data_8V8Q
# 
_entry.id   8V8Q 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8V8Q         pdb_00008v8q 10.2210/pdb8v8q/pdb 
WWPDB D_1000278834 ?            ?                   
# 
_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       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        8V8Q 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-05 
_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                 4 
_pdbx_contact_author.email              michelle.krogsgaard@nyulangone.org 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Krogsgaard 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5006-7981 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Oltean, N.'     1 0009-0000-6715-6593 
'Nyovanie, S.'   2 0000-0003-0966-0024 
'Hashem, A.'     3 0009-0004-0434-0712 
'Patskovska, L.' 4 0000-0002-8910-0504 
'Patskovsky, Y.' 5 0000-0003-3316-2295 
'Krogsgaard, M.' 6 0000-0001-5006-7981 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'HUMAN LEUKOCYTE ANTIGEN B*07:02 IN COMPLEX WITH MERS-CoV EPITOPE N95-103 (A95S mutant)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Oltean, N.'     1 0009-0000-6715-6593 
primary 'Nyovanie, S.'   2 0000-0003-0966-0024 
primary 'Hashem, A.'     3 0009-0004-0434-0712 
primary 'Patskovska, L.' 4 0000-0002-8910-0504 
primary 'Patskovsky, Y.' 5 0000-0003-3316-2295 
primary 'Krogsgaard, M.' 6 0000-0001-5006-7981 
# 
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 'HLA class I histocompatibility antigen, B alpha chain' 32093.211 1   ? ?    'extracellular domain' ? 
2 polymer     man Beta-2-microglobulin                                    11879.356 1   ? ?    ?                      ? 
3 polymer     syn Nucleoprotein                                           1283.410  1   ? A95S 'residues 95-103'      ? 
4 non-polymer syn 'BICARBONATE ION'                                       61.017    2   ? ?    ?                      ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                 106.120   2   ? ?    ?                      ? 
6 non-polymer syn 'CHLORIDE ION'                                          35.453    1   ? ?    ?                      ? 
7 water       nat water                                                   18.015    419 ? ?    ?                      ? 
# 
_entity_name_com.entity_id   3 
_entity_name_com.name        'Nucleocapsid protein,NC,Protein N' 
# 
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 
;MGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLR
NLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAY
LEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDR
TFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWE
;
;MGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLR
NLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAY
LEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDR
TFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWE
;
A ? 
2 'polypeptide(L)' no no 
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
B ? 
3 'polypeptide(L)' no no SPRWYFYYT SPRWYFYYT C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'BICARBONATE ION'       BCT 
5 'DI(HYDROXYETHYL)ETHER' PEG 
6 'CHLORIDE ION'          CL  
7 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   GLY n 
1 3   SER n 
1 4   HIS n 
1 5   SER n 
1 6   MET n 
1 7   ARG n 
1 8   TYR n 
1 9   PHE n 
1 10  TYR n 
1 11  THR n 
1 12  SER n 
1 13  VAL n 
1 14  SER n 
1 15  ARG n 
1 16  PRO n 
1 17  GLY n 
1 18  ARG n 
1 19  GLY n 
1 20  GLU n 
1 21  PRO n 
1 22  ARG n 
1 23  PHE n 
1 24  ILE n 
1 25  SER n 
1 26  VAL n 
1 27  GLY n 
1 28  TYR n 
1 29  VAL n 
1 30  ASP n 
1 31  ASP n 
1 32  THR n 
1 33  GLN n 
1 34  PHE n 
1 35  VAL n 
1 36  ARG n 
1 37  PHE n 
1 38  ASP n 
1 39  SER n 
1 40  ASP n 
1 41  ALA n 
1 42  ALA n 
1 43  SER n 
1 44  PRO n 
1 45  ARG n 
1 46  GLU n 
1 47  GLU n 
1 48  PRO n 
1 49  ARG n 
1 50  ALA n 
1 51  PRO n 
1 52  TRP n 
1 53  ILE n 
1 54  GLU n 
1 55  GLN n 
1 56  GLU n 
1 57  GLY n 
1 58  PRO n 
1 59  GLU n 
1 60  TYR n 
1 61  TRP n 
1 62  ASP n 
1 63  ARG n 
1 64  ASN n 
1 65  THR n 
1 66  GLN n 
1 67  ILE n 
1 68  TYR n 
1 69  LYS n 
1 70  ALA n 
1 71  GLN n 
1 72  ALA n 
1 73  GLN n 
1 74  THR n 
1 75  ASP n 
1 76  ARG n 
1 77  GLU n 
1 78  SER n 
1 79  LEU n 
1 80  ARG n 
1 81  ASN n 
1 82  LEU n 
1 83  ARG n 
1 84  GLY n 
1 85  TYR n 
1 86  TYR n 
1 87  ASN n 
1 88  GLN n 
1 89  SER n 
1 90  GLU n 
1 91  ALA n 
1 92  GLY n 
1 93  SER n 
1 94  HIS n 
1 95  THR n 
1 96  LEU n 
1 97  GLN n 
1 98  SER n 
1 99  MET n 
1 100 TYR n 
1 101 GLY n 
1 102 CYS n 
1 103 ASP n 
1 104 VAL n 
1 105 GLY n 
1 106 PRO n 
1 107 ASP n 
1 108 GLY n 
1 109 ARG n 
1 110 LEU n 
1 111 LEU n 
1 112 ARG n 
1 113 GLY n 
1 114 HIS n 
1 115 ASP n 
1 116 GLN n 
1 117 TYR n 
1 118 ALA n 
1 119 TYR n 
1 120 ASP n 
1 121 GLY n 
1 122 LYS n 
1 123 ASP n 
1 124 TYR n 
1 125 ILE n 
1 126 ALA n 
1 127 LEU n 
1 128 ASN n 
1 129 GLU n 
1 130 ASP n 
1 131 LEU n 
1 132 ARG n 
1 133 SER n 
1 134 TRP n 
1 135 THR n 
1 136 ALA n 
1 137 ALA n 
1 138 ASP n 
1 139 THR n 
1 140 ALA n 
1 141 ALA n 
1 142 GLN n 
1 143 ILE n 
1 144 THR n 
1 145 GLN n 
1 146 ARG n 
1 147 LYS n 
1 148 TRP n 
1 149 GLU n 
1 150 ALA n 
1 151 ALA n 
1 152 ARG n 
1 153 GLU n 
1 154 ALA n 
1 155 GLU n 
1 156 GLN n 
1 157 ARG n 
1 158 ARG n 
1 159 ALA n 
1 160 TYR n 
1 161 LEU n 
1 162 GLU n 
1 163 GLY n 
1 164 GLU n 
1 165 CYS n 
1 166 VAL n 
1 167 GLU n 
1 168 TRP n 
1 169 LEU n 
1 170 ARG n 
1 171 ARG n 
1 172 TYR n 
1 173 LEU n 
1 174 GLU n 
1 175 ASN n 
1 176 GLY n 
1 177 LYS n 
1 178 ASP n 
1 179 LYS n 
1 180 LEU n 
1 181 GLU n 
1 182 ARG n 
1 183 ALA n 
1 184 ASP n 
1 185 PRO n 
1 186 PRO n 
1 187 LYS n 
1 188 THR n 
1 189 HIS n 
1 190 VAL n 
1 191 THR n 
1 192 HIS n 
1 193 HIS n 
1 194 PRO n 
1 195 ILE n 
1 196 SER n 
1 197 ASP n 
1 198 HIS n 
1 199 GLU n 
1 200 ALA n 
1 201 THR n 
1 202 LEU n 
1 203 ARG n 
1 204 CYS n 
1 205 TRP n 
1 206 ALA n 
1 207 LEU n 
1 208 GLY n 
1 209 PHE n 
1 210 TYR n 
1 211 PRO n 
1 212 ALA n 
1 213 GLU n 
1 214 ILE n 
1 215 THR n 
1 216 LEU n 
1 217 THR n 
1 218 TRP n 
1 219 GLN n 
1 220 ARG n 
1 221 ASP n 
1 222 GLY n 
1 223 GLU n 
1 224 ASP n 
1 225 GLN n 
1 226 THR n 
1 227 GLN n 
1 228 ASP n 
1 229 THR n 
1 230 GLU n 
1 231 LEU n 
1 232 VAL n 
1 233 GLU n 
1 234 THR n 
1 235 ARG n 
1 236 PRO n 
1 237 ALA n 
1 238 GLY n 
1 239 ASP n 
1 240 ARG n 
1 241 THR n 
1 242 PHE n 
1 243 GLN n 
1 244 LYS n 
1 245 TRP n 
1 246 ALA n 
1 247 ALA n 
1 248 VAL n 
1 249 VAL n 
1 250 VAL n 
1 251 PRO n 
1 252 SER n 
1 253 GLY n 
1 254 GLU n 
1 255 GLU n 
1 256 GLN n 
1 257 ARG n 
1 258 TYR n 
1 259 THR n 
1 260 CYS n 
1 261 HIS n 
1 262 VAL n 
1 263 GLN n 
1 264 HIS n 
1 265 GLU n 
1 266 GLY n 
1 267 LEU n 
1 268 PRO n 
1 269 LYS n 
1 270 PRO n 
1 271 LEU n 
1 272 THR n 
1 273 LEU n 
1 274 ARG n 
1 275 TRP n 
1 276 GLU n 
2 1   MET n 
2 2   ILE n 
2 3   GLN n 
2 4   ARG n 
2 5   THR n 
2 6   PRO n 
2 7   LYS n 
2 8   ILE n 
2 9   GLN n 
2 10  VAL n 
2 11  TYR n 
2 12  SER n 
2 13  ARG n 
2 14  HIS n 
2 15  PRO n 
2 16  ALA n 
2 17  GLU n 
2 18  ASN n 
2 19  GLY n 
2 20  LYS n 
2 21  SER n 
2 22  ASN n 
2 23  PHE n 
2 24  LEU n 
2 25  ASN n 
2 26  CYS n 
2 27  TYR n 
2 28  VAL n 
2 29  SER n 
2 30  GLY n 
2 31  PHE n 
2 32  HIS n 
2 33  PRO n 
2 34  SER n 
2 35  ASP n 
2 36  ILE n 
2 37  GLU n 
2 38  VAL n 
2 39  ASP n 
2 40  LEU n 
2 41  LEU n 
2 42  LYS n 
2 43  ASN n 
2 44  GLY n 
2 45  GLU n 
2 46  ARG n 
2 47  ILE n 
2 48  GLU n 
2 49  LYS n 
2 50  VAL n 
2 51  GLU n 
2 52  HIS n 
2 53  SER n 
2 54  ASP n 
2 55  LEU n 
2 56  SER n 
2 57  PHE n 
2 58  SER n 
2 59  LYS n 
2 60  ASP n 
2 61  TRP n 
2 62  SER n 
2 63  PHE n 
2 64  TYR n 
2 65  LEU n 
2 66  LEU n 
2 67  TYR n 
2 68  TYR n 
2 69  THR n 
2 70  GLU n 
2 71  PHE n 
2 72  THR n 
2 73  PRO n 
2 74  THR n 
2 75  GLU n 
2 76  LYS n 
2 77  ASP n 
2 78  GLU n 
2 79  TYR n 
2 80  ALA n 
2 81  CYS n 
2 82  ARG n 
2 83  VAL n 
2 84  ASN n 
2 85  HIS n 
2 86  VAL n 
2 87  THR n 
2 88  LEU n 
2 89  SER n 
2 90  GLN n 
2 91  PRO n 
2 92  LYS n 
2 93  ILE n 
2 94  VAL n 
2 95  LYS n 
2 96  TRP n 
2 97  ASP n 
2 98  ARG n 
2 99  ASP n 
2 100 MET n 
3 1   SER n 
3 2   PRO n 
3 3   ARG n 
3 4   TRP n 
3 5   TYR n 
3 6   PHE n 
3 7   TYR n 
3 8   TYR n 
3 9   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' 1 276 human ? HLA-B                      ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 100 human ? 'B2M, CDABP0092, HDCMA22P' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       9 
_pdbx_entity_src_syn.organism_scientific    'Middle East respiratory syndrome-related coronavirus' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       1335626 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
BCT non-polymer         . 'BICARBONATE ION'       ? 'C H O3 -1'      61.017  
CL  non-polymer         . 'CHLORIDE ION'          ? 'Cl -1'          35.453  
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  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
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   0   ?   ?   ?   A . n 
A 1 2   GLY 2   1   1   GLY GLY A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   HIS 4   3   3   HIS HIS A . n 
A 1 5   SER 5   4   4   SER SER A . n 
A 1 6   MET 6   5   5   MET MET A . n 
A 1 7   ARG 7   6   6   ARG ARG A . n 
A 1 8   TYR 8   7   7   TYR TYR A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  TYR 10  9   9   TYR TYR A . n 
A 1 11  THR 11  10  10  THR THR A . n 
A 1 12  SER 12  11  11  SER SER A . n 
A 1 13  VAL 13  12  12  VAL VAL A . n 
A 1 14  SER 14  13  13  SER SER A . n 
A 1 15  ARG 15  14  14  ARG ARG A . n 
A 1 16  PRO 16  15  15  PRO PRO A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ARG 18  17  17  ARG ARG A . n 
A 1 19  GLY 19  18  18  GLY GLY A . n 
A 1 20  GLU 20  19  19  GLU GLU A . n 
A 1 21  PRO 21  20  20  PRO PRO A . n 
A 1 22  ARG 22  21  21  ARG ARG A . n 
A 1 23  PHE 23  22  22  PHE PHE A . n 
A 1 24  ILE 24  23  23  ILE ILE A . n 
A 1 25  SER 25  24  24  SER SER A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  GLY 27  26  26  GLY GLY A . n 
A 1 28  TYR 28  27  27  TYR TYR A . n 
A 1 29  VAL 29  28  28  VAL VAL A . n 
A 1 30  ASP 30  29  29  ASP ASP A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  THR 32  31  31  THR THR A . n 
A 1 33  GLN 33  32  32  GLN GLN A . n 
A 1 34  PHE 34  33  33  PHE PHE A . n 
A 1 35  VAL 35  34  34  VAL VAL A . n 
A 1 36  ARG 36  35  35  ARG ARG A . n 
A 1 37  PHE 37  36  36  PHE PHE A . n 
A 1 38  ASP 38  37  37  ASP ASP A . n 
A 1 39  SER 39  38  38  SER SER A . n 
A 1 40  ASP 40  39  39  ASP ASP A . n 
A 1 41  ALA 41  40  40  ALA ALA A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  SER 43  42  42  SER SER A . n 
A 1 44  PRO 44  43  43  PRO PRO A . n 
A 1 45  ARG 45  44  44  ARG ARG A . n 
A 1 46  GLU 46  45  45  GLU GLU A . n 
A 1 47  GLU 47  46  46  GLU GLU A . n 
A 1 48  PRO 48  47  47  PRO PRO A . n 
A 1 49  ARG 49  48  48  ARG ARG A . n 
A 1 50  ALA 50  49  49  ALA ALA A . n 
A 1 51  PRO 51  50  50  PRO PRO A . n 
A 1 52  TRP 52  51  51  TRP TRP A . n 
A 1 53  ILE 53  52  52  ILE ILE A . n 
A 1 54  GLU 54  53  53  GLU GLU A . n 
A 1 55  GLN 55  54  54  GLN GLN A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  PRO 58  57  57  PRO PRO A . n 
A 1 59  GLU 59  58  58  GLU GLU A . n 
A 1 60  TYR 60  59  59  TYR TYR A . n 
A 1 61  TRP 61  60  60  TRP TRP A . n 
A 1 62  ASP 62  61  61  ASP ASP A . n 
A 1 63  ARG 63  62  62  ARG ARG A . n 
A 1 64  ASN 64  63  63  ASN ASN A . n 
A 1 65  THR 65  64  64  THR THR A . n 
A 1 66  GLN 66  65  65  GLN GLN A . n 
A 1 67  ILE 67  66  66  ILE ILE A . n 
A 1 68  TYR 68  67  67  TYR TYR A . n 
A 1 69  LYS 69  68  68  LYS LYS A . n 
A 1 70  ALA 70  69  69  ALA ALA A . n 
A 1 71  GLN 71  70  70  GLN GLN A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  GLN 73  72  72  GLN GLN A . n 
A 1 74  THR 74  73  73  THR THR A . n 
A 1 75  ASP 75  74  74  ASP ASP A . n 
A 1 76  ARG 76  75  75  ARG ARG A . n 
A 1 77  GLU 77  76  76  GLU GLU A . n 
A 1 78  SER 78  77  77  SER SER A . n 
A 1 79  LEU 79  78  78  LEU LEU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  ASN 81  80  80  ASN ASN A . n 
A 1 82  LEU 82  81  81  LEU LEU A . n 
A 1 83  ARG 83  82  82  ARG ARG A . n 
A 1 84  GLY 84  83  83  GLY GLY A . n 
A 1 85  TYR 85  84  84  TYR TYR A . n 
A 1 86  TYR 86  85  85  TYR TYR A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  GLN 88  87  87  GLN GLN A . n 
A 1 89  SER 89  88  88  SER SER A . n 
A 1 90  GLU 90  89  89  GLU GLU A . n 
A 1 91  ALA 91  90  90  ALA ALA A . n 
A 1 92  GLY 92  91  91  GLY GLY A . n 
A 1 93  SER 93  92  92  SER SER A . n 
A 1 94  HIS 94  93  93  HIS HIS A . n 
A 1 95  THR 95  94  94  THR THR A . n 
A 1 96  LEU 96  95  95  LEU LEU A . n 
A 1 97  GLN 97  96  96  GLN GLN A . n 
A 1 98  SER 98  97  97  SER SER A . n 
A 1 99  MET 99  98  98  MET MET A . n 
A 1 100 TYR 100 99  99  TYR TYR A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 CYS 102 101 101 CYS CYS A . n 
A 1 103 ASP 103 102 102 ASP ASP A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 GLY 105 104 104 GLY GLY A . n 
A 1 106 PRO 106 105 105 PRO PRO A . n 
A 1 107 ASP 107 106 106 ASP ASP A . n 
A 1 108 GLY 108 107 107 GLY GLY A . n 
A 1 109 ARG 109 108 108 ARG ARG A . n 
A 1 110 LEU 110 109 109 LEU LEU A . n 
A 1 111 LEU 111 110 110 LEU LEU A . n 
A 1 112 ARG 112 111 111 ARG ARG A . n 
A 1 113 GLY 113 112 112 GLY GLY A . n 
A 1 114 HIS 114 113 113 HIS HIS A . n 
A 1 115 ASP 115 114 114 ASP ASP A . n 
A 1 116 GLN 116 115 115 GLN GLN A . n 
A 1 117 TYR 117 116 116 TYR TYR A . n 
A 1 118 ALA 118 117 117 ALA ALA A . n 
A 1 119 TYR 119 118 118 TYR TYR A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 GLY 121 120 120 GLY GLY A . n 
A 1 122 LYS 122 121 121 LYS LYS A . n 
A 1 123 ASP 123 122 122 ASP ASP A . n 
A 1 124 TYR 124 123 123 TYR TYR A . n 
A 1 125 ILE 125 124 124 ILE ILE A . n 
A 1 126 ALA 126 125 125 ALA ALA A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 ASN 128 127 127 ASN ASN A . n 
A 1 129 GLU 129 128 128 GLU GLU A . n 
A 1 130 ASP 130 129 129 ASP ASP A . n 
A 1 131 LEU 131 130 130 LEU LEU A . n 
A 1 132 ARG 132 131 131 ARG ARG A . n 
A 1 133 SER 133 132 132 SER SER A . n 
A 1 134 TRP 134 133 133 TRP TRP A . n 
A 1 135 THR 135 134 134 THR THR A . n 
A 1 136 ALA 136 135 135 ALA ALA A . n 
A 1 137 ALA 137 136 136 ALA ALA A . n 
A 1 138 ASP 138 137 137 ASP ASP A . n 
A 1 139 THR 139 138 138 THR THR A . n 
A 1 140 ALA 140 139 139 ALA ALA A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLN 142 141 141 GLN GLN A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 THR 144 143 143 THR THR A . n 
A 1 145 GLN 145 144 144 GLN GLN A . n 
A 1 146 ARG 146 145 145 ARG ARG A . n 
A 1 147 LYS 147 146 146 LYS LYS A . n 
A 1 148 TRP 148 147 147 TRP TRP A . n 
A 1 149 GLU 149 148 148 GLU GLU A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 ALA 151 150 150 ALA ALA A . n 
A 1 152 ARG 152 151 151 ARG ARG A . n 
A 1 153 GLU 153 152 152 GLU GLU A . n 
A 1 154 ALA 154 153 153 ALA ALA A . n 
A 1 155 GLU 155 154 154 GLU GLU A . n 
A 1 156 GLN 156 155 155 GLN GLN A . n 
A 1 157 ARG 157 156 156 ARG ARG A . n 
A 1 158 ARG 158 157 157 ARG ARG A . n 
A 1 159 ALA 159 158 158 ALA ALA A . n 
A 1 160 TYR 160 159 159 TYR TYR A . n 
A 1 161 LEU 161 160 160 LEU LEU A . n 
A 1 162 GLU 162 161 161 GLU GLU A . n 
A 1 163 GLY 163 162 162 GLY GLY A . n 
A 1 164 GLU 164 163 163 GLU GLU A . n 
A 1 165 CYS 165 164 164 CYS CYS A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 GLU 167 166 166 GLU GLU A . n 
A 1 168 TRP 168 167 167 TRP TRP A . n 
A 1 169 LEU 169 168 168 LEU LEU A . n 
A 1 170 ARG 170 169 169 ARG ARG A . n 
A 1 171 ARG 171 170 170 ARG ARG A . n 
A 1 172 TYR 172 171 171 TYR TYR A . n 
A 1 173 LEU 173 172 172 LEU LEU A . n 
A 1 174 GLU 174 173 173 GLU GLU A . n 
A 1 175 ASN 175 174 174 ASN ASN A . n 
A 1 176 GLY 176 175 175 GLY GLY A . n 
A 1 177 LYS 177 176 176 LYS LYS A . n 
A 1 178 ASP 178 177 177 ASP ASP A . n 
A 1 179 LYS 179 178 178 LYS LYS A . n 
A 1 180 LEU 180 179 179 LEU LEU A . n 
A 1 181 GLU 181 180 180 GLU GLU A . n 
A 1 182 ARG 182 181 181 ARG ARG A . n 
A 1 183 ALA 183 182 182 ALA ALA A . n 
A 1 184 ASP 184 183 183 ASP ASP A . n 
A 1 185 PRO 185 184 184 PRO PRO A . n 
A 1 186 PRO 186 185 185 PRO PRO A . n 
A 1 187 LYS 187 186 186 LYS LYS A . n 
A 1 188 THR 188 187 187 THR THR A . n 
A 1 189 HIS 189 188 188 HIS HIS A . n 
A 1 190 VAL 190 189 189 VAL VAL A . n 
A 1 191 THR 191 190 190 THR THR A . n 
A 1 192 HIS 192 191 191 HIS HIS A . n 
A 1 193 HIS 193 192 192 HIS HIS A . n 
A 1 194 PRO 194 193 193 PRO PRO A . n 
A 1 195 ILE 195 194 194 ILE ILE A . n 
A 1 196 SER 196 195 195 SER SER A . n 
A 1 197 ASP 197 196 196 ASP ASP A . n 
A 1 198 HIS 198 197 197 HIS HIS A . n 
A 1 199 GLU 199 198 198 GLU GLU A . n 
A 1 200 ALA 200 199 199 ALA ALA A . n 
A 1 201 THR 201 200 200 THR THR A . n 
A 1 202 LEU 202 201 201 LEU LEU A . n 
A 1 203 ARG 203 202 202 ARG ARG A . n 
A 1 204 CYS 204 203 203 CYS CYS A . n 
A 1 205 TRP 205 204 204 TRP TRP A . n 
A 1 206 ALA 206 205 205 ALA ALA A . n 
A 1 207 LEU 207 206 206 LEU LEU A . n 
A 1 208 GLY 208 207 207 GLY GLY A . n 
A 1 209 PHE 209 208 208 PHE PHE A . n 
A 1 210 TYR 210 209 209 TYR TYR A . n 
A 1 211 PRO 211 210 210 PRO PRO A . n 
A 1 212 ALA 212 211 211 ALA ALA A . n 
A 1 213 GLU 213 212 212 GLU GLU A . n 
A 1 214 ILE 214 213 213 ILE ILE A . n 
A 1 215 THR 215 214 214 THR THR A . n 
A 1 216 LEU 216 215 215 LEU LEU A . n 
A 1 217 THR 217 216 216 THR THR A . n 
A 1 218 TRP 218 217 217 TRP TRP A . n 
A 1 219 GLN 219 218 218 GLN GLN A . n 
A 1 220 ARG 220 219 219 ARG ARG A . n 
A 1 221 ASP 221 220 220 ASP ASP A . n 
A 1 222 GLY 222 221 221 GLY GLY A . n 
A 1 223 GLU 223 222 222 GLU GLU A . n 
A 1 224 ASP 224 223 223 ASP ASP A . n 
A 1 225 GLN 225 224 224 GLN GLN A . n 
A 1 226 THR 226 225 225 THR THR A . n 
A 1 227 GLN 227 226 226 GLN GLN A . n 
A 1 228 ASP 228 227 227 ASP ASP A . n 
A 1 229 THR 229 228 228 THR THR A . n 
A 1 230 GLU 230 229 229 GLU GLU A . n 
A 1 231 LEU 231 230 230 LEU LEU A . n 
A 1 232 VAL 232 231 231 VAL VAL A . n 
A 1 233 GLU 233 232 232 GLU GLU A . n 
A 1 234 THR 234 233 233 THR THR A . n 
A 1 235 ARG 235 234 234 ARG ARG A . n 
A 1 236 PRO 236 235 235 PRO PRO A . n 
A 1 237 ALA 237 236 236 ALA ALA A . n 
A 1 238 GLY 238 237 237 GLY GLY A . n 
A 1 239 ASP 239 238 238 ASP ASP A . n 
A 1 240 ARG 240 239 239 ARG ARG A . n 
A 1 241 THR 241 240 240 THR THR A . n 
A 1 242 PHE 242 241 241 PHE PHE A . n 
A 1 243 GLN 243 242 242 GLN GLN A . n 
A 1 244 LYS 244 243 243 LYS LYS A . n 
A 1 245 TRP 245 244 244 TRP TRP A . n 
A 1 246 ALA 246 245 245 ALA ALA A . n 
A 1 247 ALA 247 246 246 ALA ALA A . n 
A 1 248 VAL 248 247 247 VAL VAL A . n 
A 1 249 VAL 249 248 248 VAL VAL A . n 
A 1 250 VAL 250 249 249 VAL VAL A . n 
A 1 251 PRO 251 250 250 PRO PRO A . n 
A 1 252 SER 252 251 251 SER SER A . n 
A 1 253 GLY 253 252 252 GLY GLY A . n 
A 1 254 GLU 254 253 253 GLU GLU A . n 
A 1 255 GLU 255 254 254 GLU GLU A . n 
A 1 256 GLN 256 255 255 GLN GLN A . n 
A 1 257 ARG 257 256 256 ARG ARG A . n 
A 1 258 TYR 258 257 257 TYR TYR A . n 
A 1 259 THR 259 258 258 THR THR A . n 
A 1 260 CYS 260 259 259 CYS CYS A . n 
A 1 261 HIS 261 260 260 HIS HIS A . n 
A 1 262 VAL 262 261 261 VAL VAL A . n 
A 1 263 GLN 263 262 262 GLN GLN A . n 
A 1 264 HIS 264 263 263 HIS HIS A . n 
A 1 265 GLU 265 264 264 GLU GLU A . n 
A 1 266 GLY 266 265 265 GLY GLY A . n 
A 1 267 LEU 267 266 266 LEU LEU A . n 
A 1 268 PRO 268 267 267 PRO PRO A . n 
A 1 269 LYS 269 268 268 LYS LYS A . n 
A 1 270 PRO 270 269 269 PRO PRO A . n 
A 1 271 LEU 271 270 270 LEU LEU A . n 
A 1 272 THR 272 271 271 THR THR A . n 
A 1 273 LEU 273 272 272 LEU LEU A . n 
A 1 274 ARG 274 273 273 ARG ARG A . n 
A 1 275 TRP 275 274 274 TRP TRP A . n 
A 1 276 GLU 276 275 275 GLU GLU A . n 
B 2 1   MET 1   0   0   MET MET B . n 
B 2 2   ILE 2   1   1   ILE ILE B . n 
B 2 3   GLN 3   2   2   GLN GLN B . n 
B 2 4   ARG 4   3   3   ARG ARG B . n 
B 2 5   THR 5   4   4   THR THR B . n 
B 2 6   PRO 6   5   5   PRO PRO B . n 
B 2 7   LYS 7   6   6   LYS LYS B . n 
B 2 8   ILE 8   7   7   ILE ILE B . n 
B 2 9   GLN 9   8   8   GLN GLN B . n 
B 2 10  VAL 10  9   9   VAL VAL B . n 
B 2 11  TYR 11  10  10  TYR TYR B . n 
B 2 12  SER 12  11  11  SER SER B . n 
B 2 13  ARG 13  12  12  ARG ARG B . n 
B 2 14  HIS 14  13  13  HIS HIS B . n 
B 2 15  PRO 15  14  14  PRO PRO B . n 
B 2 16  ALA 16  15  15  ALA ALA B . n 
B 2 17  GLU 17  16  16  GLU GLU B . n 
B 2 18  ASN 18  17  17  ASN ASN B . n 
B 2 19  GLY 19  18  18  GLY GLY B . n 
B 2 20  LYS 20  19  19  LYS LYS B . n 
B 2 21  SER 21  20  20  SER SER B . n 
B 2 22  ASN 22  21  21  ASN ASN B . n 
B 2 23  PHE 23  22  22  PHE PHE B . n 
B 2 24  LEU 24  23  23  LEU LEU B . n 
B 2 25  ASN 25  24  24  ASN ASN B . n 
B 2 26  CYS 26  25  25  CYS CYS B . n 
B 2 27  TYR 27  26  26  TYR TYR B . n 
B 2 28  VAL 28  27  27  VAL VAL B . n 
B 2 29  SER 29  28  28  SER SER B . n 
B 2 30  GLY 30  29  29  GLY GLY B . n 
B 2 31  PHE 31  30  30  PHE PHE B . n 
B 2 32  HIS 32  31  31  HIS HIS B . n 
B 2 33  PRO 33  32  32  PRO PRO B . n 
B 2 34  SER 34  33  33  SER SER B . n 
B 2 35  ASP 35  34  34  ASP ASP B . n 
B 2 36  ILE 36  35  35  ILE ILE B . n 
B 2 37  GLU 37  36  36  GLU GLU B . n 
B 2 38  VAL 38  37  37  VAL VAL B . n 
B 2 39  ASP 39  38  38  ASP ASP B . n 
B 2 40  LEU 40  39  39  LEU LEU B . n 
B 2 41  LEU 41  40  40  LEU LEU B . n 
B 2 42  LYS 42  41  41  LYS LYS B . n 
B 2 43  ASN 43  42  42  ASN ASN B . n 
B 2 44  GLY 44  43  43  GLY GLY B . n 
B 2 45  GLU 45  44  44  GLU GLU B . n 
B 2 46  ARG 46  45  45  ARG ARG B . n 
B 2 47  ILE 47  46  46  ILE ILE B . n 
B 2 48  GLU 48  47  47  GLU GLU B . n 
B 2 49  LYS 49  48  48  LYS LYS B . n 
B 2 50  VAL 50  49  49  VAL VAL B . n 
B 2 51  GLU 51  50  50  GLU GLU B . n 
B 2 52  HIS 52  51  51  HIS HIS B . n 
B 2 53  SER 53  52  52  SER SER B . n 
B 2 54  ASP 54  53  53  ASP ASP B . n 
B 2 55  LEU 55  54  54  LEU LEU B . n 
B 2 56  SER 56  55  55  SER SER B . n 
B 2 57  PHE 57  56  56  PHE PHE B . n 
B 2 58  SER 58  57  57  SER SER B . n 
B 2 59  LYS 59  58  58  LYS LYS B . n 
B 2 60  ASP 60  59  59  ASP ASP B . n 
B 2 61  TRP 61  60  60  TRP TRP B . n 
B 2 62  SER 62  61  61  SER SER B . n 
B 2 63  PHE 63  62  62  PHE PHE B . n 
B 2 64  TYR 64  63  63  TYR TYR B . n 
B 2 65  LEU 65  64  64  LEU LEU B . n 
B 2 66  LEU 66  65  65  LEU LEU B . n 
B 2 67  TYR 67  66  66  TYR TYR B . n 
B 2 68  TYR 68  67  67  TYR TYR B . n 
B 2 69  THR 69  68  68  THR THR B . n 
B 2 70  GLU 70  69  69  GLU GLU B . n 
B 2 71  PHE 71  70  70  PHE PHE B . n 
B 2 72  THR 72  71  71  THR THR B . n 
B 2 73  PRO 73  72  72  PRO PRO B . n 
B 2 74  THR 74  73  73  THR THR B . n 
B 2 75  GLU 75  74  74  GLU GLU B . n 
B 2 76  LYS 76  75  75  LYS LYS B . n 
B 2 77  ASP 77  76  76  ASP ASP B . n 
B 2 78  GLU 78  77  77  GLU GLU B . n 
B 2 79  TYR 79  78  78  TYR TYR B . n 
B 2 80  ALA 80  79  79  ALA ALA B . n 
B 2 81  CYS 81  80  80  CYS CYS B . n 
B 2 82  ARG 82  81  81  ARG ARG B . n 
B 2 83  VAL 83  82  82  VAL VAL B . n 
B 2 84  ASN 84  83  83  ASN ASN B . n 
B 2 85  HIS 85  84  84  HIS HIS B . n 
B 2 86  VAL 86  85  85  VAL VAL B . n 
B 2 87  THR 87  86  86  THR THR B . n 
B 2 88  LEU 88  87  87  LEU LEU B . n 
B 2 89  SER 89  88  88  SER SER B . n 
B 2 90  GLN 90  89  89  GLN GLN B . n 
B 2 91  PRO 91  90  90  PRO PRO B . n 
B 2 92  LYS 92  91  91  LYS LYS B . n 
B 2 93  ILE 93  92  92  ILE ILE B . n 
B 2 94  VAL 94  93  93  VAL VAL B . n 
B 2 95  LYS 95  94  94  LYS LYS B . n 
B 2 96  TRP 96  95  95  TRP TRP B . n 
B 2 97  ASP 97  96  96  ASP ASP B . n 
B 2 98  ARG 98  97  97  ARG ARG B . n 
B 2 99  ASP 99  98  98  ASP ASP B . n 
B 2 100 MET 100 99  99  MET MET B . n 
C 3 1   SER 1   1   1   SER SER C . n 
C 3 2   PRO 2   2   2   PRO PRO C . n 
C 3 3   ARG 3   3   3   ARG ARG C . n 
C 3 4   TRP 4   4   4   TRP TRP C . n 
C 3 5   TYR 5   5   5   TYR TYR C . n 
C 3 6   PHE 6   6   6   PHE PHE C . n 
C 3 7   TYR 7   7   7   TYR TYR C . n 
C 3 8   TYR 8   8   8   TYR TYR C . n 
C 3 9   THR 9   9   9   THR THR C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 BCT 1   301 301 BCT BCT A . 
E 5 PEG 1   302 401 PEG PEG A . 
F 4 BCT 1   303 101 BCT BCT A . 
G 5 PEG 1   304 101 PEG PEG A . 
H 6 CL  1   305 1   CL  CL  A . 
I 7 HOH 1   401 330 HOH HOH A . 
I 7 HOH 2   402 262 HOH HOH A . 
I 7 HOH 3   403 151 HOH HOH A . 
I 7 HOH 4   404 245 HOH HOH A . 
I 7 HOH 5   405 398 HOH HOH A . 
I 7 HOH 6   406 385 HOH HOH A . 
I 7 HOH 7   407 277 HOH HOH A . 
I 7 HOH 8   408 146 HOH HOH A . 
I 7 HOH 9   409 32  HOH HOH A . 
I 7 HOH 10  410 130 HOH HOH A . 
I 7 HOH 11  411 244 HOH HOH A . 
I 7 HOH 12  412 193 HOH HOH A . 
I 7 HOH 13  413 128 HOH HOH A . 
I 7 HOH 14  414 289 HOH HOH A . 
I 7 HOH 15  415 192 HOH HOH A . 
I 7 HOH 16  416 297 HOH HOH A . 
I 7 HOH 17  417 95  HOH HOH A . 
I 7 HOH 18  418 164 HOH HOH A . 
I 7 HOH 19  419 186 HOH HOH A . 
I 7 HOH 20  420 197 HOH HOH A . 
I 7 HOH 21  421 387 HOH HOH A . 
I 7 HOH 22  422 205 HOH HOH A . 
I 7 HOH 23  423 316 HOH HOH A . 
I 7 HOH 24  424 67  HOH HOH A . 
I 7 HOH 25  425 384 HOH HOH A . 
I 7 HOH 26  426 331 HOH HOH A . 
I 7 HOH 27  427 90  HOH HOH A . 
I 7 HOH 28  428 386 HOH HOH A . 
I 7 HOH 29  429 284 HOH HOH A . 
I 7 HOH 30  430 27  HOH HOH A . 
I 7 HOH 31  431 52  HOH HOH A . 
I 7 HOH 32  432 379 HOH HOH A . 
I 7 HOH 33  433 325 HOH HOH A . 
I 7 HOH 34  434 200 HOH HOH A . 
I 7 HOH 35  435 172 HOH HOH A . 
I 7 HOH 36  436 149 HOH HOH A . 
I 7 HOH 37  437 267 HOH HOH A . 
I 7 HOH 38  438 104 HOH HOH A . 
I 7 HOH 39  439 198 HOH HOH A . 
I 7 HOH 40  440 329 HOH HOH A . 
I 7 HOH 41  441 83  HOH HOH A . 
I 7 HOH 42  442 37  HOH HOH A . 
I 7 HOH 43  443 173 HOH HOH A . 
I 7 HOH 44  444 295 HOH HOH A . 
I 7 HOH 45  445 66  HOH HOH A . 
I 7 HOH 46  446 174 HOH HOH A . 
I 7 HOH 47  447 237 HOH HOH A . 
I 7 HOH 48  448 257 HOH HOH A . 
I 7 HOH 49  449 246 HOH HOH A . 
I 7 HOH 50  450 286 HOH HOH A . 
I 7 HOH 51  451 53  HOH HOH A . 
I 7 HOH 52  452 120 HOH HOH A . 
I 7 HOH 53  453 31  HOH HOH A . 
I 7 HOH 54  454 123 HOH HOH A . 
I 7 HOH 55  455 73  HOH HOH A . 
I 7 HOH 56  456 72  HOH HOH A . 
I 7 HOH 57  457 271 HOH HOH A . 
I 7 HOH 58  458 68  HOH HOH A . 
I 7 HOH 59  459 85  HOH HOH A . 
I 7 HOH 60  460 17  HOH HOH A . 
I 7 HOH 61  461 256 HOH HOH A . 
I 7 HOH 62  462 150 HOH HOH A . 
I 7 HOH 63  463 375 HOH HOH A . 
I 7 HOH 64  464 23  HOH HOH A . 
I 7 HOH 65  465 288 HOH HOH A . 
I 7 HOH 66  466 402 HOH HOH A . 
I 7 HOH 67  467 259 HOH HOH A . 
I 7 HOH 68  468 30  HOH HOH A . 
I 7 HOH 69  469 121 HOH HOH A . 
I 7 HOH 70  470 25  HOH HOH A . 
I 7 HOH 71  471 93  HOH HOH A . 
I 7 HOH 72  472 127 HOH HOH A . 
I 7 HOH 73  473 77  HOH HOH A . 
I 7 HOH 74  474 45  HOH HOH A . 
I 7 HOH 75  475 167 HOH HOH A . 
I 7 HOH 76  476 24  HOH HOH A . 
I 7 HOH 77  477 110 HOH HOH A . 
I 7 HOH 78  478 143 HOH HOH A . 
I 7 HOH 79  479 236 HOH HOH A . 
I 7 HOH 80  480 302 HOH HOH A . 
I 7 HOH 81  481 274 HOH HOH A . 
I 7 HOH 82  482 109 HOH HOH A . 
I 7 HOH 83  483 212 HOH HOH A . 
I 7 HOH 84  484 395 HOH HOH A . 
I 7 HOH 85  485 401 HOH HOH A . 
I 7 HOH 86  486 196 HOH HOH A . 
I 7 HOH 87  487 207 HOH HOH A . 
I 7 HOH 88  488 269 HOH HOH A . 
I 7 HOH 89  489 333 HOH HOH A . 
I 7 HOH 90  490 2   HOH HOH A . 
I 7 HOH 91  491 40  HOH HOH A . 
I 7 HOH 92  492 171 HOH HOH A . 
I 7 HOH 93  493 158 HOH HOH A . 
I 7 HOH 94  494 184 HOH HOH A . 
I 7 HOH 95  495 238 HOH HOH A . 
I 7 HOH 96  496 404 HOH HOH A . 
I 7 HOH 97  497 153 HOH HOH A . 
I 7 HOH 98  498 221 HOH HOH A . 
I 7 HOH 99  499 99  HOH HOH A . 
I 7 HOH 100 500 183 HOH HOH A . 
I 7 HOH 101 501 62  HOH HOH A . 
I 7 HOH 102 502 307 HOH HOH A . 
I 7 HOH 103 503 191 HOH HOH A . 
I 7 HOH 104 504 134 HOH HOH A . 
I 7 HOH 105 505 91  HOH HOH A . 
I 7 HOH 106 506 306 HOH HOH A . 
I 7 HOH 107 507 26  HOH HOH A . 
I 7 HOH 108 508 49  HOH HOH A . 
I 7 HOH 109 509 118 HOH HOH A . 
I 7 HOH 110 510 292 HOH HOH A . 
I 7 HOH 111 511 165 HOH HOH A . 
I 7 HOH 112 512 88  HOH HOH A . 
I 7 HOH 113 513 6   HOH HOH A . 
I 7 HOH 114 514 216 HOH HOH A . 
I 7 HOH 115 515 34  HOH HOH A . 
I 7 HOH 116 516 299 HOH HOH A . 
I 7 HOH 117 517 304 HOH HOH A . 
I 7 HOH 118 518 294 HOH HOH A . 
I 7 HOH 119 519 378 HOH HOH A . 
I 7 HOH 120 520 157 HOH HOH A . 
I 7 HOH 121 521 278 HOH HOH A . 
I 7 HOH 122 522 1   HOH HOH A . 
I 7 HOH 123 523 75  HOH HOH A . 
I 7 HOH 124 524 82  HOH HOH A . 
I 7 HOH 125 525 7   HOH HOH A . 
I 7 HOH 126 526 5   HOH HOH A . 
I 7 HOH 127 527 14  HOH HOH A . 
I 7 HOH 128 528 421 HOH HOH A . 
I 7 HOH 129 529 3   HOH HOH A . 
I 7 HOH 130 530 282 HOH HOH A . 
I 7 HOH 131 531 81  HOH HOH A . 
I 7 HOH 132 532 76  HOH HOH A . 
I 7 HOH 133 533 328 HOH HOH A . 
I 7 HOH 134 534 159 HOH HOH A . 
I 7 HOH 135 535 117 HOH HOH A . 
I 7 HOH 136 536 140 HOH HOH A . 
I 7 HOH 137 537 185 HOH HOH A . 
I 7 HOH 138 538 202 HOH HOH A . 
I 7 HOH 139 539 168 HOH HOH A . 
I 7 HOH 140 540 317 HOH HOH A . 
I 7 HOH 141 541 383 HOH HOH A . 
I 7 HOH 142 542 29  HOH HOH A . 
I 7 HOH 143 543 382 HOH HOH A . 
I 7 HOH 144 544 230 HOH HOH A . 
I 7 HOH 145 545 98  HOH HOH A . 
I 7 HOH 146 546 126 HOH HOH A . 
I 7 HOH 147 547 124 HOH HOH A . 
I 7 HOH 148 548 47  HOH HOH A . 
I 7 HOH 149 549 16  HOH HOH A . 
I 7 HOH 150 550 155 HOH HOH A . 
I 7 HOH 151 551 57  HOH HOH A . 
I 7 HOH 152 552 97  HOH HOH A . 
I 7 HOH 153 553 281 HOH HOH A . 
I 7 HOH 154 554 407 HOH HOH A . 
I 7 HOH 155 555 148 HOH HOH A . 
I 7 HOH 156 556 276 HOH HOH A . 
I 7 HOH 157 557 315 HOH HOH A . 
I 7 HOH 158 558 138 HOH HOH A . 
I 7 HOH 159 559 300 HOH HOH A . 
I 7 HOH 160 560 242 HOH HOH A . 
I 7 HOH 161 561 11  HOH HOH A . 
I 7 HOH 162 562 287 HOH HOH A . 
I 7 HOH 163 563 188 HOH HOH A . 
I 7 HOH 164 564 142 HOH HOH A . 
I 7 HOH 165 565 21  HOH HOH A . 
I 7 HOH 166 566 355 HOH HOH A . 
I 7 HOH 167 567 107 HOH HOH A . 
I 7 HOH 168 568 247 HOH HOH A . 
I 7 HOH 169 569 305 HOH HOH A . 
I 7 HOH 170 570 43  HOH HOH A . 
I 7 HOH 171 571 70  HOH HOH A . 
I 7 HOH 172 572 235 HOH HOH A . 
I 7 HOH 173 573 272 HOH HOH A . 
I 7 HOH 174 574 391 HOH HOH A . 
I 7 HOH 175 575 217 HOH HOH A . 
I 7 HOH 176 576 136 HOH HOH A . 
I 7 HOH 177 577 320 HOH HOH A . 
I 7 HOH 178 578 323 HOH HOH A . 
I 7 HOH 179 579 255 HOH HOH A . 
I 7 HOH 180 580 291 HOH HOH A . 
I 7 HOH 181 581 8   HOH HOH A . 
I 7 HOH 182 582 203 HOH HOH A . 
I 7 HOH 183 583 222 HOH HOH A . 
I 7 HOH 184 584 254 HOH HOH A . 
I 7 HOH 185 585 106 HOH HOH A . 
I 7 HOH 186 586 377 HOH HOH A . 
I 7 HOH 187 587 312 HOH HOH A . 
I 7 HOH 188 588 318 HOH HOH A . 
I 7 HOH 189 589 169 HOH HOH A . 
I 7 HOH 190 590 239 HOH HOH A . 
I 7 HOH 191 591 170 HOH HOH A . 
I 7 HOH 192 592 175 HOH HOH A . 
I 7 HOH 193 593 296 HOH HOH A . 
I 7 HOH 194 594 310 HOH HOH A . 
I 7 HOH 195 595 321 HOH HOH A . 
I 7 HOH 196 596 41  HOH HOH A . 
I 7 HOH 197 597 397 HOH HOH A . 
I 7 HOH 198 598 182 HOH HOH A . 
I 7 HOH 199 599 243 HOH HOH A . 
I 7 HOH 200 600 403 HOH HOH A . 
I 7 HOH 201 601 326 HOH HOH A . 
I 7 HOH 202 602 199 HOH HOH A . 
I 7 HOH 203 603 114 HOH HOH A . 
I 7 HOH 204 604 177 HOH HOH A . 
I 7 HOH 205 605 264 HOH HOH A . 
I 7 HOH 206 606 249 HOH HOH A . 
I 7 HOH 207 607 248 HOH HOH A . 
I 7 HOH 208 608 353 HOH HOH A . 
I 7 HOH 209 609 303 HOH HOH A . 
I 7 HOH 210 610 161 HOH HOH A . 
I 7 HOH 211 611 388 HOH HOH A . 
I 7 HOH 212 612 241 HOH HOH A . 
I 7 HOH 213 613 125 HOH HOH A . 
I 7 HOH 214 614 327 HOH HOH A . 
I 7 HOH 215 615 283 HOH HOH A . 
I 7 HOH 216 616 285 HOH HOH A . 
I 7 HOH 217 617 290 HOH HOH A . 
I 7 HOH 218 618 270 HOH HOH A . 
I 7 HOH 219 619 180 HOH HOH A . 
I 7 HOH 220 620 280 HOH HOH A . 
I 7 HOH 221 621 311 HOH HOH A . 
I 7 HOH 222 622 354 HOH HOH A . 
I 7 HOH 223 623 390 HOH HOH A . 
I 7 HOH 224 624 261 HOH HOH A . 
I 7 HOH 225 625 322 HOH HOH A . 
I 7 HOH 226 626 38  HOH HOH A . 
I 7 HOH 227 627 176 HOH HOH A . 
I 7 HOH 228 628 266 HOH HOH A . 
I 7 HOH 229 629 293 HOH HOH A . 
I 7 HOH 230 630 265 HOH HOH A . 
I 7 HOH 231 631 258 HOH HOH A . 
I 7 HOH 232 632 253 HOH HOH A . 
I 7 HOH 233 633 232 HOH HOH A . 
I 7 HOH 234 634 234 HOH HOH A . 
I 7 HOH 235 635 420 HOH HOH A . 
I 7 HOH 236 636 381 HOH HOH A . 
I 7 HOH 237 637 224 HOH HOH A . 
I 7 HOH 238 638 308 HOH HOH A . 
I 7 HOH 239 639 260 HOH HOH A . 
I 7 HOH 240 640 309 HOH HOH A . 
I 7 HOH 241 641 399 HOH HOH A . 
I 7 HOH 242 642 50  HOH HOH A . 
I 7 HOH 243 643 263 HOH HOH A . 
I 7 HOH 244 644 298 HOH HOH A . 
I 7 HOH 245 645 119 HOH HOH A . 
I 7 HOH 246 646 357 HOH HOH A . 
I 7 HOH 247 647 78  HOH HOH A . 
I 7 HOH 248 648 141 HOH HOH A . 
I 7 HOH 249 649 113 HOH HOH A . 
I 7 HOH 250 650 364 HOH HOH A . 
I 7 HOH 251 651 313 HOH HOH A . 
I 7 HOH 252 652 268 HOH HOH A . 
I 7 HOH 253 653 233 HOH HOH A . 
I 7 HOH 254 654 231 HOH HOH A . 
I 7 HOH 255 655 206 HOH HOH A . 
I 7 HOH 256 656 227 HOH HOH A . 
I 7 HOH 257 657 144 HOH HOH A . 
I 7 HOH 258 658 208 HOH HOH A . 
I 7 HOH 259 659 211 HOH HOH A . 
I 7 HOH 260 660 389 HOH HOH A . 
I 7 HOH 261 661 279 HOH HOH A . 
J 7 HOH 1   101 371 HOH HOH B . 
J 7 HOH 2   102 376 HOH HOH B . 
J 7 HOH 3   103 335 HOH HOH B . 
J 7 HOH 4   104 365 HOH HOH B . 
J 7 HOH 5   105 370 HOH HOH B . 
J 7 HOH 6   106 350 HOH HOH B . 
J 7 HOH 7   107 367 HOH HOH B . 
J 7 HOH 8   108 413 HOH HOH B . 
J 7 HOH 9   109 201 HOH HOH B . 
J 7 HOH 10  110 373 HOH HOH B . 
J 7 HOH 11  111 372 HOH HOH B . 
J 7 HOH 12  112 181 HOH HOH B . 
J 7 HOH 13  113 154 HOH HOH B . 
J 7 HOH 14  114 380 HOH HOH B . 
J 7 HOH 15  115 405 HOH HOH B . 
J 7 HOH 16  116 22  HOH HOH B . 
J 7 HOH 17  117 86  HOH HOH B . 
J 7 HOH 18  118 71  HOH HOH B . 
J 7 HOH 19  119 79  HOH HOH B . 
J 7 HOH 20  120 204 HOH HOH B . 
J 7 HOH 21  121 51  HOH HOH B . 
J 7 HOH 22  122 147 HOH HOH B . 
J 7 HOH 23  123 356 HOH HOH B . 
J 7 HOH 24  124 209 HOH HOH B . 
J 7 HOH 25  125 60  HOH HOH B . 
J 7 HOH 26  126 361 HOH HOH B . 
J 7 HOH 27  127 112 HOH HOH B . 
J 7 HOH 28  128 12  HOH HOH B . 
J 7 HOH 29  129 131 HOH HOH B . 
J 7 HOH 30  130 400 HOH HOH B . 
J 7 HOH 31  131 301 HOH HOH B . 
J 7 HOH 32  132 18  HOH HOH B . 
J 7 HOH 33  133 250 HOH HOH B . 
J 7 HOH 34  134 108 HOH HOH B . 
J 7 HOH 35  135 160 HOH HOH B . 
J 7 HOH 36  136 195 HOH HOH B . 
J 7 HOH 37  137 9   HOH HOH B . 
J 7 HOH 38  138 137 HOH HOH B . 
J 7 HOH 39  139 369 HOH HOH B . 
J 7 HOH 40  140 178 HOH HOH B . 
J 7 HOH 41  141 374 HOH HOH B . 
J 7 HOH 42  142 166 HOH HOH B . 
J 7 HOH 43  143 132 HOH HOH B . 
J 7 HOH 44  144 189 HOH HOH B . 
J 7 HOH 45  145 416 HOH HOH B . 
J 7 HOH 46  146 411 HOH HOH B . 
J 7 HOH 47  147 92  HOH HOH B . 
J 7 HOH 48  148 394 HOH HOH B . 
J 7 HOH 49  149 80  HOH HOH B . 
J 7 HOH 50  150 213 HOH HOH B . 
J 7 HOH 51  151 103 HOH HOH B . 
J 7 HOH 52  152 139 HOH HOH B . 
J 7 HOH 53  153 215 HOH HOH B . 
J 7 HOH 54  154 358 HOH HOH B . 
J 7 HOH 55  155 69  HOH HOH B . 
J 7 HOH 56  156 368 HOH HOH B . 
J 7 HOH 57  157 122 HOH HOH B . 
J 7 HOH 58  158 35  HOH HOH B . 
J 7 HOH 59  159 116 HOH HOH B . 
J 7 HOH 60  160 56  HOH HOH B . 
J 7 HOH 61  161 48  HOH HOH B . 
J 7 HOH 62  162 345 HOH HOH B . 
J 7 HOH 63  163 336 HOH HOH B . 
J 7 HOH 64  164 334 HOH HOH B . 
J 7 HOH 65  165 10  HOH HOH B . 
J 7 HOH 66  166 65  HOH HOH B . 
J 7 HOH 67  167 135 HOH HOH B . 
J 7 HOH 68  168 229 HOH HOH B . 
J 7 HOH 69  169 163 HOH HOH B . 
J 7 HOH 70  170 61  HOH HOH B . 
J 7 HOH 71  171 89  HOH HOH B . 
J 7 HOH 72  172 20  HOH HOH B . 
J 7 HOH 73  173 28  HOH HOH B . 
J 7 HOH 74  174 15  HOH HOH B . 
J 7 HOH 75  175 339 HOH HOH B . 
J 7 HOH 76  176 337 HOH HOH B . 
J 7 HOH 77  177 162 HOH HOH B . 
J 7 HOH 78  178 84  HOH HOH B . 
J 7 HOH 79  179 347 HOH HOH B . 
J 7 HOH 80  180 44  HOH HOH B . 
J 7 HOH 81  181 64  HOH HOH B . 
J 7 HOH 82  182 96  HOH HOH B . 
J 7 HOH 83  183 360 HOH HOH B . 
J 7 HOH 84  184 344 HOH HOH B . 
J 7 HOH 85  185 348 HOH HOH B . 
J 7 HOH 86  186 54  HOH HOH B . 
J 7 HOH 87  187 46  HOH HOH B . 
J 7 HOH 88  188 13  HOH HOH B . 
J 7 HOH 89  189 36  HOH HOH B . 
J 7 HOH 90  190 393 HOH HOH B . 
J 7 HOH 91  191 415 HOH HOH B . 
J 7 HOH 92  192 343 HOH HOH B . 
J 7 HOH 93  193 396 HOH HOH B . 
J 7 HOH 94  194 214 HOH HOH B . 
J 7 HOH 95  195 349 HOH HOH B . 
J 7 HOH 96  196 156 HOH HOH B . 
J 7 HOH 97  197 4   HOH HOH B . 
J 7 HOH 98  198 412 HOH HOH B . 
J 7 HOH 99  199 251 HOH HOH B . 
J 7 HOH 100 200 341 HOH HOH B . 
J 7 HOH 101 201 133 HOH HOH B . 
J 7 HOH 102 202 33  HOH HOH B . 
J 7 HOH 103 203 19  HOH HOH B . 
J 7 HOH 104 204 63  HOH HOH B . 
J 7 HOH 105 205 219 HOH HOH B . 
J 7 HOH 106 206 100 HOH HOH B . 
J 7 HOH 107 207 414 HOH HOH B . 
J 7 HOH 108 208 252 HOH HOH B . 
J 7 HOH 109 209 359 HOH HOH B . 
J 7 HOH 110 210 338 HOH HOH B . 
J 7 HOH 111 211 410 HOH HOH B . 
J 7 HOH 112 212 187 HOH HOH B . 
J 7 HOH 113 213 240 HOH HOH B . 
J 7 HOH 114 214 340 HOH HOH B . 
J 7 HOH 115 215 220 HOH HOH B . 
J 7 HOH 116 216 152 HOH HOH B . 
J 7 HOH 117 217 94  HOH HOH B . 
J 7 HOH 118 218 418 HOH HOH B . 
J 7 HOH 119 219 115 HOH HOH B . 
J 7 HOH 120 220 409 HOH HOH B . 
J 7 HOH 121 221 319 HOH HOH B . 
J 7 HOH 122 222 179 HOH HOH B . 
J 7 HOH 123 223 190 HOH HOH B . 
J 7 HOH 124 224 392 HOH HOH B . 
J 7 HOH 125 225 225 HOH HOH B . 
J 7 HOH 126 226 111 HOH HOH B . 
J 7 HOH 127 227 408 HOH HOH B . 
J 7 HOH 128 228 366 HOH HOH B . 
J 7 HOH 129 229 363 HOH HOH B . 
J 7 HOH 130 230 342 HOH HOH B . 
J 7 HOH 131 231 101 HOH HOH B . 
J 7 HOH 132 232 226 HOH HOH B . 
J 7 HOH 133 233 39  HOH HOH B . 
J 7 HOH 134 234 352 HOH HOH B . 
J 7 HOH 135 235 417 HOH HOH B . 
J 7 HOH 136 236 223 HOH HOH B . 
J 7 HOH 137 237 145 HOH HOH B . 
J 7 HOH 138 238 314 HOH HOH B . 
J 7 HOH 139 239 351 HOH HOH B . 
J 7 HOH 140 240 74  HOH HOH B . 
J 7 HOH 141 241 332 HOH HOH B . 
J 7 HOH 142 242 362 HOH HOH B . 
J 7 HOH 143 243 228 HOH HOH B . 
J 7 HOH 144 244 210 HOH HOH B . 
J 7 HOH 145 245 406 HOH HOH B . 
J 7 HOH 146 246 346 HOH HOH B . 
K 7 HOH 1   101 102 HOH HOH C . 
K 7 HOH 2   102 42  HOH HOH C . 
K 7 HOH 3   103 55  HOH HOH C . 
K 7 HOH 4   104 273 HOH HOH C . 
K 7 HOH 5   105 59  HOH HOH C . 
K 7 HOH 6   106 275 HOH HOH C . 
K 7 HOH 7   107 87  HOH HOH C . 
K 7 HOH 8   108 105 HOH HOH C . 
K 7 HOH 9   109 218 HOH HOH C . 
K 7 HOH 10  110 58  HOH HOH C . 
K 7 HOH 11  111 419 HOH HOH C . 
K 7 HOH 12  112 324 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 108 ? CG  ? A ARG 109 CG  
2  1 Y 1 A ARG 108 ? CD  ? A ARG 109 CD  
3  1 Y 1 A ARG 108 ? NE  ? A ARG 109 NE  
4  1 Y 1 A ARG 108 ? CZ  ? A ARG 109 CZ  
5  1 Y 1 A ARG 108 ? NH1 ? A ARG 109 NH1 
6  1 Y 1 A ARG 108 ? NH2 ? A ARG 109 NH2 
7  1 Y 1 B LYS 48  ? CG  ? B LYS 49  CG  
8  1 Y 1 B LYS 48  ? CD  ? B LYS 49  CD  
9  1 Y 1 B LYS 48  ? CE  ? B LYS 49  CE  
10 1 Y 1 B LYS 48  ? NZ  ? B LYS 49  NZ  
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0257 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8V8Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.858 
_cell.length_a_esd                 ? 
_cell.length_b                     153.872 
_cell.length_b_esd                 ? 
_cell.length_c                     87.572 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8V8Q 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   8V8Q 
_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             2.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.69 
_exptl_crystal.description                  'Thin plate' 
_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    '0.1 M HEPES: NaOH, pH 7.5, 25 % PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-28 
_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                    'Si (111)' 
_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   0.97934 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          23.7 
_reflns.entry_id                                       8V8Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               29.19 
_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                                     40656 
_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                     0 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.0 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.101 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.093 
_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                                    1.85 
_reflns_shell.d_res_low                                     1.89 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2482 
_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                               7.1 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.846 
_reflns_shell.pdbx_Rpim_I_all                               0.316 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.847 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.784 
_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]                            2.18 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.76 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.43 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.230 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8V8Q 
_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                            1.85 
_refine.ls_d_res_low                             28.92 
_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                     39413 
_refine.ls_number_reflns_R_free                  1217 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 3.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17088 
_refine.ls_R_factor_R_free                       0.20956 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16969 
_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                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      7LG0 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.121 
_refine.pdbx_overall_ESU_R_Free                  0.119 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.200 
_refine.overall_SU_ML                            0.093 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        28.92 
_refine_hist.number_atoms_solvent             419 
_refine_hist.number_atoms_total               3618 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3176 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.013  3307 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2847 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.580  1.662  4489 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.378  1.581  6606 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.392  5.000  386  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 29.529 21.290 217  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.859 15.000 525  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.905 15.000 32   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  402  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  3782 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  778  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.736  3.051  1544 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.737  3.051  1543 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.849  4.551  1927 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.847  4.551  1928 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.343  3.623  1763 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 7.341  3.623  1764 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 9.241  5.152  2562 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.003 35.704 3840 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.044 35.104 3736 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.850 
_refine_ls_shell.d_res_low                        1.898 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             74 
_refine_ls_shell.number_reflns_R_work             2885 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.251 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.313 
# 
_struct.entry_id                     8V8Q 
_struct.title                        'HUMAN LEUKOCYTE ANTIGEN B*07:02 IN COMPLEX WITH MERS-COV EPITOPE N95-103 (A95S 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        8V8Q 
_struct_keywords.text            'Viral Protein, Complex, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 5 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 7 ? 
K N N 7 ? 
# 
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 HLAB_HUMAN P01889 ? 1 
;GSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLRN
LRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAYL
EGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWE
;
25 
2 UNP B2MG_HUMAN P61769 ? 2 
;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
;
21 
3 UNP NCAP_MERS1 K9N4V7 ? 3 APRWYFYYT 95 
# 
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 8V8Q A 2 ? 276 ? P01889 25 ? 299 ? 1 275 
2 2 8V8Q B 2 ? 100 ? P61769 21 ? 119 ? 1 99  
3 3 8V8Q C 1 ? 9   ? K9N4V7 95 ? 103 ? 1 9   
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8V8Q MET A 1 ? UNP P01889 ?   ?  'initiating methionine' 0 1 
2 8V8Q MET B 1 ? UNP P61769 ?   ?  'initiating methionine' 0 2 
3 8V8Q SER C 1 ? UNP K9N4V7 ALA 95 'engineered mutation'   1 3 
# 
_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   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 50  ? GLU A 54  ? ALA A 49  GLU A 53  5 ? 5  
HELX_P HELX_P2 AA2 GLY A 57  ? TYR A 86  ? GLY A 56  TYR A 85  1 ? 30 
HELX_P HELX_P3 AA3 ASP A 138 ? ALA A 151 ? ASP A 137 ALA A 150 1 ? 14 
HELX_P HELX_P4 AA4 ARG A 152 ? GLY A 163 ? ARG A 151 GLY A 162 1 ? 12 
HELX_P HELX_P5 AA5 GLY A 163 ? LYS A 177 ? GLY A 162 LYS A 176 1 ? 15 
HELX_P HELX_P6 AA6 LYS A 177 ? ARG A 182 ? LYS A 176 ARG A 181 1 ? 6  
HELX_P HELX_P7 AA7 GLU A 254 ? GLN A 256 ? GLU A 253 GLN A 255 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 102 SG ? ? ? 1_555 A CYS 165 SG ? ? A CYS 101 A CYS 164 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
disulf2 disulf ? ? A CYS 204 SG ? ? ? 1_555 A CYS 260 SG ? ? A CYS 203 A CYS 259 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
disulf3 disulf ? ? B CYS 26  SG ? ? ? 1_555 B CYS 81  SG ? ? B CYS 25  B CYS 80  1_555 ? ? ? ? ? ? ? 1.995 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 102 ? CYS A 165 ? CYS A 101 ? 1_555 CYS A 164 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 204 ? CYS A 260 ? CYS A 203 ? 1_555 CYS A 259 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 26  ? CYS B 81  ? CYS B 25  ? 1_555 CYS B 80  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 210 A . ? TYR 209 A PRO 211 A ? PRO 210 A 1 -2.91 
2 HIS 32  B . ? HIS 31  B PRO 33  B ? PRO 32  B 1 -0.36 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 47  ? PRO A 48  ? GLU A 46  PRO A 47  
AA1 2 THR A 32  ? ASP A 38  ? THR A 31  ASP A 37  
AA1 3 ARG A 22  ? VAL A 29  ? ARG A 21  VAL A 28  
AA1 4 HIS A 4   ? VAL A 13  ? HIS A 3   VAL A 12  
AA1 5 THR A 95  ? VAL A 104 ? THR A 94  VAL A 103 
AA1 6 LEU A 110 ? TYR A 119 ? LEU A 109 TYR A 118 
AA1 7 LYS A 122 ? LEU A 127 ? LYS A 121 LEU A 126 
AA1 8 TRP A 134 ? ALA A 136 ? TRP A 133 ALA A 135 
AA2 1 LYS A 187 ? PRO A 194 ? LYS A 186 PRO A 193 
AA2 2 GLU A 199 ? PHE A 209 ? GLU A 198 PHE A 208 
AA2 3 PHE A 242 ? PRO A 251 ? PHE A 241 PRO A 250 
AA2 4 THR A 229 ? LEU A 231 ? THR A 228 LEU A 230 
AA3 1 LYS A 187 ? PRO A 194 ? LYS A 186 PRO A 193 
AA3 2 GLU A 199 ? PHE A 209 ? GLU A 198 PHE A 208 
AA3 3 PHE A 242 ? PRO A 251 ? PHE A 241 PRO A 250 
AA3 4 ARG A 235 ? PRO A 236 ? ARG A 234 PRO A 235 
AA4 1 GLU A 223 ? ASP A 224 ? GLU A 222 ASP A 223 
AA4 2 THR A 215 ? ARG A 220 ? THR A 214 ARG A 219 
AA4 3 TYR A 258 ? GLN A 263 ? TYR A 257 GLN A 262 
AA4 4 LEU A 271 ? LEU A 273 ? LEU A 270 LEU A 272 
AA5 1 LYS B 7   ? SER B 12  ? LYS B 6   SER B 11  
AA5 2 ASN B 22  ? SER B 29  ? ASN B 21  SER B 28  
AA5 3 PHE B 63  ? PHE B 71  ? PHE B 62  PHE B 70  
AA5 4 GLU B 51  ? HIS B 52  ? GLU B 50  HIS B 51  
AA6 1 LYS B 7   ? SER B 12  ? LYS B 6   SER B 11  
AA6 2 ASN B 22  ? SER B 29  ? ASN B 21  SER B 28  
AA6 3 PHE B 63  ? PHE B 71  ? PHE B 62  PHE B 70  
AA6 4 SER B 56  ? PHE B 57  ? SER B 55  PHE B 56  
AA7 1 GLU B 45  ? ARG B 46  ? GLU B 44  ARG B 45  
AA7 2 GLU B 37  ? LYS B 42  ? GLU B 36  LYS B 41  
AA7 3 TYR B 79  ? ASN B 84  ? TYR B 78  ASN B 83  
AA7 4 LYS B 92  ? LYS B 95  ? LYS B 91  LYS B 94  
# 
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 O GLU A 47  ? O GLU A 46  N ARG A 36  ? N ARG A 35  
AA1 2 3 O PHE A 34  ? O PHE A 33  N GLY A 27  ? N GLY A 26  
AA1 3 4 O ILE A 24  ? O ILE A 23  N THR A 11  ? N THR A 10  
AA1 4 5 N TYR A 10  ? N TYR A 9   O SER A 98  ? O SER A 97  
AA1 5 6 N ASP A 103 ? N ASP A 102 O LEU A 111 ? O LEU A 110 
AA1 6 7 N ASP A 115 ? N ASP A 114 O LEU A 127 ? O LEU A 126 
AA1 7 8 N ALA A 126 ? N ALA A 125 O THR A 135 ? O THR A 134 
AA2 1 2 N LYS A 187 ? N LYS A 186 O LEU A 207 ? O LEU A 206 
AA2 2 3 N ALA A 200 ? N ALA A 199 O VAL A 250 ? O VAL A 249 
AA2 3 4 O ALA A 247 ? O ALA A 246 N GLU A 230 ? N GLU A 229 
AA3 1 2 N LYS A 187 ? N LYS A 186 O LEU A 207 ? O LEU A 206 
AA3 2 3 N ALA A 200 ? N ALA A 199 O VAL A 250 ? O VAL A 249 
AA3 3 4 O GLN A 243 ? O GLN A 242 N ARG A 235 ? N ARG A 234 
AA4 1 2 O GLU A 223 ? O GLU A 222 N ARG A 220 ? N ARG A 219 
AA4 2 3 N THR A 217 ? N THR A 216 O HIS A 261 ? O HIS A 260 
AA4 3 4 N CYS A 260 ? N CYS A 259 O LEU A 273 ? O LEU A 272 
AA5 1 2 N LYS B 7   ? N LYS B 6   O SER B 29  ? O SER B 28  
AA5 2 3 N LEU B 24  ? N LEU B 23  O THR B 69  ? O THR B 68  
AA5 3 4 O TYR B 68  ? O TYR B 67  N GLU B 51  ? N GLU B 50  
AA6 1 2 N LYS B 7   ? N LYS B 6   O SER B 29  ? O SER B 28  
AA6 2 3 N LEU B 24  ? N LEU B 23  O THR B 69  ? O THR B 68  
AA6 3 4 O TYR B 64  ? O TYR B 63  N SER B 56  ? N SER B 55  
AA7 1 2 O GLU B 45  ? O GLU B 44  N LYS B 42  ? N LYS B 41  
AA7 2 3 N LEU B 41  ? N LEU B 40  O ALA B 80  ? O ALA B 79  
AA7 3 4 N CYS B 81  ? N CYS B 80  O VAL B 94  ? O VAL B 93  
# 
_pdbx_entry_details.entry_id                   8V8Q 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             232 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             232 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.323 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.071 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               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 NE A ARG 82 ? ? CZ A ARG 82 ? ? NH1 A ARG 82 ? ? 123.37 120.30 3.07  0.50 N 
2 1 NE C ARG 3  ? ? CZ C ARG 3  ? ? NH2 C ARG 3  ? ? 117.27 120.30 -3.03 0.50 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 ASP A 29  ? ? 50.45   -122.88 
2 1 SER A 42  ? ? 46.72   71.98   
3 1 ASP A 114 ? ? -164.49 98.21   
4 1 TYR A 123 ? ? -114.83 -72.22  
5 1 LYS A 176 ? ? 55.19   -122.83 
6 1 ASP A 220 ? ? 37.52   52.54   
7 1 TRP B 60  ? ? 84.36   5.33    
# 
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 528 ? I HOH . 
2 1 C HOH 105 ? K HOH . 
3 1 C HOH 111 ? K 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      0 
_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  
BCT C    C  N N 74  
BCT O1   O  N N 75  
BCT O2   O  N N 76  
BCT O3   O  N N 77  
BCT HO3  H  N N 78  
CL  CL   CL N N 79  
CYS N    N  N N 80  
CYS CA   C  N R 81  
CYS C    C  N N 82  
CYS O    O  N N 83  
CYS CB   C  N N 84  
CYS SG   S  N N 85  
CYS OXT  O  N N 86  
CYS H    H  N N 87  
CYS H2   H  N N 88  
CYS HA   H  N N 89  
CYS HB2  H  N N 90  
CYS HB3  H  N N 91  
CYS HG   H  N N 92  
CYS HXT  H  N N 93  
GLN N    N  N N 94  
GLN CA   C  N S 95  
GLN C    C  N N 96  
GLN O    O  N N 97  
GLN CB   C  N N 98  
GLN CG   C  N N 99  
GLN CD   C  N N 100 
GLN OE1  O  N N 101 
GLN NE2  N  N N 102 
GLN OXT  O  N N 103 
GLN H    H  N N 104 
GLN H2   H  N N 105 
GLN HA   H  N N 106 
GLN HB2  H  N N 107 
GLN HB3  H  N N 108 
GLN HG2  H  N N 109 
GLN HG3  H  N N 110 
GLN HE21 H  N N 111 
GLN HE22 H  N N 112 
GLN HXT  H  N N 113 
GLU N    N  N N 114 
GLU CA   C  N S 115 
GLU C    C  N N 116 
GLU O    O  N N 117 
GLU CB   C  N N 118 
GLU CG   C  N N 119 
GLU CD   C  N N 120 
GLU OE1  O  N N 121 
GLU OE2  O  N N 122 
GLU OXT  O  N N 123 
GLU H    H  N N 124 
GLU H2   H  N N 125 
GLU HA   H  N N 126 
GLU HB2  H  N N 127 
GLU HB3  H  N N 128 
GLU HG2  H  N N 129 
GLU HG3  H  N N 130 
GLU HE2  H  N N 131 
GLU HXT  H  N N 132 
GLY N    N  N N 133 
GLY CA   C  N N 134 
GLY C    C  N N 135 
GLY O    O  N N 136 
GLY OXT  O  N N 137 
GLY H    H  N N 138 
GLY H2   H  N N 139 
GLY HA2  H  N N 140 
GLY HA3  H  N N 141 
GLY HXT  H  N N 142 
HIS N    N  N N 143 
HIS CA   C  N S 144 
HIS C    C  N N 145 
HIS O    O  N N 146 
HIS CB   C  N N 147 
HIS CG   C  Y N 148 
HIS ND1  N  Y N 149 
HIS CD2  C  Y N 150 
HIS CE1  C  Y N 151 
HIS NE2  N  Y N 152 
HIS OXT  O  N N 153 
HIS H    H  N N 154 
HIS H2   H  N N 155 
HIS HA   H  N N 156 
HIS HB2  H  N N 157 
HIS HB3  H  N N 158 
HIS HD1  H  N N 159 
HIS HD2  H  N N 160 
HIS HE1  H  N N 161 
HIS HE2  H  N N 162 
HIS HXT  H  N N 163 
HOH O    O  N N 164 
HOH H1   H  N N 165 
HOH H2   H  N N 166 
ILE N    N  N N 167 
ILE CA   C  N S 168 
ILE C    C  N N 169 
ILE O    O  N N 170 
ILE CB   C  N S 171 
ILE CG1  C  N N 172 
ILE CG2  C  N N 173 
ILE CD1  C  N N 174 
ILE OXT  O  N N 175 
ILE H    H  N N 176 
ILE H2   H  N N 177 
ILE HA   H  N N 178 
ILE HB   H  N N 179 
ILE HG12 H  N N 180 
ILE HG13 H  N N 181 
ILE HG21 H  N N 182 
ILE HG22 H  N N 183 
ILE HG23 H  N N 184 
ILE HD11 H  N N 185 
ILE HD12 H  N N 186 
ILE HD13 H  N N 187 
ILE HXT  H  N N 188 
LEU N    N  N N 189 
LEU CA   C  N S 190 
LEU C    C  N N 191 
LEU O    O  N N 192 
LEU CB   C  N N 193 
LEU CG   C  N N 194 
LEU CD1  C  N N 195 
LEU CD2  C  N N 196 
LEU OXT  O  N N 197 
LEU H    H  N N 198 
LEU H2   H  N N 199 
LEU HA   H  N N 200 
LEU HB2  H  N N 201 
LEU HB3  H  N N 202 
LEU HG   H  N N 203 
LEU HD11 H  N N 204 
LEU HD12 H  N N 205 
LEU HD13 H  N N 206 
LEU HD21 H  N N 207 
LEU HD22 H  N N 208 
LEU HD23 H  N N 209 
LEU HXT  H  N N 210 
LYS N    N  N N 211 
LYS CA   C  N S 212 
LYS C    C  N N 213 
LYS O    O  N N 214 
LYS CB   C  N N 215 
LYS CG   C  N N 216 
LYS CD   C  N N 217 
LYS CE   C  N N 218 
LYS NZ   N  N N 219 
LYS OXT  O  N N 220 
LYS H    H  N N 221 
LYS H2   H  N N 222 
LYS HA   H  N N 223 
LYS HB2  H  N N 224 
LYS HB3  H  N N 225 
LYS HG2  H  N N 226 
LYS HG3  H  N N 227 
LYS HD2  H  N N 228 
LYS HD3  H  N N 229 
LYS HE2  H  N N 230 
LYS HE3  H  N N 231 
LYS HZ1  H  N N 232 
LYS HZ2  H  N N 233 
LYS HZ3  H  N N 234 
LYS HXT  H  N N 235 
MET N    N  N N 236 
MET CA   C  N S 237 
MET C    C  N N 238 
MET O    O  N N 239 
MET CB   C  N N 240 
MET CG   C  N N 241 
MET SD   S  N N 242 
MET CE   C  N N 243 
MET OXT  O  N N 244 
MET H    H  N N 245 
MET H2   H  N N 246 
MET HA   H  N N 247 
MET HB2  H  N N 248 
MET HB3  H  N N 249 
MET HG2  H  N N 250 
MET HG3  H  N N 251 
MET HE1  H  N N 252 
MET HE2  H  N N 253 
MET HE3  H  N N 254 
MET HXT  H  N N 255 
PEG C1   C  N N 256 
PEG O1   O  N N 257 
PEG C2   C  N N 258 
PEG O2   O  N N 259 
PEG C3   C  N N 260 
PEG C4   C  N N 261 
PEG O4   O  N N 262 
PEG H11  H  N N 263 
PEG H12  H  N N 264 
PEG HO1  H  N N 265 
PEG H21  H  N N 266 
PEG H22  H  N N 267 
PEG H31  H  N N 268 
PEG H32  H  N N 269 
PEG H41  H  N N 270 
PEG H42  H  N N 271 
PEG HO4  H  N N 272 
PHE N    N  N N 273 
PHE CA   C  N S 274 
PHE C    C  N N 275 
PHE O    O  N N 276 
PHE CB   C  N N 277 
PHE CG   C  Y N 278 
PHE CD1  C  Y N 279 
PHE CD2  C  Y N 280 
PHE CE1  C  Y N 281 
PHE CE2  C  Y N 282 
PHE CZ   C  Y N 283 
PHE OXT  O  N N 284 
PHE H    H  N N 285 
PHE H2   H  N N 286 
PHE HA   H  N N 287 
PHE HB2  H  N N 288 
PHE HB3  H  N N 289 
PHE HD1  H  N N 290 
PHE HD2  H  N N 291 
PHE HE1  H  N N 292 
PHE HE2  H  N N 293 
PHE HZ   H  N N 294 
PHE HXT  H  N N 295 
PRO N    N  N N 296 
PRO CA   C  N S 297 
PRO C    C  N N 298 
PRO O    O  N N 299 
PRO CB   C  N N 300 
PRO CG   C  N N 301 
PRO CD   C  N N 302 
PRO OXT  O  N N 303 
PRO H    H  N N 304 
PRO HA   H  N N 305 
PRO HB2  H  N N 306 
PRO HB3  H  N N 307 
PRO HG2  H  N N 308 
PRO HG3  H  N N 309 
PRO HD2  H  N N 310 
PRO HD3  H  N N 311 
PRO HXT  H  N N 312 
SER N    N  N N 313 
SER CA   C  N S 314 
SER C    C  N N 315 
SER O    O  N N 316 
SER CB   C  N N 317 
SER OG   O  N N 318 
SER OXT  O  N N 319 
SER H    H  N N 320 
SER H2   H  N N 321 
SER HA   H  N N 322 
SER HB2  H  N N 323 
SER HB3  H  N N 324 
SER HG   H  N N 325 
SER HXT  H  N N 326 
THR N    N  N N 327 
THR CA   C  N S 328 
THR C    C  N N 329 
THR O    O  N N 330 
THR CB   C  N R 331 
THR OG1  O  N N 332 
THR CG2  C  N N 333 
THR OXT  O  N N 334 
THR H    H  N N 335 
THR H2   H  N N 336 
THR HA   H  N N 337 
THR HB   H  N N 338 
THR HG1  H  N N 339 
THR HG21 H  N N 340 
THR HG22 H  N N 341 
THR HG23 H  N N 342 
THR HXT  H  N N 343 
TRP N    N  N N 344 
TRP CA   C  N S 345 
TRP C    C  N N 346 
TRP O    O  N N 347 
TRP CB   C  N N 348 
TRP CG   C  Y N 349 
TRP CD1  C  Y N 350 
TRP CD2  C  Y N 351 
TRP NE1  N  Y N 352 
TRP CE2  C  Y N 353 
TRP CE3  C  Y N 354 
TRP CZ2  C  Y N 355 
TRP CZ3  C  Y N 356 
TRP CH2  C  Y N 357 
TRP OXT  O  N N 358 
TRP H    H  N N 359 
TRP H2   H  N N 360 
TRP HA   H  N N 361 
TRP HB2  H  N N 362 
TRP HB3  H  N N 363 
TRP HD1  H  N N 364 
TRP HE1  H  N N 365 
TRP HE3  H  N N 366 
TRP HZ2  H  N N 367 
TRP HZ3  H  N N 368 
TRP HH2  H  N N 369 
TRP HXT  H  N N 370 
TYR N    N  N N 371 
TYR CA   C  N S 372 
TYR C    C  N N 373 
TYR O    O  N N 374 
TYR CB   C  N N 375 
TYR CG   C  Y N 376 
TYR CD1  C  Y N 377 
TYR CD2  C  Y N 378 
TYR CE1  C  Y N 379 
TYR CE2  C  Y N 380 
TYR CZ   C  Y N 381 
TYR OH   O  N N 382 
TYR OXT  O  N N 383 
TYR H    H  N N 384 
TYR H2   H  N N 385 
TYR HA   H  N N 386 
TYR HB2  H  N N 387 
TYR HB3  H  N N 388 
TYR HD1  H  N N 389 
TYR HD2  H  N N 390 
TYR HE1  H  N N 391 
TYR HE2  H  N N 392 
TYR HH   H  N N 393 
TYR HXT  H  N N 394 
VAL N    N  N N 395 
VAL CA   C  N S 396 
VAL C    C  N N 397 
VAL O    O  N N 398 
VAL CB   C  N N 399 
VAL CG1  C  N N 400 
VAL CG2  C  N N 401 
VAL OXT  O  N N 402 
VAL H    H  N N 403 
VAL H2   H  N N 404 
VAL HA   H  N N 405 
VAL HB   H  N N 406 
VAL HG11 H  N N 407 
VAL HG12 H  N N 408 
VAL HG13 H  N N 409 
VAL HG21 H  N N 410 
VAL HG22 H  N N 411 
VAL HG23 H  N N 412 
VAL HXT  H  N N 413 
# 
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  
BCT C   O1   doub N N 70  
BCT C   O2   sing N N 71  
BCT C   O3   sing N N 72  
BCT O3  HO3  sing N N 73  
CYS N   CA   sing N N 74  
CYS N   H    sing N N 75  
CYS N   H2   sing N N 76  
CYS CA  C    sing N N 77  
CYS CA  CB   sing N N 78  
CYS CA  HA   sing N N 79  
CYS C   O    doub N N 80  
CYS C   OXT  sing N N 81  
CYS CB  SG   sing N N 82  
CYS CB  HB2  sing N N 83  
CYS CB  HB3  sing N N 84  
CYS SG  HG   sing N N 85  
CYS OXT HXT  sing N N 86  
GLN N   CA   sing N N 87  
GLN N   H    sing N N 88  
GLN N   H2   sing N N 89  
GLN CA  C    sing N N 90  
GLN CA  CB   sing N N 91  
GLN CA  HA   sing N N 92  
GLN C   O    doub N N 93  
GLN C   OXT  sing N N 94  
GLN CB  CG   sing N N 95  
GLN CB  HB2  sing N N 96  
GLN CB  HB3  sing N N 97  
GLN CG  CD   sing N N 98  
GLN CG  HG2  sing N N 99  
GLN CG  HG3  sing N N 100 
GLN CD  OE1  doub N N 101 
GLN CD  NE2  sing N N 102 
GLN NE2 HE21 sing N N 103 
GLN NE2 HE22 sing N N 104 
GLN OXT HXT  sing N N 105 
GLU N   CA   sing N N 106 
GLU N   H    sing N N 107 
GLU N   H2   sing N N 108 
GLU CA  C    sing N N 109 
GLU CA  CB   sing N N 110 
GLU CA  HA   sing N N 111 
GLU C   O    doub N N 112 
GLU C   OXT  sing N N 113 
GLU CB  CG   sing N N 114 
GLU CB  HB2  sing N N 115 
GLU CB  HB3  sing N N 116 
GLU CG  CD   sing N N 117 
GLU CG  HG2  sing N N 118 
GLU CG  HG3  sing N N 119 
GLU CD  OE1  doub N N 120 
GLU CD  OE2  sing N N 121 
GLU OE2 HE2  sing N N 122 
GLU OXT HXT  sing N N 123 
GLY N   CA   sing N N 124 
GLY N   H    sing N N 125 
GLY N   H2   sing N N 126 
GLY CA  C    sing N N 127 
GLY CA  HA2  sing N N 128 
GLY CA  HA3  sing N N 129 
GLY C   O    doub N N 130 
GLY C   OXT  sing N N 131 
GLY OXT HXT  sing N N 132 
HIS N   CA   sing N N 133 
HIS N   H    sing N N 134 
HIS N   H2   sing N N 135 
HIS CA  C    sing N N 136 
HIS CA  CB   sing N N 137 
HIS CA  HA   sing N N 138 
HIS C   O    doub N N 139 
HIS C   OXT  sing N N 140 
HIS CB  CG   sing N N 141 
HIS CB  HB2  sing N N 142 
HIS CB  HB3  sing N N 143 
HIS CG  ND1  sing Y N 144 
HIS CG  CD2  doub Y N 145 
HIS ND1 CE1  doub Y N 146 
HIS ND1 HD1  sing N N 147 
HIS CD2 NE2  sing Y N 148 
HIS CD2 HD2  sing N N 149 
HIS CE1 NE2  sing Y N 150 
HIS CE1 HE1  sing N N 151 
HIS NE2 HE2  sing N N 152 
HIS OXT HXT  sing N N 153 
HOH O   H1   sing N N 154 
HOH O   H2   sing N N 155 
ILE N   CA   sing N N 156 
ILE N   H    sing N N 157 
ILE N   H2   sing N N 158 
ILE CA  C    sing N N 159 
ILE CA  CB   sing N N 160 
ILE CA  HA   sing N N 161 
ILE C   O    doub N N 162 
ILE C   OXT  sing N N 163 
ILE CB  CG1  sing N N 164 
ILE CB  CG2  sing N N 165 
ILE CB  HB   sing N N 166 
ILE CG1 CD1  sing N N 167 
ILE CG1 HG12 sing N N 168 
ILE CG1 HG13 sing N N 169 
ILE CG2 HG21 sing N N 170 
ILE CG2 HG22 sing N N 171 
ILE CG2 HG23 sing N N 172 
ILE CD1 HD11 sing N N 173 
ILE CD1 HD12 sing N N 174 
ILE CD1 HD13 sing N N 175 
ILE OXT HXT  sing N N 176 
LEU N   CA   sing N N 177 
LEU N   H    sing N N 178 
LEU N   H2   sing N N 179 
LEU CA  C    sing N N 180 
LEU CA  CB   sing N N 181 
LEU CA  HA   sing N N 182 
LEU C   O    doub N N 183 
LEU C   OXT  sing N N 184 
LEU CB  CG   sing N N 185 
LEU CB  HB2  sing N N 186 
LEU CB  HB3  sing N N 187 
LEU CG  CD1  sing N N 188 
LEU CG  CD2  sing N N 189 
LEU CG  HG   sing N N 190 
LEU CD1 HD11 sing N N 191 
LEU CD1 HD12 sing N N 192 
LEU CD1 HD13 sing N N 193 
LEU CD2 HD21 sing N N 194 
LEU CD2 HD22 sing N N 195 
LEU CD2 HD23 sing N N 196 
LEU OXT HXT  sing N N 197 
LYS N   CA   sing N N 198 
LYS N   H    sing N N 199 
LYS N   H2   sing N N 200 
LYS CA  C    sing N N 201 
LYS CA  CB   sing N N 202 
LYS CA  HA   sing N N 203 
LYS C   O    doub N N 204 
LYS C   OXT  sing N N 205 
LYS CB  CG   sing N N 206 
LYS CB  HB2  sing N N 207 
LYS CB  HB3  sing N N 208 
LYS CG  CD   sing N N 209 
LYS CG  HG2  sing N N 210 
LYS CG  HG3  sing N N 211 
LYS CD  CE   sing N N 212 
LYS CD  HD2  sing N N 213 
LYS CD  HD3  sing N N 214 
LYS CE  NZ   sing N N 215 
LYS CE  HE2  sing N N 216 
LYS CE  HE3  sing N N 217 
LYS NZ  HZ1  sing N N 218 
LYS NZ  HZ2  sing N N 219 
LYS NZ  HZ3  sing N N 220 
LYS OXT HXT  sing N N 221 
MET N   CA   sing N N 222 
MET N   H    sing N N 223 
MET N   H2   sing N N 224 
MET CA  C    sing N N 225 
MET CA  CB   sing N N 226 
MET CA  HA   sing N N 227 
MET C   O    doub N N 228 
MET C   OXT  sing N N 229 
MET CB  CG   sing N N 230 
MET CB  HB2  sing N N 231 
MET CB  HB3  sing N N 232 
MET CG  SD   sing N N 233 
MET CG  HG2  sing N N 234 
MET CG  HG3  sing N N 235 
MET SD  CE   sing N N 236 
MET CE  HE1  sing N N 237 
MET CE  HE2  sing N N 238 
MET CE  HE3  sing N N 239 
MET OXT HXT  sing N N 240 
PEG C1  O1   sing N N 241 
PEG C1  C2   sing N N 242 
PEG C1  H11  sing N N 243 
PEG C1  H12  sing N N 244 
PEG O1  HO1  sing N N 245 
PEG C2  O2   sing N N 246 
PEG C2  H21  sing N N 247 
PEG C2  H22  sing N N 248 
PEG O2  C3   sing N N 249 
PEG C3  C4   sing N N 250 
PEG C3  H31  sing N N 251 
PEG C3  H32  sing N N 252 
PEG C4  O4   sing N N 253 
PEG C4  H41  sing N N 254 
PEG C4  H42  sing N N 255 
PEG O4  HO4  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           UL1-TR001445-06-A1-S1 
_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   7LG0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8V8Q 
_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]   0.014315 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.006499 
_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]   0.011419 
_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  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 2   ? 31.963  22.346 17.361  1.00 71.38  ? 1   GLY A N   1 
ATOM   2    C  CA  . GLY A 1 2   ? 30.760  23.192 17.061  1.00 77.77  ? 1   GLY A CA  1 
ATOM   3    C  C   . GLY A 1 2   ? 29.526  22.329 16.846  1.00 73.50  ? 1   GLY A C   1 
ATOM   4    O  O   . GLY A 1 2   ? 29.649  21.086 16.992  1.00 70.67  ? 1   GLY A O   1 
ATOM   5    N  N   . SER A 1 3   ? 28.381  22.949 16.537  1.00 52.72  ? 2   SER A N   1 
ATOM   6    C  CA  A SER A 1 3   ? 27.104  22.264 16.187  0.50 47.43  ? 2   SER A CA  1 
ATOM   7    C  CA  B SER A 1 3   ? 27.131  22.222 16.187  0.50 47.66  ? 2   SER A CA  1 
ATOM   8    C  C   . SER A 1 3   ? 26.995  22.155 14.659  1.00 42.84  ? 2   SER A C   1 
ATOM   9    O  O   . SER A 1 3   ? 27.348  23.161 13.972  1.00 34.81  ? 2   SER A O   1 
ATOM   10   C  CB  A SER A 1 3   ? 25.935  23.012 16.775  0.50 53.13  ? 2   SER A CB  1 
ATOM   11   C  CB  B SER A 1 3   ? 25.949  22.852 16.860  0.50 53.68  ? 2   SER A CB  1 
ATOM   12   O  OG  A SER A 1 3   ? 24.701  22.399 16.432  0.50 49.82  ? 2   SER A OG  1 
ATOM   13   O  OG  B SER A 1 3   ? 26.047  22.680 18.269  0.50 50.17  ? 2   SER A OG  1 
ATOM   14   N  N   . HIS A 1 4   ? 26.553  21.010 14.128  1.00 33.32  ? 3   HIS A N   1 
ATOM   15   C  CA  . HIS A 1 4   ? 26.580  20.775 12.656  1.00 28.79  ? 3   HIS A CA  1 
ATOM   16   C  C   . HIS A 1 4   ? 25.374  19.946 12.217  1.00 28.86  ? 3   HIS A C   1 
ATOM   17   O  O   . HIS A 1 4   ? 24.730  19.305 13.055  1.00 29.25  ? 3   HIS A O   1 
ATOM   18   C  CB  . HIS A 1 4   ? 27.871  20.079 12.175  1.00 29.32  ? 3   HIS A CB  1 
ATOM   19   C  CG  . HIS A 1 4   ? 29.127  20.839 12.429  1.00 29.00  ? 3   HIS A CG  1 
ATOM   20   N  ND1 . HIS A 1 4   ? 29.516  21.907 11.652  1.00 30.10  ? 3   HIS A ND1 1 
ATOM   21   C  CD2 . HIS A 1 4   ? 30.032  20.749 13.431  1.00 29.46  ? 3   HIS A CD2 1 
ATOM   22   C  CE1 . HIS A 1 4   ? 30.643  22.401 12.108  1.00 35.02  ? 3   HIS A CE1 1 
ATOM   23   N  NE2 . HIS A 1 4   ? 30.969  21.721 13.208  1.00 35.20  ? 3   HIS A NE2 1 
ATOM   24   N  N   . SER A 1 5   ? 25.123  19.944 10.901  1.00 29.21  ? 4   SER A N   1 
ATOM   25   C  CA  . SER A 1 5   ? 23.999  19.221 10.279  1.00 32.76  ? 4   SER A CA  1 
ATOM   26   C  C   . SER A 1 5   ? 24.460  18.664 8.936   1.00 26.64  ? 4   SER A C   1 
ATOM   27   O  O   . SER A 1 5   ? 25.330  19.244 8.292   1.00 29.49  ? 4   SER A O   1 
ATOM   28   C  CB  . SER A 1 5   ? 22.772  20.123 10.114  1.00 33.09  ? 4   SER A CB  1 
ATOM   29   O  OG  . SER A 1 5   ? 23.094  21.224 9.254   1.00 34.60  ? 4   SER A OG  1 
ATOM   30   N  N   . MET A 1 6   ? 23.874  17.543 8.572   1.00 29.08  ? 5   MET A N   1 
ATOM   31   C  CA  . MET A 1 6   ? 23.862  17.052 7.194   1.00 26.63  ? 5   MET A CA  1 
ATOM   32   C  C   . MET A 1 6   ? 22.386  17.004 6.772   1.00 23.04  ? 5   MET A C   1 
ATOM   33   O  O   . MET A 1 6   ? 21.550  16.484 7.526   1.00 27.67  ? 5   MET A O   1 
ATOM   34   C  CB  . MET A 1 6   ? 24.516  15.681 7.095   1.00 26.74  ? 5   MET A CB  1 
ATOM   35   C  CG  . MET A 1 6   ? 24.686  15.246 5.657   1.00 27.52  ? 5   MET A CG  1 
ATOM   36   S  SD  . MET A 1 6   ? 25.392  13.586 5.484   1.00 29.09  ? 5   MET A SD  1 
ATOM   37   C  CE  . MET A 1 6   ? 24.137  12.597 6.278   1.00 30.84  ? 5   MET A CE  1 
ATOM   38   N  N   . ARG A 1 7   ? 22.085  17.557 5.604   1.00 24.19  ? 6   ARG A N   1 
ATOM   39   C  CA  . ARG A 1 7   ? 20.710  17.557 5.055   1.00 23.29  ? 6   ARG A CA  1 
ATOM   40   C  C   . ARG A 1 7   ? 20.774  17.289 3.565   1.00 20.86  ? 6   ARG A C   1 
ATOM   41   O  O   . ARG A 1 7   ? 21.606  17.893 2.884   1.00 20.95  ? 6   ARG A O   1 
ATOM   42   C  CB  . ARG A 1 7   ? 20.001  18.888 5.323   1.00 25.17  ? 6   ARG A CB  1 
ATOM   43   C  CG  . ARG A 1 7   ? 19.480  18.946 6.743   1.00 33.41  ? 6   ARG A CG  1 
ATOM   44   C  CD  . ARG A 1 7   ? 19.111  20.344 7.149   1.00 45.69  ? 6   ARG A CD  1 
ATOM   45   N  NE  . ARG A 1 7   ? 19.078  20.459 8.596   1.00 41.71  ? 6   ARG A NE  1 
ATOM   46   C  CZ  . ARG A 1 7   ? 18.407  21.392 9.254   1.00 55.39  ? 6   ARG A CZ  1 
ATOM   47   N  NH1 . ARG A 1 7   ? 17.653  22.263 8.599   1.00 48.68  ? 6   ARG A NH1 1 
ATOM   48   N  NH2 . ARG A 1 7   ? 18.461  21.424 10.573  1.00 47.08  ? 6   ARG A NH2 1 
ATOM   49   N  N   . TYR A 1 8   ? 19.812  16.512 3.107   1.00 21.77  ? 7   TYR A N   1 
ATOM   50   C  CA  . TYR A 1 8   ? 19.518  16.283 1.683   1.00 21.59  ? 7   TYR A CA  1 
ATOM   51   C  C   . TYR A 1 8   ? 18.154  16.884 1.372   1.00 19.38  ? 7   TYR A C   1 
ATOM   52   O  O   . TYR A 1 8   ? 17.214  16.714 2.144   1.00 20.67  ? 7   TYR A O   1 
ATOM   53   C  CB  . TYR A 1 8   ? 19.596  14.786 1.330   1.00 20.74  ? 7   TYR A CB  1 
ATOM   54   C  CG  . TYR A 1 8   ? 21.015  14.281 1.275   1.00 20.68  ? 7   TYR A CG  1 
ATOM   55   C  CD1 . TYR A 1 8   ? 21.638  13.817 2.421   1.00 20.73  ? 7   TYR A CD1 1 
ATOM   56   C  CD2 . TYR A 1 8   ? 21.760  14.304 0.095   1.00 23.63  ? 7   TYR A CD2 1 
ATOM   57   C  CE1 . TYR A 1 8   ? 22.947  13.386 2.398   1.00 23.51  ? 7   TYR A CE1 1 
ATOM   58   C  CE2 . TYR A 1 8   ? 23.067  13.857 0.058   1.00 20.80  ? 7   TYR A CE2 1 
ATOM   59   C  CZ  . TYR A 1 8   ? 23.666  13.405 1.213   1.00 25.21  ? 7   TYR A CZ  1 
ATOM   60   O  OH  . TYR A 1 8   ? 24.962  12.977 1.189   1.00 26.62  ? 7   TYR A OH  1 
ATOM   61   N  N   . PHE A 1 9   ? 18.096  17.562 0.238   1.00 20.86  ? 8   PHE A N   1 
ATOM   62   C  CA  . PHE A 1 9   ? 16.919  18.267 -0.314  1.00 18.03  ? 8   PHE A CA  1 
ATOM   63   C  C   . PHE A 1 9   ? 16.612  17.650 -1.673  1.00 17.59  ? 8   PHE A C   1 
ATOM   64   O  O   . PHE A 1 9   ? 17.356  17.844 -2.624  1.00 21.15  ? 8   PHE A O   1 
ATOM   65   C  CB  . PHE A 1 9   ? 17.195  19.763 -0.426  1.00 19.04  ? 8   PHE A CB  1 
ATOM   66   C  CG  . PHE A 1 9   ? 17.562  20.424 0.876   1.00 21.08  ? 8   PHE A CG  1 
ATOM   67   C  CD1 . PHE A 1 9   ? 18.834  20.302 1.393   1.00 24.24  ? 8   PHE A CD1 1 
ATOM   68   C  CD2 . PHE A 1 9   ? 16.618  21.127 1.608   1.00 21.82  ? 8   PHE A CD2 1 
ATOM   69   C  CE1 . PHE A 1 9   ? 19.174  20.926 2.589   1.00 29.33  ? 8   PHE A CE1 1 
ATOM   70   C  CE2 . PHE A 1 9   ? 16.948  21.737 2.808   1.00 22.41  ? 8   PHE A CE2 1 
ATOM   71   C  CZ  . PHE A 1 9   ? 18.237  21.647 3.291   1.00 25.90  ? 8   PHE A CZ  1 
ATOM   72   N  N   . TYR A 1 10  ? 15.533  16.905 -1.742  1.00 19.19  ? 9   TYR A N   1 
ATOM   73   C  CA  . TYR A 1 10  ? 15.095  16.245 -2.975  1.00 21.35  ? 9   TYR A CA  1 
ATOM   74   C  C   . TYR A 1 10  ? 13.903  17.003 -3.544  1.00 19.85  ? 9   TYR A C   1 
ATOM   75   O  O   . TYR A 1 10  ? 12.944  17.346 -2.808  1.00 19.35  ? 9   TYR A O   1 
ATOM   76   C  CB  . TYR A 1 10  ? 14.660  14.808 -2.685  1.00 20.19  ? 9   TYR A CB  1 
ATOM   77   C  CG  . TYR A 1 10  ? 15.681  13.876 -2.107  1.00 21.86  ? 9   TYR A CG  1 
ATOM   78   C  CD1 . TYR A 1 10  ? 17.036  14.122 -2.159  1.00 23.57  ? 9   TYR A CD1 1 
ATOM   79   C  CD2 . TYR A 1 10  ? 15.267  12.658 -1.584  1.00 23.01  ? 9   TYR A CD2 1 
ATOM   80   C  CE1 . TYR A 1 10  ? 17.956  13.192 -1.688  1.00 22.27  ? 9   TYR A CE1 1 
ATOM   81   C  CE2 . TYR A 1 10  ? 16.164  11.728 -1.092  1.00 20.52  ? 9   TYR A CE2 1 
ATOM   82   C  CZ  . TYR A 1 10  ? 17.519  11.985 -1.168  1.00 23.73  ? 9   TYR A CZ  1 
ATOM   83   O  OH  . TYR A 1 10  ? 18.397  11.082 -0.655  1.00 26.23  ? 9   TYR A OH  1 
ATOM   84   N  N   . THR A 1 11  ? 13.926  17.158 -4.862  1.00 22.97  ? 10  THR A N   1 
ATOM   85   C  CA  . THR A 1 11  ? 12.810  17.746 -5.633  1.00 22.35  ? 10  THR A CA  1 
ATOM   86   C  C   . THR A 1 11  ? 12.472  16.810 -6.791  1.00 22.44  ? 10  THR A C   1 
ATOM   87   O  O   . THR A 1 11  ? 13.346  16.589 -7.672  1.00 22.13  ? 10  THR A O   1 
ATOM   88   C  CB  . THR A 1 11  ? 13.123  19.143 -6.179  1.00 22.06  ? 10  THR A CB  1 
ATOM   89   O  OG1 . THR A 1 11  ? 13.608  19.982 -5.133  1.00 21.25  ? 10  THR A OG1 1 
ATOM   90   C  CG2 . THR A 1 11  ? 11.889  19.746 -6.812  1.00 28.19  ? 10  THR A CG2 1 
ATOM   91   N  N   . SER A 1 12  ? 11.272  16.251 -6.784  1.00 22.08  ? 11  SER A N   1 
ATOM   92   C  CA  . SER A 1 12  ? 10.787  15.451 -7.925  1.00 23.48  ? 11  SER A CA  1 
ATOM   93   C  C   . SER A 1 12  ? 9.657   16.218 -8.600  1.00 23.88  ? 11  SER A C   1 
ATOM   94   O  O   . SER A 1 12  ? 8.760   16.695 -7.901  1.00 24.15  ? 11  SER A O   1 
ATOM   95   C  CB  . SER A 1 12  ? 10.378  14.048 -7.486  1.00 22.34  ? 11  SER A CB  1 
ATOM   96   O  OG  . SER A 1 12  ? 11.510  13.244 -7.199  1.00 25.66  ? 11  SER A OG  1 
ATOM   97   N  N   . VAL A 1 13  ? 9.675   16.288 -9.933  1.00 22.77  ? 12  VAL A N   1 
ATOM   98   C  CA  . VAL A 1 13  ? 8.663   17.063 -10.689 1.00 27.31  ? 12  VAL A CA  1 
ATOM   99   C  C   . VAL A 1 13  ? 8.138   16.144 -11.788 1.00 28.08  ? 12  VAL A C   1 
ATOM   100  O  O   . VAL A 1 13  ? 8.936   15.773 -12.624 1.00 26.85  ? 12  VAL A O   1 
ATOM   101  C  CB  . VAL A 1 13  ? 9.256   18.376 -11.237 1.00 27.46  ? 12  VAL A CB  1 
ATOM   102  C  CG1 . VAL A 1 13  ? 8.186   19.147 -12.012 1.00 30.94  ? 12  VAL A CG1 1 
ATOM   103  C  CG2 . VAL A 1 13  ? 9.847   19.229 -10.111 1.00 27.38  ? 12  VAL A CG2 1 
ATOM   104  N  N   . SER A 1 14  ? 6.872   15.745 -11.729 1.00 31.01  ? 13  SER A N   1 
ATOM   105  C  CA  . SER A 1 14  ? 6.251   14.977 -12.840 1.00 35.03  ? 13  SER A CA  1 
ATOM   106  C  C   . SER A 1 14  ? 6.143   15.892 -14.070 1.00 36.93  ? 13  SER A C   1 
ATOM   107  O  O   . SER A 1 14  ? 5.874   17.116 -13.957 1.00 33.91  ? 13  SER A O   1 
ATOM   108  C  CB  . SER A 1 14  ? 4.968   14.391 -12.468 1.00 30.04  ? 13  SER A CB  1 
ATOM   109  O  OG  . SER A 1 14  ? 4.051   15.394 -12.111 1.00 33.93  ? 13  SER A OG  1 
ATOM   110  N  N   . ARG A 1 15  ? 6.414   15.331 -15.233 1.00 41.45  ? 14  ARG A N   1 
ATOM   111  C  CA  . ARG A 1 15  ? 6.350   16.063 -16.514 1.00 38.46  ? 14  ARG A CA  1 
ATOM   112  C  C   . ARG A 1 15  ? 5.440   15.204 -17.378 1.00 53.41  ? 14  ARG A C   1 
ATOM   113  O  O   . ARG A 1 15  ? 5.927   14.300 -18.051 1.00 52.01  ? 14  ARG A O   1 
ATOM   114  C  CB  . ARG A 1 15  ? 7.770   16.243 -17.053 1.00 45.33  ? 14  ARG A CB  1 
ATOM   115  C  CG  . ARG A 1 15  ? 8.627   17.218 -16.254 1.00 64.17  ? 14  ARG A CG  1 
ATOM   116  C  CD  . ARG A 1 15  ? 9.954   17.545 -16.926 1.00 63.64  ? 14  ARG A CD  1 
ATOM   117  N  NE  . ARG A 1 15  ? 10.838  16.386 -17.043 1.00 48.25  ? 14  ARG A NE  1 
ATOM   118  C  CZ  . ARG A 1 15  ? 12.148  16.448 -17.260 1.00 50.02  ? 14  ARG A CZ  1 
ATOM   119  N  NH1 . ARG A 1 15  ? 12.747  17.621 -17.363 1.00 51.61  ? 14  ARG A NH1 1 
ATOM   120  N  NH2 . ARG A 1 15  ? 12.863  15.339 -17.336 1.00 43.64  ? 14  ARG A NH2 1 
ATOM   121  N  N   . PRO A 1 16  ? 4.097   15.327 -17.251 1.00 66.29  ? 15  PRO A N   1 
ATOM   122  C  CA  . PRO A 1 16  ? 3.190   14.378 -17.896 1.00 80.07  ? 15  PRO A CA  1 
ATOM   123  C  C   . PRO A 1 16  ? 3.393   14.497 -19.412 1.00 65.21  ? 15  PRO A C   1 
ATOM   124  O  O   . PRO A 1 16  ? 3.452   15.625 -19.906 1.00 51.80  ? 15  PRO A O   1 
ATOM   125  C  CB  . PRO A 1 16  ? 1.788   14.777 -17.406 1.00 79.93  ? 15  PRO A CB  1 
ATOM   126  C  CG  . PRO A 1 16  ? 2.063   15.622 -16.174 1.00 92.28  ? 15  PRO A CG  1 
ATOM   127  C  CD  . PRO A 1 16  ? 3.368   16.338 -16.471 1.00 81.43  ? 15  PRO A CD  1 
ATOM   128  N  N   . GLY A 1 17  ? 3.604   13.347 -20.059 1.00 55.45  ? 16  GLY A N   1 
ATOM   129  C  CA  . GLY A 1 17  ? 3.906   13.209 -21.496 1.00 72.64  ? 16  GLY A CA  1 
ATOM   130  C  C   . GLY A 1 17  ? 5.374   13.446 -21.823 1.00 86.57  ? 16  GLY A C   1 
ATOM   131  O  O   . GLY A 1 17  ? 5.651   13.799 -22.991 1.00 97.91  ? 16  GLY A O   1 
ATOM   132  N  N   . ARG A 1 18  ? 6.283   13.275 -20.851 1.00 55.01  ? 17  ARG A N   1 
ATOM   133  C  CA  . ARG A 1 18  ? 7.751   13.481 -21.046 1.00 54.21  ? 17  ARG A CA  1 
ATOM   134  C  C   . ARG A 1 18  ? 8.564   12.403 -20.311 1.00 51.44  ? 17  ARG A C   1 
ATOM   135  O  O   . ARG A 1 18  ? 9.776   12.609 -20.091 1.00 56.62  ? 17  ARG A O   1 
ATOM   136  C  CB  . ARG A 1 18  ? 8.163   14.892 -20.611 1.00 57.07  ? 17  ARG A CB  1 
ATOM   137  C  CG  . ARG A 1 18  ? 7.873   15.994 -21.624 1.00 59.11  ? 17  ARG A CG  1 
ATOM   138  C  CD  . ARG A 1 18  ? 8.748   17.223 -21.377 1.00 71.55  ? 17  ARG A CD  1 
ATOM   139  N  NE  . ARG A 1 18  ? 10.181  16.916 -21.392 1.00 74.02  ? 17  ARG A NE  1 
ATOM   140  C  CZ  . ARG A 1 18  ? 11.157  17.705 -20.928 1.00 83.21  ? 17  ARG A CZ  1 
ATOM   141  N  NH1 . ARG A 1 18  ? 12.415  17.301 -21.006 1.00 72.07  ? 17  ARG A NH1 1 
ATOM   142  N  NH2 . ARG A 1 18  ? 10.885  18.883 -20.387 1.00 81.80  ? 17  ARG A NH2 1 
ATOM   143  N  N   . GLY A 1 19  ? 7.952   11.261 -19.998 1.00 47.37  ? 18  GLY A N   1 
ATOM   144  C  CA  . GLY A 1 19  ? 8.625   10.140 -19.310 1.00 51.64  ? 18  GLY A CA  1 
ATOM   145  C  C   . GLY A 1 19  ? 8.705   10.336 -17.797 1.00 40.94  ? 18  GLY A C   1 
ATOM   146  O  O   . GLY A 1 19  ? 7.743   10.859 -17.203 1.00 44.57  ? 18  GLY A O   1 
ATOM   147  N  N   . GLU A 1 20  ? 9.787   9.866  -17.185 1.00 41.78  ? 19  GLU A N   1 
ATOM   148  C  CA  . GLU A 1 20  ? 9.930   9.774  -15.713 1.00 34.35  ? 19  GLU A CA  1 
ATOM   149  C  C   . GLU A 1 20  ? 9.947   11.192 -15.145 1.00 34.45  ? 19  GLU A C   1 
ATOM   150  O  O   . GLU A 1 20  ? 10.374  12.147 -15.788 1.00 32.44  ? 19  GLU A O   1 
ATOM   151  C  CB  . GLU A 1 20  ? 11.181  8.984  -15.353 1.00 38.63  ? 19  GLU A CB  1 
ATOM   152  C  CG  . GLU A 1 20  ? 11.147  7.546  -15.827 1.00 45.29  ? 19  GLU A CG  1 
ATOM   153  C  CD  . GLU A 1 20  ? 10.091  6.726  -15.107 1.00 49.23  ? 19  GLU A CD  1 
ATOM   154  O  OE1 . GLU A 1 20  ? 10.178  6.616  -13.870 1.00 45.83  ? 19  GLU A OE1 1 
ATOM   155  O  OE2 . GLU A 1 20  ? 9.154   6.269  -15.772 1.00 45.95  ? 19  GLU A OE2 1 
ATOM   156  N  N   . PRO A 1 21  ? 9.449   11.405 -13.913 1.00 32.68  ? 20  PRO A N   1 
ATOM   157  C  CA  . PRO A 1 21  ? 9.635   12.703 -13.269 1.00 30.09  ? 20  PRO A CA  1 
ATOM   158  C  C   . PRO A 1 21  ? 11.123  13.052 -13.240 1.00 29.35  ? 20  PRO A C   1 
ATOM   159  O  O   . PRO A 1 21  ? 11.970  12.151 -13.166 1.00 31.76  ? 20  PRO A O   1 
ATOM   160  C  CB  . PRO A 1 21  ? 9.051   12.504 -11.866 1.00 30.45  ? 20  PRO A CB  1 
ATOM   161  C  CG  . PRO A 1 21  ? 7.996   11.447 -12.111 1.00 30.67  ? 20  PRO A CG  1 
ATOM   162  C  CD  . PRO A 1 21  ? 8.629   10.491 -13.113 1.00 33.38  ? 20  PRO A CD  1 
ATOM   163  N  N   . ARG A 1 22  ? 11.410  14.350 -13.273 1.00 26.04  ? 21  ARG A N   1 
ATOM   164  C  CA  . ARG A 1 22  ? 12.785  14.842 -13.038 1.00 26.50  ? 21  ARG A CA  1 
ATOM   165  C  C   . ARG A 1 22  ? 13.062  14.721 -11.541 1.00 28.65  ? 21  ARG A C   1 
ATOM   166  O  O   . ARG A 1 22  ? 12.204  15.182 -10.733 1.00 30.29  ? 21  ARG A O   1 
ATOM   167  C  CB  . ARG A 1 22  ? 12.966  16.303 -13.456 1.00 35.24  ? 21  ARG A CB  1 
ATOM   168  C  CG  . ARG A 1 22  ? 14.416  16.750 -13.334 1.00 38.31  ? 21  ARG A CG  1 
ATOM   169  C  CD  . ARG A 1 22  ? 14.688  18.033 -14.085 1.00 55.79  ? 21  ARG A CD  1 
ATOM   170  N  NE  . ARG A 1 22  ? 15.937  18.613 -13.632 1.00 46.63  ? 21  ARG A NE  1 
ATOM   171  C  CZ  . ARG A 1 22  ? 16.464  19.757 -14.062 1.00 80.29  ? 21  ARG A CZ  1 
ATOM   172  N  NH1 . ARG A 1 22  ? 17.601  20.184 -13.532 1.00 64.12  ? 21  ARG A NH1 1 
ATOM   173  N  NH2 . ARG A 1 22  ? 15.872  20.456 -15.019 1.00 82.33  ? 21  ARG A NH2 1 
ATOM   174  N  N   . PHE A 1 23  ? 14.181  14.109 -11.195 1.00 26.60  ? 22  PHE A N   1 
ATOM   175  C  CA  . PHE A 1 23  ? 14.664  14.009 -9.800  1.00 25.47  ? 22  PHE A CA  1 
ATOM   176  C  C   . PHE A 1 23  ? 15.949  14.826 -9.664  1.00 22.40  ? 22  PHE A C   1 
ATOM   177  O  O   . PHE A 1 23  ? 16.918  14.553 -10.370 1.00 25.51  ? 22  PHE A O   1 
ATOM   178  C  CB  . PHE A 1 23  ? 14.853  12.558 -9.392  1.00 25.54  ? 22  PHE A CB  1 
ATOM   179  C  CG  . PHE A 1 23  ? 15.376  12.424 -7.990  1.00 23.19  ? 22  PHE A CG  1 
ATOM   180  C  CD1 . PHE A 1 23  ? 14.516  12.451 -6.901  1.00 23.25  ? 22  PHE A CD1 1 
ATOM   181  C  CD2 . PHE A 1 23  ? 16.731  12.284 -7.758  1.00 24.23  ? 22  PHE A CD2 1 
ATOM   182  C  CE1 . PHE A 1 23  ? 15.000  12.340 -5.614  1.00 21.69  ? 22  PHE A CE1 1 
ATOM   183  C  CE2 . PHE A 1 23  ? 17.209  12.152 -6.469  1.00 23.19  ? 22  PHE A CE2 1 
ATOM   184  C  CZ  . PHE A 1 23  ? 16.343  12.194 -5.400  1.00 20.40  ? 22  PHE A CZ  1 
ATOM   185  N  N   . ILE A 1 24  ? 15.949  15.769 -8.719  1.00 23.38  ? 23  ILE A N   1 
ATOM   186  C  CA  . ILE A 1 24  ? 17.137  16.550 -8.323  1.00 20.83  ? 23  ILE A CA  1 
ATOM   187  C  C   . ILE A 1 24  ? 17.382  16.321 -6.847  1.00 20.88  ? 23  ILE A C   1 
ATOM   188  O  O   . ILE A 1 24  ? 16.424  16.401 -6.095  1.00 24.71  ? 23  ILE A O   1 
ATOM   189  C  CB  . ILE A 1 24  ? 16.938  18.052 -8.620  1.00 30.44  ? 23  ILE A CB  1 
ATOM   190  C  CG1 . ILE A 1 24  ? 16.677  18.297 -10.108 1.00 39.86  ? 23  ILE A CG1 1 
ATOM   191  C  CG2 . ILE A 1 24  ? 18.145  18.836 -8.103  1.00 42.81  ? 23  ILE A CG2 1 
ATOM   192  C  CD1 . ILE A 1 24  ? 16.267  19.726 -10.436 1.00 53.62  ? 23  ILE A CD1 1 
ATOM   193  N  N   . SER A 1 25  ? 18.645  16.130 -6.476  1.00 19.76  ? 24  SER A N   1 
ATOM   194  C  CA  . SER A 1 25  ? 19.101  16.110 -5.068  1.00 22.36  ? 24  SER A CA  1 
ATOM   195  C  C   . SER A 1 25  ? 20.239  17.094 -4.906  1.00 23.57  ? 24  SER A C   1 
ATOM   196  O  O   . SER A 1 25  ? 21.125  17.138 -5.775  1.00 23.59  ? 24  SER A O   1 
ATOM   197  C  CB  . SER A 1 25  ? 19.581  14.754 -4.635  1.00 22.02  ? 24  SER A CB  1 
ATOM   198  O  OG  . SER A 1 25  ? 20.045  14.794 -3.283  1.00 25.15  ? 24  SER A OG  1 
ATOM   199  N  N   . VAL A 1 26  ? 20.218  17.826 -3.806  1.00 21.55  ? 25  VAL A N   1 
ATOM   200  C  CA  . VAL A 1 26  ? 21.399  18.581 -3.326  1.00 22.64  ? 25  VAL A CA  1 
ATOM   201  C  C   . VAL A 1 26  ? 21.635  18.171 -1.879  1.00 21.31  ? 25  VAL A C   1 
ATOM   202  O  O   . VAL A 1 26  ? 20.673  17.975 -1.155  1.00 23.90  ? 25  VAL A O   1 
ATOM   203  C  CB  . VAL A 1 26  ? 21.236  20.097 -3.517  1.00 22.40  ? 25  VAL A CB  1 
ATOM   204  C  CG1 . VAL A 1 26  ? 21.316  20.481 -4.983  1.00 24.55  ? 25  VAL A CG1 1 
ATOM   205  C  CG2 . VAL A 1 26  ? 19.975  20.634 -2.869  1.00 21.39  ? 25  VAL A CG2 1 
ATOM   206  N  N   . GLY A 1 27  ? 22.907  18.041 -1.491  1.00 22.28  ? 26  GLY A N   1 
ATOM   207  C  CA  . GLY A 1 27  ? 23.340  17.638 -0.147  1.00 20.23  ? 26  GLY A CA  1 
ATOM   208  C  C   . GLY A 1 27  ? 24.154  18.747 0.457   1.00 22.63  ? 26  GLY A C   1 
ATOM   209  O  O   . GLY A 1 27  ? 24.953  19.339 -0.275  1.00 25.10  ? 26  GLY A O   1 
ATOM   210  N  N   . TYR A 1 28  ? 23.944  19.019 1.742   1.00 21.56  ? 27  TYR A N   1 
ATOM   211  C  CA  . TYR A 1 28  ? 24.610  20.113 2.492   1.00 22.77  ? 27  TYR A CA  1 
ATOM   212  C  C   . TYR A 1 28  ? 25.220  19.559 3.768   1.00 21.79  ? 27  TYR A C   1 
ATOM   213  O  O   . TYR A 1 28  ? 24.628  18.674 4.370   1.00 23.50  ? 27  TYR A O   1 
ATOM   214  C  CB  . TYR A 1 28  ? 23.591  21.194 2.889   1.00 23.73  ? 27  TYR A CB  1 
ATOM   215  C  CG  . TYR A 1 28  ? 23.137  22.073 1.752   1.00 26.77  ? 27  TYR A CG  1 
ATOM   216  C  CD1 . TYR A 1 28  ? 22.163  21.640 0.870   1.00 29.30  ? 27  TYR A CD1 1 
ATOM   217  C  CD2 . TYR A 1 28  ? 23.678  23.333 1.543   1.00 28.83  ? 27  TYR A CD2 1 
ATOM   218  C  CE1 . TYR A 1 28  ? 21.731  22.430 -0.182  1.00 25.25  ? 27  TYR A CE1 1 
ATOM   219  C  CE2 . TYR A 1 28  ? 23.251  24.139 0.496   1.00 31.96  ? 27  TYR A CE2 1 
ATOM   220  C  CZ  . TYR A 1 28  ? 22.271  23.680 -0.371  1.00 28.43  ? 27  TYR A CZ  1 
ATOM   221  O  OH  . TYR A 1 28  ? 21.848  24.404 -1.435  1.00 32.11  ? 27  TYR A OH  1 
ATOM   222  N  N   . VAL A 1 29  ? 26.385  20.077 4.152   1.00 23.81  ? 28  VAL A N   1 
ATOM   223  C  CA  . VAL A 1 29  ? 26.813  20.133 5.568   1.00 25.53  ? 28  VAL A CA  1 
ATOM   224  C  C   . VAL A 1 29  ? 26.691  21.594 6.007   1.00 20.27  ? 28  VAL A C   1 
ATOM   225  O  O   . VAL A 1 29  ? 27.332  22.450 5.382   1.00 26.01  ? 28  VAL A O   1 
ATOM   226  C  CB  . VAL A 1 29  ? 28.243  19.598 5.768   1.00 28.53  ? 28  VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 29  ? 28.680  19.799 7.213   1.00 28.05  ? 28  VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 29  ? 28.363  18.127 5.376   1.00 27.39  ? 28  VAL A CG2 1 
ATOM   229  N  N   . ASP A 1 30  ? 25.876  21.842 7.031   1.00 24.12  ? 29  ASP A N   1 
ATOM   230  C  CA  . ASP A 1 30  ? 25.511  23.210 7.461   1.00 26.99  ? 29  ASP A CA  1 
ATOM   231  C  C   . ASP A 1 30  ? 25.040  23.990 6.224   1.00 26.43  ? 29  ASP A C   1 
ATOM   232  O  O   . ASP A 1 30  ? 24.148  23.474 5.541   1.00 27.51  ? 29  ASP A O   1 
ATOM   233  C  CB  . ASP A 1 30  ? 26.698  23.827 8.185   1.00 26.70  ? 29  ASP A CB  1 
ATOM   234  C  CG  . ASP A 1 30  ? 27.204  22.952 9.312   1.00 31.66  ? 29  ASP A CG  1 
ATOM   235  O  OD1 . ASP A 1 30  ? 26.361  22.302 9.961   1.00 31.39  ? 29  ASP A OD1 1 
ATOM   236  O  OD2 . ASP A 1 30  ? 28.441  22.908 9.491   1.00 33.31  ? 29  ASP A OD2 1 
ATOM   237  N  N   . ASP A 1 31  ? 25.654  25.132 5.888   1.00 25.10  ? 30  ASP A N   1 
ATOM   238  C  CA  . ASP A 1 31  ? 25.200  25.959 4.741   1.00 23.30  ? 30  ASP A CA  1 
ATOM   239  C  C   . ASP A 1 31  ? 26.146  25.737 3.563   1.00 24.07  ? 30  ASP A C   1 
ATOM   240  O  O   . ASP A 1 31  ? 26.212  26.604 2.643   1.00 26.47  ? 30  ASP A O   1 
ATOM   241  C  CB  . ASP A 1 31  ? 25.072  27.408 5.181   1.00 24.59  ? 30  ASP A CB  1 
ATOM   242  C  CG  . ASP A 1 31  ? 23.962  27.615 6.203   1.00 25.33  ? 30  ASP A CG  1 
ATOM   243  O  OD1 . ASP A 1 31  ? 22.856  27.076 5.995   1.00 28.90  ? 30  ASP A OD1 1 
ATOM   244  O  OD2 . ASP A 1 31  ? 24.189  28.327 7.184   1.00 26.05  ? 30  ASP A OD2 1 
ATOM   245  N  N   . THR A 1 32  ? 26.902  24.637 3.584   1.00 23.78  ? 31  THR A N   1 
ATOM   246  C  CA  . THR A 1 32  ? 27.843  24.290 2.496   1.00 22.57  ? 31  THR A CA  1 
ATOM   247  C  C   . THR A 1 32  ? 27.268  23.155 1.635   1.00 26.97  ? 31  THR A C   1 
ATOM   248  O  O   . THR A 1 32  ? 27.247  22.033 2.092   1.00 23.82  ? 31  THR A O   1 
ATOM   249  C  CB  . THR A 1 32  ? 29.234  23.949 3.036   1.00 25.51  ? 31  THR A CB  1 
ATOM   250  O  OG1 . THR A 1 32  ? 29.732  25.089 3.736   1.00 25.73  ? 31  THR A OG1 1 
ATOM   251  C  CG2 . THR A 1 32  ? 30.207  23.639 1.926   1.00 27.32  ? 31  THR A CG2 1 
ATOM   252  N  N   . GLN A 1 33  ? 26.871  23.454 0.405   1.00 24.85  ? 32  GLN A N   1 
ATOM   253  C  CA  . GLN A 1 33  ? 26.462  22.416 -0.590  1.00 24.58  ? 32  GLN A CA  1 
ATOM   254  C  C   . GLN A 1 33  ? 27.693  21.593 -0.958  1.00 28.57  ? 32  GLN A C   1 
ATOM   255  O  O   . GLN A 1 33  ? 28.727  22.204 -1.275  1.00 26.25  ? 32  GLN A O   1 
ATOM   256  C  CB  . GLN A 1 33  ? 25.912  23.002 -1.881  1.00 27.17  ? 32  GLN A CB  1 
ATOM   257  C  CG  . GLN A 1 33  ? 25.091  21.970 -2.659  1.00 27.06  ? 32  GLN A CG  1 
ATOM   258  C  CD  . GLN A 1 33  ? 24.848  22.400 -4.080  1.00 27.30  ? 32  GLN A CD  1 
ATOM   259  O  OE1 . GLN A 1 33  ? 24.704  23.585 -4.344  1.00 28.07  ? 32  GLN A OE1 1 
ATOM   260  N  NE2 . GLN A 1 33  ? 24.727  21.435 -4.986  1.00 27.71  ? 32  GLN A NE2 1 
ATOM   261  N  N   . PHE A 1 34  ? 27.611  20.262 -0.933  1.00 25.34  ? 33  PHE A N   1 
ATOM   262  C  CA  . PHE A 1 34  ? 28.794  19.434 -1.289  1.00 28.94  ? 33  PHE A CA  1 
ATOM   263  C  C   . PHE A 1 34  ? 28.499  18.460 -2.432  1.00 28.20  ? 33  PHE A C   1 
ATOM   264  O  O   . PHE A 1 34  ? 29.466  18.013 -3.039  1.00 27.37  ? 33  PHE A O   1 
ATOM   265  C  CB  . PHE A 1 34  ? 29.393  18.764 -0.055  1.00 27.22  ? 33  PHE A CB  1 
ATOM   266  C  CG  . PHE A 1 34  ? 28.580  17.658 0.564   1.00 26.32  ? 33  PHE A CG  1 
ATOM   267  C  CD1 . PHE A 1 34  ? 27.531  17.941 1.425   1.00 21.35  ? 33  PHE A CD1 1 
ATOM   268  C  CD2 . PHE A 1 34  ? 28.953  16.336 0.396   1.00 28.46  ? 33  PHE A CD2 1 
ATOM   269  C  CE1 . PHE A 1 34  ? 26.807  16.911 2.027   1.00 25.57  ? 33  PHE A CE1 1 
ATOM   270  C  CE2 . PHE A 1 34  ? 28.237  15.309 0.996   1.00 27.21  ? 33  PHE A CE2 1 
ATOM   271  C  CZ  . PHE A 1 34  ? 27.148  15.595 1.789   1.00 28.70  ? 33  PHE A CZ  1 
ATOM   272  N  N   . VAL A 1 35  ? 27.238  18.147 -2.735  1.00 23.99  ? 34  VAL A N   1 
ATOM   273  C  CA  . VAL A 1 35  ? 26.908  17.208 -3.839  1.00 25.20  ? 34  VAL A CA  1 
ATOM   274  C  C   . VAL A 1 35  ? 25.633  17.647 -4.558  1.00 23.77  ? 34  VAL A C   1 
ATOM   275  O  O   . VAL A 1 35  ? 24.771  18.386 -3.989  1.00 24.37  ? 34  VAL A O   1 
ATOM   276  C  CB  . VAL A 1 35  ? 26.795  15.753 -3.341  1.00 24.80  ? 34  VAL A CB  1 
ATOM   277  C  CG1 . VAL A 1 35  ? 28.163  15.174 -2.940  1.00 24.68  ? 34  VAL A CG1 1 
ATOM   278  C  CG2 . VAL A 1 35  ? 25.781  15.618 -2.218  1.00 26.84  ? 34  VAL A CG2 1 
ATOM   279  N  N   . ARG A 1 36  ? 25.514  17.193 -5.789  1.00 21.46  ? 35  ARG A N   1 
ATOM   280  C  CA  . ARG A 1 36  ? 24.244  17.287 -6.530  1.00 24.91  ? 35  ARG A CA  1 
ATOM   281  C  C   . ARG A 1 36  ? 24.047  16.004 -7.334  1.00 23.54  ? 35  ARG A C   1 
ATOM   282  O  O   . ARG A 1 36  ? 25.037  15.294 -7.646  1.00 25.47  ? 35  ARG A O   1 
ATOM   283  C  CB  . ARG A 1 36  ? 24.219  18.492 -7.467  1.00 26.60  ? 35  ARG A CB  1 
ATOM   284  C  CG  . ARG A 1 36  ? 25.285  18.438 -8.544  1.00 28.48  ? 35  ARG A CG  1 
ATOM   285  C  CD  . ARG A 1 36  ? 25.146  19.587 -9.527  1.00 29.95  ? 35  ARG A CD  1 
ATOM   286  N  NE  . ARG A 1 36  ? 26.086  19.502 -10.642 1.00 28.30  ? 35  ARG A NE  1 
ATOM   287  C  CZ  . ARG A 1 36  ? 26.472  20.530 -11.405 1.00 36.66  ? 35  ARG A CZ  1 
ATOM   288  N  NH1 . ARG A 1 36  ? 26.016  21.749 -11.164 1.00 26.96  ? 35  ARG A NH1 1 
ATOM   289  N  NH2 . ARG A 1 36  ? 27.310  20.330 -12.411 1.00 31.80  ? 35  ARG A NH2 1 
ATOM   290  N  N   . PHE A 1 37  ? 22.797  15.756 -7.688  1.00 25.01  ? 36  PHE A N   1 
ATOM   291  C  CA  . PHE A 1 37  ? 22.409  14.701 -8.645  1.00 22.47  ? 36  PHE A CA  1 
ATOM   292  C  C   . PHE A 1 37  ? 21.219  15.239 -9.421  1.00 23.60  ? 36  PHE A C   1 
ATOM   293  O  O   . PHE A 1 37  ? 20.354  15.834 -8.817  1.00 23.22  ? 36  PHE A O   1 
ATOM   294  C  CB  . PHE A 1 37  ? 22.070  13.405 -7.919  1.00 23.35  ? 36  PHE A CB  1 
ATOM   295  C  CG  . PHE A 1 37  ? 21.557  12.361 -8.881  1.00 23.38  ? 36  PHE A CG  1 
ATOM   296  C  CD1 . PHE A 1 37  ? 20.207  12.297 -9.210  1.00 22.45  ? 36  PHE A CD1 1 
ATOM   297  C  CD2 . PHE A 1 37  ? 22.444  11.505 -9.525  1.00 23.05  ? 36  PHE A CD2 1 
ATOM   298  C  CE1 . PHE A 1 37  ? 19.731  11.343 -10.108 1.00 28.26  ? 36  PHE A CE1 1 
ATOM   299  C  CE2 . PHE A 1 37  ? 21.961  10.539 -10.400 1.00 28.70  ? 36  PHE A CE2 1 
ATOM   300  C  CZ  . PHE A 1 37  ? 20.616  10.486 -10.722 1.00 26.47  ? 36  PHE A CZ  1 
ATOM   301  N  N   . ASP A 1 38  ? 21.190  15.029 -10.721 1.00 22.73  ? 37  ASP A N   1 
ATOM   302  C  CA  . ASP A 1 38  ? 20.082  15.516 -11.580 1.00 25.92  ? 37  ASP A CA  1 
ATOM   303  C  C   . ASP A 1 38  ? 19.804  14.426 -12.615 1.00 24.01  ? 37  ASP A C   1 
ATOM   304  O  O   . ASP A 1 38  ? 20.722  14.127 -13.413 1.00 27.83  ? 37  ASP A O   1 
ATOM   305  C  CB  . ASP A 1 38  ? 20.461  16.875 -12.168 1.00 27.04  ? 37  ASP A CB  1 
ATOM   306  C  CG  . ASP A 1 38  ? 19.443  17.497 -13.101 1.00 33.93  ? 37  ASP A CG  1 
ATOM   307  O  OD1 . ASP A 1 38  ? 18.429  16.858 -13.399 1.00 31.29  ? 37  ASP A OD1 1 
ATOM   308  O  OD2 . ASP A 1 38  ? 19.675  18.633 -13.507 1.00 36.69  ? 37  ASP A OD2 1 
ATOM   309  N  N   . SER A 1 39  ? 18.630  13.807 -12.539 1.00 26.82  ? 38  SER A N   1 
ATOM   310  C  CA  . SER A 1 39  ? 18.144  12.752 -13.464 1.00 27.02  ? 38  SER A CA  1 
ATOM   311  C  C   . SER A 1 39  ? 18.154  13.219 -14.935 1.00 39.91  ? 38  SER A C   1 
ATOM   312  O  O   . SER A 1 39  ? 18.164  12.334 -15.774 1.00 41.13  ? 38  SER A O   1 
ATOM   313  C  CB  . SER A 1 39  ? 16.793  12.274 -13.031 1.00 32.15  ? 38  SER A CB  1 
ATOM   314  O  OG  . SER A 1 39  ? 15.787  13.250 -13.272 1.00 31.60  ? 38  SER A OG  1 
ATOM   315  N  N   . ASP A 1 40  ? 18.187  14.530 -15.219 1.00 32.83  ? 39  ASP A N   1 
ATOM   316  C  CA  . ASP A 1 40  ? 18.242  15.168 -16.575 1.00 46.26  ? 39  ASP A CA  1 
ATOM   317  C  C   . ASP A 1 40  ? 19.660  15.481 -17.073 1.00 42.93  ? 39  ASP A C   1 
ATOM   318  O  O   . ASP A 1 40  ? 19.794  15.895 -18.242 1.00 56.11  ? 39  ASP A O   1 
ATOM   319  C  CB  . ASP A 1 40  ? 17.651  16.579 -16.598 1.00 39.46  ? 39  ASP A CB  1 
ATOM   320  C  CG  . ASP A 1 40  ? 16.206  16.663 -17.022 1.00 50.81  ? 39  ASP A CG  1 
ATOM   321  O  OD1 . ASP A 1 40  ? 15.571  15.604 -17.127 1.00 43.15  ? 39  ASP A OD1 1 
ATOM   322  O  OD2 . ASP A 1 40  ? 15.741  17.804 -17.251 1.00 60.71  ? 39  ASP A OD2 1 
ATOM   323  N  N   . ALA A 1 41  ? 20.663  15.330 -16.227 1.00 47.99  ? 40  ALA A N   1 
ATOM   324  C  CA  . ALA A 1 41  ? 22.031  15.691 -16.636 1.00 48.88  ? 40  ALA A CA  1 
ATOM   325  C  C   . ALA A 1 41  ? 22.631  14.626 -17.548 1.00 59.99  ? 40  ALA A C   1 
ATOM   326  O  O   . ALA A 1 41  ? 22.097  13.523 -17.648 1.00 46.28  ? 40  ALA A O   1 
ATOM   327  C  CB  . ALA A 1 41  ? 22.889  15.936 -15.436 1.00 48.00  ? 40  ALA A CB  1 
ATOM   328  N  N   . ALA A 1 42  ? 23.736  14.989 -18.192 1.00 72.14  ? 41  ALA A N   1 
ATOM   329  C  CA  . ALA A 1 42  ? 24.435  14.028 -19.062 1.00 82.04  ? 41  ALA A CA  1 
ATOM   330  C  C   . ALA A 1 42  ? 25.086  12.980 -18.159 1.00 67.10  ? 41  ALA A C   1 
ATOM   331  O  O   . ALA A 1 42  ? 25.815  13.367 -17.236 1.00 63.23  ? 41  ALA A O   1 
ATOM   332  C  CB  . ALA A 1 42  ? 25.441  14.748 -19.922 1.00 79.77  ? 41  ALA A CB  1 
ATOM   333  N  N   . SER A 1 43  ? 24.752  11.734 -18.501 1.00 49.42  ? 42  SER A N   1 
ATOM   334  C  CA  . SER A 1 43  ? 25.168  10.515 -17.779 1.00 67.51  ? 42  SER A CA  1 
ATOM   335  C  C   . SER A 1 43  ? 24.932  10.769 -16.294 1.00 47.66  ? 42  SER A C   1 
ATOM   336  O  O   . SER A 1 43  ? 25.930  10.852 -15.592 1.00 47.62  ? 42  SER A O   1 
ATOM   337  C  CB  . SER A 1 43  ? 26.590  10.212 -18.077 1.00 72.76  ? 42  SER A CB  1 
ATOM   338  O  OG  . SER A 1 43  ? 26.766  10.122 -19.476 1.00 70.33  ? 42  SER A OG  1 
ATOM   339  N  N   . PRO A 1 44  ? 23.665  10.805 -15.806 1.00 42.99  ? 43  PRO A N   1 
ATOM   340  C  CA  . PRO A 1 44  ? 23.377  11.186 -14.430 1.00 29.74  ? 43  PRO A CA  1 
ATOM   341  C  C   . PRO A 1 44  ? 24.222  10.413 -13.422 1.00 32.54  ? 43  PRO A C   1 
ATOM   342  O  O   . PRO A 1 44  ? 24.230  9.233  -13.390 1.00 31.01  ? 43  PRO A O   1 
ATOM   343  C  CB  . PRO A 1 44  ? 21.919  10.792 -14.210 1.00 34.83  ? 43  PRO A CB  1 
ATOM   344  C  CG  . PRO A 1 44  ? 21.322  10.854 -15.578 1.00 42.81  ? 43  PRO A CG  1 
ATOM   345  C  CD  . PRO A 1 44  ? 22.444  10.550 -16.547 1.00 40.90  ? 43  PRO A CD  1 
ATOM   346  N  N   . ARG A 1 45  ? 24.936  11.200 -12.640 1.00 30.66  ? 44  ARG A N   1 
ATOM   347  C  CA  . ARG A 1 45  ? 25.858  10.697 -11.615 1.00 27.02  ? 44  ARG A CA  1 
ATOM   348  C  C   . ARG A 1 45  ? 25.906  11.737 -10.501 1.00 28.37  ? 44  ARG A C   1 
ATOM   349  O  O   . ARG A 1 45  ? 25.734  12.896 -10.800 1.00 31.84  ? 44  ARG A O   1 
ATOM   350  C  CB  . ARG A 1 45  ? 27.235  10.592 -12.269 1.00 31.22  ? 44  ARG A CB  1 
ATOM   351  C  CG  . ARG A 1 45  ? 28.246  9.787  -11.476 1.00 50.33  ? 44  ARG A CG  1 
ATOM   352  C  CD  . ARG A 1 45  ? 29.128  8.908  -12.338 1.00 52.08  ? 44  ARG A CD  1 
ATOM   353  N  NE  . ARG A 1 45  ? 30.138  8.224  -11.553 1.00 51.35  ? 44  ARG A NE  1 
ATOM   354  C  CZ  . ARG A 1 45  ? 31.285  8.767  -11.177 1.00 55.33  ? 44  ARG A CZ  1 
ATOM   355  N  NH1 . ARG A 1 45  ? 31.591  10.000 -11.530 1.00 48.61  ? 44  ARG A NH1 1 
ATOM   356  N  NH2 . ARG A 1 45  ? 32.139  8.070  -10.460 1.00 58.03  ? 44  ARG A NH2 1 
ATOM   357  N  N   . GLU A 1 46  ? 26.194  11.319 -9.279  1.00 24.42  ? 45  GLU A N   1 
ATOM   358  C  CA  . GLU A 1 46  ? 26.393  12.318 -8.214  1.00 23.56  ? 45  GLU A CA  1 
ATOM   359  C  C   . GLU A 1 46  ? 27.677  13.074 -8.557  1.00 27.54  ? 45  GLU A C   1 
ATOM   360  O  O   . GLU A 1 46  ? 28.630  12.446 -8.970  1.00 27.00  ? 45  GLU A O   1 
ATOM   361  C  CB  . GLU A 1 46  ? 26.577  11.646 -6.867  1.00 24.87  ? 45  GLU A CB  1 
ATOM   362  C  CG  . GLU A 1 46  ? 26.451  12.616 -5.725  1.00 24.48  ? 45  GLU A CG  1 
ATOM   363  C  CD  . GLU A 1 46  ? 26.739  11.999 -4.372  1.00 23.74  ? 45  GLU A CD  1 
ATOM   364  O  OE1 . GLU A 1 46  ? 26.012  12.277 -3.438  1.00 25.56  ? 45  GLU A OE1 1 
ATOM   365  O  OE2 . GLU A 1 46  ? 27.685  11.251 -4.283  1.00 27.06  ? 45  GLU A OE2 1 
ATOM   366  N  N   . GLU A 1 47  ? 27.690  14.375 -8.309  1.00 28.50  ? 46  GLU A N   1 
ATOM   367  C  CA  . GLU A 1 47  ? 28.850  15.241 -8.641  1.00 23.74  ? 46  GLU A CA  1 
ATOM   368  C  C   . GLU A 1 47  ? 29.212  16.068 -7.428  1.00 27.41  ? 46  GLU A C   1 
ATOM   369  O  O   . GLU A 1 47  ? 28.337  16.538 -6.697  1.00 25.81  ? 46  GLU A O   1 
ATOM   370  C  CB  . GLU A 1 47  ? 28.524  16.167 -9.813  1.00 29.05  ? 46  GLU A CB  1 
ATOM   371  C  CG  . GLU A 1 47  ? 28.232  15.407 -11.085 1.00 28.58  ? 46  GLU A CG  1 
ATOM   372  C  CD  . GLU A 1 47  ? 27.772  16.210 -12.277 1.00 39.17  ? 46  GLU A CD  1 
ATOM   373  O  OE1 . GLU A 1 47  ? 27.384  17.390 -12.102 1.00 37.00  ? 46  GLU A OE1 1 
ATOM   374  O  OE2 . GLU A 1 47  ? 27.801  15.636 -13.389 1.00 39.46  ? 46  GLU A OE2 1 
ATOM   375  N  N   . PRO A 1 48  ? 30.517  16.351 -7.266  1.00 33.47  ? 47  PRO A N   1 
ATOM   376  C  CA  . PRO A 1 48  ? 30.998  17.158 -6.152  1.00 29.28  ? 47  PRO A CA  1 
ATOM   377  C  C   . PRO A 1 48  ? 30.710  18.653 -6.376  1.00 27.02  ? 47  PRO A C   1 
ATOM   378  O  O   . PRO A 1 48  ? 30.741  19.166 -7.491  1.00 26.75  ? 47  PRO A O   1 
ATOM   379  C  CB  . PRO A 1 48  ? 32.501  16.848 -6.179  1.00 29.41  ? 47  PRO A CB  1 
ATOM   380  C  CG  . PRO A 1 48  ? 32.808  16.682 -7.634  1.00 31.26  ? 47  PRO A CG  1 
ATOM   381  C  CD  . PRO A 1 48  ? 31.603  15.922 -8.168  1.00 33.79  ? 47  PRO A CD  1 
ATOM   382  N  N   . ARG A 1 49  ? 30.412  19.362 -5.300  1.00 28.46  ? 48  ARG A N   1 
ATOM   383  C  CA  . ARG A 1 49  ? 30.128  20.813 -5.374  1.00 27.00  ? 48  ARG A CA  1 
ATOM   384  C  C   . ARG A 1 49  ? 30.865  21.557 -4.266  1.00 27.76  ? 48  ARG A C   1 
ATOM   385  O  O   . ARG A 1 49  ? 30.637  22.789 -4.159  1.00 31.18  ? 48  ARG A O   1 
ATOM   386  C  CB  . ARG A 1 49  ? 28.620  21.024 -5.265  1.00 25.93  ? 48  ARG A CB  1 
ATOM   387  C  CG  . ARG A 1 49  ? 27.863  20.462 -6.452  1.00 25.76  ? 48  ARG A CG  1 
ATOM   388  C  CD  . ARG A 1 49  ? 28.197  21.175 -7.737  1.00 24.09  ? 48  ARG A CD  1 
ATOM   389  N  NE  . ARG A 1 49  ? 27.415  22.391 -7.893  1.00 31.41  ? 48  ARG A NE  1 
ATOM   390  C  CZ  . ARG A 1 49  ? 27.679  23.376 -8.752  1.00 28.06  ? 48  ARG A CZ  1 
ATOM   391  N  NH1 . ARG A 1 49  ? 28.715  23.294 -9.561  1.00 38.05  ? 48  ARG A NH1 1 
ATOM   392  N  NH2 . ARG A 1 49  ? 26.877  24.421 -8.828  1.00 33.06  ? 48  ARG A NH2 1 
ATOM   393  N  N   . ALA A 1 50  ? 31.705  20.845 -3.511  1.00 27.78  ? 49  ALA A N   1 
ATOM   394  C  CA  . ALA A 1 50  ? 32.628  21.434 -2.512  1.00 32.83  ? 49  ALA A CA  1 
ATOM   395  C  C   . ALA A 1 50  ? 33.996  20.776 -2.645  1.00 37.25  ? 49  ALA A C   1 
ATOM   396  O  O   . ALA A 1 50  ? 34.094  19.616 -3.041  1.00 30.30  ? 49  ALA A O   1 
ATOM   397  C  CB  . ALA A 1 50  ? 32.089  21.252 -1.130  1.00 34.36  ? 49  ALA A CB  1 
ATOM   398  N  N   . PRO A 1 51  ? 35.101  21.515 -2.393  1.00 39.86  ? 50  PRO A N   1 
ATOM   399  C  CA  . PRO A 1 51  ? 36.433  20.976 -2.653  1.00 38.49  ? 50  PRO A CA  1 
ATOM   400  C  C   . PRO A 1 51  ? 36.769  19.730 -1.815  1.00 32.85  ? 50  PRO A C   1 
ATOM   401  O  O   . PRO A 1 51  ? 37.417  18.880 -2.346  1.00 34.79  ? 50  PRO A O   1 
ATOM   402  C  CB  . PRO A 1 51  ? 37.398  22.152 -2.367  1.00 43.28  ? 50  PRO A CB  1 
ATOM   403  C  CG  . PRO A 1 51  ? 36.583  23.163 -1.572  1.00 43.80  ? 50  PRO A CG  1 
ATOM   404  C  CD  . PRO A 1 51  ? 35.128  22.923 -1.947  1.00 39.60  ? 50  PRO A CD  1 
ATOM   405  N  N   . TRP A 1 52  ? 36.301  19.637 -0.565  1.00 32.19  ? 51  TRP A N   1 
ATOM   406  C  CA  . TRP A 1 52  ? 36.746  18.602 0.404   1.00 35.07  ? 51  TRP A CA  1 
ATOM   407  C  C   . TRP A 1 52  ? 36.066  17.243 0.143   1.00 38.51  ? 51  TRP A C   1 
ATOM   408  O  O   . TRP A 1 52  ? 36.486  16.233 0.752   1.00 33.63  ? 51  TRP A O   1 
ATOM   409  C  CB  . TRP A 1 52  ? 36.499  19.068 1.837   1.00 39.53  ? 51  TRP A CB  1 
ATOM   410  C  CG  . TRP A 1 52  ? 35.177  19.733 2.048   1.00 34.04  ? 51  TRP A CG  1 
ATOM   411  C  CD1 . TRP A 1 52  ? 34.920  21.068 2.070   1.00 37.45  ? 51  TRP A CD1 1 
ATOM   412  C  CD2 . TRP A 1 52  ? 33.921  19.080 2.271   1.00 27.24  ? 51  TRP A CD2 1 
ATOM   413  N  NE1 . TRP A 1 52  ? 33.598  21.294 2.326   1.00 31.70  ? 51  TRP A NE1 1 
ATOM   414  C  CE2 . TRP A 1 52  ? 32.954  20.097 2.439   1.00 27.42  ? 51  TRP A CE2 1 
ATOM   415  C  CE3 . TRP A 1 52  ? 33.530  17.746 2.365   1.00 30.51  ? 51  TRP A CE3 1 
ATOM   416  C  CZ2 . TRP A 1 52  ? 31.617  19.815 2.675   1.00 35.24  ? 51  TRP A CZ2 1 
ATOM   417  C  CZ3 . TRP A 1 52  ? 32.209  17.467 2.622   1.00 32.85  ? 51  TRP A CZ3 1 
ATOM   418  C  CH2 . TRP A 1 52  ? 31.274  18.489 2.771   1.00 28.46  ? 51  TRP A CH2 1 
ATOM   419  N  N   . ILE A 1 53  ? 35.084  17.178 -0.751  1.00 35.34  ? 52  ILE A N   1 
ATOM   420  C  CA  . ILE A 1 53  ? 34.432  15.876 -1.069  1.00 35.58  ? 52  ILE A CA  1 
ATOM   421  C  C   . ILE A 1 53  ? 35.106  15.265 -2.299  1.00 34.98  ? 52  ILE A C   1 
ATOM   422  O  O   . ILE A 1 53  ? 34.908  14.058 -2.535  1.00 33.72  ? 52  ILE A O   1 
ATOM   423  C  CB  . ILE A 1 53  ? 32.904  16.036 -1.237  1.00 27.81  ? 52  ILE A CB  1 
ATOM   424  C  CG1 . ILE A 1 53  ? 32.166  14.709 -1.018  1.00 23.95  ? 52  ILE A CG1 1 
ATOM   425  C  CG2 . ILE A 1 53  ? 32.563  16.661 -2.573  1.00 28.53  ? 52  ILE A CG2 1 
ATOM   426  C  CD1 . ILE A 1 53  ? 32.314  14.136 0.358   1.00 32.09  ? 52  ILE A CD1 1 
ATOM   427  N  N   . GLU A 1 54  ? 35.892  16.044 -3.045  1.00 37.57  ? 53  GLU A N   1 
ATOM   428  C  CA  . GLU A 1 54  ? 36.553  15.577 -4.298  1.00 37.68  ? 53  GLU A CA  1 
ATOM   429  C  C   . GLU A 1 54  ? 37.520  14.427 -3.987  1.00 39.32  ? 53  GLU A C   1 
ATOM   430  O  O   . GLU A 1 54  ? 37.766  13.634 -4.894  1.00 44.38  ? 53  GLU A O   1 
ATOM   431  C  CB  . GLU A 1 54  ? 37.262  16.738 -4.995  1.00 41.39  ? 53  GLU A CB  1 
ATOM   432  C  CG  . GLU A 1 54  ? 36.295  17.718 -5.635  1.00 40.55  ? 53  GLU A CG  1 
ATOM   433  C  CD  . GLU A 1 54  ? 36.914  18.983 -6.199  1.00 62.84  ? 53  GLU A CD  1 
ATOM   434  O  OE1 . GLU A 1 54  ? 38.153  19.123 -6.138  1.00 54.28  ? 53  GLU A OE1 1 
ATOM   435  O  OE2 . GLU A 1 54  ? 36.147  19.843 -6.676  1.00 53.51  ? 53  GLU A OE2 1 
ATOM   436  N  N   . GLN A 1 55  ? 37.961  14.292 -2.733  1.00 41.95  ? 54  GLN A N   1 
ATOM   437  C  CA  . GLN A 1 55  ? 38.903  13.233 -2.276  1.00 48.64  ? 54  GLN A CA  1 
ATOM   438  C  C   . GLN A 1 55  ? 38.206  11.867 -2.212  1.00 55.96  ? 54  GLN A C   1 
ATOM   439  O  O   . GLN A 1 55  ? 38.918  10.864 -2.029  1.00 50.98  ? 54  GLN A O   1 
ATOM   440  C  CB  . GLN A 1 55  ? 39.541  13.595 -0.924  1.00 46.65  ? 54  GLN A CB  1 
ATOM   441  C  CG  . GLN A 1 55  ? 38.599  13.611 0.274   1.00 61.01  ? 54  GLN A CG  1 
ATOM   442  C  CD  . GLN A 1 55  ? 39.183  14.340 1.470   1.00 76.23  ? 54  GLN A CD  1 
ATOM   443  O  OE1 . GLN A 1 55  ? 39.525  13.734 2.482   1.00 73.24  ? 54  GLN A OE1 1 
ATOM   444  N  NE2 . GLN A 1 55  ? 39.304  15.658 1.376   1.00 56.00  ? 54  GLN A NE2 1 
ATOM   445  N  N   . GLU A 1 56  ? 36.875  11.814 -2.313  1.00 45.58  ? 55  GLU A N   1 
ATOM   446  C  CA  . GLU A 1 56  ? 36.129  10.529 -2.283  1.00 39.92  ? 55  GLU A CA  1 
ATOM   447  C  C   . GLU A 1 56  ? 36.433  9.788  -3.593  1.00 33.38  ? 55  GLU A C   1 
ATOM   448  O  O   . GLU A 1 56  ? 36.497  10.429 -4.679  1.00 38.31  ? 55  GLU A O   1 
ATOM   449  C  CB  . GLU A 1 56  ? 34.638  10.773 -2.018  1.00 35.42  ? 55  GLU A CB  1 
ATOM   450  C  CG  . GLU A 1 56  ? 34.372  11.322 -0.628  1.00 36.66  ? 55  GLU A CG  1 
ATOM   451  C  CD  . GLU A 1 56  ? 34.632  10.379 0.524   1.00 43.24  ? 55  GLU A CD  1 
ATOM   452  O  OE1 . GLU A 1 56  ? 34.894  9.204  0.234   1.00 42.58  ? 55  GLU A OE1 1 
ATOM   453  O  OE2 . GLU A 1 56  ? 34.522  10.810 1.711   1.00 45.98  ? 55  GLU A OE2 1 
ATOM   454  N  N   . GLY A 1 57  ? 36.699  8.485  -3.490  1.00 38.31  ? 56  GLY A N   1 
ATOM   455  C  CA  . GLY A 1 57  ? 37.021  7.648  -4.658  1.00 36.02  ? 56  GLY A CA  1 
ATOM   456  C  C   . GLY A 1 57  ? 35.787  7.406  -5.523  1.00 41.17  ? 56  GLY A C   1 
ATOM   457  O  O   . GLY A 1 57  ? 34.680  7.777  -5.152  1.00 37.65  ? 56  GLY A O   1 
ATOM   458  N  N   . PRO A 1 58  ? 35.952  6.809  -6.716  1.00 39.05  ? 57  PRO A N   1 
ATOM   459  C  CA  . PRO A 1 58  ? 34.831  6.524  -7.604  1.00 39.88  ? 57  PRO A CA  1 
ATOM   460  C  C   . PRO A 1 58  ? 33.788  5.571  -6.990  1.00 33.83  ? 57  PRO A C   1 
ATOM   461  O  O   . PRO A 1 58  ? 32.642  5.669  -7.377  1.00 33.58  ? 57  PRO A O   1 
ATOM   462  C  CB  . PRO A 1 58  ? 35.510  5.896  -8.836  1.00 44.52  ? 57  PRO A CB  1 
ATOM   463  C  CG  . PRO A 1 58  ? 36.806  5.359  -8.317  1.00 49.82  ? 57  PRO A CG  1 
ATOM   464  C  CD  . PRO A 1 58  ? 37.238  6.351  -7.267  1.00 50.78  ? 57  PRO A CD  1 
ATOM   465  N  N   . GLU A 1 59  ? 34.172  4.686  -6.064  1.00 33.49  ? 58  GLU A N   1 
ATOM   466  C  CA  . GLU A 1 59  ? 33.194  3.811  -5.351  1.00 37.97  ? 58  GLU A CA  1 
ATOM   467  C  C   . GLU A 1 59  ? 32.128  4.660  -4.619  1.00 39.07  ? 58  GLU A C   1 
ATOM   468  O  O   . GLU A 1 59  ? 30.957  4.228  -4.578  1.00 35.47  ? 58  GLU A O   1 
ATOM   469  C  CB  . GLU A 1 59  ? 33.879  2.815  -4.403  1.00 45.97  ? 58  GLU A CB  1 
ATOM   470  C  CG  . GLU A 1 59  ? 34.650  3.444  -3.254  1.00 67.41  ? 58  GLU A CG  1 
ATOM   471  C  CD  . GLU A 1 59  ? 35.993  4.068  -3.620  1.00 81.54  ? 58  GLU A CD  1 
ATOM   472  O  OE1 . GLU A 1 59  ? 36.463  3.872  -4.780  1.00 58.50  ? 58  GLU A OE1 1 
ATOM   473  O  OE2 . GLU A 1 59  ? 36.562  4.762  -2.749  1.00 77.06  ? 58  GLU A OE2 1 
ATOM   474  N  N   . TYR A 1 60  ? 32.500  5.832  -4.095  1.00 34.32  ? 59  TYR A N   1 
ATOM   475  C  CA  . TYR A 1 60  ? 31.572  6.797  -3.439  1.00 28.78  ? 59  TYR A CA  1 
ATOM   476  C  C   . TYR A 1 60  ? 30.512  7.277  -4.442  1.00 29.61  ? 59  TYR A C   1 
ATOM   477  O  O   . TYR A 1 60  ? 29.283  7.121  -4.174  1.00 26.71  ? 59  TYR A O   1 
ATOM   478  C  CB  . TYR A 1 60  ? 32.373  7.960  -2.861  1.00 31.51  ? 59  TYR A CB  1 
ATOM   479  C  CG  . TYR A 1 60  ? 31.566  9.001  -2.137  1.00 27.90  ? 59  TYR A CG  1 
ATOM   480  C  CD1 . TYR A 1 60  ? 31.276  8.878  -0.780  1.00 29.45  ? 59  TYR A CD1 1 
ATOM   481  C  CD2 . TYR A 1 60  ? 31.123  10.130 -2.812  1.00 28.36  ? 59  TYR A CD2 1 
ATOM   482  C  CE1 . TYR A 1 60  ? 30.546  9.857  -0.118  1.00 30.05  ? 59  TYR A CE1 1 
ATOM   483  C  CE2 . TYR A 1 60  ? 30.362  11.098 -2.172  1.00 29.68  ? 59  TYR A CE2 1 
ATOM   484  C  CZ  . TYR A 1 60  ? 30.083  10.966 -0.821  1.00 30.61  ? 59  TYR A CZ  1 
ATOM   485  O  OH  . TYR A 1 60  ? 29.348  11.940 -0.206  1.00 27.66  ? 59  TYR A OH  1 
ATOM   486  N  N   . TRP A 1 61  ? 30.971  7.888  -5.541  1.00 27.36  ? 60  TRP A N   1 
ATOM   487  C  CA  . TRP A 1 61  ? 30.110  8.507  -6.581  1.00 28.73  ? 60  TRP A CA  1 
ATOM   488  C  C   . TRP A 1 61  ? 29.224  7.417  -7.205  1.00 33.13  ? 60  TRP A C   1 
ATOM   489  O  O   . TRP A 1 61  ? 28.039  7.677  -7.417  1.00 29.94  ? 60  TRP A O   1 
ATOM   490  C  CB  . TRP A 1 61  ? 30.961  9.260  -7.613  1.00 30.18  ? 60  TRP A CB  1 
ATOM   491  C  CG  . TRP A 1 61  ? 31.900  10.205 -6.938  1.00 34.93  ? 60  TRP A CG  1 
ATOM   492  C  CD1 . TRP A 1 61  ? 33.243  10.058 -6.746  1.00 41.76  ? 60  TRP A CD1 1 
ATOM   493  C  CD2 . TRP A 1 61  ? 31.529  11.404 -6.228  1.00 34.48  ? 60  TRP A CD2 1 
ATOM   494  N  NE1 . TRP A 1 61  ? 33.735  11.091 -5.990  1.00 42.10  ? 60  TRP A NE1 1 
ATOM   495  C  CE2 . TRP A 1 61  ? 32.713  11.953 -5.691  1.00 36.22  ? 60  TRP A CE2 1 
ATOM   496  C  CE3 . TRP A 1 61  ? 30.325  12.078 -6.051  1.00 32.78  ? 60  TRP A CE3 1 
ATOM   497  C  CZ2 . TRP A 1 61  ? 32.708  13.107 -4.918  1.00 32.53  ? 60  TRP A CZ2 1 
ATOM   498  C  CZ3 . TRP A 1 61  ? 30.329  13.265 -5.360  1.00 33.76  ? 60  TRP A CZ3 1 
ATOM   499  C  CH2 . TRP A 1 61  ? 31.502  13.748 -4.772  1.00 32.03  ? 60  TRP A CH2 1 
ATOM   500  N  N   . ASP A 1 62  ? 29.770  6.223  -7.470  1.00 30.00  ? 61  ASP A N   1 
ATOM   501  C  CA  . ASP A 1 62  ? 28.993  5.119  -8.096  1.00 30.14  ? 61  ASP A CA  1 
ATOM   502  C  C   . ASP A 1 62  ? 27.922  4.624  -7.112  1.00 26.85  ? 61  ASP A C   1 
ATOM   503  O  O   . ASP A 1 62  ? 26.781  4.410  -7.530  1.00 28.45  ? 61  ASP A O   1 
ATOM   504  C  CB  . ASP A 1 62  ? 29.908  3.997  -8.597  1.00 33.96  ? 61  ASP A CB  1 
ATOM   505  C  CG  . ASP A 1 62  ? 30.816  4.373  -9.768  1.00 42.04  ? 61  ASP A CG  1 
ATOM   506  O  OD1 . ASP A 1 62  ? 30.493  5.328  -10.525 1.00 47.40  ? 61  ASP A OD1 1 
ATOM   507  O  OD2 . ASP A 1 62  ? 31.861  3.714  -9.913  1.00 55.34  ? 61  ASP A OD2 1 
ATOM   508  N  N   . ARG A 1 63  ? 28.265  4.441  -5.852  1.00 27.44  ? 62  ARG A N   1 
ATOM   509  C  CA  . ARG A 1 63  ? 27.287  3.984  -4.828  1.00 28.07  ? 62  ARG A CA  1 
ATOM   510  C  C   . ARG A 1 63  ? 26.141  4.995  -4.705  1.00 28.50  ? 62  ARG A C   1 
ATOM   511  O  O   . ARG A 1 63  ? 24.981  4.588  -4.731  1.00 24.45  ? 62  ARG A O   1 
ATOM   512  C  CB  . ARG A 1 63  ? 27.960  3.811  -3.471  1.00 24.20  ? 62  ARG A CB  1 
ATOM   513  C  CG  . ARG A 1 63  ? 27.007  3.493  -2.325  1.00 24.53  ? 62  ARG A CG  1 
ATOM   514  C  CD  . ARG A 1 63  ? 27.745  3.246  -1.005  1.00 29.57  ? 62  ARG A CD  1 
ATOM   515  N  NE  . ARG A 1 63  ? 26.796  2.778  -0.021  1.00 29.95  ? 62  ARG A NE  1 
ATOM   516  C  CZ  . ARG A 1 63  ? 26.099  3.537  0.825   1.00 33.24  ? 62  ARG A CZ  1 
ATOM   517  N  NH1 . ARG A 1 63  ? 26.303  4.841  0.917   1.00 29.18  ? 62  ARG A NH1 1 
ATOM   518  N  NH2 . ARG A 1 63  ? 25.230  2.964  1.633   1.00 32.75  ? 62  ARG A NH2 1 
ATOM   519  N  N   . ASN A 1 64  ? 26.472  6.276  -4.554  1.00 26.29  ? 63  ASN A N   1 
ATOM   520  C  CA  . ASN A 1 64  ? 25.470  7.343  -4.291  1.00 25.67  ? 63  ASN A CA  1 
ATOM   521  C  C   . ASN A 1 64  ? 24.600  7.469  -5.537  1.00 25.20  ? 63  ASN A C   1 
ATOM   522  O  O   . ASN A 1 64  ? 23.380  7.553  -5.388  1.00 27.34  ? 63  ASN A O   1 
ATOM   523  C  CB  . ASN A 1 64  ? 26.171  8.609  -3.831  1.00 22.52  ? 63  ASN A CB  1 
ATOM   524  C  CG  . ASN A 1 64  ? 26.862  8.411  -2.494  1.00 22.73  ? 63  ASN A CG  1 
ATOM   525  O  OD1 . ASN A 1 64  ? 26.641  7.406  -1.830  1.00 27.43  ? 63  ASN A OD1 1 
ATOM   526  N  ND2 . ASN A 1 64  ? 27.642  9.392  -2.045  1.00 23.42  ? 63  ASN A ND2 1 
ATOM   527  N  N   . THR A 1 65  ? 25.198  7.320  -6.721  1.00 23.37  ? 64  THR A N   1 
ATOM   528  C  CA  . THR A 1 65  ? 24.435  7.322  -7.989  1.00 23.90  ? 64  THR A CA  1 
ATOM   529  C  C   . THR A 1 65  ? 23.355  6.240  -7.956  1.00 25.22  ? 64  THR A C   1 
ATOM   530  O  O   . THR A 1 65  ? 22.216  6.538  -8.332  1.00 24.22  ? 64  THR A O   1 
ATOM   531  C  CB  . THR A 1 65  ? 25.373  7.239  -9.184  1.00 26.56  ? 64  THR A CB  1 
ATOM   532  O  OG1 . THR A 1 65  ? 26.151  8.428  -9.096  1.00 27.68  ? 64  THR A OG1 1 
ATOM   533  C  CG2 . THR A 1 65  ? 24.636  7.180  -10.493 1.00 28.94  ? 64  THR A CG2 1 
ATOM   534  N  N   . GLN A 1 66  ? 23.697  5.024  -7.551  1.00 26.71  ? 65  GLN A N   1 
ATOM   535  C  CA  . GLN A 1 66  ? 22.722  3.910  -7.534  1.00 24.37  ? 65  GLN A CA  1 
ATOM   536  C  C   . GLN A 1 66  ? 21.577  4.247  -6.558  1.00 23.51  ? 65  GLN A C   1 
ATOM   537  O  O   . GLN A 1 66  ? 20.417  3.947  -6.848  1.00 26.74  ? 65  GLN A O   1 
ATOM   538  C  CB  . GLN A 1 66  ? 23.426  2.617  -7.134  1.00 29.93  ? 65  GLN A CB  1 
ATOM   539  C  CG  . GLN A 1 66  ? 24.468  2.119  -8.132  1.00 34.89  ? 65  GLN A CG  1 
ATOM   540  C  CD  . GLN A 1 66  ? 24.936  0.732  -7.733  1.00 43.75  ? 65  GLN A CD  1 
ATOM   541  O  OE1 . GLN A 1 66  ? 24.170  -0.225 -7.768  1.00 50.96  ? 65  GLN A OE1 1 
ATOM   542  N  NE2 . GLN A 1 66  ? 26.198  0.615  -7.355  1.00 46.06  ? 65  GLN A NE2 1 
ATOM   543  N  N   . ILE A 1 67  ? 21.902  4.831  -5.413  1.00 25.21  ? 66  ILE A N   1 
ATOM   544  C  CA  . ILE A 1 67  ? 20.891  5.185  -4.377  1.00 23.49  ? 66  ILE A CA  1 
ATOM   545  C  C   . ILE A 1 67  ? 19.966  6.236  -4.991  1.00 25.42  ? 66  ILE A C   1 
ATOM   546  O  O   . ILE A 1 67  ? 18.744  6.098  -4.839  1.00 25.57  ? 66  ILE A O   1 
ATOM   547  C  CB  . ILE A 1 67  ? 21.602  5.649  -3.087  1.00 24.14  ? 66  ILE A CB  1 
ATOM   548  C  CG1 . ILE A 1 67  ? 22.367  4.498  -2.433  1.00 23.01  ? 66  ILE A CG1 1 
ATOM   549  C  CG2 . ILE A 1 67  ? 20.620  6.309  -2.143  1.00 23.86  ? 66  ILE A CG2 1 
ATOM   550  C  CD1 . ILE A 1 67  ? 23.338  4.884  -1.335  1.00 23.61  ? 66  ILE A CD1 1 
ATOM   551  N  N   . TYR A 1 68  ? 20.509  7.271  -5.646  1.00 24.15  ? 67  TYR A N   1 
ATOM   552  C  CA  . TYR A 1 68  ? 19.675  8.369  -6.194  1.00 24.92  ? 67  TYR A CA  1 
ATOM   553  C  C   . TYR A 1 68  ? 18.741  7.809  -7.256  1.00 22.96  ? 67  TYR A C   1 
ATOM   554  O  O   . TYR A 1 68  ? 17.582  8.192  -7.294  1.00 24.29  ? 67  TYR A O   1 
ATOM   555  C  CB  . TYR A 1 68  ? 20.472  9.509  -6.809  1.00 24.11  ? 67  TYR A CB  1 
ATOM   556  C  CG  . TYR A 1 68  ? 21.226  10.350 -5.820  1.00 24.75  ? 67  TYR A CG  1 
ATOM   557  C  CD1 . TYR A 1 68  ? 20.580  11.030 -4.799  1.00 26.99  ? 67  TYR A CD1 1 
ATOM   558  C  CD2 . TYR A 1 68  ? 22.596  10.474 -5.944  1.00 24.17  ? 67  TYR A CD2 1 
ATOM   559  C  CE1 . TYR A 1 68  ? 21.287  11.855 -3.940  1.00 25.19  ? 67  TYR A CE1 1 
ATOM   560  C  CE2 . TYR A 1 68  ? 23.323  11.258 -5.078  1.00 28.05  ? 67  TYR A CE2 1 
ATOM   561  C  CZ  . TYR A 1 68  ? 22.661  11.968 -4.091  1.00 28.72  ? 67  TYR A CZ  1 
ATOM   562  O  OH  . TYR A 1 68  ? 23.404  12.756 -3.279  1.00 23.95  ? 67  TYR A OH  1 
ATOM   563  N  N   . LYS A 1 69  ? 19.224  6.899  -8.092  1.00 23.69  ? 68  LYS A N   1 
ATOM   564  C  CA  . LYS A 1 69  ? 18.358  6.309  -9.143  1.00 27.11  ? 68  LYS A CA  1 
ATOM   565  C  C   . LYS A 1 69  ? 17.165  5.566  -8.526  1.00 24.45  ? 68  LYS A C   1 
ATOM   566  O  O   . LYS A 1 69  ? 16.069  5.617  -9.076  1.00 26.06  ? 68  LYS A O   1 
ATOM   567  C  CB  . LYS A 1 69  ? 19.194  5.405  -10.047 1.00 30.38  ? 68  LYS A CB  1 
ATOM   568  C  CG  . LYS A 1 69  ? 19.989  6.206  -11.061 1.00 32.65  ? 68  LYS A CG  1 
ATOM   569  C  CD  . LYS A 1 69  ? 21.051  5.386  -11.723 1.00 38.91  ? 68  LYS A CD  1 
ATOM   570  C  CE  . LYS A 1 69  ? 21.792  6.180  -12.772 1.00 42.55  ? 68  LYS A CE  1 
ATOM   571  N  NZ  . LYS A 1 69  ? 22.686  5.292  -13.543 1.00 45.29  ? 68  LYS A NZ  1 
ATOM   572  N  N   . ALA A 1 70  ? 17.386  4.855  -7.440  1.00 23.66  ? 69  ALA A N   1 
ATOM   573  C  CA  . ALA A 1 70  ? 16.330  4.123  -6.730  1.00 28.16  ? 69  ALA A CA  1 
ATOM   574  C  C   . ALA A 1 70  ? 15.444  5.143  -6.023  1.00 25.70  ? 69  ALA A C   1 
ATOM   575  O  O   . ALA A 1 70  ? 14.228  4.926  -5.972  1.00 23.85  ? 69  ALA A O   1 
ATOM   576  C  CB  . ALA A 1 70  ? 16.923  3.131  -5.771  1.00 24.08  ? 69  ALA A CB  1 
ATOM   577  N  N   . GLN A 1 71  ? 16.007  6.233  -5.501  1.00 24.90  ? 70  GLN A N   1 
ATOM   578  C  CA  . GLN A 1 71  ? 15.154  7.287  -4.874  1.00 25.83  ? 70  GLN A CA  1 
ATOM   579  C  C   . GLN A 1 71  ? 14.204  7.897  -5.900  1.00 23.87  ? 70  GLN A C   1 
ATOM   580  O  O   . GLN A 1 71  ? 13.029  8.163  -5.565  1.00 25.18  ? 70  GLN A O   1 
ATOM   581  C  CB  . GLN A 1 71  ? 15.983  8.420  -4.270  1.00 24.28  ? 70  GLN A CB  1 
ATOM   582  C  CG  . GLN A 1 71  ? 15.143  9.429  -3.501  1.00 22.53  ? 70  GLN A CG  1 
ATOM   583  C  CD  . GLN A 1 71  ? 14.511  8.835  -2.263  1.00 21.10  ? 70  GLN A CD  1 
ATOM   584  O  OE1 . GLN A 1 71  ? 15.213  8.358  -1.356  1.00 25.52  ? 70  GLN A OE1 1 
ATOM   585  N  NE2 . GLN A 1 71  ? 13.189  8.831  -2.244  1.00 23.32  ? 70  GLN A NE2 1 
ATOM   586  N  N   . ALA A 1 72  ? 14.677  8.128  -7.114  1.00 26.25  ? 71  ALA A N   1 
ATOM   587  C  CA  . ALA A 1 72  ? 13.857  8.775  -8.158  1.00 23.51  ? 71  ALA A CA  1 
ATOM   588  C  C   . ALA A 1 72  ? 12.634  7.896  -8.420  1.00 23.16  ? 71  ALA A C   1 
ATOM   589  O  O   . ALA A 1 72  ? 11.513  8.409  -8.474  1.00 25.27  ? 71  ALA A O   1 
ATOM   590  C  CB  . ALA A 1 72  ? 14.671  8.980  -9.407  1.00 25.75  ? 71  ALA A CB  1 
ATOM   591  N  N   . GLN A 1 73  ? 12.826  6.594  -8.542  1.00 23.63  ? 72  GLN A N   1 
ATOM   592  C  CA  . GLN A 1 73  ? 11.700  5.641  -8.793  1.00 22.15  ? 72  GLN A CA  1 
ATOM   593  C  C   . GLN A 1 73  ? 10.725  5.647  -7.618  1.00 23.76  ? 72  GLN A C   1 
ATOM   594  O  O   . GLN A 1 73  ? 9.510   5.554  -7.830  1.00 25.59  ? 72  GLN A O   1 
ATOM   595  C  CB  . GLN A 1 73  ? 12.278  4.238  -8.989  1.00 29.13  ? 72  GLN A CB  1 
ATOM   596  C  CG  . GLN A 1 73  ? 13.115  4.116  -10.257 1.00 33.75  ? 72  GLN A CG  1 
ATOM   597  C  CD  . GLN A 1 73  ? 13.897  2.832  -10.313 1.00 42.43  ? 72  GLN A CD  1 
ATOM   598  O  OE1 . GLN A 1 73  ? 14.480  2.390  -9.329  1.00 41.32  ? 72  GLN A OE1 1 
ATOM   599  N  NE2 . GLN A 1 73  ? 13.892  2.211  -11.476 1.00 37.47  ? 72  GLN A NE2 1 
ATOM   600  N  N   . THR A 1 74  ? 11.252  5.645  -6.402  1.00 24.16  ? 73  THR A N   1 
ATOM   601  C  CA  . THR A 1 74  ? 10.430  5.728  -5.174  1.00 21.38  ? 73  THR A CA  1 
ATOM   602  C  C   . THR A 1 74  ? 9.552   6.986  -5.252  1.00 24.42  ? 73  THR A C   1 
ATOM   603  O  O   . THR A 1 74  ? 8.341   6.868  -4.978  1.00 23.49  ? 73  THR A O   1 
ATOM   604  C  CB  . THR A 1 74  ? 11.319  5.754  -3.936  1.00 26.86  ? 73  THR A CB  1 
ATOM   605  O  OG1 . THR A 1 74  ? 12.199  4.628  -3.963  1.00 26.12  ? 73  THR A OG1 1 
ATOM   606  C  CG2 . THR A 1 74  ? 10.519  5.821  -2.664  1.00 27.54  ? 73  THR A CG2 1 
ATOM   607  N  N   . ASP A 1 75  ? 10.150  8.138  -5.538  1.00 24.91  ? 74  ASP A N   1 
ATOM   608  C  CA  . ASP A 1 75  ? 9.448   9.454  -5.577  1.00 22.16  ? 74  ASP A CA  1 
ATOM   609  C  C   . ASP A 1 75  ? 8.404   9.408  -6.696  1.00 22.39  ? 74  ASP A C   1 
ATOM   610  O  O   . ASP A 1 75  ? 7.315   9.964  -6.519  1.00 23.74  ? 74  ASP A O   1 
ATOM   611  C  CB  . ASP A 1 75  ? 10.413  10.618 -5.792  1.00 22.37  ? 74  ASP A CB  1 
ATOM   612  C  CG  . ASP A 1 75  ? 11.083  11.175 -4.543  1.00 26.63  ? 74  ASP A CG  1 
ATOM   613  O  OD1 . ASP A 1 75  ? 11.154  10.450 -3.493  1.00 28.26  ? 74  ASP A OD1 1 
ATOM   614  O  OD2 . ASP A 1 75  ? 11.546  12.332 -4.629  1.00 29.42  ? 74  ASP A OD2 1 
ATOM   615  N  N   . ARG A 1 76  ? 8.711   8.748  -7.796  1.00 21.04  ? 75  ARG A N   1 
ATOM   616  C  CA  . ARG A 1 76  ? 7.729   8.584  -8.893  1.00 25.76  ? 75  ARG A CA  1 
ATOM   617  C  C   . ARG A 1 76  ? 6.482   7.903  -8.318  1.00 24.18  ? 75  ARG A C   1 
ATOM   618  O  O   . ARG A 1 76  ? 5.355   8.374  -8.587  1.00 23.06  ? 75  ARG A O   1 
ATOM   619  C  CB  . ARG A 1 76  ? 8.332   7.796  -10.065 1.00 27.48  ? 75  ARG A CB  1 
ATOM   620  C  CG  . ARG A 1 76  ? 7.337   7.488  -11.181 1.00 37.97  ? 75  ARG A CG  1 
ATOM   621  C  CD  . ARG A 1 76  ? 7.837   6.346  -12.057 1.00 39.32  ? 75  ARG A CD  1 
ATOM   622  N  NE  . ARG A 1 76  ? 7.722   5.073  -11.364 1.00 37.88  ? 75  ARG A NE  1 
ATOM   623  C  CZ  . ARG A 1 76  ? 8.525   4.028  -11.514 1.00 32.08  ? 75  ARG A CZ  1 
ATOM   624  N  NH1 . ARG A 1 76  ? 8.296   2.927  -10.816 1.00 45.41  ? 75  ARG A NH1 1 
ATOM   625  N  NH2 . ARG A 1 76  ? 9.568   4.087  -12.323 1.00 34.11  ? 75  ARG A NH2 1 
ATOM   626  N  N   . GLU A 1 77  ? 6.658   6.830  -7.550  1.00 28.03  ? 76  GLU A N   1 
ATOM   627  C  CA  . GLU A 1 77  ? 5.521   6.097  -6.940  1.00 26.26  ? 76  GLU A CA  1 
ATOM   628  C  C   . GLU A 1 77  ? 4.818   6.958  -5.883  1.00 28.50  ? 76  GLU A C   1 
ATOM   629  O  O   . GLU A 1 77  ? 3.550   6.986  -5.856  1.00 25.57  ? 76  GLU A O   1 
ATOM   630  C  CB  . GLU A 1 77  ? 6.024   4.781  -6.360  1.00 30.77  ? 76  GLU A CB  1 
ATOM   631  C  CG  . GLU A 1 77  ? 6.359   3.780  -7.454  1.00 33.00  ? 76  GLU A CG  1 
ATOM   632  C  CD  . GLU A 1 77  ? 5.270   3.670  -8.503  1.00 36.31  ? 76  GLU A CD  1 
ATOM   633  O  OE1 . GLU A 1 77  ? 4.117   3.425  -8.083  1.00 31.22  ? 76  GLU A OE1 1 
ATOM   634  O  OE2 . GLU A 1 77  ? 5.564   3.866  -9.721  1.00 32.71  ? 76  GLU A OE2 1 
ATOM   635  N  N   . SER A 1 78  ? 5.576   7.690  -5.064  1.00 23.88  ? 77  SER A N   1 
ATOM   636  C  CA  . SER A 1 78  ? 4.963   8.661  -4.127  1.00 25.29  ? 77  SER A CA  1 
ATOM   637  C  C   . SER A 1 78  ? 4.080   9.620  -4.914  1.00 21.30  ? 77  SER A C   1 
ATOM   638  O  O   . SER A 1 78  ? 2.955   9.859  -4.462  1.00 26.66  ? 77  SER A O   1 
ATOM   639  C  CB  . SER A 1 78  ? 5.970   9.391  -3.302  1.00 27.83  ? 77  SER A CB  1 
ATOM   640  O  OG  . SER A 1 78  ? 6.548   8.518  -2.335  1.00 25.90  ? 77  SER A OG  1 
ATOM   641  N  N   . LEU A 1 79  ? 4.576   10.171 -6.011  1.00 25.06  ? 78  LEU A N   1 
ATOM   642  C  CA  . LEU A 1 79  ? 3.785   11.164 -6.794  1.00 26.35  ? 78  LEU A CA  1 
ATOM   643  C  C   . LEU A 1 79  ? 2.512   10.490 -7.340  1.00 25.06  ? 78  LEU A C   1 
ATOM   644  O  O   . LEU A 1 79  ? 1.444   11.100 -7.291  1.00 25.96  ? 78  LEU A O   1 
ATOM   645  C  CB  . LEU A 1 79  ? 4.644   11.721 -7.930  1.00 22.97  ? 78  LEU A CB  1 
ATOM   646  C  CG  . LEU A 1 79  ? 5.692   12.757 -7.551  1.00 21.64  ? 78  LEU A CG  1 
ATOM   647  C  CD1 . LEU A 1 79  ? 6.680   12.968 -8.670  1.00 26.37  ? 78  LEU A CD1 1 
ATOM   648  C  CD2 . LEU A 1 79  ? 5.069   14.074 -7.152  1.00 27.28  ? 78  LEU A CD2 1 
ATOM   649  N  N   . ARG A 1 80  ? 2.593   9.232  -7.760  1.00 24.91  ? 79  ARG A N   1 
ATOM   650  C  CA  . ARG A 1 80  ? 1.428   8.506  -8.328  1.00 25.56  ? 79  ARG A CA  1 
ATOM   651  C  C   . ARG A 1 80  ? 0.380   8.345  -7.202  1.00 25.66  ? 79  ARG A C   1 
ATOM   652  O  O   . ARG A 1 80  ? -0.808  8.650  -7.424  1.00 26.12  ? 79  ARG A O   1 
ATOM   653  C  CB  . ARG A 1 80  ? 1.944   7.239  -9.017  1.00 26.72  ? 79  ARG A CB  1 
ATOM   654  C  CG  . ARG A 1 80  ? 0.840   6.358  -9.597  1.00 36.67  ? 79  ARG A CG  1 
ATOM   655  C  CD  . ARG A 1 80  ? 1.325   5.129  -10.358 1.00 36.46  ? 79  ARG A CD  1 
ATOM   656  N  NE  . ARG A 1 80  ? 1.653   4.065  -9.411  1.00 38.26  ? 79  ARG A NE  1 
ATOM   657  C  CZ  . ARG A 1 80  ? 0.773   3.247  -8.811  1.00 43.98  ? 79  ARG A CZ  1 
ATOM   658  N  NH1 . ARG A 1 80  ? 1.189   2.311  -7.971  1.00 40.86  ? 79  ARG A NH1 1 
ATOM   659  N  NH2 . ARG A 1 80  ? -0.520  3.363  -9.052  1.00 39.59  ? 79  ARG A NH2 1 
ATOM   660  N  N   . ASN A 1 81  ? 0.800   7.931  -5.997  1.00 24.54  ? 80  ASN A N   1 
ATOM   661  C  CA  . ASN A 1 81  ? -0.092  7.765  -4.822  1.00 21.44  ? 80  ASN A CA  1 
ATOM   662  C  C   . ASN A 1 81  ? -0.762  9.107  -4.439  1.00 26.70  ? 80  ASN A C   1 
ATOM   663  O  O   . ASN A 1 81  ? -1.942  9.136  -4.088  1.00 25.36  ? 80  ASN A O   1 
ATOM   664  C  CB  . ASN A 1 81  ? 0.736   7.271  -3.628  1.00 23.15  ? 80  ASN A CB  1 
ATOM   665  C  CG  . ASN A 1 81  ? 1.238   5.860  -3.845  1.00 28.53  ? 80  ASN A CG  1 
ATOM   666  O  OD1 . ASN A 1 81  ? 0.868   5.226  -4.828  1.00 25.84  ? 80  ASN A OD1 1 
ATOM   667  N  ND2 . ASN A 1 81  ? 2.117   5.383  -2.971  1.00 28.38  ? 80  ASN A ND2 1 
ATOM   668  N  N   . LEU A 1 82  ? 0.009   10.199 -4.401  1.00 28.42  ? 81  LEU A N   1 
ATOM   669  C  CA  . LEU A 1 82  ? -0.502  11.538 -4.011  1.00 24.26  ? 81  LEU A CA  1 
ATOM   670  C  C   . LEU A 1 82  ? -1.581  11.993 -5.004  1.00 24.23  ? 81  LEU A C   1 
ATOM   671  O  O   . LEU A 1 82  ? -2.583  12.571 -4.556  1.00 25.19  ? 81  LEU A O   1 
ATOM   672  C  CB  . LEU A 1 82  ? 0.696   12.499 -3.979  1.00 24.36  ? 81  LEU A CB  1 
ATOM   673  C  CG  . LEU A 1 82  ? 1.632   12.282 -2.793  1.00 27.12  ? 81  LEU A CG  1 
ATOM   674  C  CD1 . LEU A 1 82  ? 3.023   12.809 -3.068  1.00 31.93  ? 81  LEU A CD1 1 
ATOM   675  C  CD2 . LEU A 1 82  ? 1.079   12.948 -1.542  1.00 32.15  ? 81  LEU A CD2 1 
ATOM   676  N  N   . ARG A 1 83  ? -1.340  11.813 -6.313  1.00 23.53  ? 82  ARG A N   1 
ATOM   677  C  CA  . ARG A 1 83  ? -2.342  12.106 -7.371  1.00 29.64  ? 82  ARG A CA  1 
ATOM   678  C  C   . ARG A 1 83  ? -3.679  11.466 -6.965  1.00 34.98  ? 82  ARG A C   1 
ATOM   679  O  O   . ARG A 1 83  ? -4.719  12.153 -7.015  1.00 33.52  ? 82  ARG A O   1 
ATOM   680  C  CB  . ARG A 1 83  ? -1.793  11.581 -8.695  1.00 34.15  ? 82  ARG A CB  1 
ATOM   681  C  CG  . ARG A 1 83  ? -2.341  12.198 -9.966  1.00 57.84  ? 82  ARG A CG  1 
ATOM   682  C  CD  . ARG A 1 83  ? -1.255  12.216 -11.046 1.00 62.75  ? 82  ARG A CD  1 
ATOM   683  N  NE  . ARG A 1 83  ? -0.928  10.906 -11.615 1.00 69.42  ? 82  ARG A NE  1 
ATOM   684  C  CZ  . ARG A 1 83  ? 0.291   10.326 -11.669 1.00 79.42  ? 82  ARG A CZ  1 
ATOM   685  N  NH1 . ARG A 1 83  ? 1.392   10.885 -11.166 1.00 44.74  ? 82  ARG A NH1 1 
ATOM   686  N  NH2 . ARG A 1 83  ? 0.391   9.138  -12.241 1.00 73.61  ? 82  ARG A NH2 1 
ATOM   687  N  N   . GLY A 1 84  ? -3.663  10.194 -6.550  1.00 30.15  ? 83  GLY A N   1 
ATOM   688  C  CA  . GLY A 1 84  ? -4.875  9.464  -6.145  1.00 31.94  ? 83  GLY A CA  1 
ATOM   689  C  C   . GLY A 1 84  ? -5.496  10.063 -4.908  1.00 31.51  ? 83  GLY A C   1 
ATOM   690  O  O   . GLY A 1 84  ? -6.714  10.254 -4.899  1.00 32.22  ? 83  GLY A O   1 
ATOM   691  N  N   . TYR A 1 85  ? -4.701  10.366 -3.883  1.00 27.95  ? 84  TYR A N   1 
ATOM   692  C  CA  . TYR A 1 85  ? -5.216  10.904 -2.605  1.00 28.43  ? 84  TYR A CA  1 
ATOM   693  C  C   . TYR A 1 85  ? -5.960  12.216 -2.874  1.00 33.25  ? 84  TYR A C   1 
ATOM   694  O  O   . TYR A 1 85  ? -6.940  12.514 -2.171  1.00 32.45  ? 84  TYR A O   1 
ATOM   695  C  CB  . TYR A 1 85  ? -4.095  11.206 -1.620  1.00 28.08  ? 84  TYR A CB  1 
ATOM   696  C  CG  . TYR A 1 85  ? -3.224  10.028 -1.234  1.00 30.12  ? 84  TYR A CG  1 
ATOM   697  C  CD1 . TYR A 1 85  ? -3.680  8.710  -1.319  1.00 30.18  ? 84  TYR A CD1 1 
ATOM   698  C  CD2 . TYR A 1 85  ? -1.962  10.251 -0.696  1.00 25.29  ? 84  TYR A CD2 1 
ATOM   699  C  CE1 . TYR A 1 85  ? -2.860  7.647  -0.956  1.00 30.06  ? 84  TYR A CE1 1 
ATOM   700  C  CE2 . TYR A 1 85  ? -1.145  9.200  -0.313  1.00 31.51  ? 84  TYR A CE2 1 
ATOM   701  C  CZ  . TYR A 1 85  ? -1.597  7.895  -0.445  1.00 33.11  ? 84  TYR A CZ  1 
ATOM   702  O  OH  . TYR A 1 85  ? -0.793  6.869  -0.030  1.00 29.72  ? 84  TYR A OH  1 
ATOM   703  N  N   . TYR A 1 86  ? -5.432  13.021 -3.798  1.00 29.68  ? 85  TYR A N   1 
ATOM   704  C  CA  . TYR A 1 86  ? -5.902  14.403 -4.065  1.00 30.26  ? 85  TYR A CA  1 
ATOM   705  C  C   . TYR A 1 86  ? -6.903  14.428 -5.223  1.00 37.06  ? 85  TYR A C   1 
ATOM   706  O  O   . TYR A 1 86  ? -7.384  15.537 -5.513  1.00 36.04  ? 85  TYR A O   1 
ATOM   707  C  CB  . TYR A 1 86  ? -4.723  15.350 -4.272  1.00 27.22  ? 85  TYR A CB  1 
ATOM   708  C  CG  . TYR A 1 86  ? -4.046  15.730 -2.980  1.00 32.10  ? 85  TYR A CG  1 
ATOM   709  C  CD1 . TYR A 1 86  ? -4.659  16.596 -2.093  1.00 31.78  ? 85  TYR A CD1 1 
ATOM   710  C  CD2 . TYR A 1 86  ? -2.830  15.167 -2.609  1.00 25.56  ? 85  TYR A CD2 1 
ATOM   711  C  CE1 . TYR A 1 86  ? -4.050  16.948 -0.898  1.00 33.14  ? 85  TYR A CE1 1 
ATOM   712  C  CE2 . TYR A 1 86  ? -2.217  15.504 -1.414  1.00 24.75  ? 85  TYR A CE2 1 
ATOM   713  C  CZ  . TYR A 1 86  ? -2.818  16.404 -0.558  1.00 31.64  ? 85  TYR A CZ  1 
ATOM   714  O  OH  . TYR A 1 86  ? -2.259  16.725 0.649   1.00 28.88  ? 85  TYR A OH  1 
ATOM   715  N  N   . ASN A 1 87  ? -7.258  13.265 -5.781  1.00 29.32  ? 86  ASN A N   1 
ATOM   716  C  CA  . ASN A 1 87  ? -8.262  13.118 -6.859  1.00 33.69  ? 86  ASN A CA  1 
ATOM   717  C  C   . ASN A 1 87  ? -7.782  13.945 -8.047  1.00 42.11  ? 86  ASN A C   1 
ATOM   718  O  O   . ASN A 1 87  ? -8.619  14.468 -8.786  1.00 31.27  ? 86  ASN A O   1 
ATOM   719  C  CB  . ASN A 1 87  ? -9.647  13.597 -6.423  1.00 34.69  ? 86  ASN A CB  1 
ATOM   720  C  CG  . ASN A 1 87  ? -10.270 12.722 -5.361  1.00 44.59  ? 86  ASN A CG  1 
ATOM   721  O  OD1 . ASN A 1 87  ? -10.584 13.187 -4.271  1.00 50.99  ? 86  ASN A OD1 1 
ATOM   722  N  ND2 . ASN A 1 87  ? -10.458 11.456 -5.679  1.00 38.62  ? 86  ASN A ND2 1 
ATOM   723  N  N   . GLN A 1 88  ? -6.471  14.086 -8.214  1.00 31.19  ? 87  GLN A N   1 
ATOM   724  C  CA  . GLN A 1 88  ? -5.926  14.943 -9.294  1.00 37.96  ? 87  GLN A CA  1 
ATOM   725  C  C   . GLN A 1 88  ? -5.943  14.172 -10.618 1.00 39.29  ? 87  GLN A C   1 
ATOM   726  O  O   . GLN A 1 88  ? -5.891  12.933 -10.604 1.00 39.31  ? 87  GLN A O   1 
ATOM   727  C  CB  . GLN A 1 88  ? -4.548  15.455 -8.891  1.00 25.63  ? 87  GLN A CB  1 
ATOM   728  C  CG  . GLN A 1 88  ? -4.600  16.345 -7.678  1.00 32.21  ? 87  GLN A CG  1 
ATOM   729  C  CD  . GLN A 1 88  ? -3.221  16.532 -7.096  1.00 36.26  ? 87  GLN A CD  1 
ATOM   730  O  OE1 . GLN A 1 88  ? -2.388  15.622 -7.123  1.00 29.26  ? 87  GLN A OE1 1 
ATOM   731  N  NE2 . GLN A 1 88  ? -2.969  17.732 -6.595  1.00 28.96  ? 87  GLN A NE2 1 
ATOM   732  N  N   . SER A 1 89  ? -6.005  14.911 -11.724 1.00 50.52  ? 88  SER A N   1 
ATOM   733  C  CA  . SER A 1 89  ? -5.926  14.405 -13.116 1.00 53.48  ? 88  SER A CA  1 
ATOM   734  C  C   . SER A 1 89  ? -4.517  13.874 -13.378 1.00 53.67  ? 88  SER A C   1 
ATOM   735  O  O   . SER A 1 89  ? -3.621  14.183 -12.595 1.00 38.34  ? 88  SER A O   1 
ATOM   736  C  CB  . SER A 1 89  ? -6.288  15.507 -14.101 1.00 71.05  ? 88  SER A CB  1 
ATOM   737  O  OG  . SER A 1 89  ? -5.578  16.720 -13.836 1.00 52.39  ? 88  SER A OG  1 
ATOM   738  N  N   . GLU A 1 90  ? -4.316  13.168 -14.490 1.00 53.65  ? 89  GLU A N   1 
ATOM   739  C  CA  . GLU A 1 90  ? -2.989  12.624 -14.891 1.00 49.07  ? 89  GLU A CA  1 
ATOM   740  C  C   . GLU A 1 90  ? -2.248  13.677 -15.743 1.00 39.38  ? 89  GLU A C   1 
ATOM   741  O  O   . GLU A 1 90  ? -1.032  13.510 -15.975 1.00 49.68  ? 89  GLU A O   1 
ATOM   742  C  CB  . GLU A 1 90  ? -3.149  11.292 -15.637 1.00 74.39  ? 89  GLU A CB  1 
ATOM   743  C  CG  . GLU A 1 90  ? -4.331  10.436 -15.183 1.00 86.00  ? 89  GLU A CG  1 
ATOM   744  C  CD  . GLU A 1 90  ? -4.123  9.628  -13.908 1.00 104.10 ? 89  GLU A CD  1 
ATOM   745  O  OE1 . GLU A 1 90  ? -4.285  8.394  -13.977 1.00 92.80  ? 89  GLU A OE1 1 
ATOM   746  O  OE2 . GLU A 1 90  ? -3.819  10.225 -12.841 1.00 102.57 ? 89  GLU A OE2 1 
ATOM   747  N  N   . ALA A 1 91  ? -2.930  14.743 -16.163 1.00 39.67  ? 90  ALA A N   1 
ATOM   748  C  CA  . ALA A 1 91  ? -2.398  15.799 -17.066 1.00 49.70  ? 90  ALA A CA  1 
ATOM   749  C  C   . ALA A 1 91  ? -1.562  16.868 -16.328 1.00 50.65  ? 90  ALA A C   1 
ATOM   750  O  O   . ALA A 1 91  ? -0.707  17.478 -16.976 1.00 46.13  ? 90  ALA A O   1 
ATOM   751  C  CB  . ALA A 1 91  ? -3.539  16.455 -17.800 1.00 57.85  ? 90  ALA A CB  1 
ATOM   752  N  N   . GLY A 1 92  ? -1.821  17.164 -15.055 1.00 36.38  ? 91  GLY A N   1 
ATOM   753  C  CA  . GLY A 1 92  ? -1.089  18.232 -14.345 1.00 40.97  ? 91  GLY A CA  1 
ATOM   754  C  C   . GLY A 1 92  ? 0.299   17.784 -13.881 1.00 33.73  ? 91  GLY A C   1 
ATOM   755  O  O   . GLY A 1 92  ? 0.466   16.583 -13.521 1.00 35.20  ? 91  GLY A O   1 
ATOM   756  N  N   . SER A 1 93  ? 1.273   18.697 -13.894 1.00 36.45  ? 92  SER A N   1 
ATOM   757  C  CA  . SER A 1 93  ? 2.607   18.493 -13.284 1.00 29.14  ? 92  SER A CA  1 
ATOM   758  C  C   . SER A 1 93  ? 2.455   18.655 -11.764 1.00 29.82  ? 92  SER A C   1 
ATOM   759  O  O   . SER A 1 93  ? 1.675   19.508 -11.312 1.00 28.55  ? 92  SER A O   1 
ATOM   760  C  CB  . SER A 1 93  ? 3.624   19.422 -13.886 1.00 37.43  ? 92  SER A CB  1 
ATOM   761  O  OG  . SER A 1 93  ? 4.859   19.368 -13.169 1.00 31.86  ? 92  SER A OG  1 
ATOM   762  N  N   . HIS A 1 94  ? 3.166   17.863 -10.977 1.00 29.58  ? 93  HIS A N   1 
ATOM   763  C  CA  . HIS A 1 94  ? 3.162   17.987 -9.501  1.00 27.63  ? 93  HIS A CA  1 
ATOM   764  C  C   . HIS A 1 94  ? 4.608   17.853 -8.991  1.00 25.17  ? 93  HIS A C   1 
ATOM   765  O  O   . HIS A 1 94  ? 5.461   17.326 -9.712  1.00 25.12  ? 93  HIS A O   1 
ATOM   766  C  CB  . HIS A 1 94  ? 2.222   16.946 -8.881  1.00 26.73  ? 93  HIS A CB  1 
ATOM   767  C  CG  . HIS A 1 94  ? 0.808   17.136 -9.314  1.00 23.80  ? 93  HIS A CG  1 
ATOM   768  N  ND1 . HIS A 1 94  ? -0.052  18.004 -8.665  1.00 24.68  ? 93  HIS A ND1 1 
ATOM   769  C  CD2 . HIS A 1 94  ? 0.139   16.631 -10.384 1.00 30.84  ? 93  HIS A CD2 1 
ATOM   770  C  CE1 . HIS A 1 94  ? -1.209  17.998 -9.301  1.00 29.53  ? 93  HIS A CE1 1 
ATOM   771  N  NE2 . HIS A 1 94  ? -1.109  17.170 -10.365 1.00 26.85  ? 93  HIS A NE2 1 
ATOM   772  N  N   . THR A 1 95  ? 4.838   18.400 -7.806  1.00 25.16  ? 94  THR A N   1 
ATOM   773  C  CA  . THR A 1 95  ? 6.153   18.486 -7.170  1.00 20.86  ? 94  THR A CA  1 
ATOM   774  C  C   . THR A 1 95  ? 6.077   17.789 -5.819  1.00 20.94  ? 94  THR A C   1 
ATOM   775  O  O   . THR A 1 95  ? 5.164   18.125 -5.037  1.00 23.52  ? 94  THR A O   1 
ATOM   776  C  CB  . THR A 1 95  ? 6.556   19.948 -6.957  1.00 24.61  ? 94  THR A CB  1 
ATOM   777  O  OG1 . THR A 1 95  ? 6.525   20.556 -8.240  1.00 24.01  ? 94  THR A OG1 1 
ATOM   778  C  CG2 . THR A 1 95  ? 7.932   20.075 -6.343  1.00 24.66  ? 94  THR A CG2 1 
ATOM   779  N  N   . LEU A 1 96  ? 7.073   16.941 -5.549  1.00 20.85  ? 95  LEU A N   1 
ATOM   780  C  CA  . LEU A 1 96  ? 7.377   16.450 -4.189  1.00 22.28  ? 95  LEU A CA  1 
ATOM   781  C  C   . LEU A 1 96  ? 8.743   16.981 -3.770  1.00 22.88  ? 95  LEU A C   1 
ATOM   782  O  O   . LEU A 1 96  ? 9.774   16.666 -4.435  1.00 26.14  ? 95  LEU A O   1 
ATOM   783  C  CB  . LEU A 1 96  ? 7.364   14.926 -4.157  1.00 23.93  ? 95  LEU A CB  1 
ATOM   784  C  CG  . LEU A 1 96  ? 7.549   14.287 -2.787  1.00 22.69  ? 95  LEU A CG  1 
ATOM   785  C  CD1 . LEU A 1 96  ? 6.401   14.641 -1.860  1.00 20.80  ? 95  LEU A CD1 1 
ATOM   786  C  CD2 . LEU A 1 96  ? 7.718   12.766 -2.948  1.00 27.18  ? 95  LEU A CD2 1 
ATOM   787  N  N   . GLN A 1 97  ? 8.749   17.681 -2.645  1.00 24.58  ? 96  GLN A N   1 
ATOM   788  C  CA  . GLN A 1 97  ? 9.970   18.157 -1.966  1.00 21.48  ? 96  GLN A CA  1 
ATOM   789  C  C   . GLN A 1 97  ? 10.155  17.303 -0.713  1.00 22.40  ? 96  GLN A C   1 
ATOM   790  O  O   . GLN A 1 97  ? 9.197   17.077 -0.007  1.00 21.50  ? 96  GLN A O   1 
ATOM   791  C  CB  . GLN A 1 97  ? 9.891   19.645 -1.619  1.00 22.90  ? 96  GLN A CB  1 
ATOM   792  C  CG  . GLN A 1 97  ? 9.980   20.568 -2.828  1.00 22.26  ? 96  GLN A CG  1 
ATOM   793  C  CD  . GLN A 1 97  ? 9.581   21.973 -2.462  1.00 23.11  ? 96  GLN A CD  1 
ATOM   794  O  OE1 . GLN A 1 97  ? 8.408   22.347 -2.524  1.00 23.54  ? 96  GLN A OE1 1 
ATOM   795  N  NE2 . GLN A 1 97  ? 10.557  22.736 -1.982  1.00 20.95  ? 96  GLN A NE2 1 
ATOM   796  N  N   . SER A 1 98  ? 11.347  16.758 -0.536  1.00 24.45  ? 97  SER A N   1 
ATOM   797  C  CA  . SER A 1 98  ? 11.690  15.925 0.628   1.00 24.15  ? 97  SER A CA  1 
ATOM   798  C  C   . SER A 1 98  ? 12.942  16.508 1.228   1.00 20.68  ? 97  SER A C   1 
ATOM   799  O  O   . SER A 1 98  ? 13.895  16.840 0.468   1.00 24.18  ? 97  SER A O   1 
ATOM   800  C  CB  . SER A 1 98  ? 11.906  14.473 0.262   1.00 26.02  ? 97  SER A CB  1 
ATOM   801  O  OG  . SER A 1 98  ? 10.898  14.015 -0.579  1.00 23.72  ? 97  SER A OG  1 
ATOM   802  N  N   . MET A 1 99  ? 12.978  16.590 2.551   1.00 23.53  ? 98  MET A N   1 
ATOM   803  C  CA  . MET A 1 99  ? 14.201  17.018 3.255   1.00 21.75  ? 98  MET A CA  1 
ATOM   804  C  C   . MET A 1 99  ? 14.379  16.097 4.452   1.00 21.24  ? 98  MET A C   1 
ATOM   805  O  O   . MET A 1 99  ? 13.427  15.911 5.197   1.00 19.48  ? 98  MET A O   1 
ATOM   806  C  CB  . MET A 1 99  ? 14.118  18.457 3.754   1.00 22.51  ? 98  MET A CB  1 
ATOM   807  C  CG  . MET A 1 99  ? 15.445  18.938 4.305   1.00 35.23  ? 98  MET A CG  1 
ATOM   808  S  SD  . MET A 1 99  ? 15.747  18.422 6.036   1.00 38.37  ? 98  MET A SD  1 
ATOM   809  C  CE  . MET A 1 99  ? 14.914  19.789 6.843   1.00 40.87  ? 98  MET A CE  1 
ATOM   810  N  N   . TYR A 1 100 ? 15.556  15.540 4.617   1.00 20.72  ? 99  TYR A N   1 
ATOM   811  C  CA  . TYR A 1 100 ? 15.845  14.736 5.823   1.00 23.08  ? 99  TYR A CA  1 
ATOM   812  C  C   . TYR A 1 100 ? 17.263  15.044 6.246   1.00 27.04  ? 99  TYR A C   1 
ATOM   813  O  O   . TYR A 1 100 ? 18.069  15.496 5.427   1.00 24.20  ? 99  TYR A O   1 
ATOM   814  C  CB  . TYR A 1 100 ? 15.628  13.239 5.617   1.00 21.45  ? 99  TYR A CB  1 
ATOM   815  C  CG  . TYR A 1 100 ? 16.584  12.630 4.627   1.00 23.49  ? 99  TYR A CG  1 
ATOM   816  C  CD1 . TYR A 1 100 ? 17.793  12.116 5.038   1.00 21.92  ? 99  TYR A CD1 1 
ATOM   817  C  CD2 . TYR A 1 100 ? 16.285  12.610 3.272   1.00 25.38  ? 99  TYR A CD2 1 
ATOM   818  C  CE1 . TYR A 1 100 ? 18.700  11.580 4.139   1.00 25.32  ? 99  TYR A CE1 1 
ATOM   819  C  CE2 . TYR A 1 100 ? 17.177  12.083 2.349   1.00 27.80  ? 99  TYR A CE2 1 
ATOM   820  C  CZ  . TYR A 1 100 ? 18.375  11.540 2.788   1.00 24.42  ? 99  TYR A CZ  1 
ATOM   821  O  OH  . TYR A 1 100 ? 19.257  11.055 1.882   1.00 21.43  ? 99  TYR A OH  1 
ATOM   822  N  N   . GLY A 1 101 ? 17.562  14.762 7.515   1.00 24.12  ? 100 GLY A N   1 
ATOM   823  C  CA  . GLY A 1 101 ? 18.949  14.905 7.949   1.00 23.14  ? 100 GLY A CA  1 
ATOM   824  C  C   . GLY A 1 101 ? 19.063  14.906 9.452   1.00 23.21  ? 100 GLY A C   1 
ATOM   825  O  O   . GLY A 1 101 ? 18.043  14.757 10.157  1.00 23.30  ? 100 GLY A O   1 
ATOM   826  N  N   . CYS A 1 102 ? 20.278  15.119 9.908   1.00 27.08  ? 101 CYS A N   1 
ATOM   827  C  CA  . CYS A 1 102 ? 20.620  15.028 11.338  1.00 26.78  ? 101 CYS A CA  1 
ATOM   828  C  C   . CYS A 1 102 ? 21.383  16.289 11.734  1.00 26.03  ? 101 CYS A C   1 
ATOM   829  O  O   . CYS A 1 102 ? 22.235  16.730 10.948  1.00 27.43  ? 101 CYS A O   1 
ATOM   830  C  CB  . CYS A 1 102 ? 21.414  13.743 11.587  1.00 29.79  ? 101 CYS A CB  1 
ATOM   831  S  SG  . CYS A 1 102 ? 22.738  13.455 10.384  1.00 29.75  ? 101 CYS A SG  1 
ATOM   832  N  N   . ASP A 1 103 ? 21.045  16.813 12.910  1.00 28.05  ? 102 ASP A N   1 
ATOM   833  C  CA  . ASP A 1 103 ? 21.782  17.890 13.607  1.00 32.35  ? 102 ASP A CA  1 
ATOM   834  C  C   . ASP A 1 103 ? 22.498  17.256 14.808  1.00 30.23  ? 102 ASP A C   1 
ATOM   835  O  O   . ASP A 1 103 ? 21.862  16.479 15.532  1.00 32.04  ? 102 ASP A O   1 
ATOM   836  C  CB  . ASP A 1 103 ? 20.857  18.979 14.128  1.00 31.10  ? 102 ASP A CB  1 
ATOM   837  C  CG  . ASP A 1 103 ? 19.920  19.620 13.116  1.00 42.24  ? 102 ASP A CG  1 
ATOM   838  O  OD1 . ASP A 1 103 ? 20.141  19.475 11.874  1.00 32.21  ? 102 ASP A OD1 1 
ATOM   839  O  OD2 . ASP A 1 103 ? 18.978  20.268 13.585  1.00 35.13  ? 102 ASP A OD2 1 
ATOM   840  N  N   . VAL A 1 104 ? 23.775  17.547 14.975  1.00 30.11  ? 103 VAL A N   1 
ATOM   841  C  CA  . VAL A 1 104 ? 24.601  16.977 16.075  1.00 39.44  ? 103 VAL A CA  1 
ATOM   842  C  C   . VAL A 1 104 ? 25.190  18.147 16.850  1.00 37.52  ? 103 VAL A C   1 
ATOM   843  O  O   . VAL A 1 104 ? 25.452  19.185 16.229  1.00 36.93  ? 103 VAL A O   1 
ATOM   844  C  CB  . VAL A 1 104 ? 25.709  16.036 15.560  1.00 37.98  ? 103 VAL A CB  1 
ATOM   845  C  CG1 . VAL A 1 104 ? 25.130  14.872 14.763  1.00 40.03  ? 103 VAL A CG1 1 
ATOM   846  C  CG2 . VAL A 1 104 ? 26.776  16.782 14.767  1.00 36.56  ? 103 VAL A CG2 1 
ATOM   847  N  N   . GLY A 1 105 ? 25.396  17.969 18.158  1.00 45.66  ? 104 GLY A N   1 
ATOM   848  C  CA  . GLY A 1 105 ? 26.124  18.949 18.975  1.00 39.54  ? 104 GLY A CA  1 
ATOM   849  C  C   . GLY A 1 105 ? 27.613  18.633 18.952  1.00 60.44  ? 104 GLY A C   1 
ATOM   850  O  O   . GLY A 1 105 ? 28.039  17.796 18.156  1.00 51.69  ? 104 GLY A O   1 
ATOM   851  N  N   . PRO A 1 106 ? 28.429  19.277 19.823  1.00 67.45  ? 105 PRO A N   1 
ATOM   852  C  CA  . PRO A 1 106 ? 29.873  19.035 19.870  1.00 61.40  ? 105 PRO A CA  1 
ATOM   853  C  C   . PRO A 1 106 ? 30.237  17.577 20.198  1.00 63.12  ? 105 PRO A C   1 
ATOM   854  O  O   . PRO A 1 106 ? 31.199  17.108 19.632  1.00 54.85  ? 105 PRO A O   1 
ATOM   855  C  CB  . PRO A 1 106 ? 30.368  20.002 20.957  1.00 65.98  ? 105 PRO A CB  1 
ATOM   856  C  CG  . PRO A 1 106 ? 29.293  21.071 21.014  1.00 65.58  ? 105 PRO A CG  1 
ATOM   857  C  CD  . PRO A 1 106 ? 28.008  20.303 20.789  1.00 69.51  ? 105 PRO A CD  1 
ATOM   858  N  N   . ASP A 1 107 ? 29.457  16.889 21.047  1.00 62.10  ? 106 ASP A N   1 
ATOM   859  C  CA  . ASP A 1 107 ? 29.666  15.444 21.354  1.00 59.37  ? 106 ASP A CA  1 
ATOM   860  C  C   . ASP A 1 107 ? 29.505  14.626 20.060  1.00 79.41  ? 106 ASP A C   1 
ATOM   861  O  O   . ASP A 1 107 ? 30.053  13.508 19.983  1.00 60.07  ? 106 ASP A O   1 
ATOM   862  C  CB  . ASP A 1 107 ? 28.746  14.944 22.474  1.00 60.82  ? 106 ASP A CB  1 
ATOM   863  C  CG  . ASP A 1 107 ? 27.289  14.719 22.096  1.00 88.50  ? 106 ASP A CG  1 
ATOM   864  O  OD1 . ASP A 1 107 ? 26.930  14.982 20.921  1.00 70.36  ? 106 ASP A OD1 1 
ATOM   865  O  OD2 . ASP A 1 107 ? 26.515  14.277 22.987  1.00 75.70  ? 106 ASP A OD2 1 
ATOM   866  N  N   . GLY A 1 108 ? 28.767  15.151 19.078  1.00 62.61  ? 107 GLY A N   1 
ATOM   867  C  CA  . GLY A 1 108 ? 28.612  14.524 17.755  1.00 58.28  ? 107 GLY A CA  1 
ATOM   868  C  C   . GLY A 1 108 ? 27.558  13.433 17.773  1.00 50.49  ? 107 GLY A C   1 
ATOM   869  O  O   . GLY A 1 108 ? 27.576  12.592 16.872  1.00 62.51  ? 107 GLY A O   1 
ATOM   870  N  N   . ARG A 1 109 ? 26.667  13.442 18.765  1.00 48.12  ? 108 ARG A N   1 
ATOM   871  C  CA  . ARG A 1 109 ? 25.481  12.551 18.808  1.00 58.51  ? 108 ARG A CA  1 
ATOM   872  C  C   . ARG A 1 109 ? 24.274  13.374 18.339  1.00 42.46  ? 108 ARG A C   1 
ATOM   873  O  O   . ARG A 1 109 ? 24.301  14.612 18.487  1.00 43.98  ? 108 ARG A O   1 
ATOM   874  C  CB  . ARG A 1 109 ? 25.275  11.979 20.211  1.00 51.01  ? 108 ARG A CB  1 
ATOM   875  N  N   . LEU A 1 110 ? 23.276  12.698 17.770  1.00 42.15  ? 109 LEU A N   1 
ATOM   876  C  CA  . LEU A 1 110 ? 22.032  13.335 17.267  1.00 45.05  ? 109 LEU A CA  1 
ATOM   877  C  C   . LEU A 1 110 ? 21.490  14.284 18.341  1.00 48.73  ? 109 LEU A C   1 
ATOM   878  O  O   . LEU A 1 110 ? 21.346  13.874 19.494  1.00 41.32  ? 109 LEU A O   1 
ATOM   879  C  CB  . LEU A 1 110 ? 20.979  12.286 16.889  1.00 44.78  ? 109 LEU A CB  1 
ATOM   880  C  CG  . LEU A 1 110 ? 19.778  12.855 16.127  1.00 42.96  ? 109 LEU A CG  1 
ATOM   881  C  CD1 . LEU A 1 110 ? 20.207  13.353 14.759  1.00 44.28  ? 109 LEU A CD1 1 
ATOM   882  C  CD2 . LEU A 1 110 ? 18.686  11.823 15.990  1.00 51.15  ? 109 LEU A CD2 1 
ATOM   883  N  N   . LEU A 1 111 ? 21.255  15.528 17.948  1.00 31.72  ? 110 LEU A N   1 
ATOM   884  C  CA  . LEU A 1 111 ? 20.553  16.563 18.736  1.00 36.22  ? 110 LEU A CA  1 
ATOM   885  C  C   . LEU A 1 111 ? 19.106  16.671 18.224  1.00 39.66  ? 110 LEU A C   1 
ATOM   886  O  O   . LEU A 1 111 ? 18.198  16.874 19.015  1.00 38.02  ? 110 LEU A O   1 
ATOM   887  C  CB  . LEU A 1 111 ? 21.336  17.863 18.554  1.00 42.29  ? 110 LEU A CB  1 
ATOM   888  C  CG  . LEU A 1 111 ? 21.292  18.841 19.719  1.00 61.44  ? 110 LEU A CG  1 
ATOM   889  C  CD1 . LEU A 1 111 ? 22.179  18.353 20.857  1.00 64.47  ? 110 LEU A CD1 1 
ATOM   890  C  CD2 . LEU A 1 111 ? 21.717  20.230 19.255  1.00 62.98  ? 110 LEU A CD2 1 
ATOM   891  N  N   . ARG A 1 112 ? 18.891  16.472 16.924  1.00 40.74  ? 111 ARG A N   1 
ATOM   892  C  CA  . ARG A 1 112 ? 17.582  16.683 16.260  1.00 31.17  ? 111 ARG A CA  1 
ATOM   893  C  C   . ARG A 1 112 ? 17.631  16.005 14.885  1.00 29.36  ? 111 ARG A C   1 
ATOM   894  O  O   . ARG A 1 112 ? 18.637  16.187 14.145  1.00 32.50  ? 111 ARG A O   1 
ATOM   895  C  CB  . ARG A 1 112 ? 17.274  18.185 16.185  1.00 42.59  ? 111 ARG A CB  1 
ATOM   896  C  CG  . ARG A 1 112 ? 16.036  18.555 15.374  1.00 49.15  ? 111 ARG A CG  1 
ATOM   897  C  CD  . ARG A 1 112 ? 14.768  17.903 15.905  1.00 72.26  ? 111 ARG A CD  1 
ATOM   898  N  NE  . ARG A 1 112 ? 13.531  18.297 15.230  1.00 63.00  ? 111 ARG A NE  1 
ATOM   899  C  CZ  . ARG A 1 112 ? 12.965  19.502 15.304  1.00 87.79  ? 111 ARG A CZ  1 
ATOM   900  N  NH1 . ARG A 1 112 ? 11.838  19.726 14.651  1.00 98.54  ? 111 ARG A NH1 1 
ATOM   901  N  NH2 . ARG A 1 112 ? 13.518  20.480 16.008  1.00 77.32  ? 111 ARG A NH2 1 
ATOM   902  N  N   . GLY A 1 113 ? 16.587  15.230 14.595  1.00 31.05  ? 112 GLY A N   1 
ATOM   903  C  CA  . GLY A 1 113 ? 16.358  14.535 13.323  1.00 32.72  ? 112 GLY A CA  1 
ATOM   904  C  C   . GLY A 1 113 ? 15.258  15.241 12.552  1.00 30.70  ? 112 GLY A C   1 
ATOM   905  O  O   . GLY A 1 113 ? 14.315  15.764 13.193  1.00 30.86  ? 112 GLY A O   1 
ATOM   906  N  N   . HIS A 1 114 ? 15.382  15.267 11.226  1.00 28.52  ? 113 HIS A N   1 
ATOM   907  C  CA  . HIS A 1 114 ? 14.359  15.848 10.332  1.00 24.57  ? 113 HIS A CA  1 
ATOM   908  C  C   . HIS A 1 114 ? 14.068  14.841 9.254   1.00 21.53  ? 113 HIS A C   1 
ATOM   909  O  O   . HIS A 1 114 ? 15.052  14.256 8.746   1.00 25.69  ? 113 HIS A O   1 
ATOM   910  C  CB  . HIS A 1 114 ? 14.866  17.106 9.623   1.00 28.47  ? 113 HIS A CB  1 
ATOM   911  C  CG  . HIS A 1 114 ? 15.396  18.127 10.557  1.00 28.57  ? 113 HIS A CG  1 
ATOM   912  N  ND1 . HIS A 1 114 ? 14.587  19.023 11.166  1.00 27.67  ? 113 HIS A ND1 1 
ATOM   913  C  CD2 . HIS A 1 114 ? 16.647  18.360 11.001  1.00 35.23  ? 113 HIS A CD2 1 
ATOM   914  C  CE1 . HIS A 1 114 ? 15.306  19.788 11.967  1.00 31.38  ? 113 HIS A CE1 1 
ATOM   915  N  NE2 . HIS A 1 114 ? 16.582  19.406 11.869  1.00 39.34  ? 113 HIS A NE2 1 
ATOM   916  N  N   . ASP A 1 115 ? 12.802  14.744 8.864   1.00 23.53  ? 114 ASP A N   1 
ATOM   917  C  CA  . ASP A 1 115 ? 12.376  13.851 7.770   1.00 19.38  ? 114 ASP A CA  1 
ATOM   918  C  C   . ASP A 1 115 ? 10.986  14.282 7.357   1.00 23.22  ? 114 ASP A C   1 
ATOM   919  O  O   . ASP A 1 115 ? 10.011  13.941 8.068   1.00 25.21  ? 114 ASP A O   1 
ATOM   920  C  CB  . ASP A 1 115 ? 12.463  12.406 8.252   1.00 21.93  ? 114 ASP A CB  1 
ATOM   921  C  CG  . ASP A 1 115 ? 12.513  11.368 7.160   1.00 27.00  ? 114 ASP A CG  1 
ATOM   922  O  OD1 . ASP A 1 115 ? 12.267  11.743 5.965   1.00 26.32  ? 114 ASP A OD1 1 
ATOM   923  O  OD2 . ASP A 1 115 ? 12.778  10.173 7.512   1.00 26.88  ? 114 ASP A OD2 1 
ATOM   924  N  N   . GLN A 1 116 ? 10.884  15.076 6.286   1.00 22.22  ? 115 GLN A N   1 
ATOM   925  C  CA  . GLN A 1 116 ? 9.609   15.785 6.038   1.00 21.23  ? 115 GLN A CA  1 
ATOM   926  C  C   . GLN A 1 116 ? 9.394   15.963 4.537   1.00 22.71  ? 115 GLN A C   1 
ATOM   927  O  O   . GLN A 1 116 ? 10.335  15.731 3.756   1.00 21.99  ? 115 GLN A O   1 
ATOM   928  C  CB  . GLN A 1 116 ? 9.588   17.119 6.791   1.00 25.51  ? 115 GLN A CB  1 
ATOM   929  C  CG  . GLN A 1 116 ? 10.757  18.052 6.522   1.00 27.05  ? 115 GLN A CG  1 
ATOM   930  C  CD  . GLN A 1 116 ? 10.887  19.112 7.600   1.00 37.28  ? 115 GLN A CD  1 
ATOM   931  O  OE1 . GLN A 1 116 ? 11.246  20.238 7.319   1.00 36.02  ? 115 GLN A OE1 1 
ATOM   932  N  NE2 . GLN A 1 116 ? 10.602  18.762 8.850   1.00 38.13  ? 115 GLN A NE2 1 
ATOM   933  N  N   . TYR A 1 117 ? 8.163   16.306 4.192   1.00 23.66  ? 116 TYR A N   1 
ATOM   934  C  CA  . TYR A 1 117 ? 7.639   16.267 2.808   1.00 22.00  ? 116 TYR A CA  1 
ATOM   935  C  C   . TYR A 1 117 ? 6.671   17.430 2.578   1.00 23.21  ? 116 TYR A C   1 
ATOM   936  O  O   . TYR A 1 117 ? 5.842   17.785 3.451   1.00 23.73  ? 116 TYR A O   1 
ATOM   937  C  CB  . TYR A 1 117 ? 6.917   14.961 2.511   1.00 21.69  ? 116 TYR A CB  1 
ATOM   938  C  CG  . TYR A 1 117 ? 7.759   13.726 2.737   1.00 24.30  ? 116 TYR A CG  1 
ATOM   939  C  CD1 . TYR A 1 117 ? 7.860   13.132 3.994   1.00 23.69  ? 116 TYR A CD1 1 
ATOM   940  C  CD2 . TYR A 1 117 ? 8.438   13.134 1.680   1.00 25.14  ? 116 TYR A CD2 1 
ATOM   941  C  CE1 . TYR A 1 117 ? 8.683   12.029 4.196   1.00 22.79  ? 116 TYR A CE1 1 
ATOM   942  C  CE2 . TYR A 1 117 ? 9.205   11.993 1.854   1.00 28.30  ? 116 TYR A CE2 1 
ATOM   943  C  CZ  . TYR A 1 117 ? 9.356   11.462 3.122   1.00 27.62  ? 116 TYR A CZ  1 
ATOM   944  O  OH  . TYR A 1 117 ? 10.134  10.343 3.278   1.00 24.29  ? 116 TYR A OH  1 
ATOM   945  N  N   . ALA A 1 118 ? 6.794   17.999 1.387   1.00 21.60  ? 117 ALA A N   1 
ATOM   946  C  CA  . ALA A 1 118 ? 5.865   19.023 0.872   1.00 26.05  ? 117 ALA A CA  1 
ATOM   947  C  C   . ALA A 1 118 ? 5.397   18.551 -0.489  1.00 22.00  ? 117 ALA A C   1 
ATOM   948  O  O   . ALA A 1 118 ? 6.250   18.100 -1.280  1.00 22.40  ? 117 ALA A O   1 
ATOM   949  C  CB  . ALA A 1 118 ? 6.536   20.369 0.790   1.00 27.49  ? 117 ALA A CB  1 
ATOM   950  N  N   . TYR A 1 119 ? 4.093   18.645 -0.739  1.00 25.54  ? 118 TYR A N   1 
ATOM   951  C  CA  . TYR A 1 119 ? 3.487   18.305 -2.036  1.00 25.73  ? 118 TYR A CA  1 
ATOM   952  C  C   . TYR A 1 119 ? 2.919   19.587 -2.658  1.00 22.19  ? 118 TYR A C   1 
ATOM   953  O  O   . TYR A 1 119 ? 2.176   20.311 -1.995  1.00 23.21  ? 118 TYR A O   1 
ATOM   954  C  CB  . TYR A 1 119 ? 2.425   17.227 -1.868  1.00 24.94  ? 118 TYR A CB  1 
ATOM   955  C  CG  . TYR A 1 119 ? 1.814   16.775 -3.170  1.00 23.88  ? 118 TYR A CG  1 
ATOM   956  C  CD1 . TYR A 1 119 ? 2.596   16.266 -4.188  1.00 24.96  ? 118 TYR A CD1 1 
ATOM   957  C  CD2 . TYR A 1 119 ? 0.434   16.813 -3.362  1.00 26.34  ? 118 TYR A CD2 1 
ATOM   958  C  CE1 . TYR A 1 119 ? 2.049   15.860 -5.389  1.00 21.28  ? 118 TYR A CE1 1 
ATOM   959  C  CE2 . TYR A 1 119 ? -0.141  16.384 -4.543  1.00 24.17  ? 118 TYR A CE2 1 
ATOM   960  C  CZ  . TYR A 1 119 ? 0.669   15.902 -5.557  1.00 23.59  ? 118 TYR A CZ  1 
ATOM   961  O  OH  . TYR A 1 119 ? 0.127   15.450 -6.712  1.00 27.98  ? 118 TYR A OH  1 
ATOM   962  N  N   . ASP A 1 120 ? 3.258   19.825 -3.910  1.00 22.72  ? 119 ASP A N   1 
ATOM   963  C  CA  . ASP A 1 120 ? 2.855   21.058 -4.634  1.00 22.57  ? 119 ASP A CA  1 
ATOM   964  C  C   . ASP A 1 120 ? 3.039   22.285 -3.739  1.00 24.59  ? 119 ASP A C   1 
ATOM   965  O  O   . ASP A 1 120 ? 2.166   23.173 -3.746  1.00 24.75  ? 119 ASP A O   1 
ATOM   966  C  CB  . ASP A 1 120 ? 1.414   20.888 -5.122  1.00 24.61  ? 119 ASP A CB  1 
ATOM   967  C  CG  . ASP A 1 120 ? 1.279   19.940 -6.293  1.00 23.77  ? 119 ASP A CG  1 
ATOM   968  O  OD1 . ASP A 1 120 ? 2.292   19.669 -6.918  1.00 25.10  ? 119 ASP A OD1 1 
ATOM   969  O  OD2 . ASP A 1 120 ? 0.133   19.521 -6.590  1.00 28.75  ? 119 ASP A OD2 1 
ATOM   970  N  N   . GLY A 1 121 ? 4.192   22.382 -3.060  1.00 22.68  ? 120 GLY A N   1 
ATOM   971  C  CA  . GLY A 1 121 ? 4.625   23.606 -2.372  1.00 25.07  ? 120 GLY A CA  1 
ATOM   972  C  C   . GLY A 1 121 ? 3.966   23.805 -1.022  1.00 26.95  ? 120 GLY A C   1 
ATOM   973  O  O   . GLY A 1 121 ? 4.179   24.888 -0.464  1.00 26.75  ? 120 GLY A O   1 
ATOM   974  N  N   . LYS A 1 122 ? 3.176   22.839 -0.533  1.00 24.86  ? 121 LYS A N   1 
ATOM   975  C  CA  . LYS A 1 122 ? 2.439   22.903 0.757   1.00 25.27  ? 121 LYS A CA  1 
ATOM   976  C  C   . LYS A 1 122 ? 2.946   21.760 1.647   1.00 25.10  ? 121 LYS A C   1 
ATOM   977  O  O   . LYS A 1 122 ? 3.238   20.660 1.092   1.00 24.14  ? 121 LYS A O   1 
ATOM   978  C  CB  . LYS A 1 122 ? 0.920   22.781 0.549   1.00 30.31  ? 121 LYS A CB  1 
ATOM   979  C  CG  . LYS A 1 122 ? 0.250   23.987 -0.113  1.00 37.94  ? 121 LYS A CG  1 
ATOM   980  C  CD  . LYS A 1 122 ? 0.501   25.311 0.616   1.00 59.43  ? 121 LYS A CD  1 
ATOM   981  C  CE  . LYS A 1 122 ? -0.056  26.542 -0.083  1.00 71.94  ? 121 LYS A CE  1 
ATOM   982  N  NZ  . LYS A 1 122 ? -0.447  27.596 0.889   1.00 59.05  ? 121 LYS A NZ  1 
ATOM   983  N  N   . ASP A 1 123 ? 3.024   21.991 2.958   1.00 24.11  ? 122 ASP A N   1 
ATOM   984  C  CA  . ASP A 1 123 ? 3.320   20.932 3.961   1.00 24.85  ? 122 ASP A CA  1 
ATOM   985  C  C   . ASP A 1 123 ? 2.489   19.695 3.668   1.00 25.45  ? 122 ASP A C   1 
ATOM   986  O  O   . ASP A 1 123 ? 1.269   19.796 3.379   1.00 22.06  ? 122 ASP A O   1 
ATOM   987  C  CB  . ASP A 1 123 ? 3.000   21.345 5.395   1.00 28.64  ? 122 ASP A CB  1 
ATOM   988  C  CG  . ASP A 1 123 ? 3.789   22.504 5.974   1.00 37.55  ? 122 ASP A CG  1 
ATOM   989  O  OD1 . ASP A 1 123 ? 4.853   22.884 5.409   1.00 35.64  ? 122 ASP A OD1 1 
ATOM   990  O  OD2 . ASP A 1 123 ? 3.332   23.020 7.013   1.00 36.67  ? 122 ASP A OD2 1 
ATOM   991  N  N   . TYR A 1 124 ? 3.120   18.525 3.731   1.00 24.86  ? 123 TYR A N   1 
ATOM   992  C  CA  . TYR A 1 124 ? 2.385   17.262 3.561   1.00 27.93  ? 123 TYR A CA  1 
ATOM   993  C  C   . TYR A 1 124 ? 2.447   16.491 4.883   1.00 27.18  ? 123 TYR A C   1 
ATOM   994  O  O   . TYR A 1 124 ? 1.431   16.344 5.561   1.00 25.84  ? 123 TYR A O   1 
ATOM   995  C  CB  . TYR A 1 124 ? 2.899   16.501 2.333   1.00 26.00  ? 123 TYR A CB  1 
ATOM   996  C  CG  . TYR A 1 124 ? 2.080   15.267 2.059   1.00 24.08  ? 123 TYR A CG  1 
ATOM   997  C  CD1 . TYR A 1 124 ? 0.779   15.362 1.613   1.00 23.18  ? 123 TYR A CD1 1 
ATOM   998  C  CD2 . TYR A 1 124 ? 2.546   14.017 2.425   1.00 23.66  ? 123 TYR A CD2 1 
ATOM   999  C  CE1 . TYR A 1 124 ? -0.001  14.234 1.409   1.00 30.96  ? 123 TYR A CE1 1 
ATOM   1000 C  CE2 . TYR A 1 124 ? 1.798   12.878 2.203   1.00 27.29  ? 123 TYR A CE2 1 
ATOM   1001 C  CZ  . TYR A 1 124 ? 0.512   12.986 1.704   1.00 28.84  ? 123 TYR A CZ  1 
ATOM   1002 O  OH  . TYR A 1 124 ? -0.243  11.880 1.525   1.00 27.34  ? 123 TYR A OH  1 
ATOM   1003 N  N   . ILE A 1 125 ? 3.615   15.950 5.207   1.00 26.24  ? 124 ILE A N   1 
ATOM   1004 C  CA  . ILE A 1 125 ? 3.810   15.158 6.451   1.00 21.95  ? 124 ILE A CA  1 
ATOM   1005 C  C   . ILE A 1 125 ? 5.246   15.396 6.932   1.00 25.63  ? 124 ILE A C   1 
ATOM   1006 O  O   . ILE A 1 125 ? 6.132   15.606 6.112   1.00 23.86  ? 124 ILE A O   1 
ATOM   1007 C  CB  . ILE A 1 125 ? 3.445   13.672 6.226   1.00 21.88  ? 124 ILE A CB  1 
ATOM   1008 C  CG1 . ILE A 1 125 ? 3.188   12.964 7.565   1.00 23.88  ? 124 ILE A CG1 1 
ATOM   1009 C  CG2 . ILE A 1 125 ? 4.495   12.942 5.416   1.00 24.99  ? 124 ILE A CG2 1 
ATOM   1010 C  CD1 . ILE A 1 125 ? 2.723   11.528 7.482   1.00 27.46  ? 124 ILE A CD1 1 
ATOM   1011 N  N   . ALA A 1 126 ? 5.451   15.419 8.244   1.00 23.64  ? 125 ALA A N   1 
ATOM   1012 C  CA  . ALA A 1 126 ? 6.778   15.640 8.849   1.00 28.27  ? 125 ALA A CA  1 
ATOM   1013 C  C   . ALA A 1 126 ? 6.936   14.701 10.040  1.00 28.74  ? 125 ALA A C   1 
ATOM   1014 O  O   . ALA A 1 126 ? 5.993   14.583 10.879  1.00 24.50  ? 125 ALA A O   1 
ATOM   1015 C  CB  . ALA A 1 126 ? 6.955   17.072 9.274   1.00 25.62  ? 125 ALA A CB  1 
ATOM   1016 N  N   . LEU A 1 127 ? 8.105   14.106 10.140  1.00 22.71  ? 126 LEU A N   1 
ATOM   1017 C  CA  . LEU A 1 127 ? 8.505   13.370 11.368  1.00 26.93  ? 126 LEU A CA  1 
ATOM   1018 C  C   . LEU A 1 127 ? 8.670   14.373 12.517  1.00 26.74  ? 126 LEU A C   1 
ATOM   1019 O  O   . LEU A 1 127 ? 9.412   15.373 12.387  1.00 27.86  ? 126 LEU A O   1 
ATOM   1020 C  CB  . LEU A 1 127 ? 9.788   12.584 11.095  1.00 25.02  ? 126 LEU A CB  1 
ATOM   1021 C  CG  . LEU A 1 127 ? 10.211  11.635 12.221  1.00 24.16  ? 126 LEU A CG  1 
ATOM   1022 C  CD1 . LEU A 1 127 ? 9.144   10.572 12.497  1.00 23.43  ? 126 LEU A CD1 1 
ATOM   1023 C  CD2 . LEU A 1 127 ? 11.543  10.994 11.872  1.00 27.14  ? 126 LEU A CD2 1 
ATOM   1024 N  N   . ASN A 1 128 ? 7.958   14.135 13.620  1.00 30.22  ? 127 ASN A N   1 
ATOM   1025 C  CA  . ASN A 1 128 ? 8.007   15.012 14.811  1.00 28.57  ? 127 ASN A CA  1 
ATOM   1026 C  C   . ASN A 1 128 ? 9.380   14.887 15.471  1.00 31.47  ? 127 ASN A C   1 
ATOM   1027 O  O   . ASN A 1 128 ? 10.114  13.909 15.202  1.00 30.32  ? 127 ASN A O   1 
ATOM   1028 C  CB  . ASN A 1 128 ? 6.901   14.657 15.799  1.00 36.25  ? 127 ASN A CB  1 
ATOM   1029 C  CG  . ASN A 1 128 ? 5.518   14.936 15.254  1.00 31.01  ? 127 ASN A CG  1 
ATOM   1030 O  OD1 . ASN A 1 128 ? 4.571   14.237 15.598  1.00 35.76  ? 127 ASN A OD1 1 
ATOM   1031 N  ND2 . ASN A 1 128 ? 5.406   15.915 14.372  1.00 27.67  ? 127 ASN A ND2 1 
ATOM   1032 N  N   . GLU A 1 129 ? 9.709   15.868 16.301  1.00 30.85  ? 128 GLU A N   1 
ATOM   1033 C  CA  . GLU A 1 129 ? 11.003  15.963 17.024  1.00 33.44  ? 128 GLU A CA  1 
ATOM   1034 C  C   . GLU A 1 129 ? 11.267  14.708 17.880  1.00 26.91  ? 128 GLU A C   1 
ATOM   1035 O  O   . GLU A 1 129 ? 12.438  14.379 18.055  1.00 33.66  ? 128 GLU A O   1 
ATOM   1036 C  CB  . GLU A 1 129 ? 10.975  17.229 17.873  1.00 39.46  ? 128 GLU A CB  1 
ATOM   1037 C  CG  . GLU A 1 129 ? 12.305  17.581 18.481  1.00 57.64  ? 128 GLU A CG  1 
ATOM   1038 C  CD  . GLU A 1 129 ? 12.336  19.009 18.999  1.00 87.46  ? 128 GLU A CD  1 
ATOM   1039 O  OE1 . GLU A 1 129 ? 11.244  19.650 19.034  1.00 65.66  ? 128 GLU A OE1 1 
ATOM   1040 O  OE2 . GLU A 1 129 ? 13.443  19.478 19.355  1.00 78.74  ? 128 GLU A OE2 1 
ATOM   1041 N  N   . ASP A 1 130 ? 10.236  14.002 18.339  1.00 36.78  ? 129 ASP A N   1 
ATOM   1042 C  CA  . ASP A 1 130 ? 10.438  12.759 19.130  1.00 43.03  ? 129 ASP A CA  1 
ATOM   1043 C  C   . ASP A 1 130 ? 10.916  11.624 18.213  1.00 40.90  ? 129 ASP A C   1 
ATOM   1044 O  O   . ASP A 1 130 ? 11.298  10.591 18.743  1.00 35.01  ? 129 ASP A O   1 
ATOM   1045 C  CB  . ASP A 1 130 ? 9.198   12.388 19.953  1.00 39.04  ? 129 ASP A CB  1 
ATOM   1046 C  CG  . ASP A 1 130 ? 7.947   11.993 19.180  1.00 46.89  ? 129 ASP A CG  1 
ATOM   1047 O  OD1 . ASP A 1 130 ? 8.026   11.787 17.952  1.00 42.02  ? 129 ASP A OD1 1 
ATOM   1048 O  OD2 . ASP A 1 130 ? 6.898   11.875 19.821  1.00 54.83  ? 129 ASP A OD2 1 
ATOM   1049 N  N   . LEU A 1 131 ? 10.877  11.774 16.888  1.00 32.88  ? 130 LEU A N   1 
ATOM   1050 C  CA  . LEU A 1 131 ? 11.242  10.706 15.920  1.00 30.28  ? 130 LEU A CA  1 
ATOM   1051 C  C   . LEU A 1 131 ? 10.390  9.446  16.129  1.00 27.71  ? 130 LEU A C   1 
ATOM   1052 O  O   . LEU A 1 131 ? 10.830  8.353  15.695  1.00 33.05  ? 130 LEU A O   1 
ATOM   1053 C  CB  . LEU A 1 131 ? 12.745  10.385 16.035  1.00 32.00  ? 130 LEU A CB  1 
ATOM   1054 C  CG  . LEU A 1 131 ? 13.684  11.584 16.045  1.00 33.13  ? 130 LEU A CG  1 
ATOM   1055 C  CD1 . LEU A 1 131 ? 15.141  11.143 16.130  1.00 36.86  ? 130 LEU A CD1 1 
ATOM   1056 C  CD2 . LEU A 1 131 ? 13.480  12.491 14.835  1.00 33.95  ? 130 LEU A CD2 1 
ATOM   1057 N  N   . ARG A 1 132 ? 9.193   9.577  16.700  1.00 30.80  ? 131 ARG A N   1 
ATOM   1058 C  CA  . ARG A 1 132 ? 8.270   8.441  16.991  1.00 36.99  ? 131 ARG A CA  1 
ATOM   1059 C  C   . ARG A 1 132 ? 6.902   8.650  16.340  1.00 36.31  ? 131 ARG A C   1 
ATOM   1060 O  O   . ARG A 1 132 ? 6.152   7.690  16.253  1.00 40.92  ? 131 ARG A O   1 
ATOM   1061 C  CB  . ARG A 1 132 ? 8.041   8.306  18.501  1.00 51.45  ? 131 ARG A CB  1 
ATOM   1062 C  CG  . ARG A 1 132 ? 9.250   7.832  19.297  1.00 65.03  ? 131 ARG A CG  1 
ATOM   1063 C  CD  . ARG A 1 132 ? 8.887   7.620  20.758  1.00 68.39  ? 131 ARG A CD  1 
ATOM   1064 N  NE  . ARG A 1 132 ? 10.057  7.316  21.575  1.00 101.21 ? 131 ARG A NE  1 
ATOM   1065 C  CZ  . ARG A 1 132 ? 10.856  8.215  22.158  1.00 115.24 ? 131 ARG A CZ  1 
ATOM   1066 N  NH1 . ARG A 1 132 ? 10.629  9.514  22.028  1.00 100.55 ? 131 ARG A NH1 1 
ATOM   1067 N  NH2 . ARG A 1 132 ? 11.890  7.802  22.876  1.00 93.46  ? 131 ARG A NH2 1 
ATOM   1068 N  N   . SER A 1 133 ? 6.592   9.872  15.906  1.00 33.94  ? 132 SER A N   1 
ATOM   1069 C  CA  . SER A 1 133 ? 5.225   10.304 15.545  1.00 29.64  ? 132 SER A CA  1 
ATOM   1070 C  C   . SER A 1 133 ? 5.299   11.285 14.362  1.00 27.80  ? 132 SER A C   1 
ATOM   1071 O  O   . SER A 1 133 ? 6.385   11.863 14.121  1.00 28.89  ? 132 SER A O   1 
ATOM   1072 C  CB  . SER A 1 133 ? 4.583   10.911 16.771  1.00 31.06  ? 132 SER A CB  1 
ATOM   1073 O  OG  . SER A 1 133 ? 5.303   12.051 17.238  1.00 33.87  ? 132 SER A OG  1 
ATOM   1074 N  N   . TRP A 1 134 ? 4.175   11.478 13.693  1.00 25.71  ? 133 TRP A N   1 
ATOM   1075 C  CA  . TRP A 1 134 ? 4.067   12.222 12.412  1.00 28.08  ? 133 TRP A CA  1 
ATOM   1076 C  C   . TRP A 1 134 ? 3.096   13.382 12.603  1.00 34.84  ? 133 TRP A C   1 
ATOM   1077 O  O   . TRP A 1 134 ? 2.060   13.180 13.274  1.00 31.93  ? 133 TRP A O   1 
ATOM   1078 C  CB  . TRP A 1 134 ? 3.541   11.307 11.317  1.00 33.47  ? 133 TRP A CB  1 
ATOM   1079 C  CG  . TRP A 1 134 ? 4.410   10.122 11.051  1.00 34.04  ? 133 TRP A CG  1 
ATOM   1080 C  CD1 . TRP A 1 134 ? 4.276   8.834  11.503  1.00 38.14  ? 133 TRP A CD1 1 
ATOM   1081 C  CD2 . TRP A 1 134 ? 5.576   10.153 10.227  1.00 27.73  ? 133 TRP A CD2 1 
ATOM   1082 N  NE1 . TRP A 1 134 ? 5.297   8.060  11.006  1.00 30.15  ? 133 TRP A NE1 1 
ATOM   1083 C  CE2 . TRP A 1 134 ? 6.111   8.846  10.228  1.00 29.28  ? 133 TRP A CE2 1 
ATOM   1084 C  CE3 . TRP A 1 134 ? 6.215   11.167 9.507   1.00 26.93  ? 133 TRP A CE3 1 
ATOM   1085 C  CZ2 . TRP A 1 134 ? 7.240   8.527  9.485   1.00 29.79  ? 133 TRP A CZ2 1 
ATOM   1086 C  CZ3 . TRP A 1 134 ? 7.358   10.855 8.812   1.00 34.46  ? 133 TRP A CZ3 1 
ATOM   1087 C  CH2 . TRP A 1 134 ? 7.876   9.555  8.830   1.00 33.04  ? 133 TRP A CH2 1 
ATOM   1088 N  N   . THR A 1 135 ? 3.363   14.507 11.953  1.00 29.78  ? 134 THR A N   1 
ATOM   1089 C  CA  . THR A 1 135 ? 2.366   15.595 11.769  1.00 28.99  ? 134 THR A CA  1 
ATOM   1090 C  C   . THR A 1 135 ? 1.908   15.599 10.308  1.00 25.00  ? 134 THR A C   1 
ATOM   1091 O  O   . THR A 1 135 ? 2.745   15.867 9.422   1.00 28.09  ? 134 THR A O   1 
ATOM   1092 C  CB  . THR A 1 135 ? 2.933   16.942 12.225  1.00 29.63  ? 134 THR A CB  1 
ATOM   1093 O  OG1 . THR A 1 135 ? 3.230   16.859 13.622  1.00 32.00  ? 134 THR A OG1 1 
ATOM   1094 C  CG2 . THR A 1 135 ? 1.956   18.080 12.007  1.00 31.74  ? 134 THR A CG2 1 
ATOM   1095 N  N   . ALA A 1 136 ? 0.653   15.279 10.064  1.00 24.70  ? 135 ALA A N   1 
ATOM   1096 C  CA  . ALA A 1 136 ? 0.035   15.321 8.722   1.00 27.23  ? 135 ALA A CA  1 
ATOM   1097 C  C   . ALA A 1 136 ? -0.631  16.696 8.586   1.00 33.19  ? 135 ALA A C   1 
ATOM   1098 O  O   . ALA A 1 136 ? -1.227  17.155 9.569   1.00 30.18  ? 135 ALA A O   1 
ATOM   1099 C  CB  . ALA A 1 136 ? -0.914  14.170 8.544   1.00 28.45  ? 135 ALA A CB  1 
ATOM   1100 N  N   . ALA A 1 137 ? -0.444  17.354 7.443   1.00 32.30  ? 136 ALA A N   1 
ATOM   1101 C  CA  . ALA A 1 137 ? -0.887  18.744 7.166   1.00 33.60  ? 136 ALA A CA  1 
ATOM   1102 C  C   . ALA A 1 137 ? -2.394  18.792 6.880   1.00 31.35  ? 136 ALA A C   1 
ATOM   1103 O  O   . ALA A 1 137 ? -3.023  19.864 7.117   1.00 34.58  ? 136 ALA A O   1 
ATOM   1104 C  CB  . ALA A 1 137 ? -0.096  19.283 6.005   1.00 38.55  ? 136 ALA A CB  1 
ATOM   1105 N  N   . ASP A 1 138 ? -2.954  17.692 6.383   1.00 29.95  ? 137 ASP A N   1 
ATOM   1106 C  CA  . ASP A 1 138 ? -4.338  17.640 5.859   1.00 32.34  ? 137 ASP A CA  1 
ATOM   1107 C  C   . ASP A 1 138 ? -4.827  16.198 5.855   1.00 37.46  ? 137 ASP A C   1 
ATOM   1108 O  O   . ASP A 1 138 ? -4.091  15.317 6.320   1.00 34.41  ? 137 ASP A O   1 
ATOM   1109 C  CB  . ASP A 1 138 ? -4.405  18.265 4.462   1.00 38.23  ? 137 ASP A CB  1 
ATOM   1110 C  CG  . ASP A 1 138 ? -3.591  17.545 3.402   1.00 42.38  ? 137 ASP A CG  1 
ATOM   1111 O  OD1 . ASP A 1 138 ? -3.199  16.388 3.630   1.00 35.57  ? 137 ASP A OD1 1 
ATOM   1112 O  OD2 . ASP A 1 138 ? -3.372  18.144 2.347   1.00 35.68  ? 137 ASP A OD2 1 
ATOM   1113 N  N   . THR A 1 139 ? -6.022  15.952 5.317   1.00 37.27  ? 138 THR A N   1 
ATOM   1114 C  CA  . THR A 1 139 ? -6.708  14.652 5.504   1.00 38.49  ? 138 THR A CA  1 
ATOM   1115 C  C   . THR A 1 139 ? -6.019  13.653 4.578   1.00 38.02  ? 138 THR A C   1 
ATOM   1116 O  O   . THR A 1 139 ? -5.930  12.499 4.943   1.00 39.20  ? 138 THR A O   1 
ATOM   1117 C  CB  . THR A 1 139 ? -8.233  14.761 5.325   1.00 39.27  ? 138 THR A CB  1 
ATOM   1118 O  OG1 . THR A 1 139 ? -8.498  15.022 3.956   1.00 52.30  ? 138 THR A OG1 1 
ATOM   1119 C  CG2 . THR A 1 139 ? -8.849  15.843 6.169   1.00 40.22  ? 138 THR A CG2 1 
ATOM   1120 N  N   . ALA A 1 140 ? -5.544  14.102 3.419   1.00 32.92  ? 139 ALA A N   1 
ATOM   1121 C  CA  . ALA A 1 140 ? -4.814  13.260 2.455   1.00 32.98  ? 139 ALA A CA  1 
ATOM   1122 C  C   . ALA A 1 140 ? -3.573  12.703 3.150   1.00 30.05  ? 139 ALA A C   1 
ATOM   1123 O  O   . ALA A 1 140 ? -3.320  11.527 3.030   1.00 38.32  ? 139 ALA A O   1 
ATOM   1124 C  CB  . ALA A 1 140 ? -4.453  14.050 1.229   1.00 33.66  ? 139 ALA A CB  1 
ATOM   1125 N  N   . ALA A 1 141 ? -2.838  13.544 3.856   1.00 30.28  ? 140 ALA A N   1 
ATOM   1126 C  CA  . ALA A 1 141 ? -1.550  13.173 4.466   1.00 29.19  ? 140 ALA A CA  1 
ATOM   1127 C  C   . ALA A 1 141 ? -1.787  12.210 5.633   1.00 37.80  ? 140 ALA A C   1 
ATOM   1128 O  O   . ALA A 1 141 ? -0.858  11.498 6.014   1.00 28.58  ? 140 ALA A O   1 
ATOM   1129 C  CB  . ALA A 1 141 ? -0.857  14.428 4.910   1.00 28.59  ? 140 ALA A CB  1 
ATOM   1130 N  N   . GLN A 1 142 ? -2.976  12.262 6.233   1.00 28.65  ? 141 GLN A N   1 
ATOM   1131 C  CA  . GLN A 1 142 ? -3.434  11.285 7.249   1.00 36.13  ? 141 GLN A CA  1 
ATOM   1132 C  C   . GLN A 1 142 ? -3.483  9.883  6.633   1.00 30.28  ? 141 GLN A C   1 
ATOM   1133 O  O   . GLN A 1 142 ? -3.255  8.952  7.388   1.00 33.75  ? 141 GLN A O   1 
ATOM   1134 C  CB  . GLN A 1 142 ? -4.771  11.729 7.866   1.00 37.67  ? 141 GLN A CB  1 
ATOM   1135 C  CG  . GLN A 1 142 ? -4.617  12.940 8.785   1.00 35.68  ? 141 GLN A CG  1 
ATOM   1136 C  CD  . GLN A 1 142 ? -5.946  13.414 9.328   1.00 50.19  ? 141 GLN A CD  1 
ATOM   1137 O  OE1 . GLN A 1 142 ? -6.959  12.748 9.173   1.00 43.08  ? 141 GLN A OE1 1 
ATOM   1138 N  NE2 . GLN A 1 142 ? -5.961  14.576 9.959   1.00 44.49  ? 141 GLN A NE2 1 
ATOM   1139 N  N   . ILE A 1 143 ? -3.710  9.727  5.324   1.00 28.23  ? 142 ILE A N   1 
ATOM   1140 C  CA  . ILE A 1 143 ? -3.630  8.386  4.690   1.00 30.14  ? 142 ILE A CA  1 
ATOM   1141 C  C   . ILE A 1 143 ? -2.179  7.878  4.829   1.00 39.88  ? 142 ILE A C   1 
ATOM   1142 O  O   . ILE A 1 143 ? -1.947  6.721  5.294   1.00 32.81  ? 142 ILE A O   1 
ATOM   1143 C  CB  . ILE A 1 143 ? -4.094  8.427  3.226   1.00 30.87  ? 142 ILE A CB  1 
ATOM   1144 C  CG1 . ILE A 1 143 ? -5.562  8.839  3.067   1.00 35.25  ? 142 ILE A CG1 1 
ATOM   1145 C  CG2 . ILE A 1 143 ? -3.813  7.106  2.534   1.00 35.11  ? 142 ILE A CG2 1 
ATOM   1146 C  CD1 . ILE A 1 143 ? -5.910  9.187  1.634   1.00 36.39  ? 142 ILE A CD1 1 
ATOM   1147 N  N   . THR A 1 144 ? -1.206  8.707  4.447   1.00 30.22  ? 143 THR A N   1 
ATOM   1148 C  CA  . THR A 1 144 ? 0.230   8.364  4.557   1.00 27.77  ? 143 THR A CA  1 
ATOM   1149 C  C   . THR A 1 144 ? 0.576   8.103  6.029   1.00 29.81  ? 143 THR A C   1 
ATOM   1150 O  O   . THR A 1 144 ? 1.322   7.121  6.315   1.00 28.70  ? 143 THR A O   1 
ATOM   1151 C  CB  . THR A 1 144 ? 1.102   9.460  3.939   1.00 25.51  ? 143 THR A CB  1 
ATOM   1152 O  OG1 . THR A 1 144 ? 0.736   9.564  2.562   1.00 26.67  ? 143 THR A OG1 1 
ATOM   1153 C  CG2 . THR A 1 144 ? 2.577   9.152  4.099   1.00 28.32  ? 143 THR A CG2 1 
ATOM   1154 N  N   . GLN A 1 145 ? 0.082   8.951  6.943   1.00 23.95  ? 144 GLN A N   1 
ATOM   1155 C  CA  . GLN A 1 145 ? 0.366   8.830  8.384   1.00 28.67  ? 144 GLN A CA  1 
ATOM   1156 C  C   . GLN A 1 145 ? -0.117  7.447  8.847   1.00 29.82  ? 144 GLN A C   1 
ATOM   1157 O  O   . GLN A 1 145 ? 0.660   6.764  9.488   1.00 28.10  ? 144 GLN A O   1 
ATOM   1158 C  CB  . GLN A 1 145 ? -0.290  9.942  9.202   1.00 30.30  ? 144 GLN A CB  1 
ATOM   1159 C  CG  . GLN A 1 145 ? -0.138  9.755  10.702  1.00 27.16  ? 144 GLN A CG  1 
ATOM   1160 C  CD  . GLN A 1 145 ? -0.588  10.961 11.491  1.00 34.91  ? 144 GLN A CD  1 
ATOM   1161 O  OE1 . GLN A 1 145 ? -1.283  11.832 10.982  1.00 40.70  ? 144 GLN A OE1 1 
ATOM   1162 N  NE2 . GLN A 1 145 ? -0.286  10.969 12.773  1.00 36.65  ? 144 GLN A NE2 1 
ATOM   1163 N  N   . ARG A 1 146 ? -1.344  7.040  8.513   1.00 29.59  ? 145 ARG A N   1 
ATOM   1164 C  CA  . ARG A 1 146 ? -1.895  5.752  9.018   1.00 34.55  ? 145 ARG A CA  1 
ATOM   1165 C  C   . ARG A 1 146 ? -1.029  4.618  8.467   1.00 34.63  ? 145 ARG A C   1 
ATOM   1166 O  O   . ARG A 1 146 ? -0.716  3.695  9.235   1.00 32.89  ? 145 ARG A O   1 
ATOM   1167 C  CB  . ARG A 1 146 ? -3.379  5.583  8.666   1.00 38.05  ? 145 ARG A CB  1 
ATOM   1168 C  CG  . ARG A 1 146 ? -4.298  6.502  9.467   1.00 41.12  ? 145 ARG A CG  1 
ATOM   1169 C  CD  . ARG A 1 146 ? -5.762  6.130  9.280   1.00 41.40  ? 145 ARG A CD  1 
ATOM   1170 N  NE  . ARG A 1 146 ? -6.215  6.431  7.930   1.00 49.08  ? 145 ARG A NE  1 
ATOM   1171 C  CZ  . ARG A 1 146 ? -6.583  7.645  7.514   1.00 38.78  ? 145 ARG A CZ  1 
ATOM   1172 N  NH1 . ARG A 1 146 ? -6.578  8.676  8.345   1.00 43.92  ? 145 ARG A NH1 1 
ATOM   1173 N  NH2 . ARG A 1 146 ? -6.992  7.811  6.277   1.00 42.08  ? 145 ARG A NH2 1 
ATOM   1174 N  N   . LYS A 1 147 ? -0.662  4.682  7.188   1.00 27.11  ? 146 LYS A N   1 
ATOM   1175 C  CA  . LYS A 1 147 ? 0.134   3.622  6.533   1.00 32.07  ? 146 LYS A CA  1 
ATOM   1176 C  C   . LYS A 1 147 ? 1.498   3.505  7.226   1.00 32.09  ? 146 LYS A C   1 
ATOM   1177 O  O   . LYS A 1 147 ? 1.932   2.348  7.545   1.00 30.09  ? 146 LYS A O   1 
ATOM   1178 C  CB  . LYS A 1 147 ? 0.271   3.892  5.038   1.00 38.24  ? 146 LYS A CB  1 
ATOM   1179 C  CG  . LYS A 1 147 ? 1.182   2.922  4.296   1.00 49.14  ? 146 LYS A CG  1 
ATOM   1180 C  CD  . LYS A 1 147 ? 0.959   2.916  2.796   1.00 53.76  ? 146 LYS A CD  1 
ATOM   1181 C  CE  . LYS A 1 147 ? 1.312   4.226  2.126   1.00 70.14  ? 146 LYS A CE  1 
ATOM   1182 N  NZ  . LYS A 1 147 ? 2.512   4.088  1.270   1.00 69.50  ? 146 LYS A NZ  1 
ATOM   1183 N  N   . TRP A 1 148 ? 2.158   4.637  7.468   1.00 26.89  ? 147 TRP A N   1 
ATOM   1184 C  CA  . TRP A 1 148 ? 3.537   4.659  8.010   1.00 25.99  ? 147 TRP A CA  1 
ATOM   1185 C  C   . TRP A 1 148 ? 3.527   4.265  9.486   1.00 29.75  ? 147 TRP A C   1 
ATOM   1186 O  O   . TRP A 1 148 ? 4.461   3.599  9.933   1.00 30.06  ? 147 TRP A O   1 
ATOM   1187 C  CB  . TRP A 1 148 ? 4.205   6.020  7.798   1.00 28.32  ? 147 TRP A CB  1 
ATOM   1188 C  CG  . TRP A 1 148 ? 4.604   6.284  6.381   1.00 26.40  ? 147 TRP A CG  1 
ATOM   1189 C  CD1 . TRP A 1 148 ? 4.518   5.444  5.317   1.00 28.28  ? 147 TRP A CD1 1 
ATOM   1190 C  CD2 . TRP A 1 148 ? 5.172   7.510  5.878   1.00 25.95  ? 147 TRP A CD2 1 
ATOM   1191 N  NE1 . TRP A 1 148 ? 4.963   6.075  4.187   1.00 26.99  ? 147 TRP A NE1 1 
ATOM   1192 C  CE2 . TRP A 1 148 ? 5.376   7.335  4.505   1.00 21.92  ? 147 TRP A CE2 1 
ATOM   1193 C  CE3 . TRP A 1 148 ? 5.528   8.723  6.465   1.00 26.84  ? 147 TRP A CE3 1 
ATOM   1194 C  CZ2 . TRP A 1 148 ? 5.956   8.328  3.712   1.00 25.38  ? 147 TRP A CZ2 1 
ATOM   1195 C  CZ3 . TRP A 1 148 ? 6.079   9.717  5.684   1.00 24.63  ? 147 TRP A CZ3 1 
ATOM   1196 C  CH2 . TRP A 1 148 ? 6.281   9.515  4.324   1.00 23.20  ? 147 TRP A CH2 1 
ATOM   1197 N  N   . GLU A 1 149 ? 2.452   4.591  10.188  1.00 29.50  ? 148 GLU A N   1 
ATOM   1198 C  CA  . GLU A 1 149 ? 2.270   4.182  11.601  1.00 29.71  ? 148 GLU A CA  1 
ATOM   1199 C  C   . GLU A 1 149 ? 2.089   2.661  11.660  1.00 31.77  ? 148 GLU A C   1 
ATOM   1200 O  O   . GLU A 1 149 ? 2.782   2.036  12.416  1.00 34.02  ? 148 GLU A O   1 
ATOM   1201 C  CB  . GLU A 1 149 ? 1.041   4.869  12.184  1.00 32.96  ? 148 GLU A CB  1 
ATOM   1202 C  CG  . GLU A 1 149 ? 1.290   6.304  12.569  1.00 39.27  ? 148 GLU A CG  1 
ATOM   1203 C  CD  . GLU A 1 149 ? 0.040   7.048  12.986  1.00 48.65  ? 148 GLU A CD  1 
ATOM   1204 O  OE1 . GLU A 1 149 ? -1.047  6.551  12.743  1.00 49.62  ? 148 GLU A OE1 1 
ATOM   1205 O  OE2 . GLU A 1 149 ? 0.162   8.112  13.529  1.00 50.03  ? 148 GLU A OE2 1 
ATOM   1206 N  N   . ALA A 1 150 ? 1.174   2.118  10.868  1.00 31.47  ? 149 ALA A N   1 
ATOM   1207 C  CA  . ALA A 1 150 ? 0.917   0.662  10.823  1.00 35.22  ? 149 ALA A CA  1 
ATOM   1208 C  C   . ALA A 1 150 ? 2.222   -0.098 10.518  1.00 44.54  ? 149 ALA A C   1 
ATOM   1209 O  O   . ALA A 1 150 ? 2.454   -1.168 11.139  1.00 40.50  ? 149 ALA A O   1 
ATOM   1210 C  CB  . ALA A 1 150 ? -0.140  0.344  9.810   1.00 38.82  ? 149 ALA A CB  1 
ATOM   1211 N  N   . ALA A 1 151 ? 3.080   0.442  9.646   1.00 34.87  ? 150 ALA A N   1 
ATOM   1212 C  CA  . ALA A 1 151 ? 4.309   -0.239 9.174   1.00 29.00  ? 150 ALA A CA  1 
ATOM   1213 C  C   . ALA A 1 151 ? 5.505   0.104  10.061  1.00 25.08  ? 150 ALA A C   1 
ATOM   1214 O  O   . ALA A 1 151 ? 6.596   -0.433 9.818   1.00 27.61  ? 150 ALA A O   1 
ATOM   1215 C  CB  . ALA A 1 151 ? 4.571   0.079  7.730   1.00 37.31  ? 150 ALA A CB  1 
ATOM   1216 N  N   . ARG A 1 152 ? 5.310   0.915  11.095  1.00 27.08  ? 151 ARG A N   1 
ATOM   1217 C  CA  . ARG A 1 152 ? 6.351   1.218  12.099  1.00 32.33  ? 151 ARG A CA  1 
ATOM   1218 C  C   . ARG A 1 152 ? 7.578   1.838  11.419  1.00 37.96  ? 151 ARG A C   1 
ATOM   1219 O  O   . ARG A 1 152 ? 8.707   1.671  11.917  1.00 25.90  ? 151 ARG A O   1 
ATOM   1220 C  CB  . ARG A 1 152 ? 6.682   -0.071 12.861  1.00 30.78  ? 151 ARG A CB  1 
ATOM   1221 C  CG  . ARG A 1 152 ? 5.528   -0.547 13.740  1.00 36.22  ? 151 ARG A CG  1 
ATOM   1222 C  CD  . ARG A 1 152 ? 5.802   -1.890 14.435  1.00 38.09  ? 151 ARG A CD  1 
ATOM   1223 N  NE  . ARG A 1 152 ? 7.091   -1.913 15.117  1.00 33.07  ? 151 ARG A NE  1 
ATOM   1224 C  CZ  . ARG A 1 152 ? 7.799   -3.019 15.369  1.00 44.96  ? 151 ARG A CZ  1 
ATOM   1225 N  NH1 . ARG A 1 152 ? 8.973   -2.946 15.972  1.00 37.23  ? 151 ARG A NH1 1 
ATOM   1226 N  NH2 . ARG A 1 152 ? 7.328   -4.202 15.028  1.00 38.18  ? 151 ARG A NH2 1 
ATOM   1227 N  N   . GLU A 1 153 ? 7.382   2.605  10.350  1.00 31.35  ? 152 GLU A N   1 
ATOM   1228 C  CA  . GLU A 1 153 ? 8.527   3.128  9.555   1.00 33.17  ? 152 GLU A CA  1 
ATOM   1229 C  C   . GLU A 1 153 ? 9.292   4.211  10.338  1.00 31.16  ? 152 GLU A C   1 
ATOM   1230 O  O   . GLU A 1 153 ? 10.493  4.338  10.116  1.00 30.04  ? 152 GLU A O   1 
ATOM   1231 C  CB  . GLU A 1 153 ? 8.016   3.490  8.154   1.00 32.54  ? 152 GLU A CB  1 
ATOM   1232 C  CG  . GLU A 1 153 ? 7.660   2.219  7.368   1.00 40.12  ? 152 GLU A CG  1 
ATOM   1233 C  CD  . GLU A 1 153 ? 7.208   2.338  5.914   1.00 50.21  ? 152 GLU A CD  1 
ATOM   1234 O  OE1 . GLU A 1 153 ? 7.197   3.501  5.388   1.00 35.34  ? 152 GLU A OE1 1 
ATOM   1235 O  OE2 . GLU A 1 153 ? 6.840   1.251  5.309   1.00 36.27  ? 152 GLU A OE2 1 
ATOM   1236 N  N   . ALA A 1 154 ? 8.662   4.955  11.250  1.00 31.15  ? 153 ALA A N   1 
ATOM   1237 C  CA  . ALA A 1 154 ? 9.351   5.949  12.106  1.00 30.39  ? 153 ALA A CA  1 
ATOM   1238 C  C   . ALA A 1 154 ? 10.552  5.291  12.813  1.00 32.90  ? 153 ALA A C   1 
ATOM   1239 O  O   . ALA A 1 154 ? 11.580  5.961  12.970  1.00 30.85  ? 153 ALA A O   1 
ATOM   1240 C  CB  . ALA A 1 154 ? 8.383   6.551  13.093  1.00 29.56  ? 153 ALA A CB  1 
ATOM   1241 N  N   . GLU A 1 155 ? 10.439  4.030  13.244  1.00 34.46  ? 154 GLU A N   1 
ATOM   1242 C  CA  . GLU A 1 155 ? 11.528  3.341  13.999  1.00 31.68  ? 154 GLU A CA  1 
ATOM   1243 C  C   . GLU A 1 155 ? 12.755  3.196  13.100  1.00 31.21  ? 154 GLU A C   1 
ATOM   1244 O  O   . GLU A 1 155 ? 13.886  3.413  13.588  1.00 35.98  ? 154 GLU A O   1 
ATOM   1245 C  CB  . GLU A 1 155 ? 11.120  1.954  14.492  1.00 29.57  ? 154 GLU A CB  1 
ATOM   1246 C  CG  . GLU A 1 155 ? 10.046  1.987  15.551  1.00 48.00  ? 154 GLU A CG  1 
ATOM   1247 C  CD  . GLU A 1 155 ? 9.468   0.611  15.816  1.00 54.12  ? 154 GLU A CD  1 
ATOM   1248 O  OE1 . GLU A 1 155 ? 10.256  -0.385 15.726  1.00 41.33  ? 154 GLU A OE1 1 
ATOM   1249 O  OE2 . GLU A 1 155 ? 8.236   0.539  16.051  1.00 32.34  ? 154 GLU A OE2 1 
ATOM   1250 N  N   . GLN A 1 156 ? 12.550  2.819  11.839  1.00 30.38  ? 155 GLN A N   1 
ATOM   1251 C  CA  . GLN A 1 156 ? 13.653  2.701  10.847  1.00 35.58  ? 155 GLN A CA  1 
ATOM   1252 C  C   . GLN A 1 156 ? 14.226  4.097  10.531  1.00 33.83  ? 155 GLN A C   1 
ATOM   1253 O  O   . GLN A 1 156 ? 15.455  4.237  10.468  1.00 31.77  ? 155 GLN A O   1 
ATOM   1254 C  CB  . GLN A 1 156 ? 13.195  1.962  9.589   1.00 38.43  ? 155 GLN A CB  1 
ATOM   1255 C  CG  . GLN A 1 156 ? 14.379  1.462  8.752   1.00 52.60  ? 155 GLN A CG  1 
ATOM   1256 C  CD  . GLN A 1 156 ? 13.971  0.910  7.406   1.00 56.35  ? 155 GLN A CD  1 
ATOM   1257 O  OE1 . GLN A 1 156 ? 13.428  1.628  6.574   1.00 37.80  ? 155 GLN A OE1 1 
ATOM   1258 N  NE2 . GLN A 1 156 ? 14.226  -0.374 7.183   1.00 56.29  ? 155 GLN A NE2 1 
ATOM   1259 N  N   . ARG A 1 157 ? 13.388  5.113  10.359  1.00 33.95  ? 156 ARG A N   1 
ATOM   1260 C  CA  . ARG A 1 157 ? 13.882  6.475  10.037  1.00 33.83  ? 156 ARG A CA  1 
ATOM   1261 C  C   . ARG A 1 157 ? 14.682  6.994  11.245  1.00 28.23  ? 156 ARG A C   1 
ATOM   1262 O  O   . ARG A 1 157 ? 15.815  7.512  11.057  1.00 30.11  ? 156 ARG A O   1 
ATOM   1263 C  CB  . ARG A 1 157 ? 12.710  7.374  9.645   1.00 31.69  ? 156 ARG A CB  1 
ATOM   1264 C  CG  . ARG A 1 157 ? 12.066  6.933  8.335   1.00 31.58  ? 156 ARG A CG  1 
ATOM   1265 C  CD  . ARG A 1 157 ? 10.702  7.551  8.286   1.00 32.81  ? 156 ARG A CD  1 
ATOM   1266 N  NE  . ARG A 1 157 ? 9.903   7.344  7.080   1.00 27.28  ? 156 ARG A NE  1 
ATOM   1267 C  CZ  . ARG A 1 157 ? 9.869   8.163  6.037   1.00 33.00  ? 156 ARG A CZ  1 
ATOM   1268 N  NH1 . ARG A 1 157 ? 10.727  9.164  5.922   1.00 33.00  ? 156 ARG A NH1 1 
ATOM   1269 N  NH2 . ARG A 1 157 ? 9.023   7.912  5.070   1.00 32.89  ? 156 ARG A NH2 1 
ATOM   1270 N  N   . ARG A 1 158 ? 14.178  6.741  12.445  1.00 30.10  ? 157 ARG A N   1 
ATOM   1271 C  CA  . ARG A 1 158 ? 14.845  7.176  13.695  1.00 29.40  ? 157 ARG A CA  1 
ATOM   1272 C  C   . ARG A 1 158 ? 16.200  6.466  13.780  1.00 30.53  ? 157 ARG A C   1 
ATOM   1273 O  O   . ARG A 1 158 ? 17.201  7.143  14.027  1.00 28.32  ? 157 ARG A O   1 
ATOM   1274 C  CB  . ARG A 1 158 ? 13.976  6.911  14.927  1.00 31.64  ? 157 ARG A CB  1 
ATOM   1275 C  CG  . ARG A 1 158 ? 14.676  7.292  16.217  1.00 39.65  ? 157 ARG A CG  1 
ATOM   1276 C  CD  . ARG A 1 158 ? 13.942  6.776  17.435  1.00 45.16  ? 157 ARG A CD  1 
ATOM   1277 N  NE  . ARG A 1 158 ? 14.644  7.256  18.612  1.00 61.35  ? 157 ARG A NE  1 
ATOM   1278 C  CZ  . ARG A 1 158 ? 14.217  7.101  19.853  1.00 70.61  ? 157 ARG A CZ  1 
ATOM   1279 N  NH1 . ARG A 1 158 ? 13.076  6.471  20.083  1.00 59.78  ? 157 ARG A NH1 1 
ATOM   1280 N  NH2 . ARG A 1 158 ? 14.927  7.593  20.853  1.00 71.57  ? 157 ARG A NH2 1 
ATOM   1281 N  N   . ALA A 1 159 ? 16.249  5.161  13.525  1.00 31.46  ? 158 ALA A N   1 
ATOM   1282 C  CA  . ALA A 1 159 ? 17.521  4.417  13.678  1.00 39.53  ? 158 ALA A CA  1 
ATOM   1283 C  C   . ALA A 1 159 ? 18.544  4.975  12.677  1.00 35.51  ? 158 ALA A C   1 
ATOM   1284 O  O   . ALA A 1 159 ? 19.741  5.133  13.044  1.00 32.67  ? 158 ALA A O   1 
ATOM   1285 C  CB  . ALA A 1 159 ? 17.299  2.918  13.557  1.00 40.26  ? 158 ALA A CB  1 
ATOM   1286 N  N   . TYR A 1 160 ? 18.085  5.324  11.475  1.00 28.16  ? 159 TYR A N   1 
ATOM   1287 C  CA  . TYR A 1 160 ? 18.921  5.869  10.373  1.00 27.20  ? 159 TYR A CA  1 
ATOM   1288 C  C   . TYR A 1 160 ? 19.494  7.240  10.766  1.00 32.40  ? 159 TYR A C   1 
ATOM   1289 O  O   . TYR A 1 160 ? 20.719  7.514  10.628  1.00 30.40  ? 159 TYR A O   1 
ATOM   1290 C  CB  . TYR A 1 160 ? 18.133  6.000  9.053   1.00 31.48  ? 159 TYR A CB  1 
ATOM   1291 C  CG  . TYR A 1 160 ? 18.852  6.942  8.120   1.00 28.92  ? 159 TYR A CG  1 
ATOM   1292 C  CD1 . TYR A 1 160 ? 19.960  6.547  7.391   1.00 28.10  ? 159 TYR A CD1 1 
ATOM   1293 C  CD2 . TYR A 1 160 ? 18.519  8.288  8.092   1.00 37.55  ? 159 TYR A CD2 1 
ATOM   1294 C  CE1 . TYR A 1 160 ? 20.688  7.450  6.630   1.00 28.58  ? 159 TYR A CE1 1 
ATOM   1295 C  CE2 . TYR A 1 160 ? 19.229  9.202  7.326   1.00 27.58  ? 159 TYR A CE2 1 
ATOM   1296 C  CZ  . TYR A 1 160 ? 20.332  8.787  6.603   1.00 31.05  ? 159 TYR A CZ  1 
ATOM   1297 O  OH  . TYR A 1 160 ? 21.031  9.717  5.872   1.00 28.21  ? 159 TYR A OH  1 
ATOM   1298 N  N   . LEU A 1 161 ? 18.638  8.104  11.296  1.00 32.66  ? 160 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 161 ? 19.005  9.491  11.651  1.00 29.17  ? 160 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 161 ? 20.006  9.477  12.802  1.00 35.18  ? 160 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 161 ? 20.899  10.356 12.793  1.00 30.01  ? 160 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 161 ? 17.734  10.271 12.015  1.00 33.30  ? 160 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 161 ? 16.791  10.505 10.840  1.00 27.58  ? 160 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 161 ? 15.480  11.123 11.288  1.00 26.66  ? 160 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 161 ? 17.451  11.370 9.774   1.00 35.76  ? 160 LEU A CD2 1 
ATOM   1306 N  N   . GLU A 1 162 ? 19.852  8.536  13.744  1.00 31.43  ? 161 GLU A N   1 
ATOM   1307 C  CA  . GLU A 1 162 ? 20.700  8.411  14.957  1.00 31.91  ? 161 GLU A CA  1 
ATOM   1308 C  C   . GLU A 1 162 ? 22.034  7.751  14.621  1.00 33.46  ? 161 GLU A C   1 
ATOM   1309 O  O   . GLU A 1 162 ? 23.000  7.928  15.391  1.00 31.71  ? 161 GLU A O   1 
ATOM   1310 C  CB  . GLU A 1 162 ? 20.006  7.563  16.017  1.00 35.90  ? 161 GLU A CB  1 
ATOM   1311 C  CG  . GLU A 1 162 ? 18.893  8.293  16.742  1.00 42.36  ? 161 GLU A CG  1 
ATOM   1312 C  CD  . GLU A 1 162 ? 18.021  7.439  17.661  1.00 49.45  ? 161 GLU A CD  1 
ATOM   1313 O  OE1 . GLU A 1 162 ? 18.123  6.198  17.612  1.00 46.92  ? 161 GLU A OE1 1 
ATOM   1314 O  OE2 . GLU A 1 162 ? 17.217  8.025  18.408  1.00 43.61  ? 161 GLU A OE2 1 
ATOM   1315 N  N   . GLY A 1 163 ? 22.063  6.961  13.548  1.00 33.92  ? 162 GLY A N   1 
ATOM   1316 C  CA  . GLY A 1 163 ? 23.179  6.059  13.244  1.00 29.23  ? 162 GLY A CA  1 
ATOM   1317 C  C   . GLY A 1 163 ? 23.915  6.519  12.014  1.00 32.20  ? 162 GLY A C   1 
ATOM   1318 O  O   . GLY A 1 163 ? 24.774  7.413  12.127  1.00 30.99  ? 162 GLY A O   1 
ATOM   1319 N  N   . GLU A 1 164 ? 23.549  5.964  10.860  1.00 32.05  ? 163 GLU A N   1 
ATOM   1320 C  CA  . GLU A 1 164 ? 24.259  6.242  9.593   1.00 28.50  ? 163 GLU A CA  1 
ATOM   1321 C  C   . GLU A 1 164 ? 24.396  7.753  9.335   1.00 22.27  ? 163 GLU A C   1 
ATOM   1322 O  O   . GLU A 1 164 ? 25.461  8.196  8.883   1.00 29.30  ? 163 GLU A O   1 
ATOM   1323 C  CB  . GLU A 1 164 ? 23.528  5.539  8.457   1.00 31.46  ? 163 GLU A CB  1 
ATOM   1324 C  CG  . GLU A 1 164 ? 24.070  5.958  7.125   1.00 29.00  ? 163 GLU A CG  1 
ATOM   1325 C  CD  . GLU A 1 164 ? 23.463  5.200  5.978   1.00 37.51  ? 163 GLU A CD  1 
ATOM   1326 O  OE1 . GLU A 1 164 ? 22.756  4.190  6.262   1.00 36.56  ? 163 GLU A OE1 1 
ATOM   1327 O  OE2 . GLU A 1 164 ? 23.622  5.680  4.828   1.00 40.80  ? 163 GLU A OE2 1 
ATOM   1328 N  N   . CYS A 1 165 ? 23.336  8.515  9.519   1.00 29.83  ? 164 CYS A N   1 
ATOM   1329 C  CA  . CYS A 1 165 ? 23.317  9.961  9.168   1.00 26.00  ? 164 CYS A CA  1 
ATOM   1330 C  C   . CYS A 1 165 ? 24.459  10.657 9.903   1.00 26.72  ? 164 CYS A C   1 
ATOM   1331 O  O   . CYS A 1 165 ? 25.244  11.388 9.285   1.00 27.61  ? 164 CYS A O   1 
ATOM   1332 C  CB  . CYS A 1 165 ? 21.980  10.583 9.540   1.00 32.09  ? 164 CYS A CB  1 
ATOM   1333 S  SG  . CYS A 1 165 ? 21.816  12.277 8.927   1.00 29.21  ? 164 CYS A SG  1 
ATOM   1334 N  N   . VAL A 1 166 ? 24.560  10.411 11.197  1.00 27.08  ? 165 VAL A N   1 
ATOM   1335 C  CA  . VAL A 1 166 ? 25.575  11.056 12.071  1.00 26.33  ? 165 VAL A CA  1 
ATOM   1336 C  C   . VAL A 1 166 ? 26.986  10.591 11.675  1.00 31.36  ? 165 VAL A C   1 
ATOM   1337 O  O   . VAL A 1 166 ? 27.947  11.395 11.735  1.00 28.07  ? 165 VAL A O   1 
ATOM   1338 C  CB  . VAL A 1 166 ? 25.197  10.749 13.526  1.00 30.00  ? 165 VAL A CB  1 
ATOM   1339 C  CG1 . VAL A 1 166 ? 26.341  11.013 14.471  1.00 44.86  ? 165 VAL A CG1 1 
ATOM   1340 C  CG2 . VAL A 1 166 ? 23.940  11.500 13.924  1.00 37.35  ? 165 VAL A CG2 1 
ATOM   1341 N  N   . GLU A 1 167 ? 27.120  9.343  11.232  1.00 29.68  ? 166 GLU A N   1 
ATOM   1342 C  CA  . GLU A 1 167 ? 28.428  8.762  10.874  1.00 30.18  ? 166 GLU A CA  1 
ATOM   1343 C  C   . GLU A 1 167 ? 28.901  9.442  9.592   1.00 32.96  ? 166 GLU A C   1 
ATOM   1344 O  O   . GLU A 1 167 ? 30.087  9.737  9.486   1.00 31.95  ? 166 GLU A O   1 
ATOM   1345 C  CB  . GLU A 1 167 ? 28.323  7.235  10.758  1.00 39.59  ? 166 GLU A CB  1 
ATOM   1346 C  CG  . GLU A 1 167 ? 28.132  6.558  12.100  1.00 47.96  ? 166 GLU A CG  1 
ATOM   1347 C  CD  . GLU A 1 167 ? 29.032  7.151  13.179  1.00 54.46  ? 166 GLU A CD  1 
ATOM   1348 O  OE1 . GLU A 1 167 ? 30.254  7.206  12.945  1.00 49.31  ? 166 GLU A OE1 1 
ATOM   1349 O  OE2 . GLU A 1 167 ? 28.509  7.614  14.217  1.00 60.37  ? 166 GLU A OE2 1 
ATOM   1350 N  N   . TRP A 1 168 ? 28.025  9.659  8.616   1.00 29.59  ? 167 TRP A N   1 
ATOM   1351 C  CA  . TRP A 1 168 ? 28.444  10.347 7.374   1.00 25.87  ? 167 TRP A CA  1 
ATOM   1352 C  C   . TRP A 1 168 ? 28.849  11.778 7.718   1.00 24.93  ? 167 TRP A C   1 
ATOM   1353 O  O   . TRP A 1 168 ? 29.879  12.227 7.238   1.00 29.63  ? 167 TRP A O   1 
ATOM   1354 C  CB  . TRP A 1 168 ? 27.367  10.301 6.282   1.00 28.42  ? 167 TRP A CB  1 
ATOM   1355 C  CG  . TRP A 1 168 ? 27.362  9.004  5.540   1.00 27.35  ? 167 TRP A CG  1 
ATOM   1356 C  CD1 . TRP A 1 168 ? 26.390  8.056  5.566   1.00 32.18  ? 167 TRP A CD1 1 
ATOM   1357 C  CD2 . TRP A 1 168 ? 28.416  8.481  4.712   1.00 29.63  ? 167 TRP A CD2 1 
ATOM   1358 N  NE1 . TRP A 1 168 ? 26.762  6.983  4.813   1.00 28.25  ? 167 TRP A NE1 1 
ATOM   1359 C  CE2 . TRP A 1 168 ? 27.997  7.216  4.271   1.00 28.88  ? 167 TRP A CE2 1 
ATOM   1360 C  CE3 . TRP A 1 168 ? 29.652  8.964  4.284   1.00 28.19  ? 167 TRP A CE3 1 
ATOM   1361 C  CZ2 . TRP A 1 168 ? 28.773  6.439  3.429   1.00 31.86  ? 167 TRP A CZ2 1 
ATOM   1362 C  CZ3 . TRP A 1 168 ? 30.415  8.196  3.434   1.00 32.82  ? 167 TRP A CZ3 1 
ATOM   1363 C  CH2 . TRP A 1 168 ? 29.982  6.947  3.021   1.00 36.74  ? 167 TRP A CH2 1 
ATOM   1364 N  N   . LEU A 1 169 ? 28.076  12.442 8.567   1.00 26.54  ? 168 LEU A N   1 
ATOM   1365 C  CA  . LEU A 1 169 ? 28.357  13.855 8.936   1.00 26.34  ? 168 LEU A CA  1 
ATOM   1366 C  C   . LEU A 1 169 ? 29.738  13.933 9.605   1.00 35.17  ? 168 LEU A C   1 
ATOM   1367 O  O   . LEU A 1 169 ? 30.533  14.838 9.247   1.00 31.67  ? 168 LEU A O   1 
ATOM   1368 C  CB  . LEU A 1 169 ? 27.244  14.328 9.867   1.00 26.04  ? 168 LEU A CB  1 
ATOM   1369 C  CG  . LEU A 1 169 ? 27.464  15.719 10.446  1.00 26.12  ? 168 LEU A CG  1 
ATOM   1370 C  CD1 . LEU A 1 169 ? 27.798  16.699 9.338   1.00 24.89  ? 168 LEU A CD1 1 
ATOM   1371 C  CD2 . LEU A 1 169 ? 26.261  16.153 11.265  1.00 26.24  ? 168 LEU A CD2 1 
ATOM   1372 N  N   . ARG A 1 170 ? 30.035  12.976 10.489  1.00 31.13  ? 169 ARG A N   1 
ATOM   1373 C  CA  . ARG A 1 170 ? 31.348  12.876 11.195  1.00 31.66  ? 169 ARG A CA  1 
ATOM   1374 C  C   . ARG A 1 170 ? 32.492  12.776 10.182  1.00 30.49  ? 169 ARG A C   1 
ATOM   1375 O  O   . ARG A 1 170 ? 33.473  13.528 10.288  1.00 33.21  ? 169 ARG A O   1 
ATOM   1376 C  CB  . ARG A 1 170 ? 31.326  11.678 12.144  1.00 46.65  ? 169 ARG A CB  1 
ATOM   1377 C  CG  . ARG A 1 170 ? 32.435  11.682 13.189  1.00 61.68  ? 169 ARG A CG  1 
ATOM   1378 C  CD  . ARG A 1 170 ? 32.220  10.585 14.228  1.00 81.87  ? 169 ARG A CD  1 
ATOM   1379 N  NE  . ARG A 1 170 ? 30.958  10.752 14.950  1.00 90.86  ? 169 ARG A NE  1 
ATOM   1380 C  CZ  . ARG A 1 170 ? 30.499  9.946  15.905  1.00 95.62  ? 169 ARG A CZ  1 
ATOM   1381 N  NH1 . ARG A 1 170 ? 29.338  10.207 16.484  1.00 91.31  ? 169 ARG A NH1 1 
ATOM   1382 N  NH2 . ARG A 1 170 ? 31.198  8.891  16.287  1.00 124.36 ? 169 ARG A NH2 1 
ATOM   1383 N  N   . ARG A 1 171 ? 32.356  11.901 9.185   1.00 32.96  ? 170 ARG A N   1 
ATOM   1384 C  CA  . ARG A 1 171 ? 33.376  11.732 8.127   1.00 34.93  ? 170 ARG A CA  1 
ATOM   1385 C  C   . ARG A 1 171 ? 33.556  13.042 7.350   1.00 33.67  ? 170 ARG A C   1 
ATOM   1386 O  O   . ARG A 1 171 ? 34.694  13.406 7.069   1.00 35.72  ? 170 ARG A O   1 
ATOM   1387 C  CB  . ARG A 1 171 ? 32.973  10.613 7.166   1.00 40.85  ? 170 ARG A CB  1 
ATOM   1388 C  CG  . ARG A 1 171 ? 33.908  10.444 5.979   1.00 45.15  ? 170 ARG A CG  1 
ATOM   1389 C  CD  . ARG A 1 171 ? 33.292  9.393  5.102   1.00 55.01  ? 170 ARG A CD  1 
ATOM   1390 N  NE  . ARG A 1 171 ? 34.011  9.078  3.882   1.00 50.74  ? 170 ARG A NE  1 
ATOM   1391 C  CZ  . ARG A 1 171 ? 34.794  8.019  3.719   1.00 65.48  ? 170 ARG A CZ  1 
ATOM   1392 N  NH1 . ARG A 1 171 ? 35.058  7.208  4.729   1.00 59.18  ? 170 ARG A NH1 1 
ATOM   1393 N  NH2 . ARG A 1 171 ? 35.337  7.784  2.540   1.00 66.99  ? 170 ARG A NH2 1 
ATOM   1394 N  N   . TYR A 1 172 ? 32.470  13.699 6.949   1.00 30.03  ? 171 TYR A N   1 
ATOM   1395 C  CA  . TYR A 1 172 ? 32.545  14.961 6.165   1.00 33.12  ? 171 TYR A CA  1 
ATOM   1396 C  C   . TYR A 1 172 ? 33.230  16.083 6.969   1.00 30.18  ? 171 TYR A C   1 
ATOM   1397 O  O   . TYR A 1 172 ? 34.046  16.797 6.388   1.00 31.38  ? 171 TYR A O   1 
ATOM   1398 C  CB  . TYR A 1 172 ? 31.167  15.380 5.643   1.00 30.35  ? 171 TYR A CB  1 
ATOM   1399 C  CG  . TYR A 1 172 ? 30.561  14.342 4.739   1.00 28.28  ? 171 TYR A CG  1 
ATOM   1400 C  CD1 . TYR A 1 172 ? 31.359  13.566 3.905   1.00 26.88  ? 171 TYR A CD1 1 
ATOM   1401 C  CD2 . TYR A 1 172 ? 29.192  14.123 4.730   1.00 26.43  ? 171 TYR A CD2 1 
ATOM   1402 C  CE1 . TYR A 1 172 ? 30.801  12.600 3.069   1.00 33.31  ? 171 TYR A CE1 1 
ATOM   1403 C  CE2 . TYR A 1 172 ? 28.624  13.156 3.912   1.00 28.73  ? 171 TYR A CE2 1 
ATOM   1404 C  CZ  . TYR A 1 172 ? 29.429  12.362 3.104   1.00 31.91  ? 171 TYR A CZ  1 
ATOM   1405 O  OH  . TYR A 1 172 ? 28.866  11.427 2.276   1.00 27.08  ? 171 TYR A OH  1 
ATOM   1406 N  N   . LEU A 1 173 ? 32.910  16.229 8.247   1.00 29.72  ? 172 LEU A N   1 
ATOM   1407 C  CA  . LEU A 1 173 ? 33.603  17.209 9.139   1.00 34.05  ? 172 LEU A CA  1 
ATOM   1408 C  C   . LEU A 1 173 ? 35.108  16.904 9.193   1.00 41.59  ? 172 LEU A C   1 
ATOM   1409 O  O   . LEU A 1 173 ? 35.924  17.858 9.056   1.00 37.68  ? 172 LEU A O   1 
ATOM   1410 C  CB  . LEU A 1 173 ? 32.953  17.139 10.521  1.00 37.20  ? 172 LEU A CB  1 
ATOM   1411 C  CG  . LEU A 1 173 ? 31.515  17.661 10.578  1.00 29.69  ? 172 LEU A CG  1 
ATOM   1412 C  CD1 . LEU A 1 173 ? 30.924  17.413 11.953  1.00 34.34  ? 172 LEU A CD1 1 
ATOM   1413 C  CD2 . LEU A 1 173 ? 31.447  19.146 10.226  1.00 32.10  ? 172 LEU A CD2 1 
ATOM   1414 N  N   . GLU A 1 174 ? 35.473  15.623 9.302   1.00 44.88  ? 173 GLU A N   1 
ATOM   1415 C  CA  . GLU A 1 174 ? 36.888  15.164 9.213   1.00 45.31  ? 173 GLU A CA  1 
ATOM   1416 C  C   . GLU A 1 174 ? 37.483  15.562 7.850   1.00 41.75  ? 173 GLU A C   1 
ATOM   1417 O  O   . GLU A 1 174 ? 38.570  16.152 7.849   1.00 49.95  ? 173 GLU A O   1 
ATOM   1418 C  CB  . GLU A 1 174 ? 36.958  13.661 9.486   1.00 56.31  ? 173 GLU A CB  1 
ATOM   1419 C  CG  . GLU A 1 174 ? 38.367  13.103 9.572   1.00 81.41  ? 173 GLU A CG  1 
ATOM   1420 C  CD  . GLU A 1 174 ? 39.198  13.649 10.719  1.00 93.14  ? 173 GLU A CD  1 
ATOM   1421 O  OE1 . GLU A 1 174 ? 38.608  14.198 11.669  1.00 99.20  ? 173 GLU A OE1 1 
ATOM   1422 O  OE2 . GLU A 1 174 ? 40.433  13.527 10.655  1.00 101.87 ? 173 GLU A OE2 1 
ATOM   1423 N  N   . ASN A 1 175 ? 36.805  15.317 6.725   1.00 39.49  ? 174 ASN A N   1 
ATOM   1424 C  CA  . ASN A 1 175 ? 37.301  15.730 5.380   1.00 38.69  ? 174 ASN A CA  1 
ATOM   1425 C  C   . ASN A 1 175 ? 37.477  17.259 5.329   1.00 36.66  ? 174 ASN A C   1 
ATOM   1426 O  O   . ASN A 1 175 ? 38.458  17.731 4.749   1.00 38.29  ? 174 ASN A O   1 
ATOM   1427 C  CB  . ASN A 1 175 ? 36.342  15.395 4.228   1.00 44.65  ? 174 ASN A CB  1 
ATOM   1428 C  CG  . ASN A 1 175 ? 36.128  13.923 3.933   1.00 69.61  ? 174 ASN A CG  1 
ATOM   1429 O  OD1 . ASN A 1 175 ? 36.755  13.056 4.537   1.00 54.35  ? 174 ASN A OD1 1 
ATOM   1430 N  ND2 . ASN A 1 175 ? 35.233  13.633 2.995   1.00 49.73  ? 174 ASN A ND2 1 
ATOM   1431 N  N   . GLY A 1 176 ? 36.438  17.979 5.746   1.00 36.05  ? 175 GLY A N   1 
ATOM   1432 C  CA  . GLY A 1 176 ? 36.348  19.439 5.584   1.00 36.64  ? 175 GLY A CA  1 
ATOM   1433 C  C   . GLY A 1 176 ? 37.214  20.227 6.530   1.00 37.19  ? 175 GLY A C   1 
ATOM   1434 O  O   . GLY A 1 176 ? 37.598  21.309 6.146   1.00 41.30  ? 175 GLY A O   1 
ATOM   1435 N  N   . LYS A 1 177 ? 37.376  19.753 7.759   1.00 37.36  ? 176 LYS A N   1 
ATOM   1436 C  CA  . LYS A 1 177 ? 38.237  20.450 8.747   1.00 49.64  ? 176 LYS A CA  1 
ATOM   1437 C  C   . LYS A 1 177 ? 37.787  21.910 8.909   1.00 52.49  ? 176 LYS A C   1 
ATOM   1438 O  O   . LYS A 1 177 ? 36.645  22.127 9.238   1.00 35.76  ? 176 LYS A O   1 
ATOM   1439 C  CB  . LYS A 1 177 ? 39.715  20.225 8.415   1.00 59.21  ? 176 LYS A CB  1 
ATOM   1440 C  CG  . LYS A 1 177 ? 40.150  18.772 8.526   1.00 70.82  ? 176 LYS A CG  1 
ATOM   1441 C  CD  . LYS A 1 177 ? 41.607  18.531 8.251   1.00 85.64  ? 176 LYS A CD  1 
ATOM   1442 C  CE  . LYS A 1 177 ? 41.880  18.233 6.797   1.00 88.58  ? 176 LYS A CE  1 
ATOM   1443 N  NZ  . LYS A 1 177 ? 41.335  16.913 6.400   1.00 82.73  ? 176 LYS A NZ  1 
ATOM   1444 N  N   . ASP A 1 178 ? 38.697  22.853 8.672   1.00 53.52  ? 177 ASP A N   1 
ATOM   1445 C  CA  . ASP A 1 178 ? 38.450  24.312 8.841   1.00 56.15  ? 177 ASP A CA  1 
ATOM   1446 C  C   . ASP A 1 178 ? 37.377  24.831 7.879   1.00 45.54  ? 177 ASP A C   1 
ATOM   1447 O  O   . ASP A 1 178 ? 36.762  25.820 8.204   1.00 38.68  ? 177 ASP A O   1 
ATOM   1448 C  CB  . ASP A 1 178 ? 39.744  25.118 8.760   1.00 54.17  ? 177 ASP A CB  1 
ATOM   1449 C  CG  . ASP A 1 178 ? 40.492  24.870 7.470   1.00 59.91  ? 177 ASP A CG  1 
ATOM   1450 O  OD1 . ASP A 1 178 ? 41.131  23.827 7.363   1.00 77.99  ? 177 ASP A OD1 1 
ATOM   1451 O  OD2 . ASP A 1 178 ? 40.374  25.692 6.571   1.00 76.44  ? 177 ASP A OD2 1 
ATOM   1452 N  N   . LYS A 1 179 ? 37.248  24.232 6.702   1.00 41.88  ? 178 LYS A N   1 
ATOM   1453 C  CA  . LYS A 1 179 ? 36.248  24.698 5.709   1.00 45.61  ? 178 LYS A CA  1 
ATOM   1454 C  C   . LYS A 1 179 ? 34.824  24.517 6.247   1.00 40.20  ? 178 LYS A C   1 
ATOM   1455 O  O   . LYS A 1 179 ? 33.936  25.209 5.798   1.00 40.28  ? 178 LYS A O   1 
ATOM   1456 C  CB  . LYS A 1 179 ? 36.466  24.012 4.360   1.00 58.79  ? 178 LYS A CB  1 
ATOM   1457 C  CG  . LYS A 1 179 ? 37.845  24.212 3.752   1.00 65.63  ? 178 LYS A CG  1 
ATOM   1458 C  CD  . LYS A 1 179 ? 37.845  24.285 2.240   1.00 85.62  ? 178 LYS A CD  1 
ATOM   1459 C  CE  . LYS A 1 179 ? 39.209  24.518 1.626   1.00 89.11  ? 178 LYS A CE  1 
ATOM   1460 N  NZ  . LYS A 1 179 ? 39.128  24.963 0.212   1.00 84.12  ? 178 LYS A NZ  1 
ATOM   1461 N  N   . LEU A 1 180 ? 34.626  23.587 7.160   1.00 30.89  ? 179 LEU A N   1 
ATOM   1462 C  CA  . LEU A 1 180 ? 33.281  23.366 7.741   1.00 38.45  ? 179 LEU A CA  1 
ATOM   1463 C  C   . LEU A 1 180 ? 33.246  23.896 9.177   1.00 32.67  ? 179 LEU A C   1 
ATOM   1464 O  O   . LEU A 1 180 ? 32.174  24.346 9.594   1.00 34.32  ? 179 LEU A O   1 
ATOM   1465 C  CB  . LEU A 1 180 ? 32.934  21.877 7.641   1.00 31.43  ? 179 LEU A CB  1 
ATOM   1466 C  CG  . LEU A 1 180 ? 32.760  21.346 6.224   1.00 30.14  ? 179 LEU A CG  1 
ATOM   1467 C  CD1 . LEU A 1 180 ? 32.517  19.833 6.251   1.00 32.75  ? 179 LEU A CD1 1 
ATOM   1468 C  CD2 . LEU A 1 180 ? 31.612  22.057 5.507   1.00 30.76  ? 179 LEU A CD2 1 
ATOM   1469 N  N   . GLU A 1 181 ? 34.359  23.819 9.920   1.00 35.85  ? 180 GLU A N   1 
ATOM   1470 C  CA  . GLU A 1 181 ? 34.383  24.225 11.350  1.00 42.08  ? 180 GLU A CA  1 
ATOM   1471 C  C   . GLU A 1 181 ? 34.287  25.768 11.473  1.00 41.29  ? 180 GLU A C   1 
ATOM   1472 O  O   . GLU A 1 181 ? 33.626  26.236 12.427  1.00 55.61  ? 180 GLU A O   1 
ATOM   1473 C  CB  . GLU A 1 181 ? 35.597  23.594 12.045  1.00 43.16  ? 180 GLU A CB  1 
ATOM   1474 C  CG  . GLU A 1 181 ? 35.401  23.491 13.541  1.00 46.19  ? 180 GLU A CG  1 
ATOM   1475 C  CD  . GLU A 1 181 ? 34.143  22.735 13.942  1.00 54.40  ? 180 GLU A CD  1 
ATOM   1476 O  OE1 . GLU A 1 181 ? 33.433  23.229 14.831  1.00 75.86  ? 180 GLU A OE1 1 
ATOM   1477 O  OE2 . GLU A 1 181 ? 33.885  21.637 13.374  1.00 62.44  ? 180 GLU A OE2 1 
ATOM   1478 N  N   . ARG A 1 182 ? 34.870  26.530 10.553  1.00 52.45  ? 181 ARG A N   1 
ATOM   1479 C  CA  . ARG A 1 182 ? 34.852  28.026 10.521  1.00 55.72  ? 181 ARG A CA  1 
ATOM   1480 C  C   . ARG A 1 182 ? 33.475  28.619 10.840  1.00 45.94  ? 181 ARG A C   1 
ATOM   1481 O  O   . ARG A 1 182 ? 32.466  28.160 10.303  1.00 63.34  ? 181 ARG A O   1 
ATOM   1482 C  CB  . ARG A 1 182 ? 35.231  28.562 9.134   1.00 85.30  ? 181 ARG A CB  1 
ATOM   1483 C  CG  . ARG A 1 182 ? 34.235  28.241 8.020   1.00 64.63  ? 181 ARG A CG  1 
ATOM   1484 C  CD  . ARG A 1 182 ? 34.327  29.174 6.817   1.00 65.80  ? 181 ARG A CD  1 
ATOM   1485 N  NE  . ARG A 1 182 ? 33.493  28.680 5.723   1.00 56.71  ? 181 ARG A NE  1 
ATOM   1486 C  CZ  . ARG A 1 182 ? 32.882  29.409 4.788   1.00 48.14  ? 181 ARG A CZ  1 
ATOM   1487 N  NH1 . ARG A 1 182 ? 32.132  28.777 3.902   1.00 39.92  ? 181 ARG A NH1 1 
ATOM   1488 N  NH2 . ARG A 1 182 ? 32.955  30.741 4.747   1.00 33.44  ? 181 ARG A NH2 1 
ATOM   1489 N  N   . ALA A 1 183 ? 33.449  29.633 11.702  1.00 37.92  ? 182 ALA A N   1 
ATOM   1490 C  CA  . ALA A 1 183 ? 32.408  30.678 11.750  1.00 27.05  ? 182 ALA A CA  1 
ATOM   1491 C  C   . ALA A 1 183 ? 33.046  32.005 11.313  1.00 37.36  ? 182 ALA A C   1 
ATOM   1492 O  O   . ALA A 1 183 ? 33.895  32.516 12.051  1.00 41.17  ? 182 ALA A O   1 
ATOM   1493 C  CB  . ALA A 1 183 ? 31.808  30.727 13.127  1.00 31.76  ? 182 ALA A CB  1 
ATOM   1494 N  N   . ASP A 1 184 ? 32.746  32.480 10.099  1.00 26.68  ? 183 ASP A N   1 
ATOM   1495 C  CA  . ASP A 1 184 ? 33.248  33.777 9.575   1.00 24.86  ? 183 ASP A CA  1 
ATOM   1496 C  C   . ASP A 1 184 ? 32.292  34.859 10.058  1.00 26.80  ? 183 ASP A C   1 
ATOM   1497 O  O   . ASP A 1 184 ? 31.106  34.861 9.686   1.00 22.18  ? 183 ASP A O   1 
ATOM   1498 C  CB  . ASP A 1 184 ? 33.397  33.779 8.062   1.00 34.78  ? 183 ASP A CB  1 
ATOM   1499 C  CG  . ASP A 1 184 ? 34.465  32.823 7.548   1.00 46.45  ? 183 ASP A CG  1 
ATOM   1500 O  OD1 . ASP A 1 184 ? 35.481  32.614 8.240   1.00 36.51  ? 183 ASP A OD1 1 
ATOM   1501 O  OD2 . ASP A 1 184 ? 34.260  32.288 6.461   1.00 32.54  ? 183 ASP A OD2 1 
ATOM   1502 N  N   . PRO A 1 185 ? 32.778  35.765 10.934  1.00 27.98  ? 184 PRO A N   1 
ATOM   1503 C  CA  . PRO A 1 185 ? 31.963  36.837 11.491  1.00 26.08  ? 184 PRO A CA  1 
ATOM   1504 C  C   . PRO A 1 185 ? 31.612  37.813 10.399  1.00 21.43  ? 184 PRO A C   1 
ATOM   1505 O  O   . PRO A 1 185 ? 32.339  37.961 9.401   1.00 19.91  ? 184 PRO A O   1 
ATOM   1506 C  CB  . PRO A 1 185 ? 32.848  37.520 12.556  1.00 28.40  ? 184 PRO A CB  1 
ATOM   1507 C  CG  . PRO A 1 185 ? 34.245  37.190 12.105  1.00 31.97  ? 184 PRO A CG  1 
ATOM   1508 C  CD  . PRO A 1 185 ? 34.163  35.827 11.445  1.00 32.78  ? 184 PRO A CD  1 
ATOM   1509 N  N   . PRO A 1 186 ? 30.468  38.485 10.540  1.00 21.34  ? 185 PRO A N   1 
ATOM   1510 C  CA  . PRO A 1 186 ? 30.070  39.480 9.566   1.00 28.37  ? 185 PRO A CA  1 
ATOM   1511 C  C   . PRO A 1 186 ? 30.997  40.680 9.606   1.00 26.92  ? 185 PRO A C   1 
ATOM   1512 O  O   . PRO A 1 186 ? 31.385  41.092 10.677  1.00 24.85  ? 185 PRO A O   1 
ATOM   1513 C  CB  . PRO A 1 186 ? 28.673  39.895 10.019  1.00 21.60  ? 185 PRO A CB  1 
ATOM   1514 C  CG  . PRO A 1 186 ? 28.667  39.621 11.488  1.00 20.65  ? 185 PRO A CG  1 
ATOM   1515 C  CD  . PRO A 1 186 ? 29.463  38.349 11.616  1.00 22.70  ? 185 PRO A CD  1 
ATOM   1516 N  N   . LYS A 1 187 ? 31.220  41.261 8.429   1.00 23.87  ? 186 LYS A N   1 
ATOM   1517 C  CA  . LYS A 1 187 ? 31.786  42.618 8.275   1.00 25.28  ? 186 LYS A CA  1 
ATOM   1518 C  C   . LYS A 1 187 ? 30.622  43.593 8.355   1.00 23.71  ? 186 LYS A C   1 
ATOM   1519 O  O   . LYS A 1 187 ? 29.756  43.484 7.499   1.00 24.31  ? 186 LYS A O   1 
ATOM   1520 C  CB  . LYS A 1 187 ? 32.493  42.706 6.922   1.00 28.96  ? 186 LYS A CB  1 
ATOM   1521 C  CG  . LYS A 1 187 ? 33.452  41.538 6.654   1.00 38.50  ? 186 LYS A CG  1 
ATOM   1522 C  CD  . LYS A 1 187 ? 34.044  41.525 5.245   1.00 35.29  ? 186 LYS A CD  1 
ATOM   1523 C  CE  . LYS A 1 187 ? 34.978  40.353 5.070   1.00 47.79  ? 186 LYS A CE  1 
ATOM   1524 N  NZ  . LYS A 1 187 ? 36.101  40.408 6.046   1.00 48.61  ? 186 LYS A NZ  1 
ATOM   1525 N  N   . THR A 1 188 ? 30.581  44.496 9.326   1.00 20.23  ? 187 THR A N   1 
ATOM   1526 C  CA  . THR A 1 188 ? 29.397  45.356 9.579   1.00 19.88  ? 187 THR A CA  1 
ATOM   1527 C  C   . THR A 1 188 ? 29.724  46.811 9.307   1.00 21.97  ? 187 THR A C   1 
ATOM   1528 O  O   . THR A 1 188 ? 30.901  47.243 9.597   1.00 24.76  ? 187 THR A O   1 
ATOM   1529 C  CB  . THR A 1 188 ? 28.897  45.140 10.999  1.00 25.99  ? 187 THR A CB  1 
ATOM   1530 O  OG1 . THR A 1 188 ? 29.967  45.481 11.899  1.00 24.99  ? 187 THR A OG1 1 
ATOM   1531 C  CG2 . THR A 1 188 ? 28.438  43.720 11.180  1.00 22.89  ? 187 THR A CG2 1 
ATOM   1532 N  N   . HIS A 1 189 ? 28.728  47.540 8.797   1.00 24.15  ? 188 HIS A N   1 
ATOM   1533 C  CA  . HIS A 1 189 ? 28.801  49.006 8.590   1.00 23.91  ? 188 HIS A CA  1 
ATOM   1534 C  C   . HIS A 1 189 ? 27.400  49.558 8.460   1.00 27.31  ? 188 HIS A C   1 
ATOM   1535 O  O   . HIS A 1 189 ? 26.483  48.805 8.155   1.00 24.06  ? 188 HIS A O   1 
ATOM   1536 C  CB  . HIS A 1 189 ? 29.691  49.371 7.383   1.00 22.16  ? 188 HIS A CB  1 
ATOM   1537 C  CG  . HIS A 1 189 ? 29.123  49.091 6.029   1.00 24.65  ? 188 HIS A CG  1 
ATOM   1538 N  ND1 . HIS A 1 189 ? 29.152  47.822 5.450   1.00 22.41  ? 188 HIS A ND1 1 
ATOM   1539 C  CD2 . HIS A 1 189 ? 28.595  49.927 5.108   1.00 25.11  ? 188 HIS A CD2 1 
ATOM   1540 C  CE1 . HIS A 1 189 ? 28.659  47.903 4.226   1.00 24.63  ? 188 HIS A CE1 1 
ATOM   1541 N  NE2 . HIS A 1 189 ? 28.296  49.190 4.002   1.00 22.70  ? 188 HIS A NE2 1 
ATOM   1542 N  N   . VAL A 1 190 ? 27.294  50.848 8.689   1.00 25.46  ? 189 VAL A N   1 
ATOM   1543 C  CA  . VAL A 1 190 ? 26.035  51.609 8.591   1.00 25.19  ? 189 VAL A CA  1 
ATOM   1544 C  C   . VAL A 1 190 ? 26.205  52.678 7.522   1.00 27.42  ? 189 VAL A C   1 
ATOM   1545 O  O   . VAL A 1 190 ? 27.217  53.401 7.532   1.00 26.45  ? 189 VAL A O   1 
ATOM   1546 C  CB  . VAL A 1 190 ? 25.646  52.205 9.947   1.00 26.07  ? 189 VAL A CB  1 
ATOM   1547 C  CG1 . VAL A 1 190 ? 24.385  53.030 9.798   1.00 26.16  ? 189 VAL A CG1 1 
ATOM   1548 C  CG2 . VAL A 1 190 ? 25.501  51.092 10.985  1.00 25.68  ? 189 VAL A CG2 1 
ATOM   1549 N  N   . THR A 1 191 ? 25.200  52.783 6.661   1.00 26.94  ? 190 THR A N   1 
ATOM   1550 C  CA  . THR A 1 191 ? 25.092  53.836 5.639   1.00 26.61  ? 190 THR A CA  1 
ATOM   1551 C  C   . THR A 1 191 ? 23.877  54.710 5.947   1.00 26.33  ? 190 THR A C   1 
ATOM   1552 O  O   . THR A 1 191 ? 22.936  54.251 6.623   1.00 23.81  ? 190 THR A O   1 
ATOM   1553 C  CB  . THR A 1 191 ? 25.078  53.216 4.227   1.00 26.41  ? 190 THR A CB  1 
ATOM   1554 O  OG1 . THR A 1 191 ? 24.016  52.274 4.076   1.00 25.11  ? 190 THR A OG1 1 
ATOM   1555 C  CG2 . THR A 1 191 ? 26.382  52.539 3.901   1.00 27.16  ? 190 THR A CG2 1 
ATOM   1556 N  N   . HIS A 1 192 ? 23.887  55.918 5.390   1.00 28.06  ? 191 HIS A N   1 
ATOM   1557 C  CA  . HIS A 1 192 ? 22.919  56.999 5.683   1.00 28.58  ? 191 HIS A CA  1 
ATOM   1558 C  C   . HIS A 1 192 ? 22.343  57.476 4.355   1.00 30.77  ? 191 HIS A C   1 
ATOM   1559 O  O   . HIS A 1 192 ? 23.142  57.816 3.485   1.00 33.01  ? 191 HIS A O   1 
ATOM   1560 C  CB  . HIS A 1 192 ? 23.688  58.095 6.431   1.00 34.11  ? 191 HIS A CB  1 
ATOM   1561 C  CG  . HIS A 1 192 ? 22.874  59.279 6.810   1.00 34.05  ? 191 HIS A CG  1 
ATOM   1562 N  ND1 . HIS A 1 192 ? 22.550  60.267 5.890   1.00 38.86  ? 191 HIS A ND1 1 
ATOM   1563 C  CD2 . HIS A 1 192 ? 22.319  59.642 7.984   1.00 38.01  ? 191 HIS A CD2 1 
ATOM   1564 C  CE1 . HIS A 1 192 ? 21.830  61.188 6.496   1.00 56.55  ? 191 HIS A CE1 1 
ATOM   1565 N  NE2 . HIS A 1 192 ? 21.688  60.843 7.780   1.00 36.17  ? 191 HIS A NE2 1 
ATOM   1566 N  N   . HIS A 1 193 ? 21.031  57.444 4.181   1.00 32.31  ? 192 HIS A N   1 
ATOM   1567 C  CA  . HIS A 1 193 ? 20.378  57.719 2.877   1.00 34.85  ? 192 HIS A CA  1 
ATOM   1568 C  C   . HIS A 1 193 ? 19.259  58.739 3.098   1.00 33.20  ? 192 HIS A C   1 
ATOM   1569 O  O   . HIS A 1 193 ? 18.146  58.353 3.466   1.00 33.24  ? 192 HIS A O   1 
ATOM   1570 C  CB  . HIS A 1 193 ? 19.907  56.401 2.256   1.00 31.74  ? 192 HIS A CB  1 
ATOM   1571 C  CG  . HIS A 1 193 ? 20.944  55.336 2.251   1.00 40.37  ? 192 HIS A CG  1 
ATOM   1572 N  ND1 . HIS A 1 193 ? 21.805  55.152 1.185   1.00 32.31  ? 192 HIS A ND1 1 
ATOM   1573 C  CD2 . HIS A 1 193 ? 21.263  54.399 3.175   1.00 33.82  ? 192 HIS A CD2 1 
ATOM   1574 C  CE1 . HIS A 1 193 ? 22.612  54.141 1.462   1.00 37.49  ? 192 HIS A CE1 1 
ATOM   1575 N  NE2 . HIS A 1 193 ? 22.300  53.654 2.665   1.00 30.38  ? 192 HIS A NE2 1 
ATOM   1576 N  N   . PRO A 1 194 ? 19.540  60.059 2.925   1.00 43.96  ? 193 PRO A N   1 
ATOM   1577 C  CA  . PRO A 1 194 ? 18.538  61.116 3.094   1.00 41.45  ? 193 PRO A CA  1 
ATOM   1578 C  C   . PRO A 1 194 ? 17.299  60.856 2.238   1.00 38.20  ? 193 PRO A C   1 
ATOM   1579 O  O   . PRO A 1 194 ? 17.466  60.447 1.094   1.00 42.58  ? 193 PRO A O   1 
ATOM   1580 C  CB  . PRO A 1 194 ? 19.233  62.398 2.623   1.00 46.69  ? 193 PRO A CB  1 
ATOM   1581 C  CG  . PRO A 1 194 ? 20.711  62.100 2.800   1.00 48.59  ? 193 PRO A CG  1 
ATOM   1582 C  CD  . PRO A 1 194 ? 20.852  60.610 2.540   1.00 50.50  ? 193 PRO A CD  1 
ATOM   1583 N  N   . ILE A 1 195 ? 16.122  61.025 2.834   1.00 42.80  ? 194 ILE A N   1 
ATOM   1584 C  CA  . ILE A 1 195 ? 14.825  60.827 2.129   1.00 52.02  ? 194 ILE A CA  1 
ATOM   1585 C  C   . ILE A 1 195 ? 14.289  62.218 1.783   1.00 53.40  ? 194 ILE A C   1 
ATOM   1586 O  O   . ILE A 1 195 ? 14.075  62.511 0.629   1.00 55.17  ? 194 ILE A O   1 
ATOM   1587 C  CB  . ILE A 1 195 ? 13.849  60.043 3.015   1.00 45.83  ? 194 ILE A CB  1 
ATOM   1588 C  CG1 . ILE A 1 195 ? 14.287  58.590 3.178   1.00 46.53  ? 194 ILE A CG1 1 
ATOM   1589 C  CG2 . ILE A 1 195 ? 12.454  60.124 2.445   1.00 57.47  ? 194 ILE A CG2 1 
ATOM   1590 C  CD1 . ILE A 1 195 ? 13.743  57.944 4.411   1.00 55.91  ? 194 ILE A CD1 1 
ATOM   1591 N  N   . SER A 1 196 ? 14.099  63.024 2.809   1.00 61.97  ? 195 SER A N   1 
ATOM   1592 C  CA  . SER A 1 196 ? 13.661  64.438 2.714   1.00 65.66  ? 195 SER A CA  1 
ATOM   1593 C  C   . SER A 1 196 ? 14.601  65.253 3.600   1.00 66.77  ? 195 SER A C   1 
ATOM   1594 O  O   . SER A 1 196 ? 15.658  64.756 3.989   1.00 58.28  ? 195 SER A O   1 
ATOM   1595 C  CB  . SER A 1 196 ? 12.241  64.567 3.156   1.00 61.06  ? 195 SER A CB  1 
ATOM   1596 O  OG  . SER A 1 196 ? 12.080  64.102 4.475   1.00 50.45  ? 195 SER A OG  1 
ATOM   1597 N  N   . ASP A 1 197 ? 14.241  66.484 3.933   1.00 75.63  ? 196 ASP A N   1 
ATOM   1598 C  CA  . ASP A 1 197 ? 15.129  67.228 4.862   1.00 75.01  ? 196 ASP A CA  1 
ATOM   1599 C  C   . ASP A 1 197 ? 14.776  66.839 6.298   1.00 71.24  ? 196 ASP A C   1 
ATOM   1600 O  O   . ASP A 1 197 ? 15.527  67.194 7.192   1.00 96.16  ? 196 ASP A O   1 
ATOM   1601 C  CB  . ASP A 1 197 ? 15.140  68.737 4.598   1.00 94.66  ? 196 ASP A CB  1 
ATOM   1602 C  CG  . ASP A 1 197 ? 16.225  69.173 3.622   1.00 114.55 ? 196 ASP A CG  1 
ATOM   1603 O  OD1 . ASP A 1 197 ? 17.369  69.352 4.053   1.00 133.21 ? 196 ASP A OD1 1 
ATOM   1604 O  OD2 . ASP A 1 197 ? 15.915  69.336 2.439   1.00 85.22  ? 196 ASP A OD2 1 
ATOM   1605 N  N   . HIS A 1 198 ? 13.652  66.168 6.517   1.00 56.61  ? 197 HIS A N   1 
ATOM   1606 C  CA  . HIS A 1 198 ? 13.292  65.781 7.895   1.00 70.82  ? 197 HIS A CA  1 
ATOM   1607 C  C   . HIS A 1 198 ? 13.651  64.320 8.201   1.00 83.73  ? 197 HIS A C   1 
ATOM   1608 O  O   . HIS A 1 198 ? 13.672  64.005 9.382   1.00 57.35  ? 197 HIS A O   1 
ATOM   1609 C  CB  . HIS A 1 198 ? 11.809  66.073 8.081   1.00 77.90  ? 197 HIS A CB  1 
ATOM   1610 C  CG  . HIS A 1 198 ? 11.394  67.284 7.322   1.00 109.15 ? 197 HIS A CG  1 
ATOM   1611 N  ND1 . HIS A 1 198 ? 11.630  68.562 7.787   1.00 105.03 ? 197 HIS A ND1 1 
ATOM   1612 C  CD2 . HIS A 1 198 ? 10.803  67.423 6.118   1.00 114.07 ? 197 HIS A CD2 1 
ATOM   1613 C  CE1 . HIS A 1 198 ? 11.178  69.433 6.918   1.00 100.30 ? 197 HIS A CE1 1 
ATOM   1614 N  NE2 . HIS A 1 198 ? 10.670  68.761 5.887   1.00 118.85 ? 197 HIS A NE2 1 
ATOM   1615 N  N   . GLU A 1 199 ? 14.005  63.498 7.204   1.00 65.83  ? 198 GLU A N   1 
ATOM   1616 C  CA  . GLU A 1 199 ? 14.203  62.046 7.487   1.00 59.09  ? 198 GLU A CA  1 
ATOM   1617 C  C   . GLU A 1 199 ? 15.305  61.381 6.650   1.00 57.36  ? 198 GLU A C   1 
ATOM   1618 O  O   . GLU A 1 199 ? 15.451  61.726 5.493   1.00 39.96  ? 198 GLU A O   1 
ATOM   1619 C  CB  . GLU A 1 199 ? 12.950  61.301 7.033   1.00 57.22  ? 198 GLU A CB  1 
ATOM   1620 C  CG  . GLU A 1 199 ? 11.725  61.547 7.876   1.00 67.77  ? 198 GLU A CG  1 
ATOM   1621 C  CD  . GLU A 1 199 ? 10.581  60.616 7.557   1.00 53.89  ? 198 GLU A CD  1 
ATOM   1622 O  OE1 . GLU A 1 199 ? 10.216  60.526 6.394   1.00 53.29  ? 198 GLU A OE1 1 
ATOM   1623 O  OE2 . GLU A 1 199 ? 10.086  59.976 8.478   1.00 59.57  ? 198 GLU A OE2 1 
ATOM   1624 N  N   . ALA A 1 200 ? 15.952  60.357 7.221   1.00 39.36  ? 199 ALA A N   1 
ATOM   1625 C  CA  . ALA A 1 200 ? 16.963  59.558 6.495   1.00 42.20  ? 199 ALA A CA  1 
ATOM   1626 C  C   . ALA A 1 200 ? 16.846  58.085 6.893   1.00 33.98  ? 199 ALA A C   1 
ATOM   1627 O  O   . ALA A 1 200 ? 16.521  57.815 8.055   1.00 37.36  ? 199 ALA A O   1 
ATOM   1628 C  CB  . ALA A 1 200 ? 18.343  60.113 6.754   1.00 41.45  ? 199 ALA A CB  1 
ATOM   1629 N  N   . THR A 1 201 ? 17.041  57.184 5.931   1.00 32.64  ? 200 THR A N   1 
ATOM   1630 C  CA  . THR A 1 201 ? 17.240  55.725 6.162   1.00 31.36  ? 200 THR A CA  1 
ATOM   1631 C  C   . THR A 1 201 ? 18.654  55.507 6.714   1.00 26.04  ? 200 THR A C   1 
ATOM   1632 O  O   . THR A 1 201 ? 19.661  55.889 6.048   1.00 31.55  ? 200 THR A O   1 
ATOM   1633 C  CB  . THR A 1 201 ? 17.022  54.912 4.884   1.00 34.68  ? 200 THR A CB  1 
ATOM   1634 O  OG1 . THR A 1 201 ? 15.713  55.223 4.407   1.00 39.58  ? 200 THR A OG1 1 
ATOM   1635 C  CG2 . THR A 1 201 ? 17.144  53.417 5.087   1.00 31.31  ? 200 THR A CG2 1 
ATOM   1636 N  N   . LEU A 1 202 ? 18.736  54.853 7.858   1.00 31.53  ? 201 LEU A N   1 
ATOM   1637 C  CA  . LEU A 1 202 ? 19.988  54.201 8.306   1.00 24.90  ? 201 LEU A CA  1 
ATOM   1638 C  C   . LEU A 1 202 ? 19.897  52.730 7.919   1.00 30.01  ? 201 LEU A C   1 
ATOM   1639 O  O   . LEU A 1 202 ? 18.902  52.098 8.259   1.00 27.20  ? 201 LEU A O   1 
ATOM   1640 C  CB  . LEU A 1 202 ? 20.160  54.355 9.817   1.00 29.63  ? 201 LEU A CB  1 
ATOM   1641 C  CG  . LEU A 1 202 ? 20.233  55.788 10.328  1.00 31.07  ? 201 LEU A CG  1 
ATOM   1642 C  CD1 . LEU A 1 202 ? 20.671  55.789 11.779  1.00 41.21  ? 201 LEU A CD1 1 
ATOM   1643 C  CD2 . LEU A 1 202 ? 21.187  56.646 9.485   1.00 33.93  ? 201 LEU A CD2 1 
ATOM   1644 N  N   . ARG A 1 203 ? 20.897  52.234 7.197   1.00 27.53  ? 202 ARG A N   1 
ATOM   1645 C  CA  . ARG A 1 203 ? 20.945  50.840 6.723   1.00 24.90  ? 202 ARG A CA  1 
ATOM   1646 C  C   . ARG A 1 203 ? 22.175  50.194 7.371   1.00 25.97  ? 202 ARG A C   1 
ATOM   1647 O  O   . ARG A 1 203 ? 23.316  50.714 7.198   1.00 25.99  ? 202 ARG A O   1 
ATOM   1648 C  CB  . ARG A 1 203 ? 21.017  50.776 5.194   1.00 23.34  ? 202 ARG A CB  1 
ATOM   1649 C  CG  . ARG A 1 203 ? 21.053  49.345 4.672   1.00 21.80  ? 202 ARG A CG  1 
ATOM   1650 C  CD  . ARG A 1 203 ? 20.792  49.204 3.189   1.00 22.47  ? 202 ARG A CD  1 
ATOM   1651 N  NE  . ARG A 1 203 ? 19.436  49.590 2.915   1.00 25.25  ? 202 ARG A NE  1 
ATOM   1652 C  CZ  . ARG A 1 203 ? 19.034  50.679 2.247   1.00 32.61  ? 202 ARG A CZ  1 
ATOM   1653 N  NH1 . ARG A 1 203 ? 19.887  51.514 1.697   1.00 32.41  ? 202 ARG A NH1 1 
ATOM   1654 N  NH2 . ARG A 1 203 ? 17.744  50.940 2.137   1.00 29.74  ? 202 ARG A NH2 1 
ATOM   1655 N  N   . CYS A 1 204 ? 21.915  49.158 8.164   1.00 24.99  ? 203 CYS A N   1 
ATOM   1656 C  CA  . CYS A 1 204 ? 22.929  48.361 8.875   1.00 19.96  ? 203 CYS A CA  1 
ATOM   1657 C  C   . CYS A 1 204 ? 23.203  47.085 8.070   1.00 22.71  ? 203 CYS A C   1 
ATOM   1658 O  O   . CYS A 1 204 ? 22.270  46.283 7.816   1.00 22.20  ? 203 CYS A O   1 
ATOM   1659 C  CB  . CYS A 1 204 ? 22.455  48.057 10.279  1.00 21.64  ? 203 CYS A CB  1 
ATOM   1660 S  SG  . CYS A 1 204 ? 23.728  47.203 11.223  1.00 25.46  ? 203 CYS A SG  1 
ATOM   1661 N  N   . TRP A 1 205 ? 24.432  46.949 7.596   1.00 22.27  ? 204 TRP A N   1 
ATOM   1662 C  CA  . TRP A 1 205 ? 24.892  45.846 6.716   1.00 20.58  ? 204 TRP A CA  1 
ATOM   1663 C  C   . TRP A 1 205 ? 25.710  44.837 7.495   1.00 19.82  ? 204 TRP A C   1 
ATOM   1664 O  O   . TRP A 1 205 ? 26.570  45.233 8.282   1.00 21.23  ? 204 TRP A O   1 
ATOM   1665 C  CB  . TRP A 1 205 ? 25.814  46.386 5.636   1.00 21.73  ? 204 TRP A CB  1 
ATOM   1666 C  CG  . TRP A 1 205 ? 25.199  47.370 4.716   1.00 24.73  ? 204 TRP A CG  1 
ATOM   1667 C  CD1 . TRP A 1 205 ? 25.012  48.701 4.910   1.00 28.41  ? 204 TRP A CD1 1 
ATOM   1668 C  CD2 . TRP A 1 205 ? 24.767  47.073 3.394   1.00 22.24  ? 204 TRP A CD2 1 
ATOM   1669 N  NE1 . TRP A 1 205 ? 24.475  49.251 3.788   1.00 29.78  ? 204 TRP A NE1 1 
ATOM   1670 C  CE2 . TRP A 1 205 ? 24.356  48.288 2.835   1.00 22.79  ? 204 TRP A CE2 1 
ATOM   1671 C  CE3 . TRP A 1 205 ? 24.733  45.910 2.641   1.00 25.83  ? 204 TRP A CE3 1 
ATOM   1672 C  CZ2 . TRP A 1 205 ? 23.862  48.357 1.542   1.00 32.30  ? 204 TRP A CZ2 1 
ATOM   1673 C  CZ3 . TRP A 1 205 ? 24.263  45.987 1.350   1.00 28.55  ? 204 TRP A CZ3 1 
ATOM   1674 C  CH2 . TRP A 1 205 ? 23.842  47.196 0.822   1.00 27.46  ? 204 TRP A CH2 1 
ATOM   1675 N  N   . ALA A 1 206 ? 25.508  43.578 7.176   1.00 19.76  ? 205 ALA A N   1 
ATOM   1676 C  CA  . ALA A 1 206 ? 26.362  42.460 7.582   1.00 21.17  ? 205 ALA A CA  1 
ATOM   1677 C  C   . ALA A 1 206 ? 26.744  41.736 6.307   1.00 24.42  ? 205 ALA A C   1 
ATOM   1678 O  O   . ALA A 1 206 ? 25.811  41.266 5.599   1.00 22.35  ? 205 ALA A O   1 
ATOM   1679 C  CB  . ALA A 1 206 ? 25.614  41.534 8.493   1.00 23.68  ? 205 ALA A CB  1 
ATOM   1680 N  N   . LEU A 1 207 ? 28.035  41.620 6.052   1.00 22.34  ? 206 LEU A N   1 
ATOM   1681 C  CA  . LEU A 1 207 ? 28.564  40.980 4.823   1.00 18.91  ? 206 LEU A CA  1 
ATOM   1682 C  C   . LEU A 1 207 ? 29.615  39.928 5.172   1.00 21.99  ? 206 LEU A C   1 
ATOM   1683 O  O   . LEU A 1 207 ? 30.333  40.094 6.199   1.00 23.10  ? 206 LEU A O   1 
ATOM   1684 C  CB  . LEU A 1 207 ? 29.163  42.048 3.908   1.00 23.16  ? 206 LEU A CB  1 
ATOM   1685 C  CG  . LEU A 1 207 ? 28.189  43.121 3.426   1.00 23.71  ? 206 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A 1 207 ? 28.959  44.240 2.758   1.00 30.06  ? 206 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A 1 207 ? 27.163  42.531 2.489   1.00 26.08  ? 206 LEU A CD2 1 
ATOM   1688 N  N   . GLY A 1 208 ? 29.727  38.927 4.301   1.00 23.09  ? 207 GLY A N   1 
ATOM   1689 C  CA  . GLY A 1 208 ? 30.848  37.973 4.327   1.00 22.37  ? 207 GLY A CA  1 
ATOM   1690 C  C   . GLY A 1 208 ? 30.776  37.033 5.508   1.00 22.61  ? 207 GLY A C   1 
ATOM   1691 O  O   . GLY A 1 208 ? 31.799  36.502 5.864   1.00 27.35  ? 207 GLY A O   1 
ATOM   1692 N  N   . PHE A 1 209 ? 29.587  36.776 6.066   1.00 22.58  ? 208 PHE A N   1 
ATOM   1693 C  CA  . PHE A 1 209 ? 29.431  35.861 7.211   1.00 21.78  ? 208 PHE A CA  1 
ATOM   1694 C  C   . PHE A 1 209 ? 29.044  34.456 6.754   1.00 25.73  ? 208 PHE A C   1 
ATOM   1695 O  O   . PHE A 1 209 ? 28.405  34.211 5.694   1.00 24.51  ? 208 PHE A O   1 
ATOM   1696 C  CB  . PHE A 1 209 ? 28.434  36.374 8.243   1.00 22.40  ? 208 PHE A CB  1 
ATOM   1697 C  CG  . PHE A 1 209 ? 27.057  36.692 7.714   1.00 21.28  ? 208 PHE A CG  1 
ATOM   1698 C  CD1 . PHE A 1 209 ? 26.755  37.944 7.208   1.00 18.52  ? 208 PHE A CD1 1 
ATOM   1699 C  CD2 . PHE A 1 209 ? 26.045  35.762 7.844   1.00 24.38  ? 208 PHE A CD2 1 
ATOM   1700 C  CE1 . PHE A 1 209 ? 25.460  38.234 6.807   1.00 19.22  ? 208 PHE A CE1 1 
ATOM   1701 C  CE2 . PHE A 1 209 ? 24.772  36.046 7.389   1.00 22.24  ? 208 PHE A CE2 1 
ATOM   1702 C  CZ  . PHE A 1 209 ? 24.478  37.285 6.904   1.00 21.26  ? 208 PHE A CZ  1 
ATOM   1703 N  N   . TYR A 1 210 ? 29.422  33.527 7.625   1.00 21.42  ? 209 TYR A N   1 
ATOM   1704 C  CA  . TYR A 1 210 ? 29.113  32.092 7.530   1.00 20.44  ? 209 TYR A CA  1 
ATOM   1705 C  C   . TYR A 1 210 ? 29.174  31.533 8.948   1.00 25.04  ? 209 TYR A C   1 
ATOM   1706 O  O   . TYR A 1 210 ? 30.148  31.751 9.666   1.00 25.34  ? 209 TYR A O   1 
ATOM   1707 C  CB  . TYR A 1 210 ? 30.092  31.392 6.601   1.00 22.02  ? 209 TYR A CB  1 
ATOM   1708 C  CG  . TYR A 1 210 ? 29.793  29.929 6.467   1.00 26.83  ? 209 TYR A CG  1 
ATOM   1709 C  CD1 . TYR A 1 210 ? 30.187  29.033 7.449   1.00 27.75  ? 209 TYR A CD1 1 
ATOM   1710 C  CD2 . TYR A 1 210 ? 29.082  29.443 5.374   1.00 27.05  ? 209 TYR A CD2 1 
ATOM   1711 C  CE1 . TYR A 1 210 ? 29.868  27.685 7.354   1.00 24.38  ? 209 TYR A CE1 1 
ATOM   1712 C  CE2 . TYR A 1 210 ? 28.765  28.097 5.272   1.00 26.34  ? 209 TYR A CE2 1 
ATOM   1713 C  CZ  . TYR A 1 210 ? 29.189  27.211 6.246   1.00 26.12  ? 209 TYR A CZ  1 
ATOM   1714 O  OH  . TYR A 1 210 ? 28.858  25.880 6.213   1.00 26.49  ? 209 TYR A OH  1 
ATOM   1715 N  N   . PRO A 1 211 ? 28.218  30.690 9.361   1.00 24.97  ? 210 PRO A N   1 
ATOM   1716 C  CA  . PRO A 1 211 ? 27.064  30.313 8.539   1.00 28.28  ? 210 PRO A CA  1 
ATOM   1717 C  C   . PRO A 1 211 ? 25.987  31.390 8.361   1.00 26.26  ? 210 PRO A C   1 
ATOM   1718 O  O   . PRO A 1 211 ? 26.177  32.526 8.785   1.00 23.91  ? 210 PRO A O   1 
ATOM   1719 C  CB  . PRO A 1 211 ? 26.495  29.089 9.268   1.00 31.85  ? 210 PRO A CB  1 
ATOM   1720 C  CG  . PRO A 1 211 ? 26.940  29.244 10.693  1.00 34.57  ? 210 PRO A CG  1 
ATOM   1721 C  CD  . PRO A 1 211 ? 28.281  29.944 10.622  1.00 28.83  ? 210 PRO A CD  1 
ATOM   1722 N  N   . ALA A 1 212 ? 24.873  31.039 7.692   1.00 21.17  ? 211 ALA A N   1 
ATOM   1723 C  CA  . ALA A 1 212 ? 23.864  32.029 7.245   1.00 22.47  ? 211 ALA A CA  1 
ATOM   1724 C  C   . ALA A 1 212 ? 23.076  32.619 8.415   1.00 21.20  ? 211 ALA A C   1 
ATOM   1725 O  O   . ALA A 1 212 ? 22.630  33.771 8.307   1.00 22.19  ? 211 ALA A O   1 
ATOM   1726 C  CB  . ALA A 1 212 ? 22.938  31.401 6.212   1.00 25.09  ? 211 ALA A CB  1 
ATOM   1727 N  N   . GLU A 1 213 ? 22.866  31.854 9.491   1.00 21.73  ? 212 GLU A N   1 
ATOM   1728 C  CA  . GLU A 1 213 ? 22.061  32.289 10.656  1.00 24.44  ? 212 GLU A CA  1 
ATOM   1729 C  C   . GLU A 1 213 ? 22.659  33.588 11.192  1.00 22.82  ? 212 GLU A C   1 
ATOM   1730 O  O   . GLU A 1 213 ? 23.868  33.633 11.472  1.00 22.69  ? 212 GLU A O   1 
ATOM   1731 C  CB  . GLU A 1 213 ? 22.079  31.234 11.761  1.00 22.09  ? 212 GLU A CB  1 
ATOM   1732 C  CG  . GLU A 1 213 ? 21.309  31.604 13.006  1.00 27.54  ? 212 GLU A CG  1 
ATOM   1733 C  CD  . GLU A 1 213 ? 19.847  31.939 12.763  1.00 37.84  ? 212 GLU A CD  1 
ATOM   1734 O  OE1 . GLU A 1 213 ? 19.205  31.254 11.940  1.00 50.03  ? 212 GLU A OE1 1 
ATOM   1735 O  OE2 . GLU A 1 213 ? 19.358  32.893 13.386  1.00 46.53  ? 212 GLU A OE2 1 
ATOM   1736 N  N   . ILE A 1 214 ? 21.828  34.596 11.346  1.00 22.52  ? 213 ILE A N   1 
ATOM   1737 C  CA  . ILE A 1 214 ? 22.233  35.914 11.885  1.00 23.71  ? 213 ILE A CA  1 
ATOM   1738 C  C   . ILE A 1 214 ? 20.989  36.632 12.408  1.00 29.39  ? 213 ILE A C   1 
ATOM   1739 O  O   . ILE A 1 214 ? 19.880  36.367 11.895  1.00 24.72  ? 213 ILE A O   1 
ATOM   1740 C  CB  . ILE A 1 214 ? 22.951  36.734 10.802  1.00 22.58  ? 213 ILE A CB  1 
ATOM   1741 C  CG1 . ILE A 1 214 ? 23.778  37.871 11.391  1.00 22.35  ? 213 ILE A CG1 1 
ATOM   1742 C  CG2 . ILE A 1 214 ? 22.011  37.275 9.748   1.00 23.08  ? 213 ILE A CG2 1 
ATOM   1743 C  CD1 . ILE A 1 214 ? 24.710  38.504 10.358  1.00 23.15  ? 213 ILE A CD1 1 
ATOM   1744 N  N   . THR A 1 215 ? 21.161  37.488 13.409  1.00 22.43  ? 214 THR A N   1 
ATOM   1745 C  CA  . THR A 1 215 ? 20.124  38.462 13.821  1.00 23.01  ? 214 THR A CA  1 
ATOM   1746 C  C   . THR A 1 215 ? 20.647  39.894 13.708  1.00 26.61  ? 214 THR A C   1 
ATOM   1747 O  O   . THR A 1 215 ? 21.700  40.191 14.284  1.00 24.07  ? 214 THR A O   1 
ATOM   1748 C  CB  . THR A 1 215 ? 19.578  38.088 15.200  1.00 27.45  ? 214 THR A CB  1 
ATOM   1749 O  OG1 . THR A 1 215 ? 19.276  36.694 15.157  1.00 25.94  ? 214 THR A OG1 1 
ATOM   1750 C  CG2 . THR A 1 215 ? 18.347  38.895 15.543  1.00 29.05  ? 214 THR A CG2 1 
ATOM   1751 N  N   . LEU A 1 216 ? 19.936  40.729 12.944  1.00 22.35  ? 215 LEU A N   1 
ATOM   1752 C  CA  . LEU A 1 216 ? 20.179  42.173 12.797  1.00 20.96  ? 215 LEU A CA  1 
ATOM   1753 C  C   . LEU A 1 216 ? 18.947  42.880 13.356  1.00 29.18  ? 215 LEU A C   1 
ATOM   1754 O  O   . LEU A 1 216 ? 17.847  42.603 12.872  1.00 30.69  ? 215 LEU A O   1 
ATOM   1755 C  CB  . LEU A 1 216 ? 20.256  42.588 11.327  1.00 25.64  ? 215 LEU A CB  1 
ATOM   1756 C  CG  . LEU A 1 216 ? 21.535  42.354 10.558  1.00 33.66  ? 215 LEU A CG  1 
ATOM   1757 C  CD1 . LEU A 1 216 ? 21.388  43.026 9.192   1.00 27.25  ? 215 LEU A CD1 1 
ATOM   1758 C  CD2 . LEU A 1 216 ? 22.728  42.920 11.306  1.00 40.94  ? 215 LEU A CD2 1 
ATOM   1759 N  N   . THR A 1 217 ? 19.123  43.802 14.273  1.00 25.58  ? 216 THR A N   1 
ATOM   1760 C  CA  . THR A 1 217 ? 18.007  44.586 14.835  1.00 27.43  ? 216 THR A CA  1 
ATOM   1761 C  C   . THR A 1 217 ? 18.485  46.031 14.958  1.00 29.50  ? 216 THR A C   1 
ATOM   1762 O  O   . THR A 1 217 ? 19.702  46.237 15.158  1.00 27.94  ? 216 THR A O   1 
ATOM   1763 C  CB  . THR A 1 217 ? 17.553  44.002 16.180  1.00 28.99  ? 216 THR A CB  1 
ATOM   1764 O  OG1 . THR A 1 217 ? 18.707  43.903 17.002  1.00 30.85  ? 216 THR A OG1 1 
ATOM   1765 C  CG2 . THR A 1 217 ? 16.917  42.625 16.063  1.00 38.58  ? 216 THR A CG2 1 
ATOM   1766 N  N   . TRP A 1 218 ? 17.552  46.974 14.834  1.00 24.51  ? 217 TRP A N   1 
ATOM   1767 C  CA  . TRP A 1 218 ? 17.754  48.383 15.245  1.00 22.07  ? 217 TRP A CA  1 
ATOM   1768 C  C   . TRP A 1 218 ? 17.087  48.580 16.610  1.00 28.56  ? 217 TRP A C   1 
ATOM   1769 O  O   . TRP A 1 218 ? 16.003  48.047 16.854  1.00 26.14  ? 217 TRP A O   1 
ATOM   1770 C  CB  . TRP A 1 218 ? 17.208  49.350 14.197  1.00 27.74  ? 217 TRP A CB  1 
ATOM   1771 C  CG  . TRP A 1 218 ? 18.131  49.595 13.044  1.00 26.38  ? 217 TRP A CG  1 
ATOM   1772 C  CD1 . TRP A 1 218 ? 18.073  49.015 11.803  1.00 27.95  ? 217 TRP A CD1 1 
ATOM   1773 C  CD2 . TRP A 1 218 ? 19.284  50.456 13.025  1.00 27.64  ? 217 TRP A CD2 1 
ATOM   1774 N  NE1 . TRP A 1 218 ? 19.069  49.505 10.998  1.00 25.21  ? 217 TRP A NE1 1 
ATOM   1775 C  CE2 . TRP A 1 218 ? 19.832  50.387 11.716  1.00 25.35  ? 217 TRP A CE2 1 
ATOM   1776 C  CE3 . TRP A 1 218 ? 19.878  51.308 13.960  1.00 28.54  ? 217 TRP A CE3 1 
ATOM   1777 C  CZ2 . TRP A 1 218 ? 20.957  51.117 11.345  1.00 27.66  ? 217 TRP A CZ2 1 
ATOM   1778 C  CZ3 . TRP A 1 218 ? 20.989  52.026 13.588  1.00 28.98  ? 217 TRP A CZ3 1 
ATOM   1779 C  CH2 . TRP A 1 218 ? 21.514  51.942 12.299  1.00 30.34  ? 217 TRP A CH2 1 
ATOM   1780 N  N   . GLN A 1 219 ? 17.731  49.328 17.469  1.00 30.80  ? 218 GLN A N   1 
ATOM   1781 C  CA  . GLN A 1 219 ? 17.104  49.819 18.708  1.00 32.23  ? 218 GLN A CA  1 
ATOM   1782 C  C   . GLN A 1 219 ? 17.116  51.345 18.679  1.00 36.91  ? 218 GLN A C   1 
ATOM   1783 O  O   . GLN A 1 219 ? 18.044  51.948 18.085  1.00 32.68  ? 218 GLN A O   1 
ATOM   1784 C  CB  . GLN A 1 219 ? 17.870  49.270 19.909  1.00 28.20  ? 218 GLN A CB  1 
ATOM   1785 C  CG  . GLN A 1 219 ? 17.673  47.781 20.117  1.00 30.67  ? 218 GLN A CG  1 
ATOM   1786 C  CD  . GLN A 1 219 ? 18.536  47.247 21.227  1.00 36.20  ? 218 GLN A CD  1 
ATOM   1787 O  OE1 . GLN A 1 219 ? 18.984  48.012 22.075  1.00 36.23  ? 218 GLN A OE1 1 
ATOM   1788 N  NE2 . GLN A 1 219 ? 18.794  45.944 21.199  1.00 31.93  ? 218 GLN A NE2 1 
ATOM   1789 N  N   . ARG A 1 220 ? 16.103  51.942 19.311  1.00 41.39  ? 219 ARG A N   1 
ATOM   1790 C  CA  . ARG A 1 220 ? 16.055  53.394 19.600  1.00 36.36  ? 219 ARG A CA  1 
ATOM   1791 C  C   . ARG A 1 220 ? 16.123  53.523 21.122  1.00 35.08  ? 219 ARG A C   1 
ATOM   1792 O  O   . ARG A 1 220 ? 15.220  52.974 21.808  1.00 37.16  ? 219 ARG A O   1 
ATOM   1793 C  CB  . ARG A 1 220 ? 14.803  54.018 18.971  1.00 41.31  ? 219 ARG A CB  1 
ATOM   1794 C  CG  . ARG A 1 220 ? 14.713  55.527 19.174  1.00 45.02  ? 219 ARG A CG  1 
ATOM   1795 C  CD  . ARG A 1 220 ? 13.293  56.047 19.001  1.00 48.27  ? 219 ARG A CD  1 
ATOM   1796 N  NE  . ARG A 1 220 ? 13.244  57.508 19.079  1.00 64.48  ? 219 ARG A NE  1 
ATOM   1797 C  CZ  . ARG A 1 220 ? 13.300  58.248 20.194  1.00 60.17  ? 219 ARG A CZ  1 
ATOM   1798 N  NH1 . ARG A 1 220 ? 13.411  57.694 21.399  1.00 53.79  ? 219 ARG A NH1 1 
ATOM   1799 N  NH2 . ARG A 1 220 ? 13.244  59.564 20.088  1.00 54.76  ? 219 ARG A NH2 1 
ATOM   1800 N  N   . ASP A 1 221 ? 17.188  54.156 21.613  1.00 39.77  ? 220 ASP A N   1 
ATOM   1801 C  CA  . ASP A 1 221 ? 17.564  54.201 23.054  1.00 57.96  ? 220 ASP A CA  1 
ATOM   1802 C  C   . ASP A 1 221 ? 17.258  52.845 23.703  1.00 46.38  ? 220 ASP A C   1 
ATOM   1803 O  O   . ASP A 1 221 ? 16.578  52.811 24.730  1.00 38.59  ? 220 ASP A O   1 
ATOM   1804 C  CB  . ASP A 1 221 ? 16.884  55.375 23.767  1.00 45.37  ? 220 ASP A CB  1 
ATOM   1805 C  CG  . ASP A 1 221 ? 17.336  56.732 23.255  1.00 56.75  ? 220 ASP A CG  1 
ATOM   1806 O  OD1 . ASP A 1 221 ? 18.568  56.939 23.099  1.00 46.98  ? 220 ASP A OD1 1 
ATOM   1807 O  OD2 . ASP A 1 221 ? 16.452  57.564 23.004  1.00 57.81  ? 220 ASP A OD2 1 
ATOM   1808 N  N   . GLY A 1 222 ? 17.752  51.752 23.123  1.00 42.81  ? 221 GLY A N   1 
ATOM   1809 C  CA  . GLY A 1 222 ? 17.662  50.412 23.733  1.00 47.44  ? 221 GLY A CA  1 
ATOM   1810 C  C   . GLY A 1 222 ? 16.304  49.746 23.550  1.00 35.31  ? 221 GLY A C   1 
ATOM   1811 O  O   . GLY A 1 222 ? 16.175  48.583 23.951  1.00 40.88  ? 221 GLY A O   1 
ATOM   1812 N  N   . GLU A 1 223 ? 15.328  50.402 22.922  1.00 28.58  ? 222 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 223 ? 13.971  49.835 22.690  1.00 36.65  ? 222 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 223 ? 13.903  49.250 21.278  1.00 48.66  ? 222 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 223 ? 14.302  49.951 20.308  1.00 34.03  ? 222 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 223 ? 12.882  50.892 22.869  1.00 42.44  ? 222 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 223 ? 12.914  51.568 24.238  1.00 47.04  ? 222 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 223 ? 12.723  50.657 25.451  1.00 55.10  ? 222 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 223 ? 11.934  49.670 25.366  1.00 44.73  ? 222 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 223 ? 13.377  50.936 26.485  1.00 45.64  ? 222 GLU A OE2 1 
ATOM   1821 N  N   . ASP A 1 224 ? 13.383  48.031 21.155  1.00 43.40  ? 223 ASP A N   1 
ATOM   1822 C  CA  . ASP A 1 224 ? 13.421  47.321 19.856  1.00 52.11  ? 223 ASP A CA  1 
ATOM   1823 C  C   . ASP A 1 224 ? 12.465  48.019 18.889  1.00 51.97  ? 223 ASP A C   1 
ATOM   1824 O  O   . ASP A 1 224 ? 11.484  48.616 19.357  1.00 41.67  ? 223 ASP A O   1 
ATOM   1825 C  CB  . ASP A 1 224 ? 13.195  45.816 19.981  1.00 63.75  ? 223 ASP A CB  1 
ATOM   1826 C  CG  . ASP A 1 224 ? 14.205  45.096 19.096  1.00 78.43  ? 223 ASP A CG  1 
ATOM   1827 O  OD1 . ASP A 1 224 ? 14.034  45.135 17.847  1.00 50.90  ? 223 ASP A OD1 1 
ATOM   1828 O  OD2 . ASP A 1 224 ? 15.221  44.620 19.648  1.00 71.20  ? 223 ASP A OD2 1 
ATOM   1829 N  N   . GLN A 1 225 ? 12.829  48.019 17.600  1.00 47.73  ? 224 GLN A N   1 
ATOM   1830 C  CA  . GLN A 1 225 ? 12.142  48.753 16.513  1.00 44.03  ? 224 GLN A CA  1 
ATOM   1831 C  C   . GLN A 1 225 ? 11.623  47.765 15.472  1.00 43.50  ? 224 GLN A C   1 
ATOM   1832 O  O   . GLN A 1 225 ? 11.597  48.134 14.290  1.00 40.78  ? 224 GLN A O   1 
ATOM   1833 C  CB  . GLN A 1 225 ? 13.117  49.715 15.838  1.00 40.76  ? 224 GLN A CB  1 
ATOM   1834 C  CG  . GLN A 1 225 ? 13.676  50.775 16.766  1.00 49.98  ? 224 GLN A CG  1 
ATOM   1835 C  CD  . GLN A 1 225 ? 12.569  51.667 17.260  1.00 56.65  ? 224 GLN A CD  1 
ATOM   1836 O  OE1 . GLN A 1 225 ? 11.950  52.388 16.488  1.00 55.59  ? 224 GLN A OE1 1 
ATOM   1837 N  NE2 . GLN A 1 225 ? 12.278  51.576 18.547  1.00 57.60  ? 224 GLN A NE2 1 
ATOM   1838 N  N   . THR A 1 226 ? 11.204  46.573 15.893  1.00 52.85  ? 225 THR A N   1 
ATOM   1839 C  CA  . THR A 1 226 ? 10.854  45.448 14.981  1.00 65.49  ? 225 THR A CA  1 
ATOM   1840 C  C   . THR A 1 226 ? 9.841   45.933 13.927  1.00 55.84  ? 225 THR A C   1 
ATOM   1841 O  O   . THR A 1 226 ? 10.088  45.714 12.720  1.00 46.84  ? 225 THR A O   1 
ATOM   1842 C  CB  . THR A 1 226 ? 10.431  44.214 15.795  1.00 66.89  ? 225 THR A CB  1 
ATOM   1843 O  OG1 . THR A 1 226 ? 11.431  43.205 15.624  1.00 85.71  ? 225 THR A OG1 1 
ATOM   1844 C  CG2 . THR A 1 226 ? 9.076   43.667 15.404  1.00 72.64  ? 225 THR A CG2 1 
ATOM   1845 N  N   . GLN A 1 227 ? 8.761   46.601 14.347  1.00 42.02  ? 226 GLN A N   1 
ATOM   1846 C  CA  . GLN A 1 227 ? 7.661   47.012 13.437  1.00 52.48  ? 226 GLN A CA  1 
ATOM   1847 C  C   . GLN A 1 227 ? 8.149   48.065 12.433  1.00 47.08  ? 226 GLN A C   1 
ATOM   1848 O  O   . GLN A 1 227 ? 7.534   48.157 11.388  1.00 51.33  ? 226 GLN A O   1 
ATOM   1849 C  CB  . GLN A 1 227 ? 6.454   47.530 14.232  1.00 63.00  ? 226 GLN A CB  1 
ATOM   1850 C  CG  . GLN A 1 227 ? 5.781   46.463 15.094  1.00 77.57  ? 226 GLN A CG  1 
ATOM   1851 C  CD  . GLN A 1 227 ? 5.676   45.115 14.411  1.00 81.48  ? 226 GLN A CD  1 
ATOM   1852 O  OE1 . GLN A 1 227 ? 5.323   45.013 13.240  1.00 60.52  ? 226 GLN A OE1 1 
ATOM   1853 N  NE2 . GLN A 1 227 ? 6.002   44.054 15.134  1.00 68.64  ? 226 GLN A NE2 1 
ATOM   1854 N  N   . ASP A 1 228 ? 9.191   48.842 12.739  1.00 41.25  ? 227 ASP A N   1 
ATOM   1855 C  CA  . ASP A 1 228 ? 9.654   49.953 11.857  1.00 45.26  ? 227 ASP A CA  1 
ATOM   1856 C  C   . ASP A 1 228 ? 10.985  49.608 11.176  1.00 37.90  ? 227 ASP A C   1 
ATOM   1857 O  O   . ASP A 1 228 ? 11.610  50.521 10.603  1.00 39.73  ? 227 ASP A O   1 
ATOM   1858 C  CB  . ASP A 1 228 ? 9.803   51.253 12.641  1.00 57.11  ? 227 ASP A CB  1 
ATOM   1859 C  CG  . ASP A 1 228 ? 8.490   51.673 13.266  1.00 69.44  ? 227 ASP A CG  1 
ATOM   1860 O  OD1 . ASP A 1 228 ? 7.519   51.807 12.503  1.00 52.84  ? 227 ASP A OD1 1 
ATOM   1861 O  OD2 . ASP A 1 228 ? 8.444   51.802 14.507  1.00 64.84  ? 227 ASP A OD2 1 
ATOM   1862 N  N   . THR A 1 229 ? 11.418  48.355 11.239  1.00 39.25  ? 228 THR A N   1 
ATOM   1863 C  CA  . THR A 1 229 ? 12.653  47.910 10.548  1.00 40.53  ? 228 THR A CA  1 
ATOM   1864 C  C   . THR A 1 229 ? 12.283  47.208 9.236   1.00 35.40  ? 228 THR A C   1 
ATOM   1865 O  O   . THR A 1 229 ? 11.492  46.279 9.275   1.00 40.05  ? 228 THR A O   1 
ATOM   1866 C  CB  . THR A 1 229 ? 13.490  47.023 11.464  1.00 41.50  ? 228 THR A CB  1 
ATOM   1867 O  OG1 . THR A 1 229 ? 13.761  47.764 12.659  1.00 34.74  ? 228 THR A OG1 1 
ATOM   1868 C  CG2 . THR A 1 229 ? 14.775  46.590 10.789  1.00 36.89  ? 228 THR A CG2 1 
ATOM   1869 N  N   . GLU A 1 230 ? 12.960  47.594 8.153   1.00 37.40  ? 229 GLU A N   1 
ATOM   1870 C  CA  . GLU A 1 230 ? 12.917  46.856 6.867   1.00 33.46  ? 229 GLU A CA  1 
ATOM   1871 C  C   . GLU A 1 230 ? 14.122  45.908 6.895   1.00 36.16  ? 229 GLU A C   1 
ATOM   1872 O  O   . GLU A 1 230 ? 15.227  46.382 7.037   1.00 31.80  ? 229 GLU A O   1 
ATOM   1873 C  CB  . GLU A 1 230 ? 13.024  47.735 5.633   1.00 36.72  ? 229 GLU A CB  1 
ATOM   1874 C  CG  . GLU A 1 230 ? 13.063  46.875 4.394   1.00 38.72  ? 229 GLU A CG  1 
ATOM   1875 C  CD  . GLU A 1 230 ? 13.014  47.599 3.071   1.00 42.30  ? 229 GLU A CD  1 
ATOM   1876 O  OE1 . GLU A 1 230 ? 13.069  48.795 3.095   1.00 48.52  ? 229 GLU A OE1 1 
ATOM   1877 O  OE2 . GLU A 1 230 ? 12.896  46.946 2.049   1.00 43.83  ? 229 GLU A OE2 1 
ATOM   1878 N  N   . LEU A 1 231 ? 13.865  44.622 6.737   1.00 29.91  ? 230 LEU A N   1 
ATOM   1879 C  CA  . LEU A 1 231 ? 14.849  43.523 6.895   1.00 31.96  ? 230 LEU A CA  1 
ATOM   1880 C  C   . LEU A 1 231 ? 14.807  42.743 5.591   1.00 39.95  ? 230 LEU A C   1 
ATOM   1881 O  O   . LEU A 1 231 ? 13.704  42.317 5.254   1.00 43.12  ? 230 LEU A O   1 
ATOM   1882 C  CB  . LEU A 1 231 ? 14.370  42.706 8.098   1.00 40.45  ? 230 LEU A CB  1 
ATOM   1883 C  CG  . LEU A 1 231 ? 15.401  41.829 8.778   1.00 51.82  ? 230 LEU A CG  1 
ATOM   1884 C  CD1 . LEU A 1 231 ? 16.415  42.687 9.508   1.00 50.89  ? 230 LEU A CD1 1 
ATOM   1885 C  CD2 . LEU A 1 231 ? 14.729  40.855 9.737   1.00 51.84  ? 230 LEU A CD2 1 
ATOM   1886 N  N   . VAL A 1 232 ? 15.914  42.620 4.851   1.00 27.83  ? 231 VAL A N   1 
ATOM   1887 C  CA  . VAL A 1 232 ? 15.920  41.778 3.617   1.00 24.58  ? 231 VAL A CA  1 
ATOM   1888 C  C   . VAL A 1 232 ? 16.235  40.345 4.021   1.00 27.93  ? 231 VAL A C   1 
ATOM   1889 O  O   . VAL A 1 232 ? 16.912  40.117 5.039   1.00 25.00  ? 231 VAL A O   1 
ATOM   1890 C  CB  . VAL A 1 232 ? 16.864  42.282 2.508   1.00 26.51  ? 231 VAL A CB  1 
ATOM   1891 C  CG1 . VAL A 1 232 ? 16.398  43.617 1.934   1.00 27.40  ? 231 VAL A CG1 1 
ATOM   1892 C  CG2 . VAL A 1 232 ? 18.323  42.336 2.963   1.00 23.12  ? 231 VAL A CG2 1 
ATOM   1893 N  N   . GLU A 1 233 ? 15.730  39.407 3.257   1.00 21.12  ? 232 GLU A N   1 
ATOM   1894 C  CA  . GLU A 1 233 ? 16.067  37.979 3.434   1.00 23.88  ? 232 GLU A CA  1 
ATOM   1895 C  C   . GLU A 1 233 ? 17.588  37.854 3.355   1.00 22.25  ? 232 GLU A C   1 
ATOM   1896 O  O   . GLU A 1 233 ? 18.195  38.436 2.428   1.00 21.98  ? 232 GLU A O   1 
ATOM   1897 C  CB  . GLU A 1 233 ? 15.522  37.084 2.318   1.00 27.32  ? 232 GLU A CB  1 
ATOM   1898 C  CG  . GLU A 1 233 ? 14.033  36.772 2.350   1.00 49.47  ? 232 GLU A CG  1 
ATOM   1899 C  CD  . GLU A 1 233 ? 13.573  35.628 1.416   1.00 60.42  ? 232 GLU A CD  1 
ATOM   1900 O  OE1 . GLU A 1 233 ? 14.362  35.136 0.475   1.00 29.96  ? 232 GLU A OE1 1 
ATOM   1901 O  OE2 . GLU A 1 233 ? 12.405  35.198 1.615   1.00 53.73  ? 232 GLU A OE2 1 
ATOM   1902 N  N   . THR A 1 234 ? 18.162  36.992 4.175   1.00 18.94  ? 233 THR A N   1 
ATOM   1903 C  CA  . THR A 1 234 ? 19.576  36.612 4.073   1.00 21.21  ? 233 THR A CA  1 
ATOM   1904 C  C   . THR A 1 234 ? 19.834  36.025 2.694   1.00 23.31  ? 233 THR A C   1 
ATOM   1905 O  O   . THR A 1 234 ? 19.020  35.185 2.196   1.00 23.04  ? 233 THR A O   1 
ATOM   1906 C  CB  . THR A 1 234 ? 19.926  35.656 5.198   1.00 21.44  ? 233 THR A CB  1 
ATOM   1907 O  OG1 . THR A 1 234 ? 19.591  36.373 6.392   1.00 20.28  ? 233 THR A OG1 1 
ATOM   1908 C  CG2 . THR A 1 234 ? 21.383  35.263 5.182   1.00 24.55  ? 233 THR A CG2 1 
ATOM   1909 N  N   . ARG A 1 235 ? 20.896  36.461 2.060   1.00 22.84  ? 234 ARG A N   1 
ATOM   1910 C  CA  . ARG A 1 235 ? 21.124  36.177 0.624   1.00 20.70  ? 234 ARG A CA  1 
ATOM   1911 C  C   . ARG A 1 235 ? 22.558  35.731 0.434   1.00 27.79  ? 234 ARG A C   1 
ATOM   1912 O  O   . ARG A 1 235 ? 23.455  36.207 1.100   1.00 23.70  ? 234 ARG A O   1 
ATOM   1913 C  CB  . ARG A 1 235 ? 20.834  37.392 -0.245  1.00 19.02  ? 234 ARG A CB  1 
ATOM   1914 C  CG  . ARG A 1 235 ? 21.739  38.599 0.005   1.00 32.46  ? 234 ARG A CG  1 
ATOM   1915 C  CD  . ARG A 1 235 ? 21.104  39.925 -0.333  1.00 23.66  ? 234 ARG A CD  1 
ATOM   1916 N  NE  . ARG A 1 235 ? 22.089  40.981 -0.483  1.00 25.40  ? 234 ARG A NE  1 
ATOM   1917 C  CZ  . ARG A 1 235 ? 21.828  42.239 -0.735  1.00 22.99  ? 234 ARG A CZ  1 
ATOM   1918 N  NH1 . ARG A 1 235 ? 20.584  42.626 -0.944  1.00 24.61  ? 234 ARG A NH1 1 
ATOM   1919 N  NH2 . ARG A 1 235 ? 22.833  43.110 -0.848  1.00 22.14  ? 234 ARG A NH2 1 
ATOM   1920 N  N   . PRO A 1 236 ? 22.811  34.780 -0.473  1.00 23.84  ? 235 PRO A N   1 
ATOM   1921 C  CA  . PRO A 1 236 ? 24.164  34.260 -0.670  1.00 20.16  ? 235 PRO A CA  1 
ATOM   1922 C  C   . PRO A 1 236 ? 25.029  35.227 -1.485  1.00 24.32  ? 235 PRO A C   1 
ATOM   1923 O  O   . PRO A 1 236 ? 24.533  35.823 -2.444  1.00 23.05  ? 235 PRO A O   1 
ATOM   1924 C  CB  . PRO A 1 236 ? 23.949  32.991 -1.504  1.00 21.29  ? 235 PRO A CB  1 
ATOM   1925 C  CG  . PRO A 1 236 ? 22.651  33.286 -2.260  1.00 23.66  ? 235 PRO A CG  1 
ATOM   1926 C  CD  . PRO A 1 236 ? 21.789  34.085 -1.295  1.00 27.09  ? 235 PRO A CD  1 
ATOM   1927 N  N   . ALA A 1 237 ? 26.316  35.336 -1.156  1.00 24.62  ? 236 ALA A N   1 
ATOM   1928 C  CA  . ALA A 1 237 ? 27.238  36.264 -1.869  1.00 24.79  ? 236 ALA A CA  1 
ATOM   1929 C  C   . ALA A 1 237 ? 27.826  35.569 -3.097  1.00 22.49  ? 236 ALA A C   1 
ATOM   1930 O  O   . ALA A 1 237 ? 28.354  36.311 -3.960  1.00 22.80  ? 236 ALA A O   1 
ATOM   1931 C  CB  . ALA A 1 237 ? 28.344  36.794 -0.969  1.00 24.45  ? 236 ALA A CB  1 
ATOM   1932 N  N   . GLY A 1 238 ? 27.773  34.226 -3.119  1.00 23.76  ? 237 GLY A N   1 
ATOM   1933 C  CA  . GLY A 1 238 ? 28.276  33.359 -4.200  1.00 24.31  ? 237 GLY A CA  1 
ATOM   1934 C  C   . GLY A 1 238 ? 29.656  32.815 -3.905  1.00 27.51  ? 237 GLY A C   1 
ATOM   1935 O  O   . GLY A 1 238 ? 30.150  32.023 -4.710  1.00 28.30  ? 237 GLY A O   1 
ATOM   1936 N  N   . ASP A 1 239 ? 30.273  33.230 -2.781  1.00 27.87  ? 238 ASP A N   1 
ATOM   1937 C  CA  . ASP A 1 239 ? 31.620  32.767 -2.351  1.00 27.18  ? 238 ASP A CA  1 
ATOM   1938 C  C   . ASP A 1 239 ? 31.507  31.992 -1.041  1.00 33.27  ? 238 ASP A C   1 
ATOM   1939 O  O   . ASP A 1 239 ? 32.444  32.063 -0.252  1.00 28.56  ? 238 ASP A O   1 
ATOM   1940 C  CB  . ASP A 1 239 ? 32.572  33.948 -2.165  1.00 29.46  ? 238 ASP A CB  1 
ATOM   1941 C  CG  . ASP A 1 239 ? 32.107  34.954 -1.121  1.00 26.09  ? 238 ASP A CG  1 
ATOM   1942 O  OD1 . ASP A 1 239 ? 30.981  34.809 -0.574  1.00 26.46  ? 238 ASP A OD1 1 
ATOM   1943 O  OD2 . ASP A 1 239 ? 32.823  35.920 -0.930  1.00 29.84  ? 238 ASP A OD2 1 
ATOM   1944 N  N   . ARG A 1 240 ? 30.374  31.335 -0.812  1.00 26.65  ? 239 ARG A N   1 
ATOM   1945 C  CA  . ARG A 1 240 ? 30.012  30.572 0.416   1.00 29.00  ? 239 ARG A CA  1 
ATOM   1946 C  C   . ARG A 1 240 ? 30.013  31.500 1.640   1.00 24.95  ? 239 ARG A C   1 
ATOM   1947 O  O   . ARG A 1 240 ? 30.456  31.049 2.725   1.00 26.76  ? 239 ARG A O   1 
ATOM   1948 C  CB  . ARG A 1 240 ? 30.925  29.352 0.612   1.00 33.59  ? 239 ARG A CB  1 
ATOM   1949 C  CG  . ARG A 1 240 ? 31.025  28.444 -0.611  1.00 48.32  ? 239 ARG A CG  1 
ATOM   1950 C  CD  . ARG A 1 240 ? 31.900  27.222 -0.363  1.00 61.04  ? 239 ARG A CD  1 
ATOM   1951 N  NE  . ARG A 1 240 ? 31.715  26.195 -1.380  1.00 46.39  ? 239 ARG A NE  1 
ATOM   1952 C  CZ  . ARG A 1 240 ? 32.509  25.987 -2.434  1.00 70.08  ? 239 ARG A CZ  1 
ATOM   1953 N  NH1 . ARG A 1 240 ? 33.604  26.718 -2.614  1.00 54.88  ? 239 ARG A NH1 1 
ATOM   1954 N  NH2 . ARG A 1 240 ? 32.201  25.027 -3.298  1.00 44.19  ? 239 ARG A NH2 1 
ATOM   1955 N  N   . THR A 1 241 ? 29.659  32.764 1.458   1.00 27.07  ? 240 THR A N   1 
ATOM   1956 C  CA  . THR A 1 241 ? 29.284  33.699 2.545   1.00 24.20  ? 240 THR A CA  1 
ATOM   1957 C  C   . THR A 1 241 ? 27.918  34.291 2.233   1.00 26.42  ? 240 THR A C   1 
ATOM   1958 O  O   . THR A 1 241 ? 27.411  34.074 1.122   1.00 22.19  ? 240 THR A O   1 
ATOM   1959 C  CB  . THR A 1 241 ? 30.306  34.798 2.795   1.00 23.42  ? 240 THR A CB  1 
ATOM   1960 O  OG1 . THR A 1 241 ? 30.235  35.736 1.728   1.00 26.31  ? 240 THR A OG1 1 
ATOM   1961 C  CG2 . THR A 1 241 ? 31.717  34.261 2.981   1.00 28.74  ? 240 THR A CG2 1 
ATOM   1962 N  N   . PHE A 1 242 ? 27.356  34.989 3.206   1.00 22.54  ? 241 PHE A N   1 
ATOM   1963 C  CA  . PHE A 1 242 ? 25.964  35.491 3.188   1.00 23.56  ? 241 PHE A CA  1 
ATOM   1964 C  C   . PHE A 1 242 ? 25.977  36.965 3.490   1.00 22.36  ? 241 PHE A C   1 
ATOM   1965 O  O   . PHE A 1 242 ? 26.958  37.493 3.956   1.00 23.27  ? 241 PHE A O   1 
ATOM   1966 C  CB  . PHE A 1 242 ? 25.083  34.680 4.128   1.00 22.49  ? 241 PHE A CB  1 
ATOM   1967 C  CG  . PHE A 1 242 ? 24.981  33.240 3.706   1.00 22.03  ? 241 PHE A CG  1 
ATOM   1968 C  CD1 . PHE A 1 242 ? 25.887  32.298 4.158   1.00 20.48  ? 241 PHE A CD1 1 
ATOM   1969 C  CD2 . PHE A 1 242 ? 24.003  32.838 2.818   1.00 24.83  ? 241 PHE A CD2 1 
ATOM   1970 C  CE1 . PHE A 1 242 ? 25.802  30.968 3.774   1.00 26.46  ? 241 PHE A CE1 1 
ATOM   1971 C  CE2 . PHE A 1 242 ? 23.930  31.517 2.406   1.00 23.86  ? 241 PHE A CE2 1 
ATOM   1972 C  CZ  . PHE A 1 242 ? 24.835  30.587 2.866   1.00 29.40  ? 241 PHE A CZ  1 
ATOM   1973 N  N   . GLN A 1 243 ? 24.870  37.599 3.198   1.00 20.47  ? 242 GLN A N   1 
ATOM   1974 C  CA  . GLN A 1 243 ? 24.689  39.046 3.377   1.00 20.17  ? 242 GLN A CA  1 
ATOM   1975 C  C   . GLN A 1 243 ? 23.297  39.290 3.931   1.00 22.71  ? 242 GLN A C   1 
ATOM   1976 O  O   . GLN A 1 243 ? 22.341  38.482 3.646   1.00 21.19  ? 242 GLN A O   1 
ATOM   1977 C  CB  . GLN A 1 243 ? 24.758  39.788 2.047   1.00 22.39  ? 242 GLN A CB  1 
ATOM   1978 C  CG  . GLN A 1 243 ? 25.975  39.450 1.194   1.00 24.64  ? 242 GLN A CG  1 
ATOM   1979 C  CD  . GLN A 1 243 ? 25.999  40.280 -0.083  1.00 22.76  ? 242 GLN A CD  1 
ATOM   1980 O  OE1 . GLN A 1 243 ? 25.031  40.965 -0.445  1.00 22.09  ? 242 GLN A OE1 1 
ATOM   1981 N  NE2 . GLN A 1 243 ? 27.137  40.276 -0.751  1.00 23.32  ? 242 GLN A NE2 1 
ATOM   1982 N  N   . LYS A 1 244 ? 23.168  40.382 4.665   1.00 22.99  ? 243 LYS A N   1 
ATOM   1983 C  CA  . LYS A 1 244 ? 21.856  40.840 5.163   1.00 19.57  ? 243 LYS A CA  1 
ATOM   1984 C  C   . LYS A 1 244 ? 21.972  42.313 5.459   1.00 21.37  ? 243 LYS A C   1 
ATOM   1985 O  O   . LYS A 1 244 ? 23.098  42.789 5.747   1.00 20.29  ? 243 LYS A O   1 
ATOM   1986 C  CB  . LYS A 1 244 ? 21.437  40.032 6.386   1.00 22.58  ? 243 LYS A CB  1 
ATOM   1987 C  CG  . LYS A 1 244 ? 19.929  40.054 6.657   1.00 23.89  ? 243 LYS A CG  1 
ATOM   1988 C  CD  . LYS A 1 244 ? 19.531  39.281 7.906   1.00 21.44  ? 243 LYS A CD  1 
ATOM   1989 C  CE  . LYS A 1 244 ? 18.034  39.221 8.087   1.00 25.29  ? 243 LYS A CE  1 
ATOM   1990 N  NZ  . LYS A 1 244 ? 17.428  38.266 7.138   1.00 24.92  ? 243 LYS A NZ  1 
ATOM   1991 N  N   . TRP A 1 245 ? 20.863  43.024 5.384   1.00 19.26  ? 244 TRP A N   1 
ATOM   1992 C  CA  . TRP A 1 245 ? 20.800  44.389 5.930   1.00 21.19  ? 244 TRP A CA  1 
ATOM   1993 C  C   . TRP A 1 245 ? 19.418  44.630 6.520   1.00 19.44  ? 244 TRP A C   1 
ATOM   1994 O  O   . TRP A 1 245 ? 18.454  43.863 6.201   1.00 22.37  ? 244 TRP A O   1 
ATOM   1995 C  CB  . TRP A 1 245 ? 21.220  45.461 4.909   1.00 19.86  ? 244 TRP A CB  1 
ATOM   1996 C  CG  . TRP A 1 245 ? 20.416  45.575 3.652   1.00 22.59  ? 244 TRP A CG  1 
ATOM   1997 C  CD1 . TRP A 1 245 ? 20.840  45.232 2.403   1.00 25.58  ? 244 TRP A CD1 1 
ATOM   1998 C  CD2 . TRP A 1 245 ? 19.126  46.177 3.481   1.00 22.97  ? 244 TRP A CD2 1 
ATOM   1999 N  NE1 . TRP A 1 245 ? 19.882  45.518 1.483   1.00 22.97  ? 244 TRP A NE1 1 
ATOM   2000 C  CE2 . TRP A 1 245 ? 18.830  46.118 2.106   1.00 22.45  ? 244 TRP A CE2 1 
ATOM   2001 C  CE3 . TRP A 1 245 ? 18.196  46.771 4.341   1.00 28.07  ? 244 TRP A CE3 1 
ATOM   2002 C  CZ2 . TRP A 1 245 ? 17.651  46.637 1.574   1.00 28.15  ? 244 TRP A CZ2 1 
ATOM   2003 C  CZ3 . TRP A 1 245 ? 17.031  47.269 3.817   1.00 30.74  ? 244 TRP A CZ3 1 
ATOM   2004 C  CH2 . TRP A 1 245 ? 16.772  47.226 2.452   1.00 26.06  ? 244 TRP A CH2 1 
ATOM   2005 N  N   . ALA A 1 246 ? 19.391  45.580 7.427   1.00 20.85  ? 245 ALA A N   1 
ATOM   2006 C  CA  . ALA A 1 246 ? 18.222  46.026 8.192   1.00 21.68  ? 245 ALA A CA  1 
ATOM   2007 C  C   . ALA A 1 246 ? 18.218  47.544 8.126   1.00 23.25  ? 245 ALA A C   1 
ATOM   2008 O  O   . ALA A 1 246 ? 19.294  48.172 8.341   1.00 24.09  ? 245 ALA A O   1 
ATOM   2009 C  CB  . ALA A 1 246 ? 18.281  45.530 9.604   1.00 21.96  ? 245 ALA A CB  1 
ATOM   2010 N  N   . ALA A 1 247 ? 17.065  48.151 7.841   1.00 26.46  ? 246 ALA A N   1 
ATOM   2011 C  CA  . ALA A 1 247 ? 16.974  49.622 7.672   1.00 27.42  ? 246 ALA A CA  1 
ATOM   2012 C  C   . ALA A 1 247 ? 15.829  50.215 8.498   1.00 30.82  ? 246 ALA A C   1 
ATOM   2013 O  O   . ALA A 1 247 ? 14.790  49.561 8.623   1.00 30.81  ? 246 ALA A O   1 
ATOM   2014 C  CB  . ALA A 1 247 ? 16.822  49.969 6.217   1.00 32.20  ? 246 ALA A CB  1 
ATOM   2015 N  N   . VAL A 1 248 ? 16.041  51.428 9.005   1.00 29.87  ? 247 VAL A N   1 
ATOM   2016 C  CA  . VAL A 1 248 ? 15.050  52.183 9.818   1.00 31.90  ? 247 VAL A CA  1 
ATOM   2017 C  C   . VAL A 1 248 ? 15.068  53.643 9.347   1.00 37.64  ? 247 VAL A C   1 
ATOM   2018 O  O   . VAL A 1 248 ? 16.132  54.155 8.943   1.00 31.99  ? 247 VAL A O   1 
ATOM   2019 C  CB  . VAL A 1 248 ? 15.363  52.017 11.316  1.00 34.07  ? 247 VAL A CB  1 
ATOM   2020 C  CG1 . VAL A 1 248 ? 16.740  52.557 11.680  1.00 36.50  ? 247 VAL A CG1 1 
ATOM   2021 C  CG2 . VAL A 1 248 ? 14.295  52.645 12.187  1.00 47.13  ? 247 VAL A CG2 1 
ATOM   2022 N  N   . VAL A 1 249 ? 13.907  54.290 9.343   1.00 34.16  ? 248 VAL A N   1 
ATOM   2023 C  CA  . VAL A 1 249 ? 13.778  55.716 8.915   1.00 33.64  ? 248 VAL A CA  1 
ATOM   2024 C  C   . VAL A 1 249 ? 13.917  56.589 10.156  1.00 33.23  ? 248 VAL A C   1 
ATOM   2025 O  O   . VAL A 1 249 ? 13.186  56.379 11.114  1.00 38.96  ? 248 VAL A O   1 
ATOM   2026 C  CB  . VAL A 1 249 ? 12.449  55.940 8.180   1.00 36.23  ? 248 VAL A CB  1 
ATOM   2027 C  CG1 . VAL A 1 249 ? 12.257  57.411 7.814   1.00 48.08  ? 248 VAL A CG1 1 
ATOM   2028 C  CG2 . VAL A 1 249 ? 12.338  55.049 6.951   1.00 39.96  ? 248 VAL A CG2 1 
ATOM   2029 N  N   . VAL A 1 250 ? 14.879  57.490 10.167  1.00 37.81  ? 249 VAL A N   1 
ATOM   2030 C  CA  . VAL A 1 250 ? 15.321  58.217 11.389  1.00 40.08  ? 249 VAL A CA  1 
ATOM   2031 C  C   . VAL A 1 250 ? 15.037  59.699 11.168  1.00 52.08  ? 249 VAL A C   1 
ATOM   2032 O  O   . VAL A 1 250 ? 15.447  60.236 10.143  1.00 43.30  ? 249 VAL A O   1 
ATOM   2033 C  CB  . VAL A 1 250 ? 16.814  57.932 11.622  1.00 42.89  ? 249 VAL A CB  1 
ATOM   2034 C  CG1 . VAL A 1 250 ? 17.480  58.917 12.564  1.00 44.52  ? 249 VAL A CG1 1 
ATOM   2035 C  CG2 . VAL A 1 250 ? 17.012  56.492 12.101  1.00 39.68  ? 249 VAL A CG2 1 
ATOM   2036 N  N   . PRO A 1 251 ? 14.358  60.408 12.106  1.00 42.28  ? 250 PRO A N   1 
ATOM   2037 C  CA  . PRO A 1 251 ? 14.327  61.873 12.065  1.00 40.56  ? 250 PRO A CA  1 
ATOM   2038 C  C   . PRO A 1 251 ? 15.740  62.476 12.120  1.00 43.99  ? 250 PRO A C   1 
ATOM   2039 O  O   . PRO A 1 251 ? 16.547  62.004 12.903  1.00 43.44  ? 250 PRO A O   1 
ATOM   2040 C  CB  . PRO A 1 251 ? 13.516  62.266 13.325  1.00 42.44  ? 250 PRO A CB  1 
ATOM   2041 C  CG  . PRO A 1 251 ? 12.741  61.009 13.682  1.00 52.05  ? 250 PRO A CG  1 
ATOM   2042 C  CD  . PRO A 1 251 ? 13.651  59.864 13.279  1.00 42.32  ? 250 PRO A CD  1 
ATOM   2043 N  N   . SER A 1 252 ? 16.018  63.493 11.298  1.00 46.98  ? 251 SER A N   1 
ATOM   2044 C  CA  . SER A 1 252 ? 17.293  64.258 11.316  1.00 49.26  ? 251 SER A CA  1 
ATOM   2045 C  C   . SER A 1 252 ? 17.563  64.734 12.740  1.00 54.56  ? 251 SER A C   1 
ATOM   2046 O  O   . SER A 1 252 ? 16.595  65.198 13.390  1.00 60.02  ? 251 SER A O   1 
ATOM   2047 C  CB  . SER A 1 252 ? 17.257  65.415 10.350  1.00 60.70  ? 251 SER A CB  1 
ATOM   2048 O  OG  . SER A 1 252 ? 16.806  64.968 9.084   1.00 60.29  ? 251 SER A OG  1 
ATOM   2049 N  N   . GLY A 1 253 ? 18.809  64.586 13.205  1.00 55.24  ? 252 GLY A N   1 
ATOM   2050 C  CA  . GLY A 1 253 ? 19.259  64.976 14.557  1.00 55.16  ? 252 GLY A CA  1 
ATOM   2051 C  C   . GLY A 1 253 ? 19.123  63.863 15.591  1.00 53.70  ? 252 GLY A C   1 
ATOM   2052 O  O   . GLY A 1 253 ? 19.738  64.002 16.674  1.00 50.98  ? 252 GLY A O   1 
ATOM   2053 N  N   . GLU A 1 254 ? 18.363  62.798 15.297  1.00 44.50  ? 253 GLU A N   1 
ATOM   2054 C  CA  . GLU A 1 254 ? 18.098  61.677 16.246  1.00 48.51  ? 253 GLU A CA  1 
ATOM   2055 C  C   . GLU A 1 254 ? 18.991  60.459 15.932  1.00 47.30  ? 253 GLU A C   1 
ATOM   2056 O  O   . GLU A 1 254 ? 18.899  59.448 16.657  1.00 39.37  ? 253 GLU A O   1 
ATOM   2057 C  CB  . GLU A 1 254 ? 16.616  61.297 16.193  1.00 69.14  ? 253 GLU A CB  1 
ATOM   2058 C  CG  . GLU A 1 254 ? 15.702  62.346 16.798  1.00 75.78  ? 253 GLU A CG  1 
ATOM   2059 C  CD  . GLU A 1 254 ? 14.295  61.846 17.069  1.00 100.36 ? 253 GLU A CD  1 
ATOM   2060 O  OE1 . GLU A 1 254 ? 14.148  60.706 17.576  1.00 98.55  ? 253 GLU A OE1 1 
ATOM   2061 O  OE2 . GLU A 1 254 ? 13.346  62.588 16.750  1.00 113.11 ? 253 GLU A OE2 1 
ATOM   2062 N  N   . GLU A 1 255 ? 19.851  60.554 14.925  1.00 49.82  ? 254 GLU A N   1 
ATOM   2063 C  CA  . GLU A 1 255 ? 20.702  59.408 14.509  1.00 43.40  ? 254 GLU A CA  1 
ATOM   2064 C  C   . GLU A 1 255 ? 21.456  58.757 15.676  1.00 47.41  ? 254 GLU A C   1 
ATOM   2065 O  O   . GLU A 1 255 ? 21.570  57.552 15.671  1.00 45.59  ? 254 GLU A O   1 
ATOM   2066 C  CB  . GLU A 1 255 ? 21.682  59.863 13.428  1.00 42.39  ? 254 GLU A CB  1 
ATOM   2067 C  CG  . GLU A 1 255 ? 20.997  60.225 12.134  1.00 41.61  ? 254 GLU A CG  1 
ATOM   2068 C  CD  . GLU A 1 255 ? 20.730  61.705 11.959  1.00 49.35  ? 254 GLU A CD  1 
ATOM   2069 O  OE1 . GLU A 1 255 ? 20.803  62.450 12.917  1.00 47.66  ? 254 GLU A OE1 1 
ATOM   2070 O  OE2 . GLU A 1 255 ? 20.483  62.092 10.850  1.00 60.47  ? 254 GLU A OE2 1 
ATOM   2071 N  N   . GLN A 1 256 ? 21.878  59.517 16.674  1.00 36.58  ? 255 GLN A N   1 
ATOM   2072 C  CA  . GLN A 1 256 ? 22.737  58.953 17.753  1.00 43.38  ? 255 GLN A CA  1 
ATOM   2073 C  C   . GLN A 1 256 ? 21.887  58.218 18.810  1.00 44.26  ? 255 GLN A C   1 
ATOM   2074 O  O   . GLN A 1 256 ? 22.490  57.533 19.664  1.00 45.77  ? 255 GLN A O   1 
ATOM   2075 C  CB  . GLN A 1 256 ? 23.677  60.031 18.304  1.00 63.68  ? 255 GLN A CB  1 
ATOM   2076 C  CG  . GLN A 1 256 ? 24.803  60.392 17.327  1.00 76.64  ? 255 GLN A CG  1 
ATOM   2077 C  CD  . GLN A 1 256 ? 25.390  59.216 16.566  1.00 83.14  ? 255 GLN A CD  1 
ATOM   2078 O  OE1 . GLN A 1 256 ? 25.938  58.274 17.145  1.00 49.10  ? 255 GLN A OE1 1 
ATOM   2079 N  NE2 . GLN A 1 256 ? 25.286  59.261 15.243  1.00 69.51  ? 255 GLN A NE2 1 
ATOM   2080 N  N   . ARG A 1 257 ? 20.556  58.255 18.689  1.00 37.91  ? 256 ARG A N   1 
ATOM   2081 C  CA  . ARG A 1 257 ? 19.621  57.427 19.498  1.00 41.82  ? 256 ARG A CA  1 
ATOM   2082 C  C   . ARG A 1 257 ? 19.557  55.981 18.968  1.00 42.62  ? 256 ARG A C   1 
ATOM   2083 O  O   . ARG A 1 257 ? 19.103  55.097 19.708  1.00 39.19  ? 256 ARG A O   1 
ATOM   2084 C  CB  . ARG A 1 257 ? 18.212  58.016 19.437  1.00 43.99  ? 256 ARG A CB  1 
ATOM   2085 C  CG  . ARG A 1 257 ? 18.042  59.335 20.183  1.00 47.34  ? 256 ARG A CG  1 
ATOM   2086 C  CD  . ARG A 1 257 ? 16.567  59.694 20.267  1.00 52.61  ? 256 ARG A CD  1 
ATOM   2087 N  NE  . ARG A 1 257 ? 16.356  60.975 20.920  1.00 61.40  ? 256 ARG A NE  1 
ATOM   2088 C  CZ  . ARG A 1 257 ? 16.234  61.169 22.237  1.00 55.57  ? 256 ARG A CZ  1 
ATOM   2089 N  NH1 . ARG A 1 257 ? 16.058  62.393 22.697  1.00 50.80  ? 256 ARG A NH1 1 
ATOM   2090 N  NH2 . ARG A 1 257 ? 16.284  60.165 23.094  1.00 41.61  ? 256 ARG A NH2 1 
ATOM   2091 N  N   . TYR A 1 258 ? 19.943  55.754 17.711  1.00 33.39  ? 257 TYR A N   1 
ATOM   2092 C  CA  . TYR A 1 258 ? 19.702  54.469 16.997  1.00 32.14  ? 257 TYR A CA  1 
ATOM   2093 C  C   . TYR A 1 258 ? 20.962  53.613 17.058  1.00 29.57  ? 257 TYR A C   1 
ATOM   2094 O  O   . TYR A 1 258 ? 22.059  54.092 16.770  1.00 32.04  ? 257 TYR A O   1 
ATOM   2095 C  CB  . TYR A 1 258 ? 19.259  54.767 15.572  1.00 33.15  ? 257 TYR A CB  1 
ATOM   2096 C  CG  . TYR A 1 258 ? 17.834  55.236 15.508  1.00 37.16  ? 257 TYR A CG  1 
ATOM   2097 C  CD1 . TYR A 1 258 ? 17.486  56.572 15.680  1.00 39.86  ? 257 TYR A CD1 1 
ATOM   2098 C  CD2 . TYR A 1 258 ? 16.816  54.314 15.365  1.00 30.81  ? 257 TYR A CD2 1 
ATOM   2099 C  CE1 . TYR A 1 258 ? 16.156  56.974 15.646  1.00 38.11  ? 257 TYR A CE1 1 
ATOM   2100 C  CE2 . TYR A 1 258 ? 15.491  54.698 15.296  1.00 38.12  ? 257 TYR A CE2 1 
ATOM   2101 C  CZ  . TYR A 1 258 ? 15.155  56.027 15.475  1.00 43.46  ? 257 TYR A CZ  1 
ATOM   2102 O  OH  . TYR A 1 258 ? 13.835  56.347 15.405  1.00 45.87  ? 257 TYR A OH  1 
ATOM   2103 N  N   . THR A 1 259 ? 20.808  52.354 17.465  1.00 32.41  ? 258 THR A N   1 
ATOM   2104 C  CA  . THR A 1 259 ? 21.925  51.390 17.467  1.00 25.97  ? 258 THR A CA  1 
ATOM   2105 C  C   . THR A 1 259 ? 21.528  50.172 16.643  1.00 28.39  ? 258 THR A C   1 
ATOM   2106 O  O   . THR A 1 259 ? 20.378  49.680 16.761  1.00 28.87  ? 258 THR A O   1 
ATOM   2107 C  CB  . THR A 1 259 ? 22.366  51.024 18.883  1.00 28.29  ? 258 THR A CB  1 
ATOM   2108 O  OG1 . THR A 1 259 ? 21.228  50.540 19.570  1.00 33.93  ? 258 THR A OG1 1 
ATOM   2109 C  CG2 . THR A 1 259 ? 22.977  52.190 19.614  1.00 30.36  ? 258 THR A CG2 1 
ATOM   2110 N  N   . CYS A 1 260 ? 22.489  49.640 15.897  1.00 25.13  ? 259 CYS A N   1 
ATOM   2111 C  CA  . CYS A 1 260 ? 22.273  48.377 15.164  1.00 23.62  ? 259 CYS A CA  1 
ATOM   2112 C  C   . CYS A 1 260 ? 22.999  47.289 15.917  1.00 24.31  ? 259 CYS A C   1 
ATOM   2113 O  O   . CYS A 1 260 ? 24.153  47.522 16.356  1.00 26.47  ? 259 CYS A O   1 
ATOM   2114 C  CB  . CYS A 1 260 ? 22.738  48.450 13.715  1.00 26.48  ? 259 CYS A CB  1 
ATOM   2115 S  SG  . CYS A 1 260 ? 22.682  46.827 12.907  1.00 28.00  ? 259 CYS A SG  1 
ATOM   2116 N  N   . HIS A 1 261 ? 22.339  46.141 16.073  1.00 23.09  ? 260 HIS A N   1 
ATOM   2117 C  CA  . HIS A 1 261 ? 22.821  45.040 16.924  1.00 21.20  ? 260 HIS A CA  1 
ATOM   2118 C  C   . HIS A 1 261 ? 22.967  43.812 16.041  1.00 23.83  ? 260 HIS A C   1 
ATOM   2119 O  O   . HIS A 1 261 ? 22.006  43.453 15.380  1.00 24.20  ? 260 HIS A O   1 
ATOM   2120 C  CB  . HIS A 1 261 ? 21.878  44.787 18.112  1.00 24.91  ? 260 HIS A CB  1 
ATOM   2121 C  CG  . HIS A 1 261 ? 21.829  45.946 19.044  1.00 28.83  ? 260 HIS A CG  1 
ATOM   2122 N  ND1 . HIS A 1 261 ? 22.458  45.945 20.270  1.00 36.50  ? 260 HIS A ND1 1 
ATOM   2123 C  CD2 . HIS A 1 261 ? 21.279  47.168 18.896  1.00 31.12  ? 260 HIS A CD2 1 
ATOM   2124 C  CE1 . HIS A 1 261 ? 22.254  47.113 20.860  1.00 33.74  ? 260 HIS A CE1 1 
ATOM   2125 N  NE2 . HIS A 1 261 ? 21.566  47.891 20.026  1.00 27.04  ? 260 HIS A NE2 1 
ATOM   2126 N  N   . VAL A 1 262 ? 24.148  43.210 16.036  1.00 21.18  ? 261 VAL A N   1 
ATOM   2127 C  CA  . VAL A 1 262 ? 24.450  42.090 15.125  1.00 22.53  ? 261 VAL A CA  1 
ATOM   2128 C  C   . VAL A 1 262 ? 24.857  40.869 15.951  1.00 25.73  ? 261 VAL A C   1 
ATOM   2129 O  O   . VAL A 1 262 ? 25.884  40.924 16.616  1.00 24.41  ? 261 VAL A O   1 
ATOM   2130 C  CB  . VAL A 1 262 ? 25.528  42.526 14.131  1.00 24.57  ? 261 VAL A CB  1 
ATOM   2131 C  CG1 . VAL A 1 262 ? 25.773  41.433 13.116  1.00 22.36  ? 261 VAL A CG1 1 
ATOM   2132 C  CG2 . VAL A 1 262 ? 25.117  43.845 13.484  1.00 23.62  ? 261 VAL A CG2 1 
ATOM   2133 N  N   . GLN A 1 263 ? 24.065  39.812 15.868  1.00 20.06  ? 262 GLN A N   1 
ATOM   2134 C  CA  . GLN A 1 263 ? 24.343  38.531 16.557  1.00 21.75  ? 262 GLN A CA  1 
ATOM   2135 C  C   . GLN A 1 263 ? 24.710  37.495 15.515  1.00 21.68  ? 262 GLN A C   1 
ATOM   2136 O  O   . GLN A 1 263 ? 23.936  37.346 14.582  1.00 21.33  ? 262 GLN A O   1 
ATOM   2137 C  CB  . GLN A 1 263 ? 23.119  38.023 17.318  1.00 25.69  ? 262 GLN A CB  1 
ATOM   2138 C  CG  . GLN A 1 263 ? 22.647  38.970 18.400  1.00 35.34  ? 262 GLN A CG  1 
ATOM   2139 C  CD  . GLN A 1 263 ? 21.268  38.524 18.812  1.00 42.60  ? 262 GLN A CD  1 
ATOM   2140 O  OE1 . GLN A 1 263 ? 21.041  37.355 19.097  1.00 38.18  ? 262 GLN A OE1 1 
ATOM   2141 N  NE2 . GLN A 1 263 ? 20.323  39.427 18.699  1.00 30.00  ? 262 GLN A NE2 1 
ATOM   2142 N  N   . HIS A 1 264 ? 25.839  36.823 15.704  1.00 20.07  ? 263 HIS A N   1 
ATOM   2143 C  CA  . HIS A 1 264 ? 26.333  35.788 14.782  1.00 22.71  ? 263 HIS A CA  1 
ATOM   2144 C  C   . HIS A 1 264 ? 27.209  34.843 15.580  1.00 23.10  ? 263 HIS A C   1 
ATOM   2145 O  O   . HIS A 1 264 ? 27.906  35.322 16.499  1.00 23.59  ? 263 HIS A O   1 
ATOM   2146 C  CB  . HIS A 1 264 ? 27.039  36.418 13.571  1.00 19.84  ? 263 HIS A CB  1 
ATOM   2147 C  CG  . HIS A 1 264 ? 27.346  35.423 12.520  1.00 22.92  ? 263 HIS A CG  1 
ATOM   2148 N  ND1 . HIS A 1 264 ? 28.537  34.755 12.505  1.00 21.17  ? 263 HIS A ND1 1 
ATOM   2149 C  CD2 . HIS A 1 264 ? 26.596  34.936 11.491  1.00 19.98  ? 263 HIS A CD2 1 
ATOM   2150 C  CE1 . HIS A 1 264 ? 28.550  33.911 11.497  1.00 25.07  ? 263 HIS A CE1 1 
ATOM   2151 N  NE2 . HIS A 1 264 ? 27.343  34.004 10.851  1.00 18.33  ? 263 HIS A NE2 1 
ATOM   2152 N  N   . GLU A 1 265 ? 27.228  33.579 15.173  1.00 21.56  ? 264 GLU A N   1 
ATOM   2153 C  CA  . GLU A 1 265 ? 28.073  32.527 15.787  1.00 29.30  ? 264 GLU A CA  1 
ATOM   2154 C  C   . GLU A 1 265 ? 29.548  32.972 15.802  1.00 27.53  ? 264 GLU A C   1 
ATOM   2155 O  O   . GLU A 1 265 ? 30.292  32.573 16.692  1.00 24.48  ? 264 GLU A O   1 
ATOM   2156 C  CB  . GLU A 1 265 ? 27.881  31.251 14.969  1.00 27.60  ? 264 GLU A CB  1 
ATOM   2157 C  CG  . GLU A 1 265 ? 28.687  30.095 15.450  1.00 37.43  ? 264 GLU A CG  1 
ATOM   2158 C  CD  . GLU A 1 265 ? 28.406  28.838 14.656  1.00 42.85  ? 264 GLU A CD  1 
ATOM   2159 O  OE1 . GLU A 1 265 ? 29.214  27.926 14.742  1.00 41.55  ? 264 GLU A OE1 1 
ATOM   2160 O  OE2 . GLU A 1 265 ? 27.373  28.786 13.979  1.00 41.57  ? 264 GLU A OE2 1 
ATOM   2161 N  N   . GLY A 1 266 ? 29.985  33.740 14.818  1.00 20.34  ? 265 GLY A N   1 
ATOM   2162 C  CA  . GLY A 1 266 ? 31.394  34.163 14.719  1.00 24.63  ? 265 GLY A CA  1 
ATOM   2163 C  C   . GLY A 1 266 ? 31.727  35.340 15.612  1.00 26.07  ? 265 GLY A C   1 
ATOM   2164 O  O   . GLY A 1 266 ? 32.896  35.730 15.636  1.00 24.73  ? 265 GLY A O   1 
ATOM   2165 N  N   . LEU A 1 267 ? 30.744  35.923 16.294  1.00 18.98  ? 266 LEU A N   1 
ATOM   2166 C  CA  . LEU A 1 267 ? 30.922  37.054 17.236  1.00 18.05  ? 266 LEU A CA  1 
ATOM   2167 C  C   . LEU A 1 267 ? 30.691  36.554 18.661  1.00 23.82  ? 266 LEU A C   1 
ATOM   2168 O  O   . LEU A 1 267 ? 29.598  36.137 19.017  1.00 25.44  ? 266 LEU A O   1 
ATOM   2169 C  CB  . LEU A 1 267 ? 29.944  38.178 16.934  1.00 20.74  ? 266 LEU A CB  1 
ATOM   2170 C  CG  . LEU A 1 267 ? 29.979  38.761 15.522  1.00 24.71  ? 266 LEU A CG  1 
ATOM   2171 C  CD1 . LEU A 1 267 ? 28.772  39.648 15.288  1.00 25.42  ? 266 LEU A CD1 1 
ATOM   2172 C  CD2 . LEU A 1 267 ? 31.258  39.523 15.301  1.00 21.10  ? 266 LEU A CD2 1 
ATOM   2173 N  N   . PRO A 1 268 ? 31.707  36.606 19.531  1.00 26.16  ? 267 PRO A N   1 
ATOM   2174 C  CA  . PRO A 1 268 ? 31.532  36.195 20.925  1.00 26.62  ? 267 PRO A CA  1 
ATOM   2175 C  C   . PRO A 1 268 ? 30.402  36.944 21.631  1.00 23.49  ? 267 PRO A C   1 
ATOM   2176 O  O   . PRO A 1 268 ? 29.726  36.382 22.466  1.00 20.42  ? 267 PRO A O   1 
ATOM   2177 C  CB  . PRO A 1 268 ? 32.883  36.600 21.530  1.00 31.38  ? 267 PRO A CB  1 
ATOM   2178 C  CG  . PRO A 1 268 ? 33.829  36.334 20.385  1.00 43.00  ? 267 PRO A CG  1 
ATOM   2179 C  CD  . PRO A 1 268 ? 33.099  36.980 19.218  1.00 34.38  ? 267 PRO A CD  1 
ATOM   2180 N  N   . LYS A 1 269 ? 30.288  38.234 21.367  1.00 25.07  ? 268 LYS A N   1 
ATOM   2181 C  CA  . LYS A 1 269 ? 29.080  38.962 21.816  1.00 35.58  ? 268 LYS A CA  1 
ATOM   2182 C  C   . LYS A 1 269 ? 28.592  39.739 20.623  1.00 25.83  ? 268 LYS A C   1 
ATOM   2183 O  O   . LYS A 1 269 ? 29.366  40.013 19.710  1.00 24.94  ? 268 LYS A O   1 
ATOM   2184 C  CB  . LYS A 1 269 ? 29.346  39.898 23.003  1.00 35.09  ? 268 LYS A CB  1 
ATOM   2185 C  CG  . LYS A 1 269 ? 30.396  40.972 22.794  1.00 36.70  ? 268 LYS A CG  1 
ATOM   2186 C  CD  . LYS A 1 269 ? 30.690  41.748 24.096  1.00 38.09  ? 268 LYS A CD  1 
ATOM   2187 C  CE  . LYS A 1 269 ? 29.422  42.211 24.778  1.00 37.76  ? 268 LYS A CE  1 
ATOM   2188 N  NZ  . LYS A 1 269 ? 29.683  42.943 26.032  1.00 34.85  ? 268 LYS A NZ  1 
ATOM   2189 N  N   . PRO A 1 270 ? 27.319  40.151 20.641  1.00 29.87  ? 269 PRO A N   1 
ATOM   2190 C  CA  . PRO A 1 270 ? 26.787  40.930 19.547  1.00 28.84  ? 269 PRO A CA  1 
ATOM   2191 C  C   . PRO A 1 270 ? 27.537  42.269 19.408  1.00 30.93  ? 269 PRO A C   1 
ATOM   2192 O  O   . PRO A 1 270 ? 28.002  42.815 20.365  1.00 21.63  ? 269 PRO A O   1 
ATOM   2193 C  CB  . PRO A 1 270 ? 25.300  41.140 19.870  1.00 43.10  ? 269 PRO A CB  1 
ATOM   2194 C  CG  . PRO A 1 270 ? 25.039  40.446 21.199  1.00 43.47  ? 269 PRO A CG  1 
ATOM   2195 C  CD  . PRO A 1 270 ? 26.341  39.863 21.691  1.00 37.61  ? 269 PRO A CD  1 
ATOM   2196 N  N   . LEU A 1 271 ? 27.661  42.740 18.173  1.00 25.11  ? 270 LEU A N   1 
ATOM   2197 C  CA  . LEU A 1 271 ? 28.236  44.073 17.855  1.00 25.80  ? 270 LEU A CA  1 
ATOM   2198 C  C   . LEU A 1 271 ? 27.124  45.103 17.956  1.00 26.91  ? 270 LEU A C   1 
ATOM   2199 O  O   . LEU A 1 271 ? 26.001  44.801 17.549  1.00 26.05  ? 270 LEU A O   1 
ATOM   2200 C  CB  . LEU A 1 271 ? 28.864  44.070 16.456  1.00 24.65  ? 270 LEU A CB  1 
ATOM   2201 C  CG  . LEU A 1 271 ? 30.070  43.158 16.324  1.00 26.85  ? 270 LEU A CG  1 
ATOM   2202 C  CD1 . LEU A 1 271 ? 30.471  42.996 14.867  1.00 32.75  ? 270 LEU A CD1 1 
ATOM   2203 C  CD2 . LEU A 1 271 ? 31.239  43.675 17.169  1.00 40.41  ? 270 LEU A CD2 1 
ATOM   2204 N  N   . THR A 1 272 ? 27.433  46.287 18.490  1.00 21.60  ? 271 THR A N   1 
ATOM   2205 C  CA  . THR A 1 272 ? 26.546  47.452 18.463  1.00 23.46  ? 271 THR A CA  1 
ATOM   2206 C  C   . THR A 1 272 ? 27.183  48.491 17.552  1.00 27.45  ? 271 THR A C   1 
ATOM   2207 O  O   . THR A 1 272 ? 28.324  48.834 17.797  1.00 28.91  ? 271 THR A O   1 
ATOM   2208 C  CB  . THR A 1 272 ? 26.359  48.027 19.865  1.00 30.20  ? 271 THR A CB  1 
ATOM   2209 O  OG1 . THR A 1 272 ? 25.761  46.959 20.603  1.00 32.22  ? 271 THR A OG1 1 
ATOM   2210 C  CG2 . THR A 1 272 ? 25.485  49.255 19.845  1.00 35.34  ? 271 THR A CG2 1 
ATOM   2211 N  N   . LEU A 1 273 ? 26.473  48.939 16.536  1.00 26.34  ? 272 LEU A N   1 
ATOM   2212 C  CA  . LEU A 1 273 ? 26.996  49.979 15.624  1.00 25.07  ? 272 LEU A CA  1 
ATOM   2213 C  C   . LEU A 1 273 ? 26.063  51.175 15.656  1.00 27.32  ? 272 LEU A C   1 
ATOM   2214 O  O   . LEU A 1 273 ? 24.860  51.026 15.958  1.00 26.29  ? 272 LEU A O   1 
ATOM   2215 C  CB  . LEU A 1 273 ? 26.993  49.441 14.199  1.00 28.33  ? 272 LEU A CB  1 
ATOM   2216 C  CG  . LEU A 1 273 ? 27.902  48.278 13.869  1.00 31.52  ? 272 LEU A CG  1 
ATOM   2217 C  CD1 . LEU A 1 273 ? 27.156  46.972 14.027  1.00 35.09  ? 272 LEU A CD1 1 
ATOM   2218 C  CD2 . LEU A 1 273 ? 28.352  48.443 12.420  1.00 35.41  ? 272 LEU A CD2 1 
ATOM   2219 N  N   . ARG A 1 274 ? 26.594  52.320 15.265  1.00 29.95  ? 273 ARG A N   1 
ATOM   2220 C  CA  . ARG A 1 274 ? 25.807  53.561 15.076  1.00 35.59  ? 273 ARG A CA  1 
ATOM   2221 C  C   . ARG A 1 274 ? 26.217  54.183 13.753  1.00 28.72  ? 273 ARG A C   1 
ATOM   2222 O  O   . ARG A 1 274 ? 27.335  53.887 13.260  1.00 29.27  ? 273 ARG A O   1 
ATOM   2223 C  CB  . ARG A 1 274 ? 26.093  54.594 16.165  1.00 37.31  ? 273 ARG A CB  1 
ATOM   2224 C  CG  . ARG A 1 274 ? 26.220  53.991 17.551  1.00 59.43  ? 273 ARG A CG  1 
ATOM   2225 C  CD  . ARG A 1 274 ? 26.859  54.911 18.578  1.00 65.75  ? 273 ARG A CD  1 
ATOM   2226 N  NE  . ARG A 1 274 ? 26.308  54.558 19.874  1.00 66.00  ? 273 ARG A NE  1 
ATOM   2227 C  CZ  . ARG A 1 274 ? 25.074  54.861 20.261  1.00 69.53  ? 273 ARG A CZ  1 
ATOM   2228 N  NH1 . ARG A 1 274 ? 24.282  55.566 19.463  1.00 76.35  ? 273 ARG A NH1 1 
ATOM   2229 N  NH2 . ARG A 1 274 ? 24.641  54.461 21.445  1.00 62.64  ? 273 ARG A NH2 1 
ATOM   2230 N  N   . TRP A 1 275 ? 25.368  55.050 13.242  1.00 26.57  ? 274 TRP A N   1 
ATOM   2231 C  CA  . TRP A 1 275 ? 25.754  55.913 12.106  1.00 31.03  ? 274 TRP A CA  1 
ATOM   2232 C  C   . TRP A 1 275 ? 26.975  56.747 12.521  1.00 32.77  ? 274 TRP A C   1 
ATOM   2233 O  O   . TRP A 1 275 ? 26.899  57.486 13.548  1.00 31.94  ? 274 TRP A O   1 
ATOM   2234 C  CB  . TRP A 1 275 ? 24.588  56.761 11.621  1.00 32.54  ? 274 TRP A CB  1 
ATOM   2235 C  CG  . TRP A 1 275 ? 25.080  57.829 10.694  1.00 30.30  ? 274 TRP A CG  1 
ATOM   2236 C  CD1 . TRP A 1 275 ? 24.986  59.176 10.885  1.00 32.89  ? 274 TRP A CD1 1 
ATOM   2237 C  CD2 . TRP A 1 275 ? 25.821  57.642 9.471   1.00 29.97  ? 274 TRP A CD2 1 
ATOM   2238 N  NE1 . TRP A 1 275 ? 25.560  59.843 9.837   1.00 30.84  ? 274 TRP A NE1 1 
ATOM   2239 C  CE2 . TRP A 1 275 ? 26.074  58.932 8.951   1.00 25.25  ? 274 TRP A CE2 1 
ATOM   2240 C  CE3 . TRP A 1 275 ? 26.255  56.526 8.743   1.00 28.74  ? 274 TRP A CE3 1 
ATOM   2241 C  CZ2 . TRP A 1 275 ? 26.771  59.127 7.762   1.00 28.43  ? 274 TRP A CZ2 1 
ATOM   2242 C  CZ3 . TRP A 1 275 ? 26.931  56.722 7.559   1.00 29.89  ? 274 TRP A CZ3 1 
ATOM   2243 C  CH2 . TRP A 1 275 ? 27.209  58.014 7.097   1.00 31.07  ? 274 TRP A CH2 1 
ATOM   2244 N  N   . GLU A 1 276 ? 28.071  56.543 11.784  1.00 38.19  ? 275 GLU A N   1 
ATOM   2245 C  CA  . GLU A 1 276 ? 29.406  57.169 11.968  1.00 46.98  ? 275 GLU A CA  1 
ATOM   2246 C  C   . GLU A 1 276 ? 29.916  57.666 10.616  1.00 50.09  ? 275 GLU A C   1 
ATOM   2247 O  O   . GLU A 1 276 ? 29.941  56.906 9.606   1.00 33.74  ? 275 GLU A O   1 
ATOM   2248 C  CB  . GLU A 1 276 ? 30.421  56.140 12.464  1.00 53.67  ? 275 GLU A CB  1 
ATOM   2249 C  CG  . GLU A 1 276 ? 30.590  56.076 13.964  1.00 65.99  ? 275 GLU A CG  1 
ATOM   2250 C  CD  . GLU A 1 276 ? 31.737  55.168 14.377  1.00 66.09  ? 275 GLU A CD  1 
ATOM   2251 O  OE1 . GLU A 1 276 ? 31.730  54.719 15.533  1.00 79.55  ? 275 GLU A OE1 1 
ATOM   2252 O  OE2 . GLU A 1 276 ? 32.638  54.905 13.528  1.00 58.83  ? 275 GLU A OE2 1 
ATOM   2253 O  OXT . GLU A 1 276 ? 30.318  58.805 10.563  1.00 43.01  ? 275 GLU A OXT 1 
ATOM   2254 N  N   . MET B 2 1   ? -3.019  23.517 -7.947  1.00 35.02  ? 0   MET B N   1 
ATOM   2255 C  CA  . MET B 2 1   ? -1.850  23.895 -7.153  1.00 29.55  ? 0   MET B CA  1 
ATOM   2256 C  C   . MET B 2 1   ? -1.898  25.406 -6.933  1.00 25.57  ? 0   MET B C   1 
ATOM   2257 O  O   . MET B 2 1   ? -2.299  26.143 -7.881  1.00 28.21  ? 0   MET B O   1 
ATOM   2258 C  CB  . MET B 2 1   ? -0.541  23.501 -7.856  1.00 34.66  ? 0   MET B CB  1 
ATOM   2259 C  CG  . MET B 2 1   ? 0.434   24.647 -8.116  1.00 38.07  ? 0   MET B CG  1 
ATOM   2260 S  SD  . MET B 2 1   ? 1.776   24.030 -9.136  1.00 55.34  ? 0   MET B SD  1 
ATOM   2261 C  CE  . MET B 2 1   ? 1.357   24.836 -10.686 1.00 56.06  ? 0   MET B CE  1 
ATOM   2262 N  N   . ILE B 2 2   ? -1.517  25.821 -5.739  1.00 23.46  ? 1   ILE B N   1 
ATOM   2263 C  CA  . ILE B 2 2   ? -1.341  27.248 -5.370  1.00 25.57  ? 1   ILE B CA  1 
ATOM   2264 C  C   . ILE B 2 2   ? 0.060   27.674 -5.848  1.00 27.24  ? 1   ILE B C   1 
ATOM   2265 O  O   . ILE B 2 2   ? 1.065   27.051 -5.523  1.00 26.93  ? 1   ILE B O   1 
ATOM   2266 C  CB  . ILE B 2 2   ? -1.572  27.480 -3.872  1.00 32.44  ? 1   ILE B CB  1 
ATOM   2267 C  CG1 . ILE B 2 2   ? -2.979  27.005 -3.477  1.00 38.89  ? 1   ILE B CG1 1 
ATOM   2268 C  CG2 . ILE B 2 2   ? -1.347  28.957 -3.536  1.00 35.83  ? 1   ILE B CG2 1 
ATOM   2269 C  CD1 . ILE B 2 2   ? -3.327  27.121 -2.005  1.00 42.21  ? 1   ILE B CD1 1 
ATOM   2270 N  N   . GLN B 2 3   ? 0.103   28.705 -6.661  1.00 23.91  ? 2   GLN B N   1 
ATOM   2271 C  CA  . GLN B 2 3   ? 1.370   29.232 -7.199  1.00 24.16  ? 2   GLN B CA  1 
ATOM   2272 C  C   . GLN B 2 3   ? 1.858   30.358 -6.282  1.00 32.19  ? 2   GLN B C   1 
ATOM   2273 O  O   . GLN B 2 3   ? 1.034   31.045 -5.586  1.00 34.29  ? 2   GLN B O   1 
ATOM   2274 C  CB  . GLN B 2 3   ? 1.145   29.689 -8.625  1.00 29.76  ? 2   GLN B CB  1 
ATOM   2275 C  CG  . GLN B 2 3   ? 0.672   28.563 -9.517  1.00 30.14  ? 2   GLN B CG  1 
ATOM   2276 C  CD  . GLN B 2 3   ? 0.455   29.015 -10.939 1.00 44.87  ? 2   GLN B CD  1 
ATOM   2277 O  OE1 . GLN B 2 3   ? 0.766   28.277 -11.871 1.00 48.28  ? 2   GLN B OE1 1 
ATOM   2278 N  NE2 . GLN B 2 3   ? -0.078  30.215 -11.114 1.00 30.27  ? 2   GLN B NE2 1 
ATOM   2279 N  N   . ARG B 2 4   ? 3.166   30.531 -6.255  1.00 25.35  ? 3   ARG B N   1 
ATOM   2280 C  CA  . ARG B 2 4   ? 3.809   31.595 -5.469  1.00 27.73  ? 3   ARG B CA  1 
ATOM   2281 C  C   . ARG B 2 4   ? 4.795   32.349 -6.356  1.00 21.84  ? 3   ARG B C   1 
ATOM   2282 O  O   . ARG B 2 4   ? 5.610   31.719 -7.028  1.00 22.40  ? 3   ARG B O   1 
ATOM   2283 C  CB  . ARG B 2 4   ? 4.512   30.995 -4.257  1.00 28.95  ? 3   ARG B CB  1 
ATOM   2284 C  CG  . ARG B 2 4   ? 3.553   30.700 -3.118  1.00 36.96  ? 3   ARG B CG  1 
ATOM   2285 C  CD  . ARG B 2 4   ? 4.268   30.522 -1.784  1.00 43.44  ? 3   ARG B CD  1 
ATOM   2286 N  NE  . ARG B 2 4   ? 5.104   29.335 -1.805  1.00 36.69  ? 3   ARG B NE  1 
ATOM   2287 C  CZ  . ARG B 2 4   ? 4.652   28.095 -1.829  1.00 45.95  ? 3   ARG B CZ  1 
ATOM   2288 N  NH1 . ARG B 2 4   ? 3.344   27.878 -1.837  1.00 40.70  ? 3   ARG B NH1 1 
ATOM   2289 N  NH2 . ARG B 2 4   ? 5.517   27.078 -1.824  1.00 47.30  ? 3   ARG B NH2 1 
ATOM   2290 N  N   . THR B 2 5   ? 4.671   33.674 -6.340  1.00 22.07  ? 4   THR B N   1 
ATOM   2291 C  CA  . THR B 2 5   ? 5.522   34.583 -7.119  1.00 20.36  ? 4   THR B CA  1 
ATOM   2292 C  C   . THR B 2 5   ? 6.937   34.608 -6.537  1.00 21.79  ? 4   THR B C   1 
ATOM   2293 O  O   . THR B 2 5   ? 7.111   34.679 -5.314  1.00 22.90  ? 4   THR B O   1 
ATOM   2294 C  CB  . THR B 2 5   ? 4.929   35.999 -7.095  1.00 28.41  ? 4   THR B CB  1 
ATOM   2295 O  OG1 . THR B 2 5   ? 3.533   35.901 -7.388  1.00 35.90  ? 4   THR B OG1 1 
ATOM   2296 C  CG2 . THR B 2 5   ? 5.596   36.882 -8.113  1.00 34.21  ? 4   THR B CG2 1 
ATOM   2297 N  N   . PRO B 2 6   ? 7.987   34.635 -7.374  1.00 20.31  ? 5   PRO B N   1 
ATOM   2298 C  CA  . PRO B 2 6   ? 9.344   34.761 -6.856  1.00 21.96  ? 5   PRO B CA  1 
ATOM   2299 C  C   . PRO B 2 6   ? 9.592   36.122 -6.209  1.00 26.22  ? 5   PRO B C   1 
ATOM   2300 O  O   . PRO B 2 6   ? 9.059   37.126 -6.643  1.00 25.91  ? 5   PRO B O   1 
ATOM   2301 C  CB  . PRO B 2 6   ? 10.265  34.633 -8.066  1.00 21.28  ? 5   PRO B CB  1 
ATOM   2302 C  CG  . PRO B 2 6   ? 9.346   35.056 -9.219  1.00 22.43  ? 5   PRO B CG  1 
ATOM   2303 C  CD  . PRO B 2 6   ? 7.965   34.557 -8.847  1.00 20.77  ? 5   PRO B CD  1 
ATOM   2304 N  N   . LYS B 2 7   ? 10.341  36.087 -5.119  1.00 20.88  ? 6   LYS B N   1 
ATOM   2305 C  CA  . LYS B 2 7   ? 11.043  37.254 -4.562  1.00 21.23  ? 6   LYS B CA  1 
ATOM   2306 C  C   . LYS B 2 7   ? 12.357  37.374 -5.314  1.00 20.36  ? 6   LYS B C   1 
ATOM   2307 O  O   . LYS B 2 7   ? 12.952  36.333 -5.737  1.00 21.66  ? 6   LYS B O   1 
ATOM   2308 C  CB  . LYS B 2 7   ? 11.298  37.027 -3.073  1.00 26.75  ? 6   LYS B CB  1 
ATOM   2309 C  CG  . LYS B 2 7   ? 10.052  36.958 -2.205  1.00 38.54  ? 6   LYS B CG  1 
ATOM   2310 C  CD  . LYS B 2 7   ? 10.341  36.399 -0.807  1.00 55.28  ? 6   LYS B CD  1 
ATOM   2311 C  CE  . LYS B 2 7   ? 9.090   36.184 0.017   1.00 68.18  ? 6   LYS B CE  1 
ATOM   2312 N  NZ  . LYS B 2 7   ? 9.366   36.355 1.461   1.00 81.68  ? 6   LYS B NZ  1 
ATOM   2313 N  N   . ILE B 2 8   ? 12.860  38.602 -5.394  1.00 20.51  ? 7   ILE B N   1 
ATOM   2314 C  CA  . ILE B 2 8   ? 14.037  38.891 -6.224  1.00 21.76  ? 7   ILE B CA  1 
ATOM   2315 C  C   . ILE B 2 8   ? 14.885  39.876 -5.437  1.00 19.97  ? 7   ILE B C   1 
ATOM   2316 O  O   . ILE B 2 8   ? 14.337  40.907 -5.034  1.00 24.21  ? 7   ILE B O   1 
ATOM   2317 C  CB  . ILE B 2 8   ? 13.604  39.465 -7.585  1.00 22.28  ? 7   ILE B CB  1 
ATOM   2318 C  CG1 . ILE B 2 8   ? 12.675  38.517 -8.350  1.00 24.78  ? 7   ILE B CG1 1 
ATOM   2319 C  CG2 . ILE B 2 8   ? 14.819  39.815 -8.415  1.00 23.96  ? 7   ILE B CG2 1 
ATOM   2320 C  CD1 . ILE B 2 8   ? 11.984  39.176 -9.527  1.00 27.55  ? 7   ILE B CD1 1 
ATOM   2321 N  N   . GLN B 2 9   ? 16.160  39.565 -5.287  1.00 21.55  ? 8   GLN B N   1 
ATOM   2322 C  CA  . GLN B 2 9   ? 17.151  40.576 -4.870  1.00 21.75  ? 8   GLN B CA  1 
ATOM   2323 C  C   . GLN B 2 9   ? 18.276  40.572 -5.881  1.00 21.01  ? 8   GLN B C   1 
ATOM   2324 O  O   . GLN B 2 9   ? 18.744  39.502 -6.245  1.00 21.73  ? 8   GLN B O   1 
ATOM   2325 C  CB  . GLN B 2 9   ? 17.707  40.271 -3.482  1.00 22.50  ? 8   GLN B CB  1 
ATOM   2326 C  CG  . GLN B 2 9   ? 16.674  40.368 -2.379  1.00 21.85  ? 8   GLN B CG  1 
ATOM   2327 C  CD  . GLN B 2 9   ? 17.372  40.353 -1.037  1.00 25.74  ? 8   GLN B CD  1 
ATOM   2328 O  OE1 . GLN B 2 9   ? 18.115  41.280 -0.717  1.00 22.99  ? 8   GLN B OE1 1 
ATOM   2329 N  NE2 . GLN B 2 9   ? 17.162  39.293 -0.272  1.00 23.71  ? 8   GLN B NE2 1 
ATOM   2330 N  N   . VAL B 2 10  ? 18.722  41.764 -6.255  1.00 19.71  ? 9   VAL B N   1 
ATOM   2331 C  CA  . VAL B 2 10  ? 19.865  41.987 -7.157  1.00 21.12  ? 9   VAL B CA  1 
ATOM   2332 C  C   . VAL B 2 10  ? 20.876  42.818 -6.380  1.00 21.62  ? 9   VAL B C   1 
ATOM   2333 O  O   . VAL B 2 10  ? 20.456  43.814 -5.787  1.00 25.20  ? 9   VAL B O   1 
ATOM   2334 C  CB  . VAL B 2 10  ? 19.437  42.736 -8.422  1.00 24.48  ? 9   VAL B CB  1 
ATOM   2335 C  CG1 . VAL B 2 10  ? 20.548  42.674 -9.435  1.00 25.71  ? 9   VAL B CG1 1 
ATOM   2336 C  CG2 . VAL B 2 10  ? 18.133  42.197 -8.955  1.00 41.25  ? 9   VAL B CG2 1 
ATOM   2337 N  N   . TYR B 2 11  ? 22.122  42.373 -6.382  1.00 21.79  ? 10  TYR B N   1 
ATOM   2338 C  CA  . TYR B 2 11  ? 23.148  42.873 -5.451  1.00 23.09  ? 10  TYR B CA  1 
ATOM   2339 C  C   . TYR B 2 11  ? 24.510  42.377 -5.898  1.00 26.72  ? 10  TYR B C   1 
ATOM   2340 O  O   . TYR B 2 11  ? 24.633  41.400 -6.626  1.00 24.68  ? 10  TYR B O   1 
ATOM   2341 C  CB  . TYR B 2 11  ? 22.794  42.438 -4.021  1.00 18.63  ? 10  TYR B CB  1 
ATOM   2342 C  CG  . TYR B 2 11  ? 22.701  40.965 -3.788  1.00 21.41  ? 10  TYR B CG  1 
ATOM   2343 C  CD1 . TYR B 2 11  ? 21.549  40.282 -4.150  1.00 20.71  ? 10  TYR B CD1 1 
ATOM   2344 C  CD2 . TYR B 2 11  ? 23.788  40.222 -3.316  1.00 19.84  ? 10  TYR B CD2 1 
ATOM   2345 C  CE1 . TYR B 2 11  ? 21.440  38.924 -3.968  1.00 19.83  ? 10  TYR B CE1 1 
ATOM   2346 C  CE2 . TYR B 2 11  ? 23.687  38.855 -3.140  1.00 20.57  ? 10  TYR B CE2 1 
ATOM   2347 C  CZ  . TYR B 2 11  ? 22.504  38.206 -3.475  1.00 20.04  ? 10  TYR B CZ  1 
ATOM   2348 O  OH  . TYR B 2 11  ? 22.348  36.858 -3.348  1.00 21.04  ? 10  TYR B OH  1 
ATOM   2349 N  N   . SER B 2 12  ? 25.550  43.067 -5.441  1.00 23.68  ? 11  SER B N   1 
ATOM   2350 C  CA  . SER B 2 12  ? 26.941  42.694 -5.741  1.00 22.69  ? 11  SER B CA  1 
ATOM   2351 C  C   . SER B 2 12  ? 27.489  41.846 -4.595  1.00 27.08  ? 11  SER B C   1 
ATOM   2352 O  O   . SER B 2 12  ? 27.029  42.006 -3.457  1.00 25.40  ? 11  SER B O   1 
ATOM   2353 C  CB  . SER B 2 12  ? 27.796  43.929 -5.964  1.00 25.17  ? 11  SER B CB  1 
ATOM   2354 O  OG  . SER B 2 12  ? 27.692  44.784 -4.864  1.00 27.32  ? 11  SER B OG  1 
ATOM   2355 N  N   . ARG B 2 13  ? 28.447  40.990 -4.903  1.00 23.54  ? 12  ARG B N   1 
ATOM   2356 C  CA  . ARG B 2 13  ? 29.112  40.122 -3.915  1.00 25.24  ? 12  ARG B CA  1 
ATOM   2357 C  C   . ARG B 2 13  ? 29.876  41.004 -2.909  1.00 28.75  ? 12  ARG B C   1 
ATOM   2358 O  O   . ARG B 2 13  ? 29.858  40.664 -1.749  1.00 25.06  ? 12  ARG B O   1 
ATOM   2359 C  CB  . ARG B 2 13  ? 30.067  39.174 -4.626  1.00 29.96  ? 12  ARG B CB  1 
ATOM   2360 C  CG  . ARG B 2 13  ? 30.840  38.290 -3.659  1.00 29.19  ? 12  ARG B CG  1 
ATOM   2361 C  CD  . ARG B 2 13  ? 31.851  37.476 -4.428  1.00 32.96  ? 12  ARG B CD  1 
ATOM   2362 N  NE  . ARG B 2 13  ? 31.195  36.448 -5.206  1.00 31.79  ? 12  ARG B NE  1 
ATOM   2363 C  CZ  . ARG B 2 13  ? 31.816  35.563 -5.968  1.00 32.96  ? 12  ARG B CZ  1 
ATOM   2364 N  NH1 . ARG B 2 13  ? 33.141  35.525 -6.024  1.00 33.31  ? 12  ARG B NH1 1 
ATOM   2365 N  NH2 . ARG B 2 13  ? 31.092  34.669 -6.618  1.00 30.81  ? 12  ARG B NH2 1 
ATOM   2366 N  N   . HIS B 2 14  ? 30.540  42.056 -3.384  1.00 27.73  ? 13  HIS B N   1 
ATOM   2367 C  CA  . HIS B 2 14  ? 31.345  43.024 -2.608  1.00 25.99  ? 13  HIS B CA  1 
ATOM   2368 C  C   . HIS B 2 14  ? 30.716  44.411 -2.753  1.00 27.61  ? 13  HIS B C   1 
ATOM   2369 O  O   . HIS B 2 14  ? 30.118  44.744 -3.771  1.00 26.19  ? 13  HIS B O   1 
ATOM   2370 C  CB  . HIS B 2 14  ? 32.815  42.940 -3.075  1.00 27.09  ? 13  HIS B CB  1 
ATOM   2371 C  CG  . HIS B 2 14  ? 33.409  41.576 -2.995  1.00 27.17  ? 13  HIS B CG  1 
ATOM   2372 N  ND1 . HIS B 2 14  ? 33.742  40.981 -1.783  1.00 35.84  ? 13  HIS B ND1 1 
ATOM   2373 C  CD2 . HIS B 2 14  ? 33.802  40.708 -3.946  1.00 31.77  ? 13  HIS B CD2 1 
ATOM   2374 C  CE1 . HIS B 2 14  ? 34.249  39.775 -2.004  1.00 34.73  ? 13  HIS B CE1 1 
ATOM   2375 N  NE2 . HIS B 2 14  ? 34.283  39.575 -3.322  1.00 33.75  ? 13  HIS B NE2 1 
ATOM   2376 N  N   . PRO B 2 15  ? 30.866  45.305 -1.752  1.00 25.60  ? 14  PRO B N   1 
ATOM   2377 C  CA  . PRO B 2 15  ? 30.376  46.674 -1.871  1.00 28.68  ? 14  PRO B CA  1 
ATOM   2378 C  C   . PRO B 2 15  ? 31.007  47.261 -3.131  1.00 29.40  ? 14  PRO B C   1 
ATOM   2379 O  O   . PRO B 2 15  ? 32.213  47.100 -3.334  1.00 27.10  ? 14  PRO B O   1 
ATOM   2380 C  CB  . PRO B 2 15  ? 30.874  47.359 -0.589  1.00 33.12  ? 14  PRO B CB  1 
ATOM   2381 C  CG  . PRO B 2 15  ? 30.988  46.189 0.376   1.00 32.46  ? 14  PRO B CG  1 
ATOM   2382 C  CD  . PRO B 2 15  ? 31.521  45.048 -0.447  1.00 27.67  ? 14  PRO B CD  1 
ATOM   2383 N  N   . ALA B 2 16  ? 30.180  47.800 -4.016  1.00 28.45  ? 15  ALA B N   1 
ATOM   2384 C  CA  . ALA B 2 16  ? 30.636  48.201 -5.366  1.00 31.34  ? 15  ALA B CA  1 
ATOM   2385 C  C   . ALA B 2 16  ? 31.465  49.502 -5.281  1.00 25.89  ? 15  ALA B C   1 
ATOM   2386 O  O   . ALA B 2 16  ? 31.092  50.402 -4.517  1.00 26.40  ? 15  ALA B O   1 
ATOM   2387 C  CB  . ALA B 2 16  ? 29.476  48.378 -6.288  1.00 30.74  ? 15  ALA B CB  1 
ATOM   2388 N  N   . GLU B 2 17  ? 32.441  49.617 -6.174  1.00 28.88  ? 16  GLU B N   1 
ATOM   2389 C  CA  . GLU B 2 17  ? 33.107  50.898 -6.523  1.00 31.22  ? 16  GLU B CA  1 
ATOM   2390 C  C   . GLU B 2 17  ? 33.293  50.952 -8.034  1.00 24.09  ? 16  GLU B C   1 
ATOM   2391 O  O   . GLU B 2 17  ? 33.655  49.929 -8.630  1.00 30.56  ? 16  GLU B O   1 
ATOM   2392 C  CB  . GLU B 2 17  ? 34.501  50.996 -5.916  1.00 38.88  ? 16  GLU B CB  1 
ATOM   2393 C  CG  . GLU B 2 17  ? 34.540  51.262 -4.427  1.00 48.63  ? 16  GLU B CG  1 
ATOM   2394 C  CD  . GLU B 2 17  ? 35.974  51.551 -3.997  1.00 53.79  ? 16  GLU B CD  1 
ATOM   2395 O  OE1 . GLU B 2 17  ? 36.766  50.583 -3.860  1.00 36.26  ? 16  GLU B OE1 1 
ATOM   2396 O  OE2 . GLU B 2 17  ? 36.320  52.744 -3.881  1.00 33.98  ? 16  GLU B OE2 1 
ATOM   2397 N  N   . ASN B 2 18  ? 33.128  52.126 -8.624  1.00 29.92  ? 17  ASN B N   1 
ATOM   2398 C  CA  . ASN B 2 18  ? 33.268  52.250 -10.097 1.00 29.59  ? 17  ASN B CA  1 
ATOM   2399 C  C   . ASN B 2 18  ? 34.656  51.747 -10.497 1.00 36.63  ? 17  ASN B C   1 
ATOM   2400 O  O   . ASN B 2 18  ? 35.646  52.058 -9.804  1.00 31.62  ? 17  ASN B O   1 
ATOM   2401 C  CB  . ASN B 2 18  ? 32.958  53.673 -10.566 1.00 32.29  ? 17  ASN B CB  1 
ATOM   2402 C  CG  . ASN B 2 18  ? 31.536  54.083 -10.259 1.00 41.76  ? 17  ASN B CG  1 
ATOM   2403 O  OD1 . ASN B 2 18  ? 30.642  53.230 -10.186 1.00 35.90  ? 17  ASN B OD1 1 
ATOM   2404 N  ND2 . ASN B 2 18  ? 31.328  55.377 -10.067 1.00 29.91  ? 17  ASN B ND2 1 
ATOM   2405 N  N   . GLY B 2 19  ? 34.719  50.965 -11.570 1.00 30.04  ? 18  GLY B N   1 
ATOM   2406 C  CA  . GLY B 2 19  ? 35.982  50.469 -12.142 1.00 30.42  ? 18  GLY B CA  1 
ATOM   2407 C  C   . GLY B 2 19  ? 36.526  49.269 -11.426 1.00 31.24  ? 18  GLY B C   1 
ATOM   2408 O  O   . GLY B 2 19  ? 37.553  48.780 -11.857 1.00 34.41  ? 18  GLY B O   1 
ATOM   2409 N  N   . LYS B 2 20  ? 35.887  48.783 -10.357 1.00 29.19  ? 19  LYS B N   1 
ATOM   2410 C  CA  . LYS B 2 20  ? 36.454  47.639 -9.592  1.00 29.41  ? 19  LYS B CA  1 
ATOM   2411 C  C   . LYS B 2 20  ? 35.647  46.381 -9.916  1.00 36.03  ? 19  LYS B C   1 
ATOM   2412 O  O   . LYS B 2 20  ? 34.402  46.410 -9.782  1.00 33.97  ? 19  LYS B O   1 
ATOM   2413 C  CB  . LYS B 2 20  ? 36.402  47.877 -8.079  1.00 39.23  ? 19  LYS B CB  1 
ATOM   2414 C  CG  . LYS B 2 20  ? 36.992  49.197 -7.608  1.00 48.59  ? 19  LYS B CG  1 
ATOM   2415 C  CD  . LYS B 2 20  ? 38.362  49.455 -8.152  1.00 66.15  ? 19  LYS B CD  1 
ATOM   2416 C  CE  . LYS B 2 20  ? 39.020  50.670 -7.539  1.00 72.27  ? 19  LYS B CE  1 
ATOM   2417 N  NZ  . LYS B 2 20  ? 40.441  50.744 -7.943  1.00 79.07  ? 19  LYS B NZ  1 
ATOM   2418 N  N   . SER B 2 21  ? 36.349  45.354 -10.352 1.00 33.03  ? 20  SER B N   1 
ATOM   2419 C  CA  . SER B 2 21  ? 35.806  44.025 -10.713 1.00 40.74  ? 20  SER B CA  1 
ATOM   2420 C  C   . SER B 2 21  ? 35.028  43.490 -9.515  1.00 32.10  ? 20  SER B C   1 
ATOM   2421 O  O   . SER B 2 21  ? 35.432  43.732 -8.361  1.00 27.13  ? 20  SER B O   1 
ATOM   2422 C  CB  . SER B 2 21  ? 36.909  43.107 -11.111 1.00 34.59  ? 20  SER B CB  1 
ATOM   2423 O  OG  . SER B 2 21  ? 36.364  41.908 -11.633 1.00 47.17  ? 20  SER B OG  1 
ATOM   2424 N  N   . ASN B 2 22  ? 33.945  42.773 -9.774  1.00 32.73  ? 21  ASN B N   1 
ATOM   2425 C  CA  . ASN B 2 22  ? 32.992  42.363 -8.717  1.00 24.80  ? 21  ASN B CA  1 
ATOM   2426 C  C   . ASN B 2 22  ? 32.170  41.216 -9.325  1.00 34.02  ? 21  ASN B C   1 
ATOM   2427 O  O   . ASN B 2 22  ? 32.517  40.722 -10.427 1.00 31.23  ? 21  ASN B O   1 
ATOM   2428 C  CB  . ASN B 2 22  ? 32.232  43.606 -8.231  1.00 24.29  ? 21  ASN B CB  1 
ATOM   2429 C  CG  . ASN B 2 22  ? 31.592  43.492 -6.861  1.00 25.63  ? 21  ASN B CG  1 
ATOM   2430 O  OD1 . ASN B 2 22  ? 31.245  42.415 -6.385  1.00 25.10  ? 21  ASN B OD1 1 
ATOM   2431 N  ND2 . ASN B 2 22  ? 31.346  44.629 -6.253  1.00 23.48  ? 21  ASN B ND2 1 
ATOM   2432 N  N   . PHE B 2 23  ? 31.147  40.767 -8.615  1.00 27.95  ? 22  PHE B N   1 
ATOM   2433 C  CA  . PHE B 2 23  ? 30.152  39.778 -9.111  1.00 28.81  ? 22  PHE B CA  1 
ATOM   2434 C  C   . PHE B 2 23  ? 28.753  40.340 -8.906  1.00 28.91  ? 22  PHE B C   1 
ATOM   2435 O  O   . PHE B 2 23  ? 28.441  40.900 -7.810  1.00 26.50  ? 22  PHE B O   1 
ATOM   2436 C  CB  . PHE B 2 23  ? 30.273  38.432 -8.404  1.00 28.10  ? 22  PHE B CB  1 
ATOM   2437 C  CG  . PHE B 2 23  ? 31.493  37.667 -8.822  1.00 32.78  ? 22  PHE B CG  1 
ATOM   2438 C  CD1 . PHE B 2 23  ? 32.743  38.050 -8.370  1.00 39.96  ? 22  PHE B CD1 1 
ATOM   2439 C  CD2 . PHE B 2 23  ? 31.390  36.607 -9.707  1.00 45.20  ? 22  PHE B CD2 1 
ATOM   2440 C  CE1 . PHE B 2 23  ? 33.876  37.376 -8.792  1.00 42.50  ? 22  PHE B CE1 1 
ATOM   2441 C  CE2 . PHE B 2 23  ? 32.523  35.931 -10.123 1.00 47.74  ? 22  PHE B CE2 1 
ATOM   2442 C  CZ  . PHE B 2 23  ? 33.760  36.315 -9.654  1.00 44.76  ? 22  PHE B CZ  1 
ATOM   2443 N  N   . LEU B 2 24  ? 27.941  40.194 -9.949  1.00 23.97  ? 23  LEU B N   1 
ATOM   2444 C  CA  . LEU B 2 24  ? 26.531  40.620 -9.964  1.00 24.85  ? 23  LEU B CA  1 
ATOM   2445 C  C   . LEU B 2 24  ? 25.713  39.364 -9.683  1.00 23.13  ? 23  LEU B C   1 
ATOM   2446 O  O   . LEU B 2 24  ? 25.882  38.326 -10.401 1.00 23.39  ? 23  LEU B O   1 
ATOM   2447 C  CB  . LEU B 2 24  ? 26.156  41.223 -11.315 1.00 28.45  ? 23  LEU B CB  1 
ATOM   2448 C  CG  . LEU B 2 24  ? 24.710  41.712 -11.460 1.00 25.29  ? 23  LEU B CG  1 
ATOM   2449 C  CD1 . LEU B 2 24  ? 24.343  42.813 -10.477 1.00 26.19  ? 23  LEU B CD1 1 
ATOM   2450 C  CD2 . LEU B 2 24  ? 24.431  42.171 -12.877 1.00 25.83  ? 23  LEU B CD2 1 
ATOM   2451 N  N   . ASN B 2 25  ? 24.872  39.473 -8.674  1.00 21.83  ? 24  ASN B N   1 
ATOM   2452 C  CA  . ASN B 2 25  ? 24.032  38.356 -8.195  1.00 23.03  ? 24  ASN B CA  1 
ATOM   2453 C  C   . ASN B 2 25  ? 22.574  38.732 -8.418  1.00 20.61  ? 24  ASN B C   1 
ATOM   2454 O  O   . ASN B 2 25  ? 22.182  39.858 -8.113  1.00 23.06  ? 24  ASN B O   1 
ATOM   2455 C  CB  . ASN B 2 25  ? 24.257  38.086 -6.704  1.00 21.86  ? 24  ASN B CB  1 
ATOM   2456 C  CG  . ASN B 2 25  ? 25.639  37.544 -6.401  1.00 25.75  ? 24  ASN B CG  1 
ATOM   2457 O  OD1 . ASN B 2 25  ? 26.176  36.741 -7.174  1.00 29.41  ? 24  ASN B OD1 1 
ATOM   2458 N  ND2 . ASN B 2 25  ? 26.185  37.907 -5.242  1.00 27.81  ? 24  ASN B ND2 1 
ATOM   2459 N  N   . CYS B 2 26  ? 21.786  37.749 -8.807  1.00 22.65  ? 25  CYS B N   1 
ATOM   2460 C  CA  . CYS B 2 26  ? 20.329  37.837 -8.723  1.00 21.60  ? 25  CYS B CA  1 
ATOM   2461 C  C   . CYS B 2 26  ? 19.843  36.600 -7.986  1.00 20.01  ? 25  CYS B C   1 
ATOM   2462 O  O   . CYS B 2 26  ? 20.115  35.468 -8.435  1.00 20.24  ? 25  CYS B O   1 
ATOM   2463 C  CB  . CYS B 2 26  ? 19.709  37.960 -10.105 1.00 22.73  ? 25  CYS B CB  1 
ATOM   2464 S  SG  . CYS B 2 26  ? 17.937  38.154 -9.932  1.00 24.00  ? 25  CYS B SG  1 
ATOM   2465 N  N   . TYR B 2 27  ? 19.232  36.817 -6.834  1.00 19.92  ? 26  TYR B N   1 
ATOM   2466 C  CA  . TYR B 2 27  ? 18.767  35.756 -5.931  1.00 20.66  ? 26  TYR B CA  1 
ATOM   2467 C  C   . TYR B 2 27  ? 17.258  35.733 -6.083  1.00 20.37  ? 26  TYR B C   1 
ATOM   2468 O  O   . TYR B 2 27  ? 16.590  36.739 -5.768  1.00 22.04  ? 26  TYR B O   1 
ATOM   2469 C  CB  . TYR B 2 27  ? 19.258  36.013 -4.503  1.00 21.51  ? 26  TYR B CB  1 
ATOM   2470 C  CG  . TYR B 2 27  ? 18.866  34.959 -3.505  1.00 19.40  ? 26  TYR B CG  1 
ATOM   2471 C  CD1 . TYR B 2 27  ? 19.360  33.670 -3.617  1.00 21.48  ? 26  TYR B CD1 1 
ATOM   2472 C  CD2 . TYR B 2 27  ? 18.032  35.249 -2.446  1.00 23.91  ? 26  TYR B CD2 1 
ATOM   2473 C  CE1 . TYR B 2 27  ? 19.056  32.694 -2.685  1.00 20.22  ? 26  TYR B CE1 1 
ATOM   2474 C  CE2 . TYR B 2 27  ? 17.698  34.272 -1.517  1.00 23.20  ? 26  TYR B CE2 1 
ATOM   2475 C  CZ  . TYR B 2 27  ? 18.189  32.999 -1.659  1.00 21.11  ? 26  TYR B CZ  1 
ATOM   2476 O  OH  . TYR B 2 27  ? 17.857  32.047 -0.764  1.00 29.78  ? 26  TYR B OH  1 
ATOM   2477 N  N   . VAL B 2 28  ? 16.733  34.590 -6.513  1.00 19.11  ? 27  VAL B N   1 
ATOM   2478 C  CA  . VAL B 2 28  ? 15.268  34.379 -6.628  1.00 19.31  ? 27  VAL B CA  1 
ATOM   2479 C  C   . VAL B 2 28  ? 14.885  33.319 -5.602  1.00 20.13  ? 27  VAL B C   1 
ATOM   2480 O  O   . VAL B 2 28  ? 15.583  32.294 -5.502  1.00 24.01  ? 27  VAL B O   1 
ATOM   2481 C  CB  . VAL B 2 28  ? 14.830  33.994 -8.061  1.00 19.50  ? 27  VAL B CB  1 
ATOM   2482 C  CG1 . VAL B 2 28  ? 15.022  35.168 -9.004  1.00 26.84  ? 27  VAL B CG1 1 
ATOM   2483 C  CG2 . VAL B 2 28  ? 15.516  32.773 -8.588  1.00 25.52  ? 27  VAL B CG2 1 
ATOM   2484 N  N   . SER B 2 29  ? 13.792  33.544 -4.901  1.00 17.83  ? 28  SER B N   1 
ATOM   2485 C  CA  . SER B 2 29  ? 13.340  32.590 -3.881  1.00 21.08  ? 28  SER B CA  1 
ATOM   2486 C  C   . SER B 2 29  ? 11.838  32.627 -3.730  1.00 21.10  ? 28  SER B C   1 
ATOM   2487 O  O   . SER B 2 29  ? 11.210  33.629 -4.103  1.00 21.33  ? 28  SER B O   1 
ATOM   2488 C  CB  . SER B 2 29  ? 14.035  32.894 -2.564  1.00 23.39  ? 28  SER B CB  1 
ATOM   2489 O  OG  . SER B 2 29  ? 13.748  34.202 -2.186  1.00 21.94  ? 28  SER B OG  1 
ATOM   2490 N  N   . GLY B 2 30  ? 11.314  31.578 -3.086  1.00 22.19  ? 29  GLY B N   1 
ATOM   2491 C  CA  . GLY B 2 30  ? 9.941   31.497 -2.584  1.00 25.65  ? 29  GLY B CA  1 
ATOM   2492 C  C   . GLY B 2 30  ? 8.948   31.317 -3.722  1.00 22.07  ? 29  GLY B C   1 
ATOM   2493 O  O   . GLY B 2 30  ? 7.778   31.543 -3.478  1.00 25.22  ? 29  GLY B O   1 
ATOM   2494 N  N   . PHE B 2 31  ? 9.417   30.833 -4.865  1.00 23.77  ? 30  PHE B N   1 
ATOM   2495 C  CA  . PHE B 2 31  ? 8.590   30.680 -6.088  1.00 22.85  ? 30  PHE B CA  1 
ATOM   2496 C  C   . PHE B 2 31  ? 8.053   29.256 -6.097  1.00 22.20  ? 30  PHE B C   1 
ATOM   2497 O  O   . PHE B 2 31  ? 8.732   28.289 -5.635  1.00 20.65  ? 30  PHE B O   1 
ATOM   2498 C  CB  . PHE B 2 31  ? 9.351   30.986 -7.380  1.00 21.16  ? 30  PHE B CB  1 
ATOM   2499 C  CG  . PHE B 2 31  ? 10.706  30.357 -7.523  1.00 22.86  ? 30  PHE B CG  1 
ATOM   2500 C  CD1 . PHE B 2 31  ? 11.826  30.979 -6.976  1.00 20.34  ? 30  PHE B CD1 1 
ATOM   2501 C  CD2 . PHE B 2 31  ? 10.860  29.156 -8.184  1.00 20.67  ? 30  PHE B CD2 1 
ATOM   2502 C  CE1 . PHE B 2 31  ? 13.067  30.399 -7.107  1.00 21.31  ? 30  PHE B CE1 1 
ATOM   2503 C  CE2 . PHE B 2 31  ? 12.111  28.576 -8.331  1.00 26.44  ? 30  PHE B CE2 1 
ATOM   2504 C  CZ  . PHE B 2 31  ? 13.217  29.204 -7.803  1.00 22.24  ? 30  PHE B CZ  1 
ATOM   2505 N  N   . HIS B 2 32  ? 6.821   29.142 -6.547  1.00 24.99  ? 31  HIS B N   1 
ATOM   2506 C  CA  . HIS B 2 32  ? 6.233   27.821 -6.836  1.00 22.49  ? 31  HIS B CA  1 
ATOM   2507 C  C   . HIS B 2 32  ? 5.323   27.943 -8.043  1.00 19.68  ? 31  HIS B C   1 
ATOM   2508 O  O   . HIS B 2 32  ? 4.474   28.830 -8.110  1.00 21.06  ? 31  HIS B O   1 
ATOM   2509 C  CB  . HIS B 2 32  ? 5.501   27.260 -5.618  1.00 20.33  ? 31  HIS B CB  1 
ATOM   2510 C  CG  . HIS B 2 32  ? 5.262   25.817 -5.815  1.00 21.38  ? 31  HIS B CG  1 
ATOM   2511 N  ND1 . HIS B 2 32  ? 6.196   24.877 -5.417  1.00 23.72  ? 31  HIS B ND1 1 
ATOM   2512 C  CD2 . HIS B 2 32  ? 4.240   25.158 -6.435  1.00 23.39  ? 31  HIS B CD2 1 
ATOM   2513 C  CE1 . HIS B 2 32  ? 5.744   23.678 -5.813  1.00 26.89  ? 31  HIS B CE1 1 
ATOM   2514 N  NE2 . HIS B 2 32  ? 4.551   23.830 -6.440  1.00 22.86  ? 31  HIS B NE2 1 
ATOM   2515 N  N   . PRO B 2 33  ? 5.408   27.022 -9.009  1.00 19.75  ? 32  PRO B N   1 
ATOM   2516 C  CA  . PRO B 2 33  ? 6.321   25.887 -9.015  1.00 20.79  ? 32  PRO B CA  1 
ATOM   2517 C  C   . PRO B 2 33  ? 7.771   26.242 -9.363  1.00 23.39  ? 32  PRO B C   1 
ATOM   2518 O  O   . PRO B 2 33  ? 8.065   27.413 -9.437  1.00 25.09  ? 32  PRO B O   1 
ATOM   2519 C  CB  . PRO B 2 33  ? 5.732   24.979 -10.113 1.00 27.30  ? 32  PRO B CB  1 
ATOM   2520 C  CG  . PRO B 2 33  ? 5.062   25.932 -11.059 1.00 30.50  ? 32  PRO B CG  1 
ATOM   2521 C  CD  . PRO B 2 33  ? 4.482   26.999 -10.166 1.00 30.23  ? 32  PRO B CD  1 
ATOM   2522 N  N   . SER B 2 34  ? 8.639   25.244 -9.566  1.00 21.04  ? 33  SER B N   1 
ATOM   2523 C  CA  . SER B 2 34  ? 10.109  25.429 -9.488  1.00 22.70  ? 33  SER B CA  1 
ATOM   2524 C  C   . SER B 2 34  ? 10.661  25.952 -10.821 1.00 24.85  ? 33  SER B C   1 
ATOM   2525 O  O   . SER B 2 34  ? 11.824  26.449 -10.849 1.00 25.96  ? 33  SER B O   1 
ATOM   2526 C  CB  . SER B 2 34  ? 10.808  24.169 -9.047  1.00 24.95  ? 33  SER B CB  1 
ATOM   2527 O  OG  . SER B 2 34  ? 10.634  23.112 -9.972  1.00 26.33  ? 33  SER B OG  1 
ATOM   2528 N  N   . ASP B 2 35  ? 9.934   25.779 -11.923 1.00 25.50  ? 34  ASP B N   1 
ATOM   2529 C  CA  . ASP B 2 35  ? 10.466  26.257 -13.225 1.00 24.65  ? 34  ASP B CA  1 
ATOM   2530 C  C   . ASP B 2 35  ? 10.519  27.783 -13.204 1.00 21.77  ? 34  ASP B C   1 
ATOM   2531 O  O   . ASP B 2 35  ? 9.564   28.416 -12.806 1.00 23.23  ? 34  ASP B O   1 
ATOM   2532 C  CB  . ASP B 2 35  ? 9.666   25.801 -14.436 1.00 28.20  ? 34  ASP B CB  1 
ATOM   2533 C  CG  . ASP B 2 35  ? 9.761   24.301 -14.679 1.00 39.38  ? 34  ASP B CG  1 
ATOM   2534 O  OD1 . ASP B 2 35  ? 10.829  23.715 -14.407 1.00 50.15  ? 34  ASP B OD1 1 
ATOM   2535 O  OD2 . ASP B 2 35  ? 8.784   23.750 -15.164 1.00 48.78  ? 34  ASP B OD2 1 
ATOM   2536 N  N   . ILE B 2 36  ? 11.646  28.329 -13.611 1.00 23.69  ? 35  ILE B N   1 
ATOM   2537 C  CA  . ILE B 2 36  ? 11.856  29.795 -13.573 1.00 21.68  ? 35  ILE B CA  1 
ATOM   2538 C  C   . ILE B 2 36  ? 12.947  30.133 -14.572 1.00 24.16  ? 35  ILE B C   1 
ATOM   2539 O  O   . ILE B 2 36  ? 13.805  29.273 -14.889 1.00 24.39  ? 35  ILE B O   1 
ATOM   2540 C  CB  . ILE B 2 36  ? 12.192  30.253 -12.137 1.00 20.26  ? 35  ILE B CB  1 
ATOM   2541 C  CG1 . ILE B 2 36  ? 12.096  31.771 -11.993 1.00 23.43  ? 35  ILE B CG1 1 
ATOM   2542 C  CG2 . ILE B 2 36  ? 13.539  29.704 -11.694 1.00 21.59  ? 35  ILE B CG2 1 
ATOM   2543 C  CD1 . ILE B 2 36  ? 11.839  32.255 -10.574 1.00 23.17  ? 35  ILE B CD1 1 
ATOM   2544 N  N   . GLU B 2 37  ? 12.926  31.364 -15.033 1.00 23.70  ? 36  GLU B N   1 
ATOM   2545 C  CA  . GLU B 2 37  ? 13.935  31.852 -15.981 1.00 23.16  ? 36  GLU B CA  1 
ATOM   2546 C  C   . GLU B 2 37  ? 14.497  33.166 -15.438 1.00 21.28  ? 36  GLU B C   1 
ATOM   2547 O  O   . GLU B 2 37  ? 13.725  34.038 -15.072 1.00 21.35  ? 36  GLU B O   1 
ATOM   2548 C  CB  . GLU B 2 37  ? 13.317  32.051 -17.348 1.00 23.17  ? 36  GLU B CB  1 
ATOM   2549 C  CG  . GLU B 2 37  ? 14.367  32.372 -18.368 1.00 28.90  ? 36  GLU B CG  1 
ATOM   2550 C  CD  . GLU B 2 37  ? 13.776  32.675 -19.734 1.00 39.59  ? 36  GLU B CD  1 
ATOM   2551 O  OE1 . GLU B 2 37  ? 12.505  32.777 -19.841 1.00 26.87  ? 36  GLU B OE1 1 
ATOM   2552 O  OE2 . GLU B 2 37  ? 14.589  32.751 -20.671 1.00 30.77  ? 36  GLU B OE2 1 
ATOM   2553 N  N   . VAL B 2 38  ? 15.821  33.281 -15.423 1.00 26.69  ? 37  VAL B N   1 
ATOM   2554 C  CA  . VAL B 2 38  ? 16.505  34.467 -14.843 1.00 22.85  ? 37  VAL B CA  1 
ATOM   2555 C  C   . VAL B 2 38  ? 17.594  34.904 -15.810 1.00 21.07  ? 37  VAL B C   1 
ATOM   2556 O  O   . VAL B 2 38  ? 18.407  34.055 -16.170 1.00 23.86  ? 37  VAL B O   1 
ATOM   2557 C  CB  . VAL B 2 38  ? 17.067  34.164 -13.442 1.00 24.05  ? 37  VAL B CB  1 
ATOM   2558 C  CG1 . VAL B 2 38  ? 17.765  35.400 -12.882 1.00 26.07  ? 37  VAL B CG1 1 
ATOM   2559 C  CG2 . VAL B 2 38  ? 15.980  33.661 -12.497 1.00 24.25  ? 37  VAL B CG2 1 
ATOM   2560 N  N   . ASP B 2 39  ? 17.537  36.167 -16.216 1.00 21.08  ? 38  ASP B N   1 
ATOM   2561 C  CA  . ASP B 2 39  ? 18.572  36.834 -17.031 1.00 22.95  ? 38  ASP B CA  1 
ATOM   2562 C  C   . ASP B 2 39  ? 19.126  38.015 -16.238 1.00 23.59  ? 38  ASP B C   1 
ATOM   2563 O  O   . ASP B 2 39  ? 18.357  38.743 -15.608 1.00 24.70  ? 38  ASP B O   1 
ATOM   2564 C  CB  . ASP B 2 39  ? 18.027  37.338 -18.363 1.00 26.88  ? 38  ASP B CB  1 
ATOM   2565 C  CG  . ASP B 2 39  ? 17.702  36.216 -19.339 1.00 26.43  ? 38  ASP B CG  1 
ATOM   2566 O  OD1 . ASP B 2 39  ? 18.485  35.237 -19.427 1.00 31.94  ? 38  ASP B OD1 1 
ATOM   2567 O  OD2 . ASP B 2 39  ? 16.697  36.348 -19.990 1.00 34.27  ? 38  ASP B OD2 1 
ATOM   2568 N  N   . LEU B 2 40  ? 20.426  38.211 -16.357 1.00 25.58  ? 39  LEU B N   1 
ATOM   2569 C  CA  . LEU B 2 40  ? 21.084  39.466 -15.940 1.00 23.77  ? 39  LEU B CA  1 
ATOM   2570 C  C   . LEU B 2 40  ? 21.247  40.362 -17.176 1.00 24.11  ? 39  LEU B C   1 
ATOM   2571 O  O   . LEU B 2 40  ? 21.673  39.854 -18.264 1.00 25.92  ? 39  LEU B O   1 
ATOM   2572 C  CB  . LEU B 2 40  ? 22.432  39.147 -15.274 1.00 25.60  ? 39  LEU B CB  1 
ATOM   2573 C  CG  . LEU B 2 40  ? 22.356  38.252 -14.039 1.00 26.04  ? 39  LEU B CG  1 
ATOM   2574 C  CD1 . LEU B 2 40  ? 23.722  37.963 -13.482 1.00 28.05  ? 39  LEU B CD1 1 
ATOM   2575 C  CD2 . LEU B 2 40  ? 21.460  38.867 -13.003 1.00 30.93  ? 39  LEU B CD2 1 
ATOM   2576 N  N   . LEU B 2 41  ? 20.935  41.645 -16.976 1.00 25.63  ? 40  LEU B N   1 
ATOM   2577 C  CA  . LEU B 2 41  ? 20.872  42.674 -18.042 1.00 26.08  ? 40  LEU B CA  1 
ATOM   2578 C  C   . LEU B 2 41  ? 21.971  43.702 -17.807 1.00 29.05  ? 40  LEU B C   1 
ATOM   2579 O  O   . LEU B 2 41  ? 22.167  44.121 -16.626 1.00 26.33  ? 40  LEU B O   1 
ATOM   2580 C  CB  . LEU B 2 41  ? 19.514  43.360 -17.998 1.00 25.99  ? 40  LEU B CB  1 
ATOM   2581 C  CG  . LEU B 2 41  ? 18.307  42.456 -18.245 1.00 23.37  ? 40  LEU B CG  1 
ATOM   2582 C  CD1 . LEU B 2 41  ? 17.130  43.303 -18.592 1.00 26.56  ? 40  LEU B CD1 1 
ATOM   2583 C  CD2 . LEU B 2 41  ? 18.550  41.425 -19.318 1.00 29.98  ? 40  LEU B CD2 1 
ATOM   2584 N  N   . LYS B 2 42  ? 22.673  44.058 -18.877 1.00 24.01  ? 41  LYS B N   1 
ATOM   2585 C  CA  . LYS B 2 42  ? 23.543  45.266 -18.866 1.00 25.53  ? 41  LYS B CA  1 
ATOM   2586 C  C   . LYS B 2 42  ? 22.967  46.261 -19.866 1.00 31.53  ? 41  LYS B C   1 
ATOM   2587 O  O   . LYS B 2 42  ? 22.824  45.871 -21.056 1.00 30.48  ? 41  LYS B O   1 
ATOM   2588 C  CB  . LYS B 2 42  ? 24.975  44.901 -19.206 1.00 28.51  ? 41  LYS B CB  1 
ATOM   2589 C  CG  . LYS B 2 42  ? 25.879  46.131 -19.299 1.00 31.07  ? 41  LYS B CG  1 
ATOM   2590 C  CD  . LYS B 2 42  ? 27.302  45.749 -19.614 1.00 35.49  ? 41  LYS B CD  1 
ATOM   2591 C  CE  . LYS B 2 42  ? 28.194  46.958 -19.813 1.00 42.93  ? 41  LYS B CE  1 
ATOM   2592 N  NZ  . LYS B 2 42  ? 29.593  46.505 -19.912 1.00 37.67  ? 41  LYS B NZ  1 
ATOM   2593 N  N   . ASN B 2 43  ? 22.540  47.429 -19.387 1.00 30.87  ? 42  ASN B N   1 
ATOM   2594 C  CA  . ASN B 2 43  ? 21.910  48.483 -20.226 1.00 38.42  ? 42  ASN B CA  1 
ATOM   2595 C  C   . ASN B 2 43  ? 20.810  47.819 -21.067 1.00 43.61  ? 42  ASN B C   1 
ATOM   2596 O  O   . ASN B 2 43  ? 20.712  48.114 -22.270 1.00 33.23  ? 42  ASN B O   1 
ATOM   2597 C  CB  . ASN B 2 43  ? 22.972  49.203 -21.062 1.00 33.12  ? 42  ASN B CB  1 
ATOM   2598 C  CG  . ASN B 2 43  ? 23.971  49.926 -20.182 1.00 31.21  ? 42  ASN B CG  1 
ATOM   2599 O  OD1 . ASN B 2 43  ? 23.567  50.687 -19.299 1.00 32.63  ? 42  ASN B OD1 1 
ATOM   2600 N  ND2 . ASN B 2 43  ? 25.255  49.656 -20.387 1.00 33.20  ? 42  ASN B ND2 1 
ATOM   2601 N  N   . GLY B 2 44  ? 20.027  46.928 -20.455 1.00 32.43  ? 43  GLY B N   1 
ATOM   2602 C  CA  . GLY B 2 44  ? 18.829  46.348 -21.078 1.00 36.72  ? 43  GLY B CA  1 
ATOM   2603 C  C   . GLY B 2 44  ? 19.125  45.140 -21.946 1.00 36.44  ? 43  GLY B C   1 
ATOM   2604 O  O   . GLY B 2 44  ? 18.157  44.479 -22.353 1.00 36.07  ? 43  GLY B O   1 
ATOM   2605 N  N   . GLU B 2 45  ? 20.388  44.802 -22.191 1.00 28.63  ? 44  GLU B N   1 
ATOM   2606 C  CA  . GLU B 2 45  ? 20.765  43.625 -23.010 1.00 32.61  ? 44  GLU B CA  1 
ATOM   2607 C  C   . GLU B 2 45  ? 21.158  42.436 -22.118 1.00 33.34  ? 44  GLU B C   1 
ATOM   2608 O  O   . GLU B 2 45  ? 21.884  42.617 -21.150 1.00 27.02  ? 44  GLU B O   1 
ATOM   2609 C  CB  . GLU B 2 45  ? 21.919  43.947 -23.959 1.00 37.36  ? 44  GLU B CB  1 
ATOM   2610 C  CG  . GLU B 2 45  ? 21.652  45.137 -24.880 1.00 53.62  ? 44  GLU B CG  1 
ATOM   2611 C  CD  . GLU B 2 45  ? 20.483  44.954 -25.835 1.00 70.70  ? 44  GLU B CD  1 
ATOM   2612 O  OE1 . GLU B 2 45  ? 19.837  45.964 -26.180 1.00 71.00  ? 44  GLU B OE1 1 
ATOM   2613 O  OE2 . GLU B 2 45  ? 20.209  43.797 -26.215 1.00 62.55  ? 44  GLU B OE2 1 
ATOM   2614 N  N   . ARG B 2 46  ? 20.721  41.241 -22.478 1.00 27.03  ? 45  ARG B N   1 
ATOM   2615 C  CA  . ARG B 2 46  ? 21.017  39.975 -21.751 1.00 24.53  ? 45  ARG B CA  1 
ATOM   2616 C  C   . ARG B 2 46  ? 22.523  39.715 -21.746 1.00 33.00  ? 45  ARG B C   1 
ATOM   2617 O  O   . ARG B 2 46  ? 23.151  39.757 -22.802 1.00 32.00  ? 45  ARG B O   1 
ATOM   2618 C  CB  . ARG B 2 46  ? 20.291  38.789 -22.401 1.00 38.08  ? 45  ARG B CB  1 
ATOM   2619 C  CG  . ARG B 2 46  ? 20.329  37.514 -21.566 1.00 37.01  ? 45  ARG B CG  1 
ATOM   2620 C  CD  . ARG B 2 46  ? 19.710  36.312 -22.284 1.00 49.19  ? 45  ARG B CD  1 
ATOM   2621 N  NE  . ARG B 2 46  ? 20.758  35.522 -22.927 1.00 69.03  ? 45  ARG B NE  1 
ATOM   2622 C  CZ  . ARG B 2 46  ? 21.532  34.616 -22.310 1.00 54.59  ? 45  ARG B CZ  1 
ATOM   2623 N  NH1 . ARG B 2 46  ? 22.481  33.991 -22.987 1.00 65.97  ? 45  ARG B NH1 1 
ATOM   2624 N  NH2 . ARG B 2 46  ? 21.347  34.323 -21.032 1.00 58.19  ? 45  ARG B NH2 1 
ATOM   2625 N  N   . ILE B 2 47  ? 23.091  39.455 -20.574 1.00 28.93  ? 46  ILE B N   1 
ATOM   2626 C  CA  . ILE B 2 47  ? 24.524  39.103 -20.397 1.00 28.44  ? 46  ILE B CA  1 
ATOM   2627 C  C   . ILE B 2 47  ? 24.618  37.623 -20.730 1.00 34.98  ? 46  ILE B C   1 
ATOM   2628 O  O   . ILE B 2 47  ? 23.795  36.846 -20.227 1.00 30.33  ? 46  ILE B O   1 
ATOM   2629 C  CB  . ILE B 2 47  ? 25.036  39.462 -18.978 1.00 31.99  ? 46  ILE B CB  1 
ATOM   2630 C  CG1 . ILE B 2 47  ? 24.916  40.967 -18.683 1.00 30.96  ? 46  ILE B CG1 1 
ATOM   2631 C  CG2 . ILE B 2 47  ? 26.476  38.984 -18.819 1.00 33.82  ? 46  ILE B CG2 1 
ATOM   2632 C  CD1 . ILE B 2 47  ? 25.160  41.360 -17.238 1.00 32.02  ? 46  ILE B CD1 1 
ATOM   2633 N  N   A GLU B 2 48  ? 25.647  37.218 -21.476 0.50 36.39  ? 47  GLU B N   1 
ATOM   2634 N  N   B GLU B 2 48  ? 25.518  37.282 -21.660 0.50 29.53  ? 47  GLU B N   1 
ATOM   2635 C  CA  A GLU B 2 48  ? 25.873  35.789 -21.800 0.50 36.45  ? 47  GLU B CA  1 
ATOM   2636 C  CA  B GLU B 2 48  ? 25.574  35.962 -22.331 0.50 31.61  ? 47  GLU B CA  1 
ATOM   2637 C  C   A GLU B 2 48  ? 26.766  35.131 -20.737 0.50 33.38  ? 47  GLU B C   1 
ATOM   2638 C  C   B GLU B 2 48  ? 26.025  34.870 -21.357 0.50 28.20  ? 47  GLU B C   1 
ATOM   2639 O  O   A GLU B 2 48  ? 27.490  35.857 -20.000 0.50 29.54  ? 47  GLU B O   1 
ATOM   2640 O  O   B GLU B 2 48  ? 25.353  33.827 -21.307 0.50 39.69  ? 47  GLU B O   1 
ATOM   2641 C  CB  A GLU B 2 48  ? 26.416  35.675 -23.222 0.50 55.26  ? 47  GLU B CB  1 
ATOM   2642 C  CB  B GLU B 2 48  ? 26.546  36.017 -23.509 0.50 40.10  ? 47  GLU B CB  1 
ATOM   2643 C  CG  A GLU B 2 48  ? 25.377  36.063 -24.256 0.50 58.72  ? 47  GLU B CG  1 
ATOM   2644 C  CG  B GLU B 2 48  ? 25.999  36.734 -24.726 0.50 40.95  ? 47  GLU B CG  1 
ATOM   2645 C  CD  A GLU B 2 48  ? 25.554  35.385 -25.599 0.50 72.28  ? 47  GLU B CD  1 
ATOM   2646 C  CD  B GLU B 2 48  ? 26.936  36.649 -25.922 0.50 39.16  ? 47  GLU B CD  1 
ATOM   2647 O  OE1 A GLU B 2 48  ? 26.255  34.349 -25.650 0.50 69.22  ? 47  GLU B OE1 1 
ATOM   2648 O  OE1 B GLU B 2 48  ? 27.584  35.577 -26.097 0.50 29.32  ? 47  GLU B OE1 1 
ATOM   2649 O  OE2 A GLU B 2 48  ? 24.992  35.898 -26.584 0.50 90.08  ? 47  GLU B OE2 1 
ATOM   2650 O  OE2 B GLU B 2 48  ? 27.051  37.662 -26.647 0.50 47.51  ? 47  GLU B OE2 1 
ATOM   2651 N  N   A LYS B 2 49  ? 26.647  33.805 -20.628 0.50 24.43  ? 48  LYS B N   1 
ATOM   2652 N  N   B LYS B 2 49  ? 27.147  35.093 -20.668 0.50 34.81  ? 48  LYS B N   1 
ATOM   2653 C  CA  A LYS B 2 49  ? 27.532  32.906 -19.846 0.50 32.04  ? 48  LYS B CA  1 
ATOM   2654 C  CA  B LYS B 2 49  ? 27.813  34.117 -19.769 0.50 30.09  ? 48  LYS B CA  1 
ATOM   2655 C  C   A LYS B 2 49  ? 27.351  33.190 -18.346 0.50 36.27  ? 48  LYS B C   1 
ATOM   2656 C  C   B LYS B 2 49  ? 27.298  34.306 -18.340 0.50 29.55  ? 48  LYS B C   1 
ATOM   2657 O  O   A LYS B 2 49  ? 28.253  32.842 -17.560 0.50 45.01  ? 48  LYS B O   1 
ATOM   2658 O  O   B LYS B 2 49  ? 27.911  35.128 -17.619 0.50 34.83  ? 48  LYS B O   1 
ATOM   2659 C  CB  A LYS B 2 49  ? 28.984  33.069 -20.310 0.50 45.65  ? 48  LYS B CB  1 
ATOM   2660 C  CB  B LYS B 2 49  ? 29.331  34.333 -19.759 0.50 35.31  ? 48  LYS B CB  1 
ATOM   2661 N  N   . VAL B 2 50  ? 26.169  33.685 -17.977 1.00 30.79  ? 49  VAL B N   1 
ATOM   2662 C  CA  . VAL B 2 50  ? 25.718  33.771 -16.568 1.00 25.62  ? 49  VAL B CA  1 
ATOM   2663 C  C   . VAL B 2 50  ? 25.604  32.347 -16.036 1.00 34.31  ? 49  VAL B C   1 
ATOM   2664 O  O   . VAL B 2 50  ? 25.068  31.490 -16.741 1.00 32.50  ? 49  VAL B O   1 
ATOM   2665 C  CB  . VAL B 2 50  ? 24.389  34.552 -16.486 1.00 29.62  ? 49  VAL B CB  1 
ATOM   2666 C  CG1 . VAL B 2 50  ? 23.733  34.444 -15.101 1.00 30.46  ? 49  VAL B CG1 1 
ATOM   2667 C  CG2 . VAL B 2 50  ? 24.576  36.011 -16.894 1.00 29.31  ? 49  VAL B CG2 1 
ATOM   2668 N  N   . GLU B 2 51  ? 26.051  32.116 -14.810 1.00 25.87  ? 50  GLU B N   1 
ATOM   2669 C  CA  . GLU B 2 51  ? 25.967  30.790 -14.159 1.00 26.83  ? 50  GLU B CA  1 
ATOM   2670 C  C   . GLU B 2 51  ? 24.868  30.864 -13.101 1.00 26.35  ? 50  GLU B C   1 
ATOM   2671 O  O   . GLU B 2 51  ? 24.448  31.973 -12.695 1.00 26.00  ? 50  GLU B O   1 
ATOM   2672 C  CB  . GLU B 2 51  ? 27.315  30.408 -13.541 1.00 34.20  ? 50  GLU B CB  1 
ATOM   2673 C  CG  . GLU B 2 51  ? 28.428  30.282 -14.574 1.00 43.60  ? 50  GLU B CG  1 
ATOM   2674 C  CD  . GLU B 2 51  ? 29.775  30.059 -13.921 1.00 56.97  ? 50  GLU B CD  1 
ATOM   2675 O  OE1 . GLU B 2 51  ? 30.521  31.048 -13.721 1.00 64.33  ? 50  GLU B OE1 1 
ATOM   2676 O  OE2 . GLU B 2 51  ? 30.042  28.906 -13.563 1.00 65.40  ? 50  GLU B OE2 1 
ATOM   2677 N  N   . HIS B 2 52  ? 24.400  29.710 -12.669 1.00 27.48  ? 51  HIS B N   1 
ATOM   2678 C  CA  . HIS B 2 52  ? 23.407  29.623 -11.575 1.00 26.00  ? 51  HIS B CA  1 
ATOM   2679 C  C   . HIS B 2 52  ? 23.729  28.424 -10.691 1.00 28.89  ? 51  HIS B C   1 
ATOM   2680 O  O   . HIS B 2 52  ? 24.477  27.511 -11.101 1.00 26.88  ? 51  HIS B O   1 
ATOM   2681 C  CB  . HIS B 2 52  ? 21.989  29.562 -12.140 1.00 24.34  ? 51  HIS B CB  1 
ATOM   2682 C  CG  . HIS B 2 52  ? 21.814  28.427 -13.094 1.00 26.66  ? 51  HIS B CG  1 
ATOM   2683 N  ND1 . HIS B 2 52  ? 21.534  27.137 -12.661 1.00 30.37  ? 51  HIS B ND1 1 
ATOM   2684 C  CD2 . HIS B 2 52  ? 21.968  28.361 -14.430 1.00 31.09  ? 51  HIS B CD2 1 
ATOM   2685 C  CE1 . HIS B 2 52  ? 21.465  26.331 -13.700 1.00 36.23  ? 51  HIS B CE1 1 
ATOM   2686 N  NE2 . HIS B 2 52  ? 21.787  27.046 -14.800 1.00 33.81  ? 51  HIS B NE2 1 
ATOM   2687 N  N   . SER B 2 53  ? 23.115  28.437 -9.522  1.00 29.45  ? 52  SER B N   1 
ATOM   2688 C  CA  . SER B 2 53  ? 23.216  27.358 -8.517  1.00 29.55  ? 52  SER B CA  1 
ATOM   2689 C  C   . SER B 2 53  ? 22.283  26.214 -8.905  1.00 24.99  ? 52  SER B C   1 
ATOM   2690 O  O   . SER B 2 53  ? 21.424  26.382 -9.771  1.00 27.16  ? 52  SER B O   1 
ATOM   2691 C  CB  . SER B 2 53  ? 22.874  27.880 -7.147  1.00 23.18  ? 52  SER B CB  1 
ATOM   2692 O  OG  . SER B 2 53  ? 21.574  28.431 -7.154  1.00 25.22  ? 52  SER B OG  1 
ATOM   2693 N  N   . ASP B 2 54  ? 22.456  25.095 -8.226  1.00 24.30  ? 53  ASP B N   1 
ATOM   2694 C  CA  . ASP B 2 54  ? 21.583  23.917 -8.359  1.00 26.47  ? 53  ASP B CA  1 
ATOM   2695 C  C   . ASP B 2 54  ? 20.294  24.227 -7.618  1.00 28.19  ? 53  ASP B C   1 
ATOM   2696 O  O   . ASP B 2 54  ? 20.379  24.824 -6.531  1.00 28.31  ? 53  ASP B O   1 
ATOM   2697 C  CB  . ASP B 2 54  ? 22.262  22.691 -7.757  1.00 21.63  ? 53  ASP B CB  1 
ATOM   2698 C  CG  . ASP B 2 54  ? 23.654  22.442 -8.323  1.00 26.01  ? 53  ASP B CG  1 
ATOM   2699 O  OD1 . ASP B 2 54  ? 23.817  22.629 -9.552  1.00 25.17  ? 53  ASP B OD1 1 
ATOM   2700 O  OD2 . ASP B 2 54  ? 24.566  22.071 -7.530  1.00 25.82  ? 53  ASP B OD2 1 
ATOM   2701 N  N   . LEU B 2 55  ? 19.162  23.734 -8.115  1.00 23.39  ? 54  LEU B N   1 
ATOM   2702 C  CA  . LEU B 2 55  ? 17.865  23.958 -7.450  1.00 24.63  ? 54  LEU B CA  1 
ATOM   2703 C  C   . LEU B 2 55  ? 17.926  23.403 -6.029  1.00 24.55  ? 54  LEU B C   1 
ATOM   2704 O  O   . LEU B 2 55  ? 18.224  22.196 -5.810  1.00 25.16  ? 54  LEU B O   1 
ATOM   2705 C  CB  . LEU B 2 55  ? 16.723  23.320 -8.240  1.00 25.40  ? 54  LEU B CB  1 
ATOM   2706 C  CG  . LEU B 2 55  ? 15.342  23.587 -7.648  1.00 22.53  ? 54  LEU B CG  1 
ATOM   2707 C  CD1 . LEU B 2 55  ? 15.007  25.071 -7.653  1.00 25.26  ? 54  LEU B CD1 1 
ATOM   2708 C  CD2 . LEU B 2 55  ? 14.294  22.803 -8.411  1.00 25.83  ? 54  LEU B CD2 1 
ATOM   2709 N  N   . SER B 2 56  ? 17.590  24.253 -5.078  1.00 23.15  ? 55  SER B N   1 
ATOM   2710 C  CA  . SER B 2 56  ? 17.549  23.886 -3.649  1.00 25.30  ? 55  SER B CA  1 
ATOM   2711 C  C   . SER B 2 56  ? 16.315  24.550 -3.057  1.00 25.55  ? 55  SER B C   1 
ATOM   2712 O  O   . SER B 2 56  ? 15.633  25.308 -3.787  1.00 22.85  ? 55  SER B O   1 
ATOM   2713 C  CB  . SER B 2 56  ? 18.817  24.322 -2.936  1.00 29.05  ? 55  SER B CB  1 
ATOM   2714 O  OG  . SER B 2 56  ? 18.838  23.809 -1.615  1.00 27.57  ? 55  SER B OG  1 
ATOM   2715 N  N   . PHE B 2 57  ? 16.061  24.297 -1.790  1.00 19.46  ? 56  PHE B N   1 
ATOM   2716 C  CA  . PHE B 2 57  ? 14.979  24.968 -1.043  1.00 22.61  ? 56  PHE B CA  1 
ATOM   2717 C  C   . PHE B 2 57  ? 15.364  25.015 0.428   1.00 27.26  ? 56  PHE B C   1 
ATOM   2718 O  O   . PHE B 2 57  ? 16.231  24.235 0.854   1.00 24.12  ? 56  PHE B O   1 
ATOM   2719 C  CB  . PHE B 2 57  ? 13.643  24.261 -1.284  1.00 23.04  ? 56  PHE B CB  1 
ATOM   2720 C  CG  . PHE B 2 57  ? 13.625  22.771 -1.054  1.00 21.27  ? 56  PHE B CG  1 
ATOM   2721 C  CD1 . PHE B 2 57  ? 13.362  22.270 0.205   1.00 22.52  ? 56  PHE B CD1 1 
ATOM   2722 C  CD2 . PHE B 2 57  ? 13.829  21.878 -2.091  1.00 20.26  ? 56  PHE B CD2 1 
ATOM   2723 C  CE1 . PHE B 2 57  ? 13.256  20.903 0.430   1.00 22.26  ? 56  PHE B CE1 1 
ATOM   2724 C  CE2 . PHE B 2 57  ? 13.767  20.509 -1.867  1.00 22.23  ? 56  PHE B CE2 1 
ATOM   2725 C  CZ  . PHE B 2 57  ? 13.499  20.028 -0.600  1.00 26.09  ? 56  PHE B CZ  1 
ATOM   2726 N  N   . SER B 2 58  ? 14.731  25.920 1.156   1.00 21.17  ? 57  SER B N   1 
ATOM   2727 C  CA  . SER B 2 58  ? 14.959  26.100 2.610   1.00 22.86  ? 57  SER B CA  1 
ATOM   2728 C  C   . SER B 2 58  ? 14.064  25.118 3.348   1.00 25.25  ? 57  SER B C   1 
ATOM   2729 O  O   . SER B 2 58  ? 13.158  24.502 2.728   1.00 22.11  ? 57  SER B O   1 
ATOM   2730 C  CB  . SER B 2 58  ? 14.673  27.508 3.047   1.00 29.11  ? 57  SER B CB  1 
ATOM   2731 O  OG  . SER B 2 58  ? 15.212  28.431 2.132   1.00 35.35  ? 57  SER B OG  1 
ATOM   2732 N  N   . LYS B 2 59  ? 14.232  25.042 4.660   1.00 24.39  ? 58  LYS B N   1 
ATOM   2733 C  CA  . LYS B 2 59  ? 13.470  24.097 5.496   1.00 29.18  ? 58  LYS B CA  1 
ATOM   2734 C  C   . LYS B 2 59  ? 11.974  24.411 5.392   1.00 23.11  ? 58  LYS B C   1 
ATOM   2735 O  O   . LYS B 2 59  ? 11.172  23.505 5.565   1.00 25.35  ? 58  LYS B O   1 
ATOM   2736 C  CB  . LYS B 2 59  ? 13.983  24.204 6.933   1.00 34.09  ? 58  LYS B CB  1 
ATOM   2737 C  CG  . LYS B 2 59  ? 13.360  23.243 7.928   1.00 52.59  ? 58  LYS B CG  1 
ATOM   2738 C  CD  . LYS B 2 59  ? 13.872  23.481 9.347   1.00 59.91  ? 58  LYS B CD  1 
ATOM   2739 C  CE  . LYS B 2 59  ? 13.205  22.586 10.367  1.00 66.83  ? 58  LYS B CE  1 
ATOM   2740 N  NZ  . LYS B 2 59  ? 11.779  22.349 10.034  1.00 68.39  ? 58  LYS B NZ  1 
ATOM   2741 N  N   . ASP B 2 60  ? 11.597  25.658 5.105   1.00 25.26  ? 59  ASP B N   1 
ATOM   2742 C  CA  . ASP B 2 60  ? 10.175  26.066 4.952   1.00 28.45  ? 59  ASP B CA  1 
ATOM   2743 C  C   . ASP B 2 60  ? 9.684   25.830 3.506   1.00 22.85  ? 59  ASP B C   1 
ATOM   2744 O  O   . ASP B 2 60  ? 8.562   26.292 3.179   1.00 24.92  ? 59  ASP B O   1 
ATOM   2745 C  CB  . ASP B 2 60  ? 10.025  27.541 5.337   1.00 31.25  ? 59  ASP B CB  1 
ATOM   2746 C  CG  . ASP B 2 60  ? 10.737  28.472 4.370   1.00 38.84  ? 59  ASP B CG  1 
ATOM   2747 O  OD1 . ASP B 2 60  ? 11.360  27.970 3.415   1.00 34.92  ? 59  ASP B OD1 1 
ATOM   2748 O  OD2 . ASP B 2 60  ? 10.633  29.682 4.548   1.00 34.52  ? 59  ASP B OD2 1 
ATOM   2749 N  N   . TRP B 2 61  ? 10.464  25.143 2.672   1.00 22.31  ? 60  TRP B N   1 
ATOM   2750 C  CA  . TRP B 2 61  ? 10.081  24.644 1.321   1.00 21.28  ? 60  TRP B CA  1 
ATOM   2751 C  C   . TRP B 2 61  ? 10.267  25.738 0.259   1.00 24.91  ? 60  TRP B C   1 
ATOM   2752 O  O   . TRP B 2 61  ? 9.967   25.459 -0.915  1.00 21.40  ? 60  TRP B O   1 
ATOM   2753 C  CB  . TRP B 2 61  ? 8.641   24.073 1.267   1.00 27.66  ? 60  TRP B CB  1 
ATOM   2754 C  CG  . TRP B 2 61  ? 8.342   23.006 2.290   1.00 28.93  ? 60  TRP B CG  1 
ATOM   2755 C  CD1 . TRP B 2 61  ? 7.425   23.072 3.304   1.00 29.46  ? 60  TRP B CD1 1 
ATOM   2756 C  CD2 . TRP B 2 61  ? 8.990   21.727 2.426   1.00 24.94  ? 60  TRP B CD2 1 
ATOM   2757 N  NE1 . TRP B 2 61  ? 7.427   21.919 4.042   1.00 27.77  ? 60  TRP B NE1 1 
ATOM   2758 C  CE2 . TRP B 2 61  ? 8.378   21.066 3.511   1.00 27.64  ? 60  TRP B CE2 1 
ATOM   2759 C  CE3 . TRP B 2 61  ? 9.976   21.052 1.695   1.00 29.24  ? 60  TRP B CE3 1 
ATOM   2760 C  CZ2 . TRP B 2 61  ? 8.762   19.780 3.907   1.00 24.15  ? 60  TRP B CZ2 1 
ATOM   2761 C  CZ3 . TRP B 2 61  ? 10.321  19.760 2.050   1.00 26.15  ? 60  TRP B CZ3 1 
ATOM   2762 C  CH2 . TRP B 2 61  ? 9.730   19.143 3.158   1.00 23.38  ? 60  TRP B CH2 1 
ATOM   2763 N  N   . SER B 2 62  ? 10.826  26.898 0.639   1.00 24.20  ? 61  SER B N   1 
ATOM   2764 C  CA  . SER B 2 62  ? 11.052  28.029 -0.279  1.00 23.74  ? 61  SER B CA  1 
ATOM   2765 C  C   . SER B 2 62  ? 12.176  27.616 -1.223  1.00 23.41  ? 61  SER B C   1 
ATOM   2766 O  O   . SER B 2 62  ? 13.309  27.470 -0.762  1.00 23.58  ? 61  SER B O   1 
ATOM   2767 C  CB  . SER B 2 62  ? 11.267  29.333 0.455   1.00 24.11  ? 61  SER B CB  1 
ATOM   2768 O  OG  . SER B 2 62  ? 11.854  30.285 -0.412  1.00 28.58  ? 61  SER B OG  1 
ATOM   2769 N  N   . PHE B 2 63  ? 11.851  27.375 -2.503  1.00 19.27  ? 62  PHE B N   1 
ATOM   2770 C  CA  . PHE B 2 63  ? 12.873  27.159 -3.553  1.00 18.77  ? 62  PHE B CA  1 
ATOM   2771 C  C   . PHE B 2 63  ? 13.742  28.413 -3.621  1.00 25.55  ? 62  PHE B C   1 
ATOM   2772 O  O   . PHE B 2 63  ? 13.186  29.526 -3.444  1.00 23.54  ? 62  PHE B O   1 
ATOM   2773 C  CB  . PHE B 2 63  ? 12.267  26.931 -4.938  1.00 20.83  ? 62  PHE B CB  1 
ATOM   2774 C  CG  . PHE B 2 63  ? 11.681  25.549 -5.124  1.00 22.96  ? 62  PHE B CG  1 
ATOM   2775 C  CD1 . PHE B 2 63  ? 12.499  24.432 -5.105  1.00 24.62  ? 62  PHE B CD1 1 
ATOM   2776 C  CD2 . PHE B 2 63  ? 10.320  25.366 -5.272  1.00 23.60  ? 62  PHE B CD2 1 
ATOM   2777 C  CE1 . PHE B 2 63  ? 11.969  23.155 -5.250  1.00 25.26  ? 62  PHE B CE1 1 
ATOM   2778 C  CE2 . PHE B 2 63  ? 9.808   24.096 -5.503  1.00 25.53  ? 62  PHE B CE2 1 
ATOM   2779 C  CZ  . PHE B 2 63  ? 10.628  22.996 -5.456  1.00 24.55  ? 62  PHE B CZ  1 
ATOM   2780 N  N   . TYR B 2 64  ? 14.995  28.241 -4.015  1.00 22.72  ? 63  TYR B N   1 
ATOM   2781 C  CA  . TYR B 2 64  ? 15.907  29.379 -4.276  1.00 24.13  ? 63  TYR B CA  1 
ATOM   2782 C  C   . TYR B 2 64  ? 16.940  28.980 -5.320  1.00 22.52  ? 63  TYR B C   1 
ATOM   2783 O  O   . TYR B 2 64  ? 17.382  27.838 -5.336  1.00 22.94  ? 63  TYR B O   1 
ATOM   2784 C  CB  . TYR B 2 64  ? 16.485  29.919 -2.966  1.00 19.03  ? 63  TYR B CB  1 
ATOM   2785 C  CG  . TYR B 2 64  ? 17.373  28.970 -2.204  1.00 21.44  ? 63  TYR B CG  1 
ATOM   2786 C  CD1 . TYR B 2 64  ? 18.718  28.836 -2.514  1.00 23.54  ? 63  TYR B CD1 1 
ATOM   2787 C  CD2 . TYR B 2 64  ? 16.866  28.244 -1.137  1.00 26.03  ? 63  TYR B CD2 1 
ATOM   2788 C  CE1 . TYR B 2 64  ? 19.532  27.956 -1.813  1.00 25.20  ? 63  TYR B CE1 1 
ATOM   2789 C  CE2 . TYR B 2 64  ? 17.662  27.367 -0.417  1.00 25.11  ? 63  TYR B CE2 1 
ATOM   2790 C  CZ  . TYR B 2 64  ? 19.002  27.240 -0.752  1.00 24.60  ? 63  TYR B CZ  1 
ATOM   2791 O  OH  . TYR B 2 64  ? 19.796  26.381 -0.066  1.00 24.66  ? 63  TYR B OH  1 
ATOM   2792 N  N   . LEU B 2 65  ? 17.354  29.981 -6.096  1.00 21.89  ? 64  LEU B N   1 
ATOM   2793 C  CA  . LEU B 2 65  ? 18.468  29.924 -7.048  1.00 21.84  ? 64  LEU B CA  1 
ATOM   2794 C  C   . LEU B 2 65  ? 19.233  31.235 -6.977  1.00 20.09  ? 64  LEU B C   1 
ATOM   2795 O  O   . LEU B 2 65  ? 18.585  32.292 -6.830  1.00 18.97  ? 64  LEU B O   1 
ATOM   2796 C  CB  . LEU B 2 65  ? 17.943  29.720 -8.472  1.00 23.59  ? 64  LEU B CB  1 
ATOM   2797 C  CG  . LEU B 2 65  ? 17.259  28.382 -8.732  1.00 27.23  ? 64  LEU B CG  1 
ATOM   2798 C  CD1 . LEU B 2 65  ? 16.481  28.454 -10.032 1.00 27.08  ? 64  LEU B CD1 1 
ATOM   2799 C  CD2 . LEU B 2 65  ? 18.262  27.255 -8.781  1.00 25.20  ? 64  LEU B CD2 1 
ATOM   2800 N  N   . LEU B 2 66  ? 20.549  31.137 -7.158  1.00 22.70  ? 65  LEU B N   1 
ATOM   2801 C  CA  . LEU B 2 66  ? 21.455  32.270 -7.385  1.00 22.70  ? 65  LEU B CA  1 
ATOM   2802 C  C   . LEU B 2 66  ? 21.955  32.213 -8.826  1.00 25.49  ? 65  LEU B C   1 
ATOM   2803 O  O   . LEU B 2 66  ? 22.540  31.182 -9.224  1.00 23.99  ? 65  LEU B O   1 
ATOM   2804 C  CB  . LEU B 2 66  ? 22.638  32.153 -6.432  1.00 22.76  ? 65  LEU B CB  1 
ATOM   2805 C  CG  . LEU B 2 66  ? 23.614  33.320 -6.533  1.00 22.38  ? 65  LEU B CG  1 
ATOM   2806 C  CD1 . LEU B 2 66  ? 22.938  34.626 -6.203  1.00 25.51  ? 65  LEU B CD1 1 
ATOM   2807 C  CD2 . LEU B 2 66  ? 24.789  33.082 -5.608  1.00 22.22  ? 65  LEU B CD2 1 
ATOM   2808 N  N   . TYR B 2 67  ? 21.759  33.311 -9.536  1.00 23.52  ? 66  TYR B N   1 
ATOM   2809 C  CA  . TYR B 2 67  ? 22.353  33.568 -10.859 1.00 23.92  ? 66  TYR B CA  1 
ATOM   2810 C  C   . TYR B 2 67  ? 23.414  34.651 -10.712 1.00 20.85  ? 66  TYR B C   1 
ATOM   2811 O  O   . TYR B 2 67  ? 23.181  35.621 -10.027 1.00 21.03  ? 66  TYR B O   1 
ATOM   2812 C  CB  . TYR B 2 67  ? 21.302  34.069 -11.848 1.00 27.40  ? 66  TYR B CB  1 
ATOM   2813 C  CG  . TYR B 2 67  ? 20.392  32.970 -12.321 1.00 22.83  ? 66  TYR B CG  1 
ATOM   2814 C  CD1 . TYR B 2 67  ? 19.436  32.441 -11.479 1.00 26.85  ? 66  TYR B CD1 1 
ATOM   2815 C  CD2 . TYR B 2 67  ? 20.496  32.448 -13.607 1.00 25.65  ? 66  TYR B CD2 1 
ATOM   2816 C  CE1 . TYR B 2 67  ? 18.598  31.414 -11.907 1.00 28.07  ? 66  TYR B CE1 1 
ATOM   2817 C  CE2 . TYR B 2 67  ? 19.644  31.447 -14.056 1.00 25.38  ? 66  TYR B CE2 1 
ATOM   2818 C  CZ  . TYR B 2 67  ? 18.713  30.911 -13.195 1.00 31.20  ? 66  TYR B CZ  1 
ATOM   2819 O  OH  . TYR B 2 67  ? 17.901  29.905 -13.625 1.00 29.21  ? 66  TYR B OH  1 
ATOM   2820 N  N   . TYR B 2 68  ? 24.556  34.473 -11.367 1.00 23.11  ? 67  TYR B N   1 
ATOM   2821 C  CA  . TYR B 2 68  ? 25.710  35.352 -11.097 1.00 24.74  ? 67  TYR B CA  1 
ATOM   2822 C  C   . TYR B 2 68  ? 26.652  35.392 -12.295 1.00 27.16  ? 67  TYR B C   1 
ATOM   2823 O  O   . TYR B 2 68  ? 26.713  34.467 -13.122 1.00 26.34  ? 67  TYR B O   1 
ATOM   2824 C  CB  . TYR B 2 68  ? 26.454  34.912 -9.825  1.00 26.35  ? 67  TYR B CB  1 
ATOM   2825 C  CG  . TYR B 2 68  ? 26.964  33.493 -9.852  1.00 23.77  ? 67  TYR B CG  1 
ATOM   2826 C  CD1 . TYR B 2 68  ? 26.131  32.464 -9.454  1.00 30.90  ? 67  TYR B CD1 1 
ATOM   2827 C  CD2 . TYR B 2 68  ? 28.233  33.163 -10.309 1.00 29.84  ? 67  TYR B CD2 1 
ATOM   2828 C  CE1 . TYR B 2 68  ? 26.534  31.142 -9.486  1.00 31.14  ? 67  TYR B CE1 1 
ATOM   2829 C  CE2 . TYR B 2 68  ? 28.667  31.847 -10.313 1.00 31.37  ? 67  TYR B CE2 1 
ATOM   2830 C  CZ  . TYR B 2 68  ? 27.807  30.831 -9.909  1.00 35.62  ? 67  TYR B CZ  1 
ATOM   2831 O  OH  . TYR B 2 68  ? 28.141  29.502 -9.910  1.00 39.63  ? 67  TYR B OH  1 
ATOM   2832 N  N   . THR B 2 69  ? 27.338  36.518 -12.386 1.00 25.98  ? 68  THR B N   1 
ATOM   2833 C  CA  . THR B 2 69  ? 28.379  36.769 -13.383 1.00 30.22  ? 68  THR B CA  1 
ATOM   2834 C  C   . THR B 2 69  ? 29.382  37.788 -12.825 1.00 27.63  ? 68  THR B C   1 
ATOM   2835 O  O   . THR B 2 69  ? 28.983  38.684 -12.030 1.00 28.77  ? 68  THR B O   1 
ATOM   2836 C  CB  . THR B 2 69  ? 27.748  37.261 -14.686 1.00 27.56  ? 68  THR B CB  1 
ATOM   2837 O  OG1 . THR B 2 69  ? 28.835  37.199 -15.602 1.00 36.45  ? 68  THR B OG1 1 
ATOM   2838 C  CG2 . THR B 2 69  ? 27.179  38.658 -14.610 1.00 31.26  ? 68  THR B CG2 1 
ATOM   2839 N  N   . GLU B 2 70  ? 30.617  37.719 -13.316 1.00 29.01  ? 69  GLU B N   1 
ATOM   2840 C  CA  . GLU B 2 70  ? 31.627  38.793 -13.107 1.00 31.98  ? 69  GLU B CA  1 
ATOM   2841 C  C   . GLU B 2 70  ? 31.137  40.080 -13.762 1.00 36.35  ? 69  GLU B C   1 
ATOM   2842 O  O   . GLU B 2 70  ? 30.497  40.023 -14.801 1.00 34.21  ? 69  GLU B O   1 
ATOM   2843 C  CB  . GLU B 2 70  ? 32.976  38.386 -13.694 1.00 52.54  ? 69  GLU B CB  1 
ATOM   2844 C  CG  . GLU B 2 70  ? 33.576  37.170 -13.019 1.00 70.18  ? 69  GLU B CG  1 
ATOM   2845 C  CD  . GLU B 2 70  ? 35.097  37.107 -12.986 1.00 100.43 ? 69  GLU B CD  1 
ATOM   2846 O  OE1 . GLU B 2 70  ? 35.725  38.070 -12.487 1.00 97.76  ? 69  GLU B OE1 1 
ATOM   2847 O  OE2 . GLU B 2 70  ? 35.652  36.086 -13.444 1.00 85.30  ? 69  GLU B OE2 1 
ATOM   2848 N  N   . PHE B 2 71  ? 31.381  41.228 -13.151 1.00 30.23  ? 70  PHE B N   1 
ATOM   2849 C  CA  . PHE B 2 71  ? 31.096  42.532 -13.784 1.00 29.87  ? 70  PHE B CA  1 
ATOM   2850 C  C   . PHE B 2 71  ? 31.964  43.612 -13.123 1.00 35.71  ? 70  PHE B C   1 
ATOM   2851 O  O   . PHE B 2 71  ? 32.393  43.463 -11.981 1.00 31.64  ? 70  PHE B O   1 
ATOM   2852 C  CB  . PHE B 2 71  ? 29.608  42.855 -13.723 1.00 28.60  ? 70  PHE B CB  1 
ATOM   2853 C  CG  . PHE B 2 71  ? 29.134  43.512 -12.448 1.00 29.81  ? 70  PHE B CG  1 
ATOM   2854 C  CD1 . PHE B 2 71  ? 29.449  42.985 -11.203 1.00 25.50  ? 70  PHE B CD1 1 
ATOM   2855 C  CD2 . PHE B 2 71  ? 28.297  44.610 -12.499 1.00 29.08  ? 70  PHE B CD2 1 
ATOM   2856 C  CE1 . PHE B 2 71  ? 28.945  43.579 -10.052 1.00 28.65  ? 70  PHE B CE1 1 
ATOM   2857 C  CE2 . PHE B 2 71  ? 27.807  45.202 -11.346 1.00 28.48  ? 70  PHE B CE2 1 
ATOM   2858 C  CZ  . PHE B 2 71  ? 28.134  44.682 -10.121 1.00 31.15  ? 70  PHE B CZ  1 
ATOM   2859 N  N   . THR B 2 72  ? 32.209  44.683 -13.855 1.00 30.07  ? 71  THR B N   1 
ATOM   2860 C  CA  . THR B 2 72  ? 32.946  45.861 -13.380 1.00 29.57  ? 71  THR B CA  1 
ATOM   2861 C  C   . THR B 2 72  ? 31.980  47.024 -13.407 1.00 29.92  ? 71  THR B C   1 
ATOM   2862 O  O   . THR B 2 72  ? 31.805  47.652 -14.434 1.00 38.25  ? 71  THR B O   1 
ATOM   2863 C  CB  . THR B 2 72  ? 34.191  46.096 -14.231 1.00 38.00  ? 71  THR B CB  1 
ATOM   2864 O  OG1 . THR B 2 72  ? 35.029  44.947 -14.069 1.00 35.91  ? 71  THR B OG1 1 
ATOM   2865 C  CG2 . THR B 2 72  ? 34.920  47.364 -13.832 1.00 35.53  ? 71  THR B CG2 1 
ATOM   2866 N  N   . PRO B 2 73  ? 31.312  47.362 -12.290 1.00 29.47  ? 72  PRO B N   1 
ATOM   2867 C  CA  . PRO B 2 73  ? 30.330  48.437 -12.314 1.00 30.04  ? 72  PRO B CA  1 
ATOM   2868 C  C   . PRO B 2 73  ? 31.012  49.767 -12.655 1.00 30.70  ? 72  PRO B C   1 
ATOM   2869 O  O   . PRO B 2 73  ? 32.179  49.922 -12.392 1.00 32.08  ? 72  PRO B O   1 
ATOM   2870 C  CB  . PRO B 2 73  ? 29.787  48.477 -10.880 1.00 41.29  ? 72  PRO B CB  1 
ATOM   2871 C  CG  . PRO B 2 73  ? 30.920  47.907 -10.071 1.00 31.52  ? 72  PRO B CG  1 
ATOM   2872 C  CD  . PRO B 2 73  ? 31.514  46.819 -10.948 1.00 31.92  ? 72  PRO B CD  1 
ATOM   2873 N  N   . THR B 2 74  ? 30.252  50.691 -13.218 1.00 30.50  ? 73  THR B N   1 
ATOM   2874 C  CA  . THR B 2 74  ? 30.711  52.040 -13.613 1.00 37.25  ? 73  THR B CA  1 
ATOM   2875 C  C   . THR B 2 74  ? 29.654  53.001 -13.094 1.00 40.15  ? 73  THR B C   1 
ATOM   2876 O  O   . THR B 2 74  ? 28.645  52.530 -12.544 1.00 35.84  ? 73  THR B O   1 
ATOM   2877 C  CB  . THR B 2 74  ? 30.915  52.132 -15.133 1.00 38.20  ? 73  THR B CB  1 
ATOM   2878 O  OG1 . THR B 2 74  ? 29.600  51.981 -15.668 1.00 37.01  ? 73  THR B OG1 1 
ATOM   2879 C  CG2 . THR B 2 74  ? 31.858  51.080 -15.682 1.00 34.19  ? 73  THR B CG2 1 
ATOM   2880 N  N   . GLU B 2 75  ? 29.846  54.295 -13.292 1.00 33.10  ? 74  GLU B N   1 
ATOM   2881 C  CA  . GLU B 2 75  ? 28.864  55.297 -12.833 1.00 33.53  ? 74  GLU B CA  1 
ATOM   2882 C  C   . GLU B 2 75  ? 27.569  55.136 -13.624 1.00 37.80  ? 74  GLU B C   1 
ATOM   2883 O  O   . GLU B 2 75  ? 26.498  55.345 -13.020 1.00 37.76  ? 74  GLU B O   1 
ATOM   2884 C  CB  . GLU B 2 75  ? 29.365  56.734 -13.016 1.00 34.42  ? 74  GLU B CB  1 
ATOM   2885 C  CG  . GLU B 2 75  ? 28.505  57.770 -12.307 1.00 49.17  ? 74  GLU B CG  1 
ATOM   2886 C  CD  . GLU B 2 75  ? 28.843  59.213 -12.676 1.00 76.78  ? 74  GLU B CD  1 
ATOM   2887 O  OE1 . GLU B 2 75  ? 30.021  59.470 -13.006 1.00 52.71  ? 74  GLU B OE1 1 
ATOM   2888 O  OE2 . GLU B 2 75  ? 27.929  60.079 -12.644 1.00 73.00  ? 74  GLU B OE2 1 
ATOM   2889 N  N   . LYS B 2 76  ? 27.677  54.832 -14.918 1.00 30.20  ? 75  LYS B N   1 
ATOM   2890 C  CA  . LYS B 2 76  ? 26.599  55.130 -15.901 1.00 39.54  ? 75  LYS B CA  1 
ATOM   2891 C  C   . LYS B 2 76  ? 25.937  53.827 -16.364 1.00 34.68  ? 75  LYS B C   1 
ATOM   2892 O  O   . LYS B 2 76  ? 24.768  53.918 -16.734 1.00 39.32  ? 75  LYS B O   1 
ATOM   2893 C  CB  . LYS B 2 76  ? 27.129  55.900 -17.121 1.00 54.56  ? 75  LYS B CB  1 
ATOM   2894 C  CG  . LYS B 2 76  ? 27.749  57.272 -16.852 1.00 68.01  ? 75  LYS B CG  1 
ATOM   2895 C  CD  . LYS B 2 76  ? 26.771  58.430 -16.664 1.00 71.20  ? 75  LYS B CD  1 
ATOM   2896 C  CE  . LYS B 2 76  ? 26.087  58.420 -15.311 1.00 84.35  ? 75  LYS B CE  1 
ATOM   2897 N  NZ  . LYS B 2 76  ? 25.570  59.755 -14.927 1.00 80.10  ? 75  LYS B NZ  1 
ATOM   2898 N  N   . ASP B 2 77  ? 26.652  52.690 -16.364 1.00 30.98  ? 76  ASP B N   1 
ATOM   2899 C  CA  . ASP B 2 77  ? 26.084  51.382 -16.813 1.00 36.65  ? 76  ASP B CA  1 
ATOM   2900 C  C   . ASP B 2 77  ? 24.961  50.962 -15.856 1.00 39.17  ? 76  ASP B C   1 
ATOM   2901 O  O   . ASP B 2 77  ? 25.127  51.113 -14.637 1.00 36.39  ? 76  ASP B O   1 
ATOM   2902 C  CB  . ASP B 2 77  ? 27.143  50.289 -16.913 1.00 30.42  ? 76  ASP B CB  1 
ATOM   2903 C  CG  . ASP B 2 77  ? 28.073  50.523 -18.080 1.00 42.73  ? 76  ASP B CG  1 
ATOM   2904 O  OD1 . ASP B 2 77  ? 27.561  50.755 -19.177 1.00 37.54  ? 76  ASP B OD1 1 
ATOM   2905 O  OD2 . ASP B 2 77  ? 29.274  50.518 -17.864 1.00 38.67  ? 76  ASP B OD2 1 
ATOM   2906 N  N   . GLU B 2 78  ? 23.846  50.482 -16.409 1.00 34.92  ? 77  GLU B N   1 
ATOM   2907 C  CA  . GLU B 2 78  ? 22.653  50.048 -15.645 1.00 30.60  ? 77  GLU B CA  1 
ATOM   2908 C  C   . GLU B 2 78  ? 22.637  48.516 -15.653 1.00 34.55  ? 77  GLU B C   1 
ATOM   2909 O  O   . GLU B 2 78  ? 22.714  47.931 -16.745 1.00 30.44  ? 77  GLU B O   1 
ATOM   2910 C  CB  . GLU B 2 78  ? 21.402  50.658 -16.270 1.00 40.83  ? 77  GLU B CB  1 
ATOM   2911 C  CG  . GLU B 2 78  ? 21.393  52.171 -16.200 1.00 52.39  ? 77  GLU B CG  1 
ATOM   2912 C  CD  . GLU B 2 78  ? 20.246  52.827 -16.951 1.00 56.08  ? 77  GLU B CD  1 
ATOM   2913 O  OE1 . GLU B 2 78  ? 20.466  53.894 -17.543 1.00 64.50  ? 77  GLU B OE1 1 
ATOM   2914 O  OE2 . GLU B 2 78  ? 19.145  52.261 -16.942 1.00 66.59  ? 77  GLU B OE2 1 
ATOM   2915 N  N   . TYR B 2 79  ? 22.587  47.880 -14.483 1.00 29.68  ? 78  TYR B N   1 
ATOM   2916 C  CA  . TYR B 2 79  ? 22.446  46.403 -14.366 1.00 25.03  ? 78  TYR B CA  1 
ATOM   2917 C  C   . TYR B 2 79  ? 21.072  46.071 -13.781 1.00 22.10  ? 78  TYR B C   1 
ATOM   2918 O  O   . TYR B 2 79  ? 20.494  46.864 -13.004 1.00 24.85  ? 78  TYR B O   1 
ATOM   2919 C  CB  . TYR B 2 79  ? 23.599  45.809 -13.566 1.00 29.02  ? 78  TYR B CB  1 
ATOM   2920 C  CG  . TYR B 2 79  ? 24.924  45.980 -14.251 1.00 26.75  ? 78  TYR B CG  1 
ATOM   2921 C  CD1 . TYR B 2 79  ? 25.702  47.109 -14.051 1.00 27.62  ? 78  TYR B CD1 1 
ATOM   2922 C  CD2 . TYR B 2 79  ? 25.367  45.022 -15.138 1.00 27.54  ? 78  TYR B CD2 1 
ATOM   2923 C  CE1 . TYR B 2 79  ? 26.916  47.254 -14.696 1.00 31.48  ? 78  TYR B CE1 1 
ATOM   2924 C  CE2 . TYR B 2 79  ? 26.574  45.147 -15.789 1.00 34.38  ? 78  TYR B CE2 1 
ATOM   2925 C  CZ  . TYR B 2 79  ? 27.347  46.274 -15.573 1.00 33.44  ? 78  TYR B CZ  1 
ATOM   2926 O  OH  . TYR B 2 79  ? 28.519  46.363 -16.244 1.00 36.83  ? 78  TYR B OH  1 
ATOM   2927 N  N   . ALA B 2 80  ? 20.531  44.935 -14.195 1.00 23.98  ? 79  ALA B N   1 
ATOM   2928 C  CA  . ALA B 2 80  ? 19.216  44.492 -13.700 1.00 23.34  ? 79  ALA B CA  1 
ATOM   2929 C  C   . ALA B 2 80  ? 19.112  42.979 -13.788 1.00 21.70  ? 79  ALA B C   1 
ATOM   2930 O  O   . ALA B 2 80  ? 19.947  42.311 -14.433 1.00 26.90  ? 79  ALA B O   1 
ATOM   2931 C  CB  . ALA B 2 80  ? 18.080  45.158 -14.443 1.00 26.65  ? 79  ALA B CB  1 
ATOM   2932 N  N   . CYS B 2 81  ? 18.097  42.496 -13.102 1.00 23.52  ? 80  CYS B N   1 
ATOM   2933 C  CA  . CYS B 2 81  ? 17.683  41.092 -13.147 1.00 22.18  ? 80  CYS B CA  1 
ATOM   2934 C  C   . CYS B 2 81  ? 16.268  41.055 -13.721 1.00 19.08  ? 80  CYS B C   1 
ATOM   2935 O  O   . CYS B 2 81  ? 15.427  41.906 -13.320 1.00 26.15  ? 80  CYS B O   1 
ATOM   2936 C  CB  . CYS B 2 81  ? 17.684  40.519 -11.740 1.00 30.13  ? 80  CYS B CB  1 
ATOM   2937 S  SG  . CYS B 2 81  ? 17.422  38.743 -11.767 1.00 29.35  ? 80  CYS B SG  1 
ATOM   2938 N  N   . ARG B 2 82  ? 16.066  40.123 -14.653 1.00 23.48  ? 81  ARG B N   1 
ATOM   2939 C  CA  . ARG B 2 82  ? 14.798  39.948 -15.377 1.00 22.39  ? 81  ARG B CA  1 
ATOM   2940 C  C   . ARG B 2 82  ? 14.370  38.493 -15.199 1.00 20.05  ? 81  ARG B C   1 
ATOM   2941 O  O   . ARG B 2 82  ? 15.101  37.580 -15.621 1.00 19.80  ? 81  ARG B O   1 
ATOM   2942 C  CB  . ARG B 2 82  ? 14.943  40.328 -16.851 1.00 22.65  ? 81  ARG B CB  1 
ATOM   2943 C  CG  . ARG B 2 82  ? 13.696  40.037 -17.673 1.00 22.16  ? 81  ARG B CG  1 
ATOM   2944 C  CD  . ARG B 2 82  ? 13.879  40.447 -19.140 1.00 22.32  ? 81  ARG B CD  1 
ATOM   2945 N  NE  . ARG B 2 82  ? 14.798  39.549 -19.821 1.00 22.36  ? 81  ARG B NE  1 
ATOM   2946 C  CZ  . ARG B 2 82  ? 15.448  39.851 -20.932 1.00 25.33  ? 81  ARG B CZ  1 
ATOM   2947 N  NH1 . ARG B 2 82  ? 15.319  41.058 -21.445 1.00 28.85  ? 81  ARG B NH1 1 
ATOM   2948 N  NH2 . ARG B 2 82  ? 16.274  38.987 -21.465 1.00 25.16  ? 81  ARG B NH2 1 
ATOM   2949 N  N   . VAL B 2 83  ? 13.190  38.318 -14.625 1.00 18.78  ? 82  VAL B N   1 
ATOM   2950 C  CA  . VAL B 2 83  ? 12.669  37.007 -14.215 1.00 20.63  ? 82  VAL B CA  1 
ATOM   2951 C  C   . VAL B 2 83  ? 11.354  36.737 -14.952 1.00 20.47  ? 82  VAL B C   1 
ATOM   2952 O  O   . VAL B 2 83  ? 10.537  37.615 -15.007 1.00 21.58  ? 82  VAL B O   1 
ATOM   2953 C  CB  . VAL B 2 83  ? 12.476  36.998 -12.695 1.00 22.37  ? 82  VAL B CB  1 
ATOM   2954 C  CG1 . VAL B 2 83  ? 11.920  35.663 -12.237 1.00 24.08  ? 82  VAL B CG1 1 
ATOM   2955 C  CG2 . VAL B 2 83  ? 13.789  37.314 -11.985 1.00 23.69  ? 82  VAL B CG2 1 
ATOM   2956 N  N   . ASN B 2 84  ? 11.241  35.540 -15.511 1.00 23.51  ? 83  ASN B N   1 
ATOM   2957 C  CA  . ASN B 2 84  ? 9.985   34.963 -16.010 1.00 23.40  ? 83  ASN B CA  1 
ATOM   2958 C  C   . ASN B 2 84  ? 9.613   33.779 -15.137 1.00 21.48  ? 83  ASN B C   1 
ATOM   2959 O  O   . ASN B 2 84  ? 10.490  32.961 -14.812 1.00 20.00  ? 83  ASN B O   1 
ATOM   2960 C  CB  . ASN B 2 84  ? 10.104  34.614 -17.488 1.00 24.67  ? 83  ASN B CB  1 
ATOM   2961 C  CG  . ASN B 2 84  ? 10.157  35.891 -18.296 1.00 25.08  ? 83  ASN B CG  1 
ATOM   2962 O  OD1 . ASN B 2 84  ? 9.179   36.628 -18.320 1.00 24.52  ? 83  ASN B OD1 1 
ATOM   2963 N  ND2 . ASN B 2 84  ? 11.303  36.176 -18.906 1.00 27.05  ? 83  ASN B ND2 1 
ATOM   2964 N  N   . HIS B 2 85  ? 8.340   33.737 -14.784 1.00 24.58  ? 84  HIS B N   1 
ATOM   2965 C  CA  . HIS B 2 85  ? 7.744   32.655 -13.960 1.00 24.40  ? 84  HIS B CA  1 
ATOM   2966 C  C   . HIS B 2 85  ? 6.277   32.590 -14.341 1.00 27.30  ? 84  HIS B C   1 
ATOM   2967 O  O   . HIS B 2 85  ? 5.758   33.613 -14.780 1.00 22.17  ? 84  HIS B O   1 
ATOM   2968 C  CB  . HIS B 2 85  ? 7.951   32.926 -12.470 1.00 22.87  ? 84  HIS B CB  1 
ATOM   2969 C  CG  . HIS B 2 85  ? 7.518   31.791 -11.599 1.00 20.17  ? 84  HIS B CG  1 
ATOM   2970 N  ND1 . HIS B 2 85  ? 6.322   31.835 -10.939 1.00 21.32  ? 84  HIS B ND1 1 
ATOM   2971 C  CD2 . HIS B 2 85  ? 8.120   30.641 -11.249 1.00 20.32  ? 84  HIS B CD2 1 
ATOM   2972 C  CE1 . HIS B 2 85  ? 6.170   30.733 -10.236 1.00 22.35  ? 84  HIS B CE1 1 
ATOM   2973 N  NE2 . HIS B 2 85  ? 7.252   29.978 -10.408 1.00 21.45  ? 84  HIS B NE2 1 
ATOM   2974 N  N   . VAL B 2 86  ? 5.653   31.429 -14.198 1.00 28.52  ? 85  VAL B N   1 
ATOM   2975 C  CA  . VAL B 2 86  ? 4.233   31.262 -14.586 1.00 25.51  ? 85  VAL B CA  1 
ATOM   2976 C  C   . VAL B 2 86  ? 3.376   32.279 -13.838 1.00 29.55  ? 85  VAL B C   1 
ATOM   2977 O  O   . VAL B 2 86  ? 2.385   32.674 -14.412 1.00 23.79  ? 85  VAL B O   1 
ATOM   2978 C  CB  . VAL B 2 86  ? 3.769   29.807 -14.372 1.00 27.50  ? 85  VAL B CB  1 
ATOM   2979 C  CG1 . VAL B 2 86  ? 3.676   29.456 -12.877 1.00 26.08  ? 85  VAL B CG1 1 
ATOM   2980 C  CG2 . VAL B 2 86  ? 2.444   29.528 -15.082 1.00 35.24  ? 85  VAL B CG2 1 
ATOM   2981 N  N   . THR B 2 87  ? 3.721   32.745 -12.627 1.00 22.18  ? 86  THR B N   1 
ATOM   2982 C  CA  . THR B 2 87  ? 2.879   33.703 -11.861 1.00 22.39  ? 86  THR B CA  1 
ATOM   2983 C  C   . THR B 2 87  ? 2.970   35.148 -12.395 1.00 24.02  ? 86  THR B C   1 
ATOM   2984 O  O   . THR B 2 87  ? 2.164   35.985 -11.958 1.00 24.95  ? 86  THR B O   1 
ATOM   2985 C  CB  . THR B 2 87  ? 3.281   33.772 -10.388 1.00 27.85  ? 86  THR B CB  1 
ATOM   2986 O  OG1 . THR B 2 87  ? 4.681   34.074 -10.375 1.00 21.88  ? 86  THR B OG1 1 
ATOM   2987 C  CG2 . THR B 2 87  ? 2.953   32.486 -9.665  1.00 30.27  ? 86  THR B CG2 1 
ATOM   2988 N  N   . LEU B 2 88  ? 3.881   35.398 -13.329 1.00 29.20  ? 87  LEU B N   1 
ATOM   2989 C  CA  . LEU B 2 88  ? 4.188   36.772 -13.832 1.00 28.47  ? 87  LEU B CA  1 
ATOM   2990 C  C   . LEU B 2 88  ? 3.603   36.939 -15.246 1.00 26.02  ? 87  LEU B C   1 
ATOM   2991 O  O   . LEU B 2 88  ? 3.982   36.185 -16.151 1.00 29.77  ? 87  LEU B O   1 
ATOM   2992 C  CB  . LEU B 2 88  ? 5.699   36.938 -13.842 1.00 22.59  ? 87  LEU B CB  1 
ATOM   2993 C  CG  . LEU B 2 88  ? 6.396   36.933 -12.475 1.00 23.27  ? 87  LEU B CG  1 
ATOM   2994 C  CD1 . LEU B 2 88  ? 7.892   36.965 -12.650 1.00 26.90  ? 87  LEU B CD1 1 
ATOM   2995 C  CD2 . LEU B 2 88  ? 5.918   38.051 -11.586 1.00 25.55  ? 87  LEU B CD2 1 
ATOM   2996 N  N   . SER B 2 89  ? 2.781   37.955 -15.435 1.00 22.75  ? 88  SER B N   1 
ATOM   2997 C  CA  . SER B 2 89  ? 2.113   38.246 -16.733 1.00 27.04  ? 88  SER B CA  1 
ATOM   2998 C  C   . SER B 2 89  ? 3.075   38.937 -17.694 1.00 29.86  ? 88  SER B C   1 
ATOM   2999 O  O   . SER B 2 89  ? 2.840   38.892 -18.933 1.00 27.99  ? 88  SER B O   1 
ATOM   3000 C  CB  . SER B 2 89  ? 0.876   39.064 -16.494 1.00 28.90  ? 88  SER B CB  1 
ATOM   3001 O  OG  . SER B 2 89  ? -0.032  38.249 -15.817 1.00 34.13  ? 88  SER B OG  1 
ATOM   3002 N  N   . GLN B 2 90  ? 4.124   39.541 -17.147 1.00 22.82  ? 89  GLN B N   1 
ATOM   3003 C  CA  . GLN B 2 90  ? 5.207   40.193 -17.926 1.00 26.18  ? 89  GLN B CA  1 
ATOM   3004 C  C   . GLN B 2 90  ? 6.507   39.833 -17.219 1.00 22.48  ? 89  GLN B C   1 
ATOM   3005 O  O   . GLN B 2 90  ? 6.476   39.459 -16.033 1.00 22.18  ? 89  GLN B O   1 
ATOM   3006 C  CB  . GLN B 2 90  ? 5.041   41.714 -17.957 1.00 29.42  ? 89  GLN B CB  1 
ATOM   3007 C  CG  . GLN B 2 90  ? 3.790   42.192 -18.665 1.00 43.42  ? 89  GLN B CG  1 
ATOM   3008 C  CD  . GLN B 2 90  ? 2.596   42.285 -17.741 1.00 64.70  ? 89  GLN B CD  1 
ATOM   3009 O  OE1 . GLN B 2 90  ? 2.737   42.354 -16.525 1.00 57.11  ? 89  GLN B OE1 1 
ATOM   3010 N  NE2 . GLN B 2 90  ? 1.400   42.281 -18.310 1.00 44.63  ? 89  GLN B NE2 1 
ATOM   3011 N  N   . PRO B 2 91  ? 7.679   39.980 -17.863 1.00 24.97  ? 90  PRO B N   1 
ATOM   3012 C  CA  . PRO B 2 91  ? 8.933   39.754 -17.145 1.00 19.24  ? 90  PRO B CA  1 
ATOM   3013 C  C   . PRO B 2 91  ? 9.022   40.794 -16.017 1.00 22.91  ? 90  PRO B C   1 
ATOM   3014 O  O   . PRO B 2 91  ? 8.594   41.961 -16.161 1.00 23.32  ? 90  PRO B O   1 
ATOM   3015 C  CB  . PRO B 2 91  ? 10.026  39.929 -18.195 1.00 21.24  ? 90  PRO B CB  1 
ATOM   3016 C  CG  . PRO B 2 91  ? 9.274   39.851 -19.533 1.00 27.52  ? 90  PRO B CG  1 
ATOM   3017 C  CD  . PRO B 2 91  ? 7.911   40.421 -19.245 1.00 23.69  ? 90  PRO B CD  1 
ATOM   3018 N  N   . LYS B 2 92  ? 9.553   40.346 -14.885 1.00 22.02  ? 91  LYS B N   1 
ATOM   3019 C  CA  . LYS B 2 92  ? 9.760   41.223 -13.725 1.00 22.65  ? 91  LYS B CA  1 
ATOM   3020 C  C   . LYS B 2 92  ? 11.205  41.686 -13.761 1.00 21.33  ? 91  LYS B C   1 
ATOM   3021 O  O   . LYS B 2 92  ? 12.114  40.815 -13.763 1.00 23.06  ? 91  LYS B O   1 
ATOM   3022 C  CB  . LYS B 2 92  ? 9.428   40.485 -12.437 1.00 27.35  ? 91  LYS B CB  1 
ATOM   3023 C  CG  . LYS B 2 92  ? 9.684   41.294 -11.160 1.00 30.10  ? 91  LYS B CG  1 
ATOM   3024 C  CD  . LYS B 2 92  ? 8.756   42.437 -10.921 1.00 49.73  ? 91  LYS B CD  1 
ATOM   3025 C  CE  . LYS B 2 92  ? 9.055   43.143 -9.613  1.00 56.68  ? 91  LYS B CE  1 
ATOM   3026 N  NZ  . LYS B 2 92  ? 8.564   44.539 -9.639  1.00 59.63  ? 91  LYS B NZ  1 
ATOM   3027 N  N   . ILE B 2 93  ? 11.403  43.010 -13.845 1.00 24.19  ? 92  ILE B N   1 
ATOM   3028 C  CA  . ILE B 2 93  ? 12.782  43.578 -13.965 1.00 25.59  ? 92  ILE B CA  1 
ATOM   3029 C  C   . ILE B 2 93  ? 13.117  44.312 -12.663 1.00 22.86  ? 92  ILE B C   1 
ATOM   3030 O  O   . ILE B 2 93  ? 12.378  45.217 -12.295 1.00 25.22  ? 92  ILE B O   1 
ATOM   3031 C  CB  . ILE B 2 93  ? 12.937  44.460 -15.226 1.00 26.63  ? 92  ILE B CB  1 
ATOM   3032 C  CG1 . ILE B 2 93  ? 12.780  43.613 -16.498 1.00 25.66  ? 92  ILE B CG1 1 
ATOM   3033 C  CG2 . ILE B 2 93  ? 14.266  45.199 -15.200 1.00 28.60  ? 92  ILE B CG2 1 
ATOM   3034 C  CD1 . ILE B 2 93  ? 12.851  44.380 -17.783 1.00 38.70  ? 92  ILE B CD1 1 
ATOM   3035 N  N   . VAL B 2 94  ? 14.208  43.914 -12.000 1.00 21.90  ? 93  VAL B N   1 
ATOM   3036 C  CA  . VAL B 2 94  ? 14.675  44.598 -10.765 1.00 23.75  ? 93  VAL B CA  1 
ATOM   3037 C  C   . VAL B 2 94  ? 16.057  45.175 -11.044 1.00 20.68  ? 93  VAL B C   1 
ATOM   3038 O  O   . VAL B 2 94  ? 16.944  44.430 -11.457 1.00 21.93  ? 93  VAL B O   1 
ATOM   3039 C  CB  . VAL B 2 94  ? 14.702  43.673 -9.542  1.00 24.99  ? 93  VAL B CB  1 
ATOM   3040 C  CG1 . VAL B 2 94  ? 15.188  44.442 -8.314  1.00 28.60  ? 93  VAL B CG1 1 
ATOM   3041 C  CG2 . VAL B 2 94  ? 13.341  43.033 -9.299  1.00 30.15  ? 93  VAL B CG2 1 
ATOM   3042 N  N   . LYS B 2 95  ? 16.181  46.488 -10.904 1.00 25.10  ? 94  LYS B N   1 
ATOM   3043 C  CA  . LYS B 2 95  ? 17.428  47.215 -11.218 1.00 28.44  ? 94  LYS B CA  1 
ATOM   3044 C  C   . LYS B 2 95  ? 18.414  46.992 -10.076 1.00 25.67  ? 94  LYS B C   1 
ATOM   3045 O  O   . LYS B 2 95  ? 17.971  46.958 -8.920  1.00 28.03  ? 94  LYS B O   1 
ATOM   3046 C  CB  . LYS B 2 95  ? 17.150  48.708 -11.358 1.00 34.43  ? 94  LYS B CB  1 
ATOM   3047 C  CG  . LYS B 2 95  ? 16.227  49.082 -12.507 1.00 47.35  ? 94  LYS B CG  1 
ATOM   3048 C  CD  . LYS B 2 95  ? 15.834  50.556 -12.505 1.00 52.72  ? 94  LYS B CD  1 
ATOM   3049 C  CE  . LYS B 2 95  ? 16.623  51.393 -13.489 1.00 83.01  ? 94  LYS B CE  1 
ATOM   3050 N  NZ  . LYS B 2 95  ? 16.033  52.744 -13.653 1.00 85.46  ? 94  LYS B NZ  1 
ATOM   3051 N  N   . TRP B 2 96  ? 19.678  46.836 -10.409 1.00 26.50  ? 95  TRP B N   1 
ATOM   3052 C  CA  . TRP B 2 96  ? 20.753  46.804 -9.409  1.00 22.84  ? 95  TRP B CA  1 
ATOM   3053 C  C   . TRP B 2 96  ? 20.955  48.209 -8.840  1.00 30.90  ? 95  TRP B C   1 
ATOM   3054 O  O   . TRP B 2 96  ? 21.109  49.148 -9.638  1.00 27.67  ? 95  TRP B O   1 
ATOM   3055 C  CB  . TRP B 2 96  ? 22.046  46.273 -10.007 1.00 23.67  ? 95  TRP B CB  1 
ATOM   3056 C  CG  . TRP B 2 96  ? 23.143  46.283 -9.003  1.00 22.57  ? 95  TRP B CG  1 
ATOM   3057 C  CD1 . TRP B 2 96  ? 23.139  45.712 -7.769  1.00 31.10  ? 95  TRP B CD1 1 
ATOM   3058 C  CD2 . TRP B 2 96  ? 24.366  47.006 -9.101  1.00 27.38  ? 95  TRP B CD2 1 
ATOM   3059 N  NE1 . TRP B 2 96  ? 24.325  45.949 -7.124  1.00 30.32  ? 95  TRP B NE1 1 
ATOM   3060 C  CE2 . TRP B 2 96  ? 25.101  46.735 -7.927  1.00 27.31  ? 95  TRP B CE2 1 
ATOM   3061 C  CE3 . TRP B 2 96  ? 24.931  47.805 -10.103 1.00 30.90  ? 95  TRP B CE3 1 
ATOM   3062 C  CZ2 . TRP B 2 96  ? 26.359  47.282 -7.706  1.00 30.75  ? 95  TRP B CZ2 1 
ATOM   3063 C  CZ3 . TRP B 2 96  ? 26.169  48.352 -9.877  1.00 30.95  ? 95  TRP B CZ3 1 
ATOM   3064 C  CH2 . TRP B 2 96  ? 26.874  48.080 -8.703  1.00 29.19  ? 95  TRP B CH2 1 
ATOM   3065 N  N   . ASP B 2 97  ? 20.950  48.316 -7.513  1.00 25.43  ? 96  ASP B N   1 
ATOM   3066 C  CA  . ASP B 2 97  ? 21.256  49.527 -6.713  1.00 25.98  ? 96  ASP B CA  1 
ATOM   3067 C  C   . ASP B 2 97  ? 22.359  49.140 -5.725  1.00 32.00  ? 96  ASP B C   1 
ATOM   3068 O  O   . ASP B 2 97  ? 22.122  48.287 -4.845  1.00 27.01  ? 96  ASP B O   1 
ATOM   3069 C  CB  . ASP B 2 97  ? 20.007  50.028 -5.997  1.00 28.84  ? 96  ASP B CB  1 
ATOM   3070 C  CG  . ASP B 2 97  ? 20.232  51.283 -5.180  1.00 31.32  ? 96  ASP B CG  1 
ATOM   3071 O  OD1 . ASP B 2 97  ? 21.411  51.593 -4.823  1.00 30.13  ? 96  ASP B OD1 1 
ATOM   3072 O  OD2 . ASP B 2 97  ? 19.245  51.926 -4.920  1.00 32.53  ? 96  ASP B OD2 1 
ATOM   3073 N  N   . ARG B 2 98  ? 23.550  49.706 -5.884  1.00 28.25  ? 97  ARG B N   1 
ATOM   3074 C  CA  . ARG B 2 98  ? 24.729  49.364 -5.039  1.00 30.30  ? 97  ARG B CA  1 
ATOM   3075 C  C   . ARG B 2 98  ? 24.478  49.662 -3.559  1.00 26.40  ? 97  ARG B C   1 
ATOM   3076 O  O   . ARG B 2 98  ? 25.229  49.103 -2.760  1.00 28.92  ? 97  ARG B O   1 
ATOM   3077 C  CB  . ARG B 2 98  ? 25.970  50.128 -5.486  1.00 30.99  ? 97  ARG B CB  1 
ATOM   3078 C  CG  . ARG B 2 98  ? 25.875  51.633 -5.296  1.00 33.84  ? 97  ARG B CG  1 
ATOM   3079 C  CD  . ARG B 2 98  ? 27.064  52.291 -5.981  1.00 38.73  ? 97  ARG B CD  1 
ATOM   3080 N  NE  . ARG B 2 98  ? 27.068  52.135 -7.441  1.00 35.25  ? 97  ARG B NE  1 
ATOM   3081 C  CZ  . ARG B 2 98  ? 28.140  52.281 -8.229  1.00 42.18  ? 97  ARG B CZ  1 
ATOM   3082 N  NH1 . ARG B 2 98  ? 28.016  52.139 -9.539  1.00 31.66  ? 97  ARG B NH1 1 
ATOM   3083 N  NH2 . ARG B 2 98  ? 29.337  52.554 -7.715  1.00 37.31  ? 97  ARG B NH2 1 
ATOM   3084 N  N   . ASP B 2 99  ? 23.449  50.437 -3.206  1.00 27.77  ? 98  ASP B N   1 
ATOM   3085 C  CA  . ASP B 2 99  ? 23.120  50.742 -1.781  1.00 30.82  ? 98  ASP B CA  1 
ATOM   3086 C  C   . ASP B 2 99  ? 22.046  49.789 -1.229  1.00 26.09  ? 98  ASP B C   1 
ATOM   3087 O  O   . ASP B 2 99  ? 21.549  50.046 -0.138  1.00 29.41  ? 98  ASP B O   1 
ATOM   3088 C  CB  . ASP B 2 99  ? 22.725  52.200 -1.646  1.00 33.32  ? 98  ASP B CB  1 
ATOM   3089 C  CG  . ASP B 2 99  ? 23.908  53.101 -1.961  1.00 29.62  ? 98  ASP B CG  1 
ATOM   3090 O  OD1 . ASP B 2 99  ? 25.055  52.637 -1.798  1.00 37.49  ? 98  ASP B OD1 1 
ATOM   3091 O  OD2 . ASP B 2 99  ? 23.675  54.171 -2.472  1.00 41.73  ? 98  ASP B OD2 1 
ATOM   3092 N  N   . MET B 2 100 ? 21.746  48.702 -1.931  1.00 25.47  ? 99  MET B N   1 
ATOM   3093 C  CA  . MET B 2 100 ? 20.730  47.740 -1.440  1.00 24.77  ? 99  MET B CA  1 
ATOM   3094 C  C   . MET B 2 100 ? 21.151  46.302 -1.717  1.00 24.35  ? 99  MET B C   1 
ATOM   3095 O  O   . MET B 2 100 ? 20.426  45.409 -1.250  1.00 27.90  ? 99  MET B O   1 
ATOM   3096 C  CB  . MET B 2 100 ? 19.381  48.023 -2.101  1.00 29.19  ? 99  MET B CB  1 
ATOM   3097 C  CG  . MET B 2 100 ? 18.740  49.255 -1.532  1.00 38.29  ? 99  MET B CG  1 
ATOM   3098 S  SD  . MET B 2 100 ? 17.233  49.553 -2.399  1.00 53.49  ? 99  MET B SD  1 
ATOM   3099 C  CE  . MET B 2 100 ? 16.912  51.231 -1.851  1.00 70.38  ? 99  MET B CE  1 
ATOM   3100 O  OXT . MET B 2 100 ? 22.109  46.006 -2.347  1.00 28.41  ? 99  MET B OXT 1 
ATOM   3101 N  N   . SER C 3 1   ? 26.289  10.827 2.684   1.00 26.02  ? 1   SER C N   1 
ATOM   3102 C  CA  . SER C 3 1   ? 25.723  10.043 1.561   1.00 24.95  ? 1   SER C CA  1 
ATOM   3103 C  C   . SER C 3 1   ? 24.207  9.938  1.695   1.00 23.25  ? 1   SER C C   1 
ATOM   3104 O  O   . SER C 3 1   ? 23.656  9.872  2.799   1.00 23.30  ? 1   SER C O   1 
ATOM   3105 C  CB  . SER C 3 1   ? 26.352  8.663  1.468   1.00 27.33  ? 1   SER C CB  1 
ATOM   3106 O  OG  . SER C 3 1   ? 27.744  8.783  1.233   1.00 26.54  ? 1   SER C OG  1 
ATOM   3107 N  N   . PRO C 3 2   ? 23.488  9.880  0.564   1.00 25.02  ? 2   PRO C N   1 
ATOM   3108 C  CA  . PRO C 3 2   ? 22.032  9.756  0.591   1.00 21.47  ? 2   PRO C CA  1 
ATOM   3109 C  C   . PRO C 3 2   ? 21.621  8.413  1.200   1.00 30.42  ? 2   PRO C C   1 
ATOM   3110 O  O   . PRO C 3 2   ? 22.323  7.410  1.083   1.00 27.71  ? 2   PRO C O   1 
ATOM   3111 C  CB  . PRO C 3 2   ? 21.636  9.813  -0.860  1.00 25.93  ? 2   PRO C CB  1 
ATOM   3112 C  CG  . PRO C 3 2   ? 22.889  9.303  -1.585  1.00 22.48  ? 2   PRO C CG  1 
ATOM   3113 C  CD  . PRO C 3 2   ? 24.035  9.845  -0.793  1.00 23.19  ? 2   PRO C CD  1 
ATOM   3114 N  N   . ARG C 3 3   ? 20.483  8.407  1.860   1.00 25.60  ? 3   ARG C N   1 
ATOM   3115 C  CA  . ARG C 3 3   ? 20.044  7.190  2.556   1.00 22.49  ? 3   ARG C CA  1 
ATOM   3116 C  C   . ARG C 3 3   ? 19.551  6.191  1.514   1.00 24.48  ? 3   ARG C C   1 
ATOM   3117 O  O   . ARG C 3 3   ? 19.007  6.607  0.485   1.00 24.43  ? 3   ARG C O   1 
ATOM   3118 C  CB  . ARG C 3 3   ? 19.025  7.543  3.615   1.00 31.72  ? 3   ARG C CB  1 
ATOM   3119 C  CG  . ARG C 3 3   ? 17.685  7.946  3.064   1.00 26.98  ? 3   ARG C CG  1 
ATOM   3120 C  CD  . ARG C 3 3   ? 16.741  7.888  4.270   1.00 37.15  ? 3   ARG C CD  1 
ATOM   3121 N  NE  . ARG C 3 3   ? 15.554  8.638  3.914   1.00 24.42  ? 3   ARG C NE  1 
ATOM   3122 C  CZ  . ARG C 3 3   ? 14.702  9.200  4.762   1.00 33.41  ? 3   ARG C CZ  1 
ATOM   3123 N  NH1 . ARG C 3 3   ? 14.854  9.071  6.080   1.00 22.61  ? 3   ARG C NH1 1 
ATOM   3124 N  NH2 . ARG C 3 3   ? 13.703  9.907  4.243   1.00 26.31  ? 3   ARG C NH2 1 
ATOM   3125 N  N   . TRP C 3 4   ? 19.662  4.905  1.830   1.00 25.80  ? 4   TRP C N   1 
ATOM   3126 C  CA  . TRP C 3 4   ? 19.306  3.807  0.892   1.00 21.84  ? 4   TRP C CA  1 
ATOM   3127 C  C   . TRP C 3 4   ? 18.052  3.104  1.383   1.00 24.91  ? 4   TRP C C   1 
ATOM   3128 O  O   . TRP C 3 4   ? 17.693  2.064  0.825   1.00 24.96  ? 4   TRP C O   1 
ATOM   3129 C  CB  . TRP C 3 4   ? 20.499  2.863  0.705   1.00 25.37  ? 4   TRP C CB  1 
ATOM   3130 C  CG  . TRP C 3 4   ? 21.068  2.341  1.981   1.00 24.43  ? 4   TRP C CG  1 
ATOM   3131 C  CD1 . TRP C 3 4   ? 21.972  2.958  2.788   1.00 27.17  ? 4   TRP C CD1 1 
ATOM   3132 C  CD2 . TRP C 3 4   ? 20.732  1.089  2.625   1.00 25.93  ? 4   TRP C CD2 1 
ATOM   3133 N  NE1 . TRP C 3 4   ? 22.258  2.163  3.858   1.00 29.48  ? 4   TRP C NE1 1 
ATOM   3134 C  CE2 . TRP C 3 4   ? 21.501  1.022  3.802   1.00 26.69  ? 4   TRP C CE2 1 
ATOM   3135 C  CE3 . TRP C 3 4   ? 19.915  -0.002 2.295   1.00 28.36  ? 4   TRP C CE3 1 
ATOM   3136 C  CZ2 . TRP C 3 4   ? 21.463  -0.085 4.649   1.00 27.57  ? 4   TRP C CZ2 1 
ATOM   3137 C  CZ3 . TRP C 3 4   ? 19.879  -1.102 3.128   1.00 28.48  ? 4   TRP C CZ3 1 
ATOM   3138 C  CH2 . TRP C 3 4   ? 20.634  -1.128 4.301   1.00 26.44  ? 4   TRP C CH2 1 
ATOM   3139 N  N   . TYR C 3 5   ? 17.376  3.683  2.365   1.00 24.90  ? 5   TYR C N   1 
ATOM   3140 C  CA  . TYR C 3 5   ? 15.996  3.280  2.720   1.00 28.19  ? 5   TYR C CA  1 
ATOM   3141 C  C   . TYR C 3 5   ? 15.013  4.166  1.983   1.00 27.67  ? 5   TYR C C   1 
ATOM   3142 O  O   . TYR C 3 5   ? 15.191  5.395  2.025   1.00 25.68  ? 5   TYR C O   1 
ATOM   3143 C  CB  . TYR C 3 5   ? 15.738  3.421  4.212   1.00 26.62  ? 5   TYR C CB  1 
ATOM   3144 C  CG  . TYR C 3 5   ? 16.788  2.747  5.060   1.00 31.46  ? 5   TYR C CG  1 
ATOM   3145 C  CD1 . TYR C 3 5   ? 17.027  1.380  4.980   1.00 43.05  ? 5   TYR C CD1 1 
ATOM   3146 C  CD2 . TYR C 3 5   ? 17.554  3.490  5.948   1.00 44.05  ? 5   TYR C CD2 1 
ATOM   3147 C  CE1 . TYR C 3 5   ? 17.993  0.768  5.771   1.00 33.69  ? 5   TYR C CE1 1 
ATOM   3148 C  CE2 . TYR C 3 5   ? 18.504  2.895  6.758   1.00 37.56  ? 5   TYR C CE2 1 
ATOM   3149 C  CZ  . TYR C 3 5   ? 18.724  1.530  6.665   1.00 44.17  ? 5   TYR C CZ  1 
ATOM   3150 O  OH  . TYR C 3 5   ? 19.675  0.968  7.454   1.00 36.91  ? 5   TYR C OH  1 
ATOM   3151 N  N   . PHE C 3 6   ? 13.993  3.538  1.393   1.00 21.78  ? 6   PHE C N   1 
ATOM   3152 C  CA  . PHE C 3 6   ? 12.985  4.201  0.534   1.00 23.46  ? 6   PHE C CA  1 
ATOM   3153 C  C   . PHE C 3 6   ? 11.596  3.980  1.102   1.00 27.72  ? 6   PHE C C   1 
ATOM   3154 O  O   . PHE C 3 6   ? 11.208  2.842  1.474   1.00 30.53  ? 6   PHE C O   1 
ATOM   3155 C  CB  . PHE C 3 6   ? 13.123  3.697  -0.891  1.00 23.77  ? 6   PHE C CB  1 
ATOM   3156 C  CG  . PHE C 3 6   ? 14.532  3.804  -1.405  1.00 29.41  ? 6   PHE C CG  1 
ATOM   3157 C  CD1 . PHE C 3 6   ? 15.141  5.051  -1.508  1.00 25.25  ? 6   PHE C CD1 1 
ATOM   3158 C  CD2 . PHE C 3 6   ? 15.279  2.669  -1.691  1.00 23.10  ? 6   PHE C CD2 1 
ATOM   3159 C  CE1 . PHE C 3 6   ? 16.445  5.164  -1.960  1.00 27.95  ? 6   PHE C CE1 1 
ATOM   3160 C  CE2 . PHE C 3 6   ? 16.564  2.789  -2.188  1.00 26.23  ? 6   PHE C CE2 1 
ATOM   3161 C  CZ  . PHE C 3 6   ? 17.165  4.022  -2.271  1.00 30.84  ? 6   PHE C CZ  1 
ATOM   3162 N  N   . TYR C 3 7   ? 10.798  5.037  1.071   1.00 24.51  ? 7   TYR C N   1 
ATOM   3163 C  CA  . TYR C 3 7   ? 9.430   5.036  1.642   1.00 28.89  ? 7   TYR C CA  1 
ATOM   3164 C  C   . TYR C 3 7   ? 8.474   5.708  0.658   1.00 29.18  ? 7   TYR C C   1 
ATOM   3165 O  O   . TYR C 3 7   ? 8.881   6.691  0.027   1.00 29.98  ? 7   TYR C O   1 
ATOM   3166 C  CB  . TYR C 3 7   ? 9.471   5.803  2.956   1.00 31.36  ? 7   TYR C CB  1 
ATOM   3167 C  CG  . TYR C 3 7   ? 10.584  5.409  3.886   1.00 35.11  ? 7   TYR C CG  1 
ATOM   3168 C  CD1 . TYR C 3 7   ? 10.408  4.349  4.758   1.00 27.58  ? 7   TYR C CD1 1 
ATOM   3169 C  CD2 . TYR C 3 7   ? 11.795  6.098  3.909   1.00 32.58  ? 7   TYR C CD2 1 
ATOM   3170 C  CE1 . TYR C 3 7   ? 11.406  3.991  5.641   1.00 29.23  ? 7   TYR C CE1 1 
ATOM   3171 C  CE2 . TYR C 3 7   ? 12.804  5.741  4.789   1.00 33.61  ? 7   TYR C CE2 1 
ATOM   3172 C  CZ  . TYR C 3 7   ? 12.607  4.663  5.642   1.00 27.42  ? 7   TYR C CZ  1 
ATOM   3173 O  OH  . TYR C 3 7   ? 13.589  4.282  6.506   1.00 30.59  ? 7   TYR C OH  1 
ATOM   3174 N  N   . TYR C 3 8   ? 7.329   5.086  0.438   1.00 30.17  ? 8   TYR C N   1 
ATOM   3175 C  CA  . TYR C 3 8   ? 6.274   5.546  -0.484  1.00 30.18  ? 8   TYR C CA  1 
ATOM   3176 C  C   . TYR C 3 8   ? 5.256   6.286  0.389   1.00 29.03  ? 8   TYR C C   1 
ATOM   3177 O  O   . TYR C 3 8   ? 4.768   5.701  1.403   1.00 26.51  ? 8   TYR C O   1 
ATOM   3178 C  CB  . TYR C 3 8   ? 5.556   4.385  -1.187  1.00 37.94  ? 8   TYR C CB  1 
ATOM   3179 C  CG  . TYR C 3 8   ? 6.248   3.532  -2.235  1.00 50.98  ? 8   TYR C CG  1 
ATOM   3180 C  CD1 . TYR C 3 8   ? 7.359   3.937  -2.965  1.00 33.18  ? 8   TYR C CD1 1 
ATOM   3181 C  CD2 . TYR C 3 8   ? 5.688   2.300  -2.568  1.00 78.86  ? 8   TYR C CD2 1 
ATOM   3182 C  CE1 . TYR C 3 8   ? 7.925   3.109  -3.932  1.00 37.82  ? 8   TYR C CE1 1 
ATOM   3183 C  CE2 . TYR C 3 8   ? 6.230   1.473  -3.542  1.00 64.49  ? 8   TYR C CE2 1 
ATOM   3184 C  CZ  . TYR C 3 8   ? 7.355   1.880  -4.240  1.00 57.64  ? 8   TYR C CZ  1 
ATOM   3185 O  OH  . TYR C 3 8   ? 7.875   1.066  -5.220  1.00 40.50  ? 8   TYR C OH  1 
ATOM   3186 N  N   . THR C 3 9   ? 4.873   7.500  0.005   1.00 27.32  ? 9   THR C N   1 
ATOM   3187 C  CA  . THR C 3 9   ? 3.667   8.175  0.564   1.00 27.58  ? 9   THR C CA  1 
ATOM   3188 C  C   . THR C 3 9   ? 2.417   7.328  0.325   1.00 29.59  ? 9   THR C C   1 
ATOM   3189 O  O   . THR C 3 9   ? 2.386   6.375  -0.484  1.00 31.50  ? 9   THR C O   1 
ATOM   3190 C  CB  . THR C 3 9   ? 3.529   9.583  -0.009  1.00 32.91  ? 9   THR C CB  1 
ATOM   3191 O  OG1 . THR C 3 9   ? 3.413   9.376  -1.415  1.00 33.13  ? 9   THR C OG1 1 
ATOM   3192 C  CG2 . THR C 3 9   ? 4.707   10.450 0.376   1.00 34.37  ? 9   THR C CG2 1 
ATOM   3193 O  OXT . THR C 3 9   ? 1.407   7.598  0.966   1.00 28.47  ? 9   THR C OXT 1 
HETATM 3194 C  C   . BCT D 4 .   ? 26.718  30.625 -1.908  1.00 23.92  ? 301 BCT A C   1 
HETATM 3195 O  O1  . BCT D 4 .   ? 26.256  30.563 -3.132  1.00 44.33  ? 301 BCT A O1  1 
HETATM 3196 O  O2  . BCT D 4 .   ? 26.094  29.983 -1.046  1.00 32.52  ? 301 BCT A O2  1 
HETATM 3197 O  O3  . BCT D 4 .   ? 27.622  31.522 -1.650  1.00 38.06  ? 301 BCT A O3  1 
HETATM 3198 C  C1  . PEG E 5 .   ? 30.499  5.371  6.605   1.00 58.33  ? 302 PEG A C1  1 
HETATM 3199 O  O1  . PEG E 5 .   ? 31.750  6.041  6.782   1.00 65.59  ? 302 PEG A O1  1 
HETATM 3200 C  C2  . PEG E 5 .   ? 29.475  5.874  7.563   1.00 49.34  ? 302 PEG A C2  1 
HETATM 3201 O  O2  . PEG E 5 .   ? 28.246  5.167  7.423   1.00 51.70  ? 302 PEG A O2  1 
HETATM 3202 C  C3  . PEG E 5 .   ? 28.163  3.958  8.170   1.00 55.08  ? 302 PEG A C3  1 
HETATM 3203 C  C4  . PEG E 5 .   ? 27.393  4.162  9.445   1.00 63.85  ? 302 PEG A C4  1 
HETATM 3204 O  O4  . PEG E 5 .   ? 26.441  3.132  9.689   1.00 60.85  ? 302 PEG A O4  1 
HETATM 3205 C  C   . BCT F 4 .   ? 17.275  25.271 6.478   1.00 62.65  ? 303 BCT A C   1 
HETATM 3206 O  O1  . BCT F 4 .   ? 16.758  26.113 5.699   1.00 33.97  ? 303 BCT A O1  1 
HETATM 3207 O  O2  . BCT F 4 .   ? 17.571  25.462 7.671   1.00 54.44  ? 303 BCT A O2  1 
HETATM 3208 O  O3  . BCT F 4 .   ? 17.463  24.050 6.016   1.00 49.76  ? 303 BCT A O3  1 
HETATM 3209 C  C1  . PEG G 5 .   ? 28.607  0.480  3.410   1.00 59.05  ? 304 PEG A C1  1 
HETATM 3210 O  O1  . PEG G 5 .   ? 28.799  1.138  2.175   1.00 52.14  ? 304 PEG A O1  1 
HETATM 3211 C  C2  . PEG G 5 .   ? 27.196  0.571  3.893   1.00 45.56  ? 304 PEG A C2  1 
HETATM 3212 O  O2  . PEG G 5 .   ? 26.325  -0.093 2.987   1.00 45.89  ? 304 PEG A O2  1 
HETATM 3213 C  C3  . PEG G 5 .   ? 24.984  -0.146 3.457   1.00 32.77  ? 304 PEG A C3  1 
HETATM 3214 C  C4  . PEG G 5 .   ? 24.120  -0.800 2.436   1.00 33.05  ? 304 PEG A C4  1 
HETATM 3215 O  O4  . PEG G 5 .   ? 24.247  -0.195 1.174   1.00 37.27  ? 304 PEG A O4  1 
HETATM 3216 CL CL  . CL  H 6 .   ? 16.230  35.239 5.876   1.00 50.53  ? 305 CL  A CL  1 
HETATM 3217 O  O   . HOH I 7 .   ? 34.944  19.813 12.485  1.00 49.32  ? 401 HOH A O   1 
HETATM 3218 O  O   . HOH I 7 .   ? 10.554  14.109 -17.172 1.00 60.24  ? 402 HOH A O   1 
HETATM 3219 O  O   . HOH I 7 .   ? 16.960  58.355 0.229   1.00 48.02  ? 403 HOH A O   1 
HETATM 3220 O  O   . HOH I 7 .   ? 35.532  32.769 13.694  1.00 49.19  ? 404 HOH A O   1 
HETATM 3221 O  O   . HOH I 7 .   ? 11.573  52.816 10.068  1.00 47.70  ? 405 HOH A O   1 
HETATM 3222 O  O   . HOH I 7 .   ? 13.916  53.684 4.137   1.00 43.73  ? 406 HOH A O   1 
HETATM 3223 O  O   . HOH I 7 .   ? 16.861  4.190  17.270  1.00 46.15  ? 407 HOH A O   1 
HETATM 3224 O  O   . HOH I 7 .   ? 7.623   5.723  6.184   1.00 36.75  ? 408 HOH A O   1 
HETATM 3225 O  O   . HOH I 7 .   ? 24.058  5.774  2.470   1.00 24.22  ? 409 HOH A O   1 
HETATM 3226 O  O   . HOH I 7 .   ? 23.072  11.349 -20.174 1.00 47.75  ? 410 HOH A O   1 
HETATM 3227 O  O   . HOH I 7 .   ? 30.507  27.078 11.212  1.00 52.48  ? 411 HOH A O   1 
HETATM 3228 O  O   . HOH I 7 .   ? 4.852   26.222 1.439   1.00 38.53  ? 412 HOH A O   1 
HETATM 3229 O  O   . HOH I 7 .   ? 17.668  9.955  -15.921 1.00 42.90  ? 413 HOH A O   1 
HETATM 3230 O  O   . HOH I 7 .   ? 36.300  7.437  -0.742  1.00 43.71  ? 414 HOH A O   1 
HETATM 3231 O  O   . HOH I 7 .   ? 36.910  10.078 -7.099  1.00 49.36  ? 415 HOH A O   1 
HETATM 3232 O  O   . HOH I 7 .   ? -8.459  14.126 1.643   1.00 46.20  ? 416 HOH A O   1 
HETATM 3233 O  O   . HOH I 7 .   ? 4.256   3.174  -11.722 1.00 33.73  ? 417 HOH A O   1 
HETATM 3234 O  O   . HOH I 7 .   ? 9.022   50.027 16.155  1.00 52.25  ? 418 HOH A O   1 
HETATM 3235 O  O   . HOH I 7 .   ? 32.622  37.832 0.655   1.00 44.41  ? 419 HOH A O   1 
HETATM 3236 O  O   . HOH I 7 .   ? 32.997  2.132  -8.357  1.00 47.28  ? 420 HOH A O   1 
HETATM 3237 O  O   . HOH I 7 .   ? 12.579  44.471 1.911   1.00 52.05  ? 421 HOH A O   1 
HETATM 3238 O  O   . HOH I 7 .   ? 0.982   0.226  6.614   1.00 38.82  ? 422 HOH A O   1 
HETATM 3239 O  O   . HOH I 7 .   ? 2.047   9.514  14.401  1.00 40.25  ? 423 HOH A O   1 
HETATM 3240 O  O   . HOH I 7 .   ? 8.966   9.076  -1.963  1.00 33.32  ? 424 HOH A O   1 
HETATM 3241 O  O   . HOH I 7 .   ? 18.361  61.187 9.860   1.00 48.39  ? 425 HOH A O   1 
HETATM 3242 O  O   . HOH I 7 .   ? 34.390  37.320 8.101   1.00 37.02  ? 426 HOH A O   1 
HETATM 3243 O  O   . HOH I 7 .   ? 34.247  36.701 5.334   1.00 37.11  ? 427 HOH A O   1 
HETATM 3244 O  O   . HOH I 7 .   ? 15.087  50.292 3.188   1.00 38.77  ? 428 HOH A O   1 
HETATM 3245 O  O   . HOH I 7 .   ? 33.688  20.238 -6.295  1.00 44.60  ? 429 HOH A O   1 
HETATM 3246 O  O   . HOH I 7 .   ? 22.833  28.872 9.242   1.00 24.23  ? 430 HOH A O   1 
HETATM 3247 O  O   . HOH I 7 .   ? 20.961  3.911  14.895  1.00 30.22  ? 431 HOH A O   1 
HETATM 3248 O  O   . HOH I 7 .   ? 20.422  47.643 24.126  1.00 35.34  ? 432 HOH A O   1 
HETATM 3249 O  O   . HOH I 7 .   ? 24.732  2.612  6.091   1.00 50.88  ? 433 HOH A O   1 
HETATM 3250 O  O   . HOH I 7 .   ? 21.492  25.360 7.275   1.00 39.98  ? 434 HOH A O   1 
HETATM 3251 O  O   . HOH I 7 .   ? 31.825  40.598 19.439  1.00 29.40  ? 435 HOH A O   1 
HETATM 3252 O  O   . HOH I 7 .   ? 12.105  10.102 -11.667 1.00 35.90  ? 436 HOH A O   1 
HETATM 3253 O  O   . HOH I 7 .   ? -1.251  4.364  -0.106  1.00 48.53  ? 437 HOH A O   1 
HETATM 3254 O  O   . HOH I 7 .   ? 3.016   3.192  -5.786  1.00 38.36  ? 438 HOH A O   1 
HETATM 3255 O  O   . HOH I 7 .   ? -4.335  20.417 1.668   1.00 36.86  ? 439 HOH A O   1 
HETATM 3256 O  O   . HOH I 7 .   ? 35.128  20.205 9.993   1.00 53.39  ? 440 HOH A O   1 
HETATM 3257 O  O   . HOH I 7 .   ? 25.054  29.735 13.438  1.00 27.05  ? 441 HOH A O   1 
HETATM 3258 O  O   . HOH I 7 .   ? 17.918  8.586  -1.092  1.00 24.10  ? 442 HOH A O   1 
HETATM 3259 O  O   . HOH I 7 .   ? 13.164  54.506 22.088  1.00 43.41  ? 443 HOH A O   1 
HETATM 3260 O  O   . HOH I 7 .   ? -7.577  10.628 5.612   1.00 37.68  ? 444 HOH A O   1 
HETATM 3261 O  O   . HOH I 7 .   ? -2.963  16.661 -12.285 1.00 30.61  ? 445 HOH A O   1 
HETATM 3262 O  O   . HOH I 7 .   ? -2.536  7.691  -9.090  1.00 40.44  ? 446 HOH A O   1 
HETATM 3263 O  O   . HOH I 7 .   ? 24.229  29.612 -4.429  1.00 37.11  ? 447 HOH A O   1 
HETATM 3264 O  O   . HOH I 7 .   ? 15.252  13.353 -15.882 1.00 43.10  ? 448 HOH A O   1 
HETATM 3265 O  O   . HOH I 7 .   ? 12.030  20.941 4.949   1.00 47.48  ? 449 HOH A O   1 
HETATM 3266 O  O   . HOH I 7 .   ? 29.260  13.529 -13.790 1.00 35.04  ? 450 HOH A O   1 
HETATM 3267 O  O   . HOH I 7 .   ? 30.006  24.424 8.030   1.00 29.81  ? 451 HOH A O   1 
HETATM 3268 O  O   . HOH I 7 .   ? 27.928  34.148 19.147  1.00 39.79  ? 452 HOH A O   1 
HETATM 3269 O  O   . HOH I 7 .   ? 16.050  6.247  -11.602 1.00 27.11  ? 453 HOH A O   1 
HETATM 3270 O  O   . HOH I 7 .   ? 26.374  44.500 21.503  1.00 40.50  ? 454 HOH A O   1 
HETATM 3271 O  O   . HOH I 7 .   ? 29.585  24.724 -1.672  1.00 31.70  ? 455 HOH A O   1 
HETATM 3272 O  O   . HOH I 7 .   ? 0.964   22.720 8.067   1.00 29.19  ? 456 HOH A O   1 
HETATM 3273 O  O   . HOH I 7 .   ? 4.518   2.687  2.189   1.00 43.92  ? 457 HOH A O   1 
HETATM 3274 O  O   . HOH I 7 .   ? 6.871   3.295  2.800   1.00 32.71  ? 458 HOH A O   1 
HETATM 3275 O  O   . HOH I 7 .   ? 28.427  6.408  -0.192  1.00 28.40  ? 459 HOH A O   1 
HETATM 3276 O  O   . HOH I 7 .   ? 26.539  12.372 -0.818  1.00 25.18  ? 460 HOH A O   1 
HETATM 3277 O  O   . HOH I 7 .   ? 2.024   13.401 -10.727 1.00 38.95  ? 461 HOH A O   1 
HETATM 3278 O  O   . HOH I 7 .   ? 17.125  33.601 3.104   1.00 33.39  ? 462 HOH A O   1 
HETATM 3279 O  O   . HOH I 7 .   ? 31.440  47.394 12.952  1.00 40.27  ? 463 HOH A O   1 
HETATM 3280 O  O   . HOH I 7 .   ? 25.122  32.480 13.482  1.00 23.55  ? 464 HOH A O   1 
HETATM 3281 O  O   . HOH I 7 .   ? 30.937  18.899 -10.105 1.00 43.43  ? 465 HOH A O   1 
HETATM 3282 O  O   . HOH I 7 .   ? 30.159  44.097 21.217  1.00 45.36  ? 466 HOH A O   1 
HETATM 3283 O  O   . HOH I 7 .   ? 19.739  12.662 -18.501 1.00 48.43  ? 467 HOH A O   1 
HETATM 3284 O  O   . HOH I 7 .   ? 11.288  14.528 -3.160  1.00 22.62  ? 468 HOH A O   1 
HETATM 3285 O  O   . HOH I 7 .   ? 32.317  55.782 9.229   1.00 33.35  ? 469 HOH A O   1 
HETATM 3286 O  O   . HOH I 7 .   ? 11.953  7.306  -12.016 1.00 37.52  ? 470 HOH A O   1 
HETATM 3287 O  O   . HOH I 7 .   ? 11.472  11.384 -1.024  1.00 28.88  ? 471 HOH A O   1 
HETATM 3288 O  O   . HOH I 7 .   ? 27.239  28.316 0.681   1.00 36.93  ? 472 HOH A O   1 
HETATM 3289 O  O   . HOH I 7 .   ? 32.235  25.984 3.834   1.00 34.23  ? 473 HOH A O   1 
HETATM 3290 O  O   . HOH I 7 .   ? 30.277  56.709 6.974   1.00 30.29  ? 474 HOH A O   1 
HETATM 3291 O  O   . HOH I 7 .   ? 32.275  49.447 10.177  1.00 34.43  ? 475 HOH A O   1 
HETATM 3292 O  O   . HOH I 7 .   ? 19.727  1.710  -8.121  1.00 25.53  ? 476 HOH A O   1 
HETATM 3293 O  O   . HOH I 7 .   ? 37.747  38.406 5.426   1.00 44.98  ? 477 HOH A O   1 
HETATM 3294 O  O   . HOH I 7 .   ? 4.599   9.613  -10.831 1.00 36.95  ? 478 HOH A O   1 
HETATM 3295 O  O   . HOH I 7 .   ? 10.054  9.138  0.891   1.00 46.62  ? 479 HOH A O   1 
HETATM 3296 O  O   . HOH I 7 .   ? -2.179  22.399 6.952   1.00 41.20  ? 480 HOH A O   1 
HETATM 3297 O  O   . HOH I 7 .   ? 13.534  0.042  4.417   1.00 45.32  ? 481 HOH A O   1 
HETATM 3298 O  O   . HOH I 7 .   ? 14.383  2.950  16.182  1.00 36.68  ? 482 HOH A O   1 
HETATM 3299 O  O   . HOH I 7 .   ? 32.101  33.510 18.439  1.00 38.13  ? 483 HOH A O   1 
HETATM 3300 O  O   . HOH I 7 .   ? 19.002  34.055 10.846  1.00 52.91  ? 484 HOH A O   1 
HETATM 3301 O  O   . HOH I 7 .   ? 29.892  55.911 17.090  1.00 51.27  ? 485 HOH A O   1 
HETATM 3302 O  O   . HOH I 7 .   ? 32.384  30.682 -5.370  1.00 47.09  ? 486 HOH A O   1 
HETATM 3303 O  O   . HOH I 7 .   ? 11.870  16.746 13.743  1.00 40.13  ? 487 HOH A O   1 
HETATM 3304 O  O   . HOH I 7 .   ? -3.386  4.466  4.951   1.00 35.27  ? 488 HOH A O   1 
HETATM 3305 O  O   . HOH I 7 .   ? 39.333  9.292  0.127   1.00 54.05  ? 489 HOH A O   1 
HETATM 3306 O  O   . HOH I 7 .   ? 24.113  60.849 3.765   1.00 35.91  ? 490 HOH A O   1 
HETATM 3307 O  O   . HOH I 7 .   ? 23.885  14.532 -11.897 1.00 26.90  ? 491 HOH A O   1 
HETATM 3308 O  O   . HOH I 7 .   ? 23.467  9.666  17.410  1.00 37.04  ? 492 HOH A O   1 
HETATM 3309 O  O   . HOH I 7 .   ? 14.885  14.772 16.969  1.00 35.79  ? 493 HOH A O   1 
HETATM 3310 O  O   . HOH I 7 .   ? 30.697  12.429 -10.719 1.00 43.23  ? 494 HOH A O   1 
HETATM 3311 O  O   . HOH I 7 .   ? 25.338  25.935 -3.155  1.00 35.37  ? 495 HOH A O   1 
HETATM 3312 O  O   . HOH I 7 .   ? 28.672  57.848 15.564  1.00 61.99  ? 496 HOH A O   1 
HETATM 3313 O  O   . HOH I 7 .   ? 23.098  55.481 14.659  1.00 31.25  ? 497 HOH A O   1 
HETATM 3314 O  O   . HOH I 7 .   ? 27.994  45.041 26.341  1.00 34.87  ? 498 HOH A O   1 
HETATM 3315 O  O   . HOH I 7 .   ? 10.122  48.510 27.017  1.00 45.27  ? 499 HOH A O   1 
HETATM 3316 O  O   . HOH I 7 .   ? 23.357  26.613 -1.880  1.00 34.60  ? 500 HOH A O   1 
HETATM 3317 O  O   . HOH I 7 .   ? 22.723  15.354 -3.668  1.00 25.40  ? 501 HOH A O   1 
HETATM 3318 O  O   . HOH I 7 .   ? 5.170   22.461 8.931   1.00 45.58  ? 502 HOH A O   1 
HETATM 3319 O  O   . HOH I 7 .   ? 10.139  -0.624 11.655  1.00 46.90  ? 503 HOH A O   1 
HETATM 3320 O  O   . HOH I 7 .   ? 8.006   22.434 -9.548  1.00 26.16  ? 504 HOH A O   1 
HETATM 3321 O  O   . HOH I 7 .   ? -0.850  20.534 -11.375 1.00 33.40  ? 505 HOH A O   1 
HETATM 3322 O  O   . HOH I 7 .   ? 24.774  16.651 20.984  1.00 58.19  ? 506 HOH A O   1 
HETATM 3323 O  O   . HOH I 7 .   ? 21.804  26.439 3.558   1.00 34.09  ? 507 HOH A O   1 
HETATM 3324 O  O   . HOH I 7 .   ? 21.086  34.652 15.053  1.00 33.53  ? 508 HOH A O   1 
HETATM 3325 O  O   . HOH I 7 .   ? 31.931  43.582 11.923  1.00 33.47  ? 509 HOH A O   1 
HETATM 3326 O  O   . HOH I 7 .   ? 11.646  2.156  -4.993  1.00 46.79  ? 510 HOH A O   1 
HETATM 3327 O  O   . HOH I 7 .   ? -8.263  14.334 -0.617  1.00 47.56  ? 511 HOH A O   1 
HETATM 3328 O  O   . HOH I 7 .   ? 16.291  19.846 -4.612  1.00 24.69  ? 512 HOH A O   1 
HETATM 3329 O  O   . HOH I 7 .   ? 19.956  34.363 8.306   1.00 23.36  ? 513 HOH A O   1 
HETATM 3330 O  O   . HOH I 7 .   ? 38.926  16.692 -1.680  1.00 43.29  ? 514 HOH A O   1 
HETATM 3331 O  O   . HOH I 7 .   ? 30.660  45.563 5.853   1.00 28.14  ? 515 HOH A O   1 
HETATM 3332 O  O   . HOH I 7 .   ? 0.037   18.884 1.098   1.00 48.85  ? 516 HOH A O   1 
HETATM 3333 O  O   . HOH I 7 .   ? -8.484  17.429 -3.842  1.00 36.88  ? 517 HOH A O   1 
HETATM 3334 O  O   . HOH I 7 .   ? -8.500  10.441 -1.242  1.00 39.87  ? 518 HOH A O   1 
HETATM 3335 O  O   . HOH I 7 .   ? 24.763  47.719 23.059  1.00 37.73  ? 519 HOH A O   1 
HETATM 3336 O  O   . HOH I 7 .   ? -3.399  6.795  -4.267  1.00 34.82  ? 520 HOH A O   1 
HETATM 3337 O  O   . HOH I 7 .   ? 12.021  9.569  -18.784 1.00 51.13  ? 521 HOH A O   1 
HETATM 3338 O  O   . HOH I 7 .   ? 6.409   20.552 -3.179  1.00 24.03  ? 522 HOH A O   1 
HETATM 3339 O  O   . HOH I 7 .   ? -2.184  20.774 -5.740  1.00 31.78  ? 523 HOH A O   1 
HETATM 3340 O  O   . HOH I 7 .   ? 22.622  21.307 6.339   1.00 30.72  ? 524 HOH A O   1 
HETATM 3341 O  O   . HOH I 7 .   ? 12.225  13.220 3.621   1.00 23.26  ? 525 HOH A O   1 
HETATM 3342 O  O   . HOH I 7 .   ? 10.885  16.347 10.244  1.00 25.38  ? 526 HOH A O   1 
HETATM 3343 O  O   . HOH I 7 .   ? 15.088  37.409 -0.952  1.00 24.96  ? 527 HOH A O   1 
HETATM 3344 O  O   . HOH I 7 .   ? 26.929  0.000  0.000   0.50 37.95  ? 528 HOH A O   1 
HETATM 3345 O  O   . HOH I 7 .   ? 1.643   13.702 -8.258  1.00 23.33  ? 529 HOH A O   1 
HETATM 3346 O  O   . HOH I 7 .   ? 27.103  23.647 -12.888 1.00 49.11  ? 530 HOH A O   1 
HETATM 3347 O  O   . HOH I 7 .   ? 24.957  25.085 -6.683  1.00 22.43  ? 531 HOH A O   1 
HETATM 3348 O  O   . HOH I 7 .   ? -2.432  3.116  11.364  1.00 36.79  ? 532 HOH A O   1 
HETATM 3349 O  O   . HOH I 7 .   ? 32.388  8.485  10.463  1.00 38.70  ? 533 HOH A O   1 
HETATM 3350 O  O   . HOH I 7 .   ? 19.690  52.427 20.945  1.00 34.14  ? 534 HOH A O   1 
HETATM 3351 O  O   . HOH I 7 .   ? 32.300  43.779 26.573  1.00 30.44  ? 535 HOH A O   1 
HETATM 3352 O  O   . HOH I 7 .   ? 28.753  54.370 9.715   1.00 31.82  ? 536 HOH A O   1 
HETATM 3353 O  O   . HOH I 7 .   ? 6.651   12.443 -15.164 1.00 37.12  ? 537 HOH A O   1 
HETATM 3354 O  O   . HOH I 7 .   ? 21.168  62.023 18.058  1.00 53.59  ? 538 HOH A O   1 
HETATM 3355 O  O   . HOH I 7 .   ? -6.748  10.596 -9.301  1.00 42.64  ? 539 HOH A O   1 
HETATM 3356 O  O   . HOH I 7 .   ? 1.099   12.078 15.674  1.00 45.89  ? 540 HOH A O   1 
HETATM 3357 O  O   . HOH I 7 .   ? 29.231  51.816 13.123  1.00 45.20  ? 541 HOH A O   1 
HETATM 3358 O  O   . HOH I 7 .   ? 3.894   21.640 -8.124  1.00 26.24  ? 542 HOH A O   1 
HETATM 3359 O  O   . HOH I 7 .   ? 29.323  52.385 15.940  1.00 46.75  ? 543 HOH A O   1 
HETATM 3360 O  O   . HOH I 7 .   ? 23.421  29.271 -0.539  1.00 40.87  ? 544 HOH A O   1 
HETATM 3361 O  O   . HOH I 7 .   ? 5.636   18.770 6.081   1.00 29.95  ? 545 HOH A O   1 
HETATM 3362 O  O   . HOH I 7 .   ? 30.550  21.334 -10.415 1.00 39.19  ? 546 HOH A O   1 
HETATM 3363 O  O   . HOH I 7 .   ? 5.768   5.353  11.710  1.00 31.10  ? 547 HOH A O   1 
HETATM 3364 O  O   . HOH I 7 .   ? 29.158  38.518 1.571   1.00 24.47  ? 548 HOH A O   1 
HETATM 3365 O  O   . HOH I 7 .   ? 20.315  41.603 16.731  1.00 28.10  ? 549 HOH A O   1 
HETATM 3366 O  O   . HOH I 7 .   ? -1.220  19.737 10.704  1.00 33.00  ? 550 HOH A O   1 
HETATM 3367 O  O   . HOH I 7 .   ? 15.013  45.835 14.336  1.00 31.16  ? 551 HOH A O   1 
HETATM 3368 O  O   . HOH I 7 .   ? 14.665  37.928 7.664   1.00 35.47  ? 552 HOH A O   1 
HETATM 3369 O  O   . HOH I 7 .   ? 22.213  23.873 9.748   1.00 44.01  ? 553 HOH A O   1 
HETATM 3370 O  O   . HOH I 7 .   ? -0.249  30.223 1.937   1.00 40.50  ? 554 HOH A O   1 
HETATM 3371 O  O   . HOH I 7 .   ? 26.759  3.983  -10.334 1.00 37.61  ? 555 HOH A O   1 
HETATM 3372 O  O   . HOH I 7 .   ? 10.421  5.560  16.047  1.00 37.27  ? 556 HOH A O   1 
HETATM 3373 O  O   . HOH I 7 .   ? 7.861   15.376 19.102  1.00 38.55  ? 557 HOH A O   1 
HETATM 3374 O  O   . HOH I 7 .   ? 17.665  39.794 11.496  1.00 36.50  ? 558 HOH A O   1 
HETATM 3375 O  O   . HOH I 7 .   ? -0.500  19.671 -1.246  1.00 35.79  ? 559 HOH A O   1 
HETATM 3376 O  O   . HOH I 7 .   ? 20.390  28.417 5.484   1.00 43.17  ? 560 HOH A O   1 
HETATM 3377 O  O   . HOH I 7 .   ? 11.369  11.168 -9.204  1.00 26.58  ? 561 HOH A O   1 
HETATM 3378 O  O   . HOH I 7 .   ? 27.899  6.039  -11.497 1.00 40.41  ? 562 HOH A O   1 
HETATM 3379 O  O   . HOH I 7 .   ? -5.663  20.821 6.491   1.00 41.22  ? 563 HOH A O   1 
HETATM 3380 O  O   . HOH I 7 .   ? 14.029  40.360 1.140   1.00 35.30  ? 564 HOH A O   1 
HETATM 3381 O  O   . HOH I 7 .   ? 26.243  56.664 3.909   1.00 29.57  ? 565 HOH A O   1 
HETATM 3382 O  O   . HOH I 7 .   ? 29.546  52.045 10.038  1.00 31.70  ? 566 HOH A O   1 
HETATM 3383 O  O   . HOH I 7 .   ? 27.468  50.249 1.447   1.00 28.92  ? 567 HOH A O   1 
HETATM 3384 O  O   . HOH I 7 .   ? 13.090  18.147 -10.091 1.00 36.56  ? 568 HOH A O   1 
HETATM 3385 O  O   . HOH I 7 .   ? 18.801  21.254 16.302  1.00 50.67  ? 569 HOH A O   1 
HETATM 3386 O  O   . HOH I 7 .   ? 20.509  32.705 2.027   1.00 31.97  ? 570 HOH A O   1 
HETATM 3387 O  O   . HOH I 7 .   ? 27.210  26.072 -0.809  1.00 29.85  ? 571 HOH A O   1 
HETATM 3388 O  O   . HOH I 7 .   ? 20.280  4.390  4.746   1.00 39.56  ? 572 HOH A O   1 
HETATM 3389 O  O   . HOH I 7 .   ? 4.084   1.454  4.377   1.00 38.97  ? 573 HOH A O   1 
HETATM 3390 O  O   . HOH I 7 .   ? 32.430  30.588 17.023  1.00 53.14  ? 574 HOH A O   1 
HETATM 3391 O  O   . HOH I 7 .   ? 31.794  28.404 16.062  1.00 42.31  ? 575 HOH A O   1 
HETATM 3392 O  O   . HOH I 7 .   ? 21.765  3.629  10.744  1.00 33.99  ? 576 HOH A O   1 
HETATM 3393 O  O   . HOH I 7 .   ? -3.674  13.047 12.193  1.00 54.82  ? 577 HOH A O   1 
HETATM 3394 O  O   . HOH I 7 .   ? 17.212  1.878  10.367  1.00 42.85  ? 578 HOH A O   1 
HETATM 3395 O  O   . HOH I 7 .   ? 35.412  55.389 14.421  1.00 37.64  ? 579 HOH A O   1 
HETATM 3396 O  O   . HOH I 7 .   ? 15.780  0.034  -12.137 1.00 42.29  ? 580 HOH A O   1 
HETATM 3397 O  O   . HOH I 7 .   ? 35.600  39.252 8.723   1.00 38.14  ? 581 HOH A O   1 
HETATM 3398 O  O   . HOH I 7 .   ? -6.111  4.992  5.345   1.00 42.99  ? 582 HOH A O   1 
HETATM 3399 O  O   . HOH I 7 .   ? 3.448   18.311 7.899   1.00 30.35  ? 583 HOH A O   1 
HETATM 3400 O  O   . HOH I 7 .   ? 4.806   21.687 -11.317 1.00 47.94  ? 584 HOH A O   1 
HETATM 3401 O  O   . HOH I 7 .   ? -1.157  14.490 12.311  1.00 31.20  ? 585 HOH A O   1 
HETATM 3402 O  O   . HOH I 7 .   ? 30.188  46.414 19.608  1.00 34.24  ? 586 HOH A O   1 
HETATM 3403 O  O   . HOH I 7 .   ? 18.131  36.216 9.490   1.00 38.41  ? 587 HOH A O   1 
HETATM 3404 O  O   . HOH I 7 .   ? 7.717   18.071 16.606  1.00 45.63  ? 588 HOH A O   1 
HETATM 3405 O  O   . HOH I 7 .   ? 25.564  13.798 -14.191 1.00 37.72  ? 589 HOH A O   1 
HETATM 3406 O  O   . HOH I 7 .   ? 18.769  27.235 3.762   1.00 46.76  ? 590 HOH A O   1 
HETATM 3407 O  O   . HOH I 7 .   ? 10.965  43.819 6.591   1.00 36.01  ? 591 HOH A O   1 
HETATM 3408 O  O   . HOH I 7 .   ? 24.267  3.871  -11.387 1.00 36.75  ? 592 HOH A O   1 
HETATM 3409 O  O   . HOH I 7 .   ? -6.490  16.700 2.140   1.00 42.87  ? 593 HOH A O   1 
HETATM 3410 O  O   . HOH I 7 .   ? 8.176   20.151 10.072  1.00 44.20  ? 594 HOH A O   1 
HETATM 3411 O  O   . HOH I 7 .   ? 4.657   -4.903 13.714  1.00 41.87  ? 595 HOH A O   1 
HETATM 3412 O  O   . HOH I 7 .   ? 26.784  37.427 18.556  1.00 28.01  ? 596 HOH A O   1 
HETATM 3413 O  O   . HOH I 7 .   ? 11.238  54.252 12.209  1.00 46.78  ? 597 HOH A O   1 
HETATM 3414 O  O   . HOH I 7 .   ? 23.971  17.533 -11.735 1.00 42.10  ? 598 HOH A O   1 
HETATM 3415 O  O   . HOH I 7 .   ? 28.298  25.732 10.803  1.00 43.90  ? 599 HOH A O   1 
HETATM 3416 O  O   . HOH I 7 .   ? 30.735  47.687 16.177  1.00 44.19  ? 600 HOH A O   1 
HETATM 3417 O  O   . HOH I 7 .   ? 26.154  3.821  4.534   1.00 36.73  ? 601 HOH A O   1 
HETATM 3418 O  O   . HOH I 7 .   ? 17.926  53.767 0.674   1.00 42.11  ? 602 HOH A O   1 
HETATM 3419 O  O   . HOH I 7 .   ? 36.562  35.544 8.817   1.00 42.26  ? 603 HOH A O   1 
HETATM 3420 O  O   . HOH I 7 .   ? 33.525  24.402 1.676   1.00 37.70  ? 604 HOH A O   1 
HETATM 3421 O  O   . HOH I 7 .   ? -2.065  5.543  -10.774 1.00 43.85  ? 605 HOH A O   1 
HETATM 3422 O  O   . HOH I 7 .   ? 22.679  19.441 -12.787 1.00 41.98  ? 606 HOH A O   1 
HETATM 3423 O  O   . HOH I 7 .   ? 21.154  18.938 -8.914  1.00 49.36  ? 607 HOH A O   1 
HETATM 3424 O  O   . HOH I 7 .   ? 39.257  21.149 3.392   1.00 57.27  ? 608 HOH A O   1 
HETATM 3425 O  O   . HOH I 7 .   ? -7.321  18.891 5.582   1.00 41.87  ? 609 HOH A O   1 
HETATM 3426 O  O   . HOH I 7 .   ? 23.094  36.784 21.522  1.00 37.18  ? 610 HOH A O   1 
HETATM 3427 O  O   . HOH I 7 .   ? 12.642  39.425 6.277   1.00 47.08  ? 611 HOH A O   1 
HETATM 3428 O  O   . HOH I 7 .   ? 15.926  29.029 6.911   1.00 48.51  ? 612 HOH A O   1 
HETATM 3429 O  O   . HOH I 7 .   ? 20.620  23.218 5.757   1.00 35.09  ? 613 HOH A O   1 
HETATM 3430 O  O   . HOH I 7 .   ? 28.943  3.230  4.826   1.00 51.13  ? 614 HOH A O   1 
HETATM 3431 O  O   . HOH I 7 .   ? 34.087  22.830 -5.264  1.00 43.05  ? 615 HOH A O   1 
HETATM 3432 O  O   . HOH I 7 .   ? 31.646  24.639 -6.722  1.00 47.04  ? 616 HOH A O   1 
HETATM 3433 O  O   . HOH I 7 .   ? 35.037  9.663  -9.863  1.00 53.12  ? 617 HOH A O   1 
HETATM 3434 O  O   . HOH I 7 .   ? -3.232  2.426  6.943   1.00 42.89  ? 618 HOH A O   1 
HETATM 3435 O  O   . HOH I 7 .   ? 0.744   30.181 -1.043  1.00 42.98  ? 619 HOH A O   1 
HETATM 3436 O  O   . HOH I 7 .   ? 14.702  9.960  -12.889 1.00 43.29  ? 620 HOH A O   1 
HETATM 3437 O  O   . HOH I 7 .   ? 20.057  29.341 9.147   1.00 50.46  ? 621 HOH A O   1 
HETATM 3438 O  O   . HOH I 7 .   ? 39.642  20.420 0.261   1.00 58.57  ? 622 HOH A O   1 
HETATM 3439 O  O   . HOH I 7 .   ? 24.852  34.392 18.077  1.00 40.74  ? 623 HOH A O   1 
HETATM 3440 O  O   . HOH I 7 .   ? 13.721  11.470 -17.118 1.00 49.07  ? 624 HOH A O   1 
HETATM 3441 O  O   . HOH I 7 .   ? 14.929  0.134  14.971  1.00 45.15  ? 625 HOH A O   1 
HETATM 3442 O  O   . HOH I 7 .   ? 23.499  33.597 15.539  1.00 32.88  ? 626 HOH A O   1 
HETATM 3443 O  O   . HOH I 7 .   ? 27.281  46.979 1.093   1.00 39.43  ? 627 HOH A O   1 
HETATM 3444 O  O   . HOH I 7 .   ? -2.170  4.396  -2.587  1.00 48.65  ? 628 HOH A O   1 
HETATM 3445 O  O   . HOH I 7 .   ? 10.865  0.641  -9.159  1.00 51.24  ? 629 HOH A O   1 
HETATM 3446 O  O   . HOH I 7 .   ? -3.333  5.857  -6.690  1.00 42.80  ? 630 HOH A O   1 
HETATM 3447 O  O   . HOH I 7 .   ? 13.936  6.695  -13.091 1.00 39.00  ? 631 HOH A O   1 
HETATM 3448 O  O   . HOH I 7 .   ? 12.676  20.062 -12.093 1.00 41.65  ? 632 HOH A O   1 
HETATM 3449 O  O   . HOH I 7 .   ? 28.701  28.279 -5.180  1.00 47.62  ? 633 HOH A O   1 
HETATM 3450 O  O   . HOH I 7 .   ? 29.942  26.339 -6.234  1.00 43.24  ? 634 HOH A O   1 
HETATM 3451 O  O   . HOH I 7 .   ? 2.397   0.434  -4.704  1.00 42.04  ? 635 HOH A O   1 
HETATM 3452 O  O   . HOH I 7 .   ? 26.732  44.855 24.199  1.00 33.35  ? 636 HOH A O   1 
HETATM 3453 O  O   . HOH I 7 .   ? 26.015  27.509 -5.656  1.00 30.70  ? 637 HOH A O   1 
HETATM 3454 O  O   . HOH I 7 .   ? 3.748   20.137 9.711   1.00 39.44  ? 638 HOH A O   1 
HETATM 3455 O  O   . HOH I 7 .   ? 18.599  8.861  -13.811 1.00 38.42  ? 639 HOH A O   1 
HETATM 3456 O  O   . HOH I 7 .   ? 5.331   19.728 11.615  1.00 39.77  ? 640 HOH A O   1 
HETATM 3457 O  O   . HOH I 7 .   ? 32.321  27.698 -6.396  1.00 43.11  ? 641 HOH A O   1 
HETATM 3458 O  O   . HOH I 7 .   ? 19.015  32.205 7.125   1.00 31.37  ? 642 HOH A O   1 
HETATM 3459 O  O   . HOH I 7 .   ? 4.240   7.905  -13.056 1.00 50.73  ? 643 HOH A O   1 
HETATM 3460 O  O   . HOH I 7 .   ? -6.472  18.838 -0.293  1.00 49.96  ? 644 HOH A O   1 
HETATM 3461 O  O   . HOH I 7 .   ? 20.750  23.971 3.239   1.00 24.14  ? 645 HOH A O   1 
HETATM 3462 O  O   . HOH I 7 .   ? 29.137  52.348 1.436   1.00 43.97  ? 646 HOH A O   1 
HETATM 3463 O  O   . HOH I 7 .   ? 25.949  55.503 1.450   1.00 40.02  ? 647 HOH A O   1 
HETATM 3464 O  O   . HOH I 7 .   ? 23.934  27.875 11.750  1.00 29.10  ? 648 HOH A O   1 
HETATM 3465 O  O   . HOH I 7 .   ? 28.793  55.918 4.554   1.00 33.93  ? 649 HOH A O   1 
HETATM 3466 O  O   . HOH I 7 .   ? 34.314  38.391 2.816   1.00 52.11  ? 650 HOH A O   1 
HETATM 3467 O  O   . HOH I 7 .   ? 16.524  33.951 8.018   1.00 49.69  ? 651 HOH A O   1 
HETATM 3468 O  O   . HOH I 7 .   ? -3.038  3.704  2.390   1.00 45.14  ? 652 HOH A O   1 
HETATM 3469 O  O   . HOH I 7 .   ? 18.203  2.185  -12.199 1.00 39.96  ? 653 HOH A O   1 
HETATM 3470 O  O   . HOH I 7 .   ? -1.668  0.431  5.820   1.00 42.93  ? 654 HOH A O   1 
HETATM 3471 O  O   . HOH I 7 .   ? 17.144  8.784  -11.997 1.00 37.23  ? 655 HOH A O   1 
HETATM 3472 O  O   . HOH I 7 .   ? 30.786  5.156  -0.049  1.00 33.78  ? 656 HOH A O   1 
HETATM 3473 O  O   . HOH I 7 .   ? 19.866  31.395 4.418   1.00 42.54  ? 657 HOH A O   1 
HETATM 3474 O  O   . HOH I 7 .   ? 17.631  4.516  -13.184 1.00 37.18  ? 658 HOH A O   1 
HETATM 3475 O  O   . HOH I 7 .   ? -8.092  17.224 -1.140  1.00 42.26  ? 659 HOH A O   1 
HETATM 3476 O  O   . HOH I 7 .   ? 13.829  37.734 10.194  1.00 45.23  ? 660 HOH A O   1 
HETATM 3477 O  O   . HOH I 7 .   ? 14.780  7.505  -15.667 1.00 47.72  ? 661 HOH A O   1 
HETATM 3478 O  O   . HOH J 7 .   ? 29.669  48.310 -16.034 1.00 48.26  ? 101 HOH B O   1 
HETATM 3479 O  O   . HOH J 7 .   ? -1.307  31.846 -10.087 1.00 38.30  ? 102 HOH B O   1 
HETATM 3480 O  O   . HOH J 7 .   ? 35.274  40.094 -10.617 1.00 45.24  ? 103 HOH B O   1 
HETATM 3481 O  O   . HOH J 7 .   ? 34.156  42.191 0.241   1.00 38.27  ? 104 HOH B O   1 
HETATM 3482 O  O   . HOH J 7 .   ? 29.918  44.595 -17.061 1.00 40.64  ? 105 HOH B O   1 
HETATM 3483 O  O   . HOH J 7 .   ? 6.436   34.637 -2.951  1.00 51.35  ? 106 HOH B O   1 
HETATM 3484 O  O   . HOH J 7 .   ? 37.274  45.182 -15.122 1.00 45.27  ? 107 HOH B O   1 
HETATM 3485 O  O   . HOH J 7 .   ? 7.391   24.504 -13.239 1.00 38.48  ? 108 HOH B O   1 
HETATM 3486 O  O   . HOH J 7 .   ? 12.144  22.849 -11.948 1.00 41.09  ? 109 HOH B O   1 
HETATM 3487 O  O   . HOH J 7 .   ? 35.635  40.781 -13.748 1.00 58.73  ? 110 HOH B O   1 
HETATM 3488 O  O   . HOH J 7 .   ? 30.890  48.808 -18.774 1.00 47.42  ? 111 HOH B O   1 
HETATM 3489 O  O   . HOH J 7 .   ? 41.670  52.499 -6.588  1.00 35.98  ? 112 HOH B O   1 
HETATM 3490 O  O   . HOH J 7 .   ? 8.731   43.774 -17.969 1.00 30.80  ? 113 HOH B O   1 
HETATM 3491 O  O   . HOH J 7 .   ? 7.118   36.096 -16.888 1.00 27.96  ? 114 HOH B O   1 
HETATM 3492 O  O   . HOH J 7 .   ? 2.701   37.132 -9.717  1.00 47.98  ? 115 HOH B O   1 
HETATM 3493 O  O   . HOH J 7 .   ? 20.294  46.367 -5.464  1.00 25.19  ? 116 HOH B O   1 
HETATM 3494 O  O   . HOH J 7 .   ? 14.286  30.396 0.736   1.00 44.42  ? 117 HOH B O   1 
HETATM 3495 O  O   . HOH J 7 .   ? 14.130  25.496 -11.520 1.00 32.80  ? 118 HOH B O   1 
HETATM 3496 O  O   . HOH J 7 .   ? 1.189   37.207 -19.988 1.00 27.47  ? 119 HOH B O   1 
HETATM 3497 O  O   . HOH J 7 .   ? 10.717  31.056 -19.085 1.00 36.41  ? 120 HOH B O   1 
HETATM 3498 O  O   . HOH J 7 .   ? 11.523  33.269 -22.194 1.00 36.69  ? 121 HOH B O   1 
HETATM 3499 O  O   . HOH J 7 .   ? 39.181  51.609 -3.956  1.00 40.01  ? 122 HOH B O   1 
HETATM 3500 O  O   . HOH J 7 .   ? -5.192  23.955 -6.526  1.00 30.05  ? 123 HOH B O   1 
HETATM 3501 O  O   . HOH J 7 .   ? 0.110   36.659 -13.468 1.00 35.19  ? 124 HOH B O   1 
HETATM 3502 O  O   . HOH J 7 .   ? 2.044   26.006 -3.300  1.00 27.94  ? 125 HOH B O   1 
HETATM 3503 O  O   . HOH J 7 .   ? 16.722  51.269 -5.364  1.00 45.91  ? 126 HOH B O   1 
HETATM 3504 O  O   . HOH J 7 .   ? 17.491  32.812 -19.814 1.00 36.29  ? 127 HOH B O   1 
HETATM 3505 O  O   . HOH J 7 .   ? 8.897   27.540 -3.094  1.00 25.99  ? 128 HOH B O   1 
HETATM 3506 O  O   . HOH J 7 .   ? 12.734  30.996 3.583   1.00 44.11  ? 129 HOH B O   1 
HETATM 3507 O  O   . HOH J 7 .   ? 31.747  32.908 -8.502  1.00 49.97  ? 130 HOH B O   1 
HETATM 3508 O  O   . HOH J 7 .   ? 34.604  54.736 -4.307  1.00 51.28  ? 131 HOH B O   1 
HETATM 3509 O  O   . HOH J 7 .   ? 28.212  35.021 -7.145  1.00 26.52  ? 132 HOH B O   1 
HETATM 3510 O  O   . HOH J 7 .   ? 21.993  21.790 -11.319 1.00 36.89  ? 133 HOH B O   1 
HETATM 3511 O  O   . HOH J 7 .   ? 19.785  51.473 -9.698  1.00 34.82  ? 134 HOH B O   1 
HETATM 3512 O  O   . HOH J 7 .   ? 8.460   39.347 -8.019  1.00 40.84  ? 135 HOH B O   1 
HETATM 3513 O  O   . HOH J 7 .   ? 22.234  53.875 -5.971  1.00 42.83  ? 136 HOH B O   1 
HETATM 3514 O  O   . HOH J 7 .   ? 20.052  27.186 -5.285  1.00 22.65  ? 137 HOH B O   1 
HETATM 3515 O  O   . HOH J 7 .   ? 8.937   23.047 6.993   1.00 34.83  ? 138 HOH B O   1 
HETATM 3516 O  O   . HOH J 7 .   ? 29.408  33.494 -13.561 1.00 45.92  ? 139 HOH B O   1 
HETATM 3517 O  O   . HOH J 7 .   ? 0.062   31.952 -3.243  1.00 33.93  ? 140 HOH B O   1 
HETATM 3518 O  O   . HOH J 7 .   ? 34.342  42.412 -14.694 1.00 48.38  ? 141 HOH B O   1 
HETATM 3519 O  O   . HOH J 7 .   ? 35.017  37.410 -4.766  1.00 40.71  ? 142 HOH B O   1 
HETATM 3520 O  O   . HOH J 7 .   ? 7.426   27.797 1.238   1.00 27.13  ? 143 HOH B O   1 
HETATM 3521 O  O   . HOH J 7 .   ? 27.174  50.283 -12.890 1.00 33.45  ? 144 HOH B O   1 
HETATM 3522 O  O   . HOH J 7 .   ? 13.837  43.272 -20.939 1.00 42.41  ? 145 HOH B O   1 
HETATM 3523 O  O   . HOH J 7 .   ? 15.262  27.445 -13.512 1.00 47.35  ? 146 HOH B O   1 
HETATM 3524 O  O   . HOH J 7 .   ? 6.493   26.671 4.901   1.00 32.36  ? 147 HOH B O   1 
HETATM 3525 O  O   . HOH J 7 .   ? 30.841  39.892 0.669   1.00 44.04  ? 148 HOH B O   1 
HETATM 3526 O  O   . HOH J 7 .   ? 18.654  25.000 1.985   1.00 29.80  ? 149 HOH B O   1 
HETATM 3527 O  O   . HOH J 7 .   ? 9.233   21.063 -15.172 1.00 42.21  ? 150 HOH B O   1 
HETATM 3528 O  O   . HOH J 7 .   ? 7.734   29.213 -1.064  1.00 31.80  ? 151 HOH B O   1 
HETATM 3529 O  O   . HOH J 7 .   ? 26.994  26.483 -10.802 1.00 35.59  ? 152 HOH B O   1 
HETATM 3530 O  O   . HOH J 7 .   ? 27.390  49.131 -1.082  1.00 32.12  ? 153 HOH B O   1 
HETATM 3531 O  O   . HOH J 7 .   ? 29.042  50.611 -2.715  1.00 39.81  ? 154 HOH B O   1 
HETATM 3532 O  O   . HOH J 7 .   ? 12.190  37.915 -20.825 1.00 30.94  ? 155 HOH B O   1 
HETATM 3533 O  O   . HOH J 7 .   ? 31.357  35.692 -15.013 1.00 43.36  ? 156 HOH B O   1 
HETATM 3534 O  O   . HOH J 7 .   ? 34.647  43.726 -5.729  1.00 36.68  ? 157 HOH B O   1 
HETATM 3535 O  O   . HOH J 7 .   ? 7.044   28.813 -13.829 1.00 24.26  ? 158 HOH B O   1 
HETATM 3536 O  O   . HOH J 7 .   ? 15.839  32.831 0.946   1.00 35.86  ? 159 HOH B O   1 
HETATM 3537 O  O   . HOH J 7 .   ? 33.013  46.952 -7.450  1.00 27.39  ? 160 HOH B O   1 
HETATM 3538 O  O   . HOH J 7 .   ? 14.651  43.601 -4.456  1.00 28.85  ? 161 HOH B O   1 
HETATM 3539 O  O   . HOH J 7 .   ? 24.871  45.516 -22.896 1.00 40.67  ? 162 HOH B O   1 
HETATM 3540 O  O   . HOH J 7 .   ? 38.011  44.406 -7.574  1.00 41.90  ? 163 HOH B O   1 
HETATM 3541 O  O   . HOH J 7 .   ? 34.656  33.658 -7.419  1.00 48.26  ? 164 HOH B O   1 
HETATM 3542 O  O   . HOH J 7 .   ? 7.618   25.121 -3.041  1.00 22.77  ? 165 HOH B O   1 
HETATM 3543 O  O   . HOH J 7 .   ? 15.225  28.538 -17.178 1.00 33.98  ? 166 HOH B O   1 
HETATM 3544 O  O   . HOH J 7 .   ? 9.252   44.785 -14.008 1.00 28.79  ? 167 HOH B O   1 
HETATM 3545 O  O   . HOH J 7 .   ? -1.047  36.213 -17.444 1.00 35.59  ? 168 HOH B O   1 
HETATM 3546 O  O   . HOH J 7 .   ? 20.749  33.935 -17.720 1.00 41.09  ? 169 HOH B O   1 
HETATM 3547 O  O   . HOH J 7 .   ? 6.150   41.213 -13.855 1.00 27.09  ? 170 HOH B O   1 
HETATM 3548 O  O   . HOH J 7 .   ? 27.432  47.316 -3.634  1.00 30.85  ? 171 HOH B O   1 
HETATM 3549 O  O   . HOH J 7 .   ? 22.450  49.484 -12.097 1.00 25.27  ? 172 HOH B O   1 
HETATM 3550 O  O   . HOH J 7 .   ? 20.088  30.788 0.434   1.00 35.85  ? 173 HOH B O   1 
HETATM 3551 O  O   . HOH J 7 .   ? -2.134  30.296 -7.361  1.00 27.15  ? 174 HOH B O   1 
HETATM 3552 O  O   . HOH J 7 .   ? 32.394  55.164 -14.179 1.00 33.45  ? 175 HOH B O   1 
HETATM 3553 O  O   . HOH J 7 .   ? 39.087  45.860 -10.886 1.00 45.78  ? 176 HOH B O   1 
HETATM 3554 O  O   . HOH J 7 .   ? 30.132  53.397 -5.125  1.00 40.73  ? 177 HOH B O   1 
HETATM 3555 O  O   . HOH J 7 .   ? 23.774  24.727 -11.462 1.00 30.35  ? 178 HOH B O   1 
HETATM 3556 O  O   . HOH J 7 .   ? 2.727   39.876 -13.345 1.00 36.25  ? 179 HOH B O   1 
HETATM 3557 O  O   . HOH J 7 .   ? -0.680  23.840 -3.875  1.00 30.42  ? 180 HOH B O   1 
HETATM 3558 O  O   . HOH J 7 .   ? 21.581  36.474 -18.467 1.00 28.76  ? 181 HOH B O   1 
HETATM 3559 O  O   . HOH J 7 .   ? 14.112  36.046 -17.821 1.00 36.34  ? 182 HOH B O   1 
HETATM 3560 O  O   . HOH J 7 .   ? 19.337  54.075 -3.016  1.00 57.03  ? 183 HOH B O   1 
HETATM 3561 O  O   . HOH J 7 .   ? 26.108  48.149 -22.689 1.00 40.77  ? 184 HOH B O   1 
HETATM 3562 O  O   . HOH J 7 .   ? 1.536   33.817 -7.206  1.00 43.73  ? 185 HOH B O   1 
HETATM 3563 O  O   . HOH J 7 .   ? 25.652  44.109 -2.022  1.00 27.89  ? 186 HOH B O   1 
HETATM 3564 O  O   . HOH J 7 .   ? 22.195  31.177 -16.576 1.00 39.11  ? 187 HOH B O   1 
HETATM 3565 O  O   . HOH J 7 .   ? 14.914  36.582 -3.352  1.00 21.73  ? 188 HOH B O   1 
HETATM 3566 O  O   . HOH J 7 .   ? 17.718  46.489 -6.073  1.00 26.97  ? 189 HOH B O   1 
HETATM 3567 O  O   . HOH J 7 .   ? -0.434  36.166 -10.676 1.00 40.33  ? 190 HOH B O   1 
HETATM 3568 O  O   . HOH J 7 .   ? 15.645  45.665 -21.496 1.00 52.26  ? 191 HOH B O   1 
HETATM 3569 O  O   . HOH J 7 .   ? 20.018  46.749 -17.546 1.00 35.64  ? 192 HOH B O   1 
HETATM 3570 O  O   . HOH J 7 .   ? 24.612  32.009 -24.984 1.00 52.47  ? 193 HOH B O   1 
HETATM 3571 O  O   . HOH J 7 .   ? 28.667  56.124 -9.068  1.00 45.60  ? 194 HOH B O   1 
HETATM 3572 O  O   . HOH J 7 .   ? 3.002   34.825 -4.202  1.00 35.63  ? 195 HOH B O   1 
HETATM 3573 O  O   . HOH J 7 .   ? 19.505  49.547 -13.738 1.00 35.19  ? 196 HOH B O   1 
HETATM 3574 O  O   . HOH J 7 .   ? 17.195  43.996 -5.036  1.00 23.33  ? 197 HOH B O   1 
HETATM 3575 O  O   . HOH J 7 .   ? 17.197  30.936 -16.634 1.00 41.34  ? 198 HOH B O   1 
HETATM 3576 O  O   . HOH J 7 .   ? 19.172  22.397 -10.790 1.00 38.42  ? 199 HOH B O   1 
HETATM 3577 O  O   . HOH J 7 .   ? 24.275  51.437 -8.255  1.00 32.23  ? 200 HOH B O   1 
HETATM 3578 O  O   . HOH J 7 .   ? 7.598   32.195 -0.561  1.00 51.62  ? 201 HOH B O   1 
HETATM 3579 O  O   . HOH J 7 .   ? 13.977  48.145 -9.721  1.00 29.05  ? 202 HOH B O   1 
HETATM 3580 O  O   . HOH J 7 .   ? 24.586  45.707 -4.127  1.00 26.93  ? 203 HOH B O   1 
HETATM 3581 O  O   . HOH J 7 .   ? 17.765  44.008 -1.964  1.00 33.42  ? 204 HOH B O   1 
HETATM 3582 O  O   . HOH J 7 .   ? 25.339  27.375 -14.347 1.00 25.31  ? 205 HOH B O   1 
HETATM 3583 O  O   . HOH J 7 .   ? 34.553  46.478 -5.189  1.00 35.31  ? 206 HOH B O   1 
HETATM 3584 O  O   . HOH J 7 .   ? 19.156  50.212 -19.228 1.00 50.70  ? 207 HOH B O   1 
HETATM 3585 O  O   . HOH J 7 .   ? 19.339  24.788 -11.412 1.00 38.12  ? 208 HOH B O   1 
HETATM 3586 O  O   . HOH J 7 .   ? 28.072  53.022 -2.556  1.00 42.59  ? 209 HOH B O   1 
HETATM 3587 O  O   . HOH J 7 .   ? 30.431  55.488 -16.391 1.00 37.95  ? 210 HOH B O   1 
HETATM 3588 O  O   . HOH J 7 .   ? 13.501  26.004 -14.840 1.00 33.00  ? 211 HOH B O   1 
HETATM 3589 O  O   . HOH J 7 .   ? 22.096  28.386 -3.960  1.00 35.81  ? 212 HOH B O   1 
HETATM 3590 O  O   . HOH J 7 .   ? 13.536  27.975 6.315   1.00 38.25  ? 213 HOH B O   1 
HETATM 3591 O  O   . HOH J 7 .   ? 34.158  53.452 -13.763 1.00 35.79  ? 214 HOH B O   1 
HETATM 3592 O  O   . HOH J 7 .   ? 10.598  29.515 -16.653 1.00 33.13  ? 215 HOH B O   1 
HETATM 3593 O  O   . HOH J 7 .   ? 7.841   29.610 -16.172 1.00 35.99  ? 216 HOH B O   1 
HETATM 3594 O  O   . HOH J 7 .   ? 6.602   43.741 -13.938 1.00 36.51  ? 217 HOH B O   1 
HETATM 3595 O  O   . HOH J 7 .   ? 33.029  57.691 -13.278 1.00 36.77  ? 218 HOH B O   1 
HETATM 3596 O  O   . HOH J 7 .   ? 7.359   20.538 7.272   1.00 50.10  ? 219 HOH B O   1 
HETATM 3597 O  O   . HOH J 7 .   ? 11.734  27.227 -17.165 1.00 39.03  ? 220 HOH B O   1 
HETATM 3598 O  O   . HOH J 7 .   ? 36.358  54.521 -12.497 1.00 38.03  ? 221 HOH B O   1 
HETATM 3599 O  O   . HOH J 7 .   ? 7.022   22.267 -12.231 1.00 40.21  ? 222 HOH B O   1 
HETATM 3600 O  O   . HOH J 7 .   ? 27.206  45.662 -0.806  1.00 40.16  ? 223 HOH B O   1 
HETATM 3601 O  O   . HOH J 7 .   ? 0.040   33.812 -9.655  1.00 39.32  ? 224 HOH B O   1 
HETATM 3602 O  O   . HOH J 7 .   ? 36.083  55.874 -10.158 1.00 32.94  ? 225 HOH B O   1 
HETATM 3603 O  O   . HOH J 7 .   ? 24.760  24.741 -13.781 1.00 40.39  ? 226 HOH B O   1 
HETATM 3604 O  O   . HOH J 7 .   ? 36.771  42.865 -3.474  1.00 48.78  ? 227 HOH B O   1 
HETATM 3605 O  O   . HOH J 7 .   ? 35.369  39.895 -7.124  1.00 55.05  ? 228 HOH B O   1 
HETATM 3606 O  O   . HOH J 7 .   ? -1.174  34.600 -14.163 1.00 43.54  ? 229 HOH B O   1 
HETATM 3607 O  O   . HOH J 7 .   ? 19.904  52.075 -12.581 1.00 44.16  ? 230 HOH B O   1 
HETATM 3608 O  O   . HOH J 7 .   ? 3.116   25.677 -14.092 1.00 36.23  ? 231 HOH B O   1 
HETATM 3609 O  O   . HOH J 7 .   ? 9.272   46.051 -16.572 1.00 34.43  ? 232 HOH B O   1 
HETATM 3610 O  O   . HOH J 7 .   ? 5.740   26.472 -14.337 1.00 31.37  ? 233 HOH B O   1 
HETATM 3611 O  O   . HOH J 7 .   ? 35.826  44.564 -0.994  1.00 48.29  ? 234 HOH B O   1 
HETATM 3612 O  O   . HOH J 7 .   ? 11.544  42.892 -21.006 1.00 46.19  ? 235 HOH B O   1 
HETATM 3613 O  O   . HOH J 7 .   ? 32.296  42.277 1.975   1.00 34.71  ? 236 HOH B O   1 
HETATM 3614 O  O   . HOH J 7 .   ? 15.388  44.488 -1.555  1.00 39.56  ? 237 HOH B O   1 
HETATM 3615 O  O   . HOH J 7 .   ? 19.971  29.691 2.704   1.00 54.37  ? 238 HOH B O   1 
HETATM 3616 O  O   . HOH J 7 .   ? 1.393   33.995 -2.426  1.00 48.11  ? 239 HOH B O   1 
HETATM 3617 O  O   . HOH J 7 .   ? -2.593  32.495 -3.681  1.00 35.67  ? 240 HOH B O   1 
HETATM 3618 O  O   . HOH J 7 .   ? 3.210   39.883 -10.287 1.00 45.96  ? 241 HOH B O   1 
HETATM 3619 O  O   . HOH J 7 .   ? 17.324  51.836 -8.856  1.00 41.93  ? 242 HOH B O   1 
HETATM 3620 O  O   . HOH J 7 .   ? -4.908  23.528 -3.976  1.00 32.57  ? 243 HOH B O   1 
HETATM 3621 O  O   . HOH J 7 .   ? 13.889  42.593 -0.563  1.00 42.96  ? 244 HOH B O   1 
HETATM 3622 O  O   . HOH J 7 .   ? 6.386   40.564 -8.653  1.00 41.02  ? 245 HOH B O   1 
HETATM 3623 O  O   . HOH J 7 .   ? 6.684   44.732 -19.437 1.00 46.34  ? 246 HOH B O   1 
HETATM 3624 O  O   . HOH K 7 .   ? 23.197  8.545  4.911   1.00 32.63  ? 101 HOH C O   1 
HETATM 3625 O  O   . HOH K 7 .   ? 21.613  2.596  8.021   1.00 35.51  ? 102 HOH C O   1 
HETATM 3626 O  O   . HOH K 7 .   ? 14.725  7.888  1.295   1.00 27.90  ? 103 HOH C O   1 
HETATM 3627 O  O   . HOH K 7 .   ? 9.571   1.185  2.755   1.00 37.70  ? 104 HOH C O   1 
HETATM 3628 O  O   . HOH K 7 .   ? 16.225  0.000  -0.000  0.50 25.32  ? 105 HOH C O   1 
HETATM 3629 O  O   . HOH K 7 .   ? 15.603  6.226  6.861   1.00 42.83  ? 106 HOH C O   1 
HETATM 3630 O  O   . HOH K 7 .   ? 9.800   2.409  -6.899  1.00 36.20  ? 107 HOH C O   1 
HETATM 3631 O  O   . HOH K 7 .   ? 12.959  11.215 1.774   1.00 33.87  ? 108 HOH C O   1 
HETATM 3632 O  O   . HOH K 7 .   ? 14.009  0.567  1.679   1.00 29.08  ? 109 HOH C O   1 
HETATM 3633 O  O   . HOH K 7 .   ? 12.131  7.628  0.359   1.00 26.60  ? 110 HOH C O   1 
HETATM 3634 O  O   . HOH K 7 .   ? 11.838  -0.000 0.000   0.50 34.92  ? 111 HOH C O   1 
HETATM 3635 O  O   . HOH K 7 .   ? 19.616  2.048  10.944  1.00 45.21  ? 112 HOH C O   1 
# 
