C C   . TYR B 1 98  ? 1.214   -30.515 20.794  1.00 20.10 ? 85  TYR B C   1 
ATOM   2148 O O   . TYR B 1 98  ? 2.325   -30.098 21.264  1.00 18.36 ? 85  TYR B O   1 
ATOM   2149 C CB  . TYR B 1 98  ? 0.770   -33.091 20.693  1.00 19.90 ? 85  TYR B CB  1 
ATOM   2150 C CG  . TYR B 1 98  ? 1.678   -33.484 21.832  1.00 20.02 ? 85  TYR B CG  1 
ATOM   2151 C CD1 . TYR B 1 98  ? 1.588   -32.860 23.069  1.00 19.08 ? 85  TYR B CD1 1 
ATOM   2152 C CD2 . TYR B 1 98  ? 2.611   -34.498 21.680  1.00 19.99 ? 85  TYR B CD2 1 
ATOM   2153 C CE1 . TYR B 1 98  ? 2.422   -33.205 24.113  1.00 19.48 ? 85  TYR B CE1 1 
ATOM   2154 C CE2 . TYR B 1 98  ? 3.436   -34.870 22.727  1.00 20.53 ? 85  TYR B CE2 1 
ATOM   2155 C CZ  . TYR B 1 98  ? 3.353   -34.210 23.942  1.00 20.94 ? 85  TYR B CZ  1 
ATOM   2156 O OH  . TYR B 1 98  ? 4.179   -34.567 24.976  1.00 23.30 ? 85  TYR B OH  1 
ATOM   2157 N N   . TYR B 1 99  ? 0.030   -29.902 20.959  1.00 20.24 ? 86  TYR B N   1 
ATOM   2158 C CA  . TYR B 1 99  ? -0.232  -28.666 21.739  1.00 19.47 ? 86  TYR B CA  1 
ATOM   2159 C C   . TYR B 1 99  ? -1.486  -28.822 22.600  1.00 18.86 ? 86  TYR B C   1 
ATOM   2160 O O   . TYR B 1 99  ? -2.554  -29.116 22.056  1.00 18.63 ? 86  TYR B O   1 
ATOM   2161 C CB  . TYR B 1 99  ? -0.562  -27.488 20.828  1.00 18.79 ? 86  TYR B CB  1 
ATOM   2162 C CG  . TYR B 1 99  ? 0.529   -26.976 19.928  1.00 18.95 ? 86  TYR B CG  1 
ATOM   2163 C CD1 . TYR B 1 99  ? 0.826   -27.607 18.730  1.00 19.05 ? 86  TYR B CD1 1 
ATOM   2164 C CD2 . TYR B 1 99  ? 1.187   -25.790 20.217  1.00 18.78 ? 86  TYR B CD2 1 
ATOM   2165 C CE1 . TYR B 1 99  ? 1.791   -27.102 17.870  1.00 18.94 ? 86  TYR B CE1 1 
ATOM   2166 C CE2 . TYR B 1 99  ? 2.153   -25.273 19.367  1.00 19.21 ? 86  TYR B CE2 1 
ATOM   2167 C CZ  . TYR B 1 99  ? 2.453   -25.929 18.187  1.00 19.29 ? 86  TYR B CZ  1 
ATOM   2168 O OH  . TYR B 1 99  ? 3.382   -25.410 17.330  1.00 21.45 ? 86  TYR B OH  1 
ATOM   2169 N N   . ILE B 1 100 ? -1.355  -28.577 23.900  1.00 19.13 ? 87  ILE B N   1 
ATOM   2170 C CA  . ILE B 1 100 ? -2.494  -28.372 24.841  1.00 18.95 ? 87  ILE B CA  1 
ATOM   2171 C C   . ILE B 1 100 ? -2.519  -26.884 25.152  1.00 18.22 ? 87  ILE B C   1 
ATOM   2172 O O   . ILE B 1 100 ? -1.718  -26.462 25.986  1.00 18.89 ? 87  ILE B O   1 
ATOM   2173 C CB  . ILE B 1 100 ? -2.320  -29.206 26.117  1.00 19.27 ? 87  ILE B CB  1 
ATOM   2174 C CG1 . ILE B 1 100 ? -2.266  -30.698 25.780  1.00 19.44 ? 87  ILE B CG1 1 
ATOM   2175 C CG2 . ILE B 1 100 ? -3.414  -28.864 27.127  1.00 19.35 ? 87  ILE B CG2 1 
ATOM   2176 C CD1 . ILE B 1 100 ? -1.691  -31.557 26.866  1.00 19.98 ? 87  ILE B CD1 1 
ATOM   2177 N N   . VAL B 1 101 ? -3.303  -26.111 24.409  1.00 17.36 ? 88  VAL B N   1 
ATOM   2178 C CA  . VAL B 1 101 ? -3.196  -24.625 24.430  1.00 17.47 ? 88  VAL B CA  1 
ATOM   2179 C C   . VAL B 1 101 ? -4.018  -24.099 25.606  1.00 18.23 ? 88  VAL B C   1 
ATOM   2180 O O   . VAL B 1 101 ? -5.268  -24.293 25.630  1.00 17.29 ? 88  VAL B O   1 
ATOM   2181 C CB  . VAL B 1 101 ? -3.614  -23.982 23.100  1.00 16.64 ? 88  VAL B CB  1 
ATOM   2182 C CG1 . VAL B 1 101 ? -3.621  -22.465 23.192  1.00 16.51 ? 88  VAL B CG1 1 
ATOM   2183 C CG2 . VAL B 1 101 ? -2.728  -24.453 21.966  1.00 17.01 ? 88  VAL B CG2 1 
ATOM   2184 N N   . GLU B 1 102 ? -3.302  -23.485 26.541  1.00 19.18 ? 89  GLU B N   1 
ATOM   2185 C CA  . GLU B 1 102 ? -3.829  -22.829 27.757  1.00 20.16 ? 89  GLU B CA  1 
ATOM   2186 C C   . GLU B 1 102 ? -4.289  -21.423 27.384  1.00 20.16 ? 89  GLU B C   1 
ATOM   2187 O O   . GLU B 1 102 ? -5.336  -20.976 27.865  1.00 19.66 ? 89  GLU B O   1 
ATOM   2188 C CB  . GLU B 1 102 ? -2.723  -22.817 28.805  1.00 20.95 ? 89  GLU B CB  1 
ATOM   2189 C CG  . GLU B 1 102 ? -2.428  -24.210 29.309  1.00 21.97 ? 89  GLU B CG  1 
ATOM   2190 C CD  . GLU B 1 102 ? -3.591  -24.730 30.135  1.00 22.69 ? 89  GLU B CD  1 
ATOM   2191 O OE1 . GLU B 1 102 ? -4.461  -25.428 29.559  1.00 21.81 ? 89  GLU B OE1 1 
ATOM   2192 O OE2 . GLU B 1 102 ? -3.640  -24.386 31.341  1.00 22.15 ? 89  GLU B OE2 1 
ATOM   2193 N N   . SER B 1 103 ? -3.550  -20.766 26.505  1.00 20.24 ? 90  SER B N   1 
ATOM   2194 C CA  . SER B 1 103 ? -3.936  -19.428 26.008  1.00 20.77 ? 90  SER B CA  1 
ATOM   2195 C C   . SER B 1 103 ? -3.302  -19.157 24.641  1.00 19.73 ? 90  SER B C   1 
ATOM   2196 O O   . SER B 1 103 ? -2.157  -19.582 24.405  1.00 19.27 ? 90  SER B O   1 
ATOM   2197 C CB  . SER B 1 103 ? -3.580  -18.377 27.028  1.00 20.93 ? 90  SER B CB  1 
ATOM   2198 O OG  . SER B 1 103 ? -4.138  -17.139 26.650  1.00 24.07 ? 90  SER B OG  1 
ATOM   2199 N N   . PHE B 1 104 ? -4.054  -18.462 23.783  1.00 20.38 ? 91  PHE B N   1 
ATOM   2200 C CA  . PHE B 1 104 ? -3.581  -17.816 22.534  1.00 19.08 ? 91  PHE B CA  1 
ATOM   2201 C C   . PHE B 1 104 ? -4.069  -16.366 22.548  1.00 20.22 ? 91  PHE B C   1 
ATOM   2202 O O   . PHE B 1 104 ? -5.107  -16.087 23.193  1.00 18.14 ? 91  PHE B O   1 
ATOM   2203 C CB  . PHE B 1 104 ? -4.028  -18.626 21.319  1.00 18.25 ? 91  PHE B CB  1 
ATOM   2204 C CG  . PHE B 1 104 ? -5.504  -18.634 21.044  1.00 17.60 ? 91  PHE B CG  1 
ATOM   2205 C CD1 . PHE B 1 104 ? -6.137  -17.521 20.511  1.00 17.59 ? 91  PHE B CD1 1 
ATOM   2206 C CD2 . PHE B 1 104 ? -6.265  -19.763 21.300  1.00 18.00 ? 91  PHE B CD2 1 
ATOM   2207 C CE1 . PHE B 1 104 ? -7.500  -17.540 20.252  1.00 17.62 ? 91  PHE B CE1 1 
ATOM   2208 C CE2 . PHE B 1 104 ? -7.629  -19.785 21.030  1.00 17.61 ? 91  PHE B CE2 1 
ATOM   2209 C CZ  . PHE B 1 104 ? -8.241  -18.674 20.504  1.00 17.77 ? 91  PHE B CZ  1 
ATOM   2210 N N   . SER B 1 105 ? -3.327  -15.472 21.885  1.00 21.74 ? 92  SER B N   1 
ATOM   2211 C CA  . SER B 1 105 ? -3.554  -14.007 21.907  1.00 23.20 ? 92  SER B CA  1 
ATOM   2212 C C   . SER B 1 105 ? -4.458  -13.584 20.739  1.00 24.17 ? 92  SER B C   1 
ATOM   2213 O O   . SER B 1 105 ? -5.650  -13.350 20.962  1.00 30.08 ? 92  SER B O   1 
ATOM   2214 C CB  . SER B 1 105 ? -2.242  -13.290 21.872  1.00 26.20 ? 92  SER B CB  1 
ATOM   2215 O OG  . SER B 1 105 ? -1.499  -13.685 20.717  1.00 29.23 ? 92  SER B OG  1 
ATOM   2216 N N   . THR B 1 106 ? -3.917  -13.471 19.531  1.00 23.61 ? 93  THR B N   1 
ATOM   2217 C CA  . THR B 1 106 ? -4.570  -12.768 18.393  1.00 23.46 ? 93  THR B CA  1 
ATOM   2218 C C   . THR B 1 106 ? -4.912  -13.760 17.276  1.00 23.29 ? 93  THR B C   1 
ATOM   2219 O O   . THR B 1 106 ? -5.501  -13.338 16.251  1.00 24.11 ? 93  THR B O   1 
ATOM   2220 C CB  . THR B 1 106 ? -3.675  -11.622 17.897  1.00 23.08 ? 93  THR B CB  1 
ATOM   2221 O OG1 . THR B 1 106 ? -2.385  -12.155 17.601  1.00 21.98 ? 93  THR B OG1 1 
ATOM   2222 C CG2 . THR B 1 106 ? -3.537  -10.510 18.915  1.00 22.60 ? 93  THR B CG2 1 
ATOM   2223 N N   . TYR B 1 107 ? -4.582  -15.035 17.462  1.00 22.92 ? 94  TYR B N   1 
ATOM   2224 C CA  . TYR B 1 107 ? -4.752  -16.068 16.416  1.00 22.78 ? 94  TYR B CA  1 
ATOM   2225 C C   . TYR B 1 107 ? -5.053  -17.420 17.069  1.00 23.06 ? 94  TYR B C   1 
ATOM   2226 O O   . TYR B 1 107 ? -4.262  -17.911 17.891  1.00 24.07 ? 94  TYR B O   1 
ATOM   2227 C CB  . TYR B 1 107 ? -3.518  -16.128 15.513  1.00 22.19 ? 94  TYR B CB  1 
ATOM   2228 C CG  . TYR B 1 107 ? -3.704  -17.081 14.367  1.00 21.18 ? 94  TYR B CG  1 
ATOM   2229 C CD1 . TYR B 1 107 ? -4.478  -16.743 13.266  1.00 21.36 ? 94  TYR B CD1 1 
ATOM   2230 C CD2 . TYR B 1 107 ? -3.199  -18.362 14.438  1.00 21.34 ? 94  TYR B CD2 1 
ATOM   2231 C CE1 . TYR B 1 107 ? -4.678  -17.638 12.230  1.00 21.71 ? 94  TYR B CE1 1 
ATOM   2232 C CE2 . TYR B 1 107 ? -3.384  -19.270 13.412  1.00 21.38 ? 94  TYR B CE2 1 
ATOM   2233 C CZ  . TYR B 1 107 ? -4.119  -18.907 12.303  1.00 22.16 ? 94  TYR B CZ  1 
ATOM   2234 O OH  . TYR B 1 107 ? -4.300  -19.833 11.319  1.00 23.03 ? 94  TYR B OH  1 
ATOM   2235 N N   . ASP B 1 108 ? -6.200  -17.983 16.705  1.00 23.80 ? 95  ASP B N   1 
ATOM   2236 C CA  . ASP B 1 108 ? -6.628  -19.345 17.090  1.00 24.90 ? 95  ASP B CA  1 
ATOM   2237 C C   . ASP B 1 108 ? -5.894  -20.337 16.194  1.00 26.08 ? 95  ASP B C   1 
ATOM   2238 O O   . ASP B 1 108 ? -6.215  -20.440 15.011  1.00 30.11 ? 95  ASP B O   1 
ATOM   2239 C CB  . ASP B 1 108 ? -8.145  -19.489 16.993  1.00 23.82 ? 95  ASP B CB  1 
ATOM   2240 C CG  . ASP B 1 108 ? -8.608  -20.809 17.560  1.00 23.46 ? 95  ASP B CG  1 
ATOM   2241 O OD1 . ASP B 1 108 ? -7.759  -21.693 17.661  1.00 24.22 ? 95  ASP B OD1 1 
ATOM   2242 O OD2 . ASP B 1 108 ? -9.795  -20.925 17.939  1.00 24.05 ? 95  ASP B OD2 1 
ATOM   2243 N N   . PRO B 1 109 ? -4.897  -21.091 16.715  1.00 27.35 ? 96  PRO B N   1 
ATOM   2244 C CA  . PRO B 1 109 ? -4.104  -22.003 15.888  1.00 27.95 ? 96  PRO B CA  1 
ATOM   2245 C C   . PRO B 1 109 ? -4.879  -23.181 15.285  1.00 29.70 ? 96  PRO B C   1 
ATOM   2246 O O   . PRO B 1 109 ? -4.324  -23.827 14.454  1.00 32.22 ? 96  PRO B O   1 
ATOM   2247 C CB  . PRO B 1 109 ? -3.092  -22.598 16.869  1.00 29.21 ? 96  PRO B CB  1 
ATOM   2248 C CG  . PRO B 1 109 ? -3.774  -22.466 18.228  1.00 28.69 ? 96  PRO B CG  1 
ATOM   2249 C CD  . PRO B 1 109 ? -4.496  -21.142 18.134  1.00 27.95 ? 96  PRO B CD  1 
ATOM   2250 N N   . SER B 1 110 ? -6.102  -23.446 15.754  1.00 31.60 ? 97  SER B N   1 
ATOM   2251 C CA  . SER B 1 110 ? -7.003  -24.513 15.248  1.00 33.58 ? 97  SER B CA  1 
ATOM   2252 C C   . SER B 1 110 ? -7.842  -23.998 14.064  1.00 38.15 ? 97  SER B C   1 
ATOM   2253 O O   . SER B 1 110 ? -8.619  -24.811 13.480  1.00 39.50 ? 97  SER B O   1 
ATOM   2254 C CB  . SER B 1 110 ? -7.880  -25.026 16.354  1.00 31.87 ? 97  SER B CB  1 
ATOM   2255 O OG  . SER B 1 110 ? -8.800  -24.026 16.775  1.00 30.33 ? 97  SER B OG  1 
ATOM   2256 N N   . THR B 1 111 ? -7.751  -22.699 13.743  1.00 36.05 ? 98  THR B N   1 
ATOM   2257 C CA  . THR B 1 111 ? -8.320  -22.133 12.494  1.00 35.71 ? 98  THR B CA  1 
ATOM   2258 C C   . THR B 1 111 ? -7.850  -23.029 11.345  1.00 37.27 ? 98  THR B C   1 
ATOM   2259 O O   . THR B 1 111 ? -6.628  -23.235 11.225  1.00 37.69 ? 98  THR B O   1 
ATOM   2260 C CB  . THR B 1 111 ? -7.888  -20.678 12.252  1.00 33.66 ? 98  THR B CB  1 
ATOM   2261 O OG1 . THR B 1 111 ? -8.066  -19.902 13.437  1.00 28.00 ? 98  THR B OG1 1 
ATOM   2262 C CG2 . THR B 1 111 ? -8.652  -20.053 11.103  1.00 32.93 ? 98  THR B CG2 1 
ATOM   2263 N N   . GLY B 1 112 ? -8.779  -23.580 10.570  1.00 41.75 ? 99  GLY B N   1 
ATOM   2264 C CA  . GLY B 1 112 ? -8.462  -24.469 9.437   1.00 47.10 ? 99  GLY B CA  1 
ATOM   2265 C C   . GLY B 1 112 ? -8.623  -25.925 9.822   1.00 49.47 ? 99  GLY B C   1 
ATOM   2266 O O   . GLY B 1 112 ? -9.407  -26.621 9.151   1.00 54.25 ? 99  GLY B O   1 
ATOM   2267 N N   . ALA B 1 113 ? -7.935  -26.349 10.886  1.00 48.65 ? 100 ALA B N   1 
ATOM   2268 C CA  . ALA B 1 113 ? -7.969  -27.717 11.459  1.00 48.14 ? 100 ALA B CA  1 
ATOM   2269 C C   . ALA B 1 113 ? -9.405  -28.232 11.544  1.00 46.44 ? 100 ALA B C   1 
ATOM   2270 O O   . ALA B 1 113 ? -10.325 -27.397 11.588  1.00 44.03 ? 100 ALA B O   1 
ATOM   2271 C CB  . ALA B 1 113 ? -7.332  -27.733 12.826  1.00 50.02 ? 100 ALA B CB  1 
ATOM   2272 N N   . GLN B 1 114 ? -9.559  -29.563 11.581  1.00 49.03 ? 101 GLN B N   1 
ATOM   2273 C CA  . GLN B 1 114 ? -10.860 -30.280 11.692  1.00 48.80 ? 101 GLN B CA  1 
ATOM   2274 C C   . GLN B 1 114 ? -11.089 -30.651 13.165  1.00 44.04 ? 101 GLN B C   1 
ATOM   2275 O O   . GLN B 1 114 ? -10.209 -31.358 13.742  1.00 40.45 ? 101 GLN B O   1 
ATOM   2276 C CB  . GLN B 1 114 ? -10.861 -31.496 10.753  1.00 53.61 ? 101 GLN B CB  1 
ATOM   2277 C CG  . GLN B 1 114 ? -12.071 -32.420 10.904  1.00 58.07 ? 101 GLN B CG  1 
ATOM   2278 C CD  . GLN B 1 114 ? -13.400 -31.701 10.863  1.00 61.90 ? 101 GLN B CD  1 
ATOM   2279 O OE1 . GLN B 1 114 ? -14.291 -31.954 11.674  1.00 61.80 ? 101 GLN B OE1 1 
ATOM   2280 N NE2 . GLN B 1 114 ? -13.549 -30.792 9.911   1.00 67.89 ? 101 GLN B NE2 1 
ATOM   2281 N N   . GLU B 1 115 ? -12.211 -30.185 13.736  1.00 38.36 ? 102 GLU B N   1 
ATOM   2282 C CA  . GLU B 1 115 ? -12.585 -30.378 15.162  1.00 37.63 ? 102 GLU B CA  1 
ATOM   2283 C C   . GLU B 1 115 ? -13.114 -31.796 15.360  1.00 38.77 ? 102 GLU B C   1 
ATOM   2284 O O   . GLU B 1 115 ? -14.080 -32.155 14.657  1.00 45.69 ? 102 GLU B O   1 
ATOM   2285 C CB  . GLU B 1 115 ? -13.658 -29.401 15.638  1.00 38.15 ? 102 GLU B CB  1 
ATOM   2286 C CG  . GLU B 1 115 ? -14.273 -29.833 16.959  1.00 39.16 ? 102 GLU B CG  1 
ATOM   2287 C CD  . GLU B 1 115 ? -14.908 -28.742 17.797  1.00 43.91 ? 102 GLU B CD  1 
ATOM   2288 O OE1 . GLU B 1 115 ? -15.288 -29.046 18.961  1.00 44.61 ? 102 GLU B OE1 1 
ATOM   2289 O OE2 . GLU B 1 115 ? -15.016 -27.594 17.297  1.00 45.64 ? 102 GLU B OE2 1 
ATOM   2290 N N   . LEU B 1 116 ? -12.537 -32.537 16.312  1.00 33.69 ? 103 LEU B N   1 
ATOM   2291 C CA  . LEU B 1 116 ? -12.760 -33.994 16.483  1.00 32.42 ? 103 LEU B CA  1 
ATOM   2292 C C   . LEU B 1 116 ? -13.551 -34.276 17.756  1.00 32.88 ? 103 LEU B C   1 
ATOM   2293 O O   . LEU B 1 116 ? -13.882 -35.451 17.967  1.00 37.92 ? 103 LEU B O   1 
ATOM   2294 C CB  . LEU B 1 116 ? -11.404 -34.706 16.531  1.00 31.24 ? 103 LEU B CB  1 
ATOM   2295 C CG  . LEU B 1 116 ? -10.570 -34.587 15.259  1.00 31.52 ? 103 LEU B CG  1 
ATOM   2296 C CD1 . LEU B 1 116 ? -9.249  -35.314 15.401  1.00 32.43 ? 103 LEU B CD1 1 
ATOM   2297 C CD2 . LEU B 1 116 ? -11.341 -35.110 14.060  1.00 32.14 ? 103 LEU B CD2 1 
ATOM   2298 N N   . GLY B 1 117 ? -13.809 -33.270 18.590  1.00 30.48 ? 104 GLY B N   1 
ATOM   2299 C CA  . GLY B 1 117 ? -14.462 -33.487 19.891  1.00 29.97 ? 104 GLY B CA  1 
ATOM   2300 C C   . GLY B 1 117 ? -13.942 -32.540 20.942  1.00 29.57 ? 104 GLY B C   1 
ATOM   2301 O O   . GLY B 1 117 ? -13.154 -31.652 20.585  1.00 28.34 ? 104 GLY B O   1 
ATOM   2302 N N   . THR B 1 118 ? -14.396 -32.717 22.183  1.00 28.49 ? 105 THR B N   1 
ATOM   2303 C CA  . THR B 1 118 ? -13.996 -31.885 23.337  1.00 29.60 ? 105 THR B CA  1 
ATOM   2304 C C   . THR B 1 118 ? -13.600 -32.795 24.497  1.00 29.12 ? 105 THR B C   1 
ATOM   2305 O O   . THR B 1 118 ? -14.103 -33.911 24.566  1.00 30.42 ? 105 THR B O   1 
ATOM   2306 C CB  . THR B 1 118 ? -15.093 -30.888 23.718  1.00 29.37 ? 105 THR B CB  1 
ATOM   2307 O OG1 . THR B 1 118 ? -16.207 -31.648 24.148  1.00 28.26 ? 105 THR B OG1 1 
ATOM   2308 C CG2 . THR B 1 118 ? -15.507 -29.987 22.579  1.00 31.33 ? 105 THR B CG2 1 
ATOM   2309 N N   . VAL B 1 119 ? -12.702 -32.323 25.358  1.00 28.48 ? 106 VAL B N   1 
ATOM   2310 C CA  . VAL B 1 119 ? -12.285 -33.059 26.584  1.00 27.42 ? 106 VAL B CA  1 
ATOM   2311 C C   . VAL B 1 119 ? -12.402 -32.079 27.749  1.00 26.87 ? 106 VAL B C   1 
ATOM   2312 O O   . VAL B 1 119 ? -11.965 -30.897 27.598  1.00 25.45 ? 106 VAL B O   1 
ATOM   2313 C CB  . VAL B 1 119 ? -10.884 -33.687 26.444  1.00 27.08 ? 106 VAL B CB  1 
ATOM   2314 C CG1 . VAL B 1 119 ? -9.848  -32.678 25.981  1.00 26.97 ? 106 VAL B CG1 1 
ATOM   2315 C CG2 . VAL B 1 119 ? -10.434 -34.375 27.724  1.00 27.00 ? 106 VAL B CG2 1 
ATOM   2316 N N   . GLU B 1 120 ? -13.054 -32.538 28.818  1.00 26.64 ? 107 GLU B N   1 
ATOM   2317 C CA  . GLU B 1 120 ? -13.288 -31.764 30.052  1.00 28.32 ? 107 GLU B CA  1 
ATOM   2318 C C   . GLU B 1 120 ? -12.286 -32.289 31.069  1.00 27.47 ? 107 GLU B C   1 
ATOM   2319 O O   . GLU B 1 120 ? -12.342 -33.468 31.377  1.00 29.73 ? 107 GLU B O   1 
ATOM   2320 C CB  . GLU B 1 120 ? -14.739 -31.894 30.510  1.00 34.00 ? 107 GLU B CB  1 
ATOM   2321 C CG  . GLU B 1 120 ? -15.744 -31.449 29.456  1.00 39.64 ? 107 GLU B CG  1 
ATOM   2322 C CD  . GLU B 1 120 ? -17.206 -31.515 29.873  1.00 44.03 ? 107 GLU B CD  1 
ATOM   2323 O OE1 . GLU B 1 120 ? -17.547 -31.000 30.967  1.00 44.55 ? 107 GLU B OE1 1 
ATOM   2324 O OE2 . GLU B 1 120 ? -18.004 -32.084 29.099  1.00 50.10 ? 107 GLU B OE2 1 
ATOM   2325 N N   . THR B 1 121 ? -11.357 -31.434 31.491  1.00 27.03 ? 108 THR B N   1 
ATOM   2326 C CA  . THR B 1 121 ? -10.221 -31.749 32.392  1.00 24.99 ? 108 THR B CA  1 
ATOM   2327 C C   . THR B 1 121 ? -9.720  -30.419 32.952  1.00 24.60 ? 108 THR B C   1 
ATOM   2328 O O   . THR B 1 121 ? -9.885  -29.417 32.251  1.00 23.67 ? 108 THR B O   1 
ATOM   2329 C CB  . THR B 1 121 ? -9.142  -32.530 31.635  1.00 24.02 ? 108 THR B CB  1 
ATOM   2330 O OG1 . THR B 1 121 ? -8.089  -32.863 32.531  1.00 21.52 ? 108 THR B OG1 1 
ATOM   2331 C CG2 . THR B 1 121 ? -8.574  -31.762 30.460  1.00 24.68 ? 108 THR B CG2 1 
ATOM   2332 N N   . ASP B 1 122 ? -9.174  -30.428 34.171  1.00 26.27 ? 109 ASP B N   1 
ATOM   2333 C CA  . ASP B 1 122 ? -8.521  -29.268 34.842  1.00 26.71 ? 109 ASP B CA  1 
ATOM   2334 C C   . ASP B 1 122 ? -9.452  -28.054 34.867  1.00 28.06 ? 109 ASP B C   1 
ATOM   2335 O O   . ASP B 1 122 ? -8.988  -26.936 34.586  1.00 29.86 ? 109 ASP B O   1 
ATOM   2336 C CB  . ASP B 1 122 ? -7.180  -29.015 34.172  1.00 26.73 ? 109 ASP B CB  1 
ATOM   2337 C CG  . ASP B 1 122 ? -6.376  -30.302 34.133  1.00 26.59 ? 109 ASP B CG  1 
ATOM   2338 O OD1 . ASP B 1 122 ? -6.121  -30.861 35.219  1.00 24.60 ? 109 ASP B OD1 1 
ATOM   2339 O OD2 . ASP B 1 122 ? -6.053  -30.756 33.018  1.00 27.73 ? 109 ASP B OD2 1 
ATOM   2340 N N   . ASP B 1 123 ? -10.719 -28.296 35.201  1.00 30.37 ? 110 ASP B N   1 
ATOM   2341 C CA  . ASP B 1 123 ? -11.774 -27.278 35.433  1.00 33.48 ? 110 ASP B CA  1 
ATOM   2342 C C   . ASP B 1 123 ? -11.941 -26.488 34.132  1.00 33.31 ? 110 ASP B C   1 
ATOM   2343 O O   . ASP B 1 123 ? -12.287 -25.306 34.189  1.00 33.52 ? 110 ASP B O   1 
ATOM   2344 C CB  . ASP B 1 123 ? -11.477 -26.469 36.701  1.00 37.78 ? 110 ASP B CB  1 
ATOM   2345 C CG  . ASP B 1 123 ? -11.276 -27.354 37.934  1.00 43.19 ? 110 ASP B CG  1 
ATOM   2346 O OD1 . ASP B 1 123 ? -12.290 -27.860 38.474  1.00 42.00 ? 110 ASP B OD1 1 
ATOM   2347 O OD2 . ASP B 1 123 ? -10.091 -27.575 38.332  1.00 47.98 ? 110 ASP B OD2 1 
ATOM   2348 N N   . GLY B 1 124 ? -11.777 -27.167 32.994  1.00 31.68 ? 111 GLY B N   1 
ATOM   2349 C CA  . GLY B 1 124 ? -11.928 -26.556 31.663  1.00 29.98 ? 111 GLY B CA  1 
ATOM   2350 C C   . GLY B 1 124 ? -12.487 -27.518 30.629  1.00 27.77 ? 111 GLY B C   1 
ATOM   2351 O O   . GLY B 1 124 ? -12.566 -28.745 30.895  1.00 22.75 ? 111 GLY B O   1 
ATOM   2352 N N   . THR B 1 125 ? -12.855 -26.938 29.487  1.00 26.28 ? 112 THR B N   1 
ATOM   2353 C CA  . THR B 1 125 ? -13.248 -27.600 28.229  1.00 26.21 ? 112 THR B CA  1 
ATOM   2354 C C   . THR B 1 125 ? -12.178 -27.327 27.186  1.00 25.85 ? 112 THR B C   1 
ATOM   2355 O O   . THR B 1 125 ? -11.855 -26.154 26.982  1.00 27.16 ? 112 THR B O   1 
ATOM   2356 C CB  . THR B 1 125 ? -14.575 -27.044 27.714  1.00 28.13 ? 112 THR B CB  1 
ATOM   2357 O OG1 . THR B 1 125 ? -15.464 -27.152 28.819  1.00 28.47 ? 112 THR B OG1 1 
ATOM   2358 C CG2 . THR B 1 125 ? -15.110 -27.794 26.512  1.00 29.33 ? 112 THR B CG2 1 
ATOM   2359 N N   . TYR B 1 126 ? -11.669 -28.368 26.536  1.00 26.44 ? 113 TYR B N   1 
ATOM   2360 C CA  . TYR B 1 126 ? -10.690 -28.229 25.434  1.00 25.40 ? 113 TYR B CA  1 
ATOM   2361 C C   . TYR B 1 126 ? -11.311 -28.786 24.166  1.00 26.31 ? 113 TYR B C   1 
ATOM   2362 O O   . TYR B 1 126 ? -11.888 -29.882 24.229  1.00 31.07 ? 113 TYR B O   1 
ATOM   2363 C CB  . TYR B 1 126 ? -9.388  -28.941 25.786  1.00 25.59 ? 113 TYR B CB  1 
ATOM   2364 C CG  . TYR B 1 126 ? -8.630  -28.344 26.944  1.00 23.89 ? 113 TYR B CG  1 
ATOM   2365 C CD1 . TYR B 1 126 ? -9.054  -28.521 28.251  1.00 23.39 ? 113 TYR B CD1 1 
ATOM   2366 C CD2 . TYR B 1 126 ? -7.450  -27.646 26.735  1.00 23.75 ? 113 TYR B CD2 1 
ATOM   2367 C CE1 . TYR B 1 126 ? -8.329  -28.006 29.317  1.00 23.82 ? 113 TYR B CE1 1 
ATOM   2368 C CE2 . TYR B 1 126 ? -6.723  -27.108 27.786  1.00 23.07 ? 113 TYR B CE2 1 
ATOM   2369 C CZ  . TYR B 1 126 ? -7.161  -27.292 29.084  1.00 22.98 ? 113 TYR B CZ  1 
ATOM   2370 O OH  . TYR B 1 126 ? -6.438  -26.769 30.117  1.00 22.36 ? 113 TYR B OH  1 
ATOM   2371 N N   . LYS B 1 127 ? -11.221 -28.043 23.066  1.00 26.74 ? 114 LYS B N   1 
ATOM   2372 C CA  . LYS B 1 127 ? -11.622 -28.534 21.725  1.00 26.74 ? 114 LYS B CA  1 
ATOM   2373 C C   . LYS B 1 127 ? -10.395 -29.189 21.090  1.00 24.99 ? 114 LYS B C   1 
ATOM   2374 O O   . LYS B 1 127 ? -9.268  -28.651 21.220  1.00 22.31 ? 114 LYS B O   1 
ATOM   2375 C CB  . LYS B 1 127 ? -12.201 -27.407 20.869  1.00 30.48 ? 114 LYS B CB  1 
ATOM   2376 C CG  . LYS B 1 127 ? -13.424 -26.708 21.452  1.00 33.06 ? 114 LYS B CG  1 
ATOM   2377 C CD  . LYS B 1 127 ? -14.113 -25.783 20.458  1.00 37.24 ? 114 LYS B CD  1 
ATOM   2378 C CE  . LYS B 1 127 ? -15.088 -24.810 21.100  1.00 41.82 ? 114 LYS B CE  1 
ATOM   2379 N NZ  . LYS B 1 127 ? -15.742 -23.929 20.098  1.00 42.85 ? 114 LYS B NZ  1 
ATOM   2380 N N   . ILE B 1 128 ? -10.626 -30.332 20.462  1.00 25.19 ? 115 ILE B N   1 
ATOM   2381 C CA  . ILE B 1 128 ? -9.588  -31.274 19.962  1.00 25.08 ? 115 ILE B CA  1 
ATOM   2382 C C   . ILE B 1 128 ? -9.538  -31.112 18.449  1.00 24.20 ? 115 ILE B C   1 
ATOM   2383 O O   . ILE B 1 128 ? -10.623 -31.112 17.847  1.00 23.74 ? 115 ILE B O   1 
ATOM   2384 C CB  . ILE B 1 128 ? -9.937  -32.720 20.379  1.00 26.47 ? 115 ILE B CB  1 
ATOM   2385 C CG1 . ILE B 1 128 ? -9.916  -32.869 21.905  1.00 27.34 ? 115 ILE B CG1 1 
ATOM   2386 C CG2 . ILE B 1 128 ? -9.025  -33.722 19.686  1.00 26.08 ? 115 ILE B CG2 1 
ATOM   2387 C CD1 . ILE B 1 128 ? -10.384 -34.229 22.422  1.00 29.44 ? 115 ILE B CD1 1 
ATOM   2388 N N   . TYR B 1 129 ? -8.343  -30.976 17.866  1.00 23.21 ? 116 TYR B N   1 
ATOM   2389 C CA  . TYR B 1 129 ? -8.161  -30.785 16.407  1.00 21.69 ? 116 TYR B CA  1 
ATOM   2390 C C   . TYR B 1 129 ? -6.974  -31.593 15.919  1.00 23.31 ? 116 TYR B C   1 
ATOM   2391 O O   . TYR B 1 129 ? -6.078  -31.931 16.722  1.00 24.82 ? 116 TYR B O   1 
ATOM   2392 C CB  . TYR B 1 129 ? -7.901  -29.322 16.064  1.00 21.43 ? 116 TYR B CB  1 
ATOM   2393 C CG  . TYR B 1 129 ? -8.955  -28.362 16.545  1.00 21.90 ? 116 TYR B CG  1 
ATOM   2394 C CD1 . TYR B 1 129 ? -8.966  -27.925 17.860  1.00 21.79 ? 116 TYR B CD1 1 
ATOM   2395 C CD2 . TYR B 1 129 ? -9.918  -27.864 15.681  1.00 21.20 ? 116 TYR B CD2 1 
ATOM   2396 C CE1 . TYR B 1 129 ? -9.915  -27.024 18.310  1.00 22.81 ? 116 TYR B CE1 1 
ATOM   2397 C CE2 . TYR B 1 129 ? -10.868 -26.953 16.110  1.00 21.80 ? 116 TYR B CE2 1 
ATOM   2398 C CZ  . TYR B 1 129 ? -10.881 -26.548 17.435  1.00 23.13 ? 116 TYR B CZ  1 
ATOM   2399 O OH  . TYR B 1 129 ? -11.817 -25.660 17.883  1.00 23.77 ? 116 TYR B OH  1 
ATOM   2400 N N   . GLN B 1 130 ? -6.948  -31.833 14.611  1.00 24.49 ? 117 GLN B N   1 
ATOM   2401 C CA  . GLN B 1 130 ? -5.814  -32.479 13.922  1.00 26.06 ? 117 GLN B CA  1 
ATOM   2402 C C   . GLN B 1 130 ? -5.536  -31.709 12.631  1.00 26.53 ? 117 GLN B C   1 
ATOM   2403 O O   . GLN B 1 130 ? -6.492  -31.352 11.952  1.00 24.65 ? 117 GLN B O   1 
ATOM   2404 C CB  . GLN B 1 130 ? -6.156  -33.948 13.708  1.00 28.83 ? 117 GLN B CB  1 
ATOM   2405 C CG  . GLN B 1 130 ? -5.027  -34.744 13.085  1.00 32.33 ? 117 GLN B CG  1 
ATOM   2406 C CD  . GLN B 1 130 ? -5.375  -35.206 11.692  1.00 32.87 ? 117 GLN B CD  1 
ATOM   2407 O OE1 . GLN B 1 130 ? -5.798  -36.342 11.493  1.00 39.74 ? 117 GLN B OE1 1 
ATOM   2408 N NE2 . GLN B 1 130 ? -5.202  -34.329 10.722  1.00 31.49 ? 117 GLN B NE2 1 
ATOM   2409 N N   . THR B 1 131 ? -4.266  -31.409 12.357  1.00 28.48 ? 118 THR B N   1 
ATOM   2410 C CA  . THR B 1 131 ? -3.776  -30.818 11.085  1.00 30.20 ? 118 THR B CA  1 
ATOM   2411 C C   . THR B 1 131 ? -2.576  -31.652 10.634  1.00 30.22 ? 118 THR B C   1 
ATOM   2412 O O   . THR B 1 131 ? -2.166  -32.558 11.391  1.00 27.05 ? 118 THR B O   1 
ATOM   2413 C CB  . THR B 1 131 ? -3.413  -29.327 11.219  1.00 32.95 ? 118 THR B CB  1 
ATOM   2414 O OG1 . THR B 1 131 ? -2.594  -29.067 12.362  1.00 33.36 ? 118 THR B OG1 1 
ATOM   2415 C CG2 . THR B 1 131 ? -4.621  -28.435 11.365  1.00 35.35 ? 118 THR B CG2 1 
ATOM   2416 N N   . THR B 1 132 ? -2.064  -31.353 9.442   1.00 30.58 ? 119 THR B N   1 
ATOM   2417 C CA  . THR B 1 132 ? -0.854  -31.967 8.851   1.00 31.86 ? 119 THR B CA  1 
ATOM   2418 C C   . THR B 1 132 ? 0.089   -30.842 8.436   1.00 31.08 ? 119 THR B C   1 
ATOM   2419 O O   . THR B 1 132 ? -0.392  -29.864 7.870   1.00 27.69 ? 119 THR B O   1 
ATOM   2420 C CB  . THR B 1 132 ? -1.215  -32.872 7.670   1.00 33.14 ? 119 THR B CB  1 
ATOM   2421 O OG1 . THR B 1 132 ? -2.268  -33.720 8.133   1.00 37.64 ? 119 THR B OG1 1 
ATOM   2422 C CG2 . THR B 1 132 ? -0.052  -33.703 7.167   1.00 32.72 ? 119 THR B CG2 1 
ATOM   2423 N N   . ARG B 1 133 ? 1.375   -30.990 8.745   1.00 32.06 ? 120 ARG B N   1 
ATOM   2424 C CA  . ARG B 1 133 ? 2.447   -30.073 8.303   1.00 32.64 ? 120 ARG B CA  1 
ATOM   2425 C C   . ARG B 1 133 ? 3.245   -30.813 7.233   1.00 32.98 ? 120 ARG B C   1 
ATOM   2426 O O   . ARG B 1 133 ? 3.660   -31.963 7.505   1.00 30.06 ? 120 ARG B O   1 
ATOM   2427 C CB  . ARG B 1 133 ? 3.283   -29.654 9.514   1.00 35.18 ? 120 ARG B CB  1 
ATOM   2428 C CG  . ARG B 1 133 ? 2.488   -28.857 10.538  1.00 36.81 ? 120 ARG B CG  1 
ATOM   2429 C CD  . ARG B 1 133 ? 2.323   -27.411 10.122  1.00 38.90 ? 120 ARG B CD  1 
ATOM   2430 N NE  . ARG B 1 133 ? 3.507   -26.634 10.475  1.00 42.22 ? 120 ARG B NE  1 
ATOM   2431 C CZ  . ARG B 1 133 ? 4.321   -26.008 9.621   1.00 46.34 ? 120 ARG B CZ  1 
ATOM   2432 N NH1 . ARG B 1 133 ? 4.108   -26.046 8.312   1.00 47.68 ? 120 ARG B NH1 1 
ATOM   2433 N NH2 . ARG B 1 133 ? 5.359   -25.335 10.090  1.00 45.71 ? 120 ARG B NH2 1 
ATOM   2434 N N   . GLU B 1 134 ? 3.382   -30.200 6.054   1.00 33.84 ? 121 GLU B N   1 
ATOM   2435 C CA  . GLU B 1 134 ? 4.042   -30.799 4.865   1.00 35.51 ? 121 GLU B CA  1 
ATOM   2436 C C   . GLU B 1 134 ? 5.415   -30.152 4.716   1.00 34.36 ? 121 GLU B C   1 
ATOM   2437 O O   . GLU B 1 134 ? 5.464   -28.926 4.605   1.00 32.35 ? 121 GLU B O   1 
ATOM   2438 C CB  . GLU B 1 134 ? 3.220   -30.586 3.598   1.00 38.92 ? 121 GLU B CB  1 
ATOM   2439 C CG  . GLU B 1 134 ? 1.756   -30.954 3.753   1.00 45.69 ? 121 GLU B CG  1 
ATOM   2440 C CD  . GLU B 1 134 ? 1.146   -31.736 2.599   1.00 51.56 ? 121 GLU B CD  1 
ATOM   2441 O OE1 . GLU B 1 134 ? 0.138   -32.445 2.849   1.00 52.11 ? 121 GLU B OE1 1 
ATOM   2442 O OE2 . GLU B 1 134 ? 1.679   -31.642 1.458   1.00 54.75 ? 121 GLU B OE2 1 
ATOM   2443 N N   . ASN B 1 135 ? 6.479   -30.952 4.756   1.00 33.02 ? 122 ASN B N   1 
ATOM   2444 C CA  . ASN B 1 135 ? 7.865   -30.483 4.499   1.00 32.68 ? 122 ASN B CA  1 
ATOM   2445 C C   . ASN B 1 135 ? 8.156   -29.312 5.439   1.00 31.72 ? 122 ASN B C   1 
ATOM   2446 O O   . ASN B 1 135 ? 8.628   -28.261 4.955   1.00 30.81 ? 122 ASN B O   1 
ATOM   2447 C CB  . ASN B 1 135 ? 8.061   -30.186 3.009   1.00 34.58 ? 122 ASN B CB  1 
ATOM   2448 C CG  . ASN B 1 135 ? 8.139   -31.471 2.208   1.00 36.06 ? 122 ASN B CG  1 
ATOM   2449 O OD1 . ASN B 1 135 ? 9.076   -32.254 2.381   1.00 39.10 ? 122 ASN B OD1 1 
ATOM   2450 N ND2 . ASN B 1 135 ? 7.152   -31.716 1.364   1.00 33.89 ? 122 ASN B ND2 1 
ATOM   2451 N N   . ALA B 1 136 ? 7.902   -29.527 6.737   1.00 29.44 ? 123 ALA B N   1 
ATOM   2452 C CA  . ALA B 1 136 ? 8.078   -28.541 7.823   1.00 28.02 ? 123 ALA B CA  1 
ATOM   2453 C C   . ALA B 1 136 ? 9.285   -28.934 8.668   1.00 27.73 ? 123 ALA B C   1 
ATOM   2454 O O   . ALA B 1 136 ? 9.712   -30.084 8.658   1.00 29.26 ? 123 ALA B O   1 
ATOM   2455 C CB  . ALA B 1 136 ? 6.821   -28.479 8.654   1.00 27.71 ? 123 ALA B CB  1 
ATOM   2456 N N   . PRO B 1 137 ? 9.892   -27.988 9.413   1.00 27.18 ? 124 PRO B N   1 
ATOM   2457 C CA  . PRO B 1 137 ? 10.898  -28.333 10.411  1.00 26.21 ? 124 PRO B CA  1 
ATOM   2458 C C   . PRO B 1 137 ? 10.340  -29.322 11.441  1.00 25.73 ? 124 PRO B C   1 
ATOM   2459 O O   . PRO B 1 137 ? 9.142   -29.325 11.680  1.00 26.16 ? 124 PRO B O   1 
ATOM   2460 C CB  . PRO B 1 137 ? 11.238  -26.984 11.068  1.00 28.02 ? 124 PRO B CB  1 
ATOM   2461 C CG  . PRO B 1 137 ? 10.891  -25.952 10.017  1.00 27.74 ? 124 PRO B CG  1 
ATOM   2462 C CD  . PRO B 1 137 ? 9.700   -26.530 9.282   1.00 28.34 ? 124 PRO B CD  1 
ATOM   2463 N N   . SER B 1 138 ? 11.207  -30.167 11.996  1.00 23.71 ? 125 SER B N   1 
ATOM   2464 C CA  . SER B 1 138 ? 10.827  -31.161 13.028  1.00 23.46 ? 125 SER B CA  1 
ATOM   2465 C C   . SER B 1 138 ? 12.052  -31.500 13.866  1.00 24.06 ? 125 SER B C   1 
ATOM   2466 O O   . SER B 1 138 ? 13.185  -31.182 13.446  1.00 23.36 ? 125 SER B O   1 
ATOM   2467 C CB  . SER B 1 138 ? 10.243  -32.417 12.405  1.00 24.25 ? 125 SER B CB  1 
ATOM   2468 O OG  . SER B 1 138 ? 11.242  -33.421 12.229  1.00 21.87 ? 125 SER B OG  1 
ATOM   2469 N N   . ILE B 1 139 ? 11.823  -32.215 14.958  1.00 24.87 ? 126 ILE B N   1 
ATOM   2470 C CA  . ILE B 1 139 ? 12.906  -32.740 15.833  1.00 25.94 ? 126 ILE B CA  1 
ATOM   2471 C C   . ILE B 1 139 ? 13.783  -33.745 15.056  1.00 27.69 ? 126 ILE B C   1 
ATOM   2472 O O   . ILE B 1 139 ? 14.892  -34.072 15.575  1.00 26.61 ? 126 ILE B O   1 
ATOM   2473 C CB  . ILE B 1 139 ? 12.277  -33.338 17.104  1.00 26.77 ? 126 ILE B CB  1 
ATOM   2474 C CG1 . ILE B 1 139 ? 11.400  -34.559 16.806  1.00 27.68 ? 126 ILE B CG1 1 
ATOM   2475 C CG2 . ILE B 1 139 ? 11.517  -32.251 17.868  1.00 27.51 ? 126 ILE B CG2 1 
ATOM   2476 C CD1 . ILE B 1 139 ? 11.091  -35.410 18.036  1.00 27.80 ? 126 ILE B CD1 1 
ATOM   2477 N N   . GLU B 1 140 ? 13.296  -34.236 13.898  1.00 27.34 ? 127 GLU B N   1 
ATOM   2478 C CA  . GLU B 1 140 ? 13.913  -35.291 13.032  1.00 26.39 ? 127 GLU B CA  1 
ATOM   2479 C C   . GLU B 1 140 ? 14.397  -34.710 11.695  1.00 24.36 ? 127 GLU B C   1 
ATOM   2480 O O   . GLU B 1 140 ? 14.874  -35.493 10.878  1.00 25.09 ? 127 GLU B O   1 
ATOM   2481 C CB  . GLU B 1 140 ? 12.885  -36.357 12.638  1.00 26.71 ? 127 GLU B CB  1 
ATOM   2482 C CG  . GLU B 1 140 ? 12.646  -37.424 13.671  1.00 27.97 ? 127 GLU B CG  1 
ATOM   2483 C CD  . GLU B 1 140 ? 11.637  -38.453 13.194  1.00 29.68 ? 127 GLU B CD  1 
ATOM   2484 O OE1 . GLU B 1 140 ? 11.316  -39.370 13.990  1.00 34.71 ? 127 GLU B OE1 1 
ATOM   2485 O OE2 . GLU B 1 140 ? 11.200  -38.364 12.018  1.00 26.17 ? 127 GLU B OE2 1 
ATOM   2486 N N   . GLY B 1 141 ? 14.213  -33.413 11.457  1.00 22.19 ? 128 GLY B N   1 
ATOM   2487 C CA  . GLY B 1 141 ? 14.479  -32.758 10.167  1.00 22.21 ? 128 GLY B CA  1 
ATOM   2488 C C   . GLY B 1 141 ? 13.193  -32.455 9.420   1.00 23.54 ? 128 GLY B C   1 
ATOM   2489 O O   . GLY B 1 141 ? 12.088  -32.737 9.956   1.00 24.22 ? 128 GLY B O   1 
ATOM   2490 N N   . THR B 1 142 ? 13.323  -31.862 8.237   1.00 23.16 ? 129 THR B N   1 
ATOM   2491 C CA  . THR B 1 142 ? 12.201  -31.599 7.308   1.00 24.05 ? 129 THR B CA  1 
ATOM   2492 C C   . THR B 1 142 ? 11.416  -32.894 7.166   1.00 24.68 ? 129 THR B C   1 
ATOM   2493 O O   . THR B 1 142 ? 12.031  -33.920 6.830   1.00 25.56 ? 129 THR B O   1 
ATOM   2494 C CB  . THR B 1 142 ? 12.681  -31.139 5.929   1.00 24.06 ? 129 THR B CB  1 
ATOM   2495 O OG1 . THR B 1 142 ? 13.447  -29.957 6.124   1.00 22.73 ? 129 THR B OG1 1 
ATOM   2496 C CG2 . THR B 1 142 ? 11.541  -30.853 4.977   1.00 25.38 ? 129 THR B CG2 1 
ATOM   2497 N N   . ALA B 1 143 ? 10.113  -32.835 7.409   1.00 24.31 ? 130 ALA B N   1 
ATOM   2498 C CA  . ALA B 1 143 ? 9.249   -34.026 7.540   1.00 24.45 ? 130 ALA B CA  1 
ATOM   2499 C C   . ALA B 1 143 ? 7.799   -33.621 7.304   1.00 23.48 ? 130 ALA B C   1 
ATOM   2500 O O   . ALA B 1 143 ? 7.478   -32.412 7.475   1.00 27.52 ? 130 ALA B O   1 
ATOM   2501 C CB  . ALA B 1 143 ? 9.442   -34.641 8.906   1.00 24.50 ? 130 ALA B CB  1 
ATOM   2502 N N   . THR B 1 144 ? 6.966   -34.580 6.917   1.00 21.05 ? 131 THR B N   1 
ATOM   2503 C CA  . THR B 1 144 ? 5.496   -34.423 6.924   1.00 21.04 ? 131 THR B CA  1 
ATOM   2504 C C   . THR B 1 144 ? 4.907   -35.194 8.113   1.00 21.66 ? 131 THR B C   1 
ATOM   2505 O O   . THR B 1 144 ? 5.049   -36.415 8.159   1.00 22.74 ? 131 THR B O   1 
ATOM   2506 C CB  . THR B 1 144 ? 4.904   -34.805 5.571   1.00 20.20 ? 131 THR B CB  1 
ATOM   2507 O OG1 . THR B 1 144 ? 5.437   -33.878 4.619   1.00 18.63 ? 131 THR B OG1 1 
ATOM   2508 C CG2 . THR B 1 144 ? 3.391   -34.779 5.605   1.00 20.42 ? 131 THR B CG2 1 
ATOM   2509 N N   . PHE B 1 145 ? 4.247   -34.486 9.029   1.00 22.49 ? 132 PHE B N   1 
ATOM   2510 C CA  . PHE B 1 145 ? 3.736   -35.029 10.310  1.00 22.88 ? 132 PHE B CA  1 
ATOM   2511 C C   . PHE B 1 145 ? 2.374   -34.426 10.638  1.00 22.80 ? 132 PHE B C   1 
ATOM   2512 O O   . PHE B 1 145 ? 2.061   -33.328 10.155  1.00 24.13 ? 132 PHE B O   1 
ATOM   2513 C CB  . PHE B 1 145 ? 4.706   -34.721 11.454  1.00 23.67 ? 132 PHE B CB  1 
ATOM   2514 C CG  . PHE B 1 145 ? 5.156   -33.283 11.546  1.00 22.44 ? 132 PHE B CG  1 
ATOM   2515 C CD1 . PHE B 1 145 ? 6.269   -32.843 10.842  1.00 22.10 ? 132 PHE B CD1 1 
ATOM   2516 C CD2 . PHE B 1 145 ? 4.480   -32.382 12.347  1.00 21.33 ? 132 PHE B CD2 1 
ATOM   2517 C CE1 . PHE B 1 145 ? 6.690   -31.527 10.931  1.00 22.58 ? 132 PHE B CE1 1 
ATOM   2518 C CE2 . PHE B 1 145 ? 4.900   -31.063 12.439  1.00 22.47 ? 132 PHE B CE2 1 
ATOM   2519 C CZ  . PHE B 1 145 ? 6.003   -30.637 11.728  1.00 23.60 ? 132 PHE B CZ  1 
ATOM   2520 N N   . ASN B 1 146 ? 1.609   -35.145 11.459  1.00 23.39 ? 133 ASN B N   1 
ATOM   2521 C CA  . ASN B 1 146 ? 0.369   -34.652 12.102  1.00 24.34 ? 133 ASN B CA  1 
ATOM   2522 C C   . ASN B 1 146 ? 0.743   -33.732 13.268  1.00 22.26 ? 133 ASN B C   1 
ATOM   2523 O O   . ASN B 1 146 ? 1.773   -33.966 13.893  1.00 20.00 ? 133 ASN B O   1 
ATOM   2524 C CB  . ASN B 1 146 ? -0.526  -35.789 12.604  1.00 26.28 ? 133 ASN B CB  1 
ATOM   2525 C CG  . ASN B 1 146 ? -1.011  -36.710 11.505  1.00 28.55 ? 133 ASN B CG  1 
ATOM   2526 O OD1 . ASN B 1 146 ? -1.424  -36.254 10.441  1.00 29.79 ? 133 ASN B OD1 1 
ATOM   2527 N ND2 . ASN B 1 146 ? -0.975  -38.010 11.763  1.00 30.85 ? 133 ASN B ND2 1 
ATOM   2528 N N   . GLN B 1 147 ? -0.081  -32.708 13.491  1.00 23.64 ? 134 GLN B N   1 
ATOM   2529 C CA  . GLN B 1 147 ? -0.156  -31.876 14.712  1.00 23.90 ? 134 GLN B CA  1 
ATOM   2530 C C   . GLN B 1 147 ? -1.467  -32.222 15.414  1.00 21.51 ? 134 GLN B C   1 
ATOM   2531 O O   . GLN B 1 147 ? -2.492  -32.227 14.729  1.00 21.52 ? 134 GLN B O   1 
ATOM   2532 C CB  . GLN B 1 147 ? -0.188  -30.382 14.388  1.00 25.06 ? 134 GLN B CB  1 
ATOM   2533 C CG  . GLN B 1 147 ? 1.124   -29.758 13.958  1.00 27.46 ? 134 GLN B CG  1 
ATOM   2534 C CD  . GLN B 1 147 ? 0.913   -28.269 13.778  1.00 29.89 ? 134 GLN B CD  1 
ATOM   2535 O OE1 . GLN B 1 147 ? -0.050  -27.825 13.152  1.00 31.29 ? 134 GLN B OE1 1 
ATOM   2536 N NE2 . GLN B 1 147 ? 1.791   -27.470 14.353  1.00 30.50 ? 134 GLN B NE2 1 
ATOM   2537 N N   . TYR B 1 148 ? -1.454  -32.456 16.724  1.00 20.92 ? 135 TYR B N   1 
ATOM   2538 C CA  . TYR B 1 148 ? -2.695  -32.658 17.523  1.00 21.23 ? 135 TYR B CA  1 
ATOM   2539 C C   . TYR B 1 148 ? -2.885  -31.445 18.446  1.00 21.50 ? 135 TYR B C   1 
ATOM   2540 O O   . TYR B 1 148 ? -1.883  -30.932 19.015  1.00 21.50 ? 135 TYR B O   1 
ATOM   2541 C CB  . TYR B 1 148 ? -2.677  -33.987 18.291  1.00 21.30 ? 135 TYR B CB  1 
ATOM   2542 C CG  . TYR B 1 148 ? -2.368  -35.252 17.516  1.00 20.87 ? 135 TYR B CG  1 
ATOM   2543 C CD1 . TYR B 1 148 ? -2.564  -35.359 16.150  1.00 20.51 ? 135 TYR B CD1 1 
ATOM   2544 C CD2 . TYR B 1 148 ? -1.940  -36.388 18.183  1.00 21.12 ? 135 TYR B CD2 1 
ATOM   2545 C CE1 . TYR B 1 148 ? -2.283  -36.533 15.466  1.00 20.38 ? 135 TYR B CE1 1 
ATOM   2546 C CE2 . TYR B 1 148 ? -1.679  -37.576 17.521  1.00 21.00 ? 135 TYR B CE2 1 
ATOM   2547 C CZ  . TYR B 1 148 ? -1.856  -37.654 16.149  1.00 20.70 ? 135 TYR B CZ  1 
ATOM   2548 O OH  . TYR B 1 148 ? -1.596  -38.817 15.477  1.00 19.24 ? 135 TYR B OH  1 
ATOM   2549 N N   . TRP B 1 149 ? -4.129  -30.973 18.575  1.00 21.13 ? 136 TRP B N   1 
ATOM   2550 C CA  . TRP B 1 149 ? -4.476  -29.796 19.416  1.00 22.23 ? 136 TRP B CA  1 
ATOM   2551 C C   . TRP B 1 149 ? -5.537  -30.167 20.457  1.00 23.41 ? 136 TRP B C   1 
ATOM   2552 O O   . TRP B 1 149 ? -6.470  -30.897 20.107  1.00 26.24 ? 136 TRP B O   1 
ATOM   2553 C CB  . TRP B 1 149 ? -4.959  -28.631 18.545  1.00 21.70 ? 136 TRP B CB  1 
ATOM   2554 C CG  . TRP B 1 149 ? -3.998  -28.223 17.470  1.00 21.14 ? 136 TRP B CG  1 
ATOM   2555 C CD1 . TRP B 1 149 ? -3.866  -28.749 16.218  1.00 20.97 ? 136 TRP B CD1 1 
ATOM   2556 C CD2 . TRP B 1 149 ? -3.052  -27.149 17.552  1.00 21.64 ? 136 TRP B CD2 1 
ATOM   2557 N NE1 . TRP B 1 149 ? -2.887  -28.094 15.524  1.00 20.60 ? 136 TRP B NE1 1 
ATOM   2558 C CE2 . TRP B 1 149 ? -2.376  -27.101 16.314  1.00 21.56 ? 136 TRP B CE2 1 
ATOM   2559 C CE3 . TRP B 1 149 ? -2.683  -26.261 18.569  1.00 21.25 ? 136 TRP B CE3 1 
ATOM   2560 C CZ2 . TRP B 1 149 ? -1.345  -26.194 16.073  1.00 22.75 ? 136 TRP B CZ2 1 
ATOM   2561 C CZ3 . TRP B 1 149 ? -1.682  -25.348 18.322  1.00 22.31 ? 136 TRP B CZ3 1 
ATOM   2562 C CH2 . TRP B 1 149 ? -1.014  -25.326 17.094  1.00 22.88 ? 136 TRP B CH2 1 
ATOM   2563 N N   . SER B 1 150 ? -5.360  -29.700 21.694  1.00 22.29 ? 137 SER B N   1 
ATOM   2564 C CA  . SER B 1 150 ? -6.424  -29.459 22.694  1.00 22.20 ? 137 SER B CA  1 
ATOM   2565 C C   . SER B 1 150 ? -6.398  -27.966 22.987  1.00 22.08 ? 137 SER B C   1 
ATOM   2566 O O   . SER B 1 150 ? -5.399  -27.536 23.553  1.00 21.65 ? 137 SER B O   1 
ATOM   2567 C CB  . SER B 1 150 ? -6.187  -30.216 23.967  1.00 23.41 ? 137 SER B CB  1 
ATOM   2568 O OG  . SER B 1 150 ? -6.802  -31.480 23.952  1.00 23.59 ? 137 SER B OG  1 
ATOM   2569 N N   . VAL B 1 151 ? -7.434  -27.212 22.637  1.00 21.42 ? 138 VAL B N   1 
ATOM   2570 C CA  . VAL B 1 151 ? -7.440  -25.733 22.844  1.00 22.16 ? 138 VAL B CA  1 
ATOM   2571 C C   . VAL B 1 151 ? -8.494  -25.394 23.907  1.00 22.45 ? 138 VAL B C   1 
ATOM   2572 O O   . VAL B 1 151 ? -9.699  -25.635 23.673  1.00 23.07 ? 138 VAL B O   1 
ATOM   2573 C CB  . VAL B 1 151 ? -7.690  -24.977 21.525  1.00 22.28 ? 138 VAL B CB  1 
ATOM   2574 C CG1 . VAL B 1 151 ? -7.701  -23.474 21.742  1.00 23.00 ? 138 VAL B CG1 1 
ATOM   2575 C CG2 . VAL B 1 151 ? -6.688  -25.359 20.446  1.00 22.65 ? 138 VAL B CG2 1 
ATOM   2576 N N   . ARG B 1 152 ? -8.057  -24.837 25.033  1.00 22.32 ? 139 ARG B N   1 
ATOM   2577 C CA  . ARG B 1 152 ? -8.960  -24.440 26.142  1.00 22.92 ? 139 ARG B CA  1 
ATOM   2578 C C   . ARG B 1 152 ? -9.934  -23.361 25.639  1.00 23.08 ? 139 ARG B C   1 
ATOM   2579 O O   . ARG B 1 152 ? -9.464  -22.374 25.035  1.00 21.80 ? 139 ARG B O   1 
ATOM   2580 C CB  . ARG B 1 152 ? -8.139  -23.954 27.337  1.00 21.91 ? 139 ARG B CB  1 
ATOM   2581 C CG  . ARG B 1 152 ? -8.792  -24.257 28.676  1.00 22.89 ? 139 ARG B CG  1 
ATOM   2582 C CD  . ARG B 1 152 ? -8.008  -23.659 29.831  1.00 23.32 ? 139 ARG B CD  1 
ATOM   2583 N NE  . ARG B 1 152 ? -8.866  -23.433 30.983  1.00 23.28 ? 139 ARG B NE  1 
ATOM   2584 C CZ  . ARG B 1 152 ? -9.035  -24.293 31.976  1.00 25.06 ? 139 ARG B CZ  1 
ATOM   2585 N NH1 . ARG B 1 152 ? -8.405  -25.461 31.994  1.00 26.03 ? 139 ARG B NH1 1 
ATOM   2586 N NH2 . ARG B 1 152 ? -9.843  -23.975 32.964  1.00 27.58 ? 139 ARG B NH2 1 
ATOM   2587 N N   . THR B 1 153 ? -11.239 -23.546 25.875  1.00 23.22 ? 140 THR B N   1 
ATOM   2588 C CA  . THR B 1 153 ? -12.315 -22.632 25.397  1.00 24.19 ? 140 THR B CA  1 
ATOM   2589 C C   . THR B 1 153 ? -12.261 -21.337 26.198  1.00 24.78 ? 140 THR B C   1 
ATOM   2590 O O   . THR B 1 153 ? -12.607 -20.293 25.614  1.00 29.16 ? 140 THR B O   1 
ATOM   2591 C CB  . THR B 1 153 ? -13.722 -23.235 25.506  1.00 24.10 ? 140 THR B CB  1 
ATOM   2592 O OG1 . THR B 1 153 ? -13.965 -23.648 26.853  1.00 21.46 ? 140 THR B OG1 1 
ATOM   2593 C CG2 . THR B 1 153 ? -13.928 -24.396 24.552  1.00 25.50 ? 140 THR B CG2 1 
ATOM   2594 N N   . ASP B 1 154 ? -11.854 -21.428 27.470  1.00 26.24 ? 141 ASP B N   1 
ATOM   2595 C CA  . ASP B 1 154 ? -11.644 -20.293 28.409  1.00 25.84 ? 141 ASP B CA  1 
ATOM   2596 C C   . ASP B 1 154 ? -10.135 -20.203 28.693  1.00 24.13 ? 141 ASP B C   1 
ATOM   2597 O O   . ASP B 1 154 ? -9.574  -21.070 29.401  1.00 20.53 ? 141 ASP B O   1 
ATOM   2598 C CB  . ASP B 1 154 ? -12.520 -20.457 29.658  1.00 29.15 ? 141 ASP B CB  1 
ATOM   2599 C CG  . ASP B 1 154 ? -12.530 -19.269 30.621  1.00 34.65 ? 141 ASP B CG  1 
ATOM   2600 O OD1 . ASP B 1 154 ? -11.751 -18.306 30.418  1.00 36.59 ? 141 ASP B OD1 1 
ATOM   2601 O OD2 . ASP B 1 154 ? -13.327 -19.308 31.584  1.00 43.05 ? 141 ASP B OD2 1 
ATOM   2602 N N   . HIS B 1 155 ? -9.483  -19.196 28.121  1.00 23.08 ? 142 HIS B N   1 
ATOM   2603 C CA  . HIS B 1 155 ? -8.016  -19.018 28.217  1.00 23.30 ? 142 HIS B CA  1 
ATOM   2604 C C   . HIS B 1 155 ? -7.620  -18.790 29.682  1.00 21.76 ? 142 HIS B C   1 
ATOM   2605 O O   . HIS B 1 155 ? -8.425  -18.253 30.448  1.00 23.01 ? 142 HIS B O   1 
ATOM   2606 C CB  . HIS B 1 155 ? -7.556  -17.886 27.296  1.00 24.37 ? 142 HIS B CB  1 
ATOM   2607 C CG  . HIS B 1 155 ? -7.851  -18.106 25.850  1.00 24.59 ? 142 HIS B CG  1 
ATOM   2608 N ND1 . HIS B 1 155 ? -7.647  -17.120 24.907  1.00 24.89 ? 142 HIS B ND1 1 
ATOM   2609 C CD2 . HIS B 1 155 ? -8.345  -19.176 25.187  1.00 26.02 ? 142 HIS B CD2 1 
ATOM   2610 C CE1 . HIS B 1 155 ? -7.987  -17.581 23.717  1.00 25.81 ? 142 HIS B CE1 1 
ATOM   2611 N NE2 . HIS B 1 155 ? -8.418  -18.841 23.861  1.00 26.38 ? 142 HIS B NE2 1 
ATOM   2612 N N   . ARG B 1 156 ? -6.430  -19.226 30.071  1.00 21.05 ? 143 ARG B N   1 
ATOM   2613 C CA  . ARG B 1 156 ? -5.875  -18.945 31.416  1.00 20.67 ? 143 ARG B CA  1 
ATOM   2614 C C   . ARG B 1 156 ? -4.356  -19.000 31.358  1.00 19.24 ? 143 ARG B C   1 
ATOM   2615 O O   . ARG B 1 156 ? -3.795  -19.596 30.413  1.00 20.84 ? 143 ARG B O   1 
ATOM   2616 C CB  . ARG B 1 156 ? -6.413  -19.946 32.442  1.00 21.82 ? 143 ARG B CB  1 
ATOM   2617 C CG  . ARG B 1 156 ? -6.023  -21.388 32.160  1.00 22.52 ? 143 ARG B CG  1 
ATOM   2618 C CD  . ARG B 1 156 ? -6.360  -22.306 33.311  1.00 22.45 ? 143 ARG B CD  1 
ATOM   2619 N NE  . ARG B 1 156 ? -5.723  -23.582 33.029  1.00 22.92 ? 143 ARG B NE  1 
ATOM   2620 C CZ  . ARG B 1 156 ? -5.811  -24.669 33.780  1.00 22.09 ? 143 ARG B CZ  1 
ATOM   2621 N NH1 . ARG B 1 156 ? -6.519  -24.665 34.902  1.00 21.24 ? 143 ARG B NH1 1 
ATOM   2622 N NH2 . ARG B 1 156 ? -5.165  -25.757 33.395  1.00 22.44 ? 143 ARG B NH2 1 
ATOM   2623 N N   . VAL B 1 157 ? -3.733  -18.407 32.360  1.00 18.16 ? 144 VAL B N   1 
ATOM   2624 C CA  . VAL B 1 157 ? -2.266  -18.441 32.579  1.00 17.50 ? 144 VAL B CA  1 
ATOM   2625 C C   . VAL B 1 157 ? -2.070  -18.963 34.000  1.00 18.15 ? 144 VAL B C   1 
ATOM   2626 O O   . VAL B 1 157 ? -1.987  -18.142 34.957  1.00 17.54 ? 144 VAL B O   1 
ATOM   2627 C CB  . VAL B 1 157 ? -1.607  -17.072 32.354  1.00 16.50 ? 144 VAL B CB  1 
ATOM   2628 C CG1 . VAL B 1 157 ? -0.120  -17.124 32.650  1.00 15.98 ? 144 VAL B CG1 1 
ATOM   2629 C CG2 . VAL B 1 157 ? -1.853  -16.543 30.953  1.00 16.56 ? 144 VAL B CG2 1 
ATOM   2630 N N   . GLY B 1 158 ? -2.056  -20.291 34.121  1.00 17.29 ? 145 GLY B N   1 
ATOM   2631 C CA  . GLY B 1 158 ? -1.685  -20.959 35.373  1.00 17.57 ? 145 GLY B CA  1 
ATOM   2632 C C   . GLY B 1 158 ? -2.715  -21.982 35.777  1.00 17.77 ? 145 GLY B C   1 
ATOM   2633 O O   . GLY B 1 158 ? -3.896  -21.665 35.804  1.00 17.11 ? 145 GLY B O   1 
ATOM   2634 N N   . GLY B 1 159 ? -2.259  -23.178 36.105  1.00 18.88 ? 146 GLY B N   1 
ATOM   2635 C CA  . GLY B 1 159 ? -3.143  -24.237 36.605  1.00 20.08 ? 146 GLY B CA  1 
ATOM   2636 C C   . GLY B 1 159 ? -2.513  -25.591 36.422  1.00 19.61 ? 146 GLY B C   1 
ATOM   2637 O O   . GLY B 1 159 ? -1.274  -25.669 36.280  1.00 20.38 ? 146 GLY B O   1 
ATOM   2638 N N   . THR B 1 160 ? -3.349  -26.614 36.406  1.00 20.76 ? 147 THR B N   1 
ATOM   2639 C CA  . THR B 1 160 ? -2.933  -28.035 36.329  1.00 23.37 ? 147 THR B CA  1 
ATOM   2640 C C   . THR B 1 160 ? -3.274  -28.538 34.922  1.00 22.96 ? 147 THR B C   1 
ATOM   2641 O O   . THR B 1 160 ? -4.401  -28.263 34.444  1.00 22.84 ? 147 THR B O   1 
ATOM   2642 C CB  . THR B 1 160 ? -3.536  -28.820 37.505  1.00 23.36 ? 147 THR B CB  1 
ATOM   2643 O OG1 . THR B 1 160 ? -2.750  -28.486 38.650  1.00 24.23 ? 147 THR B OG1 1 
ATOM   2644 C CG2 . THR B 1 160 ? -3.509  -30.319 37.324  1.00 24.39 ? 147 THR B CG2 1 
ATOM   2645 N N   . VAL B 1 161 ? -2.314  -29.165 34.249  1.00 22.41 ? 148 VAL B N   1 
ATOM   2646 C CA  . VAL B 1 161 ? -2.599  -29.899 32.980  1.00 24.53 ? 148 VAL B CA  1 
ATOM   2647 C C   . VAL B 1 161 ? -2.377  -31.393 33.232  1.00 22.86 ? 148 VAL B C   1 
ATOM   2648 O O   . VAL B 1 161 ? -1.226  -31.805 33.478  1.00 22.76 ? 148 VAL B O   1 
ATOM   2649 C CB  . VAL B 1 161 ? -1.815  -29.357 31.772  1.00 23.28 ? 148 VAL B CB  1 
ATOM   2650 C CG1 . VAL B 1 161 ? -2.116  -30.161 30.511  1.00 22.76 ? 148 VAL B CG1 1 
ATOM   2651 C CG2 . VAL B 1 161 ? -2.138  -27.889 31.563  1.00 22.37 ? 148 VAL B CG2 1 
ATOM   2652 N N   . THR B 1 162 ? -3.484  -32.135 33.247  1.00 22.31 ? 149 THR B N   1 
ATOM   2653 C CA  . THR B 1 162 ? -3.520  -33.610 33.350  1.00 22.58 ? 149 THR B CA  1 
ATOM   2654 C C   . THR B 1 162 ? -3.340  -34.152 31.933  1.00 21.00 ? 149 THR B C   1 
ATOM   2655 O O   . THR B 1 162 ? -4.349  -34.308 31.227  1.00 19.10 ? 149 THR B O   1 
ATOM   2656 C CB  . THR B 1 162 ? -4.804  -34.052 34.059  1.00 23.09 ? 149 THR B CB  1 
ATOM   2657 O OG1 . THR B 1 162 ? -4.954  -33.240 35.228  1.00 22.66 ? 149 THR B OG1 1 
ATOM   2658 C CG2 . THR B 1 162 ? -4.778  -35.518 34.431  1.00 23.36 ? 149 THR B CG2 1 
ATOM   2659 N N   . THR B 1 163 ? -2.092  -34.367 31.519  1.00 20.95 ? 150 THR B N   1 
ATOM   2660 C CA  . THR B 1 163 ? -1.754  -34.683 30.106  1.00 22.41 ? 150 THR B CA  1 
ATOM   2661 C C   . THR B 1 163 ? -2.458  -35.989 29.690  1.00 22.63 ? 150 THR B C   1 
ATOM   2662 O O   . THR B 1 163 ? -2.990  -36.039 28.551  1.00 20.59 ? 150 THR B O   1 
ATOM   2663 C CB  . THR B 1 163 ? -0.237  -34.658 29.902  1.00 22.82 ? 150 THR B CB  1 
ATOM   2664 O OG1 . THR B 1 163 ? 0.367   -35.629 30.754  1.00 23.05 ? 150 THR B OG1 1 
ATOM   2665 C CG2 . THR B 1 163 ? 0.353   -33.292 30.196  1.00 23.66 ? 150 THR B CG2 1 
ATOM   2666 N N   . GLN B 1 164 ? -2.509  -36.983 30.583  1.00 24.12 ? 151 GLN B N   1 
ATOM   2667 C CA  . GLN B 1 164 ? -3.137  -38.309 30.320  1.00 27.33 ? 151 GLN B CA  1 
ATOM   2668 C C   . GLN B 1 164 ? -4.543  -38.136 29.745  1.00 24.76 ? 151 GLN B C   1 
ATOM   2669 O O   . GLN B 1 164 ? -4.875  -38.901 28.835  1.00 25.70 ? 151 GLN B O   1 
ATOM   2670 C CB  . GLN B 1 164 ? -3.212  -39.173 31.586  1.00 31.79 ? 151 GLN B CB  1 
ATOM   2671 C CG  . GLN B 1 164 ? -3.437  -40.656 31.302  1.00 32.78 ? 151 GLN B CG  1 
ATOM   2672 C CD  . GLN B 1 164 ? -2.374  -41.251 30.404  1.00 37.01 ? 151 GLN B CD  1 
ATOM   2673 O OE1 . GLN B 1 164 ? -1.286  -41.621 30.853  1.00 40.99 ? 151 GLN B OE1 1 
ATOM   2674 N NE2 . GLN B 1 164 ? -2.686  -41.369 29.120  1.00 34.98 ? 151 GLN B NE2 1 
ATOM   2675 N N   . ASN B 1 165 ? -5.327  -37.186 30.263  1.00 24.06 ? 152 ASN B N   1 
ATOM   2676 C CA  . ASN B 1 165 ? -6.711  -36.880 29.794  1.00 24.51 ? 152 ASN B CA  1 
ATOM   2677 C C   . ASN B 1 165 ? -6.664  -36.372 28.347  1.00 23.31 ? 152 ASN B C   1 
ATOM   2678 O O   . ASN B 1 165 ? -7.585  -36.694 27.583  1.00 22.98 ? 152 ASN B O   1 
ATOM   2679 C CB  . ASN B 1 165 ? -7.461  -35.893 30.705  1.00 24.72 ? 152 ASN B CB  1 
ATOM   2680 C CG  . ASN B 1 165 ? -7.690  -36.419 32.110  1.00 26.90 ? 152 ASN B CG  1 
ATOM   2681 O OD1 . ASN B 1 165 ? -7.439  -37.585 32.386  1.00 31.07 ? 152 ASN B OD1 1 
ATOM   2682 N ND2 . ASN B 1 165 ? -8.132  -35.572 33.028  1.00 27.56 ? 152 ASN B ND2 1 
ATOM   2683 N N   . HIS B 1 166 ? -5.643  -35.601 27.970  1.00 23.02 ? 153 HIS B N   1 
ATOM   2684 C CA  . HIS B 1 166 ? -5.491  -35.080 26.586  1.00 22.01 ? 153 HIS B CA  1 
ATOM   2685 C C   . HIS B 1 166 ? -5.027  -36.199 25.652  1.00 22.53 ? 153 HIS B C   1 
ATOM   2686 O O   . HIS B 1 166 ? -5.601  -36.304 24.581  1.00 25.63 ? 153 HIS B O   1 
ATOM   2687 C CB  . HIS B 1 166 ? -4.542  -33.887 26.548  1.00 21.00 ? 153 HIS B CB  1 
ATOM   2688 C CG  . HIS B 1 166 ? -5.150  -32.682 27.165  1.00 20.11 ? 153 HIS B CG  1 
ATOM   2689 N ND1 . HIS B 1 166 ? -6.160  -31.989 26.543  1.00 18.88 ? 153 HIS B ND1 1 
ATOM   2690 C CD2 . HIS B 1 166 ? -4.943  -32.094 28.364  1.00 19.51 ? 153 HIS B CD2 1 
ATOM   2691 C CE1 . HIS B 1 166 ? -6.532  -30.996 27.318  1.00 19.49 ? 153 HIS B CE1 1 
ATOM   2692 N NE2 . HIS B 1 166 ? -5.790  -31.035 28.442  1.00 18.89 ? 153 HIS B NE2 1 
ATOM   2693 N N   . PHE B 1 167 ? -4.036  -36.993 26.049  1.00 22.32 ? 154 PHE B N   1 
ATOM   2694 C CA  . PHE B 1 167 ? -3.547  -38.169 25.271  1.00 23.63 ? 154 PHE B CA  1 
ATOM   2695 C C   . PHE B 1 167 ? -4.703  -39.178 25.082  1.00 24.39 ? 154 PHE B C   1 
ATOM   2696 O O   . PHE B 1 167 ? -4.861  -39.658 23.946  1.00 22.54 ? 154 PHE B O   1 
ATOM   2697 C CB  . PHE B 1 167 ? -2.305  -38.794 25.920  1.00 21.85 ? 154 PHE B CB  1 
ATOM   2698 C CG  . PHE B 1 167 ? -1.162  -37.835 26.175  1.00 23.56 ? 154 PHE B CG  1 
ATOM   2699 C CD1 . PHE B 1 167 ? -0.975  -36.708 25.391  1.00 24.83 ? 154 PHE B CD1 1 
ATOM   2700 C CD2 . PHE B 1 167 ? -0.245  -38.074 27.185  1.00 24.73 ? 154 PHE B CD2 1 
ATOM   2701 C CE1 . PHE B 1 167 ? 0.077   -35.838 25.630  1.00 25.52 ? 154 PHE B CE1 1 
ATOM   2702 C CE2 . PHE B 1 167 ? 0.819   -37.216 27.417  1.00 24.05 ? 154 PHE B CE2 1 
ATOM   2703 C CZ  . PHE B 1 167 ? 0.982   -36.103 26.634  1.00 25.62 ? 154 PHE B CZ  1 
ATOM   2704 N N   . ASP B 1 168 ? -5.505  -39.446 26.125  1.00 24.27 ? 155 ASP B N   1 
ATOM   2705 C CA  . ASP B 1 168 ? -6.635  -40.415 26.078  1.00 27.24 ? 155 ASP B CA  1 
ATOM   2706 C C   . ASP B 1 168 ? -7.714  -39.903 25.115  1.00 26.47 ? 155 ASP B C   1 
ATOM   2707 O O   . ASP B 1 168 ? -8.119  -40.698 24.225  1.00 28.76 ? 155 ASP B O   1 
ATOM   2708 C CB  . ASP B 1 168 ? -7.166  -40.769 27.477  1.00 28.48 ? 155 ASP B CB  1 
ATOM   2709 C CG  . ASP B 1 168 ? -6.228  -41.721 28.204  1.00 31.47 ? 155 ASP B CG  1 
ATOM   2710 O OD1 . ASP B 1 168 ? -5.118  -41.926 27.692  1.00 32.61 ? 155 ASP B OD1 1 
ATOM   2711 O OD2 . ASP B 1 168 ? -6.588  -42.232 29.283  1.00 34.11 ? 155 ASP B OD2 1 
ATOM   2712 N N   . ALA B 1 169 ? -8.152  -38.647 25.243  1.00 25.24 ? 156 ALA B N   1 
ATOM   2713 C CA  . ALA B 1 169 ? -9.149  -38.049 24.318  1.00 24.75 ? 156 ALA B CA  1 
ATOM   2714 C C   . ALA B 1 169 ? -8.597  -38.126 22.887  1.00 24.67 ? 156 ALA B C   1 
ATOM   2715 O O   . ALA B 1 169 ? -9.371  -38.488 21.988  1.00 24.73 ? 156 ALA B O   1 
ATOM   2716 C CB  . ALA B 1 169 ? -9.512  -36.636 24.709  1.00 24.16 ? 156 ALA B CB  1 
ATOM   2717 N N   . TRP B 1 170 ? -7.300  -37.872 22.689  1.00 24.34 ? 157 TRP B N   1 
ATOM   2718 C CA  . TRP B 1 170 ? -6.671  -37.910 21.339  1.00 27.34 ? 157 TRP B CA  1 
ATOM   2719 C C   . TRP B 1 170 ? -6.763  -39.332 20.764  1.00 26.75 ? 157 TRP B C   1 
ATOM   2720 O O   . TRP B 1 170 ? -7.166  -39.463 19.601  1.00 25.38 ? 157 TRP B O   1 
ATOM   2721 C CB  . TRP B 1 170 ? -5.221  -37.395 21.354  1.00 28.89 ? 157 TRP B CB  1 
ATOM   2722 C CG  . TRP B 1 170 ? -5.086  -35.924 21.616  1.00 30.29 ? 157 TRP B CG  1 
ATOM   2723 C CD1 . TRP B 1 170 ? -6.069  -34.981 21.555  1.00 32.35 ? 157 TRP B CD1 1 
ATOM   2724 C CD2 . TRP B 1 170 ? -3.888  -35.220 21.997  1.00 30.63 ? 157 TRP B CD2 1 
ATOM   2725 N NE1 . TRP B 1 170 ? -5.570  -33.747 21.880  1.00 33.07 ? 157 TRP B NE1 1 
ATOM   2726 C CE2 . TRP B 1 170 ? -4.234  -33.859 22.149  1.00 31.71 ? 157 TRP B CE2 1 
ATOM   2727 C CE3 . TRP B 1 170 ? -2.560  -35.603 22.227  1.00 28.59 ? 157 TRP B CE3 1 
ATOM   2728 C CZ2 . TRP B 1 170 ? -3.304  -32.885 22.522  1.00 29.27 ? 157 TRP B CZ2 1 
ATOM   2729 C CZ3 . TRP B 1 170 ? -1.649  -34.644 22.610  1.00 28.71 ? 157 TRP B CZ3 1 
ATOM   2730 C CH2 . TRP B 1 170 ? -2.018  -33.304 22.752  1.00 28.09 ? 157 TRP B CH2 1 
ATOM   2731 N N   . LYS B 1 171 ? -6.418  -40.350 21.553  1.00 29.80 ? 158 LYS B N   1 
ATOM   2732 C CA  . LYS B 1 171 ? -6.465  -41.780 21.140  1.00 31.81 ? 158 LYS B CA  1 
ATOM   2733 C C   . LYS B 1 171 ? -7.904  -42.108 20.744  1.00 32.36 ? 158 LYS B C   1 
ATOM   2734 O O   . LYS B 1 171 ? -8.090  -42.651 19.646  1.00 30.74 ? 158 LYS B O   1 
ATOM   2735 C CB  . LYS B 1 171 ? -6.023  -42.726 22.256  1.00 34.04 ? 158 LYS B CB  1 
ATOM   2736 C CG  . LYS B 1 171 ? -4.755  -42.352 23.015  1.00 38.27 ? 158 LYS B CG  1 
ATOM   2737 C CD  . LYS B 1 171 ? -3.455  -42.752 22.356  1.00 42.21 ? 158 LYS B CD  1 
ATOM   2738 C CE  . LYS B 1 171 ? -2.314  -42.845 23.354  1.00 45.77 ? 158 LYS B CE  1 
ATOM   2739 N NZ  . LYS B 1 171 ? -2.554  -43.894 24.379  1.00 46.32 ? 158 LYS B NZ  1 
ATOM   2740 N N   . ASN B 1 172 ? -8.871  -41.718 21.586  1.00 33.44 ? 159 ASN B N   1 
ATOM   2741 C CA  . ASN B 1 172 ? -10.320 -42.044 21.445  1.00 35.54 ? 159 ASN B CA  1 
ATOM   2742 C C   . ASN B 1 172 ? -10.923 -41.392 20.196  1.00 32.31 ? 159 ASN B C   1 
ATOM   2743 O O   . ASN B 1 172 ? -11.956 -41.885 19.741  1.00 31.98 ? 159 ASN B O   1 
ATOM   2744 C CB  . ASN B 1 172 ? -11.144 -41.608 22.663  1.00 39.15 ? 159 ASN B CB  1 
ATOM   2745 C CG  . ASN B 1 172 ? -11.347 -42.737 23.649  1.00 43.44 ? 159 ASN B CG  1 
ATOM   2746 O OD1 . ASN B 1 172 ? -12.086 -43.684 23.369  1.00 47.36 ? 159 ASN B OD1 1 
ATOM   2747 N ND2 . ASN B 1 172 ? -10.680 -42.655 24.791  1.00 42.98 ? 159 ASN B ND2 1 
ATOM   2748 N N   . ALA B 1 173 ? -10.349 -40.284 19.725  1.00 30.24 ? 160 ALA B N   1 
ATOM   2749 C CA  . ALA B 1 173 ? -10.724 -39.617 18.465  1.00 29.41 ? 160 ALA B CA  1 
ATOM   2750 C C   . ALA B 1 173 ? -10.060 -40.358 17.300  1.00 29.63 ? 160 ALA B C   1 
ATOM   2751 O O   . ALA B 1 173 ? -10.367 -40.038 16.157  1.00 29.63 ? 160 ALA B O   1 
ATOM   2752 C CB  . ALA B 1 173 ? -10.313 -38.170 18.514  1.00 29.77 ? 160 ALA B CB  1 
ATOM   2753 N N   . GLY B 1 174 ? -9.189  -41.326 17.588  1.00 29.31 ? 161 GLY B N   1 
ATOM   2754 C CA  . GLY B 1 174 ? -8.499  -42.137 16.568  1.00 29.64 ? 161 GLY B CA  1 
ATOM   2755 C C   . GLY B 1 174 ? -7.179  -41.514 16.149  1.00 30.72 ? 161 GLY B C   1 
ATOM   2756 O O   . GLY B 1 174 ? -6.837  -41.607 14.962  1.00 29.18 ? 161 GLY B O   1 
ATOM   2757 N N   . LEU B 1 175 ? -6.447  -40.899 17.083  1.00 31.06 ? 162 LEU B N   1 
ATOM   2758 C CA  . LEU B 1 175 ? -5.158  -40.240 16.769  1.00 31.30 ? 162 LEU B CA  1 
ATOM   2759 C C   . LEU B 1 175 ? -4.028  -41.064 17.391  1.00 33.47 ? 162 LEU B C   1 
ATOM   2760 O O   . LEU B 1 175 ? -4.042  -41.266 18.605  1.00 36.11 ? 162 LEU B O   1 
ATOM   2761 C CB  . LEU B 1 175 ? -5.179  -38.796 17.272  1.00 28.05 ? 162 LEU B CB  1 
ATOM   2762 C CG  . LEU B 1 175 ? -6.278  -37.914 16.687  1.00 26.62 ? 162 LEU B CG  1 
ATOM   2763 C CD1 . LEU B 1 175 ? -6.206  -36.516 17.276  1.00 26.62 ? 162 LEU B CD1 1 
ATOM   2764 C CD2 . LEU B 1 175 ? -6.206  -37.847 15.175  1.00 26.27 ? 162 LEU B CD2 1 
ATOM   2765 N N   . GLU B 1 176 ? -3.126  -41.570 16.551  1.00 37.47 ? 163 GLU B N   1 
ATOM   2766 C CA  . GLU B 1 176 ? -1.971  -42.417 16.952  1.00 39.07 ? 163 GLU B CA  1 
ATOM   2767 C C   . GLU B 1 176 ? -0.913  -41.529 17.626  1.00 34.88 ? 163 GLU B C   1 
ATOM   2768 O O   . GLU B 1 176 ? -0.607  -40.441 17.099  1.00 30.65 ? 163 GLU B O   1 
ATOM   2769 C CB  . GLU B 1 176 ? -1.424  -43.139 15.717  1.00 46.19 ? 163 GLU B CB  1 
ATOM   2770 C CG  . GLU B 1 176 ? -0.197  -43.995 15.992  1.00 54.96 ? 163 GLU B CG  1 
ATOM   2771 C CD  . GLU B 1 176 ? -0.472  -45.455 16.311  1.00 61.53 ? 163 GLU B CD  1 
ATOM   2772 O OE1 . GLU B 1 176 ? 0.106   -45.963 17.306  1.00 64.24 ? 163 GLU B OE1 1 
ATOM   2773 O OE2 . GLU B 1 176 ? -1.249  -46.085 15.553  1.00 67.05 ? 163 GLU B OE2 1 
ATOM   2774 N N   . MET B 1 177 ? -0.393  -41.982 18.762  1.00 33.36 ? 164 MET B N   1 
ATOM   2775 C CA  . MET B 1 177 ? 0.767   -41.384 19.460  1.00 33.46 ? 164 MET B CA  1 
ATOM   2776 C C   . MET B 1 177 ? 1.909   -42.396 19.411  1.00 31.62 ? 164 MET B C   1 
ATOM   2777 O O   . MET B 1 177 ? 1.642   -43.593 19.577  1.00 31.41 ? 164 MET B O   1 
ATOM   2778 C CB  . MET B 1 177 ? 0.447   -41.083 20.923  1.00 35.74 ? 164 MET B CB  1 
ATOM   2779 C CG  . MET B 1 177 ? -0.786  -40.233 21.104  1.00 40.63 ? 164 MET B CG  1 
ATOM   2780 S SD  . MET B 1 177 ? -0.356  -38.508 21.299  1.00 44.65 ? 164 MET B SD  1 
ATOM   2781 C CE  . MET B 1 177 ? 0.162   -38.514 23.014  1.00 43.21 ? 164 MET B CE  1 
ATOM   2782 N N   . GLY B 1 178 ? 3.125   -41.912 19.181  1.00 28.48 ? 165 GLY B N   1 
ATOM   2783 C CA  . GLY B 1 178 ? 4.341   -42.728 19.137  1.00 27.35 ? 165 GLY B CA  1 
ATOM   2784 C C   . GLY B 1 178 ? 5.052   -42.658 20.462  1.00 25.86 ? 165 GLY B C   1 
ATOM   2785 O O   . GLY B 1 178 ? 4.370   -42.419 21.472  1.00 27.46 ? 165 GLY B O   1 
ATOM   2786 N N   . THR B 1 179 ? 6.359   -42.890 20.445  1.00 24.02 ? 166 THR B N   1 
ATOM   2787 C CA  . THR B 1 179 ? 7.249   -42.753 21.614  1.00 25.69 ? 166 THR B CA  1 
ATOM   2788 C C   . THR B 1 179 ? 7.390   -41.259 21.915  1.00 25.21 ? 166 THR B C   1 
ATOM   2789 O O   . THR B 1 179 ? 7.572   -40.485 20.955  1.00 24.69 ? 166 THR B O   1 
ATOM   2790 C CB  . THR B 1 179 ? 8.618   -43.396 21.359  1.00 26.30 ? 166 THR B CB  1 
ATOM   2791 O OG1 . THR B 1 179 ? 8.378   -44.613 20.656  1.00 27.34 ? 166 THR B OG1 1 
ATOM   2792 C CG2 . THR B 1 179 ? 9.374   -43.652 22.644  1.00 26.83 ? 166 THR B CG2 1 
ATOM   2793 N N   . HIS B 1 180 ? 7.298   -40.881 23.189  1.00 23.90 ? 167 HIS B N   1 
ATOM   2794 C CA  . HIS B 1 180 ? 7.379   -39.471 23.636  1.00 25.15 ? 167 HIS B CA  1 
ATOM   2795 C C   . HIS B 1 180 ? 8.835   -38.992 23.549  1.00 25.23 ? 167 HIS B C   1 
ATOM   2796 O O   . HIS B 1 180 ? 9.730   -39.647 24.121  1.00 24.87 ? 167 HIS B O   1 
ATOM   2797 C CB  . HIS B 1 180 ? 6.750   -39.304 25.024  1.00 25.43 ? 167 HIS B CB  1 
ATOM   2798 C CG  . HIS B 1 180 ? 5.269   -39.457 25.021  1.00 28.00 ? 167 HIS B CG  1 
ATOM   2799 N ND1 . HIS B 1 180 ? 4.626   -40.429 24.273  1.00 31.38 ? 167 HIS B ND1 1 
ATOM   2800 C CD2 . HIS B 1 180 ? 4.302   -38.795 25.683  1.00 29.46 ? 167 HIS B CD2 1 
ATOM   2801 C CE1 . HIS B 1 180 ? 3.327   -40.349 24.474  1.00 30.94 ? 167 HIS B CE1 1 
ATOM   2802 N NE2 . HIS B 1 180 ? 3.106   -39.346 25.328  1.00 30.67 ? 167 HIS B NE2 1 
ATOM   2803 N N   . ASN B 1 181 ? 9.040   -37.891 22.826  1.00 24.12 ? 168 ASN B N   1 
ATOM   2804 C CA  . ASN B 1 181 ? 10.238  -37.025 22.934  1.00 23.49 ? 168 ASN B CA  1 
ATOM   2805 C C   . ASN B 1 181 ? 9.960   -36.008 24.044  1.00 23.54 ? 168 ASN B C   1 
ATOM   2806 O O   . ASN B 1 181 ? 9.135   -36.313 24.927  1.00 24.60 ? 168 ASN B O   1 
ATOM   2807 C CB  . ASN B 1 181 ? 10.542  -36.372 21.591  1.00 23.45 ? 168 ASN B CB  1 
ATOM   2808 C CG  . ASN B 1 181 ? 12.007  -36.051 21.431  1.00 23.87 ? 168 ASN B CG  1 
ATOM   2809 O OD1 . ASN B 1 181 ? 12.475  -35.007 21.885  1.00 25.56 ? 168 ASN B OD1 1 
ATOM   2810 N ND2 . ASN B 1 181 ? 12.718  -36.941 20.766  1.00 22.67 ? 168 ASN B ND2 1 
ATOM   2811 N N   . TYR B 1 182 ? 10.552  -34.818 23.981  1.00 23.22 ? 169 TYR B N   1 
ATOM   2812 C CA  . TYR B 1 182 ? 10.383  -33.786 25.032  1.00 23.23 ? 169 TYR B CA  1 
ATOM   2813 C C   . TYR B 1 182 ? 8.930   -33.300 25.074  1.00 23.86 ? 169 TYR B C   1 
ATOM   2814 O O   . TYR B 1 182 ? 8.251   -33.281 24.043  1.00 26.04 ? 169 TYR B O   1 
ATOM   2815 C CB  . TYR B 1 182 ? 11.385  -32.649 24.856  1.00 22.73 ? 169 TYR B CB  1 
ATOM   2816 C CG  . TYR B 1 182 ? 11.128  -31.728 23.694  1.00 22.60 ? 169 TYR B CG  1 
ATOM   2817 C CD1 . TYR B 1 182 ? 10.105  -30.797 23.732  1.00 21.53 ? 169 TYR B CD1 1 
ATOM   2818 C CD2 . TYR B 1 182 ? 11.930  -31.765 22.564  1.00 22.24 ? 169 TYR B CD2 1 
ATOM   2819 C CE1 . TYR B 1 182 ? 9.874   -29.935 22.674  1.00 21.06 ? 169 TYR B CE1 1 
ATOM   2820 C CE2 . TYR B 1 182 ? 11.711  -30.909 21.499  1.00 21.79 ? 169 TYR B CE2 1 
ATOM   2821 C CZ  . TYR B 1 182 ? 10.676  -29.991 21.551  1.00 20.74 ? 169 TYR B CZ  1 
ATOM   2822 O OH  . TYR B 1 182 ? 10.468  -29.127 20.516  1.00 19.60 ? 169 TYR B OH  1 
ATOM   2823 N N   . MET B 1 183 ? 8.475   -32.980 26.290  1.00 23.36 ? 170 MET B N   1 
ATOM   2824 C CA  . MET B 1 183 ? 7.235   -32.237 26.609  1.00 21.31 ? 170 MET B CA  1 
ATOM   2825 C C   . MET B 1 183 ? 7.597   -31.037 27.503  1.00 21.53 ? 170 MET B C   1 
ATOM   2826 O O   . MET B 1 183 ? 8.282   -31.237 28.546  1.00 21.28 ? 170 MET B O   1 
ATOM   2827 C CB  . MET B 1 183 ? 6.252   -33.146 27.345  1.00 20.61 ? 170 MET B CB  1 
ATOM   2828 C CG  . MET B 1 183 ? 4.943   -32.467 27.644  1.00 20.65 ? 170 MET B CG  1 
ATOM   2829 S SD  . MET B 1 183 ? 3.710   -33.622 28.259  1.00 21.49 ? 170 MET B SD  1 
ATOM   2830 C CE  . MET B 1 183 ? 4.462   -34.104 29.809  1.00 22.03 ? 170 MET B CE  1 
ATOM   2831 N N   . ILE B 1 184 ? 7.170   -29.832 27.129  1.00 21.19 ? 171 ILE B N   1 
ATOM   2832 C CA  . ILE B 1 184 ? 7.549   -28.570 27.835  1.00 21.30 ? 171 ILE B CA  1 
ATOM   2833 C C   . ILE B 1 184 ? 6.312   -27.678 27.969  1.00 20.64 ? 171 ILE B C   1 
ATOM   2834 O O   . ILE B 1 184 ? 5.410   -27.786 27.147  1.00 23.11 ? 171 ILE B O   1 
ATOM   2835 C CB  . ILE B 1 184 ? 8.690   -27.834 27.100  1.00 22.23 ? 171 ILE B CB  1 
ATOM   2836 C CG1 . ILE B 1 184 ? 8.359   -27.585 25.629  1.00 22.11 ? 171 ILE B CG1 1 
ATOM   2837 C CG2 . ILE B 1 184 ? 10.030  -28.548 27.244  1.00 22.34 ? 171 ILE B CG2 1 
ATOM   2838 C CD1 . ILE B 1 184 ? 9.236   -26.515 24.998  1.00 22.29 ? 171 ILE B CD1 1 
ATOM   2839 N N   . VAL B 1 185 ? 6.273   -26.816 28.972  1.00 19.67 ? 172 VAL B N   1 
ATOM   2840 C CA  . VAL B 1 185 ? 5.266   -25.720 29.032  1.00 20.33 ? 172 VAL B CA  1 
ATOM   2841 C C   . VAL B 1 185 ? 5.835   -24.564 28.193  1.00 19.24 ? 172 VAL B C   1 
ATOM   2842 O O   . VAL B 1 185 ? 6.736   -23.873 28.679  1.00 19.88 ? 172 VAL B O   1 
ATOM   2843 C CB  . VAL B 1 185 ? 4.945   -25.321 30.486  1.00 20.05 ? 172 VAL B CB  1 
ATOM   2844 C CG1 . VAL B 1 185 ? 3.737   -24.404 30.536  1.00 20.28 ? 172 VAL B CG1 1 
ATOM   2845 C CG2 . VAL B 1 185 ? 4.736   -26.540 31.375  1.00 19.16 ? 172 VAL B CG2 1 
ATOM   2846 N N   . ALA B 1 186 ? 5.369   -24.405 26.957  1.00 18.07 ? 173 ALA B N   1 
ATOM   2847 C CA  . ALA B 1 186 ? 6.046   -23.613 25.908  1.00 18.96 ? 173 ALA B CA  1 
ATOM   2848 C C   . ALA B 1 186 ? 5.360   -22.260 25.694  1.00 18.61 ? 173 ALA B C   1 
ATOM   2849 O O   . ALA B 1 186 ? 4.130   -22.232 25.568  1.00 16.90 ? 173 ALA B O   1 
ATOM   2850 C CB  . ALA B 1 186 ? 6.078   -24.394 24.620  1.00 20.29 ? 173 ALA B CB  1 
ATOM   2851 N N   . THR B 1 187 ? 6.156   -21.186 25.649  1.00 18.38 ? 174 THR B N   1 
ATOM   2852 C CA  . THR B 1 187 ? 5.786   -19.885 25.053  1.00 18.23 ? 174 THR B CA  1 
ATOM   2853 C C   . THR B 1 187 ? 6.185   -19.930 23.574  1.00 19.68 ? 174 THR B C   1 
ATOM   2854 O O   . THR B 1 187 ? 7.366   -20.168 23.269  1.00 19.32 ? 174 THR B O   1 
ATOM   2855 C CB  . THR B 1 187 ? 6.433   -18.743 25.835  1.00 17.77 ? 174 THR B CB  1 
ATOM   2856 O OG1 . THR B 1 187 ? 6.062   -18.978 27.193  1.00 17.19 ? 174 THR B OG1 1 
ATOM   2857 C CG2 . THR B 1 187 ? 6.019   -17.364 25.357  1.00 17.24 ? 174 THR B CG2 1 
ATOM   2858 N N   . GLU B 1 188 ? 5.223   -19.752 22.681  1.00 20.46 ? 175 GLU B N   1 
ATOM   2859 C CA  . GLU B 1 188 ? 5.496   -19.721 21.228  1.00 22.26 ? 175 GLU B CA  1 
ATOM   2860 C C   . GLU B 1 188 ? 5.082   -18.341 20.711  1.00 22.98 ? 175 GLU B C   1 
ATOM   2861 O O   . GLU B 1 188 ? 4.069   -17.796 21.213  1.00 22.10 ? 175 GLU B O   1 
ATOM   2862 C CB  . GLU B 1 188 ? 4.766   -20.860 20.510  1.00 21.16 ? 175 GLU B CB  1 
ATOM   2863 C CG  . GLU B 1 188 ? 4.795   -20.711 19.003  1.00 21.03 ? 175 GLU B CG  1 
ATOM   2864 C CD  . GLU B 1 188 ? 4.698   -21.995 18.207  1.00 22.48 ? 175 GLU B CD  1 
ATOM   2865 O OE1 . GLU B 1 188 ? 4.751   -21.899 16.965  1.00 23.80 ? 175 GLU B OE1 1 
ATOM   2866 O OE2 . GLU B 1 188 ? 4.611   -23.092 18.822  1.00 22.71 ? 175 GLU B OE2 1 
ATOM   2867 N N   . GLY B 1 189 ? 5.835   -17.806 19.756  1.00 21.86 ? 176 GLY B N   1 
ATOM   2868 C CA  . GLY B 1 189 ? 5.474   -16.538 19.104  1.00 25.09 ? 176 GLY B CA  1 
ATOM   2869 C C   . GLY B 1 189 ? 5.623   -16.620 17.604  1.00 25.50 ? 176 GLY B C   1 
ATOM   2870 O O   . GLY B 1 189 ? 6.318   -17.512 17.138  1.00 25.14 ? 176 GLY B O   1 
ATOM   2871 N N   . TYR B 1 190 ? 4.976   -15.712 16.884  1.00 28.13 ? 177 TYR B N   1 
ATOM   2872 C CA  . TYR B 1 190 ? 5.212   -15.487 15.438  1.00 30.10 ? 177 TYR B CA  1 
ATOM   2873 C C   . TYR B 1 190 ? 4.860   -14.042 15.088  1.00 29.34 ? 177 TYR B C   1 
ATOM   2874 O O   . TYR B 1 190 ? 3.704   -13.634 15.333  1.00 30.81 ? 177 TYR B O   1 
ATOM   2875 C CB  . TYR B 1 190 ? 4.402   -16.457 14.582  1.00 32.49 ? 177 TYR B CB  1 
ATOM   2876 C CG  . TYR B 1 190 ? 4.819   -16.398 13.141  1.00 35.99 ? 177 TYR B CG  1 
ATOM   2877 C CD1 . TYR B 1 190 ? 6.112   -16.740 12.777  1.00 39.37 ? 177 TYR B CD1 1 
ATOM   2878 C CD2 . TYR B 1 190 ? 3.965   -15.927 12.160  1.00 36.79 ? 177 TYR B CD2 1 
ATOM   2879 C CE1 . TYR B 1 190 ? 6.537   -16.663 11.461  1.00 39.87 ? 177 TYR B CE1 1 
ATOM   2880 C CE2 . TYR B 1 190 ? 4.376   -15.836 10.841  1.00 39.48 ? 177 TYR B CE2 1 
ATOM   2881 C CZ  . TYR B 1 190 ? 5.661   -16.218 10.487  1.00 42.47 ? 177 TYR B CZ  1 
ATOM   2882 O OH  . TYR B 1 190 ? 6.071   -16.128 9.187   1.00 46.87 ? 177 TYR B OH  1 
ATOM   2883 N N   . GLN B 1 191 ? 5.833   -13.290 14.569  1.00 27.34 ? 178 GLN B N   1 
ATOM   2884 C CA  . GLN B 1 191 ? 5.627   -11.909 14.087  1.00 26.07 ? 178 GLN B CA  1 
ATOM   2885 C C   . GLN B 1 191 ? 4.911   -11.120 15.180  1.00 24.83 ? 178 GLN B C   1 
ATOM   2886 O O   . GLN B 1 191 ? 3.807   -10.593 14.914  1.00 23.03 ? 178 GLN B O   1 
ATOM   2887 C CB  . GLN B 1 191 ? 4.819   -11.926 12.799  1.00 28.93 ? 178 GLN B CB  1 
ATOM   2888 C CG  . GLN B 1 191 ? 5.582   -12.538 11.641  1.00 31.58 ? 178 GLN B CG  1 
ATOM   2889 C CD  . GLN B 1 191 ? 4.866   -12.283 10.339  1.00 35.54 ? 178 GLN B CD  1 
ATOM   2890 O OE1 . GLN B 1 191 ? 3.646   -12.110 10.305  1.00 35.44 ? 178 GLN B OE1 1 
ATOM   2891 N NE2 . GLN B 1 191 ? 5.636   -12.242 9.260   1.00 38.11 ? 178 GLN B NE2 1 
ATOM   2892 N N   . SER B 1 192 ? 5.536   -11.055 16.356  1.00 22.66 ? 179 SER B N   1 
ATOM   2893 C CA  . SER B 1 192 ? 4.999   -10.407 17.573  1.00 21.36 ? 179 SER B CA  1 
ATOM   2894 C C   . SER B 1 192 ? 6.157   -9.974  18.458  1.00 20.57 ? 179 SER B C   1 
ATOM   2895 O O   . SER B 1 192 ? 7.314   -10.265 18.124  1.00 21.47 ? 179 SER B O   1 
ATOM   2896 C CB  . SER B 1 192 ? 4.055   -11.330 18.319  1.00 22.40 ? 179 SER B CB  1 
ATOM   2897 O OG  . SER B 1 192 ? 4.613   -12.623 18.489  1.00 21.76 ? 179 SER B OG  1 
ATOM   2898 N N   . SER B 1 193 ? 5.831   -9.252  19.520  1.00 19.37 ? 180 SER B N   1 
ATOM   2899 C CA  . SER B 1 193 ? 6.732   -8.899  20.640  1.00 17.51 ? 180 SER B CA  1 
ATOM   2900 C C   . SER B 1 193 ? 6.050   -9.394  21.906  1.00 17.67 ? 180 SER B C   1 
ATOM   2901 O O   . SER B 1 193 ? 4.867   -9.815  21.837  1.00 16.96 ? 180 SER B O   1 
ATOM   2902 C CB  . SER B 1 193 ? 6.962   -7.412  20.696  1.00 17.80 ? 180 SER B CB  1 
ATOM   2903 O OG  . SER B 1 193 ? 7.207   -6.879  19.396  1.00 18.34 ? 180 SER B OG  1 
ATOM   2904 N N   . GLY B 1 194 ? 6.752   -9.330  23.023  1.00 17.58 ? 181 GLY B N   1 
ATOM   2905 C CA  . GLY B 1 194 ? 6.160   -9.667  24.317  1.00 17.97 ? 181 GLY B CA  1 
ATOM   2906 C C   . GLY B 1 194 ? 7.194   -10.217 25.261  1.00 18.10 ? 181 GLY B C   1 
ATOM   2907 O O   . GLY B 1 194 ? 8.387   -10.250 24.932  1.00 19.09 ? 181 GLY B O   1 
ATOM   2908 N N   . SER B 1 195 ? 6.737   -10.600 26.430  1.00 18.00 ? 182 SER B N   1 
ATOM   2909 C CA  . SER B 1 195 ? 7.579   -11.240 27.460  1.00 18.79 ? 182 SER B CA  1 
ATOM   2910 C C   . SER B 1 195 ? 6.700   -12.234 28.216  1.00 18.40 ? 182 SER B C   1 
ATOM   2911 O O   . SER B 1 195 ? 5.463   -12.064 28.230  1.00 17.84 ? 182 SER B O   1 
ATOM   2912 C CB  . SER B 1 195 ? 8.191   -10.208 28.359  1.00 18.93 ? 182 SER B CB  1 
ATOM   2913 O OG  . SER B 1 195 ? 7.168   -9.486  29.010  1.00 18.81 ? 182 SER B OG  1 
ATOM   2914 N N   . ALA B 1 196 ? 7.312   -13.284 28.728  1.00 18.03 ? 183 ALA B N   1 
ATOM   2915 C CA  . ALA B 1 196 ? 6.647   -14.290 29.568  1.00 17.78 ? 183 ALA B CA  1 
ATOM   2916 C C   . ALA B 1 196 ? 7.666   -14.736 30.604  1.00 18.09 ? 183 ALA B C   1 
ATOM   2917 O O   . ALA B 1 196 ? 8.875   -14.788 30.257  1.00 18.62 ? 183 ALA B O   1 
ATOM   2918 C CB  . ALA B 1 196 ? 6.154   -15.423 28.714  1.00 18.77 ? 183 ALA B CB  1 
ATOM   2919 N N   . SER B 1 197 ? 7.219   -14.955 31.836  1.00 18.47 ? 184 SER B N   1 
ATOM   2920 C CA  . SER B 1 197 ? 8.029   -15.619 32.881  1.00 20.04 ? 184 SER B CA  1 
ATOM   2921 C C   . SER B 1 197 ? 7.186   -16.732 33.476  1.00 20.62 ? 184 SER B C   1 
ATOM   2922 O O   . SER B 1 197 ? 6.241   -16.400 34.189  1.00 21.54 ? 184 SER B O   1 
ATOM   2923 C CB  . SER B 1 197 ? 8.501   -14.677 33.932  1.00 20.63 ? 184 SER B CB  1 
ATOM   2924 O OG  . SER B 1 197 ? 9.127   -15.415 34.971  1.00 23.74 ? 184 SER B OG  1 
ATOM   2925 N N   . ILE B 1 198 ? 7.508   -17.986 33.140  1.00 21.25 ? 185 ILE B N   1 
ATOM   2926 C CA  . ILE B 1 198 ? 6.674   -19.187 33.443  1.00 20.71 ? 185 ILE B CA  1 
ATOM   2927 C C   . ILE B 1 198 ? 7.492   -20.082 34.367  1.00 19.93 ? 185 ILE B C   1 
ATOM   2928 O O   . ILE B 1 198 ? 8.674   -20.280 34.051  1.00 19.42 ? 185 ILE B O   1 
ATOM   2929 C CB  . ILE B 1 198 ? 6.242   -19.934 32.162  1.00 20.22 ? 185 ILE B CB  1 
ATOM   2930 C CG1 . ILE B 1 198 ? 5.421   -19.049 31.235  1.00 20.75 ? 185 ILE B CG1 1 
ATOM   2931 C CG2 . ILE B 1 198 ? 5.488   -21.213 32.507  1.00 20.00 ? 185 ILE B CG2 1 
ATOM   2932 C CD1 . ILE B 1 198 ? 3.990   -18.853 31.720  1.00 22.48 ? 185 ILE B CD1 1 
ATOM   2933 N N   . THR B 1 199 ? 6.872   -20.597 35.436  1.00 19.08 ? 186 THR B N   1 
ATOM   2934 C CA  . THR B 1 199 ? 7.499   -21.566 36.368  1.00 20.58 ? 186 THR B CA  1 
ATOM   2935 C C   . THR B 1 199 ? 6.728   -22.881 36.270  1.00 21.44 ? 186 THR B C   1 
ATOM   2936 O O   . THR B 1 199 ? 5.546   -22.903 36.668  1.00 20.46 ? 186 THR B O   1 
ATOM   2937 C CB  . THR B 1 199 ? 7.548   -21.048 37.817  1.00 19.83 ? 186 THR B CB  1 
ATOM   2938 O OG1 . THR B 1 199 ? 8.266   -19.809 37.842  1.00 17.40 ? 186 THR B OG1 1 
ATOM   2939 C CG2 . THR B 1 199 ? 8.155   -22.063 38.763  1.00 18.66 ? 186 THR B CG2 1 
ATOM   2940 N N   . VAL B 1 200 ? 7.395   -23.912 35.753  1.00 22.98 ? 187 VAL B N   1 
ATOM   2941 C CA  . VAL B 1 200 ? 6.958   -25.342 35.760  1.00 24.73 ? 187 VAL B CA  1 
ATOM   2942 C C   . VAL B 1 200 ? 7.296   -25.977 37.123  1.00 26.60 ? 187 VAL B C   1 
ATOM   2943 O O   . VAL B 1 200 ? 8.413   -25.726 37.647  1.00 25.09 ? 187 VAL B O   1 
ATOM   2944 C CB  . VAL B 1 200 ? 7.670   -26.091 34.614  1.00 25.06 ? 187 VAL B CB  1 
ATOM   2945 C CG1 . VAL B 1 200 ? 7.172   -27.518 34.470  1.00 26.05 ? 187 VAL B CG1 1 
ATOM   2946 C CG2 . VAL B 1 200 ? 7.566   -25.345 33.295  1.00 24.40 ? 187 VAL B CG2 1 
ATOM   2947 N N   . GLN B 1 201 ? 6.414   -26.829 37.658  1.00 32.07 ? 188 GLN B N   1 
ATOM   2948 C CA  . GLN B 1 201 ? 6.767   -27.810 38.736  1.00 35.72 ? 188 GLN B CA  1 
ATOM   2949 C C   . GLN B 1 201 ? 6.252   -29.217 38.367  1.00 37.08 ? 188 GLN B C   1 
ATOM   2950 O O   . GLN B 1 201 ? 5.216   -29.506 37.687  1.00 35.94 ? 188 GLN B O   1 
ATOM   2951 C CB  . GLN B 1 201 ? 6.255   -27.302 40.088  1.00 38.06 ? 188 GLN B CB  1 
ATOM   2952 C CG  . GLN B 1 201 ? 4.743   -27.405 40.241  1.00 42.70 ? 188 GLN B CG  1 
ATOM   2953 C CD  . GLN B 1 201 ? 4.077   -26.214 40.891  1.00 45.81 ? 188 GLN B CD  1 
ATOM   2954 O OE1 . GLN B 1 201 ? 3.528   -26.309 41.994  1.00 51.84 ? 188 GLN B OE1 1 
ATOM   2955 N NE2 . GLN B 1 201 ? 4.096   -25.090 40.193  1.00 44.16 ? 188 GLN B NE2 1 
HETATM 2956 O O   . HOH C 2 .   ? 3.219   10.673  3.551   1.00 19.01 ? 201 HOH A O   1 
HETATM 2957 O O   . HOH C 2 .   ? -12.002 -18.959 4.390   1.00 33.27 ? 202 HOH A O   1 
HETATM 2958 O O   . HOH C 2 .   ? -25.453 -5.767  1.464   1.00 29.14 ? 203 HOH A O   1 
HETATM 2959 O O   . HOH C 2 .   ? 1.633   2.467   -8.544  1.00 18.93 ? 204 HOH A O   1 
HETATM 2960 O O   . HOH C 2 .   ? -19.130 -4.305  -2.437  1.00 19.56 ? 205 HOH A O   1 
HETATM 2961 O O   . HOH C 2 .   ? 8.952   -8.603  3.166   1.00 22.72 ? 206 HOH A O   1 
HETATM 2962 O O   . HOH C 2 .   ? 6.956   3.213   13.079  1.00 27.92 ? 207 HOH A O   1 
HETATM 2963 O O   . HOH C 2 .   ? 1.242   17.645  -0.015  1.00 25.99 ? 208 HOH A O   1 
HETATM 2964 O O   . HOH C 2 .   ? 16.496  8.710   -0.130  1.00 36.22 ? 209 HOH A O   1 
HETATM 2965 O O   . HOH C 2 .   ? -9.211  8.923   11.162  1.00 15.47 ? 210 HOH A O   1 
HETATM 2966 O O   . HOH C 2 .   ? 5.231   -16.517 -12.947 1.00 15.91 ? 211 HOH A O   1 
HETATM 2967 O O   . HOH C 2 .   ? 1.010   5.272   -8.094  1.00 17.55 ? 212 HOH A O   1 
HETATM 2968 O O   . HOH C 2 .   ? 2.143   -0.495  16.763  1.00 35.27 ? 213 HOH A O   1 
HETATM 2969 O O   . HOH C 2 .   ? 8.325   5.206   -12.635 1.00 35.98 ? 214 HOH A O   1 
HETATM 2970 O O   . HOH C 2 .   ? 10.557  1.069   10.988  1.00 29.54 ? 215 HOH A O   1 
HETATM 2971 O O   . HOH C 2 .   ? 6.731   -15.716 0.113   1.00 28.69 ? 216 HOH A O   1 
HETATM 2972 O O   . HOH C 2 .   ? -10.136 -15.633 3.694   1.00 35.16 ? 217 HOH A O   1 
HETATM 2973 O O   . HOH C 2 .   ? 6.638   10.149  11.914  1.00 30.38 ? 218 HOH A O   1 
HETATM 2974 O O   . HOH C 2 .   ? -2.638  -0.864  -14.837 1.00 31.13 ? 219 HOH A O   1 
HETATM 2975 O O   . HOH C 2 .   ? 9.591   -8.905  7.788   1.00 33.04 ? 220 HOH A O   1 
HETATM 2976 O O   . HOH C 2 .   ? -7.304  11.659  -2.018  1.00 25.19 ? 221 HOH A O   1 
HETATM 2977 O O   . HOH C 2 .   ? -5.352  -7.513  -7.061  1.00 35.05 ? 222 HOH A O   1 
HETATM 2978 O O   . HOH C 2 .   ? -6.865  -14.352 4.465   1.00 22.77 ? 223 HOH A O   1 
HETATM 2979 O O   . HOH C 2 .   ? -3.838  7.784   -10.792 1.00 38.19 ? 224 HOH A O   1 
HETATM 2980 O O   . HOH C 2 .   ? 8.862   0.870   -16.715 1.00 28.96 ? 225 HOH A O   1 
HETATM 2981 O O   . HOH C 2 .   ? 0.821   -9.464  0.993   1.00 30.20 ? 226 HOH A O   1 
HETATM 2982 O O   . HOH C 2 .   ? -14.495 10.928  -3.185  1.00 30.58 ? 227 HOH A O   1 
HETATM 2983 O O   . HOH C 2 .   ? -12.997 -14.890 3.311   1.00 23.49 ? 228 HOH A O   1 
HETATM 2984 O O   . HOH C 2 .   ? 4.541   -7.820  4.843   1.00 38.51 ? 229 HOH A O   1 
HETATM 2985 O O   . HOH C 2 .   ? -7.651  12.419  7.282   1.00 18.95 ? 230 HOH A O   1 
HETATM 2986 O O   . HOH C 2 .   ? -1.488  -11.426 14.930  1.00 17.55 ? 231 HOH A O   1 
HETATM 2987 O O   . HOH C 2 .   ? 12.404  -5.905  -8.664  1.00 29.37 ? 232 HOH A O   1 
HETATM 2988 O O   . HOH C 2 .   ? 0.408   0.014   -15.612 1.00 37.43 ? 233 HOH A O   1 
HETATM 2989 O O   . HOH C 2 .   ? 15.547  -5.803  11.104  1.00 36.92 ? 234 HOH A O   1 
HETATM 2990 O O   . HOH C 2 .   ? 18.396  8.027   1.493   1.00 33.89 ? 235 HOH A O   1 
HETATM 2991 O O   . HOH C 2 .   ? 21.742  7.238   -4.314  1.00 25.24 ? 236 HOH A O   1 
HETATM 2992 O O   . HOH C 2 .   ? -14.557 9.588   -1.149  1.00 20.79 ? 237 HOH A O   1 
HETATM 2993 O O   . HOH C 2 .   ? 4.863   -9.554  -0.503  1.00 33.11 ? 238 HOH A O   1 
HETATM 2994 O O   . HOH C 2 .   ? -0.224  -16.141 2.402   1.00 41.97 ? 239 HOH A O   1 
HETATM 2995 O O   . HOH C 2 .   ? -18.326 1.397   7.547   1.00 38.76 ? 240 HOH A O   1 
HETATM 2996 O O   . HOH C 2 .   ? 1.155   -10.576 15.783  1.00 17.42 ? 241 HOH A O   1 
HETATM 2997 O O   . HOH C 2 .   ? -12.415 3.102   16.392  1.00 30.88 ? 242 HOH A O   1 
HETATM 2998 O O   . HOH C 2 .   ? 14.509  12.725  -1.677  1.00 31.73 ? 243 HOH A O   1 
HETATM 2999 O O   . HOH C 2 .   ? -15.435 11.396  0.812   1.00 31.62 ? 244 HOH A O   1 
HETATM 3000 O O   . HOH C 2 .   ? 10.655  -11.317 11.771  1.00 35.09 ? 245 HOH A O   1 
HETATM 3001 O O   . HOH C 2 .   ? -17.596 -13.070 -2.419  1.00 27.71 ? 246 HOH A O   1 
HETATM 3002 O O   . HOH C 2 .   ? 4.953   -8.462  2.338   1.00 30.17 ? 247 HOH A O   1 
HETATM 3003 O O   . HOH C 2 .   ? 16.071  -0.028  11.212  1.00 32.51 ? 248 HOH A O   1 
HETATM 3004 O O   . HOH C 2 .   ? 2.228   13.497  -4.198  1.00 14.46 ? 249 HOH A O   1 
HETATM 3005 O O   . HOH C 2 .   ? -20.000 2.046   -8.897  1.00 31.78 ? 250 HOH A O   1 
HETATM 3006 O O   . HOH C 2 .   ? 7.419   13.272  -10.862 1.00 38.20 ? 251 HOH A O   1 
HETATM 3007 O O   . HOH C 2 .   ? -1.090  -3.755  2.006   1.00 19.80 ? 252 HOH A O   1 
HETATM 3008 O O   . HOH C 2 .   ? -3.366  -18.574 4.978   1.00 34.95 ? 253 HOH A O   1 
HETATM 3009 O O   . HOH C 2 .   ? -13.883 -0.511  12.150  1.00 37.28 ? 254 HOH A O   1 
HETATM 3010 O O   . HOH C 2 .   ? -7.638  -9.556  -6.079  1.00 33.79 ? 255 HOH A O   1 
HETATM 3011 O O   . HOH C 2 .   ? -25.095 -2.586  -5.103  1.00 26.37 ? 256 HOH A O   1 
HETATM 3012 O O   . HOH C 2 .   ? 15.875  -8.641  2.663   1.00 39.61 ? 257 HOH A O   1 
HETATM 3013 O O   . HOH C 2 .   ? -12.722 -17.529 12.985  1.00 23.15 ? 258 HOH A O   1 
HETATM 3014 O O   . HOH C 2 .   ? -1.360  -2.180  4.221   1.00 18.71 ? 259 HOH A O   1 
HETATM 3015 O O   . HOH C 2 .   ? 13.458  14.093  4.096   1.00 27.76 ? 260 HOH A O   1 
HETATM 3016 O O   . HOH C 2 .   ? -10.287 -15.811 -2.667  1.00 25.30 ? 261 HOH A O   1 
HETATM 3017 O O   . HOH C 2 .   ? 1.264   4.147   -15.308 1.00 28.34 ? 262 HOH A O   1 
HETATM 3018 O O   . HOH C 2 .   ? -16.674 3.294   -10.992 1.00 40.08 ? 263 HOH A O   1 
HETATM 3019 O O   . HOH C 2 .   ? -13.748 -9.984  13.883  1.00 24.62 ? 264 HOH A O   1 
HETATM 3020 O O   . HOH C 2 .   ? 3.678   5.173   -14.565 1.00 19.90 ? 265 HOH A O   1 
HETATM 3021 O O   . HOH C 2 .   ? 0.922   -14.604 -7.960  1.00 37.42 ? 266 HOH A O   1 
HETATM 3022 O O   . HOH C 2 .   ? 4.514   17.647  3.287   1.00 19.04 ? 267 HOH A O   1 
HETATM 3023 O O   . HOH C 2 .   ? -14.685 5.599   6.815   1.00 18.65 ? 268 HOH A O   1 
HETATM 3024 O O   . HOH C 2 .   ? 5.819   18.549  -0.335  1.00 29.44 ? 269 HOH A O   1 
HETATM 3025 O O   . HOH C 2 .   ? -3.416  -5.462  18.042  1.00 28.39 ? 270 HOH A O   1 
HETATM 3026 O O   . HOH C 2 .   ? -3.104  -9.126  -10.936 1.00 32.20 ? 271 HOH A O   1 
HETATM 3027 O O   . HOH C 2 .   ? -8.073  -21.250 7.615   1.00 22.12 ? 272 HOH A O   1 
HETATM 3028 O O   . HOH C 2 .   ? 3.635   5.290   17.142  1.00 24.56 ? 273 HOH A O   1 
HETATM 3029 O O   . HOH C 2 .   ? 7.155   -8.274  6.478   1.00 30.81 ? 274 HOH A O   1 
HETATM 3030 O O   . HOH C 2 .   ? 0.500   11.009  16.171  1.00 29.29 ? 275 HOH A O   1 
HETATM 3031 O O   . HOH C 2 .   ? -15.762 6.978   12.064  1.00 44.93 ? 276 HOH A O   1 
HETATM 3032 O O   . HOH C 2 .   ? 18.264  10.165  5.088   1.00 25.62 ? 277 HOH A O   1 
HETATM 3033 O O   . HOH C 2 .   ? 16.482  -0.896  -7.222  1.00 26.93 ? 278 HOH A O   1 
HETATM 3034 O O   . HOH C 2 .   ? 1.236   11.262  13.222  1.00 27.49 ? 279 HOH A O   1 
HETATM 3035 O O   . HOH C 2 .   ? 2.018   12.908  14.583  1.00 35.17 ? 280 HOH A O   1 
HETATM 3036 O O   . HOH C 2 .   ? -2.230  4.138   15.289  1.00 25.48 ? 281 HOH A O   1 
HETATM 3037 O O   . HOH C 2 .   ? 9.895   15.502  0.983   1.00 31.98 ? 282 HOH A O   1 
HETATM 3038 O O   . HOH C 2 .   ? -11.515 -8.974  -11.973 1.00 40.63 ? 283 HOH A O   1 
HETATM 3039 O O   . HOH C 2 .   ? -1.203  16.014  -6.235  1.00 33.67 ? 284 HOH A O   1 
HETATM 3040 O O   . HOH C 2 .   ? 0.116   11.539  -14.769 1.00 41.10 ? 285 HOH A O   1 
HETATM 3041 O O   . HOH C 2 .   ? 4.302   -10.375 -2.235  1.00 36.81 ? 286 HOH A O   1 
HETATM 3042 O O   . HOH C 2 .   ? 15.693  -2.679  10.317  1.00 29.04 ? 287 HOH A O   1 
HETATM 3043 O O   . HOH C 2 .   ? 8.004   5.347   -14.926 1.00 32.23 ? 288 HOH A O   1 
HETATM 3044 O O   . HOH C 2 .   ? -17.954 -4.898  -9.471  1.00 23.69 ? 289 HOH A O   1 
HETATM 3045 O O   . HOH C 2 .   ? 17.549  -8.133  0.324   1.00 23.91 ? 290 HOH A O   1 
HETATM 3046 O O   . HOH C 2 .   ? -18.834 -5.294  -6.900  1.00 37.19 ? 291 HOH A O   1 
HETATM 3047 O O   . HOH C 2 .   ? -21.236 5.106   5.991   1.00 31.44 ? 292 HOH A O   1 
HETATM 3048 O O   . HOH C 2 .   ? 19.756  9.444   -7.112  1.00 35.90 ? 293 HOH A O   1 
HETATM 3049 O O   . HOH C 2 .   ? 17.903  -5.991  9.780   1.00 37.58 ? 294 HOH A O   1 
HETATM 3050 O O   . HOH C 2 .   ? -9.116  4.534   -11.287 1.00 29.81 ? 295 HOH A O   1 
HETATM 3051 O O   . HOH C 2 .   ? 15.869  13.810  3.786   1.00 29.27 ? 296 HOH A O   1 
HETATM 3052 O O   . HOH C 2 .   ? 7.337   8.996   -9.664  1.00 35.63 ? 297 HOH A O   1 
HETATM 3053 O O   . HOH C 2 .   ? 17.109  10.348  -8.300  1.00 29.73 ? 298 HOH A O   1 
HETATM 3054 O O   . HOH C 2 .   ? -2.238  -8.544  -4.049  1.00 24.55 ? 299 HOH A O   1 
HETATM 3055 O O   . HOH C 2 .   ? -19.439 7.010   -9.728  1.00 38.67 ? 300 HOH A O   1 
HETATM 3056 O O   . HOH C 2 .   ? 2.699   7.768   -13.007 1.00 41.69 ? 301 HOH A O   1 
HETATM 3057 O O   . HOH C 2 .   ? -12.116 -10.391 -10.243 1.00 32.20 ? 302 HOH A O   1 
HETATM 3058 O O   . HOH C 2 .   ? -2.269  -13.971 -9.104  1.00 36.06 ? 303 HOH A O   1 
HETATM 3059 O O   . HOH C 2 .   ? 8.148   6.851   -10.539 1.00 25.59 ? 304 HOH A O   1 
HETATM 3060 O O   . HOH C 2 .   ? 0.568   -1.491  -17.742 1.00 35.90 ? 305 HOH A O   1 
HETATM 3061 O O   . HOH C 2 .   ? -3.132  6.226   16.030  1.00 30.91 ? 306 HOH A O   1 
HETATM 3062 O O   . HOH C 2 .   ? -15.806 -11.880 9.728   1.00 32.57 ? 307 HOH A O   1 
HETATM 3063 O O   . HOH C 2 .   ? 5.454   -21.329 -10.343 1.00 37.74 ? 308 HOH A O   1 
HETATM 3064 O O   . HOH C 2 .   ? -1.142  -10.519 -5.441  1.00 35.23 ? 309 HOH A O   1 
HETATM 3065 O O   . HOH C 2 .   ? -21.333 -12.878 2.038   1.00 38.83 ? 310 HOH A O   1 
HETATM 3066 O O   . HOH C 2 .   ? -9.574  -22.371 6.142   1.00 36.32 ? 311 HOH A O   1 
HETATM 3067 O O   . HOH C 2 .   ? 19.939  9.504   0.055   1.00 38.56 ? 312 HOH A O   1 
HETATM 3068 O O   . HOH C 2 .   ? -9.466  7.063   -12.067 1.00 41.10 ? 313 HOH A O   1 
HETATM 3069 O O   . HOH C 2 .   ? -4.001  -0.572  17.064  1.00 31.42 ? 314 HOH A O   1 
HETATM 3070 O O   . HOH C 2 .   ? 7.516   20.064  -2.640  1.00 39.36 ? 315 HOH A O   1 
HETATM 3071 O O   . HOH C 2 .   ? -13.134 14.312  -4.559  1.00 40.94 ? 316 HOH A O   1 
HETATM 3072 O O   . HOH C 2 .   ? 4.483   19.950  1.985   1.00 37.02 ? 317 HOH A O   1 
HETATM 3073 O O   . HOH C 2 .   ? 6.839   18.072  -10.468 1.00 35.28 ? 318 HOH A O   1 
HETATM 3074 O O   . HOH C 2 .   ? -6.237  14.843  -7.685  1.00 30.80 ? 319 HOH A O   1 
HETATM 3075 O O   . HOH D 2 .   ? 4.387   -23.157 39.863  1.00 45.17 ? 201 HOH B O   1 
HETATM 3076 O O   . HOH D 2 .   ? 9.435   -40.698 13.826  1.00 28.75 ? 202 HOH B O   1 
HETATM 3077 O O   . HOH D 2 .   ? -0.507  -17.282 36.680  1.00 17.99 ? 203 HOH B O   1 
HETATM 3078 O O   . HOH D 2 .   ? -4.311  -22.287 11.309  1.00 32.68 ? 204 HOH B O   1 
HETATM 3079 O O   . HOH D 2 .   ? 14.870  -34.730 22.405  1.00 35.74 ? 205 HOH B O   1 
HETATM 3080 O O   . HOH D 2 .   ? -5.591  -29.532 30.874  1.00 17.38 ? 206 HOH B O   1 
HETATM 3081 O O   . HOH D 2 .   ? 15.471  -14.758 16.576  1.00 30.15 ? 207 HOH B O   1 
HETATM 3082 O O   . HOH D 2 .   ? 6.086   -36.137 24.388  1.00 14.45 ? 208 HOH B O   1 
HETATM 3083 O O   . HOH D 2 .   ? 12.577  -15.764 15.696  1.00 25.17 ? 209 HOH B O   1 
HETATM 3084 O O   . HOH D 2 .   ? 2.198   -37.929 11.959  1.00 27.97 ? 210 HOH B O   1 
HETATM 3085 O O   . HOH D 2 .   ? 9.850   -25.125 39.697  1.00 24.97 ? 211 HOH B O   1 
HETATM 3086 O O   . HOH D 2 .   ? 7.318   -17.546 37.048  1.00 24.52 ? 212 HOH B O   1 
HETATM 3087 O O   . HOH D 2 .   ? -0.768  -25.868 11.608  1.00 22.50 ? 213 HOH B O   1 
HETATM 3088 O O   . HOH D 2 .   ? -4.539  -38.615 11.454  1.00 39.52 ? 214 HOH B O   1 
HETATM 3089 O O   . HOH D 2 .   ? 6.351   -45.574 18.766  1.00 22.42 ? 215 HOH B O   1 
HETATM 3090 O O   . HOH D 2 .   ? 2.555   -43.731 22.859  1.00 34.32 ? 216 HOH B O   1 
HETATM 3091 O O   . HOH D 2 .   ? 14.536  -34.749 6.862   1.00 15.35 ? 217 HOH B O   1 
HETATM 3092 O O   . HOH D 2 .   ? -3.968  -16.398 35.183  1.00 30.45 ? 218 HOH B O   1 
HETATM 3093 O O   . HOH D 2 .   ? -0.941  -44.101 29.975  1.00 34.19 ? 219 HOH B O   1 
HETATM 3094 O O   . HOH D 2 .   ? -0.991  -22.124 38.481  1.00 20.57 ? 220 HOH B O   1 
HETATM 3095 O O   . HOH D 2 .   ? 5.153   -34.021 1.977   1.00 36.25 ? 221 HOH B O   1 
HETATM 3096 O O   . HOH D 2 .   ? 5.309   -25.466 15.355  1.00 38.64 ? 222 HOH B O   1 
HETATM 3097 O O   . HOH D 2 .   ? 12.035  -40.486 22.961  1.00 34.01 ? 223 HOH B O   1 
HETATM 3098 O O   . HOH D 2 .   ? -10.171 -20.715 22.944  1.00 32.83 ? 224 HOH B O   1 
HETATM 3099 O O   . HOH D 2 .   ? 9.800   -46.026 18.799  1.00 26.75 ? 225 HOH B O   1 
HETATM 3100 O O   . HOH D 2 .   ? 4.951   -36.431 27.054  1.00 19.25 ? 226 HOH B O   1 
HETATM 3101 O O   . HOH D 2 .   ? 8.089   -41.409 28.960  1.00 36.96 ? 227 HOH B O   1 
HETATM 3102 O O   . HOH D 2 .   ? 6.077   -33.793 -0.095  1.00 39.26 ? 228 HOH B O   1 
HETATM 3103 O O   . HOH D 2 .   ? 22.945  -17.272 22.683  1.00 28.95 ? 229 HOH B O   1 
HETATM 3104 O O   . HOH D 2 .   ? -14.417 -25.152 16.118  1.00 35.60 ? 230 HOH B O   1 
HETATM 3105 O O   . HOH D 2 .   ? 18.748  -32.145 23.386  1.00 36.96 ? 231 HOH B O   1 
HETATM 3106 O O   . HOH D 2 .   ? -10.603 -23.191 19.385  1.00 25.47 ? 232 HOH B O   1 
HETATM 3107 O O   . HOH D 2 .   ? 18.153  -12.758 16.095  1.00 44.30 ? 233 HOH B O   1 
HETATM 3108 O O   . HOH D 2 .   ? -0.913  -40.039 34.795  1.00 41.13 ? 234 HOH B O   1 
HETATM 3109 O O   . HOH D 2 .   ? 4.955   -24.121 21.430  1.00 19.96 ? 235 HOH B O   1 
HETATM 3110 O O   . HOH D 2 .   ? 2.780   -22.713 23.008  1.00 17.19 ? 236 HOH B O   1 
HETATM 3111 O O   . HOH D 2 .   ? 12.186  -32.059 37.425  1.00 37.94 ? 237 HOH B O   1 
HETATM 3112 O O   . HOH D 2 .   ? 17.532  -13.488 18.745  1.00 27.74 ? 238 HOH B O   1 
HETATM 3113 O O   . HOH D 2 .   ? 2.473   -36.052 37.569  1.00 32.97 ? 239 HOH B O   1 
HETATM 3114 O O   . HOH D 2 .   ? 6.807   -42.987 25.119  1.00 26.60 ? 240 HOH B O   1 
HETATM 3115 O O   . HOH D 2 .   ? 5.241   -27.167 12.805  1.00 35.51 ? 241 HOH B O   1 
HETATM 3116 O O   . HOH D 2 .   ? 20.519  -18.184 34.721  1.00 33.71 ? 242 HOH B O   1 
HETATM 3117 O O   . HOH D 2 .   ? 0.730   -40.914 34.763  1.00 40.22 ? 243 HOH B O   1 
HETATM 3118 O O   . HOH D 2 .   ? -1.657  -36.571 33.511  1.00 27.41 ? 244 HOH B O   1 
HETATM 3119 O O   . HOH D 2 .   ? -10.564 -18.081 33.131  1.00 30.55 ? 245 HOH B O   1 
HETATM 3120 O O   . HOH D 2 .   ? 21.350  -26.351 37.169  1.00 34.77 ? 246 HOH B O   1 
HETATM 3121 O O   . HOH D 2 .   ? 14.048  -14.660 37.960  1.00 32.76 ? 247 HOH B O   1 
HETATM 3122 O O   . HOH D 2 .   ? -5.277  -15.423 28.855  1.00 27.80 ? 248 HOH B O   1 
HETATM 3123 O O   . HOH D 2 .   ? 20.112  -19.097 31.085  1.00 28.21 ? 249 HOH B O   1 
HETATM 3124 O O   . HOH D 2 .   ? -1.561  -44.405 20.139  1.00 23.95 ? 250 HOH B O   1 
HETATM 3125 O O   . HOH D 2 .   ? -4.961  -33.897 38.181  1.00 33.88 ? 251 HOH B O   1 
HETATM 3126 O O   . HOH D 2 .   ? 11.489  -27.477 18.190  1.00 22.45 ? 252 HOH B O   1 
HETATM 3127 O O   . HOH D 2 .   ? -8.383  -36.423 35.995  1.00 41.25 ? 253 HOH B O   1 
HETATM 3128 O O   . HOH D 2 .   ? 19.541  -31.230 20.810  1.00 35.46 ? 254 HOH B O   1 
HETATM 3129 O O   . HOH D 2 .   ? 9.574   -6.132  23.400  1.00 31.97 ? 255 HOH B O   1 
HETATM 3130 O O   . HOH D 2 .   ? -1.887  -8.801  22.034  1.00 36.70 ? 256 HOH B O   1 
HETATM 3131 O O   . HOH D 2 .   ? -11.011 -16.812 26.808  1.00 25.00 ? 257 HOH B O   1 
HETATM 3132 O O   . HOH D 2 .   ? 14.098  -29.669 10.865  1.00 27.72 ? 258 HOH B O   1 
HETATM 3133 O O   . HOH D 2 .   ? 19.296  -19.696 16.305  1.00 40.11 ? 259 HOH B O   1 
HETATM 3134 O O   . HOH D 2 .   ? 8.435   -2.088  16.538  1.00 39.54 ? 260 HOH B O   1 
HETATM 3135 O O   . HOH D 2 .   ? 15.672  -31.619 17.364  1.00 33.66 ? 261 HOH B O   1 
HETATM 3136 O O   . HOH D 2 .   ? 22.170  -26.957 22.497  1.00 33.06 ? 262 HOH B O   1 
HETATM 3137 O O   . HOH D 2 .   ? -14.490 -35.322 28.466  1.00 27.57 ? 263 HOH B O   1 
HETATM 3138 O O   . HOH D 2 .   ? 13.177  -5.238  16.654  1.00 25.86 ? 264 HOH B O   1 
HETATM 3139 O O   . HOH D 2 .   ? 4.423   -17.643 6.887   1.00 42.09 ? 265 HOH B O   1 
HETATM 3140 O O   . HOH D 2 .   ? 16.851  -24.748 41.620  1.00 31.22 ? 266 HOH B O   1 
HETATM 3141 O O   . HOH D 2 .   ? 15.333  -10.115 11.276  1.00 30.80 ? 267 HOH B O   1 
HETATM 3142 O O   . HOH D 2 .   ? -0.414  -42.173 26.951  1.00 37.28 ? 268 HOH B O   1 
HETATM 3143 O O   . HOH D 2 .   ? 1.172   -12.758 13.400  1.00 36.97 ? 269 HOH B O   1 
HETATM 3144 O O   . HOH D 2 .   ? 14.553  -9.195  22.833  1.00 42.86 ? 270 HOH B O   1 
HETATM 3145 O O   . HOH D 2 .   ? 14.008  -34.649 32.067  1.00 21.02 ? 271 HOH B O   1 
HETATM 3146 O O   . HOH D 2 .   ? 22.890  -28.386 29.580  1.00 32.65 ? 272 HOH B O   1 
HETATM 3147 O O   . HOH D 2 .   ? 4.411   -19.092 41.884  1.00 36.19 ? 273 HOH B O   1 
HETATM 3148 O O   . HOH D 2 .   ? 20.484  -29.654 35.857  1.00 38.54 ? 274 HOH B O   1 
HETATM 3149 O O   . HOH D 2 .   ? 1.901   -23.791 14.666  1.00 27.81 ? 275 HOH B O   1 
HETATM 3150 O O   . HOH D 2 .   ? -3.740  -40.481 13.320  1.00 29.24 ? 276 HOH B O   1 
HETATM 3151 O O   . HOH D 2 .   ? -13.079 -30.830 34.805  1.00 34.68 ? 277 HOH B O   1 
HETATM 3152 O O   . HOH D 2 .   ? 15.142  -11.549 31.463  1.00 41.70 ? 278 HOH B O   1 
HETATM 3153 O O   . HOH D 2 .   ? -9.584  -33.275 36.264  1.00 29.67 ? 279 HOH B O   1 
HETATM 3154 O O   . HOH D 2 .   ? -18.422 -25.020 22.220  1.00 36.81 ? 280 HOH B O   1 
HETATM 3155 O O   . HOH D 2 .   ? 7.683   -25.333 14.906  1.00 42.95 ? 281 HOH B O   1 
HETATM 3156 O O   . HOH D 2 .   ? 21.909  -27.726 35.521  1.00 33.07 ? 282 HOH B O   1 
HETATM 3157 O O   . HOH D 2 .   ? 13.266  -10.750 10.368  1.00 29.60 ? 283 HOH B O   1 
HETATM 3158 O O   . HOH D 2 .   ? 0.622   -42.130 24.620  1.00 28.63 ? 284 HOH B O   1 
HETATM 3159 O O   . HOH D 2 .   ? 15.285  -32.964 20.738  1.00 32.09 ? 285 HOH B O   1 
HETATM 3160 O O   . HOH D 2 .   ? 4.283   -13.610 39.074  1.00 35.73 ? 286 HOH B O   1 
HETATM 3161 O O   . HOH D 2 .   ? 12.968  -31.387 39.390  1.00 43.62 ? 287 HOH B O   1 
HETATM 3162 O O   . HOH D 2 .   ? -15.901 -27.070 32.674  1.00 38.74 ? 288 HOH B O   1 
HETATM 3163 O O   . HOH D 2 .   ? -6.519  -38.392 36.081  1.00 27.93 ? 289 HOH B O   1 
HETATM 3164 O O   . HOH D 2 .   ? -8.838  -38.751 12.000  1.00 33.67 ? 290 HOH B O   1 
HETATM 3165 O O   . HOH D 2 .   ? 16.203  -34.615 31.852  1.00 40.14 ? 291 HOH B O   1 
HETATM 3166 O O   . HOH D 2 .   ? 7.056   -43.680 33.108  1.00 33.47 ? 292 HOH B O   1 
HETATM 3167 O O   . HOH D 2 .   ? 0.112   -37.860 7.094   1.00 32.15 ? 293 HOH B O   1 
HETATM 3168 O O   . HOH D 2 .   ? -5.774  -15.117 31.265  1.00 27.87 ? 294 HOH B O   1 
HETATM 3169 O O   . HOH D 2 .   ? -2.627  -11.205 27.359  1.00 29.97 ? 295 HOH B O   1 
HETATM 3170 O O   . HOH D 2 .   ? 13.097  -13.526 35.564  1.00 26.39 ? 296 HOH B O   1 
HETATM 3171 O O   . HOH D 2 .   ? 12.438  -27.947 16.079  1.00 26.39 ? 297 HOH B O   1 
HETATM 3172 O O   . HOH D 2 .   ? 4.578   -19.594 11.155  1.00 36.75 ? 298 HOH B O   1 
HETATM 3173 O O   . HOH D 2 .   ? -13.809 -40.061 13.494  1.00 34.87 ? 299 HOH B O   1 
HETATM 3174 O O   . HOH D 2 .   ? 24.676  -26.062 24.701  1.00 29.36 ? 300 HOH B O   1 
HETATM 3175 O O   . HOH D 2 .   ? 3.152   -13.472 5.700   1.00 35.35 ? 301 HOH B O   1 
HETATM 3176 O O   . HOH D 2 .   ? 19.324  -33.085 27.121  1.00 38.40 ? 302 HOH B O   1 
HETATM 3177 O O   . HOH D 2 .   ? -1.327  -42.995 36.354  1.00 38.79 ? 303 HOH B O   1 
# 
