data_9D5U
# 
_entry.id   9D5U 
# 
_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   9D5U         pdb_00009d5u 10.2210/pdb9d5u/pdb 
WWPDB D_1000287362 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        9D5U 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rholz@mines.edu 
_pdbx_contact_author.name_first         Richard 
_pdbx_contact_author.name_last          Holz 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6093-2799 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Miller, C.G.' 1 0009-0000-9169-1051 
'Holz, R.C.'   2 ?                   
'Liu, D.'      3 ?                   
# 
_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.Inorg.Biochem. 
_citation.journal_id_ASTM           JIBIDJ 
_citation.journal_id_CSD            0525 
_citation.journal_id_ISSN           0162-0134 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            262 
_citation.language                  ? 
_citation.page_first                112763 
_citation.page_last                 112763 
_citation.title                     
'Catalytic and post-translational maturation roles of a conserved active site serine residue in nitrile hydratases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jinorgbio.2024.112763 
_citation.pdbx_database_id_PubMed   39447484 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Miller, C.'  1 ? 
primary 'Knutson, K.' 2 ? 
primary 'Liu, D.'     3 ? 
primary 'Bennett, B.' 4 ? 
primary 'Holz, R.C.'  5 ? 
# 
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 'Cobalt-containing nitrile hydratase subunit alpha' 23155.592 1   4.2.1.84 S112A ? ? 
2 polymer     man 'Cobalt-containing nitrile hydratase subunit beta'  26170.148 1   4.2.1.84 ?     ? ? 
3 non-polymer syn GLYCEROL                                            92.094    1   ?        ?     ? ? 
4 water       nat water                                               18.015    251 ?        ?     ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 L-NHase,L-nitrilase 
2 L-NHase,L-nitrilase 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MTENILRKSDEEIQKEITARVKALESMLIEQGILTTSMIDRMAEIYENEVGPHLGAKVVVKAWTDPEFKKRLLADGTEAC
KELGIGGLQGEDMMWVENTDEVHHVVVCTLCACYPWPVLGLPPNWFKEPQYRSRVVREPRQLLKEEFGFEVPPSKEIKVW
DSSSEMRFVVLPQRPAGTDGWSEEELATLVTRESMIGVEPAKAV
;
;MTENILRKSDEEIQKEITARVKALESMLIEQGILTTSMIDRMAEIYENEVGPHLGAKVVVKAWTDPEFKKRLLADGTEAC
KELGIGGLQGEDMMWVENTDEVHHVVVCTLCACYPWPVLGLPPNWFKEPQYRSRVVREPRQLLKEEFGFEVPPSKEIKVW
DSSSEMRFVVLPQRPAGTDGWSEEELATLVTRESMIGVEPAKAV
;
A ? 
2 'polypeptide(L)' no no 
;MNGVYDVGGTDGLGPINRPADEPVFRAEWEKVAFAMFPATFRAGFMGLDEFRFGIEQMNPAEYLESPYYWHWIRTYIHHG
VRTGKIDLEELERRTQYYRENPDAPLPEHEQKPELIEFVNQAVYGGLPASREVDRPPKFKEGDVVRFSTASPKGHARRAR
YVRGKTGTVVKHHGAYIYPDTAGNGLGECPEHLYTVRFTAQELWGPEGDPNSSVYYDCWEPYIELVDT
;
;MNGVYDVGGTDGLGPINRPADEPVFRAEWEKVAFAMFPATFRAGFMGLDEFRFGIEQMNPAEYLESPYYWHWIRTYIHHG
VRTGKIDLEELERRTQYYRENPDAPLPEHEQKPELIEFVNQAVYGGLPASREVDRPPKFKEGDVVRFSTASPKGHARRAR
YVRGKTGTVVKHHGAYIYPDTAGNGLGECPEHLYTVRFTAQELWGPEGDPNSSVYYDCWEPYIELVDT
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCEROL GOL 
4 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   GLU n 
1 4   ASN n 
1 5   ILE n 
1 6   LEU n 
1 7   ARG n 
1 8   LYS n 
1 9   SER n 
1 10  ASP n 
1 11  GLU n 
1 12  GLU n 
1 13  ILE n 
1 14  GLN n 
1 15  LYS n 
1 16  GLU n 
1 17  ILE n 
1 18  THR n 
1 19  ALA n 
1 20  ARG n 
1 21  VAL n 
1 22  LYS n 
1 23  ALA n 
1 24  LEU n 
1 25  GLU n 
1 26  SER n 
1 27  MET n 
1 28  LEU n 
1 29  ILE n 
1 30  GLU n 
1 31  GLN n 
1 32  GLY n 
1 33  ILE n 
1 34  LEU n 
1 35  THR n 
1 36  THR n 
1 37  SER n 
1 38  MET n 
1 39  ILE n 
1 40  ASP n 
1 41  ARG n 
1 42  MET n 
1 43  ALA n 
1 44  GLU n 
1 45  ILE n 
1 46  TYR n 
1 47  GLU n 
1 48  ASN n 
1 49  GLU n 
1 50  VAL n 
1 51  GLY n 
1 52  PRO n 
1 53  HIS n 
1 54  LEU n 
1 55  GLY n 
1 56  ALA n 
1 57  LYS n 
1 58  VAL n 
1 59  VAL n 
1 60  VAL n 
1 61  LYS n 
1 62  ALA n 
1 63  TRP n 
1 64  THR n 
1 65  ASP n 
1 66  PRO n 
1 67  GLU n 
1 68  PHE n 
1 69  LYS n 
1 70  LYS n 
1 71  ARG n 
1 72  LEU n 
1 73  LEU n 
1 74  ALA n 
1 75  ASP n 
1 76  GLY n 
1 77  THR n 
1 78  GLU n 
1 79  ALA n 
1 80  CYS n 
1 81  LYS n 
1 82  GLU n 
1 83  LEU n 
1 84  GLY n 
1 85  ILE n 
1 86  GLY n 
1 87  GLY n 
1 88  LEU n 
1 89  GLN n 
1 90  GLY n 
1 91  GLU n 
1 92  ASP n 
1 93  MET n 
1 94  MET n 
1 95  TRP n 
1 96  VAL n 
1 97  GLU n 
1 98  ASN n 
1 99  THR n 
1 100 ASP n 
1 101 GLU n 
1 102 VAL n 
1 103 HIS n 
1 104 HIS n 
1 105 VAL n 
1 106 VAL n 
1 107 VAL n 
1 108 CYS n 
1 109 THR n 
1 110 LEU n 
1 111 CYS n 
1 112 ALA n 
1 113 CYS n 
1 114 TYR n 
1 115 PRO n 
1 116 TRP n 
1 117 PRO n 
1 118 VAL n 
1 119 LEU n 
1 120 GLY n 
1 121 LEU n 
1 122 PRO n 
1 123 PRO n 
1 124 ASN n 
1 125 TRP n 
1 126 PHE n 
1 127 LYS n 
1 128 GLU n 
1 129 PRO n 
1 130 GLN n 
1 131 TYR n 
1 132 ARG n 
1 133 SER n 
1 134 ARG n 
1 135 VAL n 
1 136 VAL n 
1 137 ARG n 
1 138 GLU n 
1 139 PRO n 
1 140 ARG n 
1 141 GLN n 
1 142 LEU n 
1 143 LEU n 
1 144 LYS n 
1 145 GLU n 
1 146 GLU n 
1 147 PHE n 
1 148 GLY n 
1 149 PHE n 
1 150 GLU n 
1 151 VAL n 
1 152 PRO n 
1 153 PRO n 
1 154 SER n 
1 155 LYS n 
1 156 GLU n 
1 157 ILE n 
1 158 LYS n 
1 159 VAL n 
1 160 TRP n 
1 161 ASP n 
1 162 SER n 
1 163 SER n 
1 164 SER n 
1 165 GLU n 
1 166 MET n 
1 167 ARG n 
1 168 PHE n 
1 169 VAL n 
1 170 VAL n 
1 171 LEU n 
1 172 PRO n 
1 173 GLN n 
1 174 ARG n 
1 175 PRO n 
1 176 ALA n 
1 177 GLY n 
1 178 THR n 
1 179 ASP n 
1 180 GLY n 
1 181 TRP n 
1 182 SER n 
1 183 GLU n 
1 184 GLU n 
1 185 GLU n 
1 186 LEU n 
1 187 ALA n 
1 188 THR n 
1 189 LEU n 
1 190 VAL n 
1 191 THR n 
1 192 ARG n 
1 193 GLU n 
1 194 SER n 
1 195 MET n 
1 196 ILE n 
1 197 GLY n 
1 198 VAL n 
1 199 GLU n 
1 200 PRO n 
1 201 ALA n 
1 202 LYS n 
1 203 ALA n 
1 204 VAL n 
2 1   MET n 
2 2   ASN n 
2 3   GLY n 
2 4   VAL n 
2 5   TYR n 
2 6   ASP n 
2 7   VAL n 
2 8   GLY n 
2 9   GLY n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  LEU n 
2 14  GLY n 
2 15  PRO n 
2 16  ILE n 
2 17  ASN n 
2 18  ARG n 
2 19  PRO n 
2 20  ALA n 
2 21  ASP n 
2 22  GLU n 
2 23  PRO n 
2 24  VAL n 
2 25  PHE n 
2 26  ARG n 
2 27  ALA n 
2 28  GLU n 
2 29  TRP n 
2 30  GLU n 
2 31  LYS n 
2 32  VAL n 
2 33  ALA n 
2 34  PHE n 
2 35  ALA n 
2 36  MET n 
2 37  PHE n 
2 38  PRO n 
2 39  ALA n 
2 40  THR n 
2 41  PHE n 
2 42  ARG n 
2 43  ALA n 
2 44  GLY n 
2 45  PHE n 
2 46  MET n 
2 47  GLY n 
2 48  LEU n 
2 49  ASP n 
2 50  GLU n 
2 51  PHE n 
2 52  ARG n 
2 53  PHE n 
2 54  GLY n 
2 55  ILE n 
2 56  GLU n 
2 57  GLN n 
2 58  MET n 
2 59  ASN n 
2 60  PRO n 
2 61  ALA n 
2 62  GLU n 
2 63  TYR n 
2 64  LEU n 
2 65  GLU n 
2 66  SER n 
2 67  PRO n 
2 68  TYR n 
2 69  TYR n 
2 70  TRP n 
2 71  HIS n 
2 72  TRP n 
2 73  ILE n 
2 74  ARG n 
2 75  THR n 
2 76  TYR n 
2 77  ILE n 
2 78  HIS n 
2 79  HIS n 
2 80  GLY n 
2 81  VAL n 
2 82  ARG n 
2 83  THR n 
2 84  GLY n 
2 85  LYS n 
2 86  ILE n 
2 87  ASP n 
2 88  LEU n 
2 89  GLU n 
2 90  GLU n 
2 91  LEU n 
2 92  GLU n 
2 93  ARG n 
2 94  ARG n 
2 95  THR n 
2 96  GLN n 
2 97  TYR n 
2 98  TYR n 
2 99  ARG n 
2 100 GLU n 
2 101 ASN n 
2 102 PRO n 
2 103 ASP n 
2 104 ALA n 
2 105 PRO n 
2 106 LEU n 
2 107 PRO n 
2 108 GLU n 
2 109 HIS n 
2 110 GLU n 
2 111 GLN n 
2 112 LYS n 
2 113 PRO n 
2 114 GLU n 
2 115 LEU n 
2 116 ILE n 
2 117 GLU n 
2 118 PHE n 
2 119 VAL n 
2 120 ASN n 
2 121 GLN n 
2 122 ALA n 
2 123 VAL n 
2 124 TYR n 
2 125 GLY n 
2 126 GLY n 
2 127 LEU n 
2 128 PRO n 
2 129 ALA n 
2 130 SER n 
2 131 ARG n 
2 132 GLU n 
2 133 VAL n 
2 134 ASP n 
2 135 ARG n 
2 136 PRO n 
2 137 PRO n 
2 138 LYS n 
2 139 PHE n 
2 140 LYS n 
2 141 GLU n 
2 142 GLY n 
2 143 ASP n 
2 144 VAL n 
2 145 VAL n 
2 146 ARG n 
2 147 PHE n 
2 148 SER n 
2 149 THR n 
2 150 ALA n 
2 151 SER n 
2 152 PRO n 
2 153 LYS n 
2 154 GLY n 
2 155 HIS n 
2 156 ALA n 
2 157 ARG n 
2 158 ARG n 
2 159 ALA n 
2 160 ARG n 
2 161 TYR n 
2 162 VAL n 
2 163 ARG n 
2 164 GLY n 
2 165 LYS n 
2 166 THR n 
2 167 GLY n 
2 168 THR n 
2 169 VAL n 
2 170 VAL n 
2 171 LYS n 
2 172 HIS n 
2 173 HIS n 
2 174 GLY n 
2 175 ALA n 
2 176 TYR n 
2 177 ILE n 
2 178 TYR n 
2 179 PRO n 
2 180 ASP n 
2 181 THR n 
2 182 ALA n 
2 183 GLY n 
2 184 ASN n 
2 185 GLY n 
2 186 LEU n 
2 187 GLY n 
2 188 GLU n 
2 189 CYS n 
2 190 PRO n 
2 191 GLU n 
2 192 HIS n 
2 193 LEU n 
2 194 TYR n 
2 195 THR n 
2 196 VAL n 
2 197 ARG n 
2 198 PHE n 
2 199 THR n 
2 200 ALA n 
2 201 GLN n 
2 202 GLU n 
2 203 LEU n 
2 204 TRP n 
2 205 GLY n 
2 206 PRO n 
2 207 GLU n 
2 208 GLY n 
2 209 ASP n 
2 210 PRO n 
2 211 ASN n 
2 212 SER n 
2 213 SER n 
2 214 VAL n 
2 215 TYR n 
2 216 TYR n 
2 217 ASP n 
2 218 CYS n 
2 219 TRP n 
2 220 GLU n 
2 221 PRO n 
2 222 TYR n 
2 223 ILE n 
2 224 GLU n 
2 225 LEU n 
2 226 VAL n 
2 227 ASP n 
2 228 THR n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 204 ? ? ? ? ? ? ? ? ? 'Pseudonocardia thermophila' 1848 ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 228 ? ? ? ? ? ? ? ? ? 'Pseudonocardia thermophila' 1848 ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  MET 27  27  27  MET MET A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  MET 38  38  38  MET MET A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  MET 42  42  42  MET MET A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  TRP 63  63  63  TRP TRP A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  CYS 80  80  80  CYS CYS A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  MET 93  93  93  MET MET A . n 
A 1 94  MET 94  94  94  MET MET A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 CYS 108 108 108 CYS CYS A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 CYS 111 111 111 CYS CSD A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 CYS 113 113 113 CYS CSO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 TRP 116 116 116 TRP TRP A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 TRP 125 125 125 TRP TRP A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 PRO 139 139 139 PRO PRO A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 LYS 144 144 144 LYS LYS A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 TRP 160 160 160 TRP TRP A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 TRP 181 181 181 TRP TRP A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 MET 195 195 195 MET MET A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
B 2 1   MET 1   1   1   MET MET B . n 
B 2 2   ASN 2   2   2   ASN ASN B . n 
B 2 3   GLY 3   3   3   GLY GLY B . n 
B 2 4   VAL 4   4   4   VAL VAL B . n 
B 2 5   TYR 5   5   5   TYR TYR B . n 
B 2 6   ASP 6   6   6   ASP ASP B . n 
B 2 7   VAL 7   7   7   VAL VAL B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   GLY 9   9   9   GLY GLY B . n 
B 2 10  THR 10  10  10  THR THR B . n 
B 2 11  ASP 11  11  11  ASP ASP B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  LEU 13  13  13  LEU LEU B . n 
B 2 14  GLY 14  14  14  GLY GLY B . n 
B 2 15  PRO 15  15  15  PRO PRO B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  ASN 17  17  17  ASN ASN B . n 
B 2 18  ARG 18  18  18  ARG ARG B . n 
B 2 19  PRO 19  19  19  PRO PRO B . n 
B 2 20  ALA 20  20  20  ALA ALA B . n 
B 2 21  ASP 21  21  21  ASP ASP B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  PRO 23  23  23  PRO PRO B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  PHE 25  25  25  PHE PHE B . n 
B 2 26  ARG 26  26  26  ARG ARG B . n 
B 2 27  ALA 27  27  27  ALA ALA B . n 
B 2 28  GLU 28  28  28  GLU GLU B . n 
B 2 29  TRP 29  29  29  TRP TRP B . n 
B 2 30  GLU 30  30  30  GLU GLU B . n 
B 2 31  LYS 31  31  31  LYS LYS B . n 
B 2 32  VAL 32  32  32  VAL VAL B . n 
B 2 33  ALA 33  33  33  ALA ALA B . n 
B 2 34  PHE 34  34  34  PHE PHE B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  MET 36  36  36  MET MET B . n 
B 2 37  PHE 37  37  37  PHE PHE B . n 
B 2 38  PRO 38  38  38  PRO PRO B . n 
B 2 39  ALA 39  39  39  ALA ALA B . n 
B 2 40  THR 40  40  40  THR THR B . n 
B 2 41  PHE 41  41  41  PHE PHE B . n 
B 2 42  ARG 42  42  42  ARG ARG B . n 
B 2 43  ALA 43  43  43  ALA ALA B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  PHE 45  45  45  PHE PHE B . n 
B 2 46  MET 46  46  46  MET MET B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  LEU 48  48  48  LEU LEU B . n 
B 2 49  ASP 49  49  49  ASP ASP B . n 
B 2 50  GLU 50  50  50  GLU GLU B . n 
B 2 51  PHE 51  51  51  PHE PHE B . n 
B 2 52  ARG 52  52  52  ARG ARG B . n 
B 2 53  PHE 53  53  53  PHE PHE B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  ILE 55  55  55  ILE ILE B . n 
B 2 56  GLU 56  56  56  GLU GLU B . n 
B 2 57  GLN 57  57  57  GLN GLN B . n 
B 2 58  MET 58  58  58  MET MET B . n 
B 2 59  ASN 59  59  59  ASN ASN B . n 
B 2 60  PRO 60  60  60  PRO PRO B . n 
B 2 61  ALA 61  61  61  ALA ALA B . n 
B 2 62  GLU 62  62  62  GLU GLU B . n 
B 2 63  TYR 63  63  63  TYR TYR B . n 
B 2 64  LEU 64  64  64  LEU LEU B . n 
B 2 65  GLU 65  65  65  GLU GLU B . n 
B 2 66  SER 66  66  66  SER SER B . n 
B 2 67  PRO 67  67  67  PRO PRO B . n 
B 2 68  TYR 68  68  68  TYR TYR B . n 
B 2 69  TYR 69  69  69  TYR TYR B . n 
B 2 70  TRP 70  70  70  TRP TRP B . n 
B 2 71  HIS 71  71  71  HIS HIS B . n 
B 2 72  TRP 72  72  72  TRP TRP B . n 
B 2 73  ILE 73  73  73  ILE ILE B . n 
B 2 74  ARG 74  74  74  ARG ARG B . n 
B 2 75  THR 75  75  75  THR THR B . n 
B 2 76  TYR 76  76  76  TYR TYR B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  HIS 78  78  78  HIS HIS B . n 
B 2 79  HIS 79  79  79  HIS HIS B . n 
B 2 80  GLY 80  80  80  GLY GLY B . n 
B 2 81  VAL 81  81  81  VAL VAL B . n 
B 2 82  ARG 82  82  82  ARG ARG B . n 
B 2 83  THR 83  83  83  THR THR B . n 
B 2 84  GLY 84  84  84  GLY GLY B . n 
B 2 85  LYS 85  85  85  LYS LYS B . n 
B 2 86  ILE 86  86  86  ILE ILE B . n 
B 2 87  ASP 87  87  87  ASP ASP B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  GLU 89  89  89  GLU GLU B . n 
B 2 90  GLU 90  90  90  GLU GLU B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  GLU 92  92  92  GLU GLU B . n 
B 2 93  ARG 93  93  93  ARG ARG B . n 
B 2 94  ARG 94  94  94  ARG ARG B . n 
B 2 95  THR 95  95  95  THR THR B . n 
B 2 96  GLN 96  96  96  GLN GLN B . n 
B 2 97  TYR 97  97  97  TYR TYR B . n 
B 2 98  TYR 98  98  98  TYR TYR B . n 
B 2 99  ARG 99  99  99  ARG ARG B . n 
B 2 100 GLU 100 100 100 GLU GLU B . n 
B 2 101 ASN 101 101 101 ASN ASN B . n 
B 2 102 PRO 102 102 102 PRO PRO B . n 
B 2 103 ASP 103 103 103 ASP ASP B . n 
B 2 104 ALA 104 104 104 ALA ALA B . n 
B 2 105 PRO 105 105 105 PRO PRO B . n 
B 2 106 LEU 106 106 106 LEU LEU B . n 
B 2 107 PRO 107 107 107 PRO PRO B . n 
B 2 108 GLU 108 108 108 GLU GLU B . n 
B 2 109 HIS 109 109 109 HIS HIS B . n 
B 2 110 GLU 110 110 110 GLU GLU B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 LYS 112 112 112 LYS LYS B . n 
B 2 113 PRO 113 113 113 PRO PRO B . n 
B 2 114 GLU 114 114 114 GLU GLU B . n 
B 2 115 LEU 115 115 115 LEU LEU B . n 
B 2 116 ILE 116 116 116 ILE ILE B . n 
B 2 117 GLU 117 117 117 GLU GLU B . n 
B 2 118 PHE 118 118 118 PHE PHE B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 ASN 120 120 120 ASN ASN B . n 
B 2 121 GLN 121 121 121 GLN GLN B . n 
B 2 122 ALA 122 122 122 ALA ALA B . n 
B 2 123 VAL 123 123 123 VAL VAL B . n 
B 2 124 TYR 124 124 124 TYR TYR B . n 
B 2 125 GLY 125 125 125 GLY GLY B . n 
B 2 126 GLY 126 126 126 GLY GLY B . n 
B 2 127 LEU 127 127 127 LEU LEU B . n 
B 2 128 PRO 128 128 128 PRO PRO B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 SER 130 130 130 SER SER B . n 
B 2 131 ARG 131 131 131 ARG ARG B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 VAL 133 133 133 VAL VAL B . n 
B 2 134 ASP 134 134 134 ASP ASP B . n 
B 2 135 ARG 135 135 135 ARG ARG B . n 
B 2 136 PRO 136 136 136 PRO PRO B . n 
B 2 137 PRO 137 137 137 PRO PRO B . n 
B 2 138 LYS 138 138 138 LYS LYS B . n 
B 2 139 PHE 139 139 139 PHE PHE B . n 
B 2 140 LYS 140 140 140 LYS LYS B . n 
B 2 141 GLU 141 141 141 GLU GLU B . n 
B 2 142 GLY 142 142 142 GLY GLY B . n 
B 2 143 ASP 143 143 143 ASP ASP B . n 
B 2 144 VAL 144 144 144 VAL VAL B . n 
B 2 145 VAL 145 145 145 VAL VAL B . n 
B 2 146 ARG 146 146 146 ARG ARG B . n 
B 2 147 PHE 147 147 147 PHE PHE B . n 
B 2 148 SER 148 148 148 SER SER B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 ALA 150 150 150 ALA ALA B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 PRO 152 152 152 PRO PRO B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 GLY 154 154 154 GLY GLY B . n 
B 2 155 HIS 155 155 155 HIS HIS B . n 
B 2 156 ALA 156 156 156 ALA ALA B . n 
B 2 157 ARG 157 157 157 ARG ARG B . n 
B 2 158 ARG 158 158 158 ARG ARG B . n 
B 2 159 ALA 159 159 159 ALA ALA B . n 
B 2 160 ARG 160 160 160 ARG ARG B . n 
B 2 161 TYR 161 161 161 TYR TYR B . n 
B 2 162 VAL 162 162 162 VAL VAL B . n 
B 2 163 ARG 163 163 163 ARG ARG B . n 
B 2 164 GLY 164 164 164 GLY GLY B . n 
B 2 165 LYS 165 165 165 LYS LYS B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 GLY 167 167 167 GLY GLY B . n 
B 2 168 THR 168 168 168 THR THR B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 VAL 170 170 170 VAL VAL B . n 
B 2 171 LYS 171 171 171 LYS LYS B . n 
B 2 172 HIS 172 172 172 HIS HIS B . n 
B 2 173 HIS 173 173 173 HIS HIS B . n 
B 2 174 GLY 174 174 174 GLY GLY B . n 
B 2 175 ALA 175 175 175 ALA ALA B . n 
B 2 176 TYR 176 176 176 TYR TYR B . n 
B 2 177 ILE 177 177 177 ILE ILE B . n 
B 2 178 TYR 178 178 178 TYR TYR B . n 
B 2 179 PRO 179 179 179 PRO PRO B . n 
B 2 180 ASP 180 180 180 ASP ASP B . n 
B 2 181 THR 181 181 181 THR THR B . n 
B 2 182 ALA 182 182 182 ALA ALA B . n 
B 2 183 GLY 183 183 183 GLY GLY B . n 
B 2 184 ASN 184 184 184 ASN ASN B . n 
B 2 185 GLY 185 185 185 GLY GLY B . n 
B 2 186 LEU 186 186 186 LEU LEU B . n 
B 2 187 GLY 187 187 187 GLY GLY B . n 
B 2 188 GLU 188 188 188 GLU GLU B . n 
B 2 189 CYS 189 189 189 CYS CYS B . n 
B 2 190 PRO 190 190 190 PRO PRO B . n 
B 2 191 GLU 191 191 191 GLU GLU B . n 
B 2 192 HIS 192 192 192 HIS HIS B . n 
B 2 193 LEU 193 193 193 LEU LEU B . n 
B 2 194 TYR 194 194 194 TYR TYR B . n 
B 2 195 THR 195 195 195 THR THR B . n 
B 2 196 VAL 196 196 196 VAL VAL B . n 
B 2 197 ARG 197 197 197 ARG ARG B . n 
B 2 198 PHE 198 198 198 PHE PHE B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 ALA 200 200 200 ALA ALA B . n 
B 2 201 GLN 201 201 201 GLN GLN B . n 
B 2 202 GLU 202 202 202 GLU GLU B . n 
B 2 203 LEU 203 203 203 LEU LEU B . n 
B 2 204 TRP 204 204 204 TRP TRP B . n 
B 2 205 GLY 205 205 205 GLY GLY B . n 
B 2 206 PRO 206 206 206 PRO PRO B . n 
B 2 207 GLU 207 207 207 GLU GLU B . n 
B 2 208 GLY 208 208 208 GLY GLY B . n 
B 2 209 ASP 209 209 209 ASP ASP B . n 
B 2 210 PRO 210 210 210 PRO PRO B . n 
B 2 211 ASN 211 211 211 ASN ASN B . n 
B 2 212 SER 212 212 212 SER SER B . n 
B 2 213 SER 213 213 213 SER SER B . n 
B 2 214 VAL 214 214 214 VAL VAL B . n 
B 2 215 TYR 215 215 215 TYR TYR B . n 
B 2 216 TYR 216 216 216 TYR TYR B . n 
B 2 217 ASP 217 217 217 ASP ASP B . n 
B 2 218 CYS 218 218 218 CYS CYS B . n 
B 2 219 TRP 219 219 219 TRP TRP B . n 
B 2 220 GLU 220 220 220 GLU GLU B . n 
B 2 221 PRO 221 221 221 PRO PRO B . n 
B 2 222 TYR 222 222 222 TYR TYR B . n 
B 2 223 ILE 223 223 223 ILE ILE B . n 
B 2 224 GLU 224 224 224 GLU GLU B . n 
B 2 225 LEU 225 225 225 LEU LEU B . n 
B 2 226 VAL 226 226 226 VAL VAL B . n 
B 2 227 ASP 227 227 227 ASP ASP B . n 
B 2 228 THR 228 228 228 THR THR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GOL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 GOL 1   301 301 GOL LIG A . 
D 4 HOH 1   401 191 HOH HOH A . 
D 4 HOH 2   402 142 HOH HOH A . 
D 4 HOH 3   403 67  HOH HOH A . 
D 4 HOH 4   404 41  HOH HOH A . 
D 4 HOH 5   405 153 HOH HOH A . 
D 4 HOH 6   406 40  HOH HOH A . 
D 4 HOH 7   407 195 HOH HOH A . 
D 4 HOH 8   408 177 HOH HOH A . 
D 4 HOH 9   409 169 HOH HOH A . 
D 4 HOH 10  410 56  HOH HOH A . 
D 4 HOH 11  411 175 HOH HOH A . 
D 4 HOH 12  412 62  HOH HOH A . 
D 4 HOH 13  413 57  HOH HOH A . 
D 4 HOH 14  414 58  HOH HOH A . 
D 4 HOH 15  415 167 HOH HOH A . 
D 4 HOH 16  416 98  HOH HOH A . 
D 4 HOH 17  417 74  HOH HOH A . 
D 4 HOH 18  418 19  HOH HOH A . 
D 4 HOH 19  419 248 HOH HOH A . 
D 4 HOH 20  420 171 HOH HOH A . 
D 4 HOH 21  421 120 HOH HOH A . 
D 4 HOH 22  422 100 HOH HOH A . 
D 4 HOH 23  423 226 HOH HOH A . 
D 4 HOH 24  424 18  HOH HOH A . 
D 4 HOH 25  425 38  HOH HOH A . 
D 4 HOH 26  426 190 HOH HOH A . 
D 4 HOH 27  427 215 HOH HOH A . 
D 4 HOH 28  428 115 HOH HOH A . 
D 4 HOH 29  429 87  HOH HOH A . 
D 4 HOH 30  430 42  HOH HOH A . 
D 4 HOH 31  431 178 HOH HOH A . 
D 4 HOH 32  432 14  HOH HOH A . 
D 4 HOH 33  433 146 HOH HOH A . 
D 4 HOH 34  434 194 HOH HOH A . 
D 4 HOH 35  435 136 HOH HOH A . 
D 4 HOH 36  436 173 HOH HOH A . 
D 4 HOH 37  437 111 HOH HOH A . 
D 4 HOH 38  438 151 HOH HOH A . 
D 4 HOH 39  439 26  HOH HOH A . 
D 4 HOH 40  440 30  HOH HOH A . 
D 4 HOH 41  441 78  HOH HOH A . 
D 4 HOH 42  442 35  HOH HOH A . 
D 4 HOH 43  443 211 HOH HOH A . 
D 4 HOH 44  444 201 HOH HOH A . 
D 4 HOH 45  445 113 HOH HOH A . 
D 4 HOH 46  446 85  HOH HOH A . 
D 4 HOH 47  447 37  HOH HOH A . 
D 4 HOH 48  448 22  HOH HOH A . 
D 4 HOH 49  449 221 HOH HOH A . 
D 4 HOH 50  450 131 HOH HOH A . 
D 4 HOH 51  451 150 HOH HOH A . 
D 4 HOH 52  452 126 HOH HOH A . 
D 4 HOH 53  453 50  HOH HOH A . 
D 4 HOH 54  454 43  HOH HOH A . 
D 4 HOH 55  455 157 HOH HOH A . 
D 4 HOH 56  456 8   HOH HOH A . 
D 4 HOH 57  457 1   HOH HOH A . 
D 4 HOH 58  458 129 HOH HOH A . 
D 4 HOH 59  459 76  HOH HOH A . 
D 4 HOH 60  460 176 HOH HOH A . 
D 4 HOH 61  461 25  HOH HOH A . 
D 4 HOH 62  462 144 HOH HOH A . 
D 4 HOH 63  463 135 HOH HOH A . 
D 4 HOH 64  464 90  HOH HOH A . 
D 4 HOH 65  465 82  HOH HOH A . 
D 4 HOH 66  466 45  HOH HOH A . 
D 4 HOH 67  467 123 HOH HOH A . 
D 4 HOH 68  468 9   HOH HOH A . 
D 4 HOH 69  469 207 HOH HOH A . 
D 4 HOH 70  470 32  HOH HOH A . 
D 4 HOH 71  471 7   HOH HOH A . 
D 4 HOH 72  472 121 HOH HOH A . 
D 4 HOH 73  473 93  HOH HOH A . 
D 4 HOH 74  474 155 HOH HOH A . 
D 4 HOH 75  475 162 HOH HOH A . 
D 4 HOH 76  476 105 HOH HOH A . 
D 4 HOH 77  477 237 HOH HOH A . 
D 4 HOH 78  478 17  HOH HOH A . 
D 4 HOH 79  479 130 HOH HOH A . 
D 4 HOH 80  480 180 HOH HOH A . 
D 4 HOH 81  481 91  HOH HOH A . 
D 4 HOH 82  482 200 HOH HOH A . 
D 4 HOH 83  483 147 HOH HOH A . 
D 4 HOH 84  484 232 HOH HOH A . 
D 4 HOH 85  485 149 HOH HOH A . 
D 4 HOH 86  486 106 HOH HOH A . 
D 4 HOH 87  487 231 HOH HOH A . 
D 4 HOH 88  488 225 HOH HOH A . 
D 4 HOH 89  489 249 HOH HOH A . 
D 4 HOH 90  490 251 HOH HOH A . 
D 4 HOH 91  491 104 HOH HOH A . 
E 4 HOH 1   301 204 HOH HOH B . 
E 4 HOH 2   302 145 HOH HOH B . 
E 4 HOH 3   303 243 HOH HOH B . 
E 4 HOH 4   304 65  HOH HOH B . 
E 4 HOH 5   305 166 HOH HOH B . 
E 4 HOH 6   306 208 HOH HOH B . 
E 4 HOH 7   307 116 HOH HOH B . 
E 4 HOH 8   308 188 HOH HOH B . 
E 4 HOH 9   309 4   HOH HOH B . 
E 4 HOH 10  310 187 HOH HOH B . 
E 4 HOH 11  311 83  HOH HOH B . 
E 4 HOH 12  312 39  HOH HOH B . 
E 4 HOH 13  313 103 HOH HOH B . 
E 4 HOH 14  314 21  HOH HOH B . 
E 4 HOH 15  315 156 HOH HOH B . 
E 4 HOH 16  316 80  HOH HOH B . 
E 4 HOH 17  317 79  HOH HOH B . 
E 4 HOH 18  318 86  HOH HOH B . 
E 4 HOH 19  319 29  HOH HOH B . 
E 4 HOH 20  320 28  HOH HOH B . 
E 4 HOH 21  321 102 HOH HOH B . 
E 4 HOH 22  322 88  HOH HOH B . 
E 4 HOH 23  323 53  HOH HOH B . 
E 4 HOH 24  324 46  HOH HOH B . 
E 4 HOH 25  325 128 HOH HOH B . 
E 4 HOH 26  326 213 HOH HOH B . 
E 4 HOH 27  327 148 HOH HOH B . 
E 4 HOH 28  328 16  HOH HOH B . 
E 4 HOH 29  329 118 HOH HOH B . 
E 4 HOH 30  330 159 HOH HOH B . 
E 4 HOH 31  331 89  HOH HOH B . 
E 4 HOH 32  332 48  HOH HOH B . 
E 4 HOH 33  333 31  HOH HOH B . 
E 4 HOH 34  334 66  HOH HOH B . 
E 4 HOH 35  335 59  HOH HOH B . 
E 4 HOH 36  336 112 HOH HOH B . 
E 4 HOH 37  337 49  HOH HOH B . 
E 4 HOH 38  338 54  HOH HOH B . 
E 4 HOH 39  339 110 HOH HOH B . 
E 4 HOH 40  340 107 HOH HOH B . 
E 4 HOH 41  341 94  HOH HOH B . 
E 4 HOH 42  342 216 HOH HOH B . 
E 4 HOH 43  343 203 HOH HOH B . 
E 4 HOH 44  344 64  HOH HOH B . 
E 4 HOH 45  345 138 HOH HOH B . 
E 4 HOH 46  346 114 HOH HOH B . 
E 4 HOH 47  347 240 HOH HOH B . 
E 4 HOH 48  348 164 HOH HOH B . 
E 4 HOH 49  349 2   HOH HOH B . 
E 4 HOH 50  350 81  HOH HOH B . 
E 4 HOH 51  351 84  HOH HOH B . 
E 4 HOH 52  352 141 HOH HOH B . 
E 4 HOH 53  353 44  HOH HOH B . 
E 4 HOH 54  354 109 HOH HOH B . 
E 4 HOH 55  355 75  HOH HOH B . 
E 4 HOH 56  356 55  HOH HOH B . 
E 4 HOH 57  357 52  HOH HOH B . 
E 4 HOH 58  358 184 HOH HOH B . 
E 4 HOH 59  359 117 HOH HOH B . 
E 4 HOH 60  360 11  HOH HOH B . 
E 4 HOH 61  361 51  HOH HOH B . 
E 4 HOH 62  362 163 HOH HOH B . 
E 4 HOH 63  363 6   HOH HOH B . 
E 4 HOH 64  364 197 HOH HOH B . 
E 4 HOH 65  365 134 HOH HOH B . 
E 4 HOH 66  366 229 HOH HOH B . 
E 4 HOH 67  367 71  HOH HOH B . 
E 4 HOH 68  368 33  HOH HOH B . 
E 4 HOH 69  369 61  HOH HOH B . 
E 4 HOH 70  370 137 HOH HOH B . 
E 4 HOH 71  371 13  HOH HOH B . 
E 4 HOH 72  372 158 HOH HOH B . 
E 4 HOH 73  373 23  HOH HOH B . 
E 4 HOH 74  374 140 HOH HOH B . 
E 4 HOH 75  375 10  HOH HOH B . 
E 4 HOH 76  376 34  HOH HOH B . 
E 4 HOH 77  377 202 HOH HOH B . 
E 4 HOH 78  378 101 HOH HOH B . 
E 4 HOH 79  379 172 HOH HOH B . 
E 4 HOH 80  380 192 HOH HOH B . 
E 4 HOH 81  381 127 HOH HOH B . 
E 4 HOH 82  382 60  HOH HOH B . 
E 4 HOH 83  383 218 HOH HOH B . 
E 4 HOH 84  384 5   HOH HOH B . 
E 4 HOH 85  385 27  HOH HOH B . 
E 4 HOH 86  386 92  HOH HOH B . 
E 4 HOH 87  387 143 HOH HOH B . 
E 4 HOH 88  388 230 HOH HOH B . 
E 4 HOH 89  389 183 HOH HOH B . 
E 4 HOH 90  390 95  HOH HOH B . 
E 4 HOH 91  391 206 HOH HOH B . 
E 4 HOH 92  392 108 HOH HOH B . 
E 4 HOH 93  393 73  HOH HOH B . 
E 4 HOH 94  394 220 HOH HOH B . 
E 4 HOH 95  395 160 HOH HOH B . 
E 4 HOH 96  396 99  HOH HOH B . 
E 4 HOH 97  397 36  HOH HOH B . 
E 4 HOH 98  398 3   HOH HOH B . 
E 4 HOH 99  399 205 HOH HOH B . 
E 4 HOH 100 400 133 HOH HOH B . 
E 4 HOH 101 401 189 HOH HOH B . 
E 4 HOH 102 402 235 HOH HOH B . 
E 4 HOH 103 403 199 HOH HOH B . 
E 4 HOH 104 404 63  HOH HOH B . 
E 4 HOH 105 405 119 HOH HOH B . 
E 4 HOH 106 406 193 HOH HOH B . 
E 4 HOH 107 407 12  HOH HOH B . 
E 4 HOH 108 408 72  HOH HOH B . 
E 4 HOH 109 409 96  HOH HOH B . 
E 4 HOH 110 410 209 HOH HOH B . 
E 4 HOH 111 411 68  HOH HOH B . 
E 4 HOH 112 412 132 HOH HOH B . 
E 4 HOH 113 413 77  HOH HOH B . 
E 4 HOH 114 414 161 HOH HOH B . 
E 4 HOH 115 415 212 HOH HOH B . 
E 4 HOH 116 416 170 HOH HOH B . 
E 4 HOH 117 417 179 HOH HOH B . 
E 4 HOH 118 418 124 HOH HOH B . 
E 4 HOH 119 419 214 HOH HOH B . 
E 4 HOH 120 420 20  HOH HOH B . 
E 4 HOH 121 421 69  HOH HOH B . 
E 4 HOH 122 422 219 HOH HOH B . 
E 4 HOH 123 423 168 HOH HOH B . 
E 4 HOH 124 424 97  HOH HOH B . 
E 4 HOH 125 425 196 HOH HOH B . 
E 4 HOH 126 426 224 HOH HOH B . 
E 4 HOH 127 427 247 HOH HOH B . 
E 4 HOH 128 428 70  HOH HOH B . 
E 4 HOH 129 429 233 HOH HOH B . 
E 4 HOH 130 430 236 HOH HOH B . 
E 4 HOH 131 431 222 HOH HOH B . 
E 4 HOH 132 432 228 HOH HOH B . 
E 4 HOH 133 433 125 HOH HOH B . 
E 4 HOH 134 434 227 HOH HOH B . 
E 4 HOH 135 435 185 HOH HOH B . 
E 4 HOH 136 436 198 HOH HOH B . 
E 4 HOH 137 437 244 HOH HOH B . 
E 4 HOH 138 438 186 HOH HOH B . 
E 4 HOH 139 439 122 HOH HOH B . 
E 4 HOH 140 440 234 HOH HOH B . 
E 4 HOH 141 441 241 HOH HOH B . 
E 4 HOH 142 442 15  HOH HOH B . 
E 4 HOH 143 443 238 HOH HOH B . 
E 4 HOH 144 444 182 HOH HOH B . 
E 4 HOH 145 445 181 HOH HOH B . 
E 4 HOH 146 446 239 HOH HOH B . 
E 4 HOH 147 447 152 HOH HOH B . 
E 4 HOH 148 448 210 HOH HOH B . 
E 4 HOH 149 449 47  HOH HOH B . 
E 4 HOH 150 450 154 HOH HOH B . 
E 4 HOH 151 451 217 HOH HOH B . 
E 4 HOH 152 452 223 HOH HOH B . 
E 4 HOH 153 453 250 HOH HOH B . 
E 4 HOH 154 454 246 HOH HOH B . 
E 4 HOH 155 455 174 HOH HOH B . 
E 4 HOH 156 456 245 HOH HOH B . 
E 4 HOH 157 457 165 HOH HOH B . 
E 4 HOH 158 458 242 HOH HOH B . 
E 4 HOH 159 459 139 HOH HOH B . 
E 4 HOH 160 460 252 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D5U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.837 
_cell.length_a_esd                 ? 
_cell.length_b                     65.837 
_cell.length_b_esd                 ? 
_cell.length_c                     185.637 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9D5U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 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                   9D5U 
_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             2.35 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.76 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.2 M sodium citrate tribasic in 0.1 M HEPES at pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979460 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979460 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D5U 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.35 
_reflns.d_resolution_low                               35.99 
_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                                     100941 
_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                           97.60 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_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                              0.034 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.35 
_reflns_shell.d_res_low                                     1.38 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8715 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  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                          85.20 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.470 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9D5U 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.35 
_refine.ls_d_res_low                             35.99 
_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                     100941 
_refine.ls_number_reflns_R_free                  2044 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.60 
_refine.ls_percent_reflns_R_free                 2.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2521 
_refine.ls_R_factor_R_free                       0.2590 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2392 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          18.59 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.85 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.01 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3464 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.number_atoms_solvent             251 
_refine_hist.number_atoms_total               3721 
_refine_hist.d_res_high                       1.35 
_refine_hist.d_res_low                        35.99 
# 
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' ? 0.020 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 2.048 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.207 ? 482 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.080 ? 503 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 640 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.35 1.38 . . 120 5841 80.00 . . . . 0.3152 . . . . . . . . . . . 0.3152 
'X-RAY DIFFRACTION' 1.38 1.42 . . 142 6724 92.00 . . . . 0.3119 . . . . . . . . . . . 0.3126 
'X-RAY DIFFRACTION' 1.42 1.46 . . 136 6958 94.00 . . . . 0.2954 . . . . . . . . . . . 0.2954 
'X-RAY DIFFRACTION' 1.46 1.51 . . 136 6861 95.00 . . . . 0.2811 . . . . . . . . . . . 0.2811 
'X-RAY DIFFRACTION' 1.51 1.56 . . 146 7112 97.00 . . . . 0.3053 . . . . . . . . . . . 0.3053 
'X-RAY DIFFRACTION' 1.56 1.63 . . 146 7145 98.00 . . . . 0.2892 . . . . . . . . . . . 0.2892 
'X-RAY DIFFRACTION' 1.63 1.70 . . 146 7164 98.00 . . . . 0.3251 . . . . . . . . . . . 0.3517 
'X-RAY DIFFRACTION' 1.70 1.79 . . 142 7182 98.00 . . . . 0.3023 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 1.79 1.90 . . 148 7186 98.00 . . . . 0.3038 . . . . . . . . . . . 0.3038 
'X-RAY DIFFRACTION' 1.90 2.05 . . 147 7240 98.00 . . . . 0.2830 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 2.05 2.26 . . 144 7221 98.00 . . . . 0.2635 . . . . . . . . . . . 0.2977 
'X-RAY DIFFRACTION' 2.26 2.58 . . 149 7289 98.00 . . . . 0.2497 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 2.58 3.25 . . 152 7372 98.00 . . . . 0.2331 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 3.25 10   . . 158 7634 98.00 . . . . 0.1945 . . . . . . . . . . . 0.2463 
# 
_struct.entry_id                     9D5U 
_struct.title                        'Nitrile hydratase S112A mutant' 
_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        9D5U 
_struct_keywords.text            'Nitrile hydratase, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP NHAA_PSETH Q7SID2 ? 1 
;MTENILRKSDEEIQKEITARVKALESMLIEQGILTTSMIDRMAEIYENEVGPHLGAKVVVKAWTDPEFKKRLLADGTEAC
KELGIGGLQGEDMMWVENTDEVHHVVVCTLCSCYPWPVLGLPPNWFKEPQYRSRVVREPRQLLKEEFGFEVPPSKEIKVW
DSSSEMRFVVLPQRPAGTDGWSEEELATLVTRESMIGVEPAKAV
;
1 
2 UNP NHAB_PSETH Q7SID3 ? 2 
;MNGVYDVGGTDGLGPINRPADEPVFRAEWEKVAFAMFPATFRAGFMGLDEFRFGIEQMNPAEYLESPYYWHWIRTYIHHG
VRTGKIDLEELERRTQYYRENPDAPLPEHEQKPELIEFVNQAVYGGLPASREVDRPPKFKEGDVVRFSTASPKGHARRAR
YVRGKTGTVVKHHGAYIYPDTAGNGLGECPEHLYTVRFTAQELWGPEGDPNSSVYYDCWEPYIELVDT
;
1 
# 
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 9D5U A 1 ? 204 ? Q7SID2 1 ? 204 ? 1 204 
2 2 9D5U B 1 ? 228 ? Q7SID3 1 ? 228 ? 1 228 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9D5U 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      112 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q7SID2 
_struct_ref_seq_dif.db_mon_id                    SER 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          112 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            112 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 21760 ? 
1 MORE         -115  ? 
1 'SSA (A^2)'  32920 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z      1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_645 y+1,x-1,-z -0.5000000000 0.8660254038 0.0000000000 98.7555000000 0.8660254038 0.5000000000 
0.0000000000 -57.0165145090 0.0000000000 0.0000000000 -1.0000000000 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 SER A 9   ? GLN A 31  ? SER A 9   GLN A 31  1 ? 23 
HELX_P HELX_P2  AA2 THR A 35  ? GLU A 49  ? THR A 35  GLU A 49  1 ? 15 
HELX_P HELX_P3  AA3 GLY A 51  ? ASP A 65  ? GLY A 51  ASP A 65  1 ? 15 
HELX_P HELX_P4  AA4 ASP A 65  ? ASP A 75  ? ASP A 65  ASP A 75  1 ? 11 
HELX_P HELX_P5  AA5 ASP A 75  ? LEU A 83  ? ASP A 75  LEU A 83  1 ? 9  
HELX_P HELX_P6  AA6 PRO A 115 ? GLY A 120 ? PRO A 115 GLY A 120 1 ? 6  
HELX_P HELX_P7  AA7 PRO A 123 ? GLU A 128 ? PRO A 123 GLU A 128 1 ? 6  
HELX_P HELX_P8  AA8 GLU A 128 ? VAL A 136 ? GLU A 128 VAL A 136 1 ? 9  
HELX_P HELX_P9  AA9 GLU A 138 ? GLY A 148 ? GLU A 138 GLY A 148 1 ? 11 
HELX_P HELX_P10 AB1 SER A 182 ? THR A 188 ? SER A 182 THR A 188 1 ? 7  
HELX_P HELX_P11 AB2 THR A 191 ? GLY A 197 ? THR A 191 GLY A 197 1 ? 7  
HELX_P HELX_P12 AB3 ALA B 27  ? ALA B 43  ? ALA B 27  ALA B 43  1 ? 17 
HELX_P HELX_P13 AB4 GLY B 47  ? GLN B 57  ? GLY B 47  GLN B 57  1 ? 11 
HELX_P HELX_P14 AB5 ASN B 59  ? SER B 66  ? ASN B 59  SER B 66  1 ? 8  
HELX_P HELX_P15 AB6 PRO B 67  ? THR B 83  ? PRO B 67  THR B 83  1 ? 17 
HELX_P HELX_P16 AB7 ASP B 87  ? ASN B 101 ? ASP B 87  ASN B 101 1 ? 15 
HELX_P HELX_P17 AB8 LYS B 112 ? GLY B 126 ? LYS B 112 GLY B 126 1 ? 15 
HELX_P HELX_P18 AB9 TYR B 178 ? GLY B 183 ? TYR B 178 GLY B 183 1 ? 6  
HELX_P HELX_P19 AC1 ALA B 200 ? GLY B 205 ? ALA B 200 GLY B 205 1 ? 6  
HELX_P HELX_P20 AC2 PRO B 206 ? GLY B 208 ? PRO B 206 GLY B 208 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            108 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            113 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       B 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             108 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             113 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.869 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       108 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      113 
_pdbx_modification_feature.modified_residue_label_alt_id      B 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        108 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       113 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
# 
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 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? 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 MET A 93  ? GLU A 97  ? MET A 93  GLU A 97  
AA1 2 ARG A 167 ? LEU A 171 ? ARG A 167 LEU A 171 
AA2 1 VAL A 102 ? VAL A 107 ? VAL A 102 VAL A 107 
AA2 2 GLU A 156 ? ASP A 161 ? GLU A 156 ASP A 161 
AA2 3 SER B 212 ? TRP B 219 ? SER B 212 TRP B 219 
AA2 4 GLU B 191 ? THR B 199 ? GLU B 191 THR B 199 
AA2 5 THR B 166 ? TYR B 176 ? THR B 166 TYR B 176 
AA2 6 SER B 130 ? ARG B 131 ? SER B 130 ARG B 131 
AA3 1 VAL A 102 ? VAL A 107 ? VAL A 102 VAL A 107 
AA3 2 GLU A 156 ? ASP A 161 ? GLU A 156 ASP A 161 
AA3 3 SER B 212 ? TRP B 219 ? SER B 212 TRP B 219 
AA3 4 GLU B 191 ? THR B 199 ? GLU B 191 THR B 199 
AA3 5 THR B 166 ? TYR B 176 ? THR B 166 TYR B 176 
AA3 6 VAL B 144 ? PHE B 147 ? VAL B 144 PHE B 147 
AA3 7 ILE B 223 ? ASP B 227 ? ILE B 223 ASP B 227 
# 
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 MET A 94  ? N MET A 94  O ARG A 167 ? O ARG A 167 
AA2 1 2 N VAL A 105 ? N VAL A 105 O TRP A 160 ? O TRP A 160 
AA2 2 3 N VAL A 159 ? N VAL A 159 O TYR B 215 ? O TYR B 215 
AA2 3 4 O CYS B 218 ? O CYS B 218 N TYR B 194 ? N TYR B 194 
AA2 4 5 O LEU B 193 ? O LEU B 193 N HIS B 173 ? N HIS B 173 
AA2 5 6 O ALA B 175 ? O ALA B 175 N ARG B 131 ? N ARG B 131 
AA3 1 2 N VAL A 105 ? N VAL A 105 O TRP A 160 ? O TRP A 160 
AA3 2 3 N VAL A 159 ? N VAL A 159 O TYR B 215 ? O TYR B 215 
AA3 3 4 O CYS B 218 ? O CYS B 218 N TYR B 194 ? N TYR B 194 
AA3 4 5 O LEU B 193 ? O LEU B 193 N HIS B 173 ? N HIS B 173 
AA3 5 6 O GLY B 167 ? O GLY B 167 N VAL B 145 ? N VAL B 145 
AA3 6 7 N VAL B 144 ? N VAL B 144 O VAL B 226 ? O VAL B 226 
# 
_pdbx_entry_details.entry_id                   9D5U 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 402 ? ? O B HOH 456 ? ? 2.10 
2 1 O  A HOH 468 ? ? O B HOH 428 ? ? 2.13 
3 1 NZ A LYS 202 ? ? O A HOH 401 ? ? 2.13 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C  B ASP 209 ? ? O  B ASP 209 ? ? 1.361 1.229 0.132  0.019 N 
2 1 N  B PRO 210 ? ? CA B PRO 210 ? ? 1.300 1.468 -0.168 0.017 N 
3 1 CA B PRO 210 ? ? CB B PRO 210 ? ? 1.364 1.531 -0.167 0.020 N 
4 1 CB B PRO 210 ? ? CG B PRO 210 ? ? 1.955 1.495 0.460  0.050 N 
5 1 CG B PRO 210 ? ? CD B PRO 210 ? ? 0.675 1.502 -0.827 0.033 N 
6 1 CD B PRO 210 ? ? N  B PRO 210 ? ? 1.582 1.474 0.108  0.014 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA B ASP 209 ? ? C  B ASP 209 ? ? O  B ASP 209 ? ? 104.53 120.10 -15.57  2.10 N 
2 1 C  B ASP 209 ? ? N  B PRO 210 ? ? CD B PRO 210 ? ? 165.78 128.40 37.38   2.10 Y 
3 1 CA B PRO 210 ? ? N  B PRO 210 ? ? CD B PRO 210 ? ? 81.14  111.70 -30.56  1.40 N 
4 1 N  B PRO 210 ? ? CA B PRO 210 ? ? CB B PRO 210 ? ? 94.62  103.30 -8.68   1.20 N 
5 1 CA B PRO 210 ? ? CB B PRO 210 ? ? CG B PRO 210 ? ? 90.96  104.80 -13.84  1.90 N 
6 1 CB B PRO 210 ? ? CG B PRO 210 ? ? CD B PRO 210 ? ? 0.04   106.50 -106.46 3.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 8   ? ? -52.65  176.29  
2  1 CYS A 111 ? ? -152.47 -110.87 
3  1 ALA A 112 ? ? -149.10 21.30   
4  1 ALA A 112 ? ? -149.10 22.28   
5  1 ASN B 2   ? ? -85.05  49.17   
6  1 MET B 46  ? ? 176.00  165.67  
7  1 ARG B 157 ? ? -115.51 61.26   
8  1 ARG B 158 ? ? -115.11 68.99   
9  1 ILE B 177 ? ? -35.27  137.89  
10 1 CYS B 189 ? ? 34.58   64.83   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 403 ? D HOH . 
2 1 B HOH 437 ? E HOH . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'National Science Foundation (NSF, United States)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           CHE-2204024 
_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   1IRE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D5U 
_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]   0.015189 
_atom_sites.fract_transf_matrix[1][2]   0.008769 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017539 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005387 
_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 
H 
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   . THR A 1 2   ? 36.871 -30.484 -3.927  1.00 23.66 ? 2   THR A N   1 
ATOM   2    C CA  . THR A 1 2   ? 37.288 -30.813 -5.284  1.00 24.85 ? 2   THR A CA  1 
ATOM   3    C C   . THR A 1 2   ? 37.456 -32.351 -5.387  1.00 23.65 ? 2   THR A C   1 
ATOM   4    O O   . THR A 1 2   ? 37.434 -33.054 -4.360  1.00 22.22 ? 2   THR A O   1 
ATOM   5    C CB  . THR A 1 2   ? 38.587 -30.040 -5.663  1.00 24.08 ? 2   THR A CB  1 
ATOM   6    O OG1 . THR A 1 2   ? 38.235 -28.709 -6.067  1.00 26.87 ? 2   THR A OG1 1 
ATOM   7    C CG2 . THR A 1 2   ? 39.335 -30.710 -6.819  1.00 22.02 ? 2   THR A CG2 1 
ATOM   8    N N   . GLU A 1 3   ? 37.572 -32.875 -6.612  1.00 23.65 ? 3   GLU A N   1 
ATOM   9    C CA  . GLU A 1 3   ? 37.792 -34.303 -6.790  1.00 20.60 ? 3   GLU A CA  1 
ATOM   10   C C   . GLU A 1 3   ? 39.250 -34.662 -6.509  1.00 19.72 ? 3   GLU A C   1 
ATOM   11   O O   . GLU A 1 3   ? 40.177 -34.027 -7.029  1.00 18.47 ? 3   GLU A O   1 
ATOM   12   C CB  . GLU A 1 3   ? 37.390 -34.752 -8.195  1.00 22.69 ? 3   GLU A CB  1 
ATOM   13   C CG  . GLU A 1 3   ? 37.576 -36.279 -8.415  1.00 23.30 ? 3   GLU A CG  1 
ATOM   14   C CD  . GLU A 1 3   ? 37.247 -36.750 -9.820  1.00 24.05 ? 3   GLU A CD  1 
ATOM   15   O OE1 . GLU A 1 3   ? 36.066 -37.063 -10.097 1.00 28.32 ? 3   GLU A OE1 1 
ATOM   16   O OE2 . GLU A 1 3   ? 38.167 -36.825 -10.656 1.00 22.45 ? 3   GLU A OE2 1 
ATOM   17   N N   . ASN A 1 4   ? 39.442 -35.693 -5.687  1.00 19.45 ? 4   ASN A N   1 
ATOM   18   C CA  . ASN A 1 4   ? 40.753 -36.279 -5.411  1.00 17.92 ? 4   ASN A CA  1 
ATOM   19   C C   . ASN A 1 4   ? 40.630 -37.786 -5.605  1.00 16.03 ? 4   ASN A C   1 
ATOM   20   O O   . ASN A 1 4   ? 40.030 -38.471 -4.778  1.00 16.52 ? 4   ASN A O   1 
ATOM   21   C CB  . ASN A 1 4   ? 41.158 -36.005 -3.973  1.00 17.65 ? 4   ASN A CB  1 
ATOM   22   C CG  . ASN A 1 4   ? 42.509 -36.557 -3.648  1.00 16.43 ? 4   ASN A CG  1 
ATOM   23   O OD1 . ASN A 1 4   ? 43.129 -37.270 -4.471  1.00 15.56 ? 4   ASN A OD1 1 
ATOM   24   N ND2 . ASN A 1 4   ? 42.987 -36.251 -2.434  1.00 16.44 ? 4   ASN A ND2 1 
ATOM   25   N N   . ILE A 1 5   ? 41.212 -38.308 -6.679  1.00 16.83 ? 5   ILE A N   1 
ATOM   26   C CA  . ILE A 1 5   ? 41.088 -39.730 -6.956  1.00 17.11 ? 5   ILE A CA  1 
ATOM   27   C C   . ILE A 1 5   ? 41.741 -40.581 -5.868  1.00 17.52 ? 5   ILE A C   1 
ATOM   28   O O   . ILE A 1 5   ? 41.574 -41.809 -5.849  1.00 15.55 ? 5   ILE A O   1 
ATOM   29   C CB  . ILE A 1 5   ? 41.636 -40.094 -8.366  1.00 18.92 ? 5   ILE A CB  1 
ATOM   30   C CG1 . ILE A 1 5   ? 43.156 -39.866 -8.457  1.00 18.37 ? 5   ILE A CG1 1 
ATOM   31   C CG2 . ILE A 1 5   ? 40.883 -39.321 -9.468  1.00 17.05 ? 5   ILE A CG2 1 
ATOM   32   C CD1 . ILE A 1 5   ? 43.827 -40.696 -9.525  1.00 16.07 ? 5   ILE A CD1 1 
ATOM   33   N N   . LEU A 1 6   ? 42.490 -39.951 -4.959  1.00 17.21 ? 6   LEU A N   1 
ATOM   34   C CA  . LEU A 1 6   ? 43.184 -40.655 -3.888  1.00 16.87 ? 6   LEU A CA  1 
ATOM   35   C C   . LEU A 1 6   ? 42.336 -40.846 -2.632  1.00 15.00 ? 6   LEU A C   1 
ATOM   36   O O   . LEU A 1 6   ? 42.744 -41.610 -1.745  1.00 15.81 ? 6   LEU A O   1 
ATOM   37   C CB  . LEU A 1 6   ? 44.491 -39.913 -3.508  1.00 14.86 ? 6   LEU A CB  1 
ATOM   38   C CG  . LEU A 1 6   ? 45.438 -39.381 -4.599  1.00 15.03 ? 6   LEU A CG  1 
ATOM   39   C CD1 . LEU A 1 6   ? 46.623 -38.606 -3.983  1.00 15.36 ? 6   LEU A CD1 1 
ATOM   40   C CD2 . LEU A 1 6   ? 45.955 -40.522 -5.507  1.00 16.57 ? 6   LEU A CD2 1 
ATOM   41   N N   . ARG A 1 7   ? 41.172 -40.185 -2.545  1.00 16.15 ? 7   ARG A N   1 
ATOM   42   C CA  . ARG A 1 7   ? 40.457 -39.952 -1.290  1.00 17.60 ? 7   ARG A CA  1 
ATOM   43   C C   . ARG A 1 7   ? 39.330 -40.971 -1.095  1.00 17.76 ? 7   ARG A C   1 
ATOM   44   O O   . ARG A 1 7   ? 38.432 -41.068 -1.935  1.00 20.38 ? 7   ARG A O   1 
ATOM   45   C CB  . ARG A 1 7   ? 39.892 -38.527 -1.297  1.00 16.90 ? 7   ARG A CB  1 
ATOM   46   C CG  . ARG A 1 7   ? 39.475 -37.995 0.061   1.00 19.22 ? 7   ARG A CG  1 
ATOM   47   C CD  . ARG A 1 7   ? 39.084 -36.501 -0.001  1.00 19.92 ? 7   ARG A CD  1 
ATOM   48   N NE  . ARG A 1 7   ? 37.867 -36.269 -0.776  1.00 21.22 ? 7   ARG A NE  1 
ATOM   49   C CZ  . ARG A 1 7   ? 37.785 -35.427 -1.801  1.00 21.24 ? 7   ARG A CZ  1 
ATOM   50   N NH1 . ARG A 1 7   ? 38.812 -34.665 -2.142  1.00 19.80 ? 7   ARG A NH1 1 
ATOM   51   N NH2 . ARG A 1 7   ? 36.648 -35.357 -2.505  1.00 21.80 ? 7   ARG A NH2 1 
ATOM   52   N N   . LYS A 1 8   ? 39.364 -41.700 0.027   1.00 17.18 ? 8   LYS A N   1 
ATOM   53   C CA  . LYS A 1 8   ? 38.302 -42.631 0.431   1.00 18.83 ? 8   LYS A CA  1 
ATOM   54   C C   . LYS A 1 8   ? 36.930 -41.950 0.431   1.00 18.68 ? 8   LYS A C   1 
ATOM   55   O O   . LYS A 1 8   ? 36.817 -40.727 0.224   1.00 16.18 ? 8   LYS A O   1 
ATOM   56   C CB  . LYS A 1 8   ? 38.541 -43.115 1.865   1.00 17.96 ? 8   LYS A CB  1 
ATOM   57   C CG  . LYS A 1 8   ? 39.822 -43.885 2.094   1.00 17.63 ? 8   LYS A CG  1 
ATOM   58   C CD  . LYS A 1 8   ? 40.078 -43.939 3.592   1.00 18.80 ? 8   LYS A CD  1 
ATOM   59   C CE  . LYS A 1 8   ? 40.957 -45.102 4.012   1.00 21.12 ? 8   LYS A CE  1 
ATOM   60   N NZ  . LYS A 1 8   ? 40.598 -45.623 5.366   1.00 22.81 ? 8   LYS A NZ  1 
ATOM   61   N N   . SER A 1 9   ? 35.879 -42.728 0.710   1.00 17.99 ? 9   SER A N   1 
ATOM   62   C CA  . SER A 1 9   ? 34.538 -42.151 0.799   1.00 20.57 ? 9   SER A CA  1 
ATOM   63   C C   . SER A 1 9   ? 34.391 -41.399 2.114   1.00 17.27 ? 9   SER A C   1 
ATOM   64   O O   . SER A 1 9   ? 35.070 -41.700 3.097   1.00 16.33 ? 9   SER A O   1 
ATOM   65   C CB  . SER A 1 9   ? 33.451 -43.232 0.715   1.00 17.90 ? 9   SER A CB  1 
ATOM   66   O OG  . SER A 1 9   ? 33.459 -44.054 1.852   1.00 18.60 ? 9   SER A OG  1 
ATOM   67   N N   . ASP A 1 10  ? 33.508 -40.397 2.112   1.00 17.68 ? 10  ASP A N   1 
ATOM   68   C CA  . ASP A 1 10  ? 33.192 -39.683 3.348   1.00 21.09 ? 10  ASP A CA  1 
ATOM   69   C C   . ASP A 1 10  ? 32.748 -40.662 4.437   1.00 20.05 ? 10  ASP A C   1 
ATOM   70   O O   . ASP A 1 10  ? 33.026 -40.460 5.626   1.00 16.50 ? 10  ASP A O   1 
ATOM   71   C CB  . ASP A 1 10  ? 32.083 -38.638 3.101   1.00 23.11 ? 10  ASP A CB  1 
ATOM   72   C CG  . ASP A 1 10  ? 32.560 -37.428 2.260   1.00 29.33 ? 10  ASP A CG  1 
ATOM   73   O OD1 . ASP A 1 10  ? 33.778 -37.123 2.250   1.00 29.07 ? 10  ASP A OD1 1 
ATOM   74   O OD2 . ASP A 1 10  ? 31.694 -36.749 1.633   1.00 30.92 ? 10  ASP A OD2 1 
ATOM   75   N N   . GLU A 1 11  ? 32.063 -41.741 4.038   1.00 23.21 ? 11  GLU A N   1 
ATOM   76   C CA  . GLU A 1 11  ? 31.665 -42.774 4.984   1.00 21.44 ? 11  GLU A CA  1 
ATOM   77   C C   . GLU A 1 11  ? 32.881 -43.483 5.561   1.00 18.23 ? 11  GLU A C   1 
ATOM   78   O O   . GLU A 1 11  ? 33.014 -43.616 6.778   1.00 19.23 ? 11  GLU A O   1 
ATOM   79   C CB  . GLU A 1 11  ? 30.749 -43.782 4.284   1.00 23.74 ? 11  GLU A CB  1 
ATOM   80   C CG  . GLU A 1 11  ? 29.309 -43.295 4.070   1.00 27.55 ? 11  GLU A CG  1 
ATOM   81   C CD  . GLU A 1 11  ? 28.909 -43.299 2.590   1.00 36.45 ? 11  GLU A CD  1 
ATOM   82   O OE1 . GLU A 1 11  ? 27.729 -42.963 2.287   1.00 37.57 ? 11  GLU A OE1 1 
ATOM   83   O OE2 . GLU A 1 11  ? 29.783 -43.620 1.730   1.00 35.93 ? 11  GLU A OE2 1 
ATOM   84   N N   . GLU A 1 12  ? 33.779 -43.952 4.705   1.00 18.65 ? 12  GLU A N   1 
ATOM   85   C CA  . GLU A 1 12  ? 34.953 -44.653 5.210   1.00 19.19 ? 12  GLU A CA  1 
ATOM   86   C C   . GLU A 1 12  ? 35.807 -43.742 6.087   1.00 18.87 ? 12  GLU A C   1 
ATOM   87   O O   . GLU A 1 12  ? 36.390 -44.207 7.078   1.00 18.01 ? 12  GLU A O   1 
ATOM   88   C CB  . GLU A 1 12  ? 35.755 -45.242 4.040   1.00 20.88 ? 12  GLU A CB  1 
ATOM   89   C CG  . GLU A 1 12  ? 35.197 -46.602 3.507   1.00 26.99 ? 12  GLU A CG  1 
ATOM   90   C CD  . GLU A 1 12  ? 34.781 -47.598 4.635   1.00 31.16 ? 12  GLU A CD  1 
ATOM   91   O OE1 . GLU A 1 12  ? 35.687 -48.061 5.383   1.00 31.31 ? 12  GLU A OE1 1 
ATOM   92   O OE2 . GLU A 1 12  ? 33.557 -47.920 4.773   1.00 27.44 ? 12  GLU A OE2 1 
ATOM   93   N N   . ILE A 1 13  ? 35.864 -42.439 5.758   1.00 17.83 ? 13  ILE A N   1 
ATOM   94   C CA  . ILE A 1 13  ? 36.636 -41.484 6.551   1.00 15.55 ? 13  ILE A CA  1 
ATOM   95   C C   . ILE A 1 13  ? 36.044 -41.339 7.946   1.00 15.61 ? 13  ILE A C   1 
ATOM   96   O O   . ILE A 1 13  ? 36.759 -41.401 8.960   1.00 14.32 ? 13  ILE A O   1 
ATOM   97   C CB  . ILE A 1 13  ? 36.729 -40.126 5.834   1.00 14.33 ? 13  ILE A CB  1 
ATOM   98   C CG1 . ILE A 1 13  ? 37.616 -40.221 4.603   1.00 16.12 ? 13  ILE A CG1 1 
ATOM   99   C CG2 . ILE A 1 13  ? 37.331 -39.094 6.734   1.00 16.47 ? 13  ILE A CG2 1 
ATOM   100  C CD1 . ILE A 1 13  ? 37.577 -38.989 3.753   1.00 17.66 ? 13  ILE A CD1 1 
ATOM   101  N N   . GLN A 1 14  ? 34.718 -41.140 8.016   1.00 18.08 ? 14  GLN A N   1 
ATOM   102  C CA  . GLN A 1 14  ? 34.064 -40.876 9.297   1.00 17.27 ? 14  GLN A CA  1 
ATOM   103  C C   . GLN A 1 14  ? 34.171 -42.079 10.216  1.00 15.60 ? 14  GLN A C   1 
ATOM   104  O O   . GLN A 1 14  ? 34.346 -41.930 11.438  1.00 14.31 ? 14  GLN A O   1 
ATOM   105  C CB  . GLN A 1 14  ? 32.593 -40.546 9.069   1.00 16.92 ? 14  GLN A CB  1 
ATOM   106  C CG  . GLN A 1 14  ? 32.368 -39.194 8.428   1.00 18.67 ? 14  GLN A CG  1 
ATOM   107  C CD  . GLN A 1 14  ? 32.818 -38.065 9.324   1.00 20.48 ? 14  GLN A CD  1 
ATOM   108  O OE1 . GLN A 1 14  ? 32.481 -38.041 10.524  1.00 21.57 ? 14  GLN A OE1 1 
ATOM   109  N NE2 . GLN A 1 14  ? 33.573 -37.117 8.758   1.00 18.49 ? 14  GLN A NE2 1 
ATOM   110  N N   . LYS A 1 15  ? 34.073 -43.283 9.634   1.00 16.63 ? 15  LYS A N   1 
ATOM   111  C CA  . LYS A 1 15  ? 34.117 -44.501 10.435  1.00 17.88 ? 15  LYS A CA  1 
ATOM   112  C C   . LYS A 1 15  ? 35.508 -44.701 11.048  1.00 15.35 ? 15  LYS A C   1 
ATOM   113  O O   . LYS A 1 15  ? 35.634 -45.083 12.220  1.00 15.63 ? 15  LYS A O   1 
ATOM   114  C CB  . LYS A 1 15  ? 33.687 -45.662 9.539   1.00 19.38 ? 15  LYS A CB  1 
ATOM   115  C CG  . LYS A 1 15  ? 33.730 -47.061 10.134  1.00 20.87 ? 15  LYS A CG  1 
ATOM   116  C CD  . LYS A 1 15  ? 35.085 -47.654 10.070  1.00 24.68 ? 15  LYS A CD  1 
ATOM   117  C CE  . LYS A 1 15  ? 35.282 -48.674 11.148  1.00 25.82 ? 15  LYS A CE  1 
ATOM   118  N NZ  . LYS A 1 15  ? 36.298 -49.658 10.635  1.00 29.50 ? 15  LYS A NZ  1 
ATOM   119  N N   . GLU A 1 16  ? 36.560 -44.381 10.277  1.00 16.93 ? 16  GLU A N   1 
ATOM   120  C CA  . GLU A 1 16  ? 37.930 -44.468 10.775  1.00 15.63 ? 16  GLU A CA  1 
ATOM   121  C C   . GLU A 1 16  ? 38.189 -43.425 11.859  1.00 14.35 ? 16  GLU A C   1 
ATOM   122  O O   . GLU A 1 16  ? 38.763 -43.725 12.915  1.00 12.82 ? 16  GLU A O   1 
ATOM   123  C CB  . GLU A 1 16  ? 38.898 -44.295 9.603   1.00 15.55 ? 16  GLU A CB  1 
ATOM   124  C CG  . GLU A 1 16  ? 40.364 -44.396 10.009  1.00 16.68 ? 16  GLU A CG  1 
ATOM   125  C CD  . GLU A 1 16  ? 40.719 -45.728 10.629  1.00 17.23 ? 16  GLU A CD  1 
ATOM   126  O OE1 . GLU A 1 16  ? 40.049 -46.727 10.318  1.00 19.10 ? 16  GLU A OE1 1 
ATOM   127  O OE2 . GLU A 1 16  ? 41.670 -45.777 11.427  1.00 16.94 ? 16  GLU A OE2 1 
ATOM   128  N N   . ILE A 1 17  ? 37.803 -42.176 11.598  1.00 15.20 ? 17  ILE A N   1 
ATOM   129  C CA  . ILE A 1 17  ? 37.949 -41.128 12.607  1.00 14.21 ? 17  ILE A CA  1 
ATOM   130  C C   . ILE A 1 17  ? 37.250 -41.538 13.896  1.00 12.93 ? 17  ILE A C   1 
ATOM   131  O O   . ILE A 1 17  ? 37.800 -41.387 14.986  1.00 13.97 ? 17  ILE A O   1 
ATOM   132  C CB  . ILE A 1 17  ? 37.422 -39.789 12.049  1.00 13.66 ? 17  ILE A CB  1 
ATOM   133  C CG1 . ILE A 1 17  ? 38.320 -39.289 10.912  1.00 14.01 ? 17  ILE A CG1 1 
ATOM   134  C CG2 . ILE A 1 17  ? 37.300 -38.750 13.151  1.00 14.94 ? 17  ILE A CG2 1 
ATOM   135  C CD1 . ILE A 1 17  ? 37.777 -38.045 10.240  1.00 14.47 ? 17  ILE A CD1 1 
ATOM   136  N N   . THR A 1 18  ? 36.038 -42.102 13.792  1.00 12.98 ? 18  THR A N   1 
ATOM   137  C CA  . THR A 1 18  ? 35.279 -42.447 14.991  1.00 12.73 ? 18  THR A CA  1 
ATOM   138  C C   . THR A 1 18  ? 36.037 -43.442 15.875  1.00 12.46 ? 18  THR A C   1 
ATOM   139  O O   . THR A 1 18  ? 36.182 -43.234 17.088  1.00 12.39 ? 18  THR A O   1 
ATOM   140  C CB  . THR A 1 18  ? 33.922 -43.009 14.577  1.00 14.97 ? 18  THR A CB  1 
ATOM   141  O OG1 . THR A 1 18  ? 33.176 -41.998 13.893  1.00 14.43 ? 18  THR A OG1 1 
ATOM   142  C CG2 . THR A 1 18  ? 33.148 -43.499 15.790  1.00 13.22 ? 18  THR A CG2 1 
ATOM   143  N N   . ALA A 1 19  ? 36.511 -44.549 15.278  1.00 15.28 ? 19  ALA A N   1 
ATOM   144  C CA  . ALA A 1 19  ? 37.277 -45.553 16.023  1.00 13.81 ? 19  ALA A CA  1 
ATOM   145  C C   . ALA A 1 19  ? 38.503 -44.932 16.679  1.00 12.36 ? 19  ALA A C   1 
ATOM   146  O O   . ALA A 1 19  ? 38.812 -45.228 17.836  1.00 12.38 ? 19  ALA A O   1 
ATOM   147  C CB  . ALA A 1 19  ? 37.706 -46.694 15.092  1.00 12.71 ? 19  ALA A CB  1 
ATOM   148  N N   . ARG A 1 20  ? 39.201 -44.051 15.952  1.00 14.17 ? 20  ARG A N   1 
ATOM   149  C CA  . ARG A 1 20  ? 40.399 -43.403 16.481  1.00 12.99 ? 20  ARG A CA  1 
ATOM   150  C C   . ARG A 1 20  ? 40.075 -42.483 17.661  1.00 12.10 ? 20  ARG A C   1 
ATOM   151  O O   . ARG A 1 20  ? 40.774 -42.501 18.680  1.00 11.98 ? 20  ARG A O   1 
ATOM   152  C CB  . ARG A 1 20  ? 41.117 -42.642 15.366  1.00 13.22 ? 20  ARG A CB  1 
ATOM   153  C CG  . ARG A 1 20  ? 41.622 -43.557 14.311  1.00 13.39 ? 20  ARG A CG  1 
ATOM   154  C CD  . ARG A 1 20  ? 42.730 -42.926 13.566  1.00 15.82 ? 20  ARG A CD  1 
ATOM   155  N NE  . ARG A 1 20  ? 43.316 -43.832 12.584  1.00 18.06 ? 20  ARG A NE  1 
ATOM   156  C CZ  . ARG A 1 20  ? 44.620 -43.945 12.366  1.00 20.86 ? 20  ARG A CZ  1 
ATOM   157  N NH1 . ARG A 1 20  ? 45.495 -43.283 13.102  1.00 23.02 ? 20  ARG A NH1 1 
ATOM   158  N NH2 . ARG A 1 20  ? 45.059 -44.735 11.381  1.00 20.62 ? 20  ARG A NH2 1 
ATOM   159  N N   . VAL A 1 21  ? 39.038 -41.649 17.528  1.00 12.78 ? 21  VAL A N   1 
ATOM   160  C CA  . VAL A 1 21  ? 38.647 -40.761 18.628  1.00 14.35 ? 21  VAL A CA  1 
ATOM   161  C C   . VAL A 1 21  ? 38.211 -41.560 19.860  1.00 13.85 ? 21  VAL A C   1 
ATOM   162  O O   . VAL A 1 21  ? 38.575 -41.232 21.006  1.00 12.39 ? 21  VAL A O   1 
ATOM   163  C CB  . VAL A 1 21  ? 37.564 -39.766 18.157  1.00 14.28 ? 21  VAL A CB  1 
ATOM   164  C CG1 . VAL A 1 21  ? 37.005 -39.009 19.356  1.00 14.25 ? 21  VAL A CG1 1 
ATOM   165  C CG2 . VAL A 1 21  ? 38.146 -38.801 17.118  1.00 14.47 ? 21  VAL A CG2 1 
ATOM   166  N N   . LYS A 1 22  ? 37.409 -42.622 19.644  1.00 14.98 ? 22  LYS A N   1 
ATOM   167  C CA  . LYS A 1 22  ? 36.968 -43.438 20.771  1.00 14.28 ? 22  LYS A CA  1 
ATOM   168  C C   . LYS A 1 22  ? 38.152 -44.091 21.452  1.00 13.37 ? 22  LYS A C   1 
ATOM   169  O O   . LYS A 1 22  ? 38.203 -44.153 22.679  1.00 15.86 ? 22  LYS A O   1 
ATOM   170  C CB  . LYS A 1 22  ? 35.949 -44.490 20.332  1.00 15.26 ? 22  LYS A CB  1 
ATOM   171  C CG  . LYS A 1 22  ? 35.233 -45.140 21.512  1.00 16.10 ? 22  LYS A CG  1 
ATOM   172  C CD  . LYS A 1 22  ? 33.963 -45.879 21.092  1.00 16.78 ? 22  LYS A CD  1 
ATOM   173  C CE  . LYS A 1 22  ? 33.198 -46.393 22.298  1.00 15.34 ? 22  LYS A CE  1 
ATOM   174  N NZ  . LYS A 1 22  ? 31.954 -47.046 21.858  1.00 14.89 ? 22  LYS A NZ  1 
ATOM   175  N N   . ALA A 1 23  ? 39.122 -44.584 20.673  1.00 12.64 ? 23  ALA A N   1 
ATOM   176  C CA  . ALA A 1 23  ? 40.298 -45.182 21.291  1.00 14.11 ? 23  ALA A CA  1 
ATOM   177  C C   . ALA A 1 23  ? 41.075 -44.147 22.094  1.00 14.35 ? 23  ALA A C   1 
ATOM   178  O O   . ALA A 1 23  ? 41.480 -44.414 23.236  1.00 14.84 ? 23  ALA A O   1 
ATOM   179  C CB  . ALA A 1 23  ? 41.182 -45.831 20.234  1.00 15.03 ? 23  ALA A CB  1 
ATOM   180  N N   . LEU A 1 24  ? 41.309 -42.955 21.507  1.00 14.12 ? 24  LEU A N   1 
ATOM   181  C CA  . LEU A 1 24  ? 42.005 -41.910 22.249  1.00 11.87 ? 24  LEU A CA  1 
ATOM   182  C C   . LEU A 1 24  ? 41.194 -41.480 23.462  1.00 13.56 ? 24  LEU A C   1 
ATOM   183  O O   . LEU A 1 24  ? 41.730 -41.335 24.566  1.00 12.92 ? 24  LEU A O   1 
ATOM   184  C CB  . LEU A 1 24  ? 42.349 -40.738 21.341  1.00 11.46 ? 24  LEU A CB  1 
ATOM   185  C CG  . LEU A 1 24  ? 43.068 -39.553 22.017  1.00 13.29 ? 24  LEU A CG  1 
ATOM   186  C CD1 . LEU A 1 24  ? 44.381 -39.998 22.667  1.00 13.43 ? 24  LEU A CD1 1 
ATOM   187  C CD2 . LEU A 1 24  ? 43.317 -38.406 21.013  1.00 12.64 ? 24  LEU A CD2 1 
ATOM   188  N N   . GLU A 1 25  ? 39.880 -41.338 23.294  1.00 13.53 ? 25  GLU A N   1 
ATOM   189  C CA  . GLU A 1 25  ? 39.017 -40.981 24.418  1.00 14.12 ? 25  GLU A CA  1 
ATOM   190  C C   . GLU A 1 25  ? 39.141 -41.971 25.584  1.00 14.16 ? 25  GLU A C   1 
ATOM   191  O O   . GLU A 1 25  ? 39.206 -41.566 26.754  1.00 12.78 ? 25  GLU A O   1 
ATOM   192  C CB  . GLU A 1 25  ? 37.570 -40.916 23.917  1.00 13.24 ? 25  GLU A CB  1 
ATOM   193  C CG  . GLU A 1 25  ? 36.603 -40.500 24.966  1.00 15.61 ? 25  GLU A CG  1 
ATOM   194  C CD  . GLU A 1 25  ? 35.205 -40.541 24.467  1.00 13.62 ? 25  GLU A CD  1 
ATOM   195  O OE1 . GLU A 1 25  ? 35.018 -40.992 23.323  1.00 14.30 ? 25  GLU A OE1 1 
ATOM   196  O OE2 . GLU A 1 25  ? 34.313 -40.122 25.234  1.00 16.87 ? 25  GLU A OE2 1 
ATOM   197  N N   . SER A 1 26  ? 39.142 -43.277 25.281  1.00 13.73 ? 26  SER A N   1 
ATOM   198  C CA  . SER A 1 26  ? 39.265 -44.285 26.328  1.00 14.45 ? 26  SER A CA  1 
ATOM   199  C C   . SER A 1 26  ? 40.568 -44.133 27.122  1.00 14.71 ? 26  SER A C   1 
ATOM   200  O O   . SER A 1 26  ? 40.585 -44.344 28.343  1.00 15.47 ? 26  SER A O   1 
ATOM   201  C CB  . SER A 1 26  ? 39.108 -45.689 25.725  1.00 14.48 ? 26  SER A CB  1 
ATOM   202  O OG  . SER A 1 26  ? 40.205 -46.060 24.897  1.00 15.38 ? 26  SER A OG  1 
ATOM   203  N N   . MET A 1 27  ? 41.665 -43.741 26.452  1.00 14.87 ? 27  MET A N   1 
ATOM   204  C CA  . MET A 1 27  ? 42.955 -43.624 27.139  1.00 14.47 ? 27  MET A CA  1 
ATOM   205  C C   . MET A 1 27  ? 42.979 -42.414 28.066  1.00 14.05 ? 27  MET A C   1 
ATOM   206  O O   . MET A 1 27  ? 43.436 -42.506 29.215  1.00 15.15 ? 27  MET A O   1 
ATOM   207  C CB  . MET A 1 27  ? 44.103 -43.555 26.116  1.00 15.40 ? 27  MET A CB  1 
ATOM   208  C CG  . MET A 1 27  ? 44.279 -44.857 25.325  1.00 17.82 ? 27  MET A CG  1 
ATOM   209  S SD  . MET A 1 27  ? 45.663 -44.928 24.167  1.00 20.20 ? 27  MET A SD  1 
ATOM   210  C CE  . MET A 1 27  ? 47.042 -45.039 25.296  1.00 18.77 ? 27  MET A CE  1 
ATOM   211  N N   . LEU A 1 28  ? 42.453 -41.277 27.592  1.00 15.12 ? 28  LEU A N   1 
ATOM   212  C CA  . LEU A 1 28  ? 42.357 -40.079 28.423  1.00 13.70 ? 28  LEU A CA  1 
ATOM   213  C C   . LEU A 1 28  ? 41.388 -40.294 29.585  1.00 13.28 ? 28  LEU A C   1 
ATOM   214  O O   . LEU A 1 28  ? 41.618 -39.767 30.676  1.00 12.73 ? 28  LEU A O   1 
ATOM   215  C CB  . LEU A 1 28  ? 41.946 -38.895 27.541  1.00 15.31 ? 28  LEU A CB  1 
ATOM   216  C CG  . LEU A 1 28  ? 42.886 -38.593 26.338  1.00 13.58 ? 28  LEU A CG  1 
ATOM   217  C CD1 . LEU A 1 28  ? 42.519 -37.291 25.623  1.00 14.40 ? 28  LEU A CD1 1 
ATOM   218  C CD2 . LEU A 1 28  ? 44.322 -38.582 26.788  1.00 13.94 ? 28  LEU A CD2 1 
ATOM   219  N N   . ILE A 1 29  ? 40.325 -41.093 29.381  1.00 13.81 ? 29  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29  ? 39.427 -41.418 30.490  1.00 14.80 ? 29  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29  ? 40.177 -42.180 31.574  1.00 13.52 ? 29  ILE A C   1 
ATOM   222  O O   . ILE A 1 29  ? 40.055 -41.890 32.767  1.00 13.57 ? 29  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29  ? 38.201 -42.217 30.009  1.00 14.96 ? 29  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29  ? 37.199 -41.321 29.258  1.00 16.68 ? 29  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29  ? 37.497 -42.797 31.222  1.00 14.03 ? 29  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29  ? 35.988 -42.055 28.667  1.00 14.94 ? 29  ILE A CD1 1 
ATOM   227  N N   . GLU A 1 30  ? 40.946 -43.191 31.172  1.00 15.06 ? 30  GLU A N   1 
ATOM   228  C CA  . GLU A 1 30  ? 41.668 -43.992 32.144  1.00 14.73 ? 30  GLU A CA  1 
ATOM   229  C C   . GLU A 1 30  ? 42.743 -43.187 32.842  1.00 12.28 ? 30  GLU A C   1 
ATOM   230  O O   . GLU A 1 30  ? 43.190 -43.579 33.914  1.00 13.07 ? 30  GLU A O   1 
ATOM   231  C CB  . GLU A 1 30  ? 42.306 -45.182 31.450  1.00 17.08 ? 30  GLU A CB  1 
ATOM   232  C CG  . GLU A 1 30  ? 41.331 -46.252 31.031  1.00 17.31 ? 30  GLU A CG  1 
ATOM   233  C CD  . GLU A 1 30  ? 42.039 -47.428 30.378  1.00 22.78 ? 30  GLU A CD  1 
ATOM   234  O OE1 . GLU A 1 30  ? 43.249 -47.307 30.022  1.00 22.34 ? 30  GLU A OE1 1 
ATOM   235  O OE2 . GLU A 1 30  ? 41.379 -48.476 30.217  1.00 25.18 ? 30  GLU A OE2 1 
ATOM   236  N N   . GLN A 1 31  ? 43.170 -42.076 32.262  1.00 14.18 ? 31  GLN A N   1 
ATOM   237  C CA  . GLN A 1 31  ? 44.135 -41.218 32.935  1.00 15.88 ? 31  GLN A CA  1 
ATOM   238  C C   . GLN A 1 31  ? 43.500 -40.324 33.990  1.00 15.78 ? 31  GLN A C   1 
ATOM   239  O O   . GLN A 1 31  ? 44.226 -39.733 34.797  1.00 17.68 ? 31  GLN A O   1 
ATOM   240  C CB  . GLN A 1 31  ? 44.840 -40.348 31.907  1.00 17.22 ? 31  GLN A CB  1 
ATOM   241  C CG  . GLN A 1 31  ? 45.795 -41.104 31.009  1.00 17.54 ? 31  GLN A CG  1 
ATOM   242  C CD  . GLN A 1 31  ? 46.418 -40.196 29.960  1.00 20.07 ? 31  GLN A CD  1 
ATOM   243  O OE1 . GLN A 1 31  ? 46.573 -38.983 30.193  1.00 20.84 ? 31  GLN A OE1 1 
ATOM   244  N NE2 . GLN A 1 31  ? 46.755 -40.764 28.789  1.00 18.02 ? 31  GLN A NE2 1 
ATOM   245  N N   . GLY A 1 32  ? 42.172 -40.213 34.012  1.00 16.00 ? 32  GLY A N   1 
ATOM   246  C CA  . GLY A 1 32  ? 41.483 -39.375 34.976  1.00 16.48 ? 32  GLY A CA  1 
ATOM   247  C C   . GLY A 1 32  ? 41.279 -37.928 34.547  1.00 17.53 ? 32  GLY A C   1 
ATOM   248  O O   . GLY A 1 32  ? 40.711 -37.142 35.322  1.00 17.46 ? 32  GLY A O   1 
ATOM   249  N N   . ILE A 1 33  ? 41.704 -37.560 33.331  1.00 16.10 ? 33  ILE A N   1 
ATOM   250  C CA  . ILE A 1 33  ? 41.703 -36.167 32.883  1.00 15.52 ? 33  ILE A CA  1 
ATOM   251  C C   . ILE A 1 33  ? 40.460 -35.804 32.081  1.00 15.41 ? 33  ILE A C   1 
ATOM   252  O O   . ILE A 1 33  ? 40.272 -34.621 31.749  1.00 17.10 ? 33  ILE A O   1 
ATOM   253  C CB  . ILE A 1 33  ? 42.968 -35.840 32.050  1.00 14.91 ? 33  ILE A CB  1 
ATOM   254  C CG1 . ILE A 1 33  ? 42.900 -36.538 30.679  1.00 14.42 ? 33  ILE A CG1 1 
ATOM   255  C CG2 . ILE A 1 33  ? 44.247 -36.225 32.841  1.00 14.97 ? 33  ILE A CG2 1 
ATOM   256  C CD1 . ILE A 1 33  ? 43.851 -36.034 29.649  1.00 15.22 ? 33  ILE A CD1 1 
ATOM   257  N N   . LEU A 1 34  ? 39.620 -36.773 31.741  1.00 14.87 ? 34  LEU A N   1 
ATOM   258  C CA  . LEU A 1 34  ? 38.493 -36.542 30.864  1.00 14.86 ? 34  LEU A CA  1 
ATOM   259  C C   . LEU A 1 34  ? 37.322 -37.363 31.363  1.00 16.82 ? 34  LEU A C   1 
ATOM   260  O O   . LEU A 1 34  ? 37.494 -38.528 31.747  1.00 15.95 ? 34  LEU A O   1 
ATOM   261  C CB  . LEU A 1 34  ? 38.821 -36.979 29.425  1.00 16.72 ? 34  LEU A CB  1 
ATOM   262  C CG  . LEU A 1 34  ? 37.752 -36.768 28.348  1.00 15.73 ? 34  LEU A CG  1 
ATOM   263  C CD1 . LEU A 1 34  ? 37.521 -35.289 28.062  1.00 18.25 ? 34  LEU A CD1 1 
ATOM   264  C CD2 . LEU A 1 34  ? 38.136 -37.492 27.091  1.00 15.36 ? 34  LEU A CD2 1 
ATOM   265  N N   . THR A 1 35  ? 36.131 -36.758 31.336  1.00 15.33 ? 35  THR A N   1 
ATOM   266  C CA  . THR A 1 35  ? 34.914 -37.447 31.740  1.00 14.58 ? 35  THR A CA  1 
ATOM   267  C C   . THR A 1 35  ? 33.820 -37.161 30.715  1.00 15.29 ? 35  THR A C   1 
ATOM   268  O O   . THR A 1 35  ? 33.884 -36.184 29.969  1.00 13.94 ? 35  THR A O   1 
ATOM   269  C CB  . THR A 1 35  ? 34.443 -36.995 33.144  1.00 15.97 ? 35  THR A CB  1 
ATOM   270  O OG1 . THR A 1 35  ? 34.070 -35.609 33.094  1.00 14.68 ? 35  THR A OG1 1 
ATOM   271  C CG2 . THR A 1 35  ? 35.554 -37.179 34.167  1.00 14.20 ? 35  THR A CG2 1 
ATOM   272  N N   . THR A 1 36  ? 32.811 -38.037 30.695  1.00 13.37 ? 36  THR A N   1 
ATOM   273  C CA  . THR A 1 36  ? 31.594 -37.795 29.920  1.00 14.74 ? 36  THR A CA  1 
ATOM   274  C C   . THR A 1 36  ? 30.922 -36.450 30.267  1.00 13.73 ? 36  THR A C   1 
ATOM   275  O O   . THR A 1 36  ? 30.529 -35.698 29.371  1.00 16.13 ? 36  THR A O   1 
ATOM   276  C CB  . THR A 1 36  ? 30.629 -38.993 30.078  1.00 14.07 ? 36  THR A CB  1 
ATOM   277  O OG1 . THR A 1 36  ? 30.420 -39.307 31.461  1.00 13.87 ? 36  THR A OG1 1 
ATOM   278  C CG2 . THR A 1 36  ? 31.212 -40.221 29.406  1.00 15.67 ? 36  THR A CG2 1 
ATOM   279  N N   . SER A 1 37  ? 30.745 -36.141 31.554  1.00 14.25 ? 37  SER A N   1 
ATOM   280  C CA  . SER A 1 37  ? 30.104 -34.878 31.910  1.00 14.25 ? 37  SER A CA  1 
ATOM   281  C C   . SER A 1 37  ? 30.932 -33.694 31.419  1.00 16.90 ? 37  SER A C   1 
ATOM   282  O O   . SER A 1 37  ? 30.380 -32.674 30.991  1.00 16.49 ? 37  SER A O   1 
ATOM   283  C CB  . SER A 1 37  ? 29.876 -34.784 33.420  1.00 14.24 ? 37  SER A CB  1 
ATOM   284  O OG  . SER A 1 37  ? 31.088 -34.861 34.178  1.00 14.27 ? 37  SER A OG  1 
ATOM   285  N N   . MET A 1 38  ? 32.263 -33.813 31.470  1.00 15.01 ? 38  MET A N   1 
ATOM   286  C CA  . MET A 1 38  ? 33.126 -32.770 30.921  1.00 15.24 ? 38  MET A CA  1 
ATOM   287  C C   . MET A 1 38  ? 32.910 -32.569 29.415  1.00 16.87 ? 38  MET A C   1 
ATOM   288  O O   . MET A 1 38  ? 33.008 -31.440 28.911  1.00 16.96 ? 38  MET A O   1 
ATOM   289  C CB  . MET A 1 38  ? 34.573 -33.130 31.236  1.00 17.21 ? 38  MET A CB  1 
ATOM   290  C CG  . MET A 1 38  ? 35.505 -31.946 31.388  1.00 21.28 ? 38  MET A CG  1 
ATOM   291  S SD  . MET A 1 38  ? 37.208 -32.505 31.213  1.00 18.30 ? 38  MET A SD  1 
ATOM   292  C CE  . MET A 1 38  ? 38.045 -30.950 30.958  1.00 21.67 ? 38  MET A CE  1 
ATOM   293  N N   . ILE A 1 39  ? 32.600 -33.638 28.674  1.00 14.71 ? 39  ILE A N   1 
ATOM   294  C CA  . ILE A 1 39  ? 32.341 -33.510 27.237  1.00 16.12 ? 39  ILE A CA  1 
ATOM   295  C C   . ILE A 1 39  ? 30.971 -32.882 26.976  1.00 16.36 ? 39  ILE A C   1 
ATOM   296  O O   . ILE A 1 39  ? 30.803 -32.062 26.048  1.00 14.27 ? 39  ILE A O   1 
ATOM   297  C CB  . ILE A 1 39  ? 32.425 -34.895 26.574  1.00 16.06 ? 39  ILE A CB  1 
ATOM   298  C CG1 . ILE A 1 39  ? 33.842 -35.444 26.672  1.00 16.74 ? 39  ILE A CG1 1 
ATOM   299  C CG2 . ILE A 1 39  ? 31.870 -34.839 25.142  1.00 14.31 ? 39  ILE A CG2 1 
ATOM   300  C CD1 . ILE A 1 39  ? 33.912 -36.929 26.306  1.00 16.08 ? 39  ILE A CD1 1 
ATOM   301  N N   . ASP A 1 40  ? 29.953 -33.319 27.737  1.00 16.18 ? 40  ASP A N   1 
ATOM   302  C CA  . ASP A 1 40  ? 28.608 -32.763 27.576  1.00 17.49 ? 40  ASP A CA  1 
ATOM   303  C C   . ASP A 1 40  ? 28.610 -31.255 27.814  1.00 14.77 ? 40  ASP A C   1 
ATOM   304  O O   . ASP A 1 40  ? 28.080 -30.491 27.001  1.00 15.05 ? 40  ASP A O   1 
ATOM   305  C CB  . ASP A 1 40  ? 27.621 -33.477 28.519  1.00 17.10 ? 40  ASP A CB  1 
ATOM   306  C CG  . ASP A 1 40  ? 27.296 -34.909 28.080  1.00 18.72 ? 40  ASP A CG  1 
ATOM   307  O OD1 . ASP A 1 40  ? 27.674 -35.307 26.946  1.00 20.13 ? 40  ASP A OD1 1 
ATOM   308  O OD2 . ASP A 1 40  ? 26.662 -35.640 28.878  1.00 19.00 ? 40  ASP A OD2 1 
ATOM   309  N N   . ARG A 1 41  ? 29.252 -30.820 28.913  1.00 15.49 ? 41  ARG A N   1 
ATOM   310  C CA  . ARG A 1 41  ? 29.246 -29.414 29.319  1.00 14.85 ? 41  ARG A CA  1 
ATOM   311  C C   . ARG A 1 41  ? 29.908 -28.511 28.270  1.00 16.51 ? 41  ARG A C   1 
ATOM   312  O O   . ARG A 1 41  ? 29.390 -27.436 27.935  1.00 16.07 ? 41  ARG A O   1 
ATOM   313  C CB  . ARG A 1 41  ? 29.903 -29.271 30.695  1.00 14.54 ? 41  ARG A CB  1 
ATOM   314  C CG  . ARG A 1 41  ? 29.931 -27.839 31.256  1.00 15.91 ? 41  ARG A CG  1 
ATOM   315  C CD  . ARG A 1 41  ? 28.518 -27.249 31.433  1.00 15.09 ? 41  ARG A CD  1 
ATOM   316  N NE  . ARG A 1 41  ? 28.560 -25.815 31.717  1.00 17.25 ? 41  ARG A NE  1 
ATOM   317  C CZ  . ARG A 1 41  ? 27.705 -24.915 31.221  1.00 20.24 ? 41  ARG A CZ  1 
ATOM   318  N NH1 . ARG A 1 41  ? 26.670 -25.273 30.473  1.00 18.17 ? 41  ARG A NH1 1 
ATOM   319  N NH2 . ARG A 1 41  ? 27.903 -23.617 31.470  1.00 21.10 ? 41  ARG A NH2 1 
ATOM   320  N N   . MET A 1 42  ? 31.052 -28.918 27.735  1.00 15.79 ? 42  MET A N   1 
ATOM   321  C CA  . MET A 1 42  ? 31.644 -28.132 26.654  1.00 15.93 ? 42  MET A CA  1 
ATOM   322  C C   . MET A 1 42  ? 30.702 -28.044 25.468  1.00 16.00 ? 42  MET A C   1 
ATOM   323  O O   . MET A 1 42  ? 30.631 -27.006 24.794  1.00 15.76 ? 42  MET A O   1 
ATOM   324  C CB  . MET A 1 42  ? 32.973 -28.753 26.206  1.00 16.32 ? 42  MET A CB  1 
ATOM   325  C CG  . MET A 1 42  ? 34.142 -28.524 27.145  1.00 17.12 ? 42  MET A CG  1 
ATOM   326  S SD  . MET A 1 42  ? 34.576 -26.766 27.139  1.00 19.28 ? 42  MET A SD  1 
ATOM   327  C CE  . MET A 1 42  ? 35.418 -26.579 25.571  1.00 12.77 ? 42  MET A CE  1 
ATOM   328  N N   . ALA A 1 43  ? 29.978 -29.136 25.183  1.00 16.44 ? 43  ALA A N   1 
ATOM   329  C CA  . ALA A 1 43  ? 29.159 -29.176 23.984  1.00 15.20 ? 43  ALA A CA  1 
ATOM   330  C C   . ALA A 1 43  ? 27.858 -28.423 24.191  1.00 16.02 ? 43  ALA A C   1 
ATOM   331  O O   . ALA A 1 43  ? 27.332 -27.807 23.257  1.00 17.90 ? 43  ALA A O   1 
ATOM   332  C CB  . ALA A 1 43  ? 28.888 -30.624 23.608  1.00 15.96 ? 43  ALA A CB  1 
ATOM   333  N N   . GLU A 1 44  ? 27.332 -28.462 25.403  1.00 16.58 ? 44  GLU A N   1 
ATOM   334  C CA  . GLU A 1 44  ? 26.144 -27.680 25.716  1.00 18.73 ? 44  GLU A CA  1 
ATOM   335  C C   . GLU A 1 44  ? 26.433 -26.185 25.650  1.00 16.97 ? 44  GLU A C   1 
ATOM   336  O O   . GLU A 1 44  ? 25.642 -25.422 25.095  1.00 15.75 ? 44  GLU A O   1 
ATOM   337  C CB  . GLU A 1 44  ? 25.636 -28.107 27.087  1.00 17.08 ? 44  GLU A CB  1 
ATOM   338  C CG  . GLU A 1 44  ? 25.089 -27.040 27.970  1.00 19.87 ? 44  GLU A CG  1 
ATOM   339  C CD  . GLU A 1 44  ? 24.515 -27.631 29.260  1.00 28.16 ? 44  GLU A CD  1 
ATOM   340  O OE1 . GLU A 1 44  ? 25.280 -27.961 30.222  1.00 24.34 ? 44  GLU A OE1 1 
ATOM   341  O OE2 . GLU A 1 44  ? 23.268 -27.776 29.309  1.00 35.44 ? 44  GLU A OE2 1 
ATOM   342  N N   . ILE A 1 45  ? 27.593 -25.767 26.161  1.00 17.29 ? 45  ILE A N   1 
ATOM   343  C CA  . ILE A 1 45  ? 27.952 -24.348 26.192  1.00 17.51 ? 45  ILE A CA  1 
ATOM   344  C C   . ILE A 1 45  ? 27.930 -23.743 24.789  1.00 18.07 ? 45  ILE A C   1 
ATOM   345  O O   . ILE A 1 45  ? 27.381 -22.648 24.575  1.00 17.09 ? 45  ILE A O   1 
ATOM   346  C CB  . ILE A 1 45  ? 29.317 -24.148 26.881  1.00 17.48 ? 45  ILE A CB  1 
ATOM   347  C CG1 . ILE A 1 45  ? 29.245 -24.496 28.378  1.00 16.56 ? 45  ILE A CG1 1 
ATOM   348  C CG2 . ILE A 1 45  ? 29.801 -22.701 26.690  1.00 19.42 ? 45  ILE A CG2 1 
ATOM   349  C CD1 . ILE A 1 45  ? 30.602 -24.517 29.093  1.00 15.85 ? 45  ILE A CD1 1 
ATOM   350  N N   . TYR A 1 46  ? 28.548 -24.434 23.811  1.00 15.34 ? 46  TYR A N   1 
ATOM   351  C CA  . TYR A 1 46  ? 28.721 -23.893 22.461  1.00 17.26 ? 46  TYR A CA  1 
ATOM   352  C C   . TYR A 1 46  ? 27.654 -24.335 21.468  1.00 17.10 ? 46  TYR A C   1 
ATOM   353  O O   . TYR A 1 46  ? 27.609 -23.809 20.353  1.00 14.75 ? 46  TYR A O   1 
ATOM   354  C CB  . TYR A 1 46  ? 30.159 -24.109 21.925  1.00 17.87 ? 46  TYR A CB  1 
ATOM   355  C CG  . TYR A 1 46  ? 31.188 -23.301 22.713  1.00 18.29 ? 46  TYR A CG  1 
ATOM   356  C CD1 . TYR A 1 46  ? 31.451 -21.959 22.391  1.00 16.43 ? 46  TYR A CD1 1 
ATOM   357  C CD2 . TYR A 1 46  ? 31.840 -23.853 23.826  1.00 15.80 ? 46  TYR A CD2 1 
ATOM   358  C CE1 . TYR A 1 46  ? 32.366 -21.208 23.140  1.00 15.78 ? 46  TYR A CE1 1 
ATOM   359  C CE2 . TYR A 1 46  ? 32.753 -23.102 24.582  1.00 16.74 ? 46  TYR A CE2 1 
ATOM   360  C CZ  . TYR A 1 46  ? 33.006 -21.783 24.234  1.00 15.67 ? 46  TYR A CZ  1 
ATOM   361  O OH  . TYR A 1 46  ? 33.902 -21.069 24.991  1.00 14.98 ? 46  TYR A OH  1 
ATOM   362  N N   . GLU A 1 47  ? 26.783 -25.269 21.853  1.00 17.65 ? 47  GLU A N   1 
ATOM   363  C CA  . GLU A 1 47  ? 25.577 -25.504 21.074  1.00 18.51 ? 47  GLU A CA  1 
ATOM   364  C C   . GLU A 1 47  ? 24.485 -24.485 21.418  1.00 19.94 ? 47  GLU A C   1 
ATOM   365  O O   . GLU A 1 47  ? 23.861 -23.902 20.525  1.00 21.76 ? 47  GLU A O   1 
ATOM   366  C CB  . GLU A 1 47  ? 25.091 -26.938 21.303  1.00 19.54 ? 47  GLU A CB  1 
ATOM   367  C CG  . GLU A 1 47  ? 25.855 -27.987 20.503  1.00 18.93 ? 47  GLU A CG  1 
ATOM   368  C CD  . GLU A 1 47  ? 25.235 -29.370 20.635  1.00 19.13 ? 47  GLU A CD  1 
ATOM   369  O OE1 . GLU A 1 47  ? 24.663 -29.646 21.708  1.00 22.52 ? 47  GLU A OE1 1 
ATOM   370  O OE2 . GLU A 1 47  ? 25.296 -30.163 19.675  1.00 18.69 ? 47  GLU A OE2 1 
ATOM   371  N N   . ASN A 1 48  ? 24.287 -24.205 22.697  1.00 20.43 ? 48  ASN A N   1 
ATOM   372  C CA  . ASN A 1 48  ? 23.093 -23.504 23.150  1.00 21.95 ? 48  ASN A CA  1 
ATOM   373  C C   . ASN A 1 48  ? 23.359 -22.258 24.002  1.00 21.49 ? 48  ASN A C   1 
ATOM   374  O O   . ASN A 1 48  ? 22.434 -21.460 24.176  1.00 22.81 ? 48  ASN A O   1 
ATOM   375  C CB  . ASN A 1 48  ? 22.198 -24.462 23.962  1.00 22.75 ? 48  ASN A CB  1 
ATOM   376  C CG  . ASN A 1 48  ? 22.044 -25.823 23.306  1.00 22.79 ? 48  ASN A CG  1 
ATOM   377  O OD1 . ASN A 1 48  ? 21.573 -25.941 22.179  1.00 25.46 ? 48  ASN A OD1 1 
ATOM   378  N ND2 . ASN A 1 48  ? 22.432 -26.871 24.034  1.00 28.06 ? 48  ASN A ND2 1 
ATOM   379  N N   . GLU A 1 49  ? 24.557 -22.071 24.558  1.00 18.08 ? 49  GLU A N   1 
ATOM   380  C CA  . GLU A 1 49  ? 24.820 -20.905 25.396  1.00 21.06 ? 49  GLU A CA  1 
ATOM   381  C C   . GLU A 1 49  ? 25.533 -19.760 24.658  1.00 22.89 ? 49  GLU A C   1 
ATOM   382  O O   . GLU A 1 49  ? 25.001 -18.641 24.570  1.00 20.45 ? 49  GLU A O   1 
ATOM   383  C CB  . GLU A 1 49  ? 25.486 -21.285 26.737  1.00 21.82 ? 49  GLU A CB  1 
ATOM   384  C CG  . GLU A 1 49  ? 24.639 -22.203 27.657  1.00 20.98 ? 49  GLU A CG  1 
ATOM   385  C CD  . GLU A 1 49  ? 25.355 -22.618 28.970  1.00 22.98 ? 49  GLU A CD  1 
ATOM   386  O OE1 . GLU A 1 49  ? 26.303 -21.909 29.442  1.00 24.50 ? 49  GLU A OE1 1 
ATOM   387  O OE2 . GLU A 1 49  ? 24.944 -23.642 29.564  1.00 21.07 ? 49  GLU A OE2 1 
ATOM   388  N N   . VAL A 1 50  ? 26.730 -20.009 24.114  1.00 20.87 ? 50  VAL A N   1 
ATOM   389  C CA  . VAL A 1 50  ? 27.508 -18.976 23.431  1.00 17.81 ? 50  VAL A CA  1 
ATOM   390  C C   . VAL A 1 50  ? 27.244 -19.066 21.942  1.00 19.69 ? 50  VAL A C   1 
ATOM   391  O O   . VAL A 1 50  ? 27.426 -20.132 21.333  1.00 19.68 ? 50  VAL A O   1 
ATOM   392  C CB  . VAL A 1 50  ? 29.007 -19.133 23.712  1.00 18.03 ? 50  VAL A CB  1 
ATOM   393  C CG1 . VAL A 1 50  ? 29.781 -18.076 22.947  1.00 18.07 ? 50  VAL A CG1 1 
ATOM   394  C CG2 . VAL A 1 50  ? 29.289 -19.025 25.205  1.00 19.29 ? 50  VAL A CG2 1 
ATOM   395  N N   . GLY A 1 51  ? 26.834 -17.951 21.345  1.00 16.04 ? 51  GLY A N   1 
ATOM   396  C CA  . GLY A 1 51  ? 26.540 -17.925 19.940  1.00 15.52 ? 51  GLY A CA  1 
ATOM   397  C C   . GLY A 1 51  ? 26.498 -16.514 19.421  1.00 16.18 ? 51  GLY A C   1 
ATOM   398  O O   . GLY A 1 51  ? 26.606 -15.553 20.187  1.00 17.28 ? 51  GLY A O   1 
ATOM   399  N N   . PRO A 1 52  ? 26.340 -16.364 18.103  1.00 18.72 ? 52  PRO A N   1 
ATOM   400  C CA  . PRO A 1 52  ? 26.308 -15.011 17.494  1.00 19.26 ? 52  PRO A CA  1 
ATOM   401  C C   . PRO A 1 52  ? 25.167 -14.122 17.962  1.00 18.21 ? 52  PRO A C   1 
ATOM   402  O O   . PRO A 1 52  ? 25.133 -12.942 17.568  1.00 18.63 ? 52  PRO A O   1 
ATOM   403  C CB  . PRO A 1 52  ? 26.190 -15.305 15.988  1.00 20.85 ? 52  PRO A CB  1 
ATOM   404  C CG  . PRO A 1 52  ? 25.502 -16.681 15.932  1.00 17.34 ? 52  PRO A CG  1 
ATOM   405  C CD  . PRO A 1 52  ? 26.192 -17.419 17.083  1.00 17.54 ? 52  PRO A CD  1 
ATOM   406  N N   . HIS A 1 53  ? 24.208 -14.649 18.726  1.00 16.95 ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 23.188 -13.780 19.310  1.00 18.18 ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 23.795 -12.821 20.306  1.00 18.42 ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 23.277 -11.712 20.502  1.00 18.79 ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 22.070 -14.608 19.950  1.00 18.59 ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 22.537 -15.492 21.058  1.00 18.08 ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 23.210 -16.675 20.823  1.00 19.04 ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 22.425 -15.380 22.401  1.00 19.01 ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 23.501 -17.253 21.975  1.00 18.17 ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 23.030 -16.492 22.949  1.00 19.71 ? 53  HIS A NE2 1 
ATOM   416  N N   . LEU A 1 54  ? 24.882 -13.238 20.950  1.00 17.03 ? 54  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54  ? 25.584 -12.381 21.886  1.00 16.51 ? 54  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54  ? 26.180 -11.166 21.169  1.00 17.85 ? 54  LEU A C   1 
ATOM   419  O O   . LEU A 1 54  ? 26.064 -10.025 21.640  1.00 17.65 ? 54  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54  ? 26.672 -13.209 22.562  1.00 16.85 ? 54  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54  ? 26.125 -14.363 23.396  1.00 16.06 ? 54  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54  ? 27.255 -15.148 23.988  1.00 15.49 ? 54  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54  ? 25.169 -13.868 24.489  1.00 18.87 ? 54  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55  ? 26.832 -11.398 20.027  1.00 15.99 ? 55  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55  ? 27.383 -10.303 19.261  1.00 15.55 ? 55  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55  ? 26.322 -9.328  18.799  1.00 18.15 ? 55  GLY A C   1 
ATOM   427  O O   . GLY A 1 55  ? 26.529 -8.119  18.856  1.00 18.90 ? 55  GLY A O   1 
ATOM   428  N N   . ALA A 1 56  ? 25.169 -9.834  18.341  1.00 17.32 ? 56  ALA A N   1 
ATOM   429  C CA  . ALA A 1 56  ? 24.099 -8.944  17.885  1.00 16.53 ? 56  ALA A CA  1 
ATOM   430  C C   . ALA A 1 56  ? 23.671 -7.961  18.977  1.00 17.35 ? 56  ALA A C   1 
ATOM   431  O O   . ALA A 1 56  ? 23.355 -6.803  18.682  1.00 17.98 ? 56  ALA A O   1 
ATOM   432  C CB  . ALA A 1 56  ? 22.915 -9.752  17.366  1.00 18.01 ? 56  ALA A CB  1 
ATOM   433  N N   . LYS A 1 57  ? 23.668 -8.396  20.241  1.00 17.54 ? 57  LYS A N   1 
ATOM   434  C CA  . LYS A 1 57  ? 23.279 -7.514  21.342  1.00 17.56 ? 57  LYS A CA  1 
ATOM   435  C C   . LYS A 1 57  ? 24.227 -6.332  21.470  1.00 20.11 ? 57  LYS A C   1 
ATOM   436  O O   . LYS A 1 57  ? 23.795 -5.208  21.772  1.00 19.43 ? 57  LYS A O   1 
ATOM   437  C CB  . LYS A 1 57  ? 23.286 -8.274  22.663  1.00 21.19 ? 57  LYS A CB  1 
ATOM   438  C CG  . LYS A 1 57  ? 22.288 -9.385  22.797  1.00 20.84 ? 57  LYS A CG  1 
ATOM   439  C CD  . LYS A 1 57  ? 22.655 -10.226 23.997  1.00 19.58 ? 57  LYS A CD  1 
ATOM   440  C CE  . LYS A 1 57  ? 22.545 -9.402  25.274  1.00 27.44 ? 57  LYS A CE  1 
ATOM   441  N NZ  . LYS A 1 57  ? 22.490 -10.270 26.517  1.00 33.03 ? 57  LYS A NZ  1 
ATOM   442  N N   . VAL A 1 58  ? 25.530 -6.573  21.306  1.00 17.44 ? 58  VAL A N   1 
ATOM   443  C CA  . VAL A 1 58  ? 26.490 -5.467  21.306  1.00 18.51 ? 58  VAL A CA  1 
ATOM   444  C C   . VAL A 1 58  ? 26.213 -4.534  20.132  1.00 17.30 ? 58  VAL A C   1 
ATOM   445  O O   . VAL A 1 58  ? 26.137 -3.308  20.290  1.00 17.81 ? 58  VAL A O   1 
ATOM   446  C CB  . VAL A 1 58  ? 27.934 -6.005  21.259  1.00 19.27 ? 58  VAL A CB  1 
ATOM   447  C CG1 . VAL A 1 58  ? 28.941 -4.840  21.257  1.00 18.05 ? 58  VAL A CG1 1 
ATOM   448  C CG2 . VAL A 1 58  ? 28.182 -6.968  22.397  1.00 17.47 ? 58  VAL A CG2 1 
ATOM   449  N N   . VAL A 1 59  ? 26.050 -5.109  18.937  1.00 15.76 ? 59  VAL A N   1 
ATOM   450  C CA  . VAL A 1 59  ? 25.883 -4.312  17.726  1.00 17.97 ? 59  VAL A CA  1 
ATOM   451  C C   . VAL A 1 59  ? 24.687 -3.375  17.862  1.00 19.71 ? 59  VAL A C   1 
ATOM   452  O O   . VAL A 1 59  ? 24.778 -2.183  17.536  1.00 19.60 ? 59  VAL A O   1 
ATOM   453  C CB  . VAL A 1 59  ? 25.778 -5.206  16.473  1.00 15.65 ? 59  VAL A CB  1 
ATOM   454  C CG1 . VAL A 1 59  ? 25.423 -4.371  15.275  1.00 16.55 ? 59  VAL A CG1 1 
ATOM   455  C CG2 . VAL A 1 59  ? 27.082 -5.933  16.211  1.00 15.81 ? 59  VAL A CG2 1 
ATOM   456  N N   . VAL A 1 60  ? 23.547 -3.896  18.338  1.00 19.45 ? 60  VAL A N   1 
ATOM   457  C CA  . VAL A 1 60  ? 22.355 -3.049  18.433  1.00 18.87 ? 60  VAL A CA  1 
ATOM   458  C C   . VAL A 1 60  ? 22.476 -2.047  19.565  1.00 19.04 ? 60  VAL A C   1 
ATOM   459  O O   . VAL A 1 60  ? 21.833 -0.993  19.514  1.00 19.16 ? 60  VAL A O   1 
ATOM   460  C CB  . VAL A 1 60  ? 21.048 -3.853  18.551  1.00 19.67 ? 60  VAL A CB  1 
ATOM   461  C CG1 . VAL A 1 60  ? 20.893 -4.788  17.335  1.00 21.32 ? 60  VAL A CG1 1 
ATOM   462  C CG2 . VAL A 1 60  ? 20.990 -4.593  19.867  1.00 21.22 ? 60  VAL A CG2 1 
ATOM   463  N N   . LYS A 1 61  ? 23.291 -2.352  20.585  1.00 19.19 ? 61  LYS A N   1 
ATOM   464  C CA  . LYS A 1 61  ? 23.621 -1.368  21.616  1.00 19.65 ? 61  LYS A CA  1 
ATOM   465  C C   . LYS A 1 61  ? 24.466 -0.226  21.060  1.00 20.66 ? 61  LYS A C   1 
ATOM   466  O O   . LYS A 1 61  ? 24.231 0.944   21.395  1.00 21.71 ? 61  LYS A O   1 
ATOM   467  C CB  . LYS A 1 61  ? 24.372 -2.011  22.763  1.00 17.79 ? 61  LYS A CB  1 
ATOM   468  C CG  . LYS A 1 61  ? 24.501 -1.082  23.929  1.00 18.44 ? 61  LYS A CG  1 
ATOM   469  C CD  . LYS A 1 61  ? 25.337 -1.678  25.019  1.00 19.00 ? 61  LYS A CD  1 
ATOM   470  C CE  . LYS A 1 61  ? 25.442 -0.709  26.126  1.00 18.86 ? 61  LYS A CE  1 
ATOM   471  N NZ  . LYS A 1 61  ? 24.094 -0.518  26.702  1.00 21.61 ? 61  LYS A NZ  1 
ATOM   472  N N   . ALA A 1 62  ? 25.486 -0.542  20.250  1.00 17.54 ? 62  ALA A N   1 
ATOM   473  C CA  . ALA A 1 62  ? 26.297 0.517   19.648  1.00 17.86 ? 62  ALA A CA  1 
ATOM   474  C C   . ALA A 1 62  ? 25.493 1.323   18.635  1.00 17.43 ? 62  ALA A C   1 
ATOM   475  O O   . ALA A 1 62  ? 25.690 2.536   18.500  1.00 16.81 ? 62  ALA A O   1 
ATOM   476  C CB  . ALA A 1 62  ? 27.542 -0.083  18.993  1.00 17.33 ? 62  ALA A CB  1 
ATOM   477  N N   . TRP A 1 63  ? 24.584 0.656   17.920  1.00 18.43 ? 63  TRP A N   1 
ATOM   478  C CA  . TRP A 1 63  ? 23.743 1.334   16.946  1.00 19.76 ? 63  TRP A CA  1 
ATOM   479  C C   . TRP A 1 63  ? 22.832 2.351   17.610  1.00 20.43 ? 63  TRP A C   1 
ATOM   480  O O   . TRP A 1 63  ? 22.418 3.333   16.974  1.00 21.60 ? 63  TRP A O   1 
ATOM   481  C CB  . TRP A 1 63  ? 22.868 0.319   16.217  1.00 18.94 ? 63  TRP A CB  1 
ATOM   482  C CG  . TRP A 1 63  ? 23.525 -0.379  15.113  1.00 18.43 ? 63  TRP A CG  1 
ATOM   483  C CD1 . TRP A 1 63  ? 24.787 -0.157  14.622  1.00 17.40 ? 63  TRP A CD1 1 
ATOM   484  C CD2 . TRP A 1 63  ? 22.944 -1.411  14.315  1.00 17.98 ? 63  TRP A CD2 1 
ATOM   485  N NE1 . TRP A 1 63  ? 25.025 -0.999  13.562  1.00 18.89 ? 63  TRP A NE1 1 
ATOM   486  C CE2 . TRP A 1 63  ? 23.909 -1.776  13.345  1.00 19.07 ? 63  TRP A CE2 1 
ATOM   487  C CE3 . TRP A 1 63  ? 21.693 -2.058  14.317  1.00 16.75 ? 63  TRP A CE3 1 
ATOM   488  C CZ2 . TRP A 1 63  ? 23.667 -2.779  12.377  1.00 19.27 ? 63  TRP A CZ2 1 
ATOM   489  C CZ3 . TRP A 1 63  ? 21.450 -3.045  13.366  1.00 19.07 ? 63  TRP A CZ3 1 
ATOM   490  C CH2 . TRP A 1 63  ? 22.441 -3.402  12.401  1.00 20.25 ? 63  TRP A CH2 1 
ATOM   491  N N   . THR A 1 64  ? 22.492 2.121   18.870  1.00 19.44 ? 64  THR A N   1 
ATOM   492  C CA  . THR A 1 64  ? 21.476 2.912   19.548  1.00 21.41 ? 64  THR A CA  1 
ATOM   493  C C   . THR A 1 64  ? 22.038 3.689   20.736  1.00 21.70 ? 64  THR A C   1 
ATOM   494  O O   . THR A 1 64  ? 21.271 4.338   21.465  1.00 23.83 ? 64  THR A O   1 
ATOM   495  C CB  . THR A 1 64  ? 20.311 2.000   19.970  1.00 19.36 ? 64  THR A CB  1 
ATOM   496  O OG1 . THR A 1 64  ? 20.785 0.983   20.861  1.00 18.60 ? 64  THR A OG1 1 
ATOM   497  C CG2 . THR A 1 64  ? 19.723 1.319   18.730  1.00 19.89 ? 64  THR A CG2 1 
ATOM   498  N N   . ASP A 1 65  ? 23.351 3.651   20.958  1.00 21.41 ? 65  ASP A N   1 
ATOM   499  C CA  . ASP A 1 65  ? 23.934 4.246   22.162  1.00 21.62 ? 65  ASP A CA  1 
ATOM   500  C C   . ASP A 1 65  ? 25.327 4.736   21.798  1.00 22.43 ? 65  ASP A C   1 
ATOM   501  O O   . ASP A 1 65  ? 26.329 4.024   21.990  1.00 20.88 ? 65  ASP A O   1 
ATOM   502  C CB  . ASP A 1 65  ? 23.950 3.256   23.331  1.00 20.39 ? 65  ASP A CB  1 
ATOM   503  C CG  . ASP A 1 65  ? 24.374 3.881   24.653  1.00 19.67 ? 65  ASP A CG  1 
ATOM   504  O OD1 . ASP A 1 65  ? 25.048 4.933   24.665  1.00 22.20 ? 65  ASP A OD1 1 
ATOM   505  O OD2 . ASP A 1 65  ? 24.016 3.316   25.698  1.00 19.32 ? 65  ASP A OD2 1 
ATOM   506  N N   . PRO A 1 66  ? 25.429 5.968   21.266  1.00 22.86 ? 66  PRO A N   1 
ATOM   507  C CA  . PRO A 1 66  ? 26.722 6.446   20.743  1.00 21.66 ? 66  PRO A CA  1 
ATOM   508  C C   . PRO A 1 66  ? 27.830 6.449   21.767  1.00 21.67 ? 66  PRO A C   1 
ATOM   509  O O   . PRO A 1 66  ? 28.995 6.263   21.400  1.00 23.34 ? 66  PRO A O   1 
ATOM   510  C CB  . PRO A 1 66  ? 26.387 7.862   20.257  1.00 22.54 ? 66  PRO A CB  1 
ATOM   511  C CG  . PRO A 1 66  ? 24.953 7.763   19.868  1.00 21.38 ? 66  PRO A CG  1 
ATOM   512  C CD  . PRO A 1 66  ? 24.361 6.952   21.004  1.00 21.39 ? 66  PRO A CD  1 
ATOM   513  N N   . GLU A 1 67  ? 27.513 6.654   23.040  1.00 22.14 ? 67  GLU A N   1 
ATOM   514  C CA  . GLU A 1 67  ? 28.555 6.608   24.058  1.00 22.98 ? 67  GLU A CA  1 
ATOM   515  C C   . GLU A 1 67  ? 29.044 5.177   24.262  1.00 22.62 ? 67  GLU A C   1 
ATOM   516  O O   . GLU A 1 67  ? 30.255 4.935   24.323  1.00 21.30 ? 67  GLU A O   1 
ATOM   517  C CB  . GLU A 1 67  ? 28.069 7.255   25.362  1.00 24.91 ? 67  GLU A CB  1 
ATOM   518  C CG  . GLU A 1 67  ? 28.053 8.810   25.316  1.00 29.62 ? 67  GLU A CG  1 
ATOM   519  C CD  . GLU A 1 67  ? 29.419 9.454   24.934  1.00 38.33 ? 67  GLU A CD  1 
ATOM   520  O OE1 . GLU A 1 67  ? 30.377 9.404   25.762  1.00 44.21 ? 67  GLU A OE1 1 
ATOM   521  O OE2 . GLU A 1 67  ? 29.538 10.000  23.800  1.00 36.53 ? 67  GLU A OE2 1 
ATOM   522  N N   . PHE A 1 68  ? 28.128 4.202   24.327  1.00 22.31 ? 68  PHE A N   1 
ATOM   523  C CA  . PHE A 1 68  ? 28.598 2.817   24.329  1.00 21.55 ? 68  PHE A CA  1 
ATOM   524  C C   . PHE A 1 68  ? 29.419 2.511   23.083  1.00 20.65 ? 68  PHE A C   1 
ATOM   525  O O   . PHE A 1 68  ? 30.431 1.796   23.157  1.00 19.83 ? 68  PHE A O   1 
ATOM   526  C CB  . PHE A 1 68  ? 27.463 1.798   24.472  1.00 20.87 ? 68  PHE A CB  1 
ATOM   527  C CG  . PHE A 1 68  ? 27.942 0.360   24.321  1.00 19.61 ? 68  PHE A CG  1 
ATOM   528  C CD1 . PHE A 1 68  ? 28.689 -0.247  25.322  1.00 19.90 ? 68  PHE A CD1 1 
ATOM   529  C CD2 . PHE A 1 68  ? 27.663 -0.364  23.175  1.00 21.10 ? 68  PHE A CD2 1 
ATOM   530  C CE1 . PHE A 1 68  ? 29.142 -1.542  25.196  1.00 18.92 ? 68  PHE A CE1 1 
ATOM   531  C CE2 . PHE A 1 68  ? 28.117 -1.681  23.044  1.00 20.93 ? 68  PHE A CE2 1 
ATOM   532  C CZ  . PHE A 1 68  ? 28.859 -2.264  24.059  1.00 18.25 ? 68  PHE A CZ  1 
ATOM   533  N N   . LYS A 1 69  ? 28.995 3.030   21.928  1.00 18.48 ? 69  LYS A N   1 
ATOM   534  C CA  . LYS A 1 69  ? 29.704 2.737   20.686  1.00 20.05 ? 69  LYS A CA  1 
ATOM   535  C C   . LYS A 1 69  ? 31.150 3.217   20.768  1.00 21.09 ? 69  LYS A C   1 
ATOM   536  O O   . LYS A 1 69  ? 32.076 2.509   20.355  1.00 21.58 ? 69  LYS A O   1 
ATOM   537  C CB  . LYS A 1 69  ? 28.958 3.360   19.509  1.00 17.55 ? 69  LYS A CB  1 
ATOM   538  C CG  . LYS A 1 69  ? 29.570 3.083   18.175  1.00 19.81 ? 69  LYS A CG  1 
ATOM   539  C CD  . LYS A 1 69  ? 28.716 3.666   17.062  1.00 20.13 ? 69  LYS A CD  1 
ATOM   540  C CE  . LYS A 1 69  ? 29.364 3.454   15.709  1.00 22.13 ? 69  LYS A CE  1 
ATOM   541  N NZ  . LYS A 1 69  ? 28.458 3.946   14.644  1.00 22.64 ? 69  LYS A NZ  1 
ATOM   542  N N   . LYS A 1 70  ? 31.362 4.403   21.343  1.00 20.76 ? 70  LYS A N   1 
ATOM   543  C CA  . LYS A 1 70  ? 32.712 4.893   21.620  1.00 22.13 ? 70  LYS A CA  1 
ATOM   544  C C   . LYS A 1 70  ? 33.518 3.888   22.441  1.00 20.60 ? 70  LYS A C   1 
ATOM   545  O O   . LYS A 1 70  ? 34.630 3.502   22.055  1.00 20.35 ? 70  LYS A O   1 
ATOM   546  C CB  . LYS A 1 70  ? 32.633 6.239   22.360  1.00 24.66 ? 70  LYS A CB  1 
ATOM   547  C CG  . LYS A 1 70  ? 33.694 7.274   21.946  1.00 26.78 ? 70  LYS A CG  1 
ATOM   548  C CD  . LYS A 1 70  ? 33.847 8.390   23.010  1.00 32.47 ? 70  LYS A CD  1 
ATOM   549  C CE  . LYS A 1 70  ? 34.888 9.462   22.603  1.00 30.76 ? 70  LYS A CE  1 
ATOM   550  N NZ  . LYS A 1 70  ? 36.231 9.241   23.202  1.00 29.99 ? 70  LYS A NZ  1 
ATOM   551  N N   . ARG A 1 71  ? 32.977 3.477   23.592  1.00 20.50 ? 71  ARG A N   1 
ATOM   552  C CA  . ARG A 1 71  ? 33.692 2.573   24.501  1.00 20.22 ? 71  ARG A CA  1 
ATOM   553  C C   . ARG A 1 71  ? 33.991 1.233   23.830  1.00 21.57 ? 71  ARG A C   1 
ATOM   554  O O   . ARG A 1 71  ? 35.058 0.635   24.060  1.00 20.88 ? 71  ARG A O   1 
ATOM   555  C CB  . ARG A 1 71  ? 32.846 2.335   25.753  1.00 20.01 ? 71  ARG A CB  1 
ATOM   556  C CG  . ARG A 1 71  ? 32.538 3.585   26.539  1.00 19.74 ? 71  ARG A CG  1 
ATOM   557  C CD  . ARG A 1 71  ? 32.054 3.283   27.945  1.00 19.15 ? 71  ARG A CD  1 
ATOM   558  N NE  . ARG A 1 71  ? 30.769 2.593   27.961  1.00 20.02 ? 71  ARG A NE  1 
ATOM   559  C CZ  . ARG A 1 71  ? 29.597 3.176   27.739  1.00 21.17 ? 71  ARG A CZ  1 
ATOM   560  N NH1 . ARG A 1 71  ? 29.519 4.429   27.312  1.00 21.85 ? 71  ARG A NH1 1 
ATOM   561  N NH2 . ARG A 1 71  ? 28.475 2.482   27.922  1.00 19.24 ? 71  ARG A NH2 1 
ATOM   562  N N   . LEU A 1 72  ? 33.048 0.738   23.012  1.00 20.26 ? 72  LEU A N   1 
ATOM   563  C CA  . LEU A 1 72  ? 33.269 -0.507  22.275  1.00 19.82 ? 72  LEU A CA  1 
ATOM   564  C C   . LEU A 1 72  ? 34.495 -0.392  21.382  1.00 19.67 ? 72  LEU A C   1 
ATOM   565  O O   . LEU A 1 72  ? 35.395 -1.235  21.429  1.00 20.59 ? 72  LEU A O   1 
ATOM   566  C CB  . LEU A 1 72  ? 32.032 -0.844  21.443  1.00 17.95 ? 72  LEU A CB  1 
ATOM   567  C CG  . LEU A 1 72  ? 32.093 -2.130  20.602  1.00 17.81 ? 72  LEU A CG  1 
ATOM   568  C CD1 . LEU A 1 72  ? 32.192 -3.352  21.511  1.00 17.33 ? 72  LEU A CD1 1 
ATOM   569  C CD2 . LEU A 1 72  ? 30.881 -2.237  19.702  1.00 16.61 ? 72  LEU A CD2 1 
ATOM   570  N N   . LEU A 1 73  ? 34.546 0.665   20.571  1.00 19.09 ? 73  LEU A N   1 
ATOM   571  C CA  . LEU A 1 73  ? 35.645 0.889   19.644  1.00 20.95 ? 73  LEU A CA  1 
ATOM   572  C C   . LEU A 1 73  ? 36.959 1.255   20.353  1.00 20.97 ? 73  LEU A C   1 
ATOM   573  O O   . LEU A 1 73  ? 38.039 1.112   19.763  1.00 23.10 ? 73  LEU A O   1 
ATOM   574  C CB  . LEU A 1 73  ? 35.238 1.971   18.639  1.00 18.67 ? 73  LEU A CB  1 
ATOM   575  C CG  . LEU A 1 73  ? 34.003 1.703   17.776  1.00 18.12 ? 73  LEU A CG  1 
ATOM   576  C CD1 . LEU A 1 73  ? 33.622 2.938   16.922  1.00 20.63 ? 73  LEU A CD1 1 
ATOM   577  C CD2 . LEU A 1 73  ? 34.169 0.478   16.884  1.00 16.37 ? 73  LEU A CD2 1 
ATOM   578  N N   . ALA A 1 74  ? 36.906 1.730   21.586  1.00 20.13 ? 74  ALA A N   1 
ATOM   579  C CA  . ALA A 1 74  ? 38.154 2.029   22.276  1.00 22.17 ? 74  ALA A CA  1 
ATOM   580  C C   . ALA A 1 74  ? 38.735 0.784   22.947  1.00 24.27 ? 74  ALA A C   1 
ATOM   581  O O   . ALA A 1 74  ? 39.953 0.570   22.919  1.00 28.59 ? 74  ALA A O   1 
ATOM   582  C CB  . ALA A 1 74  ? 37.930 3.155   23.294  1.00 23.15 ? 74  ALA A CB  1 
ATOM   583  N N   . ASP A 1 75  ? 37.889 -0.051  23.553  1.00 23.05 ? 75  ASP A N   1 
ATOM   584  C CA  . ASP A 1 75  ? 38.353 -1.283  24.193  1.00 21.79 ? 75  ASP A CA  1 
ATOM   585  C C   . ASP A 1 75  ? 37.196 -2.279  24.136  1.00 21.87 ? 75  ASP A C   1 
ATOM   586  O O   . ASP A 1 75  ? 36.257 -2.185  24.935  1.00 20.90 ? 75  ASP A O   1 
ATOM   587  C CB  . ASP A 1 75  ? 38.810 -1.012  25.622  1.00 24.46 ? 75  ASP A CB  1 
ATOM   588  C CG  . ASP A 1 75  ? 39.567 -2.184  26.241  1.00 24.36 ? 75  ASP A CG  1 
ATOM   589  O OD1 . ASP A 1 75  ? 40.635 -1.968  26.849  1.00 26.02 ? 75  ASP A OD1 1 
ATOM   590  O OD2 . ASP A 1 75  ? 39.061 -3.328  26.154  1.00 25.25 ? 75  ASP A OD2 1 
ATOM   591  N N   . GLY A 1 76  ? 37.270 -3.217  23.182  1.00 20.76 ? 76  GLY A N   1 
ATOM   592  C CA  . GLY A 1 76  ? 36.150 -4.119  22.936  1.00 20.07 ? 76  GLY A CA  1 
ATOM   593  C C   . GLY A 1 76  ? 35.888 -5.106  24.067  1.00 19.91 ? 76  GLY A C   1 
ATOM   594  O O   . GLY A 1 76  ? 34.733 -5.382  24.409  1.00 19.51 ? 76  GLY A O   1 
ATOM   595  N N   . THR A 1 77  ? 36.947 -5.662  24.659  1.00 19.33 ? 77  THR A N   1 
ATOM   596  C CA  . THR A 1 77  ? 36.750 -6.564  25.786  1.00 20.01 ? 77  THR A CA  1 
ATOM   597  C C   . THR A 1 77  ? 35.991 -5.866  26.911  1.00 21.70 ? 77  THR A C   1 
ATOM   598  O O   . THR A 1 77  ? 35.020 -6.399  27.465  1.00 19.75 ? 77  THR A O   1 
ATOM   599  C CB  . THR A 1 77  ? 38.112 -7.074  26.271  1.00 20.09 ? 77  THR A CB  1 
ATOM   600  O OG1 . THR A 1 77  ? 38.692 -7.891  25.244  1.00 19.64 ? 77  THR A OG1 1 
ATOM   601  C CG2 . THR A 1 77  ? 37.973 -7.902  27.565  1.00 20.85 ? 77  THR A CG2 1 
ATOM   602  N N   . GLU A 1 78  ? 36.429 -4.659  27.270  1.00 23.84 ? 78  GLU A N   1 
ATOM   603  C CA  . GLU A 1 78  ? 35.808 -3.961  28.390  1.00 22.65 ? 78  GLU A CA  1 
ATOM   604  C C   . GLU A 1 78  ? 34.359 -3.612  28.084  1.00 19.24 ? 78  GLU A C   1 
ATOM   605  O O   . GLU A 1 78  ? 33.486 -3.766  28.941  1.00 20.78 ? 78  GLU A O   1 
ATOM   606  C CB  . GLU A 1 78  ? 36.614 -2.702  28.689  1.00 22.86 ? 78  GLU A CB  1 
ATOM   607  C CG  . GLU A 1 78  ? 38.081 -2.990  28.727  1.00 23.47 ? 78  GLU A CG  1 
ATOM   608  C CD  . GLU A 1 78  ? 38.438 -3.924  29.854  1.00 28.51 ? 78  GLU A CD  1 
ATOM   609  O OE1 . GLU A 1 78  ? 37.521 -4.325  30.622  1.00 26.96 ? 78  GLU A OE1 1 
ATOM   610  O OE2 . GLU A 1 78  ? 39.637 -4.288  29.945  1.00 33.42 ? 78  GLU A OE2 1 
ATOM   611  N N   . ALA A 1 79  ? 34.095 -3.138  26.868  1.00 17.70 ? 79  ALA A N   1 
ATOM   612  C CA  . ALA A 1 79  ? 32.751 -2.728  26.508  1.00 18.59 ? 79  ALA A CA  1 
ATOM   613  C C   . ALA A 1 79  ? 31.790 -3.913  26.537  1.00 21.27 ? 79  ALA A C   1 
ATOM   614  O O   . ALA A 1 79  ? 30.682 -3.818  27.083  1.00 20.99 ? 79  ALA A O   1 
ATOM   615  C CB  . ALA A 1 79  ? 32.765 -2.045  25.145  1.00 18.71 ? 79  ALA A CB  1 
ATOM   616  N N   . CYS A 1 80  ? 32.202 -5.048  25.962  1.00 19.21 ? 80  CYS A N   1 
ATOM   617  C CA  . CYS A 1 80  ? 31.346 -6.227  25.977  1.00 18.45 ? 80  CYS A CA  1 
ATOM   618  C C   . CYS A 1 80  ? 31.102 -6.711  27.416  1.00 19.75 ? 80  CYS A C   1 
ATOM   619  O O   . CYS A 1 80  ? 29.998 -7.163  27.750  1.00 20.20 ? 80  CYS A O   1 
ATOM   620  C CB  . CYS A 1 80  ? 31.953 -7.303  25.067  1.00 16.77 ? 80  CYS A CB  1 
ATOM   621  S SG  . CYS A 1 80  ? 31.893 -6.905  23.281  1.00 14.90 ? 80  CYS A SG  1 
ATOM   622  N N   . LYS A 1 81  ? 32.111 -6.595  28.291  1.00 18.75 ? 81  LYS A N   1 
ATOM   623  C CA  . LYS A 1 81  ? 31.920 -6.907  29.706  1.00 19.46 ? 81  LYS A CA  1 
ATOM   624  C C   . LYS A 1 81  ? 30.717 -6.183  30.316  1.00 19.99 ? 81  LYS A C   1 
ATOM   625  O O   . LYS A 1 81  ? 30.136 -6.668  31.294  1.00 18.70 ? 81  LYS A O   1 
ATOM   626  C CB  . LYS A 1 81  ? 33.209 -6.629  30.515  1.00 20.00 ? 81  LYS A CB  1 
ATOM   627  C CG  . LYS A 1 81  ? 34.040 -7.881  30.828  1.00 22.32 ? 81  LYS A CG  1 
ATOM   628  C CD  . LYS A 1 81  ? 35.527 -7.696  30.546  1.00 25.67 ? 81  LYS A CD  1 
ATOM   629  C CE  . LYS A 1 81  ? 36.347 -8.902  31.040  1.00 28.87 ? 81  LYS A CE  1 
ATOM   630  N NZ  . LYS A 1 81  ? 37.801 -8.551  31.277  1.00 29.22 ? 81  LYS A NZ  1 
ATOM   631  N N   . GLU A 1 82  ? 30.330 -5.019  29.771  1.00 21.19 ? 82  GLU A N   1 
ATOM   632  C CA  . GLU A 1 82  ? 29.187 -4.302  30.343  1.00 21.37 ? 82  GLU A CA  1 
ATOM   633  C C   . GLU A 1 82  ? 27.893 -5.114  30.224  1.00 22.88 ? 82  GLU A C   1 
ATOM   634  O O   . GLU A 1 82  ? 27.037 -5.059  31.121  1.00 22.93 ? 82  GLU A O   1 
ATOM   635  C CB  . GLU A 1 82  ? 29.024 -2.932  29.686  1.00 20.24 ? 82  GLU A CB  1 
ATOM   636  C CG  . GLU A 1 82  ? 30.186 -1.969  29.901  1.00 21.62 ? 82  GLU A CG  1 
ATOM   637  C CD  . GLU A 1 82  ? 29.939 -0.609  29.224  1.00 21.16 ? 82  GLU A CD  1 
ATOM   638  O OE1 . GLU A 1 82  ? 28.767 -0.174  29.172  1.00 20.83 ? 82  GLU A OE1 1 
ATOM   639  O OE2 . GLU A 1 82  ? 30.911 -0.014  28.700  1.00 18.87 ? 82  GLU A OE2 1 
ATOM   640  N N   . LEU A 1 83  ? 27.745 -5.878  29.129  1.00 24.35 ? 83  LEU A N   1 
ATOM   641  C CA  . LEU A 1 83  ? 26.575 -6.701  28.836  1.00 20.91 ? 83  LEU A CA  1 
ATOM   642  C C   . LEU A 1 83  ? 26.705 -8.135  29.361  1.00 22.59 ? 83  LEU A C   1 
ATOM   643  O O   . LEU A 1 83  ? 25.891 -8.994  28.996  1.00 23.78 ? 83  LEU A O   1 
ATOM   644  C CB  . LEU A 1 83  ? 26.354 -6.748  27.322  1.00 21.24 ? 83  LEU A CB  1 
ATOM   645  C CG  . LEU A 1 83  ? 25.956 -5.489  26.546  1.00 20.75 ? 83  LEU A CG  1 
ATOM   646  C CD1 . LEU A 1 83  ? 27.213 -4.704  26.236  1.00 22.52 ? 83  LEU A CD1 1 
ATOM   647  C CD2 . LEU A 1 83  ? 25.217 -5.835  25.268  1.00 19.23 ? 83  LEU A CD2 1 
ATOM   648  N N   . GLY A 1 84  ? 27.714 -8.420  30.186  1.00 22.36 ? 84  GLY A N   1 
ATOM   649  C CA  . GLY A 1 84  ? 27.964 -9.787  30.608  1.00 20.99 ? 84  GLY A CA  1 
ATOM   650  C C   . GLY A 1 84  ? 28.472 -10.699 29.507  1.00 22.42 ? 84  GLY A C   1 
ATOM   651  O O   . GLY A 1 84  ? 28.232 -11.904 29.568  1.00 24.12 ? 84  GLY A O   1 
ATOM   652  N N   . ILE A 1 85  ? 29.162 -10.158 28.499  1.00 19.44 ? 85  ILE A N   1 
ATOM   653  C CA  . ILE A 1 85  ? 29.700 -10.925 27.380  1.00 20.41 ? 85  ILE A CA  1 
ATOM   654  C C   . ILE A 1 85  ? 31.232 -10.881 27.418  1.00 21.58 ? 85  ILE A C   1 
ATOM   655  O O   . ILE A 1 85  ? 31.843 -9.805  27.552  1.00 19.06 ? 85  ILE A O   1 
ATOM   656  C CB  . ILE A 1 85  ? 29.134 -10.423 26.033  1.00 21.69 ? 85  ILE A CB  1 
ATOM   657  C CG1 . ILE A 1 85  ? 27.598 -10.564 25.998  1.00 17.17 ? 85  ILE A CG1 1 
ATOM   658  C CG2 . ILE A 1 85  ? 29.822 -11.106 24.824  1.00 19.65 ? 85  ILE A CG2 1 
ATOM   659  C CD1 . ILE A 1 85  ? 26.937 -9.973  24.768  1.00 15.82 ? 85  ILE A CD1 1 
ATOM   660  N N   . GLY A 1 86  ? 31.851 -12.049 27.302  1.00 22.80 ? 86  GLY A N   1 
ATOM   661  C CA  . GLY A 1 86  ? 33.299 -12.141 27.273  1.00 21.30 ? 86  GLY A CA  1 
ATOM   662  C C   . GLY A 1 86  ? 33.743 -13.556 27.588  1.00 20.14 ? 86  GLY A C   1 
ATOM   663  O O   . GLY A 1 86  ? 32.929 -14.453 27.791  1.00 19.76 ? 86  GLY A O   1 
ATOM   664  N N   . GLY A 1 87  ? 35.064 -13.742 27.613  1.00 17.05 ? 87  GLY A N   1 
ATOM   665  C CA  . GLY A 1 87  ? 35.644 -14.990 28.049  1.00 16.23 ? 87  GLY A CA  1 
ATOM   666  C C   . GLY A 1 87  ? 36.495 -15.638 26.969  1.00 16.54 ? 87  GLY A C   1 
ATOM   667  O O   . GLY A 1 87  ? 37.069 -14.963 26.103  1.00 16.05 ? 87  GLY A O   1 
ATOM   668  N N   . LEU A 1 88  ? 36.551 -16.962 27.027  1.00 16.19 ? 88  LEU A N   1 
ATOM   669  C CA  . LEU A 1 88  ? 37.505 -17.740 26.244  1.00 17.32 ? 88  LEU A CA  1 
ATOM   670  C C   . LEU A 1 88  ? 37.485 -17.332 24.785  1.00 16.45 ? 88  LEU A C   1 
ATOM   671  O O   . LEU A 1 88  ? 36.436 -17.359 24.126  1.00 15.68 ? 88  LEU A O   1 
ATOM   672  C CB  . LEU A 1 88  ? 37.163 -19.236 26.340  1.00 18.45 ? 88  LEU A CB  1 
ATOM   673  C CG  . LEU A 1 88  ? 38.196 -20.285 25.865  1.00 16.73 ? 88  LEU A CG  1 
ATOM   674  C CD1 . LEU A 1 88  ? 39.519 -20.154 26.626  1.00 17.30 ? 88  LEU A CD1 1 
ATOM   675  C CD2 . LEU A 1 88  ? 37.637 -21.705 25.954  1.00 15.69 ? 88  LEU A CD2 1 
ATOM   676  N N   . GLN A 1 89  ? 38.671 -16.995 24.272  1.00 16.47 ? 89  GLN A N   1 
ATOM   677  C CA  . GLN A 1 89  ? 38.925 -16.703 22.856  1.00 15.84 ? 89  GLN A CA  1 
ATOM   678  C C   . GLN A 1 89  ? 38.337 -15.362 22.400  1.00 14.96 ? 89  GLN A C   1 
ATOM   679  O O   . GLN A 1 89  ? 38.285 -15.081 21.187  1.00 14.43 ? 89  GLN A O   1 
ATOM   680  C CB  . GLN A 1 89  ? 38.551 -17.874 21.924  1.00 15.83 ? 89  GLN A CB  1 
ATOM   681  C CG  . GLN A 1 89  ? 39.610 -19.008 21.902  1.00 15.60 ? 89  GLN A CG  1 
ATOM   682  C CD  . GLN A 1 89  ? 40.976 -18.531 21.434  1.00 15.92 ? 89  GLN A CD  1 
ATOM   683  O OE1 . GLN A 1 89  ? 41.182 -18.237 20.253  1.00 16.16 ? 89  GLN A OE1 1 
ATOM   684  N NE2 . GLN A 1 89  ? 41.896 -18.399 22.368  1.00 15.37 ? 89  GLN A NE2 1 
ATOM   685  N N   . GLY A 1 90  ? 37.880 -14.538 23.344  1.00 15.75 ? 90  GLY A N   1 
ATOM   686  C CA  . GLY A 1 90  ? 37.626 -13.128 23.120  1.00 14.50 ? 90  GLY A CA  1 
ATOM   687  C C   . GLY A 1 90  ? 38.143 -12.334 24.302  1.00 15.50 ? 90  GLY A C   1 
ATOM   688  O O   . GLY A 1 90  ? 37.521 -11.350 24.702  1.00 17.61 ? 90  GLY A O   1 
ATOM   689  N N   . GLU A 1 91  ? 39.262 -12.774 24.900  1.00 15.37 ? 91  GLU A N   1 
ATOM   690  C CA  . GLU A 1 91  ? 39.895 -12.034 25.988  1.00 14.52 ? 91  GLU A CA  1 
ATOM   691  C C   . GLU A 1 91  ? 40.458 -10.690 25.531  1.00 15.00 ? 91  GLU A C   1 
ATOM   692  O O   . GLU A 1 91  ? 40.630 -9.782  26.361  1.00 15.62 ? 91  GLU A O   1 
ATOM   693  C CB  . GLU A 1 91  ? 41.053 -12.837 26.581  1.00 15.26 ? 91  GLU A CB  1 
ATOM   694  C CG  . GLU A 1 91  ? 40.686 -14.195 27.130  1.00 15.01 ? 91  GLU A CG  1 
ATOM   695  C CD  . GLU A 1 91  ? 40.743 -15.275 26.057  1.00 14.98 ? 91  GLU A CD  1 
ATOM   696  O OE1 . GLU A 1 91  ? 40.925 -14.948 24.875  1.00 14.13 ? 91  GLU A OE1 1 
ATOM   697  O OE2 . GLU A 1 91  ? 40.628 -16.463 26.412  1.00 16.36 ? 91  GLU A OE2 1 
ATOM   698  N N   . ASP A 1 92  ? 40.750 -10.557 24.236  1.00 13.82 ? 92  ASP A N   1 
ATOM   699  C CA  . ASP A 1 92  ? 41.184 -9.303  23.633  1.00 15.44 ? 92  ASP A CA  1 
ATOM   700  C C   . ASP A 1 92  ? 40.359 -9.133  22.357  1.00 15.79 ? 92  ASP A C   1 
ATOM   701  O O   . ASP A 1 92  ? 40.610 -9.772  21.333  1.00 18.12 ? 92  ASP A O   1 
ATOM   702  C CB  . ASP A 1 92  ? 42.689 -9.322  23.333  1.00 15.91 ? 92  ASP A CB  1 
ATOM   703  C CG  . ASP A 1 92  ? 43.544 -9.347  24.583  1.00 17.39 ? 92  ASP A CG  1 
ATOM   704  O OD1 . ASP A 1 92  ? 43.876 -8.246  25.099  1.00 16.34 ? 92  ASP A OD1 1 
ATOM   705  O OD2 . ASP A 1 92  ? 43.889 -10.471 25.058  1.00 16.40 ? 92  ASP A OD2 1 
ATOM   706  N N   . MET A 1 93  ? 39.356 -8.276  22.412  1.00 16.79 ? 93  MET A N   1 
ATOM   707  C CA  . MET A 1 93  ? 38.496 -8.001  21.276  1.00 16.39 ? 93  MET A CA  1 
ATOM   708  C C   . MET A 1 93  ? 38.717 -6.569  20.828  1.00 16.17 ? 93  MET A C   1 
ATOM   709  O O   . MET A 1 93  ? 38.811 -5.657  21.659  1.00 16.99 ? 93  MET A O   1 
ATOM   710  C CB  . MET A 1 93  ? 37.036 -8.240  21.660  1.00 17.24 ? 93  MET A CB  1 
ATOM   711  C CG  . MET A 1 93  ? 36.657 -9.698  21.582  1.00 18.49 ? 93  MET A CG  1 
ATOM   712  S SD  . MET A 1 93  ? 34.913 -10.035 21.921  1.00 22.48 ? 93  MET A SD  1 
ATOM   713  C CE  . MET A 1 93  ? 34.816 -9.431  23.624  1.00 17.50 ? 93  MET A CE  1 
ATOM   714  N N   . MET A 1 94  ? 38.839 -6.393  19.519  1.00 16.50 ? 94  MET A N   1 
ATOM   715  C CA  . MET A 1 94  ? 38.895 -5.085  18.890  1.00 17.98 ? 94  MET A CA  1 
ATOM   716  C C   . MET A 1 94  ? 37.822 -5.026  17.831  1.00 15.66 ? 94  MET A C   1 
ATOM   717  O O   . MET A 1 94  ? 37.875 -5.768  16.844  1.00 15.75 ? 94  MET A O   1 
ATOM   718  C CB  . MET A 1 94  ? 40.246 -4.802  18.233  1.00 18.37 ? 94  MET A CB  1 
ATOM   719  C CG  . MET A 1 94  ? 40.346 -3.366  17.759  1.00 20.79 ? 94  MET A CG  1 
ATOM   720  S SD  . MET A 1 94  ? 42.002 -2.853  17.365  1.00 23.32 ? 94  MET A SD  1 
ATOM   721  C CE  . MET A 1 94  ? 41.681 -1.568  16.129  1.00 24.92 ? 94  MET A CE  1 
ATOM   722  N N   . TRP A 1 95  ? 36.877 -4.112  18.023  1.00 17.22 ? 95  TRP A N   1 
ATOM   723  C CA  . TRP A 1 95  ? 35.766 -3.927  17.107  1.00 17.50 ? 95  TRP A CA  1 
ATOM   724  C C   . TRP A 1 95  ? 36.094 -2.794  16.145  1.00 17.52 ? 95  TRP A C   1 
ATOM   725  O O   . TRP A 1 95  ? 36.628 -1.760  16.560  1.00 19.05 ? 95  TRP A O   1 
ATOM   726  C CB  . TRP A 1 95  ? 34.494 -3.612  17.895  1.00 17.55 ? 95  TRP A CB  1 
ATOM   727  C CG  . TRP A 1 95  ? 33.934 -4.804  18.655  1.00 17.29 ? 95  TRP A CG  1 
ATOM   728  C CD1 . TRP A 1 95  ? 34.508 -5.448  19.721  1.00 16.67 ? 95  TRP A CD1 1 
ATOM   729  C CD2 . TRP A 1 95  ? 32.707 -5.497  18.384  1.00 17.08 ? 95  TRP A CD2 1 
ATOM   730  N NE1 . TRP A 1 95  ? 33.703 -6.482  20.141  1.00 16.99 ? 95  TRP A NE1 1 
ATOM   731  C CE2 . TRP A 1 95  ? 32.598 -6.542  19.335  1.00 15.74 ? 95  TRP A CE2 1 
ATOM   732  C CE3 . TRP A 1 95  ? 31.689 -5.337  17.431  1.00 17.31 ? 95  TRP A CE3 1 
ATOM   733  C CZ2 . TRP A 1 95  ? 31.496 -7.420  19.374  1.00 17.05 ? 95  TRP A CZ2 1 
ATOM   734  C CZ3 . TRP A 1 95  ? 30.587 -6.212  17.479  1.00 16.39 ? 95  TRP A CZ3 1 
ATOM   735  C CH2 . TRP A 1 95  ? 30.508 -7.233  18.446  1.00 16.46 ? 95  TRP A CH2 1 
ATOM   736  N N   . VAL A 1 96  ? 35.779 -3.004  14.863  1.00 16.81 ? 96  VAL A N   1 
ATOM   737  C CA  . VAL A 1 96  ? 36.147 -2.107  13.771  1.00 16.62 ? 96  VAL A CA  1 
ATOM   738  C C   . VAL A 1 96  ? 34.895 -1.772  12.973  1.00 18.88 ? 96  VAL A C   1 
ATOM   739  O O   . VAL A 1 96  ? 34.183 -2.675  12.509  1.00 18.35 ? 96  VAL A O   1 
ATOM   740  C CB  . VAL A 1 96  ? 37.243 -2.705  12.866  1.00 17.41 ? 96  VAL A CB  1 
ATOM   741  C CG1 . VAL A 1 96  ? 38.549 -2.854  13.635  1.00 15.46 ? 96  VAL A CG1 1 
ATOM   742  C CG2 . VAL A 1 96  ? 36.798 -4.067  12.280  1.00 17.05 ? 96  VAL A CG2 1 
ATOM   743  N N   . GLU A 1 97  ? 34.658 -0.474  12.777  1.00 18.52 ? 97  GLU A N   1 
ATOM   744  C CA  . GLU A 1 97  ? 33.380 0.044   12.303  1.00 18.68 ? 97  GLU A CA  1 
ATOM   745  C C   . GLU A 1 97  ? 33.362 0.171   10.774  1.00 20.33 ? 97  GLU A C   1 
ATOM   746  O O   . GLU A 1 97  ? 34.218 0.855   10.183  1.00 19.42 ? 97  GLU A O   1 
ATOM   747  C CB  . GLU A 1 97  ? 33.135 1.390   12.992  1.00 21.53 ? 97  GLU A CB  1 
ATOM   748  C CG  . GLU A 1 97  ? 31.812 2.093   12.681  1.00 23.42 ? 97  GLU A CG  1 
ATOM   749  C CD  . GLU A 1 97  ? 31.786 3.560   13.167  1.00 25.25 ? 97  GLU A CD  1 
ATOM   750  O OE1 . GLU A 1 97  ? 32.778 4.031   13.798  1.00 28.45 ? 97  GLU A OE1 1 
ATOM   751  O OE2 . GLU A 1 97  ? 30.776 4.244   12.901  1.00 23.98 ? 97  GLU A OE2 1 
ATOM   752  N N   . ASN A 1 98  ? 32.391 -0.497  10.140  1.00 17.66 ? 98  ASN A N   1 
ATOM   753  C CA  . ASN A 1 98  ? 32.088 -0.282  8.731   1.00 17.80 ? 98  ASN A CA  1 
ATOM   754  C C   . ASN A 1 98  ? 31.509 1.116   8.527   1.00 20.32 ? 98  ASN A C   1 
ATOM   755  O O   . ASN A 1 98  ? 30.649 1.567   9.295   1.00 20.52 ? 98  ASN A O   1 
ATOM   756  C CB  . ASN A 1 98  ? 31.050 -1.296  8.255   1.00 18.03 ? 98  ASN A CB  1 
ATOM   757  C CG  . ASN A 1 98  ? 31.661 -2.624  7.921   1.00 18.11 ? 98  ASN A CG  1 
ATOM   758  O OD1 . ASN A 1 98  ? 32.880 -2.748  7.842   1.00 17.48 ? 98  ASN A OD1 1 
ATOM   759  N ND2 . ASN A 1 98  ? 30.821 -3.624  7.688   1.00 17.58 ? 98  ASN A ND2 1 
ATOM   760  N N   . THR A 1 99  ? 31.978 1.798   7.481   1.00 20.12 ? 99  THR A N   1 
ATOM   761  C CA  . THR A 1 99  ? 31.467 3.129   7.154   1.00 22.92 ? 99  THR A CA  1 
ATOM   762  C C   . THR A 1 99  ? 31.083 3.240   5.683   1.00 22.11 ? 99  THR A C   1 
ATOM   763  O O   . THR A 1 99  ? 31.010 2.236   4.953   1.00 21.49 ? 99  THR A O   1 
ATOM   764  C CB  . THR A 1 99  ? 32.490 4.215   7.500   1.00 21.55 ? 99  THR A CB  1 
ATOM   765  O OG1 . THR A 1 99  ? 33.641 4.102   6.643   1.00 19.68 ? 99  THR A OG1 1 
ATOM   766  C CG2 . THR A 1 99  ? 32.907 4.073   8.962   1.00 22.84 ? 99  THR A CG2 1 
ATOM   767  N N   . ASP A 1 100 ? 30.819 4.463   5.242   1.00 22.06 ? 100 ASP A N   1 
ATOM   768  C CA  . ASP A 1 100 ? 30.582 4.665   3.825   1.00 23.98 ? 100 ASP A CA  1 
ATOM   769  C C   . ASP A 1 100 ? 31.882 4.613   3.030   1.00 21.90 ? 100 ASP A C   1 
ATOM   770  O O   . ASP A 1 100 ? 31.849 4.381   1.815   1.00 20.03 ? 100 ASP A O   1 
ATOM   771  C CB  . ASP A 1 100 ? 29.888 6.014   3.621   1.00 26.78 ? 100 ASP A CB  1 
ATOM   772  C CG  . ASP A 1 100 ? 28.500 6.040   4.222   1.00 28.87 ? 100 ASP A CG  1 
ATOM   773  O OD1 . ASP A 1 100 ? 27.941 4.950   4.437   1.00 30.66 ? 100 ASP A OD1 1 
ATOM   774  O OD2 . ASP A 1 100 ? 27.974 7.143   4.509   1.00 36.55 ? 100 ASP A OD2 1 
ATOM   775  N N   . GLU A 1 101 ? 33.025 4.795   3.701   1.00 22.10 ? 101 GLU A N   1 
ATOM   776  C CA  . GLU A 1 101 ? 34.326 4.852   3.041   1.00 23.33 ? 101 GLU A CA  1 
ATOM   777  C C   . GLU A 1 101 ? 35.176 3.603   3.258   1.00 22.56 ? 101 GLU A C   1 
ATOM   778  O O   . GLU A 1 101 ? 36.137 3.389   2.505   1.00 21.21 ? 101 GLU A O   1 
ATOM   779  C CB  . GLU A 1 101 ? 35.120 6.073   3.542   1.00 24.30 ? 101 GLU A CB  1 
ATOM   780  C CG  . GLU A 1 101 ? 34.424 7.442   3.318   1.00 25.51 ? 101 GLU A CG  1 
ATOM   781  C CD  . GLU A 1 101 ? 33.158 7.606   4.180   1.00 29.74 ? 101 GLU A CD  1 
ATOM   782  O OE1 . GLU A 1 101 ? 33.245 7.412   5.416   1.00 27.13 ? 101 GLU A OE1 1 
ATOM   783  O OE2 . GLU A 1 101 ? 32.064 7.900   3.624   1.00 31.21 ? 101 GLU A OE2 1 
ATOM   784  N N   . VAL A 1 102 ? 34.844 2.776   4.257   1.00 22.54 ? 102 VAL A N   1 
ATOM   785  C CA  . VAL A 1 102 ? 35.661 1.625   4.640   1.00 21.86 ? 102 VAL A CA  1 
ATOM   786  C C   . VAL A 1 102 ? 34.759 0.423   4.839   1.00 19.87 ? 102 VAL A C   1 
ATOM   787  O O   . VAL A 1 102 ? 33.746 0.507   5.542   1.00 19.08 ? 102 VAL A O   1 
ATOM   788  C CB  . VAL A 1 102 ? 36.468 1.876   5.933   1.00 21.35 ? 102 VAL A CB  1 
ATOM   789  C CG1 . VAL A 1 102 ? 37.282 0.634   6.277   1.00 19.87 ? 102 VAL A CG1 1 
ATOM   790  C CG2 . VAL A 1 102 ? 37.387 3.120   5.807   1.00 20.35 ? 102 VAL A CG2 1 
ATOM   791  N N   . HIS A 1 103 ? 35.144 -0.704  4.252   1.00 20.76 ? 103 HIS A N   1 
ATOM   792  C CA  . HIS A 1 103 ? 34.574 -1.995  4.623   1.00 20.02 ? 103 HIS A CA  1 
ATOM   793  C C   . HIS A 1 103 ? 35.631 -2.921  5.234   1.00 18.39 ? 103 HIS A C   1 
ATOM   794  O O   . HIS A 1 103 ? 36.761 -3.011  4.735   1.00 17.95 ? 103 HIS A O   1 
ATOM   795  C CB  . HIS A 1 103 ? 33.939 -2.699  3.449   1.00 18.70 ? 103 HIS A CB  1 
ATOM   796  C CG  . HIS A 1 103 ? 33.247 -3.945  3.860   1.00 19.12 ? 103 HIS A CG  1 
ATOM   797  N ND1 . HIS A 1 103 ? 32.031 -3.929  4.507   1.00 18.43 ? 103 HIS A ND1 1 
ATOM   798  C CD2 . HIS A 1 103 ? 33.646 -5.238  3.823   1.00 18.85 ? 103 HIS A CD2 1 
ATOM   799  C CE1 . HIS A 1 103 ? 31.679 -5.167  4.797   1.00 18.92 ? 103 HIS A CE1 1 
ATOM   800  N NE2 . HIS A 1 103 ? 32.642 -5.979  4.392   1.00 19.80 ? 103 HIS A NE2 1 
ATOM   801  N N   . HIS A 1 104 ? 35.253 -3.625  6.298   1.00 16.91 ? 104 HIS A N   1 
ATOM   802  C CA  . HIS A 1 104 ? 36.148 -4.516  7.031   1.00 18.08 ? 104 HIS A CA  1 
ATOM   803  C C   . HIS A 1 104 ? 35.729 -5.976  6.853   1.00 17.78 ? 104 HIS A C   1 
ATOM   804  O O   . HIS A 1 104 ? 34.542 -6.312  6.882   1.00 16.19 ? 104 HIS A O   1 
ATOM   805  C CB  . HIS A 1 104 ? 36.146 -4.212  8.532   1.00 18.44 ? 104 HIS A CB  1 
ATOM   806  C CG  . HIS A 1 104 ? 36.515 -2.800  8.884   1.00 19.52 ? 104 HIS A CG  1 
ATOM   807  N ND1 . HIS A 1 104 ? 37.826 -2.376  8.997   1.00 18.99 ? 104 HIS A ND1 1 
ATOM   808  C CD2 . HIS A 1 104 ? 35.744 -1.728  9.206   1.00 19.35 ? 104 HIS A CD2 1 
ATOM   809  C CE1 . HIS A 1 104 ? 37.847 -1.106  9.370   1.00 19.05 ? 104 HIS A CE1 1 
ATOM   810  N NE2 . HIS A 1 104 ? 36.597 -0.685  9.489   1.00 18.82 ? 104 HIS A NE2 1 
ATOM   811  N N   . VAL A 1 105 ? 36.720 -6.850  6.702   1.00 18.56 ? 105 VAL A N   1 
ATOM   812  C CA  . VAL A 1 105 ? 36.497 -8.290  6.659   1.00 16.65 ? 105 VAL A CA  1 
ATOM   813  C C   . VAL A 1 105 ? 37.592 -8.972  7.452   1.00 16.63 ? 105 VAL A C   1 
ATOM   814  O O   . VAL A 1 105 ? 38.735 -8.506  7.507   1.00 15.78 ? 105 VAL A O   1 
ATOM   815  C CB  . VAL A 1 105 ? 36.338 -8.852  5.224   1.00 18.17 ? 105 VAL A CB  1 
ATOM   816  C CG1 . VAL A 1 105 ? 37.632 -8.734  4.430   1.00 18.69 ? 105 VAL A CG1 1 
ATOM   817  C CG2 . VAL A 1 105 ? 35.914 -10.305 5.292   1.00 16.21 ? 105 VAL A CG2 1 
ATOM   818  N N   . VAL A 1 106 ? 37.237 -10.085 8.078   1.00 16.34 ? 106 VAL A N   1 
ATOM   819  C CA  . VAL A 1 106 ? 38.122 -10.734 9.038   1.00 17.61 ? 106 VAL A CA  1 
ATOM   820  C C   . VAL A 1 106 ? 38.422 -12.175 8.608   1.00 16.27 ? 106 VAL A C   1 
ATOM   821  O O   . VAL A 1 106 ? 37.570 -12.878 8.042   1.00 16.26 ? 106 VAL A O   1 
ATOM   822  C CB  . VAL A 1 106 ? 37.568 -10.630 10.475  1.00 15.71 ? 106 VAL A CB  1 
ATOM   823  C CG1 . VAL A 1 106 ? 38.558 -11.186 11.490  1.00 14.74 ? 106 VAL A CG1 1 
ATOM   824  C CG2 . VAL A 1 106 ? 37.200 -9.164  10.790  1.00 14.85 ? 106 VAL A CG2 1 
ATOM   825  N N   . VAL A 1 107 ? 39.662 -12.598 8.858   1.00 16.89 ? 107 VAL A N   1 
ATOM   826  C CA  . VAL A 1 107 ? 40.131 -13.925 8.482   1.00 14.91 ? 107 VAL A CA  1 
ATOM   827  C C   . VAL A 1 107 ? 41.201 -14.348 9.483   1.00 15.04 ? 107 VAL A C   1 
ATOM   828  O O   . VAL A 1 107 ? 41.770 -13.521 10.198  1.00 15.14 ? 107 VAL A O   1 
ATOM   829  C CB  . VAL A 1 107 ? 40.638 -13.923 7.016   1.00 17.13 ? 107 VAL A CB  1 
ATOM   830  C CG1 . VAL A 1 107 ? 41.862 -13.004 6.833   1.00 15.81 ? 107 VAL A CG1 1 
ATOM   831  C CG2 . VAL A 1 107 ? 40.918 -15.351 6.513   1.00 16.76 ? 107 VAL A CG2 1 
ATOM   832  N N   . CYS A 1 108 ? 41.434 -15.653 9.578   1.00 12.70 ? 108 CYS A N   1 
ATOM   833  C CA  . CYS A 1 108 ? 42.627 -16.204 10.207  1.00 13.60 ? 108 CYS A CA  1 
ATOM   834  C C   . CYS A 1 108 ? 43.341 -17.101 9.180   1.00 14.71 ? 108 CYS A C   1 
ATOM   835  O O   . CYS A 1 108 ? 43.070 -18.301 9.106   1.00 15.72 ? 108 CYS A O   1 
ATOM   836  C CB  . CYS A 1 108 ? 42.286 -16.971 11.463  1.00 14.86 ? 108 CYS A CB  1 
ATOM   837  S SG  . CYS A 1 108 ? 43.765 -17.480 12.385  1.00 16.94 ? 108 CYS A SG  1 
ATOM   838  N N   . THR A 1 109 ? 44.246 -16.517 8.376   1.00 14.18 ? 109 THR A N   1 
ATOM   839  C CA  . THR A 1 109 ? 44.944 -17.297 7.351   1.00 13.14 ? 109 THR A CA  1 
ATOM   840  C C   . THR A 1 109 ? 45.783 -18.438 7.940   1.00 14.32 ? 109 THR A C   1 
ATOM   841  O O   . THR A 1 109 ? 45.980 -19.463 7.266   1.00 13.79 ? 109 THR A O   1 
ATOM   842  C CB  . THR A 1 109 ? 45.805 -16.389 6.453   1.00 14.96 ? 109 THR A CB  1 
ATOM   843  O OG1 . THR A 1 109 ? 46.920 -15.842 7.192   1.00 13.78 ? 109 THR A OG1 1 
ATOM   844  C CG2 . THR A 1 109 ? 44.978 -15.241 5.881   1.00 15.74 ? 109 THR A CG2 1 
ATOM   845  N N   . LEU A 1 110 ? 46.302 -18.280 9.164   1.00 13.28 ? 110 LEU A N   1 
ATOM   846  C CA  . LEU A 1 110 ? 47.202 -19.286 9.756   1.00 14.69 ? 110 LEU A CA  1 
ATOM   847  C C   . LEU A 1 110 ? 46.506 -20.461 10.457  1.00 15.54 ? 110 LEU A C   1 
ATOM   848  O O   . LEU A 1 110 ? 47.076 -21.555 10.563  1.00 15.49 ? 110 LEU A O   1 
ATOM   849  C CB  . LEU A 1 110 ? 48.284 -18.672 10.667  1.00 12.90 ? 110 LEU A CB  1 
ATOM   850  C CG  . LEU A 1 110 ? 49.352 -17.732 10.100  1.00 12.21 ? 110 LEU A CG  1 
ATOM   851  C CD1 . LEU A 1 110 ? 50.078 -17.045 11.228  1.00 13.91 ? 110 LEU A CD1 1 
ATOM   852  C CD2 . LEU A 1 110 ? 50.337 -18.493 9.268   1.00 13.41 ? 110 LEU A CD2 1 
ATOM   853  N N   . CYS A 1 111 ? 45.289 -20.241 10.952  1.00 16.11 ? 111 CYS A N   1 
ATOM   854  C CA  . CYS A 1 111 ? 44.540 -21.336 11.537  1.00 16.96 ? 111 CYS A CA  1 
ATOM   855  C C   . CYS A 1 111 ? 43.043 -21.154 11.449  1.00 15.08 ? 111 CYS A C   1 
ATOM   856  O O   . CYS A 1 111 ? 42.442 -21.221 10.381  1.00 19.45 ? 111 CYS A O   1 
ATOM   857  C CB  . CYS A 1 111 ? 44.940 -21.726 12.970  1.00 17.32 ? 111 CYS A CB  1 
ATOM   858  S SG  . CYS A 1 111 ? 45.125 -20.318 14.003  1.00 16.60 ? 111 CYS A SG  1 
ATOM   859  N N   . ALA A 1 112 ? 42.431 -20.935 12.603  1.00 16.28 ? 112 ALA A N   1 
ATOM   860  C CA  . ALA A 1 112 ? 40.976 -20.825 12.672  1.00 17.70 ? 112 ALA A CA  1 
ATOM   861  C C   . ALA A 1 112 ? 40.466 -19.891 13.779  1.00 15.56 ? 112 ALA A C   1 
ATOM   862  O O   . ALA A 1 112 ? 39.308 -20.014 14.203  1.00 15.16 ? 112 ALA A O   1 
ATOM   863  C CB  . ALA A 1 112 ? 40.363 -22.211 12.835  1.00 16.26 ? 112 ALA A CB  1 
ATOM   864  N N   A CYS A 1 113 ? 41.332 -18.979 14.237  0.23 16.03 ? 113 CYS A N   1 
ATOM   865  N N   B CYS A 1 113 ? 41.303 -18.964 14.235  0.77 15.96 ? 113 CYS A N   1 
ATOM   866  C CA  A CYS A 1 113 ? 41.012 -18.028 15.314  0.23 15.76 ? 113 CYS A CA  1 
ATOM   867  C CA  B CYS A 1 113 ? 40.937 -18.164 15.401  0.77 15.74 ? 113 CYS A CA  1 
ATOM   868  C C   A CYS A 1 113 ? 39.721 -17.253 15.075  0.23 14.72 ? 113 CYS A C   1 
ATOM   869  C C   B CYS A 1 113 ? 39.789 -17.193 15.124  0.77 14.61 ? 113 CYS A C   1 
ATOM   870  O O   A CYS A 1 113 ? 39.428 -16.843 13.952  0.23 14.50 ? 113 CYS A O   1 
ATOM   871  O O   B CYS A 1 113 ? 39.654 -16.625 14.038  0.77 14.14 ? 113 CYS A O   1 
ATOM   872  C CB  A CYS A 1 113 ? 42.158 -17.031 15.549  0.23 16.57 ? 113 CYS A CB  1 
ATOM   873  C CB  B CYS A 1 113 ? 42.144 -17.461 16.021  0.77 16.84 ? 113 CYS A CB  1 
ATOM   874  S SG  A CYS A 1 113 ? 43.712 -17.846 15.992  0.23 17.71 ? 113 CYS A SG  1 
ATOM   875  S SG  B CYS A 1 113 ? 42.878 -16.311 14.850  0.77 16.90 ? 113 CYS A SG  1 
ATOM   876  N N   . TYR A 1 114 ? 38.966 -17.026 16.146  1.00 15.35 ? 114 TYR A N   1 
ATOM   877  C CA  . TYR A 1 114 ? 37.628 -16.482 15.989  1.00 15.74 ? 114 TYR A CA  1 
ATOM   878  C C   . TYR A 1 114 ? 37.151 -16.045 17.372  1.00 15.55 ? 114 TYR A C   1 
ATOM   879  O O   . TYR A 1 114 ? 37.478 -16.708 18.361  1.00 13.54 ? 114 TYR A O   1 
ATOM   880  C CB  . TYR A 1 114 ? 36.762 -17.630 15.444  1.00 16.88 ? 114 TYR A CB  1 
ATOM   881  C CG  . TYR A 1 114 ? 35.406 -17.318 14.845  1.00 15.16 ? 114 TYR A CG  1 
ATOM   882  C CD1 . TYR A 1 114 ? 35.300 -16.865 13.546  1.00 14.20 ? 114 TYR A CD1 1 
ATOM   883  C CD2 . TYR A 1 114 ? 34.232 -17.585 15.550  1.00 15.06 ? 114 TYR A CD2 1 
ATOM   884  C CE1 . TYR A 1 114 ? 34.058 -16.646 12.970  1.00 16.34 ? 114 TYR A CE1 1 
ATOM   885  C CE2 . TYR A 1 114 ? 32.984 -17.352 14.982  1.00 13.99 ? 114 TYR A CE2 1 
ATOM   886  C CZ  . TYR A 1 114 ? 32.903 -16.880 13.705  1.00 14.72 ? 114 TYR A CZ  1 
ATOM   887  O OH  . TYR A 1 114 ? 31.682 -16.658 13.120  1.00 14.51 ? 114 TYR A OH  1 
ATOM   888  N N   . PRO A 1 115 ? 36.406 -14.901 17.445  1.00 13.98 ? 115 PRO A N   1 
ATOM   889  C CA  . PRO A 1 115 ? 35.944 -14.398 18.745  1.00 14.76 ? 115 PRO A CA  1 
ATOM   890  C C   . PRO A 1 115 ? 34.789 -15.186 19.349  1.00 15.35 ? 115 PRO A C   1 
ATOM   891  O O   . PRO A 1 115 ? 33.632 -14.771 19.252  1.00 15.63 ? 115 PRO A O   1 
ATOM   892  C CB  . PRO A 1 115 ? 35.539 -12.955 18.420  1.00 14.42 ? 115 PRO A CB  1 
ATOM   893  C CG  . PRO A 1 115 ? 35.047 -13.041 17.028  1.00 15.73 ? 115 PRO A CG  1 
ATOM   894  C CD  . PRO A 1 115 ? 36.055 -13.965 16.358  1.00 17.10 ? 115 PRO A CD  1 
ATOM   895  N N   . TRP A 1 116 ? 35.098 -16.310 19.996  1.00 15.31 ? 116 TRP A N   1 
ATOM   896  C CA  . TRP A 1 116 ? 34.056 -17.186 20.536  1.00 14.95 ? 116 TRP A CA  1 
ATOM   897  C C   . TRP A 1 116 ? 32.983 -16.491 21.374  1.00 15.74 ? 116 TRP A C   1 
ATOM   898  O O   . TRP A 1 116 ? 31.804 -16.854 21.215  1.00 16.74 ? 116 TRP A O   1 
ATOM   899  C CB  . TRP A 1 116 ? 34.684 -18.355 21.311  1.00 15.40 ? 116 TRP A CB  1 
ATOM   900  C CG  . TRP A 1 116 ? 35.491 -19.342 20.462  1.00 15.59 ? 116 TRP A CG  1 
ATOM   901  C CD1 . TRP A 1 116 ? 35.689 -19.314 19.105  1.00 15.85 ? 116 TRP A CD1 1 
ATOM   902  C CD2 . TRP A 1 116 ? 36.142 -20.533 20.931  1.00 14.71 ? 116 TRP A CD2 1 
ATOM   903  N NE1 . TRP A 1 116 ? 36.446 -20.406 18.704  1.00 15.35 ? 116 TRP A NE1 1 
ATOM   904  C CE2 . TRP A 1 116 ? 36.725 -21.168 19.808  1.00 14.25 ? 116 TRP A CE2 1 
ATOM   905  C CE3 . TRP A 1 116 ? 36.286 -21.126 22.194  1.00 16.16 ? 116 TRP A CE3 1 
ATOM   906  C CZ2 . TRP A 1 116 ? 37.452 -22.355 19.916  1.00 14.26 ? 116 TRP A CZ2 1 
ATOM   907  C CZ3 . TRP A 1 116 ? 37.014 -22.321 22.296  1.00 14.56 ? 116 TRP A CZ3 1 
ATOM   908  C CH2 . TRP A 1 116 ? 37.580 -22.912 21.169  1.00 14.68 ? 116 TRP A CH2 1 
ATOM   909  N N   . PRO A 1 117 ? 33.295 -15.530 22.275  1.00 16.51 ? 117 PRO A N   1 
ATOM   910  C CA  . PRO A 1 117 ? 32.265 -15.027 23.208  1.00 16.40 ? 117 PRO A CA  1 
ATOM   911  C C   . PRO A 1 117 ? 31.159 -14.207 22.546  1.00 15.44 ? 117 PRO A C   1 
ATOM   912  O O   . PRO A 1 117 ? 30.116 -13.979 23.164  1.00 17.09 ? 117 PRO A O   1 
ATOM   913  C CB  . PRO A 1 117 ? 33.079 -14.161 24.184  1.00 16.45 ? 117 PRO A CB  1 
ATOM   914  C CG  . PRO A 1 117 ? 34.428 -14.775 24.166  1.00 14.71 ? 117 PRO A CG  1 
ATOM   915  C CD  . PRO A 1 117 ? 34.626 -15.035 22.681  1.00 14.59 ? 117 PRO A CD  1 
ATOM   916  N N   . VAL A 1 118 ? 31.352 -13.751 21.322  1.00 15.99 ? 118 VAL A N   1 
ATOM   917  C CA  . VAL A 1 118 ? 30.325 -12.993 20.618  1.00 18.36 ? 118 VAL A CA  1 
ATOM   918  C C   . VAL A 1 118 ? 29.819 -13.682 19.352  1.00 17.50 ? 118 VAL A C   1 
ATOM   919  O O   . VAL A 1 118 ? 28.734 -13.330 18.865  1.00 16.18 ? 118 VAL A O   1 
ATOM   920  C CB  . VAL A 1 118 ? 30.809 -11.561 20.301  1.00 17.95 ? 118 VAL A CB  1 
ATOM   921  C CG1 . VAL A 1 118 ? 30.902 -10.761 21.597  1.00 18.52 ? 118 VAL A CG1 1 
ATOM   922  C CG2 . VAL A 1 118 ? 32.168 -11.593 19.553  1.00 16.12 ? 118 VAL A CG2 1 
ATOM   923  N N   . LEU A 1 119 ? 30.555 -14.650 18.789  1.00 16.43 ? 119 LEU A N   1 
ATOM   924  C CA  . LEU A 1 119 ? 30.142 -15.363 17.603  1.00 16.32 ? 119 LEU A CA  1 
ATOM   925  C C   . LEU A 1 119 ? 30.035 -16.874 17.819  1.00 15.69 ? 119 LEU A C   1 
ATOM   926  O O   . LEU A 1 119 ? 29.512 -17.575 16.938  1.00 17.69 ? 119 LEU A O   1 
ATOM   927  C CB  . LEU A 1 119 ? 31.112 -15.072 16.442  1.00 15.65 ? 119 LEU A CB  1 
ATOM   928  C CG  . LEU A 1 119 ? 31.295 -13.623 15.904  1.00 16.78 ? 119 LEU A CG  1 
ATOM   929  C CD1 . LEU A 1 119 ? 32.269 -13.536 14.694  1.00 14.68 ? 119 LEU A CD1 1 
ATOM   930  C CD2 . LEU A 1 119 ? 29.952 -12.951 15.568  1.00 21.54 ? 119 LEU A CD2 1 
ATOM   931  N N   . GLY A 1 120 ? 30.481 -17.396 18.951  1.00 15.23 ? 120 GLY A N   1 
ATOM   932  C CA  . GLY A 1 120 ? 30.451 -18.837 19.070  1.00 16.46 ? 120 GLY A CA  1 
ATOM   933  C C   . GLY A 1 120 ? 31.523 -19.423 18.152  1.00 15.88 ? 120 GLY A C   1 
ATOM   934  O O   . GLY A 1 120 ? 32.368 -18.715 17.600  1.00 14.23 ? 120 GLY A O   1 
ATOM   935  N N   . LEU A 1 121 ? 31.468 -20.750 17.986  1.00 15.30 ? 121 LEU A N   1 
ATOM   936  C CA  . LEU A 1 121 ? 32.469 -21.421 17.167  1.00 14.29 ? 121 LEU A CA  1 
ATOM   937  C C   . LEU A 1 121 ? 32.310 -21.034 15.691  1.00 16.00 ? 121 LEU A C   1 
ATOM   938  O O   . LEU A 1 121 ? 31.194 -20.851 15.195  1.00 16.47 ? 121 LEU A O   1 
ATOM   939  C CB  . LEU A 1 121 ? 32.336 -22.932 17.342  1.00 13.98 ? 121 LEU A CB  1 
ATOM   940  C CG  . LEU A 1 121 ? 32.438 -23.353 18.808  1.00 15.31 ? 121 LEU A CG  1 
ATOM   941  C CD1 . LEU A 1 121 ? 32.318 -24.873 19.053  1.00 14.30 ? 121 LEU A CD1 1 
ATOM   942  C CD2 . LEU A 1 121 ? 33.744 -22.816 19.430  1.00 14.75 ? 121 LEU A CD2 1 
ATOM   943  N N   . PRO A 1 122 ? 33.411 -20.907 14.953  1.00 15.47 ? 122 PRO A N   1 
ATOM   944  C CA  . PRO A 1 122 ? 33.299 -20.498 13.551  1.00 16.08 ? 122 PRO A CA  1 
ATOM   945  C C   . PRO A 1 122 ? 32.634 -21.532 12.700  1.00 17.54 ? 122 PRO A C   1 
ATOM   946  O O   . PRO A 1 122 ? 32.755 -22.761 12.937  1.00 15.60 ? 122 PRO A O   1 
ATOM   947  C CB  . PRO A 1 122 ? 34.775 -20.286 13.141  1.00 16.42 ? 122 PRO A CB  1 
ATOM   948  C CG  . PRO A 1 122 ? 35.526 -21.264 14.028  1.00 14.42 ? 122 PRO A CG  1 
ATOM   949  C CD  . PRO A 1 122 ? 34.819 -21.084 15.364  1.00 17.28 ? 122 PRO A CD  1 
ATOM   950  N N   . PRO A 1 123 ? 31.905 -21.130 11.642  1.00 16.41 ? 123 PRO A N   1 
ATOM   951  C CA  . PRO A 1 123 ? 31.374 -22.093 10.690  1.00 16.02 ? 123 PRO A CA  1 
ATOM   952  C C   . PRO A 1 123 ? 32.544 -22.747 9.975   1.00 18.18 ? 123 PRO A C   1 
ATOM   953  O O   . PRO A 1 123 ? 33.676 -22.259 10.026  1.00 16.12 ? 123 PRO A O   1 
ATOM   954  C CB  . PRO A 1 123 ? 30.546 -21.221 9.734   1.00 15.92 ? 123 PRO A CB  1 
ATOM   955  C CG  . PRO A 1 123 ? 31.291 -19.888 9.758   1.00 15.21 ? 123 PRO A CG  1 
ATOM   956  C CD  . PRO A 1 123 ? 31.659 -19.728 11.190  1.00 15.23 ? 123 PRO A CD  1 
ATOM   957  N N   . ASN A 1 124 ? 32.268 -23.871 9.294   1.00 17.87 ? 124 ASN A N   1 
ATOM   958  C CA  . ASN A 1 124 ? 33.381 -24.632 8.734   1.00 16.66 ? 124 ASN A CA  1 
ATOM   959  C C   . ASN A 1 124 ? 34.082 -23.868 7.623   1.00 14.89 ? 124 ASN A C   1 
ATOM   960  O O   . ASN A 1 124 ? 35.310 -23.952 7.519   1.00 14.96 ? 124 ASN A O   1 
ATOM   961  C CB  . ASN A 1 124 ? 32.977 -26.072 8.338   1.00 15.85 ? 124 ASN A CB  1 
ATOM   962  C CG  . ASN A 1 124 ? 32.950 -27.015 9.544   1.00 18.81 ? 124 ASN A CG  1 
ATOM   963  O OD1 . ASN A 1 124 ? 33.989 -27.319 10.145  1.00 18.32 ? 124 ASN A OD1 1 
ATOM   964  N ND2 . ASN A 1 124 ? 31.761 -27.492 9.896   1.00 21.40 ? 124 ASN A ND2 1 
ATOM   965  N N   . TRP A 1 125 ? 33.339 -23.080 6.833   1.00 13.17 ? 125 TRP A N   1 
ATOM   966  C CA  . TRP A 1 125 ? 33.945 -22.364 5.710   1.00 14.46 ? 125 TRP A CA  1 
ATOM   967  C C   . TRP A 1 125 ? 34.999 -21.364 6.177   1.00 15.56 ? 125 TRP A C   1 
ATOM   968  O O   . TRP A 1 125 ? 35.950 -21.072 5.430   1.00 15.53 ? 125 TRP A O   1 
ATOM   969  C CB  . TRP A 1 125 ? 32.895 -21.644 4.849   1.00 14.15 ? 125 TRP A CB  1 
ATOM   970  C CG  . TRP A 1 125 ? 32.122 -20.554 5.557   1.00 15.76 ? 125 TRP A CG  1 
ATOM   971  C CD1 . TRP A 1 125 ? 30.897 -20.668 6.165   1.00 19.09 ? 125 TRP A CD1 1 
ATOM   972  C CD2 . TRP A 1 125 ? 32.497 -19.174 5.685   1.00 17.69 ? 125 TRP A CD2 1 
ATOM   973  N NE1 . TRP A 1 125 ? 30.502 -19.449 6.698   1.00 17.21 ? 125 TRP A NE1 1 
ATOM   974  C CE2 . TRP A 1 125 ? 31.464 -18.518 6.415   1.00 16.94 ? 125 TRP A CE2 1 
ATOM   975  C CE3 . TRP A 1 125 ? 33.617 -18.431 5.280   1.00 16.59 ? 125 TRP A CE3 1 
ATOM   976  C CZ2 . TRP A 1 125 ? 31.513 -17.159 6.734   1.00 18.09 ? 125 TRP A CZ2 1 
ATOM   977  C CZ3 . TRP A 1 125 ? 33.668 -17.074 5.608   1.00 17.04 ? 125 TRP A CZ3 1 
ATOM   978  C CH2 . TRP A 1 125 ? 32.618 -16.456 6.330   1.00 18.73 ? 125 TRP A CH2 1 
ATOM   979  N N   . PHE A 1 126 ? 34.841 -20.818 7.389   1.00 14.60 ? 126 PHE A N   1 
ATOM   980  C CA  . PHE A 1 126 ? 35.826 -19.874 7.907   1.00 15.15 ? 126 PHE A CA  1 
ATOM   981  C C   . PHE A 1 126 ? 37.127 -20.576 8.289   1.00 15.10 ? 126 PHE A C   1 
ATOM   982  O O   . PHE A 1 126 ? 38.210 -19.981 8.213   1.00 14.70 ? 126 PHE A O   1 
ATOM   983  C CB  . PHE A 1 126 ? 35.238 -19.091 9.089   1.00 15.35 ? 126 PHE A CB  1 
ATOM   984  C CG  . PHE A 1 126 ? 36.175 -18.050 9.659   1.00 17.08 ? 126 PHE A CG  1 
ATOM   985  C CD1 . PHE A 1 126 ? 37.096 -18.395 10.670  1.00 14.95 ? 126 PHE A CD1 1 
ATOM   986  C CD2 . PHE A 1 126 ? 36.142 -16.721 9.182   1.00 15.93 ? 126 PHE A CD2 1 
ATOM   987  C CE1 . PHE A 1 126 ? 37.966 -17.432 11.209  1.00 15.76 ? 126 PHE A CE1 1 
ATOM   988  C CE2 . PHE A 1 126 ? 37.009 -15.743 9.716   1.00 15.26 ? 126 PHE A CE2 1 
ATOM   989  C CZ  . PHE A 1 126 ? 37.920 -16.100 10.731  1.00 15.39 ? 126 PHE A CZ  1 
ATOM   990  N N   . LYS A 1 127 ? 37.045 -21.836 8.693   1.00 14.10 ? 127 LYS A N   1 
ATOM   991  C CA  . LYS A 1 127 ? 38.240 -22.572 9.084   1.00 15.57 ? 127 LYS A CA  1 
ATOM   992  C C   . LYS A 1 127 ? 38.991 -23.191 7.900   1.00 15.89 ? 127 LYS A C   1 
ATOM   993  O O   . LYS A 1 127 ? 40.145 -23.599 8.076   1.00 15.29 ? 127 LYS A O   1 
ATOM   994  C CB  . LYS A 1 127 ? 37.838 -23.647 10.094  1.00 14.15 ? 127 LYS A CB  1 
ATOM   995  C CG  . LYS A 1 127 ? 37.186 -23.069 11.318  1.00 14.88 ? 127 LYS A CG  1 
ATOM   996  C CD  . LYS A 1 127 ? 36.802 -24.094 12.378  1.00 15.82 ? 127 LYS A CD  1 
ATOM   997  C CE  . LYS A 1 127 ? 35.520 -24.866 12.041  1.00 16.32 ? 127 LYS A CE  1 
ATOM   998  N NZ  . LYS A 1 127 ? 35.048 -25.659 13.239  1.00 14.57 ? 127 LYS A NZ  1 
ATOM   999  N N   . GLU A 1 128 ? 38.392 -23.229 6.696   1.00 13.90 ? 128 GLU A N   1 
ATOM   1000 C CA  . GLU A 1 128 ? 38.906 -24.032 5.595   1.00 15.48 ? 128 GLU A CA  1 
ATOM   1001 C C   . GLU A 1 128 ? 39.792 -23.222 4.649   1.00 16.92 ? 128 GLU A C   1 
ATOM   1002 O O   . GLU A 1 128 ? 39.808 -21.984 4.681   1.00 15.85 ? 128 GLU A O   1 
ATOM   1003 C CB  . GLU A 1 128 ? 37.751 -24.686 4.831   1.00 15.16 ? 128 GLU A CB  1 
ATOM   1004 C CG  . GLU A 1 128 ? 37.140 -25.831 5.631   1.00 17.51 ? 128 GLU A CG  1 
ATOM   1005 C CD  . GLU A 1 128 ? 35.736 -26.216 5.199   1.00 14.30 ? 128 GLU A CD  1 
ATOM   1006 O OE1 . GLU A 1 128 ? 35.254 -25.728 4.168   1.00 16.45 ? 128 GLU A OE1 1 
ATOM   1007 O OE2 . GLU A 1 128 ? 35.122 -27.004 5.922   1.00 15.93 ? 128 GLU A OE2 1 
ATOM   1008 N N   . PRO A 1 129 ? 40.560 -23.914 3.791   1.00 17.52 ? 129 PRO A N   1 
ATOM   1009 C CA  . PRO A 1 129 ? 41.654 -23.244 3.060   1.00 15.96 ? 129 PRO A CA  1 
ATOM   1010 C C   . PRO A 1 129 ? 41.194 -22.339 1.945   1.00 16.81 ? 129 PRO A C   1 
ATOM   1011 O O   . PRO A 1 129 ? 41.986 -21.482 1.516   1.00 17.08 ? 129 PRO A O   1 
ATOM   1012 C CB  . PRO A 1 129 ? 42.467 -24.422 2.495   1.00 16.73 ? 129 PRO A CB  1 
ATOM   1013 C CG  . PRO A 1 129 ? 42.165 -25.569 3.461   1.00 17.92 ? 129 PRO A CG  1 
ATOM   1014 C CD  . PRO A 1 129 ? 40.676 -25.384 3.701   1.00 18.09 ? 129 PRO A CD  1 
ATOM   1015 N N   . GLN A 1 130 ? 39.966 -22.515 1.440   1.00 15.39 ? 130 GLN A N   1 
ATOM   1016 C CA  . GLN A 1 130 ? 39.517 -21.725 0.296   1.00 15.04 ? 130 GLN A CA  1 
ATOM   1017 C C   . GLN A 1 130 ? 39.285 -20.265 0.691   1.00 15.20 ? 130 GLN A C   1 
ATOM   1018 O O   . GLN A 1 130 ? 39.775 -19.342 0.023   1.00 14.03 ? 130 GLN A O   1 
ATOM   1019 C CB  . GLN A 1 130 ? 38.255 -22.345 -0.299  1.00 14.13 ? 130 GLN A CB  1 
ATOM   1020 C CG  . GLN A 1 130 ? 38.484 -23.716 -0.926  1.00 16.84 ? 130 GLN A CG  1 
ATOM   1021 C CD  . GLN A 1 130 ? 38.845 -24.781 0.109   1.00 15.78 ? 130 GLN A CD  1 
ATOM   1022 O OE1 . GLN A 1 130 ? 38.276 -24.814 1.196   1.00 15.14 ? 130 GLN A OE1 1 
ATOM   1023 N NE2 . GLN A 1 130 ? 39.774 -25.669 -0.242  1.00 15.16 ? 130 GLN A NE2 1 
ATOM   1024 N N   . TYR A 1 131 ? 38.538 -20.042 1.780   1.00 15.35 ? 131 TYR A N   1 
ATOM   1025 C CA  . TYR A 1 131 ? 38.308 -18.680 2.256   1.00 16.92 ? 131 TYR A CA  1 
ATOM   1026 C C   . TYR A 1 131 ? 39.610 -18.060 2.748   1.00 17.25 ? 131 TYR A C   1 
ATOM   1027 O O   . TYR A 1 131 ? 39.928 -16.902 2.428   1.00 15.51 ? 131 TYR A O   1 
ATOM   1028 C CB  . TYR A 1 131 ? 37.266 -18.666 3.385   1.00 16.45 ? 131 TYR A CB  1 
ATOM   1029 C CG  . TYR A 1 131 ? 37.130 -17.299 4.039   1.00 16.21 ? 131 TYR A CG  1 
ATOM   1030 C CD1 . TYR A 1 131 ? 36.476 -16.243 3.372   1.00 17.37 ? 131 TYR A CD1 1 
ATOM   1031 C CD2 . TYR A 1 131 ? 37.675 -17.050 5.310   1.00 15.58 ? 131 TYR A CD2 1 
ATOM   1032 C CE1 . TYR A 1 131 ? 36.369 -14.966 3.963   1.00 16.89 ? 131 TYR A CE1 1 
ATOM   1033 C CE2 . TYR A 1 131 ? 37.570 -15.787 5.917   1.00 16.64 ? 131 TYR A CE2 1 
ATOM   1034 C CZ  . TYR A 1 131 ? 36.919 -14.737 5.233   1.00 17.12 ? 131 TYR A CZ  1 
ATOM   1035 O OH  . TYR A 1 131 ? 36.811 -13.478 5.836   1.00 14.99 ? 131 TYR A OH  1 
ATOM   1036 N N   . ARG A 1 132 ? 40.373 -18.824 3.544   1.00 15.53 ? 132 ARG A N   1 
ATOM   1037 C CA  . ARG A 1 132 ? 41.545 -18.262 4.206   1.00 14.95 ? 132 ARG A CA  1 
ATOM   1038 C C   . ARG A 1 132 ? 42.610 -17.854 3.194   1.00 15.07 ? 132 ARG A C   1 
ATOM   1039 O O   . ARG A 1 132 ? 43.223 -16.785 3.331   1.00 13.92 ? 132 ARG A O   1 
ATOM   1040 C CB  . ARG A 1 132 ? 42.059 -19.254 5.237   1.00 13.86 ? 132 ARG A CB  1 
ATOM   1041 C CG  . ARG A 1 132 ? 41.186 -19.363 6.463   1.00 12.52 ? 132 ARG A CG  1 
ATOM   1042 C CD  . ARG A 1 132 ? 41.499 -20.624 7.233   1.00 13.60 ? 132 ARG A CD  1 
ATOM   1043 N NE  . ARG A 1 132 ? 42.932 -20.778 7.437   1.00 14.51 ? 132 ARG A NE  1 
ATOM   1044 C CZ  . ARG A 1 132 ? 43.560 -21.944 7.465   1.00 16.89 ? 132 ARG A CZ  1 
ATOM   1045 N NH1 . ARG A 1 132 ? 42.908 -23.080 7.253   1.00 14.87 ? 132 ARG A NH1 1 
ATOM   1046 N NH2 . ARG A 1 132 ? 44.870 -21.972 7.730   1.00 14.26 ? 132 ARG A NH2 1 
ATOM   1047 N N   . SER A 1 133 ? 42.792 -18.660 2.136   1.00 14.27 ? 133 SER A N   1 
ATOM   1048 C CA  . SER A 1 133 ? 43.860 -18.409 1.169   1.00 15.27 ? 133 SER A CA  1 
ATOM   1049 C C   . SER A 1 133 ? 43.562 -17.201 0.284   1.00 15.89 ? 133 SER A C   1 
ATOM   1050 O O   . SER A 1 133 ? 44.477 -16.436 -0.041  1.00 15.69 ? 133 SER A O   1 
ATOM   1051 C CB  . SER A 1 133 ? 44.098 -19.646 0.304   1.00 14.73 ? 133 SER A CB  1 
ATOM   1052 O OG  . SER A 1 133 ? 43.008 -19.913 -0.571  1.00 15.17 ? 133 SER A OG  1 
ATOM   1053 N N   . ARG A 1 134 ? 42.285 -17.026 -0.129  1.00 16.80 ? 134 ARG A N   1 
ATOM   1054 C CA  . ARG A 1 134 ? 41.858 -16.040 -1.137  1.00 18.32 ? 134 ARG A CA  1 
ATOM   1055 C C   . ARG A 1 134 ? 41.503 -14.644 -0.584  1.00 16.63 ? 134 ARG A C   1 
ATOM   1056 O O   . ARG A 1 134 ? 41.695 -13.647 -1.289  1.00 16.15 ? 134 ARG A O   1 
ATOM   1057 C CB  . ARG A 1 134 ? 40.650 -16.558 -1.935  1.00 17.64 ? 134 ARG A CB  1 
ATOM   1058 C CG  . ARG A 1 134 ? 40.336 -15.656 -3.112  1.00 21.41 ? 134 ARG A CG  1 
ATOM   1059 C CD  . ARG A 1 134 ? 39.068 -16.060 -3.883  1.00 24.78 ? 134 ARG A CD  1 
ATOM   1060 N NE  . ARG A 1 134 ? 38.888 -15.238 -5.079  1.00 26.72 ? 134 ARG A NE  1 
ATOM   1061 C CZ  . ARG A 1 134 ? 37.726 -15.034 -5.688  1.00 25.33 ? 134 ARG A CZ  1 
ATOM   1062 N NH1 . ARG A 1 134 ? 36.605 -15.588 -5.248  1.00 23.73 ? 134 ARG A NH1 1 
ATOM   1063 N NH2 . ARG A 1 134 ? 37.688 -14.244 -6.756  1.00 26.06 ? 134 ARG A NH2 1 
ATOM   1064 N N   . VAL A 1 135 ? 40.975 -14.546 0.639   1.00 15.69 ? 135 VAL A N   1 
ATOM   1065 C CA  . VAL A 1 135 ? 40.390 -13.282 1.074   1.00 17.32 ? 135 VAL A CA  1 
ATOM   1066 C C   . VAL A 1 135 ? 41.457 -12.204 1.263   1.00 16.79 ? 135 VAL A C   1 
ATOM   1067 O O   . VAL A 1 135 ? 41.191 -11.021 1.039   1.00 14.79 ? 135 VAL A O   1 
ATOM   1068 C CB  . VAL A 1 135 ? 39.466 -13.490 2.297   1.00 17.03 ? 135 VAL A CB  1 
ATOM   1069 C CG1 . VAL A 1 135 ? 40.274 -13.767 3.554   1.00 15.88 ? 135 VAL A CG1 1 
ATOM   1070 C CG2 . VAL A 1 135 ? 38.524 -12.278 2.499   1.00 17.86 ? 135 VAL A CG2 1 
ATOM   1071 N N   . VAL A 1 136 ? 42.676 -12.587 1.663   1.00 18.10 ? 136 VAL A N   1 
ATOM   1072 C CA  . VAL A 1 136 ? 43.762 -11.607 1.794   1.00 17.09 ? 136 VAL A CA  1 
ATOM   1073 C C   . VAL A 1 136 ? 44.278 -11.138 0.447   1.00 16.72 ? 136 VAL A C   1 
ATOM   1074 O O   . VAL A 1 136 ? 44.945 -10.099 0.372   1.00 18.40 ? 136 VAL A O   1 
ATOM   1075 C CB  . VAL A 1 136 ? 44.939 -12.113 2.662   1.00 15.66 ? 136 VAL A CB  1 
ATOM   1076 C CG1 . VAL A 1 136 ? 44.543 -12.220 4.112   1.00 16.99 ? 136 VAL A CG1 1 
ATOM   1077 C CG2 . VAL A 1 136 ? 45.464 -13.452 2.123   1.00 15.73 ? 136 VAL A CG2 1 
ATOM   1078 N N   . ARG A 1 137 ? 43.995 -11.875 -0.617  1.00 15.71 ? 137 ARG A N   1 
ATOM   1079 C CA  . ARG A 1 137 ? 44.555 -11.644 -1.942  1.00 17.20 ? 137 ARG A CA  1 
ATOM   1080 C C   . ARG A 1 137 ? 43.564 -10.972 -2.895  1.00 19.86 ? 137 ARG A C   1 
ATOM   1081 O O   . ARG A 1 137 ? 43.953 -10.076 -3.652  1.00 20.21 ? 137 ARG A O   1 
ATOM   1082 C CB  . ARG A 1 137 ? 45.009 -12.997 -2.514  1.00 16.76 ? 137 ARG A CB  1 
ATOM   1083 C CG  . ARG A 1 137 ? 45.701 -12.966 -3.889  1.00 20.18 ? 137 ARG A CG  1 
ATOM   1084 C CD  . ARG A 1 137 ? 46.575 -14.236 -4.053  1.00 20.04 ? 137 ARG A CD  1 
ATOM   1085 N NE  . ARG A 1 137 ? 46.932 -14.580 -5.422  1.00 19.77 ? 137 ARG A NE  1 
ATOM   1086 C CZ  . ARG A 1 137 ? 47.797 -13.899 -6.166  1.00 21.21 ? 137 ARG A CZ  1 
ATOM   1087 N NH1 . ARG A 1 137 ? 48.419 -12.825 -5.693  1.00 23.23 ? 137 ARG A NH1 1 
ATOM   1088 N NH2 . ARG A 1 137 ? 48.055 -14.312 -7.406  1.00 19.70 ? 137 ARG A NH2 1 
ATOM   1089 N N   . GLU A 1 138 ? 42.284 -11.365 -2.857  1.00 18.07 ? 138 GLU A N   1 
ATOM   1090 C CA  . GLU A 1 138 ? 41.255 -10.838 -3.754  1.00 19.31 ? 138 GLU A CA  1 
ATOM   1091 C C   . GLU A 1 138 ? 39.969 -10.632 -2.969  1.00 20.75 ? 138 GLU A C   1 
ATOM   1092 O O   . GLU A 1 138 ? 38.927 -11.210 -3.297  1.00 20.20 ? 138 GLU A O   1 
ATOM   1093 C CB  . GLU A 1 138 ? 40.982 -11.830 -4.869  1.00 22.57 ? 138 GLU A CB  1 
ATOM   1094 C CG  . GLU A 1 138 ? 42.110 -12.090 -5.808  1.00 25.24 ? 138 GLU A CG  1 
ATOM   1095 C CD  . GLU A 1 138 ? 41.821 -13.316 -6.654  1.00 29.31 ? 138 GLU A CD  1 
ATOM   1096 O OE1 . GLU A 1 138 ? 42.289 -13.333 -7.822  1.00 33.04 ? 138 GLU A OE1 1 
ATOM   1097 O OE2 . GLU A 1 138 ? 41.140 -14.256 -6.133  1.00 29.17 ? 138 GLU A OE2 1 
ATOM   1098 N N   . PRO A 1 139 ? 40.008 -9.809  -1.902  1.00 21.95 ? 139 PRO A N   1 
ATOM   1099 C CA  . PRO A 1 139 ? 38.792 -9.642  -1.066  1.00 21.02 ? 139 PRO A CA  1 
ATOM   1100 C C   . PRO A 1 139 ? 37.574 -9.167  -1.850  1.00 21.27 ? 139 PRO A C   1 
ATOM   1101 O O   . PRO A 1 139 ? 36.463 -9.670  -1.619  1.00 20.18 ? 139 PRO A O   1 
ATOM   1102 C CB  . PRO A 1 139 ? 39.235 -8.621  -0.001  1.00 19.13 ? 139 PRO A CB  1 
ATOM   1103 C CG  . PRO A 1 139 ? 40.304 -7.808  -0.725  1.00 19.05 ? 139 PRO A CG  1 
ATOM   1104 C CD  . PRO A 1 139 ? 41.084 -8.887  -1.477  1.00 18.22 ? 139 PRO A CD  1 
ATOM   1105 N N   . ARG A 1 140 ? 37.757 -8.221  -2.785  1.00 21.45 ? 140 ARG A N   1 
ATOM   1106 C CA  . ARG A 1 140 ? 36.615 -7.642  -3.485  1.00 21.03 ? 140 ARG A CA  1 
ATOM   1107 C C   . ARG A 1 140 ? 35.939 -8.681  -4.365  1.00 21.41 ? 140 ARG A C   1 
ATOM   1108 O O   . ARG A 1 140 ? 34.714 -8.811  -4.340  1.00 21.80 ? 140 ARG A O   1 
ATOM   1109 C CB  . ARG A 1 140 ? 37.048 -6.433  -4.313  1.00 21.68 ? 140 ARG A CB  1 
ATOM   1110 C CG  . ARG A 1 140 ? 35.951 -5.365  -4.496  1.00 22.04 ? 140 ARG A CG  1 
ATOM   1111 C CD  . ARG A 1 140 ? 36.506 -4.110  -5.186  1.00 20.48 ? 140 ARG A CD  1 
ATOM   1112 N NE  . ARG A 1 140 ? 37.627 -3.524  -4.470  1.00 18.76 ? 140 ARG A NE  1 
ATOM   1113 C CZ  . ARG A 1 140 ? 37.508 -2.621  -3.507  1.00 21.03 ? 140 ARG A CZ  1 
ATOM   1114 N NH1 . ARG A 1 140 ? 36.321 -2.156  -3.136  1.00 22.35 ? 140 ARG A NH1 1 
ATOM   1115 N NH2 . ARG A 1 140 ? 38.604 -2.168  -2.896  1.00 20.33 ? 140 ARG A NH2 1 
ATOM   1116 N N   . GLN A 1 141 ? 36.727 -9.431  -5.146  1.00 21.94 ? 141 GLN A N   1 
ATOM   1117 C CA  . GLN A 1 141 ? 36.174 -10.500 -5.981  1.00 22.11 ? 141 GLN A CA  1 
ATOM   1118 C C   . GLN A 1 141 ? 35.578 -11.604 -5.129  1.00 23.01 ? 141 GLN A C   1 
ATOM   1119 O O   . GLN A 1 141 ? 34.566 -12.202 -5.506  1.00 25.48 ? 141 GLN A O   1 
ATOM   1120 C CB  . GLN A 1 141 ? 37.269 -11.109 -6.853  1.00 23.87 ? 141 GLN A CB  1 
ATOM   1121 C CG  . GLN A 1 141 ? 37.952 -10.142 -7.806  1.00 25.36 ? 141 GLN A CG  1 
ATOM   1122 C CD  . GLN A 1 141 ? 39.240 -9.584  -7.223  1.00 28.43 ? 141 GLN A CD  1 
ATOM   1123 O OE1 . GLN A 1 141 ? 39.280 -9.121  -6.062  1.00 28.07 ? 141 GLN A OE1 1 
ATOM   1124 N NE2 . GLN A 1 141 ? 40.322 -9.670  -8.003  1.00 31.96 ? 141 GLN A NE2 1 
ATOM   1125 N N   . LEU A 1 142 ? 36.199 -11.901 -3.981  1.00 21.22 ? 142 LEU A N   1 
ATOM   1126 C CA  . LEU A 1 142 ? 35.738 -13.013 -3.156  1.00 21.02 ? 142 LEU A CA  1 
ATOM   1127 C C   . LEU A 1 142 ? 34.384 -12.708 -2.524  1.00 22.74 ? 142 LEU A C   1 
ATOM   1128 O O   . LEU A 1 142 ? 33.521 -13.595 -2.422  1.00 22.42 ? 142 LEU A O   1 
ATOM   1129 C CB  . LEU A 1 142 ? 36.788 -13.328 -2.087  1.00 20.78 ? 142 LEU A CB  1 
ATOM   1130 C CG  . LEU A 1 142 ? 36.547 -14.536 -1.206  1.00 17.37 ? 142 LEU A CG  1 
ATOM   1131 C CD1 . LEU A 1 142 ? 37.853 -15.030 -0.718  1.00 17.09 ? 142 LEU A CD1 1 
ATOM   1132 C CD2 . LEU A 1 142 ? 35.669 -14.158 -0.046  1.00 21.26 ? 142 LEU A CD2 1 
ATOM   1133 N N   . LEU A 1 143 ? 34.180 -11.456 -2.091  1.00 22.01 ? 143 LEU A N   1 
ATOM   1134 C CA  . LEU A 1 143 ? 32.906 -11.089 -1.470  1.00 23.83 ? 143 LEU A CA  1 
ATOM   1135 C C   . LEU A 1 143 ? 31.766 -11.112 -2.476  1.00 22.47 ? 143 LEU A C   1 
ATOM   1136 O O   . LEU A 1 143 ? 30.631 -11.443 -2.122  1.00 23.13 ? 143 LEU A O   1 
ATOM   1137 C CB  . LEU A 1 143 ? 32.985 -9.715  -0.794  1.00 22.89 ? 143 LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 143 ? 33.832 -9.492  0.462   1.00 21.14 ? 143 LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 143 ? 33.620 -8.071  0.995   1.00 20.42 ? 143 LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 143 ? 33.482 -10.505 1.529   1.00 20.16 ? 143 LEU A CD2 1 
ATOM   1141 N N   . LYS A 1 144 ? 32.035 -10.726 -3.718  1.00 22.69 ? 144 LYS A N   1 
ATOM   1142 C CA  . LYS A 1 144 ? 30.982 -10.748 -4.723  1.00 23.09 ? 144 LYS A CA  1 
ATOM   1143 C C   . LYS A 1 144 ? 30.654 -12.181 -5.126  1.00 26.05 ? 144 LYS A C   1 
ATOM   1144 O O   . LYS A 1 144 ? 29.487 -12.600 -5.078  1.00 26.37 ? 144 LYS A O   1 
ATOM   1145 C CB  . LYS A 1 144 ? 31.395 -9.906  -5.927  1.00 24.33 ? 144 LYS A CB  1 
ATOM   1146 C CG  . LYS A 1 144 ? 30.347 -9.773  -7.041  1.00 24.92 ? 144 LYS A CG  1 
ATOM   1147 C CD  . LYS A 1 144 ? 30.876 -8.789  -8.086  1.00 29.90 ? 144 LYS A CD  1 
ATOM   1148 C CE  . LYS A 1 144 ? 30.866 -9.350  -9.497  1.00 30.52 ? 144 LYS A CE  1 
ATOM   1149 N NZ  . LYS A 1 144 ? 30.091 -8.511  -10.428 1.00 28.23 ? 144 LYS A NZ  1 
ATOM   1150 N N   . GLU A 1 145 ? 31.676 -12.964 -5.488  1.00 24.69 ? 145 GLU A N   1 
ATOM   1151 C CA  . GLU A 1 145 ? 31.429 -14.312 -5.992  1.00 25.92 ? 145 GLU A CA  1 
ATOM   1152 C C   . GLU A 1 145 ? 30.852 -15.234 -4.914  1.00 25.51 ? 145 GLU A C   1 
ATOM   1153 O O   . GLU A 1 145 ? 29.843 -15.921 -5.135  1.00 26.73 ? 145 GLU A O   1 
ATOM   1154 C CB  . GLU A 1 145 ? 32.702 -14.893 -6.611  1.00 25.08 ? 145 GLU A CB  1 
ATOM   1155 C CG  . GLU A 1 145 ? 33.182 -14.152 -7.847  1.00 29.62 ? 145 GLU A CG  1 
ATOM   1156 C CD  . GLU A 1 145 ? 34.655 -14.435 -8.146  1.00 33.64 ? 145 GLU A CD  1 
ATOM   1157 O OE1 . GLU A 1 145 ? 35.243 -13.690 -8.971  1.00 30.18 ? 145 GLU A OE1 1 
ATOM   1158 O OE2 . GLU A 1 145 ? 35.214 -15.400 -7.550  1.00 33.45 ? 145 GLU A OE2 1 
ATOM   1159 N N   . GLU A 1 146 ? 31.477 -15.275 -3.741  1.00 24.53 ? 146 GLU A N   1 
ATOM   1160 C CA  . GLU A 1 146 ? 31.012 -16.196 -2.720  1.00 21.92 ? 146 GLU A CA  1 
ATOM   1161 C C   . GLU A 1 146 ? 29.707 -15.707 -2.085  1.00 24.48 ? 146 GLU A C   1 
ATOM   1162 O O   . GLU A 1 146 ? 28.718 -16.447 -2.036  1.00 27.27 ? 146 GLU A O   1 
ATOM   1163 C CB  . GLU A 1 146 ? 32.114 -16.461 -1.692  1.00 20.31 ? 146 GLU A CB  1 
ATOM   1164 C CG  . GLU A 1 146 ? 31.771 -17.563 -0.657  1.00 24.27 ? 146 GLU A CG  1 
ATOM   1165 C CD  . GLU A 1 146 ? 31.115 -18.816 -1.247  1.00 23.61 ? 146 GLU A CD  1 
ATOM   1166 O OE1 . GLU A 1 146 ? 30.200 -19.381 -0.585  1.00 20.38 ? 146 GLU A OE1 1 
ATOM   1167 O OE2 . GLU A 1 146 ? 31.569 -19.257 -2.335  1.00 25.03 ? 146 GLU A OE2 1 
ATOM   1168 N N   . PHE A 1 147 ? 29.666 -14.453 -1.624  1.00 22.99 ? 147 PHE A N   1 
ATOM   1169 C CA  . PHE A 1 147 ? 28.557 -13.962 -0.810  1.00 22.41 ? 147 PHE A CA  1 
ATOM   1170 C C   . PHE A 1 147 ? 27.645 -12.988 -1.542  1.00 24.70 ? 147 PHE A C   1 
ATOM   1171 O O   . PHE A 1 147 ? 26.800 -12.361 -0.897  1.00 25.20 ? 147 PHE A O   1 
ATOM   1172 C CB  . PHE A 1 147 ? 29.088 -13.290 0.453   1.00 21.82 ? 147 PHE A CB  1 
ATOM   1173 C CG  . PHE A 1 147 ? 29.881 -14.208 1.317   1.00 20.90 ? 147 PHE A CG  1 
ATOM   1174 C CD1 . PHE A 1 147 ? 31.250 -14.331 1.138   1.00 22.24 ? 147 PHE A CD1 1 
ATOM   1175 C CD2 . PHE A 1 147 ? 29.261 -14.979 2.281   1.00 21.66 ? 147 PHE A CD2 1 
ATOM   1176 C CE1 . PHE A 1 147 ? 31.995 -15.200 1.933   1.00 22.72 ? 147 PHE A CE1 1 
ATOM   1177 C CE2 . PHE A 1 147 ? 29.993 -15.850 3.077   1.00 21.45 ? 147 PHE A CE2 1 
ATOM   1178 C CZ  . PHE A 1 147 ? 31.366 -15.963 2.900   1.00 21.07 ? 147 PHE A CZ  1 
ATOM   1179 N N   . GLY A 1 148 ? 27.797 -12.832 -2.855  1.00 25.41 ? 148 GLY A N   1 
ATOM   1180 C CA  . GLY A 1 148 ? 27.002 -11.859 -3.580  1.00 25.30 ? 148 GLY A CA  1 
ATOM   1181 C C   . GLY A 1 148 ? 27.103 -10.446 -3.050  1.00 24.65 ? 148 GLY A C   1 
ATOM   1182 O O   . GLY A 1 148 ? 26.203 -9.636  -3.301  1.00 25.70 ? 148 GLY A O   1 
ATOM   1183 N N   . PHE A 1 149 ? 28.187 -10.114 -2.339  1.00 24.25 ? 149 PHE A N   1 
ATOM   1184 C CA  . PHE A 1 149 ? 28.347 -8.817  -1.674  1.00 25.45 ? 149 PHE A CA  1 
ATOM   1185 C C   . PHE A 1 149 ? 29.249 -7.932  -2.524  1.00 21.32 ? 149 PHE A C   1 
ATOM   1186 O O   . PHE A 1 149 ? 30.462 -8.133  -2.564  1.00 21.79 ? 149 PHE A O   1 
ATOM   1187 C CB  . PHE A 1 149 ? 28.923 -9.000  -0.267  1.00 22.95 ? 149 PHE A CB  1 
ATOM   1188 C CG  . PHE A 1 149 ? 29.008 -7.708  0.544   1.00 22.89 ? 149 PHE A CG  1 
ATOM   1189 C CD1 . PHE A 1 149 ? 28.124 -6.636  0.301   1.00 21.61 ? 149 PHE A CD1 1 
ATOM   1190 C CD2 . PHE A 1 149 ? 29.916 -7.590  1.596   1.00 19.88 ? 149 PHE A CD2 1 
ATOM   1191 C CE1 . PHE A 1 149 ? 28.198 -5.475  1.054   1.00 18.47 ? 149 PHE A CE1 1 
ATOM   1192 C CE2 . PHE A 1 149 ? 29.978 -6.441  2.348   1.00 18.30 ? 149 PHE A CE2 1 
ATOM   1193 C CZ  . PHE A 1 149 ? 29.119 -5.383  2.073   1.00 17.71 ? 149 PHE A CZ  1 
ATOM   1194 N N   . GLU A 1 150 ? 28.661 -6.948  -3.189  1.00 22.82 ? 150 GLU A N   1 
ATOM   1195 C CA  . GLU A 1 150 ? 29.391 -6.115  -4.139  1.00 25.85 ? 150 GLU A CA  1 
ATOM   1196 C C   . GLU A 1 150 ? 29.846 -4.822  -3.458  1.00 25.51 ? 150 GLU A C   1 
ATOM   1197 O O   . GLU A 1 150 ? 29.028 -3.956  -3.133  1.00 25.34 ? 150 GLU A O   1 
ATOM   1198 C CB  . GLU A 1 150 ? 28.556 -5.852  -5.392  1.00 28.01 ? 150 GLU A CB  1 
ATOM   1199 C CG  . GLU A 1 150 ? 29.363 -5.416  -6.591  1.00 27.63 ? 150 GLU A CG  1 
ATOM   1200 C CD  . GLU A 1 150 ? 28.485 -4.931  -7.722  1.00 37.09 ? 150 GLU A CD  1 
ATOM   1201 O OE1 . GLU A 1 150 ? 28.305 -5.707  -8.703  1.00 37.15 ? 150 GLU A OE1 1 
ATOM   1202 O OE2 . GLU A 1 150 ? 27.981 -3.780  -7.629  1.00 45.44 ? 150 GLU A OE2 1 
ATOM   1203 N N   . VAL A 1 151 ? 31.151 -4.708  -3.234  1.00 23.62 ? 151 VAL A N   1 
ATOM   1204 C CA  . VAL A 1 151 ? 31.764 -3.515  -2.658  1.00 23.31 ? 151 VAL A CA  1 
ATOM   1205 C C   . VAL A 1 151 ? 32.264 -2.651  -3.812  1.00 24.54 ? 151 VAL A C   1 
ATOM   1206 O O   . VAL A 1 151 ? 33.143 -3.098  -4.581  1.00 22.49 ? 151 VAL A O   1 
ATOM   1207 C CB  . VAL A 1 151 ? 32.904 -3.881  -1.691  1.00 22.53 ? 151 VAL A CB  1 
ATOM   1208 C CG1 . VAL A 1 151 ? 33.499 -2.639  -1.046  1.00 22.16 ? 151 VAL A CG1 1 
ATOM   1209 C CG2 . VAL A 1 151 ? 32.416 -4.857  -0.632  1.00 20.94 ? 151 VAL A CG2 1 
ATOM   1210 N N   . PRO A 1 152 ? 31.748 -1.435  -3.981  1.00 25.96 ? 152 PRO A N   1 
ATOM   1211 C CA  . PRO A 1 152 ? 32.140 -0.612  -5.142  1.00 24.14 ? 152 PRO A CA  1 
ATOM   1212 C C   . PRO A 1 152 ? 33.649 -0.460  -5.203  1.00 22.47 ? 152 PRO A C   1 
ATOM   1213 O O   . PRO A 1 152 ? 34.317 -0.391  -4.159  1.00 24.48 ? 152 PRO A O   1 
ATOM   1214 C CB  . PRO A 1 152 ? 31.474 0.733   -4.827  1.00 25.21 ? 152 PRO A CB  1 
ATOM   1215 C CG  . PRO A 1 152 ? 30.255 0.343   -4.026  1.00 24.08 ? 152 PRO A CG  1 
ATOM   1216 C CD  . PRO A 1 152 ? 30.798 -0.712  -3.104  1.00 22.72 ? 152 PRO A CD  1 
ATOM   1217 N N   . PRO A 1 153 ? 34.225 -0.379  -6.404  1.00 23.26 ? 153 PRO A N   1 
ATOM   1218 C CA  . PRO A 1 153 ? 35.693 -0.318  -6.508  1.00 23.84 ? 153 PRO A CA  1 
ATOM   1219 C C   . PRO A 1 153 ? 36.345 0.830   -5.750  1.00 25.12 ? 153 PRO A C   1 
ATOM   1220 O O   . PRO A 1 153 ? 37.489 0.680   -5.293  1.00 22.20 ? 153 PRO A O   1 
ATOM   1221 C CB  . PRO A 1 153 ? 35.885 -0.222  -8.026  1.00 21.11 ? 153 PRO A CB  1 
ATOM   1222 C CG  . PRO A 1 153 ? 34.692 0.561   -8.392  1.00 21.50 ? 153 PRO A CG  1 
ATOM   1223 C CD  . PRO A 1 153 ? 33.664 -0.311  -7.760  1.00 21.45 ? 153 PRO A CD  1 
ATOM   1224 N N   . SER A 1 154 ? 35.647 1.964   -5.581  1.00 26.39 ? 154 SER A N   1 
ATOM   1225 C CA  . SER A 1 154 ? 36.195 3.149   -4.918  1.00 26.11 ? 154 SER A CA  1 
ATOM   1226 C C   . SER A 1 154 ? 36.215 3.054   -3.386  1.00 27.21 ? 154 SER A C   1 
ATOM   1227 O O   . SER A 1 154 ? 36.892 3.873   -2.732  1.00 27.44 ? 154 SER A O   1 
ATOM   1228 C CB  . SER A 1 154 ? 35.421 4.393   -5.375  1.00 24.78 ? 154 SER A CB  1 
ATOM   1229 O OG  . SER A 1 154 ? 34.040 4.249   -5.106  1.00 23.39 ? 154 SER A OG  1 
ATOM   1230 N N   . LYS A 1 155 ? 35.501 2.092   -2.794  1.00 23.04 ? 155 LYS A N   1 
ATOM   1231 C CA  . LYS A 1 155 ? 35.474 1.943   -1.353  1.00 21.24 ? 155 LYS A CA  1 
ATOM   1232 C C   . LYS A 1 155 ? 36.617 1.041   -0.932  1.00 21.67 ? 155 LYS A C   1 
ATOM   1233 O O   . LYS A 1 155 ? 36.870 0.016   -1.562  1.00 22.70 ? 155 LYS A O   1 
ATOM   1234 C CB  . LYS A 1 155 ? 34.152 1.310   -0.926  1.00 22.51 ? 155 LYS A CB  1 
ATOM   1235 C CG  . LYS A 1 155 ? 33.926 1.303   0.578   1.00 23.05 ? 155 LYS A CG  1 
ATOM   1236 C CD  . LYS A 1 155 ? 32.476 0.982   0.877   1.00 21.98 ? 155 LYS A CD  1 
ATOM   1237 C CE  . LYS A 1 155 ? 32.188 1.075   2.346   1.00 21.23 ? 155 LYS A CE  1 
ATOM   1238 N NZ  . LYS A 1 155 ? 30.758 0.844   2.620   1.00 19.66 ? 155 LYS A NZ  1 
ATOM   1239 N N   . GLU A 1 156 ? 37.305 1.418   0.140   1.00 23.36 ? 156 GLU A N   1 
ATOM   1240 C CA  . GLU A 1 156 ? 38.452 0.633   0.569   1.00 23.88 ? 156 GLU A CA  1 
ATOM   1241 C C   . GLU A 1 156 ? 37.972 -0.607  1.305   1.00 22.04 ? 156 GLU A C   1 
ATOM   1242 O O   . GLU A 1 156 ? 37.001 -0.553  2.063   1.00 21.11 ? 156 GLU A O   1 
ATOM   1243 C CB  . GLU A 1 156 ? 39.376 1.418   1.492   1.00 22.05 ? 156 GLU A CB  1 
ATOM   1244 C CG  . GLU A 1 156 ? 40.580 0.552   1.871   1.00 23.89 ? 156 GLU A CG  1 
ATOM   1245 C CD  . GLU A 1 156 ? 41.526 1.211   2.836   1.00 26.65 ? 156 GLU A CD  1 
ATOM   1246 O OE1 . GLU A 1 156 ? 41.187 2.301   3.353   1.00 28.40 ? 156 GLU A OE1 1 
ATOM   1247 O OE2 . GLU A 1 156 ? 42.603 0.629   3.093   1.00 27.28 ? 156 GLU A OE2 1 
ATOM   1248 N N   . ILE A 1 157 ? 38.651 -1.731  1.062   1.00 21.68 ? 157 ILE A N   1 
ATOM   1249 C CA  . ILE A 1 157 ? 38.476 -2.949  1.846   1.00 23.19 ? 157 ILE A CA  1 
ATOM   1250 C C   . ILE A 1 157 ? 39.735 -3.228  2.659   1.00 20.68 ? 157 ILE A C   1 
ATOM   1251 O O   . ILE A 1 157 ? 40.848 -3.284  2.112   1.00 21.55 ? 157 ILE A O   1 
ATOM   1252 C CB  . ILE A 1 157 ? 38.068 -4.158  0.991   1.00 22.52 ? 157 ILE A CB  1 
ATOM   1253 C CG1 . ILE A 1 157 ? 36.752 -3.863  0.276   1.00 22.50 ? 157 ILE A CG1 1 
ATOM   1254 C CG2 . ILE A 1 157 ? 37.954 -5.424  1.868   1.00 19.93 ? 157 ILE A CG2 1 
ATOM   1255 C CD1 . ILE A 1 157 ? 36.378 -4.945  -0.663  1.00 22.45 ? 157 ILE A CD1 1 
ATOM   1256 N N   . LYS A 1 158 ? 39.550 -3.388  3.964   1.00 18.78 ? 158 LYS A N   1 
ATOM   1257 C CA  . LYS A 1 158 ? 40.621 -3.655  4.903   1.00 18.04 ? 158 LYS A CA  1 
ATOM   1258 C C   . LYS A 1 158 ? 40.387 -5.064  5.405   1.00 17.33 ? 158 LYS A C   1 
ATOM   1259 O O   . LYS A 1 158 ? 39.358 -5.330  6.026   1.00 17.33 ? 158 LYS A O   1 
ATOM   1260 C CB  . LYS A 1 158 ? 40.565 -2.681  6.082   1.00 19.54 ? 158 LYS A CB  1 
ATOM   1261 C CG  . LYS A 1 158 ? 40.828 -1.206  5.739   1.00 19.68 ? 158 LYS A CG  1 
ATOM   1262 C CD  . LYS A 1 158 ? 40.751 -0.326  7.004   1.00 20.40 ? 158 LYS A CD  1 
ATOM   1263 C CE  . LYS A 1 158 ? 40.968 1.151   6.669   1.00 24.05 ? 158 LYS A CE  1 
ATOM   1264 N NZ  . LYS A 1 158 ? 42.363 1.405   6.118   1.00 28.09 ? 158 LYS A NZ  1 
ATOM   1265 N N   . VAL A 1 159 ? 41.323 -5.964  5.123   1.00 16.42 ? 159 VAL A N   1 
ATOM   1266 C CA  . VAL A 1 159 ? 41.244 -7.354  5.580   1.00 16.29 ? 159 VAL A CA  1 
ATOM   1267 C C   . VAL A 1 159 ? 42.086 -7.515  6.832   1.00 15.80 ? 159 VAL A C   1 
ATOM   1268 O O   . VAL A 1 159 ? 43.251 -7.102  6.860   1.00 15.91 ? 159 VAL A O   1 
ATOM   1269 C CB  . VAL A 1 159 ? 41.659 -8.350  4.484   1.00 14.54 ? 159 VAL A CB  1 
ATOM   1270 C CG1 . VAL A 1 159 ? 41.509 -9.775  5.007   1.00 16.24 ? 159 VAL A CG1 1 
ATOM   1271 C CG2 . VAL A 1 159 ? 40.788 -8.150  3.239   1.00 15.03 ? 159 VAL A CG2 1 
ATOM   1272 N N   . TRP A 1 160 ? 41.484 -8.060  7.886   1.00 15.64 ? 160 TRP A N   1 
ATOM   1273 C CA  . TRP A 1 160 ? 42.152 -8.203  9.165   1.00 16.71 ? 160 TRP A CA  1 
ATOM   1274 C C   . TRP A 1 160 ? 42.521 -9.672  9.318   1.00 18.39 ? 160 TRP A C   1 
ATOM   1275 O O   . TRP A 1 160 ? 41.642 -10.525 9.454   1.00 19.48 ? 160 TRP A O   1 
ATOM   1276 C CB  . TRP A 1 160 ? 41.305 -7.680  10.335  1.00 14.96 ? 160 TRP A CB  1 
ATOM   1277 C CG  . TRP A 1 160 ? 40.959 -6.185  10.254  1.00 16.91 ? 160 TRP A CG  1 
ATOM   1278 C CD1 . TRP A 1 160 ? 40.014 -5.582  9.435   1.00 16.93 ? 160 TRP A CD1 1 
ATOM   1279 C CD2 . TRP A 1 160 ? 41.588 -5.117  10.989  1.00 18.42 ? 160 TRP A CD2 1 
ATOM   1280 N NE1 . TRP A 1 160 ? 40.014 -4.220  9.645   1.00 16.97 ? 160 TRP A NE1 1 
ATOM   1281 C CE2 . TRP A 1 160 ? 40.967 -3.908  10.585  1.00 17.28 ? 160 TRP A CE2 1 
ATOM   1282 C CE3 . TRP A 1 160 ? 42.608 -5.067  11.969  1.00 17.74 ? 160 TRP A CE3 1 
ATOM   1283 C CZ2 . TRP A 1 160 ? 41.343 -2.665  11.122  1.00 18.50 ? 160 TRP A CZ2 1 
ATOM   1284 C CZ3 . TRP A 1 160 ? 42.968 -3.839  12.506  1.00 16.68 ? 160 TRP A CZ3 1 
ATOM   1285 C CH2 . TRP A 1 160 ? 42.343 -2.658  12.083  1.00 17.08 ? 160 TRP A CH2 1 
ATOM   1286 N N   . ASP A 1 161 ? 43.822 -9.964  9.271   1.00 18.87 ? 161 ASP A N   1 
ATOM   1287 C CA  . ASP A 1 161 ? 44.360 -11.316 9.434   1.00 17.08 ? 161 ASP A CA  1 
ATOM   1288 C C   . ASP A 1 161 ? 44.756 -11.442 10.890  1.00 15.49 ? 161 ASP A C   1 
ATOM   1289 O O   . ASP A 1 161 ? 45.772 -10.880 11.314  1.00 16.51 ? 161 ASP A O   1 
ATOM   1290 C CB  . ASP A 1 161 ? 45.573 -11.502 8.520   1.00 16.19 ? 161 ASP A CB  1 
ATOM   1291 C CG  . ASP A 1 161 ? 46.030 -12.970 8.433   1.00 18.12 ? 161 ASP A CG  1 
ATOM   1292 O OD1 . ASP A 1 161 ? 45.418 -13.821 9.122   1.00 16.54 ? 161 ASP A OD1 1 
ATOM   1293 O OD2 . ASP A 1 161 ? 46.993 -13.272 7.678   1.00 16.41 ? 161 ASP A OD2 1 
ATOM   1294 N N   . SER A 1 162 ? 43.950 -12.154 11.674  1.00 15.94 ? 162 SER A N   1 
ATOM   1295 C CA  . SER A 1 162 ? 44.209 -12.239 13.120  1.00 17.77 ? 162 SER A CA  1 
ATOM   1296 C C   . SER A 1 162 ? 45.260 -13.318 13.378  1.00 17.89 ? 162 SER A C   1 
ATOM   1297 O O   . SER A 1 162 ? 44.967 -14.520 13.476  1.00 17.54 ? 162 SER A O   1 
ATOM   1298 C CB  . SER A 1 162 ? 42.937 -12.399 13.964  1.00 18.13 ? 162 SER A CB  1 
ATOM   1299 O OG  . SER A 1 162 ? 42.365 -13.678 13.862  1.00 19.22 ? 162 SER A OG  1 
ATOM   1300 N N   . SER A 1 163 ? 46.512 -12.865 13.440  1.00 16.19 ? 163 SER A N   1 
ATOM   1301 C CA  . SER A 1 163 ? 47.680 -13.698 13.686  1.00 16.22 ? 163 SER A CA  1 
ATOM   1302 C C   . SER A 1 163 ? 48.054 -13.751 15.154  1.00 14.78 ? 163 SER A C   1 
ATOM   1303 O O   . SER A 1 163 ? 48.909 -14.560 15.537  1.00 13.28 ? 163 SER A O   1 
ATOM   1304 C CB  . SER A 1 163 ? 48.854 -13.171 12.832  1.00 16.86 ? 163 SER A CB  1 
ATOM   1305 O OG  . SER A 1 163 ? 49.049 -11.762 13.040  1.00 14.95 ? 163 SER A OG  1 
ATOM   1306 N N   . SER A 1 164 ? 47.430 -12.916 15.979  1.00 13.53 ? 164 SER A N   1 
ATOM   1307 C CA  . SER A 1 164 ? 47.698 -12.842 17.408  1.00 15.21 ? 164 SER A CA  1 
ATOM   1308 C C   . SER A 1 164 ? 46.442 -13.249 18.197  1.00 16.53 ? 164 SER A C   1 
ATOM   1309 O O   . SER A 1 164 ? 45.464 -13.764 17.626  1.00 17.17 ? 164 SER A O   1 
ATOM   1310 C CB  . SER A 1 164 ? 48.269 -11.461 17.795  1.00 17.09 ? 164 SER A CB  1 
ATOM   1311 O OG  . SER A 1 164 ? 47.250 -10.466 17.891  1.00 18.23 ? 164 SER A OG  1 
ATOM   1312 N N   . GLU A 1 165 ? 46.494 -13.071 19.521  1.00 14.75 ? 165 GLU A N   1 
ATOM   1313 C CA  . GLU A 1 165 ? 45.337 -13.354 20.352  1.00 14.23 ? 165 GLU A CA  1 
ATOM   1314 C C   . GLU A 1 165 ? 44.352 -12.206 20.362  1.00 16.61 ? 165 GLU A C   1 
ATOM   1315 O O   . GLU A 1 165 ? 43.319 -12.289 21.039  1.00 15.85 ? 165 GLU A O   1 
ATOM   1316 C CB  . GLU A 1 165 ? 45.755 -13.734 21.771  1.00 16.59 ? 165 GLU A CB  1 
ATOM   1317 C CG  . GLU A 1 165 ? 46.328 -15.139 21.826  1.00 16.81 ? 165 GLU A CG  1 
ATOM   1318 C CD  . GLU A 1 165 ? 45.396 -16.154 21.142  1.00 17.02 ? 165 GLU A CD  1 
ATOM   1319 O OE1 . GLU A 1 165 ? 44.334 -16.469 21.729  1.00 19.04 ? 165 GLU A OE1 1 
ATOM   1320 O OE2 . GLU A 1 165 ? 45.694 -16.598 20.020  1.00 17.61 ? 165 GLU A OE2 1 
ATOM   1321 N N   . MET A 1 166 ? 44.669 -11.135 19.639  1.00 17.43 ? 166 MET A N   1 
ATOM   1322 C CA  . MET A 1 166 ? 43.718 -10.062 19.436  1.00 17.60 ? 166 MET A CA  1 
ATOM   1323 C C   . MET A 1 166 ? 42.640 -10.594 18.485  1.00 15.73 ? 166 MET A C   1 
ATOM   1324 O O   . MET A 1 166 ? 42.930 -11.285 17.502  1.00 14.11 ? 166 MET A O   1 
ATOM   1325 C CB  . MET A 1 166 ? 44.453 -8.876  18.809  1.00 16.94 ? 166 MET A CB  1 
ATOM   1326 C CG  . MET A 1 166 ? 43.610 -7.633  18.679  1.00 21.01 ? 166 MET A CG  1 
ATOM   1327 S SD  . MET A 1 166 ? 43.196 -7.129  20.381  1.00 26.06 ? 166 MET A SD  1 
ATOM   1328 C CE  . MET A 1 166 ? 44.784 -7.412  21.178  1.00 13.02 ? 166 MET A CE  1 
ATOM   1329 N N   . ARG A 1 167 ? 41.383 -10.317 18.808  1.00 16.01 ? 167 ARG A N   1 
ATOM   1330 C CA  . ARG A 1 167 ? 40.250 -10.837 18.047  1.00 17.27 ? 167 ARG A CA  1 
ATOM   1331 C C   . ARG A 1 167 ? 39.510 -9.654  17.441  1.00 16.99 ? 167 ARG A C   1 
ATOM   1332 O O   . ARG A 1 167 ? 39.018 -8.787  18.168  1.00 18.97 ? 167 ARG A O   1 
ATOM   1333 C CB  . ARG A 1 167 ? 39.310 -11.630 18.963  1.00 16.26 ? 167 ARG A CB  1 
ATOM   1334 C CG  . ARG A 1 167 ? 39.883 -12.927 19.551  1.00 15.25 ? 167 ARG A CG  1 
ATOM   1335 C CD  . ARG A 1 167 ? 39.920 -14.073 18.501  1.00 16.49 ? 167 ARG A CD  1 
ATOM   1336 N NE  . ARG A 1 167 ? 40.754 -15.191 18.940  1.00 16.15 ? 167 ARG A NE  1 
ATOM   1337 C CZ  . ARG A 1 167 ? 42.043 -15.332 18.674  1.00 17.04 ? 167 ARG A CZ  1 
ATOM   1338 N NH1 . ARG A 1 167 ? 42.674 -14.501 17.856  1.00 16.46 ? 167 ARG A NH1 1 
ATOM   1339 N NH2 . ARG A 1 167 ? 42.716 -16.334 19.244  1.00 16.54 ? 167 ARG A NH2 1 
ATOM   1340 N N   . PHE A 1 168 ? 39.427 -9.616  16.125  1.00 15.90 ? 168 PHE A N   1 
ATOM   1341 C CA  . PHE A 1 168 ? 38.771 -8.513  15.436  1.00 18.57 ? 168 PHE A CA  1 
ATOM   1342 C C   . PHE A 1 168 ? 37.334 -8.911  15.108  1.00 18.16 ? 168 PHE A C   1 
ATOM   1343 O O   . PHE A 1 168 ? 37.077 -10.038 14.674  1.00 17.84 ? 168 PHE A O   1 
ATOM   1344 C CB  . PHE A 1 168 ? 39.533 -8.178  14.155  1.00 18.13 ? 168 PHE A CB  1 
ATOM   1345 C CG  . PHE A 1 168 ? 41.001 -7.956  14.382  1.00 20.08 ? 168 PHE A CG  1 
ATOM   1346 C CD1 . PHE A 1 168 ? 41.454 -6.820  15.043  1.00 20.88 ? 168 PHE A CD1 1 
ATOM   1347 C CD2 . PHE A 1 168 ? 41.936 -8.917  13.969  1.00 19.02 ? 168 PHE A CD2 1 
ATOM   1348 C CE1 . PHE A 1 168 ? 42.842 -6.628  15.272  1.00 22.13 ? 168 PHE A CE1 1 
ATOM   1349 C CE2 . PHE A 1 168 ? 43.304 -8.733  14.180  1.00 18.76 ? 168 PHE A CE2 1 
ATOM   1350 C CZ  . PHE A 1 168 ? 43.763 -7.591  14.830  1.00 20.36 ? 168 PHE A CZ  1 
ATOM   1351 N N   . VAL A 1 169 ? 36.405 -7.979  15.317  1.00 17.58 ? 169 VAL A N   1 
ATOM   1352 C CA  . VAL A 1 169 ? 34.987 -8.202  15.069  1.00 15.83 ? 169 VAL A CA  1 
ATOM   1353 C C   . VAL A 1 169 ? 34.479 -6.959  14.341  1.00 16.80 ? 169 VAL A C   1 
ATOM   1354 O O   . VAL A 1 169 ? 34.766 -5.836  14.765  1.00 16.91 ? 169 VAL A O   1 
ATOM   1355 C CB  . VAL A 1 169 ? 34.247 -8.402  16.416  1.00 16.37 ? 169 VAL A CB  1 
ATOM   1356 C CG1 . VAL A 1 169 ? 32.884 -9.049  16.216  1.00 17.66 ? 169 VAL A CG1 1 
ATOM   1357 C CG2 . VAL A 1 169 ? 35.093 -9.206  17.429  1.00 15.55 ? 169 VAL A CG2 1 
ATOM   1358 N N   . VAL A 1 170 ? 33.753 -7.142  13.242  1.00 15.65 ? 170 VAL A N   1 
ATOM   1359 C CA  . VAL A 1 170 ? 33.216 -6.001  12.498  1.00 15.01 ? 170 VAL A CA  1 
ATOM   1360 C C   . VAL A 1 170 ? 31.931 -5.499  13.154  1.00 16.62 ? 170 VAL A C   1 
ATOM   1361 O O   . VAL A 1 170 ? 31.051 -6.286  13.553  1.00 18.11 ? 170 VAL A O   1 
ATOM   1362 C CB  . VAL A 1 170 ? 33.005 -6.353  11.010  1.00 16.36 ? 170 VAL A CB  1 
ATOM   1363 C CG1 . VAL A 1 170 ? 32.429 -5.172  10.243  1.00 15.87 ? 170 VAL A CG1 1 
ATOM   1364 C CG2 . VAL A 1 170 ? 34.317 -6.763  10.372  1.00 15.25 ? 170 VAL A CG2 1 
ATOM   1365 N N   . LEU A 1 171 ? 31.823 -4.175  13.282  1.00 16.09 ? 171 LEU A N   1 
ATOM   1366 C CA  . LEU A 1 171 ? 30.586 -3.493  13.638  1.00 16.99 ? 171 LEU A CA  1 
ATOM   1367 C C   . LEU A 1 171 ? 29.903 -3.081  12.341  1.00 17.61 ? 171 LEU A C   1 
ATOM   1368 O O   . LEU A 1 171 ? 30.331 -2.109  11.714  1.00 17.18 ? 171 LEU A O   1 
ATOM   1369 C CB  . LEU A 1 171 ? 30.896 -2.251  14.473  1.00 17.38 ? 171 LEU A CB  1 
ATOM   1370 C CG  . LEU A 1 171 ? 29.706 -1.348  14.800  1.00 17.85 ? 171 LEU A CG  1 
ATOM   1371 C CD1 . LEU A 1 171 ? 28.622 -2.141  15.514  1.00 17.05 ? 171 LEU A CD1 1 
ATOM   1372 C CD2 . LEU A 1 171 ? 30.139 -0.156  15.635  1.00 17.37 ? 171 LEU A CD2 1 
ATOM   1373 N N   . PRO A 1 172 ? 28.861 -3.788  11.892  1.00 17.80 ? 172 PRO A N   1 
ATOM   1374 C CA  . PRO A 1 172 ? 28.243 -3.449  10.601  1.00 17.60 ? 172 PRO A CA  1 
ATOM   1375 C C   . PRO A 1 172 ? 27.482 -2.131  10.663  1.00 16.91 ? 172 PRO A C   1 
ATOM   1376 O O   . PRO A 1 172 ? 26.980 -1.739  11.716  1.00 17.44 ? 172 PRO A O   1 
ATOM   1377 C CB  . PRO A 1 172 ? 27.270 -4.611  10.368  1.00 18.67 ? 172 PRO A CB  1 
ATOM   1378 C CG  . PRO A 1 172 ? 26.836 -4.964  11.773  1.00 17.98 ? 172 PRO A CG  1 
ATOM   1379 C CD  . PRO A 1 172 ? 28.142 -4.888  12.562  1.00 16.36 ? 172 PRO A CD  1 
ATOM   1380 N N   . GLN A 1 173 ? 27.388 -1.463  9.500   1.00 19.29 ? 173 GLN A N   1 
ATOM   1381 C CA  . GLN A 1 173 ? 26.559 -0.264  9.357   1.00 20.60 ? 173 GLN A CA  1 
ATOM   1382 C C   . GLN A 1 173 ? 25.072 -0.597  9.520   1.00 19.90 ? 173 GLN A C   1 
ATOM   1383 O O   . GLN A 1 173 ? 24.553 -1.548  8.912   1.00 19.62 ? 173 GLN A O   1 
ATOM   1384 C CB  . GLN A 1 173 ? 26.773 0.379   7.986   1.00 18.90 ? 173 GLN A CB  1 
ATOM   1385 C CG  . GLN A 1 173 ? 27.945 1.343   7.860   1.00 19.59 ? 173 GLN A CG  1 
ATOM   1386 C CD  . GLN A 1 173 ? 27.930 2.081   6.511   1.00 22.44 ? 173 GLN A CD  1 
ATOM   1387 O OE1 . GLN A 1 173 ? 28.198 1.490   5.456   1.00 20.87 ? 173 GLN A OE1 1 
ATOM   1388 N NE2 . GLN A 1 173 ? 27.601 3.374   6.544   1.00 22.18 ? 173 GLN A NE2 1 
ATOM   1389 N N   . ARG A 1 174 ? 24.380 0.227   10.306  1.00 20.38 ? 174 ARG A N   1 
ATOM   1390 C CA  . ARG A 1 174 ? 22.956 0.025   10.545  1.00 19.69 ? 174 ARG A CA  1 
ATOM   1391 C C   . ARG A 1 174 ? 22.185 0.182   9.237   1.00 22.39 ? 174 ARG A C   1 
ATOM   1392 O O   . ARG A 1 174 ? 22.427 1.139   8.487   1.00 22.54 ? 174 ARG A O   1 
ATOM   1393 C CB  . ARG A 1 174 ? 22.482 1.047   11.567  1.00 18.88 ? 174 ARG A CB  1 
ATOM   1394 C CG  . ARG A 1 174 ? 21.027 0.939   11.928  1.00 20.35 ? 174 ARG A CG  1 
ATOM   1395 C CD  . ARG A 1 174 ? 20.732 1.925   13.048  1.00 23.89 ? 174 ARG A CD  1 
ATOM   1396 N NE  . ARG A 1 174 ? 19.324 2.003   13.436  1.00 22.44 ? 174 ARG A NE  1 
ATOM   1397 C CZ  . ARG A 1 174 ? 18.885 2.550   14.562  1.00 20.29 ? 174 ARG A CZ  1 
ATOM   1398 N NH1 . ARG A 1 174 ? 19.719 3.058   15.457  1.00 20.73 ? 174 ARG A NH1 1 
ATOM   1399 N NH2 . ARG A 1 174 ? 17.577 2.595   14.787  1.00 19.89 ? 174 ARG A NH2 1 
ATOM   1400 N N   . PRO A 1 175 ? 21.280 -0.737  8.908   1.00 22.41 ? 175 PRO A N   1 
ATOM   1401 C CA  . PRO A 1 175 ? 20.572 -0.626  7.630   1.00 24.17 ? 175 PRO A CA  1 
ATOM   1402 C C   . PRO A 1 175 ? 19.703 0.624   7.612   1.00 23.53 ? 175 PRO A C   1 
ATOM   1403 O O   . PRO A 1 175 ? 19.116 1.011   8.636   1.00 23.10 ? 175 PRO A O   1 
ATOM   1404 C CB  . PRO A 1 175 ? 19.710 -1.901  7.600   1.00 22.06 ? 175 PRO A CB  1 
ATOM   1405 C CG  . PRO A 1 175 ? 20.499 -2.864  8.379   1.00 22.54 ? 175 PRO A CG  1 
ATOM   1406 C CD  . PRO A 1 175 ? 20.972 -2.019  9.565   1.00 23.93 ? 175 PRO A CD  1 
ATOM   1407 N N   . ALA A 1 176 ? 19.631 1.252   6.432   1.00 21.63 ? 176 ALA A N   1 
ATOM   1408 C CA  . ALA A 1 176 ? 18.686 2.339   6.230   1.00 23.95 ? 176 ALA A CA  1 
ATOM   1409 C C   . ALA A 1 176 ? 17.253 1.837   6.451   1.00 25.50 ? 176 ALA A C   1 
ATOM   1410 O O   . ALA A 1 176 ? 16.952 0.654   6.265   1.00 23.41 ? 176 ALA A O   1 
ATOM   1411 C CB  . ALA A 1 176 ? 18.844 2.903   4.819   1.00 22.44 ? 176 ALA A CB  1 
ATOM   1412 N N   . GLY A 1 177 ? 16.366 2.750   6.878   1.00 26.77 ? 177 GLY A N   1 
ATOM   1413 C CA  . GLY A 1 177 ? 14.968 2.431   7.131   1.00 25.24 ? 177 GLY A CA  1 
ATOM   1414 C C   . GLY A 1 177 ? 14.639 1.890   8.510   1.00 23.66 ? 177 GLY A C   1 
ATOM   1415 O O   . GLY A 1 177 ? 13.506 1.447   8.742   1.00 23.94 ? 177 GLY A O   1 
ATOM   1416 N N   . THR A 1 178 ? 15.582 1.912   9.439   1.00 22.64 ? 178 THR A N   1 
ATOM   1417 C CA  . THR A 1 178 ? 15.382 1.331   10.757  1.00 23.23 ? 178 THR A CA  1 
ATOM   1418 C C   . THR A 1 178 ? 15.293 2.385   11.846  1.00 24.27 ? 178 THR A C   1 
ATOM   1419 O O   . THR A 1 178 ? 15.554 2.078   13.016  1.00 22.41 ? 178 THR A O   1 
ATOM   1420 C CB  . THR A 1 178 ? 16.488 0.312   11.055  1.00 23.98 ? 178 THR A CB  1 
ATOM   1421 O OG1 . THR A 1 178 ? 17.776 0.968   10.982  1.00 23.09 ? 178 THR A OG1 1 
ATOM   1422 C CG2 . THR A 1 178 ? 16.420 -0.871  10.071  1.00 23.10 ? 178 THR A CG2 1 
ATOM   1423 N N   . ASP A 1 179 ? 14.937 3.624   11.478  1.00 25.61 ? 179 ASP A N   1 
ATOM   1424 C CA  . ASP A 1 179 ? 14.890 4.712   12.449  1.00 23.33 ? 179 ASP A CA  1 
ATOM   1425 C C   . ASP A 1 179 ? 13.851 4.399   13.521  1.00 24.70 ? 179 ASP A C   1 
ATOM   1426 O O   . ASP A 1 179 ? 12.727 3.980   13.218  1.00 24.43 ? 179 ASP A O   1 
ATOM   1427 C CB  . ASP A 1 179 ? 14.572 6.041   11.760  1.00 27.53 ? 179 ASP A CB  1 
ATOM   1428 C CG  . ASP A 1 179 ? 15.591 6.407   10.631  1.00 34.86 ? 179 ASP A CG  1 
ATOM   1429 O OD1 . ASP A 1 179 ? 16.777 5.983   10.697  1.00 31.84 ? 179 ASP A OD1 1 
ATOM   1430 O OD2 . ASP A 1 179 ? 15.209 7.156   9.689   1.00 40.44 ? 179 ASP A OD2 1 
ATOM   1431 N N   . GLY A 1 180 ? 14.252 4.563   14.782  1.00 24.05 ? 180 GLY A N   1 
ATOM   1432 C CA  . GLY A 1 180 ? 13.410 4.317   15.938  1.00 22.85 ? 180 GLY A CA  1 
ATOM   1433 C C   . GLY A 1 180 ? 13.168 2.868   16.302  1.00 21.79 ? 180 GLY A C   1 
ATOM   1434 O O   . GLY A 1 180 ? 12.416 2.612   17.245  1.00 22.42 ? 180 GLY A O   1 
ATOM   1435 N N   . TRP A 1 181 ? 13.769 1.909   15.592  1.00 26.22 ? 181 TRP A N   1 
ATOM   1436 C CA  . TRP A 1 181 ? 13.533 0.500   15.898  1.00 23.24 ? 181 TRP A CA  1 
ATOM   1437 C C   . TRP A 1 181 ? 13.995 0.186   17.307  1.00 22.34 ? 181 TRP A C   1 
ATOM   1438 O O   . TRP A 1 181 ? 14.952 0.780   17.813  1.00 22.57 ? 181 TRP A O   1 
ATOM   1439 C CB  . TRP A 1 181 ? 14.262 -0.422  14.909  1.00 22.83 ? 181 TRP A CB  1 
ATOM   1440 C CG  . TRP A 1 181 ? 13.591 -0.574  13.573  1.00 24.76 ? 181 TRP A CG  1 
ATOM   1441 C CD1 . TRP A 1 181 ? 12.761 0.332   12.945  1.00 25.78 ? 181 TRP A CD1 1 
ATOM   1442 C CD2 . TRP A 1 181 ? 13.636 -1.722  12.723  1.00 23.43 ? 181 TRP A CD2 1 
ATOM   1443 N NE1 . TRP A 1 181 ? 12.332 -0.174  11.740  1.00 23.59 ? 181 TRP A NE1 1 
ATOM   1444 C CE2 . TRP A 1 181 ? 12.852 -1.432  11.581  1.00 23.55 ? 181 TRP A CE2 1 
ATOM   1445 C CE3 . TRP A 1 181 ? 14.285 -2.952  12.799  1.00 22.25 ? 181 TRP A CE3 1 
ATOM   1446 C CZ2 . TRP A 1 181 ? 12.703 -2.331  10.534  1.00 23.40 ? 181 TRP A CZ2 1 
ATOM   1447 C CZ3 . TRP A 1 181 ? 14.128 -3.853  11.746  1.00 22.55 ? 181 TRP A CZ3 1 
ATOM   1448 C CH2 . TRP A 1 181 ? 13.345 -3.537  10.638  1.00 24.12 ? 181 TRP A CH2 1 
ATOM   1449 N N   . SER A 1 182 ? 13.282 -0.740  17.951  1.00 22.63 ? 182 SER A N   1 
ATOM   1450 C CA  . SER A 1 182 ? 13.727 -1.278  19.229  1.00 23.61 ? 182 SER A CA  1 
ATOM   1451 C C   . SER A 1 182 ? 14.981 -2.130  19.035  1.00 21.99 ? 182 SER A C   1 
ATOM   1452 O O   . SER A 1 182 ? 15.285 -2.596  17.929  1.00 22.60 ? 182 SER A O   1 
ATOM   1453 C CB  . SER A 1 182 ? 12.624 -2.127  19.838  1.00 22.77 ? 182 SER A CB  1 
ATOM   1454 O OG  . SER A 1 182 ? 12.384 -3.232  18.997  1.00 24.40 ? 182 SER A OG  1 
ATOM   1455 N N   . GLU A 1 183 ? 15.731 -2.308  20.123  1.00 20.94 ? 183 GLU A N   1 
ATOM   1456 C CA  . GLU A 1 183 ? 16.937 -3.134  20.053  1.00 23.24 ? 183 GLU A CA  1 
ATOM   1457 C C   . GLU A 1 183 ? 16.614 -4.560  19.604  1.00 23.88 ? 183 GLU A C   1 
ATOM   1458 O O   . GLU A 1 183 ? 17.300 -5.118  18.736  1.00 23.92 ? 183 GLU A O   1 
ATOM   1459 C CB  . GLU A 1 183 ? 17.665 -3.122  21.399  1.00 24.20 ? 183 GLU A CB  1 
ATOM   1460 C CG  . GLU A 1 183 ? 18.462 -1.838  21.634  1.00 24.51 ? 183 GLU A CG  1 
ATOM   1461 C CD  . GLU A 1 183 ? 19.151 -1.804  22.969  1.00 25.16 ? 183 GLU A CD  1 
ATOM   1462 O OE1 . GLU A 1 183 ? 20.312 -2.293  23.055  1.00 25.98 ? 183 GLU A OE1 1 
ATOM   1463 O OE2 . GLU A 1 183 ? 18.534 -1.270  23.920  1.00 23.43 ? 183 GLU A OE2 1 
ATOM   1464 N N   . GLU A 1 184 ? 15.569 -5.166  20.190  1.00 25.23 ? 184 GLU A N   1 
ATOM   1465 C CA  . GLU A 1 184 ? 15.119 -6.506  19.788  1.00 26.87 ? 184 GLU A CA  1 
ATOM   1466 C C   . GLU A 1 184 ? 14.900 -6.608  18.286  1.00 25.62 ? 184 GLU A C   1 
ATOM   1467 O O   . GLU A 1 184 ? 15.327 -7.572  17.639  1.00 23.81 ? 184 GLU A O   1 
ATOM   1468 C CB  . GLU A 1 184 ? 13.790 -6.792  20.465  1.00 28.62 ? 184 GLU A CB  1 
ATOM   1469 C CG  . GLU A 1 184 ? 13.146 -8.049  19.977  1.00 30.11 ? 184 GLU A CG  1 
ATOM   1470 C CD  . GLU A 1 184 ? 12.782 -8.945  21.119  1.00 36.77 ? 184 GLU A CD  1 
ATOM   1471 O OE1 . GLU A 1 184 ? 13.437 -8.833  22.187  1.00 35.73 ? 184 GLU A OE1 1 
ATOM   1472 O OE2 . GLU A 1 184 ? 11.816 -9.730  20.957  1.00 41.90 ? 184 GLU A OE2 1 
ATOM   1473 N N   . GLU A 1 185 ? 14.191 -5.619  17.734  1.00 25.66 ? 185 GLU A N   1 
ATOM   1474 C CA  . GLU A 1 185 ? 13.790 -5.614  16.337  1.00 23.32 ? 185 GLU A CA  1 
ATOM   1475 C C   . GLU A 1 185 ? 15.001 -5.457  15.430  1.00 21.00 ? 185 GLU A C   1 
ATOM   1476 O O   . GLU A 1 185 ? 15.060 -6.077  14.361  1.00 19.31 ? 185 GLU A O   1 
ATOM   1477 C CB  . GLU A 1 185 ? 12.848 -4.432  16.169  1.00 23.91 ? 185 GLU A CB  1 
ATOM   1478 C CG  . GLU A 1 185 ? 11.502 -4.651  16.837  1.00 27.53 ? 185 GLU A CG  1 
ATOM   1479 C CD  . GLU A 1 185 ? 10.531 -3.518  16.566  1.00 34.52 ? 185 GLU A CD  1 
ATOM   1480 O OE1 . GLU A 1 185 ? 10.989 -2.484  16.021  1.00 33.74 ? 185 GLU A OE1 1 
ATOM   1481 O OE2 . GLU A 1 185 ? 9.330  -3.638  16.935  1.00 34.77 ? 185 GLU A OE2 1 
ATOM   1482 N N   . LEU A 1 186 ? 15.971 -4.622  15.851  1.00 21.77 ? 186 LEU A N   1 
ATOM   1483 C CA  . LEU A 1 186 ? 17.193 -4.396  15.082  1.00 21.42 ? 186 LEU A CA  1 
ATOM   1484 C C   . LEU A 1 186 ? 18.085 -5.635  15.057  1.00 21.04 ? 186 LEU A C   1 
ATOM   1485 O O   . LEU A 1 186 ? 18.751 -5.899  14.042  1.00 18.95 ? 186 LEU A O   1 
ATOM   1486 C CB  . LEU A 1 186 ? 17.968 -3.192  15.640  1.00 21.76 ? 186 LEU A CB  1 
ATOM   1487 C CG  . LEU A 1 186 ? 17.530 -1.730  15.430  1.00 20.15 ? 186 LEU A CG  1 
ATOM   1488 C CD1 . LEU A 1 186 ? 18.343 -0.810  16.357  1.00 19.46 ? 186 LEU A CD1 1 
ATOM   1489 C CD2 . LEU A 1 186 ? 17.673 -1.292  13.990  1.00 17.67 ? 186 LEU A CD2 1 
ATOM   1490 N N   . ALA A 1 187 ? 18.112 -6.399  16.170  1.00 22.51 ? 187 ALA A N   1 
ATOM   1491 C CA  . ALA A 1 187 ? 18.972 -7.590  16.274  1.00 23.35 ? 187 ALA A CA  1 
ATOM   1492 C C   . ALA A 1 187 ? 18.660 -8.627  15.194  1.00 22.63 ? 187 ALA A C   1 
ATOM   1493 O O   . ALA A 1 187 ? 19.561 -9.363  14.756  1.00 21.75 ? 187 ALA A O   1 
ATOM   1494 C CB  . ALA A 1 187 ? 18.836 -8.231  17.657  1.00 20.17 ? 187 ALA A CB  1 
ATOM   1495 N N   . THR A 1 188 ? 17.388 -8.714  14.770  1.00 23.52 ? 188 THR A N   1 
ATOM   1496 C CA  . THR A 1 188 ? 16.995 -9.614  13.695  1.00 20.63 ? 188 THR A CA  1 
ATOM   1497 C C   . THR A 1 188 ? 17.773 -9.341  12.418  1.00 21.35 ? 188 THR A C   1 
ATOM   1498 O O   . THR A 1 188 ? 17.899 -10.236 11.575  1.00 21.20 ? 188 THR A O   1 
ATOM   1499 C CB  . THR A 1 188 ? 15.488 -9.515  13.481  1.00 19.64 ? 188 THR A CB  1 
ATOM   1500 O OG1 . THR A 1 188 ? 15.159 -8.220  12.955  1.00 21.53 ? 188 THR A OG1 1 
ATOM   1501 C CG2 . THR A 1 188 ? 14.748 -9.718  14.806  1.00 20.34 ? 188 THR A CG2 1 
ATOM   1502 N N   . LEU A 1 189 ? 18.330 -8.138  12.272  1.00 20.26 ? 189 LEU A N   1 
ATOM   1503 C CA  . LEU A 1 189 ? 19.112 -7.775  11.101  1.00 20.53 ? 189 LEU A CA  1 
ATOM   1504 C C   . LEU A 1 189 ? 20.605 -8.102  11.229  1.00 19.06 ? 189 LEU A C   1 
ATOM   1505 O O   . LEU A 1 189 ? 21.327 -8.009  10.225  1.00 19.97 ? 189 LEU A O   1 
ATOM   1506 C CB  . LEU A 1 189 ? 18.911 -6.275  10.771  1.00 23.74 ? 189 LEU A CB  1 
ATOM   1507 C CG  . LEU A 1 189 ? 17.502 -5.678  10.626  1.00 21.65 ? 189 LEU A CG  1 
ATOM   1508 C CD1 . LEU A 1 189 ? 17.550 -4.199  10.322  1.00 20.50 ? 189 LEU A CD1 1 
ATOM   1509 C CD2 . LEU A 1 189 ? 16.765 -6.402  9.511   1.00 22.03 ? 189 LEU A CD2 1 
ATOM   1510 N N   . VAL A 1 190 ? 21.086 -8.465  12.424  1.00 20.18 ? 190 VAL A N   1 
ATOM   1511 C CA  . VAL A 1 190 ? 22.509 -8.714  12.664  1.00 18.37 ? 190 VAL A CA  1 
ATOM   1512 C C   . VAL A 1 190 ? 22.793 -10.203 12.525  1.00 18.33 ? 190 VAL A C   1 
ATOM   1513 O O   . VAL A 1 190 ? 22.146 -11.031 13.177  1.00 20.59 ? 190 VAL A O   1 
ATOM   1514 C CB  . VAL A 1 190 ? 22.943 -8.204  14.043  1.00 17.90 ? 190 VAL A CB  1 
ATOM   1515 C CG1 . VAL A 1 190 ? 24.466 -8.286  14.186  1.00 15.77 ? 190 VAL A CG1 1 
ATOM   1516 C CG2 . VAL A 1 190 ? 22.430 -6.767  14.273  1.00 20.73 ? 190 VAL A CG2 1 
ATOM   1517 N N   . THR A 1 191 ? 23.779 -10.540 11.696  1.00 18.43 ? 191 THR A N   1 
ATOM   1518 C CA  . THR A 1 191 ? 24.144 -11.917 11.390  1.00 18.42 ? 191 THR A CA  1 
ATOM   1519 C C   . THR A 1 191 ? 25.624 -12.163 11.660  1.00 19.56 ? 191 THR A C   1 
ATOM   1520 O O   . THR A 1 191 ? 26.449 -11.241 11.642  1.00 17.25 ? 191 THR A O   1 
ATOM   1521 C CB  . THR A 1 191 ? 23.852 -12.279 9.918   1.00 20.03 ? 191 THR A CB  1 
ATOM   1522 O OG1 . THR A 1 191 ? 24.611 -11.434 9.027   1.00 17.68 ? 191 THR A OG1 1 
ATOM   1523 C CG2 . THR A 1 191 ? 22.368 -12.162 9.616   1.00 19.39 ? 191 THR A CG2 1 
ATOM   1524 N N   . ARG A 1 192 ? 25.941 -13.437 11.928  1.00 19.37 ? 192 ARG A N   1 
ATOM   1525 C CA  . ARG A 1 192 ? 27.325 -13.914 11.939  1.00 21.13 ? 192 ARG A CA  1 
ATOM   1526 C C   . ARG A 1 192 ? 28.134 -13.322 10.789  1.00 16.73 ? 192 ARG A C   1 
ATOM   1527 O O   . ARG A 1 192 ? 29.210 -12.744 10.986  1.00 16.04 ? 192 ARG A O   1 
ATOM   1528 C CB  . ARG A 1 192 ? 27.279 -15.446 11.814  1.00 20.86 ? 192 ARG A CB  1 
ATOM   1529 C CG  . ARG A 1 192 ? 28.449 -16.155 12.408  1.00 19.85 ? 192 ARG A CG  1 
ATOM   1530 C CD  . ARG A 1 192 ? 28.840 -17.367 11.594  1.00 19.53 ? 192 ARG A CD  1 
ATOM   1531 N NE  . ARG A 1 192 ? 28.282 -18.586 12.166  1.00 21.89 ? 192 ARG A NE  1 
ATOM   1532 C CZ  . ARG A 1 192 ? 28.789 -19.227 13.223  1.00 21.41 ? 192 ARG A CZ  1 
ATOM   1533 N NH1 . ARG A 1 192 ? 29.790 -18.710 13.953  1.00 15.44 ? 192 ARG A NH1 1 
ATOM   1534 N NH2 . ARG A 1 192 ? 28.264 -20.404 13.582  1.00 21.69 ? 192 ARG A NH2 1 
ATOM   1535 N N   . GLU A 1 193 ? 27.600 -13.471 9.578   1.00 17.23 ? 193 GLU A N   1 
ATOM   1536 C CA  . GLU A 1 193 ? 28.239 -12.977 8.361   1.00 17.54 ? 193 GLU A CA  1 
ATOM   1537 C C   . GLU A 1 193 ? 28.544 -11.483 8.461   1.00 18.31 ? 193 GLU A C   1 
ATOM   1538 O O   . GLU A 1 193 ? 29.579 -11.023 7.962   1.00 16.74 ? 193 GLU A O   1 
ATOM   1539 C CB  . GLU A 1 193 ? 27.300 -13.230 7.176   1.00 18.34 ? 193 GLU A CB  1 
ATOM   1540 C CG  . GLU A 1 193 ? 27.158 -14.698 6.793   1.00 20.55 ? 193 GLU A CG  1 
ATOM   1541 C CD  . GLU A 1 193 ? 26.429 -15.533 7.854   1.00 20.74 ? 193 GLU A CD  1 
ATOM   1542 O OE1 . GLU A 1 193 ? 25.600 -14.993 8.632   1.00 18.02 ? 193 GLU A OE1 1 
ATOM   1543 O OE2 . GLU A 1 193 ? 26.710 -16.751 7.913   1.00 24.88 ? 193 GLU A OE2 1 
ATOM   1544 N N   . SER A 1 194 ? 27.644 -10.702 9.083   1.00 17.42 ? 194 SER A N   1 
ATOM   1545 C CA  . SER A 1 194 ? 27.846 -9.252  9.103   1.00 17.95 ? 194 SER A CA  1 
ATOM   1546 C C   . SER A 1 194 ? 28.938 -8.840  10.102  1.00 17.82 ? 194 SER A C   1 
ATOM   1547 O O   . SER A 1 194 ? 29.601 -7.816  9.899   1.00 16.27 ? 194 SER A O   1 
ATOM   1548 C CB  . SER A 1 194 ? 26.525 -8.501  9.368   1.00 17.46 ? 194 SER A CB  1 
ATOM   1549 O OG  . SER A 1 194 ? 26.090 -8.651  10.710  1.00 16.30 ? 194 SER A OG  1 
ATOM   1550 N N   . MET A 1 195 ? 29.157 -9.623  11.160  1.00 16.08 ? 195 MET A N   1 
ATOM   1551 C CA  . MET A 1 195 ? 30.241 -9.343  12.092  1.00 16.47 ? 195 MET A CA  1 
ATOM   1552 C C   . MET A 1 195 ? 31.568 -10.001 11.704  1.00 15.90 ? 195 MET A C   1 
ATOM   1553 O O   . MET A 1 195 ? 32.570 -9.758  12.385  1.00 15.76 ? 195 MET A O   1 
ATOM   1554 C CB  . MET A 1 195 ? 29.849 -9.704  13.525  1.00 16.91 ? 195 MET A CB  1 
ATOM   1555 C CG  . MET A 1 195 ? 28.578 -9.038  14.037  1.00 15.48 ? 195 MET A CG  1 
ATOM   1556 S SD  . MET A 1 195 ? 28.094 -9.691  15.631  1.00 17.56 ? 195 MET A SD  1 
ATOM   1557 C CE  . MET A 1 195 ? 26.796 -10.842 15.117  1.00 17.83 ? 195 MET A CE  1 
ATOM   1558 N N   . ILE A 1 196 ? 31.600 -10.820 10.643  1.00 15.47 ? 196 ILE A N   1 
ATOM   1559 C CA  . ILE A 1 196 ? 32.867 -11.246 10.029  1.00 16.40 ? 196 ILE A CA  1 
ATOM   1560 C C   . ILE A 1 196 ? 33.342 -10.291 8.917   1.00 17.55 ? 196 ILE A C   1 
ATOM   1561 O O   . ILE A 1 196 ? 34.546 -10.243 8.609   1.00 17.21 ? 196 ILE A O   1 
ATOM   1562 C CB  . ILE A 1 196 ? 32.752 -12.677 9.457   1.00 16.22 ? 196 ILE A CB  1 
ATOM   1563 C CG1 . ILE A 1 196 ? 32.521 -13.706 10.552  1.00 15.48 ? 196 ILE A CG1 1 
ATOM   1564 C CG2 . ILE A 1 196 ? 34.000 -13.050 8.618   1.00 16.42 ? 196 ILE A CG2 1 
ATOM   1565 C CD1 . ILE A 1 196 ? 32.275 -15.125 10.009  1.00 13.32 ? 196 ILE A CD1 1 
ATOM   1566 N N   . GLY A 1 197 ? 32.430 -9.517  8.305   1.00 18.02 ? 197 GLY A N   1 
ATOM   1567 C CA  . GLY A 1 197 ? 32.763 -8.703  7.156   1.00 17.26 ? 197 GLY A CA  1 
ATOM   1568 C C   . GLY A 1 197 ? 32.385 -9.306  5.824   1.00 17.33 ? 197 GLY A C   1 
ATOM   1569 O O   . GLY A 1 197 ? 32.548 -8.639  4.795   1.00 17.72 ? 197 GLY A O   1 
ATOM   1570 N N   . VAL A 1 198 ? 31.849 -10.539 5.804   1.00 17.16 ? 198 VAL A N   1 
ATOM   1571 C CA  . VAL A 1 198 ? 31.531 -11.199 4.535   1.00 18.17 ? 198 VAL A CA  1 
ATOM   1572 C C   . VAL A 1 198 ? 30.172 -10.809 3.984   1.00 17.53 ? 198 VAL A C   1 
ATOM   1573 O O   . VAL A 1 198 ? 29.894 -11.087 2.815   1.00 17.91 ? 198 VAL A O   1 
ATOM   1574 C CB  . VAL A 1 198 ? 31.656 -12.732 4.626   1.00 19.88 ? 198 VAL A CB  1 
ATOM   1575 C CG1 . VAL A 1 198 ? 33.127 -13.148 4.873   1.00 18.07 ? 198 VAL A CG1 1 
ATOM   1576 C CG2 . VAL A 1 198 ? 30.725 -13.285 5.693   1.00 18.40 ? 198 VAL A CG2 1 
ATOM   1577 N N   . GLU A 1 199 ? 29.326 -10.171 4.792   1.00 18.33 ? 199 GLU A N   1 
ATOM   1578 C CA  . GLU A 1 199 ? 28.023 -9.658  4.385   1.00 18.94 ? 199 GLU A CA  1 
ATOM   1579 C C   . GLU A 1 199 ? 27.723 -8.391  5.169   1.00 15.72 ? 199 GLU A C   1 
ATOM   1580 O O   . GLU A 1 199 ? 28.183 -8.241  6.306   1.00 15.05 ? 199 GLU A O   1 
ATOM   1581 C CB  . GLU A 1 199 ? 26.920 -10.674 4.703   1.00 17.51 ? 199 GLU A CB  1 
ATOM   1582 C CG  . GLU A 1 199 ? 26.915 -11.870 3.802   1.00 18.97 ? 199 GLU A CG  1 
ATOM   1583 C CD  . GLU A 1 199 ? 25.858 -12.885 4.213   1.00 20.88 ? 199 GLU A CD  1 
ATOM   1584 O OE1 . GLU A 1 199 ? 25.087 -12.584 5.172   1.00 17.37 ? 199 GLU A OE1 1 
ATOM   1585 O OE2 . GLU A 1 199 ? 25.767 -13.937 3.510   1.00 21.44 ? 199 GLU A OE2 1 
ATOM   1586 N N   . PRO A 1 200 ? 26.926 -7.487  4.609   1.00 19.59 ? 200 PRO A N   1 
ATOM   1587 C CA  . PRO A 1 200 ? 26.332 -6.419  5.425   1.00 18.47 ? 200 PRO A CA  1 
ATOM   1588 C C   . PRO A 1 200 ? 25.239 -7.003  6.309   1.00 19.61 ? 200 PRO A C   1 
ATOM   1589 O O   . PRO A 1 200 ? 24.828 -8.164  6.156   1.00 18.05 ? 200 PRO A O   1 
ATOM   1590 C CB  . PRO A 1 200 ? 25.734 -5.486  4.373   1.00 15.64 ? 200 PRO A CB  1 
ATOM   1591 C CG  . PRO A 1 200 ? 25.268 -6.444  3.330   1.00 19.01 ? 200 PRO A CG  1 
ATOM   1592 C CD  . PRO A 1 200 ? 26.422 -7.451  3.223   1.00 19.55 ? 200 PRO A CD  1 
ATOM   1593 N N   . ALA A 1 201 ? 24.794 -6.183  7.272   1.00 20.87 ? 201 ALA A N   1 
ATOM   1594 C CA  . ALA A 1 201 ? 23.594 -6.495  8.057   1.00 22.24 ? 201 ALA A CA  1 
ATOM   1595 C C   . ALA A 1 201 ? 22.403 -6.688  7.108   1.00 21.60 ? 201 ALA A C   1 
ATOM   1596 O O   . ALA A 1 201 ? 22.444 -6.297  5.923   1.00 19.55 ? 201 ALA A O   1 
ATOM   1597 C CB  . ALA A 1 201 ? 23.316 -5.382  9.084   1.00 19.49 ? 201 ALA A CB  1 
ATOM   1598 N N   . LYS A 1 202 ? 21.341 -7.320  7.610   1.00 21.80 ? 202 LYS A N   1 
ATOM   1599 C CA  . LYS A 1 202 ? 20.214 -7.599  6.714   1.00 24.46 ? 202 LYS A CA  1 
ATOM   1600 C C   . LYS A 1 202 ? 19.527 -6.309  6.263   1.00 22.97 ? 202 LYS A C   1 
ATOM   1601 O O   . LYS A 1 202 ? 19.394 -5.346  7.029   1.00 25.42 ? 202 LYS A O   1 
ATOM   1602 C CB  . LYS A 1 202 ? 19.198 -8.549  7.357   1.00 25.23 ? 202 LYS A CB  1 
ATOM   1603 C CG  . LYS A 1 202 ? 19.626 -10.005 7.314   1.00 24.29 ? 202 LYS A CG  1 
ATOM   1604 C CD  . LYS A 1 202 ? 18.765 -10.832 8.252   1.00 26.42 ? 202 LYS A CD  1 
ATOM   1605 C CE  . LYS A 1 202 ? 19.418 -12.162 8.634   1.00 24.64 ? 202 LYS A CE  1 
ATOM   1606 N NZ  . LYS A 1 202 ? 19.558 -12.268 10.125  1.00 24.16 ? 202 LYS A NZ  1 
ATOM   1607 N N   . ALA A 1 203 ? 19.097 -6.291  5.009   1.00 23.18 ? 203 ALA A N   1 
ATOM   1608 C CA  . ALA A 1 203 ? 18.433 -5.115  4.478   1.00 23.45 ? 203 ALA A CA  1 
ATOM   1609 C C   . ALA A 1 203 ? 17.007 -5.041  4.999   1.00 25.73 ? 203 ALA A C   1 
ATOM   1610 O O   . ALA A 1 203 ? 16.487 -5.980  5.611   1.00 26.67 ? 203 ALA A O   1 
ATOM   1611 C CB  . ALA A 1 203 ? 18.419 -5.142  2.957   1.00 21.69 ? 203 ALA A CB  1 
ATOM   1612 N N   . VAL A 1 204 ? 16.389 -3.883  4.774   1.00 30.37 ? 204 VAL A N   1 
ATOM   1613 C CA  . VAL A 1 204 ? 14.974 -3.637  5.086   1.00 30.39 ? 204 VAL A CA  1 
ATOM   1614 C C   . VAL A 1 204 ? 14.716 -3.621  6.587   1.00 28.76 ? 204 VAL A C   1 
ATOM   1615 O O   . VAL A 1 204 ? 14.844 -2.582  7.253   1.00 30.64 ? 204 VAL A O   1 
ATOM   1616 C CB  . VAL A 1 204 ? 14.030 -4.634  4.323   1.00 31.62 ? 204 VAL A CB  1 
ATOM   1617 C CG1 . VAL A 1 204 ? 12.566 -4.411  4.714   1.00 29.33 ? 204 VAL A CG1 1 
ATOM   1618 C CG2 . VAL A 1 204 ? 14.243 -4.523  2.803   1.00 28.39 ? 204 VAL A CG2 1 
ATOM   1619 N N   . MET B 2 1   ? 56.963 -22.587 11.064  1.00 17.27 ? 1   MET B N   1 
ATOM   1620 C CA  . MET B 2 1   ? 57.516 -23.255 9.881   1.00 18.89 ? 1   MET B CA  1 
ATOM   1621 C C   . MET B 2 1   ? 56.878 -22.773 8.597   1.00 17.71 ? 1   MET B C   1 
ATOM   1622 O O   . MET B 2 1   ? 55.824 -22.128 8.598   1.00 15.71 ? 1   MET B O   1 
ATOM   1623 C CB  . MET B 2 1   ? 57.258 -24.773 9.912   1.00 23.64 ? 1   MET B CB  1 
ATOM   1624 C CG  . MET B 2 1   ? 55.770 -25.186 10.135  1.00 23.09 ? 1   MET B CG  1 
ATOM   1625 S SD  . MET B 2 1   ? 55.203 -26.757 9.396   1.00 28.76 ? 1   MET B SD  1 
ATOM   1626 C CE  . MET B 2 1   ? 56.647 -27.833 9.574   1.00 19.90 ? 1   MET B CE  1 
ATOM   1627 N N   . ASN B 2 2   ? 57.503 -23.167 7.492   1.00 16.72 ? 2   ASN B N   1 
ATOM   1628 C CA  . ASN B 2 2   ? 56.982 -22.920 6.156   1.00 17.74 ? 2   ASN B CA  1 
ATOM   1629 C C   . ASN B 2 2   ? 55.983 -24.011 5.744   1.00 19.11 ? 2   ASN B C   1 
ATOM   1630 O O   . ASN B 2 2   ? 56.083 -24.587 4.656   1.00 18.05 ? 2   ASN B O   1 
ATOM   1631 C CB  . ASN B 2 2   ? 58.138 -22.868 5.168   1.00 17.83 ? 2   ASN B CB  1 
ATOM   1632 C CG  . ASN B 2 2   ? 59.072 -21.694 5.406   1.00 19.25 ? 2   ASN B CG  1 
ATOM   1633 O OD1 . ASN B 2 2   ? 58.796 -20.829 6.252   1.00 19.99 ? 2   ASN B OD1 1 
ATOM   1634 N ND2 . ASN B 2 2   ? 60.178 -21.638 4.636   1.00 19.39 ? 2   ASN B ND2 1 
ATOM   1635 N N   . GLY B 2 3   ? 55.005 -24.321 6.624   1.00 18.64 ? 3   GLY B N   1 
ATOM   1636 C CA  . GLY B 2 3   ? 54.066 -25.380 6.329   1.00 17.25 ? 3   GLY B CA  1 
ATOM   1637 C C   . GLY B 2 3   ? 52.921 -24.956 5.424   1.00 16.08 ? 3   GLY B C   1 
ATOM   1638 O O   . GLY B 2 3   ? 52.642 -23.766 5.212   1.00 16.84 ? 3   GLY B O   1 
ATOM   1639 N N   . VAL B 2 4   ? 52.228 -25.973 4.890   1.00 15.58 ? 4   VAL B N   1 
ATOM   1640 C CA  . VAL B 2 4   ? 51.127 -25.728 3.953   1.00 16.04 ? 4   VAL B CA  1 
ATOM   1641 C C   . VAL B 2 4   ? 49.980 -24.989 4.626   1.00 14.54 ? 4   VAL B C   1 
ATOM   1642 O O   . VAL B 2 4   ? 49.214 -24.280 3.960   1.00 16.80 ? 4   VAL B O   1 
ATOM   1643 C CB  . VAL B 2 4   ? 50.660 -27.035 3.264   1.00 16.77 ? 4   VAL B CB  1 
ATOM   1644 C CG1 . VAL B 2 4   ? 49.409 -26.780 2.438   1.00 15.77 ? 4   VAL B CG1 1 
ATOM   1645 C CG2 . VAL B 2 4   ? 51.761 -27.605 2.371   1.00 14.53 ? 4   VAL B CG2 1 
ATOM   1646 N N   . TYR B 2 5   ? 49.840 -25.145 5.942   1.00 14.46 ? 5   TYR B N   1 
ATOM   1647 C CA  . TYR B 2 5   ? 48.790 -24.470 6.691   1.00 14.62 ? 5   TYR B CA  1 
ATOM   1648 C C   . TYR B 2 5   ? 48.830 -22.947 6.491   1.00 14.99 ? 5   TYR B C   1 
ATOM   1649 O O   . TYR B 2 5   ? 47.790 -22.281 6.567   1.00 13.69 ? 5   TYR B O   1 
ATOM   1650 C CB  . TYR B 2 5   ? 48.970 -24.815 8.166   1.00 13.63 ? 5   TYR B CB  1 
ATOM   1651 C CG  . TYR B 2 5   ? 50.134 -24.064 8.781   1.00 15.69 ? 5   TYR B CG  1 
ATOM   1652 C CD1 . TYR B 2 5   ? 51.427 -24.562 8.695   1.00 15.09 ? 5   TYR B CD1 1 
ATOM   1653 C CD2 . TYR B 2 5   ? 49.943 -22.820 9.397   1.00 15.13 ? 5   TYR B CD2 1 
ATOM   1654 C CE1 . TYR B 2 5   ? 52.499 -23.857 9.234   1.00 16.32 ? 5   TYR B CE1 1 
ATOM   1655 C CE2 . TYR B 2 5   ? 50.995 -22.117 9.933   1.00 14.54 ? 5   TYR B CE2 1 
ATOM   1656 C CZ  . TYR B 2 5   ? 52.275 -22.626 9.849   1.00 17.35 ? 5   TYR B CZ  1 
ATOM   1657 O OH  . TYR B 2 5   ? 53.323 -21.908 10.409  1.00 18.33 ? 5   TYR B OH  1 
ATOM   1658 N N   . ASP B 2 6   ? 50.022 -22.380 6.265   1.00 15.44 ? 6   ASP B N   1 
ATOM   1659 C CA  . ASP B 2 6   ? 50.219 -20.941 6.036   1.00 15.51 ? 6   ASP B CA  1 
ATOM   1660 C C   . ASP B 2 6   ? 49.747 -20.623 4.614   1.00 15.04 ? 6   ASP B C   1 
ATOM   1661 O O   . ASP B 2 6   ? 50.526 -20.491 3.659   1.00 14.72 ? 6   ASP B O   1 
ATOM   1662 C CB  . ASP B 2 6   ? 51.686 -20.604 6.290   1.00 16.52 ? 6   ASP B CB  1 
ATOM   1663 C CG  . ASP B 2 6   ? 52.072 -19.194 5.881   1.00 17.52 ? 6   ASP B CG  1 
ATOM   1664 O OD1 . ASP B 2 6   ? 51.200 -18.306 5.692   1.00 13.89 ? 6   ASP B OD1 1 
ATOM   1665 O OD2 . ASP B 2 6   ? 53.305 -18.999 5.708   1.00 18.34 ? 6   ASP B OD2 1 
ATOM   1666 N N   . VAL B 2 7   ? 48.416 -20.516 4.471   1.00 15.88 ? 7   VAL B N   1 
ATOM   1667 C CA  . VAL B 2 7   ? 47.760 -20.533 3.148   1.00 15.79 ? 7   VAL B CA  1 
ATOM   1668 C C   . VAL B 2 7   ? 47.449 -19.144 2.579   1.00 14.70 ? 7   VAL B C   1 
ATOM   1669 O O   . VAL B 2 7   ? 46.999 -19.049 1.419   1.00 13.53 ? 7   VAL B O   1 
ATOM   1670 C CB  . VAL B 2 7   ? 46.478 -21.403 3.145   1.00 16.40 ? 7   VAL B CB  1 
ATOM   1671 C CG1 . VAL B 2 7   ? 46.804 -22.814 3.598   1.00 14.93 ? 7   VAL B CG1 1 
ATOM   1672 C CG2 . VAL B 2 7   ? 45.397 -20.773 4.068   1.00 13.58 ? 7   VAL B CG2 1 
ATOM   1673 N N   . GLY B 2 8   ? 47.666 -18.073 3.352   1.00 16.11 ? 8   GLY B N   1 
ATOM   1674 C CA  . GLY B 2 8   ? 47.400 -16.735 2.850   1.00 14.45 ? 8   GLY B CA  1 
ATOM   1675 C C   . GLY B 2 8   ? 48.112 -16.462 1.549   1.00 14.96 ? 8   GLY B C   1 
ATOM   1676 O O   . GLY B 2 8   ? 49.332 -16.583 1.463   1.00 15.52 ? 8   GLY B O   1 
ATOM   1677 N N   . GLY B 2 9   ? 47.360 -16.110 0.519   1.00 15.74 ? 9   GLY B N   1 
ATOM   1678 C CA  . GLY B 2 9   ? 47.938 -15.815 -0.779  1.00 16.22 ? 9   GLY B CA  1 
ATOM   1679 C C   . GLY B 2 9   ? 48.127 -17.002 -1.694  1.00 15.93 ? 9   GLY B C   1 
ATOM   1680 O O   . GLY B 2 9   ? 48.557 -16.804 -2.840  1.00 16.67 ? 9   GLY B O   1 
ATOM   1681 N N   . THR B 2 10  ? 47.811 -18.220 -1.229  1.00 15.12 ? 10  THR B N   1 
ATOM   1682 C CA  . THR B 2 10  ? 47.880 -19.408 -2.072  1.00 15.49 ? 10  THR B CA  1 
ATOM   1683 C C   . THR B 2 10  ? 46.749 -19.432 -3.108  1.00 16.09 ? 10  THR B C   1 
ATOM   1684 O O   . THR B 2 10  ? 45.603 -19.072 -2.819  1.00 17.79 ? 10  THR B O   1 
ATOM   1685 C CB  . THR B 2 10  ? 47.820 -20.660 -1.192  1.00 15.84 ? 10  THR B CB  1 
ATOM   1686 O OG1 . THR B 2 10  ? 48.998 -20.736 -0.390  1.00 17.46 ? 10  THR B OG1 1 
ATOM   1687 C CG2 . THR B 2 10  ? 47.717 -21.927 -2.042  1.00 17.07 ? 10  THR B CG2 1 
ATOM   1688 N N   . ASP B 2 11  ? 47.067 -19.851 -4.317  1.00 14.81 ? 11  ASP B N   1 
ATOM   1689 C CA  . ASP B 2 11  ? 46.065 -20.011 -5.346  1.00 16.83 ? 11  ASP B CA  1 
ATOM   1690 C C   . ASP B 2 11  ? 45.656 -21.481 -5.490  1.00 17.66 ? 11  ASP B C   1 
ATOM   1691 O O   . ASP B 2 11  ? 46.308 -22.398 -4.983  1.00 16.83 ? 11  ASP B O   1 
ATOM   1692 C CB  . ASP B 2 11  ? 46.562 -19.469 -6.692  1.00 18.02 ? 11  ASP B CB  1 
ATOM   1693 C CG  . ASP B 2 11  ? 46.730 -17.983 -6.691  1.00 19.06 ? 11  ASP B CG  1 
ATOM   1694 O OD1 . ASP B 2 11  ? 45.947 -17.311 -5.983  1.00 20.22 ? 11  ASP B OD1 1 
ATOM   1695 O OD2 . ASP B 2 11  ? 47.605 -17.485 -7.422  1.00 18.05 ? 11  ASP B OD2 1 
ATOM   1696 N N   . GLY B 2 12  ? 44.551 -21.690 -6.209  1.00 17.53 ? 12  GLY B N   1 
ATOM   1697 C CA  . GLY B 2 12  ? 44.193 -23.010 -6.694  1.00 16.10 ? 12  GLY B CA  1 
ATOM   1698 C C   . GLY B 2 12  ? 43.650 -23.954 -5.655  1.00 16.37 ? 12  GLY B C   1 
ATOM   1699 O O   . GLY B 2 12  ? 43.660 -25.171 -5.893  1.00 15.86 ? 12  GLY B O   1 
ATOM   1700 N N   . LEU B 2 13  ? 43.188 -23.435 -4.504  1.00 14.52 ? 13  LEU B N   1 
ATOM   1701 C CA  . LEU B 2 13  ? 42.599 -24.271 -3.459  1.00 16.77 ? 13  LEU B CA  1 
ATOM   1702 C C   . LEU B 2 13  ? 41.119 -24.608 -3.703  1.00 18.70 ? 13  LEU B C   1 
ATOM   1703 O O   . LEU B 2 13  ? 40.588 -25.531 -3.060  1.00 17.99 ? 13  LEU B O   1 
ATOM   1704 C CB  . LEU B 2 13  ? 42.805 -23.654 -2.068  1.00 17.68 ? 13  LEU B CB  1 
ATOM   1705 C CG  . LEU B 2 13  ? 44.271 -23.371 -1.720  1.00 20.15 ? 13  LEU B CG  1 
ATOM   1706 C CD1 . LEU B 2 13  ? 44.505 -23.121 -0.221  1.00 18.45 ? 13  LEU B CD1 1 
ATOM   1707 C CD2 . LEU B 2 13  ? 45.168 -24.504 -2.218  1.00 20.72 ? 13  LEU B CD2 1 
ATOM   1708 N N   . GLY B 2 14  ? 40.454 -23.890 -4.615  1.00 18.26 ? 14  GLY B N   1 
ATOM   1709 C CA  . GLY B 2 14  ? 39.110 -24.213 -5.025  1.00 18.16 ? 14  GLY B CA  1 
ATOM   1710 C C   . GLY B 2 14  ? 38.077 -23.325 -4.377  1.00 16.26 ? 14  GLY B C   1 
ATOM   1711 O O   . GLY B 2 14  ? 38.370 -22.540 -3.474  1.00 16.32 ? 14  GLY B O   1 
ATOM   1712 N N   . PRO B 2 15  ? 36.828 -23.455 -4.820  1.00 19.64 ? 15  PRO B N   1 
ATOM   1713 C CA  . PRO B 2 15  ? 35.768 -22.563 -4.323  1.00 18.55 ? 15  PRO B CA  1 
ATOM   1714 C C   . PRO B 2 15  ? 35.352 -22.917 -2.909  1.00 17.85 ? 15  PRO B C   1 
ATOM   1715 O O   . PRO B 2 15  ? 35.555 -24.028 -2.413  1.00 18.07 ? 15  PRO B O   1 
ATOM   1716 C CB  . PRO B 2 15  ? 34.617 -22.791 -5.313  1.00 19.60 ? 15  PRO B CB  1 
ATOM   1717 C CG  . PRO B 2 15  ? 34.813 -24.250 -5.694  1.00 20.21 ? 15  PRO B CG  1 
ATOM   1718 C CD  . PRO B 2 15  ? 36.323 -24.367 -5.867  1.00 18.29 ? 15  PRO B CD  1 
ATOM   1719 N N   . ILE B 2 16  ? 34.769 -21.919 -2.246  1.00 21.78 ? 16  ILE B N   1 
ATOM   1720 C CA  . ILE B 2 16  ? 34.391 -22.060 -0.850  1.00 20.82 ? 16  ILE B CA  1 
ATOM   1721 C C   . ILE B 2 16  ? 33.186 -22.986 -0.771  1.00 21.68 ? 16  ILE B C   1 
ATOM   1722 O O   . ILE B 2 16  ? 32.200 -22.805 -1.501  1.00 21.16 ? 16  ILE B O   1 
ATOM   1723 C CB  . ILE B 2 16  ? 34.081 -20.679 -0.260  1.00 18.91 ? 16  ILE B CB  1 
ATOM   1724 C CG1 . ILE B 2 16  ? 35.352 -19.826 -0.250  1.00 18.69 ? 16  ILE B CG1 1 
ATOM   1725 C CG2 . ILE B 2 16  ? 33.514 -20.815 1.142   1.00 18.16 ? 16  ILE B CG2 1 
ATOM   1726 C CD1 . ILE B 2 16  ? 35.141 -18.394 0.165   1.00 19.08 ? 16  ILE B CD1 1 
ATOM   1727 N N   . ASN B 2 17  ? 33.266 -24.003 0.085   1.00 19.47 ? 17  ASN B N   1 
ATOM   1728 C CA  . ASN B 2 17  ? 32.139 -24.907 0.282   1.00 24.21 ? 17  ASN B CA  1 
ATOM   1729 C C   . ASN B 2 17  ? 31.380 -24.403 1.496   1.00 21.58 ? 17  ASN B C   1 
ATOM   1730 O O   . ASN B 2 17  ? 31.895 -24.430 2.617   1.00 21.62 ? 17  ASN B O   1 
ATOM   1731 C CB  . ASN B 2 17  ? 32.565 -26.358 0.493   1.00 26.19 ? 17  ASN B CB  1 
ATOM   1732 C CG  . ASN B 2 17  ? 31.351 -27.298 0.744   1.00 33.08 ? 17  ASN B CG  1 
ATOM   1733 O OD1 . ASN B 2 17  ? 30.252 -27.093 0.183   1.00 31.84 ? 17  ASN B OD1 1 
ATOM   1734 N ND2 . ASN B 2 17  ? 31.544 -28.315 1.605   1.00 35.45 ? 17  ASN B ND2 1 
ATOM   1735 N N   . ARG B 2 18  ? 30.157 -23.941 1.279   1.00 22.95 ? 18  ARG B N   1 
ATOM   1736 C CA  . ARG B 2 18  ? 29.414 -23.257 2.334   1.00 23.22 ? 18  ARG B CA  1 
ATOM   1737 C C   . ARG B 2 18  ? 27.958 -23.703 2.243   1.00 25.28 ? 18  ARG B C   1 
ATOM   1738 O O   . ARG B 2 18  ? 27.175 -23.188 1.425   1.00 24.96 ? 18  ARG B O   1 
ATOM   1739 C CB  . ARG B 2 18  ? 29.590 -21.744 2.197   1.00 22.20 ? 18  ARG B CB  1 
ATOM   1740 C CG  . ARG B 2 18  ? 28.920 -20.876 3.221   1.00 21.12 ? 18  ARG B CG  1 
ATOM   1741 C CD  . ARG B 2 18  ? 29.396 -19.438 2.999   1.00 21.59 ? 18  ARG B CD  1 
ATOM   1742 N NE  . ARG B 2 18  ? 28.946 -18.842 1.738   1.00 23.57 ? 18  ARG B NE  1 
ATOM   1743 C CZ  . ARG B 2 18  ? 27.906 -18.019 1.623   1.00 22.63 ? 18  ARG B CZ  1 
ATOM   1744 N NH1 . ARG B 2 18  ? 27.159 -17.689 2.671   1.00 23.80 ? 18  ARG B NH1 1 
ATOM   1745 N NH2 . ARG B 2 18  ? 27.602 -17.522 0.431   1.00 22.30 ? 18  ARG B NH2 1 
ATOM   1746 N N   . PRO B 2 19  ? 27.580 -24.723 3.014   1.00 23.74 ? 19  PRO B N   1 
ATOM   1747 C CA  . PRO B 2 19  ? 26.169 -25.105 3.069   1.00 25.09 ? 19  PRO B CA  1 
ATOM   1748 C C   . PRO B 2 19  ? 25.337 -23.911 3.514   1.00 27.67 ? 19  PRO B C   1 
ATOM   1749 O O   . PRO B 2 19  ? 25.827 -23.010 4.203   1.00 30.48 ? 19  PRO B O   1 
ATOM   1750 C CB  . PRO B 2 19  ? 26.162 -26.213 4.127   1.00 24.37 ? 19  PRO B CB  1 
ATOM   1751 C CG  . PRO B 2 19  ? 27.541 -26.802 4.002   1.00 25.03 ? 19  PRO B CG  1 
ATOM   1752 C CD  . PRO B 2 19  ? 28.411 -25.612 3.846   1.00 21.97 ? 19  PRO B CD  1 
ATOM   1753 N N   . ALA B 2 20  ? 24.072 -23.890 3.099   1.00 25.99 ? 20  ALA B N   1 
ATOM   1754 C CA  . ALA B 2 20  ? 23.169 -22.857 3.593   1.00 28.28 ? 20  ALA B CA  1 
ATOM   1755 C C   . ALA B 2 20  ? 23.037 -22.886 5.125   1.00 27.85 ? 20  ALA B C   1 
ATOM   1756 O O   . ALA B 2 20  ? 22.671 -21.870 5.738   1.00 28.57 ? 20  ALA B O   1 
ATOM   1757 C CB  . ALA B 2 20  ? 21.798 -22.990 2.909   1.00 29.24 ? 20  ALA B CB  1 
ATOM   1758 N N   . ASP B 2 21  ? 23.324 -24.017 5.765   1.00 26.40 ? 21  ASP B N   1 
ATOM   1759 C CA  . ASP B 2 21  ? 23.319 -24.055 7.218   1.00 24.50 ? 21  ASP B CA  1 
ATOM   1760 C C   . ASP B 2 21  ? 23.998 -25.351 7.641   1.00 23.35 ? 21  ASP B C   1 
ATOM   1761 O O   . ASP B 2 21  ? 24.175 -26.264 6.833   1.00 25.30 ? 21  ASP B O   1 
ATOM   1762 C CB  . ASP B 2 21  ? 21.894 -23.967 7.761   1.00 24.21 ? 21  ASP B CB  1 
ATOM   1763 C CG  . ASP B 2 21  ? 21.833 -23.483 9.202   1.00 30.45 ? 21  ASP B CG  1 
ATOM   1764 O OD1 . ASP B 2 21  ? 22.789 -22.822 9.688   1.00 31.90 ? 21  ASP B OD1 1 
ATOM   1765 O OD2 . ASP B 2 21  ? 20.810 -23.770 9.868   1.00 31.97 ? 21  ASP B OD2 1 
ATOM   1766 N N   . GLU B 2 22  ? 24.378 -25.418 8.905   1.00 25.17 ? 22  GLU B N   1 
ATOM   1767 C CA  . GLU B 2 22  ? 25.112 -26.568 9.429   1.00 25.62 ? 22  GLU B CA  1 
ATOM   1768 C C   . GLU B 2 22  ? 25.122 -26.572 10.956  1.00 20.75 ? 22  GLU B C   1 
ATOM   1769 O O   . GLU B 2 22  ? 25.103 -25.513 11.598  1.00 21.69 ? 22  GLU B O   1 
ATOM   1770 C CB  . GLU B 2 22  ? 26.569 -26.527 8.956   1.00 27.45 ? 22  GLU B CB  1 
ATOM   1771 C CG  . GLU B 2 22  ? 27.332 -25.325 9.505   1.00 23.73 ? 22  GLU B CG  1 
ATOM   1772 C CD  . GLU B 2 22  ? 28.715 -25.221 8.939   1.00 20.84 ? 22  GLU B CD  1 
ATOM   1773 O OE1 . GLU B 2 22  ? 28.872 -25.292 7.713   1.00 23.42 ? 22  GLU B OE1 1 
ATOM   1774 O OE2 . GLU B 2 22  ? 29.651 -25.098 9.735   1.00 20.94 ? 22  GLU B OE2 1 
ATOM   1775 N N   . PRO B 2 23  ? 25.185 -27.738 11.581  1.00 23.08 ? 23  PRO B N   1 
ATOM   1776 C CA  . PRO B 2 23  ? 25.152 -27.789 13.046  1.00 21.23 ? 23  PRO B CA  1 
ATOM   1777 C C   . PRO B 2 23  ? 26.516 -27.423 13.600  1.00 21.27 ? 23  PRO B C   1 
ATOM   1778 O O   . PRO B 2 23  ? 27.540 -27.487 12.909  1.00 20.28 ? 23  PRO B O   1 
ATOM   1779 C CB  . PRO B 2 23  ? 24.857 -29.268 13.333  1.00 19.62 ? 23  PRO B CB  1 
ATOM   1780 C CG  . PRO B 2 23  ? 25.648 -29.957 12.229  1.00 22.25 ? 23  PRO B CG  1 
ATOM   1781 C CD  . PRO B 2 23  ? 25.373 -29.083 10.987  1.00 22.98 ? 23  PRO B CD  1 
ATOM   1782 N N   . VAL B 2 24  ? 26.512 -27.040 14.876  1.00 18.91 ? 24  VAL B N   1 
ATOM   1783 C CA  . VAL B 2 24  ? 27.775 -26.782 15.558  1.00 19.38 ? 24  VAL B CA  1 
ATOM   1784 C C   . VAL B 2 24  ? 28.693 -27.987 15.411  1.00 21.32 ? 24  VAL B C   1 
ATOM   1785 O O   . VAL B 2 24  ? 29.805 -27.884 14.865  1.00 20.58 ? 24  VAL B O   1 
ATOM   1786 C CB  . VAL B 2 24  ? 27.534 -26.414 17.030  1.00 17.79 ? 24  VAL B CB  1 
ATOM   1787 C CG1 . VAL B 2 24  ? 28.847 -26.275 17.742  1.00 18.55 ? 24  VAL B CG1 1 
ATOM   1788 C CG2 . VAL B 2 24  ? 26.764 -25.119 17.109  1.00 19.16 ? 24  VAL B CG2 1 
ATOM   1789 N N   . PHE B 2 25  ? 28.218 -29.154 15.875  1.00 20.37 ? 25  PHE B N   1 
ATOM   1790 C CA  . PHE B 2 25  ? 28.953 -30.419 15.831  1.00 19.42 ? 25  PHE B CA  1 
ATOM   1791 C C   . PHE B 2 25  ? 28.266 -31.343 14.841  1.00 19.64 ? 25  PHE B C   1 
ATOM   1792 O O   . PHE B 2 25  ? 27.064 -31.610 14.955  1.00 20.42 ? 25  PHE B O   1 
ATOM   1793 C CB  . PHE B 2 25  ? 29.007 -31.042 17.209  1.00 15.30 ? 25  PHE B CB  1 
ATOM   1794 C CG  . PHE B 2 25  ? 29.727 -30.207 18.177  1.00 16.90 ? 25  PHE B CG  1 
ATOM   1795 C CD1 . PHE B 2 25  ? 31.100 -30.011 18.040  1.00 18.60 ? 25  PHE B CD1 1 
ATOM   1796 C CD2 . PHE B 2 25  ? 29.048 -29.559 19.200  1.00 18.84 ? 25  PHE B CD2 1 
ATOM   1797 C CE1 . PHE B 2 25  ? 31.811 -29.221 18.948  1.00 17.87 ? 25  PHE B CE1 1 
ATOM   1798 C CE2 . PHE B 2 25  ? 29.733 -28.758 20.119  1.00 18.41 ? 25  PHE B CE2 1 
ATOM   1799 C CZ  . PHE B 2 25  ? 31.131 -28.594 19.990  1.00 19.59 ? 25  PHE B CZ  1 
ATOM   1800 N N   . ARG B 2 26  ? 29.020 -31.800 13.860  1.00 17.07 ? 26  ARG B N   1 
ATOM   1801 C CA  . ARG B 2 26  ? 28.432 -32.585 12.799  1.00 18.66 ? 26  ARG B CA  1 
ATOM   1802 C C   . ARG B 2 26  ? 28.302 -34.064 13.164  1.00 18.23 ? 26  ARG B C   1 
ATOM   1803 O O   . ARG B 2 26  ? 27.601 -34.795 12.455  1.00 20.49 ? 26  ARG B O   1 
ATOM   1804 C CB  . ARG B 2 26  ? 29.271 -32.377 11.546  1.00 18.55 ? 26  ARG B CB  1 
ATOM   1805 C CG  . ARG B 2 26  ? 29.380 -30.891 11.165  1.00 20.01 ? 26  ARG B CG  1 
ATOM   1806 C CD  . ARG B 2 26  ? 30.256 -30.670 9.917   1.00 20.89 ? 26  ARG B CD  1 
ATOM   1807 N NE  . ARG B 2 26  ? 31.673 -30.899 10.209  1.00 21.07 ? 26  ARG B NE  1 
ATOM   1808 C CZ  . ARG B 2 26  ? 32.658 -30.698 9.344   1.00 20.68 ? 26  ARG B CZ  1 
ATOM   1809 N NH1 . ARG B 2 26  ? 32.430 -30.229 8.132   1.00 22.67 ? 26  ARG B NH1 1 
ATOM   1810 N NH2 . ARG B 2 26  ? 33.908 -30.950 9.712   1.00 21.19 ? 26  ARG B NH2 1 
ATOM   1811 N N   . ALA B 2 27  ? 28.932 -34.504 14.255  1.00 16.78 ? 27  ALA B N   1 
ATOM   1812 C CA  . ALA B 2 27  ? 28.923 -35.901 14.659  1.00 16.64 ? 27  ALA B CA  1 
ATOM   1813 C C   . ALA B 2 27  ? 29.386 -35.966 16.094  1.00 17.57 ? 27  ALA B C   1 
ATOM   1814 O O   . ALA B 2 27  ? 30.075 -35.063 16.577  1.00 18.52 ? 27  ALA B O   1 
ATOM   1815 C CB  . ALA B 2 27  ? 29.841 -36.746 13.769  1.00 16.51 ? 27  ALA B CB  1 
ATOM   1816 N N   . GLU B 2 28  ? 28.992 -37.049 16.782  1.00 19.29 ? 28  GLU B N   1 
ATOM   1817 C CA  . GLU B 2 28  ? 29.403 -37.250 18.174  1.00 17.62 ? 28  GLU B CA  1 
ATOM   1818 C C   . GLU B 2 28  ? 30.911 -37.181 18.365  1.00 16.75 ? 28  GLU B C   1 
ATOM   1819 O O   . GLU B 2 28  ? 31.386 -36.631 19.360  1.00 17.11 ? 28  GLU B O   1 
ATOM   1820 C CB  . GLU B 2 28  ? 28.861 -38.566 18.727  1.00 18.78 ? 28  GLU B CB  1 
ATOM   1821 C CG  . GLU B 2 28  ? 27.395 -38.486 19.059  1.00 20.94 ? 28  GLU B CG  1 
ATOM   1822 C CD  . GLU B 2 28  ? 27.122 -37.299 19.984  1.00 23.03 ? 28  GLU B CD  1 
ATOM   1823 O OE1 . GLU B 2 28  ? 27.493 -37.413 21.166  1.00 23.93 ? 28  GLU B OE1 1 
ATOM   1824 O OE2 . GLU B 2 28  ? 26.556 -36.258 19.539  1.00 24.35 ? 28  GLU B OE2 1 
ATOM   1825 N N   . TRP B 2 29  ? 31.682 -37.767 17.453  1.00 16.48 ? 29  TRP B N   1 
ATOM   1826 C CA  . TRP B 2 29  ? 33.132 -37.705 17.614  1.00 15.96 ? 29  TRP B CA  1 
ATOM   1827 C C   . TRP B 2 29  ? 33.633 -36.260 17.689  1.00 15.16 ? 29  TRP B C   1 
ATOM   1828 O O   . TRP B 2 29  ? 34.599 -35.987 18.414  1.00 15.58 ? 29  TRP B O   1 
ATOM   1829 C CB  . TRP B 2 29  ? 33.858 -38.528 16.535  1.00 15.57 ? 29  TRP B CB  1 
ATOM   1830 C CG  . TRP B 2 29  ? 33.920 -37.918 15.143  1.00 15.17 ? 29  TRP B CG  1 
ATOM   1831 C CD1 . TRP B 2 29  ? 33.114 -38.202 14.090  1.00 13.73 ? 29  TRP B CD1 1 
ATOM   1832 C CD2 . TRP B 2 29  ? 34.873 -36.931 14.673  1.00 15.25 ? 29  TRP B CD2 1 
ATOM   1833 N NE1 . TRP B 2 29  ? 33.499 -37.468 12.984  1.00 14.82 ? 29  TRP B NE1 1 
ATOM   1834 C CE2 . TRP B 2 29  ? 34.576 -36.680 13.321  1.00 15.17 ? 29  TRP B CE2 1 
ATOM   1835 C CE3 . TRP B 2 29  ? 35.951 -36.243 15.269  1.00 14.19 ? 29  TRP B CE3 1 
ATOM   1836 C CZ2 . TRP B 2 29  ? 35.310 -35.762 12.554  1.00 15.36 ? 29  TRP B CZ2 1 
ATOM   1837 C CZ3 . TRP B 2 29  ? 36.683 -35.346 14.500  1.00 12.50 ? 29  TRP B CZ3 1 
ATOM   1838 C CH2 . TRP B 2 29  ? 36.353 -35.106 13.172  1.00 14.22 ? 29  TRP B CH2 1 
ATOM   1839 N N   . GLU B 2 30  ? 32.974 -35.318 16.995  1.00 14.77 ? 30  GLU B N   1 
ATOM   1840 C CA  . GLU B 2 30  ? 33.417 -33.917 17.024  1.00 16.02 ? 30  GLU B CA  1 
ATOM   1841 C C   . GLU B 2 30  ? 33.257 -33.292 18.412  1.00 16.53 ? 30  GLU B C   1 
ATOM   1842 O O   . GLU B 2 30  ? 34.125 -32.532 18.863  1.00 15.45 ? 30  GLU B O   1 
ATOM   1843 C CB  . GLU B 2 30  ? 32.666 -33.095 15.973  1.00 16.70 ? 30  GLU B CB  1 
ATOM   1844 C CG  . GLU B 2 30  ? 33.022 -33.453 14.518  1.00 14.95 ? 30  GLU B CG  1 
ATOM   1845 C CD  . GLU B 2 30  ? 32.540 -32.405 13.534  1.00 15.20 ? 30  GLU B CD  1 
ATOM   1846 O OE1 . GLU B 2 30  ? 31.779 -31.493 13.960  1.00 15.36 ? 30  GLU B OE1 1 
ATOM   1847 O OE2 . GLU B 2 30  ? 32.934 -32.492 12.346  1.00 15.73 ? 30  GLU B OE2 1 
ATOM   1848 N N   . LYS B 2 31  ? 32.152 -33.588 19.107  1.00 16.07 ? 31  LYS B N   1 
ATOM   1849 C CA  . LYS B 2 31  ? 32.014 -33.138 20.485  1.00 15.25 ? 31  LYS B CA  1 
ATOM   1850 C C   . LYS B 2 31  ? 33.184 -33.620 21.322  1.00 14.09 ? 31  LYS B C   1 
ATOM   1851 O O   . LYS B 2 31  ? 33.680 -32.888 22.183  1.00 13.56 ? 31  LYS B O   1 
ATOM   1852 C CB  . LYS B 2 31  ? 30.706 -33.666 21.082  1.00 15.80 ? 31  LYS B CB  1 
ATOM   1853 C CG  . LYS B 2 31  ? 29.469 -33.194 20.335  1.00 19.90 ? 31  LYS B CG  1 
ATOM   1854 C CD  . LYS B 2 31  ? 28.140 -33.678 20.978  1.00 20.35 ? 31  LYS B CD  1 
ATOM   1855 C CE  . LYS B 2 31  ? 26.923 -33.232 20.146  1.00 20.86 ? 31  LYS B CE  1 
ATOM   1856 N NZ  . LYS B 2 31  ? 25.610 -33.707 20.690  1.00 23.00 ? 31  LYS B NZ  1 
ATOM   1857 N N   . VAL B 2 32  ? 33.633 -34.854 21.071  1.00 14.54 ? 32  VAL B N   1 
ATOM   1858 C CA  . VAL B 2 32  ? 34.700 -35.464 21.855  1.00 14.20 ? 32  VAL B CA  1 
ATOM   1859 C C   . VAL B 2 32  ? 36.034 -34.764 21.587  1.00 13.20 ? 32  VAL B C   1 
ATOM   1860 O O   . VAL B 2 32  ? 36.717 -34.314 22.515  1.00 12.84 ? 32  VAL B O   1 
ATOM   1861 C CB  . VAL B 2 32  ? 34.767 -36.978 21.565  1.00 14.74 ? 32  VAL B CB  1 
ATOM   1862 C CG1 . VAL B 2 32  ? 35.900 -37.642 22.382  1.00 15.75 ? 32  VAL B CG1 1 
ATOM   1863 C CG2 . VAL B 2 32  ? 33.410 -37.652 21.858  1.00 15.97 ? 32  VAL B CG2 1 
ATOM   1864 N N   . ALA B 2 33  ? 36.426 -34.676 20.318  1.00 13.79 ? 33  ALA B N   1 
ATOM   1865 C CA  . ALA B 2 33  ? 37.647 -33.961 19.958  1.00 14.03 ? 33  ALA B CA  1 
ATOM   1866 C C   . ALA B 2 33  ? 37.655 -32.571 20.582  1.00 15.13 ? 33  ALA B C   1 
ATOM   1867 O O   . ALA B 2 33  ? 38.661 -32.133 21.153  1.00 14.59 ? 33  ALA B O   1 
ATOM   1868 C CB  . ALA B 2 33  ? 37.733 -33.861 18.437  1.00 14.10 ? 33  ALA B CB  1 
ATOM   1869 N N   . PHE B 2 34  ? 36.514 -31.876 20.508  1.00 16.36 ? 34  PHE B N   1 
ATOM   1870 C CA  . PHE B 2 34  ? 36.397 -30.531 21.065  1.00 16.70 ? 34  PHE B CA  1 
ATOM   1871 C C   . PHE B 2 34  ? 36.689 -30.507 22.569  1.00 15.36 ? 34  PHE B C   1 
ATOM   1872 O O   . PHE B 2 34  ? 37.545 -29.738 23.040  1.00 13.95 ? 34  PHE B O   1 
ATOM   1873 C CB  . PHE B 2 34  ? 35.002 -29.991 20.758  1.00 16.05 ? 34  PHE B CB  1 
ATOM   1874 C CG  . PHE B 2 34  ? 34.776 -28.611 21.268  1.00 16.95 ? 34  PHE B CG  1 
ATOM   1875 C CD1 . PHE B 2 34  ? 35.486 -27.543 20.737  1.00 18.08 ? 34  PHE B CD1 1 
ATOM   1876 C CD2 . PHE B 2 34  ? 33.894 -28.388 22.308  1.00 14.51 ? 34  PHE B CD2 1 
ATOM   1877 C CE1 . PHE B 2 34  ? 35.304 -26.259 21.216  1.00 16.62 ? 34  PHE B CE1 1 
ATOM   1878 C CE2 . PHE B 2 34  ? 33.698 -27.132 22.776  1.00 17.59 ? 34  PHE B CE2 1 
ATOM   1879 C CZ  . PHE B 2 34  ? 34.416 -26.053 22.229  1.00 16.44 ? 34  PHE B CZ  1 
ATOM   1880 N N   . ALA B 2 35  ? 35.983 -31.345 23.343  1.00 14.44 ? 35  ALA B N   1 
ATOM   1881 C CA  . ALA B 2 35  ? 36.119 -31.354 24.798  1.00 14.80 ? 35  ALA B CA  1 
ATOM   1882 C C   . ALA B 2 35  ? 37.493 -31.822 25.266  1.00 15.37 ? 35  ALA B C   1 
ATOM   1883 O O   . ALA B 2 35  ? 37.853 -31.600 26.426  1.00 15.48 ? 35  ALA B O   1 
ATOM   1884 C CB  . ALA B 2 35  ? 35.031 -32.230 25.432  1.00 15.95 ? 35  ALA B CB  1 
ATOM   1885 N N   . MET B 2 36  ? 38.255 -32.465 24.380  1.00 17.42 ? 36  MET B N   1 
ATOM   1886 C CA  . MET B 2 36  ? 39.580 -33.007 24.681  1.00 16.38 ? 36  MET B CA  1 
ATOM   1887 C C   . MET B 2 36  ? 40.616 -31.899 24.786  1.00 15.80 ? 36  MET B C   1 
ATOM   1888 O O   . MET B 2 36  ? 41.685 -32.105 25.368  1.00 15.17 ? 36  MET B O   1 
ATOM   1889 C CB  . MET B 2 36  ? 39.916 -33.901 23.498  1.00 15.09 ? 36  MET B CB  1 
ATOM   1890 C CG  . MET B 2 36  ? 39.505 -35.357 23.699  1.00 16.70 ? 36  MET B CG  1 
ATOM   1891 S SD  . MET B 2 36  ? 40.057 -36.365 22.315  1.00 16.73 ? 36  MET B SD  1 
ATOM   1892 C CE  . MET B 2 36  ? 39.345 -37.946 22.813  1.00 14.34 ? 36  MET B CE  1 
ATOM   1893 N N   . PHE B 2 37  ? 40.311 -30.729 24.250  1.00 15.69 ? 37  PHE B N   1 
ATOM   1894 C CA  . PHE B 2 37  ? 41.182 -29.573 24.366  1.00 17.17 ? 37  PHE B CA  1 
ATOM   1895 C C   . PHE B 2 37  ? 41.352 -29.131 25.832  1.00 19.10 ? 37  PHE B C   1 
ATOM   1896 O O   . PHE B 2 37  ? 42.475 -29.213 26.376  1.00 17.28 ? 37  PHE B O   1 
ATOM   1897 C CB  . PHE B 2 37  ? 40.661 -28.454 23.473  1.00 16.54 ? 37  PHE B CB  1 
ATOM   1898 C CG  . PHE B 2 37  ? 41.642 -27.370 23.266  1.00 19.12 ? 37  PHE B CG  1 
ATOM   1899 C CD1 . PHE B 2 37  ? 42.225 -27.169 22.038  1.00 22.41 ? 37  PHE B CD1 1 
ATOM   1900 C CD2 . PHE B 2 37  ? 41.994 -26.534 24.315  1.00 25.20 ? 37  PHE B CD2 1 
ATOM   1901 C CE1 . PHE B 2 37  ? 43.152 -26.127 21.840  1.00 23.81 ? 37  PHE B CE1 1 
ATOM   1902 C CE2 . PHE B 2 37  ? 42.920 -25.517 24.135  1.00 24.99 ? 37  PHE B CE2 1 
ATOM   1903 C CZ  . PHE B 2 37  ? 43.499 -25.319 22.893  1.00 22.86 ? 37  PHE B CZ  1 
ATOM   1904 N N   . PRO B 2 38  ? 40.294 -28.650 26.522  1.00 16.97 ? 38  PRO B N   1 
ATOM   1905 C CA  . PRO B 2 38  ? 40.466 -28.350 27.952  1.00 16.09 ? 38  PRO B CA  1 
ATOM   1906 C C   . PRO B 2 38  ? 41.081 -29.508 28.753  1.00 15.47 ? 38  PRO B C   1 
ATOM   1907 O O   . PRO B 2 38  ? 41.871 -29.263 29.675  1.00 15.05 ? 38  PRO B O   1 
ATOM   1908 C CB  . PRO B 2 38  ? 39.050 -27.940 28.390  1.00 15.27 ? 38  PRO B CB  1 
ATOM   1909 C CG  . PRO B 2 38  ? 38.166 -28.581 27.380  1.00 15.47 ? 38  PRO B CG  1 
ATOM   1910 C CD  . PRO B 2 38  ? 38.901 -28.423 26.095  1.00 14.75 ? 38  PRO B CD  1 
ATOM   1911 N N   . ALA B 2 39  ? 40.793 -30.765 28.375  1.00 15.34 ? 39  ALA B N   1 
ATOM   1912 C CA  . ALA B 2 39  ? 41.256 -31.916 29.151  1.00 15.81 ? 39  ALA B CA  1 
ATOM   1913 C C   . ALA B 2 39  ? 42.780 -32.090 29.045  1.00 16.53 ? 39  ALA B C   1 
ATOM   1914 O O   . ALA B 2 39  ? 43.466 -32.318 30.057  1.00 16.81 ? 39  ALA B O   1 
ATOM   1915 C CB  . ALA B 2 39  ? 40.511 -33.183 28.705  1.00 14.41 ? 39  ALA B CB  1 
ATOM   1916 N N   . THR B 2 40  ? 43.333 -31.982 27.827  1.00 16.77 ? 40  THR B N   1 
ATOM   1917 C CA  . THR B 2 40  ? 44.777 -32.130 27.660  1.00 16.01 ? 40  THR B CA  1 
ATOM   1918 C C   . THR B 2 40  ? 45.517 -30.886 28.124  1.00 17.63 ? 40  THR B C   1 
ATOM   1919 O O   . THR B 2 40  ? 46.617 -30.985 28.694  1.00 16.20 ? 40  THR B O   1 
ATOM   1920 C CB  . THR B 2 40  ? 45.108 -32.461 26.202  1.00 15.82 ? 40  THR B CB  1 
ATOM   1921 O OG1 . THR B 2 40  ? 44.649 -31.420 25.344  1.00 14.57 ? 40  THR B OG1 1 
ATOM   1922 C CG2 . THR B 2 40  ? 44.400 -33.763 25.785  1.00 16.03 ? 40  THR B CG2 1 
ATOM   1923 N N   . PHE B 2 41  ? 44.916 -29.708 27.918  1.00 19.13 ? 41  PHE B N   1 
ATOM   1924 C CA  . PHE B 2 41  ? 45.488 -28.471 28.459  1.00 18.32 ? 41  PHE B CA  1 
ATOM   1925 C C   . PHE B 2 41  ? 45.716 -28.568 29.976  1.00 16.48 ? 41  PHE B C   1 
ATOM   1926 O O   . PHE B 2 41  ? 46.834 -28.380 30.460  1.00 16.69 ? 41  PHE B O   1 
ATOM   1927 C CB  . PHE B 2 41  ? 44.621 -27.268 28.025  1.00 17.48 ? 41  PHE B CB  1 
ATOM   1928 C CG  . PHE B 2 41  ? 45.116 -25.924 28.547  1.00 18.52 ? 41  PHE B CG  1 
ATOM   1929 C CD1 . PHE B 2 41  ? 44.749 -25.462 29.802  1.00 18.26 ? 41  PHE B CD1 1 
ATOM   1930 C CD2 . PHE B 2 41  ? 45.977 -25.145 27.786  1.00 19.09 ? 41  PHE B CD2 1 
ATOM   1931 C CE1 . PHE B 2 41  ? 45.221 -24.239 30.283  1.00 19.20 ? 41  PHE B CE1 1 
ATOM   1932 C CE2 . PHE B 2 41  ? 46.447 -23.919 28.266  1.00 18.56 ? 41  PHE B CE2 1 
ATOM   1933 C CZ  . PHE B 2 41  ? 46.078 -23.476 29.513  1.00 16.76 ? 41  PHE B CZ  1 
ATOM   1934 N N   . ARG B 2 42  ? 44.673 -28.911 30.739  1.00 15.34 ? 42  ARG B N   1 
ATOM   1935 C CA  . ARG B 2 42  ? 44.808 -29.014 32.193  1.00 16.70 ? 42  ARG B CA  1 
ATOM   1936 C C   . ARG B 2 42  ? 45.800 -30.103 32.614  1.00 17.17 ? 42  ARG B C   1 
ATOM   1937 O O   . ARG B 2 42  ? 46.454 -29.974 33.658  1.00 16.66 ? 42  ARG B O   1 
ATOM   1938 C CB  . ARG B 2 42  ? 43.429 -29.256 32.832  1.00 17.03 ? 42  ARG B CB  1 
ATOM   1939 C CG  . ARG B 2 42  ? 43.360 -29.151 34.388  1.00 18.10 ? 42  ARG B CG  1 
ATOM   1940 C CD  . ARG B 2 42  ? 41.913 -29.454 34.910  1.00 17.90 ? 42  ARG B CD  1 
ATOM   1941 N NE  . ARG B 2 42  ? 41.674 -29.001 36.283  1.00 21.91 ? 42  ARG B NE  1 
ATOM   1942 C CZ  . ARG B 2 42  ? 41.814 -29.739 37.382  1.00 21.95 ? 42  ARG B CZ  1 
ATOM   1943 N NH1 . ARG B 2 42  ? 42.142 -31.025 37.316  1.00 22.50 ? 42  ARG B NH1 1 
ATOM   1944 N NH2 . ARG B 2 42  ? 41.611 -29.177 38.573  1.00 16.82 ? 42  ARG B NH2 1 
ATOM   1945 N N   . ALA B 2 43  ? 45.917 -31.187 31.832  1.00 16.82 ? 43  ALA B N   1 
ATOM   1946 C CA  . ALA B 2 43  ? 46.845 -32.274 32.128  1.00 15.58 ? 43  ALA B CA  1 
ATOM   1947 C C   . ALA B 2 43  ? 48.272 -31.950 31.709  1.00 15.24 ? 43  ALA B C   1 
ATOM   1948 O O   . ALA B 2 43  ? 49.171 -32.760 31.927  1.00 14.65 ? 43  ALA B O   1 
ATOM   1949 C CB  . ALA B 2 43  ? 46.366 -33.569 31.449  1.00 15.14 ? 43  ALA B CB  1 
ATOM   1950 N N   . GLY B 2 44  ? 48.497 -30.794 31.098  1.00 18.83 ? 44  GLY B N   1 
ATOM   1951 C CA  . GLY B 2 44  ? 49.845 -30.393 30.731  1.00 18.79 ? 44  GLY B CA  1 
ATOM   1952 C C   . GLY B 2 44  ? 50.363 -30.993 29.450  1.00 18.94 ? 44  GLY B C   1 
ATOM   1953 O O   . GLY B 2 44  ? 51.581 -31.087 29.283  1.00 19.69 ? 44  GLY B O   1 
ATOM   1954 N N   . PHE B 2 45  ? 49.472 -31.393 28.531  1.00 17.38 ? 45  PHE B N   1 
ATOM   1955 C CA  . PHE B 2 45  ? 49.894 -31.888 27.222  1.00 15.97 ? 45  PHE B CA  1 
ATOM   1956 C C   . PHE B 2 45  ? 50.558 -30.781 26.410  1.00 18.12 ? 45  PHE B C   1 
ATOM   1957 O O   . PHE B 2 45  ? 51.486 -31.038 25.626  1.00 16.56 ? 45  PHE B O   1 
ATOM   1958 C CB  . PHE B 2 45  ? 48.668 -32.382 26.449  1.00 15.23 ? 45  PHE B CB  1 
ATOM   1959 C CG  . PHE B 2 45  ? 48.249 -33.777 26.793  1.00 15.89 ? 45  PHE B CG  1 
ATOM   1960 C CD1 . PHE B 2 45  ? 48.078 -34.171 28.125  1.00 17.31 ? 45  PHE B CD1 1 
ATOM   1961 C CD2 . PHE B 2 45  ? 47.965 -34.692 25.781  1.00 17.52 ? 45  PHE B CD2 1 
ATOM   1962 C CE1 . PHE B 2 45  ? 47.664 -35.465 28.446  1.00 15.88 ? 45  PHE B CE1 1 
ATOM   1963 C CE2 . PHE B 2 45  ? 47.540 -35.986 26.097  1.00 16.98 ? 45  PHE B CE2 1 
ATOM   1964 C CZ  . PHE B 2 45  ? 47.398 -36.363 27.435  1.00 15.76 ? 45  PHE B CZ  1 
ATOM   1965 N N   . MET B 2 46  ? 50.073 -29.547 26.561  1.00 17.80 ? 46  MET B N   1 
ATOM   1966 C CA  . MET B 2 46  ? 50.475 -28.440 25.702  1.00 18.06 ? 46  MET B CA  1 
ATOM   1967 C C   . MET B 2 46  ? 49.654 -27.209 26.092  1.00 18.09 ? 46  MET B C   1 
ATOM   1968 O O   . MET B 2 46  ? 48.644 -27.297 26.800  1.00 17.24 ? 46  MET B O   1 
ATOM   1969 C CB  . MET B 2 46  ? 50.202 -28.796 24.231  1.00 17.29 ? 46  MET B CB  1 
ATOM   1970 C CG  . MET B 2 46  ? 48.766 -28.537 23.794  1.00 17.20 ? 46  MET B CG  1 
ATOM   1971 S SD  . MET B 2 46  ? 47.531 -29.804 24.249  1.00 23.04 ? 46  MET B SD  1 
ATOM   1972 C CE  . MET B 2 46  ? 46.466 -29.676 22.824  1.00 22.65 ? 46  MET B CE  1 
ATOM   1973 N N   . GLY B 2 47  ? 50.109 -26.053 25.609  1.00 17.01 ? 47  GLY B N   1 
ATOM   1974 C CA  . GLY B 2 47  ? 49.338 -24.834 25.635  1.00 16.08 ? 47  GLY B CA  1 
ATOM   1975 C C   . GLY B 2 47  ? 48.854 -24.439 24.252  1.00 14.90 ? 47  GLY B C   1 
ATOM   1976 O O   . GLY B 2 47  ? 48.956 -25.187 23.280  1.00 14.98 ? 47  GLY B O   1 
ATOM   1977 N N   . LEU B 2 48  ? 48.328 -23.212 24.166  1.00 16.58 ? 48  LEU B N   1 
ATOM   1978 C CA  . LEU B 2 48  ? 47.697 -22.766 22.923  1.00 14.42 ? 48  LEU B CA  1 
ATOM   1979 C C   . LEU B 2 48  ? 48.684 -22.762 21.761  1.00 13.30 ? 48  LEU B C   1 
ATOM   1980 O O   . LEU B 2 48  ? 48.382 -23.273 20.678  1.00 14.01 ? 48  LEU B O   1 
ATOM   1981 C CB  . LEU B 2 48  ? 47.081 -21.377 23.113  1.00 13.93 ? 48  LEU B CB  1 
ATOM   1982 C CG  . LEU B 2 48  ? 46.362 -20.901 21.861  1.00 16.10 ? 48  LEU B CG  1 
ATOM   1983 C CD1 . LEU B 2 48  ? 45.317 -21.951 21.402  1.00 14.41 ? 48  LEU B CD1 1 
ATOM   1984 C CD2 . LEU B 2 48  ? 45.718 -19.529 22.109  1.00 15.25 ? 48  LEU B CD2 1 
ATOM   1985 N N   . ASP B 2 49  ? 49.860 -22.142 21.955  1.00 13.46 ? 49  ASP B N   1 
ATOM   1986 C CA  . ASP B 2 49  ? 50.838 -22.025 20.879  1.00 13.03 ? 49  ASP B CA  1 
ATOM   1987 C C   . ASP B 2 49  ? 51.371 -23.392 20.482  1.00 12.01 ? 49  ASP B C   1 
ATOM   1988 O O   . ASP B 2 49  ? 51.506 -23.686 19.285  1.00 12.31 ? 49  ASP B O   1 
ATOM   1989 C CB  . ASP B 2 49  ? 51.973 -21.082 21.308  1.00 13.12 ? 49  ASP B CB  1 
ATOM   1990 C CG  . ASP B 2 49  ? 51.452 -19.730 21.800  1.00 12.47 ? 49  ASP B CG  1 
ATOM   1991 O OD1 . ASP B 2 49  ? 51.029 -19.634 22.956  1.00 12.06 ? 49  ASP B OD1 1 
ATOM   1992 O OD2 . ASP B 2 49  ? 51.458 -18.761 21.010  1.00 16.19 ? 49  ASP B OD2 1 
ATOM   1993 N N   . GLU B 2 50  ? 51.649 -24.242 21.480  1.00 13.06 ? 50  GLU B N   1 
ATOM   1994 C CA  . GLU B 2 50  ? 52.091 -25.611 21.216  1.00 13.41 ? 50  GLU B CA  1 
ATOM   1995 C C   . GLU B 2 50  ? 51.020 -26.422 20.489  1.00 12.95 ? 50  GLU B C   1 
ATOM   1996 O O   . GLU B 2 50  ? 51.327 -27.149 19.540  1.00 12.41 ? 50  GLU B O   1 
ATOM   1997 C CB  . GLU B 2 50  ? 52.488 -26.281 22.531  1.00 15.01 ? 50  GLU B CB  1 
ATOM   1998 C CG  . GLU B 2 50  ? 53.839 -25.774 23.099  1.00 15.35 ? 50  GLU B CG  1 
ATOM   1999 C CD  . GLU B 2 50  ? 54.061 -26.127 24.546  1.00 14.66 ? 50  GLU B CD  1 
ATOM   2000 O OE1 . GLU B 2 50  ? 53.124 -25.990 25.359  1.00 15.45 ? 50  GLU B OE1 1 
ATOM   2001 O OE2 . GLU B 2 50  ? 55.187 -26.550 24.884  1.00 16.05 ? 50  GLU B OE2 1 
ATOM   2002 N N   . PHE B 2 51  ? 49.760 -26.319 20.944  1.00 15.05 ? 51  PHE B N   1 
ATOM   2003 C CA  . PHE B 2 51  ? 48.623 -26.917 20.248  1.00 13.87 ? 51  PHE B CA  1 
ATOM   2004 C C   . PHE B 2 51  ? 48.648 -26.590 18.753  1.00 14.08 ? 51  PHE B C   1 
ATOM   2005 O O   . PHE B 2 51  ? 48.538 -27.478 17.897  1.00 12.46 ? 51  PHE B O   1 
ATOM   2006 C CB  . PHE B 2 51  ? 47.321 -26.441 20.912  1.00 14.53 ? 51  PHE B CB  1 
ATOM   2007 C CG  . PHE B 2 51  ? 46.061 -26.834 20.164  1.00 16.66 ? 51  PHE B CG  1 
ATOM   2008 C CD1 . PHE B 2 51  ? 45.519 -26.006 19.192  1.00 17.32 ? 51  PHE B CD1 1 
ATOM   2009 C CD2 . PHE B 2 51  ? 45.405 -28.022 20.452  1.00 16.70 ? 51  PHE B CD2 1 
ATOM   2010 C CE1 . PHE B 2 51  ? 44.357 -26.359 18.497  1.00 18.11 ? 51  PHE B CE1 1 
ATOM   2011 C CE2 . PHE B 2 51  ? 44.240 -28.389 19.769  1.00 15.49 ? 51  PHE B CE2 1 
ATOM   2012 C CZ  . PHE B 2 51  ? 43.710 -27.558 18.798  1.00 17.27 ? 51  PHE B CZ  1 
ATOM   2013 N N   . ARG B 2 52  ? 48.808 -25.307 18.414  1.00 14.06 ? 52  ARG B N   1 
ATOM   2014 C CA  . ARG B 2 52  ? 48.788 -24.920 17.008  1.00 13.83 ? 52  ARG B CA  1 
ATOM   2015 C C   . ARG B 2 52  ? 49.976 -25.516 16.248  1.00 14.03 ? 52  ARG B C   1 
ATOM   2016 O O   . ARG B 2 52  ? 49.852 -25.850 15.066  1.00 14.24 ? 52  ARG B O   1 
ATOM   2017 C CB  . ARG B 2 52  ? 48.811 -23.403 16.899  1.00 13.11 ? 52  ARG B CB  1 
ATOM   2018 C CG  . ARG B 2 52  ? 47.680 -22.680 17.557  1.00 12.22 ? 52  ARG B CG  1 
ATOM   2019 C CD  . ARG B 2 52  ? 47.745 -21.221 17.136  1.00 15.17 ? 52  ARG B CD  1 
ATOM   2020 N NE  . ARG B 2 52  ? 46.529 -20.487 17.452  1.00 15.49 ? 52  ARG B NE  1 
ATOM   2021 C CZ  . ARG B 2 52  ? 46.441 -19.510 18.342  1.00 16.87 ? 52  ARG B CZ  1 
ATOM   2022 N NH1 . ARG B 2 52  ? 47.511 -19.059 18.986  1.00 15.44 ? 52  ARG B NH1 1 
ATOM   2023 N NH2 . ARG B 2 52  ? 45.246 -18.968 18.590  1.00 17.37 ? 52  ARG B NH2 1 
ATOM   2024 N N   . PHE B 2 53  ? 51.130 -25.652 16.910  1.00 12.73 ? 53  PHE B N   1 
ATOM   2025 C CA  . PHE B 2 53  ? 52.301 -26.200 16.233  1.00 13.82 ? 53  PHE B CA  1 
ATOM   2026 C C   . PHE B 2 53  ? 52.086 -27.662 15.863  1.00 14.85 ? 53  PHE B C   1 
ATOM   2027 O O   . PHE B 2 53  ? 52.540 -28.112 14.804  1.00 13.63 ? 53  PHE B O   1 
ATOM   2028 C CB  . PHE B 2 53  ? 53.531 -26.050 17.135  1.00 13.41 ? 53  PHE B CB  1 
ATOM   2029 C CG  . PHE B 2 53  ? 54.820 -26.326 16.437  1.00 13.61 ? 53  PHE B CG  1 
ATOM   2030 C CD1 . PHE B 2 53  ? 54.990 -25.984 15.117  1.00 14.47 ? 53  PHE B CD1 1 
ATOM   2031 C CD2 . PHE B 2 53  ? 55.874 -26.900 17.122  1.00 16.09 ? 53  PHE B CD2 1 
ATOM   2032 C CE1 . PHE B 2 53  ? 56.186 -26.241 14.458  1.00 16.41 ? 53  PHE B CE1 1 
ATOM   2033 C CE2 . PHE B 2 53  ? 57.078 -27.140 16.481  1.00 15.02 ? 53  PHE B CE2 1 
ATOM   2034 C CZ  . PHE B 2 53  ? 57.232 -26.813 15.158  1.00 15.53 ? 53  PHE B CZ  1 
ATOM   2035 N N   . GLY B 2 54  ? 51.405 -28.431 16.738  1.00 16.65 ? 54  GLY B N   1 
ATOM   2036 C CA  . GLY B 2 54  ? 51.125 -29.830 16.415  1.00 15.64 ? 54  GLY B CA  1 
ATOM   2037 C C   . GLY B 2 54  ? 50.324 -29.960 15.132  1.00 16.08 ? 54  GLY B C   1 
ATOM   2038 O O   . GLY B 2 54  ? 50.626 -30.794 14.273  1.00 16.01 ? 54  GLY B O   1 
ATOM   2039 N N   . ILE B 2 55  ? 49.301 -29.117 14.972  1.00 14.33 ? 55  ILE B N   1 
ATOM   2040 C CA  . ILE B 2 55  ? 48.528 -29.119 13.739  1.00 13.14 ? 55  ILE B CA  1 
ATOM   2041 C C   . ILE B 2 55  ? 49.412 -28.747 12.548  1.00 14.53 ? 55  ILE B C   1 
ATOM   2042 O O   . ILE B 2 55  ? 49.267 -29.305 11.450  1.00 14.34 ? 55  ILE B O   1 
ATOM   2043 C CB  . ILE B 2 55  ? 47.308 -28.186 13.892  1.00 13.34 ? 55  ILE B CB  1 
ATOM   2044 C CG1 . ILE B 2 55  ? 46.367 -28.706 14.994  1.00 13.90 ? 55  ILE B CG1 1 
ATOM   2045 C CG2 . ILE B 2 55  ? 46.591 -28.001 12.542  1.00 13.42 ? 55  ILE B CG2 1 
ATOM   2046 C CD1 . ILE B 2 55  ? 45.134 -27.809 15.289  1.00 13.02 ? 55  ILE B CD1 1 
ATOM   2047 N N   . GLU B 2 56  ? 50.358 -27.813 12.744  1.00 14.99 ? 56  GLU B N   1 
ATOM   2048 C CA  . GLU B 2 56  ? 51.225 -27.354 11.653  1.00 15.21 ? 56  GLU B CA  1 
ATOM   2049 C C   . GLU B 2 56  ? 52.209 -28.422 11.165  1.00 17.14 ? 56  GLU B C   1 
ATOM   2050 O O   . GLU B 2 56  ? 52.805 -28.250 10.090  1.00 16.78 ? 56  GLU B O   1 
ATOM   2051 C CB  . GLU B 2 56  ? 51.989 -26.103 12.092  1.00 15.17 ? 56  GLU B CB  1 
ATOM   2052 C CG  . GLU B 2 56  ? 51.079 -24.922 12.430  1.00 14.79 ? 56  GLU B CG  1 
ATOM   2053 C CD  . GLU B 2 56  ? 51.766 -23.825 13.227  1.00 14.26 ? 56  GLU B CD  1 
ATOM   2054 O OE1 . GLU B 2 56  ? 52.940 -23.960 13.582  1.00 14.63 ? 56  GLU B OE1 1 
ATOM   2055 O OE2 . GLU B 2 56  ? 51.121 -22.811 13.500  1.00 14.53 ? 56  GLU B OE2 1 
ATOM   2056 N N   . GLN B 2 57  ? 52.400 -29.511 11.917  1.00 16.35 ? 57  GLN B N   1 
ATOM   2057 C CA  . GLN B 2 57  ? 53.305 -30.597 11.525  1.00 17.86 ? 57  GLN B CA  1 
ATOM   2058 C C   . GLN B 2 57  ? 52.562 -31.786 10.917  1.00 19.68 ? 57  GLN B C   1 
ATOM   2059 O O   . GLN B 2 57  ? 53.162 -32.849 10.677  1.00 19.90 ? 57  GLN B O   1 
ATOM   2060 C CB  . GLN B 2 57  ? 54.124 -31.037 12.732  1.00 17.55 ? 57  GLN B CB  1 
ATOM   2061 C CG  . GLN B 2 57  ? 55.031 -29.947 13.290  1.00 15.21 ? 57  GLN B CG  1 
ATOM   2062 C CD  . GLN B 2 57  ? 55.653 -30.350 14.600  1.00 16.96 ? 57  GLN B CD  1 
ATOM   2063 O OE1 . GLN B 2 57  ? 56.595 -31.133 14.627  1.00 19.33 ? 57  GLN B OE1 1 
ATOM   2064 N NE2 . GLN B 2 57  ? 55.118 -29.827 15.711  1.00 16.66 ? 57  GLN B NE2 1 
ATOM   2065 N N   . MET B 2 58  ? 51.264 -31.620 10.681  1.00 17.88 ? 58  MET B N   1 
ATOM   2066 C CA  . MET B 2 58  ? 50.419 -32.614 10.052  1.00 17.15 ? 58  MET B CA  1 
ATOM   2067 C C   . MET B 2 58  ? 50.913 -32.888 8.631   1.00 17.94 ? 58  MET B C   1 
ATOM   2068 O O   . MET B 2 58  ? 51.610 -32.077 8.005   1.00 16.48 ? 58  MET B O   1 
ATOM   2069 C CB  . MET B 2 58  ? 48.997 -32.032 10.020  1.00 16.44 ? 58  MET B CB  1 
ATOM   2070 C CG  . MET B 2 58  ? 48.106 -32.503 11.173  1.00 15.53 ? 58  MET B CG  1 
ATOM   2071 S SD  . MET B 2 58  ? 46.405 -31.911 10.984  1.00 14.05 ? 58  MET B SD  1 
ATOM   2072 C CE  . MET B 2 58  ? 45.809 -33.074 9.715   1.00 13.68 ? 58  MET B CE  1 
ATOM   2073 N N   . ASN B 2 59  ? 50.545 -34.055 8.114   1.00 18.75 ? 59  ASN B N   1 
ATOM   2074 C CA  . ASN B 2 59  ? 50.737 -34.305 6.703   1.00 17.70 ? 59  ASN B CA  1 
ATOM   2075 C C   . ASN B 2 59  ? 49.903 -33.286 5.916   1.00 18.04 ? 59  ASN B C   1 
ATOM   2076 O O   . ASN B 2 59  ? 48.727 -33.048 6.259   1.00 16.13 ? 59  ASN B O   1 
ATOM   2077 C CB  . ASN B 2 59  ? 50.331 -35.752 6.407   1.00 19.14 ? 59  ASN B CB  1 
ATOM   2078 C CG  . ASN B 2 59  ? 50.100 -36.026 4.927   1.00 20.21 ? 59  ASN B CG  1 
ATOM   2079 O OD1 . ASN B 2 59  ? 49.897 -35.123 4.109   1.00 21.95 ? 59  ASN B OD1 1 
ATOM   2080 N ND2 . ASN B 2 59  ? 50.199 -37.302 4.563   1.00 21.42 ? 59  ASN B ND2 1 
ATOM   2081 N N   . PRO B 2 60  ? 50.475 -32.632 4.900   1.00 16.97 ? 60  PRO B N   1 
ATOM   2082 C CA  . PRO B 2 60  ? 49.767 -31.503 4.275   1.00 17.18 ? 60  PRO B CA  1 
ATOM   2083 C C   . PRO B 2 60  ? 48.493 -31.896 3.532   1.00 17.79 ? 60  PRO B C   1 
ATOM   2084 O O   . PRO B 2 60  ? 47.497 -31.155 3.612   1.00 16.08 ? 60  PRO B O   1 
ATOM   2085 C CB  . PRO B 2 60  ? 50.834 -30.922 3.330   1.00 17.71 ? 60  PRO B CB  1 
ATOM   2086 C CG  . PRO B 2 60  ? 52.099 -31.261 3.981   1.00 18.35 ? 60  PRO B CG  1 
ATOM   2087 C CD  . PRO B 2 60  ? 51.875 -32.680 4.457   1.00 20.47 ? 60  PRO B CD  1 
ATOM   2088 N N   . ALA B 2 61  ? 48.492 -33.030 2.800   1.00 16.65 ? 61  ALA B N   1 
ATOM   2089 C CA  . ALA B 2 61  ? 47.292 -33.427 2.051   1.00 17.59 ? 61  ALA B CA  1 
ATOM   2090 C C   . ALA B 2 61  ? 46.139 -33.771 2.988   1.00 15.39 ? 61  ALA B C   1 
ATOM   2091 O O   . ALA B 2 61  ? 44.988 -33.406 2.726   1.00 16.06 ? 61  ALA B O   1 
ATOM   2092 C CB  . ALA B 2 61  ? 47.598 -34.607 1.121   1.00 17.03 ? 61  ALA B CB  1 
ATOM   2093 N N   . GLU B 2 62  ? 46.441 -34.461 4.085   1.00 14.97 ? 62  GLU B N   1 
ATOM   2094 C CA  . GLU B 2 62  ? 45.452 -34.730 5.117   1.00 15.31 ? 62  GLU B CA  1 
ATOM   2095 C C   . GLU B 2 62  ? 44.946 -33.443 5.776   1.00 15.94 ? 62  GLU B C   1 
ATOM   2096 O O   . GLU B 2 62  ? 43.737 -33.262 5.943   1.00 16.81 ? 62  GLU B O   1 
ATOM   2097 C CB  . GLU B 2 62  ? 46.075 -35.636 6.176   1.00 15.58 ? 62  GLU B CB  1 
ATOM   2098 C CG  . GLU B 2 62  ? 45.081 -36.186 7.128   1.00 15.15 ? 62  GLU B CG  1 
ATOM   2099 C CD  . GLU B 2 62  ? 45.739 -36.937 8.219   1.00 15.57 ? 62  GLU B CD  1 
ATOM   2100 O OE1 . GLU B 2 62  ? 46.152 -36.308 9.211   1.00 15.06 ? 62  GLU B OE1 1 
ATOM   2101 O OE2 . GLU B 2 62  ? 45.858 -38.171 8.086   1.00 19.00 ? 62  GLU B OE2 1 
ATOM   2102 N N   . TYR B 2 63  ? 45.853 -32.562 6.216   1.00 14.04 ? 63  TYR B N   1 
ATOM   2103 C CA  . TYR B 2 63  ? 45.432 -31.287 6.782   1.00 12.94 ? 63  TYR B CA  1 
ATOM   2104 C C   . TYR B 2 63  ? 44.408 -30.602 5.883   1.00 14.90 ? 63  TYR B C   1 
ATOM   2105 O O   . TYR B 2 63  ? 43.363 -30.133 6.353   1.00 14.69 ? 63  TYR B O   1 
ATOM   2106 C CB  . TYR B 2 63  ? 46.649 -30.381 6.964   1.00 12.96 ? 63  TYR B CB  1 
ATOM   2107 C CG  . TYR B 2 63  ? 46.272 -28.955 7.321   1.00 13.31 ? 63  TYR B CG  1 
ATOM   2108 C CD1 . TYR B 2 63  ? 45.995 -28.608 8.620   1.00 13.83 ? 63  TYR B CD1 1 
ATOM   2109 C CD2 . TYR B 2 63  ? 46.166 -27.971 6.337   1.00 14.36 ? 63  TYR B CD2 1 
ATOM   2110 C CE1 . TYR B 2 63  ? 45.649 -27.344 8.954   1.00 13.90 ? 63  TYR B CE1 1 
ATOM   2111 C CE2 . TYR B 2 63  ? 45.813 -26.691 6.659   1.00 13.34 ? 63  TYR B CE2 1 
ATOM   2112 C CZ  . TYR B 2 63  ? 45.561 -26.391 7.961   1.00 14.03 ? 63  TYR B CZ  1 
ATOM   2113 O OH  . TYR B 2 63  ? 45.228 -25.107 8.333   1.00 19.47 ? 63  TYR B OH  1 
ATOM   2114 N N   . LEU B 2 64  ? 44.694 -30.563 4.571   1.00 14.78 ? 64  LEU B N   1 
ATOM   2115 C CA  . LEU B 2 64  ? 43.916 -29.776 3.612   1.00 15.68 ? 64  LEU B CA  1 
ATOM   2116 C C   . LEU B 2 64  ? 42.509 -30.325 3.401   1.00 16.66 ? 64  LEU B C   1 
ATOM   2117 O O   . LEU B 2 64  ? 41.583 -29.546 3.112   1.00 18.08 ? 64  LEU B O   1 
ATOM   2118 C CB  . LEU B 2 64  ? 44.631 -29.764 2.263   1.00 15.20 ? 64  LEU B CB  1 
ATOM   2119 C CG  . LEU B 2 64  ? 45.944 -28.994 2.158   1.00 14.46 ? 64  LEU B CG  1 
ATOM   2120 C CD1 . LEU B 2 64  ? 46.583 -29.315 0.820   1.00 17.05 ? 64  LEU B CD1 1 
ATOM   2121 C CD2 . LEU B 2 64  ? 45.718 -27.511 2.314   1.00 15.00 ? 64  LEU B CD2 1 
ATOM   2122 N N   . GLU B 2 65  ? 42.332 -31.650 3.495   1.00 15.72 ? 65  GLU B N   1 
ATOM   2123 C CA  . GLU B 2 65  ? 41.056 -32.301 3.199   1.00 17.58 ? 65  GLU B CA  1 
ATOM   2124 C C   . GLU B 2 65  ? 40.432 -33.097 4.353   1.00 16.03 ? 65  GLU B C   1 
ATOM   2125 O O   . GLU B 2 65  ? 39.372 -33.691 4.167   1.00 16.57 ? 65  GLU B O   1 
ATOM   2126 C CB  . GLU B 2 65  ? 41.160 -33.197 1.956   1.00 16.53 ? 65  GLU B CB  1 
ATOM   2127 C CG  . GLU B 2 65  ? 41.507 -32.465 0.664   1.00 16.45 ? 65  GLU B CG  1 
ATOM   2128 C CD  . GLU B 2 65  ? 41.339 -33.362 -0.597  1.00 16.47 ? 65  GLU B CD  1 
ATOM   2129 O OE1 . GLU B 2 65  ? 41.596 -34.577 -0.536  1.00 17.34 ? 65  GLU B OE1 1 
ATOM   2130 O OE2 . GLU B 2 65  ? 40.954 -32.850 -1.652  1.00 17.05 ? 65  GLU B OE2 1 
ATOM   2131 N N   . SER B 2 66  ? 41.022 -33.128 5.514   1.00 14.61 ? 66  SER B N   1 
ATOM   2132 C CA  . SER B 2 66  ? 40.384 -33.845 6.593   1.00 14.54 ? 66  SER B CA  1 
ATOM   2133 C C   . SER B 2 66  ? 39.358 -32.948 7.295   1.00 17.26 ? 66  SER B C   1 
ATOM   2134 O O   . SER B 2 66  ? 39.419 -31.715 7.193   1.00 17.85 ? 66  SER B O   1 
ATOM   2135 C CB  . SER B 2 66  ? 41.434 -34.283 7.611   1.00 15.88 ? 66  SER B CB  1 
ATOM   2136 O OG  . SER B 2 66  ? 42.059 -33.146 8.210   1.00 16.23 ? 66  SER B OG  1 
ATOM   2137 N N   . PRO B 2 67  ? 38.421 -33.545 8.048   1.00 16.88 ? 67  PRO B N   1 
ATOM   2138 C CA  . PRO B 2 67  ? 37.563 -32.748 8.931   1.00 15.90 ? 67  PRO B CA  1 
ATOM   2139 C C   . PRO B 2 67  ? 38.390 -31.938 9.921   1.00 13.70 ? 67  PRO B C   1 
ATOM   2140 O O   . PRO B 2 67  ? 39.343 -32.434 10.512  1.00 14.04 ? 67  PRO B O   1 
ATOM   2141 C CB  . PRO B 2 67  ? 36.731 -33.818 9.653   1.00 16.79 ? 67  PRO B CB  1 
ATOM   2142 C CG  . PRO B 2 67  ? 36.649 -34.945 8.638   1.00 17.07 ? 67  PRO B CG  1 
ATOM   2143 C CD  . PRO B 2 67  ? 38.049 -34.981 8.089   1.00 17.16 ? 67  PRO B CD  1 
ATOM   2144 N N   . TYR B 2 68  ? 37.985 -30.684 10.120  1.00 14.06 ? 68  TYR B N   1 
ATOM   2145 C CA  . TYR B 2 68  ? 38.705 -29.761 10.991  1.00 13.92 ? 68  TYR B CA  1 
ATOM   2146 C C   . TYR B 2 68  ? 39.111 -30.397 12.314  1.00 13.93 ? 68  TYR B C   1 
ATOM   2147 O O   . TYR B 2 68  ? 40.284 -30.351 12.695  1.00 13.63 ? 68  TYR B O   1 
ATOM   2148 C CB  . TYR B 2 68  ? 37.855 -28.508 11.238  1.00 15.06 ? 68  TYR B CB  1 
ATOM   2149 C CG  . TYR B 2 68  ? 38.488 -27.546 12.201  1.00 12.87 ? 68  TYR B CG  1 
ATOM   2150 C CD1 . TYR B 2 68  ? 39.500 -26.677 11.784  1.00 14.60 ? 68  TYR B CD1 1 
ATOM   2151 C CD2 . TYR B 2 68  ? 38.110 -27.530 13.546  1.00 12.66 ? 68  TYR B CD2 1 
ATOM   2152 C CE1 . TYR B 2 68  ? 40.102 -25.786 12.673  1.00 12.21 ? 68  TYR B CE1 1 
ATOM   2153 C CE2 . TYR B 2 68  ? 38.707 -26.655 14.442  1.00 14.45 ? 68  TYR B CE2 1 
ATOM   2154 C CZ  . TYR B 2 68  ? 39.714 -25.776 13.985  1.00 13.20 ? 68  TYR B CZ  1 
ATOM   2155 O OH  . TYR B 2 68  ? 40.302 -24.901 14.855  1.00 13.45 ? 68  TYR B OH  1 
ATOM   2156 N N   . TYR B 2 69  ? 38.144 -30.954 13.069  1.00 14.65 ? 69  TYR B N   1 
ATOM   2157 C CA  . TYR B 2 69  ? 38.441 -31.450 14.420  1.00 12.99 ? 69  TYR B CA  1 
ATOM   2158 C C   . TYR B 2 69  ? 39.379 -32.648 14.416  1.00 10.71 ? 69  TYR B C   1 
ATOM   2159 O O   . TYR B 2 69  ? 39.958 -32.967 15.460  1.00 10.80 ? 69  TYR B O   1 
ATOM   2160 C CB  . TYR B 2 69  ? 37.159 -31.772 15.191  1.00 13.15 ? 69  TYR B CB  1 
ATOM   2161 C CG  . TYR B 2 69  ? 36.464 -30.535 15.703  1.00 14.09 ? 69  TYR B CG  1 
ATOM   2162 C CD1 . TYR B 2 69  ? 37.066 -29.715 16.638  1.00 14.07 ? 69  TYR B CD1 1 
ATOM   2163 C CD2 . TYR B 2 69  ? 35.222 -30.145 15.174  1.00 17.29 ? 69  TYR B CD2 1 
ATOM   2164 C CE1 . TYR B 2 69  ? 36.434 -28.539 17.093  1.00 17.42 ? 69  TYR B CE1 1 
ATOM   2165 C CE2 . TYR B 2 69  ? 34.574 -28.988 15.613  1.00 16.10 ? 69  TYR B CE2 1 
ATOM   2166 C CZ  . TYR B 2 69  ? 35.183 -28.181 16.572  1.00 18.35 ? 69  TYR B CZ  1 
ATOM   2167 O OH  . TYR B 2 69  ? 34.527 -27.030 16.994  1.00 16.59 ? 69  TYR B OH  1 
ATOM   2168 N N   . TRP B 2 70  ? 39.523 -33.312 13.269  1.00 13.33 ? 70  TRP B N   1 
ATOM   2169 C CA  . TRP B 2 70  ? 40.578 -34.309 13.109  1.00 13.08 ? 70  TRP B CA  1 
ATOM   2170 C C   . TRP B 2 70  ? 41.969 -33.690 13.307  1.00 14.27 ? 70  TRP B C   1 
ATOM   2171 O O   . TRP B 2 70  ? 42.875 -34.342 13.856  1.00 13.22 ? 70  TRP B O   1 
ATOM   2172 C CB  . TRP B 2 70  ? 40.486 -34.980 11.744  1.00 12.18 ? 70  TRP B CB  1 
ATOM   2173 C CG  . TRP B 2 70  ? 41.631 -35.883 11.589  1.00 13.41 ? 70  TRP B CG  1 
ATOM   2174 C CD1 . TRP B 2 70  ? 42.678 -35.750 10.746  1.00 14.56 ? 70  TRP B CD1 1 
ATOM   2175 C CD2 . TRP B 2 70  ? 41.890 -37.032 12.390  1.00 14.06 ? 70  TRP B CD2 1 
ATOM   2176 N NE1 . TRP B 2 70  ? 43.567 -36.789 10.930  1.00 14.54 ? 70  TRP B NE1 1 
ATOM   2177 C CE2 . TRP B 2 70  ? 43.107 -37.583 11.945  1.00 15.19 ? 70  TRP B CE2 1 
ATOM   2178 C CE3 . TRP B 2 70  ? 41.196 -37.664 13.440  1.00 13.34 ? 70  TRP B CE3 1 
ATOM   2179 C CZ2 . TRP B 2 70  ? 43.652 -38.736 12.511  1.00 16.99 ? 70  TRP B CZ2 1 
ATOM   2180 C CZ3 . TRP B 2 70  ? 41.738 -38.805 14.013  1.00 13.93 ? 70  TRP B CZ3 1 
ATOM   2181 C CH2 . TRP B 2 70  ? 42.951 -39.330 13.551  1.00 15.61 ? 70  TRP B CH2 1 
ATOM   2182 N N   . HIS B 2 71  ? 42.167 -32.437 12.858  1.00 12.70 ? 71  HIS B N   1 
ATOM   2183 C CA  . HIS B 2 71  ? 43.410 -31.732 13.190  1.00 12.95 ? 71  HIS B CA  1 
ATOM   2184 C C   . HIS B 2 71  ? 43.661 -31.749 14.693  1.00 13.34 ? 71  HIS B C   1 
ATOM   2185 O O   . HIS B 2 71  ? 44.789 -32.006 15.149  1.00 13.21 ? 71  HIS B O   1 
ATOM   2186 C CB  . HIS B 2 71  ? 43.341 -30.288 12.710  1.00 11.88 ? 71  HIS B CB  1 
ATOM   2187 C CG  . HIS B 2 71  ? 43.007 -30.153 11.260  1.00 13.79 ? 71  HIS B CG  1 
ATOM   2188 N ND1 . HIS B 2 71  ? 42.899 -28.927 10.634  1.00 14.67 ? 71  HIS B ND1 1 
ATOM   2189 C CD2 . HIS B 2 71  ? 42.729 -31.083 10.314  1.00 13.14 ? 71  HIS B CD2 1 
ATOM   2190 C CE1 . HIS B 2 71  ? 42.589 -29.113 9.363   1.00 13.68 ? 71  HIS B CE1 1 
ATOM   2191 N NE2 . HIS B 2 71  ? 42.470 -30.412 9.147   1.00 14.07 ? 71  HIS B NE2 1 
ATOM   2192 N N   . TRP B 2 72  ? 42.609 -31.507 15.491  1.00 12.42 ? 72  TRP B N   1 
ATOM   2193 C CA  . TRP B 2 72  ? 42.772 -31.488 16.933  1.00 12.33 ? 72  TRP B CA  1 
ATOM   2194 C C   . TRP B 2 72  ? 43.219 -32.841 17.453  1.00 13.24 ? 72  TRP B C   1 
ATOM   2195 O O   . TRP B 2 72  ? 44.104 -32.920 18.316  1.00 13.34 ? 72  TRP B O   1 
ATOM   2196 C CB  . TRP B 2 72  ? 41.481 -31.055 17.626  1.00 14.01 ? 72  TRP B CB  1 
ATOM   2197 C CG  . TRP B 2 72  ? 41.118 -29.622 17.368  1.00 15.01 ? 72  TRP B CG  1 
ATOM   2198 C CD1 . TRP B 2 72  ? 41.439 -28.879 16.265  1.00 14.63 ? 72  TRP B CD1 1 
ATOM   2199 C CD2 . TRP B 2 72  ? 40.384 -28.746 18.249  1.00 17.09 ? 72  TRP B CD2 1 
ATOM   2200 N NE1 . TRP B 2 72  ? 40.923 -27.593 16.391  1.00 16.81 ? 72  TRP B NE1 1 
ATOM   2201 C CE2 . TRP B 2 72  ? 40.279 -27.487 17.598  1.00 15.57 ? 72  TRP B CE2 1 
ATOM   2202 C CE3 . TRP B 2 72  ? 39.792 -28.907 19.508  1.00 16.69 ? 72  TRP B CE3 1 
ATOM   2203 C CZ2 . TRP B 2 72  ? 39.604 -26.405 18.167  1.00 15.33 ? 72  TRP B CZ2 1 
ATOM   2204 C CZ3 . TRP B 2 72  ? 39.128 -27.825 20.078  1.00 17.10 ? 72  TRP B CZ3 1 
ATOM   2205 C CH2 . TRP B 2 72  ? 39.041 -26.587 19.401  1.00 15.79 ? 72  TRP B CH2 1 
ATOM   2206 N N   . ILE B 2 73  ? 42.611 -33.920 16.949  1.00 12.93 ? 73  ILE B N   1 
ATOM   2207 C CA  . ILE B 2 73  ? 43.037 -35.259 17.354  1.00 13.72 ? 73  ILE B CA  1 
ATOM   2208 C C   . ILE B 2 73  ? 44.532 -35.448 17.095  1.00 14.36 ? 73  ILE B C   1 
ATOM   2209 O O   . ILE B 2 73  ? 45.281 -35.921 17.967  1.00 13.74 ? 73  ILE B O   1 
ATOM   2210 C CB  . ILE B 2 73  ? 42.193 -36.333 16.647  1.00 12.63 ? 73  ILE B CB  1 
ATOM   2211 C CG1 . ILE B 2 73  ? 40.713 -36.121 16.972  1.00 12.33 ? 73  ILE B CG1 1 
ATOM   2212 C CG2 . ILE B 2 73  ? 42.651 -37.730 17.081  1.00 13.82 ? 73  ILE B CG2 1 
ATOM   2213 C CD1 . ILE B 2 73  ? 40.373 -36.212 18.417  1.00 12.05 ? 73  ILE B CD1 1 
ATOM   2214 N N   . ARG B 2 74  ? 44.992 -35.053 15.904  1.00 12.84 ? 74  ARG B N   1 
ATOM   2215 C CA  . ARG B 2 74  ? 46.404 -35.203 15.558  1.00 13.14 ? 74  ARG B CA  1 
ATOM   2216 C C   . ARG B 2 74  ? 47.306 -34.473 16.543  1.00 14.76 ? 74  ARG B C   1 
ATOM   2217 O O   . ARG B 2 74  ? 48.297 -35.035 17.046  1.00 14.90 ? 74  ARG B O   1 
ATOM   2218 C CB  . ARG B 2 74  ? 46.638 -34.683 14.156  1.00 12.17 ? 74  ARG B CB  1 
ATOM   2219 C CG  . ARG B 2 74  ? 46.201 -35.668 13.087  1.00 15.07 ? 74  ARG B CG  1 
ATOM   2220 C CD  . ARG B 2 74  ? 47.004 -36.958 13.149  1.00 14.58 ? 74  ARG B CD  1 
ATOM   2221 N NE  . ARG B 2 74  ? 46.845 -37.719 11.916  1.00 15.45 ? 74  ARG B NE  1 
ATOM   2222 C CZ  . ARG B 2 74  ? 47.228 -38.981 11.770  1.00 17.66 ? 74  ARG B CZ  1 
ATOM   2223 N NH1 . ARG B 2 74  ? 47.826 -39.635 12.753  1.00 17.09 ? 74  ARG B NH1 1 
ATOM   2224 N NH2 . ARG B 2 74  ? 47.029 -39.589 10.602  1.00 18.63 ? 74  ARG B NH2 1 
ATOM   2225 N N   . THR B 2 75  ? 46.993 -33.207 16.826  1.00 14.28 ? 75  THR B N   1 
ATOM   2226 C CA  . THR B 2 75  ? 47.838 -32.474 17.767  1.00 14.36 ? 75  THR B CA  1 
ATOM   2227 C C   . THR B 2 75  ? 47.794 -33.077 19.184  1.00 14.86 ? 75  THR B C   1 
ATOM   2228 O O   . THR B 2 75  ? 48.807 -33.053 19.900  1.00 12.30 ? 75  THR B O   1 
ATOM   2229 C CB  . THR B 2 75  ? 47.514 -30.964 17.728  1.00 13.68 ? 75  THR B CB  1 
ATOM   2230 O OG1 . THR B 2 75  ? 48.622 -30.228 18.245  1.00 15.08 ? 75  THR B OG1 1 
ATOM   2231 C CG2 . THR B 2 75  ? 46.304 -30.626 18.574  1.00 14.93 ? 75  THR B CG2 1 
ATOM   2232 N N   . TYR B 2 76  ? 46.639 -33.620 19.607  1.00 12.71 ? 76  TYR B N   1 
ATOM   2233 C CA  . TYR B 2 76  ? 46.575 -34.317 20.882  1.00 13.08 ? 76  TYR B CA  1 
ATOM   2234 C C   . TYR B 2 76  ? 47.571 -35.458 20.921  1.00 13.48 ? 76  TYR B C   1 
ATOM   2235 O O   . TYR B 2 76  ? 48.319 -35.618 21.892  1.00 14.82 ? 76  TYR B O   1 
ATOM   2236 C CB  . TYR B 2 76  ? 45.189 -34.903 21.090  1.00 13.95 ? 76  TYR B CB  1 
ATOM   2237 C CG  . TYR B 2 76  ? 44.112 -33.890 21.233  1.00 15.83 ? 76  TYR B CG  1 
ATOM   2238 C CD1 . TYR B 2 76  ? 44.375 -32.634 21.781  1.00 15.43 ? 76  TYR B CD1 1 
ATOM   2239 C CD2 . TYR B 2 76  ? 42.817 -34.191 20.834  1.00 15.58 ? 76  TYR B CD2 1 
ATOM   2240 C CE1 . TYR B 2 76  ? 43.363 -31.710 21.914  1.00 17.43 ? 76  TYR B CE1 1 
ATOM   2241 C CE2 . TYR B 2 76  ? 41.800 -33.280 20.970  1.00 16.20 ? 76  TYR B CE2 1 
ATOM   2242 C CZ  . TYR B 2 76  ? 42.071 -32.048 21.513  1.00 16.21 ? 76  TYR B CZ  1 
ATOM   2243 O OH  . TYR B 2 76  ? 41.048 -31.151 21.614  1.00 17.97 ? 76  TYR B OH  1 
ATOM   2244 N N   . ILE B 2 77  ? 47.545 -36.296 19.889  1.00 13.40 ? 77  ILE B N   1 
ATOM   2245 C CA  . ILE B 2 77  ? 48.431 -37.449 19.828  1.00 13.87 ? 77  ILE B CA  1 
ATOM   2246 C C   . ILE B 2 77  ? 49.877 -36.986 19.757  1.00 14.85 ? 77  ILE B C   1 
ATOM   2247 O O   . ILE B 2 77  ? 50.769 -37.568 20.399  1.00 14.55 ? 77  ILE B O   1 
ATOM   2248 C CB  . ILE B 2 77  ? 48.023 -38.300 18.614  1.00 13.16 ? 77  ILE B CB  1 
ATOM   2249 C CG1 . ILE B 2 77  ? 46.597 -38.805 18.842  1.00 11.92 ? 77  ILE B CG1 1 
ATOM   2250 C CG2 . ILE B 2 77  ? 49.016 -39.404 18.378  1.00 14.03 ? 77  ILE B CG2 1 
ATOM   2251 C CD1 . ILE B 2 77  ? 45.982 -39.459 17.652  1.00 13.07 ? 77  ILE B CD1 1 
ATOM   2252 N N   . HIS B 2 78  ? 50.123 -35.915 18.993  1.00 12.57 ? 78  HIS B N   1 
ATOM   2253 C CA  . HIS B 2 78  ? 51.474 -35.378 18.850  1.00 14.72 ? 78  HIS B CA  1 
ATOM   2254 C C   . HIS B 2 78  ? 52.125 -35.106 20.206  1.00 14.35 ? 78  HIS B C   1 
ATOM   2255 O O   . HIS B 2 78  ? 53.218 -35.597 20.505  1.00 15.04 ? 78  HIS B O   1 
ATOM   2256 C CB  . HIS B 2 78  ? 51.424 -34.105 18.005  1.00 13.35 ? 78  HIS B CB  1 
ATOM   2257 C CG  . HIS B 2 78  ? 52.735 -33.395 17.932  1.00 15.06 ? 78  HIS B CG  1 
ATOM   2258 N ND1 . HIS B 2 78  ? 53.679 -33.679 16.974  1.00 17.38 ? 78  HIS B ND1 1 
ATOM   2259 C CD2 . HIS B 2 78  ? 53.289 -32.461 18.739  1.00 17.79 ? 78  HIS B CD2 1 
ATOM   2260 C CE1 . HIS B 2 78  ? 54.749 -32.927 17.167  1.00 17.59 ? 78  HIS B CE1 1 
ATOM   2261 N NE2 . HIS B 2 78  ? 54.536 -32.177 18.232  1.00 18.96 ? 78  HIS B NE2 1 
ATOM   2262 N N   . HIS B 2 79  ? 51.449 -34.343 21.053  1.00 14.04 ? 79  HIS B N   1 
ATOM   2263 C CA  . HIS B 2 79  ? 51.998 -33.950 22.340  1.00 14.62 ? 79  HIS B CA  1 
ATOM   2264 C C   . HIS B 2 79  ? 51.836 -35.043 23.390  1.00 17.38 ? 79  HIS B C   1 
ATOM   2265 O O   . HIS B 2 79  ? 52.623 -35.101 24.351  1.00 16.68 ? 79  HIS B O   1 
ATOM   2266 C CB  . HIS B 2 79  ? 51.307 -32.671 22.809  1.00 17.06 ? 79  HIS B CB  1 
ATOM   2267 C CG  . HIS B 2 79  ? 51.616 -31.487 21.956  1.00 17.40 ? 79  HIS B CG  1 
ATOM   2268 N ND1 . HIS B 2 79  ? 52.865 -30.909 21.922  1.00 15.03 ? 79  HIS B ND1 1 
ATOM   2269 C CD2 . HIS B 2 79  ? 50.855 -30.814 21.052  1.00 15.91 ? 79  HIS B CD2 1 
ATOM   2270 C CE1 . HIS B 2 79  ? 52.853 -29.908 21.055  1.00 16.83 ? 79  HIS B CE1 1 
ATOM   2271 N NE2 . HIS B 2 79  ? 51.648 -29.831 20.511  1.00 15.50 ? 79  HIS B NE2 1 
ATOM   2272 N N   . GLY B 2 80  ? 50.828 -35.911 23.238  1.00 16.12 ? 80  GLY B N   1 
ATOM   2273 C CA  . GLY B 2 80  ? 50.750 -37.077 24.105  1.00 17.56 ? 80  GLY B CA  1 
ATOM   2274 C C   . GLY B 2 80  ? 51.997 -37.936 24.024  1.00 17.78 ? 80  GLY B C   1 
ATOM   2275 O O   . GLY B 2 80  ? 52.538 -38.360 25.047  1.00 19.34 ? 80  GLY B O   1 
ATOM   2276 N N   . VAL B 2 81  ? 52.478 -38.189 22.805  1.00 17.13 ? 81  VAL B N   1 
ATOM   2277 C CA  . VAL B 2 81  ? 53.712 -38.956 22.639  1.00 18.86 ? 81  VAL B CA  1 
ATOM   2278 C C   . VAL B 2 81  ? 54.926 -38.106 23.009  1.00 18.81 ? 81  VAL B C   1 
ATOM   2279 O O   . VAL B 2 81  ? 55.859 -38.586 23.660  1.00 18.10 ? 81  VAL B O   1 
ATOM   2280 C CB  . VAL B 2 81  ? 53.805 -39.546 21.218  1.00 20.14 ? 81  VAL B CB  1 
ATOM   2281 C CG1 . VAL B 2 81  ? 55.139 -40.270 21.018  1.00 19.53 ? 81  VAL B CG1 1 
ATOM   2282 C CG2 . VAL B 2 81  ? 52.623 -40.493 20.945  1.00 19.12 ? 81  VAL B CG2 1 
ATOM   2283 N N   . ARG B 2 82  ? 54.921 -36.826 22.609  1.00 19.88 ? 82  ARG B N   1 
ATOM   2284 C CA  . ARG B 2 82  ? 56.004 -35.899 22.949  1.00 19.41 ? 82  ARG B CA  1 
ATOM   2285 C C   . ARG B 2 82  ? 56.291 -35.886 24.451  1.00 17.85 ? 82  ARG B C   1 
ATOM   2286 O O   . ARG B 2 82  ? 57.446 -36.004 24.881  1.00 16.43 ? 82  ARG B O   1 
ATOM   2287 C CB  . ARG B 2 82  ? 55.661 -34.479 22.460  1.00 17.71 ? 82  ARG B CB  1 
ATOM   2288 C CG  . ARG B 2 82  ? 56.738 -33.427 22.798  1.00 20.14 ? 82  ARG B CG  1 
ATOM   2289 C CD  . ARG B 2 82  ? 56.327 -31.979 22.432  1.00 18.75 ? 82  ARG B CD  1 
ATOM   2290 N NE  . ARG B 2 82  ? 55.276 -31.491 23.314  1.00 14.79 ? 82  ARG B NE  1 
ATOM   2291 C CZ  . ARG B 2 82  ? 55.472 -30.995 24.523  1.00 14.72 ? 82  ARG B CZ  1 
ATOM   2292 N NH1 . ARG B 2 82  ? 56.685 -30.847 25.025  1.00 17.42 ? 82  ARG B NH1 1 
ATOM   2293 N NH2 . ARG B 2 82  ? 54.420 -30.639 25.253  1.00 17.67 ? 82  ARG B NH2 1 
ATOM   2294 N N   . THR B 2 83  ? 55.254 -35.707 25.265  1.00 16.31 ? 83  THR B N   1 
ATOM   2295 C CA  . THR B 2 83  ? 55.431 -35.708 26.710  1.00 19.33 ? 83  THR B CA  1 
ATOM   2296 C C   . THR B 2 83  ? 55.543 -37.119 27.303  1.00 18.90 ? 83  THR B C   1 
ATOM   2297 O O   . THR B 2 83  ? 55.890 -37.256 28.480  1.00 20.36 ? 83  THR B O   1 
ATOM   2298 C CB  . THR B 2 83  ? 54.279 -34.931 27.382  1.00 20.32 ? 83  THR B CB  1 
ATOM   2299 O OG1 . THR B 2 83  ? 53.023 -35.570 27.077  1.00 20.27 ? 83  THR B OG1 1 
ATOM   2300 C CG2 . THR B 2 83  ? 54.241 -33.478 26.876  1.00 16.95 ? 83  THR B CG2 1 
ATOM   2301 N N   . GLY B 2 84  ? 55.248 -38.162 26.523  1.00 20.62 ? 84  GLY B N   1 
ATOM   2302 C CA  . GLY B 2 84  ? 55.221 -39.524 27.025  1.00 18.82 ? 84  GLY B CA  1 
ATOM   2303 C C   . GLY B 2 84  ? 53.921 -39.940 27.671  1.00 21.75 ? 84  GLY B C   1 
ATOM   2304 O O   . GLY B 2 84  ? 53.850 -41.043 28.232  1.00 21.01 ? 84  GLY B O   1 
ATOM   2305 N N   . LYS B 2 85  ? 52.886 -39.091 27.612  1.00 23.05 ? 85  LYS B N   1 
ATOM   2306 C CA  . LYS B 2 85  ? 51.585 -39.394 28.208  1.00 23.00 ? 85  LYS B CA  1 
ATOM   2307 C C   . LYS B 2 85  ? 50.733 -40.344 27.365  1.00 19.67 ? 85  LYS B C   1 
ATOM   2308 O O   . LYS B 2 85  ? 49.765 -40.913 27.893  1.00 18.18 ? 85  LYS B O   1 
ATOM   2309 C CB  . LYS B 2 85  ? 50.797 -38.097 28.477  1.00 21.08 ? 85  LYS B CB  1 
ATOM   2310 C CG  . LYS B 2 85  ? 51.433 -37.208 29.507  1.00 20.15 ? 85  LYS B CG  1 
ATOM   2311 C CD  . LYS B 2 85  ? 50.702 -35.899 29.648  1.00 18.99 ? 85  LYS B CD  1 
ATOM   2312 C CE  . LYS B 2 85  ? 51.606 -34.883 30.327  1.00 18.28 ? 85  LYS B CE  1 
ATOM   2313 N NZ  . LYS B 2 85  ? 51.633 -35.204 31.770  1.00 19.46 ? 85  LYS B NZ  1 
ATOM   2314 N N   . ILE B 2 86  ? 51.054 -40.516 26.086  1.00 17.31 ? 86  ILE B N   1 
ATOM   2315 C CA  . ILE B 2 86  ? 50.275 -41.353 25.185  1.00 19.20 ? 86  ILE B CA  1 
ATOM   2316 C C   . ILE B 2 86  ? 51.217 -42.408 24.621  1.00 20.49 ? 86  ILE B C   1 
ATOM   2317 O O   . ILE B 2 86  ? 52.203 -42.072 23.949  1.00 18.06 ? 86  ILE B O   1 
ATOM   2318 C CB  . ILE B 2 86  ? 49.605 -40.534 24.057  1.00 17.71 ? 86  ILE B CB  1 
ATOM   2319 C CG1 . ILE B 2 86  ? 48.505 -39.628 24.629  1.00 16.69 ? 86  ILE B CG1 1 
ATOM   2320 C CG2 . ILE B 2 86  ? 49.006 -41.444 23.000  1.00 16.91 ? 86  ILE B CG2 1 
ATOM   2321 C CD1 . ILE B 2 86  ? 47.336 -40.389 25.205  1.00 17.73 ? 86  ILE B CD1 1 
ATOM   2322 N N   . ASP B 2 87  ? 50.911 -43.679 24.888  1.00 20.42 ? 87  ASP B N   1 
ATOM   2323 C CA  . ASP B 2 87  ? 51.692 -44.798 24.363  1.00 20.65 ? 87  ASP B CA  1 
ATOM   2324 C C   . ASP B 2 87  ? 51.062 -45.248 23.043  1.00 22.75 ? 87  ASP B C   1 
ATOM   2325 O O   . ASP B 2 87  ? 49.918 -45.736 23.019  1.00 22.54 ? 87  ASP B O   1 
ATOM   2326 C CB  . ASP B 2 87  ? 51.738 -45.932 25.382  1.00 20.93 ? 87  ASP B CB  1 
ATOM   2327 C CG  . ASP B 2 87  ? 52.676 -47.049 24.966  1.00 23.62 ? 87  ASP B CG  1 
ATOM   2328 O OD1 . ASP B 2 87  ? 52.257 -47.894 24.139  1.00 23.75 ? 87  ASP B OD1 1 
ATOM   2329 O OD2 . ASP B 2 87  ? 53.830 -47.056 25.468  1.00 22.00 ? 87  ASP B OD2 1 
ATOM   2330 N N   . LEU B 2 88  ? 51.811 -45.071 21.942  1.00 22.17 ? 88  LEU B N   1 
ATOM   2331 C CA  . LEU B 2 88  ? 51.254 -45.266 20.601  1.00 22.25 ? 88  LEU B CA  1 
ATOM   2332 C C   . LEU B 2 88  ? 50.724 -46.683 20.397  1.00 23.19 ? 88  LEU B C   1 
ATOM   2333 O O   . LEU B 2 88  ? 49.648 -46.871 19.814  1.00 23.20 ? 88  LEU B O   1 
ATOM   2334 C CB  . LEU B 2 88  ? 52.306 -44.965 19.532  1.00 21.04 ? 88  LEU B CB  1 
ATOM   2335 C CG  . LEU B 2 88  ? 52.309 -43.621 18.841  1.00 20.90 ? 88  LEU B CG  1 
ATOM   2336 C CD1 . LEU B 2 88  ? 53.298 -43.699 17.714  1.00 23.77 ? 88  LEU B CD1 1 
ATOM   2337 C CD2 . LEU B 2 88  ? 50.944 -43.291 18.320  1.00 23.33 ? 88  LEU B CD2 1 
ATOM   2338 N N   . GLU B 2 89  ? 51.508 -47.701 20.793  1.00 22.37 ? 89  GLU B N   1 
ATOM   2339 C CA  . GLU B 2 89  ? 51.127 -49.079 20.492  1.00 20.79 ? 89  GLU B CA  1 
ATOM   2340 C C   . GLU B 2 89  ? 49.817 -49.446 21.181  1.00 20.13 ? 89  GLU B C   1 
ATOM   2341 O O   . GLU B 2 89  ? 48.949 -50.104 20.587  1.00 19.22 ? 89  GLU B O   1 
ATOM   2342 C CB  . GLU B 2 89  ? 52.266 -50.032 20.850  1.00 19.22 ? 89  GLU B CB  1 
ATOM   2343 C CG  . GLU B 2 89  ? 53.423 -50.019 19.837  1.00 20.00 ? 89  GLU B CG  1 
ATOM   2344 C CD  . GLU B 2 89  ? 54.144 -48.672 19.755  1.00 22.47 ? 89  GLU B CD  1 
ATOM   2345 O OE1 . GLU B 2 89  ? 54.413 -48.080 20.836  1.00 24.70 ? 89  GLU B OE1 1 
ATOM   2346 O OE2 . GLU B 2 89  ? 54.463 -48.219 18.626  1.00 22.28 ? 89  GLU B OE2 1 
ATOM   2347 N N   . GLU B 2 90  ? 49.647 -48.997 22.422  1.00 20.34 ? 90  GLU B N   1 
ATOM   2348 C CA  . GLU B 2 90  ? 48.352 -49.086 23.085  1.00 21.22 ? 90  GLU B CA  1 
ATOM   2349 C C   . GLU B 2 90  ? 47.269 -48.379 22.268  1.00 21.60 ? 90  GLU B C   1 
ATOM   2350 O O   . GLU B 2 90  ? 46.219 -48.964 21.959  1.00 20.00 ? 90  GLU B O   1 
ATOM   2351 C CB  . GLU B 2 90  ? 48.466 -48.489 24.491  1.00 21.31 ? 90  GLU B CB  1 
ATOM   2352 C CG  . GLU B 2 90  ? 47.181 -48.540 25.325  1.00 23.06 ? 90  GLU B CG  1 
ATOM   2353 C CD  . GLU B 2 90  ? 46.646 -49.956 25.497  1.00 26.91 ? 90  GLU B CD  1 
ATOM   2354 O OE1 . GLU B 2 90  ? 47.384 -50.931 25.171  1.00 26.97 ? 90  GLU B OE1 1 
ATOM   2355 O OE2 . GLU B 2 90  ? 45.500 -50.093 25.979  1.00 25.72 ? 90  GLU B OE2 1 
ATOM   2356 N N   . LEU B 2 91  ? 47.519 -47.119 21.883  1.00 18.10 ? 91  LEU B N   1 
ATOM   2357 C CA  . LEU B 2 91  ? 46.532 -46.386 21.100  1.00 18.85 ? 91  LEU B CA  1 
ATOM   2358 C C   . LEU B 2 91  ? 46.125 -47.132 19.826  1.00 18.41 ? 91  LEU B C   1 
ATOM   2359 O O   . LEU B 2 91  ? 44.937 -47.208 19.483  1.00 16.46 ? 91  LEU B O   1 
ATOM   2360 C CB  . LEU B 2 91  ? 47.040 -44.974 20.799  1.00 18.54 ? 91  LEU B CB  1 
ATOM   2361 C CG  . LEU B 2 91  ? 46.127 -44.078 19.952  1.00 17.67 ? 91  LEU B CG  1 
ATOM   2362 C CD1 . LEU B 2 91  ? 44.717 -43.920 20.575  1.00 16.13 ? 91  LEU B CD1 1 
ATOM   2363 C CD2 . LEU B 2 91  ? 46.802 -42.716 19.831  1.00 15.31 ? 91  LEU B CD2 1 
ATOM   2364 N N   . GLU B 2 92  ? 47.102 -47.669 19.091  1.00 20.17 ? 92  GLU B N   1 
ATOM   2365 C CA  . GLU B 2 92  ? 46.771 -48.397 17.867  1.00 21.03 ? 92  GLU B CA  1 
ATOM   2366 C C   . GLU B 2 92  ? 45.982 -49.668 18.169  1.00 19.43 ? 92  GLU B C   1 
ATOM   2367 O O   . GLU B 2 92  ? 45.058 -50.023 17.418  1.00 18.49 ? 92  GLU B O   1 
ATOM   2368 C CB  . GLU B 2 92  ? 48.030 -48.696 17.047  1.00 22.01 ? 92  GLU B CB  1 
ATOM   2369 C CG  . GLU B 2 92  ? 48.619 -47.465 16.393  1.00 25.21 ? 92  GLU B CG  1 
ATOM   2370 C CD  . GLU B 2 92  ? 49.974 -47.740 15.782  1.00 33.93 ? 92  GLU B CD  1 
ATOM   2371 O OE1 . GLU B 2 92  ? 50.371 -48.938 15.742  1.00 35.95 ? 92  GLU B OE1 1 
ATOM   2372 O OE2 . GLU B 2 92  ? 50.647 -46.764 15.360  1.00 32.57 ? 92  GLU B OE2 1 
ATOM   2373 N N   . ARG B 2 93  ? 46.325 -50.365 19.255  1.00 17.82 ? 93  ARG B N   1 
ATOM   2374 C CA  . ARG B 2 93  ? 45.591 -51.579 19.580  1.00 19.45 ? 93  ARG B CA  1 
ATOM   2375 C C   . ARG B 2 93  ? 44.145 -51.262 19.925  1.00 18.98 ? 93  ARG B C   1 
ATOM   2376 O O   . ARG B 2 93  ? 43.231 -52.022 19.584  1.00 17.57 ? 93  ARG B O   1 
ATOM   2377 C CB  . ARG B 2 93  ? 46.232 -52.269 20.770  1.00 21.39 ? 93  ARG B CB  1 
ATOM   2378 C CG  . ARG B 2 93  ? 45.603 -53.632 21.021  1.00 23.46 ? 93  ARG B CG  1 
ATOM   2379 C CD  . ARG B 2 93  ? 45.975 -54.150 22.365  1.00 24.55 ? 93  ARG B CD  1 
ATOM   2380 N NE  . ARG B 2 93  ? 45.317 -53.316 23.374  1.00 31.31 ? 93  ARG B NE  1 
ATOM   2381 C CZ  . ARG B 2 93  ? 44.055 -53.460 23.777  1.00 30.08 ? 93  ARG B CZ  1 
ATOM   2382 N NH1 . ARG B 2 93  ? 43.276 -54.428 23.302  1.00 27.88 ? 93  ARG B NH1 1 
ATOM   2383 N NH2 . ARG B 2 93  ? 43.558 -52.610 24.678  1.00 27.14 ? 93  ARG B NH2 1 
ATOM   2384 N N   . ARG B 2 94  ? 43.927 -50.158 20.634  1.00 17.98 ? 94  ARG B N   1 
ATOM   2385 C CA  . ARG B 2 94  ? 42.570 -49.796 21.024  1.00 17.23 ? 94  ARG B CA  1 
ATOM   2386 C C   . ARG B 2 94  ? 41.751 -49.310 19.840  1.00 17.10 ? 94  ARG B C   1 
ATOM   2387 O O   . ARG B 2 94  ? 40.530 -49.499 19.813  1.00 18.17 ? 94  ARG B O   1 
ATOM   2388 C CB  . ARG B 2 94  ? 42.624 -48.710 22.083  1.00 17.24 ? 94  ARG B CB  1 
ATOM   2389 C CG  . ARG B 2 94  ? 43.300 -49.163 23.321  1.00 20.76 ? 94  ARG B CG  1 
ATOM   2390 C CD  . ARG B 2 94  ? 42.891 -48.312 24.467  1.00 21.13 ? 94  ARG B CD  1 
ATOM   2391 N NE  . ARG B 2 94  ? 43.415 -48.839 25.717  1.00 20.99 ? 94  ARG B NE  1 
ATOM   2392 C CZ  . ARG B 2 94  ? 43.064 -48.382 26.909  1.00 23.23 ? 94  ARG B CZ  1 
ATOM   2393 N NH1 . ARG B 2 94  ? 42.204 -47.380 27.036  1.00 21.11 ? 94  ARG B NH1 1 
ATOM   2394 N NH2 . ARG B 2 94  ? 43.592 -48.938 28.003  1.00 25.15 ? 94  ARG B NH2 1 
ATOM   2395 N N   . THR B 2 95  ? 42.395 -48.638 18.881  1.00 17.47 ? 95  THR B N   1 
ATOM   2396 C CA  . THR B 2 95  ? 41.703 -48.190 17.677  1.00 15.94 ? 95  THR B CA  1 
ATOM   2397 C C   . THR B 2 95  ? 41.116 -49.380 16.934  1.00 16.35 ? 95  THR B C   1 
ATOM   2398 O O   . THR B 2 95  ? 39.966 -49.340 16.496  1.00 16.17 ? 95  THR B O   1 
ATOM   2399 C CB  . THR B 2 95  ? 42.682 -47.380 16.810  1.00 15.29 ? 95  THR B CB  1 
ATOM   2400 O OG1 . THR B 2 95  ? 43.117 -46.235 17.544  1.00 15.26 ? 95  THR B OG1 1 
ATOM   2401 C CG2 . THR B 2 95  ? 42.048 -46.906 15.530  1.00 14.76 ? 95  THR B CG2 1 
ATOM   2402 N N   . GLN B 2 96  ? 41.892 -50.461 16.815  1.00 19.08 ? 96  GLN B N   1 
ATOM   2403 C CA  . GLN B 2 96  ? 41.434 -51.695 16.169  1.00 20.10 ? 96  GLN B CA  1 
ATOM   2404 C C   . GLN B 2 96  ? 40.353 -52.388 16.989  1.00 17.65 ? 96  GLN B C   1 
ATOM   2405 O O   . GLN B 2 96  ? 39.484 -53.070 16.434  1.00 19.47 ? 96  GLN B O   1 
ATOM   2406 C CB  . GLN B 2 96  ? 42.624 -52.648 15.951  1.00 20.52 ? 96  GLN B CB  1 
ATOM   2407 C CG  . GLN B 2 96  ? 42.272 -53.969 15.280  1.00 21.66 ? 96  GLN B CG  1 
ATOM   2408 C CD  . GLN B 2 96  ? 41.927 -53.826 13.796  1.00 23.07 ? 96  GLN B CD  1 
ATOM   2409 O OE1 . GLN B 2 96  ? 41.989 -52.736 13.204  1.00 22.25 ? 96  GLN B OE1 1 
ATOM   2410 N NE2 . GLN B 2 96  ? 41.568 -54.944 13.181  1.00 26.44 ? 96  GLN B NE2 1 
ATOM   2411 N N   . TYR B 2 97  ? 40.382 -52.222 18.298  1.00 16.70 ? 97  TYR B N   1 
ATOM   2412 C CA  . TYR B 2 97  ? 39.280 -52.707 19.112  1.00 18.33 ? 97  TYR B CA  1 
ATOM   2413 C C   . TYR B 2 97  ? 37.976 -51.980 18.765  1.00 18.40 ? 97  TYR B C   1 
ATOM   2414 O O   . TYR B 2 97  ? 36.931 -52.613 18.560  1.00 17.56 ? 97  TYR B O   1 
ATOM   2415 C CB  . TYR B 2 97  ? 39.651 -52.581 20.594  1.00 19.88 ? 97  TYR B CB  1 
ATOM   2416 C CG  . TYR B 2 97  ? 38.576 -53.021 21.577  1.00 20.45 ? 97  TYR B CG  1 
ATOM   2417 C CD1 . TYR B 2 97  ? 38.257 -54.370 21.724  1.00 21.98 ? 97  TYR B CD1 1 
ATOM   2418 C CD2 . TYR B 2 97  ? 37.927 -52.098 22.387  1.00 20.04 ? 97  TYR B CD2 1 
ATOM   2419 C CE1 . TYR B 2 97  ? 37.290 -54.784 22.622  1.00 21.31 ? 97  TYR B CE1 1 
ATOM   2420 C CE2 . TYR B 2 97  ? 36.955 -52.496 23.304  1.00 22.57 ? 97  TYR B CE2 1 
ATOM   2421 C CZ  . TYR B 2 97  ? 36.643 -53.852 23.420  1.00 25.58 ? 97  TYR B CZ  1 
ATOM   2422 O OH  . TYR B 2 97  ? 35.676 -54.279 24.330  1.00 25.53 ? 97  TYR B OH  1 
ATOM   2423 N N   . TYR B 2 98  ? 38.029 -50.648 18.648  1.00 16.11 ? 98  TYR B N   1 
ATOM   2424 C CA  . TYR B 2 98  ? 36.821 -49.865 18.399  1.00 16.61 ? 98  TYR B CA  1 
ATOM   2425 C C   . TYR B 2 98  ? 36.421 -49.818 16.943  1.00 16.66 ? 98  TYR B C   1 
ATOM   2426 O O   . TYR B 2 98  ? 35.270 -49.480 16.640  1.00 17.68 ? 98  TYR B O   1 
ATOM   2427 C CB  . TYR B 2 98  ? 36.993 -48.444 18.906  1.00 16.11 ? 98  TYR B CB  1 
ATOM   2428 C CG  . TYR B 2 98  ? 36.866 -48.373 20.388  1.00 16.60 ? 98  TYR B CG  1 
ATOM   2429 C CD1 . TYR B 2 98  ? 35.687 -48.785 21.015  1.00 16.70 ? 98  TYR B CD1 1 
ATOM   2430 C CD2 . TYR B 2 98  ? 37.906 -47.888 21.176  1.00 15.74 ? 98  TYR B CD2 1 
ATOM   2431 C CE1 . TYR B 2 98  ? 35.542 -48.718 22.365  1.00 16.58 ? 98  TYR B CE1 1 
ATOM   2432 C CE2 . TYR B 2 98  ? 37.777 -47.826 22.528  1.00 16.06 ? 98  TYR B CE2 1 
ATOM   2433 C CZ  . TYR B 2 98  ? 36.580 -48.242 23.130  1.00 19.14 ? 98  TYR B CZ  1 
ATOM   2434 O OH  . TYR B 2 98  ? 36.415 -48.178 24.503  1.00 20.57 ? 98  TYR B OH  1 
ATOM   2435 N N   . ARG B 2 99  ? 37.356 -50.088 16.038  1.00 16.81 ? 99  ARG B N   1 
ATOM   2436 C CA  . ARG B 2 99  ? 36.993 -50.462 14.683  1.00 16.78 ? 99  ARG B CA  1 
ATOM   2437 C C   . ARG B 2 99  ? 36.078 -51.685 14.702  1.00 17.95 ? 99  ARG B C   1 
ATOM   2438 O O   . ARG B 2 99  ? 35.025 -51.690 14.061  1.00 18.46 ? 99  ARG B O   1 
ATOM   2439 C CB  . ARG B 2 99  ? 38.264 -50.758 13.888  1.00 17.04 ? 99  ARG B CB  1 
ATOM   2440 C CG  . ARG B 2 99  ? 39.051 -49.542 13.425  1.00 17.64 ? 99  ARG B CG  1 
ATOM   2441 C CD  . ARG B 2 99  ? 40.151 -49.951 12.406  1.00 19.03 ? 99  ARG B CD  1 
ATOM   2442 N NE  . ARG B 2 99  ? 41.139 -48.900 12.115  1.00 21.79 ? 99  ARG B NE  1 
ATOM   2443 C CZ  . ARG B 2 99  ? 42.380 -48.863 12.603  1.00 19.62 ? 99  ARG B CZ  1 
ATOM   2444 N NH1 . ARG B 2 99  ? 42.798 -49.751 13.498  1.00 19.11 ? 99  ARG B NH1 1 
ATOM   2445 N NH2 . ARG B 2 99  ? 43.225 -47.924 12.170  1.00 16.84 ? 99  ARG B NH2 1 
ATOM   2446 N N   . GLU B 2 100 ? 36.444 -52.721 15.472  1.00 17.79 ? 100 GLU B N   1 
ATOM   2447 C CA  . GLU B 2 100 ? 35.727 -53.997 15.458  1.00 18.86 ? 100 GLU B CA  1 
ATOM   2448 C C   . GLU B 2 100 ? 34.581 -54.064 16.453  1.00 20.10 ? 100 GLU B C   1 
ATOM   2449 O O   . GLU B 2 100 ? 33.716 -54.944 16.316  1.00 20.75 ? 100 GLU B O   1 
ATOM   2450 C CB  . GLU B 2 100 ? 36.669 -55.156 15.805  1.00 19.61 ? 100 GLU B CB  1 
ATOM   2451 C CG  . GLU B 2 100 ? 37.810 -55.345 14.841  1.00 21.51 ? 100 GLU B CG  1 
ATOM   2452 C CD  . GLU B 2 100 ? 38.861 -56.312 15.357  1.00 25.70 ? 100 GLU B CD  1 
ATOM   2453 O OE1 . GLU B 2 100 ? 38.866 -56.622 16.573  1.00 24.60 ? 100 GLU B OE1 1 
ATOM   2454 O OE2 . GLU B 2 100 ? 39.711 -56.730 14.542  1.00 29.23 ? 100 GLU B OE2 1 
ATOM   2455 N N   . ASN B 2 101 ? 34.581 -53.203 17.472  1.00 17.82 ? 101 ASN B N   1 
ATOM   2456 C CA  . ASN B 2 101 ? 33.534 -53.159 18.491  1.00 18.65 ? 101 ASN B CA  1 
ATOM   2457 C C   . ASN B 2 101 ? 33.118 -51.707 18.688  1.00 18.22 ? 101 ASN B C   1 
ATOM   2458 O O   . ASN B 2 101 ? 33.326 -51.126 19.766  1.00 17.74 ? 101 ASN B O   1 
ATOM   2459 C CB  . ASN B 2 101 ? 34.033 -53.756 19.809  1.00 20.65 ? 101 ASN B CB  1 
ATOM   2460 C CG  . ASN B 2 101 ? 34.675 -55.138 19.624  1.00 21.93 ? 101 ASN B CG  1 
ATOM   2461 O OD1 . ASN B 2 101 ? 33.973 -56.154 19.593  1.00 21.30 ? 101 ASN B OD1 1 
ATOM   2462 N ND2 . ASN B 2 101 ? 36.009 -55.176 19.533  1.00 20.15 ? 101 ASN B ND2 1 
ATOM   2463 N N   . PRO B 2 102 ? 32.533 -51.086 17.657  1.00 17.31 ? 102 PRO B N   1 
ATOM   2464 C CA  . PRO B 2 102 ? 32.279 -49.635 17.723  1.00 17.82 ? 102 PRO B CA  1 
ATOM   2465 C C   . PRO B 2 102 ? 31.307 -49.242 18.826  1.00 19.34 ? 102 PRO B C   1 
ATOM   2466 O O   . PRO B 2 102 ? 31.281 -48.074 19.251  1.00 18.02 ? 102 PRO B O   1 
ATOM   2467 C CB  . PRO B 2 102 ? 31.727 -49.327 16.330  1.00 19.02 ? 102 PRO B CB  1 
ATOM   2468 C CG  . PRO B 2 102 ? 31.082 -50.631 15.910  1.00 19.27 ? 102 PRO B CG  1 
ATOM   2469 C CD  . PRO B 2 102 ? 32.065 -51.659 16.387  1.00 17.05 ? 102 PRO B CD  1 
ATOM   2470 N N   . ASP B 2 103 ? 30.538 -50.198 19.340  1.00 18.76 ? 103 ASP B N   1 
ATOM   2471 C CA  . ASP B 2 103 ? 29.606 -49.971 20.429  1.00 17.19 ? 103 ASP B CA  1 
ATOM   2472 C C   . ASP B 2 103 ? 30.129 -50.450 21.785  1.00 17.89 ? 103 ASP B C   1 
ATOM   2473 O O   . ASP B 2 103 ? 29.429 -50.331 22.792  1.00 20.96 ? 103 ASP B O   1 
ATOM   2474 C CB  . ASP B 2 103 ? 28.257 -50.621 20.085  1.00 17.65 ? 103 ASP B CB  1 
ATOM   2475 C CG  . ASP B 2 103 ? 27.620 -50.009 18.849  1.00 19.51 ? 103 ASP B CG  1 
ATOM   2476 O OD1 . ASP B 2 103 ? 27.888 -48.810 18.577  1.00 18.56 ? 103 ASP B OD1 1 
ATOM   2477 O OD2 . ASP B 2 103 ? 26.850 -50.712 18.152  1.00 19.09 ? 103 ASP B OD2 1 
ATOM   2478 N N   . ALA B 2 104 ? 31.343 -50.968 21.857  1.00 18.95 ? 104 ALA B N   1 
ATOM   2479 C CA  . ALA B 2 104 ? 31.877 -51.346 23.150  1.00 19.17 ? 104 ALA B CA  1 
ATOM   2480 C C   . ALA B 2 104 ? 31.829 -50.142 24.093  1.00 20.41 ? 104 ALA B C   1 
ATOM   2481 O O   . ALA B 2 104 ? 31.819 -48.985 23.648  1.00 17.66 ? 104 ALA B O   1 
ATOM   2482 C CB  . ALA B 2 104 ? 33.315 -51.830 22.992  1.00 20.78 ? 104 ALA B CB  1 
ATOM   2483 N N   . PRO B 2 105 ? 31.792 -50.385 25.399  1.00 21.67 ? 105 PRO B N   1 
ATOM   2484 C CA  . PRO B 2 105 ? 31.733 -49.272 26.346  1.00 21.93 ? 105 PRO B CA  1 
ATOM   2485 C C   . PRO B 2 105 ? 33.095 -48.604 26.487  1.00 22.75 ? 105 PRO B C   1 
ATOM   2486 O O   . PRO B 2 105 ? 34.145 -49.169 26.152  1.00 19.85 ? 105 PRO B O   1 
ATOM   2487 C CB  . PRO B 2 105 ? 31.299 -49.952 27.652  1.00 20.83 ? 105 PRO B CB  1 
ATOM   2488 C CG  . PRO B 2 105 ? 31.920 -51.290 27.537  1.00 23.72 ? 105 PRO B CG  1 
ATOM   2489 C CD  . PRO B 2 105 ? 31.684 -51.681 26.094  1.00 20.86 ? 105 PRO B CD  1 
ATOM   2490 N N   . LEU B 2 106 ? 33.046 -47.349 26.951  1.00 21.23 ? 106 LEU B N   1 
ATOM   2491 C CA  . LEU B 2 106 ? 34.237 -46.646 27.387  1.00 21.22 ? 106 LEU B CA  1 
ATOM   2492 C C   . LEU B 2 106 ? 34.666 -47.161 28.766  1.00 20.57 ? 106 LEU B C   1 
ATOM   2493 O O   . LEU B 2 106 ? 33.873 -47.786 29.481  1.00 20.87 ? 106 LEU B O   1 
ATOM   2494 C CB  . LEU B 2 106 ? 33.935 -45.156 27.461  1.00 19.61 ? 106 LEU B CB  1 
ATOM   2495 C CG  . LEU B 2 106 ? 33.761 -44.506 26.083  1.00 21.64 ? 106 LEU B CG  1 
ATOM   2496 C CD1 . LEU B 2 106 ? 33.152 -43.100 26.224  1.00 20.93 ? 106 LEU B CD1 1 
ATOM   2497 C CD2 . LEU B 2 106 ? 35.077 -44.465 25.286  1.00 18.02 ? 106 LEU B CD2 1 
ATOM   2498 N N   . PRO B 2 107 ? 35.921 -46.926 29.158  1.00 17.43 ? 107 PRO B N   1 
ATOM   2499 C CA  . PRO B 2 107 ? 36.356 -47.307 30.504  1.00 18.45 ? 107 PRO B CA  1 
ATOM   2500 C C   . PRO B 2 107 ? 35.426 -46.744 31.575  1.00 19.46 ? 107 PRO B C   1 
ATOM   2501 O O   . PRO B 2 107 ? 34.905 -45.630 31.447  1.00 18.78 ? 107 PRO B O   1 
ATOM   2502 C CB  . PRO B 2 107 ? 37.755 -46.683 30.601  1.00 17.61 ? 107 PRO B CB  1 
ATOM   2503 C CG  . PRO B 2 107 ? 38.220 -46.658 29.208  1.00 16.38 ? 107 PRO B CG  1 
ATOM   2504 C CD  . PRO B 2 107 ? 37.008 -46.242 28.429  1.00 17.50 ? 107 PRO B CD  1 
ATOM   2505 N N   . GLU B 2 108 ? 35.205 -47.540 32.633  1.00 19.05 ? 108 GLU B N   1 
ATOM   2506 C CA  . GLU B 2 108 ? 34.514 -47.052 33.815  1.00 18.29 ? 108 GLU B CA  1 
ATOM   2507 C C   . GLU B 2 108 ? 35.330 -45.931 34.430  1.00 20.52 ? 108 GLU B C   1 
ATOM   2508 O O   . GLU B 2 108 ? 36.555 -46.019 34.516  1.00 18.94 ? 108 GLU B O   1 
ATOM   2509 C CB  . GLU B 2 108 ? 34.366 -48.168 34.844  1.00 19.31 ? 108 GLU B CB  1 
ATOM   2510 C CG  . GLU B 2 108 ? 33.612 -49.408 34.310  1.00 25.99 ? 108 GLU B CG  1 
ATOM   2511 C CD  . GLU B 2 108 ? 32.067 -49.272 34.341  1.00 32.66 ? 108 GLU B CD  1 
ATOM   2512 O OE1 . GLU B 2 108 ? 31.515 -48.130 34.273  1.00 28.91 ? 108 GLU B OE1 1 
ATOM   2513 O OE2 . GLU B 2 108 ? 31.398 -50.330 34.452  1.00 34.44 ? 108 GLU B OE2 1 
ATOM   2514 N N   . HIS B 2 109 ? 34.648 -44.863 34.851  1.00 20.07 ? 109 HIS B N   1 
ATOM   2515 C CA  . HIS B 2 109 ? 35.342 -43.714 35.426  1.00 18.75 ? 109 HIS B CA  1 
ATOM   2516 C C   . HIS B 2 109 ? 34.399 -42.948 36.354  1.00 18.57 ? 109 HIS B C   1 
ATOM   2517 O O   . HIS B 2 109 ? 33.173 -43.065 36.267  1.00 16.61 ? 109 HIS B O   1 
ATOM   2518 C CB  . HIS B 2 109 ? 35.962 -42.795 34.350  1.00 17.43 ? 109 HIS B CB  1 
ATOM   2519 C CG  . HIS B 2 109 ? 34.951 -42.109 33.471  1.00 17.28 ? 109 HIS B CG  1 
ATOM   2520 N ND1 . HIS B 2 109 ? 34.297 -42.749 32.440  1.00 18.99 ? 109 HIS B ND1 1 
ATOM   2521 C CD2 . HIS B 2 109 ? 34.478 -40.837 33.487  1.00 15.12 ? 109 HIS B CD2 1 
ATOM   2522 C CE1 . HIS B 2 109 ? 33.474 -41.897 31.850  1.00 17.52 ? 109 HIS B CE1 1 
ATOM   2523 N NE2 . HIS B 2 109 ? 33.570 -40.729 32.465  1.00 14.29 ? 109 HIS B NE2 1 
ATOM   2524 N N   . GLU B 2 110 ? 35.001 -42.171 37.256  1.00 17.34 ? 110 GLU B N   1 
ATOM   2525 C CA  . GLU B 2 110 ? 34.256 -41.326 38.167  1.00 18.61 ? 110 GLU B CA  1 
ATOM   2526 C C   . GLU B 2 110 ? 34.148 -39.926 37.572  1.00 19.01 ? 110 GLU B C   1 
ATOM   2527 O O   . GLU B 2 110 ? 35.070 -39.437 36.908  1.00 16.20 ? 110 GLU B O   1 
ATOM   2528 C CB  . GLU B 2 110 ? 34.959 -41.246 39.523  1.00 20.64 ? 110 GLU B CB  1 
ATOM   2529 C CG  . GLU B 2 110 ? 36.286 -40.483 39.460  1.00 25.04 ? 110 GLU B CG  1 
ATOM   2530 C CD  . GLU B 2 110 ? 36.729 -39.911 40.820  1.00 32.35 ? 110 GLU B CD  1 
ATOM   2531 O OE1 . GLU B 2 110 ? 37.776 -39.199 40.868  1.00 29.61 ? 110 GLU B OE1 1 
ATOM   2532 O OE2 . GLU B 2 110 ? 36.027 -40.192 41.840  1.00 36.78 ? 110 GLU B OE2 1 
ATOM   2533 N N   . GLN B 2 111 ? 32.993 -39.298 37.775  1.00 19.77 ? 111 GLN B N   1 
ATOM   2534 C CA  . GLN B 2 111 ? 32.850 -37.904 37.379  1.00 20.18 ? 111 GLN B CA  1 
ATOM   2535 C C   . GLN B 2 111 ? 33.615 -37.019 38.366  1.00 18.71 ? 111 GLN B C   1 
ATOM   2536 O O   . GLN B 2 111 ? 33.762 -37.340 39.553  1.00 18.74 ? 111 GLN B O   1 
ATOM   2537 C CB  . GLN B 2 111 ? 31.366 -37.500 37.268  1.00 15.85 ? 111 GLN B CB  1 
ATOM   2538 C CG  . GLN B 2 111 ? 30.542 -38.372 36.289  1.00 16.99 ? 111 GLN B CG  1 
ATOM   2539 C CD  . GLN B 2 111 ? 31.154 -38.531 34.879  1.00 15.74 ? 111 GLN B CD  1 
ATOM   2540 O OE1 . GLN B 2 111 ? 31.484 -37.552 34.199  1.00 15.55 ? 111 GLN B OE1 1 
ATOM   2541 N NE2 . GLN B 2 111 ? 31.297 -39.784 34.431  1.00 14.64 ? 111 GLN B NE2 1 
ATOM   2542 N N   . LYS B 2 112 ? 34.139 -35.915 37.847  1.00 19.17 ? 112 LYS B N   1 
ATOM   2543 C CA  . LYS B 2 112 ? 35.010 -35.021 38.609  1.00 21.43 ? 112 LYS B CA  1 
ATOM   2544 C C   . LYS B 2 112 ? 34.460 -33.603 38.558  1.00 18.98 ? 112 LYS B C   1 
ATOM   2545 O O   . LYS B 2 112 ? 34.497 -32.967 37.481  1.00 19.60 ? 112 LYS B O   1 
ATOM   2546 C CB  . LYS B 2 112 ? 36.458 -35.086 38.108  1.00 21.00 ? 112 LYS B CB  1 
ATOM   2547 C CG  . LYS B 2 112 ? 37.242 -36.292 38.645  1.00 22.17 ? 112 LYS B CG  1 
ATOM   2548 C CD  . LYS B 2 112 ? 38.556 -36.481 37.916  1.00 21.22 ? 112 LYS B CD  1 
ATOM   2549 C CE  . LYS B 2 112 ? 39.303 -37.692 38.483  1.00 24.89 ? 112 LYS B CE  1 
ATOM   2550 N NZ  . LYS B 2 112 ? 40.733 -37.764 38.030  1.00 22.79 ? 112 LYS B NZ  1 
ATOM   2551 N N   . PRO B 2 113 ? 33.934 -33.084 39.673  1.00 18.64 ? 113 PRO B N   1 
ATOM   2552 C CA  . PRO B 2 113 ? 33.355 -31.725 39.645  1.00 20.82 ? 113 PRO B CA  1 
ATOM   2553 C C   . PRO B 2 113 ? 34.363 -30.641 39.315  1.00 19.61 ? 113 PRO B C   1 
ATOM   2554 O O   . PRO B 2 113 ? 33.985 -29.618 38.722  1.00 17.94 ? 113 PRO B O   1 
ATOM   2555 C CB  . PRO B 2 113 ? 32.769 -31.564 41.058  1.00 22.28 ? 113 PRO B CB  1 
ATOM   2556 C CG  . PRO B 2 113 ? 33.519 -32.565 41.883  1.00 20.79 ? 113 PRO B CG  1 
ATOM   2557 C CD  . PRO B 2 113 ? 33.700 -33.738 40.966  1.00 19.04 ? 113 PRO B CD  1 
ATOM   2558 N N   . GLU B 2 114 ? 35.638 -30.847 39.664  1.00 19.24 ? 114 GLU B N   1 
ATOM   2559 C CA  . GLU B 2 114 ? 36.644 -29.816 39.418  1.00 19.67 ? 114 GLU B CA  1 
ATOM   2560 C C   . GLU B 2 114 ? 36.871 -29.613 37.934  1.00 19.84 ? 114 GLU B C   1 
ATOM   2561 O O   . GLU B 2 114 ? 37.276 -28.511 37.529  1.00 18.13 ? 114 GLU B O   1 
ATOM   2562 C CB  . GLU B 2 114 ? 37.972 -30.147 40.094  1.00 17.37 ? 114 GLU B CB  1 
ATOM   2563 C CG  . GLU B 2 114 ? 38.551 -31.515 39.704  1.00 22.51 ? 114 GLU B CG  1 
ATOM   2564 C CD  . GLU B 2 114 ? 38.200 -32.654 40.679  1.00 26.28 ? 114 GLU B CD  1 
ATOM   2565 O OE1 . GLU B 2 114 ? 37.090 -32.648 41.277  1.00 24.72 ? 114 GLU B OE1 1 
ATOM   2566 O OE2 . GLU B 2 114 ? 39.057 -33.569 40.846  1.00 30.63 ? 114 GLU B OE2 1 
ATOM   2567 N N   . LEU B 2 115 ? 36.608 -30.662 37.109  1.00 19.29 ? 115 LEU B N   1 
ATOM   2568 C CA  . LEU B 2 115 ? 36.733 -30.554 35.653  1.00 18.44 ? 115 LEU B CA  1 
ATOM   2569 C C   . LEU B 2 115 ? 35.568 -29.779 35.046  1.00 18.13 ? 115 LEU B C   1 
ATOM   2570 O O   . LEU B 2 115 ? 35.723 -29.131 34.006  1.00 17.62 ? 115 LEU B O   1 
ATOM   2571 C CB  . LEU B 2 115 ? 36.779 -31.940 35.013  1.00 18.21 ? 115 LEU B CB  1 
ATOM   2572 C CG  . LEU B 2 115 ? 37.950 -32.836 35.433  1.00 19.33 ? 115 LEU B CG  1 
ATOM   2573 C CD1 . LEU B 2 115 ? 37.953 -34.123 34.609  1.00 17.24 ? 115 LEU B CD1 1 
ATOM   2574 C CD2 . LEU B 2 115 ? 39.305 -32.113 35.388  1.00 20.54 ? 115 LEU B CD2 1 
ATOM   2575 N N   . ILE B 2 116 ? 34.395 -29.840 35.675  1.00 17.87 ? 116 ILE B N   1 
ATOM   2576 C CA  . ILE B 2 116 ? 33.336 -28.928 35.285  1.00 17.90 ? 116 ILE B CA  1 
ATOM   2577 C C   . ILE B 2 116 ? 33.686 -27.510 35.736  1.00 18.87 ? 116 ILE B C   1 
ATOM   2578 O O   . ILE B 2 116 ? 33.585 -26.553 34.948  1.00 17.45 ? 116 ILE B O   1 
ATOM   2579 C CB  . ILE B 2 116 ? 31.976 -29.407 35.825  1.00 16.91 ? 116 ILE B CB  1 
ATOM   2580 C CG1 . ILE B 2 116 ? 31.687 -30.840 35.361  1.00 16.69 ? 116 ILE B CG1 1 
ATOM   2581 C CG2 . ILE B 2 116 ? 30.869 -28.502 35.318  1.00 16.95 ? 116 ILE B CG2 1 
ATOM   2582 C CD1 . ILE B 2 116 ? 31.732 -31.018 33.891  1.00 14.40 ? 116 ILE B CD1 1 
ATOM   2583 N N   . GLU B 2 117 ? 34.120 -27.361 37.004  1.00 17.97 ? 117 GLU B N   1 
ATOM   2584 C CA  . GLU B 2 117 ? 34.579 -26.063 37.500  1.00 18.43 ? 117 GLU B CA  1 
ATOM   2585 C C   . GLU B 2 117 ? 35.620 -25.473 36.567  1.00 17.61 ? 117 GLU B C   1 
ATOM   2586 O O   . GLU B 2 117 ? 35.559 -24.292 36.210  1.00 17.21 ? 117 GLU B O   1 
ATOM   2587 C CB  . GLU B 2 117 ? 35.164 -26.171 38.909  1.00 19.90 ? 117 GLU B CB  1 
ATOM   2588 C CG  . GLU B 2 117 ? 34.174 -26.503 40.032  1.00 23.98 ? 117 GLU B CG  1 
ATOM   2589 C CD  . GLU B 2 117 ? 34.832 -27.120 41.300  1.00 29.89 ? 117 GLU B CD  1 
ATOM   2590 O OE1 . GLU B 2 117 ? 34.156 -27.952 41.995  1.00 28.70 ? 117 GLU B OE1 1 
ATOM   2591 O OE2 . GLU B 2 117 ? 36.015 -26.781 41.602  1.00 28.21 ? 117 GLU B OE2 1 
ATOM   2592 N N   . PHE B 2 118 ? 36.581 -26.295 36.151  1.00 19.08 ? 118 PHE B N   1 
ATOM   2593 C CA  . PHE B 2 118 ? 37.602 -25.834 35.218  1.00 17.97 ? 118 PHE B CA  1 
ATOM   2594 C C   . PHE B 2 118 ? 36.973 -25.307 33.937  1.00 17.74 ? 118 PHE B C   1 
ATOM   2595 O O   . PHE B 2 118 ? 37.242 -24.172 33.520  1.00 17.63 ? 118 PHE B O   1 
ATOM   2596 C CB  . PHE B 2 118 ? 38.559 -26.980 34.915  1.00 17.78 ? 118 PHE B CB  1 
ATOM   2597 C CG  . PHE B 2 118 ? 39.745 -26.571 34.117  1.00 17.95 ? 118 PHE B CG  1 
ATOM   2598 C CD1 . PHE B 2 118 ? 40.839 -25.962 34.740  1.00 18.32 ? 118 PHE B CD1 1 
ATOM   2599 C CD2 . PHE B 2 118 ? 39.791 -26.815 32.742  1.00 20.03 ? 118 PHE B CD2 1 
ATOM   2600 C CE1 . PHE B 2 118 ? 41.972 -25.593 34.004  1.00 18.71 ? 118 PHE B CE1 1 
ATOM   2601 C CE2 . PHE B 2 118 ? 40.924 -26.434 31.975  1.00 19.46 ? 118 PHE B CE2 1 
ATOM   2602 C CZ  . PHE B 2 118 ? 42.014 -25.826 32.613  1.00 18.89 ? 118 PHE B CZ  1 
ATOM   2603 N N   . VAL B 2 119 ? 36.114 -26.121 33.308  1.00 18.99 ? 119 VAL B N   1 
ATOM   2604 C CA  . VAL B 2 119 ? 35.479 -25.748 32.039  1.00 17.28 ? 119 VAL B CA  1 
ATOM   2605 C C   . VAL B 2 119 ? 34.802 -24.387 32.160  1.00 18.54 ? 119 VAL B C   1 
ATOM   2606 O O   . VAL B 2 119 ? 35.057 -23.469 31.363  1.00 17.78 ? 119 VAL B O   1 
ATOM   2607 C CB  . VAL B 2 119 ? 34.476 -26.830 31.594  1.00 17.50 ? 119 VAL B CB  1 
ATOM   2608 C CG1 . VAL B 2 119 ? 33.513 -26.259 30.546  1.00 18.26 ? 119 VAL B CG1 1 
ATOM   2609 C CG2 . VAL B 2 119 ? 35.204 -28.028 31.020  1.00 17.91 ? 119 VAL B CG2 1 
ATOM   2610 N N   . ASN B 2 120 ? 33.905 -24.259 33.155  1.00 19.10 ? 120 ASN B N   1 
ATOM   2611 C CA  . ASN B 2 120 ? 33.107 -23.041 33.323  1.00 19.15 ? 120 ASN B CA  1 
ATOM   2612 C C   . ASN B 2 120 ? 33.996 -21.815 33.514  1.00 19.67 ? 120 ASN B C   1 
ATOM   2613 O O   . ASN B 2 120 ? 33.812 -20.789 32.844  1.00 17.97 ? 120 ASN B O   1 
ATOM   2614 C CB  . ASN B 2 120 ? 32.140 -23.214 34.494  1.00 17.19 ? 120 ASN B CB  1 
ATOM   2615 C CG  . ASN B 2 120 ? 30.973 -24.103 34.145  1.00 16.21 ? 120 ASN B CG  1 
ATOM   2616 O OD1 . ASN B 2 120 ? 30.639 -24.241 32.974  1.00 19.10 ? 120 ASN B OD1 1 
ATOM   2617 N ND2 . ASN B 2 120 ? 30.358 -24.725 35.148  1.00 16.75 ? 120 ASN B ND2 1 
ATOM   2618 N N   . GLN B 2 121 ? 34.961 -21.907 34.441  1.00 21.33 ? 121 GLN B N   1 
ATOM   2619 C CA  . GLN B 2 121 ? 35.937 -20.837 34.636  1.00 21.64 ? 121 GLN B CA  1 
ATOM   2620 C C   . GLN B 2 121 ? 36.599 -20.438 33.315  1.00 21.91 ? 121 GLN B C   1 
ATOM   2621 O O   . GLN B 2 121 ? 36.661 -19.249 32.968  1.00 21.20 ? 121 GLN B O   1 
ATOM   2622 C CB  . GLN B 2 121 ? 36.984 -21.269 35.671  1.00 19.87 ? 121 GLN B CB  1 
ATOM   2623 C CG  . GLN B 2 121 ? 37.748 -20.126 36.337  1.00 24.59 ? 121 GLN B CG  1 
ATOM   2624 C CD  . GLN B 2 121 ? 38.862 -19.529 35.453  1.00 27.45 ? 121 GLN B CD  1 
ATOM   2625 O OE1 . GLN B 2 121 ? 39.603 -20.260 34.779  1.00 25.75 ? 121 GLN B OE1 1 
ATOM   2626 N NE2 . GLN B 2 121 ? 39.005 -18.193 35.490  1.00 26.36 ? 121 GLN B NE2 1 
ATOM   2627 N N   . ALA B 2 122 ? 37.095 -21.420 32.554  1.00 19.38 ? 122 ALA B N   1 
ATOM   2628 C CA  . ALA B 2 122 ? 37.796 -21.076 31.323  1.00 19.03 ? 122 ALA B CA  1 
ATOM   2629 C C   . ALA B 2 122 ? 36.865 -20.418 30.298  1.00 19.22 ? 122 ALA B C   1 
ATOM   2630 O O   . ALA B 2 122 ? 37.278 -19.491 29.588  1.00 20.46 ? 122 ALA B O   1 
ATOM   2631 C CB  . ALA B 2 122 ? 38.498 -22.301 30.743  1.00 16.81 ? 122 ALA B CB  1 
ATOM   2632 N N   . VAL B 2 123 ? 35.614 -20.879 30.192  1.00 16.85 ? 123 VAL B N   1 
ATOM   2633 C CA  . VAL B 2 123 ? 34.728 -20.353 29.154  1.00 18.17 ? 123 VAL B CA  1 
ATOM   2634 C C   . VAL B 2 123 ? 34.328 -18.913 29.450  1.00 19.67 ? 123 VAL B C   1 
ATOM   2635 O O   . VAL B 2 123 ? 34.213 -18.082 28.533  1.00 19.27 ? 123 VAL B O   1 
ATOM   2636 C CB  . VAL B 2 123 ? 33.492 -21.251 28.967  1.00 19.45 ? 123 VAL B CB  1 
ATOM   2637 C CG1 . VAL B 2 123 ? 32.443 -20.527 28.118  1.00 16.38 ? 123 VAL B CG1 1 
ATOM   2638 C CG2 . VAL B 2 123 ? 33.902 -22.570 28.295  1.00 19.47 ? 123 VAL B CG2 1 
ATOM   2639 N N   . TYR B 2 124 ? 34.085 -18.596 30.725  1.00 18.51 ? 124 TYR B N   1 
ATOM   2640 C CA  . TYR B 2 124 ? 33.503 -17.307 31.059  1.00 18.85 ? 124 TYR B CA  1 
ATOM   2641 C C   . TYR B 2 124 ? 34.531 -16.278 31.509  1.00 19.25 ? 124 TYR B C   1 
ATOM   2642 O O   . TYR B 2 124 ? 34.335 -15.075 31.265  1.00 17.97 ? 124 TYR B O   1 
ATOM   2643 C CB  . TYR B 2 124 ? 32.321 -17.491 32.030  1.00 20.57 ? 124 TYR B CB  1 
ATOM   2644 C CG  . TYR B 2 124 ? 31.149 -18.095 31.274  1.00 21.35 ? 124 TYR B CG  1 
ATOM   2645 C CD1 . TYR B 2 124 ? 30.562 -17.384 30.212  1.00 23.16 ? 124 TYR B CD1 1 
ATOM   2646 C CD2 . TYR B 2 124 ? 30.687 -19.396 31.548  1.00 20.33 ? 124 TYR B CD2 1 
ATOM   2647 C CE1 . TYR B 2 124 ? 29.531 -17.923 29.461  1.00 24.39 ? 124 TYR B CE1 1 
ATOM   2648 C CE2 . TYR B 2 124 ? 29.645 -19.960 30.797  1.00 20.96 ? 124 TYR B CE2 1 
ATOM   2649 C CZ  . TYR B 2 124 ? 29.067 -19.212 29.752  1.00 28.64 ? 124 TYR B CZ  1 
ATOM   2650 O OH  . TYR B 2 124 ? 28.023 -19.730 28.972  1.00 29.82 ? 124 TYR B OH  1 
ATOM   2651 N N   . GLY B 2 125 ? 35.650 -16.735 32.088  1.00 19.24 ? 125 GLY B N   1 
ATOM   2652 C CA  . GLY B 2 125 ? 36.778 -15.882 32.431  1.00 18.36 ? 125 GLY B CA  1 
ATOM   2653 C C   . GLY B 2 125 ? 37.841 -15.783 31.348  1.00 19.97 ? 125 GLY B C   1 
ATOM   2654 O O   . GLY B 2 125 ? 38.537 -14.770 31.258  1.00 20.81 ? 125 GLY B O   1 
ATOM   2655 N N   . GLY B 2 126 ? 37.973 -16.824 30.510  1.00 18.19 ? 126 GLY B N   1 
ATOM   2656 C CA  . GLY B 2 126 ? 38.961 -16.838 29.460  1.00 16.69 ? 126 GLY B CA  1 
ATOM   2657 C C   . GLY B 2 126 ? 40.319 -17.282 29.970  1.00 17.14 ? 126 GLY B C   1 
ATOM   2658 O O   . GLY B 2 126 ? 40.503 -17.608 31.151  1.00 18.18 ? 126 GLY B O   1 
ATOM   2659 N N   . LEU B 2 127 ? 41.284 -17.299 29.031  1.00 16.80 ? 127 LEU B N   1 
ATOM   2660 C CA  . LEU B 2 127 ? 42.703 -17.564 29.292  1.00 16.69 ? 127 LEU B CA  1 
ATOM   2661 C C   . LEU B 2 127 ? 43.524 -16.430 28.675  1.00 17.52 ? 127 LEU B C   1 
ATOM   2662 O O   . LEU B 2 127 ? 44.173 -16.592 27.629  1.00 16.54 ? 127 LEU B O   1 
ATOM   2663 C CB  . LEU B 2 127 ? 43.144 -18.913 28.712  1.00 18.67 ? 127 LEU B CB  1 
ATOM   2664 C CG  . LEU B 2 127 ? 44.490 -19.461 29.258  1.00 19.36 ? 127 LEU B CG  1 
ATOM   2665 C CD1 . LEU B 2 127 ? 44.339 -20.190 30.602  1.00 18.65 ? 127 LEU B CD1 1 
ATOM   2666 C CD2 . LEU B 2 127 ? 45.202 -20.340 28.239  1.00 18.43 ? 127 LEU B CD2 1 
ATOM   2667 N N   . PRO B 2 128 ? 43.518 -15.256 29.303  1.00 17.59 ? 128 PRO B N   1 
ATOM   2668 C CA  . PRO B 2 128 ? 44.107 -14.077 28.649  1.00 16.26 ? 128 PRO B CA  1 
ATOM   2669 C C   . PRO B 2 128 ? 45.619 -14.218 28.466  1.00 15.21 ? 128 PRO B C   1 
ATOM   2670 O O   . PRO B 2 128 ? 46.337 -14.639 29.382  1.00 16.27 ? 128 PRO B O   1 
ATOM   2671 C CB  . PRO B 2 128 ? 43.749 -12.944 29.619  1.00 16.03 ? 128 PRO B CB  1 
ATOM   2672 C CG  . PRO B 2 128 ? 43.620 -13.660 30.948  1.00 17.59 ? 128 PRO B CG  1 
ATOM   2673 C CD  . PRO B 2 128 ? 42.918 -14.919 30.605  1.00 15.24 ? 128 PRO B CD  1 
ATOM   2674 N N   . ALA B 2 129 ? 46.098 -13.833 27.280  1.00 15.99 ? 129 ALA B N   1 
ATOM   2675 C CA  . ALA B 2 129 ? 47.510 -13.944 26.923  1.00 15.71 ? 129 ALA B CA  1 
ATOM   2676 C C   . ALA B 2 129 ? 48.315 -12.673 27.183  1.00 16.99 ? 129 ALA B C   1 
ATOM   2677 O O   . ALA B 2 129 ? 49.543 -12.687 26.988  1.00 15.95 ? 129 ALA B O   1 
ATOM   2678 C CB  . ALA B 2 129 ? 47.672 -14.359 25.460  1.00 12.95 ? 129 ALA B CB  1 
ATOM   2679 N N   . SER B 2 130 ? 47.670 -11.574 27.589  1.00 15.90 ? 130 SER B N   1 
ATOM   2680 C CA  . SER B 2 130 ? 48.407 -10.330 27.795  1.00 15.66 ? 130 SER B CA  1 
ATOM   2681 C C   . SER B 2 130 ? 49.303 -10.441 29.032  1.00 17.22 ? 130 SER B C   1 
ATOM   2682 O O   . SER B 2 130 ? 48.983 -11.132 30.012  1.00 15.96 ? 130 SER B O   1 
ATOM   2683 C CB  . SER B 2 130 ? 47.441 -9.169  27.967  1.00 15.40 ? 130 SER B CB  1 
ATOM   2684 O OG  . SER B 2 130 ? 46.575 -9.443  29.036  1.00 19.46 ? 130 SER B OG  1 
ATOM   2685 N N   . ARG B 2 131 ? 50.451 -9.765  28.974  1.00 16.43 ? 131 ARG B N   1 
ATOM   2686 C CA  . ARG B 2 131 ? 51.436 -9.856  30.038  1.00 18.15 ? 131 ARG B CA  1 
ATOM   2687 C C   . ARG B 2 131 ? 52.082 -8.492  30.220  1.00 18.04 ? 131 ARG B C   1 
ATOM   2688 O O   . ARG B 2 131 ? 52.099 -7.668  29.303  1.00 18.44 ? 131 ARG B O   1 
ATOM   2689 C CB  . ARG B 2 131 ? 52.500 -10.930 29.735  1.00 17.75 ? 131 ARG B CB  1 
ATOM   2690 C CG  . ARG B 2 131 ? 51.977 -12.365 29.613  1.00 15.05 ? 131 ARG B CG  1 
ATOM   2691 C CD  . ARG B 2 131 ? 51.579 -12.941 30.985  1.00 18.21 ? 131 ARG B CD  1 
ATOM   2692 N NE  . ARG B 2 131 ? 51.205 -14.353 30.910  1.00 16.57 ? 131 ARG B NE  1 
ATOM   2693 C CZ  . ARG B 2 131 ? 49.976 -14.799 30.660  1.00 16.69 ? 131 ARG B CZ  1 
ATOM   2694 N NH1 . ARG B 2 131 ? 48.950 -13.971 30.522  1.00 15.17 ? 131 ARG B NH1 1 
ATOM   2695 N NH2 . ARG B 2 131 ? 49.772 -16.114 30.534  1.00 16.70 ? 131 ARG B NH2 1 
ATOM   2696 N N   . GLU B 2 132 ? 52.602 -8.256  31.423  1.00 18.52 ? 132 GLU B N   1 
ATOM   2697 C CA  . GLU B 2 132 ? 53.355 -7.040  31.685  1.00 22.87 ? 132 GLU B CA  1 
ATOM   2698 C C   . GLU B 2 132 ? 54.851 -7.296  31.492  1.00 22.67 ? 132 GLU B C   1 
ATOM   2699 O O   . GLU B 2 132 ? 55.364 -8.366  31.835  1.00 20.13 ? 132 GLU B O   1 
ATOM   2700 C CB  . GLU B 2 132 ? 53.080 -6.530  33.103  1.00 25.40 ? 132 GLU B CB  1 
ATOM   2701 C CG  . GLU B 2 132 ? 51.677 -5.954  33.316  1.00 28.28 ? 132 GLU B CG  1 
ATOM   2702 C CD  . GLU B 2 132 ? 51.677 -4.432  33.495  1.00 34.75 ? 132 GLU B CD  1 
ATOM   2703 O OE1 . GLU B 2 132 ? 52.045 -3.702  32.528  1.00 32.99 ? 132 GLU B OE1 1 
ATOM   2704 O OE2 . GLU B 2 132 ? 51.312 -3.964  34.606  1.00 38.57 ? 132 GLU B OE2 1 
ATOM   2705 N N   . VAL B 2 133 ? 55.547 -6.308  30.927  1.00 22.09 ? 133 VAL B N   1 
ATOM   2706 C CA  . VAL B 2 133 ? 56.981 -6.406  30.679  1.00 22.44 ? 133 VAL B CA  1 
ATOM   2707 C C   . VAL B 2 133 ? 57.680 -5.161  31.223  1.00 27.32 ? 133 VAL B C   1 
ATOM   2708 O O   . VAL B 2 133 ? 57.096 -4.072  31.291  1.00 26.45 ? 133 VAL B O   1 
ATOM   2709 C CB  . VAL B 2 133 ? 57.307 -6.583  29.180  1.00 22.37 ? 133 VAL B CB  1 
ATOM   2710 C CG1 . VAL B 2 133 ? 56.786 -7.929  28.663  1.00 20.36 ? 133 VAL B CG1 1 
ATOM   2711 C CG2 . VAL B 2 133 ? 56.758 -5.381  28.364  1.00 20.88 ? 133 VAL B CG2 1 
ATOM   2712 N N   . ASP B 2 134 ? 58.959 -5.326  31.592  1.00 27.77 ? 134 ASP B N   1 
ATOM   2713 C CA  . ASP B 2 134 ? 59.765 -4.207  32.069  1.00 26.45 ? 134 ASP B CA  1 
ATOM   2714 C C   . ASP B 2 134 ? 60.230 -3.291  30.947  1.00 23.86 ? 134 ASP B C   1 
ATOM   2715 O O   . ASP B 2 134 ? 60.618 -2.154  31.226  1.00 24.65 ? 134 ASP B O   1 
ATOM   2716 C CB  . ASP B 2 134 ? 61.008 -4.708  32.828  1.00 30.04 ? 134 ASP B CB  1 
ATOM   2717 C CG  . ASP B 2 134 ? 60.665 -5.368  34.169  1.00 32.37 ? 134 ASP B CG  1 
ATOM   2718 O OD1 . ASP B 2 134 ? 59.843 -4.785  34.927  1.00 32.79 ? 134 ASP B OD1 1 
ATOM   2719 O OD2 . ASP B 2 134 ? 61.244 -6.452  34.477  1.00 32.31 ? 134 ASP B OD2 1 
ATOM   2720 N N   . ARG B 2 135 ? 60.224 -3.759  29.703  1.00 23.56 ? 135 ARG B N   1 
ATOM   2721 C CA  . ARG B 2 135 ? 60.687 -2.891  28.623  1.00 25.97 ? 135 ARG B CA  1 
ATOM   2722 C C   . ARG B 2 135 ? 59.514 -2.106  28.009  1.00 25.32 ? 135 ARG B C   1 
ATOM   2723 O O   . ARG B 2 135 ? 58.408 -2.656  27.847  1.00 22.69 ? 135 ARG B O   1 
ATOM   2724 C CB  . ARG B 2 135 ? 61.349 -3.713  27.512  1.00 25.94 ? 135 ARG B CB  1 
ATOM   2725 C CG  . ARG B 2 135 ? 60.344 -4.357  26.532  1.00 25.19 ? 135 ARG B CG  1 
ATOM   2726 C CD  . ARG B 2 135 ? 61.007 -5.382  25.647  1.00 25.05 ? 135 ARG B CD  1 
ATOM   2727 N NE  . ARG B 2 135 ? 61.532 -6.495  26.431  1.00 32.15 ? 135 ARG B NE  1 
ATOM   2728 C CZ  . ARG B 2 135 ? 60.929 -7.672  26.565  1.00 30.19 ? 135 ARG B CZ  1 
ATOM   2729 N NH1 . ARG B 2 135 ? 59.777 -7.931  25.959  1.00 25.11 ? 135 ARG B NH1 1 
ATOM   2730 N NH2 . ARG B 2 135 ? 61.503 -8.618  27.316  1.00 31.20 ? 135 ARG B NH2 1 
ATOM   2731 N N   . PRO B 2 136 ? 59.737 -0.834  27.654  1.00 24.45 ? 136 PRO B N   1 
ATOM   2732 C CA  . PRO B 2 136 ? 58.708 -0.071  26.925  1.00 24.31 ? 136 PRO B CA  1 
ATOM   2733 C C   . PRO B 2 136 ? 58.620 -0.490  25.462  1.00 21.03 ? 136 PRO B C   1 
ATOM   2734 O O   . PRO B 2 136 ? 59.560 -1.065  24.887  1.00 18.74 ? 136 PRO B O   1 
ATOM   2735 C CB  . PRO B 2 136 ? 59.195 1.388   27.072  1.00 24.10 ? 136 PRO B CB  1 
ATOM   2736 C CG  . PRO B 2 136 ? 60.676 1.264   27.131  1.00 22.67 ? 136 PRO B CG  1 
ATOM   2737 C CD  . PRO B 2 136 ? 60.870 0.039   28.035  1.00 24.58 ? 136 PRO B CD  1 
ATOM   2738 N N   . PRO B 2 137 ? 57.497 -0.204  24.814  1.00 17.59 ? 137 PRO B N   1 
ATOM   2739 C CA  . PRO B 2 137 ? 57.372 -0.547  23.402  1.00 17.77 ? 137 PRO B CA  1 
ATOM   2740 C C   . PRO B 2 137 ? 58.460 0.137   22.596  1.00 17.04 ? 137 PRO B C   1 
ATOM   2741 O O   . PRO B 2 137 ? 58.798 1.291   22.838  1.00 18.26 ? 137 PRO B O   1 
ATOM   2742 C CB  . PRO B 2 137 ? 55.973 -0.018  23.041  1.00 17.78 ? 137 PRO B CB  1 
ATOM   2743 C CG  . PRO B 2 137 ? 55.762 1.093   24.044  1.00 18.29 ? 137 PRO B CG  1 
ATOM   2744 C CD  . PRO B 2 137 ? 56.319 0.533   25.297  1.00 18.87 ? 137 PRO B CD  1 
ATOM   2745 N N   . LYS B 2 138 ? 59.007 -0.588  21.629  1.00 15.45 ? 138 LYS B N   1 
ATOM   2746 C CA  . LYS B 2 138 ? 60.006 -0.013  20.738  1.00 17.93 ? 138 LYS B CA  1 
ATOM   2747 C C   . LYS B 2 138 ? 59.382 0.894   19.674  1.00 17.38 ? 138 LYS B C   1 
ATOM   2748 O O   . LYS B 2 138 ? 60.014 1.885   19.262  1.00 16.48 ? 138 LYS B O   1 
ATOM   2749 C CB  . LYS B 2 138 ? 60.862 -1.134  20.114  1.00 16.64 ? 138 LYS B CB  1 
ATOM   2750 C CG  . LYS B 2 138 ? 62.164 -0.659  19.481  1.00 17.76 ? 138 LYS B CG  1 
ATOM   2751 C CD  . LYS B 2 138 ? 63.102 -1.835  19.237  1.00 19.43 ? 138 LYS B CD  1 
ATOM   2752 C CE  . LYS B 2 138 ? 64.304 -1.388  18.425  1.00 21.52 ? 138 LYS B CE  1 
ATOM   2753 N NZ  . LYS B 2 138 ? 65.001 -2.513  17.735  1.00 22.61 ? 138 LYS B NZ  1 
ATOM   2754 N N   . PHE B 2 139 ? 58.155 0.587   19.235  1.00 15.62 ? 139 PHE B N   1 
ATOM   2755 C CA  . PHE B 2 139 ? 57.519 1.259   18.105  1.00 15.95 ? 139 PHE B CA  1 
ATOM   2756 C C   . PHE B 2 139 ? 56.229 1.953   18.532  1.00 14.97 ? 139 PHE B C   1 
ATOM   2757 O O   . PHE B 2 139 ? 55.757 1.820   19.668  1.00 15.30 ? 139 PHE B O   1 
ATOM   2758 C CB  . PHE B 2 139 ? 57.239 0.283   16.943  1.00 15.94 ? 139 PHE B CB  1 
ATOM   2759 C CG  . PHE B 2 139 ? 58.449 -0.489  16.510  1.00 16.36 ? 139 PHE B CG  1 
ATOM   2760 C CD1 . PHE B 2 139 ? 59.475 0.139   15.818  1.00 16.32 ? 139 PHE B CD1 1 
ATOM   2761 C CD2 . PHE B 2 139 ? 58.593 -1.827  16.861  1.00 16.18 ? 139 PHE B CD2 1 
ATOM   2762 C CE1 . PHE B 2 139 ? 60.608 -0.559  15.453  1.00 16.71 ? 139 PHE B CE1 1 
ATOM   2763 C CE2 . PHE B 2 139 ? 59.731 -2.527  16.495  1.00 14.42 ? 139 PHE B CE2 1 
ATOM   2764 C CZ  . PHE B 2 139 ? 60.729 -1.892  15.799  1.00 16.47 ? 139 PHE B CZ  1 
ATOM   2765 N N   . LYS B 2 140 ? 55.658 2.689   17.576  1.00 16.12 ? 140 LYS B N   1 
ATOM   2766 C CA  . LYS B 2 140 ? 54.479 3.506   17.833  1.00 16.59 ? 140 LYS B CA  1 
ATOM   2767 C C   . LYS B 2 140 ? 53.725 3.750   16.527  1.00 15.43 ? 140 LYS B C   1 
ATOM   2768 O O   . LYS B 2 140 ? 54.290 3.665   15.428  1.00 15.58 ? 140 LYS B O   1 
ATOM   2769 C CB  . LYS B 2 140 ? 54.861 4.834   18.505  1.00 19.00 ? 140 LYS B CB  1 
ATOM   2770 C CG  . LYS B 2 140 ? 55.659 5.759   17.593  1.00 18.74 ? 140 LYS B CG  1 
ATOM   2771 C CD  . LYS B 2 140 ? 55.990 7.095   18.270  1.00 19.12 ? 140 LYS B CD  1 
ATOM   2772 C CE  . LYS B 2 140 ? 56.572 8.121   17.270  1.00 20.50 ? 140 LYS B CE  1 
ATOM   2773 N NZ  . LYS B 2 140 ? 57.866 7.783   16.607  1.00 20.64 ? 140 LYS B NZ  1 
ATOM   2774 N N   . GLU B 2 141 ? 52.434 4.080   16.668  1.00 15.89 ? 141 GLU B N   1 
ATOM   2775 C CA  . GLU B 2 141 ? 51.580 4.340   15.511  1.00 15.89 ? 141 GLU B CA  1 
ATOM   2776 C C   . GLU B 2 141 ? 52.222 5.333   14.534  1.00 15.63 ? 141 GLU B C   1 
ATOM   2777 O O   . GLU B 2 141 ? 52.803 6.351   14.924  1.00 15.03 ? 141 GLU B O   1 
ATOM   2778 C CB  . GLU B 2 141 ? 50.238 4.891   15.996  1.00 17.58 ? 141 GLU B CB  1 
ATOM   2779 C CG  . GLU B 2 141 ? 49.443 3.928   16.896  1.00 21.10 ? 141 GLU B CG  1 
ATOM   2780 C CD  . GLU B 2 141 ? 48.054 4.468   17.257  1.00 23.67 ? 141 GLU B CD  1 
ATOM   2781 O OE1 . GLU B 2 141 ? 47.593 5.383   16.541  1.00 30.94 ? 141 GLU B OE1 1 
ATOM   2782 O OE2 . GLU B 2 141 ? 47.435 4.003   18.248  1.00 19.67 ? 141 GLU B OE2 1 
ATOM   2783 N N   . GLY B 2 142 ? 52.086 5.038   13.245  1.00 17.75 ? 142 GLY B N   1 
ATOM   2784 C CA  . GLY B 2 142 ? 52.676 5.826   12.182  1.00 16.61 ? 142 GLY B CA  1 
ATOM   2785 C C   . GLY B 2 142 ? 54.065 5.395   11.753  1.00 15.74 ? 142 GLY B C   1 
ATOM   2786 O O   . GLY B 2 142 ? 54.464 5.695   10.626  1.00 14.86 ? 142 GLY B O   1 
ATOM   2787 N N   . ASP B 2 143 ? 54.807 4.710   12.629  1.00 15.81 ? 143 ASP B N   1 
ATOM   2788 C CA  . ASP B 2 143 ? 56.099 4.147   12.263  1.00 17.66 ? 143 ASP B CA  1 
ATOM   2789 C C   . ASP B 2 143 ? 55.970 3.231   11.047  1.00 18.96 ? 143 ASP B C   1 
ATOM   2790 O O   . ASP B 2 143 ? 55.084 2.367   10.982  1.00 16.09 ? 143 ASP B O   1 
ATOM   2791 C CB  . ASP B 2 143 ? 56.678 3.339   13.424  1.00 17.87 ? 143 ASP B CB  1 
ATOM   2792 C CG  . ASP B 2 143 ? 57.235 4.214   14.538  1.00 19.64 ? 143 ASP B CG  1 
ATOM   2793 O OD1 . ASP B 2 143 ? 57.266 5.459   14.377  1.00 22.52 ? 143 ASP B OD1 1 
ATOM   2794 O OD2 . ASP B 2 143 ? 57.659 3.652   15.568  1.00 18.39 ? 143 ASP B OD2 1 
ATOM   2795 N N   . VAL B 2 144 ? 56.866 3.433   10.077  1.00 20.64 ? 144 VAL B N   1 
ATOM   2796 C CA  . VAL B 2 144 ? 57.027 2.535   8.934   1.00 20.29 ? 144 VAL B CA  1 
ATOM   2797 C C   . VAL B 2 144 ? 58.027 1.452   9.331   1.00 21.07 ? 144 VAL B C   1 
ATOM   2798 O O   . VAL B 2 144 ? 59.132 1.754   9.810   1.00 20.47 ? 144 VAL B O   1 
ATOM   2799 C CB  . VAL B 2 144 ? 57.484 3.302   7.681   1.00 20.72 ? 144 VAL B CB  1 
ATOM   2800 C CG1 . VAL B 2 144 ? 57.756 2.343   6.573   1.00 20.81 ? 144 VAL B CG1 1 
ATOM   2801 C CG2 . VAL B 2 144 ? 56.417 4.306   7.256   1.00 19.39 ? 144 VAL B CG2 1 
ATOM   2802 N N   . VAL B 2 145 ? 57.617 0.188   9.174   1.00 19.77 ? 145 VAL B N   1 
ATOM   2803 C CA  . VAL B 2 145 ? 58.363 -0.966  9.664   1.00 19.32 ? 145 VAL B CA  1 
ATOM   2804 C C   . VAL B 2 145 ? 58.488 -2.004  8.552   1.00 18.83 ? 145 VAL B C   1 
ATOM   2805 O O   . VAL B 2 145 ? 57.737 -2.006  7.572   1.00 18.62 ? 145 VAL B O   1 
ATOM   2806 C CB  . VAL B 2 145 ? 57.740 -1.587  10.939  1.00 15.84 ? 145 VAL B CB  1 
ATOM   2807 C CG1 . VAL B 2 145 ? 57.862 -0.621  12.130  1.00 17.66 ? 145 VAL B CG1 1 
ATOM   2808 C CG2 . VAL B 2 145 ? 56.282 -1.924  10.677  1.00 15.45 ? 145 VAL B CG2 1 
ATOM   2809 N N   . ARG B 2 146 ? 59.486 -2.868  8.691   1.00 17.33 ? 146 ARG B N   1 
ATOM   2810 C CA  . ARG B 2 146 ? 59.724 -3.934  7.733   1.00 17.93 ? 146 ARG B CA  1 
ATOM   2811 C C   . ARG B 2 146 ? 59.641 -5.264  8.481   1.00 14.83 ? 146 ARG B C   1 
ATOM   2812 O O   . ARG B 2 146 ? 60.124 -5.385  9.606   1.00 14.39 ? 146 ARG B O   1 
ATOM   2813 C CB  . ARG B 2 146 ? 61.079 -3.757  6.996   1.00 16.16 ? 146 ARG B CB  1 
ATOM   2814 C CG  . ARG B 2 146 ? 61.445 -4.963  6.123   1.00 20.95 ? 146 ARG B CG  1 
ATOM   2815 C CD  . ARG B 2 146 ? 62.506 -4.644  5.051   1.00 29.09 ? 146 ARG B CD  1 
ATOM   2816 N NE  . ARG B 2 146 ? 63.271 -5.825  4.634   1.00 33.45 ? 146 ARG B NE  1 
ATOM   2817 C CZ  . ARG B 2 146 ? 63.186 -6.415  3.438   1.00 34.48 ? 146 ARG B CZ  1 
ATOM   2818 N NH1 . ARG B 2 146 ? 62.358 -5.970  2.496   1.00 30.07 ? 146 ARG B NH1 1 
ATOM   2819 N NH2 . ARG B 2 146 ? 63.945 -7.488  3.183   1.00 31.57 ? 146 ARG B NH2 1 
ATOM   2820 N N   . PHE B 2 147 ? 58.980 -6.242  7.868   1.00 16.08 ? 147 PHE B N   1 
ATOM   2821 C CA  . PHE B 2 147 ? 58.742 -7.537  8.490   1.00 14.40 ? 147 PHE B CA  1 
ATOM   2822 C C   . PHE B 2 147 ? 59.932 -8.452  8.237   1.00 11.83 ? 147 PHE B C   1 
ATOM   2823 O O   . PHE B 2 147 ? 60.486 -8.496  7.136   1.00 13.15 ? 147 PHE B O   1 
ATOM   2824 C CB  . PHE B 2 147 ? 57.467 -8.170  7.917   1.00 15.16 ? 147 PHE B CB  1 
ATOM   2825 C CG  . PHE B 2 147 ? 56.888 -9.258  8.775   1.00 14.15 ? 147 PHE B CG  1 
ATOM   2826 C CD1 . PHE B 2 147 ? 57.390 -10.552 8.710   1.00 14.32 ? 147 PHE B CD1 1 
ATOM   2827 C CD2 . PHE B 2 147 ? 55.845 -8.995  9.643   1.00 13.18 ? 147 PHE B CD2 1 
ATOM   2828 C CE1 . PHE B 2 147 ? 56.860 -11.565 9.496   1.00 14.32 ? 147 PHE B CE1 1 
ATOM   2829 C CE2 . PHE B 2 147 ? 55.294 -10.008 10.445  1.00 14.87 ? 147 PHE B CE2 1 
ATOM   2830 C CZ  . PHE B 2 147 ? 55.807 -11.295 10.373  1.00 14.65 ? 147 PHE B CZ  1 
ATOM   2831 N N   . SER B 2 148 ? 60.283 -9.201  9.265   1.00 12.70 ? 148 SER B N   1 
ATOM   2832 C CA  . SER B 2 148 ? 61.468 -10.044 9.256   1.00 14.51 ? 148 SER B CA  1 
ATOM   2833 C C   . SER B 2 148 ? 61.438 -11.031 8.087   1.00 15.57 ? 148 SER B C   1 
ATOM   2834 O O   . SER B 2 148 ? 60.377 -11.515 7.665   1.00 14.01 ? 148 SER B O   1 
ATOM   2835 C CB  . SER B 2 148 ? 61.546 -10.804 10.591  1.00 13.49 ? 148 SER B CB  1 
ATOM   2836 O OG  . SER B 2 148 ? 62.571 -11.768 10.595  1.00 13.38 ? 148 SER B OG  1 
ATOM   2837 N N   . THR B 2 149 ? 62.630 -11.329 7.556   1.00 16.87 ? 149 THR B N   1 
ATOM   2838 C CA  . THR B 2 149 ? 62.788 -12.361 6.535   1.00 16.81 ? 149 THR B CA  1 
ATOM   2839 C C   . THR B 2 149 ? 63.265 -13.703 7.109   1.00 17.07 ? 149 THR B C   1 
ATOM   2840 O O   . THR B 2 149 ? 63.565 -14.626 6.332   1.00 18.52 ? 149 THR B O   1 
ATOM   2841 C CB  . THR B 2 149 ? 63.732 -11.875 5.444   1.00 17.46 ? 149 THR B CB  1 
ATOM   2842 O OG1 . THR B 2 149 ? 64.986 -11.511 6.040   1.00 18.48 ? 149 THR B OG1 1 
ATOM   2843 C CG2 . THR B 2 149 ? 63.133 -10.661 4.734   1.00 17.31 ? 149 THR B CG2 1 
ATOM   2844 N N   . ALA B 2 150 ? 63.347 -13.835 8.437   1.00 15.56 ? 150 ALA B N   1 
ATOM   2845 C CA  . ALA B 2 150 ? 63.740 -15.107 9.023   1.00 16.73 ? 150 ALA B CA  1 
ATOM   2846 C C   . ALA B 2 150 ? 62.664 -16.147 8.743   1.00 17.77 ? 150 ALA B C   1 
ATOM   2847 O O   . ALA B 2 150 ? 61.483 -15.828 8.578   1.00 14.63 ? 150 ALA B O   1 
ATOM   2848 C CB  . ALA B 2 150 ? 63.954 -14.979 10.517  1.00 15.08 ? 150 ALA B CB  1 
ATOM   2849 N N   . SER B 2 151 ? 63.089 -17.406 8.679   1.00 17.86 ? 151 SER B N   1 
ATOM   2850 C CA  . SER B 2 151 ? 62.222 -18.503 8.247   1.00 17.95 ? 151 SER B CA  1 
ATOM   2851 C C   . SER B 2 151 ? 62.402 -19.680 9.190   1.00 18.60 ? 151 SER B C   1 
ATOM   2852 O O   . SER B 2 151 ? 62.865 -20.760 8.798   1.00 18.29 ? 151 SER B O   1 
ATOM   2853 C CB  . SER B 2 151 ? 62.538 -18.883 6.805   1.00 18.66 ? 151 SER B CB  1 
ATOM   2854 O OG  . SER B 2 151 ? 63.909 -19.229 6.683   1.00 18.60 ? 151 SER B OG  1 
ATOM   2855 N N   . PRO B 2 152 ? 62.031 -19.503 10.451  1.00 16.80 ? 152 PRO B N   1 
ATOM   2856 C CA  . PRO B 2 152 ? 62.273 -20.552 11.448  1.00 19.31 ? 152 PRO B CA  1 
ATOM   2857 C C   . PRO B 2 152 ? 61.535 -21.847 11.117  1.00 18.16 ? 152 PRO B C   1 
ATOM   2858 O O   . PRO B 2 152 ? 60.483 -21.851 10.474  1.00 18.30 ? 152 PRO B O   1 
ATOM   2859 C CB  . PRO B 2 152 ? 61.752 -19.927 12.744  1.00 19.50 ? 152 PRO B CB  1 
ATOM   2860 C CG  . PRO B 2 152 ? 60.705 -18.946 12.252  1.00 18.66 ? 152 PRO B CG  1 
ATOM   2861 C CD  . PRO B 2 152 ? 61.342 -18.350 11.034  1.00 17.16 ? 152 PRO B CD  1 
ATOM   2862 N N   . LYS B 2 153 ? 62.119 -22.960 11.562  1.00 19.29 ? 153 LYS B N   1 
ATOM   2863 C CA  . LYS B 2 153 ? 61.508 -24.269 11.334  1.00 19.42 ? 153 LYS B CA  1 
ATOM   2864 C C   . LYS B 2 153 ? 60.415 -24.549 12.357  1.00 19.11 ? 153 LYS B C   1 
ATOM   2865 O O   . LYS B 2 153 ? 59.465 -25.289 12.056  1.00 18.31 ? 153 LYS B O   1 
ATOM   2866 C CB  . LYS B 2 153 ? 62.564 -25.388 11.403  1.00 18.81 ? 153 LYS B CB  1 
ATOM   2867 C CG  . LYS B 2 153 ? 63.531 -25.414 10.236  1.00 22.04 ? 153 LYS B CG  1 
ATOM   2868 C CD  . LYS B 2 153 ? 62.909 -25.924 8.964   1.00 23.84 ? 153 LYS B CD  1 
ATOM   2869 C CE  . LYS B 2 153 ? 62.646 -27.418 9.022   1.00 23.93 ? 153 LYS B CE  1 
ATOM   2870 N NZ  . LYS B 2 153 ? 61.506 -27.756 8.130   1.00 24.26 ? 153 LYS B NZ  1 
ATOM   2871 N N   . GLY B 2 154 ? 60.534 -23.966 13.553  1.00 16.40 ? 154 GLY B N   1 
ATOM   2872 C CA  . GLY B 2 154 ? 59.557 -24.137 14.606  1.00 15.88 ? 154 GLY B CA  1 
ATOM   2873 C C   . GLY B 2 154 ? 58.354 -23.203 14.470  1.00 14.98 ? 154 GLY B C   1 
ATOM   2874 O O   . GLY B 2 154 ? 58.141 -22.529 13.458  1.00 13.84 ? 154 GLY B O   1 
ATOM   2875 N N   . HIS B 2 155 ? 57.565 -23.166 15.544  1.00 15.47 ? 155 HIS B N   1 
ATOM   2876 C CA  . HIS B 2 155 ? 56.341 -22.378 15.536  1.00 15.76 ? 155 HIS B CA  1 
ATOM   2877 C C   . HIS B 2 155 ? 56.643 -20.879 15.602  1.00 14.75 ? 155 HIS B C   1 
ATOM   2878 O O   . HIS B 2 155 ? 57.544 -20.427 16.321  1.00 13.48 ? 155 HIS B O   1 
ATOM   2879 C CB  . HIS B 2 155 ? 55.426 -22.795 16.692  1.00 14.80 ? 155 HIS B CB  1 
ATOM   2880 C CG  . HIS B 2 155 ? 54.100 -22.077 16.710  1.00 15.35 ? 155 HIS B CG  1 
ATOM   2881 N ND1 . HIS B 2 155 ? 53.140 -22.253 15.731  1.00 13.93 ? 155 HIS B ND1 1 
ATOM   2882 C CD2 . HIS B 2 155 ? 53.558 -21.224 17.620  1.00 15.28 ? 155 HIS B CD2 1 
ATOM   2883 C CE1 . HIS B 2 155 ? 52.091 -21.493 16.008  1.00 13.67 ? 155 HIS B CE1 1 
ATOM   2884 N NE2 . HIS B 2 155 ? 52.304 -20.883 17.162  1.00 13.98 ? 155 HIS B NE2 1 
ATOM   2885 N N   . ALA B 2 156 ? 55.863 -20.123 14.838  1.00 14.18 ? 156 ALA B N   1 
ATOM   2886 C CA  . ALA B 2 156 ? 55.872 -18.670 14.828  1.00 14.14 ? 156 ALA B CA  1 
ATOM   2887 C C   . ALA B 2 156 ? 54.635 -18.258 14.055  1.00 15.71 ? 156 ALA B C   1 
ATOM   2888 O O   . ALA B 2 156 ? 53.956 -19.100 13.451  1.00 15.02 ? 156 ALA B O   1 
ATOM   2889 C CB  . ALA B 2 156 ? 57.132 -18.103 14.156  1.00 14.53 ? 156 ALA B CB  1 
ATOM   2890 N N   . ARG B 2 157 ? 54.338 -16.953 14.084  1.00 13.40 ? 157 ARG B N   1 
ATOM   2891 C CA  . ARG B 2 157 ? 53.184 -16.451 13.326  1.00 15.95 ? 157 ARG B CA  1 
ATOM   2892 C C   . ARG B 2 157 ? 53.698 -15.511 12.240  1.00 15.25 ? 157 ARG B C   1 
ATOM   2893 O O   . ARG B 2 157 ? 53.367 -14.314 12.220  1.00 14.09 ? 157 ARG B O   1 
ATOM   2894 C CB  . ARG B 2 157 ? 52.169 -15.733 14.234  1.00 13.48 ? 157 ARG B CB  1 
ATOM   2895 C CG  . ARG B 2 157 ? 51.722 -16.557 15.440  1.00 14.12 ? 157 ARG B CG  1 
ATOM   2896 C CD  . ARG B 2 157 ? 50.880 -17.758 15.051  1.00 15.81 ? 157 ARG B CD  1 
ATOM   2897 N NE  . ARG B 2 157 ? 49.468 -17.440 14.861  1.00 14.83 ? 157 ARG B NE  1 
ATOM   2898 C CZ  . ARG B 2 157 ? 48.556 -18.323 14.472  1.00 15.26 ? 157 ARG B CZ  1 
ATOM   2899 N NH1 . ARG B 2 157 ? 48.893 -19.552 14.123  1.00 13.99 ? 157 ARG B NH1 1 
ATOM   2900 N NH2 . ARG B 2 157 ? 47.273 -17.971 14.462  1.00 13.51 ? 157 ARG B NH2 1 
ATOM   2901 N N   . ARG B 2 158 ? 54.515 -16.054 11.344  1.00 13.41 ? 158 ARG B N   1 
ATOM   2902 C CA  . ARG B 2 158 ? 55.186 -15.293 10.294  1.00 14.73 ? 158 ARG B CA  1 
ATOM   2903 C C   . ARG B 2 158 ? 54.659 -15.763 8.945   1.00 14.77 ? 158 ARG B C   1 
ATOM   2904 O O   . ARG B 2 158 ? 55.383 -16.387 8.168   1.00 15.97 ? 158 ARG B O   1 
ATOM   2905 C CB  . ARG B 2 158 ? 56.733 -15.444 10.391  1.00 13.98 ? 158 ARG B CB  1 
ATOM   2906 C CG  . ARG B 2 158 ? 57.290 -15.055 11.737  1.00 15.44 ? 158 ARG B CG  1 
ATOM   2907 C CD  . ARG B 2 158 ? 58.711 -15.560 11.950  1.00 14.61 ? 158 ARG B CD  1 
ATOM   2908 N NE  . ARG B 2 158 ? 59.264 -15.124 13.229  1.00 13.86 ? 158 ARG B NE  1 
ATOM   2909 C CZ  . ARG B 2 158 ? 60.109 -14.109 13.375  1.00 12.57 ? 158 ARG B CZ  1 
ATOM   2910 N NH1 . ARG B 2 158 ? 60.466 -13.354 12.343  1.00 13.77 ? 158 ARG B NH1 1 
ATOM   2911 N NH2 . ARG B 2 158 ? 60.595 -13.841 14.583  1.00 11.63 ? 158 ARG B NH2 1 
ATOM   2912 N N   . ALA B 2 159 ? 53.395 -15.456 8.661   1.00 14.37 ? 159 ALA B N   1 
ATOM   2913 C CA  . ALA B 2 159 ? 52.844 -15.770 7.356   1.00 13.40 ? 159 ALA B CA  1 
ATOM   2914 C C   . ALA B 2 159 ? 53.835 -15.386 6.270   1.00 15.77 ? 159 ALA B C   1 
ATOM   2915 O O   . ALA B 2 159 ? 54.463 -14.318 6.333   1.00 16.25 ? 159 ALA B O   1 
ATOM   2916 C CB  . ALA B 2 159 ? 51.530 -15.017 7.160   1.00 14.13 ? 159 ALA B CB  1 
ATOM   2917 N N   . ARG B 2 160 ? 53.978 -16.269 5.268   1.00 13.93 ? 160 ARG B N   1 
ATOM   2918 C CA  . ARG B 2 160 ? 54.988 -16.061 4.233   1.00 15.34 ? 160 ARG B CA  1 
ATOM   2919 C C   . ARG B 2 160 ? 54.672 -14.859 3.324   1.00 16.23 ? 160 ARG B C   1 
ATOM   2920 O O   . ARG B 2 160 ? 55.587 -14.253 2.747   1.00 15.16 ? 160 ARG B O   1 
ATOM   2921 C CB  . ARG B 2 160 ? 55.118 -17.330 3.410   1.00 17.08 ? 160 ARG B CB  1 
ATOM   2922 C CG  . ARG B 2 160 ? 56.134 -18.314 3.944   1.00 18.01 ? 160 ARG B CG  1 
ATOM   2923 C CD  . ARG B 2 160 ? 55.993 -19.644 3.205   1.00 24.58 ? 160 ARG B CD  1 
ATOM   2924 N NE  . ARG B 2 160 ? 54.627 -20.174 3.216   1.00 23.30 ? 160 ARG B NE  1 
ATOM   2925 C CZ  . ARG B 2 160 ? 54.224 -21.211 2.483   1.00 25.68 ? 160 ARG B CZ  1 
ATOM   2926 N NH1 . ARG B 2 160 ? 55.036 -21.800 1.607   1.00 26.11 ? 160 ARG B NH1 1 
ATOM   2927 N NH2 . ARG B 2 160 ? 52.977 -21.674 2.633   1.00 22.75 ? 160 ARG B NH2 1 
ATOM   2928 N N   . TYR B 2 161 ? 53.391 -14.496 3.188   1.00 15.48 ? 161 TYR B N   1 
ATOM   2929 C CA  . TYR B 2 161 ? 53.002 -13.388 2.329   1.00 13.54 ? 161 TYR B CA  1 
ATOM   2930 C C   . TYR B 2 161 ? 53.376 -12.020 2.898   1.00 12.67 ? 161 TYR B C   1 
ATOM   2931 O O   . TYR B 2 161 ? 53.355 -11.045 2.132   1.00 13.57 ? 161 TYR B O   1 
ATOM   2932 C CB  . TYR B 2 161 ? 51.504 -13.492 1.919   1.00 14.65 ? 161 TYR B CB  1 
ATOM   2933 C CG  . TYR B 2 161 ? 50.496 -13.014 2.964   1.00 14.74 ? 161 TYR B CG  1 
ATOM   2934 C CD1 . TYR B 2 161 ? 49.994 -13.879 3.941   1.00 16.53 ? 161 TYR B CD1 1 
ATOM   2935 C CD2 . TYR B 2 161 ? 50.058 -11.702 2.988   1.00 15.68 ? 161 TYR B CD2 1 
ATOM   2936 C CE1 . TYR B 2 161 ? 49.087 -13.441 4.916   1.00 15.68 ? 161 TYR B CE1 1 
ATOM   2937 C CE2 . TYR B 2 161 ? 49.143 -11.259 3.949   1.00 16.17 ? 161 TYR B CE2 1 
ATOM   2938 C CZ  . TYR B 2 161 ? 48.657 -12.129 4.909   1.00 15.76 ? 161 TYR B CZ  1 
ATOM   2939 O OH  . TYR B 2 161 ? 47.744 -11.679 5.853   1.00 15.93 ? 161 TYR B OH  1 
ATOM   2940 N N   . VAL B 2 162 ? 53.735 -11.924 4.191   1.00 12.99 ? 162 VAL B N   1 
ATOM   2941 C CA  . VAL B 2 162 ? 54.106 -10.638 4.796   1.00 14.38 ? 162 VAL B CA  1 
ATOM   2942 C C   . VAL B 2 162 ? 55.604 -10.473 5.015   1.00 14.82 ? 162 VAL B C   1 
ATOM   2943 O O   . VAL B 2 162 ? 56.047 -9.361  5.348   1.00 14.46 ? 162 VAL B O   1 
ATOM   2944 C CB  . VAL B 2 162 ? 53.347 -10.353 6.111   1.00 12.85 ? 162 VAL B CB  1 
ATOM   2945 C CG1 . VAL B 2 162 ? 51.838 -10.339 5.874   1.00 15.01 ? 162 VAL B CG1 1 
ATOM   2946 C CG2 . VAL B 2 162 ? 53.730 -11.339 7.184   1.00 12.97 ? 162 VAL B CG2 1 
ATOM   2947 N N   . ARG B 2 163 ? 56.396 -11.535 4.866   1.00 14.86 ? 163 ARG B N   1 
ATOM   2948 C CA  . ARG B 2 163 ? 57.808 -11.450 5.210   1.00 14.30 ? 163 ARG B CA  1 
ATOM   2949 C C   . ARG B 2 163 ? 58.559 -10.532 4.255   1.00 14.06 ? 163 ARG B C   1 
ATOM   2950 O O   . ARG B 2 163 ? 58.353 -10.556 3.035   1.00 13.95 ? 163 ARG B O   1 
ATOM   2951 C CB  . ARG B 2 163 ? 58.427 -12.830 5.164   1.00 15.10 ? 163 ARG B CB  1 
ATOM   2952 C CG  . ARG B 2 163 ? 57.812 -13.773 6.153   1.00 15.61 ? 163 ARG B CG  1 
ATOM   2953 C CD  . ARG B 2 163 ? 58.644 -15.023 6.195   1.00 15.45 ? 163 ARG B CD  1 
ATOM   2954 N NE  . ARG B 2 163 ? 57.952 -16.112 6.853   1.00 15.12 ? 163 ARG B NE  1 
ATOM   2955 C CZ  . ARG B 2 163 ? 58.329 -17.376 6.765   1.00 17.28 ? 163 ARG B CZ  1 
ATOM   2956 N NH1 . ARG B 2 163 ? 59.394 -17.726 6.049   1.00 17.00 ? 163 ARG B NH1 1 
ATOM   2957 N NH2 . ARG B 2 163 ? 57.616 -18.310 7.402   1.00 16.59 ? 163 ARG B NH2 1 
ATOM   2958 N N   . GLY B 2 164 ? 59.454 -9.728  4.828   1.00 15.03 ? 164 GLY B N   1 
ATOM   2959 C CA  . GLY B 2 164 ? 60.212 -8.767  4.058   1.00 15.89 ? 164 GLY B CA  1 
ATOM   2960 C C   . GLY B 2 164 ? 59.400 -7.627  3.504   1.00 16.49 ? 164 GLY B C   1 
ATOM   2961 O O   . GLY B 2 164 ? 59.927 -6.829  2.719   1.00 17.66 ? 164 GLY B O   1 
ATOM   2962 N N   . LYS B 2 165 ? 58.136 -7.513  3.902   1.00 16.13 ? 165 LYS B N   1 
ATOM   2963 C CA  . LYS B 2 165 ? 57.251 -6.439  3.463   1.00 16.79 ? 165 LYS B CA  1 
ATOM   2964 C C   . LYS B 2 165 ? 57.278 -5.259  4.446   1.00 14.81 ? 165 LYS B C   1 
ATOM   2965 O O   . LYS B 2 165 ? 57.636 -5.391  5.615   1.00 15.08 ? 165 LYS B O   1 
ATOM   2966 C CB  . LYS B 2 165 ? 55.826 -6.985  3.351   1.00 17.02 ? 165 LYS B CB  1 
ATOM   2967 C CG  . LYS B 2 165 ? 55.704 -8.156  2.404   1.00 13.79 ? 165 LYS B CG  1 
ATOM   2968 C CD  . LYS B 2 165 ? 55.764 -7.679  1.002   1.00 15.38 ? 165 LYS B CD  1 
ATOM   2969 C CE  . LYS B 2 165 ? 55.800 -8.819  0.054   1.00 15.47 ? 165 LYS B CE  1 
ATOM   2970 N NZ  . LYS B 2 165 ? 56.158 -8.321  -1.276  1.00 19.36 ? 165 LYS B NZ  1 
ATOM   2971 N N   . THR B 2 166 ? 56.872 -4.093  3.946   1.00 18.12 ? 166 THR B N   1 
ATOM   2972 C CA  . THR B 2 166 ? 56.894 -2.833  4.692   1.00 16.42 ? 166 THR B CA  1 
ATOM   2973 C C   . THR B 2 166 ? 55.468 -2.367  4.946   1.00 14.71 ? 166 THR B C   1 
ATOM   2974 O O   . THR B 2 166 ? 54.654 -2.307  4.016   1.00 17.29 ? 166 THR B O   1 
ATOM   2975 C CB  . THR B 2 166 ? 57.594 -1.742  3.877   1.00 16.39 ? 166 THR B CB  1 
ATOM   2976 O OG1 . THR B 2 166 ? 58.942 -2.144  3.608   1.00 20.04 ? 166 THR B OG1 1 
ATOM   2977 C CG2 . THR B 2 166 ? 57.610 -0.437  4.653   1.00 17.84 ? 166 THR B CG2 1 
ATOM   2978 N N   . GLY B 2 167 ? 55.175 -2.019  6.191   1.00 15.91 ? 167 GLY B N   1 
ATOM   2979 C CA  . GLY B 2 167 ? 53.888 -1.464  6.555   1.00 17.54 ? 167 GLY B CA  1 
ATOM   2980 C C   . GLY B 2 167 ? 54.021 -0.413  7.644   1.00 17.85 ? 167 GLY B C   1 
ATOM   2981 O O   . GLY B 2 167 ? 55.115 -0.149  8.152   1.00 19.46 ? 167 GLY B O   1 
ATOM   2982 N N   . THR B 2 168 ? 52.883 0.171   8.008   1.00 15.07 ? 168 THR B N   1 
ATOM   2983 C CA  . THR B 2 168 ? 52.825 1.213   9.020   1.00 16.23 ? 168 THR B CA  1 
ATOM   2984 C C   . THR B 2 168 ? 52.160 0.652   10.270  1.00 15.35 ? 168 THR B C   1 
ATOM   2985 O O   . THR B 2 168 ? 51.112 0.008   10.177  1.00 15.69 ? 168 THR B O   1 
ATOM   2986 C CB  . THR B 2 168 ? 52.030 2.436   8.523   1.00 16.57 ? 168 THR B CB  1 
ATOM   2987 O OG1 . THR B 2 168 ? 52.588 2.931   7.301   1.00 20.03 ? 168 THR B OG1 1 
ATOM   2988 C CG2 . THR B 2 168 ? 52.059 3.563   9.569   1.00 18.56 ? 168 THR B CG2 1 
ATOM   2989 N N   . VAL B 2 169 ? 52.767 0.902   11.433  1.00 14.12 ? 169 VAL B N   1 
ATOM   2990 C CA  . VAL B 2 169 ? 52.161 0.480   12.684  1.00 14.95 ? 169 VAL B CA  1 
ATOM   2991 C C   . VAL B 2 169 ? 50.843 1.214   12.868  1.00 17.27 ? 169 VAL B C   1 
ATOM   2992 O O   . VAL B 2 169 ? 50.739 2.424   12.626  1.00 16.29 ? 169 VAL B O   1 
ATOM   2993 C CB  . VAL B 2 169 ? 53.114 0.651   13.879  1.00 14.98 ? 169 VAL B CB  1 
ATOM   2994 C CG1 . VAL B 2 169 ? 52.393 0.312   15.148  1.00 15.17 ? 169 VAL B CG1 1 
ATOM   2995 C CG2 . VAL B 2 169 ? 54.341 -0.252  13.738  1.00 13.62 ? 169 VAL B CG2 1 
ATOM   2996 N N   . VAL B 2 170 ? 49.815 0.461   13.247  1.00 17.04 ? 170 VAL B N   1 
ATOM   2997 C CA  . VAL B 2 170 ? 48.472 0.978   13.426  1.00 17.30 ? 170 VAL B CA  1 
ATOM   2998 C C   . VAL B 2 170 ? 48.115 1.094   14.903  1.00 17.52 ? 170 VAL B C   1 
ATOM   2999 O O   . VAL B 2 170 ? 47.520 2.086   15.337  1.00 18.51 ? 170 VAL B O   1 
ATOM   3000 C CB  . VAL B 2 170 ? 47.462 0.086   12.658  1.00 18.44 ? 170 VAL B CB  1 
ATOM   3001 C CG1 . VAL B 2 170 ? 46.018 0.481   12.933  1.00 21.36 ? 170 VAL B CG1 1 
ATOM   3002 C CG2 . VAL B 2 170 ? 47.755 0.142   11.165  1.00 16.79 ? 170 VAL B CG2 1 
ATOM   3003 N N   . LYS B 2 171 ? 48.514 0.119   15.703  1.00 17.26 ? 171 LYS B N   1 
ATOM   3004 C CA  . LYS B 2 171 ? 48.201 0.176   17.118  1.00 18.48 ? 171 LYS B CA  1 
ATOM   3005 C C   . LYS B 2 171 ? 49.198 -0.710  17.852  1.00 16.86 ? 171 LYS B C   1 
ATOM   3006 O O   . LYS B 2 171 ? 49.566 -1.770  17.349  1.00 17.10 ? 171 LYS B O   1 
ATOM   3007 C CB  . LYS B 2 171 ? 46.753 -0.300  17.363  1.00 18.23 ? 171 LYS B CB  1 
ATOM   3008 C CG  . LYS B 2 171 ? 46.225 -0.010  18.758  1.00 20.73 ? 171 LYS B CG  1 
ATOM   3009 C CD  . LYS B 2 171 ? 44.729 -0.291  18.884  1.00 22.81 ? 171 LYS B CD  1 
ATOM   3010 C CE  . LYS B 2 171 ? 44.163 0.281   20.203  1.00 28.04 ? 171 LYS B CE  1 
ATOM   3011 N NZ  . LYS B 2 171 ? 45.206 0.560   21.267  1.00 27.93 ? 171 LYS B NZ  1 
ATOM   3012 N N   . HIS B 2 172 ? 49.655 -0.256  19.015  1.00 15.72 ? 172 HIS B N   1 
ATOM   3013 C CA  . HIS B 2 172 ? 50.366 -1.108  19.956  1.00 15.55 ? 172 HIS B CA  1 
ATOM   3014 C C   . HIS B 2 172 ? 49.343 -1.619  20.954  1.00 16.94 ? 172 HIS B C   1 
ATOM   3015 O O   . HIS B 2 172 ? 48.500 -0.845  21.418  1.00 19.21 ? 172 HIS B O   1 
ATOM   3016 C CB  . HIS B 2 172 ? 51.414 -0.295  20.704  1.00 15.42 ? 172 HIS B CB  1 
ATOM   3017 C CG  . HIS B 2 172 ? 51.963 -0.979  21.919  1.00 16.80 ? 172 HIS B CG  1 
ATOM   3018 N ND1 . HIS B 2 172 ? 51.826 -0.462  23.191  1.00 17.03 ? 172 HIS B ND1 1 
ATOM   3019 C CD2 . HIS B 2 172 ? 52.708 -2.106  22.046  1.00 15.47 ? 172 HIS B CD2 1 
ATOM   3020 C CE1 . HIS B 2 172 ? 52.441 -1.257  24.053  1.00 18.04 ? 172 HIS B CE1 1 
ATOM   3021 N NE2 . HIS B 2 172 ? 52.985 -2.261  23.380  1.00 16.83 ? 172 HIS B NE2 1 
ATOM   3022 N N   . HIS B 2 173 ? 49.400 -2.923  21.272  1.00 16.14 ? 173 HIS B N   1 
ATOM   3023 C CA  . HIS B 2 173 ? 48.371 -3.572  22.092  1.00 15.59 ? 173 HIS B CA  1 
ATOM   3024 C C   . HIS B 2 173 ? 48.806 -3.910  23.509  1.00 16.02 ? 173 HIS B C   1 
ATOM   3025 O O   . HIS B 2 173 ? 47.987 -4.417  24.291  1.00 17.04 ? 173 HIS B O   1 
ATOM   3026 C CB  . HIS B 2 173 ? 47.849 -4.859  21.436  1.00 14.83 ? 173 HIS B CB  1 
ATOM   3027 C CG  . HIS B 2 173 ? 47.243 -4.653  20.087  1.00 15.01 ? 173 HIS B CG  1 
ATOM   3028 N ND1 . HIS B 2 173 ? 46.012 -4.062  19.912  1.00 14.78 ? 173 HIS B ND1 1 
ATOM   3029 C CD2 . HIS B 2 173 ? 47.683 -4.986  18.849  1.00 13.47 ? 173 HIS B CD2 1 
ATOM   3030 C CE1 . HIS B 2 173 ? 45.729 -4.023  18.621  1.00 15.16 ? 173 HIS B CE1 1 
ATOM   3031 N NE2 . HIS B 2 173 ? 46.725 -4.580  17.956  1.00 14.96 ? 173 HIS B NE2 1 
ATOM   3032 N N   . GLY B 2 174 ? 50.045 -3.632  23.880  1.00 16.78 ? 174 GLY B N   1 
ATOM   3033 C CA  . GLY B 2 174 ? 50.623 -4.218  25.083  1.00 16.29 ? 174 GLY B CA  1 
ATOM   3034 C C   . GLY B 2 174 ? 51.457 -5.453  24.752  1.00 14.27 ? 174 GLY B C   1 
ATOM   3035 O O   . GLY B 2 174 ? 51.611 -5.861  23.592  1.00 14.94 ? 174 GLY B O   1 
ATOM   3036 N N   . ALA B 2 175 ? 51.991 -6.058  25.796  1.00 14.08 ? 175 ALA B N   1 
ATOM   3037 C CA  . ALA B 2 175 ? 52.839 -7.229  25.631  1.00 15.23 ? 175 ALA B CA  1 
ATOM   3038 C C   . ALA B 2 175 ? 52.015 -8.503  25.789  1.00 16.09 ? 175 ALA B C   1 
ATOM   3039 O O   . ALA B 2 175 ? 51.091 -8.569  26.609  1.00 16.27 ? 175 ALA B O   1 
ATOM   3040 C CB  . ALA B 2 175 ? 53.973 -7.213  26.659  1.00 16.67 ? 175 ALA B CB  1 
ATOM   3041 N N   . TYR B 2 176 ? 52.365 -9.521  25.003  1.00 16.15 ? 176 TYR B N   1 
ATOM   3042 C CA  . TYR B 2 176 ? 51.631 -10.781 24.960  1.00 16.17 ? 176 TYR B CA  1 
ATOM   3043 C C   . TYR B 2 176 ? 52.600 -11.947 24.825  1.00 17.81 ? 176 TYR B C   1 
ATOM   3044 O O   . TYR B 2 176 ? 53.695 -11.793 24.269  1.00 15.99 ? 176 TYR B O   1 
ATOM   3045 C CB  . TYR B 2 176 ? 50.659 -10.836 23.777  1.00 13.46 ? 176 TYR B CB  1 
ATOM   3046 C CG  . TYR B 2 176 ? 49.478 -9.927  23.952  1.00 14.50 ? 176 TYR B CG  1 
ATOM   3047 C CD1 . TYR B 2 176 ? 49.580 -8.568  23.706  1.00 15.42 ? 176 TYR B CD1 1 
ATOM   3048 C CD2 . TYR B 2 176 ? 48.264 -10.426 24.388  1.00 14.92 ? 176 TYR B CD2 1 
ATOM   3049 C CE1 . TYR B 2 176 ? 48.488 -7.727  23.882  1.00 15.64 ? 176 TYR B CE1 1 
ATOM   3050 C CE2 . TYR B 2 176 ? 47.170 -9.604  24.550  1.00 15.09 ? 176 TYR B CE2 1 
ATOM   3051 C CZ  . TYR B 2 176 ? 47.287 -8.260  24.310  1.00 14.40 ? 176 TYR B CZ  1 
ATOM   3052 O OH  . TYR B 2 176 ? 46.194 -7.451  24.502  1.00 14.98 ? 176 TYR B OH  1 
ATOM   3053 N N   . ILE B 2 177 ? 52.174 -13.117 25.346  1.00 16.47 ? 177 ILE B N   1 
ATOM   3054 C CA  . ILE B 2 177 ? 52.842 -14.393 25.111  1.00 14.41 ? 177 ILE B CA  1 
ATOM   3055 C C   . ILE B 2 177 ? 53.381 -14.380 23.690  1.00 13.74 ? 177 ILE B C   1 
ATOM   3056 O O   . ILE B 2 177 ? 52.711 -13.920 22.756  1.00 13.70 ? 177 ILE B O   1 
ATOM   3057 C CB  . ILE B 2 177 ? 51.878 -15.574 25.338  1.00 14.25 ? 177 ILE B CB  1 
ATOM   3058 C CG1 . ILE B 2 177 ? 51.528 -15.693 26.813  1.00 15.53 ? 177 ILE B CG1 1 
ATOM   3059 C CG2 . ILE B 2 177 ? 52.488 -16.899 24.882  1.00 14.37 ? 177 ILE B CG2 1 
ATOM   3060 C CD1 . ILE B 2 177 ? 50.572 -16.856 27.140  1.00 15.24 ? 177 ILE B CD1 1 
ATOM   3061 N N   . TYR B 2 178 ? 54.598 -14.877 23.522  1.00 12.94 ? 178 TYR B N   1 
ATOM   3062 C CA  . TYR B 2 178 ? 55.303 -14.832 22.249  1.00 13.22 ? 178 TYR B CA  1 
ATOM   3063 C C   . TYR B 2 178 ? 55.255 -16.214 21.587  1.00 12.98 ? 178 TYR B C   1 
ATOM   3064 O O   . TYR B 2 178 ? 55.855 -17.170 22.116  1.00 13.91 ? 178 TYR B O   1 
ATOM   3065 C CB  . TYR B 2 178 ? 56.754 -14.401 22.524  1.00 13.39 ? 178 TYR B CB  1 
ATOM   3066 C CG  . TYR B 2 178 ? 57.617 -14.179 21.340  1.00 13.20 ? 178 TYR B CG  1 
ATOM   3067 C CD1 . TYR B 2 178 ? 57.128 -13.561 20.195  1.00 12.21 ? 178 TYR B CD1 1 
ATOM   3068 C CD2 . TYR B 2 178 ? 58.950 -14.566 21.364  1.00 13.59 ? 178 TYR B CD2 1 
ATOM   3069 C CE1 . TYR B 2 178 ? 57.948 -13.357 19.084  1.00 15.77 ? 178 TYR B CE1 1 
ATOM   3070 C CE2 . TYR B 2 178 ? 59.774 -14.355 20.268  1.00 12.56 ? 178 TYR B CE2 1 
ATOM   3071 C CZ  . TYR B 2 178 ? 59.290 -13.755 19.132  1.00 14.42 ? 178 TYR B CZ  1 
ATOM   3072 O OH  . TYR B 2 178 ? 60.121 -13.557 18.040  1.00 14.61 ? 178 TYR B OH  1 
ATOM   3073 N N   . PRO B 2 179 ? 54.560 -16.378 20.461  1.00 13.28 ? 179 PRO B N   1 
ATOM   3074 C CA  . PRO B 2 179 ? 54.486 -17.713 19.828  1.00 13.12 ? 179 PRO B CA  1 
ATOM   3075 C C   . PRO B 2 179 ? 55.831 -18.384 19.621  1.00 14.03 ? 179 PRO B C   1 
ATOM   3076 O O   . PRO B 2 179 ? 55.957 -19.588 19.859  1.00 14.04 ? 179 PRO B O   1 
ATOM   3077 C CB  . PRO B 2 179 ? 53.823 -17.408 18.476  1.00 13.20 ? 179 PRO B CB  1 
ATOM   3078 C CG  . PRO B 2 179 ? 52.944 -16.231 18.788  1.00 13.68 ? 179 PRO B CG  1 
ATOM   3079 C CD  . PRO B 2 179 ? 53.817 -15.374 19.673  1.00 13.85 ? 179 PRO B CD  1 
ATOM   3080 N N   . ASP B 2 180 ? 56.844 -17.637 19.181  1.00 15.28 ? 180 ASP B N   1 
ATOM   3081 C CA  . ASP B 2 180 ? 58.117 -18.227 18.758  1.00 14.55 ? 180 ASP B CA  1 
ATOM   3082 C C   . ASP B 2 180 ? 58.872 -18.894 19.898  1.00 14.70 ? 180 ASP B C   1 
ATOM   3083 O O   . ASP B 2 180 ? 59.724 -19.752 19.647  1.00 14.79 ? 180 ASP B O   1 
ATOM   3084 C CB  . ASP B 2 180 ? 59.007 -17.170 18.107  1.00 13.31 ? 180 ASP B CB  1 
ATOM   3085 C CG  . ASP B 2 180 ? 58.331 -16.500 16.967  1.00 12.69 ? 180 ASP B CG  1 
ATOM   3086 O OD1 . ASP B 2 180 ? 57.128 -16.223 17.089  1.00 14.05 ? 180 ASP B OD1 1 
ATOM   3087 O OD2 . ASP B 2 180 ? 58.984 -16.297 15.925  1.00 15.01 ? 180 ASP B OD2 1 
ATOM   3088 N N   . THR B 2 181 ? 58.618 -18.501 21.136  1.00 13.97 ? 181 THR B N   1 
ATOM   3089 C CA  . THR B 2 181 ? 59.105 -19.318 22.230  1.00 14.35 ? 181 THR B CA  1 
ATOM   3090 C C   . THR B 2 181 ? 58.012 -20.254 22.750  1.00 14.73 ? 181 THR B C   1 
ATOM   3091 O O   . THR B 2 181 ? 58.255 -21.457 22.896  1.00 14.54 ? 181 THR B O   1 
ATOM   3092 C CB  . THR B 2 181 ? 59.744 -18.450 23.349  1.00 15.57 ? 181 THR B CB  1 
ATOM   3093 O OG1 . THR B 2 181 ? 58.844 -17.403 23.796  1.00 13.71 ? 181 THR B OG1 1 
ATOM   3094 C CG2 . THR B 2 181 ? 61.070 -17.847 22.859  1.00 13.04 ? 181 THR B CG2 1 
ATOM   3095 N N   . ALA B 2 182 ? 56.791 -19.740 22.952  1.00 13.29 ? 182 ALA B N   1 
ATOM   3096 C CA  . ALA B 2 182 ? 55.750 -20.525 23.609  1.00 13.80 ? 182 ALA B CA  1 
ATOM   3097 C C   . ALA B 2 182 ? 55.446 -21.792 22.831  1.00 13.98 ? 182 ALA B C   1 
ATOM   3098 O O   . ALA B 2 182 ? 55.440 -22.887 23.404  1.00 14.10 ? 182 ALA B O   1 
ATOM   3099 C CB  . ALA B 2 182 ? 54.482 -19.697 23.758  1.00 14.51 ? 182 ALA B CB  1 
ATOM   3100 N N   . GLY B 2 183 ? 55.169 -21.660 21.531  1.00 13.67 ? 183 GLY B N   1 
ATOM   3101 C CA  . GLY B 2 183 ? 54.836 -22.796 20.679  1.00 13.77 ? 183 GLY B CA  1 
ATOM   3102 C C   . GLY B 2 183 ? 55.933 -23.847 20.578  1.00 15.38 ? 183 GLY B C   1 
ATOM   3103 O O   . GLY B 2 183 ? 55.677 -24.952 20.072  1.00 15.29 ? 183 GLY B O   1 
ATOM   3104 N N   . ASN B 2 184 ? 57.144 -23.537 21.057  1.00 15.44 ? 184 ASN B N   1 
ATOM   3105 C CA  . ASN B 2 184 ? 58.285 -24.435 20.930  1.00 14.82 ? 184 ASN B CA  1 
ATOM   3106 C C   . ASN B 2 184 ? 58.765 -24.957 22.283  1.00 14.95 ? 184 ASN B C   1 
ATOM   3107 O O   . ASN B 2 184 ? 59.858 -25.527 22.361  1.00 16.02 ? 184 ASN B O   1 
ATOM   3108 C CB  . ASN B 2 184 ? 59.383 -23.752 20.112  1.00 13.53 ? 184 ASN B CB  1 
ATOM   3109 C CG  . ASN B 2 184 ? 58.943 -23.482 18.679  1.00 14.61 ? 184 ASN B CG  1 
ATOM   3110 O OD1 . ASN B 2 184 ? 58.690 -24.401 17.928  1.00 15.65 ? 184 ASN B OD1 1 
ATOM   3111 N ND2 . ASN B 2 184 ? 58.782 -22.210 18.315  1.00 15.31 ? 184 ASN B ND2 1 
ATOM   3112 N N   . GLY B 2 185 ? 57.965 -24.795 23.341  1.00 13.63 ? 185 GLY B N   1 
ATOM   3113 C CA  . GLY B 2 185 ? 58.292 -25.281 24.666  1.00 13.24 ? 185 GLY B CA  1 
ATOM   3114 C C   . GLY B 2 185 ? 59.250 -24.418 25.455  1.00 13.82 ? 185 GLY B C   1 
ATOM   3115 O O   . GLY B 2 185 ? 59.839 -24.899 26.412  1.00 15.20 ? 185 GLY B O   1 
ATOM   3116 N N   . LEU B 2 186 ? 59.419 -23.151 25.082  1.00 14.31 ? 186 LEU B N   1 
ATOM   3117 C CA  . LEU B 2 186 ? 60.494 -22.303 25.572  1.00 12.30 ? 186 LEU B CA  1 
ATOM   3118 C C   . LEU B 2 186 ? 59.975 -21.155 26.402  1.00 14.09 ? 186 LEU B C   1 
ATOM   3119 O O   . LEU B 2 186 ? 60.715 -20.188 26.636  1.00 14.85 ? 186 LEU B O   1 
ATOM   3120 C CB  . LEU B 2 186 ? 61.327 -21.770 24.408  1.00 14.33 ? 186 LEU B CB  1 
ATOM   3121 C CG  . LEU B 2 186 ? 62.003 -22.830 23.524  1.00 15.39 ? 186 LEU B CG  1 
ATOM   3122 C CD1 . LEU B 2 186 ? 62.597 -22.262 22.227  1.00 15.14 ? 186 LEU B CD1 1 
ATOM   3123 C CD2 . LEU B 2 186 ? 63.091 -23.538 24.353  1.00 17.53 ? 186 LEU B CD2 1 
ATOM   3124 N N   . GLY B 2 187 ? 58.712 -21.241 26.861  1.00 15.57 ? 187 GLY B N   1 
ATOM   3125 C CA  . GLY B 2 187 ? 58.155 -20.279 27.798  1.00 14.15 ? 187 GLY B CA  1 
ATOM   3126 C C   . GLY B 2 187 ? 57.465 -19.103 27.120  1.00 13.70 ? 187 GLY B C   1 
ATOM   3127 O O   . GLY B 2 187 ? 57.443 -18.946 25.893  1.00 13.37 ? 187 GLY B O   1 
ATOM   3128 N N   . GLU B 2 188 ? 56.898 -18.241 27.967  1.00 14.20 ? 188 GLU B N   1 
ATOM   3129 C CA  . GLU B 2 188 ? 56.059 -17.153 27.450  1.00 16.66 ? 188 GLU B CA  1 
ATOM   3130 C C   . GLU B 2 188 ? 56.895 -16.048 26.799  1.00 14.05 ? 188 GLU B C   1 
ATOM   3131 O O   . GLU B 2 188 ? 56.524 -15.524 25.733  1.00 11.81 ? 188 GLU B O   1 
ATOM   3132 C CB  . GLU B 2 188 ? 55.173 -16.588 28.575  1.00 14.81 ? 188 GLU B CB  1 
ATOM   3133 C CG  . GLU B 2 188 ? 54.186 -17.586 29.145  1.00 14.30 ? 188 GLU B CG  1 
ATOM   3134 C CD  . GLU B 2 188 ? 53.309 -16.969 30.178  1.00 16.17 ? 188 GLU B CD  1 
ATOM   3135 O OE1 . GLU B 2 188 ? 53.596 -15.828 30.582  1.00 17.40 ? 188 GLU B OE1 1 
ATOM   3136 O OE2 . GLU B 2 188 ? 52.336 -17.627 30.624  1.00 16.69 ? 188 GLU B OE2 1 
ATOM   3137 N N   . CYS B 2 189 ? 58.018 -15.654 27.468  1.00 15.42 ? 189 CYS B N   1 
ATOM   3138 C CA  . CYS B 2 189 ? 58.939 -14.606 27.040  1.00 13.84 ? 189 CYS B CA  1 
ATOM   3139 C C   . CYS B 2 189 ? 58.169 -13.503 26.342  1.00 14.68 ? 189 CYS B C   1 
ATOM   3140 O O   . CYS B 2 189 ? 58.383 -13.278 25.148  1.00 13.98 ? 189 CYS B O   1 
ATOM   3141 C CB  . CYS B 2 189 ? 59.971 -15.195 26.086  1.00 14.56 ? 189 CYS B CB  1 
ATOM   3142 S SG  . CYS B 2 189 ? 60.740 -16.715 26.798  1.00 18.00 ? 189 CYS B SG  1 
ATOM   3143 N N   . PRO B 2 190 ? 57.282 -12.789 27.055  1.00 15.99 ? 190 PRO B N   1 
ATOM   3144 C CA  . PRO B 2 190 ? 56.310 -11.925 26.371  1.00 15.57 ? 190 PRO B CA  1 
ATOM   3145 C C   . PRO B 2 190 ? 56.985 -10.773 25.640  1.00 14.54 ? 190 PRO B C   1 
ATOM   3146 O O   . PRO B 2 190 ? 58.041 -10.273 26.040  1.00 15.48 ? 190 PRO B O   1 
ATOM   3147 C CB  . PRO B 2 190 ? 55.435 -11.414 27.520  1.00 15.95 ? 190 PRO B CB  1 
ATOM   3148 C CG  . PRO B 2 190 ? 55.592 -12.479 28.601  1.00 17.98 ? 190 PRO B CG  1 
ATOM   3149 C CD  . PRO B 2 190 ? 57.040 -12.814 28.512  1.00 15.13 ? 190 PRO B CD  1 
ATOM   3150 N N   . GLU B 2 191 ? 56.341 -10.357 24.559  1.00 13.03 ? 191 GLU B N   1 
ATOM   3151 C CA  . GLU B 2 191 ? 56.833 -9.306  23.697  1.00 14.96 ? 191 GLU B CA  1 
ATOM   3152 C C   . GLU B 2 191 ? 55.678 -8.371  23.372  1.00 16.68 ? 191 GLU B C   1 
ATOM   3153 O O   . GLU B 2 191 ? 54.513 -8.791  23.322  1.00 14.51 ? 191 GLU B O   1 
ATOM   3154 C CB  . GLU B 2 191 ? 57.388 -9.879  22.368  1.00 15.85 ? 191 GLU B CB  1 
ATOM   3155 C CG  . GLU B 2 191 ? 58.666 -10.679 22.534  1.00 16.31 ? 191 GLU B CG  1 
ATOM   3156 C CD  . GLU B 2 191 ? 59.897 -9.803  22.572  1.00 17.17 ? 191 GLU B CD  1 
ATOM   3157 O OE1 . GLU B 2 191 ? 59.803 -8.629  22.149  1.00 16.41 ? 191 GLU B OE1 1 
ATOM   3158 O OE2 . GLU B 2 191 ? 60.945 -10.280 23.058  1.00 18.21 ? 191 GLU B OE2 1 
ATOM   3159 N N   . HIS B 2 192 ? 56.020 -7.105  23.117  1.00 15.25 ? 192 HIS B N   1 
ATOM   3160 C CA  . HIS B 2 192 ? 55.020 -6.142  22.701  1.00 14.53 ? 192 HIS B CA  1 
ATOM   3161 C C   . HIS B 2 192 ? 54.382 -6.560  21.378  1.00 14.47 ? 192 HIS B C   1 
ATOM   3162 O O   . HIS B 2 192 ? 55.032 -7.140  20.502  1.00 14.38 ? 192 HIS B O   1 
ATOM   3163 C CB  . HIS B 2 192 ? 55.654 -4.749  22.623  1.00 16.04 ? 192 HIS B CB  1 
ATOM   3164 C CG  . HIS B 2 192 ? 55.926 -4.157  23.970  1.00 16.88 ? 192 HIS B CG  1 
ATOM   3165 N ND1 . HIS B 2 192 ? 54.912 -3.785  24.838  1.00 15.45 ? 192 HIS B ND1 1 
ATOM   3166 C CD2 . HIS B 2 192 ? 57.092 -3.911  24.618  1.00 16.92 ? 192 HIS B CD2 1 
ATOM   3167 C CE1 . HIS B 2 192 ? 55.442 -3.328  25.959  1.00 18.30 ? 192 HIS B CE1 1 
ATOM   3168 N NE2 . HIS B 2 192 ? 56.763 -3.389  25.850  1.00 20.47 ? 192 HIS B NE2 1 
ATOM   3169 N N   . LEU B 2 193 ? 53.089 -6.275  21.244  1.00 13.66 ? 193 LEU B N   1 
ATOM   3170 C CA  . LEU B 2 193 ? 52.311 -6.681  20.095  1.00 13.84 ? 193 LEU B CA  1 
ATOM   3171 C C   . LEU B 2 193 ? 51.748 -5.442  19.397  1.00 14.31 ? 193 LEU B C   1 
ATOM   3172 O O   . LEU B 2 193 ? 51.256 -4.512  20.050  1.00 14.51 ? 193 LEU B O   1 
ATOM   3173 C CB  . LEU B 2 193 ? 51.170 -7.609  20.540  1.00 13.14 ? 193 LEU B CB  1 
ATOM   3174 C CG  . LEU B 2 193 ? 50.329 -8.268  19.433  1.00 14.54 ? 193 LEU B CG  1 
ATOM   3175 C CD1 . LEU B 2 193 ? 51.119 -9.328  18.666  1.00 13.98 ? 193 LEU B CD1 1 
ATOM   3176 C CD2 . LEU B 2 193 ? 49.016 -8.825  19.978  1.00 13.50 ? 193 LEU B CD2 1 
ATOM   3177 N N   . TYR B 2 194 ? 51.797 -5.446  18.068  1.00 13.73 ? 194 TYR B N   1 
ATOM   3178 C CA  . TYR B 2 194 ? 51.336 -4.336  17.254  1.00 13.75 ? 194 TYR B CA  1 
ATOM   3179 C C   . TYR B 2 194 ? 50.546 -4.880  16.077  1.00 14.21 ? 194 TYR B C   1 
ATOM   3180 O O   . TYR B 2 194 ? 50.872 -5.933  15.528  1.00 15.35 ? 194 TYR B O   1 
ATOM   3181 C CB  . TYR B 2 194 ? 52.524 -3.570  16.651  1.00 15.03 ? 194 TYR B CB  1 
ATOM   3182 C CG  . TYR B 2 194 ? 53.606 -3.147  17.641  1.00 15.75 ? 194 TYR B CG  1 
ATOM   3183 C CD1 . TYR B 2 194 ? 54.673 -4.004  17.958  1.00 15.80 ? 194 TYR B CD1 1 
ATOM   3184 C CD2 . TYR B 2 194 ? 53.577 -1.890  18.239  1.00 13.90 ? 194 TYR B CD2 1 
ATOM   3185 C CE1 . TYR B 2 194 ? 55.662 -3.613  18.854  1.00 14.76 ? 194 TYR B CE1 1 
ATOM   3186 C CE2 . TYR B 2 194 ? 54.551 -1.503  19.126  1.00 16.16 ? 194 TYR B CE2 1 
ATOM   3187 C CZ  . TYR B 2 194 ? 55.597 -2.352  19.429  1.00 14.92 ? 194 TYR B CZ  1 
ATOM   3188 O OH  . TYR B 2 194 ? 56.557 -1.935  20.309  1.00 12.69 ? 194 TYR B OH  1 
ATOM   3189 N N   . THR B 2 195 ? 49.529 -4.136  15.665  1.00 14.73 ? 195 THR B N   1 
ATOM   3190 C CA  . THR B 2 195 ? 48.945 -4.325  14.351  1.00 14.55 ? 195 THR B CA  1 
ATOM   3191 C C   . THR B 2 195 ? 49.738 -3.486  13.354  1.00 15.48 ? 195 THR B C   1 
ATOM   3192 O O   . THR B 2 195 ? 50.182 -2.366  13.668  1.00 15.73 ? 195 THR B O   1 
ATOM   3193 C CB  . THR B 2 195 ? 47.470 -3.899  14.329  1.00 14.81 ? 195 THR B CB  1 
ATOM   3194 O OG1 . THR B 2 195 ? 46.704 -4.800  15.131  1.00 14.76 ? 195 THR B OG1 1 
ATOM   3195 C CG2 . THR B 2 195 ? 46.928 -3.933  12.914  1.00 14.02 ? 195 THR B CG2 1 
ATOM   3196 N N   . VAL B 2 196 ? 49.902 -4.032  12.152  1.00 15.12 ? 196 VAL B N   1 
ATOM   3197 C CA  . VAL B 2 196 ? 50.654 -3.414  11.072  1.00 14.56 ? 196 VAL B CA  1 
ATOM   3198 C C   . VAL B 2 196 ? 49.792 -3.477  9.818   1.00 16.53 ? 196 VAL B C   1 
ATOM   3199 O O   . VAL B 2 196 ? 49.111 -4.480  9.567   1.00 15.70 ? 196 VAL B O   1 
ATOM   3200 C CB  . VAL B 2 196 ? 52.027 -4.113  10.889  1.00 14.56 ? 196 VAL B CB  1 
ATOM   3201 C CG1 . VAL B 2 196 ? 52.780 -3.534  9.716   1.00 17.47 ? 196 VAL B CG1 1 
ATOM   3202 C CG2 . VAL B 2 196 ? 52.878 -3.966  12.150  1.00 13.48 ? 196 VAL B CG2 1 
ATOM   3203 N N   . ARG B 2 197 ? 49.794 -2.391  9.048   1.00 15.51 ? 197 ARG B N   1 
ATOM   3204 C CA  . ARG B 2 197 ? 48.985 -2.273  7.846   1.00 18.07 ? 197 ARG B CA  1 
ATOM   3205 C C   . ARG B 2 197 ? 49.895 -2.400  6.620   1.00 18.98 ? 197 ARG B C   1 
ATOM   3206 O O   . ARG B 2 197 ? 50.907 -1.685  6.506   1.00 16.55 ? 197 ARG B O   1 
ATOM   3207 C CB  . ARG B 2 197 ? 48.184 -0.951  7.827   1.00 19.10 ? 197 ARG B CB  1 
ATOM   3208 C CG  . ARG B 2 197 ? 47.586 -0.573  6.445   1.00 19.69 ? 197 ARG B CG  1 
ATOM   3209 C CD  . ARG B 2 197 ? 47.080 0.893   6.375   1.00 25.89 ? 197 ARG B CD  1 
ATOM   3210 N NE  . ARG B 2 197 ? 45.984 1.087   5.411   1.00 33.66 ? 197 ARG B NE  1 
ATOM   3211 C CZ  . ARG B 2 197 ? 45.383 2.252   5.150   1.00 36.17 ? 197 ARG B CZ  1 
ATOM   3212 N NH1 . ARG B 2 197 ? 45.757 3.383   5.745   1.00 39.05 ? 197 ARG B NH1 1 
ATOM   3213 N NH2 . ARG B 2 197 ? 44.385 2.286   4.266   1.00 29.42 ? 197 ARG B NH2 1 
ATOM   3214 N N   . PHE B 2 198 ? 49.540 -3.314  5.713   1.00 14.96 ? 198 PHE B N   1 
ATOM   3215 C CA  . PHE B 2 198 ? 50.255 -3.520  4.459   1.00 16.72 ? 198 PHE B CA  1 
ATOM   3216 C C   . PHE B 2 198 ? 49.291 -3.294  3.298   1.00 16.73 ? 198 PHE B C   1 
ATOM   3217 O O   . PHE B 2 198 ? 48.196 -3.861  3.271   1.00 17.78 ? 198 PHE B O   1 
ATOM   3218 C CB  . PHE B 2 198 ? 50.830 -4.936  4.404   1.00 16.03 ? 198 PHE B CB  1 
ATOM   3219 C CG  . PHE B 2 198 ? 51.777 -5.249  5.529   1.00 15.58 ? 198 PHE B CG  1 
ATOM   3220 C CD1 . PHE B 2 198 ? 53.143 -4.989  5.402   1.00 15.70 ? 198 PHE B CD1 1 
ATOM   3221 C CD2 . PHE B 2 198 ? 51.306 -5.818  6.715   1.00 16.33 ? 198 PHE B CD2 1 
ATOM   3222 C CE1 . PHE B 2 198 ? 54.033 -5.285  6.457   1.00 17.26 ? 198 PHE B CE1 1 
ATOM   3223 C CE2 . PHE B 2 198 ? 52.185 -6.116  7.778   1.00 16.40 ? 198 PHE B CE2 1 
ATOM   3224 C CZ  . PHE B 2 198 ? 53.552 -5.853  7.650   1.00 16.27 ? 198 PHE B CZ  1 
ATOM   3225 N N   . THR B 2 199 ? 49.660 -2.433  2.362   1.00 16.73 ? 199 THR B N   1 
ATOM   3226 C CA  . THR B 2 199 ? 48.772 -2.229  1.239   1.00 16.33 ? 199 THR B CA  1 
ATOM   3227 C C   . THR B 2 199 ? 48.759 -3.505  0.413   1.00 19.21 ? 199 THR B C   1 
ATOM   3228 O O   . THR B 2 199 ? 49.712 -4.292  0.445   1.00 17.58 ? 199 THR B O   1 
ATOM   3229 C CB  . THR B 2 199 ? 49.245 -1.060  0.386   1.00 18.21 ? 199 THR B CB  1 
ATOM   3230 O OG1 . THR B 2 199 ? 50.471 -1.424  -0.289  1.00 18.69 ? 199 THR B OG1 1 
ATOM   3231 C CG2 . THR B 2 199 ? 49.444 0.191   1.265   1.00 13.53 ? 199 THR B CG2 1 
ATOM   3232 N N   . ALA B 2 200 ? 47.658 -3.717  -0.327  1.00 18.62 ? 200 ALA B N   1 
ATOM   3233 C CA  . ALA B 2 200 ? 47.611 -4.881  -1.206  1.00 19.39 ? 200 ALA B CA  1 
ATOM   3234 C C   . ALA B 2 200 ? 48.682 -4.797  -2.296  1.00 19.43 ? 200 ALA B C   1 
ATOM   3235 O O   . ALA B 2 200 ? 49.183 -5.825  -2.760  1.00 18.64 ? 200 ALA B O   1 
ATOM   3236 C CB  . ALA B 2 200 ? 46.203 -5.072  -1.783  1.00 20.27 ? 200 ALA B CB  1 
ATOM   3237 N N   . GLN B 2 201 ? 49.060 -3.592  -2.716  1.00 19.18 ? 201 GLN B N   1 
ATOM   3238 C CA  . GLN B 2 201 ? 50.077 -3.512  -3.761  1.00 21.90 ? 201 GLN B CA  1 
ATOM   3239 C C   . GLN B 2 201 ? 51.461 -3.824  -3.210  1.00 18.27 ? 201 GLN B C   1 
ATOM   3240 O O   . GLN B 2 201 ? 52.313 -4.349  -3.938  1.00 17.37 ? 201 GLN B O   1 
ATOM   3241 C CB  . GLN B 2 201 ? 50.072 -2.125  -4.398  1.00 24.08 ? 201 GLN B CB  1 
ATOM   3242 C CG  . GLN B 2 201 ? 48.669 -1.593  -4.630  1.00 27.35 ? 201 GLN B CG  1 
ATOM   3243 C CD  . GLN B 2 201 ? 48.098 -2.095  -5.906  1.00 30.75 ? 201 GLN B CD  1 
ATOM   3244 O OE1 . GLN B 2 201 ? 47.974 -3.308  -6.081  1.00 31.18 ? 201 GLN B OE1 1 
ATOM   3245 N NE2 . GLN B 2 201 ? 47.716 -1.174  -6.814  1.00 33.01 ? 201 GLN B NE2 1 
ATOM   3246 N N   . GLU B 2 202 ? 51.710 -3.479  -1.944  1.00 17.94 ? 202 GLU B N   1 
ATOM   3247 C CA  . GLU B 2 202 ? 52.910 -3.962  -1.278  1.00 16.03 ? 202 GLU B CA  1 
ATOM   3248 C C   . GLU B 2 202 ? 52.925 -5.495  -1.252  1.00 17.74 ? 202 GLU B C   1 
ATOM   3249 O O   . GLU B 2 202 ? 53.970 -6.127  -1.503  1.00 15.36 ? 202 GLU B O   1 
ATOM   3250 C CB  . GLU B 2 202 ? 53.011 -3.355  0.120   1.00 13.75 ? 202 GLU B CB  1 
ATOM   3251 C CG  . GLU B 2 202 ? 54.117 -3.909  0.995   1.00 13.73 ? 202 GLU B CG  1 
ATOM   3252 C CD  . GLU B 2 202 ? 55.513 -3.548  0.480   1.00 15.76 ? 202 GLU B CD  1 
ATOM   3253 O OE1 . GLU B 2 202 ? 55.625 -2.643  -0.358  1.00 15.26 ? 202 GLU B OE1 1 
ATOM   3254 O OE2 . GLU B 2 202 ? 56.509 -4.174  0.911   1.00 16.46 ? 202 GLU B OE2 1 
ATOM   3255 N N   . LEU B 2 203 ? 51.751 -6.112  -1.014  1.00 16.21 ? 203 LEU B N   1 
ATOM   3256 C CA  . LEU B 2 203 ? 51.687 -7.558  -0.833  1.00 15.45 ? 203 LEU B CA  1 
ATOM   3257 C C   . LEU B 2 203 ? 51.766 -8.313  -2.160  1.00 15.16 ? 203 LEU B C   1 
ATOM   3258 O O   . LEU B 2 203 ? 52.532 -9.279  -2.288  1.00 16.81 ? 203 LEU B O   1 
ATOM   3259 C CB  . LEU B 2 203 ? 50.450 -7.929  -0.021  1.00 14.72 ? 203 LEU B CB  1 
ATOM   3260 C CG  . LEU B 2 203 ? 50.451 -7.338  1.387   1.00 15.06 ? 203 LEU B CG  1 
ATOM   3261 C CD1 . LEU B 2 203 ? 49.156 -7.697  2.105   1.00 17.94 ? 203 LEU B CD1 1 
ATOM   3262 C CD2 . LEU B 2 203 ? 51.656 -7.815  2.193   1.00 14.79 ? 203 LEU B CD2 1 
ATOM   3263 N N   . TRP B 2 204 ? 51.007 -7.886  -3.163  1.00 15.19 ? 204 TRP B N   1 
ATOM   3264 C CA  . TRP B 2 204 ? 50.750 -8.708  -4.339  1.00 17.11 ? 204 TRP B CA  1 
ATOM   3265 C C   . TRP B 2 204 ? 51.332 -8.121  -5.613  1.00 18.46 ? 204 TRP B C   1 
ATOM   3266 O O   . TRP B 2 204 ? 51.139 -8.693  -6.690  1.00 18.92 ? 204 TRP B O   1 
ATOM   3267 C CB  . TRP B 2 204 ? 49.230 -8.953  -4.491  1.00 17.45 ? 204 TRP B CB  1 
ATOM   3268 C CG  . TRP B 2 204 ? 48.572 -9.270  -3.149  1.00 18.21 ? 204 TRP B CG  1 
ATOM   3269 C CD1 . TRP B 2 204 ? 47.659 -8.494  -2.457  1.00 16.39 ? 204 TRP B CD1 1 
ATOM   3270 C CD2 . TRP B 2 204 ? 48.780 -10.442 -2.350  1.00 16.73 ? 204 TRP B CD2 1 
ATOM   3271 N NE1 . TRP B 2 204 ? 47.312 -9.111  -1.277  1.00 15.47 ? 204 TRP B NE1 1 
ATOM   3272 C CE2 . TRP B 2 204 ? 47.981 -10.303 -1.181  1.00 15.77 ? 204 TRP B CE2 1 
ATOM   3273 C CE3 . TRP B 2 204 ? 49.565 -11.586 -2.504  1.00 15.79 ? 204 TRP B CE3 1 
ATOM   3274 C CZ2 . TRP B 2 204 ? 47.947 -11.266 -0.175  1.00 16.17 ? 204 TRP B CZ2 1 
ATOM   3275 C CZ3 . TRP B 2 204 ? 49.536 -12.543 -1.498  1.00 16.97 ? 204 TRP B CZ3 1 
ATOM   3276 C CH2 . TRP B 2 204 ? 48.723 -12.377 -0.345  1.00 15.81 ? 204 TRP B CH2 1 
ATOM   3277 N N   . GLY B 2 205 ? 52.044 -7.001  -5.526  1.00 18.15 ? 205 GLY B N   1 
ATOM   3278 C CA  . GLY B 2 205 ? 52.600 -6.372  -6.699  1.00 18.92 ? 205 GLY B CA  1 
ATOM   3279 C C   . GLY B 2 205 ? 51.553 -5.576  -7.449  1.00 22.40 ? 205 GLY B C   1 
ATOM   3280 O O   . GLY B 2 205 ? 50.726 -4.867  -6.864  1.00 23.95 ? 205 GLY B O   1 
ATOM   3281 N N   . PRO B 2 206 ? 51.571 -5.687  -8.775  1.00 26.33 ? 206 PRO B N   1 
ATOM   3282 C CA  . PRO B 2 206 ? 50.497 -5.079  -9.585  1.00 26.29 ? 206 PRO B CA  1 
ATOM   3283 C C   . PRO B 2 206 ? 49.166 -5.824  -9.487  1.00 29.43 ? 206 PRO B C   1 
ATOM   3284 O O   . PRO B 2 206 ? 48.125 -5.228  -9.808  1.00 29.49 ? 206 PRO B O   1 
ATOM   3285 C CB  . PRO B 2 206 ? 51.049 -5.173  -11.011 1.00 30.26 ? 206 PRO B CB  1 
ATOM   3286 C CG  . PRO B 2 206 ? 51.969 -6.406  -10.949 1.00 26.13 ? 206 PRO B CG  1 
ATOM   3287 C CD  . PRO B 2 206 ? 52.592 -6.371  -9.593  1.00 23.63 ? 206 PRO B CD  1 
ATOM   3288 N N   . GLU B 2 207 ? 49.168 -7.109  -9.079  1.00 26.17 ? 207 GLU B N   1 
ATOM   3289 C CA  . GLU B 2 207 ? 47.942 -7.897  -9.001  1.00 25.69 ? 207 GLU B CA  1 
ATOM   3290 C C   . GLU B 2 207 ? 47.078 -7.539  -7.806  1.00 28.13 ? 207 GLU B C   1 
ATOM   3291 O O   . GLU B 2 207 ? 46.000 -8.126  -7.652  1.00 28.20 ? 207 GLU B O   1 
ATOM   3292 C CB  . GLU B 2 207 ? 48.245 -9.398  -8.963  1.00 25.01 ? 207 GLU B CB  1 
ATOM   3293 C CG  . GLU B 2 207 ? 48.600 -10.041 -10.301 1.00 24.55 ? 207 GLU B CG  1 
ATOM   3294 C CD  . GLU B 2 207 ? 50.034 -9.787  -10.738 1.00 22.53 ? 207 GLU B CD  1 
ATOM   3295 O OE1 . GLU B 2 207 ? 50.801 -9.171  -9.965  1.00 22.51 ? 207 GLU B OE1 1 
ATOM   3296 O OE2 . GLU B 2 207 ? 50.399 -10.275 -11.841 1.00 24.35 ? 207 GLU B OE2 1 
ATOM   3297 N N   . GLY B 2 208 ? 47.518 -6.597  -6.961  1.00 28.96 ? 208 GLY B N   1 
ATOM   3298 C CA  . GLY B 2 208 ? 46.763 -6.229  -5.765  1.00 29.35 ? 208 GLY B CA  1 
ATOM   3299 C C   . GLY B 2 208 ? 45.727 -5.131  -6.001  1.00 30.37 ? 208 GLY B C   1 
ATOM   3300 O O   . GLY B 2 208 ? 45.865 -4.287  -6.879  1.00 28.61 ? 208 GLY B O   1 
ATOM   3301 N N   . ASP B 2 209 ? 44.683 -5.139  -5.197  1.00 31.12 ? 209 ASP B N   1 
ATOM   3302 C CA  . ASP B 2 209 ? 43.595 -4.068  -5.402  1.00 27.22 ? 209 ASP B CA  1 
ATOM   3303 C C   . ASP B 2 209 ? 44.022 -2.530  -5.156  1.00 25.61 ? 209 ASP B C   1 
ATOM   3304 O O   . ASP B 2 209 ? 44.645 -2.538  -3.946  1.00 23.24 ? 209 ASP B O   1 
ATOM   3305 C CB  . ASP B 2 209 ? 42.493 -4.549  -4.372  1.00 28.09 ? 209 ASP B CB  1 
ATOM   3306 C CG  . ASP B 2 209 ? 41.247 -3.714  -4.534  1.00 28.47 ? 209 ASP B CG  1 
ATOM   3307 O OD1 . ASP B 2 209 ? 41.354 -2.484  -4.333  1.00 27.46 ? 209 ASP B OD1 1 
ATOM   3308 O OD2 . ASP B 2 209 ? 40.172 -4.272  -4.875  1.00 29.61 ? 209 ASP B OD2 1 
ATOM   3309 N N   . PRO B 2 210 ? 43.846 -1.315  -5.919  1.00 32.09 ? 210 PRO B N   1 
ATOM   3310 C CA  . PRO B 2 210 ? 44.682 -0.380  -5.578  1.00 29.49 ? 210 PRO B CA  1 
ATOM   3311 C C   . PRO B 2 210 ? 44.083 0.225   -4.303  1.00 29.71 ? 210 PRO B C   1 
ATOM   3312 O O   . PRO B 2 210 ? 44.627 1.193   -3.781  1.00 27.43 ? 210 PRO B O   1 
ATOM   3313 C CB  . PRO B 2 210 ? 44.478 0.365   -6.702  1.00 31.00 ? 210 PRO B CB  1 
ATOM   3314 C CG  . PRO B 2 210 ? 42.716 -0.442  -6.957  1.00 33.35 ? 210 PRO B CG  1 
ATOM   3315 C CD  . PRO B 2 210 ? 43.324 -0.163  -6.869  1.00 33.22 ? 210 PRO B CD  1 
ATOM   3316 N N   . ASN B 2 211 ? 42.913 -0.282  -3.844  1.00 27.95 ? 211 ASN B N   1 
ATOM   3317 C CA  . ASN B 2 211 ? 42.101 0.336   -2.800  1.00 25.68 ? 211 ASN B CA  1 
ATOM   3318 C C   . ASN B 2 211 ? 41.793 -0.672  -1.702  1.00 24.99 ? 211 ASN B C   1 
ATOM   3319 O O   . ASN B 2 211 ? 40.646 -0.843  -1.277  1.00 22.17 ? 211 ASN B O   1 
ATOM   3320 C CB  . ASN B 2 211 ? 40.811 0.882   -3.398  1.00 23.76 ? 211 ASN B CB  1 
ATOM   3321 C CG  . ASN B 2 211 ? 40.147 1.869   -2.510  1.00 25.91 ? 211 ASN B CG  1 
ATOM   3322 O OD1 . ASN B 2 211 ? 38.946 2.120   -2.611  1.00 28.19 ? 211 ASN B OD1 1 
ATOM   3323 N ND2 . ASN B 2 211 ? 40.923 2.455   -1.609  1.00 32.96 ? 211 ASN B ND2 1 
ATOM   3324 N N   . SER B 2 212 ? 42.833 -1.353  -1.218  1.00 23.98 ? 212 SER B N   1 
ATOM   3325 C CA  . SER B 2 212 ? 42.637 -2.418  -0.247  1.00 21.84 ? 212 SER B CA  1 
ATOM   3326 C C   . SER B 2 212 ? 43.926 -2.600  0.546   1.00 20.51 ? 212 SER B C   1 
ATOM   3327 O O   . SER B 2 212 ? 45.029 -2.374  0.032   1.00 19.37 ? 212 SER B O   1 
ATOM   3328 C CB  . SER B 2 212 ? 42.244 -3.716  -0.962  1.00 21.71 ? 212 SER B CB  1 
ATOM   3329 O OG  . SER B 2 212 ? 42.136 -4.776  -0.045  1.00 23.37 ? 212 SER B OG  1 
ATOM   3330 N N   . SER B 2 213 ? 43.773 -3.016  1.799   1.00 18.80 ? 213 SER B N   1 
ATOM   3331 C CA  . SER B 2 213 ? 44.909 -3.177  2.696   1.00 21.25 ? 213 SER B CA  1 
ATOM   3332 C C   . SER B 2 213 ? 44.672 -4.384  3.596   1.00 17.49 ? 213 SER B C   1 
ATOM   3333 O O   . SER B 2 213 ? 43.533 -4.724  3.918   1.00 17.45 ? 213 SER B O   1 
ATOM   3334 C CB  . SER B 2 213 ? 45.151 -1.916  3.587   1.00 22.47 ? 213 SER B CB  1 
ATOM   3335 O OG  . SER B 2 213 ? 45.786 -0.860  2.858   1.00 23.69 ? 213 SER B OG  1 
ATOM   3336 N N   . VAL B 2 214 ? 45.766 -5.029  3.998   1.00 15.69 ? 214 VAL B N   1 
ATOM   3337 C CA  . VAL B 2 214 ? 45.727 -6.151  4.926   1.00 16.40 ? 214 VAL B CA  1 
ATOM   3338 C C   . VAL B 2 214 ? 46.344 -5.692  6.241   1.00 17.10 ? 214 VAL B C   1 
ATOM   3339 O O   . VAL B 2 214 ? 47.451 -5.127  6.255   1.00 16.12 ? 214 VAL B O   1 
ATOM   3340 C CB  . VAL B 2 214 ? 46.416 -7.419  4.365   1.00 15.81 ? 214 VAL B CB  1 
ATOM   3341 C CG1 . VAL B 2 214 ? 46.398 -8.550  5.398   1.00 15.30 ? 214 VAL B CG1 1 
ATOM   3342 C CG2 . VAL B 2 214 ? 45.765 -7.876  3.049   1.00 14.31 ? 214 VAL B CG2 1 
ATOM   3343 N N   . TYR B 2 215 ? 45.620 -5.935  7.340   1.00 16.99 ? 215 TYR B N   1 
ATOM   3344 C CA  . TYR B 2 215 ? 46.073 -5.647  8.687   1.00 15.47 ? 215 TYR B CA  1 
ATOM   3345 C C   . TYR B 2 215 ? 46.547 -6.944  9.338   1.00 16.92 ? 215 TYR B C   1 
ATOM   3346 O O   . TYR B 2 215 ? 45.823 -7.941  9.326   1.00 16.74 ? 215 TYR B O   1 
ATOM   3347 C CB  . TYR B 2 215 ? 44.920 -5.027  9.469   1.00 16.36 ? 215 TYR B CB  1 
ATOM   3348 C CG  . TYR B 2 215 ? 44.577 -3.628  9.017   1.00 16.82 ? 215 TYR B CG  1 
ATOM   3349 C CD1 . TYR B 2 215 ? 44.050 -3.388  7.775   1.00 17.18 ? 215 TYR B CD1 1 
ATOM   3350 C CD2 . TYR B 2 215 ? 44.796 -2.535  9.857   1.00 19.98 ? 215 TYR B CD2 1 
ATOM   3351 C CE1 . TYR B 2 215 ? 43.734 -2.089  7.369   1.00 19.92 ? 215 TYR B CE1 1 
ATOM   3352 C CE2 . TYR B 2 215 ? 44.500 -1.235  9.451   1.00 19.30 ? 215 TYR B CE2 1 
ATOM   3353 C CZ  . TYR B 2 215 ? 43.961 -1.024  8.215   1.00 20.07 ? 215 TYR B CZ  1 
ATOM   3354 O OH  . TYR B 2 215 ? 43.663 0.272   7.827   1.00 21.95 ? 215 TYR B OH  1 
ATOM   3355 N N   . TYR B 2 216 ? 47.762 -6.928  9.906   1.00 15.56 ? 216 TYR B N   1 
ATOM   3356 C CA  . TYR B 2 216 ? 48.411 -8.136  10.396  1.00 13.93 ? 216 TYR B CA  1 
ATOM   3357 C C   . TYR B 2 216 ? 49.109 -7.844  11.709  1.00 14.71 ? 216 TYR B C   1 
ATOM   3358 O O   . TYR B 2 216 ? 49.812 -6.843  11.823  1.00 15.66 ? 216 TYR B O   1 
ATOM   3359 C CB  . TYR B 2 216 ? 49.475 -8.607  9.388   1.00 15.50 ? 216 TYR B CB  1 
ATOM   3360 C CG  . TYR B 2 216 ? 50.103 -9.974  9.678   1.00 14.36 ? 216 TYR B CG  1 
ATOM   3361 C CD1 . TYR B 2 216 ? 51.162 -10.109 10.584  1.00 14.09 ? 216 TYR B CD1 1 
ATOM   3362 C CD2 . TYR B 2 216 ? 49.687 -11.113 8.983   1.00 15.81 ? 216 TYR B CD2 1 
ATOM   3363 C CE1 . TYR B 2 216 ? 51.741 -11.337 10.831  1.00 12.83 ? 216 TYR B CE1 1 
ATOM   3364 C CE2 . TYR B 2 216 ? 50.269 -12.343 9.216   1.00 15.64 ? 216 TYR B CE2 1 
ATOM   3365 C CZ  . TYR B 2 216 ? 51.299 -12.444 10.131  1.00 14.82 ? 216 TYR B CZ  1 
ATOM   3366 O OH  . TYR B 2 216 ? 51.870 -13.679 10.344  1.00 16.61 ? 216 TYR B OH  1 
ATOM   3367 N N   . ASP B 2 217 ? 48.964 -8.737  12.685  1.00 12.66 ? 217 ASP B N   1 
ATOM   3368 C CA  . ASP B 2 217 ? 49.537 -8.518  14.003  1.00 13.60 ? 217 ASP B CA  1 
ATOM   3369 C C   . ASP B 2 217 ? 50.968 -9.031  14.052  1.00 15.07 ? 217 ASP B C   1 
ATOM   3370 O O   . ASP B 2 217 ? 51.253 -10.153 13.603  1.00 14.98 ? 217 ASP B O   1 
ATOM   3371 C CB  . ASP B 2 217 ? 48.692 -9.185  15.095  1.00 15.01 ? 217 ASP B CB  1 
ATOM   3372 C CG  . ASP B 2 217 ? 47.374 -8.440  15.360  1.00 16.36 ? 217 ASP B CG  1 
ATOM   3373 O OD1 . ASP B 2 217 ? 47.131 -7.386  14.700  1.00 16.48 ? 217 ASP B OD1 1 
ATOM   3374 O OD2 . ASP B 2 217 ? 46.591 -8.898  16.224  1.00 15.78 ? 217 ASP B OD2 1 
ATOM   3375 N N   . CYS B 2 218 ? 51.865 -8.206  14.604  1.00 13.69 ? 218 CYS B N   1 
ATOM   3376 C CA  . CYS B 2 218 ? 53.292 -8.500  14.652  1.00 13.14 ? 218 CYS B CA  1 
ATOM   3377 C C   . CYS B 2 218 ? 53.814 -8.345  16.076  1.00 13.07 ? 218 CYS B C   1 
ATOM   3378 O O   . CYS B 2 218 ? 53.587 -7.311  16.715  1.00 13.77 ? 218 CYS B O   1 
ATOM   3379 C CB  . CYS B 2 218 ? 54.071 -7.588  13.686  1.00 13.06 ? 218 CYS B CB  1 
ATOM   3380 S SG  . CYS B 2 218 ? 53.397 -7.405  12.030  1.00 15.64 ? 218 CYS B SG  1 
ATOM   3381 N N   . TRP B 2 219 ? 54.506 -9.366  16.575  1.00 11.72 ? 219 TRP B N   1 
ATOM   3382 C CA  . TRP B 2 219 ? 55.274 -9.217  17.796  1.00 12.09 ? 219 TRP B CA  1 
ATOM   3383 C C   . TRP B 2 219 ? 56.568 -8.451  17.514  1.00 12.75 ? 219 TRP B C   1 
ATOM   3384 O O   . TRP B 2 219 ? 57.144 -8.530  16.425  1.00 12.35 ? 219 TRP B O   1 
ATOM   3385 C CB  . TRP B 2 219 ? 55.613 -10.589 18.369  1.00 14.87 ? 219 TRP B CB  1 
ATOM   3386 C CG  . TRP B 2 219 ? 54.425 -11.238 19.041  1.00 15.29 ? 219 TRP B CG  1 
ATOM   3387 C CD1 . TRP B 2 219 ? 54.145 -11.280 20.390  1.00 14.81 ? 219 TRP B CD1 1 
ATOM   3388 C CD2 . TRP B 2 219 ? 53.329 -11.894 18.380  1.00 15.12 ? 219 TRP B CD2 1 
ATOM   3389 N NE1 . TRP B 2 219 ? 52.945 -11.946 20.611  1.00 15.34 ? 219 TRP B NE1 1 
ATOM   3390 C CE2 . TRP B 2 219 ? 52.427 -12.331 19.396  1.00 15.09 ? 219 TRP B CE2 1 
ATOM   3391 C CE3 . TRP B 2 219 ? 53.024 -12.161 17.040  1.00 14.20 ? 219 TRP B CE3 1 
ATOM   3392 C CZ2 . TRP B 2 219 ? 51.261 -13.028 19.098  1.00 12.94 ? 219 TRP B CZ2 1 
ATOM   3393 C CZ3 . TRP B 2 219 ? 51.851 -12.847 16.751  1.00 13.11 ? 219 TRP B CZ3 1 
ATOM   3394 C CH2 . TRP B 2 219 ? 50.999 -13.278 17.778  1.00 13.06 ? 219 TRP B CH2 1 
ATOM   3395 N N   . GLU B 2 220 ? 57.019 -7.698  18.519  1.00 14.73 ? 220 GLU B N   1 
ATOM   3396 C CA  . GLU B 2 220 ? 58.092 -6.708  18.343  1.00 13.46 ? 220 GLU B CA  1 
ATOM   3397 C C   . GLU B 2 220 ? 59.271 -7.205  17.523  1.00 11.96 ? 220 GLU B C   1 
ATOM   3398 O O   . GLU B 2 220 ? 59.711 -6.465  16.633  1.00 12.36 ? 220 GLU B O   1 
ATOM   3399 C CB  . GLU B 2 220 ? 58.548 -6.191  19.719  1.00 14.49 ? 220 GLU B CB  1 
ATOM   3400 C CG  . GLU B 2 220 ? 59.307 -4.906  19.667  1.00 12.97 ? 220 GLU B CG  1 
ATOM   3401 C CD  . GLU B 2 220 ? 59.346 -4.212  21.000  1.00 14.54 ? 220 GLU B CD  1 
ATOM   3402 O OE1 . GLU B 2 220 ? 60.250 -4.516  21.814  1.00 16.39 ? 220 GLU B OE1 1 
ATOM   3403 O OE2 . GLU B 2 220 ? 58.470 -3.358  21.248  1.00 14.78 ? 220 GLU B OE2 1 
ATOM   3404 N N   . PRO B 2 221 ? 59.820 -8.410  17.752  1.00 11.42 ? 221 PRO B N   1 
ATOM   3405 C CA  . PRO B 2 221 ? 61.008 -8.838  16.986  1.00 13.40 ? 221 PRO B CA  1 
ATOM   3406 C C   . PRO B 2 221 ? 60.739 -9.103  15.519  1.00 13.00 ? 221 PRO B C   1 
ATOM   3407 O O   . PRO B 2 221 ? 61.697 -9.236  14.737  1.00 11.63 ? 221 PRO B O   1 
ATOM   3408 C CB  . PRO B 2 221 ? 61.470 -10.099 17.726  1.00 13.47 ? 221 PRO B CB  1 
ATOM   3409 C CG  . PRO B 2 221 ? 60.922 -9.902  19.137  1.00 15.49 ? 221 PRO B CG  1 
ATOM   3410 C CD  . PRO B 2 221 ? 59.552 -9.325  18.865  1.00 13.59 ? 221 PRO B CD  1 
ATOM   3411 N N   . TYR B 2 222 ? 59.463 -9.165  15.113  1.00 12.94 ? 222 TYR B N   1 
ATOM   3412 C CA  . TYR B 2 222 ? 59.138 -9.397  13.713  1.00 12.16 ? 222 TYR B CA  1 
ATOM   3413 C C   . TYR B 2 222 ? 59.430 -8.179  12.861  1.00 12.46 ? 222 TYR B C   1 
ATOM   3414 O O   . TYR B 2 222 ? 59.643 -8.304  11.646  1.00 11.88 ? 222 TYR B O   1 
ATOM   3415 C CB  . TYR B 2 222 ? 57.652 -9.668  13.568  1.00 12.68 ? 222 TYR B CB  1 
ATOM   3416 C CG  . TYR B 2 222 ? 57.170 -11.003 14.080  1.00 14.90 ? 222 TYR B CG  1 
ATOM   3417 C CD1 . TYR B 2 222 ? 58.004 -11.856 14.808  1.00 13.67 ? 222 TYR B CD1 1 
ATOM   3418 C CD2 . TYR B 2 222 ? 55.856 -11.393 13.848  1.00 14.40 ? 222 TYR B CD2 1 
ATOM   3419 C CE1 . TYR B 2 222 ? 57.523 -13.072 15.278  1.00 14.99 ? 222 TYR B CE1 1 
ATOM   3420 C CE2 . TYR B 2 222 ? 55.368 -12.593 14.315  1.00 13.30 ? 222 TYR B CE2 1 
ATOM   3421 C CZ  . TYR B 2 222 ? 56.198 -13.425 15.018  1.00 14.73 ? 222 TYR B CZ  1 
ATOM   3422 O OH  . TYR B 2 222 ? 55.683 -14.618 15.458  1.00 15.19 ? 222 TYR B OH  1 
ATOM   3423 N N   . ILE B 2 223 ? 59.391 -6.990  13.462  1.00 13.66 ? 223 ILE B N   1 
ATOM   3424 C CA  . ILE B 2 223 ? 59.409 -5.753  12.694  1.00 14.19 ? 223 ILE B CA  1 
ATOM   3425 C C   . ILE B 2 223 ? 60.586 -4.886  13.145  1.00 13.48 ? 223 ILE B C   1 
ATOM   3426 O O   . ILE B 2 223 ? 60.904 -4.816  14.343  1.00 13.80 ? 223 ILE B O   1 
ATOM   3427 C CB  . ILE B 2 223 ? 58.063 -5.001  12.791  1.00 14.61 ? 223 ILE B CB  1 
ATOM   3428 C CG1 . ILE B 2 223 ? 57.633 -4.869  14.257  1.00 14.08 ? 223 ILE B CG1 1 
ATOM   3429 C CG2 . ILE B 2 223 ? 57.007 -5.741  11.972  1.00 13.28 ? 223 ILE B CG2 1 
ATOM   3430 C CD1 . ILE B 2 223 ? 56.442 -3.927  14.465  1.00 15.90 ? 223 ILE B CD1 1 
ATOM   3431 N N   . GLU B 2 224 ? 61.239 -4.258  12.171  1.00 14.51 ? 224 GLU B N   1 
ATOM   3432 C CA  . GLU B 2 224 ? 62.300 -3.305  12.423  1.00 18.21 ? 224 GLU B CA  1 
ATOM   3433 C C   . GLU B 2 224 ? 61.929 -1.995  11.735  1.00 20.10 ? 224 GLU B C   1 
ATOM   3434 O O   . GLU B 2 224 ? 61.150 -1.967  10.767  1.00 17.48 ? 224 GLU B O   1 
ATOM   3435 C CB  . GLU B 2 224 ? 63.647 -3.832  11.909  1.00 17.95 ? 224 GLU B CB  1 
ATOM   3436 C CG  . GLU B 2 224 ? 63.942 -3.479  10.468  1.00 23.07 ? 224 GLU B CG  1 
ATOM   3437 C CD  . GLU B 2 224 ? 65.446 -3.388  10.180  1.00 28.62 ? 224 GLU B CD  1 
ATOM   3438 O OE1 . GLU B 2 224 ? 66.236 -3.488  11.142  1.00 25.03 ? 224 GLU B OE1 1 
ATOM   3439 O OE2 . GLU B 2 224 ? 65.837 -3.202  8.994   1.00 33.12 ? 224 GLU B OE2 1 
ATOM   3440 N N   . LEU B 2 225 ? 62.501 -0.904  12.242  1.00 21.38 ? 225 LEU B N   1 
ATOM   3441 C CA  . LEU B 2 225 ? 62.077 0.427   11.822  1.00 21.76 ? 225 LEU B CA  1 
ATOM   3442 C C   . LEU B 2 225 ? 62.580 0.763   10.420  1.00 22.90 ? 225 LEU B C   1 
ATOM   3443 O O   . LEU B 2 225 ? 63.687 0.383   10.019  1.00 23.07 ? 225 LEU B O   1 
ATOM   3444 C CB  . LEU B 2 225 ? 62.521 1.471   12.864  1.00 25.44 ? 225 LEU B CB  1 
ATOM   3445 C CG  . LEU B 2 225 ? 61.955 2.898   12.920  1.00 25.19 ? 225 LEU B CG  1 
ATOM   3446 C CD1 . LEU B 2 225 ? 60.465 2.875   13.252  1.00 23.80 ? 225 LEU B CD1 1 
ATOM   3447 C CD2 . LEU B 2 225 ? 62.722 3.723   13.981  1.00 21.18 ? 225 LEU B CD2 1 
ATOM   3448 N N   . VAL B 2 226 ? 61.706 1.399   9.648   1.00 25.35 ? 226 VAL B N   1 
ATOM   3449 C CA  . VAL B 2 226 ? 62.062 2.064   8.401   1.00 27.81 ? 226 VAL B CA  1 
ATOM   3450 C C   . VAL B 2 226 ? 62.045 3.590   8.574   1.00 29.50 ? 226 VAL B C   1 
ATOM   3451 O O   . VAL B 2 226 ? 63.024 4.281   8.263   1.00 31.11 ? 226 VAL B O   1 
ATOM   3452 C CB  . VAL B 2 226 ? 61.146 1.601   7.234   1.00 24.43 ? 226 VAL B CB  1 
ATOM   3453 C CG1 . VAL B 2 226 ? 61.430 2.356   5.946   1.00 24.79 ? 226 VAL B CG1 1 
ATOM   3454 C CG2 . VAL B 2 226 ? 61.290 0.114   6.987   1.00 23.24 ? 226 VAL B CG2 1 
ATOM   3455 N N   . ASP B 2 227 ? 60.953 4.124   9.116   1.00 26.77 ? 227 ASP B N   1 
ATOM   3456 C CA  . ASP B 2 227 ? 60.818 5.555   9.324   1.00 28.82 ? 227 ASP B CA  1 
ATOM   3457 C C   . ASP B 2 227 ? 59.940 5.747   10.548  1.00 27.86 ? 227 ASP B C   1 
ATOM   3458 O O   . ASP B 2 227 ? 58.992 4.990   10.761  1.00 25.46 ? 227 ASP B O   1 
ATOM   3459 C CB  . ASP B 2 227 ? 60.140 6.200   8.107   1.00 32.44 ? 227 ASP B CB  1 
ATOM   3460 C CG  . ASP B 2 227 ? 60.976 6.075   6.831   1.00 36.04 ? 227 ASP B CG  1 
ATOM   3461 O OD1 . ASP B 2 227 ? 62.194 6.416   6.870   1.00 38.73 ? 227 ASP B OD1 1 
ATOM   3462 O OD2 . ASP B 2 227 ? 60.403 5.620   5.800   1.00 35.01 ? 227 ASP B OD2 1 
ATOM   3463 N N   . THR B 2 228 ? 60.252 6.761   11.344  1.00 30.22 ? 228 THR B N   1 
ATOM   3464 C CA  . THR B 2 228 ? 59.525 7.017   12.588  1.00 28.33 ? 228 THR B CA  1 
ATOM   3465 C C   . THR B 2 228 ? 58.312 7.945   12.362  1.00 30.39 ? 228 THR B C   1 
ATOM   3466 O O   . THR B 2 228 ? 57.296 7.875   13.079  1.00 30.04 ? 228 THR B O   1 
ATOM   3467 C CB  . THR B 2 228 ? 60.466 7.669   13.636  1.00 28.93 ? 228 THR B CB  1 
ATOM   3468 O OG1 . THR B 2 228 ? 59.933 7.480   14.946  1.00 28.93 ? 228 THR B OG1 1 
ATOM   3469 C CG2 . THR B 2 228 ? 60.580 9.171   13.368  1.00 32.55 ? 228 THR B CG2 1 
ATOM   3470 O OXT . THR B 2 228 ? 58.303 8.812   11.469  1.00 31.62 ? 228 THR B OXT 1 
HETATM 3471 C C1  . GOL C 3 .   ? 44.152 -22.482 16.404  1.00 21.17 ? 301 GOL A C1  1 
HETATM 3472 O O1  . GOL C 3 .   ? 44.089 -23.537 15.425  1.00 20.54 ? 301 GOL A O1  1 
HETATM 3473 C C2  . GOL C 3 .   ? 42.804 -21.811 16.600  1.00 20.80 ? 301 GOL A C2  1 
HETATM 3474 O O2  . GOL C 3 .   ? 42.941 -20.573 17.318  1.00 17.25 ? 301 GOL A O2  1 
HETATM 3475 C C3  . GOL C 3 .   ? 41.816 -22.724 17.302  1.00 20.04 ? 301 GOL A C3  1 
HETATM 3476 O O3  . GOL C 3 .   ? 41.795 -22.516 18.711  1.00 22.06 ? 301 GOL A O3  1 
HETATM 3477 H H11 . GOL C 3 .   ? 44.824 -21.831 16.114  1.00 25.54 ? 301 GOL A H11 1 
HETATM 3478 H H12 . GOL C 3 .   ? 44.476 -22.861 17.247  1.00 25.54 ? 301 GOL A H12 1 
HETATM 3479 H HO1 . GOL C 3 .   ? 43.710 -23.220 14.734  1.00 24.78 ? 301 GOL A HO1 1 
HETATM 3480 H H2  . GOL C 3 .   ? 42.448 -21.578 15.718  1.00 25.10 ? 301 GOL A H2  1 
HETATM 3481 H HO2 . GOL C 3 .   ? 42.706 -20.721 18.121  1.00 20.84 ? 301 GOL A HO2 1 
HETATM 3482 H H31 . GOL C 3 .   ? 42.047 -23.663 17.146  1.00 24.19 ? 301 GOL A H31 1 
HETATM 3483 H H32 . GOL C 3 .   ? 40.909 -22.568 16.968  1.00 24.19 ? 301 GOL A H32 1 
HETATM 3484 H HO3 . GOL C 3 .   ? 41.314 -23.136 19.037  1.00 26.62 ? 301 GOL A HO3 1 
HETATM 3485 O O   . HOH D 4 .   ? 19.377 -12.812 12.173  1.00 27.60 ? 401 HOH A O   1 
HETATM 3486 O O   . HOH D 4 .   ? 25.121 1.976   11.676  1.00 24.93 ? 402 HOH A O   1 
HETATM 3487 O O   . HOH D 4 .   ? 27.202 -0.000  30.939  0.50 15.67 ? 403 HOH A O   1 
HETATM 3488 O O   . HOH D 4 .   ? 25.496 -29.348 17.448  1.00 20.16 ? 404 HOH A O   1 
HETATM 3489 O O   . HOH D 4 .   ? 32.323 4.070   -3.421  1.00 23.82 ? 405 HOH A O   1 
HETATM 3490 O O   . HOH D 4 .   ? 24.121 -10.825 6.729   1.00 17.33 ? 406 HOH A O   1 
HETATM 3491 O O   . HOH D 4 .   ? 38.010 -47.918 9.716   1.00 22.88 ? 407 HOH A O   1 
HETATM 3492 O O   . HOH D 4 .   ? 21.545 -4.802  22.651  1.00 21.67 ? 408 HOH A O   1 
HETATM 3493 O O   . HOH D 4 .   ? 42.490 -44.563 6.547   1.00 26.16 ? 409 HOH A O   1 
HETATM 3494 O O   . HOH D 4 .   ? 43.720 -15.391 23.871  1.00 15.53 ? 410 HOH A O   1 
HETATM 3495 O O   . HOH D 4 .   ? 17.781 -1.833  4.720   1.00 25.86 ? 411 HOH A O   1 
HETATM 3496 O O   . HOH D 4 .   ? 32.724 -7.478  -3.605  1.00 20.81 ? 412 HOH A O   1 
HETATM 3497 O O   . HOH D 4 .   ? 31.043 -24.111 6.630   1.00 17.11 ? 413 HOH A O   1 
HETATM 3498 O O   . HOH D 4 .   ? 34.303 -28.478 12.380  1.00 17.42 ? 414 HOH A O   1 
HETATM 3499 O O   . HOH D 4 .   ? 24.413 -32.308 18.637  1.00 23.28 ? 415 HOH A O   1 
HETATM 3500 O O   . HOH D 4 .   ? 42.755 -5.967  24.939  1.00 18.00 ? 416 HOH A O   1 
HETATM 3501 O O   . HOH D 4 .   ? 29.335 -21.668 19.047  1.00 19.26 ? 417 HOH A O   1 
HETATM 3502 O O   . HOH D 4 .   ? 41.451 -12.903 22.670  1.00 14.45 ? 418 HOH A O   1 
HETATM 3503 O O   . HOH D 4 .   ? 36.820 -51.599 9.054   1.00 34.40 ? 419 HOH A O   1 
HETATM 3504 O O   . HOH D 4 .   ? 31.852 -25.110 13.394  1.00 17.90 ? 420 HOH A O   1 
HETATM 3505 O O   . HOH D 4 .   ? 27.392 1.687   14.058  1.00 21.19 ? 421 HOH A O   1 
HETATM 3506 O O   . HOH D 4 .   ? 47.671 -37.605 32.071  1.00 19.40 ? 422 HOH A O   1 
HETATM 3507 O O   . HOH D 4 .   ? 23.535 -14.412 6.114   1.00 23.29 ? 423 HOH A O   1 
HETATM 3508 O O   . HOH D 4 .   ? 38.355 -20.758 16.481  1.00 14.08 ? 424 HOH A O   1 
HETATM 3509 O O   . HOH D 4 .   ? 38.459 -39.947 33.682  1.00 15.76 ? 425 HOH A O   1 
HETATM 3510 O O   . HOH D 4 .   ? 40.484 -32.510 -9.113  1.00 20.87 ? 426 HOH A O   1 
HETATM 3511 O O   . HOH D 4 .   ? 33.190 -4.474  -6.785  1.00 23.24 ? 427 HOH A O   1 
HETATM 3512 O O   . HOH D 4 .   ? 25.196 -3.333  7.130   1.00 19.90 ? 428 HOH A O   1 
HETATM 3513 O O   . HOH D 4 .   ? 34.155 -18.494 24.666  1.00 16.25 ? 429 HOH A O   1 
HETATM 3514 O O   . HOH D 4 .   ? 33.505 -34.317 35.285  1.00 15.01 ? 430 HOH A O   1 
HETATM 3515 O O   . HOH D 4 .   ? 33.852 -3.122  31.446  1.00 23.03 ? 431 HOH A O   1 
HETATM 3516 O O   . HOH D 4 .   ? 35.829 -24.257 1.947   1.00 16.30 ? 432 HOH A O   1 
HETATM 3517 O O   . HOH D 4 .   ? 35.385 5.926   7.347   1.00 24.25 ? 433 HOH A O   1 
HETATM 3518 O O   . HOH D 4 .   ? 33.920 -19.194 -3.516  1.00 21.63 ? 434 HOH A O   1 
HETATM 3519 O O   . HOH D 4 .   ? 36.584 -10.982 27.143  1.00 20.66 ? 435 HOH A O   1 
HETATM 3520 O O   . HOH D 4 .   ? 39.624 -18.864 17.940  1.00 18.21 ? 436 HOH A O   1 
HETATM 3521 O O   . HOH D 4 .   ? 29.725 -6.464  7.560   1.00 18.64 ? 437 HOH A O   1 
HETATM 3522 O O   . HOH D 4 .   ? 28.799 -21.718 15.991  1.00 18.78 ? 438 HOH A O   1 
HETATM 3523 O O   . HOH D 4 .   ? 34.137 -46.707 13.720  1.00 15.28 ? 439 HOH A O   1 
HETATM 3524 O O   . HOH D 4 .   ? 36.762 -21.920 3.018   1.00 15.63 ? 440 HOH A O   1 
HETATM 3525 O O   . HOH D 4 .   ? 41.715 -18.560 25.140  1.00 16.19 ? 441 HOH A O   1 
HETATM 3526 O O   . HOH D 4 .   ? 28.331 -2.825  7.084   1.00 16.70 ? 442 HOH A O   1 
HETATM 3527 O O   . HOH D 4 .   ? 41.354 -25.992 8.252   1.00 18.14 ? 443 HOH A O   1 
HETATM 3528 O O   . HOH D 4 .   ? 38.558 -0.051  17.350  1.00 21.31 ? 444 HOH A O   1 
HETATM 3529 O O   . HOH D 4 .   ? 29.253 0.615   11.401  1.00 20.01 ? 445 HOH A O   1 
HETATM 3530 O O   . HOH D 4 .   ? 31.320 -0.639  5.209   1.00 20.21 ? 446 HOH A O   1 
HETATM 3531 O O   . HOH D 4 .   ? 28.038 -19.111 7.892   1.00 15.96 ? 447 HOH A O   1 
HETATM 3532 O O   . HOH D 4 .   ? 45.121 -11.316 15.904  1.00 14.93 ? 448 HOH A O   1 
HETATM 3533 O O   . HOH D 4 .   ? 37.790 -2.208  20.594  1.00 20.97 ? 449 HOH A O   1 
HETATM 3534 O O   . HOH D 4 .   ? 30.233 -41.970 31.980  1.00 16.14 ? 450 HOH A O   1 
HETATM 3535 O O   . HOH D 4 .   ? 29.746 6.234   7.045   1.00 23.25 ? 451 HOH A O   1 
HETATM 3536 O O   . HOH D 4 .   ? 39.877 -17.889 9.169   1.00 18.12 ? 452 HOH A O   1 
HETATM 3537 O O   . HOH D 4 .   ? 34.729 -11.235 13.279  1.00 18.25 ? 453 HOH A O   1 
HETATM 3538 O O   . HOH D 4 .   ? 33.613 -29.271 5.444   1.00 21.39 ? 454 HOH A O   1 
HETATM 3539 O O   . HOH D 4 .   ? 18.498 4.841   17.203  1.00 24.44 ? 455 HOH A O   1 
HETATM 3540 O O   . HOH D 4 .   ? 48.373 -12.337 21.439  1.00 12.81 ? 456 HOH A O   1 
HETATM 3541 O O   . HOH D 4 .   ? 42.015 -32.605 32.557  1.00 13.00 ? 457 HOH A O   1 
HETATM 3542 O O   . HOH D 4 .   ? 16.171 3.245   17.319  1.00 22.07 ? 458 HOH A O   1 
HETATM 3543 O O   . HOH D 4 .   ? 31.539 -40.149 24.896  1.00 18.22 ? 459 HOH A O   1 
HETATM 3544 O O   . HOH D 4 .   ? 20.594 -10.921 20.358  1.00 22.43 ? 460 HOH A O   1 
HETATM 3545 O O   . HOH D 4 .   ? 36.090 5.148   20.302  1.00 16.89 ? 461 HOH A O   1 
HETATM 3546 O O   . HOH D 4 .   ? 25.768 -31.841 26.101  1.00 18.93 ? 462 HOH A O   1 
HETATM 3547 O O   . HOH D 4 .   ? 47.109 -43.523 28.293  1.00 19.41 ? 463 HOH A O   1 
HETATM 3548 O O   . HOH D 4 .   ? 48.288 -16.080 18.938  1.00 15.39 ? 464 HOH A O   1 
HETATM 3549 O O   . HOH D 4 .   ? 33.508 4.814   -0.477  1.00 18.73 ? 465 HOH A O   1 
HETATM 3550 O O   . HOH D 4 .   ? 36.810 1.217   13.671  1.00 20.12 ? 466 HOH A O   1 
HETATM 3551 O O   . HOH D 4 .   ? 30.040 -39.319 11.366  1.00 21.99 ? 467 HOH A O   1 
HETATM 3552 O O   . HOH D 4 .   ? 48.202 -22.519 13.079  1.00 15.13 ? 468 HOH A O   1 
HETATM 3553 O O   . HOH D 4 .   ? 20.492 -11.760 16.185  1.00 20.90 ? 469 HOH A O   1 
HETATM 3554 O O   . HOH D 4 .   ? 23.919 -15.364 12.876  1.00 15.96 ? 470 HOH A O   1 
HETATM 3555 O O   . HOH D 4 .   ? 39.609 -12.447 15.295  1.00 19.09 ? 471 HOH A O   1 
HETATM 3556 O O   . HOH D 4 .   ? 31.160 6.887   27.240  1.00 20.74 ? 472 HOH A O   1 
HETATM 3557 O O   . HOH D 4 .   ? 34.258 -41.355 18.367  1.00 15.87 ? 473 HOH A O   1 
HETATM 3558 O O   . HOH D 4 .   ? 37.838 -27.441 2.571   1.00 18.29 ? 474 HOH A O   1 
HETATM 3559 O O   . HOH D 4 .   ? 22.567 -18.357 18.418  1.00 20.20 ? 475 HOH A O   1 
HETATM 3560 O O   . HOH D 4 .   ? 44.241 -7.288  -0.435  1.00 18.39 ? 476 HOH A O   1 
HETATM 3561 O O   . HOH D 4 .   ? 24.706 7.902   24.318  1.00 23.72 ? 477 HOH A O   1 
HETATM 3562 O O   . HOH D 4 .   ? 46.460 -15.913 11.017  1.00 12.51 ? 478 HOH A O   1 
HETATM 3563 O O   . HOH D 4 .   ? 36.169 -17.853 -3.307  1.00 21.03 ? 479 HOH A O   1 
HETATM 3564 O O   . HOH D 4 .   ? 47.179 -39.183 34.518  1.00 23.46 ? 480 HOH A O   1 
HETATM 3565 O O   . HOH D 4 .   ? 22.646 -9.512  4.506   1.00 21.35 ? 481 HOH A O   1 
HETATM 3566 O O   . HOH D 4 .   ? 25.533 -6.621  -3.064  1.00 21.69 ? 482 HOH A O   1 
HETATM 3567 O O   . HOH D 4 .   ? 39.201 -12.642 -9.080  1.00 25.24 ? 483 HOH A O   1 
HETATM 3568 O O   . HOH D 4 .   ? 20.642 3.813   9.135   1.00 23.33 ? 484 HOH A O   1 
HETATM 3569 O O   . HOH D 4 .   ? 36.563 -45.952 1.095   1.00 20.06 ? 485 HOH A O   1 
HETATM 3570 O O   . HOH D 4 .   ? 32.825 -34.076 7.333   1.00 22.45 ? 486 HOH A O   1 
HETATM 3571 O O   . HOH D 4 .   ? 23.493 -1.883  5.573   1.00 27.23 ? 487 HOH A O   1 
HETATM 3572 O O   . HOH D 4 .   ? 25.545 1.411   30.269  1.00 21.90 ? 488 HOH A O   1 
HETATM 3573 O O   . HOH D 4 .   ? 20.355 -1.452  3.758   1.00 25.47 ? 489 HOH A O   1 
HETATM 3574 O O   . HOH D 4 .   ? 39.920 -29.860 -9.582  1.00 22.99 ? 490 HOH A O   1 
HETATM 3575 O O   . HOH D 4 .   ? 36.117 -13.900 12.976  1.00 18.15 ? 491 HOH A O   1 
HETATM 3576 O O   . HOH E 4 .   ? 45.207 -7.768  11.520  1.00 20.41 ? 301 HOH B O   1 
HETATM 3577 O O   . HOH E 4 .   ? 54.756 -24.241 12.211  1.00 20.45 ? 302 HOH B O   1 
HETATM 3578 O O   . HOH E 4 .   ? 59.069 -26.759 10.339  1.00 21.00 ? 303 HOH B O   1 
HETATM 3579 O O   . HOH E 4 .   ? 46.846 -5.399  26.092  1.00 15.01 ? 304 HOH B O   1 
HETATM 3580 O O   . HOH E 4 .   ? 33.831 -50.006 12.824  1.00 22.93 ? 305 HOH B O   1 
HETATM 3581 O O   . HOH E 4 .   ? 49.644 -35.513 33.096  1.00 23.76 ? 306 HOH B O   1 
HETATM 3582 O O   . HOH E 4 .   ? 57.397 10.415  13.057  1.00 31.43 ? 307 HOH B O   1 
HETATM 3583 O O   . HOH E 4 .   ? 29.559 -37.493 22.460  1.00 22.51 ? 308 HOH B O   1 
HETATM 3584 O O   . HOH E 4 .   ? 44.616 -13.292 25.412  1.00 14.21 ? 309 HOH B O   1 
HETATM 3585 O O   . HOH E 4 .   ? 33.964 -50.119 30.275  1.00 22.31 ? 310 HOH B O   1 
HETATM 3586 O O   . HOH E 4 .   ? 32.702 -17.253 26.741  1.00 18.43 ? 311 HOH B O   1 
HETATM 3587 O O   . HOH E 4 .   ? 44.745 -17.628 25.437  1.00 15.67 ? 312 HOH B O   1 
HETATM 3588 O O   . HOH E 4 .   ? 54.615 -21.773 12.556  1.00 19.85 ? 313 HOH B O   1 
HETATM 3589 O O   . HOH E 4 .   ? 32.274 -26.556 15.983  1.00 14.05 ? 314 HOH B O   1 
HETATM 3590 O O   . HOH E 4 .   ? 44.545 -16.887 -3.484  1.00 19.68 ? 315 HOH B O   1 
HETATM 3591 O O   . HOH E 4 .   ? 49.046 -52.152 23.702  1.00 22.91 ? 316 HOH B O   1 
HETATM 3592 O O   . HOH E 4 .   ? 59.302 -20.025 9.162   1.00 16.87 ? 317 HOH B O   1 
HETATM 3593 O O   . HOH E 4 .   ? 60.632 -12.884 24.017  1.00 15.25 ? 318 HOH B O   1 
HETATM 3594 O O   . HOH E 4 .   ? 27.161 -52.362 16.211  1.00 19.10 ? 319 HOH B O   1 
HETATM 3595 O O   . HOH E 4 .   ? 54.791 -19.834 8.076   1.00 16.62 ? 320 HOH B O   1 
HETATM 3596 O O   . HOH E 4 .   ? 52.950 -27.127 27.662  1.00 22.72 ? 321 HOH B O   1 
HETATM 3597 O O   . HOH E 4 .   ? 41.117 -28.061 1.019   1.00 18.49 ? 322 HOH B O   1 
HETATM 3598 O O   . HOH E 4 .   ? 60.093 -20.018 15.914  1.00 17.86 ? 323 HOH B O   1 
HETATM 3599 O O   . HOH E 4 .   ? 50.383 -19.369 18.084  1.00 14.44 ? 324 HOH B O   1 
HETATM 3600 O O   . HOH E 4 .   ? 46.106 -24.889 10.811  1.00 18.46 ? 325 HOH B O   1 
HETATM 3601 O O   . HOH E 4 .   ? 53.483 -30.091 27.747  1.00 20.51 ? 326 HOH B O   1 
HETATM 3602 O O   . HOH E 4 .   ? 61.200 -17.606 15.305  1.00 19.60 ? 327 HOH B O   1 
HETATM 3603 O O   . HOH E 4 .   ? 53.039 -11.344 -0.495  1.00 13.46 ? 328 HOH B O   1 
HETATM 3604 O O   . HOH E 4 .   ? 52.861 -29.766 7.543   1.00 18.64 ? 329 HOH B O   1 
HETATM 3605 O O   . HOH E 4 .   ? 48.967 -28.250 9.013   1.00 15.55 ? 330 HOH B O   1 
HETATM 3606 O O   . HOH E 4 .   ? 50.909 -33.427 13.896  1.00 19.68 ? 331 HOH B O   1 
HETATM 3607 O O   . HOH E 4 .   ? 50.072 -14.352 22.638  1.00 12.60 ? 332 HOH B O   1 
HETATM 3608 O O   . HOH E 4 .   ? 25.641 -52.636 19.567  1.00 16.05 ? 333 HOH B O   1 
HETATM 3609 O O   . HOH E 4 .   ? 48.631 -17.368 5.751   1.00 13.62 ? 334 HOH B O   1 
HETATM 3610 O O   . HOH E 4 .   ? 51.678 -20.319 12.685  1.00 15.19 ? 335 HOH B O   1 
HETATM 3611 O O   . HOH E 4 .   ? 49.717 -16.726 20.899  1.00 15.23 ? 336 HOH B O   1 
HETATM 3612 O O   . HOH E 4 .   ? 43.257 -26.441 11.586  1.00 13.90 ? 337 HOH B O   1 
HETATM 3613 O O   . HOH E 4 .   ? 64.955 -9.776  8.092   1.00 16.72 ? 338 HOH B O   1 
HETATM 3614 O O   . HOH E 4 .   ? 56.718 -12.233 1.373   1.00 16.56 ? 339 HOH B O   1 
HETATM 3615 O O   . HOH E 4 .   ? 45.270 -49.770 14.569  1.00 18.77 ? 340 HOH B O   1 
HETATM 3616 O O   . HOH E 4 .   ? 56.226 -30.178 18.903  1.00 19.11 ? 341 HOH B O   1 
HETATM 3617 O O   . HOH E 4 .   ? 62.376 -19.963 19.150  1.00 18.32 ? 342 HOH B O   1 
HETATM 3618 O O   . HOH E 4 .   ? 32.352 -30.989 23.583  1.00 17.56 ? 343 HOH B O   1 
HETATM 3619 O O   . HOH E 4 .   ? 58.757 -6.583  23.582  1.00 17.74 ? 344 HOH B O   1 
HETATM 3620 O O   . HOH E 4 .   ? 58.074 3.634   24.000  1.00 24.26 ? 345 HOH B O   1 
HETATM 3621 O O   . HOH E 4 .   ? 31.788 -45.551 35.097  1.00 22.00 ? 346 HOH B O   1 
HETATM 3622 O O   . HOH E 4 .   ? 39.945 -5.868  -7.071  1.00 22.20 ? 347 HOH B O   1 
HETATM 3623 O O   . HOH E 4 .   ? 39.795 -1.263  -6.209  1.00 25.89 ? 348 HOH B O   1 
HETATM 3624 O O   . HOH E 4 .   ? 51.343 -16.984 3.264   1.00 13.92 ? 349 HOH B O   1 
HETATM 3625 O O   . HOH E 4 .   ? 32.808 -34.448 10.446  1.00 15.16 ? 350 HOH B O   1 
HETATM 3626 O O   . HOH E 4 .   ? 29.836 -25.769 12.379  1.00 18.22 ? 351 HOH B O   1 
HETATM 3627 O O   . HOH E 4 .   ? 31.043 -40.150 39.495  1.00 18.08 ? 352 HOH B O   1 
HETATM 3628 O O   . HOH E 4 .   ? 34.414 -46.890 16.390  1.00 13.59 ? 353 HOH B O   1 
HETATM 3629 O O   . HOH E 4 .   ? 31.810 -28.550 13.109  1.00 18.20 ? 354 HOH B O   1 
HETATM 3630 O O   . HOH E 4 .   ? 53.996 -4.188  30.117  1.00 20.60 ? 355 HOH B O   1 
HETATM 3631 O O   . HOH E 4 .   ? 43.093 -20.912 -3.411  1.00 17.90 ? 356 HOH B O   1 
HETATM 3632 O O   . HOH E 4 .   ? 59.755 -13.948 9.608   1.00 13.31 ? 357 HOH B O   1 
HETATM 3633 O O   . HOH E 4 .   ? 62.466 -16.106 4.281   1.00 21.28 ? 358 HOH B O   1 
HETATM 3634 O O   . HOH E 4 .   ? 61.673 -6.813  21.209  1.00 16.46 ? 359 HOH B O   1 
HETATM 3635 O O   . HOH E 4 .   ? 35.658 -24.777 15.847  1.00 11.44 ? 360 HOH B O   1 
HETATM 3636 O O   . HOH E 4 .   ? 51.080 -21.219 25.238  1.00 14.60 ? 361 HOH B O   1 
HETATM 3637 O O   . HOH E 4 .   ? 62.896 -13.428 17.940  1.00 20.25 ? 362 HOH B O   1 
HETATM 3638 O O   . HOH E 4 .   ? 49.064 -35.859 9.636   1.00 14.09 ? 363 HOH B O   1 
HETATM 3639 O O   . HOH E 4 .   ? 45.873 -16.409 16.306  1.00 18.64 ? 364 HOH B O   1 
HETATM 3640 O O   . HOH E 4 .   ? 59.692 -10.790 28.233  1.00 22.40 ? 365 HOH B O   1 
HETATM 3641 O O   . HOH E 4 .   ? 55.149 -48.915 23.398  1.00 21.01 ? 366 HOH B O   1 
HETATM 3642 O O   . HOH E 4 .   ? 47.315 -25.001 -5.162  1.00 14.35 ? 367 HOH B O   1 
HETATM 3643 O O   . HOH E 4 .   ? 52.451 -1.063  2.809   1.00 15.48 ? 368 HOH B O   1 
HETATM 3644 O O   . HOH E 4 .   ? 62.531 -11.831 14.047  1.00 14.51 ? 369 HOH B O   1 
HETATM 3645 O O   . HOH E 4 .   ? 50.841 -16.796 -0.900  1.00 20.93 ? 370 HOH B O   1 
HETATM 3646 O O   . HOH E 4 .   ? 60.095 -26.842 17.758  1.00 14.81 ? 371 HOH B O   1 
HETATM 3647 O O   . HOH E 4 .   ? 40.650 -22.817 34.142  1.00 22.00 ? 372 HOH B O   1 
HETATM 3648 O O   . HOH E 4 .   ? 35.413 -31.074 12.119  1.00 13.19 ? 373 HOH B O   1 
HETATM 3649 O O   . HOH E 4 .   ? 37.813 -39.420 36.155  1.00 17.73 ? 374 HOH B O   1 
HETATM 3650 O O   . HOH E 4 .   ? 54.661 -18.798 10.563  1.00 15.96 ? 375 HOH B O   1 
HETATM 3651 O O   . HOH E 4 .   ? 50.379 -52.385 19.606  1.00 16.82 ? 376 HOH B O   1 
HETATM 3652 O O   . HOH E 4 .   ? 30.284 -52.987 18.730  1.00 19.79 ? 377 HOH B O   1 
HETATM 3653 O O   . HOH E 4 .   ? 32.385 -45.976 17.627  1.00 16.96 ? 378 HOH B O   1 
HETATM 3654 O O   . HOH E 4 .   ? 25.041 -29.002 6.940   1.00 28.68 ? 379 HOH B O   1 
HETATM 3655 O O   . HOH E 4 .   ? 61.235 -19.086 3.835   1.00 19.84 ? 380 HOH B O   1 
HETATM 3656 O O   . HOH E 4 .   ? 52.419 -4.363  28.083  1.00 19.47 ? 381 HOH B O   1 
HETATM 3657 O O   . HOH E 4 .   ? 64.375 -0.455  14.382  1.00 16.92 ? 382 HOH B O   1 
HETATM 3658 O O   . HOH E 4 .   ? 36.510 -50.098 32.313  1.00 19.91 ? 383 HOH B O   1 
HETATM 3659 O O   . HOH E 4 .   ? 48.957 -17.793 23.782  1.00 13.48 ? 384 HOH B O   1 
HETATM 3660 O O   . HOH E 4 .   ? 49.138 2.451   20.000  1.00 19.30 ? 385 HOH B O   1 
HETATM 3661 O O   . HOH E 4 .   ? 61.402 -3.171  24.108  1.00 18.70 ? 386 HOH B O   1 
HETATM 3662 O O   . HOH E 4 .   ? 51.069 0.567   4.679   1.00 18.62 ? 387 HOH B O   1 
HETATM 3663 O O   . HOH E 4 .   ? 65.293 4.385   10.078  1.00 28.42 ? 388 HOH B O   1 
HETATM 3664 O O   . HOH E 4 .   ? 30.634 -39.812 15.668  1.00 18.94 ? 389 HOH B O   1 
HETATM 3665 O O   . HOH E 4 .   ? 32.275 -26.117 4.962   1.00 18.43 ? 390 HOH B O   1 
HETATM 3666 O O   . HOH E 4 .   ? 49.797 -23.299 1.277   1.00 17.48 ? 391 HOH B O   1 
HETATM 3667 O O   . HOH E 4 .   ? 61.805 2.715   17.105  1.00 19.57 ? 392 HOH B O   1 
HETATM 3668 O O   . HOH E 4 .   ? 55.921 -27.655 21.161  1.00 17.93 ? 393 HOH B O   1 
HETATM 3669 O O   . HOH E 4 .   ? 53.511 2.900   21.203  1.00 16.51 ? 394 HOH B O   1 
HETATM 3670 O O   . HOH E 4 .   ? 56.793 -19.149 30.748  1.00 17.64 ? 395 HOH B O   1 
HETATM 3671 O O   . HOH E 4 .   ? 31.085 -56.232 16.500  1.00 22.77 ? 396 HOH B O   1 
HETATM 3672 O O   . HOH E 4 .   ? 38.079 -23.437 16.097  1.00 14.58 ? 397 HOH B O   1 
HETATM 3673 O O   . HOH E 4 .   ? 56.403 -23.050 26.182  1.00 13.20 ? 398 HOH B O   1 
HETATM 3674 O O   . HOH E 4 .   ? 50.801 -27.743 6.958   1.00 18.23 ? 399 HOH B O   1 
HETATM 3675 O O   . HOH E 4 .   ? 30.212 -46.492 27.016  1.00 20.78 ? 400 HOH B O   1 
HETATM 3676 O O   . HOH E 4 .   ? 53.159 -34.900 14.320  1.00 19.16 ? 401 HOH B O   1 
HETATM 3677 O O   . HOH E 4 .   ? 63.492 -11.351 21.971  1.00 24.94 ? 402 HOH B O   1 
HETATM 3678 O O   . HOH E 4 .   ? 38.919 -28.850 4.224   1.00 19.99 ? 403 HOH B O   1 
HETATM 3679 O O   . HOH E 4 .   ? 47.237 -1.261  -2.434  1.00 20.86 ? 404 HOH B O   1 
HETATM 3680 O O   . HOH E 4 .   ? 51.956 -23.347 24.302  1.00 17.62 ? 405 HOH B O   1 
HETATM 3681 O O   . HOH E 4 .   ? 24.185 -26.903 16.738  1.00 18.95 ? 406 HOH B O   1 
HETATM 3682 O O   . HOH E 4 .   ? 48.655 -21.257 26.396  1.00 14.81 ? 407 HOH B O   1 
HETATM 3683 O O   . HOH E 4 .   ? 51.648 3.845   19.539  1.00 19.82 ? 408 HOH B O   1 
HETATM 3684 O O   . HOH E 4 .   ? 44.203 -3.263  22.150  1.00 17.80 ? 409 HOH B O   1 
HETATM 3685 O O   . HOH E 4 .   ? 55.640 -36.484 18.979  1.00 19.35 ? 410 HOH B O   1 
HETATM 3686 O O   . HOH E 4 .   ? 41.541 -27.754 6.143   1.00 17.73 ? 411 HOH B O   1 
HETATM 3687 O O   . HOH E 4 .   ? 47.291 -17.198 28.099  1.00 18.75 ? 412 HOH B O   1 
HETATM 3688 O O   . HOH E 4 .   ? 60.899 -19.288 29.513  1.00 16.26 ? 413 HOH B O   1 
HETATM 3689 O O   . HOH E 4 .   ? 38.009 -42.195 37.526  1.00 21.31 ? 414 HOH B O   1 
HETATM 3690 O O   . HOH E 4 .   ? 35.921 -29.421 8.033   1.00 19.69 ? 415 HOH B O   1 
HETATM 3691 O O   . HOH E 4 .   ? 52.633 7.862   17.564  1.00 16.59 ? 416 HOH B O   1 
HETATM 3692 O O   . HOH E 4 .   ? 51.631 2.534   23.715  1.00 20.45 ? 417 HOH B O   1 
HETATM 3693 O O   . HOH E 4 .   ? 62.746 -26.126 21.566  1.00 19.15 ? 418 HOH B O   1 
HETATM 3694 O O   . HOH E 4 .   ? 40.775 -21.828 -6.848  1.00 16.15 ? 419 HOH B O   1 
HETATM 3695 O O   . HOH E 4 .   ? 43.917 -35.812 1.065   1.00 16.02 ? 420 HOH B O   1 
HETATM 3696 O O   . HOH E 4 .   ? 62.527 -5.337  17.166  1.00 16.04 ? 421 HOH B O   1 
HETATM 3697 O O   . HOH E 4 .   ? 42.351 -21.213 35.824  1.00 35.63 ? 422 HOH B O   1 
HETATM 3698 O O   . HOH E 4 .   ? 34.617 -28.057 1.281   1.00 22.18 ? 423 HOH B O   1 
HETATM 3699 O O   . HOH E 4 .   ? 55.746 -1.766  29.168  1.00 24.44 ? 424 HOH B O   1 
HETATM 3700 O O   . HOH E 4 .   ? 51.960 -20.523 29.496  1.00 19.66 ? 425 HOH B O   1 
HETATM 3701 O O   . HOH E 4 .   ? 43.806 -55.762 20.501  1.00 24.46 ? 426 HOH B O   1 
HETATM 3702 O O   . HOH E 4 .   ? 53.053 -10.999 -13.428 1.00 16.57 ? 427 HOH B O   1 
HETATM 3703 O O   . HOH E 4 .   ? 47.330 -24.230 13.992  1.00 16.12 ? 428 HOH B O   1 
HETATM 3704 O O   . HOH E 4 .   ? 49.270 -6.162  27.624  1.00 18.33 ? 429 HOH B O   1 
HETATM 3705 O O   . HOH E 4 .   ? 24.207 -32.062 16.296  1.00 17.76 ? 430 HOH B O   1 
HETATM 3706 O O   . HOH E 4 .   ? 51.359 -35.548 34.930  1.00 21.21 ? 431 HOH B O   1 
HETATM 3707 O O   . HOH E 4 .   ? 51.848 -10.488 33.587  1.00 23.01 ? 432 HOH B O   1 
HETATM 3708 O O   . HOH E 4 .   ? 49.163 -44.373 27.502  1.00 20.38 ? 433 HOH B O   1 
HETATM 3709 O O   . HOH E 4 .   ? 57.200 -19.356 10.998  1.00 19.23 ? 434 HOH B O   1 
HETATM 3710 O O   . HOH E 4 .   ? 37.890 -12.163 29.433  1.00 19.67 ? 435 HOH B O   1 
HETATM 3711 O O   . HOH E 4 .   ? 46.925 -3.271  27.210  1.00 19.87 ? 436 HOH B O   1 
HETATM 3712 O O   . HOH E 4 .   ? 52.241 -23.549 0.000   0.50 16.64 ? 437 HOH B O   1 
HETATM 3713 O O   . HOH E 4 .   ? 50.208 -37.111 15.290  1.00 18.05 ? 438 HOH B O   1 
HETATM 3714 O O   . HOH E 4 .   ? 42.851 -33.007 34.693  1.00 19.57 ? 439 HOH B O   1 
HETATM 3715 O O   . HOH E 4 .   ? 51.510 -27.628 29.709  1.00 23.13 ? 440 HOH B O   1 
HETATM 3716 O O   . HOH E 4 .   ? 31.433 -44.495 30.971  1.00 26.38 ? 441 HOH B O   1 
HETATM 3717 O O   . HOH E 4 .   ? 49.719 -35.458 12.357  1.00 18.34 ? 442 HOH B O   1 
HETATM 3718 O O   . HOH E 4 .   ? 42.045 -22.003 32.615  1.00 23.25 ? 443 HOH B O   1 
HETATM 3719 O O   . HOH E 4 .   ? 61.960 -12.127 26.175  1.00 19.03 ? 444 HOH B O   1 
HETATM 3720 O O   . HOH E 4 .   ? 31.529 -41.210 18.882  1.00 27.01 ? 445 HOH B O   1 
HETATM 3721 O O   . HOH E 4 .   ? 62.450 -23.293 18.255  1.00 19.20 ? 446 HOH B O   1 
HETATM 3722 O O   . HOH E 4 .   ? 56.742 -12.182 -1.390  1.00 20.49 ? 447 HOH B O   1 
HETATM 3723 O O   . HOH E 4 .   ? 59.356 -28.202 19.500  1.00 22.27 ? 448 HOH B O   1 
HETATM 3724 O O   . HOH E 4 .   ? 47.332 -18.487 25.732  1.00 16.82 ? 449 HOH B O   1 
HETATM 3725 O O   . HOH E 4 .   ? 53.054 -20.178 27.427  1.00 17.86 ? 450 HOH B O   1 
HETATM 3726 O O   . HOH E 4 .   ? 57.504 5.152   21.892  1.00 24.43 ? 451 HOH B O   1 
HETATM 3727 O O   . HOH E 4 .   ? 59.600 -11.601 30.333  1.00 21.97 ? 452 HOH B O   1 
HETATM 3728 O O   . HOH E 4 .   ? 30.882 -40.508 20.870  1.00 19.77 ? 453 HOH B O   1 
HETATM 3729 O O   . HOH E 4 .   ? 31.380 -43.871 19.019  1.00 21.78 ? 454 HOH B O   1 
HETATM 3730 O O   . HOH E 4 .   ? 62.774 -25.553 18.774  1.00 23.84 ? 455 HOH B O   1 
HETATM 3731 O O   . HOH E 4 .   ? 63.737 -12.901 20.571  1.00 19.23 ? 456 HOH B O   1 
HETATM 3732 O O   . HOH E 4 .   ? 53.658 -0.515  27.700  1.00 18.64 ? 457 HOH B O   1 
HETATM 3733 O O   . HOH E 4 .   ? 49.389 -47.753 27.870  1.00 24.14 ? 458 HOH B O   1 
HETATM 3734 O O   . HOH E 4 .   ? 49.471 -21.032 29.115  1.00 19.75 ? 459 HOH B O   1 
HETATM 3735 O O   . HOH E 4 .   ? 44.573 -22.701 33.404  1.00 22.78 ? 460 HOH B O   1 
# 
