data_5U9M
# 
_entry.id   5U9M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.283 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5U9M         
WWPDB D_1000225539 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5U9M 
_pdbx_database_status.recvd_initial_deposition_date   2016-12-16 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Taylor, A.B.'  1 ? 
'Hart, P.J.'    2 ? 
'Winkler, D.D.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J. Biol. Chem.' 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                12025 
_citation.page_last                 12040 
_citation.title                     
'Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1074/jbc.M117.775981 
_citation.pdbx_database_id_PubMed   28533431 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Fetherolf, M.M.'    1 
primary 'Boyd, S.D.'         2 
primary 'Taylor, A.B.'       3 
primary 'Kim, H.J.'          4 
primary 'Wohlschlegel, J.A.' 5 
primary 'Blackburn, N.J.'    6 
primary 'Hart, P.J.'         7 
primary 'Winge, D.R.'        8 
primary 'Winkler, D.D.'      9 
# 
_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                     5U9M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     99.097 
_cell.length_a_esd                 ? 
_cell.length_b                     184.353 
_cell.length_b_esd                 ? 
_cell.length_c                     48.514 
_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             ? 
# 
_symmetry.entry_id                         5U9M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Superoxide dismutase [Cu-Zn]'            15836.590 2   1.15.1.1 H46R,H48Q         ? ? 
2 polymer     man 'Superoxide dismutase 1 copper chaperone' 27028.498 2   ?        E238A,E239A,R240A ? ? 
3 non-polymer syn 'ZINC ION'                                65.409    3   ?        ?                 ? ? 
4 water       nat water                                     18.015    120 ?        ?                 ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
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 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFRVQEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFRVQEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
A,C ? 
2 'polypeptide(L)' no no 
;TTNDTYEATYAIPMHCENCVNDIKACLKNVPGINSLNFDIEQQIMSVESSVAPSTIINTLRNCGKDAIIRGAGKPNSSAV
AILETFQKYTIDQKKDTAVRGLARIVQVGENKTLFDITVNGVPEAGNYHASIHEKGDVSKGVESTGKVWHKFDEPIECFN
ESDLGKNLYSGKTFLSAPLPTWQLIGRSFVISKSLNHPENEPSSVKDYSFLGVIARSAGVWENNKQVCACTGKTVWAAAK
DALANNIK
;
;TTNDTYEATYAIPMHCENCVNDIKACLKNVPGINSLNFDIEQQIMSVESSVAPSTIINTLRNCGKDAIIRGAGKPNSSAV
AILETFQKYTIDQKKDTAVRGLARIVQVGENKTLFDITVNGVPEAGNYHASIHEKGDVSKGVESTGKVWHKFDEPIECFN
ESDLGKNLYSGKTFLSAPLPTWQLIGRSFVISKSLNHPENEPSSVKDYSFLGVIARSAGVWENNKQVCACTGKTVWAAAK
DALANNIK
;
B,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  ARG n 
1 47  VAL n 
1 48  GLN n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
2 1   THR n 
2 2   THR n 
2 3   ASN n 
2 4   ASP n 
2 5   THR n 
2 6   TYR n 
2 7   GLU n 
2 8   ALA n 
2 9   THR n 
2 10  TYR n 
2 11  ALA n 
2 12  ILE n 
2 13  PRO n 
2 14  MET n 
2 15  HIS n 
2 16  CYS n 
2 17  GLU n 
2 18  ASN n 
2 19  CYS n 
2 20  VAL n 
2 21  ASN n 
2 22  ASP n 
2 23  ILE n 
2 24  LYS n 
2 25  ALA n 
2 26  CYS n 
2 27  LEU n 
2 28  LYS n 
2 29  ASN n 
2 30  VAL n 
2 31  PRO n 
2 32  GLY n 
2 33  ILE n 
2 34  ASN n 
2 35  SER n 
2 36  LEU n 
2 37  ASN n 
2 38  PHE n 
2 39  ASP n 
2 40  ILE n 
2 41  GLU n 
2 42  GLN n 
2 43  GLN n 
2 44  ILE n 
2 45  MET n 
2 46  SER n 
2 47  VAL n 
2 48  GLU n 
2 49  SER n 
2 50  SER n 
2 51  VAL n 
2 52  ALA n 
2 53  PRO n 
2 54  SER n 
2 55  THR n 
2 56  ILE n 
2 57  ILE n 
2 58  ASN n 
2 59  THR n 
2 60  LEU n 
2 61  ARG n 
2 62  ASN n 
2 63  CYS n 
2 64  GLY n 
2 65  LYS n 
2 66  ASP n 
2 67  ALA n 
2 68  ILE n 
2 69  ILE n 
2 70  ARG n 
2 71  GLY n 
2 72  ALA n 
2 73  GLY n 
2 74  LYS n 
2 75  PRO n 
2 76  ASN n 
2 77  SER n 
2 78  SER n 
2 79  ALA n 
2 80  VAL n 
2 81  ALA n 
2 82  ILE n 
2 83  LEU n 
2 84  GLU n 
2 85  THR n 
2 86  PHE n 
2 87  GLN n 
2 88  LYS n 
2 89  TYR n 
2 90  THR n 
2 91  ILE n 
2 92  ASP n 
2 93  GLN n 
2 94  LYS n 
2 95  LYS n 
2 96  ASP n 
2 97  THR n 
2 98  ALA n 
2 99  VAL n 
2 100 ARG n 
2 101 GLY n 
2 102 LEU n 
2 103 ALA n 
2 104 ARG n 
2 105 ILE n 
2 106 VAL n 
2 107 GLN n 
2 108 VAL n 
2 109 GLY n 
2 110 GLU n 
2 111 ASN n 
2 112 LYS n 
2 113 THR n 
2 114 LEU n 
2 115 PHE n 
2 116 ASP n 
2 117 ILE n 
2 118 THR n 
2 119 VAL n 
2 120 ASN n 
2 121 GLY n 
2 122 VAL n 
2 123 PRO n 
2 124 GLU n 
2 125 ALA n 
2 126 GLY n 
2 127 ASN n 
2 128 TYR n 
2 129 HIS n 
2 130 ALA n 
2 131 SER n 
2 132 ILE n 
2 133 HIS n 
2 134 GLU n 
2 135 LYS n 
2 136 GLY n 
2 137 ASP n 
2 138 VAL n 
2 139 SER n 
2 140 LYS n 
2 141 GLY n 
2 142 VAL n 
2 143 GLU n 
2 144 SER n 
2 145 THR n 
2 146 GLY n 
2 147 LYS n 
2 148 VAL n 
2 149 TRP n 
2 150 HIS n 
2 151 LYS n 
2 152 PHE n 
2 153 ASP n 
2 154 GLU n 
2 155 PRO n 
2 156 ILE n 
2 157 GLU n 
2 158 CYS n 
2 159 PHE n 
2 160 ASN n 
2 161 GLU n 
2 162 SER n 
2 163 ASP n 
2 164 LEU n 
2 165 GLY n 
2 166 LYS n 
2 167 ASN n 
2 168 LEU n 
2 169 TYR n 
2 170 SER n 
2 171 GLY n 
2 172 LYS n 
2 173 THR n 
2 174 PHE n 
2 175 LEU n 
2 176 SER n 
2 177 ALA n 
2 178 PRO n 
2 179 LEU n 
2 180 PRO n 
2 181 THR n 
2 182 TRP n 
2 183 GLN n 
2 184 LEU n 
2 185 ILE n 
2 186 GLY n 
2 187 ARG n 
2 188 SER n 
2 189 PHE n 
2 190 VAL n 
2 191 ILE n 
2 192 SER n 
2 193 LYS n 
2 194 SER n 
2 195 LEU n 
2 196 ASN n 
2 197 HIS n 
2 198 PRO n 
2 199 GLU n 
2 200 ASN n 
2 201 GLU n 
2 202 PRO n 
2 203 SER n 
2 204 SER n 
2 205 VAL n 
2 206 LYS n 
2 207 ASP n 
2 208 TYR n 
2 209 SER n 
2 210 PHE n 
2 211 LEU n 
2 212 GLY n 
2 213 VAL n 
2 214 ILE n 
2 215 ALA n 
2 216 ARG n 
2 217 SER n 
2 218 ALA n 
2 219 GLY n 
2 220 VAL n 
2 221 TRP n 
2 222 GLU n 
2 223 ASN n 
2 224 ASN n 
2 225 LYS n 
2 226 GLN n 
2 227 VAL n 
2 228 CYS n 
2 229 ALA n 
2 230 CYS n 
2 231 THR n 
2 232 GLY n 
2 233 LYS n 
2 234 THR n 
2 235 VAL n 
2 236 TRP n 
2 237 ALA n 
2 238 ALA n 
2 239 ALA n 
2 240 LYS n 
2 241 ASP n 
2 242 ALA n 
2 243 LEU n 
2 244 ALA n 
2 245 ASN n 
2 246 ASN n 
2 247 ILE n 
2 248 LYS 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' 1 153 Human           ? SOD1                              ? ?                     ? ? ? ? 
'Homo sapiens'                                          9606   ? ? ? ? ? ? ? ? 'Saccharomyces cerevisiae'   4932   ? ? ? ? ? ? 
EG118 ? ? ? ? ? ? ? Plasmid ? ? ? YEP351 ? ? 
2 1 sample 'Biological sequence' 1 248 
;Baker's yeast
;
? 'CCS1, LYS7, YMR038C, YM9532.03C' ? 'ATCC 204508 / S288c' ? ? ? ? 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c)' 559292 
? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ?     ? ? ? ? ? ? ? Plasmid ? ? ? PKA6H  ? ? 
# 
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 SODC_HUMAN P00441 ? 1 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
2 
2 UNP CCS1_YEAST P40202 ? 2 
;TTNDTYEATYAIPMHCENCVNDIKACLKNVPGINSLNFDIEQQIMSVESSVAPSTIINTLRNCGKDAIIRGAGKPNSSAV
AILETFQKYTIDQKKDTAVRGLARIVQVGENKTLFDITVNGVPEAGNYHASIHEKGDVSKGVESTGKVWHKFDEPIECFN
ESDLGKNLYSGKTFLSAPLPTWQLIGRSFVISKSLNHPENEPSSVKDYSFLGVIARSAGVWENNKQVCACTGKTVWEERK
DALANNIK
;
2 
# 
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 5U9M A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 2 5U9M B 1 ? 248 ? P40202 2 ? 249 ? 2 249 
3 1 5U9M C 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4 2 5U9M D 1 ? 248 ? P40202 2 ? 249 ? 2 249 
# 
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 5U9M ARG A 46  ? UNP P00441 HIS 47  'engineered mutation' 46  1  
1 5U9M GLN A 48  ? UNP P00441 HIS 49  'engineered mutation' 48  2  
2 5U9M ALA B 237 ? UNP P40202 GLU 238 'engineered mutation' 238 3  
2 5U9M ALA B 238 ? UNP P40202 GLU 239 'engineered mutation' 239 4  
2 5U9M ALA B 239 ? UNP P40202 ARG 240 'engineered mutation' 240 5  
3 5U9M ARG C 46  ? UNP P00441 HIS 47  'engineered mutation' 46  6  
3 5U9M GLN C 48  ? UNP P00441 HIS 49  'engineered mutation' 48  7  
4 5U9M ALA D 237 ? UNP P40202 GLU 238 'engineered mutation' 238 8  
4 5U9M ALA D 238 ? UNP P40202 GLU 239 'engineered mutation' 239 9  
4 5U9M ALA D 239 ? UNP P40202 ARG 240 'engineered mutation' 240 10 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_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                   5U9M 
_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            2.58 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         52.41 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25 % PEG 3350, 0.2 M ammonium sulfate, 0.1 M bis-tris pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2009-02-21 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate            45.51 
_reflns.entry_id                         5U9M 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.35 
_reflns.d_resolution_low                 48.51 
_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                       38015 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.9 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  7.0 
_reflns.pdbx_Rmerge_I_obs                0.112 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            13.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.35 
_reflns_shell.d_res_low                   2.48 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2.0 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        100 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                1.125 
_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             7.3 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5U9M 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.350 
_refine.ls_d_res_low                             46.917 
_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                     37948 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_percent_reflns_R_free                 5.27 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1887 
_refine.ls_R_factor_R_free                       0.2349 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1861 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          1.39 
_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                      1OZU,1JK9 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 23.18 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.32 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5734 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         3 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               5857 
_refine_hist.d_res_high                       2.350 
_refine_hist.d_res_low                        46.917 
# 
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' ? 0.009  ? 5832 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.142  ? 7886 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.126 ? 2116 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 890  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 1037 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.3500 2.4088  . . 140 2509 100.00 . . . 0.3276 . 0.2665 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4088 2.4739  . . 140 2531 100.00 . . . 0.2971 . 0.2644 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4739 2.5467  . . 143 2549 100.00 . . . 0.3174 . 0.2489 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.5467 2.6289  . . 139 2512 100.00 . . . 0.2813 . 0.2396 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.6289 2.7229  . . 142 2543 100.00 . . . 0.2772 . 0.2342 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7229 2.8319  . . 141 2546 100.00 . . . 0.3005 . 0.2145 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8319 2.9607  . . 140 2513 100.00 . . . 0.2758 . 0.2343 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.9607 3.1168  . . 141 2556 100.00 . . . 0.2889 . 0.2274 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.1168 3.3120  . . 144 2563 100.00 . . . 0.2542 . 0.2027 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.3120 3.5677  . . 141 2554 100.00 . . . 0.2544 . 0.1931 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.5677 3.9265  . . 145 2583 100.00 . . . 0.2228 . 0.1713 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.9265 4.4943  . . 143 2595 100.00 . . . 0.2098 . 0.1452 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.4943 5.6608  . . 146 2625 100.00 . . . 0.1797 . 0.1464 . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.6608 46.9260 . . 155 2769 99.00  . . . 0.1940 . 0.1646 . . . . . . . . . . 
# 
_struct.entry_id                     5U9M 
_struct.title                        
'Copper-Zinc Superoxide Dismutase is Activated through a Sulfenic Acid Intermediate at a Copper-ion Entry Site' 
_struct.pdbx_descriptor              'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1), Superoxide dismutase 1 copper chaperone' 
_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        5U9M 
_struct_keywords.text            'oxidoreductase-chaperone complex, Cu-Zn superoxide dismutase, metallochaperone' 
_struct_keywords.pdbx_keywords   oxidoreductase/chaperone 
# 
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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
# 
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 GLY A 56  ? GLY A 61  ? GLY A 56  GLY A 61  1 ? 6  
HELX_P HELX_P2  AA2 SER A 107 ? CYS A 111 ? SER A 107 CYS A 111 5 ? 5  
HELX_P HELX_P3  AA3 GLU A 133 ? GLY A 138 ? GLU A 133 GLY A 138 1 ? 6  
HELX_P HELX_P4  AA4 GLU B 17  ? LYS B 28  ? GLU B 18  LYS B 29  1 ? 12 
HELX_P HELX_P5  AA5 ALA B 52  ? LEU B 60  ? ALA B 53  LEU B 61  1 ? 9  
HELX_P HELX_P6  AA6 LYS B 140 ? GLY B 146 ? LYS B 141 GLY B 147 5 ? 7  
HELX_P HELX_P7  AA7 PRO B 180 ? LEU B 184 ? PRO B 181 LEU B 185 5 ? 5  
HELX_P HELX_P8  AA8 GLY C 56  ? GLY C 61  ? GLY C 56  GLY C 61  1 ? 6  
HELX_P HELX_P9  AA9 SER C 107 ? CYS C 111 ? SER C 107 CYS C 111 5 ? 5  
HELX_P HELX_P10 AB1 ASN C 131 ? GLY C 138 ? ASN C 131 GLY C 138 1 ? 8  
HELX_P HELX_P11 AB2 GLU D 17  ? LYS D 28  ? GLU D 18  LYS D 29  1 ? 12 
HELX_P HELX_P12 AB3 ALA D 52  ? ASN D 62  ? ALA D 53  ASN D 63  1 ? 11 
HELX_P HELX_P13 AB4 LYS D 140 ? GLY D 146 ? LYS D 141 GLY D 147 5 ? 7  
HELX_P HELX_P14 AB5 PRO D 180 ? LEU D 184 ? PRO D 181 LEU D 185 5 ? 5  
HELX_P HELX_P15 AB6 HIS D 197 ? GLU D 201 ? HIS D 198 GLU D 202 5 ? 5  
# 
_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 
disulf1  disulf ? ? D CYS 26 SG  ? ? ? 1_555 D CYS 63 SG ? ? D CYS 27 D CYS 64  1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc1  metalc ? ? A HIS 63 ND1 ? ? ? 1_555 E ZN  .  ZN ? ? A HIS 63 A ZN  201 1_555 ? ? ? ? ? ? ? 1.955 ? 
metalc2  metalc ? ? A HIS 71 ND1 ? ? ? 1_555 E ZN  .  ZN ? ? A HIS 71 A ZN  201 1_555 ? ? ? ? ? ? ? 2.132 ? 
metalc3  metalc ? ? A HIS 80 ND1 ? ? ? 1_555 E ZN  .  ZN ? ? A HIS 80 A ZN  201 1_555 ? ? ? ? ? ? ? 1.992 ? 
metalc4  metalc ? ? A ASP 83 OD1 ? ? ? 1_555 E ZN  .  ZN ? ? A ASP 83 A ZN  201 1_555 ? ? ? ? ? ? ? 2.074 ? 
metalc5  metalc ? ? A ASP 83 OD2 ? ? ? 1_555 E ZN  .  ZN ? ? A ASP 83 A ZN  201 1_555 ? ? ? ? ? ? ? 2.688 ? 
metalc6  metalc ? ? B CYS 16 SG  ? ? ? 1_555 F ZN  .  ZN ? ? B CYS 17 B ZN  301 1_555 ? ? ? ? ? ? ? 2.276 ? 
metalc7  metalc ? ? B CYS 19 SG  ? ? ? 1_555 F ZN  .  ZN ? ? B CYS 20 B ZN  301 1_555 ? ? ? ? ? ? ? 2.357 ? 
metalc8  metalc ? ? C HIS 63 ND1 ? ? ? 1_555 G ZN  .  ZN ? ? C HIS 63 C ZN  201 1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc9  metalc ? ? C HIS 71 ND1 ? ? ? 1_555 G ZN  .  ZN ? ? C HIS 71 C ZN  201 1_555 ? ? ? ? ? ? ? 2.060 ? 
metalc10 metalc ? ? C HIS 80 ND1 ? ? ? 1_555 G ZN  .  ZN ? ? C HIS 80 C ZN  201 1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc11 metalc ? ? C ASP 83 OD1 ? ? ? 1_555 G ZN  .  ZN ? ? C ASP 83 C ZN  201 1_555 ? ? ? ? ? ? ? 1.898 ? 
metalc12 metalc ? ? D CYS 16 SG  ? ? ? 1_555 F ZN  .  ZN ? ? D CYS 17 B ZN  301 1_656 ? ? ? ? ? ? ? 2.652 ? 
metalc13 metalc ? ? D CYS 19 SG  ? ? ? 1_555 F ZN  .  ZN ? ? D CYS 20 B ZN  301 1_656 ? ? ? ? ? ? ? 2.917 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 9 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
AA7 ? 9 ? 
AA8 ? 4 ? 
AA9 ? 9 ? 
AB1 ? 6 ? 
AB2 ? 2 ? 
# 
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 
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 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
AA4 8 9 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA7 7 8 ? anti-parallel 
AA7 8 9 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AA9 7 8 ? anti-parallel 
AA9 8 9 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB2 1 2 ? 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 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA1 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA1 3 GLN A 15  ? GLU A 21  ? GLN A 15  GLU A 21  
AA1 4 LYS A 3   ? LYS A 9   ? LYS A 3   LYS A 9   
AA1 5 GLY A 150 ? GLN A 153 ? GLY A 150 GLN A 153 
AA2 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AA2 2 GLY A 41  ? VAL A 47  ? GLY A 41  VAL A 47  
AA2 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AA2 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
AA3 1 ILE B 33  ? ASP B 39  ? ILE B 34  ASP B 40  
AA3 2 ILE B 44  ? SER B 49  ? ILE B 45  SER B 50  
AA3 3 ALA B 8   ? ALA B 11  ? ALA B 9   ALA B 12  
AA3 4 ILE B 68  ? ARG B 70  ? ILE B 69  ARG B 71  
AA4 1 VAL B 148 ? CYS B 158 ? VAL B 149 CYS B 159 
AA4 2 GLY B 126 ? HIS B 133 ? GLY B 127 HIS B 134 
AA4 3 SER B 188 ? SER B 194 ? SER B 189 SER B 195 
AA4 4 ASP B 207 ? VAL B 213 ? ASP B 208 VAL B 214 
AA4 5 SER B 78  ? THR B 85  ? SER B 79  THR B 86  
AA4 6 VAL B 99  ? GLN B 107 ? VAL B 100 GLN B 108 
AA4 7 THR B 113 ? VAL B 122 ? THR B 114 VAL B 123 
AA4 8 TYR B 169 ? ALA B 177 ? TYR B 170 ALA B 178 
AA4 9 ASN B 160 ? GLU B 161 ? ASN B 161 GLU B 162 
AA5 1 VAL B 148 ? CYS B 158 ? VAL B 149 CYS B 159 
AA5 2 GLY B 126 ? HIS B 133 ? GLY B 127 HIS B 134 
AA5 3 SER B 188 ? SER B 194 ? SER B 189 SER B 195 
AA5 4 ASP B 207 ? VAL B 213 ? ASP B 208 VAL B 214 
AA5 5 SER B 78  ? THR B 85  ? SER B 79  THR B 86  
AA5 6 ALA B 215 ? ARG B 216 ? ALA B 216 ARG B 217 
AA6 1 GLN B 226 ? CYS B 228 ? GLN B 227 CYS B 229 
AA6 2 THR B 234 ? ALA B 237 ? THR B 235 ALA B 238 
AA7 1 LYS C 3   ? LYS C 9   ? LYS C 3   LYS C 9   
AA7 2 GLN C 15  ? GLU C 21  ? GLN C 15  GLU C 21  
AA7 3 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
AA7 4 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
AA7 5 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
AA7 6 GLY C 41  ? VAL C 47  ? GLY C 41  VAL C 47  
AA7 7 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
AA7 8 ARG C 143 ? GLN C 153 ? ARG C 143 GLN C 153 
AA7 9 LYS C 3   ? LYS C 9   ? LYS C 3   LYS C 9   
AA8 1 ILE D 33  ? ASP D 39  ? ILE D 34  ASP D 40  
AA8 2 ILE D 44  ? SER D 49  ? ILE D 45  SER D 50  
AA8 3 TYR D 6   ? ALA D 11  ? TYR D 7   ALA D 12  
AA8 4 ILE D 68  ? ARG D 70  ? ILE D 69  ARG D 71  
AA9 1 VAL D 148 ? CYS D 158 ? VAL D 149 CYS D 159 
AA9 2 GLY D 126 ? HIS D 133 ? GLY D 127 HIS D 134 
AA9 3 SER D 188 ? SER D 194 ? SER D 189 SER D 195 
AA9 4 ASP D 207 ? VAL D 213 ? ASP D 208 VAL D 214 
AA9 5 SER D 78  ? THR D 85  ? SER D 79  THR D 86  
AA9 6 VAL D 99  ? GLN D 107 ? VAL D 100 GLN D 108 
AA9 7 THR D 113 ? VAL D 122 ? THR D 114 VAL D 123 
AA9 8 GLY D 165 ? ALA D 177 ? GLY D 166 ALA D 178 
AA9 9 ASN D 160 ? SER D 162 ? ASN D 161 SER D 163 
AB1 1 VAL D 148 ? CYS D 158 ? VAL D 149 CYS D 159 
AB1 2 GLY D 126 ? HIS D 133 ? GLY D 127 HIS D 134 
AB1 3 SER D 188 ? SER D 194 ? SER D 189 SER D 195 
AB1 4 ASP D 207 ? VAL D 213 ? ASP D 208 VAL D 214 
AB1 5 SER D 78  ? THR D 85  ? SER D 79  THR D 86  
AB1 6 ALA D 215 ? SER D 217 ? ALA D 216 SER D 218 
AB2 1 GLN D 226 ? CYS D 228 ? GLN D 227 CYS D 229 
AB2 2 THR D 234 ? ALA D 237 ? THR D 235 ALA D 238 
# 
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 ALA A 95  ? O ALA A 95  N ILE A 35  ? N ILE A 35  
AA1 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
AA1 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
AA1 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AA2 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
AA2 2 3 N GLY A 44  ? N GLY A 44  O HIS A 120 ? O HIS A 120 
AA2 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
AA3 1 2 N ASN B 37  ? N ASN B 38  O SER B 46  ? O SER B 47  
AA3 2 3 O MET B 45  ? O MET B 46  N TYR B 10  ? N TYR B 11  
AA3 3 4 N THR B 9   ? N THR B 10  O ARG B 70  ? O ARG B 71  
AA4 1 2 O ILE B 156 ? O ILE B 157 N TYR B 128 ? N TYR B 129 
AA4 2 3 N HIS B 129 ? N HIS B 130 O SER B 192 ? O SER B 193 
AA4 3 4 N LYS B 193 ? N LYS B 194 O TYR B 208 ? O TYR B 209 
AA4 4 5 O LEU B 211 ? O LEU B 212 N GLU B 84  ? N GLU B 85  
AA4 5 6 N ALA B 79  ? N ALA B 80  O ILE B 105 ? O ILE B 106 
AA4 6 7 N ARG B 104 ? N ARG B 105 O ASP B 116 ? O ASP B 117 
AA4 7 8 N VAL B 119 ? N VAL B 120 O GLY B 171 ? O GLY B 172 
AA4 8 9 O SER B 170 ? O SER B 171 N ASN B 160 ? N ASN B 161 
AA5 1 2 O ILE B 156 ? O ILE B 157 N TYR B 128 ? N TYR B 129 
AA5 2 3 N HIS B 129 ? N HIS B 130 O SER B 192 ? O SER B 193 
AA5 3 4 N LYS B 193 ? N LYS B 194 O TYR B 208 ? O TYR B 209 
AA5 4 5 O LEU B 211 ? O LEU B 212 N GLU B 84  ? N GLU B 85  
AA5 5 6 N VAL B 80  ? N VAL B 81  O ALA B 215 ? O ALA B 216 
AA6 1 2 N VAL B 227 ? N VAL B 228 O TRP B 236 ? O TRP B 237 
AA7 1 2 N CYS C 6   ? N CYS C 6   O ILE C 18  ? O ILE C 18  
AA7 2 3 N GLU C 21  ? N GLU C 21  O LYS C 30  ? O LYS C 30  
AA7 3 4 N ILE C 35  ? N ILE C 35  O ALA C 95  ? O ALA C 95  
AA7 4 5 O ASP C 96  ? O ASP C 96  N THR C 88  ? N THR C 88  
AA7 5 6 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
AA7 6 7 N ARG C 46  ? N ARG C 46  O VAL C 118 ? O VAL C 118 
AA7 7 8 N LEU C 117 ? N LEU C 117 O GLY C 147 ? O GLY C 147 
AA7 8 9 O GLY C 150 ? O GLY C 150 N VAL C 5   ? N VAL C 5   
AA8 1 2 N ASN D 34  ? N ASN D 35  O GLU D 48  ? O GLU D 49  
AA8 2 3 O VAL D 47  ? O VAL D 48  N ALA D 8   ? N ALA D 9   
AA8 3 4 N ALA D 11  ? N ALA D 12  O ILE D 68  ? O ILE D 69  
AA9 1 2 O TRP D 149 ? O TRP D 150 N ILE D 132 ? N ILE D 133 
AA9 2 3 N SER D 131 ? N SER D 132 O VAL D 190 ? O VAL D 191 
AA9 3 4 N LYS D 193 ? N LYS D 194 O TYR D 208 ? O TYR D 209 
AA9 4 5 O LEU D 211 ? O LEU D 212 N GLU D 84  ? N GLU D 85  
AA9 5 6 N ALA D 79  ? N ALA D 80  O ILE D 105 ? O ILE D 106 
AA9 6 7 N ARG D 104 ? N ARG D 105 O ASP D 116 ? O ASP D 117 
AA9 7 8 N VAL D 119 ? N VAL D 120 O GLY D 171 ? O GLY D 172 
AA9 8 9 O SER D 170 ? O SER D 171 N ASN D 160 ? N ASN D 161 
AB1 1 2 O TRP D 149 ? O TRP D 150 N ILE D 132 ? N ILE D 133 
AB1 2 3 N SER D 131 ? N SER D 132 O VAL D 190 ? O VAL D 191 
AB1 3 4 N LYS D 193 ? N LYS D 194 O TYR D 208 ? O TYR D 209 
AB1 4 5 O LEU D 211 ? O LEU D 212 N GLU D 84  ? N GLU D 85  
AB1 5 6 N VAL D 80  ? N VAL D 81  O ALA D 215 ? O ALA D 216 
AB2 1 2 N VAL D 227 ? N VAL D 228 O TRP D 236 ? O TRP D 237 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN 201 ? 4 'binding site for residue ZN A 201' 
AC2 Software B ZN 301 ? 4 'binding site for residue ZN B 301' 
AC3 Software C ZN 201 ? 4 'binding site for residue ZN C 201' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 63 ? HIS A 63 . ? 1_555 ? 
2  AC1 4 HIS A 71 ? HIS A 71 . ? 1_555 ? 
3  AC1 4 HIS A 80 ? HIS A 80 . ? 1_555 ? 
4  AC1 4 ASP A 83 ? ASP A 83 . ? 1_555 ? 
5  AC2 4 CYS B 16 ? CYS B 17 . ? 1_555 ? 
6  AC2 4 CYS B 19 ? CYS B 20 . ? 1_555 ? 
7  AC2 4 CYS D 16 ? CYS D 17 . ? 1_454 ? 
8  AC2 4 CYS D 19 ? CYS D 20 . ? 1_454 ? 
9  AC3 4 HIS C 63 ? HIS C 63 . ? 1_555 ? 
10 AC3 4 HIS C 71 ? HIS C 71 . ? 1_555 ? 
11 AC3 4 HIS C 80 ? HIS C 80 . ? 1_555 ? 
12 AC3 4 ASP C 83 ? ASP C 83 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5U9M 
_atom_sites.fract_transf_matrix[1][1]   0.010091 
_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]   0.005424 
_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]   0.020613 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 98.315  211.548 23.524  1.00 57.89  ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 98.931  211.951 22.259  1.00 58.14  ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 99.706  213.262 22.440  1.00 58.05  ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 99.123  214.329 22.659  1.00 54.17  ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 97.865  212.097 21.173  1.00 50.47  ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 101.023 213.186 22.303  1.00 54.10  ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 101.874 214.287 22.727  1.00 43.43  ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 102.746 214.870 21.606  1.00 42.72  ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 103.160 216.028 21.664  1.00 37.80  ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 102.753 213.834 23.927  1.00 48.27  ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 103.341 214.980 24.549  1.00 70.34  ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 103.863 212.904 23.495  1.00 46.70  ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 102.997 214.093 20.569  1.00 39.68  ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 103.758 214.610 19.436  1.00 41.32  ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 103.088 214.204 18.124  1.00 36.18  ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 102.553 213.103 18.005  1.00 38.83  ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 105.201 214.107 19.474  1.00 53.84  ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 106.165 214.923 20.322  1.00 59.22  ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 107.586 214.750 19.796  1.00 68.31  ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 108.611 214.855 20.912  1.00 85.05  ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 109.996 214.567 20.432  1.00 87.51  1 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 103.085 215.099 17.149  1.00 38.01  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 102.556 214.750 15.822  1.00 34.22  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 103.507 215.290 14.767  1.00 31.91  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 104.305 216.166 15.061  1.00 33.69  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 101.145 215.290 15.638  1.00 22.99  ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 103.420 214.779 13.546  1.00 26.76  ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 104.300 215.205 12.470  1.00 28.15  ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 103.564 215.212 11.141  1.00 31.92  ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 102.604 214.456 10.928  1.00 34.69  ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 105.531 214.275 12.338  1.00 39.34  ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 105.089 212.892 11.840  1.00 32.22  ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 106.575 214.874 11.392  1.00 30.89  ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 103.996 216.078 10.239  1.00 32.24  ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 103.402 216.120 8.925   1.00 29.02  ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 104.448 216.292 7.832   1.00 30.53  ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 105.280 217.197 7.908   1.00 27.19  ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 102.373 217.261 8.839   1.00 33.24  ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 101.544 217.396 7.204   1.00 36.28  ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 104.385 215.436 6.815   1.00 30.73  ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 105.208 215.612 5.619   1.00 35.31  ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 104.432 216.354 4.505   1.00 32.97  ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 103.568 215.783 3.841   1.00 29.32  ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 105.698 214.269 5.083   1.00 33.62  ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 106.518 214.451 3.745   1.00 25.97  ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 106.505 213.574 6.159   1.00 30.88  ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 104.768 217.621 4.305   1.00 30.51  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 104.150 218.434 3.268   1.00 31.41  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 104.834 218.172 1.948   1.00 37.84  ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 106.049 218.365 1.812   1.00 35.83  ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 104.257 219.919 3.594   1.00 26.05  ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 103.689 220.383 4.931   1.00 38.80  ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 103.992 221.853 5.103   1.00 40.95  ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 102.192 220.147 5.000   1.00 38.57  ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 104.057 217.742 0.971   1.00 30.68  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 104.577 217.695 -0.371  1.00 39.15  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 103.482 218.021 -1.370  1.00 41.74  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 102.286 218.006 -1.036  1.00 36.46  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 105.220 216.332 -0.645  1.00 43.49  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 104.306 215.157 -0.504  1.00 35.54  ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 105.128 213.876 -0.572  1.00 55.09  ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 104.424 212.800 -1.395  1.00 65.54  ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 103.242 212.267 -0.664  1.00 70.62  1 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 103.916 218.391 -2.571  1.00 40.41  ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 103.019 218.748 -3.649  1.00 44.28  ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 103.607 218.413 -5.009  1.00 52.84  ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 104.581 217.674 -5.115  1.00 47.87  ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 102.997 218.964 -6.052  1.00 54.08  ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 103.375 218.682 -7.440  1.00 55.76  ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? 104.570 219.481 -7.892  1.00 50.60  ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? 105.081 219.262 -8.977  1.00 61.16  ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 102.207 218.956 -8.379  1.00 50.97  ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 101.044 218.030 -8.133  1.00 68.01  ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 101.295 216.828 -7.875  1.00 76.60  ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 99.887  218.505 -8.183  1.00 74.59  1 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? 104.974 220.449 -7.078  1.00 51.68  ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 106.065 221.331 -7.430  1.00 33.58  ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 107.224 221.224 -6.465  1.00 43.11  ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 107.416 220.194 -5.813  1.00 45.76  ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 108.003 222.308 -6.362  1.00 42.02  ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 109.164 222.393 -5.486  1.00 47.91  ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 108.814 222.475 -3.987  1.00 47.04  ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 109.660 222.142 -3.163  1.00 55.25  ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? 109.844 223.684 -5.949  1.00 44.96  ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? 108.753 224.503 -6.513  1.00 33.88  ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 107.823 223.534 -7.159  1.00 42.36  ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 107.601 222.894 -3.640  1.00 48.37  ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 107.272 223.114 -2.234  1.00 41.27  ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 107.192 221.793 -1.503  1.00 39.09  ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 106.476 220.888 -1.902  1.00 40.94  ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 105.947 223.871 -2.059  1.00 44.79  ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 105.716 224.222 -0.575  1.00 29.79  ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 105.981 225.126 -2.884  1.00 39.49  ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 107.959 221.695 -0.431  1.00 34.31  ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 107.982 220.498 0.378   1.00 44.51  ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 108.518 220.872 1.745   1.00 34.31  ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 109.209 221.879 1.901   1.00 38.48  ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 108.833 219.413 -0.275  1.00 42.23  ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 110.317 219.701 -0.262  1.00 52.92  ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 111.123 218.635 -0.996  1.00 70.25  ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 111.591 217.669 -0.390  1.00 78.12  ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 111.307 218.821 -2.302  1.00 69.72  ? 15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 108.156 220.098 2.754   1.00 34.90  ? 16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 108.570 220.456 4.092   1.00 38.06  ? 16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 108.128 219.448 5.113   1.00 39.02  ? 16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 107.342 218.547 4.802   1.00 38.40  ? 16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 108.664 219.587 6.317   1.00 36.14  ? 17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 108.213 218.809 7.465   1.00 35.07  ? 17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 107.845 219.691 8.637   1.00 35.38  ? 17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 108.605 220.580 9.027   1.00 32.95  ? 17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 109.266 217.804 7.909   1.00 36.31  ? 17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 109.433 216.743 6.820   1.00 38.56  ? 17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 108.835 217.117 9.204   1.00 32.64  ? 17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 110.521 215.728 7.109   1.00 48.07  ? 17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 106.667 219.439 9.193   1.00 36.32  ? 18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 106.179 220.209 10.322  1.00 33.34  ? 18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 105.952 219.308 11.541  1.00 33.09  ? 18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 105.334 218.243 11.433  1.00 29.69  ? 18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 104.885 220.923 9.962   1.00 31.47  ? 18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 105.083 221.782 8.709   1.00 29.94  ? 18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 104.440 221.774 11.108  1.00 30.70  ? 18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 105.861 223.050 8.979   1.00 25.41  ? 18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 106.479 219.724 12.694  1.00 32.94  ? 19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 106.276 218.976 13.925  1.00 28.63  ? 19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 105.318 219.684 14.831  1.00 34.55  ? 19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 105.241 220.903 14.822  1.00 37.25  ? 19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 107.595 218.757 14.643  1.00 36.04  ? 19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 108.601 218.086 13.760  1.00 41.19  ? 19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 109.488 218.743 13.233  1.00 43.49  ? 19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 108.448 216.782 13.552  1.00 40.83  ? 19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 104.590 218.895 15.604  1.00 35.27  ? 20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 103.676 219.376 16.620  1.00 33.89  ? 20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 104.031 218.709 17.959  1.00 35.81  ? 20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 104.354 217.529 18.012  1.00 35.34  ? 20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 102.227 219.056 16.241  1.00 31.06  ? 20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 101.797 219.618 14.903  1.00 41.51  ? 20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 102.174 218.988 13.718  1.00 33.73  ? 20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 100.971 220.739 14.833  1.00 36.35  ? 20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 101.785 219.488 12.485  1.00 34.41  ? 20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 100.565 221.245 13.605  1.00 36.33  ? 20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 100.980 220.612 12.422  1.00 35.47  ? 20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 103.961 219.471 19.035  1.00 36.79  ? 21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 104.239 218.953 20.356  1.00 38.67  ? 21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 103.307 219.603 21.365  1.00 38.83  ? 21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 103.103 220.817 21.339  1.00 36.64  ? 21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 105.687 219.200 20.732  1.00 49.26  ? 21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 106.084 218.607 22.074  1.00 58.91  ? 21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 107.519 218.917 22.426  1.00 68.53  ? 21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 108.423 218.173 21.975  1.00 75.96  ? 21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 107.732 219.916 23.145  1.00 73.60  1 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 102.693 218.779 22.203  1.00 37.30  ? 22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 101.773 219.236 23.245  1.00 42.87  ? 22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 101.941 218.453 24.551  1.00 46.17  ? 22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 101.469 217.321 24.682  1.00 47.19  ? 22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 100.333 219.116 22.753  1.00 38.49  ? 22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 99.314  219.845 23.600  1.00 35.33  ? 22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 97.900  219.487 23.208  1.00 34.06  ? 22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 97.656  218.440 22.600  1.00 31.56  ? 22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 96.960  220.371 23.523  1.00 38.81  ? 22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 102.610 219.049 25.517  1.00 48.15  ? 23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 102.935 218.337 26.745  1.00 53.36  ? 23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 101.689 218.035 27.587  1.00 48.14  ? 23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 101.481 216.903 28.014  1.00 48.50  ? 23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 103.973 219.137 27.514  1.00 54.06  ? 23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 105.201 219.377 26.653  1.00 55.71  ? 23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 106.279 220.166 27.346  1.00 74.44  ? 23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 107.523 220.208 26.479  1.00 70.81  ? 23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 108.504 221.212 26.970  1.00 78.81  1 23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 100.865 219.044 27.812  1.00 50.98  ? 24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 99.610  218.879 28.541  1.00 51.99  ? 24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 98.421  218.768 27.592  1.00 47.76  ? 24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 98.400  219.411 26.552  1.00 40.83  ? 24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 99.392  220.048 29.511  1.00 51.06  ? 24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 100.457 220.228 30.578  1.00 64.17  ? 24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 100.460 219.093 31.607  1.00 92.75  ? 24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 99.486  218.299 31.647  1.00 90.91  ? 24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 101.426 219.013 32.398  1.00 92.70  1 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 97.437  217.948 27.941  1.00 47.84  ? 25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 96.284  217.762 27.073  1.00 41.50  ? 25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 95.548  219.076 26.792  1.00 46.65  ? 25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 94.899  219.209 25.753  1.00 54.19  ? 25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 95.304  216.749 27.670  1.00 51.99  ? 25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 94.892  217.128 28.966  1.00 55.31  ? 25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 95.630  220.036 27.712  1.00 40.21  ? 26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 95.042  221.353 27.479  1.00 42.79  ? 26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 96.085  222.435 27.550  1.00 36.48  ? 26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 95.776  223.575 27.897  1.00 33.85  ? 26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 93.922  221.685 28.501  1.00 39.47  ? 26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 94.387  221.591 29.976  1.00 52.00  ? 26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 95.577  221.432 30.274  1.00 42.42  ? 26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 93.438  221.737 30.895  1.00 35.56  ? 26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 97.320  222.071 27.234  1.00 36.14  ? 27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 98.391  223.041 27.112  1.00 37.44  ? 27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 98.458  223.510 25.665  1.00 36.89  ? 27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 97.744  222.989 24.813  1.00 35.89  ? 27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 99.333  224.474 25.374  1.00 33.69  ? 28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 99.441  224.947 23.987  1.00 38.03  ? 28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 100.100 223.906 23.073  1.00 40.47  ? 28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 100.752 222.966 23.543  1.00 39.09  ? 28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 100.317 226.202 24.102  1.00 33.35  ? 28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 101.125 225.991 25.361  1.00 48.11  ? 28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 100.273 225.146 26.292  1.00 37.11  ? 28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 99.908  224.055 21.770  1.00 37.23  ? 29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 100.627 223.208 20.835  1.00 39.58  ? 29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 101.759 224.010 20.227  1.00 33.10  ? 29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 101.544 225.110 19.704  1.00 35.07  ? 29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 99.728  222.646 19.718  1.00 37.48  ? 29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 100.574 221.807 18.758  1.00 28.59  ? 29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 98.592  221.808 20.309  1.00 30.61  ? 29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 102.966 223.466 20.345  1.00 36.29  ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 104.152 224.015 19.711  1.00 39.52  ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 104.215 223.435 18.301  1.00 37.30  ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 104.007 222.231 18.107  1.00 36.30  ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 105.411 223.676 20.522  1.00 42.97  ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 106.615 224.515 20.160  1.00 52.83  ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 107.889 223.987 20.835  1.00 74.94  ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 109.086 224.032 19.892  1.00 58.32  ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 110.230 223.260 20.429  1.00 70.16  1 30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 104.471 224.292 17.318  1.00 34.44  ? 31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 104.435 223.898 15.910  1.00 34.97  ? 31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 105.663 224.441 15.209  1.00 39.69  ? 31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 105.838 225.653 15.102  1.00 42.33  ? 31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 103.157 224.430 15.174  1.00 33.77  ? 31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 103.188 224.055 13.689  1.00 30.15  ? 31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 101.898 223.937 15.837  1.00 31.74  ? 31  VAL A CG2 1 
ATOM   226  N  N   . TRP A 1 32  ? 106.531 223.564 14.742  1.00 32.23  ? 32  TRP A N   1 
ATOM   227  C  CA  . TRP A 1 32  ? 107.767 224.040 14.170  1.00 35.68  ? 32  TRP A CA  1 
ATOM   228  C  C   . TRP A 1 32  ? 108.226 223.092 13.093  1.00 35.42  ? 32  TRP A C   1 
ATOM   229  O  O   . TRP A 1 32  ? 107.806 221.937 13.033  1.00 35.29  ? 32  TRP A O   1 
ATOM   230  C  CB  . TRP A 1 32  ? 108.854 224.203 15.247  1.00 31.50  ? 32  TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 32  ? 109.547 222.916 15.586  1.00 37.81  ? 32  TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 32  ? 110.741 222.461 15.088  1.00 39.75  ? 32  TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 32  ? 109.080 221.913 16.489  1.00 37.83  ? 32  TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 32  ? 111.047 221.236 15.637  1.00 47.02  ? 32  TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 32  ? 110.047 220.880 16.507  1.00 41.21  ? 32  TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 32  ? 107.941 221.785 17.288  1.00 38.08  ? 32  TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 32  ? 109.901 219.736 17.287  1.00 40.56  ? 32  TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 32  ? 107.801 220.646 18.072  1.00 48.33  ? 32  TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 32  ? 108.777 219.639 18.067  1.00 47.91  ? 32  TRP A CH2 1 
ATOM   240  N  N   . GLY A 1 33  ? 109.062 223.618 12.217  1.00 32.52  ? 33  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 33  ? 109.597 222.862 11.122  1.00 29.49  ? 33  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 33  ? 109.972 223.834 10.020  1.00 39.14  ? 33  GLY A C   1 
ATOM   243  O  O   . GLY A 1 33  ? 110.075 225.050 10.244  1.00 37.13  ? 33  GLY A O   1 
ATOM   244  N  N   . SER A 1 34  ? 110.169 223.292 8.824   1.00 36.67  ? 34  SER A N   1 
ATOM   245  C  CA  . SER A 1 34  ? 110.598 224.087 7.680   1.00 43.41  ? 34  SER A CA  1 
ATOM   246  C  C   . SER A 1 34  ? 109.863 223.718 6.401   1.00 36.51  ? 34  SER A C   1 
ATOM   247  O  O   . SER A 1 34  ? 109.534 222.550 6.177   1.00 37.75  ? 34  SER A O   1 
ATOM   248  C  CB  . SER A 1 34  ? 112.101 223.937 7.452   1.00 43.54  ? 34  SER A CB  1 
ATOM   249  O  OG  . SER A 1 34  ? 112.525 224.850 6.450   1.00 57.43  ? 34  SER A OG  1 
ATOM   250  N  N   . ILE A 1 35  ? 109.604 224.727 5.576   1.00 35.51  ? 35  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 35  ? 109.046 224.536 4.251   1.00 40.15  ? 35  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 35  ? 109.939 225.248 3.250   1.00 40.83  ? 35  ILE A C   1 
ATOM   253  O  O   . ILE A 1 35  ? 110.254 226.431 3.429   1.00 40.67  ? 35  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 35  ? 107.625 225.092 4.125   1.00 41.04  ? 35  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 35  ? 106.744 224.621 5.287   1.00 39.22  ? 35  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 35  ? 107.030 224.733 2.752   1.00 33.33  ? 35  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 35  ? 105.342 225.208 5.251   1.00 30.26  ? 35  ILE A CD1 1 
ATOM   258  N  N   . LYS A 1 36  ? 110.345 224.533 2.203   1.00 37.65  ? 36  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 36  ? 111.218 225.118 1.196   1.00 40.97  ? 36  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 36  ? 110.535 225.132 -0.158  1.00 39.52  ? 36  LYS A C   1 
ATOM   261  O  O   . LYS A 1 36  ? 109.513 224.470 -0.348  1.00 42.44  ? 36  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 36  ? 112.552 224.362 1.135   1.00 45.50  ? 36  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 36  ? 112.501 222.922 0.642   1.00 56.01  ? 36  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 36  ? 113.904 222.318 0.718   1.00 56.40  ? 36  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 36  ? 114.089 221.079 -0.145  1.00 61.05  ? 36  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 36  ? 115.549 220.814 -0.384  1.00 71.20  1 36  LYS A NZ  1 
ATOM   267  N  N   . GLY A 1 37  ? 111.076 225.910 -1.091  1.00 45.62  ? 37  GLY A N   1 
ATOM   268  C  CA  . GLY A 1 37  ? 110.544 225.944 -2.448  1.00 43.52  ? 37  GLY A CA  1 
ATOM   269  C  C   . GLY A 1 37  ? 109.396 226.920 -2.630  1.00 45.91  ? 37  GLY A C   1 
ATOM   270  O  O   . GLY A 1 37  ? 108.660 226.868 -3.620  1.00 44.82  ? 37  GLY A O   1 
ATOM   271  N  N   . LEU A 1 38  ? 109.243 227.805 -1.654  1.00 39.39  ? 38  LEU A N   1 
ATOM   272  C  CA  . LEU A 1 38  ? 108.202 228.815 -1.669  1.00 42.90  ? 38  LEU A CA  1 
ATOM   273  C  C   . LEU A 1 38  ? 108.728 230.068 -2.336  1.00 49.29  ? 38  LEU A C   1 
ATOM   274  O  O   . LEU A 1 38  ? 109.938 230.290 -2.389  1.00 51.20  ? 38  LEU A O   1 
ATOM   275  C  CB  . LEU A 1 38  ? 107.754 229.150 -0.241  1.00 45.95  ? 38  LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 38  ? 107.046 228.037 0.525   1.00 47.31  ? 38  LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 38  ? 106.965 228.357 2.000   1.00 38.93  ? 38  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 38  ? 105.658 227.844 -0.085  1.00 39.22  ? 38  LEU A CD2 1 
ATOM   279  N  N   . THR A 1 39  ? 107.825 230.891 -2.847  1.00 42.65  ? 39  THR A N   1 
ATOM   280  C  CA  . THR A 1 39  ? 108.212 232.226 -3.261  1.00 42.55  ? 39  THR A CA  1 
ATOM   281  C  C   . THR A 1 39  ? 108.333 233.080 -2.019  1.00 47.27  ? 39  THR A C   1 
ATOM   282  O  O   . THR A 1 39  ? 107.666 232.808 -1.019  1.00 42.65  ? 39  THR A O   1 
ATOM   283  C  CB  . THR A 1 39  ? 107.197 232.859 -4.212  1.00 43.62  ? 39  THR A CB  1 
ATOM   284  O  OG1 . THR A 1 39  ? 105.942 232.961 -3.534  1.00 45.50  ? 39  THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 39  ? 107.020 232.015 -5.477  1.00 27.71  ? 39  THR A CG2 1 
ATOM   286  N  N   . GLU A 1 40  ? 109.166 234.116 -2.092  1.00 50.76  ? 40  GLU A N   1 
ATOM   287  C  CA  . GLU A 1 40  ? 109.363 235.044 -0.986  1.00 49.16  ? 40  GLU A CA  1 
ATOM   288  C  C   . GLU A 1 40  ? 108.017 235.611 -0.567  1.00 54.80  ? 40  GLU A C   1 
ATOM   289  O  O   . GLU A 1 40  ? 107.177 235.885 -1.419  1.00 51.86  ? 40  GLU A O   1 
ATOM   290  C  CB  . GLU A 1 40  ? 110.300 236.177 -1.404  1.00 49.48  ? 40  GLU A CB  1 
ATOM   291  C  CG  . GLU A 1 40  ? 110.856 237.049 -0.267  1.00 60.04  ? 40  GLU A CG  1 
ATOM   292  C  CD  . GLU A 1 40  ? 111.853 238.097 -0.775  1.00 66.96  ? 40  GLU A CD  1 
ATOM   293  O  OE1 . GLU A 1 40  ? 111.841 238.385 -1.990  1.00 74.60  ? 40  GLU A OE1 1 
ATOM   294  O  OE2 . GLU A 1 40  ? 112.646 238.628 0.030   1.00 61.15  1 40  GLU A OE2 1 
ATOM   295  N  N   . GLY A 1 41  ? 107.815 235.803 0.735   1.00 45.34  ? 41  GLY A N   1 
ATOM   296  C  CA  . GLY A 1 41  ? 106.559 236.354 1.216   1.00 50.85  ? 41  GLY A CA  1 
ATOM   297  C  C   . GLY A 1 41  ? 105.708 235.459 2.100   1.00 46.22  ? 41  GLY A C   1 
ATOM   298  O  O   . GLY A 1 41  ? 106.169 234.449 2.622   1.00 45.67  ? 41  GLY A O   1 
ATOM   299  N  N   . LEU A 1 42  ? 104.448 235.852 2.242   1.00 49.92  ? 42  LEU A N   1 
ATOM   300  C  CA  . LEU A 1 42  ? 103.493 235.220 3.143   1.00 36.14  ? 42  LEU A CA  1 
ATOM   301  C  C   . LEU A 1 42  ? 102.623 234.157 2.474   1.00 39.96  ? 42  LEU A C   1 
ATOM   302  O  O   . LEU A 1 42  ? 102.098 234.350 1.367   1.00 34.61  ? 42  LEU A O   1 
ATOM   303  C  CB  . LEU A 1 42  ? 102.585 236.273 3.758   1.00 34.79  ? 42  LEU A CB  1 
ATOM   304  C  CG  . LEU A 1 42  ? 103.240 237.052 4.895   1.00 53.16  ? 42  LEU A CG  1 
ATOM   305  C  CD1 . LEU A 1 42  ? 104.206 238.102 4.328   1.00 58.90  ? 42  LEU A CD1 1 
ATOM   306  C  CD2 . LEU A 1 42  ? 102.209 237.672 5.820   1.00 45.09  ? 42  LEU A CD2 1 
ATOM   307  N  N   . HIS A 1 43  ? 102.449 233.038 3.169   1.00 37.41  ? 43  HIS A N   1 
ATOM   308  C  CA  . HIS A 1 43  ? 101.671 231.932 2.635   1.00 35.35  ? 43  HIS A CA  1 
ATOM   309  C  C   . HIS A 1 43  ? 100.645 231.394 3.637   1.00 32.20  ? 43  HIS A C   1 
ATOM   310  O  O   . HIS A 1 43  ? 100.992 231.094 4.767   1.00 36.50  ? 43  HIS A O   1 
ATOM   311  C  CB  . HIS A 1 43  ? 102.633 230.833 2.203   1.00 31.23  ? 43  HIS A CB  1 
ATOM   312  C  CG  . HIS A 1 43  ? 103.556 231.260 1.115   1.00 40.46  ? 43  HIS A CG  1 
ATOM   313  N  ND1 . HIS A 1 43  ? 103.342 230.945 -0.211  1.00 38.36  ? 43  HIS A ND1 1 
ATOM   314  C  CD2 . HIS A 1 43  ? 104.667 232.030 1.148   1.00 32.55  ? 43  HIS A CD2 1 
ATOM   315  C  CE1 . HIS A 1 43  ? 104.300 231.477 -0.944  1.00 32.13  ? 43  HIS A CE1 1 
ATOM   316  N  NE2 . HIS A 1 43  ? 105.118 232.137 -0.144  1.00 42.81  ? 43  HIS A NE2 1 
ATOM   317  N  N   . GLY A 1 44  ? 99.393  231.261 3.201   1.00 36.90  ? 44  GLY A N   1 
ATOM   318  C  CA  . GLY A 1 44  ? 98.330  230.695 4.019   1.00 31.14  ? 44  GLY A CA  1 
ATOM   319  C  C   . GLY A 1 44  ? 98.685  229.286 4.480   1.00 36.79  ? 44  GLY A C   1 
ATOM   320  O  O   . GLY A 1 44  ? 99.218  228.480 3.714   1.00 34.62  ? 44  GLY A O   1 
ATOM   321  N  N   . PHE A 1 45  ? 98.376  229.007 5.742   1.00 28.49  ? 45  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 45  ? 98.852  227.835 6.450   1.00 33.56  ? 45  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 45  ? 97.739  227.370 7.377   1.00 32.28  ? 45  PHE A C   1 
ATOM   324  O  O   . PHE A 1 45  ? 97.423  228.053 8.341   1.00 31.36  ? 45  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 45  ? 100.117 228.187 7.248   1.00 33.19  ? 45  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 45  ? 100.849 227.001 7.815   1.00 33.50  ? 45  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 45  ? 101.339 226.006 6.983   1.00 30.81  ? 45  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 45  ? 101.100 226.917 9.178   1.00 32.06  ? 45  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 45  ? 102.046 224.918 7.502   1.00 30.19  ? 45  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 45  ? 101.799 225.845 9.710   1.00 32.76  ? 45  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 45  ? 102.266 224.833 8.867   1.00 36.51  ? 45  PHE A CZ  1 
ATOM   332  N  N   . ARG A 1 46  ? 97.126  226.230 7.092   1.00 25.47  ? 46  ARG A N   1 
ATOM   333  C  CA  . ARG A 1 46  ? 95.976  225.833 7.882   1.00 28.25  ? 46  ARG A CA  1 
ATOM   334  C  C   . ARG A 1 46  ? 95.732  224.340 7.823   1.00 28.37  ? 46  ARG A C   1 
ATOM   335  O  O   . ARG A 1 46  ? 96.370  223.614 7.055   1.00 28.60  ? 46  ARG A O   1 
ATOM   336  C  CB  . ARG A 1 46  ? 94.702  226.580 7.436   1.00 31.91  ? 46  ARG A CB  1 
ATOM   337  C  CG  . ARG A 1 46  ? 94.144  226.187 6.066   1.00 31.01  ? 46  ARG A CG  1 
ATOM   338  C  CD  . ARG A 1 46  ? 94.838  226.948 4.951   1.00 27.17  ? 46  ARG A CD  1 
ATOM   339  N  NE  . ARG A 1 46  ? 94.701  228.393 5.117   1.00 31.81  ? 46  ARG A NE  1 
ATOM   340  C  CZ  . ARG A 1 46  ? 94.015  229.180 4.291   1.00 32.06  ? 46  ARG A CZ  1 
ATOM   341  N  NH1 . ARG A 1 46  ? 93.417  228.662 3.230   1.00 28.24  1 46  ARG A NH1 1 
ATOM   342  N  NH2 . ARG A 1 46  ? 93.928  230.480 4.525   1.00 30.31  ? 46  ARG A NH2 1 
ATOM   343  N  N   . VAL A 1 47  ? 94.823  223.896 8.681   1.00 24.47  ? 47  VAL A N   1 
ATOM   344  C  CA  . VAL A 1 47  ? 94.437  222.505 8.774   1.00 28.31  ? 47  VAL A CA  1 
ATOM   345  C  C   . VAL A 1 47  ? 93.012  222.340 8.264   1.00 28.53  ? 47  VAL A C   1 
ATOM   346  O  O   . VAL A 1 47  ? 92.123  223.086 8.646   1.00 27.20  ? 47  VAL A O   1 
ATOM   347  C  CB  . VAL A 1 47  ? 94.509  222.001 10.226  1.00 25.73  ? 47  VAL A CB  1 
ATOM   348  C  CG1 . VAL A 1 47  ? 94.185  220.531 10.301  1.00 26.45  ? 47  VAL A CG1 1 
ATOM   349  C  CG2 . VAL A 1 47  ? 95.863  222.270 10.799  1.00 22.92  ? 47  VAL A CG2 1 
ATOM   350  N  N   . GLN A 1 48  ? 92.802  221.341 7.421   1.00 25.76  ? 48  GLN A N   1 
ATOM   351  C  CA  . GLN A 1 48  ? 91.482  221.054 6.890   1.00 28.37  ? 48  GLN A CA  1 
ATOM   352  C  C   . GLN A 1 48  ? 90.721  220.104 7.803   1.00 33.28  ? 48  GLN A C   1 
ATOM   353  O  O   . GLN A 1 48  ? 91.299  219.516 8.713   1.00 33.68  ? 48  GLN A O   1 
ATOM   354  C  CB  . GLN A 1 48  ? 91.598  220.455 5.492   1.00 29.61  ? 48  GLN A CB  1 
ATOM   355  C  CG  . GLN A 1 48  ? 92.548  221.209 4.588   1.00 35.89  ? 48  GLN A CG  1 
ATOM   356  C  CD  . GLN A 1 48  ? 91.936  222.520 4.155   1.00 34.25  ? 48  GLN A CD  1 
ATOM   357  O  OE1 . GLN A 1 48  ? 90.730  222.605 3.998   1.00 38.57  ? 48  GLN A OE1 1 
ATOM   358  N  NE2 . GLN A 1 48  ? 92.751  223.530 3.945   1.00 34.79  ? 48  GLN A NE2 1 
ATOM   359  N  N   . GLU A 1 49  ? 89.421  219.981 7.555   1.00 28.20  ? 49  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 49  ? 88.544  219.120 8.330   1.00 33.48  ? 49  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 49  ? 88.946  217.655 8.241   1.00 37.65  ? 49  GLU A C   1 
ATOM   362  O  O   . GLU A 1 49  ? 88.949  216.928 9.257   1.00 29.53  ? 49  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 49  ? 87.102  219.291 7.873   1.00 28.87  ? 49  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 49  ? 86.098  218.492 8.684   1.00 37.44  ? 49  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 49  ? 84.654  218.776 8.300   1.00 40.94  ? 49  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 49  ? 84.430  219.556 7.351   1.00 52.79  ? 49  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 49  ? 83.736  218.248 8.969   1.00 48.02  1 49  GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 50  ? 89.292  217.221 7.033   1.00 29.38  ? 50  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? 89.676  215.831 6.842   1.00 31.74  ? 50  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? 91.112  215.736 6.433   1.00 29.81  ? 50  PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? 91.756  216.744 6.183   1.00 33.18  ? 50  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? 88.778  215.142 5.807   1.00 31.56  ? 50  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? 87.324  215.234 6.144   1.00 39.92  ? 50  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? 86.796  214.463 7.171   1.00 28.67  ? 50  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? 86.483  216.099 5.441   1.00 36.12  ? 50  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? 85.472  214.558 7.501   1.00 31.60  ? 50  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? 85.161  216.199 5.757   1.00 27.92  ? 50  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? 84.645  215.424 6.783   1.00 40.26  ? 50  PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 51  ? 91.619  214.512 6.382   1.00 29.47  ? 51  GLY A N   1 
ATOM   380  C  CA  . GLY A 1 51  ? 92.947  214.284 5.836   1.00 35.05  ? 51  GLY A CA  1 
ATOM   381  C  C   . GLY A 1 51  ? 92.908  213.517 4.518   1.00 36.06  ? 51  GLY A C   1 
ATOM   382  O  O   . GLY A 1 51  ? 93.948  213.118 3.998   1.00 35.65  ? 51  GLY A O   1 
ATOM   383  N  N   . ASP A 1 52  ? 91.698  213.296 3.995   1.00 36.45  ? 52  ASP A N   1 
ATOM   384  C  CA  . ASP A 1 52  ? 91.477  212.547 2.758   1.00 34.74  ? 52  ASP A CA  1 
ATOM   385  C  C   . ASP A 1 52  ? 91.990  213.341 1.550   1.00 34.26  ? 52  ASP A C   1 
ATOM   386  O  O   . ASP A 1 52  ? 91.424  214.376 1.200   1.00 37.91  ? 52  ASP A O   1 
ATOM   387  C  CB  . ASP A 1 52  ? 89.978  212.241 2.607   1.00 34.20  ? 52  ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 52  ? 89.666  211.283 1.457   1.00 46.34  ? 52  ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 52  ? 90.486  211.143 0.507   1.00 33.73  ? 52  ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 52  ? 88.574  210.661 1.528   1.00 43.15  1 52  ASP A OD2 1 
ATOM   391  N  N   . ASN A 1 53  ? 93.074  212.890 0.930   1.00 34.89  ? 53  ASN A N   1 
ATOM   392  C  CA  . ASN A 1 53  ? 93.633  213.654 -0.189  1.00 39.16  ? 53  ASN A CA  1 
ATOM   393  C  C   . ASN A 1 53  ? 93.448  212.928 -1.530  1.00 39.95  ? 53  ASN A C   1 
ATOM   394  O  O   . ASN A 1 53  ? 94.203  213.152 -2.478  1.00 36.19  ? 53  ASN A O   1 
ATOM   395  C  CB  . ASN A 1 53  ? 95.117  213.975 0.024   1.00 28.15  ? 53  ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 53  ? 95.372  214.836 1.268   1.00 43.42  ? 53  ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 53  ? 94.544  215.669 1.651   1.00 46.33  ? 53  ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 53  ? 96.552  214.655 1.886   1.00 45.89  ? 53  ASN A ND2 1 
ATOM   399  N  N   . THR A 1 54  ? 92.445  212.060 -1.601  1.00 37.71  ? 54  THR A N   1 
ATOM   400  C  CA  . THR A 1 54  ? 92.165  211.322 -2.822  1.00 43.67  ? 54  THR A CA  1 
ATOM   401  C  C   . THR A 1 54  ? 91.619  212.239 -3.941  1.00 49.58  ? 54  THR A C   1 
ATOM   402  O  O   . THR A 1 54  ? 91.903  212.029 -5.113  1.00 47.52  ? 54  THR A O   1 
ATOM   403  C  CB  . THR A 1 54  ? 91.192  210.169 -2.551  1.00 39.16  ? 54  THR A CB  1 
ATOM   404  O  OG1 . THR A 1 54  ? 90.014  210.664 -1.900  1.00 46.39  ? 54  THR A OG1 1 
ATOM   405  C  CG2 . THR A 1 54  ? 91.855  209.133 -1.656  1.00 33.53  ? 54  THR A CG2 1 
ATOM   406  N  N   . ALA A 1 55  ? 90.841  213.247 -3.560  1.00 43.85  ? 55  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 55  ? 90.208  214.172 -4.492  1.00 39.21  ? 55  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 55  ? 90.548  215.650 -4.240  1.00 45.92  ? 55  ALA A C   1 
ATOM   409  O  O   . ALA A 1 55  ? 89.696  216.518 -4.414  1.00 55.89  ? 55  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 55  ? 88.683  213.977 -4.446  1.00 33.46  ? 55  ALA A CB  1 
ATOM   411  N  N   . GLY A 1 56  ? 91.753  215.941 -3.768  1.00 54.01  ? 56  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 56  ? 92.155  217.322 -3.534  1.00 45.48  ? 56  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 56  ? 91.290  218.070 -2.535  1.00 56.19  ? 56  GLY A C   1 
ATOM   414  O  O   . GLY A 1 56  ? 90.878  217.512 -1.512  1.00 58.23  ? 56  GLY A O   1 
ATOM   415  N  N   . CYS A 1 57  ? 91.004  219.333 -2.848  1.00 51.11  ? 57  CYS A N   1 
ATOM   416  C  CA  . CYS A 1 57  ? 90.260  220.236 -1.965  1.00 49.36  ? 57  CYS A CA  1 
ATOM   417  C  C   . CYS A 1 57  ? 88.941  219.648 -1.556  1.00 49.57  ? 57  CYS A C   1 
ATOM   418  O  O   . CYS A 1 57  ? 88.459  219.870 -0.445  1.00 60.24  ? 57  CYS A O   1 
ATOM   419  C  CB  . CYS A 1 57  ? 90.005  221.586 -2.630  1.00 52.72  ? 57  CYS A CB  1 
ATOM   420  S  SG  . CYS A 1 57  ? 91.467  222.325 -3.370  1.00 87.60  ? 57  CYS A SG  1 
ATOM   421  N  N   . THR A 1 58  ? 88.370  218.882 -2.470  1.00 41.34  ? 58  THR A N   1 
ATOM   422  C  CA  . THR A 1 58  ? 87.033  218.351 -2.309  1.00 46.62  ? 58  THR A CA  1 
ATOM   423  C  C   . THR A 1 58  ? 86.920  217.368 -1.148  1.00 50.23  ? 58  THR A C   1 
ATOM   424  O  O   . THR A 1 58  ? 85.991  217.448 -0.337  1.00 49.16  ? 58  THR A O   1 
ATOM   425  C  CB  . THR A 1 58  ? 86.613  217.636 -3.602  1.00 50.51  ? 58  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 58  ? 87.044  218.412 -4.732  1.00 55.42  ? 58  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 58  ? 85.101  217.407 -3.638  1.00 44.11  ? 58  THR A CG2 1 
ATOM   428  N  N   . SER A 1 59  ? 87.890  216.461 -1.062  1.00 39.77  ? 59  SER A N   1 
ATOM   429  C  CA  . SER A 1 59  ? 87.851  215.397 -0.070  1.00 42.67  ? 59  SER A CA  1 
ATOM   430  C  C   . SER A 1 59  ? 88.395  215.869 1.294   1.00 42.76  ? 59  SER A C   1 
ATOM   431  O  O   . SER A 1 59  ? 88.056  215.294 2.310   1.00 42.29  ? 59  SER A O   1 
ATOM   432  C  CB  . SER A 1 59  ? 88.626  214.162 -0.581  1.00 40.27  ? 59  SER A CB  1 
ATOM   433  O  OG  . SER A 1 59  ? 89.925  214.511 -1.053  1.00 32.52  ? 59  SER A OG  1 
ATOM   434  N  N   . ALA A 1 60  ? 89.240  216.907 1.306   1.00 39.37  ? 60  ALA A N   1 
ATOM   435  C  CA  . ALA A 1 60  ? 89.835  217.368 2.559   1.00 39.87  ? 60  ALA A CA  1 
ATOM   436  C  C   . ALA A 1 60  ? 88.893  218.282 3.330   1.00 46.29  ? 60  ALA A C   1 
ATOM   437  O  O   . ALA A 1 60  ? 89.116  218.549 4.522   1.00 37.12  ? 60  ALA A O   1 
ATOM   438  C  CB  . ALA A 1 60  ? 91.154  218.085 2.303   1.00 30.39  ? 60  ALA A CB  1 
ATOM   439  N  N   . GLY A 1 61  ? 87.847  218.771 2.665   1.00 37.15  ? 61  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? 86.878  219.606 3.356   1.00 32.45  ? 61  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? 87.295  221.046 3.628   1.00 34.92  ? 61  GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? 88.378  221.500 3.255   1.00 27.57  ? 61  GLY A O   1 
ATOM   443  N  N   . PRO A 1 62  ? 86.406  221.796 4.271   1.00 30.66  ? 62  PRO A N   1 
ATOM   444  C  CA  . PRO A 1 62  ? 86.773  223.171 4.650   1.00 32.06  ? 62  PRO A CA  1 
ATOM   445  C  C   . PRO A 1 62  ? 87.810  223.191 5.795   1.00 31.28  ? 62  PRO A C   1 
ATOM   446  O  O   . PRO A 1 62  ? 88.267  222.136 6.246   1.00 28.51  ? 62  PRO A O   1 
ATOM   447  C  CB  . PRO A 1 62  ? 85.428  223.794 5.080   1.00 29.78  ? 62  PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 62  ? 84.569  222.618 5.506   1.00 34.65  ? 62  PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 62  ? 85.033  221.418 4.662   1.00 26.92  ? 62  PRO A CD  1 
ATOM   450  N  N   . HIS A 1 63  ? 88.212  224.379 6.219   1.00 27.62  ? 63  HIS A N   1 
ATOM   451  C  CA  . HIS A 1 63  ? 89.060  224.525 7.402   1.00 26.77  ? 63  HIS A CA  1 
ATOM   452  C  C   . HIS A 1 63  ? 88.460  223.784 8.559   1.00 26.22  ? 63  HIS A C   1 
ATOM   453  O  O   . HIS A 1 63  ? 87.243  223.793 8.746   1.00 25.87  ? 63  HIS A O   1 
ATOM   454  C  CB  . HIS A 1 63  ? 89.238  226.005 7.758   1.00 21.85  ? 63  HIS A CB  1 
ATOM   455  C  CG  . HIS A 1 63  ? 89.946  226.773 6.701   1.00 29.57  ? 63  HIS A CG  1 
ATOM   456  N  ND1 . HIS A 1 63  ? 90.330  228.083 6.857   1.00 35.99  ? 63  HIS A ND1 1 
ATOM   457  C  CD2 . HIS A 1 63  ? 90.374  226.396 5.471   1.00 24.88  ? 63  HIS A CD2 1 
ATOM   458  C  CE1 . HIS A 1 63  ? 90.950  228.489 5.761   1.00 26.25  ? 63  HIS A CE1 1 
ATOM   459  N  NE2 . HIS A 1 63  ? 91.004  227.479 4.914   1.00 24.73  ? 63  HIS A NE2 1 
ATOM   460  N  N   . PHE A 1 64  ? 89.320  223.113 9.316   1.00 27.22  ? 64  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 64  ? 88.884  222.399 10.507  1.00 27.98  ? 64  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 64  ? 88.188  223.415 11.419  1.00 32.76  ? 64  PHE A C   1 
ATOM   463  O  O   . PHE A 1 64  ? 88.796  224.433 11.820  1.00 25.64  ? 64  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 64  ? 90.053  221.713 11.199  1.00 24.18  ? 64  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 64  ? 89.665  220.962 12.423  1.00 28.50  ? 64  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 64  ? 88.513  220.184 12.442  1.00 23.85  ? 64  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 64  ? 90.456  221.011 13.558  1.00 28.43  ? 64  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 64  ? 88.163  219.470 13.571  1.00 24.20  ? 64  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 64  ? 90.108  220.292 14.698  1.00 26.58  ? 64  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 64  ? 88.955  219.523 14.699  1.00 29.79  ? 64  PHE A CZ  1 
ATOM   471  N  N   . ASN A 1 65  ? 86.906  223.144 11.685  1.00 21.84  ? 65  ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? 86.014  224.114 12.303  1.00 30.57  ? 65  ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? 84.944  223.474 13.201  1.00 37.09  ? 65  ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? 83.755  223.611 12.933  1.00 36.50  ? 65  ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? 85.336  224.920 11.209  1.00 26.68  ? 65  ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? 84.558  226.095 11.732  1.00 34.62  ? 65  ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? 84.792  226.582 12.843  1.00 33.70  ? 65  ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? 83.571  226.535 10.943  1.00 30.64  ? 65  ASN A ND2 1 
ATOM   479  N  N   . PRO A 1 66  ? 85.353  222.768 14.268  1.00 33.69  ? 66  PRO A N   1 
ATOM   480  C  CA  . PRO A 1 66  ? 84.321  222.081 15.055  1.00 33.70  ? 66  PRO A CA  1 
ATOM   481  C  C   . PRO A 1 66  ? 83.418  223.026 15.817  1.00 36.51  ? 66  PRO A C   1 
ATOM   482  O  O   . PRO A 1 66  ? 82.313  222.631 16.156  1.00 42.96  ? 66  PRO A O   1 
ATOM   483  C  CB  . PRO A 1 66  ? 85.124  221.216 16.019  1.00 30.40  ? 66  PRO A CB  1 
ATOM   484  C  CG  . PRO A 1 66  ? 86.475  221.890 16.110  1.00 35.43  ? 66  PRO A CG  1 
ATOM   485  C  CD  . PRO A 1 66  ? 86.711  222.529 14.777  1.00 28.31  ? 66  PRO A CD  1 
ATOM   486  N  N   . LEU A 1 67  ? 83.838  224.268 16.014  1.00 34.16  ? 67  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 67  ? 83.024  225.211 16.757  1.00 32.37  ? 67  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 67  ? 82.121  226.049 15.832  1.00 39.43  ? 67  LEU A C   1 
ATOM   489  O  O   . LEU A 1 67  ? 81.355  226.901 16.318  1.00 36.06  ? 67  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 67  ? 83.930  226.128 17.582  1.00 32.89  ? 67  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 67  ? 84.761  225.409 18.642  1.00 37.89  ? 67  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 67  ? 85.646  226.370 19.367  1.00 33.11  ? 67  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 67  ? 83.831  224.693 19.618  1.00 39.56  ? 67  LEU A CD2 1 
ATOM   494  N  N   . SER A 1 68  ? 82.195  225.783 14.518  1.00 35.83  ? 68  SER A N   1 
ATOM   495  C  CA  . SER A 1 68  ? 81.385  226.499 13.504  1.00 35.14  ? 68  SER A CA  1 
ATOM   496  C  C   . SER A 1 68  ? 81.568  228.000 13.623  1.00 31.58  ? 68  SER A C   1 
ATOM   497  O  O   . SER A 1 68  ? 80.641  228.750 13.909  1.00 40.84  ? 68  SER A O   1 
ATOM   498  C  CB  . SER A 1 68  ? 79.893  226.143 13.602  1.00 35.26  ? 68  SER A CB  1 
ATOM   499  O  OG  . SER A 1 68  ? 79.678  224.736 13.461  1.00 38.91  ? 68  SER A OG  1 
ATOM   500  N  N   . ARG A 1 69  ? 82.799  228.432 13.466  1.00 33.87  ? 69  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 69  ? 83.099  229.837 13.507  1.00 30.15  ? 69  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 69  ? 83.332  230.299 12.082  1.00 38.67  ? 69  ARG A C   1 
ATOM   503  O  O   . ARG A 1 69  ? 83.269  229.496 11.157  1.00 33.17  ? 69  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 69  ? 84.336  230.087 14.381  1.00 35.60  ? 69  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 69  ? 84.229  229.613 15.838  1.00 37.39  ? 69  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 69  ? 83.306  230.541 16.629  1.00 28.93  ? 69  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 69  ? 82.695  229.864 17.766  1.00 40.29  ? 69  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 69  ? 83.278  229.723 18.956  1.00 33.57  ? 69  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 69  ? 84.505  230.187 19.164  1.00 32.92  1 69  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 69  ? 82.647  229.087 19.920  1.00 27.27  ? 69  ARG A NH2 1 
ATOM   511  N  N   . LYS A 1 70  ? 83.595  231.589 11.924  1.00 34.09  ? 70  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 70  ? 84.062  232.157 10.674  1.00 42.90  ? 70  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 70  ? 85.578  232.193 10.672  1.00 41.02  ? 70  LYS A C   1 
ATOM   514  O  O   . LYS A 1 70  ? 86.212  232.138 11.729  1.00 34.56  ? 70  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 70  ? 83.470  233.555 10.474  1.00 32.26  ? 70  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 70  ? 81.971  233.450 10.292  1.00 36.47  ? 70  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 70  ? 81.275  234.752 10.049  1.00 42.14  ? 70  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 70  ? 79.766  234.479 9.883   1.00 65.87  ? 70  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 70  ? 79.453  233.333 8.931   1.00 38.80  1 70  LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 71  ? 86.149  232.337 9.484   1.00 27.78  ? 71  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 71  ? 87.591  232.308 9.311   1.00 29.18  ? 71  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 71  ? 88.249  233.499 9.995   1.00 26.85  ? 71  HIS A C   1 
ATOM   523  O  O   . HIS A 1 71  ? 87.671  234.583 10.044  1.00 27.93  ? 71  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 71  ? 87.928  232.283 7.810   1.00 32.70  ? 71  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 71  ? 89.390  232.297 7.519   1.00 23.17  ? 71  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 71  ? 90.169  231.159 7.558   1.00 20.71  ? 71  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 71  ? 90.227  233.324 7.235   1.00 25.45  ? 71  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 71  ? 91.422  231.485 7.294   1.00 27.21  ? 71  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 71  ? 91.486  232.792 7.091   1.00 27.52  ? 71  HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 72  ? 89.448  233.296 10.536  1.00 28.26  ? 72  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 72  ? 90.211  234.392 11.103  1.00 28.25  ? 72  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 72  ? 91.716  234.153 11.142  1.00 31.30  ? 72  GLY A C   1 
ATOM   533  O  O   . GLY A 1 72  ? 92.201  233.090 10.766  1.00 30.14  ? 72  GLY A O   1 
ATOM   534  N  N   . GLY A 1 73  ? 92.452  235.164 11.589  1.00 24.99  ? 73  GLY A N   1 
ATOM   535  C  CA  . GLY A 1 73  ? 93.866  235.029 11.868  1.00 36.14  ? 73  GLY A CA  1 
ATOM   536  C  C   . GLY A 1 73  ? 93.986  234.230 13.154  1.00 34.57  ? 73  GLY A C   1 
ATOM   537  O  O   . GLY A 1 73  ? 93.009  234.104 13.884  1.00 37.51  ? 73  GLY A O   1 
ATOM   538  N  N   . PRO A 1 74  ? 95.177  233.673 13.432  1.00 36.77  ? 74  PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? 95.303  232.791 14.601  1.00 38.96  ? 74  PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? 95.057  233.513 15.932  1.00 41.01  ? 74  PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? 94.537  232.912 16.859  1.00 34.09  ? 74  PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? 96.755  232.271 14.507  1.00 41.07  ? 74  PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? 97.468  233.204 13.601  1.00 28.45  ? 74  PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? 96.419  233.740 12.644  1.00 36.66  ? 74  PRO A CD  1 
ATOM   545  N  N   . LYS A 1 75  ? 95.389  234.796 15.995  1.00 40.99  ? 75  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 75  ? 95.259  235.572 17.221  1.00 42.89  ? 75  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 75  ? 93.831  236.086 17.392  1.00 49.17  ? 75  LYS A C   1 
ATOM   548  O  O   . LYS A 1 75  ? 93.513  236.716 18.391  1.00 54.32  ? 75  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 75  ? 96.262  236.741 17.231  1.00 40.10  ? 75  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 75  ? 97.741  236.302 17.266  1.00 52.04  ? 75  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 75  ? 98.725  237.486 17.337  1.00 65.28  ? 75  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 75  ? 98.615  238.389 16.092  1.00 79.23  ? 75  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 75  ? 99.496  239.604 16.107  1.00 76.21  1 75  LYS A NZ  1 
ATOM   554  N  N   . ASP A 1 76  ? 92.974  235.852 16.403  1.00 48.25  ? 76  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 76  ? 91.638  236.423 16.475  1.00 42.26  ? 76  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 76  ? 90.720  235.569 17.328  1.00 38.89  ? 76  ASP A C   1 
ATOM   557  O  O   . ASP A 1 76  ? 90.820  234.345 17.363  1.00 39.98  ? 76  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 76  ? 91.049  236.630 15.063  1.00 43.91  ? 76  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 76  ? 91.833  237.668 14.246  1.00 48.72  ? 76  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 76  ? 92.437  238.570 14.866  1.00 55.69  ? 76  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 76  ? 91.848  237.594 12.989  1.00 56.08  1 76  ASP A OD2 1 
ATOM   562  N  N   . GLU A 1 77  ? 89.802  236.251 17.996  1.00 42.57  ? 77  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 77  ? 88.768  235.637 18.819  1.00 37.54  ? 77  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 77  ? 87.798  234.795 17.974  1.00 37.22  ? 77  GLU A C   1 
ATOM   565  O  O   . GLU A 1 77  ? 87.263  233.788 18.427  1.00 40.67  ? 77  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 77  ? 88.039  236.751 19.586  1.00 47.00  ? 77  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 77  ? 87.189  236.293 20.760  1.00 38.63  ? 77  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 77  ? 86.958  237.415 21.785  1.00 66.16  ? 77  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 77  ? 86.617  238.549 21.357  1.00 56.74  ? 77  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 77  ? 87.120  237.160 23.014  1.00 56.09  1 77  GLU A OE2 1 
ATOM   571  N  N   . GLU A 1 78  ? 87.508  235.284 16.775  1.00 39.75  ? 78  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 78  ? 86.743  234.557 15.777  1.00 30.05  ? 78  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 78  ? 87.669  233.905 14.730  1.00 37.71  ? 78  GLU A C   1 
ATOM   574  O  O   . GLU A 1 78  ? 88.315  234.609 13.949  1.00 40.05  ? 78  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 78  ? 85.765  235.502 15.089  1.00 33.99  ? 78  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 78  ? 84.827  234.812 14.097  1.00 33.61  ? 78  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 78  ? 83.709  234.078 14.789  1.00 44.83  ? 78  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 78  ? 83.558  234.240 16.032  1.00 53.50  ? 78  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 78  ? 82.967  233.346 14.093  1.00 46.48  1 78  GLU A OE2 1 
ATOM   580  N  N   . ARG A 1 79  ? 87.745  232.577 14.715  1.00 36.68  ? 79  ARG A N   1 
ATOM   581  C  CA  . ARG A 1 79  ? 88.646  231.863 13.810  1.00 30.71  ? 79  ARG A CA  1 
ATOM   582  C  C   . ARG A 1 79  ? 88.228  230.394 13.771  1.00 33.21  ? 79  ARG A C   1 
ATOM   583  O  O   . ARG A 1 79  ? 87.537  229.920 14.672  1.00 33.06  ? 79  ARG A O   1 
ATOM   584  C  CB  . ARG A 1 79  ? 90.109  231.992 14.254  1.00 23.51  ? 79  ARG A CB  1 
ATOM   585  C  CG  . ARG A 1 79  ? 90.317  231.516 15.716  1.00 27.74  ? 79  ARG A CG  1 
ATOM   586  C  CD  . ARG A 1 79  ? 91.770  231.234 16.009  1.00 27.97  ? 79  ARG A CD  1 
ATOM   587  N  NE  . ARG A 1 79  ? 92.161  229.917 15.498  1.00 30.61  ? 79  ARG A NE  1 
ATOM   588  C  CZ  . ARG A 1 79  ? 93.342  229.364 15.730  1.00 32.96  ? 79  ARG A CZ  1 
ATOM   589  N  NH1 . ARG A 1 79  ? 94.214  230.025 16.467  1.00 29.77  1 79  ARG A NH1 1 
ATOM   590  N  NH2 . ARG A 1 79  ? 93.645  228.156 15.243  1.00 30.23  ? 79  ARG A NH2 1 
ATOM   591  N  N   . HIS A 1 80  ? 88.600  229.690 12.708  1.00 27.34  ? 80  HIS A N   1 
ATOM   592  C  CA  . HIS A 1 80  ? 88.418  228.236 12.674  1.00 30.70  ? 80  HIS A CA  1 
ATOM   593  C  C   . HIS A 1 80  ? 89.498  227.641 13.560  1.00 27.42  ? 80  HIS A C   1 
ATOM   594  O  O   . HIS A 1 80  ? 90.538  228.281 13.773  1.00 31.10  ? 80  HIS A O   1 
ATOM   595  C  CB  . HIS A 1 80  ? 88.523  227.666 11.252  1.00 25.47  ? 80  HIS A CB  1 
ATOM   596  C  CG  . HIS A 1 80  ? 87.539  228.243 10.277  1.00 26.72  ? 80  HIS A CG  1 
ATOM   597  N  ND1 . HIS A 1 80  ? 87.895  228.624 8.999   1.00 29.48  ? 80  HIS A ND1 1 
ATOM   598  C  CD2 . HIS A 1 80  ? 86.206  228.462 10.376  1.00 30.69  ? 80  HIS A CD2 1 
ATOM   599  C  CE1 . HIS A 1 80  ? 86.833  229.086 8.367   1.00 31.93  ? 80  HIS A CE1 1 
ATOM   600  N  NE2 . HIS A 1 80  ? 85.794  228.990 9.177   1.00 34.21  ? 80  HIS A NE2 1 
ATOM   601  N  N   . VAL A 1 81  ? 89.276  226.440 14.083  1.00 28.79  ? 81  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 81  ? 90.347  225.762 14.824  1.00 29.76  ? 81  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 81  ? 91.583  225.580 13.956  1.00 26.55  ? 81  VAL A C   1 
ATOM   604  O  O   . VAL A 1 81  ? 92.702  225.756 14.425  1.00 27.41  ? 81  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 81  ? 89.912  224.378 15.380  1.00 31.82  ? 81  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 81  ? 91.154  223.597 15.916  1.00 25.86  ? 81  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 81  ? 88.875  224.555 16.489  1.00 25.14  ? 81  VAL A CG2 1 
ATOM   608  N  N   . GLY A 1 82  ? 91.363  225.256 12.677  1.00 32.54  ? 82  GLY A N   1 
ATOM   609  C  CA  . GLY A 1 82  ? 92.440  225.004 11.738  1.00 24.91  ? 82  GLY A CA  1 
ATOM   610  C  C   . GLY A 1 82  ? 93.220  226.215 11.253  1.00 32.57  ? 82  GLY A C   1 
ATOM   611  O  O   . GLY A 1 82  ? 94.186  226.049 10.506  1.00 30.95  ? 82  GLY A O   1 
ATOM   612  N  N   . ASP A 1 83  ? 92.845  227.423 11.679  1.00 30.19  ? 83  ASP A N   1 
ATOM   613  C  CA  . ASP A 1 83  ? 93.487  228.612 11.118  1.00 31.74  ? 83  ASP A CA  1 
ATOM   614  C  C   . ASP A 1 83  ? 94.823  228.969 11.761  1.00 32.07  ? 83  ASP A C   1 
ATOM   615  O  O   . ASP A 1 83  ? 94.867  229.515 12.843  1.00 40.54  ? 83  ASP A O   1 
ATOM   616  C  CB  . ASP A 1 83  ? 92.550  229.810 11.220  1.00 25.78  ? 83  ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 83  ? 91.335  229.665 10.345  1.00 34.37  ? 83  ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 83  ? 91.362  228.818 9.407   1.00 28.24  ? 83  ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 83  ? 90.349  230.394 10.615  1.00 30.34  1 83  ASP A OD2 1 
ATOM   620  N  N   . LEU A 1 84  ? 95.907  228.742 11.048  1.00 31.45  ? 84  LEU A N   1 
ATOM   621  C  CA  . LEU A 1 84  ? 97.238  228.990 11.573  1.00 33.63  ? 84  LEU A CA  1 
ATOM   622  C  C   . LEU A 1 84  ? 97.901  230.178 10.874  1.00 39.23  ? 84  LEU A C   1 
ATOM   623  O  O   . LEU A 1 84  ? 99.126  230.305 10.872  1.00 39.81  ? 84  LEU A O   1 
ATOM   624  C  CB  . LEU A 1 84  ? 98.104  227.742 11.429  1.00 20.45  ? 84  LEU A CB  1 
ATOM   625  C  CG  . LEU A 1 84  ? 97.570  226.544 12.208  1.00 29.07  ? 84  LEU A CG  1 
ATOM   626  C  CD1 . LEU A 1 84  ? 98.465  225.341 11.967  1.00 33.28  ? 84  LEU A CD1 1 
ATOM   627  C  CD2 . LEU A 1 84  ? 97.453  226.836 13.687  1.00 24.58  ? 84  LEU A CD2 1 
ATOM   628  N  N   . GLY A 1 85  ? 97.107  231.006 10.209  1.00 33.44  ? 85  GLY A N   1 
ATOM   629  C  CA  . GLY A 1 85  ? 97.653  232.241 9.689   1.00 34.22  ? 85  GLY A CA  1 
ATOM   630  C  C   . GLY A 1 85  ? 98.587  232.083 8.513   1.00 35.98  ? 85  GLY A C   1 
ATOM   631  O  O   . GLY A 1 85  ? 98.306  231.354 7.557   1.00 29.63  ? 85  GLY A O   1 
ATOM   632  N  N   . ASN A 1 86  ? 99.707  232.790 8.577   1.00 41.28  ? 86  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 86  ? 100.677 232.789 7.491   1.00 36.49  ? 86  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 86  ? 102.047 232.325 7.904   1.00 39.79  ? 86  ASN A C   1 
ATOM   635  O  O   . ASN A 1 86  ? 102.544 232.672 8.977   1.00 35.62  ? 86  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 86  ? 100.810 234.185 6.895   1.00 40.22  ? 86  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 86  ? 99.596  234.585 6.101   1.00 38.55  ? 86  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 86  ? 99.180  233.873 5.182   1.00 40.58  ? 86  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 86  ? 99.016  235.726 6.444   1.00 39.53  ? 86  ASN A ND2 1 
ATOM   640  N  N   . VAL A 1 87  ? 102.681 231.562 7.034   1.00 34.01  ? 87  VAL A N   1 
ATOM   641  C  CA  . VAL A 1 87  ? 104.100 231.336 7.206   1.00 37.08  ? 87  VAL A CA  1 
ATOM   642  C  C   . VAL A 1 87  ? 104.823 232.266 6.261   1.00 35.92  ? 87  VAL A C   1 
ATOM   643  O  O   . VAL A 1 87  ? 104.249 232.715 5.273   1.00 33.71  ? 87  VAL A O   1 
ATOM   644  C  CB  . VAL A 1 87  ? 104.497 229.878 6.961   1.00 40.00  ? 87  VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 87  ? 103.830 228.995 8.004   1.00 37.35  ? 87  VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 87  ? 104.185 229.470 5.513   1.00 27.70  ? 87  VAL A CG2 1 
ATOM   647  N  N   . THR A 1 88  ? 106.053 232.606 6.623   1.00 39.73  ? 88  THR A N   1 
ATOM   648  C  CA  . THR A 1 88  ? 106.853 233.556 5.859   1.00 46.37  ? 88  THR A CA  1 
ATOM   649  C  C   . THR A 1 88  ? 108.071 232.917 5.217   1.00 40.47  ? 88  THR A C   1 
ATOM   650  O  O   . THR A 1 88  ? 108.929 232.380 5.899   1.00 46.32  ? 88  THR A O   1 
ATOM   651  C  CB  . THR A 1 88  ? 107.337 234.722 6.733   1.00 49.12  ? 88  THR A CB  1 
ATOM   652  O  OG1 . THR A 1 88  ? 106.222 235.274 7.441   1.00 55.81  ? 88  THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 88  ? 107.971 235.814 5.858   1.00 40.99  ? 88  THR A CG2 1 
ATOM   654  N  N   . ALA A 1 89  ? 108.148 232.997 3.899   1.00 44.62  ? 89  ALA A N   1 
ATOM   655  C  CA  . ALA A 1 89  ? 109.305 232.483 3.176   1.00 44.24  ? 89  ALA A CA  1 
ATOM   656  C  C   . ALA A 1 89  ? 110.318 233.597 2.968   1.00 46.59  ? 89  ALA A C   1 
ATOM   657  O  O   . ALA A 1 89  ? 109.959 234.693 2.531   1.00 50.66  ? 89  ALA A O   1 
ATOM   658  C  CB  . ALA A 1 89  ? 108.885 231.898 1.839   1.00 43.79  ? 89  ALA A CB  1 
ATOM   659  N  N   . ASP A 1 90  ? 111.581 233.327 3.281   1.00 53.71  ? 90  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 90  ? 112.619 234.322 3.047   1.00 49.85  ? 90  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 90  ? 113.003 234.369 1.560   1.00 52.82  ? 90  ASP A C   1 
ATOM   662  O  O   . ASP A 1 90  ? 112.335 233.770 0.715   1.00 51.35  ? 90  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 90  ? 113.843 234.070 3.950   1.00 50.25  ? 90  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 90  ? 114.542 232.728 3.690   1.00 60.70  ? 90  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 90  ? 114.416 232.125 2.591   1.00 54.12  ? 90  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 90  ? 115.273 232.286 4.608   1.00 66.10  1 90  ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 91  ? 114.054 235.122 1.246   1.00 60.24  ? 91  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 91  ? 114.498 235.310 -0.134  1.00 63.48  ? 91  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 91  ? 114.931 234.008 -0.809  1.00 60.53  ? 91  LYS A C   1 
ATOM   670  O  O   . LYS A 1 91  ? 114.836 233.874 -2.038  1.00 53.15  ? 91  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 91  ? 115.616 236.358 -0.169  1.00 65.80  ? 91  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 91  ? 116.646 236.207 0.949   1.00 76.28  ? 91  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 91  ? 117.688 237.320 0.916   1.00 76.18  ? 91  LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 91  ? 118.670 237.209 2.078   1.00 74.68  ? 91  LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 91  ? 119.703 238.277 2.009   1.00 79.35  1 91  LYS A NZ  1 
ATOM   676  N  N   . ASP A 1 92  ? 115.366 233.039 -0.008  1.00 52.45  ? 92  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? 115.872 231.773 -0.543  1.00 58.24  ? 92  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? 114.740 230.758 -0.639  1.00 58.57  ? 92  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? 114.962 229.569 -0.890  1.00 54.20  ? 92  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? 117.021 231.240 0.319   1.00 60.73  ? 92  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? 118.175 232.229 0.423   1.00 74.67  ? 92  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? 118.880 232.411 -0.597  1.00 72.94  ? 92  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? 118.372 232.832 1.510   1.00 75.48  1 92  ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 93  ? 113.523 231.260 -0.438  1.00 54.58  ? 93  GLY A N   1 
ATOM   685  C  CA  . GLY A 1 93  ? 112.306 230.492 -0.578  1.00 49.68  ? 93  GLY A CA  1 
ATOM   686  C  C   . GLY A 1 93  ? 112.023 229.556 0.573   1.00 45.56  ? 93  GLY A C   1 
ATOM   687  O  O   . GLY A 1 93  ? 111.224 228.633 0.442   1.00 44.30  ? 93  GLY A O   1 
ATOM   688  N  N   . VAL A 1 94  ? 112.639 229.818 1.717   1.00 44.68  ? 94  VAL A N   1 
ATOM   689  C  CA  . VAL A 1 94  ? 112.482 228.924 2.854   1.00 49.65  ? 94  VAL A CA  1 
ATOM   690  C  C   . VAL A 1 94  ? 111.679 229.559 3.971   1.00 46.55  ? 94  VAL A C   1 
ATOM   691  O  O   . VAL A 1 94  ? 112.034 230.630 4.462   1.00 47.66  ? 94  VAL A O   1 
ATOM   692  C  CB  . VAL A 1 94  ? 113.850 228.492 3.419   1.00 52.88  ? 94  VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 94  ? 113.657 227.747 4.719   1.00 44.53  ? 94  VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 94  ? 114.577 227.598 2.406   1.00 42.88  ? 94  VAL A CG2 1 
ATOM   695  N  N   . ALA A 1 95  ? 110.592 228.903 4.372   1.00 45.56  ? 95  ALA A N   1 
ATOM   696  C  CA  . ALA A 1 95  ? 109.822 229.372 5.525   1.00 43.82  ? 95  ALA A CA  1 
ATOM   697  C  C   . ALA A 1 95  ? 110.174 228.563 6.758   1.00 41.93  ? 95  ALA A C   1 
ATOM   698  O  O   . ALA A 1 95  ? 109.887 227.366 6.814   1.00 46.27  ? 95  ALA A O   1 
ATOM   699  C  CB  . ALA A 1 95  ? 108.298 229.300 5.248   1.00 35.98  ? 95  ALA A CB  1 
ATOM   700  N  N   . ASP A 1 96  ? 110.792 229.211 7.742   1.00 47.89  ? 96  ASP A N   1 
ATOM   701  C  CA  . ASP A 1 96  ? 111.070 228.558 9.018   1.00 41.69  ? 96  ASP A CA  1 
ATOM   702  C  C   . ASP A 1 96  ? 109.919 228.843 9.972   1.00 51.49  ? 96  ASP A C   1 
ATOM   703  O  O   . ASP A 1 96  ? 109.677 229.975 10.397  1.00 49.52  ? 96  ASP A O   1 
ATOM   704  C  CB  . ASP A 1 96  ? 112.418 228.995 9.609   1.00 52.86  ? 96  ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 96  ? 113.610 228.427 8.835   1.00 69.38  ? 96  ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 96  ? 113.808 227.186 8.863   1.00 67.99  ? 96  ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 96  ? 114.347 229.211 8.199   1.00 73.22  1 96  ASP A OD2 1 
ATOM   708  N  N   . VAL A 1 97  ? 109.201 227.776 10.280  1.00 39.36  ? 97  VAL A N   1 
ATOM   709  C  CA  . VAL A 1 97  ? 107.943 227.863 10.985  1.00 44.39  ? 97  VAL A CA  1 
ATOM   710  C  C   . VAL A 1 97  ? 108.173 227.686 12.457  1.00 38.03  ? 97  VAL A C   1 
ATOM   711  O  O   . VAL A 1 97  ? 108.781 226.696 12.884  1.00 39.38  ? 97  VAL A O   1 
ATOM   712  C  CB  . VAL A 1 97  ? 106.970 226.785 10.511  1.00 44.52  ? 97  VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 97  ? 105.687 226.877 11.299  1.00 38.51  ? 97  VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 97  ? 106.722 226.955 9.046   1.00 34.62  ? 97  VAL A CG2 1 
ATOM   715  N  N   . SER A 1 98  ? 107.735 228.660 13.233  1.00 43.26  ? 98  SER A N   1 
ATOM   716  C  CA  . SER A 1 98  ? 107.826 228.540 14.672  1.00 42.45  ? 98  SER A CA  1 
ATOM   717  C  C   . SER A 1 98  ? 106.588 229.183 15.272  1.00 47.79  ? 98  SER A C   1 
ATOM   718  O  O   . SER A 1 98  ? 106.430 230.393 15.238  1.00 43.50  ? 98  SER A O   1 
ATOM   719  C  CB  . SER A 1 98  ? 109.116 229.180 15.167  1.00 45.22  ? 98  SER A CB  1 
ATOM   720  O  OG  . SER A 1 98  ? 109.576 228.539 16.344  1.00 56.26  ? 98  SER A OG  1 
ATOM   721  N  N   . ILE A 1 99  ? 105.692 228.344 15.777  1.00 50.04  ? 99  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 99  ? 104.359 228.752 16.221  1.00 40.76  ? 99  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 99  ? 104.022 228.123 17.572  1.00 39.05  ? 99  ILE A C   1 
ATOM   724  O  O   . ILE A 1 99  ? 104.393 226.981 17.853  1.00 42.52  ? 99  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 99  ? 103.265 228.328 15.180  1.00 39.10  ? 99  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 99  ? 103.408 229.088 13.874  1.00 45.56  ? 99  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 99  ? 101.864 228.547 15.705  1.00 35.26  ? 99  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 99  ? 102.521 228.533 12.778  1.00 42.59  ? 99  ILE A CD1 1 
ATOM   729  N  N   . GLU A 1 100 ? 103.350 228.887 18.418  1.00 40.45  ? 100 GLU A N   1 
ATOM   730  C  CA  . GLU A 1 100 ? 102.612 228.342 19.542  1.00 39.97  ? 100 GLU A CA  1 
ATOM   731  C  C   . GLU A 1 100 ? 101.162 228.676 19.290  1.00 37.82  ? 100 GLU A C   1 
ATOM   732  O  O   . GLU A 1 100 ? 100.835 229.836 19.014  1.00 39.41  ? 100 GLU A O   1 
ATOM   733  C  CB  . GLU A 1 100 ? 103.062 228.930 20.880  1.00 44.32  ? 100 GLU A CB  1 
ATOM   734  C  CG  . GLU A 1 100 ? 104.111 228.120 21.637  1.00 56.43  ? 100 GLU A CG  1 
ATOM   735  C  CD  . GLU A 1 100 ? 104.168 228.496 23.121  1.00 77.41  ? 100 GLU A CD  1 
ATOM   736  O  OE1 . GLU A 1 100 ? 104.038 229.696 23.458  1.00 82.16  ? 100 GLU A OE1 1 
ATOM   737  O  OE2 . GLU A 1 100 ? 104.338 227.584 23.957  1.00 85.73  1 100 GLU A OE2 1 
ATOM   738  N  N   . ASP A 1 101 ? 100.291 227.675 19.388  1.00 34.38  ? 101 ASP A N   1 
ATOM   739  C  CA  . ASP A 1 101 ? 98.863  227.898 19.213  1.00 32.83  ? 101 ASP A CA  1 
ATOM   740  C  C   . ASP A 1 101 ? 98.049  227.285 20.339  1.00 37.47  ? 101 ASP A C   1 
ATOM   741  O  O   . ASP A 1 101 ? 98.319  226.166 20.769  1.00 34.25  ? 101 ASP A O   1 
ATOM   742  C  CB  . ASP A 1 101 ? 98.374  227.333 17.879  1.00 30.65  ? 101 ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 101 ? 97.008  227.877 17.490  1.00 41.00  ? 101 ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 101 ? 96.934  229.100 17.180  1.00 38.42  ? 101 ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 101 ? 96.018  227.091 17.500  1.00 37.10  1 101 ASP A OD2 1 
ATOM   746  N  N   . SER A 1 102 ? 97.045  228.024 20.799  1.00 31.94  ? 102 SER A N   1 
ATOM   747  C  CA  . SER A 1 102 ? 96.238  227.591 21.929  1.00 38.65  ? 102 SER A CA  1 
ATOM   748  C  C   . SER A 1 102 ? 94.940  226.913 21.520  1.00 35.26  ? 102 SER A C   1 
ATOM   749  O  O   . SER A 1 102 ? 94.242  226.365 22.380  1.00 31.33  ? 102 SER A O   1 
ATOM   750  C  CB  . SER A 1 102 ? 95.892  228.778 22.826  1.00 39.20  ? 102 SER A CB  1 
ATOM   751  O  OG  . SER A 1 102 ? 97.022  229.590 23.020  1.00 52.73  ? 102 SER A OG  1 
ATOM   752  N  N   . VAL A 1 103 ? 94.602  226.966 20.233  1.00 32.02  ? 103 VAL A N   1 
ATOM   753  C  CA  . VAL A 1 103 ? 93.281  226.488 19.790  1.00 27.79  ? 103 VAL A CA  1 
ATOM   754  C  C   . VAL A 1 103 ? 93.353  225.075 19.219  1.00 27.63  ? 103 VAL A C   1 
ATOM   755  O  O   . VAL A 1 103 ? 92.521  224.227 19.549  1.00 25.83  ? 103 VAL A O   1 
ATOM   756  C  CB  . VAL A 1 103 ? 92.675  227.412 18.760  1.00 31.87  ? 103 VAL A CB  1 
ATOM   757  C  CG1 . VAL A 1 103 ? 91.236  227.013 18.496  1.00 29.91  ? 103 VAL A CG1 1 
ATOM   758  C  CG2 . VAL A 1 103 ? 92.764  228.852 19.243  1.00 26.43  ? 103 VAL A CG2 1 
ATOM   759  N  N   . ILE A 1 104 ? 94.374  224.788 18.408  1.00 34.44  ? 104 ILE A N   1 
ATOM   760  C  CA  . ILE A 1 104 ? 94.545  223.411 17.979  1.00 31.28  ? 104 ILE A CA  1 
ATOM   761  C  C   . ILE A 1 104 ? 94.999  222.573 19.170  1.00 38.36  ? 104 ILE A C   1 
ATOM   762  O  O   . ILE A 1 104 ? 95.449  223.098 20.190  1.00 37.90  ? 104 ILE A O   1 
ATOM   763  C  CB  . ILE A 1 104 ? 95.540  223.262 16.859  1.00 30.68  ? 104 ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 104 ? 96.875  223.879 17.247  1.00 33.11  ? 104 ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 104 ? 95.005  223.895 15.571  1.00 26.96  ? 104 ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 104 ? 97.951  223.564 16.253  1.00 28.82  ? 104 ILE A CD1 1 
ATOM   767  N  N   . SER A 1 105 ? 94.885  221.265 19.024  1.00 32.74  ? 105 SER A N   1 
ATOM   768  C  CA  . SER A 1 105 ? 95.194  220.357 20.102  1.00 36.44  ? 105 SER A CA  1 
ATOM   769  C  C   . SER A 1 105 ? 95.598  219.025 19.506  1.00 31.64  ? 105 SER A C   1 
ATOM   770  O  O   . SER A 1 105 ? 95.364  218.798 18.335  1.00 33.43  ? 105 SER A O   1 
ATOM   771  C  CB  . SER A 1 105 ? 93.988  220.189 21.020  1.00 34.68  ? 105 SER A CB  1 
ATOM   772  O  OG  . SER A 1 105 ? 94.234  219.175 21.959  1.00 44.27  ? 105 SER A OG  1 
ATOM   773  N  N   . LEU A 1 106 ? 96.210  218.152 20.298  1.00 32.83  ? 106 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 106 ? 96.523  216.816 19.815  1.00 33.88  ? 106 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 106 ? 95.578  215.786 20.430  1.00 39.15  ? 106 LEU A C   1 
ATOM   776  O  O   . LEU A 1 106 ? 95.856  214.584 20.413  1.00 43.86  ? 106 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 106 ? 97.971  216.460 20.096  1.00 34.48  ? 106 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 106 ? 99.030  217.290 19.378  1.00 29.67  ? 106 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 106 ? 100.395 216.623 19.549  1.00 32.60  ? 106 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 106 ? 98.716  217.481 17.896  1.00 30.66  ? 106 LEU A CD2 1 
ATOM   781  N  N   . SER A 1 107 ? 94.457  216.264 20.965  1.00 32.89  ? 107 SER A N   1 
ATOM   782  C  CA  . SER A 1 107 ? 93.443  215.380 21.537  1.00 40.70  ? 107 SER A CA  1 
ATOM   783  C  C   . SER A 1 107 ? 92.146  216.151 21.715  1.00 38.19  ? 107 SER A C   1 
ATOM   784  O  O   . SER A 1 107 ? 92.147  217.382 21.674  1.00 36.30  ? 107 SER A O   1 
ATOM   785  C  CB  . SER A 1 107 ? 93.930  214.803 22.877  1.00 42.80  ? 107 SER A CB  1 
ATOM   786  O  OG  . SER A 1 107 ? 94.311  215.854 23.755  1.00 50.62  ? 107 SER A OG  1 
ATOM   787  N  N   . GLY A 1 108 ? 91.037  215.436 21.887  1.00 42.70  ? 108 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 108 ? 89.754  216.074 22.159  1.00 35.71  ? 108 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 108 ? 89.084  216.642 20.915  1.00 47.61  ? 108 GLY A C   1 
ATOM   790  O  O   . GLY A 1 108 ? 89.456  216.300 19.784  1.00 36.84  ? 108 GLY A O   1 
ATOM   791  N  N   . ASP A 1 109 ? 88.124  217.545 21.118  1.00 45.53  ? 109 ASP A N   1 
ATOM   792  C  CA  . ASP A 1 109 ? 87.333  218.073 20.011  1.00 40.10  ? 109 ASP A CA  1 
ATOM   793  C  C   . ASP A 1 109 ? 88.159  218.871 19.010  1.00 38.94  ? 109 ASP A C   1 
ATOM   794  O  O   . ASP A 1 109 ? 87.791  218.935 17.853  1.00 29.77  ? 109 ASP A O   1 
ATOM   795  C  CB  . ASP A 1 109 ? 86.199  218.964 20.525  1.00 41.12  ? 109 ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 109 ? 84.994  218.167 21.024  1.00 58.83  ? 109 ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 109 ? 84.866  216.964 20.685  1.00 53.67  ? 109 ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 109 ? 84.154  218.761 21.735  1.00 64.65  1 109 ASP A OD2 1 
ATOM   799  N  N   . HIS A 1 110 ? 89.286  219.435 19.447  1.00 34.60  ? 110 HIS A N   1 
ATOM   800  C  CA  . HIS A 1 110 ? 90.134  220.237 18.568  1.00 33.80  ? 110 HIS A CA  1 
ATOM   801  C  C   . HIS A 1 110 ? 91.332  219.466 18.039  1.00 32.66  ? 110 HIS A C   1 
ATOM   802  O  O   . HIS A 1 110 ? 92.281  220.052 17.507  1.00 28.16  ? 110 HIS A O   1 
ATOM   803  C  CB  . HIS A 1 110 ? 90.678  221.469 19.286  1.00 31.93  ? 110 HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 110 ? 89.631  222.430 19.744  1.00 35.20  ? 110 HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 110 ? 89.919  223.749 20.036  1.00 39.05  ? 110 HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 110 ? 88.316  222.263 20.013  1.00 35.91  ? 110 HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 110 ? 88.818  224.358 20.444  1.00 35.92  ? 110 HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 110 ? 87.833  223.478 20.446  1.00 38.73  ? 110 HIS A NE2 1 
ATOM   809  N  N   . CYS A 1 111 ? 91.297  218.153 18.185  1.00 32.99  ? 111 CYS A N   1 
ATOM   810  C  CA  . CYS A 1 111 ? 92.413  217.328 17.757  1.00 31.60  ? 111 CYS A CA  1 
ATOM   811  C  C   . CYS A 1 111 ? 92.618  217.365 16.230  1.00 31.34  ? 111 CYS A C   1 
ATOM   812  O  O   . CYS A 1 111 ? 91.708  217.054 15.455  1.00 33.50  ? 111 CYS A O   1 
ATOM   813  C  CB  . CYS A 1 111 ? 92.196  215.903 18.223  1.00 26.99  ? 111 CYS A CB  1 
ATOM   814  S  SG  . CYS A 1 111 ? 93.408  214.800 17.612  1.00 31.79  ? 111 CYS A SG  1 
ATOM   815  N  N   . ILE A 1 112 ? 93.825  217.720 15.818  1.00 28.00  ? 112 ILE A N   1 
ATOM   816  C  CA  . ILE A 1 112 ? 94.157  217.847 14.408  1.00 33.97  ? 112 ILE A CA  1 
ATOM   817  C  C   . ILE A 1 112 ? 94.827  216.633 13.798  1.00 30.26  ? 112 ILE A C   1 
ATOM   818  O  O   . ILE A 1 112 ? 95.126  216.635 12.613  1.00 32.37  ? 112 ILE A O   1 
ATOM   819  C  CB  . ILE A 1 112 ? 95.081  219.033 14.170  1.00 28.24  ? 112 ILE A CB  1 
ATOM   820  C  CG1 . ILE A 1 112 ? 96.348  218.883 15.018  1.00 28.09  ? 112 ILE A CG1 1 
ATOM   821  C  CG2 . ILE A 1 112 ? 94.350  220.314 14.500  1.00 26.03  ? 112 ILE A CG2 1 
ATOM   822  C  CD1 . ILE A 1 112 ? 97.397  219.924 14.700  1.00 27.62  ? 112 ILE A CD1 1 
ATOM   823  N  N   . ILE A 1 113 ? 95.087  215.601 14.592  1.00 28.48  ? 113 ILE A N   1 
ATOM   824  C  CA  . ILE A 1 113 ? 95.739  214.421 14.037  1.00 30.21  ? 113 ILE A CA  1 
ATOM   825  C  C   . ILE A 1 113 ? 94.824  213.744 13.001  1.00 27.49  ? 113 ILE A C   1 
ATOM   826  O  O   . ILE A 1 113 ? 93.612  213.638 13.186  1.00 32.31  ? 113 ILE A O   1 
ATOM   827  C  CB  . ILE A 1 113 ? 96.155  213.442 15.148  1.00 33.90  ? 113 ILE A CB  1 
ATOM   828  C  CG1 . ILE A 1 113 ? 97.245  214.085 16.003  1.00 31.35  ? 113 ILE A CG1 1 
ATOM   829  C  CG2 . ILE A 1 113 ? 96.708  212.142 14.554  1.00 32.13  ? 113 ILE A CG2 1 
ATOM   830  C  CD1 . ILE A 1 113 ? 97.438  213.395 17.284  1.00 30.92  ? 113 ILE A CD1 1 
ATOM   831  N  N   . GLY A 1 114 ? 95.404  213.324 11.889  1.00 31.77  ? 114 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 114 ? 94.624  212.682 10.837  1.00 35.56  ? 114 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 114 ? 93.940  213.679 9.908   1.00 30.58  ? 114 GLY A C   1 
ATOM   834  O  O   . GLY A 1 114 ? 93.044  213.321 9.165   1.00 33.12  ? 114 GLY A O   1 
ATOM   835  N  N   . ARG A 1 115 ? 94.325  214.945 9.988   1.00 27.58  ? 115 ARG A N   1 
ATOM   836  C  CA  . ARG A 1 115 ? 93.766  215.980 9.113   1.00 31.15  ? 115 ARG A CA  1 
ATOM   837  C  C   . ARG A 1 115 ? 94.878  216.548 8.227   1.00 30.93  ? 115 ARG A C   1 
ATOM   838  O  O   . ARG A 1 115 ? 96.074  216.408 8.524   1.00 32.24  ? 115 ARG A O   1 
ATOM   839  C  CB  . ARG A 1 115 ? 93.097  217.088 9.924   1.00 27.20  ? 115 ARG A CB  1 
ATOM   840  C  CG  . ARG A 1 115 ? 91.963  216.584 10.788  1.00 34.59  ? 115 ARG A CG  1 
ATOM   841  C  CD  . ARG A 1 115 ? 91.224  217.722 11.471  1.00 32.03  ? 115 ARG A CD  1 
ATOM   842  N  NE  . ARG A 1 115 ? 90.634  217.311 12.738  1.00 32.11  ? 115 ARG A NE  1 
ATOM   843  C  CZ  . ARG A 1 115 ? 89.485  216.649 12.870  1.00 36.08  ? 115 ARG A CZ  1 
ATOM   844  N  NH1 . ARG A 1 115 ? 88.786  216.314 11.804  1.00 25.58  1 115 ARG A NH1 1 
ATOM   845  N  NH2 . ARG A 1 115 ? 89.030  216.318 14.083  1.00 29.79  ? 115 ARG A NH2 1 
ATOM   846  N  N   . THR A 1 116 ? 94.484  217.162 7.123   1.00 35.58  ? 116 THR A N   1 
ATOM   847  C  CA  . THR A 1 116 ? 95.445  217.701 6.171   1.00 24.72  ? 116 THR A CA  1 
ATOM   848  C  C   . THR A 1 116 ? 95.927  219.062 6.610   1.00 24.86  ? 116 THR A C   1 
ATOM   849  O  O   . THR A 1 116 ? 95.121  219.954 6.855   1.00 26.81  ? 116 THR A O   1 
ATOM   850  C  CB  . THR A 1 116 ? 94.839  217.848 4.788   1.00 34.20  ? 116 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 116 ? 94.296  216.599 4.378   1.00 42.25  ? 116 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 116 ? 95.890  218.333 3.783   1.00 29.75  ? 116 THR A CG2 1 
ATOM   853  N  N   . LEU A 1 117 ? 97.246  219.209 6.694   1.00 29.98  ? 117 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 117 ? 97.904  220.500 6.850   1.00 27.10  ? 117 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 117 ? 98.247  221.024 5.443   1.00 34.86  ? 117 LEU A C   1 
ATOM   856  O  O   . LEU A 1 117 ? 98.757  220.259 4.635   1.00 30.54  ? 117 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 117 ? 99.157  220.341 7.701   1.00 29.20  ? 117 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 117 ? 100.003 221.590 7.898   1.00 34.93  ? 117 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 117 ? 99.208  222.564 8.755   1.00 27.42  ? 117 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 117 ? 101.351 221.223 8.510   1.00 33.43  ? 117 LEU A CD2 1 
ATOM   861  N  N   . VAL A 1 118 ? 97.976  222.299 5.147   1.00 25.73  ? 118 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 118 ? 98.153  222.822 3.786   1.00 28.71  ? 118 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 118 ? 98.901  224.145 3.777   1.00 32.02  ? 118 VAL A C   1 
ATOM   864  O  O   . VAL A 1 118 ? 98.693  224.980 4.663   1.00 33.75  ? 118 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 118 ? 96.769  223.050 3.060   1.00 31.61  ? 118 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 118 ? 96.986  223.333 1.593   1.00 36.58  ? 118 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 118 ? 95.892  221.842 3.147   1.00 30.56  ? 118 VAL A CG2 1 
ATOM   868  N  N   . VAL A 1 119 ? 99.771  224.355 2.791   1.00 26.44  ? 119 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 119 ? 100.380 225.679 2.628   1.00 28.96  ? 119 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 119 ? 100.043 226.206 1.239   1.00 31.87  ? 119 VAL A C   1 
ATOM   871  O  O   . VAL A 1 119 ? 100.125 225.490 0.250   1.00 29.37  ? 119 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 119 ? 101.920 225.675 2.892   1.00 32.23  ? 119 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 119 ? 102.639 224.639 2.050   1.00 29.04  ? 119 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 119 ? 102.513 227.079 2.693   1.00 35.91  ? 119 VAL A CG2 1 
ATOM   875  N  N   . HIS A 1 120 ? 99.632  227.467 1.194   1.00 33.40  ? 120 HIS A N   1 
ATOM   876  C  CA  . HIS A 1 120 ? 99.010  228.052 0.014   1.00 36.48  ? 120 HIS A CA  1 
ATOM   877  C  C   . HIS A 1 120 ? 99.946  229.016 -0.699  1.00 37.15  ? 120 HIS A C   1 
ATOM   878  O  O   . HIS A 1 120 ? 100.921 229.461 -0.121  1.00 29.42  ? 120 HIS A O   1 
ATOM   879  C  CB  . HIS A 1 120 ? 97.710  228.791 0.388   1.00 27.75  ? 120 HIS A CB  1 
ATOM   880  C  CG  . HIS A 1 120 ? 96.536  227.892 0.562   1.00 29.47  ? 120 HIS A CG  1 
ATOM   881  N  ND1 . HIS A 1 120 ? 95.543  227.778 -0.392  1.00 32.46  ? 120 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A 1 120 ? 96.190  227.054 1.566   1.00 28.98  ? 120 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A 1 120 ? 94.641  226.903 0.012   1.00 26.53  ? 120 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A 1 120 ? 95.007  226.453 1.201   1.00 41.78  ? 120 HIS A NE2 1 
ATOM   885  N  N   . GLU A 1 121 ? 99.614  229.351 -1.949  1.00 36.42  ? 121 GLU A N   1 
ATOM   886  C  CA  . GLU A 1 121 ? 100.424 230.266 -2.738  1.00 36.78  ? 121 GLU A CA  1 
ATOM   887  C  C   . GLU A 1 121 ? 100.362 231.709 -2.243  1.00 35.11  ? 121 GLU A C   1 
ATOM   888  O  O   . GLU A 1 121 ? 101.374 232.413 -2.243  1.00 40.88  ? 121 GLU A O   1 
ATOM   889  C  CB  . GLU A 1 121 ? 100.015 230.221 -4.210  1.00 40.13  ? 121 GLU A CB  1 
ATOM   890  C  CG  . GLU A 1 121 ? 100.746 231.274 -5.025  1.00 45.63  ? 121 GLU A CG  1 
ATOM   891  C  CD  . GLU A 1 121 ? 100.573 231.102 -6.509  1.00 63.61  ? 121 GLU A CD  1 
ATOM   892  O  OE1 . GLU A 1 121 ? 101.190 231.883 -7.266  1.00 73.92  ? 121 GLU A OE1 1 
ATOM   893  O  OE2 . GLU A 1 121 ? 99.815  230.198 -6.924  1.00 74.56  1 121 GLU A OE2 1 
ATOM   894  N  N   . LYS A 1 122 ? 99.183  232.149 -1.818  1.00 31.45  ? 122 LYS A N   1 
ATOM   895  C  CA  . LYS A 1 122 ? 99.018  233.543 -1.405  1.00 35.73  ? 122 LYS A CA  1 
ATOM   896  C  C   . LYS A 1 122 ? 98.776  233.659 0.099   1.00 45.80  ? 122 LYS A C   1 
ATOM   897  O  O   . LYS A 1 122 ? 98.444  232.669 0.776   1.00 40.20  ? 122 LYS A O   1 
ATOM   898  C  CB  . LYS A 1 122 ? 97.847  234.196 -2.159  1.00 31.11  ? 122 LYS A CB  1 
ATOM   899  C  CG  . LYS A 1 122 ? 97.851  233.927 -3.667  1.00 34.65  ? 122 LYS A CG  1 
ATOM   900  C  CD  . LYS A 1 122 ? 98.710  234.937 -4.402  1.00 40.25  ? 122 LYS A CD  1 
ATOM   901  C  CE  . LYS A 1 122 ? 98.580  234.792 -5.902  1.00 48.45  ? 122 LYS A CE  1 
ATOM   902  N  NZ  . LYS A 1 122 ? 99.060  236.003 -6.604  1.00 57.04  1 122 LYS A NZ  1 
ATOM   903  N  N   . ALA A 1 123 ? 98.929  234.877 0.619   1.00 40.00  ? 123 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 123 ? 98.699  235.123 2.031   1.00 30.09  ? 123 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 123 ? 97.229  234.941 2.351   1.00 40.59  ? 123 ALA A C   1 
ATOM   906  O  O   . ALA A 1 123 ? 96.332  235.209 1.533   1.00 39.80  ? 123 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 123 ? 99.157  236.517 2.416   1.00 28.39  ? 123 ALA A CB  1 
ATOM   908  N  N   . ASP A 1 124 ? 97.000  234.440 3.549   1.00 38.87  ? 124 ASP A N   1 
ATOM   909  C  CA  . ASP A 1 124 ? 95.702  234.433 4.187   1.00 36.60  ? 124 ASP A CA  1 
ATOM   910  C  C   . ASP A 1 124 ? 95.363  235.891 4.559   1.00 36.87  ? 124 ASP A C   1 
ATOM   911  O  O   . ASP A 1 124 ? 96.185  236.570 5.198   1.00 36.40  ? 124 ASP A O   1 
ATOM   912  C  CB  . ASP A 1 124 ? 95.786  233.543 5.428   1.00 39.60  ? 124 ASP A CB  1 
ATOM   913  C  CG  . ASP A 1 124 ? 94.455  233.312 6.110   1.00 40.52  ? 124 ASP A CG  1 
ATOM   914  O  OD1 . ASP A 1 124 ? 93.550  234.175 6.022   1.00 35.80  ? 124 ASP A OD1 1 
ATOM   915  O  OD2 . ASP A 1 124 ? 94.357  232.272 6.806   1.00 35.54  1 124 ASP A OD2 1 
ATOM   916  N  N   . ASP A 1 125 ? 94.185  236.385 4.158   1.00 41.02  ? 125 ASP A N   1 
ATOM   917  C  CA  . ASP A 1 125 ? 93.792  237.771 4.482   1.00 36.84  ? 125 ASP A CA  1 
ATOM   918  C  C   . ASP A 1 125 ? 93.176  237.829 5.874   1.00 30.62  ? 125 ASP A C   1 
ATOM   919  O  O   . ASP A 1 125 ? 92.666  238.858 6.307   1.00 39.10  ? 125 ASP A O   1 
ATOM   920  C  CB  . ASP A 1 125 ? 92.852  238.379 3.391   1.00 32.80  ? 125 ASP A CB  1 
ATOM   921  C  CG  . ASP A 1 125 ? 91.465  237.723 3.301   1.00 33.06  ? 125 ASP A CG  1 
ATOM   922  O  OD1 . ASP A 1 125 ? 90.942  237.131 4.262   1.00 38.33  ? 125 ASP A OD1 1 
ATOM   923  O  OD2 . ASP A 1 125 ? 90.864  237.812 2.213   1.00 47.52  1 125 ASP A OD2 1 
ATOM   924  N  N   . LEU A 1 126 ? 93.211  236.689 6.550   1.00 36.25  ? 126 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 126 ? 92.902  236.574 7.974   1.00 36.35  ? 126 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 126 ? 91.474  237.002 8.224   1.00 38.36  ? 126 LEU A C   1 
ATOM   927  O  O   . LEU A 1 126 ? 91.169  237.489 9.299   1.00 41.68  ? 126 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 126 ? 93.870  237.396 8.842   1.00 30.39  ? 126 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 126 ? 95.381  237.251 8.602   1.00 33.99  ? 126 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 126 ? 96.126  238.117 9.584   1.00 31.44  ? 126 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 126 ? 95.882  235.811 8.696   1.00 29.08  ? 126 LEU A CD2 1 
ATOM   932  N  N   . GLY A 1 127 ? 90.611  236.828 7.217   1.00 37.10  ? 127 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 127 ? 89.189  237.132 7.335   1.00 33.82  ? 127 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 127 ? 88.920  238.640 7.341   1.00 37.66  ? 127 GLY A C   1 
ATOM   935  O  O   . GLY A 1 127 ? 87.809  239.061 7.561   1.00 37.21  ? 127 GLY A O   1 
ATOM   936  N  N   . LYS A 1 128 ? 89.954  239.436 7.075   1.00 39.12  ? 128 LYS A N   1 
ATOM   937  C  CA  . LYS A 1 128 ? 89.889  240.902 7.101   1.00 42.26  ? 128 LYS A CA  1 
ATOM   938  C  C   . LYS A 1 128 ? 89.710  241.417 5.665   1.00 51.78  ? 128 LYS A C   1 
ATOM   939  O  O   . LYS A 1 128 ? 89.959  242.586 5.347   1.00 54.70  ? 128 LYS A O   1 
ATOM   940  C  CB  . LYS A 1 128 ? 91.143  241.500 7.769   1.00 45.88  ? 128 LYS A CB  1 
ATOM   941  C  CG  . LYS A 1 128 ? 91.223  241.232 9.290   1.00 47.34  ? 128 LYS A CG  1 
ATOM   942  C  CD  . LYS A 1 128 ? 92.509  241.800 9.931   1.00 63.45  ? 128 LYS A CD  1 
ATOM   943  C  CE  . LYS A 1 128 ? 92.632  241.494 11.448  1.00 69.12  ? 128 LYS A CE  1 
ATOM   944  N  NZ  . LYS A 1 128 ? 93.037  240.078 11.784  1.00 67.32  1 128 LYS A NZ  1 
ATOM   945  N  N   . GLY A 1 129 ? 89.397  240.492 4.770   1.00 53.64  ? 129 GLY A N   1 
ATOM   946  C  CA  . GLY A 1 129 ? 89.143  240.850 3.395   1.00 47.66  ? 129 GLY A CA  1 
ATOM   947  C  C   . GLY A 1 129 ? 87.705  241.351 3.285   1.00 51.07  ? 129 GLY A C   1 
ATOM   948  O  O   . GLY A 1 129 ? 86.863  241.087 4.166   1.00 48.82  ? 129 GLY A O   1 
ATOM   949  N  N   . GLY A 1 130 ? 87.429  242.127 2.242   1.00 38.34  ? 130 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 130 ? 86.103  242.700 2.083   1.00 41.30  ? 130 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 130 ? 85.176  241.888 1.197   1.00 39.79  ? 130 GLY A C   1 
ATOM   952  O  O   . GLY A 1 130 ? 84.476  242.446 0.375   1.00 45.26  ? 130 GLY A O   1 
ATOM   953  N  N   . ASN A 1 131 ? 85.150  240.579 1.389   1.00 34.72  ? 131 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 131 ? 84.260  239.708 0.647   1.00 38.89  ? 131 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 131 ? 83.866  238.522 1.508   1.00 33.69  ? 131 ASN A C   1 
ATOM   956  O  O   . ASN A 1 131 ? 84.447  238.283 2.569   1.00 35.41  ? 131 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 131 ? 84.924  239.226 -0.643  1.00 34.77  ? 131 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 131 ? 86.306  238.681 -0.389  1.00 37.57  ? 131 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 131 ? 86.481  237.492 -0.095  1.00 39.54  ? 131 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 131 ? 87.296  239.559 -0.447  1.00 38.34  ? 131 ASN A ND2 1 
ATOM   961  N  N   . GLU A 1 132 ? 82.850  237.800 1.068   1.00 30.63  ? 132 GLU A N   1 
ATOM   962  C  CA  . GLU A 1 132 ? 82.372  236.683 1.833   1.00 36.47  ? 132 GLU A CA  1 
ATOM   963  C  C   . GLU A 1 132 ? 83.404  235.563 1.881   1.00 41.95  ? 132 GLU A C   1 
ATOM   964  O  O   . GLU A 1 132 ? 83.538  234.886 2.901   1.00 41.29  ? 132 GLU A O   1 
ATOM   965  C  CB  . GLU A 1 132 ? 81.047  236.187 1.263   1.00 36.13  ? 132 GLU A CB  1 
ATOM   966  C  CG  . GLU A 1 132 ? 80.376  235.122 2.097   1.00 40.00  ? 132 GLU A CG  1 
ATOM   967  C  CD  . GLU A 1 132 ? 79.006  234.723 1.554   1.00 52.48  ? 132 GLU A CD  1 
ATOM   968  O  OE1 . GLU A 1 132 ? 78.071  234.601 2.370   1.00 66.49  ? 132 GLU A OE1 1 
ATOM   969  O  OE2 . GLU A 1 132 ? 78.855  234.527 0.326   1.00 53.39  1 132 GLU A OE2 1 
ATOM   970  N  N   . GLU A 1 133 ? 84.154  235.374 0.803   1.00 33.50  ? 133 GLU A N   1 
ATOM   971  C  CA  . GLU A 1 133 ? 85.119  234.277 0.777   1.00 38.09  ? 133 GLU A CA  1 
ATOM   972  C  C   . GLU A 1 133 ? 86.227  234.485 1.827   1.00 31.54  ? 133 GLU A C   1 
ATOM   973  O  O   . GLU A 1 133 ? 86.806  233.540 2.338   1.00 27.89  ? 133 GLU A O   1 
ATOM   974  C  CB  . GLU A 1 133 ? 85.714  234.112 -0.624  1.00 26.91  ? 133 GLU A CB  1 
ATOM   975  C  CG  . GLU A 1 133 ? 86.318  232.757 -0.859  1.00 43.51  ? 133 GLU A CG  1 
ATOM   976  C  CD  . GLU A 1 133 ? 85.304  231.626 -0.696  1.00 45.18  ? 133 GLU A CD  1 
ATOM   977  O  OE1 . GLU A 1 133 ? 84.098  231.849 -0.960  1.00 45.54  ? 133 GLU A OE1 1 
ATOM   978  O  OE2 . GLU A 1 133 ? 85.727  230.497 -0.344  1.00 58.11  1 133 GLU A OE2 1 
ATOM   979  N  N   . SER A 1 134 ? 86.536  235.737 2.113   1.00 26.17  ? 134 SER A N   1 
ATOM   980  C  CA  . SER A 1 134 ? 87.486  236.058 3.140   1.00 29.40  ? 134 SER A CA  1 
ATOM   981  C  C   . SER A 1 134 ? 87.095  235.427 4.477   1.00 35.16  ? 134 SER A C   1 
ATOM   982  O  O   . SER A 1 134 ? 87.941  234.920 5.190   1.00 36.01  ? 134 SER A O   1 
ATOM   983  C  CB  . SER A 1 134 ? 87.578  237.575 3.285   1.00 37.33  ? 134 SER A CB  1 
ATOM   984  O  OG  . SER A 1 134 ? 88.380  237.909 4.390   1.00 39.24  ? 134 SER A OG  1 
ATOM   985  N  N   . THR A 1 135 ? 85.804  235.437 4.788   1.00 31.03  ? 135 THR A N   1 
ATOM   986  C  CA  . THR A 1 135 ? 85.318  234.939 6.054   1.00 29.73  ? 135 THR A CA  1 
ATOM   987  C  C   . THR A 1 135 ? 85.122  233.436 6.020   1.00 36.84  ? 135 THR A C   1 
ATOM   988  O  O   . THR A 1 135 ? 84.599  232.857 6.964   1.00 34.45  ? 135 THR A O   1 
ATOM   989  C  CB  . THR A 1 135 ? 83.985  235.619 6.465   1.00 33.47  ? 135 THR A CB  1 
ATOM   990  O  OG1 . THR A 1 135 ? 82.865  234.999 5.813   1.00 32.78  ? 135 THR A OG1 1 
ATOM   991  C  CG2 . THR A 1 135 ? 84.026  237.117 6.166   1.00 32.33  ? 135 THR A CG2 1 
ATOM   992  N  N   . LYS A 1 136 ? 85.462  232.812 4.899   1.00 34.03  ? 136 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 136 ? 85.375  231.353 4.788   1.00 36.69  ? 136 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 136 ? 86.775  230.711 4.681   1.00 34.18  ? 136 LYS A C   1 
ATOM   995  O  O   . LYS A 1 136 ? 87.054  229.725 5.363   1.00 36.66  ? 136 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 136 ? 84.476  230.964 3.594   1.00 35.07  ? 136 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 136 ? 82.990  231.124 3.903   1.00 37.13  ? 136 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 136 ? 82.117  231.366 2.674   1.00 48.63  ? 136 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 136 ? 82.317  230.366 1.569   1.00 49.12  ? 136 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 136 ? 81.071  230.336 0.737   1.00 67.98  1 136 LYS A NZ  1 
ATOM   1001 N  N   . THR A 1 137 ? 87.650  231.253 3.833   1.00 25.52  ? 137 THR A N   1 
ATOM   1002 C  CA  . THR A 1 137 ? 88.967  230.631 3.615   1.00 29.84  ? 137 THR A CA  1 
ATOM   1003 C  C   . THR A 1 137 ? 90.142  231.598 3.694   1.00 30.04  ? 137 THR A C   1 
ATOM   1004 O  O   . THR A 1 137 ? 91.304  231.196 3.610   1.00 31.18  ? 137 THR A O   1 
ATOM   1005 C  CB  . THR A 1 137 ? 89.065  229.958 2.231   1.00 29.58  ? 137 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 137 ? 89.294  230.965 1.233   1.00 38.98  ? 137 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 137 ? 87.818  229.165 1.909   1.00 23.63  ? 137 THR A CG2 1 
ATOM   1008 N  N   . GLY A 1 138 ? 89.855  232.883 3.815   1.00 26.95  ? 138 GLY A N   1 
ATOM   1009 C  CA  . GLY A 1 138 ? 90.937  233.849 3.826   1.00 27.67  ? 138 GLY A CA  1 
ATOM   1010 C  C   . GLY A 1 138 ? 91.638  234.089 2.480   1.00 36.73  ? 138 GLY A C   1 
ATOM   1011 O  O   . GLY A 1 138 ? 92.643  234.814 2.447   1.00 31.48  ? 138 GLY A O   1 
ATOM   1012 N  N   . ASN A 1 139 ? 91.103  233.536 1.381   1.00 27.77  ? 139 ASN A N   1 
ATOM   1013 C  CA  . ASN A 1 139 ? 91.589  233.891 0.028   1.00 35.72  ? 139 ASN A CA  1 
ATOM   1014 C  C   . ASN A 1 139 ? 93.046  233.626 -0.233  1.00 30.52  ? 139 ASN A C   1 
ATOM   1015 O  O   . ASN A 1 139 ? 93.747  234.513 -0.707  1.00 34.28  ? 139 ASN A O   1 
ATOM   1016 C  CB  . ASN A 1 139 ? 91.345  235.377 -0.248  1.00 37.18  ? 139 ASN A CB  1 
ATOM   1017 C  CG  . ASN A 1 139 ? 89.882  235.698 -0.419  1.00 36.26  ? 139 ASN A CG  1 
ATOM   1018 O  OD1 . ASN A 1 139 ? 89.182  235.055 -1.201  1.00 33.71  ? 139 ASN A OD1 1 
ATOM   1019 N  ND2 . ASN A 1 139 ? 89.396  236.651 0.365   1.00 35.87  ? 139 ASN A ND2 1 
ATOM   1020 N  N   . ALA A 1 140 ? 93.539  232.474 0.179   1.00 32.73  ? 140 ALA A N   1 
ATOM   1021 C  CA  . ALA A 1 140 ? 94.972  232.215 0.102   1.00 31.86  ? 140 ALA A CA  1 
ATOM   1022 C  C   . ALA A 1 140 ? 95.429  231.659 -1.254  1.00 33.45  ? 140 ALA A C   1 
ATOM   1023 O  O   . ALA A 1 140 ? 96.598  231.307 -1.423  1.00 31.50  ? 140 ALA A O   1 
ATOM   1024 C  CB  . ALA A 1 140 ? 95.373  231.290 1.212   1.00 32.53  ? 140 ALA A CB  1 
ATOM   1025 N  N   . GLY A 1 141 ? 94.502  231.571 -2.206  1.00 29.57  ? 141 GLY A N   1 
ATOM   1026 C  CA  . GLY A 1 141 ? 94.822  231.099 -3.544  1.00 36.57  ? 141 GLY A CA  1 
ATOM   1027 C  C   . GLY A 1 141 ? 94.991  229.596 -3.568  1.00 37.72  ? 141 GLY A C   1 
ATOM   1028 O  O   . GLY A 1 141 ? 94.379  228.900 -2.762  1.00 32.10  ? 141 GLY A O   1 
ATOM   1029 N  N   . SER A 1 142 ? 95.819  229.090 -4.482  1.00 35.35  ? 142 SER A N   1 
ATOM   1030 C  CA  . SER A 1 142 ? 95.908  227.639 -4.683  1.00 37.53  ? 142 SER A CA  1 
ATOM   1031 C  C   . SER A 1 142 ? 96.822  226.977 -3.638  1.00 31.58  ? 142 SER A C   1 
ATOM   1032 O  O   . SER A 1 142 ? 97.642  227.638 -2.990  1.00 31.82  ? 142 SER A O   1 
ATOM   1033 C  CB  . SER A 1 142 ? 96.416  227.292 -6.091  1.00 33.48  ? 142 SER A CB  1 
ATOM   1034 O  OG  . SER A 1 142 ? 97.722  227.798 -6.248  1.00 43.16  ? 142 SER A OG  1 
ATOM   1035 N  N   . ARG A 1 143 ? 96.606  225.676 -3.456  1.00 35.80  ? 143 ARG A N   1 
ATOM   1036 C  CA  . ARG A 1 143 ? 97.399  224.817 -2.580  1.00 34.43  ? 143 ARG A CA  1 
ATOM   1037 C  C   . ARG A 1 143 ? 98.739  224.493 -3.222  1.00 37.64  ? 143 ARG A C   1 
ATOM   1038 O  O   . ARG A 1 143 ? 98.781  224.009 -4.333  1.00 43.36  ? 143 ARG A O   1 
ATOM   1039 C  CB  . ARG A 1 143 ? 96.665  223.502 -2.293  1.00 30.11  ? 143 ARG A CB  1 
ATOM   1040 C  CG  . ARG A 1 143 ? 95.270  223.628 -1.722  1.00 49.80  ? 143 ARG A CG  1 
ATOM   1041 C  CD  . ARG A 1 143 ? 94.590  222.274 -1.776  1.00 56.74  ? 143 ARG A CD  1 
ATOM   1042 N  NE  . ARG A 1 143 ? 93.707  222.037 -0.625  1.00 77.92  ? 143 ARG A NE  1 
ATOM   1043 C  CZ  . ARG A 1 143 ? 92.758  222.859 -0.161  1.00 73.69  ? 143 ARG A CZ  1 
ATOM   1044 N  NH1 . ARG A 1 143 ? 92.484  224.027 -0.755  1.00 53.56  1 143 ARG A NH1 1 
ATOM   1045 N  NH2 . ARG A 1 143 ? 92.057  222.483 0.910   1.00 57.10  ? 143 ARG A NH2 1 
ATOM   1046 N  N   . LEU A 1 144 ? 99.835  224.757 -2.533  1.00 38.67  ? 144 LEU A N   1 
ATOM   1047 C  CA  . LEU A 1 144 ? 101.138 224.372 -3.047  1.00 35.92  ? 144 LEU A CA  1 
ATOM   1048 C  C   . LEU A 1 144 ? 101.546 222.991 -2.527  1.00 40.75  ? 144 LEU A C   1 
ATOM   1049 O  O   . LEU A 1 144 ? 102.126 222.203 -3.267  1.00 37.79  ? 144 LEU A O   1 
ATOM   1050 C  CB  . LEU A 1 144 ? 102.177 225.423 -2.661  1.00 35.38  ? 144 LEU A CB  1 
ATOM   1051 C  CG  . LEU A 1 144 ? 101.982 226.800 -3.300  1.00 37.47  ? 144 LEU A CG  1 
ATOM   1052 C  CD1 . LEU A 1 144 ? 103.103 227.711 -2.923  1.00 35.55  ? 144 LEU A CD1 1 
ATOM   1053 C  CD2 . LEU A 1 144 ? 101.924 226.666 -4.803  1.00 32.95  ? 144 LEU A CD2 1 
ATOM   1054 N  N   . ALA A 1 145 ? 101.241 222.696 -1.256  1.00 39.92  ? 145 ALA A N   1 
ATOM   1055 C  CA  . ALA A 1 145 ? 101.642 221.422 -0.658  1.00 41.38  ? 145 ALA A CA  1 
ATOM   1056 C  C   . ALA A 1 145 ? 100.787 221.048 0.530   1.00 41.31  ? 145 ALA A C   1 
ATOM   1057 O  O   . ALA A 1 145 ? 100.254 221.898 1.252   1.00 37.54  ? 145 ALA A O   1 
ATOM   1058 C  CB  . ALA A 1 145 ? 103.139 221.441 -0.246  1.00 31.82  ? 145 ALA A CB  1 
ATOM   1059 N  N   . CYS A 1 146 ? 100.661 219.752 0.734   1.00 38.33  ? 146 CYS A N   1 
ATOM   1060 C  CA  . CYS A 1 146 ? 99.870  219.268 1.839   1.00 30.97  ? 146 CYS A CA  1 
ATOM   1061 C  C   . CYS A 1 146 ? 100.379 217.921 2.349   1.00 35.77  ? 146 CYS A C   1 
ATOM   1062 O  O   . CYS A 1 146 ? 101.135 217.237 1.677   1.00 30.60  ? 146 CYS A O   1 
ATOM   1063 C  CB  . CYS A 1 146 ? 98.408  219.159 1.417   1.00 34.46  ? 146 CYS A CB  1 
ATOM   1064 S  SG  . CYS A 1 146 ? 98.054  217.775 0.301   1.00 43.52  ? 146 CYS A SG  1 
ATOM   1065 N  N   . GLY A 1 147 ? 99.937  217.560 3.547   1.00 34.04  ? 147 GLY A N   1 
ATOM   1066 C  CA  . GLY A 1 147 ? 100.214 216.267 4.118   1.00 29.49  ? 147 GLY A CA  1 
ATOM   1067 C  C   . GLY A 1 147 ? 99.232  215.974 5.219   1.00 30.23  ? 147 GLY A C   1 
ATOM   1068 O  O   . GLY A 1 147 ? 98.562  216.878 5.733   1.00 33.16  ? 147 GLY A O   1 
ATOM   1069 N  N   . VAL A 1 148 ? 99.150  214.702 5.582   1.00 26.45  ? 148 VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 148 ? 98.308  214.286 6.685   1.00 30.32  ? 148 VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 148 ? 99.106  214.353 8.001   1.00 33.06  ? 148 VAL A C   1 
ATOM   1072 O  O   . VAL A 1 148 ? 100.234 213.875 8.071   1.00 37.38  ? 148 VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 148 ? 97.780  212.853 6.477   1.00 31.70  ? 148 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 148 ? 96.787  212.506 7.551   1.00 29.30  ? 148 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 148 ? 97.189  212.675 5.063   1.00 29.90  ? 148 VAL A CG2 1 
ATOM   1076 N  N   . ILE A 1 149 ? 98.527  214.952 9.034   1.00 33.76  ? 149 ILE A N   1 
ATOM   1077 C  CA  . ILE A 1 149 ? 99.171  215.007 10.347  1.00 25.63  ? 149 ILE A CA  1 
ATOM   1078 C  C   . ILE A 1 149 ? 99.054  213.618 11.005  1.00 33.64  ? 149 ILE A C   1 
ATOM   1079 O  O   . ILE A 1 149 ? 97.957  213.123 11.234  1.00 29.46  ? 149 ILE A O   1 
ATOM   1080 C  CB  . ILE A 1 149 ? 98.531  216.092 11.236  1.00 24.87  ? 149 ILE A CB  1 
ATOM   1081 C  CG1 . ILE A 1 149 ? 98.668  217.457 10.568  1.00 28.26  ? 149 ILE A CG1 1 
ATOM   1082 C  CG2 . ILE A 1 149 ? 99.190  216.143 12.622  1.00 25.92  ? 149 ILE A CG2 1 
ATOM   1083 C  CD1 . ILE A 1 149 ? 97.891  218.548 11.239  1.00 26.56  ? 149 ILE A CD1 1 
ATOM   1084 N  N   . GLY A 1 150 ? 100.186 212.988 11.289  1.00 29.40  ? 150 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 150 ? 100.178 211.677 11.894  1.00 33.86  ? 150 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 150 ? 100.823 211.677 13.275  1.00 36.07  ? 150 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 150 ? 101.516 212.628 13.661  1.00 32.85  ? 150 GLY A O   1 
ATOM   1088 N  N   . ILE A 1 151 ? 100.586 210.601 14.020  1.00 42.22  ? 151 ILE A N   1 
ATOM   1089 C  CA  . ILE A 1 151 ? 101.176 210.410 15.349  1.00 39.35  ? 151 ILE A CA  1 
ATOM   1090 C  C   . ILE A 1 151 ? 102.692 210.231 15.280  1.00 38.79  ? 151 ILE A C   1 
ATOM   1091 O  O   . ILE A 1 151 ? 103.182 209.408 14.519  1.00 38.39  ? 151 ILE A O   1 
ATOM   1092 C  CB  . ILE A 1 151 ? 100.548 209.194 16.050  1.00 38.41  ? 151 ILE A CB  1 
ATOM   1093 C  CG1 . ILE A 1 151 ? 99.030  209.375 16.128  1.00 37.47  ? 151 ILE A CG1 1 
ATOM   1094 C  CG2 . ILE A 1 151 ? 101.146 209.011 17.447  1.00 40.72  ? 151 ILE A CG2 1 
ATOM   1095 C  CD1 . ILE A 1 151 ? 98.264  208.118 16.397  1.00 44.01  ? 151 ILE A CD1 1 
ATOM   1096 N  N   . ALA A 1 152 ? 103.425 211.027 16.060  1.00 38.60  ? 152 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 152 ? 104.881 210.923 16.135  1.00 47.21  ? 152 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 152 ? 105.348 210.355 17.472  1.00 57.29  ? 152 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 152 ? 106.481 209.895 17.560  1.00 58.99  ? 152 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 152 ? 105.528 212.280 15.905  1.00 41.29  ? 152 ALA A CB  1 
ATOM   1101 N  N   . GLN A 1 153 ? 104.444 210.359 18.464  1.00 49.73  ? 153 GLN A N   1 
ATOM   1102 C  CA  . GLN A 1 153 ? 104.627 209.869 19.858  1.00 75.85  ? 153 GLN A CA  1 
ATOM   1103 C  C   . GLN A 1 153 ? 103.453 210.278 20.770  1.00 78.89  ? 153 GLN A C   1 
ATOM   1104 O  O   . GLN A 1 153 ? 102.422 210.835 20.373  1.00 67.32  ? 153 GLN A O   1 
ATOM   1105 C  CB  . GLN A 1 153 ? 105.901 210.397 20.562  1.00 89.03  ? 153 GLN A CB  1 
ATOM   1106 C  CG  . GLN A 1 153 ? 107.243 209.690 20.329  1.00 99.25  ? 153 GLN A CG  1 
ATOM   1107 C  CD  . GLN A 1 153 ? 108.432 210.547 20.787  1.00 106.42 ? 153 GLN A CD  1 
ATOM   1108 O  OE1 . GLN A 1 153 ? 108.262 211.699 21.208  1.00 109.52 ? 153 GLN A OE1 1 
ATOM   1109 N  NE2 . GLN A 1 153 ? 109.638 209.991 20.693  1.00 111.26 ? 153 GLN A NE2 1 
ATOM   1110 O  OXT . GLN A 1 153 ? 103.521 210.053 21.984  1.00 88.17  1 153 GLN A OXT 1 
ATOM   1111 N  N   . GLU B 2 7   ? 76.204  196.524 10.068  1.00 91.75  ? 8   GLU B N   1 
ATOM   1112 C  CA  . GLU B 2 7   ? 75.591  197.452 9.119   1.00 87.16  ? 8   GLU B CA  1 
ATOM   1113 C  C   . GLU B 2 7   ? 76.623  198.207 8.294   1.00 86.96  ? 8   GLU B C   1 
ATOM   1114 O  O   . GLU B 2 7   ? 77.552  198.799 8.836   1.00 86.55  ? 8   GLU B O   1 
ATOM   1115 C  CB  . GLU B 2 7   ? 74.688  198.460 9.839   1.00 94.29  ? 8   GLU B CB  1 
ATOM   1116 C  CG  . GLU B 2 7   ? 74.213  199.605 8.925   1.00 103.08 ? 8   GLU B CG  1 
ATOM   1117 C  CD  . GLU B 2 7   ? 73.333  200.647 9.619   1.00 110.58 ? 8   GLU B CD  1 
ATOM   1118 O  OE1 . GLU B 2 7   ? 72.709  200.329 10.657  1.00 113.76 ? 8   GLU B OE1 1 
ATOM   1119 O  OE2 . GLU B 2 7   ? 73.269  201.792 9.116   1.00 103.59 1 8   GLU B OE2 1 
ATOM   1120 N  N   . ALA B 2 8   ? 76.443  198.182 6.976   1.00 93.03  ? 9   ALA B N   1 
ATOM   1121 C  CA  . ALA B 2 8   ? 77.337  198.856 6.041   1.00 79.04  ? 9   ALA B CA  1 
ATOM   1122 C  C   . ALA B 2 8   ? 76.546  199.674 5.013   1.00 76.35  ? 9   ALA B C   1 
ATOM   1123 O  O   . ALA B 2 8   ? 75.376  199.394 4.762   1.00 85.42  ? 9   ALA B O   1 
ATOM   1124 C  CB  . ALA B 2 8   ? 78.220  197.832 5.343   1.00 75.52  ? 9   ALA B CB  1 
ATOM   1125 N  N   . THR B 2 9   ? 77.180  200.679 4.415   1.00 63.62  ? 10  THR B N   1 
ATOM   1126 C  CA  . THR B 2 9   ? 76.530  201.479 3.377   1.00 68.95  ? 10  THR B CA  1 
ATOM   1127 C  C   . THR B 2 9   ? 77.241  201.301 2.036   1.00 66.62  ? 10  THR B C   1 
ATOM   1128 O  O   . THR B 2 9   ? 78.465  201.358 1.974   1.00 71.31  ? 10  THR B O   1 
ATOM   1129 C  CB  . THR B 2 9   ? 76.492  202.971 3.764   1.00 57.11  ? 10  THR B CB  1 
ATOM   1130 O  OG1 . THR B 2 9   ? 75.544  203.159 4.820   1.00 79.30  ? 10  THR B OG1 1 
ATOM   1131 C  CG2 . THR B 2 9   ? 76.106  203.841 2.577   1.00 55.93  ? 10  THR B CG2 1 
ATOM   1132 N  N   . TYR B 2 10  ? 76.478  201.064 0.970   1.00 68.79  ? 11  TYR B N   1 
ATOM   1133 C  CA  . TYR B 2 10  ? 77.055  200.839 -0.354  1.00 63.36  ? 11  TYR B CA  1 
ATOM   1134 C  C   . TYR B 2 10  ? 76.616  201.919 -1.339  1.00 66.30  ? 11  TYR B C   1 
ATOM   1135 O  O   . TYR B 2 10  ? 75.484  202.388 -1.281  1.00 77.47  ? 11  TYR B O   1 
ATOM   1136 C  CB  . TYR B 2 10  ? 76.657  199.463 -0.876  1.00 63.29  ? 11  TYR B CB  1 
ATOM   1137 C  CG  . TYR B 2 10  ? 77.085  198.309 0.007   1.00 65.11  ? 11  TYR B CG  1 
ATOM   1138 C  CD1 . TYR B 2 10  ? 76.362  197.972 1.149   1.00 72.48  ? 11  TYR B CD1 1 
ATOM   1139 C  CD2 . TYR B 2 10  ? 78.200  197.548 -0.307  1.00 67.99  ? 11  TYR B CD2 1 
ATOM   1140 C  CE1 . TYR B 2 10  ? 76.745  196.911 1.955   1.00 74.44  ? 11  TYR B CE1 1 
ATOM   1141 C  CE2 . TYR B 2 10  ? 78.592  196.488 0.494   1.00 78.25  ? 11  TYR B CE2 1 
ATOM   1142 C  CZ  . TYR B 2 10  ? 77.863  196.175 1.621   1.00 74.40  ? 11  TYR B CZ  1 
ATOM   1143 O  OH  . TYR B 2 10  ? 78.255  195.125 2.414   1.00 80.07  ? 11  TYR B OH  1 
ATOM   1144 N  N   . ALA B 2 11  ? 77.512  202.309 -2.240  1.00 65.20  ? 12  ALA B N   1 
ATOM   1145 C  CA  . ALA B 2 11  ? 77.205  203.279 -3.300  1.00 69.13  ? 12  ALA B CA  1 
ATOM   1146 C  C   . ALA B 2 11  ? 76.897  202.616 -4.646  1.00 83.03  ? 12  ALA B C   1 
ATOM   1147 O  O   . ALA B 2 11  ? 77.582  201.666 -5.040  1.00 77.12  ? 12  ALA B O   1 
ATOM   1148 C  CB  . ALA B 2 11  ? 78.349  204.259 -3.470  1.00 60.30  ? 12  ALA B CB  1 
ATOM   1149 N  N   . ILE B 2 12  ? 75.862  203.108 -5.336  1.00 92.70  ? 13  ILE B N   1 
ATOM   1150 C  CA  . ILE B 2 12  ? 75.492  202.594 -6.660  1.00 98.18  ? 13  ILE B CA  1 
ATOM   1151 C  C   . ILE B 2 12  ? 75.401  203.748 -7.670  1.00 91.33  ? 13  ILE B C   1 
ATOM   1152 O  O   . ILE B 2 12  ? 74.421  203.893 -8.406  1.00 95.89  ? 13  ILE B O   1 
ATOM   1153 C  CB  . ILE B 2 12  ? 74.142  201.835 -6.642  1.00 92.09  ? 13  ILE B CB  1 
ATOM   1154 C  CG1 . ILE B 2 12  ? 73.957  201.050 -5.337  1.00 85.37  ? 13  ILE B CG1 1 
ATOM   1155 C  CG2 . ILE B 2 12  ? 74.025  200.931 -7.872  1.00 91.68  ? 13  ILE B CG2 1 
ATOM   1156 C  CD1 . ILE B 2 12  ? 74.713  199.741 -5.283  1.00 81.40  ? 13  ILE B CD1 1 
ATOM   1157 N  N   . CYS B 2 16  ? 67.790  206.641 -11.548 1.00 122.86 ? 17  CYS B N   1 
ATOM   1158 C  CA  . CYS B 2 16  ? 66.368  206.976 -11.534 1.00 119.56 ? 17  CYS B CA  1 
ATOM   1159 C  C   . CYS B 2 16  ? 65.574  206.015 -10.648 1.00 124.39 ? 17  CYS B C   1 
ATOM   1160 O  O   . CYS B 2 16  ? 66.131  205.344 -9.777  1.00 125.23 ? 17  CYS B O   1 
ATOM   1161 C  CB  . CYS B 2 16  ? 65.783  206.939 -12.944 1.00 122.11 ? 17  CYS B CB  1 
ATOM   1162 S  SG  . CYS B 2 16  ? 65.600  205.254 -13.555 1.00 133.26 ? 17  CYS B SG  1 
ATOM   1163 N  N   . GLU B 2 17  ? 64.262  205.974 -10.869 1.00 121.73 ? 18  GLU B N   1 
ATOM   1164 C  CA  . GLU B 2 17  ? 63.378  205.114 -10.090 1.00 120.54 ? 18  GLU B CA  1 
ATOM   1165 C  C   . GLU B 2 17  ? 63.308  203.672 -10.597 1.00 118.42 ? 18  GLU B C   1 
ATOM   1166 O  O   . GLU B 2 17  ? 62.980  202.754 -9.840  1.00 111.67 ? 18  GLU B O   1 
ATOM   1167 C  CB  . GLU B 2 17  ? 61.967  205.706 -10.067 1.00 115.05 ? 18  GLU B CB  1 
ATOM   1168 C  CG  . GLU B 2 17  ? 61.705  206.595 -8.883  1.00 109.64 ? 18  GLU B CG  1 
ATOM   1169 C  CD  . GLU B 2 17  ? 61.873  205.850 -7.573  1.00 125.98 ? 18  GLU B CD  1 
ATOM   1170 O  OE1 . GLU B 2 17  ? 61.699  204.609 -7.557  1.00 116.50 ? 18  GLU B OE1 1 
ATOM   1171 O  OE2 . GLU B 2 17  ? 62.172  206.507 -6.554  1.00 127.30 1 18  GLU B OE2 1 
ATOM   1172 N  N   . ASN B 2 18  ? 63.612  203.481 -11.878 1.00 116.94 ? 19  ASN B N   1 
ATOM   1173 C  CA  . ASN B 2 18  ? 63.650  202.146 -12.477 1.00 124.71 ? 19  ASN B CA  1 
ATOM   1174 C  C   . ASN B 2 18  ? 64.953  201.433 -12.109 1.00 126.10 ? 19  ASN B C   1 
ATOM   1175 O  O   . ASN B 2 18  ? 65.038  200.205 -12.122 1.00 125.74 ? 19  ASN B O   1 
ATOM   1176 C  CB  . ASN B 2 18  ? 63.469  202.230 -14.000 1.00 132.63 ? 19  ASN B CB  1 
ATOM   1177 C  CG  . ASN B 2 18  ? 63.034  200.900 -14.629 1.00 128.39 ? 19  ASN B CG  1 
ATOM   1178 O  OD1 . ASN B 2 18  ? 63.247  199.818 -14.071 1.00 136.00 ? 19  ASN B OD1 1 
ATOM   1179 N  ND2 . ASN B 2 18  ? 62.395  200.989 -15.792 1.00 105.67 ? 19  ASN B ND2 1 
ATOM   1180 N  N   . CYS B 2 19  ? 65.969  202.225 -11.782 1.00 129.34 ? 20  CYS B N   1 
ATOM   1181 C  CA  . CYS B 2 19  ? 67.261  201.698 -11.358 1.00 129.14 ? 20  CYS B CA  1 
ATOM   1182 C  C   . CYS B 2 19  ? 67.127  200.987 -10.016 1.00 126.73 ? 20  CYS B C   1 
ATOM   1183 O  O   . CYS B 2 19  ? 67.837  200.022 -9.741  1.00 127.32 ? 20  CYS B O   1 
ATOM   1184 C  CB  . CYS B 2 19  ? 68.300  202.819 -11.256 1.00 126.30 ? 20  CYS B CB  1 
ATOM   1185 S  SG  . CYS B 2 19  ? 68.837  203.491 -12.840 1.00 141.55 ? 20  CYS B SG  1 
ATOM   1186 N  N   . VAL B 2 20  ? 66.220  201.493 -9.186  1.00 128.00 ? 21  VAL B N   1 
ATOM   1187 C  CA  . VAL B 2 20  ? 66.048  201.055 -7.800  1.00 127.87 ? 21  VAL B CA  1 
ATOM   1188 C  C   . VAL B 2 20  ? 65.701  199.573 -7.631  1.00 127.96 ? 21  VAL B C   1 
ATOM   1189 O  O   . VAL B 2 20  ? 66.351  198.856 -6.867  1.00 120.38 ? 21  VAL B O   1 
ATOM   1190 C  CB  . VAL B 2 20  ? 64.944  201.864 -7.108  1.00 127.79 ? 21  VAL B CB  1 
ATOM   1191 C  CG1 . VAL B 2 20  ? 65.005  201.644 -5.606  1.00 114.23 ? 21  VAL B CG1 1 
ATOM   1192 C  CG2 . VAL B 2 20  ? 65.092  203.331 -7.439  1.00 125.50 ? 21  VAL B CG2 1 
ATOM   1193 N  N   . ASN B 2 21  ? 64.658  199.128 -8.330  1.00 137.60 ? 22  ASN B N   1 
ATOM   1194 C  CA  . ASN B 2 21  ? 64.190  197.749 -8.213  1.00 131.98 ? 22  ASN B CA  1 
ATOM   1195 C  C   . ASN B 2 21  ? 65.046  196.784 -9.028  1.00 129.63 ? 22  ASN B C   1 
ATOM   1196 O  O   . ASN B 2 21  ? 65.002  195.573 -8.816  1.00 124.89 ? 22  ASN B O   1 
ATOM   1197 C  CB  . ASN B 2 21  ? 62.725  197.649 -8.664  1.00 126.18 ? 22  ASN B CB  1 
ATOM   1198 C  CG  . ASN B 2 21  ? 62.468  198.349 -9.998  1.00 129.68 ? 22  ASN B CG  1 
ATOM   1199 O  OD1 . ASN B 2 21  ? 63.349  198.427 -10.855 1.00 133.08 ? 22  ASN B OD1 1 
ATOM   1200 N  ND2 . ASN B 2 21  ? 61.255  198.859 -10.173 1.00 124.14 ? 22  ASN B ND2 1 
ATOM   1201 N  N   . ASP B 2 22  ? 65.821  197.340 -9.956  1.00 132.47 ? 23  ASP B N   1 
ATOM   1202 C  CA  . ASP B 2 22  ? 66.820  196.600 -10.725 1.00 135.87 ? 23  ASP B CA  1 
ATOM   1203 C  C   . ASP B 2 22  ? 67.863  195.962 -9.789  1.00 133.27 ? 23  ASP B C   1 
ATOM   1204 O  O   . ASP B 2 22  ? 68.281  194.811 -9.980  1.00 123.07 ? 23  ASP B O   1 
ATOM   1205 C  CB  . ASP B 2 22  ? 67.477  197.561 -11.739 1.00 133.42 ? 23  ASP B CB  1 
ATOM   1206 C  CG  . ASP B 2 22  ? 68.390  196.862 -12.739 1.00 138.26 ? 23  ASP B CG  1 
ATOM   1207 O  OD1 . ASP B 2 22  ? 68.382  195.614 -12.815 1.00 144.49 ? 23  ASP B OD1 1 
ATOM   1208 O  OD2 . ASP B 2 22  ? 69.113  197.580 -13.466 1.00 128.91 1 23  ASP B OD2 1 
ATOM   1209 N  N   . ILE B 2 23  ? 68.247  196.725 -8.765  1.00 136.00 ? 24  ILE B N   1 
ATOM   1210 C  CA  . ILE B 2 23  ? 69.257  196.322 -7.780  1.00 133.04 ? 24  ILE B CA  1 
ATOM   1211 C  C   . ILE B 2 23  ? 68.717  195.458 -6.637  1.00 123.66 ? 24  ILE B C   1 
ATOM   1212 O  O   . ILE B 2 23  ? 69.320  194.436 -6.292  1.00 110.27 ? 24  ILE B O   1 
ATOM   1213 C  CB  . ILE B 2 23  ? 69.951  197.558 -7.173  1.00 123.77 ? 24  ILE B CB  1 
ATOM   1214 C  CG1 . ILE B 2 23  ? 70.463  198.468 -8.296  1.00 122.89 ? 24  ILE B CG1 1 
ATOM   1215 C  CG2 . ILE B 2 23  ? 71.095  197.127 -6.274  1.00 107.54 ? 24  ILE B CG2 1 
ATOM   1216 C  CD1 . ILE B 2 23  ? 70.632  199.918 -7.898  1.00 113.24 ? 24  ILE B CD1 1 
ATOM   1217 N  N   . LYS B 2 24  ? 67.600  195.880 -6.041  1.00 125.61 ? 25  LYS B N   1 
ATOM   1218 C  CA  . LYS B 2 24  ? 66.978  195.102 -4.975  1.00 122.22 ? 25  LYS B CA  1 
ATOM   1219 C  C   . LYS B 2 24  ? 66.666  193.707 -5.466  1.00 122.37 ? 25  LYS B C   1 
ATOM   1220 O  O   . LYS B 2 24  ? 66.796  192.738 -4.721  1.00 119.95 ? 25  LYS B O   1 
ATOM   1221 C  CB  . LYS B 2 24  ? 65.700  195.756 -4.459  1.00 114.22 ? 25  LYS B CB  1 
ATOM   1222 C  CG  . LYS B 2 24  ? 65.319  195.232 -3.084  1.00 110.60 ? 25  LYS B CG  1 
ATOM   1223 C  CD  . LYS B 2 24  ? 64.128  195.953 -2.490  1.00 113.71 ? 25  LYS B CD  1 
ATOM   1224 C  CE  . LYS B 2 24  ? 64.135  195.854 -0.967  1.00 108.25 ? 25  LYS B CE  1 
ATOM   1225 N  NZ  . LYS B 2 24  ? 64.135  194.441 -0.493  1.00 106.46 1 25  LYS B NZ  1 
ATOM   1226 N  N   . ALA B 2 25  ? 66.256  193.622 -6.728  1.00 118.74 ? 26  ALA B N   1 
ATOM   1227 C  CA  . ALA B 2 25  ? 66.072  192.347 -7.402  1.00 120.69 ? 26  ALA B CA  1 
ATOM   1228 C  C   . ALA B 2 25  ? 67.324  191.489 -7.314  1.00 118.40 ? 26  ALA B C   1 
ATOM   1229 O  O   . ALA B 2 25  ? 67.296  190.396 -6.748  1.00 117.24 ? 26  ALA B O   1 
ATOM   1230 C  CB  . ALA B 2 25  ? 65.696  192.568 -8.859  1.00 117.95 ? 26  ALA B CB  1 
ATOM   1231 N  N   . CYS B 2 26  ? 68.425  192.017 -7.841  1.00 112.22 ? 27  CYS B N   1 
ATOM   1232 C  CA  . CYS B 2 26  ? 69.669  191.267 -7.998  1.00 114.79 ? 27  CYS B CA  1 
ATOM   1233 C  C   . CYS B 2 26  ? 70.142  190.620 -6.691  1.00 114.91 ? 27  CYS B C   1 
ATOM   1234 O  O   . CYS B 2 26  ? 70.868  189.626 -6.702  1.00 114.54 ? 27  CYS B O   1 
ATOM   1235 C  CB  . CYS B 2 26  ? 70.762  192.180 -8.565  1.00 113.79 ? 27  CYS B CB  1 
ATOM   1236 S  SG  . CYS B 2 26  ? 72.184  191.309 -9.295  1.00 117.20 ? 27  CYS B SG  1 
ATOM   1237 N  N   . LEU B 2 27  ? 69.722  191.188 -5.568  1.00 117.26 ? 28  LEU B N   1 
ATOM   1238 C  CA  . LEU B 2 27  ? 70.222  190.781 -4.259  1.00 120.78 ? 28  LEU B CA  1 
ATOM   1239 C  C   . LEU B 2 27  ? 69.359  189.762 -3.519  1.00 120.71 ? 28  LEU B C   1 
ATOM   1240 O  O   . LEU B 2 27  ? 69.826  189.127 -2.574  1.00 117.89 ? 28  LEU B O   1 
ATOM   1241 C  CB  . LEU B 2 27  ? 70.372  192.013 -3.364  1.00 116.37 ? 28  LEU B CB  1 
ATOM   1242 C  CG  . LEU B 2 27  ? 71.400  193.065 -3.765  1.00 114.68 ? 28  LEU B CG  1 
ATOM   1243 C  CD1 . LEU B 2 27  ? 71.287  194.260 -2.831  1.00 111.49 ? 28  LEU B CD1 1 
ATOM   1244 C  CD2 . LEU B 2 27  ? 72.807  192.473 -3.746  1.00 100.89 ? 28  LEU B CD2 1 
ATOM   1245 N  N   . LYS B 2 28  ? 68.114  189.595 -3.946  1.00 120.11 ? 29  LYS B N   1 
ATOM   1246 C  CA  . LYS B 2 28  ? 67.112  188.979 -3.077  1.00 124.55 ? 29  LYS B CA  1 
ATOM   1247 C  C   . LYS B 2 28  ? 67.371  187.536 -2.617  1.00 121.72 ? 29  LYS B C   1 
ATOM   1248 O  O   . LYS B 2 28  ? 67.010  187.182 -1.495  1.00 113.91 ? 29  LYS B O   1 
ATOM   1249 C  CB  . LYS B 2 28  ? 65.748  189.030 -3.770  1.00 120.47 ? 29  LYS B CB  1 
ATOM   1250 C  CG  . LYS B 2 28  ? 65.127  190.417 -3.805  1.00 119.86 ? 29  LYS B CG  1 
ATOM   1251 C  CD  . LYS B 2 28  ? 65.272  191.142 -2.473  1.00 115.25 ? 29  LYS B CD  1 
ATOM   1252 C  CE  . LYS B 2 28  ? 64.432  190.493 -1.385  1.00 112.07 ? 29  LYS B CE  1 
ATOM   1253 N  NZ  . LYS B 2 28  ? 64.655  191.153 -0.074  1.00 106.15 1 29  LYS B NZ  1 
ATOM   1254 N  N   . ASN B 2 29  ? 68.005  186.711 -3.448  1.00 124.58 ? 30  ASN B N   1 
ATOM   1255 C  CA  . ASN B 2 29  ? 68.179  185.297 -3.095  1.00 123.22 ? 30  ASN B CA  1 
ATOM   1256 C  C   . ASN B 2 29  ? 69.341  185.079 -2.123  1.00 126.22 ? 30  ASN B C   1 
ATOM   1257 O  O   . ASN B 2 29  ? 69.642  183.943 -1.735  1.00 118.59 ? 30  ASN B O   1 
ATOM   1258 C  CB  . ASN B 2 29  ? 68.369  184.429 -4.354  1.00 119.46 ? 30  ASN B CB  1 
ATOM   1259 C  CG  . ASN B 2 29  ? 69.595  184.818 -5.170  1.00 114.39 ? 30  ASN B CG  1 
ATOM   1260 O  OD1 . ASN B 2 29  ? 69.945  185.997 -5.276  1.00 119.54 ? 30  ASN B OD1 1 
ATOM   1261 N  ND2 . ASN B 2 29  ? 70.249  183.818 -5.763  1.00 92.66  ? 30  ASN B ND2 1 
ATOM   1262 N  N   . VAL B 2 30  ? 69.985  186.173 -1.721  1.00 129.31 ? 31  VAL B N   1 
ATOM   1263 C  CA  . VAL B 2 30  ? 71.153  186.087 -0.854  1.00 121.36 ? 31  VAL B CA  1 
ATOM   1264 C  C   . VAL B 2 30  ? 70.732  186.168 0.617   1.00 116.10 ? 31  VAL B C   1 
ATOM   1265 O  O   . VAL B 2 30  ? 70.077  187.126 1.036   1.00 112.70 ? 31  VAL B O   1 
ATOM   1266 C  CB  . VAL B 2 30  ? 72.172  187.201 -1.180  1.00 116.98 ? 31  VAL B CB  1 
ATOM   1267 C  CG1 . VAL B 2 30  ? 73.448  187.015 -0.369  1.00 110.52 ? 31  VAL B CG1 1 
ATOM   1268 C  CG2 . VAL B 2 30  ? 72.476  187.220 -2.675  1.00 108.50 ? 31  VAL B CG2 1 
ATOM   1269 N  N   . PRO B 2 31  ? 71.129  185.157 1.401   1.00 112.42 ? 32  PRO B N   1 
ATOM   1270 C  CA  . PRO B 2 31  ? 70.864  184.983 2.835   1.00 111.39 ? 32  PRO B CA  1 
ATOM   1271 C  C   . PRO B 2 31  ? 71.802  185.777 3.737   1.00 110.67 ? 32  PRO B C   1 
ATOM   1272 O  O   . PRO B 2 31  ? 72.826  186.278 3.271   1.00 113.92 ? 32  PRO B O   1 
ATOM   1273 C  CB  . PRO B 2 31  ? 71.064  183.483 3.045   1.00 110.85 ? 32  PRO B CB  1 
ATOM   1274 C  CG  . PRO B 2 31  ? 72.039  183.085 2.001   1.00 110.89 ? 32  PRO B CG  1 
ATOM   1275 C  CD  . PRO B 2 31  ? 71.858  184.010 0.830   1.00 108.03 ? 32  PRO B CD  1 
ATOM   1276 N  N   . GLY B 2 32  ? 71.440  185.896 5.014   1.00 111.37 ? 33  GLY B N   1 
ATOM   1277 C  CA  . GLY B 2 32  ? 72.227  186.657 5.969   1.00 112.62 ? 33  GLY B CA  1 
ATOM   1278 C  C   . GLY B 2 32  ? 71.814  188.116 5.993   1.00 109.42 ? 33  GLY B C   1 
ATOM   1279 O  O   . GLY B 2 32  ? 72.204  188.874 6.881   1.00 104.70 ? 33  GLY B O   1 
ATOM   1280 N  N   . ILE B 2 33  ? 71.007  188.500 5.011   1.00 110.29 ? 34  ILE B N   1 
ATOM   1281 C  CA  . ILE B 2 33  ? 70.481  189.852 4.933   1.00 107.93 ? 34  ILE B CA  1 
ATOM   1282 C  C   . ILE B 2 33  ? 69.243  190.030 5.809   1.00 110.82 ? 34  ILE B C   1 
ATOM   1283 O  O   . ILE B 2 33  ? 68.241  189.331 5.642   1.00 108.13 ? 34  ILE B O   1 
ATOM   1284 C  CB  . ILE B 2 33  ? 70.124  190.224 3.479   1.00 109.77 ? 34  ILE B CB  1 
ATOM   1285 C  CG1 . ILE B 2 33  ? 71.373  190.165 2.591   1.00 107.63 ? 34  ILE B CG1 1 
ATOM   1286 C  CG2 . ILE B 2 33  ? 69.438  191.590 3.426   1.00 102.13 ? 34  ILE B CG2 1 
ATOM   1287 C  CD1 . ILE B 2 33  ? 71.122  190.540 1.146   1.00 104.47 ? 34  ILE B CD1 1 
ATOM   1288 N  N   . ASN B 2 34  ? 69.336  190.965 6.751   1.00 110.12 ? 35  ASN B N   1 
ATOM   1289 C  CA  . ASN B 2 34  ? 68.252  191.269 7.682   1.00 109.11 ? 35  ASN B CA  1 
ATOM   1290 C  C   . ASN B 2 34  ? 67.314  192.338 7.121   1.00 109.24 ? 35  ASN B C   1 
ATOM   1291 O  O   . ASN B 2 34  ? 66.100  192.277 7.318   1.00 103.57 ? 35  ASN B O   1 
ATOM   1292 C  CB  . ASN B 2 34  ? 68.815  191.709 9.036   1.00 109.88 ? 35  ASN B CB  1 
ATOM   1293 C  CG  . ASN B 2 34  ? 69.765  190.685 9.631   1.00 106.02 ? 35  ASN B CG  1 
ATOM   1294 O  OD1 . ASN B 2 34  ? 70.325  189.851 8.915   1.00 105.52 ? 35  ASN B OD1 1 
ATOM   1295 N  ND2 . ASN B 2 34  ? 69.941  190.734 10.949  1.00 92.79  ? 35  ASN B ND2 1 
ATOM   1296 N  N   . SER B 2 35  ? 67.894  193.338 6.459   1.00 114.21 ? 36  SER B N   1 
ATOM   1297 C  CA  . SER B 2 35  ? 67.130  194.432 5.861   1.00 116.78 ? 36  SER B CA  1 
ATOM   1298 C  C   . SER B 2 35  ? 67.930  195.134 4.756   1.00 111.83 ? 36  SER B C   1 
ATOM   1299 O  O   . SER B 2 35  ? 69.142  194.951 4.640   1.00 108.26 ? 36  SER B O   1 
ATOM   1300 C  CB  . SER B 2 35  ? 66.696  195.449 6.932   1.00 116.22 ? 36  SER B CB  1 
ATOM   1301 O  OG  . SER B 2 35  ? 67.805  196.113 7.518   1.00 115.02 ? 36  SER B OG  1 
ATOM   1302 N  N   . LEU B 2 36  ? 67.232  195.915 3.937   1.00 110.51 ? 37  LEU B N   1 
ATOM   1303 C  CA  . LEU B 2 36  ? 67.856  196.729 2.896   1.00 109.21 ? 37  LEU B CA  1 
ATOM   1304 C  C   . LEU B 2 36  ? 67.182  198.087 2.899   1.00 108.35 ? 37  LEU B C   1 
ATOM   1305 O  O   . LEU B 2 36  ? 65.959  198.173 2.829   1.00 113.42 ? 37  LEU B O   1 
ATOM   1306 C  CB  . LEU B 2 36  ? 67.726  196.095 1.507   1.00 114.88 ? 37  LEU B CB  1 
ATOM   1307 C  CG  . LEU B 2 36  ? 68.104  194.634 1.275   1.00 115.23 ? 37  LEU B CG  1 
ATOM   1308 C  CD1 . LEU B 2 36  ? 67.490  194.140 -0.027  1.00 115.38 ? 37  LEU B CD1 1 
ATOM   1309 C  CD2 . LEU B 2 36  ? 69.608  194.487 1.237   1.00 110.65 ? 37  LEU B CD2 1 
ATOM   1310 N  N   . ASN B 2 37  ? 67.973  199.150 2.960   1.00 103.49 ? 38  ASN B N   1 
ATOM   1311 C  CA  . ASN B 2 37  ? 67.410  200.489 2.888   1.00 106.67 ? 38  ASN B CA  1 
ATOM   1312 C  C   . ASN B 2 37  ? 68.026  201.258 1.736   1.00 101.77 ? 38  ASN B C   1 
ATOM   1313 O  O   . ASN B 2 37  ? 69.171  201.013 1.359   1.00 103.68 ? 38  ASN B O   1 
ATOM   1314 C  CB  . ASN B 2 37  ? 67.622  201.226 4.206   1.00 111.39 ? 38  ASN B CB  1 
ATOM   1315 C  CG  . ASN B 2 37  ? 66.699  200.727 5.300   1.00 123.98 ? 38  ASN B CG  1 
ATOM   1316 O  OD1 . ASN B 2 37  ? 66.946  199.683 5.910   1.00 121.92 ? 38  ASN B OD1 1 
ATOM   1317 N  ND2 . ASN B 2 37  ? 65.619  201.461 5.542   1.00 120.53 ? 38  ASN B ND2 1 
ATOM   1318 N  N   . PHE B 2 38  ? 67.266  202.174 1.154   1.00 100.07 ? 39  PHE B N   1 
ATOM   1319 C  CA  . PHE B 2 38  ? 67.734  202.834 -0.055  1.00 101.45 ? 39  PHE B CA  1 
ATOM   1320 C  C   . PHE B 2 38  ? 67.574  204.353 -0.035  1.00 100.79 ? 39  PHE B C   1 
ATOM   1321 O  O   . PHE B 2 38  ? 66.607  204.895 0.505   1.00 107.01 ? 39  PHE B O   1 
ATOM   1322 C  CB  . PHE B 2 38  ? 67.023  202.238 -1.276  1.00 99.83  ? 39  PHE B CB  1 
ATOM   1323 C  CG  . PHE B 2 38  ? 67.481  200.840 -1.623  1.00 103.06 ? 39  PHE B CG  1 
ATOM   1324 C  CD1 . PHE B 2 38  ? 67.091  199.749 -0.855  1.00 99.63  ? 39  PHE B CD1 1 
ATOM   1325 C  CD2 . PHE B 2 38  ? 68.301  200.619 -2.716  1.00 94.52  ? 39  PHE B CD2 1 
ATOM   1326 C  CE1 . PHE B 2 38  ? 67.515  198.470 -1.164  1.00 98.21  ? 39  PHE B CE1 1 
ATOM   1327 C  CE2 . PHE B 2 38  ? 68.724  199.341 -3.034  1.00 101.39 ? 39  PHE B CE2 1 
ATOM   1328 C  CZ  . PHE B 2 38  ? 68.331  198.265 -2.254  1.00 104.79 ? 39  PHE B CZ  1 
ATOM   1329 N  N   . ASP B 2 39  ? 68.569  205.026 -0.598  1.00 98.95  ? 40  ASP B N   1 
ATOM   1330 C  CA  . ASP B 2 39  ? 68.542  206.472 -0.763  1.00 103.49 ? 40  ASP B CA  1 
ATOM   1331 C  C   . ASP B 2 39  ? 69.039  206.841 -2.163  1.00 106.50 ? 40  ASP B C   1 
ATOM   1332 O  O   . ASP B 2 39  ? 70.232  207.077 -2.366  1.00 104.40 ? 40  ASP B O   1 
ATOM   1333 C  CB  . ASP B 2 39  ? 69.404  207.148 0.304   1.00 101.86 ? 40  ASP B CB  1 
ATOM   1334 C  CG  . ASP B 2 39  ? 69.086  208.618 0.465   1.00 102.49 ? 40  ASP B CG  1 
ATOM   1335 O  OD1 . ASP B 2 39  ? 69.402  209.404 -0.460  1.00 100.36 ? 40  ASP B OD1 1 
ATOM   1336 O  OD2 . ASP B 2 39  ? 68.528  208.981 1.523   1.00 98.04  1 40  ASP B OD2 1 
ATOM   1337 N  N   . ILE B 2 40  ? 68.122  206.912 -3.122  1.00 108.88 ? 41  ILE B N   1 
ATOM   1338 C  CA  . ILE B 2 40  ? 68.502  207.060 -4.528  1.00 108.26 ? 41  ILE B CA  1 
ATOM   1339 C  C   . ILE B 2 40  ? 68.973  208.481 -4.819  1.00 107.17 ? 41  ILE B C   1 
ATOM   1340 O  O   . ILE B 2 40  ? 69.622  208.739 -5.839  1.00 103.52 ? 41  ILE B O   1 
ATOM   1341 C  CB  . ILE B 2 40  ? 67.351  206.685 -5.468  1.00 105.86 ? 41  ILE B CB  1 
ATOM   1342 C  CG1 . ILE B 2 40  ? 66.126  207.558 -5.192  1.00 104.33 ? 41  ILE B CG1 1 
ATOM   1343 C  CG2 . ILE B 2 40  ? 67.017  205.217 -5.299  1.00 103.49 ? 41  ILE B CG2 1 
ATOM   1344 C  CD1 . ILE B 2 40  ? 64.910  207.153 -5.977  1.00 101.84 ? 41  ILE B CD1 1 
ATOM   1345 N  N   . GLU B 2 41  ? 68.643  209.391 -3.906  1.00 104.89 ? 42  GLU B N   1 
ATOM   1346 C  CA  . GLU B 2 41  ? 69.090  210.774 -3.976  1.00 110.14 ? 42  GLU B CA  1 
ATOM   1347 C  C   . GLU B 2 41  ? 70.616  210.858 -3.912  1.00 114.47 ? 42  GLU B C   1 
ATOM   1348 O  O   . GLU B 2 41  ? 71.256  211.438 -4.798  1.00 105.92 ? 42  GLU B O   1 
ATOM   1349 C  CB  . GLU B 2 41  ? 68.471  211.568 -2.828  1.00 110.28 ? 42  GLU B CB  1 
ATOM   1350 C  CG  . GLU B 2 41  ? 68.956  212.991 -2.707  1.00 112.73 ? 42  GLU B CG  1 
ATOM   1351 C  CD  . GLU B 2 41  ? 68.152  213.773 -1.694  1.00 118.99 ? 42  GLU B CD  1 
ATOM   1352 O  OE1 . GLU B 2 41  ? 67.221  213.183 -1.101  1.00 117.32 ? 42  GLU B OE1 1 
ATOM   1353 O  OE2 . GLU B 2 41  ? 68.453  214.970 -1.487  1.00 118.32 1 42  GLU B OE2 1 
ATOM   1354 N  N   . GLN B 2 42  ? 71.185  210.294 -2.846  1.00 113.42 ? 43  GLN B N   1 
ATOM   1355 C  CA  . GLN B 2 42  ? 72.637  210.206 -2.676  1.00 110.09 ? 43  GLN B CA  1 
ATOM   1356 C  C   . GLN B 2 42  ? 73.240  209.039 -3.472  1.00 107.74 ? 43  GLN B C   1 
ATOM   1357 O  O   . GLN B 2 42  ? 74.463  208.879 -3.529  1.00 102.02 ? 43  GLN B O   1 
ATOM   1358 C  CB  . GLN B 2 42  ? 72.982  210.058 -1.195  1.00 104.96 ? 43  GLN B CB  1 
ATOM   1359 C  CG  . GLN B 2 42  ? 72.704  211.298 -0.370  1.00 108.52 ? 43  GLN B CG  1 
ATOM   1360 C  CD  . GLN B 2 42  ? 72.809  211.036 1.119   1.00 109.21 ? 43  GLN B CD  1 
ATOM   1361 O  OE1 . GLN B 2 42  ? 72.313  210.026 1.618   1.00 102.46 ? 43  GLN B OE1 1 
ATOM   1362 N  NE2 . GLN B 2 42  ? 73.444  211.955 1.842   1.00 110.28 ? 43  GLN B NE2 1 
ATOM   1363 N  N   . GLN B 2 43  ? 72.366  208.248 -4.095  1.00 104.39 ? 44  GLN B N   1 
ATOM   1364 C  CA  . GLN B 2 43  ? 72.743  207.032 -4.814  1.00 97.50  ? 44  GLN B CA  1 
ATOM   1365 C  C   . GLN B 2 43  ? 73.479  206.036 -3.922  1.00 89.42  ? 44  GLN B C   1 
ATOM   1366 O  O   . GLN B 2 43  ? 74.524  205.516 -4.307  1.00 85.95  ? 44  GLN B O   1 
ATOM   1367 C  CB  . GLN B 2 43  ? 73.608  207.363 -6.040  1.00 96.78  ? 44  GLN B CB  1 
ATOM   1368 C  CG  . GLN B 2 43  ? 72.829  207.813 -7.273  1.00 98.83  ? 44  GLN B CG  1 
ATOM   1369 C  CD  . GLN B 2 43  ? 73.728  208.115 -8.464  1.00 99.25  ? 44  GLN B CD  1 
ATOM   1370 O  OE1 . GLN B 2 43  ? 74.685  208.880 -8.357  1.00 102.83 ? 44  GLN B OE1 1 
ATOM   1371 N  NE2 . GLN B 2 43  ? 73.428  207.506 -9.603  1.00 101.30 ? 44  GLN B NE2 1 
ATOM   1372 N  N   . ILE B 2 44  ? 72.929  205.770 -2.736  1.00 84.33  ? 45  ILE B N   1 
ATOM   1373 C  CA  . ILE B 2 44  ? 73.525  204.801 -1.812  1.00 88.49  ? 45  ILE B CA  1 
ATOM   1374 C  C   . ILE B 2 44  ? 72.516  203.762 -1.346  1.00 86.23  ? 45  ILE B C   1 
ATOM   1375 O  O   . ILE B 2 44  ? 71.328  203.850 -1.647  1.00 95.39  ? 45  ILE B O   1 
ATOM   1376 C  CB  . ILE B 2 44  ? 74.126  205.470 -0.550  1.00 81.12  ? 45  ILE B CB  1 
ATOM   1377 C  CG1 . ILE B 2 44  ? 73.029  205.913 0.417   1.00 92.35  ? 45  ILE B CG1 1 
ATOM   1378 C  CG2 . ILE B 2 44  ? 75.030  206.629 -0.927  1.00 87.42  ? 45  ILE B CG2 1 
ATOM   1379 C  CD1 . ILE B 2 44  ? 73.564  206.553 1.676   1.00 87.83  ? 45  ILE B CD1 1 
ATOM   1380 N  N   . MET B 2 45  ? 73.000  202.787 -0.589  1.00 80.11  ? 46  MET B N   1 
ATOM   1381 C  CA  . MET B 2 45  ? 72.157  201.716 -0.076  1.00 86.33  ? 46  MET B CA  1 
ATOM   1382 C  C   . MET B 2 45  ? 72.731  201.162 1.222   1.00 90.94  ? 46  MET B C   1 
ATOM   1383 O  O   . MET B 2 45  ? 73.879  200.724 1.264   1.00 84.98  ? 46  MET B O   1 
ATOM   1384 C  CB  . MET B 2 45  ? 72.040  200.601 -1.111  1.00 86.33  ? 46  MET B CB  1 
ATOM   1385 C  CG  . MET B 2 45  ? 71.629  199.252 -0.547  1.00 100.09 ? 46  MET B CG  1 
ATOM   1386 S  SD  . MET B 2 45  ? 72.213  197.888 -1.580  1.00 114.37 ? 46  MET B SD  1 
ATOM   1387 C  CE  . MET B 2 45  ? 72.100  198.627 -3.207  1.00 95.98  ? 46  MET B CE  1 
ATOM   1388 N  N   . SER B 2 46  ? 71.930  201.173 2.278   1.00 90.90  ? 47  SER B N   1 
ATOM   1389 C  CA  . SER B 2 46  ? 72.372  200.653 3.562   1.00 84.50  ? 47  SER B CA  1 
ATOM   1390 C  C   . SER B 2 46  ? 71.910  199.215 3.731   1.00 87.13  ? 47  SER B C   1 
ATOM   1391 O  O   . SER B 2 46  ? 70.790  198.875 3.363   1.00 94.45  ? 47  SER B O   1 
ATOM   1392 C  CB  . SER B 2 46  ? 71.858  201.536 4.702   1.00 92.88  ? 47  SER B CB  1 
ATOM   1393 O  OG  . SER B 2 46  ? 72.089  202.908 4.418   1.00 93.85  ? 47  SER B OG  1 
ATOM   1394 N  N   . VAL B 2 47  ? 72.792  198.363 4.246   1.00 87.90  ? 48  VAL B N   1 
ATOM   1395 C  CA  . VAL B 2 47  ? 72.482  196.946 4.445   1.00 95.93  ? 48  VAL B CA  1 
ATOM   1396 C  C   . VAL B 2 47  ? 72.961  196.462 5.814   1.00 98.04  ? 48  VAL B C   1 
ATOM   1397 O  O   . VAL B 2 47  ? 74.167  196.379 6.065   1.00 93.66  ? 48  VAL B O   1 
ATOM   1398 C  CB  . VAL B 2 47  ? 73.130  196.056 3.364   1.00 96.47  ? 48  VAL B CB  1 
ATOM   1399 C  CG1 . VAL B 2 47  ? 72.883  194.587 3.675   1.00 94.98  ? 48  VAL B CG1 1 
ATOM   1400 C  CG2 . VAL B 2 47  ? 72.601  196.411 1.983   1.00 102.10 ? 48  VAL B CG2 1 
ATOM   1401 N  N   . GLU B 2 48  ? 72.023  196.099 6.683   1.00 99.89  ? 49  GLU B N   1 
ATOM   1402 C  CA  . GLU B 2 48  ? 72.384  195.607 8.009   1.00 108.06 ? 49  GLU B CA  1 
ATOM   1403 C  C   . GLU B 2 48  ? 72.395  194.090 7.992   1.00 104.14 ? 49  GLU B C   1 
ATOM   1404 O  O   . GLU B 2 48  ? 71.379  193.459 7.696   1.00 99.06  ? 49  GLU B O   1 
ATOM   1405 C  CB  . GLU B 2 48  ? 71.418  196.150 9.071   1.00 107.58 ? 49  GLU B CB  1 
ATOM   1406 C  CG  . GLU B 2 48  ? 71.804  195.812 10.509  1.00 114.93 ? 49  GLU B CG  1 
ATOM   1407 C  CD  . GLU B 2 48  ? 70.845  196.406 11.533  1.00 114.76 ? 49  GLU B CD  1 
ATOM   1408 O  OE1 . GLU B 2 48  ? 69.700  196.742 11.156  1.00 113.56 ? 49  GLU B OE1 1 
ATOM   1409 O  OE2 . GLU B 2 48  ? 71.247  196.548 12.712  1.00 103.44 1 49  GLU B OE2 1 
ATOM   1410 N  N   . SER B 2 49  ? 73.554  193.510 8.299   1.00 97.11  ? 50  SER B N   1 
ATOM   1411 C  CA  . SER B 2 49  ? 73.725  192.075 8.139   1.00 100.51 ? 50  SER B CA  1 
ATOM   1412 C  C   . SER B 2 49  ? 74.907  191.466 8.880   1.00 105.09 ? 50  SER B C   1 
ATOM   1413 O  O   . SER B 2 49  ? 75.715  192.166 9.498   1.00 107.06 ? 50  SER B O   1 
ATOM   1414 C  CB  . SER B 2 49  ? 73.856  191.751 6.656   1.00 97.30  ? 50  SER B CB  1 
ATOM   1415 O  OG  . SER B 2 49  ? 75.005  192.380 6.121   1.00 93.07  ? 50  SER B OG  1 
ATOM   1416 N  N   . SER B 2 50  ? 74.958  190.137 8.824   1.00 110.18 ? 51  SER B N   1 
ATOM   1417 C  CA  . SER B 2 50  ? 76.107  189.348 9.255   1.00 108.59 ? 51  SER B CA  1 
ATOM   1418 C  C   . SER B 2 50  ? 76.787  188.740 8.020   1.00 104.86 ? 51  SER B C   1 
ATOM   1419 O  O   . SER B 2 50  ? 77.624  187.842 8.134   1.00 102.30 ? 51  SER B O   1 
ATOM   1420 C  CB  . SER B 2 50  ? 75.690  188.254 10.241  1.00 94.73  ? 51  SER B CB  1 
ATOM   1421 O  OG  . SER B 2 50  ? 74.722  187.396 9.667   1.00 98.45  ? 51  SER B OG  1 
ATOM   1422 N  N   . VAL B 2 51  ? 76.407  189.227 6.838   1.00 102.23 ? 52  VAL B N   1 
ATOM   1423 C  CA  . VAL B 2 51  ? 76.936  188.704 5.578   1.00 100.78 ? 52  VAL B CA  1 
ATOM   1424 C  C   . VAL B 2 51  ? 78.123  189.522 5.038   1.00 101.08 ? 52  VAL B C   1 
ATOM   1425 O  O   . VAL B 2 51  ? 78.179  190.749 5.195   1.00 95.82  ? 52  VAL B O   1 
ATOM   1426 C  CB  . VAL B 2 51  ? 75.826  188.639 4.498   1.00 95.96  ? 52  VAL B CB  1 
ATOM   1427 C  CG1 . VAL B 2 51  ? 75.432  190.022 4.040   1.00 88.36  ? 52  VAL B CG1 1 
ATOM   1428 C  CG2 . VAL B 2 51  ? 76.272  187.795 3.315   1.00 100.95 ? 52  VAL B CG2 1 
ATOM   1429 N  N   . ALA B 2 52  ? 79.088  188.819 4.439   1.00 105.38 ? 53  ALA B N   1 
ATOM   1430 C  CA  . ALA B 2 52  ? 80.267  189.441 3.832   1.00 96.87  ? 53  ALA B CA  1 
ATOM   1431 C  C   . ALA B 2 52  ? 79.909  190.494 2.776   1.00 100.76 ? 53  ALA B C   1 
ATOM   1432 O  O   . ALA B 2 52  ? 79.067  190.245 1.907   1.00 95.45  ? 53  ALA B O   1 
ATOM   1433 C  CB  . ALA B 2 52  ? 81.158  188.364 3.213   1.00 88.56  ? 53  ALA B CB  1 
ATOM   1434 N  N   . PRO B 2 53  ? 80.569  191.668 2.840   1.00 98.01  ? 54  PRO B N   1 
ATOM   1435 C  CA  . PRO B 2 53  ? 80.395  192.772 1.885   1.00 89.09  ? 54  PRO B CA  1 
ATOM   1436 C  C   . PRO B 2 53  ? 80.906  192.441 0.481   1.00 95.67  ? 54  PRO B C   1 
ATOM   1437 O  O   . PRO B 2 53  ? 80.384  192.963 -0.507  1.00 89.39  ? 54  PRO B O   1 
ATOM   1438 C  CB  . PRO B 2 53  ? 81.214  193.900 2.504   1.00 81.47  ? 54  PRO B CB  1 
ATOM   1439 C  CG  . PRO B 2 53  ? 82.224  193.198 3.351   1.00 92.18  ? 54  PRO B CG  1 
ATOM   1440 C  CD  . PRO B 2 53  ? 81.506  192.023 3.918   1.00 88.18  ? 54  PRO B CD  1 
ATOM   1441 N  N   . SER B 2 54  ? 81.929  191.595 0.398   1.00 92.33  ? 55  SER B N   1 
ATOM   1442 C  CA  . SER B 2 54  ? 82.428  191.134 -0.893  1.00 88.07  ? 55  SER B CA  1 
ATOM   1443 C  C   . SER B 2 54  ? 81.369  190.312 -1.630  1.00 92.43  ? 55  SER B C   1 
ATOM   1444 O  O   . SER B 2 54  ? 81.346  190.262 -2.864  1.00 85.03  ? 55  SER B O   1 
ATOM   1445 C  CB  . SER B 2 54  ? 83.698  190.306 -0.702  1.00 88.83  ? 55  SER B CB  1 
ATOM   1446 O  OG  . SER B 2 54  ? 83.438  189.196 0.138   1.00 94.98  ? 55  SER B OG  1 
ATOM   1447 N  N   . THR B 2 55  ? 80.473  189.699 -0.860  1.00 95.99  ? 56  THR B N   1 
ATOM   1448 C  CA  . THR B 2 55  ? 79.362  188.933 -1.413  1.00 95.33  ? 56  THR B CA  1 
ATOM   1449 C  C   . THR B 2 55  ? 78.353  189.882 -2.048  1.00 91.64  ? 56  THR B C   1 
ATOM   1450 O  O   . THR B 2 55  ? 77.946  189.713 -3.205  1.00 84.56  ? 56  THR B O   1 
ATOM   1451 C  CB  . THR B 2 55  ? 78.643  188.105 -0.323  1.00 90.89  ? 56  THR B CB  1 
ATOM   1452 O  OG1 . THR B 2 55  ? 79.603  187.424 0.494   1.00 90.08  ? 56  THR B OG1 1 
ATOM   1453 C  CG2 . THR B 2 55  ? 77.658  187.117 -0.945  1.00 89.98  ? 56  THR B CG2 1 
ATOM   1454 N  N   . ILE B 2 56  ? 77.968  190.882 -1.262  1.00 79.98  ? 57  ILE B N   1 
ATOM   1455 C  CA  . ILE B 2 56  ? 77.055  191.928 -1.684  1.00 81.27  ? 57  ILE B CA  1 
ATOM   1456 C  C   . ILE B 2 56  ? 77.493  192.605 -2.992  1.00 86.79  ? 57  ILE B C   1 
ATOM   1457 O  O   . ILE B 2 56  ? 76.684  192.794 -3.919  1.00 81.37  ? 57  ILE B O   1 
ATOM   1458 C  CB  . ILE B 2 56  ? 76.922  192.979 -0.572  1.00 84.09  ? 57  ILE B CB  1 
ATOM   1459 C  CG1 . ILE B 2 56  ? 76.760  192.284 0.786   1.00 90.30  ? 57  ILE B CG1 1 
ATOM   1460 C  CG2 . ILE B 2 56  ? 75.790  193.962 -0.870  1.00 72.97  ? 57  ILE B CG2 1 
ATOM   1461 C  CD1 . ILE B 2 56  ? 75.367  191.772 1.045   1.00 81.87  ? 57  ILE B CD1 1 
ATOM   1462 N  N   . ILE B 2 57  ? 78.780  192.947 -3.062  1.00 83.82  ? 58  ILE B N   1 
ATOM   1463 C  CA  . ILE B 2 57  ? 79.338  193.691 -4.191  1.00 82.40  ? 58  ILE B CA  1 
ATOM   1464 C  C   . ILE B 2 57  ? 79.533  192.867 -5.473  1.00 93.01  ? 58  ILE B C   1 
ATOM   1465 O  O   . ILE B 2 57  ? 79.215  193.334 -6.581  1.00 87.88  ? 58  ILE B O   1 
ATOM   1466 C  CB  . ILE B 2 57  ? 80.701  194.325 -3.797  1.00 80.83  ? 58  ILE B CB  1 
ATOM   1467 C  CG1 . ILE B 2 57  ? 80.479  195.530 -2.874  1.00 84.63  ? 58  ILE B CG1 1 
ATOM   1468 C  CG2 . ILE B 2 57  ? 81.497  194.733 -5.037  1.00 78.13  ? 58  ILE B CG2 1 
ATOM   1469 C  CD1 . ILE B 2 57  ? 81.726  196.008 -2.150  1.00 80.84  ? 58  ILE B CD1 1 
ATOM   1470 N  N   . ASN B 2 58  ? 80.032  191.642 -5.327  1.00 97.37  ? 59  ASN B N   1 
ATOM   1471 C  CA  . ASN B 2 58  ? 80.292  190.798 -6.491  1.00 92.47  ? 59  ASN B CA  1 
ATOM   1472 C  C   . ASN B 2 58  ? 79.008  190.361 -7.168  1.00 91.63  ? 59  ASN B C   1 
ATOM   1473 O  O   . ASN B 2 58  ? 78.949  190.251 -8.399  1.00 90.21  ? 59  ASN B O   1 
ATOM   1474 C  CB  . ASN B 2 58  ? 81.145  189.594 -6.111  1.00 91.33  ? 59  ASN B CB  1 
ATOM   1475 C  CG  . ASN B 2 58  ? 82.623  189.826 -6.397  1.00 97.46  ? 59  ASN B CG  1 
ATOM   1476 O  OD1 . ASN B 2 58  ? 83.095  189.572 -7.508  1.00 99.74  ? 59  ASN B OD1 1 
ATOM   1477 N  ND2 . ASN B 2 58  ? 83.354  190.334 -5.406  1.00 89.75  ? 59  ASN B ND2 1 
ATOM   1478 N  N   . THR B 2 59  ? 77.986  190.116 -6.353  1.00 92.90  ? 60  THR B N   1 
ATOM   1479 C  CA  . THR B 2 59  ? 76.663  189.791 -6.862  1.00 92.37  ? 60  THR B CA  1 
ATOM   1480 C  C   . THR B 2 59  ? 76.248  190.850 -7.886  1.00 96.25  ? 60  THR B C   1 
ATOM   1481 O  O   . THR B 2 59  ? 75.810  190.525 -8.991  1.00 97.63  ? 60  THR B O   1 
ATOM   1482 C  CB  . THR B 2 59  ? 75.629  189.721 -5.721  1.00 87.29  ? 60  THR B CB  1 
ATOM   1483 O  OG1 . THR B 2 59  ? 76.086  188.810 -4.715  1.00 78.01  ? 60  THR B OG1 1 
ATOM   1484 C  CG2 . THR B 2 59  ? 74.274  189.260 -6.243  1.00 93.72  ? 60  THR B CG2 1 
ATOM   1485 N  N   . LEU B 2 60  ? 76.421  192.116 -7.517  1.00 97.88  ? 61  LEU B N   1 
ATOM   1486 C  CA  . LEU B 2 60  ? 76.139  193.236 -8.413  1.00 94.09  ? 61  LEU B CA  1 
ATOM   1487 C  C   . LEU B 2 60  ? 77.186  193.351 -9.530  1.00 85.51  ? 61  LEU B C   1 
ATOM   1488 O  O   . LEU B 2 60  ? 76.854  193.386 -10.718 1.00 86.09  ? 61  LEU B O   1 
ATOM   1489 C  CB  . LEU B 2 60  ? 76.068  194.531 -7.610  1.00 89.56  ? 61  LEU B CB  1 
ATOM   1490 C  CG  . LEU B 2 60  ? 74.949  194.516 -6.561  1.00 89.25  ? 61  LEU B CG  1 
ATOM   1491 C  CD1 . LEU B 2 60  ? 75.061  195.697 -5.592  1.00 79.94  ? 61  LEU B CD1 1 
ATOM   1492 C  CD2 . LEU B 2 60  ? 73.573  194.461 -7.214  1.00 94.09  ? 61  LEU B CD2 1 
ATOM   1493 N  N   . ASP B 2 66  ? 77.746  197.302 -10.293 1.00 81.71  ? 67  ASP B N   1 
ATOM   1494 C  CA  . ASP B 2 66  ? 78.961  197.842 -9.686  1.00 89.64  ? 67  ASP B CA  1 
ATOM   1495 C  C   . ASP B 2 66  ? 78.656  198.614 -8.409  1.00 89.42  ? 67  ASP B C   1 
ATOM   1496 O  O   . ASP B 2 66  ? 77.964  199.633 -8.440  1.00 93.89  ? 67  ASP B O   1 
ATOM   1497 C  CB  . ASP B 2 66  ? 79.692  198.758 -10.674 1.00 90.34  ? 67  ASP B CB  1 
ATOM   1498 C  CG  . ASP B 2 66  ? 81.077  199.168 -10.184 1.00 96.43  ? 67  ASP B CG  1 
ATOM   1499 O  OD1 . ASP B 2 66  ? 81.573  198.579 -9.197  1.00 97.50  ? 67  ASP B OD1 1 
ATOM   1500 O  OD2 . ASP B 2 66  ? 81.671  200.084 -10.790 1.00 91.98  1 67  ASP B OD2 1 
ATOM   1501 N  N   . ALA B 2 67  ? 79.192  198.130 -7.293  1.00 83.80  ? 68  ALA B N   1 
ATOM   1502 C  CA  . ALA B 2 67  ? 78.952  198.740 -5.988  1.00 76.26  ? 68  ALA B CA  1 
ATOM   1503 C  C   . ALA B 2 67  ? 80.230  198.832 -5.144  1.00 77.37  ? 68  ALA B C   1 
ATOM   1504 O  O   . ALA B 2 67  ? 81.026  197.892 -5.106  1.00 66.80  ? 68  ALA B O   1 
ATOM   1505 C  CB  . ALA B 2 67  ? 77.881  197.963 -5.239  1.00 77.97  ? 68  ALA B CB  1 
ATOM   1506 N  N   . ILE B 2 68  ? 80.429  199.971 -4.484  1.00 73.21  ? 69  ILE B N   1 
ATOM   1507 C  CA  . ILE B 2 68  ? 81.567  200.137 -3.585  1.00 69.22  ? 69  ILE B CA  1 
ATOM   1508 C  C   . ILE B 2 68  ? 81.118  200.291 -2.135  1.00 68.19  ? 69  ILE B C   1 
ATOM   1509 O  O   . ILE B 2 68  ? 80.003  200.758 -1.873  1.00 63.92  ? 69  ILE B O   1 
ATOM   1510 C  CB  . ILE B 2 68  ? 82.428  201.349 -3.971  1.00 66.59  ? 69  ILE B CB  1 
ATOM   1511 C  CG1 . ILE B 2 68  ? 81.576  202.618 -3.968  1.00 62.71  ? 69  ILE B CG1 1 
ATOM   1512 C  CG2 . ILE B 2 68  ? 83.060  201.138 -5.338  1.00 71.98  ? 69  ILE B CG2 1 
ATOM   1513 C  CD1 . ILE B 2 68  ? 82.332  203.841 -3.543  1.00 73.90  ? 69  ILE B CD1 1 
ATOM   1514 N  N   . ILE B 2 69  ? 81.983  199.882 -1.205  1.00 64.50  ? 70  ILE B N   1 
ATOM   1515 C  CA  . ILE B 2 69  ? 81.782  200.170 0.210   1.00 60.09  ? 70  ILE B CA  1 
ATOM   1516 C  C   . ILE B 2 69  ? 81.897  201.687 0.392   1.00 56.88  ? 70  ILE B C   1 
ATOM   1517 O  O   . ILE B 2 69  ? 82.796  202.335 -0.150  1.00 54.58  ? 70  ILE B O   1 
ATOM   1518 C  CB  . ILE B 2 69  ? 82.797  199.410 1.129   1.00 58.30  ? 70  ILE B CB  1 
ATOM   1519 C  CG1 . ILE B 2 69  ? 82.171  199.100 2.488   1.00 58.58  ? 70  ILE B CG1 1 
ATOM   1520 C  CG2 . ILE B 2 69  ? 84.089  200.190 1.347   1.00 53.34  ? 70  ILE B CG2 1 
ATOM   1521 C  CD1 . ILE B 2 69  ? 80.986  198.190 2.405   1.00 73.12  ? 70  ILE B CD1 1 
ATOM   1522 N  N   . ARG B 2 70  ? 80.969  202.254 1.147   1.00 51.56  ? 71  ARG B N   1 
ATOM   1523 C  CA  . ARG B 2 70  ? 80.956  203.694 1.340   1.00 58.83  ? 71  ARG B CA  1 
ATOM   1524 C  C   . ARG B 2 70  ? 80.842  203.959 2.831   1.00 55.17  ? 71  ARG B C   1 
ATOM   1525 O  O   . ARG B 2 70  ? 80.510  203.055 3.606   1.00 48.04  ? 71  ARG B O   1 
ATOM   1526 C  CB  . ARG B 2 70  ? 79.795  204.345 0.574   1.00 57.99  ? 71  ARG B CB  1 
ATOM   1527 C  CG  . ARG B 2 70  ? 80.062  205.775 0.123   1.00 63.95  ? 71  ARG B CG  1 
ATOM   1528 C  CD  . ARG B 2 70  ? 78.929  206.306 -0.758  1.00 72.94  ? 71  ARG B CD  1 
ATOM   1529 N  NE  . ARG B 2 70  ? 78.607  207.706 -0.495  1.00 67.17  ? 71  ARG B NE  1 
ATOM   1530 C  CZ  . ARG B 2 70  ? 78.137  208.156 0.666   1.00 72.54  ? 71  ARG B CZ  1 
ATOM   1531 N  NH1 . ARG B 2 70  ? 77.942  207.316 1.675   1.00 70.93  1 71  ARG B NH1 1 
ATOM   1532 N  NH2 . ARG B 2 70  ? 77.874  209.447 0.823   1.00 71.74  ? 71  ARG B NH2 1 
ATOM   1533 N  N   . GLY B 2 71  ? 81.147  205.186 3.232   1.00 51.40  ? 72  GLY B N   1 
ATOM   1534 C  CA  . GLY B 2 71  ? 81.033  205.570 4.621   1.00 50.78  ? 72  GLY B CA  1 
ATOM   1535 C  C   . GLY B 2 71  ? 79.603  205.924 4.949   1.00 63.28  ? 72  GLY B C   1 
ATOM   1536 O  O   . GLY B 2 71  ? 78.895  206.482 4.113   1.00 66.28  ? 72  GLY B O   1 
ATOM   1537 N  N   . ALA B 2 72  ? 79.168  205.575 6.154   1.00 64.86  ? 73  ALA B N   1 
ATOM   1538 C  CA  . ALA B 2 72  ? 77.913  206.086 6.693   1.00 73.21  ? 73  ALA B CA  1 
ATOM   1539 C  C   . ALA B 2 72  ? 78.073  207.567 7.062   1.00 79.28  ? 73  ALA B C   1 
ATOM   1540 O  O   . ALA B 2 72  ? 79.101  208.178 6.771   1.00 83.50  ? 73  ALA B O   1 
ATOM   1541 C  CB  . ALA B 2 72  ? 77.485  205.275 7.898   1.00 75.44  ? 73  ALA B CB  1 
ATOM   1542 N  N   . GLY B 2 73  ? 77.054  208.159 7.674   1.00 82.17  ? 74  GLY B N   1 
ATOM   1543 C  CA  . GLY B 2 73  ? 77.154  209.543 8.115   1.00 89.81  ? 74  GLY B CA  1 
ATOM   1544 C  C   . GLY B 2 73  ? 77.813  209.702 9.481   1.00 84.78  ? 74  GLY B C   1 
ATOM   1545 O  O   . GLY B 2 73  ? 78.172  210.814 9.884   1.00 76.05  ? 74  GLY B O   1 
ATOM   1546 N  N   . LYS B 2 74  ? 77.932  208.582 10.195  1.00 81.85  ? 75  LYS B N   1 
ATOM   1547 C  CA  . LYS B 2 74  ? 78.513  208.526 11.539  1.00 78.39  ? 75  LYS B CA  1 
ATOM   1548 C  C   . LYS B 2 74  ? 79.856  209.244 11.623  1.00 77.30  ? 75  LYS B C   1 
ATOM   1549 O  O   . LYS B 2 74  ? 80.746  209.010 10.802  1.00 77.19  ? 75  LYS B O   1 
ATOM   1550 C  CB  . LYS B 2 74  ? 78.663  207.071 11.985  1.00 79.94  ? 75  LYS B CB  1 
ATOM   1551 C  CG  . LYS B 2 74  ? 77.328  206.358 12.165  1.00 89.22  ? 75  LYS B CG  1 
ATOM   1552 C  CD  . LYS B 2 74  ? 77.463  204.860 11.976  1.00 88.63  ? 75  LYS B CD  1 
ATOM   1553 C  CE  . LYS B 2 74  ? 78.515  204.301 12.931  1.00 86.02  ? 75  LYS B CE  1 
ATOM   1554 N  NZ  . LYS B 2 74  ? 78.001  204.220 14.331  1.00 91.88  1 75  LYS B NZ  1 
ATOM   1555 N  N   . PRO B 2 75  ? 80.010  210.114 12.632  1.00 72.11  ? 76  PRO B N   1 
ATOM   1556 C  CA  . PRO B 2 75  ? 81.204  210.958 12.733  1.00 68.17  ? 76  PRO B CA  1 
ATOM   1557 C  C   . PRO B 2 75  ? 82.437  210.169 13.148  1.00 64.53  ? 76  PRO B C   1 
ATOM   1558 O  O   . PRO B 2 75  ? 82.342  209.304 14.024  1.00 54.96  ? 76  PRO B O   1 
ATOM   1559 C  CB  . PRO B 2 75  ? 80.830  211.985 13.803  1.00 67.96  ? 76  PRO B CB  1 
ATOM   1560 C  CG  . PRO B 2 75  ? 79.680  211.413 14.536  1.00 76.73  ? 76  PRO B CG  1 
ATOM   1561 C  CD  . PRO B 2 75  ? 79.110  210.255 13.786  1.00 68.32  ? 76  PRO B CD  1 
ATOM   1562 N  N   . ASN B 2 76  ? 83.570  210.483 12.516  1.00 58.54  ? 77  ASN B N   1 
ATOM   1563 C  CA  . ASN B 2 76  ? 84.842  209.788 12.736  1.00 57.93  ? 77  ASN B CA  1 
ATOM   1564 C  C   . ASN B 2 76  ? 84.739  208.269 12.587  1.00 53.74  ? 77  ASN B C   1 
ATOM   1565 O  O   . ASN B 2 76  ? 85.279  207.507 13.394  1.00 51.83  ? 77  ASN B O   1 
ATOM   1566 C  CB  . ASN B 2 76  ? 85.416  210.151 14.116  1.00 50.40  ? 77  ASN B CB  1 
ATOM   1567 C  CG  . ASN B 2 76  ? 85.568  211.671 14.307  1.00 67.99  ? 77  ASN B CG  1 
ATOM   1568 O  OD1 . ASN B 2 76  ? 86.368  212.339 13.620  1.00 57.15  ? 77  ASN B OD1 1 
ATOM   1569 N  ND2 . ASN B 2 76  ? 84.789  212.223 15.240  1.00 68.62  ? 77  ASN B ND2 1 
ATOM   1570 N  N   . SER B 2 77  ? 84.039  207.842 11.542  1.00 42.67  ? 78  SER B N   1 
ATOM   1571 C  CA  . SER B 2 77  ? 83.851  206.430 11.265  1.00 49.52  ? 78  SER B CA  1 
ATOM   1572 C  C   . SER B 2 77  ? 84.586  206.024 9.981   1.00 51.57  ? 78  SER B C   1 
ATOM   1573 O  O   . SER B 2 77  ? 84.827  204.833 9.739   1.00 45.00  ? 78  SER B O   1 
ATOM   1574 C  CB  . SER B 2 77  ? 82.350  206.101 11.144  1.00 54.40  ? 78  SER B CB  1 
ATOM   1575 O  OG  . SER B 2 77  ? 81.747  206.743 10.024  1.00 59.32  ? 78  SER B OG  1 
ATOM   1576 N  N   . SER B 2 78  ? 84.971  207.010 9.178   1.00 34.66  ? 79  SER B N   1 
ATOM   1577 C  CA  . SER B 2 78  ? 85.607  206.701 7.910   1.00 41.07  ? 79  SER B CA  1 
ATOM   1578 C  C   . SER B 2 78  ? 87.013  207.235 7.804   1.00 39.62  ? 79  SER B C   1 
ATOM   1579 O  O   . SER B 2 78  ? 87.308  208.360 8.190   1.00 39.21  ? 79  SER B O   1 
ATOM   1580 C  CB  . SER B 2 78  ? 84.786  207.257 6.736   1.00 38.59  ? 79  SER B CB  1 
ATOM   1581 O  OG  . SER B 2 78  ? 83.549  206.584 6.598   1.00 52.69  ? 79  SER B OG  1 
ATOM   1582 N  N   . ALA B 2 79  ? 87.871  206.435 7.205   1.00 36.71  ? 80  ALA B N   1 
ATOM   1583 C  CA  . ALA B 2 79  ? 89.222  206.882 6.957   1.00 41.98  ? 80  ALA B CA  1 
ATOM   1584 C  C   . ALA B 2 79  ? 89.745  206.420 5.590   1.00 39.72  ? 80  ALA B C   1 
ATOM   1585 O  O   . ALA B 2 79  ? 89.176  205.548 4.933   1.00 35.03  ? 80  ALA B O   1 
ATOM   1586 C  CB  . ALA B 2 79  ? 90.137  206.409 8.072   1.00 28.28  ? 80  ALA B CB  1 
ATOM   1587 N  N   . VAL B 2 80  ? 90.836  207.039 5.169   1.00 40.88  ? 81  VAL B N   1 
ATOM   1588 C  CA  . VAL B 2 80  ? 91.541  206.634 3.971   1.00 32.42  ? 81  VAL B CA  1 
ATOM   1589 C  C   . VAL B 2 80  ? 93.067  206.677 4.202   1.00 39.06  ? 81  VAL B C   1 
ATOM   1590 O  O   . VAL B 2 80  ? 93.585  207.425 5.049   1.00 35.50  ? 81  VAL B O   1 
ATOM   1591 C  CB  . VAL B 2 80  ? 91.145  207.518 2.774   1.00 36.31  ? 81  VAL B CB  1 
ATOM   1592 C  CG1 . VAL B 2 80  ? 91.848  208.867 2.840   1.00 36.32  ? 81  VAL B CG1 1 
ATOM   1593 C  CG2 . VAL B 2 80  ? 91.437  206.814 1.479   1.00 38.67  ? 81  VAL B CG2 1 
ATOM   1594 N  N   . ALA B 2 81  ? 93.780  205.831 3.470   1.00 42.31  ? 82  ALA B N   1 
ATOM   1595 C  CA  . ALA B 2 81  ? 95.225  205.896 3.432   1.00 34.48  ? 82  ALA B CA  1 
ATOM   1596 C  C   . ALA B 2 81  ? 95.705  205.742 1.991   1.00 35.04  ? 82  ALA B C   1 
ATOM   1597 O  O   . ALA B 2 81  ? 95.472  204.717 1.342   1.00 34.86  ? 82  ALA B O   1 
ATOM   1598 C  CB  . ALA B 2 81  ? 95.828  204.836 4.327   1.00 33.12  ? 82  ALA B CB  1 
ATOM   1599 N  N   . ILE B 2 82  ? 96.368  206.778 1.498   1.00 32.43  ? 83  ILE B N   1 
ATOM   1600 C  CA  . ILE B 2 82  ? 96.962  206.744 0.176   1.00 32.47  ? 83  ILE B CA  1 
ATOM   1601 C  C   . ILE B 2 82  ? 98.352  206.169 0.327   1.00 36.82  ? 83  ILE B C   1 
ATOM   1602 O  O   . ILE B 2 82  ? 99.183  206.740 1.017   1.00 39.14  ? 83  ILE B O   1 
ATOM   1603 C  CB  . ILE B 2 82  ? 97.030  208.142 -0.477  1.00 37.81  ? 83  ILE B CB  1 
ATOM   1604 C  CG1 . ILE B 2 82  ? 95.652  208.816 -0.475  1.00 36.16  ? 83  ILE B CG1 1 
ATOM   1605 C  CG2 . ILE B 2 82  ? 97.563  208.044 -1.923  1.00 32.96  ? 83  ILE B CG2 1 
ATOM   1606 C  CD1 . ILE B 2 82  ? 95.704  210.256 -0.977  1.00 28.19  ? 83  ILE B CD1 1 
ATOM   1607 N  N   . LEU B 2 83  ? 98.595  205.030 -0.311  1.00 35.77  ? 84  LEU B N   1 
ATOM   1608 C  CA  . LEU B 2 83  ? 99.832  204.280 -0.115  1.00 37.82  ? 84  LEU B CA  1 
ATOM   1609 C  C   . LEU B 2 83  ? 100.853 204.553 -1.211  1.00 37.94  ? 84  LEU B C   1 
ATOM   1610 O  O   . LEU B 2 83  ? 100.624 204.234 -2.368  1.00 41.15  ? 84  LEU B O   1 
ATOM   1611 C  CB  . LEU B 2 83  ? 99.528  202.785 -0.060  1.00 37.14  ? 84  LEU B CB  1 
ATOM   1612 C  CG  . LEU B 2 83  ? 98.274  202.514 0.754   1.00 32.12  ? 84  LEU B CG  1 
ATOM   1613 C  CD1 . LEU B 2 83  ? 97.942  201.052 0.648   1.00 28.30  ? 84  LEU B CD1 1 
ATOM   1614 C  CD2 . LEU B 2 83  ? 98.477  202.953 2.198   1.00 35.45  ? 84  LEU B CD2 1 
ATOM   1615 N  N   . GLU B 2 84  ? 101.974 205.148 -0.832  1.00 38.46  ? 85  GLU B N   1 
ATOM   1616 C  CA  . GLU B 2 84  ? 103.012 205.556 -1.767  1.00 41.49  ? 85  GLU B CA  1 
ATOM   1617 C  C   . GLU B 2 84  ? 104.345 204.905 -1.440  1.00 45.74  ? 85  GLU B C   1 
ATOM   1618 O  O   . GLU B 2 84  ? 104.652 204.692 -0.247  1.00 40.55  ? 85  GLU B O   1 
ATOM   1619 C  CB  . GLU B 2 84  ? 103.170 207.088 -1.732  1.00 43.16  ? 85  GLU B CB  1 
ATOM   1620 C  CG  . GLU B 2 84  ? 102.084 207.855 -2.462  1.00 53.66  ? 85  GLU B CG  1 
ATOM   1621 C  CD  . GLU B 2 84  ? 102.146 209.373 -2.239  1.00 62.69  ? 85  GLU B CD  1 
ATOM   1622 O  OE1 . GLU B 2 84  ? 102.686 210.087 -3.116  1.00 59.55  ? 85  GLU B OE1 1 
ATOM   1623 O  OE2 . GLU B 2 84  ? 101.663 209.851 -1.186  1.00 62.18  1 85  GLU B OE2 1 
ATOM   1624 N  N   . THR B 2 85  ? 105.159 204.635 -2.469  1.00 38.78  ? 86  THR B N   1 
ATOM   1625 C  CA  . THR B 2 85  ? 106.522 204.174 -2.217  1.00 38.78  ? 86  THR B CA  1 
ATOM   1626 C  C   . THR B 2 85  ? 107.316 205.338 -1.657  1.00 41.03  ? 86  THR B C   1 
ATOM   1627 O  O   . THR B 2 85  ? 107.055 206.492 -1.959  1.00 51.74  ? 86  THR B O   1 
ATOM   1628 C  CB  . THR B 2 85  ? 107.250 203.639 -3.474  1.00 40.64  ? 86  THR B CB  1 
ATOM   1629 O  OG1 . THR B 2 85  ? 107.284 204.666 -4.471  1.00 40.02  ? 86  THR B OG1 1 
ATOM   1630 C  CG2 . THR B 2 85  ? 106.571 202.399 -4.044  1.00 38.31  ? 86  THR B CG2 1 
ATOM   1631 N  N   . PHE B 2 86  ? 108.284 205.022 -0.822  1.00 51.39  ? 87  PHE B N   1 
ATOM   1632 C  CA  . PHE B 2 86  ? 109.148 206.029 -0.250  1.00 49.14  ? 87  PHE B CA  1 
ATOM   1633 C  C   . PHE B 2 86  ? 110.549 205.955 -0.825  1.00 51.32  ? 87  PHE B C   1 
ATOM   1634 O  O   . PHE B 2 86  ? 111.189 206.976 -1.031  1.00 52.17  ? 87  PHE B O   1 
ATOM   1635 C  CB  . PHE B 2 86  ? 109.221 205.903 1.266   1.00 45.16  ? 87  PHE B CB  1 
ATOM   1636 C  CG  . PHE B 2 86  ? 110.223 206.823 1.866   1.00 48.90  ? 87  PHE B CG  1 
ATOM   1637 C  CD1 . PHE B 2 86  ? 109.941 208.177 2.001   1.00 49.81  ? 87  PHE B CD1 1 
ATOM   1638 C  CD2 . PHE B 2 86  ? 111.472 206.357 2.238   1.00 46.23  ? 87  PHE B CD2 1 
ATOM   1639 C  CE1 . PHE B 2 86  ? 110.880 209.051 2.528   1.00 46.01  ? 87  PHE B CE1 1 
ATOM   1640 C  CE2 . PHE B 2 86  ? 112.419 207.224 2.769   1.00 52.85  ? 87  PHE B CE2 1 
ATOM   1641 C  CZ  . PHE B 2 86  ? 112.122 208.575 2.916   1.00 51.40  ? 87  PHE B CZ  1 
ATOM   1642 N  N   . GLN B 2 87  ? 111.063 204.740 -0.969  1.00 53.15  ? 88  GLN B N   1 
ATOM   1643 C  CA  . GLN B 2 87  ? 112.362 204.530 -1.607  1.00 55.54  ? 88  GLN B CA  1 
ATOM   1644 C  C   . GLN B 2 87  ? 112.245 204.455 -3.110  1.00 59.11  ? 88  GLN B C   1 
ATOM   1645 O  O   . GLN B 2 87  ? 111.154 204.247 -3.652  1.00 55.99  ? 88  GLN B O   1 
ATOM   1646 C  CB  . GLN B 2 87  ? 113.030 203.262 -1.084  1.00 49.23  ? 88  GLN B CB  1 
ATOM   1647 C  CG  . GLN B 2 87  ? 113.987 203.576 0.006   1.00 62.53  ? 88  GLN B CG  1 
ATOM   1648 C  CD  . GLN B 2 87  ? 113.848 202.631 1.147   1.00 75.93  ? 88  GLN B CD  1 
ATOM   1649 O  OE1 . GLN B 2 87  ? 113.082 201.665 1.074   1.00 71.21  ? 88  GLN B OE1 1 
ATOM   1650 N  NE2 . GLN B 2 87  ? 114.537 202.928 2.245   1.00 79.34  ? 88  GLN B NE2 1 
ATOM   1651 N  N   . LYS B 2 88  ? 113.375 204.677 -3.773  1.00 68.74  ? 89  LYS B N   1 
ATOM   1652 C  CA  . LYS B 2 88  ? 113.505 204.471 -5.210  1.00 61.45  ? 89  LYS B CA  1 
ATOM   1653 C  C   . LYS B 2 88  ? 113.950 203.021 -5.375  1.00 60.78  ? 89  LYS B C   1 
ATOM   1654 O  O   . LYS B 2 88  ? 114.901 202.574 -4.727  1.00 63.65  ? 89  LYS B O   1 
ATOM   1655 C  CB  . LYS B 2 88  ? 114.497 205.476 -5.808  1.00 66.51  ? 89  LYS B CB  1 
ATOM   1656 C  CG  . LYS B 2 88  ? 114.734 205.413 -7.312  1.00 83.02  ? 89  LYS B CG  1 
ATOM   1657 C  CD  . LYS B 2 88  ? 115.802 206.447 -7.705  1.00 84.30  ? 89  LYS B CD  1 
ATOM   1658 C  CE  . LYS B 2 88  ? 116.289 206.295 -9.142  1.00 95.89  ? 89  LYS B CE  1 
ATOM   1659 N  NZ  . LYS B 2 88  ? 117.389 207.262 -9.439  1.00 72.76  1 89  LYS B NZ  1 
ATOM   1660 N  N   . TYR B 2 89  ? 113.214 202.257 -6.171  1.00 65.01  ? 90  TYR B N   1 
ATOM   1661 C  CA  . TYR B 2 89  ? 113.586 200.867 -6.407  1.00 65.94  ? 90  TYR B CA  1 
ATOM   1662 C  C   . TYR B 2 89  ? 114.069 200.680 -7.824  1.00 64.91  ? 90  TYR B C   1 
ATOM   1663 O  O   . TYR B 2 89  ? 113.499 201.237 -8.761  1.00 65.96  ? 90  TYR B O   1 
ATOM   1664 C  CB  . TYR B 2 89  ? 112.419 199.920 -6.148  1.00 63.34  ? 90  TYR B CB  1 
ATOM   1665 C  CG  . TYR B 2 89  ? 111.921 199.927 -4.736  1.00 56.50  ? 90  TYR B CG  1 
ATOM   1666 C  CD1 . TYR B 2 89  ? 112.488 199.101 -3.779  1.00 51.86  ? 90  TYR B CD1 1 
ATOM   1667 C  CD2 . TYR B 2 89  ? 110.866 200.742 -4.364  1.00 50.25  ? 90  TYR B CD2 1 
ATOM   1668 C  CE1 . TYR B 2 89  ? 112.031 199.101 -2.475  1.00 52.23  ? 90  TYR B CE1 1 
ATOM   1669 C  CE2 . TYR B 2 89  ? 110.398 200.748 -3.069  1.00 56.33  ? 90  TYR B CE2 1 
ATOM   1670 C  CZ  . TYR B 2 89  ? 110.981 199.925 -2.131  1.00 50.68  ? 90  TYR B CZ  1 
ATOM   1671 O  OH  . TYR B 2 89  ? 110.503 199.928 -0.855  1.00 46.12  ? 90  TYR B OH  1 
ATOM   1672 N  N   . THR B 2 90  ? 115.105 199.869 -7.972  1.00 71.01  ? 91  THR B N   1 
ATOM   1673 C  CA  . THR B 2 90  ? 115.628 199.529 -9.281  1.00 69.19  ? 91  THR B CA  1 
ATOM   1674 C  C   . THR B 2 90  ? 114.538 198.921 -10.136 1.00 67.47  ? 91  THR B C   1 
ATOM   1675 O  O   . THR B 2 90  ? 114.372 199.307 -11.281 1.00 69.16  ? 91  THR B O   1 
ATOM   1676 C  CB  . THR B 2 90  ? 116.815 198.569 -9.172  1.00 76.20  ? 91  THR B CB  1 
ATOM   1677 O  OG1 . THR B 2 90  ? 117.834 199.189 -8.383  1.00 68.93  ? 91  THR B OG1 1 
ATOM   1678 C  CG2 . THR B 2 90  ? 117.380 198.261 -10.541 1.00 80.53  ? 91  THR B CG2 1 
ATOM   1679 N  N   . ILE B 2 91  ? 113.786 197.984 -9.568  1.00 66.65  ? 92  ILE B N   1 
ATOM   1680 C  CA  . ILE B 2 91  ? 112.726 197.285 -10.299 1.00 66.95  ? 92  ILE B CA  1 
ATOM   1681 C  C   . ILE B 2 91  ? 111.479 198.126 -10.562 1.00 63.18  ? 92  ILE B C   1 
ATOM   1682 O  O   . ILE B 2 91  ? 110.575 197.706 -11.286 1.00 57.87  ? 92  ILE B O   1 
ATOM   1683 C  CB  . ILE B 2 91  ? 112.274 196.040 -9.553  1.00 68.10  ? 92  ILE B CB  1 
ATOM   1684 C  CG1 . ILE B 2 91  ? 111.616 196.449 -8.233  1.00 58.18  ? 92  ILE B CG1 1 
ATOM   1685 C  CG2 . ILE B 2 91  ? 113.455 195.110 -9.343  1.00 60.54  ? 92  ILE B CG2 1 
ATOM   1686 C  CD1 . ILE B 2 91  ? 110.987 195.313 -7.506  1.00 64.95  ? 92  ILE B CD1 1 
ATOM   1687 N  N   . ASP B 2 92  ? 111.433 199.304 -9.958  1.00 65.12  ? 93  ASP B N   1 
ATOM   1688 C  CA  . ASP B 2 92  ? 110.260 200.162 -10.027 1.00 66.23  ? 93  ASP B CA  1 
ATOM   1689 C  C   . ASP B 2 92  ? 110.534 201.339 -10.953 1.00 70.51  ? 93  ASP B C   1 
ATOM   1690 O  O   . ASP B 2 92  ? 111.177 202.318 -10.577 1.00 75.08  ? 93  ASP B O   1 
ATOM   1691 C  CB  . ASP B 2 92  ? 109.887 200.649 -8.623  1.00 67.93  ? 93  ASP B CB  1 
ATOM   1692 C  CG  . ASP B 2 92  ? 108.443 201.091 -8.512  1.00 72.84  ? 93  ASP B CG  1 
ATOM   1693 O  OD1 . ASP B 2 92  ? 107.865 201.530 -9.528  1.00 64.79  ? 93  ASP B OD1 1 
ATOM   1694 O  OD2 . ASP B 2 92  ? 107.889 201.001 -7.390  1.00 67.26  1 93  ASP B OD2 1 
ATOM   1695 N  N   . GLN B 2 93  ? 110.050 201.232 -12.179 1.00 70.98  ? 94  GLN B N   1 
ATOM   1696 C  CA  . GLN B 2 93  ? 110.339 202.248 -13.169 1.00 77.77  ? 94  GLN B CA  1 
ATOM   1697 C  C   . GLN B 2 93  ? 109.128 203.136 -13.469 1.00 79.08  ? 94  GLN B C   1 
ATOM   1698 O  O   . GLN B 2 93  ? 109.200 204.024 -14.314 1.00 75.87  ? 94  GLN B O   1 
ATOM   1699 C  CB  . GLN B 2 93  ? 110.853 201.572 -14.442 1.00 82.38  ? 94  GLN B CB  1 
ATOM   1700 C  CG  . GLN B 2 93  ? 112.168 200.823 -14.226 1.00 69.44  ? 94  GLN B CG  1 
ATOM   1701 C  CD  . GLN B 2 93  ? 113.286 201.735 -13.730 1.00 80.59  ? 94  GLN B CD  1 
ATOM   1702 O  OE1 . GLN B 2 93  ? 113.285 202.939 -13.983 1.00 85.64  ? 94  GLN B OE1 1 
ATOM   1703 N  NE2 . GLN B 2 93  ? 114.240 201.163 -13.011 1.00 81.28  ? 94  GLN B NE2 1 
ATOM   1704 N  N   . LYS B 2 94  ? 108.036 202.925 -12.738 1.00 75.69  ? 95  LYS B N   1 
ATOM   1705 C  CA  . LYS B 2 94  ? 106.873 203.808 -12.819 1.00 75.83  ? 95  LYS B CA  1 
ATOM   1706 C  C   . LYS B 2 94  ? 107.181 205.136 -12.125 1.00 72.35  ? 95  LYS B C   1 
ATOM   1707 O  O   . LYS B 2 94  ? 107.152 205.219 -10.895 1.00 72.05  ? 95  LYS B O   1 
ATOM   1708 C  CB  . LYS B 2 94  ? 105.651 203.131 -12.194 1.00 68.53  ? 95  LYS B CB  1 
ATOM   1709 C  CG  . LYS B 2 94  ? 104.368 203.941 -12.238 1.00 64.21  ? 95  LYS B CG  1 
ATOM   1710 C  CD  . LYS B 2 94  ? 103.178 203.077 -11.805 1.00 59.15  ? 95  LYS B CD  1 
ATOM   1711 C  CE  . LYS B 2 94  ? 101.858 203.853 -11.795 1.00 59.17  ? 95  LYS B CE  1 
ATOM   1712 N  NZ  . LYS B 2 94  ? 101.505 204.449 -13.114 1.00 63.88  1 95  LYS B NZ  1 
ATOM   1713 N  N   . LYS B 2 95  ? 107.473 206.173 -12.911 1.00 70.04  ? 96  LYS B N   1 
ATOM   1714 C  CA  . LYS B 2 95  ? 107.971 207.426 -12.345 1.00 70.79  ? 96  LYS B CA  1 
ATOM   1715 C  C   . LYS B 2 95  ? 106.976 208.572 -12.384 1.00 58.00  ? 96  LYS B C   1 
ATOM   1716 O  O   . LYS B 2 95  ? 107.287 209.667 -11.935 1.00 65.94  ? 96  LYS B O   1 
ATOM   1717 C  CB  . LYS B 2 95  ? 109.247 207.855 -13.071 1.00 74.43  ? 96  LYS B CB  1 
ATOM   1718 C  CG  . LYS B 2 95  ? 110.388 206.882 -12.907 1.00 77.31  ? 96  LYS B CG  1 
ATOM   1719 C  CD  . LYS B 2 95  ? 110.729 206.716 -11.432 1.00 82.24  ? 96  LYS B CD  1 
ATOM   1720 C  CE  . LYS B 2 95  ? 111.621 205.497 -11.193 1.00 90.10  ? 96  LYS B CE  1 
ATOM   1721 N  NZ  . LYS B 2 95  ? 112.945 205.592 -11.877 1.00 86.03  1 96  LYS B NZ  1 
ATOM   1722 N  N   . ASP B 2 96  ? 105.775 208.321 -12.887 1.00 60.21  ? 97  ASP B N   1 
ATOM   1723 C  CA  . ASP B 2 96  ? 104.777 209.388 -12.970 1.00 69.91  ? 97  ASP B CA  1 
ATOM   1724 C  C   . ASP B 2 96  ? 104.062 209.640 -11.635 1.00 65.87  ? 97  ASP B C   1 
ATOM   1725 O  O   . ASP B 2 96  ? 103.573 210.749 -11.388 1.00 68.22  ? 97  ASP B O   1 
ATOM   1726 C  CB  . ASP B 2 96  ? 103.754 209.090 -14.080 1.00 60.54  ? 97  ASP B CB  1 
ATOM   1727 C  CG  . ASP B 2 96  ? 103.047 207.765 -13.898 1.00 70.59  ? 97  ASP B CG  1 
ATOM   1728 O  OD1 . ASP B 2 96  ? 103.609 206.894 -13.196 1.00 62.85  ? 97  ASP B OD1 1 
ATOM   1729 O  OD2 . ASP B 2 96  ? 101.931 207.602 -14.461 1.00 66.93  1 97  ASP B OD2 1 
ATOM   1730 N  N   . THR B 2 97  ? 104.026 208.618 -10.777 1.00 62.59  ? 98  THR B N   1 
ATOM   1731 C  CA  . THR B 2 97  ? 103.466 208.731 -9.427  1.00 52.09  ? 98  THR B CA  1 
ATOM   1732 C  C   . THR B 2 97  ? 104.049 207.634 -8.543  1.00 48.85  ? 98  THR B C   1 
ATOM   1733 O  O   . THR B 2 97  ? 104.426 206.575 -9.033  1.00 52.43  ? 98  THR B O   1 
ATOM   1734 C  CB  . THR B 2 97  ? 101.907 208.637 -9.427  1.00 54.92  ? 98  THR B CB  1 
ATOM   1735 O  OG1 . THR B 2 97  ? 101.395 208.871 -8.104  1.00 47.47  ? 98  THR B OG1 1 
ATOM   1736 C  CG2 . THR B 2 97  ? 101.424 207.271 -9.954  1.00 49.56  ? 98  THR B CG2 1 
ATOM   1737 N  N   . ALA B 2 98  ? 104.149 207.901 -7.245  1.00 54.52  ? 99  ALA B N   1 
ATOM   1738 C  CA  . ALA B 2 98  ? 104.595 206.887 -6.282  1.00 45.46  ? 99  ALA B CA  1 
ATOM   1739 C  C   . ALA B 2 98  ? 103.412 206.149 -5.636  1.00 41.07  ? 99  ALA B C   1 
ATOM   1740 O  O   . ALA B 2 98  ? 103.607 205.249 -4.825  1.00 47.80  ? 99  ALA B O   1 
ATOM   1741 C  CB  . ALA B 2 98  ? 105.491 207.527 -5.186  1.00 39.87  ? 99  ALA B CB  1 
ATOM   1742 N  N   . VAL B 2 99  ? 102.188 206.535 -5.975  1.00 43.43  ? 100 VAL B N   1 
ATOM   1743 C  CA  . VAL B 2 99  ? 101.021 205.837 -5.449  1.00 40.33  ? 100 VAL B CA  1 
ATOM   1744 C  C   . VAL B 2 99  ? 100.981 204.417 -6.027  1.00 47.23  ? 100 VAL B C   1 
ATOM   1745 O  O   . VAL B 2 99  ? 101.131 204.217 -7.230  1.00 40.32  ? 100 VAL B O   1 
ATOM   1746 C  CB  . VAL B 2 99  ? 99.712  206.603 -5.751  1.00 39.04  ? 100 VAL B CB  1 
ATOM   1747 C  CG1 . VAL B 2 99  ? 98.485  205.822 -5.292  1.00 31.09  ? 100 VAL B CG1 1 
ATOM   1748 C  CG2 . VAL B 2 99  ? 99.735  207.975 -5.086  1.00 35.54  ? 100 VAL B CG2 1 
ATOM   1749 N  N   . ARG B 2 100 ? 100.827 203.434 -5.144  1.00 41.53  ? 101 ARG B N   1 
ATOM   1750 C  CA  . ARG B 2 100 ? 100.723 202.039 -5.546  1.00 46.07  ? 101 ARG B CA  1 
ATOM   1751 C  C   . ARG B 2 100 ? 99.432  201.430 -5.011  1.00 41.00  ? 101 ARG B C   1 
ATOM   1752 O  O   . ARG B 2 100 ? 98.993  200.380 -5.457  1.00 40.19  ? 101 ARG B O   1 
ATOM   1753 C  CB  . ARG B 2 100 ? 101.929 201.249 -5.045  1.00 42.47  ? 101 ARG B CB  1 
ATOM   1754 C  CG  . ARG B 2 100 ? 103.279 201.719 -5.587  1.00 43.59  ? 101 ARG B CG  1 
ATOM   1755 C  CD  . ARG B 2 100 ? 103.430 201.394 -7.056  1.00 41.91  ? 101 ARG B CD  1 
ATOM   1756 N  NE  . ARG B 2 100 ? 104.620 201.996 -7.647  1.00 50.82  ? 101 ARG B NE  1 
ATOM   1757 C  CZ  . ARG B 2 100 ? 104.638 203.159 -8.296  1.00 53.28  ? 101 ARG B CZ  1 
ATOM   1758 N  NH1 . ARG B 2 100 ? 103.526 203.860 -8.457  1.00 51.84  1 101 ARG B NH1 1 
ATOM   1759 N  NH2 . ARG B 2 100 ? 105.770 203.621 -8.792  1.00 52.77  ? 101 ARG B NH2 1 
ATOM   1760 N  N   . GLY B 2 101 ? 98.829  202.092 -4.038  1.00 40.36  ? 102 GLY B N   1 
ATOM   1761 C  CA  . GLY B 2 101 ? 97.682  201.515 -3.377  1.00 34.24  ? 102 GLY B CA  1 
ATOM   1762 C  C   . GLY B 2 101 ? 96.819  202.507 -2.654  1.00 36.47  ? 102 GLY B C   1 
ATOM   1763 O  O   . GLY B 2 101 ? 97.227  203.634 -2.381  1.00 34.09  ? 102 GLY B O   1 
ATOM   1764 N  N   . LEU B 2 102 ? 95.613  202.056 -2.337  1.00 40.94  ? 103 LEU B N   1 
ATOM   1765 C  CA  . LEU B 2 102 ? 94.608  202.857 -1.667  1.00 35.67  ? 103 LEU B CA  1 
ATOM   1766 C  C   . LEU B 2 102 ? 93.864  202.017 -0.650  1.00 34.47  ? 103 LEU B C   1 
ATOM   1767 O  O   . LEU B 2 102 ? 93.330  200.958 -0.979  1.00 39.01  ? 103 LEU B O   1 
ATOM   1768 C  CB  . LEU B 2 102 ? 93.614  203.421 -2.675  1.00 36.05  ? 103 LEU B CB  1 
ATOM   1769 C  CG  . LEU B 2 102 ? 92.526  204.290 -2.062  1.00 39.87  ? 103 LEU B CG  1 
ATOM   1770 C  CD1 . LEU B 2 102 ? 93.171  205.543 -1.510  1.00 31.22  ? 103 LEU B CD1 1 
ATOM   1771 C  CD2 . LEU B 2 102 ? 91.377  204.595 -3.054  1.00 34.46  ? 103 LEU B CD2 1 
ATOM   1772 N  N   . ALA B 2 103 ? 93.798  202.490 0.584   1.00 35.87  ? 104 ALA B N   1 
ATOM   1773 C  CA  . ALA B 2 103 ? 92.974  201.802 1.565   1.00 36.82  ? 104 ALA B CA  1 
ATOM   1774 C  C   . ALA B 2 103 ? 91.770  202.674 1.882   1.00 33.92  ? 104 ALA B C   1 
ATOM   1775 O  O   . ALA B 2 103 ? 91.931  203.814 2.290   1.00 32.26  ? 104 ALA B O   1 
ATOM   1776 C  CB  . ALA B 2 103 ? 93.765  201.491 2.830   1.00 34.13  ? 104 ALA B CB  1 
ATOM   1777 N  N   . ARG B 2 104 ? 90.571  202.149 1.664   1.00 35.69  ? 105 ARG B N   1 
ATOM   1778 C  CA  . ARG B 2 104 ? 89.356  202.810 2.138   1.00 34.03  ? 105 ARG B CA  1 
ATOM   1779 C  C   . ARG B 2 104 ? 88.877  202.039 3.336   1.00 39.91  ? 105 ARG B C   1 
ATOM   1780 O  O   . ARG B 2 104 ? 88.709  200.816 3.279   1.00 39.83  ? 105 ARG B O   1 
ATOM   1781 C  CB  . ARG B 2 104 ? 88.264  202.866 1.070   1.00 37.33  ? 105 ARG B CB  1 
ATOM   1782 C  CG  . ARG B 2 104 ? 88.448  203.957 0.033   1.00 42.95  ? 105 ARG B CG  1 
ATOM   1783 C  CD  . ARG B 2 104 ? 87.575  203.690 -1.156  1.00 41.52  ? 105 ARG B CD  1 
ATOM   1784 N  NE  . ARG B 2 104 ? 87.618  204.769 -2.126  1.00 45.52  ? 105 ARG B NE  1 
ATOM   1785 C  CZ  . ARG B 2 104 ? 86.876  204.793 -3.226  1.00 51.41  ? 105 ARG B CZ  1 
ATOM   1786 N  NH1 . ARG B 2 104 ? 86.033  203.805 -3.485  1.00 55.60  1 105 ARG B NH1 1 
ATOM   1787 N  NH2 . ARG B 2 104 ? 86.970  205.808 -4.061  1.00 58.21  ? 105 ARG B NH2 1 
ATOM   1788 N  N   . ILE B 2 105 ? 88.655  202.765 4.420   1.00 41.84  ? 106 ILE B N   1 
ATOM   1789 C  CA  . ILE B 2 105 ? 88.373  202.174 5.712   1.00 35.42  ? 106 ILE B CA  1 
ATOM   1790 C  C   . ILE B 2 105 ? 87.016  202.640 6.217   1.00 38.50  ? 106 ILE B C   1 
ATOM   1791 O  O   . ILE B 2 105 ? 86.748  203.836 6.235   1.00 45.12  ? 106 ILE B O   1 
ATOM   1792 C  CB  . ILE B 2 105 ? 89.465  202.563 6.718   1.00 42.11  ? 106 ILE B CB  1 
ATOM   1793 C  CG1 . ILE B 2 105 ? 90.854  202.313 6.113   1.00 38.18  ? 106 ILE B CG1 1 
ATOM   1794 C  CG2 . ILE B 2 105 ? 89.269  201.839 8.040   1.00 37.12  ? 106 ILE B CG2 1 
ATOM   1795 C  CD1 . ILE B 2 105 ? 92.008  202.662 7.047   1.00 35.83  ? 106 ILE B CD1 1 
ATOM   1796 N  N   . VAL B 2 106 ? 86.148  201.713 6.611   1.00 41.23  ? 107 VAL B N   1 
ATOM   1797 C  CA  . VAL B 2 106 ? 84.862  202.098 7.206   1.00 42.23  ? 107 VAL B CA  1 
ATOM   1798 C  C   . VAL B 2 106 ? 84.594  201.339 8.495   1.00 45.66  ? 107 VAL B C   1 
ATOM   1799 O  O   . VAL B 2 106 ? 84.861  200.142 8.618   1.00 48.49  ? 107 VAL B O   1 
ATOM   1800 C  CB  . VAL B 2 106 ? 83.659  201.869 6.237   1.00 40.24  ? 107 VAL B CB  1 
ATOM   1801 C  CG1 . VAL B 2 106 ? 83.777  202.771 5.022   1.00 36.40  ? 107 VAL B CG1 1 
ATOM   1802 C  CG2 . VAL B 2 106 ? 83.584  200.425 5.817   1.00 46.02  ? 107 VAL B CG2 1 
ATOM   1803 N  N   . GLN B 2 107 ? 84.065  202.036 9.479   1.00 49.67  ? 108 GLN B N   1 
ATOM   1804 C  CA  . GLN B 2 107 ? 83.672  201.334 10.679  1.00 52.14  ? 108 GLN B CA  1 
ATOM   1805 C  C   . GLN B 2 107 ? 82.333  200.675 10.396  1.00 52.25  ? 108 GLN B C   1 
ATOM   1806 O  O   . GLN B 2 107 ? 81.395  201.305 9.902   1.00 52.86  ? 108 GLN B O   1 
ATOM   1807 C  CB  . GLN B 2 107 ? 83.606  202.259 11.886  1.00 43.41  ? 108 GLN B CB  1 
ATOM   1808 C  CG  . GLN B 2 107 ? 83.362  201.512 13.165  1.00 51.59  ? 108 GLN B CG  1 
ATOM   1809 C  CD  . GLN B 2 107 ? 83.788  202.288 14.397  1.00 59.33  ? 108 GLN B CD  1 
ATOM   1810 O  OE1 . GLN B 2 107 ? 84.782  203.016 14.386  1.00 53.72  ? 108 GLN B OE1 1 
ATOM   1811 N  NE2 . GLN B 2 107 ? 83.035  202.128 15.474  1.00 75.36  ? 108 GLN B NE2 1 
ATOM   1812 N  N   . VAL B 2 108 ? 82.268  199.388 10.675  1.00 54.39  ? 109 VAL B N   1 
ATOM   1813 C  CA  . VAL B 2 108 ? 81.116  198.602 10.313  1.00 65.16  ? 109 VAL B CA  1 
ATOM   1814 C  C   . VAL B 2 108 ? 80.540  197.963 11.572  1.00 67.85  ? 109 VAL B C   1 
ATOM   1815 O  O   . VAL B 2 108 ? 79.483  197.341 11.539  1.00 81.65  ? 109 VAL B O   1 
ATOM   1816 C  CB  . VAL B 2 108 ? 81.498  197.554 9.234   1.00 62.14  ? 109 VAL B CB  1 
ATOM   1817 C  CG1 . VAL B 2 108 ? 82.319  196.421 9.837   1.00 57.98  ? 109 VAL B CG1 1 
ATOM   1818 C  CG2 . VAL B 2 108 ? 80.266  197.077 8.483   1.00 70.31  ? 109 VAL B CG2 1 
ATOM   1819 N  N   . GLY B 2 109 ? 81.218  198.176 12.694  1.00 66.31  ? 110 GLY B N   1 
ATOM   1820 C  CA  . GLY B 2 109 ? 80.796  197.609 13.963  1.00 69.22  ? 110 GLY B CA  1 
ATOM   1821 C  C   . GLY B 2 109 ? 81.127  198.580 15.074  1.00 69.12  ? 110 GLY B C   1 
ATOM   1822 O  O   . GLY B 2 109 ? 81.495  199.712 14.798  1.00 79.32  ? 110 GLY B O   1 
ATOM   1823 N  N   . GLU B 2 110 ? 81.023  198.155 16.326  1.00 70.73  ? 111 GLU B N   1 
ATOM   1824 C  CA  . GLU B 2 110 ? 81.383  199.039 17.431  1.00 73.61  ? 111 GLU B CA  1 
ATOM   1825 C  C   . GLU B 2 110 ? 82.897  198.982 17.630  1.00 67.36  ? 111 GLU B C   1 
ATOM   1826 O  O   . GLU B 2 110 ? 83.551  199.989 17.917  1.00 58.06  ? 111 GLU B O   1 
ATOM   1827 C  CB  . GLU B 2 110 ? 80.652  198.642 18.712  1.00 75.59  ? 111 GLU B CB  1 
ATOM   1828 C  CG  . GLU B 2 110 ? 80.911  199.573 19.883  1.00 82.02  ? 111 GLU B CG  1 
ATOM   1829 C  CD  . GLU B 2 110 ? 80.556  198.939 21.221  1.00 97.92  ? 111 GLU B CD  1 
ATOM   1830 O  OE1 . GLU B 2 110 ? 79.970  197.832 21.227  1.00 97.67  ? 111 GLU B OE1 1 
ATOM   1831 O  OE2 . GLU B 2 110 ? 80.862  199.552 22.269  1.00 93.68  1 111 GLU B OE2 1 
ATOM   1832 N  N   . ASN B 2 111 ? 83.440  197.779 17.504  1.00 61.50  ? 112 ASN B N   1 
ATOM   1833 C  CA  . ASN B 2 111 ? 84.879  197.587 17.444  1.00 60.12  ? 112 ASN B CA  1 
ATOM   1834 C  C   . ASN B 2 111 ? 85.224  196.780 16.228  1.00 60.26  ? 112 ASN B C   1 
ATOM   1835 O  O   . ASN B 2 111 ? 86.074  195.904 16.292  1.00 63.56  ? 112 ASN B O   1 
ATOM   1836 C  CB  . ASN B 2 111 ? 85.400  196.890 18.699  1.00 66.04  ? 112 ASN B CB  1 
ATOM   1837 C  CG  . ASN B 2 111 ? 85.360  197.781 19.905  1.00 70.77  ? 112 ASN B CG  1 
ATOM   1838 O  OD1 . ASN B 2 111 ? 86.253  198.602 20.111  1.00 76.58  ? 112 ASN B OD1 1 
ATOM   1839 N  ND2 . ASN B 2 111 ? 84.314  197.639 20.710  1.00 72.74  ? 112 ASN B ND2 1 
ATOM   1840 N  N   . LYS B 2 112 ? 84.531  197.048 15.126  1.00 62.80  ? 113 LYS B N   1 
ATOM   1841 C  CA  . LYS B 2 112 ? 84.772  196.316 13.891  1.00 59.42  ? 113 LYS B CA  1 
ATOM   1842 C  C   . LYS B 2 112 ? 85.022  197.271 12.743  1.00 56.21  ? 113 LYS B C   1 
ATOM   1843 O  O   . LYS B 2 112 ? 84.294  198.238 12.545  1.00 61.66  ? 113 LYS B O   1 
ATOM   1844 C  CB  . LYS B 2 112 ? 83.589  195.390 13.581  1.00 64.68  ? 113 LYS B CB  1 
ATOM   1845 C  CG  . LYS B 2 112 ? 83.396  194.281 14.625  1.00 76.48  ? 113 LYS B CG  1 
ATOM   1846 C  CD  . LYS B 2 112 ? 82.098  193.479 14.429  1.00 88.33  ? 113 LYS B CD  1 
ATOM   1847 C  CE  . LYS B 2 112 ? 80.882  194.177 15.050  1.00 86.85  ? 113 LYS B CE  1 
ATOM   1848 N  NZ  . LYS B 2 112 ? 79.598  193.479 14.724  1.00 101.13 1 113 LYS B NZ  1 
ATOM   1849 N  N   . THR B 2 113 ? 86.045  196.991 11.958  1.00 59.30  ? 114 THR B N   1 
ATOM   1850 C  CA  . THR B 2 113 ? 86.353  197.873 10.850  1.00 55.66  ? 114 THR B CA  1 
ATOM   1851 C  C   . THR B 2 113 ? 86.729  197.094 9.582   1.00 52.58  ? 114 THR B C   1 
ATOM   1852 O  O   . THR B 2 113 ? 87.308  196.004 9.639   1.00 50.78  ? 114 THR B O   1 
ATOM   1853 C  CB  . THR B 2 113 ? 87.466  198.877 11.264  1.00 47.68  ? 114 THR B CB  1 
ATOM   1854 O  OG1 . THR B 2 113 ? 87.662  199.838 10.231  1.00 55.68  ? 114 THR B OG1 1 
ATOM   1855 C  CG2 . THR B 2 113 ? 88.762  198.172 11.567  1.00 43.43  ? 114 THR B CG2 1 
ATOM   1856 N  N   . LEU B 2 114 ? 86.359  197.659 8.437   1.00 42.88  ? 115 LEU B N   1 
ATOM   1857 C  CA  . LEU B 2 114 ? 86.546  197.000 7.159   1.00 45.09  ? 115 LEU B CA  1 
ATOM   1858 C  C   . LEU B 2 114 ? 87.457  197.813 6.241   1.00 48.27  ? 115 LEU B C   1 
ATOM   1859 O  O   . LEU B 2 114 ? 87.384  199.040 6.194   1.00 42.19  ? 115 LEU B O   1 
ATOM   1860 C  CB  . LEU B 2 114 ? 85.187  196.763 6.503   1.00 53.24  ? 115 LEU B CB  1 
ATOM   1861 C  CG  . LEU B 2 114 ? 85.101  196.300 5.046   1.00 66.63  ? 115 LEU B CG  1 
ATOM   1862 C  CD1 . LEU B 2 114 ? 85.808  194.977 4.789   1.00 61.19  ? 115 LEU B CD1 1 
ATOM   1863 C  CD2 . LEU B 2 114 ? 83.630  196.215 4.645   1.00 77.54  ? 115 LEU B CD2 1 
ATOM   1864 N  N   . PHE B 2 115 ? 88.331  197.118 5.526   1.00 42.46  ? 116 PHE B N   1 
ATOM   1865 C  CA  . PHE B 2 115 ? 89.338  197.774 4.726   1.00 40.48  ? 116 PHE B CA  1 
ATOM   1866 C  C   . PHE B 2 115 ? 89.222  197.396 3.253   1.00 39.95  ? 116 PHE B C   1 
ATOM   1867 O  O   . PHE B 2 115 ? 89.435  196.249 2.895   1.00 46.96  ? 116 PHE B O   1 
ATOM   1868 C  CB  . PHE B 2 115 ? 90.734  197.420 5.233   1.00 41.02  ? 116 PHE B CB  1 
ATOM   1869 C  CG  . PHE B 2 115 ? 90.997  197.852 6.630   1.00 41.84  ? 116 PHE B CG  1 
ATOM   1870 C  CD1 . PHE B 2 115 ? 90.418  197.180 7.701   1.00 49.32  ? 116 PHE B CD1 1 
ATOM   1871 C  CD2 . PHE B 2 115 ? 91.823  198.941 6.886   1.00 39.60  ? 116 PHE B CD2 1 
ATOM   1872 C  CE1 . PHE B 2 115 ? 90.666  197.577 9.013   1.00 43.52  ? 116 PHE B CE1 1 
ATOM   1873 C  CE2 . PHE B 2 115 ? 92.070  199.359 8.200   1.00 41.83  ? 116 PHE B CE2 1 
ATOM   1874 C  CZ  . PHE B 2 115 ? 91.487  198.674 9.267   1.00 44.70  ? 116 PHE B CZ  1 
ATOM   1875 N  N   . ASP B 2 116 ? 88.918  198.371 2.408   1.00 36.78  ? 117 ASP B N   1 
ATOM   1876 C  CA  . ASP B 2 116 ? 88.843  198.168 0.959   1.00 41.36  ? 117 ASP B CA  1 
ATOM   1877 C  C   . ASP B 2 116 ? 90.212  198.491 0.388   1.00 39.35  ? 117 ASP B C   1 
ATOM   1878 O  O   . ASP B 2 116 ? 90.582  199.659 0.258   1.00 44.68  ? 117 ASP B O   1 
ATOM   1879 C  CB  . ASP B 2 116 ? 87.767  199.057 0.329   1.00 42.56  ? 117 ASP B CB  1 
ATOM   1880 C  CG  . ASP B 2 116 ? 87.661  198.887 -1.189  1.00 55.57  ? 117 ASP B CG  1 
ATOM   1881 O  OD1 . ASP B 2 116 ? 88.537  198.240 -1.808  1.00 56.93  ? 117 ASP B OD1 1 
ATOM   1882 O  OD2 . ASP B 2 116 ? 86.700  199.436 -1.775  1.00 57.50  1 117 ASP B OD2 1 
ATOM   1883 N  N   . ILE B 2 117 ? 90.983  197.455 0.089   1.00 38.87  ? 118 ILE B N   1 
ATOM   1884 C  CA  . ILE B 2 117 ? 92.349  197.648 -0.368  1.00 44.35  ? 118 ILE B CA  1 
ATOM   1885 C  C   . ILE B 2 117 ? 92.472  197.370 -1.846  1.00 42.47  ? 118 ILE B C   1 
ATOM   1886 O  O   . ILE B 2 117 ? 92.019  196.339 -2.327  1.00 47.51  ? 118 ILE B O   1 
ATOM   1887 C  CB  . ILE B 2 117 ? 93.342  196.742 0.368   1.00 48.99  ? 118 ILE B CB  1 
ATOM   1888 C  CG1 . ILE B 2 117 ? 93.038  196.744 1.857   1.00 41.32  ? 118 ILE B CG1 1 
ATOM   1889 C  CG2 . ILE B 2 117 ? 94.785  197.145 0.039   1.00 40.04  ? 118 ILE B CG2 1 
ATOM   1890 C  CD1 . ILE B 2 117 ? 93.098  198.101 2.444   1.00 45.37  ? 118 ILE B CD1 1 
ATOM   1891 N  N   . THR B 2 118 ? 93.082  198.299 -2.559  1.00 41.62  ? 119 THR B N   1 
ATOM   1892 C  CA  . THR B 2 118 ? 93.406  198.099 -3.961  1.00 40.30  ? 119 THR B CA  1 
ATOM   1893 C  C   . THR B 2 118 ? 94.892  198.330 -4.176  1.00 40.53  ? 119 THR B C   1 
ATOM   1894 O  O   . THR B 2 118 ? 95.471  199.246 -3.619  1.00 39.53  ? 119 THR B O   1 
ATOM   1895 C  CB  . THR B 2 118 ? 92.598  199.033 -4.880  1.00 46.47  ? 119 THR B CB  1 
ATOM   1896 O  OG1 . THR B 2 118 ? 92.641  200.369 -4.356  1.00 44.48  ? 119 THR B OG1 1 
ATOM   1897 C  CG2 . THR B 2 118 ? 91.142  198.582 -4.979  1.00 42.13  ? 119 THR B CG2 1 
ATOM   1898 N  N   . VAL B 2 119 ? 95.512  197.484 -4.980  1.00 48.25  ? 120 VAL B N   1 
ATOM   1899 C  CA  . VAL B 2 119 ? 96.908  197.675 -5.337  1.00 38.67  ? 120 VAL B CA  1 
ATOM   1900 C  C   . VAL B 2 119 ? 97.007  197.700 -6.856  1.00 49.31  ? 120 VAL B C   1 
ATOM   1901 O  O   . VAL B 2 119 ? 96.303  196.956 -7.551  1.00 50.86  ? 120 VAL B O   1 
ATOM   1902 C  CB  . VAL B 2 119 ? 97.807  196.566 -4.720  1.00 42.43  ? 120 VAL B CB  1 
ATOM   1903 C  CG1 . VAL B 2 119 ? 99.244  196.710 -5.153  1.00 42.54  ? 120 VAL B CG1 1 
ATOM   1904 C  CG2 . VAL B 2 119 ? 97.706  196.595 -3.187  1.00 43.35  ? 120 VAL B CG2 1 
ATOM   1905 N  N   . ASN B 2 120 ? 97.854  198.582 -7.377  1.00 48.32  ? 121 ASN B N   1 
ATOM   1906 C  CA  . ASN B 2 120 ? 97.987  198.702 -8.815  1.00 45.98  ? 121 ASN B CA  1 
ATOM   1907 C  C   . ASN B 2 120 ? 99.304  199.351 -9.184  1.00 47.36  ? 121 ASN B C   1 
ATOM   1908 O  O   . ASN B 2 120 ? 99.648  200.400 -8.655  1.00 49.87  ? 121 ASN B O   1 
ATOM   1909 C  CB  . ASN B 2 120 ? 96.811  199.498 -9.396  1.00 43.63  ? 121 ASN B CB  1 
ATOM   1910 C  CG  . ASN B 2 120 ? 96.653  199.282 -10.897 1.00 62.86  ? 121 ASN B CG  1 
ATOM   1911 O  OD1 . ASN B 2 120 ? 97.363  198.468 -11.487 1.00 60.00  ? 121 ASN B OD1 1 
ATOM   1912 N  ND2 . ASN B 2 120 ? 95.700  199.984 -11.512 1.00 57.50  ? 121 ASN B ND2 1 
ATOM   1913 N  N   . GLY B 2 121 ? 100.046 198.711 -10.086 1.00 49.06  ? 122 GLY B N   1 
ATOM   1914 C  CA  . GLY B 2 121 ? 101.293 199.259 -10.590 1.00 45.76  ? 122 GLY B CA  1 
ATOM   1915 C  C   . GLY B 2 121 ? 102.550 198.782 -9.877  1.00 47.66  ? 122 GLY B C   1 
ATOM   1916 O  O   . GLY B 2 121 ? 103.626 199.363 -10.048 1.00 50.20  ? 122 GLY B O   1 
ATOM   1917 N  N   . VAL B 2 122 ? 102.427 197.723 -9.084  1.00 50.74  ? 123 VAL B N   1 
ATOM   1918 C  CA  . VAL B 2 122 ? 103.598 197.117 -8.458  1.00 54.93  ? 123 VAL B CA  1 
ATOM   1919 C  C   . VAL B 2 122 ? 104.340 196.256 -9.489  1.00 56.19  ? 123 VAL B C   1 
ATOM   1920 O  O   . VAL B 2 122 ? 103.710 195.630 -10.337 1.00 52.40  ? 123 VAL B O   1 
ATOM   1921 C  CB  . VAL B 2 122 ? 103.213 196.277 -7.238  1.00 43.77  ? 123 VAL B CB  1 
ATOM   1922 C  CG1 . VAL B 2 122 ? 102.813 197.185 -6.103  1.00 45.18  ? 123 VAL B CG1 1 
ATOM   1923 C  CG2 . VAL B 2 122 ? 102.080 195.332 -7.593  1.00 52.28  ? 123 VAL B CG2 1 
ATOM   1924 N  N   . PRO B 2 123 ? 105.682 196.227 -9.416  1.00 52.93  ? 124 PRO B N   1 
ATOM   1925 C  CA  . PRO B 2 123 ? 106.535 195.532 -10.396 1.00 64.84  ? 124 PRO B CA  1 
ATOM   1926 C  C   . PRO B 2 123 ? 106.557 194.001 -10.271 1.00 65.56  ? 124 PRO B C   1 
ATOM   1927 O  O   . PRO B 2 123 ? 106.614 193.308 -11.280 1.00 68.60  ? 124 PRO B O   1 
ATOM   1928 C  CB  . PRO B 2 123 ? 107.936 196.088 -10.098 1.00 59.67  ? 124 PRO B CB  1 
ATOM   1929 C  CG  . PRO B 2 123 ? 107.735 197.221 -9.157  1.00 56.03  ? 124 PRO B CG  1 
ATOM   1930 C  CD  . PRO B 2 123 ? 106.490 196.916 -8.403  1.00 48.60  ? 124 PRO B CD  1 
ATOM   1931 N  N   . GLU B 2 124 ? 106.520 193.487 -9.047  1.00 66.24  ? 125 GLU B N   1 
ATOM   1932 C  CA  . GLU B 2 124 ? 106.584 192.048 -8.802  1.00 56.46  ? 125 GLU B CA  1 
ATOM   1933 C  C   . GLU B 2 124 ? 105.237 191.484 -8.396  1.00 58.95  ? 125 GLU B C   1 
ATOM   1934 O  O   . GLU B 2 124 ? 104.646 191.935 -7.411  1.00 59.81  ? 125 GLU B O   1 
ATOM   1935 C  CB  . GLU B 2 124 ? 107.602 191.727 -7.696  1.00 57.12  ? 125 GLU B CB  1 
ATOM   1936 C  CG  . GLU B 2 124 ? 109.026 192.236 -7.943  1.00 68.62  ? 125 GLU B CG  1 
ATOM   1937 C  CD  . GLU B 2 124 ? 110.067 191.607 -7.002  1.00 69.83  ? 125 GLU B CD  1 
ATOM   1938 O  OE1 . GLU B 2 124 ? 109.672 191.095 -5.933  1.00 60.71  ? 125 GLU B OE1 1 
ATOM   1939 O  OE2 . GLU B 2 124 ? 111.280 191.622 -7.334  1.00 69.00  1 125 GLU B OE2 1 
ATOM   1940 N  N   . ALA B 2 125 ? 104.764 190.490 -9.140  1.00 53.82  ? 126 ALA B N   1 
ATOM   1941 C  CA  . ALA B 2 125 ? 103.603 189.712 -8.726  1.00 50.72  ? 126 ALA B CA  1 
ATOM   1942 C  C   . ALA B 2 125 ? 103.913 189.037 -7.394  1.00 50.32  ? 126 ALA B C   1 
ATOM   1943 O  O   . ALA B 2 125 ? 105.080 188.814 -7.062  1.00 57.41  ? 126 ALA B O   1 
ATOM   1944 C  CB  . ALA B 2 125 ? 103.233 188.683 -9.773  1.00 51.74  ? 126 ALA B CB  1 
ATOM   1945 N  N   . GLY B 2 126 ? 102.879 188.744 -6.613  1.00 51.28  ? 127 GLY B N   1 
ATOM   1946 C  CA  . GLY B 2 126 ? 103.096 188.159 -5.304  1.00 56.10  ? 127 GLY B CA  1 
ATOM   1947 C  C   . GLY B 2 126 ? 102.017 188.433 -4.277  1.00 53.12  ? 127 GLY B C   1 
ATOM   1948 O  O   . GLY B 2 126 ? 101.047 189.144 -4.529  1.00 47.50  ? 127 GLY B O   1 
ATOM   1949 N  N   . ASN B 2 127 ? 102.165 187.816 -3.114  1.00 55.21  ? 128 ASN B N   1 
ATOM   1950 C  CA  . ASN B 2 127 ? 101.341 188.175 -1.971  1.00 57.80  ? 128 ASN B CA  1 
ATOM   1951 C  C   . ASN B 2 127 ? 101.948 189.364 -1.233  1.00 60.75  ? 128 ASN B C   1 
ATOM   1952 O  O   . ASN B 2 127 ? 103.092 189.293 -0.781  1.00 54.31  ? 128 ASN B O   1 
ATOM   1953 C  CB  . ASN B 2 127 ? 101.188 186.991 -1.019  1.00 60.31  ? 128 ASN B CB  1 
ATOM   1954 C  CG  . ASN B 2 127 ? 100.291 185.905 -1.577  1.00 62.09  ? 128 ASN B CG  1 
ATOM   1955 O  OD1 . ASN B 2 127 ? 99.234  186.181 -2.144  1.00 63.71  ? 128 ASN B OD1 1 
ATOM   1956 N  ND2 . ASN B 2 127 ? 100.719 184.664 -1.433  1.00 61.62  ? 128 ASN B ND2 1 
ATOM   1957 N  N   . TYR B 2 128 ? 101.181 190.445 -1.098  1.00 59.02  ? 129 TYR B N   1 
ATOM   1958 C  CA  . TYR B 2 128 ? 101.645 191.616 -0.343  1.00 51.24  ? 129 TYR B CA  1 
ATOM   1959 C  C   . TYR B 2 128 ? 100.975 191.611 1.032   1.00 49.80  ? 129 TYR B C   1 
ATOM   1960 O  O   . TYR B 2 128 ? 99.820  191.210 1.174   1.00 48.97  ? 129 TYR B O   1 
ATOM   1961 C  CB  . TYR B 2 128 ? 101.366 192.914 -1.125  1.00 39.36  ? 129 TYR B CB  1 
ATOM   1962 C  CG  . TYR B 2 128 ? 102.275 193.093 -2.337  1.00 45.48  ? 129 TYR B CG  1 
ATOM   1963 C  CD1 . TYR B 2 128 ? 102.122 192.299 -3.461  1.00 48.62  ? 129 TYR B CD1 1 
ATOM   1964 C  CD2 . TYR B 2 128 ? 103.283 194.045 -2.351  1.00 50.32  ? 129 TYR B CD2 1 
ATOM   1965 C  CE1 . TYR B 2 128 ? 102.939 192.439 -4.561  1.00 53.25  ? 129 TYR B CE1 1 
ATOM   1966 C  CE2 . TYR B 2 128 ? 104.118 194.197 -3.458  1.00 45.64  ? 129 TYR B CE2 1 
ATOM   1967 C  CZ  . TYR B 2 128 ? 103.938 193.387 -4.563  1.00 55.99  ? 129 TYR B CZ  1 
ATOM   1968 O  OH  . TYR B 2 128 ? 104.743 193.516 -5.685  1.00 58.60  ? 129 TYR B OH  1 
ATOM   1969 N  N   . HIS B 2 129 ? 101.710 192.030 2.055   1.00 47.59  ? 130 HIS B N   1 
ATOM   1970 C  CA  . HIS B 2 129 ? 101.201 191.930 3.414   1.00 49.53  ? 130 HIS B CA  1 
ATOM   1971 C  C   . HIS B 2 129 ? 100.893 193.290 4.011   1.00 48.00  ? 130 HIS B C   1 
ATOM   1972 O  O   . HIS B 2 129 ? 101.732 194.190 4.008   1.00 47.25  ? 130 HIS B O   1 
ATOM   1973 C  CB  . HIS B 2 129 ? 102.213 191.184 4.268   1.00 51.67  ? 130 HIS B CB  1 
ATOM   1974 C  CG  . HIS B 2 129 ? 102.685 189.906 3.646   1.00 64.97  ? 130 HIS B CG  1 
ATOM   1975 N  ND1 . HIS B 2 129 ? 101.862 188.813 3.475   1.00 65.53  ? 130 HIS B ND1 1 
ATOM   1976 C  CD2 . HIS B 2 129 ? 103.889 189.555 3.135   1.00 64.97  ? 130 HIS B CD2 1 
ATOM   1977 C  CE1 . HIS B 2 129 ? 102.542 187.839 2.899   1.00 68.13  ? 130 HIS B CE1 1 
ATOM   1978 N  NE2 . HIS B 2 129 ? 103.775 188.262 2.683   1.00 71.20  ? 130 HIS B NE2 1 
ATOM   1979 N  N   . ALA B 2 130 ? 99.699  193.430 4.565   1.00 42.31  ? 131 ALA B N   1 
ATOM   1980 C  CA  . ALA B 2 130 ? 99.284  194.724 5.089   1.00 47.46  ? 131 ALA B CA  1 
ATOM   1981 C  C   . ALA B 2 130 ? 99.451  194.761 6.584   1.00 43.50  ? 131 ALA B C   1 
ATOM   1982 O  O   . ALA B 2 130 ? 99.135  193.798 7.267   1.00 48.27  ? 131 ALA B O   1 
ATOM   1983 C  CB  . ALA B 2 130 ? 97.832  195.023 4.709   1.00 35.59  ? 131 ALA B CB  1 
ATOM   1984 N  N   . SER B 2 131 ? 99.953  195.870 7.098   1.00 38.58  ? 132 SER B N   1 
ATOM   1985 C  CA  . SER B 2 131 ? 100.018 196.050 8.540   1.00 45.99  ? 132 SER B CA  1 
ATOM   1986 C  C   . SER B 2 131 ? 99.743  197.510 8.906   1.00 47.01  ? 132 SER B C   1 
ATOM   1987 O  O   . SER B 2 131 ? 99.815  198.386 8.065   1.00 44.54  ? 132 SER B O   1 
ATOM   1988 C  CB  . SER B 2 131 ? 101.383 195.608 9.095   1.00 50.49  ? 132 SER B CB  1 
ATOM   1989 O  OG  . SER B 2 131 ? 102.448 196.394 8.588   1.00 48.18  ? 132 SER B OG  1 
ATOM   1990 N  N   . ILE B 2 132 ? 99.406  197.770 10.161  1.00 41.61  ? 133 ILE B N   1 
ATOM   1991 C  CA  . ILE B 2 132 ? 99.309  199.132 10.612  1.00 34.37  ? 133 ILE B CA  1 
ATOM   1992 C  C   . ILE B 2 132 ? 100.440 199.374 11.574  1.00 45.64  ? 133 ILE B C   1 
ATOM   1993 O  O   . ILE B 2 132 ? 100.607 198.610 12.506  1.00 51.96  ? 133 ILE B O   1 
ATOM   1994 C  CB  . ILE B 2 132 ? 97.968  199.417 11.287  1.00 44.86  ? 133 ILE B CB  1 
ATOM   1995 C  CG1 . ILE B 2 132 ? 96.842  199.271 10.270  1.00 42.43  ? 133 ILE B CG1 1 
ATOM   1996 C  CG2 . ILE B 2 132 ? 97.949  200.817 11.918  1.00 34.72  ? 133 ILE B CG2 1 
ATOM   1997 C  CD1 . ILE B 2 132 ? 95.513  199.634 10.808  1.00 45.36  ? 133 ILE B CD1 1 
ATOM   1998 N  N   . HIS B 2 133 ? 101.227 200.421 11.357  1.00 38.16  ? 134 HIS B N   1 
ATOM   1999 C  CA  . HIS B 2 133 ? 102.316 200.715 12.274  1.00 40.29  ? 134 HIS B CA  1 
ATOM   2000 C  C   . HIS B 2 133 ? 101.929 201.784 13.288  1.00 42.11  ? 134 HIS B C   1 
ATOM   2001 O  O   . HIS B 2 133 ? 100.929 202.461 13.128  1.00 41.23  ? 134 HIS B O   1 
ATOM   2002 C  CB  . HIS B 2 133 ? 103.576 201.114 11.522  1.00 42.67  ? 134 HIS B CB  1 
ATOM   2003 C  CG  . HIS B 2 133 ? 104.262 199.961 10.869  1.00 45.98  ? 134 HIS B CG  1 
ATOM   2004 N  ND1 . HIS B 2 133 ? 105.577 199.644 11.122  1.00 47.24  ? 134 HIS B ND1 1 
ATOM   2005 C  CD2 . HIS B 2 133 ? 103.807 199.028 10.001  1.00 46.23  ? 134 HIS B CD2 1 
ATOM   2006 C  CE1 . HIS B 2 133 ? 105.910 198.573 10.425  1.00 43.12  ? 134 HIS B CE1 1 
ATOM   2007 N  NE2 . HIS B 2 133 ? 104.853 198.177 9.739   1.00 42.16  ? 134 HIS B NE2 1 
ATOM   2008 N  N   . GLU B 2 134 ? 102.687 201.874 14.371  1.00 47.36  ? 135 GLU B N   1 
ATOM   2009 C  CA  . GLU B 2 134 ? 102.244 202.674 15.502  1.00 51.29  ? 135 GLU B CA  1 
ATOM   2010 C  C   . GLU B 2 134 ? 102.155 204.153 15.157  1.00 42.78  ? 135 GLU B C   1 
ATOM   2011 O  O   . GLU B 2 134 ? 101.190 204.816 15.507  1.00 43.68  ? 135 GLU B O   1 
ATOM   2012 C  CB  . GLU B 2 134 ? 103.158 202.487 16.704  1.00 42.76  ? 135 GLU B CB  1 
ATOM   2013 C  CG  . GLU B 2 134 ? 102.603 203.211 17.922  1.00 67.51  ? 135 GLU B CG  1 
ATOM   2014 C  CD  . GLU B 2 134 ? 103.289 202.841 19.223  1.00 84.19  ? 135 GLU B CD  1 
ATOM   2015 O  OE1 . GLU B 2 134 ? 104.427 202.317 19.184  1.00 76.16  ? 135 GLU B OE1 1 
ATOM   2016 O  OE2 . GLU B 2 134 ? 102.673 203.080 20.285  1.00 84.40  1 135 GLU B OE2 1 
ATOM   2017 N  N   . LYS B 2 135 ? 103.150 204.646 14.437  1.00 36.44  ? 136 LYS B N   1 
ATOM   2018 C  CA  . LYS B 2 135 ? 103.276 206.068 14.197  1.00 44.17  ? 136 LYS B CA  1 
ATOM   2019 C  C   . LYS B 2 135 ? 102.978 206.456 12.750  1.00 45.61  ? 136 LYS B C   1 
ATOM   2020 O  O   . LYS B 2 135 ? 103.272 205.711 11.816  1.00 47.17  ? 136 LYS B O   1 
ATOM   2021 C  CB  . LYS B 2 135 ? 104.670 206.520 14.587  1.00 41.72  ? 136 LYS B CB  1 
ATOM   2022 C  CG  . LYS B 2 135 ? 104.957 206.294 16.064  1.00 45.99  ? 136 LYS B CG  1 
ATOM   2023 C  CD  . LYS B 2 135 ? 106.313 206.883 16.454  1.00 62.87  ? 136 LYS B CD  1 
ATOM   2024 C  CE  . LYS B 2 135 ? 107.436 206.222 15.669  1.00 61.37  ? 136 LYS B CE  1 
ATOM   2025 N  NZ  . LYS B 2 135 ? 108.625 207.113 15.497  1.00 67.17  1 136 LYS B NZ  1 
ATOM   2026 N  N   . GLY B 2 136 ? 102.362 207.622 12.591  1.00 40.32  ? 137 GLY B N   1 
ATOM   2027 C  CA  . GLY B 2 136 ? 102.053 208.176 11.286  1.00 40.08  ? 137 GLY B CA  1 
ATOM   2028 C  C   . GLY B 2 136 ? 103.118 209.144 10.826  1.00 41.30  ? 137 GLY B C   1 
ATOM   2029 O  O   . GLY B 2 136 ? 102.803 210.223 10.327  1.00 41.10  ? 137 GLY B O   1 
ATOM   2030 N  N   . ASP B 2 137 ? 104.373 208.761 11.047  1.00 37.86  ? 138 ASP B N   1 
ATOM   2031 C  CA  . ASP B 2 137 ? 105.545 209.513 10.619  1.00 43.63  ? 138 ASP B CA  1 
ATOM   2032 C  C   . ASP B 2 137 ? 106.180 208.860 9.384   1.00 43.36  ? 138 ASP B C   1 
ATOM   2033 O  O   . ASP B 2 137 ? 106.944 207.910 9.511   1.00 42.71  ? 138 ASP B O   1 
ATOM   2034 C  CB  . ASP B 2 137 ? 106.559 209.598 11.775  1.00 38.76  ? 138 ASP B CB  1 
ATOM   2035 C  CG  . ASP B 2 137 ? 107.791 210.434 11.440  1.00 45.68  ? 138 ASP B CG  1 
ATOM   2036 O  OD1 . ASP B 2 137 ? 108.082 210.673 10.245  1.00 44.41  ? 138 ASP B OD1 1 
ATOM   2037 O  OD2 . ASP B 2 137 ? 108.490 210.838 12.390  1.00 47.92  1 138 ASP B OD2 1 
ATOM   2038 N  N   . VAL B 2 138 ? 105.905 209.405 8.201   1.00 39.47  ? 139 VAL B N   1 
ATOM   2039 C  CA  . VAL B 2 138 ? 106.433 208.839 6.961   1.00 38.71  ? 139 VAL B CA  1 
ATOM   2040 C  C   . VAL B 2 138 ? 107.603 209.678 6.411   1.00 41.56  ? 139 VAL B C   1 
ATOM   2041 O  O   . VAL B 2 138 ? 107.941 209.589 5.231   1.00 47.06  ? 139 VAL B O   1 
ATOM   2042 C  CB  . VAL B 2 138 ? 105.319 208.686 5.861   1.00 45.19  ? 139 VAL B CB  1 
ATOM   2043 C  CG1 . VAL B 2 138 ? 104.202 207.713 6.315   1.00 33.80  ? 139 VAL B CG1 1 
ATOM   2044 C  CG2 . VAL B 2 138 ? 104.722 210.041 5.468   1.00 33.85  ? 139 VAL B CG2 1 
ATOM   2045 N  N   . SER B 2 139 ? 108.244 210.471 7.269   1.00 41.94  ? 140 SER B N   1 
ATOM   2046 C  CA  . SER B 2 139 ? 109.431 211.224 6.845   1.00 40.73  ? 140 SER B CA  1 
ATOM   2047 C  C   . SER B 2 139 ? 110.550 210.285 6.364   1.00 45.63  ? 140 SER B C   1 
ATOM   2048 O  O   . SER B 2 139 ? 111.254 210.586 5.405   1.00 47.29  ? 140 SER B O   1 
ATOM   2049 C  CB  . SER B 2 139 ? 109.955 212.122 7.976   1.00 44.19  ? 140 SER B CB  1 
ATOM   2050 O  OG  . SER B 2 139 ? 110.331 211.381 9.140   1.00 48.80  ? 140 SER B OG  1 
ATOM   2051 N  N   . LYS B 2 140 ? 110.703 209.143 7.023   1.00 47.45  ? 141 LYS B N   1 
ATOM   2052 C  CA  . LYS B 2 140 ? 111.742 208.179 6.651   1.00 54.75  ? 141 LYS B CA  1 
ATOM   2053 C  C   . LYS B 2 140 ? 111.158 206.884 6.066   1.00 51.83  ? 141 LYS B C   1 
ATOM   2054 O  O   . LYS B 2 140 ? 111.760 205.812 6.190   1.00 50.19  ? 141 LYS B O   1 
ATOM   2055 C  CB  . LYS B 2 140 ? 112.602 207.840 7.878   1.00 49.28  ? 141 LYS B CB  1 
ATOM   2056 C  CG  . LYS B 2 140 ? 113.522 208.969 8.383   1.00 52.50  ? 141 LYS B CG  1 
ATOM   2057 C  CD  . LYS B 2 140 ? 113.613 208.912 9.911   1.00 71.68  ? 141 LYS B CD  1 
ATOM   2058 C  CE  . LYS B 2 140 ? 114.955 209.382 10.462  1.00 73.72  ? 141 LYS B CE  1 
ATOM   2059 N  NZ  . LYS B 2 140 ? 115.079 209.083 11.928  1.00 72.41  1 141 LYS B NZ  1 
ATOM   2060 N  N   . GLY B 2 141 ? 109.977 206.969 5.458   1.00 47.24  ? 142 GLY B N   1 
ATOM   2061 C  CA  . GLY B 2 141 ? 109.336 205.779 4.933   1.00 41.34  ? 142 GLY B CA  1 
ATOM   2062 C  C   . GLY B 2 141 ? 108.977 204.858 6.086   1.00 45.11  ? 142 GLY B C   1 
ATOM   2063 O  O   . GLY B 2 141 ? 108.761 205.328 7.201   1.00 41.32  ? 142 GLY B O   1 
ATOM   2064 N  N   . VAL B 2 142 ? 108.974 203.547 5.842   1.00 46.24  ? 143 VAL B N   1 
ATOM   2065 C  CA  . VAL B 2 142 ? 108.591 202.592 6.876   1.00 45.56  ? 143 VAL B CA  1 
ATOM   2066 C  C   . VAL B 2 142 ? 109.397 202.732 8.171   1.00 44.18  ? 143 VAL B C   1 
ATOM   2067 O  O   . VAL B 2 142 ? 108.853 202.596 9.268   1.00 44.67  ? 143 VAL B O   1 
ATOM   2068 C  CB  . VAL B 2 142 ? 108.739 201.148 6.379   1.00 45.67  ? 143 VAL B CB  1 
ATOM   2069 C  CG1 . VAL B 2 142 ? 108.212 200.172 7.440   1.00 46.82  ? 143 VAL B CG1 1 
ATOM   2070 C  CG2 . VAL B 2 142 ? 107.996 200.974 5.103   1.00 43.76  ? 143 VAL B CG2 1 
ATOM   2071 N  N   . GLU B 2 143 ? 110.683 203.028 8.037   1.00 51.36  ? 144 GLU B N   1 
ATOM   2072 C  CA  . GLU B 2 143 ? 111.560 203.151 9.193   1.00 44.99  ? 144 GLU B CA  1 
ATOM   2073 C  C   . GLU B 2 143 ? 111.003 204.090 10.280  1.00 53.92  ? 144 GLU B C   1 
ATOM   2074 O  O   . GLU B 2 143 ? 111.114 203.797 11.464  1.00 58.25  ? 144 GLU B O   1 
ATOM   2075 C  CB  . GLU B 2 143 ? 112.938 203.638 8.757   1.00 49.61  ? 144 GLU B CB  1 
ATOM   2076 C  CG  . GLU B 2 143 ? 113.802 204.093 9.922   1.00 69.53  ? 144 GLU B CG  1 
ATOM   2077 C  CD  . GLU B 2 143 ? 115.113 204.714 9.480   1.00 81.08  ? 144 GLU B CD  1 
ATOM   2078 O  OE1 . GLU B 2 143 ? 115.698 205.494 10.272  1.00 84.17  ? 144 GLU B OE1 1 
ATOM   2079 O  OE2 . GLU B 2 143 ? 115.548 204.427 8.340   1.00 86.44  1 144 GLU B OE2 1 
ATOM   2080 N  N   . SER B 2 144 ? 110.385 205.202 9.891   1.00 47.48  ? 145 SER B N   1 
ATOM   2081 C  CA  . SER B 2 144 ? 109.954 206.173 10.892  1.00 41.98  ? 145 SER B CA  1 
ATOM   2082 C  C   . SER B 2 144 ? 108.573 205.895 11.482  1.00 41.07  ? 145 SER B C   1 
ATOM   2083 O  O   . SER B 2 144 ? 108.171 206.591 12.408  1.00 43.29  ? 145 SER B O   1 
ATOM   2084 C  CB  . SER B 2 144 ? 109.979 207.595 10.306  1.00 45.83  ? 145 SER B CB  1 
ATOM   2085 O  OG  . SER B 2 144 ? 109.355 207.670 9.025   1.00 44.15  ? 145 SER B OG  1 
ATOM   2086 N  N   . THR B 2 145 ? 107.865 204.874 10.984  1.00 39.46  ? 146 THR B N   1 
ATOM   2087 C  CA  . THR B 2 145 ? 106.513 204.564 11.478  1.00 40.98  ? 146 THR B CA  1 
ATOM   2088 C  C   . THR B 2 145 ? 106.530 203.708 12.736  1.00 46.95  ? 146 THR B C   1 
ATOM   2089 O  O   . THR B 2 145 ? 105.475 203.393 13.297  1.00 48.51  ? 146 THR B O   1 
ATOM   2090 C  CB  . THR B 2 145 ? 105.657 203.820 10.438  1.00 41.87  ? 146 THR B CB  1 
ATOM   2091 O  OG1 . THR B 2 145 ? 106.177 202.499 10.240  1.00 43.83  ? 146 THR B OG1 1 
ATOM   2092 C  CG2 . THR B 2 145 ? 105.643 204.574 9.113   1.00 44.60  ? 146 THR B CG2 1 
ATOM   2093 N  N   . GLY B 2 146 ? 107.717 203.313 13.175  1.00 45.02  ? 147 GLY B N   1 
ATOM   2094 C  CA  . GLY B 2 146 ? 107.818 202.537 14.390  1.00 47.95  ? 147 GLY B CA  1 
ATOM   2095 C  C   . GLY B 2 146 ? 107.313 201.117 14.237  1.00 48.40  ? 147 GLY B C   1 
ATOM   2096 O  O   . GLY B 2 146 ? 107.295 200.563 13.145  1.00 43.54  ? 147 GLY B O   1 
ATOM   2097 N  N   . LYS B 2 147 ? 106.869 200.546 15.348  1.00 51.76  ? 148 LYS B N   1 
ATOM   2098 C  CA  . LYS B 2 147 ? 106.593 199.121 15.438  1.00 57.78  ? 148 LYS B CA  1 
ATOM   2099 C  C   . LYS B 2 147 ? 105.289 198.734 14.732  1.00 53.78  ? 148 LYS B C   1 
ATOM   2100 O  O   . LYS B 2 147 ? 104.430 199.574 14.505  1.00 50.79  ? 148 LYS B O   1 
ATOM   2101 C  CB  . LYS B 2 147 ? 106.517 198.724 16.909  1.00 60.79  ? 148 LYS B CB  1 
ATOM   2102 C  CG  . LYS B 2 147 ? 107.391 199.589 17.823  1.00 76.85  ? 148 LYS B CG  1 
ATOM   2103 C  CD  . LYS B 2 147 ? 108.889 199.385 17.632  1.00 78.71  ? 148 LYS B CD  1 
ATOM   2104 C  CE  . LYS B 2 147 ? 109.678 200.216 18.656  1.00 82.30  ? 148 LYS B CE  1 
ATOM   2105 N  NZ  . LYS B 2 147 ? 109.361 201.689 18.615  1.00 70.91  1 148 LYS B NZ  1 
ATOM   2106 N  N   . VAL B 2 148 ? 105.151 197.468 14.357  1.00 46.84  ? 149 VAL B N   1 
ATOM   2107 C  CA  . VAL B 2 148 ? 103.857 196.972 13.923  1.00 49.15  ? 149 VAL B CA  1 
ATOM   2108 C  C   . VAL B 2 148 ? 102.881 197.115 15.090  1.00 54.96  ? 149 VAL B C   1 
ATOM   2109 O  O   . VAL B 2 148 ? 103.233 196.891 16.249  1.00 54.49  ? 149 VAL B O   1 
ATOM   2110 C  CB  . VAL B 2 148 ? 103.918 195.507 13.445  1.00 43.89  ? 149 VAL B CB  1 
ATOM   2111 C  CG1 . VAL B 2 148 ? 102.540 195.019 13.079  1.00 42.43  ? 149 VAL B CG1 1 
ATOM   2112 C  CG2 . VAL B 2 148 ? 104.830 195.395 12.235  1.00 42.53  ? 149 VAL B CG2 1 
ATOM   2113 N  N   . TRP B 2 149 ? 101.667 197.544 14.779  1.00 50.43  ? 150 TRP B N   1 
ATOM   2114 C  CA  . TRP B 2 149 ? 100.652 197.820 15.786  1.00 47.76  ? 150 TRP B CA  1 
ATOM   2115 C  C   . TRP B 2 149 ? 99.492  196.886 15.541  1.00 52.29  ? 150 TRP B C   1 
ATOM   2116 O  O   . TRP B 2 149 ? 98.838  196.443 16.476  1.00 45.75  ? 150 TRP B O   1 
ATOM   2117 C  CB  . TRP B 2 149 ? 100.209 199.280 15.706  1.00 46.77  ? 150 TRP B CB  1 
ATOM   2118 C  CG  . TRP B 2 149 ? 99.212  199.720 16.718  1.00 49.42  ? 150 TRP B CG  1 
ATOM   2119 C  CD1 . TRP B 2 149 ? 99.465  200.114 17.999  1.00 56.28  ? 150 TRP B CD1 1 
ATOM   2120 C  CD2 . TRP B 2 149 ? 97.810  199.888 16.517  1.00 48.50  ? 150 TRP B CD2 1 
ATOM   2121 N  NE1 . TRP B 2 149 ? 98.301  200.490 18.618  1.00 53.79  ? 150 TRP B NE1 1 
ATOM   2122 C  CE2 . TRP B 2 149 ? 97.267  200.363 17.729  1.00 51.70  ? 150 TRP B CE2 1 
ATOM   2123 C  CE3 . TRP B 2 149 ? 96.954  199.670 15.434  1.00 43.66  ? 150 TRP B CE3 1 
ATOM   2124 C  CZ2 . TRP B 2 149 ? 95.903  200.621 17.892  1.00 50.11  ? 150 TRP B CZ2 1 
ATOM   2125 C  CZ3 . TRP B 2 149 ? 95.607  199.929 15.591  1.00 50.66  ? 150 TRP B CZ3 1 
ATOM   2126 C  CH2 . TRP B 2 149 ? 95.092  200.405 16.817  1.00 56.85  ? 150 TRP B CH2 1 
ATOM   2127 N  N   . HIS B 2 150 ? 99.244  196.591 14.264  1.00 46.74  ? 151 HIS B N   1 
ATOM   2128 C  CA  . HIS B 2 150 ? 98.299  195.548 13.910  1.00 47.34  ? 151 HIS B CA  1 
ATOM   2129 C  C   . HIS B 2 150 ? 98.739  194.850 12.646  1.00 53.53  ? 151 HIS B C   1 
ATOM   2130 O  O   . HIS B 2 150 ? 98.941  195.483 11.615  1.00 57.93  ? 151 HIS B O   1 
ATOM   2131 C  CB  . HIS B 2 150 ? 96.888  196.078 13.721  1.00 40.39  ? 151 HIS B CB  1 
ATOM   2132 C  CG  . HIS B 2 150 ? 95.908  195.005 13.350  1.00 53.56  ? 151 HIS B CG  1 
ATOM   2133 N  ND1 . HIS B 2 150 ? 95.155  194.326 14.287  1.00 50.69  ? 151 HIS B ND1 1 
ATOM   2134 C  CD2 . HIS B 2 150 ? 95.591  194.461 12.150  1.00 50.20  ? 151 HIS B CD2 1 
ATOM   2135 C  CE1 . HIS B 2 150 ? 94.405  193.425 13.677  1.00 49.93  ? 151 HIS B CE1 1 
ATOM   2136 N  NE2 . HIS B 2 150 ? 94.652  193.485 12.380  1.00 54.74  ? 151 HIS B NE2 1 
ATOM   2137 N  N   . LYS B 2 151 ? 98.889  193.535 12.729  1.00 54.15  ? 152 LYS B N   1 
ATOM   2138 C  CA  . LYS B 2 151 ? 99.247  192.770 11.557  1.00 54.01  ? 152 LYS B CA  1 
ATOM   2139 C  C   . LYS B 2 151 ? 97.996  192.130 10.992  1.00 49.08  ? 152 LYS B C   1 
ATOM   2140 O  O   . LYS B 2 151 ? 97.219  191.533 11.721  1.00 54.54  ? 152 LYS B O   1 
ATOM   2141 C  CB  . LYS B 2 151 ? 100.287 191.705 11.871  1.00 53.27  ? 152 LYS B CB  1 
ATOM   2142 C  CG  . LYS B 2 151 ? 100.796 191.019 10.620  1.00 59.28  ? 152 LYS B CG  1 
ATOM   2143 C  CD  . LYS B 2 151 ? 101.809 189.933 10.913  1.00 67.41  ? 152 LYS B CD  1 
ATOM   2144 C  CE  . LYS B 2 151 ? 102.205 189.212 9.627   1.00 79.39  ? 152 LYS B CE  1 
ATOM   2145 N  NZ  . LYS B 2 151 ? 103.186 188.113 9.865   1.00 77.93  1 152 LYS B NZ  1 
ATOM   2146 N  N   . PHE B 2 152 ? 97.807  192.283 9.687   1.00 53.51  ? 153 PHE B N   1 
ATOM   2147 C  CA  . PHE B 2 152 ? 96.724  191.635 8.970   1.00 52.65  ? 153 PHE B CA  1 
ATOM   2148 C  C   . PHE B 2 152 ? 97.215  190.309 8.443   1.00 58.90  ? 153 PHE B C   1 
ATOM   2149 O  O   . PHE B 2 152 ? 98.138  190.272 7.628   1.00 64.32  ? 153 PHE B O   1 
ATOM   2150 C  CB  . PHE B 2 152 ? 96.253  192.481 7.800   1.00 44.77  ? 153 PHE B CB  1 
ATOM   2151 C  CG  . PHE B 2 152 ? 95.442  193.677 8.179   1.00 49.53  ? 153 PHE B CG  1 
ATOM   2152 C  CD1 . PHE B 2 152 ? 94.095  193.548 8.478   1.00 45.33  ? 153 PHE B CD1 1 
ATOM   2153 C  CD2 . PHE B 2 152 ? 96.018  194.942 8.204   1.00 38.44  ? 153 PHE B CD2 1 
ATOM   2154 C  CE1 . PHE B 2 152 ? 93.338  194.658 8.795   1.00 44.91  ? 153 PHE B CE1 1 
ATOM   2155 C  CE2 . PHE B 2 152 ? 95.281  196.053 8.526   1.00 37.89  ? 153 PHE B CE2 1 
ATOM   2156 C  CZ  . PHE B 2 152 ? 93.935  195.919 8.824   1.00 47.10  ? 153 PHE B CZ  1 
ATOM   2157 N  N   . ASP B 2 153 ? 96.588  189.227 8.885   1.00 61.42  ? 154 ASP B N   1 
ATOM   2158 C  CA  . ASP B 2 153 ? 97.014  187.892 8.478   1.00 66.15  ? 154 ASP B CA  1 
ATOM   2159 C  C   . ASP B 2 153 ? 96.782  187.654 6.982   1.00 69.84  ? 154 ASP B C   1 
ATOM   2160 O  O   . ASP B 2 153 ? 97.626  187.063 6.307   1.00 64.41  ? 154 ASP B O   1 
ATOM   2161 C  CB  . ASP B 2 153 ? 96.303  186.831 9.317   1.00 66.46  ? 154 ASP B CB  1 
ATOM   2162 C  CG  . ASP B 2 153 ? 96.774  186.820 10.771  1.00 77.77  ? 154 ASP B CG  1 
ATOM   2163 O  OD1 . ASP B 2 153 ? 97.949  187.175 11.042  1.00 73.71  ? 154 ASP B OD1 1 
ATOM   2164 O  OD2 . ASP B 2 153 ? 95.964  186.455 11.649  1.00 88.63  1 154 ASP B OD2 1 
ATOM   2165 N  N   . GLU B 2 154 ? 95.650  188.128 6.466   1.00 58.61  ? 155 GLU B N   1 
ATOM   2166 C  CA  . GLU B 2 154 ? 95.312  187.906 5.064   1.00 62.35  ? 155 GLU B CA  1 
ATOM   2167 C  C   . GLU B 2 154 ? 96.206  188.697 4.133   1.00 58.38  ? 155 GLU B C   1 
ATOM   2168 O  O   . GLU B 2 154 ? 96.471  189.880 4.352   1.00 58.49  ? 155 GLU B O   1 
ATOM   2169 C  CB  . GLU B 2 154 ? 93.848  188.253 4.783   1.00 60.03  ? 155 GLU B CB  1 
ATOM   2170 C  CG  . GLU B 2 154 ? 92.959  187.042 4.680   1.00 67.89  ? 155 GLU B CG  1 
ATOM   2171 C  CD  . GLU B 2 154 ? 92.671  186.422 6.028   1.00 97.72  ? 155 GLU B CD  1 
ATOM   2172 O  OE1 . GLU B 2 154 ? 92.694  187.164 7.035   1.00 90.33  ? 155 GLU B OE1 1 
ATOM   2173 O  OE2 . GLU B 2 154 ? 92.450  185.189 6.086   1.00 109.93 1 155 GLU B OE2 1 
ATOM   2174 N  N   . PRO B 2 155 ? 96.664  188.037 3.069   1.00 60.13  ? 156 PRO B N   1 
ATOM   2175 C  CA  . PRO B 2 155 ? 97.525  188.677 2.079   1.00 58.02  ? 156 PRO B CA  1 
ATOM   2176 C  C   . PRO B 2 155 ? 96.708  189.417 1.041   1.00 50.41  ? 156 PRO B C   1 
ATOM   2177 O  O   . PRO B 2 155 ? 95.531  189.137 0.852   1.00 49.66  ? 156 PRO B O   1 
ATOM   2178 C  CB  . PRO B 2 155 ? 98.240  187.498 1.436   1.00 57.46  ? 156 PRO B CB  1 
ATOM   2179 C  CG  . PRO B 2 155 ? 97.185  186.424 1.462   1.00 56.23  ? 156 PRO B CG  1 
ATOM   2180 C  CD  . PRO B 2 155 ? 96.433  186.617 2.757   1.00 54.85  ? 156 PRO B CD  1 
ATOM   2181 N  N   . ILE B 2 156 ? 97.339  190.372 0.379   1.00 53.58  ? 157 ILE B N   1 
ATOM   2182 C  CA  . ILE B 2 156 ? 96.778  190.951 -0.825  1.00 47.78  ? 157 ILE B CA  1 
ATOM   2183 C  C   . ILE B 2 156 ? 97.385  190.197 -1.990  1.00 49.75  ? 157 ILE B C   1 
ATOM   2184 O  O   . ILE B 2 156 ? 98.595  190.263 -2.199  1.00 50.18  ? 157 ILE B O   1 
ATOM   2185 C  CB  . ILE B 2 156 ? 97.070  192.453 -0.967  1.00 55.55  ? 157 ILE B CB  1 
ATOM   2186 C  CG1 . ILE B 2 156 ? 96.481  193.235 0.209   1.00 58.49  ? 157 ILE B CG1 1 
ATOM   2187 C  CG2 . ILE B 2 156 ? 96.506  192.967 -2.279  1.00 56.14  ? 157 ILE B CG2 1 
ATOM   2188 C  CD1 . ILE B 2 156 ? 97.472  193.540 1.303   1.00 51.83  ? 157 ILE B CD1 1 
ATOM   2189 N  N   . GLU B 2 157 ? 96.564  189.417 -2.688  1.00 57.24  ? 158 GLU B N   1 
ATOM   2190 C  CA  . GLU B 2 157 ? 97.031  188.626 -3.818  1.00 48.19  ? 158 GLU B CA  1 
ATOM   2191 C  C   . GLU B 2 157 ? 97.228  189.490 -5.042  1.00 52.83  ? 158 GLU B C   1 
ATOM   2192 O  O   . GLU B 2 157 ? 96.250  189.871 -5.683  1.00 54.26  ? 158 GLU B O   1 
ATOM   2193 C  CB  . GLU B 2 157 ? 96.049  187.507 -4.154  1.00 48.72  ? 158 GLU B CB  1 
ATOM   2194 C  CG  . GLU B 2 157 ? 95.950  186.422 -3.107  1.00 63.79  ? 158 GLU B CG  1 
ATOM   2195 C  CD  . GLU B 2 157 ? 94.824  185.440 -3.390  1.00 75.77  ? 158 GLU B CD  1 
ATOM   2196 O  OE1 . GLU B 2 157 ? 94.538  185.197 -4.582  1.00 75.50  ? 158 GLU B OE1 1 
ATOM   2197 O  OE2 . GLU B 2 157 ? 94.237  184.906 -2.422  1.00 71.04  1 158 GLU B OE2 1 
ATOM   2198 N  N   . CYS B 2 158 ? 98.476  189.819 -5.360  1.00 43.21  ? 159 CYS B N   1 
ATOM   2199 C  CA  . CYS B 2 158 ? 98.751  190.622 -6.553  1.00 56.45  ? 159 CYS B CA  1 
ATOM   2200 C  C   . CYS B 2 158 ? 99.369  189.810 -7.695  1.00 66.63  ? 159 CYS B C   1 
ATOM   2201 O  O   . CYS B 2 158 ? 100.578 189.873 -7.937  1.00 59.66  ? 159 CYS B O   1 
ATOM   2202 C  CB  . CYS B 2 158 ? 99.663  191.794 -6.207  1.00 58.26  ? 159 CYS B CB  1 
ATOM   2203 S  SG  . CYS B 2 158 ? 98.933  192.905 -5.002  1.00 50.16  ? 159 CYS B SG  1 
ATOM   2204 N  N   . PHE B 2 159 ? 98.530  189.076 -8.417  1.00 67.31  ? 160 PHE B N   1 
ATOM   2205 C  CA  . PHE B 2 159 ? 99.013  188.270 -9.530  1.00 63.33  ? 160 PHE B CA  1 
ATOM   2206 C  C   . PHE B 2 159 ? 98.311  188.650 -10.826 1.00 60.10  ? 160 PHE B C   1 
ATOM   2207 O  O   . PHE B 2 159 ? 98.724  188.233 -11.902 1.00 70.57  ? 160 PHE B O   1 
ATOM   2208 C  CB  . PHE B 2 159 ? 98.834  186.776 -9.232  1.00 57.87  ? 160 PHE B CB  1 
ATOM   2209 C  CG  . PHE B 2 159 ? 99.640  186.287 -8.054  1.00 57.88  ? 160 PHE B CG  1 
ATOM   2210 C  CD1 . PHE B 2 159 ? 99.129  186.357 -6.762  1.00 66.68  ? 160 PHE B CD1 1 
ATOM   2211 C  CD2 . PHE B 2 159 ? 100.904 185.752 -8.236  1.00 54.43  ? 160 PHE B CD2 1 
ATOM   2212 C  CE1 . PHE B 2 159 ? 99.869  185.911 -5.671  1.00 55.62  ? 160 PHE B CE1 1 
ATOM   2213 C  CE2 . PHE B 2 159 ? 101.649 185.301 -7.158  1.00 59.22  ? 160 PHE B CE2 1 
ATOM   2214 C  CZ  . PHE B 2 159 ? 101.128 185.380 -5.874  1.00 58.11  ? 160 PHE B CZ  1 
ATOM   2215 N  N   . ASN B 2 160 ? 97.247  189.435 -10.718 1.00 56.84  ? 161 ASN B N   1 
ATOM   2216 C  CA  . ASN B 2 160 ? 96.570  189.969 -11.892 1.00 61.14  ? 161 ASN B CA  1 
ATOM   2217 C  C   . ASN B 2 160 ? 97.472  190.950 -12.605 1.00 64.56  ? 161 ASN B C   1 
ATOM   2218 O  O   . ASN B 2 160 ? 98.161  191.735 -11.966 1.00 63.86  ? 161 ASN B O   1 
ATOM   2219 C  CB  . ASN B 2 160 ? 95.266  190.657 -11.506 1.00 62.65  ? 161 ASN B CB  1 
ATOM   2220 C  CG  . ASN B 2 160 ? 94.423  189.811 -10.590 1.00 75.54  ? 161 ASN B CG  1 
ATOM   2221 O  OD1 . ASN B 2 160 ? 94.717  188.631 -10.376 1.00 84.25  ? 161 ASN B OD1 1 
ATOM   2222 N  ND2 . ASN B 2 160 ? 93.377  190.406 -10.027 1.00 74.01  ? 161 ASN B ND2 1 
ATOM   2223 N  N   . GLU B 2 161 ? 97.467  190.922 -13.928 1.00 72.33  ? 162 GLU B N   1 
ATOM   2224 C  CA  . GLU B 2 161 ? 98.244  191.895 -14.670 1.00 69.95  ? 162 GLU B CA  1 
ATOM   2225 C  C   . GLU B 2 161 ? 97.570  193.251 -14.512 1.00 71.78  ? 162 GLU B C   1 
ATOM   2226 O  O   . GLU B 2 161 ? 96.350  193.322 -14.348 1.00 74.62  ? 162 GLU B O   1 
ATOM   2227 C  CB  . GLU B 2 161 ? 98.360  191.494 -16.136 1.00 80.78  ? 162 GLU B CB  1 
ATOM   2228 C  CG  . GLU B 2 161 ? 99.245  190.274 -16.352 1.00 85.77  ? 162 GLU B CG  1 
ATOM   2229 C  CD  . GLU B 2 161 ? 99.694  190.117 -17.794 1.00 107.99 ? 162 GLU B CD  1 
ATOM   2230 O  OE1 . GLU B 2 161 ? 99.417  191.025 -18.610 1.00 110.20 ? 162 GLU B OE1 1 
ATOM   2231 O  OE2 . GLU B 2 161 ? 100.288 189.064 -18.119 1.00 97.76  1 162 GLU B OE2 1 
ATOM   2232 N  N   . SER B 2 162 ? 98.364  194.320 -14.554 1.00 67.79  ? 163 SER B N   1 
ATOM   2233 C  CA  . SER B 2 162 ? 97.856  195.671 -14.323 1.00 69.16  ? 163 SER B CA  1 
ATOM   2234 C  C   . SER B 2 162 ? 97.580  196.375 -15.641 1.00 75.78  ? 163 SER B C   1 
ATOM   2235 O  O   . SER B 2 162 ? 98.375  196.281 -16.577 1.00 78.56  ? 163 SER B O   1 
ATOM   2236 C  CB  . SER B 2 162 ? 98.856  196.483 -13.495 1.00 67.17  ? 163 SER B CB  1 
ATOM   2237 O  OG  . SER B 2 162 ? 98.644  197.879 -13.628 1.00 58.29  ? 163 SER B OG  1 
ATOM   2238 N  N   . ASP B 2 163 ? 96.477  197.115 -15.701 1.00 70.84  ? 164 ASP B N   1 
ATOM   2239 C  CA  . ASP B 2 163 ? 96.153  197.893 -16.895 1.00 74.84  ? 164 ASP B CA  1 
ATOM   2240 C  C   . ASP B 2 163 ? 97.201  198.968 -17.199 1.00 77.99  ? 164 ASP B C   1 
ATOM   2241 O  O   . ASP B 2 163 ? 97.219  199.525 -18.292 1.00 86.96  ? 164 ASP B O   1 
ATOM   2242 C  CB  . ASP B 2 163 ? 94.776  198.553 -16.758 1.00 80.32  ? 164 ASP B CB  1 
ATOM   2243 C  CG  . ASP B 2 163 ? 94.534  199.132 -15.371 1.00 83.66  ? 164 ASP B CG  1 
ATOM   2244 O  OD1 . ASP B 2 163 ? 95.503  199.656 -14.770 1.00 76.46  1 164 ASP B OD1 1 
ATOM   2245 O  OD2 . ASP B 2 163 ? 93.369  199.079 -14.899 1.00 69.43  ? 164 ASP B OD2 1 
ATOM   2246 N  N   . LEU B 2 164 ? 98.068  199.256 -16.235 1.00 74.76  ? 165 LEU B N   1 
ATOM   2247 C  CA  . LEU B 2 164 ? 99.128  200.247 -16.408 1.00 77.02  ? 165 LEU B CA  1 
ATOM   2248 C  C   . LEU B 2 164 ? 100.305 199.744 -17.257 1.00 79.05  ? 165 LEU B C   1 
ATOM   2249 O  O   . LEU B 2 164 ? 101.387 200.337 -17.241 1.00 76.56  ? 165 LEU B O   1 
ATOM   2250 C  CB  . LEU B 2 164 ? 99.635  200.703 -15.039 1.00 71.41  ? 165 LEU B CB  1 
ATOM   2251 C  CG  . LEU B 2 164 ? 98.585  201.380 -14.156 1.00 66.91  ? 165 LEU B CG  1 
ATOM   2252 C  CD1 . LEU B 2 164 ? 99.088  201.456 -12.729 1.00 67.49  ? 165 LEU B CD1 1 
ATOM   2253 C  CD2 . LEU B 2 164 ? 98.226  202.761 -14.666 1.00 54.04  ? 165 LEU B CD2 1 
ATOM   2254 N  N   . GLY B 2 165 ? 100.103 198.651 -17.988 1.00 84.38  ? 166 GLY B N   1 
ATOM   2255 C  CA  . GLY B 2 165 ? 101.150 198.115 -18.843 1.00 85.14  ? 166 GLY B CA  1 
ATOM   2256 C  C   . GLY B 2 165 ? 101.651 196.754 -18.394 1.00 82.64  ? 166 GLY B C   1 
ATOM   2257 O  O   . GLY B 2 165 ? 101.195 196.210 -17.388 1.00 82.35  ? 166 GLY B O   1 
ATOM   2258 N  N   . LYS B 2 166 ? 102.581 196.192 -19.154 1.00 83.23  ? 167 LYS B N   1 
ATOM   2259 C  CA  . LYS B 2 166 ? 103.142 194.890 -18.824 1.00 86.71  ? 167 LYS B CA  1 
ATOM   2260 C  C   . LYS B 2 166 ? 104.236 194.989 -17.766 1.00 79.68  ? 167 LYS B C   1 
ATOM   2261 O  O   . LYS B 2 166 ? 104.824 196.053 -17.572 1.00 73.54  ? 167 LYS B O   1 
ATOM   2262 C  CB  . LYS B 2 166 ? 103.686 194.217 -20.087 1.00 95.41  ? 167 LYS B CB  1 
ATOM   2263 C  CG  . LYS B 2 166 ? 104.721 195.040 -20.867 1.00 96.62  ? 167 LYS B CG  1 
ATOM   2264 C  CD  . LYS B 2 166 ? 105.298 194.226 -22.025 1.00 94.08  ? 167 LYS B CD  1 
ATOM   2265 C  CE  . LYS B 2 166 ? 106.098 195.076 -23.005 1.00 89.23  ? 167 LYS B CE  1 
ATOM   2266 N  NZ  . LYS B 2 166 ? 105.225 195.920 -23.876 1.00 75.41  1 167 LYS B NZ  1 
ATOM   2267 N  N   . ASN B 2 167 ? 104.513 193.855 -17.119 1.00 82.64  ? 168 ASN B N   1 
ATOM   2268 C  CA  . ASN B 2 167 ? 105.429 193.754 -15.971 1.00 84.88  ? 168 ASN B CA  1 
ATOM   2269 C  C   . ASN B 2 167 ? 104.960 194.552 -14.754 1.00 76.40  ? 168 ASN B C   1 
ATOM   2270 O  O   . ASN B 2 167 ? 105.751 194.854 -13.859 1.00 70.96  ? 168 ASN B O   1 
ATOM   2271 C  CB  . ASN B 2 167 ? 106.845 194.200 -16.360 1.00 87.30  ? 168 ASN B CB  1 
ATOM   2272 C  CG  . ASN B 2 167 ? 107.417 193.394 -17.519 1.00 91.41  ? 168 ASN B CG  1 
ATOM   2273 O  OD1 . ASN B 2 167 ? 107.021 192.248 -17.756 1.00 84.81  ? 168 ASN B OD1 1 
ATOM   2274 N  ND2 . ASN B 2 167 ? 108.356 193.991 -18.245 1.00 89.11  ? 168 ASN B ND2 1 
ATOM   2275 N  N   . LEU B 2 168 ? 103.670 194.883 -14.742 1.00 67.46  ? 169 LEU B N   1 
ATOM   2276 C  CA  . LEU B 2 168 ? 103.022 195.569 -13.631 1.00 63.10  ? 169 LEU B CA  1 
ATOM   2277 C  C   . LEU B 2 168 ? 101.850 194.725 -13.166 1.00 63.71  ? 169 LEU B C   1 
ATOM   2278 O  O   . LEU B 2 168 ? 101.185 194.067 -13.966 1.00 61.18  ? 169 LEU B O   1 
ATOM   2279 C  CB  . LEU B 2 168 ? 102.556 196.975 -14.040 1.00 59.30  ? 169 LEU B CB  1 
ATOM   2280 C  CG  . LEU B 2 168 ? 103.664 198.001 -14.336 1.00 61.47  ? 169 LEU B CG  1 
ATOM   2281 C  CD1 . LEU B 2 168 ? 103.120 199.405 -14.585 1.00 48.31  ? 169 LEU B CD1 1 
ATOM   2282 C  CD2 . LEU B 2 168 ? 104.666 198.026 -13.188 1.00 54.47  ? 169 LEU B CD2 1 
ATOM   2283 N  N   . TYR B 2 169 ? 101.617 194.704 -11.864 1.00 59.05  ? 170 TYR B N   1 
ATOM   2284 C  CA  . TYR B 2 169 ? 100.566 193.855 -11.332 1.00 59.19  ? 170 TYR B CA  1 
ATOM   2285 C  C   . TYR B 2 169 ? 99.623  194.606 -10.408 1.00 58.69  ? 170 TYR B C   1 
ATOM   2286 O  O   . TYR B 2 169 ? 99.929  195.700 -9.925  1.00 58.15  ? 170 TYR B O   1 
ATOM   2287 C  CB  . TYR B 2 169 ? 101.184 192.652 -10.624 1.00 55.80  ? 170 TYR B CB  1 
ATOM   2288 C  CG  . TYR B 2 169 ? 102.112 191.878 -11.523 1.00 67.28  ? 170 TYR B CG  1 
ATOM   2289 C  CD1 . TYR B 2 169 ? 101.620 190.931 -12.419 1.00 67.49  ? 170 TYR B CD1 1 
ATOM   2290 C  CD2 . TYR B 2 169 ? 103.474 192.133 -11.518 1.00 65.80  ? 170 TYR B CD2 1 
ATOM   2291 C  CE1 . TYR B 2 169 ? 102.473 190.235 -13.256 1.00 65.29  ? 170 TYR B CE1 1 
ATOM   2292 C  CE2 . TYR B 2 169 ? 104.325 191.451 -12.345 1.00 62.68  ? 170 TYR B CE2 1 
ATOM   2293 C  CZ  . TYR B 2 169 ? 103.830 190.501 -13.210 1.00 65.42  ? 170 TYR B CZ  1 
ATOM   2294 O  OH  . TYR B 2 169 ? 104.710 189.830 -14.031 1.00 70.17  ? 170 TYR B OH  1 
ATOM   2295 N  N   . SER B 2 170 ? 98.472  193.994 -10.177 1.00 50.80  ? 171 SER B N   1 
ATOM   2296 C  CA  . SER B 2 170 ? 97.409  194.596 -9.406  1.00 46.32  ? 171 SER B CA  1 
ATOM   2297 C  C   . SER B 2 170 ? 96.816  193.555 -8.474  1.00 57.76  ? 171 SER B C   1 
ATOM   2298 O  O   . SER B 2 170 ? 97.035  192.350 -8.641  1.00 55.20  ? 171 SER B O   1 
ATOM   2299 C  CB  . SER B 2 170 ? 96.326  195.155 -10.326 1.00 53.37  ? 171 SER B CB  1 
ATOM   2300 O  OG  . SER B 2 170 ? 95.620  194.101 -10.955 1.00 58.56  ? 171 SER B OG  1 
ATOM   2301 N  N   . GLY B 2 171 ? 96.088  194.024 -7.471  1.00 49.29  ? 172 GLY B N   1 
ATOM   2302 C  CA  . GLY B 2 171 ? 95.397  193.133 -6.575  1.00 42.93  ? 172 GLY B CA  1 
ATOM   2303 C  C   . GLY B 2 171 ? 94.338  193.891 -5.812  1.00 53.21  ? 172 GLY B C   1 
ATOM   2304 O  O   . GLY B 2 171 ? 94.353  195.119 -5.786  1.00 53.18  ? 172 GLY B O   1 
ATOM   2305 N  N   . LYS B 2 172 ? 93.403  193.162 -5.213  1.00 51.15  ? 173 LYS B N   1 
ATOM   2306 C  CA  . LYS B 2 172 ? 92.384  193.762 -4.373  1.00 49.86  ? 173 LYS B CA  1 
ATOM   2307 C  C   . LYS B 2 172 ? 91.895  192.772 -3.327  1.00 51.17  ? 173 LYS B C   1 
ATOM   2308 O  O   . LYS B 2 172 ? 91.889  191.564 -3.556  1.00 48.23  ? 173 LYS B O   1 
ATOM   2309 C  CB  . LYS B 2 172 ? 91.215  194.268 -5.212  1.00 44.10  ? 173 LYS B CB  1 
ATOM   2310 C  CG  . LYS B 2 172 ? 90.484  193.212 -5.979  1.00 49.82  ? 173 LYS B CG  1 
ATOM   2311 C  CD  . LYS B 2 172 ? 89.291  193.824 -6.713  1.00 68.32  ? 173 LYS B CD  1 
ATOM   2312 C  CE  . LYS B 2 172 ? 88.506  192.776 -7.488  1.00 76.87  ? 173 LYS B CE  1 
ATOM   2313 N  NZ  . LYS B 2 172 ? 87.508  193.404 -8.389  1.00 77.37  1 173 LYS B NZ  1 
ATOM   2314 N  N   . THR B 2 173 ? 91.515  193.295 -2.169  1.00 47.14  ? 174 THR B N   1 
ATOM   2315 C  CA  . THR B 2 173 ? 90.908  192.485 -1.130  1.00 47.46  ? 174 THR B CA  1 
ATOM   2316 C  C   . THR B 2 173 ? 90.231  193.357 -0.087  1.00 49.77  ? 174 THR B C   1 
ATOM   2317 O  O   . THR B 2 173 ? 90.594  194.517 0.100   1.00 53.40  ? 174 THR B O   1 
ATOM   2318 C  CB  . THR B 2 173 ? 91.924  191.581 -0.410  1.00 54.32  ? 174 THR B CB  1 
ATOM   2319 O  OG1 . THR B 2 173 ? 91.218  190.652 0.420   1.00 70.53  ? 174 THR B OG1 1 
ATOM   2320 C  CG2 . THR B 2 173 ? 92.856  192.392 0.453   1.00 53.63  ? 174 THR B CG2 1 
ATOM   2321 N  N   . PHE B 2 174 ? 89.258  192.783 0.606   1.00 44.06  ? 175 PHE B N   1 
ATOM   2322 C  CA  . PHE B 2 174 ? 88.716  193.403 1.800   1.00 50.75  ? 175 PHE B CA  1 
ATOM   2323 C  C   . PHE B 2 174 ? 89.442  192.805 2.996   1.00 52.14  ? 175 PHE B C   1 
ATOM   2324 O  O   . PHE B 2 174 ? 89.616  191.592 3.072   1.00 55.91  ? 175 PHE B O   1 
ATOM   2325 C  CB  . PHE B 2 174 ? 87.213  193.163 1.930   1.00 51.42  ? 175 PHE B CB  1 
ATOM   2326 C  CG  . PHE B 2 174 ? 86.365  194.002 1.011   1.00 55.79  ? 175 PHE B CG  1 
ATOM   2327 C  CD1 . PHE B 2 174 ? 85.995  195.288 1.366   1.00 56.22  ? 175 PHE B CD1 1 
ATOM   2328 C  CD2 . PHE B 2 174 ? 85.892  193.487 -0.181  1.00 57.63  ? 175 PHE B CD2 1 
ATOM   2329 C  CE1 . PHE B 2 174 ? 85.194  196.054 0.541   1.00 53.66  ? 175 PHE B CE1 1 
ATOM   2330 C  CE2 . PHE B 2 174 ? 85.088  194.255 -1.014  1.00 65.12  ? 175 PHE B CE2 1 
ATOM   2331 C  CZ  . PHE B 2 174 ? 84.748  195.542 -0.649  1.00 59.92  ? 175 PHE B CZ  1 
ATOM   2332 N  N   . LEU B 2 175 ? 89.880  193.652 3.921   1.00 50.47  ? 176 LEU B N   1 
ATOM   2333 C  CA  . LEU B 2 175 ? 90.444  193.163 5.174   1.00 50.67  ? 176 LEU B CA  1 
ATOM   2334 C  C   . LEU B 2 175 ? 89.512  193.530 6.324   1.00 51.76  ? 176 LEU B C   1 
ATOM   2335 O  O   . LEU B 2 175 ? 88.588  194.327 6.167   1.00 55.69  ? 176 LEU B O   1 
ATOM   2336 C  CB  . LEU B 2 175 ? 91.845  193.734 5.427   1.00 45.04  ? 176 LEU B CB  1 
ATOM   2337 C  CG  . LEU B 2 175 ? 92.994  193.462 4.458   1.00 49.94  ? 176 LEU B CG  1 
ATOM   2338 C  CD1 . LEU B 2 175 ? 94.231  194.259 4.860   1.00 46.57  ? 176 LEU B CD1 1 
ATOM   2339 C  CD2 . LEU B 2 175 ? 93.309  191.983 4.442   1.00 47.86  ? 176 LEU B CD2 1 
ATOM   2340 N  N   . SER B 2 176 ? 89.778  192.965 7.490   1.00 53.02  ? 177 SER B N   1 
ATOM   2341 C  CA  . SER B 2 176 ? 88.971  193.249 8.657   1.00 47.49  ? 177 SER B CA  1 
ATOM   2342 C  C   . SER B 2 176 ? 89.834  193.297 9.901   1.00 48.88  ? 177 SER B C   1 
ATOM   2343 O  O   . SER B 2 176 ? 90.878  192.647 9.997   1.00 52.49  ? 177 SER B O   1 
ATOM   2344 C  CB  . SER B 2 176 ? 87.869  192.193 8.797   1.00 54.28  ? 177 SER B CB  1 
ATOM   2345 O  OG  . SER B 2 176 ? 87.346  192.160 10.109  1.00 68.69  ? 177 SER B OG  1 
ATOM   2346 N  N   . ALA B 2 177 ? 89.371  194.068 10.872  1.00 55.26  ? 178 ALA B N   1 
ATOM   2347 C  CA  . ALA B 2 177 ? 90.076  194.216 12.117  1.00 52.93  ? 178 ALA B CA  1 
ATOM   2348 C  C   . ALA B 2 177 ? 89.089  194.483 13.221  1.00 58.00  ? 178 ALA B C   1 
ATOM   2349 O  O   . ALA B 2 177 ? 88.060  195.121 12.994  1.00 61.21  ? 178 ALA B O   1 
ATOM   2350 C  CB  . ALA B 2 177 ? 91.105  195.351 12.024  1.00 56.92  ? 178 ALA B CB  1 
ATOM   2351 N  N   . PRO B 2 178 ? 89.397  193.983 14.424  1.00 62.68  ? 179 PRO B N   1 
ATOM   2352 C  CA  . PRO B 2 178 ? 88.594  194.244 15.616  1.00 59.07  ? 179 PRO B CA  1 
ATOM   2353 C  C   . PRO B 2 178 ? 88.945  195.591 16.244  1.00 58.74  ? 179 PRO B C   1 
ATOM   2354 O  O   . PRO B 2 178 ? 89.173  195.655 17.451  1.00 58.18  ? 179 PRO B O   1 
ATOM   2355 C  CB  . PRO B 2 178 ? 88.980  193.102 16.541  1.00 57.11  ? 179 PRO B CB  1 
ATOM   2356 C  CG  . PRO B 2 178 ? 90.402  192.810 16.164  1.00 55.74  ? 179 PRO B CG  1 
ATOM   2357 C  CD  . PRO B 2 178 ? 90.510  193.053 14.698  1.00 47.35  ? 179 PRO B CD  1 
ATOM   2358 N  N   . LEU B 2 179 ? 88.987  196.645 15.435  1.00 52.31  ? 180 LEU B N   1 
ATOM   2359 C  CA  . LEU B 2 179 ? 89.386  197.964 15.912  1.00 53.40  ? 180 LEU B CA  1 
ATOM   2360 C  C   . LEU B 2 179 ? 88.398  199.007 15.449  1.00 51.96  ? 180 LEU B C   1 
ATOM   2361 O  O   . LEU B 2 179 ? 87.887  198.908 14.349  1.00 53.45  ? 180 LEU B O   1 
ATOM   2362 C  CB  . LEU B 2 179 ? 90.793  198.318 15.423  1.00 51.07  ? 180 LEU B CB  1 
ATOM   2363 C  CG  . LEU B 2 179 ? 91.904  197.390 15.927  1.00 55.92  ? 180 LEU B CG  1 
ATOM   2364 C  CD1 . LEU B 2 179 ? 93.130  197.477 15.049  1.00 50.52  ? 180 LEU B CD1 1 
ATOM   2365 C  CD2 . LEU B 2 179 ? 92.251  197.698 17.381  1.00 59.29  ? 180 LEU B CD2 1 
ATOM   2366 N  N   . PRO B 2 180 ? 88.103  200.006 16.298  1.00 52.06  ? 181 PRO B N   1 
ATOM   2367 C  CA  . PRO B 2 180 ? 87.270  201.106 15.816  1.00 56.98  ? 181 PRO B CA  1 
ATOM   2368 C  C   . PRO B 2 180 ? 88.126  202.026 14.953  1.00 52.38  ? 181 PRO B C   1 
ATOM   2369 O  O   . PRO B 2 180 ? 89.346  202.024 15.090  1.00 47.80  ? 181 PRO B O   1 
ATOM   2370 C  CB  . PRO B 2 180 ? 86.815  201.797 17.106  1.00 46.56  ? 181 PRO B CB  1 
ATOM   2371 C  CG  . PRO B 2 180 ? 87.934  201.583 18.029  1.00 42.91  ? 181 PRO B CG  1 
ATOM   2372 C  CD  . PRO B 2 180 ? 88.499  200.207 17.700  1.00 50.66  ? 181 PRO B CD  1 
ATOM   2373 N  N   . THR B 2 181 ? 87.500  202.789 14.075  1.00 45.48  ? 182 THR B N   1 
ATOM   2374 C  CA  . THR B 2 181 ? 88.235  203.644 13.174  1.00 42.63  ? 182 THR B CA  1 
ATOM   2375 C  C   . THR B 2 181 ? 89.070  204.659 13.942  1.00 44.02  ? 182 THR B C   1 
ATOM   2376 O  O   . THR B 2 181 ? 90.209  204.937 13.560  1.00 45.02  ? 182 THR B O   1 
ATOM   2377 C  CB  . THR B 2 181 ? 87.274  204.384 12.213  1.00 43.59  ? 182 THR B CB  1 
ATOM   2378 O  OG1 . THR B 2 181 ? 86.748  203.448 11.267  1.00 50.00  ? 182 THR B OG1 1 
ATOM   2379 C  CG2 . THR B 2 181 ? 87.986  205.507 11.456  1.00 40.51  ? 182 THR B CG2 1 
ATOM   2380 N  N   . TRP B 2 182 ? 88.528  205.186 15.038  1.00 42.80  ? 183 TRP B N   1 
ATOM   2381 C  CA  . TRP B 2 182 ? 89.194  206.284 15.743  1.00 45.55  ? 183 TRP B CA  1 
ATOM   2382 C  C   . TRP B 2 182 ? 90.560  205.895 16.309  1.00 45.55  ? 183 TRP B C   1 
ATOM   2383 O  O   . TRP B 2 182 ? 91.402  206.757 16.581  1.00 45.34  ? 183 TRP B O   1 
ATOM   2384 C  CB  . TRP B 2 182 ? 88.301  206.830 16.846  1.00 43.30  ? 183 TRP B CB  1 
ATOM   2385 C  CG  . TRP B 2 182 ? 88.022  205.868 17.954  1.00 52.14  ? 183 TRP B CG  1 
ATOM   2386 C  CD1 . TRP B 2 182 ? 86.917  205.075 18.088  1.00 41.79  ? 183 TRP B CD1 1 
ATOM   2387 C  CD2 . TRP B 2 182 ? 88.855  205.594 19.089  1.00 48.73  ? 183 TRP B CD2 1 
ATOM   2388 N  NE1 . TRP B 2 182 ? 87.012  204.326 19.232  1.00 46.86  ? 183 TRP B NE1 1 
ATOM   2389 C  CE2 . TRP B 2 182 ? 88.189  204.620 19.866  1.00 50.76  ? 183 TRP B CE2 1 
ATOM   2390 C  CE3 . TRP B 2 182 ? 90.100  206.069 19.521  1.00 44.04  ? 183 TRP B CE3 1 
ATOM   2391 C  CZ2 . TRP B 2 182 ? 88.722  204.117 21.055  1.00 54.83  ? 183 TRP B CZ2 1 
ATOM   2392 C  CZ3 . TRP B 2 182 ? 90.628  205.570 20.701  1.00 54.14  ? 183 TRP B CZ3 1 
ATOM   2393 C  CH2 . TRP B 2 182 ? 89.937  204.603 21.457  1.00 53.24  ? 183 TRP B CH2 1 
ATOM   2394 N  N   . GLN B 2 183 ? 90.781  204.598 16.445  1.00 41.93  ? 184 GLN B N   1 
ATOM   2395 C  CA  . GLN B 2 183 ? 92.031  204.079 16.966  1.00 44.88  ? 184 GLN B CA  1 
ATOM   2396 C  C   . GLN B 2 183 ? 93.116  203.999 15.901  1.00 46.73  ? 184 GLN B C   1 
ATOM   2397 O  O   . GLN B 2 183 ? 94.288  203.817 16.228  1.00 43.17  ? 184 GLN B O   1 
ATOM   2398 C  CB  . GLN B 2 183 ? 91.820  202.692 17.576  1.00 46.01  ? 184 GLN B CB  1 
ATOM   2399 C  CG  . GLN B 2 183 ? 91.643  202.719 19.075  1.00 58.08  ? 184 GLN B CG  1 
ATOM   2400 C  CD  . GLN B 2 183 ? 91.596  201.338 19.689  1.00 64.72  ? 184 GLN B CD  1 
ATOM   2401 O  OE1 . GLN B 2 183 ? 90.524  200.818 20.002  1.00 64.07  ? 184 GLN B OE1 1 
ATOM   2402 N  NE2 . GLN B 2 183 ? 92.766  200.725 19.843  1.00 66.76  ? 184 GLN B NE2 1 
ATOM   2403 N  N   . LEU B 2 184 ? 92.713  204.094 14.636  1.00 39.01  ? 185 LEU B N   1 
ATOM   2404 C  CA  . LEU B 2 184 ? 93.649  204.016 13.508  1.00 40.70  ? 185 LEU B CA  1 
ATOM   2405 C  C   . LEU B 2 184 ? 94.089  205.377 13.003  1.00 35.30  ? 185 LEU B C   1 
ATOM   2406 O  O   . LEU B 2 184 ? 95.070  205.475 12.281  1.00 40.64  ? 185 LEU B O   1 
ATOM   2407 C  CB  . LEU B 2 184 ? 93.028  203.244 12.332  1.00 37.54  ? 185 LEU B CB  1 
ATOM   2408 C  CG  . LEU B 2 184 ? 92.260  201.967 12.663  1.00 37.38  ? 185 LEU B CG  1 
ATOM   2409 C  CD1 . LEU B 2 184 ? 91.503  201.452 11.457  1.00 36.77  ? 185 LEU B CD1 1 
ATOM   2410 C  CD2 . LEU B 2 184 ? 93.227  200.935 13.159  1.00 42.87  ? 185 LEU B CD2 1 
ATOM   2411 N  N   . ILE B 2 185 ? 93.343  206.417 13.361  1.00 33.80  ? 186 ILE B N   1 
ATOM   2412 C  CA  . ILE B 2 185 ? 93.590  207.747 12.822  1.00 37.98  ? 186 ILE B CA  1 
ATOM   2413 C  C   . ILE B 2 185 ? 94.987  208.215 13.178  1.00 35.28  ? 186 ILE B C   1 
ATOM   2414 O  O   . ILE B 2 185 ? 95.387  208.163 14.324  1.00 42.37  ? 186 ILE B O   1 
ATOM   2415 C  CB  . ILE B 2 185 ? 92.568  208.780 13.334  1.00 40.96  ? 186 ILE B CB  1 
ATOM   2416 C  CG1 . ILE B 2 185 ? 91.150  208.397 12.897  1.00 28.32  ? 186 ILE B CG1 1 
ATOM   2417 C  CG2 . ILE B 2 185 ? 92.935  210.171 12.842  1.00 32.54  ? 186 ILE B CG2 1 
ATOM   2418 C  CD1 . ILE B 2 185 ? 91.022  208.175 11.404  1.00 34.73  ? 186 ILE B CD1 1 
ATOM   2419 N  N   . GLY B 2 186 ? 95.749  208.641 12.191  1.00 30.42  ? 187 GLY B N   1 
ATOM   2420 C  CA  . GLY B 2 186 ? 97.054  209.191 12.476  1.00 33.83  ? 187 GLY B CA  1 
ATOM   2421 C  C   . GLY B 2 186 ? 98.175  208.182 12.494  1.00 34.92  ? 187 GLY B C   1 
ATOM   2422 O  O   . GLY B 2 186 ? 99.327  208.552 12.653  1.00 32.88  ? 187 GLY B O   1 
ATOM   2423 N  N   . ARG B 2 187 ? 97.845  206.906 12.333  1.00 33.42  ? 188 ARG B N   1 
ATOM   2424 C  CA  . ARG B 2 187 ? 98.873  205.870 12.268  1.00 36.91  ? 188 ARG B CA  1 
ATOM   2425 C  C   . ARG B 2 187 ? 99.219  205.589 10.818  1.00 34.27  ? 188 ARG B C   1 
ATOM   2426 O  O   . ARG B 2 187 ? 98.636  206.175 9.919   1.00 42.18  ? 188 ARG B O   1 
ATOM   2427 C  CB  . ARG B 2 187 ? 98.402  204.597 12.956  1.00 34.97  ? 188 ARG B CB  1 
ATOM   2428 C  CG  . ARG B 2 187 ? 98.018  204.803 14.403  1.00 41.27  ? 188 ARG B CG  1 
ATOM   2429 C  CD  . ARG B 2 187 ? 97.513  203.498 14.962  1.00 44.97  ? 188 ARG B CD  1 
ATOM   2430 N  NE  . ARG B 2 187 ? 97.035  203.652 16.320  1.00 47.56  ? 188 ARG B NE  1 
ATOM   2431 C  CZ  . ARG B 2 187 ? 97.814  203.958 17.347  1.00 50.67  ? 188 ARG B CZ  1 
ATOM   2432 N  NH1 . ARG B 2 187 ? 99.116  204.148 17.164  1.00 50.12  1 188 ARG B NH1 1 
ATOM   2433 N  NH2 . ARG B 2 187 ? 97.289  204.068 18.555  1.00 51.59  ? 188 ARG B NH2 1 
ATOM   2434 N  N   . SER B 2 188 ? 100.145 204.670 10.590  1.00 38.13  ? 189 SER B N   1 
ATOM   2435 C  CA  . SER B 2 188 ? 100.578 204.369 9.236   1.00 37.79  ? 189 SER B CA  1 
ATOM   2436 C  C   . SER B 2 188 ? 99.979  203.069 8.750   1.00 39.67  ? 189 SER B C   1 
ATOM   2437 O  O   . SER B 2 188 ? 99.929  202.101 9.488   1.00 45.99  ? 189 SER B O   1 
ATOM   2438 C  CB  . SER B 2 188 ? 102.086 204.286 9.171   1.00 37.70  ? 189 SER B CB  1 
ATOM   2439 O  OG  . SER B 2 188 ? 102.647 205.580 9.094   1.00 49.03  ? 189 SER B OG  1 
ATOM   2440 N  N   . PHE B 2 189 ? 99.488  203.073 7.518   1.00 37.66  ? 190 PHE B N   1 
ATOM   2441 C  CA  . PHE B 2 189 ? 99.063  201.859 6.869   1.00 35.85  ? 190 PHE B CA  1 
ATOM   2442 C  C   . PHE B 2 189 ? 100.197 201.502 5.922   1.00 37.56  ? 190 PHE B C   1 
ATOM   2443 O  O   . PHE B 2 189 ? 100.619 202.333 5.135   1.00 34.36  ? 190 PHE B O   1 
ATOM   2444 C  CB  . PHE B 2 189 ? 97.751  202.040 6.116   1.00 35.65  ? 190 PHE B CB  1 
ATOM   2445 C  CG  . PHE B 2 189 ? 97.088  200.740 5.764   1.00 37.33  ? 190 PHE B CG  1 
ATOM   2446 C  CD1 . PHE B 2 189 ? 97.495  200.029 4.667   1.00 29.88  ? 190 PHE B CD1 1 
ATOM   2447 C  CD2 . PHE B 2 189 ? 96.040  200.241 6.529   1.00 43.16  ? 190 PHE B CD2 1 
ATOM   2448 C  CE1 . PHE B 2 189 ? 96.911  198.825 4.343   1.00 39.27  ? 190 PHE B CE1 1 
ATOM   2449 C  CE2 . PHE B 2 189 ? 95.442  199.032 6.208   1.00 43.88  ? 190 PHE B CE2 1 
ATOM   2450 C  CZ  . PHE B 2 189 ? 95.878  198.327 5.105   1.00 39.63  ? 190 PHE B CZ  1 
ATOM   2451 N  N   . VAL B 2 190 ? 100.702 200.278 6.025   1.00 33.66  ? 191 VAL B N   1 
ATOM   2452 C  CA  . VAL B 2 190 ? 101.903 199.869 5.311   1.00 35.84  ? 191 VAL B CA  1 
ATOM   2453 C  C   . VAL B 2 190 ? 101.652 198.560 4.583   1.00 42.47  ? 191 VAL B C   1 
ATOM   2454 O  O   . VAL B 2 190 ? 101.135 197.606 5.174   1.00 47.66  ? 191 VAL B O   1 
ATOM   2455 C  CB  . VAL B 2 190 ? 103.121 199.694 6.271   1.00 37.92  ? 191 VAL B CB  1 
ATOM   2456 C  CG1 . VAL B 2 190 ? 104.358 199.229 5.512   1.00 36.57  ? 191 VAL B CG1 1 
ATOM   2457 C  CG2 . VAL B 2 190 ? 103.422 200.971 7.000   1.00 30.92  ? 191 VAL B CG2 1 
ATOM   2458 N  N   . ILE B 2 191 ? 101.996 198.520 3.298   1.00 40.06  ? 192 ILE B N   1 
ATOM   2459 C  CA  . ILE B 2 191 ? 101.944 197.284 2.522   1.00 38.43  ? 192 ILE B CA  1 
ATOM   2460 C  C   . ILE B 2 191 ? 103.338 196.954 1.988   1.00 48.50  ? 192 ILE B C   1 
ATOM   2461 O  O   . ILE B 2 191 ? 104.039 197.830 1.469   1.00 43.10  ? 192 ILE B O   1 
ATOM   2462 C  CB  . ILE B 2 191 ? 100.955 197.369 1.369   1.00 36.62  ? 192 ILE B CB  1 
ATOM   2463 C  CG1 . ILE B 2 191 ? 99.536  197.485 1.897   1.00 37.52  ? 192 ILE B CG1 1 
ATOM   2464 C  CG2 . ILE B 2 191 ? 101.029 196.120 0.510   1.00 41.56  ? 192 ILE B CG2 1 
ATOM   2465 C  CD1 . ILE B 2 191 ? 98.502  197.546 0.802   1.00 33.20  ? 192 ILE B CD1 1 
ATOM   2466 N  N   . SER B 2 192 ? 103.772 195.707 2.171   1.00 51.44  ? 193 SER B N   1 
ATOM   2467 C  CA  . SER B 2 192 ? 105.092 195.316 1.687   1.00 53.14  ? 193 SER B CA  1 
ATOM   2468 C  C   . SER B 2 192 ? 105.213 193.869 1.234   1.00 54.70  ? 193 SER B C   1 
ATOM   2469 O  O   . SER B 2 192 ? 104.392 193.009 1.575   1.00 51.87  ? 193 SER B O   1 
ATOM   2470 C  CB  . SER B 2 192 ? 106.131 195.588 2.768   1.00 45.20  ? 193 SER B CB  1 
ATOM   2471 O  OG  . SER B 2 192 ? 105.694 195.028 3.983   1.00 53.34  ? 193 SER B OG  1 
ATOM   2472 N  N   . LYS B 2 193 ? 106.267 193.613 0.470   1.00 48.55  ? 194 LYS B N   1 
ATOM   2473 C  CA  . LYS B 2 193 ? 106.598 192.269 0.059   1.00 50.08  ? 194 LYS B CA  1 
ATOM   2474 C  C   . LYS B 2 193 ? 108.105 192.158 0.017   1.00 53.81  ? 194 LYS B C   1 
ATOM   2475 O  O   . LYS B 2 193 ? 108.781 193.109 -0.350  1.00 52.22  ? 194 LYS B O   1 
ATOM   2476 C  CB  . LYS B 2 193 ? 106.008 191.947 -1.309  1.00 44.51  ? 194 LYS B CB  1 
ATOM   2477 C  CG  . LYS B 2 193 ? 106.204 190.511 -1.720  1.00 39.70  ? 194 LYS B CG  1 
ATOM   2478 C  CD  . LYS B 2 193 ? 105.739 190.273 -3.121  1.00 49.42  ? 194 LYS B CD  1 
ATOM   2479 C  CE  . LYS B 2 193 ? 106.710 190.885 -4.103  1.00 52.55  ? 194 LYS B CE  1 
ATOM   2480 N  NZ  . LYS B 2 193 ? 108.018 190.145 -4.059  1.00 48.95  1 194 LYS B NZ  1 
ATOM   2481 N  N   . SER B 2 194 ? 108.631 190.993 0.375   1.00 56.99  ? 195 SER B N   1 
ATOM   2482 C  CA  . SER B 2 194 ? 110.051 190.741 0.225   1.00 49.01  ? 195 SER B CA  1 
ATOM   2483 C  C   . SER B 2 194 ? 110.425 190.896 -1.237  1.00 53.55  ? 195 SER B C   1 
ATOM   2484 O  O   . SER B 2 194 ? 109.699 190.437 -2.117  1.00 52.77  ? 195 SER B O   1 
ATOM   2485 C  CB  . SER B 2 194 ? 110.427 189.349 0.723   1.00 48.71  ? 195 SER B CB  1 
ATOM   2486 O  OG  . SER B 2 194 ? 110.036 189.155 2.067   1.00 72.59  ? 195 SER B OG  1 
ATOM   2487 N  N   . LEU B 2 195 ? 111.513 191.609 -1.499  1.00 54.10  ? 196 LEU B N   1 
ATOM   2488 C  CA  . LEU B 2 195 ? 112.020 191.712 -2.858  1.00 55.99  ? 196 LEU B CA  1 
ATOM   2489 C  C   . LEU B 2 195 ? 112.447 190.334 -3.345  1.00 62.66  ? 196 LEU B C   1 
ATOM   2490 O  O   . LEU B 2 195 ? 113.016 189.556 -2.579  1.00 63.41  ? 196 LEU B O   1 
ATOM   2491 C  CB  . LEU B 2 195 ? 113.185 192.687 -2.907  1.00 53.16  ? 196 LEU B CB  1 
ATOM   2492 C  CG  . LEU B 2 195 ? 112.740 194.122 -2.672  1.00 56.36  ? 196 LEU B CG  1 
ATOM   2493 C  CD1 . LEU B 2 195 ? 113.848 194.919 -2.026  1.00 68.14  ? 196 LEU B CD1 1 
ATOM   2494 C  CD2 . LEU B 2 195 ? 112.328 194.756 -3.989  1.00 55.78  ? 196 LEU B CD2 1 
ATOM   2495 N  N   . ASN B 2 196 ? 112.167 190.020 -4.604  1.00 62.18  ? 197 ASN B N   1 
ATOM   2496 C  CA  . ASN B 2 196 ? 112.701 188.795 -5.182  1.00 68.26  ? 197 ASN B CA  1 
ATOM   2497 C  C   . ASN B 2 196 ? 114.209 188.906 -5.313  1.00 65.38  ? 197 ASN B C   1 
ATOM   2498 O  O   . ASN B 2 196 ? 114.939 187.948 -5.087  1.00 74.15  ? 197 ASN B O   1 
ATOM   2499 C  CB  . ASN B 2 196 ? 112.085 188.500 -6.546  1.00 66.03  ? 197 ASN B CB  1 
ATOM   2500 C  CG  . ASN B 2 196 ? 110.609 188.189 -6.460  1.00 62.72  ? 197 ASN B CG  1 
ATOM   2501 O  OD1 . ASN B 2 196 ? 110.104 187.839 -5.400  1.00 64.33  ? 197 ASN B OD1 1 
ATOM   2502 N  ND2 . ASN B 2 196 ? 109.909 188.305 -7.584  1.00 66.04  ? 197 ASN B ND2 1 
ATOM   2503 N  N   . HIS B 2 197 ? 114.676 190.094 -5.659  1.00 68.37  ? 198 HIS B N   1 
ATOM   2504 C  CA  . HIS B 2 197 ? 116.096 190.297 -5.875  1.00 70.92  ? 198 HIS B CA  1 
ATOM   2505 C  C   . HIS B 2 197 ? 116.636 191.442 -5.037  1.00 65.06  ? 198 HIS B C   1 
ATOM   2506 O  O   . HIS B 2 197 ? 116.842 192.543 -5.542  1.00 68.80  ? 198 HIS B O   1 
ATOM   2507 C  CB  . HIS B 2 197 ? 116.365 190.536 -7.365  1.00 73.84  ? 198 HIS B CB  1 
ATOM   2508 C  CG  . HIS B 2 197 ? 115.924 189.402 -8.246  1.00 78.38  ? 198 HIS B CG  1 
ATOM   2509 N  ND1 . HIS B 2 197 ? 116.450 188.129 -8.142  1.00 76.43  ? 198 HIS B ND1 1 
ATOM   2510 C  CD2 . HIS B 2 197 ? 115.017 189.352 -9.250  1.00 78.71  ? 198 HIS B CD2 1 
ATOM   2511 C  CE1 . HIS B 2 197 ? 115.877 187.344 -9.037  1.00 77.65  ? 198 HIS B CE1 1 
ATOM   2512 N  NE2 . HIS B 2 197 ? 115.004 188.061 -9.723  1.00 75.97  ? 198 HIS B NE2 1 
ATOM   2513 N  N   . PRO B 2 198 ? 116.851 191.183 -3.740  1.00 66.82  ? 199 PRO B N   1 
ATOM   2514 C  CA  . PRO B 2 198 ? 117.418 192.165 -2.806  1.00 72.90  ? 199 PRO B CA  1 
ATOM   2515 C  C   . PRO B 2 198 ? 118.811 192.612 -3.238  1.00 78.51  ? 199 PRO B C   1 
ATOM   2516 O  O   . PRO B 2 198 ? 119.231 193.745 -2.960  1.00 78.81  ? 199 PRO B O   1 
ATOM   2517 C  CB  . PRO B 2 198 ? 117.492 191.394 -1.477  1.00 67.72  ? 199 PRO B CB  1 
ATOM   2518 C  CG  . PRO B 2 198 ? 116.550 190.236 -1.643  1.00 74.64  ? 199 PRO B CG  1 
ATOM   2519 C  CD  . PRO B 2 198 ? 116.587 189.886 -3.093  1.00 57.70  ? 199 PRO B CD  1 
ATOM   2520 N  N   . GLU B 2 199 ? 119.511 191.695 -3.902  1.00 77.45  ? 200 GLU B N   1 
ATOM   2521 C  CA  . GLU B 2 199 ? 120.842 191.914 -4.459  1.00 77.77  ? 200 GLU B CA  1 
ATOM   2522 C  C   . GLU B 2 199 ? 120.944 193.158 -5.325  1.00 86.08  ? 200 GLU B C   1 
ATOM   2523 O  O   . GLU B 2 199 ? 121.810 194.004 -5.115  1.00 94.79  ? 200 GLU B O   1 
ATOM   2524 C  CB  . GLU B 2 199 ? 121.244 190.699 -5.277  1.00 76.64  ? 200 GLU B CB  1 
ATOM   2525 C  CG  . GLU B 2 199 ? 120.651 189.418 -4.739  1.00 79.35  ? 200 GLU B CG  1 
ATOM   2526 C  CD  . GLU B 2 199 ? 119.713 188.763 -5.722  1.00 84.65  ? 200 GLU B CD  1 
ATOM   2527 O  OE1 . GLU B 2 199 ? 119.967 188.861 -6.946  1.00 87.28  ? 200 GLU B OE1 1 
ATOM   2528 O  OE2 . GLU B 2 199 ? 118.720 188.155 -5.268  1.00 85.25  1 200 GLU B OE2 1 
ATOM   2529 N  N   . ASN B 2 200 ? 120.062 193.250 -6.313  1.00 83.54  ? 201 ASN B N   1 
ATOM   2530 C  CA  . ASN B 2 200 ? 120.081 194.339 -7.283  1.00 78.92  ? 201 ASN B CA  1 
ATOM   2531 C  C   . ASN B 2 200 ? 119.697 195.694 -6.689  1.00 84.19  ? 201 ASN B C   1 
ATOM   2532 O  O   . ASN B 2 200 ? 119.809 196.722 -7.355  1.00 87.84  ? 201 ASN B O   1 
ATOM   2533 C  CB  . ASN B 2 200 ? 119.149 194.007 -8.447  1.00 75.51  ? 201 ASN B CB  1 
ATOM   2534 C  CG  . ASN B 2 200 ? 119.457 192.662 -9.071  1.00 80.17  ? 201 ASN B CG  1 
ATOM   2535 O  OD1 . ASN B 2 200 ? 120.612 192.232 -9.113  1.00 89.11  ? 201 ASN B OD1 1 
ATOM   2536 N  ND2 . ASN B 2 200 ? 118.423 191.988 -9.562  1.00 82.13  ? 201 ASN B ND2 1 
ATOM   2537 N  N   . GLU B 2 201 ? 119.251 195.690 -5.438  1.00 79.40  ? 202 GLU B N   1 
ATOM   2538 C  CA  . GLU B 2 201 ? 118.866 196.917 -4.756  1.00 83.41  ? 202 GLU B CA  1 
ATOM   2539 C  C   . GLU B 2 201 ? 119.978 197.421 -3.863  1.00 86.02  ? 202 GLU B C   1 
ATOM   2540 O  O   . GLU B 2 201 ? 120.254 196.834 -2.820  1.00 87.91  ? 202 GLU B O   1 
ATOM   2541 C  CB  . GLU B 2 201 ? 117.590 196.711 -3.934  1.00 81.12  ? 202 GLU B CB  1 
ATOM   2542 C  CG  . GLU B 2 201 ? 116.341 196.404 -4.757  1.00 75.82  ? 202 GLU B CG  1 
ATOM   2543 C  CD  . GLU B 2 201 ? 116.017 197.496 -5.770  1.00 77.43  ? 202 GLU B CD  1 
ATOM   2544 O  OE1 . GLU B 2 201 ? 116.411 198.665 -5.547  1.00 75.48  ? 202 GLU B OE1 1 
ATOM   2545 O  OE2 . GLU B 2 201 ? 115.350 197.193 -6.784  1.00 72.92  1 202 GLU B OE2 1 
ATOM   2546 N  N   . PRO B 2 202 ? 120.636 198.507 -4.289  1.00 97.21  ? 203 PRO B N   1 
ATOM   2547 C  CA  . PRO B 2 202 ? 121.823 199.062 -3.629  1.00 100.14 ? 203 PRO B CA  1 
ATOM   2548 C  C   . PRO B 2 202 ? 121.535 199.475 -2.192  1.00 98.94  ? 203 PRO B C   1 
ATOM   2549 O  O   . PRO B 2 202 ? 122.404 199.384 -1.317  1.00 97.03  ? 203 PRO B O   1 
ATOM   2550 C  CB  . PRO B 2 202 ? 122.160 200.292 -4.482  1.00 95.80  ? 203 PRO B CB  1 
ATOM   2551 C  CG  . PRO B 2 202 ? 120.863 200.663 -5.133  1.00 94.34  ? 203 PRO B CG  1 
ATOM   2552 C  CD  . PRO B 2 202 ? 120.172 199.360 -5.397  1.00 90.66  ? 203 PRO B CD  1 
ATOM   2553 N  N   . SER B 2 203 ? 120.292 199.881 -1.953  1.00 90.36  ? 204 SER B N   1 
ATOM   2554 C  CA  . SER B 2 203 ? 119.890 200.512 -0.698  1.00 96.23  ? 204 SER B CA  1 
ATOM   2555 C  C   . SER B 2 203 ? 120.016 199.603 0.539   1.00 97.79  ? 204 SER B C   1 
ATOM   2556 O  O   . SER B 2 203 ? 119.683 200.021 1.655   1.00 96.65  ? 204 SER B O   1 
ATOM   2557 C  CB  . SER B 2 203 ? 118.447 201.024 -0.827  1.00 93.57  ? 204 SER B CB  1 
ATOM   2558 O  OG  . SER B 2 203 ? 118.275 202.293 -0.214  1.00 85.79  ? 204 SER B OG  1 
ATOM   2559 N  N   . SER B 2 204 ? 120.477 198.367 0.338   1.00 90.38  ? 205 SER B N   1 
ATOM   2560 C  CA  . SER B 2 204 ? 120.519 197.365 1.404   1.00 91.34  ? 205 SER B CA  1 
ATOM   2561 C  C   . SER B 2 204 ? 119.101 197.135 1.938   1.00 95.82  ? 205 SER B C   1 
ATOM   2562 O  O   . SER B 2 204 ? 118.899 196.703 3.079   1.00 87.41  ? 205 SER B O   1 
ATOM   2563 C  CB  . SER B 2 204 ? 121.466 197.808 2.524   1.00 88.02  ? 205 SER B CB  1 
ATOM   2564 O  OG  . SER B 2 204 ? 122.724 198.191 1.995   1.00 88.43  ? 205 SER B OG  1 
ATOM   2565 N  N   . VAL B 2 205 ? 118.131 197.448 1.085   1.00 88.06  ? 206 VAL B N   1 
ATOM   2566 C  CA  . VAL B 2 205 ? 116.722 197.297 1.379   1.00 71.31  ? 206 VAL B CA  1 
ATOM   2567 C  C   . VAL B 2 205 ? 116.233 195.922 0.953   1.00 77.04  ? 206 VAL B C   1 
ATOM   2568 O  O   . VAL B 2 205 ? 116.525 195.452 -0.150  1.00 72.63  ? 206 VAL B O   1 
ATOM   2569 C  CB  . VAL B 2 205 ? 115.896 198.387 0.676   1.00 82.45  ? 206 VAL B CB  1 
ATOM   2570 C  CG1 . VAL B 2 205 ? 116.197 198.409 -0.822  1.00 75.00  ? 206 VAL B CG1 1 
ATOM   2571 C  CG2 . VAL B 2 205 ? 114.420 198.171 0.924   1.00 78.64  ? 206 VAL B CG2 1 
ATOM   2572 N  N   . LYS B 2 206 ? 115.517 195.261 1.851   1.00 74.12  ? 207 LYS B N   1 
ATOM   2573 C  CA  . LYS B 2 206 ? 115.077 193.893 1.620   1.00 73.49  ? 207 LYS B CA  1 
ATOM   2574 C  C   . LYS B 2 206 ? 113.616 193.842 1.172   1.00 69.17  ? 207 LYS B C   1 
ATOM   2575 O  O   . LYS B 2 206 ? 113.194 192.875 0.531   1.00 66.12  ? 207 LYS B O   1 
ATOM   2576 C  CB  . LYS B 2 206 ? 115.343 193.053 2.872   1.00 77.04  ? 207 LYS B CB  1 
ATOM   2577 C  CG  . LYS B 2 206 ? 116.805 193.205 3.333   1.00 79.16  ? 207 LYS B CG  1 
ATOM   2578 C  CD  . LYS B 2 206 ? 117.110 192.618 4.707   1.00 79.69  ? 207 LYS B CD  1 
ATOM   2579 C  CE  . LYS B 2 206 ? 118.536 192.982 5.136   1.00 75.08  ? 207 LYS B CE  1 
ATOM   2580 N  NZ  . LYS B 2 206 ? 118.914 192.455 6.483   1.00 76.72  1 207 LYS B NZ  1 
ATOM   2581 N  N   . ASP B 2 207 ? 112.865 194.909 1.453   1.00 67.11  ? 208 ASP B N   1 
ATOM   2582 C  CA  . ASP B 2 207 ? 111.421 194.923 1.194   1.00 63.30  ? 208 ASP B CA  1 
ATOM   2583 C  C   . ASP B 2 207 ? 110.964 195.998 0.210   1.00 58.64  ? 208 ASP B C   1 
ATOM   2584 O  O   . ASP B 2 207 ? 111.526 197.086 0.139   1.00 58.02  ? 208 ASP B O   1 
ATOM   2585 C  CB  . ASP B 2 207 ? 110.636 195.129 2.493   1.00 61.43  ? 208 ASP B CB  1 
ATOM   2586 C  CG  . ASP B 2 207 ? 110.601 193.897 3.367   1.00 71.16  ? 208 ASP B CG  1 
ATOM   2587 O  OD1 . ASP B 2 207 ? 110.707 192.775 2.831   1.00 75.74  ? 208 ASP B OD1 1 
ATOM   2588 O  OD2 . ASP B 2 207 ? 110.454 194.051 4.598   1.00 80.15  1 208 ASP B OD2 1 
ATOM   2589 N  N   . TYR B 2 208 ? 109.911 195.674 -0.530  1.00 48.77  ? 209 TYR B N   1 
ATOM   2590 C  CA  . TYR B 2 208 ? 109.211 196.631 -1.373  1.00 47.43  ? 209 TYR B CA  1 
ATOM   2591 C  C   . TYR B 2 208 ? 107.987 197.097 -0.606  1.00 49.99  ? 209 TYR B C   1 
ATOM   2592 O  O   . TYR B 2 208 ? 107.059 196.322 -0.387  1.00 44.13  ? 209 TYR B O   1 
ATOM   2593 C  CB  . TYR B 2 208 ? 108.800 196.000 -2.702  1.00 46.05  ? 209 TYR B CB  1 
ATOM   2594 C  CG  . TYR B 2 208 ? 108.135 196.954 -3.661  1.00 46.12  ? 209 TYR B CG  1 
ATOM   2595 C  CD1 . TYR B 2 208 ? 108.885 197.740 -4.530  1.00 43.81  ? 209 TYR B CD1 1 
ATOM   2596 C  CD2 . TYR B 2 208 ? 106.746 197.084 -3.684  1.00 49.50  ? 209 TYR B CD2 1 
ATOM   2597 C  CE1 . TYR B 2 208 ? 108.269 198.618 -5.400  1.00 54.58  ? 209 TYR B CE1 1 
ATOM   2598 C  CE2 . TYR B 2 208 ? 106.124 197.965 -4.541  1.00 46.47  ? 209 TYR B CE2 1 
ATOM   2599 C  CZ  . TYR B 2 208 ? 106.888 198.731 -5.396  1.00 52.84  ? 209 TYR B CZ  1 
ATOM   2600 O  OH  . TYR B 2 208 ? 106.272 199.603 -6.254  1.00 48.74  ? 209 TYR B OH  1 
ATOM   2601 N  N   . SER B 2 209 ? 108.001 198.356 -0.182  1.00 48.69  ? 210 SER B N   1 
ATOM   2602 C  CA  . SER B 2 209 ? 106.982 198.888 0.719   1.00 41.04  ? 210 SER B CA  1 
ATOM   2603 C  C   . SER B 2 209 ? 106.357 200.158 0.170   1.00 40.19  ? 210 SER B C   1 
ATOM   2604 O  O   . SER B 2 209 ? 107.042 200.990 -0.436  1.00 33.84  ? 210 SER B O   1 
ATOM   2605 C  CB  . SER B 2 209 ? 107.575 199.190 2.100   1.00 40.36  ? 210 SER B CB  1 
ATOM   2606 O  OG  . SER B 2 209 ? 108.296 198.098 2.641   1.00 52.43  ? 210 SER B OG  1 
ATOM   2607 N  N   . PHE B 2 210 ? 105.048 200.278 0.358   1.00 37.42  ? 211 PHE B N   1 
ATOM   2608 C  CA  . PHE B 2 210 ? 104.335 201.528 0.130   1.00 40.28  ? 211 PHE B CA  1 
ATOM   2609 C  C   . PHE B 2 210 ? 103.321 201.764 1.251   1.00 42.29  ? 211 PHE B C   1 
ATOM   2610 O  O   . PHE B 2 210 ? 102.703 200.819 1.768   1.00 36.17  ? 211 PHE B O   1 
ATOM   2611 C  CB  . PHE B 2 210 ? 103.651 201.570 -1.248  1.00 32.36  ? 211 PHE B CB  1 
ATOM   2612 C  CG  . PHE B 2 210 ? 103.014 200.271 -1.690  1.00 44.06  ? 211 PHE B CG  1 
ATOM   2613 C  CD1 . PHE B 2 210 ? 103.784 199.220 -2.165  1.00 45.92  ? 211 PHE B CD1 1 
ATOM   2614 C  CD2 . PHE B 2 210 ? 101.639 200.135 -1.707  1.00 42.96  ? 211 PHE B CD2 1 
ATOM   2615 C  CE1 . PHE B 2 210 ? 103.189 198.055 -2.608  1.00 47.24  ? 211 PHE B CE1 1 
ATOM   2616 C  CE2 . PHE B 2 210 ? 101.045 198.982 -2.153  1.00 42.81  ? 211 PHE B CE2 1 
ATOM   2617 C  CZ  . PHE B 2 210 ? 101.813 197.940 -2.600  1.00 40.09  ? 211 PHE B CZ  1 
ATOM   2618 N  N   . LEU B 2 211 ? 103.158 203.029 1.624   1.00 38.32  ? 212 LEU B N   1 
ATOM   2619 C  CA  . LEU B 2 211 ? 102.476 203.363 2.873   1.00 41.04  ? 212 LEU B CA  1 
ATOM   2620 C  C   . LEU B 2 211 ? 101.860 204.753 2.845   1.00 37.05  ? 212 LEU B C   1 
ATOM   2621 O  O   . LEU B 2 211 ? 102.135 205.533 1.937   1.00 36.61  ? 212 LEU B O   1 
ATOM   2622 C  CB  . LEU B 2 211 ? 103.441 203.259 4.061   1.00 38.62  ? 212 LEU B CB  1 
ATOM   2623 C  CG  . LEU B 2 211 ? 104.562 204.293 4.088   1.00 35.72  ? 212 LEU B CG  1 
ATOM   2624 C  CD1 . LEU B 2 211 ? 105.099 204.417 5.496   1.00 30.04  ? 212 LEU B CD1 1 
ATOM   2625 C  CD2 . LEU B 2 211 ? 105.679 203.911 3.120   1.00 35.30  ? 212 LEU B CD2 1 
ATOM   2626 N  N   . GLY B 2 212 ? 100.999 205.022 3.822   1.00 34.58  ? 213 GLY B N   1 
ATOM   2627 C  CA  . GLY B 2 212 ? 100.408 206.324 4.009   1.00 36.83  ? 213 GLY B CA  1 
ATOM   2628 C  C   . GLY B 2 212 ? 99.842  206.537 5.406   1.00 43.20  ? 213 GLY B C   1 
ATOM   2629 O  O   . GLY B 2 212 ? 99.450  205.595 6.086   1.00 40.65  ? 213 GLY B O   1 
ATOM   2630 N  N   . VAL B 2 213 ? 99.786  207.787 5.841   1.00 35.87  ? 214 VAL B N   1 
ATOM   2631 C  CA  . VAL B 2 213 ? 99.140  208.081 7.100   1.00 35.86  ? 214 VAL B CA  1 
ATOM   2632 C  C   . VAL B 2 213 ? 97.635  207.822 6.969   1.00 37.78  ? 214 VAL B C   1 
ATOM   2633 O  O   . VAL B 2 213 ? 96.993  208.195 5.978   1.00 34.82  ? 214 VAL B O   1 
ATOM   2634 C  CB  . VAL B 2 213 ? 99.389  209.534 7.546   1.00 39.82  ? 214 VAL B CB  1 
ATOM   2635 C  CG1 . VAL B 2 213 ? 98.772  209.779 8.935   1.00 32.89  ? 214 VAL B CG1 1 
ATOM   2636 C  CG2 . VAL B 2 213 ? 100.886 209.817 7.573   1.00 27.31  ? 214 VAL B CG2 1 
ATOM   2637 N  N   . ILE B 2 214 ? 97.074  207.139 7.957   1.00 33.00  ? 215 ILE B N   1 
ATOM   2638 C  CA  . ILE B 2 214 ? 95.649  206.906 7.961   1.00 35.12  ? 215 ILE B CA  1 
ATOM   2639 C  C   . ILE B 2 214 ? 94.923  208.207 8.308   1.00 36.83  ? 215 ILE B C   1 
ATOM   2640 O  O   . ILE B 2 214 ? 95.120  208.770 9.379   1.00 39.00  ? 215 ILE B O   1 
ATOM   2641 C  CB  . ILE B 2 214 ? 95.294  205.810 8.939   1.00 35.29  ? 215 ILE B CB  1 
ATOM   2642 C  CG1 . ILE B 2 214 ? 95.988  204.520 8.490   1.00 33.75  ? 215 ILE B CG1 1 
ATOM   2643 C  CG2 . ILE B 2 214 ? 93.780  205.667 9.042   1.00 31.42  ? 215 ILE B CG2 1 
ATOM   2644 C  CD1 . ILE B 2 214 ? 95.968  203.415 9.498   1.00 35.83  ? 215 ILE B CD1 1 
ATOM   2645 N  N   . ALA B 2 215 ? 94.097  208.676 7.381   1.00 37.11  ? 216 ALA B N   1 
ATOM   2646 C  CA  . ALA B 2 215 ? 93.525  210.018 7.450   1.00 36.50  ? 216 ALA B CA  1 
ATOM   2647 C  C   . ALA B 2 215 ? 92.035  209.979 7.671   1.00 35.74  ? 216 ALA B C   1 
ATOM   2648 O  O   . ALA B 2 215 ? 91.343  209.096 7.142   1.00 36.02  ? 216 ALA B O   1 
ATOM   2649 C  CB  . ALA B 2 215 ? 93.824  210.771 6.181   1.00 25.79  ? 216 ALA B CB  1 
ATOM   2650 N  N   . ARG B 2 216 ? 91.532  210.952 8.425   1.00 32.69  ? 217 ARG B N   1 
ATOM   2651 C  CA  . ARG B 2 216 ? 90.096  211.108 8.590   1.00 29.35  ? 217 ARG B CA  1 
ATOM   2652 C  C   . ARG B 2 216 ? 89.521  211.386 7.241   1.00 29.02  ? 217 ARG B C   1 
ATOM   2653 O  O   . ARG B 2 216 ? 90.135  212.105 6.437   1.00 29.77  ? 217 ARG B O   1 
ATOM   2654 C  CB  . ARG B 2 216 ? 89.758  212.228 9.565   1.00 29.39  ? 217 ARG B CB  1 
ATOM   2655 C  CG  . ARG B 2 216 ? 90.370  212.060 10.944  1.00 30.76  ? 217 ARG B CG  1 
ATOM   2656 C  CD  . ARG B 2 216 ? 90.169  213.335 11.721  1.00 26.70  ? 217 ARG B CD  1 
ATOM   2657 N  NE  . ARG B 2 216 ? 90.893  213.349 12.975  1.00 41.50  ? 217 ARG B NE  1 
ATOM   2658 C  CZ  . ARG B 2 216 ? 90.371  213.026 14.152  1.00 39.62  ? 217 ARG B CZ  1 
ATOM   2659 N  NH1 . ARG B 2 216 ? 89.100  212.647 14.249  1.00 34.15  1 217 ARG B NH1 1 
ATOM   2660 N  NH2 . ARG B 2 216 ? 91.131  213.098 15.229  1.00 38.93  ? 217 ARG B NH2 1 
ATOM   2661 N  N   . SER B 2 217 ? 88.358  210.802 6.979   1.00 33.24  ? 218 SER B N   1 
ATOM   2662 C  CA  . SER B 2 217 ? 87.683  210.971 5.695   1.00 35.11  ? 218 SER B CA  1 
ATOM   2663 C  C   . SER B 2 217 ? 86.194  211.069 5.915   1.00 39.47  ? 218 SER B C   1 
ATOM   2664 O  O   . SER B 2 217 ? 85.664  210.471 6.845   1.00 42.31  ? 218 SER B O   1 
ATOM   2665 C  CB  . SER B 2 217 ? 87.994  209.804 4.740   1.00 36.30  ? 218 SER B CB  1 
ATOM   2666 O  OG  . SER B 2 217 ? 87.262  209.905 3.517   1.00 36.49  ? 218 SER B OG  1 
ATOM   2667 N  N   . ALA B 2 218 ? 85.515  211.822 5.057   1.00 39.38  ? 219 ALA B N   1 
ATOM   2668 C  CA  . ALA B 2 218 ? 84.065  211.905 5.125   1.00 37.91  ? 219 ALA B CA  1 
ATOM   2669 C  C   . ALA B 2 218 ? 83.437  210.580 4.697   1.00 46.88  ? 219 ALA B C   1 
ATOM   2670 O  O   . ALA B 2 218 ? 82.312  210.257 5.094   1.00 53.44  ? 219 ALA B O   1 
ATOM   2671 C  CB  . ALA B 2 218 ? 83.560  213.044 4.253   1.00 33.70  ? 219 ALA B CB  1 
ATOM   2672 N  N   . GLY B 2 219 ? 84.177  209.819 3.890   1.00 42.31  ? 220 GLY B N   1 
ATOM   2673 C  CA  . GLY B 2 219 ? 83.726  208.523 3.431   1.00 46.26  ? 220 GLY B CA  1 
ATOM   2674 C  C   . GLY B 2 219 ? 82.702  208.604 2.311   1.00 50.09  ? 220 GLY B C   1 
ATOM   2675 O  O   . GLY B 2 219 ? 81.983  207.640 2.049   1.00 53.60  ? 220 GLY B O   1 
ATOM   2676 N  N   . VAL B 2 220 ? 82.629  209.757 1.656   1.00 46.15  ? 221 VAL B N   1 
ATOM   2677 C  CA  . VAL B 2 220 ? 81.790  209.917 0.472   1.00 56.51  ? 221 VAL B CA  1 
ATOM   2678 C  C   . VAL B 2 220 ? 82.623  209.733 -0.789  1.00 54.72  ? 221 VAL B C   1 
ATOM   2679 O  O   . VAL B 2 220 ? 82.964  210.690 -1.477  1.00 59.75  ? 221 VAL B O   1 
ATOM   2680 C  CB  . VAL B 2 220 ? 81.096  211.279 0.457   1.00 59.40  ? 221 VAL B CB  1 
ATOM   2681 C  CG1 . VAL B 2 220 ? 80.146  211.377 -0.743  1.00 71.99  ? 221 VAL B CG1 1 
ATOM   2682 C  CG2 . VAL B 2 220 ? 80.314  211.457 1.750   1.00 52.79  ? 221 VAL B CG2 1 
ATOM   2683 N  N   . TRP B 2 221 ? 82.962  208.482 -1.071  1.00 57.44  ? 222 TRP B N   1 
ATOM   2684 C  CA  . TRP B 2 221 ? 83.823  208.157 -2.194  1.00 61.13  ? 222 TRP B CA  1 
ATOM   2685 C  C   . TRP B 2 221 ? 82.976  207.843 -3.408  1.00 66.04  ? 222 TRP B C   1 
ATOM   2686 O  O   . TRP B 2 221 ? 81.849  207.343 -3.294  1.00 66.62  ? 222 TRP B O   1 
ATOM   2687 C  CB  . TRP B 2 221 ? 84.725  206.961 -1.878  1.00 57.44  ? 222 TRP B CB  1 
ATOM   2688 C  CG  . TRP B 2 221 ? 85.435  207.098 -0.597  1.00 55.77  ? 222 TRP B CG  1 
ATOM   2689 C  CD1 . TRP B 2 221 ? 86.335  208.075 -0.242  1.00 61.81  ? 222 TRP B CD1 1 
ATOM   2690 C  CD2 . TRP B 2 221 ? 85.330  206.224 0.524   1.00 51.85  ? 222 TRP B CD2 1 
ATOM   2691 N  NE1 . TRP B 2 221 ? 86.780  207.865 1.049   1.00 50.61  ? 222 TRP B NE1 1 
ATOM   2692 C  CE2 . TRP B 2 221 ? 86.181  206.735 1.539   1.00 47.62  ? 222 TRP B CE2 1 
ATOM   2693 C  CE3 . TRP B 2 221 ? 84.597  205.062 0.774   1.00 49.94  ? 222 TRP B CE3 1 
ATOM   2694 C  CZ2 . TRP B 2 221 ? 86.315  206.120 2.779   1.00 43.52  ? 222 TRP B CZ2 1 
ATOM   2695 C  CZ3 . TRP B 2 221 ? 84.728  204.453 2.009   1.00 49.50  ? 222 TRP B CZ3 1 
ATOM   2696 C  CH2 . TRP B 2 221 ? 85.586  204.979 2.995   1.00 49.56  ? 222 TRP B CH2 1 
ATOM   2697 N  N   . GLU B 2 222 ? 83.543  208.121 -4.573  1.00 74.77  ? 223 GLU B N   1 
ATOM   2698 C  CA  . GLU B 2 222 ? 82.866  207.882 -5.838  1.00 76.08  ? 223 GLU B CA  1 
ATOM   2699 C  C   . GLU B 2 222 ? 83.155  206.447 -6.270  1.00 76.81  ? 223 GLU B C   1 
ATOM   2700 O  O   . GLU B 2 222 ? 83.899  205.723 -5.598  1.00 72.34  ? 223 GLU B O   1 
ATOM   2701 C  CB  . GLU B 2 222 ? 83.319  208.903 -6.891  1.00 77.33  ? 223 GLU B CB  1 
ATOM   2702 C  CG  . GLU B 2 222 ? 84.713  208.662 -7.474  1.00 81.35  ? 223 GLU B CG  1 
ATOM   2703 C  CD  . GLU B 2 222 ? 85.864  208.901 -6.500  1.00 75.32  ? 223 GLU B CD  1 
ATOM   2704 O  OE1 . GLU B 2 222 ? 85.630  209.212 -5.311  1.00 77.62  ? 223 GLU B OE1 1 
ATOM   2705 O  OE2 . GLU B 2 222 ? 87.023  208.766 -6.938  1.00 68.90  1 223 GLU B OE2 1 
ATOM   2706 N  N   . ASN B 2 223 ? 82.566  206.036 -7.385  1.00 79.46  ? 224 ASN B N   1 
ATOM   2707 C  CA  . ASN B 2 223 ? 82.663  204.652 -7.825  1.00 81.49  ? 224 ASN B CA  1 
ATOM   2708 C  C   . ASN B 2 223 ? 84.100  204.180 -8.124  1.00 79.02  ? 224 ASN B C   1 
ATOM   2709 O  O   . ASN B 2 223 ? 84.548  203.177 -7.566  1.00 83.61  ? 224 ASN B O   1 
ATOM   2710 C  CB  . ASN B 2 223 ? 81.779  204.445 -9.052  1.00 85.49  ? 224 ASN B CB  1 
ATOM   2711 C  CG  . ASN B 2 223 ? 81.734  202.999 -9.490  1.00 95.80  ? 224 ASN B CG  1 
ATOM   2712 O  OD1 . ASN B 2 223 ? 81.782  202.087 -8.659  1.00 98.37  ? 224 ASN B OD1 1 
ATOM   2713 N  ND2 . ASN B 2 223 ? 81.639  202.775 -10.797 1.00 102.67 ? 224 ASN B ND2 1 
ATOM   2714 N  N   . ASN B 2 224 ? 84.813  204.883 -9.002  1.00 72.27  ? 225 ASN B N   1 
ATOM   2715 C  CA  . ASN B 2 224 ? 86.199  204.530 -9.319  1.00 67.16  ? 225 ASN B CA  1 
ATOM   2716 C  C   . ASN B 2 224 ? 87.159  204.892 -8.191  1.00 75.19  ? 225 ASN B C   1 
ATOM   2717 O  O   . ASN B 2 224 ? 87.101  205.985 -7.617  1.00 77.63  ? 225 ASN B O   1 
ATOM   2718 C  CB  . ASN B 2 224 ? 86.653  205.186 -10.625 1.00 73.47  ? 225 ASN B CB  1 
ATOM   2719 C  CG  . ASN B 2 224 ? 86.532  206.701 -10.601 1.00 83.58  ? 225 ASN B CG  1 
ATOM   2720 O  OD1 . ASN B 2 224 ? 85.570  207.255 -10.063 1.00 82.56  ? 225 ASN B OD1 1 
ATOM   2721 N  ND2 . ASN B 2 224 ? 87.502  207.379 -11.205 1.00 88.10  ? 225 ASN B ND2 1 
ATOM   2722 N  N   . LYS B 2 225 ? 88.018  203.946 -7.845  1.00 63.46  ? 226 LYS B N   1 
ATOM   2723 C  CA  . LYS B 2 225 ? 88.935  204.143 -6.738  1.00 56.25  ? 226 LYS B CA  1 
ATOM   2724 C  C   . LYS B 2 225 ? 90.218  204.796 -7.232  1.00 54.17  ? 226 LYS B C   1 
ATOM   2725 O  O   . LYS B 2 225 ? 91.137  204.116 -7.671  1.00 58.98  ? 226 LYS B O   1 
ATOM   2726 C  CB  . LYS B 2 225 ? 89.217  202.803 -6.066  1.00 53.55  ? 226 LYS B CB  1 
ATOM   2727 C  CG  . LYS B 2 225 ? 87.940  202.011 -5.802  1.00 50.24  ? 226 LYS B CG  1 
ATOM   2728 C  CD  . LYS B 2 225 ? 88.228  200.630 -5.262  1.00 45.18  ? 226 LYS B CD  1 
ATOM   2729 C  CE  . LYS B 2 225 ? 86.970  199.959 -4.733  1.00 45.27  ? 226 LYS B CE  1 
ATOM   2730 N  NZ  . LYS B 2 225 ? 87.263  198.535 -4.421  1.00 49.18  1 226 LYS B NZ  1 
ATOM   2731 N  N   . GLN B 2 226 ? 90.281  206.122 -7.151  1.00 49.51  ? 227 GLN B N   1 
ATOM   2732 C  CA  . GLN B 2 226 ? 91.370  206.847 -7.781  1.00 53.96  ? 227 GLN B CA  1 
ATOM   2733 C  C   . GLN B 2 226 ? 92.023  207.872 -6.865  1.00 53.48  ? 227 GLN B C   1 
ATOM   2734 O  O   . GLN B 2 226 ? 91.490  208.225 -5.807  1.00 50.44  ? 227 GLN B O   1 
ATOM   2735 C  CB  . GLN B 2 226 ? 90.870  207.552 -9.038  1.00 54.97  ? 227 GLN B CB  1 
ATOM   2736 C  CG  . GLN B 2 226 ? 89.876  208.652 -8.739  1.00 62.98  ? 227 GLN B CG  1 
ATOM   2737 C  CD  . GLN B 2 226 ? 89.470  209.432 -9.977  1.00 76.86  ? 227 GLN B CD  1 
ATOM   2738 O  OE1 . GLN B 2 226 ? 89.946  209.163 -11.083 1.00 77.25  ? 227 GLN B OE1 1 
ATOM   2739 N  NE2 . GLN B 2 226 ? 88.595  210.418 -9.792  1.00 70.84  ? 227 GLN B NE2 1 
ATOM   2740 N  N   . VAL B 2 227 ? 93.185  208.351 -7.295  1.00 50.32  ? 228 VAL B N   1 
ATOM   2741 C  CA  . VAL B 2 227 ? 93.935  209.336 -6.544  1.00 48.52  ? 228 VAL B CA  1 
ATOM   2742 C  C   . VAL B 2 227 ? 94.403  210.449 -7.451  1.00 43.09  ? 228 VAL B C   1 
ATOM   2743 O  O   . VAL B 2 227 ? 95.074  210.202 -8.446  1.00 54.82  ? 228 VAL B O   1 
ATOM   2744 C  CB  . VAL B 2 227 ? 95.158  208.717 -5.833  1.00 41.08  ? 228 VAL B CB  1 
ATOM   2745 C  CG1 . VAL B 2 227 ? 95.944  209.788 -5.158  1.00 37.52  ? 228 VAL B CG1 1 
ATOM   2746 C  CG2 . VAL B 2 227 ? 94.722  207.670 -4.832  1.00 40.35  ? 228 VAL B CG2 1 
ATOM   2747 N  N   . CYS B 2 228 ? 94.076  211.676 -7.067  1.00 48.86  ? 229 CYS B N   1 
ATOM   2748 C  CA  . CYS B 2 228 ? 94.415  212.855 -7.839  1.00 61.13  ? 229 CYS B CA  1 
ATOM   2749 C  C   . CYS B 2 228 ? 95.596  213.623 -7.242  1.00 65.36  ? 229 CYS B C   1 
ATOM   2750 O  O   . CYS B 2 228 ? 95.871  213.525 -6.044  1.00 64.16  ? 229 CYS B O   1 
ATOM   2751 C  CB  . CYS B 2 228 ? 93.177  213.746 -7.954  1.00 54.47  ? 229 CYS B CB  1 
ATOM   2752 S  SG  . CYS B 2 228 ? 91.791  212.846 -8.738  1.00 62.85  ? 229 CYS B SG  1 
ATOM   2753 N  N   . ALA B 2 229 ? 96.310  214.361 -8.092  1.00 64.22  ? 230 ALA B N   1 
ATOM   2754 C  CA  . ALA B 2 229 ? 97.378  215.256 -7.641  1.00 64.94  ? 230 ALA B CA  1 
ATOM   2755 C  C   . ALA B 2 229 ? 96.777  216.492 -6.967  1.00 68.92  ? 230 ALA B C   1 
ATOM   2756 O  O   . ALA B 2 229 ? 95.567  216.706 -7.064  1.00 75.04  ? 230 ALA B O   1 
ATOM   2757 C  CB  . ALA B 2 229 ? 98.257  215.656 -8.809  1.00 62.70  ? 230 ALA B CB  1 
ATOM   2758 N  N   . CYS B 2 230 ? 97.597  217.292 -6.277  1.00 76.00  ? 231 CYS B N   1 
ATOM   2759 C  CA  . CYS B 2 230 ? 97.135  218.587 -5.737  1.00 76.03  ? 231 CYS B CA  1 
ATOM   2760 C  C   . CYS B 2 230 ? 96.443  219.438 -6.807  1.00 77.75  ? 231 CYS B C   1 
ATOM   2761 O  O   . CYS B 2 230 ? 95.545  220.211 -6.495  1.00 81.98  ? 231 CYS B O   1 
ATOM   2762 C  CB  . CYS B 2 230 ? 98.288  219.374 -5.101  1.00 68.15  ? 231 CYS B CB  1 
ATOM   2763 S  SG  . CYS B 2 230 ? 98.358  219.249 -3.291  1.00 85.54  ? 231 CYS B SG  1 
ATOM   2764 N  N   . THR B 2 231 ? 96.877  219.286 -8.058  1.00 84.43  ? 232 THR B N   1 
ATOM   2765 C  CA  . THR B 2 231 ? 96.225  219.881 -9.228  1.00 84.22  ? 232 THR B CA  1 
ATOM   2766 C  C   . THR B 2 231 ? 94.761  219.494 -9.369  1.00 87.62  ? 232 THR B C   1 
ATOM   2767 O  O   . THR B 2 231 ? 93.900  220.344 -9.574  1.00 91.76  ? 232 THR B O   1 
ATOM   2768 C  CB  . THR B 2 231 ? 96.923  219.448 -10.538 1.00 90.55  ? 232 THR B CB  1 
ATOM   2769 O  OG1 . THR B 2 231 ? 98.311  219.805 -10.491 1.00 91.19  ? 232 THR B OG1 1 
ATOM   2770 C  CG2 . THR B 2 231 ? 96.241  220.084 -11.763 1.00 79.98  ? 232 THR B CG2 1 
ATOM   2771 N  N   . GLY B 2 232 ? 94.494  218.196 -9.255  1.00 83.35  ? 233 GLY B N   1 
ATOM   2772 C  CA  . GLY B 2 232 ? 93.193  217.642 -9.575  1.00 78.73  ? 233 GLY B CA  1 
ATOM   2773 C  C   . GLY B 2 232 ? 93.267  216.587 -10.661 1.00 80.38  ? 233 GLY B C   1 
ATOM   2774 O  O   . GLY B 2 232 ? 92.341  215.782 -10.812 1.00 79.94  ? 233 GLY B O   1 
ATOM   2775 N  N   . LYS B 2 233 ? 94.368  216.588 -11.409 1.00 72.49  ? 234 LYS B N   1 
ATOM   2776 C  CA  . LYS B 2 233 ? 94.640  215.555 -12.407 1.00 70.57  ? 234 LYS B CA  1 
ATOM   2777 C  C   . LYS B 2 233 ? 94.669  214.174 -11.744 1.00 70.20  ? 234 LYS B C   1 
ATOM   2778 O  O   . LYS B 2 233 ? 95.144  214.037 -10.618 1.00 60.98  ? 234 LYS B O   1 
ATOM   2779 C  CB  . LYS B 2 233 ? 95.965  215.822 -13.119 1.00 68.79  ? 234 LYS B CB  1 
ATOM   2780 C  CG  . LYS B 2 233 ? 96.352  214.761 -14.145 1.00 78.22  ? 234 LYS B CG  1 
ATOM   2781 C  CD  . LYS B 2 233 ? 97.867  214.720 -14.361 1.00 87.43  ? 234 LYS B CD  1 
ATOM   2782 C  CE  . LYS B 2 233 ? 98.249  214.158 -15.733 1.00 83.39  ? 234 LYS B CE  1 
ATOM   2783 N  NZ  . LYS B 2 233 ? 97.471  212.956 -16.165 1.00 72.65  1 234 LYS B NZ  1 
ATOM   2784 N  N   . THR B 2 234 ? 94.127  213.166 -12.419 1.00 64.90  ? 235 THR B N   1 
ATOM   2785 C  CA  . THR B 2 234 ? 94.156  211.795 -11.914 1.00 58.48  ? 235 THR B CA  1 
ATOM   2786 C  C   . THR B 2 234 ? 95.522  211.182 -12.142 1.00 60.40  ? 235 THR B C   1 
ATOM   2787 O  O   . THR B 2 234 ? 95.982  211.125 -13.274 1.00 66.42  ? 235 THR B O   1 
ATOM   2788 C  CB  . THR B 2 234 ? 93.107  210.905 -12.610 1.00 57.94  ? 235 THR B CB  1 
ATOM   2789 O  OG1 . THR B 2 234 ? 91.787  211.257 -12.167 1.00 57.31  ? 235 THR B OG1 1 
ATOM   2790 C  CG2 . THR B 2 234 ? 93.377  209.436 -12.314 1.00 55.61  ? 235 THR B CG2 1 
ATOM   2791 N  N   . VAL B 2 235 ? 96.190  210.744 -11.077 1.00 61.46  ? 236 VAL B N   1 
ATOM   2792 C  CA  . VAL B 2 235 ? 97.551  210.219 -11.213 1.00 49.96  ? 236 VAL B CA  1 
ATOM   2793 C  C   . VAL B 2 235 ? 97.630  208.708 -10.974 1.00 51.62  ? 236 VAL B C   1 
ATOM   2794 O  O   . VAL B 2 235 ? 98.653  208.083 -11.253 1.00 57.76  ? 236 VAL B O   1 
ATOM   2795 C  CB  . VAL B 2 235 ? 98.517  210.919 -10.254 1.00 51.13  ? 236 VAL B CB  1 
ATOM   2796 C  CG1 . VAL B 2 235 ? 98.446  212.414 -10.470 1.00 57.30  ? 236 VAL B CG1 1 
ATOM   2797 C  CG2 . VAL B 2 235 ? 98.185  210.554 -8.805  1.00 49.00  ? 236 VAL B CG2 1 
ATOM   2798 N  N   . TRP B 2 236 ? 96.538  208.125 -10.486 1.00 51.26  ? 237 TRP B N   1 
ATOM   2799 C  CA  . TRP B 2 236 ? 96.479  206.695 -10.199 1.00 45.47  ? 237 TRP B CA  1 
ATOM   2800 C  C   . TRP B 2 236 ? 95.023  206.258 -10.014 1.00 48.78  ? 237 TRP B C   1 
ATOM   2801 O  O   . TRP B 2 236 ? 94.163  207.042 -9.611  1.00 49.81  ? 237 TRP B O   1 
ATOM   2802 C  CB  . TRP B 2 236 ? 97.313  206.366 -8.951  1.00 41.99  ? 237 TRP B CB  1 
ATOM   2803 C  CG  . TRP B 2 236 ? 97.341  204.912 -8.509  1.00 44.39  ? 237 TRP B CG  1 
ATOM   2804 C  CD1 . TRP B 2 236 ? 98.338  204.005 -8.743  1.00 49.23  ? 237 TRP B CD1 1 
ATOM   2805 C  CD2 . TRP B 2 236 ? 96.354  204.222 -7.720  1.00 45.94  ? 237 TRP B CD2 1 
ATOM   2806 N  NE1 . TRP B 2 236 ? 98.031  202.796 -8.156  1.00 50.17  ? 237 TRP B NE1 1 
ATOM   2807 C  CE2 . TRP B 2 236 ? 96.818  202.902 -7.528  1.00 48.62  ? 237 TRP B CE2 1 
ATOM   2808 C  CE3 . TRP B 2 236 ? 95.129  204.592 -7.158  1.00 42.28  ? 237 TRP B CE3 1 
ATOM   2809 C  CZ2 . TRP B 2 236 ? 96.094  201.950 -6.804  1.00 47.75  ? 237 TRP B CZ2 1 
ATOM   2810 C  CZ3 . TRP B 2 236 ? 94.409  203.642 -6.448  1.00 43.86  ? 237 TRP B CZ3 1 
ATOM   2811 C  CH2 . TRP B 2 236 ? 94.893  202.341 -6.275  1.00 45.89  ? 237 TRP B CH2 1 
ATOM   2812 N  N   . ALA B 2 237 ? 94.755  205.000 -10.321 1.00 46.95  ? 238 ALA B N   1 
ATOM   2813 C  CA  . ALA B 2 237 ? 93.433  204.426 -10.125 1.00 51.16  ? 238 ALA B CA  1 
ATOM   2814 C  C   . ALA B 2 237 ? 93.553  202.940 -9.846  1.00 48.28  ? 238 ALA B C   1 
ATOM   2815 O  O   . ALA B 2 237 ? 94.558  202.329 -10.169 1.00 40.33  ? 238 ALA B O   1 
ATOM   2816 C  CB  . ALA B 2 237 ? 92.564  204.663 -11.321 1.00 43.54  ? 238 ALA B CB  1 
ATOM   2817 N  N   . ALA B 2 238 ? 92.546  202.377 -9.192  1.00 52.94  ? 239 ALA B N   1 
ATOM   2818 C  CA  . ALA B 2 238 ? 92.483  200.937 -9.015  1.00 52.14  ? 239 ALA B CA  1 
ATOM   2819 C  C   . ALA B 2 238 ? 92.363  200.283 -10.389 1.00 53.34  ? 239 ALA B C   1 
ATOM   2820 O  O   . ALA B 2 238 ? 91.926  200.920 -11.355 1.00 58.84  ? 239 ALA B O   1 
ATOM   2821 C  CB  . ALA B 2 238 ? 91.321  200.553 -8.120  1.00 36.98  ? 239 ALA B CB  1 
ATOM   2822 N  N   . ALA B 2 239 ? 92.771  199.024 -10.476 1.00 55.02  ? 240 ALA B N   1 
ATOM   2823 C  CA  . ALA B 2 239 ? 92.669  198.260 -11.715 1.00 63.02  ? 240 ALA B CA  1 
ATOM   2824 C  C   . ALA B 2 239 ? 91.216  197.903 -12.048 1.00 62.92  ? 240 ALA B C   1 
ATOM   2825 O  O   . ALA B 2 239 ? 90.386  197.745 -11.152 1.00 66.82  ? 240 ALA B O   1 
ATOM   2826 C  CB  . ALA B 2 239 ? 93.513  197.007 -11.626 1.00 52.33  ? 240 ALA B CB  1 
ATOM   2827 N  N   . LYS B 2 240 ? 90.922  197.788 -13.343 1.00 73.70  ? 241 LYS B N   1 
ATOM   2828 C  CA  . LYS B 2 240 ? 89.579  197.456 -13.815 1.00 78.13  ? 241 LYS B CA  1 
ATOM   2829 C  C   . LYS B 2 240 ? 89.212  196.017 -13.467 1.00 69.61  ? 241 LYS B C   1 
ATOM   2830 O  O   . LYS B 2 240 ? 88.046  195.621 -13.565 1.00 80.76  ? 241 LYS B O   1 
ATOM   2831 C  CB  . LYS B 2 240 ? 89.472  197.641 -15.335 1.00 80.91  ? 241 LYS B CB  1 
ATOM   2832 C  CG  . LYS B 2 240 ? 89.709  199.049 -15.843 1.00 86.30  ? 241 LYS B CG  1 
ATOM   2833 C  CD  . LYS B 2 240 ? 88.681  200.028 -15.301 1.00 89.69  ? 241 LYS B CD  1 
ATOM   2834 C  CE  . LYS B 2 240 ? 88.857  201.415 -15.926 1.00 96.72  ? 241 LYS B CE  1 
ATOM   2835 N  NZ  . LYS B 2 240 ? 87.835  202.396 -15.445 1.00 100.25 1 241 LYS B NZ  1 
ATOM   2836 N  N   . ALA C 1 1   ? 130.984 209.485 0.480   1.00 63.52  ? 1   ALA C N   1 
ATOM   2837 C  CA  . ALA C 1 1   ? 130.198 209.632 1.710   1.00 58.92  ? 1   ALA C CA  1 
ATOM   2838 C  C   . ALA C 1 1   ? 129.231 210.799 1.562   1.00 55.54  ? 1   ALA C C   1 
ATOM   2839 O  O   . ALA C 1 1   ? 129.641 211.905 1.246   1.00 50.40  ? 1   ALA C O   1 
ATOM   2840 C  CB  . ALA C 1 1   ? 131.099 209.820 2.920   1.00 50.51  ? 1   ALA C CB  1 
ATOM   2841 N  N   . THR C 1 2   ? 127.939 210.536 1.711   1.00 55.16  ? 2   THR C N   1 
ATOM   2842 C  CA  . THR C 1 2   ? 126.945 211.534 1.362   1.00 41.52  ? 2   THR C CA  1 
ATOM   2843 C  C   . THR C 1 2   ? 126.112 211.888 2.588   1.00 43.58  ? 2   THR C C   1 
ATOM   2844 O  O   . THR C 1 2   ? 125.505 212.964 2.656   1.00 38.40  ? 2   THR C O   1 
ATOM   2845 C  CB  . THR C 1 2   ? 126.043 211.032 0.209   1.00 51.60  ? 2   THR C CB  1 
ATOM   2846 O  OG1 . THR C 1 2   ? 125.424 212.142 -0.452  1.00 72.84  ? 2   THR C OG1 1 
ATOM   2847 C  CG2 . THR C 1 2   ? 124.989 210.037 0.703   1.00 48.07  ? 2   THR C CG2 1 
ATOM   2848 N  N   . LYS C 1 3   ? 126.093 210.990 3.568   1.00 39.33  ? 3   LYS C N   1 
ATOM   2849 C  CA  . LYS C 1 3   ? 125.387 211.270 4.822   1.00 41.71  ? 3   LYS C CA  1 
ATOM   2850 C  C   . LYS C 1 3   ? 126.186 210.881 6.053   1.00 36.68  ? 3   LYS C C   1 
ATOM   2851 O  O   . LYS C 1 3   ? 126.852 209.857 6.088   1.00 38.30  ? 3   LYS C O   1 
ATOM   2852 C  CB  . LYS C 1 3   ? 124.026 210.568 4.866   1.00 55.44  ? 3   LYS C CB  1 
ATOM   2853 C  CG  . LYS C 1 3   ? 122.867 211.369 4.276   1.00 61.39  ? 3   LYS C CG  1 
ATOM   2854 C  CD  . LYS C 1 3   ? 121.566 210.942 4.958   1.00 73.00  ? 3   LYS C CD  1 
ATOM   2855 C  CE  . LYS C 1 3   ? 120.515 212.048 4.935   1.00 86.00  ? 3   LYS C CE  1 
ATOM   2856 N  NZ  . LYS C 1 3   ? 119.226 211.604 5.554   1.00 85.73  1 3   LYS C NZ  1 
ATOM   2857 N  N   . ALA C 1 4   ? 126.107 211.715 7.074   1.00 37.51  ? 4   ALA C N   1 
ATOM   2858 C  CA  . ALA C 1 4   ? 126.769 211.418 8.330   1.00 34.89  ? 4   ALA C CA  1 
ATOM   2859 C  C   . ALA C 1 4   ? 125.825 211.700 9.496   1.00 33.85  ? 4   ALA C C   1 
ATOM   2860 O  O   . ALA C 1 4   ? 124.780 212.343 9.327   1.00 32.87  ? 4   ALA C O   1 
ATOM   2861 C  CB  . ALA C 1 4   ? 128.064 212.224 8.459   1.00 26.85  ? 4   ALA C CB  1 
ATOM   2862 N  N   . VAL C 1 5   ? 126.161 211.174 10.667  1.00 30.07  ? 5   VAL C N   1 
ATOM   2863 C  CA  . VAL C 1 5   ? 125.330 211.427 11.838  1.00 34.32  ? 5   VAL C CA  1 
ATOM   2864 C  C   . VAL C 1 5   ? 126.207 211.499 13.089  1.00 32.91  ? 5   VAL C C   1 
ATOM   2865 O  O   . VAL C 1 5   ? 127.258 210.867 13.155  1.00 35.78  ? 5   VAL C O   1 
ATOM   2866 C  CB  . VAL C 1 5   ? 124.216 210.335 11.987  1.00 36.79  ? 5   VAL C CB  1 
ATOM   2867 C  CG1 . VAL C 1 5   ? 124.812 208.958 12.262  1.00 33.95  ? 5   VAL C CG1 1 
ATOM   2868 C  CG2 . VAL C 1 5   ? 123.218 210.723 13.038  1.00 34.43  ? 5   VAL C CG2 1 
ATOM   2869 N  N   . CYS C 1 6   ? 125.780 212.283 14.071  1.00 33.98  ? 6   CYS C N   1 
ATOM   2870 C  CA  . CYS C 1 6   ? 126.502 212.366 15.328  1.00 30.74  ? 6   CYS C CA  1 
ATOM   2871 C  C   . CYS C 1 6   ? 125.560 212.298 16.526  1.00 34.20  ? 6   CYS C C   1 
ATOM   2872 O  O   . CYS C 1 6   ? 124.618 213.087 16.627  1.00 38.28  ? 6   CYS C O   1 
ATOM   2873 C  CB  . CYS C 1 6   ? 127.308 213.656 15.393  1.00 34.38  ? 6   CYS C CB  1 
ATOM   2874 S  SG  . CYS C 1 6   ? 128.195 213.885 16.976  1.00 40.92  ? 6   CYS C SG  1 
ATOM   2875 N  N   . VAL C 1 7   ? 125.834 211.392 17.457  1.00 30.96  ? 7   VAL C N   1 
ATOM   2876 C  CA  . VAL C 1 7   ? 125.048 211.346 18.690  1.00 35.47  ? 7   VAL C CA  1 
ATOM   2877 C  C   . VAL C 1 7   ? 125.711 212.150 19.805  1.00 28.75  ? 7   VAL C C   1 
ATOM   2878 O  O   . VAL C 1 7   ? 126.746 211.761 20.320  1.00 28.74  ? 7   VAL C O   1 
ATOM   2879 C  CB  . VAL C 1 7   ? 124.832 209.899 19.163  1.00 36.57  ? 7   VAL C CB  1 
ATOM   2880 C  CG1 . VAL C 1 7   ? 124.064 209.874 20.494  1.00 30.01  ? 7   VAL C CG1 1 
ATOM   2881 C  CG2 . VAL C 1 7   ? 124.112 209.104 18.084  1.00 32.43  ? 7   VAL C CG2 1 
ATOM   2882 N  N   . LEU C 1 8   ? 125.130 213.294 20.135  1.00 30.64  ? 8   LEU C N   1 
ATOM   2883 C  CA  . LEU C 1 8   ? 125.643 214.140 21.202  1.00 30.92  ? 8   LEU C CA  1 
ATOM   2884 C  C   . LEU C 1 8   ? 125.154 213.702 22.561  1.00 39.43  ? 8   LEU C C   1 
ATOM   2885 O  O   . LEU C 1 8   ? 123.947 213.724 22.839  1.00 39.94  ? 8   LEU C O   1 
ATOM   2886 C  CB  . LEU C 1 8   ? 125.248 215.621 21.002  1.00 27.79  ? 8   LEU C CB  1 
ATOM   2887 C  CG  . LEU C 1 8   ? 125.695 216.327 19.725  1.00 39.09  ? 8   LEU C CG  1 
ATOM   2888 C  CD1 . LEU C 1 8   ? 125.182 217.756 19.702  1.00 35.06  ? 8   LEU C CD1 1 
ATOM   2889 C  CD2 . LEU C 1 8   ? 127.232 216.286 19.614  1.00 39.17  ? 8   LEU C CD2 1 
ATOM   2890 N  N   . LYS C 1 9   ? 126.093 213.371 23.435  1.00 34.09  ? 9   LYS C N   1 
ATOM   2891 C  CA  . LYS C 1 9   ? 125.739 213.180 24.809  1.00 34.76  ? 9   LYS C CA  1 
ATOM   2892 C  C   . LYS C 1 9   ? 126.840 213.649 25.739  1.00 40.83  ? 9   LYS C C   1 
ATOM   2893 O  O   . LYS C 1 9   ? 128.023 213.720 25.366  1.00 42.71  ? 9   LYS C O   1 
ATOM   2894 C  CB  . LYS C 1 9   ? 125.416 211.713 25.068  1.00 41.98  ? 9   LYS C CB  1 
ATOM   2895 C  CG  . LYS C 1 9   ? 126.539 210.783 24.805  1.00 35.62  ? 9   LYS C CG  1 
ATOM   2896 C  CD  . LYS C 1 9   ? 126.073 209.344 24.934  1.00 54.04  ? 9   LYS C CD  1 
ATOM   2897 C  CE  . LYS C 1 9   ? 127.105 208.508 25.691  1.00 61.98  ? 9   LYS C CE  1 
ATOM   2898 N  NZ  . LYS C 1 9   ? 128.322 208.286 24.865  1.00 68.88  1 9   LYS C NZ  1 
ATOM   2899 N  N   . GLY C 1 10  ? 126.447 213.920 26.977  1.00 41.87  ? 10  GLY C N   1 
ATOM   2900 C  CA  . GLY C 1 10  ? 127.367 214.396 27.988  1.00 44.68  ? 10  GLY C CA  1 
ATOM   2901 C  C   . GLY C 1 10  ? 126.983 213.872 29.363  1.00 57.18  ? 10  GLY C C   1 
ATOM   2902 O  O   . GLY C 1 10  ? 126.172 212.948 29.498  1.00 52.94  ? 10  GLY C O   1 
ATOM   2903 N  N   . ASP C 1 11  ? 127.582 214.452 30.392  1.00 49.71  ? 11  ASP C N   1 
ATOM   2904 C  CA  . ASP C 1 11  ? 127.363 213.976 31.739  1.00 57.80  ? 11  ASP C CA  1 
ATOM   2905 C  C   . ASP C 1 11  ? 126.064 214.514 32.315  1.00 52.78  ? 11  ASP C C   1 
ATOM   2906 O  O   . ASP C 1 11  ? 125.596 214.039 33.339  1.00 64.91  ? 11  ASP C O   1 
ATOM   2907 C  CB  . ASP C 1 11  ? 128.538 214.370 32.625  1.00 50.32  ? 11  ASP C CB  1 
ATOM   2908 C  CG  . ASP C 1 11  ? 129.829 213.737 32.172  1.00 68.74  ? 11  ASP C CG  1 
ATOM   2909 O  OD1 . ASP C 1 11  ? 129.789 212.565 31.734  1.00 76.62  ? 11  ASP C OD1 1 
ATOM   2910 O  OD2 . ASP C 1 11  ? 130.881 214.402 32.264  1.00 75.12  1 11  ASP C OD2 1 
ATOM   2911 N  N   . GLY C 1 12  ? 125.473 215.493 31.645  1.00 46.91  ? 12  GLY C N   1 
ATOM   2912 C  CA  . GLY C 1 12  ? 124.292 216.147 32.172  1.00 34.65  ? 12  GLY C CA  1 
ATOM   2913 C  C   . GLY C 1 12  ? 123.090 215.924 31.292  1.00 42.99  ? 12  GLY C C   1 
ATOM   2914 O  O   . GLY C 1 12  ? 122.992 214.912 30.611  1.00 45.93  ? 12  GLY C O   1 
ATOM   2915 N  N   . PRO C 1 13  ? 122.157 216.874 31.317  1.00 45.03  ? 13  PRO C N   1 
ATOM   2916 C  CA  . PRO C 1 13  ? 120.893 216.862 30.557  1.00 47.15  ? 13  PRO C CA  1 
ATOM   2917 C  C   . PRO C 1 13  ? 121.042 217.065 29.027  1.00 51.38  ? 13  PRO C C   1 
ATOM   2918 O  O   . PRO C 1 13  ? 120.118 216.741 28.276  1.00 55.71  ? 13  PRO C O   1 
ATOM   2919 C  CB  . PRO C 1 13  ? 120.103 218.031 31.175  1.00 43.75  ? 13  PRO C CB  1 
ATOM   2920 C  CG  . PRO C 1 13  ? 121.176 218.972 31.729  1.00 40.11  ? 13  PRO C CG  1 
ATOM   2921 C  CD  . PRO C 1 13  ? 122.278 218.042 32.215  1.00 39.34  ? 13  PRO C CD  1 
ATOM   2922 N  N   . VAL C 1 14  ? 122.163 217.631 28.586  1.00 50.07  ? 14  VAL C N   1 
ATOM   2923 C  CA  . VAL C 1 14  ? 122.368 217.929 27.174  1.00 40.00  ? 14  VAL C CA  1 
ATOM   2924 C  C   . VAL C 1 14  ? 122.577 216.654 26.358  1.00 40.40  ? 14  VAL C C   1 
ATOM   2925 O  O   . VAL C 1 14  ? 123.436 215.821 26.661  1.00 39.95  ? 14  VAL C O   1 
ATOM   2926 C  CB  . VAL C 1 14  ? 123.568 218.885 26.955  1.00 44.61  ? 14  VAL C CB  1 
ATOM   2927 C  CG1 . VAL C 1 14  ? 123.724 219.248 25.476  1.00 31.92  ? 14  VAL C CG1 1 
ATOM   2928 C  CG2 . VAL C 1 14  ? 123.388 220.155 27.792  1.00 43.74  ? 14  VAL C CG2 1 
ATOM   2929 N  N   . GLN C 1 15  ? 121.749 216.511 25.331  1.00 33.33  ? 15  GLN C N   1 
ATOM   2930 C  CA  . GLN C 1 15  ? 121.828 215.376 24.432  1.00 44.98  ? 15  GLN C CA  1 
ATOM   2931 C  C   . GLN C 1 15  ? 121.142 215.732 23.131  1.00 32.68  ? 15  GLN C C   1 
ATOM   2932 O  O   . GLN C 1 15  ? 120.251 216.583 23.091  1.00 37.49  ? 15  GLN C O   1 
ATOM   2933 C  CB  . GLN C 1 15  ? 121.185 214.128 25.033  1.00 38.89  ? 15  GLN C CB  1 
ATOM   2934 C  CG  . GLN C 1 15  ? 119.686 214.235 25.142  1.00 52.83  ? 15  GLN C CG  1 
ATOM   2935 C  CD  . GLN C 1 15  ? 119.049 213.009 25.746  1.00 69.37  ? 15  GLN C CD  1 
ATOM   2936 O  OE1 . GLN C 1 15  ? 118.603 212.111 25.025  1.00 74.22  ? 15  GLN C OE1 1 
ATOM   2937 N  NE2 . GLN C 1 15  ? 119.009 212.953 27.075  1.00 70.27  ? 15  GLN C NE2 1 
ATOM   2938 N  N   . GLY C 1 16  ? 121.556 215.073 22.066  1.00 35.04  ? 16  GLY C N   1 
ATOM   2939 C  CA  . GLY C 1 16  ? 121.017 215.374 20.756  1.00 34.70  ? 16  GLY C CA  1 
ATOM   2940 C  C   . GLY C 1 16  ? 121.531 214.432 19.691  1.00 37.50  ? 16  GLY C C   1 
ATOM   2941 O  O   . GLY C 1 16  ? 122.512 213.716 19.880  1.00 32.26  ? 16  GLY C O   1 
ATOM   2942 N  N   . ILE C 1 17  ? 120.868 214.451 18.542  1.00 39.66  ? 17  ILE C N   1 
ATOM   2943 C  CA  . ILE C 1 17  ? 121.377 213.727 17.391  1.00 41.54  ? 17  ILE C CA  1 
ATOM   2944 C  C   . ILE C 1 17  ? 121.527 214.764 16.289  1.00 37.63  ? 17  ILE C C   1 
ATOM   2945 O  O   . ILE C 1 17  ? 120.619 215.580 16.065  1.00 33.85  ? 17  ILE C O   1 
ATOM   2946 C  CB  . ILE C 1 17  ? 120.434 212.592 16.922  1.00 37.66  ? 17  ILE C CB  1 
ATOM   2947 C  CG1 . ILE C 1 17  ? 120.054 211.680 18.088  1.00 43.56  ? 17  ILE C CG1 1 
ATOM   2948 C  CG2 . ILE C 1 17  ? 121.059 211.863 15.720  1.00 31.62  ? 17  ILE C CG2 1 
ATOM   2949 C  CD1 . ILE C 1 17  ? 119.025 210.622 17.731  1.00 47.78  ? 17  ILE C CD1 1 
ATOM   2950 N  N   . ILE C 1 18  ? 122.682 214.779 15.635  1.00 38.46  ? 18  ILE C N   1 
ATOM   2951 C  CA  . ILE C 1 18  ? 122.902 215.744 14.553  1.00 34.51  ? 18  ILE C CA  1 
ATOM   2952 C  C   . ILE C 1 18  ? 123.154 215.020 13.260  1.00 32.07  ? 18  ILE C C   1 
ATOM   2953 O  O   . ILE C 1 18  ? 123.950 214.072 13.209  1.00 35.10  ? 18  ILE C O   1 
ATOM   2954 C  CB  . ILE C 1 18  ? 124.064 216.678 14.852  1.00 32.35  ? 18  ILE C CB  1 
ATOM   2955 C  CG1 . ILE C 1 18  ? 123.831 217.362 16.200  1.00 30.12  ? 18  ILE C CG1 1 
ATOM   2956 C  CG2 . ILE C 1 18  ? 124.206 217.699 13.742  1.00 31.59  ? 18  ILE C CG2 1 
ATOM   2957 C  CD1 . ILE C 1 18  ? 122.815 218.423 16.160  1.00 28.10  ? 18  ILE C CD1 1 
ATOM   2958 N  N   . ASN C 1 19  ? 122.449 215.445 12.219  1.00 36.02  ? 19  ASN C N   1 
ATOM   2959 C  CA  . ASN C 1 19  ? 122.618 214.855 10.901  1.00 31.32  ? 19  ASN C CA  1 
ATOM   2960 C  C   . ASN C 1 19  ? 123.402 215.757 9.962   1.00 38.42  ? 19  ASN C C   1 
ATOM   2961 O  O   . ASN C 1 19  ? 123.333 216.993 10.054  1.00 35.06  ? 19  ASN C O   1 
ATOM   2962 C  CB  . ASN C 1 19  ? 121.265 214.549 10.264  1.00 34.25  ? 19  ASN C CB  1 
ATOM   2963 C  CG  . ASN C 1 19  ? 120.400 213.669 11.122  1.00 40.43  ? 19  ASN C CG  1 
ATOM   2964 O  OD1 . ASN C 1 19  ? 119.444 214.137 11.729  1.00 39.24  ? 19  ASN C OD1 1 
ATOM   2965 N  ND2 . ASN C 1 19  ? 120.750 212.391 11.206  1.00 43.49  ? 19  ASN C ND2 1 
ATOM   2966 N  N   . PHE C 1 20  ? 124.136 215.115 9.057   1.00 32.93  ? 20  PHE C N   1 
ATOM   2967 C  CA  . PHE C 1 20  ? 124.886 215.794 8.022   1.00 31.86  ? 20  PHE C CA  1 
ATOM   2968 C  C   . PHE C 1 20  ? 124.526 215.205 6.673   1.00 35.60  ? 20  PHE C C   1 
ATOM   2969 O  O   . PHE C 1 20  ? 124.443 213.986 6.512   1.00 33.87  ? 20  PHE C O   1 
ATOM   2970 C  CB  . PHE C 1 20  ? 126.408 215.658 8.241   1.00 33.45  ? 20  PHE C CB  1 
ATOM   2971 C  CG  . PHE C 1 20  ? 126.872 216.163 9.568   1.00 41.81  ? 20  PHE C CG  1 
ATOM   2972 C  CD1 . PHE C 1 20  ? 126.755 215.370 10.709  1.00 30.68  ? 20  PHE C CD1 1 
ATOM   2973 C  CD2 . PHE C 1 20  ? 127.396 217.439 9.685   1.00 36.77  ? 20  PHE C CD2 1 
ATOM   2974 C  CE1 . PHE C 1 20  ? 127.163 215.850 11.939  1.00 34.06  ? 20  PHE C CE1 1 
ATOM   2975 C  CE2 . PHE C 1 20  ? 127.812 217.923 10.918  1.00 36.35  ? 20  PHE C CE2 1 
ATOM   2976 C  CZ  . PHE C 1 20  ? 127.703 217.134 12.044  1.00 34.54  ? 20  PHE C CZ  1 
ATOM   2977 N  N   . GLU C 1 21  ? 124.386 216.070 5.685   1.00 38.33  ? 21  GLU C N   1 
ATOM   2978 C  CA  . GLU C 1 21  ? 124.049 215.620 4.346   1.00 43.23  ? 21  GLU C CA  1 
ATOM   2979 C  C   . GLU C 1 21  ? 124.792 216.458 3.324   1.00 37.35  ? 21  GLU C C   1 
ATOM   2980 O  O   . GLU C 1 21  ? 124.747 217.700 3.347   1.00 37.12  ? 21  GLU C O   1 
ATOM   2981 C  CB  . GLU C 1 21  ? 122.528 215.704 4.124   1.00 47.44  ? 21  GLU C CB  1 
ATOM   2982 C  CG  . GLU C 1 21  ? 122.037 215.194 2.767   1.00 58.84  ? 21  GLU C CG  1 
ATOM   2983 C  CD  . GLU C 1 21  ? 120.521 215.373 2.584   1.00 73.43  ? 21  GLU C CD  1 
ATOM   2984 O  OE1 . GLU C 1 21  ? 119.753 214.494 3.038   1.00 79.82  ? 21  GLU C OE1 1 
ATOM   2985 O  OE2 . GLU C 1 21  ? 120.098 216.397 1.993   1.00 76.53  1 21  GLU C OE2 1 
ATOM   2986 N  N   . GLN C 1 22  ? 125.479 215.772 2.425   1.00 39.64  ? 22  GLN C N   1 
ATOM   2987 C  CA  . GLN C 1 22  ? 126.172 216.460 1.355   1.00 43.46  ? 22  GLN C CA  1 
ATOM   2988 C  C   . GLN C 1 22  ? 125.877 215.719 0.048   1.00 46.01  ? 22  GLN C C   1 
ATOM   2989 O  O   . GLN C 1 22  ? 126.489 214.687 -0.264  1.00 48.47  ? 22  GLN C O   1 
ATOM   2990 C  CB  . GLN C 1 22  ? 127.666 216.534 1.623   1.00 37.57  ? 22  GLN C CB  1 
ATOM   2991 C  CG  . GLN C 1 22  ? 128.333 217.534 0.720   1.00 35.86  ? 22  GLN C CG  1 
ATOM   2992 C  CD  . GLN C 1 22  ? 129.849 217.467 0.735   1.00 35.58  ? 22  GLN C CD  1 
ATOM   2993 O  OE1 . GLN C 1 22  ? 130.456 216.454 1.092   1.00 38.65  ? 22  GLN C OE1 1 
ATOM   2994 N  NE2 . GLN C 1 22  ? 130.469 218.563 0.337   1.00 38.76  ? 22  GLN C NE2 1 
ATOM   2995 N  N   . LYS C 1 23  ? 124.925 216.263 -0.703  1.00 41.49  ? 23  LYS C N   1 
ATOM   2996 C  CA  . LYS C 1 23  ? 124.403 215.616 -1.910  1.00 55.90  ? 23  LYS C CA  1 
ATOM   2997 C  C   . LYS C 1 23  ? 125.447 215.580 -3.022  1.00 50.32  ? 23  LYS C C   1 
ATOM   2998 O  O   . LYS C 1 23  ? 125.734 214.529 -3.592  1.00 52.17  ? 23  LYS C O   1 
ATOM   2999 C  CB  . LYS C 1 23  ? 123.149 216.352 -2.413  1.00 59.19  ? 23  LYS C CB  1 
ATOM   3000 C  CG  . LYS C 1 23  ? 121.997 216.497 -1.414  1.00 59.88  ? 23  LYS C CG  1 
ATOM   3001 C  CD  . LYS C 1 23  ? 120.843 217.317 -2.042  1.00 76.21  ? 23  LYS C CD  1 
ATOM   3002 C  CE  . LYS C 1 23  ? 119.597 217.396 -1.143  1.00 72.47  ? 23  LYS C CE  1 
ATOM   3003 N  NZ  . LYS C 1 23  ? 118.609 218.433 -1.596  1.00 76.99  1 23  LYS C NZ  1 
ATOM   3004 N  N   . GLU C 1 24  ? 126.039 216.737 -3.295  1.00 54.47  ? 24  GLU C N   1 
ATOM   3005 C  CA  . GLU C 1 24  ? 127.056 216.847 -4.329  1.00 54.84  ? 24  GLU C CA  1 
ATOM   3006 C  C   . GLU C 1 24  ? 128.449 216.784 -3.693  1.00 51.43  ? 24  GLU C C   1 
ATOM   3007 O  O   . GLU C 1 24  ? 128.678 217.379 -2.636  1.00 42.92  ? 24  GLU C O   1 
ATOM   3008 C  CB  . GLU C 1 24  ? 126.854 218.152 -5.104  1.00 54.77  ? 24  GLU C CB  1 
ATOM   3009 C  CG  . GLU C 1 24  ? 125.425 218.308 -5.650  1.00 65.80  ? 24  GLU C CG  1 
ATOM   3010 C  CD  . GLU C 1 24  ? 125.046 217.268 -6.710  1.00 91.80  ? 24  GLU C CD  1 
ATOM   3011 O  OE1 . GLU C 1 24  ? 125.947 216.583 -7.251  1.00 89.13  ? 24  GLU C OE1 1 
ATOM   3012 O  OE2 . GLU C 1 24  ? 123.830 217.127 -6.989  1.00 90.71  1 24  GLU C OE2 1 
ATOM   3013 N  N   . SER C 1 25  ? 129.384 216.102 -4.353  1.00 52.32  ? 25  SER C N   1 
ATOM   3014 C  CA  . SER C 1 25  ? 130.719 215.874 -3.784  1.00 47.30  ? 25  SER C CA  1 
ATOM   3015 C  C   . SER C 1 25  ? 131.438 217.169 -3.384  1.00 50.13  ? 25  SER C C   1 
ATOM   3016 O  O   . SER C 1 25  ? 132.277 217.157 -2.484  1.00 47.66  ? 25  SER C O   1 
ATOM   3017 C  CB  . SER C 1 25  ? 131.580 215.076 -4.769  1.00 53.88  ? 25  SER C CB  1 
ATOM   3018 O  OG  . SER C 1 25  ? 131.606 215.698 -6.041  1.00 57.21  ? 25  SER C OG  1 
ATOM   3019 N  N   . ASN C 1 26  ? 131.122 218.271 -4.063  1.00 45.23  ? 26  ASN C N   1 
ATOM   3020 C  CA  . ASN C 1 26  ? 131.607 219.592 -3.651  1.00 43.89  ? 26  ASN C CA  1 
ATOM   3021 C  C   . ASN C 1 26  ? 130.462 220.578 -3.420  1.00 40.11  ? 26  ASN C C   1 
ATOM   3022 O  O   . ASN C 1 26  ? 130.580 221.770 -3.712  1.00 39.94  ? 26  ASN C O   1 
ATOM   3023 C  CB  . ASN C 1 26  ? 132.628 220.135 -4.661  1.00 39.06  ? 26  ASN C CB  1 
ATOM   3024 C  CG  . ASN C 1 26  ? 132.129 220.033 -6.070  1.00 55.48  ? 26  ASN C CG  1 
ATOM   3025 O  OD1 . ASN C 1 26  ? 130.954 219.711 -6.290  1.00 55.23  ? 26  ASN C OD1 1 
ATOM   3026 N  ND2 . ASN C 1 26  ? 133.010 220.267 -7.042  1.00 41.65  ? 26  ASN C ND2 1 
ATOM   3027 N  N   . GLY C 1 27  ? 129.335 220.072 -2.919  1.00 42.49  ? 27  GLY C N   1 
ATOM   3028 C  CA  . GLY C 1 27  ? 128.249 220.943 -2.500  1.00 37.95  ? 27  GLY C CA  1 
ATOM   3029 C  C   . GLY C 1 27  ? 128.390 221.327 -1.036  1.00 36.12  ? 27  GLY C C   1 
ATOM   3030 O  O   . GLY C 1 27  ? 129.294 220.853 -0.342  1.00 37.27  ? 27  GLY C O   1 
ATOM   3031 N  N   . PRO C 1 28  ? 127.495 222.192 -0.549  1.00 31.75  ? 28  PRO C N   1 
ATOM   3032 C  CA  . PRO C 1 28  ? 127.569 222.539 0.867   1.00 38.31  ? 28  PRO C CA  1 
ATOM   3033 C  C   . PRO C 1 28  ? 127.141 221.356 1.726   1.00 41.67  ? 28  PRO C C   1 
ATOM   3034 O  O   . PRO C 1 28  ? 126.607 220.388 1.199   1.00 39.79  ? 28  PRO C O   1 
ATOM   3035 C  CB  . PRO C 1 28  ? 126.613 223.725 0.996   1.00 35.81  ? 28  PRO C CB  1 
ATOM   3036 C  CG  . PRO C 1 28  ? 125.697 223.605 -0.161  1.00 43.52  ? 28  PRO C CG  1 
ATOM   3037 C  CD  . PRO C 1 28  ? 126.438 222.934 -1.258  1.00 34.68  ? 28  PRO C CD  1 
ATOM   3038 N  N   . VAL C 1 29  ? 127.444 221.390 3.016   1.00 35.62  ? 29  VAL C N   1 
ATOM   3039 C  CA  . VAL C 1 29  ? 126.946 220.350 3.899   1.00 41.36  ? 29  VAL C CA  1 
ATOM   3040 C  C   . VAL C 1 29  ? 125.749 220.886 4.636   1.00 33.90  ? 29  VAL C C   1 
ATOM   3041 O  O   . VAL C 1 29  ? 125.791 221.976 5.216   1.00 36.50  ? 29  VAL C O   1 
ATOM   3042 C  CB  . VAL C 1 29  ? 127.992 219.865 4.894   1.00 38.19  ? 29  VAL C CB  1 
ATOM   3043 C  CG1 . VAL C 1 29  ? 127.374 218.834 5.859   1.00 29.84  ? 29  VAL C CG1 1 
ATOM   3044 C  CG2 . VAL C 1 29  ? 129.168 219.276 4.137   1.00 32.64  ? 29  VAL C CG2 1 
ATOM   3045 N  N   . LYS C 1 30  ? 124.659 220.140 4.559   1.00 34.66  ? 30  LYS C N   1 
ATOM   3046 C  CA  . LYS C 1 30  ? 123.468 220.509 5.303   1.00 41.48  ? 30  LYS C CA  1 
ATOM   3047 C  C   . LYS C 1 30  ? 123.613 219.893 6.719   1.00 39.13  ? 30  LYS C C   1 
ATOM   3048 O  O   . LYS C 1 30  ? 124.054 218.744 6.868   1.00 35.09  ? 30  LYS C O   1 
ATOM   3049 C  CB  . LYS C 1 30  ? 122.215 220.035 4.546   1.00 45.72  ? 30  LYS C CB  1 
ATOM   3050 C  CG  . LYS C 1 30  ? 120.895 220.703 4.956   1.00 58.24  ? 30  LYS C CG  1 
ATOM   3051 C  CD  . LYS C 1 30  ? 119.698 219.973 4.293   1.00 78.18  ? 30  LYS C CD  1 
ATOM   3052 C  CE  . LYS C 1 30  ? 118.510 219.759 5.263   1.00 65.08  ? 30  LYS C CE  1 
ATOM   3053 N  NZ  . LYS C 1 30  ? 117.503 218.763 4.753   1.00 70.77  1 30  LYS C NZ  1 
ATOM   3054 N  N   . VAL C 1 31  ? 123.304 220.664 7.757   1.00 40.04  ? 31  VAL C N   1 
ATOM   3055 C  CA  . VAL C 1 31  ? 123.520 220.188 9.132   1.00 37.75  ? 31  VAL C CA  1 
ATOM   3056 C  C   . VAL C 1 31  ? 122.277 220.445 9.962   1.00 38.72  ? 31  VAL C C   1 
ATOM   3057 O  O   . VAL C 1 31  ? 121.921 221.594 10.221  1.00 41.42  ? 31  VAL C O   1 
ATOM   3058 C  CB  . VAL C 1 31  ? 124.756 220.874 9.800   1.00 36.75  ? 31  VAL C CB  1 
ATOM   3059 C  CG1 . VAL C 1 31  ? 124.989 220.360 11.228  1.00 30.03  ? 31  VAL C CG1 1 
ATOM   3060 C  CG2 . VAL C 1 31  ? 125.995 220.628 8.980   1.00 33.88  ? 31  VAL C CG2 1 
ATOM   3061 N  N   . TRP C 1 32  ? 121.595 219.386 10.384  1.00 32.03  ? 32  TRP C N   1 
ATOM   3062 C  CA  . TRP C 1 32  ? 120.353 219.630 11.124  1.00 40.34  ? 32  TRP C CA  1 
ATOM   3063 C  C   . TRP C 1 32  ? 120.078 218.601 12.202  1.00 36.22  ? 32  TRP C C   1 
ATOM   3064 O  O   . TRP C 1 32  ? 120.534 217.445 12.140  1.00 34.09  ? 32  TRP C O   1 
ATOM   3065 C  CB  . TRP C 1 32  ? 119.132 219.701 10.175  1.00 31.40  ? 32  TRP C CB  1 
ATOM   3066 C  CG  . TRP C 1 32  ? 118.658 218.362 9.781   1.00 37.85  ? 32  TRP C CG  1 
ATOM   3067 C  CD1 . TRP C 1 32  ? 117.634 217.643 10.343  1.00 41.90  ? 32  TRP C CD1 1 
ATOM   3068 C  CD2 . TRP C 1 32  ? 119.218 217.536 8.763   1.00 36.81  ? 32  TRP C CD2 1 
ATOM   3069 N  NE1 . TRP C 1 32  ? 117.525 216.422 9.720   1.00 45.78  ? 32  TRP C NE1 1 
ATOM   3070 C  CE2 . TRP C 1 32  ? 118.491 216.332 8.751   1.00 35.18  ? 32  TRP C CE2 1 
ATOM   3071 C  CE3 . TRP C 1 32  ? 120.276 217.695 7.861   1.00 37.65  ? 32  TRP C CE3 1 
ATOM   3072 C  CZ2 . TRP C 1 32  ? 118.773 215.302 7.862   1.00 43.43  ? 32  TRP C CZ2 1 
ATOM   3073 C  CZ3 . TRP C 1 32  ? 120.563 216.669 6.991   1.00 44.73  ? 32  TRP C CZ3 1 
ATOM   3074 C  CH2 . TRP C 1 32  ? 119.812 215.487 6.991   1.00 49.18  ? 32  TRP C CH2 1 
ATOM   3075 N  N   . GLY C 1 33  ? 119.288 219.030 13.178  1.00 32.61  ? 33  GLY C N   1 
ATOM   3076 C  CA  . GLY C 1 33  ? 118.893 218.146 14.250  1.00 31.26  ? 33  GLY C CA  1 
ATOM   3077 C  C   . GLY C 1 33  ? 118.460 218.899 15.470  1.00 37.23  ? 33  GLY C C   1 
ATOM   3078 O  O   . GLY C 1 33  ? 118.187 220.088 15.433  1.00 43.19  ? 33  GLY C O   1 
ATOM   3079 N  N   . SER C 1 34  ? 118.404 218.215 16.586  1.00 36.11  ? 34  SER C N   1 
ATOM   3080 C  CA  . SER C 1 34  ? 117.883 218.888 17.743  1.00 44.92  ? 34  SER C CA  1 
ATOM   3081 C  C   . SER C 1 34  ? 118.782 218.618 18.931  1.00 36.30  ? 34  SER C C   1 
ATOM   3082 O  O   . SER C 1 34  ? 119.332 217.527 19.065  1.00 38.47  ? 34  SER C O   1 
ATOM   3083 C  CB  . SER C 1 34  ? 116.450 218.422 17.997  1.00 40.37  ? 34  SER C CB  1 
ATOM   3084 O  OG  . SER C 1 34  ? 115.836 219.233 18.972  1.00 62.49  ? 34  SER C OG  1 
ATOM   3085 N  N   . ILE C 1 35  ? 118.960 219.623 19.774  1.00 37.57  ? 35  ILE C N   1 
ATOM   3086 C  CA  . ILE C 1 35  ? 119.677 219.424 21.032  1.00 42.97  ? 35  ILE C CA  1 
ATOM   3087 C  C   . ILE C 1 35  ? 118.813 219.917 22.178  1.00 38.85  ? 35  ILE C C   1 
ATOM   3088 O  O   . ILE C 1 35  ? 118.293 221.030 22.131  1.00 42.27  ? 35  ILE C O   1 
ATOM   3089 C  CB  . ILE C 1 35  ? 121.015 220.164 21.079  1.00 40.74  ? 35  ILE C CB  1 
ATOM   3090 C  CG1 . ILE C 1 35  ? 121.846 219.868 19.827  1.00 40.92  ? 35  ILE C CG1 1 
ATOM   3091 C  CG2 . ILE C 1 35  ? 121.770 219.778 22.347  1.00 35.08  ? 35  ILE C CG2 1 
ATOM   3092 C  CD1 . ILE C 1 35  ? 123.172 220.635 19.768  1.00 32.12  ? 35  ILE C CD1 1 
ATOM   3093 N  N   . LYS C 1 36  ? 118.644 219.089 23.197  1.00 39.17  ? 36  LYS C N   1 
ATOM   3094 C  CA  . LYS C 1 36  ? 117.823 219.483 24.330  1.00 39.28  ? 36  LYS C CA  1 
ATOM   3095 C  C   . LYS C 1 36  ? 118.674 219.517 25.571  1.00 42.91  ? 36  LYS C C   1 
ATOM   3096 O  O   . LYS C 1 36  ? 119.784 218.986 25.582  1.00 42.93  ? 36  LYS C O   1 
ATOM   3097 C  CB  . LYS C 1 36  ? 116.632 218.537 24.517  1.00 42.48  ? 36  LYS C CB  1 
ATOM   3098 C  CG  . LYS C 1 36  ? 117.044 217.124 24.886  1.00 57.69  ? 36  LYS C CG  1 
ATOM   3099 C  CD  . LYS C 1 36  ? 115.850 216.179 25.065  1.00 56.00  ? 36  LYS C CD  1 
ATOM   3100 C  CE  . LYS C 1 36  ? 116.272 214.939 25.865  1.00 60.75  ? 36  LYS C CE  1 
ATOM   3101 N  NZ  . LYS C 1 36  ? 115.131 214.192 26.476  1.00 75.13  1 36  LYS C NZ  1 
ATOM   3102 N  N   . GLY C 1 37  ? 118.141 220.136 26.621  1.00 46.16  ? 37  GLY C N   1 
ATOM   3103 C  CA  . GLY C 1 37  ? 118.833 220.224 27.891  1.00 43.34  ? 37  GLY C CA  1 
ATOM   3104 C  C   . GLY C 1 37  ? 119.738 221.438 27.973  1.00 48.07  ? 37  GLY C C   1 
ATOM   3105 O  O   . GLY C 1 37  ? 120.586 221.537 28.863  1.00 48.44  ? 37  GLY C O   1 
ATOM   3106 N  N   . LEU C 1 38  ? 119.552 222.375 27.051  1.00 39.00  ? 38  LEU C N   1 
ATOM   3107 C  CA  . LEU C 1 38  ? 120.371 223.565 27.027  1.00 45.33  ? 38  LEU C CA  1 
ATOM   3108 C  C   . LEU C 1 38  ? 119.707 224.655 27.838  1.00 51.68  ? 38  LEU C C   1 
ATOM   3109 O  O   . LEU C 1 38  ? 118.510 224.598 28.076  1.00 57.25  ? 38  LEU C O   1 
ATOM   3110 C  CB  . LEU C 1 38  ? 120.616 224.008 25.588  1.00 46.53  ? 38  LEU C CB  1 
ATOM   3111 C  CG  . LEU C 1 38  ? 121.488 222.978 24.856  1.00 45.65  ? 38  LEU C CG  1 
ATOM   3112 C  CD1 . LEU C 1 38  ? 121.491 223.207 23.350  1.00 42.59  ? 38  LEU C CD1 1 
ATOM   3113 C  CD2 . LEU C 1 38  ? 122.906 223.044 25.419  1.00 36.72  ? 38  LEU C CD2 1 
ATOM   3114 N  N   . THR C 1 39  ? 120.485 225.614 28.324  1.00 45.11  ? 39  THR C N   1 
ATOM   3115 C  CA  . THR C 1 39  ? 119.878 226.807 28.880  1.00 45.08  ? 39  THR C CA  1 
ATOM   3116 C  C   . THR C 1 39  ? 119.499 227.681 27.699  1.00 51.19  ? 39  THR C C   1 
ATOM   3117 O  O   . THR C 1 39  ? 120.075 227.565 26.612  1.00 41.83  ? 39  THR C O   1 
ATOM   3118 C  CB  . THR C 1 39  ? 120.810 227.564 29.838  1.00 48.66  ? 39  THR C CB  1 
ATOM   3119 O  OG1 . THR C 1 39  ? 121.931 228.069 29.104  1.00 50.94  ? 39  THR C OG1 1 
ATOM   3120 C  CG2 . THR C 1 39  ? 121.274 226.640 30.981  1.00 31.24  ? 39  THR C CG2 1 
ATOM   3121 N  N   . GLU C 1 40  ? 118.514 228.541 27.897  1.00 50.64  ? 40  GLU C N   1 
ATOM   3122 C  CA  . GLU C 1 40  ? 118.082 229.413 26.827  1.00 54.37  ? 40  GLU C CA  1 
ATOM   3123 C  C   . GLU C 1 40  ? 119.296 230.219 26.356  1.00 53.48  ? 40  GLU C C   1 
ATOM   3124 O  O   . GLU C 1 40  ? 120.210 230.457 27.139  1.00 50.88  ? 40  GLU C O   1 
ATOM   3125 C  CB  . GLU C 1 40  ? 116.937 230.311 27.292  1.00 51.36  ? 40  GLU C CB  1 
ATOM   3126 C  CG  . GLU C 1 40  ? 116.191 230.963 26.158  1.00 57.14  ? 40  GLU C CG  1 
ATOM   3127 C  CD  . GLU C 1 40  ? 114.996 231.767 26.631  1.00 69.20  ? 40  GLU C CD  1 
ATOM   3128 O  OE1 . GLU C 1 40  ? 114.946 232.104 27.840  1.00 77.54  ? 40  GLU C OE1 1 
ATOM   3129 O  OE2 . GLU C 1 40  ? 114.112 232.063 25.788  1.00 65.37  1 40  GLU C OE2 1 
ATOM   3130 N  N   . GLY C 1 41  ? 119.354 230.554 25.069  1.00 43.18  ? 41  GLY C N   1 
ATOM   3131 C  CA  . GLY C 1 41  ? 120.464 231.351 24.575  1.00 47.52  ? 41  GLY C CA  1 
ATOM   3132 C  C   . GLY C 1 41  ? 121.391 230.698 23.552  1.00 47.66  ? 41  GLY C C   1 
ATOM   3133 O  O   . GLY C 1 41  ? 121.049 229.706 22.892  1.00 46.75  ? 41  GLY C O   1 
ATOM   3134 N  N   . LEU C 1 42  ? 122.568 231.292 23.393  1.00 49.45  ? 42  LEU C N   1 
ATOM   3135 C  CA  . LEU C 1 42  ? 123.534 230.833 22.400  1.00 41.70  ? 42  LEU C CA  1 
ATOM   3136 C  C   . LEU C 1 42  ? 124.565 229.873 22.972  1.00 38.52  ? 42  LEU C C   1 
ATOM   3137 O  O   . LEU C 1 42  ? 125.118 230.091 24.044  1.00 37.00  ? 42  LEU C O   1 
ATOM   3138 C  CB  . LEU C 1 42  ? 124.247 232.023 21.747  1.00 37.80  ? 42  LEU C CB  1 
ATOM   3139 C  CG  . LEU C 1 42  ? 123.600 232.757 20.564  1.00 54.58  ? 42  LEU C CG  1 
ATOM   3140 C  CD1 . LEU C 1 42  ? 122.419 233.613 20.976  1.00 58.36  ? 42  LEU C CD1 1 
ATOM   3141 C  CD2 . LEU C 1 42  ? 124.659 233.625 19.892  1.00 45.78  ? 42  LEU C CD2 1 
ATOM   3142 N  N   . HIS C 1 43  ? 124.833 228.819 22.216  1.00 34.03  ? 43  HIS C N   1 
ATOM   3143 C  CA  . HIS C 1 43  ? 125.823 227.833 22.591  1.00 35.17  ? 43  HIS C CA  1 
ATOM   3144 C  C   . HIS C 1 43  ? 126.794 227.571 21.453  1.00 33.89  ? 43  HIS C C   1 
ATOM   3145 O  O   . HIS C 1 43  ? 126.376 227.328 20.315  1.00 37.08  ? 43  HIS C O   1 
ATOM   3146 C  CB  . HIS C 1 43  ? 125.146 226.529 23.000  1.00 34.90  ? 43  HIS C CB  1 
ATOM   3147 C  CG  . HIS C 1 43  ? 124.312 226.659 24.226  1.00 44.45  ? 43  HIS C CG  1 
ATOM   3148 N  ND1 . HIS C 1 43  ? 124.792 226.335 25.479  1.00 38.54  ? 43  HIS C ND1 1 
ATOM   3149 C  CD2 . HIS C 1 43  ? 123.031 227.070 24.401  1.00 33.28  ? 43  HIS C CD2 1 
ATOM   3150 C  CE1 . HIS C 1 43  ? 123.847 226.559 26.375  1.00 37.16  ? 43  HIS C CE1 1 
ATOM   3151 N  NE2 . HIS C 1 43  ? 122.773 227.011 25.749  1.00 46.18  ? 43  HIS C NE2 1 
ATOM   3152 N  N   . GLY C 1 44  ? 128.086 227.651 21.754  1.00 35.31  ? 44  GLY C N   1 
ATOM   3153 C  CA  . GLY C 1 44  ? 129.121 227.321 20.790  1.00 31.60  ? 44  GLY C CA  1 
ATOM   3154 C  C   . GLY C 1 44  ? 129.044 225.888 20.265  1.00 32.29  ? 44  GLY C C   1 
ATOM   3155 O  O   . GLY C 1 44  ? 128.805 224.937 21.006  1.00 34.37  ? 44  GLY C O   1 
ATOM   3156 N  N   . PHE C 1 45  ? 129.293 225.749 18.973  1.00 31.18  ? 45  PHE C N   1 
ATOM   3157 C  CA  . PHE C 1 45  ? 129.031 224.530 18.217  1.00 34.56  ? 45  PHE C CA  1 
ATOM   3158 C  C   . PHE C 1 45  ? 130.130 224.383 17.162  1.00 33.56  ? 45  PHE C C   1 
ATOM   3159 O  O   . PHE C 1 45  ? 130.222 225.183 16.249  1.00 34.29  ? 45  PHE C O   1 
ATOM   3160 C  CB  . PHE C 1 45  ? 127.631 224.630 17.585  1.00 32.05  ? 45  PHE C CB  1 
ATOM   3161 C  CG  . PHE C 1 45  ? 127.116 223.353 16.974  1.00 34.73  ? 45  PHE C CG  1 
ATOM   3162 C  CD1 . PHE C 1 45  ? 126.963 222.202 17.742  1.00 35.50  ? 45  PHE C CD1 1 
ATOM   3163 C  CD2 . PHE C 1 45  ? 126.708 223.327 15.632  1.00 34.86  ? 45  PHE C CD2 1 
ATOM   3164 C  CE1 . PHE C 1 45  ? 126.455 221.021 17.168  1.00 33.83  ? 45  PHE C CE1 1 
ATOM   3165 C  CE2 . PHE C 1 45  ? 126.191 222.158 15.049  1.00 36.61  ? 45  PHE C CE2 1 
ATOM   3166 C  CZ  . PHE C 1 45  ? 126.068 221.001 15.816  1.00 37.94  ? 45  PHE C CZ  1 
ATOM   3167 N  N   . ARG C 1 46  ? 130.980 223.381 17.290  1.00 30.31  ? 46  ARG C N   1 
ATOM   3168 C  CA  . ARG C 1 46  ? 132.115 223.278 16.407  1.00 25.40  ? 46  ARG C CA  1 
ATOM   3169 C  C   . ARG C 1 46  ? 132.607 221.851 16.320  1.00 30.20  ? 46  ARG C C   1 
ATOM   3170 O  O   . ARG C 1 46  ? 132.170 220.988 17.081  1.00 28.55  ? 46  ARG C O   1 
ATOM   3171 C  CB  . ARG C 1 46  ? 133.256 224.180 16.870  1.00 31.79  ? 46  ARG C CB  1 
ATOM   3172 C  CG  . ARG C 1 46  ? 133.884 223.814 18.230  1.00 31.92  ? 46  ARG C CG  1 
ATOM   3173 C  CD  . ARG C 1 46  ? 133.053 224.330 19.392  1.00 29.83  ? 46  ARG C CD  1 
ATOM   3174 N  NE  . ARG C 1 46  ? 132.839 225.774 19.338  1.00 33.17  ? 46  ARG C NE  1 
ATOM   3175 C  CZ  . ARG C 1 46  ? 133.515 226.656 20.077  1.00 37.52  ? 46  ARG C CZ  1 
ATOM   3176 N  NH1 . ARG C 1 46  ? 134.454 226.237 20.927  1.00 23.43  1 46  ARG C NH1 1 
ATOM   3177 N  NH2 . ARG C 1 46  ? 133.252 227.962 19.968  1.00 31.34  ? 46  ARG C NH2 1 
ATOM   3178 N  N   . VAL C 1 47  ? 133.512 221.619 15.367  1.00 27.02  ? 47  VAL C N   1 
ATOM   3179 C  CA  . VAL C 1 47  ? 134.132 220.322 15.149  1.00 29.19  ? 47  VAL C CA  1 
ATOM   3180 C  C   . VAL C 1 47  ? 135.608 220.361 15.515  1.00 28.46  ? 47  VAL C C   1 
ATOM   3181 O  O   . VAL C 1 47  ? 136.279 221.320 15.190  1.00 29.35  ? 47  VAL C O   1 
ATOM   3182 C  CB  . VAL C 1 47  ? 133.960 219.896 13.694  1.00 26.13  ? 47  VAL C CB  1 
ATOM   3183 C  CG1 . VAL C 1 47  ? 134.525 218.514 13.461  1.00 27.03  ? 47  VAL C CG1 1 
ATOM   3184 C  CG2 . VAL C 1 47  ? 132.499 219.939 13.365  1.00 23.72  ? 47  VAL C CG2 1 
ATOM   3185 N  N   . GLN C 1 48  ? 136.089 219.344 16.225  1.00 21.84  ? 48  GLN C N   1 
ATOM   3186 C  CA  . GLN C 1 48  ? 137.494 219.244 16.624  1.00 26.51  ? 48  GLN C CA  1 
ATOM   3187 C  C   . GLN C 1 48  ? 138.332 218.488 15.596  1.00 34.95  ? 48  GLN C C   1 
ATOM   3188 O  O   . GLN C 1 48  ? 137.795 217.779 14.732  1.00 28.92  ? 48  GLN C O   1 
ATOM   3189 C  CB  . GLN C 1 48  ? 137.606 218.537 17.975  1.00 29.88  ? 48  GLN C CB  1 
ATOM   3190 C  CG  . GLN C 1 48  ? 136.539 219.045 18.977  1.00 36.16  ? 48  GLN C CG  1 
ATOM   3191 C  CD  . GLN C 1 48  ? 136.845 220.418 19.516  1.00 33.96  ? 48  GLN C CD  1 
ATOM   3192 O  OE1 . GLN C 1 48  ? 138.009 220.756 19.780  1.00 34.86  ? 48  GLN C OE1 1 
ATOM   3193 N  NE2 . GLN C 1 48  ? 135.817 221.247 19.620  1.00 36.16  ? 48  GLN C NE2 1 
ATOM   3194 N  N   . GLU C 1 49  ? 139.647 218.595 15.746  1.00 27.76  ? 49  GLU C N   1 
ATOM   3195 C  CA  . GLU C 1 49  ? 140.581 217.946 14.851  1.00 32.20  ? 49  GLU C CA  1 
ATOM   3196 C  C   . GLU C 1 49  ? 140.423 216.429 14.888  1.00 36.25  ? 49  GLU C C   1 
ATOM   3197 O  O   . GLU C 1 49  ? 140.360 215.774 13.848  1.00 28.11  ? 49  GLU C O   1 
ATOM   3198 C  CB  . GLU C 1 49  ? 142.010 218.336 15.222  1.00 28.41  ? 49  GLU C CB  1 
ATOM   3199 C  CG  . GLU C 1 49  ? 143.074 217.804 14.283  1.00 36.18  ? 49  GLU C CG  1 
ATOM   3200 C  CD  . GLU C 1 49  ? 144.496 218.286 14.626  1.00 41.53  ? 49  GLU C CD  1 
ATOM   3201 O  OE1 . GLU C 1 49  ? 144.691 219.036 15.616  1.00 48.74  ? 49  GLU C OE1 1 
ATOM   3202 O  OE2 . GLU C 1 49  ? 145.439 217.880 13.918  1.00 49.56  1 49  GLU C OE2 1 
ATOM   3203 N  N   . PHE C 1 50  ? 140.310 215.870 16.088  1.00 30.44  ? 50  PHE C N   1 
ATOM   3204 C  CA  . PHE C 1 50  ? 140.178 214.430 16.217  1.00 30.13  ? 50  PHE C CA  1 
ATOM   3205 C  C   . PHE C 1 50  ? 138.812 214.093 16.781  1.00 31.97  ? 50  PHE C C   1 
ATOM   3206 O  O   . PHE C 1 50  ? 138.069 214.987 17.196  1.00 32.19  ? 50  PHE C O   1 
ATOM   3207 C  CB  . PHE C 1 50  ? 141.278 213.877 17.115  1.00 32.58  ? 50  PHE C CB  1 
ATOM   3208 C  CG  . PHE C 1 50  ? 142.653 214.205 16.648  1.00 33.49  ? 50  PHE C CG  1 
ATOM   3209 C  CD1 . PHE C 1 50  ? 143.246 213.476 15.628  1.00 30.04  ? 50  PHE C CD1 1 
ATOM   3210 C  CD2 . PHE C 1 50  ? 143.350 215.269 17.201  1.00 33.28  ? 50  PHE C CD2 1 
ATOM   3211 C  CE1 . PHE C 1 50  ? 144.549 213.786 15.183  1.00 33.08  ? 50  PHE C CE1 1 
ATOM   3212 C  CE2 . PHE C 1 50  ? 144.639 215.583 16.765  1.00 32.60  ? 50  PHE C CE2 1 
ATOM   3213 C  CZ  . PHE C 1 50  ? 145.234 214.842 15.745  1.00 32.87  ? 50  PHE C CZ  1 
ATOM   3214 N  N   . GLY C 1 51  ? 138.487 212.805 16.806  1.00 31.42  ? 51  GLY C N   1 
ATOM   3215 C  CA  . GLY C 1 51  ? 137.256 212.354 17.425  1.00 34.58  ? 51  GLY C CA  1 
ATOM   3216 C  C   . GLY C 1 51  ? 137.505 211.529 18.671  1.00 36.21  ? 51  GLY C C   1 
ATOM   3217 O  O   . GLY C 1 51  ? 136.586 210.997 19.278  1.00 40.55  ? 51  GLY C O   1 
ATOM   3218 N  N   . ASP C 1 52  ? 138.773 211.440 19.034  1.00 35.16  ? 52  ASP C N   1 
ATOM   3219 C  CA  . ASP C 1 52  ? 139.263 210.708 20.184  1.00 34.39  ? 52  ASP C CA  1 
ATOM   3220 C  C   . ASP C 1 52  ? 138.842 211.413 21.487  1.00 34.08  ? 52  ASP C C   1 
ATOM   3221 O  O   . ASP C 1 52  ? 139.325 212.489 21.806  1.00 38.96  ? 52  ASP C O   1 
ATOM   3222 C  CB  . ASP C 1 52  ? 140.781 210.595 20.044  1.00 34.74  ? 52  ASP C CB  1 
ATOM   3223 C  CG  . ASP C 1 52  ? 141.423 209.735 21.100  1.00 46.33  ? 52  ASP C CG  1 
ATOM   3224 O  OD1 . ASP C 1 52  ? 140.839 209.542 22.195  1.00 35.54  ? 52  ASP C OD1 1 
ATOM   3225 O  OD2 . ASP C 1 52  ? 142.556 209.273 20.818  1.00 43.48  1 52  ASP C OD2 1 
ATOM   3226 N  N   . ASN C 1 53  ? 137.928 210.799 22.226  1.00 33.97  ? 53  ASN C N   1 
ATOM   3227 C  CA  . ASN C 1 53  ? 137.347 211.399 23.427  1.00 37.12  ? 53  ASN C CA  1 
ATOM   3228 C  C   . ASN C 1 53  ? 137.772 210.694 24.736  1.00 40.14  ? 53  ASN C C   1 
ATOM   3229 O  O   . ASN C 1 53  ? 137.090 210.771 25.755  1.00 35.14  ? 53  ASN C O   1 
ATOM   3230 C  CB  . ASN C 1 53  ? 135.820 211.397 23.306  1.00 33.09  ? 53  ASN C CB  1 
ATOM   3231 C  CG  . ASN C 1 53  ? 135.306 212.246 22.120  1.00 40.36  ? 53  ASN C CG  1 
ATOM   3232 O  OD1 . ASN C 1 53  ? 135.867 213.287 21.790  1.00 43.20  ? 53  ASN C OD1 1 
ATOM   3233 N  ND2 . ASN C 1 53  ? 134.238 211.788 21.485  1.00 43.78  ? 53  ASN C ND2 1 
ATOM   3234 N  N   . THR C 1 54  ? 138.911 210.012 24.692  1.00 38.77  ? 54  THR C N   1 
ATOM   3235 C  CA  . THR C 1 54  ? 139.445 209.308 25.850  1.00 43.91  ? 54  THR C CA  1 
ATOM   3236 C  C   . THR C 1 54  ? 139.914 210.274 26.934  1.00 50.12  ? 54  THR C C   1 
ATOM   3237 O  O   . THR C 1 54  ? 139.748 210.005 28.128  1.00 53.49  ? 54  THR C O   1 
ATOM   3238 C  CB  . THR C 1 54  ? 140.611 208.397 25.450  1.00 41.22  ? 54  THR C CB  1 
ATOM   3239 O  OG1 . THR C 1 54  ? 141.547 209.146 24.672  1.00 42.10  ? 54  THR C OG1 1 
ATOM   3240 C  CG2 . THR C 1 54  ? 140.117 207.250 24.593  1.00 35.87  ? 54  THR C CG2 1 
ATOM   3241 N  N   . ALA C 1 55  ? 140.472 211.409 26.520  1.00 44.66  ? 55  ALA C N   1 
ATOM   3242 C  CA  . ALA C 1 55  ? 141.023 212.381 27.467  1.00 42.43  ? 55  ALA C CA  1 
ATOM   3243 C  C   . ALA C 1 55  ? 140.398 213.768 27.365  1.00 50.47  ? 55  ALA C C   1 
ATOM   3244 O  O   . ALA C 1 55  ? 141.071 214.766 27.608  1.00 59.25  ? 55  ALA C O   1 
ATOM   3245 C  CB  . ALA C 1 55  ? 142.545 212.494 27.273  1.00 36.04  ? 55  ALA C CB  1 
ATOM   3246 N  N   . GLY C 1 56  ? 139.129 213.851 27.000  1.00 50.68  ? 56  GLY C N   1 
ATOM   3247 C  CA  . GLY C 1 56  ? 138.515 215.157 26.904  1.00 47.50  ? 56  GLY C CA  1 
ATOM   3248 C  C   . GLY C 1 56  ? 139.195 216.069 25.888  1.00 59.38  ? 56  GLY C C   1 
ATOM   3249 O  O   . GLY C 1 56  ? 139.599 215.641 24.792  1.00 55.43  ? 56  GLY C O   1 
ATOM   3250 N  N   . CYS C 1 57  ? 139.343 217.334 26.274  1.00 54.72  ? 57  CYS C N   1 
ATOM   3251 C  CA  . CYS C 1 57  ? 139.860 218.373 25.396  1.00 49.36  ? 57  CYS C CA  1 
ATOM   3252 C  C   . CYS C 1 57  ? 141.199 218.019 24.768  1.00 50.55  ? 57  CYS C C   1 
ATOM   3253 O  O   . CYS C 1 57  ? 141.467 218.343 23.600  1.00 63.76  ? 57  CYS C O   1 
ATOM   3254 C  CB  . CYS C 1 57  ? 140.014 219.672 26.182  1.00 57.43  ? 57  CYS C CB  1 
ATOM   3255 S  SG  . CYS C 1 57  ? 138.576 220.098 27.149  1.00 83.22  ? 57  CYS C SG  1 
ATOM   3256 N  N   . THR C 1 58  ? 142.030 217.353 25.553  1.00 37.46  ? 58  THR C N   1 
ATOM   3257 C  CA  . THR C 1 58  ? 143.394 217.040 25.153  1.00 47.31  ? 58  THR C CA  1 
ATOM   3258 C  C   . THR C 1 58  ? 143.453 215.991 24.032  1.00 45.92  ? 58  THR C C   1 
ATOM   3259 O  O   . THR C 1 58  ? 144.316 216.078 23.161  1.00 55.84  ? 58  THR C O   1 
ATOM   3260 C  CB  . THR C 1 58  ? 144.264 216.607 26.387  1.00 49.04  ? 58  THR C CB  1 
ATOM   3261 O  OG1 . THR C 1 58  ? 144.732 215.263 26.237  1.00 55.87  ? 58  THR C OG1 1 
ATOM   3262 C  CG2 . THR C 1 58  ? 143.486 216.750 27.698  1.00 44.70  ? 58  THR C CG2 1 
ATOM   3263 N  N   . SER C 1 59  ? 142.591 214.977 24.061  1.00 41.58  ? 59  SER C N   1 
ATOM   3264 C  CA  . SER C 1 59  ? 142.695 213.921 23.045  1.00 39.90  ? 59  SER C CA  1 
ATOM   3265 C  C   . SER C 1 59  ? 142.001 214.304 21.731  1.00 37.14  ? 59  SER C C   1 
ATOM   3266 O  O   . SER C 1 59  ? 142.411 213.851 20.669  1.00 41.42  ? 59  SER C O   1 
ATOM   3267 C  CB  . SER C 1 59  ? 142.139 212.576 23.575  1.00 41.79  ? 59  SER C CB  1 
ATOM   3268 O  OG  . SER C 1 59  ? 140.842 212.692 24.147  1.00 33.26  ? 59  SER C OG  1 
ATOM   3269 N  N   . ALA C 1 60  ? 140.997 215.173 21.800  1.00 31.45  ? 60  ALA C N   1 
ATOM   3270 C  CA  . ALA C 1 60  ? 140.232 215.572 20.617  1.00 38.44  ? 60  ALA C CA  1 
ATOM   3271 C  C   . ALA C 1 60  ? 140.911 216.686 19.811  1.00 44.24  ? 60  ALA C C   1 
ATOM   3272 O  O   . ALA C 1 60  ? 140.499 216.983 18.684  1.00 36.65  ? 60  ALA C O   1 
ATOM   3273 C  CB  . ALA C 1 60  ? 138.828 216.001 21.013  1.00 30.82  ? 60  ALA C CB  1 
ATOM   3274 N  N   . GLY C 1 61  ? 141.934 217.310 20.396  1.00 42.39  ? 61  GLY C N   1 
ATOM   3275 C  CA  . GLY C 1 61  ? 142.682 218.365 19.727  1.00 27.74  ? 61  GLY C CA  1 
ATOM   3276 C  C   . GLY C 1 61  ? 141.971 219.702 19.713  1.00 33.49  ? 61  GLY C C   1 
ATOM   3277 O  O   . GLY C 1 61  ? 140.847 219.832 20.243  1.00 31.07  ? 61  GLY C O   1 
ATOM   3278 N  N   . PRO C 1 62  ? 142.611 220.721 19.098  1.00 37.19  ? 62  PRO C N   1 
ATOM   3279 C  CA  . PRO C 1 62  ? 141.979 222.046 18.916  1.00 34.30  ? 62  PRO C CA  1 
ATOM   3280 C  C   . PRO C 1 62  ? 140.856 221.977 17.868  1.00 28.61  ? 62  PRO C C   1 
ATOM   3281 O  O   . PRO C 1 62  ? 140.603 220.887 17.339  1.00 25.92  ? 62  PRO C O   1 
ATOM   3282 C  CB  . PRO C 1 62  ? 143.133 222.930 18.439  1.00 30.58  ? 62  PRO C CB  1 
ATOM   3283 C  CG  . PRO C 1 62  ? 144.089 221.975 17.780  1.00 27.94  ? 62  PRO C CG  1 
ATOM   3284 C  CD  . PRO C 1 62  ? 143.957 220.652 18.501  1.00 26.49  ? 62  PRO C CD  1 
ATOM   3285 N  N   . HIS C 1 63  ? 140.171 223.085 17.594  1.00 26.21  ? 63  HIS C N   1 
ATOM   3286 C  CA  . HIS C 1 63  ? 139.215 223.102 16.470  1.00 28.57  ? 63  HIS C CA  1 
ATOM   3287 C  C   . HIS C 1 63  ? 139.837 222.587 15.170  1.00 23.58  ? 63  HIS C C   1 
ATOM   3288 O  O   . HIS C 1 63  ? 141.025 222.795 14.927  1.00 28.74  ? 63  HIS C O   1 
ATOM   3289 C  CB  . HIS C 1 63  ? 138.656 224.502 16.247  1.00 24.03  ? 63  HIS C CB  1 
ATOM   3290 C  CG  . HIS C 1 63  ? 137.872 225.007 17.411  1.00 30.71  ? 63  HIS C CG  1 
ATOM   3291 N  ND1 . HIS C 1 63  ? 137.111 226.153 17.360  1.00 35.31  ? 63  HIS C ND1 1 
ATOM   3292 C  CD2 . HIS C 1 63  ? 137.741 224.522 18.669  1.00 23.75  ? 63  HIS C CD2 1 
ATOM   3293 C  CE1 . HIS C 1 63  ? 136.528 226.344 18.529  1.00 25.90  ? 63  HIS C CE1 1 
ATOM   3294 N  NE2 . HIS C 1 63  ? 136.906 225.377 19.345  1.00 21.59  ? 63  HIS C NE2 1 
ATOM   3295 N  N   . PHE C 1 64  ? 139.059 221.852 14.380  1.00 25.20  ? 64  PHE C N   1 
ATOM   3296 C  CA  . PHE C 1 64  ? 139.544 221.347 13.084  1.00 29.95  ? 64  PHE C CA  1 
ATOM   3297 C  C   . PHE C 1 64  ? 140.034 222.511 12.232  1.00 27.84  ? 64  PHE C C   1 
ATOM   3298 O  O   . PHE C 1 64  ? 139.269 223.406 11.882  1.00 28.67  ? 64  PHE C O   1 
ATOM   3299 C  CB  . PHE C 1 64  ? 138.443 220.588 12.374  1.00 27.01  ? 64  PHE C CB  1 
ATOM   3300 C  CG  . PHE C 1 64  ? 138.845 219.971 11.065  1.00 24.67  ? 64  PHE C CG  1 
ATOM   3301 C  CD1 . PHE C 1 64  ? 140.038 219.335 10.931  1.00 22.26  ? 64  PHE C CD1 1 
ATOM   3302 C  CD2 . PHE C 1 64  ? 137.945 219.947 9.997   1.00 27.94  ? 64  PHE C CD2 1 
ATOM   3303 C  CE1 . PHE C 1 64  ? 140.386 218.729 9.752   1.00 25.42  ? 64  PHE C CE1 1 
ATOM   3304 C  CE2 . PHE C 1 64  ? 138.255 219.339 8.823   1.00 26.44  ? 64  PHE C CE2 1 
ATOM   3305 C  CZ  . PHE C 1 64  ? 139.497 218.723 8.688   1.00 33.06  ? 64  PHE C CZ  1 
ATOM   3306 N  N   . ASN C 1 65  ? 141.315 222.491 11.901  1.00 27.66  ? 65  ASN C N   1 
ATOM   3307 C  CA  . ASN C 1 65  ? 141.951 223.673 11.332  1.00 33.40  ? 65  ASN C CA  1 
ATOM   3308 C  C   . ASN C 1 65  ? 143.033 223.353 10.289  1.00 33.90  ? 65  ASN C C   1 
ATOM   3309 O  O   . ASN C 1 65  ? 144.182 223.744 10.444  1.00 39.10  ? 65  ASN C O   1 
ATOM   3310 C  CB  . ASN C 1 65  ? 142.522 224.506 12.494  1.00 26.74  ? 65  ASN C CB  1 
ATOM   3311 C  CG  . ASN C 1 65  ? 143.008 225.879 12.067  1.00 34.81  ? 65  ASN C CG  1 
ATOM   3312 O  OD1 . ASN C 1 65  ? 142.676 226.353 10.978  1.00 35.52  ? 65  ASN C OD1 1 
ATOM   3313 N  ND2 . ASN C 1 65  ? 143.726 226.564 12.963  1.00 29.45  ? 65  ASN C ND2 1 
ATOM   3314 N  N   . PRO C 1 66  ? 142.661 222.658 9.195   1.00 35.56  ? 66  PRO C N   1 
ATOM   3315 C  CA  . PRO C 1 66  ? 143.688 222.253 8.218   1.00 33.63  ? 66  PRO C CA  1 
ATOM   3316 C  C   . PRO C 1 66  ? 144.289 223.425 7.429   1.00 36.58  ? 66  PRO C C   1 
ATOM   3317 O  O   . PRO C 1 66  ? 145.333 223.270 6.830   1.00 40.39  ? 66  PRO C O   1 
ATOM   3318 C  CB  . PRO C 1 66  ? 142.930 221.302 7.279   1.00 30.58  ? 66  PRO C CB  1 
ATOM   3319 C  CG  . PRO C 1 66  ? 141.533 221.687 7.384   1.00 33.39  ? 66  PRO C CG  1 
ATOM   3320 C  CD  . PRO C 1 66  ? 141.319 222.194 8.796   1.00 31.01  ? 66  PRO C CD  1 
ATOM   3321 N  N   . LEU C 1 67  ? 143.627 224.573 7.416   1.00 36.86  ? 67  LEU C N   1 
ATOM   3322 C  CA  . LEU C 1 67  ? 144.156 225.744 6.729   1.00 34.70  ? 67  LEU C CA  1 
ATOM   3323 C  C   . LEU C 1 67  ? 144.922 226.690 7.658   1.00 36.01  ? 67  LEU C C   1 
ATOM   3324 O  O   . LEU C 1 67  ? 145.326 227.771 7.239   1.00 36.72  ? 67  LEU C O   1 
ATOM   3325 C  CB  . LEU C 1 67  ? 143.021 226.494 6.017   1.00 36.34  ? 67  LEU C CB  1 
ATOM   3326 C  CG  . LEU C 1 67  ? 142.399 225.651 4.899   1.00 34.37  ? 67  LEU C CG  1 
ATOM   3327 C  CD1 . LEU C 1 67  ? 141.283 226.405 4.218   1.00 31.04  ? 67  LEU C CD1 1 
ATOM   3328 C  CD2 . LEU C 1 67  ? 143.466 225.208 3.909   1.00 31.71  ? 67  LEU C CD2 1 
ATOM   3329 N  N   . SER C 1 68  ? 145.083 226.292 8.918   1.00 33.18  ? 68  SER C N   1 
ATOM   3330 C  CA  . SER C 1 68  ? 145.864 227.042 9.905   1.00 32.90  ? 68  SER C CA  1 
ATOM   3331 C  C   . SER C 1 68  ? 145.445 228.485 10.091  1.00 31.27  ? 68  SER C C   1 
ATOM   3332 O  O   . SER C 1 68  ? 146.263 229.382 10.006  1.00 36.10  ? 68  SER C O   1 
ATOM   3333 C  CB  . SER C 1 68  ? 147.332 227.034 9.506   1.00 27.79  ? 68  SER C CB  1 
ATOM   3334 O  OG  . SER C 1 68  ? 147.787 225.707 9.336   1.00 38.23  ? 68  SER C OG  1 
ATOM   3335 N  N   . ARG C 1 69  ? 144.178 228.699 10.388  1.00 24.80  ? 69  ARG C N   1 
ATOM   3336 C  CA  . ARG C 1 69  ? 143.682 230.029 10.607  1.00 22.75  ? 69  ARG C CA  1 
ATOM   3337 C  C   . ARG C 1 69  ? 143.417 230.271 12.093  1.00 35.97  ? 69  ARG C C   1 
ATOM   3338 O  O   . ARG C 1 69  ? 143.563 229.391 12.957  1.00 25.53  ? 69  ARG C O   1 
ATOM   3339 C  CB  . ARG C 1 69  ? 142.394 230.264 9.814   1.00 29.08  ? 69  ARG C CB  1 
ATOM   3340 C  CG  . ARG C 1 69  ? 142.522 229.914 8.342   1.00 29.19  ? 69  ARG C CG  1 
ATOM   3341 C  CD  . ARG C 1 69  ? 143.480 230.795 7.598   1.00 17.69  ? 69  ARG C CD  1 
ATOM   3342 N  NE  . ARG C 1 69  ? 143.273 232.237 7.797   1.00 29.38  ? 69  ARG C NE  1 
ATOM   3343 C  CZ  . ARG C 1 69  ? 142.512 233.013 7.028   1.00 28.87  ? 69  ARG C CZ  1 
ATOM   3344 N  NH1 . ARG C 1 69  ? 141.833 232.490 6.008   1.00 33.19  1 69  ARG C NH1 1 
ATOM   3345 N  NH2 . ARG C 1 69  ? 142.407 234.308 7.296   1.00 28.27  ? 69  ARG C NH2 1 
ATOM   3346 N  N   . LYS C 1 70  ? 142.976 231.475 12.380  1.00 42.39  ? 70  LYS C N   1 
ATOM   3347 C  CA  . LYS C 1 70  ? 142.477 231.753 13.698  1.00 30.99  ? 70  LYS C CA  1 
ATOM   3348 C  C   . LYS C 1 70  ? 140.998 231.456 13.724  1.00 33.44  ? 70  LYS C C   1 
ATOM   3349 O  O   . LYS C 1 70  ? 140.357 231.305 12.669  1.00 34.60  ? 70  LYS C O   1 
ATOM   3350 C  CB  . LYS C 1 70  ? 142.756 233.197 14.075  1.00 28.93  ? 70  LYS C CB  1 
ATOM   3351 C  CG  . LYS C 1 70  ? 144.236 233.482 14.287  1.00 37.95  ? 70  LYS C CG  1 
ATOM   3352 C  CD  . LYS C 1 70  ? 144.412 234.922 14.763  1.00 45.79  ? 70  LYS C CD  1 
ATOM   3353 C  CE  . LYS C 1 70  ? 145.868 235.288 15.040  1.00 40.06  ? 70  LYS C CE  1 
ATOM   3354 N  NZ  . LYS C 1 70  ? 145.982 236.760 15.273  1.00 48.28  1 70  LYS C NZ  1 
ATOM   3355 N  N   . HIS C 1 71  ? 140.467 231.342 14.936  1.00 29.23  ? 71  HIS C N   1 
ATOM   3356 C  CA  . HIS C 1 71  ? 139.064 231.059 15.156  1.00 33.02  ? 71  HIS C CA  1 
ATOM   3357 C  C   . HIS C 1 71  ? 138.153 232.202 14.685  1.00 29.78  ? 71  HIS C C   1 
ATOM   3358 O  O   . HIS C 1 71  ? 138.478 233.368 14.841  1.00 32.37  ? 71  HIS C O   1 
ATOM   3359 C  CB  . HIS C 1 71  ? 138.837 230.760 16.656  1.00 30.53  ? 71  HIS C CB  1 
ATOM   3360 C  CG  . HIS C 1 71  ? 137.409 230.554 17.004  1.00 22.36  ? 71  HIS C CG  1 
ATOM   3361 N  ND1 . HIS C 1 71  ? 136.748 229.375 16.738  1.00 21.23  ? 71  HIS C ND1 1 
ATOM   3362 C  CD2 . HIS C 1 71  ? 136.496 231.391 17.555  1.00 25.12  ? 71  HIS C CD2 1 
ATOM   3363 C  CE1 . HIS C 1 71  ? 135.490 229.484 17.131  1.00 30.56  ? 71  HIS C CE1 1 
ATOM   3364 N  NE2 . HIS C 1 71  ? 135.308 230.696 17.627  1.00 30.27  ? 71  HIS C NE2 1 
ATOM   3365 N  N   . GLY C 1 72  ? 137.000 231.867 14.125  1.00 23.02  ? 72  GLY C N   1 
ATOM   3366 C  CA  . GLY C 1 72  ? 136.059 232.899 13.753  1.00 29.83  ? 72  GLY C CA  1 
ATOM   3367 C  C   . GLY C 1 72  ? 134.663 232.342 13.684  1.00 32.99  ? 72  GLY C C   1 
ATOM   3368 O  O   . GLY C 1 72  ? 134.471 231.143 13.858  1.00 26.88  ? 72  GLY C O   1 
ATOM   3369 N  N   . GLY C 1 73  ? 133.689 233.204 13.413  1.00 30.99  ? 73  GLY C N   1 
ATOM   3370 C  CA  . GLY C 1 73  ? 132.335 232.751 13.146  1.00 31.24  ? 73  GLY C CA  1 
ATOM   3371 C  C   . GLY C 1 73  ? 132.228 232.110 11.762  1.00 37.75  ? 73  GLY C C   1 
ATOM   3372 O  O   . GLY C 1 73  ? 133.094 232.299 10.915  1.00 34.60  ? 73  GLY C O   1 
ATOM   3373 N  N   . PRO C 1 74  ? 131.144 231.367 11.515  1.00 35.26  ? 74  PRO C N   1 
ATOM   3374 C  CA  . PRO C 1 74  ? 131.048 230.617 10.254  1.00 40.65  ? 74  PRO C CA  1 
ATOM   3375 C  C   . PRO C 1 74  ? 131.042 231.538 9.030   1.00 42.60  ? 74  PRO C C   1 
ATOM   3376 O  O   . PRO C 1 74  ? 131.527 231.128 7.985   1.00 34.41  ? 74  PRO C O   1 
ATOM   3377 C  CB  . PRO C 1 74  ? 129.724 229.848 10.375  1.00 30.43  ? 74  PRO C CB  1 
ATOM   3378 C  CG  . PRO C 1 74  ? 129.098 230.269 11.651  1.00 37.10  ? 74  PRO C CG  1 
ATOM   3379 C  CD  . PRO C 1 74  ? 129.885 231.383 12.268  1.00 32.69  ? 74  PRO C CD  1 
ATOM   3380 N  N   . LYS C 1 75  ? 130.548 232.765 9.171   1.00 47.09  ? 75  LYS C N   1 
ATOM   3381 C  CA  . LYS C 1 75  ? 130.444 233.658 8.029   1.00 39.49  ? 75  LYS C CA  1 
ATOM   3382 C  C   . LYS C 1 75  ? 131.745 234.382 7.747   1.00 49.02  ? 75  LYS C C   1 
ATOM   3383 O  O   . LYS C 1 75  ? 131.868 235.031 6.720   1.00 55.24  ? 75  LYS C O   1 
ATOM   3384 C  CB  . LYS C 1 75  ? 129.352 234.701 8.253   1.00 45.42  ? 75  LYS C CB  1 
ATOM   3385 C  CG  . LYS C 1 75  ? 127.955 234.128 8.463   1.00 62.96  ? 75  LYS C CG  1 
ATOM   3386 C  CD  . LYS C 1 75  ? 126.889 235.235 8.536   1.00 53.46  ? 75  LYS C CD  1 
ATOM   3387 C  CE  . LYS C 1 75  ? 127.132 236.198 9.669   1.00 53.42  ? 75  LYS C CE  1 
ATOM   3388 N  NZ  . LYS C 1 75  ? 126.140 237.313 9.675   1.00 72.82  1 75  LYS C NZ  1 
ATOM   3389 N  N   . ASP C 1 76  ? 132.725 234.269 8.638   1.00 48.06  ? 76  ASP C N   1 
ATOM   3390 C  CA  . ASP C 1 76  ? 133.955 235.060 8.500   1.00 38.35  ? 76  ASP C CA  1 
ATOM   3391 C  C   . ASP C 1 76  ? 134.934 234.430 7.536   1.00 39.87  ? 76  ASP C C   1 
ATOM   3392 O  O   . ASP C 1 76  ? 135.011 233.201 7.424   1.00 41.85  ? 76  ASP C O   1 
ATOM   3393 C  CB  . ASP C 1 76  ? 134.660 235.237 9.854   1.00 42.17  ? 76  ASP C CB  1 
ATOM   3394 C  CG  . ASP C 1 76  ? 133.836 236.028 10.848  1.00 59.41  ? 76  ASP C CG  1 
ATOM   3395 O  OD1 . ASP C 1 76  ? 133.023 236.881 10.414  1.00 67.19  ? 76  ASP C OD1 1 
ATOM   3396 O  OD2 . ASP C 1 76  ? 133.995 235.783 12.069  1.00 65.51  1 76  ASP C OD2 1 
ATOM   3397 N  N   . GLU C 1 77  ? 135.713 235.266 6.865   1.00 40.81  ? 77  GLU C N   1 
ATOM   3398 C  CA  . GLU C 1 77  ? 136.799 234.749 6.029   1.00 41.64  ? 77  GLU C CA  1 
ATOM   3399 C  C   . GLU C 1 77  ? 137.884 234.044 6.858   1.00 37.73  ? 77  GLU C C   1 
ATOM   3400 O  O   . GLU C 1 77  ? 138.365 232.985 6.487   1.00 40.26  ? 77  GLU C O   1 
ATOM   3401 C  CB  . GLU C 1 77  ? 137.430 235.875 5.223   1.00 30.26  ? 77  GLU C CB  1 
ATOM   3402 C  CG  . GLU C 1 77  ? 138.409 235.376 4.139   1.00 55.78  ? 77  GLU C CG  1 
ATOM   3403 C  CD  . GLU C 1 77  ? 139.812 235.058 4.695   1.00 49.81  ? 77  GLU C CD  1 
ATOM   3404 O  OE1 . GLU C 1 77  ? 140.467 234.104 4.211   1.00 49.95  ? 77  GLU C OE1 1 
ATOM   3405 O  OE2 . GLU C 1 77  ? 140.258 235.759 5.629   1.00 43.90  1 77  GLU C OE2 1 
ATOM   3406 N  N   . GLU C 1 78  ? 138.251 234.615 7.997   1.00 37.82  ? 78  GLU C N   1 
ATOM   3407 C  CA  . GLU C 1 78  ? 139.192 233.932 8.876   1.00 35.46  ? 78  GLU C CA  1 
ATOM   3408 C  C   . GLU C 1 78  ? 138.455 233.088 9.946   1.00 31.84  ? 78  GLU C C   1 
ATOM   3409 O  O   . GLU C 1 78  ? 137.828 233.629 10.841  1.00 30.08  ? 78  GLU C O   1 
ATOM   3410 C  CB  . GLU C 1 78  ? 140.121 234.920 9.575   1.00 32.51  ? 78  GLU C CB  1 
ATOM   3411 C  CG  . GLU C 1 78  ? 141.044 234.146 10.524  1.00 39.46  ? 78  GLU C CG  1 
ATOM   3412 C  CD  . GLU C 1 78  ? 142.276 234.888 10.953  1.00 46.37  ? 78  GLU C CD  1 
ATOM   3413 O  OE1 . GLU C 1 78  ? 142.119 236.015 11.468  1.00 40.64  ? 78  GLU C OE1 1 
ATOM   3414 O  OE2 . GLU C 1 78  ? 143.399 234.321 10.784  1.00 56.41  1 78  GLU C OE2 1 
ATOM   3415 N  N   . ARG C 1 79  ? 138.555 231.769 9.823   1.00 24.17  ? 79  ARG C N   1 
ATOM   3416 C  CA  . ARG C 1 79  ? 137.876 230.827 10.692  1.00 26.07  ? 79  ARG C CA  1 
ATOM   3417 C  C   . ARG C 1 79  ? 138.515 229.478 10.525  1.00 27.34  ? 79  ARG C C   1 
ATOM   3418 O  O   . ARG C 1 79  ? 139.148 229.197 9.510   1.00 32.05  ? 79  ARG C O   1 
ATOM   3419 C  CB  . ARG C 1 79  ? 136.377 230.720 10.383  1.00 26.18  ? 79  ARG C CB  1 
ATOM   3420 C  CG  . ARG C 1 79  ? 136.114 230.391 8.893   1.00 35.61  ? 79  ARG C CG  1 
ATOM   3421 C  CD  . ARG C 1 79  ? 134.710 229.870 8.636   1.00 28.38  ? 79  ARG C CD  1 
ATOM   3422 N  NE  . ARG C 1 79  ? 134.582 228.442 8.876   1.00 28.63  ? 79  ARG C NE  1 
ATOM   3423 C  CZ  . ARG C 1 79  ? 133.492 227.740 8.583   1.00 41.25  ? 79  ARG C CZ  1 
ATOM   3424 N  NH1 . ARG C 1 79  ? 132.423 228.346 8.069   1.00 35.45  1 79  ARG C NH1 1 
ATOM   3425 N  NH2 . ARG C 1 79  ? 133.467 226.432 8.803   1.00 38.47  ? 79  ARG C NH2 1 
ATOM   3426 N  N   . HIS C 1 80  ? 138.355 228.642 11.537  1.00 29.01  ? 80  HIS C N   1 
ATOM   3427 C  CA  . HIS C 1 80  ? 138.770 227.255 11.424  1.00 30.79  ? 80  HIS C CA  1 
ATOM   3428 C  C   . HIS C 1 80  ? 137.727 226.553 10.550  1.00 29.17  ? 80  HIS C C   1 
ATOM   3429 O  O   . HIS C 1 80  ? 136.540 226.909 10.577  1.00 31.65  ? 80  HIS C O   1 
ATOM   3430 C  CB  . HIS C 1 80  ? 138.842 226.579 12.810  1.00 27.82  ? 80  HIS C CB  1 
ATOM   3431 C  CG  . HIS C 1 80  ? 139.729 227.270 13.795  1.00 24.28  ? 80  HIS C CG  1 
ATOM   3432 N  ND1 . HIS C 1 80  ? 139.358 227.478 15.108  1.00 30.50  ? 80  HIS C ND1 1 
ATOM   3433 C  CD2 . HIS C 1 80  ? 140.986 227.759 13.680  1.00 31.17  ? 80  HIS C CD2 1 
ATOM   3434 C  CE1 . HIS C 1 80  ? 140.342 228.073 15.755  1.00 30.75  ? 80  HIS C CE1 1 
ATOM   3435 N  NE2 . HIS C 1 80  ? 141.342 228.257 14.913  1.00 35.29  ? 80  HIS C NE2 1 
ATOM   3436 N  N   . VAL C 1 81  ? 138.138 225.513 9.844   1.00 29.13  ? 81  VAL C N   1 
ATOM   3437 C  CA  . VAL C 1 81  ? 137.180 224.700 9.113   1.00 31.61  ? 81  VAL C CA  1 
ATOM   3438 C  C   . VAL C 1 81  ? 136.069 224.160 10.064  1.00 28.19  ? 81  VAL C C   1 
ATOM   3439 O  O   . VAL C 1 81  ? 134.897 224.134 9.701   1.00 32.26  ? 81  VAL C O   1 
ATOM   3440 C  CB  . VAL C 1 81  ? 137.902 223.546 8.370   1.00 34.64  ? 81  VAL C CB  1 
ATOM   3441 C  CG1 . VAL C 1 81  ? 136.907 222.518 7.851   1.00 30.30  ? 81  VAL C CG1 1 
ATOM   3442 C  CG2 . VAL C 1 81  ? 138.746 224.114 7.213   1.00 30.01  ? 81  VAL C CG2 1 
ATOM   3443 N  N   . GLY C 1 82  ? 136.425 223.773 11.284  1.00 32.22  ? 82  GLY C N   1 
ATOM   3444 C  CA  . GLY C 1 82  ? 135.441 223.274 12.235  1.00 24.84  ? 82  GLY C CA  1 
ATOM   3445 C  C   . GLY C 1 82  ? 134.510 224.306 12.882  1.00 31.49  ? 82  GLY C C   1 
ATOM   3446 O  O   . GLY C 1 82  ? 133.664 223.947 13.696  1.00 33.17  ? 82  GLY C O   1 
ATOM   3447 N  N   . ASP C 1 83  ? 134.653 225.589 12.551  1.00 31.62  ? 83  ASP C N   1 
ATOM   3448 C  CA  . ASP C 1 83  ? 133.875 226.610 13.257  1.00 30.84  ? 83  ASP C CA  1 
ATOM   3449 C  C   . ASP C 1 83  ? 132.461 226.684 12.685  1.00 36.82  ? 83  ASP C C   1 
ATOM   3450 O  O   . ASP C 1 83  ? 132.273 227.089 11.552  1.00 38.43  ? 83  ASP C O   1 
ATOM   3451 C  CB  . ASP C 1 83  ? 134.533 227.993 13.198  1.00 25.17  ? 83  ASP C CB  1 
ATOM   3452 C  CG  . ASP C 1 83  ? 135.838 228.072 13.987  1.00 35.80  ? 83  ASP C CG  1 
ATOM   3453 O  OD1 . ASP C 1 83  ? 136.085 227.197 14.847  1.00 28.95  ? 83  ASP C OD1 1 
ATOM   3454 O  OD2 . ASP C 1 83  ? 136.610 229.033 13.749  1.00 29.06  1 83  ASP C OD2 1 
ATOM   3455 N  N   . LEU C 1 84  ? 131.475 226.254 13.471  1.00 36.09  ? 84  LEU C N   1 
ATOM   3456 C  CA  . LEU C 1 84  ? 130.086 226.227 13.032  1.00 33.75  ? 84  LEU C CA  1 
ATOM   3457 C  C   . LEU C 1 84  ? 129.209 227.222 13.794  1.00 35.36  ? 84  LEU C C   1 
ATOM   3458 O  O   . LEU C 1 84  ? 128.000 227.180 13.701  1.00 35.07  ? 84  LEU C O   1 
ATOM   3459 C  CB  . LEU C 1 84  ? 129.532 224.802 13.179  1.00 25.53  ? 84  LEU C CB  1 
ATOM   3460 C  CG  . LEU C 1 84  ? 130.228 223.759 12.287  1.00 31.19  ? 84  LEU C CG  1 
ATOM   3461 C  CD1 . LEU C 1 84  ? 129.669 222.356 12.533  1.00 35.82  ? 84  LEU C CD1 1 
ATOM   3462 C  CD2 . LEU C 1 84  ? 130.040 224.150 10.797  1.00 29.31  ? 84  LEU C CD2 1 
ATOM   3463 N  N   . GLY C 1 85  ? 129.835 228.148 14.500  1.00 32.81  ? 85  GLY C N   1 
ATOM   3464 C  CA  . GLY C 1 85  ? 129.130 229.221 15.183  1.00 36.09  ? 85  GLY C CA  1 
ATOM   3465 C  C   . GLY C 1 85  ? 128.410 228.844 16.472  1.00 33.04  ? 85  GLY C C   1 
ATOM   3466 O  O   . GLY C 1 85  ? 128.931 228.105 17.292  1.00 29.88  ? 85  GLY C O   1 
ATOM   3467 N  N   . ASN C 1 86  ? 127.197 229.359 16.620  1.00 39.48  ? 86  ASN C N   1 
ATOM   3468 C  CA  . ASN C 1 86  ? 126.353 229.161 17.781  1.00 33.32  ? 86  ASN C CA  1 
ATOM   3469 C  C   . ASN C 1 86  ? 125.038 228.480 17.384  1.00 40.96  ? 86  ASN C C   1 
ATOM   3470 O  O   . ASN C 1 86  ? 124.459 228.808 16.353  1.00 38.96  ? 86  ASN C O   1 
ATOM   3471 C  CB  . ASN C 1 86  ? 126.047 230.500 18.444  1.00 37.35  ? 86  ASN C CB  1 
ATOM   3472 C  CG  . ASN C 1 86  ? 127.219 231.068 19.203  1.00 36.43  ? 86  ASN C CG  1 
ATOM   3473 O  OD1 . ASN C 1 86  ? 127.751 230.435 20.110  1.00 42.13  ? 86  ASN C OD1 1 
ATOM   3474 N  ND2 . ASN C 1 86  ? 127.628 232.274 18.841  1.00 40.09  ? 86  ASN C ND2 1 
ATOM   3475 N  N   . VAL C 1 87  ? 124.559 227.540 18.194  1.00 40.10  ? 87  VAL C N   1 
ATOM   3476 C  CA  . VAL C 1 87  ? 123.189 227.070 18.025  1.00 35.30  ? 87  VAL C CA  1 
ATOM   3477 C  C   . VAL C 1 87  ? 122.367 227.773 19.094  1.00 41.66  ? 87  VAL C C   1 
ATOM   3478 O  O   . VAL C 1 87  ? 122.905 228.137 20.148  1.00 44.53  ? 87  VAL C O   1 
ATOM   3479 C  CB  . VAL C 1 87  ? 123.074 225.534 18.129  1.00 41.24  ? 87  VAL C CB  1 
ATOM   3480 C  CG1 . VAL C 1 87  ? 124.068 224.905 17.171  1.00 36.60  ? 87  VAL C CG1 1 
ATOM   3481 C  CG2 . VAL C 1 87  ? 123.356 225.046 19.520  1.00 32.43  ? 87  VAL C CG2 1 
ATOM   3482 N  N   . THR C 1 88  ? 121.081 227.998 18.829  1.00 40.87  ? 88  THR C N   1 
ATOM   3483 C  CA  . THR C 1 88  ? 120.259 228.777 19.751  1.00 44.66  ? 88  THR C CA  1 
ATOM   3484 C  C   . THR C 1 88  ? 119.190 227.920 20.418  1.00 42.51  ? 88  THR C C   1 
ATOM   3485 O  O   . THR C 1 88  ? 118.370 227.291 19.747  1.00 45.21  ? 88  THR C O   1 
ATOM   3486 C  CB  . THR C 1 88  ? 119.587 229.972 19.044  1.00 49.09  ? 88  THR C CB  1 
ATOM   3487 O  OG1 . THR C 1 88  ? 120.576 230.696 18.307  1.00 53.60  ? 88  THR C OG1 1 
ATOM   3488 C  CG2 . THR C 1 88  ? 118.945 230.928 20.083  1.00 43.88  ? 88  THR C CG2 1 
ATOM   3489 N  N   . ALA C 1 89  ? 119.208 227.901 21.747  1.00 45.82  ? 89  ALA C N   1 
ATOM   3490 C  CA  . ALA C 1 89  ? 118.214 227.147 22.517  1.00 47.26  ? 89  ALA C CA  1 
ATOM   3491 C  C   . ALA C 1 89  ? 117.004 228.016 22.854  1.00 44.81  ? 89  ALA C C   1 
ATOM   3492 O  O   . ALA C 1 89  ? 117.172 229.144 23.323  1.00 51.84  ? 89  ALA C O   1 
ATOM   3493 C  CB  . ALA C 1 89  ? 118.839 226.595 23.778  1.00 43.50  ? 89  ALA C CB  1 
ATOM   3494 N  N   . ASP C 1 90  ? 115.792 227.500 22.618  1.00 50.37  ? 90  ASP C N   1 
ATOM   3495 C  CA  . ASP C 1 90  ? 114.558 228.247 22.939  1.00 50.92  ? 90  ASP C CA  1 
ATOM   3496 C  C   . ASP C 1 90  ? 114.252 228.213 24.445  1.00 55.65  ? 90  ASP C C   1 
ATOM   3497 O  O   . ASP C 1 90  ? 115.050 227.686 25.236  1.00 60.06  ? 90  ASP C O   1 
ATOM   3498 C  CB  . ASP C 1 90  ? 113.352 227.713 22.133  1.00 52.68  ? 90  ASP C CB  1 
ATOM   3499 C  CG  . ASP C 1 90  ? 112.963 226.274 22.491  1.00 55.40  ? 90  ASP C CG  1 
ATOM   3500 O  OD1 . ASP C 1 90  ? 113.269 225.813 23.609  1.00 53.78  ? 90  ASP C OD1 1 
ATOM   3501 O  OD2 . ASP C 1 90  ? 112.335 225.595 21.643  1.00 63.16  1 90  ASP C OD2 1 
ATOM   3502 N  N   . LYS C 1 91  ? 113.093 228.731 24.847  1.00 56.92  ? 91  LYS C N   1 
ATOM   3503 C  CA  . LYS C 1 91  ? 112.765 228.799 26.285  1.00 66.98  ? 91  LYS C CA  1 
ATOM   3504 C  C   . LYS C 1 91  ? 112.736 227.418 26.959  1.00 57.83  ? 91  LYS C C   1 
ATOM   3505 O  O   . LYS C 1 91  ? 112.849 227.315 28.168  1.00 52.52  ? 91  LYS C O   1 
ATOM   3506 C  CB  . LYS C 1 91  ? 111.411 229.477 26.530  1.00 70.43  ? 91  LYS C CB  1 
ATOM   3507 C  CG  . LYS C 1 91  ? 110.261 228.958 25.660  1.00 76.16  ? 91  LYS C CG  1 
ATOM   3508 C  CD  . LYS C 1 91  ? 108.959 229.691 25.971  1.00 76.79  ? 91  LYS C CD  1 
ATOM   3509 C  CE  . LYS C 1 91  ? 107.821 229.200 25.089  1.00 74.62  ? 91  LYS C CE  1 
ATOM   3510 N  NZ  . LYS C 1 91  ? 106.537 229.871 25.423  1.00 80.25  1 91  LYS C NZ  1 
ATOM   3511 N  N   . ASP C 1 92  ? 112.515 226.363 26.187  1.00 56.92  ? 92  ASP C N   1 
ATOM   3512 C  CA  . ASP C 1 92  ? 112.406 225.030 26.777  1.00 61.02  ? 92  ASP C CA  1 
ATOM   3513 C  C   . ASP C 1 92  ? 113.738 224.281 26.764  1.00 56.67  ? 92  ASP C C   1 
ATOM   3514 O  O   . ASP C 1 92  ? 113.806 223.089 27.080  1.00 53.84  ? 92  ASP C O   1 
ATOM   3515 C  CB  . ASP C 1 92  ? 111.324 224.232 26.047  1.00 63.48  ? 92  ASP C CB  1 
ATOM   3516 C  CG  . ASP C 1 92  ? 109.980 224.949 26.057  1.00 74.75  ? 92  ASP C CG  1 
ATOM   3517 O  OD1 . ASP C 1 92  ? 109.357 225.042 27.141  1.00 67.37  ? 92  ASP C OD1 1 
ATOM   3518 O  OD2 . ASP C 1 92  ? 109.559 225.422 24.977  1.00 79.40  1 92  ASP C OD2 1 
ATOM   3519 N  N   . GLY C 1 93  ? 114.800 224.997 26.418  1.00 53.10  ? 93  GLY C N   1 
ATOM   3520 C  CA  . GLY C 1 93  ? 116.120 224.411 26.410  1.00 47.05  ? 93  GLY C CA  1 
ATOM   3521 C  C   . GLY C 1 93  ? 116.365 223.550 25.193  1.00 44.98  ? 93  GLY C C   1 
ATOM   3522 O  O   . GLY C 1 93  ? 117.198 222.648 25.200  1.00 44.65  ? 93  GLY C O   1 
ATOM   3523 N  N   . VAL C 1 94  ? 115.608 223.798 24.138  1.00 47.38  ? 94  VAL C N   1 
ATOM   3524 C  CA  . VAL C 1 94  ? 115.788 223.019 22.923  1.00 47.29  ? 94  VAL C CA  1 
ATOM   3525 C  C   . VAL C 1 94  ? 116.372 223.876 21.819  1.00 46.66  ? 94  VAL C C   1 
ATOM   3526 O  O   . VAL C 1 94  ? 115.857 224.951 21.488  1.00 48.70  ? 94  VAL C O   1 
ATOM   3527 C  CB  . VAL C 1 94  ? 114.482 222.367 22.471  1.00 52.87  ? 94  VAL C CB  1 
ATOM   3528 C  CG1 . VAL C 1 94  ? 114.585 221.900 21.024  1.00 47.69  ? 94  VAL C CG1 1 
ATOM   3529 C  CG2 . VAL C 1 94  ? 114.140 221.220 23.423  1.00 40.36  ? 94  VAL C CG2 1 
ATOM   3530 N  N   . ALA C 1 95  ? 117.503 223.412 21.299  1.00 48.07  ? 95  ALA C N   1 
ATOM   3531 C  CA  . ALA C 1 95  ? 118.133 224.039 20.149  1.00 43.76  ? 95  ALA C CA  1 
ATOM   3532 C  C   . ALA C 1 95  ? 117.786 223.218 18.933  1.00 42.49  ? 95  ALA C C   1 
ATOM   3533 O  O   . ALA C 1 95  ? 118.149 222.037 18.826  1.00 46.38  ? 95  ALA C O   1 
ATOM   3534 C  CB  . ALA C 1 95  ? 119.635 224.147 20.332  1.00 38.92  ? 95  ALA C CB  1 
ATOM   3535 N  N   . ASP C 1 96  ? 117.032 223.828 18.037  1.00 48.94  ? 96  ASP C N   1 
ATOM   3536 C  CA  . ASP C 1 96  ? 116.706 223.182 16.786  1.00 41.87  ? 96  ASP C CA  1 
ATOM   3537 C  C   . ASP C 1 96  ? 117.750 223.667 15.761  1.00 50.72  ? 96  ASP C C   1 
ATOM   3538 O  O   . ASP C 1 96  ? 117.788 224.836 15.383  1.00 52.53  ? 96  ASP C O   1 
ATOM   3539 C  CB  . ASP C 1 96  ? 115.255 223.511 16.401  1.00 52.79  ? 96  ASP C CB  1 
ATOM   3540 C  CG  . ASP C 1 96  ? 114.224 222.912 17.413  1.00 73.79  ? 96  ASP C CG  1 
ATOM   3541 O  OD1 . ASP C 1 96  ? 114.107 221.664 17.497  1.00 67.70  ? 96  ASP C OD1 1 
ATOM   3542 O  OD2 . ASP C 1 96  ? 113.536 223.685 18.137  1.00 75.62  1 96  ASP C OD2 1 
ATOM   3543 N  N   . VAL C 1 97  ? 118.624 222.767 15.342  1.00 41.26  ? 97  VAL C N   1 
ATOM   3544 C  CA  . VAL C 1 97  ? 119.788 223.139 14.539  1.00 41.49  ? 97  VAL C CA  1 
ATOM   3545 C  C   . VAL C 1 97  ? 119.531 223.026 13.049  1.00 40.03  ? 97  VAL C C   1 
ATOM   3546 O  O   . VAL C 1 97  ? 119.204 221.952 12.563  1.00 40.28  ? 97  VAL C O   1 
ATOM   3547 C  CB  . VAL C 1 97  ? 121.007 222.256 14.917  1.00 43.84  ? 97  VAL C CB  1 
ATOM   3548 C  CG1 . VAL C 1 97  ? 122.171 222.432 13.957  1.00 43.07  ? 97  VAL C CG1 1 
ATOM   3549 C  CG2 . VAL C 1 97  ? 121.426 222.532 16.349  1.00 36.62  ? 97  VAL C CG2 1 
ATOM   3550 N  N   . SER C 1 98  ? 119.695 224.139 12.328  1.00 44.28  ? 98  SER C N   1 
ATOM   3551 C  CA  . SER C 1 98  ? 119.578 224.145 10.868  1.00 42.34  ? 98  SER C CA  1 
ATOM   3552 C  C   . SER C 1 98  ? 120.668 225.041 10.252  1.00 53.55  ? 98  SER C C   1 
ATOM   3553 O  O   . SER C 1 98  ? 120.580 226.281 10.262  1.00 47.33  ? 98  SER C O   1 
ATOM   3554 C  CB  . SER C 1 98  ? 118.183 224.619 10.430  1.00 46.41  ? 98  SER C CB  1 
ATOM   3555 O  OG  . SER C 1 98  ? 117.799 224.066 9.172   1.00 53.42  ? 98  SER C OG  1 
ATOM   3556 N  N   . ILE C 1 99  ? 121.671 224.386 9.676   1.00 43.37  ? 99  ILE C N   1 
ATOM   3557 C  CA  . ILE C 1 99  ? 122.877 225.046 9.205   1.00 43.01  ? 99  ILE C CA  1 
ATOM   3558 C  C   . ILE C 1 99  ? 123.237 224.589 7.785   1.00 41.19  ? 99  ILE C C   1 
ATOM   3559 O  O   . ILE C 1 99  ? 123.113 223.409 7.431   1.00 39.54  ? 99  ILE C O   1 
ATOM   3560 C  CB  . ILE C 1 99  ? 124.057 224.766 10.180  1.00 39.09  ? 99  ILE C CB  1 
ATOM   3561 C  CG1 . ILE C 1 99  ? 123.832 225.524 11.481  1.00 47.26  ? 99  ILE C CG1 1 
ATOM   3562 C  CG2 . ILE C 1 99  ? 125.391 225.202 9.611   1.00 28.73  ? 99  ILE C CG2 1 
ATOM   3563 C  CD1 . ILE C 1 99  ? 124.830 225.175 12.571  1.00 43.98  ? 99  ILE C CD1 1 
ATOM   3564 N  N   . GLU C 1 100 ? 123.662 225.537 6.965   1.00 39.09  ? 100 GLU C N   1 
ATOM   3565 C  CA  . GLU C 1 100 ? 124.330 225.206 5.715   1.00 45.05  ? 100 GLU C CA  1 
ATOM   3566 C  C   . GLU C 1 100 ? 125.738 225.751 5.797   1.00 38.04  ? 100 GLU C C   1 
ATOM   3567 O  O   . GLU C 1 100 ? 125.935 226.899 6.212   1.00 40.40  ? 100 GLU C O   1 
ATOM   3568 C  CB  . GLU C 1 100 ? 123.586 225.778 4.514   1.00 38.96  ? 100 GLU C CB  1 
ATOM   3569 C  CG  . GLU C 1 100 ? 122.607 224.796 3.899   1.00 56.93  ? 100 GLU C CG  1 
ATOM   3570 C  CD  . GLU C 1 100 ? 122.215 225.165 2.479   1.00 76.13  ? 100 GLU C CD  1 
ATOM   3571 O  OE1 . GLU C 1 100 ? 122.045 226.374 2.199   1.00 81.18  ? 100 GLU C OE1 1 
ATOM   3572 O  OE2 . GLU C 1 100 ? 122.073 224.241 1.647   1.00 80.13  1 100 GLU C OE2 1 
ATOM   3573 N  N   . ASP C 1 101 ? 126.720 224.917 5.480   1.00 34.63  ? 101 ASP C N   1 
ATOM   3574 C  CA  . ASP C 1 101 ? 128.111 225.384 5.505   1.00 38.81  ? 101 ASP C CA  1 
ATOM   3575 C  C   . ASP C 1 101 ? 128.861 224.927 4.256   1.00 36.84  ? 101 ASP C C   1 
ATOM   3576 O  O   . ASP C 1 101 ? 128.673 223.812 3.771   1.00 32.20  ? 101 ASP C O   1 
ATOM   3577 C  CB  . ASP C 1 101 ? 128.851 224.916 6.767   1.00 32.04  ? 101 ASP C CB  1 
ATOM   3578 C  CG  . ASP C 1 101 ? 130.120 225.745 7.046   1.00 43.50  ? 101 ASP C CG  1 
ATOM   3579 O  OD1 . ASP C 1 101 ? 129.974 226.934 7.417   1.00 40.31  ? 101 ASP C OD1 1 
ATOM   3580 O  OD2 . ASP C 1 101 ? 131.255 225.218 6.900   1.00 40.47  1 101 ASP C OD2 1 
ATOM   3581 N  N   . SER C 1 102 ? 129.684 225.817 3.723   1.00 30.35  ? 102 SER C N   1 
ATOM   3582 C  CA  . SER C 1 102 ? 130.386 225.540 2.480   1.00 37.40  ? 102 SER C CA  1 
ATOM   3583 C  C   . SER C 1 102 ? 131.807 225.049 2.719   1.00 36.03  ? 102 SER C C   1 
ATOM   3584 O  O   . SER C 1 102 ? 132.477 224.638 1.786   1.00 33.38  ? 102 SER C O   1 
ATOM   3585 C  CB  . SER C 1 102 ? 130.413 226.790 1.596   1.00 42.48  ? 102 SER C CB  1 
ATOM   3586 O  OG  . SER C 1 102 ? 131.229 227.804 2.158   1.00 53.17  ? 102 SER C OG  1 
ATOM   3587 N  N   . VAL C 1 103 ? 132.255 225.082 3.974   1.00 32.87  ? 103 VAL C N   1 
ATOM   3588 C  CA  . VAL C 1 103 ? 133.666 224.852 4.282   1.00 30.06  ? 103 VAL C CA  1 
ATOM   3589 C  C   . VAL C 1 103 ? 133.948 223.415 4.732   1.00 28.01  ? 103 VAL C C   1 
ATOM   3590 O  O   . VAL C 1 103 ? 134.959 222.816 4.370   1.00 26.85  ? 103 VAL C O   1 
ATOM   3591 C  CB  . VAL C 1 103 ? 134.143 225.833 5.368   1.00 32.31  ? 103 VAL C CB  1 
ATOM   3592 C  CG1 . VAL C 1 103 ? 135.600 225.716 5.560   1.00 35.55  ? 103 VAL C CG1 1 
ATOM   3593 C  CG2 . VAL C 1 103 ? 133.752 227.262 5.017   1.00 28.66  ? 103 VAL C CG2 1 
ATOM   3594 N  N   . ILE C 1 104 ? 133.063 222.876 5.551   1.00 35.35  ? 104 ILE C N   1 
ATOM   3595 C  CA  . ILE C 1 104 ? 133.170 221.484 5.940   1.00 33.34  ? 104 ILE C CA  1 
ATOM   3596 C  C   . ILE C 1 104 ? 132.803 220.622 4.759   1.00 35.44  ? 104 ILE C C   1 
ATOM   3597 O  O   . ILE C 1 104 ? 132.249 221.107 3.770   1.00 40.19  ? 104 ILE C O   1 
ATOM   3598 C  CB  . ILE C 1 104 ? 132.257 221.135 7.137   1.00 31.76  ? 104 ILE C CB  1 
ATOM   3599 C  CG1 . ILE C 1 104 ? 130.810 221.502 6.845   1.00 35.40  ? 104 ILE C CG1 1 
ATOM   3600 C  CG2 . ILE C 1 104 ? 132.742 221.827 8.398   1.00 30.29  ? 104 ILE C CG2 1 
ATOM   3601 C  CD1 . ILE C 1 104 ? 129.827 220.979 7.902   1.00 34.94  ? 104 ILE C CD1 1 
ATOM   3602 N  N   . SER C 1 105 ? 133.095 219.339 4.877   1.00 29.98  ? 105 SER C N   1 
ATOM   3603 C  CA  . SER C 1 105 ? 132.805 218.376 3.835   1.00 36.00  ? 105 SER C CA  1 
ATOM   3604 C  C   . SER C 1 105 ? 132.604 216.972 4.437   1.00 32.84  ? 105 SER C C   1 
ATOM   3605 O  O   . SER C 1 105 ? 133.019 216.721 5.558   1.00 31.02  ? 105 SER C O   1 
ATOM   3606 C  CB  . SER C 1 105 ? 133.948 218.375 2.812   1.00 36.38  ? 105 SER C CB  1 
ATOM   3607 O  OG  . SER C 1 105 ? 133.808 217.298 1.899   1.00 43.69  ? 105 SER C OG  1 
ATOM   3608 N  N   . LEU C 1 106 ? 132.002 216.046 3.688   1.00 37.03  ? 106 LEU C N   1 
ATOM   3609 C  CA  . LEU C 1 106 ? 131.895 214.662 4.163   1.00 33.75  ? 106 LEU C CA  1 
ATOM   3610 C  C   . LEU C 1 106 ? 132.893 213.762 3.451   1.00 39.42  ? 106 LEU C C   1 
ATOM   3611 O  O   . LEU C 1 106 ? 132.795 212.539 3.496   1.00 39.64  ? 106 LEU C O   1 
ATOM   3612 C  CB  . LEU C 1 106 ? 130.484 214.132 3.965   1.00 37.71  ? 106 LEU C CB  1 
ATOM   3613 C  CG  . LEU C 1 106 ? 129.391 214.817 4.796   1.00 35.14  ? 106 LEU C CG  1 
ATOM   3614 C  CD1 . LEU C 1 106 ? 128.089 214.000 4.693   1.00 31.24  ? 106 LEU C CD1 1 
ATOM   3615 C  CD2 . LEU C 1 106 ? 129.841 214.953 6.261   1.00 29.61  ? 106 LEU C CD2 1 
ATOM   3616 N  N   . SER C 1 107 ? 133.862 214.403 2.804   1.00 37.43  ? 107 SER C N   1 
ATOM   3617 C  CA  . SER C 1 107 ? 134.949 213.739 2.089   1.00 40.47  ? 107 SER C CA  1 
ATOM   3618 C  C   . SER C 1 107 ? 136.055 214.751 1.857   1.00 41.78  ? 107 SER C C   1 
ATOM   3619 O  O   . SER C 1 107 ? 135.814 215.964 1.926   1.00 42.21  ? 107 SER C O   1 
ATOM   3620 C  CB  . SER C 1 107 ? 134.470 213.186 0.737   1.00 43.26  ? 107 SER C CB  1 
ATOM   3621 O  OG  . SER C 1 107 ? 133.862 214.222 -0.034  1.00 52.28  ? 107 SER C OG  1 
ATOM   3622 N  N   . GLY C 1 108 ? 137.253 214.260 1.558   1.00 43.67  ? 108 GLY C N   1 
ATOM   3623 C  CA  . GLY C 1 108 ? 138.365 215.123 1.184   1.00 41.48  ? 108 GLY C CA  1 
ATOM   3624 C  C   . GLY C 1 108 ? 139.116 215.777 2.332   1.00 41.97  ? 108 GLY C C   1 
ATOM   3625 O  O   . GLY C 1 108 ? 139.056 215.322 3.459   1.00 42.50  ? 108 GLY C O   1 
ATOM   3626 N  N   . ASP C 1 109 ? 139.839 216.843 2.025   1.00 44.12  ? 109 ASP C N   1 
ATOM   3627 C  CA  . ASP C 1 109 ? 140.744 217.468 2.981   1.00 42.12  ? 109 ASP C CA  1 
ATOM   3628 C  C   . ASP C 1 109 ? 140.006 218.111 4.158   1.00 42.79  ? 109 ASP C C   1 
ATOM   3629 O  O   . ASP C 1 109 ? 140.588 218.322 5.205   1.00 36.34  ? 109 ASP C O   1 
ATOM   3630 C  CB  . ASP C 1 109 ? 141.612 218.512 2.264   1.00 38.71  ? 109 ASP C CB  1 
ATOM   3631 C  CG  . ASP C 1 109 ? 142.751 217.878 1.473   1.00 61.20  ? 109 ASP C CG  1 
ATOM   3632 O  OD1 . ASP C 1 109 ? 143.087 216.707 1.759   1.00 55.40  ? 109 ASP C OD1 1 
ATOM   3633 O  OD2 . ASP C 1 109 ? 143.291 218.536 0.547   1.00 72.44  1 109 ASP C OD2 1 
ATOM   3634 N  N   . HIS C 1 110 ? 138.746 218.471 3.937   1.00 33.58  ? 110 HIS C N   1 
ATOM   3635 C  CA  . HIS C 1 110 ? 137.894 219.091 4.932   1.00 33.94  ? 110 HIS C CA  1 
ATOM   3636 C  C   . HIS C 1 110 ? 136.880 218.124 5.493   1.00 34.34  ? 110 HIS C C   1 
ATOM   3637 O  O   . HIS C 1 110 ? 135.862 218.555 6.045   1.00 28.72  ? 110 HIS C O   1 
ATOM   3638 C  CB  . HIS C 1 110 ? 137.181 220.305 4.335   1.00 30.41  ? 110 HIS C CB  1 
ATOM   3639 C  CG  . HIS C 1 110 ? 138.116 221.406 3.965   1.00 37.29  ? 110 HIS C CG  1 
ATOM   3640 N  ND1 . HIS C 1 110 ? 137.690 222.687 3.682   1.00 43.54  ? 110 HIS C ND1 1 
ATOM   3641 C  CD2 . HIS C 1 110 ? 139.470 221.434 3.908   1.00 36.65  ? 110 HIS C CD2 1 
ATOM   3642 C  CE1 . HIS C 1 110 ? 138.742 223.443 3.415   1.00 42.00  ? 110 HIS C CE1 1 
ATOM   3643 N  NE2 . HIS C 1 110 ? 139.833 222.708 3.550   1.00 39.11  ? 110 HIS C NE2 1 
ATOM   3644 N  N   . CYS C 1 111 ? 137.136 216.827 5.312   1.00 35.92  ? 111 CYS C N   1 
ATOM   3645 C  CA  . CYS C 1 111 ? 136.225 215.781 5.772   1.00 32.87  ? 111 CYS C CA  1 
ATOM   3646 C  C   . CYS C 1 111 ? 136.105 215.823 7.309   1.00 32.33  ? 111 CYS C C   1 
ATOM   3647 O  O   . CYS C 1 111 ? 137.108 215.843 8.033   1.00 31.65  ? 111 CYS C O   1 
ATOM   3648 C  CB  . CYS C 1 111 ? 136.717 214.408 5.291   1.00 27.34  ? 111 CYS C CB  1 
ATOM   3649 S  SG  . CYS C 1 111 ? 135.803 212.950 5.940   1.00 39.93  ? 111 CYS C SG  1 
ATOM   3650 N  N   . ILE C 1 112 ? 134.883 215.913 7.803   1.00 30.65  ? 112 ILE C N   1 
ATOM   3651 C  CA  . ILE C 1 112 ? 134.670 215.978 9.250   1.00 32.98  ? 112 ILE C CA  1 
ATOM   3652 C  C   . ILE C 1 112 ? 134.292 214.616 9.855   1.00 34.05  ? 112 ILE C C   1 
ATOM   3653 O  O   . ILE C 1 112 ? 134.165 214.499 11.062  1.00 34.04  ? 112 ILE C O   1 
ATOM   3654 C  CB  . ILE C 1 112 ? 133.583 216.994 9.620   1.00 27.21  ? 112 ILE C CB  1 
ATOM   3655 C  CG1 . ILE C 1 112 ? 132.250 216.626 8.959   1.00 27.54  ? 112 ILE C CG1 1 
ATOM   3656 C  CG2 . ILE C 1 112 ? 134.009 218.432 9.259   1.00 25.54  ? 112 ILE C CG2 1 
ATOM   3657 C  CD1 . ILE C 1 112 ? 131.125 217.514 9.380   1.00 28.54  ? 112 ILE C CD1 1 
ATOM   3658 N  N   . ILE C 1 113 ? 134.124 213.589 9.021   1.00 33.21  ? 113 ILE C N   1 
ATOM   3659 C  CA  . ILE C 1 113 ? 133.772 212.279 9.544   1.00 27.94  ? 113 ILE C CA  1 
ATOM   3660 C  C   . ILE C 1 113 ? 134.912 211.772 10.421  1.00 31.82  ? 113 ILE C C   1 
ATOM   3661 O  O   . ILE C 1 113 ? 136.094 211.903 10.082  1.00 36.67  ? 113 ILE C O   1 
ATOM   3662 C  CB  . ILE C 1 113 ? 133.450 211.250 8.409   1.00 36.10  ? 113 ILE C CB  1 
ATOM   3663 C  CG1 . ILE C 1 113 ? 132.120 211.599 7.734   1.00 33.48  ? 113 ILE C CG1 1 
ATOM   3664 C  CG2 . ILE C 1 113 ? 133.283 209.842 8.948   1.00 30.60  ? 113 ILE C CG2 1 
ATOM   3665 C  CD1 . ILE C 1 113 ? 131.898 210.877 6.395   1.00 32.60  ? 113 ILE C CD1 1 
ATOM   3666 N  N   . GLY C 1 114 ? 134.542 211.209 11.564  1.00 28.88  ? 114 GLY C N   1 
ATOM   3667 C  CA  . GLY C 1 114 ? 135.501 210.662 12.493  1.00 35.90  ? 114 GLY C CA  1 
ATOM   3668 C  C   . GLY C 1 114 ? 136.059 211.727 13.410  1.00 33.74  ? 114 GLY C C   1 
ATOM   3669 O  O   . GLY C 1 114 ? 137.041 211.490 14.105  1.00 33.39  ? 114 GLY C O   1 
ATOM   3670 N  N   . ARG C 1 115 ? 135.433 212.900 13.419  1.00 26.39  ? 115 ARG C N   1 
ATOM   3671 C  CA  . ARG C 1 115 ? 135.908 213.974 14.270  1.00 30.72  ? 115 ARG C CA  1 
ATOM   3672 C  C   . ARG C 1 115 ? 134.814 214.273 15.280  1.00 32.15  ? 115 ARG C C   1 
ATOM   3673 O  O   . ARG C 1 115 ? 133.643 214.004 15.031  1.00 34.39  ? 115 ARG C O   1 
ATOM   3674 C  CB  . ARG C 1 115 ? 136.283 215.236 13.444  1.00 27.59  ? 115 ARG C CB  1 
ATOM   3675 C  CG  . ARG C 1 115 ? 137.423 215.021 12.423  1.00 36.90  ? 115 ARG C CG  1 
ATOM   3676 C  CD  . ARG C 1 115 ? 137.868 216.323 11.722  1.00 30.81  ? 115 ARG C CD  1 
ATOM   3677 N  NE  . ARG C 1 115 ? 138.383 216.075 10.381  1.00 29.90  ? 115 ARG C NE  1 
ATOM   3678 C  CZ  . ARG C 1 115 ? 139.619 215.668 10.087  1.00 36.52  ? 115 ARG C CZ  1 
ATOM   3679 N  NH1 . ARG C 1 115 ? 140.510 215.490 11.041  1.00 28.92  1 115 ARG C NH1 1 
ATOM   3680 N  NH2 . ARG C 1 115 ? 139.984 215.473 8.814   1.00 32.13  ? 115 ARG C NH2 1 
ATOM   3681 N  N   . THR C 1 116 ? 135.192 214.850 16.407  1.00 27.62  ? 116 THR C N   1 
ATOM   3682 C  CA  . THR C 1 116 ? 134.234 215.148 17.453  1.00 28.89  ? 116 THR C CA  1 
ATOM   3683 C  C   . THR C 1 116 ? 133.477 216.412 17.205  1.00 27.14  ? 116 THR C C   1 
ATOM   3684 O  O   . THR C 1 116 ? 134.069 217.442 16.928  1.00 31.33  ? 116 THR C O   1 
ATOM   3685 C  CB  . THR C 1 116 ? 134.903 215.269 18.826  1.00 32.36  ? 116 THR C CB  1 
ATOM   3686 O  OG1 . THR C 1 116 ? 135.492 214.010 19.159  1.00 32.87  ? 116 THR C OG1 1 
ATOM   3687 C  CG2 . THR C 1 116 ? 133.880 215.618 19.867  1.00 28.36  ? 116 THR C CG2 1 
ATOM   3688 N  N   . LEU C 1 117 ? 132.154 216.313 17.298  1.00 26.95  ? 117 LEU C N   1 
ATOM   3689 C  CA  . LEU C 1 117 ? 131.292 217.475 17.318  1.00 28.74  ? 117 LEU C CA  1 
ATOM   3690 C  C   . LEU C 1 117 ? 131.011 217.887 18.771  1.00 35.62  ? 117 LEU C C   1 
ATOM   3691 O  O   . LEU C 1 117 ? 130.748 217.035 19.619  1.00 35.84  ? 117 LEU C O   1 
ATOM   3692 C  CB  . LEU C 1 117 ? 129.995 217.172 16.571  1.00 29.79  ? 117 LEU C CB  1 
ATOM   3693 C  CG  . LEU C 1 117 ? 128.965 218.284 16.503  1.00 33.84  ? 117 LEU C CG  1 
ATOM   3694 C  CD1 . LEU C 1 117 ? 129.515 219.416 15.645  1.00 24.84  ? 117 LEU C CD1 1 
ATOM   3695 C  CD2 . LEU C 1 117 ? 127.640 217.752 15.964  1.00 32.79  ? 117 LEU C CD2 1 
ATOM   3696 N  N   . VAL C 1 118 ? 131.098 219.177 19.066  1.00 26.07  ? 118 VAL C N   1 
ATOM   3697 C  CA  . VAL C 1 118 ? 130.901 219.657 20.434  1.00 28.88  ? 118 VAL C CA  1 
ATOM   3698 C  C   . VAL C 1 118 ? 129.925 220.831 20.502  1.00 33.16  ? 118 VAL C C   1 
ATOM   3699 O  O   . VAL C 1 118 ? 129.896 221.696 19.615  1.00 36.51  ? 118 VAL C O   1 
ATOM   3700 C  CB  . VAL C 1 118 ? 132.234 220.098 21.090  1.00 31.89  ? 118 VAL C CB  1 
ATOM   3701 C  CG1 . VAL C 1 118 ? 132.019 220.443 22.556  1.00 35.57  ? 118 VAL C CG1 1 
ATOM   3702 C  CG2 . VAL C 1 118 ? 133.247 218.996 20.999  1.00 30.06  ? 118 VAL C CG2 1 
ATOM   3703 N  N   . VAL C 1 119 ? 129.097 220.833 21.539  1.00 28.71  ? 119 VAL C N   1 
ATOM   3704 C  CA  . VAL C 1 119 ? 128.241 221.969 21.854  1.00 29.63  ? 119 VAL C CA  1 
ATOM   3705 C  C   . VAL C 1 119 ? 128.646 222.418 23.262  1.00 35.85  ? 119 VAL C C   1 
ATOM   3706 O  O   . VAL C 1 119 ? 128.906 221.580 24.128  1.00 30.64  ? 119 VAL C O   1 
ATOM   3707 C  CB  . VAL C 1 119 ? 126.722 221.621 21.758  1.00 30.18  ? 119 VAL C CB  1 
ATOM   3708 C  CG1 . VAL C 1 119 ? 126.346 220.393 22.607  1.00 30.30  ? 119 VAL C CG1 1 
ATOM   3709 C  CG2 . VAL C 1 119 ? 125.868 222.818 22.128  1.00 37.43  ? 119 VAL C CG2 1 
ATOM   3710 N  N   . HIS C 1 120 ? 128.776 223.728 23.461  1.00 32.12  ? 120 HIS C N   1 
ATOM   3711 C  CA  . HIS C 1 120 ? 129.383 224.256 24.673  1.00 34.83  ? 120 HIS C CA  1 
ATOM   3712 C  C   . HIS C 1 120 ? 128.337 224.930 25.547  1.00 36.62  ? 120 HIS C C   1 
ATOM   3713 O  O   . HIS C 1 120 ? 127.263 225.295 25.069  1.00 32.68  ? 120 HIS C O   1 
ATOM   3714 C  CB  . HIS C 1 120 ? 130.489 225.259 24.331  1.00 33.56  ? 120 HIS C CB  1 
ATOM   3715 C  CG  . HIS C 1 120 ? 131.762 224.627 23.855  1.00 34.75  ? 120 HIS C CG  1 
ATOM   3716 N  ND1 . HIS C 1 120 ? 132.886 224.529 24.642  1.00 31.95  ? 120 HIS C ND1 1 
ATOM   3717 C  CD2 . HIS C 1 120 ? 132.091 224.078 22.657  1.00 29.53  ? 120 HIS C CD2 1 
ATOM   3718 C  CE1 . HIS C 1 120 ? 133.845 223.925 23.959  1.00 29.35  ? 120 HIS C CE1 1 
ATOM   3719 N  NE2 . HIS C 1 120 ? 133.387 223.648 22.749  1.00 36.58  ? 120 HIS C NE2 1 
ATOM   3720 N  N   . GLU C 1 121 ? 128.693 225.170 26.805  1.00 33.28  ? 121 GLU C N   1 
ATOM   3721 C  CA  . GLU C 1 121 ? 127.782 225.784 27.749  1.00 38.61  ? 121 GLU C CA  1 
ATOM   3722 C  C   . GLU C 1 121 ? 127.426 227.232 27.407  1.00 37.15  ? 121 GLU C C   1 
ATOM   3723 O  O   . GLU C 1 121 ? 126.287 227.658 27.606  1.00 46.63  ? 121 GLU C O   1 
ATOM   3724 C  CB  . GLU C 1 121 ? 128.380 225.732 29.159  1.00 39.68  ? 121 GLU C CB  1 
ATOM   3725 C  CG  . GLU C 1 121 ? 127.511 226.504 30.159  1.00 48.72  ? 121 GLU C CG  1 
ATOM   3726 C  CD  . GLU C 1 121 ? 127.891 226.298 31.623  1.00 61.92  ? 121 GLU C CD  1 
ATOM   3727 O  OE1 . GLU C 1 121 ? 127.137 226.790 32.488  1.00 74.99  ? 121 GLU C OE1 1 
ATOM   3728 O  OE2 . GLU C 1 121 ? 128.905 225.630 31.917  1.00 68.76  1 121 GLU C OE2 1 
ATOM   3729 N  N   . LYS C 1 122 ? 128.400 227.999 26.936  1.00 29.48  ? 122 LYS C N   1 
ATOM   3730 C  CA  . LYS C 1 122 ? 128.177 229.418 26.647  1.00 33.93  ? 122 LYS C CA  1 
ATOM   3731 C  C   . LYS C 1 122 ? 128.383 229.736 25.161  1.00 43.58  ? 122 LYS C C   1 
ATOM   3732 O  O   . LYS C 1 122 ? 128.847 228.890 24.384  1.00 38.12  ? 122 LYS C O   1 
ATOM   3733 C  CB  . LYS C 1 122 ? 129.096 230.286 27.492  1.00 33.31  ? 122 LYS C CB  1 
ATOM   3734 C  CG  . LYS C 1 122 ? 129.170 229.906 28.977  1.00 33.97  ? 122 LYS C CG  1 
ATOM   3735 C  CD  . LYS C 1 122 ? 128.064 230.597 29.807  1.00 45.38  ? 122 LYS C CD  1 
ATOM   3736 C  CE  . LYS C 1 122 ? 128.387 230.489 31.329  1.00 55.99  ? 122 LYS C CE  1 
ATOM   3737 N  NZ  . LYS C 1 122 ? 127.720 231.547 32.185  1.00 58.72  1 122 LYS C NZ  1 
ATOM   3738 N  N   . ALA C 1 123 ? 128.031 230.959 24.778  1.00 35.38  ? 123 ALA C N   1 
ATOM   3739 C  CA  . ALA C 1 123 ? 128.159 231.395 23.407  1.00 33.67  ? 123 ALA C CA  1 
ATOM   3740 C  C   . ALA C 1 123 ? 129.599 231.510 22.906  1.00 36.75  ? 123 ALA C C   1 
ATOM   3741 O  O   . ALA C 1 123 ? 130.505 231.886 23.640  1.00 40.36  ? 123 ALA C O   1 
ATOM   3742 C  CB  . ALA C 1 123 ? 127.446 232.732 23.222  1.00 29.96  ? 123 ALA C CB  1 
ATOM   3743 N  N   . ASP C 1 124 ? 129.773 231.180 21.629  1.00 37.63  ? 124 ASP C N   1 
ATOM   3744 C  CA  . ASP C 1 124 ? 131.000 231.451 20.857  1.00 40.22  ? 124 ASP C CA  1 
ATOM   3745 C  C   . ASP C 1 124 ? 131.082 232.953 20.533  1.00 39.20  ? 124 ASP C C   1 
ATOM   3746 O  O   . ASP C 1 124 ? 130.151 233.509 19.938  1.00 36.89  ? 124 ASP C O   1 
ATOM   3747 C  CB  . ASP C 1 124 ? 130.977 230.590 19.570  1.00 37.98  ? 124 ASP C CB  1 
ATOM   3748 C  CG  . ASP C 1 124 ? 132.281 230.618 18.786  1.00 38.19  ? 124 ASP C CG  1 
ATOM   3749 O  OD1 . ASP C 1 124 ? 132.999 231.638 18.765  1.00 33.09  ? 124 ASP C OD1 1 
ATOM   3750 O  OD2 . ASP C 1 124 ? 132.604 229.562 18.207  1.00 38.44  1 124 ASP C OD2 1 
ATOM   3751 N  N   . ASP C 1 125 ? 132.176 233.617 20.913  1.00 40.88  ? 125 ASP C N   1 
ATOM   3752 C  CA  . ASP C 1 125 ? 132.271 235.069 20.661  1.00 40.47  ? 125 ASP C CA  1 
ATOM   3753 C  C   . ASP C 1 125 ? 132.817 235.377 19.248  1.00 33.18  ? 125 ASP C C   1 
ATOM   3754 O  O   . ASP C 1 125 ? 133.063 236.540 18.891  1.00 36.21  ? 125 ASP C O   1 
ATOM   3755 C  CB  . ASP C 1 125 ? 133.114 235.770 21.759  1.00 33.94  ? 125 ASP C CB  1 
ATOM   3756 C  CG  . ASP C 1 125 ? 134.610 235.431 21.699  1.00 34.26  ? 125 ASP C CG  1 
ATOM   3757 O  OD1 . ASP C 1 125 ? 135.108 235.040 20.626  1.00 37.63  ? 125 ASP C OD1 1 
ATOM   3758 O  OD2 . ASP C 1 125 ? 135.310 235.585 22.731  1.00 47.24  1 125 ASP C OD2 1 
ATOM   3759 N  N   . LEU C 1 126 ? 132.999 234.314 18.470  1.00 33.73  ? 126 LEU C N   1 
ATOM   3760 C  CA  . LEU C 1 126 ? 133.311 234.382 17.034  1.00 35.91  ? 126 LEU C CA  1 
ATOM   3761 C  C   . LEU C 1 126 ? 134.685 234.986 16.753  1.00 38.01  ? 126 LEU C C   1 
ATOM   3762 O  O   . LEU C 1 126 ? 134.907 235.576 15.700  1.00 38.58  ? 126 LEU C O   1 
ATOM   3763 C  CB  . LEU C 1 126 ? 132.231 235.173 16.290  1.00 29.23  ? 126 LEU C CB  1 
ATOM   3764 C  CG  . LEU C 1 126 ? 130.803 234.738 16.647  1.00 35.06  ? 126 LEU C CG  1 
ATOM   3765 C  CD1 . LEU C 1 126 ? 129.783 235.569 15.884  1.00 34.85  ? 126 LEU C CD1 1 
ATOM   3766 C  CD2 . LEU C 1 126 ? 130.611 233.246 16.414  1.00 27.85  ? 126 LEU C CD2 1 
ATOM   3767 N  N   . GLY C 1 127 ? 135.597 234.824 17.709  1.00 33.60  ? 127 GLY C N   1 
ATOM   3768 C  CA  . GLY C 1 127 ? 136.972 235.216 17.530  1.00 33.15  ? 127 GLY C CA  1 
ATOM   3769 C  C   . GLY C 1 127 ? 137.245 236.704 17.531  1.00 38.39  ? 127 GLY C C   1 
ATOM   3770 O  O   . GLY C 1 127 ? 138.342 237.120 17.177  1.00 36.26  ? 127 GLY C O   1 
ATOM   3771 N  N   . LYS C 1 128 ? 136.264 237.513 17.913  1.00 36.53  ? 128 LYS C N   1 
ATOM   3772 C  CA  . LYS C 1 128 ? 136.447 238.959 17.828  1.00 39.63  ? 128 LYS C CA  1 
ATOM   3773 C  C   . LYS C 1 128 ? 136.929 239.627 19.121  1.00 44.73  ? 128 LYS C C   1 
ATOM   3774 O  O   . LYS C 1 128 ? 137.154 240.829 19.138  1.00 53.32  ? 128 LYS C O   1 
ATOM   3775 C  CB  . LYS C 1 128 ? 135.121 239.603 17.403  1.00 44.49  ? 128 LYS C CB  1 
ATOM   3776 C  CG  . LYS C 1 128 ? 134.709 239.318 15.967  1.00 42.20  ? 128 LYS C CG  1 
ATOM   3777 C  CD  . LYS C 1 128 ? 133.348 239.913 15.660  1.00 58.33  ? 128 LYS C CD  1 
ATOM   3778 C  CE  . LYS C 1 128 ? 132.908 239.554 14.251  1.00 68.89  ? 128 LYS C CE  1 
ATOM   3779 N  NZ  . LYS C 1 128 ? 132.464 238.126 14.147  1.00 66.14  1 128 LYS C NZ  1 
ATOM   3780 N  N   . GLY C 1 129 ? 137.179 238.851 20.173  1.00 51.71  ? 129 GLY C N   1 
ATOM   3781 C  CA  . GLY C 1 129 ? 137.604 239.427 21.436  1.00 42.43  ? 129 GLY C CA  1 
ATOM   3782 C  C   . GLY C 1 129 ? 139.079 239.748 21.514  1.00 44.35  ? 129 GLY C C   1 
ATOM   3783 O  O   . GLY C 1 129 ? 139.892 239.143 20.832  1.00 43.93  ? 129 GLY C O   1 
ATOM   3784 N  N   . GLY C 1 130 ? 139.424 240.655 22.414  1.00 39.50  ? 130 GLY C N   1 
ATOM   3785 C  CA  . GLY C 1 130 ? 140.784 241.131 22.580  1.00 38.24  ? 130 GLY C CA  1 
ATOM   3786 C  C   . GLY C 1 130 ? 141.632 240.306 23.541  1.00 44.18  ? 130 GLY C C   1 
ATOM   3787 O  O   . GLY C 1 130 ? 142.231 240.834 24.484  1.00 45.04  ? 130 GLY C O   1 
ATOM   3788 N  N   . ASN C 1 131 ? 141.633 238.991 23.322  1.00 38.32  ? 131 ASN C N   1 
ATOM   3789 C  CA  . ASN C 1 131 ? 142.484 238.054 24.046  1.00 39.80  ? 131 ASN C CA  1 
ATOM   3790 C  C   . ASN C 1 131 ? 142.810 236.881 23.133  1.00 31.53  ? 131 ASN C C   1 
ATOM   3791 O  O   . ASN C 1 131 ? 142.088 236.621 22.175  1.00 35.49  ? 131 ASN C O   1 
ATOM   3792 C  CB  . ASN C 1 131 ? 141.795 237.559 25.327  1.00 32.56  ? 131 ASN C CB  1 
ATOM   3793 C  CG  . ASN C 1 131 ? 140.374 237.097 25.071  1.00 33.23  ? 131 ASN C CG  1 
ATOM   3794 O  OD1 . ASN C 1 131 ? 140.134 235.939 24.733  1.00 33.18  ? 131 ASN C OD1 1 
ATOM   3795 N  ND2 . ASN C 1 131 ? 139.422 238.013 25.216  1.00 34.68  ? 131 ASN C ND2 1 
ATOM   3796 N  N   . GLU C 1 132 ? 143.854 236.132 23.442  1.00 31.00  ? 132 GLU C N   1 
ATOM   3797 C  CA  . GLU C 1 132 ? 144.212 235.049 22.554  1.00 37.45  ? 132 GLU C CA  1 
ATOM   3798 C  C   . GLU C 1 132 ? 143.132 233.952 22.558  1.00 39.72  ? 132 GLU C C   1 
ATOM   3799 O  O   . GLU C 1 132 ? 142.896 233.303 21.538  1.00 36.62  ? 132 GLU C O   1 
ATOM   3800 C  CB  . GLU C 1 132 ? 145.563 234.446 22.910  1.00 38.87  ? 132 GLU C CB  1 
ATOM   3801 C  CG  . GLU C 1 132 ? 146.018 233.460 21.822  1.00 38.11  ? 132 GLU C CG  1 
ATOM   3802 C  CD  . GLU C 1 132 ? 147.361 232.858 22.105  1.00 48.24  ? 132 GLU C CD  1 
ATOM   3803 O  OE1 . GLU C 1 132 ? 148.205 232.796 21.188  1.00 63.18  ? 132 GLU C OE1 1 
ATOM   3804 O  OE2 . GLU C 1 132 ? 147.580 232.449 23.261  1.00 59.63  1 132 GLU C OE2 1 
ATOM   3805 N  N   . GLU C 1 133 ? 142.462 233.764 23.690  1.00 37.81  ? 133 GLU C N   1 
ATOM   3806 C  CA  . GLU C 1 133 ? 141.475 232.692 23.802  1.00 39.70  ? 133 GLU C CA  1 
ATOM   3807 C  C   . GLU C 1 133 ? 140.325 232.832 22.805  1.00 30.29  ? 133 GLU C C   1 
ATOM   3808 O  O   . GLU C 1 133 ? 139.803 231.836 22.287  1.00 26.41  ? 133 GLU C O   1 
ATOM   3809 C  CB  . GLU C 1 133 ? 140.896 232.639 25.217  1.00 22.48  ? 133 GLU C CB  1 
ATOM   3810 C  CG  . GLU C 1 133 ? 140.131 231.359 25.482  1.00 41.51  ? 133 GLU C CG  1 
ATOM   3811 C  CD  . GLU C 1 133 ? 140.975 230.091 25.391  1.00 44.80  ? 133 GLU C CD  1 
ATOM   3812 O  OE1 . GLU C 1 133 ? 142.159 230.085 25.795  1.00 45.74  ? 133 GLU C OE1 1 
ATOM   3813 O  OE2 . GLU C 1 133 ? 140.450 229.100 24.845  1.00 60.02  1 133 GLU C OE2 1 
ATOM   3814 N  N   . SER C 1 134 ? 139.940 234.071 22.551  1.00 28.25  ? 134 SER C N   1 
ATOM   3815 C  CA  . SER C 1 134 ? 138.929 234.362 21.554  1.00 29.23  ? 134 SER C CA  1 
ATOM   3816 C  C   . SER C 1 134 ? 139.386 233.808 20.211  1.00 34.35  ? 134 SER C C   1 
ATOM   3817 O  O   . SER C 1 134 ? 138.607 233.225 19.483  1.00 34.24  ? 134 SER C O   1 
ATOM   3818 C  CB  . SER C 1 134 ? 138.679 235.859 21.472  1.00 32.02  ? 134 SER C CB  1 
ATOM   3819 O  OG  . SER C 1 134 ? 137.787 236.165 20.435  1.00 36.54  ? 134 SER C OG  1 
ATOM   3820 N  N   . THR C 1 135 ? 140.676 233.933 19.918  1.00 32.56  ? 135 THR C N   1 
ATOM   3821 C  CA  . THR C 1 135 ? 141.150 233.552 18.606  1.00 31.12  ? 135 THR C CA  1 
ATOM   3822 C  C   . THR C 1 135 ? 141.438 232.067 18.521  1.00 36.67  ? 135 THR C C   1 
ATOM   3823 O  O   . THR C 1 135 ? 141.749 231.561 17.446  1.00 34.53  ? 135 THR C O   1 
ATOM   3824 C  CB  . THR C 1 135 ? 142.403 234.337 18.211  1.00 31.13  ? 135 THR C CB  1 
ATOM   3825 O  OG1 . THR C 1 135 ? 143.567 233.766 18.823  1.00 31.04  ? 135 THR C OG1 1 
ATOM   3826 C  CG2 . THR C 1 135 ? 142.262 235.805 18.600  1.00 31.32  ? 135 THR C CG2 1 
ATOM   3827 N  N   . LYS C 1 136 ? 141.252 231.357 19.629  1.00 32.20  ? 136 LYS C N   1 
ATOM   3828 C  CA  . LYS C 1 136 ? 141.469 229.918 19.626  1.00 37.03  ? 136 LYS C CA  1 
ATOM   3829 C  C   . LYS C 1 136 ? 140.168 229.128 19.724  1.00 36.18  ? 136 LYS C C   1 
ATOM   3830 O  O   . LYS C 1 136 ? 139.946 228.208 18.918  1.00 33.45  ? 136 LYS C O   1 
ATOM   3831 C  CB  . LYS C 1 136 ? 142.391 229.518 20.759  1.00 33.68  ? 136 LYS C CB  1 
ATOM   3832 C  CG  . LYS C 1 136 ? 143.830 229.801 20.474  1.00 34.13  ? 136 LYS C CG  1 
ATOM   3833 C  CD  . LYS C 1 136 ? 144.590 229.911 21.793  1.00 53.36  ? 136 LYS C CD  1 
ATOM   3834 C  CE  . LYS C 1 136 ? 144.295 228.732 22.720  1.00 49.41  ? 136 LYS C CE  1 
ATOM   3835 N  NZ  . LYS C 1 136 ? 145.430 228.496 23.650  1.00 67.23  1 136 LYS C NZ  1 
ATOM   3836 N  N   . THR C 1 137 ? 139.304 229.514 20.669  1.00 26.71  ? 137 THR C N   1 
ATOM   3837 C  CA  . THR C 1 137 ? 138.065 228.780 20.929  1.00 29.98  ? 137 THR C CA  1 
ATOM   3838 C  C   . THR C 1 137 ? 136.814 229.613 20.982  1.00 29.89  ? 137 THR C C   1 
ATOM   3839 O  O   . THR C 1 137 ? 135.713 229.074 21.100  1.00 34.50  ? 137 THR C O   1 
ATOM   3840 C  CB  . THR C 1 137 ? 138.133 228.031 22.253  1.00 29.87  ? 137 THR C CB  1 
ATOM   3841 O  OG1 . THR C 1 137 ? 137.954 228.964 23.328  1.00 40.97  ? 137 THR C OG1 1 
ATOM   3842 C  CG2 . THR C 1 137 ? 139.488 227.323 22.377  1.00 26.23  ? 137 THR C CG2 1 
ATOM   3843 N  N   . GLY C 1 138 ? 136.954 230.925 20.911  1.00 28.88  ? 138 GLY C N   1 
ATOM   3844 C  CA  . GLY C 1 138 ? 135.777 231.763 21.001  1.00 27.65  ? 138 GLY C CA  1 
ATOM   3845 C  C   . GLY C 1 138 ? 135.171 231.864 22.400  1.00 37.24  ? 138 GLY C C   1 
ATOM   3846 O  O   . GLY C 1 138 ? 134.057 232.366 22.528  1.00 36.32  ? 138 GLY C O   1 
ATOM   3847 N  N   . ASN C 1 139 ? 135.886 231.389 23.429  1.00 31.09  ? 139 ASN C N   1 
ATOM   3848 C  CA  . ASN C 1 139 ? 135.481 231.560 24.829  1.00 34.66  ? 139 ASN C CA  1 
ATOM   3849 C  C   . ASN C 1 139 ? 134.114 230.961 25.165  1.00 36.51  ? 139 ASN C C   1 
ATOM   3850 O  O   . ASN C 1 139 ? 133.409 231.469 26.046  1.00 31.57  ? 139 ASN C O   1 
ATOM   3851 C  CB  . ASN C 1 139 ? 135.437 233.054 25.215  1.00 35.74  ? 139 ASN C CB  1 
ATOM   3852 C  CG  . ASN C 1 139 ? 136.808 233.665 25.350  1.00 40.01  ? 139 ASN C CG  1 
ATOM   3853 O  OD1 . ASN C 1 139 ? 137.672 233.103 26.018  1.00 37.58  ? 139 ASN C OD1 1 
ATOM   3854 N  ND2 . ASN C 1 139 ? 137.019 234.828 24.720  1.00 41.38  ? 139 ASN C ND2 1 
ATOM   3855 N  N   . ALA C 1 140 ? 133.793 229.834 24.535  1.00 37.58  ? 140 ALA C N   1 
ATOM   3856 C  CA  . ALA C 1 140 ? 132.465 229.251 24.646  1.00 32.94  ? 140 ALA C CA  1 
ATOM   3857 C  C   . ALA C 1 140 ? 132.331 228.454 25.931  1.00 34.85  ? 140 ALA C C   1 
ATOM   3858 O  O   . ALA C 1 140 ? 131.291 227.845 26.182  1.00 34.01  ? 140 ALA C O   1 
ATOM   3859 C  CB  . ALA C 1 140 ? 132.177 228.358 23.459  1.00 31.17  ? 140 ALA C CB  1 
ATOM   3860 N  N   . GLY C 1 141 ? 133.384 228.445 26.739  1.00 23.97  ? 141 GLY C N   1 
ATOM   3861 C  CA  . GLY C 1 141 ? 133.275 227.796 28.025  1.00 38.16  ? 141 GLY C CA  1 
ATOM   3862 C  C   . GLY C 1 141 ? 133.307 226.292 27.890  1.00 40.26  ? 141 GLY C C   1 
ATOM   3863 O  O   . GLY C 1 141 ? 133.839 225.768 26.911  1.00 37.76  ? 141 GLY C O   1 
ATOM   3864 N  N   . SER C 1 142 ? 132.704 225.593 28.840  1.00 33.14  ? 142 SER C N   1 
ATOM   3865 C  CA  . SER C 1 142 ? 132.912 224.154 28.921  1.00 35.41  ? 142 SER C CA  1 
ATOM   3866 C  C   . SER C 1 142 ? 132.031 223.360 27.961  1.00 31.06  ? 142 SER C C   1 
ATOM   3867 O  O   . SER C 1 142 ? 130.993 223.833 27.506  1.00 40.22  ? 142 SER C O   1 
ATOM   3868 C  CB  . SER C 1 142 ? 132.741 223.699 30.378  1.00 37.65  ? 142 SER C CB  1 
ATOM   3869 O  OG  . SER C 1 142 ? 131.473 224.039 30.882  1.00 50.74  ? 142 SER C OG  1 
ATOM   3870 N  N   . ARG C 1 143 ? 132.491 222.168 27.612  1.00 39.22  ? 143 ARG C N   1 
ATOM   3871 C  CA  . ARG C 1 143 ? 131.778 221.270 26.708  1.00 36.74  ? 143 ARG C CA  1 
ATOM   3872 C  C   . ARG C 1 143 ? 130.612 220.641 27.467  1.00 40.28  ? 143 ARG C C   1 
ATOM   3873 O  O   . ARG C 1 143 ? 130.832 220.043 28.506  1.00 41.68  ? 143 ARG C O   1 
ATOM   3874 C  CB  . ARG C 1 143 ? 132.716 220.175 26.201  1.00 30.22  ? 143 ARG C CB  1 
ATOM   3875 C  CG  . ARG C 1 143 ? 134.012 220.725 25.672  1.00 56.29  ? 143 ARG C CG  1 
ATOM   3876 C  CD  . ARG C 1 143 ? 135.029 219.632 25.465  1.00 56.99  ? 143 ARG C CD  1 
ATOM   3877 N  NE  . ARG C 1 143 ? 136.106 220.006 24.553  1.00 67.63  ? 143 ARG C NE  1 
ATOM   3878 C  CZ  . ARG C 1 143 ? 136.710 219.141 23.745  1.00 69.18  ? 143 ARG C CZ  1 
ATOM   3879 N  NH1 . ARG C 1 143 ? 136.290 217.870 23.713  1.00 54.15  1 143 ARG C NH1 1 
ATOM   3880 N  NH2 . ARG C 1 143 ? 137.716 219.541 22.968  1.00 57.40  ? 143 ARG C NH2 1 
ATOM   3881 N  N   . LEU C 1 144 ? 129.384 220.767 26.971  1.00 38.73  ? 144 LEU C N   1 
ATOM   3882 C  CA  . LEU C 1 144 ? 128.272 220.091 27.640  1.00 41.41  ? 144 LEU C CA  1 
ATOM   3883 C  C   . LEU C 1 144 ? 128.014 218.711 27.061  1.00 40.13  ? 144 LEU C C   1 
ATOM   3884 O  O   . LEU C 1 144 ? 127.626 217.783 27.779  1.00 39.13  ? 144 LEU C O   1 
ATOM   3885 C  CB  . LEU C 1 144 ? 126.995 220.930 27.610  1.00 35.83  ? 144 LEU C CB  1 
ATOM   3886 C  CG  . LEU C 1 144 ? 127.101 222.195 28.473  1.00 38.52  ? 144 LEU C CG  1 
ATOM   3887 C  CD1 . LEU C 1 144 ? 125.765 222.905 28.604  1.00 30.42  ? 144 LEU C CD1 1 
ATOM   3888 C  CD2 . LEU C 1 144 ? 127.703 221.895 29.846  1.00 36.43  ? 144 LEU C CD2 1 
ATOM   3889 N  N   . ALA C 1 145 ? 128.229 218.577 25.763  1.00 38.96  ? 145 ALA C N   1 
ATOM   3890 C  CA  . ALA C 1 145 ? 127.977 217.321 25.092  1.00 43.24  ? 145 ALA C CA  1 
ATOM   3891 C  C   . ALA C 1 145 ? 128.844 217.192 23.858  1.00 43.29  ? 145 ALA C C   1 
ATOM   3892 O  O   . ALA C 1 145 ? 129.157 218.177 23.177  1.00 36.62  ? 145 ALA C O   1 
ATOM   3893 C  CB  . ALA C 1 145 ? 126.481 217.202 24.714  1.00 29.88  ? 145 ALA C CB  1 
ATOM   3894 N  N   . CYS C 1 146 ? 129.196 215.962 23.539  1.00 36.01  ? 146 CYS C N   1 
ATOM   3895 C  CA  . CYS C 1 146 ? 129.998 215.756 22.367  1.00 34.33  ? 146 CYS C CA  1 
ATOM   3896 C  C   . CYS C 1 146 ? 129.696 214.390 21.751  1.00 39.65  ? 146 CYS C C   1 
ATOM   3897 O  O   . CYS C 1 146 ? 129.001 213.560 22.367  1.00 37.20  ? 146 CYS C O   1 
ATOM   3898 C  CB  . CYS C 1 146 ? 131.485 215.917 22.720  1.00 36.50  ? 146 CYS C CB  1 
ATOM   3899 S  SG  . CYS C 1 146 ? 132.202 214.580 23.613  1.00 40.87  ? 146 CYS C SG  1 
ATOM   3900 N  N   . GLY C 1 147 ? 130.143 214.184 20.511  1.00 29.61  ? 147 GLY C N   1 
ATOM   3901 C  CA  . GLY C 1 147 ? 130.016 212.885 19.877  1.00 30.36  ? 147 GLY C CA  1 
ATOM   3902 C  C   . GLY C 1 147 ? 130.937 212.734 18.681  1.00 30.51  ? 147 GLY C C   1 
ATOM   3903 O  O   . GLY C 1 147 ? 131.439 213.716 18.168  1.00 34.08  ? 147 GLY C O   1 
ATOM   3904 N  N   . VAL C 1 148 ? 131.169 211.508 18.234  1.00 31.49  ? 148 VAL C N   1 
ATOM   3905 C  CA  . VAL C 1 148 ? 131.957 211.308 17.028  1.00 30.59  ? 148 VAL C CA  1 
ATOM   3906 C  C   . VAL C 1 148 ? 131.031 211.301 15.824  1.00 32.40  ? 148 VAL C C   1 
ATOM   3907 O  O   . VAL C 1 148 ? 129.998 210.649 15.839  1.00 39.15  ? 148 VAL C O   1 
ATOM   3908 C  CB  . VAL C 1 148 ? 132.750 210.010 17.060  1.00 31.19  ? 148 VAL C CB  1 
ATOM   3909 C  CG1 . VAL C 1 148 ? 133.736 209.953 15.857  1.00 30.15  ? 148 VAL C CG1 1 
ATOM   3910 C  CG2 . VAL C 1 148 ? 133.486 209.881 18.387  1.00 27.59  ? 148 VAL C CG2 1 
ATOM   3911 N  N   . ILE C 1 149 ? 131.406 212.044 14.787  1.00 34.24  ? 149 ILE C N   1 
ATOM   3912 C  CA  . ILE C 1 149 ? 130.648 212.109 13.548  1.00 26.98  ? 149 ILE C CA  1 
ATOM   3913 C  C   . ILE C 1 149 ? 130.862 210.817 12.782  1.00 32.59  ? 149 ILE C C   1 
ATOM   3914 O  O   . ILE C 1 149 ? 132.002 210.469 12.474  1.00 29.34  ? 149 ILE C O   1 
ATOM   3915 C  CB  . ILE C 1 149 ? 131.076 213.329 12.707  1.00 25.69  ? 149 ILE C CB  1 
ATOM   3916 C  CG1 . ILE C 1 149 ? 130.849 214.610 13.503  1.00 29.06  ? 149 ILE C CG1 1 
ATOM   3917 C  CG2 . ILE C 1 149 ? 130.303 213.403 11.406  1.00 26.00  ? 149 ILE C CG2 1 
ATOM   3918 C  CD1 . ILE C 1 149 ? 131.397 215.856 12.809  1.00 32.20  ? 149 ILE C CD1 1 
ATOM   3919 N  N   . GLY C 1 150 ? 129.783 210.082 12.508  1.00 28.73  ? 150 GLY C N   1 
ATOM   3920 C  CA  . GLY C 1 150 ? 129.908 208.809 11.803  1.00 32.95  ? 150 GLY C CA  1 
ATOM   3921 C  C   . GLY C 1 150 ? 129.211 208.709 10.446  1.00 31.57  ? 150 GLY C C   1 
ATOM   3922 O  O   . GLY C 1 150 ? 128.327 209.496 10.127  1.00 32.61  ? 150 GLY C O   1 
ATOM   3923 N  N   . ILE C 1 151 ? 129.585 207.710 9.655   1.00 40.74  ? 151 ILE C N   1 
ATOM   3924 C  CA  . ILE C 1 151 ? 128.911 207.475 8.378   1.00 41.51  ? 151 ILE C CA  1 
ATOM   3925 C  C   . ILE C 1 151 ? 127.443 207.080 8.582   1.00 39.71  ? 151 ILE C C   1 
ATOM   3926 O  O   . ILE C 1 151 ? 127.134 206.139 9.319   1.00 40.09  ? 151 ILE C O   1 
ATOM   3927 C  CB  . ILE C 1 151 ? 129.600 206.376 7.584   1.00 41.06  ? 151 ILE C CB  1 
ATOM   3928 C  CG1 . ILE C 1 151 ? 131.024 206.787 7.252   1.00 39.14  ? 151 ILE C CG1 1 
ATOM   3929 C  CG2 . ILE C 1 151 ? 128.850 206.118 6.310   1.00 41.55  ? 151 ILE C CG2 1 
ATOM   3930 C  CD1 . ILE C 1 151 ? 131.888 205.632 6.794   1.00 43.36  ? 151 ILE C CD1 1 
ATOM   3931 N  N   . ALA C 1 152 ? 126.534 207.786 7.920   1.00 44.95  ? 152 ALA C N   1 
ATOM   3932 C  CA  . ALA C 1 152 ? 125.120 207.462 8.062   1.00 48.62  ? 152 ALA C CA  1 
ATOM   3933 C  C   . ALA C 1 152 ? 124.577 206.775 6.828   1.00 56.38  ? 152 ALA C C   1 
ATOM   3934 O  O   . ALA C 1 152 ? 123.482 206.222 6.902   1.00 71.45  ? 152 ALA C O   1 
ATOM   3935 C  CB  . ALA C 1 152 ? 124.291 208.722 8.360   1.00 38.87  ? 152 ALA C CB  1 
ATOM   3936 N  N   . GLN C 1 153 ? 125.317 206.892 5.716   1.00 50.69  ? 153 GLN C N   1 
ATOM   3937 C  CA  . GLN C 1 153 ? 125.076 206.258 4.388   1.00 80.63  ? 153 GLN C CA  1 
ATOM   3938 C  C   . GLN C 1 153 ? 125.745 207.042 3.248   1.00 79.76  ? 153 GLN C C   1 
ATOM   3939 O  O   . GLN C 1 153 ? 126.526 207.981 3.457   1.00 73.34  ? 153 GLN C O   1 
ATOM   3940 C  CB  . GLN C 1 153 ? 123.585 206.063 4.078   1.00 85.20  ? 153 GLN C CB  1 
ATOM   3941 C  CG  . GLN C 1 153 ? 123.042 204.727 4.589   1.00 79.86  ? 153 GLN C CG  1 
ATOM   3942 C  CD  . GLN C 1 153 ? 121.564 204.781 4.876   1.00 89.67  ? 153 GLN C CD  1 
ATOM   3943 O  OE1 . GLN C 1 153 ? 120.951 205.851 4.811   1.00 91.29  ? 153 GLN C OE1 1 
ATOM   3944 N  NE2 . GLN C 1 153 ? 120.986 203.639 5.243   1.00 91.82  ? 153 GLN C NE2 1 
ATOM   3945 O  OXT . GLN C 1 153 ? 125.519 206.734 2.073   1.00 84.15  1 153 GLN C OXT 1 
ATOM   3946 N  N   . THR D 2 5   ? 154.946 190.301 7.327   1.00 89.15  ? 6   THR D N   1 
ATOM   3947 C  CA  . THR D 2 5   ? 155.818 191.314 7.921   1.00 97.72  ? 6   THR D CA  1 
ATOM   3948 C  C   . THR D 2 5   ? 155.103 192.657 8.143   1.00 102.67 ? 6   THR D C   1 
ATOM   3949 O  O   . THR D 2 5   ? 154.315 193.096 7.303   1.00 100.99 ? 6   THR D O   1 
ATOM   3950 C  CB  . THR D 2 5   ? 157.072 191.544 7.051   1.00 99.75  ? 6   THR D CB  1 
ATOM   3951 O  OG1 . THR D 2 5   ? 157.537 192.889 7.227   1.00 92.06  ? 6   THR D OG1 1 
ATOM   3952 C  CG2 . THR D 2 5   ? 156.762 191.290 5.570   1.00 97.07  ? 6   THR D CG2 1 
ATOM   3953 N  N   . TYR D 2 6   ? 155.381 193.296 9.283   1.00 104.98 ? 7   TYR D N   1 
ATOM   3954 C  CA  . TYR D 2 6   ? 154.762 194.580 9.647   1.00 98.30  ? 7   TYR D CA  1 
ATOM   3955 C  C   . TYR D 2 6   ? 155.773 195.536 10.313  1.00 98.67  ? 7   TYR D C   1 
ATOM   3956 O  O   . TYR D 2 6   ? 156.941 195.187 10.497  1.00 105.34 ? 7   TYR D O   1 
ATOM   3957 C  CB  . TYR D 2 6   ? 153.536 194.349 10.565  1.00 86.52  ? 7   TYR D CB  1 
ATOM   3958 C  CG  . TYR D 2 6   ? 153.800 193.986 12.038  1.00 101.58 ? 7   TYR D CG  1 
ATOM   3959 C  CD1 . TYR D 2 6   ? 154.193 194.957 12.964  1.00 103.33 ? 7   TYR D CD1 1 
ATOM   3960 C  CD2 . TYR D 2 6   ? 153.597 192.690 12.515  1.00 101.73 ? 7   TYR D CD2 1 
ATOM   3961 C  CE1 . TYR D 2 6   ? 154.417 194.647 14.308  1.00 95.70  ? 7   TYR D CE1 1 
ATOM   3962 C  CE2 . TYR D 2 6   ? 153.815 192.374 13.867  1.00 97.92  ? 7   TYR D CE2 1 
ATOM   3963 C  CZ  . TYR D 2 6   ? 154.224 193.363 14.752  1.00 96.37  ? 7   TYR D CZ  1 
ATOM   3964 O  OH  . TYR D 2 6   ? 154.449 193.092 16.083  1.00 97.29  ? 7   TYR D OH  1 
ATOM   3965 N  N   . GLU D 2 7   ? 155.331 196.746 10.655  1.00 92.48  ? 8   GLU D N   1 
ATOM   3966 C  CA  . GLU D 2 7   ? 156.139 197.650 11.483  1.00 90.47  ? 8   GLU D CA  1 
ATOM   3967 C  C   . GLU D 2 7   ? 155.277 198.464 12.458  1.00 89.26  ? 8   GLU D C   1 
ATOM   3968 O  O   . GLU D 2 7   ? 154.324 199.122 12.039  1.00 86.49  ? 8   GLU D O   1 
ATOM   3969 C  CB  . GLU D 2 7   ? 156.954 198.613 10.627  1.00 91.19  ? 8   GLU D CB  1 
ATOM   3970 C  CG  . GLU D 2 7   ? 157.614 199.675 11.481  1.00 101.27 ? 8   GLU D CG  1 
ATOM   3971 C  CD  . GLU D 2 7   ? 158.368 200.693 10.682  1.00 110.15 ? 8   GLU D CD  1 
ATOM   3972 O  OE1 . GLU D 2 7   ? 158.736 200.383 9.530   1.00 115.61 ? 8   GLU D OE1 1 
ATOM   3973 O  OE2 . GLU D 2 7   ? 158.597 201.800 11.215  1.00 104.37 1 8   GLU D OE2 1 
ATOM   3974 N  N   . ALA D 2 8   ? 155.636 198.454 13.744  1.00 91.70  ? 9   ALA D N   1 
ATOM   3975 C  CA  . ALA D 2 8   ? 154.867 199.175 14.764  1.00 80.66  ? 9   ALA D CA  1 
ATOM   3976 C  C   . ALA D 2 8   ? 155.740 200.063 15.662  1.00 72.45  ? 9   ALA D C   1 
ATOM   3977 O  O   . ALA D 2 8   ? 156.944 199.854 15.788  1.00 81.10  ? 9   ALA D O   1 
ATOM   3978 C  CB  . ALA D 2 8   ? 154.070 198.181 15.616  1.00 74.49  ? 9   ALA D CB  1 
ATOM   3979 N  N   . THR D 2 9   ? 155.108 201.053 16.283  1.00 64.46  ? 10  THR D N   1 
ATOM   3980 C  CA  . THR D 2 9   ? 155.778 201.976 17.198  1.00 68.90  ? 10  THR D CA  1 
ATOM   3981 C  C   . THR D 2 9   ? 155.262 201.764 18.626  1.00 65.13  ? 10  THR D C   1 
ATOM   3982 O  O   . THR D 2 9   ? 154.052 201.706 18.855  1.00 71.80  ? 10  THR D O   1 
ATOM   3983 C  CB  . THR D 2 9   ? 155.558 203.439 16.757  1.00 52.63  ? 10  THR D CB  1 
ATOM   3984 O  OG1 . THR D 2 9   ? 156.344 203.698 15.590  1.00 81.93  ? 10  THR D OG1 1 
ATOM   3985 C  CG2 . THR D 2 9   ? 155.964 204.414 17.832  1.00 54.80  ? 10  THR D CG2 1 
ATOM   3986 N  N   . TYR D 2 10  ? 156.175 201.636 19.584  1.00 68.76  ? 11  TYR D N   1 
ATOM   3987 C  CA  . TYR D 2 10  ? 155.788 201.388 20.976  1.00 67.44  ? 11  TYR D CA  1 
ATOM   3988 C  C   . TYR D 2 10  ? 156.199 202.518 21.922  1.00 67.29  ? 11  TYR D C   1 
ATOM   3989 O  O   . TYR D 2 10  ? 157.247 203.124 21.739  1.00 74.27  ? 11  TYR D O   1 
ATOM   3990 C  CB  . TYR D 2 10  ? 156.395 200.065 21.461  1.00 61.73  ? 11  TYR D CB  1 
ATOM   3991 C  CG  . TYR D 2 10  ? 155.936 198.845 20.690  1.00 64.44  ? 11  TYR D CG  1 
ATOM   3992 C  CD1 . TYR D 2 10  ? 156.471 198.536 19.443  1.00 73.05  ? 11  TYR D CD1 1 
ATOM   3993 C  CD2 . TYR D 2 10  ? 154.976 197.987 21.219  1.00 70.44  ? 11  TYR D CD2 1 
ATOM   3994 C  CE1 . TYR D 2 10  ? 156.048 197.402 18.733  1.00 76.12  ? 11  TYR D CE1 1 
ATOM   3995 C  CE2 . TYR D 2 10  ? 154.549 196.855 20.519  1.00 81.06  ? 11  TYR D CE2 1 
ATOM   3996 C  CZ  . TYR D 2 10  ? 155.085 196.566 19.277  1.00 74.21  ? 11  TYR D CZ  1 
ATOM   3997 O  OH  . TYR D 2 10  ? 154.662 195.445 18.589  1.00 76.15  ? 11  TYR D OH  1 
ATOM   3998 N  N   . ALA D 2 11  ? 155.370 202.804 22.925  1.00 64.78  ? 12  ALA D N   1 
ATOM   3999 C  CA  . ALA D 2 11  ? 155.755 203.755 23.966  1.00 65.57  ? 12  ALA D CA  1 
ATOM   4000 C  C   . ALA D 2 11  ? 156.260 203.031 25.203  1.00 78.26  ? 12  ALA D C   1 
ATOM   4001 O  O   . ALA D 2 11  ? 155.575 202.166 25.743  1.00 71.95  ? 12  ALA D O   1 
ATOM   4002 C  CB  . ALA D 2 11  ? 154.596 204.629 24.342  1.00 59.74  ? 12  ALA D CB  1 
ATOM   4003 N  N   . ILE D 2 12  ? 157.440 203.429 25.674  1.00 83.62  ? 13  ILE D N   1 
ATOM   4004 C  CA  . ILE D 2 12  ? 158.055 202.853 26.868  1.00 74.51  ? 13  ILE D CA  1 
ATOM   4005 C  C   . ILE D 2 12  ? 158.543 203.952 27.794  1.00 84.75  ? 13  ILE D C   1 
ATOM   4006 O  O   . ILE D 2 12  ? 159.211 204.879 27.346  1.00 87.09  ? 13  ILE D O   1 
ATOM   4007 C  CB  . ILE D 2 12  ? 159.256 201.951 26.540  1.00 73.98  ? 13  ILE D CB  1 
ATOM   4008 C  CG1 . ILE D 2 12  ? 159.032 201.156 25.251  1.00 70.26  ? 13  ILE D CG1 1 
ATOM   4009 C  CG2 . ILE D 2 12  ? 159.569 201.051 27.721  1.00 79.25  ? 13  ILE D CG2 1 
ATOM   4010 C  CD1 . ILE D 2 12  ? 159.444 201.906 23.993  1.00 83.46  ? 13  ILE D CD1 1 
ATOM   4011 N  N   . PRO D 2 13  ? 158.219 203.856 29.090  1.00 85.22  ? 14  PRO D N   1 
ATOM   4012 C  CA  . PRO D 2 13  ? 158.755 204.865 30.013  1.00 93.60  ? 14  PRO D CA  1 
ATOM   4013 C  C   . PRO D 2 13  ? 160.272 204.744 30.196  1.00 89.10  ? 14  PRO D C   1 
ATOM   4014 O  O   . PRO D 2 13  ? 160.740 203.809 30.844  1.00 88.16  ? 14  PRO D O   1 
ATOM   4015 C  CB  . PRO D 2 13  ? 158.004 204.586 31.329  1.00 85.81  ? 14  PRO D CB  1 
ATOM   4016 C  CG  . PRO D 2 13  ? 157.407 203.225 31.177  1.00 81.81  ? 14  PRO D CG  1 
ATOM   4017 C  CD  . PRO D 2 13  ? 157.184 203.013 29.712  1.00 84.02  ? 14  PRO D CD  1 
ATOM   4018 N  N   . CYS D 2 16  ? 165.867 207.118 31.743  1.00 116.86 ? 17  CYS D N   1 
ATOM   4019 C  CA  . CYS D 2 16  ? 167.134 207.729 31.359  1.00 126.82 ? 17  CYS D CA  1 
ATOM   4020 C  C   . CYS D 2 16  ? 167.864 206.841 30.350  1.00 125.37 ? 17  CYS D C   1 
ATOM   4021 O  O   . CYS D 2 16  ? 167.253 205.951 29.756  1.00 123.03 ? 17  CYS D O   1 
ATOM   4022 C  CB  . CYS D 2 16  ? 167.994 207.990 32.596  1.00 124.06 ? 17  CYS D CB  1 
ATOM   4023 S  SG  . CYS D 2 16  ? 168.631 206.505 33.393  1.00 120.51 ? 17  CYS D SG  1 
ATOM   4024 N  N   . GLU D 2 17  ? 169.169 207.050 30.188  1.00 121.95 ? 18  GLU D N   1 
ATOM   4025 C  CA  . GLU D 2 17  ? 169.954 206.323 29.183  1.00 125.12 ? 18  GLU D CA  1 
ATOM   4026 C  C   . GLU D 2 17  ? 170.303 204.894 29.604  1.00 129.11 ? 18  GLU D C   1 
ATOM   4027 O  O   . GLU D 2 17  ? 170.723 204.081 28.774  1.00 125.97 ? 18  GLU D O   1 
ATOM   4028 C  CB  . GLU D 2 17  ? 171.229 207.095 28.833  1.00 121.88 ? 18  GLU D CB  1 
ATOM   4029 C  CG  . GLU D 2 17  ? 171.072 208.023 27.626  1.00 117.65 ? 18  GLU D CG  1 
ATOM   4030 C  CD  . GLU D 2 17  ? 170.696 207.295 26.336  1.00 113.40 ? 18  GLU D CD  1 
ATOM   4031 O  OE1 . GLU D 2 17  ? 171.047 206.106 26.174  1.00 114.50 ? 18  GLU D OE1 1 
ATOM   4032 O  OE2 . GLU D 2 17  ? 170.025 207.917 25.485  1.00 115.24 1 18  GLU D OE2 1 
ATOM   4033 N  N   . ASN D 2 18  ? 170.152 204.599 30.892  1.00 132.63 ? 19  ASN D N   1 
ATOM   4034 C  CA  . ASN D 2 18  ? 170.307 203.234 31.380  1.00 136.41 ? 19  ASN D CA  1 
ATOM   4035 C  C   . ASN D 2 18  ? 169.135 202.386 30.921  1.00 135.23 ? 19  ASN D C   1 
ATOM   4036 O  O   . ASN D 2 18  ? 169.247 201.169 30.771  1.00 133.13 ? 19  ASN D O   1 
ATOM   4037 C  CB  . ASN D 2 18  ? 170.389 203.215 32.908  1.00 138.49 ? 19  ASN D CB  1 
ATOM   4038 C  CG  . ASN D 2 18  ? 170.769 201.855 33.458  1.00 134.18 ? 19  ASN D CG  1 
ATOM   4039 O  OD1 . ASN D 2 18  ? 169.899 201.020 33.730  1.00 127.26 ? 19  ASN D OD1 1 
ATOM   4040 N  ND2 . ASN D 2 18  ? 172.064 201.624 33.630  1.00 126.23 ? 19  ASN D ND2 1 
ATOM   4041 N  N   . CYS D 2 19  ? 168.000 203.041 30.715  1.00 132.15 ? 20  CYS D N   1 
ATOM   4042 C  CA  . CYS D 2 19  ? 166.822 202.368 30.198  1.00 132.69 ? 20  CYS D CA  1 
ATOM   4043 C  C   . CYS D 2 19  ? 166.896 202.027 28.707  1.00 136.81 ? 20  CYS D C   1 
ATOM   4044 O  O   . CYS D 2 19  ? 166.463 200.948 28.303  1.00 134.31 ? 20  CYS D O   1 
ATOM   4045 C  CB  . CYS D 2 19  ? 165.582 203.220 30.465  1.00 129.21 ? 20  CYS D CB  1 
ATOM   4046 S  SG  . CYS D 2 19  ? 165.105 203.285 32.198  1.00 122.87 ? 20  CYS D SG  1 
ATOM   4047 N  N   . VAL D 2 20  ? 167.483 202.918 27.905  1.00 139.69 ? 21  VAL D N   1 
ATOM   4048 C  CA  . VAL D 2 20  ? 167.398 202.823 26.439  1.00 135.86 ? 21  VAL D CA  1 
ATOM   4049 C  C   . VAL D 2 20  ? 167.954 201.545 25.800  1.00 132.97 ? 21  VAL D C   1 
ATOM   4050 O  O   . VAL D 2 20  ? 167.226 200.818 25.124  1.00 133.94 ? 21  VAL D O   1 
ATOM   4051 C  CB  . VAL D 2 20  ? 168.122 204.018 25.777  1.00 126.57 ? 21  VAL D CB  1 
ATOM   4052 C  CG1 . VAL D 2 20  ? 167.819 204.067 24.286  1.00 115.87 ? 21  VAL D CG1 1 
ATOM   4053 C  CG2 . VAL D 2 20  ? 167.730 205.317 26.457  1.00 124.26 ? 21  VAL D CG2 1 
ATOM   4054 N  N   . ASN D 2 21  ? 169.230 201.260 26.019  1.00 131.87 ? 22  ASN D N   1 
ATOM   4055 C  CA  . ASN D 2 21  ? 169.833 200.068 25.433  1.00 136.20 ? 22  ASN D CA  1 
ATOM   4056 C  C   . ASN D 2 21  ? 169.548 198.816 26.260  1.00 133.05 ? 22  ASN D C   1 
ATOM   4057 O  O   . ASN D 2 21  ? 169.763 197.695 25.799  1.00 130.71 ? 22  ASN D O   1 
ATOM   4058 C  CB  . ASN D 2 21  ? 171.335 200.276 25.224  1.00 139.35 ? 22  ASN D CB  1 
ATOM   4059 C  CG  . ASN D 2 21  ? 172.000 200.949 26.400  1.00 136.70 ? 22  ASN D CG  1 
ATOM   4060 O  OD1 . ASN D 2 21  ? 171.563 200.813 27.543  1.00 133.32 ? 22  ASN D OD1 1 
ATOM   4061 N  ND2 . ASN D 2 21  ? 173.063 201.696 26.124  1.00 135.07 ? 22  ASN D ND2 1 
ATOM   4062 N  N   . ASP D 2 22  ? 169.058 199.020 27.481  1.00 134.38 ? 23  ASP D N   1 
ATOM   4063 C  CA  . ASP D 2 22  ? 168.562 197.930 28.316  1.00 128.36 ? 23  ASP D CA  1 
ATOM   4064 C  C   . ASP D 2 22  ? 167.480 197.186 27.547  1.00 124.77 ? 23  ASP D C   1 
ATOM   4065 O  O   . ASP D 2 22  ? 167.337 195.967 27.665  1.00 122.90 ? 23  ASP D O   1 
ATOM   4066 C  CB  . ASP D 2 22  ? 168.012 198.455 29.643  1.00 122.17 ? 23  ASP D CB  1 
ATOM   4067 C  CG  . ASP D 2 22  ? 167.652 197.341 30.608  1.00 122.76 ? 23  ASP D CG  1 
ATOM   4068 O  OD1 . ASP D 2 22  ? 168.028 196.177 30.346  1.00 122.29 ? 23  ASP D OD1 1 
ATOM   4069 O  OD2 . ASP D 2 22  ? 166.996 197.630 31.632  1.00 122.23 1 23  ASP D OD2 1 
ATOM   4070 N  N   . ILE D 2 23  ? 166.734 197.944 26.748  1.00 126.59 ? 24  ILE D N   1 
ATOM   4071 C  CA  . ILE D 2 23  ? 165.625 197.413 25.966  1.00 126.66 ? 24  ILE D CA  1 
ATOM   4072 C  C   . ILE D 2 23  ? 166.114 196.681 24.723  1.00 123.78 ? 24  ILE D C   1 
ATOM   4073 O  O   . ILE D 2 23  ? 165.671 195.566 24.430  1.00 116.38 ? 24  ILE D O   1 
ATOM   4074 C  CB  . ILE D 2 23  ? 164.681 198.532 25.493  1.00 116.33 ? 24  ILE D CB  1 
ATOM   4075 C  CG1 . ILE D 2 23  ? 164.334 199.492 26.633  1.00 116.60 ? 24  ILE D CG1 1 
ATOM   4076 C  CG2 . ILE D 2 23  ? 163.451 197.930 24.862  1.00 110.00 ? 24  ILE D CG2 1 
ATOM   4077 C  CD1 . ILE D 2 23  ? 163.283 198.984 27.578  1.00 112.27 ? 24  ILE D CD1 1 
ATOM   4078 N  N   . LYS D 2 24  ? 167.025 197.324 23.994  1.00 126.59 ? 25  LYS D N   1 
ATOM   4079 C  CA  . LYS D 2 24  ? 167.618 196.738 22.795  1.00 125.77 ? 25  LYS D CA  1 
ATOM   4080 C  C   . LYS D 2 24  ? 168.254 195.414 23.196  1.00 122.97 ? 25  LYS D C   1 
ATOM   4081 O  O   . LYS D 2 24  ? 168.204 194.434 22.451  1.00 121.27 ? 25  LYS D O   1 
ATOM   4082 C  CB  . LYS D 2 24  ? 168.649 197.688 22.166  1.00 118.81 ? 25  LYS D CB  1 
ATOM   4083 C  CG  . LYS D 2 24  ? 168.908 197.453 20.678  1.00 114.19 ? 25  LYS D CG  1 
ATOM   4084 C  CD  . LYS D 2 24  ? 169.832 198.520 20.092  1.00 114.65 ? 25  LYS D CD  1 
ATOM   4085 C  CE  . LYS D 2 24  ? 169.614 198.693 18.587  1.00 108.94 ? 25  LYS D CE  1 
ATOM   4086 N  NZ  . LYS D 2 24  ? 169.810 197.442 17.801  1.00 105.36 1 25  LYS D NZ  1 
ATOM   4087 N  N   . ALA D 2 25  ? 168.837 195.404 24.392  1.00 117.55 ? 26  ALA D N   1 
ATOM   4088 C  CA  . ALA D 2 25  ? 169.320 194.183 25.018  1.00 121.01 ? 26  ALA D CA  1 
ATOM   4089 C  C   . ALA D 2 25  ? 168.193 193.170 25.063  1.00 119.19 ? 26  ALA D C   1 
ATOM   4090 O  O   . ALA D 2 25  ? 168.297 192.066 24.522  1.00 120.16 ? 26  ALA D O   1 
ATOM   4091 C  CB  . ALA D 2 25  ? 169.837 194.464 26.421  1.00 117.76 ? 26  ALA D CB  1 
ATOM   4092 N  N   . CYS D 2 26  ? 167.111 193.579 25.711  1.00 111.98 ? 27  CYS D N   1 
ATOM   4093 C  CA  . CYS D 2 26  ? 165.978 192.720 25.986  1.00 112.62 ? 27  CYS D CA  1 
ATOM   4094 C  C   . CYS D 2 26  ? 165.394 192.049 24.734  1.00 116.98 ? 27  CYS D C   1 
ATOM   4095 O  O   . CYS D 2 26  ? 164.856 190.940 24.810  1.00 117.26 ? 27  CYS D O   1 
ATOM   4096 C  CB  . CYS D 2 26  ? 164.905 193.547 26.691  1.00 111.09 ? 27  CYS D CB  1 
ATOM   4097 S  SG  . CYS D 2 26  ? 163.658 192.601 27.555  1.00 119.14 ? 27  CYS D SG  1 
ATOM   4098 N  N   . LEU D 2 27  ? 165.533 192.700 23.580  1.00 119.15 ? 28  LEU D N   1 
ATOM   4099 C  CA  . LEU D 2 27  ? 164.860 192.237 22.365  1.00 121.15 ? 28  LEU D CA  1 
ATOM   4100 C  C   . LEU D 2 27  ? 165.710 191.380 21.417  1.00 120.33 ? 28  LEU D C   1 
ATOM   4101 O  O   . LEU D 2 27  ? 165.161 190.656 20.585  1.00 114.62 ? 28  LEU D O   1 
ATOM   4102 C  CB  . LEU D 2 27  ? 164.327 193.446 21.586  1.00 116.93 ? 28  LEU D CB  1 
ATOM   4103 C  CG  . LEU D 2 27  ? 163.231 194.298 22.234  1.00 113.87 ? 28  LEU D CG  1 
ATOM   4104 C  CD1 . LEU D 2 27  ? 162.949 195.516 21.373  1.00 112.55 ? 28  LEU D CD1 1 
ATOM   4105 C  CD2 . LEU D 2 27  ? 161.955 193.494 22.460  1.00 100.68 ? 28  LEU D CD2 1 
ATOM   4106 N  N   . LYS D 2 28  ? 167.034 191.456 21.535  1.00 119.29 ? 29  LYS D N   1 
ATOM   4107 C  CA  . LYS D 2 28  ? 167.910 190.923 20.488  1.00 123.85 ? 29  LYS D CA  1 
ATOM   4108 C  C   . LYS D 2 28  ? 167.803 189.407 20.294  1.00 122.69 ? 29  LYS D C   1 
ATOM   4109 O  O   . LYS D 2 28  ? 167.995 188.907 19.185  1.00 116.64 ? 29  LYS D O   1 
ATOM   4110 C  CB  . LYS D 2 28  ? 169.371 191.306 20.750  1.00 120.92 ? 29  LYS D CB  1 
ATOM   4111 C  CG  . LYS D 2 28  ? 169.713 192.756 20.407  1.00 118.67 ? 29  LYS D CG  1 
ATOM   4112 C  CD  . LYS D 2 28  ? 169.122 193.173 19.066  1.00 113.04 ? 29  LYS D CD  1 
ATOM   4113 C  CE  . LYS D 2 28  ? 169.795 192.443 17.915  1.00 109.77 ? 29  LYS D CE  1 
ATOM   4114 N  NZ  . LYS D 2 28  ? 169.156 192.772 16.617  1.00 102.96 1 29  LYS D NZ  1 
ATOM   4115 N  N   . ASN D 2 29  ? 167.473 188.681 21.358  1.00 126.37 ? 30  ASN D N   1 
ATOM   4116 C  CA  . ASN D 2 29  ? 167.463 187.218 21.309  1.00 124.16 ? 30  ASN D CA  1 
ATOM   4117 C  C   . ASN D 2 29  ? 166.245 186.637 20.576  1.00 122.98 ? 30  ASN D C   1 
ATOM   4118 O  O   . ASN D 2 29  ? 166.096 185.414 20.479  1.00 116.07 ? 30  ASN D O   1 
ATOM   4119 C  CB  . ASN D 2 29  ? 167.546 186.648 22.737  1.00 118.63 ? 30  ASN D CB  1 
ATOM   4120 C  CG  . ASN D 2 29  ? 166.401 187.123 23.636  1.00 111.89 ? 30  ASN D CG  1 
ATOM   4121 O  OD1 . ASN D 2 29  ? 165.941 188.265 23.538  1.00 114.82 ? 30  ASN D OD1 1 
ATOM   4122 N  ND2 . ASN D 2 29  ? 165.957 186.249 24.536  1.00 95.13  ? 30  ASN D ND2 1 
ATOM   4123 N  N   . VAL D 2 30  ? 165.393 187.521 20.054  1.00 125.98 ? 31  VAL D N   1 
ATOM   4124 C  CA  . VAL D 2 30  ? 164.145 187.133 19.385  1.00 118.91 ? 31  VAL D CA  1 
ATOM   4125 C  C   . VAL D 2 30  ? 164.242 186.974 17.870  1.00 115.21 ? 31  VAL D C   1 
ATOM   4126 O  O   . VAL D 2 30  ? 164.675 187.898 17.171  1.00 108.32 ? 31  VAL D O   1 
ATOM   4127 C  CB  . VAL D 2 30  ? 163.034 188.161 19.654  1.00 116.12 ? 31  VAL D CB  1 
ATOM   4128 C  CG1 . VAL D 2 30  ? 161.707 187.679 19.076  1.00 107.59 ? 31  VAL D CG1 1 
ATOM   4129 C  CG2 . VAL D 2 30  ? 162.914 188.426 21.138  1.00 111.99 ? 31  VAL D CG2 1 
ATOM   4130 N  N   . PRO D 2 31  ? 163.816 185.806 17.354  1.00 116.16 ? 32  PRO D N   1 
ATOM   4131 C  CA  . PRO D 2 31  ? 163.814 185.636 15.897  1.00 111.44 ? 32  PRO D CA  1 
ATOM   4132 C  C   . PRO D 2 31  ? 162.567 186.288 15.313  1.00 107.44 ? 32  PRO D C   1 
ATOM   4133 O  O   . PRO D 2 31  ? 161.594 186.501 16.036  1.00 112.67 ? 32  PRO D O   1 
ATOM   4134 C  CB  . PRO D 2 31  ? 163.791 184.115 15.715  1.00 107.15 ? 32  PRO D CB  1 
ATOM   4135 C  CG  . PRO D 2 31  ? 163.091 183.602 16.956  1.00 103.39 ? 32  PRO D CG  1 
ATOM   4136 C  CD  . PRO D 2 31  ? 163.373 184.590 18.069  1.00 104.04 ? 32  PRO D CD  1 
ATOM   4137 N  N   . GLY D 2 32  ? 162.581 186.592 14.023  1.00 108.22 ? 33  GLY D N   1 
ATOM   4138 C  CA  . GLY D 2 32  ? 161.448 187.258 13.402  1.00 111.44 ? 33  GLY D CA  1 
ATOM   4139 C  C   . GLY D 2 32  ? 161.486 188.779 13.520  1.00 110.48 ? 33  GLY D C   1 
ATOM   4140 O  O   . GLY D 2 32  ? 160.741 189.471 12.830  1.00 103.43 ? 33  GLY D O   1 
ATOM   4141 N  N   . ILE D 2 33  ? 162.328 189.300 14.411  1.00 112.76 ? 34  ILE D N   1 
ATOM   4142 C  CA  . ILE D 2 33  ? 162.558 190.742 14.507  1.00 105.68 ? 34  ILE D CA  1 
ATOM   4143 C  C   . ILE D 2 33  ? 163.667 191.149 13.556  1.00 107.55 ? 34  ILE D C   1 
ATOM   4144 O  O   . ILE D 2 33  ? 164.789 190.652 13.663  1.00 104.09 ? 34  ILE D O   1 
ATOM   4145 C  CB  . ILE D 2 33  ? 162.922 191.190 15.926  1.00 108.96 ? 34  ILE D CB  1 
ATOM   4146 C  CG1 . ILE D 2 33  ? 161.726 190.995 16.862  1.00 108.17 ? 34  ILE D CG1 1 
ATOM   4147 C  CG2 . ILE D 2 33  ? 163.337 192.656 15.922  1.00 103.30 ? 34  ILE D CG2 1 
ATOM   4148 C  CD1 . ILE D 2 33  ? 161.982 191.449 18.285  1.00 105.30 ? 34  ILE D CD1 1 
ATOM   4149 N  N   . ASN D 2 34  ? 163.349 192.056 12.637  1.00 107.93 ? 35  ASN D N   1 
ATOM   4150 C  CA  . ASN D 2 34  ? 164.299 192.487 11.618  1.00 108.58 ? 35  ASN D CA  1 
ATOM   4151 C  C   . ASN D 2 34  ? 165.174 193.675 12.000  1.00 110.37 ? 35  ASN D C   1 
ATOM   4152 O  O   . ASN D 2 34  ? 166.382 193.662 11.755  1.00 109.07 ? 35  ASN D O   1 
ATOM   4153 C  CB  . ASN D 2 34  ? 163.543 192.836 10.335  1.00 112.09 ? 35  ASN D CB  1 
ATOM   4154 C  CG  . ASN D 2 34  ? 162.654 191.710 9.863   1.00 104.81 ? 35  ASN D CG  1 
ATOM   4155 O  OD1 . ASN D 2 34  ? 161.513 191.581 10.305  1.00 103.62 ? 35  ASN D OD1 1 
ATOM   4156 N  ND2 . ASN D 2 34  ? 163.173 190.884 8.963   1.00 95.50  ? 35  ASN D ND2 1 
ATOM   4157 N  N   . SER D 2 35  ? 164.573 194.691 12.610  1.00 110.24 ? 36  SER D N   1 
ATOM   4158 C  CA  . SER D 2 35  ? 165.318 195.897 12.957  1.00 114.18 ? 36  SER D CA  1 
ATOM   4159 C  C   . SER D 2 35  ? 164.647 196.660 14.089  1.00 113.04 ? 36  SER D C   1 
ATOM   4160 O  O   . SER D 2 35  ? 163.469 196.449 14.383  1.00 108.65 ? 36  SER D O   1 
ATOM   4161 C  CB  . SER D 2 35  ? 165.482 196.800 11.724  1.00 114.20 ? 36  SER D CB  1 
ATOM   4162 O  OG  . SER D 2 35  ? 164.235 197.285 11.252  1.00 111.58 ? 36  SER D OG  1 
ATOM   4163 N  N   . LEU D 2 36  ? 165.415 197.542 14.722  1.00 109.35 ? 37  LEU D N   1 
ATOM   4164 C  CA  . LEU D 2 36  ? 164.928 198.362 15.824  1.00 107.51 ? 37  LEU D CA  1 
ATOM   4165 C  C   . LEU D 2 36  ? 165.479 199.789 15.736  1.00 108.56 ? 37  LEU D C   1 
ATOM   4166 O  O   . LEU D 2 36  ? 166.679 199.979 15.546  1.00 111.52 ? 37  LEU D O   1 
ATOM   4167 C  CB  . LEU D 2 36  ? 165.320 197.731 17.173  1.00 115.28 ? 37  LEU D CB  1 
ATOM   4168 C  CG  . LEU D 2 36  ? 165.063 196.238 17.446  1.00 113.79 ? 37  LEU D CG  1 
ATOM   4169 C  CD1 . LEU D 2 36  ? 165.903 195.729 18.618  1.00 112.87 ? 37  LEU D CD1 1 
ATOM   4170 C  CD2 . LEU D 2 36  ? 163.591 195.958 17.694  1.00 108.42 ? 37  LEU D CD2 1 
ATOM   4171 N  N   . ASN D 2 37  ? 164.603 200.785 15.853  1.00 108.44 ? 38  ASN D N   1 
ATOM   4172 C  CA  . ASN D 2 37  ? 165.021 202.191 15.929  1.00 110.07 ? 38  ASN D CA  1 
ATOM   4173 C  C   . ASN D 2 37  ? 164.507 202.870 17.188  1.00 101.38 ? 38  ASN D C   1 
ATOM   4174 O  O   . ASN D 2 37  ? 163.460 202.503 17.721  1.00 101.58 ? 38  ASN D O   1 
ATOM   4175 C  CB  . ASN D 2 37  ? 164.564 202.982 14.700  1.00 112.85 ? 38  ASN D CB  1 
ATOM   4176 C  CG  . ASN D 2 37  ? 165.440 202.734 13.491  1.00 124.01 ? 38  ASN D CG  1 
ATOM   4177 O  OD1 . ASN D 2 37  ? 165.316 201.711 12.816  1.00 123.61 ? 38  ASN D OD1 1 
ATOM   4178 N  ND2 . ASN D 2 37  ? 166.339 203.677 13.210  1.00 120.32 ? 38  ASN D ND2 1 
ATOM   4179 N  N   . PHE D 2 38  ? 165.244 203.869 17.659  1.00 97.91  ? 39  PHE D N   1 
ATOM   4180 C  CA  . PHE D 2 38  ? 164.921 204.494 18.930  1.00 98.86  ? 39  PHE D CA  1 
ATOM   4181 C  C   . PHE D 2 38  ? 164.874 206.000 18.812  1.00 100.61 ? 39  PHE D C   1 
ATOM   4182 O  O   . PHE D 2 38  ? 165.681 206.610 18.115  1.00 109.33 ? 39  PHE D O   1 
ATOM   4183 C  CB  . PHE D 2 38  ? 165.929 204.077 19.997  1.00 98.62  ? 39  PHE D CB  1 
ATOM   4184 C  CG  . PHE D 2 38  ? 165.777 202.648 20.433  1.00 103.76 ? 39  PHE D CG  1 
ATOM   4185 C  CD1 . PHE D 2 38  ? 166.190 201.606 19.606  1.00 99.00  ? 39  PHE D CD1 1 
ATOM   4186 C  CD2 . PHE D 2 38  ? 165.208 202.343 21.660  1.00 95.14  ? 39  PHE D CD2 1 
ATOM   4187 C  CE1 . PHE D 2 38  ? 166.042 200.282 19.993  1.00 100.05 ? 39  PHE D CE1 1 
ATOM   4188 C  CE2 . PHE D 2 38  ? 165.058 201.021 22.060  1.00 103.56 ? 39  PHE D CE2 1 
ATOM   4189 C  CZ  . PHE D 2 38  ? 165.477 199.987 21.223  1.00 107.82 ? 39  PHE D CZ  1 
ATOM   4190 N  N   . ASP D 2 39  ? 163.908 206.587 19.505  1.00 98.04  ? 40  ASP D N   1 
ATOM   4191 C  CA  . ASP D 2 39  ? 163.733 208.030 19.555  1.00 101.83 ? 40  ASP D CA  1 
ATOM   4192 C  C   . ASP D 2 39  ? 163.512 208.372 21.015  1.00 107.05 ? 40  ASP D C   1 
ATOM   4193 O  O   . ASP D 2 39  ? 162.382 208.385 21.497  1.00 109.07 ? 40  ASP D O   1 
ATOM   4194 C  CB  . ASP D 2 39  ? 162.547 208.470 18.690  1.00 102.03 ? 40  ASP D CB  1 
ATOM   4195 C  CG  . ASP D 2 39  ? 162.583 209.946 18.348  1.00 101.33 ? 40  ASP D CG  1 
ATOM   4196 O  OD1 . ASP D 2 39  ? 163.453 210.656 18.890  1.00 103.34 ? 40  ASP D OD1 1 
ATOM   4197 O  OD2 . ASP D 2 39  ? 161.734 210.393 17.546  1.00 92.80  1 40  ASP D OD2 1 
ATOM   4198 N  N   . ILE D 2 40  ? 164.598 208.668 21.715  1.00 107.64 ? 41  ILE D N   1 
ATOM   4199 C  CA  . ILE D 2 40  ? 164.565 208.741 23.168  1.00 106.02 ? 41  ILE D CA  1 
ATOM   4200 C  C   . ILE D 2 40  ? 163.846 209.977 23.714  1.00 104.57 ? 41  ILE D C   1 
ATOM   4201 O  O   . ILE D 2 40  ? 163.394 209.983 24.865  1.00 100.99 ? 41  ILE D O   1 
ATOM   4202 C  CB  . ILE D 2 40  ? 165.999 208.701 23.709  1.00 105.51 ? 41  ILE D CB  1 
ATOM   4203 C  CG1 . ILE D 2 40  ? 166.825 209.835 23.094  1.00 103.78 ? 41  ILE D CG1 1 
ATOM   4204 C  CG2 . ILE D 2 40  ? 166.643 207.372 23.361  1.00 103.84 ? 41  ILE D CG2 1 
ATOM   4205 C  CD1 . ILE D 2 40  ? 168.299 209.784 23.437  1.00 101.34 ? 41  ILE D CD1 1 
ATOM   4206 N  N   . GLU D 2 41  ? 163.735 211.014 22.888  1.00 105.02 ? 42  GLU D N   1 
ATOM   4207 C  CA  . GLU D 2 41  ? 162.982 212.208 23.259  1.00 110.95 ? 42  GLU D CA  1 
ATOM   4208 C  C   . GLU D 2 41  ? 161.488 211.921 23.363  1.00 110.92 ? 42  GLU D C   1 
ATOM   4209 O  O   . GLU D 2 41  ? 160.867 212.175 24.399  1.00 103.36 ? 42  GLU D O   1 
ATOM   4210 C  CB  . GLU D 2 41  ? 163.233 213.350 22.270  1.00 112.29 ? 42  GLU D CB  1 
ATOM   4211 C  CG  . GLU D 2 41  ? 162.384 214.588 22.560  1.00 114.85 ? 42  GLU D CG  1 
ATOM   4212 C  CD  . GLU D 2 41  ? 162.812 215.801 21.759  1.00 117.85 ? 42  GLU D CD  1 
ATOM   4213 O  OE1 . GLU D 2 41  ? 163.777 215.685 20.973  1.00 114.75 ? 42  GLU D OE1 1 
ATOM   4214 O  OE2 . GLU D 2 41  ? 162.188 216.872 21.926  1.00 112.39 1 42  GLU D OE2 1 
ATOM   4215 N  N   . GLN D 2 42  ? 160.923 211.379 22.285  1.00 111.40 ? 43  GLN D N   1 
ATOM   4216 C  CA  . GLN D 2 42  ? 159.503 211.025 22.248  1.00 113.39 ? 43  GLN D CA  1 
ATOM   4217 C  C   . GLN D 2 42  ? 159.210 209.742 23.040  1.00 109.37 ? 43  GLN D C   1 
ATOM   4218 O  O   . GLN D 2 42  ? 158.049 209.339 23.170  1.00 101.44 ? 43  GLN D O   1 
ATOM   4219 C  CB  . GLN D 2 42  ? 159.019 210.859 20.793  1.00 107.99 ? 43  GLN D CB  1 
ATOM   4220 C  CG  . GLN D 2 42  ? 158.913 212.150 19.967  1.00 108.95 ? 43  GLN D CG  1 
ATOM   4221 C  CD  . GLN D 2 42  ? 158.669 211.891 18.475  1.00 107.83 ? 43  GLN D CD  1 
ATOM   4222 O  OE1 . GLN D 2 42  ? 159.313 211.035 17.861  1.00 97.38  ? 43  GLN D OE1 1 
ATOM   4223 N  NE2 . GLN D 2 42  ? 157.729 212.630 17.894  1.00 107.34 ? 43  GLN D NE2 1 
ATOM   4224 N  N   . GLN D 2 43  ? 160.268 209.108 23.552  1.00 106.60 ? 44  GLN D N   1 
ATOM   4225 C  CA  . GLN D 2 43  ? 160.158 207.854 24.300  1.00 97.45  ? 44  GLN D CA  1 
ATOM   4226 C  C   . GLN D 2 43  ? 159.420 206.782 23.524  1.00 87.75  ? 44  GLN D C   1 
ATOM   4227 O  O   . GLN D 2 43  ? 158.499 206.161 24.050  1.00 80.71  ? 44  GLN D O   1 
ATOM   4228 C  CB  . GLN D 2 43  ? 159.461 208.068 25.639  1.00 96.08  ? 44  GLN D CB  1 
ATOM   4229 C  CG  . GLN D 2 43  ? 160.354 208.613 26.728  1.00 99.10  ? 44  GLN D CG  1 
ATOM   4230 C  CD  . GLN D 2 43  ? 159.608 208.751 28.030  1.00 101.39 ? 44  GLN D CD  1 
ATOM   4231 O  OE1 . GLN D 2 43  ? 158.530 209.350 28.078  1.00 102.17 ? 44  GLN D OE1 1 
ATOM   4232 N  NE2 . GLN D 2 43  ? 160.159 208.171 29.094  1.00 98.79  ? 44  GLN D NE2 1 
ATOM   4233 N  N   . ILE D 2 44  ? 159.816 206.578 22.273  1.00 82.99  ? 45  ILE D N   1 
ATOM   4234 C  CA  . ILE D 2 44  ? 159.185 205.569 21.438  1.00 87.05  ? 45  ILE D CA  1 
ATOM   4235 C  C   . ILE D 2 44  ? 160.228 204.627 20.863  1.00 85.05  ? 45  ILE D C   1 
ATOM   4236 O  O   . ILE D 2 44  ? 161.423 204.786 21.083  1.00 92.46  ? 45  ILE D O   1 
ATOM   4237 C  CB  . ILE D 2 44  ? 158.358 206.185 20.266  1.00 81.90  ? 45  ILE D CB  1 
ATOM   4238 C  CG1 . ILE D 2 44  ? 159.271 206.730 19.163  1.00 93.64  ? 45  ILE D CG1 1 
ATOM   4239 C  CG2 . ILE D 2 44  ? 157.397 207.260 20.764  1.00 86.12  ? 45  ILE D CG2 1 
ATOM   4240 C  CD1 . ILE D 2 44  ? 158.513 207.316 17.982  1.00 88.57  ? 45  ILE D CD1 1 
ATOM   4241 N  N   . MET D 2 45  ? 159.751 203.616 20.157  1.00 81.24  ? 46  MET D N   1 
ATOM   4242 C  CA  . MET D 2 45  ? 160.614 202.628 19.546  1.00 89.11  ? 46  MET D CA  1 
ATOM   4243 C  C   . MET D 2 45  ? 159.907 202.003 18.344  1.00 91.79  ? 46  MET D C   1 
ATOM   4244 O  O   . MET D 2 45  ? 158.777 201.524 18.465  1.00 81.79  ? 46  MET D O   1 
ATOM   4245 C  CB  . MET D 2 45  ? 161.001 201.557 20.563  1.00 87.22  ? 46  MET D CB  1 
ATOM   4246 C  CG  . MET D 2 45  ? 161.492 200.259 19.929  1.00 100.27 ? 46  MET D CG  1 
ATOM   4247 S  SD  . MET D 2 45  ? 161.269 198.821 20.998  1.00 117.91 ? 46  MET D SD  1 
ATOM   4248 C  CE  . MET D 2 45  ? 161.535 199.584 22.586  1.00 96.64  ? 46  MET D CE  1 
ATOM   4249 N  N   . SER D 2 46  ? 160.565 202.004 17.190  1.00 90.63  ? 47  SER D N   1 
ATOM   4250 C  CA  . SER D 2 46  ? 159.981 201.414 15.993  1.00 86.34  ? 47  SER D CA  1 
ATOM   4251 C  C   . SER D 2 46  ? 160.433 199.956 15.848  1.00 89.79  ? 47  SER D C   1 
ATOM   4252 O  O   . SER D 2 46  ? 161.609 199.648 16.035  1.00 93.75  ? 47  SER D O   1 
ATOM   4253 C  CB  . SER D 2 46  ? 160.381 202.230 14.772  1.00 94.21  ? 47  SER D CB  1 
ATOM   4254 O  OG  . SER D 2 46  ? 160.222 203.610 15.050  1.00 98.79  ? 47  SER D OG  1 
ATOM   4255 N  N   . VAL D 2 47  ? 159.504 199.059 15.520  1.00 88.95  ? 48  VAL D N   1 
ATOM   4256 C  CA  . VAL D 2 47  ? 159.821 197.628 15.422  1.00 95.41  ? 48  VAL D CA  1 
ATOM   4257 C  C   . VAL D 2 47  ? 159.248 196.939 14.179  1.00 97.37  ? 48  VAL D C   1 
ATOM   4258 O  O   . VAL D 2 47  ? 158.033 196.823 14.019  1.00 91.11  ? 48  VAL D O   1 
ATOM   4259 C  CB  . VAL D 2 47  ? 159.311 196.841 16.661  1.00 94.84  ? 48  VAL D CB  1 
ATOM   4260 C  CG1 . VAL D 2 47  ? 159.527 195.346 16.476  1.00 93.47  ? 48  VAL D CG1 1 
ATOM   4261 C  CG2 . VAL D 2 47  ? 159.992 197.320 17.933  1.00 101.78 ? 48  VAL D CG2 1 
ATOM   4262 N  N   . GLU D 2 48  ? 160.138 196.479 13.305  1.00 98.54  ? 49  GLU D N   1 
ATOM   4263 C  CA  . GLU D 2 48  ? 159.739 195.723 12.127  1.00 105.36 ? 49  GLU D CA  1 
ATOM   4264 C  C   . GLU D 2 48  ? 159.892 194.233 12.426  1.00 102.28 ? 49  GLU D C   1 
ATOM   4265 O  O   . GLU D 2 48  ? 160.990 193.781 12.741  1.00 99.12  ? 49  GLU D O   1 
ATOM   4266 C  CB  . GLU D 2 48  ? 160.587 196.108 10.910  1.00 104.61 ? 49  GLU D CB  1 
ATOM   4267 C  CG  . GLU D 2 48  ? 160.141 195.439 9.611   1.00 114.39 ? 49  GLU D CG  1 
ATOM   4268 C  CD  . GLU D 2 48  ? 161.022 195.786 8.420   1.00 113.05 ? 49  GLU D CD  1 
ATOM   4269 O  OE1 . GLU D 2 48  ? 162.183 196.205 8.631   1.00 111.08 ? 49  GLU D OE1 1 
ATOM   4270 O  OE2 . GLU D 2 48  ? 160.551 195.634 7.271   1.00 102.21 1 49  GLU D OE2 1 
ATOM   4271 N  N   . SER D 2 49  ? 158.807 193.467 12.329  1.00 95.48  ? 50  SER D N   1 
ATOM   4272 C  CA  . SER D 2 49  ? 158.861 192.054 12.697  1.00 98.98  ? 50  SER D CA  1 
ATOM   4273 C  C   . SER D 2 49  ? 157.738 191.238 12.071  1.00 103.46 ? 50  SER D C   1 
ATOM   4274 O  O   . SER D 2 49  ? 156.780 191.785 11.532  1.00 104.41 ? 50  SER D O   1 
ATOM   4275 C  CB  . SER D 2 49  ? 158.799 191.890 14.221  1.00 98.10  ? 50  SER D CB  1 
ATOM   4276 O  OG  . SER D 2 49  ? 157.564 192.355 14.748  1.00 93.09  ? 50  SER D OG  1 
ATOM   4277 N  N   . SER D 2 50  ? 157.867 189.916 12.163  1.00 110.02 ? 51  SER D N   1 
ATOM   4278 C  CA  . SER D 2 50  ? 156.806 188.985 11.779  1.00 108.87 ? 51  SER D CA  1 
ATOM   4279 C  C   . SER D 2 50  ? 156.256 188.313 13.023  1.00 103.96 ? 51  SER D C   1 
ATOM   4280 O  O   . SER D 2 50  ? 155.523 187.327 12.944  1.00 102.50 ? 51  SER D O   1 
ATOM   4281 C  CB  . SER D 2 50  ? 157.322 187.930 10.793  1.00 96.33  ? 51  SER D CB  1 
ATOM   4282 O  OG  . SER D 2 50  ? 158.407 187.200 11.346  1.00 94.61  ? 51  SER D OG  1 
ATOM   4283 N  N   . VAL D 2 51  ? 156.660 188.825 14.176  1.00 101.18 ? 52  VAL D N   1 
ATOM   4284 C  CA  . VAL D 2 51  ? 156.234 188.255 15.436  1.00 99.55  ? 52  VAL D CA  1 
ATOM   4285 C  C   . VAL D 2 51  ? 155.075 189.101 15.942  1.00 96.84  ? 52  VAL D C   1 
ATOM   4286 O  O   . VAL D 2 51  ? 155.042 190.310 15.715  1.00 96.52  ? 52  VAL D O   1 
ATOM   4287 C  CB  . VAL D 2 51  ? 157.395 188.188 16.460  1.00 97.13  ? 52  VAL D CB  1 
ATOM   4288 C  CG1 . VAL D 2 51  ? 157.751 189.577 16.973  1.00 89.73  ? 52  VAL D CG1 1 
ATOM   4289 C  CG2 . VAL D 2 51  ? 157.041 187.254 17.606  1.00 100.73 ? 52  VAL D CG2 1 
ATOM   4290 N  N   . ALA D 2 52  ? 154.112 188.453 16.589  1.00 102.47 ? 53  ALA D N   1 
ATOM   4291 C  CA  . ALA D 2 52  ? 152.957 189.134 17.163  1.00 97.28  ? 53  ALA D CA  1 
ATOM   4292 C  C   . ALA D 2 52  ? 153.419 190.274 18.059  1.00 97.95  ? 53  ALA D C   1 
ATOM   4293 O  O   . ALA D 2 52  ? 154.463 190.172 18.710  1.00 92.88  ? 53  ALA D O   1 
ATOM   4294 C  CB  . ALA D 2 52  ? 152.084 188.158 17.941  1.00 87.48  ? 53  ALA D CB  1 
ATOM   4295 N  N   . PRO D 2 53  ? 152.676 191.392 18.045  1.00 98.54  ? 54  PRO D N   1 
ATOM   4296 C  CA  . PRO D 2 53  ? 153.010 192.548 18.889  1.00 93.64  ? 54  PRO D CA  1 
ATOM   4297 C  C   . PRO D 2 53  ? 152.942 192.200 20.377  1.00 93.79  ? 54  PRO D C   1 
ATOM   4298 O  O   . PRO D 2 53  ? 153.665 192.795 21.181  1.00 88.04  ? 54  PRO D O   1 
ATOM   4299 C  CB  . PRO D 2 53  ? 151.945 193.580 18.505  1.00 81.60  ? 54  PRO D CB  1 
ATOM   4300 C  CG  . PRO D 2 53  ? 150.812 192.764 17.974  1.00 88.67  ? 54  PRO D CG  1 
ATOM   4301 C  CD  . PRO D 2 53  ? 151.457 191.622 17.251  1.00 85.02  ? 54  PRO D CD  1 
ATOM   4302 N  N   . SER D 2 54  ? 152.092 191.231 20.721  1.00 92.98  ? 55  SER D N   1 
ATOM   4303 C  CA  . SER D 2 54  ? 152.001 190.710 22.085  1.00 85.05  ? 55  SER D CA  1 
ATOM   4304 C  C   . SER D 2 54  ? 153.306 190.054 22.531  1.00 91.01  ? 55  SER D C   1 
ATOM   4305 O  O   . SER D 2 54  ? 153.540 189.926 23.719  1.00 84.87  ? 55  SER D O   1 
ATOM   4306 C  CB  . SER D 2 54  ? 150.851 189.703 22.217  1.00 89.58  ? 55  SER D CB  1 
ATOM   4307 O  OG  . SER D 2 54  ? 151.007 188.600 21.337  1.00 93.86  ? 55  SER D OG  1 
ATOM   4308 N  N   . THR D 2 55  ? 154.127 189.592 21.589  1.00 93.61  ? 56  THR D N   1 
ATOM   4309 C  CA  . THR D 2 55  ? 155.458 189.086 21.930  1.00 93.45  ? 56  THR D CA  1 
ATOM   4310 C  C   . THR D 2 55  ? 156.411 190.227 22.294  1.00 89.17  ? 56  THR D C   1 
ATOM   4311 O  O   . THR D 2 55  ? 157.091 190.162 23.317  1.00 84.62  ? 56  THR D O   1 
ATOM   4312 C  CB  . THR D 2 55  ? 156.097 188.258 20.796  1.00 91.88  ? 56  THR D CB  1 
ATOM   4313 O  OG1 . THR D 2 55  ? 155.228 187.184 20.405  1.00 85.28  ? 56  THR D OG1 1 
ATOM   4314 C  CG2 . THR D 2 55  ? 157.396 187.663 21.285  1.00 87.75  ? 56  THR D CG2 1 
ATOM   4315 N  N   . ILE D 2 56  ? 156.478 191.249 21.440  1.00 80.70  ? 57  ILE D N   1 
ATOM   4316 C  CA  . ILE D 2 56  ? 157.278 192.444 21.716  1.00 82.40  ? 57  ILE D CA  1 
ATOM   4317 C  C   . ILE D 2 56  ? 156.945 193.009 23.077  1.00 82.90  ? 57  ILE D C   1 
ATOM   4318 O  O   . ILE D 2 56  ? 157.824 193.334 23.864  1.00 82.95  ? 57  ILE D O   1 
ATOM   4319 C  CB  . ILE D 2 56  ? 157.037 193.548 20.686  1.00 82.11  ? 57  ILE D CB  1 
ATOM   4320 C  CG1 . ILE D 2 56  ? 157.150 192.987 19.267  1.00 90.00  ? 57  ILE D CG1 1 
ATOM   4321 C  CG2 . ILE D 2 56  ? 158.010 194.694 20.907  1.00 69.56  ? 57  ILE D CG2 1 
ATOM   4322 C  CD1 . ILE D 2 56  ? 158.563 192.828 18.798  1.00 79.69  ? 57  ILE D CD1 1 
ATOM   4323 N  N   . ILE D 2 57  ? 155.649 193.107 23.336  1.00 79.51  ? 58  ILE D N   1 
ATOM   4324 C  CA  . ILE D 2 57  ? 155.124 193.688 24.557  1.00 81.58  ? 58  ILE D CA  1 
ATOM   4325 C  C   . ILE D 2 57  ? 155.320 192.736 25.739  1.00 89.25  ? 58  ILE D C   1 
ATOM   4326 O  O   . ILE D 2 57  ? 155.628 193.181 26.850  1.00 85.67  ? 58  ILE D O   1 
ATOM   4327 C  CB  . ILE D 2 57  ? 153.636 194.081 24.363  1.00 79.04  ? 58  ILE D CB  1 
ATOM   4328 C  CG1 . ILE D 2 57  ? 153.571 195.374 23.558  1.00 77.82  ? 58  ILE D CG1 1 
ATOM   4329 C  CG2 . ILE D 2 57  ? 152.928 194.274 25.681  1.00 77.55  ? 58  ILE D CG2 1 
ATOM   4330 C  CD1 . ILE D 2 57  ? 152.236 195.672 23.010  1.00 78.72  ? 58  ILE D CD1 1 
ATOM   4331 N  N   . ASN D 2 58  ? 155.149 191.432 25.502  1.00 95.79  ? 59  ASN D N   1 
ATOM   4332 C  CA  . ASN D 2 58  ? 155.328 190.429 26.559  1.00 91.84  ? 59  ASN D CA  1 
ATOM   4333 C  C   . ASN D 2 58  ? 156.799 190.371 26.951  1.00 89.57  ? 59  ASN D C   1 
ATOM   4334 O  O   . ASN D 2 58  ? 157.141 190.266 28.131  1.00 92.54  ? 59  ASN D O   1 
ATOM   4335 C  CB  . ASN D 2 58  ? 154.875 189.030 26.105  1.00 92.11  ? 59  ASN D CB  1 
ATOM   4336 C  CG  . ASN D 2 58  ? 153.431 188.716 26.479  1.00 95.03  ? 59  ASN D CG  1 
ATOM   4337 O  OD1 . ASN D 2 58  ? 152.756 189.513 27.134  1.00 95.95  ? 59  ASN D OD1 1 
ATOM   4338 N  ND2 . ASN D 2 58  ? 152.944 187.556 26.038  1.00 88.55  ? 59  ASN D ND2 1 
ATOM   4339 N  N   . THR D 2 59  ? 157.663 190.441 25.944  1.00 90.53  ? 60  THR D N   1 
ATOM   4340 C  CA  . THR D 2 59  ? 159.102 190.492 26.150  1.00 89.20  ? 60  THR D CA  1 
ATOM   4341 C  C   . THR D 2 59  ? 159.457 191.651 27.067  1.00 94.70  ? 60  THR D C   1 
ATOM   4342 O  O   . THR D 2 59  ? 160.207 191.488 28.027  1.00 95.98  ? 60  THR D O   1 
ATOM   4343 C  CB  . THR D 2 59  ? 159.854 190.623 24.820  1.00 83.88  ? 60  THR D CB  1 
ATOM   4344 O  OG1 . THR D 2 59  ? 159.459 189.556 23.953  1.00 76.72  ? 60  THR D OG1 1 
ATOM   4345 C  CG2 . THR D 2 59  ? 161.351 190.548 25.037  1.00 91.59  ? 60  THR D CG2 1 
ATOM   4346 N  N   . LEU D 2 60  ? 158.880 192.815 26.788  1.00 94.82  ? 61  LEU D N   1 
ATOM   4347 C  CA  . LEU D 2 60  ? 159.126 193.992 27.606  1.00 90.50  ? 61  LEU D CA  1 
ATOM   4348 C  C   . LEU D 2 60  ? 158.525 193.869 29.006  1.00 83.95  ? 61  LEU D C   1 
ATOM   4349 O  O   . LEU D 2 60  ? 159.129 194.327 29.971  1.00 82.90  ? 61  LEU D O   1 
ATOM   4350 C  CB  . LEU D 2 60  ? 158.599 195.232 26.885  1.00 88.19  ? 61  LEU D CB  1 
ATOM   4351 C  CG  . LEU D 2 60  ? 159.388 195.492 25.601  1.00 84.94  ? 61  LEU D CG  1 
ATOM   4352 C  CD1 . LEU D 2 60  ? 158.721 196.498 24.699  1.00 76.39  ? 61  LEU D CD1 1 
ATOM   4353 C  CD2 . LEU D 2 60  ? 160.753 195.979 25.987  1.00 89.60  ? 61  LEU D CD2 1 
ATOM   4354 N  N   . ARG D 2 61  ? 157.357 193.242 29.130  1.00 85.62  ? 62  ARG D N   1 
ATOM   4355 C  CA  . ARG D 2 61  ? 156.772 193.007 30.451  1.00 84.54  ? 62  ARG D CA  1 
ATOM   4356 C  C   . ARG D 2 61  ? 157.655 192.074 31.281  1.00 94.42  ? 62  ARG D C   1 
ATOM   4357 O  O   . ARG D 2 61  ? 157.771 192.230 32.502  1.00 86.94  ? 62  ARG D O   1 
ATOM   4358 C  CB  . ARG D 2 61  ? 155.361 192.415 30.344  1.00 91.55  ? 62  ARG D CB  1 
ATOM   4359 C  CG  . ARG D 2 61  ? 154.313 193.342 29.756  1.00 95.61  ? 62  ARG D CG  1 
ATOM   4360 C  CD  . ARG D 2 61  ? 152.918 192.753 29.949  1.00 109.85 ? 62  ARG D CD  1 
ATOM   4361 N  NE  . ARG D 2 61  ? 151.888 193.474 29.200  1.00 111.97 ? 62  ARG D NE  1 
ATOM   4362 C  CZ  . ARG D 2 61  ? 151.240 194.542 29.655  1.00 100.71 ? 62  ARG D CZ  1 
ATOM   4363 N  NH1 . ARG D 2 61  ? 151.522 195.021 30.858  1.00 95.46  1 62  ARG D NH1 1 
ATOM   4364 N  NH2 . ARG D 2 61  ? 150.315 195.132 28.907  1.00 91.90  ? 62  ARG D NH2 1 
ATOM   4365 N  N   . ASN D 2 62  ? 158.282 191.107 30.614  1.00 92.84  ? 63  ASN D N   1 
ATOM   4366 C  CA  . ASN D 2 62  ? 159.171 190.167 31.290  1.00 85.54  ? 63  ASN D CA  1 
ATOM   4367 C  C   . ASN D 2 62  ? 160.485 190.825 31.693  1.00 96.59  ? 63  ASN D C   1 
ATOM   4368 O  O   . ASN D 2 62  ? 161.316 190.214 32.365  1.00 89.91  ? 63  ASN D O   1 
ATOM   4369 C  CB  . ASN D 2 62  ? 159.441 188.957 30.402  1.00 85.83  ? 63  ASN D CB  1 
ATOM   4370 C  CG  . ASN D 2 62  ? 158.178 188.191 30.069  1.00 96.18  ? 63  ASN D CG  1 
ATOM   4371 O  OD1 . ASN D 2 62  ? 157.322 187.977 30.931  1.00 96.64  ? 63  ASN D OD1 1 
ATOM   4372 N  ND2 . ASN D 2 62  ? 158.044 187.788 28.807  1.00 91.40  ? 63  ASN D ND2 1 
ATOM   4373 N  N   . CYS D 2 63  ? 160.666 192.073 31.265  1.00 98.43  ? 64  CYS D N   1 
ATOM   4374 C  CA  . CYS D 2 63  ? 161.804 192.884 31.679  1.00 93.03  ? 64  CYS D CA  1 
ATOM   4375 C  C   . CYS D 2 63  ? 161.354 194.036 32.560  1.00 93.32  ? 64  CYS D C   1 
ATOM   4376 O  O   . CYS D 2 63  ? 162.048 195.050 32.654  1.00 104.02 ? 64  CYS D O   1 
ATOM   4377 C  CB  . CYS D 2 63  ? 162.557 193.437 30.469  1.00 98.02  ? 64  CYS D CB  1 
ATOM   4378 S  SG  . CYS D 2 63  ? 163.459 192.204 29.535  1.00 120.72 ? 64  CYS D SG  1 
ATOM   4379 N  N   . GLY D 2 64  ? 160.190 193.883 33.189  1.00 84.44  ? 65  GLY D N   1 
ATOM   4380 C  CA  . GLY D 2 64  ? 159.661 194.897 34.088  1.00 93.28  ? 65  GLY D CA  1 
ATOM   4381 C  C   . GLY D 2 64  ? 159.493 196.251 33.426  1.00 82.22  ? 65  GLY D C   1 
ATOM   4382 O  O   . GLY D 2 64  ? 159.746 197.297 34.030  1.00 78.88  ? 65  GLY D O   1 
ATOM   4383 N  N   . LYS D 2 65  ? 159.071 196.221 32.169  1.00 81.79  ? 66  LYS D N   1 
ATOM   4384 C  CA  . LYS D 2 65  ? 158.930 197.427 31.376  1.00 85.21  ? 66  LYS D CA  1 
ATOM   4385 C  C   . LYS D 2 65  ? 157.646 197.372 30.559  1.00 77.90  ? 66  LYS D C   1 
ATOM   4386 O  O   . LYS D 2 65  ? 157.594 196.744 29.512  1.00 93.28  ? 66  LYS D O   1 
ATOM   4387 C  CB  . LYS D 2 65  ? 160.154 197.612 30.477  1.00 80.43  ? 66  LYS D CB  1 
ATOM   4388 C  CG  . LYS D 2 65  ? 161.390 198.069 31.246  1.00 90.27  ? 66  LYS D CG  1 
ATOM   4389 C  CD  . LYS D 2 65  ? 162.672 197.511 30.662  1.00 99.22  ? 66  LYS D CD  1 
ATOM   4390 C  CE  . LYS D 2 65  ? 163.898 198.083 31.363  1.00 108.07 ? 66  LYS D CE  1 
ATOM   4391 N  NZ  . LYS D 2 65  ? 163.976 197.702 32.803  1.00 105.65 1 66  LYS D NZ  1 
ATOM   4392 N  N   . ASP D 2 66  ? 156.608 198.024 31.068  1.00 81.42  ? 67  ASP D N   1 
ATOM   4393 C  CA  . ASP D 2 66  ? 155.309 198.080 30.411  1.00 87.22  ? 67  ASP D CA  1 
ATOM   4394 C  C   . ASP D 2 66  ? 155.342 199.004 29.202  1.00 88.11  ? 67  ASP D C   1 
ATOM   4395 O  O   . ASP D 2 66  ? 155.672 200.185 29.311  1.00 91.39  ? 67  ASP D O   1 
ATOM   4396 C  CB  . ASP D 2 66  ? 154.223 198.540 31.382  1.00 92.32  ? 67  ASP D CB  1 
ATOM   4397 C  CG  . ASP D 2 66  ? 152.829 198.372 30.810  1.00 95.40  ? 67  ASP D CG  1 
ATOM   4398 O  OD1 . ASP D 2 66  ? 152.696 197.690 29.771  1.00 96.98  ? 67  ASP D OD1 1 
ATOM   4399 O  OD2 . ASP D 2 66  ? 151.870 198.925 31.389  1.00 91.52  1 67  ASP D OD2 1 
ATOM   4400 N  N   . ALA D 2 67  ? 154.975 198.461 28.051  1.00 81.99  ? 68  ALA D N   1 
ATOM   4401 C  CA  . ALA D 2 67  ? 155.032 199.205 26.813  1.00 71.30  ? 68  ALA D CA  1 
ATOM   4402 C  C   . ALA D 2 67  ? 153.701 199.078 26.103  1.00 76.03  ? 68  ALA D C   1 
ATOM   4403 O  O   . ALA D 2 67  ? 153.111 198.000 26.058  1.00 67.73  ? 68  ALA D O   1 
ATOM   4404 C  CB  . ALA D 2 67  ? 156.156 198.698 25.939  1.00 73.10  ? 68  ALA D CB  1 
ATOM   4405 N  N   . ILE D 2 68  ? 153.217 200.193 25.567  1.00 73.59  ? 69  ILE D N   1 
ATOM   4406 C  CA  . ILE D 2 68  ? 151.962 200.191 24.840  1.00 66.16  ? 69  ILE D CA  1 
ATOM   4407 C  C   . ILE D 2 68  ? 152.179 200.458 23.363  1.00 64.42  ? 69  ILE D C   1 
ATOM   4408 O  O   . ILE D 2 68  ? 153.145 201.105 22.964  1.00 61.41  ? 69  ILE D O   1 
ATOM   4409 C  CB  . ILE D 2 68  ? 150.975 201.250 25.369  1.00 63.04  ? 69  ILE D CB  1 
ATOM   4410 C  CG1 . ILE D 2 68  ? 151.541 202.655 25.165  1.00 62.78  ? 69  ILE D CG1 1 
ATOM   4411 C  CG2 . ILE D 2 68  ? 150.610 200.973 26.815  1.00 71.55  ? 69  ILE D CG2 1 
ATOM   4412 C  CD1 . ILE D 2 68  ? 150.479 203.692 24.855  1.00 73.45  ? 69  ILE D CD1 1 
ATOM   4413 N  N   . ILE D 2 69  ? 151.263 199.953 22.552  1.00 60.04  ? 70  ILE D N   1 
ATOM   4414 C  CA  . ILE D 2 69  ? 151.237 200.323 21.160  1.00 57.58  ? 70  ILE D CA  1 
ATOM   4415 C  C   . ILE D 2 69  ? 150.896 201.817 21.083  1.00 54.86  ? 70  ILE D C   1 
ATOM   4416 O  O   . ILE D 2 69  ? 150.050 202.337 21.817  1.00 53.42  ? 70  ILE D O   1 
ATOM   4417 C  CB  . ILE D 2 69  ? 150.237 199.453 20.355  1.00 58.58  ? 70  ILE D CB  1 
ATOM   4418 C  CG1 . ILE D 2 69  ? 150.768 199.243 18.944  1.00 60.56  ? 70  ILE D CG1 1 
ATOM   4419 C  CG2 . ILE D 2 69  ? 148.806 200.059 20.344  1.00 52.07  ? 70  ILE D CG2 1 
ATOM   4420 C  CD1 . ILE D 2 69  ? 152.072 198.527 18.921  1.00 73.66  ? 70  ILE D CD1 1 
ATOM   4421 N  N   . ARG D 2 70  ? 151.614 202.523 20.232  1.00 52.72  ? 71  ARG D N   1 
ATOM   4422 C  CA  . ARG D 2 70  ? 151.400 203.944 20.109  1.00 59.25  ? 71  ARG D CA  1 
ATOM   4423 C  C   . ARG D 2 70  ? 151.317 204.304 18.636  1.00 50.69  ? 71  ARG D C   1 
ATOM   4424 O  O   . ARG D 2 70  ? 151.679 203.505 17.773  1.00 53.24  ? 71  ARG D O   1 
ATOM   4425 C  CB  . ARG D 2 70  ? 152.508 204.720 20.811  1.00 61.30  ? 71  ARG D CB  1 
ATOM   4426 C  CG  . ARG D 2 70  ? 152.048 206.063 21.322  1.00 62.30  ? 71  ARG D CG  1 
ATOM   4427 C  CD  . ARG D 2 70  ? 153.128 206.770 22.103  1.00 71.22  ? 71  ARG D CD  1 
ATOM   4428 N  NE  . ARG D 2 70  ? 153.164 208.180 21.752  1.00 63.28  ? 71  ARG D NE  1 
ATOM   4429 C  CZ  . ARG D 2 70  ? 153.473 208.612 20.537  1.00 69.66  ? 71  ARG D CZ  1 
ATOM   4430 N  NH1 . ARG D 2 70  ? 153.786 207.738 19.585  1.00 71.14  1 71  ARG D NH1 1 
ATOM   4431 N  NH2 . ARG D 2 70  ? 153.483 209.911 20.272  1.00 75.40  ? 71  ARG D NH2 1 
ATOM   4432 N  N   . GLY D 2 71  ? 150.822 205.498 18.343  1.00 49.26  ? 72  GLY D N   1 
ATOM   4433 C  CA  . GLY D 2 71  ? 150.705 205.921 16.965  1.00 54.53  ? 72  GLY D CA  1 
ATOM   4434 C  C   . GLY D 2 71  ? 152.037 206.431 16.436  1.00 70.07  ? 72  GLY D C   1 
ATOM   4435 O  O   . GLY D 2 71  ? 152.794 207.117 17.137  1.00 68.41  ? 72  GLY D O   1 
ATOM   4436 N  N   . ALA D 2 72  ? 152.322 206.090 15.186  1.00 64.60  ? 73  ALA D N   1 
ATOM   4437 C  CA  . ALA D 2 72  ? 153.413 206.712 14.466  1.00 74.80  ? 73  ALA D CA  1 
ATOM   4438 C  C   . ALA D 2 72  ? 153.003 208.141 14.119  1.00 80.10  ? 73  ALA D C   1 
ATOM   4439 O  O   . ALA D 2 72  ? 151.910 208.590 14.480  1.00 81.70  ? 73  ALA D O   1 
ATOM   4440 C  CB  . ALA D 2 72  ? 153.756 205.913 13.205  1.00 77.00  ? 73  ALA D CB  1 
ATOM   4441 N  N   . GLY D 2 73  ? 153.861 208.849 13.395  1.00 82.57  ? 74  GLY D N   1 
ATOM   4442 C  CA  . GLY D 2 73  ? 153.550 210.208 12.992  1.00 88.35  ? 74  GLY D CA  1 
ATOM   4443 C  C   . GLY D 2 73  ? 152.700 210.252 11.735  1.00 85.08  ? 74  GLY D C   1 
ATOM   4444 O  O   . GLY D 2 73  ? 152.085 211.284 11.437  1.00 75.88  ? 74  GLY D O   1 
ATOM   4445 N  N   . LYS D 2 74  ? 152.644 209.120 11.031  1.00 78.33  ? 75  LYS D N   1 
ATOM   4446 C  CA  . LYS D 2 74  ? 151.884 208.989 9.792   1.00 78.47  ? 75  LYS D CA  1 
ATOM   4447 C  C   . LYS D 2 74  ? 150.488 209.607 9.979   1.00 79.47  ? 75  LYS D C   1 
ATOM   4448 O  O   . LYS D 2 74  ? 149.814 209.338 10.979  1.00 78.63  ? 75  LYS D O   1 
ATOM   4449 C  CB  . LYS D 2 74  ? 151.780 207.507 9.392   1.00 78.40  ? 75  LYS D CB  1 
ATOM   4450 C  CG  . LYS D 2 74  ? 153.101 206.823 8.975   1.00 87.91  ? 75  LYS D CG  1 
ATOM   4451 C  CD  . LYS D 2 74  ? 153.134 205.299 9.318   1.00 88.91  ? 75  LYS D CD  1 
ATOM   4452 C  CE  . LYS D 2 74  ? 151.978 204.438 8.755   1.00 81.35  ? 75  LYS D CE  1 
ATOM   4453 N  NZ  . LYS D 2 74  ? 152.081 204.074 7.316   1.00 86.69  1 75  LYS D NZ  1 
ATOM   4454 N  N   . PRO D 2 75  ? 150.075 210.483 9.048   1.00 65.92  ? 76  PRO D N   1 
ATOM   4455 C  CA  . PRO D 2 75  ? 148.798 211.204 9.162   1.00 74.56  ? 76  PRO D CA  1 
ATOM   4456 C  C   . PRO D 2 75  ? 147.593 210.296 8.884   1.00 67.50  ? 76  PRO D C   1 
ATOM   4457 O  O   . PRO D 2 75  ? 147.662 209.467 7.971   1.00 59.90  ? 76  PRO D O   1 
ATOM   4458 C  CB  . PRO D 2 75  ? 148.908 212.307 8.102   1.00 78.31  ? 76  PRO D CB  1 
ATOM   4459 C  CG  . PRO D 2 75  ? 150.005 211.889 7.178   1.00 73.19  ? 76  PRO D CG  1 
ATOM   4460 C  CD  . PRO D 2 75  ? 150.792 210.773 7.794   1.00 67.39  ? 76  PRO D CD  1 
ATOM   4461 N  N   . ASN D 2 76  ? 146.518 210.450 9.655   1.00 56.89  ? 77  ASN D N   1 
ATOM   4462 C  CA  . ASN D 2 76  ? 145.341 209.576 9.547   1.00 59.86  ? 77  ASN D CA  1 
ATOM   4463 C  C   . ASN D 2 76  ? 145.730 208.097 9.615   1.00 52.76  ? 77  ASN D C   1 
ATOM   4464 O  O   . ASN D 2 76  ? 145.243 207.288 8.829   1.00 54.32  ? 77  ASN D O   1 
ATOM   4465 C  CB  . ASN D 2 76  ? 144.545 209.851 8.256   1.00 49.71  ? 77  ASN D CB  1 
ATOM   4466 C  CG  . ASN D 2 76  ? 143.141 209.189 8.261   1.00 64.72  ? 77  ASN D CG  1 
ATOM   4467 O  OD1 . ASN D 2 76  ? 142.707 208.621 9.269   1.00 53.61  ? 77  ASN D OD1 1 
ATOM   4468 N  ND2 . ASN D 2 76  ? 142.437 209.271 7.131   1.00 62.41  ? 77  ASN D ND2 1 
ATOM   4469 N  N   . SER D 2 77  ? 146.627 207.761 10.542  1.00 45.89  ? 78  SER D N   1 
ATOM   4470 C  CA  . SER D 2 77  ? 147.106 206.391 10.706  1.00 48.75  ? 78  SER D CA  1 
ATOM   4471 C  C   . SER D 2 77  ? 146.677 205.761 12.031  1.00 47.02  ? 78  SER D C   1 
ATOM   4472 O  O   . SER D 2 77  ? 146.854 204.572 12.232  1.00 44.81  ? 78  SER D O   1 
ATOM   4473 C  CB  . SER D 2 77  ? 148.634 206.341 10.576  1.00 55.85  ? 78  SER D CB  1 
ATOM   4474 O  OG  . SER D 2 77  ? 149.283 207.055 11.622  1.00 62.44  ? 78  SER D OG  1 
ATOM   4475 N  N   . SER D 2 78  ? 146.184 206.575 12.957  1.00 42.12  ? 79  SER D N   1 
ATOM   4476 C  CA  . SER D 2 78  ? 145.777 206.099 14.280  1.00 41.65  ? 79  SER D CA  1 
ATOM   4477 C  C   . SER D 2 78  ? 144.299 206.377 14.492  1.00 44.94  ? 79  SER D C   1 
ATOM   4478 O  O   . SER D 2 78  ? 143.777 207.381 14.011  1.00 41.87  ? 79  SER D O   1 
ATOM   4479 C  CB  . SER D 2 78  ? 146.595 206.747 15.401  1.00 39.39  ? 79  SER D CB  1 
ATOM   4480 O  OG  . SER D 2 78  ? 147.938 206.311 15.357  1.00 58.11  ? 79  SER D OG  1 
ATOM   4481 N  N   . ALA D 2 79  ? 143.616 205.461 15.173  1.00 39.75  ? 80  ALA D N   1 
ATOM   4482 C  CA  . ALA D 2 79  ? 142.208 205.658 15.490  1.00 41.16  ? 80  ALA D CA  1 
ATOM   4483 C  C   . ALA D 2 79  ? 141.870 205.088 16.856  1.00 38.58  ? 80  ALA D C   1 
ATOM   4484 O  O   . ALA D 2 79  ? 142.619 204.288 17.415  1.00 40.25  ? 80  ALA D O   1 
ATOM   4485 C  CB  . ALA D 2 79  ? 141.321 205.028 14.412  1.00 30.72  ? 80  ALA D CB  1 
ATOM   4486 N  N   . VAL D 2 80  ? 140.724 205.481 17.383  1.00 40.64  ? 81  VAL D N   1 
ATOM   4487 C  CA  . VAL D 2 80  ? 140.278 204.927 18.640  1.00 34.74  ? 81  VAL D CA  1 
ATOM   4488 C  C   . VAL D 2 80  ? 138.757 204.708 18.574  1.00 37.32  ? 81  VAL D C   1 
ATOM   4489 O  O   . VAL D 2 80  ? 138.056 205.398 17.836  1.00 38.87  ? 81  VAL D O   1 
ATOM   4490 C  CB  . VAL D 2 80  ? 140.687 205.867 19.805  1.00 35.45  ? 81  VAL D CB  1 
ATOM   4491 C  CG1 . VAL D 2 80  ? 139.669 206.977 19.976  1.00 34.86  ? 81  VAL D CG1 1 
ATOM   4492 C  CG2 . VAL D 2 80  ? 140.831 205.108 21.078  1.00 41.21  ? 81  VAL D CG2 1 
ATOM   4493 N  N   . ALA D 2 81  ? 138.250 203.732 19.318  1.00 37.99  ? 82  ALA D N   1 
ATOM   4494 C  CA  . ALA D 2 81  ? 136.811 203.574 19.474  1.00 34.66  ? 82  ALA D CA  1 
ATOM   4495 C  C   . ALA D 2 81  ? 136.524 203.294 20.943  1.00 39.46  ? 82  ALA D C   1 
ATOM   4496 O  O   . ALA D 2 81  ? 137.066 202.350 21.513  1.00 40.29  ? 82  ALA D O   1 
ATOM   4497 C  CB  . ALA D 2 81  ? 136.272 202.458 18.590  1.00 34.05  ? 82  ALA D CB  1 
ATOM   4498 N  N   . ILE D 2 82  ? 135.727 204.154 21.564  1.00 33.59  ? 83  ILE D N   1 
ATOM   4499 C  CA  . ILE D 2 82  ? 135.304 203.947 22.929  1.00 33.84  ? 83  ILE D CA  1 
ATOM   4500 C  C   . ILE D 2 82  ? 134.021 203.121 22.905  1.00 39.19  ? 83  ILE D C   1 
ATOM   4501 O  O   . ILE D 2 82  ? 133.027 203.542 22.327  1.00 42.31  ? 83  ILE D O   1 
ATOM   4502 C  CB  . ILE D 2 82  ? 135.103 205.280 23.638  1.00 37.33  ? 83  ILE D CB  1 
ATOM   4503 C  CG1 . ILE D 2 82  ? 136.376 206.120 23.486  1.00 34.82  ? 83  ILE D CG1 1 
ATOM   4504 C  CG2 . ILE D 2 82  ? 134.753 205.063 25.104  1.00 32.13  ? 83  ILE D CG2 1 
ATOM   4505 C  CD1 . ILE D 2 82  ? 136.273 207.540 24.020  1.00 26.20  ? 83  ILE D CD1 1 
ATOM   4506 N  N   . LEU D 2 83  ? 134.051 201.941 23.517  1.00 37.23  ? 84  LEU D N   1 
ATOM   4507 C  CA  . LEU D 2 83  ? 132.941 200.997 23.409  1.00 38.82  ? 84  LEU D CA  1 
ATOM   4508 C  C   . LEU D 2 83  ? 131.966 201.094 24.586  1.00 41.80  ? 84  LEU D C   1 
ATOM   4509 O  O   . LEU D 2 83  ? 132.288 200.749 25.731  1.00 46.77  ? 84  LEU D O   1 
ATOM   4510 C  CB  . LEU D 2 83  ? 133.492 199.578 23.273  1.00 36.61  ? 84  LEU D CB  1 
ATOM   4511 C  CG  . LEU D 2 83  ? 134.644 199.507 22.268  1.00 33.44  ? 84  LEU D CG  1 
ATOM   4512 C  CD1 . LEU D 2 83  ? 135.330 198.162 22.252  1.00 32.22  ? 84  LEU D CD1 1 
ATOM   4513 C  CD2 . LEU D 2 83  ? 134.118 199.836 20.885  1.00 38.38  ? 84  LEU D CD2 1 
ATOM   4514 N  N   . GLU D 2 84  ? 130.756 201.540 24.276  1.00 39.77  ? 85  GLU D N   1 
ATOM   4515 C  CA  . GLU D 2 84  ? 129.730 201.790 25.275  1.00 42.22  ? 85  GLU D CA  1 
ATOM   4516 C  C   . GLU D 2 84  ? 128.514 200.903 25.016  1.00 49.03  ? 85  GLU D C   1 
ATOM   4517 O  O   . GLU D 2 84  ? 128.194 200.587 23.854  1.00 41.31  ? 85  GLU D O   1 
ATOM   4518 C  CB  . GLU D 2 84  ? 129.298 203.266 25.267  1.00 43.55  ? 85  GLU D CB  1 
ATOM   4519 C  CG  . GLU D 2 84  ? 130.280 204.227 25.929  1.00 56.09  ? 85  GLU D CG  1 
ATOM   4520 C  CD  . GLU D 2 84  ? 129.878 205.699 25.780  1.00 64.57  ? 85  GLU D CD  1 
ATOM   4521 O  OE1 . GLU D 2 84  ? 129.361 206.278 26.763  1.00 64.94  ? 85  GLU D OE1 1 
ATOM   4522 O  OE2 . GLU D 2 84  ? 130.092 206.280 24.690  1.00 66.44  1 85  GLU D OE2 1 
ATOM   4523 N  N   . THR D 2 85  ? 127.843 200.495 26.093  1.00 40.48  ? 86  THR D N   1 
ATOM   4524 C  CA  . THR D 2 85  ? 126.602 199.735 25.951  1.00 42.54  ? 86  THR D CA  1 
ATOM   4525 C  C   . THR D 2 85  ? 125.508 200.693 25.532  1.00 43.80  ? 86  THR D C   1 
ATOM   4526 O  O   . THR D 2 85  ? 125.548 201.870 25.889  1.00 53.16  ? 86  THR D O   1 
ATOM   4527 C  CB  . THR D 2 85  ? 126.179 199.001 27.259  1.00 45.60  ? 86  THR D CB  1 
ATOM   4528 O  OG1 . THR D 2 85  ? 125.852 199.944 28.293  1.00 46.28  ? 86  THR D OG1 1 
ATOM   4529 C  CG2 . THR D 2 85  ? 127.275 198.065 27.717  1.00 39.92  ? 86  THR D CG2 1 
ATOM   4530 N  N   . PHE D 2 86  ? 124.534 200.190 24.776  1.00 52.71  ? 87  PHE D N   1 
ATOM   4531 C  CA  . PHE D 2 86  ? 123.404 201.006 24.363  1.00 46.04  ? 87  PHE D CA  1 
ATOM   4532 C  C   . PHE D 2 86  ? 122.112 200.588 25.089  1.00 53.87  ? 87  PHE D C   1 
ATOM   4533 O  O   . PHE D 2 86  ? 121.397 201.434 25.619  1.00 51.73  ? 87  PHE D O   1 
ATOM   4534 C  CB  . PHE D 2 86  ? 123.211 200.924 22.852  1.00 42.17  ? 87  PHE D CB  1 
ATOM   4535 C  CG  . PHE D 2 86  ? 122.009 201.684 22.359  1.00 50.42  ? 87  PHE D CG  1 
ATOM   4536 C  CD1 . PHE D 2 86  ? 122.050 203.066 22.238  1.00 52.39  ? 87  PHE D CD1 1 
ATOM   4537 C  CD2 . PHE D 2 86  ? 120.830 201.023 22.035  1.00 49.91  ? 87  PHE D CD2 1 
ATOM   4538 C  CE1 . PHE D 2 86  ? 120.935 203.777 21.792  1.00 50.75  ? 87  PHE D CE1 1 
ATOM   4539 C  CE2 . PHE D 2 86  ? 119.719 201.717 21.587  1.00 52.69  ? 87  PHE D CE2 1 
ATOM   4540 C  CZ  . PHE D 2 86  ? 119.769 203.098 21.466  1.00 53.21  ? 87  PHE D CZ  1 
ATOM   4541 N  N   . GLN D 2 87  ? 121.828 199.290 25.159  1.00 53.64  ? 88  GLN D N   1 
ATOM   4542 C  CA  . GLN D 2 87  ? 120.646 198.856 25.898  1.00 55.53  ? 88  GLN D CA  1 
ATOM   4543 C  C   . GLN D 2 87  ? 120.869 198.754 27.415  1.00 59.97  ? 88  GLN D C   1 
ATOM   4544 O  O   . GLN D 2 87  ? 121.991 198.594 27.896  1.00 57.84  ? 88  GLN D O   1 
ATOM   4545 C  CB  . GLN D 2 87  ? 120.157 197.526 25.344  1.00 47.85  ? 88  GLN D CB  1 
ATOM   4546 C  CG  . GLN D 2 87  ? 119.051 197.726 24.352  1.00 61.11  ? 88  GLN D CG  1 
ATOM   4547 C  CD  . GLN D 2 87  ? 119.209 196.864 23.142  1.00 76.47  ? 88  GLN D CD  1 
ATOM   4548 O  OE1 . GLN D 2 87  ? 120.116 196.040 23.074  1.00 73.79  ? 88  GLN D OE1 1 
ATOM   4549 N  NE2 . GLN D 2 87  ? 118.345 197.065 22.155  1.00 82.55  ? 88  GLN D NE2 1 
ATOM   4550 N  N   . LYS D 2 88  ? 119.790 198.846 28.177  1.00 65.22  ? 89  LYS D N   1 
ATOM   4551 C  CA  . LYS D 2 88  ? 119.908 198.633 29.609  1.00 62.87  ? 89  LYS D CA  1 
ATOM   4552 C  C   . LYS D 2 88  ? 119.745 197.153 29.860  1.00 61.76  ? 89  LYS D C   1 
ATOM   4553 O  O   . LYS D 2 88  ? 118.768 196.554 29.409  1.00 68.01  ? 89  LYS D O   1 
ATOM   4554 C  CB  . LYS D 2 88  ? 118.866 199.422 30.406  1.00 66.39  ? 89  LYS D CB  1 
ATOM   4555 C  CG  . LYS D 2 88  ? 119.005 199.203 31.917  1.00 85.04  ? 89  LYS D CG  1 
ATOM   4556 C  CD  . LYS D 2 88  ? 117.926 199.898 32.748  1.00 88.18  ? 89  LYS D CD  1 
ATOM   4557 C  CE  . LYS D 2 88  ? 117.990 199.418 34.211  1.00 98.51  ? 89  LYS D CE  1 
ATOM   4558 N  NZ  . LYS D 2 88  ? 116.910 199.976 35.084  1.00 70.72  1 89  LYS D NZ  1 
ATOM   4559 N  N   . TYR D 2 89  ? 120.708 196.556 30.553  1.00 61.20  ? 90  TYR D N   1 
ATOM   4560 C  CA  . TYR D 2 89  ? 120.619 195.134 30.863  1.00 66.57  ? 90  TYR D CA  1 
ATOM   4561 C  C   . TYR D 2 89  ? 120.343 194.931 32.353  1.00 66.80  ? 90  TYR D C   1 
ATOM   4562 O  O   . TYR D 2 89  ? 120.836 195.690 33.192  1.00 69.18  ? 90  TYR D O   1 
ATOM   4563 C  CB  . TYR D 2 89  ? 121.896 194.400 30.461  1.00 60.68  ? 90  TYR D CB  1 
ATOM   4564 C  CG  . TYR D 2 89  ? 122.237 194.428 28.974  1.00 61.88  ? 90  TYR D CG  1 
ATOM   4565 C  CD1 . TYR D 2 89  ? 121.751 193.456 28.104  1.00 53.73  ? 90  TYR D CD1 1 
ATOM   4566 C  CD2 . TYR D 2 89  ? 123.085 195.407 28.449  1.00 53.49  ? 90  TYR D CD2 1 
ATOM   4567 C  CE1 . TYR D 2 89  ? 122.086 193.470 26.739  1.00 54.27  ? 90  TYR D CE1 1 
ATOM   4568 C  CE2 . TYR D 2 89  ? 123.424 195.430 27.100  1.00 54.85  ? 90  TYR D CE2 1 
ATOM   4569 C  CZ  . TYR D 2 89  ? 122.923 194.461 26.249  1.00 53.40  ? 90  TYR D CZ  1 
ATOM   4570 O  OH  . TYR D 2 89  ? 123.263 194.490 24.915  1.00 47.33  ? 90  TYR D OH  1 
ATOM   4571 N  N   . THR D 2 90  ? 119.514 193.938 32.667  1.00 72.19  ? 91  THR D N   1 
ATOM   4572 C  CA  . THR D 2 90  ? 119.252 193.541 34.051  1.00 67.88  ? 91  THR D CA  1 
ATOM   4573 C  C   . THR D 2 90  ? 120.566 193.173 34.729  1.00 71.32  ? 91  THR D C   1 
ATOM   4574 O  O   . THR D 2 90  ? 120.885 193.632 35.832  1.00 73.85  ? 91  THR D O   1 
ATOM   4575 C  CB  . THR D 2 90  ? 118.307 192.320 34.119  1.00 75.77  ? 91  THR D CB  1 
ATOM   4576 O  OG1 . THR D 2 90  ? 117.109 192.587 33.383  1.00 74.60  ? 91  THR D OG1 1 
ATOM   4577 C  CG2 . THR D 2 90  ? 117.963 191.968 35.561  1.00 80.28  ? 91  THR D CG2 1 
ATOM   4578 N  N   . ILE D 2 91  ? 121.342 192.363 34.016  1.00 69.69  ? 92  ILE D N   1 
ATOM   4579 C  CA  . ILE D 2 91  ? 122.594 191.818 34.514  1.00 65.22  ? 92  ILE D CA  1 
ATOM   4580 C  C   . ILE D 2 91  ? 123.708 192.849 34.613  1.00 66.49  ? 92  ILE D C   1 
ATOM   4581 O  O   . ILE D 2 91  ? 124.758 192.590 35.208  1.00 66.97  ? 92  ILE D O   1 
ATOM   4582 C  CB  . ILE D 2 91  ? 123.064 190.673 33.607  1.00 63.90  ? 92  ILE D CB  1 
ATOM   4583 C  CG1 . ILE D 2 91  ? 123.261 191.191 32.188  1.00 63.59  ? 92  ILE D CG1 1 
ATOM   4584 C  CG2 . ILE D 2 91  ? 122.028 189.582 33.558  1.00 62.50  ? 92  ILE D CG2 1 
ATOM   4585 C  CD1 . ILE D 2 91  ? 123.863 190.180 31.250  1.00 66.70  ? 92  ILE D CD1 1 
ATOM   4586 N  N   . ASP D 2 92  ? 123.501 194.015 34.018  1.00 68.06  ? 93  ASP D N   1 
ATOM   4587 C  CA  . ASP D 2 92  ? 124.540 195.024 34.056  1.00 66.32  ? 93  ASP D CA  1 
ATOM   4588 C  C   . ASP D 2 92  ? 124.085 196.153 34.950  1.00 73.84  ? 93  ASP D C   1 
ATOM   4589 O  O   . ASP D 2 92  ? 123.335 197.030 34.520  1.00 78.46  ? 93  ASP D O   1 
ATOM   4590 C  CB  . ASP D 2 92  ? 124.872 195.532 32.655  1.00 67.58  ? 93  ASP D CB  1 
ATOM   4591 C  CG  . ASP D 2 92  ? 126.256 196.174 32.579  1.00 74.26  ? 93  ASP D CG  1 
ATOM   4592 O  OD1 . ASP D 2 92  ? 126.728 196.720 33.603  1.00 61.72  ? 93  ASP D OD1 1 
ATOM   4593 O  OD2 . ASP D 2 92  ? 126.882 196.110 31.492  1.00 67.63  1 93  ASP D OD2 1 
ATOM   4594 N  N   . GLN D 2 93  ? 124.548 196.139 36.194  1.00 67.64  ? 94  GLN D N   1 
ATOM   4595 C  CA  . GLN D 2 93  ? 124.114 197.135 37.162  1.00 75.75  ? 94  GLN D CA  1 
ATOM   4596 C  C   . GLN D 2 93  ? 125.202 198.178 37.402  1.00 81.63  ? 94  GLN D C   1 
ATOM   4597 O  O   . GLN D 2 93  ? 125.090 199.003 38.312  1.00 80.97  ? 94  GLN D O   1 
ATOM   4598 C  CB  . GLN D 2 93  ? 123.686 196.468 38.476  1.00 83.93  ? 94  GLN D CB  1 
ATOM   4599 C  CG  . GLN D 2 93  ? 122.430 195.582 38.357  1.00 73.26  ? 94  GLN D CG  1 
ATOM   4600 C  CD  . GLN D 2 93  ? 121.181 196.354 37.905  1.00 82.54  ? 94  GLN D CD  1 
ATOM   4601 O  OE1 . GLN D 2 93  ? 121.055 197.563 38.136  1.00 85.99  ? 94  GLN D OE1 1 
ATOM   4602 N  NE2 . GLN D 2 93  ? 120.259 195.654 37.247  1.00 79.31  ? 94  GLN D NE2 1 
ATOM   4603 N  N   . LYS D 2 94  ? 126.259 198.127 36.589  1.00 78.04  ? 95  LYS D N   1 
ATOM   4604 C  CA  . LYS D 2 94  ? 127.278 199.181 36.583  1.00 77.13  ? 95  LYS D CA  1 
ATOM   4605 C  C   . LYS D 2 94  ? 126.702 200.438 35.929  1.00 71.45  ? 95  LYS D C   1 
ATOM   4606 O  O   . LYS D 2 94  ? 126.629 200.525 34.703  1.00 75.43  ? 95  LYS D O   1 
ATOM   4607 C  CB  . LYS D 2 94  ? 128.545 198.727 35.838  1.00 69.29  ? 95  LYS D CB  1 
ATOM   4608 C  CG  . LYS D 2 94  ? 129.664 199.770 35.834  1.00 61.60  ? 95  LYS D CG  1 
ATOM   4609 C  CD  . LYS D 2 94  ? 130.966 199.209 35.298  1.00 59.79  ? 95  LYS D CD  1 
ATOM   4610 C  CE  . LYS D 2 94  ? 132.071 200.266 35.306  1.00 61.14  ? 95  LYS D CE  1 
ATOM   4611 N  NZ  . LYS D 2 94  ? 132.351 200.846 36.660  1.00 61.74  1 95  LYS D NZ  1 
ATOM   4612 N  N   . LYS D 2 95  ? 126.296 201.412 36.737  1.00 67.32  ? 96  LYS D N   1 
ATOM   4613 C  CA  . LYS D 2 95  ? 125.568 202.561 36.197  1.00 70.84  ? 96  LYS D CA  1 
ATOM   4614 C  C   . LYS D 2 95  ? 126.362 203.870 36.228  1.00 62.88  ? 96  LYS D C   1 
ATOM   4615 O  O   . LYS D 2 95  ? 125.842 204.923 35.851  1.00 73.50  ? 96  LYS D O   1 
ATOM   4616 C  CB  . LYS D 2 95  ? 124.243 202.744 36.947  1.00 78.23  ? 96  LYS D CB  1 
ATOM   4617 C  CG  . LYS D 2 95  ? 123.293 201.564 36.813  1.00 78.68  ? 96  LYS D CG  1 
ATOM   4618 C  CD  . LYS D 2 95  ? 122.960 201.285 35.361  1.00 83.12  ? 96  LYS D CD  1 
ATOM   4619 C  CE  . LYS D 2 95  ? 122.292 199.916 35.187  1.00 92.17  ? 96  LYS D CE  1 
ATOM   4620 N  NZ  . LYS D 2 95  ? 120.967 199.774 35.882  1.00 90.16  1 96  LYS D NZ  1 
ATOM   4621 N  N   . ASP D 2 96  ? 127.613 203.812 36.670  1.00 62.34  ? 97  ASP D N   1 
ATOM   4622 C  CA  . ASP D 2 96  ? 128.453 205.012 36.737  1.00 72.47  ? 97  ASP D CA  1 
ATOM   4623 C  C   . ASP D 2 96  ? 129.012 205.369 35.359  1.00 63.34  ? 97  ASP D C   1 
ATOM   4624 O  O   . ASP D 2 96  ? 129.414 206.503 35.125  1.00 67.84  ? 97  ASP D O   1 
ATOM   4625 C  CB  . ASP D 2 96  ? 129.594 204.830 37.749  1.00 62.83  ? 97  ASP D CB  1 
ATOM   4626 C  CG  . ASP D 2 96  ? 130.475 203.623 37.439  1.00 71.66  ? 97  ASP D CG  1 
ATOM   4627 O  OD1 . ASP D 2 96  ? 130.015 202.696 36.729  1.00 58.55  ? 97  ASP D OD1 1 
ATOM   4628 O  OD2 . ASP D 2 96  ? 131.632 203.600 37.918  1.00 71.48  1 97  ASP D OD2 1 
ATOM   4629 N  N   . THR D 2 97  ? 129.075 204.381 34.473  1.00 61.04  ? 98  THR D N   1 
ATOM   4630 C  CA  . THR D 2 97  ? 129.474 204.588 33.086  1.00 50.53  ? 98  THR D CA  1 
ATOM   4631 C  C   . THR D 2 97  ? 129.002 203.440 32.213  1.00 52.89  ? 98  THR D C   1 
ATOM   4632 O  O   . THR D 2 97  ? 128.946 202.292 32.660  1.00 54.08  ? 98  THR D O   1 
ATOM   4633 C  CB  . THR D 2 97  ? 130.996 204.720 32.953  1.00 56.64  ? 98  THR D CB  1 
ATOM   4634 O  OG1 . THR D 2 97  ? 131.337 204.917 31.572  1.00 51.71  ? 98  THR D OG1 1 
ATOM   4635 C  CG2 . THR D 2 97  ? 131.690 203.449 33.480  1.00 49.54  ? 98  THR D CG2 1 
ATOM   4636 N  N   . ALA D 2 98  ? 128.704 203.727 30.952  1.00 52.18  ? 99  ALA D N   1 
ATOM   4637 C  CA  . ALA D 2 98  ? 128.310 202.655 30.054  1.00 40.07  ? 99  ALA D CA  1 
ATOM   4638 C  C   . ALA D 2 98  ? 129.514 202.119 29.278  1.00 40.12  ? 99  ALA D C   1 
ATOM   4639 O  O   . ALA D 2 98  ? 129.392 201.181 28.504  1.00 45.38  ? 99  ALA D O   1 
ATOM   4640 C  CB  . ALA D 2 98  ? 127.242 203.125 29.121  1.00 40.92  ? 99  ALA D CB  1 
ATOM   4641 N  N   . VAL D 2 99  ? 130.677 202.718 29.496  1.00 40.89  ? 100 VAL D N   1 
ATOM   4642 C  CA  . VAL D 2 99  ? 131.904 202.240 28.870  1.00 40.58  ? 100 VAL D CA  1 
ATOM   4643 C  C   . VAL D 2 99  ? 132.274 200.839 29.383  1.00 47.92  ? 100 VAL D C   1 
ATOM   4644 O  O   . VAL D 2 99  ? 132.335 200.603 30.601  1.00 43.07  ? 100 VAL D O   1 
ATOM   4645 C  CB  . VAL D 2 99  ? 133.069 203.224 29.131  1.00 39.64  ? 100 VAL D CB  1 
ATOM   4646 C  CG1 . VAL D 2 99  ? 134.395 202.659 28.621  1.00 38.65  ? 100 VAL D CG1 1 
ATOM   4647 C  CG2 . VAL D 2 99  ? 132.771 204.587 28.499  1.00 35.94  ? 100 VAL D CG2 1 
ATOM   4648 N  N   . ARG D 2 100 ? 132.513 199.916 28.454  1.00 42.79  ? 101 ARG D N   1 
ATOM   4649 C  CA  . ARG D 2 100 ? 132.925 198.554 28.802  1.00 44.39  ? 101 ARG D CA  1 
ATOM   4650 C  C   . ARG D 2 100 ? 134.251 198.192 28.131  1.00 46.60  ? 101 ARG D C   1 
ATOM   4651 O  O   . ARG D 2 100 ? 134.923 197.239 28.537  1.00 44.65  ? 101 ARG D O   1 
ATOM   4652 C  CB  . ARG D 2 100 ? 131.848 197.526 28.410  1.00 41.24  ? 101 ARG D CB  1 
ATOM   4653 C  CG  . ARG D 2 100 ? 130.509 197.731 29.095  1.00 43.90  ? 101 ARG D CG  1 
ATOM   4654 C  CD  . ARG D 2 100 ? 130.608 197.464 30.607  1.00 44.85  ? 101 ARG D CD  1 
ATOM   4655 N  NE  . ARG D 2 100 ? 129.399 197.909 31.285  1.00 49.90  ? 101 ARG D NE  1 
ATOM   4656 C  CZ  . ARG D 2 100 ? 129.245 199.112 31.840  1.00 55.84  ? 101 ARG D CZ  1 
ATOM   4657 N  NH1 . ARG D 2 100 ? 130.234 200.006 31.811  1.00 52.44  1 101 ARG D NH1 1 
ATOM   4658 N  NH2 . ARG D 2 100 ? 128.098 199.427 32.432  1.00 51.70  ? 101 ARG D NH2 1 
ATOM   4659 N  N   . GLY D 2 101 ? 134.630 198.962 27.113  1.00 41.08  ? 102 GLY D N   1 
ATOM   4660 C  CA  . GLY D 2 101 ? 135.800 198.623 26.325  1.00 38.65  ? 102 GLY D CA  1 
ATOM   4661 C  C   . GLY D 2 101 ? 136.446 199.769 25.551  1.00 42.00  ? 102 GLY D C   1 
ATOM   4662 O  O   . GLY D 2 101 ? 135.885 200.860 25.378  1.00 36.52  ? 102 GLY D O   1 
ATOM   4663 N  N   . LEU D 2 102 ? 137.659 199.500 25.092  1.00 42.52  ? 103 LEU D N   1 
ATOM   4664 C  CA  . LEU D 2 102 ? 138.447 200.476 24.367  1.00 39.18  ? 103 LEU D CA  1 
ATOM   4665 C  C   . LEU D 2 102 ? 139.190 199.800 23.237  1.00 34.11  ? 103 LEU D C   1 
ATOM   4666 O  O   . LEU D 2 102 ? 139.799 198.744 23.424  1.00 40.80  ? 103 LEU D O   1 
ATOM   4667 C  CB  . LEU D 2 102 ? 139.410 201.185 25.319  1.00 38.54  ? 103 LEU D CB  1 
ATOM   4668 C  CG  . LEU D 2 102 ? 140.295 202.247 24.687  1.00 43.29  ? 103 LEU D CG  1 
ATOM   4669 C  CD1 . LEU D 2 102 ? 139.392 203.361 24.149  1.00 34.53  ? 103 LEU D CD1 1 
ATOM   4670 C  CD2 . LEU D 2 102 ? 141.260 202.785 25.743  1.00 35.27  ? 103 LEU D CD2 1 
ATOM   4671 N  N   . ALA D 2 103 ? 139.079 200.366 22.046  1.00 37.72  ? 104 ALA D N   1 
ATOM   4672 C  CA  . ALA D 2 103 ? 139.863 199.899 20.911  1.00 32.35  ? 104 ALA D CA  1 
ATOM   4673 C  C   . ALA D 2 103 ? 140.864 200.986 20.539  1.00 35.96  ? 104 ALA D C   1 
ATOM   4674 O  O   . ALA D 2 103 ? 140.486 202.136 20.274  1.00 37.18  ? 104 ALA D O   1 
ATOM   4675 C  CB  . ALA D 2 103 ? 138.951 199.540 19.723  1.00 31.98  ? 104 ALA D CB  1 
ATOM   4676 N  N   . ARG D 2 104 ? 142.147 200.649 20.577  1.00 39.08  ? 105 ARG D N   1 
ATOM   4677 C  CA  . ARG D 2 104 ? 143.162 201.534 20.024  1.00 36.94  ? 105 ARG D CA  1 
ATOM   4678 C  C   . ARG D 2 104 ? 143.641 200.945 18.723  1.00 39.86  ? 105 ARG D C   1 
ATOM   4679 O  O   . ARG D 2 104 ? 144.002 199.772 18.672  1.00 43.46  ? 105 ARG D O   1 
ATOM   4680 C  CB  . ARG D 2 104 ? 144.320 201.722 20.990  1.00 43.76  ? 105 ARG D CB  1 
ATOM   4681 C  CG  . ARG D 2 104 ? 144.024 202.700 22.099  1.00 40.39  ? 105 ARG D CG  1 
ATOM   4682 C  CD  . ARG D 2 104 ? 145.037 202.538 23.219  1.00 44.39  ? 105 ARG D CD  1 
ATOM   4683 N  NE  . ARG D 2 104 ? 144.852 203.517 24.284  1.00 45.42  ? 105 ARG D NE  1 
ATOM   4684 C  CZ  . ARG D 2 104 ? 145.643 203.626 25.348  1.00 54.23  ? 105 ARG D CZ  1 
ATOM   4685 N  NH1 . ARG D 2 104 ? 146.684 202.812 25.488  1.00 54.50  1 105 ARG D NH1 1 
ATOM   4686 N  NH2 . ARG D 2 104 ? 145.398 204.557 26.269  1.00 53.92  ? 105 ARG D NH2 1 
ATOM   4687 N  N   . ILE D 2 105 ? 143.627 201.754 17.670  1.00 44.40  ? 106 ILE D N   1 
ATOM   4688 C  CA  . ILE D 2 105 ? 143.924 201.287 16.315  1.00 35.63  ? 106 ILE D CA  1 
ATOM   4689 C  C   . ILE D 2 105 ? 145.125 202.028 15.709  1.00 41.04  ? 106 ILE D C   1 
ATOM   4690 O  O   . ILE D 2 105 ? 145.172 203.256 15.698  1.00 41.94  ? 106 ILE D O   1 
ATOM   4691 C  CB  . ILE D 2 105 ? 142.707 201.474 15.372  1.00 40.75  ? 106 ILE D CB  1 
ATOM   4692 C  CG1 . ILE D 2 105 ? 141.414 200.933 16.005  1.00 38.51  ? 106 ILE D CG1 1 
ATOM   4693 C  CG2 . ILE D 2 105 ? 142.985 200.851 13.998  1.00 35.62  ? 106 ILE D CG2 1 
ATOM   4694 C  CD1 . ILE D 2 105 ? 140.180 201.127 15.102  1.00 37.14  ? 106 ILE D CD1 1 
ATOM   4695 N  N   . VAL D 2 106 ? 146.094 201.282 15.197  1.00 40.57  ? 107 VAL D N   1 
ATOM   4696 C  CA  . VAL D 2 106 ? 147.208 201.903 14.499  1.00 42.93  ? 107 VAL D CA  1 
ATOM   4697 C  C   . VAL D 2 106 ? 147.391 201.225 13.163  1.00 46.39  ? 107 VAL D C   1 
ATOM   4698 O  O   . VAL D 2 106 ? 147.185 200.020 13.040  1.00 48.91  ? 107 VAL D O   1 
ATOM   4699 C  CB  . VAL D 2 106 ? 148.516 201.849 15.301  1.00 38.70  ? 107 VAL D CB  1 
ATOM   4700 C  CG1 . VAL D 2 106 ? 148.389 202.707 16.560  1.00 38.04  ? 107 VAL D CG1 1 
ATOM   4701 C  CG2 . VAL D 2 106 ? 148.877 200.413 15.657  1.00 45.54  ? 107 VAL D CG2 1 
ATOM   4702 N  N   . GLN D 2 107 ? 147.714 202.012 12.144  1.00 46.07  ? 108 GLN D N   1 
ATOM   4703 C  CA  . GLN D 2 107 ? 148.062 201.426 10.867  1.00 49.84  ? 108 GLN D CA  1 
ATOM   4704 C  C   . GLN D 2 107 ? 149.454 200.879 11.031  1.00 55.14  ? 108 GLN D C   1 
ATOM   4705 O  O   . GLN D 2 107 ? 150.357 201.563 11.518  1.00 58.12  ? 108 GLN D O   1 
ATOM   4706 C  CB  . GLN D 2 107 ? 147.997 202.421 9.715   1.00 45.28  ? 108 GLN D CB  1 
ATOM   4707 C  CG  . GLN D 2 107 ? 148.287 201.764 8.381   1.00 46.90  ? 108 GLN D CG  1 
ATOM   4708 C  CD  . GLN D 2 107 ? 147.730 202.546 7.220   1.00 61.19  ? 108 GLN D CD  1 
ATOM   4709 O  OE1 . GLN D 2 107 ? 146.647 203.126 7.312   1.00 56.08  ? 108 GLN D OE1 1 
ATOM   4710 N  NE2 . GLN D 2 107 ? 148.475 202.585 6.120   1.00 75.02  ? 108 GLN D NE2 1 
ATOM   4711 N  N   . VAL D 2 108 ? 149.615 199.620 10.659  1.00 57.92  ? 109 VAL D N   1 
ATOM   4712 C  CA  . VAL D 2 108 ? 150.839 198.928 10.963  1.00 65.39  ? 109 VAL D CA  1 
ATOM   4713 C  C   . VAL D 2 108 ? 151.486 198.431 9.665   1.00 69.88  ? 109 VAL D C   1 
ATOM   4714 O  O   . VAL D 2 108 ? 152.591 197.891 9.664   1.00 86.98  ? 109 VAL D O   1 
ATOM   4715 C  CB  . VAL D 2 108 ? 150.544 197.770 11.934  1.00 62.55  ? 109 VAL D CB  1 
ATOM   4716 C  CG1 . VAL D 2 108 ? 150.025 196.563 11.174  1.00 57.62  ? 109 VAL D CG1 1 
ATOM   4717 C  CG2 . VAL D 2 108 ? 151.761 197.417 12.734  1.00 71.69  ? 109 VAL D CG2 1 
ATOM   4718 N  N   . GLY D 2 109 ? 150.801 198.645 8.553   1.00 64.93  ? 110 GLY D N   1 
ATOM   4719 C  CA  . GLY D 2 109 ? 151.278 198.175 7.269   1.00 70.59  ? 110 GLY D CA  1 
ATOM   4720 C  C   . GLY D 2 109 ? 150.812 199.133 6.208   1.00 70.59  ? 110 GLY D C   1 
ATOM   4721 O  O   . GLY D 2 109 ? 150.374 200.233 6.520   1.00 85.03  ? 110 GLY D O   1 
ATOM   4722 N  N   . GLU D 2 110 ? 150.900 198.732 4.952   1.00 68.94  ? 111 GLU D N   1 
ATOM   4723 C  CA  . GLU D 2 110 ? 150.367 199.577 3.902   1.00 76.03  ? 111 GLU D CA  1 
ATOM   4724 C  C   . GLU D 2 110 ? 148.864 199.330 3.810   1.00 69.84  ? 111 GLU D C   1 
ATOM   4725 O  O   . GLU D 2 110 ? 148.076 200.249 3.596   1.00 61.63  ? 111 GLU D O   1 
ATOM   4726 C  CB  . GLU D 2 110 ? 151.069 199.310 2.580   1.00 76.52  ? 111 GLU D CB  1 
ATOM   4727 C  CG  . GLU D 2 110 ? 150.604 200.206 1.463   1.00 82.63  ? 111 GLU D CG  1 
ATOM   4728 C  CD  . GLU D 2 110 ? 151.056 199.696 0.122   1.00 96.12  ? 111 GLU D CD  1 
ATOM   4729 O  OE1 . GLU D 2 110 ? 151.887 198.760 0.101   1.00 95.52  ? 111 GLU D OE1 1 
ATOM   4730 O  OE2 . GLU D 2 110 ? 150.570 200.212 -0.904  1.00 93.19  1 111 GLU D OE2 1 
ATOM   4731 N  N   . ASN D 2 111 ? 148.478 198.070 3.952   1.00 60.96  ? 112 ASN D N   1 
ATOM   4732 C  CA  . ASN D 2 111 ? 147.083 197.730 4.141   1.00 60.19  ? 112 ASN D CA  1 
ATOM   4733 C  C   . ASN D 2 111 ? 146.902 196.839 5.359   1.00 65.74  ? 112 ASN D C   1 
ATOM   4734 O  O   . ASN D 2 111 ? 146.165 195.868 5.309   1.00 70.96  ? 112 ASN D O   1 
ATOM   4735 C  CB  . ASN D 2 111 ? 146.510 197.058 2.892   1.00 70.10  ? 112 ASN D CB  1 
ATOM   4736 C  CG  . ASN D 2 111 ? 146.329 198.034 1.750   1.00 71.54  ? 112 ASN D CG  1 
ATOM   4737 O  OD1 . ASN D 2 111 ? 145.603 199.026 1.874   1.00 77.40  ? 112 ASN D OD1 1 
ATOM   4738 N  ND2 . ASN D 2 111 ? 147.013 197.778 0.641   1.00 70.68  ? 112 ASN D ND2 1 
ATOM   4739 N  N   . LYS D 2 112 ? 147.619 197.133 6.435   1.00 61.67  ? 113 LYS D N   1 
ATOM   4740 C  CA  . LYS D 2 112 ? 147.506 196.341 7.653   1.00 62.88  ? 113 LYS D CA  1 
ATOM   4741 C  C   . LYS D 2 112 ? 147.236 197.249 8.837   1.00 58.97  ? 113 LYS D C   1 
ATOM   4742 O  O   . LYS D 2 112 ? 147.825 198.319 8.969   1.00 61.12  ? 113 LYS D O   1 
ATOM   4743 C  CB  . LYS D 2 112 ? 148.772 195.499 7.892   1.00 66.62  ? 113 LYS D CB  1 
ATOM   4744 C  CG  . LYS D 2 112 ? 149.002 194.435 6.816   1.00 78.69  ? 113 LYS D CG  1 
ATOM   4745 C  CD  . LYS D 2 112 ? 150.351 193.733 6.925   1.00 84.95  ? 113 LYS D CD  1 
ATOM   4746 C  CE  . LYS D 2 112 ? 150.529 192.753 5.762   1.00 86.13  ? 113 LYS D CE  1 
ATOM   4747 N  NZ  . LYS D 2 112 ? 151.799 191.972 5.811   1.00 99.43  1 113 LYS D NZ  1 
ATOM   4748 N  N   . THR D 2 113 ? 146.334 196.837 9.703   1.00 56.64  ? 114 THR D N   1 
ATOM   4749 C  CA  . THR D 2 113 ? 146.051 197.651 10.866  1.00 56.34  ? 114 THR D CA  1 
ATOM   4750 C  C   . THR D 2 113 ? 145.977 196.737 12.076  1.00 51.42  ? 114 THR D C   1 
ATOM   4751 O  O   . THR D 2 113 ? 145.596 195.576 11.961  1.00 61.60  ? 114 THR D O   1 
ATOM   4752 C  CB  . THR D 2 113 ? 144.761 198.471 10.676  1.00 48.30  ? 114 THR D CB  1 
ATOM   4753 O  OG1 . THR D 2 113 ? 144.597 199.354 11.778  1.00 57.60  ? 114 THR D OG1 1 
ATOM   4754 C  CG2 . THR D 2 113 ? 143.564 197.576 10.561  1.00 47.21  ? 114 THR D CG2 1 
ATOM   4755 N  N   . LEU D 2 114 ? 146.392 197.244 13.226  1.00 45.98  ? 115 LEU D N   1 
ATOM   4756 C  CA  . LEU D 2 114 ? 146.516 196.427 14.423  1.00 45.82  ? 115 LEU D CA  1 
ATOM   4757 C  C   . LEU D 2 114 ? 145.625 197.005 15.515  1.00 46.79  ? 115 LEU D C   1 
ATOM   4758 O  O   . LEU D 2 114 ? 145.541 198.222 15.641  1.00 43.41  ? 115 LEU D O   1 
ATOM   4759 C  CB  . LEU D 2 114 ? 147.990 196.367 14.845  1.00 52.81  ? 115 LEU D CB  1 
ATOM   4760 C  CG  . LEU D 2 114 ? 148.458 195.707 16.141  1.00 64.13  ? 115 LEU D CG  1 
ATOM   4761 C  CD1 . LEU D 2 114 ? 148.069 194.244 16.166  1.00 62.39  ? 115 LEU D CD1 1 
ATOM   4762 C  CD2 . LEU D 2 114 ? 149.967 195.859 16.263  1.00 77.33  ? 115 LEU D CD2 1 
ATOM   4763 N  N   . PHE D 2 115 ? 144.955 196.146 16.290  1.00 40.86  ? 116 PHE D N   1 
ATOM   4764 C  CA  . PHE D 2 115 ? 143.933 196.599 17.255  1.00 40.73  ? 116 PHE D CA  1 
ATOM   4765 C  C   . PHE D 2 115 ? 144.241 196.222 18.695  1.00 44.46  ? 116 PHE D C   1 
ATOM   4766 O  O   . PHE D 2 115 ? 144.279 195.039 19.027  1.00 49.26  ? 116 PHE D O   1 
ATOM   4767 C  CB  . PHE D 2 115 ? 142.562 196.020 16.893  1.00 45.92  ? 116 PHE D CB  1 
ATOM   4768 C  CG  . PHE D 2 115 ? 142.056 196.443 15.537  1.00 42.68  ? 116 PHE D CG  1 
ATOM   4769 C  CD1 . PHE D 2 115 ? 142.662 195.972 14.386  1.00 45.07  ? 116 PHE D CD1 1 
ATOM   4770 C  CD2 . PHE D 2 115 ? 140.943 197.261 15.419  1.00 40.20  ? 116 PHE D CD2 1 
ATOM   4771 C  CE1 . PHE D 2 115 ? 142.212 196.334 13.163  1.00 42.04  ? 116 PHE D CE1 1 
ATOM   4772 C  CE2 . PHE D 2 115 ? 140.471 197.631 14.177  1.00 41.00  ? 116 PHE D CE2 1 
ATOM   4773 C  CZ  . PHE D 2 115 ? 141.110 197.167 13.043  1.00 48.36  ? 116 PHE D CZ  1 
ATOM   4774 N  N   . ASP D 2 116 ? 144.434 197.225 19.547  1.00 35.24  ? 117 ASP D N   1 
ATOM   4775 C  CA  . ASP D 2 116 ? 144.681 197.000 20.968  1.00 43.74  ? 117 ASP D CA  1 
ATOM   4776 C  C   . ASP D 2 116 ? 143.345 197.073 21.707  1.00 43.03  ? 117 ASP D C   1 
ATOM   4777 O  O   . ASP D 2 116 ? 142.869 198.150 22.049  1.00 46.03  ? 117 ASP D O   1 
ATOM   4778 C  CB  . ASP D 2 116 ? 145.709 198.030 21.507  1.00 41.12  ? 117 ASP D CB  1 
ATOM   4779 C  CG  . ASP D 2 116 ? 145.995 197.892 23.011  1.00 57.12  ? 117 ASP D CG  1 
ATOM   4780 O  OD1 . ASP D 2 116 ? 145.246 197.187 23.735  1.00 59.43  ? 117 ASP D OD1 1 
ATOM   4781 O  OD2 . ASP D 2 116 ? 146.999 198.501 23.475  1.00 58.52  1 117 ASP D OD2 1 
ATOM   4782 N  N   . ILE D 2 117 ? 142.781 195.904 21.998  1.00 46.51  ? 118 ILE D N   1 
ATOM   4783 C  CA  . ILE D 2 117 ? 141.462 195.804 22.595  1.00 44.74  ? 118 ILE D CA  1 
ATOM   4784 C  C   . ILE D 2 117 ? 141.517 195.480 24.073  1.00 45.00  ? 118 ILE D C   1 
ATOM   4785 O  O   . ILE D 2 117 ? 142.140 194.507 24.471  1.00 54.89  ? 118 ILE D O   1 
ATOM   4786 C  CB  . ILE D 2 117 ? 140.617 194.699 21.923  1.00 46.30  ? 118 ILE D CB  1 
ATOM   4787 C  CG1 . ILE D 2 117 ? 140.605 194.840 20.402  1.00 41.72  ? 118 ILE D CG1 1 
ATOM   4788 C  CG2 . ILE D 2 117 ? 139.200 194.717 22.473  1.00 42.84  ? 118 ILE D CG2 1 
ATOM   4789 C  CD1 . ILE D 2 117 ? 140.031 196.138 19.912  1.00 46.45  ? 118 ILE D CD1 1 
ATOM   4790 N  N   . THR D 2 118 ? 140.835 196.277 24.883  1.00 46.48  ? 119 THR D N   1 
ATOM   4791 C  CA  . THR D 2 118 ? 140.679 195.978 26.301  1.00 43.13  ? 119 THR D CA  1 
ATOM   4792 C  C   . THR D 2 118 ? 139.208 196.011 26.697  1.00 45.20  ? 119 THR D C   1 
ATOM   4793 O  O   . THR D 2 118 ? 138.481 196.906 26.277  1.00 44.64  ? 119 THR D O   1 
ATOM   4794 C  CB  . THR D 2 118 ? 141.421 196.970 27.177  1.00 47.98  ? 119 THR D CB  1 
ATOM   4795 O  OG1 . THR D 2 118 ? 141.035 198.299 26.806  1.00 49.65  ? 119 THR D OG1 1 
ATOM   4796 C  CG2 . THR D 2 118 ? 142.943 196.779 27.051  1.00 46.31  ? 119 THR D CG2 1 
ATOM   4797 N  N   . VAL D 2 119 ? 138.779 195.047 27.513  1.00 53.85  ? 120 VAL D N   1 
ATOM   4798 C  CA  . VAL D 2 119 ? 137.410 195.007 28.040  1.00 38.39  ? 120 VAL D CA  1 
ATOM   4799 C  C   . VAL D 2 119 ? 137.455 194.908 29.555  1.00 47.54  ? 120 VAL D C   1 
ATOM   4800 O  O   . VAL D 2 119 ? 138.316 194.235 30.105  1.00 57.55  ? 120 VAL D O   1 
ATOM   4801 C  CB  . VAL D 2 119 ? 136.597 193.818 27.451  1.00 43.77  ? 120 VAL D CB  1 
ATOM   4802 C  CG1 . VAL D 2 119 ? 135.186 193.799 28.016  1.00 45.41  ? 120 VAL D CG1 1 
ATOM   4803 C  CG2 . VAL D 2 119 ? 136.535 193.916 25.939  1.00 41.54  ? 120 VAL D CG2 1 
ATOM   4804 N  N   . ASN D 2 120 ? 136.545 195.590 30.234  1.00 46.68  ? 121 ASN D N   1 
ATOM   4805 C  CA  . ASN D 2 120 ? 136.547 195.598 31.684  1.00 47.56  ? 121 ASN D CA  1 
ATOM   4806 C  C   . ASN D 2 120 ? 135.171 196.002 32.233  1.00 53.11  ? 121 ASN D C   1 
ATOM   4807 O  O   . ASN D 2 120 ? 134.597 197.020 31.818  1.00 52.17  ? 121 ASN D O   1 
ATOM   4808 C  CB  . ASN D 2 120 ? 137.650 196.545 32.202  1.00 47.02  ? 121 ASN D CB  1 
ATOM   4809 C  CG  . ASN D 2 120 ? 137.980 196.318 33.677  1.00 62.42  ? 121 ASN D CG  1 
ATOM   4810 O  OD1 . ASN D 2 120 ? 137.470 195.393 34.301  1.00 61.22  ? 121 ASN D OD1 1 
ATOM   4811 N  ND2 . ASN D 2 120 ? 138.844 197.159 34.232  1.00 58.29  ? 121 ASN D ND2 1 
ATOM   4812 N  N   . GLY D 2 121 ? 134.638 195.203 33.156  1.00 49.57  ? 122 GLY D N   1 
ATOM   4813 C  CA  . GLY D 2 121 ? 133.367 195.516 33.792  1.00 45.40  ? 122 GLY D CA  1 
ATOM   4814 C  C   . GLY D 2 121 ? 132.148 194.853 33.168  1.00 46.96  ? 122 GLY D C   1 
ATOM   4815 O  O   . GLY D 2 121 ? 131.020 195.274 33.439  1.00 51.03  ? 122 GLY D O   1 
ATOM   4816 N  N   . VAL D 2 122 ? 132.366 193.838 32.322  1.00 53.22  ? 123 VAL D N   1 
ATOM   4817 C  CA  . VAL D 2 122 ? 131.267 193.045 31.760  1.00 51.66  ? 123 VAL D CA  1 
ATOM   4818 C  C   . VAL D 2 122 ? 130.738 192.071 32.818  1.00 60.15  ? 123 VAL D C   1 
ATOM   4819 O  O   . VAL D 2 122 ? 131.516 191.545 33.621  1.00 61.54  ? 123 VAL D O   1 
ATOM   4820 C  CB  . VAL D 2 122 ? 131.693 192.229 30.514  1.00 44.78  ? 123 VAL D CB  1 
ATOM   4821 C  CG1 . VAL D 2 122 ? 131.801 193.107 29.273  1.00 52.08  ? 123 VAL D CG1 1 
ATOM   4822 C  CG2 . VAL D 2 122 ? 132.991 191.482 30.773  1.00 54.85  ? 123 VAL D CG2 1 
ATOM   4823 N  N   . PRO D 2 123 ? 129.410 191.842 32.836  1.00 59.02  ? 124 PRO D N   1 
ATOM   4824 C  CA  . PRO D 2 123 ? 128.792 190.971 33.848  1.00 64.06  ? 124 PRO D CA  1 
ATOM   4825 C  C   . PRO D 2 123 ? 128.990 189.463 33.583  1.00 67.13  ? 124 PRO D C   1 
ATOM   4826 O  O   . PRO D 2 123 ? 129.157 188.714 34.546  1.00 75.46  ? 124 PRO D O   1 
ATOM   4827 C  CB  . PRO D 2 123 ? 127.297 191.348 33.781  1.00 62.29  ? 124 PRO D CB  1 
ATOM   4828 C  CG  . PRO D 2 123 ? 127.219 192.596 32.928  1.00 62.76  ? 124 PRO D CG  1 
ATOM   4829 C  CD  . PRO D 2 123 ? 128.397 192.499 31.993  1.00 52.92  ? 124 PRO D CD  1 
ATOM   4830 N  N   . GLU D 2 124 ? 128.969 189.027 32.324  1.00 62.62  ? 125 GLU D N   1 
ATOM   4831 C  CA  . GLU D 2 124 ? 129.111 187.605 32.013  1.00 56.73  ? 125 GLU D CA  1 
ATOM   4832 C  C   . GLU D 2 124 ? 130.496 187.322 31.439  1.00 62.08  ? 125 GLU D C   1 
ATOM   4833 O  O   . GLU D 2 124 ? 130.878 187.899 30.420  1.00 66.42  ? 125 GLU D O   1 
ATOM   4834 C  CB  . GLU D 2 124 ? 128.017 187.137 31.024  1.00 55.55  ? 125 GLU D CB  1 
ATOM   4835 C  CG  . GLU D 2 124 ? 126.578 187.445 31.504  1.00 68.66  ? 125 GLU D CG  1 
ATOM   4836 C  CD  . GLU D 2 124 ? 125.449 186.674 30.775  1.00 72.15  ? 125 GLU D CD  1 
ATOM   4837 O  OE1 . GLU D 2 124 ? 125.653 186.161 29.644  1.00 64.96  ? 125 GLU D OE1 1 
ATOM   4838 O  OE2 . GLU D 2 124 ? 124.335 186.595 31.353  1.00 68.62  1 125 GLU D OE2 1 
ATOM   4839 N  N   . ALA D 2 125 ? 131.248 186.436 32.092  1.00 60.13  ? 126 ALA D N   1 
ATOM   4840 C  CA  . ALA D 2 125 ? 132.500 185.925 31.532  1.00 50.88  ? 126 ALA D CA  1 
ATOM   4841 C  C   . ALA D 2 125 ? 132.222 185.173 30.238  1.00 50.14  ? 126 ALA D C   1 
ATOM   4842 O  O   . ALA D 2 125 ? 131.124 184.648 30.039  1.00 59.33  ? 126 ALA D O   1 
ATOM   4843 C  CB  . ALA D 2 125 ? 133.207 185.026 32.541  1.00 54.06  ? 126 ALA D CB  1 
ATOM   4844 N  N   . GLY D 2 126 ? 133.196 185.117 29.341  1.00 55.59  ? 127 GLY D N   1 
ATOM   4845 C  CA  . GLY D 2 126 ? 132.959 184.448 28.070  1.00 56.09  ? 127 GLY D CA  1 
ATOM   4846 C  C   . GLY D 2 126 ? 133.826 184.915 26.919  1.00 55.76  ? 127 GLY D C   1 
ATOM   4847 O  O   . GLY D 2 126 ? 134.598 185.862 27.042  1.00 56.76  ? 127 GLY D O   1 
ATOM   4848 N  N   . ASN D 2 127 ? 133.698 184.239 25.788  1.00 58.13  ? 128 ASN D N   1 
ATOM   4849 C  CA  . ASN D 2 127 ? 134.307 184.722 24.566  1.00 59.60  ? 128 ASN D CA  1 
ATOM   4850 C  C   . ASN D 2 127 ? 133.398 185.773 23.948  1.00 66.23  ? 128 ASN D C   1 
ATOM   4851 O  O   . ASN D 2 127 ? 132.208 185.516 23.708  1.00 57.38  ? 128 ASN D O   1 
ATOM   4852 C  CB  . ASN D 2 127 ? 134.561 183.579 23.572  1.00 61.28  ? 128 ASN D CB  1 
ATOM   4853 C  CG  . ASN D 2 127 ? 135.707 182.683 23.999  1.00 66.32  ? 128 ASN D CG  1 
ATOM   4854 O  OD1 . ASN D 2 127 ? 136.741 183.166 24.456  1.00 70.08  ? 128 ASN D OD1 1 
ATOM   4855 N  ND2 . ASN D 2 127 ? 135.532 181.376 23.855  1.00 64.29  ? 128 ASN D ND2 1 
ATOM   4856 N  N   . TYR D 2 128 ? 133.958 186.968 23.747  1.00 62.79  ? 129 TYR D N   1 
ATOM   4857 C  CA  . TYR D 2 128 ? 133.266 188.057 23.063  1.00 52.07  ? 129 TYR D CA  1 
ATOM   4858 C  C   . TYR D 2 128 ? 133.814 188.215 21.652  1.00 49.64  ? 129 TYR D C   1 
ATOM   4859 O  O   . TYR D 2 128 ? 135.007 188.026 21.428  1.00 55.08  ? 129 TYR D O   1 
ATOM   4860 C  CB  . TYR D 2 128 ? 133.407 189.361 23.842  1.00 38.71  ? 129 TYR D CB  1 
ATOM   4861 C  CG  . TYR D 2 128 ? 132.587 189.404 25.119  1.00 49.54  ? 129 TYR D CG  1 
ATOM   4862 C  CD1 . TYR D 2 128 ? 132.949 188.650 26.232  1.00 51.03  ? 129 TYR D CD1 1 
ATOM   4863 C  CD2 . TYR D 2 128 ? 131.450 190.206 25.214  1.00 51.58  ? 129 TYR D CD2 1 
ATOM   4864 C  CE1 . TYR D 2 128 ? 132.210 188.698 27.400  1.00 52.94  ? 129 TYR D CE1 1 
ATOM   4865 C  CE2 . TYR D 2 128 ? 130.702 190.260 26.382  1.00 47.96  ? 129 TYR D CE2 1 
ATOM   4866 C  CZ  . TYR D 2 128 ? 131.092 189.502 27.473  1.00 54.49  ? 129 TYR D CZ  1 
ATOM   4867 O  OH  . TYR D 2 128 ? 130.360 189.536 28.634  1.00 55.10  ? 129 TYR D OH  1 
ATOM   4868 N  N   . HIS D 2 129 ? 132.943 188.554 20.708  1.00 43.50  ? 130 HIS D N   1 
ATOM   4869 C  CA  . HIS D 2 129 ? 133.327 188.672 19.303  1.00 52.35  ? 130 HIS D CA  1 
ATOM   4870 C  C   . HIS D 2 129 ? 133.309 190.125 18.841  1.00 53.19  ? 130 HIS D C   1 
ATOM   4871 O  O   . HIS D 2 129 ? 132.375 190.884 19.151  1.00 48.77  ? 130 HIS D O   1 
ATOM   4872 C  CB  . HIS D 2 129 ? 132.408 187.856 18.384  1.00 54.06  ? 130 HIS D CB  1 
ATOM   4873 C  CG  . HIS D 2 129 ? 131.136 187.396 19.031  1.00 67.67  ? 130 HIS D CG  1 
ATOM   4874 N  ND1 . HIS D 2 129 ? 131.101 186.404 19.993  1.00 71.11  ? 130 HIS D ND1 1 
ATOM   4875 C  CD2 . HIS D 2 129 ? 129.852 187.792 18.851  1.00 68.70  ? 130 HIS D CD2 1 
ATOM   4876 C  CE1 . HIS D 2 129 ? 129.851 186.207 20.375  1.00 75.25  ? 130 HIS D CE1 1 
ATOM   4877 N  NE2 . HIS D 2 129 ? 129.073 187.037 19.698  1.00 77.64  ? 130 HIS D NE2 1 
ATOM   4878 N  N   . ALA D 2 130 ? 134.363 190.519 18.135  1.00 47.52  ? 131 ALA D N   1 
ATOM   4879 C  CA  . ALA D 2 130 ? 134.460 191.882 17.623  1.00 51.16  ? 131 ALA D CA  1 
ATOM   4880 C  C   . ALA D 2 130 ? 134.119 191.923 16.139  1.00 46.59  ? 131 ALA D C   1 
ATOM   4881 O  O   . ALA D 2 130 ? 134.524 191.055 15.364  1.00 45.89  ? 131 ALA D O   1 
ATOM   4882 C  CB  . ALA D 2 130 ? 135.858 192.462 17.862  1.00 43.03  ? 131 ALA D CB  1 
ATOM   4883 N  N   . SER D 2 131 ? 133.368 192.939 15.750  1.00 40.55  ? 132 SER D N   1 
ATOM   4884 C  CA  . SER D 2 131 ? 133.101 193.173 14.341  1.00 47.59  ? 132 SER D CA  1 
ATOM   4885 C  C   . SER D 2 131 ? 133.104 194.673 14.069  1.00 50.15  ? 132 SER D C   1 
ATOM   4886 O  O   . SER D 2 131 ? 132.958 195.495 14.986  1.00 44.51  ? 132 SER D O   1 
ATOM   4887 C  CB  . SER D 2 131 ? 131.769 192.544 13.930  1.00 52.45  ? 132 SER D CB  1 
ATOM   4888 O  OG  . SER D 2 131 ? 130.700 193.100 14.685  1.00 56.48  ? 132 SER D OG  1 
ATOM   4889 N  N   . ILE D 2 132 ? 133.305 195.025 12.810  1.00 45.34  ? 133 ILE D N   1 
ATOM   4890 C  CA  . ILE D 2 132 ? 133.197 196.403 12.388  1.00 37.60  ? 133 ILE D CA  1 
ATOM   4891 C  C   . ILE D 2 132 ? 132.002 196.475 11.468  1.00 46.31  ? 133 ILE D C   1 
ATOM   4892 O  O   . ILE D 2 132 ? 131.896 195.693 10.533  1.00 48.75  ? 133 ILE D O   1 
ATOM   4893 C  CB  . ILE D 2 132 ? 134.479 196.885 11.686  1.00 44.34  ? 133 ILE D CB  1 
ATOM   4894 C  CG1 . ILE D 2 132 ? 135.675 196.778 12.639  1.00 41.82  ? 133 ILE D CG1 1 
ATOM   4895 C  CG2 . ILE D 2 132 ? 134.290 198.299 11.137  1.00 38.54  ? 133 ILE D CG2 1 
ATOM   4896 C  CD1 . ILE D 2 132 ? 136.964 197.300 12.055  1.00 47.82  ? 133 ILE D CD1 1 
ATOM   4897 N  N   . HIS D 2 133 ? 131.078 197.379 11.755  1.00 47.71  ? 134 HIS D N   1 
ATOM   4898 C  CA  . HIS D 2 133 ? 129.872 197.519 10.949  1.00 39.88  ? 134 HIS D CA  1 
ATOM   4899 C  C   . HIS D 2 133 ? 129.984 198.706 10.006  1.00 48.33  ? 134 HIS D C   1 
ATOM   4900 O  O   . HIS D 2 133 ? 130.777 199.621 10.252  1.00 49.79  ? 134 HIS D O   1 
ATOM   4901 C  CB  . HIS D 2 133 ? 128.662 197.665 11.862  1.00 44.48  ? 134 HIS D CB  1 
ATOM   4902 C  CG  . HIS D 2 133 ? 128.313 196.406 12.595  1.00 50.23  ? 134 HIS D CG  1 
ATOM   4903 N  ND1 . HIS D 2 133 ? 127.059 195.831 12.537  1.00 48.17  ? 134 HIS D ND1 1 
ATOM   4904 C  CD2 . HIS D 2 133 ? 129.057 195.607 13.397  1.00 47.25  ? 134 HIS D CD2 1 
ATOM   4905 C  CE1 . HIS D 2 133 ? 127.043 194.742 13.286  1.00 48.15  ? 134 HIS D CE1 1 
ATOM   4906 N  NE2 . HIS D 2 133 ? 128.243 194.581 13.818  1.00 43.82  ? 134 HIS D NE2 1 
ATOM   4907 N  N   . GLU D 2 134 ? 129.156 198.714 8.962   1.00 49.96  ? 135 GLU D N   1 
ATOM   4908 C  CA  . GLU D 2 134 ? 129.316 199.634 7.835   1.00 50.25  ? 135 GLU D CA  1 
ATOM   4909 C  C   . GLU D 2 134 ? 129.188 201.090 8.247   1.00 42.45  ? 135 GLU D C   1 
ATOM   4910 O  O   . GLU D 2 134 ? 129.922 201.952 7.772   1.00 45.13  ? 135 GLU D O   1 
ATOM   4911 C  CB  . GLU D 2 134 ? 128.277 199.330 6.746   1.00 46.37  ? 135 GLU D CB  1 
ATOM   4912 C  CG  . GLU D 2 134 ? 128.735 198.368 5.648   1.00 65.70  ? 135 GLU D CG  1 
ATOM   4913 C  CD  . GLU D 2 134 ? 127.561 197.751 4.880   1.00 86.43  ? 135 GLU D CD  1 
ATOM   4914 O  OE1 . GLU D 2 134 ? 126.436 198.306 4.949   1.00 82.29  ? 135 GLU D OE1 1 
ATOM   4915 O  OE2 . GLU D 2 134 ? 127.761 196.701 4.222   1.00 83.35  1 135 GLU D OE2 1 
ATOM   4916 N  N   . LYS D 2 135 ? 128.228 201.349 9.120   1.00 38.01  ? 136 LYS D N   1 
ATOM   4917 C  CA  . LYS D 2 135 ? 127.845 202.709 9.468   1.00 45.41  ? 136 LYS D CA  1 
ATOM   4918 C  C   . LYS D 2 135 ? 128.215 203.068 10.891  1.00 44.61  ? 136 LYS D C   1 
ATOM   4919 O  O   . LYS D 2 135 ? 128.149 202.229 11.800  1.00 46.92  ? 136 LYS D O   1 
ATOM   4920 C  CB  . LYS D 2 135 ? 126.333 202.900 9.249   1.00 44.40  ? 136 LYS D CB  1 
ATOM   4921 C  CG  . LYS D 2 135 ? 125.911 202.670 7.783   1.00 42.60  ? 136 LYS D CG  1 
ATOM   4922 C  CD  . LYS D 2 135 ? 124.449 203.012 7.560   1.00 65.33  ? 136 LYS D CD  1 
ATOM   4923 C  CE  . LYS D 2 135 ? 123.527 202.148 8.425   1.00 64.54  ? 136 LYS D CE  1 
ATOM   4924 N  NZ  . LYS D 2 135 ? 122.228 202.828 8.726   1.00 67.87  1 136 LYS D NZ  1 
ATOM   4925 N  N   . GLY D 2 136 ? 128.602 204.324 11.079  1.00 40.09  ? 137 GLY D N   1 
ATOM   4926 C  CA  . GLY D 2 136 ? 128.898 204.828 12.407  1.00 37.90  ? 137 GLY D CA  1 
ATOM   4927 C  C   . GLY D 2 136 ? 127.687 205.499 13.025  1.00 41.49  ? 137 GLY D C   1 
ATOM   4928 O  O   . GLY D 2 136 ? 127.809 206.566 13.630  1.00 42.34  ? 137 GLY D O   1 
ATOM   4929 N  N   . ASP D 2 137 ? 126.512 204.891 12.849  1.00 37.03  ? 138 ASP D N   1 
ATOM   4930 C  CA  . ASP D 2 137 ? 125.289 205.426 13.433  1.00 44.53  ? 138 ASP D CA  1 
ATOM   4931 C  C   . ASP D 2 137 ? 124.892 204.605 14.660  1.00 46.85  ? 138 ASP D C   1 
ATOM   4932 O  O   . ASP D 2 137 ? 124.337 203.508 14.542  1.00 44.26  ? 138 ASP D O   1 
ATOM   4933 C  CB  . ASP D 2 137 ? 124.137 205.447 12.427  1.00 37.96  ? 138 ASP D CB  1 
ATOM   4934 C  CG  . ASP D 2 137 ? 122.894 206.162 12.990  1.00 48.70  ? 138 ASP D CG  1 
ATOM   4935 O  OD1 . ASP D 2 137 ? 122.808 206.339 14.236  1.00 43.95  ? 138 ASP D OD1 1 
ATOM   4936 O  OD2 . ASP D 2 137 ? 122.001 206.546 12.201  1.00 48.20  1 138 ASP D OD2 1 
ATOM   4937 N  N   . VAL D 2 138 ? 125.181 205.141 15.839  1.00 42.90  ? 139 VAL D N   1 
ATOM   4938 C  CA  . VAL D 2 138 ? 124.908 204.419 17.065  1.00 40.56  ? 139 VAL D CA  1 
ATOM   4939 C  C   . VAL D 2 138 ? 123.704 204.992 17.800  1.00 43.83  ? 139 VAL D C   1 
ATOM   4940 O  O   . VAL D 2 138 ? 123.544 204.759 18.992  1.00 50.32  ? 139 VAL D O   1 
ATOM   4941 C  CB  . VAL D 2 138 ? 126.129 204.441 17.992  1.00 44.82  ? 139 VAL D CB  1 
ATOM   4942 C  CG1 . VAL D 2 138 ? 127.328 203.807 17.291  1.00 34.95  ? 139 VAL D CG1 1 
ATOM   4943 C  CG2 . VAL D 2 138 ? 126.455 205.870 18.418  1.00 36.06  ? 139 VAL D CG2 1 
ATOM   4944 N  N   . SER D 2 139 ? 122.860 205.739 17.093  1.00 40.52  ? 140 SER D N   1 
ATOM   4945 C  CA  . SER D 2 139 ? 121.645 206.283 17.695  1.00 44.80  ? 140 SER D CA  1 
ATOM   4946 C  C   . SER D 2 139 ? 120.674 205.185 18.203  1.00 53.43  ? 140 SER D C   1 
ATOM   4947 O  O   . SER D 2 139 ? 120.022 205.357 19.242  1.00 52.57  ? 140 SER D O   1 
ATOM   4948 C  CB  . SER D 2 139 ? 120.951 207.219 16.709  1.00 39.25  ? 140 SER D CB  1 
ATOM   4949 O  OG  . SER D 2 139 ? 120.627 206.541 15.511  1.00 49.97  ? 140 SER D OG  1 
ATOM   4950 N  N   . LYS D 2 140 ? 120.573 204.077 17.470  1.00 48.17  ? 141 LYS D N   1 
ATOM   4951 C  CA  . LYS D 2 140 ? 119.722 202.958 17.873  1.00 55.02  ? 141 LYS D CA  1 
ATOM   4952 C  C   . LYS D 2 140 ? 120.550 201.723 18.283  1.00 53.00  ? 141 LYS D C   1 
ATOM   4953 O  O   . LYS D 2 140 ? 120.097 200.590 18.141  1.00 56.17  ? 141 LYS D O   1 
ATOM   4954 C  CB  . LYS D 2 140 ? 118.727 202.621 16.747  1.00 51.29  ? 141 LYS D CB  1 
ATOM   4955 C  CG  . LYS D 2 140 ? 117.587 203.656 16.626  1.00 53.47  ? 141 LYS D CG  1 
ATOM   4956 C  CD  . LYS D 2 140 ? 117.172 203.958 15.175  1.00 72.75  ? 141 LYS D CD  1 
ATOM   4957 C  CE  . LYS D 2 140 ? 116.588 202.749 14.447  1.00 77.65  ? 141 LYS D CE  1 
ATOM   4958 N  NZ  . LYS D 2 140 ? 116.024 203.116 13.103  1.00 75.03  1 141 LYS D NZ  1 
ATOM   4959 N  N   . GLY D 2 141 ? 121.760 201.960 18.793  1.00 48.61  ? 142 GLY D N   1 
ATOM   4960 C  CA  . GLY D 2 141 ? 122.667 200.902 19.206  1.00 43.25  ? 142 GLY D CA  1 
ATOM   4961 C  C   . GLY D 2 141 ? 123.179 200.107 18.040  1.00 42.31  ? 142 GLY D C   1 
ATOM   4962 O  O   . GLY D 2 141 ? 123.357 200.665 16.963  1.00 41.10  ? 142 GLY D O   1 
ATOM   4963 N  N   . VAL D 2 142 ? 123.437 198.819 18.253  1.00 41.58  ? 143 VAL D N   1 
ATOM   4964 C  CA  . VAL D 2 142 ? 123.937 197.951 17.181  1.00 47.28  ? 143 VAL D CA  1 
ATOM   4965 C  C   . VAL D 2 142 ? 123.015 197.950 15.966  1.00 46.32  ? 143 VAL D C   1 
ATOM   4966 O  O   . VAL D 2 142 ? 123.472 197.880 14.832  1.00 45.61  ? 143 VAL D O   1 
ATOM   4967 C  CB  . VAL D 2 142 ? 124.123 196.506 17.661  1.00 45.47  ? 143 VAL D CB  1 
ATOM   4968 C  CG1 . VAL D 2 142 ? 124.750 195.669 16.565  1.00 43.04  ? 143 VAL D CG1 1 
ATOM   4969 C  CG2 . VAL D 2 142 ? 125.000 196.486 18.894  1.00 48.88  ? 143 VAL D CG2 1 
ATOM   4970 N  N   . GLU D 2 143 ? 121.711 198.021 16.230  1.00 54.92  ? 144 GLU D N   1 
ATOM   4971 C  CA  . GLU D 2 143 ? 120.674 197.999 15.208  1.00 41.66  ? 144 GLU D CA  1 
ATOM   4972 C  C   . GLU D 2 143 ? 120.902 199.021 14.098  1.00 52.94  ? 144 GLU D C   1 
ATOM   4973 O  O   . GLU D 2 143 ? 120.702 198.720 12.924  1.00 55.06  ? 144 GLU D O   1 
ATOM   4974 C  CB  . GLU D 2 143 ? 119.323 198.233 15.881  1.00 51.86  ? 144 GLU D CB  1 
ATOM   4975 C  CG  . GLU D 2 143 ? 118.173 198.568 14.958  1.00 67.40  ? 144 GLU D CG  1 
ATOM   4976 C  CD  . GLU D 2 143 ? 116.916 198.925 15.738  1.00 79.87  ? 144 GLU D CD  1 
ATOM   4977 O  OE1 . GLU D 2 143 ? 116.033 199.612 15.180  1.00 86.42  ? 144 GLU D OE1 1 
ATOM   4978 O  OE2 . GLU D 2 143 ? 116.815 198.523 16.918  1.00 84.04  1 144 GLU D OE2 1 
ATOM   4979 N  N   . SER D 2 144 ? 121.341 200.224 14.468  1.00 51.49  ? 145 SER D N   1 
ATOM   4980 C  CA  . SER D 2 144 ? 121.529 201.308 13.490  1.00 45.30  ? 145 SER D CA  1 
ATOM   4981 C  C   . SER D 2 144 ? 122.903 201.304 12.817  1.00 40.91  ? 145 SER D C   1 
ATOM   4982 O  O   . SER D 2 144 ? 123.168 202.117 11.943  1.00 46.68  ? 145 SER D O   1 
ATOM   4983 C  CB  . SER D 2 144 ? 121.277 202.671 14.147  1.00 44.54  ? 145 SER D CB  1 
ATOM   4984 O  OG  . SER D 2 144 ? 121.920 202.779 15.416  1.00 48.09  ? 145 SER D OG  1 
ATOM   4985 N  N   . THR D 2 145 ? 123.775 200.387 13.196  1.00 35.88  ? 146 THR D N   1 
ATOM   4986 C  CA  . THR D 2 145 ? 125.102 200.378 12.598  1.00 42.97  ? 146 THR D CA  1 
ATOM   4987 C  C   . THR D 2 145 ? 125.134 199.657 11.240  1.00 49.52  ? 146 THR D C   1 
ATOM   4988 O  O   . THR D 2 145 ? 126.169 199.602 10.576  1.00 47.09  ? 146 THR D O   1 
ATOM   4989 C  CB  . THR D 2 145 ? 126.134 199.728 13.536  1.00 41.05  ? 146 THR D CB  1 
ATOM   4990 O  OG1 . THR D 2 145 ? 125.828 198.341 13.698  1.00 46.01  ? 146 THR D OG1 1 
ATOM   4991 C  CG2 . THR D 2 145 ? 126.116 200.396 14.890  1.00 41.35  ? 146 THR D CG2 1 
ATOM   4992 N  N   . GLY D 2 146 ? 123.993 199.117 10.824  1.00 52.34  ? 147 GLY D N   1 
ATOM   4993 C  CA  . GLY D 2 146 ? 123.909 198.413 9.559   1.00 51.77  ? 147 GLY D CA  1 
ATOM   4994 C  C   . GLY D 2 146 ? 124.628 197.079 9.629   1.00 52.09  ? 147 GLY D C   1 
ATOM   4995 O  O   . GLY D 2 146 ? 124.794 196.528 10.713  1.00 47.20  ? 147 GLY D O   1 
ATOM   4996 N  N   . LYS D 2 147 ? 125.038 196.558 8.473   1.00 54.52  ? 148 LYS D N   1 
ATOM   4997 C  CA  . LYS D 2 147 ? 125.581 195.196 8.369   1.00 61.28  ? 148 LYS D CA  1 
ATOM   4998 C  C   . LYS D 2 147 ? 127.024 195.094 8.851   1.00 53.09  ? 148 LYS D C   1 
ATOM   4999 O  O   . LYS D 2 147 ? 127.741 196.080 8.860   1.00 57.36  ? 148 LYS D O   1 
ATOM   5000 C  CB  . LYS D 2 147 ? 125.491 194.690 6.918   1.00 62.79  ? 148 LYS D CB  1 
ATOM   5001 C  CG  . LYS D 2 147 ? 124.230 195.116 6.165   1.00 80.37  ? 148 LYS D CG  1 
ATOM   5002 C  CD  . LYS D 2 147 ? 122.982 194.390 6.704   1.00 82.17  ? 148 LYS D CD  1 
ATOM   5003 C  CE  . LYS D 2 147 ? 121.743 194.724 5.890   1.00 80.95  ? 148 LYS D CE  1 
ATOM   5004 N  NZ  . LYS D 2 147 ? 121.509 196.202 5.858   1.00 71.71  1 148 LYS D NZ  1 
ATOM   5005 N  N   . VAL D 2 148 ? 127.448 193.891 9.220   1.00 47.87  ? 149 VAL D N   1 
ATOM   5006 C  CA  . VAL D 2 148 ? 128.853 193.615 9.518   1.00 53.75  ? 149 VAL D CA  1 
ATOM   5007 C  C   . VAL D 2 148 ? 129.686 193.927 8.272   1.00 56.24  ? 149 VAL D C   1 
ATOM   5008 O  O   . VAL D 2 148 ? 129.268 193.630 7.159   1.00 64.54  ? 149 VAL D O   1 
ATOM   5009 C  CB  . VAL D 2 148 ? 129.060 192.139 9.972   1.00 44.58  ? 149 VAL D CB  1 
ATOM   5010 C  CG1 . VAL D 2 148 ? 130.546 191.805 10.144  1.00 42.32  ? 149 VAL D CG1 1 
ATOM   5011 C  CG2 . VAL D 2 148 ? 128.295 191.882 11.248  1.00 39.67  ? 149 VAL D CG2 1 
ATOM   5012 N  N   . TRP D 2 149 ? 130.840 194.559 8.469   1.00 48.83  ? 150 TRP D N   1 
ATOM   5013 C  CA  . TRP D 2 149 ? 131.669 195.060 7.379   1.00 47.09  ? 150 TRP D CA  1 
ATOM   5014 C  C   . TRP D 2 149 ? 133.021 194.353 7.412   1.00 50.75  ? 150 TRP D C   1 
ATOM   5015 O  O   . TRP D 2 149 ? 133.668 194.150 6.382   1.00 51.74  ? 150 TRP D O   1 
ATOM   5016 C  CB  . TRP D 2 149 ? 131.814 196.580 7.509   1.00 46.09  ? 150 TRP D CB  1 
ATOM   5017 C  CG  . TRP D 2 149 ? 132.544 197.296 6.400   1.00 55.30  ? 150 TRP D CG  1 
ATOM   5018 C  CD1 . TRP D 2 149 ? 132.018 197.727 5.203   1.00 55.92  ? 150 TRP D CD1 1 
ATOM   5019 C  CD2 . TRP D 2 149 ? 133.925 197.703 6.400   1.00 54.00  ? 150 TRP D CD2 1 
ATOM   5020 N  NE1 . TRP D 2 149 ? 132.991 198.367 4.462   1.00 58.13  ? 150 TRP D NE1 1 
ATOM   5021 C  CE2 . TRP D 2 149 ? 134.167 198.365 5.170   1.00 55.51  ? 150 TRP D CE2 1 
ATOM   5022 C  CE3 . TRP D 2 149 ? 134.978 197.572 7.319   1.00 47.40  ? 150 TRP D CE3 1 
ATOM   5023 C  CZ2 . TRP D 2 149 ? 135.418 198.881 4.833   1.00 54.18  ? 150 TRP D CZ2 1 
ATOM   5024 C  CZ3 . TRP D 2 149 ? 136.220 198.090 6.988   1.00 50.22  ? 150 TRP D CZ3 1 
ATOM   5025 C  CH2 . TRP D 2 149 ? 136.431 198.734 5.752   1.00 61.39  ? 150 TRP D CH2 1 
ATOM   5026 N  N   . HIS D 2 150 ? 133.461 194.017 8.616   1.00 45.89  ? 151 HIS D N   1 
ATOM   5027 C  CA  . HIS D 2 150 ? 134.613 193.147 8.808   1.00 49.11  ? 151 HIS D CA  1 
ATOM   5028 C  C   . HIS D 2 150 ? 134.422 192.355 10.099  1.00 56.74  ? 151 HIS D C   1 
ATOM   5029 O  O   . HIS D 2 150 ? 134.214 192.940 11.167  1.00 57.90  ? 151 HIS D O   1 
ATOM   5030 C  CB  . HIS D 2 150 ? 135.921 193.936 8.857   1.00 42.86  ? 151 HIS D CB  1 
ATOM   5031 C  CG  . HIS D 2 150 ? 137.120 193.075 9.114   1.00 52.11  ? 151 HIS D CG  1 
ATOM   5032 N  ND1 . HIS D 2 150 ? 137.892 192.549 8.100   1.00 45.41  ? 151 HIS D ND1 1 
ATOM   5033 C  CD2 . HIS D 2 150 ? 137.660 192.620 10.270  1.00 53.16  ? 151 HIS D CD2 1 
ATOM   5034 C  CE1 . HIS D 2 150 ? 138.868 191.827 8.621   1.00 49.72  ? 151 HIS D CE1 1 
ATOM   5035 N  NE2 . HIS D 2 150 ? 138.751 191.852 9.937   1.00 53.13  ? 151 HIS D NE2 1 
ATOM   5036 N  N   . LYS D 2 151 ? 134.490 191.029 10.012  1.00 56.97  ? 152 LYS D N   1 
ATOM   5037 C  CA  . LYS D 2 151 ? 134.327 190.199 11.199  1.00 55.32  ? 152 LYS D CA  1 
ATOM   5038 C  C   . LYS D 2 151 ? 135.688 189.717 11.677  1.00 51.93  ? 152 LYS D C   1 
ATOM   5039 O  O   . LYS D 2 151 ? 136.509 189.264 10.885  1.00 51.67  ? 152 LYS D O   1 
ATOM   5040 C  CB  . LYS D 2 151 ? 133.386 189.021 10.905  1.00 59.01  ? 152 LYS D CB  1 
ATOM   5041 C  CG  . LYS D 2 151 ? 132.922 188.239 12.135  1.00 61.74  ? 152 LYS D CG  1 
ATOM   5042 C  CD  . LYS D 2 151 ? 131.954 187.110 11.742  1.00 70.72  ? 152 LYS D CD  1 
ATOM   5043 C  CE  . LYS D 2 151 ? 131.515 186.276 12.958  1.00 83.42  ? 152 LYS D CE  1 
ATOM   5044 N  NZ  . LYS D 2 151 ? 130.580 185.163 12.587  1.00 76.73  1 152 LYS D NZ  1 
ATOM   5045 N  N   . PHE D 2 152 ? 135.938 189.847 12.973  1.00 56.32  ? 153 PHE D N   1 
ATOM   5046 C  CA  . PHE D 2 152 ? 137.174 189.334 13.544  1.00 56.43  ? 153 PHE D CA  1 
ATOM   5047 C  C   . PHE D 2 152 ? 136.965 187.920 14.061  1.00 59.46  ? 153 PHE D C   1 
ATOM   5048 O  O   . PHE D 2 152 ? 136.115 187.686 14.932  1.00 65.59  ? 153 PHE D O   1 
ATOM   5049 C  CB  . PHE D 2 152 ? 137.689 190.240 14.664  1.00 53.21  ? 153 PHE D CB  1 
ATOM   5050 C  CG  . PHE D 2 152 ? 138.199 191.563 14.174  1.00 52.27  ? 153 PHE D CG  1 
ATOM   5051 C  CD1 . PHE D 2 152 ? 139.429 191.654 13.545  1.00 48.09  ? 153 PHE D CD1 1 
ATOM   5052 C  CD2 . PHE D 2 152 ? 137.456 192.718 14.367  1.00 40.91  ? 153 PHE D CD2 1 
ATOM   5053 C  CE1 . PHE D 2 152 ? 139.902 192.866 13.092  1.00 46.72  ? 153 PHE D CE1 1 
ATOM   5054 C  CE2 . PHE D 2 152 ? 137.916 193.933 13.917  1.00 42.00  ? 153 PHE D CE2 1 
ATOM   5055 C  CZ  . PHE D 2 152 ? 139.151 194.010 13.275  1.00 47.76  ? 153 PHE D CZ  1 
ATOM   5056 N  N   . ASP D 2 153 ? 137.760 186.997 13.522  1.00 64.51  ? 154 ASP D N   1 
ATOM   5057 C  CA  . ASP D 2 153 ? 137.668 185.574 13.833  1.00 67.80  ? 154 ASP D CA  1 
ATOM   5058 C  C   . ASP D 2 153 ? 137.988 185.297 15.281  1.00 75.09  ? 154 ASP D C   1 
ATOM   5059 O  O   . ASP D 2 153 ? 137.312 184.516 15.954  1.00 76.76  ? 154 ASP D O   1 
ATOM   5060 C  CB  . ASP D 2 153 ? 138.640 184.783 12.964  1.00 70.58  ? 154 ASP D CB  1 
ATOM   5061 C  CG  . ASP D 2 153 ? 138.231 184.747 11.518  1.00 78.41  ? 154 ASP D CG  1 
ATOM   5062 O  OD1 . ASP D 2 153 ? 137.011 184.796 11.245  1.00 74.62  ? 154 ASP D OD1 1 
ATOM   5063 O  OD2 . ASP D 2 153 ? 139.137 184.684 10.657  1.00 91.56  1 154 ASP D OD2 1 
ATOM   5064 N  N   . GLU D 2 154 ? 139.030 185.963 15.752  1.00 61.14  ? 155 GLU D N   1 
ATOM   5065 C  CA  . GLU D 2 154 ? 139.528 185.774 17.092  1.00 62.60  ? 155 GLU D CA  1 
ATOM   5066 C  C   . GLU D 2 154 ? 138.577 186.395 18.102  1.00 60.90  ? 155 GLU D C   1 
ATOM   5067 O  O   . GLU D 2 154 ? 138.010 187.465 17.868  1.00 59.33  ? 155 GLU D O   1 
ATOM   5068 C  CB  . GLU D 2 154 ? 140.920 186.379 17.220  1.00 67.55  ? 155 GLU D CB  1 
ATOM   5069 C  CG  . GLU D 2 154 ? 141.903 185.862 16.175  1.00 70.24  ? 155 GLU D CG  1 
ATOM   5070 C  CD  . GLU D 2 154 ? 141.663 186.472 14.789  1.00 97.26  ? 155 GLU D CD  1 
ATOM   5071 O  OE1 . GLU D 2 154 ? 141.125 187.611 14.702  1.00 84.14  ? 155 GLU D OE1 1 
ATOM   5072 O  OE2 . GLU D 2 154 ? 141.992 185.795 13.788  1.00 109.22 1 155 GLU D OE2 1 
ATOM   5073 N  N   . PRO D 2 155 ? 138.348 185.685 19.204  1.00 62.56  ? 156 PRO D N   1 
ATOM   5074 C  CA  . PRO D 2 155 ? 137.527 186.189 20.304  1.00 61.86  ? 156 PRO D CA  1 
ATOM   5075 C  C   . PRO D 2 155 ? 138.307 187.045 21.308  1.00 53.89  ? 156 PRO D C   1 
ATOM   5076 O  O   . PRO D 2 155 ? 139.539 186.982 21.381  1.00 54.40  ? 156 PRO D O   1 
ATOM   5077 C  CB  . PRO D 2 155 ? 137.007 184.903 20.958  1.00 65.10  ? 156 PRO D CB  1 
ATOM   5078 C  CG  . PRO D 2 155 ? 138.088 183.925 20.721  1.00 59.84  ? 156 PRO D CG  1 
ATOM   5079 C  CD  . PRO D 2 155 ? 138.659 184.251 19.358  1.00 59.00  ? 156 PRO D CD  1 
ATOM   5080 N  N   . ILE D 2 156 ? 137.577 187.863 22.056  1.00 51.80  ? 157 ILE D N   1 
ATOM   5081 C  CA  . ILE D 2 156 ? 138.144 188.560 23.195  1.00 52.09  ? 157 ILE D CA  1 
ATOM   5082 C  C   . ILE D 2 156 ? 137.856 187.740 24.451  1.00 56.59  ? 157 ILE D C   1 
ATOM   5083 O  O   . ILE D 2 156 ? 136.718 187.710 24.939  1.00 52.89  ? 157 ILE D O   1 
ATOM   5084 C  CB  . ILE D 2 156 ? 137.568 189.987 23.333  1.00 57.91  ? 157 ILE D CB  1 
ATOM   5085 C  CG1 . ILE D 2 156 ? 137.889 190.817 22.089  1.00 60.57  ? 157 ILE D CG1 1 
ATOM   5086 C  CG2 . ILE D 2 156 ? 138.135 190.679 24.540  1.00 58.69  ? 157 ILE D CG2 1 
ATOM   5087 C  CD1 . ILE D 2 156 ? 136.769 190.862 21.089  1.00 55.79  ? 157 ILE D CD1 1 
ATOM   5088 N  N   . GLU D 2 157 ? 138.899 187.102 24.983  1.00 56.30  ? 158 GLU D N   1 
ATOM   5089 C  CA  . GLU D 2 157 ? 138.747 186.203 26.115  1.00 49.89  ? 158 GLU D CA  1 
ATOM   5090 C  C   . GLU D 2 157 ? 138.560 186.989 27.396  1.00 54.70  ? 158 GLU D C   1 
ATOM   5091 O  O   . GLU D 2 157 ? 139.520 187.460 28.010  1.00 55.75  ? 158 GLU D O   1 
ATOM   5092 C  CB  . GLU D 2 157 ? 139.956 185.258 26.202  1.00 51.77  ? 158 GLU D CB  1 
ATOM   5093 C  CG  . GLU D 2 157 ? 140.013 184.278 25.014  1.00 62.32  ? 158 GLU D CG  1 
ATOM   5094 C  CD  . GLU D 2 157 ? 141.309 183.481 24.915  1.00 79.95  ? 158 GLU D CD  1 
ATOM   5095 O  OE1 . GLU D 2 157 ? 141.917 183.163 25.964  1.00 82.18  ? 158 GLU D OE1 1 
ATOM   5096 O  OE2 . GLU D 2 157 ? 141.712 183.164 23.771  1.00 78.39  1 158 GLU D OE2 1 
ATOM   5097 N  N   . CYS D 2 158 ? 137.302 187.098 27.808  1.00 46.08  ? 159 CYS D N   1 
ATOM   5098 C  CA  . CYS D 2 158 ? 136.955 187.823 29.013  1.00 61.16  ? 159 CYS D CA  1 
ATOM   5099 C  C   . CYS D 2 158 ? 136.592 186.881 30.163  1.00 70.41  ? 159 CYS D C   1 
ATOM   5100 O  O   . CYS D 2 158 ? 135.410 186.653 30.458  1.00 65.30  ? 159 CYS D O   1 
ATOM   5101 C  CB  . CYS D 2 158 ? 135.804 188.796 28.731  1.00 63.56  ? 159 CYS D CB  1 
ATOM   5102 S  SG  . CYS D 2 158 ? 136.213 190.052 27.493  1.00 59.80  ? 159 CYS D SG  1 
ATOM   5103 N  N   . PHE D 2 159 ? 137.625 186.333 30.801  1.00 68.47  ? 160 PHE D N   1 
ATOM   5104 C  CA  . PHE D 2 159 ? 137.438 185.457 31.948  1.00 64.30  ? 160 PHE D CA  1 
ATOM   5105 C  C   . PHE D 2 159 ? 138.233 185.954 33.162  1.00 61.83  ? 160 PHE D C   1 
ATOM   5106 O  O   . PHE D 2 159 ? 138.035 185.460 34.268  1.00 70.03  ? 160 PHE D O   1 
ATOM   5107 C  CB  . PHE D 2 159 ? 137.848 184.019 31.607  1.00 63.02  ? 160 PHE D CB  1 
ATOM   5108 C  CG  . PHE D 2 159 ? 137.044 183.394 30.491  1.00 63.06  ? 160 PHE D CG  1 
ATOM   5109 C  CD1 . PHE D 2 159 ? 135.826 182.787 30.744  1.00 68.47  ? 160 PHE D CD1 1 
ATOM   5110 C  CD2 . PHE D 2 159 ? 137.521 183.409 29.184  1.00 59.02  ? 160 PHE D CD2 1 
ATOM   5111 C  CE1 . PHE D 2 159 ? 135.093 182.208 29.706  1.00 60.84  ? 160 PHE D CE1 1 
ATOM   5112 C  CE2 . PHE D 2 159 ? 136.800 182.830 28.148  1.00 62.56  ? 160 PHE D CE2 1 
ATOM   5113 C  CZ  . PHE D 2 159 ? 135.587 182.230 28.410  1.00 60.36  ? 160 PHE D CZ  1 
ATOM   5114 N  N   . ASN D 2 160 ? 139.123 186.928 32.963  1.00 58.26  ? 161 ASN D N   1 
ATOM   5115 C  CA  . ASN D 2 160 ? 139.886 187.492 34.080  1.00 64.03  ? 161 ASN D CA  1 
ATOM   5116 C  C   . ASN D 2 160 ? 138.944 188.179 35.047  1.00 67.15  ? 161 ASN D C   1 
ATOM   5117 O  O   . ASN D 2 160 ? 138.007 188.843 34.614  1.00 68.72  ? 161 ASN D O   1 
ATOM   5118 C  CB  . ASN D 2 160 ? 140.915 188.512 33.599  1.00 60.57  ? 161 ASN D CB  1 
ATOM   5119 C  CG  . ASN D 2 160 ? 141.714 188.023 32.431  1.00 73.68  ? 161 ASN D CG  1 
ATOM   5120 O  OD1 . ASN D 2 160 ? 141.649 186.851 32.063  1.00 86.29  ? 161 ASN D OD1 1 
ATOM   5121 N  ND2 . ASN D 2 160 ? 142.463 188.927 31.815  1.00 78.70  ? 161 ASN D ND2 1 
ATOM   5122 N  N   . GLU D 2 161 ? 139.163 188.046 36.349  1.00 73.85  ? 162 GLU D N   1 
ATOM   5123 C  CA  . GLU D 2 161 ? 138.319 188.812 37.251  1.00 71.18  ? 162 GLU D CA  1 
ATOM   5124 C  C   . GLU D 2 161 ? 138.696 190.283 37.101  1.00 73.60  ? 162 GLU D C   1 
ATOM   5125 O  O   . GLU D 2 161 ? 139.829 190.619 36.725  1.00 75.93  ? 162 GLU D O   1 
ATOM   5126 C  CB  . GLU D 2 161 ? 138.438 188.338 38.701  1.00 82.24  ? 162 GLU D CB  1 
ATOM   5127 C  CG  . GLU D 2 161 ? 137.732 187.007 38.968  1.00 87.06  ? 162 GLU D CG  1 
ATOM   5128 C  CD  . GLU D 2 161 ? 137.470 186.754 40.450  1.00 106.99 ? 162 GLU D CD  1 
ATOM   5129 O  OE1 . GLU D 2 161 ? 137.777 187.641 41.280  1.00 107.03 ? 162 GLU D OE1 1 
ATOM   5130 O  OE2 . GLU D 2 161 ? 136.943 185.669 40.783  1.00 98.39  1 162 GLU D OE2 1 
ATOM   5131 N  N   . SER D 2 162 ? 137.710 191.146 37.319  1.00 67.83  ? 163 SER D N   1 
ATOM   5132 C  CA  . SER D 2 162 ? 137.880 192.579 37.138  1.00 70.20  ? 163 SER D CA  1 
ATOM   5133 C  C   . SER D 2 162 ? 138.108 193.282 38.465  1.00 72.99  ? 163 SER D C   1 
ATOM   5134 O  O   . SER D 2 162 ? 137.518 192.920 39.481  1.00 75.70  ? 163 SER D O   1 
ATOM   5135 C  CB  . SER D 2 162 ? 136.661 193.182 36.426  1.00 71.91  ? 163 SER D CB  1 
ATOM   5136 O  OG  . SER D 2 162 ? 136.558 194.587 36.649  1.00 64.94  ? 163 SER D OG  1 
ATOM   5137 N  N   . ASP D 2 163 ? 138.994 194.268 38.453  1.00 73.19  ? 164 ASP D N   1 
ATOM   5138 C  CA  . ASP D 2 163 ? 139.215 195.117 39.615  1.00 78.42  ? 164 ASP D CA  1 
ATOM   5139 C  C   . ASP D 2 163 ? 137.984 195.966 39.976  1.00 80.79  ? 164 ASP D C   1 
ATOM   5140 O  O   . ASP D 2 163 ? 137.889 196.480 41.094  1.00 87.80  ? 164 ASP D O   1 
ATOM   5141 C  CB  . ASP D 2 163 ? 140.445 196.006 39.381  1.00 81.26  ? 164 ASP D CB  1 
ATOM   5142 C  CG  . ASP D 2 163 ? 140.539 196.517 37.951  1.00 81.62  ? 164 ASP D CG  1 
ATOM   5143 O  OD1 . ASP D 2 163 ? 139.491 196.841 37.353  1.00 77.86  1 164 ASP D OD1 1 
ATOM   5144 O  OD2 . ASP D 2 163 ? 141.671 196.571 37.420  1.00 70.92  ? 164 ASP D OD2 1 
ATOM   5145 N  N   . LEU D 2 164 ? 137.035 196.084 39.044  1.00 74.77  ? 165 LEU D N   1 
ATOM   5146 C  CA  . LEU D 2 164 ? 135.795 196.832 39.279  1.00 77.78  ? 165 LEU D CA  1 
ATOM   5147 C  C   . LEU D 2 164 ? 134.781 196.078 40.154  1.00 78.41  ? 165 LEU D C   1 
ATOM   5148 O  O   . LEU D 2 164 ? 133.603 196.440 40.192  1.00 73.57  ? 165 LEU D O   1 
ATOM   5149 C  CB  . LEU D 2 164 ? 135.132 197.198 37.945  1.00 72.88  ? 165 LEU D CB  1 
ATOM   5150 C  CG  . LEU D 2 164 ? 135.873 198.115 36.975  1.00 66.96  ? 165 LEU D CG  1 
ATOM   5151 C  CD1 . LEU D 2 164 ? 135.214 198.038 35.609  1.00 64.92  ? 165 LEU D CD1 1 
ATOM   5152 C  CD2 . LEU D 2 164 ? 135.870 199.547 37.490  1.00 57.83  ? 165 LEU D CD2 1 
ATOM   5153 N  N   . GLY D 2 165 ? 135.236 195.024 40.831  1.00 83.04  ? 166 GLY D N   1 
ATOM   5154 C  CA  . GLY D 2 165 ? 134.395 194.241 41.725  1.00 82.76  ? 166 GLY D CA  1 
ATOM   5155 C  C   . GLY D 2 165 ? 134.159 192.816 41.253  1.00 82.55  ? 166 GLY D C   1 
ATOM   5156 O  O   . GLY D 2 165 ? 134.563 192.445 40.147  1.00 81.38  ? 166 GLY D O   1 
ATOM   5157 N  N   . LYS D 2 166 ? 133.477 192.019 42.076  1.00 85.36  ? 167 LYS D N   1 
ATOM   5158 C  CA  . LYS D 2 166 ? 133.202 190.624 41.722  1.00 89.08  ? 167 LYS D CA  1 
ATOM   5159 C  C   . LYS D 2 166 ? 132.002 190.562 40.787  1.00 81.99  ? 167 LYS D C   1 
ATOM   5160 O  O   . LYS D 2 166 ? 131.253 191.538 40.660  1.00 76.52  ? 167 LYS D O   1 
ATOM   5161 C  CB  . LYS D 2 166 ? 132.962 189.751 42.964  1.00 95.17  ? 167 LYS D CB  1 
ATOM   5162 C  CG  . LYS D 2 166 ? 131.807 190.189 43.865  1.00 97.42  ? 167 LYS D CG  1 
ATOM   5163 C  CD  . LYS D 2 166 ? 131.579 189.189 45.002  1.00 93.06  ? 167 LYS D CD  1 
ATOM   5164 C  CE  . LYS D 2 166 ? 130.612 189.726 46.049  1.00 87.00  ? 167 LYS D CE  1 
ATOM   5165 N  NZ  . LYS D 2 166 ? 131.215 190.800 46.883  1.00 73.33  1 167 LYS D NZ  1 
ATOM   5166 N  N   . ASN D 2 167 ? 131.851 189.419 40.118  1.00 82.74  ? 168 ASN D N   1 
ATOM   5167 C  CA  . ASN D 2 167 ? 130.863 189.234 39.055  1.00 83.15  ? 168 ASN D CA  1 
ATOM   5168 C  C   . ASN D 2 167 ? 131.102 190.170 37.874  1.00 78.23  ? 168 ASN D C   1 
ATOM   5169 O  O   . ASN D 2 167 ? 130.197 190.391 37.067  1.00 76.37  ? 168 ASN D O   1 
ATOM   5170 C  CB  . ASN D 2 167 ? 129.437 189.439 39.571  1.00 86.70  ? 168 ASN D CB  1 
ATOM   5171 C  CG  . ASN D 2 167 ? 129.079 188.495 40.688  1.00 91.72  ? 168 ASN D CG  1 
ATOM   5172 O  OD1 . ASN D 2 167 ? 129.638 187.403 40.802  1.00 90.60  ? 168 ASN D OD1 1 
ATOM   5173 N  ND2 . ASN D 2 167 ? 128.134 188.909 41.525  1.00 88.40  ? 168 ASN D ND2 1 
ATOM   5174 N  N   . LEU D 2 168 ? 132.305 190.732 37.786  1.00 70.56  ? 169 LEU D N   1 
ATOM   5175 C  CA  . LEU D 2 168 ? 132.685 191.546 36.638  1.00 66.64  ? 169 LEU D CA  1 
ATOM   5176 C  C   . LEU D 2 168 ? 133.952 190.962 36.062  1.00 65.05  ? 169 LEU D C   1 
ATOM   5177 O  O   . LEU D 2 168 ? 134.840 190.543 36.807  1.00 64.88  ? 169 LEU D O   1 
ATOM   5178 C  CB  . LEU D 2 168 ? 132.887 193.011 37.022  1.00 58.05  ? 169 LEU D CB  1 
ATOM   5179 C  CG  . LEU D 2 168 ? 131.613 193.727 37.463  1.00 58.35  ? 169 LEU D CG  1 
ATOM   5180 C  CD1 . LEU D 2 168 ? 131.852 195.213 37.619  1.00 54.80  ? 169 LEU D CD1 1 
ATOM   5181 C  CD2 . LEU D 2 168 ? 130.497 193.465 36.482  1.00 54.94  ? 169 LEU D CD2 1 
ATOM   5182 N  N   . TYR D 2 169 ? 134.057 190.960 34.739  1.00 63.01  ? 170 TYR D N   1 
ATOM   5183 C  CA  . TYR D 2 169 ? 135.202 190.334 34.097  1.00 59.05  ? 170 TYR D CA  1 
ATOM   5184 C  C   . TYR D 2 169 ? 135.904 191.278 33.135  1.00 61.07  ? 170 TYR D C   1 
ATOM   5185 O  O   . TYR D 2 169 ? 135.365 192.323 32.756  1.00 61.63  ? 170 TYR D O   1 
ATOM   5186 C  CB  . TYR D 2 169 ? 134.764 189.054 33.379  1.00 59.53  ? 170 TYR D CB  1 
ATOM   5187 C  CG  . TYR D 2 169 ? 134.030 188.137 34.326  1.00 74.81  ? 170 TYR D CG  1 
ATOM   5188 C  CD1 . TYR D 2 169 ? 134.728 187.327 35.224  1.00 68.67  ? 170 TYR D CD1 1 
ATOM   5189 C  CD2 . TYR D 2 169 ? 132.635 188.105 34.352  1.00 72.12  ? 170 TYR D CD2 1 
ATOM   5190 C  CE1 . TYR D 2 169 ? 134.054 186.503 36.116  1.00 65.82  ? 170 TYR D CE1 1 
ATOM   5191 C  CE2 . TYR D 2 169 ? 131.954 187.274 35.238  1.00 71.52  ? 170 TYR D CE2 1 
ATOM   5192 C  CZ  . TYR D 2 169 ? 132.670 186.479 36.118  1.00 68.11  ? 170 TYR D CZ  1 
ATOM   5193 O  OH  . TYR D 2 169 ? 131.995 185.666 37.001  1.00 74.84  ? 170 TYR D OH  1 
ATOM   5194 N  N   . SER D 2 170 ? 137.130 190.909 32.777  1.00 53.92  ? 171 SER D N   1 
ATOM   5195 C  CA  . SER D 2 170 ? 137.975 191.724 31.938  1.00 46.20  ? 171 SER D CA  1 
ATOM   5196 C  C   . SER D 2 170 ? 138.657 190.828 30.933  1.00 56.39  ? 171 SER D C   1 
ATOM   5197 O  O   . SER D 2 170 ? 138.735 189.621 31.119  1.00 61.33  ? 171 SER D O   1 
ATOM   5198 C  CB  . SER D 2 170 ? 138.998 192.503 32.780  1.00 55.62  ? 171 SER D CB  1 
ATOM   5199 O  OG  . SER D 2 170 ? 139.983 191.665 33.362  1.00 56.12  ? 171 SER D OG  1 
ATOM   5200 N  N   . GLY D 2 171 ? 139.134 191.423 29.854  1.00 51.17  ? 172 GLY D N   1 
ATOM   5201 C  CA  . GLY D 2 171 ? 139.874 190.694 28.849  1.00 46.67  ? 172 GLY D CA  1 
ATOM   5202 C  C   . GLY D 2 171 ? 140.650 191.701 28.022  1.00 54.55  ? 172 GLY D C   1 
ATOM   5203 O  O   . GLY D 2 171 ? 140.335 192.900 28.019  1.00 51.98  ? 172 GLY D O   1 
ATOM   5204 N  N   . LYS D 2 172 ? 141.661 191.215 27.316  1.00 50.36  ? 173 LYS D N   1 
ATOM   5205 C  CA  . LYS D 2 172 ? 142.459 192.063 26.444  1.00 54.36  ? 173 LYS D CA  1 
ATOM   5206 C  C   . LYS D 2 172 ? 142.997 191.224 25.320  1.00 51.38  ? 173 LYS D C   1 
ATOM   5207 O  O   . LYS D 2 172 ? 143.254 190.044 25.495  1.00 53.92  ? 173 LYS D O   1 
ATOM   5208 C  CB  . LYS D 2 172 ? 143.610 192.722 27.210  1.00 52.62  ? 173 LYS D CB  1 
ATOM   5209 C  CG  . LYS D 2 172 ? 144.599 191.738 27.812  1.00 54.93  ? 173 LYS D CG  1 
ATOM   5210 C  CD  . LYS D 2 172 ? 145.792 192.446 28.471  1.00 70.81  ? 173 LYS D CD  1 
ATOM   5211 C  CE  . LYS D 2 172 ? 146.809 191.455 29.059  1.00 80.19  ? 173 LYS D CE  1 
ATOM   5212 N  NZ  . LYS D 2 172 ? 147.852 192.123 29.910  1.00 81.63  1 173 LYS D NZ  1 
ATOM   5213 N  N   . THR D 2 173 ? 143.172 191.827 24.159  1.00 53.72  ? 174 THR D N   1 
ATOM   5214 C  CA  . THR D 2 173 ? 143.730 191.093 23.042  1.00 49.82  ? 174 THR D CA  1 
ATOM   5215 C  C   . THR D 2 173 ? 144.181 192.034 21.949  1.00 48.80  ? 174 THR D C   1 
ATOM   5216 O  O   . THR D 2 173 ? 143.742 193.188 21.882  1.00 50.49  ? 174 THR D O   1 
ATOM   5217 C  CB  . THR D 2 173 ? 142.698 190.077 22.462  1.00 58.20  ? 174 THR D CB  1 
ATOM   5218 O  OG1 . THR D 2 173 ? 143.349 189.180 21.550  1.00 69.07  ? 174 THR D OG1 1 
ATOM   5219 C  CG2 . THR D 2 173 ? 141.538 190.798 21.758  1.00 53.51  ? 174 THR D CG2 1 
ATOM   5220 N  N   . PHE D 2 174 ? 145.103 191.543 21.133  1.00 43.82  ? 175 PHE D N   1 
ATOM   5221 C  CA  . PHE D 2 174 ? 145.440 192.181 19.878  1.00 52.91  ? 175 PHE D CA  1 
ATOM   5222 C  C   . PHE D 2 174 ? 144.710 191.494 18.738  1.00 52.57  ? 175 PHE D C   1 
ATOM   5223 O  O   . PHE D 2 174 ? 144.684 190.271 18.662  1.00 59.20  ? 175 PHE D O   1 
ATOM   5224 C  CB  . PHE D 2 174 ? 146.947 192.149 19.635  1.00 52.21  ? 175 PHE D CB  1 
ATOM   5225 C  CG  . PHE D 2 174 ? 147.702 193.148 20.451  1.00 59.03  ? 175 PHE D CG  1 
ATOM   5226 C  CD1 . PHE D 2 174 ? 148.179 192.816 21.703  1.00 55.89  ? 175 PHE D CD1 1 
ATOM   5227 C  CD2 . PHE D 2 174 ? 147.919 194.428 19.969  1.00 59.24  ? 175 PHE D CD2 1 
ATOM   5228 C  CE1 . PHE D 2 174 ? 148.872 193.736 22.459  1.00 60.72  ? 175 PHE D CE1 1 
ATOM   5229 C  CE2 . PHE D 2 174 ? 148.606 195.354 20.721  1.00 64.60  ? 175 PHE D CE2 1 
ATOM   5230 C  CZ  . PHE D 2 174 ? 149.084 195.009 21.969  1.00 62.42  ? 175 PHE D CZ  1 
ATOM   5231 N  N   . LEU D 2 175 ? 144.103 192.290 17.869  1.00 51.00  ? 176 LEU D N   1 
ATOM   5232 C  CA  . LEU D 2 175 ? 143.527 191.792 16.630  1.00 49.62  ? 176 LEU D CA  1 
ATOM   5233 C  C   . LEU D 2 175 ? 144.304 192.392 15.492  1.00 50.56  ? 176 LEU D C   1 
ATOM   5234 O  O   . LEU D 2 175 ? 145.146 193.254 15.702  1.00 54.09  ? 176 LEU D O   1 
ATOM   5235 C  CB  . LEU D 2 175 ? 142.042 192.149 16.490  1.00 45.76  ? 176 LEU D CB  1 
ATOM   5236 C  CG  . LEU D 2 175 ? 141.105 191.633 17.577  1.00 52.51  ? 176 LEU D CG  1 
ATOM   5237 C  CD1 . LEU D 2 175 ? 139.690 192.150 17.324  1.00 52.87  ? 176 LEU D CD1 1 
ATOM   5238 C  CD2 . LEU D 2 175 ? 141.142 190.113 17.634  1.00 51.63  ? 176 LEU D CD2 1 
ATOM   5239 N  N   . SER D 2 176 ? 144.030 191.926 14.284  1.00 50.72  ? 177 SER D N   1 
ATOM   5240 C  CA  . SER D 2 176 ? 144.647 192.499 13.107  1.00 50.53  ? 177 SER D CA  1 
ATOM   5241 C  C   . SER D 2 176 ? 143.656 192.476 11.948  1.00 49.77  ? 177 SER D C   1 
ATOM   5242 O  O   . SER D 2 176 ? 142.705 191.697 11.952  1.00 55.29  ? 177 SER D O   1 
ATOM   5243 C  CB  . SER D 2 176 ? 145.935 191.756 12.750  1.00 57.35  ? 177 SER D CB  1 
ATOM   5244 O  OG  . SER D 2 176 ? 146.311 192.039 11.408  1.00 74.97  ? 177 SER D OG  1 
ATOM   5245 N  N   . ALA D 2 177 ? 143.858 193.354 10.975  1.00 52.91  ? 178 ALA D N   1 
ATOM   5246 C  CA  . ALA D 2 177 ? 143.009 193.374 9.792   1.00 53.45  ? 178 ALA D CA  1 
ATOM   5247 C  C   . ALA D 2 177 ? 143.842 193.807 8.603   1.00 59.09  ? 178 ALA D C   1 
ATOM   5248 O  O   . ALA D 2 177 ? 144.753 194.622 8.733   1.00 65.94  ? 178 ALA D O   1 
ATOM   5249 C  CB  . ALA D 2 177 ? 141.819 194.305 9.979   1.00 53.99  ? 178 ALA D CB  1 
ATOM   5250 N  N   . PRO D 2 178 ? 143.546 193.242 7.433   1.00 64.36  ? 179 PRO D N   1 
ATOM   5251 C  CA  . PRO D 2 178 ? 144.227 193.651 6.205   1.00 57.09  ? 179 PRO D CA  1 
ATOM   5252 C  C   . PRO D 2 178 ? 143.591 194.909 5.637   1.00 60.99  ? 179 PRO D C   1 
ATOM   5253 O  O   . PRO D 2 178 ? 143.293 194.988 4.442   1.00 58.16  ? 179 PRO D O   1 
ATOM   5254 C  CB  . PRO D 2 178 ? 144.027 192.454 5.283   1.00 58.67  ? 179 PRO D CB  1 
ATOM   5255 C  CG  . PRO D 2 178 ? 142.707 191.881 5.729   1.00 61.03  ? 179 PRO D CG  1 
ATOM   5256 C  CD  . PRO D 2 178 ? 142.627 192.108 7.217   1.00 50.76  ? 179 PRO D CD  1 
ATOM   5257 N  N   . LEU D 2 179 ? 143.407 195.901 6.504   1.00 57.71  ? 180 LEU D N   1 
ATOM   5258 C  CA  . LEU D 2 179 ? 142.750 197.149 6.128   1.00 59.95  ? 180 LEU D CA  1 
ATOM   5259 C  C   . LEU D 2 179 ? 143.559 198.348 6.609   1.00 55.21  ? 180 LEU D C   1 
ATOM   5260 O  O   . LEU D 2 179 ? 144.156 198.296 7.677   1.00 53.99  ? 180 LEU D O   1 
ATOM   5261 C  CB  . LEU D 2 179 ? 141.331 197.190 6.709   1.00 53.06  ? 180 LEU D CB  1 
ATOM   5262 C  CG  . LEU D 2 179 ? 140.390 196.097 6.188   1.00 57.28  ? 180 LEU D CG  1 
ATOM   5263 C  CD1 . LEU D 2 179 ? 139.227 195.846 7.147   1.00 50.24  ? 180 LEU D CD1 1 
ATOM   5264 C  CD2 . LEU D 2 179 ? 139.880 196.479 4.789   1.00 58.25  ? 180 LEU D CD2 1 
ATOM   5265 N  N   . PRO D 2 180 ? 143.618 199.414 5.799   1.00 50.49  ? 181 PRO D N   1 
ATOM   5266 C  CA  . PRO D 2 180 ? 144.217 200.667 6.269   1.00 57.30  ? 181 PRO D CA  1 
ATOM   5267 C  C   . PRO D 2 180 ? 143.242 201.442 7.183   1.00 53.44  ? 181 PRO D C   1 
ATOM   5268 O  O   . PRO D 2 180 ? 142.019 201.264 7.132   1.00 48.75  ? 181 PRO D O   1 
ATOM   5269 C  CB  . PRO D 2 180 ? 144.514 201.423 4.968   1.00 49.91  ? 181 PRO D CB  1 
ATOM   5270 C  CG  . PRO D 2 180 ? 143.459 200.939 4.028   1.00 48.45  ? 181 PRO D CG  1 
ATOM   5271 C  CD  . PRO D 2 180 ? 143.217 199.491 4.384   1.00 52.74  ? 181 PRO D CD  1 
ATOM   5272 N  N   . THR D 2 181 ? 143.799 202.291 8.033   1.00 46.99  ? 182 THR D N   1 
ATOM   5273 C  CA  . THR D 2 181 ? 143.015 203.011 9.028   1.00 42.89  ? 182 THR D CA  1 
ATOM   5274 C  C   . THR D 2 181 ? 141.960 203.927 8.409   1.00 45.19  ? 182 THR D C   1 
ATOM   5275 O  O   . THR D 2 181 ? 140.854 204.045 8.952   1.00 45.15  ? 182 THR D O   1 
ATOM   5276 C  CB  . THR D 2 181 ? 143.938 203.785 9.950   1.00 42.56  ? 182 THR D CB  1 
ATOM   5277 O  OG1 . THR D 2 181 ? 144.618 202.844 10.787  1.00 50.45  ? 182 THR D OG1 1 
ATOM   5278 C  CG2 . THR D 2 181 ? 143.165 204.745 10.824  1.00 46.13  ? 182 THR D CG2 1 
ATOM   5279 N  N   . TRP D 2 182 ? 142.288 204.541 7.269   1.00 44.86  ? 183 TRP D N   1 
ATOM   5280 C  CA  . TRP D 2 182 ? 141.409 205.533 6.649   1.00 48.60  ? 183 TRP D CA  1 
ATOM   5281 C  C   . TRP D 2 182 ? 140.082 204.909 6.227   1.00 46.31  ? 183 TRP D C   1 
ATOM   5282 O  O   . TRP D 2 182 ? 139.092 205.617 6.023   1.00 50.08  ? 183 TRP D O   1 
ATOM   5283 C  CB  . TRP D 2 182 ? 142.077 206.192 5.429   1.00 43.91  ? 183 TRP D CB  1 
ATOM   5284 C  CG  . TRP D 2 182 ? 142.260 205.296 4.231   1.00 51.98  ? 183 TRP D CG  1 
ATOM   5285 C  CD1 . TRP D 2 182 ? 143.382 204.583 3.888   1.00 47.66  ? 183 TRP D CD1 1 
ATOM   5286 C  CD2 . TRP D 2 182 ? 141.295 205.037 3.201   1.00 49.06  ? 183 TRP D CD2 1 
ATOM   5287 N  NE1 . TRP D 2 182 ? 143.164 203.886 2.718   1.00 46.48  ? 183 TRP D NE1 1 
ATOM   5288 C  CE2 . TRP D 2 182 ? 141.892 204.151 2.278   1.00 52.95  ? 183 TRP D CE2 1 
ATOM   5289 C  CE3 . TRP D 2 182 ? 139.982 205.462 2.976   1.00 45.90  ? 183 TRP D CE3 1 
ATOM   5290 C  CZ2 . TRP D 2 182 ? 141.221 203.689 1.150   1.00 52.18  ? 183 TRP D CZ2 1 
ATOM   5291 C  CZ3 . TRP D 2 182 ? 139.316 204.999 1.857   1.00 55.59  ? 183 TRP D CZ3 1 
ATOM   5292 C  CH2 . TRP D 2 182 ? 139.936 204.125 0.957   1.00 53.28  ? 183 TRP D CH2 1 
ATOM   5293 N  N   . GLN D 2 183 ? 140.068 203.588 6.085   1.00 44.05  ? 184 GLN D N   1 
ATOM   5294 C  CA  . GLN D 2 183 ? 138.861 202.867 5.676   1.00 45.84  ? 184 GLN D CA  1 
ATOM   5295 C  C   . GLN D 2 183 ? 137.940 202.555 6.852   1.00 44.39  ? 184 GLN D C   1 
ATOM   5296 O  O   . GLN D 2 183 ? 136.755 202.281 6.665   1.00 45.24  ? 184 GLN D O   1 
ATOM   5297 C  CB  . GLN D 2 183 ? 139.249 201.574 4.969   1.00 48.54  ? 184 GLN D CB  1 
ATOM   5298 C  CG  . GLN D 2 183 ? 139.300 201.686 3.450   1.00 59.09  ? 184 GLN D CG  1 
ATOM   5299 C  CD  . GLN D 2 183 ? 139.594 200.355 2.780   1.00 66.01  ? 184 GLN D CD  1 
ATOM   5300 O  OE1 . GLN D 2 183 ? 140.740 200.076 2.429   1.00 66.20  ? 184 GLN D OE1 1 
ATOM   5301 N  NE2 . GLN D 2 183 ? 138.566 199.532 2.595   1.00 66.12  ? 184 GLN D NE2 1 
ATOM   5302 N  N   . LEU D 2 184 ? 138.481 202.635 8.062   1.00 39.85  ? 185 LEU D N   1 
ATOM   5303 C  CA  . LEU D 2 184 ? 137.728 202.315 9.271   1.00 36.57  ? 185 LEU D CA  1 
ATOM   5304 C  C   . LEU D 2 184 ? 137.100 203.572 9.885   1.00 42.80  ? 185 LEU D C   1 
ATOM   5305 O  O   . LEU D 2 184 ? 136.162 203.484 10.705  1.00 42.72  ? 185 LEU D O   1 
ATOM   5306 C  CB  . LEU D 2 184 ? 138.644 201.648 10.296  1.00 34.12  ? 185 LEU D CB  1 
ATOM   5307 C  CG  . LEU D 2 184 ? 139.650 200.609 9.797   1.00 38.72  ? 185 LEU D CG  1 
ATOM   5308 C  CD1 . LEU D 2 184 ? 140.656 200.275 10.871  1.00 38.50  ? 185 LEU D CD1 1 
ATOM   5309 C  CD2 . LEU D 2 184 ? 138.967 199.326 9.330   1.00 42.53  ? 185 LEU D CD2 1 
ATOM   5310 N  N   . ILE D 2 185 ? 137.623 204.737 9.488   1.00 37.60  ? 186 ILE D N   1 
ATOM   5311 C  CA  . ILE D 2 185 ? 137.199 205.996 10.079  1.00 38.89  ? 186 ILE D CA  1 
ATOM   5312 C  C   . ILE D 2 185 ? 135.707 206.233 9.878   1.00 37.75  ? 186 ILE D C   1 
ATOM   5313 O  O   . ILE D 2 185 ? 135.216 206.181 8.753   1.00 41.54  ? 186 ILE D O   1 
ATOM   5314 C  CB  . ILE D 2 185 ? 137.970 207.174 9.482   1.00 42.07  ? 186 ILE D CB  1 
ATOM   5315 C  CG1 . ILE D 2 185 ? 139.474 207.014 9.758   1.00 29.85  ? 186 ILE D CG1 1 
ATOM   5316 C  CG2 . ILE D 2 185 ? 137.392 208.500 10.015  1.00 34.33  ? 186 ILE D CG2 1 
ATOM   5317 C  CD1 . ILE D 2 185 ? 139.822 206.833 11.235  1.00 32.03  ? 186 ILE D CD1 1 
ATOM   5318 N  N   . GLY D 2 186 ? 134.991 206.481 10.973  1.00 32.18  ? 187 GLY D N   1 
ATOM   5319 C  CA  . GLY D 2 186 ? 133.578 206.789 10.882  1.00 34.53  ? 187 GLY D CA  1 
ATOM   5320 C  C   . GLY D 2 186 ? 132.649 205.585 10.911  1.00 35.05  ? 187 GLY D C   1 
ATOM   5321 O  O   . GLY D 2 186 ? 131.445 205.760 10.882  1.00 36.76  ? 187 GLY D O   1 
ATOM   5322 N  N   . ARG D 2 187 ? 133.197 204.373 10.949  1.00 32.31  ? 188 ARG D N   1 
ATOM   5323 C  CA  . ARG D 2 187 ? 132.380 203.167 11.044  1.00 36.64  ? 188 ARG D CA  1 
ATOM   5324 C  C   . ARG D 2 187 ? 132.217 202.778 12.499  1.00 36.60  ? 188 ARG D C   1 
ATOM   5325 O  O   . ARG D 2 187 ? 132.686 203.488 13.377  1.00 43.47  ? 188 ARG D O   1 
ATOM   5326 C  CB  . ARG D 2 187 ? 133.000 202.011 10.259  1.00 37.17  ? 188 ARG D CB  1 
ATOM   5327 C  CG  . ARG D 2 187 ? 133.220 202.328 8.775   1.00 40.53  ? 188 ARG D CG  1 
ATOM   5328 C  CD  . ARG D 2 187 ? 133.824 201.136 8.064   1.00 46.88  ? 188 ARG D CD  1 
ATOM   5329 N  NE  . ARG D 2 187 ? 134.190 201.407 6.676   1.00 50.75  ? 188 ARG D NE  1 
ATOM   5330 C  CZ  . ARG D 2 187 ? 133.328 201.713 5.714   1.00 51.88  ? 188 ARG D CZ  1 
ATOM   5331 N  NH1 . ARG D 2 187 ? 132.035 201.838 5.985   1.00 45.58  1 188 ARG D NH1 1 
ATOM   5332 N  NH2 . ARG D 2 187 ? 133.770 201.919 4.483   1.00 53.87  ? 188 ARG D NH2 1 
ATOM   5333 N  N   . SER D 2 188 ? 131.524 201.672 12.755  1.00 40.55  ? 189 SER D N   1 
ATOM   5334 C  CA  . SER D 2 188 ? 131.293 201.222 14.123  1.00 40.32  ? 189 SER D CA  1 
ATOM   5335 C  C   . SER D 2 188 ? 132.143 200.020 14.507  1.00 41.12  ? 189 SER D C   1 
ATOM   5336 O  O   . SER D 2 188 ? 132.279 199.078 13.742  1.00 48.92  ? 189 SER D O   1 
ATOM   5337 C  CB  . SER D 2 188 ? 129.824 200.885 14.339  1.00 38.68  ? 189 SER D CB  1 
ATOM   5338 O  OG  . SER D 2 188 ? 129.079 202.064 14.583  1.00 50.20  ? 189 SER D OG  1 
ATOM   5339 N  N   . PHE D 2 189 ? 132.718 200.077 15.700  1.00 39.95  ? 190 PHE D N   1 
ATOM   5340 C  CA  . PHE D 2 189 ? 133.381 198.927 16.295  1.00 39.50  ? 190 PHE D CA  1 
ATOM   5341 C  C   . PHE D 2 189 ? 132.456 198.308 17.349  1.00 42.01  ? 190 PHE D C   1 
ATOM   5342 O  O   . PHE D 2 189 ? 131.943 199.000 18.246  1.00 37.94  ? 190 PHE D O   1 
ATOM   5343 C  CB  . PHE D 2 189 ? 134.711 199.335 16.921  1.00 42.22  ? 190 PHE D CB  1 
ATOM   5344 C  CG  . PHE D 2 189 ? 135.622 198.182 17.203  1.00 42.21  ? 190 PHE D CG  1 
ATOM   5345 C  CD1 . PHE D 2 189 ? 135.530 197.478 18.396  1.00 36.47  ? 190 PHE D CD1 1 
ATOM   5346 C  CD2 . PHE D 2 189 ? 136.558 197.786 16.258  1.00 38.93  ? 190 PHE D CD2 1 
ATOM   5347 C  CE1 . PHE D 2 189 ? 136.379 196.410 18.636  1.00 42.54  ? 190 PHE D CE1 1 
ATOM   5348 C  CE2 . PHE D 2 189 ? 137.398 196.719 16.494  1.00 41.28  ? 190 PHE D CE2 1 
ATOM   5349 C  CZ  . PHE D 2 189 ? 137.314 196.030 17.673  1.00 39.80  ? 190 PHE D CZ  1 
ATOM   5350 N  N   . VAL D 2 190 ? 132.226 197.006 17.229  1.00 39.66  ? 191 VAL D N   1 
ATOM   5351 C  CA  . VAL D 2 190 ? 131.231 196.345 18.064  1.00 39.07  ? 191 VAL D CA  1 
ATOM   5352 C  C   . VAL D 2 190 ? 131.787 195.106 18.738  1.00 42.97  ? 191 VAL D C   1 
ATOM   5353 O  O   . VAL D 2 190 ? 132.399 194.243 18.092  1.00 46.36  ? 191 VAL D O   1 
ATOM   5354 C  CB  . VAL D 2 190 ? 129.987 195.951 17.239  1.00 40.16  ? 191 VAL D CB  1 
ATOM   5355 C  CG1 . VAL D 2 190 ? 128.989 195.208 18.123  1.00 41.45  ? 191 VAL D CG1 1 
ATOM   5356 C  CG2 . VAL D 2 190 ? 129.350 197.179 16.621  1.00 32.02  ? 191 VAL D CG2 1 
ATOM   5357 N  N   . ILE D 2 191 ? 131.598 195.031 20.050  1.00 43.39  ? 192 ILE D N   1 
ATOM   5358 C  CA  . ILE D 2 191 ? 131.957 193.826 20.779  1.00 39.45  ? 192 ILE D CA  1 
ATOM   5359 C  C   . ILE D 2 191 ? 130.676 193.336 21.434  1.00 49.53  ? 192 ILE D C   1 
ATOM   5360 O  O   . ILE D 2 191 ? 129.955 194.108 22.057  1.00 49.91  ? 192 ILE D O   1 
ATOM   5361 C  CB  . ILE D 2 191 ? 133.076 194.061 21.822  1.00 41.93  ? 192 ILE D CB  1 
ATOM   5362 C  CG1 . ILE D 2 191 ? 134.373 194.487 21.129  1.00 42.60  ? 192 ILE D CG1 1 
ATOM   5363 C  CG2 . ILE D 2 191 ? 133.348 192.792 22.631  1.00 41.31  ? 192 ILE D CG2 1 
ATOM   5364 C  CD1 . ILE D 2 191 ? 135.523 194.723 22.091  1.00 38.37  ? 192 ILE D CD1 1 
ATOM   5365 N  N   . SER D 2 192 ? 130.367 192.061 21.231  1.00 53.51  ? 193 SER D N   1 
ATOM   5366 C  CA  . SER D 2 192 ? 129.164 191.471 21.790  1.00 56.22  ? 193 SER D CA  1 
ATOM   5367 C  C   . SER D 2 192 ? 129.357 189.999 22.095  1.00 57.90  ? 193 SER D C   1 
ATOM   5368 O  O   . SER D 2 192 ? 130.331 189.371 21.674  1.00 52.14  ? 193 SER D O   1 
ATOM   5369 C  CB  . SER D 2 192 ? 127.965 191.634 20.847  1.00 48.68  ? 193 SER D CB  1 
ATOM   5370 O  OG  . SER D 2 192 ? 128.285 191.164 19.556  1.00 55.84  ? 193 SER D OG  1 
ATOM   5371 N  N   . LYS D 2 193 ? 128.416 189.479 22.866  1.00 54.70  ? 194 LYS D N   1 
ATOM   5372 C  CA  . LYS D 2 193 ? 128.307 188.062 23.164  1.00 56.42  ? 194 LYS D CA  1 
ATOM   5373 C  C   . LYS D 2 193 ? 126.829 187.716 23.289  1.00 60.58  ? 194 LYS D C   1 
ATOM   5374 O  O   . LYS D 2 193 ? 126.015 188.565 23.688  1.00 53.38  ? 194 LYS D O   1 
ATOM   5375 C  CB  . LYS D 2 193 ? 129.062 187.706 24.450  1.00 48.18  ? 194 LYS D CB  1 
ATOM   5376 C  CG  . LYS D 2 193 ? 129.063 186.214 24.819  1.00 45.91  ? 194 LYS D CG  1 
ATOM   5377 C  CD  . LYS D 2 193 ? 129.785 185.996 26.147  1.00 51.98  ? 194 LYS D CD  1 
ATOM   5378 C  CE  . LYS D 2 193 ? 128.993 186.523 27.361  1.00 52.13  ? 194 LYS D CE  1 
ATOM   5379 N  NZ  . LYS D 2 193 ? 127.756 185.754 27.672  1.00 48.65  1 194 LYS D NZ  1 
ATOM   5380 N  N   . SER D 2 194 ? 126.479 186.492 22.904  1.00 61.72  ? 195 SER D N   1 
ATOM   5381 C  CA  . SER D 2 194 ? 125.148 185.964 23.163  1.00 49.93  ? 195 SER D CA  1 
ATOM   5382 C  C   . SER D 2 194 ? 124.931 185.958 24.676  1.00 53.81  ? 195 SER D C   1 
ATOM   5383 O  O   . SER D 2 194 ? 125.786 185.467 25.423  1.00 51.40  ? 195 SER D O   1 
ATOM   5384 C  CB  . SER D 2 194 ? 125.037 184.558 22.598  1.00 51.42  ? 195 SER D CB  1 
ATOM   5385 O  OG  . SER D 2 194 ? 125.433 184.558 21.232  1.00 74.16  ? 195 SER D OG  1 
ATOM   5386 N  N   . LEU D 2 195 ? 123.804 186.498 25.134  1.00 54.80  ? 196 LEU D N   1 
ATOM   5387 C  CA  . LEU D 2 195 ? 123.477 186.465 26.565  1.00 58.32  ? 196 LEU D CA  1 
ATOM   5388 C  C   . LEU D 2 195 ? 123.324 185.029 27.083  1.00 64.72  ? 196 LEU D C   1 
ATOM   5389 O  O   . LEU D 2 195 ? 122.808 184.151 26.389  1.00 67.32  ? 196 LEU D O   1 
ATOM   5390 C  CB  . LEU D 2 195 ? 122.184 187.230 26.850  1.00 56.42  ? 196 LEU D CB  1 
ATOM   5391 C  CG  . LEU D 2 195 ? 122.113 188.747 26.720  1.00 59.83  ? 196 LEU D CG  1 
ATOM   5392 C  CD1 . LEU D 2 195 ? 120.689 189.193 26.368  1.00 65.82  ? 196 LEU D CD1 1 
ATOM   5393 C  CD2 . LEU D 2 195 ? 122.558 189.376 28.016  1.00 54.63  ? 196 LEU D CD2 1 
ATOM   5394 N  N   . ASN D 2 196 ? 123.788 184.776 28.296  1.00 64.18  ? 197 ASN D N   1 
ATOM   5395 C  CA  . ASN D 2 196 ? 123.499 183.488 28.913  1.00 71.64  ? 197 ASN D CA  1 
ATOM   5396 C  C   . ASN D 2 196 ? 122.006 183.340 29.277  1.00 66.46  ? 197 ASN D C   1 
ATOM   5397 O  O   . ASN D 2 196 ? 121.433 182.260 29.146  1.00 74.72  ? 197 ASN D O   1 
ATOM   5398 C  CB  . ASN D 2 196 ? 124.389 183.288 30.135  1.00 67.28  ? 197 ASN D CB  1 
ATOM   5399 C  CG  . ASN D 2 196 ? 125.849 183.175 29.760  1.00 62.75  ? 197 ASN D CG  1 
ATOM   5400 O  OD1 . ASN D 2 196 ? 126.184 182.868 28.612  1.00 66.67  ? 197 ASN D OD1 1 
ATOM   5401 N  ND2 . ASN D 2 196 ? 126.728 183.443 30.717  1.00 67.86  ? 197 ASN D ND2 1 
ATOM   5402 N  N   . HIS D 2 197 ? 121.373 184.421 29.716  1.00 67.36  ? 198 HIS D N   1 
ATOM   5403 C  CA  . HIS D 2 197 ? 119.969 184.342 30.109  1.00 73.37  ? 198 HIS D CA  1 
ATOM   5404 C  C   . HIS D 2 197 ? 119.095 185.370 29.374  1.00 66.15  ? 198 HIS D C   1 
ATOM   5405 O  O   . HIS D 2 197 ? 118.682 186.368 29.966  1.00 68.50  ? 198 HIS D O   1 
ATOM   5406 C  CB  . HIS D 2 197 ? 119.835 184.517 31.633  1.00 74.02  ? 198 HIS D CB  1 
ATOM   5407 C  CG  . HIS D 2 197 ? 120.574 183.482 32.432  1.00 79.32  ? 198 HIS D CG  1 
ATOM   5408 N  ND1 . HIS D 2 197 ? 120.269 182.137 32.376  1.00 80.40  ? 198 HIS D ND1 1 
ATOM   5409 C  CD2 . HIS D 2 197 ? 121.606 183.594 33.304  1.00 79.77  ? 198 HIS D CD2 1 
ATOM   5410 C  CE1 . HIS D 2 197 ? 121.081 181.468 33.176  1.00 78.25  ? 198 HIS D CE1 1 
ATOM   5411 N  NE2 . HIS D 2 197 ? 121.902 182.328 33.752  1.00 72.36  ? 198 HIS D NE2 1 
ATOM   5412 N  N   . PRO D 2 198 ? 118.780 185.102 28.088  1.00 71.50  ? 199 PRO D N   1 
ATOM   5413 C  CA  . PRO D 2 198 ? 117.939 185.971 27.243  1.00 72.62  ? 199 PRO D CA  1 
ATOM   5414 C  C   . PRO D 2 198 ? 116.543 186.186 27.814  1.00 78.16  ? 199 PRO D C   1 
ATOM   5415 O  O   . PRO D 2 198 ? 115.908 187.211 27.563  1.00 77.99  ? 199 PRO D O   1 
ATOM   5416 C  CB  . PRO D 2 198 ? 117.847 185.202 25.918  1.00 64.92  ? 199 PRO D CB  1 
ATOM   5417 C  CG  . PRO D 2 198 ? 118.995 184.250 25.941  1.00 73.83  ? 199 PRO D CG  1 
ATOM   5418 C  CD  . PRO D 2 198 ? 119.208 183.888 27.370  1.00 57.98  ? 199 PRO D CD  1 
ATOM   5419 N  N   . GLU D 2 199 ? 116.073 185.181 28.546  1.00 80.48  ? 200 GLU D N   1 
ATOM   5420 C  CA  . GLU D 2 199 ? 114.789 185.200 29.234  1.00 79.65  ? 200 GLU D CA  1 
ATOM   5421 C  C   . GLU D 2 199 ? 114.587 186.421 30.132  1.00 90.07  ? 200 GLU D C   1 
ATOM   5422 O  O   . GLU D 2 199 ? 113.593 187.134 29.993  1.00 95.37  ? 200 GLU D O   1 
ATOM   5423 C  CB  . GLU D 2 199 ? 114.638 183.925 30.067  1.00 78.33  ? 200 GLU D CB  1 
ATOM   5424 C  CG  . GLU D 2 199 ? 115.640 182.832 29.704  1.00 79.86  ? 200 GLU D CG  1 
ATOM   5425 C  CD  . GLU D 2 199 ? 116.650 182.568 30.806  1.00 86.47  ? 200 GLU D CD  1 
ATOM   5426 O  OE1 . GLU D 2 199 ? 116.325 182.825 31.988  1.00 88.94  ? 200 GLU D OE1 1 
ATOM   5427 O  OE2 . GLU D 2 199 ? 117.772 182.105 30.487  1.00 87.57  1 200 GLU D OE2 1 
ATOM   5428 N  N   . ASN D 2 200 ? 115.528 186.648 31.051  1.00 84.03  ? 201 ASN D N   1 
ATOM   5429 C  CA  . ASN D 2 200 ? 115.411 187.715 32.048  1.00 77.89  ? 201 ASN D CA  1 
ATOM   5430 C  C   . ASN D 2 200 ? 115.511 189.121 31.490  1.00 85.50  ? 201 ASN D C   1 
ATOM   5431 O  O   . ASN D 2 200 ? 115.312 190.094 32.223  1.00 85.52  ? 201 ASN D O   1 
ATOM   5432 C  CB  . ASN D 2 200 ? 116.483 187.560 33.120  1.00 77.67  ? 201 ASN D CB  1 
ATOM   5433 C  CG  . ASN D 2 200 ? 116.484 186.193 33.736  1.00 83.08  ? 201 ASN D CG  1 
ATOM   5434 O  OD1 . ASN D 2 200 ? 115.438 185.557 33.857  1.00 89.57  ? 201 ASN D OD1 1 
ATOM   5435 N  ND2 . ASN D 2 200 ? 117.661 185.727 34.137  1.00 83.18  ? 201 ASN D ND2 1 
ATOM   5436 N  N   . GLU D 2 201 ? 115.849 189.234 30.208  1.00 83.08  ? 202 GLU D N   1 
ATOM   5437 C  CA  . GLU D 2 201 ? 115.961 190.545 29.585  1.00 88.82  ? 202 GLU D CA  1 
ATOM   5438 C  C   . GLU D 2 201 ? 114.674 190.796 28.797  1.00 86.88  ? 202 GLU D C   1 
ATOM   5439 O  O   . GLU D 2 201 ? 114.479 190.210 27.728  1.00 82.89  ? 202 GLU D O   1 
ATOM   5440 C  CB  . GLU D 2 201 ? 117.207 190.638 28.685  1.00 81.14  ? 202 GLU D CB  1 
ATOM   5441 C  CG  . GLU D 2 201 ? 118.559 190.376 29.397  1.00 74.55  ? 202 GLU D CG  1 
ATOM   5442 C  CD  . GLU D 2 201 ? 118.830 191.245 30.638  1.00 78.59  ? 202 GLU D CD  1 
ATOM   5443 O  OE1 . GLU D 2 201 ? 118.266 192.354 30.758  1.00 78.75  ? 202 GLU D OE1 1 
ATOM   5444 O  OE2 . GLU D 2 201 ? 119.642 190.817 31.492  1.00 74.64  1 202 GLU D OE2 1 
ATOM   5445 N  N   . PRO D 2 202 ? 113.801 191.681 29.328  1.00 97.78  ? 203 PRO D N   1 
ATOM   5446 C  CA  . PRO D 2 202 ? 112.428 191.926 28.845  1.00 101.28 ? 203 PRO D CA  1 
ATOM   5447 C  C   . PRO D 2 202 ? 112.339 192.354 27.381  1.00 99.28  ? 203 PRO D C   1 
ATOM   5448 O  O   . PRO D 2 202 ? 111.343 192.078 26.703  1.00 97.33  ? 203 PRO D O   1 
ATOM   5449 C  CB  . PRO D 2 202 ? 111.929 193.051 29.765  1.00 97.26  ? 203 PRO D CB  1 
ATOM   5450 C  CG  . PRO D 2 202 ? 113.175 193.718 30.278  1.00 94.68  ? 203 PRO D CG  1 
ATOM   5451 C  CD  . PRO D 2 202 ? 114.169 192.606 30.419  1.00 89.55  ? 203 PRO D CD  1 
ATOM   5452 N  N   . SER D 2 203 ? 113.382 193.024 26.910  1.00 90.64  ? 204 SER D N   1 
ATOM   5453 C  CA  . SER D 2 203 ? 113.386 193.645 25.595  1.00 94.63  ? 204 SER D CA  1 
ATOM   5454 C  C   . SER D 2 203 ? 113.328 192.656 24.419  1.00 96.46  ? 204 SER D C   1 
ATOM   5455 O  O   . SER D 2 203 ? 113.302 193.078 23.258  1.00 94.10  ? 204 SER D O   1 
ATOM   5456 C  CB  . SER D 2 203 ? 114.633 194.521 25.477  1.00 94.87  ? 204 SER D CB  1 
ATOM   5457 O  OG  . SER D 2 203 ? 115.265 194.644 26.746  1.00 87.22  ? 204 SER D OG  1 
ATOM   5458 N  N   . SER D 2 204 ? 113.311 191.356 24.715  1.00 87.26  ? 205 SER D N   1 
ATOM   5459 C  CA  . SER D 2 204 ? 113.429 190.333 23.679  1.00 86.86  ? 205 SER D CA  1 
ATOM   5460 C  C   . SER D 2 204 ? 114.752 190.541 22.932  1.00 95.19  ? 205 SER D C   1 
ATOM   5461 O  O   . SER D 2 204 ? 114.897 190.187 21.759  1.00 87.95  ? 205 SER D O   1 
ATOM   5462 C  CB  . SER D 2 204 ? 112.233 190.354 22.726  1.00 87.43  ? 205 SER D CB  1 
ATOM   5463 O  OG  . SER D 2 204 ? 111.014 190.293 23.445  1.00 86.84  ? 205 SER D OG  1 
ATOM   5464 N  N   . VAL D 2 205 ? 115.707 191.137 23.641  1.00 89.20  ? 206 VAL D N   1 
ATOM   5465 C  CA  . VAL D 2 205 ? 117.033 191.417 23.117  1.00 75.94  ? 206 VAL D CA  1 
ATOM   5466 C  C   . VAL D 2 205 ? 117.938 190.201 23.342  1.00 83.65  ? 206 VAL D C   1 
ATOM   5467 O  O   . VAL D 2 205 ? 118.003 189.664 24.454  1.00 77.34  ? 206 VAL D O   1 
ATOM   5468 C  CB  . VAL D 2 205 ? 117.639 192.670 23.787  1.00 82.70  ? 206 VAL D CB  1 
ATOM   5469 C  CG1 . VAL D 2 205 ? 117.590 192.548 25.305  1.00 77.29  ? 206 VAL D CG1 1 
ATOM   5470 C  CG2 . VAL D 2 205 ? 119.065 192.900 23.308  1.00 78.20  ? 206 VAL D CG2 1 
ATOM   5471 N  N   . LYS D 2 206 ? 118.665 189.792 22.301  1.00 74.50  ? 207 LYS D N   1 
ATOM   5472 C  CA  . LYS D 2 206 ? 119.396 188.529 22.354  1.00 74.81  ? 207 LYS D CA  1 
ATOM   5473 C  C   . LYS D 2 206 ? 120.861 188.642 22.790  1.00 72.10  ? 207 LYS D C   1 
ATOM   5474 O  O   . LYS D 2 206 ? 121.429 187.670 23.295  1.00 68.97  ? 207 LYS D O   1 
ATOM   5475 C  CB  . LYS D 2 206 ? 119.379 187.854 20.968  1.00 79.16  ? 207 LYS D CB  1 
ATOM   5476 C  CG  . LYS D 2 206 ? 118.023 187.726 20.259  1.00 81.81  ? 207 LYS D CG  1 
ATOM   5477 C  CD  . LYS D 2 206 ? 118.228 187.267 18.797  1.00 78.95  ? 207 LYS D CD  1 
ATOM   5478 C  CE  . LYS D 2 206 ? 116.937 187.274 17.971  1.00 75.62  ? 207 LYS D CE  1 
ATOM   5479 N  NZ  . LYS D 2 206 ? 116.008 186.159 18.320  1.00 76.99  1 207 LYS D NZ  1 
ATOM   5480 N  N   . ASP D 2 207 ? 121.462 189.820 22.616  1.00 72.27  ? 208 ASP D N   1 
ATOM   5481 C  CA  . ASP D 2 207 ? 122.915 189.973 22.787  1.00 65.70  ? 208 ASP D CA  1 
ATOM   5482 C  C   . ASP D 2 207 ? 123.367 191.027 23.797  1.00 60.09  ? 208 ASP D C   1 
ATOM   5483 O  O   . ASP D 2 207 ? 122.663 192.005 24.061  1.00 60.13  ? 208 ASP D O   1 
ATOM   5484 C  CB  . ASP D 2 207 ? 123.558 190.296 21.442  1.00 60.52  ? 208 ASP D CB  1 
ATOM   5485 C  CG  . ASP D 2 207 ? 123.558 189.119 20.510  1.00 71.22  ? 208 ASP D CG  1 
ATOM   5486 O  OD1 . ASP D 2 207 ? 123.537 187.970 21.004  1.00 76.07  ? 208 ASP D OD1 1 
ATOM   5487 O  OD2 . ASP D 2 207 ? 123.575 189.345 19.282  1.00 80.67  1 208 ASP D OD2 1 
ATOM   5488 N  N   . TYR D 2 208 ? 124.547 190.810 24.371  1.00 51.37  ? 209 TYR D N   1 
ATOM   5489 C  CA  . TYR D 2 208 ? 125.193 191.836 25.185  1.00 53.06  ? 209 TYR D CA  1 
ATOM   5490 C  C   . TYR D 2 208 ? 126.235 192.542 24.347  1.00 53.93  ? 209 TYR D C   1 
ATOM   5491 O  O   . TYR D 2 208 ? 127.264 191.955 24.024  1.00 50.11  ? 209 TYR D O   1 
ATOM   5492 C  CB  . TYR D 2 208 ? 125.850 191.242 26.429  1.00 47.51  ? 209 TYR D CB  1 
ATOM   5493 C  CG  . TYR D 2 208 ? 126.423 192.283 27.359  1.00 44.23  ? 209 TYR D CG  1 
ATOM   5494 C  CD1 . TYR D 2 208 ? 125.614 192.904 28.305  1.00 45.15  ? 209 TYR D CD1 1 
ATOM   5495 C  CD2 . TYR D 2 208 ? 127.767 192.651 27.297  1.00 47.57  ? 209 TYR D CD2 1 
ATOM   5496 C  CE1 . TYR D 2 208 ? 126.121 193.871 29.176  1.00 54.86  ? 209 TYR D CE1 1 
ATOM   5497 C  CE2 . TYR D 2 208 ? 128.286 193.620 28.163  1.00 45.77  ? 209 TYR D CE2 1 
ATOM   5498 C  CZ  . TYR D 2 208 ? 127.454 194.225 29.101  1.00 54.77  ? 209 TYR D CZ  1 
ATOM   5499 O  OH  . TYR D 2 208 ? 127.940 195.176 29.976  1.00 54.51  ? 209 TYR D OH  1 
ATOM   5500 N  N   . SER D 2 209 ? 125.975 193.802 24.014  1.00 51.62  ? 210 SER D N   1 
ATOM   5501 C  CA  . SER D 2 209 ? 126.805 194.532 23.061  1.00 42.82  ? 210 SER D CA  1 
ATOM   5502 C  C   . SER D 2 209 ? 127.295 195.879 23.573  1.00 43.10  ? 210 SER D C   1 
ATOM   5503 O  O   . SER D 2 209 ? 126.536 196.635 24.196  1.00 40.97  ? 210 SER D O   1 
ATOM   5504 C  CB  . SER D 2 209 ? 126.021 194.757 21.770  1.00 43.30  ? 210 SER D CB  1 
ATOM   5505 O  OG  . SER D 2 209 ? 125.473 193.551 21.285  1.00 54.11  ? 210 SER D OG  1 
ATOM   5506 N  N   . PHE D 2 210 ? 128.547 196.209 23.270  1.00 38.05  ? 211 PHE D N   1 
ATOM   5507 C  CA  . PHE D 2 210 ? 129.015 197.575 23.516  1.00 44.02  ? 211 PHE D CA  1 
ATOM   5508 C  C   . PHE D 2 210 ? 129.757 198.044 22.278  1.00 41.20  ? 211 PHE D C   1 
ATOM   5509 O  O   . PHE D 2 210 ? 130.420 197.257 21.607  1.00 38.56  ? 211 PHE D O   1 
ATOM   5510 C  CB  . PHE D 2 210 ? 129.883 197.699 24.805  1.00 36.71  ? 211 PHE D CB  1 
ATOM   5511 C  CG  . PHE D 2 210 ? 130.846 196.544 25.050  1.00 46.33  ? 211 PHE D CG  1 
ATOM   5512 C  CD1 . PHE D 2 210 ? 130.384 195.308 25.499  1.00 46.42  ? 211 PHE D CD1 1 
ATOM   5513 C  CD2 . PHE D 2 210 ? 132.220 196.716 24.891  1.00 47.46  ? 211 PHE D CD2 1 
ATOM   5514 C  CE1 . PHE D 2 210 ? 131.270 194.249 25.743  1.00 45.73  ? 211 PHE D CE1 1 
ATOM   5515 C  CE2 . PHE D 2 210 ? 133.121 195.661 25.137  1.00 46.34  ? 211 PHE D CE2 1 
ATOM   5516 C  CZ  . PHE D 2 210 ? 132.637 194.426 25.569  1.00 43.12  ? 211 PHE D CZ  1 
ATOM   5517 N  N   . LEU D 2 211 ? 129.614 199.328 21.960  1.00 40.00  ? 212 LEU D N   1 
ATOM   5518 C  CA  . LEU D 2 211 ? 130.031 199.808 20.648  1.00 40.52  ? 212 LEU D CA  1 
ATOM   5519 C  C   . LEU D 2 211 ? 130.449 201.272 20.638  1.00 40.13  ? 212 LEU D C   1 
ATOM   5520 O  O   . LEU D 2 211 ? 130.073 202.059 21.507  1.00 37.29  ? 212 LEU D O   1 
ATOM   5521 C  CB  . LEU D 2 211 ? 128.894 199.602 19.629  1.00 44.67  ? 212 LEU D CB  1 
ATOM   5522 C  CG  . LEU D 2 211 ? 127.581 200.408 19.783  1.00 39.33  ? 212 LEU D CG  1 
ATOM   5523 C  CD1 . LEU D 2 211 ? 126.826 200.446 18.478  1.00 31.04  ? 212 LEU D CD1 1 
ATOM   5524 C  CD2 . LEU D 2 211 ? 126.693 199.829 20.855  1.00 35.06  ? 212 LEU D CD2 1 
ATOM   5525 N  N   . GLY D 2 212 ? 131.193 201.643 19.603  1.00 42.40  ? 213 GLY D N   1 
ATOM   5526 C  CA  . GLY D 2 212 ? 131.603 203.023 19.436  1.00 39.95  ? 213 GLY D CA  1 
ATOM   5527 C  C   . GLY D 2 212 ? 131.983 203.324 18.010  1.00 44.77  ? 213 GLY D C   1 
ATOM   5528 O  O   . GLY D 2 212 ? 132.440 202.439 17.252  1.00 40.54  ? 213 GLY D O   1 
ATOM   5529 N  N   . VAL D 2 213 ? 131.785 204.584 17.634  1.00 39.75  ? 214 VAL D N   1 
ATOM   5530 C  CA  . VAL D 2 213 ? 132.230 205.046 16.334  1.00 33.83  ? 214 VAL D CA  1 
ATOM   5531 C  C   . VAL D 2 213 ? 133.739 205.068 16.294  1.00 34.90  ? 214 VAL D C   1 
ATOM   5532 O  O   . VAL D 2 213 ? 134.384 205.588 17.202  1.00 31.54  ? 214 VAL D O   1 
ATOM   5533 C  CB  . VAL D 2 213 ? 131.690 206.453 15.994  1.00 39.94  ? 214 VAL D CB  1 
ATOM   5534 C  CG1 . VAL D 2 213 ? 132.224 206.900 14.621  1.00 35.97  ? 214 VAL D CG1 1 
ATOM   5535 C  CG2 . VAL D 2 213 ? 130.157 206.456 16.039  1.00 27.57  ? 214 VAL D CG2 1 
ATOM   5536 N  N   . ILE D 2 214 ? 134.313 204.510 15.238  1.00 33.65  ? 215 ILE D N   1 
ATOM   5537 C  CA  . ILE D 2 214 ? 135.752 204.562 15.118  1.00 35.20  ? 215 ILE D CA  1 
ATOM   5538 C  C   . ILE D 2 214 ? 136.165 205.981 14.746  1.00 36.07  ? 215 ILE D C   1 
ATOM   5539 O  O   . ILE D 2 214 ? 135.792 206.488 13.695  1.00 43.57  ? 215 ILE D O   1 
ATOM   5540 C  CB  . ILE D 2 214 ? 136.270 203.563 14.097  1.00 35.93  ? 215 ILE D CB  1 
ATOM   5541 C  CG1 . ILE D 2 214 ? 135.982 202.134 14.583  1.00 36.51  ? 215 ILE D CG1 1 
ATOM   5542 C  CG2 . ILE D 2 214 ? 137.758 203.757 13.902  1.00 32.66  ? 215 ILE D CG2 1 
ATOM   5543 C  CD1 . ILE D 2 214 ? 136.203 201.060 13.552  1.00 35.03  ? 215 ILE D CD1 1 
ATOM   5544 N  N   . ALA D 2 215 ? 136.948 206.601 15.618  1.00 35.20  ? 216 ALA D N   1 
ATOM   5545 C  CA  . ALA D 2 215 ? 137.267 208.033 15.552  1.00 35.99  ? 216 ALA D CA  1 
ATOM   5546 C  C   . ALA D 2 215 ? 138.735 208.284 15.208  1.00 37.63  ? 216 ALA D C   1 
ATOM   5547 O  O   . ALA D 2 215 ? 139.617 207.479 15.545  1.00 35.69  ? 216 ALA D O   1 
ATOM   5548 C  CB  . ALA D 2 215 ? 136.924 208.707 16.885  1.00 28.26  ? 216 ALA D CB  1 
ATOM   5549 N  N   . ARG D 2 216 ? 139.000 209.382 14.508  1.00 33.33  ? 217 ARG D N   1 
ATOM   5550 C  CA  . ARG D 2 216 ? 140.383 209.786 14.280  1.00 34.07  ? 217 ARG D CA  1 
ATOM   5551 C  C   . ARG D 2 216 ? 141.110 210.085 15.604  1.00 32.24  ? 217 ARG D C   1 
ATOM   5552 O  O   . ARG D 2 216 ? 140.543 210.653 16.543  1.00 31.37  ? 217 ARG D O   1 
ATOM   5553 C  CB  . ARG D 2 216 ? 140.435 211.015 13.385  1.00 31.48  ? 217 ARG D CB  1 
ATOM   5554 C  CG  . ARG D 2 216 ? 139.748 210.838 12.061  1.00 30.76  ? 217 ARG D CG  1 
ATOM   5555 C  CD  . ARG D 2 216 ? 139.634 212.170 11.380  1.00 28.79  ? 217 ARG D CD  1 
ATOM   5556 N  NE  . ARG D 2 216 ? 138.840 212.063 10.168  1.00 41.91  ? 217 ARG D NE  1 
ATOM   5557 C  CZ  . ARG D 2 216 ? 139.372 211.900 8.965   1.00 40.23  ? 217 ARG D CZ  1 
ATOM   5558 N  NH1 . ARG D 2 216 ? 140.695 211.836 8.848   1.00 34.80  1 217 ARG D NH1 1 
ATOM   5559 N  NH2 . ARG D 2 216 ? 138.588 211.809 7.897   1.00 38.02  ? 217 ARG D NH2 1 
ATOM   5560 N  N   . SER D 2 217 ? 142.366 209.679 15.673  1.00 34.39  ? 218 SER D N   1 
ATOM   5561 C  CA  . SER D 2 217 ? 143.179 209.946 16.850  1.00 38.88  ? 218 SER D CA  1 
ATOM   5562 C  C   . SER D 2 217 ? 144.626 210.281 16.476  1.00 41.10  ? 218 SER D C   1 
ATOM   5563 O  O   . SER D 2 217 ? 145.143 209.779 15.473  1.00 37.03  ? 218 SER D O   1 
ATOM   5564 C  CB  . SER D 2 217 ? 143.168 208.753 17.791  1.00 39.64  ? 218 SER D CB  1 
ATOM   5565 O  OG  . SER D 2 217 ? 144.067 208.994 18.856  1.00 36.91  ? 218 SER D OG  1 
ATOM   5566 N  N   . ALA D 2 218 ? 145.267 211.119 17.290  1.00 39.38  ? 219 ALA D N   1 
ATOM   5567 C  CA  . ALA D 2 218 ? 146.687 211.435 17.108  1.00 39.10  ? 219 ALA D CA  1 
ATOM   5568 C  C   . ALA D 2 218 ? 147.546 210.234 17.454  1.00 45.78  ? 219 ALA D C   1 
ATOM   5569 O  O   . ALA D 2 218 ? 148.685 210.116 16.998  1.00 57.81  ? 219 ALA D O   1 
ATOM   5570 C  CB  . ALA D 2 218 ? 147.095 212.639 17.954  1.00 34.05  ? 219 ALA D CB  1 
ATOM   5571 N  N   . GLY D 2 219 ? 147.000 209.344 18.271  1.00 46.72  ? 220 GLY D N   1 
ATOM   5572 C  CA  . GLY D 2 219 ? 147.699 208.125 18.635  1.00 47.98  ? 220 GLY D CA  1 
ATOM   5573 C  C   . GLY D 2 219 ? 148.738 208.368 19.699  1.00 49.54  ? 220 GLY D C   1 
ATOM   5574 O  O   . GLY D 2 219 ? 149.651 207.573 19.869  1.00 54.80  ? 220 GLY D O   1 
ATOM   5575 N  N   . VAL D 2 220 ? 148.597 209.478 20.410  1.00 46.93  ? 221 VAL D N   1 
ATOM   5576 C  CA  . VAL D 2 220 ? 149.454 209.773 21.545  1.00 56.99  ? 221 VAL D CA  1 
ATOM   5577 C  C   . VAL D 2 220 ? 148.766 209.314 22.824  1.00 56.38  ? 221 VAL D C   1 
ATOM   5578 O  O   . VAL D 2 220 ? 148.301 210.120 23.629  1.00 60.83  ? 221 VAL D O   1 
ATOM   5579 C  CB  . VAL D 2 220 ? 149.786 211.281 21.620  1.00 56.62  ? 221 VAL D CB  1 
ATOM   5580 C  CG1 . VAL D 2 220 ? 150.773 211.572 22.744  1.00 66.58  ? 221 VAL D CG1 1 
ATOM   5581 C  CG2 . VAL D 2 220 ? 150.374 211.720 20.319  1.00 51.67  ? 221 VAL D CG2 1 
ATOM   5582 N  N   . TRP D 2 221 ? 148.720 207.999 23.002  1.00 56.24  ? 222 TRP D N   1 
ATOM   5583 C  CA  . TRP D 2 221 ? 148.067 207.398 24.150  1.00 62.91  ? 222 TRP D CA  1 
ATOM   5584 C  C   . TRP D 2 221 ? 149.074 207.172 25.258  1.00 64.56  ? 222 TRP D C   1 
ATOM   5585 O  O   . TRP D 2 221 ? 150.256 206.923 25.006  1.00 67.80  ? 222 TRP D O   1 
ATOM   5586 C  CB  . TRP D 2 221 ? 147.417 206.059 23.790  1.00 58.75  ? 222 TRP D CB  1 
ATOM   5587 C  CG  . TRP D 2 221 ? 146.481 206.117 22.661  1.00 56.36  ? 222 TRP D CG  1 
ATOM   5588 C  CD1 . TRP D 2 221 ? 145.317 206.828 22.602  1.00 63.05  ? 222 TRP D CD1 1 
ATOM   5589 C  CD2 . TRP D 2 221 ? 146.594 205.426 21.416  1.00 53.52  ? 222 TRP D CD2 1 
ATOM   5590 N  NE1 . TRP D 2 221 ? 144.701 206.628 21.389  1.00 53.63  ? 222 TRP D NE1 1 
ATOM   5591 C  CE2 . TRP D 2 221 ? 145.466 205.774 20.640  1.00 47.07  ? 222 TRP D CE2 1 
ATOM   5592 C  CE3 . TRP D 2 221 ? 147.538 204.550 20.881  1.00 53.06  ? 222 TRP D CE3 1 
ATOM   5593 C  CZ2 . TRP D 2 221 ? 145.258 205.283 19.360  1.00 40.19  ? 222 TRP D CZ2 1 
ATOM   5594 C  CZ3 . TRP D 2 221 ? 147.332 204.063 19.611  1.00 49.83  ? 222 TRP D CZ3 1 
ATOM   5595 C  CH2 . TRP D 2 221 ? 146.193 204.430 18.860  1.00 47.86  ? 222 TRP D CH2 1 
ATOM   5596 N  N   . GLU D 2 222 ? 148.583 207.246 26.485  1.00 66.24  ? 223 GLU D N   1 
ATOM   5597 C  CA  . GLU D 2 222 ? 149.388 207.025 27.671  1.00 72.07  ? 223 GLU D CA  1 
ATOM   5598 C  C   . GLU D 2 222 ? 149.368 205.540 28.049  1.00 74.41  ? 223 GLU D C   1 
ATOM   5599 O  O   . GLU D 2 222 ? 148.660 204.742 27.433  1.00 69.75  ? 223 GLU D O   1 
ATOM   5600 C  CB  . GLU D 2 222 ? 148.868 207.888 28.829  1.00 78.31  ? 223 GLU D CB  1 
ATOM   5601 C  CG  . GLU D 2 222 ? 147.541 207.386 29.456  1.00 80.95  ? 223 GLU D CG  1 
ATOM   5602 C  CD  . GLU D 2 222 ? 146.291 207.593 28.587  1.00 73.08  ? 223 GLU D CD  1 
ATOM   5603 O  OE1 . GLU D 2 222 ? 146.393 208.121 27.458  1.00 78.06  ? 223 GLU D OE1 1 
ATOM   5604 O  OE2 . GLU D 2 222 ? 145.196 207.197 29.030  1.00 65.46  1 223 GLU D OE2 1 
ATOM   5605 N  N   . ASN D 2 223 ? 150.135 205.181 29.072  1.00 80.10  ? 224 ASN D N   1 
ATOM   5606 C  CA  . ASN D 2 223 ? 150.276 203.788 29.499  1.00 82.95  ? 224 ASN D CA  1 
ATOM   5607 C  C   . ASN D 2 223 ? 148.977 203.132 29.988  1.00 80.12  ? 224 ASN D C   1 
ATOM   5608 O  O   . ASN D 2 223 ? 148.603 202.054 29.515  1.00 84.02  ? 224 ASN D O   1 
ATOM   5609 C  CB  . ASN D 2 223 ? 151.332 203.683 30.595  1.00 88.00  ? 224 ASN D CB  1 
ATOM   5610 C  CG  . ASN D 2 223 ? 151.553 202.258 31.047  1.00 95.82  ? 224 ASN D CG  1 
ATOM   5611 O  OD1 . ASN D 2 223 ? 151.305 201.911 32.207  1.00 99.17  ? 224 ASN D OD1 1 
ATOM   5612 N  ND2 . ASN D 2 223 ? 152.003 201.413 30.126  1.00 99.58  ? 224 ASN D ND2 1 
ATOM   5613 N  N   . ASN D 2 224 ? 148.320 203.741 30.972  1.00 76.91  ? 225 ASN D N   1 
ATOM   5614 C  CA  . ASN D 2 224 ? 147.045 203.214 31.435  1.00 69.46  ? 225 ASN D CA  1 
ATOM   5615 C  C   . ASN D 2 224 ? 145.965 203.529 30.407  1.00 75.95  ? 225 ASN D C   1 
ATOM   5616 O  O   . ASN D 2 224 ? 145.803 204.669 29.967  1.00 79.85  ? 225 ASN D O   1 
ATOM   5617 C  CB  . ASN D 2 224 ? 146.662 203.776 32.808  1.00 78.34  ? 225 ASN D CB  1 
ATOM   5618 C  CG  . ASN D 2 224 ? 146.563 205.290 32.818  1.00 83.56  ? 225 ASN D CG  1 
ATOM   5619 O  OD1 . ASN D 2 224 ? 147.364 205.980 32.191  1.00 78.35  ? 225 ASN D OD1 1 
ATOM   5620 N  ND2 . ASN D 2 224 ? 145.575 205.813 33.539  1.00 90.91  ? 225 ASN D ND2 1 
ATOM   5621 N  N   . LYS D 2 225 ? 145.225 202.502 30.027  1.00 67.58  ? 226 LYS D N   1 
ATOM   5622 C  CA  . LYS D 2 225 ? 144.214 202.624 29.000  1.00 56.74  ? 226 LYS D CA  1 
ATOM   5623 C  C   . LYS D 2 225 ? 142.897 203.027 29.652  1.00 54.75  ? 226 LYS D C   1 
ATOM   5624 O  O   . LYS D 2 225 ? 142.174 202.180 30.170  1.00 61.74  ? 226 LYS D O   1 
ATOM   5625 C  CB  . LYS D 2 225 ? 144.107 201.300 28.237  1.00 55.80  ? 226 LYS D CB  1 
ATOM   5626 C  CG  . LYS D 2 225 ? 145.473 200.767 27.835  1.00 46.84  ? 226 LYS D CG  1 
ATOM   5627 C  CD  . LYS D 2 225 ? 145.414 199.362 27.282  1.00 42.17  ? 226 LYS D CD  1 
ATOM   5628 C  CE  . LYS D 2 225 ? 146.734 198.973 26.642  1.00 47.11  ? 226 LYS D CE  1 
ATOM   5629 N  NZ  . LYS D 2 225 ? 146.815 197.524 26.336  1.00 51.84  1 226 LYS D NZ  1 
ATOM   5630 N  N   . GLN D 2 226 ? 142.601 204.323 29.652  1.00 50.88  ? 227 GLN D N   1 
ATOM   5631 C  CA  . GLN D 2 226 ? 141.449 204.833 30.392  1.00 53.90  ? 227 GLN D CA  1 
ATOM   5632 C  C   . GLN D 2 226 ? 140.553 205.770 29.573  1.00 51.62  ? 227 GLN D C   1 
ATOM   5633 O  O   . GLN D 2 226 ? 140.895 206.177 28.468  1.00 48.23  ? 227 GLN D O   1 
ATOM   5634 C  CB  . GLN D 2 226 ? 141.915 205.539 31.666  1.00 53.66  ? 227 GLN D CB  1 
ATOM   5635 C  CG  . GLN D 2 226 ? 142.746 206.798 31.474  1.00 60.88  ? 227 GLN D CG  1 
ATOM   5636 C  CD  . GLN D 2 226 ? 143.057 207.478 32.808  1.00 75.19  ? 227 GLN D CD  1 
ATOM   5637 O  OE1 . GLN D 2 226 ? 142.609 207.031 33.863  1.00 74.56  ? 227 GLN D OE1 1 
ATOM   5638 N  NE2 . GLN D 2 226 ? 143.846 208.539 32.766  1.00 67.17  ? 227 GLN D NE2 1 
ATOM   5639 N  N   . VAL D 2 227 ? 139.382 206.076 30.119  1.00 50.39  ? 228 VAL D N   1 
ATOM   5640 C  CA  . VAL D 2 227 ? 138.433 206.958 29.458  1.00 46.54  ? 228 VAL D CA  1 
ATOM   5641 C  C   . VAL D 2 227 ? 137.936 207.973 30.465  1.00 46.41  ? 228 VAL D C   1 
ATOM   5642 O  O   . VAL D 2 227 ? 137.504 207.605 31.555  1.00 58.25  ? 228 VAL D O   1 
ATOM   5643 C  CB  . VAL D 2 227 ? 137.229 206.181 28.872  1.00 47.95  ? 228 VAL D CB  1 
ATOM   5644 C  CG1 . VAL D 2 227 ? 136.220 207.142 28.255  1.00 37.00  ? 228 VAL D CG1 1 
ATOM   5645 C  CG2 . VAL D 2 227 ? 137.690 205.124 27.845  1.00 39.38  ? 228 VAL D CG2 1 
ATOM   5646 N  N   . CYS D 2 228 ? 137.999 209.253 30.119  1.00 56.68  ? 229 CYS D N   1 
ATOM   5647 C  CA  . CYS D 2 228 ? 137.538 210.293 31.041  1.00 64.06  ? 229 CYS D CA  1 
ATOM   5648 C  C   . CYS D 2 228 ? 136.166 210.793 30.631  1.00 67.78  ? 229 CYS D C   1 
ATOM   5649 O  O   . CYS D 2 228 ? 135.788 210.695 29.456  1.00 71.94  ? 229 CYS D O   1 
ATOM   5650 C  CB  . CYS D 2 228 ? 138.523 211.470 31.100  1.00 56.12  ? 229 CYS D CB  1 
ATOM   5651 S  SG  . CYS D 2 228 ? 140.192 211.025 31.643  1.00 73.93  ? 229 CYS D SG  1 
ATOM   5652 N  N   . ALA D 2 229 ? 135.414 211.303 31.604  1.00 63.80  ? 230 ALA D N   1 
ATOM   5653 C  CA  . ALA D 2 229 ? 134.141 211.961 31.331  1.00 64.50  ? 230 ALA D CA  1 
ATOM   5654 C  C   . ALA D 2 229 ? 134.389 213.339 30.734  1.00 72.77  ? 230 ALA D C   1 
ATOM   5655 O  O   . ALA D 2 229 ? 135.523 213.849 30.780  1.00 72.74  ? 230 ALA D O   1 
ATOM   5656 C  CB  . ALA D 2 229 ? 133.307 212.080 32.606  1.00 68.71  ? 230 ALA D CB  1 
ATOM   5657 N  N   . CYS D 2 230 ? 133.322 213.942 30.201  1.00 73.04  ? 231 CYS D N   1 
ATOM   5658 C  CA  . CYS D 2 230 ? 133.348 215.328 29.725  1.00 75.51  ? 231 CYS D CA  1 
ATOM   5659 C  C   . CYS D 2 230 ? 133.944 216.254 30.813  1.00 82.00  ? 231 CYS D C   1 
ATOM   5660 O  O   . CYS D 2 230 ? 134.608 217.248 30.516  1.00 81.56  ? 231 CYS D O   1 
ATOM   5661 C  CB  . CYS D 2 230 ? 131.931 215.781 29.328  1.00 68.85  ? 231 CYS D CB  1 
ATOM   5662 S  SG  . CYS D 2 230 ? 131.485 215.661 27.554  1.00 84.25  ? 231 CYS D SG  1 
ATOM   5663 N  N   . THR D 2 231 ? 133.714 215.883 32.071  1.00 87.36  ? 232 THR D N   1 
ATOM   5664 C  CA  . THR D 2 231 ? 134.298 216.527 33.252  1.00 85.58  ? 232 THR D CA  1 
ATOM   5665 C  C   . THR D 2 231 ? 135.834 216.610 33.274  1.00 86.27  ? 232 THR D C   1 
ATOM   5666 O  O   . THR D 2 231 ? 136.405 217.657 33.574  1.00 92.21  ? 232 THR D O   1 
ATOM   5667 C  CB  . THR D 2 231 ? 133.860 215.771 34.537  1.00 90.13  ? 232 THR D CB  1 
ATOM   5668 O  OG1 . THR D 2 231 ? 132.426 215.719 34.620  1.00 89.31  ? 232 THR D OG1 1 
ATOM   5669 C  CG2 . THR D 2 231 ? 134.443 216.432 35.783  1.00 85.48  ? 232 THR D CG2 1 
ATOM   5670 N  N   . GLY D 2 232 ? 136.489 215.493 32.971  1.00 82.51  ? 233 GLY D N   1 
ATOM   5671 C  CA  . GLY D 2 232 ? 137.922 215.345 33.176  1.00 82.38  ? 233 GLY D CA  1 
ATOM   5672 C  C   . GLY D 2 232 ? 138.129 214.197 34.154  1.00 87.44  ? 233 GLY D C   1 
ATOM   5673 O  O   . GLY D 2 232 ? 139.227 213.628 34.277  1.00 79.96  ? 233 GLY D O   1 
ATOM   5674 N  N   . LYS D 2 233 ? 137.038 213.881 34.856  1.00 79.37  ? 234 LYS D N   1 
ATOM   5675 C  CA  . LYS D 2 233 ? 136.931 212.746 35.771  1.00 74.52  ? 234 LYS D CA  1 
ATOM   5676 C  C   . LYS D 2 233 ? 137.201 211.438 35.028  1.00 71.94  ? 234 LYS D C   1 
ATOM   5677 O  O   . LYS D 2 233 ? 136.696 211.229 33.931  1.00 61.56  ? 234 LYS D O   1 
ATOM   5678 C  CB  . LYS D 2 233 ? 135.525 212.758 36.406  1.00 70.17  ? 234 LYS D CB  1 
ATOM   5679 C  CG  . LYS D 2 233 ? 135.154 211.601 37.330  1.00 82.25  ? 234 LYS D CG  1 
ATOM   5680 C  CD  . LYS D 2 233 ? 133.615 211.442 37.405  1.00 90.25  ? 234 LYS D CD  1 
ATOM   5681 C  CE  . LYS D 2 233 ? 133.140 210.727 38.682  1.00 84.49  ? 234 LYS D CE  1 
ATOM   5682 N  NZ  . LYS D 2 233 ? 133.961 209.525 39.029  1.00 74.07  1 234 LYS D NZ  1 
ATOM   5683 N  N   . THR D 2 234 ? 138.012 210.563 35.608  1.00 66.66  ? 235 THR D N   1 
ATOM   5684 C  CA  . THR D 2 234 ? 138.250 209.265 34.986  1.00 63.03  ? 235 THR D CA  1 
ATOM   5685 C  C   . THR D 2 234 ? 137.113 208.309 35.347  1.00 62.26  ? 235 THR D C   1 
ATOM   5686 O  O   . THR D 2 234 ? 136.850 208.079 36.523  1.00 66.47  ? 235 THR D O   1 
ATOM   5687 C  CB  . THR D 2 234 ? 139.614 208.682 35.385  1.00 60.20  ? 235 THR D CB  1 
ATOM   5688 O  OG1 . THR D 2 234 ? 140.644 209.418 34.712  1.00 61.14  ? 235 THR D OG1 1 
ATOM   5689 C  CG2 . THR D 2 234 ? 139.704 207.206 34.991  1.00 55.77  ? 235 THR D CG2 1 
ATOM   5690 N  N   . VAL D 2 235 ? 136.437 207.770 34.331  1.00 61.94  ? 236 VAL D N   1 
ATOM   5691 C  CA  . VAL D 2 235 ? 135.238 206.953 34.538  1.00 55.96  ? 236 VAL D CA  1 
ATOM   5692 C  C   . VAL D 2 235 ? 135.401 205.464 34.237  1.00 55.18  ? 236 VAL D C   1 
ATOM   5693 O  O   . VAL D 2 235 ? 134.487 204.681 34.503  1.00 61.02  ? 236 VAL D O   1 
ATOM   5694 C  CB  . VAL D 2 235 ? 134.050 207.476 33.688  1.00 54.90  ? 236 VAL D CB  1 
ATOM   5695 C  CG1 . VAL D 2 235 ? 133.757 208.922 34.031  1.00 58.37  ? 236 VAL D CG1 1 
ATOM   5696 C  CG2 . VAL D 2 235 ? 134.328 207.296 32.190  1.00 50.26  ? 236 VAL D CG2 1 
ATOM   5697 N  N   . TRP D 2 236 ? 136.542 205.090 33.662  1.00 52.62  ? 237 TRP D N   1 
ATOM   5698 C  CA  . TRP D 2 236 ? 136.822 203.701 33.306  1.00 48.05  ? 237 TRP D CA  1 
ATOM   5699 C  C   . TRP D 2 236 ? 138.296 203.553 32.972  1.00 53.03  ? 237 TRP D C   1 
ATOM   5700 O  O   . TRP D 2 236 ? 138.925 204.505 32.497  1.00 50.88  ? 237 TRP D O   1 
ATOM   5701 C  CB  . TRP D 2 236 ? 135.952 203.279 32.114  1.00 42.62  ? 237 TRP D CB  1 
ATOM   5702 C  CG  . TRP D 2 236 ? 136.099 201.864 31.591  1.00 45.37  ? 237 TRP D CG  1 
ATOM   5703 C  CD1 . TRP D 2 236 ? 135.261 200.803 31.838  1.00 48.41  ? 237 TRP D CD1 1 
ATOM   5704 C  CD2 . TRP D 2 236 ? 137.108 201.371 30.681  1.00 50.41  ? 237 TRP D CD2 1 
ATOM   5705 N  NE1 . TRP D 2 236 ? 135.695 199.683 31.150  1.00 51.15  ? 237 TRP D NE1 1 
ATOM   5706 C  CE2 . TRP D 2 236 ? 136.823 200.002 30.438  1.00 50.38  ? 237 TRP D CE2 1 
ATOM   5707 C  CE3 . TRP D 2 236 ? 138.208 201.952 30.044  1.00 43.38  ? 237 TRP D CE3 1 
ATOM   5708 C  CZ2 . TRP D 2 236 ? 137.608 199.210 29.591  1.00 46.80  ? 237 TRP D CZ2 1 
ATOM   5709 C  CZ3 . TRP D 2 236 ? 138.992 201.159 29.208  1.00 44.29  ? 237 TRP D CZ3 1 
ATOM   5710 C  CH2 . TRP D 2 236 ? 138.685 199.803 28.990  1.00 48.30  ? 237 TRP D CH2 1 
ATOM   5711 N  N   . ALA D 2 237 ? 138.833 202.359 33.208  1.00 50.69  ? 238 ALA D N   1 
ATOM   5712 C  CA  . ALA D 2 237 ? 140.211 202.032 32.854  1.00 51.97  ? 238 ALA D CA  1 
ATOM   5713 C  C   . ALA D 2 237 ? 140.280 200.542 32.521  1.00 51.45  ? 238 ALA D C   1 
ATOM   5714 O  O   . ALA D 2 237 ? 139.508 199.750 33.069  1.00 46.64  ? 238 ALA D O   1 
ATOM   5715 C  CB  . ALA D 2 237 ? 141.166 202.383 34.001  1.00 37.27  ? 238 ALA D CB  1 
ATOM   5716 N  N   . ALA D 2 238 ? 141.203 200.144 31.647  1.00 52.22  ? 239 ALA D N   1 
ATOM   5717 C  CA  . ALA D 2 238 ? 141.399 198.720 31.399  1.00 53.24  ? 239 ALA D CA  1 
ATOM   5718 C  C   . ALA D 2 238 ? 141.853 198.098 32.710  1.00 52.96  ? 239 ALA D C   1 
ATOM   5719 O  O   . ALA D 2 238 ? 142.393 198.800 33.564  1.00 64.14  ? 239 ALA D O   1 
ATOM   5720 C  CB  . ALA D 2 238 ? 142.423 198.483 30.299  1.00 43.24  ? 239 ALA D CB  1 
ATOM   5721 N  N   . ALA D 2 239 ? 141.613 196.807 32.897  1.00 57.74  ? 240 ALA D N   1 
ATOM   5722 C  CA  . ALA D 2 239 ? 142.100 196.136 34.104  1.00 65.69  ? 240 ALA D CA  1 
ATOM   5723 C  C   . ALA D 2 239 ? 143.624 195.952 34.027  1.00 63.56  ? 240 ALA D C   1 
ATOM   5724 O  O   . ALA D 2 239 ? 144.167 195.698 32.954  1.00 68.71  ? 240 ALA D O   1 
ATOM   5725 C  CB  . ALA D 2 239 ? 141.395 194.790 34.285  1.00 50.91  ? 240 ALA D CB  1 
ATOM   5726 N  N   . LYS D 2 240 ? 144.315 196.083 35.156  1.00 74.98  ? 241 LYS D N   1 
ATOM   5727 C  CA  . LYS D 2 240 ? 145.770 195.908 35.172  1.00 78.17  ? 241 LYS D CA  1 
ATOM   5728 C  C   . LYS D 2 240 ? 146.170 194.437 35.069  1.00 69.04  ? 241 LYS D C   1 
ATOM   5729 O  O   . LYS D 2 240 ? 147.352 194.096 35.113  1.00 76.76  ? 241 LYS D O   1 
ATOM   5730 C  CB  . LYS D 2 240 ? 146.370 196.542 36.426  1.00 79.87  ? 241 LYS D CB  1 
ATOM   5731 C  CG  . LYS D 2 240 ? 146.161 198.059 36.520  1.00 86.43  ? 241 LYS D CG  1 
ATOM   5732 C  CD  . LYS D 2 240 ? 146.838 198.808 35.367  1.00 85.98  ? 241 LYS D CD  1 
ATOM   5733 C  CE  . LYS D 2 240 ? 146.739 200.321 35.556  1.00 93.31  ? 241 LYS D CE  1 
ATOM   5734 N  NZ  . LYS D 2 240 ? 147.435 201.082 34.476  1.00 94.64  1 241 LYS D NZ  1 
HETATM 5735 ZN ZN  . ZN  E 3 .   ? 89.659  229.225 8.295   1.00 28.02  ? 201 ZN  A ZN  1 
HETATM 5736 ZN ZN  . ZN  F 3 .   ? 67.650  204.775 -14.421 0.86 159.60 ? 301 ZN  B ZN  1 
HETATM 5737 ZN ZN  . ZN  G 3 .   ? 137.547 227.637 15.974  1.00 31.29  ? 201 ZN  C ZN  1 
HETATM 5738 O  O   . HOH H 4 .   ? 89.051  241.844 0.696   1.00 43.98  ? 301 HOH A O   1 
HETATM 5739 O  O   . HOH H 4 .   ? 98.850  230.483 16.905  1.00 40.67  ? 302 HOH A O   1 
HETATM 5740 O  O   . HOH H 4 .   ? 89.276  232.865 -2.211  1.00 29.19  ? 303 HOH A O   1 
HETATM 5741 O  O   . HOH H 4 .   ? 80.665  232.677 14.458  1.00 39.89  ? 304 HOH A O   1 
HETATM 5742 O  O   . HOH H 4 .   ? 102.766 213.565 2.968   1.00 44.40  ? 305 HOH A O   1 
HETATM 5743 O  O   . HOH H 4 .   ? 92.789  225.533 2.403   1.00 35.21  ? 306 HOH A O   1 
HETATM 5744 O  O   . HOH H 4 .   ? 104.705 234.348 9.249   1.00 42.53  ? 307 HOH A O   1 
HETATM 5745 O  O   . HOH H 4 .   ? 87.117  231.422 17.462  1.00 36.90  ? 308 HOH A O   1 
HETATM 5746 O  O   . HOH H 4 .   ? 99.806  236.951 8.548   1.00 47.71  ? 309 HOH A O   1 
HETATM 5747 O  O   . HOH H 4 .   ? 85.775  221.026 10.753  1.00 33.32  ? 310 HOH A O   1 
HETATM 5748 O  O   . HOH H 4 .   ? 86.860  227.147 5.380   1.00 30.94  ? 311 HOH A O   1 
HETATM 5749 O  O   . HOH H 4 .   ? 102.471 213.371 6.809   1.00 33.33  ? 312 HOH A O   1 
HETATM 5750 O  O   . HOH H 4 .   ? 95.547  229.963 7.252   1.00 29.90  ? 313 HOH A O   1 
HETATM 5751 O  O   . HOH H 4 .   ? 80.508  227.794 18.942  1.00 43.81  ? 314 HOH A O   1 
HETATM 5752 O  O   . HOH H 4 .   ? 87.633  236.689 12.366  1.00 44.33  ? 315 HOH A O   1 
HETATM 5753 O  O   . HOH H 4 .   ? 94.311  231.883 9.579   1.00 42.30  ? 316 HOH A O   1 
HETATM 5754 O  O   . HOH H 4 .   ? 98.102  212.540 1.211   1.00 38.91  ? 317 HOH A O   1 
HETATM 5755 O  O   . HOH H 4 .   ? 87.350  228.092 16.675  1.00 35.21  ? 318 HOH A O   1 
HETATM 5756 O  O   . HOH H 4 .   ? 94.488  237.107 -0.347  1.00 40.71  ? 319 HOH A O   1 
HETATM 5757 O  O   . HOH H 4 .   ? 101.618 210.572 23.869  1.00 52.10  ? 320 HOH A O   1 
HETATM 5758 O  O   . HOH H 4 .   ? 91.973  229.088 -1.483  1.00 32.39  ? 321 HOH A O   1 
HETATM 5759 O  O   . HOH H 4 .   ? 86.297  226.102 15.076  1.00 28.34  ? 322 HOH A O   1 
HETATM 5760 O  O   . HOH H 4 .   ? 85.488  223.161 21.900  1.00 44.17  ? 323 HOH A O   1 
HETATM 5761 O  O   . HOH H 4 .   ? 91.727  231.367 -2.400  1.00 32.19  ? 324 HOH A O   1 
HETATM 5762 O  O   . HOH H 4 .   ? 97.199  230.700 19.982  1.00 43.22  ? 325 HOH A O   1 
HETATM 5763 O  O   . HOH H 4 .   ? 105.062 221.960 -4.378  1.00 42.76  ? 326 HOH A O   1 
HETATM 5764 O  O   . HOH H 4 .   ? 90.013  219.806 22.134  1.00 42.68  ? 327 HOH A O   1 
HETATM 5765 O  O   . HOH H 4 .   ? 107.574 231.542 8.733   1.00 45.78  ? 328 HOH A O   1 
HETATM 5766 O  O   . HOH H 4 .   ? 83.569  230.097 7.768   1.00 34.48  ? 329 HOH A O   1 
HETATM 5767 O  O   . HOH H 4 .   ? 92.272  218.371 28.962  1.00 44.39  ? 330 HOH A O   1 
HETATM 5768 O  O   . HOH H 4 .   ? 95.149  211.053 2.318   1.00 31.25  ? 331 HOH A O   1 
HETATM 5769 O  O   . HOH H 4 .   ? 101.161 212.739 4.724   1.00 33.38  ? 332 HOH A O   1 
HETATM 5770 O  O   . HOH H 4 .   ? 104.151 231.493 11.173  1.00 42.27  ? 333 HOH A O   1 
HETATM 5771 O  O   . HOH H 4 .   ? 96.090  236.726 13.831  1.00 46.83  ? 334 HOH A O   1 
HETATM 5772 O  O   . HOH H 4 .   ? 91.132  212.442 21.867  1.00 53.59  ? 335 HOH A O   1 
HETATM 5773 O  O   . HOH H 4 .   ? 100.925 214.452 0.567   1.00 43.58  ? 336 HOH A O   1 
HETATM 5774 O  O   . HOH H 4 .   ? 113.469 241.474 -0.502  1.00 54.27  ? 337 HOH A O   1 
HETATM 5775 O  O   . HOH H 4 .   ? 87.704  238.107 15.740  1.00 46.85  ? 338 HOH A O   1 
HETATM 5776 O  O   . HOH H 4 .   ? 100.007 234.507 11.050  1.00 37.36  ? 339 HOH A O   1 
HETATM 5777 O  O   . HOH H 4 .   ? 116.844 227.494 7.592   1.00 63.49  ? 340 HOH A O   1 
HETATM 5778 O  O   . HOH H 4 .   ? 92.148  244.774 5.244   1.00 42.63  ? 341 HOH A O   1 
HETATM 5779 O  O   . HOH H 4 .   ? 97.488  239.331 5.730   1.00 41.89  ? 342 HOH A O   1 
HETATM 5780 O  O   . HOH H 4 .   ? 97.580  215.990 30.340  1.00 51.44  ? 343 HOH A O   1 
HETATM 5781 O  O   . HOH H 4 .   ? 99.501  239.136 7.594   1.00 48.49  ? 344 HOH A O   1 
HETATM 5782 O  O   . HOH I 4 .   ? 100.460 208.740 0.829   1.00 46.06  ? 401 HOH B O   1 
HETATM 5783 O  O   . HOH I 4 .   ? 81.917  208.340 7.243   1.00 51.17  ? 402 HOH B O   1 
HETATM 5784 O  O   . HOH I 4 .   ? 84.295  198.713 -2.140  1.00 47.36  ? 403 HOH B O   1 
HETATM 5785 O  O   . HOH I 4 .   ? 103.084 195.423 5.884   1.00 39.40  ? 404 HOH B O   1 
HETATM 5786 O  O   . HOH I 4 .   ? 85.455  205.428 15.169  1.00 42.47  ? 405 HOH B O   1 
HETATM 5787 O  O   . HOH I 4 .   ? 109.156 202.463 0.214   1.00 41.85  ? 406 HOH B O   1 
HETATM 5788 O  O   . HOH I 4 .   ? 84.172  209.623 9.046   1.00 47.04  ? 407 HOH B O   1 
HETATM 5789 O  O   . HOH I 4 .   ? 106.848 187.623 -5.285  1.00 44.46  ? 408 HOH B O   1 
HETATM 5790 O  O   . HOH I 4 .   ? 103.977 211.736 8.309   1.00 32.76  ? 409 HOH B O   1 
HETATM 5791 O  O   . HOH I 4 .   ? 92.626  198.071 20.735  1.00 57.52  ? 410 HOH B O   1 
HETATM 5792 O  O   . HOH I 4 .   ? 103.467 210.272 -5.898  1.00 46.14  ? 411 HOH B O   1 
HETATM 5793 O  O   . HOH I 4 .   ? 94.304  189.672 10.466  1.00 53.30  ? 412 HOH B O   1 
HETATM 5794 O  O   . HOH I 4 .   ? 96.873  209.076 3.267   1.00 37.34  ? 413 HOH B O   1 
HETATM 5795 O  O   . HOH I 4 .   ? 87.268  209.831 10.674  1.00 43.62  ? 414 HOH B O   1 
HETATM 5796 O  O   . HOH I 4 .   ? 100.235 209.962 3.866   1.00 44.13  ? 415 HOH B O   1 
HETATM 5797 O  O   . HOH I 4 .   ? 100.962 191.447 7.457   1.00 47.00  ? 416 HOH B O   1 
HETATM 5798 O  O   . HOH I 4 .   ? 87.409  190.741 4.942   1.00 54.28  ? 417 HOH B O   1 
HETATM 5799 O  O   . HOH I 4 .   ? 92.414  196.250 -15.477 1.00 64.12  ? 418 HOH B O   1 
HETATM 5800 O  O   . HOH I 4 .   ? 88.829  212.651 17.315  1.00 43.57  ? 419 HOH B O   1 
HETATM 5801 O  O   . HOH I 4 .   ? 91.253  209.927 16.752  1.00 51.73  ? 420 HOH B O   1 
HETATM 5802 O  O   . HOH I 4 .   ? 110.205 202.555 3.029   1.00 41.82  ? 421 HOH B O   1 
HETATM 5803 O  O   . HOH I 4 .   ? 86.218  212.113 10.207  1.00 48.22  ? 422 HOH B O   1 
HETATM 5804 O  O   . HOH I 4 .   ? 98.552  212.230 -1.860  1.00 51.94  ? 423 HOH B O   1 
HETATM 5805 O  O   . HOH I 4 .   ? 99.193  212.210 -4.261  1.00 47.07  ? 424 HOH B O   1 
HETATM 5806 O  O   . HOH J 4 .   ? 143.861 212.177 19.835  1.00 43.70  ? 301 HOH C O   1 
HETATM 5807 O  O   . HOH J 4 .   ? 121.842 222.973 30.279  1.00 44.79  ? 302 HOH C O   1 
HETATM 5808 O  O   . HOH J 4 .   ? 127.895 228.046 7.857   1.00 39.82  ? 303 HOH C O   1 
HETATM 5809 O  O   . HOH J 4 .   ? 146.387 229.878 6.264   1.00 37.85  ? 304 HOH C O   1 
HETATM 5810 O  O   . HOH J 4 .   ? 139.988 227.655 7.636   1.00 36.10  ? 305 HOH C O   1 
HETATM 5811 O  O   . HOH J 4 .   ? 137.106 218.166 1.638   1.00 38.60  ? 306 HOH C O   1 
HETATM 5812 O  O   . HOH J 4 .   ? 131.514 227.188 17.238  1.00 33.51  ? 307 HOH C O   1 
HETATM 5813 O  O   . HOH J 4 .   ? 139.855 235.270 15.948  1.00 34.41  ? 308 HOH C O   1 
HETATM 5814 O  O   . HOH J 4 .   ? 138.267 235.365 12.721  1.00 37.71  ? 309 HOH C O   1 
HETATM 5815 O  O   . HOH J 4 .   ? 141.230 225.552 8.946   1.00 36.16  ? 310 HOH C O   1 
HETATM 5816 O  O   . HOH J 4 .   ? 135.140 237.824 6.863   1.00 41.78  ? 311 HOH C O   1 
HETATM 5817 O  O   . HOH J 4 .   ? 139.989 238.909 18.172  1.00 39.24  ? 312 HOH C O   1 
HETATM 5818 O  O   . HOH J 4 .   ? 131.025 222.003 1.267   1.00 33.21  ? 313 HOH C O   1 
HETATM 5819 O  O   . HOH J 4 .   ? 140.820 225.735 18.636  1.00 24.75  ? 314 HOH C O   1 
HETATM 5820 O  O   . HOH J 4 .   ? 131.003 236.925 12.111  1.00 57.52  ? 315 HOH C O   1 
HETATM 5821 O  O   . HOH J 4 .   ? 139.616 237.824 7.174   1.00 49.82  ? 316 HOH C O   1 
HETATM 5822 O  O   . HOH J 4 .   ? 143.160 220.675 12.552  1.00 40.97  ? 317 HOH C O   1 
HETATM 5823 O  O   . HOH J 4 .   ? 125.840 228.374 12.640  1.00 39.79  ? 318 HOH C O   1 
HETATM 5824 O  O   . HOH J 4 .   ? 145.099 237.237 25.579  1.00 39.19  ? 319 HOH C O   1 
HETATM 5825 O  O   . HOH J 4 .   ? 127.957 209.501 17.202  1.00 29.73  ? 320 HOH C O   1 
HETATM 5826 O  O   . HOH J 4 .   ? 136.686 215.109 23.638  1.00 43.30  ? 321 HOH C O   1 
HETATM 5827 O  O   . HOH J 4 .   ? 128.136 209.615 21.316  1.00 30.66  ? 322 HOH C O   1 
HETATM 5828 O  O   . HOH J 4 .   ? 141.385 229.794 5.391   1.00 31.07  ? 323 HOH C O   1 
HETATM 5829 O  O   . HOH J 4 .   ? 132.278 229.697 15.038  1.00 36.93  ? 324 HOH C O   1 
HETATM 5830 O  O   . HOH J 4 .   ? 126.153 230.556 14.182  1.00 41.23  ? 325 HOH C O   1 
HETATM 5831 O  O   . HOH J 4 .   ? 140.925 216.760 29.755  1.00 48.22  ? 326 HOH C O   1 
HETATM 5832 O  O   . HOH J 4 .   ? 120.900 226.425 13.786  1.00 47.05  ? 327 HOH C O   1 
HETATM 5833 O  O   . HOH J 4 .   ? 119.649 227.366 16.305  1.00 48.05  ? 328 HOH C O   1 
HETATM 5834 O  O   . HOH J 4 .   ? 123.839 228.335 7.956   1.00 50.04  ? 329 HOH C O   1 
HETATM 5835 O  O   . HOH J 4 .   ? 125.131 217.457 29.414  1.00 41.44  ? 330 HOH C O   1 
HETATM 5836 O  O   . HOH J 4 .   ? 129.593 228.924 5.170   1.00 47.88  ? 331 HOH C O   1 
HETATM 5837 O  O   . HOH J 4 .   ? 140.179 217.339 -1.004  1.00 39.95  ? 332 HOH C O   1 
HETATM 5838 O  O   . HOH J 4 .   ? 129.689 209.023 19.504  1.00 41.35  ? 333 HOH C O   1 
HETATM 5839 O  O   . HOH J 4 .   ? 143.357 224.919 15.646  1.00 35.90  ? 334 HOH C O   1 
HETATM 5840 O  O   . HOH J 4 .   ? 116.634 224.326 30.639  1.00 45.31  ? 335 HOH C O   1 
HETATM 5841 O  O   . HOH J 4 .   ? 136.424 238.529 24.214  1.00 45.74  ? 336 HOH C O   1 
HETATM 5842 O  O   . HOH J 4 .   ? 133.162 236.060 25.124  1.00 42.35  ? 337 HOH C O   1 
HETATM 5843 O  O   . HOH K 4 .   ? 130.918 205.297 22.764  1.00 41.59  ? 301 HOH D O   1 
HETATM 5844 O  O   . HOH K 4 .   ? 145.308 205.012 6.835   1.00 53.82  ? 302 HOH D O   1 
HETATM 5845 O  O   . HOH K 4 .   ? 124.164 197.921 24.204  1.00 42.32  ? 303 HOH D O   1 
HETATM 5846 O  O   . HOH K 4 .   ? 143.225 209.068 11.730  1.00 42.87  ? 304 HOH D O   1 
HETATM 5847 O  O   . HOH K 4 .   ? 126.795 207.795 15.668  1.00 35.46  ? 305 HOH D O   1 
HETATM 5848 O  O   . HOH K 4 .   ? 146.180 211.880 11.833  1.00 48.61  ? 306 HOH D O   1 
HETATM 5849 O  O   . HOH K 4 .   ? 142.837 205.995 26.685  1.00 50.03  ? 307 HOH D O   1 
HETATM 5850 O  O   . HOH K 4 .   ? 120.091 208.438 12.093  1.00 53.50  ? 308 HOH D O   1 
HETATM 5851 O  O   . HOH K 4 .   ? 146.539 209.377 13.148  1.00 35.17  ? 309 HOH D O   1 
HETATM 5852 O  O   . HOH K 4 .   ? 134.903 206.192 19.913  1.00 33.00  ? 310 HOH D O   1 
HETATM 5853 O  O   . HOH K 4 .   ? 139.227 208.488 5.921   1.00 45.92  ? 311 HOH D O   1 
HETATM 5854 O  O   . HOH K 4 .   ? 161.635 212.692 27.136  1.00 72.04  ? 312 HOH D O   1 
HETATM 5855 O  O   . HOH K 4 .   ? 154.774 212.212 18.534  1.00 63.59  ? 313 HOH D O   1 
HETATM 5856 O  O   . HOH K 4 .   ? 136.729 209.428 6.083   1.00 48.93  ? 314 HOH D O   1 
HETATM 5857 O  O   . HOH K 4 .   ? 143.625 211.928 11.977  1.00 50.57  ? 315 HOH D O   1 
# 
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   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  ARG 46  46  46  ARG ARG A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 2 1   THR 1   2   ?   ?   ?   B . n 
B 2 2   THR 2   3   ?   ?   ?   B . n 
B 2 3   ASN 3   4   ?   ?   ?   B . n 
B 2 4   ASP 4   5   ?   ?   ?   B . n 
B 2 5   THR 5   6   ?   ?   ?   B . n 
B 2 6   TYR 6   7   ?   ?   ?   B . n 
B 2 7   GLU 7   8   8   GLU GLU B . n 
B 2 8   ALA 8   9   9   ALA ALA B . n 
B 2 9   THR 9   10  10  THR THR B . n 
B 2 10  TYR 10  11  11  TYR TYR B . n 
B 2 11  ALA 11  12  12  ALA ALA B . n 
B 2 12  ILE 12  13  13  ILE ILE B . n 
B 2 13  PRO 13  14  ?   ?   ?   B . n 
B 2 14  MET 14  15  ?   ?   ?   B . n 
B 2 15  HIS 15  16  ?   ?   ?   B . n 
B 2 16  CYS 16  17  17  CYS CYS B . n 
B 2 17  GLU 17  18  18  GLU GLU B . n 
B 2 18  ASN 18  19  19  ASN ASN B . n 
B 2 19  CYS 19  20  20  CYS CYS B . n 
B 2 20  VAL 20  21  21  VAL VAL B . n 
B 2 21  ASN 21  22  22  ASN ASN B . n 
B 2 22  ASP 22  23  23  ASP ASP B . n 
B 2 23  ILE 23  24  24  ILE ILE B . n 
B 2 24  LYS 24  25  25  LYS LYS B . n 
B 2 25  ALA 25  26  26  ALA ALA B . n 
B 2 26  CYS 26  27  27  CYS CYS B . n 
B 2 27  LEU 27  28  28  LEU LEU B . n 
B 2 28  LYS 28  29  29  LYS LYS B . n 
B 2 29  ASN 29  30  30  ASN ASN B . n 
B 2 30  VAL 30  31  31  VAL VAL B . n 
B 2 31  PRO 31  32  32  PRO PRO B . n 
B 2 32  GLY 32  33  33  GLY GLY B . n 
B 2 33  ILE 33  34  34  ILE ILE B . n 
B 2 34  ASN 34  35  35  ASN ASN B . n 
B 2 35  SER 35  36  36  SER SER B . n 
B 2 36  LEU 36  37  37  LEU LEU B . n 
B 2 37  ASN 37  38  38  ASN ASN B . n 
B 2 38  PHE 38  39  39  PHE PHE B . n 
B 2 39  ASP 39  40  40  ASP ASP B . n 
B 2 40  ILE 40  41  41  ILE ILE B . n 
B 2 41  GLU 41  42  42  GLU GLU B . n 
B 2 42  GLN 42  43  43  GLN GLN B . n 
B 2 43  GLN 43  44  44  GLN GLN B . n 
B 2 44  ILE 44  45  45  ILE ILE B . n 
B 2 45  MET 45  46  46  MET MET B . n 
B 2 46  SER 46  47  47  SER SER B . n 
B 2 47  VAL 47  48  48  VAL VAL B . n 
B 2 48  GLU 48  49  49  GLU GLU B . n 
B 2 49  SER 49  50  50  SER SER B . n 
B 2 50  SER 50  51  51  SER SER B . n 
B 2 51  VAL 51  52  52  VAL VAL B . n 
B 2 52  ALA 52  53  53  ALA ALA B . n 
B 2 53  PRO 53  54  54  PRO PRO B . n 
B 2 54  SER 54  55  55  SER SER B . n 
B 2 55  THR 55  56  56  THR THR B . n 
B 2 56  ILE 56  57  57  ILE ILE B . n 
B 2 57  ILE 57  58  58  ILE ILE B . n 
B 2 58  ASN 58  59  59  ASN ASN B . n 
B 2 59  THR 59  60  60  THR THR B . n 
B 2 60  LEU 60  61  61  LEU LEU B . n 
B 2 61  ARG 61  62  ?   ?   ?   B . n 
B 2 62  ASN 62  63  ?   ?   ?   B . n 
B 2 63  CYS 63  64  ?   ?   ?   B . n 
B 2 64  GLY 64  65  ?   ?   ?   B . n 
B 2 65  LYS 65  66  ?   ?   ?   B . n 
B 2 66  ASP 66  67  67  ASP ASP B . n 
B 2 67  ALA 67  68  68  ALA ALA B . n 
B 2 68  ILE 68  69  69  ILE ILE B . n 
B 2 69  ILE 69  70  70  ILE ILE B . n 
B 2 70  ARG 70  71  71  ARG ARG B . n 
B 2 71  GLY 71  72  72  GLY GLY B . n 
B 2 72  ALA 72  73  73  ALA ALA B . n 
B 2 73  GLY 73  74  74  GLY GLY B . n 
B 2 74  LYS 74  75  75  LYS LYS B . n 
B 2 75  PRO 75  76  76  PRO PRO B . n 
B 2 76  ASN 76  77  77  ASN ASN B . n 
B 2 77  SER 77  78  78  SER SER B . n 
B 2 78  SER 78  79  79  SER SER B . n 
B 2 79  ALA 79  80  80  ALA ALA B . n 
B 2 80  VAL 80  81  81  VAL VAL B . n 
B 2 81  ALA 81  82  82  ALA ALA B . n 
B 2 82  ILE 82  83  83  ILE ILE B . n 
B 2 83  LEU 83  84  84  LEU LEU B . n 
B 2 84  GLU 84  85  85  GLU GLU B . n 
B 2 85  THR 85  86  86  THR THR B . n 
B 2 86  PHE 86  87  87  PHE PHE B . n 
B 2 87  GLN 87  88  88  GLN GLN B . n 
B 2 88  LYS 88  89  89  LYS LYS B . n 
B 2 89  TYR 89  90  90  TYR TYR B . n 
B 2 90  THR 90  91  91  THR THR B . n 
B 2 91  ILE 91  92  92  ILE ILE B . n 
B 2 92  ASP 92  93  93  ASP ASP B . n 
B 2 93  GLN 93  94  94  GLN GLN B . n 
B 2 94  LYS 94  95  95  LYS LYS B . n 
B 2 95  LYS 95  96  96  LYS LYS B . n 
B 2 96  ASP 96  97  97  ASP ASP B . n 
B 2 97  THR 97  98  98  THR THR B . n 
B 2 98  ALA 98  99  99  ALA ALA B . n 
B 2 99  VAL 99  100 100 VAL VAL B . n 
B 2 100 ARG 100 101 101 ARG ARG B . n 
B 2 101 GLY 101 102 102 GLY GLY B . n 
B 2 102 LEU 102 103 103 LEU LEU B . n 
B 2 103 ALA 103 104 104 ALA ALA B . n 
B 2 104 ARG 104 105 105 ARG ARG B . n 
B 2 105 ILE 105 106 106 ILE ILE B . n 
B 2 106 VAL 106 107 107 VAL VAL B . n 
B 2 107 GLN 107 108 108 GLN GLN B . n 
B 2 108 VAL 108 109 109 VAL VAL B . n 
B 2 109 GLY 109 110 110 GLY GLY B . n 
B 2 110 GLU 110 111 111 GLU GLU B . n 
B 2 111 ASN 111 112 112 ASN ASN B . n 
B 2 112 LYS 112 113 113 LYS LYS B . n 
B 2 113 THR 113 114 114 THR THR B . n 
B 2 114 LEU 114 115 115 LEU LEU B . n 
B 2 115 PHE 115 116 116 PHE PHE B . n 
B 2 116 ASP 116 117 117 ASP ASP B . n 
B 2 117 ILE 117 118 118 ILE ILE B . n 
B 2 118 THR 118 119 119 THR THR B . n 
B 2 119 VAL 119 120 120 VAL VAL B . n 
B 2 120 ASN 120 121 121 ASN ASN B . n 
B 2 121 GLY 121 122 122 GLY GLY B . n 
B 2 122 VAL 122 123 123 VAL VAL B . n 
B 2 123 PRO 123 124 124 PRO PRO B . n 
B 2 124 GLU 124 125 125 GLU GLU B . n 
B 2 125 ALA 125 126 126 ALA ALA B . n 
B 2 126 GLY 126 127 127 GLY GLY B . n 
B 2 127 ASN 127 128 128 ASN ASN B . n 
B 2 128 TYR 128 129 129 TYR TYR B . n 
B 2 129 HIS 129 130 130 HIS HIS B . n 
B 2 130 ALA 130 131 131 ALA ALA B . n 
B 2 131 SER 131 132 132 SER SER B . n 
B 2 132 ILE 132 133 133 ILE ILE B . n 
B 2 133 HIS 133 134 134 HIS HIS B . n 
B 2 134 GLU 134 135 135 GLU GLU B . n 
B 2 135 LYS 135 136 136 LYS LYS B . n 
B 2 136 GLY 136 137 137 GLY GLY B . n 
B 2 137 ASP 137 138 138 ASP ASP B . n 
B 2 138 VAL 138 139 139 VAL VAL B . n 
B 2 139 SER 139 140 140 SER SER B . n 
B 2 140 LYS 140 141 141 LYS LYS B . n 
B 2 141 GLY 141 142 142 GLY GLY B . n 
B 2 142 VAL 142 143 143 VAL VAL B . n 
B 2 143 GLU 143 144 144 GLU GLU B . n 
B 2 144 SER 144 145 145 SER SER B . n 
B 2 145 THR 145 146 146 THR THR B . n 
B 2 146 GLY 146 147 147 GLY GLY B . n 
B 2 147 LYS 147 148 148 LYS LYS B . n 
B 2 148 VAL 148 149 149 VAL VAL B . n 
B 2 149 TRP 149 150 150 TRP TRP B . n 
B 2 150 HIS 150 151 151 HIS HIS B . n 
B 2 151 LYS 151 152 152 LYS LYS B . n 
B 2 152 PHE 152 153 153 PHE PHE B . n 
B 2 153 ASP 153 154 154 ASP ASP B . n 
B 2 154 GLU 154 155 155 GLU GLU B . n 
B 2 155 PRO 155 156 156 PRO PRO B . n 
B 2 156 ILE 156 157 157 ILE ILE B . n 
B 2 157 GLU 157 158 158 GLU GLU B . n 
B 2 158 CYS 158 159 159 CYS CYS B . n 
B 2 159 PHE 159 160 160 PHE PHE B . n 
B 2 160 ASN 160 161 161 ASN ASN B . n 
B 2 161 GLU 161 162 162 GLU GLU B . n 
B 2 162 SER 162 163 163 SER SER B . n 
B 2 163 ASP 163 164 164 ASP ASP B . n 
B 2 164 LEU 164 165 165 LEU LEU B . n 
B 2 165 GLY 165 166 166 GLY GLY B . n 
B 2 166 LYS 166 167 167 LYS LYS B . n 
B 2 167 ASN 167 168 168 ASN ASN B . n 
B 2 168 LEU 168 169 169 LEU LEU B . n 
B 2 169 TYR 169 170 170 TYR TYR B . n 
B 2 170 SER 170 171 171 SER SER B . n 
B 2 171 GLY 171 172 172 GLY GLY B . n 
B 2 172 LYS 172 173 173 LYS LYS B . n 
B 2 173 THR 173 174 174 THR THR B . n 
B 2 174 PHE 174 175 175 PHE PHE B . n 
B 2 175 LEU 175 176 176 LEU LEU B . n 
B 2 176 SER 176 177 177 SER SER B . n 
B 2 177 ALA 177 178 178 ALA ALA B . n 
B 2 178 PRO 178 179 179 PRO PRO B . n 
B 2 179 LEU 179 180 180 LEU LEU B . n 
B 2 180 PRO 180 181 181 PRO PRO B . n 
B 2 181 THR 181 182 182 THR THR B . n 
B 2 182 TRP 182 183 183 TRP TRP B . n 
B 2 183 GLN 183 184 184 GLN GLN B . n 
B 2 184 LEU 184 185 185 LEU LEU B . n 
B 2 185 ILE 185 186 186 ILE ILE B . n 
B 2 186 GLY 186 187 187 GLY GLY B . n 
B 2 187 ARG 187 188 188 ARG ARG B . n 
B 2 188 SER 188 189 189 SER SER B . n 
B 2 189 PHE 189 190 190 PHE PHE B . n 
B 2 190 VAL 190 191 191 VAL VAL B . n 
B 2 191 ILE 191 192 192 ILE ILE B . n 
B 2 192 SER 192 193 193 SER SER B . n 
B 2 193 LYS 193 194 194 LYS LYS B . n 
B 2 194 SER 194 195 195 SER SER B . n 
B 2 195 LEU 195 196 196 LEU LEU B . n 
B 2 196 ASN 196 197 197 ASN ASN B . n 
B 2 197 HIS 197 198 198 HIS HIS B . n 
B 2 198 PRO 198 199 199 PRO PRO B . n 
B 2 199 GLU 199 200 200 GLU GLU B . n 
B 2 200 ASN 200 201 201 ASN ASN B . n 
B 2 201 GLU 201 202 202 GLU GLU B . n 
B 2 202 PRO 202 203 203 PRO PRO B . n 
B 2 203 SER 203 204 204 SER SER B . n 
B 2 204 SER 204 205 205 SER SER B . n 
B 2 205 VAL 205 206 206 VAL VAL B . n 
B 2 206 LYS 206 207 207 LYS LYS B . n 
B 2 207 ASP 207 208 208 ASP ASP B . n 
B 2 208 TYR 208 209 209 TYR TYR B . n 
B 2 209 SER 209 210 210 SER SER B . n 
B 2 210 PHE 210 211 211 PHE PHE B . n 
B 2 211 LEU 211 212 212 LEU LEU B . n 
B 2 212 GLY 212 213 213 GLY GLY B . n 
B 2 213 VAL 213 214 214 VAL VAL B . n 
B 2 214 ILE 214 215 215 ILE ILE B . n 
B 2 215 ALA 215 216 216 ALA ALA B . n 
B 2 216 ARG 216 217 217 ARG ARG B . n 
B 2 217 SER 217 218 218 SER SER B . n 
B 2 218 ALA 218 219 219 ALA ALA B . n 
B 2 219 GLY 219 220 220 GLY GLY B . n 
B 2 220 VAL 220 221 221 VAL VAL B . n 
B 2 221 TRP 221 222 222 TRP TRP B . n 
B 2 222 GLU 222 223 223 GLU GLU B . n 
B 2 223 ASN 223 224 224 ASN ASN B . n 
B 2 224 ASN 224 225 225 ASN ASN B . n 
B 2 225 LYS 225 226 226 LYS LYS B . n 
B 2 226 GLN 226 227 227 GLN GLN B . n 
B 2 227 VAL 227 228 228 VAL VAL B . n 
B 2 228 CYS 228 229 229 CYS CYS B . n 
B 2 229 ALA 229 230 230 ALA ALA B . n 
B 2 230 CYS 230 231 231 CYS CYS B . n 
B 2 231 THR 231 232 232 THR THR B . n 
B 2 232 GLY 232 233 233 GLY GLY B . n 
B 2 233 LYS 233 234 234 LYS LYS B . n 
B 2 234 THR 234 235 235 THR THR B . n 
B 2 235 VAL 235 236 236 VAL VAL B . n 
B 2 236 TRP 236 237 237 TRP TRP B . n 
B 2 237 ALA 237 238 238 ALA ALA B . n 
B 2 238 ALA 238 239 239 ALA ALA B . n 
B 2 239 ALA 239 240 240 ALA ALA B . n 
B 2 240 LYS 240 241 241 LYS LYS B . n 
B 2 241 ASP 241 242 ?   ?   ?   B . n 
B 2 242 ALA 242 243 ?   ?   ?   B . n 
B 2 243 LEU 243 244 ?   ?   ?   B . n 
B 2 244 ALA 244 245 ?   ?   ?   B . n 
B 2 245 ASN 245 246 ?   ?   ?   B . n 
B 2 246 ASN 246 247 ?   ?   ?   B . n 
B 2 247 ILE 247 248 ?   ?   ?   B . n 
B 2 248 LYS 248 249 ?   ?   ?   B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  ARG 46  46  46  ARG ARG C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  GLN 48  48  48  GLN GLN C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 2 1   THR 1   2   ?   ?   ?   D . n 
D 2 2   THR 2   3   ?   ?   ?   D . n 
D 2 3   ASN 3   4   ?   ?   ?   D . n 
D 2 4   ASP 4   5   ?   ?   ?   D . n 
D 2 5   THR 5   6   6   THR THR D . n 
D 2 6   TYR 6   7   7   TYR TYR D . n 
D 2 7   GLU 7   8   8   GLU GLU D . n 
D 2 8   ALA 8   9   9   ALA ALA D . n 
D 2 9   THR 9   10  10  THR THR D . n 
D 2 10  TYR 10  11  11  TYR TYR D . n 
D 2 11  ALA 11  12  12  ALA ALA D . n 
D 2 12  ILE 12  13  13  ILE ILE D . n 
D 2 13  PRO 13  14  14  PRO PRO D . n 
D 2 14  MET 14  15  ?   ?   ?   D . n 
D 2 15  HIS 15  16  ?   ?   ?   D . n 
D 2 16  CYS 16  17  17  CYS CYS D . n 
D 2 17  GLU 17  18  18  GLU GLU D . n 
D 2 18  ASN 18  19  19  ASN ASN D . n 
D 2 19  CYS 19  20  20  CYS CYS D . n 
D 2 20  VAL 20  21  21  VAL VAL D . n 
D 2 21  ASN 21  22  22  ASN ASN D . n 
D 2 22  ASP 22  23  23  ASP ASP D . n 
D 2 23  ILE 23  24  24  ILE ILE D . n 
D 2 24  LYS 24  25  25  LYS LYS D . n 
D 2 25  ALA 25  26  26  ALA ALA D . n 
D 2 26  CYS 26  27  27  CYS CYS D . n 
D 2 27  LEU 27  28  28  LEU LEU D . n 
D 2 28  LYS 28  29  29  LYS LYS D . n 
D 2 29  ASN 29  30  30  ASN ASN D . n 
D 2 30  VAL 30  31  31  VAL VAL D . n 
D 2 31  PRO 31  32  32  PRO PRO D . n 
D 2 32  GLY 32  33  33  GLY GLY D . n 
D 2 33  ILE 33  34  34  ILE ILE D . n 
D 2 34  ASN 34  35  35  ASN ASN D . n 
D 2 35  SER 35  36  36  SER SER D . n 
D 2 36  LEU 36  37  37  LEU LEU D . n 
D 2 37  ASN 37  38  38  ASN ASN D . n 
D 2 38  PHE 38  39  39  PHE PHE D . n 
D 2 39  ASP 39  40  40  ASP ASP D . n 
D 2 40  ILE 40  41  41  ILE ILE D . n 
D 2 41  GLU 41  42  42  GLU GLU D . n 
D 2 42  GLN 42  43  43  GLN GLN D . n 
D 2 43  GLN 43  44  44  GLN GLN D . n 
D 2 44  ILE 44  45  45  ILE ILE D . n 
D 2 45  MET 45  46  46  MET MET D . n 
D 2 46  SER 46  47  47  SER SER D . n 
D 2 47  VAL 47  48  48  VAL VAL D . n 
D 2 48  GLU 48  49  49  GLU GLU D . n 
D 2 49  SER 49  50  50  SER SER D . n 
D 2 50  SER 50  51  51  SER SER D . n 
D 2 51  VAL 51  52  52  VAL VAL D . n 
D 2 52  ALA 52  53  53  ALA ALA D . n 
D 2 53  PRO 53  54  54  PRO PRO D . n 
D 2 54  SER 54  55  55  SER SER D . n 
D 2 55  THR 55  56  56  THR THR D . n 
D 2 56  ILE 56  57  57  ILE ILE D . n 
D 2 57  ILE 57  58  58  ILE ILE D . n 
D 2 58  ASN 58  59  59  ASN ASN D . n 
D 2 59  THR 59  60  60  THR THR D . n 
D 2 60  LEU 60  61  61  LEU LEU D . n 
D 2 61  ARG 61  62  62  ARG ARG D . n 
D 2 62  ASN 62  63  63  ASN ASN D . n 
D 2 63  CYS 63  64  64  CYS CYS D . n 
D 2 64  GLY 64  65  65  GLY GLY D . n 
D 2 65  LYS 65  66  66  LYS LYS D . n 
D 2 66  ASP 66  67  67  ASP ASP D . n 
D 2 67  ALA 67  68  68  ALA ALA D . n 
D 2 68  ILE 68  69  69  ILE ILE D . n 
D 2 69  ILE 69  70  70  ILE ILE D . n 
D 2 70  ARG 70  71  71  ARG ARG D . n 
D 2 71  GLY 71  72  72  GLY GLY D . n 
D 2 72  ALA 72  73  73  ALA ALA D . n 
D 2 73  GLY 73  74  74  GLY GLY D . n 
D 2 74  LYS 74  75  75  LYS LYS D . n 
D 2 75  PRO 75  76  76  PRO PRO D . n 
D 2 76  ASN 76  77  77  ASN ASN D . n 
D 2 77  SER 77  78  78  SER SER D . n 
D 2 78  SER 78  79  79  SER SER D . n 
D 2 79  ALA 79  80  80  ALA ALA D . n 
D 2 80  VAL 80  81  81  VAL VAL D . n 
D 2 81  ALA 81  82  82  ALA ALA D . n 
D 2 82  ILE 82  83  83  ILE ILE D . n 
D 2 83  LEU 83  84  84  LEU LEU D . n 
D 2 84  GLU 84  85  85  GLU GLU D . n 
D 2 85  THR 85  86  86  THR THR D . n 
D 2 86  PHE 86  87  87  PHE PHE D . n 
D 2 87  GLN 87  88  88  GLN GLN D . n 
D 2 88  LYS 88  89  89  LYS LYS D . n 
D 2 89  TYR 89  90  90  TYR TYR D . n 
D 2 90  THR 90  91  91  THR THR D . n 
D 2 91  ILE 91  92  92  ILE ILE D . n 
D 2 92  ASP 92  93  93  ASP ASP D . n 
D 2 93  GLN 93  94  94  GLN GLN D . n 
D 2 94  LYS 94  95  95  LYS LYS D . n 
D 2 95  LYS 95  96  96  LYS LYS D . n 
D 2 96  ASP 96  97  97  ASP ASP D . n 
D 2 97  THR 97  98  98  THR THR D . n 
D 2 98  ALA 98  99  99  ALA ALA D . n 
D 2 99  VAL 99  100 100 VAL VAL D . n 
D 2 100 ARG 100 101 101 ARG ARG D . n 
D 2 101 GLY 101 102 102 GLY GLY D . n 
D 2 102 LEU 102 103 103 LEU LEU D . n 
D 2 103 ALA 103 104 104 ALA ALA D . n 
D 2 104 ARG 104 105 105 ARG ARG D . n 
D 2 105 ILE 105 106 106 ILE ILE D . n 
D 2 106 VAL 106 107 107 VAL VAL D . n 
D 2 107 GLN 107 108 108 GLN GLN D . n 
D 2 108 VAL 108 109 109 VAL VAL D . n 
D 2 109 GLY 109 110 110 GLY GLY D . n 
D 2 110 GLU 110 111 111 GLU GLU D . n 
D 2 111 ASN 111 112 112 ASN ASN D . n 
D 2 112 LYS 112 113 113 LYS LYS D . n 
D 2 113 THR 113 114 114 THR THR D . n 
D 2 114 LEU 114 115 115 LEU LEU D . n 
D 2 115 PHE 115 116 116 PHE PHE D . n 
D 2 116 ASP 116 117 117 ASP ASP D . n 
D 2 117 ILE 117 118 118 ILE ILE D . n 
D 2 118 THR 118 119 119 THR THR D . n 
D 2 119 VAL 119 120 120 VAL VAL D . n 
D 2 120 ASN 120 121 121 ASN ASN D . n 
D 2 121 GLY 121 122 122 GLY GLY D . n 
D 2 122 VAL 122 123 123 VAL VAL D . n 
D 2 123 PRO 123 124 124 PRO PRO D . n 
D 2 124 GLU 124 125 125 GLU GLU D . n 
D 2 125 ALA 125 126 126 ALA ALA D . n 
D 2 126 GLY 126 127 127 GLY GLY D . n 
D 2 127 ASN 127 128 128 ASN ASN D . n 
D 2 128 TYR 128 129 129 TYR TYR D . n 
D 2 129 HIS 129 130 130 HIS HIS D . n 
D 2 130 ALA 130 131 131 ALA ALA D . n 
D 2 131 SER 131 132 132 SER SER D . n 
D 2 132 ILE 132 133 133 ILE ILE D . n 
D 2 133 HIS 133 134 134 HIS HIS D . n 
D 2 134 GLU 134 135 135 GLU GLU D . n 
D 2 135 LYS 135 136 136 LYS LYS D . n 
D 2 136 GLY 136 137 137 GLY GLY D . n 
D 2 137 ASP 137 138 138 ASP ASP D . n 
D 2 138 VAL 138 139 139 VAL VAL D . n 
D 2 139 SER 139 140 140 SER SER D . n 
D 2 140 LYS 140 141 141 LYS LYS D . n 
D 2 141 GLY 141 142 142 GLY GLY D . n 
D 2 142 VAL 142 143 143 VAL VAL D . n 
D 2 143 GLU 143 144 144 GLU GLU D . n 
D 2 144 SER 144 145 145 SER SER D . n 
D 2 145 THR 145 146 146 THR THR D . n 
D 2 146 GLY 146 147 147 GLY GLY D . n 
D 2 147 LYS 147 148 148 LYS LYS D . n 
D 2 148 VAL 148 149 149 VAL VAL D . n 
D 2 149 TRP 149 150 150 TRP TRP D . n 
D 2 150 HIS 150 151 151 HIS HIS D . n 
D 2 151 LYS 151 152 152 LYS LYS D . n 
D 2 152 PHE 152 153 153 PHE PHE D . n 
D 2 153 ASP 153 154 154 ASP ASP D . n 
D 2 154 GLU 154 155 155 GLU GLU D . n 
D 2 155 PRO 155 156 156 PRO PRO D . n 
D 2 156 ILE 156 157 157 ILE ILE D . n 
D 2 157 GLU 157 158 158 GLU GLU D . n 
D 2 158 CYS 158 159 159 CYS CYS D . n 
D 2 159 PHE 159 160 160 PHE PHE D . n 
D 2 160 ASN 160 161 161 ASN ASN D . n 
D 2 161 GLU 161 162 162 GLU GLU D . n 
D 2 162 SER 162 163 163 SER SER D . n 
D 2 163 ASP 163 164 164 ASP ASP D . n 
D 2 164 LEU 164 165 165 LEU LEU D . n 
D 2 165 GLY 165 166 166 GLY GLY D . n 
D 2 166 LYS 166 167 167 LYS LYS D . n 
D 2 167 ASN 167 168 168 ASN ASN D . n 
D 2 168 LEU 168 169 169 LEU LEU D . n 
D 2 169 TYR 169 170 170 TYR TYR D . n 
D 2 170 SER 170 171 171 SER SER D . n 
D 2 171 GLY 171 172 172 GLY GLY D . n 
D 2 172 LYS 172 173 173 LYS LYS D . n 
D 2 173 THR 173 174 174 THR THR D . n 
D 2 174 PHE 174 175 175 PHE PHE D . n 
D 2 175 LEU 175 176 176 LEU LEU D . n 
D 2 176 SER 176 177 177 SER SER D . n 
D 2 177 ALA 177 178 178 ALA ALA D . n 
D 2 178 PRO 178 179 179 PRO PRO D . n 
D 2 179 LEU 179 180 180 LEU LEU D . n 
D 2 180 PRO 180 181 181 PRO PRO D . n 
D 2 181 THR 181 182 182 THR THR D . n 
D 2 182 TRP 182 183 183 TRP TRP D . n 
D 2 183 GLN 183 184 184 GLN GLN D . n 
D 2 184 LEU 184 185 185 LEU LEU D . n 
D 2 185 ILE 185 186 186 ILE ILE D . n 
D 2 186 GLY 186 187 187 GLY GLY D . n 
D 2 187 ARG 187 188 188 ARG ARG D . n 
D 2 188 SER 188 189 189 SER SER D . n 
D 2 189 PHE 189 190 190 PHE PHE D . n 
D 2 190 VAL 190 191 191 VAL VAL D . n 
D 2 191 ILE 191 192 192 ILE ILE D . n 
D 2 192 SER 192 193 193 SER SER D . n 
D 2 193 LYS 193 194 194 LYS LYS D . n 
D 2 194 SER 194 195 195 SER SER D . n 
D 2 195 LEU 195 196 196 LEU LEU D . n 
D 2 196 ASN 196 197 197 ASN ASN D . n 
D 2 197 HIS 197 198 198 HIS HIS D . n 
D 2 198 PRO 198 199 199 PRO PRO D . n 
D 2 199 GLU 199 200 200 GLU GLU D . n 
D 2 200 ASN 200 201 201 ASN ASN D . n 
D 2 201 GLU 201 202 202 GLU GLU D . n 
D 2 202 PRO 202 203 203 PRO PRO D . n 
D 2 203 SER 203 204 204 SER SER D . n 
D 2 204 SER 204 205 205 SER SER D . n 
D 2 205 VAL 205 206 206 VAL VAL D . n 
D 2 206 LYS 206 207 207 LYS LYS D . n 
D 2 207 ASP 207 208 208 ASP ASP D . n 
D 2 208 TYR 208 209 209 TYR TYR D . n 
D 2 209 SER 209 210 210 SER SER D . n 
D 2 210 PHE 210 211 211 PHE PHE D . n 
D 2 211 LEU 211 212 212 LEU LEU D . n 
D 2 212 GLY 212 213 213 GLY GLY D . n 
D 2 213 VAL 213 214 214 VAL VAL D . n 
D 2 214 ILE 214 215 215 ILE ILE D . n 
D 2 215 ALA 215 216 216 ALA ALA D . n 
D 2 216 ARG 216 217 217 ARG ARG D . n 
D 2 217 SER 217 218 218 SER SER D . n 
D 2 218 ALA 218 219 219 ALA ALA D . n 
D 2 219 GLY 219 220 220 GLY GLY D . n 
D 2 220 VAL 220 221 221 VAL VAL D . n 
D 2 221 TRP 221 222 222 TRP TRP D . n 
D 2 222 GLU 222 223 223 GLU GLU D . n 
D 2 223 ASN 223 224 224 ASN ASN D . n 
D 2 224 ASN 224 225 225 ASN ASN D . n 
D 2 225 LYS 225 226 226 LYS LYS D . n 
D 2 226 GLN 226 227 227 GLN GLN D . n 
D 2 227 VAL 227 228 228 VAL VAL D . n 
D 2 228 CYS 228 229 229 CYS CYS D . n 
D 2 229 ALA 229 230 230 ALA ALA D . n 
D 2 230 CYS 230 231 231 CYS CYS D . n 
D 2 231 THR 231 232 232 THR THR D . n 
D 2 232 GLY 232 233 233 GLY GLY D . n 
D 2 233 LYS 233 234 234 LYS LYS D . n 
D 2 234 THR 234 235 235 THR THR D . n 
D 2 235 VAL 235 236 236 VAL VAL D . n 
D 2 236 TRP 236 237 237 TRP TRP D . n 
D 2 237 ALA 237 238 238 ALA ALA D . n 
D 2 238 ALA 238 239 239 ALA ALA D . n 
D 2 239 ALA 239 240 240 ALA ALA D . n 
D 2 240 LYS 240 241 241 LYS LYS D . n 
D 2 241 ASP 241 242 ?   ?   ?   D . n 
D 2 242 ALA 242 243 ?   ?   ?   D . n 
D 2 243 LEU 243 244 ?   ?   ?   D . n 
D 2 244 ALA 244 245 ?   ?   ?   D . n 
D 2 245 ASN 245 246 ?   ?   ?   D . n 
D 2 246 ASN 246 247 ?   ?   ?   D . n 
D 2 247 ILE 247 248 ?   ?   ?   D . n 
D 2 248 LYS 248 249 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 ZN  1  201 155 ZN  ZN  A . 
F 3 ZN  1  301 301 ZN  ZN  B . 
G 3 ZN  1  201 155 ZN  ZN  C . 
H 4 HOH 1  301 74  HOH HOH A . 
H 4 HOH 2  302 10  HOH HOH A . 
H 4 HOH 3  303 48  HOH HOH A . 
H 4 HOH 4  304 44  HOH HOH A . 
H 4 HOH 5  305 88  HOH HOH A . 
H 4 HOH 6  306 4   HOH HOH A . 
H 4 HOH 7  307 79  HOH HOH A . 
H 4 HOH 8  308 104 HOH HOH A . 
H 4 HOH 9  309 65  HOH HOH A . 
H 4 HOH 10 310 53  HOH HOH A . 
H 4 HOH 11 311 15  HOH HOH A . 
H 4 HOH 12 312 101 HOH HOH A . 
H 4 HOH 13 313 7   HOH HOH A . 
H 4 HOH 14 314 25  HOH HOH A . 
H 4 HOH 15 315 66  HOH HOH A . 
H 4 HOH 16 316 6   HOH HOH A . 
H 4 HOH 17 317 46  HOH HOH A . 
H 4 HOH 18 318 36  HOH HOH A . 
H 4 HOH 19 319 38  HOH HOH A . 
H 4 HOH 20 320 55  HOH HOH A . 
H 4 HOH 21 321 106 HOH HOH A . 
H 4 HOH 22 322 1   HOH HOH A . 
H 4 HOH 23 323 75  HOH HOH A . 
H 4 HOH 24 324 100 HOH HOH A . 
H 4 HOH 25 325 107 HOH HOH A . 
H 4 HOH 26 326 9   HOH HOH A . 
H 4 HOH 27 327 31  HOH HOH A . 
H 4 HOH 28 328 63  HOH HOH A . 
H 4 HOH 29 329 43  HOH HOH A . 
H 4 HOH 30 330 40  HOH HOH A . 
H 4 HOH 31 331 45  HOH HOH A . 
H 4 HOH 32 332 102 HOH HOH A . 
H 4 HOH 33 333 78  HOH HOH A . 
H 4 HOH 34 334 83  HOH HOH A . 
H 4 HOH 35 335 35  HOH HOH A . 
H 4 HOH 36 336 91  HOH HOH A . 
H 4 HOH 37 337 99  HOH HOH A . 
H 4 HOH 38 338 60  HOH HOH A . 
H 4 HOH 39 339 119 HOH HOH A . 
H 4 HOH 40 340 92  HOH HOH A . 
H 4 HOH 41 341 50  HOH HOH A . 
H 4 HOH 42 342 95  HOH HOH A . 
H 4 HOH 43 343 87  HOH HOH A . 
H 4 HOH 44 344 90  HOH HOH A . 
I 4 HOH 1  401 52  HOH HOH B . 
I 4 HOH 2  402 11  HOH HOH B . 
I 4 HOH 3  403 18  HOH HOH B . 
I 4 HOH 4  404 17  HOH HOH B . 
I 4 HOH 5  405 32  HOH HOH B . 
I 4 HOH 6  406 71  HOH HOH B . 
I 4 HOH 7  407 16  HOH HOH B . 
I 4 HOH 8  408 67  HOH HOH B . 
I 4 HOH 9  409 14  HOH HOH B . 
I 4 HOH 10 410 116 HOH HOH B . 
I 4 HOH 11 411 111 HOH HOH B . 
I 4 HOH 12 412 121 HOH HOH B . 
I 4 HOH 13 413 58  HOH HOH B . 
I 4 HOH 14 414 24  HOH HOH B . 
I 4 HOH 15 415 70  HOH HOH B . 
I 4 HOH 16 416 33  HOH HOH B . 
I 4 HOH 17 417 89  HOH HOH B . 
I 4 HOH 18 418 117 HOH HOH B . 
I 4 HOH 19 419 120 HOH HOH B . 
I 4 HOH 20 420 96  HOH HOH B . 
I 4 HOH 21 421 73  HOH HOH B . 
I 4 HOH 22 422 109 HOH HOH B . 
I 4 HOH 23 423 97  HOH HOH B . 
I 4 HOH 24 424 85  HOH HOH B . 
J 4 HOH 1  301 29  HOH HOH C . 
J 4 HOH 2  302 30  HOH HOH C . 
J 4 HOH 3  303 47  HOH HOH C . 
J 4 HOH 4  304 72  HOH HOH C . 
J 4 HOH 5  305 56  HOH HOH C . 
J 4 HOH 6  306 13  HOH HOH C . 
J 4 HOH 7  307 5   HOH HOH C . 
J 4 HOH 8  308 8   HOH HOH C . 
J 4 HOH 9  309 81  HOH HOH C . 
J 4 HOH 10 310 3   HOH HOH C . 
J 4 HOH 11 311 42  HOH HOH C . 
J 4 HOH 12 312 26  HOH HOH C . 
J 4 HOH 13 313 2   HOH HOH C . 
J 4 HOH 14 314 12  HOH HOH C . 
J 4 HOH 15 315 84  HOH HOH C . 
J 4 HOH 16 316 37  HOH HOH C . 
J 4 HOH 17 317 61  HOH HOH C . 
J 4 HOH 18 318 69  HOH HOH C . 
J 4 HOH 19 319 21  HOH HOH C . 
J 4 HOH 20 320 51  HOH HOH C . 
J 4 HOH 21 321 23  HOH HOH C . 
J 4 HOH 22 322 19  HOH HOH C . 
J 4 HOH 23 323 28  HOH HOH C . 
J 4 HOH 24 324 20  HOH HOH C . 
J 4 HOH 25 325 77  HOH HOH C . 
J 4 HOH 26 326 86  HOH HOH C . 
J 4 HOH 27 327 115 HOH HOH C . 
J 4 HOH 28 328 68  HOH HOH C . 
J 4 HOH 29 329 105 HOH HOH C . 
J 4 HOH 30 330 57  HOH HOH C . 
J 4 HOH 31 331 112 HOH HOH C . 
J 4 HOH 32 332 82  HOH HOH C . 
J 4 HOH 33 333 62  HOH HOH C . 
J 4 HOH 34 334 108 HOH HOH C . 
J 4 HOH 35 335 93  HOH HOH C . 
J 4 HOH 36 336 114 HOH HOH C . 
J 4 HOH 37 337 94  HOH HOH C . 
K 4 HOH 1  301 41  HOH HOH D . 
K 4 HOH 2  302 49  HOH HOH D . 
K 4 HOH 3  303 27  HOH HOH D . 
K 4 HOH 4  304 39  HOH HOH D . 
K 4 HOH 5  305 54  HOH HOH D . 
K 4 HOH 6  306 64  HOH HOH D . 
K 4 HOH 7  307 34  HOH HOH D . 
K 4 HOH 8  308 80  HOH HOH D . 
K 4 HOH 9  309 22  HOH HOH D . 
K 4 HOH 10 310 103 HOH HOH D . 
K 4 HOH 11 311 76  HOH HOH D . 
K 4 HOH 12 312 110 HOH HOH D . 
K 4 HOH 13 313 98  HOH HOH D . 
K 4 HOH 14 314 113 HOH HOH D . 
K 4 HOH 15 315 118 HOH HOH D . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,H,I 
2 1 C,D,G,J,K   
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1840  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  17830 ? 
2 'ABSA (A^2)' 1860  ? 
2 MORE         -13   ? 
2 'SSA (A^2)'  17630 ? 
# 
_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_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 101.2 ? 
2  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 112.8 ? 
3  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 127.4 ? 
4  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 89.9  ? 
5  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 99.6  ? 
6  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 118.6 ? 
7  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 143.2 ? 
8  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 80.9  ? 
9  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 93.1  ? 
10 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 54.0  ? 
11 SG  ? B CYS 16 ? B CYS 17 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 19 ? B CYS 20 ? 1_555 108.2 ? 
12 SG  ? B CYS 16 ? B CYS 17 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? D CYS 16 ? D CYS 17 ? 1_555 130.4 ? 
13 SG  ? B CYS 19 ? B CYS 20 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? D CYS 16 ? D CYS 17 ? 1_555 42.8  ? 
14 SG  ? B CYS 16 ? B CYS 17 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? D CYS 19 ? D CYS 20 ? 1_555 130.6 ? 
15 SG  ? B CYS 19 ? B CYS 20 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? D CYS 19 ? D CYS 20 ? 1_555 41.3  ? 
16 SG  ? D CYS 16 ? D CYS 17 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? D CYS 19 ? D CYS 20 ? 1_555 1.7   ? 
17 ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 105.9 ? 
18 ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 114.8 ? 
19 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 125.1 ? 
20 ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 94.0  ? 
21 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 96.7  ? 
22 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 114.8 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2017-05-31 
2 'Structure model' 1 1 2017-06-07 
3 'Structure model' 1 2 2017-08-02 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_citation.journal_volume' 
2 3 'Structure model' '_citation.page_first'     
3 3 'Structure model' '_citation.page_last'      
4 3 'Structure model' '_citation.title'          
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.9_1692 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   D 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    93 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OH 
_pdbx_validate_close_contact.auth_asym_id_2   D 
_pdbx_validate_close_contact.auth_comp_id_2   TYR 
_pdbx_validate_close_contact.auth_seq_id_2    209 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.07 
# 
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 CYS B 159 ? ? -106.64 79.31 
2 1 PRO B 179 ? ? -82.28  49.31 
3 1 SER B 204 ? ? -63.88  0.43  
4 1 ASN C 65  ? ? -145.52 59.73 
5 1 CYS D 159 ? ? -105.48 79.43 
6 1 PRO D 179 ? ? -82.09  49.00 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B THR 2   ? B THR 1   
2  1 Y 1 B THR 3   ? B THR 2   
3  1 Y 1 B ASN 4   ? B ASN 3   
4  1 Y 1 B ASP 5   ? B ASP 4   
5  1 Y 1 B THR 6   ? B THR 5   
6  1 Y 1 B TYR 7   ? B TYR 6   
7  1 Y 1 B PRO 14  ? B PRO 13  
8  1 Y 1 B MET 15  ? B MET 14  
9  1 Y 1 B HIS 16  ? B HIS 15  
10 1 Y 1 B ARG 62  ? B ARG 61  
11 1 Y 1 B ASN 63  ? B ASN 62  
12 1 Y 1 B CYS 64  ? B CYS 63  
13 1 Y 1 B GLY 65  ? B GLY 64  
14 1 Y 1 B LYS 66  ? B LYS 65  
15 1 Y 1 B ASP 242 ? B ASP 241 
16 1 Y 1 B ALA 243 ? B ALA 242 
17 1 Y 1 B LEU 244 ? B LEU 243 
18 1 Y 1 B ALA 245 ? B ALA 244 
19 1 Y 1 B ASN 246 ? B ASN 245 
20 1 Y 1 B ASN 247 ? B ASN 246 
21 1 Y 1 B ILE 248 ? B ILE 247 
22 1 Y 1 B LYS 249 ? B LYS 248 
23 1 Y 1 D THR 2   ? D THR 1   
24 1 Y 1 D THR 3   ? D THR 2   
25 1 Y 1 D ASN 4   ? D ASN 3   
26 1 Y 1 D ASP 5   ? D ASP 4   
27 1 Y 1 D MET 15  ? D MET 14  
28 1 Y 1 D HIS 16  ? D HIS 15  
29 1 Y 1 D ASP 242 ? D ASP 241 
30 1 Y 1 D ALA 243 ? D ALA 242 
31 1 Y 1 D LEU 244 ? D LEU 243 
32 1 Y 1 D ALA 245 ? D ALA 244 
33 1 Y 1 D ASN 246 ? D ASN 245 
34 1 Y 1 D ASN 247 ? D ASN 246 
35 1 Y 1 D ILE 248 ? D ILE 247 
36 1 Y 1 D LYS 249 ? D LYS 248 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'ZINC ION' ZN  
4 water      HOH 
# 
