data_8ZBC
# 
_entry.id   8ZBC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZBC         pdb_00008zbc 10.2210/pdb8zbc/pdb 
WWPDB D_1300047356 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZBC 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              6210201100@stu.jiangnan.edu.cn 
_pdbx_contact_author.name_first         zihao 
_pdbx_contact_author.name_last          yin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0001-7770-4992 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yin, Z.'  1 ? 
'Jing, W.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'An acyltransferase with selective perhydrolytic activity' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yin, Z.'  1 ? 
primary 'Jing, W.' 2 ? 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'SGNH/GDSL hydrolase family protein' 
_entity.formula_weight             25028.111 
_entity.pdbx_number_of_molecules   6 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;QDKIKRVFVFGD(SEP)LTWGWTPVAPIVPTTRHPHADRWTTVLGENLGDGYELVVDGLSGRTTNIDDPNDPKLNGADYL
PAALAAHEPLDLVIILLGTNDTKTYLNRTPFEIGLGAGALINMVQKSPGWDWTDYPPPPVLLISPPPLGETIDPLAAPIF
VDGLAKSEALPGVYKAIAEAAGESFFDAGSVVSTDGVDGIHFTAETNRTLGAAVAQKVKTLLQPKLAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QDKIKRVFVFGDSLTWGWTPVAPIVPTTRHPHADRWTTVLGENLGDGYELVVDGLSGRTTNIDDPNDPKLNGADYLPAAL
AAHEPLDLVIILLGTNDTKTYLNRTPFEIGLGAGALINMVQKSPGWDWTDYPPPPVLLISPPPLGETIDPLAAPIFVDGL
AKSEALPGVYKAIAEAAGESFFDAGSVVSTDGVDGIHFTAETNRTLGAAVAQKVKTLLQPKLAAALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   ASP n 
1 3   LYS n 
1 4   ILE n 
1 5   LYS n 
1 6   ARG n 
1 7   VAL n 
1 8   PHE n 
1 9   VAL n 
1 10  PHE n 
1 11  GLY n 
1 12  ASP n 
1 13  SEP n 
1 14  LEU n 
1 15  THR n 
1 16  TRP n 
1 17  GLY n 
1 18  TRP n 
1 19  THR n 
1 20  PRO n 
1 21  VAL n 
1 22  ALA n 
1 23  PRO n 
1 24  ILE n 
1 25  VAL n 
1 26  PRO n 
1 27  THR n 
1 28  THR n 
1 29  ARG n 
1 30  HIS n 
1 31  PRO n 
1 32  HIS n 
1 33  ALA n 
1 34  ASP n 
1 35  ARG n 
1 36  TRP n 
1 37  THR n 
1 38  THR n 
1 39  VAL n 
1 40  LEU n 
1 41  GLY n 
1 42  GLU n 
1 43  ASN n 
1 44  LEU n 
1 45  GLY n 
1 46  ASP n 
1 47  GLY n 
1 48  TYR n 
1 49  GLU n 
1 50  LEU n 
1 51  VAL n 
1 52  VAL n 
1 53  ASP n 
1 54  GLY n 
1 55  LEU n 
1 56  SER n 
1 57  GLY n 
1 58  ARG n 
1 59  THR n 
1 60  THR n 
1 61  ASN n 
1 62  ILE n 
1 63  ASP n 
1 64  ASP n 
1 65  PRO n 
1 66  ASN n 
1 67  ASP n 
1 68  PRO n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  GLY n 
1 73  ALA n 
1 74  ASP n 
1 75  TYR n 
1 76  LEU n 
1 77  PRO n 
1 78  ALA n 
1 79  ALA n 
1 80  LEU n 
1 81  ALA n 
1 82  ALA n 
1 83  HIS n 
1 84  GLU n 
1 85  PRO n 
1 86  LEU n 
1 87  ASP n 
1 88  LEU n 
1 89  VAL n 
1 90  ILE n 
1 91  ILE n 
1 92  LEU n 
1 93  LEU n 
1 94  GLY n 
1 95  THR n 
1 96  ASN n 
1 97  ASP n 
1 98  THR n 
1 99  LYS n 
1 100 THR n 
1 101 TYR n 
1 102 LEU n 
1 103 ASN n 
1 104 ARG n 
1 105 THR n 
1 106 PRO n 
1 107 PHE n 
1 108 GLU n 
1 109 ILE n 
1 110 GLY n 
1 111 LEU n 
1 112 GLY n 
1 113 ALA n 
1 114 GLY n 
1 115 ALA n 
1 116 LEU n 
1 117 ILE n 
1 118 ASN n 
1 119 MET n 
1 120 VAL n 
1 121 GLN n 
1 122 LYS n 
1 123 SER n 
1 124 PRO n 
1 125 GLY n 
1 126 TRP n 
1 127 ASP n 
1 128 TRP n 
1 129 THR n 
1 130 ASP n 
1 131 TYR n 
1 132 PRO n 
1 133 PRO n 
1 134 PRO n 
1 135 PRO n 
1 136 VAL n 
1 137 LEU n 
1 138 LEU n 
1 139 ILE n 
1 140 SER n 
1 141 PRO n 
1 142 PRO n 
1 143 PRO n 
1 144 LEU n 
1 145 GLY n 
1 146 GLU n 
1 147 THR n 
1 148 ILE n 
1 149 ASP n 
1 150 PRO n 
1 151 LEU n 
1 152 ALA n 
1 153 ALA n 
1 154 PRO n 
1 155 ILE n 
1 156 PHE n 
1 157 VAL n 
1 158 ASP n 
1 159 GLY n 
1 160 LEU n 
1 161 ALA n 
1 162 LYS n 
1 163 SER n 
1 164 GLU n 
1 165 ALA n 
1 166 LEU n 
1 167 PRO n 
1 168 GLY n 
1 169 VAL n 
1 170 TYR n 
1 171 LYS n 
1 172 ALA n 
1 173 ILE n 
1 174 ALA n 
1 175 GLU n 
1 176 ALA n 
1 177 ALA n 
1 178 GLY n 
1 179 GLU n 
1 180 SER n 
1 181 PHE n 
1 182 PHE n 
1 183 ASP n 
1 184 ALA n 
1 185 GLY n 
1 186 SER n 
1 187 VAL n 
1 188 VAL n 
1 189 SER n 
1 190 THR n 
1 191 ASP n 
1 192 GLY n 
1 193 VAL n 
1 194 ASP n 
1 195 GLY n 
1 196 ILE n 
1 197 HIS n 
1 198 PHE n 
1 199 THR n 
1 200 ALA n 
1 201 GLU n 
1 202 THR n 
1 203 ASN n 
1 204 ARG n 
1 205 THR n 
1 206 LEU n 
1 207 GLY n 
1 208 ALA n 
1 209 ALA n 
1 210 VAL n 
1 211 ALA n 
1 212 GLN n 
1 213 LYS n 
1 214 VAL n 
1 215 LYS n 
1 216 THR n 
1 217 LEU n 
1 218 LEU n 
1 219 GLN n 
1 220 PRO n 
1 221 LYS n 
1 222 LEU n 
1 223 ALA n 
1 224 ALA n 
1 225 ALA n 
1 226 LEU n 
1 227 GLU n 
1 228 HIS n 
1 229 HIS n 
1 230 HIS n 
1 231 HIS n 
1 232 HIS n 
1 233 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   233 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 HBA54_08925 
_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      'Pelagibius litoralis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     374515 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?               'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ?               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?               'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?               'C6 H10 N3 O2 1' 156.162 
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 
SEP 'L-peptide linking' n PHOSPHOSERINE   PHOSPHONOSERINE 'C3 H8 N O6 P'   185.072 
SER 'L-peptide linking' y SERINE          ?               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  PHE 10  10  10  PHE PHE A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  SEP 13  13  13  SEP SEP A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  TRP 18  18  18  TRP TRP A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  PRO 26  26  26  PRO PRO A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  HIS 30  30  30  HIS HIS A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  HIS 32  32  32  HIS HIS A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  TRP 36  36  36  TRP TRP A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  HIS 83  83  83  HIS HIS A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 TRP 126 126 126 TRP TRP A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 TRP 128 128 128 TRP TRP A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 GLN 212 212 212 GLN GLN A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 HIS 229 229 ?   ?   ?   A . n 
A 1 230 HIS 230 230 ?   ?   ?   A . n 
A 1 231 HIS 231 231 ?   ?   ?   A . n 
A 1 232 HIS 232 232 ?   ?   ?   A . n 
A 1 233 HIS 233 233 ?   ?   ?   A . n 
B 1 1   GLN 1   1   1   GLN GLN B . n 
B 1 2   ASP 2   2   2   ASP ASP B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ARG 6   6   6   ARG ARG B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  PHE 10  10  10  PHE PHE B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  SEP 13  13  13  SEP SEP B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  THR 15  15  15  THR THR B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  TRP 18  18  18  TRP TRP B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  VAL 21  21  21  VAL VAL B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  PRO 26  26  26  PRO PRO B . n 
B 1 27  THR 27  27  27  THR THR B . n 
B 1 28  THR 28  28  28  THR THR B . n 
B 1 29  ARG 29  29  29  ARG ARG B . n 
B 1 30  HIS 30  30  30  HIS HIS B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  HIS 32  32  32  HIS HIS B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  TRP 36  36  36  TRP TRP B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  THR 38  38  38  THR THR B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  LEU 40  40  40  LEU LEU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  ASN 43  43  43  ASN ASN B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  ASP 46  46  46  ASP ASP B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  TYR 48  48  48  TYR TYR B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  ILE 62  62  62  ILE ILE B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  ASP 64  64  64  ASP ASP B . n 
B 1 65  PRO 65  65  65  PRO PRO B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  TYR 75  75  75  TYR TYR B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  PRO 77  77  77  PRO PRO B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  HIS 83  83  83  HIS HIS B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  THR 95  95  95  THR THR B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 ILE 117 117 117 ILE ILE B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 MET 119 119 119 MET MET B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 GLN 121 121 121 GLN GLN B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 GLY 125 125 125 GLY GLY B . n 
B 1 126 TRP 126 126 126 TRP TRP B . n 
B 1 127 ASP 127 127 127 ASP ASP B . n 
B 1 128 TRP 128 128 128 TRP TRP B . n 
B 1 129 THR 129 129 129 THR THR B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 TYR 131 131 131 TYR TYR B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 PRO 135 135 135 PRO PRO B . n 
B 1 136 VAL 136 136 136 VAL VAL B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 SER 140 140 140 SER SER B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 ILE 148 148 148 ILE ILE B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 PRO 150 150 150 PRO PRO B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 SER 163 163 163 SER SER B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 PRO 167 167 167 PRO PRO B . n 
B 1 168 GLY 168 168 168 GLY GLY B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 GLU 175 175 175 GLU GLU B . n 
B 1 176 ALA 176 176 176 ALA ALA B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 PHE 182 182 182 PHE PHE B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 GLY 192 192 192 GLY GLY B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 HIS 197 197 197 HIS HIS B . n 
B 1 198 PHE 198 198 198 PHE PHE B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 GLU 201 201 201 GLU GLU B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 GLY 207 207 207 GLY GLY B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 GLN 212 212 212 GLN GLN B . n 
B 1 213 LYS 213 213 213 LYS LYS B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 THR 216 216 216 THR THR B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 LEU 226 226 226 LEU LEU B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 HIS 228 228 228 HIS HIS B . n 
B 1 229 HIS 229 229 ?   ?   ?   B . n 
B 1 230 HIS 230 230 ?   ?   ?   B . n 
B 1 231 HIS 231 231 ?   ?   ?   B . n 
B 1 232 HIS 232 232 ?   ?   ?   B . n 
B 1 233 HIS 233 233 ?   ?   ?   B . n 
C 1 1   GLN 1   1   ?   ?   ?   C . n 
C 1 2   ASP 2   2   2   ASP ASP C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ILE 4   4   4   ILE ILE C . n 
C 1 5   LYS 5   5   5   LYS LYS C . n 
C 1 6   ARG 6   6   6   ARG ARG C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   PHE 8   8   8   PHE PHE C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  PHE 10  10  10  PHE PHE C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  ASP 12  12  12  ASP ASP C . n 
C 1 13  SEP 13  13  13  SEP SEP C . n 
C 1 14  LEU 14  14  14  LEU LEU C . n 
C 1 15  THR 15  15  15  THR THR C . n 
C 1 16  TRP 16  16  16  TRP TRP C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  TRP 18  18  18  TRP TRP C . n 
C 1 19  THR 19  19  19  THR THR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  VAL 21  21  21  VAL VAL C . n 
C 1 22  ALA 22  22  22  ALA ALA C . n 
C 1 23  PRO 23  23  23  PRO PRO C . n 
C 1 24  ILE 24  24  24  ILE ILE C . n 
C 1 25  VAL 25  25  25  VAL VAL C . n 
C 1 26  PRO 26  26  26  PRO PRO C . n 
C 1 27  THR 27  27  27  THR THR C . n 
C 1 28  THR 28  28  28  THR THR C . n 
C 1 29  ARG 29  29  29  ARG ARG C . n 
C 1 30  HIS 30  30  30  HIS HIS C . n 
C 1 31  PRO 31  31  31  PRO PRO C . n 
C 1 32  HIS 32  32  32  HIS HIS C . n 
C 1 33  ALA 33  33  33  ALA ALA C . n 
C 1 34  ASP 34  34  34  ASP ASP C . n 
C 1 35  ARG 35  35  35  ARG ARG C . n 
C 1 36  TRP 36  36  36  TRP TRP C . n 
C 1 37  THR 37  37  37  THR THR C . n 
C 1 38  THR 38  38  38  THR THR C . n 
C 1 39  VAL 39  39  39  VAL VAL C . n 
C 1 40  LEU 40  40  40  LEU LEU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  GLU 42  42  42  GLU GLU C . n 
C 1 43  ASN 43  43  43  ASN ASN C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  GLY 45  45  45  GLY GLY C . n 
C 1 46  ASP 46  46  46  ASP ASP C . n 
C 1 47  GLY 47  47  47  GLY GLY C . n 
C 1 48  TYR 48  48  48  TYR TYR C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  LEU 50  50  50  LEU LEU C . n 
C 1 51  VAL 51  51  51  VAL VAL C . n 
C 1 52  VAL 52  52  52  VAL VAL C . n 
C 1 53  ASP 53  53  53  ASP ASP C . n 
C 1 54  GLY 54  54  54  GLY GLY C . n 
C 1 55  LEU 55  55  55  LEU LEU C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  THR 59  59  59  THR THR C . n 
C 1 60  THR 60  60  60  THR THR C . n 
C 1 61  ASN 61  61  61  ASN ASN C . n 
C 1 62  ILE 62  62  62  ILE ILE C . n 
C 1 63  ASP 63  63  63  ASP ASP C . n 
C 1 64  ASP 64  64  64  ASP ASP C . n 
C 1 65  PRO 65  65  65  PRO PRO C . n 
C 1 66  ASN 66  66  66  ASN ASN C . n 
C 1 67  ASP 67  67  67  ASP ASP C . n 
C 1 68  PRO 68  68  68  PRO PRO C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  TYR 75  75  75  TYR TYR C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  PRO 77  77  77  PRO PRO C . n 
C 1 78  ALA 78  78  78  ALA ALA C . n 
C 1 79  ALA 79  79  79  ALA ALA C . n 
C 1 80  LEU 80  80  80  LEU LEU C . n 
C 1 81  ALA 81  81  81  ALA ALA C . n 
C 1 82  ALA 82  82  82  ALA ALA C . n 
C 1 83  HIS 83  83  83  HIS HIS C . n 
C 1 84  GLU 84  84  84  GLU GLU C . n 
C 1 85  PRO 85  85  85  PRO PRO C . n 
C 1 86  LEU 86  86  86  LEU LEU C . n 
C 1 87  ASP 87  87  87  ASP ASP C . n 
C 1 88  LEU 88  88  88  LEU LEU C . n 
C 1 89  VAL 89  89  89  VAL VAL C . n 
C 1 90  ILE 90  90  90  ILE ILE C . n 
C 1 91  ILE 91  91  91  ILE ILE C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  LEU 93  93  93  LEU LEU C . n 
C 1 94  GLY 94  94  94  GLY GLY C . n 
C 1 95  THR 95  95  95  THR THR C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  THR 98  98  98  THR THR C . n 
C 1 99  LYS 99  99  99  LYS LYS C . n 
C 1 100 THR 100 100 100 THR THR C . n 
C 1 101 TYR 101 101 101 TYR TYR C . n 
C 1 102 LEU 102 102 102 LEU LEU C . n 
C 1 103 ASN 103 103 103 ASN ASN C . n 
C 1 104 ARG 104 104 104 ARG ARG C . n 
C 1 105 THR 105 105 105 THR THR C . n 
C 1 106 PRO 106 106 106 PRO PRO C . n 
C 1 107 PHE 107 107 107 PHE PHE C . n 
C 1 108 GLU 108 108 108 GLU GLU C . n 
C 1 109 ILE 109 109 109 ILE ILE C . n 
C 1 110 GLY 110 110 110 GLY GLY C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 GLY 112 112 112 GLY GLY C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 ILE 117 117 117 ILE ILE C . n 
C 1 118 ASN 118 118 118 ASN ASN C . n 
C 1 119 MET 119 119 119 MET MET C . n 
C 1 120 VAL 120 120 120 VAL VAL C . n 
C 1 121 GLN 121 121 121 GLN GLN C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 PRO 124 124 124 PRO PRO C . n 
C 1 125 GLY 125 125 125 GLY GLY C . n 
C 1 126 TRP 126 126 126 TRP TRP C . n 
C 1 127 ASP 127 127 127 ASP ASP C . n 
C 1 128 TRP 128 128 128 TRP TRP C . n 
C 1 129 THR 129 129 129 THR THR C . n 
C 1 130 ASP 130 130 130 ASP ASP C . n 
C 1 131 TYR 131 131 131 TYR TYR C . n 
C 1 132 PRO 132 132 132 PRO PRO C . n 
C 1 133 PRO 133 133 133 PRO PRO C . n 
C 1 134 PRO 134 134 134 PRO PRO C . n 
C 1 135 PRO 135 135 135 PRO PRO C . n 
C 1 136 VAL 136 136 136 VAL VAL C . n 
C 1 137 LEU 137 137 137 LEU LEU C . n 
C 1 138 LEU 138 138 138 LEU LEU C . n 
C 1 139 ILE 139 139 139 ILE ILE C . n 
C 1 140 SER 140 140 140 SER SER C . n 
C 1 141 PRO 141 141 141 PRO PRO C . n 
C 1 142 PRO 142 142 142 PRO PRO C . n 
C 1 143 PRO 143 143 143 PRO PRO C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 GLY 145 145 145 GLY GLY C . n 
C 1 146 GLU 146 146 146 GLU GLU C . n 
C 1 147 THR 147 147 147 THR THR C . n 
C 1 148 ILE 148 148 148 ILE ILE C . n 
C 1 149 ASP 149 149 149 ASP ASP C . n 
C 1 150 PRO 150 150 150 PRO PRO C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 ALA 153 153 153 ALA ALA C . n 
C 1 154 PRO 154 154 154 PRO PRO C . n 
C 1 155 ILE 155 155 155 ILE ILE C . n 
C 1 156 PHE 156 156 156 PHE PHE C . n 
C 1 157 VAL 157 157 157 VAL VAL C . n 
C 1 158 ASP 158 158 158 ASP ASP C . n 
C 1 159 GLY 159 159 159 GLY GLY C . n 
C 1 160 LEU 160 160 160 LEU LEU C . n 
C 1 161 ALA 161 161 161 ALA ALA C . n 
C 1 162 LYS 162 162 162 LYS LYS C . n 
C 1 163 SER 163 163 163 SER SER C . n 
C 1 164 GLU 164 164 164 GLU GLU C . n 
C 1 165 ALA 165 165 165 ALA ALA C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 PRO 167 167 167 PRO PRO C . n 
C 1 168 GLY 168 168 168 GLY GLY C . n 
C 1 169 VAL 169 169 169 VAL VAL C . n 
C 1 170 TYR 170 170 170 TYR TYR C . n 
C 1 171 LYS 171 171 171 LYS LYS C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 ILE 173 173 173 ILE ILE C . n 
C 1 174 ALA 174 174 174 ALA ALA C . n 
C 1 175 GLU 175 175 175 GLU GLU C . n 
C 1 176 ALA 176 176 176 ALA ALA C . n 
C 1 177 ALA 177 177 177 ALA ALA C . n 
C 1 178 GLY 178 178 178 GLY GLY C . n 
C 1 179 GLU 179 179 179 GLU GLU C . n 
C 1 180 SER 180 180 180 SER SER C . n 
C 1 181 PHE 181 181 181 PHE PHE C . n 
C 1 182 PHE 182 182 182 PHE PHE C . n 
C 1 183 ASP 183 183 183 ASP ASP C . n 
C 1 184 ALA 184 184 184 ALA ALA C . n 
C 1 185 GLY 185 185 185 GLY GLY C . n 
C 1 186 SER 186 186 186 SER SER C . n 
C 1 187 VAL 187 187 187 VAL VAL C . n 
C 1 188 VAL 188 188 188 VAL VAL C . n 
C 1 189 SER 189 189 189 SER SER C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 ASP 191 191 191 ASP ASP C . n 
C 1 192 GLY 192 192 192 GLY GLY C . n 
C 1 193 VAL 193 193 193 VAL VAL C . n 
C 1 194 ASP 194 194 194 ASP ASP C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 ILE 196 196 196 ILE ILE C . n 
C 1 197 HIS 197 197 197 HIS HIS C . n 
C 1 198 PHE 198 198 198 PHE PHE C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 ALA 200 200 200 ALA ALA C . n 
C 1 201 GLU 201 201 201 GLU GLU C . n 
C 1 202 THR 202 202 202 THR THR C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 ARG 204 204 204 ARG ARG C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 LEU 206 206 206 LEU LEU C . n 
C 1 207 GLY 207 207 207 GLY GLY C . n 
C 1 208 ALA 208 208 208 ALA ALA C . n 
C 1 209 ALA 209 209 209 ALA ALA C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 ALA 211 211 211 ALA ALA C . n 
C 1 212 GLN 212 212 212 GLN GLN C . n 
C 1 213 LYS 213 213 213 LYS LYS C . n 
C 1 214 VAL 214 214 214 VAL VAL C . n 
C 1 215 LYS 215 215 215 LYS LYS C . n 
C 1 216 THR 216 216 216 THR THR C . n 
C 1 217 LEU 217 217 217 LEU LEU C . n 
C 1 218 LEU 218 218 218 LEU LEU C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 PRO 220 220 ?   ?   ?   C . n 
C 1 221 LYS 221 221 ?   ?   ?   C . n 
C 1 222 LEU 222 222 ?   ?   ?   C . n 
C 1 223 ALA 223 223 ?   ?   ?   C . n 
C 1 224 ALA 224 224 ?   ?   ?   C . n 
C 1 225 ALA 225 225 ?   ?   ?   C . n 
C 1 226 LEU 226 226 ?   ?   ?   C . n 
C 1 227 GLU 227 227 ?   ?   ?   C . n 
C 1 228 HIS 228 228 ?   ?   ?   C . n 
C 1 229 HIS 229 229 ?   ?   ?   C . n 
C 1 230 HIS 230 230 ?   ?   ?   C . n 
C 1 231 HIS 231 231 ?   ?   ?   C . n 
C 1 232 HIS 232 232 ?   ?   ?   C . n 
C 1 233 HIS 233 233 ?   ?   ?   C . n 
D 1 1   GLN 1   1   ?   ?   ?   D . n 
D 1 2   ASP 2   2   2   ASP ASP D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ILE 4   4   4   ILE ILE D . n 
D 1 5   LYS 5   5   5   LYS LYS D . n 
D 1 6   ARG 6   6   6   ARG ARG D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   PHE 8   8   8   PHE PHE D . n 
D 1 9   VAL 9   9   9   VAL VAL D . n 
D 1 10  PHE 10  10  10  PHE PHE D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  ASP 12  12  12  ASP ASP D . n 
D 1 13  SEP 13  13  13  SEP SEP D . n 
D 1 14  LEU 14  14  14  LEU LEU D . n 
D 1 15  THR 15  15  15  THR THR D . n 
D 1 16  TRP 16  16  16  TRP TRP D . n 
D 1 17  GLY 17  17  17  GLY GLY D . n 
D 1 18  TRP 18  18  18  TRP TRP D . n 
D 1 19  THR 19  19  19  THR THR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  VAL 21  21  21  VAL VAL D . n 
D 1 22  ALA 22  22  22  ALA ALA D . n 
D 1 23  PRO 23  23  23  PRO PRO D . n 
D 1 24  ILE 24  24  24  ILE ILE D . n 
D 1 25  VAL 25  25  25  VAL VAL D . n 
D 1 26  PRO 26  26  26  PRO PRO D . n 
D 1 27  THR 27  27  27  THR THR D . n 
D 1 28  THR 28  28  28  THR THR D . n 
D 1 29  ARG 29  29  29  ARG ARG D . n 
D 1 30  HIS 30  30  30  HIS HIS D . n 
D 1 31  PRO 31  31  31  PRO PRO D . n 
D 1 32  HIS 32  32  32  HIS HIS D . n 
D 1 33  ALA 33  33  33  ALA ALA D . n 
D 1 34  ASP 34  34  34  ASP ASP D . n 
D 1 35  ARG 35  35  35  ARG ARG D . n 
D 1 36  TRP 36  36  36  TRP TRP D . n 
D 1 37  THR 37  37  37  THR THR D . n 
D 1 38  THR 38  38  38  THR THR D . n 
D 1 39  VAL 39  39  39  VAL VAL D . n 
D 1 40  LEU 40  40  40  LEU LEU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  GLU 42  42  42  GLU GLU D . n 
D 1 43  ASN 43  43  43  ASN ASN D . n 
D 1 44  LEU 44  44  44  LEU LEU D . n 
D 1 45  GLY 45  45  45  GLY GLY D . n 
D 1 46  ASP 46  46  46  ASP ASP D . n 
D 1 47  GLY 47  47  47  GLY GLY D . n 
D 1 48  TYR 48  48  48  TYR TYR D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  LEU 50  50  50  LEU LEU D . n 
D 1 51  VAL 51  51  51  VAL VAL D . n 
D 1 52  VAL 52  52  52  VAL VAL D . n 
D 1 53  ASP 53  53  53  ASP ASP D . n 
D 1 54  GLY 54  54  54  GLY GLY D . n 
D 1 55  LEU 55  55  55  LEU LEU D . n 
D 1 56  SER 56  56  56  SER SER D . n 
D 1 57  GLY 57  57  57  GLY GLY D . n 
D 1 58  ARG 58  58  58  ARG ARG D . n 
D 1 59  THR 59  59  59  THR THR D . n 
D 1 60  THR 60  60  60  THR THR D . n 
D 1 61  ASN 61  61  61  ASN ASN D . n 
D 1 62  ILE 62  62  62  ILE ILE D . n 
D 1 63  ASP 63  63  63  ASP ASP D . n 
D 1 64  ASP 64  64  64  ASP ASP D . n 
D 1 65  PRO 65  65  65  PRO PRO D . n 
D 1 66  ASN 66  66  66  ASN ASN D . n 
D 1 67  ASP 67  67  67  ASP ASP D . n 
D 1 68  PRO 68  68  68  PRO PRO D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  ALA 73  73  73  ALA ALA D . n 
D 1 74  ASP 74  74  74  ASP ASP D . n 
D 1 75  TYR 75  75  75  TYR TYR D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  PRO 77  77  77  PRO PRO D . n 
D 1 78  ALA 78  78  78  ALA ALA D . n 
D 1 79  ALA 79  79  79  ALA ALA D . n 
D 1 80  LEU 80  80  80  LEU LEU D . n 
D 1 81  ALA 81  81  81  ALA ALA D . n 
D 1 82  ALA 82  82  82  ALA ALA D . n 
D 1 83  HIS 83  83  83  HIS HIS D . n 
D 1 84  GLU 84  84  84  GLU GLU D . n 
D 1 85  PRO 85  85  85  PRO PRO D . n 
D 1 86  LEU 86  86  86  LEU LEU D . n 
D 1 87  ASP 87  87  87  ASP ASP D . n 
D 1 88  LEU 88  88  88  LEU LEU D . n 
D 1 89  VAL 89  89  89  VAL VAL D . n 
D 1 90  ILE 90  90  90  ILE ILE D . n 
D 1 91  ILE 91  91  91  ILE ILE D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  LEU 93  93  93  LEU LEU D . n 
D 1 94  GLY 94  94  94  GLY GLY D . n 
D 1 95  THR 95  95  95  THR THR D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  ASP 97  97  97  ASP ASP D . n 
D 1 98  THR 98  98  98  THR THR D . n 
D 1 99  LYS 99  99  99  LYS LYS D . n 
D 1 100 THR 100 100 100 THR THR D . n 
D 1 101 TYR 101 101 101 TYR TYR D . n 
D 1 102 LEU 102 102 102 LEU LEU D . n 
D 1 103 ASN 103 103 103 ASN ASN D . n 
D 1 104 ARG 104 104 104 ARG ARG D . n 
D 1 105 THR 105 105 105 THR THR D . n 
D 1 106 PRO 106 106 106 PRO PRO D . n 
D 1 107 PHE 107 107 107 PHE PHE D . n 
D 1 108 GLU 108 108 108 GLU GLU D . n 
D 1 109 ILE 109 109 109 ILE ILE D . n 
D 1 110 GLY 110 110 110 GLY GLY D . n 
D 1 111 LEU 111 111 111 LEU LEU D . n 
D 1 112 GLY 112 112 112 GLY GLY D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ALA 115 115 115 ALA ALA D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 ILE 117 117 117 ILE ILE D . n 
D 1 118 ASN 118 118 118 ASN ASN D . n 
D 1 119 MET 119 119 119 MET MET D . n 
D 1 120 VAL 120 120 120 VAL VAL D . n 
D 1 121 GLN 121 121 121 GLN GLN D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 PRO 124 124 124 PRO PRO D . n 
D 1 125 GLY 125 125 125 GLY GLY D . n 
D 1 126 TRP 126 126 126 TRP TRP D . n 
D 1 127 ASP 127 127 127 ASP ASP D . n 
D 1 128 TRP 128 128 128 TRP TRP D . n 
D 1 129 THR 129 129 129 THR THR D . n 
D 1 130 ASP 130 130 130 ASP ASP D . n 
D 1 131 TYR 131 131 131 TYR TYR D . n 
D 1 132 PRO 132 132 132 PRO PRO D . n 
D 1 133 PRO 133 133 133 PRO PRO D . n 
D 1 134 PRO 134 134 134 PRO PRO D . n 
D 1 135 PRO 135 135 135 PRO PRO D . n 
D 1 136 VAL 136 136 136 VAL VAL D . n 
D 1 137 LEU 137 137 137 LEU LEU D . n 
D 1 138 LEU 138 138 138 LEU LEU D . n 
D 1 139 ILE 139 139 139 ILE ILE D . n 
D 1 140 SER 140 140 140 SER SER D . n 
D 1 141 PRO 141 141 141 PRO PRO D . n 
D 1 142 PRO 142 142 142 PRO PRO D . n 
D 1 143 PRO 143 143 143 PRO PRO D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 GLY 145 145 145 GLY GLY D . n 
D 1 146 GLU 146 146 146 GLU GLU D . n 
D 1 147 THR 147 147 147 THR THR D . n 
D 1 148 ILE 148 148 148 ILE ILE D . n 
D 1 149 ASP 149 149 149 ASP ASP D . n 
D 1 150 PRO 150 150 150 PRO PRO D . n 
D 1 151 LEU 151 151 151 LEU LEU D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 ALA 153 153 153 ALA ALA D . n 
D 1 154 PRO 154 154 154 PRO PRO D . n 
D 1 155 ILE 155 155 155 ILE ILE D . n 
D 1 156 PHE 156 156 156 PHE PHE D . n 
D 1 157 VAL 157 157 157 VAL VAL D . n 
D 1 158 ASP 158 158 158 ASP ASP D . n 
D 1 159 GLY 159 159 159 GLY GLY D . n 
D 1 160 LEU 160 160 160 LEU LEU D . n 
D 1 161 ALA 161 161 161 ALA ALA D . n 
D 1 162 LYS 162 162 162 LYS LYS D . n 
D 1 163 SER 163 163 163 SER SER D . n 
D 1 164 GLU 164 164 164 GLU GLU D . n 
D 1 165 ALA 165 165 165 ALA ALA D . n 
D 1 166 LEU 166 166 166 LEU LEU D . n 
D 1 167 PRO 167 167 167 PRO PRO D . n 
D 1 168 GLY 168 168 168 GLY GLY D . n 
D 1 169 VAL 169 169 169 VAL VAL D . n 
D 1 170 TYR 170 170 170 TYR TYR D . n 
D 1 171 LYS 171 171 171 LYS LYS D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 ILE 173 173 173 ILE ILE D . n 
D 1 174 ALA 174 174 174 ALA ALA D . n 
D 1 175 GLU 175 175 175 GLU GLU D . n 
D 1 176 ALA 176 176 176 ALA ALA D . n 
D 1 177 ALA 177 177 177 ALA ALA D . n 
D 1 178 GLY 178 178 178 GLY GLY D . n 
D 1 179 GLU 179 179 179 GLU GLU D . n 
D 1 180 SER 180 180 180 SER SER D . n 
D 1 181 PHE 181 181 181 PHE PHE D . n 
D 1 182 PHE 182 182 182 PHE PHE D . n 
D 1 183 ASP 183 183 183 ASP ASP D . n 
D 1 184 ALA 184 184 184 ALA ALA D . n 
D 1 185 GLY 185 185 185 GLY GLY D . n 
D 1 186 SER 186 186 186 SER SER D . n 
D 1 187 VAL 187 187 187 VAL VAL D . n 
D 1 188 VAL 188 188 188 VAL VAL D . n 
D 1 189 SER 189 189 189 SER SER D . n 
D 1 190 THR 190 190 190 THR THR D . n 
D 1 191 ASP 191 191 191 ASP ASP D . n 
D 1 192 GLY 192 192 192 GLY GLY D . n 
D 1 193 VAL 193 193 193 VAL VAL D . n 
D 1 194 ASP 194 194 194 ASP ASP D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 ILE 196 196 196 ILE ILE D . n 
D 1 197 HIS 197 197 197 HIS HIS D . n 
D 1 198 PHE 198 198 198 PHE PHE D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 ALA 200 200 200 ALA ALA D . n 
D 1 201 GLU 201 201 201 GLU GLU D . n 
D 1 202 THR 202 202 202 THR THR D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 ARG 204 204 204 ARG ARG D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 LEU 206 206 206 LEU LEU D . n 
D 1 207 GLY 207 207 207 GLY GLY D . n 
D 1 208 ALA 208 208 208 ALA ALA D . n 
D 1 209 ALA 209 209 209 ALA ALA D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 ALA 211 211 211 ALA ALA D . n 
D 1 212 GLN 212 212 212 GLN GLN D . n 
D 1 213 LYS 213 213 213 LYS LYS D . n 
D 1 214 VAL 214 214 214 VAL VAL D . n 
D 1 215 LYS 215 215 215 LYS LYS D . n 
D 1 216 THR 216 216 216 THR THR D . n 
D 1 217 LEU 217 217 217 LEU LEU D . n 
D 1 218 LEU 218 218 218 LEU LEU D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 PRO 220 220 220 PRO PRO D . n 
D 1 221 LYS 221 221 221 LYS LYS D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 ALA 223 223 223 ALA ALA D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 ALA 225 225 225 ALA ALA D . n 
D 1 226 LEU 226 226 226 LEU LEU D . n 
D 1 227 GLU 227 227 227 GLU GLU D . n 
D 1 228 HIS 228 228 228 HIS HIS D . n 
D 1 229 HIS 229 229 ?   ?   ?   D . n 
D 1 230 HIS 230 230 ?   ?   ?   D . n 
D 1 231 HIS 231 231 ?   ?   ?   D . n 
D 1 232 HIS 232 232 ?   ?   ?   D . n 
D 1 233 HIS 233 233 ?   ?   ?   D . n 
E 1 1   GLN 1   1   ?   ?   ?   E . n 
E 1 2   ASP 2   2   2   ASP ASP E . n 
E 1 3   LYS 3   3   3   LYS LYS E . n 
E 1 4   ILE 4   4   4   ILE ILE E . n 
E 1 5   LYS 5   5   5   LYS LYS E . n 
E 1 6   ARG 6   6   6   ARG ARG E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   PHE 8   8   8   PHE PHE E . n 
E 1 9   VAL 9   9   9   VAL VAL E . n 
E 1 10  PHE 10  10  10  PHE PHE E . n 
E 1 11  GLY 11  11  11  GLY GLY E . n 
E 1 12  ASP 12  12  12  ASP ASP E . n 
E 1 13  SEP 13  13  13  SEP SEP E . n 
E 1 14  LEU 14  14  14  LEU LEU E . n 
E 1 15  THR 15  15  15  THR THR E . n 
E 1 16  TRP 16  16  16  TRP TRP E . n 
E 1 17  GLY 17  17  17  GLY GLY E . n 
E 1 18  TRP 18  18  18  TRP TRP E . n 
E 1 19  THR 19  19  19  THR THR E . n 
E 1 20  PRO 20  20  20  PRO PRO E . n 
E 1 21  VAL 21  21  21  VAL VAL E . n 
E 1 22  ALA 22  22  22  ALA ALA E . n 
E 1 23  PRO 23  23  23  PRO PRO E . n 
E 1 24  ILE 24  24  24  ILE ILE E . n 
E 1 25  VAL 25  25  25  VAL VAL E . n 
E 1 26  PRO 26  26  26  PRO PRO E . n 
E 1 27  THR 27  27  27  THR THR E . n 
E 1 28  THR 28  28  28  THR THR E . n 
E 1 29  ARG 29  29  29  ARG ARG E . n 
E 1 30  HIS 30  30  30  HIS HIS E . n 
E 1 31  PRO 31  31  31  PRO PRO E . n 
E 1 32  HIS 32  32  32  HIS HIS E . n 
E 1 33  ALA 33  33  33  ALA ALA E . n 
E 1 34  ASP 34  34  34  ASP ASP E . n 
E 1 35  ARG 35  35  35  ARG ARG E . n 
E 1 36  TRP 36  36  36  TRP TRP E . n 
E 1 37  THR 37  37  37  THR THR E . n 
E 1 38  THR 38  38  38  THR THR E . n 
E 1 39  VAL 39  39  39  VAL VAL E . n 
E 1 40  LEU 40  40  40  LEU LEU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  GLU 42  42  42  GLU GLU E . n 
E 1 43  ASN 43  43  43  ASN ASN E . n 
E 1 44  LEU 44  44  44  LEU LEU E . n 
E 1 45  GLY 45  45  45  GLY GLY E . n 
E 1 46  ASP 46  46  46  ASP ASP E . n 
E 1 47  GLY 47  47  47  GLY GLY E . n 
E 1 48  TYR 48  48  48  TYR TYR E . n 
E 1 49  GLU 49  49  49  GLU GLU E . n 
E 1 50  LEU 50  50  50  LEU LEU E . n 
E 1 51  VAL 51  51  51  VAL VAL E . n 
E 1 52  VAL 52  52  52  VAL VAL E . n 
E 1 53  ASP 53  53  53  ASP ASP E . n 
E 1 54  GLY 54  54  54  GLY GLY E . n 
E 1 55  LEU 55  55  55  LEU LEU E . n 
E 1 56  SER 56  56  56  SER SER E . n 
E 1 57  GLY 57  57  57  GLY GLY E . n 
E 1 58  ARG 58  58  58  ARG ARG E . n 
E 1 59  THR 59  59  59  THR THR E . n 
E 1 60  THR 60  60  60  THR THR E . n 
E 1 61  ASN 61  61  61  ASN ASN E . n 
E 1 62  ILE 62  62  62  ILE ILE E . n 
E 1 63  ASP 63  63  63  ASP ASP E . n 
E 1 64  ASP 64  64  64  ASP ASP E . n 
E 1 65  PRO 65  65  65  PRO PRO E . n 
E 1 66  ASN 66  66  66  ASN ASN E . n 
E 1 67  ASP 67  67  67  ASP ASP E . n 
E 1 68  PRO 68  68  68  PRO PRO E . n 
E 1 69  LYS 69  69  69  LYS LYS E . n 
E 1 70  LEU 70  70  70  LEU LEU E . n 
E 1 71  ASN 71  71  71  ASN ASN E . n 
E 1 72  GLY 72  72  72  GLY GLY E . n 
E 1 73  ALA 73  73  73  ALA ALA E . n 
E 1 74  ASP 74  74  74  ASP ASP E . n 
E 1 75  TYR 75  75  75  TYR TYR E . n 
E 1 76  LEU 76  76  76  LEU LEU E . n 
E 1 77  PRO 77  77  77  PRO PRO E . n 
E 1 78  ALA 78  78  78  ALA ALA E . n 
E 1 79  ALA 79  79  79  ALA ALA E . n 
E 1 80  LEU 80  80  80  LEU LEU E . n 
E 1 81  ALA 81  81  81  ALA ALA E . n 
E 1 82  ALA 82  82  82  ALA ALA E . n 
E 1 83  HIS 83  83  83  HIS HIS E . n 
E 1 84  GLU 84  84  84  GLU GLU E . n 
E 1 85  PRO 85  85  85  PRO PRO E . n 
E 1 86  LEU 86  86  86  LEU LEU E . n 
E 1 87  ASP 87  87  87  ASP ASP E . n 
E 1 88  LEU 88  88  88  LEU LEU E . n 
E 1 89  VAL 89  89  89  VAL VAL E . n 
E 1 90  ILE 90  90  90  ILE ILE E . n 
E 1 91  ILE 91  91  91  ILE ILE E . n 
E 1 92  LEU 92  92  92  LEU LEU E . n 
E 1 93  LEU 93  93  93  LEU LEU E . n 
E 1 94  GLY 94  94  94  GLY GLY E . n 
E 1 95  THR 95  95  95  THR THR E . n 
E 1 96  ASN 96  96  96  ASN ASN E . n 
E 1 97  ASP 97  97  97  ASP ASP E . n 
E 1 98  THR 98  98  98  THR THR E . n 
E 1 99  LYS 99  99  99  LYS LYS E . n 
E 1 100 THR 100 100 100 THR THR E . n 
E 1 101 TYR 101 101 101 TYR TYR E . n 
E 1 102 LEU 102 102 102 LEU LEU E . n 
E 1 103 ASN 103 103 103 ASN ASN E . n 
E 1 104 ARG 104 104 104 ARG ARG E . n 
E 1 105 THR 105 105 105 THR THR E . n 
E 1 106 PRO 106 106 106 PRO PRO E . n 
E 1 107 PHE 107 107 107 PHE PHE E . n 
E 1 108 GLU 108 108 108 GLU GLU E . n 
E 1 109 ILE 109 109 109 ILE ILE E . n 
E 1 110 GLY 110 110 110 GLY GLY E . n 
E 1 111 LEU 111 111 111 LEU LEU E . n 
E 1 112 GLY 112 112 112 GLY GLY E . n 
E 1 113 ALA 113 113 113 ALA ALA E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 ALA 115 115 115 ALA ALA E . n 
E 1 116 LEU 116 116 116 LEU LEU E . n 
E 1 117 ILE 117 117 117 ILE ILE E . n 
E 1 118 ASN 118 118 118 ASN ASN E . n 
E 1 119 MET 119 119 119 MET MET E . n 
E 1 120 VAL 120 120 120 VAL VAL E . n 
E 1 121 GLN 121 121 121 GLN GLN E . n 
E 1 122 LYS 122 122 122 LYS LYS E . n 
E 1 123 SER 123 123 123 SER SER E . n 
E 1 124 PRO 124 124 124 PRO PRO E . n 
E 1 125 GLY 125 125 125 GLY GLY E . n 
E 1 126 TRP 126 126 126 TRP TRP E . n 
E 1 127 ASP 127 127 127 ASP ASP E . n 
E 1 128 TRP 128 128 128 TRP TRP E . n 
E 1 129 THR 129 129 129 THR THR E . n 
E 1 130 ASP 130 130 130 ASP ASP E . n 
E 1 131 TYR 131 131 131 TYR TYR E . n 
E 1 132 PRO 132 132 132 PRO PRO E . n 
E 1 133 PRO 133 133 133 PRO PRO E . n 
E 1 134 PRO 134 134 134 PRO PRO E . n 
E 1 135 PRO 135 135 135 PRO PRO E . n 
E 1 136 VAL 136 136 136 VAL VAL E . n 
E 1 137 LEU 137 137 137 LEU LEU E . n 
E 1 138 LEU 138 138 138 LEU LEU E . n 
E 1 139 ILE 139 139 139 ILE ILE E . n 
E 1 140 SER 140 140 140 SER SER E . n 
E 1 141 PRO 141 141 141 PRO PRO E . n 
E 1 142 PRO 142 142 142 PRO PRO E . n 
E 1 143 PRO 143 143 143 PRO PRO E . n 
E 1 144 LEU 144 144 144 LEU LEU E . n 
E 1 145 GLY 145 145 145 GLY GLY E . n 
E 1 146 GLU 146 146 146 GLU GLU E . n 
E 1 147 THR 147 147 147 THR THR E . n 
E 1 148 ILE 148 148 148 ILE ILE E . n 
E 1 149 ASP 149 149 149 ASP ASP E . n 
E 1 150 PRO 150 150 150 PRO PRO E . n 
E 1 151 LEU 151 151 151 LEU LEU E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 ALA 153 153 153 ALA ALA E . n 
E 1 154 PRO 154 154 154 PRO PRO E . n 
E 1 155 ILE 155 155 155 ILE ILE E . n 
E 1 156 PHE 156 156 156 PHE PHE E . n 
E 1 157 VAL 157 157 157 VAL VAL E . n 
E 1 158 ASP 158 158 158 ASP ASP E . n 
E 1 159 GLY 159 159 159 GLY GLY E . n 
E 1 160 LEU 160 160 160 LEU LEU E . n 
E 1 161 ALA 161 161 161 ALA ALA E . n 
E 1 162 LYS 162 162 162 LYS LYS E . n 
E 1 163 SER 163 163 163 SER SER E . n 
E 1 164 GLU 164 164 164 GLU GLU E . n 
E 1 165 ALA 165 165 165 ALA ALA E . n 
E 1 166 LEU 166 166 166 LEU LEU E . n 
E 1 167 PRO 167 167 167 PRO PRO E . n 
E 1 168 GLY 168 168 168 GLY GLY E . n 
E 1 169 VAL 169 169 169 VAL VAL E . n 
E 1 170 TYR 170 170 170 TYR TYR E . n 
E 1 171 LYS 171 171 171 LYS LYS E . n 
E 1 172 ALA 172 172 172 ALA ALA E . n 
E 1 173 ILE 173 173 173 ILE ILE E . n 
E 1 174 ALA 174 174 174 ALA ALA E . n 
E 1 175 GLU 175 175 175 GLU GLU E . n 
E 1 176 ALA 176 176 176 ALA ALA E . n 
E 1 177 ALA 177 177 177 ALA ALA E . n 
E 1 178 GLY 178 178 178 GLY GLY E . n 
E 1 179 GLU 179 179 179 GLU GLU E . n 
E 1 180 SER 180 180 180 SER SER E . n 
E 1 181 PHE 181 181 181 PHE PHE E . n 
E 1 182 PHE 182 182 182 PHE PHE E . n 
E 1 183 ASP 183 183 183 ASP ASP E . n 
E 1 184 ALA 184 184 184 ALA ALA E . n 
E 1 185 GLY 185 185 185 GLY GLY E . n 
E 1 186 SER 186 186 186 SER SER E . n 
E 1 187 VAL 187 187 187 VAL VAL E . n 
E 1 188 VAL 188 188 188 VAL VAL E . n 
E 1 189 SER 189 189 189 SER SER E . n 
E 1 190 THR 190 190 190 THR THR E . n 
E 1 191 ASP 191 191 191 ASP ASP E . n 
E 1 192 GLY 192 192 192 GLY GLY E . n 
E 1 193 VAL 193 193 193 VAL VAL E . n 
E 1 194 ASP 194 194 194 ASP ASP E . n 
E 1 195 GLY 195 195 195 GLY GLY E . n 
E 1 196 ILE 196 196 196 ILE ILE E . n 
E 1 197 HIS 197 197 197 HIS HIS E . n 
E 1 198 PHE 198 198 198 PHE PHE E . n 
E 1 199 THR 199 199 199 THR THR E . n 
E 1 200 ALA 200 200 200 ALA ALA E . n 
E 1 201 GLU 201 201 201 GLU GLU E . n 
E 1 202 THR 202 202 202 THR THR E . n 
E 1 203 ASN 203 203 203 ASN ASN E . n 
E 1 204 ARG 204 204 204 ARG ARG E . n 
E 1 205 THR 205 205 205 THR THR E . n 
E 1 206 LEU 206 206 206 LEU LEU E . n 
E 1 207 GLY 207 207 207 GLY GLY E . n 
E 1 208 ALA 208 208 208 ALA ALA E . n 
E 1 209 ALA 209 209 209 ALA ALA E . n 
E 1 210 VAL 210 210 210 VAL VAL E . n 
E 1 211 ALA 211 211 211 ALA ALA E . n 
E 1 212 GLN 212 212 212 GLN GLN E . n 
E 1 213 LYS 213 213 213 LYS LYS E . n 
E 1 214 VAL 214 214 214 VAL VAL E . n 
E 1 215 LYS 215 215 215 LYS LYS E . n 
E 1 216 THR 216 216 216 THR THR E . n 
E 1 217 LEU 217 217 217 LEU LEU E . n 
E 1 218 LEU 218 218 218 LEU LEU E . n 
E 1 219 GLN 219 219 219 GLN GLN E . n 
E 1 220 PRO 220 220 ?   ?   ?   E . n 
E 1 221 LYS 221 221 ?   ?   ?   E . n 
E 1 222 LEU 222 222 ?   ?   ?   E . n 
E 1 223 ALA 223 223 ?   ?   ?   E . n 
E 1 224 ALA 224 224 ?   ?   ?   E . n 
E 1 225 ALA 225 225 ?   ?   ?   E . n 
E 1 226 LEU 226 226 ?   ?   ?   E . n 
E 1 227 GLU 227 227 ?   ?   ?   E . n 
E 1 228 HIS 228 228 ?   ?   ?   E . n 
E 1 229 HIS 229 229 ?   ?   ?   E . n 
E 1 230 HIS 230 230 ?   ?   ?   E . n 
E 1 231 HIS 231 231 ?   ?   ?   E . n 
E 1 232 HIS 232 232 ?   ?   ?   E . n 
E 1 233 HIS 233 233 ?   ?   ?   E . n 
F 1 1   GLN 1   1   ?   ?   ?   F . n 
F 1 2   ASP 2   2   2   ASP ASP F . n 
F 1 3   LYS 3   3   3   LYS LYS F . n 
F 1 4   ILE 4   4   4   ILE ILE F . n 
F 1 5   LYS 5   5   5   LYS LYS F . n 
F 1 6   ARG 6   6   6   ARG ARG F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   PHE 8   8   8   PHE PHE F . n 
F 1 9   VAL 9   9   9   VAL VAL F . n 
F 1 10  PHE 10  10  10  PHE PHE F . n 
F 1 11  GLY 11  11  11  GLY GLY F . n 
F 1 12  ASP 12  12  12  ASP ASP F . n 
F 1 13  SEP 13  13  13  SEP SEP F . n 
F 1 14  LEU 14  14  14  LEU LEU F . n 
F 1 15  THR 15  15  15  THR THR F . n 
F 1 16  TRP 16  16  16  TRP TRP F . n 
F 1 17  GLY 17  17  17  GLY GLY F . n 
F 1 18  TRP 18  18  18  TRP TRP F . n 
F 1 19  THR 19  19  19  THR THR F . n 
F 1 20  PRO 20  20  20  PRO PRO F . n 
F 1 21  VAL 21  21  21  VAL VAL F . n 
F 1 22  ALA 22  22  22  ALA ALA F . n 
F 1 23  PRO 23  23  23  PRO PRO F . n 
F 1 24  ILE 24  24  24  ILE ILE F . n 
F 1 25  VAL 25  25  25  VAL VAL F . n 
F 1 26  PRO 26  26  26  PRO PRO F . n 
F 1 27  THR 27  27  27  THR THR F . n 
F 1 28  THR 28  28  28  THR THR F . n 
F 1 29  ARG 29  29  29  ARG ARG F . n 
F 1 30  HIS 30  30  30  HIS HIS F . n 
F 1 31  PRO 31  31  31  PRO PRO F . n 
F 1 32  HIS 32  32  32  HIS HIS F . n 
F 1 33  ALA 33  33  33  ALA ALA F . n 
F 1 34  ASP 34  34  34  ASP ASP F . n 
F 1 35  ARG 35  35  35  ARG ARG F . n 
F 1 36  TRP 36  36  36  TRP TRP F . n 
F 1 37  THR 37  37  37  THR THR F . n 
F 1 38  THR 38  38  38  THR THR F . n 
F 1 39  VAL 39  39  39  VAL VAL F . n 
F 1 40  LEU 40  40  40  LEU LEU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  GLU 42  42  42  GLU GLU F . n 
F 1 43  ASN 43  43  43  ASN ASN F . n 
F 1 44  LEU 44  44  44  LEU LEU F . n 
F 1 45  GLY 45  45  45  GLY GLY F . n 
F 1 46  ASP 46  46  46  ASP ASP F . n 
F 1 47  GLY 47  47  47  GLY GLY F . n 
F 1 48  TYR 48  48  48  TYR TYR F . n 
F 1 49  GLU 49  49  49  GLU GLU F . n 
F 1 50  LEU 50  50  50  LEU LEU F . n 
F 1 51  VAL 51  51  51  VAL VAL F . n 
F 1 52  VAL 52  52  52  VAL VAL F . n 
F 1 53  ASP 53  53  53  ASP ASP F . n 
F 1 54  GLY 54  54  54  GLY GLY F . n 
F 1 55  LEU 55  55  55  LEU LEU F . n 
F 1 56  SER 56  56  56  SER SER F . n 
F 1 57  GLY 57  57  57  GLY GLY F . n 
F 1 58  ARG 58  58  58  ARG ARG F . n 
F 1 59  THR 59  59  59  THR THR F . n 
F 1 60  THR 60  60  60  THR THR F . n 
F 1 61  ASN 61  61  61  ASN ASN F . n 
F 1 62  ILE 62  62  62  ILE ILE F . n 
F 1 63  ASP 63  63  63  ASP ASP F . n 
F 1 64  ASP 64  64  64  ASP ASP F . n 
F 1 65  PRO 65  65  65  PRO PRO F . n 
F 1 66  ASN 66  66  66  ASN ASN F . n 
F 1 67  ASP 67  67  67  ASP ASP F . n 
F 1 68  PRO 68  68  68  PRO PRO F . n 
F 1 69  LYS 69  69  69  LYS LYS F . n 
F 1 70  LEU 70  70  70  LEU LEU F . n 
F 1 71  ASN 71  71  71  ASN ASN F . n 
F 1 72  GLY 72  72  72  GLY GLY F . n 
F 1 73  ALA 73  73  73  ALA ALA F . n 
F 1 74  ASP 74  74  74  ASP ASP F . n 
F 1 75  TYR 75  75  75  TYR TYR F . n 
F 1 76  LEU 76  76  76  LEU LEU F . n 
F 1 77  PRO 77  77  77  PRO PRO F . n 
F 1 78  ALA 78  78  78  ALA ALA F . n 
F 1 79  ALA 79  79  79  ALA ALA F . n 
F 1 80  LEU 80  80  80  LEU LEU F . n 
F 1 81  ALA 81  81  81  ALA ALA F . n 
F 1 82  ALA 82  82  82  ALA ALA F . n 
F 1 83  HIS 83  83  83  HIS HIS F . n 
F 1 84  GLU 84  84  84  GLU GLU F . n 
F 1 85  PRO 85  85  85  PRO PRO F . n 
F 1 86  LEU 86  86  86  LEU LEU F . n 
F 1 87  ASP 87  87  87  ASP ASP F . n 
F 1 88  LEU 88  88  88  LEU LEU F . n 
F 1 89  VAL 89  89  89  VAL VAL F . n 
F 1 90  ILE 90  90  90  ILE ILE F . n 
F 1 91  ILE 91  91  91  ILE ILE F . n 
F 1 92  LEU 92  92  92  LEU LEU F . n 
F 1 93  LEU 93  93  93  LEU LEU F . n 
F 1 94  GLY 94  94  94  GLY GLY F . n 
F 1 95  THR 95  95  95  THR THR F . n 
F 1 96  ASN 96  96  96  ASN ASN F . n 
F 1 97  ASP 97  97  97  ASP ASP F . n 
F 1 98  THR 98  98  98  THR THR F . n 
F 1 99  LYS 99  99  99  LYS LYS F . n 
F 1 100 THR 100 100 100 THR THR F . n 
F 1 101 TYR 101 101 101 TYR TYR F . n 
F 1 102 LEU 102 102 102 LEU LEU F . n 
F 1 103 ASN 103 103 103 ASN ASN F . n 
F 1 104 ARG 104 104 104 ARG ARG F . n 
F 1 105 THR 105 105 105 THR THR F . n 
F 1 106 PRO 106 106 106 PRO PRO F . n 
F 1 107 PHE 107 107 107 PHE PHE F . n 
F 1 108 GLU 108 108 108 GLU GLU F . n 
F 1 109 ILE 109 109 109 ILE ILE F . n 
F 1 110 GLY 110 110 110 GLY GLY F . n 
F 1 111 LEU 111 111 111 LEU LEU F . n 
F 1 112 GLY 112 112 112 GLY GLY F . n 
F 1 113 ALA 113 113 113 ALA ALA F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 ALA 115 115 115 ALA ALA F . n 
F 1 116 LEU 116 116 116 LEU LEU F . n 
F 1 117 ILE 117 117 117 ILE ILE F . n 
F 1 118 ASN 118 118 118 ASN ASN F . n 
F 1 119 MET 119 119 119 MET MET F . n 
F 1 120 VAL 120 120 120 VAL VAL F . n 
F 1 121 GLN 121 121 121 GLN GLN F . n 
F 1 122 LYS 122 122 122 LYS LYS F . n 
F 1 123 SER 123 123 123 SER SER F . n 
F 1 124 PRO 124 124 124 PRO PRO F . n 
F 1 125 GLY 125 125 125 GLY GLY F . n 
F 1 126 TRP 126 126 126 TRP TRP F . n 
F 1 127 ASP 127 127 127 ASP ASP F . n 
F 1 128 TRP 128 128 128 TRP TRP F . n 
F 1 129 THR 129 129 129 THR THR F . n 
F 1 130 ASP 130 130 130 ASP ASP F . n 
F 1 131 TYR 131 131 131 TYR TYR F . n 
F 1 132 PRO 132 132 132 PRO PRO F . n 
F 1 133 PRO 133 133 133 PRO PRO F . n 
F 1 134 PRO 134 134 134 PRO PRO F . n 
F 1 135 PRO 135 135 135 PRO PRO F . n 
F 1 136 VAL 136 136 136 VAL VAL F . n 
F 1 137 LEU 137 137 137 LEU LEU F . n 
F 1 138 LEU 138 138 138 LEU LEU F . n 
F 1 139 ILE 139 139 139 ILE ILE F . n 
F 1 140 SER 140 140 140 SER SER F . n 
F 1 141 PRO 141 141 141 PRO PRO F . n 
F 1 142 PRO 142 142 142 PRO PRO F . n 
F 1 143 PRO 143 143 143 PRO PRO F . n 
F 1 144 LEU 144 144 144 LEU LEU F . n 
F 1 145 GLY 145 145 145 GLY GLY F . n 
F 1 146 GLU 146 146 146 GLU GLU F . n 
F 1 147 THR 147 147 147 THR THR F . n 
F 1 148 ILE 148 148 148 ILE ILE F . n 
F 1 149 ASP 149 149 149 ASP ASP F . n 
F 1 150 PRO 150 150 150 PRO PRO F . n 
F 1 151 LEU 151 151 151 LEU LEU F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 ALA 153 153 153 ALA ALA F . n 
F 1 154 PRO 154 154 154 PRO PRO F . n 
F 1 155 ILE 155 155 155 ILE ILE F . n 
F 1 156 PHE 156 156 156 PHE PHE F . n 
F 1 157 VAL 157 157 157 VAL VAL F . n 
F 1 158 ASP 158 158 158 ASP ASP F . n 
F 1 159 GLY 159 159 159 GLY GLY F . n 
F 1 160 LEU 160 160 160 LEU LEU F . n 
F 1 161 ALA 161 161 161 ALA ALA F . n 
F 1 162 LYS 162 162 162 LYS LYS F . n 
F 1 163 SER 163 163 163 SER SER F . n 
F 1 164 GLU 164 164 164 GLU GLU F . n 
F 1 165 ALA 165 165 165 ALA ALA F . n 
F 1 166 LEU 166 166 166 LEU LEU F . n 
F 1 167 PRO 167 167 167 PRO PRO F . n 
F 1 168 GLY 168 168 168 GLY GLY F . n 
F 1 169 VAL 169 169 169 VAL VAL F . n 
F 1 170 TYR 170 170 170 TYR TYR F . n 
F 1 171 LYS 171 171 171 LYS LYS F . n 
F 1 172 ALA 172 172 172 ALA ALA F . n 
F 1 173 ILE 173 173 173 ILE ILE F . n 
F 1 174 ALA 174 174 174 ALA ALA F . n 
F 1 175 GLU 175 175 175 GLU GLU F . n 
F 1 176 ALA 176 176 176 ALA ALA F . n 
F 1 177 ALA 177 177 177 ALA ALA F . n 
F 1 178 GLY 178 178 178 GLY GLY F . n 
F 1 179 GLU 179 179 179 GLU GLU F . n 
F 1 180 SER 180 180 180 SER SER F . n 
F 1 181 PHE 181 181 181 PHE PHE F . n 
F 1 182 PHE 182 182 182 PHE PHE F . n 
F 1 183 ASP 183 183 183 ASP ASP F . n 
F 1 184 ALA 184 184 184 ALA ALA F . n 
F 1 185 GLY 185 185 185 GLY GLY F . n 
F 1 186 SER 186 186 186 SER SER F . n 
F 1 187 VAL 187 187 187 VAL VAL F . n 
F 1 188 VAL 188 188 188 VAL VAL F . n 
F 1 189 SER 189 189 189 SER SER F . n 
F 1 190 THR 190 190 190 THR THR F . n 
F 1 191 ASP 191 191 191 ASP ASP F . n 
F 1 192 GLY 192 192 192 GLY GLY F . n 
F 1 193 VAL 193 193 193 VAL VAL F . n 
F 1 194 ASP 194 194 194 ASP ASP F . n 
F 1 195 GLY 195 195 195 GLY GLY F . n 
F 1 196 ILE 196 196 196 ILE ILE F . n 
F 1 197 HIS 197 197 197 HIS HIS F . n 
F 1 198 PHE 198 198 198 PHE PHE F . n 
F 1 199 THR 199 199 199 THR THR F . n 
F 1 200 ALA 200 200 200 ALA ALA F . n 
F 1 201 GLU 201 201 201 GLU GLU F . n 
F 1 202 THR 202 202 202 THR THR F . n 
F 1 203 ASN 203 203 203 ASN ASN F . n 
F 1 204 ARG 204 204 204 ARG ARG F . n 
F 1 205 THR 205 205 205 THR THR F . n 
F 1 206 LEU 206 206 206 LEU LEU F . n 
F 1 207 GLY 207 207 207 GLY GLY F . n 
F 1 208 ALA 208 208 208 ALA ALA F . n 
F 1 209 ALA 209 209 209 ALA ALA F . n 
F 1 210 VAL 210 210 210 VAL VAL F . n 
F 1 211 ALA 211 211 211 ALA ALA F . n 
F 1 212 GLN 212 212 212 GLN GLN F . n 
F 1 213 LYS 213 213 213 LYS LYS F . n 
F 1 214 VAL 214 214 214 VAL VAL F . n 
F 1 215 LYS 215 215 215 LYS LYS F . n 
F 1 216 THR 216 216 216 THR THR F . n 
F 1 217 LEU 217 217 217 LEU LEU F . n 
F 1 218 LEU 218 218 218 LEU LEU F . n 
F 1 219 GLN 219 219 219 GLN GLN F . n 
F 1 220 PRO 220 220 ?   ?   ?   F . n 
F 1 221 LYS 221 221 ?   ?   ?   F . n 
F 1 222 LEU 222 222 ?   ?   ?   F . n 
F 1 223 ALA 223 223 ?   ?   ?   F . n 
F 1 224 ALA 224 224 ?   ?   ?   F . n 
F 1 225 ALA 225 225 ?   ?   ?   F . n 
F 1 226 LEU 226 226 ?   ?   ?   F . n 
F 1 227 GLU 227 227 ?   ?   ?   F . n 
F 1 228 HIS 228 228 ?   ?   ?   F . n 
F 1 229 HIS 229 229 ?   ?   ?   F . n 
F 1 230 HIS 230 230 ?   ?   ?   F . n 
F 1 231 HIS 231 231 ?   ?   ?   F . n 
F 1 232 HIS 232 232 ?   ?   ?   F . n 
F 1 233 HIS 233 233 ?   ?   ?   F . n 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZBC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     131.750 
_cell.length_a_esd                 ? 
_cell.length_b                     165.350 
_cell.length_b_esd                 ? 
_cell.length_c                     150.460 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZBC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZBC 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.92 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '60% v/v Tacsimate, 5mM Ethyl acetate, 5mM Hydrogen peroxide' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'Bruker PHOTON II' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.45 
_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                      'SEALED TUBE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER D8 QUEST' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.45 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZBC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.97 
_reflns.d_resolution_low                               48.17 
_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                                     32663 
_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                           96.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.159 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.97 
_reflns_shell.d_res_low                                     3.13 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12145 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.418 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -1.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.95 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.05 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.992 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.902 
_refine.correlation_coeff_Fo_to_Fc_free          0.870 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZBC 
_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                            2.97 
_refine.ls_d_res_low                             48.17 
_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                     31033 
_refine.ls_number_reflns_R_free                  1626 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.37 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21033 
_refine.ls_R_factor_R_free                       0.23910 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20883 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.418 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             17.788 
_refine.overall_SU_ML                            0.316 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.97 
_refine_hist.d_res_low                        48.17 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               10071 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        10071 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.019  10347 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  9749  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.513  1.975  14211 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.806  3.000  22557 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.191  5.000  1330  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 39.723 24.937 397   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.330 15.000 1493  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 19.607 15.000 36    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.075  0.200  1648  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.021  11599 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  2049  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.282  2.376  5338  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.279  2.376  5337  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.181  3.555  6662  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.181  3.555  6663  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.217  2.472  5009  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.217  2.472  5010  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.089  3.670  7550  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.534  28.380 11342 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.534  28.383 11343 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 1  'interatomic distance' ? A 7231 ? ? 1  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 2  'interatomic distance' ? B 7231 ? ? 1  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 3  'interatomic distance' ? A 6980 ? ? 2  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 4  'interatomic distance' ? C 6980 ? ? 2  
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 5  'interatomic distance' ? A 7225 ? ? 3  
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 6  'interatomic distance' ? D 7225 ? ? 3  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 7  'interatomic distance' ? A 6974 ? ? 4  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 8  'interatomic distance' ? E 6974 ? ? 4  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 9  'interatomic distance' ? A 6994 ? ? 5  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 10 'interatomic distance' ? F 6994 ? ? 5  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 11 'interatomic distance' ? B 6977 ? ? 6  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 12 'interatomic distance' ? C 6977 ? ? 6  
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 13 'interatomic distance' ? B 7206 ? ? 7  
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 14 'interatomic distance' ? D 7206 ? ? 7  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 15 'interatomic distance' ? B 6954 ? ? 8  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 16 'interatomic distance' ? E 6954 ? ? 8  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 17 'interatomic distance' ? B 6982 ? ? 9  
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 18 'interatomic distance' ? F 6982 ? ? 9  
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 19 'interatomic distance' ? C 6976 ? ? 10 
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 20 'interatomic distance' ? D 6976 ? ? 10 
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 21 'interatomic distance' ? C 7014 ? ? 11 
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 22 'interatomic distance' ? E 7014 ? ? 11 
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 23 'interatomic distance' ? C 7005 ? ? 12 
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 24 'interatomic distance' ? F 7005 ? ? 12 
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 25 'interatomic distance' ? D 6979 ? ? 13 
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 26 'interatomic distance' ? E 6979 ? ? 13 
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 27 'interatomic distance' ? D 7010 ? ? 14 
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 28 'interatomic distance' ? F 7010 ? ? 14 
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 29 'interatomic distance' ? E 6975 ? ? 15 
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 30 'interatomic distance' ? F 6975 ? ? 15 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.970 
_refine_ls_shell.d_res_low                        3.047 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             107 
_refine_ls_shell.number_reflns_R_work             2330 
_refine_ls_shell.percent_reflns_obs               97.91 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.313 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.341 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1  ? 1  
2  ? 2  
3  ? 3  
4  ? 4  
5  ? 5  
6  ? 6  
7  ? 7  
8  ? 8  
9  ? 9  
10 ? 10 
11 ? 11 
12 ? 12 
13 ? 13 
14 ? 14 
15 ? 15 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1  ? 
2  ? 
3  ? 
4  ? 
5  ? 
6  ? 
7  ? 
8  ? 
9  ? 
10 ? 
11 ? 
12 ? 
13 ? 
14 ? 
15 ? 
# 
_struct.entry_id                     8ZBC 
_struct.title                        'An acyltransferase with selective perhydrolytic activity' 
_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        8ZBC 
_struct_keywords.text            'Perhydrolase, Hexmaer, SGNH superfamily, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 1 ? 
F N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A967CBZ5_9PROT 
_struct_ref.pdbx_db_accession          A0A967CBZ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QDKIKRVFVFGDSLTWGWTPVAPIVPTTRHPHADRWTTVLGENLGDGYELVVDGLSGRTTNIDDPNDPKLNGADYLPAAL
AAHEPLDLVIILLGTNDTKTYLNRTPFEIGLGAGALINMVQKSPGWDWTDYPPPPVLLISPPPLGETIDPLAAPIFVDGL
AKSEALPGVYKAIAEAAGESFFDAGSVVSTDGVDGIHFTAETNRTLGAAVAQKVKTLLQP
;
_struct_ref.pdbx_align_begin           32 
# 
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 8ZBC A 1 ? 220 ? A0A967CBZ5 32 ? 251 ? 1 220 
2 1 8ZBC B 1 ? 220 ? A0A967CBZ5 32 ? 251 ? 1 220 
3 1 8ZBC C 1 ? 220 ? A0A967CBZ5 32 ? 251 ? 1 220 
4 1 8ZBC D 1 ? 220 ? A0A967CBZ5 32 ? 251 ? 1 220 
5 1 8ZBC E 1 ? 220 ? A0A967CBZ5 32 ? 251 ? 1 220 
6 1 8ZBC F 1 ? 220 ? A0A967CBZ5 32 ? 251 ? 1 220 
# 
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 8ZBC LYS A 221 ? UNP A0A967CBZ5 ? ? 'expression tag' 221 1  
1 8ZBC LEU A 222 ? UNP A0A967CBZ5 ? ? 'expression tag' 222 2  
1 8ZBC ALA A 223 ? UNP A0A967CBZ5 ? ? 'expression tag' 223 3  
1 8ZBC ALA A 224 ? UNP A0A967CBZ5 ? ? 'expression tag' 224 4  
1 8ZBC ALA A 225 ? UNP A0A967CBZ5 ? ? 'expression tag' 225 5  
1 8ZBC LEU A 226 ? UNP A0A967CBZ5 ? ? 'expression tag' 226 6  
1 8ZBC GLU A 227 ? UNP A0A967CBZ5 ? ? 'expression tag' 227 7  
1 8ZBC HIS A 228 ? UNP A0A967CBZ5 ? ? 'expression tag' 228 8  
1 8ZBC HIS A 229 ? UNP A0A967CBZ5 ? ? 'expression tag' 229 9  
1 8ZBC HIS A 230 ? UNP A0A967CBZ5 ? ? 'expression tag' 230 10 
1 8ZBC HIS A 231 ? UNP A0A967CBZ5 ? ? 'expression tag' 231 11 
1 8ZBC HIS A 232 ? UNP A0A967CBZ5 ? ? 'expression tag' 232 12 
1 8ZBC HIS A 233 ? UNP A0A967CBZ5 ? ? 'expression tag' 233 13 
2 8ZBC LYS B 221 ? UNP A0A967CBZ5 ? ? 'expression tag' 221 14 
2 8ZBC LEU B 222 ? UNP A0A967CBZ5 ? ? 'expression tag' 222 15 
2 8ZBC ALA B 223 ? UNP A0A967CBZ5 ? ? 'expression tag' 223 16 
2 8ZBC ALA B 224 ? UNP A0A967CBZ5 ? ? 'expression tag' 224 17 
2 8ZBC ALA B 225 ? UNP A0A967CBZ5 ? ? 'expression tag' 225 18 
2 8ZBC LEU B 226 ? UNP A0A967CBZ5 ? ? 'expression tag' 226 19 
2 8ZBC GLU B 227 ? UNP A0A967CBZ5 ? ? 'expression tag' 227 20 
2 8ZBC HIS B 228 ? UNP A0A967CBZ5 ? ? 'expression tag' 228 21 
2 8ZBC HIS B 229 ? UNP A0A967CBZ5 ? ? 'expression tag' 229 22 
2 8ZBC HIS B 230 ? UNP A0A967CBZ5 ? ? 'expression tag' 230 23 
2 8ZBC HIS B 231 ? UNP A0A967CBZ5 ? ? 'expression tag' 231 24 
2 8ZBC HIS B 232 ? UNP A0A967CBZ5 ? ? 'expression tag' 232 25 
2 8ZBC HIS B 233 ? UNP A0A967CBZ5 ? ? 'expression tag' 233 26 
3 8ZBC LYS C 221 ? UNP A0A967CBZ5 ? ? 'expression tag' 221 27 
3 8ZBC LEU C 222 ? UNP A0A967CBZ5 ? ? 'expression tag' 222 28 
3 8ZBC ALA C 223 ? UNP A0A967CBZ5 ? ? 'expression tag' 223 29 
3 8ZBC ALA C 224 ? UNP A0A967CBZ5 ? ? 'expression tag' 224 30 
3 8ZBC ALA C 225 ? UNP A0A967CBZ5 ? ? 'expression tag' 225 31 
3 8ZBC LEU C 226 ? UNP A0A967CBZ5 ? ? 'expression tag' 226 32 
3 8ZBC GLU C 227 ? UNP A0A967CBZ5 ? ? 'expression tag' 227 33 
3 8ZBC HIS C 228 ? UNP A0A967CBZ5 ? ? 'expression tag' 228 34 
3 8ZBC HIS C 229 ? UNP A0A967CBZ5 ? ? 'expression tag' 229 35 
3 8ZBC HIS C 230 ? UNP A0A967CBZ5 ? ? 'expression tag' 230 36 
3 8ZBC HIS C 231 ? UNP A0A967CBZ5 ? ? 'expression tag' 231 37 
3 8ZBC HIS C 232 ? UNP A0A967CBZ5 ? ? 'expression tag' 232 38 
3 8ZBC HIS C 233 ? UNP A0A967CBZ5 ? ? 'expression tag' 233 39 
4 8ZBC LYS D 221 ? UNP A0A967CBZ5 ? ? 'expression tag' 221 40 
4 8ZBC LEU D 222 ? UNP A0A967CBZ5 ? ? 'expression tag' 222 41 
4 8ZBC ALA D 223 ? UNP A0A967CBZ5 ? ? 'expression tag' 223 42 
4 8ZBC ALA D 224 ? UNP A0A967CBZ5 ? ? 'expression tag' 224 43 
4 8ZBC ALA D 225 ? UNP A0A967CBZ5 ? ? 'expression tag' 225 44 
4 8ZBC LEU D 226 ? UNP A0A967CBZ5 ? ? 'expression tag' 226 45 
4 8ZBC GLU D 227 ? UNP A0A967CBZ5 ? ? 'expression tag' 227 46 
4 8ZBC HIS D 228 ? UNP A0A967CBZ5 ? ? 'expression tag' 228 47 
4 8ZBC HIS D 229 ? UNP A0A967CBZ5 ? ? 'expression tag' 229 48 
4 8ZBC HIS D 230 ? UNP A0A967CBZ5 ? ? 'expression tag' 230 49 
4 8ZBC HIS D 231 ? UNP A0A967CBZ5 ? ? 'expression tag' 231 50 
4 8ZBC HIS D 232 ? UNP A0A967CBZ5 ? ? 'expression tag' 232 51 
4 8ZBC HIS D 233 ? UNP A0A967CBZ5 ? ? 'expression tag' 233 52 
5 8ZBC LYS E 221 ? UNP A0A967CBZ5 ? ? 'expression tag' 221 53 
5 8ZBC LEU E 222 ? UNP A0A967CBZ5 ? ? 'expression tag' 222 54 
5 8ZBC ALA E 223 ? UNP A0A967CBZ5 ? ? 'expression tag' 223 55 
5 8ZBC ALA E 224 ? UNP A0A967CBZ5 ? ? 'expression tag' 224 56 
5 8ZBC ALA E 225 ? UNP A0A967CBZ5 ? ? 'expression tag' 225 57 
5 8ZBC LEU E 226 ? UNP A0A967CBZ5 ? ? 'expression tag' 226 58 
5 8ZBC GLU E 227 ? UNP A0A967CBZ5 ? ? 'expression tag' 227 59 
5 8ZBC HIS E 228 ? UNP A0A967CBZ5 ? ? 'expression tag' 228 60 
5 8ZBC HIS E 229 ? UNP A0A967CBZ5 ? ? 'expression tag' 229 61 
5 8ZBC HIS E 230 ? UNP A0A967CBZ5 ? ? 'expression tag' 230 62 
5 8ZBC HIS E 231 ? UNP A0A967CBZ5 ? ? 'expression tag' 231 63 
5 8ZBC HIS E 232 ? UNP A0A967CBZ5 ? ? 'expression tag' 232 64 
5 8ZBC HIS E 233 ? UNP A0A967CBZ5 ? ? 'expression tag' 233 65 
6 8ZBC LYS F 221 ? UNP A0A967CBZ5 ? ? 'expression tag' 221 66 
6 8ZBC LEU F 222 ? UNP A0A967CBZ5 ? ? 'expression tag' 222 67 
6 8ZBC ALA F 223 ? UNP A0A967CBZ5 ? ? 'expression tag' 223 68 
6 8ZBC ALA F 224 ? UNP A0A967CBZ5 ? ? 'expression tag' 224 69 
6 8ZBC ALA F 225 ? UNP A0A967CBZ5 ? ? 'expression tag' 225 70 
6 8ZBC LEU F 226 ? UNP A0A967CBZ5 ? ? 'expression tag' 226 71 
6 8ZBC GLU F 227 ? UNP A0A967CBZ5 ? ? 'expression tag' 227 72 
6 8ZBC HIS F 228 ? UNP A0A967CBZ5 ? ? 'expression tag' 228 73 
6 8ZBC HIS F 229 ? UNP A0A967CBZ5 ? ? 'expression tag' 229 74 
6 8ZBC HIS F 230 ? UNP A0A967CBZ5 ? ? 'expression tag' 230 75 
6 8ZBC HIS F 231 ? UNP A0A967CBZ5 ? ? 'expression tag' 231 76 
6 8ZBC HIS F 232 ? UNP A0A967CBZ5 ? ? 'expression tag' 232 77 
6 8ZBC HIS F 233 ? UNP A0A967CBZ5 ? ? 'expression tag' 233 78 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
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)' 11910 ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  48700 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 D,E,F 
1 2 B     
1 3 A,C   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z               1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000    
2 'crystal symmetry operation' 4_554 x,-y,-z-1           1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 
-1.0000000000 0.0000000000 0.0000000000  0.0000000000 0.0000000000 -1.0000000000 -150.4600000000 
3 'crystal symmetry operation' 6_554 -x+1/2,-y+1/2,z-1/2 -1.0000000000 0.0000000000 0.0000000000 65.8750000000 0.0000000000 
-1.0000000000 0.0000000000 82.6750000000 0.0000000000 0.0000000000 1.0000000000  -75.2300000000  
# 
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 ASP A 12  ? GLY A 17  ? ASP A 12  GLY A 17  1 ? 6  
HELX_P HELX_P2  AA2 PRO A 31  ? ASP A 34  ? PRO A 31  ASP A 34  5 ? 4  
HELX_P HELX_P3  AA3 ARG A 35  ? GLY A 45  ? ARG A 35  GLY A 45  1 ? 11 
HELX_P HELX_P4  AA4 ASN A 71  ? GLU A 84  ? ASN A 71  GLU A 84  1 ? 14 
HELX_P HELX_P5  AA5 THR A 95  ? ASN A 103 ? THR A 95  ASN A 103 5 ? 9  
HELX_P HELX_P6  AA6 THR A 105 ? LYS A 122 ? THR A 105 LYS A 122 1 ? 18 
HELX_P HELX_P7  AA7 ALA A 152 ? VAL A 157 ? ALA A 152 VAL A 157 5 ? 6  
HELX_P HELX_P8  AA8 ASP A 158 ? ALA A 165 ? ASP A 158 ALA A 165 1 ? 8  
HELX_P HELX_P9  AA9 ALA A 165 ? ALA A 177 ? ALA A 165 ALA A 177 1 ? 13 
HELX_P HELX_P10 AB1 GLY A 185 ? VAL A 187 ? GLY A 185 VAL A 187 5 ? 3  
HELX_P HELX_P11 AB2 THR A 199 ? GLN A 219 ? THR A 199 GLN A 219 1 ? 21 
HELX_P HELX_P12 AB3 GLN A 219 ? GLU A 227 ? GLN A 219 GLU A 227 1 ? 9  
HELX_P HELX_P13 AB4 ASP B 12  ? GLY B 17  ? ASP B 12  GLY B 17  1 ? 6  
HELX_P HELX_P14 AB5 PRO B 31  ? ASP B 34  ? PRO B 31  ASP B 34  5 ? 4  
HELX_P HELX_P15 AB6 ARG B 35  ? GLY B 45  ? ARG B 35  GLY B 45  1 ? 11 
HELX_P HELX_P16 AB7 ASN B 71  ? GLU B 84  ? ASN B 71  GLU B 84  1 ? 14 
HELX_P HELX_P17 AB8 THR B 95  ? ASN B 103 ? THR B 95  ASN B 103 5 ? 9  
HELX_P HELX_P18 AB9 THR B 105 ? LYS B 122 ? THR B 105 LYS B 122 1 ? 18 
HELX_P HELX_P19 AC1 ALA B 152 ? VAL B 157 ? ALA B 152 VAL B 157 5 ? 6  
HELX_P HELX_P20 AC2 ASP B 158 ? ALA B 165 ? ASP B 158 ALA B 165 1 ? 8  
HELX_P HELX_P21 AC3 ALA B 165 ? ALA B 177 ? ALA B 165 ALA B 177 1 ? 13 
HELX_P HELX_P22 AC4 GLY B 185 ? VAL B 187 ? GLY B 185 VAL B 187 5 ? 3  
HELX_P HELX_P23 AC5 THR B 199 ? GLN B 219 ? THR B 199 GLN B 219 1 ? 21 
HELX_P HELX_P24 AC6 GLN B 219 ? HIS B 228 ? GLN B 219 HIS B 228 1 ? 10 
HELX_P HELX_P25 AC7 ASP C 12  ? GLY C 17  ? ASP C 12  GLY C 17  1 ? 6  
HELX_P HELX_P26 AC8 PRO C 31  ? ASP C 34  ? PRO C 31  ASP C 34  5 ? 4  
HELX_P HELX_P27 AC9 ARG C 35  ? GLY C 45  ? ARG C 35  GLY C 45  1 ? 11 
HELX_P HELX_P28 AD1 ASN C 71  ? GLU C 84  ? ASN C 71  GLU C 84  1 ? 14 
HELX_P HELX_P29 AD2 THR C 95  ? ASN C 103 ? THR C 95  ASN C 103 5 ? 9  
HELX_P HELX_P30 AD3 THR C 105 ? LYS C 122 ? THR C 105 LYS C 122 1 ? 18 
HELX_P HELX_P31 AD4 ALA C 152 ? VAL C 157 ? ALA C 152 VAL C 157 5 ? 6  
HELX_P HELX_P32 AD5 ASP C 158 ? ALA C 165 ? ASP C 158 ALA C 165 1 ? 8  
HELX_P HELX_P33 AD6 ALA C 165 ? ALA C 177 ? ALA C 165 ALA C 177 1 ? 13 
HELX_P HELX_P34 AD7 GLY C 185 ? VAL C 187 ? GLY C 185 VAL C 187 5 ? 3  
HELX_P HELX_P35 AD8 THR C 199 ? GLN C 219 ? THR C 199 GLN C 219 1 ? 21 
HELX_P HELX_P36 AD9 ASP D 12  ? GLY D 17  ? ASP D 12  GLY D 17  1 ? 6  
HELX_P HELX_P37 AE1 PRO D 31  ? ASP D 34  ? PRO D 31  ASP D 34  5 ? 4  
HELX_P HELX_P38 AE2 ARG D 35  ? GLY D 45  ? ARG D 35  GLY D 45  1 ? 11 
HELX_P HELX_P39 AE3 ASN D 71  ? GLU D 84  ? ASN D 71  GLU D 84  1 ? 14 
HELX_P HELX_P40 AE4 THR D 95  ? ASN D 103 ? THR D 95  ASN D 103 5 ? 9  
HELX_P HELX_P41 AE5 THR D 105 ? LYS D 122 ? THR D 105 LYS D 122 1 ? 18 
HELX_P HELX_P42 AE6 ALA D 152 ? VAL D 157 ? ALA D 152 VAL D 157 5 ? 6  
HELX_P HELX_P43 AE7 ASP D 158 ? ALA D 165 ? ASP D 158 ALA D 165 1 ? 8  
HELX_P HELX_P44 AE8 ALA D 165 ? ALA D 177 ? ALA D 165 ALA D 177 1 ? 13 
HELX_P HELX_P45 AE9 GLY D 185 ? VAL D 187 ? GLY D 185 VAL D 187 5 ? 3  
HELX_P HELX_P46 AF1 THR D 199 ? GLN D 219 ? THR D 199 GLN D 219 1 ? 21 
HELX_P HELX_P47 AF2 GLN D 219 ? HIS D 228 ? GLN D 219 HIS D 228 1 ? 10 
HELX_P HELX_P48 AF3 ASP E 12  ? GLY E 17  ? ASP E 12  GLY E 17  1 ? 6  
HELX_P HELX_P49 AF4 PRO E 31  ? ASP E 34  ? PRO E 31  ASP E 34  5 ? 4  
HELX_P HELX_P50 AF5 ARG E 35  ? GLY E 45  ? ARG E 35  GLY E 45  1 ? 11 
HELX_P HELX_P51 AF6 ASN E 71  ? GLU E 84  ? ASN E 71  GLU E 84  1 ? 14 
HELX_P HELX_P52 AF7 THR E 95  ? ASN E 103 ? THR E 95  ASN E 103 5 ? 9  
HELX_P HELX_P53 AF8 THR E 105 ? LYS E 122 ? THR E 105 LYS E 122 1 ? 18 
HELX_P HELX_P54 AF9 ALA E 152 ? VAL E 157 ? ALA E 152 VAL E 157 5 ? 6  
HELX_P HELX_P55 AG1 ASP E 158 ? ALA E 165 ? ASP E 158 ALA E 165 1 ? 8  
HELX_P HELX_P56 AG2 ALA E 165 ? ALA E 177 ? ALA E 165 ALA E 177 1 ? 13 
HELX_P HELX_P57 AG3 GLY E 185 ? VAL E 187 ? GLY E 185 VAL E 187 5 ? 3  
HELX_P HELX_P58 AG4 THR E 199 ? GLN E 219 ? THR E 199 GLN E 219 1 ? 21 
HELX_P HELX_P59 AG5 ASP F 12  ? GLY F 17  ? ASP F 12  GLY F 17  1 ? 6  
HELX_P HELX_P60 AG6 PRO F 31  ? ASP F 34  ? PRO F 31  ASP F 34  5 ? 4  
HELX_P HELX_P61 AG7 ARG F 35  ? GLY F 45  ? ARG F 35  GLY F 45  1 ? 11 
HELX_P HELX_P62 AG8 ASN F 71  ? GLU F 84  ? ASN F 71  GLU F 84  1 ? 14 
HELX_P HELX_P63 AG9 THR F 95  ? ASN F 103 ? THR F 95  ASN F 103 5 ? 9  
HELX_P HELX_P64 AH1 THR F 105 ? LYS F 122 ? THR F 105 LYS F 122 1 ? 18 
HELX_P HELX_P65 AH2 ALA F 152 ? VAL F 157 ? ALA F 152 VAL F 157 5 ? 6  
HELX_P HELX_P66 AH3 ASP F 158 ? ALA F 165 ? ASP F 158 ALA F 165 1 ? 8  
HELX_P HELX_P67 AH4 ALA F 165 ? ALA F 177 ? ALA F 165 ALA F 177 1 ? 13 
HELX_P HELX_P68 AH5 GLY F 185 ? VAL F 187 ? GLY F 185 VAL F 187 5 ? 3  
HELX_P HELX_P69 AH6 THR F 199 ? GLN F 219 ? THR F 199 GLN F 219 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? A ASP 12 C ? ? ? 1_555 A SEP 13 N ? ? A ASP 12 A SEP 13 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale2  covale both ? A SEP 13 C ? ? ? 1_555 A LEU 14 N ? ? A SEP 13 A LEU 14 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale3  covale both ? B ASP 12 C ? ? ? 1_555 B SEP 13 N ? ? B ASP 12 B SEP 13 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale4  covale both ? B SEP 13 C ? ? ? 1_555 B LEU 14 N ? ? B SEP 13 B LEU 14 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale5  covale both ? C ASP 12 C ? ? ? 1_555 C SEP 13 N ? ? C ASP 12 C SEP 13 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale6  covale both ? C SEP 13 C ? ? ? 1_555 C LEU 14 N ? ? C SEP 13 C LEU 14 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale7  covale both ? D ASP 12 C ? ? ? 1_555 D SEP 13 N ? ? D ASP 12 D SEP 13 1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale8  covale both ? D SEP 13 C ? ? ? 1_555 D LEU 14 N ? ? D SEP 13 D LEU 14 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale9  covale both ? E ASP 12 C ? ? ? 1_555 E SEP 13 N ? ? E ASP 12 E SEP 13 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale10 covale both ? E SEP 13 C ? ? ? 1_555 E LEU 14 N ? ? E SEP 13 E LEU 14 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale11 covale both ? F ASP 12 C ? ? ? 1_555 F SEP 13 N ? ? F ASP 12 F SEP 13 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale12 covale both ? F SEP 13 C ? ? ? 1_555 F LEU 14 N ? ? F SEP 13 F LEU 14 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 SEP A 13 ? . . . . SEP A 13 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
2 SEP B 13 ? . . . . SEP B 13 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
3 SEP C 13 ? . . . . SEP C 13 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
4 SEP D 13 ? . . . . SEP D 13 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
5 SEP E 13 ? . . . . SEP E 13 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
6 SEP F 13 ? . . . . SEP F 13 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  ALA 22 A . ? ALA 22 A PRO 23 A ? PRO 23 A 1 -3.98 
2  VAL 25 A . ? VAL 25 A PRO 26 A ? PRO 26 A 1 -4.12 
3  GLU 84 A . ? GLU 84 A PRO 85 A ? PRO 85 A 1 4.60  
4  ALA 22 B . ? ALA 22 B PRO 23 B ? PRO 23 B 1 -3.81 
5  VAL 25 B . ? VAL 25 B PRO 26 B ? PRO 26 B 1 -3.53 
6  GLU 84 B . ? GLU 84 B PRO 85 B ? PRO 85 B 1 3.86  
7  ALA 22 C . ? ALA 22 C PRO 23 C ? PRO 23 C 1 -2.61 
8  VAL 25 C . ? VAL 25 C PRO 26 C ? PRO 26 C 1 -2.05 
9  GLU 84 C . ? GLU 84 C PRO 85 C ? PRO 85 C 1 4.69  
10 ALA 22 D . ? ALA 22 D PRO 23 D ? PRO 23 D 1 -2.24 
11 VAL 25 D . ? VAL 25 D PRO 26 D ? PRO 26 D 1 -2.19 
12 GLU 84 D . ? GLU 84 D PRO 85 D ? PRO 85 D 1 4.15  
13 ALA 22 E . ? ALA 22 E PRO 23 E ? PRO 23 E 1 -3.68 
14 VAL 25 E . ? VAL 25 E PRO 26 E ? PRO 26 E 1 -0.97 
15 GLU 84 E . ? GLU 84 E PRO 85 E ? PRO 85 E 1 4.17  
16 ALA 22 F . ? ALA 22 F PRO 23 F ? PRO 23 F 1 -2.75 
17 VAL 25 F . ? VAL 25 F PRO 26 F ? PRO 26 F 1 -1.15 
18 GLU 84 F . ? GLU 84 F PRO 85 F ? PRO 85 F 1 4.56  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA4 1 2 ? parallel 
AA4 2 3 ? parallel 
AA4 3 4 ? parallel 
AA4 4 5 ? parallel 
AA5 1 2 ? parallel 
AA5 2 3 ? parallel 
AA5 3 4 ? parallel 
AA5 4 5 ? parallel 
AA6 1 2 ? parallel 
AA6 2 3 ? parallel 
AA6 3 4 ? parallel 
AA6 4 5 ? 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 TYR A 48  ? GLY A 54  ? TYR A 48  GLY A 54  
AA1 2 LYS A 5   ? GLY A 11  ? LYS A 5   GLY A 11  
AA1 3 LEU A 88  ? LEU A 92  ? LEU A 88  LEU A 92  
AA1 4 VAL A 136 ? SER A 140 ? VAL A 136 SER A 140 
AA1 5 SER A 180 ? ASP A 183 ? SER A 180 ASP A 183 
AA2 1 TYR B 48  ? GLY B 54  ? TYR B 48  GLY B 54  
AA2 2 LYS B 5   ? GLY B 11  ? LYS B 5   GLY B 11  
AA2 3 LEU B 88  ? LEU B 92  ? LEU B 88  LEU B 92  
AA2 4 VAL B 136 ? SER B 140 ? VAL B 136 SER B 140 
AA2 5 SER B 180 ? ASP B 183 ? SER B 180 ASP B 183 
AA3 1 TYR C 48  ? GLY C 54  ? TYR C 48  GLY C 54  
AA3 2 LYS C 5   ? GLY C 11  ? LYS C 5   GLY C 11  
AA3 3 LEU C 88  ? LEU C 92  ? LEU C 88  LEU C 92  
AA3 4 VAL C 136 ? SER C 140 ? VAL C 136 SER C 140 
AA3 5 SER C 180 ? ASP C 183 ? SER C 180 ASP C 183 
AA4 1 TYR D 48  ? GLY D 54  ? TYR D 48  GLY D 54  
AA4 2 LYS D 5   ? GLY D 11  ? LYS D 5   GLY D 11  
AA4 3 LEU D 88  ? LEU D 92  ? LEU D 88  LEU D 92  
AA4 4 VAL D 136 ? SER D 140 ? VAL D 136 SER D 140 
AA4 5 SER D 180 ? ASP D 183 ? SER D 180 ASP D 183 
AA5 1 TYR E 48  ? GLY E 54  ? TYR E 48  GLY E 54  
AA5 2 LYS E 5   ? GLY E 11  ? LYS E 5   GLY E 11  
AA5 3 LEU E 88  ? LEU E 92  ? LEU E 88  LEU E 92  
AA5 4 VAL E 136 ? SER E 140 ? VAL E 136 SER E 140 
AA5 5 SER E 180 ? ASP E 183 ? SER E 180 ASP E 183 
AA6 1 TYR F 48  ? GLY F 54  ? TYR F 48  GLY F 54  
AA6 2 LYS F 5   ? GLY F 11  ? LYS F 5   GLY F 11  
AA6 3 LEU F 88  ? LEU F 92  ? LEU F 88  LEU F 92  
AA6 4 VAL F 136 ? SER F 140 ? VAL F 136 SER F 140 
AA6 5 SER F 180 ? ASP F 183 ? SER F 180 ASP F 183 
# 
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 ASP A 53  ? O ASP A 53  N VAL A 9   ? N VAL A 9   
AA1 2 3 N PHE A 8   ? N PHE A 8   O ILE A 90  ? O ILE A 90  
AA1 3 4 N ILE A 91  ? N ILE A 91  O ILE A 139 ? O ILE A 139 
AA1 4 5 N LEU A 138 ? N LEU A 138 O SER A 180 ? O SER A 180 
AA2 1 2 O ASP B 53  ? O ASP B 53  N VAL B 9   ? N VAL B 9   
AA2 2 3 N PHE B 8   ? N PHE B 8   O ILE B 90  ? O ILE B 90  
AA2 3 4 N ILE B 91  ? N ILE B 91  O ILE B 139 ? O ILE B 139 
AA2 4 5 N LEU B 138 ? N LEU B 138 O SER B 180 ? O SER B 180 
AA3 1 2 O ASP C 53  ? O ASP C 53  N VAL C 9   ? N VAL C 9   
AA3 2 3 N PHE C 8   ? N PHE C 8   O ILE C 90  ? O ILE C 90  
AA3 3 4 N ILE C 91  ? N ILE C 91  O ILE C 139 ? O ILE C 139 
AA3 4 5 N LEU C 138 ? N LEU C 138 O SER C 180 ? O SER C 180 
AA4 1 2 O ASP D 53  ? O ASP D 53  N VAL D 9   ? N VAL D 9   
AA4 2 3 N PHE D 8   ? N PHE D 8   O ILE D 90  ? O ILE D 90  
AA4 3 4 N ILE D 91  ? N ILE D 91  O ILE D 139 ? O ILE D 139 
AA4 4 5 N LEU D 138 ? N LEU D 138 O SER D 180 ? O SER D 180 
AA5 1 2 O ASP E 53  ? O ASP E 53  N VAL E 9   ? N VAL E 9   
AA5 2 3 N PHE E 10  ? N PHE E 10  O ILE E 90  ? O ILE E 90  
AA5 3 4 N ILE E 91  ? N ILE E 91  O ILE E 139 ? O ILE E 139 
AA5 4 5 N LEU E 138 ? N LEU E 138 O SER E 180 ? O SER E 180 
AA6 1 2 O ASP F 53  ? O ASP F 53  N VAL F 9   ? N VAL F 9   
AA6 2 3 N PHE F 8   ? N PHE F 8   O ILE F 90  ? O ILE F 90  
AA6 3 4 N ILE F 91  ? N ILE F 91  O ILE F 139 ? O ILE F 139 
AA6 4 5 N LEU F 138 ? N LEU F 138 O SER F 180 ? O SER F 180 
# 
_pdbx_entry_details.entry_id                   8ZBC 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 C A SER 123 ? ? N A PRO 124 ? ? CA A PRO 124 ? ? 133.15 119.30 13.85  1.50 Y 
2  1 C A SER 123 ? ? N A PRO 124 ? ? CD A PRO 124 ? ? 101.09 128.40 -27.31 2.10 Y 
3  1 C B SER 123 ? ? N B PRO 124 ? ? CA B PRO 124 ? ? 133.15 119.30 13.85  1.50 Y 
4  1 C B SER 123 ? ? N B PRO 124 ? ? CD B PRO 124 ? ? 101.71 128.40 -26.69 2.10 Y 
5  1 C C SER 123 ? ? N C PRO 124 ? ? CA C PRO 124 ? ? 133.04 119.30 13.74  1.50 Y 
6  1 C C SER 123 ? ? N C PRO 124 ? ? CD C PRO 124 ? ? 101.90 128.40 -26.50 2.10 Y 
7  1 C D SER 123 ? ? N D PRO 124 ? ? CA D PRO 124 ? ? 132.83 119.30 13.53  1.50 Y 
8  1 C D SER 123 ? ? N D PRO 124 ? ? CD D PRO 124 ? ? 101.31 128.40 -27.09 2.10 Y 
9  1 C E SER 123 ? ? N E PRO 124 ? ? CA E PRO 124 ? ? 133.19 119.30 13.89  1.50 Y 
10 1 C E SER 123 ? ? N E PRO 124 ? ? CD E PRO 124 ? ? 101.04 128.40 -27.36 2.10 Y 
11 1 C F SER 123 ? ? N F PRO 124 ? ? CA F PRO 124 ? ? 133.04 119.30 13.74  1.50 Y 
12 1 C F SER 123 ? ? N F PRO 124 ? ? CD F PRO 124 ? ? 101.56 128.40 -26.84 2.10 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 12  ? ? -113.24 -149.33 
2  1 ASN A 61  ? ? -152.17 26.96   
3  1 ASP A 67  ? ? -162.10 113.60  
4  1 PRO A 124 ? ? 0.48    143.10  
5  1 ASP A 158 ? ? 57.95   9.54    
6  1 ASP B 2   ? ? -39.78  113.53  
7  1 ASP B 12  ? ? -112.90 -149.33 
8  1 ASN B 61  ? ? -151.81 27.46   
9  1 ASP B 67  ? ? -163.00 115.01  
10 1 PRO B 124 ? ? 1.19    142.92  
11 1 ASP B 158 ? ? 57.65   11.88   
12 1 ASP C 12  ? ? -113.05 -149.24 
13 1 ASN C 61  ? ? -152.10 27.10   
14 1 ASP C 67  ? ? -162.26 114.56  
15 1 PRO C 124 ? ? 0.31    143.50  
16 1 ASP C 158 ? ? 58.14   10.02   
17 1 ASP D 12  ? ? -113.32 -149.48 
18 1 ASN D 61  ? ? -151.76 26.99   
19 1 ASP D 67  ? ? -162.47 114.04  
20 1 PRO D 124 ? ? 1.59    142.53  
21 1 ASP D 158 ? ? 58.07   12.40   
22 1 ASP E 12  ? ? -113.58 -149.27 
23 1 ASN E 61  ? ? -152.16 27.78   
24 1 ASP E 67  ? ? -163.07 114.83  
25 1 PRO E 124 ? ? 2.28    143.30  
26 1 ASP E 158 ? ? 57.50   11.65   
27 1 ASP F 12  ? ? -113.08 -149.12 
28 1 ASN F 61  ? ? -151.84 26.92   
29 1 ASP F 67  ? ? -162.43 113.89  
30 1 PRO F 124 ? ? 0.92    142.97  
31 1 ASP F 158 ? ? 57.68   11.60   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 SER A 123 ? ? PRO A 124 ? ? -114.43 
2 1 SER B 123 ? ? PRO B 124 ? ? -115.01 
3 1 SER C 123 ? ? PRO C 124 ? ? -114.75 
4 1 SER D 123 ? ? PRO D 124 ? ? -115.69 
5 1 SER E 123 ? ? PRO E 124 ? ? -116.14 
6 1 SER F 123 ? ? PRO F 124 ? ? -114.94 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A SEP 13 A SEP 13 ? SER 'modified residue' 
2 B SEP 13 B SEP 13 ? SER 'modified residue' 
3 C SEP 13 C SEP 13 ? SER 'modified residue' 
4 D SEP 13 D SEP 13 ? SER 'modified residue' 
5 E SEP 13 E SEP 13 ? SER 'modified residue' 
6 F SEP 13 F SEP 13 ? SER 'modified residue' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLN 1   ? A GLN 1   
2  1 Y 1 A HIS 229 ? A HIS 229 
3  1 Y 1 A HIS 230 ? A HIS 230 
4  1 Y 1 A HIS 231 ? A HIS 231 
5  1 Y 1 A HIS 232 ? A HIS 232 
6  1 Y 1 A HIS 233 ? A HIS 233 
7  1 Y 1 B HIS 229 ? B HIS 229 
8  1 Y 1 B HIS 230 ? B HIS 230 
9  1 Y 1 B HIS 231 ? B HIS 231 
10 1 Y 1 B HIS 232 ? B HIS 232 
11 1 Y 1 B HIS 233 ? B HIS 233 
12 1 Y 1 C GLN 1   ? C GLN 1   
13 1 Y 1 C PRO 220 ? C PRO 220 
14 1 Y 1 C LYS 221 ? C LYS 221 
15 1 Y 1 C LEU 222 ? C LEU 222 
16 1 Y 1 C ALA 223 ? C ALA 223 
17 1 Y 1 C ALA 224 ? C ALA 224 
18 1 Y 1 C ALA 225 ? C ALA 225 
19 1 Y 1 C LEU 226 ? C LEU 226 
20 1 Y 1 C GLU 227 ? C GLU 227 
21 1 Y 1 C HIS 228 ? C HIS 228 
22 1 Y 1 C HIS 229 ? C HIS 229 
23 1 Y 1 C HIS 230 ? C HIS 230 
24 1 Y 1 C HIS 231 ? C HIS 231 
25 1 Y 1 C HIS 232 ? C HIS 232 
26 1 Y 1 C HIS 233 ? C HIS 233 
27 1 Y 1 D GLN 1   ? D GLN 1   
28 1 Y 1 D HIS 229 ? D HIS 229 
29 1 Y 1 D HIS 230 ? D HIS 230 
30 1 Y 1 D HIS 231 ? D HIS 231 
31 1 Y 1 D HIS 232 ? D HIS 232 
32 1 Y 1 D HIS 233 ? D HIS 233 
33 1 Y 1 E GLN 1   ? E GLN 1   
34 1 Y 1 E PRO 220 ? E PRO 220 
35 1 Y 1 E LYS 221 ? E LYS 221 
36 1 Y 1 E LEU 222 ? E LEU 222 
37 1 Y 1 E ALA 223 ? E ALA 223 
38 1 Y 1 E ALA 224 ? E ALA 224 
39 1 Y 1 E ALA 225 ? E ALA 225 
40 1 Y 1 E LEU 226 ? E LEU 226 
41 1 Y 1 E GLU 227 ? E GLU 227 
42 1 Y 1 E HIS 228 ? E HIS 228 
43 1 Y 1 E HIS 229 ? E HIS 229 
44 1 Y 1 E HIS 230 ? E HIS 230 
45 1 Y 1 E HIS 231 ? E HIS 231 
46 1 Y 1 E HIS 232 ? E HIS 232 
47 1 Y 1 E HIS 233 ? E HIS 233 
48 1 Y 1 F GLN 1   ? F GLN 1   
49 1 Y 1 F PRO 220 ? F PRO 220 
50 1 Y 1 F LYS 221 ? F LYS 221 
51 1 Y 1 F LEU 222 ? F LEU 222 
52 1 Y 1 F ALA 223 ? F ALA 223 
53 1 Y 1 F ALA 224 ? F ALA 224 
54 1 Y 1 F ALA 225 ? F ALA 225 
55 1 Y 1 F LEU 226 ? F LEU 226 
56 1 Y 1 F GLU 227 ? F GLU 227 
57 1 Y 1 F HIS 228 ? F HIS 228 
58 1 Y 1 F HIS 229 ? F HIS 229 
59 1 Y 1 F HIS 230 ? F HIS 230 
60 1 Y 1 F HIS 231 ? F HIS 231 
61 1 Y 1 F HIS 232 ? F HIS 232 
62 1 Y 1 F HIS 233 ? F HIS 233 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
ILE N    N N N 144 
ILE CA   C N S 145 
ILE C    C N N 146 
ILE O    O N N 147 
ILE CB   C N S 148 
ILE CG1  C N N 149 
ILE CG2  C N N 150 
ILE CD1  C N N 151 
ILE OXT  O N N 152 
ILE H    H N N 153 
ILE H2   H N N 154 
ILE HA   H N N 155 
ILE HB   H N N 156 
ILE HG12 H N N 157 
ILE HG13 H N N 158 
ILE HG21 H N N 159 
ILE HG22 H N N 160 
ILE HG23 H N N 161 
ILE HD11 H N N 162 
ILE HD12 H N N 163 
ILE HD13 H N N 164 
ILE HXT  H N N 165 
LEU N    N N N 166 
LEU CA   C N S 167 
LEU C    C N N 168 
LEU O    O N N 169 
LEU CB   C N N 170 
LEU CG   C N N 171 
LEU CD1  C N N 172 
LEU CD2  C N N 173 
LEU OXT  O N N 174 
LEU H    H N N 175 
LEU H2   H N N 176 
LEU HA   H N N 177 
LEU HB2  H N N 178 
LEU HB3  H N N 179 
LEU HG   H N N 180 
LEU HD11 H N N 181 
LEU HD12 H N N 182 
LEU HD13 H N N 183 
LEU HD21 H N N 184 
LEU HD22 H N N 185 
LEU HD23 H N N 186 
LEU HXT  H N N 187 
LYS N    N N N 188 
LYS CA   C N S 189 
LYS C    C N N 190 
LYS O    O N N 191 
LYS CB   C N N 192 
LYS CG   C N N 193 
LYS CD   C N N 194 
LYS CE   C N N 195 
LYS NZ   N N N 196 
LYS OXT  O N N 197 
LYS H    H N N 198 
LYS H2   H N N 199 
LYS HA   H N N 200 
LYS HB2  H N N 201 
LYS HB3  H N N 202 
LYS HG2  H N N 203 
LYS HG3  H N N 204 
LYS HD2  H N N 205 
LYS HD3  H N N 206 
LYS HE2  H N N 207 
LYS HE3  H N N 208 
LYS HZ1  H N N 209 
LYS HZ2  H N N 210 
LYS HZ3  H N N 211 
LYS HXT  H N N 212 
MET N    N N N 213 
MET CA   C N S 214 
MET C    C N N 215 
MET O    O N N 216 
MET CB   C N N 217 
MET CG   C N N 218 
MET SD   S N N 219 
MET CE   C N N 220 
MET OXT  O N N 221 
MET H    H N N 222 
MET H2   H N N 223 
MET HA   H N N 224 
MET HB2  H N N 225 
MET HB3  H N N 226 
MET HG2  H N N 227 
MET HG3  H N N 228 
MET HE1  H N N 229 
MET HE2  H N N 230 
MET HE3  H N N 231 
MET HXT  H N N 232 
PHE N    N N N 233 
PHE CA   C N S 234 
PHE C    C N N 235 
PHE O    O N N 236 
PHE CB   C N N 237 
PHE CG   C Y N 238 
PHE CD1  C Y N 239 
PHE CD2  C Y N 240 
PHE CE1  C Y N 241 
PHE CE2  C Y N 242 
PHE CZ   C Y N 243 
PHE OXT  O N N 244 
PHE H    H N N 245 
PHE H2   H N N 246 
PHE HA   H N N 247 
PHE HB2  H N N 248 
PHE HB3  H N N 249 
PHE HD1  H N N 250 
PHE HD2  H N N 251 
PHE HE1  H N N 252 
PHE HE2  H N N 253 
PHE HZ   H N N 254 
PHE HXT  H N N 255 
PRO N    N N N 256 
PRO CA   C N S 257 
PRO C    C N N 258 
PRO O    O N N 259 
PRO CB   C N N 260 
PRO CG   C N N 261 
PRO CD   C N N 262 
PRO OXT  O N N 263 
PRO H    H N N 264 
PRO HA   H N N 265 
PRO HB2  H N N 266 
PRO HB3  H N N 267 
PRO HG2  H N N 268 
PRO HG3  H N N 269 
PRO HD2  H N N 270 
PRO HD3  H N N 271 
PRO HXT  H N N 272 
SEP N    N N N 273 
SEP CA   C N S 274 
SEP CB   C N N 275 
SEP OG   O N N 276 
SEP C    C N N 277 
SEP O    O N N 278 
SEP OXT  O N N 279 
SEP P    P N N 280 
SEP O1P  O N N 281 
SEP O2P  O N N 282 
SEP O3P  O N N 283 
SEP H    H N N 284 
SEP H2   H N N 285 
SEP HA   H N N 286 
SEP HB2  H N N 287 
SEP HB3  H N N 288 
SEP HXT  H N N 289 
SEP HOP2 H N N 290 
SEP HOP3 H N N 291 
SER N    N N N 292 
SER CA   C N S 293 
SER C    C N N 294 
SER O    O N N 295 
SER CB   C N N 296 
SER OG   O N N 297 
SER OXT  O N N 298 
SER H    H N N 299 
SER H2   H N N 300 
SER HA   H N N 301 
SER HB2  H N N 302 
SER HB3  H N N 303 
SER HG   H N N 304 
SER HXT  H N N 305 
THR N    N N N 306 
THR CA   C N S 307 
THR C    C N N 308 
THR O    O N N 309 
THR CB   C N R 310 
THR OG1  O N N 311 
THR CG2  C N N 312 
THR OXT  O N N 313 
THR H    H N N 314 
THR H2   H N N 315 
THR HA   H N N 316 
THR HB   H N N 317 
THR HG1  H N N 318 
THR HG21 H N N 319 
THR HG22 H N N 320 
THR HG23 H N N 321 
THR HXT  H N N 322 
TRP N    N N N 323 
TRP CA   C N S 324 
TRP C    C N N 325 
TRP O    O N N 326 
TRP CB   C N N 327 
TRP CG   C Y N 328 
TRP CD1  C Y N 329 
TRP CD2  C Y N 330 
TRP NE1  N Y N 331 
TRP CE2  C Y N 332 
TRP CE3  C Y N 333 
TRP CZ2  C Y N 334 
TRP CZ3  C Y N 335 
TRP CH2  C Y N 336 
TRP OXT  O N N 337 
TRP H    H N N 338 
TRP H2   H N N 339 
TRP HA   H N N 340 
TRP HB2  H N N 341 
TRP HB3  H N N 342 
TRP HD1  H N N 343 
TRP HE1  H N N 344 
TRP HE3  H N N 345 
TRP HZ2  H N N 346 
TRP HZ3  H N N 347 
TRP HH2  H N N 348 
TRP HXT  H N N 349 
TYR N    N N N 350 
TYR CA   C N S 351 
TYR C    C N N 352 
TYR O    O N N 353 
TYR CB   C N N 354 
TYR CG   C Y N 355 
TYR CD1  C Y N 356 
TYR CD2  C Y N 357 
TYR CE1  C Y N 358 
TYR CE2  C Y N 359 
TYR CZ   C Y N 360 
TYR OH   O N N 361 
TYR OXT  O N N 362 
TYR H    H N N 363 
TYR H2   H N N 364 
TYR HA   H N N 365 
TYR HB2  H N N 366 
TYR HB3  H N N 367 
TYR HD1  H N N 368 
TYR HD2  H N N 369 
TYR HE1  H N N 370 
TYR HE2  H N N 371 
TYR HH   H N N 372 
TYR HXT  H N N 373 
VAL N    N N N 374 
VAL CA   C N S 375 
VAL C    C N N 376 
VAL O    O N N 377 
VAL CB   C N N 378 
VAL CG1  C N N 379 
VAL CG2  C N N 380 
VAL OXT  O N N 381 
VAL H    H N N 382 
VAL H2   H N N 383 
VAL HA   H N N 384 
VAL HB   H N N 385 
VAL HG11 H N N 386 
VAL HG12 H N N 387 
VAL HG13 H N N 388 
VAL HG21 H N N 389 
VAL HG22 H N N 390 
VAL HG23 H N N 391 
VAL HXT  H N N 392 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
ILE N   CA   sing N N 137 
ILE N   H    sing N N 138 
ILE N   H2   sing N N 139 
ILE CA  C    sing N N 140 
ILE CA  CB   sing N N 141 
ILE CA  HA   sing N N 142 
ILE C   O    doub N N 143 
ILE C   OXT  sing N N 144 
ILE CB  CG1  sing N N 145 
ILE CB  CG2  sing N N 146 
ILE CB  HB   sing N N 147 
ILE CG1 CD1  sing N N 148 
ILE CG1 HG12 sing N N 149 
ILE CG1 HG13 sing N N 150 
ILE CG2 HG21 sing N N 151 
ILE CG2 HG22 sing N N 152 
ILE CG2 HG23 sing N N 153 
ILE CD1 HD11 sing N N 154 
ILE CD1 HD12 sing N N 155 
ILE CD1 HD13 sing N N 156 
ILE OXT HXT  sing N N 157 
LEU N   CA   sing N N 158 
LEU N   H    sing N N 159 
LEU N   H2   sing N N 160 
LEU CA  C    sing N N 161 
LEU CA  CB   sing N N 162 
LEU CA  HA   sing N N 163 
LEU C   O    doub N N 164 
LEU C   OXT  sing N N 165 
LEU CB  CG   sing N N 166 
LEU CB  HB2  sing N N 167 
LEU CB  HB3  sing N N 168 
LEU CG  CD1  sing N N 169 
LEU CG  CD2  sing N N 170 
LEU CG  HG   sing N N 171 
LEU CD1 HD11 sing N N 172 
LEU CD1 HD12 sing N N 173 
LEU CD1 HD13 sing N N 174 
LEU CD2 HD21 sing N N 175 
LEU CD2 HD22 sing N N 176 
LEU CD2 HD23 sing N N 177 
LEU OXT HXT  sing N N 178 
LYS N   CA   sing N N 179 
LYS N   H    sing N N 180 
LYS N   H2   sing N N 181 
LYS CA  C    sing N N 182 
LYS CA  CB   sing N N 183 
LYS CA  HA   sing N N 184 
LYS C   O    doub N N 185 
LYS C   OXT  sing N N 186 
LYS CB  CG   sing N N 187 
LYS CB  HB2  sing N N 188 
LYS CB  HB3  sing N N 189 
LYS CG  CD   sing N N 190 
LYS CG  HG2  sing N N 191 
LYS CG  HG3  sing N N 192 
LYS CD  CE   sing N N 193 
LYS CD  HD2  sing N N 194 
LYS CD  HD3  sing N N 195 
LYS CE  NZ   sing N N 196 
LYS CE  HE2  sing N N 197 
LYS CE  HE3  sing N N 198 
LYS NZ  HZ1  sing N N 199 
LYS NZ  HZ2  sing N N 200 
LYS NZ  HZ3  sing N N 201 
LYS OXT HXT  sing N N 202 
MET N   CA   sing N N 203 
MET N   H    sing N N 204 
MET N   H2   sing N N 205 
MET CA  C    sing N N 206 
MET CA  CB   sing N N 207 
MET CA  HA   sing N N 208 
MET C   O    doub N N 209 
MET C   OXT  sing N N 210 
MET CB  CG   sing N N 211 
MET CB  HB2  sing N N 212 
MET CB  HB3  sing N N 213 
MET CG  SD   sing N N 214 
MET CG  HG2  sing N N 215 
MET CG  HG3  sing N N 216 
MET SD  CE   sing N N 217 
MET CE  HE1  sing N N 218 
MET CE  HE2  sing N N 219 
MET CE  HE3  sing N N 220 
MET OXT HXT  sing N N 221 
PHE N   CA   sing N N 222 
PHE N   H    sing N N 223 
PHE N   H2   sing N N 224 
PHE CA  C    sing N N 225 
PHE CA  CB   sing N N 226 
PHE CA  HA   sing N N 227 
PHE C   O    doub N N 228 
PHE C   OXT  sing N N 229 
PHE CB  CG   sing N N 230 
PHE CB  HB2  sing N N 231 
PHE CB  HB3  sing N N 232 
PHE CG  CD1  doub Y N 233 
PHE CG  CD2  sing Y N 234 
PHE CD1 CE1  sing Y N 235 
PHE CD1 HD1  sing N N 236 
PHE CD2 CE2  doub Y N 237 
PHE CD2 HD2  sing N N 238 
PHE CE1 CZ   doub Y N 239 
PHE CE1 HE1  sing N N 240 
PHE CE2 CZ   sing Y N 241 
PHE CE2 HE2  sing N N 242 
PHE CZ  HZ   sing N N 243 
PHE OXT HXT  sing N N 244 
PRO N   CA   sing N N 245 
PRO N   CD   sing N N 246 
PRO N   H    sing N N 247 
PRO CA  C    sing N N 248 
PRO CA  CB   sing N N 249 
PRO CA  HA   sing N N 250 
PRO C   O    doub N N 251 
PRO C   OXT  sing N N 252 
PRO CB  CG   sing N N 253 
PRO CB  HB2  sing N N 254 
PRO CB  HB3  sing N N 255 
PRO CG  CD   sing N N 256 
PRO CG  HG2  sing N N 257 
PRO CG  HG3  sing N N 258 
PRO CD  HD2  sing N N 259 
PRO CD  HD3  sing N N 260 
PRO OXT HXT  sing N N 261 
SEP N   CA   sing N N 262 
SEP N   H    sing N N 263 
SEP N   H2   sing N N 264 
SEP CA  CB   sing N N 265 
SEP CA  C    sing N N 266 
SEP CA  HA   sing N N 267 
SEP CB  OG   sing N N 268 
SEP CB  HB2  sing N N 269 
SEP CB  HB3  sing N N 270 
SEP OG  P    sing N N 271 
SEP C   O    doub N N 272 
SEP C   OXT  sing N N 273 
SEP OXT HXT  sing N N 274 
SEP P   O1P  doub N N 275 
SEP P   O2P  sing N N 276 
SEP P   O3P  sing N N 277 
SEP O2P HOP2 sing N N 278 
SEP O3P HOP3 sing N N 279 
SER N   CA   sing N N 280 
SER N   H    sing N N 281 
SER N   H2   sing N N 282 
SER CA  C    sing N N 283 
SER CA  CB   sing N N 284 
SER CA  HA   sing N N 285 
SER C   O    doub N N 286 
SER C   OXT  sing N N 287 
SER CB  OG   sing N N 288 
SER CB  HB2  sing N N 289 
SER CB  HB3  sing N N 290 
SER OG  HG   sing N N 291 
SER OXT HXT  sing N N 292 
THR N   CA   sing N N 293 
THR N   H    sing N N 294 
THR N   H2   sing N N 295 
THR CA  C    sing N N 296 
THR CA  CB   sing N N 297 
THR CA  HA   sing N N 298 
THR C   O    doub N N 299 
THR C   OXT  sing N N 300 
THR CB  OG1  sing N N 301 
THR CB  CG2  sing N N 302 
THR CB  HB   sing N N 303 
THR OG1 HG1  sing N N 304 
THR CG2 HG21 sing N N 305 
THR CG2 HG22 sing N N 306 
THR CG2 HG23 sing N N 307 
THR OXT HXT  sing N N 308 
TRP N   CA   sing N N 309 
TRP N   H    sing N N 310 
TRP N   H2   sing N N 311 
TRP CA  C    sing N N 312 
TRP CA  CB   sing N N 313 
TRP CA  HA   sing N N 314 
TRP C   O    doub N N 315 
TRP C   OXT  sing N N 316 
TRP CB  CG   sing N N 317 
TRP CB  HB2  sing N N 318 
TRP CB  HB3  sing N N 319 
TRP CG  CD1  doub Y N 320 
TRP CG  CD2  sing Y N 321 
TRP CD1 NE1  sing Y N 322 
TRP CD1 HD1  sing N N 323 
TRP CD2 CE2  doub Y N 324 
TRP CD2 CE3  sing Y N 325 
TRP NE1 CE2  sing Y N 326 
TRP NE1 HE1  sing N N 327 
TRP CE2 CZ2  sing Y N 328 
TRP CE3 CZ3  doub Y N 329 
TRP CE3 HE3  sing N N 330 
TRP CZ2 CH2  doub Y N 331 
TRP CZ2 HZ2  sing N N 332 
TRP CZ3 CH2  sing Y N 333 
TRP CZ3 HZ3  sing N N 334 
TRP CH2 HH2  sing N N 335 
TRP OXT HXT  sing N N 336 
TYR N   CA   sing N N 337 
TYR N   H    sing N N 338 
TYR N   H2   sing N N 339 
TYR CA  C    sing N N 340 
TYR CA  CB   sing N N 341 
TYR CA  HA   sing N N 342 
TYR C   O    doub N N 343 
TYR C   OXT  sing N N 344 
TYR CB  CG   sing N N 345 
TYR CB  HB2  sing N N 346 
TYR CB  HB3  sing N N 347 
TYR CG  CD1  doub Y N 348 
TYR CG  CD2  sing Y N 349 
TYR CD1 CE1  sing Y N 350 
TYR CD1 HD1  sing N N 351 
TYR CD2 CE2  doub Y N 352 
TYR CD2 HD2  sing N N 353 
TYR CE1 CZ   doub Y N 354 
TYR CE1 HE1  sing N N 355 
TYR CE2 CZ   sing Y N 356 
TYR CE2 HE2  sing N N 357 
TYR CZ  OH   sing N N 358 
TYR OH  HH   sing N N 359 
TYR OXT HXT  sing N N 360 
VAL N   CA   sing N N 361 
VAL N   H    sing N N 362 
VAL N   H2   sing N N 363 
VAL CA  C    sing N N 364 
VAL CA  CB   sing N N 365 
VAL CA  HA   sing N N 366 
VAL C   O    doub N N 367 
VAL C   OXT  sing N N 368 
VAL CB  CG1  sing N N 369 
VAL CB  CG2  sing N N 370 
VAL CB  HB   sing N N 371 
VAL CG1 HG11 sing N N 372 
VAL CG1 HG12 sing N N 373 
VAL CG1 HG13 sing N N 374 
VAL CG2 HG21 sing N N 375 
VAL CG2 HG22 sing N N 376 
VAL CG2 HG23 sing N N 377 
VAL OXT HXT  sing N N 378 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5HOE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZBC 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007590 
_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]   0.006048 
_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]   0.006646 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . ASP A 1 2   ? 16.909  1.095   -31.913  1.00 58.78 ? 2   ASP A N   1 
ATOM   2     C CA  . ASP A 1 2   ? 18.228  1.530   -31.394  1.00 59.33 ? 2   ASP A CA  1 
ATOM   3     C C   . ASP A 1 2   ? 18.569  2.973   -31.756  1.00 58.72 ? 2   ASP A C   1 
ATOM   4     O O   . ASP A 1 2   ? 18.874  3.295   -32.897  1.00 63.98 ? 2   ASP A O   1 
ATOM   5     C CB  . ASP A 1 2   ? 19.347  0.596   -31.900  1.00 58.85 ? 2   ASP A CB  1 
ATOM   6     C CG  . ASP A 1 2   ? 19.540  -0.612  -31.015  1.00 55.84 ? 2   ASP A CG  1 
ATOM   7     O OD1 . ASP A 1 2   ? 19.373  -0.468  -29.784  1.00 48.22 ? 2   ASP A OD1 1 
ATOM   8     O OD2 . ASP A 1 2   ? 19.852  -1.699  -31.563  1.00 56.40 ? 2   ASP A OD2 1 
ATOM   9     N N   . LYS A 1 3   ? 18.627  3.818   -30.727  1.00 55.64 ? 3   LYS A N   1 
ATOM   10    C CA  . LYS A 1 3   ? 19.293  5.129   -30.764  1.00 55.77 ? 3   LYS A CA  1 
ATOM   11    C C   . LYS A 1 3   ? 20.678  5.045   -31.455  1.00 50.99 ? 3   LYS A C   1 
ATOM   12    O O   . LYS A 1 3   ? 21.468  4.146   -31.164  1.00 51.57 ? 3   LYS A O   1 
ATOM   13    C CB  . LYS A 1 3   ? 19.434  5.610   -29.312  1.00 60.99 ? 3   LYS A CB  1 
ATOM   14    C CG  . LYS A 1 3   ? 20.030  6.996   -29.115  1.00 65.97 ? 3   LYS A CG  1 
ATOM   15    C CD  . LYS A 1 3   ? 20.794  7.139   -27.795  1.00 68.97 ? 3   LYS A CD  1 
ATOM   16    C CE  . LYS A 1 3   ? 21.955  8.120   -27.960  1.00 73.09 ? 3   LYS A CE  1 
ATOM   17    N NZ  . LYS A 1 3   ? 22.114  9.136   -26.895  1.00 73.40 ? 3   LYS A NZ  1 
ATOM   18    N N   . ILE A 1 4   ? 20.946  5.965   -32.380  1.00 44.46 ? 4   ILE A N   1 
ATOM   19    C CA  . ILE A 1 4   ? 22.263  6.057   -33.024  1.00 42.44 ? 4   ILE A CA  1 
ATOM   20    C C   . ILE A 1 4   ? 23.238  6.713   -32.048  1.00 38.84 ? 4   ILE A C   1 
ATOM   21    O O   . ILE A 1 4   ? 22.928  7.740   -31.461  1.00 37.93 ? 4   ILE A O   1 
ATOM   22    C CB  . ILE A 1 4   ? 22.186  6.893   -34.335  1.00 43.43 ? 4   ILE A CB  1 
ATOM   23    C CG1 . ILE A 1 4   ? 21.324  6.168   -35.377  1.00 44.35 ? 4   ILE A CG1 1 
ATOM   24    C CG2 . ILE A 1 4   ? 23.566  7.193   -34.913  1.00 41.81 ? 4   ILE A CG2 1 
ATOM   25    C CD1 . ILE A 1 4   ? 20.809  7.078   -36.476  1.00 45.26 ? 4   ILE A CD1 1 
ATOM   26    N N   . LYS A 1 5   ? 24.407  6.121   -31.884  1.00 37.20 ? 5   LYS A N   1 
ATOM   27    C CA  . LYS A 1 5   ? 25.389  6.578   -30.886  1.00 34.49 ? 5   LYS A CA  1 
ATOM   28    C C   . LYS A 1 5   ? 26.306  7.681   -31.401  1.00 30.54 ? 5   LYS A C   1 
ATOM   29    O O   . LYS A 1 5   ? 26.953  7.537   -32.435  1.00 29.80 ? 5   LYS A O   1 
ATOM   30    C CB  . LYS A 1 5   ? 26.223  5.388   -30.401  1.00 36.15 ? 5   LYS A CB  1 
ATOM   31    C CG  . LYS A 1 5   ? 25.402  4.509   -29.491  1.00 38.98 ? 5   LYS A CG  1 
ATOM   32    C CD  . LYS A 1 5   ? 26.156  3.276   -29.053  1.00 40.22 ? 5   LYS A CD  1 
ATOM   33    C CE  . LYS A 1 5   ? 25.312  2.468   -28.094  1.00 43.35 ? 5   LYS A CE  1 
ATOM   34    N NZ  . LYS A 1 5   ? 25.385  1.001   -28.381  1.00 45.88 ? 5   LYS A NZ  1 
ATOM   35    N N   . ARG A 1 6   ? 26.373  8.779   -30.662  1.00 27.16 ? 6   ARG A N   1 
ATOM   36    C CA  . ARG A 1 6   ? 27.103  9.954   -31.105  1.00 25.14 ? 6   ARG A CA  1 
ATOM   37    C C   . ARG A 1 6   ? 28.484  10.050  -30.440  1.00 24.16 ? 6   ARG A C   1 
ATOM   38    O O   . ARG A 1 6   ? 28.601  10.063  -29.209  1.00 25.50 ? 6   ARG A O   1 
ATOM   39    C CB  . ARG A 1 6   ? 26.262  11.209  -30.869  1.00 25.03 ? 6   ARG A CB  1 
ATOM   40    C CG  . ARG A 1 6   ? 25.057  11.284  -31.800  1.00 24.74 ? 6   ARG A CG  1 
ATOM   41    C CD  . ARG A 1 6   ? 24.030  12.346  -31.408  1.00 24.72 ? 6   ARG A CD  1 
ATOM   42    N NE  . ARG A 1 6   ? 24.641  13.642  -31.114  1.00 25.44 ? 6   ARG A NE  1 
ATOM   43    C CZ  . ARG A 1 6   ? 25.211  14.441  -32.017  1.00 26.72 ? 6   ARG A CZ  1 
ATOM   44    N NH1 . ARG A 1 6   ? 25.261  14.089  -33.300  1.00 27.99 ? 6   ARG A NH1 1 
ATOM   45    N NH2 . ARG A 1 6   ? 25.746  15.596  -31.636  1.00 27.29 ? 6   ARG A NH2 1 
ATOM   46    N N   . VAL A 1 7   ? 29.535  10.088  -31.268  1.00 22.16 ? 7   VAL A N   1 
ATOM   47    C CA  . VAL A 1 7   ? 30.913  10.163  -30.780  1.00 20.81 ? 7   VAL A CA  1 
ATOM   48    C C   . VAL A 1 7   ? 31.592  11.475  -31.211  1.00 20.47 ? 7   VAL A C   1 
ATOM   49    O O   . VAL A 1 7   ? 31.701  11.765  -32.402  1.00 21.97 ? 7   VAL A O   1 
ATOM   50    C CB  . VAL A 1 7   ? 31.728  8.976   -31.292  1.00 19.96 ? 7   VAL A CB  1 
ATOM   51    C CG1 . VAL A 1 7   ? 33.160  9.037   -30.769  1.00 20.30 ? 7   VAL A CG1 1 
ATOM   52    C CG2 . VAL A 1 7   ? 31.069  7.677   -30.876  1.00 19.58 ? 7   VAL A CG2 1 
ATOM   53    N N   . PHE A 1 8   ? 32.045  12.256  -30.237  1.00 18.92 ? 8   PHE A N   1 
ATOM   54    C CA  . PHE A 1 8   ? 32.679  13.537  -30.498  1.00 18.51 ? 8   PHE A CA  1 
ATOM   55    C C   . PHE A 1 8   ? 34.186  13.381  -30.396  1.00 19.37 ? 8   PHE A C   1 
ATOM   56    O O   . PHE A 1 8   ? 34.686  12.892  -29.389  1.00 20.37 ? 8   PHE A O   1 
ATOM   57    C CB  . PHE A 1 8   ? 32.188  14.571  -29.494  1.00 17.76 ? 8   PHE A CB  1 
ATOM   58    C CG  . PHE A 1 8   ? 32.820  15.923  -29.649  1.00 17.98 ? 8   PHE A CG  1 
ATOM   59    C CD1 . PHE A 1 8   ? 32.872  16.550  -30.885  1.00 18.22 ? 8   PHE A CD1 1 
ATOM   60    C CD2 . PHE A 1 8   ? 33.337  16.586  -28.543  1.00 18.13 ? 8   PHE A CD2 1 
ATOM   61    C CE1 . PHE A 1 8   ? 33.456  17.787  -31.016  1.00 17.99 ? 8   PHE A CE1 1 
ATOM   62    C CE2 . PHE A 1 8   ? 33.945  17.824  -28.677  1.00 17.94 ? 8   PHE A CE2 1 
ATOM   63    C CZ  . PHE A 1 8   ? 33.995  18.423  -29.917  1.00 17.91 ? 8   PHE A CZ  1 
ATOM   64    N N   . VAL A 1 9   ? 34.901  13.783  -31.442  1.00 20.58 ? 9   VAL A N   1 
ATOM   65    C CA  . VAL A 1 9   ? 36.359  13.670  -31.485  1.00 21.81 ? 9   VAL A CA  1 
ATOM   66    C C   . VAL A 1 9   ? 36.997  15.050  -31.419  1.00 21.91 ? 9   VAL A C   1 
ATOM   67    O O   . VAL A 1 9   ? 36.773  15.901  -32.283  1.00 21.78 ? 9   VAL A O   1 
ATOM   68    C CB  . VAL A 1 9   ? 36.846  12.987  -32.774  1.00 21.99 ? 9   VAL A CB  1 
ATOM   69    C CG1 . VAL A 1 9   ? 38.329  12.685  -32.674  1.00 21.66 ? 9   VAL A CG1 1 
ATOM   70    C CG2 . VAL A 1 9   ? 36.060  11.715  -33.038  1.00 22.12 ? 9   VAL A CG2 1 
ATOM   71    N N   . PHE A 1 10  ? 37.823  15.246  -30.399  1.00 22.42 ? 10  PHE A N   1 
ATOM   72    C CA  . PHE A 1 10  ? 38.381  16.553  -30.070  1.00 22.45 ? 10  PHE A CA  1 
ATOM   73    C C   . PHE A 1 10  ? 39.888  16.437  -30.164  1.00 23.16 ? 10  PHE A C   1 
ATOM   74    O O   . PHE A 1 10  ? 40.500  15.742  -29.368  1.00 24.60 ? 10  PHE A O   1 
ATOM   75    C CB  . PHE A 1 10  ? 37.955  16.925  -28.648  1.00 20.85 ? 10  PHE A CB  1 
ATOM   76    C CG  . PHE A 1 10  ? 38.282  18.325  -28.256  1.00 20.40 ? 10  PHE A CG  1 
ATOM   77    C CD1 . PHE A 1 10  ? 37.747  19.389  -28.948  1.00 20.13 ? 10  PHE A CD1 1 
ATOM   78    C CD2 . PHE A 1 10  ? 39.108  18.584  -27.170  1.00 20.75 ? 10  PHE A CD2 1 
ATOM   79    C CE1 . PHE A 1 10  ? 38.033  20.686  -28.575  1.00 20.20 ? 10  PHE A CE1 1 
ATOM   80    C CE2 . PHE A 1 10  ? 39.407  19.883  -26.793  1.00 20.44 ? 10  PHE A CE2 1 
ATOM   81    C CZ  . PHE A 1 10  ? 38.869  20.931  -27.497  1.00 20.36 ? 10  PHE A CZ  1 
ATOM   82    N N   . GLY A 1 11  ? 40.487  17.102  -31.143  1.00 23.08 ? 11  GLY A N   1 
ATOM   83    C CA  . GLY A 1 11  ? 41.926  16.969  -31.356  1.00 23.37 ? 11  GLY A CA  1 
ATOM   84    C C   . GLY A 1 11  ? 42.597  18.172  -31.980  1.00 23.13 ? 11  GLY A C   1 
ATOM   85    O O   . GLY A 1 11  ? 42.066  19.268  -31.968  1.00 20.71 ? 11  GLY A O   1 
ATOM   86    N N   . ASP A 1 12  ? 43.777  17.927  -32.538  1.00 24.62 ? 12  ASP A N   1 
ATOM   87    C CA  . ASP A 1 12  ? 44.618  18.970  -33.099  1.00 24.30 ? 12  ASP A CA  1 
ATOM   88    C C   . ASP A 1 12  ? 44.695  18.763  -34.617  1.00 25.70 ? 12  ASP A C   1 
ATOM   89    O O   . ASP A 1 12  ? 43.746  18.266  -35.207  1.00 24.98 ? 12  ASP A O   1 
ATOM   90    C CB  . ASP A 1 12  ? 46.000  18.984  -32.397  1.00 23.73 ? 12  ASP A CB  1 
ATOM   91    C CG  . ASP A 1 12  ? 46.626  17.604  -32.262  1.00 22.59 ? 12  ASP A CG  1 
ATOM   92    O OD1 . ASP A 1 12  ? 46.296  16.718  -33.082  1.00 20.97 ? 12  ASP A OD1 1 
ATOM   93    O OD2 . ASP A 1 12  ? 47.419  17.414  -31.292  1.00 23.17 ? 12  ASP A OD2 1 
HETATM 94    N N   . SEP A 1 13  ? 45.802  19.136  -35.246  1.00 28.03 ? 13  SEP A N   1 
HETATM 95    C CA  . SEP A 1 13  ? 45.938  19.073  -36.702  1.00 30.71 ? 13  SEP A CA  1 
HETATM 96    C CB  . SEP A 1 13  ? 47.234  19.747  -37.145  1.00 37.95 ? 13  SEP A CB  1 
HETATM 97    O OG  . SEP A 1 13  ? 48.300  19.295  -36.289  1.00 52.68 ? 13  SEP A OG  1 
HETATM 98    C C   . SEP A 1 13  ? 45.921  17.645  -37.182  1.00 27.06 ? 13  SEP A C   1 
HETATM 99    O O   . SEP A 1 13  ? 45.529  17.384  -38.305  1.00 26.56 ? 13  SEP A O   1 
HETATM 100   P P   . SEP A 1 13  ? 49.276  20.045  -35.181  1.00 60.27 ? 13  SEP A P   1 
HETATM 101   O O1P . SEP A 1 13  ? 48.346  20.829  -34.271  1.00 63.81 ? 13  SEP A O1P 1 
HETATM 102   O O2P . SEP A 1 13  ? 49.795  18.813  -34.452  1.00 60.62 ? 13  SEP A O2P 1 
HETATM 103   O O3P . SEP A 1 13  ? 50.268  20.943  -35.908  1.00 54.70 ? 13  SEP A O3P 1 
ATOM   104   N N   . LEU A 1 14  ? 46.341  16.708  -36.334  1.00 24.83 ? 14  LEU A N   1 
ATOM   105   C CA  . LEU A 1 14  ? 46.256  15.278  -36.645  1.00 23.13 ? 14  LEU A CA  1 
ATOM   106   C C   . LEU A 1 14  ? 44.828  14.849  -36.940  1.00 23.38 ? 14  LEU A C   1 
ATOM   107   O O   . LEU A 1 14  ? 44.594  13.962  -37.756  1.00 24.38 ? 14  LEU A O   1 
ATOM   108   C CB  . LEU A 1 14  ? 46.791  14.419  -35.491  1.00 21.82 ? 14  LEU A CB  1 
ATOM   109   C CG  . LEU A 1 14  ? 48.262  14.542  -35.092  1.00 21.44 ? 14  LEU A CG  1 
ATOM   110   C CD1 . LEU A 1 14  ? 48.599  13.712  -33.854  1.00 21.24 ? 14  LEU A CD1 1 
ATOM   111   C CD2 . LEU A 1 14  ? 49.128  14.104  -36.240  1.00 21.50 ? 14  LEU A CD2 1 
ATOM   112   N N   . THR A 1 15  ? 43.884  15.482  -36.248  1.00 23.07 ? 15  THR A N   1 
ATOM   113   C CA  . THR A 1 15  ? 42.457  15.186  -36.361  1.00 22.38 ? 15  THR A CA  1 
ATOM   114   C C   . THR A 1 15  ? 41.763  16.083  -37.415  1.00 21.66 ? 15  THR A C   1 
ATOM   115   O O   . THR A 1 15  ? 40.788  15.671  -38.033  1.00 21.71 ? 15  THR A O   1 
ATOM   116   C CB  . THR A 1 15  ? 41.806  15.351  -34.980  1.00 22.31 ? 15  THR A CB  1 
ATOM   117   O OG1 . THR A 1 15  ? 42.490  14.505  -34.034  1.00 23.39 ? 15  THR A OG1 1 
ATOM   118   C CG2 . THR A 1 15  ? 40.331  15.011  -35.021  1.00 22.16 ? 15  THR A CG2 1 
ATOM   119   N N   . TRP A 1 16  ? 42.276  17.297  -37.620  1.00 20.70 ? 16  TRP A N   1 
ATOM   120   C CA  . TRP A 1 16  ? 41.852  18.152  -38.729  1.00 19.79 ? 16  TRP A CA  1 
ATOM   121   C C   . TRP A 1 16  ? 42.155  17.479  -40.054  1.00 19.34 ? 16  TRP A C   1 
ATOM   122   O O   . TRP A 1 16  ? 41.327  17.459  -40.956  1.00 20.02 ? 16  TRP A O   1 
ATOM   123   C CB  . TRP A 1 16  ? 42.590  19.501  -38.674  1.00 19.86 ? 16  TRP A CB  1 
ATOM   124   C CG  . TRP A 1 16  ? 42.262  20.480  -39.795  1.00 19.50 ? 16  TRP A CG  1 
ATOM   125   C CD1 . TRP A 1 16  ? 41.092  21.159  -39.972  1.00 19.29 ? 16  TRP A CD1 1 
ATOM   126   C CD2 . TRP A 1 16  ? 43.127  20.889  -40.865  1.00 18.76 ? 16  TRP A CD2 1 
ATOM   127   N NE1 . TRP A 1 16  ? 41.161  21.946  -41.099  1.00 19.14 ? 16  TRP A NE1 1 
ATOM   128   C CE2 . TRP A 1 16  ? 42.404  21.806  -41.659  1.00 18.96 ? 16  TRP A CE2 1 
ATOM   129   C CE3 . TRP A 1 16  ? 44.432  20.553  -41.242  1.00 18.13 ? 16  TRP A CE3 1 
ATOM   130   C CZ2 . TRP A 1 16  ? 42.952  22.401  -42.798  1.00 18.50 ? 16  TRP A CZ2 1 
ATOM   131   C CZ3 . TRP A 1 16  ? 44.965  21.134  -42.386  1.00 17.83 ? 16  TRP A CZ3 1 
ATOM   132   C CH2 . TRP A 1 16  ? 44.230  22.045  -43.147  1.00 18.02 ? 16  TRP A CH2 1 
ATOM   133   N N   . GLY A 1 17  ? 43.360  16.935  -40.165  1.00 18.38 ? 17  GLY A N   1 
ATOM   134   C CA  . GLY A 1 17  ? 43.814  16.241  -41.376  1.00 17.86 ? 17  GLY A CA  1 
ATOM   135   C C   . GLY A 1 17  ? 44.971  16.932  -42.058  1.00 16.82 ? 17  GLY A C   1 
ATOM   136   O O   . GLY A 1 17  ? 44.923  17.184  -43.254  1.00 16.80 ? 17  GLY A O   1 
ATOM   137   N N   . TRP A 1 18  ? 46.017  17.230  -41.304  1.00 16.81 ? 18  TRP A N   1 
ATOM   138   C CA  . TRP A 1 18  ? 47.207  17.864  -41.858  1.00 17.74 ? 18  TRP A CA  1 
ATOM   139   C C   . TRP A 1 18  ? 47.922  16.913  -42.788  1.00 18.21 ? 18  TRP A C   1 
ATOM   140   O O   . TRP A 1 18  ? 48.319  15.828  -42.368  1.00 17.94 ? 18  TRP A O   1 
ATOM   141   C CB  . TRP A 1 18  ? 48.134  18.310  -40.740  1.00 18.20 ? 18  TRP A CB  1 
ATOM   142   C CG  . TRP A 1 18  ? 49.356  19.094  -41.165  1.00 18.68 ? 18  TRP A CG  1 
ATOM   143   C CD1 . TRP A 1 18  ? 50.358  18.674  -41.999  1.00 19.70 ? 18  TRP A CD1 1 
ATOM   144   C CD2 . TRP A 1 18  ? 49.726  20.401  -40.723  1.00 18.81 ? 18  TRP A CD2 1 
ATOM   145   N NE1 . TRP A 1 18  ? 51.306  19.657  -42.120  1.00 20.12 ? 18  TRP A NE1 1 
ATOM   146   C CE2 . TRP A 1 18  ? 50.938  20.728  -41.341  1.00 19.29 ? 18  TRP A CE2 1 
ATOM   147   C CE3 . TRP A 1 18  ? 49.145  21.333  -39.861  1.00 19.14 ? 18  TRP A CE3 1 
ATOM   148   C CZ2 . TRP A 1 18  ? 51.577  21.953  -41.123  1.00 19.00 ? 18  TRP A CZ2 1 
ATOM   149   C CZ3 . TRP A 1 18  ? 49.795  22.560  -39.654  1.00 19.02 ? 18  TRP A CZ3 1 
ATOM   150   C CH2 . TRP A 1 18  ? 50.985  22.847  -40.281  1.00 18.85 ? 18  TRP A CH2 1 
ATOM   151   N N   . THR A 1 19  ? 48.086  17.330  -44.046  1.00 19.14 ? 19  THR A N   1 
ATOM   152   C CA  . THR A 1 19  ? 48.842  16.559  -45.028  1.00 19.32 ? 19  THR A CA  1 
ATOM   153   C C   . THR A 1 19  ? 50.330  16.898  -44.863  1.00 20.14 ? 19  THR A C   1 
ATOM   154   O O   . THR A 1 19  ? 50.709  18.044  -45.066  1.00 19.50 ? 19  THR A O   1 
ATOM   155   C CB  . THR A 1 19  ? 48.404  16.876  -46.474  1.00 18.55 ? 19  THR A CB  1 
ATOM   156   O OG1 . THR A 1 19  ? 47.017  16.589  -46.644  1.00 17.64 ? 19  THR A OG1 1 
ATOM   157   C CG2 . THR A 1 19  ? 49.177  16.034  -47.454  1.00 18.16 ? 19  THR A CG2 1 
ATOM   158   N N   . PRO A 1 20  ? 51.172  15.909  -44.477  1.00 21.58 ? 20  PRO A N   1 
ATOM   159   C CA  . PRO A 1 20  ? 52.595  16.168  -44.353  1.00 22.03 ? 20  PRO A CA  1 
ATOM   160   C C   . PRO A 1 20  ? 53.258  16.473  -45.702  1.00 21.74 ? 20  PRO A C   1 
ATOM   161   O O   . PRO A 1 20  ? 53.011  15.767  -46.679  1.00 19.68 ? 20  PRO A O   1 
ATOM   162   C CB  . PRO A 1 20  ? 53.156  14.863  -43.759  1.00 22.11 ? 20  PRO A CB  1 
ATOM   163   C CG  . PRO A 1 20  ? 52.144  13.816  -43.990  1.00 21.80 ? 20  PRO A CG  1 
ATOM   164   C CD  . PRO A 1 20  ? 50.832  14.532  -44.066  1.00 22.28 ? 20  PRO A CD  1 
ATOM   165   N N   . VAL A 1 21  ? 54.071  17.533  -45.731  1.00 21.73 ? 21  VAL A N   1 
ATOM   166   C CA  . VAL A 1 21  ? 54.660  18.028  -46.974  1.00 21.37 ? 21  VAL A CA  1 
ATOM   167   C C   . VAL A 1 21  ? 56.002  18.709  -46.730  1.00 21.37 ? 21  VAL A C   1 
ATOM   168   O O   . VAL A 1 21  ? 56.401  18.948  -45.588  1.00 21.86 ? 21  VAL A O   1 
ATOM   169   C CB  . VAL A 1 21  ? 53.724  19.046  -47.672  1.00 21.44 ? 21  VAL A CB  1 
ATOM   170   C CG1 . VAL A 1 21  ? 52.531  18.352  -48.293  1.00 21.33 ? 21  VAL A CG1 1 
ATOM   171   C CG2 . VAL A 1 21  ? 53.250  20.119  -46.695  1.00 22.19 ? 21  VAL A CG2 1 
ATOM   172   N N   . ALA A 1 22  ? 56.698  19.015  -47.819  1.00 21.20 ? 22  ALA A N   1 
ATOM   173   C CA  . ALA A 1 22  ? 57.960  19.721  -47.766  1.00 21.21 ? 22  ALA A CA  1 
ATOM   174   C C   . ALA A 1 22  ? 57.911  20.892  -48.755  1.00 22.48 ? 22  ALA A C   1 
ATOM   175   O O   . ALA A 1 22  ? 57.610  20.688  -49.931  1.00 22.89 ? 22  ALA A O   1 
ATOM   176   C CB  . ALA A 1 22  ? 59.080  18.770  -48.123  1.00 20.18 ? 22  ALA A CB  1 
ATOM   177   N N   . PRO A 1 23  ? 58.153  22.121  -48.292  1.00 24.51 ? 23  PRO A N   1 
ATOM   178   C CA  . PRO A 1 23  ? 58.380  22.423  -46.877  1.00 25.80 ? 23  PRO A CA  1 
ATOM   179   C C   . PRO A 1 23  ? 57.105  22.224  -46.026  1.00 26.81 ? 23  PRO A C   1 
ATOM   180   O O   . PRO A 1 23  ? 55.994  22.154  -46.569  1.00 26.23 ? 23  PRO A O   1 
ATOM   181   C CB  . PRO A 1 23  ? 58.835  23.889  -46.907  1.00 25.17 ? 23  PRO A CB  1 
ATOM   182   C CG  . PRO A 1 23  ? 58.281  24.445  -48.189  1.00 25.13 ? 23  PRO A CG  1 
ATOM   183   C CD  . PRO A 1 23  ? 57.706  23.319  -49.018  1.00 24.91 ? 23  PRO A CD  1 
ATOM   184   N N   . ILE A 1 24  ? 57.299  22.137  -44.709  1.00 28.44 ? 24  ILE A N   1 
ATOM   185   C CA  . ILE A 1 24  ? 56.227  21.778  -43.734  1.00 28.99 ? 24  ILE A CA  1 
ATOM   186   C C   . ILE A 1 24  ? 54.930  22.577  -43.919  1.00 29.75 ? 24  ILE A C   1 
ATOM   187   O O   . ILE A 1 24  ? 53.850  22.015  -43.777  1.00 31.23 ? 24  ILE A O   1 
ATOM   188   C CB  . ILE A 1 24  ? 56.708  21.895  -42.264  1.00 27.61 ? 24  ILE A CB  1 
ATOM   189   C CG1 . ILE A 1 24  ? 55.650  21.441  -41.293  1.00 27.14 ? 24  ILE A CG1 1 
ATOM   190   C CG2 . ILE A 1 24  ? 57.146  23.311  -41.909  1.00 28.61 ? 24  ILE A CG2 1 
ATOM   191   C CD1 . ILE A 1 24  ? 56.144  21.281  -39.847  1.00 28.07 ? 24  ILE A CD1 1 
ATOM   192   N N   . VAL A 1 25  ? 55.075  23.865  -44.245  1.00 29.47 ? 25  VAL A N   1 
ATOM   193   C CA  . VAL A 1 25  ? 53.981  24.782  -44.525  1.00 28.81 ? 25  VAL A CA  1 
ATOM   194   C C   . VAL A 1 25  ? 54.218  25.500  -45.865  1.00 28.69 ? 25  VAL A C   1 
ATOM   195   O O   . VAL A 1 25  ? 55.361  25.709  -46.244  1.00 28.06 ? 25  VAL A O   1 
ATOM   196   C CB  . VAL A 1 25  ? 53.778  25.843  -43.422  1.00 28.23 ? 25  VAL A CB  1 
ATOM   197   C CG1 . VAL A 1 25  ? 53.444  25.175  -42.102  1.00 27.08 ? 25  VAL A CG1 1 
ATOM   198   C CG2 . VAL A 1 25  ? 55.000  26.755  -43.289  1.00 27.42 ? 25  VAL A CG2 1 
ATOM   199   N N   . PRO A 1 26  ? 53.156  25.865  -46.586  1.00 28.54 ? 26  PRO A N   1 
ATOM   200   C CA  . PRO A 1 26  ? 51.769  25.558  -46.240  1.00 28.27 ? 26  PRO A CA  1 
ATOM   201   C C   . PRO A 1 26  ? 51.360  24.119  -46.589  1.00 27.39 ? 26  PRO A C   1 
ATOM   202   O O   . PRO A 1 26  ? 51.970  23.479  -47.450  1.00 26.38 ? 26  PRO A O   1 
ATOM   203   C CB  . PRO A 1 26  ? 50.992  26.527  -47.123  1.00 29.58 ? 26  PRO A CB  1 
ATOM   204   C CG  . PRO A 1 26  ? 51.871  26.738  -48.335  1.00 29.14 ? 26  PRO A CG  1 
ATOM   205   C CD  . PRO A 1 26  ? 53.291  26.474  -47.923  1.00 28.20 ? 26  PRO A CD  1 
ATOM   206   N N   . THR A 1 27  ? 50.328  23.638  -45.902  1.00 25.76 ? 27  THR A N   1 
ATOM   207   C CA  . THR A 1 27  ? 49.742  22.321  -46.149  1.00 24.13 ? 27  THR A CA  1 
ATOM   208   C C   . THR A 1 27  ? 48.339  22.487  -46.722  1.00 23.68 ? 27  THR A C   1 
ATOM   209   O O   . THR A 1 27  ? 47.809  23.603  -46.833  1.00 24.96 ? 27  THR A O   1 
ATOM   210   C CB  . THR A 1 27  ? 49.680  21.461  -44.858  1.00 23.43 ? 27  THR A CB  1 
ATOM   211   O OG1 . THR A 1 27  ? 49.093  20.174  -45.135  1.00 23.94 ? 27  THR A OG1 1 
ATOM   212   C CG2 . THR A 1 27  ? 48.861  22.146  -43.763  1.00 23.64 ? 27  THR A CG2 1 
ATOM   213   N N   . THR A 1 28  ? 47.749  21.369  -47.113  1.00 22.52 ? 28  THR A N   1 
ATOM   214   C CA  . THR A 1 28  ? 46.344  21.326  -47.485  1.00 22.26 ? 28  THR A CA  1 
ATOM   215   C C   . THR A 1 28  ? 45.721  20.172  -46.708  1.00 21.82 ? 28  THR A C   1 
ATOM   216   O O   . THR A 1 28  ? 46.430  19.257  -46.254  1.00 22.32 ? 28  THR A O   1 
ATOM   217   C CB  . THR A 1 28  ? 46.139  21.122  -49.003  1.00 22.53 ? 28  THR A CB  1 
ATOM   218   O OG1 . THR A 1 28  ? 46.460  19.777  -49.345  1.00 23.27 ? 28  THR A OG1 1 
ATOM   219   C CG2 . THR A 1 28  ? 47.002  22.076  -49.832  1.00 22.00 ? 28  THR A CG2 1 
ATOM   220   N N   . ARG A 1 29  ? 44.405  20.218  -46.552  1.00 21.01 ? 29  ARG A N   1 
ATOM   221   C CA  . ARG A 1 29  ? 43.700  19.244  -45.718  1.00 20.58 ? 29  ARG A CA  1 
ATOM   222   C C   . ARG A 1 29  ? 43.606  17.904  -46.417  1.00 19.93 ? 29  ARG A C   1 
ATOM   223   O O   . ARG A 1 29  ? 43.240  17.844  -47.587  1.00 19.94 ? 29  ARG A O   1 
ATOM   224   C CB  . ARG A 1 29  ? 42.288  19.742  -45.386  1.00 20.32 ? 29  ARG A CB  1 
ATOM   225   C CG  . ARG A 1 29  ? 41.879  19.460  -43.949  1.00 20.17 ? 29  ARG A CG  1 
ATOM   226   C CD  . ARG A 1 29  ? 40.496  18.870  -43.826  1.00 19.84 ? 29  ARG A CD  1 
ATOM   227   N NE  . ARG A 1 29  ? 39.459  19.816  -43.400  1.00 19.29 ? 29  ARG A NE  1 
ATOM   228   C CZ  . ARG A 1 29  ? 38.742  19.731  -42.281  1.00 18.98 ? 29  ARG A CZ  1 
ATOM   229   N NH1 . ARG A 1 29  ? 38.950  18.769  -41.400  1.00 19.14 ? 29  ARG A NH1 1 
ATOM   230   N NH2 . ARG A 1 29  ? 37.805  20.628  -42.032  1.00 19.18 ? 29  ARG A NH2 1 
ATOM   231   N N   . HIS A 1 30  ? 43.940  16.824  -45.719  1.00 20.14 ? 30  HIS A N   1 
ATOM   232   C CA  . HIS A 1 30  ? 43.722  15.491  -46.272  1.00 20.92 ? 30  HIS A CA  1 
ATOM   233   C C   . HIS A 1 30  ? 42.304  15.435  -46.846  1.00 21.44 ? 30  HIS A C   1 
ATOM   234   O O   . HIS A 1 30  ? 41.361  15.930  -46.221  1.00 20.96 ? 30  HIS A O   1 
ATOM   235   C CB  . HIS A 1 30  ? 43.842  14.401  -45.196  1.00 20.94 ? 30  HIS A CB  1 
ATOM   236   C CG  . HIS A 1 30  ? 45.238  13.928  -44.940  1.00 20.32 ? 30  HIS A CG  1 
ATOM   237   N ND1 . HIS A 1 30  ? 45.956  13.197  -45.860  1.00 19.76 ? 30  HIS A ND1 1 
ATOM   238   C CD2 . HIS A 1 30  ? 46.019  14.028  -43.841  1.00 20.01 ? 30  HIS A CD2 1 
ATOM   239   C CE1 . HIS A 1 30  ? 47.135  12.886  -45.347  1.00 20.12 ? 30  HIS A CE1 1 
ATOM   240   N NE2 . HIS A 1 30  ? 47.201  13.388  -44.126  1.00 20.00 ? 30  HIS A NE2 1 
ATOM   241   N N   . PRO A 1 31  ? 42.141  14.830  -48.030  1.00 22.28 ? 31  PRO A N   1 
ATOM   242   C CA  . PRO A 1 31  ? 40.783  14.541  -48.489  1.00 22.28 ? 31  PRO A CA  1 
ATOM   243   C C   . PRO A 1 31  ? 40.004  13.792  -47.426  1.00 22.12 ? 31  PRO A C   1 
ATOM   244   O O   . PRO A 1 31  ? 40.588  12.965  -46.713  1.00 22.83 ? 31  PRO A O   1 
ATOM   245   C CB  . PRO A 1 31  ? 41.005  13.635  -49.710  1.00 22.66 ? 31  PRO A CB  1 
ATOM   246   C CG  . PRO A 1 31  ? 42.401  13.919  -50.170  1.00 22.86 ? 31  PRO A CG  1 
ATOM   247   C CD  . PRO A 1 31  ? 43.181  14.370  -48.976  1.00 22.45 ? 31  PRO A CD  1 
ATOM   248   N N   . HIS A 1 32  ? 38.705  14.062  -47.321  1.00 22.48 ? 32  HIS A N   1 
ATOM   249   C CA  . HIS A 1 32  ? 37.857  13.425  -46.306  1.00 23.45 ? 32  HIS A CA  1 
ATOM   250   C C   . HIS A 1 32  ? 38.053  11.893  -46.266  1.00 24.13 ? 32  HIS A C   1 
ATOM   251   O O   . HIS A 1 32  ? 38.150  11.290  -45.198  1.00 23.85 ? 32  HIS A O   1 
ATOM   252   C CB  . HIS A 1 32  ? 36.386  13.768  -46.573  1.00 24.18 ? 32  HIS A CB  1 
ATOM   253   C CG  . HIS A 1 32  ? 35.434  13.248  -45.535  1.00 24.42 ? 32  HIS A CG  1 
ATOM   254   N ND1 . HIS A 1 32  ? 34.842  12.003  -45.623  1.00 23.35 ? 32  HIS A ND1 1 
ATOM   255   C CD2 . HIS A 1 32  ? 34.969  13.812  -44.393  1.00 24.14 ? 32  HIS A CD2 1 
ATOM   256   C CE1 . HIS A 1 32  ? 34.055  11.825  -44.577  1.00 23.25 ? 32  HIS A CE1 1 
ATOM   257   N NE2 . HIS A 1 32  ? 34.117  12.904  -43.814  1.00 23.35 ? 32  HIS A NE2 1 
ATOM   258   N N   . ALA A 1 33  ? 38.135  11.278  -47.440  1.00 24.54 ? 33  ALA A N   1 
ATOM   259   C CA  . ALA A 1 33  ? 38.317  9.831   -47.557  1.00 23.97 ? 33  ALA A CA  1 
ATOM   260   C C   . ALA A 1 33  ? 39.561  9.304   -46.831  1.00 23.00 ? 33  ALA A C   1 
ATOM   261   O O   . ALA A 1 33  ? 39.570  8.156   -46.400  1.00 23.21 ? 33  ALA A O   1 
ATOM   262   C CB  . ALA A 1 33  ? 38.351  9.439   -49.037  1.00 24.01 ? 33  ALA A CB  1 
ATOM   263   N N   . ASP A 1 34  ? 40.587  10.142  -46.691  1.00 22.67 ? 34  ASP A N   1 
ATOM   264   C CA  . ASP A 1 34  ? 41.860  9.757   -46.066  1.00 23.04 ? 34  ASP A CA  1 
ATOM   265   C C   . ASP A 1 34  ? 42.031  10.150  -44.594  1.00 22.82 ? 34  ASP A C   1 
ATOM   266   O O   . ASP A 1 34  ? 43.102  9.907   -44.029  1.00 22.78 ? 34  ASP A O   1 
ATOM   267   C CB  . ASP A 1 34  ? 43.019  10.391  -46.847  1.00 23.44 ? 34  ASP A CB  1 
ATOM   268   C CG  . ASP A 1 34  ? 43.097  9.914   -48.273  1.00 23.12 ? 34  ASP A CG  1 
ATOM   269   O OD1 . ASP A 1 34  ? 42.670  8.764   -48.540  1.00 23.96 ? 34  ASP A OD1 1 
ATOM   270   O OD2 . ASP A 1 34  ? 43.610  10.692  -49.108  1.00 22.93 ? 34  ASP A OD2 1 
ATOM   271   N N   . ARG A 1 35  ? 41.020  10.761  -43.977  1.00 23.12 ? 35  ARG A N   1 
ATOM   272   C CA  . ARG A 1 35  ? 41.149  11.236  -42.578  1.00 22.85 ? 35  ARG A CA  1 
ATOM   273   C C   . ARG A 1 35  ? 40.892  10.114  -41.574  1.00 21.63 ? 35  ARG A C   1 
ATOM   274   O O   . ARG A 1 35  ? 39.989  9.290   -41.765  1.00 21.60 ? 35  ARG A O   1 
ATOM   275   C CB  . ARG A 1 35  ? 40.202  12.399  -42.306  1.00 23.47 ? 35  ARG A CB  1 
ATOM   276   C CG  . ARG A 1 35  ? 40.514  13.645  -43.107  1.00 24.04 ? 35  ARG A CG  1 
ATOM   277   C CD  . ARG A 1 35  ? 39.550  14.775  -42.799  1.00 24.48 ? 35  ARG A CD  1 
ATOM   278   N NE  . ARG A 1 35  ? 39.407  15.659  -43.949  1.00 25.66 ? 35  ARG A NE  1 
ATOM   279   C CZ  . ARG A 1 35  ? 38.349  16.436  -44.195  1.00 27.21 ? 35  ARG A CZ  1 
ATOM   280   N NH1 . ARG A 1 35  ? 37.310  16.471  -43.358  1.00 28.12 ? 35  ARG A NH1 1 
ATOM   281   N NH2 . ARG A 1 35  ? 38.322  17.186  -45.296  1.00 26.64 ? 35  ARG A NH2 1 
ATOM   282   N N   . TRP A 1 36  ? 41.677  10.082  -40.499  1.00 20.78 ? 36  TRP A N   1 
ATOM   283   C CA  . TRP A 1 36  ? 41.581  8.974   -39.526  1.00 20.29 ? 36  TRP A CA  1 
ATOM   284   C C   . TRP A 1 36  ? 40.166  8.870   -38.939  1.00 21.31 ? 36  TRP A C   1 
ATOM   285   O O   . TRP A 1 36  ? 39.637  7.767   -38.790  1.00 21.33 ? 36  TRP A O   1 
ATOM   286   C CB  . TRP A 1 36  ? 42.669  9.063   -38.430  1.00 19.06 ? 36  TRP A CB  1 
ATOM   287   C CG  . TRP A 1 36  ? 42.347  9.891   -37.207  1.00 18.22 ? 36  TRP A CG  1 
ATOM   288   C CD1 . TRP A 1 36  ? 42.640  11.214  -36.989  1.00 17.94 ? 36  TRP A CD1 1 
ATOM   289   C CD2 . TRP A 1 36  ? 41.698  9.430   -36.020  1.00 17.49 ? 36  TRP A CD2 1 
ATOM   290   N NE1 . TRP A 1 36  ? 42.215  11.595  -35.735  1.00 17.73 ? 36  TRP A NE1 1 
ATOM   291   C CE2 . TRP A 1 36  ? 41.622  10.520  -35.131  1.00 17.62 ? 36  TRP A CE2 1 
ATOM   292   C CE3 . TRP A 1 36  ? 41.158  8.200   -35.629  1.00 17.13 ? 36  TRP A CE3 1 
ATOM   293   C CZ2 . TRP A 1 36  ? 41.036  10.412  -33.876  1.00 17.69 ? 36  TRP A CZ2 1 
ATOM   294   C CZ3 . TRP A 1 36  ? 40.556  8.103   -34.405  1.00 17.18 ? 36  TRP A CZ3 1 
ATOM   295   C CH2 . TRP A 1 36  ? 40.503  9.198   -33.530  1.00 17.37 ? 36  TRP A CH2 1 
ATOM   296   N N   . THR A 1 37  ? 39.560  10.020  -38.642  1.00 22.24 ? 37  THR A N   1 
ATOM   297   C CA  . THR A 1 37  ? 38.192  10.074  -38.145  1.00 22.65 ? 37  THR A CA  1 
ATOM   298   C C   . THR A 1 37  ? 37.188  9.485   -39.128  1.00 21.75 ? 37  THR A C   1 
ATOM   299   O O   . THR A 1 37  ? 36.205  8.865   -38.720  1.00 20.91 ? 37  THR A O   1 
ATOM   300   C CB  . THR A 1 37  ? 37.767  11.531  -37.834  1.00 24.83 ? 37  THR A CB  1 
ATOM   301   O OG1 . THR A 1 37  ? 38.128  12.389  -38.927  1.00 25.36 ? 37  THR A OG1 1 
ATOM   302   C CG2 . THR A 1 37  ? 38.451  12.025  -36.577  1.00 25.02 ? 37  THR A CG2 1 
ATOM   303   N N   . THR A 1 38  ? 37.419  9.689   -40.420  1.00 20.44 ? 38  THR A N   1 
ATOM   304   C CA  . THR A 1 38  ? 36.532  9.127   -41.438  1.00 19.77 ? 38  THR A CA  1 
ATOM   305   C C   . THR A 1 38  ? 36.600  7.596   -41.448  1.00 19.91 ? 38  THR A C   1 
ATOM   306   O O   . THR A 1 38  ? 35.572  6.913   -41.500  1.00 20.58 ? 38  THR A O   1 
ATOM   307   C CB  . THR A 1 38  ? 36.850  9.688   -42.828  1.00 18.89 ? 38  THR A CB  1 
ATOM   308   O OG1 . THR A 1 38  ? 36.580  11.090  -42.818  1.00 19.13 ? 38  THR A OG1 1 
ATOM   309   C CG2 . THR A 1 38  ? 36.002  9.051   -43.872  1.00 18.89 ? 38  THR A CG2 1 
ATOM   310   N N   . VAL A 1 39  ? 37.813  7.061   -41.388  1.00 19.25 ? 39  VAL A N   1 
ATOM   311   C CA  . VAL A 1 39  ? 37.991  5.625   -41.353  1.00 19.60 ? 39  VAL A CA  1 
ATOM   312   C C   . VAL A 1 39  ? 37.414  5.066   -40.053  1.00 20.32 ? 39  VAL A C   1 
ATOM   313   O O   . VAL A 1 39  ? 36.757  4.042   -40.057  1.00 21.38 ? 39  VAL A O   1 
ATOM   314   C CB  . VAL A 1 39  ? 39.455  5.210   -41.541  1.00 19.36 ? 39  VAL A CB  1 
ATOM   315   C CG1 . VAL A 1 39  ? 39.614  3.697   -41.351  1.00 19.02 ? 39  VAL A CG1 1 
ATOM   316   C CG2 . VAL A 1 39  ? 39.943  5.631   -42.925  1.00 18.71 ? 39  VAL A CG2 1 
ATOM   317   N N   . LEU A 1 40  ? 37.640  5.759   -38.948  1.00 20.57 ? 40  LEU A N   1 
ATOM   318   C CA  . LEU A 1 40  ? 36.957  5.434   -37.686  1.00 20.98 ? 40  LEU A CA  1 
ATOM   319   C C   . LEU A 1 40  ? 35.434  5.294   -37.886  1.00 21.89 ? 40  LEU A C   1 
ATOM   320   O O   . LEU A 1 40  ? 34.811  4.366   -37.376  1.00 22.68 ? 40  LEU A O   1 
ATOM   321   C CB  . LEU A 1 40  ? 37.250  6.495   -36.623  1.00 20.76 ? 40  LEU A CB  1 
ATOM   322   C CG  . LEU A 1 40  ? 36.387  6.441   -35.354  1.00 20.72 ? 40  LEU A CG  1 
ATOM   323   C CD1 . LEU A 1 40  ? 36.661  5.207   -34.525  1.00 20.30 ? 40  LEU A CD1 1 
ATOM   324   C CD2 . LEU A 1 40  ? 36.576  7.689   -34.495  1.00 20.90 ? 40  LEU A CD2 1 
ATOM   325   N N   . GLY A 1 41  ? 34.849  6.236   -38.615  1.00 22.92 ? 41  GLY A N   1 
ATOM   326   C CA  . GLY A 1 41  ? 33.414  6.247   -38.883  1.00 24.00 ? 41  GLY A CA  1 
ATOM   327   C C   . GLY A 1 41  ? 32.955  5.059   -39.707  1.00 25.42 ? 41  GLY A C   1 
ATOM   328   O O   . GLY A 1 41  ? 31.918  4.439   -39.390  1.00 23.36 ? 41  GLY A O   1 
ATOM   329   N N   . GLU A 1 42  ? 33.735  4.740   -40.750  1.00 28.07 ? 42  GLU A N   1 
ATOM   330   C CA  . GLU A 1 42  ? 33.429  3.628   -41.640  1.00 30.57 ? 42  GLU A CA  1 
ATOM   331   C C   . GLU A 1 42  ? 33.493  2.284   -40.933  1.00 29.38 ? 42  GLU A C   1 
ATOM   332   O O   . GLU A 1 42  ? 32.618  1.439   -41.127  1.00 30.23 ? 42  GLU A O   1 
ATOM   333   C CB  . GLU A 1 42  ? 34.378  3.585   -42.819  1.00 33.70 ? 42  GLU A CB  1 
ATOM   334   C CG  . GLU A 1 42  ? 33.992  4.397   -44.018  1.00 37.48 ? 42  GLU A CG  1 
ATOM   335   C CD  . GLU A 1 42  ? 35.237  4.795   -44.848  1.00 42.96 ? 42  GLU A CD  1 
ATOM   336   O OE1 . GLU A 1 42  ? 35.176  5.831   -45.585  1.00 45.60 ? 42  GLU A OE1 1 
ATOM   337   O OE2 . GLU A 1 42  ? 36.288  4.067   -44.809  1.00 42.29 ? 42  GLU A OE2 1 
ATOM   338   N N   . ASN A 1 43  ? 34.515  2.096   -40.109  1.00 28.45 ? 43  ASN A N   1 
ATOM   339   C CA  . ASN A 1 43  ? 34.669  0.865   -39.361  1.00 29.47 ? 43  ASN A CA  1 
ATOM   340   C C   . ASN A 1 43  ? 33.667  0.700   -38.225  1.00 31.01 ? 43  ASN A C   1 
ATOM   341   O O   . ASN A 1 43  ? 33.502  -0.397  -37.721  1.00 31.79 ? 43  ASN A O   1 
ATOM   342   C CB  . ASN A 1 43  ? 36.076  0.755   -38.792  1.00 29.71 ? 43  ASN A CB  1 
ATOM   343   C CG  . ASN A 1 43  ? 37.074  0.239   -39.808  1.00 28.16 ? 43  ASN A CG  1 
ATOM   344   O OD1 . ASN A 1 43  ? 37.396  -0.931  -39.812  1.00 27.52 ? 43  ASN A OD1 1 
ATOM   345   N ND2 . ASN A 1 43  ? 37.580  1.121   -40.662  1.00 28.36 ? 43  ASN A ND2 1 
ATOM   346   N N   . LEU A 1 44  ? 33.034  1.786   -37.795  1.00 32.99 ? 44  LEU A N   1 
ATOM   347   C CA  . LEU A 1 44  ? 32.007  1.725   -36.735  1.00 35.46 ? 44  LEU A CA  1 
ATOM   348   C C   . LEU A 1 44  ? 30.646  1.294   -37.284  1.00 38.51 ? 44  LEU A C   1 
ATOM   349   O O   . LEU A 1 44  ? 29.904  0.573   -36.614  1.00 34.40 ? 44  LEU A O   1 
ATOM   350   C CB  . LEU A 1 44  ? 31.878  3.066   -35.995  1.00 33.36 ? 44  LEU A CB  1 
ATOM   351   C CG  . LEU A 1 44  ? 32.915  3.340   -34.900  1.00 33.49 ? 44  LEU A CG  1 
ATOM   352   C CD1 . LEU A 1 44  ? 32.824  4.764   -34.384  1.00 32.74 ? 44  LEU A CD1 1 
ATOM   353   C CD2 . LEU A 1 44  ? 32.794  2.350   -33.735  1.00 34.71 ? 44  LEU A CD2 1 
ATOM   354   N N   . GLY A 1 45  ? 30.325  1.763   -38.497  1.00 42.29 ? 45  GLY A N   1 
ATOM   355   C CA  . GLY A 1 45  ? 29.065  1.435   -39.154  1.00 43.81 ? 45  GLY A CA  1 
ATOM   356   C C   . GLY A 1 45  ? 27.922  2.403   -38.859  1.00 45.94 ? 45  GLY A C   1 
ATOM   357   O O   . GLY A 1 45  ? 28.130  3.450   -38.238  1.00 49.55 ? 45  GLY A O   1 
ATOM   358   N N   . ASP A 1 46  ? 26.725  2.039   -39.325  1.00 49.17 ? 46  ASP A N   1 
ATOM   359   C CA  . ASP A 1 46  ? 25.531  2.881   -39.189  1.00 48.90 ? 46  ASP A CA  1 
ATOM   360   C C   . ASP A 1 46  ? 25.055  3.067   -37.757  1.00 44.47 ? 46  ASP A C   1 
ATOM   361   O O   . ASP A 1 46  ? 24.263  3.969   -37.484  1.00 41.95 ? 46  ASP A O   1 
ATOM   362   C CB  . ASP A 1 46  ? 24.365  2.292   -40.005  1.00 50.63 ? 46  ASP A CB  1 
ATOM   363   C CG  . ASP A 1 46  ? 24.611  2.335   -41.495  1.00 51.20 ? 46  ASP A CG  1 
ATOM   364   O OD1 . ASP A 1 46  ? 25.464  3.115   -41.982  1.00 52.17 ? 46  ASP A OD1 1 
ATOM   365   O OD2 . ASP A 1 46  ? 23.903  1.589   -42.177  1.00 53.18 ? 46  ASP A OD2 1 
ATOM   366   N N   . GLY A 1 47  ? 25.512  2.200   -36.858  1.00 42.00 ? 47  GLY A N   1 
ATOM   367   C CA  . GLY A 1 47  ? 25.171  2.327   -35.439  1.00 39.07 ? 47  GLY A CA  1 
ATOM   368   C C   . GLY A 1 47  ? 25.719  3.598   -34.806  1.00 36.85 ? 47  GLY A C   1 
ATOM   369   O O   . GLY A 1 47  ? 25.241  4.008   -33.743  1.00 33.80 ? 47  GLY A O   1 
ATOM   370   N N   . TYR A 1 48  ? 26.707  4.217   -35.469  1.00 35.24 ? 48  TYR A N   1 
ATOM   371   C CA  . TYR A 1 48  ? 27.406  5.379   -34.945  1.00 33.96 ? 48  TYR A CA  1 
ATOM   372   C C   . TYR A 1 48  ? 27.405  6.569   -35.909  1.00 31.17 ? 48  TYR A C   1 
ATOM   373   O O   . TYR A 1 48  ? 27.297  6.414   -37.118  1.00 29.35 ? 48  TYR A O   1 
ATOM   374   C CB  . TYR A 1 48  ? 28.843  5.001   -34.602  1.00 35.01 ? 48  TYR A CB  1 
ATOM   375   C CG  . TYR A 1 48  ? 28.964  3.863   -33.613  1.00 35.95 ? 48  TYR A CG  1 
ATOM   376   C CD1 . TYR A 1 48  ? 28.774  2.536   -34.018  1.00 35.79 ? 48  TYR A CD1 1 
ATOM   377   C CD2 . TYR A 1 48  ? 29.278  4.108   -32.279  1.00 36.64 ? 48  TYR A CD2 1 
ATOM   378   C CE1 . TYR A 1 48  ? 28.893  1.491   -33.119  1.00 36.48 ? 48  TYR A CE1 1 
ATOM   379   C CE2 . TYR A 1 48  ? 29.393  3.061   -31.383  1.00 37.45 ? 48  TYR A CE2 1 
ATOM   380   C CZ  . TYR A 1 48  ? 29.203  1.757   -31.806  1.00 36.93 ? 48  TYR A CZ  1 
ATOM   381   O OH  . TYR A 1 48  ? 29.338  0.756   -30.890  1.00 38.77 ? 48  TYR A OH  1 
ATOM   382   N N   . GLU A 1 49  ? 27.554  7.755   -35.320  1.00 28.94 ? 49  GLU A N   1 
ATOM   383   C CA  . GLU A 1 49  ? 27.575  9.032   -36.011  1.00 27.49 ? 49  GLU A CA  1 
ATOM   384   C C   . GLU A 1 49  ? 28.682  9.897   -35.362  1.00 24.70 ? 49  GLU A C   1 
ATOM   385   O O   . GLU A 1 49  ? 28.678  10.098  -34.157  1.00 24.65 ? 49  GLU A O   1 
ATOM   386   C CB  . GLU A 1 49  ? 26.189  9.656   -35.852  1.00 29.86 ? 49  GLU A CB  1 
ATOM   387   C CG  . GLU A 1 49  ? 25.998  11.104  -36.349  1.00 32.24 ? 49  GLU A CG  1 
ATOM   388   C CD  . GLU A 1 49  ? 24.536  11.551  -36.288  1.00 33.12 ? 49  GLU A CD  1 
ATOM   389   O OE1 . GLU A 1 49  ? 24.206  12.666  -35.791  1.00 33.47 ? 49  GLU A OE1 1 
ATOM   390   O OE2 . GLU A 1 49  ? 23.690  10.770  -36.759  1.00 35.73 ? 49  GLU A OE2 1 
ATOM   391   N N   . LEU A 1 50  ? 29.636  10.388  -36.140  1.00 22.09 ? 50  LEU A N   1 
ATOM   392   C CA  . LEU A 1 50  ? 30.741  11.185  -35.581  1.00 21.02 ? 50  LEU A CA  1 
ATOM   393   C C   . LEU A 1 50  ? 30.585  12.692  -35.701  1.00 20.01 ? 50  LEU A C   1 
ATOM   394   O O   . LEU A 1 50  ? 30.009  13.184  -36.660  1.00 19.65 ? 50  LEU A O   1 
ATOM   395   C CB  . LEU A 1 50  ? 32.056  10.830  -36.273  1.00 21.66 ? 50  LEU A CB  1 
ATOM   396   C CG  . LEU A 1 50  ? 32.582  9.407   -36.163  1.00 21.46 ? 50  LEU A CG  1 
ATOM   397   C CD1 . LEU A 1 50  ? 33.933  9.401   -36.849  1.00 21.19 ? 50  LEU A CD1 1 
ATOM   398   C CD2 . LEU A 1 50  ? 32.672  8.985   -34.704  1.00 21.47 ? 50  LEU A CD2 1 
ATOM   399   N N   . VAL A 1 51  ? 31.104  13.418  -34.712  1.00 18.95 ? 51  VAL A N   1 
ATOM   400   C CA  . VAL A 1 51  ? 31.261  14.873  -34.775  1.00 18.17 ? 51  VAL A CA  1 
ATOM   401   C C   . VAL A 1 51  ? 32.729  15.154  -34.500  1.00 17.70 ? 51  VAL A C   1 
ATOM   402   O O   . VAL A 1 51  ? 33.268  14.664  -33.523  1.00 17.30 ? 51  VAL A O   1 
ATOM   403   C CB  . VAL A 1 51  ? 30.408  15.592  -33.720  1.00 17.86 ? 51  VAL A CB  1 
ATOM   404   C CG1 . VAL A 1 51  ? 30.421  17.104  -33.955  1.00 18.04 ? 51  VAL A CG1 1 
ATOM   405   C CG2 . VAL A 1 51  ? 28.997  15.073  -33.761  1.00 17.89 ? 51  VAL A CG2 1 
ATOM   406   N N   . VAL A 1 52  ? 33.376  15.930  -35.359  1.00 17.42 ? 52  VAL A N   1 
ATOM   407   C CA  . VAL A 1 52  ? 34.825  16.062  -35.318  1.00 17.94 ? 52  VAL A CA  1 
ATOM   408   C C   . VAL A 1 52  ? 35.274  17.511  -35.174  1.00 18.57 ? 52  VAL A C   1 
ATOM   409   O O   . VAL A 1 52  ? 34.834  18.381  -35.914  1.00 19.59 ? 52  VAL A O   1 
ATOM   410   C CB  . VAL A 1 52  ? 35.462  15.452  -36.578  1.00 17.84 ? 52  VAL A CB  1 
ATOM   411   C CG1 . VAL A 1 52  ? 36.979  15.515  -36.506  1.00 17.94 ? 52  VAL A CG1 1 
ATOM   412   C CG2 . VAL A 1 52  ? 35.017  13.999  -36.744  1.00 17.98 ? 52  VAL A CG2 1 
ATOM   413   N N   . ASP A 1 53  ? 36.157  17.768  -34.216  1.00 18.83 ? 53  ASP A N   1 
ATOM   414   C CA  . ASP A 1 53  ? 36.684  19.110  -34.010  1.00 19.25 ? 53  ASP A CA  1 
ATOM   415   C C   . ASP A 1 53  ? 38.189  19.060  -33.845  1.00 19.19 ? 53  ASP A C   1 
ATOM   416   O O   . ASP A 1 53  ? 38.697  18.910  -32.735  1.00 19.57 ? 53  ASP A O   1 
ATOM   417   C CB  . ASP A 1 53  ? 36.047  19.778  -32.799  1.00 19.97 ? 53  ASP A CB  1 
ATOM   418   C CG  . ASP A 1 53  ? 36.116  21.295  -32.874  1.00 20.67 ? 53  ASP A CG  1 
ATOM   419   O OD1 . ASP A 1 53  ? 37.236  21.854  -32.831  1.00 21.37 ? 53  ASP A OD1 1 
ATOM   420   O OD2 . ASP A 1 53  ? 35.044  21.922  -32.962  1.00 20.56 ? 53  ASP A OD2 1 
ATOM   421   N N   . GLY A 1 54  ? 38.894  19.187  -34.963  1.00 19.15 ? 54  GLY A N   1 
ATOM   422   C CA  . GLY A 1 54  ? 40.351  19.193  -34.984  1.00 18.64 ? 54  GLY A CA  1 
ATOM   423   C C   . GLY A 1 54  ? 40.894  20.559  -35.370  1.00 18.00 ? 54  GLY A C   1 
ATOM   424   O O   . GLY A 1 54  ? 40.602  21.057  -36.453  1.00 18.01 ? 54  GLY A O   1 
ATOM   425   N N   . LEU A 1 55  ? 41.687  21.153  -34.474  1.00 17.55 ? 55  LEU A N   1 
ATOM   426   C CA  . LEU A 1 55  ? 42.288  22.471  -34.678  1.00 16.83 ? 55  LEU A CA  1 
ATOM   427   C C   . LEU A 1 55  ? 43.806  22.378  -34.736  1.00 16.11 ? 55  LEU A C   1 
ATOM   428   O O   . LEU A 1 55  ? 44.435  22.003  -33.758  1.00 15.09 ? 55  LEU A O   1 
ATOM   429   C CB  . LEU A 1 55  ? 41.891  23.430  -33.547  1.00 16.70 ? 55  LEU A CB  1 
ATOM   430   C CG  . LEU A 1 55  ? 42.544  24.831  -33.535  1.00 16.69 ? 55  LEU A CG  1 
ATOM   431   C CD1 . LEU A 1 55  ? 42.203  25.577  -34.812  1.00 16.77 ? 55  LEU A CD1 1 
ATOM   432   C CD2 . LEU A 1 55  ? 42.129  25.662  -32.336  1.00 16.63 ? 55  LEU A CD2 1 
ATOM   433   N N   . SER A 1 56  ? 44.383  22.748  -35.877  1.00 15.82 ? 56  SER A N   1 
ATOM   434   C CA  . SER A 1 56  ? 45.832  22.819  -36.006  1.00 15.41 ? 56  SER A CA  1 
ATOM   435   C C   . SER A 1 56  ? 46.377  23.685  -34.887  1.00 15.56 ? 56  SER A C   1 
ATOM   436   O O   . SER A 1 56  ? 45.875  24.767  -34.633  1.00 15.88 ? 56  SER A O   1 
ATOM   437   C CB  . SER A 1 56  ? 46.248  23.386  -37.376  1.00 14.91 ? 56  SER A CB  1 
ATOM   438   O OG  . SER A 1 56  ? 45.616  22.706  -38.468  1.00 14.61 ? 56  SER A OG  1 
ATOM   439   N N   . GLY A 1 57  ? 47.383  23.185  -34.188  1.00 16.10 ? 57  GLY A N   1 
ATOM   440   C CA  . GLY A 1 57  ? 48.085  23.942  -33.147  1.00 16.29 ? 57  GLY A CA  1 
ATOM   441   C C   . GLY A 1 57  ? 47.558  23.790  -31.725  1.00 16.10 ? 57  GLY A C   1 
ATOM   442   O O   . GLY A 1 57  ? 48.175  24.294  -30.795  1.00 16.33 ? 57  GLY A O   1 
ATOM   443   N N   . ARG A 1 58  ? 46.457  23.064  -31.560  1.00 15.96 ? 58  ARG A N   1 
ATOM   444   C CA  . ARG A 1 58  ? 45.726  23.016  -30.289  1.00 16.16 ? 58  ARG A CA  1 
ATOM   445   C C   . ARG A 1 58  ? 46.424  22.221  -29.179  1.00 16.58 ? 58  ARG A C   1 
ATOM   446   O O   . ARG A 1 58  ? 46.959  21.121  -29.412  1.00 17.63 ? 58  ARG A O   1 
ATOM   447   C CB  . ARG A 1 58  ? 44.309  22.456  -30.518  1.00 15.71 ? 58  ARG A CB  1 
ATOM   448   C CG  . ARG A 1 58  ? 43.436  22.307  -29.270  1.00 15.15 ? 58  ARG A CG  1 
ATOM   449   C CD  . ARG A 1 58  ? 42.069  21.703  -29.627  1.00 14.67 ? 58  ARG A CD  1 
ATOM   450   N NE  . ARG A 1 58  ? 41.094  22.704  -30.049  1.00 14.19 ? 58  ARG A NE  1 
ATOM   451   C CZ  . ARG A 1 58  ? 40.003  22.469  -30.778  1.00 13.67 ? 58  ARG A CZ  1 
ATOM   452   N NH1 . ARG A 1 58  ? 39.719  21.261  -31.225  1.00 13.59 ? 58  ARG A NH1 1 
ATOM   453   N NH2 . ARG A 1 58  ? 39.192  23.466  -31.073  1.00 13.74 ? 58  ARG A NH2 1 
ATOM   454   N N   . THR A 1 59  ? 46.387  22.788  -27.971  1.00 16.57 ? 59  THR A N   1 
ATOM   455   C CA  . THR A 1 59  ? 46.956  22.173  -26.780  1.00 16.30 ? 59  THR A CA  1 
ATOM   456   C C   . THR A 1 59  ? 45.855  21.638  -25.895  1.00 16.04 ? 59  THR A C   1 
ATOM   457   O O   . THR A 1 59  ? 44.676  21.904  -26.138  1.00 15.54 ? 59  THR A O   1 
ATOM   458   C CB  . THR A 1 59  ? 47.743  23.206  -25.958  1.00 17.17 ? 59  THR A CB  1 
ATOM   459   O OG1 . THR A 1 59  ? 46.830  24.084  -25.269  1.00 18.50 ? 59  THR A OG1 1 
ATOM   460   C CG2 . THR A 1 59  ? 48.666  24.025  -26.853  1.00 17.09 ? 59  THR A CG2 1 
ATOM   461   N N   . THR A 1 60  ? 46.236  20.891  -24.859  1.00 15.99 ? 60  THR A N   1 
ATOM   462   C CA  . THR A 1 60  ? 45.274  20.425  -23.860  1.00 16.13 ? 60  THR A CA  1 
ATOM   463   C C   . THR A 1 60  ? 44.605  21.612  -23.165  1.00 16.13 ? 60  THR A C   1 
ATOM   464   O O   . THR A 1 60  ? 43.404  21.828  -23.326  1.00 16.60 ? 60  THR A O   1 
ATOM   465   C CB  . THR A 1 60  ? 45.928  19.551  -22.775  1.00 15.95 ? 60  THR A CB  1 
ATOM   466   O OG1 . THR A 1 60  ? 47.069  20.219  -22.231  1.00 16.00 ? 60  THR A OG1 1 
ATOM   467   C CG2 . THR A 1 60  ? 46.355  18.219  -23.353  1.00 16.25 ? 60  THR A CG2 1 
ATOM   468   N N   . ASN A 1 61  ? 45.392  22.382  -22.409  1.00 15.22 ? 61  ASN A N   1 
ATOM   469   C CA  . ASN A 1 61  ? 44.835  23.380  -21.490  1.00 14.25 ? 61  ASN A CA  1 
ATOM   470   C C   . ASN A 1 61  ? 45.739  24.584  -21.210  1.00 14.31 ? 61  ASN A C   1 
ATOM   471   O O   . ASN A 1 61  ? 45.625  25.205  -20.153  1.00 13.86 ? 61  ASN A O   1 
ATOM   472   C CB  . ASN A 1 61  ? 44.516  22.700  -20.164  1.00 13.47 ? 61  ASN A CB  1 
ATOM   473   C CG  . ASN A 1 61  ? 45.746  22.488  -19.306  1.00 13.13 ? 61  ASN A CG  1 
ATOM   474   O OD1 . ASN A 1 61  ? 46.857  22.355  -19.796  1.00 13.46 ? 61  ASN A OD1 1 
ATOM   475   N ND2 . ASN A 1 61  ? 45.548  22.453  -18.019  1.00 13.00 ? 61  ASN A ND2 1 
ATOM   476   N N   . ILE A 1 62  ? 46.618  24.923  -22.153  1.00 14.38 ? 62  ILE A N   1 
ATOM   477   C CA  . ILE A 1 62  ? 47.594  25.992  -21.948  1.00 14.19 ? 62  ILE A CA  1 
ATOM   478   C C   . ILE A 1 62  ? 47.585  26.972  -23.110  1.00 13.89 ? 62  ILE A C   1 
ATOM   479   O O   . ILE A 1 62  ? 47.487  26.560  -24.269  1.00 14.09 ? 62  ILE A O   1 
ATOM   480   C CB  . ILE A 1 62  ? 49.005  25.403  -21.780  1.00 14.59 ? 62  ILE A CB  1 
ATOM   481   C CG1 . ILE A 1 62  ? 50.018  26.493  -21.416  1.00 14.52 ? 62  ILE A CG1 1 
ATOM   482   C CG2 . ILE A 1 62  ? 49.455  24.686  -23.056  1.00 14.95 ? 62  ILE A CG2 1 
ATOM   483   C CD1 . ILE A 1 62  ? 51.326  25.926  -20.927  1.00 14.17 ? 62  ILE A CD1 1 
ATOM   484   N N   . ASP A 1 63  ? 47.683  28.263  -22.803  1.00 13.90 ? 63  ASP A N   1 
ATOM   485   C CA  . ASP A 1 63  ? 47.744  29.309  -23.846  1.00 13.91 ? 63  ASP A CA  1 
ATOM   486   C C   . ASP A 1 63  ? 49.034  29.241  -24.643  1.00 13.80 ? 63  ASP A C   1 
ATOM   487   O O   . ASP A 1 63  ? 50.118  29.060  -24.077  1.00 13.80 ? 63  ASP A O   1 
ATOM   488   C CB  . ASP A 1 63  ? 47.647  30.708  -23.248  1.00 13.90 ? 63  ASP A CB  1 
ATOM   489   C CG  . ASP A 1 63  ? 46.334  30.972  -22.597  1.00 14.31 ? 63  ASP A CG  1 
ATOM   490   O OD1 . ASP A 1 63  ? 45.304  30.425  -23.054  1.00 15.28 ? 63  ASP A OD1 1 
ATOM   491   O OD2 . ASP A 1 63  ? 46.326  31.751  -21.631  1.00 14.39 ? 63  ASP A OD2 1 
ATOM   492   N N   . ASP A 1 64  ? 48.910  29.388  -25.954  1.00 13.85 ? 64  ASP A N   1 
ATOM   493   C CA  . ASP A 1 64  ? 50.068  29.581  -26.808  1.00 14.29 ? 64  ASP A CA  1 
ATOM   494   C C   . ASP A 1 64  ? 50.267  31.105  -26.968  1.00 14.55 ? 64  ASP A C   1 
ATOM   495   O O   . ASP A 1 64  ? 49.388  31.808  -27.498  1.00 14.54 ? 64  ASP A O   1 
ATOM   496   C CB  . ASP A 1 64  ? 49.858  28.894  -28.157  1.00 14.62 ? 64  ASP A CB  1 
ATOM   497   C CG  . ASP A 1 64  ? 51.127  28.796  -28.963  1.00 15.14 ? 64  ASP A CG  1 
ATOM   498   O OD1 . ASP A 1 64  ? 51.806  29.824  -29.144  1.00 15.52 ? 64  ASP A OD1 1 
ATOM   499   O OD2 . ASP A 1 64  ? 51.464  27.688  -29.414  1.00 16.27 ? 64  ASP A OD2 1 
ATOM   500   N N   . PRO A 1 65  ? 51.408  31.628  -26.499  1.00 14.45 ? 65  PRO A N   1 
ATOM   501   C CA  . PRO A 1 65  ? 51.565  33.087  -26.600  1.00 14.84 ? 65  PRO A CA  1 
ATOM   502   C C   . PRO A 1 65  ? 51.586  33.601  -28.057  1.00 15.27 ? 65  PRO A C   1 
ATOM   503   O O   . PRO A 1 65  ? 51.410  34.801  -28.286  1.00 15.12 ? 65  PRO A O   1 
ATOM   504   C CB  . PRO A 1 65  ? 52.884  33.371  -25.867  1.00 14.75 ? 65  PRO A CB  1 
ATOM   505   C CG  . PRO A 1 65  ? 53.598  32.067  -25.852  1.00 14.84 ? 65  PRO A CG  1 
ATOM   506   C CD  . PRO A 1 65  ? 52.571  30.971  -25.877  1.00 14.51 ? 65  PRO A CD  1 
ATOM   507   N N   . ASN A 1 66  ? 51.764  32.698  -29.021  1.00 14.97 ? 66  ASN A N   1 
ATOM   508   C CA  . ASN A 1 66  ? 51.747  33.069  -30.440  1.00 14.60 ? 66  ASN A CA  1 
ATOM   509   C C   . ASN A 1 66  ? 50.372  33.138  -31.085  1.00 14.49 ? 66  ASN A C   1 
ATOM   510   O O   . ASN A 1 66  ? 50.229  33.679  -32.161  1.00 14.11 ? 66  ASN A O   1 
ATOM   511   C CB  . ASN A 1 66  ? 52.603  32.095  -31.241  1.00 14.58 ? 66  ASN A CB  1 
ATOM   512   C CG  . ASN A 1 66  ? 54.037  32.077  -30.777  1.00 14.73 ? 66  ASN A CG  1 
ATOM   513   O OD1 . ASN A 1 66  ? 54.774  33.015  -31.024  1.00 14.73 ? 66  ASN A OD1 1 
ATOM   514   N ND2 . ASN A 1 66  ? 54.439  31.003  -30.102  1.00 15.06 ? 66  ASN A ND2 1 
ATOM   515   N N   . ASP A 1 67  ? 49.361  32.574  -30.438  1.00 15.09 ? 67  ASP A N   1 
ATOM   516   C CA  . ASP A 1 67  ? 48.016  32.485  -31.025  1.00 15.10 ? 67  ASP A CA  1 
ATOM   517   C C   . ASP A 1 67  ? 46.991  32.210  -29.920  1.00 15.13 ? 67  ASP A C   1 
ATOM   518   O O   . ASP A 1 67  ? 46.993  31.129  -29.297  1.00 15.20 ? 67  ASP A O   1 
ATOM   519   C CB  . ASP A 1 67  ? 47.964  31.387  -32.086  1.00 14.99 ? 67  ASP A CB  1 
ATOM   520   C CG  . ASP A 1 67  ? 46.672  31.421  -32.900  1.00 15.32 ? 67  ASP A CG  1 
ATOM   521   O OD1 . ASP A 1 67  ? 45.682  32.107  -32.507  1.00 14.94 ? 67  ASP A OD1 1 
ATOM   522   O OD2 . ASP A 1 67  ? 46.660  30.753  -33.945  1.00 15.60 ? 67  ASP A OD2 1 
ATOM   523   N N   . PRO A 1 68  ? 46.105  33.186  -29.673  1.00 14.97 ? 68  PRO A N   1 
ATOM   524   C CA  . PRO A 1 68  ? 45.199  33.016  -28.547  1.00 14.84 ? 68  PRO A CA  1 
ATOM   525   C C   . PRO A 1 68  ? 44.067  32.003  -28.744  1.00 14.80 ? 68  PRO A C   1 
ATOM   526   O O   . PRO A 1 68  ? 43.330  31.790  -27.812  1.00 15.45 ? 68  PRO A O   1 
ATOM   527   C CB  . PRO A 1 68  ? 44.643  34.430  -28.321  1.00 14.71 ? 68  PRO A CB  1 
ATOM   528   C CG  . PRO A 1 68  ? 44.956  35.219  -29.531  1.00 14.36 ? 68  PRO A CG  1 
ATOM   529   C CD  . PRO A 1 68  ? 45.984  34.498  -30.336  1.00 14.69 ? 68  PRO A CD  1 
ATOM   530   N N   . LYS A 1 69  ? 43.933  31.358  -29.900  1.00 15.14 ? 69  LYS A N   1 
ATOM   531   C CA  . LYS A 1 69  ? 42.829  30.404  -30.092  1.00 16.08 ? 69  LYS A CA  1 
ATOM   532   C C   . LYS A 1 69  ? 43.166  28.919  -29.927  1.00 16.08 ? 69  LYS A C   1 
ATOM   533   O O   . LYS A 1 69  ? 42.342  28.072  -30.259  1.00 16.72 ? 69  LYS A O   1 
ATOM   534   C CB  . LYS A 1 69  ? 42.188  30.622  -31.472  1.00 17.13 ? 69  LYS A CB  1 
ATOM   535   C CG  . LYS A 1 69  ? 43.011  30.150  -32.680  1.00 17.52 ? 69  LYS A CG  1 
ATOM   536   C CD  . LYS A 1 69  ? 42.320  30.490  -33.982  1.00 17.62 ? 69  LYS A CD  1 
ATOM   537   C CE  . LYS A 1 69  ? 43.136  30.036  -35.186  1.00 17.99 ? 69  LYS A CE  1 
ATOM   538   N NZ  . LYS A 1 69  ? 44.269  30.954  -35.530  1.00 17.97 ? 69  LYS A NZ  1 
ATOM   539   N N   . LEU A 1 70  ? 44.351  28.604  -29.410  1.00 16.32 ? 70  LEU A N   1 
ATOM   540   C CA  . LEU A 1 70  ? 44.880  27.235  -29.434  1.00 16.12 ? 70  LEU A CA  1 
ATOM   541   C C   . LEU A 1 70  ? 44.712  26.439  -28.132  1.00 15.73 ? 70  LEU A C   1 
ATOM   542   O O   . LEU A 1 70  ? 45.203  25.320  -28.026  1.00 15.52 ? 70  LEU A O   1 
ATOM   543   C CB  . LEU A 1 70  ? 46.358  27.272  -29.805  1.00 16.46 ? 70  LEU A CB  1 
ATOM   544   C CG  . LEU A 1 70  ? 46.662  27.902  -31.167  1.00 17.01 ? 70  LEU A CG  1 
ATOM   545   C CD1 . LEU A 1 70  ? 48.154  27.806  -31.473  1.00 17.37 ? 70  LEU A CD1 1 
ATOM   546   C CD2 . LEU A 1 70  ? 45.850  27.230  -32.262  1.00 16.94 ? 70  LEU A CD2 1 
ATOM   547   N N   . ASN A 1 71  ? 44.027  27.007  -27.148  1.00 15.18 ? 71  ASN A N   1 
ATOM   548   C CA  . ASN A 1 71  ? 43.855  26.336  -25.882  1.00 15.15 ? 71  ASN A CA  1 
ATOM   549   C C   . ASN A 1 71  ? 42.586  25.490  -25.883  1.00 15.95 ? 71  ASN A C   1 
ATOM   550   O O   . ASN A 1 71  ? 41.477  26.019  -25.828  1.00 16.11 ? 71  ASN A O   1 
ATOM   551   C CB  . ASN A 1 71  ? 43.787  27.366  -24.773  1.00 14.87 ? 71  ASN A CB  1 
ATOM   552   C CG  . ASN A 1 71  ? 43.890  26.758  -23.396  1.00 14.44 ? 71  ASN A CG  1 
ATOM   553   O OD1 . ASN A 1 71  ? 43.343  25.686  -23.129  1.00 14.39 ? 71  ASN A OD1 1 
ATOM   554   N ND2 . ASN A 1 71  ? 44.585  27.453  -22.507  1.00 14.04 ? 71  ASN A ND2 1 
ATOM   555   N N   . GLY A 1 72  ? 42.755  24.164  -25.929  1.00 16.17 ? 72  GLY A N   1 
ATOM   556   C CA  . GLY A 1 72  ? 41.618  23.229  -25.941  1.00 15.46 ? 72  GLY A CA  1 
ATOM   557   C C   . GLY A 1 72  ? 40.577  23.501  -24.874  1.00 15.21 ? 72  GLY A C   1 
ATOM   558   O O   . GLY A 1 72  ? 39.383  23.455  -25.140  1.00 14.48 ? 72  GLY A O   1 
ATOM   559   N N   . ALA A 1 73  ? 41.039  23.801  -23.664  1.00 15.58 ? 73  ALA A N   1 
ATOM   560   C CA  . ALA A 1 73  ? 40.163  23.984  -22.509  1.00 15.77 ? 73  ALA A CA  1 
ATOM   561   C C   . ALA A 1 73  ? 39.369  25.294  -22.564  1.00 16.85 ? 73  ALA A C   1 
ATOM   562   O O   . ALA A 1 73  ? 38.316  25.403  -21.924  1.00 17.32 ? 73  ALA A O   1 
ATOM   563   C CB  . ALA A 1 73  ? 40.978  23.901  -21.239  1.00 15.47 ? 73  ALA A CB  1 
ATOM   564   N N   . ASP A 1 74  ? 39.853  26.288  -23.316  1.00 17.58 ? 74  ASP A N   1 
ATOM   565   C CA  . ASP A 1 74  ? 39.044  27.474  -23.611  1.00 18.25 ? 74  ASP A CA  1 
ATOM   566   C C   . ASP A 1 74  ? 37.789  27.121  -24.408  1.00 17.78 ? 74  ASP A C   1 
ATOM   567   O O   . ASP A 1 74  ? 36.771  27.758  -24.263  1.00 17.63 ? 74  ASP A O   1 
ATOM   568   C CB  . ASP A 1 74  ? 39.836  28.513  -24.422  1.00 19.30 ? 74  ASP A CB  1 
ATOM   569   C CG  . ASP A 1 74  ? 40.834  29.305  -23.590  1.00 19.80 ? 74  ASP A CG  1 
ATOM   570   O OD1 . ASP A 1 74  ? 40.721  29.323  -22.366  1.00 21.21 ? 74  ASP A OD1 1 
ATOM   571   O OD2 . ASP A 1 74  ? 41.730  29.936  -24.177  1.00 20.66 ? 74  ASP A OD2 1 
ATOM   572   N N   . TYR A 1 75  ? 37.879  26.099  -25.247  1.00 18.30 ? 75  TYR A N   1 
ATOM   573   C CA  . TYR A 1 75  ? 36.864  25.762  -26.260  1.00 18.59 ? 75  TYR A CA  1 
ATOM   574   C C   . TYR A 1 75  ? 35.930  24.615  -25.852  1.00 18.39 ? 75  TYR A C   1 
ATOM   575   O O   . TYR A 1 75  ? 34.755  24.600  -26.218  1.00 17.57 ? 75  TYR A O   1 
ATOM   576   C CB  . TYR A 1 75  ? 37.641  25.368  -27.515  1.00 18.60 ? 75  TYR A CB  1 
ATOM   577   C CG  . TYR A 1 75  ? 36.919  25.206  -28.836  1.00 18.92 ? 75  TYR A CG  1 
ATOM   578   C CD1 . TYR A 1 75  ? 36.373  23.980  -29.195  1.00 19.78 ? 75  TYR A CD1 1 
ATOM   579   C CD2 . TYR A 1 75  ? 36.910  26.229  -29.789  1.00 18.75 ? 75  TYR A CD2 1 
ATOM   580   C CE1 . TYR A 1 75  ? 35.776  23.796  -30.443  1.00 20.15 ? 75  TYR A CE1 1 
ATOM   581   C CE2 . TYR A 1 75  ? 36.316  26.057  -31.030  1.00 18.89 ? 75  TYR A CE2 1 
ATOM   582   C CZ  . TYR A 1 75  ? 35.757  24.842  -31.360  1.00 19.59 ? 75  TYR A CZ  1 
ATOM   583   O OH  . TYR A 1 75  ? 35.178  24.662  -32.591  1.00 20.14 ? 75  TYR A OH  1 
ATOM   584   N N   . LEU A 1 76  ? 36.455  23.661  -25.090  1.00 18.03 ? 76  LEU A N   1 
ATOM   585   C CA  . LEU A 1 76  ? 35.773  22.388  -24.899  1.00 17.82 ? 76  LEU A CA  1 
ATOM   586   C C   . LEU A 1 76  ? 34.412  22.492  -24.203  1.00 17.26 ? 76  LEU A C   1 
ATOM   587   O O   . LEU A 1 76  ? 33.470  21.828  -24.637  1.00 17.25 ? 76  LEU A O   1 
ATOM   588   C CB  . LEU A 1 76  ? 36.678  21.378  -24.176  1.00 18.26 ? 76  LEU A CB  1 
ATOM   589   C CG  . LEU A 1 76  ? 36.096  19.956  -24.058  1.00 18.63 ? 76  LEU A CG  1 
ATOM   590   C CD1 . LEU A 1 76  ? 35.723  19.379  -25.416  1.00 18.71 ? 76  LEU A CD1 1 
ATOM   591   C CD2 . LEU A 1 76  ? 37.064  19.037  -23.357  1.00 18.84 ? 76  LEU A CD2 1 
ATOM   592   N N   . PRO A 1 77  ? 34.291  23.312  -23.133  1.00 16.82 ? 77  PRO A N   1 
ATOM   593   C CA  . PRO A 1 77  ? 32.985  23.428  -22.492  1.00 17.24 ? 77  PRO A CA  1 
ATOM   594   C C   . PRO A 1 77  ? 31.868  23.786  -23.475  1.00 18.11 ? 77  PRO A C   1 
ATOM   595   O O   . PRO A 1 77  ? 30.800  23.150  -23.473  1.00 18.89 ? 77  PRO A O   1 
ATOM   596   C CB  . PRO A 1 77  ? 33.199  24.537  -21.467  1.00 16.36 ? 77  PRO A CB  1 
ATOM   597   C CG  . PRO A 1 77  ? 34.605  24.346  -21.066  1.00 16.40 ? 77  PRO A CG  1 
ATOM   598   C CD  . PRO A 1 77  ? 35.312  24.031  -22.362  1.00 16.51 ? 77  PRO A CD  1 
ATOM   599   N N   . ALA A 1 78  ? 32.126  24.782  -24.317  1.00 18.73 ? 78  ALA A N   1 
ATOM   600   C CA  . ALA A 1 78  ? 31.159  25.207  -25.322  1.00 18.80 ? 78  ALA A CA  1 
ATOM   601   C C   . ALA A 1 78  ? 30.888  24.099  -26.328  1.00 18.44 ? 78  ALA A C   1 
ATOM   602   O O   . ALA A 1 78  ? 29.751  23.833  -26.665  1.00 18.79 ? 78  ALA A O   1 
ATOM   603   C CB  . ALA A 1 78  ? 31.652  26.467  -26.031  1.00 19.02 ? 78  ALA A CB  1 
ATOM   604   N N   . ALA A 1 79  ? 31.943  23.460  -26.802  1.00 18.32 ? 79  ALA A N   1 
ATOM   605   C CA  . ALA A 1 79  ? 31.820  22.404  -27.805  1.00 18.13 ? 79  ALA A CA  1 
ATOM   606   C C   . ALA A 1 79  ? 30.947  21.260  -27.299  1.00 17.67 ? 79  ALA A C   1 
ATOM   607   O O   . ALA A 1 79  ? 30.059  20.791  -28.017  1.00 17.67 ? 79  ALA A O   1 
ATOM   608   C CB  . ALA A 1 79  ? 33.194  21.898  -28.192  1.00 18.18 ? 79  ALA A CB  1 
ATOM   609   N N   . LEU A 1 80  ? 31.178  20.845  -26.057  1.00 17.46 ? 80  LEU A N   1 
ATOM   610   C CA  . LEU A 1 80  ? 30.421  19.751  -25.460  1.00 18.14 ? 80  LEU A CA  1 
ATOM   611   C C   . LEU A 1 80  ? 28.918  20.032  -25.428  1.00 19.60 ? 80  LEU A C   1 
ATOM   612   O O   . LEU A 1 80  ? 28.100  19.156  -25.762  1.00 20.22 ? 80  LEU A O   1 
ATOM   613   C CB  . LEU A 1 80  ? 30.906  19.478  -24.034  1.00 17.78 ? 80  LEU A CB  1 
ATOM   614   C CG  . LEU A 1 80  ? 32.299  18.859  -23.902  1.00 17.34 ? 80  LEU A CG  1 
ATOM   615   C CD1 . LEU A 1 80  ? 32.835  19.020  -22.504  1.00 16.67 ? 80  LEU A CD1 1 
ATOM   616   C CD2 . LEU A 1 80  ? 32.284  17.395  -24.305  1.00 17.32 ? 80  LEU A CD2 1 
ATOM   617   N N   . ALA A 1 81  ? 28.573  21.257  -25.027  1.00 20.26 ? 81  ALA A N   1 
ATOM   618   C CA  . ALA A 1 81  ? 27.182  21.692  -24.892  1.00 20.24 ? 81  ALA A CA  1 
ATOM   619   C C   . ALA A 1 81  ? 26.513  21.877  -26.231  1.00 20.07 ? 81  ALA A C   1 
ATOM   620   O O   . ALA A 1 81  ? 25.296  21.752  -26.355  1.00 20.70 ? 81  ALA A O   1 
ATOM   621   C CB  . ALA A 1 81  ? 27.126  23.004  -24.115  1.00 20.89 ? 81  ALA A CB  1 
ATOM   622   N N   . ALA A 1 82  ? 27.323  22.214  -27.223  1.00 20.38 ? 82  ALA A N   1 
ATOM   623   C CA  . ALA A 1 82  ? 26.860  22.470  -28.585  1.00 21.20 ? 82  ALA A CA  1 
ATOM   624   C C   . ALA A 1 82  ? 26.554  21.182  -29.336  1.00 21.54 ? 82  ALA A C   1 
ATOM   625   O O   . ALA A 1 82  ? 25.823  21.206  -30.333  1.00 21.43 ? 82  ALA A O   1 
ATOM   626   C CB  . ALA A 1 82  ? 27.904  23.279  -29.350  1.00 20.84 ? 82  ALA A CB  1 
ATOM   627   N N   . HIS A 1 83  ? 27.133  20.069  -28.872  1.00 21.83 ? 83  HIS A N   1 
ATOM   628   C CA  . HIS A 1 83  ? 26.923  18.771  -29.508  1.00 22.09 ? 83  HIS A CA  1 
ATOM   629   C C   . HIS A 1 83  ? 26.208  17.756  -28.617  1.00 21.61 ? 83  HIS A C   1 
ATOM   630   O O   . HIS A 1 83  ? 26.024  16.609  -29.015  1.00 21.25 ? 83  HIS A O   1 
ATOM   631   C CB  . HIS A 1 83  ? 28.256  18.237  -30.004  1.00 22.96 ? 83  HIS A CB  1 
ATOM   632   C CG  . HIS A 1 83  ? 28.953  19.175  -30.936  1.00 23.69 ? 83  HIS A CG  1 
ATOM   633   N ND1 . HIS A 1 83  ? 28.329  19.719  -32.038  1.00 23.55 ? 83  HIS A ND1 1 
ATOM   634   C CD2 . HIS A 1 83  ? 30.212  19.673  -30.930  1.00 24.13 ? 83  HIS A CD2 1 
ATOM   635   C CE1 . HIS A 1 83  ? 29.181  20.498  -32.679  1.00 23.77 ? 83  HIS A CE1 1 
ATOM   636   N NE2 . HIS A 1 83  ? 30.330  20.489  -32.025  1.00 24.12 ? 83  HIS A NE2 1 
ATOM   637   N N   . GLU A 1 84  ? 25.794  18.173  -27.424  1.00 21.30 ? 84  GLU A N   1 
ATOM   638   C CA  . GLU A 1 84  ? 24.951  17.354  -26.558  1.00 21.06 ? 84  GLU A CA  1 
ATOM   639   C C   . GLU A 1 84  ? 23.677  16.930  -27.308  1.00 21.90 ? 84  GLU A C   1 
ATOM   640   O O   . GLU A 1 84  ? 23.065  17.769  -27.994  1.00 21.51 ? 84  GLU A O   1 
ATOM   641   C CB  . GLU A 1 84  ? 24.596  18.113  -25.273  1.00 20.65 ? 84  GLU A CB  1 
ATOM   642   C CG  . GLU A 1 84  ? 23.934  17.256  -24.212  1.00 20.44 ? 84  GLU A CG  1 
ATOM   643   C CD  . GLU A 1 84  ? 23.546  17.999  -22.949  1.00 19.81 ? 84  GLU A CD  1 
ATOM   644   O OE1 . GLU A 1 84  ? 23.743  17.412  -21.881  1.00 19.92 ? 84  GLU A OE1 1 
ATOM   645   O OE2 . GLU A 1 84  ? 23.014  19.117  -23.022  1.00 18.63 ? 84  GLU A OE2 1 
ATOM   646   N N   . PRO A 1 85  ? 23.253  15.658  -27.192  1.00 22.67 ? 85  PRO A N   1 
ATOM   647   C CA  . PRO A 1 85  ? 23.851  14.643  -26.327  1.00 21.56 ? 85  PRO A CA  1 
ATOM   648   C C   . PRO A 1 85  ? 24.861  13.762  -27.036  1.00 20.78 ? 85  PRO A C   1 
ATOM   649   O O   . PRO A 1 85  ? 24.676  13.427  -28.210  1.00 19.33 ? 85  PRO A O   1 
ATOM   650   C CB  . PRO A 1 85  ? 22.657  13.791  -25.936  1.00 21.79 ? 85  PRO A CB  1 
ATOM   651   C CG  . PRO A 1 85  ? 21.769  13.845  -27.121  1.00 22.21 ? 85  PRO A CG  1 
ATOM   652   C CD  . PRO A 1 85  ? 21.955  15.206  -27.728  1.00 22.91 ? 85  PRO A CD  1 
ATOM   653   N N   . LEU A 1 86  ? 25.907  13.383  -26.300  1.00 20.14 ? 86  LEU A N   1 
ATOM   654   C CA  . LEU A 1 86  ? 26.926  12.508  -26.823  1.00 19.97 ? 86  LEU A CA  1 
ATOM   655   C C   . LEU A 1 86  ? 26.994  11.218  -26.024  1.00 19.96 ? 86  LEU A C   1 
ATOM   656   O O   . LEU A 1 86  ? 26.627  11.166  -24.859  1.00 19.13 ? 86  LEU A O   1 
ATOM   657   C CB  . LEU A 1 86  ? 28.292  13.203  -26.791  1.00 19.94 ? 86  LEU A CB  1 
ATOM   658   C CG  . LEU A 1 86  ? 28.406  14.502  -27.594  1.00 19.92 ? 86  LEU A CG  1 
ATOM   659   C CD1 . LEU A 1 86  ? 29.624  15.281  -27.120  1.00 20.70 ? 86  LEU A CD1 1 
ATOM   660   C CD2 . LEU A 1 86  ? 28.449  14.236  -29.094  1.00 20.05 ? 86  LEU A CD2 1 
ATOM   661   N N   . ASP A 1 87  ? 27.446  10.166  -26.700  1.00 20.57 ? 87  ASP A N   1 
ATOM   662   C CA  . ASP A 1 87  ? 27.637  8.862   -26.095  1.00 21.01 ? 87  ASP A CA  1 
ATOM   663   C C   . ASP A 1 87  ? 29.097  8.584   -25.774  1.00 21.13 ? 87  ASP A C   1 
ATOM   664   O O   . ASP A 1 87  ? 29.382  7.742   -24.923  1.00 21.89 ? 87  ASP A O   1 
ATOM   665   C CB  . ASP A 1 87  ? 27.090  7.793   -27.019  1.00 21.61 ? 87  ASP A CB  1 
ATOM   666   C CG  . ASP A 1 87  ? 25.586  7.928   -27.209  1.00 21.94 ? 87  ASP A CG  1 
ATOM   667   O OD1 . ASP A 1 87  ? 25.191  8.800   -28.019  1.00 22.52 ? 87  ASP A OD1 1 
ATOM   668   O OD2 . ASP A 1 87  ? 24.809  7.220   -26.537  1.00 21.76 ? 87  ASP A OD2 1 
ATOM   669   N N   . LEU A 1 88  ? 30.014  9.303   -26.436  1.00 20.44 ? 88  LEU A N   1 
ATOM   670   C CA  . LEU A 1 88  ? 31.455  9.231   -26.129  1.00 20.21 ? 88  LEU A CA  1 
ATOM   671   C C   . LEU A 1 88  ? 32.223  10.494  -26.559  1.00 20.07 ? 88  LEU A C   1 
ATOM   672   O O   . LEU A 1 88  ? 31.897  11.122  -27.567  1.00 19.77 ? 88  LEU A O   1 
ATOM   673   C CB  . LEU A 1 88  ? 32.069  8.021   -26.824  1.00 20.04 ? 88  LEU A CB  1 
ATOM   674   C CG  . LEU A 1 88  ? 33.552  7.715   -26.567  1.00 20.05 ? 88  LEU A CG  1 
ATOM   675   C CD1 . LEU A 1 88  ? 33.792  7.282   -25.136  1.00 20.40 ? 88  LEU A CD1 1 
ATOM   676   C CD2 . LEU A 1 88  ? 34.056  6.663   -27.514  1.00 19.85 ? 88  LEU A CD2 1 
ATOM   677   N N   . VAL A 1 89  ? 33.243  10.856  -25.786  1.00 19.81 ? 89  VAL A N   1 
ATOM   678   C CA  . VAL A 1 89  ? 34.154  11.923  -26.161  1.00 19.95 ? 89  VAL A CA  1 
ATOM   679   C C   . VAL A 1 89  ? 35.558  11.337  -26.294  1.00 20.48 ? 89  VAL A C   1 
ATOM   680   O O   . VAL A 1 89  ? 36.074  10.733  -25.359  1.00 20.08 ? 89  VAL A O   1 
ATOM   681   C CB  . VAL A 1 89  ? 34.168  13.058  -25.122  1.00 19.65 ? 89  VAL A CB  1 
ATOM   682   C CG1 . VAL A 1 89  ? 35.230  14.093  -25.458  1.00 19.28 ? 89  VAL A CG1 1 
ATOM   683   C CG2 . VAL A 1 89  ? 32.810  13.733  -25.073  1.00 19.85 ? 89  VAL A CG2 1 
ATOM   684   N N   . ILE A 1 90  ? 36.156  11.513  -27.467  1.00 20.89 ? 90  ILE A N   1 
ATOM   685   C CA  . ILE A 1 90  ? 37.509  11.066  -27.722  1.00 20.82 ? 90  ILE A CA  1 
ATOM   686   C C   . ILE A 1 90  ? 38.402  12.285  -27.756  1.00 20.20 ? 90  ILE A C   1 
ATOM   687   O O   . ILE A 1 90  ? 38.097  13.260  -28.436  1.00 19.12 ? 90  ILE A O   1 
ATOM   688   C CB  . ILE A 1 90  ? 37.606  10.339  -29.074  1.00 21.48 ? 90  ILE A CB  1 
ATOM   689   C CG1 . ILE A 1 90  ? 36.859  9.002   -29.010  1.00 22.04 ? 90  ILE A CG1 1 
ATOM   690   C CG2 . ILE A 1 90  ? 39.066  10.121  -29.453  1.00 21.43 ? 90  ILE A CG2 1 
ATOM   691   C CD1 . ILE A 1 90  ? 36.813  8.282   -30.347  1.00 22.33 ? 90  ILE A CD1 1 
ATOM   692   N N   . ILE A 1 91  ? 39.508  12.225  -27.027  1.00 19.61 ? 91  ILE A N   1 
ATOM   693   C CA  . ILE A 1 91  ? 40.465  13.329  -26.980  1.00 18.61 ? 91  ILE A CA  1 
ATOM   694   C C   . ILE A 1 91  ? 41.786  12.782  -27.467  1.00 18.22 ? 91  ILE A C   1 
ATOM   695   O O   . ILE A 1 91  ? 42.335  11.856  -26.867  1.00 17.70 ? 91  ILE A O   1 
ATOM   696   C CB  . ILE A 1 91  ? 40.644  13.888  -25.548  1.00 18.58 ? 91  ILE A CB  1 
ATOM   697   C CG1 . ILE A 1 91  ? 39.304  14.355  -24.968  1.00 18.32 ? 91  ILE A CG1 1 
ATOM   698   C CG2 . ILE A 1 91  ? 41.674  15.012  -25.510  1.00 18.27 ? 91  ILE A CG2 1 
ATOM   699   C CD1 . ILE A 1 91  ? 39.360  14.629  -23.479  1.00 18.32 ? 91  ILE A CD1 1 
ATOM   700   N N   . LEU A 1 92  ? 42.277  13.343  -28.572  1.00 17.98 ? 92  LEU A N   1 
ATOM   701   C CA  . LEU A 1 92  ? 43.616  13.043  -29.077  1.00 17.60 ? 92  LEU A CA  1 
ATOM   702   C C   . LEU A 1 92  ? 44.374  14.363  -29.206  1.00 17.48 ? 92  LEU A C   1 
ATOM   703   O O   . LEU A 1 92  ? 44.350  15.029  -30.270  1.00 17.14 ? 92  LEU A O   1 
ATOM   704   C CB  . LEU A 1 92  ? 43.547  12.312  -30.412  1.00 17.17 ? 92  LEU A CB  1 
ATOM   705   C CG  . LEU A 1 92  ? 44.839  12.108  -31.193  1.00 16.72 ? 92  LEU A CG  1 
ATOM   706   C CD1 . LEU A 1 92  ? 45.867  11.441  -30.323  1.00 16.77 ? 92  LEU A CD1 1 
ATOM   707   C CD2 . LEU A 1 92  ? 44.549  11.281  -32.441  1.00 17.01 ? 92  LEU A CD2 1 
ATOM   708   N N   . LEU A 1 93  ? 45.011  14.721  -28.089  1.00 16.85 ? 93  LEU A N   1 
ATOM   709   C CA  . LEU A 1 93  ? 45.784  15.937  -27.930  1.00 16.80 ? 93  LEU A CA  1 
ATOM   710   C C   . LEU A 1 93  ? 47.025  15.642  -27.122  1.00 17.09 ? 93  LEU A C   1 
ATOM   711   O O   . LEU A 1 93  ? 47.098  14.623  -26.426  1.00 17.89 ? 93  LEU A O   1 
ATOM   712   C CB  . LEU A 1 93  ? 44.990  16.992  -27.166  1.00 16.33 ? 93  LEU A CB  1 
ATOM   713   C CG  . LEU A 1 93  ? 43.842  17.689  -27.877  1.00 16.06 ? 93  LEU A CG  1 
ATOM   714   C CD1 . LEU A 1 93  ? 43.062  18.530  -26.864  1.00 15.76 ? 93  LEU A CD1 1 
ATOM   715   C CD2 . LEU A 1 93  ? 44.346  18.532  -29.031  1.00 15.85 ? 93  LEU A CD2 1 
ATOM   716   N N   . GLY A 1 94  ? 47.985  16.564  -27.200  1.00 17.17 ? 94  GLY A N   1 
ATOM   717   C CA  . GLY A 1 94  ? 49.247  16.448  -26.472  1.00 16.95 ? 94  GLY A CA  1 
ATOM   718   C C   . GLY A 1 94  ? 50.479  16.655  -27.331  1.00 16.81 ? 94  GLY A C   1 
ATOM   719   O O   . GLY A 1 94  ? 51.564  16.914  -26.814  1.00 17.19 ? 94  GLY A O   1 
ATOM   720   N N   . THR A 1 95  ? 50.325  16.541  -28.645  1.00 16.94 ? 95  THR A N   1 
ATOM   721   C CA  . THR A 1 95  ? 51.458  16.681  -29.547  1.00 17.18 ? 95  THR A CA  1 
ATOM   722   C C   . THR A 1 95  ? 51.990  18.125  -29.502  1.00 17.91 ? 95  THR A C   1 
ATOM   723   O O   . THR A 1 95  ? 53.195  18.340  -29.353  1.00 18.50 ? 95  THR A O   1 
ATOM   724   C CB  . THR A 1 95  ? 51.092  16.223  -30.976  1.00 16.94 ? 95  THR A CB  1 
ATOM   725   O OG1 . THR A 1 95  ? 50.520  14.909  -30.914  1.00 17.70 ? 95  THR A OG1 1 
ATOM   726   C CG2 . THR A 1 95  ? 52.281  16.177  -31.858  1.00 16.81 ? 95  THR A CG2 1 
ATOM   727   N N   . ASN A 1 96  ? 51.102  19.117  -29.575  1.00 18.15 ? 96  ASN A N   1 
ATOM   728   C CA  . ASN A 1 96  ? 51.542  20.518  -29.492  1.00 17.71 ? 96  ASN A CA  1 
ATOM   729   C C   . ASN A 1 96  ? 52.042  20.913  -28.098  1.00 18.13 ? 96  ASN A C   1 
ATOM   730   O O   . ASN A 1 96  ? 52.844  21.827  -27.964  1.00 18.72 ? 96  ASN A O   1 
ATOM   731   C CB  . ASN A 1 96  ? 50.435  21.465  -29.915  1.00 17.16 ? 96  ASN A CB  1 
ATOM   732   C CG  . ASN A 1 96  ? 50.048  21.303  -31.374  1.00 16.52 ? 96  ASN A CG  1 
ATOM   733   O OD1 . ASN A 1 96  ? 50.837  21.586  -32.271  1.00 16.20 ? 96  ASN A OD1 1 
ATOM   734   N ND2 . ASN A 1 96  ? 48.825  20.873  -31.614  1.00 15.88 ? 96  ASN A ND2 1 
ATOM   735   N N   . ASP A 1 97  ? 51.583  20.222  -27.064  1.00 18.35 ? 97  ASP A N   1 
ATOM   736   C CA  . ASP A 1 97  ? 52.025  20.498  -25.697  1.00 18.84 ? 97  ASP A CA  1 
ATOM   737   C C   . ASP A 1 97  ? 53.523  20.244  -25.471  1.00 19.59 ? 97  ASP A C   1 
ATOM   738   O O   . ASP A 1 97  ? 54.104  20.746  -24.500  1.00 20.18 ? 97  ASP A O   1 
ATOM   739   C CB  . ASP A 1 97  ? 51.216  19.679  -24.684  1.00 19.37 ? 97  ASP A CB  1 
ATOM   740   C CG  . ASP A 1 97  ? 49.736  20.040  -24.669  1.00 19.60 ? 97  ASP A CG  1 
ATOM   741   O OD1 . ASP A 1 97  ? 49.056  19.766  -25.680  1.00 20.50 ? 97  ASP A OD1 1 
ATOM   742   O OD2 . ASP A 1 97  ? 49.243  20.571  -23.646  1.00 19.10 ? 97  ASP A OD2 1 
ATOM   743   N N   . THR A 1 98  ? 54.143  19.468  -26.361  1.00 19.85 ? 98  THR A N   1 
ATOM   744   C CA  . THR A 1 98  ? 55.580  19.178  -26.275  1.00 19.72 ? 98  THR A CA  1 
ATOM   745   C C   . THR A 1 98  ? 56.451  20.299  -26.844  1.00 18.98 ? 98  THR A C   1 
ATOM   746   O O   . THR A 1 98  ? 57.676  20.272  -26.697  1.00 19.01 ? 98  THR A O   1 
ATOM   747   C CB  . THR A 1 98  ? 55.921  17.881  -27.021  1.00 20.17 ? 98  THR A CB  1 
ATOM   748   O OG1 . THR A 1 98  ? 55.737  18.075  -28.429  1.00 20.76 ? 98  THR A OG1 1 
ATOM   749   C CG2 . THR A 1 98  ? 55.037  16.719  -26.533  1.00 20.19 ? 98  THR A CG2 1 
ATOM   750   N N   . LYS A 1 99  ? 55.824  21.277  -27.498  1.00 18.59 ? 99  LYS A N   1 
ATOM   751   C CA  . LYS A 1 99  ? 56.544  22.441  -28.022  1.00 18.15 ? 99  LYS A CA  1 
ATOM   752   C C   . LYS A 1 99  ? 57.383  23.088  -26.930  1.00 17.01 ? 99  LYS A C   1 
ATOM   753   O O   . LYS A 1 99  ? 56.907  23.354  -25.831  1.00 16.10 ? 99  LYS A O   1 
ATOM   754   C CB  . LYS A 1 99  ? 55.602  23.484  -28.644  1.00 18.56 ? 99  LYS A CB  1 
ATOM   755   C CG  . LYS A 1 99  ? 55.025  23.084  -29.991  1.00 18.73 ? 99  LYS A CG  1 
ATOM   756   C CD  . LYS A 1 99  ? 53.971  24.047  -30.521  1.00 18.90 ? 99  LYS A CD  1 
ATOM   757   C CE  . LYS A 1 99  ? 53.640  23.693  -31.970  1.00 19.78 ? 99  LYS A CE  1 
ATOM   758   N NZ  . LYS A 1 99  ? 52.338  24.225  -32.462  1.00 20.58 ? 99  LYS A NZ  1 
ATOM   759   N N   . THR A 1 100 ? 58.637  23.323  -27.278  1.00 16.88 ? 100 THR A N   1 
ATOM   760   C CA  . THR A 1 100 ? 59.654  23.836  -26.386  1.00 16.94 ? 100 THR A CA  1 
ATOM   761   C C   . THR A 1 100 ? 59.205  25.025  -25.540  1.00 16.67 ? 100 THR A C   1 
ATOM   762   O O   . THR A 1 100 ? 59.325  25.022  -24.328  1.00 16.30 ? 100 THR A O   1 
ATOM   763   C CB  . THR A 1 100 ? 60.926  24.229  -27.213  1.00 17.31 ? 100 THR A CB  1 
ATOM   764   O OG1 . THR A 1 100 ? 61.666  23.058  -27.575  1.00 17.32 ? 100 THR A OG1 1 
ATOM   765   C CG2 . THR A 1 100 ? 61.841  25.181  -26.402  1.00 17.60 ? 100 THR A CG2 1 
ATOM   766   N N   . TYR A 1 101 ? 58.683  26.047  -26.202  1.00 16.38 ? 101 TYR A N   1 
ATOM   767   C CA  . TYR A 1 101 ? 58.351  27.315  -25.554  1.00 15.93 ? 101 TYR A CA  1 
ATOM   768   C C   . TYR A 1 101 ? 57.206  27.225  -24.554  1.00 16.97 ? 101 TYR A C   1 
ATOM   769   O O   . TYR A 1 101 ? 57.053  28.122  -23.747  1.00 18.58 ? 101 TYR A O   1 
ATOM   770   C CB  . TYR A 1 101 ? 58.093  28.421  -26.590  1.00 15.25 ? 101 TYR A CB  1 
ATOM   771   C CG  . TYR A 1 101 ? 56.979  28.172  -27.580  1.00 14.86 ? 101 TYR A CG  1 
ATOM   772   C CD1 . TYR A 1 101 ? 55.644  28.366  -27.229  1.00 14.96 ? 101 TYR A CD1 1 
ATOM   773   C CD2 . TYR A 1 101 ? 57.252  27.780  -28.884  1.00 14.64 ? 101 TYR A CD2 1 
ATOM   774   C CE1 . TYR A 1 101 ? 54.614  28.153  -28.154  1.00 14.31 ? 101 TYR A CE1 1 
ATOM   775   C CE2 . TYR A 1 101 ? 56.227  27.573  -29.804  1.00 14.50 ? 101 TYR A CE2 1 
ATOM   776   C CZ  . TYR A 1 101 ? 54.916  27.764  -29.431  1.00 13.98 ? 101 TYR A CZ  1 
ATOM   777   O OH  . TYR A 1 101 ? 53.927  27.552  -30.344  1.00 13.10 ? 101 TYR A OH  1 
ATOM   778   N N   . LEU A 1 102 ? 56.399  26.173  -24.584  1.00 18.07 ? 102 LEU A N   1 
ATOM   779   C CA  . LEU A 1 102 ? 55.346  25.988  -23.576  1.00 18.70 ? 102 LEU A CA  1 
ATOM   780   C C   . LEU A 1 102 ? 55.899  25.399  -22.287  1.00 19.37 ? 102 LEU A C   1 
ATOM   781   O O   . LEU A 1 102 ? 55.233  25.413  -21.252  1.00 18.88 ? 102 LEU A O   1 
ATOM   782   C CB  . LEU A 1 102 ? 54.238  25.081  -24.121  1.00 19.11 ? 102 LEU A CB  1 
ATOM   783   C CG  . LEU A 1 102 ? 53.576  25.563  -25.418  1.00 18.97 ? 102 LEU A CG  1 
ATOM   784   C CD1 . LEU A 1 102 ? 52.649  24.481  -25.921  1.00 18.69 ? 102 LEU A CD1 1 
ATOM   785   C CD2 . LEU A 1 102 ? 52.819  26.860  -25.194  1.00 18.97 ? 102 LEU A CD2 1 
ATOM   786   N N   . ASN A 1 103 ? 57.107  24.848  -22.357  1.00 21.02 ? 103 ASN A N   1 
ATOM   787   C CA  . ASN A 1 103 ? 57.868  24.486  -21.162  1.00 22.58 ? 103 ASN A CA  1 
ATOM   788   C C   . ASN A 1 103 ? 57.128  23.492  -20.245  1.00 22.17 ? 103 ASN A C   1 
ATOM   789   O O   . ASN A 1 103 ? 57.140  23.629  -19.021  1.00 22.80 ? 103 ASN A O   1 
ATOM   790   C CB  . ASN A 1 103 ? 58.261  25.773  -20.423  1.00 23.39 ? 103 ASN A CB  1 
ATOM   791   C CG  . ASN A 1 103 ? 59.182  25.517  -19.256  1.00 25.01 ? 103 ASN A CG  1 
ATOM   792   O OD1 . ASN A 1 103 ? 60.270  24.928  -19.408  1.00 26.28 ? 103 ASN A OD1 1 
ATOM   793   N ND2 . ASN A 1 103 ? 58.746  25.945  -18.063  1.00 25.90 ? 103 ASN A ND2 1 
ATOM   794   N N   . ARG A 1 104 ? 56.498  22.477  -20.840  1.00 20.80 ? 104 ARG A N   1 
ATOM   795   C CA  . ARG A 1 104 ? 55.722  21.508  -20.078  1.00 19.41 ? 104 ARG A CA  1 
ATOM   796   C C   . ARG A 1 104 ? 56.452  20.191  -19.855  1.00 18.52 ? 104 ARG A C   1 
ATOM   797   O O   . ARG A 1 104 ? 57.175  19.715  -20.716  1.00 17.66 ? 104 ARG A O   1 
ATOM   798   C CB  . ARG A 1 104 ? 54.407  21.202  -20.787  1.00 19.42 ? 104 ARG A CB  1 
ATOM   799   C CG  . ARG A 1 104 ? 53.719  22.377  -21.442  1.00 19.02 ? 104 ARG A CG  1 
ATOM   800   C CD  . ARG A 1 104 ? 52.228  22.133  -21.577  1.00 18.32 ? 104 ARG A CD  1 
ATOM   801   N NE  . ARG A 1 104 ? 51.500  22.443  -20.350  1.00 17.81 ? 104 ARG A NE  1 
ATOM   802   C CZ  . ARG A 1 104 ? 50.195  22.252  -20.168  1.00 18.00 ? 104 ARG A CZ  1 
ATOM   803   N NH1 . ARG A 1 104 ? 49.433  21.740  -21.124  1.00 18.41 ? 104 ARG A NH1 1 
ATOM   804   N NH2 . ARG A 1 104 ? 49.642  22.566  -19.020  1.00 18.18 ? 104 ARG A NH2 1 
ATOM   805   N N   . THR A 1 105 ? 56.227  19.609  -18.681  1.00 18.13 ? 105 THR A N   1 
ATOM   806   C CA  . THR A 1 105 ? 56.668  18.258  -18.395  1.00 17.76 ? 105 THR A CA  1 
ATOM   807   C C   . THR A 1 105 ? 55.551  17.331  -18.832  1.00 17.73 ? 105 THR A C   1 
ATOM   808   O O   . THR A 1 105 ? 54.417  17.780  -19.001  1.00 18.29 ? 105 THR A O   1 
ATOM   809   C CB  . THR A 1 105 ? 56.899  18.046  -16.899  1.00 17.61 ? 105 THR A CB  1 
ATOM   810   O OG1 . THR A 1 105 ? 55.631  18.066  -16.207  1.00 17.59 ? 105 THR A OG1 1 
ATOM   811   C CG2 . THR A 1 105 ? 57.848  19.124  -16.366  1.00 17.40 ? 105 THR A CG2 1 
ATOM   812   N N   . PRO A 1 106 ? 55.853  16.033  -19.018  1.00 16.97 ? 106 PRO A N   1 
ATOM   813   C CA  . PRO A 1 106 ? 54.801  15.065  -19.362  1.00 16.64 ? 106 PRO A CA  1 
ATOM   814   C C   . PRO A 1 106 ? 53.689  14.983  -18.326  1.00 16.13 ? 106 PRO A C   1 
ATOM   815   O O   . PRO A 1 106 ? 52.532  14.876  -18.697  1.00 16.25 ? 106 PRO A O   1 
ATOM   816   C CB  . PRO A 1 106 ? 55.555  13.740  -19.429  1.00 16.91 ? 106 PRO A CB  1 
ATOM   817   C CG  . PRO A 1 106 ? 56.955  14.132  -19.776  1.00 16.81 ? 106 PRO A CG  1 
ATOM   818   C CD  . PRO A 1 106 ? 57.196  15.440  -19.095  1.00 16.66 ? 106 PRO A CD  1 
ATOM   819   N N   . PHE A 1 107 ? 54.034  15.033  -17.043  1.00 16.17 ? 107 PHE A N   1 
ATOM   820   C CA  . PHE A 1 107 ? 53.037  15.021  -15.970  1.00 16.32 ? 107 PHE A CA  1 
ATOM   821   C C   . PHE A 1 107 ? 52.119  16.239  -16.092  1.00 16.90 ? 107 PHE A C   1 
ATOM   822   O O   . PHE A 1 107 ? 50.901  16.134  -15.926  1.00 17.26 ? 107 PHE A O   1 
ATOM   823   C CB  . PHE A 1 107 ? 53.698  14.981  -14.592  1.00 16.15 ? 107 PHE A CB  1 
ATOM   824   C CG  . PHE A 1 107 ? 52.722  15.041  -13.447  1.00 15.70 ? 107 PHE A CG  1 
ATOM   825   C CD1 . PHE A 1 107 ? 51.843  14.005  -13.228  1.00 16.07 ? 107 PHE A CD1 1 
ATOM   826   C CD2 . PHE A 1 107 ? 52.693  16.124  -12.586  1.00 15.51 ? 107 PHE A CD2 1 
ATOM   827   C CE1 . PHE A 1 107 ? 50.949  14.042  -12.158  1.00 16.54 ? 107 PHE A CE1 1 
ATOM   828   C CE2 . PHE A 1 107 ? 51.793  16.177  -11.536  1.00 15.86 ? 107 PHE A CE2 1 
ATOM   829   C CZ  . PHE A 1 107 ? 50.921  15.137  -11.312  1.00 15.92 ? 107 PHE A CZ  1 
ATOM   830   N N   . GLU A 1 108 ? 52.706  17.398  -16.396  1.00 16.89 ? 108 GLU A N   1 
ATOM   831   C CA  . GLU A 1 108 ? 51.919  18.593  -16.588  1.00 16.67 ? 108 GLU A CA  1 
ATOM   832   C C   . GLU A 1 108 ? 50.920  18.410  -17.734  1.00 17.04 ? 108 GLU A C   1 
ATOM   833   O O   . GLU A 1 108 ? 49.784  18.870  -17.656  1.00 17.06 ? 108 GLU A O   1 
ATOM   834   C CB  . GLU A 1 108 ? 52.827  19.774  -16.899  1.00 16.58 ? 108 GLU A CB  1 
ATOM   835   C CG  . GLU A 1 108 ? 52.068  21.092  -16.998  1.00 16.00 ? 108 GLU A CG  1 
ATOM   836   C CD  . GLU A 1 108 ? 52.992  22.261  -17.162  1.00 15.67 ? 108 GLU A CD  1 
ATOM   837   O OE1 . GLU A 1 108 ? 52.805  23.035  -18.103  1.00 16.04 ? 108 GLU A OE1 1 
ATOM   838   O OE2 . GLU A 1 108 ? 53.959  22.378  -16.392  1.00 15.48 ? 108 GLU A OE2 1 
ATOM   839   N N   . ILE A 1 109 ? 51.362  17.751  -18.799  1.00 16.93 ? 109 ILE A N   1 
ATOM   840   C CA  . ILE A 1 109 ? 50.531  17.556  -19.976  1.00 16.72 ? 109 ILE A CA  1 
ATOM   841   C C   . ILE A 1 109 ? 49.405  16.579  -19.638  1.00 16.73 ? 109 ILE A C   1 
ATOM   842   O O   . ILE A 1 109 ? 48.267  16.768  -20.066  1.00 16.89 ? 109 ILE A O   1 
ATOM   843   C CB  . ILE A 1 109 ? 51.361  17.061  -21.185  1.00 16.66 ? 109 ILE A CB  1 
ATOM   844   C CG1 . ILE A 1 109 ? 52.447  18.088  -21.541  1.00 16.31 ? 109 ILE A CG1 1 
ATOM   845   C CG2 . ILE A 1 109 ? 50.460  16.833  -22.389  1.00 16.95 ? 109 ILE A CG2 1 
ATOM   846   C CD1 . ILE A 1 109 ? 53.535  17.588  -22.468  1.00 15.97 ? 109 ILE A CD1 1 
ATOM   847   N N   . GLY A 1 110 ? 49.718  15.554  -18.852  1.00 16.57 ? 110 GLY A N   1 
ATOM   848   C CA  . GLY A 1 110 ? 48.692  14.682  -18.305  1.00 16.81 ? 110 GLY A CA  1 
ATOM   849   C C   . GLY A 1 110 ? 47.613  15.435  -17.541  1.00 17.40 ? 110 GLY A C   1 
ATOM   850   O O   . GLY A 1 110 ? 46.417  15.217  -17.739  1.00 16.94 ? 110 GLY A O   1 
ATOM   851   N N   . LEU A 1 111 ? 48.041  16.324  -16.654  1.00 18.41 ? 111 LEU A N   1 
ATOM   852   C CA  . LEU A 1 111 ? 47.111  17.162  -15.888  1.00 18.42 ? 111 LEU A CA  1 
ATOM   853   C C   . LEU A 1 111 ? 46.217  17.992  -16.822  1.00 19.07 ? 111 LEU A C   1 
ATOM   854   O O   . LEU A 1 111 ? 45.031  18.207  -16.538  1.00 19.17 ? 111 LEU A O   1 
ATOM   855   C CB  . LEU A 1 111 ? 47.875  18.083  -14.945  1.00 17.83 ? 111 LEU A CB  1 
ATOM   856   C CG  . LEU A 1 111 ? 48.555  17.371  -13.765  1.00 17.83 ? 111 LEU A CG  1 
ATOM   857   C CD1 . LEU A 1 111 ? 49.332  18.397  -12.957  1.00 18.03 ? 111 LEU A CD1 1 
ATOM   858   C CD2 . LEU A 1 111 ? 47.574  16.623  -12.882  1.00 18.02 ? 111 LEU A CD2 1 
ATOM   859   N N   . GLY A 1 112 ? 46.794  18.449  -17.931  1.00 18.98 ? 112 GLY A N   1 
ATOM   860   C CA  . GLY A 1 112 ? 46.061  19.206  -18.934  1.00 18.97 ? 112 GLY A CA  1 
ATOM   861   C C   . GLY A 1 112 ? 44.968  18.370  -19.556  1.00 19.08 ? 112 GLY A C   1 
ATOM   862   O O   . GLY A 1 112 ? 43.820  18.813  -19.668  1.00 20.49 ? 112 GLY A O   1 
ATOM   863   N N   . ALA A 1 113 ? 45.321  17.149  -19.950  1.00 18.52 ? 113 ALA A N   1 
ATOM   864   C CA  . ALA A 1 113 ? 44.344  16.209  -20.469  1.00 18.35 ? 113 ALA A CA  1 
ATOM   865   C C   . ALA A 1 113 ? 43.308  15.921  -19.405  1.00 18.63 ? 113 ALA A C   1 
ATOM   866   O O   . ALA A 1 113 ? 42.121  15.844  -19.708  1.00 19.05 ? 113 ALA A O   1 
ATOM   867   C CB  . ALA A 1 113 ? 45.016  14.930  -20.928  1.00 18.41 ? 113 ALA A CB  1 
ATOM   868   N N   . GLY A 1 114 ? 43.759  15.775  -18.157  1.00 18.78 ? 114 GLY A N   1 
ATOM   869   C CA  . GLY A 1 114 ? 42.851  15.622  -17.014  1.00 19.41 ? 114 GLY A CA  1 
ATOM   870   C C   . GLY A 1 114 ? 41.847  16.754  -16.853  1.00 19.71 ? 114 GLY A C   1 
ATOM   871   O O   . GLY A 1 114 ? 40.666  16.515  -16.581  1.00 20.37 ? 114 GLY A O   1 
ATOM   872   N N   . ALA A 1 115 ? 42.319  17.987  -17.024  1.00 19.58 ? 115 ALA A N   1 
ATOM   873   C CA  . ALA A 1 115 ? 41.442  19.153  -16.992  1.00 19.44 ? 115 ALA A CA  1 
ATOM   874   C C   . ALA A 1 115 ? 40.314  19.022  -18.006  1.00 19.17 ? 115 ALA A C   1 
ATOM   875   O O   . ALA A 1 115 ? 39.173  19.405  -17.718  1.00 19.09 ? 115 ALA A O   1 
ATOM   876   C CB  . ALA A 1 115 ? 42.233  20.427  -17.256  1.00 19.52 ? 115 ALA A CB  1 
ATOM   877   N N   . LEU A 1 116 ? 40.641  18.497  -19.184  1.00 18.77 ? 116 LEU A N   1 
ATOM   878   C CA  . LEU A 1 116 ? 39.641  18.314  -20.227  1.00 18.80 ? 116 LEU A CA  1 
ATOM   879   C C   . LEU A 1 116 ? 38.650  17.200  -19.856  1.00 19.02 ? 116 LEU A C   1 
ATOM   880   O O   . LEU A 1 116 ? 37.446  17.366  -20.026  1.00 20.56 ? 116 LEU A O   1 
ATOM   881   C CB  . LEU A 1 116 ? 40.299  18.029  -21.587  1.00 18.35 ? 116 LEU A CB  1 
ATOM   882   C CG  . LEU A 1 116 ? 41.189  19.140  -22.147  1.00 18.10 ? 116 LEU A CG  1 
ATOM   883   C CD1 . LEU A 1 116 ? 41.781  18.747  -23.489  1.00 18.26 ? 116 LEU A CD1 1 
ATOM   884   C CD2 . LEU A 1 116 ? 40.411  20.431  -22.313  1.00 18.34 ? 116 LEU A CD2 1 
ATOM   885   N N   . ILE A 1 117 ? 39.153  16.089  -19.324  1.00 18.35 ? 117 ILE A N   1 
ATOM   886   C CA  . ILE A 1 117 ? 38.283  15.006  -18.878  1.00 18.10 ? 117 ILE A CA  1 
ATOM   887   C C   . ILE A 1 117 ? 37.283  15.534  -17.839  1.00 17.95 ? 117 ILE A C   1 
ATOM   888   O O   . ILE A 1 117 ? 36.085  15.256  -17.904  1.00 18.07 ? 117 ILE A O   1 
ATOM   889   C CB  . ILE A 1 117 ? 39.079  13.824  -18.265  1.00 18.31 ? 117 ILE A CB  1 
ATOM   890   C CG1 . ILE A 1 117 ? 39.920  13.107  -19.316  1.00 18.05 ? 117 ILE A CG1 1 
ATOM   891   C CG2 . ILE A 1 117 ? 38.125  12.811  -17.640  1.00 18.31 ? 117 ILE A CG2 1 
ATOM   892   C CD1 . ILE A 1 117 ? 41.018  12.246  -18.732  1.00 17.91 ? 117 ILE A CD1 1 
ATOM   893   N N   . ASN A 1 118 ? 37.789  16.304  -16.883  1.00 17.79 ? 118 ASN A N   1 
ATOM   894   C CA  . ASN A 1 118 ? 36.946  16.924  -15.871  1.00 17.50 ? 118 ASN A CA  1 
ATOM   895   C C   . ASN A 1 118 ? 35.859  17.836  -16.480  1.00 17.60 ? 118 ASN A C   1 
ATOM   896   O O   . ASN A 1 118 ? 34.713  17.823  -16.018  1.00 18.18 ? 118 ASN A O   1 
ATOM   897   C CB  . ASN A 1 118 ? 37.817  17.696  -14.885  1.00 17.34 ? 118 ASN A CB  1 
ATOM   898   C CG  . ASN A 1 118 ? 37.046  18.319  -13.745  1.00 16.90 ? 118 ASN A CG  1 
ATOM   899   O OD1 . ASN A 1 118 ? 36.949  19.515  -13.736  1.00 15.76 ? 118 ASN A OD1 1 
ATOM   900   N ND2 . ASN A 1 118 ? 36.506  17.530  -12.796  1.00 17.61 ? 118 ASN A ND2 1 
ATOM   901   N N   . MET A 1 119 ? 36.206  18.615  -17.503  1.00 16.95 ? 119 MET A N   1 
ATOM   902   C CA  . MET A 1 119 ? 35.203  19.436  -18.170  1.00 17.00 ? 119 MET A CA  1 
ATOM   903   C C   . MET A 1 119 ? 34.080  18.583  -18.779  1.00 17.36 ? 119 MET A C   1 
ATOM   904   O O   . MET A 1 119 ? 32.897  18.958  -18.729  1.00 17.49 ? 119 MET A O   1 
ATOM   905   C CB  . MET A 1 119 ? 35.845  20.316  -19.235  1.00 17.08 ? 119 MET A CB  1 
ATOM   906   C CG  . MET A 1 119 ? 36.596  21.507  -18.644  1.00 16.70 ? 119 MET A CG  1 
ATOM   907   S SD  . MET A 1 119 ? 37.655  22.297  -19.880  1.00 16.38 ? 119 MET A SD  1 
ATOM   908   C CE  . MET A 1 119 ? 37.853  23.903  -19.135  1.00 16.94 ? 119 MET A CE  1 
ATOM   909   N N   . VAL A 1 120 ? 34.448  17.431  -19.335  1.00 17.36 ? 120 VAL A N   1 
ATOM   910   C CA  . VAL A 1 120 ? 33.471  16.497  -19.885  1.00 17.75 ? 120 VAL A CA  1 
ATOM   911   C C   . VAL A 1 120 ? 32.594  15.911  -18.776  1.00 18.09 ? 120 VAL A C   1 
ATOM   912   O O   . VAL A 1 120 ? 31.397  15.741  -18.960  1.00 18.07 ? 120 VAL A O   1 
ATOM   913   C CB  . VAL A 1 120 ? 34.144  15.337  -20.664  1.00 17.75 ? 120 VAL A CB  1 
ATOM   914   C CG1 . VAL A 1 120 ? 33.093  14.367  -21.195  1.00 17.74 ? 120 VAL A CG1 1 
ATOM   915   C CG2 . VAL A 1 120 ? 35.003  15.865  -21.806  1.00 17.74 ? 120 VAL A CG2 1 
ATOM   916   N N   . GLN A 1 121 ? 33.194  15.592  -17.632  1.00 18.58 ? 121 GLN A N   1 
ATOM   917   C CA  . GLN A 1 121 ? 32.453  14.987  -16.522  1.00 18.76 ? 121 GLN A CA  1 
ATOM   918   C C   . GLN A 1 121 ? 31.459  15.943  -15.882  1.00 19.19 ? 121 GLN A C   1 
ATOM   919   O O   . GLN A 1 121 ? 30.405  15.528  -15.409  1.00 18.85 ? 121 GLN A O   1 
ATOM   920   C CB  . GLN A 1 121 ? 33.412  14.426  -15.471  1.00 18.35 ? 121 GLN A CB  1 
ATOM   921   C CG  . GLN A 1 121 ? 34.148  13.188  -15.965  1.00 17.90 ? 121 GLN A CG  1 
ATOM   922   C CD  . GLN A 1 121 ? 35.069  12.615  -14.923  1.00 17.35 ? 121 GLN A CD  1 
ATOM   923   O OE1 . GLN A 1 121 ? 35.368  13.254  -13.916  1.00 16.92 ? 121 GLN A OE1 1 
ATOM   924   N NE2 . GLN A 1 121 ? 35.553  11.413  -15.177  1.00 17.36 ? 121 GLN A NE2 1 
ATOM   925   N N   . LYS A 1 122 ? 31.798  17.228  -15.882  1.00 20.63 ? 122 LYS A N   1 
ATOM   926   C CA  . LYS A 1 122 ? 30.903  18.274  -15.393  1.00 21.42 ? 122 LYS A CA  1 
ATOM   927   C C   . LYS A 1 122 ? 30.073  18.886  -16.533  1.00 22.34 ? 122 LYS A C   1 
ATOM   928   O O   . LYS A 1 122 ? 29.460  19.919  -16.361  1.00 20.78 ? 122 LYS A O   1 
ATOM   929   C CB  . LYS A 1 122 ? 31.725  19.353  -14.720  1.00 21.44 ? 122 LYS A CB  1 
ATOM   930   C CG  . LYS A 1 122 ? 32.595  18.807  -13.576  1.00 21.50 ? 122 LYS A CG  1 
ATOM   931   C CD  . LYS A 1 122 ? 33.510  19.838  -12.958  1.00 20.75 ? 122 LYS A CD  1 
ATOM   932   C CE  . LYS A 1 122 ? 32.767  20.873  -12.128  1.00 20.43 ? 122 LYS A CE  1 
ATOM   933   N NZ  . LYS A 1 122 ? 33.535  22.148  -12.064  1.00 20.57 ? 122 LYS A NZ  1 
ATOM   934   N N   . SER A 1 123 ? 30.044  18.208  -17.679  1.00 25.15 ? 123 SER A N   1 
ATOM   935   C CA  . SER A 1 123 ? 29.439  18.712  -18.910  1.00 26.18 ? 123 SER A CA  1 
ATOM   936   C C   . SER A 1 123 ? 27.936  18.930  -18.775  1.00 28.04 ? 123 SER A C   1 
ATOM   937   O O   . SER A 1 123 ? 27.281  18.197  -18.032  1.00 28.37 ? 123 SER A O   1 
ATOM   938   C CB  . SER A 1 123 ? 29.693  17.740  -20.047  1.00 26.84 ? 123 SER A CB  1 
ATOM   939   O OG  . SER A 1 123 ? 29.853  18.449  -21.237  1.00 27.44 ? 123 SER A OG  1 
ATOM   940   N N   . PRO A 1 124 ? 27.374  19.755  -19.677  1.00 29.32 ? 124 PRO A N   1 
ATOM   941   C CA  . PRO A 1 124 ? 26.720  21.070  -19.569  1.00 28.61 ? 124 PRO A CA  1 
ATOM   942   C C   . PRO A 1 124 ? 26.723  21.531  -18.133  1.00 30.11 ? 124 PRO A C   1 
ATOM   943   O O   . PRO A 1 124 ? 26.540  20.727  -17.230  1.00 34.87 ? 124 PRO A O   1 
ATOM   944   C CB  . PRO A 1 124 ? 25.282  20.809  -20.026  1.00 27.89 ? 124 PRO A CB  1 
ATOM   945   C CG  . PRO A 1 124 ? 25.104  19.327  -19.864  1.00 27.35 ? 124 PRO A CG  1 
ATOM   946   C CD  . PRO A 1 124 ? 26.450  18.834  -20.367  1.00 29.15 ? 124 PRO A CD  1 
ATOM   947   N N   . GLY A 1 125 ? 26.897  22.808  -17.870  1.00 27.73 ? 125 GLY A N   1 
ATOM   948   C CA  . GLY A 1 125 ? 26.770  23.220  -16.494  1.00 27.08 ? 125 GLY A CA  1 
ATOM   949   C C   . GLY A 1 125 ? 25.364  23.646  -16.126  1.00 26.51 ? 125 GLY A C   1 
ATOM   950   O O   . GLY A 1 125 ? 25.227  24.667  -15.432  1.00 30.18 ? 125 GLY A O   1 
ATOM   951   N N   . TRP A 1 126 ? 24.321  22.928  -16.548  1.00 24.72 ? 126 TRP A N   1 
ATOM   952   C CA  . TRP A 1 126 ? 22.984  23.544  -16.473  1.00 25.43 ? 126 TRP A CA  1 
ATOM   953   C C   . TRP A 1 126 ? 21.710  22.690  -16.382  1.00 27.88 ? 126 TRP A C   1 
ATOM   954   O O   . TRP A 1 126 ? 21.712  21.506  -16.682  1.00 28.55 ? 126 TRP A O   1 
ATOM   955   C CB  . TRP A 1 126 ? 22.814  24.554  -17.630  1.00 24.21 ? 126 TRP A CB  1 
ATOM   956   C CG  . TRP A 1 126 ? 22.860  23.982  -19.035  1.00 23.26 ? 126 TRP A CG  1 
ATOM   957   C CD1 . TRP A 1 126 ? 22.348  22.787  -19.471  1.00 22.33 ? 126 TRP A CD1 1 
ATOM   958   C CD2 . TRP A 1 126 ? 23.408  24.622  -20.195  1.00 22.51 ? 126 TRP A CD2 1 
ATOM   959   N NE1 . TRP A 1 126 ? 22.573  22.636  -20.819  1.00 21.13 ? 126 TRP A NE1 1 
ATOM   960   C CE2 . TRP A 1 126 ? 23.215  23.747  -21.288  1.00 21.76 ? 126 TRP A CE2 1 
ATOM   961   C CE3 . TRP A 1 126 ? 24.049  25.851  -20.415  1.00 22.32 ? 126 TRP A CE3 1 
ATOM   962   C CZ2 . TRP A 1 126 ? 23.638  24.065  -22.581  1.00 21.64 ? 126 TRP A CZ2 1 
ATOM   963   C CZ3 . TRP A 1 126 ? 24.465  26.165  -21.709  1.00 21.43 ? 126 TRP A CZ3 1 
ATOM   964   C CH2 . TRP A 1 126 ? 24.258  25.276  -22.768  1.00 21.29 ? 126 TRP A CH2 1 
ATOM   965   N N   . ASP A 1 127 ? 20.641  23.365  -15.924  1.00 30.71 ? 127 ASP A N   1 
ATOM   966   C CA  . ASP A 1 127 ? 19.260  22.917  -15.879  1.00 31.59 ? 127 ASP A CA  1 
ATOM   967   C C   . ASP A 1 127 ? 18.553  22.764  -17.246  1.00 28.56 ? 127 ASP A C   1 
ATOM   968   O O   . ASP A 1 127 ? 17.470  22.208  -17.337  1.00 28.94 ? 127 ASP A O   1 
ATOM   969   C CB  . ASP A 1 127 ? 18.415  24.074  -15.281  1.00 36.82 ? 127 ASP A CB  1 
ATOM   970   C CG  . ASP A 1 127 ? 18.666  24.358  -13.807  1.00 43.26 ? 127 ASP A CG  1 
ATOM   971   O OD1 . ASP A 1 127 ? 19.695  23.916  -13.253  1.00 52.03 ? 127 ASP A OD1 1 
ATOM   972   O OD2 . ASP A 1 127 ? 17.798  25.067  -13.214  1.00 42.18 ? 127 ASP A OD2 1 
ATOM   973   N N   . TRP A 1 128 ? 19.117  23.408  -18.265  1.00 25.49 ? 128 TRP A N   1 
ATOM   974   C CA  . TRP A 1 128 ? 18.412  23.602  -19.541  1.00 24.15 ? 128 TRP A CA  1 
ATOM   975   C C   . TRP A 1 128 ? 18.137  22.292  -20.281  1.00 23.26 ? 128 TRP A C   1 
ATOM   976   O O   . TRP A 1 128 ? 17.169  22.179  -21.025  1.00 22.22 ? 128 TRP A O   1 
ATOM   977   C CB  . TRP A 1 128 ? 19.197  24.560  -20.444  1.00 23.83 ? 128 TRP A CB  1 
ATOM   978   C CG  . TRP A 1 128 ? 19.345  25.964  -19.881  1.00 22.27 ? 128 TRP A CG  1 
ATOM   979   C CD1 . TRP A 1 128 ? 18.716  26.473  -18.794  1.00 21.54 ? 128 TRP A CD1 1 
ATOM   980   C CD2 . TRP A 1 128 ? 20.159  27.029  -20.409  1.00 21.13 ? 128 TRP A CD2 1 
ATOM   981   N NE1 . TRP A 1 128 ? 19.097  27.768  -18.590  1.00 21.40 ? 128 TRP A NE1 1 
ATOM   982   C CE2 . TRP A 1 128 ? 19.971  28.144  -19.574  1.00 20.90 ? 128 TRP A CE2 1 
ATOM   983   C CE3 . TRP A 1 128 ? 21.014  27.149  -21.510  1.00 20.82 ? 128 TRP A CE3 1 
ATOM   984   C CZ2 . TRP A 1 128 ? 20.613  29.371  -19.794  1.00 20.26 ? 128 TRP A CZ2 1 
ATOM   985   C CZ3 . TRP A 1 128 ? 21.650  28.367  -21.726  1.00 20.86 ? 128 TRP A CZ3 1 
ATOM   986   C CH2 . TRP A 1 128 ? 21.444  29.462  -20.865  1.00 20.16 ? 128 TRP A CH2 1 
ATOM   987   N N   . THR A 1 129 ? 19.017  21.318  -20.082  1.00 22.78 ? 129 THR A N   1 
ATOM   988   C CA  . THR A 1 129 ? 18.851  19.961  -20.572  1.00 22.83 ? 129 THR A CA  1 
ATOM   989   C C   . THR A 1 129 ? 19.155  19.062  -19.391  1.00 21.93 ? 129 THR A C   1 
ATOM   990   O O   . THR A 1 129 ? 19.825  19.491  -18.455  1.00 21.67 ? 129 THR A O   1 
ATOM   991   C CB  . THR A 1 129 ? 19.845  19.635  -21.712  1.00 23.65 ? 129 THR A CB  1 
ATOM   992   O OG1 . THR A 1 129 ? 21.208  19.748  -21.260  1.00 23.78 ? 129 THR A OG1 1 
ATOM   993   C CG2 . THR A 1 129 ? 19.628  20.543  -22.903  1.00 24.53 ? 129 THR A CG2 1 
ATOM   994   N N   . ASP A 1 130 ? 18.676  17.825  -19.401  1.00 21.51 ? 130 ASP A N   1 
ATOM   995   C CA  . ASP A 1 130 ? 19.330  16.837  -18.544  1.00 22.30 ? 130 ASP A CA  1 
ATOM   996   C C   . ASP A 1 130 ? 19.514  15.494  -19.220  1.00 20.72 ? 130 ASP A C   1 
ATOM   997   O O   . ASP A 1 130 ? 18.735  14.568  -19.080  1.00 21.04 ? 130 ASP A O   1 
ATOM   998   C CB  . ASP A 1 130 ? 18.754  16.802  -17.090  1.00 23.96 ? 130 ASP A CB  1 
ATOM   999   C CG  . ASP A 1 130 ? 17.767  15.687  -16.837  1.00 25.00 ? 130 ASP A CG  1 
ATOM   1000  O OD1 . ASP A 1 130 ? 16.669  15.713  -17.416  1.00 26.96 ? 130 ASP A OD1 1 
ATOM   1001  O OD2 . ASP A 1 130 ? 18.078  14.802  -16.017  1.00 27.19 ? 130 ASP A OD2 1 
ATOM   1002  N N   . TYR A 1 131 ? 20.571  15.470  -20.021  1.00 19.51 ? 131 TYR A N   1 
ATOM   1003  C CA  . TYR A 1 131 ? 21.195  14.258  -20.487  1.00 18.71 ? 131 TYR A CA  1 
ATOM   1004  C C   . TYR A 1 131 ? 22.354  13.962  -19.550  1.00 17.62 ? 131 TYR A C   1 
ATOM   1005  O O   . TYR A 1 131 ? 22.883  14.867  -18.932  1.00 17.12 ? 131 TYR A O   1 
ATOM   1006  C CB  . TYR A 1 131 ? 21.724  14.448  -21.909  1.00 18.95 ? 131 TYR A CB  1 
ATOM   1007  C CG  . TYR A 1 131 ? 20.675  14.830  -22.941  1.00 19.26 ? 131 TYR A CG  1 
ATOM   1008  C CD1 . TYR A 1 131 ? 19.909  13.840  -23.584  1.00 19.91 ? 131 TYR A CD1 1 
ATOM   1009  C CD2 . TYR A 1 131 ? 20.483  16.148  -23.315  1.00 19.27 ? 131 TYR A CD2 1 
ATOM   1010  C CE1 . TYR A 1 131 ? 18.974  14.173  -24.544  1.00 19.86 ? 131 TYR A CE1 1 
ATOM   1011  C CE2 . TYR A 1 131 ? 19.525  16.477  -24.278  1.00 19.50 ? 131 TYR A CE2 1 
ATOM   1012  C CZ  . TYR A 1 131 ? 18.770  15.482  -24.876  1.00 19.56 ? 131 TYR A CZ  1 
ATOM   1013  O OH  . TYR A 1 131 ? 17.823  15.773  -25.832  1.00 19.58 ? 131 TYR A OH  1 
ATOM   1014  N N   . PRO A 1 132 ? 22.760  12.695  -19.440  1.00 17.30 ? 132 PRO A N   1 
ATOM   1015  C CA  . PRO A 1 132 ? 23.954  12.425  -18.643  1.00 17.52 ? 132 PRO A CA  1 
ATOM   1016  C C   . PRO A 1 132 ? 25.225  12.961  -19.301  1.00 17.15 ? 132 PRO A C   1 
ATOM   1017  O O   . PRO A 1 132 ? 25.204  13.283  -20.489  1.00 17.19 ? 132 PRO A O   1 
ATOM   1018  C CB  . PRO A 1 132 ? 24.008  10.894  -18.598  1.00 17.57 ? 132 PRO A CB  1 
ATOM   1019  C CG  . PRO A 1 132 ? 22.766  10.381  -19.233  1.00 17.18 ? 132 PRO A CG  1 
ATOM   1020  C CD  . PRO A 1 132 ? 22.222  11.476  -20.070  1.00 17.32 ? 132 PRO A CD  1 
ATOM   1021  N N   . PRO A 1 133 ? 26.327  13.062  -18.552  1.00 16.58 ? 133 PRO A N   1 
ATOM   1022  C CA  . PRO A 1 133 ? 27.584  13.389  -19.229  1.00 16.78 ? 133 PRO A CA  1 
ATOM   1023  C C   . PRO A 1 133 ? 28.176  12.140  -19.888  1.00 16.97 ? 133 PRO A C   1 
ATOM   1024  O O   . PRO A 1 133 ? 27.975  11.032  -19.392  1.00 17.06 ? 133 PRO A O   1 
ATOM   1025  C CB  . PRO A 1 133 ? 28.484  13.910  -18.103  1.00 16.71 ? 133 PRO A CB  1 
ATOM   1026  C CG  . PRO A 1 133 ? 27.870  13.415  -16.830  1.00 16.63 ? 133 PRO A CG  1 
ATOM   1027  C CD  . PRO A 1 133 ? 26.523  12.779  -17.129  1.00 16.45 ? 133 PRO A CD  1 
ATOM   1028  N N   . PRO A 1 134 ? 28.890  12.297  -21.006  1.00 16.92 ? 134 PRO A N   1 
ATOM   1029  C CA  . PRO A 1 134 ? 29.370  11.100  -21.685  1.00 17.13 ? 134 PRO A CA  1 
ATOM   1030  C C   . PRO A 1 134 ? 30.682  10.584  -21.114  1.00 17.77 ? 134 PRO A C   1 
ATOM   1031  O O   . PRO A 1 134 ? 31.443  11.350  -20.554  1.00 18.17 ? 134 PRO A O   1 
ATOM   1032  C CB  . PRO A 1 134 ? 29.579  11.574  -23.123  1.00 17.37 ? 134 PRO A CB  1 
ATOM   1033  C CG  . PRO A 1 134 ? 29.616  13.075  -23.076  1.00 17.63 ? 134 PRO A CG  1 
ATOM   1034  C CD  . PRO A 1 134 ? 29.348  13.522  -21.668  1.00 17.30 ? 134 PRO A CD  1 
ATOM   1035  N N   . PRO A 1 135 ? 30.963  9.276   -21.262  1.00 18.60 ? 135 PRO A N   1 
ATOM   1036  C CA  . PRO A 1 135 ? 32.288  8.750   -20.909  1.00 18.23 ? 135 PRO A CA  1 
ATOM   1037  C C   . PRO A 1 135 ? 33.387  9.315   -21.830  1.00 18.34 ? 135 PRO A C   1 
ATOM   1038  O O   . PRO A 1 135 ? 33.072  9.941   -22.865  1.00 20.35 ? 135 PRO A O   1 
ATOM   1039  C CB  . PRO A 1 135 ? 32.124  7.250   -21.156  1.00 18.03 ? 135 PRO A CB  1 
ATOM   1040  C CG  . PRO A 1 135 ? 31.075  7.151   -22.214  1.00 17.75 ? 135 PRO A CG  1 
ATOM   1041  C CD  . PRO A 1 135 ? 30.104  8.234   -21.864  1.00 18.09 ? 135 PRO A CD  1 
ATOM   1042  N N   . VAL A 1 136 ? 34.652  9.111   -21.467  1.00 17.33 ? 136 VAL A N   1 
ATOM   1043  C CA  . VAL A 1 136 ? 35.770  9.678   -22.222  1.00 16.36 ? 136 VAL A CA  1 
ATOM   1044  C C   . VAL A 1 136 ? 36.800  8.614   -22.553  1.00 16.28 ? 136 VAL A C   1 
ATOM   1045  O O   . VAL A 1 136 ? 37.160  7.826   -21.692  1.00 16.31 ? 136 VAL A O   1 
ATOM   1046  C CB  . VAL A 1 136 ? 36.461  10.820  -21.443  1.00 15.68 ? 136 VAL A CB  1 
ATOM   1047  C CG1 . VAL A 1 136 ? 37.667  11.344  -22.200  1.00 15.61 ? 136 VAL A CG1 1 
ATOM   1048  C CG2 . VAL A 1 136 ? 35.499  11.972  -21.231  1.00 16.01 ? 136 VAL A CG2 1 
ATOM   1049  N N   . LEU A 1 137 ? 37.260  8.611   -23.800  1.00 16.59 ? 137 LEU A N   1 
ATOM   1050  C CA  . LEU A 1 137 ? 38.426  7.844   -24.216  1.00 16.58 ? 137 LEU A CA  1 
ATOM   1051  C C   . LEU A 1 137 ? 39.568  8.815   -24.508  1.00 16.74 ? 137 LEU A C   1 
ATOM   1052  O O   . LEU A 1 137 ? 39.545  9.538   -25.509  1.00 15.40 ? 137 LEU A O   1 
ATOM   1053  C CB  . LEU A 1 137 ? 38.111  7.012   -25.464  1.00 16.96 ? 137 LEU A CB  1 
ATOM   1054  C CG  . LEU A 1 137 ? 39.268  6.344   -26.225  1.00 16.57 ? 137 LEU A CG  1 
ATOM   1055  C CD1 . LEU A 1 137 ? 40.009  5.354   -25.370  1.00 16.08 ? 137 LEU A CD1 1 
ATOM   1056  C CD2 . LEU A 1 137 ? 38.738  5.660   -27.474  1.00 16.60 ? 137 LEU A CD2 1 
ATOM   1057  N N   . LEU A 1 138 ? 40.559  8.835   -23.621  1.00 18.11 ? 138 LEU A N   1 
ATOM   1058  C CA  . LEU A 1 138 ? 41.754  9.651   -23.814  1.00 19.21 ? 138 LEU A CA  1 
ATOM   1059  C C   . LEU A 1 138 ? 42.742  8.887   -24.662  1.00 19.80 ? 138 LEU A C   1 
ATOM   1060  O O   . LEU A 1 138 ? 43.115  7.778   -24.312  1.00 20.01 ? 138 LEU A O   1 
ATOM   1061  C CB  . LEU A 1 138 ? 42.402  9.994   -22.477  1.00 19.73 ? 138 LEU A CB  1 
ATOM   1062  C CG  . LEU A 1 138 ? 43.671  10.842  -22.580  1.00 20.06 ? 138 LEU A CG  1 
ATOM   1063  C CD1 . LEU A 1 138 ? 43.397  12.167  -23.272  1.00 20.04 ? 138 LEU A CD1 1 
ATOM   1064  C CD2 . LEU A 1 138 ? 44.250  11.062  -21.187  1.00 20.50 ? 138 LEU A CD2 1 
ATOM   1065  N N   . ILE A 1 139 ? 43.159  9.480   -25.777  1.00 21.13 ? 139 ILE A N   1 
ATOM   1066  C CA  . ILE A 1 139 ? 44.134  8.852   -26.671  1.00 21.99 ? 139 ILE A CA  1 
ATOM   1067  C C   . ILE A 1 139 ? 45.443  9.611   -26.645  1.00 22.36 ? 139 ILE A C   1 
ATOM   1068  O O   . ILE A 1 139 ? 45.497  10.801  -26.931  1.00 25.33 ? 139 ILE A O   1 
ATOM   1069  C CB  . ILE A 1 139 ? 43.619  8.757   -28.133  1.00 22.45 ? 139 ILE A CB  1 
ATOM   1070  C CG1 . ILE A 1 139 ? 42.314  7.961   -28.182  1.00 22.75 ? 139 ILE A CG1 1 
ATOM   1071  C CG2 . ILE A 1 139 ? 44.660  8.075   -29.025  1.00 22.26 ? 139 ILE A CG2 1 
ATOM   1072  C CD1 . ILE A 1 139 ? 41.712  7.907   -29.562  1.00 23.20 ? 139 ILE A CD1 1 
ATOM   1073  N N   . SER A 1 140 ? 46.500  8.911   -26.296  1.00 21.78 ? 140 SER A N   1 
ATOM   1074  C CA  . SER A 1 140 ? 47.832  9.479   -26.334  1.00 21.45 ? 140 SER A CA  1 
ATOM   1075  C C   . SER A 1 140 ? 48.338  9.361   -27.759  1.00 21.58 ? 140 SER A C   1 
ATOM   1076  O O   . SER A 1 140 ? 48.172  8.320   -28.384  1.00 21.82 ? 140 SER A O   1 
ATOM   1077  C CB  . SER A 1 140 ? 48.739  8.717   -25.378  1.00 21.40 ? 140 SER A CB  1 
ATOM   1078  O OG  . SER A 1 140 ? 49.509  7.748   -26.033  1.00 22.06 ? 140 SER A OG  1 
ATOM   1079  N N   . PRO A 1 141 ? 48.955  10.422  -28.299  1.00 22.58 ? 141 PRO A N   1 
ATOM   1080  C CA  . PRO A 1 141 ? 49.508  10.347  -29.647  1.00 22.17 ? 141 PRO A CA  1 
ATOM   1081  C C   . PRO A 1 141 ? 50.811  9.555   -29.660  1.00 22.36 ? 141 PRO A C   1 
ATOM   1082  O O   . PRO A 1 141 ? 51.403  9.293   -28.605  1.00 23.00 ? 141 PRO A O   1 
ATOM   1083  C CB  . PRO A 1 141 ? 49.802  11.810  -29.981  1.00 22.40 ? 141 PRO A CB  1 
ATOM   1084  C CG  . PRO A 1 141 ? 50.147  12.422  -28.665  1.00 22.63 ? 141 PRO A CG  1 
ATOM   1085  C CD  . PRO A 1 141 ? 49.275  11.713  -27.654  1.00 23.02 ? 141 PRO A CD  1 
ATOM   1086  N N   . PRO A 1 142 ? 51.274  9.176   -30.859  1.00 21.54 ? 142 PRO A N   1 
ATOM   1087  C CA  . PRO A 1 142 ? 52.519  8.454   -30.937  1.00 21.24 ? 142 PRO A CA  1 
ATOM   1088  C C   . PRO A 1 142 ? 53.694  9.380   -30.715  1.00 22.32 ? 142 PRO A C   1 
ATOM   1089  O O   . PRO A 1 142 ? 53.515  10.596  -30.667  1.00 23.58 ? 142 PRO A O   1 
ATOM   1090  C CB  . PRO A 1 142 ? 52.508  7.925   -32.363  1.00 20.71 ? 142 PRO A CB  1 
ATOM   1091  C CG  . PRO A 1 142 ? 51.713  8.908   -33.129  1.00 20.52 ? 142 PRO A CG  1 
ATOM   1092  C CD  . PRO A 1 142 ? 50.682  9.409   -32.188  1.00 20.85 ? 142 PRO A CD  1 
ATOM   1093  N N   . PRO A 1 143 ? 54.898  8.826   -30.559  1.00 22.82 ? 143 PRO A N   1 
ATOM   1094  C CA  . PRO A 1 143 ? 56.051  9.707   -30.446  1.00 22.72 ? 143 PRO A CA  1 
ATOM   1095  C C   . PRO A 1 143 ? 56.223  10.512  -31.714  1.00 22.59 ? 143 PRO A C   1 
ATOM   1096  O O   . PRO A 1 143 ? 55.860  10.038  -32.815  1.00 23.70 ? 143 PRO A O   1 
ATOM   1097  C CB  . PRO A 1 143 ? 57.225  8.739   -30.291  1.00 22.67 ? 143 PRO A CB  1 
ATOM   1098  C CG  . PRO A 1 143 ? 56.625  7.499   -29.723  1.00 22.95 ? 143 PRO A CG  1 
ATOM   1099  C CD  . PRO A 1 143 ? 55.245  7.415   -30.314  1.00 22.78 ? 143 PRO A CD  1 
ATOM   1100  N N   . LEU A 1 144 ? 56.779  11.709  -31.554  1.00 21.01 ? 144 LEU A N   1 
ATOM   1101  C CA  . LEU A 1 144 ? 57.149  12.544  -32.675  1.00 20.33 ? 144 LEU A CA  1 
ATOM   1102  C C   . LEU A 1 144 ? 58.160  11.804  -33.543  1.00 20.55 ? 144 LEU A C   1 
ATOM   1103  O O   . LEU A 1 144 ? 58.825  10.845  -33.084  1.00 20.34 ? 144 LEU A O   1 
ATOM   1104  C CB  . LEU A 1 144 ? 57.812  13.827  -32.198  1.00 19.91 ? 144 LEU A CB  1 
ATOM   1105  C CG  . LEU A 1 144 ? 57.043  14.777  -31.287  1.00 19.98 ? 144 LEU A CG  1 
ATOM   1106  C CD1 . LEU A 1 144 ? 57.955  15.842  -30.711  1.00 19.72 ? 144 LEU A CD1 1 
ATOM   1107  C CD2 . LEU A 1 144 ? 55.915  15.449  -32.021  1.00 20.57 ? 144 LEU A CD2 1 
ATOM   1108  N N   . GLY A 1 145 ? 58.298  12.277  -34.781  1.00 20.96 ? 145 GLY A N   1 
ATOM   1109  C CA  . GLY A 1 145 ? 59.268  11.727  -35.700  1.00 22.76 ? 145 GLY A CA  1 
ATOM   1110  C C   . GLY A 1 145 ? 60.664  12.049  -35.230  1.00 25.00 ? 145 GLY A C   1 
ATOM   1111  O O   . GLY A 1 145 ? 60.887  13.048  -34.506  1.00 26.11 ? 145 GLY A O   1 
ATOM   1112  N N   . GLU A 1 146 ? 61.605  11.213  -35.632  1.00 29.46 ? 146 GLU A N   1 
ATOM   1113  C CA  . GLU A 1 146 ? 63.005  11.425  -35.258  1.00 32.73 ? 146 GLU A CA  1 
ATOM   1114  C C   . GLU A 1 146 ? 63.573  12.574  -36.053  1.00 31.80 ? 146 GLU A C   1 
ATOM   1115  O O   . GLU A 1 146 ? 64.522  13.213  -35.605  1.00 32.32 ? 146 GLU A O   1 
ATOM   1116  C CB  . GLU A 1 146 ? 63.891  10.170  -35.482  1.00 35.46 ? 146 GLU A CB  1 
ATOM   1117  C CG  . GLU A 1 146 ? 63.368  8.784   -35.134  1.00 37.42 ? 146 GLU A CG  1 
ATOM   1118  C CD  . GLU A 1 146 ? 63.923  8.197   -33.832  1.00 39.05 ? 146 GLU A CD  1 
ATOM   1119  O OE1 . GLU A 1 146 ? 63.576  7.055   -33.521  1.00 40.09 ? 146 GLU A OE1 1 
ATOM   1120  O OE2 . GLU A 1 146 ? 64.667  8.891   -33.117  1.00 40.30 ? 146 GLU A OE2 1 
ATOM   1121  N N   . THR A 1 147 ? 62.984  12.861  -37.212  1.00 31.07 ? 147 THR A N   1 
ATOM   1122  C CA  . THR A 1 147 ? 63.450  13.963  -38.064  1.00 31.76 ? 147 THR A CA  1 
ATOM   1123  C C   . THR A 1 147 ? 62.365  14.989  -38.389  1.00 29.26 ? 147 THR A C   1 
ATOM   1124  O O   . THR A 1 147 ? 61.490  14.698  -39.153  1.00 26.95 ? 147 THR A O   1 
ATOM   1125  C CB  . THR A 1 147 ? 64.055  13.425  -39.374  1.00 31.20 ? 147 THR A CB  1 
ATOM   1126  O OG1 . THR A 1 147 ? 65.054  12.455  -39.055  1.00 32.86 ? 147 THR A OG1 1 
ATOM   1127  C CG2 . THR A 1 147 ? 64.656  14.580  -40.191  1.00 30.59 ? 147 THR A CG2 1 
ATOM   1128  N N   . ILE A 1 148 ? 62.477  16.172  -37.813  1.00 27.17 ? 148 ILE A N   1 
ATOM   1129  C CA  . ILE A 1 148 ? 61.449  17.186  -37.932  1.00 25.94 ? 148 ILE A CA  1 
ATOM   1130  C C   . ILE A 1 148 ? 61.895  18.276  -38.914  1.00 25.44 ? 148 ILE A C   1 
ATOM   1131  O O   . ILE A 1 148 ? 63.066  18.668  -38.941  1.00 24.99 ? 148 ILE A O   1 
ATOM   1132  C CB  . ILE A 1 148 ? 61.092  17.768  -36.547  1.00 25.64 ? 148 ILE A CB  1 
ATOM   1133  C CG1 . ILE A 1 148 ? 60.511  16.658  -35.671  1.00 25.63 ? 148 ILE A CG1 1 
ATOM   1134  C CG2 . ILE A 1 148 ? 60.118  18.937  -36.673  1.00 25.20 ? 148 ILE A CG2 1 
ATOM   1135  C CD1 . ILE A 1 148 ? 60.448  16.964  -34.180  1.00 25.25 ? 148 ILE A CD1 1 
ATOM   1136  N N   . ASP A 1 149 ? 60.952  18.750  -39.723  1.00 26.14 ? 149 ASP A N   1 
ATOM   1137  C CA  . ASP A 1 149 ? 61.239  19.783  -40.699  1.00 27.32 ? 149 ASP A CA  1 
ATOM   1138  C C   . ASP A 1 149 ? 62.041  20.895  -40.018  1.00 28.86 ? 149 ASP A C   1 
ATOM   1139  O O   . ASP A 1 149 ? 61.638  21.376  -38.953  1.00 30.43 ? 149 ASP A O   1 
ATOM   1140  C CB  . ASP A 1 149 ? 59.942  20.323  -41.278  1.00 26.94 ? 149 ASP A CB  1 
ATOM   1141  C CG  . ASP A 1 149 ? 60.158  21.207  -42.487  1.00 27.99 ? 149 ASP A CG  1 
ATOM   1142  O OD1 . ASP A 1 149 ? 60.910  22.192  -42.388  1.00 29.16 ? 149 ASP A OD1 1 
ATOM   1143  O OD2 . ASP A 1 149 ? 59.535  20.943  -43.529  1.00 30.15 ? 149 ASP A OD2 1 
ATOM   1144  N N   . PRO A 1 150 ? 63.196  21.278  -40.604  1.00 27.84 ? 150 PRO A N   1 
ATOM   1145  C CA  . PRO A 1 150 ? 64.045  22.327  -40.058  1.00 27.64 ? 150 PRO A CA  1 
ATOM   1146  C C   . PRO A 1 150 ? 63.338  23.634  -39.638  1.00 27.01 ? 150 PRO A C   1 
ATOM   1147  O O   . PRO A 1 150 ? 63.799  24.289  -38.721  1.00 28.00 ? 150 PRO A O   1 
ATOM   1148  C CB  . PRO A 1 150 ? 65.035  22.604  -41.211  1.00 26.76 ? 150 PRO A CB  1 
ATOM   1149  C CG  . PRO A 1 150 ? 64.800  21.570  -42.275  1.00 26.72 ? 150 PRO A CG  1 
ATOM   1150  C CD  . PRO A 1 150 ? 63.900  20.546  -41.666  1.00 26.72 ? 150 PRO A CD  1 
ATOM   1151  N N   . LEU A 1 151 ? 62.268  24.009  -40.323  1.00 26.16 ? 151 LEU A N   1 
ATOM   1152  C CA  . LEU A 1 151 ? 61.469  25.177  -39.919  1.00 27.17 ? 151 LEU A CA  1 
ATOM   1153  C C   . LEU A 1 151 ? 60.818  24.990  -38.537  1.00 25.96 ? 151 LEU A C   1 
ATOM   1154  O O   . LEU A 1 151 ? 60.732  25.931  -37.758  1.00 24.57 ? 151 LEU A O   1 
ATOM   1155  C CB  . LEU A 1 151 ? 60.385  25.487  -40.943  1.00 28.77 ? 151 LEU A CB  1 
ATOM   1156  C CG  . LEU A 1 151 ? 60.854  26.194  -42.224  1.00 31.23 ? 151 LEU A CG  1 
ATOM   1157  C CD1 . LEU A 1 151 ? 60.531  25.396  -43.492  1.00 32.53 ? 151 LEU A CD1 1 
ATOM   1158  C CD2 . LEU A 1 151 ? 60.272  27.599  -42.303  1.00 31.63 ? 151 LEU A CD2 1 
ATOM   1159  N N   . ALA A 1 152 ? 60.380  23.768  -38.240  1.00 24.69 ? 152 ALA A N   1 
ATOM   1160  C CA  . ALA A 1 152 ? 59.672  23.467  -36.999  1.00 23.23 ? 152 ALA A CA  1 
ATOM   1161  C C   . ALA A 1 152 ? 60.566  22.899  -35.882  1.00 23.24 ? 152 ALA A C   1 
ATOM   1162  O O   . ALA A 1 152 ? 60.209  22.977  -34.716  1.00 23.92 ? 152 ALA A O   1 
ATOM   1163  C CB  . ALA A 1 152 ? 58.528  22.508  -37.300  1.00 22.35 ? 152 ALA A CB  1 
ATOM   1164  N N   . ALA A 1 153 ? 61.722  22.351  -36.232  1.00 22.89 ? 153 ALA A N   1 
ATOM   1165  C CA  . ALA A 1 153 ? 62.577  21.689  -35.235  1.00 22.90 ? 153 ALA A CA  1 
ATOM   1166  C C   . ALA A 1 153 ? 62.925  22.526  -33.980  1.00 22.36 ? 153 ALA A C   1 
ATOM   1167  O O   . ALA A 1 153 ? 62.869  22.002  -32.859  1.00 22.62 ? 153 ALA A O   1 
ATOM   1168  C CB  . ALA A 1 153 ? 63.839  21.172  -35.891  1.00 23.13 ? 153 ALA A CB  1 
ATOM   1169  N N   . PRO A 1 154 ? 63.271  23.821  -34.153  1.00 21.97 ? 154 PRO A N   1 
ATOM   1170  C CA  . PRO A 1 154 ? 63.605  24.651  -32.976  1.00 22.76 ? 154 PRO A CA  1 
ATOM   1171  C C   . PRO A 1 154 ? 62.502  24.696  -31.917  1.00 23.99 ? 154 PRO A C   1 
ATOM   1172  O O   . PRO A 1 154 ? 62.784  24.827  -30.733  1.00 25.69 ? 154 PRO A O   1 
ATOM   1173  C CB  . PRO A 1 154 ? 63.783  26.053  -33.572  1.00 21.71 ? 154 PRO A CB  1 
ATOM   1174  C CG  . PRO A 1 154 ? 64.136  25.814  -34.989  1.00 21.55 ? 154 PRO A CG  1 
ATOM   1175  C CD  . PRO A 1 154 ? 63.350  24.602  -35.401  1.00 21.76 ? 154 PRO A CD  1 
ATOM   1176  N N   . ILE A 1 155 ? 61.257  24.599  -32.379  1.00 23.80 ? 155 ILE A N   1 
ATOM   1177  C CA  . ILE A 1 155 ? 60.061  24.644  -31.552  1.00 23.07 ? 155 ILE A CA  1 
ATOM   1178  C C   . ILE A 1 155 ? 59.716  23.282  -30.910  1.00 22.91 ? 155 ILE A C   1 
ATOM   1179  O O   . ILE A 1 155 ? 58.863  23.222  -30.026  1.00 22.76 ? 155 ILE A O   1 
ATOM   1180  C CB  . ILE A 1 155 ? 58.924  25.280  -32.420  1.00 23.31 ? 155 ILE A CB  1 
ATOM   1181  C CG1 . ILE A 1 155 ? 58.893  26.790  -32.154  1.00 23.47 ? 155 ILE A CG1 1 
ATOM   1182  C CG2 . ILE A 1 155 ? 57.552  24.627  -32.270  1.00 22.78 ? 155 ILE A CG2 1 
ATOM   1183  C CD1 . ILE A 1 155 ? 58.050  27.579  -33.151  1.00 24.34 ? 155 ILE A CD1 1 
ATOM   1184  N N   . PHE A 1 156 ? 60.395  22.204  -31.322  1.00 22.93 ? 156 PHE A N   1 
ATOM   1185  C CA  . PHE A 1 156 ? 60.178  20.855  -30.731  1.00 22.77 ? 156 PHE A CA  1 
ATOM   1186  C C   . PHE A 1 156 ? 61.429  20.270  -30.061  1.00 22.13 ? 156 PHE A C   1 
ATOM   1187  O O   . PHE A 1 156 ? 61.606  19.047  -30.001  1.00 20.86 ? 156 PHE A O   1 
ATOM   1188  C CB  . PHE A 1 156 ? 59.639  19.863  -31.788  1.00 22.52 ? 156 PHE A CB  1 
ATOM   1189  C CG  . PHE A 1 156 ? 58.208  20.105  -32.147  1.00 22.60 ? 156 PHE A CG  1 
ATOM   1190  C CD1 . PHE A 1 156 ? 57.187  19.710  -31.310  1.00 22.94 ? 156 PHE A CD1 1 
ATOM   1191  C CD2 . PHE A 1 156 ? 57.868  20.776  -33.321  1.00 22.57 ? 156 PHE A CD2 1 
ATOM   1192  C CE1 . PHE A 1 156 ? 55.858  19.965  -31.631  1.00 22.81 ? 156 PHE A CE1 1 
ATOM   1193  C CE2 . PHE A 1 156 ? 56.550  21.027  -33.652  1.00 21.76 ? 156 PHE A CE2 1 
ATOM   1194  C CZ  . PHE A 1 156 ? 55.543  20.632  -32.807  1.00 21.75 ? 156 PHE A CZ  1 
ATOM   1195  N N   . VAL A 1 157 ? 62.285  21.132  -29.528  1.00 21.35 ? 157 VAL A N   1 
ATOM   1196  C CA  . VAL A 1 157 ? 63.456  20.669  -28.775  1.00 21.50 ? 157 VAL A CA  1 
ATOM   1197  C C   . VAL A 1 157 ? 62.951  20.013  -27.487  1.00 21.54 ? 157 VAL A C   1 
ATOM   1198  O O   . VAL A 1 157 ? 62.002  20.481  -26.884  1.00 21.85 ? 157 VAL A O   1 
ATOM   1199  C CB  . VAL A 1 157 ? 64.467  21.826  -28.506  1.00 20.95 ? 157 VAL A CB  1 
ATOM   1200  C CG1 . VAL A 1 157 ? 65.539  21.418  -27.499  1.00 20.68 ? 157 VAL A CG1 1 
ATOM   1201  C CG2 . VAL A 1 157 ? 65.065  22.319  -29.833  1.00 20.40 ? 157 VAL A CG2 1 
ATOM   1202  N N   . ASP A 1 158 ? 63.565  18.900  -27.110  1.00 22.21 ? 158 ASP A N   1 
ATOM   1203  C CA  . ASP A 1 158 ? 63.096  18.041  -26.009  1.00 22.03 ? 158 ASP A CA  1 
ATOM   1204  C C   . ASP A 1 158 ? 61.668  17.506  -26.177  1.00 21.57 ? 158 ASP A C   1 
ATOM   1205  O O   . ASP A 1 158 ? 61.149  16.915  -25.259  1.00 21.82 ? 158 ASP A O   1 
ATOM   1206  C CB  . ASP A 1 158 ? 63.206  18.769  -24.671  1.00 22.47 ? 158 ASP A CB  1 
ATOM   1207  C CG  . ASP A 1 158 ? 64.563  19.375  -24.456  1.00 23.06 ? 158 ASP A CG  1 
ATOM   1208  O OD1 . ASP A 1 158 ? 65.558  18.675  -24.673  1.00 24.77 ? 158 ASP A OD1 1 
ATOM   1209  O OD2 . ASP A 1 158 ? 64.645  20.551  -24.066  1.00 23.57 ? 158 ASP A OD2 1 
ATOM   1210  N N   . GLY A 1 159 ? 61.056  17.681  -27.338  1.00 21.40 ? 159 GLY A N   1 
ATOM   1211  C CA  . GLY A 1 159 ? 59.686  17.264  -27.546  1.00 22.47 ? 159 GLY A CA  1 
ATOM   1212  C C   . GLY A 1 159 ? 59.503  15.767  -27.691  1.00 23.35 ? 159 GLY A C   1 
ATOM   1213  O O   . GLY A 1 159 ? 58.506  15.200  -27.227  1.00 25.74 ? 159 GLY A O   1 
ATOM   1214  N N   . LEU A 1 160 ? 60.467  15.123  -28.340  1.00 22.64 ? 160 LEU A N   1 
ATOM   1215  C CA  . LEU A 1 160 ? 60.396  13.689  -28.598  1.00 21.91 ? 160 LEU A CA  1 
ATOM   1216  C C   . LEU A 1 160 ? 60.281  12.921  -27.291  1.00 21.57 ? 160 LEU A C   1 
ATOM   1217  O O   . LEU A 1 160 ? 59.405  12.067  -27.137  1.00 22.04 ? 160 LEU A O   1 
ATOM   1218  C CB  . LEU A 1 160 ? 61.625  13.245  -29.377  1.00 22.34 ? 160 LEU A CB  1 
ATOM   1219  C CG  . LEU A 1 160 ? 61.807  11.735  -29.564  1.00 22.63 ? 160 LEU A CG  1 
ATOM   1220  C CD1 . LEU A 1 160 ? 60.613  11.174  -30.322  1.00 23.09 ? 160 LEU A CD1 1 
ATOM   1221  C CD2 . LEU A 1 160 ? 63.126  11.348  -30.216  1.00 22.42 ? 160 LEU A CD2 1 
ATOM   1222  N N   . ALA A 1 161 ? 61.166  13.240  -26.351  1.00 21.23 ? 161 ALA A N   1 
ATOM   1223  C CA  . ALA A 1 161 ? 61.211  12.515  -25.087  1.00 21.16 ? 161 ALA A CA  1 
ATOM   1224  C C   . ALA A 1 161 ? 59.898  12.705  -24.322  1.00 21.50 ? 161 ALA A C   1 
ATOM   1225  O O   . ALA A 1 161 ? 59.359  11.757  -23.733  1.00 22.12 ? 161 ALA A O   1 
ATOM   1226  C CB  . ALA A 1 161 ? 62.403  12.948  -24.259  1.00 20.12 ? 161 ALA A CB  1 
ATOM   1227  N N   . LYS A 1 162 ? 59.378  13.926  -24.358  1.00 20.66 ? 162 LYS A N   1 
ATOM   1228  C CA  . LYS A 1 162 ? 58.094  14.217  -23.741  1.00 20.66 ? 162 LYS A CA  1 
ATOM   1229  C C   . LYS A 1 162 ? 56.974  13.403  -24.361  1.00 20.42 ? 162 LYS A C   1 
ATOM   1230  O O   . LYS A 1 162 ? 56.150  12.853  -23.642  1.00 20.80 ? 162 LYS A O   1 
ATOM   1231  C CB  . LYS A 1 162 ? 57.761  15.702  -23.864  1.00 20.58 ? 162 LYS A CB  1 
ATOM   1232  C CG  . LYS A 1 162 ? 58.639  16.581  -23.005  1.00 20.42 ? 162 LYS A CG  1 
ATOM   1233  C CD  . LYS A 1 162 ? 58.348  18.047  -23.277  1.00 20.61 ? 162 LYS A CD  1 
ATOM   1234  C CE  . LYS A 1 162 ? 59.463  18.958  -22.780  1.00 20.36 ? 162 LYS A CE  1 
ATOM   1235  N NZ  . LYS A 1 162 ? 58.969  20.341  -22.724  1.00 20.19 ? 162 LYS A NZ  1 
ATOM   1236  N N   . SER A 1 163 ? 56.953  13.322  -25.689  1.00 20.43 ? 163 SER A N   1 
ATOM   1237  C CA  . SER A 1 163 ? 55.903  12.579  -26.384  1.00 20.75 ? 163 SER A CA  1 
ATOM   1238  C C   . SER A 1 163 ? 55.980  11.083  -26.078  1.00 21.63 ? 163 SER A C   1 
ATOM   1239  O O   . SER A 1 163 ? 54.943  10.403  -26.032  1.00 21.70 ? 163 SER A O   1 
ATOM   1240  C CB  . SER A 1 163 ? 55.968  12.818  -27.906  1.00 20.19 ? 163 SER A CB  1 
ATOM   1241  O OG  . SER A 1 163 ? 57.121  12.252  -28.497  1.00 19.41 ? 163 SER A OG  1 
ATOM   1242  N N   . GLU A 1 164 ? 57.194  10.570  -25.854  1.00 22.06 ? 164 GLU A N   1 
ATOM   1243  C CA  . GLU A 1 164 ? 57.360  9.157   -25.510  1.00 21.95 ? 164 GLU A CA  1 
ATOM   1244  C C   . GLU A 1 164 ? 56.784  8.862   -24.131  1.00 21.39 ? 164 GLU A C   1 
ATOM   1245  O O   . GLU A 1 164 ? 56.270  7.782   -23.894  1.00 20.34 ? 164 GLU A O   1 
ATOM   1246  C CB  . GLU A 1 164 ? 58.834  8.751   -25.573  1.00 23.09 ? 164 GLU A CB  1 
ATOM   1247  C CG  . GLU A 1 164 ? 59.313  8.396   -26.978  1.00 24.19 ? 164 GLU A CG  1 
ATOM   1248  C CD  . GLU A 1 164 ? 60.828  8.454   -27.145  1.00 24.71 ? 164 GLU A CD  1 
ATOM   1249  O OE1 . GLU A 1 164 ? 61.333  8.115   -28.237  1.00 24.53 ? 164 GLU A OE1 1 
ATOM   1250  O OE2 . GLU A 1 164 ? 61.524  8.831   -26.188  1.00 25.45 ? 164 GLU A OE2 1 
ATOM   1251  N N   . ALA A 1 165 ? 56.856  9.839   -23.233  1.00 22.44 ? 165 ALA A N   1 
ATOM   1252  C CA  . ALA A 1 165 ? 56.365  9.679   -21.860  1.00 22.94 ? 165 ALA A CA  1 
ATOM   1253  C C   . ALA A 1 165 ? 54.842  9.853   -21.670  1.00 22.71 ? 165 ALA A C   1 
ATOM   1254  O O   . ALA A 1 165 ? 54.333  9.601   -20.562  1.00 22.47 ? 165 ALA A O   1 
ATOM   1255  C CB  . ALA A 1 165 ? 57.098  10.647  -20.946  1.00 23.06 ? 165 ALA A CB  1 
ATOM   1256  N N   . LEU A 1 166 ? 54.121  10.284  -22.712  1.00 21.50 ? 166 LEU A N   1 
ATOM   1257  C CA  . LEU A 1 166 ? 52.691  10.604  -22.561  1.00 20.47 ? 166 LEU A CA  1 
ATOM   1258  C C   . LEU A 1 166 ? 51.792  9.391   -22.318  1.00 18.15 ? 166 LEU A C   1 
ATOM   1259  O O   . LEU A 1 166 ? 50.942  9.439   -21.448  1.00 17.70 ? 166 LEU A O   1 
ATOM   1260  C CB  . LEU A 1 166 ? 52.169  11.421  -23.751  1.00 21.94 ? 166 LEU A CB  1 
ATOM   1261  C CG  . LEU A 1 166 ? 52.737  12.852  -23.908  1.00 23.24 ? 166 LEU A CG  1 
ATOM   1262  C CD1 . LEU A 1 166 ? 52.119  13.577  -25.104  1.00 23.31 ? 166 LEU A CD1 1 
ATOM   1263  C CD2 . LEU A 1 166 ? 52.565  13.666  -22.640  1.00 22.70 ? 166 LEU A CD2 1 
ATOM   1264  N N   . PRO A 1 167 ? 51.982  8.290   -23.068  1.00 16.90 ? 167 PRO A N   1 
ATOM   1265  C CA  . PRO A 1 167 ? 51.114  7.134   -22.826  1.00 16.50 ? 167 PRO A CA  1 
ATOM   1266  C C   . PRO A 1 167 ? 51.006  6.718   -21.333  1.00 16.11 ? 167 PRO A C   1 
ATOM   1267  O O   . PRO A 1 167 ? 49.901  6.501   -20.827  1.00 16.04 ? 167 PRO A O   1 
ATOM   1268  C CB  . PRO A 1 167 ? 51.774  6.021   -23.650  1.00 16.19 ? 167 PRO A CB  1 
ATOM   1269  C CG  . PRO A 1 167 ? 52.433  6.744   -24.762  1.00 15.96 ? 167 PRO A CG  1 
ATOM   1270  C CD  . PRO A 1 167 ? 52.918  8.035   -24.179  1.00 16.50 ? 167 PRO A CD  1 
ATOM   1271  N N   . GLY A 1 168 ? 52.133  6.616   -20.641  1.00 15.97 ? 168 GLY A N   1 
ATOM   1272  C CA  . GLY A 1 168 ? 52.124  6.220   -19.234  1.00 16.02 ? 168 GLY A CA  1 
ATOM   1273  C C   . GLY A 1 168 ? 51.327  7.171   -18.361  1.00 15.90 ? 168 GLY A C   1 
ATOM   1274  O O   . GLY A 1 168 ? 50.488  6.746   -17.566  1.00 14.99 ? 168 GLY A O   1 
ATOM   1275  N N   . VAL A 1 169 ? 51.590  8.467   -18.536  1.00 16.60 ? 169 VAL A N   1 
ATOM   1276  C CA  . VAL A 1 169 ? 50.927  9.517   -17.762  1.00 16.85 ? 169 VAL A CA  1 
ATOM   1277  C C   . VAL A 1 169 ? 49.438  9.565   -18.093  1.00 16.37 ? 169 VAL A C   1 
ATOM   1278  O O   . VAL A 1 169 ? 48.606  9.575   -17.196  1.00 15.77 ? 169 VAL A O   1 
ATOM   1279  C CB  . VAL A 1 169 ? 51.543  10.909  -18.044  1.00 17.69 ? 169 VAL A CB  1 
ATOM   1280  C CG1 . VAL A 1 169 ? 50.774  11.986  -17.310  1.00 18.40 ? 169 VAL A CG1 1 
ATOM   1281  C CG2 . VAL A 1 169 ? 52.998  10.970  -17.628  1.00 18.14 ? 169 VAL A CG2 1 
ATOM   1282  N N   . TYR A 1 170 ? 49.117  9.609   -19.387  1.00 16.78 ? 170 TYR A N   1 
ATOM   1283  C CA  . TYR A 1 170 ? 47.721  9.641   -19.859  1.00 16.81 ? 170 TYR A CA  1 
ATOM   1284  C C   . TYR A 1 170 ? 46.910  8.468   -19.309  1.00 17.24 ? 170 TYR A C   1 
ATOM   1285  O O   . TYR A 1 170 ? 45.754  8.652   -18.912  1.00 17.10 ? 170 TYR A O   1 
ATOM   1286  C CB  . TYR A 1 170 ? 47.646  9.640   -21.397  1.00 16.29 ? 170 TYR A CB  1 
ATOM   1287  C CG  . TYR A 1 170 ? 47.759  10.999  -22.060  1.00 15.96 ? 170 TYR A CG  1 
ATOM   1288  C CD1 . TYR A 1 170 ? 48.470  12.036  -21.466  1.00 15.84 ? 170 TYR A CD1 1 
ATOM   1289  C CD2 . TYR A 1 170 ? 47.170  11.235  -23.305  1.00 15.82 ? 170 TYR A CD2 1 
ATOM   1290  C CE1 . TYR A 1 170 ? 48.570  13.273  -22.071  1.00 16.05 ? 170 TYR A CE1 1 
ATOM   1291  C CE2 . TYR A 1 170 ? 47.274  12.473  -23.924  1.00 16.09 ? 170 TYR A CE2 1 
ATOM   1292  C CZ  . TYR A 1 170 ? 47.971  13.497  -23.300  1.00 16.03 ? 170 TYR A CZ  1 
ATOM   1293  O OH  . TYR A 1 170 ? 48.078  14.733  -23.897  1.00 15.21 ? 170 TYR A OH  1 
ATOM   1294  N N   . LYS A 1 171 ? 47.517  7.280   -19.276  1.00 17.61 ? 171 LYS A N   1 
ATOM   1295  C CA  . LYS A 1 171 ? 46.833  6.119   -18.743  1.00 17.93 ? 171 LYS A CA  1 
ATOM   1296  C C   . LYS A 1 171 ? 46.467  6.290   -17.266  1.00 18.04 ? 171 LYS A C   1 
ATOM   1297  O O   . LYS A 1 171 ? 45.345  5.982   -16.862  1.00 16.90 ? 171 LYS A O   1 
ATOM   1298  C CB  . LYS A 1 171 ? 47.650  4.837   -18.927  1.00 18.69 ? 171 LYS A CB  1 
ATOM   1299  C CG  . LYS A 1 171 ? 46.811  3.599   -18.636  1.00 19.79 ? 171 LYS A CG  1 
ATOM   1300  C CD  . LYS A 1 171 ? 47.482  2.305   -19.070  1.00 20.13 ? 171 LYS A CD  1 
ATOM   1301  C CE  . LYS A 1 171 ? 48.382  1.746   -17.998  1.00 20.38 ? 171 LYS A CE  1 
ATOM   1302  N NZ  . LYS A 1 171 ? 47.682  0.623   -17.330  1.00 20.81 ? 171 LYS A NZ  1 
ATOM   1303  N N   . ALA A 1 172 ? 47.415  6.777   -16.464  1.00 18.69 ? 172 ALA A N   1 
ATOM   1304  C CA  . ALA A 1 172 ? 47.176  6.966   -15.034  1.00 19.39 ? 172 ALA A CA  1 
ATOM   1305  C C   . ALA A 1 172 ? 46.074  7.993   -14.804  1.00 20.67 ? 172 ALA A C   1 
ATOM   1306  O O   . ALA A 1 172 ? 45.151  7.762   -14.016  1.00 23.38 ? 172 ALA A O   1 
ATOM   1307  C CB  . ALA A 1 172 ? 48.438  7.396   -14.324  1.00 19.34 ? 172 ALA A CB  1 
ATOM   1308  N N   . ILE A 1 173 ? 46.162  9.111   -15.514  1.00 20.03 ? 173 ILE A N   1 
ATOM   1309  C CA  . ILE A 1 173 ? 45.201  10.193  -15.383  1.00 20.08 ? 173 ILE A CA  1 
ATOM   1310  C C   . ILE A 1 173 ? 43.799  9.739   -15.783  1.00 20.01 ? 173 ILE A C   1 
ATOM   1311  O O   . ILE A 1 173 ? 42.818  10.062  -15.108  1.00 19.12 ? 173 ILE A O   1 
ATOM   1312  C CB  . ILE A 1 173 ? 45.623  11.408  -16.242  1.00 20.71 ? 173 ILE A CB  1 
ATOM   1313  C CG1 . ILE A 1 173 ? 46.918  12.044  -15.710  1.00 20.91 ? 173 ILE A CG1 1 
ATOM   1314  C CG2 . ILE A 1 173 ? 44.517  12.462  -16.283  1.00 20.39 ? 173 ILE A CG2 1 
ATOM   1315  C CD1 . ILE A 1 173 ? 46.831  12.634  -14.313  1.00 20.85 ? 173 ILE A CD1 1 
ATOM   1316  N N   . ALA A 1 174 ? 43.706  8.999   -16.884  1.00 20.90 ? 174 ALA A N   1 
ATOM   1317  C CA  . ALA A 1 174 ? 42.422  8.486   -17.372  1.00 22.64 ? 174 ALA A CA  1 
ATOM   1318  C C   . ALA A 1 174 ? 41.814  7.534   -16.357  1.00 24.11 ? 174 ALA A C   1 
ATOM   1319  O O   . ALA A 1 174 ? 40.633  7.630   -16.022  1.00 24.77 ? 174 ALA A O   1 
ATOM   1320  C CB  . ALA A 1 174 ? 42.606  7.770   -18.700  1.00 22.65 ? 174 ALA A CB  1 
ATOM   1321  N N   . GLU A 1 175 ? 42.647  6.613   -15.881  1.00 25.37 ? 175 GLU A N   1 
ATOM   1322  C CA  . GLU A 1 175 ? 42.257  5.668   -14.847  1.00 25.55 ? 175 GLU A CA  1 
ATOM   1323  C C   . GLU A 1 175 ? 41.805  6.383   -13.582  1.00 22.73 ? 175 GLU A C   1 
ATOM   1324  O O   . GLU A 1 175 ? 40.803  6.017   -13.011  1.00 21.66 ? 175 GLU A O   1 
ATOM   1325  C CB  . GLU A 1 175 ? 43.442  4.718   -14.545  1.00 28.26 ? 175 GLU A CB  1 
ATOM   1326  C CG  . GLU A 1 175 ? 43.108  3.227   -14.454  1.00 29.47 ? 175 GLU A CG  1 
ATOM   1327  C CD  . GLU A 1 175 ? 43.648  2.403   -15.615  1.00 30.09 ? 175 GLU A CD  1 
ATOM   1328  O OE1 . GLU A 1 175 ? 44.842  2.050   -15.604  1.00 31.71 ? 175 GLU A OE1 1 
ATOM   1329  O OE2 . GLU A 1 175 ? 42.856  2.137   -16.527  1.00 30.14 ? 175 GLU A OE2 1 
ATOM   1330  N N   . ALA A 1 176 ? 42.533  7.416   -13.164  1.00 21.16 ? 176 ALA A N   1 
ATOM   1331  C CA  . ALA A 1 176 ? 42.176  8.185   -11.954  1.00 20.22 ? 176 ALA A CA  1 
ATOM   1332  C C   . ALA A 1 176 ? 40.809  8.832   -12.079  1.00 19.89 ? 176 ALA A C   1 
ATOM   1333  O O   . ALA A 1 176 ? 40.115  9.013   -11.104  1.00 18.90 ? 176 ALA A O   1 
ATOM   1334  C CB  . ALA A 1 176 ? 43.222  9.248   -11.660  1.00 19.64 ? 176 ALA A CB  1 
ATOM   1335  N N   . ALA A 1 177 ? 40.443  9.191   -13.303  1.00 20.32 ? 177 ALA A N   1 
ATOM   1336  C CA  . ALA A 1 177 ? 39.153  9.800   -13.602  1.00 19.31 ? 177 ALA A CA  1 
ATOM   1337  C C   . ALA A 1 177 ? 38.044  8.769   -13.812  1.00 19.26 ? 177 ALA A C   1 
ATOM   1338  O O   . ALA A 1 177 ? 36.922  9.145   -14.100  1.00 18.90 ? 177 ALA A O   1 
ATOM   1339  C CB  . ALA A 1 177 ? 39.288  10.653  -14.859  1.00 19.38 ? 177 ALA A CB  1 
ATOM   1340  N N   . GLY A 1 178 ? 38.359  7.482   -13.706  1.00 19.33 ? 178 GLY A N   1 
ATOM   1341  C CA  . GLY A 1 178 ? 37.420  6.407   -14.035  1.00 19.09 ? 178 GLY A CA  1 
ATOM   1342  C C   . GLY A 1 178 ? 36.990  6.364   -15.488  1.00 19.24 ? 178 GLY A C   1 
ATOM   1343  O O   . GLY A 1 178 ? 35.829  6.106   -15.780  1.00 20.02 ? 178 GLY A O   1 
ATOM   1344  N N   . GLU A 1 179 ? 37.920  6.626   -16.398  1.00 19.58 ? 179 GLU A N   1 
ATOM   1345  C CA  . GLU A 1 179 ? 37.633  6.733   -17.836  1.00 19.22 ? 179 GLU A CA  1 
ATOM   1346  C C   . GLU A 1 179 ? 38.616  5.854   -18.612  1.00 18.82 ? 179 GLU A C   1 
ATOM   1347  O O   . GLU A 1 179 ? 39.400  5.140   -18.014  1.00 18.25 ? 179 GLU A O   1 
ATOM   1348  C CB  . GLU A 1 179 ? 37.730  8.197   -18.286  1.00 19.11 ? 179 GLU A CB  1 
ATOM   1349  C CG  . GLU A 1 179 ? 36.769  9.132   -17.571  1.00 18.87 ? 179 GLU A CG  1 
ATOM   1350  C CD  . GLU A 1 179 ? 35.318  8.997   -17.996  1.00 18.66 ? 179 GLU A CD  1 
ATOM   1351  O OE1 . GLU A 1 179 ? 34.463  9.729   -17.432  1.00 19.42 ? 179 GLU A OE1 1 
ATOM   1352  O OE2 . GLU A 1 179 ? 35.020  8.172   -18.883  1.00 18.14 ? 179 GLU A OE2 1 
ATOM   1353  N N   . SER A 1 180 ? 38.561  5.884   -19.937  1.00 18.52 ? 180 SER A N   1 
ATOM   1354  C CA  . SER A 1 180 ? 39.330  4.941   -20.739  1.00 18.18 ? 180 SER A CA  1 
ATOM   1355  C C   . SER A 1 180 ? 40.535  5.566   -21.413  1.00 17.85 ? 180 SER A C   1 
ATOM   1356  O O   . SER A 1 180 ? 40.622  6.780   -21.569  1.00 17.13 ? 180 SER A O   1 
ATOM   1357  C CB  . SER A 1 180 ? 38.435  4.334   -21.795  1.00 18.36 ? 180 SER A CB  1 
ATOM   1358  O OG  . SER A 1 180 ? 37.195  3.960   -21.221  1.00 18.24 ? 180 SER A OG  1 
ATOM   1359  N N   . PHE A 1 181 ? 41.456  4.700   -21.825  1.00 18.67 ? 181 PHE A N   1 
ATOM   1360  C CA  . PHE A 1 181 ? 42.725  5.092   -22.424  1.00 18.97 ? 181 PHE A CA  1 
ATOM   1361  C C   . PHE A 1 181 ? 43.084  4.250   -23.641  1.00 18.79 ? 181 PHE A C   1 
ATOM   1362  O O   . PHE A 1 181 ? 42.739  3.080   -23.712  1.00 18.78 ? 181 PHE A O   1 
ATOM   1363  C CB  . PHE A 1 181 ? 43.848  4.951   -21.411  1.00 19.33 ? 181 PHE A CB  1 
ATOM   1364  C CG  . PHE A 1 181 ? 45.204  5.088   -22.020  1.00 19.88 ? 181 PHE A CG  1 
ATOM   1365  C CD1 . PHE A 1 181 ? 45.637  6.324   -22.480  1.00 20.53 ? 181 PHE A CD1 1 
ATOM   1366  C CD2 . PHE A 1 181 ? 46.032  3.989   -22.171  1.00 19.96 ? 181 PHE A CD2 1 
ATOM   1367  C CE1 . PHE A 1 181 ? 46.872  6.472   -23.066  1.00 20.62 ? 181 PHE A CE1 1 
ATOM   1368  C CE2 . PHE A 1 181 ? 47.272  4.123   -22.743  1.00 20.46 ? 181 PHE A CE2 1 
ATOM   1369  C CZ  . PHE A 1 181 ? 47.690  5.374   -23.198  1.00 21.27 ? 181 PHE A CZ  1 
ATOM   1370  N N   . PHE A 1 182 ? 43.785  4.854   -24.593  1.00 19.73 ? 182 PHE A N   1 
ATOM   1371  C CA  . PHE A 1 182 ? 44.358  4.126   -25.722  1.00 21.14 ? 182 PHE A CA  1 
ATOM   1372  C C   . PHE A 1 182 ? 45.598  4.828   -26.240  1.00 21.52 ? 182 PHE A C   1 
ATOM   1373  O O   . PHE A 1 182 ? 45.592  6.042   -26.416  1.00 22.56 ? 182 PHE A O   1 
ATOM   1374  C CB  . PHE A 1 182 ? 43.341  3.977   -26.848  1.00 22.08 ? 182 PHE A CB  1 
ATOM   1375  C CG  . PHE A 1 182 ? 43.861  3.186   -28.028  1.00 22.63 ? 182 PHE A CG  1 
ATOM   1376  C CD1 . PHE A 1 182 ? 43.880  1.793   -27.995  1.00 23.48 ? 182 PHE A CD1 1 
ATOM   1377  C CD2 . PHE A 1 182 ? 44.331  3.825   -29.167  1.00 22.48 ? 182 PHE A CD2 1 
ATOM   1378  C CE1 . PHE A 1 182 ? 44.369  1.066   -29.061  1.00 23.22 ? 182 PHE A CE1 1 
ATOM   1379  C CE2 . PHE A 1 182 ? 44.805  3.101   -30.241  1.00 22.41 ? 182 PHE A CE2 1 
ATOM   1380  C CZ  . PHE A 1 182 ? 44.806  1.717   -30.193  1.00 22.74 ? 182 PHE A CZ  1 
ATOM   1381  N N   . ASP A 1 183 ? 46.653  4.062   -26.483  1.00 21.89 ? 183 ASP A N   1 
ATOM   1382  C CA  . ASP A 1 183 ? 47.925  4.615   -26.936  1.00 22.29 ? 183 ASP A CA  1 
ATOM   1383  C C   . ASP A 1 183 ? 48.035  4.470   -28.449  1.00 22.45 ? 183 ASP A C   1 
ATOM   1384  O O   . ASP A 1 183 ? 48.254  3.371   -28.973  1.00 22.41 ? 183 ASP A O   1 
ATOM   1385  C CB  . ASP A 1 183 ? 49.071  3.874   -26.259  1.00 23.09 ? 183 ASP A CB  1 
ATOM   1386  C CG  . ASP A 1 183 ? 50.432  4.362   -26.678  1.00 23.74 ? 183 ASP A CG  1 
ATOM   1387  O OD1 . ASP A 1 183 ? 50.549  5.384   -27.385  1.00 24.89 ? 183 ASP A OD1 1 
ATOM   1388  O OD2 . ASP A 1 183 ? 51.399  3.698   -26.263  1.00 24.87 ? 183 ASP A OD2 1 
ATOM   1389  N N   . ALA A 1 184 ? 47.905  5.585   -29.159  1.00 22.22 ? 184 ALA A N   1 
ATOM   1390  C CA  . ALA A 1 184 ? 48.021  5.538   -30.605  1.00 22.92 ? 184 ALA A CA  1 
ATOM   1391  C C   . ALA A 1 184 ? 49.383  4.958   -31.043  1.00 23.19 ? 184 ALA A C   1 
ATOM   1392  O O   . ALA A 1 184 ? 49.496  4.330   -32.090  1.00 23.44 ? 184 ALA A O   1 
ATOM   1393  C CB  . ALA A 1 184 ? 47.803  6.917   -31.179  1.00 23.07 ? 184 ALA A CB  1 
ATOM   1394  N N   . GLY A 1 185 ? 50.406  5.163   -30.223  1.00 23.40 ? 185 GLY A N   1 
ATOM   1395  C CA  . GLY A 1 185 ? 51.733  4.608   -30.477  1.00 23.13 ? 185 GLY A CA  1 
ATOM   1396  C C   . GLY A 1 185 ? 51.818  3.084   -30.480  1.00 22.19 ? 185 GLY A C   1 
ATOM   1397  O O   . GLY A 1 185 ? 52.813  2.524   -30.936  1.00 22.82 ? 185 GLY A O   1 
ATOM   1398  N N   . SER A 1 186 ? 50.791  2.411   -29.961  1.00 20.08 ? 186 SER A N   1 
ATOM   1399  C CA  . SER A 1 186 ? 50.748  0.957   -29.974  1.00 19.51 ? 186 SER A CA  1 
ATOM   1400  C C   . SER A 1 186 ? 50.420  0.380   -31.361  1.00 20.02 ? 186 SER A C   1 
ATOM   1401  O O   . SER A 1 186 ? 50.683  -0.793  -31.615  1.00 21.14 ? 186 SER A O   1 
ATOM   1402  C CB  . SER A 1 186 ? 49.739  0.438   -28.948  1.00 19.29 ? 186 SER A CB  1 
ATOM   1403  O OG  . SER A 1 186 ? 48.424  0.494   -29.438  1.00 19.06 ? 186 SER A OG  1 
ATOM   1404  N N   . VAL A 1 187 ? 49.847  1.188   -32.249  1.00 19.59 ? 187 VAL A N   1 
ATOM   1405  C CA  . VAL A 1 187 ? 49.444  0.725   -33.584  1.00 19.27 ? 187 VAL A CA  1 
ATOM   1406  C C   . VAL A 1 187 ? 49.995  1.532   -34.755  1.00 19.20 ? 187 VAL A C   1 
ATOM   1407  O O   . VAL A 1 187 ? 49.904  1.077   -35.882  1.00 18.65 ? 187 VAL A O   1 
ATOM   1408  C CB  . VAL A 1 187 ? 47.895  0.697   -33.708  1.00 20.27 ? 187 VAL A CB  1 
ATOM   1409  C CG1 . VAL A 1 187 ? 47.297  -0.330  -32.758  1.00 20.77 ? 187 VAL A CG1 1 
ATOM   1410  C CG2 . VAL A 1 187 ? 47.281  2.064   -33.425  1.00 20.44 ? 187 VAL A CG2 1 
ATOM   1411  N N   . VAL A 1 188 ? 50.524  2.731   -34.502  1.00 20.21 ? 188 VAL A N   1 
ATOM   1412  C CA  . VAL A 1 188 ? 51.125  3.583   -35.549  1.00 20.71 ? 188 VAL A CA  1 
ATOM   1413  C C   . VAL A 1 188 ? 52.268  4.447   -35.004  1.00 20.74 ? 188 VAL A C   1 
ATOM   1414  O O   . VAL A 1 188 ? 52.463  4.562   -33.778  1.00 20.46 ? 188 VAL A O   1 
ATOM   1415  C CB  . VAL A 1 188 ? 50.100  4.580   -36.167  1.00 21.50 ? 188 VAL A CB  1 
ATOM   1416  C CG1 . VAL A 1 188 ? 48.852  3.876   -36.696  1.00 21.67 ? 188 VAL A CG1 1 
ATOM   1417  C CG2 . VAL A 1 188 ? 49.688  5.649   -35.165  1.00 21.39 ? 188 VAL A CG2 1 
ATOM   1418  N N   . SER A 1 189 ? 53.006  5.072   -35.923  1.00 20.45 ? 189 SER A N   1 
ATOM   1419  C CA  . SER A 1 189 ? 53.958  6.125   -35.565  1.00 20.58 ? 189 SER A CA  1 
ATOM   1420  C C   . SER A 1 189 ? 53.903  7.293   -36.532  1.00 20.45 ? 189 SER A C   1 
ATOM   1421  O O   . SER A 1 189 ? 53.284  7.220   -37.575  1.00 21.26 ? 189 SER A O   1 
ATOM   1422  C CB  . SER A 1 189 ? 55.388  5.594   -35.438  1.00 20.41 ? 189 SER A CB  1 
ATOM   1423  O OG  . SER A 1 189 ? 55.608  4.591   -36.376  1.00 20.25 ? 189 SER A OG  1 
ATOM   1424  N N   . THR A 1 190 ? 54.551  8.378   -36.147  1.00 20.85 ? 190 THR A N   1 
ATOM   1425  C CA  . THR A 1 190 ? 54.547  9.607   -36.914  1.00 20.69 ? 190 THR A CA  1 
ATOM   1426  C C   . THR A 1 190 ? 55.462  9.413   -38.136  1.00 20.61 ? 190 THR A C   1 
ATOM   1427  O O   . THR A 1 190 ? 56.688  9.595   -38.082  1.00 20.69 ? 190 THR A O   1 
ATOM   1428  C CB  . THR A 1 190 ? 54.986  10.815  -36.047  1.00 20.57 ? 190 THR A CB  1 
ATOM   1429  O OG1 . THR A 1 190 ? 54.283  10.820  -34.808  1.00 20.70 ? 190 THR A OG1 1 
ATOM   1430  C CG2 . THR A 1 190 ? 54.726  12.110  -36.761  1.00 20.56 ? 190 THR A CG2 1 
ATOM   1431  N N   . ASP A 1 191 ? 54.827  9.031   -39.239  1.00 19.96 ? 191 ASP A N   1 
ATOM   1432  C CA  . ASP A 1 191 ? 55.523  8.704   -40.478  1.00 19.92 ? 191 ASP A CA  1 
ATOM   1433  C C   . ASP A 1 191 ? 55.482  9.829   -41.505  1.00 20.89 ? 191 ASP A C   1 
ATOM   1434  O O   . ASP A 1 191 ? 56.028  9.680   -42.597  1.00 23.03 ? 191 ASP A O   1 
ATOM   1435  C CB  . ASP A 1 191 ? 54.921  7.438   -41.099  1.00 18.72 ? 191 ASP A CB  1 
ATOM   1436  C CG  . ASP A 1 191 ? 53.520  7.646   -41.613  1.00 17.76 ? 191 ASP A CG  1 
ATOM   1437  O OD1 . ASP A 1 191 ? 52.808  8.517   -41.072  1.00 17.26 ? 191 ASP A OD1 1 
ATOM   1438  O OD2 . ASP A 1 191 ? 53.124  6.931   -42.555  1.00 18.00 ? 191 ASP A OD2 1 
ATOM   1439  N N   . GLY A 1 192 ? 54.841  10.947  -41.192  1.00 21.08 ? 192 GLY A N   1 
ATOM   1440  C CA  . GLY A 1 192 ? 54.815  12.048  -42.154  1.00 21.27 ? 192 GLY A CA  1 
ATOM   1441  C C   . GLY A 1 192 ? 56.211  12.576  -42.438  1.00 20.89 ? 192 GLY A C   1 
ATOM   1442  O O   . GLY A 1 192 ? 57.098  12.529  -41.565  1.00 21.51 ? 192 GLY A O   1 
ATOM   1443  N N   . VAL A 1 193 ? 56.406  13.096  -43.643  1.00 19.90 ? 193 VAL A N   1 
ATOM   1444  C CA  . VAL A 1 193 ? 57.712  13.614  -44.032  1.00 20.08 ? 193 VAL A CA  1 
ATOM   1445  C C   . VAL A 1 193 ? 58.218  14.750  -43.131  1.00 19.83 ? 193 VAL A C   1 
ATOM   1446  O O   . VAL A 1 193 ? 59.428  14.898  -42.962  1.00 20.23 ? 193 VAL A O   1 
ATOM   1447  C CB  . VAL A 1 193 ? 57.743  14.045  -45.515  1.00 20.51 ? 193 VAL A CB  1 
ATOM   1448  C CG1 . VAL A 1 193 ? 56.960  15.352  -45.731  1.00 21.03 ? 193 VAL A CG1 1 
ATOM   1449  C CG2 . VAL A 1 193 ? 59.189  14.143  -45.998  1.00 20.23 ? 193 VAL A CG2 1 
ATOM   1450  N N   . ASP A 1 194 ? 57.308  15.529  -42.538  1.00 19.99 ? 194 ASP A N   1 
ATOM   1451  C CA  . ASP A 1 194 ? 57.720  16.668  -41.693  1.00 20.55 ? 194 ASP A CA  1 
ATOM   1452  C C   . ASP A 1 194 ? 58.010  16.279  -40.245  1.00 19.68 ? 194 ASP A C   1 
ATOM   1453  O O   . ASP A 1 194 ? 58.368  17.138  -39.432  1.00 20.74 ? 194 ASP A O   1 
ATOM   1454  C CB  . ASP A 1 194 ? 56.698  17.829  -41.753  1.00 21.77 ? 194 ASP A CB  1 
ATOM   1455  C CG  . ASP A 1 194 ? 55.276  17.421  -41.316  1.00 22.69 ? 194 ASP A CG  1 
ATOM   1456  O OD1 . ASP A 1 194 ? 55.108  16.337  -40.698  1.00 24.32 ? 194 ASP A OD1 1 
ATOM   1457  O OD2 . ASP A 1 194 ? 54.339  18.191  -41.593  1.00 22.50 ? 194 ASP A OD2 1 
ATOM   1458  N N   . GLY A 1 195 ? 57.854  14.993  -39.919  1.00 19.14 ? 195 GLY A N   1 
ATOM   1459  C CA  . GLY A 1 195 ? 58.176  14.481  -38.585  1.00 19.17 ? 195 GLY A CA  1 
ATOM   1460  C C   . GLY A 1 195 ? 57.140  14.760  -37.509  1.00 19.11 ? 195 GLY A C   1 
ATOM   1461  O O   . GLY A 1 195 ? 57.397  14.515  -36.323  1.00 19.20 ? 195 GLY A O   1 
ATOM   1462  N N   . ILE A 1 196 ? 55.968  15.256  -37.907  1.00 19.21 ? 196 ILE A N   1 
ATOM   1463  C CA  . ILE A 1 196 ? 54.913  15.604  -36.957  1.00 20.25 ? 196 ILE A CA  1 
ATOM   1464  C C   . ILE A 1 196 ? 53.542  15.024  -37.291  1.00 20.10 ? 196 ILE A C   1 
ATOM   1465  O O   . ILE A 1 196 ? 52.835  14.577  -36.387  1.00 19.30 ? 196 ILE A O   1 
ATOM   1466  C CB  . ILE A 1 196 ? 54.801  17.135  -36.805  1.00 21.59 ? 196 ILE A CB  1 
ATOM   1467  C CG1 . ILE A 1 196 ? 56.061  17.682  -36.114  1.00 22.58 ? 196 ILE A CG1 1 
ATOM   1468  C CG2 . ILE A 1 196 ? 53.579  17.532  -35.974  1.00 21.35 ? 196 ILE A CG2 1 
ATOM   1469  C CD1 . ILE A 1 196 ? 56.398  19.084  -36.551  1.00 23.38 ? 196 ILE A CD1 1 
ATOM   1470  N N   . HIS A 1 197 ? 53.175  15.019  -38.572  1.00 19.69 ? 197 HIS A N   1 
ATOM   1471  C CA  . HIS A 1 197 ? 51.826  14.638  -38.997  1.00 19.32 ? 197 HIS A CA  1 
ATOM   1472  C C   . HIS A 1 197 ? 51.809  13.285  -39.694  1.00 19.18 ? 197 HIS A C   1 
ATOM   1473  O O   . HIS A 1 197 ? 52.847  12.637  -39.850  1.00 18.23 ? 197 HIS A O   1 
ATOM   1474  C CB  . HIS A 1 197 ? 51.259  15.727  -39.885  1.00 19.09 ? 197 HIS A CB  1 
ATOM   1475  C CG  . HIS A 1 197 ? 51.354  17.080  -39.267  1.00 19.04 ? 197 HIS A CG  1 
ATOM   1476  N ND1 . HIS A 1 197 ? 52.326  17.992  -39.609  1.00 18.74 ? 197 HIS A ND1 1 
ATOM   1477  C CD2 . HIS A 1 197 ? 50.642  17.648  -38.269  1.00 19.13 ? 197 HIS A CD2 1 
ATOM   1478  C CE1 . HIS A 1 197 ? 52.187  19.079  -38.871  1.00 19.16 ? 197 HIS A CE1 1 
ATOM   1479  N NE2 . HIS A 1 197 ? 51.173  18.895  -38.049  1.00 19.04 ? 197 HIS A NE2 1 
ATOM   1480  N N   . PHE A 1 198 ? 50.607  12.845  -40.067  1.00 19.35 ? 198 PHE A N   1 
ATOM   1481  C CA  . PHE A 1 198 ? 50.394  11.468  -40.517  1.00 19.77 ? 198 PHE A CA  1 
ATOM   1482  C C   . PHE A 1 198 ? 50.107  11.384  -42.019  1.00 20.16 ? 198 PHE A C   1 
ATOM   1483  O O   . PHE A 1 198 ? 49.482  12.270  -42.610  1.00 19.71 ? 198 PHE A O   1 
ATOM   1484  C CB  . PHE A 1 198 ? 49.190  10.830  -39.788  1.00 19.85 ? 198 PHE A CB  1 
ATOM   1485  C CG  . PHE A 1 198 ? 49.319  10.730  -38.283  1.00 19.16 ? 198 PHE A CG  1 
ATOM   1486  C CD1 . PHE A 1 198 ? 50.545  10.833  -37.631  1.00 18.86 ? 198 PHE A CD1 1 
ATOM   1487  C CD2 . PHE A 1 198 ? 48.187  10.470  -37.524  1.00 18.67 ? 198 PHE A CD2 1 
ATOM   1488  C CE1 . PHE A 1 198 ? 50.620  10.699  -36.246  1.00 18.63 ? 198 PHE A CE1 1 
ATOM   1489  C CE2 . PHE A 1 198 ? 48.268  10.349  -36.143  1.00 18.55 ? 198 PHE A CE2 1 
ATOM   1490  C CZ  . PHE A 1 198 ? 49.485  10.457  -35.500  1.00 18.34 ? 198 PHE A CZ  1 
ATOM   1491  N N   . THR A 1 199 ? 50.524  10.272  -42.608  1.00 21.02 ? 199 THR A N   1 
ATOM   1492  C CA  . THR A 1 199 ? 50.133  9.925   -43.972  1.00 20.83 ? 199 THR A CA  1 
ATOM   1493  C C   . THR A 1 199 ? 48.729  9.329   -43.932  1.00 22.39 ? 199 THR A C   1 
ATOM   1494  O O   . THR A 1 199 ? 48.222  8.992   -42.859  1.00 23.86 ? 199 THR A O   1 
ATOM   1495  C CB  . THR A 1 199 ? 51.052  8.839   -44.556  1.00 19.64 ? 199 THR A CB  1 
ATOM   1496  O OG1 . THR A 1 199 ? 50.902  7.619   -43.801  1.00 18.81 ? 199 THR A OG1 1 
ATOM   1497  C CG2 . THR A 1 199 ? 52.503  9.294   -44.545  1.00 18.76 ? 199 THR A CG2 1 
ATOM   1498  N N   . ALA A 1 200 ? 48.124  9.177   -45.099  1.00 23.82 ? 200 ALA A N   1 
ATOM   1499  C CA  . ALA A 1 200 ? 46.819  8.542   -45.204  1.00 25.33 ? 200 ALA A CA  1 
ATOM   1500  C C   . ALA A 1 200 ? 46.851  7.074   -44.766  1.00 26.75 ? 200 ALA A C   1 
ATOM   1501  O O   . ALA A 1 200 ? 45.874  6.562   -44.209  1.00 24.85 ? 200 ALA A O   1 
ATOM   1502  C CB  . ALA A 1 200 ? 46.291  8.664   -46.626  1.00 25.58 ? 200 ALA A CB  1 
ATOM   1503  N N   . GLU A 1 201 ? 47.974  6.399   -45.015  1.00 29.32 ? 201 GLU A N   1 
ATOM   1504  C CA  . GLU A 1 201 ? 48.121  5.007   -44.595  1.00 31.69 ? 201 GLU A CA  1 
ATOM   1505  C C   . GLU A 1 201 ? 48.062  4.917   -43.058  1.00 30.45 ? 201 GLU A C   1 
ATOM   1506  O O   . GLU A 1 201 ? 47.434  4.016   -42.523  1.00 29.20 ? 201 GLU A O   1 
ATOM   1507  C CB  . GLU A 1 201 ? 49.418  4.412   -45.188  1.00 35.14 ? 201 GLU A CB  1 
ATOM   1508  C CG  . GLU A 1 201 ? 50.029  3.136   -44.555  1.00 39.56 ? 201 GLU A CG  1 
ATOM   1509  C CD  . GLU A 1 201 ? 51.579  3.169   -44.493  1.00 41.89 ? 201 GLU A CD  1 
ATOM   1510  O OE1 . GLU A 1 201 ? 52.224  3.010   -43.397  1.00 41.96 ? 201 GLU A OE1 1 
ATOM   1511  O OE2 . GLU A 1 201 ? 52.162  3.362   -45.576  1.00 42.93 ? 201 GLU A OE2 1 
ATOM   1512  N N   . THR A 1 202 ? 48.720  5.847   -42.366  1.00 29.83 ? 202 THR A N   1 
ATOM   1513  C CA  . THR A 1 202 ? 48.727  5.849   -40.904  1.00 29.32 ? 202 THR A CA  1 
ATOM   1514  C C   . THR A 1 202 ? 47.352  6.207   -40.349  1.00 29.58 ? 202 THR A C   1 
ATOM   1515  O O   . THR A 1 202 ? 46.915  5.643   -39.345  1.00 30.54 ? 202 THR A O   1 
ATOM   1516  C CB  . THR A 1 202 ? 49.778  6.822   -40.346  1.00 30.27 ? 202 THR A CB  1 
ATOM   1517  O OG1 . THR A 1 202 ? 51.077  6.264   -40.547  1.00 31.85 ? 202 THR A OG1 1 
ATOM   1518  C CG2 . THR A 1 202 ? 49.590  7.065   -38.844  1.00 29.98 ? 202 THR A CG2 1 
ATOM   1519  N N   . ASN A 1 203 ? 46.681  7.151   -40.996  1.00 29.87 ? 203 ASN A N   1 
ATOM   1520  C CA  . ASN A 1 203 ? 45.311  7.497   -40.624  1.00 31.83 ? 203 ASN A CA  1 
ATOM   1521  C C   . ASN A 1 203 ? 44.404  6.267   -40.658  1.00 33.16 ? 203 ASN A C   1 
ATOM   1522  O O   . ASN A 1 203 ? 43.642  6.026   -39.731  1.00 33.15 ? 203 ASN A O   1 
ATOM   1523  C CB  . ASN A 1 203 ? 44.733  8.566   -41.564  1.00 31.11 ? 203 ASN A CB  1 
ATOM   1524  C CG  . ASN A 1 203 ? 45.214  9.967   -41.247  1.00 30.47 ? 203 ASN A CG  1 
ATOM   1525  O OD1 . ASN A 1 203 ? 45.820  10.228  -40.198  1.00 31.60 ? 203 ASN A OD1 1 
ATOM   1526  N ND2 . ASN A 1 203 ? 44.939  10.895  -42.163  1.00 29.91 ? 203 ASN A ND2 1 
ATOM   1527  N N   . ARG A 1 204 ? 44.497  5.502   -41.745  1.00 33.75 ? 204 ARG A N   1 
ATOM   1528  C CA  . ARG A 1 204 ? 43.694  4.291   -41.930  1.00 32.17 ? 204 ARG A CA  1 
ATOM   1529  C C   . ARG A 1 204 ? 43.897  3.295   -40.803  1.00 29.24 ? 204 ARG A C   1 
ATOM   1530  O O   . ARG A 1 204 ? 42.927  2.773   -40.254  1.00 29.85 ? 204 ARG A O   1 
ATOM   1531  C CB  . ARG A 1 204 ? 43.988  3.621   -43.284  1.00 34.30 ? 204 ARG A CB  1 
ATOM   1532  C CG  . ARG A 1 204 ? 43.045  4.060   -44.397  1.00 37.19 ? 204 ARG A CG  1 
ATOM   1533  C CD  . ARG A 1 204 ? 43.282  3.311   -45.704  1.00 37.66 ? 204 ARG A CD  1 
ATOM   1534  N NE  . ARG A 1 204 ? 44.428  3.838   -46.449  1.00 38.41 ? 204 ARG A NE  1 
ATOM   1535  C CZ  . ARG A 1 204 ? 44.415  4.948   -47.203  1.00 37.17 ? 204 ARG A CZ  1 
ATOM   1536  N NH1 . ARG A 1 204 ? 43.316  5.723   -47.315  1.00 36.81 ? 204 ARG A NH1 1 
ATOM   1537  N NH2 . ARG A 1 204 ? 45.534  5.304   -47.830  1.00 36.61 ? 204 ARG A NH2 1 
ATOM   1538  N N   . THR A 1 205 ? 45.150  3.034   -40.456  1.00 26.82 ? 205 THR A N   1 
ATOM   1539  C CA  . THR A 1 205 ? 45.456  2.096   -39.383  1.00 26.02 ? 205 THR A CA  1 
ATOM   1540  C C   . THR A 1 205 ? 44.833  2.577   -38.069  1.00 25.73 ? 205 THR A C   1 
ATOM   1541  O O   . THR A 1 205 ? 44.168  1.802   -37.370  1.00 25.11 ? 205 THR A O   1 
ATOM   1542  C CB  . THR A 1 205 ? 46.973  1.911   -39.206  1.00 25.12 ? 205 THR A CB  1 
ATOM   1543  O OG1 . THR A 1 205 ? 47.559  1.609   -40.471  1.00 26.14 ? 205 THR A OG1 1 
ATOM   1544  C CG2 . THR A 1 205 ? 47.281  0.783   -38.235  1.00 24.25 ? 205 THR A CG2 1 
ATOM   1545  N N   . LEU A 1 206 ? 45.037  3.860   -37.756  1.00 24.53 ? 206 LEU A N   1 
ATOM   1546  C CA  . LEU A 1 206 ? 44.549  4.456   -36.507  1.00 23.25 ? 206 LEU A CA  1 
ATOM   1547  C C   . LEU A 1 206 ? 43.035  4.428   -36.418  1.00 22.06 ? 206 LEU A C   1 
ATOM   1548  O O   . LEU A 1 206 ? 42.482  4.067   -35.379  1.00 23.85 ? 206 LEU A O   1 
ATOM   1549  C CB  . LEU A 1 206 ? 45.047  5.906   -36.362  1.00 22.82 ? 206 LEU A CB  1 
ATOM   1550  C CG  . LEU A 1 206 ? 44.683  6.639   -35.064  1.00 21.78 ? 206 LEU A CG  1 
ATOM   1551  C CD1 . LEU A 1 206 ? 45.165  5.858   -33.857  1.00 22.14 ? 206 LEU A CD1 1 
ATOM   1552  C CD2 . LEU A 1 206 ? 45.259  8.030   -35.023  1.00 21.11 ? 206 LEU A CD2 1 
ATOM   1553  N N   . GLY A 1 207 ? 42.373  4.812   -37.499  1.00 20.19 ? 207 GLY A N   1 
ATOM   1554  C CA  . GLY A 1 207 ? 40.926  4.817   -37.551  1.00 20.16 ? 207 GLY A CA  1 
ATOM   1555  C C   . GLY A 1 207 ? 40.335  3.465   -37.242  1.00 20.45 ? 207 GLY A C   1 
ATOM   1556  O O   . GLY A 1 207 ? 39.380  3.352   -36.460  1.00 20.33 ? 207 GLY A O   1 
ATOM   1557  N N   . ALA A 1 208 ? 40.917  2.432   -37.847  1.00 21.20 ? 208 ALA A N   1 
ATOM   1558  C CA  . ALA A 1 208 ? 40.424  1.060   -37.682  1.00 21.00 ? 208 ALA A CA  1 
ATOM   1559  C C   . ALA A 1 208 ? 40.689  0.553   -36.270  1.00 20.60 ? 208 ALA A C   1 
ATOM   1560  O O   . ALA A 1 208 ? 39.837  -0.110  -35.696  1.00 21.10 ? 208 ALA A O   1 
ATOM   1561  C CB  . ALA A 1 208 ? 41.050  0.135   -38.708  1.00 21.06 ? 208 ALA A CB  1 
ATOM   1562  N N   . ALA A 1 209 ? 41.861  0.873   -35.723  1.00 20.11 ? 209 ALA A N   1 
ATOM   1563  C CA  . ALA A 1 209 ? 42.225  0.468   -34.363  1.00 20.13 ? 209 ALA A CA  1 
ATOM   1564  C C   . ALA A 1 209 ? 41.353  1.142   -33.336  1.00 19.79 ? 209 ALA A C   1 
ATOM   1565  O O   . ALA A 1 209 ? 40.878  0.498   -32.411  1.00 21.59 ? 209 ALA A O   1 
ATOM   1566  C CB  . ALA A 1 209 ? 43.684  0.780   -34.074  1.00 20.34 ? 209 ALA A CB  1 
ATOM   1567  N N   . VAL A 1 210 ? 41.137  2.441   -33.492  1.00 19.64 ? 210 VAL A N   1 
ATOM   1568  C CA  . VAL A 1 210 ? 40.317  3.200   -32.530  1.00 19.36 ? 210 VAL A CA  1 
ATOM   1569  C C   . VAL A 1 210 ? 38.856  2.742   -32.565  1.00 18.68 ? 210 VAL A C   1 
ATOM   1570  O O   . VAL A 1 210 ? 38.201  2.711   -31.534  1.00 18.27 ? 210 VAL A O   1 
ATOM   1571  C CB  . VAL A 1 210 ? 40.451  4.729   -32.747  1.00 18.91 ? 210 VAL A CB  1 
ATOM   1572  C CG1 . VAL A 1 210 ? 39.460  5.499   -31.886  1.00 18.95 ? 210 VAL A CG1 1 
ATOM   1573  C CG2 . VAL A 1 210 ? 41.870  5.178   -32.436  1.00 18.35 ? 210 VAL A CG2 1 
ATOM   1574  N N   . ALA A 1 211 ? 38.369  2.365   -33.744  1.00 19.06 ? 211 ALA A N   1 
ATOM   1575  C CA  . ALA A 1 211 ? 37.013  1.835   -33.879  1.00 19.57 ? 211 ALA A CA  1 
ATOM   1576  C C   . ALA A 1 211 ? 36.786  0.578   -33.040  1.00 20.08 ? 211 ALA A C   1 
ATOM   1577  O O   . ALA A 1 211 ? 35.711  0.432   -32.449  1.00 18.89 ? 211 ALA A O   1 
ATOM   1578  C CB  . ALA A 1 211 ? 36.693  1.564   -35.342  1.00 19.47 ? 211 ALA A CB  1 
ATOM   1579  N N   . GLN A 1 212 ? 37.780  -0.316  -32.993  1.00 21.88 ? 212 GLN A N   1 
ATOM   1580  C CA  . GLN A 1 212 ? 37.703  -1.512  -32.151  1.00 24.51 ? 212 GLN A CA  1 
ATOM   1581  C C   . GLN A 1 212 ? 37.549  -1.103  -30.700  1.00 24.41 ? 212 GLN A C   1 
ATOM   1582  O O   . GLN A 1 212 ? 36.684  -1.608  -29.979  1.00 25.49 ? 212 GLN A O   1 
ATOM   1583  C CB  . GLN A 1 212 ? 38.957  -2.393  -32.274  1.00 27.92 ? 212 GLN A CB  1 
ATOM   1584  C CG  . GLN A 1 212 ? 39.226  -2.990  -33.637  1.00 32.00 ? 212 GLN A CG  1 
ATOM   1585  C CD  . GLN A 1 212 ? 39.860  -4.408  -33.578  1.00 34.09 ? 212 GLN A CD  1 
ATOM   1586  O OE1 . GLN A 1 212 ? 40.744  -4.716  -32.765  1.00 34.16 ? 212 GLN A OE1 1 
ATOM   1587  N NE2 . GLN A 1 212 ? 39.387  -5.272  -34.447  1.00 35.28 ? 212 GLN A NE2 1 
ATOM   1588  N N   . LYS A 1 213 ? 38.387  -0.172  -30.276  1.00 24.71 ? 213 LYS A N   1 
ATOM   1589  C CA  . LYS A 1 213 ? 38.375  0.308   -28.913  1.00 25.83 ? 213 LYS A CA  1 
ATOM   1590  C C   . LYS A 1 213 ? 37.027  0.920   -28.536  1.00 23.93 ? 213 LYS A C   1 
ATOM   1591  O O   . LYS A 1 213 ? 36.469  0.621   -27.483  1.00 23.28 ? 213 LYS A O   1 
ATOM   1592  C CB  . LYS A 1 213 ? 39.516  1.312   -28.715  1.00 28.40 ? 213 LYS A CB  1 
ATOM   1593  C CG  . LYS A 1 213 ? 39.672  1.764   -27.275  1.00 31.43 ? 213 LYS A CG  1 
ATOM   1594  C CD  . LYS A 1 213 ? 39.855  0.616   -26.282  1.00 33.04 ? 213 LYS A CD  1 
ATOM   1595  C CE  . LYS A 1 213 ? 40.344  1.207   -24.972  1.00 34.76 ? 213 LYS A CE  1 
ATOM   1596  N NZ  . LYS A 1 213 ? 40.101  0.357   -23.798  1.00 34.86 ? 213 LYS A NZ  1 
ATOM   1597  N N   . VAL A 1 214 ? 36.499  1.757   -29.411  1.00 23.90 ? 214 VAL A N   1 
ATOM   1598  C CA  . VAL A 1 214 ? 35.212  2.413   -29.170  1.00 25.09 ? 214 VAL A CA  1 
ATOM   1599  C C   . VAL A 1 214 ? 34.085  1.390   -28.944  1.00 26.54 ? 214 VAL A C   1 
ATOM   1600  O O   . VAL A 1 214 ? 33.336  1.504   -27.972  1.00 26.87 ? 214 VAL A O   1 
ATOM   1601  C CB  . VAL A 1 214 ? 34.836  3.366   -30.328  1.00 24.91 ? 214 VAL A CB  1 
ATOM   1602  C CG1 . VAL A 1 214 ? 33.383  3.811   -30.232  1.00 24.95 ? 214 VAL A CG1 1 
ATOM   1603  C CG2 . VAL A 1 214 ? 35.755  4.567   -30.332  1.00 24.28 ? 214 VAL A CG2 1 
ATOM   1604  N N   . LYS A 1 215 ? 33.983  0.392   -29.829  1.00 27.85 ? 215 LYS A N   1 
ATOM   1605  C CA  . LYS A 1 215 ? 32.951  -0.639  -29.715  1.00 28.07 ? 215 LYS A CA  1 
ATOM   1606  C C   . LYS A 1 215 ? 33.016  -1.408  -28.393  1.00 28.21 ? 215 LYS A C   1 
ATOM   1607  O O   . LYS A 1 215 ? 31.975  -1.752  -27.803  1.00 27.45 ? 215 LYS A O   1 
ATOM   1608  C CB  . LYS A 1 215 ? 33.061  -1.629  -30.860  1.00 28.90 ? 215 LYS A CB  1 
ATOM   1609  C CG  . LYS A 1 215 ? 32.623  -1.082  -32.207  1.00 30.32 ? 215 LYS A CG  1 
ATOM   1610  C CD  . LYS A 1 215 ? 32.900  -2.119  -33.277  1.00 31.94 ? 215 LYS A CD  1 
ATOM   1611  C CE  . LYS A 1 215 ? 32.670  -1.579  -34.664  1.00 33.06 ? 215 LYS A CE  1 
ATOM   1612  N NZ  . LYS A 1 215 ? 33.008  -2.615  -35.673  1.00 35.20 ? 215 LYS A NZ  1 
ATOM   1613  N N   . THR A 1 216 ? 34.236  -1.689  -27.940  1.00 27.50 ? 216 THR A N   1 
ATOM   1614  C CA  . THR A 1 216 ? 34.452  -2.246  -26.607  1.00 28.14 ? 216 THR A CA  1 
ATOM   1615  C C   . THR A 1 216 ? 33.779  -1.417  -25.507  1.00 27.61 ? 216 THR A C   1 
ATOM   1616  O O   . THR A 1 216 ? 33.203  -1.970  -24.573  1.00 27.70 ? 216 THR A O   1 
ATOM   1617  C CB  . THR A 1 216 ? 35.959  -2.359  -26.304  1.00 28.21 ? 216 THR A CB  1 
ATOM   1618  O OG1 . THR A 1 216 ? 36.511  -3.389  -27.124  1.00 27.21 ? 216 THR A OG1 1 
ATOM   1619  C CG2 . THR A 1 216 ? 36.236  -2.677  -24.825  1.00 28.50 ? 216 THR A CG2 1 
ATOM   1620  N N   . LEU A 1 217 ? 33.861  -0.096  -25.622  1.00 27.00 ? 217 LEU A N   1 
ATOM   1621  C CA  . LEU A 1 217 ? 33.306  0.798   -24.604  1.00 26.97 ? 217 LEU A CA  1 
ATOM   1622  C C   . LEU A 1 217 ? 31.808  1.000   -24.689  1.00 25.84 ? 217 LEU A C   1 
ATOM   1623  O O   . LEU A 1 217 ? 31.157  1.101   -23.665  1.00 24.80 ? 217 LEU A O   1 
ATOM   1624  C CB  . LEU A 1 217 ? 33.998  2.170   -24.660  1.00 27.21 ? 217 LEU A CB  1 
ATOM   1625  C CG  . LEU A 1 217 ? 35.509  2.176   -24.413  1.00 27.37 ? 217 LEU A CG  1 
ATOM   1626  C CD1 . LEU A 1 217 ? 36.000  3.591   -24.706  1.00 27.24 ? 217 LEU A CD1 1 
ATOM   1627  C CD2 . LEU A 1 217 ? 35.890  1.620   -23.022  1.00 26.94 ? 217 LEU A CD2 1 
ATOM   1628  N N   . LEU A 1 218 ? 31.257  1.050   -25.896  1.00 27.00 ? 218 LEU A N   1 
ATOM   1629  C CA  . LEU A 1 218 ? 29.843  1.395   -26.063  1.00 29.57 ? 218 LEU A CA  1 
ATOM   1630  C C   . LEU A 1 218 ? 28.872  0.224   -26.306  1.00 30.00 ? 218 LEU A C   1 
ATOM   1631  O O   . LEU A 1 218 ? 27.655  0.393   -26.182  1.00 27.82 ? 218 LEU A O   1 
ATOM   1632  C CB  . LEU A 1 218 ? 29.723  2.450   -27.166  1.00 30.48 ? 218 LEU A CB  1 
ATOM   1633  C CG  . LEU A 1 218 ? 30.486  3.769   -26.915  1.00 30.97 ? 218 LEU A CG  1 
ATOM   1634  C CD1 . LEU A 1 218 ? 30.226  4.714   -28.087  1.00 31.37 ? 218 LEU A CD1 1 
ATOM   1635  C CD2 . LEU A 1 218 ? 30.131  4.428   -25.576  1.00 30.25 ? 218 LEU A CD2 1 
ATOM   1636  N N   . GLN A 1 219 ? 29.426  -0.951  -26.599  1.00 31.08 ? 219 GLN A N   1 
ATOM   1637  C CA  . GLN A 1 219 ? 28.662  -2.174  -26.622  1.00 31.53 ? 219 GLN A CA  1 
ATOM   1638  C C   . GLN A 1 219 ? 29.334  -3.133  -25.620  1.00 33.96 ? 219 GLN A C   1 
ATOM   1639  O O   . GLN A 1 219 ? 29.828  -4.180  -26.015  1.00 37.72 ? 219 GLN A O   1 
ATOM   1640  C CB  . GLN A 1 219 ? 28.642  -2.724  -28.066  1.00 30.71 ? 219 GLN A CB  1 
ATOM   1641  C CG  . GLN A 1 219 ? 28.258  -1.648  -29.103  1.00 31.07 ? 219 GLN A CG  1 
ATOM   1642  C CD  . GLN A 1 219 ? 28.188  -2.113  -30.545  1.00 31.04 ? 219 GLN A CD  1 
ATOM   1643  O OE1 . GLN A 1 219 ? 28.610  -1.419  -31.483  1.00 30.11 ? 219 GLN A OE1 1 
ATOM   1644  N NE2 . GLN A 1 219 ? 27.628  -3.287  -30.733  1.00 31.78 ? 219 GLN A NE2 1 
ATOM   1645  N N   . PRO A 1 220 ? 29.394  -2.759  -24.322  1.00 33.25 ? 220 PRO A N   1 
ATOM   1646  C CA  . PRO A 1 220 ? 30.278  -3.473  -23.388  1.00 32.37 ? 220 PRO A CA  1 
ATOM   1647  C C   . PRO A 1 220 ? 29.789  -4.867  -23.008  1.00 31.43 ? 220 PRO A C   1 
ATOM   1648  O O   . PRO A 1 220 ? 30.614  -5.765  -22.818  1.00 29.94 ? 220 PRO A O   1 
ATOM   1649  C CB  . PRO A 1 220 ? 30.323  -2.547  -22.171  1.00 32.75 ? 220 PRO A CB  1 
ATOM   1650  C CG  . PRO A 1 220 ? 28.985  -1.850  -22.183  1.00 32.82 ? 220 PRO A CG  1 
ATOM   1651  C CD  . PRO A 1 220 ? 28.528  -1.789  -23.624  1.00 33.32 ? 220 PRO A CD  1 
ATOM   1652  N N   . LYS A 1 221 ? 28.465  -5.032  -22.895  1.00 32.82 ? 221 LYS A N   1 
ATOM   1653  C CA  . LYS A 1 221 ? 27.830  -6.363  -22.784  1.00 34.29 ? 221 LYS A CA  1 
ATOM   1654  C C   . LYS A 1 221 ? 28.337  -7.327  -23.882  1.00 32.47 ? 221 LYS A C   1 
ATOM   1655  O O   . LYS A 1 221 ? 28.607  -8.499  -23.613  1.00 29.00 ? 221 LYS A O   1 
ATOM   1656  C CB  . LYS A 1 221 ? 26.304  -6.273  -22.925  1.00 35.82 ? 221 LYS A CB  1 
ATOM   1657  C CG  . LYS A 1 221 ? 25.516  -5.871  -21.691  1.00 38.01 ? 221 LYS A CG  1 
ATOM   1658  C CD  . LYS A 1 221 ? 24.018  -6.119  -21.946  1.00 41.45 ? 221 LYS A CD  1 
ATOM   1659  C CE  . LYS A 1 221 ? 23.055  -5.086  -21.316  1.00 43.10 ? 221 LYS A CE  1 
ATOM   1660  N NZ  . LYS A 1 221 ? 23.290  -4.929  -19.855  1.00 44.79 ? 221 LYS A NZ  1 
ATOM   1661  N N   . LEU A 1 222 ? 28.447  -6.818  -25.115  1.00 31.68 ? 222 LEU A N   1 
ATOM   1662  C CA  . LEU A 1 222 ? 28.941  -7.591  -26.228  1.00 31.07 ? 222 LEU A CA  1 
ATOM   1663  C C   . LEU A 1 222 ? 30.439  -7.780  -26.104  1.00 32.27 ? 222 LEU A C   1 
ATOM   1664  O O   . LEU A 1 222 ? 30.932  -8.882  -26.294  1.00 33.49 ? 222 LEU A O   1 
ATOM   1665  C CB  . LEU A 1 222 ? 28.605  -6.899  -27.553  1.00 31.53 ? 222 LEU A CB  1 
ATOM   1666  C CG  . LEU A 1 222 ? 29.197  -7.530  -28.816  1.00 31.97 ? 222 LEU A CG  1 
ATOM   1667  C CD1 . LEU A 1 222 ? 28.759  -8.991  -28.897  1.00 32.92 ? 222 LEU A CD1 1 
ATOM   1668  C CD2 . LEU A 1 222 ? 28.798  -6.734  -30.053  1.00 30.69 ? 222 LEU A CD2 1 
ATOM   1669  N N   . ALA A 1 223 ? 31.168  -6.709  -25.795  1.00 32.08 ? 223 ALA A N   1 
ATOM   1670  C CA  . ALA A 1 223 ? 32.614  -6.813  -25.592  1.00 33.38 ? 223 ALA A CA  1 
ATOM   1671  C C   . ALA A 1 223 ? 32.907  -7.899  -24.587  1.00 34.16 ? 223 ALA A C   1 
ATOM   1672  O O   . ALA A 1 223 ? 33.754  -8.761  -24.845  1.00 34.16 ? 223 ALA A O   1 
ATOM   1673  C CB  . ALA A 1 223 ? 33.202  -5.492  -25.113  1.00 33.62 ? 223 ALA A CB  1 
ATOM   1674  N N   . ALA A 1 224 ? 32.197  -7.857  -23.454  1.00 36.24 ? 224 ALA A N   1 
ATOM   1675  C CA  . ALA A 1 224 ? 32.335  -8.860  -22.389  1.00 38.36 ? 224 ALA A CA  1 
ATOM   1676  C C   . ALA A 1 224 ? 32.188  -10.293 -22.927  1.00 39.75 ? 224 ALA A C   1 
ATOM   1677  O O   . ALA A 1 224 ? 33.111  -11.105 -22.828  1.00 38.00 ? 224 ALA A O   1 
ATOM   1678  C CB  . ALA A 1 224 ? 31.313  -8.605  -21.293  1.00 38.15 ? 224 ALA A CB  1 
ATOM   1679  N N   . ALA A 1 225 ? 31.030  -10.564 -23.531  1.00 42.27 ? 225 ALA A N   1 
ATOM   1680  C CA  . ALA A 1 225 ? 30.708  -11.880 -24.086  1.00 42.45 ? 225 ALA A CA  1 
ATOM   1681  C C   . ALA A 1 225 ? 31.764  -12.391 -25.077  1.00 45.68 ? 225 ALA A C   1 
ATOM   1682  O O   . ALA A 1 225 ? 32.040  -13.585 -25.145  1.00 48.27 ? 225 ALA A O   1 
ATOM   1683  C CB  . ALA A 1 225 ? 29.347  -11.837 -24.757  1.00 41.21 ? 225 ALA A CB  1 
ATOM   1684  N N   . LEU A 1 226 ? 32.354  -11.484 -25.848  1.00 49.86 ? 226 LEU A N   1 
ATOM   1685  C CA  . LEU A 1 226 ? 33.366  -11.856 -26.838  1.00 53.02 ? 226 LEU A CA  1 
ATOM   1686  C C   . LEU A 1 226 ? 34.671  -12.354 -26.218  1.00 56.32 ? 226 LEU A C   1 
ATOM   1687  O O   . LEU A 1 226 ? 35.301  -13.246 -26.798  1.00 61.80 ? 226 LEU A O   1 
ATOM   1688  C CB  . LEU A 1 226 ? 33.675  -10.681 -27.786  1.00 52.38 ? 226 LEU A CB  1 
ATOM   1689  C CG  . LEU A 1 226 ? 32.695  -10.384 -28.903  1.00 50.48 ? 226 LEU A CG  1 
ATOM   1690  C CD1 . LEU A 1 226 ? 33.132  -9.092  -29.574  1.00 49.73 ? 226 LEU A CD1 1 
ATOM   1691  C CD2 . LEU A 1 226 ? 32.628  -11.535 -29.897  1.00 49.28 ? 226 LEU A CD2 1 
ATOM   1692  N N   . GLU A 1 227 ? 35.072  -11.825 -25.053  1.00 57.41 ? 227 GLU A N   1 
ATOM   1693  C CA  . GLU A 1 227 ? 36.427  -12.038 -24.535  1.00 58.60 ? 227 GLU A CA  1 
ATOM   1694  C C   . GLU A 1 227 ? 36.917  -13.509 -24.468  1.00 64.81 ? 227 GLU A C   1 
ATOM   1695  O O   . GLU A 1 227 ? 38.119  -13.765 -24.585  1.00 74.38 ? 227 GLU A O   1 
ATOM   1696  C CB  . GLU A 1 227 ? 36.589  -11.344 -23.181  1.00 59.46 ? 227 GLU A CB  1 
ATOM   1697  C CG  . GLU A 1 227 ? 36.777  -9.832  -23.269  1.00 60.69 ? 227 GLU A CG  1 
ATOM   1698  C CD  . GLU A 1 227 ? 38.142  -9.348  -22.798  1.00 62.67 ? 227 GLU A CD  1 
ATOM   1699  O OE1 . GLU A 1 227 ? 39.114  -10.128 -22.903  1.00 66.90 ? 227 GLU A OE1 1 
ATOM   1700  O OE2 . GLU A 1 227 ? 38.236  -8.192  -22.325  1.00 59.47 ? 227 GLU A OE2 1 
ATOM   1701  N N   . HIS A 1 228 ? 35.995  -14.464 -24.340  1.00 65.18 ? 228 HIS A N   1 
ATOM   1702  C CA  . HIS A 1 228 ? 36.336  -15.904 -24.483  1.00 63.37 ? 228 HIS A CA  1 
ATOM   1703  C C   . HIS A 1 228 ? 36.803  -16.330 -25.915  1.00 52.32 ? 228 HIS A C   1 
ATOM   1704  O O   . HIS A 1 228 ? 37.980  -16.183 -26.287  1.00 39.78 ? 228 HIS A O   1 
ATOM   1705  C CB  . HIS A 1 228 ? 35.171  -16.766 -23.946  1.00 67.73 ? 228 HIS A CB  1 
ATOM   1706  C CG  . HIS A 1 228 ? 34.141  -17.183 -24.970  1.00 75.68 ? 228 HIS A CG  1 
ATOM   1707  N ND1 . HIS A 1 228 ? 33.189  -18.142 -24.689  1.00 75.77 ? 228 HIS A ND1 1 
ATOM   1708  C CD2 . HIS A 1 228 ? 33.914  -16.801 -26.254  1.00 76.44 ? 228 HIS A CD2 1 
ATOM   1709  C CE1 . HIS A 1 228 ? 32.418  -18.328 -25.746  1.00 73.15 ? 228 HIS A CE1 1 
ATOM   1710  N NE2 . HIS A 1 228 ? 32.840  -17.530 -26.711  1.00 75.60 ? 228 HIS A NE2 1 
ATOM   1711  N N   . GLN B 1 1   ? 44.942  1.947   -51.890  1.00 78.57 ? 1   GLN B N   1 
ATOM   1712  C CA  . GLN B 1 1   ? 45.954  1.068   -52.532  1.00 79.12 ? 1   GLN B CA  1 
ATOM   1713  C C   . GLN B 1 1   ? 45.756  -0.372  -52.090  1.00 79.02 ? 1   GLN B C   1 
ATOM   1714  O O   . GLN B 1 1   ? 45.539  -1.252  -52.930  1.00 82.59 ? 1   GLN B O   1 
ATOM   1715  C CB  . GLN B 1 1   ? 47.368  1.550   -52.195  1.00 81.18 ? 1   GLN B CB  1 
ATOM   1716  C CG  . GLN B 1 1   ? 48.421  1.120   -53.211  1.00 81.37 ? 1   GLN B CG  1 
ATOM   1717  C CD  . GLN B 1 1   ? 49.486  2.173   -53.406  1.00 80.47 ? 1   GLN B CD  1 
ATOM   1718  O OE1 . GLN B 1 1   ? 49.973  2.389   -54.515  1.00 80.71 ? 1   GLN B OE1 1 
ATOM   1719  N NE2 . GLN B 1 1   ? 49.841  2.851   -52.327  1.00 81.59 ? 1   GLN B NE2 1 
ATOM   1720  N N   . ASP B 1 2   ? 45.825  -0.590  -50.773  1.00 75.31 ? 2   ASP B N   1 
ATOM   1721  C CA  . ASP B 1 2   ? 45.514  -1.882  -50.134  1.00 74.46 ? 2   ASP B CA  1 
ATOM   1722  C C   . ASP B 1 2   ? 44.299  -2.617  -50.739  1.00 73.26 ? 2   ASP B C   1 
ATOM   1723  O O   . ASP B 1 2   ? 43.158  -2.151  -50.627  1.00 73.98 ? 2   ASP B O   1 
ATOM   1724  C CB  . ASP B 1 2   ? 45.271  -1.671  -48.639  1.00 70.12 ? 2   ASP B CB  1 
ATOM   1725  C CG  . ASP B 1 2   ? 46.539  -1.817  -47.814  1.00 67.27 ? 2   ASP B CG  1 
ATOM   1726  O OD1 . ASP B 1 2   ? 47.523  -2.455  -48.249  1.00 61.74 ? 2   ASP B OD1 1 
ATOM   1727  O OD2 . ASP B 1 2   ? 46.522  -1.327  -46.686  1.00 67.02 ? 2   ASP B OD2 1 
ATOM   1728  N N   . LYS B 1 3   ? 44.587  -3.759  -51.360  1.00 65.01 ? 3   LYS B N   1 
ATOM   1729  C CA  . LYS B 1 3   ? 43.592  -4.652  -51.932  1.00 56.48 ? 3   LYS B CA  1 
ATOM   1730  C C   . LYS B 1 3   ? 42.401  -4.914  -50.988  1.00 49.38 ? 3   LYS B C   1 
ATOM   1731  O O   . LYS B 1 3   ? 42.617  -5.195  -49.815  1.00 48.58 ? 3   LYS B O   1 
ATOM   1732  C CB  . LYS B 1 3   ? 44.286  -5.981  -52.315  1.00 57.64 ? 3   LYS B CB  1 
ATOM   1733  C CG  . LYS B 1 3   ? 43.415  -6.985  -53.078  1.00 59.88 ? 3   LYS B CG  1 
ATOM   1734  C CD  . LYS B 1 3   ? 44.193  -7.765  -54.143  1.00 60.26 ? 3   LYS B CD  1 
ATOM   1735  C CE  . LYS B 1 3   ? 43.320  -8.066  -55.355  1.00 58.69 ? 3   LYS B CE  1 
ATOM   1736  N NZ  . LYS B 1 3   ? 43.664  -9.403  -55.892  1.00 57.19 ? 3   LYS B NZ  1 
ATOM   1737  N N   . ILE B 1 4   ? 41.184  -4.794  -51.520  1.00 43.76 ? 4   ILE B N   1 
ATOM   1738  C CA  . ILE B 1 4   ? 39.959  -4.999  -50.784  1.00 40.08 ? 4   ILE B CA  1 
ATOM   1739  C C   . ILE B 1 4   ? 39.757  -6.492  -50.509  1.00 37.38 ? 4   ILE B C   1 
ATOM   1740  O O   . ILE B 1 4   ? 39.868  -7.320  -51.420  1.00 34.32 ? 4   ILE B O   1 
ATOM   1741  C CB  . ILE B 1 4   ? 38.733  -4.448  -51.576  1.00 37.38 ? 4   ILE B CB  1 
ATOM   1742  C CG1 . ILE B 1 4   ? 38.829  -2.920  -51.690  1.00 37.85 ? 4   ILE B CG1 1 
ATOM   1743  C CG2 . ILE B 1 4   ? 37.410  -4.806  -50.904  1.00 35.28 ? 4   ILE B CG2 1 
ATOM   1744  C CD1 . ILE B 1 4   ? 37.928  -2.319  -52.756  1.00 37.99 ? 4   ILE B CD1 1 
ATOM   1745  N N   . LYS B 1 5   ? 39.459  -6.814  -49.252  1.00 35.18 ? 5   LYS B N   1 
ATOM   1746  C CA  . LYS B 1 5   ? 39.347  -8.203  -48.809  1.00 32.05 ? 5   LYS B CA  1 
ATOM   1747  C C   . LYS B 1 5   ? 37.955  -8.789  -49.023  1.00 28.29 ? 5   LYS B C   1 
ATOM   1748  O O   . LYS B 1 5   ? 36.949  -8.227  -48.585  1.00 25.37 ? 5   LYS B O   1 
ATOM   1749  C CB  . LYS B 1 5   ? 39.739  -8.303  -47.333  1.00 34.23 ? 5   LYS B CB  1 
ATOM   1750  C CG  . LYS B 1 5   ? 41.233  -8.159  -47.174  1.00 36.98 ? 5   LYS B CG  1 
ATOM   1751  C CD  . LYS B 1 5   ? 41.691  -8.046  -45.737  1.00 37.29 ? 5   LYS B CD  1 
ATOM   1752  C CE  . LYS B 1 5   ? 43.208  -7.993  -45.721  1.00 37.94 ? 5   LYS B CE  1 
ATOM   1753  N NZ  . LYS B 1 5   ? 43.725  -7.058  -44.687  1.00 39.13 ? 5   LYS B NZ  1 
ATOM   1754  N N   . ARG B 1 6   ? 37.904  -9.938  -49.685  1.00 26.15 ? 6   ARG B N   1 
ATOM   1755  C CA  . ARG B 1 6   ? 36.631  -10.538 -50.078  1.00 25.17 ? 6   ARG B CA  1 
ATOM   1756  C C   . ARG B 1 6   ? 36.217  -11.668 -49.121  1.00 23.12 ? 6   ARG B C   1 
ATOM   1757  O O   . ARG B 1 6   ? 36.963  -12.633 -48.925  1.00 22.95 ? 6   ARG B O   1 
ATOM   1758  C CB  . ARG B 1 6   ? 36.708  -11.008 -51.531  1.00 25.16 ? 6   ARG B CB  1 
ATOM   1759  C CG  . ARG B 1 6   ? 36.768  -9.839  -52.514  1.00 25.93 ? 6   ARG B CG  1 
ATOM   1760  C CD  . ARG B 1 6   ? 37.115  -10.233 -53.948  1.00 26.09 ? 6   ARG B CD  1 
ATOM   1761  N NE  . ARG B 1 6   ? 36.339  -11.375 -54.425  1.00 26.77 ? 6   ARG B NE  1 
ATOM   1762  C CZ  . ARG B 1 6   ? 35.027  -11.348 -54.686  1.00 28.09 ? 6   ARG B CZ  1 
ATOM   1763  N NH1 . ARG B 1 6   ? 34.305  -10.221 -54.501  1.00 28.73 ? 6   ARG B NH1 1 
ATOM   1764  N NH2 . ARG B 1 6   ? 34.407  -12.459 -55.083  1.00 27.61 ? 6   ARG B NH2 1 
ATOM   1765  N N   . VAL B 1 7   ? 35.040  -11.520 -48.504  1.00 20.48 ? 7   VAL B N   1 
ATOM   1766  C CA  . VAL B 1 7   ? 34.528  -12.501 -47.558  1.00 19.45 ? 7   VAL B CA  1 
ATOM   1767  C C   . VAL B 1 7   ? 33.220  -13.139 -48.064  1.00 18.90 ? 7   VAL B C   1 
ATOM   1768  O O   . VAL B 1 7   ? 32.230  -12.456 -48.314  1.00 18.11 ? 7   VAL B O   1 
ATOM   1769  C CB  . VAL B 1 7   ? 34.279  -11.861 -46.187  1.00 19.21 ? 7   VAL B CB  1 
ATOM   1770  C CG1 . VAL B 1 7   ? 33.749  -12.895 -45.190  1.00 19.05 ? 7   VAL B CG1 1 
ATOM   1771  C CG2 . VAL B 1 7   ? 35.567  -11.240 -45.669  1.00 18.93 ? 7   VAL B CG2 1 
ATOM   1772  N N   . PHE B 1 8   ? 33.232  -14.460 -48.205  1.00 18.36 ? 8   PHE B N   1 
ATOM   1773  C CA  . PHE B 1 8   ? 32.083  -15.200 -48.702  1.00 17.78 ? 8   PHE B CA  1 
ATOM   1774  C C   . PHE B 1 8   ? 31.363  -15.839 -47.524  1.00 17.63 ? 8   PHE B C   1 
ATOM   1775  O O   . PHE B 1 8   ? 31.978  -16.544 -46.732  1.00 17.58 ? 8   PHE B O   1 
ATOM   1776  C CB  . PHE B 1 8   ? 32.536  -16.274 -49.688  1.00 16.94 ? 8   PHE B CB  1 
ATOM   1777  C CG  . PHE B 1 8   ? 31.419  -17.115 -50.223  1.00 16.67 ? 8   PHE B CG  1 
ATOM   1778  C CD1 . PHE B 1 8   ? 30.285  -16.532 -50.755  1.00 16.32 ? 8   PHE B CD1 1 
ATOM   1779  C CD2 . PHE B 1 8   ? 31.515  -18.507 -50.221  1.00 16.63 ? 8   PHE B CD2 1 
ATOM   1780  C CE1 . PHE B 1 8   ? 29.262  -17.311 -51.259  1.00 16.47 ? 8   PHE B CE1 1 
ATOM   1781  C CE2 . PHE B 1 8   ? 30.496  -19.292 -50.736  1.00 16.29 ? 8   PHE B CE2 1 
ATOM   1782  C CZ  . PHE B 1 8   ? 29.365  -18.694 -51.250  1.00 16.30 ? 8   PHE B CZ  1 
ATOM   1783  N N   . VAL B 1 9   ? 30.064  -15.581 -47.412  1.00 17.34 ? 9   VAL B N   1 
ATOM   1784  C CA  . VAL B 1 9   ? 29.257  -16.124 -46.323  1.00 17.60 ? 9   VAL B CA  1 
ATOM   1785  C C   . VAL B 1 9   ? 28.280  -17.156 -46.853  1.00 17.56 ? 9   VAL B C   1 
ATOM   1786  O O   . VAL B 1 9   ? 27.440  -16.852 -47.700  1.00 16.89 ? 9   VAL B O   1 
ATOM   1787  C CB  . VAL B 1 9   ? 28.439  -15.028 -45.610  1.00 18.24 ? 9   VAL B CB  1 
ATOM   1788  C CG1 . VAL B 1 9   ? 27.817  -15.592 -44.344  1.00 18.25 ? 9   VAL B CG1 1 
ATOM   1789  C CG2 . VAL B 1 9   ? 29.317  -13.829 -45.277  1.00 18.57 ? 9   VAL B CG2 1 
ATOM   1790  N N   . PHE B 1 10  ? 28.382  -18.371 -46.331  1.00 18.34 ? 10  PHE B N   1 
ATOM   1791  C CA  . PHE B 1 10  ? 27.646  -19.517 -46.842  1.00 18.37 ? 10  PHE B CA  1 
ATOM   1792  C C   . PHE B 1 10  ? 26.786  -20.042 -45.717  1.00 19.12 ? 10  PHE B C   1 
ATOM   1793  O O   . PHE B 1 10  ? 27.306  -20.566 -44.725  1.00 19.46 ? 10  PHE B O   1 
ATOM   1794  C CB  . PHE B 1 10  ? 28.650  -20.576 -47.293  1.00 18.44 ? 10  PHE B CB  1 
ATOM   1795  C CG  . PHE B 1 10  ? 28.045  -21.722 -48.030  1.00 18.58 ? 10  PHE B CG  1 
ATOM   1796  C CD1 . PHE B 1 10  ? 27.384  -21.514 -49.219  1.00 19.01 ? 10  PHE B CD1 1 
ATOM   1797  C CD2 . PHE B 1 10  ? 28.172  -23.025 -47.547  1.00 18.68 ? 10  PHE B CD2 1 
ATOM   1798  C CE1 . PHE B 1 10  ? 26.837  -22.575 -49.907  1.00 19.61 ? 10  PHE B CE1 1 
ATOM   1799  C CE2 . PHE B 1 10  ? 27.627  -24.090 -48.222  1.00 18.84 ? 10  PHE B CE2 1 
ATOM   1800  C CZ  . PHE B 1 10  ? 26.955  -23.868 -49.407  1.00 19.26 ? 10  PHE B CZ  1 
ATOM   1801  N N   . GLY B 1 11  ? 25.473  -19.897 -45.841  1.00 20.08 ? 11  GLY B N   1 
ATOM   1802  C CA  . GLY B 1 11  ? 24.576  -20.310 -44.768  1.00 21.52 ? 11  GLY B CA  1 
ATOM   1803  C C   . GLY B 1 11  ? 23.195  -20.741 -45.207  1.00 23.32 ? 11  GLY B C   1 
ATOM   1804  O O   . GLY B 1 11  ? 22.974  -21.076 -46.368  1.00 24.06 ? 11  GLY B O   1 
ATOM   1805  N N   . ASP B 1 12  ? 22.265  -20.721 -44.256  1.00 24.95 ? 12  ASP B N   1 
ATOM   1806  C CA  . ASP B 1 12  ? 20.909  -21.197 -44.465  1.00 25.92 ? 12  ASP B CA  1 
ATOM   1807  C C   . ASP B 1 12  ? 19.963  -19.989 -44.386  1.00 27.74 ? 12  ASP B C   1 
ATOM   1808  O O   . ASP B 1 12  ? 20.355  -18.884 -44.738  1.00 27.19 ? 12  ASP B O   1 
ATOM   1809  C CB  . ASP B 1 12  ? 20.574  -22.321 -43.466  1.00 26.10 ? 12  ASP B CB  1 
ATOM   1810  C CG  . ASP B 1 12  ? 20.976  -21.995 -42.024  1.00 28.00 ? 12  ASP B CG  1 
ATOM   1811  O OD1 . ASP B 1 12  ? 21.052  -20.790 -41.687  1.00 27.91 ? 12  ASP B OD1 1 
ATOM   1812  O OD2 . ASP B 1 12  ? 21.253  -22.958 -41.241  1.00 30.98 ? 12  ASP B OD2 1 
HETATM 1813  N N   . SEP B 1 13  ? 18.730  -20.188 -43.935  1.00 30.46 ? 13  SEP B N   1 
HETATM 1814  C CA  . SEP B 1 13  ? 17.718  -19.128 -43.914  1.00 33.08 ? 13  SEP B CA  1 
HETATM 1815  C CB  . SEP B 1 13  ? 16.365  -19.717 -43.508  1.00 39.59 ? 13  SEP B CB  1 
HETATM 1816  O OG  . SEP B 1 13  ? 16.556  -20.575 -42.356  1.00 50.54 ? 13  SEP B OG  1 
HETATM 1817  C C   . SEP B 1 13  ? 18.098  -18.045 -42.945  1.00 30.93 ? 13  SEP B C   1 
HETATM 1818  O O   . SEP B 1 13  ? 17.706  -16.904 -43.121  1.00 32.18 ? 13  SEP B O   1 
HETATM 1819  P P   . SEP B 1 13  ? 16.379  -22.198 -42.137  1.00 57.25 ? 13  SEP B P   1 
HETATM 1820  O O1P . SEP B 1 13  ? 17.113  -22.870 -43.289  1.00 57.13 ? 13  SEP B O1P 1 
HETATM 1821  O O2P . SEP B 1 13  ? 17.143  -22.351 -40.841  1.00 54.15 ? 13  SEP B O2P 1 
HETATM 1822  O O3P . SEP B 1 13  ? 14.896  -22.558 -42.136  1.00 55.45 ? 13  SEP B O3P 1 
ATOM   1823  N N   . LEU B 1 14  ? 18.869  -18.389 -41.911  1.00 28.36 ? 14  LEU B N   1 
ATOM   1824  C CA  . LEU B 1 14  ? 19.392  -17.399 -40.970  1.00 26.79 ? 14  LEU B CA  1 
ATOM   1825  C C   . LEU B 1 14  ? 20.231  -16.347 -41.671  1.00 25.60 ? 14  LEU B C   1 
ATOM   1826  O O   . LEU B 1 14  ? 20.246  -15.197 -41.254  1.00 25.57 ? 14  LEU B O   1 
ATOM   1827  C CB  . LEU B 1 14  ? 20.253  -18.071 -39.885  1.00 25.81 ? 14  LEU B CB  1 
ATOM   1828  C CG  . LEU B 1 14  ? 19.595  -19.071 -38.928  1.00 24.60 ? 14  LEU B CG  1 
ATOM   1829  C CD1 . LEU B 1 14  ? 20.608  -19.712 -38.005  1.00 24.58 ? 14  LEU B CD1 1 
ATOM   1830  C CD2 . LEU B 1 14  ? 18.535  -18.371 -38.101  1.00 24.64 ? 14  LEU B CD2 1 
ATOM   1831  N N   . THR B 1 15  ? 20.927  -16.765 -42.727  1.00 24.51 ? 15  THR B N   1 
ATOM   1832  C CA  . THR B 1 15  ? 21.811  -15.916 -43.518  1.00 23.34 ? 15  THR B CA  1 
ATOM   1833  C C   . THR B 1 15  ? 21.092  -15.272 -44.713  1.00 22.82 ? 15  THR B C   1 
ATOM   1834  O O   . THR B 1 15  ? 21.454  -14.178 -45.146  1.00 22.96 ? 15  THR B O   1 
ATOM   1835  C CB  . THR B 1 15  ? 23.021  -16.750 -43.972  1.00 22.97 ? 15  THR B CB  1 
ATOM   1836  O OG1 . THR B 1 15  ? 23.664  -17.334 -42.818  1.00 22.27 ? 15  THR B OG1 1 
ATOM   1837  C CG2 . THR B 1 15  ? 24.007  -15.923 -44.766  1.00 23.07 ? 15  THR B CG2 1 
ATOM   1838  N N   . TRP B 1 16  ? 20.073  -15.949 -45.244  1.00 22.24 ? 16  TRP B N   1 
ATOM   1839  C CA  . TRP B 1 16  ? 19.177  -15.356 -46.238  1.00 22.21 ? 16  TRP B CA  1 
ATOM   1840  C C   . TRP B 1 16  ? 18.455  -14.147 -45.642  1.00 22.52 ? 16  TRP B C   1 
ATOM   1841  O O   . TRP B 1 16  ? 18.345  -13.088 -46.274  1.00 23.95 ? 16  TRP B O   1 
ATOM   1842  C CB  . TRP B 1 16  ? 18.145  -16.384 -46.690  1.00 21.98 ? 16  TRP B CB  1 
ATOM   1843  C CG  . TRP B 1 16  ? 17.133  -15.884 -47.708  1.00 22.29 ? 16  TRP B CG  1 
ATOM   1844  C CD1 . TRP B 1 16  ? 17.370  -15.588 -49.019  1.00 22.85 ? 16  TRP B CD1 1 
ATOM   1845  C CD2 . TRP B 1 16  ? 15.734  -15.687 -47.500  1.00 22.77 ? 16  TRP B CD2 1 
ATOM   1846  N NE1 . TRP B 1 16  ? 16.210  -15.189 -49.637  1.00 23.46 ? 16  TRP B NE1 1 
ATOM   1847  C CE2 . TRP B 1 16  ? 15.186  -15.253 -48.727  1.00 23.74 ? 16  TRP B CE2 1 
ATOM   1848  C CE3 . TRP B 1 16  ? 14.888  -15.824 -46.399  1.00 22.94 ? 16  TRP B CE3 1 
ATOM   1849  C CZ2 . TRP B 1 16  ? 13.828  -14.955 -48.874  1.00 23.76 ? 16  TRP B CZ2 1 
ATOM   1850  C CZ3 . TRP B 1 16  ? 13.537  -15.510 -46.548  1.00 22.88 ? 16  TRP B CZ3 1 
ATOM   1851  C CH2 . TRP B 1 16  ? 13.027  -15.085 -47.768  1.00 23.27 ? 16  TRP B CH2 1 
ATOM   1852  N N   . GLY B 1 17  ? 17.950  -14.326 -44.429  1.00 22.52 ? 17  GLY B N   1 
ATOM   1853  C CA  . GLY B 1 17  ? 17.216  -13.288 -43.717  1.00 22.37 ? 17  GLY B CA  1 
ATOM   1854  C C   . GLY B 1 17  ? 15.749  -13.647 -43.486  1.00 22.37 ? 17  GLY B C   1 
ATOM   1855  O O   . GLY B 1 17  ? 14.856  -12.860 -43.802  1.00 23.13 ? 17  GLY B O   1 
ATOM   1856  N N   . TRP B 1 18  ? 15.502  -14.826 -42.926  1.00 21.58 ? 18  TRP B N   1 
ATOM   1857  C CA  . TRP B 1 18  ? 14.154  -15.258 -42.602  1.00 22.50 ? 18  TRP B CA  1 
ATOM   1858  C C   . TRP B 1 18  ? 13.589  -14.384 -41.486  1.00 22.22 ? 18  TRP B C   1 
ATOM   1859  O O   . TRP B 1 18  ? 14.160  -14.318 -40.396  1.00 21.40 ? 18  TRP B O   1 
ATOM   1860  C CB  . TRP B 1 18  ? 14.169  -16.723 -42.133  1.00 23.33 ? 18  TRP B CB  1 
ATOM   1861  C CG  . TRP B 1 18  ? 12.810  -17.342 -41.873  1.00 23.57 ? 18  TRP B CG  1 
ATOM   1862  C CD1 . TRP B 1 18  ? 11.881  -16.945 -40.958  1.00 23.86 ? 18  TRP B CD1 1 
ATOM   1863  C CD2 . TRP B 1 18  ? 12.263  -18.498 -42.520  1.00 23.48 ? 18  TRP B CD2 1 
ATOM   1864  N NE1 . TRP B 1 18  ? 10.782  -17.767 -41.016  1.00 24.01 ? 18  TRP B NE1 1 
ATOM   1865  C CE2 . TRP B 1 18  ? 11.001  -18.729 -41.970  1.00 23.36 ? 18  TRP B CE2 1 
ATOM   1866  C CE3 . TRP B 1 18  ? 12.722  -19.359 -43.527  1.00 24.03 ? 18  TRP B CE3 1 
ATOM   1867  C CZ2 . TRP B 1 18  ? 10.190  -19.788 -42.392  1.00 23.58 ? 18  TRP B CZ2 1 
ATOM   1868  C CZ3 . TRP B 1 18  ? 11.903  -20.401 -43.951  1.00 23.05 ? 18  TRP B CZ3 1 
ATOM   1869  C CH2 . TRP B 1 18  ? 10.665  -20.605 -43.386  1.00 22.70 ? 18  TRP B CH2 1 
ATOM   1870  N N   . THR B 1 19  ? 12.459  -13.740 -41.771  1.00 22.28 ? 19  THR B N   1 
ATOM   1871  C CA  . THR B 1 19  ? 11.739  -12.955 -40.778  1.00 23.04 ? 19  THR B CA  1 
ATOM   1872  C C   . THR B 1 19  ? 10.836  -13.893 -39.974  1.00 22.27 ? 19  THR B C   1 
ATOM   1873  O O   . THR B 1 19  ? 9.938   -14.494 -40.553  1.00 22.38 ? 19  THR B O   1 
ATOM   1874  C CB  . THR B 1 19  ? 10.874  -11.848 -41.432  1.00 23.44 ? 19  THR B CB  1 
ATOM   1875  O OG1 . THR B 1 19  ? 11.695  -10.967 -42.200  1.00 23.54 ? 19  THR B OG1 1 
ATOM   1876  C CG2 . THR B 1 19  ? 10.160  -11.034 -40.374  1.00 23.17 ? 19  THR B CG2 1 
ATOM   1877  N N   . PRO B 1 20  ? 11.084  -14.035 -38.649  1.00 21.88 ? 20  PRO B N   1 
ATOM   1878  C CA  . PRO B 1 20  ? 10.236  -14.924 -37.842  1.00 22.08 ? 20  PRO B CA  1 
ATOM   1879  C C   . PRO B 1 20  ? 8.822   -14.384 -37.707  1.00 21.87 ? 20  PRO B C   1 
ATOM   1880  O O   . PRO B 1 20  ? 8.649   -13.187 -37.443  1.00 21.18 ? 20  PRO B O   1 
ATOM   1881  C CB  . PRO B 1 20  ? 10.934  -14.981 -36.471  1.00 22.31 ? 20  PRO B CB  1 
ATOM   1882  C CG  . PRO B 1 20  ? 11.877  -13.851 -36.456  1.00 22.52 ? 20  PRO B CG  1 
ATOM   1883  C CD  . PRO B 1 20  ? 12.208  -13.489 -37.871  1.00 21.97 ? 20  PRO B CD  1 
ATOM   1884  N N   . VAL B 1 21  ? 7.832   -15.261 -37.911  1.00 21.69 ? 21  VAL B N   1 
ATOM   1885  C CA  . VAL B 1 21  ? 6.428   -14.856 -37.950  1.00 20.47 ? 21  VAL B CA  1 
ATOM   1886  C C   . VAL B 1 21  ? 5.505   -15.973 -37.480  1.00 19.75 ? 21  VAL B C   1 
ATOM   1887  O O   . VAL B 1 21  ? 5.920   -17.106 -37.282  1.00 20.30 ? 21  VAL B O   1 
ATOM   1888  C CB  . VAL B 1 21  ? 6.007   -14.433 -39.376  1.00 20.37 ? 21  VAL B CB  1 
ATOM   1889  C CG1 . VAL B 1 21  ? 6.595   -13.075 -39.729  1.00 19.65 ? 21  VAL B CG1 1 
ATOM   1890  C CG2 . VAL B 1 21  ? 6.413   -15.500 -40.403  1.00 20.87 ? 21  VAL B CG2 1 
ATOM   1891  N N   . ALA B 1 22  ? 4.239   -15.621 -37.292  1.00 19.07 ? 22  ALA B N   1 
ATOM   1892  C CA  . ALA B 1 22  ? 3.208   -16.564 -36.916  1.00 18.82 ? 22  ALA B CA  1 
ATOM   1893  C C   . ALA B 1 22  ? 2.017   -16.380 -37.861  1.00 19.57 ? 22  ALA B C   1 
ATOM   1894  O O   . ALA B 1 22  ? 1.524   -15.259 -38.004  1.00 19.64 ? 22  ALA B O   1 
ATOM   1895  C CB  . ALA B 1 22  ? 2.801   -16.344 -35.476  1.00 18.63 ? 22  ALA B CB  1 
ATOM   1896  N N   . PRO B 1 23  ? 1.578   -17.445 -38.546  1.00 20.32 ? 23  PRO B N   1 
ATOM   1897  C CA  . PRO B 1 23  ? 2.222   -18.758 -38.504  1.00 20.18 ? 23  PRO B CA  1 
ATOM   1898  C C   . PRO B 1 23  ? 3.616   -18.751 -39.154  1.00 20.11 ? 23  PRO B C   1 
ATOM   1899  O O   . PRO B 1 23  ? 3.946   -17.820 -39.918  1.00 20.49 ? 23  PRO B O   1 
ATOM   1900  C CB  . PRO B 1 23  ? 1.234   -19.644 -39.271  1.00 20.05 ? 23  PRO B CB  1 
ATOM   1901  C CG  . PRO B 1 23  ? 0.459   -18.701 -40.169  1.00 20.11 ? 23  PRO B CG  1 
ATOM   1902  C CD  . PRO B 1 23  ? 0.790   -17.284 -39.782  1.00 20.20 ? 23  PRO B CD  1 
ATOM   1903  N N   . ILE B 1 24  ? 4.411   -19.779 -38.840  1.00 19.87 ? 24  ILE B N   1 
ATOM   1904  C CA  . ILE B 1 24  ? 5.844   -19.859 -39.228  1.00 19.46 ? 24  ILE B CA  1 
ATOM   1905  C C   . ILE B 1 24  ? 6.111   -19.554 -40.698  1.00 19.07 ? 24  ILE B C   1 
ATOM   1906  O O   . ILE B 1 24  ? 7.110   -18.911 -41.009  1.00 19.56 ? 24  ILE B O   1 
ATOM   1907  C CB  . ILE B 1 24  ? 6.476   -21.219 -38.847  1.00 19.86 ? 24  ILE B CB  1 
ATOM   1908  C CG1 . ILE B 1 24  ? 7.974   -21.247 -39.184  1.00 19.75 ? 24  ILE B CG1 1 
ATOM   1909  C CG2 . ILE B 1 24  ? 5.753   -22.394 -39.526  1.00 20.31 ? 24  ILE B CG2 1 
ATOM   1910  C CD1 . ILE B 1 24  ? 8.695   -22.455 -38.601  1.00 19.30 ? 24  ILE B CD1 1 
ATOM   1911  N N   . VAL B 1 25  ? 5.205   -20.006 -41.572  1.00 18.54 ? 25  VAL B N   1 
ATOM   1912  C CA  . VAL B 1 25  ? 5.245   -19.761 -43.016  1.00 18.18 ? 25  VAL B CA  1 
ATOM   1913  C C   . VAL B 1 25  ? 3.887   -19.227 -43.496  1.00 18.61 ? 25  VAL B C   1 
ATOM   1914  O O   . VAL B 1 25  ? 2.861   -19.531 -42.898  1.00 19.49 ? 25  VAL B O   1 
ATOM   1915  C CB  . VAL B 1 25  ? 5.569   -21.052 -43.809  1.00 17.68 ? 25  VAL B CB  1 
ATOM   1916  C CG1 . VAL B 1 25  ? 6.945   -21.576 -43.427  1.00 17.15 ? 25  VAL B CG1 1 
ATOM   1917  C CG2 . VAL B 1 25  ? 4.489   -22.135 -43.616  1.00 17.09 ? 25  VAL B CG2 1 
ATOM   1918  N N   . PRO B 1 26  ? 3.854   -18.427 -44.567  1.00 18.39 ? 26  PRO B N   1 
ATOM   1919  C CA  . PRO B 1 26  ? 5.025   -17.953 -45.287  1.00 18.58 ? 26  PRO B CA  1 
ATOM   1920  C C   . PRO B 1 26  ? 5.717   -16.777 -44.589  1.00 19.49 ? 26  PRO B C   1 
ATOM   1921  O O   . PRO B 1 26  ? 5.090   -16.056 -43.796  1.00 21.53 ? 26  PRO B O   1 
ATOM   1922  C CB  . PRO B 1 26  ? 4.431   -17.472 -46.608  1.00 18.15 ? 26  PRO B CB  1 
ATOM   1923  C CG  . PRO B 1 26  ? 3.038   -17.064 -46.283  1.00 17.63 ? 26  PRO B CG  1 
ATOM   1924  C CD  . PRO B 1 26  ? 2.608   -17.822 -45.075  1.00 17.88 ? 26  PRO B CD  1 
ATOM   1925  N N   . THR B 1 27  ? 6.996   -16.596 -44.899  1.00 19.14 ? 27  THR B N   1 
ATOM   1926  C CA  . THR B 1 27  ? 7.783   -15.478 -44.398  1.00 18.62 ? 27  THR B CA  1 
ATOM   1927  C C   . THR B 1 27  ? 8.121   -14.526 -45.545  1.00 18.23 ? 27  THR B C   1 
ATOM   1928  O O   . THR B 1 27  ? 7.822   -14.785 -46.717  1.00 17.71 ? 27  THR B O   1 
ATOM   1929  C CB  . THR B 1 27  ? 9.087   -15.952 -43.710  1.00 18.98 ? 27  THR B CB  1 
ATOM   1930  O OG1 . THR B 1 27  ? 9.828   -14.827 -43.210  1.00 19.22 ? 27  THR B OG1 1 
ATOM   1931  C CG2 . THR B 1 27  ? 9.973   -16.740 -44.670  1.00 18.74 ? 27  THR B CG2 1 
ATOM   1932  N N   . THR B 1 28  ? 8.708   -13.398 -45.175  1.00 18.37 ? 28  THR B N   1 
ATOM   1933  C CA  . THR B 1 28  ? 9.273   -12.477 -46.139  1.00 19.04 ? 28  THR B CA  1 
ATOM   1934  C C   . THR B 1 28  ? 10.696  -12.179 -45.677  1.00 20.02 ? 28  THR B C   1 
ATOM   1935  O O   . THR B 1 28  ? 11.021  -12.351 -44.485  1.00 20.03 ? 28  THR B O   1 
ATOM   1936  C CB  . THR B 1 28  ? 8.461   -11.168 -46.273  1.00 18.07 ? 28  THR B CB  1 
ATOM   1937  O OG1 . THR B 1 28  ? 8.684   -10.352 -45.140  1.00 16.74 ? 28  THR B OG1 1 
ATOM   1938  C CG2 . THR B 1 28  ? 6.963   -11.441 -46.416  1.00 18.17 ? 28  THR B CG2 1 
ATOM   1939  N N   . ARG B 1 29  ? 11.527  -11.725 -46.618  1.00 20.12 ? 29  ARG B N   1 
ATOM   1940  C CA  . ARG B 1 29  ? 12.940  -11.530 -46.340  1.00 20.67 ? 29  ARG B CA  1 
ATOM   1941  C C   . ARG B 1 29  ? 13.161  -10.295 -45.486  1.00 20.66 ? 29  ARG B C   1 
ATOM   1942  O O   . ARG B 1 29  ? 12.612  -9.240  -45.785  1.00 21.59 ? 29  ARG B O   1 
ATOM   1943  C CB  . ARG B 1 29  ? 13.730  -11.400 -47.649  1.00 20.30 ? 29  ARG B CB  1 
ATOM   1944  C CG  . ARG B 1 29  ? 15.068  -12.140 -47.595  1.00 20.79 ? 29  ARG B CG  1 
ATOM   1945  C CD  . ARG B 1 29  ? 16.217  -11.320 -48.123  1.00 21.11 ? 29  ARG B CD  1 
ATOM   1946  N NE  . ARG B 1 29  ? 16.647  -11.664 -49.486  1.00 20.99 ? 29  ARG B NE  1 
ATOM   1947  C CZ  . ARG B 1 29  ? 17.860  -12.129 -49.810  1.00 19.99 ? 29  ARG B CZ  1 
ATOM   1948  N NH1 . ARG B 1 29  ? 18.793  -12.374 -48.888  1.00 19.44 ? 29  ARG B NH1 1 
ATOM   1949  N NH2 . ARG B 1 29  ? 18.151  -12.354 -51.077  1.00 19.96 ? 29  ARG B NH2 1 
ATOM   1950  N N   . HIS B 1 30  ? 13.956  -10.412 -44.428  1.00 21.06 ? 30  HIS B N   1 
ATOM   1951  C CA  . HIS B 1 30  ? 14.355  -9.227  -43.671  1.00 21.68 ? 30  HIS B CA  1 
ATOM   1952  C C   . HIS B 1 30  ? 14.791  -8.142  -44.653  1.00 21.70 ? 30  HIS B C   1 
ATOM   1953  O O   . HIS B 1 30  ? 15.504  -8.433  -45.622  1.00 22.40 ? 30  HIS B O   1 
ATOM   1954  C CB  . HIS B 1 30  ? 15.525  -9.520  -42.722  1.00 21.31 ? 30  HIS B CB  1 
ATOM   1955  C CG  . HIS B 1 30  ? 15.122  -10.085 -41.395  1.00 21.73 ? 30  HIS B CG  1 
ATOM   1956  N ND1 . HIS B 1 30  ? 14.440  -9.349  -40.450  1.00 21.74 ? 30  HIS B ND1 1 
ATOM   1957  C CD2 . HIS B 1 30  ? 15.350  -11.300 -40.836  1.00 21.98 ? 30  HIS B CD2 1 
ATOM   1958  C CE1 . HIS B 1 30  ? 14.255  -10.092 -39.371  1.00 22.49 ? 30  HIS B CE1 1 
ATOM   1959  N NE2 . HIS B 1 30  ? 14.796  -11.281 -39.578  1.00 22.33 ? 30  HIS B NE2 1 
ATOM   1960  N N   . PRO B 1 31  ? 14.371  -6.890  -44.418  1.00 21.95 ? 31  PRO B N   1 
ATOM   1961  C CA  . PRO B 1 31  ? 14.952  -5.800  -45.204  1.00 22.95 ? 31  PRO B CA  1 
ATOM   1962  C C   . PRO B 1 31  ? 16.474  -5.839  -45.127  1.00 24.15 ? 31  PRO B C   1 
ATOM   1963  O O   . PRO B 1 31  ? 17.023  -6.213  -44.087  1.00 24.40 ? 31  PRO B O   1 
ATOM   1964  C CB  . PRO B 1 31  ? 14.424  -4.543  -44.527  1.00 22.55 ? 31  PRO B CB  1 
ATOM   1965  C CG  . PRO B 1 31  ? 13.199  -4.976  -43.789  1.00 22.44 ? 31  PRO B CG  1 
ATOM   1966  C CD  . PRO B 1 31  ? 13.368  -6.424  -43.450  1.00 22.35 ? 31  PRO B CD  1 
ATOM   1967  N N   . HIS B 1 32  ? 17.141  -5.474  -46.220  1.00 25.52 ? 32  HIS B N   1 
ATOM   1968  C CA  . HIS B 1 32  ? 18.608  -5.526  -46.288  1.00 26.06 ? 32  HIS B CA  1 
ATOM   1969  C C   . HIS B 1 32  ? 19.280  -4.911  -45.048  1.00 27.20 ? 32  HIS B C   1 
ATOM   1970  O O   . HIS B 1 32  ? 20.220  -5.490  -44.490  1.00 27.61 ? 32  HIS B O   1 
ATOM   1971  C CB  . HIS B 1 32  ? 19.094  -4.842  -47.570  1.00 24.38 ? 32  HIS B CB  1 
ATOM   1972  C CG  . HIS B 1 32  ? 20.568  -4.942  -47.795  1.00 23.38 ? 32  HIS B CG  1 
ATOM   1973  N ND1 . HIS B 1 32  ? 21.459  -4.010  -47.315  1.00 23.54 ? 32  HIS B ND1 1 
ATOM   1974  C CD2 . HIS B 1 32  ? 21.305  -5.847  -48.471  1.00 23.71 ? 32  HIS B CD2 1 
ATOM   1975  C CE1 . HIS B 1 32  ? 22.685  -4.345  -47.666  1.00 23.71 ? 32  HIS B CE1 1 
ATOM   1976  N NE2 . HIS B 1 32  ? 22.619  -5.462  -48.364  1.00 24.88 ? 32  HIS B NE2 1 
ATOM   1977  N N   . ALA B 1 33  ? 18.773  -3.759  -44.615  1.00 28.02 ? 33  ALA B N   1 
ATOM   1978  C CA  . ALA B 1 33  ? 19.347  -3.055  -43.462  1.00 28.15 ? 33  ALA B CA  1 
ATOM   1979  C C   . ALA B 1 33  ? 19.372  -3.906  -42.172  1.00 27.98 ? 33  ALA B C   1 
ATOM   1980  O O   . ALA B 1 33  ? 20.207  -3.684  -41.314  1.00 28.38 ? 33  ALA B O   1 
ATOM   1981  C CB  . ALA B 1 33  ? 18.577  -1.754  -43.226  1.00 28.24 ? 33  ALA B CB  1 
ATOM   1982  N N   . ASP B 1 34  ? 18.455  -4.869  -42.057  1.00 27.47 ? 34  ASP B N   1 
ATOM   1983  C CA  . ASP B 1 34  ? 18.304  -5.696  -40.862  1.00 27.43 ? 34  ASP B CA  1 
ATOM   1984  C C   . ASP B 1 34  ? 18.951  -7.087  -40.935  1.00 26.74 ? 34  ASP B C   1 
ATOM   1985  O O   . ASP B 1 34  ? 18.808  -7.876  -39.993  1.00 25.78 ? 34  ASP B O   1 
ATOM   1986  C CB  . ASP B 1 34  ? 16.811  -5.915  -40.582  1.00 29.38 ? 34  ASP B CB  1 
ATOM   1987  C CG  . ASP B 1 34  ? 16.064  -4.642  -40.303  1.00 29.71 ? 34  ASP B CG  1 
ATOM   1988  O OD1 . ASP B 1 34  ? 16.685  -3.678  -39.811  1.00 29.83 ? 34  ASP B OD1 1 
ATOM   1989  O OD2 . ASP B 1 34  ? 14.843  -4.639  -40.572  1.00 30.72 ? 34  ASP B OD2 1 
ATOM   1990  N N   . ARG B 1 35  ? 19.645  -7.406  -42.030  1.00 27.15 ? 35  ARG B N   1 
ATOM   1991  C CA  . ARG B 1 35  ? 20.269  -8.739  -42.164  1.00 27.44 ? 35  ARG B CA  1 
ATOM   1992  C C   . ARG B 1 35  ? 21.624  -8.796  -41.458  1.00 27.29 ? 35  ARG B C   1 
ATOM   1993  O O   . ARG B 1 35  ? 22.411  -7.833  -41.537  1.00 26.13 ? 35  ARG B O   1 
ATOM   1994  C CB  . ARG B 1 35  ? 20.451  -9.111  -43.636  1.00 28.36 ? 35  ARG B CB  1 
ATOM   1995  C CG  . ARG B 1 35  ? 19.147  -9.252  -44.390  1.00 28.74 ? 35  ARG B CG  1 
ATOM   1996  C CD  . ARG B 1 35  ? 19.386  -9.556  -45.851  1.00 29.02 ? 35  ARG B CD  1 
ATOM   1997  N NE  . ARG B 1 35  ? 18.262  -9.079  -46.642  1.00 29.47 ? 35  ARG B NE  1 
ATOM   1998  C CZ  . ARG B 1 35  ? 18.312  -8.822  -47.953  1.00 30.51 ? 35  ARG B CZ  1 
ATOM   1999  N NH1 . ARG B 1 35  ? 19.441  -8.990  -48.645  1.00 31.29 ? 35  ARG B NH1 1 
ATOM   2000  N NH2 . ARG B 1 35  ? 17.219  -8.394  -48.580  1.00 30.09 ? 35  ARG B NH2 1 
ATOM   2001  N N   . TRP B 1 36  ? 21.914  -9.926  -40.799  1.00 25.66 ? 36  TRP B N   1 
ATOM   2002  C CA  . TRP B 1 36  ? 23.148  -10.030 -40.005  1.00 24.29 ? 36  TRP B CA  1 
ATOM   2003  C C   . TRP B 1 36  ? 24.390  -9.797  -40.878  1.00 22.93 ? 36  TRP B C   1 
ATOM   2004  O O   . TRP B 1 36  ? 25.319  -9.108  -40.464  1.00 22.26 ? 36  TRP B O   1 
ATOM   2005  C CB  . TRP B 1 36  ? 23.220  -11.360 -39.217  1.00 24.39 ? 36  TRP B CB  1 
ATOM   2006  C CG  . TRP B 1 36  ? 23.830  -12.542 -39.912  1.00 24.82 ? 36  TRP B CG  1 
ATOM   2007  C CD1 . TRP B 1 36  ? 23.175  -13.516 -40.604  1.00 25.14 ? 36  TRP B CD1 1 
ATOM   2008  C CD2 . TRP B 1 36  ? 25.215  -12.901 -39.940  1.00 24.86 ? 36  TRP B CD2 1 
ATOM   2009  N NE1 . TRP B 1 36  ? 24.070  -14.456 -41.080  1.00 24.51 ? 36  TRP B NE1 1 
ATOM   2010  C CE2 . TRP B 1 36  ? 25.327  -14.098 -40.685  1.00 25.05 ? 36  TRP B CE2 1 
ATOM   2011  C CE3 . TRP B 1 36  ? 26.370  -12.327 -39.421  1.00 24.42 ? 36  TRP B CE3 1 
ATOM   2012  C CZ2 . TRP B 1 36  ? 26.551  -14.722 -40.920  1.00 24.65 ? 36  TRP B CZ2 1 
ATOM   2013  C CZ3 . TRP B 1 36  ? 27.584  -12.928 -39.678  1.00 25.08 ? 36  TRP B CZ3 1 
ATOM   2014  C CH2 . TRP B 1 36  ? 27.668  -14.120 -40.416  1.00 24.77 ? 36  TRP B CH2 1 
ATOM   2015  N N   . THR B 1 37  ? 24.374  -10.353 -42.086  1.00 22.31 ? 37  THR B N   1 
ATOM   2016  C CA  . THR B 1 37  ? 25.448  -10.156 -43.053  1.00 22.42 ? 37  THR B CA  1 
ATOM   2017  C C   . THR B 1 37  ? 25.647  -8.694  -43.431  1.00 21.76 ? 37  THR B C   1 
ATOM   2018  O O   . THR B 1 37  ? 26.781  -8.262  -43.645  1.00 21.86 ? 37  THR B O   1 
ATOM   2019  C CB  . THR B 1 37  ? 25.213  -10.963 -44.347  1.00 22.58 ? 37  THR B CB  1 
ATOM   2020  O OG1 . THR B 1 37  ? 23.867  -10.783 -44.776  1.00 22.32 ? 37  THR B OG1 1 
ATOM   2021  C CG2 . THR B 1 37  ? 25.472  -12.425 -44.097  1.00 22.85 ? 37  THR B CG2 1 
ATOM   2022  N N   . THR B 1 38  ? 24.553  -7.941  -43.518  1.00 21.07 ? 38  THR B N   1 
ATOM   2023  C CA  . THR B 1 38  ? 24.663  -6.514  -43.825  1.00 21.05 ? 38  THR B CA  1 
ATOM   2024  C C   . THR B 1 38  ? 25.366  -5.749  -42.709  1.00 21.31 ? 38  THR B C   1 
ATOM   2025  O O   . THR B 1 38  ? 26.256  -4.932  -42.964  1.00 20.86 ? 38  THR B O   1 
ATOM   2026  C CB  . THR B 1 38  ? 23.295  -5.896  -44.113  1.00 20.57 ? 38  THR B CB  1 
ATOM   2027  O OG1 . THR B 1 38  ? 22.768  -6.475  -45.306  1.00 20.50 ? 38  THR B OG1 1 
ATOM   2028  C CG2 . THR B 1 38  ? 23.398  -4.392  -44.302  1.00 20.69 ? 38  THR B CG2 1 
ATOM   2029  N N   . VAL B 1 39  ? 24.974  -6.033  -41.473  1.00 22.16 ? 39  VAL B N   1 
ATOM   2030  C CA  . VAL B 1 39  ? 25.592  -5.381  -40.332  1.00 22.35 ? 39  VAL B CA  1 
ATOM   2031  C C   . VAL B 1 39  ? 27.040  -5.823  -40.234  1.00 22.37 ? 39  VAL B C   1 
ATOM   2032  O O   . VAL B 1 39  ? 27.901  -5.002  -39.971  1.00 23.49 ? 39  VAL B O   1 
ATOM   2033  C CB  . VAL B 1 39  ? 24.831  -5.667  -39.024  1.00 22.62 ? 39  VAL B CB  1 
ATOM   2034  C CG1 . VAL B 1 39  ? 25.583  -5.119  -37.822  1.00 22.46 ? 39  VAL B CG1 1 
ATOM   2035  C CG2 . VAL B 1 39  ? 23.430  -5.075  -39.096  1.00 22.17 ? 39  VAL B CG2 1 
ATOM   2036  N N   . LEU B 1 40  ? 27.313  -7.104  -40.461  1.00 22.56 ? 40  LEU B N   1 
ATOM   2037  C CA  . LEU B 1 40  ? 28.697  -7.578  -40.596  1.00 23.26 ? 40  LEU B CA  1 
ATOM   2038  C C   . LEU B 1 40  ? 29.502  -6.711  -41.579  1.00 24.67 ? 40  LEU B C   1 
ATOM   2039  O O   . LEU B 1 40  ? 30.640  -6.334  -41.302  1.00 24.57 ? 40  LEU B O   1 
ATOM   2040  C CB  . LEU B 1 40  ? 28.728  -9.042  -41.055  1.00 22.06 ? 40  LEU B CB  1 
ATOM   2041  C CG  . LEU B 1 40  ? 30.080  -9.585  -41.529  1.00 21.87 ? 40  LEU B CG  1 
ATOM   2042  C CD1 . LEU B 1 40  ? 31.063  -9.684  -40.364  1.00 22.49 ? 40  LEU B CD1 1 
ATOM   2043  C CD2 . LEU B 1 40  ? 29.918  -10.914 -42.226  1.00 22.02 ? 40  LEU B CD2 1 
ATOM   2044  N N   . GLY B 1 41  ? 28.900  -6.413  -42.729  1.00 26.24 ? 41  GLY B N   1 
ATOM   2045  C CA  . GLY B 1 41  ? 29.543  -5.607  -43.763  1.00 27.46 ? 41  GLY B CA  1 
ATOM   2046  C C   . GLY B 1 41  ? 29.831  -4.189  -43.325  1.00 28.23 ? 41  GLY B C   1 
ATOM   2047  O O   . GLY B 1 41  ? 30.915  -3.663  -43.580  1.00 27.44 ? 41  GLY B O   1 
ATOM   2048  N N   . GLU B 1 42  ? 28.852  -3.585  -42.661  1.00 30.61 ? 42  GLU B N   1 
ATOM   2049  C CA  . GLU B 1 42  ? 28.966  -2.210  -42.166  1.00 31.62 ? 42  GLU B CA  1 
ATOM   2050  C C   . GLU B 1 42  ? 30.017  -2.058  -41.101  1.00 30.60 ? 42  GLU B C   1 
ATOM   2051  O O   . GLU B 1 42  ? 30.784  -1.105  -41.138  1.00 34.39 ? 42  GLU B O   1 
ATOM   2052  C CB  . GLU B 1 42  ? 27.629  -1.704  -41.647  1.00 34.74 ? 42  GLU B CB  1 
ATOM   2053  C CG  . GLU B 1 42  ? 26.796  -1.051  -42.751  1.00 39.95 ? 42  GLU B CG  1 
ATOM   2054  C CD  . GLU B 1 42  ? 25.291  -1.131  -42.529  1.00 45.48 ? 42  GLU B CD  1 
ATOM   2055  O OE1 . GLU B 1 42  ? 24.575  -0.936  -43.540  1.00 48.46 ? 42  GLU B OE1 1 
ATOM   2056  O OE2 . GLU B 1 42  ? 24.849  -1.407  -41.376  1.00 51.37 ? 42  GLU B OE2 1 
ATOM   2057  N N   . ASN B 1 43  ? 30.064  -3.000  -40.167  1.00 28.39 ? 43  ASN B N   1 
ATOM   2058  C CA  . ASN B 1 43  ? 31.070  -2.979  -39.107  1.00 27.04 ? 43  ASN B CA  1 
ATOM   2059  C C   . ASN B 1 43  ? 32.481  -3.293  -39.590  1.00 27.76 ? 43  ASN B C   1 
ATOM   2060  O O   . ASN B 1 43  ? 33.439  -2.999  -38.889  1.00 27.35 ? 43  ASN B O   1 
ATOM   2061  C CB  . ASN B 1 43  ? 30.713  -3.957  -38.002  1.00 25.29 ? 43  ASN B CB  1 
ATOM   2062  C CG  . ASN B 1 43  ? 29.716  -3.399  -37.020  1.00 24.36 ? 43  ASN B CG  1 
ATOM   2063  O OD1 . ASN B 1 43  ? 30.090  -2.939  -35.953  1.00 23.85 ? 43  ASN B OD1 1 
ATOM   2064  N ND2 . ASN B 1 43  ? 28.441  -3.443  -37.368  1.00 23.31 ? 43  ASN B ND2 1 
ATOM   2065  N N   . LEU B 1 44  ? 32.609  -3.911  -40.762  1.00 29.35 ? 44  LEU B N   1 
ATOM   2066  C CA  . LEU B 1 44  ? 33.930  -4.226  -41.333  1.00 29.65 ? 44  LEU B CA  1 
ATOM   2067  C C   . LEU B 1 44  ? 34.540  -3.027  -42.047  1.00 30.25 ? 44  LEU B C   1 
ATOM   2068  O O   . LEU B 1 44  ? 35.752  -2.827  -42.002  1.00 29.87 ? 44  LEU B O   1 
ATOM   2069  C CB  . LEU B 1 44  ? 33.856  -5.431  -42.286  1.00 29.05 ? 44  LEU B CB  1 
ATOM   2070  C CG  . LEU B 1 44  ? 33.859  -6.823  -41.639  1.00 28.84 ? 44  LEU B CG  1 
ATOM   2071  C CD1 . LEU B 1 44  ? 33.575  -7.897  -42.681  1.00 29.14 ? 44  LEU B CD1 1 
ATOM   2072  C CD2 . LEU B 1 44  ? 35.167  -7.108  -40.925  1.00 28.76 ? 44  LEU B CD2 1 
ATOM   2073  N N   . GLY B 1 45  ? 33.693  -2.248  -42.720  1.00 30.94 ? 45  GLY B N   1 
ATOM   2074  C CA  . GLY B 1 45  ? 34.127  -1.050  -43.428  1.00 32.45 ? 45  GLY B CA  1 
ATOM   2075  C C   . GLY B 1 45  ? 34.466  -1.279  -44.889  1.00 33.15 ? 45  GLY B C   1 
ATOM   2076  O O   . GLY B 1 45  ? 34.274  -2.349  -45.426  1.00 34.05 ? 45  GLY B O   1 
ATOM   2077  N N   . ASP B 1 46  ? 34.992  -0.235  -45.520  1.00 35.58 ? 46  ASP B N   1 
ATOM   2078  C CA  . ASP B 1 46  ? 35.388  -0.236  -46.932  1.00 34.64 ? 46  ASP B CA  1 
ATOM   2079  C C   . ASP B 1 46  ? 36.561  -1.176  -47.226  1.00 32.53 ? 46  ASP B C   1 
ATOM   2080  O O   . ASP B 1 46  ? 36.801  -1.514  -48.389  1.00 30.34 ? 46  ASP B O   1 
ATOM   2081  C CB  . ASP B 1 46  ? 35.814  1.174   -47.369  1.00 36.86 ? 46  ASP B CB  1 
ATOM   2082  C CG  . ASP B 1 46  ? 34.677  2.187   -47.319  1.00 38.57 ? 46  ASP B CG  1 
ATOM   2083  O OD1 . ASP B 1 46  ? 33.676  1.989   -46.564  1.00 38.61 ? 46  ASP B OD1 1 
ATOM   2084  O OD2 . ASP B 1 46  ? 34.823  3.204   -48.050  1.00 38.74 ? 46  ASP B OD2 1 
ATOM   2085  N N   . GLY B 1 47  ? 37.299  -1.585  -46.188  1.00 31.02 ? 47  GLY B N   1 
ATOM   2086  C CA  . GLY B 1 47  ? 38.388  -2.544  -46.356  1.00 28.56 ? 47  GLY B CA  1 
ATOM   2087  C C   . GLY B 1 47  ? 37.919  -3.911  -46.832  1.00 27.25 ? 47  GLY B C   1 
ATOM   2088  O O   . GLY B 1 47  ? 38.719  -4.698  -47.348  1.00 24.69 ? 47  GLY B O   1 
ATOM   2089  N N   . TYR B 1 48  ? 36.616  -4.176  -46.660  1.00 27.67 ? 48  TYR B N   1 
ATOM   2090  C CA  . TYR B 1 48  ? 36.013  -5.467  -46.959  1.00 28.28 ? 48  TYR B CA  1 
ATOM   2091  C C   . TYR B 1 48  ? 34.820  -5.375  -47.900  1.00 26.44 ? 48  TYR B C   1 
ATOM   2092  O O   . TYR B 1 48  ? 34.148  -4.361  -47.981  1.00 25.62 ? 48  TYR B O   1 
ATOM   2093  C CB  . TYR B 1 48  ? 35.592  -6.148  -45.656  1.00 30.35 ? 48  TYR B CB  1 
ATOM   2094  C CG  . TYR B 1 48  ? 36.723  -6.355  -44.670  1.00 32.26 ? 48  TYR B CG  1 
ATOM   2095  C CD1 . TYR B 1 48  ? 37.196  -5.301  -43.900  1.00 34.34 ? 48  TYR B CD1 1 
ATOM   2096  C CD2 . TYR B 1 48  ? 37.307  -7.600  -44.500  1.00 34.56 ? 48  TYR B CD2 1 
ATOM   2097  C CE1 . TYR B 1 48  ? 38.222  -5.473  -42.990  1.00 35.79 ? 48  TYR B CE1 1 
ATOM   2098  C CE2 . TYR B 1 48  ? 38.335  -7.783  -43.588  1.00 36.96 ? 48  TYR B CE2 1 
ATOM   2099  C CZ  . TYR B 1 48  ? 38.788  -6.717  -42.841  1.00 36.72 ? 48  TYR B CZ  1 
ATOM   2100  O OH  . TYR B 1 48  ? 39.805  -6.888  -41.943  1.00 37.02 ? 48  TYR B OH  1 
ATOM   2101  N N   . GLU B 1 49  ? 34.569  -6.484  -48.586  1.00 26.59 ? 49  GLU B N   1 
ATOM   2102  C CA  . GLU B 1 49  ? 33.497  -6.627  -49.573  1.00 26.23 ? 49  GLU B CA  1 
ATOM   2103  C C   . GLU B 1 49  ? 32.877  -8.026  -49.375  1.00 24.49 ? 49  GLU B C   1 
ATOM   2104  O O   . GLU B 1 49  ? 33.602  -9.026  -49.408  1.00 25.04 ? 49  GLU B O   1 
ATOM   2105  C CB  . GLU B 1 49  ? 34.116  -6.477  -50.965  1.00 28.58 ? 49  GLU B CB  1 
ATOM   2106  C CG  . GLU B 1 49  ? 33.193  -6.695  -52.158  1.00 30.76 ? 49  GLU B CG  1 
ATOM   2107  C CD  . GLU B 1 49  ? 33.928  -6.937  -53.483  1.00 31.47 ? 49  GLU B CD  1 
ATOM   2108  O OE1 . GLU B 1 49  ? 33.239  -7.343  -54.424  1.00 33.68 ? 49  GLU B OE1 1 
ATOM   2109  O OE2 . GLU B 1 49  ? 35.160  -6.766  -53.614  1.00 30.29 ? 49  GLU B OE2 1 
ATOM   2110  N N   . LEU B 1 50  ? 31.569  -8.099  -49.138  1.00 22.29 ? 50  LEU B N   1 
ATOM   2111  C CA  . LEU B 1 50  ? 30.924  -9.395  -48.879  1.00 21.11 ? 50  LEU B CA  1 
ATOM   2112  C C   . LEU B 1 50  ? 30.235  -10.007 -50.091  1.00 19.72 ? 50  LEU B C   1 
ATOM   2113  O O   . LEU B 1 50  ? 29.672  -9.304  -50.927  1.00 17.87 ? 50  LEU B O   1 
ATOM   2114  C CB  . LEU B 1 50  ? 29.869  -9.276  -47.789  1.00 21.51 ? 50  LEU B CB  1 
ATOM   2115  C CG  . LEU B 1 50  ? 30.300  -8.864  -46.399  1.00 22.11 ? 50  LEU B CG  1 
ATOM   2116  C CD1 . LEU B 1 50  ? 29.055  -8.937  -45.503  1.00 22.78 ? 50  LEU B CD1 1 
ATOM   2117  C CD2 . LEU B 1 50  ? 31.437  -9.749  -45.889  1.00 21.91 ? 50  LEU B CD2 1 
ATOM   2118  N N   . VAL B 1 51  ? 30.270  -11.342 -50.152  1.00 19.19 ? 51  VAL B N   1 
ATOM   2119  C CA  . VAL B 1 51  ? 29.424  -12.119 -51.064  1.00 17.91 ? 51  VAL B CA  1 
ATOM   2120  C C   . VAL B 1 51  ? 28.630  -13.080 -50.188  1.00 16.79 ? 51  VAL B C   1 
ATOM   2121  O O   . VAL B 1 51  ? 29.210  -13.778 -49.370  1.00 16.00 ? 51  VAL B O   1 
ATOM   2122  C CB  . VAL B 1 51  ? 30.261  -12.899 -52.076  1.00 17.31 ? 51  VAL B CB  1 
ATOM   2123  C CG1 . VAL B 1 51  ? 29.369  -13.502 -53.140  1.00 17.24 ? 51  VAL B CG1 1 
ATOM   2124  C CG2 . VAL B 1 51  ? 31.284  -11.980 -52.731  1.00 16.83 ? 51  VAL B CG2 1 
ATOM   2125  N N   . VAL B 1 52  ? 27.315  -13.097 -50.346  1.00 16.32 ? 52  VAL B N   1 
ATOM   2126  C CA  . VAL B 1 52  ? 26.456  -13.826 -49.414  1.00 15.93 ? 52  VAL B CA  1 
ATOM   2127  C C   . VAL B 1 52  ? 25.589  -14.862 -50.120  1.00 15.25 ? 52  VAL B C   1 
ATOM   2128  O O   . VAL B 1 52  ? 24.911  -14.564 -51.086  1.00 13.93 ? 52  VAL B O   1 
ATOM   2129  C CB  . VAL B 1 52  ? 25.556  -12.862 -48.613  1.00 16.20 ? 52  VAL B CB  1 
ATOM   2130  C CG1 . VAL B 1 52  ? 24.728  -13.631 -47.590  1.00 16.43 ? 52  VAL B CG1 1 
ATOM   2131  C CG2 . VAL B 1 52  ? 26.393  -11.805 -47.917  1.00 16.14 ? 52  VAL B CG2 1 
ATOM   2132  N N   . ASP B 1 53  ? 25.615  -16.089 -49.610  1.00 15.86 ? 53  ASP B N   1 
ATOM   2133  C CA  . ASP B 1 53  ? 24.786  -17.156 -50.157  1.00 16.56 ? 53  ASP B CA  1 
ATOM   2134  C C   . ASP B 1 53  ? 24.060  -17.893 -49.060  1.00 17.22 ? 53  ASP B C   1 
ATOM   2135  O O   . ASP B 1 53  ? 24.571  -18.855 -48.514  1.00 17.74 ? 53  ASP B O   1 
ATOM   2136  C CB  . ASP B 1 53  ? 25.618  -18.124 -50.996  1.00 15.91 ? 53  ASP B CB  1 
ATOM   2137  C CG  . ASP B 1 53  ? 24.781  -18.837 -52.032  1.00 15.49 ? 53  ASP B CG  1 
ATOM   2138  O OD1 . ASP B 1 53  ? 23.910  -19.642 -51.647  1.00 15.67 ? 53  ASP B OD1 1 
ATOM   2139  O OD2 . ASP B 1 53  ? 25.004  -18.597 -53.231  1.00 14.99 ? 53  ASP B OD2 1 
ATOM   2140  N N   . GLY B 1 54  ? 22.858  -17.419 -48.745  1.00 18.35 ? 54  GLY B N   1 
ATOM   2141  C CA  . GLY B 1 54  ? 21.997  -18.038 -47.739  1.00 18.93 ? 54  GLY B CA  1 
ATOM   2142  C C   . GLY B 1 54  ? 20.773  -18.675 -48.373  1.00 19.09 ? 54  GLY B C   1 
ATOM   2143  O O   . GLY B 1 54  ? 19.985  -17.988 -49.011  1.00 18.80 ? 54  GLY B O   1 
ATOM   2144  N N   . LEU B 1 55  ? 20.624  -19.987 -48.178  1.00 19.84 ? 55  LEU B N   1 
ATOM   2145  C CA  . LEU B 1 55  ? 19.496  -20.757 -48.721  1.00 20.39 ? 55  LEU B CA  1 
ATOM   2146  C C   . LEU B 1 55  ? 18.640  -21.328 -47.606  1.00 20.59 ? 55  LEU B C   1 
ATOM   2147  O O   . LEU B 1 55  ? 19.110  -22.146 -46.830  1.00 20.34 ? 55  LEU B O   1 
ATOM   2148  C CB  . LEU B 1 55  ? 20.010  -21.915 -49.596  1.00 20.08 ? 55  LEU B CB  1 
ATOM   2149  C CG  . LEU B 1 55  ? 18.942  -22.879 -50.161  1.00 19.89 ? 55  LEU B CG  1 
ATOM   2150  C CD1 . LEU B 1 55  ? 17.889  -22.154 -51.000  1.00 19.59 ? 55  LEU B CD1 1 
ATOM   2151  C CD2 . LEU B 1 55  ? 19.594  -23.978 -51.002  1.00 19.73 ? 55  LEU B CD2 1 
ATOM   2152  N N   . SER B 1 56  ? 17.379  -20.907 -47.548  1.00 22.22 ? 56  SER B N   1 
ATOM   2153  C CA  . SER B 1 56  ? 16.430  -21.483 -46.600  1.00 23.54 ? 56  SER B CA  1 
ATOM   2154  C C   . SER B 1 56  ? 16.438  -22.989 -46.740  1.00 23.31 ? 56  SER B C   1 
ATOM   2155  O O   . SER B 1 56  ? 16.366  -23.507 -47.842  1.00 25.47 ? 56  SER B O   1 
ATOM   2156  C CB  . SER B 1 56  ? 15.012  -20.924 -46.820  1.00 24.80 ? 56  SER B CB  1 
ATOM   2157  O OG  . SER B 1 56  ? 14.990  -19.483 -46.887  1.00 26.39 ? 56  SER B OG  1 
ATOM   2158  N N   . GLY B 1 57  ? 16.583  -23.694 -45.626  1.00 23.05 ? 57  GLY B N   1 
ATOM   2159  C CA  . GLY B 1 57  ? 16.499  -25.160 -45.600  1.00 22.84 ? 57  GLY B CA  1 
ATOM   2160  C C   . GLY B 1 57  ? 17.805  -25.918 -45.745  1.00 22.43 ? 57  GLY B C   1 
ATOM   2161  O O   . GLY B 1 57  ? 17.824  -27.151 -45.597  1.00 21.67 ? 57  GLY B O   1 
ATOM   2162  N N   . ARG B 1 58  ? 18.893  -25.196 -46.000  1.00 22.53 ? 58  ARG B N   1 
ATOM   2163  C CA  . ARG B 1 58  ? 20.181  -25.801 -46.373  1.00 22.24 ? 58  ARG B CA  1 
ATOM   2164  C C   . ARG B 1 58  ? 20.903  -26.522 -45.220  1.00 22.04 ? 58  ARG B C   1 
ATOM   2165  O O   . ARG B 1 58  ? 20.970  -26.022 -44.076  1.00 24.49 ? 58  ARG B O   1 
ATOM   2166  C CB  . ARG B 1 58  ? 21.098  -24.737 -46.980  1.00 22.07 ? 58  ARG B CB  1 
ATOM   2167  C CG  . ARG B 1 58  ? 22.507  -25.205 -47.358  1.00 22.48 ? 58  ARG B CG  1 
ATOM   2168  C CD  . ARG B 1 58  ? 23.341  -24.046 -47.918  1.00 22.21 ? 58  ARG B CD  1 
ATOM   2169  N NE  . ARG B 1 58  ? 23.128  -23.826 -49.354  1.00 21.82 ? 58  ARG B NE  1 
ATOM   2170  C CZ  . ARG B 1 58  ? 23.390  -22.688 -49.999  1.00 21.73 ? 58  ARG B CZ  1 
ATOM   2171  N NH1 . ARG B 1 58  ? 23.845  -21.617 -49.367  1.00 21.39 ? 58  ARG B NH1 1 
ATOM   2172  N NH2 . ARG B 1 58  ? 23.180  -22.614 -51.300  1.00 21.64 ? 58  ARG B NH2 1 
ATOM   2173  N N   . THR B 1 59  ? 21.454  -27.690 -45.546  1.00 19.74 ? 59  THR B N   1 
ATOM   2174  C CA  . THR B 1 59  ? 22.206  -28.511 -44.600  1.00 18.86 ? 59  THR B CA  1 
ATOM   2175  C C   . THR B 1 59  ? 23.690  -28.409 -44.893  1.00 18.67 ? 59  THR B C   1 
ATOM   2176  O O   . THR B 1 59  ? 24.079  -27.855 -45.923  1.00 19.32 ? 59  THR B O   1 
ATOM   2177  C CB  . THR B 1 59  ? 21.811  -29.988 -44.711  1.00 18.42 ? 59  THR B CB  1 
ATOM   2178  O OG1 . THR B 1 59  ? 22.361  -30.548 -45.909  1.00 19.10 ? 59  THR B OG1 1 
ATOM   2179  C CG2 . THR B 1 59  ? 20.303  -30.133 -44.723  1.00 18.22 ? 59  THR B CG2 1 
ATOM   2180  N N   . THR B 1 60  ? 24.514  -28.953 -44.007  1.00 18.62 ? 60  THR B N   1 
ATOM   2181  C CA  . THR B 1 60  ? 25.947  -29.046 -44.258  1.00 18.44 ? 60  THR B CA  1 
ATOM   2182  C C   . THR B 1 60  ? 26.220  -29.890 -45.499  1.00 18.16 ? 60  THR B C   1 
ATOM   2183  O O   . THR B 1 60  ? 26.698  -29.374 -46.505  1.00 18.89 ? 60  THR B O   1 
ATOM   2184  C CB  . THR B 1 60  ? 26.715  -29.695 -43.073  1.00 18.80 ? 60  THR B CB  1 
ATOM   2185  O OG1 . THR B 1 60  ? 26.095  -30.938 -42.705  1.00 17.75 ? 60  THR B OG1 1 
ATOM   2186  C CG2 . THR B 1 60  ? 26.726  -28.778 -41.874  1.00 19.01 ? 60  THR B CG2 1 
ATOM   2187  N N   . ASN B 1 61  ? 25.900  -31.182 -45.427  1.00 17.87 ? 61  ASN B N   1 
ATOM   2188  C CA  . ASN B 1 61  ? 26.336  -32.142 -46.447  1.00 17.21 ? 61  ASN B CA  1 
ATOM   2189  C C   . ASN B 1 61  ? 25.421  -33.356 -46.649  1.00 16.22 ? 61  ASN B C   1 
ATOM   2190  O O   . ASN B 1 61  ? 25.884  -34.398 -47.067  1.00 15.71 ? 61  ASN B O   1 
ATOM   2191  C CB  . ASN B 1 61  ? 27.736  -32.641 -46.071  1.00 16.84 ? 61  ASN B CB  1 
ATOM   2192  C CG  . ASN B 1 61  ? 27.706  -33.695 -44.996  1.00 16.32 ? 61  ASN B CG  1 
ATOM   2193  O OD1 . ASN B 1 61  ? 26.806  -33.738 -44.161  1.00 16.74 ? 61  ASN B OD1 1 
ATOM   2194  N ND2 . ASN B 1 61  ? 28.690  -34.551 -45.012  1.00 15.75 ? 61  ASN B ND2 1 
ATOM   2195  N N   . ILE B 1 62  ? 24.137  -33.207 -46.368  1.00 15.87 ? 62  ILE B N   1 
ATOM   2196  C CA  . ILE B 1 62  ? 23.187  -34.319 -46.442  1.00 15.84 ? 62  ILE B CA  1 
ATOM   2197  C C   . ILE B 1 62  ? 21.951  -33.956 -47.258  1.00 16.08 ? 62  ILE B C   1 
ATOM   2198  O O   . ILE B 1 62  ? 21.438  -32.845 -47.143  1.00 15.29 ? 62  ILE B O   1 
ATOM   2199  C CB  . ILE B 1 62  ? 22.755  -34.760 -45.031  1.00 15.74 ? 62  ILE B CB  1 
ATOM   2200  C CG1 . ILE B 1 62  ? 21.898  -36.029 -45.090  1.00 15.37 ? 62  ILE B CG1 1 
ATOM   2201  C CG2 . ILE B 1 62  ? 22.012  -33.638 -44.317  1.00 15.63 ? 62  ILE B CG2 1 
ATOM   2202  C CD1 . ILE B 1 62  ? 21.755  -36.666 -43.743  1.00 15.01 ? 62  ILE B CD1 1 
ATOM   2203  N N   . ASP B 1 63  ? 21.494  -34.896 -48.087  1.00 17.29 ? 63  ASP B N   1 
ATOM   2204  C CA  . ASP B 1 63  ? 20.290  -34.700 -48.906  1.00 18.22 ? 63  ASP B CA  1 
ATOM   2205  C C   . ASP B 1 63  ? 19.037  -34.622 -48.067  1.00 18.80 ? 63  ASP B C   1 
ATOM   2206  O O   . ASP B 1 63  ? 18.856  -35.411 -47.127  1.00 19.23 ? 63  ASP B O   1 
ATOM   2207  C CB  . ASP B 1 63  ? 20.091  -35.829 -49.916  1.00 18.74 ? 63  ASP B CB  1 
ATOM   2208  C CG  . ASP B 1 63  ? 21.171  -35.874 -50.954  1.00 19.59 ? 63  ASP B CG  1 
ATOM   2209  O OD1 . ASP B 1 63  ? 21.689  -34.789 -51.312  1.00 18.91 ? 63  ASP B OD1 1 
ATOM   2210  O OD2 . ASP B 1 63  ? 21.512  -37.002 -51.400  1.00 19.99 ? 63  ASP B OD2 1 
ATOM   2211  N N   . ASP B 1 64  ? 18.179  -33.663 -48.402  1.00 19.16 ? 64  ASP B N   1 
ATOM   2212  C CA  . ASP B 1 64  ? 16.863  -33.598 -47.801  1.00 18.63 ? 64  ASP B CA  1 
ATOM   2213  C C   . ASP B 1 64  ? 15.901  -34.315 -48.754  1.00 18.84 ? 64  ASP B C   1 
ATOM   2214  O O   . ASP B 1 64  ? 15.711  -33.879 -49.901  1.00 19.38 ? 64  ASP B O   1 
ATOM   2215  C CB  . ASP B 1 64  ? 16.440  -32.145 -47.553  1.00 18.13 ? 64  ASP B CB  1 
ATOM   2216  C CG  . ASP B 1 64  ? 15.254  -32.044 -46.628  1.00 18.35 ? 64  ASP B CG  1 
ATOM   2217  O OD1 . ASP B 1 64  ? 14.237  -32.703 -46.903  1.00 19.27 ? 64  ASP B OD1 1 
ATOM   2218  O OD2 . ASP B 1 64  ? 15.315  -31.306 -45.633  1.00 17.81 ? 64  ASP B OD2 1 
ATOM   2219  N N   . PRO B 1 65  ? 15.287  -35.426 -48.302  1.00 18.32 ? 65  PRO B N   1 
ATOM   2220  C CA  . PRO B 1 65  ? 14.381  -36.128 -49.226  1.00 17.49 ? 65  PRO B CA  1 
ATOM   2221  C C   . PRO B 1 65  ? 13.184  -35.277 -49.689  1.00 16.33 ? 65  PRO B C   1 
ATOM   2222  O O   . PRO B 1 65  ? 12.550  -35.617 -50.674  1.00 15.19 ? 65  PRO B O   1 
ATOM   2223  C CB  . PRO B 1 65  ? 13.938  -37.363 -48.425  1.00 17.55 ? 65  PRO B CB  1 
ATOM   2224  C CG  . PRO B 1 65  ? 14.167  -37.015 -46.996  1.00 17.79 ? 65  PRO B CG  1 
ATOM   2225  C CD  . PRO B 1 65  ? 15.337  -36.071 -46.979  1.00 18.14 ? 65  PRO B CD  1 
ATOM   2226  N N   . ASN B 1 66  ? 12.908  -34.175 -48.994  1.00 16.31 ? 66  ASN B N   1 
ATOM   2227  C CA  . ASN B 1 66  ? 11.822  -33.272 -49.357  1.00 16.78 ? 66  ASN B CA  1 
ATOM   2228  C C   . ASN B 1 66  ? 12.161  -32.234 -50.418  1.00 16.81 ? 66  ASN B C   1 
ATOM   2229  O O   . ASN B 1 66  ? 11.257  -31.633 -50.983  1.00 15.89 ? 66  ASN B O   1 
ATOM   2230  C CB  . ASN B 1 66  ? 11.307  -32.547 -48.123  1.00 16.87 ? 66  ASN B CB  1 
ATOM   2231  C CG  . ASN B 1 66  ? 10.772  -33.500 -47.086  1.00 17.60 ? 66  ASN B CG  1 
ATOM   2232  O OD1 . ASN B 1 66  ? 9.710   -34.081 -47.273  1.00 17.97 ? 66  ASN B OD1 1 
ATOM   2233  N ND2 . ASN B 1 66  ? 11.516  -33.689 -45.988  1.00 18.83 ? 66  ASN B ND2 1 
ATOM   2234  N N   . ASP B 1 67  ? 13.447  -32.021 -50.686  1.00 17.46 ? 67  ASP B N   1 
ATOM   2235  C CA  . ASP B 1 67  ? 13.870  -30.983 -51.625  1.00 18.07 ? 67  ASP B CA  1 
ATOM   2236  C C   . ASP B 1 67  ? 15.321  -31.229 -52.062  1.00 19.75 ? 67  ASP B C   1 
ATOM   2237  O O   . ASP B 1 67  ? 16.263  -31.161 -51.243  1.00 22.20 ? 67  ASP B O   1 
ATOM   2238  C CB  . ASP B 1 67  ? 13.739  -29.602 -50.974  1.00 17.40 ? 67  ASP B CB  1 
ATOM   2239  C CG  . ASP B 1 67  ? 13.909  -28.467 -51.947  1.00 17.02 ? 67  ASP B CG  1 
ATOM   2240  O OD1 . ASP B 1 67  ? 14.397  -28.678 -53.087  1.00 16.50 ? 67  ASP B OD1 1 
ATOM   2241  O OD2 . ASP B 1 67  ? 13.538  -27.345 -51.544  1.00 16.66 ? 67  ASP B OD2 1 
ATOM   2242  N N   . PRO B 1 68  ? 15.517  -31.519 -53.355  1.00 19.74 ? 68  PRO B N   1 
ATOM   2243  C CA  . PRO B 1 68  ? 16.857  -31.864 -53.792  1.00 19.89 ? 68  PRO B CA  1 
ATOM   2244  C C   . PRO B 1 68  ? 17.865  -30.697 -53.875  1.00 20.20 ? 68  PRO B C   1 
ATOM   2245  O O   . PRO B 1 68  ? 19.001  -30.939 -54.207  1.00 21.75 ? 68  PRO B O   1 
ATOM   2246  C CB  . PRO B 1 68  ? 16.637  -32.499 -55.166  1.00 20.15 ? 68  PRO B CB  1 
ATOM   2247  C CG  . PRO B 1 68  ? 15.270  -32.101 -55.603  1.00 20.01 ? 68  PRO B CG  1 
ATOM   2248  C CD  . PRO B 1 68  ? 14.508  -31.625 -54.421  1.00 19.76 ? 68  PRO B CD  1 
ATOM   2249  N N   . LYS B 1 69  ? 17.492  -29.464 -53.569  1.00 19.78 ? 69  LYS B N   1 
ATOM   2250  C CA  . LYS B 1 69  ? 18.459  -28.353 -53.657  1.00 19.68 ? 69  LYS B CA  1 
ATOM   2251  C C   . LYS B 1 69  ? 19.094  -27.904 -52.333  1.00 20.70 ? 69  LYS B C   1 
ATOM   2252  O O   . LYS B 1 69  ? 19.772  -26.883 -52.313  1.00 21.51 ? 69  LYS B O   1 
ATOM   2253  C CB  . LYS B 1 69  ? 17.815  -27.136 -54.349  1.00 19.01 ? 69  LYS B CB  1 
ATOM   2254  C CG  . LYS B 1 69  ? 16.770  -26.379 -53.528  1.00 18.07 ? 69  LYS B CG  1 
ATOM   2255  C CD  . LYS B 1 69  ? 16.097  -25.302 -54.366  1.00 17.10 ? 69  LYS B CD  1 
ATOM   2256  C CE  . LYS B 1 69  ? 15.070  -24.515 -53.587  1.00 16.54 ? 69  LYS B CE  1 
ATOM   2257  N NZ  . LYS B 1 69  ? 13.777  -25.218 -53.457  1.00 16.44 ? 69  LYS B NZ  1 
ATOM   2258  N N   . LEU B 1 70  ? 18.896  -28.658 -51.256  1.00 21.60 ? 70  LEU B N   1 
ATOM   2259  C CA  . LEU B 1 70  ? 19.235  -28.189 -49.899  1.00 21.05 ? 70  LEU B CA  1 
ATOM   2260  C C   . LEU B 1 70  ? 20.558  -28.700 -49.330  1.00 21.12 ? 70  LEU B C   1 
ATOM   2261  O O   . LEU B 1 70  ? 20.878  -28.435 -48.170  1.00 21.45 ? 70  LEU B O   1 
ATOM   2262  C CB  . LEU B 1 70  ? 18.115  -28.561 -48.930  1.00 20.72 ? 70  LEU B CB  1 
ATOM   2263  C CG  . LEU B 1 70  ? 16.749  -27.999 -49.279  1.00 21.28 ? 70  LEU B CG  1 
ATOM   2264  C CD1 . LEU B 1 70  ? 15.735  -28.388 -48.209  1.00 21.10 ? 70  LEU B CD1 1 
ATOM   2265  C CD2 . LEU B 1 70  ? 16.831  -26.488 -49.441  1.00 21.54 ? 70  LEU B CD2 1 
ATOM   2266  N N   . ASN B 1 71  ? 21.330  -29.427 -50.129  1.00 20.99 ? 71  ASN B N   1 
ATOM   2267  C CA  . ASN B 1 71  ? 22.581  -29.971 -49.644  1.00 20.65 ? 71  ASN B CA  1 
ATOM   2268  C C   . ASN B 1 71  ? 23.721  -28.988 -49.915  1.00 21.11 ? 71  ASN B C   1 
ATOM   2269  O O   . ASN B 1 71  ? 24.142  -28.830 -51.066  1.00 21.93 ? 71  ASN B O   1 
ATOM   2270  C CB  . ASN B 1 71  ? 22.860  -31.292 -50.329  1.00 20.25 ? 71  ASN B CB  1 
ATOM   2271  C CG  . ASN B 1 71  ? 24.010  -32.050 -49.692  1.00 19.87 ? 71  ASN B CG  1 
ATOM   2272  O OD1 . ASN B 1 71  ? 25.009  -31.464 -49.273  1.00 19.61 ? 71  ASN B OD1 1 
ATOM   2273  N ND2 . ASN B 1 71  ? 23.879  -33.366 -49.627  1.00 19.13 ? 71  ASN B ND2 1 
ATOM   2274  N N   . GLY B 1 72  ? 24.229  -28.348 -48.856  1.00 19.76 ? 72  GLY B N   1 
ATOM   2275  C CA  . GLY B 1 72  ? 25.315  -27.378 -48.982  1.00 18.38 ? 72  GLY B CA  1 
ATOM   2276  C C   . GLY B 1 72  ? 26.500  -27.866 -49.806  1.00 17.49 ? 72  GLY B C   1 
ATOM   2277  O O   . GLY B 1 72  ? 27.032  -27.131 -50.638  1.00 16.66 ? 72  GLY B O   1 
ATOM   2278  N N   . ALA B 1 73  ? 26.887  -29.115 -49.590  1.00 17.25 ? 73  ALA B N   1 
ATOM   2279  C CA  . ALA B 1 73  ? 28.058  -29.698 -50.233  1.00 17.51 ? 73  ALA B CA  1 
ATOM   2280  C C   . ALA B 1 73  ? 27.859  -29.981 -51.730  1.00 17.38 ? 73  ALA B C   1 
ATOM   2281  O O   . ALA B 1 73  ? 28.830  -30.061 -52.485  1.00 17.56 ? 73  ALA B O   1 
ATOM   2282  C CB  . ALA B 1 73  ? 28.470  -30.964 -49.495  1.00 17.61 ? 73  ALA B CB  1 
ATOM   2283  N N   . ASP B 1 74  ? 26.613  -30.137 -52.163  1.00 17.35 ? 74  ASP B N   1 
ATOM   2284  C CA  . ASP B 1 74  ? 26.315  -30.189 -53.601  1.00 17.54 ? 74  ASP B CA  1 
ATOM   2285  C C   . ASP B 1 74  ? 26.662  -28.865 -54.292  1.00 18.09 ? 74  ASP B C   1 
ATOM   2286  O O   . ASP B 1 74  ? 27.021  -28.864 -55.444  1.00 18.28 ? 74  ASP B O   1 
ATOM   2287  C CB  . ASP B 1 74  ? 24.826  -30.470 -53.861  1.00 17.54 ? 74  ASP B CB  1 
ATOM   2288  C CG  . ASP B 1 74  ? 24.437  -31.920 -53.645  1.00 17.30 ? 74  ASP B CG  1 
ATOM   2289  O OD1 . ASP B 1 74  ? 25.322  -32.800 -53.574  1.00 17.58 ? 74  ASP B OD1 1 
ATOM   2290  O OD2 . ASP B 1 74  ? 23.221  -32.175 -53.543  1.00 16.96 ? 74  ASP B OD2 1 
ATOM   2291  N N   . TYR B 1 75  ? 26.544  -27.751 -53.573  1.00 19.02 ? 75  TYR B N   1 
ATOM   2292  C CA  . TYR B 1 75  ? 26.607  -26.394 -54.134  1.00 20.09 ? 75  TYR B CA  1 
ATOM   2293  C C   . TYR B 1 75  ? 27.974  -25.715 -53.949  1.00 21.20 ? 75  TYR B C   1 
ATOM   2294  O O   . TYR B 1 75  ? 28.418  -24.930 -54.807  1.00 21.36 ? 75  TYR B O   1 
ATOM   2295  C CB  . TYR B 1 75  ? 25.539  -25.580 -53.423  1.00 20.31 ? 75  TYR B CB  1 
ATOM   2296  C CG  . TYR B 1 75  ? 25.165  -24.189 -53.918  1.00 21.07 ? 75  TYR B CG  1 
ATOM   2297  C CD1 . TYR B 1 75  ? 24.224  -24.013 -54.927  1.00 21.44 ? 75  TYR B CD1 1 
ATOM   2298  C CD2 . TYR B 1 75  ? 25.652  -23.045 -53.276  1.00 20.91 ? 75  TYR B CD2 1 
ATOM   2299  C CE1 . TYR B 1 75  ? 23.830  -22.737 -55.323  1.00 22.26 ? 75  TYR B CE1 1 
ATOM   2300  C CE2 . TYR B 1 75  ? 25.264  -21.768 -53.664  1.00 20.80 ? 75  TYR B CE2 1 
ATOM   2301  C CZ  . TYR B 1 75  ? 24.352  -21.613 -54.681  1.00 21.19 ? 75  TYR B CZ  1 
ATOM   2302  O OH  . TYR B 1 75  ? 23.931  -20.365 -55.068  1.00 20.24 ? 75  TYR B OH  1 
ATOM   2303  N N   . LEU B 1 76  ? 28.639  -26.019 -52.831  1.00 21.66 ? 76  LEU B N   1 
ATOM   2304  C CA  . LEU B 1 76  ? 29.763  -25.205 -52.383  1.00 21.16 ? 76  LEU B CA  1 
ATOM   2305  C C   . LEU B 1 76  ? 30.951  -25.192 -53.344  1.00 21.09 ? 76  LEU B C   1 
ATOM   2306  O O   . LEU B 1 76  ? 31.521  -24.123 -53.568  1.00 21.67 ? 76  LEU B O   1 
ATOM   2307  C CB  . LEU B 1 76  ? 30.204  -25.612 -50.974  1.00 21.54 ? 76  LEU B CB  1 
ATOM   2308  C CG  . LEU B 1 76  ? 31.290  -24.731 -50.345  1.00 22.38 ? 76  LEU B CG  1 
ATOM   2309  C CD1 . LEU B 1 76  ? 30.886  -23.270 -50.311  1.00 22.38 ? 76  LEU B CD1 1 
ATOM   2310  C CD2 . LEU B 1 76  ? 31.635  -25.206 -48.934  1.00 22.99 ? 76  LEU B CD2 1 
ATOM   2311  N N   . PRO B 1 77  ? 31.344  -26.362 -53.914  1.00 19.67 ? 77  PRO B N   1 
ATOM   2312  C CA  . PRO B 1 77  ? 32.482  -26.324 -54.833  1.00 18.74 ? 77  PRO B CA  1 
ATOM   2313  C C   . PRO B 1 77  ? 32.294  -25.314 -55.965  1.00 18.68 ? 77  PRO B C   1 
ATOM   2314  O O   . PRO B 1 77  ? 33.202  -24.543 -56.256  1.00 18.53 ? 77  PRO B O   1 
ATOM   2315  C CB  . PRO B 1 77  ? 32.550  -27.751 -55.347  1.00 18.34 ? 77  PRO B CB  1 
ATOM   2316  C CG  . PRO B 1 77  ? 32.049  -28.560 -54.226  1.00 18.36 ? 77  PRO B CG  1 
ATOM   2317  C CD  . PRO B 1 77  ? 30.920  -27.745 -53.655  1.00 18.90 ? 77  PRO B CD  1 
ATOM   2318  N N   . ALA B 1 78  ? 31.120  -25.316 -56.575  1.00 19.39 ? 78  ALA B N   1 
ATOM   2319  C CA  . ALA B 1 78  ? 30.814  -24.372 -57.655  1.00 20.59 ? 78  ALA B CA  1 
ATOM   2320  C C   . ALA B 1 78  ? 30.824  -22.937 -57.154  1.00 20.04 ? 78  ALA B C   1 
ATOM   2321  O O   . ALA B 1 78  ? 31.384  -22.061 -57.794  1.00 19.85 ? 78  ALA B O   1 
ATOM   2322  C CB  . ALA B 1 78  ? 29.460  -24.693 -58.285  1.00 21.84 ? 78  ALA B CB  1 
ATOM   2323  N N   . ALA B 1 79  ? 30.206  -22.706 -56.007  1.00 19.68 ? 79  ALA B N   1 
ATOM   2324  C CA  . ALA B 1 79  ? 30.122  -21.369 -55.444  1.00 20.43 ? 79  ALA B CA  1 
ATOM   2325  C C   . ALA B 1 79  ? 31.508  -20.786 -55.187  1.00 20.20 ? 79  ALA B C   1 
ATOM   2326  O O   . ALA B 1 79  ? 31.781  -19.638 -55.528  1.00 19.19 ? 79  ALA B O   1 
ATOM   2327  C CB  . ALA B 1 79  ? 29.311  -21.401 -54.151  1.00 21.54 ? 79  ALA B CB  1 
ATOM   2328  N N   . LEU B 1 80  ? 32.388  -21.593 -54.610  1.00 21.03 ? 80  LEU B N   1 
ATOM   2329  C CA  . LEU B 1 80  ? 33.749  -21.159 -54.294  1.00 21.34 ? 80  LEU B CA  1 
ATOM   2330  C C   . LEU B 1 80  ? 34.509  -20.702 -55.533  1.00 21.85 ? 80  LEU B C   1 
ATOM   2331  O O   . LEU B 1 80  ? 35.193  -19.672 -55.508  1.00 23.50 ? 80  LEU B O   1 
ATOM   2332  C CB  . LEU B 1 80  ? 34.522  -22.287 -53.614  1.00 20.70 ? 80  LEU B CB  1 
ATOM   2333  C CG  . LEU B 1 80  ? 34.088  -22.638 -52.196  1.00 20.72 ? 80  LEU B CG  1 
ATOM   2334  C CD1 . LEU B 1 80  ? 34.633  -24.005 -51.808  1.00 20.58 ? 80  LEU B CD1 1 
ATOM   2335  C CD2 . LEU B 1 80  ? 34.529  -21.558 -51.209  1.00 21.17 ? 80  LEU B CD2 1 
ATOM   2336  N N   . ALA B 1 81  ? 34.382  -21.481 -56.611  1.00 21.50 ? 81  ALA B N   1 
ATOM   2337  C CA  . ALA B 1 81  ? 35.071  -21.223 -57.871  1.00 21.71 ? 81  ALA B CA  1 
ATOM   2338  C C   . ALA B 1 81  ? 34.509  -20.018 -58.589  1.00 22.19 ? 81  ALA B C   1 
ATOM   2339  O O   . ALA B 1 81  ? 35.213  -19.342 -59.351  1.00 23.97 ? 81  ALA B O   1 
ATOM   2340  C CB  . ALA B 1 81  ? 34.967  -22.445 -58.754  1.00 21.48 ? 81  ALA B CB  1 
ATOM   2341  N N   . ALA B 1 82  ? 33.221  -19.783 -58.363  1.00 22.71 ? 82  ALA B N   1 
ATOM   2342  C CA  . ALA B 1 82  ? 32.492  -18.687 -58.983  1.00 22.58 ? 82  ALA B CA  1 
ATOM   2343  C C   . ALA B 1 82  ? 32.799  -17.342 -58.325  1.00 22.61 ? 82  ALA B C   1 
ATOM   2344  O O   . ALA B 1 82  ? 32.565  -16.291 -58.929  1.00 21.88 ? 82  ALA B O   1 
ATOM   2345  C CB  . ALA B 1 82  ? 31.002  -18.971 -58.922  1.00 22.90 ? 82  ALA B CB  1 
ATOM   2346  N N   . HIS B 1 83  ? 33.296  -17.379 -57.088  1.00 23.23 ? 83  HIS B N   1 
ATOM   2347  C CA  . HIS B 1 83  ? 33.622  -16.167 -56.348  1.00 23.72 ? 83  HIS B CA  1 
ATOM   2348  C C   . HIS B 1 83  ? 35.109  -16.013 -56.027  1.00 24.02 ? 83  HIS B C   1 
ATOM   2349  O O   . HIS B 1 83  ? 35.503  -15.052 -55.361  1.00 24.76 ? 83  HIS B O   1 
ATOM   2350  C CB  . HIS B 1 83  ? 32.783  -16.105 -55.082  1.00 24.29 ? 83  HIS B CB  1 
ATOM   2351  C CG  . HIS B 1 83  ? 31.319  -16.160 -55.349  1.00 25.62 ? 83  HIS B CG  1 
ATOM   2352  N ND1 . HIS B 1 83  ? 30.703  -15.335 -56.270  1.00 27.99 ? 83  HIS B ND1 1 
ATOM   2353  C CD2 . HIS B 1 83  ? 30.349  -16.950 -54.836  1.00 25.00 ? 83  HIS B CD2 1 
ATOM   2354  C CE1 . HIS B 1 83  ? 29.411  -15.621 -56.309  1.00 27.96 ? 83  HIS B CE1 1 
ATOM   2355  N NE2 . HIS B 1 83  ? 29.171  -16.596 -55.445  1.00 26.71 ? 83  HIS B NE2 1 
ATOM   2356  N N   . GLU B 1 84  ? 35.931  -16.933 -56.523  1.00 23.83 ? 84  GLU B N   1 
ATOM   2357  C CA  . GLU B 1 84  ? 37.382  -16.802 -56.418  1.00 23.93 ? 84  GLU B CA  1 
ATOM   2358  C C   . GLU B 1 84  ? 37.831  -15.464 -57.068  1.00 23.92 ? 84  GLU B C   1 
ATOM   2359  O O   . GLU B 1 84  ? 37.329  -15.104 -58.145  1.00 22.45 ? 84  GLU B O   1 
ATOM   2360  C CB  . GLU B 1 84  ? 38.064  -17.992 -57.105  1.00 23.77 ? 84  GLU B CB  1 
ATOM   2361  C CG  . GLU B 1 84  ? 39.559  -18.064 -56.874  1.00 23.92 ? 84  GLU B CG  1 
ATOM   2362  C CD  . GLU B 1 84  ? 40.239  -19.218 -57.586  1.00 24.96 ? 84  GLU B CD  1 
ATOM   2363  O OE1 . GLU B 1 84  ? 41.093  -19.833 -56.932  1.00 25.73 ? 84  GLU B OE1 1 
ATOM   2364  O OE2 . GLU B 1 84  ? 39.946  -19.494 -58.775  1.00 26.08 ? 84  GLU B OE2 1 
ATOM   2365  N N   . PRO B 1 85  ? 38.765  -14.735 -56.443  1.00 23.85 ? 85  PRO B N   1 
ATOM   2366  C CA  . PRO B 1 85  ? 39.472  -15.131 -55.218  1.00 23.24 ? 85  PRO B CA  1 
ATOM   2367  C C   . PRO B 1 85  ? 38.837  -14.573 -53.958  1.00 22.49 ? 85  PRO B C   1 
ATOM   2368  O O   . PRO B 1 85  ? 38.335  -13.443 -53.962  1.00 23.96 ? 85  PRO B O   1 
ATOM   2369  C CB  . PRO B 1 85  ? 40.845  -14.493 -55.400  1.00 22.73 ? 85  PRO B CB  1 
ATOM   2370  C CG  . PRO B 1 85  ? 40.559  -13.248 -56.140  1.00 22.96 ? 85  PRO B CG  1 
ATOM   2371  C CD  . PRO B 1 85  ? 39.407  -13.567 -57.067  1.00 23.64 ? 85  PRO B CD  1 
ATOM   2372  N N   . LEU B 1 86  ? 38.890  -15.360 -52.888  1.00 20.82 ? 86  LEU B N   1 
ATOM   2373  C CA  . LEU B 1 86  ? 38.364  -14.945 -51.610  1.00 20.07 ? 86  LEU B CA  1 
ATOM   2374  C C   . LEU B 1 86  ? 39.482  -14.877 -50.573  1.00 20.63 ? 86  LEU B C   1 
ATOM   2375  O O   . LEU B 1 86  ? 40.502  -15.551 -50.680  1.00 20.30 ? 86  LEU B O   1 
ATOM   2376  C CB  . LEU B 1 86  ? 37.274  -15.904 -51.145  1.00 19.39 ? 86  LEU B CB  1 
ATOM   2377  C CG  . LEU B 1 86  ? 36.056  -16.032 -52.070  1.00 19.01 ? 86  LEU B CG  1 
ATOM   2378  C CD1 . LEU B 1 86  ? 35.256  -17.292 -51.761  1.00 18.82 ? 86  LEU B CD1 1 
ATOM   2379  C CD2 . LEU B 1 86  ? 35.161  -14.800 -51.996  1.00 18.71 ? 86  LEU B CD2 1 
ATOM   2380  N N   . ASP B 1 87  ? 39.264  -14.035 -49.567  1.00 20.73 ? 87  ASP B N   1 
ATOM   2381  C CA  . ASP B 1 87  ? 40.159  -13.908 -48.440  1.00 19.59 ? 87  ASP B CA  1 
ATOM   2382  C C   . ASP B 1 87  ? 39.652  -14.648 -47.218  1.00 19.57 ? 87  ASP B C   1 
ATOM   2383  O O   . ASP B 1 87  ? 40.454  -14.952 -46.319  1.00 20.60 ? 87  ASP B O   1 
ATOM   2384  C CB  . ASP B 1 87  ? 40.360  -12.437 -48.122  1.00 19.71 ? 87  ASP B CB  1 
ATOM   2385  C CG  . ASP B 1 87  ? 41.049  -11.709 -49.247  1.00 20.44 ? 87  ASP B CG  1 
ATOM   2386  O OD1 . ASP B 1 87  ? 40.342  -11.379 -50.216  1.00 20.38 ? 87  ASP B OD1 1 
ATOM   2387  O OD2 . ASP B 1 87  ? 42.278  -11.500 -49.204  1.00 21.67 ? 87  ASP B OD2 1 
ATOM   2388  N N   . LEU B 1 88  ? 38.342  -14.930 -47.176  1.00 19.06 ? 88  LEU B N   1 
ATOM   2389  C CA  . LEU B 1 88  ? 37.740  -15.722 -46.095  1.00 19.34 ? 88  LEU B CA  1 
ATOM   2390  C C   . LEU B 1 88  ? 36.413  -16.375 -46.504  1.00 20.03 ? 88  LEU B C   1 
ATOM   2391  O O   . LEU B 1 88  ? 35.628  -15.803 -47.259  1.00 20.33 ? 88  LEU B O   1 
ATOM   2392  C CB  . LEU B 1 88  ? 37.502  -14.840 -44.860  1.00 18.60 ? 88  LEU B CB  1 
ATOM   2393  C CG  . LEU B 1 88  ? 36.979  -15.513 -43.593  1.00 18.35 ? 88  LEU B CG  1 
ATOM   2394  C CD1 . LEU B 1 88  ? 38.005  -16.465 -42.999  1.00 18.07 ? 88  LEU B CD1 1 
ATOM   2395  C CD2 . LEU B 1 88  ? 36.562  -14.450 -42.602  1.00 18.15 ? 88  LEU B CD2 1 
ATOM   2396  N N   . VAL B 1 89  ? 36.170  -17.578 -45.987  1.00 20.51 ? 89  VAL B N   1 
ATOM   2397  C CA  . VAL B 1 89  ? 34.881  -18.231 -46.145  1.00 21.45 ? 89  VAL B CA  1 
ATOM   2398  C C   . VAL B 1 89  ? 34.271  -18.433 -44.763  1.00 21.93 ? 89  VAL B C   1 
ATOM   2399  O O   . VAL B 1 89  ? 34.885  -19.043 -43.895  1.00 23.89 ? 89  VAL B O   1 
ATOM   2400  C CB  . VAL B 1 89  ? 35.011  -19.592 -46.854  1.00 21.71 ? 89  VAL B CB  1 
ATOM   2401  C CG1 . VAL B 1 89  ? 33.670  -20.320 -46.877  1.00 21.54 ? 89  VAL B CG1 1 
ATOM   2402  C CG2 . VAL B 1 89  ? 35.520  -19.396 -48.274  1.00 22.27 ? 89  VAL B CG2 1 
ATOM   2403  N N   . ILE B 1 90  ? 33.067  -17.910 -44.566  1.00 21.07 ? 90  ILE B N   1 
ATOM   2404  C CA  . ILE B 1 90  ? 32.339  -18.086 -43.332  1.00 21.12 ? 90  ILE B CA  1 
ATOM   2405  C C   . ILE B 1 90  ? 31.225  -19.076 -43.580  1.00 21.12 ? 90  ILE B C   1 
ATOM   2406  O O   . ILE B 1 90  ? 30.483  -18.936 -44.546  1.00 22.68 ? 90  ILE B O   1 
ATOM   2407  C CB  . ILE B 1 90  ? 31.730  -16.756 -42.856  1.00 21.94 ? 90  ILE B CB  1 
ATOM   2408  C CG1 . ILE B 1 90  ? 32.844  -15.784 -42.437  1.00 22.38 ? 90  ILE B CG1 1 
ATOM   2409  C CG2 . ILE B 1 90  ? 30.753  -16.993 -41.716  1.00 22.11 ? 90  ILE B CG2 1 
ATOM   2410  C CD1 . ILE B 1 90  ? 32.350  -14.412 -42.046  1.00 22.73 ? 90  ILE B CD1 1 
ATOM   2411  N N   . ILE B 1 91  ? 31.110  -20.068 -42.705  1.00 21.12 ? 91  ILE B N   1 
ATOM   2412  C CA  . ILE B 1 91  ? 30.062  -21.071 -42.805  1.00 21.24 ? 91  ILE B CA  1 
ATOM   2413  C C   . ILE B 1 91  ? 29.246  -21.002 -41.544  1.00 20.90 ? 91  ILE B C   1 
ATOM   2414  O O   . ILE B 1 91  ? 29.774  -21.214 -40.455  1.00 20.38 ? 91  ILE B O   1 
ATOM   2415  C CB  . ILE B 1 91  ? 30.650  -22.504 -42.959  1.00 21.65 ? 91  ILE B CB  1 
ATOM   2416  C CG1 . ILE B 1 91  ? 31.477  -22.597 -44.250  1.00 21.20 ? 91  ILE B CG1 1 
ATOM   2417  C CG2 . ILE B 1 91  ? 29.550  -23.567 -43.013  1.00 21.21 ? 91  ILE B CG2 1 
ATOM   2418  C CD1 . ILE B 1 91  ? 32.372  -23.807 -44.292  1.00 21.47 ? 91  ILE B CD1 1 
ATOM   2419  N N   . LEU B 1 92  ? 27.959  -20.689 -41.703  1.00 20.78 ? 92  LEU B N   1 
ATOM   2420  C CA  . LEU B 1 92  ? 26.993  -20.717 -40.601  1.00 20.32 ? 92  LEU B CA  1 
ATOM   2421  C C   . LEU B 1 92  ? 25.844  -21.626 -41.020  1.00 19.77 ? 92  LEU B C   1 
ATOM   2422  O O   . LEU B 1 92  ? 24.839  -21.169 -41.602  1.00 19.06 ? 92  LEU B O   1 
ATOM   2423  C CB  . LEU B 1 92  ? 26.502  -19.313 -40.278  1.00 20.85 ? 92  LEU B CB  1 
ATOM   2424  C CG  . LEU B 1 92  ? 25.351  -19.191 -39.269  1.00 21.91 ? 92  LEU B CG  1 
ATOM   2425  C CD1 . LEU B 1 92  ? 25.636  -19.966 -37.983  1.00 22.92 ? 92  LEU B CD1 1 
ATOM   2426  C CD2 . LEU B 1 92  ? 25.068  -17.736 -38.939  1.00 22.51 ? 92  LEU B CD2 1 
ATOM   2427  N N   . LEU B 1 93  ? 26.040  -22.917 -40.725  1.00 19.51 ? 93  LEU B N   1 
ATOM   2428  C CA  . LEU B 1 93  ? 25.113  -23.993 -41.034  1.00 18.92 ? 93  LEU B CA  1 
ATOM   2429  C C   . LEU B 1 93  ? 25.070  -24.956 -39.870  1.00 19.47 ? 93  LEU B C   1 
ATOM   2430  O O   . LEU B 1 93  ? 25.970  -24.984 -39.035  1.00 18.80 ? 93  LEU B O   1 
ATOM   2431  C CB  . LEU B 1 93  ? 25.559  -24.775 -42.260  1.00 18.06 ? 93  LEU B CB  1 
ATOM   2432  C CG  . LEU B 1 93  ? 25.419  -24.094 -43.622  1.00 18.25 ? 93  LEU B CG  1 
ATOM   2433  C CD1 . LEU B 1 93  ? 26.147  -24.885 -44.697  1.00 18.61 ? 93  LEU B CD1 1 
ATOM   2434  C CD2 . LEU B 1 93  ? 23.971  -23.876 -44.000  1.00 17.76 ? 93  LEU B CD2 1 
ATOM   2435  N N   . GLY B 1 94  ? 24.029  -25.782 -39.857  1.00 21.31 ? 94  GLY B N   1 
ATOM   2436  C CA  . GLY B 1 94  ? 23.848  -26.821 -38.846  1.00 21.67 ? 94  GLY B CA  1 
ATOM   2437  C C   . GLY B 1 94  ? 22.464  -26.829 -38.224  1.00 22.00 ? 94  GLY B C   1 
ATOM   2438  O O   . GLY B 1 94  ? 22.055  -27.824 -37.615  1.00 24.22 ? 94  GLY B O   1 
ATOM   2439  N N   . THR B 1 95  ? 21.732  -25.730 -38.363  1.00 20.67 ? 95  THR B N   1 
ATOM   2440  C CA  . THR B 1 95  ? 20.417  -25.626 -37.749  1.00 20.18 ? 95  THR B CA  1 
ATOM   2441  C C   . THR B 1 95  ? 19.450  -26.626 -38.413  1.00 19.60 ? 95  THR B C   1 
ATOM   2442  O O   . THR B 1 95  ? 18.761  -27.368 -37.715  1.00 19.64 ? 95  THR B O   1 
ATOM   2443  C CB  . THR B 1 95  ? 19.906  -24.167 -37.808  1.00 20.10 ? 95  THR B CB  1 
ATOM   2444  O OG1 . THR B 1 95  ? 20.909  -23.304 -37.254  1.00 20.71 ? 95  THR B OG1 1 
ATOM   2445  C CG2 . THR B 1 95  ? 18.628  -23.999 -37.051  1.00 19.16 ? 95  THR B CG2 1 
ATOM   2446  N N   . ASN B 1 96  ? 19.440  -26.690 -39.748  1.00 19.13 ? 96  ASN B N   1 
ATOM   2447  C CA  . ASN B 1 96  ? 18.575  -27.649 -40.438  1.00 18.64 ? 96  ASN B CA  1 
ATOM   2448  C C   . ASN B 1 96  ? 19.011  -29.104 -40.254  1.00 18.90 ? 96  ASN B C   1 
ATOM   2449  O O   . ASN B 1 96  ? 18.200  -30.016 -40.341  1.00 18.55 ? 96  ASN B O   1 
ATOM   2450  C CB  . ASN B 1 96  ? 18.500  -27.332 -41.930  1.00 18.22 ? 96  ASN B CB  1 
ATOM   2451  C CG  . ASN B 1 96  ? 17.828  -26.013 -42.214  1.00 17.38 ? 96  ASN B CG  1 
ATOM   2452  O OD1 . ASN B 1 96  ? 16.649  -25.830 -41.944  1.00 17.21 ? 96  ASN B OD1 1 
ATOM   2453  N ND2 . ASN B 1 96  ? 18.572  -25.096 -42.774  1.00 17.47 ? 96  ASN B ND2 1 
ATOM   2454  N N   . ASP B 1 97  ? 20.294  -29.318 -39.994  1.00 19.59 ? 97  ASP B N   1 
ATOM   2455  C CA  . ASP B 1 97  ? 20.817  -30.669 -39.777  1.00 20.18 ? 97  ASP B CA  1 
ATOM   2456  C C   . ASP B 1 97  ? 20.224  -31.365 -38.538  1.00 19.51 ? 97  ASP B C   1 
ATOM   2457  O O   . ASP B 1 97  ? 20.296  -32.589 -38.417  1.00 19.48 ? 97  ASP B O   1 
ATOM   2458  C CB  . ASP B 1 97  ? 22.347  -30.645 -39.666  1.00 20.76 ? 97  ASP B CB  1 
ATOM   2459  C CG  . ASP B 1 97  ? 23.033  -30.178 -40.951  1.00 20.86 ? 97  ASP B CG  1 
ATOM   2460  O OD1 . ASP B 1 97  ? 22.881  -28.987 -41.310  1.00 20.26 ? 97  ASP B OD1 1 
ATOM   2461  O OD2 . ASP B 1 97  ? 23.740  -31.006 -41.592  1.00 21.10 ? 97  ASP B OD2 1 
ATOM   2462  N N   . THR B 1 98  ? 19.654  -30.585 -37.624  1.00 19.08 ? 98  THR B N   1 
ATOM   2463  C CA  . THR B 1 98  ? 19.035  -31.127 -36.414  1.00 18.75 ? 98  THR B CA  1 
ATOM   2464  C C   . THR B 1 98  ? 17.619  -31.666 -36.657  1.00 19.39 ? 98  THR B C   1 
ATOM   2465  O O   . THR B 1 98  ? 17.038  -32.314 -35.770  1.00 19.34 ? 98  THR B O   1 
ATOM   2466  C CB  . THR B 1 98  ? 18.957  -30.060 -35.306  1.00 17.88 ? 98  THR B CB  1 
ATOM   2467  O OG1 . THR B 1 98  ? 18.022  -29.038 -35.693  1.00 16.53 ? 98  THR B OG1 1 
ATOM   2468  C CG2 . THR B 1 98  ? 20.352  -29.453 -35.042  1.00 17.13 ? 98  THR B CG2 1 
ATOM   2469  N N   . LYS B 1 99  ? 17.070  -31.397 -37.847  1.00 19.53 ? 99  LYS B N   1 
ATOM   2470  C CA  . LYS B 1 99  ? 15.751  -31.915 -38.222  1.00 19.02 ? 99  LYS B CA  1 
ATOM   2471  C C   . LYS B 1 99  ? 15.688  -33.416 -38.020  1.00 18.00 ? 99  LYS B C   1 
ATOM   2472  O O   . LYS B 1 99  ? 16.557  -34.155 -38.455  1.00 17.14 ? 99  LYS B O   1 
ATOM   2473  C CB  . LYS B 1 99  ? 15.376  -31.558 -39.671  1.00 19.40 ? 99  LYS B CB  1 
ATOM   2474  C CG  . LYS B 1 99  ? 15.000  -30.091 -39.868  1.00 19.82 ? 99  LYS B CG  1 
ATOM   2475  C CD  . LYS B 1 99  ? 14.799  -29.703 -41.326  1.00 20.18 ? 99  LYS B CD  1 
ATOM   2476  C CE  . LYS B 1 99  ? 14.206  -28.309 -41.431  1.00 20.40 ? 99  LYS B CE  1 
ATOM   2477  N NZ  . LYS B 1 99  ? 14.360  -27.654 -42.752  1.00 20.04 ? 99  LYS B NZ  1 
ATOM   2478  N N   . THR B 1 100 ? 14.632  -33.829 -37.342  1.00 17.83 ? 100 THR B N   1 
ATOM   2479  C CA  . THR B 1 100 ? 14.402  -35.203 -36.912  1.00 17.55 ? 100 THR B CA  1 
ATOM   2480  C C   . THR B 1 100 ? 14.636  -36.228 -38.024  1.00 17.46 ? 100 THR B C   1 
ATOM   2481  O O   . THR B 1 100 ? 15.383  -37.181 -37.847  1.00 16.95 ? 100 THR B O   1 
ATOM   2482  C CB  . THR B 1 100 ? 12.959  -35.353 -36.365  1.00 17.47 ? 100 THR B CB  1 
ATOM   2483  O OG1 . THR B 1 100 ? 12.861  -34.793 -35.051  1.00 16.93 ? 100 THR B OG1 1 
ATOM   2484  C CG2 . THR B 1 100 ? 12.547  -36.829 -36.317  1.00 17.63 ? 100 THR B CG2 1 
ATOM   2485  N N   . TYR B 1 101 ? 13.990  -36.020 -39.170  1.00 17.46 ? 101 TYR B N   1 
ATOM   2486  C CA  . TYR B 1 101 ? 14.015  -36.983 -40.256  1.00 17.03 ? 101 TYR B CA  1 
ATOM   2487  C C   . TYR B 1 101 ? 15.399  -37.199 -40.907  1.00 17.62 ? 101 TYR B C   1 
ATOM   2488  O O   . TYR B 1 101 ? 15.595  -38.192 -41.586  1.00 18.44 ? 101 TYR B O   1 
ATOM   2489  C CB  . TYR B 1 101 ? 12.966  -36.645 -41.324  1.00 16.31 ? 101 TYR B CB  1 
ATOM   2490  C CG  . TYR B 1 101 ? 13.098  -35.300 -42.004  1.00 16.11 ? 101 TYR B CG  1 
ATOM   2491  C CD1 . TYR B 1 101 ? 14.006  -35.094 -43.038  1.00 16.16 ? 101 TYR B CD1 1 
ATOM   2492  C CD2 . TYR B 1 101 ? 12.280  -34.235 -41.643  1.00 16.28 ? 101 TYR B CD2 1 
ATOM   2493  C CE1 . TYR B 1 101 ? 14.100  -33.859 -43.690  1.00 15.87 ? 101 TYR B CE1 1 
ATOM   2494  C CE2 . TYR B 1 101 ? 12.372  -32.997 -42.273  1.00 15.77 ? 101 TYR B CE2 1 
ATOM   2495  C CZ  . TYR B 1 101 ? 13.274  -32.815 -43.288  1.00 15.59 ? 101 TYR B CZ  1 
ATOM   2496  O OH  . TYR B 1 101 ? 13.346  -31.596 -43.889  1.00 15.13 ? 101 TYR B OH  1 
ATOM   2497  N N   . LEU B 1 102 ? 16.349  -36.290 -40.709  1.00 17.57 ? 102 LEU B N   1 
ATOM   2498  C CA  . LEU B 1 102 ? 17.709  -36.484 -41.217  1.00 17.20 ? 102 LEU B CA  1 
ATOM   2499  C C   . LEU B 1 102 ? 18.532  -37.388 -40.302  1.00 17.07 ? 102 LEU B C   1 
ATOM   2500  O O   . LEU B 1 102 ? 19.603  -37.868 -40.685  1.00 16.88 ? 102 LEU B O   1 
ATOM   2501  C CB  . LEU B 1 102 ? 18.421  -35.150 -41.388  1.00 17.03 ? 102 LEU B CB  1 
ATOM   2502  C CG  . LEU B 1 102 ? 17.733  -34.154 -42.303  1.00 17.39 ? 102 LEU B CG  1 
ATOM   2503  C CD1 . LEU B 1 102 ? 18.402  -32.795 -42.221  1.00 17.67 ? 102 LEU B CD1 1 
ATOM   2504  C CD2 . LEU B 1 102 ? 17.727  -34.665 -43.729  1.00 17.52 ? 102 LEU B CD2 1 
ATOM   2505  N N   . ASN B 1 103 ? 18.047  -37.591 -39.078  1.00 16.34 ? 103 ASN B N   1 
ATOM   2506  C CA  . ASN B 1 103 ? 18.586  -38.622 -38.192  1.00 15.64 ? 103 ASN B CA  1 
ATOM   2507  C C   . ASN B 1 103 ? 20.094  -38.465 -37.912  1.00 14.87 ? 103 ASN B C   1 
ATOM   2508  O O   . ASN B 1 103 ? 20.848  -39.437 -37.911  1.00 14.77 ? 103 ASN B O   1 
ATOM   2509  C CB  . ASN B 1 103 ? 18.245  -39.995 -38.800  1.00 15.85 ? 103 ASN B CB  1 
ATOM   2510  C CG  . ASN B 1 103 ? 18.645  -41.150 -37.930  1.00 16.19 ? 103 ASN B CG  1 
ATOM   2511  O OD1 . ASN B 1 103 ? 18.194  -41.262 -36.804  1.00 17.18 ? 103 ASN B OD1 1 
ATOM   2512  N ND2 . ASN B 1 103 ? 19.484  -42.030 -38.454  1.00 16.45 ? 103 ASN B ND2 1 
ATOM   2513  N N   . ARG B 1 104 ? 20.528  -37.235 -37.656  1.00 14.52 ? 104 ARG B N   1 
ATOM   2514  C CA  . ARG B 1 104 ? 21.945  -36.957 -37.436  1.00 14.87 ? 104 ARG B CA  1 
ATOM   2515  C C   . ARG B 1 104 ? 22.308  -36.777 -35.971  1.00 14.91 ? 104 ARG B C   1 
ATOM   2516  O O   . ARG B 1 104 ? 21.545  -36.206 -35.212  1.00 15.59 ? 104 ARG B O   1 
ATOM   2517  C CB  . ARG B 1 104 ? 22.380  -35.699 -38.193  1.00 15.22 ? 104 ARG B CB  1 
ATOM   2518  C CG  . ARG B 1 104 ? 21.776  -35.523 -39.567  1.00 14.93 ? 104 ARG B CG  1 
ATOM   2519  C CD  . ARG B 1 104 ? 22.647  -34.650 -40.450  1.00 14.68 ? 104 ARG B CD  1 
ATOM   2520  N NE  . ARG B 1 104 ? 23.719  -35.412 -41.080  1.00 14.37 ? 104 ARG B NE  1 
ATOM   2521  C CZ  . ARG B 1 104 ? 24.682  -34.877 -41.834  1.00 14.52 ? 104 ARG B CZ  1 
ATOM   2522  N NH1 . ARG B 1 104 ? 24.737  -33.566 -42.074  1.00 14.84 ? 104 ARG B NH1 1 
ATOM   2523  N NH2 . ARG B 1 104 ? 25.609  -35.657 -42.350  1.00 14.61 ? 104 ARG B NH2 1 
ATOM   2524  N N   . THR B 1 105 ? 23.483  -37.241 -35.593  1.00 15.04 ? 105 THR B N   1 
ATOM   2525  C CA  . THR B 1 105 ? 24.064  -36.940 -34.295  1.00 14.84 ? 105 THR B CA  1 
ATOM   2526  C C   . THR B 1 105 ? 24.854  -35.648 -34.450  1.00 14.86 ? 105 THR B C   1 
ATOM   2527  O O   . THR B 1 105 ? 25.173  -35.257 -35.565  1.00 14.51 ? 105 THR B O   1 
ATOM   2528  C CB  . THR B 1 105 ? 25.038  -38.042 -33.850  1.00 14.91 ? 105 THR B CB  1 
ATOM   2529  O OG1 . THR B 1 105 ? 26.196  -38.025 -34.706  1.00 14.86 ? 105 THR B OG1 1 
ATOM   2530  C CG2 . THR B 1 105 ? 24.356  -39.390 -33.885  1.00 14.80 ? 105 THR B CG2 1 
ATOM   2531  N N   . PRO B 1 106 ? 25.188  -34.987 -33.336  1.00 15.20 ? 106 PRO B N   1 
ATOM   2532  C CA  . PRO B 1 106 ? 26.031  -33.787 -33.389  1.00 15.07 ? 106 PRO B CA  1 
ATOM   2533  C C   . PRO B 1 106 ? 27.389  -34.026 -34.026  1.00 14.81 ? 106 PRO B C   1 
ATOM   2534  O O   . PRO B 1 106 ? 27.857  -33.189 -34.787  1.00 15.10 ? 106 PRO B O   1 
ATOM   2535  C CB  . PRO B 1 106 ? 26.215  -33.421 -31.912  1.00 15.34 ? 106 PRO B CB  1 
ATOM   2536  C CG  . PRO B 1 106 ? 24.989  -33.951 -31.249  1.00 15.66 ? 106 PRO B CG  1 
ATOM   2537  C CD  . PRO B 1 106 ? 24.650  -35.213 -31.981  1.00 15.73 ? 106 PRO B CD  1 
ATOM   2538  N N   . PHE B 1 107 ? 28.021  -35.164 -33.716  1.00 14.43 ? 107 PHE B N   1 
ATOM   2539  C CA  . PHE B 1 107 ? 29.306  -35.522 -34.315  1.00 13.66 ? 107 PHE B CA  1 
ATOM   2540  C C   . PHE B 1 107 ? 29.159  -35.656 -35.829  1.00 13.50 ? 107 PHE B C   1 
ATOM   2541  O O   . PHE B 1 107 ? 30.013  -35.205 -36.585  1.00 12.74 ? 107 PHE B O   1 
ATOM   2542  C CB  . PHE B 1 107 ? 29.852  -36.807 -33.697  1.00 13.74 ? 107 PHE B CB  1 
ATOM   2543  C CG  . PHE B 1 107 ? 31.133  -37.280 -34.321  1.00 13.95 ? 107 PHE B CG  1 
ATOM   2544  C CD1 . PHE B 1 107 ? 32.292  -36.536 -34.202  1.00 14.45 ? 107 PHE B CD1 1 
ATOM   2545  C CD2 . PHE B 1 107 ? 31.180  -38.470 -35.032  1.00 14.03 ? 107 PHE B CD2 1 
ATOM   2546  C CE1 . PHE B 1 107 ? 33.479  -36.976 -34.787  1.00 15.05 ? 107 PHE B CE1 1 
ATOM   2547  C CE2 . PHE B 1 107 ? 32.341  -38.903 -35.635  1.00 14.29 ? 107 PHE B CE2 1 
ATOM   2548  C CZ  . PHE B 1 107 ? 33.495  -38.164 -35.520  1.00 14.80 ? 107 PHE B CZ  1 
ATOM   2549  N N   . GLU B 1 108 ? 28.062  -36.267 -36.273  1.00 13.54 ? 108 GLU B N   1 
ATOM   2550  C CA  . GLU B 1 108 ? 27.796  -36.386 -37.692  1.00 13.69 ? 108 GLU B CA  1 
ATOM   2551  C C   . GLU B 1 108 ? 27.704  -35.020 -38.347  1.00 13.82 ? 108 GLU B C   1 
ATOM   2552  O O   . GLU B 1 108 ? 28.181  -34.820 -39.465  1.00 14.08 ? 108 GLU B O   1 
ATOM   2553  C CB  . GLU B 1 108 ? 26.504  -37.148 -37.935  1.00 13.67 ? 108 GLU B CB  1 
ATOM   2554  C CG  . GLU B 1 108 ? 26.270  -37.431 -39.416  1.00 13.77 ? 108 GLU B CG  1 
ATOM   2555  C CD  . GLU B 1 108 ? 25.075  -38.323 -39.635  1.00 14.07 ? 108 GLU B CD  1 
ATOM   2556  O OE1 . GLU B 1 108 ? 24.175  -37.945 -40.417  1.00 13.43 ? 108 GLU B OE1 1 
ATOM   2557  O OE2 . GLU B 1 108 ? 24.981  -39.371 -38.934  1.00 14.74 ? 108 GLU B OE2 1 
ATOM   2558  N N   . ILE B 1 109 ? 27.076  -34.080 -37.656  1.00 14.22 ? 109 ILE B N   1 
ATOM   2559  C CA  . ILE B 1 109 ? 26.874  -32.736 -38.193  1.00 14.70 ? 109 ILE B CA  1 
ATOM   2560  C C   . ILE B 1 109 ? 28.215  -32.016 -38.259  1.00 15.01 ? 109 ILE B C   1 
ATOM   2561  O O   . ILE B 1 109 ? 28.501  -31.311 -39.218  1.00 14.22 ? 109 ILE B O   1 
ATOM   2562  C CB  . ILE B 1 109 ? 25.833  -31.947 -37.380  1.00 14.94 ? 109 ILE B CB  1 
ATOM   2563  C CG1 . ILE B 1 109 ? 24.472  -32.686 -37.394  1.00 15.48 ? 109 ILE B CG1 1 
ATOM   2564  C CG2 . ILE B 1 109 ? 25.662  -30.556 -37.959  1.00 14.73 ? 109 ILE B CG2 1 
ATOM   2565  C CD1 . ILE B 1 109 ? 23.467  -32.214 -36.358  1.00 15.54 ? 109 ILE B CD1 1 
ATOM   2566  N N   . GLY B 1 110 ? 29.046  -32.217 -37.246  1.00 16.16 ? 110 GLY B N   1 
ATOM   2567  C CA  . GLY B 1 110 ? 30.422  -31.744 -37.290  1.00 17.00 ? 110 GLY B CA  1 
ATOM   2568  C C   . GLY B 1 110 ? 31.186  -32.247 -38.509  1.00 17.52 ? 110 GLY B C   1 
ATOM   2569  O O   . GLY B 1 110 ? 31.855  -31.467 -39.193  1.00 17.32 ? 110 GLY B O   1 
ATOM   2570  N N   . LEU B 1 111 ? 31.092  -33.557 -38.776  1.00 17.81 ? 111 LEU B N   1 
ATOM   2571  C CA  . LEU B 1 111 ? 31.718  -34.153 -39.953  1.00 17.80 ? 111 LEU B CA  1 
ATOM   2572  C C   . LEU B 1 111 ? 31.236  -33.469 -41.235  1.00 18.21 ? 111 LEU B C   1 
ATOM   2573  O O   . LEU B 1 111 ? 32.015  -33.274 -42.184  1.00 19.06 ? 111 LEU B O   1 
ATOM   2574  C CB  . LEU B 1 111 ? 31.424  -35.646 -40.024  1.00 17.82 ? 111 LEU B CB  1 
ATOM   2575  C CG  . LEU B 1 111 ? 32.078  -36.523 -38.969  1.00 18.11 ? 111 LEU B CG  1 
ATOM   2576  C CD1 . LEU B 1 111 ? 31.610  -37.958 -39.048  1.00 17.77 ? 111 LEU B CD1 1 
ATOM   2577  C CD2 . LEU B 1 111 ? 33.577  -36.481 -39.139  1.00 18.40 ? 111 LEU B CD2 1 
ATOM   2578  N N   . GLY B 1 112 ? 29.946  -33.113 -41.257  1.00 17.98 ? 112 GLY B N   1 
ATOM   2579  C CA  . GLY B 1 112 ? 29.349  -32.437 -42.399  1.00 17.54 ? 112 GLY B CA  1 
ATOM   2580  C C   . GLY B 1 112 ? 29.970  -31.081 -42.604  1.00 17.52 ? 112 GLY B C   1 
ATOM   2581  O O   . GLY B 1 112 ? 30.339  -30.729 -43.723  1.00 17.46 ? 112 GLY B O   1 
ATOM   2582  N N   . ALA B 1 113 ? 30.089  -30.320 -41.521  1.00 17.90 ? 113 ALA B N   1 
ATOM   2583  C CA  . ALA B 1 113 ? 30.763  -29.028 -41.563  1.00 18.50 ? 113 ALA B CA  1 
ATOM   2584  C C   . ALA B 1 113 ? 32.207  -29.231 -41.989  1.00 19.28 ? 113 ALA B C   1 
ATOM   2585  O O   . ALA B 1 113 ? 32.722  -28.455 -42.787  1.00 20.97 ? 113 ALA B O   1 
ATOM   2586  C CB  . ALA B 1 113 ? 30.705  -28.345 -40.213  1.00 18.27 ? 113 ALA B CB  1 
ATOM   2587  N N   . GLY B 1 114 ? 32.841  -30.282 -41.474  1.00 19.47 ? 114 GLY B N   1 
ATOM   2588  C CA  . GLY B 1 114 ? 34.188  -30.668 -41.903  1.00 19.67 ? 114 GLY B CA  1 
ATOM   2589  C C   . GLY B 1 114 ? 34.325  -30.928 -43.402  1.00 19.67 ? 114 GLY B C   1 
ATOM   2590  O O   . GLY B 1 114 ? 35.292  -30.499 -44.038  1.00 19.45 ? 114 GLY B O   1 
ATOM   2591  N N   . ALA B 1 115 ? 33.344  -31.626 -43.966  1.00 19.31 ? 115 ALA B N   1 
ATOM   2592  C CA  . ALA B 1 115 ? 33.302  -31.861 -45.408  1.00 18.87 ? 115 ALA B CA  1 
ATOM   2593  C C   . ALA B 1 115 ? 33.330  -30.553 -46.181  1.00 18.71 ? 115 ALA B C   1 
ATOM   2594  O O   . ALA B 1 115 ? 33.964  -30.463 -47.234  1.00 18.12 ? 115 ALA B O   1 
ATOM   2595  C CB  . ALA B 1 115 ? 32.064  -32.654 -45.781  1.00 18.82 ? 115 ALA B CB  1 
ATOM   2596  N N   . LEU B 1 116 ? 32.632  -29.546 -45.664  1.00 18.84 ? 116 LEU B N   1 
ATOM   2597  C CA  . LEU B 1 116 ? 32.599  -28.238 -46.313  1.00 18.94 ? 116 LEU B CA  1 
ATOM   2598  C C   . LEU B 1 116 ? 33.942  -27.525 -46.188  1.00 18.04 ? 116 LEU B C   1 
ATOM   2599  O O   . LEU B 1 116 ? 34.437  -26.958 -47.171  1.00 17.56 ? 116 LEU B O   1 
ATOM   2600  C CB  . LEU B 1 116 ? 31.456  -27.381 -45.771  1.00 19.20 ? 116 LEU B CB  1 
ATOM   2601  C CG  . LEU B 1 116 ? 30.037  -27.923 -46.012  1.00 19.65 ? 116 LEU B CG  1 
ATOM   2602  C CD1 . LEU B 1 116 ? 28.997  -26.969 -45.427  1.00 19.71 ? 116 LEU B CD1 1 
ATOM   2603  C CD2 . LEU B 1 116 ? 29.760  -28.144 -47.500  1.00 19.34 ? 116 LEU B CD2 1 
ATOM   2604  N N   . ILE B 1 117 ? 34.544  -27.578 -45.002  1.00 17.19 ? 117 ILE B N   1 
ATOM   2605  C CA  . ILE B 1 117 ? 35.868  -26.985 -44.800  1.00 16.91 ? 117 ILE B CA  1 
ATOM   2606  C C   . ILE B 1 117 ? 36.865  -27.596 -45.801  1.00 17.25 ? 117 ILE B C   1 
ATOM   2607  O O   . ILE B 1 117 ? 37.646  -26.884 -46.449  1.00 16.25 ? 117 ILE B O   1 
ATOM   2608  C CB  . ILE B 1 117 ? 36.396  -27.196 -43.363  1.00 16.35 ? 117 ILE B CB  1 
ATOM   2609  C CG1 . ILE B 1 117 ? 35.583  -26.415 -42.345  1.00 16.00 ? 117 ILE B CG1 1 
ATOM   2610  C CG2 . ILE B 1 117 ? 37.850  -26.762 -43.264  1.00 16.43 ? 117 ILE B CG2 1 
ATOM   2611  C CD1 . ILE B 1 117 ? 35.766  -26.906 -40.919  1.00 15.78 ? 117 ILE B CD1 1 
ATOM   2612  N N   . ASN B 1 118 ? 36.821  -28.922 -45.916  1.00 17.66 ? 118 ASN B N   1 
ATOM   2613  C CA  . ASN B 1 118 ? 37.659  -29.631 -46.867  1.00 17.49 ? 118 ASN B CA  1 
ATOM   2614  C C   . ASN B 1 118 ? 37.448  -29.180 -48.317  1.00 17.94 ? 118 ASN B C   1 
ATOM   2615  O O   . ASN B 1 118 ? 38.406  -29.025 -49.064  1.00 18.91 ? 118 ASN B O   1 
ATOM   2616  C CB  . ASN B 1 118 ? 37.437  -31.139 -46.748  1.00 16.69 ? 118 ASN B CB  1 
ATOM   2617  C CG  . ASN B 1 118 ? 38.452  -31.923 -47.513  1.00 16.26 ? 118 ASN B CG  1 
ATOM   2618  O OD1 . ASN B 1 118 ? 39.646  -31.599 -47.533  1.00 17.54 ? 118 ASN B OD1 1 
ATOM   2619  N ND2 . ASN B 1 118 ? 38.008  -32.956 -48.135  1.00 15.60 ? 118 ASN B ND2 1 
ATOM   2620  N N   . MET B 1 119 ? 36.204  -28.960 -48.715  1.00 18.23 ? 119 MET B N   1 
ATOM   2621  C CA  . MET B 1 119 ? 35.929  -28.435 -50.064  1.00 18.30 ? 119 MET B CA  1 
ATOM   2622  C C   . MET B 1 119 ? 36.594  -27.081 -50.293  1.00 17.76 ? 119 MET B C   1 
ATOM   2623  O O   . MET B 1 119 ? 37.118  -26.820 -51.379  1.00 17.66 ? 119 MET B O   1 
ATOM   2624  C CB  . MET B 1 119 ? 34.421  -28.344 -50.324  1.00 18.58 ? 119 MET B CB  1 
ATOM   2625  C CG  . MET B 1 119 ? 33.807  -29.702 -50.595  1.00 19.18 ? 119 MET B CG  1 
ATOM   2626  S SD  . MET B 1 119 ? 32.023  -29.676 -50.551  1.00 19.35 ? 119 MET B SD  1 
ATOM   2627  C CE  . MET B 1 119 ? 31.660  -31.161 -51.491  1.00 18.90 ? 119 MET B CE  1 
ATOM   2628  N N   . VAL B 1 120 ? 36.578  -26.234 -49.266  1.00 17.35 ? 120 VAL B N   1 
ATOM   2629  C CA  . VAL B 1 120 ? 37.230  -24.933 -49.339  1.00 17.31 ? 120 VAL B CA  1 
ATOM   2630  C C   . VAL B 1 120 ? 38.751  -25.097 -49.433  1.00 17.09 ? 120 VAL B C   1 
ATOM   2631  O O   . VAL B 1 120 ? 39.404  -24.369 -50.161  1.00 16.89 ? 120 VAL B O   1 
ATOM   2632  C CB  . VAL B 1 120 ? 36.891  -24.043 -48.115  1.00 17.60 ? 120 VAL B CB  1 
ATOM   2633  C CG1 . VAL B 1 120 ? 37.640  -22.713 -48.183  1.00 17.45 ? 120 VAL B CG1 1 
ATOM   2634  C CG2 . VAL B 1 120 ? 35.380  -23.821 -48.006  1.00 17.43 ? 120 VAL B CG2 1 
ATOM   2635  N N   . GLN B 1 121 ? 39.312  -26.046 -48.691  1.00 16.93 ? 121 GLN B N   1 
ATOM   2636  C CA  . GLN B 1 121 ? 40.768  -26.254 -48.683  1.00 16.95 ? 121 GLN B CA  1 
ATOM   2637  C C   . GLN B 1 121 ? 41.291  -26.809 -49.999  1.00 16.82 ? 121 GLN B C   1 
ATOM   2638  O O   . GLN B 1 121 ? 42.409  -26.513 -50.396  1.00 17.19 ? 121 GLN B O   1 
ATOM   2639  C CB  . GLN B 1 121 ? 41.181  -27.153 -47.519  1.00 16.76 ? 121 GLN B CB  1 
ATOM   2640  C CG  . GLN B 1 121 ? 41.050  -26.458 -46.180  1.00 16.66 ? 121 GLN B CG  1 
ATOM   2641  C CD  . GLN B 1 121 ? 41.509  -27.323 -45.035  1.00 16.95 ? 121 GLN B CD  1 
ATOM   2642  O OE1 . GLN B 1 121 ? 41.762  -28.516 -45.210  1.00 17.65 ? 121 GLN B OE1 1 
ATOM   2643  N NE2 . GLN B 1 121 ? 41.626  -26.730 -43.849  1.00 17.08 ? 121 GLN B NE2 1 
ATOM   2644  N N   . LYS B 1 122 ? 40.471  -27.604 -50.673  1.00 17.05 ? 122 LYS B N   1 
ATOM   2645  C CA  . LYS B 1 122 ? 40.794  -28.126 -51.991  1.00 17.69 ? 122 LYS B CA  1 
ATOM   2646  C C   . LYS B 1 122 ? 40.225  -27.233 -53.108  1.00 19.83 ? 122 LYS B C   1 
ATOM   2647  O O   . LYS B 1 122 ? 40.156  -27.641 -54.261  1.00 19.96 ? 122 LYS B O   1 
ATOM   2648  C CB  . LYS B 1 122 ? 40.230  -29.537 -52.116  1.00 16.64 ? 122 LYS B CB  1 
ATOM   2649  C CG  . LYS B 1 122 ? 40.704  -30.483 -51.019  1.00 15.73 ? 122 LYS B CG  1 
ATOM   2650  C CD  . LYS B 1 122 ? 40.072  -31.837 -51.073  1.00 15.24 ? 122 LYS B CD  1 
ATOM   2651  C CE  . LYS B 1 122 ? 40.682  -32.705 -52.139  1.00 15.15 ? 122 LYS B CE  1 
ATOM   2652  N NZ  . LYS B 1 122 ? 40.053  -34.054 -52.142  1.00 14.94 ? 122 LYS B NZ  1 
ATOM   2653  N N   . SER B 1 123 ? 39.829  -26.013 -52.750  1.00 23.37 ? 123 SER B N   1 
ATOM   2654  C CA  . SER B 1 123 ? 39.097  -25.098 -53.627  1.00 25.10 ? 123 SER B CA  1 
ATOM   2655  C C   . SER B 1 123 ? 39.905  -24.688 -54.844  1.00 26.67 ? 123 SER B C   1 
ATOM   2656  O O   . SER B 1 123 ? 41.129  -24.600 -54.756  1.00 27.04 ? 123 SER B O   1 
ATOM   2657  C CB  . SER B 1 123 ? 38.695  -23.852 -52.861  1.00 25.99 ? 123 SER B CB  1 
ATOM   2658  O OG  . SER B 1 123 ? 37.462  -23.397 -53.332  1.00 28.31 ? 123 SER B OG  1 
ATOM   2659  N N   . PRO B 1 124 ? 39.207  -24.196 -55.885  1.00 28.82 ? 124 PRO B N   1 
ATOM   2660  C CA  . PRO B 1 124 ? 38.980  -24.671 -57.258  1.00 28.92 ? 124 PRO B CA  1 
ATOM   2661  C C   . PRO B 1 124 ? 39.671  -25.979 -57.470  1.00 29.33 ? 124 PRO B C   1 
ATOM   2662  O O   . PRO B 1 124 ? 40.769  -26.175 -56.979  1.00 32.20 ? 124 PRO B O   1 
ATOM   2663  C CB  . PRO B 1 124 ? 39.628  -23.568 -58.129  1.00 29.08 ? 124 PRO B CB  1 
ATOM   2664  C CG  . PRO B 1 124 ? 40.572  -22.882 -57.213  1.00 27.82 ? 124 PRO B CG  1 
ATOM   2665  C CD  . PRO B 1 124 ? 39.726  -22.814 -55.968  1.00 29.30 ? 124 PRO B CD  1 
ATOM   2666  N N   . GLY B 1 125 ? 39.097  -26.891 -58.210  1.00 29.97 ? 125 GLY B N   1 
ATOM   2667  C CA  . GLY B 1 125 ? 39.865  -28.114 -58.474  1.00 30.14 ? 125 GLY B CA  1 
ATOM   2668  C C   . GLY B 1 125 ? 40.682  -28.024 -59.746  1.00 29.21 ? 125 GLY B C   1 
ATOM   2669  O O   . GLY B 1 125 ? 40.687  -28.993 -60.501  1.00 28.51 ? 125 GLY B O   1 
ATOM   2670  N N   . TRP B 1 126 ? 41.372  -26.907 -60.004  1.00 29.09 ? 126 TRP B N   1 
ATOM   2671  C CA  . TRP B 1 126 ? 41.912  -26.711 -61.355  1.00 29.75 ? 126 TRP B CA  1 
ATOM   2672  C C   . TRP B 1 126 ? 43.144  -25.826 -61.587  1.00 31.84 ? 126 TRP B C   1 
ATOM   2673  O O   . TRP B 1 126 ? 43.523  -25.001 -60.766  1.00 32.94 ? 126 TRP B O   1 
ATOM   2674  C CB  . TRP B 1 126 ? 40.784  -26.257 -62.299  1.00 28.40 ? 126 TRP B CB  1 
ATOM   2675  C CG  . TRP B 1 126 ? 40.143  -24.913 -61.984  1.00 27.62 ? 126 TRP B CG  1 
ATOM   2676  C CD1 . TRP B 1 126 ? 40.761  -23.770 -61.517  1.00 26.84 ? 126 TRP B CD1 1 
ATOM   2677  C CD2 . TRP B 1 126 ? 38.772  -24.558 -62.186  1.00 27.04 ? 126 TRP B CD2 1 
ATOM   2678  N NE1 . TRP B 1 126 ? 39.854  -22.757 -61.381  1.00 25.96 ? 126 TRP B NE1 1 
ATOM   2679  C CE2 . TRP B 1 126 ? 38.623  -23.214 -61.774  1.00 26.35 ? 126 TRP B CE2 1 
ATOM   2680  C CE3 . TRP B 1 126 ? 37.646  -25.255 -62.649  1.00 27.15 ? 126 TRP B CE3 1 
ATOM   2681  C CZ2 . TRP B 1 126 ? 37.401  -22.549 -61.831  1.00 27.39 ? 126 TRP B CZ2 1 
ATOM   2682  C CZ3 . TRP B 1 126 ? 36.427  -24.600 -62.692  1.00 27.26 ? 126 TRP B CZ3 1 
ATOM   2683  C CH2 . TRP B 1 126 ? 36.314  -23.257 -62.286  1.00 27.51 ? 126 TRP B CH2 1 
ATOM   2684  N N   . ASP B 1 127 ? 43.758  -26.042 -62.750  1.00 35.01 ? 127 ASP B N   1 
ATOM   2685  C CA  . ASP B 1 127 ? 44.858  -25.230 -63.268  1.00 36.70 ? 127 ASP B CA  1 
ATOM   2686  C C   . ASP B 1 127 ? 44.421  -23.941 -63.955  1.00 33.29 ? 127 ASP B C   1 
ATOM   2687  O O   . ASP B 1 127 ? 45.280  -23.160 -64.355  1.00 37.88 ? 127 ASP B O   1 
ATOM   2688  C CB  . ASP B 1 127 ? 45.697  -26.080 -64.260  1.00 42.73 ? 127 ASP B CB  1 
ATOM   2689  C CG  . ASP B 1 127 ? 46.443  -27.242 -63.563  1.00 49.46 ? 127 ASP B CG  1 
ATOM   2690  O OD1 . ASP B 1 127 ? 46.766  -27.135 -62.338  1.00 50.23 ? 127 ASP B OD1 1 
ATOM   2691  O OD2 . ASP B 1 127 ? 46.759  -28.265 -64.252  1.00 54.29 ? 127 ASP B OD2 1 
ATOM   2692  N N   . TRP B 1 128 ? 43.117  -23.695 -64.102  1.00 29.05 ? 128 TRP B N   1 
ATOM   2693  C CA  . TRP B 1 128 ? 42.631  -22.512 -64.842  1.00 26.03 ? 128 TRP B CA  1 
ATOM   2694  C C   . TRP B 1 128 ? 42.992  -21.193 -64.176  1.00 25.10 ? 128 TRP B C   1 
ATOM   2695  O O   . TRP B 1 128 ? 43.151  -20.177 -64.838  1.00 22.22 ? 128 TRP B O   1 
ATOM   2696  C CB  . TRP B 1 128 ? 41.118  -22.595 -65.058  1.00 24.60 ? 128 TRP B CB  1 
ATOM   2697  C CG  . TRP B 1 128 ? 40.676  -23.759 -65.921  1.00 23.10 ? 128 TRP B CG  1 
ATOM   2698  C CD1 . TRP B 1 128 ? 41.477  -24.552 -66.659  1.00 22.57 ? 128 TRP B CD1 1 
ATOM   2699  C CD2 . TRP B 1 128 ? 39.326  -24.192 -66.187  1.00 22.03 ? 128 TRP B CD2 1 
ATOM   2700  N NE1 . TRP B 1 128 ? 40.727  -25.462 -67.362  1.00 22.33 ? 128 TRP B NE1 1 
ATOM   2701  C CE2 . TRP B 1 128 ? 39.403  -25.254 -67.098  1.00 21.74 ? 128 TRP B CE2 1 
ATOM   2702  C CE3 . TRP B 1 128 ? 38.067  -23.763 -65.765  1.00 22.09 ? 128 TRP B CE3 1 
ATOM   2703  C CZ2 . TRP B 1 128 ? 38.269  -25.931 -67.573  1.00 21.71 ? 128 TRP B CZ2 1 
ATOM   2704  C CZ3 . TRP B 1 128 ? 36.938  -24.449 -66.224  1.00 22.03 ? 128 TRP B CZ3 1 
ATOM   2705  C CH2 . TRP B 1 128 ? 37.054  -25.513 -67.131  1.00 21.30 ? 128 TRP B CH2 1 
ATOM   2706  N N   . THR B 1 129 ? 43.093  -21.226 -62.853  1.00 26.97 ? 129 THR B N   1 
ATOM   2707  C CA  . THR B 1 129 ? 43.569  -20.105 -62.047  1.00 28.18 ? 129 THR B CA  1 
ATOM   2708  C C   . THR B 1 129 ? 44.602  -20.693 -61.102  1.00 29.11 ? 129 THR B C   1 
ATOM   2709  O O   . THR B 1 129 ? 44.582  -21.894 -60.858  1.00 32.83 ? 129 THR B O   1 
ATOM   2710  C CB  . THR B 1 129 ? 42.421  -19.478 -61.211  1.00 27.58 ? 129 THR B CB  1 
ATOM   2711  O OG1 . THR B 1 129 ? 41.861  -20.440 -60.297  1.00 27.10 ? 129 THR B OG1 1 
ATOM   2712  C CG2 . THR B 1 129 ? 41.328  -18.930 -62.123  1.00 27.05 ? 129 THR B CG2 1 
ATOM   2713  N N   . ASP B 1 130 ? 45.504  -19.886 -60.565  1.00 29.82 ? 130 ASP B N   1 
ATOM   2714  C CA  . ASP B 1 130 ? 46.104  -20.288 -59.291  1.00 31.29 ? 130 ASP B CA  1 
ATOM   2715  C C   . ASP B 1 130 ? 46.222  -19.158 -58.295  1.00 28.45 ? 130 ASP B C   1 
ATOM   2716  O O   . ASP B 1 130 ? 47.239  -18.505 -58.166  1.00 27.05 ? 130 ASP B O   1 
ATOM   2717  C CB  . ASP B 1 130 ? 47.339  -21.233 -59.372  1.00 34.54 ? 130 ASP B CB  1 
ATOM   2718  C CG  . ASP B 1 130 ? 48.427  -20.758 -60.299  1.00 37.19 ? 130 ASP B CG  1 
ATOM   2719  O OD1 . ASP B 1 130 ? 49.011  -19.676 -60.101  1.00 36.84 ? 130 ASP B OD1 1 
ATOM   2720  O OD2 . ASP B 1 130 ? 48.737  -21.531 -61.234  1.00 41.88 ? 130 ASP B OD2 1 
ATOM   2721  N N   . TYR B 1 131 ? 45.088  -18.929 -57.633  1.00 27.02 ? 131 TYR B N   1 
ATOM   2722  C CA  . TYR B 1 131 ? 45.033  -18.228 -56.372  1.00 24.19 ? 131 TYR B CA  1 
ATOM   2723  C C   . TYR B 1 131 ? 45.088  -19.288 -55.273  1.00 23.24 ? 131 TYR B C   1 
ATOM   2724  O O   . TYR B 1 131 ? 44.710  -20.431 -55.487  1.00 22.16 ? 131 TYR B O   1 
ATOM   2725  C CB  . TYR B 1 131 ? 43.735  -17.469 -56.253  1.00 23.03 ? 131 TYR B CB  1 
ATOM   2726  C CG  . TYR B 1 131 ? 43.455  -16.441 -57.336  1.00 22.57 ? 131 TYR B CG  1 
ATOM   2727  C CD1 . TYR B 1 131 ? 43.913  -15.141 -57.208  1.00 22.03 ? 131 TYR B CD1 1 
ATOM   2728  C CD2 . TYR B 1 131 ? 42.671  -16.749 -58.445  1.00 22.59 ? 131 TYR B CD2 1 
ATOM   2729  C CE1 . TYR B 1 131 ? 43.633  -14.178 -58.164  1.00 21.79 ? 131 TYR B CE1 1 
ATOM   2730  C CE2 . TYR B 1 131 ? 42.379  -15.799 -59.410  1.00 22.58 ? 131 TYR B CE2 1 
ATOM   2731  C CZ  . TYR B 1 131 ? 42.870  -14.504 -59.258  1.00 22.43 ? 131 TYR B CZ  1 
ATOM   2732  O OH  . TYR B 1 131 ? 42.594  -13.496 -60.157  1.00 22.02 ? 131 TYR B OH  1 
ATOM   2733  N N   . PRO B 1 132 ? 45.586  -18.923 -54.092  1.00 23.59 ? 132 PRO B N   1 
ATOM   2734  C CA  . PRO B 1 132 ? 45.539  -19.889 -52.997  1.00 23.29 ? 132 PRO B CA  1 
ATOM   2735  C C   . PRO B 1 132 ? 44.098  -20.135 -52.524  1.00 22.20 ? 132 PRO B C   1 
ATOM   2736  O O   . PRO B 1 132 ? 43.202  -19.361 -52.856  1.00 22.98 ? 132 PRO B O   1 
ATOM   2737  C CB  . PRO B 1 132 ? 46.328  -19.193 -51.887  1.00 23.73 ? 132 PRO B CB  1 
ATOM   2738  C CG  . PRO B 1 132 ? 46.174  -17.743 -52.179  1.00 24.18 ? 132 PRO B CG  1 
ATOM   2739  C CD  . PRO B 1 132 ? 46.151  -17.630 -53.669  1.00 24.11 ? 132 PRO B CD  1 
ATOM   2740  N N   . PRO B 1 133 ? 43.872  -21.204 -51.752  1.00 20.33 ? 133 PRO B N   1 
ATOM   2741  C CA  . PRO B 1 133 ? 42.557  -21.357 -51.160  1.00 20.30 ? 133 PRO B CA  1 
ATOM   2742  C C   . PRO B 1 133 ? 42.406  -20.455 -49.925  1.00 20.55 ? 133 PRO B C   1 
ATOM   2743  O O   . PRO B 1 133 ? 43.389  -20.176 -49.240  1.00 21.50 ? 133 PRO B O   1 
ATOM   2744  C CB  . PRO B 1 133 ? 42.516  -22.843 -50.782  1.00 20.07 ? 133 PRO B CB  1 
ATOM   2745  C CG  . PRO B 1 133 ? 43.929  -23.305 -50.746  1.00 19.89 ? 133 PRO B CG  1 
ATOM   2746  C CD  . PRO B 1 133 ? 44.809  -22.230 -51.281  1.00 19.80 ? 133 PRO B CD  1 
ATOM   2747  N N   . PRO B 1 134 ? 41.188  -19.994 -49.634  1.00 20.91 ? 134 PRO B N   1 
ATOM   2748  C CA  . PRO B 1 134 ? 41.046  -19.089 -48.505  1.00 21.59 ? 134 PRO B CA  1 
ATOM   2749  C C   . PRO B 1 134 ? 40.918  -19.818 -47.166  1.00 22.77 ? 134 PRO B C   1 
ATOM   2750  O O   . PRO B 1 134 ? 40.492  -20.958 -47.137  1.00 23.50 ? 134 PRO B O   1 
ATOM   2751  C CB  . PRO B 1 134 ? 39.739  -18.346 -48.829  1.00 21.10 ? 134 PRO B CB  1 
ATOM   2752  C CG  . PRO B 1 134 ? 39.021  -19.162 -49.837  1.00 20.73 ? 134 PRO B CG  1 
ATOM   2753  C CD  . PRO B 1 134 ? 39.883  -20.323 -50.227  1.00 20.83 ? 134 PRO B CD  1 
ATOM   2754  N N   . PRO B 1 135 ? 41.252  -19.150 -46.057  1.00 24.22 ? 135 PRO B N   1 
ATOM   2755  C CA  . PRO B 1 135 ? 40.949  -19.698 -44.733  1.00 24.56 ? 135 PRO B CA  1 
ATOM   2756  C C   . PRO B 1 135 ? 39.430  -19.785 -44.478  1.00 25.61 ? 135 PRO B C   1 
ATOM   2757  O O   . PRO B 1 135 ? 38.642  -19.209 -45.235  1.00 24.36 ? 135 PRO B O   1 
ATOM   2758  C CB  . PRO B 1 135 ? 41.586  -18.682 -43.773  1.00 24.31 ? 135 PRO B CB  1 
ATOM   2759  C CG  . PRO B 1 135 ? 41.566  -17.411 -44.528  1.00 24.79 ? 135 PRO B CG  1 
ATOM   2760  C CD  . PRO B 1 135 ? 41.842  -17.801 -45.953  1.00 24.95 ? 135 PRO B CD  1 
ATOM   2761  N N   . VAL B 1 136 ? 39.038  -20.494 -43.417  1.00 25.54 ? 136 VAL B N   1 
ATOM   2762  C CA  . VAL B 1 136 ? 37.634  -20.700 -43.102  1.00 25.29 ? 136 VAL B CA  1 
ATOM   2763  C C   . VAL B 1 136 ? 37.345  -20.351 -41.649  1.00 23.98 ? 136 VAL B C   1 
ATOM   2764  O O   . VAL B 1 136 ? 38.096  -20.720 -40.764  1.00 24.99 ? 136 VAL B O   1 
ATOM   2765  C CB  . VAL B 1 136 ? 37.205  -22.165 -43.357  1.00 26.23 ? 136 VAL B CB  1 
ATOM   2766  C CG1 . VAL B 1 136 ? 35.761  -22.398 -42.936  1.00 26.78 ? 136 VAL B CG1 1 
ATOM   2767  C CG2 . VAL B 1 136 ? 37.346  -22.514 -44.819  1.00 26.35 ? 136 VAL B CG2 1 
ATOM   2768  N N   . LEU B 1 137 ? 36.253  -19.633 -41.427  1.00 22.33 ? 137 LEU B N   1 
ATOM   2769  C CA  . LEU B 1 137 ? 35.684  -19.422 -40.103  1.00 21.65 ? 137 LEU B CA  1 
ATOM   2770  C C   . LEU B 1 137 ? 34.375  -20.207 -40.014  1.00 20.46 ? 137 LEU B C   1 
ATOM   2771  O O   . LEU B 1 137 ? 33.377  -19.831 -40.627  1.00 19.99 ? 137 LEU B O   1 
ATOM   2772  C CB  . LEU B 1 137 ? 35.427  -17.929 -39.846  1.00 21.97 ? 137 LEU B CB  1 
ATOM   2773  C CG  . LEU B 1 137 ? 34.572  -17.520 -38.643  1.00 22.13 ? 137 LEU B CG  1 
ATOM   2774  C CD1 . LEU B 1 137 ? 35.197  -17.975 -37.326  1.00 22.37 ? 137 LEU B CD1 1 
ATOM   2775  C CD2 . LEU B 1 137 ? 34.384  -16.006 -38.653  1.00 22.58 ? 137 LEU B CD2 1 
ATOM   2776  N N   . LEU B 1 138 ? 34.397  -21.301 -39.256  1.00 19.42 ? 138 LEU B N   1 
ATOM   2777  C CA  . LEU B 1 138 ? 33.197  -22.095 -39.020  1.00 18.43 ? 138 LEU B CA  1 
ATOM   2778  C C   . LEU B 1 138 ? 32.429  -21.497 -37.858  1.00 17.96 ? 138 LEU B C   1 
ATOM   2779  O O   . LEU B 1 138 ? 32.983  -21.344 -36.780  1.00 17.07 ? 138 LEU B O   1 
ATOM   2780  C CB  . LEU B 1 138 ? 33.553  -23.549 -38.696  1.00 17.69 ? 138 LEU B CB  1 
ATOM   2781  C CG  . LEU B 1 138 ? 32.361  -24.454 -38.402  1.00 16.83 ? 138 LEU B CG  1 
ATOM   2782  C CD1 . LEU B 1 138 ? 31.429  -24.500 -39.605  1.00 17.31 ? 138 LEU B CD1 1 
ATOM   2783  C CD2 . LEU B 1 138 ? 32.843  -25.833 -38.026  1.00 16.54 ? 138 LEU B CD2 1 
ATOM   2784  N N   . ILE B 1 139 ? 31.161  -21.164 -38.091  1.00 17.62 ? 139 ILE B N   1 
ATOM   2785  C CA  . ILE B 1 139 ? 30.309  -20.597 -37.049  1.00 17.48 ? 139 ILE B CA  1 
ATOM   2786  C C   . ILE B 1 139 ? 29.212  -21.580 -36.673  1.00 17.84 ? 139 ILE B C   1 
ATOM   2787  O O   . ILE B 1 139 ? 28.420  -21.998 -37.503  1.00 17.32 ? 139 ILE B O   1 
ATOM   2788  C CB  . ILE B 1 139 ? 29.674  -19.244 -37.463  1.00 16.86 ? 139 ILE B CB  1 
ATOM   2789  C CG1 . ILE B 1 139 ? 30.765  -18.233 -37.808  1.00 16.61 ? 139 ILE B CG1 1 
ATOM   2790  C CG2 . ILE B 1 139 ? 28.811  -18.687 -36.332  1.00 16.73 ? 139 ILE B CG2 1 
ATOM   2791  C CD1 . ILE B 1 139 ? 30.242  -16.908 -38.285  1.00 16.31 ? 139 ILE B CD1 1 
ATOM   2792  N N   . SER B 1 140 ? 29.180  -21.939 -35.402  1.00 18.71 ? 140 SER B N   1 
ATOM   2793  C CA  . SER B 1 140 ? 28.123  -22.763 -34.877  1.00 19.15 ? 140 SER B CA  1 
ATOM   2794  C C   . SER B 1 140 ? 26.925  -21.870 -34.574  1.00 19.29 ? 140 SER B C   1 
ATOM   2795  O O   . SER B 1 140 ? 27.098  -20.801 -34.008  1.00 19.14 ? 140 SER B O   1 
ATOM   2796  C CB  . SER B 1 140 ? 28.619  -23.448 -33.609  1.00 19.55 ? 140 SER B CB  1 
ATOM   2797  O OG  . SER B 1 140 ? 27.603  -23.492 -32.657  1.00 20.24 ? 140 SER B OG  1 
ATOM   2798  N N   . PRO B 1 141 ? 25.711  -22.302 -34.938  1.00 19.74 ? 141 PRO B N   1 
ATOM   2799  C CA  . PRO B 1 141 ? 24.524  -21.521 -34.615  1.00 19.63 ? 141 PRO B CA  1 
ATOM   2800  C C   . PRO B 1 141 ? 24.138  -21.661 -33.150  1.00 19.13 ? 141 PRO B C   1 
ATOM   2801  O O   . PRO B 1 141 ? 24.630  -22.548 -32.460  1.00 18.74 ? 141 PRO B O   1 
ATOM   2802  C CB  . PRO B 1 141 ? 23.445  -22.149 -35.488  1.00 20.21 ? 141 PRO B CB  1 
ATOM   2803  C CG  . PRO B 1 141 ? 23.837  -23.573 -35.573  1.00 20.58 ? 141 PRO B CG  1 
ATOM   2804  C CD  . PRO B 1 141 ? 25.352  -23.594 -35.545  1.00 20.73 ? 141 PRO B CD  1 
ATOM   2805  N N   . PRO B 1 142 ? 23.255  -20.780 -32.674  1.00 18.86 ? 142 PRO B N   1 
ATOM   2806  C CA  . PRO B 1 142 ? 22.837  -20.890 -31.291  1.00 19.58 ? 142 PRO B CA  1 
ATOM   2807  C C   . PRO B 1 142 ? 21.861  -22.035 -31.113  1.00 19.60 ? 142 PRO B C   1 
ATOM   2808  O O   . PRO B 1 142 ? 21.409  -22.604 -32.089  1.00 18.88 ? 142 PRO B O   1 
ATOM   2809  C CB  . PRO B 1 142 ? 22.153  -19.550 -31.021  1.00 19.73 ? 142 PRO B CB  1 
ATOM   2810  C CG  . PRO B 1 142 ? 21.641  -19.146 -32.357  1.00 19.39 ? 142 PRO B CG  1 
ATOM   2811  C CD  . PRO B 1 142 ? 22.601  -19.665 -33.369  1.00 18.61 ? 142 PRO B CD  1 
ATOM   2812  N N   . PRO B 1 143 ? 21.561  -22.389 -29.860  1.00 20.88 ? 143 PRO B N   1 
ATOM   2813  C CA  . PRO B 1 143 ? 20.537  -23.396 -29.654  1.00 21.77 ? 143 PRO B CA  1 
ATOM   2814  C C   . PRO B 1 143 ? 19.213  -22.949 -30.190  1.00 22.22 ? 143 PRO B C   1 
ATOM   2815  O O   . PRO B 1 143 ? 18.924  -21.762 -30.194  1.00 23.91 ? 143 PRO B O   1 
ATOM   2816  C CB  . PRO B 1 143 ? 20.468  -23.537 -28.126  1.00 21.53 ? 143 PRO B CB  1 
ATOM   2817  C CG  . PRO B 1 143 ? 21.819  -23.125 -27.661  1.00 20.79 ? 143 PRO B CG  1 
ATOM   2818  C CD  . PRO B 1 143 ? 22.239  -22.030 -28.602  1.00 20.76 ? 143 PRO B CD  1 
ATOM   2819  N N   . LEU B 1 144 ? 18.425  -23.914 -30.629  1.00 22.95 ? 144 LEU B N   1 
ATOM   2820  C CA  . LEU B 1 144 ? 17.066  -23.663 -31.063  1.00 24.39 ? 144 LEU B CA  1 
ATOM   2821  C C   . LEU B 1 144 ? 16.259  -23.122 -29.888  1.00 25.40 ? 144 LEU B C   1 
ATOM   2822  O O   . LEU B 1 144 ? 16.649  -23.261 -28.723  1.00 25.87 ? 144 LEU B O   1 
ATOM   2823  C CB  . LEU B 1 144 ? 16.406  -24.953 -31.525  1.00 25.22 ? 144 LEU B CB  1 
ATOM   2824  C CG  . LEU B 1 144 ? 17.006  -25.748 -32.676  1.00 25.92 ? 144 LEU B CG  1 
ATOM   2825  C CD1 . LEU B 1 144 ? 16.374  -27.130 -32.755  1.00 25.32 ? 144 LEU B CD1 1 
ATOM   2826  C CD2 . LEU B 1 144 ? 16.822  -24.995 -33.977  1.00 27.15 ? 144 LEU B CD2 1 
ATOM   2827  N N   . GLY B 1 145 ? 15.120  -22.516 -30.211  1.00 25.56 ? 145 GLY B N   1 
ATOM   2828  C CA  . GLY B 1 145 ? 14.147  -22.101 -29.215  1.00 26.40 ? 145 GLY B CA  1 
ATOM   2829  C C   . GLY B 1 145 ? 13.563  -23.288 -28.485  1.00 27.53 ? 145 GLY B C   1 
ATOM   2830  O O   . GLY B 1 145 ? 13.479  -24.377 -29.033  1.00 26.86 ? 145 GLY B O   1 
ATOM   2831  N N   . GLU B 1 146 ? 13.164  -23.072 -27.236  1.00 28.81 ? 146 GLU B N   1 
ATOM   2832  C CA  . GLU B 1 146 ? 12.526  -24.121 -26.443  1.00 29.16 ? 146 GLU B CA  1 
ATOM   2833  C C   . GLU B 1 146 ? 11.125  -24.384 -26.945  1.00 27.01 ? 146 GLU B C   1 
ATOM   2834  O O   . GLU B 1 146 ? 10.623  -25.480 -26.762  1.00 27.60 ? 146 GLU B O   1 
ATOM   2835  C CB  . GLU B 1 146 ? 12.496  -23.769 -24.967  1.00 32.42 ? 146 GLU B CB  1 
ATOM   2836  C CG  . GLU B 1 146 ? 13.885  -23.824 -24.352  1.00 37.07 ? 146 GLU B CG  1 
ATOM   2837  C CD  . GLU B 1 146 ? 13.863  -24.089 -22.873  1.00 41.02 ? 146 GLU B CD  1 
ATOM   2838  O OE1 . GLU B 1 146 ? 14.973  -24.345 -22.337  1.00 44.65 ? 146 GLU B OE1 1 
ATOM   2839  O OE2 . GLU B 1 146 ? 12.777  -24.033 -22.229  1.00 42.70 ? 146 GLU B OE2 1 
ATOM   2840  N N   . THR B 1 147 ? 10.520  -23.391 -27.593  1.00 25.84 ? 147 THR B N   1 
ATOM   2841  C CA  . THR B 1 147 ? 9.176   -23.536 -28.154  1.00 24.87 ? 147 THR B CA  1 
ATOM   2842  C C   . THR B 1 147 ? 9.125   -23.222 -29.654  1.00 24.27 ? 147 THR B C   1 
ATOM   2843  O O   . THR B 1 147 ? 9.253   -22.074 -30.083  1.00 24.03 ? 147 THR B O   1 
ATOM   2844  C CB  . THR B 1 147 ? 8.173   -22.646 -27.409  1.00 24.42 ? 147 THR B CB  1 
ATOM   2845  O OG1 . THR B 1 147 ? 8.185   -23.023 -26.035  1.00 24.23 ? 147 THR B OG1 1 
ATOM   2846  C CG2 . THR B 1 147 ? 6.764   -22.814 -27.951  1.00 23.95 ? 147 THR B CG2 1 
ATOM   2847  N N   . ILE B 1 148 ? 8.898   -24.266 -30.439  1.00 23.80 ? 148 ILE B N   1 
ATOM   2848  C CA  . ILE B 1 148 ? 8.903   -24.165 -31.880  1.00 23.51 ? 148 ILE B CA  1 
ATOM   2849  C C   . ILE B 1 148 ? 7.467   -24.168 -32.419  1.00 23.21 ? 148 ILE B C   1 
ATOM   2850  O O   . ILE B 1 148 ? 6.593   -24.858 -31.893  1.00 23.45 ? 148 ILE B O   1 
ATOM   2851  C CB  . ILE B 1 148 ? 9.756   -25.308 -32.468  1.00 23.27 ? 148 ILE B CB  1 
ATOM   2852  C CG1 . ILE B 1 148 ? 11.216  -25.097 -32.038  1.00 22.83 ? 148 ILE B CG1 1 
ATOM   2853  C CG2 . ILE B 1 148 ? 9.634   -25.365 -33.992  1.00 23.15 ? 148 ILE B CG2 1 
ATOM   2854  C CD1 . ILE B 1 148 ? 12.090  -26.319 -32.163  1.00 22.92 ? 148 ILE B CD1 1 
ATOM   2855  N N   . ASP B 1 149 ? 7.233   -23.372 -33.457  1.00 22.59 ? 149 ASP B N   1 
ATOM   2856  C CA  . ASP B 1 149 ? 5.917   -23.276 -34.063  1.00 23.16 ? 149 ASP B CA  1 
ATOM   2857  C C   . ASP B 1 149 ? 5.365   -24.695 -34.255  1.00 23.85 ? 149 ASP B C   1 
ATOM   2858  O O   . ASP B 1 149 ? 6.058   -25.557 -34.805  1.00 22.90 ? 149 ASP B O   1 
ATOM   2859  C CB  . ASP B 1 149 ? 6.012   -22.544 -35.395  1.00 23.29 ? 149 ASP B CB  1 
ATOM   2860  C CG  . ASP B 1 149 ? 4.655   -22.182 -35.977  1.00 22.48 ? 149 ASP B CG  1 
ATOM   2861  O OD1 . ASP B 1 149 ? 3.806   -23.083 -36.136  1.00 21.80 ? 149 ASP B OD1 1 
ATOM   2862  O OD2 . ASP B 1 149 ? 4.468   -20.987 -36.311  1.00 22.06 ? 149 ASP B OD2 1 
ATOM   2863  N N   . PRO B 1 150 ? 4.132   -24.950 -33.764  1.00 24.24 ? 150 PRO B N   1 
ATOM   2864  C CA  . PRO B 1 150 ? 3.499   -26.256 -33.860  1.00 24.17 ? 150 PRO B CA  1 
ATOM   2865  C C   . PRO B 1 150 ? 3.533   -26.924 -35.246  1.00 24.51 ? 150 PRO B C   1 
ATOM   2866  O O   . PRO B 1 150 ? 3.575   -28.157 -35.310  1.00 24.52 ? 150 PRO B O   1 
ATOM   2867  C CB  . PRO B 1 150 ? 2.048   -25.966 -33.444  1.00 24.41 ? 150 PRO B CB  1 
ATOM   2868  C CG  . PRO B 1 150 ? 1.969   -24.517 -32.986  1.00 24.27 ? 150 PRO B CG  1 
ATOM   2869  C CD  . PRO B 1 150 ? 3.392   -24.087 -32.825  1.00 24.28 ? 150 PRO B CD  1 
ATOM   2870  N N   . LEU B 1 151 ? 3.491   -26.128 -36.326  1.00 24.35 ? 151 LEU B N   1 
ATOM   2871  C CA  . LEU B 1 151 ? 3.625   -26.681 -37.672  1.00 24.57 ? 151 LEU B CA  1 
ATOM   2872  C C   . LEU B 1 151 ? 4.999   -27.338 -37.901  1.00 24.84 ? 151 LEU B C   1 
ATOM   2873  O O   . LEU B 1 151 ? 5.095   -28.351 -38.576  1.00 24.74 ? 151 LEU B O   1 
ATOM   2874  C CB  . LEU B 1 151 ? 3.414   -25.597 -38.720  1.00 26.02 ? 151 LEU B CB  1 
ATOM   2875  C CG  . LEU B 1 151 ? 1.970   -25.186 -39.005  1.00 28.74 ? 151 LEU B CG  1 
ATOM   2876  C CD1 . LEU B 1 151 ? 1.787   -23.680 -38.815  1.00 29.45 ? 151 LEU B CD1 1 
ATOM   2877  C CD2 . LEU B 1 151 ? 1.548   -25.619 -40.407  1.00 29.24 ? 151 LEU B CD2 1 
ATOM   2878  N N   . ALA B 1 152 ? 6.051   -26.756 -37.328  1.00 24.67 ? 152 ALA B N   1 
ATOM   2879  C CA  . ALA B 1 152 ? 7.421   -27.213 -37.538  1.00 24.46 ? 152 ALA B CA  1 
ATOM   2880  C C   . ALA B 1 152 ? 7.949   -28.139 -36.429  1.00 24.08 ? 152 ALA B C   1 
ATOM   2881  O O   . ALA B 1 152 ? 8.908   -28.879 -36.648  1.00 23.08 ? 152 ALA B O   1 
ATOM   2882  C CB  . ALA B 1 152 ? 8.338   -26.003 -37.677  1.00 24.67 ? 152 ALA B CB  1 
ATOM   2883  N N   . ALA B 1 153 ? 7.335   -28.113 -35.252  1.00 23.84 ? 153 ALA B N   1 
ATOM   2884  C CA  . ALA B 1 153 ? 7.829   -28.898 -34.117  1.00 23.89 ? 153 ALA B CA  1 
ATOM   2885  C C   . ALA B 1 153 ? 8.070   -30.399 -34.390  1.00 23.68 ? 153 ALA B C   1 
ATOM   2886  O O   . ALA B 1 153 ? 9.094   -30.930 -33.965  1.00 24.21 ? 153 ALA B O   1 
ATOM   2887  C CB  . ALA B 1 153 ? 6.901   -28.724 -32.922  1.00 23.42 ? 153 ALA B CB  1 
ATOM   2888  N N   . PRO B 1 154 ? 7.147   -31.087 -35.093  1.00 23.41 ? 154 PRO B N   1 
ATOM   2889  C CA  . PRO B 1 154 ? 7.353   -32.522 -35.375  1.00 23.27 ? 154 PRO B CA  1 
ATOM   2890  C C   . PRO B 1 154 ? 8.662   -32.826 -36.089  1.00 22.31 ? 154 PRO B C   1 
ATOM   2891  O O   . PRO B 1 154 ? 9.244   -33.898 -35.863  1.00 21.84 ? 154 PRO B O   1 
ATOM   2892  C CB  . PRO B 1 154 ? 6.183   -32.870 -36.310  1.00 23.71 ? 154 PRO B CB  1 
ATOM   2893  C CG  . PRO B 1 154 ? 5.131   -31.856 -35.996  1.00 23.53 ? 154 PRO B CG  1 
ATOM   2894  C CD  . PRO B 1 154 ? 5.881   -30.597 -35.675  1.00 23.86 ? 154 PRO B CD  1 
ATOM   2895  N N   . ILE B 1 155 ? 9.103   -31.883 -36.919  1.00 21.54 ? 155 ILE B N   1 
ATOM   2896  C CA  . ILE B 1 155 ? 10.352  -32.027 -37.682  1.00 21.29 ? 155 ILE B CA  1 
ATOM   2897  C C   . ILE B 1 155 ? 11.605  -31.620 -36.899  1.00 20.81 ? 155 ILE B C   1 
ATOM   2898  O O   . ILE B 1 155 ? 12.708  -31.860 -37.358  1.00 21.91 ? 155 ILE B O   1 
ATOM   2899  C CB  . ILE B 1 155 ? 10.318  -31.404 -39.104  1.00 21.25 ? 155 ILE B CB  1 
ATOM   2900  C CG1 . ILE B 1 155 ? 10.320  -29.853 -39.099  1.00 21.32 ? 155 ILE B CG1 1 
ATOM   2901  C CG2 . ILE B 1 155 ? 9.197   -31.989 -39.952  1.00 20.78 ? 155 ILE B CG2 1 
ATOM   2902  C CD1 . ILE B 1 155 ? 10.573  -29.233 -40.440  1.00 20.46 ? 155 ILE B CD1 1 
ATOM   2903  N N   . PHE B 1 156 ? 11.446  -31.050 -35.705  1.00 21.21 ? 156 PHE B N   1 
ATOM   2904  C CA  . PHE B 1 156 ? 12.590  -30.681 -34.830  1.00 21.14 ? 156 PHE B CA  1 
ATOM   2905  C C   . PHE B 1 156 ? 12.614  -31.414 -33.482  1.00 20.76 ? 156 PHE B C   1 
ATOM   2906  O O   . PHE B 1 156 ? 13.142  -30.896 -32.502  1.00 20.39 ? 156 PHE B O   1 
ATOM   2907  C CB  . PHE B 1 156 ? 12.629  -29.158 -34.609  1.00 20.81 ? 156 PHE B CB  1 
ATOM   2908  C CG  . PHE B 1 156 ? 13.119  -28.392 -35.798  1.00 20.43 ? 156 PHE B CG  1 
ATOM   2909  C CD1 . PHE B 1 156 ? 14.472  -28.344 -36.087  1.00 20.97 ? 156 PHE B CD1 1 
ATOM   2910  C CD2 . PHE B 1 156 ? 12.241  -27.733 -36.635  1.00 20.07 ? 156 PHE B CD2 1 
ATOM   2911  C CE1 . PHE B 1 156 ? 14.935  -27.629 -37.193  1.00 20.71 ? 156 PHE B CE1 1 
ATOM   2912  C CE2 . PHE B 1 156 ? 12.698  -27.007 -37.722  1.00 19.92 ? 156 PHE B CE2 1 
ATOM   2913  C CZ  . PHE B 1 156 ? 14.047  -26.966 -38.010  1.00 20.06 ? 156 PHE B CZ  1 
ATOM   2914  N N   . VAL B 1 157 ? 12.077  -32.627 -33.446  1.00 20.96 ? 157 VAL B N   1 
ATOM   2915  C CA  . VAL B 1 157 ? 12.112  -33.435 -32.226  1.00 21.77 ? 157 VAL B CA  1 
ATOM   2916  C C   . VAL B 1 157 ? 13.572  -33.821 -31.961  1.00 22.28 ? 157 VAL B C   1 
ATOM   2917  O O   . VAL B 1 157 ? 14.317  -34.123 -32.897  1.00 23.33 ? 157 VAL B O   1 
ATOM   2918  C CB  . VAL B 1 157 ? 11.183  -34.684 -32.331  1.00 21.32 ? 157 VAL B CB  1 
ATOM   2919  C CG1 . VAL B 1 157 ? 11.397  -35.642 -31.168  1.00 20.97 ? 157 VAL B CG1 1 
ATOM   2920  C CG2 . VAL B 1 157 ? 9.722   -34.256 -32.416  1.00 21.01 ? 157 VAL B CG2 1 
ATOM   2921  N N   . ASP B 1 158 ? 13.978  -33.756 -30.696  1.00 22.22 ? 158 ASP B N   1 
ATOM   2922  C CA  . ASP B 1 158 ? 15.381  -33.925 -30.291  1.00 22.43 ? 158 ASP B CA  1 
ATOM   2923  C C   . ASP B 1 158 ? 16.367  -32.943 -30.938  1.00 21.95 ? 158 ASP B C   1 
ATOM   2924  O O   . ASP B 1 158 ? 17.581  -33.123 -30.815  1.00 22.26 ? 158 ASP B O   1 
ATOM   2925  C CB  . ASP B 1 158 ? 15.855  -35.349 -30.564  1.00 22.39 ? 158 ASP B CB  1 
ATOM   2926  C CG  . ASP B 1 158 ? 14.918  -36.382 -30.009  1.00 22.14 ? 158 ASP B CG  1 
ATOM   2927  O OD1 . ASP B 1 158 ? 14.509  -36.244 -28.836  1.00 21.78 ? 158 ASP B OD1 1 
ATOM   2928  O OD2 . ASP B 1 158 ? 14.594  -37.333 -30.750  1.00 21.78 ? 158 ASP B OD2 1 
ATOM   2929  N N   . GLY B 1 159 ? 15.863  -31.900 -31.594  1.00 20.91 ? 159 GLY B N   1 
ATOM   2930  C CA  . GLY B 1 159 ? 16.731  -30.961 -32.285  1.00 20.88 ? 159 GLY B CA  1 
ATOM   2931  C C   . GLY B 1 159 ? 17.475  -30.016 -31.344  1.00 21.29 ? 159 GLY B C   1 
ATOM   2932  O O   . GLY B 1 159 ? 18.625  -29.648 -31.595  1.00 21.22 ? 159 GLY B O   1 
ATOM   2933  N N   . LEU B 1 160 ? 16.804  -29.616 -30.268  1.00 21.71 ? 160 LEU B N   1 
ATOM   2934  C CA  . LEU B 1 160 ? 17.360  -28.670 -29.318  1.00 21.31 ? 160 LEU B CA  1 
ATOM   2935  C C   . LEU B 1 160 ? 18.655  -29.210 -28.727  1.00 21.17 ? 160 LEU B C   1 
ATOM   2936  O O   . LEU B 1 160 ? 19.672  -28.512 -28.697  1.00 21.29 ? 160 LEU B O   1 
ATOM   2937  C CB  . LEU B 1 160 ? 16.353  -28.406 -28.201  1.00 21.87 ? 160 LEU B CB  1 
ATOM   2938  C CG  . LEU B 1 160 ? 16.832  -27.591 -26.996  1.00 22.10 ? 160 LEU B CG  1 
ATOM   2939  C CD1 . LEU B 1 160 ? 17.328  -26.231 -27.462  1.00 23.12 ? 160 LEU B CD1 1 
ATOM   2940  C CD2 . LEU B 1 160 ? 15.698  -27.426 -25.992  1.00 21.80 ? 160 LEU B CD2 1 
ATOM   2941  N N   . ALA B 1 161 ? 18.618  -30.459 -28.263  1.00 20.45 ? 161 ALA B N   1 
ATOM   2942  C CA  . ALA B 1 161 ? 19.783  -31.048 -27.615  1.00 19.66 ? 161 ALA B CA  1 
ATOM   2943  C C   . ALA B 1 161 ? 20.948  -31.143 -28.594  1.00 19.93 ? 161 ALA B C   1 
ATOM   2944  O O   . ALA B 1 161 ? 22.104  -30.863 -28.239  1.00 20.57 ? 161 ALA B O   1 
ATOM   2945  C CB  . ALA B 1 161 ? 19.449  -32.397 -27.029  1.00 19.34 ? 161 ALA B CB  1 
ATOM   2946  N N   . LYS B 1 162 ? 20.637  -31.504 -29.836  1.00 20.15 ? 162 LYS B N   1 
ATOM   2947  C CA  . LYS B 1 162 ? 21.643  -31.554 -30.888  1.00 20.23 ? 162 LYS B CA  1 
ATOM   2948  C C   . LYS B 1 162 ? 22.264  -30.192 -31.123  1.00 20.13 ? 162 LYS B C   1 
ATOM   2949  O O   . LYS B 1 162 ? 23.480  -30.086 -31.242  1.00 20.58 ? 162 LYS B O   1 
ATOM   2950  C CB  . LYS B 1 162 ? 21.037  -32.065 -32.184  1.00 21.06 ? 162 LYS B CB  1 
ATOM   2951  C CG  . LYS B 1 162 ? 20.678  -33.532 -32.144  1.00 22.29 ? 162 LYS B CG  1 
ATOM   2952  C CD  . LYS B 1 162 ? 19.962  -33.990 -33.394  1.00 22.35 ? 162 LYS B CD  1 
ATOM   2953  C CE  . LYS B 1 162 ? 19.302  -35.332 -33.154  1.00 22.83 ? 162 LYS B CE  1 
ATOM   2954  N NZ  . LYS B 1 162 ? 18.927  -35.963 -34.444  1.00 23.86 ? 162 LYS B NZ  1 
ATOM   2955  N N   . SER B 1 163 ? 21.432  -29.154 -31.192  1.00 19.68 ? 163 SER B N   1 
ATOM   2956  C CA  . SER B 1 163 ? 21.924  -27.803 -31.436  1.00 19.78 ? 163 SER B CA  1 
ATOM   2957  C C   . SER B 1 163 ? 22.805  -27.302 -30.285  1.00 20.86 ? 163 SER B C   1 
ATOM   2958  O O   . SER B 1 163 ? 23.752  -26.531 -30.508  1.00 21.39 ? 163 SER B O   1 
ATOM   2959  C CB  . SER B 1 163 ? 20.772  -26.832 -31.693  1.00 19.04 ? 163 SER B CB  1 
ATOM   2960  O OG  . SER B 1 163 ? 19.991  -26.606 -30.542  1.00 17.60 ? 163 SER B OG  1 
ATOM   2961  N N   . GLU B 1 164 ? 22.509  -27.744 -29.059  1.00 20.61 ? 164 GLU B N   1 
ATOM   2962  C CA  . GLU B 1 164 ? 23.322  -27.358 -27.907  1.00 19.99 ? 164 GLU B CA  1 
ATOM   2963  C C   . GLU B 1 164 ? 24.707  -27.973 -27.987  1.00 19.47 ? 164 GLU B C   1 
ATOM   2964  O O   . GLU B 1 164 ? 25.684  -27.365 -27.554  1.00 19.24 ? 164 GLU B O   1 
ATOM   2965  C CB  . GLU B 1 164 ? 22.638  -27.744 -26.599  1.00 20.53 ? 164 GLU B CB  1 
ATOM   2966  C CG  . GLU B 1 164 ? 21.590  -26.742 -26.114  1.00 20.61 ? 164 GLU B CG  1 
ATOM   2967  C CD  . GLU B 1 164 ? 20.612  -27.336 -25.105  1.00 20.46 ? 164 GLU B CD  1 
ATOM   2968  O OE1 . GLU B 1 164 ? 19.752  -26.583 -24.596  1.00 20.13 ? 164 GLU B OE1 1 
ATOM   2969  O OE2 . GLU B 1 164 ? 20.690  -28.553 -24.819  1.00 20.16 ? 164 GLU B OE2 1 
ATOM   2970  N N   . ALA B 1 165 ? 24.792  -29.169 -28.564  1.00 19.68 ? 165 ALA B N   1 
ATOM   2971  C CA  . ALA B 1 165 ? 26.066  -29.887 -28.684  1.00 20.57 ? 165 ALA B CA  1 
ATOM   2972  C C   . ALA B 1 165 ? 26.976  -29.451 -29.852  1.00 21.13 ? 165 ALA B C   1 
ATOM   2973  O O   . ALA B 1 165 ? 28.119  -29.925 -29.943  1.00 22.27 ? 165 ALA B O   1 
ATOM   2974  C CB  . ALA B 1 165 ? 25.797  -31.374 -28.778  1.00 20.12 ? 165 ALA B CB  1 
ATOM   2975  N N   . LEU B 1 166 ? 26.488  -28.583 -30.744  1.00 20.70 ? 166 LEU B N   1 
ATOM   2976  C CA  . LEU B 1 166 ? 27.242  -28.237 -31.955  1.00 19.90 ? 166 LEU B CA  1 
ATOM   2977  C C   . LEU B 1 166 ? 28.513  -27.410 -31.692  1.00 19.06 ? 166 LEU B C   1 
ATOM   2978  O O   . LEU B 1 166 ? 29.559  -27.719 -32.248  1.00 19.15 ? 166 LEU B O   1 
ATOM   2979  C CB  . LEU B 1 166 ? 26.352  -27.542 -32.993  1.00 20.01 ? 166 LEU B CB  1 
ATOM   2980  C CG  . LEU B 1 166 ? 25.232  -28.376 -33.633  1.00 19.79 ? 166 LEU B CG  1 
ATOM   2981  C CD1 . LEU B 1 166 ? 24.445  -27.578 -34.672  1.00 19.29 ? 166 LEU B CD1 1 
ATOM   2982  C CD2 . LEU B 1 166 ? 25.777  -29.652 -34.248  1.00 19.61 ? 166 LEU B CD2 1 
ATOM   2983  N N   . PRO B 1 167 ? 28.434  -26.370 -30.843  1.00 18.18 ? 167 PRO B N   1 
ATOM   2984  C CA  . PRO B 1 167 ? 29.661  -25.591 -30.608  1.00 17.85 ? 167 PRO B CA  1 
ATOM   2985  C C   . PRO B 1 167 ? 30.897  -26.430 -30.245  1.00 17.89 ? 167 PRO B C   1 
ATOM   2986  O O   . PRO B 1 167 ? 31.977  -26.209 -30.814  1.00 18.15 ? 167 PRO B O   1 
ATOM   2987  C CB  . PRO B 1 167 ? 29.272  -24.671 -29.454  1.00 17.59 ? 167 PRO B CB  1 
ATOM   2988  C CG  . PRO B 1 167 ? 27.795  -24.521 -29.547  1.00 17.85 ? 167 PRO B CG  1 
ATOM   2989  C CD  . PRO B 1 167 ? 27.277  -25.825 -30.102  1.00 17.72 ? 167 PRO B CD  1 
ATOM   2990  N N   . GLY B 1 168 ? 30.748  -27.393 -29.332  1.00 17.78 ? 168 GLY B N   1 
ATOM   2991  C CA  . GLY B 1 168 ? 31.864  -28.235 -28.924  1.00 18.20 ? 168 GLY B CA  1 
ATOM   2992  C C   . GLY B 1 168 ? 32.463  -29.009 -30.084  1.00 18.92 ? 168 GLY B C   1 
ATOM   2993  O O   . GLY B 1 168 ? 33.690  -29.008 -30.300  1.00 19.58 ? 168 GLY B O   1 
ATOM   2994  N N   . VAL B 1 169 ? 31.584  -29.658 -30.847  1.00 19.66 ? 169 VAL B N   1 
ATOM   2995  C CA  . VAL B 1 169 ? 31.989  -30.483 -31.986  1.00 19.26 ? 169 VAL B CA  1 
ATOM   2996  C C   . VAL B 1 169 ? 32.599  -29.609 -33.080  1.00 19.29 ? 169 VAL B C   1 
ATOM   2997  O O   . VAL B 1 169 ? 33.676  -29.919 -33.582  1.00 19.00 ? 169 VAL B O   1 
ATOM   2998  C CB  . VAL B 1 169 ? 30.791  -31.260 -32.579  1.00 19.09 ? 169 VAL B CB  1 
ATOM   2999  C CG1 . VAL B 1 169 ? 31.198  -32.009 -33.836  1.00 19.07 ? 169 VAL B CG1 1 
ATOM   3000  C CG2 . VAL B 1 169 ? 30.205  -32.234 -31.572  1.00 18.74 ? 169 VAL B CG2 1 
ATOM   3001  N N   . TYR B 1 170 ? 31.897  -28.530 -33.448  1.00 19.54 ? 170 TYR B N   1 
ATOM   3002  C CA  . TYR B 1 170 ? 32.374  -27.594 -34.477  1.00 20.32 ? 170 TYR B CA  1 
ATOM   3003  C C   . TYR B 1 170 ? 33.760  -27.048 -34.155  1.00 21.49 ? 170 TYR B C   1 
ATOM   3004  O O   . TYR B 1 170 ? 34.603  -26.922 -35.052  1.00 21.24 ? 170 TYR B O   1 
ATOM   3005  C CB  . TYR B 1 170 ? 31.399  -26.422 -34.672  1.00 20.09 ? 170 TYR B CB  1 
ATOM   3006  C CG  . TYR B 1 170 ? 30.248  -26.678 -35.636  1.00 20.00 ? 170 TYR B CG  1 
ATOM   3007  C CD1 . TYR B 1 170 ? 29.730  -27.947 -35.823  1.00 20.07 ? 170 TYR B CD1 1 
ATOM   3008  C CD2 . TYR B 1 170 ? 29.658  -25.628 -36.331  1.00 20.37 ? 170 TYR B CD2 1 
ATOM   3009  C CE1 . TYR B 1 170 ? 28.671  -28.170 -36.679  1.00 20.27 ? 170 TYR B CE1 1 
ATOM   3010  C CE2 . TYR B 1 170 ? 28.595  -25.842 -37.197  1.00 20.67 ? 170 TYR B CE2 1 
ATOM   3011  C CZ  . TYR B 1 170 ? 28.103  -27.114 -37.369  1.00 20.84 ? 170 TYR B CZ  1 
ATOM   3012  O OH  . TYR B 1 170 ? 27.054  -27.347 -38.235  1.00 21.17 ? 170 TYR B OH  1 
ATOM   3013  N N   . LYS B 1 171 ? 33.999  -26.729 -32.884  1.00 22.90 ? 171 LYS B N   1 
ATOM   3014  C CA  . LYS B 1 171 ? 35.307  -26.228 -32.484  1.00 24.79 ? 171 LYS B CA  1 
ATOM   3015  C C   . LYS B 1 171 ? 36.413  -27.245 -32.741  1.00 22.71 ? 171 LYS B C   1 
ATOM   3016  O O   . LYS B 1 171 ? 37.464  -26.887 -33.281  1.00 21.22 ? 171 LYS B O   1 
ATOM   3017  C CB  . LYS B 1 171 ? 35.330  -25.785 -31.019  1.00 28.08 ? 171 LYS B CB  1 
ATOM   3018  C CG  . LYS B 1 171 ? 36.606  -24.999 -30.712  1.00 31.81 ? 171 LYS B CG  1 
ATOM   3019  C CD  . LYS B 1 171 ? 36.677  -24.428 -29.310  1.00 34.59 ? 171 LYS B CD  1 
ATOM   3020  C CE  . LYS B 1 171 ? 37.156  -25.469 -28.288  1.00 37.31 ? 171 LYS B CE  1 
ATOM   3021  N NZ  . LYS B 1 171 ? 38.648  -25.593 -28.113  1.00 39.18 ? 171 LYS B NZ  1 
ATOM   3022  N N   . ALA B 1 172 ? 36.176  -28.501 -32.354  1.00 21.84 ? 172 ALA B N   1 
ATOM   3023  C CA  . ALA B 1 172 ? 37.183  -29.552 -32.535  1.00 21.14 ? 172 ALA B CA  1 
ATOM   3024  C C   . ALA B 1 172 ? 37.475  -29.763 -34.015  1.00 20.66 ? 172 ALA B C   1 
ATOM   3025  O O   . ALA B 1 172 ? 38.638  -29.808 -34.419  1.00 20.90 ? 172 ALA B O   1 
ATOM   3026  C CB  . ALA B 1 172 ? 36.733  -30.849 -31.897  1.00 20.88 ? 172 ALA B CB  1 
ATOM   3027  N N   . ILE B 1 173 ? 36.413  -29.861 -34.808  1.00 20.55 ? 173 ILE B N   1 
ATOM   3028  C CA  . ILE B 1 173 ? 36.530  -30.084 -36.235  1.00 21.79 ? 173 ILE B CA  1 
ATOM   3029  C C   . ILE B 1 173 ? 37.291  -28.946 -36.924  1.00 21.41 ? 173 ILE B C   1 
ATOM   3030  O O   . ILE B 1 173 ? 38.145  -29.188 -37.770  1.00 22.03 ? 173 ILE B O   1 
ATOM   3031  C CB  . ILE B 1 173 ? 35.125  -30.241 -36.884  1.00 23.03 ? 173 ILE B CB  1 
ATOM   3032  C CG1 . ILE B 1 173 ? 34.432  -31.518 -36.415  1.00 23.15 ? 173 ILE B CG1 1 
ATOM   3033  C CG2 . ILE B 1 173 ? 35.213  -30.238 -38.411  1.00 23.80 ? 173 ILE B CG2 1 
ATOM   3034  C CD1 . ILE B 1 173 ? 35.130  -32.815 -36.813  1.00 23.42 ? 173 ILE B CD1 1 
ATOM   3035  N N   . ALA B 1 174 ? 36.961  -27.710 -36.562  1.00 21.89 ? 174 ALA B N   1 
ATOM   3036  C CA  . ALA B 1 174 ? 37.609  -26.531 -37.145  1.00 22.05 ? 174 ALA B CA  1 
ATOM   3037  C C   . ALA B 1 174 ? 39.089  -26.511 -36.803  1.00 22.54 ? 174 ALA B C   1 
ATOM   3038  O O   . ALA B 1 174 ? 39.947  -26.300 -37.669  1.00 21.31 ? 174 ALA B O   1 
ATOM   3039  C CB  . ALA B 1 174 ? 36.948  -25.270 -36.638  1.00 21.85 ? 174 ALA B CB  1 
ATOM   3040  N N   . GLU B 1 175 ? 39.365  -26.747 -35.522  1.00 24.48 ? 175 GLU B N   1 
ATOM   3041  C CA  . GLU B 1 175 ? 40.725  -26.839 -35.010  1.00 25.89 ? 175 GLU B CA  1 
ATOM   3042  C C   . GLU B 1 175 ? 41.491  -27.950 -35.730  1.00 25.72 ? 175 GLU B C   1 
ATOM   3043  O O   . GLU B 1 175 ? 42.630  -27.745 -36.128  1.00 27.09 ? 175 GLU B O   1 
ATOM   3044  C CB  . GLU B 1 175 ? 40.710  -27.098 -33.505  1.00 28.80 ? 175 GLU B CB  1 
ATOM   3045  C CG  . GLU B 1 175 ? 41.627  -26.195 -32.681  1.00 31.82 ? 175 GLU B CG  1 
ATOM   3046  C CD  . GLU B 1 175 ? 40.963  -25.775 -31.366  1.00 36.08 ? 175 GLU B CD  1 
ATOM   3047  O OE1 . GLU B 1 175 ? 41.123  -26.537 -30.388  1.00 40.04 ? 175 GLU B OE1 1 
ATOM   3048  O OE2 . GLU B 1 175 ? 40.250  -24.721 -31.299  1.00 36.35 ? 175 GLU B OE2 1 
ATOM   3049  N N   . ALA B 1 176 ? 40.866  -29.116 -35.915  1.00 24.81 ? 176 ALA B N   1 
ATOM   3050  C CA  . ALA B 1 176 ? 41.525  -30.243 -36.586  1.00 24.65 ? 176 ALA B CA  1 
ATOM   3051  C C   . ALA B 1 176 ? 41.910  -29.905 -38.020  1.00 23.32 ? 176 ALA B C   1 
ATOM   3052  O O   . ALA B 1 176 ? 42.883  -30.416 -38.538  1.00 22.03 ? 176 ALA B O   1 
ATOM   3053  C CB  . ALA B 1 176 ? 40.624  -31.471 -36.576  1.00 25.19 ? 176 ALA B CB  1 
ATOM   3054  N N   . ALA B 1 177 ? 41.119  -29.046 -38.648  1.00 23.13 ? 177 ALA B N   1 
ATOM   3055  C CA  . ALA B 1 177 ? 41.360  -28.596 -40.010  1.00 22.47 ? 177 ALA B CA  1 
ATOM   3056  C C   . ALA B 1 177 ? 42.356  -27.429 -40.090  1.00 22.51 ? 177 ALA B C   1 
ATOM   3057  O O   . ALA B 1 177 ? 42.631  -26.943 -41.181  1.00 22.92 ? 177 ALA B O   1 
ATOM   3058  C CB  . ALA B 1 177 ? 40.046  -28.168 -40.645  1.00 21.36 ? 177 ALA B CB  1 
ATOM   3059  N N   . GLY B 1 178 ? 42.858  -26.960 -38.949  1.00 21.64 ? 178 GLY B N   1 
ATOM   3060  C CA  . GLY B 1 178 ? 43.703  -25.785 -38.897  1.00 21.53 ? 178 GLY B CA  1 
ATOM   3061  C C   . GLY B 1 178 ? 43.000  -24.507 -39.318  1.00 22.65 ? 178 GLY B C   1 
ATOM   3062  O O   . GLY B 1 178 ? 43.603  -23.655 -39.998  1.00 25.01 ? 178 GLY B O   1 
ATOM   3063  N N   . GLU B 1 179 ? 41.727  -24.362 -38.923  1.00 21.71 ? 179 GLU B N   1 
ATOM   3064  C CA  . GLU B 1 179 ? 40.903  -23.226 -39.327  1.00 20.42 ? 179 GLU B CA  1 
ATOM   3065  C C   . GLU B 1 179 ? 40.274  -22.598 -38.088  1.00 18.15 ? 179 GLU B C   1 
ATOM   3066  O O   . GLU B 1 179 ? 40.571  -23.015 -36.982  1.00 17.61 ? 179 GLU B O   1 
ATOM   3067  C CB  . GLU B 1 179 ? 39.837  -23.690 -40.324  1.00 22.01 ? 179 GLU B CB  1 
ATOM   3068  C CG  . GLU B 1 179 ? 40.397  -24.303 -41.599  1.00 23.73 ? 179 GLU B CG  1 
ATOM   3069  C CD  . GLU B 1 179 ? 41.004  -23.303 -42.572  1.00 25.32 ? 179 GLU B CD  1 
ATOM   3070  O OE1 . GLU B 1 179 ? 41.492  -23.722 -43.646  1.00 27.27 ? 179 GLU B OE1 1 
ATOM   3071  O OE2 . GLU B 1 179 ? 40.996  -22.099 -42.281  1.00 26.24 ? 179 GLU B OE2 1 
ATOM   3072  N N   . SER B 1 180 ? 39.409  -21.607 -38.256  1.00 16.58 ? 180 SER B N   1 
ATOM   3073  C CA  . SER B 1 180 ? 38.884  -20.871 -37.119  1.00 15.99 ? 180 SER B CA  1 
ATOM   3074  C C   . SER B 1 180 ? 37.452  -21.234 -36.766  1.00 15.57 ? 180 SER B C   1 
ATOM   3075  O O   . SER B 1 180 ? 36.717  -21.778 -37.587  1.00 15.36 ? 180 SER B O   1 
ATOM   3076  C CB  . SER B 1 180 ? 38.976  -19.378 -37.397  1.00 15.97 ? 180 SER B CB  1 
ATOM   3077  O OG  . SER B 1 180 ? 40.229  -19.067 -37.949  1.00 15.58 ? 180 SER B OG  1 
ATOM   3078  N N   . PHE B 1 181 ? 37.069  -20.889 -35.533  1.00 15.21 ? 181 PHE B N   1 
ATOM   3079  C CA  . PHE B 1 181 ? 35.750  -21.197 -34.982  1.00 14.80 ? 181 PHE B CA  1 
ATOM   3080  C C   . PHE B 1 181 ? 35.136  -20.017 -34.241  1.00 14.86 ? 181 PHE B C   1 
ATOM   3081  O O   . PHE B 1 181 ? 35.837  -19.223 -33.665  1.00 15.12 ? 181 PHE B O   1 
ATOM   3082  C CB  . PHE B 1 181 ? 35.844  -22.364 -34.011  1.00 14.38 ? 181 PHE B CB  1 
ATOM   3083  C CG  . PHE B 1 181 ? 34.595  -22.567 -33.214  1.00 14.34 ? 181 PHE B CG  1 
ATOM   3084  C CD1 . PHE B 1 181 ? 33.451  -23.045 -33.829  1.00 14.31 ? 181 PHE B CD1 1 
ATOM   3085  C CD2 . PHE B 1 181 ? 34.542  -22.242 -31.864  1.00 14.10 ? 181 PHE B CD2 1 
ATOM   3086  C CE1 . PHE B 1 181 ? 32.284  -23.216 -33.113  1.00 14.13 ? 181 PHE B CE1 1 
ATOM   3087  C CE2 . PHE B 1 181 ? 33.378  -22.422 -31.147  1.00 13.83 ? 181 PHE B CE2 1 
ATOM   3088  C CZ  . PHE B 1 181 ? 32.250  -22.910 -31.768  1.00 14.07 ? 181 PHE B CZ  1 
ATOM   3089  N N   . PHE B 1 182 ? 33.815  -19.919 -34.256  1.00 15.74 ? 182 PHE B N   1 
ATOM   3090  C CA  . PHE B 1 182 ? 33.084  -18.954 -33.440  1.00 16.53 ? 182 PHE B CA  1 
ATOM   3091  C C   . PHE B 1 182 ? 31.686  -19.470 -33.129  1.00 16.99 ? 182 PHE B C   1 
ATOM   3092  O O   . PHE B 1 182 ? 30.991  -19.965 -34.010  1.00 16.89 ? 182 PHE B O   1 
ATOM   3093  C CB  . PHE B 1 182 ? 32.984  -17.612 -34.146  1.00 17.44 ? 182 PHE B CB  1 
ATOM   3094  C CG  . PHE B 1 182 ? 32.265  -16.551 -33.340  1.00 18.05 ? 182 PHE B CG  1 
ATOM   3095  C CD1 . PHE B 1 182 ? 32.921  -15.854 -32.330  1.00 18.03 ? 182 PHE B CD1 1 
ATOM   3096  C CD2 . PHE B 1 182 ? 30.924  -16.249 -33.593  1.00 18.16 ? 182 PHE B CD2 1 
ATOM   3097  C CE1 . PHE B 1 182 ? 32.266  -14.883 -31.607  1.00 18.23 ? 182 PHE B CE1 1 
ATOM   3098  C CE2 . PHE B 1 182 ? 30.265  -15.274 -32.865  1.00 17.83 ? 182 PHE B CE2 1 
ATOM   3099  C CZ  . PHE B 1 182 ? 30.941  -14.594 -31.876  1.00 18.08 ? 182 PHE B CZ  1 
ATOM   3100  N N   . ASP B 1 183 ? 31.286  -19.348 -31.867  1.00 17.69 ? 183 ASP B N   1 
ATOM   3101  C CA  . ASP B 1 183 ? 29.995  -19.840 -31.415  1.00 18.53 ? 183 ASP B CA  1 
ATOM   3102  C C   . ASP B 1 183 ? 28.986  -18.705 -31.381  1.00 19.21 ? 183 ASP B C   1 
ATOM   3103  O O   . ASP B 1 183 ? 29.031  -17.848 -30.504  1.00 19.86 ? 183 ASP B O   1 
ATOM   3104  C CB  . ASP B 1 183 ? 30.150  -20.442 -30.023  1.00 18.81 ? 183 ASP B CB  1 
ATOM   3105  C CG  . ASP B 1 183 ? 28.854  -21.001 -29.474  1.00 19.55 ? 183 ASP B CG  1 
ATOM   3106  O OD1 . ASP B 1 183 ? 27.827  -21.059 -30.193  1.00 20.51 ? 183 ASP B OD1 1 
ATOM   3107  O OD2 . ASP B 1 183 ? 28.875  -21.383 -28.292  1.00 19.81 ? 183 ASP B OD2 1 
ATOM   3108  N N   . ALA B 1 184 ? 28.054  -18.698 -32.322  1.00 19.83 ? 184 ALA B N   1 
ATOM   3109  C CA  . ALA B 1 184 ? 27.031  -17.661 -32.337  1.00 20.24 ? 184 ALA B CA  1 
ATOM   3110  C C   . ALA B 1 184 ? 26.246  -17.633 -31.017  1.00 20.47 ? 184 ALA B C   1 
ATOM   3111  O O   . ALA B 1 184 ? 25.790  -16.579 -30.581  1.00 20.59 ? 184 ALA B O   1 
ATOM   3112  C CB  . ALA B 1 184 ? 26.105  -17.867 -33.516  1.00 20.69 ? 184 ALA B CB  1 
ATOM   3113  N N   . GLY B 1 185 ? 26.111  -18.791 -30.377  1.00 21.28 ? 185 GLY B N   1 
ATOM   3114  C CA  . GLY B 1 185 ? 25.459  -18.890 -29.075  1.00 22.15 ? 185 GLY B CA  1 
ATOM   3115  C C   . GLY B 1 185 ? 26.138  -18.133 -27.937  1.00 22.30 ? 185 GLY B C   1 
ATOM   3116  O O   . GLY B 1 185 ? 25.530  -17.923 -26.885  1.00 22.04 ? 185 GLY B O   1 
ATOM   3117  N N   . SER B 1 186 ? 27.390  -17.728 -28.133  1.00 22.76 ? 186 SER B N   1 
ATOM   3118  C CA  . SER B 1 186 ? 28.112  -16.948 -27.133  1.00 23.78 ? 186 SER B CA  1 
ATOM   3119  C C   . SER B 1 186 ? 27.654  -15.480 -27.071  1.00 23.79 ? 186 SER B C   1 
ATOM   3120  O O   . SER B 1 186 ? 27.900  -14.805 -26.079  1.00 22.65 ? 186 SER B O   1 
ATOM   3121  C CB  . SER B 1 186 ? 29.623  -17.007 -27.390  1.00 24.08 ? 186 SER B CB  1 
ATOM   3122  O OG  . SER B 1 186 ? 30.007  -16.086 -28.397  1.00 24.57 ? 186 SER B OG  1 
ATOM   3123  N N   . VAL B 1 187 ? 27.003  -14.994 -28.125  1.00 25.25 ? 187 VAL B N   1 
ATOM   3124  C CA  . VAL B 1 187 ? 26.564  -13.591 -28.188  1.00 26.69 ? 187 VAL B CA  1 
ATOM   3125  C C   . VAL B 1 187 ? 25.071  -13.384 -28.461  1.00 25.85 ? 187 VAL B C   1 
ATOM   3126  O O   . VAL B 1 187 ? 24.589  -12.276 -28.278  1.00 25.16 ? 187 VAL B O   1 
ATOM   3127  C CB  . VAL B 1 187 ? 27.367  -12.804 -29.253  1.00 28.44 ? 187 VAL B CB  1 
ATOM   3128  C CG1 . VAL B 1 187 ? 28.835  -12.720 -28.861  1.00 28.89 ? 187 VAL B CG1 1 
ATOM   3129  C CG2 . VAL B 1 187 ? 27.240  -13.452 -30.632  1.00 29.10 ? 187 VAL B CG2 1 
ATOM   3130  N N   . VAL B 1 188 ? 24.364  -14.418 -28.931  1.00 25.56 ? 188 VAL B N   1 
ATOM   3131  C CA  . VAL B 1 188 ? 22.924  -14.342 -29.206  1.00 25.76 ? 188 VAL B CA  1 
ATOM   3132  C C   . VAL B 1 188 ? 22.219  -15.685 -28.982  1.00 26.70 ? 188 VAL B C   1 
ATOM   3133  O O   . VAL B 1 188 ? 22.861  -16.732 -28.817  1.00 27.06 ? 188 VAL B O   1 
ATOM   3134  C CB  . VAL B 1 188 ? 22.622  -13.943 -30.667  1.00 27.30 ? 188 VAL B CB  1 
ATOM   3135  C CG1 . VAL B 1 188 ? 23.296  -12.621 -31.048  1.00 27.80 ? 188 VAL B CG1 1 
ATOM   3136  C CG2 . VAL B 1 188 ? 23.006  -15.066 -31.645  1.00 27.68 ? 188 VAL B CG2 1 
ATOM   3137  N N   . SER B 1 189 ? 20.885  -15.648 -28.990  1.00 26.47 ? 189 SER B N   1 
ATOM   3138  C CA  . SER B 1 189 ? 20.065  -16.862 -28.933  1.00 24.81 ? 189 SER B CA  1 
ATOM   3139  C C   . SER B 1 189 ? 18.872  -16.748 -29.872  1.00 24.56 ? 189 SER B C   1 
ATOM   3140  O O   . SER B 1 189 ? 18.585  -15.670 -30.428  1.00 24.44 ? 189 SER B O   1 
ATOM   3141  C CB  . SER B 1 189 ? 19.558  -17.129 -27.521  1.00 23.39 ? 189 SER B CB  1 
ATOM   3142  O OG  . SER B 1 189 ? 20.242  -16.426 -26.512  1.00 21.68 ? 189 SER B OG  1 
ATOM   3143  N N   . THR B 1 190 ? 18.222  -17.889 -30.104  1.00 24.61 ? 190 THR B N   1 
ATOM   3144  C CA  . THR B 1 190 ? 17.142  -17.950 -31.077  1.00 24.64 ? 190 THR B CA  1 
ATOM   3145  C C   . THR B 1 190 ? 15.894  -17.312 -30.453  1.00 24.03 ? 190 THR B C   1 
ATOM   3146  O O   . THR B 1 190 ? 15.124  -17.963 -29.741  1.00 23.54 ? 190 THR B O   1 
ATOM   3147  C CB  . THR B 1 190 ? 16.894  -19.387 -31.578  1.00 24.62 ? 190 THR B CB  1 
ATOM   3148  O OG1 . THR B 1 190 ? 18.134  -19.963 -32.000  1.00 24.11 ? 190 THR B OG1 1 
ATOM   3149  C CG2 . THR B 1 190 ? 15.948  -19.405 -32.759  1.00 24.48 ? 190 THR B CG2 1 
ATOM   3150  N N   . ASP B 1 191 ? 15.726  -16.022 -30.727  1.00 23.37 ? 191 ASP B N   1 
ATOM   3151  C CA  . ASP B 1 191 ? 14.661  -15.221 -30.133  1.00 22.26 ? 191 ASP B CA  1 
ATOM   3152  C C   . ASP B 1 191 ? 13.465  -15.016 -31.063  1.00 20.85 ? 191 ASP B C   1 
ATOM   3153  O O   . ASP B 1 191 ? 12.503  -14.384 -30.689  1.00 19.51 ? 191 ASP B O   1 
ATOM   3154  C CB  . ASP B 1 191 ? 15.210  -13.856 -29.703  1.00 22.30 ? 191 ASP B CB  1 
ATOM   3155  C CG  . ASP B 1 191 ? 15.580  -12.980 -30.877  1.00 22.84 ? 191 ASP B CG  1 
ATOM   3156  O OD1 . ASP B 1 191 ? 15.935  -13.532 -31.957  1.00 24.13 ? 191 ASP B OD1 1 
ATOM   3157  O OD2 . ASP B 1 191 ? 15.522  -11.740 -30.720  1.00 22.05 ? 191 ASP B OD2 1 
ATOM   3158  N N   . GLY B 1 192 ? 13.514  -15.547 -32.269  1.00 20.93 ? 192 GLY B N   1 
ATOM   3159  C CA  . GLY B 1 192 ? 12.366  -15.426 -33.155  1.00 21.96 ? 192 GLY B CA  1 
ATOM   3160  C C   . GLY B 1 192 ? 11.144  -16.130 -32.593  1.00 21.84 ? 192 GLY B C   1 
ATOM   3161  O O   . GLY B 1 192 ? 11.250  -17.135 -31.869  1.00 21.11 ? 192 GLY B O   1 
ATOM   3162  N N   . VAL B 1 193 ? 9.979   -15.589 -32.934  1.00 21.40 ? 193 VAL B N   1 
ATOM   3163  C CA  . VAL B 1 193 ? 8.721   -16.103 -32.393  1.00 20.76 ? 193 VAL B CA  1 
ATOM   3164  C C   . VAL B 1 193 ? 8.470   -17.577 -32.760  1.00 20.63 ? 193 VAL B C   1 
ATOM   3165  O O   . VAL B 1 193 ? 7.818   -18.280 -32.005  1.00 19.69 ? 193 VAL B O   1 
ATOM   3166  C CB  . VAL B 1 193 ? 7.531   -15.215 -32.834  1.00 20.42 ? 193 VAL B CB  1 
ATOM   3167  C CG1 . VAL B 1 193 ? 7.210   -15.408 -34.332  1.00 21.02 ? 193 VAL B CG1 1 
ATOM   3168  C CG2 . VAL B 1 193 ? 6.329   -15.493 -31.957  1.00 20.55 ? 193 VAL B CG2 1 
ATOM   3169  N N   . ASP B 1 194 ? 8.994   -18.043 -33.903  1.00 21.05 ? 194 ASP B N   1 
ATOM   3170  C CA  . ASP B 1 194 ? 8.770   -19.423 -34.357  1.00 20.37 ? 194 ASP B CA  1 
ATOM   3171  C C   . ASP B 1 194 ? 9.743   -20.432 -33.739  1.00 20.44 ? 194 ASP B C   1 
ATOM   3172  O O   . ASP B 1 194 ? 9.676   -21.627 -34.039  1.00 20.91 ? 194 ASP B O   1 
ATOM   3173  C CB  . ASP B 1 194 ? 8.780   -19.536 -35.898  1.00 20.09 ? 194 ASP B CB  1 
ATOM   3174  C CG  . ASP B 1 194 ? 10.088  -19.028 -36.558  1.00 20.00 ? 194 ASP B CG  1 
ATOM   3175  O OD1 . ASP B 1 194 ? 11.094  -18.854 -35.853  1.00 18.84 ? 194 ASP B OD1 1 
ATOM   3176  O OD2 . ASP B 1 194 ? 10.081  -18.786 -37.800  1.00 20.89 ? 194 ASP B OD2 1 
ATOM   3177  N N   . GLY B 1 195 ? 10.652  -19.958 -32.893  1.00 20.70 ? 195 GLY B N   1 
ATOM   3178  C CA  . GLY B 1 195 ? 11.609  -20.831 -32.208  1.00 20.66 ? 195 GLY B CA  1 
ATOM   3179  C C   . GLY B 1 195 ? 12.806  -21.273 -33.038  1.00 20.45 ? 195 GLY B C   1 
ATOM   3180  O O   . GLY B 1 195 ? 13.562  -22.107 -32.588  1.00 20.10 ? 195 GLY B O   1 
ATOM   3181  N N   . ILE B 1 196 ? 12.975  -20.723 -34.236  1.00 21.73 ? 196 ILE B N   1 
ATOM   3182  C CA  . ILE B 1 196 ? 14.053  -21.130 -35.146  1.00 22.72 ? 196 ILE B CA  1 
ATOM   3183  C C   . ILE B 1 196 ? 14.886  -19.975 -35.714  1.00 22.59 ? 196 ILE B C   1 
ATOM   3184  O O   . ILE B 1 196 ? 16.108  -20.106 -35.807  1.00 22.58 ? 196 ILE B O   1 
ATOM   3185  C CB  . ILE B 1 196 ? 13.487  -21.971 -36.315  1.00 23.64 ? 196 ILE B CB  1 
ATOM   3186  C CG1 . ILE B 1 196 ? 12.954  -23.306 -35.780  1.00 23.66 ? 196 ILE B CG1 1 
ATOM   3187  C CG2 . ILE B 1 196 ? 14.551  -22.241 -37.382  1.00 23.80 ? 196 ILE B CG2 1 
ATOM   3188  C CD1 . ILE B 1 196 ? 11.804  -23.830 -36.598  1.00 23.93 ? 196 ILE B CD1 1 
ATOM   3189  N N   . HIS B 1 197 ? 14.241  -18.868 -36.074  1.00 21.90 ? 197 HIS B N   1 
ATOM   3190  C CA  . HIS B 1 197 ? 14.916  -17.772 -36.776  1.00 21.77 ? 197 HIS B CA  1 
ATOM   3191  C C   . HIS B 1 197 ? 15.141  -16.546 -35.905  1.00 21.31 ? 197 HIS B C   1 
ATOM   3192  O O   . HIS B 1 197 ? 14.775  -16.548 -34.729  1.00 21.00 ? 197 HIS B O   1 
ATOM   3193  C CB  . HIS B 1 197 ? 14.131  -17.415 -38.030  1.00 21.73 ? 197 HIS B CB  1 
ATOM   3194  C CG  . HIS B 1 197 ? 13.862  -18.605 -38.884  1.00 20.93 ? 197 HIS B CG  1 
ATOM   3195  N ND1 . HIS B 1 197 ? 12.644  -19.245 -38.898  1.00 21.19 ? 197 HIS B ND1 1 
ATOM   3196  C CD2 . HIS B 1 197 ? 14.676  -19.315 -39.698  1.00 20.19 ? 197 HIS B CD2 1 
ATOM   3197  C CE1 . HIS B 1 197 ? 12.709  -20.279 -39.715  1.00 20.52 ? 197 HIS B CE1 1 
ATOM   3198  N NE2 . HIS B 1 197 ? 13.931  -20.343 -40.211  1.00 19.90 ? 197 HIS B NE2 1 
ATOM   3199  N N   . PHE B 1 198 ? 15.788  -15.526 -36.476  1.00 20.33 ? 198 PHE B N   1 
ATOM   3200  C CA  . PHE B 1 198 ? 16.283  -14.393 -35.695  1.00 20.05 ? 198 PHE B CA  1 
ATOM   3201  C C   . PHE B 1 198 ? 15.493  -13.113 -35.960  1.00 20.64 ? 198 PHE B C   1 
ATOM   3202  O O   . PHE B 1 198 ? 15.034  -12.852 -37.076  1.00 20.21 ? 198 PHE B O   1 
ATOM   3203  C CB  . PHE B 1 198 ? 17.758  -14.089 -36.025  1.00 19.28 ? 198 PHE B CB  1 
ATOM   3204  C CG  . PHE B 1 198 ? 18.732  -15.210 -35.741  1.00 18.90 ? 198 PHE B CG  1 
ATOM   3205  C CD1 . PHE B 1 198 ? 18.417  -16.280 -34.900  1.00 18.74 ? 198 PHE B CD1 1 
ATOM   3206  C CD2 . PHE B 1 198 ? 20.005  -15.157 -36.278  1.00 18.73 ? 198 PHE B CD2 1 
ATOM   3207  C CE1 . PHE B 1 198 ? 19.340  -17.284 -34.643  1.00 18.00 ? 198 PHE B CE1 1 
ATOM   3208  C CE2 . PHE B 1 198 ? 20.929  -16.165 -36.028  1.00 18.45 ? 198 PHE B CE2 1 
ATOM   3209  C CZ  . PHE B 1 198 ? 20.594  -17.222 -35.205  1.00 17.91 ? 198 PHE B CZ  1 
ATOM   3210  N N   . THR B 1 199 ? 15.387  -12.294 -34.926  1.00 22.50 ? 199 THR B N   1 
ATOM   3211  C CA  . THR B 1 199 ? 14.874  -10.937 -35.063  1.00 24.62 ? 199 THR B CA  1 
ATOM   3212  C C   . THR B 1 199 ? 15.976  -10.046 -35.614  1.00 27.10 ? 199 THR B C   1 
ATOM   3213  O O   . THR B 1 199 ? 17.143  -10.445 -35.650  1.00 27.82 ? 199 THR B O   1 
ATOM   3214  C CB  . THR B 1 199 ? 14.476  -10.343 -33.700  1.00 23.98 ? 199 THR B CB  1 
ATOM   3215  O OG1 . THR B 1 199 ? 15.645  -10.216 -32.873  1.00 21.79 ? 199 THR B OG1 1 
ATOM   3216  C CG2 . THR B 1 199 ? 13.425  -11.222 -33.021  1.00 23.55 ? 199 THR B CG2 1 
ATOM   3217  N N   . ALA B 1 200 ? 15.612  -8.829  -36.014  1.00 28.15 ? 200 ALA B N   1 
ATOM   3218  C CA  . ALA B 1 200 ? 16.595  -7.874  -36.504  1.00 28.25 ? 200 ALA B CA  1 
ATOM   3219  C C   . ALA B 1 200 ? 17.561  -7.450  -35.395  1.00 30.57 ? 200 ALA B C   1 
ATOM   3220  O O   . ALA B 1 200 ? 18.735  -7.182  -35.670  1.00 32.02 ? 200 ALA B O   1 
ATOM   3221  C CB  . ALA B 1 200 ? 15.902  -6.680  -37.105  1.00 28.16 ? 200 ALA B CB  1 
ATOM   3222  N N   . GLU B 1 201 ? 17.079  -7.403  -34.156  1.00 33.37 ? 201 GLU B N   1 
ATOM   3223  C CA  . GLU B 1 201 ? 17.945  -7.083  -33.027  1.00 36.01 ? 201 GLU B CA  1 
ATOM   3224  C C   . GLU B 1 201 ? 19.049  -8.142  -32.873  1.00 33.51 ? 201 GLU B C   1 
ATOM   3225  O O   . GLU B 1 201 ? 20.211  -7.799  -32.651  1.00 34.52 ? 201 GLU B O   1 
ATOM   3226  C CB  . GLU B 1 201 ? 17.152  -6.937  -31.696  1.00 40.24 ? 201 GLU B CB  1 
ATOM   3227  C CG  . GLU B 1 201 ? 17.993  -6.385  -30.534  1.00 46.73 ? 201 GLU B CG  1 
ATOM   3228  C CD  . GLU B 1 201 ? 17.726  -7.007  -29.137  1.00 50.21 ? 201 GLU B CD  1 
ATOM   3229  O OE1 . GLU B 1 201 ? 18.706  -7.158  -28.363  1.00 48.84 ? 201 GLU B OE1 1 
ATOM   3230  O OE2 . GLU B 1 201 ? 16.562  -7.343  -28.833  1.00 50.97 ? 201 GLU B OE2 1 
ATOM   3231  N N   . THR B 1 202 ? 18.692  -9.414  -33.018  1.00 31.61 ? 202 THR B N   1 
ATOM   3232  C CA  . THR B 1 202 ? 19.664  -10.502 -32.895  1.00 30.93 ? 202 THR B CA  1 
ATOM   3233  C C   . THR B 1 202 ? 20.641  -10.503 -34.062  1.00 29.84 ? 202 THR B C   1 
ATOM   3234  O O   . THR B 1 202 ? 21.830  -10.764 -33.883  1.00 28.04 ? 202 THR B O   1 
ATOM   3235  C CB  . THR B 1 202 ? 18.960  -11.874 -32.800  1.00 31.51 ? 202 THR B CB  1 
ATOM   3236  O OG1 . THR B 1 202 ? 18.348  -12.007 -31.511  1.00 29.92 ? 202 THR B OG1 1 
ATOM   3237  C CG2 . THR B 1 202 ? 19.936  -13.022 -32.994  1.00 31.26 ? 202 THR B CG2 1 
ATOM   3238  N N   . ASN B 1 203 ? 20.138  -10.218 -35.260  1.00 29.37 ? 203 ASN B N   1 
ATOM   3239  C CA  . ASN B 1 203 ? 21.005  -10.085 -36.431  1.00 29.90 ? 203 ASN B CA  1 
ATOM   3240  C C   . ASN B 1 203 ? 22.075  -9.041  -36.203  1.00 30.76 ? 203 ASN B C   1 
ATOM   3241  O O   . ASN B 1 203 ? 23.247  -9.283  -36.487  1.00 29.88 ? 203 ASN B O   1 
ATOM   3242  C CB  . ASN B 1 203 ? 20.189  -9.692  -37.675  1.00 29.73 ? 203 ASN B CB  1 
ATOM   3243  C CG  . ASN B 1 203 ? 19.464  -10.864 -38.306  1.00 29.22 ? 203 ASN B CG  1 
ATOM   3244  O OD1 . ASN B 1 203 ? 19.698  -12.029 -37.984  1.00 29.23 ? 203 ASN B OD1 1 
ATOM   3245  N ND2 . ASN B 1 203 ? 18.590  -10.549 -39.229  1.00 29.45 ? 203 ASN B ND2 1 
ATOM   3246  N N   . ARG B 1 204 ? 21.661  -7.876  -35.693  1.00 31.61 ? 204 ARG B N   1 
ATOM   3247  C CA  . ARG B 1 204 ? 22.583  -6.764  -35.433  1.00 31.60 ? 204 ARG B CA  1 
ATOM   3248  C C   . ARG B 1 204 ? 23.699  -7.168  -34.483  1.00 28.43 ? 204 ARG B C   1 
ATOM   3249  O O   . ARG B 1 204 ? 24.866  -6.887  -34.751  1.00 26.69 ? 204 ARG B O   1 
ATOM   3250  C CB  . ARG B 1 204 ? 21.833  -5.545  -34.887  1.00 33.11 ? 204 ARG B CB  1 
ATOM   3251  C CG  . ARG B 1 204 ? 21.406  -4.549  -35.966  1.00 34.15 ? 204 ARG B CG  1 
ATOM   3252  C CD  . ARG B 1 204 ? 20.788  -3.282  -35.372  1.00 35.59 ? 204 ARG B CD  1 
ATOM   3253  N NE  . ARG B 1 204 ? 19.382  -3.499  -34.996  1.00 36.01 ? 204 ARG B NE  1 
ATOM   3254  C CZ  . ARG B 1 204 ? 18.349  -3.486  -35.845  1.00 35.41 ? 204 ARG B CZ  1 
ATOM   3255  N NH1 . ARG B 1 204 ? 18.534  -3.208  -37.134  1.00 36.09 ? 204 ARG B NH1 1 
ATOM   3256  N NH2 . ARG B 1 204 ? 17.123  -3.699  -35.401  1.00 33.73 ? 204 ARG B NH2 1 
ATOM   3257  N N   . THR B 1 205 ? 23.345  -7.825  -33.383  1.00 25.83 ? 205 THR B N   1 
ATOM   3258  C CA  . THR B 1 205 ? 24.345  -8.264  -32.414  1.00 25.50 ? 205 THR B CA  1 
ATOM   3259  C C   . THR B 1 205 ? 25.338  -9.222  -33.075  1.00 25.87 ? 205 THR B C   1 
ATOM   3260  O O   . THR B 1 205 ? 26.545  -9.053  -32.937  1.00 26.59 ? 205 THR B O   1 
ATOM   3261  C CB  . THR B 1 205 ? 23.690  -8.939  -31.196  1.00 24.43 ? 205 THR B CB  1 
ATOM   3262  O OG1 . THR B 1 205 ? 22.688  -8.068  -30.678  1.00 25.19 ? 205 THR B OG1 1 
ATOM   3263  C CG2 . THR B 1 205 ? 24.702  -9.230  -30.101  1.00 23.73 ? 205 THR B CG2 1 
ATOM   3264  N N   . LEU B 1 206 ? 24.816  -10.212 -33.802  1.00 25.12 ? 206 LEU B N   1 
ATOM   3265  C CA  . LEU B 1 206 ? 25.646  -11.240 -34.455  1.00 23.72 ? 206 LEU B CA  1 
ATOM   3266  C C   . LEU B 1 206 ? 26.574  -10.636 -35.496  1.00 23.37 ? 206 LEU B C   1 
ATOM   3267  O O   . LEU B 1 206 ? 27.749  -10.973 -35.548  1.00 23.70 ? 206 LEU B O   1 
ATOM   3268  C CB  . LEU B 1 206 ? 24.764  -12.310 -35.105  1.00 23.53 ? 206 LEU B CB  1 
ATOM   3269  C CG  . LEU B 1 206 ? 25.473  -13.484 -35.796  1.00 22.73 ? 206 LEU B CG  1 
ATOM   3270  C CD1 . LEU B 1 206 ? 26.379  -14.199 -34.824  1.00 22.24 ? 206 LEU B CD1 1 
ATOM   3271  C CD2 . LEU B 1 206 ? 24.491  -14.467 -36.385  1.00 22.54 ? 206 LEU B CD2 1 
ATOM   3272  N N   . GLY B 1 207 ? 26.038  -9.749  -36.327  1.00 22.94 ? 207 GLY B N   1 
ATOM   3273  C CA  . GLY B 1 207 ? 26.825  -9.075  -37.364  1.00 22.40 ? 207 GLY B CA  1 
ATOM   3274  C C   . GLY B 1 207 ? 28.016  -8.351  -36.794  1.00 21.82 ? 207 GLY B C   1 
ATOM   3275  O O   . GLY B 1 207 ? 29.127  -8.449  -37.313  1.00 19.80 ? 207 GLY B O   1 
ATOM   3276  N N   . ALA B 1 208 ? 27.781  -7.629  -35.705  1.00 22.97 ? 208 ALA B N   1 
ATOM   3277  C CA  . ALA B 1 208 ? 28.823  -6.827  -35.061  1.00 22.84 ? 208 ALA B CA  1 
ATOM   3278  C C   . ALA B 1 208 ? 29.849  -7.707  -34.395  1.00 22.77 ? 208 ALA B C   1 
ATOM   3279  O O   . ALA B 1 208 ? 31.029  -7.416  -34.470  1.00 24.63 ? 208 ALA B O   1 
ATOM   3280  C CB  . ALA B 1 208 ? 28.211  -5.852  -34.053  1.00 23.21 ? 208 ALA B CB  1 
ATOM   3281  N N   . ALA B 1 209 ? 29.401  -8.783  -33.752  1.00 22.21 ? 209 ALA B N   1 
ATOM   3282  C CA  . ALA B 1 209 ? 30.294  -9.733  -33.085  1.00 22.11 ? 209 ALA B CA  1 
ATOM   3283  C C   . ALA B 1 209 ? 31.152  -10.463 -34.095  1.00 22.61 ? 209 ALA B C   1 
ATOM   3284  O O   . ALA B 1 209 ? 32.331  -10.622 -33.890  1.00 24.08 ? 209 ALA B O   1 
ATOM   3285  C CB  . ALA B 1 209 ? 29.496  -10.735 -32.261  1.00 21.57 ? 209 ALA B CB  1 
ATOM   3286  N N   . VAL B 1 210 ? 30.554  -10.928 -35.184  1.00 22.30 ? 210 VAL B N   1 
ATOM   3287  C CA  . VAL B 1 210 ? 31.294  -11.671 -36.209  1.00 22.39 ? 210 VAL B CA  1 
ATOM   3288  C C   . VAL B 1 210 ? 32.322  -10.770 -36.908  1.00 22.33 ? 210 VAL B C   1 
ATOM   3289  O O   . VAL B 1 210 ? 33.411  -11.224 -37.254  1.00 22.62 ? 210 VAL B O   1 
ATOM   3290  C CB  . VAL B 1 210 ? 30.354  -12.361 -37.215  1.00 22.06 ? 210 VAL B CB  1 
ATOM   3291  C CG1 . VAL B 1 210 ? 31.143  -12.977 -38.373  1.00 22.00 ? 210 VAL B CG1 1 
ATOM   3292  C CG2 . VAL B 1 210 ? 29.533  -13.438 -36.510  1.00 22.03 ? 210 VAL B CG2 1 
ATOM   3293  N N   . ALA B 1 211 ? 31.990  -9.498  -37.088  1.00 22.13 ? 211 ALA B N   1 
ATOM   3294  C CA  . ALA B 1 211 ? 32.926  -8.539  -37.668  1.00 23.31 ? 211 ALA B CA  1 
ATOM   3295  C C   . ALA B 1 211 ? 34.209  -8.401  -36.844  1.00 24.63 ? 211 ALA B C   1 
ATOM   3296  O O   . ALA B 1 211 ? 35.286  -8.287  -37.413  1.00 25.97 ? 211 ALA B O   1 
ATOM   3297  C CB  . ALA B 1 211 ? 32.261  -7.187  -37.836  1.00 23.39 ? 211 ALA B CB  1 
ATOM   3298  N N   . GLN B 1 212 ? 34.092  -8.404  -35.512  1.00 25.96 ? 212 GLN B N   1 
ATOM   3299  C CA  . GLN B 1 212 ? 35.252  -8.369  -34.608  1.00 27.64 ? 212 GLN B CA  1 
ATOM   3300  C C   . GLN B 1 212 ? 36.124  -9.587  -34.885  1.00 27.87 ? 212 GLN B C   1 
ATOM   3301  O O   . GLN B 1 212 ? 37.336  -9.472  -35.040  1.00 30.35 ? 212 GLN B O   1 
ATOM   3302  C CB  . GLN B 1 212 ? 34.781  -8.393  -33.140  1.00 30.30 ? 212 GLN B CB  1 
ATOM   3303  C CG  . GLN B 1 212 ? 35.553  -7.518  -32.188  1.00 33.15 ? 212 GLN B CG  1 
ATOM   3304  C CD  . GLN B 1 212 ? 36.946  -8.074  -31.899  1.00 38.00 ? 212 GLN B CD  1 
ATOM   3305  O OE1 . GLN B 1 212 ? 37.083  -9.216  -31.414  1.00 36.39 ? 212 GLN B OE1 1 
ATOM   3306  N NE2 . GLN B 1 212 ? 38.007  -7.248  -32.161  1.00 41.28 ? 212 GLN B NE2 1 
ATOM   3307  N N   . LYS B 1 213 ? 35.493  -10.752 -34.932  1.00 26.57 ? 213 LYS B N   1 
ATOM   3308  C CA  . LYS B 1 213 ? 36.190  -11.998 -35.154  1.00 25.41 ? 213 LYS B CA  1 
ATOM   3309  C C   . LYS B 1 213 ? 36.937  -11.991 -36.486  1.00 25.06 ? 213 LYS B C   1 
ATOM   3310  O O   . LYS B 1 213 ? 38.110  -12.370 -36.554  1.00 25.02 ? 213 LYS B O   1 
ATOM   3311  C CB  . LYS B 1 213 ? 35.193  -13.166 -35.098  1.00 25.07 ? 213 LYS B CB  1 
ATOM   3312  C CG  . LYS B 1 213 ? 35.824  -14.534 -35.233  1.00 24.74 ? 213 LYS B CG  1 
ATOM   3313  C CD  . LYS B 1 213 ? 36.911  -14.794 -34.193  1.00 24.77 ? 213 LYS B CD  1 
ATOM   3314  C CE  . LYS B 1 213 ? 37.184  -16.273 -34.069  1.00 24.22 ? 213 LYS B CE  1 
ATOM   3315  N NZ  . LYS B 1 213 ? 38.586  -16.617 -33.783  1.00 23.91 ? 213 LYS B NZ  1 
ATOM   3316  N N   . VAL B 1 214 ? 36.261  -11.541 -37.543  1.00 24.05 ? 214 VAL B N   1 
ATOM   3317  C CA  . VAL B 1 214 ? 36.861  -11.499 -38.874  1.00 23.10 ? 214 VAL B CA  1 
ATOM   3318  C C   . VAL B 1 214 ? 38.125  -10.650 -38.893  1.00 23.49 ? 214 VAL B C   1 
ATOM   3319  O O   . VAL B 1 214 ? 39.163  -11.097 -39.403  1.00 23.92 ? 214 VAL B O   1 
ATOM   3320  C CB  . VAL B 1 214 ? 35.858  -11.000 -39.927  1.00 22.78 ? 214 VAL B CB  1 
ATOM   3321  C CG1 . VAL B 1 214 ? 36.548  -10.677 -41.242  1.00 22.32 ? 214 VAL B CG1 1 
ATOM   3322  C CG2 . VAL B 1 214 ? 34.756  -12.030 -40.150  1.00 23.48 ? 214 VAL B CG2 1 
ATOM   3323  N N   . LYS B 1 215 ? 38.052  -9.438  -38.334  1.00 24.51 ? 215 LYS B N   1 
ATOM   3324  C CA  . LYS B 1 215 ? 39.205  -8.523  -38.286  1.00 25.06 ? 215 LYS B CA  1 
ATOM   3325  C C   . LYS B 1 215 ? 40.410  -9.129  -37.567  1.00 25.74 ? 215 LYS B C   1 
ATOM   3326  O O   . LYS B 1 215 ? 41.547  -8.927  -37.982  1.00 25.47 ? 215 LYS B O   1 
ATOM   3327  C CB  . LYS B 1 215 ? 38.832  -7.221  -37.623  1.00 25.01 ? 215 LYS B CB  1 
ATOM   3328  C CG  . LYS B 1 215 ? 37.923  -6.347  -38.491  1.00 26.85 ? 215 LYS B CG  1 
ATOM   3329  C CD  . LYS B 1 215 ? 37.920  -4.868  -38.162  1.00 29.69 ? 215 LYS B CD  1 
ATOM   3330  C CE  . LYS B 1 215 ? 36.516  -4.290  -38.349  1.00 30.99 ? 215 LYS B CE  1 
ATOM   3331  N NZ  . LYS B 1 215 ? 36.318  -2.937  -37.803  1.00 32.28 ? 215 LYS B NZ  1 
ATOM   3332  N N   . THR B 1 216 ? 40.156  -9.853  -36.486  1.00 27.04 ? 216 THR B N   1 
ATOM   3333  C CA  . THR B 1 216 ? 41.191  -10.632 -35.812  1.00 27.55 ? 216 THR B CA  1 
ATOM   3334  C C   . THR B 1 216 ? 41.930  -11.570 -36.775  1.00 27.72 ? 216 THR B C   1 
ATOM   3335  O O   . THR B 1 216 ? 43.151  -11.706 -36.688  1.00 28.81 ? 216 THR B O   1 
ATOM   3336  C CB  . THR B 1 216 ? 40.582  -11.470 -34.666  1.00 28.42 ? 216 THR B CB  1 
ATOM   3337  O OG1 . THR B 1 216 ? 40.179  -10.594 -33.619  1.00 28.03 ? 216 THR B OG1 1 
ATOM   3338  C CG2 . THR B 1 216 ? 41.577  -12.506 -34.110  1.00 29.44 ? 216 THR B CG2 1 
ATOM   3339  N N   . LEU B 1 217 ? 41.192  -12.221 -37.677  1.00 26.48 ? 217 LEU B N   1 
ATOM   3340  C CA  . LEU B 1 217 ? 41.790  -13.175 -38.609  1.00 26.37 ? 217 LEU B CA  1 
ATOM   3341  C C   . LEU B 1 217 ? 42.499  -12.541 -39.800  1.00 25.98 ? 217 LEU B C   1 
ATOM   3342  O O   . LEU B 1 217 ? 43.531  -13.027 -40.228  1.00 23.00 ? 217 LEU B O   1 
ATOM   3343  C CB  . LEU B 1 217 ? 40.724  -14.149 -39.110  1.00 26.49 ? 217 LEU B CB  1 
ATOM   3344  C CG  . LEU B 1 217 ? 40.021  -15.010 -38.056  1.00 25.81 ? 217 LEU B CG  1 
ATOM   3345  C CD1 . LEU B 1 217 ? 38.838  -15.721 -38.687  1.00 26.58 ? 217 LEU B CD1 1 
ATOM   3346  C CD2 . LEU B 1 217 ? 41.014  -15.975 -37.442  1.00 24.90 ? 217 LEU B CD2 1 
ATOM   3347  N N   . LEU B 1 218 ? 41.958  -11.453 -40.328  1.00 28.13 ? 218 LEU B N   1 
ATOM   3348  C CA  . LEU B 1 218 ? 42.475  -10.888 -41.587  1.00 30.45 ? 218 LEU B CA  1 
ATOM   3349  C C   . LEU B 1 218 ? 43.351  -9.627  -41.441  1.00 31.59 ? 218 LEU B C   1 
ATOM   3350  O O   . LEU B 1 218 ? 44.052  -9.244  -42.372  1.00 30.90 ? 218 LEU B O   1 
ATOM   3351  C CB  . LEU B 1 218 ? 41.312  -10.637 -42.552  1.00 30.59 ? 218 LEU B CB  1 
ATOM   3352  C CG  . LEU B 1 218 ? 40.443  -11.848 -42.908  1.00 30.72 ? 218 LEU B CG  1 
ATOM   3353  C CD1 . LEU B 1 218 ? 39.346  -11.417 -43.895  1.00 30.50 ? 218 LEU B CD1 1 
ATOM   3354  C CD2 . LEU B 1 218 ? 41.255  -13.006 -43.482  1.00 29.42 ? 218 LEU B CD2 1 
ATOM   3355  N N   . GLN B 1 219 ? 43.346  -9.038  -40.255  1.00 32.74 ? 219 GLN B N   1 
ATOM   3356  C CA  . GLN B 1 219 ? 44.286  -8.000  -39.898  1.00 34.32 ? 219 GLN B CA  1 
ATOM   3357  C C   . GLN B 1 219 ? 44.978  -8.457  -38.606  1.00 34.57 ? 219 GLN B C   1 
ATOM   3358  O O   . GLN B 1 219 ? 44.895  -7.778  -37.574  1.00 34.15 ? 219 GLN B O   1 
ATOM   3359  C CB  . GLN B 1 219 ? 43.538  -6.661  -39.707  1.00 33.22 ? 219 GLN B CB  1 
ATOM   3360  C CG  . GLN B 1 219 ? 42.721  -6.217  -40.921  1.00 31.72 ? 219 GLN B CG  1 
ATOM   3361  C CD  . GLN B 1 219 ? 41.891  -4.961  -40.672  1.00 32.36 ? 219 GLN B CD  1 
ATOM   3362  O OE1 . GLN B 1 219 ? 40.724  -4.859  -41.071  1.00 31.50 ? 219 GLN B OE1 1 
ATOM   3363  N NE2 . GLN B 1 219 ? 42.498  -3.981  -40.011  1.00 33.08 ? 219 GLN B NE2 1 
ATOM   3364  N N   . PRO B 1 220 ? 45.709  -9.585  -38.662  1.00 36.61 ? 220 PRO B N   1 
ATOM   3365  C CA  . PRO B 1 220 ? 46.253  -10.159 -37.405  1.00 36.28 ? 220 PRO B CA  1 
ATOM   3366  C C   . PRO B 1 220 ? 47.427  -9.349  -36.832  1.00 35.41 ? 220 PRO B C   1 
ATOM   3367  O O   . PRO B 1 220 ? 47.576  -9.279  -35.629  1.00 32.75 ? 220 PRO B O   1 
ATOM   3368  C CB  . PRO B 1 220 ? 46.717  -11.565 -37.827  1.00 36.34 ? 220 PRO B CB  1 
ATOM   3369  C CG  . PRO B 1 220 ? 47.037  -11.428 -39.288  1.00 37.11 ? 220 PRO B CG  1 
ATOM   3370  C CD  . PRO B 1 220 ? 46.259  -10.256 -39.861  1.00 37.02 ? 220 PRO B CD  1 
ATOM   3371  N N   . LYS B 1 221 ? 48.255  -8.778  -37.705  1.00 36.79 ? 221 LYS B N   1 
ATOM   3372  C CA  . LYS B 1 221 ? 49.230  -7.733  -37.348  1.00 37.66 ? 221 LYS B CA  1 
ATOM   3373  C C   . LYS B 1 221 ? 48.627  -6.622  -36.477  1.00 35.82 ? 221 LYS B C   1 
ATOM   3374  O O   . LYS B 1 221 ? 49.240  -6.198  -35.505  1.00 37.45 ? 221 LYS B O   1 
ATOM   3375  C CB  . LYS B 1 221 ? 49.867  -7.107  -38.605  1.00 39.59 ? 221 LYS B CB  1 
ATOM   3376  C CG  . LYS B 1 221 ? 49.130  -7.297  -39.946  1.00 42.21 ? 221 LYS B CG  1 
ATOM   3377  C CD  . LYS B 1 221 ? 47.726  -6.678  -40.024  1.00 39.57 ? 221 LYS B CD  1 
ATOM   3378  C CE  . LYS B 1 221 ? 47.321  -6.547  -41.485  1.00 40.62 ? 221 LYS B CE  1 
ATOM   3379  N NZ  . LYS B 1 221 ? 46.517  -5.328  -41.789  1.00 41.06 ? 221 LYS B NZ  1 
ATOM   3380  N N   . LEU B 1 222 ? 47.428  -6.168  -36.825  1.00 33.48 ? 222 LEU B N   1 
ATOM   3381  C CA  . LEU B 1 222 ? 46.721  -5.161  -36.040  1.00 32.18 ? 222 LEU B CA  1 
ATOM   3382  C C   . LEU B 1 222 ? 46.180  -5.772  -34.770  1.00 32.55 ? 222 LEU B C   1 
ATOM   3383  O O   . LEU B 1 222 ? 46.331  -5.196  -33.692  1.00 32.67 ? 222 LEU B O   1 
ATOM   3384  C CB  . LEU B 1 222 ? 45.581  -4.532  -36.836  1.00 31.97 ? 222 LEU B CB  1 
ATOM   3385  C CG  . LEU B 1 222 ? 44.693  -3.534  -36.088  1.00 31.29 ? 222 LEU B CG  1 
ATOM   3386  C CD1 . LEU B 1 222 ? 45.560  -2.431  -35.500  1.00 31.52 ? 222 LEU B CD1 1 
ATOM   3387  C CD2 . LEU B 1 222 ? 43.601  -2.954  -36.982  1.00 29.37 ? 222 LEU B CD2 1 
ATOM   3388  N N   . ALA B 1 223 ? 45.550  -6.938  -34.886  1.00 36.39 ? 223 ALA B N   1 
ATOM   3389  C CA  . ALA B 1 223 ? 45.051  -7.643  -33.696  1.00 37.77 ? 223 ALA B CA  1 
ATOM   3390  C C   . ALA B 1 223 ? 46.177  -7.800  -32.685  1.00 37.41 ? 223 ALA B C   1 
ATOM   3391  O O   . ALA B 1 223 ? 45.994  -7.483  -31.511  1.00 38.99 ? 223 ALA B O   1 
ATOM   3392  C CB  . ALA B 1 223 ? 44.479  -9.004  -34.061  1.00 38.36 ? 223 ALA B CB  1 
ATOM   3393  N N   . ALA B 1 224 ? 47.333  -8.265  -33.162  1.00 35.99 ? 224 ALA B N   1 
ATOM   3394  C CA  . ALA B 1 224 ? 48.534  -8.443  -32.338  1.00 37.01 ? 224 ALA B CA  1 
ATOM   3395  C C   . ALA B 1 224 ? 48.885  -7.183  -31.576  1.00 38.78 ? 224 ALA B C   1 
ATOM   3396  O O   . ALA B 1 224 ? 48.900  -7.193  -30.321  1.00 38.28 ? 224 ALA B O   1 
ATOM   3397  C CB  . ALA B 1 224 ? 49.727  -8.870  -33.195  1.00 36.02 ? 224 ALA B CB  1 
ATOM   3398  N N   . ALA B 1 225 ? 49.125  -6.100  -32.324  1.00 39.18 ? 225 ALA B N   1 
ATOM   3399  C CA  . ALA B 1 225 ? 49.511  -4.808  -31.748  1.00 39.56 ? 225 ALA B CA  1 
ATOM   3400  C C   . ALA B 1 225 ? 48.535  -4.311  -30.679  1.00 41.48 ? 225 ALA B C   1 
ATOM   3401  O O   . ALA B 1 225 ? 48.939  -3.701  -29.692  1.00 40.39 ? 225 ALA B O   1 
ATOM   3402  C CB  . ALA B 1 225 ? 49.645  -3.779  -32.850  1.00 38.75 ? 225 ALA B CB  1 
ATOM   3403  N N   . LEU B 1 226 ? 47.247  -4.581  -30.872  1.00 46.83 ? 226 LEU B N   1 
ATOM   3404  C CA  . LEU B 1 226 ? 46.221  -4.151  -29.922  1.00 49.95 ? 226 LEU B CA  1 
ATOM   3405  C C   . LEU B 1 226 ? 46.278  -4.886  -28.582  1.00 57.23 ? 226 LEU B C   1 
ATOM   3406  O O   . LEU B 1 226 ? 45.999  -4.300  -27.544  1.00 59.97 ? 226 LEU B O   1 
ATOM   3407  C CB  . LEU B 1 226 ? 44.825  -4.253  -30.553  1.00 47.38 ? 226 LEU B CB  1 
ATOM   3408  C CG  . LEU B 1 226 ? 44.588  -3.056  -31.499  1.00 46.91 ? 226 LEU B CG  1 
ATOM   3409  C CD1 . LEU B 1 226 ? 43.464  -3.265  -32.496  1.00 48.06 ? 226 LEU B CD1 1 
ATOM   3410  C CD2 . LEU B 1 226 ? 44.306  -1.783  -30.718  1.00 46.61 ? 226 LEU B CD2 1 
ATOM   3411  N N   . GLU B 1 227 ? 46.647  -6.163  -28.603  1.00 65.52 ? 227 GLU B N   1 
ATOM   3412  C CA  . GLU B 1 227 ? 46.651  -6.999  -27.384  1.00 71.77 ? 227 GLU B CA  1 
ATOM   3413  C C   . GLU B 1 227 ? 47.756  -6.636  -26.377  1.00 72.06 ? 227 GLU B C   1 
ATOM   3414  O O   . GLU B 1 227 ? 47.505  -6.659  -25.169  1.00 71.31 ? 227 GLU B O   1 
ATOM   3415  C CB  . GLU B 1 227 ? 46.735  -8.481  -27.746  1.00 74.25 ? 227 GLU B CB  1 
ATOM   3416  C CG  . GLU B 1 227 ? 45.403  -9.043  -28.256  1.00 75.21 ? 227 GLU B CG  1 
ATOM   3417  C CD  . GLU B 1 227 ? 45.561  -10.266 -29.148  1.00 76.64 ? 227 GLU B CD  1 
ATOM   3418  O OE1 . GLU B 1 227 ? 46.596  -10.962 -29.064  1.00 77.13 ? 227 GLU B OE1 1 
ATOM   3419  O OE2 . GLU B 1 227 ? 44.639  -10.543 -29.947  1.00 73.02 ? 227 GLU B OE2 1 
ATOM   3420  N N   . HIS B 1 228 ? 48.970  -6.371  -26.880  1.00 72.26 ? 228 HIS B N   1 
ATOM   3421  C CA  . HIS B 1 228 ? 50.163  -5.917  -26.108  1.00 72.01 ? 228 HIS B CA  1 
ATOM   3422  C C   . HIS B 1 228 ? 51.109  -7.060  -25.827  1.00 62.67 ? 228 HIS B C   1 
ATOM   3423  O O   . HIS B 1 228 ? 51.971  -7.329  -26.651  1.00 53.39 ? 228 HIS B O   1 
ATOM   3424  C CB  . HIS B 1 228 ? 49.840  -5.132  -24.813  1.00 80.45 ? 228 HIS B CB  1 
ATOM   3425  C CG  . HIS B 1 228 ? 49.082  -3.856  -25.054  1.00 92.30 ? 228 HIS B CG  1 
ATOM   3426  N ND1 . HIS B 1 228 ? 49.460  -2.931  -26.010  1.00 94.64 ? 228 HIS B ND1 1 
ATOM   3427  C CD2 . HIS B 1 228 ? 47.961  -3.358  -24.475  1.00 93.46 ? 228 HIS B CD2 1 
ATOM   3428  C CE1 . HIS B 1 228 ? 48.605  -1.924  -26.011  1.00 95.40 ? 228 HIS B CE1 1 
ATOM   3429  N NE2 . HIS B 1 228 ? 47.688  -2.155  -25.087  1.00 97.64 ? 228 HIS B NE2 1 
ATOM   3430  N N   . ASP C 1 2   ? 34.429  19.746  -59.965  1.00 81.84 ? 2   ASP C N   1 
ATOM   3431  C CA  . ASP C 1 2   ? 33.551  20.526  -59.065  1.00 85.72 ? 2   ASP C CA  1 
ATOM   3432  C C   . ASP C 1 2   ? 33.726  20.194  -57.581  1.00 83.59 ? 2   ASP C C   1 
ATOM   3433  O O   . ASP C 1 2   ? 33.352  19.133  -57.108  1.00 79.09 ? 2   ASP C O   1 
ATOM   3434  C CB  . ASP C 1 2   ? 32.077  20.363  -59.464  1.00 88.77 ? 2   ASP C CB  1 
ATOM   3435  C CG  . ASP C 1 2   ? 31.655  21.378  -60.526  1.00 87.35 ? 2   ASP C CG  1 
ATOM   3436  O OD1 . ASP C 1 2   ? 32.190  22.509  -60.539  1.00 83.70 ? 2   ASP C OD1 1 
ATOM   3437  O OD2 . ASP C 1 2   ? 30.803  21.050  -61.361  1.00 82.12 ? 2   ASP C OD2 1 
ATOM   3438  N N   . LYS C 1 3   ? 34.247  21.178  -56.848  1.00 82.80 ? 3   LYS C N   1 
ATOM   3439  C CA  . LYS C 1 3   ? 34.242  21.235  -55.392  1.00 75.66 ? 3   LYS C CA  1 
ATOM   3440  C C   . LYS C 1 3   ? 32.869  20.805  -54.818  1.00 67.36 ? 3   LYS C C   1 
ATOM   3441  O O   . LYS C 1 3   ? 31.826  21.286  -55.248  1.00 66.99 ? 3   LYS C O   1 
ATOM   3442  C CB  . LYS C 1 3   ? 34.579  22.697  -54.991  1.00 73.41 ? 3   LYS C CB  1 
ATOM   3443  C CG  . LYS C 1 3   ? 34.670  23.016  -53.513  1.00 71.37 ? 3   LYS C CG  1 
ATOM   3444  C CD  . LYS C 1 3   ? 35.492  24.296  -53.345  1.00 65.53 ? 3   LYS C CD  1 
ATOM   3445  C CE  . LYS C 1 3   ? 35.978  24.487  -51.916  1.00 62.00 ? 3   LYS C CE  1 
ATOM   3446  N NZ  . LYS C 1 3   ? 37.439  24.758  -51.797  1.00 59.63 ? 3   LYS C NZ  1 
ATOM   3447  N N   . ILE C 1 4   ? 32.850  19.979  -53.791  1.00 56.53 ? 4   ILE C N   1 
ATOM   3448  C CA  . ILE C 1 4   ? 31.679  19.960  -52.844  1.00 47.37 ? 4   ILE C CA  1 
ATOM   3449  C C   . ILE C 1 4   ? 31.812  21.221  -51.970  1.00 42.52 ? 4   ILE C C   1 
ATOM   3450  O O   . ILE C 1 4   ? 32.870  21.480  -51.403  1.00 37.82 ? 4   ILE C O   1 
ATOM   3451  C CB  . ILE C 1 4   ? 31.649  18.737  -51.901  1.00 45.85 ? 4   ILE C CB  1 
ATOM   3452  C CG1 . ILE C 1 4   ? 31.847  17.397  -52.653  1.00 46.57 ? 4   ILE C CG1 1 
ATOM   3453  C CG2 . ILE C 1 4   ? 30.432  18.865  -50.965  1.00 43.66 ? 4   ILE C CG2 1 
ATOM   3454  C CD1 . ILE C 1 4   ? 33.262  16.769  -52.530  1.00 45.88 ? 4   ILE C CD1 1 
ATOM   3455  N N   . LYS C 1 5   ? 30.751  22.020  -51.886  1.00 40.05 ? 5   LYS C N   1 
ATOM   3456  C CA  . LYS C 1 5   ? 30.816  23.327  -51.234  1.00 38.33 ? 5   LYS C CA  1 
ATOM   3457  C C   . LYS C 1 5   ? 30.494  23.238  -49.743  1.00 33.60 ? 5   LYS C C   1 
ATOM   3458  O O   . LYS C 1 5   ? 29.456  22.705  -49.355  1.00 31.59 ? 5   LYS C O   1 
ATOM   3459  C CB  . LYS C 1 5   ? 29.878  24.299  -51.928  1.00 42.45 ? 5   LYS C CB  1 
ATOM   3460  C CG  . LYS C 1 5   ? 30.448  24.728  -53.258  1.00 45.14 ? 5   LYS C CG  1 
ATOM   3461  C CD  . LYS C 1 5   ? 29.613  25.715  -54.045  1.00 47.83 ? 5   LYS C CD  1 
ATOM   3462  C CE  . LYS C 1 5   ? 30.561  26.726  -54.772  1.00 50.03 ? 5   LYS C CE  1 
ATOM   3463  N NZ  . LYS C 1 5   ? 30.414  26.864  -56.248  1.00 51.49 ? 5   LYS C NZ  1 
ATOM   3464  N N   . ARG C 1 6   ? 31.385  23.770  -48.913  1.00 29.89 ? 6   ARG C N   1 
ATOM   3465  C CA  . ARG C 1 6   ? 31.276  23.605  -47.473  1.00 27.97 ? 6   ARG C CA  1 
ATOM   3466  C C   . ARG C 1 6   ? 30.685  24.846  -46.789  1.00 26.12 ? 6   ARG C C   1 
ATOM   3467  O O   . ARG C 1 6   ? 31.211  25.950  -46.926  1.00 25.09 ? 6   ARG C O   1 
ATOM   3468  C CB  . ARG C 1 6   ? 32.647  23.219  -46.901  1.00 28.02 ? 6   ARG C CB  1 
ATOM   3469  C CG  . ARG C 1 6   ? 33.049  21.801  -47.278  1.00 28.47 ? 6   ARG C CG  1 
ATOM   3470  C CD  . ARG C 1 6   ? 34.491  21.459  -46.952  1.00 29.71 ? 6   ARG C CD  1 
ATOM   3471  N NE  . ARG C 1 6   ? 34.881  21.830  -45.587  1.00 30.17 ? 6   ARG C NE  1 
ATOM   3472  C CZ  . ARG C 1 6   ? 34.435  21.245  -44.477  1.00 30.58 ? 6   ARG C CZ  1 
ATOM   3473  N NH1 . ARG C 1 6   ? 33.562  20.262  -44.529  1.00 31.47 ? 6   ARG C NH1 1 
ATOM   3474  N NH2 . ARG C 1 6   ? 34.863  21.651  -43.294  1.00 31.08 ? 6   ARG C NH2 1 
ATOM   3475  N N   . VAL C 1 7   ? 29.584  24.653  -46.069  1.00 25.25 ? 7   VAL C N   1 
ATOM   3476  C CA  . VAL C 1 7   ? 28.907  25.739  -45.356  1.00 24.24 ? 7   VAL C CA  1 
ATOM   3477  C C   . VAL C 1 7   ? 28.908  25.516  -43.839  1.00 23.10 ? 7   VAL C C   1 
ATOM   3478  O O   . VAL C 1 7   ? 28.394  24.518  -43.349  1.00 22.65 ? 7   VAL C O   1 
ATOM   3479  C CB  . VAL C 1 7   ? 27.457  25.890  -45.842  1.00 24.86 ? 7   VAL C CB  1 
ATOM   3480  C CG1 . VAL C 1 7   ? 26.767  27.043  -45.141  1.00 25.74 ? 7   VAL C CG1 1 
ATOM   3481  C CG2 . VAL C 1 7   ? 27.422  26.106  -47.342  1.00 25.22 ? 7   VAL C CG2 1 
ATOM   3482  N N   . PHE C 1 8   ? 29.483  26.460  -43.104  1.00 22.76 ? 8   PHE C N   1 
ATOM   3483  C CA  . PHE C 1 8   ? 29.550  26.387  -41.649  1.00 21.65 ? 8   PHE C CA  1 
ATOM   3484  C C   . PHE C 1 8   ? 28.470  27.269  -41.047  1.00 21.55 ? 8   PHE C C   1 
ATOM   3485  O O   . PHE C 1 8   ? 28.382  28.454  -41.378  1.00 22.13 ? 8   PHE C O   1 
ATOM   3486  C CB  . PHE C 1 8   ? 30.919  26.850  -41.169  1.00 20.94 ? 8   PHE C CB  1 
ATOM   3487  C CG  . PHE C 1 8   ? 31.082  26.834  -39.676  1.00 20.27 ? 8   PHE C CG  1 
ATOM   3488  C CD1 . PHE C 1 8   ? 30.740  25.719  -38.932  1.00 19.71 ? 8   PHE C CD1 1 
ATOM   3489  C CD2 . PHE C 1 8   ? 31.601  27.937  -39.011  1.00 19.96 ? 8   PHE C CD2 1 
ATOM   3490  C CE1 . PHE C 1 8   ? 30.900  25.705  -37.566  1.00 19.61 ? 8   PHE C CE1 1 
ATOM   3491  C CE2 . PHE C 1 8   ? 31.759  27.932  -37.628  1.00 19.33 ? 8   PHE C CE2 1 
ATOM   3492  C CZ  . PHE C 1 8   ? 31.409  26.817  -36.908  1.00 19.24 ? 8   PHE C CZ  1 
ATOM   3493  N N   . VAL C 1 9   ? 27.643  26.690  -40.178  1.00 21.18 ? 9   VAL C N   1 
ATOM   3494  C CA  . VAL C 1 9   ? 26.554  27.427  -39.535  1.00 20.77 ? 9   VAL C CA  1 
ATOM   3495  C C   . VAL C 1 9   ? 26.845  27.620  -38.056  1.00 20.48 ? 9   VAL C C   1 
ATOM   3496  O O   . VAL C 1 9   ? 26.995  26.636  -37.311  1.00 21.93 ? 9   VAL C O   1 
ATOM   3497  C CB  . VAL C 1 9   ? 25.216  26.689  -39.655  1.00 21.02 ? 9   VAL C CB  1 
ATOM   3498  C CG1 . VAL C 1 9   ? 24.086  27.597  -39.182  1.00 21.38 ? 9   VAL C CG1 1 
ATOM   3499  C CG2 . VAL C 1 9   ? 24.973  26.250  -41.090  1.00 21.33 ? 9   VAL C CG2 1 
ATOM   3500  N N   . PHE C 1 10  ? 26.899  28.880  -37.634  1.00 19.01 ? 10  PHE C N   1 
ATOM   3501  C CA  . PHE C 1 10  ? 27.321  29.238  -36.291  1.00 18.67 ? 10  PHE C CA  1 
ATOM   3502  C C   . PHE C 1 10  ? 26.168  29.951  -35.620  1.00 19.05 ? 10  PHE C C   1 
ATOM   3503  O O   . PHE C 1 10  ? 25.806  31.062  -36.028  1.00 18.86 ? 10  PHE C O   1 
ATOM   3504  C CB  . PHE C 1 10  ? 28.531  30.164  -36.398  1.00 18.35 ? 10  PHE C CB  1 
ATOM   3505  C CG  . PHE C 1 10  ? 29.203  30.449  -35.084  1.00 18.29 ? 10  PHE C CG  1 
ATOM   3506  C CD1 . PHE C 1 10  ? 29.751  29.419  -34.336  1.00 17.93 ? 10  PHE C CD1 1 
ATOM   3507  C CD2 . PHE C 1 10  ? 29.319  31.752  -34.614  1.00 18.22 ? 10  PHE C CD2 1 
ATOM   3508  C CE1 . PHE C 1 10  ? 30.380  29.685  -33.140  1.00 17.56 ? 10  PHE C CE1 1 
ATOM   3509  C CE2 . PHE C 1 10  ? 29.948  32.019  -33.411  1.00 17.89 ? 10  PHE C CE2 1 
ATOM   3510  C CZ  . PHE C 1 10  ? 30.482  30.986  -32.675  1.00 17.67 ? 10  PHE C CZ  1 
ATOM   3511  N N   . GLY C 1 11  ? 25.577  29.329  -34.604  1.00 19.82 ? 11  GLY C N   1 
ATOM   3512  C CA  . GLY C 1 11  ? 24.413  29.922  -33.950  1.00 20.49 ? 11  GLY C CA  1 
ATOM   3513  C C   . GLY C 1 11  ? 24.230  29.551  -32.496  1.00 20.20 ? 11  GLY C C   1 
ATOM   3514  O O   . GLY C 1 11  ? 25.154  29.118  -31.833  1.00 17.40 ? 11  GLY C O   1 
ATOM   3515  N N   . ASP C 1 12  ? 23.001  29.729  -32.025  1.00 22.92 ? 12  ASP C N   1 
ATOM   3516  C CA  . ASP C 1 12  ? 22.652  29.527  -30.626  1.00 25.32 ? 12  ASP C CA  1 
ATOM   3517  C C   . ASP C 1 12  ? 21.713  28.320  -30.530  1.00 26.78 ? 12  ASP C C   1 
ATOM   3518  O O   . ASP C 1 12  ? 21.826  27.403  -31.337  1.00 26.34 ? 12  ASP C O   1 
ATOM   3519  C CB  . ASP C 1 12  ? 22.064  30.822  -30.024  1.00 26.72 ? 12  ASP C CB  1 
ATOM   3520  C CG  . ASP C 1 12  ? 20.998  31.476  -30.912  1.00 27.70 ? 12  ASP C CG  1 
ATOM   3521  O OD1 . ASP C 1 12  ? 20.362  30.735  -31.719  1.00 28.35 ? 12  ASP C OD1 1 
ATOM   3522  O OD2 . ASP C 1 12  ? 20.843  32.742  -30.820  1.00 27.27 ? 12  ASP C OD2 1 
HETATM 3523  N N   . SEP C 1 13  ? 20.807  28.302  -29.560  1.00 29.66 ? 13  SEP C N   1 
HETATM 3524  C CA  . SEP C 1 13  ? 19.936  27.142  -29.316  1.00 33.18 ? 13  SEP C CA  1 
HETATM 3525  C CB  . SEP C 1 13  ? 19.142  27.342  -28.016  1.00 39.60 ? 13  SEP C CB  1 
HETATM 3526  O OG  . SEP C 1 13  ? 18.608  28.679  -28.008  1.00 52.13 ? 13  SEP C OG  1 
HETATM 3527  C C   . SEP C 1 13  ? 18.990  26.938  -30.466  1.00 29.85 ? 13  SEP C C   1 
HETATM 3528  O O   . SEP C 1 13  ? 18.556  25.824  -30.705  1.00 27.95 ? 13  SEP C O   1 
HETATM 3529  P P   . SEP C 1 13  ? 18.879  30.003  -27.062  1.00 55.57 ? 13  SEP C P   1 
HETATM 3530  O O1P . SEP C 1 13  ? 20.391  30.172  -27.001  1.00 60.60 ? 13  SEP C O1P 1 
HETATM 3531  O O2P . SEP C 1 13  ? 18.280  31.070  -27.958  1.00 58.79 ? 13  SEP C O2P 1 
HETATM 3532  O O3P . SEP C 1 13  ? 18.263  29.789  -25.683  1.00 52.79 ? 13  SEP C O3P 1 
ATOM   3533  N N   . LEU C 1 14  ? 18.661  28.008  -31.185  1.00 28.52 ? 14  LEU C N   1 
ATOM   3534  C CA  . LEU C 1 14  ? 17.835  27.909  -32.396  1.00 28.09 ? 14  LEU C CA  1 
ATOM   3535  C C   . LEU C 1 14  ? 18.468  26.991  -33.429  1.00 26.79 ? 14  LEU C C   1 
ATOM   3536  O O   . LEU C 1 14  ? 17.768  26.319  -34.171  1.00 28.03 ? 14  LEU C O   1 
ATOM   3537  C CB  . LEU C 1 14  ? 17.627  29.294  -33.045  1.00 28.68 ? 14  LEU C CB  1 
ATOM   3538  C CG  . LEU C 1 14  ? 16.869  30.372  -32.244  1.00 28.28 ? 14  LEU C CG  1 
ATOM   3539  C CD1 . LEU C 1 14  ? 16.849  31.717  -32.945  1.00 27.99 ? 14  LEU C CD1 1 
ATOM   3540  C CD2 . LEU C 1 14  ? 15.457  29.921  -31.965  1.00 27.81 ? 14  LEU C CD2 1 
ATOM   3541  N N   . THR C 1 15  ? 19.797  26.994  -33.473  1.00 25.80 ? 15  THR C N   1 
ATOM   3542  C CA  . THR C 1 15  ? 20.584  26.205  -34.418  1.00 24.31 ? 15  THR C CA  1 
ATOM   3543  C C   . THR C 1 15  ? 20.978  24.831  -33.833  1.00 23.60 ? 15  THR C C   1 
ATOM   3544  O O   . THR C 1 15  ? 21.133  23.871  -34.574  1.00 24.50 ? 15  THR C O   1 
ATOM   3545  C CB  . THR C 1 15  ? 21.836  27.017  -34.821  1.00 24.50 ? 15  THR C CB  1 
ATOM   3546  O OG1 . THR C 1 15  ? 21.433  28.294  -35.346  1.00 25.57 ? 15  THR C OG1 1 
ATOM   3547  C CG2 . THR C 1 15  ? 22.677  26.271  -35.836  1.00 23.84 ? 15  THR C CG2 1 
ATOM   3548  N N   . TRP C 1 16  ? 21.128  24.743  -32.514  1.00 22.89 ? 16  TRP C N   1 
ATOM   3549  C CA  . TRP C 1 16  ? 21.296  23.460  -31.821  1.00 22.39 ? 16  TRP C CA  1 
ATOM   3550  C C   . TRP C 1 16  ? 20.071  22.589  -32.034  1.00 21.66 ? 16  TRP C C   1 
ATOM   3551  O O   . TRP C 1 16  ? 20.187  21.399  -32.325  1.00 20.99 ? 16  TRP C O   1 
ATOM   3552  C CB  . TRP C 1 16  ? 21.487  23.685  -30.309  1.00 23.14 ? 16  TRP C CB  1 
ATOM   3553  C CG  . TRP C 1 16  ? 21.648  22.422  -29.475  1.00 23.80 ? 16  TRP C CG  1 
ATOM   3554  C CD1 . TRP C 1 16  ? 22.720  21.575  -29.459  1.00 24.62 ? 16  TRP C CD1 1 
ATOM   3555  C CD2 . TRP C 1 16  ? 20.715  21.890  -28.522  1.00 24.77 ? 16  TRP C CD2 1 
ATOM   3556  N NE1 . TRP C 1 16  ? 22.505  20.542  -28.566  1.00 25.02 ? 16  TRP C NE1 1 
ATOM   3557  C CE2 . TRP C 1 16  ? 21.287  20.720  -27.973  1.00 24.41 ? 16  TRP C CE2 1 
ATOM   3558  C CE3 . TRP C 1 16  ? 19.455  22.291  -28.075  1.00 25.67 ? 16  TRP C CE3 1 
ATOM   3559  C CZ2 . TRP C 1 16  ? 20.641  19.952  -27.011  1.00 24.07 ? 16  TRP C CZ2 1 
ATOM   3560  C CZ3 . TRP C 1 16  ? 18.806  21.516  -27.118  1.00 25.43 ? 16  TRP C CZ3 1 
ATOM   3561  C CH2 . TRP C 1 16  ? 19.401  20.361  -26.599  1.00 24.55 ? 16  TRP C CH2 1 
ATOM   3562  N N   . GLY C 1 17  ? 18.896  23.197  -31.873  1.00 20.83 ? 17  GLY C N   1 
ATOM   3563  C CA  . GLY C 1 17  ? 17.632  22.487  -32.005  1.00 20.40 ? 17  GLY C CA  1 
ATOM   3564  C C   . GLY C 1 17  ? 16.834  22.425  -30.718  1.00 20.07 ? 17  GLY C C   1 
ATOM   3565  O O   . GLY C 1 17  ? 16.376  21.357  -30.344  1.00 21.08 ? 17  GLY C O   1 
ATOM   3566  N N   . TRP C 1 18  ? 16.646  23.562  -30.052  1.00 18.73 ? 18  TRP C N   1 
ATOM   3567  C CA  . TRP C 1 18  ? 15.852  23.621  -28.832  1.00 18.15 ? 18  TRP C CA  1 
ATOM   3568  C C   . TRP C 1 18  ? 14.393  23.347  -29.161  1.00 17.90 ? 18  TRP C C   1 
ATOM   3569  O O   . TRP C 1 18  ? 13.784  24.064  -29.957  1.00 16.92 ? 18  TRP C O   1 
ATOM   3570  C CB  . TRP C 1 18  ? 15.961  25.010  -28.194  1.00 18.17 ? 18  TRP C CB  1 
ATOM   3571  C CG  . TRP C 1 18  ? 15.278  25.180  -26.853  1.00 17.90 ? 18  TRP C CG  1 
ATOM   3572  C CD1 . TRP C 1 18  ? 13.952  25.046  -26.577  1.00 17.90 ? 18  TRP C CD1 1 
ATOM   3573  C CD2 . TRP C 1 18  ? 15.901  25.554  -25.618  1.00 18.04 ? 18  TRP C CD2 1 
ATOM   3574  N NE1 . TRP C 1 18  ? 13.708  25.289  -25.242  1.00 17.92 ? 18  TRP C NE1 1 
ATOM   3575  C CE2 . TRP C 1 18  ? 14.895  25.606  -24.634  1.00 17.93 ? 18  TRP C CE2 1 
ATOM   3576  C CE3 . TRP C 1 18  ? 17.221  25.844  -25.246  1.00 18.26 ? 18  TRP C CE3 1 
ATOM   3577  C CZ2 . TRP C 1 18  ? 15.168  25.935  -23.309  1.00 17.88 ? 18  TRP C CZ2 1 
ATOM   3578  C CZ3 . TRP C 1 18  ? 17.488  26.158  -23.921  1.00 17.78 ? 18  TRP C CZ3 1 
ATOM   3579  C CH2 . TRP C 1 18  ? 16.475  26.197  -22.974  1.00 18.06 ? 18  TRP C CH2 1 
ATOM   3580  N N   . THR C 1 19  ? 13.843  22.312  -28.525  1.00 18.51 ? 19  THR C N   1 
ATOM   3581  C CA  . THR C 1 19  ? 12.428  21.983  -28.649  1.00 19.28 ? 19  THR C CA  1 
ATOM   3582  C C   . THR C 1 19  ? 11.646  22.836  -27.641  1.00 19.89 ? 19  THR C C   1 
ATOM   3583  O O   . THR C 1 19  ? 11.861  22.704  -26.433  1.00 19.32 ? 19  THR C O   1 
ATOM   3584  C CB  . THR C 1 19  ? 12.158  20.489  -28.356  1.00 19.10 ? 19  THR C CB  1 
ATOM   3585  O OG1 . THR C 1 19  ? 12.885  19.678  -29.284  1.00 19.57 ? 19  THR C OG1 1 
ATOM   3586  C CG2 . THR C 1 19  ? 10.690  20.167  -28.481  1.00 18.85 ? 19  THR C CG2 1 
ATOM   3587  N N   . PRO C 1 20  ? 10.754  23.732  -28.130  1.00 20.63 ? 20  PRO C N   1 
ATOM   3588  C CA  . PRO C 1 20  ? 9.974   24.557  -27.202  1.00 21.83 ? 20  PRO C CA  1 
ATOM   3589  C C   . PRO C 1 20  ? 8.991   23.725  -26.384  1.00 22.54 ? 20  PRO C C   1 
ATOM   3590  O O   . PRO C 1 20  ? 8.308   22.874  -26.939  1.00 23.11 ? 20  PRO C O   1 
ATOM   3591  C CB  . PRO C 1 20  ? 9.242   25.549  -28.120  1.00 21.38 ? 20  PRO C CB  1 
ATOM   3592  C CG  . PRO C 1 20  ? 9.320   24.990  -29.484  1.00 21.01 ? 20  PRO C CG  1 
ATOM   3593  C CD  . PRO C 1 20  ? 10.510  24.096  -29.536  1.00 20.65 ? 20  PRO C CD  1 
ATOM   3594  N N   . VAL C 1 21  ? 8.946   23.976  -25.077  1.00 23.61 ? 21  VAL C N   1 
ATOM   3595  C CA  . VAL C 1 21  ? 8.150   23.168  -24.149  1.00 24.05 ? 21  VAL C CA  1 
ATOM   3596  C C   . VAL C 1 21  ? 7.658   23.980  -22.959  1.00 24.84 ? 21  VAL C C   1 
ATOM   3597  O O   . VAL C 1 21  ? 8.080   25.125  -22.751  1.00 26.57 ? 21  VAL C O   1 
ATOM   3598  C CB  . VAL C 1 21  ? 8.956   21.960  -23.620  1.00 23.89 ? 21  VAL C CB  1 
ATOM   3599  C CG1 . VAL C 1 21  ? 9.119   20.907  -24.701  1.00 23.77 ? 21  VAL C CG1 1 
ATOM   3600  C CG2 . VAL C 1 21  ? 10.315  22.404  -23.097  1.00 23.95 ? 21  VAL C CG2 1 
ATOM   3601  N N   . ALA C 1 22  ? 6.757   23.380  -22.193  1.00 25.06 ? 22  ALA C N   1 
ATOM   3602  C CA  . ALA C 1 22  ? 6.226   24.011  -20.984  1.00 24.84 ? 22  ALA C CA  1 
ATOM   3603  C C   . ALA C 1 22  ? 6.318   22.992  -19.837  1.00 24.30 ? 22  ALA C C   1 
ATOM   3604  O O   . ALA C 1 22  ? 5.812   21.879  -19.974  1.00 23.89 ? 22  ALA C O   1 
ATOM   3605  C CB  . ALA C 1 22  ? 4.799   24.462  -21.202  1.00 24.18 ? 22  ALA C CB  1 
ATOM   3606  N N   . PRO C 1 23  ? 6.995   23.329  -18.738  1.00 23.00 ? 23  PRO C N   1 
ATOM   3607  C CA  . PRO C 1 23  ? 7.704   24.596  -18.582  1.00 22.91 ? 23  PRO C CA  1 
ATOM   3608  C C   . PRO C 1 23  ? 8.933   24.700  -19.508  1.00 21.77 ? 23  PRO C C   1 
ATOM   3609  O O   . PRO C 1 23  ? 9.409   23.670  -20.040  1.00 21.13 ? 23  PRO C O   1 
ATOM   3610  C CB  . PRO C 1 23  ? 8.121   24.574  -17.101  1.00 24.08 ? 23  PRO C CB  1 
ATOM   3611  C CG  . PRO C 1 23  ? 8.145   23.098  -16.717  1.00 23.70 ? 23  PRO C CG  1 
ATOM   3612  C CD  . PRO C 1 23  ? 7.542   22.298  -17.840  1.00 22.94 ? 23  PRO C CD  1 
ATOM   3613  N N   . ILE C 1 24  ? 9.412   25.934  -19.693  1.00 20.68 ? 24  ILE C N   1 
ATOM   3614  C CA  . ILE C 1 24  ? 10.481  26.259  -20.660  1.00 20.47 ? 24  ILE C CA  1 
ATOM   3615  C C   . ILE C 1 24  ? 11.690  25.337  -20.621  1.00 20.34 ? 24  ILE C C   1 
ATOM   3616  O O   . ILE C 1 24  ? 12.226  24.998  -21.685  1.00 21.90 ? 24  ILE C O   1 
ATOM   3617  C CB  . ILE C 1 24  ? 10.936  27.744  -20.564  1.00 19.99 ? 24  ILE C CB  1 
ATOM   3618  C CG1 . ILE C 1 24  ? 11.981  28.062  -21.653  1.00 19.39 ? 24  ILE C CG1 1 
ATOM   3619  C CG2 . ILE C 1 24  ? 11.469  28.072  -19.183  1.00 19.94 ? 24  ILE C CG2 1 
ATOM   3620  C CD1 . ILE C 1 24  ? 12.321  29.506  -21.768  1.00 18.79 ? 24  ILE C CD1 1 
ATOM   3621  N N   . VAL C 1 25  ? 12.088  24.934  -19.413  1.00 20.27 ? 25  VAL C N   1 
ATOM   3622  C CA  . VAL C 1 25  ? 13.178  23.957  -19.189  1.00 20.13 ? 25  VAL C CA  1 
ATOM   3623  C C   . VAL C 1 25  ? 12.695  22.836  -18.255  1.00 20.41 ? 25  VAL C C   1 
ATOM   3624  O O   . VAL C 1 25  ? 11.805  23.064  -17.426  1.00 20.07 ? 25  VAL C O   1 
ATOM   3625  C CB  . VAL C 1 25  ? 14.408  24.632  -18.540  1.00 20.62 ? 25  VAL C CB  1 
ATOM   3626  C CG1 . VAL C 1 25  ? 14.975  25.697  -19.471  1.00 21.15 ? 25  VAL C CG1 1 
ATOM   3627  C CG2 . VAL C 1 25  ? 14.091  25.214  -17.150  1.00 20.13 ? 25  VAL C CG2 1 
ATOM   3628  N N   . PRO C 1 26  ? 13.253  21.630  -18.365  1.00 20.42 ? 26  PRO C N   1 
ATOM   3629  C CA  . PRO C 1 26  ? 14.273  21.266  -19.343  1.00 20.25 ? 26  PRO C CA  1 
ATOM   3630  C C   . PRO C 1 26  ? 13.701  20.939  -20.715  1.00 19.76 ? 26  PRO C C   1 
ATOM   3631  O O   . PRO C 1 26  ? 12.531  20.593  -20.818  1.00 19.70 ? 26  PRO C O   1 
ATOM   3632  C CB  . PRO C 1 26  ? 14.901  20.018  -18.724  1.00 20.15 ? 26  PRO C CB  1 
ATOM   3633  C CG  . PRO C 1 26  ? 13.810  19.405  -17.924  1.00 19.96 ? 26  PRO C CG  1 
ATOM   3634  C CD  . PRO C 1 26  ? 12.847  20.481  -17.538  1.00 20.12 ? 26  PRO C CD  1 
ATOM   3635  N N   . THR C 1 27  ? 14.533  21.049  -21.744  1.00 19.20 ? 27  THR C N   1 
ATOM   3636  C CA  . THR C 1 27  ? 14.152  20.704  -23.122  1.00 18.91 ? 27  THR C CA  1 
ATOM   3637  C C   . THR C 1 27  ? 14.924  19.467  -23.585  1.00 19.03 ? 27  THR C C   1 
ATOM   3638  O O   . THR C 1 27  ? 15.811  18.957  -22.877  1.00 19.34 ? 27  THR C O   1 
ATOM   3639  C CB  . THR C 1 27  ? 14.420  21.879  -24.101  1.00 18.21 ? 27  THR C CB  1 
ATOM   3640  O OG1 . THR C 1 27  ? 14.046  21.519  -25.438  1.00 17.29 ? 27  THR C OG1 1 
ATOM   3641  C CG2 . THR C 1 27  ? 15.876  22.284  -24.109  1.00 18.25 ? 27  THR C CG2 1 
ATOM   3642  N N   . THR C 1 28  ? 14.571  18.985  -24.766  1.00 19.02 ? 28  THR C N   1 
ATOM   3643  C CA  . THR C 1 28  ? 15.345  17.955  -25.439  1.00 20.33 ? 28  THR C CA  1 
ATOM   3644  C C   . THR C 1 28  ? 15.571  18.438  -26.868  1.00 21.07 ? 28  THR C C   1 
ATOM   3645  O O   . THR C 1 28  ? 14.832  19.306  -27.364  1.00 22.04 ? 28  THR C O   1 
ATOM   3646  C CB  . THR C 1 28  ? 14.629  16.580  -25.458  1.00 20.63 ? 28  THR C CB  1 
ATOM   3647  O OG1 . THR C 1 28  ? 13.532  16.630  -26.383  1.00 21.21 ? 28  THR C OG1 1 
ATOM   3648  C CG2 . THR C 1 28  ? 14.120  16.186  -24.070  1.00 20.58 ? 28  THR C CG2 1 
ATOM   3649  N N   . ARG C 1 29  ? 16.588  17.874  -27.522  1.00 20.35 ? 29  ARG C N   1 
ATOM   3650  C CA  . ARG C 1 29  ? 17.005  18.344  -28.833  1.00 20.38 ? 29  ARG C CA  1 
ATOM   3651  C C   . ARG C 1 29  ? 16.026  17.904  -29.909  1.00 20.58 ? 29  ARG C C   1 
ATOM   3652  O O   . ARG C 1 29  ? 15.639  16.752  -29.960  1.00 20.95 ? 29  ARG C O   1 
ATOM   3653  C CB  . ARG C 1 29  ? 18.404  17.820  -29.170  1.00 20.50 ? 29  ARG C CB  1 
ATOM   3654  C CG  . ARG C 1 29  ? 19.281  18.860  -29.856  1.00 21.00 ? 29  ARG C CG  1 
ATOM   3655  C CD  . ARG C 1 29  ? 20.005  18.341  -31.071  1.00 21.48 ? 29  ARG C CD  1 
ATOM   3656  N NE  . ARG C 1 29  ? 21.417  18.021  -30.845  1.00 22.05 ? 29  ARG C NE  1 
ATOM   3657  C CZ  . ARG C 1 29  ? 22.452  18.607  -31.449  1.00 21.57 ? 29  ARG C CZ  1 
ATOM   3658  N NH1 . ARG C 1 29  ? 22.274  19.613  -32.321  1.00 20.98 ? 29  ARG C NH1 1 
ATOM   3659  N NH2 . ARG C 1 29  ? 23.678  18.175  -31.153  1.00 21.48 ? 29  ARG C NH2 1 
ATOM   3660  N N   . HIS C 1 30  ? 15.612  18.820  -30.770  1.00 21.47 ? 30  HIS C N   1 
ATOM   3661  C CA  . HIS C 1 30  ? 14.823  18.441  -31.943  1.00 22.20 ? 30  HIS C CA  1 
ATOM   3662  C C   . HIS C 1 30  ? 15.496  17.238  -32.610  1.00 22.90 ? 30  HIS C C   1 
ATOM   3663  O O   . HIS C 1 30  ? 16.716  17.207  -32.756  1.00 20.46 ? 30  HIS C O   1 
ATOM   3664  C CB  . HIS C 1 30  ? 14.749  19.576  -32.973  1.00 22.38 ? 30  HIS C CB  1 
ATOM   3665  C CG  . HIS C 1 30  ? 13.669  20.580  -32.717  1.00 22.48 ? 30  HIS C CG  1 
ATOM   3666  N ND1 . HIS C 1 30  ? 12.324  20.279  -32.831  1.00 23.02 ? 30  HIS C ND1 1 
ATOM   3667  C CD2 . HIS C 1 30  ? 13.737  21.897  -32.407  1.00 21.42 ? 30  HIS C CD2 1 
ATOM   3668  C CE1 . HIS C 1 30  ? 11.613  21.366  -32.577  1.00 22.02 ? 30  HIS C CE1 1 
ATOM   3669  N NE2 . HIS C 1 30  ? 12.447  22.360  -32.320  1.00 21.19 ? 30  HIS C NE2 1 
ATOM   3670  N N   . PRO C 1 31  ? 14.700  16.240  -33.022  1.00 24.87 ? 31  PRO C N   1 
ATOM   3671  C CA  . PRO C 1 31  ? 15.273  15.192  -33.871  1.00 24.48 ? 31  PRO C CA  1 
ATOM   3672  C C   . PRO C 1 31  ? 15.965  15.806  -35.083  1.00 23.98 ? 31  PRO C C   1 
ATOM   3673  O O   . PRO C 1 31  ? 15.508  16.822  -35.607  1.00 22.72 ? 31  PRO C O   1 
ATOM   3674  C CB  . PRO C 1 31  ? 14.049  14.392  -34.319  1.00 25.40 ? 31  PRO C CB  1 
ATOM   3675  C CG  . PRO C 1 31  ? 12.982  14.684  -33.316  1.00 25.36 ? 31  PRO C CG  1 
ATOM   3676  C CD  . PRO C 1 31  ? 13.258  16.044  -32.759  1.00 25.43 ? 31  PRO C CD  1 
ATOM   3677  N N   . HIS C 1 32  ? 17.055  15.186  -35.518  1.00 24.44 ? 32  HIS C N   1 
ATOM   3678  C CA  . HIS C 1 32  ? 17.848  15.691  -36.651  1.00 24.29 ? 32  HIS C CA  1 
ATOM   3679  C C   . HIS C 1 32  ? 16.967  16.049  -37.858  1.00 23.74 ? 32  HIS C C   1 
ATOM   3680  O O   . HIS C 1 32  ? 17.149  17.087  -38.489  1.00 21.17 ? 32  HIS C O   1 
ATOM   3681  C CB  . HIS C 1 32  ? 18.906  14.654  -37.048  1.00 25.05 ? 32  HIS C CB  1 
ATOM   3682  C CG  . HIS C 1 32  ? 19.838  15.109  -38.127  1.00 25.87 ? 32  HIS C CG  1 
ATOM   3683  N ND1 . HIS C 1 32  ? 19.577  14.911  -39.470  1.00 26.25 ? 32  HIS C ND1 1 
ATOM   3684  C CD2 . HIS C 1 32  ? 21.035  15.744  -38.059  1.00 25.96 ? 32  HIS C CD2 1 
ATOM   3685  C CE1 . HIS C 1 32  ? 20.573  15.411  -40.183  1.00 26.66 ? 32  HIS C CE1 1 
ATOM   3686  N NE2 . HIS C 1 32  ? 21.466  15.927  -39.353  1.00 26.12 ? 32  HIS C NE2 1 
ATOM   3687  N N   . ALA C 1 33  ? 15.993  15.192  -38.158  1.00 24.41 ? 33  ALA C N   1 
ATOM   3688  C CA  . ALA C 1 33  ? 15.092  15.398  -39.290  1.00 24.07 ? 33  ALA C CA  1 
ATOM   3689  C C   . ALA C 1 33  ? 14.346  16.740  -39.242  1.00 24.49 ? 33  ALA C C   1 
ATOM   3690  O O   . ALA C 1 33  ? 13.992  17.284  -40.286  1.00 24.25 ? 33  ALA C O   1 
ATOM   3691  C CB  . ALA C 1 33  ? 14.099  14.242  -39.367  1.00 23.67 ? 33  ALA C CB  1 
ATOM   3692  N N   . ASP C 1 34  ? 14.121  17.267  -38.034  1.00 25.52 ? 34  ASP C N   1 
ATOM   3693  C CA  . ASP C 1 34  ? 13.347  18.492  -37.822  1.00 25.53 ? 34  ASP C CA  1 
ATOM   3694  C C   . ASP C 1 34  ? 14.186  19.767  -37.619  1.00 25.19 ? 34  ASP C C   1 
ATOM   3695  O O   . ASP C 1 34  ? 13.615  20.831  -37.355  1.00 25.56 ? 34  ASP C O   1 
ATOM   3696  C CB  . ASP C 1 34  ? 12.463  18.326  -36.587  1.00 26.48 ? 34  ASP C CB  1 
ATOM   3697  C CG  . ASP C 1 34  ? 11.452  17.208  -36.726  1.00 26.98 ? 34  ASP C CG  1 
ATOM   3698  O OD1 . ASP C 1 34  ? 11.040  16.924  -37.877  1.00 28.07 ? 34  ASP C OD1 1 
ATOM   3699  O OD2 . ASP C 1 34  ? 11.065  16.633  -35.680  1.00 25.48 ? 34  ASP C OD2 1 
ATOM   3700  N N   . ARG C 1 35  ? 15.517  19.678  -37.702  1.00 23.76 ? 35  ARG C N   1 
ATOM   3701  C CA  . ARG C 1 35  ? 16.375  20.850  -37.452  1.00 23.13 ? 35  ARG C CA  1 
ATOM   3702  C C   . ARG C 1 35  ? 16.506  21.737  -38.683  1.00 22.11 ? 35  ARG C C   1 
ATOM   3703  O O   . ARG C 1 35  ? 16.628  21.234  -39.801  1.00 21.10 ? 35  ARG C O   1 
ATOM   3704  C CB  . ARG C 1 35  ? 17.760  20.416  -36.968  1.00 23.06 ? 35  ARG C CB  1 
ATOM   3705  C CG  . ARG C 1 35  ? 17.754  19.723  -35.620  1.00 22.44 ? 35  ARG C CG  1 
ATOM   3706  C CD  . ARG C 1 35  ? 19.151  19.315  -35.202  1.00 22.72 ? 35  ARG C CD  1 
ATOM   3707  N NE  . ARG C 1 35  ? 19.104  18.139  -34.340  1.00 24.10 ? 35  ARG C NE  1 
ATOM   3708  C CZ  . ARG C 1 35  ? 20.099  17.271  -34.160  1.00 25.44 ? 35  ARG C CZ  1 
ATOM   3709  N NH1 . ARG C 1 35  ? 21.265  17.425  -34.773  1.00 25.76 ? 35  ARG C NH1 1 
ATOM   3710  N NH2 . ARG C 1 35  ? 19.923  16.219  -33.362  1.00 26.41 ? 35  ARG C NH2 1 
ATOM   3711  N N   . TRP C 1 36  ? 16.498  23.056  -38.480  1.00 21.72 ? 36  TRP C N   1 
ATOM   3712  C CA  . TRP C 1 36  ? 16.500  23.986  -39.631  1.00 22.34 ? 36  TRP C CA  1 
ATOM   3713  C C   . TRP C 1 36  ? 17.712  23.777  -40.536  1.00 22.31 ? 36  TRP C C   1 
ATOM   3714  O O   . TRP C 1 36  ? 17.607  23.776  -41.753  1.00 22.90 ? 36  TRP C O   1 
ATOM   3715  C CB  . TRP C 1 36  ? 16.335  25.460  -39.191  1.00 22.41 ? 36  TRP C CB  1 
ATOM   3716  C CG  . TRP C 1 36  ? 17.578  26.220  -38.857  1.00 22.86 ? 36  TRP C CG  1 
ATOM   3717  C CD1 . TRP C 1 36  ? 18.151  26.370  -37.615  1.00 23.60 ? 36  TRP C CD1 1 
ATOM   3718  C CD2 . TRP C 1 36  ? 18.399  26.960  -39.760  1.00 23.21 ? 36  TRP C CD2 1 
ATOM   3719  N NE1 . TRP C 1 36  ? 19.281  27.160  -37.699  1.00 23.24 ? 36  TRP C NE1 1 
ATOM   3720  C CE2 . TRP C 1 36  ? 19.453  27.526  -39.008  1.00 23.42 ? 36  TRP C CE2 1 
ATOM   3721  C CE3 . TRP C 1 36  ? 18.353  27.192  -41.133  1.00 23.93 ? 36  TRP C CE3 1 
ATOM   3722  C CZ2 . TRP C 1 36  ? 20.445  28.304  -39.591  1.00 24.03 ? 36  TRP C CZ2 1 
ATOM   3723  C CZ3 . TRP C 1 36  ? 19.356  27.955  -41.713  1.00 24.36 ? 36  TRP C CZ3 1 
ATOM   3724  C CH2 . TRP C 1 36  ? 20.377  28.514  -40.941  1.00 24.25 ? 36  TRP C CH2 1 
ATOM   3725  N N   . THR C 1 37  ? 18.863  23.563  -39.915  1.00 23.79 ? 37  THR C N   1 
ATOM   3726  C CA  . THR C 1 37  ? 20.108  23.263  -40.616  1.00 24.58 ? 37  THR C CA  1 
ATOM   3727  C C   . THR C 1 37  ? 20.011  21.991  -41.452  1.00 24.97 ? 37  THR C C   1 
ATOM   3728  O O   . THR C 1 37  ? 20.592  21.922  -42.537  1.00 26.36 ? 37  THR C O   1 
ATOM   3729  C CB  . THR C 1 37  ? 21.278  23.106  -39.628  1.00 24.37 ? 37  THR C CB  1 
ATOM   3730  O OG1 . THR C 1 37  ? 20.883  22.267  -38.538  1.00 24.35 ? 37  THR C OG1 1 
ATOM   3731  C CG2 . THR C 1 37  ? 21.696  24.455  -39.084  1.00 23.91 ? 37  THR C CG2 1 
ATOM   3732  N N   . THR C 1 38  ? 19.290  20.989  -40.959  1.00 24.09 ? 38  THR C N   1 
ATOM   3733  C CA  . THR C 1 38  ? 19.116  19.753  -41.716  1.00 24.53 ? 38  THR C CA  1 
ATOM   3734  C C   . THR C 1 38  ? 18.302  19.986  -42.980  1.00 24.55 ? 38  THR C C   1 
ATOM   3735  O O   . THR C 1 38  ? 18.665  19.512  -44.065  1.00 25.48 ? 38  THR C O   1 
ATOM   3736  C CB  . THR C 1 38  ? 18.468  18.651  -40.864  1.00 24.34 ? 38  THR C CB  1 
ATOM   3737  O OG1 . THR C 1 38  ? 19.364  18.311  -39.809  1.00 24.68 ? 38  THR C OG1 1 
ATOM   3738  C CG2 . THR C 1 38  ? 18.186  17.413  -41.681  1.00 24.03 ? 38  THR C CG2 1 
ATOM   3739  N N   . VAL C 1 39  ? 17.214  20.731  -42.841  1.00 23.26 ? 39  VAL C N   1 
ATOM   3740  C CA  . VAL C 1 39  ? 16.374  21.044  -43.988  1.00 22.18 ? 39  VAL C CA  1 
ATOM   3741  C C   . VAL C 1 39  ? 17.155  21.924  -44.957  1.00 21.49 ? 39  VAL C C   1 
ATOM   3742  O O   . VAL C 1 39  ? 17.091  21.712  -46.151  1.00 20.66 ? 39  VAL C O   1 
ATOM   3743  C CB  . VAL C 1 39  ? 15.052  21.703  -43.573  1.00 21.15 ? 39  VAL C CB  1 
ATOM   3744  C CG1 . VAL C 1 39  ? 14.270  22.151  -44.792  1.00 20.70 ? 39  VAL C CG1 1 
ATOM   3745  C CG2 . VAL C 1 39  ? 14.231  20.721  -42.741  1.00 21.11 ? 39  VAL C CG2 1 
ATOM   3746  N N   . LEU C 1 40  ? 17.909  22.886  -44.437  1.00 21.40 ? 40  LEU C N   1 
ATOM   3747  C CA  . LEU C 1 40  ? 18.848  23.650  -45.259  1.00 21.69 ? 40  LEU C CA  1 
ATOM   3748  C C   . LEU C 1 40  ? 19.737  22.731  -46.105  1.00 23.14 ? 40  LEU C C   1 
ATOM   3749  O O   . LEU C 1 40  ? 19.938  22.971  -47.312  1.00 22.35 ? 40  LEU C O   1 
ATOM   3750  C CB  . LEU C 1 40  ? 19.728  24.555  -44.385  1.00 21.05 ? 40  LEU C CB  1 
ATOM   3751  C CG  . LEU C 1 40  ? 20.949  25.198  -45.072  1.00 20.20 ? 40  LEU C CG  1 
ATOM   3752  C CD1 . LEU C 1 40  ? 20.521  26.216  -46.120  1.00 19.98 ? 40  LEU C CD1 1 
ATOM   3753  C CD2 . LEU C 1 40  ? 21.855  25.845  -44.046  1.00 19.69 ? 40  LEU C CD2 1 
ATOM   3754  N N   . GLY C 1 41  ? 20.272  21.687  -45.467  1.00 25.37 ? 41  GLY C N   1 
ATOM   3755  C CA  . GLY C 1 41  ? 21.155  20.733  -46.139  1.00 26.38 ? 41  GLY C CA  1 
ATOM   3756  C C   . GLY C 1 41  ? 20.455  19.959  -47.245  1.00 27.11 ? 41  GLY C C   1 
ATOM   3757  O O   . GLY C 1 41  ? 21.005  19.792  -48.338  1.00 25.09 ? 41  GLY C O   1 
ATOM   3758  N N   . GLU C 1 42  ? 19.239  19.504  -46.945  1.00 29.25 ? 42  GLU C N   1 
ATOM   3759  C CA  . GLU C 1 42  ? 18.438  18.729  -47.888  1.00 31.21 ? 42  GLU C CA  1 
ATOM   3760  C C   . GLU C 1 42  ? 18.037  19.523  -49.105  1.00 31.64 ? 42  GLU C C   1 
ATOM   3761  O O   . GLU C 1 42  ? 18.114  19.012  -50.215  1.00 31.88 ? 42  GLU C O   1 
ATOM   3762  C CB  . GLU C 1 42  ? 17.188  18.166  -47.215  1.00 32.04 ? 42  GLU C CB  1 
ATOM   3763  C CG  . GLU C 1 42  ? 17.429  16.796  -46.589  1.00 34.30 ? 42  GLU C CG  1 
ATOM   3764  C CD  . GLU C 1 42  ? 16.507  16.483  -45.420  1.00 37.18 ? 42  GLU C CD  1 
ATOM   3765  O OE1 . GLU C 1 42  ? 16.856  15.549  -44.651  1.00 38.92 ? 42  GLU C OE1 1 
ATOM   3766  O OE2 . GLU C 1 42  ? 15.468  17.178  -45.240  1.00 37.35 ? 42  GLU C OE2 1 
ATOM   3767  N N   . ASN C 1 43  ? 17.620  20.769  -48.900  1.00 31.73 ? 43  ASN C N   1 
ATOM   3768  C CA  . ASN C 1 43  ? 17.235  21.637  -50.006  1.00 30.69 ? 43  ASN C CA  1 
ATOM   3769  C C   . ASN C 1 43  ? 18.399  22.100  -50.857  1.00 31.83 ? 43  ASN C C   1 
ATOM   3770  O O   . ASN C 1 43  ? 18.174  22.523  -51.995  1.00 32.43 ? 43  ASN C O   1 
ATOM   3771  C CB  . ASN C 1 43  ? 16.499  22.868  -49.499  1.00 30.97 ? 43  ASN C CB  1 
ATOM   3772  C CG  . ASN C 1 43  ? 15.032  22.610  -49.248  1.00 30.09 ? 43  ASN C CG  1 
ATOM   3773  O OD1 . ASN C 1 43  ? 14.212  22.952  -50.075  1.00 29.58 ? 43  ASN C OD1 1 
ATOM   3774  N ND2 . ASN C 1 43  ? 14.702  22.019  -48.109  1.00 30.08 ? 43  ASN C ND2 1 
ATOM   3775  N N   . LEU C 1 44  ? 19.625  22.033  -50.325  1.00 32.97 ? 44  LEU C N   1 
ATOM   3776  C CA  . LEU C 1 44  ? 20.817  22.432  -51.094  1.00 32.22 ? 44  LEU C CA  1 
ATOM   3777  C C   . LEU C 1 44  ? 21.292  21.305  -52.013  1.00 30.81 ? 44  LEU C C   1 
ATOM   3778  O O   . LEU C 1 44  ? 21.777  21.564  -53.095  1.00 30.38 ? 44  LEU C O   1 
ATOM   3779  C CB  . LEU C 1 44  ? 21.960  22.840  -50.144  1.00 32.56 ? 44  LEU C CB  1 
ATOM   3780  C CG  . LEU C 1 44  ? 21.923  24.271  -49.590  1.00 32.82 ? 44  LEU C CG  1 
ATOM   3781  C CD1 . LEU C 1 44  ? 22.983  24.461  -48.510  1.00 32.76 ? 44  LEU C CD1 1 
ATOM   3782  C CD2 . LEU C 1 44  ? 22.111  25.302  -50.690  1.00 30.78 ? 44  LEU C CD2 1 
ATOM   3783  N N   . GLY C 1 45  ? 21.166  20.066  -51.563  1.00 32.85 ? 45  GLY C N   1 
ATOM   3784  C CA  . GLY C 1 45  ? 21.532  18.892  -52.357  1.00 34.28 ? 45  GLY C CA  1 
ATOM   3785  C C   . GLY C 1 45  ? 22.941  18.387  -52.104  1.00 34.38 ? 45  GLY C C   1 
ATOM   3786  O O   . GLY C 1 45  ? 23.647  18.881  -51.229  1.00 35.54 ? 45  GLY C O   1 
ATOM   3787  N N   . ASP C 1 46  ? 23.346  17.431  -52.915  1.00 35.30 ? 46  ASP C N   1 
ATOM   3788  C CA  . ASP C 1 46  ? 24.670  16.779  -52.829  1.00 36.10 ? 46  ASP C CA  1 
ATOM   3789  C C   . ASP C 1 46  ? 25.820  17.734  -53.160  1.00 35.45 ? 46  ASP C C   1 
ATOM   3790  O O   . ASP C 1 46  ? 26.974  17.448  -52.840  1.00 32.55 ? 46  ASP C O   1 
ATOM   3791  C CB  . ASP C 1 46  ? 24.778  15.590  -53.816  1.00 37.56 ? 46  ASP C CB  1 
ATOM   3792  C CG  . ASP C 1 46  ? 23.692  14.530  -53.619  1.00 37.17 ? 46  ASP C CG  1 
ATOM   3793  O OD1 . ASP C 1 46  ? 23.257  14.355  -52.465  1.00 37.61 ? 46  ASP C OD1 1 
ATOM   3794  O OD2 . ASP C 1 46  ? 23.273  13.887  -54.615  1.00 34.65 ? 46  ASP C OD2 1 
ATOM   3795  N N   . GLY C 1 47  ? 25.511  18.853  -53.829  1.00 35.88 ? 47  GLY C N   1 
ATOM   3796  C CA  . GLY C 1 47  ? 26.515  19.860  -54.147  1.00 36.94 ? 47  GLY C CA  1 
ATOM   3797  C C   . GLY C 1 47  ? 27.109  20.522  -52.916  1.00 37.29 ? 47  GLY C C   1 
ATOM   3798  O O   . GLY C 1 47  ? 28.190  21.128  -52.995  1.00 37.05 ? 47  GLY C O   1 
ATOM   3799  N N   . TYR C 1 48  ? 26.409  20.400  -51.779  1.00 36.16 ? 48  TYR C N   1 
ATOM   3800  C CA  . TYR C 1 48  ? 26.788  21.068  -50.537  1.00 34.00 ? 48  TYR C CA  1 
ATOM   3801  C C   . TYR C 1 48  ? 26.928  20.097  -49.361  1.00 32.60 ? 48  TYR C C   1 
ATOM   3802  O O   . TYR C 1 48  ? 26.308  19.038  -49.328  1.00 28.73 ? 48  TYR C O   1 
ATOM   3803  C CB  . TYR C 1 48  ? 25.763  22.150  -50.212  1.00 34.10 ? 48  TYR C CB  1 
ATOM   3804  C CG  . TYR C 1 48  ? 25.601  23.200  -51.304  1.00 35.42 ? 48  TYR C CG  1 
ATOM   3805  C CD1 . TYR C 1 48  ? 24.864  22.929  -52.446  1.00 35.08 ? 48  TYR C CD1 1 
ATOM   3806  C CD2 . TYR C 1 48  ? 26.178  24.464  -51.182  1.00 36.11 ? 48  TYR C CD2 1 
ATOM   3807  C CE1 . TYR C 1 48  ? 24.698  23.873  -53.439  1.00 36.09 ? 48  TYR C CE1 1 
ATOM   3808  C CE2 . TYR C 1 48  ? 26.033  25.420  -52.176  1.00 37.81 ? 48  TYR C CE2 1 
ATOM   3809  C CZ  . TYR C 1 48  ? 25.276  25.114  -53.305  1.00 37.59 ? 48  TYR C CZ  1 
ATOM   3810  O OH  . TYR C 1 48  ? 25.075  26.039  -54.302  1.00 35.64 ? 48  TYR C OH  1 
ATOM   3811  N N   . GLU C 1 49  ? 27.740  20.506  -48.391  1.00 34.11 ? 49  GLU C N   1 
ATOM   3812  C CA  . GLU C 1 49  ? 28.051  19.748  -47.186  1.00 34.93 ? 49  GLU C CA  1 
ATOM   3813  C C   . GLU C 1 49  ? 28.060  20.737  -45.994  1.00 32.31 ? 49  GLU C C   1 
ATOM   3814  O O   . GLU C 1 49  ? 28.764  21.750  -46.025  1.00 31.87 ? 49  GLU C O   1 
ATOM   3815  C CB  . GLU C 1 49  ? 29.414  19.106  -47.414  1.00 39.89 ? 49  GLU C CB  1 
ATOM   3816  C CG  . GLU C 1 49  ? 30.181  18.481  -46.229  1.00 44.57 ? 49  GLU C CG  1 
ATOM   3817  C CD  . GLU C 1 49  ? 31.433  17.737  -46.731  1.00 47.58 ? 49  GLU C CD  1 
ATOM   3818  O OE1 . GLU C 1 49  ? 32.631  18.014  -46.363  1.00 45.31 ? 49  GLU C OE1 1 
ATOM   3819  O OE2 . GLU C 1 49  ? 31.204  16.841  -47.561  1.00 52.27 ? 49  GLU C OE2 1 
ATOM   3820  N N   . LEU C 1 50  ? 27.274  20.467  -44.960  1.00 28.62 ? 50  LEU C N   1 
ATOM   3821  C CA  . LEU C 1 50  ? 27.186  21.390  -43.810  1.00 26.27 ? 50  LEU C CA  1 
ATOM   3822  C C   . LEU C 1 50  ? 28.041  21.000  -42.608  1.00 24.61 ? 50  LEU C C   1 
ATOM   3823  O O   . LEU C 1 50  ? 28.239  19.820  -42.338  1.00 23.91 ? 50  LEU C O   1 
ATOM   3824  C CB  . LEU C 1 50  ? 25.748  21.501  -43.311  1.00 25.20 ? 50  LEU C CB  1 
ATOM   3825  C CG  . LEU C 1 50  ? 24.716  22.102  -44.246  1.00 24.63 ? 50  LEU C CG  1 
ATOM   3826  C CD1 . LEU C 1 50  ? 23.415  22.266  -43.498  1.00 25.08 ? 50  LEU C CD1 1 
ATOM   3827  C CD2 . LEU C 1 50  ? 25.147  23.437  -44.799  1.00 23.95 ? 50  LEU C CD2 1 
ATOM   3828  N N   . VAL C 1 51  ? 28.513  22.011  -41.879  1.00 23.02 ? 51  VAL C N   1 
ATOM   3829  C CA  . VAL C 1 51  ? 29.069  21.837  -40.538  1.00 21.97 ? 51  VAL C CA  1 
ATOM   3830  C C   . VAL C 1 51  ? 28.298  22.774  -39.633  1.00 22.05 ? 51  VAL C C   1 
ATOM   3831  O O   . VAL C 1 51  ? 28.168  23.958  -39.935  1.00 24.04 ? 51  VAL C O   1 
ATOM   3832  C CB  . VAL C 1 51  ? 30.562  22.204  -40.483  1.00 21.73 ? 51  VAL C CB  1 
ATOM   3833  C CG1 . VAL C 1 51  ? 31.179  21.794  -39.161  1.00 21.55 ? 51  VAL C CG1 1 
ATOM   3834  C CG2 . VAL C 1 51  ? 31.311  21.559  -41.623  1.00 22.72 ? 51  VAL C CG2 1 
ATOM   3835  N N   . VAL C 1 52  ? 27.789  22.262  -38.514  1.00 21.27 ? 52  VAL C N   1 
ATOM   3836  C CA  . VAL C 1 52  ? 26.869  23.034  -37.678  1.00 19.64 ? 52  VAL C CA  1 
ATOM   3837  C C   . VAL C 1 52  ? 27.365  23.178  -36.247  1.00 18.97 ? 52  VAL C C   1 
ATOM   3838  O O   . VAL C 1 52  ? 27.731  22.206  -35.609  1.00 18.16 ? 52  VAL C O   1 
ATOM   3839  C CB  . VAL C 1 52  ? 25.475  22.382  -37.677  1.00 19.02 ? 52  VAL C CB  1 
ATOM   3840  C CG1 . VAL C 1 52  ? 24.487  23.204  -36.854  1.00 18.94 ? 52  VAL C CG1 1 
ATOM   3841  C CG2 . VAL C 1 52  ? 24.972  22.218  -39.110  1.00 18.76 ? 52  VAL C CG2 1 
ATOM   3842  N N   . ASP C 1 53  ? 27.365  24.408  -35.744  1.00 19.39 ? 53  ASP C N   1 
ATOM   3843  C CA  . ASP C 1 53  ? 27.759  24.661  -34.359  1.00 18.54 ? 53  ASP C CA  1 
ATOM   3844  C C   . ASP C 1 53  ? 26.769  25.568  -33.675  1.00 17.45 ? 53  ASP C C   1 
ATOM   3845  O O   . ASP C 1 53  ? 26.899  26.779  -33.724  1.00 17.98 ? 53  ASP C O   1 
ATOM   3846  C CB  . ASP C 1 53  ? 29.170  25.253  -34.282  1.00 18.48 ? 53  ASP C CB  1 
ATOM   3847  C CG  . ASP C 1 53  ? 29.830  24.974  -32.956  1.00 18.37 ? 53  ASP C CG  1 
ATOM   3848  O OD1 . ASP C 1 53  ? 29.370  25.513  -31.944  1.00 18.15 ? 53  ASP C OD1 1 
ATOM   3849  O OD2 . ASP C 1 53  ? 30.799  24.195  -32.913  1.00 19.12 ? 53  ASP C OD2 1 
ATOM   3850  N N   . GLY C 1 54  ? 25.779  24.959  -33.034  1.00 17.27 ? 54  GLY C N   1 
ATOM   3851  C CA  . GLY C 1 54  ? 24.771  25.694  -32.274  1.00 17.30 ? 54  GLY C CA  1 
ATOM   3852  C C   . GLY C 1 54  ? 24.885  25.441  -30.790  1.00 16.95 ? 54  GLY C C   1 
ATOM   3853  O O   . GLY C 1 54  ? 24.805  24.295  -30.349  1.00 17.33 ? 54  GLY C O   1 
ATOM   3854  N N   . LEU C 1 55  ? 25.073  26.512  -30.026  1.00 16.79 ? 55  LEU C N   1 
ATOM   3855  C CA  . LEU C 1 55  ? 25.207  26.437  -28.559  1.00 16.39 ? 55  LEU C CA  1 
ATOM   3856  C C   . LEU C 1 55  ? 24.082  27.191  -27.877  1.00 15.58 ? 55  LEU C C   1 
ATOM   3857  O O   . LEU C 1 55  ? 23.965  28.398  -28.026  1.00 14.97 ? 55  LEU C O   1 
ATOM   3858  C CB  . LEU C 1 55  ? 26.554  27.028  -28.099  1.00 16.87 ? 55  LEU C CB  1 
ATOM   3859  C CG  . LEU C 1 55  ? 26.796  27.143  -26.581  1.00 16.67 ? 55  LEU C CG  1 
ATOM   3860  C CD1 . LEU C 1 55  ? 26.743  25.781  -25.927  1.00 16.34 ? 55  LEU C CD1 1 
ATOM   3861  C CD2 . LEU C 1 55  ? 28.119  27.820  -26.269  1.00 16.87 ? 55  LEU C CD2 1 
ATOM   3862  N N   . SER C 1 56  ? 23.274  26.475  -27.105  1.00 15.84 ? 56  SER C N   1 
ATOM   3863  C CA  . SER C 1 56  ? 22.241  27.102  -26.290  1.00 15.90 ? 56  SER C CA  1 
ATOM   3864  C C   . SER C 1 56  ? 22.874  28.193  -25.447  1.00 15.73 ? 56  SER C C   1 
ATOM   3865  O O   . SER C 1 56  ? 23.899  27.984  -24.814  1.00 15.07 ? 56  SER C O   1 
ATOM   3866  C CB  . SER C 1 56  ? 21.538  26.078  -25.384  1.00 16.36 ? 56  SER C CB  1 
ATOM   3867  O OG  . SER C 1 56  ? 21.081  24.932  -26.112  1.00 17.04 ? 56  SER C OG  1 
ATOM   3868  N N   . GLY C 1 57  ? 22.280  29.381  -25.483  1.00 16.20 ? 57  GLY C N   1 
ATOM   3869  C CA  . GLY C 1 57  ? 22.695  30.503  -24.643  1.00 16.21 ? 57  GLY C CA  1 
ATOM   3870  C C   . GLY C 1 57  ? 23.715  31.449  -25.241  1.00 16.55 ? 57  GLY C C   1 
ATOM   3871  O O   . GLY C 1 57  ? 24.016  32.481  -24.643  1.00 19.53 ? 57  GLY C O   1 
ATOM   3872  N N   . ARG C 1 58  ? 24.217  31.133  -26.434  1.00 16.02 ? 58  ARG C N   1 
ATOM   3873  C CA  . ARG C 1 58  ? 25.366  31.831  -27.015  1.00 15.74 ? 58  ARG C CA  1 
ATOM   3874  C C   . ARG C 1 58  ? 25.042  33.243  -27.525  1.00 15.71 ? 58  ARG C C   1 
ATOM   3875  O O   . ARG C 1 58  ? 23.996  33.476  -28.172  1.00 17.11 ? 58  ARG C O   1 
ATOM   3876  C CB  . ARG C 1 58  ? 25.968  30.984  -28.135  1.00 16.27 ? 58  ARG C CB  1 
ATOM   3877  C CG  . ARG C 1 58  ? 27.111  31.622  -28.937  1.00 17.05 ? 58  ARG C CG  1 
ATOM   3878  C CD  . ARG C 1 58  ? 27.565  30.705  -30.082  1.00 17.51 ? 58  ARG C CD  1 
ATOM   3879  N NE  . ARG C 1 58  ? 28.533  29.689  -29.651  1.00 17.98 ? 58  ARG C NE  1 
ATOM   3880  C CZ  . ARG C 1 58  ? 28.794  28.546  -30.292  1.00 17.97 ? 58  ARG C CZ  1 
ATOM   3881  N NH1 . ARG C 1 58  ? 28.157  28.211  -31.403  1.00 18.32 ? 58  ARG C NH1 1 
ATOM   3882  N NH2 . ARG C 1 58  ? 29.703  27.720  -29.817  1.00 18.06 ? 58  ARG C NH2 1 
ATOM   3883  N N   . THR C 1 59  ? 25.957  34.170  -27.250  1.00 14.79 ? 59  THR C N   1 
ATOM   3884  C CA  . THR C 1 59  ? 25.843  35.559  -27.678  1.00 14.38 ? 59  THR C CA  1 
ATOM   3885  C C   . THR C 1 59  ? 26.798  35.821  -28.844  1.00 14.24 ? 59  THR C C   1 
ATOM   3886  O O   . THR C 1 59  ? 27.628  34.967  -29.177  1.00 14.91 ? 59  THR C O   1 
ATOM   3887  C CB  . THR C 1 59  ? 26.239  36.513  -26.544  1.00 14.49 ? 59  THR C CB  1 
ATOM   3888  O OG1 . THR C 1 59  ? 27.672  36.502  -26.363  1.00 14.54 ? 59  THR C OG1 1 
ATOM   3889  C CG2 . THR C 1 59  ? 25.536  36.122  -25.258  1.00 14.32 ? 59  THR C CG2 1 
ATOM   3890  N N   . THR C 1 60  ? 26.690  37.004  -29.448  1.00 13.18 ? 60  THR C N   1 
ATOM   3891  C CA  . THR C 1 60  ? 27.630  37.423  -30.468  1.00 12.75 ? 60  THR C CA  1 
ATOM   3892  C C   . THR C 1 60  ? 29.056  37.494  -29.906  1.00 12.52 ? 60  THR C C   1 
ATOM   3893  O O   . THR C 1 60  ? 29.923  36.710  -30.301  1.00 12.52 ? 60  THR C O   1 
ATOM   3894  C CB  . THR C 1 60  ? 27.289  38.802  -31.053  1.00 12.94 ? 60  THR C CB  1 
ATOM   3895  O OG1 . THR C 1 60  ? 27.112  39.753  -29.996  1.00 13.27 ? 60  THR C OG1 1 
ATOM   3896  C CG2 . THR C 1 60  ? 26.034  38.739  -31.886  1.00 13.16 ? 60  THR C CG2 1 
ATOM   3897  N N   . ASN C 1 61  ? 29.286  38.420  -28.977  1.00 12.01 ? 61  ASN C N   1 
ATOM   3898  C CA  . ASN C 1 61  ? 30.641  38.761  -28.546  1.00 11.56 ? 61  ASN C CA  1 
ATOM   3899  C C   . ASN C 1 61  ? 30.762  39.285  -27.109  1.00 11.56 ? 61  ASN C C   1 
ATOM   3900  O O   . ASN C 1 61  ? 31.691  40.035  -26.795  1.00 11.18 ? 61  ASN C O   1 
ATOM   3901  C CB  . ASN C 1 61  ? 31.201  39.817  -29.478  1.00 11.47 ? 61  ASN C CB  1 
ATOM   3902  C CG  . ASN C 1 61  ? 30.669  41.213  -29.173  1.00 11.35 ? 61  ASN C CG  1 
ATOM   3903  O OD1 . ASN C 1 61  ? 29.566  41.386  -28.656  1.00 11.01 ? 61  ASN C OD1 1 
ATOM   3904  N ND2 . ASN C 1 61  ? 31.470  42.210  -29.485  1.00 11.53 ? 61  ASN C ND2 1 
ATOM   3905  N N   . ILE C 1 62  ? 29.841  38.890  -26.233  1.00 11.65 ? 62  ILE C N   1 
ATOM   3906  C CA  . ILE C 1 62  ? 29.797  39.415  -24.871  1.00 11.61 ? 62  ILE C CA  1 
ATOM   3907  C C   . ILE C 1 62  ? 29.707  38.286  -23.859  1.00 12.18 ? 62  ILE C C   1 
ATOM   3908  O O   . ILE C 1 62  ? 28.975  37.311  -24.081  1.00 12.41 ? 62  ILE C O   1 
ATOM   3909  C CB  . ILE C 1 62  ? 28.603  40.366  -24.689  1.00 11.36 ? 62  ILE C CB  1 
ATOM   3910  C CG1 . ILE C 1 62  ? 28.657  41.052  -23.326  1.00 11.00 ? 62  ILE C CG1 1 
ATOM   3911  C CG2 . ILE C 1 62  ? 27.280  39.630  -24.881  1.00 11.57 ? 62  ILE C CG2 1 
ATOM   3912  C CD1 . ILE C 1 62  ? 27.679  42.196  -23.199  1.00 10.85 ? 62  ILE C CD1 1 
ATOM   3913  N N   . ASP C 1 63  ? 30.450  38.417  -22.755  1.00 13.06 ? 63  ASP C N   1 
ATOM   3914  C CA  . ASP C 1 63  ? 30.404  37.425  -21.671  1.00 14.04 ? 63  ASP C CA  1 
ATOM   3915  C C   . ASP C 1 63  ? 29.054  37.428  -20.962  1.00 14.82 ? 63  ASP C C   1 
ATOM   3916  O O   . ASP C 1 63  ? 28.488  38.490  -20.662  1.00 14.45 ? 63  ASP C O   1 
ATOM   3917  C CB  . ASP C 1 63  ? 31.469  37.685  -20.616  1.00 14.05 ? 63  ASP C CB  1 
ATOM   3918  C CG  . ASP C 1 63  ? 32.857  37.505  -21.141  1.00 14.36 ? 63  ASP C CG  1 
ATOM   3919  O OD1 . ASP C 1 63  ? 33.101  36.706  -22.087  1.00 15.26 ? 63  ASP C OD1 1 
ATOM   3920  O OD2 . ASP C 1 63  ? 33.725  38.178  -20.573  1.00 14.50 ? 63  ASP C OD2 1 
ATOM   3921  N N   . ASP C 1 64  ? 28.547  36.220  -20.700  1.00 15.49 ? 64  ASP C N   1 
ATOM   3922  C CA  . ASP C 1 64  ? 27.397  36.057  -19.836  1.00 15.70 ? 64  ASP C CA  1 
ATOM   3923  C C   . ASP C 1 64  ? 27.933  35.799  -18.421  1.00 15.09 ? 64  ASP C C   1 
ATOM   3924  O O   . ASP C 1 64  ? 28.631  34.801  -18.183  1.00 14.55 ? 64  ASP C O   1 
ATOM   3925  C CB  . ASP C 1 64  ? 26.522  34.905  -20.320  1.00 16.31 ? 64  ASP C CB  1 
ATOM   3926  C CG  . ASP C 1 64  ? 25.146  34.904  -19.651  1.00 17.20 ? 64  ASP C CG  1 
ATOM   3927  O OD1 . ASP C 1 64  ? 25.099  34.927  -18.402  1.00 17.80 ? 64  ASP C OD1 1 
ATOM   3928  O OD2 . ASP C 1 64  ? 24.119  34.894  -20.381  1.00 17.69 ? 64  ASP C OD2 1 
ATOM   3929  N N   . PRO C 1 65  ? 27.635  36.707  -17.472  1.00 14.50 ? 65  PRO C N   1 
ATOM   3930  C CA  . PRO C 1 65  ? 28.189  36.486  -16.129  1.00 13.90 ? 65  PRO C CA  1 
ATOM   3931  C C   . PRO C 1 65  ? 27.705  35.185  -15.469  1.00 13.23 ? 65  PRO C C   1 
ATOM   3932  O O   . PRO C 1 65  ? 28.325  34.731  -14.512  1.00 12.95 ? 65  PRO C O   1 
ATOM   3933  C CB  . PRO C 1 65  ? 27.748  37.736  -15.344  1.00 13.70 ? 65  PRO C CB  1 
ATOM   3934  C CG  . PRO C 1 65  ? 26.599  38.291  -16.101  1.00 14.03 ? 65  PRO C CG  1 
ATOM   3935  C CD  . PRO C 1 65  ? 26.800  37.922  -17.544  1.00 14.15 ? 65  PRO C CD  1 
ATOM   3936  N N   . ASN C 1 66  ? 26.644  34.583  -15.997  1.00 13.15 ? 66  ASN C N   1 
ATOM   3937  C CA  . ASN C 1 66  ? 26.131  33.316  -15.476  1.00 13.79 ? 66  ASN C CA  1 
ATOM   3938  C C   . ASN C 1 66  ? 26.812  32.061  -16.015  1.00 14.28 ? 66  ASN C C   1 
ATOM   3939  O O   . ASN C 1 66  ? 26.640  30.990  -15.461  1.00 15.32 ? 66  ASN C O   1 
ATOM   3940  C CB  . ASN C 1 66  ? 24.638  33.201  -15.759  1.00 13.91 ? 66  ASN C CB  1 
ATOM   3941  C CG  . ASN C 1 66  ? 23.849  34.316  -15.118  1.00 14.07 ? 66  ASN C CG  1 
ATOM   3942  O OD1 . ASN C 1 66  ? 23.680  34.341  -13.902  1.00 14.02 ? 66  ASN C OD1 1 
ATOM   3943  N ND2 . ASN C 1 66  ? 23.361  35.249  -15.932  1.00 14.30 ? 66  ASN C ND2 1 
ATOM   3944  N N   . ASP C 1 67  ? 27.567  32.181  -17.101  1.00 14.66 ? 67  ASP C N   1 
ATOM   3945  C CA  . ASP C 1 67  ? 28.178  31.016  -17.749  1.00 14.44 ? 67  ASP C CA  1 
ATOM   3946  C C   . ASP C 1 67  ? 29.317  31.460  -18.674  1.00 14.72 ? 67  ASP C C   1 
ATOM   3947  O O   . ASP C 1 67  ? 29.096  32.145  -19.686  1.00 13.94 ? 67  ASP C O   1 
ATOM   3948  C CB  . ASP C 1 67  ? 27.122  30.240  -18.542  1.00 14.42 ? 67  ASP C CB  1 
ATOM   3949  C CG  . ASP C 1 67  ? 27.603  28.892  -19.004  1.00 14.31 ? 67  ASP C CG  1 
ATOM   3950  O OD1 . ASP C 1 67  ? 28.834  28.607  -18.971  1.00 13.63 ? 67  ASP C OD1 1 
ATOM   3951  O OD2 . ASP C 1 67  ? 26.718  28.112  -19.410  1.00 14.71 ? 67  ASP C OD2 1 
ATOM   3952  N N   . PRO C 1 68  ? 30.553  31.065  -18.327  1.00 15.33 ? 68  PRO C N   1 
ATOM   3953  C CA  . PRO C 1 68  ? 31.687  31.526  -19.117  1.00 15.47 ? 68  PRO C CA  1 
ATOM   3954  C C   . PRO C 1 68  ? 31.844  30.911  -20.509  1.00 16.03 ? 68  PRO C C   1 
ATOM   3955  O O   . PRO C 1 68  ? 32.743  31.310  -21.214  1.00 16.54 ? 68  PRO C O   1 
ATOM   3956  C CB  . PRO C 1 68  ? 32.898  31.209  -18.242  1.00 15.10 ? 68  PRO C CB  1 
ATOM   3957  C CG  . PRO C 1 68  ? 32.440  30.262  -17.207  1.00 15.34 ? 68  PRO C CG  1 
ATOM   3958  C CD  . PRO C 1 68  ? 30.953  30.257  -17.159  1.00 15.41 ? 68  PRO C CD  1 
ATOM   3959  N N   . LYS C 1 69  ? 30.988  29.989  -20.936  1.00 16.80 ? 69  LYS C N   1 
ATOM   3960  C CA  . LYS C 1 69  ? 31.156  29.387  -22.279  1.00 17.52 ? 69  LYS C CA  1 
ATOM   3961  C C   . LYS C 1 69  ? 30.273  29.947  -23.393  1.00 17.22 ? 69  LYS C C   1 
ATOM   3962  O O   . LYS C 1 69  ? 30.250  29.389  -24.478  1.00 17.41 ? 69  LYS C O   1 
ATOM   3963  C CB  . LYS C 1 69  ? 30.974  27.865  -22.211  1.00 18.65 ? 69  LYS C CB  1 
ATOM   3964  C CG  . LYS C 1 69  ? 29.556  27.362  -21.983  1.00 18.98 ? 69  LYS C CG  1 
ATOM   3965  C CD  . LYS C 1 69  ? 29.565  25.843  -21.763  1.00 19.37 ? 69  LYS C CD  1 
ATOM   3966  C CE  . LYS C 1 69  ? 28.174  25.283  -21.520  1.00 19.64 ? 69  LYS C CE  1 
ATOM   3967  N NZ  . LYS C 1 69  ? 27.692  25.487  -20.138  1.00 19.90 ? 69  LYS C NZ  1 
ATOM   3968  N N   . LEU C 1 70  ? 29.569  31.045  -23.132  1.00 17.15 ? 70  LEU C N   1 
ATOM   3969  C CA  . LEU C 1 70  ? 28.506  31.519  -24.010  1.00 17.51 ? 70  LEU C CA  1 
ATOM   3970  C C   . LEU C 1 70  ? 28.889  32.663  -24.955  1.00 17.87 ? 70  LEU C C   1 
ATOM   3971  O O   . LEU C 1 70  ? 28.036  33.175  -25.682  1.00 19.41 ? 70  LEU C O   1 
ATOM   3972  C CB  . LEU C 1 70  ? 27.296  31.945  -23.184  1.00 17.72 ? 70  LEU C CB  1 
ATOM   3973  C CG  . LEU C 1 70  ? 26.710  30.862  -22.284  1.00 17.88 ? 70  LEU C CG  1 
ATOM   3974  C CD1 . LEU C 1 70  ? 25.475  31.394  -21.567  1.00 18.23 ? 70  LEU C CD1 1 
ATOM   3975  C CD2 . LEU C 1 70  ? 26.366  29.629  -23.096  1.00 18.17 ? 70  LEU C CD2 1 
ATOM   3976  N N   . ASN C 1 71  ? 30.151  33.049  -24.979  1.00 17.16 ? 71  ASN C N   1 
ATOM   3977  C CA  . ASN C 1 71  ? 30.581  34.134  -25.840  1.00 16.14 ? 71  ASN C CA  1 
ATOM   3978  C C   . ASN C 1 71  ? 31.028  33.604  -27.195  1.00 16.83 ? 71  ASN C C   1 
ATOM   3979  O O   . ASN C 1 71  ? 32.095  32.995  -27.311  1.00 17.43 ? 71  ASN C O   1 
ATOM   3980  C CB  . ASN C 1 71  ? 31.724  34.881  -25.169  1.00 15.32 ? 71  ASN C CB  1 
ATOM   3981  C CG  . ASN C 1 71  ? 32.046  36.183  -25.848  1.00 14.68 ? 71  ASN C CG  1 
ATOM   3982  O OD1 . ASN C 1 71  ? 32.025  36.285  -27.082  1.00 13.93 ? 71  ASN C OD1 1 
ATOM   3983  N ND2 . ASN C 1 71  ? 32.363  37.193  -25.044  1.00 14.27 ? 71  ASN C ND2 1 
ATOM   3984  N N   . GLY C 1 72  ? 30.220  33.841  -28.224  1.00 17.22 ? 72  GLY C N   1 
ATOM   3985  C CA  . GLY C 1 72  ? 30.532  33.371  -29.585  1.00 17.59 ? 72  GLY C CA  1 
ATOM   3986  C C   . GLY C 1 72  ? 31.943  33.703  -30.049  1.00 17.45 ? 72  GLY C C   1 
ATOM   3987  O O   . GLY C 1 72  ? 32.615  32.865  -30.649  1.00 17.99 ? 72  GLY C O   1 
ATOM   3988  N N   . ALA C 1 73  ? 32.393  34.921  -29.754  1.00 16.79 ? 73  ALA C N   1 
ATOM   3989  C CA  . ALA C 1 73  ? 33.684  35.409  -30.216  1.00 16.53 ? 73  ALA C CA  1 
ATOM   3990  C C   . ALA C 1 73  ? 34.874  34.755  -29.497  1.00 16.30 ? 73  ALA C C   1 
ATOM   3991  O O   . ALA C 1 73  ? 35.988  34.737  -30.027  1.00 16.09 ? 73  ALA C O   1 
ATOM   3992  C CB  . ALA C 1 73  ? 33.730  36.919  -30.073  1.00 16.69 ? 73  ALA C CB  1 
ATOM   3993  N N   . ASP C 1 74  ? 34.649  34.222  -28.296  1.00 15.84 ? 74  ASP C N   1 
ATOM   3994  C CA  . ASP C 1 74  ? 35.657  33.377  -27.645  1.00 15.47 ? 74  ASP C CA  1 
ATOM   3995  C C   . ASP C 1 74  ? 35.934  32.105  -28.452  1.00 15.11 ? 74  ASP C C   1 
ATOM   3996  O O   . ASP C 1 74  ? 37.029  31.602  -28.431  1.00 14.48 ? 74  ASP C O   1 
ATOM   3997  C CB  . ASP C 1 74  ? 35.216  32.958  -26.234  1.00 15.61 ? 74  ASP C CB  1 
ATOM   3998  C CG  . ASP C 1 74  ? 35.356  34.071  -25.201  1.00 15.61 ? 74  ASP C CG  1 
ATOM   3999  O OD1 . ASP C 1 74  ? 36.038  35.061  -25.458  1.00 16.37 ? 74  ASP C OD1 1 
ATOM   4000  O OD2 . ASP C 1 74  ? 34.782  33.978  -24.106  1.00 15.65 ? 74  ASP C OD2 1 
ATOM   4001  N N   . TYR C 1 75  ? 34.929  31.599  -29.154  1.00 15.62 ? 75  TYR C N   1 
ATOM   4002  C CA  . TYR C 1 75  ? 34.952  30.272  -29.797  1.00 16.16 ? 75  TYR C CA  1 
ATOM   4003  C C   . TYR C 1 75  ? 35.246  30.314  -31.304  1.00 16.99 ? 75  TYR C C   1 
ATOM   4004  O O   . TYR C 1 75  ? 35.895  29.393  -31.858  1.00 16.99 ? 75  TYR C O   1 
ATOM   4005  C CB  . TYR C 1 75  ? 33.572  29.662  -29.573  1.00 15.97 ? 75  TYR C CB  1 
ATOM   4006  C CG  . TYR C 1 75  ? 33.313  28.200  -29.880  1.00 15.65 ? 75  TYR C CG  1 
ATOM   4007  C CD1 . TYR C 1 75  ? 33.585  27.207  -28.947  1.00 15.74 ? 75  TYR C CD1 1 
ATOM   4008  C CD2 . TYR C 1 75  ? 32.664  27.826  -31.050  1.00 15.92 ? 75  TYR C CD2 1 
ATOM   4009  C CE1 . TYR C 1 75  ? 33.280  25.871  -29.203  1.00 15.61 ? 75  TYR C CE1 1 
ATOM   4010  C CE2 . TYR C 1 75  ? 32.359  26.499  -31.324  1.00 15.77 ? 75  TYR C CE2 1 
ATOM   4011  C CZ  . TYR C 1 75  ? 32.658  25.524  -30.384  1.00 15.48 ? 75  TYR C CZ  1 
ATOM   4012  O OH  . TYR C 1 75  ? 32.333  24.209  -30.620  1.00 15.32 ? 75  TYR C OH  1 
ATOM   4013  N N   . LEU C 1 76  ? 34.779  31.375  -31.965  1.00 17.54 ? 76  LEU C N   1 
ATOM   4014  C CA  . LEU C 1 76  ? 34.716  31.378  -33.417  1.00 17.92 ? 76  LEU C CA  1 
ATOM   4015  C C   . LEU C 1 76  ? 36.079  31.256  -34.127  1.00 18.06 ? 76  LEU C C   1 
ATOM   4016  O O   . LEU C 1 76  ? 36.180  30.514  -35.101  1.00 19.32 ? 76  LEU C O   1 
ATOM   4017  C CB  . LEU C 1 76  ? 33.942  32.595  -33.928  1.00 17.91 ? 76  LEU C CB  1 
ATOM   4018  C CG  . LEU C 1 76  ? 33.684  32.610  -35.446  1.00 17.78 ? 76  LEU C CG  1 
ATOM   4019  C CD1 . LEU C 1 76  ? 32.963  31.361  -35.903  1.00 17.76 ? 76  LEU C CD1 1 
ATOM   4020  C CD2 . LEU C 1 76  ? 32.902  33.836  -35.867  1.00 17.76 ? 76  LEU C CD2 1 
ATOM   4021  N N   . PRO C 1 77  ? 37.119  31.974  -33.655  1.00 17.95 ? 77  PRO C N   1 
ATOM   4022  C CA  . PRO C 1 77  ? 38.411  31.846  -34.305  1.00 18.39 ? 77  PRO C CA  1 
ATOM   4023  C C   . PRO C 1 77  ? 38.878  30.398  -34.429  1.00 19.26 ? 77  PRO C C   1 
ATOM   4024  O O   . PRO C 1 77  ? 39.300  29.966  -35.523  1.00 20.52 ? 77  PRO C O   1 
ATOM   4025  C CB  . PRO C 1 77  ? 39.344  32.626  -33.373  1.00 18.13 ? 77  PRO C CB  1 
ATOM   4026  C CG  . PRO C 1 77  ? 38.482  33.724  -32.905  1.00 18.36 ? 77  PRO C CG  1 
ATOM   4027  C CD  . PRO C 1 77  ? 37.165  33.034  -32.636  1.00 18.33 ? 77  PRO C CD  1 
ATOM   4028  N N   . ALA C 1 78  ? 38.775  29.651  -33.322  1.00 18.55 ? 78  ALA C N   1 
ATOM   4029  C CA  . ALA C 1 78  ? 39.178  28.256  -33.314  1.00 17.71 ? 78  ALA C CA  1 
ATOM   4030  C C   . ALA C 1 78  ? 38.308  27.431  -34.254  1.00 17.10 ? 78  ALA C C   1 
ATOM   4031  O O   . ALA C 1 78  ? 38.807  26.617  -35.016  1.00 16.64 ? 78  ALA C O   1 
ATOM   4032  C CB  . ALA C 1 78  ? 39.115  27.702  -31.896  1.00 17.60 ? 78  ALA C CB  1 
ATOM   4033  N N   . ALA C 1 79  ? 37.001  27.650  -34.184  1.00 17.30 ? 79  ALA C N   1 
ATOM   4034  C CA  . ALA C 1 79  ? 36.052  26.897  -34.987  1.00 16.72 ? 79  ALA C CA  1 
ATOM   4035  C C   . ALA C 1 79  ? 36.339  27.061  -36.475  1.00 16.55 ? 79  ALA C C   1 
ATOM   4036  O O   . ALA C 1 79  ? 36.362  26.090  -37.224  1.00 16.30 ? 79  ALA C O   1 
ATOM   4037  C CB  . ALA C 1 79  ? 34.631  27.333  -34.649  1.00 16.60 ? 79  ALA C CB  1 
ATOM   4038  N N   . LEU C 1 80  ? 36.576  28.294  -36.895  1.00 17.44 ? 80  LEU C N   1 
ATOM   4039  C CA  . LEU C 1 80  ? 36.838  28.589  -38.300  1.00 17.94 ? 80  LEU C CA  1 
ATOM   4040  C C   . LEU C 1 80  ? 38.059  27.843  -38.840  1.00 18.27 ? 80  LEU C C   1 
ATOM   4041  O O   . LEU C 1 80  ? 38.018  27.297  -39.952  1.00 18.37 ? 80  LEU C O   1 
ATOM   4042  C CB  . LEU C 1 80  ? 37.045  30.089  -38.480  1.00 18.05 ? 80  LEU C CB  1 
ATOM   4043  C CG  . LEU C 1 80  ? 35.815  30.970  -38.333  1.00 18.01 ? 80  LEU C CG  1 
ATOM   4044  C CD1 . LEU C 1 80  ? 36.246  32.404  -38.138  1.00 18.37 ? 80  LEU C CD1 1 
ATOM   4045  C CD2 . LEU C 1 80  ? 34.881  30.831  -39.528  1.00 18.03 ? 80  LEU C CD2 1 
ATOM   4046  N N   . ALA C 1 81  ? 39.128  27.827  -38.038  1.00 18.14 ? 81  ALA C N   1 
ATOM   4047  C CA  . ALA C 1 81  ? 40.392  27.197  -38.406  1.00 17.93 ? 81  ALA C CA  1 
ATOM   4048  C C   . ALA C 1 81  ? 40.282  25.678  -38.415  1.00 18.46 ? 81  ALA C C   1 
ATOM   4049  O O   . ALA C 1 81  ? 41.004  24.984  -39.147  1.00 18.77 ? 81  ALA C O   1 
ATOM   4050  C CB  . ALA C 1 81  ? 41.485  27.619  -37.442  1.00 17.42 ? 81  ALA C CB  1 
ATOM   4051  N N   . ALA C 1 82  ? 39.392  25.178  -37.565  1.00 19.03 ? 82  ALA C N   1 
ATOM   4052  C CA  . ALA C 1 82  ? 39.168  23.755  -37.399  1.00 19.47 ? 82  ALA C CA  1 
ATOM   4053  C C   . ALA C 1 82  ? 38.331  23.169  -38.537  1.00 20.69 ? 82  ALA C C   1 
ATOM   4054  O O   . ALA C 1 82  ? 38.346  21.942  -38.752  1.00 20.98 ? 82  ALA C O   1 
ATOM   4055  C CB  . ALA C 1 82  ? 38.493  23.492  -36.064  1.00 19.09 ? 82  ALA C CB  1 
ATOM   4056  N N   . HIS C 1 83  ? 37.588  24.028  -39.239  1.00 20.96 ? 83  HIS C N   1 
ATOM   4057  C CA  . HIS C 1 83  ? 36.742  23.588  -40.344  1.00 21.15 ? 83  HIS C CA  1 
ATOM   4058  C C   . HIS C 1 83  ? 37.158  24.152  -41.705  1.00 21.87 ? 83  HIS C C   1 
ATOM   4059  O O   . HIS C 1 83  ? 36.497  23.889  -42.709  1.00 22.42 ? 83  HIS C O   1 
ATOM   4060  C CB  . HIS C 1 83  ? 35.290  23.913  -40.036  1.00 20.79 ? 83  HIS C CB  1 
ATOM   4061  C CG  . HIS C 1 83  ? 34.819  23.328  -38.745  1.00 20.88 ? 83  HIS C CG  1 
ATOM   4062  N ND1 . HIS C 1 83  ? 34.979  21.999  -38.439  1.00 22.07 ? 83  HIS C ND1 1 
ATOM   4063  C CD2 . HIS C 1 83  ? 34.199  23.887  -37.680  1.00 21.20 ? 83  HIS C CD2 1 
ATOM   4064  C CE1 . HIS C 1 83  ? 34.481  21.763  -37.238  1.00 22.79 ? 83  HIS C CE1 1 
ATOM   4065  N NE2 . HIS C 1 83  ? 34.004  22.896  -36.754  1.00 21.95 ? 83  HIS C NE2 1 
ATOM   4066  N N   . GLU C 1 84  ? 38.261  24.902  -41.748  1.00 22.39 ? 84  GLU C N   1 
ATOM   4067  C CA  . GLU C 1 84  ? 38.846  25.343  -43.013  1.00 22.28 ? 84  GLU C CA  1 
ATOM   4068  C C   . GLU C 1 84  ? 39.153  24.112  -43.901  1.00 22.35 ? 84  GLU C C   1 
ATOM   4069  O O   . GLU C 1 84  ? 39.670  23.104  -43.396  1.00 23.10 ? 84  GLU C O   1 
ATOM   4070  C CB  . GLU C 1 84  ? 40.132  26.139  -42.752  1.00 22.37 ? 84  GLU C CB  1 
ATOM   4071  C CG  . GLU C 1 84  ? 40.710  26.813  -43.991  1.00 22.71 ? 84  GLU C CG  1 
ATOM   4072  C CD  . GLU C 1 84  ? 42.018  27.528  -43.759  1.00 23.22 ? 84  GLU C CD  1 
ATOM   4073  O OE1 . GLU C 1 84  ? 42.137  28.656  -44.296  1.00 21.97 ? 84  GLU C OE1 1 
ATOM   4074  O OE2 . GLU C 1 84  ? 42.915  26.975  -43.050  1.00 25.17 ? 84  GLU C OE2 1 
ATOM   4075  N N   . PRO C 1 85  ? 38.859  24.167  -45.204  1.00 22.41 ? 85  PRO C N   1 
ATOM   4076  C CA  . PRO C 1 85  ? 38.347  25.353  -45.901  1.00 22.24 ? 85  PRO C CA  1 
ATOM   4077  C C   . PRO C 1 85  ? 36.839  25.373  -46.035  1.00 21.60 ? 85  PRO C C   1 
ATOM   4078  O O   . PRO C 1 85  ? 36.220  24.329  -46.222  1.00 20.46 ? 85  PRO C O   1 
ATOM   4079  C CB  . PRO C 1 85  ? 38.958  25.214  -47.291  1.00 23.22 ? 85  PRO C CB  1 
ATOM   4080  C CG  . PRO C 1 85  ? 39.003  23.731  -47.506  1.00 23.46 ? 85  PRO C CG  1 
ATOM   4081  C CD  . PRO C 1 85  ? 39.264  23.110  -46.151  1.00 22.79 ? 85  PRO C CD  1 
ATOM   4082  N N   . LEU C 1 86  ? 36.267  26.569  -45.959  1.00 21.40 ? 86  LEU C N   1 
ATOM   4083  C CA  . LEU C 1 86  ? 34.843  26.751  -46.102  1.00 21.35 ? 86  LEU C CA  1 
ATOM   4084  C C   . LEU C 1 86  ? 34.542  27.634  -47.316  1.00 20.84 ? 86  LEU C C   1 
ATOM   4085  O O   . LEU C 1 86  ? 35.353  28.451  -47.730  1.00 19.17 ? 86  LEU C O   1 
ATOM   4086  C CB  . LEU C 1 86  ? 34.261  27.381  -44.830  1.00 21.75 ? 86  LEU C CB  1 
ATOM   4087  C CG  . LEU C 1 86  ? 34.451  26.577  -43.536  1.00 21.31 ? 86  LEU C CG  1 
ATOM   4088  C CD1 . LEU C 1 86  ? 34.230  27.441  -42.311  1.00 21.33 ? 86  LEU C CD1 1 
ATOM   4089  C CD2 . LEU C 1 86  ? 33.541  25.362  -43.480  1.00 21.64 ? 86  LEU C CD2 1 
ATOM   4090  N N   . ASP C 1 87  ? 33.343  27.460  -47.856  1.00 21.26 ? 87  ASP C N   1 
ATOM   4091  C CA  . ASP C 1 87  ? 32.832  28.286  -48.931  1.00 21.38 ? 87  ASP C CA  1 
ATOM   4092  C C   . ASP C 1 87  ? 31.866  29.354  -48.441  1.00 20.69 ? 87  ASP C C   1 
ATOM   4093  O O   . ASP C 1 87  ? 31.647  30.341  -49.146  1.00 20.79 ? 87  ASP C O   1 
ATOM   4094  C CB  . ASP C 1 87  ? 32.149  27.393  -49.965  1.00 21.98 ? 87  ASP C CB  1 
ATOM   4095  C CG  . ASP C 1 87  ? 33.119  26.470  -50.633  1.00 23.05 ? 87  ASP C CG  1 
ATOM   4096  O OD1 . ASP C 1 87  ? 33.455  25.441  -49.993  1.00 23.93 ? 87  ASP C OD1 1 
ATOM   4097  O OD2 . ASP C 1 87  ? 33.583  26.788  -51.760  1.00 23.82 ? 87  ASP C OD2 1 
ATOM   4098  N N   . LEU C 1 88  ? 31.281  29.138  -47.258  1.00 19.63 ? 88  LEU C N   1 
ATOM   4099  C CA  . LEU C 1 88  ? 30.366  30.097  -46.638  1.00 19.18 ? 88  LEU C CA  1 
ATOM   4100  C C   . LEU C 1 88  ? 30.286  29.933  -45.110  1.00 20.07 ? 88  LEU C C   1 
ATOM   4101  O O   . LEU C 1 88  ? 30.336  28.825  -44.577  1.00 20.08 ? 88  LEU C O   1 
ATOM   4102  C CB  . LEU C 1 88  ? 28.972  29.982  -47.243  1.00 18.10 ? 88  LEU C CB  1 
ATOM   4103  C CG  . LEU C 1 88  ? 27.948  31.050  -46.799  1.00 17.53 ? 88  LEU C CG  1 
ATOM   4104  C CD1 . LEU C 1 88  ? 28.328  32.445  -47.289  1.00 17.08 ? 88  LEU C CD1 1 
ATOM   4105  C CD2 . LEU C 1 88  ? 26.549  30.712  -47.300  1.00 17.52 ? 88  LEU C CD2 1 
ATOM   4106  N N   . VAL C 1 89  ? 30.161  31.060  -44.410  1.00 20.25 ? 89  VAL C N   1 
ATOM   4107  C CA  . VAL C 1 89  ? 29.889  31.053  -42.980  1.00 19.81 ? 89  VAL C CA  1 
ATOM   4108  C C   . VAL C 1 89  ? 28.554  31.742  -42.749  1.00 19.54 ? 89  VAL C C   1 
ATOM   4109  O O   . VAL C 1 89  ? 28.366  32.883  -43.156  1.00 18.41 ? 89  VAL C O   1 
ATOM   4110  C CB  . VAL C 1 89  ? 30.988  31.774  -42.184  1.00 20.35 ? 89  VAL C CB  1 
ATOM   4111  C CG1 . VAL C 1 89  ? 30.615  31.890  -40.718  1.00 20.60 ? 89  VAL C CG1 1 
ATOM   4112  C CG2 . VAL C 1 89  ? 32.325  31.052  -42.334  1.00 21.06 ? 89  VAL C CG2 1 
ATOM   4113  N N   . ILE C 1 90  ? 27.629  31.028  -42.111  1.00 20.05 ? 90  ILE C N   1 
ATOM   4114  C CA  . ILE C 1 90  ? 26.330  31.570  -41.771  1.00 20.98 ? 90  ILE C CA  1 
ATOM   4115  C C   . ILE C 1 90  ? 26.310  31.836  -40.284  1.00 20.41 ? 90  ILE C C   1 
ATOM   4116  O O   . ILE C 1 90  ? 26.668  30.961  -39.495  1.00 21.55 ? 90  ILE C O   1 
ATOM   4117  C CB  . ILE C 1 90  ? 25.208  30.586  -42.117  1.00 22.94 ? 90  ILE C CB  1 
ATOM   4118  C CG1 . ILE C 1 90  ? 25.086  30.454  -43.648  1.00 24.03 ? 90  ILE C CG1 1 
ATOM   4119  C CG2 . ILE C 1 90  ? 23.882  31.058  -41.523  1.00 23.38 ? 90  ILE C CG2 1 
ATOM   4120  C CD1 . ILE C 1 90  ? 24.061  29.454  -44.129  1.00 23.70 ? 90  ILE C CD1 1 
ATOM   4121  N N   . ILE C 1 91  ? 25.893  33.043  -39.902  1.00 19.05 ? 91  ILE C N   1 
ATOM   4122  C CA  . ILE C 1 91  ? 25.824  33.425  -38.495  1.00 18.04 ? 91  ILE C CA  1 
ATOM   4123  C C   . ILE C 1 91  ? 24.384  33.774  -38.203  1.00 17.70 ? 91  ILE C C   1 
ATOM   4124  O O   . ILE C 1 91  ? 23.846  34.683  -38.820  1.00 18.18 ? 91  ILE C O   1 
ATOM   4125  C CB  . ILE C 1 91  ? 26.719  34.635  -38.165  1.00 17.97 ? 91  ILE C CB  1 
ATOM   4126  C CG1 . ILE C 1 91  ? 28.181  34.314  -38.470  1.00 18.63 ? 91  ILE C CG1 1 
ATOM   4127  C CG2 . ILE C 1 91  ? 26.601  35.040  -36.696  1.00 17.93 ? 91  ILE C CG2 1 
ATOM   4128  C CD1 . ILE C 1 91  ? 29.111  35.517  -38.441  1.00 18.88 ? 91  ILE C CD1 1 
ATOM   4129  N N   . LEU C 1 92  ? 23.766  33.022  -37.297  1.00 17.64 ? 92  LEU C N   1 
ATOM   4130  C CA  . LEU C 1 92  ? 22.432  33.315  -36.802  1.00 17.91 ? 92  LEU C CA  1 
ATOM   4131  C C   . LEU C 1 92  ? 22.496  33.395  -35.281  1.00 18.02 ? 92  LEU C C   1 
ATOM   4132  O O   . LEU C 1 92  ? 22.306  32.382  -34.555  1.00 17.82 ? 92  LEU C O   1 
ATOM   4133  C CB  . LEU C 1 92  ? 21.433  32.240  -37.247  1.00 18.14 ? 92  LEU C CB  1 
ATOM   4134  C CG  . LEU C 1 92  ? 20.026  32.267  -36.653  1.00 17.35 ? 92  LEU C CG  1 
ATOM   4135  C CD1 . LEU C 1 92  ? 19.435  33.635  -36.884  1.00 16.97 ? 92  LEU C CD1 1 
ATOM   4136  C CD2 . LEU C 1 92  ? 19.186  31.172  -37.289  1.00 16.94 ? 92  LEU C CD2 1 
ATOM   4137  N N   . LEU C 1 93  ? 22.790  34.614  -34.829  1.00 18.14 ? 93  LEU C N   1 
ATOM   4138  C CA  . LEU C 1 93  ? 22.946  34.959  -33.425  1.00 18.89 ? 93  LEU C CA  1 
ATOM   4139  C C   . LEU C 1 93  ? 22.335  36.319  -33.177  1.00 19.26 ? 93  LEU C C   1 
ATOM   4140  O O   . LEU C 1 93  ? 22.142  37.101  -34.107  1.00 18.21 ? 93  LEU C O   1 
ATOM   4141  C CB  . LEU C 1 93  ? 24.437  35.057  -33.065  1.00 18.86 ? 93  LEU C CB  1 
ATOM   4142  C CG  . LEU C 1 93  ? 25.214  33.753  -32.934  1.00 19.22 ? 93  LEU C CG  1 
ATOM   4143  C CD1 . LEU C 1 93  ? 26.686  34.080  -32.784  1.00 19.52 ? 93  LEU C CD1 1 
ATOM   4144  C CD2 . LEU C 1 93  ? 24.708  32.888  -31.768  1.00 19.77 ? 93  LEU C CD2 1 
ATOM   4145  N N   . GLY C 1 94  ? 22.092  36.605  -31.904  1.00 20.79 ? 94  GLY C N   1 
ATOM   4146  C CA  . GLY C 1 94  ? 21.539  37.896  -31.481  1.00 21.88 ? 94  GLY C CA  1 
ATOM   4147  C C   . GLY C 1 94  ? 20.348  37.763  -30.539  1.00 23.01 ? 94  GLY C C   1 
ATOM   4148  O O   . GLY C 1 94  ? 19.992  38.719  -29.847  1.00 23.83 ? 94  GLY C O   1 
ATOM   4149  N N   . THR C 1 95  ? 19.718  36.592  -30.512  1.00 22.95 ? 95  THR C N   1 
ATOM   4150  C CA  . THR C 1 95  ? 18.544  36.398  -29.679  1.00 21.63 ? 95  THR C CA  1 
ATOM   4151  C C   . THR C 1 95  ? 18.938  36.476  -28.198  1.00 20.05 ? 95  THR C C   1 
ATOM   4152  O O   . THR C 1 95  ? 18.283  37.188  -27.430  1.00 20.06 ? 95  THR C O   1 
ATOM   4153  C CB  . THR C 1 95  ? 17.838  35.069  -30.042  1.00 22.58 ? 95  THR C CB  1 
ATOM   4154  O OG1 . THR C 1 95  ? 17.601  35.030  -31.467  1.00 23.40 ? 95  THR C OG1 1 
ATOM   4155  C CG2 . THR C 1 95  ? 16.535  34.917  -29.302  1.00 22.27 ? 95  THR C CG2 1 
ATOM   4156  N N   . ASN C 1 96  ? 20.024  35.811  -27.796  1.00 18.12 ? 96  ASN C N   1 
ATOM   4157  C CA  . ASN C 1 96  ? 20.457  35.895  -26.393  1.00 16.71 ? 96  ASN C CA  1 
ATOM   4158  C C   . ASN C 1 96  ? 21.009  37.266  -26.003  1.00 15.97 ? 96  ASN C C   1 
ATOM   4159  O O   . ASN C 1 96  ? 20.976  37.648  -24.842  1.00 15.11 ? 96  ASN C O   1 
ATOM   4160  C CB  . ASN C 1 96  ? 21.490  34.819  -26.071  1.00 16.12 ? 96  ASN C CB  1 
ATOM   4161  C CG  . ASN C 1 96  ? 20.934  33.422  -26.176  1.00 15.43 ? 96  ASN C CG  1 
ATOM   4162  O OD1 . ASN C 1 96  ? 20.066  33.032  -25.413  1.00 15.23 ? 96  ASN C OD1 1 
ATOM   4163  N ND2 . ASN C 1 96  ? 21.446  32.658  -27.117  1.00 15.47 ? 96  ASN C ND2 1 
ATOM   4164  N N   . ASP C 1 97  ? 21.509  38.008  -26.981  1.00 15.97 ? 97  ASP C N   1 
ATOM   4165  C CA  . ASP C 1 97  ? 22.050  39.346  -26.728  1.00 16.30 ? 97  ASP C CA  1 
ATOM   4166  C C   . ASP C 1 97  ? 20.996  40.346  -26.232  1.00 16.24 ? 97  ASP C C   1 
ATOM   4167  O O   . ASP C 1 97  ? 21.335  41.385  -25.667  1.00 16.30 ? 97  ASP C O   1 
ATOM   4168  C CB  . ASP C 1 97  ? 22.711  39.907  -27.999  1.00 16.65 ? 97  ASP C CB  1 
ATOM   4169  C CG  . ASP C 1 97  ? 23.925  39.095  -28.442  1.00 17.02 ? 97  ASP C CG  1 
ATOM   4170  O OD1 . ASP C 1 97  ? 23.737  37.924  -28.858  1.00 17.20 ? 97  ASP C OD1 1 
ATOM   4171  O OD2 . ASP C 1 97  ? 25.065  39.633  -28.386  1.00 16.58 ? 97  ASP C OD2 1 
ATOM   4172  N N   . THR C 1 98  ? 19.719  40.033  -26.451  1.00 16.08 ? 98  THR C N   1 
ATOM   4173  C CA  . THR C 1 98  ? 18.621  40.888  -26.007  1.00 15.32 ? 98  THR C CA  1 
ATOM   4174  C C   . THR C 1 98  ? 18.278  40.689  -24.527  1.00 14.83 ? 98  THR C C   1 
ATOM   4175  O O   . THR C 1 98  ? 17.492  41.466  -23.966  1.00 14.97 ? 98  THR C O   1 
ATOM   4176  C CB  . THR C 1 98  ? 17.354  40.628  -26.837  1.00 15.30 ? 98  THR C CB  1 
ATOM   4177  O OG1 . THR C 1 98  ? 16.847  39.309  -26.533  1.00 15.47 ? 98  THR C OG1 1 
ATOM   4178  C CG2 . THR C 1 98  ? 17.639  40.770  -28.335  1.00 14.78 ? 98  THR C CG2 1 
ATOM   4179  N N   . LYS C 1 99  ? 18.857  39.663  -23.904  1.00 14.49 ? 99  LYS C N   1 
ATOM   4180  C CA  . LYS C 1 99  ? 18.647  39.404  -22.481  1.00 14.35 ? 99  LYS C CA  1 
ATOM   4181  C C   . LYS C 1 99  ? 18.950  40.649  -21.676  1.00 14.31 ? 99  LYS C C   1 
ATOM   4182  O O   . LYS C 1 99  ? 19.984  41.292  -21.835  1.00 13.33 ? 99  LYS C O   1 
ATOM   4183  C CB  . LYS C 1 99  ? 19.500  38.230  -21.961  1.00 14.12 ? 99  LYS C CB  1 
ATOM   4184  C CG  . LYS C 1 99  ? 19.007  36.867  -22.395  1.00 14.14 ? 99  LYS C CG  1 
ATOM   4185  C CD  . LYS C 1 99  ? 19.950  35.727  -22.008  1.00 14.15 ? 99  LYS C CD  1 
ATOM   4186  C CE  . LYS C 1 99  ? 19.241  34.387  -22.262  1.00 13.98 ? 99  LYS C CE  1 
ATOM   4187  N NZ  . LYS C 1 99  ? 20.117  33.213  -22.392  1.00 14.13 ? 99  LYS C NZ  1 
ATOM   4188  N N   . THR C 1 100 ? 18.003  40.962  -20.800  1.00 15.07 ? 100 THR C N   1 
ATOM   4189  C CA  . THR C 1 100 ? 17.998  42.179  -20.004  1.00 15.34 ? 100 THR C CA  1 
ATOM   4190  C C   . THR C 1 100 ? 19.317  42.460  -19.301  1.00 14.45 ? 100 THR C C   1 
ATOM   4191  O O   . THR C 1 100 ? 19.862  43.539  -19.419  1.00 14.16 ? 100 THR C O   1 
ATOM   4192  C CB  . THR C 1 100 ? 16.818  42.138  -19.034  1.00 16.24 ? 100 THR C CB  1 
ATOM   4193  O OG1 . THR C 1 100 ? 16.570  43.443  -18.574  1.00 16.59 ? 100 THR C OG1 1 
ATOM   4194  C CG2 . THR C 1 100 ? 16.919  41.106  -17.888  1.00 17.76 ? 100 THR C CG2 1 
ATOM   4195  N N   . TYR C 1 101 ? 19.841  41.471  -18.596  1.00 14.19 ? 101 TYR C N   1 
ATOM   4196  C CA  . TYR C 1 101 ? 21.047  41.655  -17.771  1.00 13.73 ? 101 TYR C CA  1 
ATOM   4197  C C   . TYR C 1 101 ? 22.323  41.946  -18.555  1.00 13.94 ? 101 TYR C C   1 
ATOM   4198  O O   . TYR C 1 101 ? 23.272  42.430  -17.971  1.00 13.91 ? 101 TYR C O   1 
ATOM   4199  C CB  . TYR C 1 101 ? 21.252  40.472  -16.809  1.00 12.85 ? 101 TYR C CB  1 
ATOM   4200  C CG  . TYR C 1 101 ? 21.410  39.115  -17.435  1.00 12.38 ? 101 TYR C CG  1 
ATOM   4201  C CD1 . TYR C 1 101 ? 22.621  38.713  -17.972  1.00 12.46 ? 101 TYR C CD1 1 
ATOM   4202  C CD2 . TYR C 1 101 ? 20.355  38.198  -17.445  1.00 12.33 ? 101 TYR C CD2 1 
ATOM   4203  C CE1 . TYR C 1 101 ? 22.782  37.439  -18.531  1.00 12.69 ? 101 TYR C CE1 1 
ATOM   4204  C CE2 . TYR C 1 101 ? 20.506  36.920  -17.980  1.00 12.09 ? 101 TYR C CE2 1 
ATOM   4205  C CZ  . TYR C 1 101 ? 21.715  36.549  -18.528  1.00 12.31 ? 101 TYR C CZ  1 
ATOM   4206  O OH  . TYR C 1 101 ? 21.857  35.317  -19.077  1.00 12.11 ? 101 TYR C OH  1 
ATOM   4207  N N   . LEU C 1 102 ? 22.356  41.662  -19.858  1.00 14.08 ? 102 LEU C N   1 
ATOM   4208  C CA  . LEU C 1 102 ? 23.523  42.007  -20.678  1.00 14.10 ? 102 LEU C CA  1 
ATOM   4209  C C   . LEU C 1 102 ? 23.504  43.481  -21.098  1.00 14.26 ? 102 LEU C C   1 
ATOM   4210  O O   . LEU C 1 102 ? 24.509  44.013  -21.573  1.00 13.65 ? 102 LEU C O   1 
ATOM   4211  C CB  . LEU C 1 102 ? 23.589  41.127  -21.913  1.00 14.09 ? 102 LEU C CB  1 
ATOM   4212  C CG  . LEU C 1 102 ? 23.629  39.622  -21.647  1.00 14.16 ? 102 LEU C CG  1 
ATOM   4213  C CD1 . LEU C 1 102 ? 23.474  38.845  -22.948  1.00 14.72 ? 102 LEU C CD1 1 
ATOM   4214  C CD2 . LEU C 1 102 ? 24.907  39.235  -20.978  1.00 14.07 ? 102 LEU C CD2 1 
ATOM   4215  N N   . ASN C 1 103 ? 22.346  44.121  -20.954  1.00 14.92 ? 103 ASN C N   1 
ATOM   4216  C CA  . ASN C 1 103 ? 22.225  45.562  -21.085  1.00 15.20 ? 103 ASN C CA  1 
ATOM   4217  C C   . ASN C 1 103 ? 22.726  46.114  -22.439  1.00 14.77 ? 103 ASN C C   1 
ATOM   4218  O O   . ASN C 1 103 ? 23.410  47.138  -22.490  1.00 13.96 ? 103 ASN C O   1 
ATOM   4219  C CB  . ASN C 1 103 ? 22.940  46.207  -19.898  1.00 16.30 ? 103 ASN C CB  1 
ATOM   4220  C CG  . ASN C 1 103 ? 22.735  47.711  -19.833  1.00 17.46 ? 103 ASN C CG  1 
ATOM   4221  O OD1 . ASN C 1 103 ? 21.599  48.193  -19.783  1.00 18.54 ? 103 ASN C OD1 1 
ATOM   4222  N ND2 . ASN C 1 103 ? 23.843  48.461  -19.841  1.00 17.50 ? 103 ASN C ND2 1 
ATOM   4223  N N   . ARG C 1 104 ? 22.362  45.440  -23.530  1.00 14.75 ? 104 ARG C N   1 
ATOM   4224  C CA  . ARG C 1 104 ? 22.840  45.833  -24.858  1.00 14.97 ? 104 ARG C CA  1 
ATOM   4225  C C   . ARG C 1 104 ? 21.795  46.597  -25.667  1.00 14.68 ? 104 ARG C C   1 
ATOM   4226  O O   . ARG C 1 104 ? 20.602  46.294  -25.615  1.00 13.70 ? 104 ARG C O   1 
ATOM   4227  C CB  . ARG C 1 104 ? 23.248  44.601  -25.675  1.00 15.28 ? 104 ARG C CB  1 
ATOM   4228  C CG  . ARG C 1 104 ? 23.978  43.521  -24.902  1.00 15.43 ? 104 ARG C CG  1 
ATOM   4229  C CD  . ARG C 1 104 ? 24.817  42.689  -25.872  1.00 15.60 ? 104 ARG C CD  1 
ATOM   4230  N NE  . ARG C 1 104 ? 26.112  43.309  -26.160  1.00 15.60 ? 104 ARG C NE  1 
ATOM   4231  C CZ  . ARG C 1 104 ? 27.013  42.822  -27.011  1.00 15.85 ? 104 ARG C CZ  1 
ATOM   4232  N NH1 . ARG C 1 104 ? 26.789  41.697  -27.696  1.00 16.11 ? 104 ARG C NH1 1 
ATOM   4233  N NH2 . ARG C 1 104 ? 28.164  43.454  -27.171  1.00 15.91 ? 104 ARG C NH2 1 
ATOM   4234  N N   . THR C 1 105 ? 22.280  47.558  -26.445  1.00 14.93 ? 105 THR C N   1 
ATOM   4235  C CA  . THR C 1 105 ? 21.461  48.238  -27.414  1.00 15.45 ? 105 THR C CA  1 
ATOM   4236  C C   . THR C 1 105 ? 21.555  47.434  -28.709  1.00 16.25 ? 105 THR C C   1 
ATOM   4237  O O   . THR C 1 105 ? 22.470  46.634  -28.873  1.00 15.84 ? 105 THR C O   1 
ATOM   4238  C CB  . THR C 1 105 ? 21.991  49.645  -27.703  1.00 15.81 ? 105 THR C CB  1 
ATOM   4239  O OG1 . THR C 1 105 ? 23.226  49.567  -28.428  1.00 16.15 ? 105 THR C OG1 1 
ATOM   4240  C CG2 . THR C 1 105 ? 22.257  50.413  -26.413  1.00 15.90 ? 105 THR C CG2 1 
ATOM   4241  N N   . PRO C 1 106 ? 20.607  47.642  -29.636  1.00 17.16 ? 106 PRO C N   1 
ATOM   4242  C CA  . PRO C 1 106 ? 20.671  46.980  -30.934  1.00 17.32 ? 106 PRO C CA  1 
ATOM   4243  C C   . PRO C 1 106 ? 21.936  47.284  -31.717  1.00 17.93 ? 106 PRO C C   1 
ATOM   4244  O O   . PRO C 1 106 ? 22.486  46.376  -32.342  1.00 20.11 ? 106 PRO C O   1 
ATOM   4245  C CB  . PRO C 1 106 ? 19.451  47.534  -31.667  1.00 17.43 ? 106 PRO C CB  1 
ATOM   4246  C CG  . PRO C 1 106 ? 18.484  47.841  -30.579  1.00 17.21 ? 106 PRO C CG  1 
ATOM   4247  C CD  . PRO C 1 106 ? 19.329  48.356  -29.447  1.00 17.19 ? 106 PRO C CD  1 
ATOM   4248  N N   . PHE C 1 107 ? 22.394  48.532  -31.685  1.00 17.89 ? 107 PHE C N   1 
ATOM   4249  C CA  . PHE C 1 107 ? 23.645  48.912  -32.365  1.00 17.72 ? 107 PHE C CA  1 
ATOM   4250  C C   . PHE C 1 107 ? 24.815  48.140  -31.763  1.00 17.22 ? 107 PHE C C   1 
ATOM   4251  O O   . PHE C 1 107 ? 25.693  47.668  -32.480  1.00 16.50 ? 107 PHE C O   1 
ATOM   4252  C CB  . PHE C 1 107 ? 23.892  50.436  -32.257  1.00 17.85 ? 107 PHE C CB  1 
ATOM   4253  C CG  . PHE C 1 107 ? 25.205  50.880  -32.848  1.00 17.39 ? 107 PHE C CG  1 
ATOM   4254  C CD1 . PHE C 1 107 ? 25.435  50.767  -34.212  1.00 17.61 ? 107 PHE C CD1 1 
ATOM   4255  C CD2 . PHE C 1 107 ? 26.209  51.400  -32.057  1.00 17.16 ? 107 PHE C CD2 1 
ATOM   4256  C CE1 . PHE C 1 107 ? 26.640  51.176  -34.775  1.00 17.34 ? 107 PHE C CE1 1 
ATOM   4257  C CE2 . PHE C 1 107 ? 27.424  51.795  -32.605  1.00 17.39 ? 107 PHE C CE2 1 
ATOM   4258  C CZ  . PHE C 1 107 ? 27.645  51.673  -33.969  1.00 17.26 ? 107 PHE C CZ  1 
ATOM   4259  N N   . GLU C 1 108 ? 24.820  48.003  -30.444  1.00 17.31 ? 108 GLU C N   1 
ATOM   4260  C CA  . GLU C 1 108 ? 25.865  47.241  -29.784  1.00 18.35 ? 108 GLU C CA  1 
ATOM   4261  C C   . GLU C 1 108 ? 25.866  45.787  -30.269  1.00 17.84 ? 108 GLU C C   1 
ATOM   4262  O O   . GLU C 1 108 ? 26.918  45.194  -30.458  1.00 17.39 ? 108 GLU C O   1 
ATOM   4263  C CB  . GLU C 1 108 ? 25.664  47.272  -28.274  1.00 19.11 ? 108 GLU C CB  1 
ATOM   4264  C CG  . GLU C 1 108 ? 26.802  46.630  -27.527  1.00 19.01 ? 108 GLU C CG  1 
ATOM   4265  C CD  . GLU C 1 108 ? 26.631  46.786  -26.024  1.00 19.30 ? 108 GLU C CD  1 
ATOM   4266  O OE1 . GLU C 1 108 ? 26.663  45.761  -25.303  1.00 19.84 ? 108 GLU C OE1 1 
ATOM   4267  O OE2 . GLU C 1 108 ? 26.446  47.941  -25.567  1.00 18.64 ? 108 GLU C OE2 1 
ATOM   4268  N N   . ILE C 1 109 ? 24.679  45.229  -30.452  1.00 17.35 ? 109 ILE C N   1 
ATOM   4269  C CA  . ILE C 1 109 ? 24.544  43.845  -30.868  1.00 17.49 ? 109 ILE C CA  1 
ATOM   4270  C C   . ILE C 1 109 ? 25.014  43.700  -32.320  1.00 16.77 ? 109 ILE C C   1 
ATOM   4271  O O   . ILE C 1 109 ? 25.680  42.719  -32.669  1.00 16.74 ? 109 ILE C O   1 
ATOM   4272  C CB  . ILE C 1 109 ? 23.096  43.327  -30.695  1.00 18.08 ? 109 ILE C CB  1 
ATOM   4273  C CG1 . ILE C 1 109 ? 22.674  43.431  -29.214  1.00 18.98 ? 109 ILE C CG1 1 
ATOM   4274  C CG2 . ILE C 1 109 ? 22.990  41.875  -31.162  1.00 17.85 ? 109 ILE C CG2 1 
ATOM   4275  C CD1 . ILE C 1 109 ? 21.188  43.285  -28.958  1.00 19.26 ? 109 ILE C CD1 1 
ATOM   4276  N N   . GLY C 1 110 ? 24.694  44.684  -33.149  1.00 15.60 ? 110 GLY C N   1 
ATOM   4277  C CA  . GLY C 1 110 ? 25.250  44.746  -34.483  1.00 15.53 ? 110 GLY C CA  1 
ATOM   4278  C C   . GLY C 1 110 ? 26.777  44.724  -34.497  1.00 15.65 ? 110 GLY C C   1 
ATOM   4279  O O   . GLY C 1 110 ? 27.394  43.969  -35.261  1.00 15.79 ? 110 GLY C O   1 
ATOM   4280  N N   . LEU C 1 111 ? 27.390  45.556  -33.652  1.00 15.82 ? 111 LEU C N   1 
ATOM   4281  C CA  . LEU C 1 111 ? 28.845  45.575  -33.512  1.00 15.26 ? 111 LEU C CA  1 
ATOM   4282  C C   . LEU C 1 111 ? 29.391  44.199  -33.129  1.00 15.27 ? 111 LEU C C   1 
ATOM   4283  O O   . LEU C 1 111 ? 30.469  43.801  -33.584  1.00 15.16 ? 111 LEU C O   1 
ATOM   4284  C CB  . LEU C 1 111 ? 29.272  46.604  -32.462  1.00 14.86 ? 111 LEU C CB  1 
ATOM   4285  C CG  . LEU C 1 111 ? 29.085  48.054  -32.831  1.00 14.77 ? 111 LEU C CG  1 
ATOM   4286  C CD1 . LEU C 1 111 ? 29.443  48.948  -31.671  1.00 14.86 ? 111 LEU C CD1 1 
ATOM   4287  C CD2 . LEU C 1 111 ? 29.953  48.403  -34.004  1.00 14.70 ? 111 LEU C CD2 1 
ATOM   4288  N N   . GLY C 1 112 ? 28.640  43.488  -32.292  1.00 15.50 ? 112 GLY C N   1 
ATOM   4289  C CA  . GLY C 1 112 ? 29.010  42.152  -31.871  1.00 15.71 ? 112 GLY C CA  1 
ATOM   4290  C C   . GLY C 1 112 ? 29.032  41.193  -33.035  1.00 15.98 ? 112 GLY C C   1 
ATOM   4291  O O   . GLY C 1 112 ? 29.999  40.439  -33.214  1.00 15.60 ? 112 GLY C O   1 
ATOM   4292  N N   . ALA C 1 113 ? 27.970  41.233  -33.839  1.00 16.07 ? 113 ALA C N   1 
ATOM   4293  C CA  . ALA C 1 113 ? 27.916  40.436  -35.060  1.00 15.55 ? 113 ALA C CA  1 
ATOM   4294  C C   . ALA C 1 113 ? 29.053  40.850  -35.977  1.00 15.45 ? 113 ALA C C   1 
ATOM   4295  O O   . ALA C 1 113 ? 29.686  40.002  -36.589  1.00 14.58 ? 113 ALA C O   1 
ATOM   4296  C CB  . ALA C 1 113 ? 26.581  40.610  -35.767  1.00 15.66 ? 113 ALA C CB  1 
ATOM   4297  N N   . GLY C 1 114 ? 29.309  42.157  -36.056  1.00 16.09 ? 114 GLY C N   1 
ATOM   4298  C CA  . GLY C 1 114 ? 30.454  42.690  -36.805  1.00 16.96 ? 114 GLY C CA  1 
ATOM   4299  C C   . GLY C 1 114 ? 31.806  42.135  -36.364  1.00 17.20 ? 114 GLY C C   1 
ATOM   4300  O O   . GLY C 1 114 ? 32.654  41.801  -37.191  1.00 16.21 ? 114 GLY C O   1 
ATOM   4301  N N   . ALA C 1 115 ? 31.999  42.032  -35.056  1.00 18.42 ? 115 ALA C N   1 
ATOM   4302  C CA  . ALA C 1 115 ? 33.205  41.423  -34.496  1.00 18.96 ? 115 ALA C CA  1 
ATOM   4303  C C   . ALA C 1 115 ? 33.407  40.020  -35.030  1.00 19.71 ? 115 ALA C C   1 
ATOM   4304  O O   . ALA C 1 115 ? 34.546  39.621  -35.319  1.00 20.51 ? 115 ALA C O   1 
ATOM   4305  C CB  . ALA C 1 115 ? 33.140  41.386  -32.971  1.00 18.73 ? 115 ALA C CB  1 
ATOM   4306  N N   . LEU C 1 116 ? 32.308  39.275  -35.153  1.00 19.73 ? 116 LEU C N   1 
ATOM   4307  C CA  . LEU C 1 116 ? 32.383  37.908  -35.656  1.00 19.28 ? 116 LEU C CA  1 
ATOM   4308  C C   . LEU C 1 116 ? 32.708  37.892  -37.151  1.00 18.83 ? 116 LEU C C   1 
ATOM   4309  O O   . LEU C 1 116 ? 33.529  37.108  -37.594  1.00 18.99 ? 116 LEU C O   1 
ATOM   4310  C CB  . LEU C 1 116 ? 31.082  37.147  -35.363  1.00 19.39 ? 116 LEU C CB  1 
ATOM   4311  C CG  . LEU C 1 116 ? 30.724  36.967  -33.882  1.00 19.31 ? 116 LEU C CG  1 
ATOM   4312  C CD1 . LEU C 1 116 ? 29.390  36.255  -33.727  1.00 18.88 ? 116 LEU C CD1 1 
ATOM   4313  C CD2 . LEU C 1 116 ? 31.824  36.229  -33.142  1.00 19.57 ? 116 LEU C CD2 1 
ATOM   4314  N N   . ILE C 1 117 ? 32.077  38.772  -37.921  1.00 18.28 ? 117 ILE C N   1 
ATOM   4315  C CA  . ILE C 1 117 ? 32.369  38.884  -39.348  1.00 18.16 ? 117 ILE C CA  1 
ATOM   4316  C C   . ILE C 1 117 ? 33.854  39.163  -39.551  1.00 18.18 ? 117 ILE C C   1 
ATOM   4317  O O   . ILE C 1 117 ? 34.507  38.535  -40.390  1.00 18.64 ? 117 ILE C O   1 
ATOM   4318  C CB  . ILE C 1 117 ? 31.527  39.986  -40.039  1.00 17.99 ? 117 ILE C CB  1 
ATOM   4319  C CG1 . ILE C 1 117 ? 30.054  39.554  -40.098  1.00 18.06 ? 117 ILE C CG1 1 
ATOM   4320  C CG2 . ILE C 1 117 ? 32.016  40.223  -41.458  1.00 17.92 ? 117 ILE C CG2 1 
ATOM   4321  C CD1 . ILE C 1 117 ? 29.082  40.666  -40.402  1.00 18.07 ? 117 ILE C CD1 1 
ATOM   4322  N N   . ASN C 1 118 ? 34.381  40.104  -38.775  1.00 17.83 ? 118 ASN C N   1 
ATOM   4323  C CA  . ASN C 1 118 ? 35.796  40.433  -38.824  1.00 17.47 ? 118 ASN C CA  1 
ATOM   4324  C C   . ASN C 1 118 ? 36.693  39.219  -38.518  1.00 18.21 ? 118 ASN C C   1 
ATOM   4325  O O   . ASN C 1 118 ? 37.719  39.012  -39.171  1.00 18.70 ? 118 ASN C O   1 
ATOM   4326  C CB  . ASN C 1 118 ? 36.113  41.578  -37.878  1.00 16.78 ? 118 ASN C CB  1 
ATOM   4327  C CG  . ASN C 1 118 ? 37.524  42.092  -38.067  1.00 16.85 ? 118 ASN C CG  1 
ATOM   4328  O OD1 . ASN C 1 118 ? 38.028  42.238  -39.203  1.00 17.32 ? 118 ASN C OD1 1 
ATOM   4329  N ND2 . ASN C 1 118 ? 38.183  42.357  -36.961  1.00 16.69 ? 118 ASN C ND2 1 
ATOM   4330  N N   . MET C 1 119 ? 36.321  38.414  -37.528  1.00 18.02 ? 119 MET C N   1 
ATOM   4331  C CA  . MET C 1 119 ? 37.078  37.194  -37.234  1.00 17.57 ? 119 MET C CA  1 
ATOM   4332  C C   . MET C 1 119 ? 37.108  36.243  -38.440  1.00 17.65 ? 119 MET C C   1 
ATOM   4333  O O   . MET C 1 119 ? 38.136  35.623  -38.713  1.00 17.56 ? 119 MET C O   1 
ATOM   4334  C CB  . MET C 1 119 ? 36.517  36.487  -36.003  1.00 17.34 ? 119 MET C CB  1 
ATOM   4335  C CG  . MET C 1 119 ? 36.885  37.169  -34.714  1.00 17.08 ? 119 MET C CG  1 
ATOM   4336  S SD  . MET C 1 119 ? 35.918  36.568  -33.321  1.00 17.64 ? 119 MET C SD  1 
ATOM   4337  C CE  . MET C 1 119 ? 36.980  37.081  -31.958  1.00 17.37 ? 119 MET C CE  1 
ATOM   4338  N N   . VAL C 1 120 ? 35.990  36.147  -39.155  1.00 17.49 ? 120 VAL C N   1 
ATOM   4339  C CA  . VAL C 1 120 ? 35.919  35.330  -40.361  1.00 17.31 ? 120 VAL C CA  1 
ATOM   4340  C C   . VAL C 1 120 ? 36.813  35.912  -41.464  1.00 16.51 ? 120 VAL C C   1 
ATOM   4341  O O   . VAL C 1 120 ? 37.471  35.173  -42.183  1.00 15.80 ? 120 VAL C O   1 
ATOM   4342  C CB  . VAL C 1 120 ? 34.466  35.198  -40.903  1.00 17.26 ? 120 VAL C CB  1 
ATOM   4343  C CG1 . VAL C 1 120 ? 34.453  34.368  -42.205  1.00 16.87 ? 120 VAL C CG1 1 
ATOM   4344  C CG2 . VAL C 1 120 ? 33.543  34.589  -39.849  1.00 16.89 ? 120 VAL C CG2 1 
ATOM   4345  N N   . GLN C 1 121 ? 36.827  37.233  -41.599  1.00 16.08 ? 121 GLN C N   1 
ATOM   4346  C CA  . GLN C 1 121 ? 37.610  37.891  -42.648  1.00 15.79 ? 121 GLN C CA  1 
ATOM   4347  C C   . GLN C 1 121 ? 39.112  37.773  -42.420  1.00 15.63 ? 121 GLN C C   1 
ATOM   4348  O O   . GLN C 1 121 ? 39.884  37.718  -43.364  1.00 16.15 ? 121 GLN C O   1 
ATOM   4349  C CB  . GLN C 1 121 ? 37.201  39.365  -42.788  1.00 15.61 ? 121 GLN C CB  1 
ATOM   4350  C CG  . GLN C 1 121 ? 35.824  39.522  -43.393  1.00 15.41 ? 121 GLN C CG  1 
ATOM   4351  C CD  . GLN C 1 121 ? 35.426  40.955  -43.615  1.00 14.71 ? 121 GLN C CD  1 
ATOM   4352  O OE1 . GLN C 1 121 ? 36.093  41.874  -43.163  1.00 14.64 ? 121 GLN C OE1 1 
ATOM   4353  N NE2 . GLN C 1 121 ? 34.341  41.153  -44.348  1.00 14.25 ? 121 GLN C NE2 1 
ATOM   4354  N N   . LYS C 1 122 ? 39.515  37.742  -41.160  1.00 15.41 ? 122 LYS C N   1 
ATOM   4355  C CA  . LYS C 1 122 ? 40.914  37.529  -40.792  1.00 15.57 ? 122 LYS C CA  1 
ATOM   4356  C C   . LYS C 1 122 ? 41.206  36.056  -40.515  1.00 15.54 ? 122 LYS C C   1 
ATOM   4357  O O   . LYS C 1 122 ? 42.242  35.730  -39.982  1.00 14.49 ? 122 LYS C O   1 
ATOM   4358  C CB  . LYS C 1 122 ? 41.244  38.363  -39.553  1.00 15.65 ? 122 LYS C CB  1 
ATOM   4359  C CG  . LYS C 1 122 ? 40.928  39.843  -39.724  1.00 15.84 ? 122 LYS C CG  1 
ATOM   4360  C CD  . LYS C 1 122 ? 41.144  40.623  -38.448  1.00 15.66 ? 122 LYS C CD  1 
ATOM   4361  C CE  . LYS C 1 122 ? 42.613  40.923  -38.222  1.00 15.45 ? 122 LYS C CE  1 
ATOM   4362  N NZ  . LYS C 1 122 ? 42.922  41.069  -36.772  1.00 15.72 ? 122 LYS C NZ  1 
ATOM   4363  N N   . SER C 1 123 ? 40.298  35.179  -40.931  1.00 16.93 ? 123 SER C N   1 
ATOM   4364  C CA  . SER C 1 123 ? 40.323  33.747  -40.608  1.00 17.12 ? 123 SER C CA  1 
ATOM   4365  C C   . SER C 1 123 ? 41.535  33.064  -41.205  1.00 17.39 ? 123 SER C C   1 
ATOM   4366  O O   . SER C 1 123 ? 42.005  33.463  -42.281  1.00 16.98 ? 123 SER C O   1 
ATOM   4367  C CB  . SER C 1 123 ? 39.075  33.067  -41.150  1.00 17.68 ? 123 SER C CB  1 
ATOM   4368  O OG  . SER C 1 123 ? 38.692  32.037  -40.309  1.00 18.31 ? 123 SER C OG  1 
ATOM   4369  N N   . PRO C 1 124 ? 41.879  31.888  -40.657  1.00 18.86 ? 124 PRO C N   1 
ATOM   4370  C CA  . PRO C 1 124 ? 43.055  31.441  -39.899  1.00 19.74 ? 124 PRO C CA  1 
ATOM   4371  C C   . PRO C 1 124 ? 44.032  32.574  -39.730  1.00 20.80 ? 124 PRO C C   1 
ATOM   4372  O O   . PRO C 1 124 ? 44.200  33.368  -40.648  1.00 23.48 ? 124 PRO C O   1 
ATOM   4373  C CB  . PRO C 1 124 ? 43.639  30.349  -40.793  1.00 19.11 ? 124 PRO C CB  1 
ATOM   4374  C CG  . PRO C 1 124 ? 43.125  30.634  -42.135  1.00 18.60 ? 124 PRO C CG  1 
ATOM   4375  C CD  . PRO C 1 124 ? 41.699  30.958  -41.793  1.00 18.96 ? 124 PRO C CD  1 
ATOM   4376  N N   . GLY C 1 125 ? 44.703  32.677  -38.611  1.00 20.29 ? 125 GLY C N   1 
ATOM   4377  C CA  . GLY C 1 125 ? 45.630  33.800  -38.513  1.00 20.41 ? 125 GLY C CA  1 
ATOM   4378  C C   . GLY C 1 125 ? 47.034  33.459  -38.956  1.00 20.27 ? 125 GLY C C   1 
ATOM   4379  O O   . GLY C 1 125 ? 47.972  33.860  -38.294  1.00 21.41 ? 125 GLY C O   1 
ATOM   4380  N N   . TRP C 1 126 ? 47.210  32.700  -40.039  1.00 20.38 ? 126 TRP C N   1 
ATOM   4381  C CA  . TRP C 1 126 ? 48.491  32.007  -40.228  1.00 21.71 ? 126 TRP C CA  1 
ATOM   4382  C C   . TRP C 1 126 ? 48.949  31.593  -41.633  1.00 22.80 ? 126 TRP C C   1 
ATOM   4383  O O   . TRP C 1 126 ? 48.165  31.499  -42.577  1.00 23.70 ? 126 TRP C O   1 
ATOM   4384  C CB  . TRP C 1 126 ? 48.539  30.784  -39.295  1.00 21.92 ? 126 TRP C CB  1 
ATOM   4385  C CG  . TRP C 1 126 ? 47.496  29.687  -39.548  1.00 21.21 ? 126 TRP C CG  1 
ATOM   4386  C CD1 . TRP C 1 126 ? 47.040  29.232  -40.750  1.00 20.34 ? 126 TRP C CD1 1 
ATOM   4387  C CD2 . TRP C 1 126 ? 46.862  28.874  -38.547  1.00 20.99 ? 126 TRP C CD2 1 
ATOM   4388  N NE1 . TRP C 1 126 ? 46.158  28.199  -40.560  1.00 20.14 ? 126 TRP C NE1 1 
ATOM   4389  C CE2 . TRP C 1 126 ? 46.039  27.949  -39.219  1.00 20.47 ? 126 TRP C CE2 1 
ATOM   4390  C CE3 . TRP C 1 126 ? 46.924  28.830  -37.143  1.00 20.60 ? 126 TRP C CE3 1 
ATOM   4391  C CZ2 . TRP C 1 126 ? 45.243  27.022  -38.540  1.00 20.02 ? 126 TRP C CZ2 1 
ATOM   4392  C CZ3 . TRP C 1 126 ? 46.151  27.885  -36.473  1.00 20.00 ? 126 TRP C CZ3 1 
ATOM   4393  C CH2 . TRP C 1 126 ? 45.320  27.002  -37.173  1.00 19.68 ? 126 TRP C CH2 1 
ATOM   4394  N N   . ASP C 1 127 ? 50.248  31.350  -41.733  1.00 24.38 ? 127 ASP C N   1 
ATOM   4395  C CA  . ASP C 1 127 ? 50.900  30.794  -42.930  1.00 25.09 ? 127 ASP C CA  1 
ATOM   4396  C C   . ASP C 1 127 ? 50.797  29.262  -43.038  1.00 24.39 ? 127 ASP C C   1 
ATOM   4397  O O   . ASP C 1 127 ? 51.249  28.703  -44.032  1.00 24.51 ? 127 ASP C O   1 
ATOM   4398  C CB  . ASP C 1 127 ? 52.383  31.234  -43.010  1.00 26.93 ? 127 ASP C CB  1 
ATOM   4399  C CG  . ASP C 1 127 ? 53.240  30.796  -41.768  1.00 29.40 ? 127 ASP C CG  1 
ATOM   4400  O OD1 . ASP C 1 127 ? 52.645  30.445  -40.723  1.00 32.55 ? 127 ASP C OD1 1 
ATOM   4401  O OD2 . ASP C 1 127 ? 54.489  30.787  -41.842  1.00 28.54 ? 127 ASP C OD2 1 
ATOM   4402  N N   . TRP C 1 128 ? 50.228  28.586  -42.039  1.00 23.51 ? 128 TRP C N   1 
ATOM   4403  C CA  . TRP C 1 128 ? 50.202  27.115  -42.017  1.00 23.65 ? 128 TRP C CA  1 
ATOM   4404  C C   . TRP C 1 128 ? 49.359  26.515  -43.149  1.00 24.19 ? 128 TRP C C   1 
ATOM   4405  O O   . TRP C 1 128 ? 49.628  25.410  -43.607  1.00 26.18 ? 128 TRP C O   1 
ATOM   4406  C CB  . TRP C 1 128 ? 49.699  26.580  -40.675  1.00 23.30 ? 128 TRP C CB  1 
ATOM   4407  C CG  . TRP C 1 128 ? 50.552  26.964  -39.485  1.00 23.58 ? 128 TRP C CG  1 
ATOM   4408  C CD1 . TRP C 1 128 ? 51.766  27.562  -39.516  1.00 23.39 ? 128 TRP C CD1 1 
ATOM   4409  C CD2 . TRP C 1 128 ? 50.255  26.744  -38.089  1.00 23.20 ? 128 TRP C CD2 1 
ATOM   4410  N NE1 . TRP C 1 128 ? 52.232  27.760  -38.243  1.00 23.27 ? 128 TRP C NE1 1 
ATOM   4411  C CE2 . TRP C 1 128 ? 51.322  27.278  -37.347  1.00 22.88 ? 128 TRP C CE2 1 
ATOM   4412  C CE3 . TRP C 1 128 ? 49.174  26.183  -37.398  1.00 22.61 ? 128 TRP C CE3 1 
ATOM   4413  C CZ2 . TRP C 1 128 ? 51.364  27.242  -35.948  1.00 23.02 ? 128 TRP C CZ2 1 
ATOM   4414  C CZ3 . TRP C 1 128 ? 49.221  26.141  -36.008  1.00 23.08 ? 128 TRP C CZ3 1 
ATOM   4415  C CH2 . TRP C 1 128 ? 50.302  26.682  -35.299  1.00 23.07 ? 128 TRP C CH2 1 
ATOM   4416  N N   . THR C 1 129 ? 48.347  27.251  -43.584  1.00 23.32 ? 129 THR C N   1 
ATOM   4417  C CA  . THR C 1 129 ? 47.539  26.924  -44.748  1.00 23.02 ? 129 THR C CA  1 
ATOM   4418  C C   . THR C 1 129 ? 47.432  28.209  -45.534  1.00 23.08 ? 129 THR C C   1 
ATOM   4419  O O   . THR C 1 129 ? 47.624  29.292  -44.948  1.00 22.79 ? 129 THR C O   1 
ATOM   4420  C CB  . THR C 1 129 ? 46.090  26.474  -44.353  1.00 23.08 ? 129 THR C CB  1 
ATOM   4421  O OG1 . THR C 1 129 ? 45.402  27.523  -43.634  1.00 22.56 ? 129 THR C OG1 1 
ATOM   4422  C CG2 . THR C 1 129 ? 46.133  25.230  -43.481  1.00 22.64 ? 129 THR C CG2 1 
ATOM   4423  N N   . ASP C 1 130 ? 47.137  28.140  -46.833  1.00 23.06 ? 130 ASP C N   1 
ATOM   4424  C CA  . ASP C 1 130 ? 46.614  29.363  -47.455  1.00 23.61 ? 130 ASP C CA  1 
ATOM   4425  C C   . ASP C 1 130 ? 45.496  29.107  -48.432  1.00 21.96 ? 130 ASP C C   1 
ATOM   4426  O O   . ASP C 1 130 ? 45.675  29.036  -49.632  1.00 21.31 ? 130 ASP C O   1 
ATOM   4427  C CB  . ASP C 1 130 ? 47.717  30.390  -47.938  1.00 24.44 ? 130 ASP C CB  1 
ATOM   4428  C CG  . ASP C 1 130 ? 48.020  30.317  -49.400  1.00 23.74 ? 130 ASP C CG  1 
ATOM   4429  O OD1 . ASP C 1 130 ? 48.546  29.293  -49.853  1.00 25.06 ? 130 ASP C OD1 1 
ATOM   4430  O OD2 . ASP C 1 130 ? 47.784  31.316  -50.095  1.00 23.46 ? 130 ASP C OD2 1 
ATOM   4431  N N   . TYR C 1 131 ? 44.324  28.942  -47.832  1.00 21.66 ? 131 TYR C N   1 
ATOM   4432  C CA  . TYR C 1 131 ? 43.044  29.059  -48.502  1.00 20.52 ? 131 TYR C CA  1 
ATOM   4433  C C   . TYR C 1 131 ? 42.573  30.496  -48.259  1.00 19.93 ? 131 TYR C C   1 
ATOM   4434  O O   . TYR C 1 131 ? 42.980  31.146  -47.292  1.00 20.10 ? 131 TYR C O   1 
ATOM   4435  C CB  . TYR C 1 131 ? 42.055  28.105  -47.863  1.00 20.65 ? 131 TYR C CB  1 
ATOM   4436  C CG  . TYR C 1 131 ? 42.421  26.630  -47.896  1.00 21.34 ? 131 TYR C CG  1 
ATOM   4437  C CD1 . TYR C 1 131 ? 42.094  25.828  -48.982  1.00 21.37 ? 131 TYR C CD1 1 
ATOM   4438  C CD2 . TYR C 1 131 ? 43.048  26.022  -46.808  1.00 21.47 ? 131 TYR C CD2 1 
ATOM   4439  C CE1 . TYR C 1 131 ? 42.415  24.475  -49.001  1.00 21.42 ? 131 TYR C CE1 1 
ATOM   4440  C CE2 . TYR C 1 131 ? 43.343  24.668  -46.814  1.00 21.88 ? 131 TYR C CE2 1 
ATOM   4441  C CZ  . TYR C 1 131 ? 43.035  23.903  -47.916  1.00 21.38 ? 131 TYR C CZ  1 
ATOM   4442  O OH  . TYR C 1 131 ? 43.311  22.560  -47.935  1.00 21.66 ? 131 TYR C OH  1 
ATOM   4443  N N   . PRO C 1 132 ? 41.705  31.019  -49.123  1.00 20.00 ? 132 PRO C N   1 
ATOM   4444  C CA  . PRO C 1 132 ? 41.158  32.348  -48.843  1.00 20.07 ? 132 PRO C CA  1 
ATOM   4445  C C   . PRO C 1 132 ? 40.208  32.324  -47.637  1.00 19.78 ? 132 PRO C C   1 
ATOM   4446  O O   . PRO C 1 132 ? 39.796  31.249  -47.206  1.00 19.38 ? 132 PRO C O   1 
ATOM   4447  C CB  . PRO C 1 132 ? 40.381  32.654  -50.130  1.00 20.05 ? 132 PRO C CB  1 
ATOM   4448  C CG  . PRO C 1 132 ? 39.964  31.312  -50.648  1.00 19.50 ? 132 PRO C CG  1 
ATOM   4449  C CD  . PRO C 1 132 ? 41.127  30.430  -50.347  1.00 19.91 ? 132 PRO C CD  1 
ATOM   4450  N N   . PRO C 1 133 ? 39.837  33.492  -47.113  1.00 19.89 ? 133 PRO C N   1 
ATOM   4451  C CA  . PRO C 1 133 ? 38.758  33.473  -46.113  1.00 20.10 ? 133 PRO C CA  1 
ATOM   4452  C C   . PRO C 1 133 ? 37.390  33.354  -46.789  1.00 19.31 ? 133 PRO C C   1 
ATOM   4453  O O   . PRO C 1 133 ? 37.219  33.837  -47.898  1.00 19.78 ? 133 PRO C O   1 
ATOM   4454  C CB  . PRO C 1 133 ? 38.918  34.816  -45.385  1.00 19.82 ? 133 PRO C CB  1 
ATOM   4455  C CG  . PRO C 1 133 ? 39.727  35.689  -46.309  1.00 19.54 ? 133 PRO C CG  1 
ATOM   4456  C CD  . PRO C 1 133 ? 40.221  34.863  -47.481  1.00 19.53 ? 133 PRO C CD  1 
ATOM   4457  N N   . PRO C 1 134 ? 36.418  32.716  -46.135  1.00 18.96 ? 134 PRO C N   1 
ATOM   4458  C CA  . PRO C 1 134 ? 35.132  32.545  -46.815  1.00 18.47 ? 134 PRO C CA  1 
ATOM   4459  C C   . PRO C 1 134 ? 34.230  33.762  -46.664  1.00 17.38 ? 134 PRO C C   1 
ATOM   4460  O O   . PRO C 1 134 ? 34.376  34.516  -45.714  1.00 16.59 ? 134 PRO C O   1 
ATOM   4461  C CB  . PRO C 1 134 ? 34.501  31.342  -46.098  1.00 19.23 ? 134 PRO C CB  1 
ATOM   4462  C CG  . PRO C 1 134 ? 35.260  31.188  -44.795  1.00 19.12 ? 134 PRO C CG  1 
ATOM   4463  C CD  . PRO C 1 134 ? 36.381  32.203  -44.755  1.00 19.21 ? 134 PRO C CD  1 
ATOM   4464  N N   . PRO C 1 135 ? 33.285  33.948  -47.599  1.00 17.30 ? 135 PRO C N   1 
ATOM   4465  C CA  . PRO C 1 135 ? 32.278  34.995  -47.423  1.00 17.54 ? 135 PRO C CA  1 
ATOM   4466  C C   . PRO C 1 135 ? 31.339  34.689  -46.247  1.00 16.78 ? 135 PRO C C   1 
ATOM   4467  O O   . PRO C 1 135 ? 31.349  33.560  -45.733  1.00 16.06 ? 135 PRO C O   1 
ATOM   4468  C CB  . PRO C 1 135 ? 31.516  34.971  -48.749  1.00 17.62 ? 135 PRO C CB  1 
ATOM   4469  C CG  . PRO C 1 135 ? 31.659  33.572  -49.217  1.00 17.43 ? 135 PRO C CG  1 
ATOM   4470  C CD  . PRO C 1 135 ? 33.061  33.192  -48.840  1.00 17.26 ? 135 PRO C CD  1 
ATOM   4471  N N   . VAL C 1 136 ? 30.551  35.683  -45.829  1.00 16.33 ? 136 VAL C N   1 
ATOM   4472  C CA  . VAL C 1 136 ? 29.677  35.527  -44.676  1.00 16.75 ? 136 VAL C CA  1 
ATOM   4473  C C   . VAL C 1 136 ? 28.259  35.954  -45.019  1.00 16.21 ? 136 VAL C C   1 
ATOM   4474  O O   . VAL C 1 136 ? 28.061  36.985  -45.647  1.00 15.99 ? 136 VAL C O   1 
ATOM   4475  C CB  . VAL C 1 136 ? 30.167  36.353  -43.464  1.00 17.38 ? 136 VAL C CB  1 
ATOM   4476  C CG1 . VAL C 1 136 ? 29.179  36.258  -42.295  1.00 17.65 ? 136 VAL C CG1 1 
ATOM   4477  C CG2 . VAL C 1 136 ? 31.539  35.887  -43.016  1.00 17.40 ? 136 VAL C CG2 1 
ATOM   4478  N N   . LEU C 1 137 ? 27.290  35.142  -44.608  1.00 15.97 ? 137 LEU C N   1 
ATOM   4479  C CA  . LEU C 1 137 ? 25.888  35.497  -44.647  1.00 16.30 ? 137 LEU C CA  1 
ATOM   4480  C C   . LEU C 1 137 ? 25.421  35.692  -43.202  1.00 17.50 ? 137 LEU C C   1 
ATOM   4481  O O   . LEU C 1 137 ? 25.277  34.711  -42.432  1.00 17.49 ? 137 LEU C O   1 
ATOM   4482  C CB  . LEU C 1 137 ? 25.068  34.391  -45.323  1.00 16.18 ? 137 LEU C CB  1 
ATOM   4483  C CG  . LEU C 1 137 ? 23.525  34.445  -45.184  1.00 16.21 ? 137 LEU C CG  1 
ATOM   4484  C CD1 . LEU C 1 137 ? 22.949  35.725  -45.811  1.00 16.18 ? 137 LEU C CD1 1 
ATOM   4485  C CD2 . LEU C 1 137 ? 22.875  33.204  -45.744  1.00 15.92 ? 137 LEU C CD2 1 
ATOM   4486  N N   . LEU C 1 138 ? 25.198  36.955  -42.825  1.00 18.55 ? 138 LEU C N   1 
ATOM   4487  C CA  . LEU C 1 138 ? 24.717  37.284  -41.484  1.00 18.77 ? 138 LEU C CA  1 
ATOM   4488  C C   . LEU C 1 138 ? 23.206  37.196  -41.508  1.00 18.97 ? 138 LEU C C   1 
ATOM   4489  O O   . LEU C 1 138 ? 22.561  37.858  -42.330  1.00 18.59 ? 138 LEU C O   1 
ATOM   4490  C CB  . LEU C 1 138 ? 25.137  38.698  -41.079  1.00 18.48 ? 138 LEU C CB  1 
ATOM   4491  C CG  . LEU C 1 138 ? 24.616  39.148  -39.715  1.00 18.62 ? 138 LEU C CG  1 
ATOM   4492  C CD1 . LEU C 1 138 ? 25.115  38.225  -38.605  1.00 18.28 ? 138 LEU C CD1 1 
ATOM   4493  C CD2 . LEU C 1 138 ? 25.029  40.580  -39.437  1.00 18.72 ? 138 LEU C CD2 1 
ATOM   4494  N N   . ILE C 1 139 ? 22.647  36.382  -40.612  1.00 19.43 ? 139 ILE C N   1 
ATOM   4495  C CA  . ILE C 1 139 ? 21.196  36.209  -40.529  1.00 19.37 ? 139 ILE C CA  1 
ATOM   4496  C C   . ILE C 1 139 ? 20.691  36.804  -39.223  1.00 18.70 ? 139 ILE C C   1 
ATOM   4497  O O   . ILE C 1 139 ? 21.106  36.412  -38.140  1.00 19.23 ? 139 ILE C O   1 
ATOM   4498  C CB  . ILE C 1 139 ? 20.759  34.735  -40.637  1.00 19.26 ? 139 ILE C CB  1 
ATOM   4499  C CG1 . ILE C 1 139 ? 21.215  34.150  -41.966  1.00 19.77 ? 139 ILE C CG1 1 
ATOM   4500  C CG2 . ILE C 1 139 ? 19.253  34.618  -40.556  1.00 19.12 ? 139 ILE C CG2 1 
ATOM   4501  C CD1 . ILE C 1 139 ? 20.864  32.679  -42.170  1.00 20.49 ? 139 ILE C CD1 1 
ATOM   4502  N N   . SER C 1 140 ? 19.780  37.754  -39.343  1.00 18.23 ? 140 SER C N   1 
ATOM   4503  C CA  . SER C 1 140 ? 19.119  38.313  -38.193  1.00 17.58 ? 140 SER C CA  1 
ATOM   4504  C C   . SER C 1 140 ? 17.986  37.373  -37.805  1.00 17.28 ? 140 SER C C   1 
ATOM   4505  O O   . SER C 1 140 ? 17.257  36.913  -38.669  1.00 16.58 ? 140 SER C O   1 
ATOM   4506  C CB  . SER C 1 140 ? 18.587  39.687  -38.558  1.00 17.71 ? 140 SER C CB  1 
ATOM   4507  O OG  . SER C 1 140 ? 17.336  39.876  -37.984  1.00 18.25 ? 140 SER C OG  1 
ATOM   4508  N N   . PRO C 1 141 ? 17.828  37.091  -36.500  1.00 17.88 ? 141 PRO C N   1 
ATOM   4509  C CA  . PRO C 1 141 ? 16.729  36.245  -36.064  1.00 17.98 ? 141 PRO C CA  1 
ATOM   4510  C C   . PRO C 1 141 ? 15.410  36.997  -36.075  1.00 17.93 ? 141 PRO C C   1 
ATOM   4511  O O   . PRO C 1 141 ? 15.395  38.224  -36.167  1.00 17.00 ? 141 PRO C O   1 
ATOM   4512  C CB  . PRO C 1 141 ? 17.108  35.889  -34.626  1.00 17.63 ? 141 PRO C CB  1 
ATOM   4513  C CG  . PRO C 1 141 ? 17.852  37.069  -34.153  1.00 17.71 ? 141 PRO C CG  1 
ATOM   4514  C CD  . PRO C 1 141 ? 18.576  37.633  -35.354  1.00 17.91 ? 141 PRO C CD  1 
ATOM   4515  N N   . PRO C 1 142 ? 14.300  36.262  -35.975  1.00 19.10 ? 142 PRO C N   1 
ATOM   4516  C CA  . PRO C 1 142 ? 13.025  36.934  -35.961  1.00 19.82 ? 142 PRO C CA  1 
ATOM   4517  C C   . PRO C 1 142 ? 12.788  37.581  -34.610  1.00 20.54 ? 142 PRO C C   1 
ATOM   4518  O O   . PRO C 1 142 ? 13.541  37.344  -33.666  1.00 19.68 ? 142 PRO C O   1 
ATOM   4519  C CB  . PRO C 1 142 ? 12.031  35.801  -36.192  1.00 19.89 ? 142 PRO C CB  1 
ATOM   4520  C CG  . PRO C 1 142 ? 12.697  34.600  -35.622  1.00 19.40 ? 142 PRO C CG  1 
ATOM   4521  C CD  . PRO C 1 142 ? 14.162  34.796  -35.862  1.00 19.36 ? 142 PRO C CD  1 
ATOM   4522  N N   . PRO C 1 143 ? 11.752  38.426  -34.517  1.00 22.01 ? 143 PRO C N   1 
ATOM   4523  C CA  . PRO C 1 143 ? 11.438  38.983  -33.228  1.00 22.28 ? 143 PRO C CA  1 
ATOM   4524  C C   . PRO C 1 143 ? 11.060  37.891  -32.255  1.00 22.68 ? 143 PRO C C   1 
ATOM   4525  O O   . PRO C 1 143 ? 10.524  36.856  -32.654  1.00 23.06 ? 143 PRO C O   1 
ATOM   4526  C CB  . PRO C 1 143 ? 10.230  39.876  -33.513  1.00 22.47 ? 143 PRO C CB  1 
ATOM   4527  C CG  . PRO C 1 143 ? 10.372  40.243  -34.943  1.00 22.30 ? 143 PRO C CG  1 
ATOM   4528  C CD  . PRO C 1 143 ? 10.973  39.046  -35.600  1.00 22.26 ? 143 PRO C CD  1 
ATOM   4529  N N   . LEU C 1 144 ? 11.338  38.140  -30.985  1.00 23.94 ? 144 LEU C N   1 
ATOM   4530  C CA  . LEU C 1 144 ? 10.900  37.273  -29.921  1.00 24.88 ? 144 LEU C CA  1 
ATOM   4531  C C   . LEU C 1 144 ? 9.383   37.198  -29.907  1.00 26.59 ? 144 LEU C C   1 
ATOM   4532  O O   . LEU C 1 144 ? 8.699   38.057  -30.478  1.00 26.83 ? 144 LEU C O   1 
ATOM   4533  C CB  . LEU C 1 144 ? 11.358  37.823  -28.570  1.00 24.30 ? 144 LEU C CB  1 
ATOM   4534  C CG  . LEU C 1 144 ? 12.843  37.996  -28.307  1.00 24.66 ? 144 LEU C CG  1 
ATOM   4535  C CD1 . LEU C 1 144 ? 13.042  38.848  -27.070  1.00 25.48 ? 144 LEU C CD1 1 
ATOM   4536  C CD2 . LEU C 1 144 ? 13.447  36.608  -28.104  1.00 25.18 ? 144 LEU C CD2 1 
ATOM   4537  N N   . GLY C 1 145 ? 8.866   36.183  -29.225  1.00 29.03 ? 145 GLY C N   1 
ATOM   4538  C CA  . GLY C 1 145 ? 7.438   36.063  -28.978  1.00 31.22 ? 145 GLY C CA  1 
ATOM   4539  C C   . GLY C 1 145 ? 6.932   37.202  -28.117  1.00 33.67 ? 145 GLY C C   1 
ATOM   4540  O O   . GLY C 1 145 ? 7.678   37.740  -27.296  1.00 32.35 ? 145 GLY C O   1 
ATOM   4541  N N   . GLU C 1 146 ? 5.665   37.571  -28.305  1.00 38.49 ? 146 GLU C N   1 
ATOM   4542  C CA  . GLU C 1 146 ? 5.055   38.605  -27.481  1.00 41.73 ? 146 GLU C CA  1 
ATOM   4543  C C   . GLU C 1 146 ? 4.811   38.090  -26.077  1.00 38.43 ? 146 GLU C C   1 
ATOM   4544  O O   . GLU C 1 146 ? 4.738   38.875  -25.152  1.00 37.23 ? 146 GLU C O   1 
ATOM   4545  C CB  . GLU C 1 146 ? 3.745   39.099  -28.100  1.00 47.58 ? 146 GLU C CB  1 
ATOM   4546  C CG  . GLU C 1 146 ? 3.992   39.906  -29.380  1.00 51.94 ? 146 GLU C CG  1 
ATOM   4547  C CD  . GLU C 1 146 ? 3.101   41.143  -29.479  1.00 53.99 ? 146 GLU C CD  1 
ATOM   4548  O OE1 . GLU C 1 146 ? 3.541   42.225  -29.971  1.00 53.38 ? 146 GLU C OE1 1 
ATOM   4549  O OE2 . GLU C 1 146 ? 1.944   41.023  -29.036  1.00 54.40 ? 146 GLU C OE2 1 
ATOM   4550  N N   . THR C 1 147 ? 4.695   36.768  -25.936  1.00 35.77 ? 147 THR C N   1 
ATOM   4551  C CA  . THR C 1 147 ? 4.495   36.130  -24.647  1.00 35.42 ? 147 THR C CA  1 
ATOM   4552  C C   . THR C 1 147 ? 5.564   35.073  -24.352  1.00 34.18 ? 147 THR C C   1 
ATOM   4553  O O   . THR C 1 147 ? 5.617   33.977  -24.964  1.00 38.66 ? 147 THR C O   1 
ATOM   4554  C CB  . THR C 1 147 ? 3.111   35.483  -24.594  1.00 37.16 ? 147 THR C CB  1 
ATOM   4555  O OG1 . THR C 1 147 ? 2.130   36.504  -24.819  1.00 37.57 ? 147 THR C OG1 1 
ATOM   4556  C CG2 . THR C 1 147 ? 2.856   34.822  -23.230  1.00 38.05 ? 147 THR C CG2 1 
ATOM   4557  N N   . ILE C 1 148 ? 6.394   35.373  -23.359  1.00 28.79 ? 148 ILE C N   1 
ATOM   4558  C CA  . ILE C 1 148 ? 7.500   34.508  -22.997  1.00 25.83 ? 148 ILE C CA  1 
ATOM   4559  C C   . ILE C 1 148 ? 7.173   33.739  -21.717  1.00 24.81 ? 148 ILE C C   1 
ATOM   4560  O O   . ILE C 1 148 ? 6.527   34.261  -20.820  1.00 24.71 ? 148 ILE C O   1 
ATOM   4561  C CB  . ILE C 1 148 ? 8.787   35.358  -22.872  1.00 24.40 ? 148 ILE C CB  1 
ATOM   4562  C CG1 . ILE C 1 148 ? 9.145   35.922  -24.247  1.00 24.16 ? 148 ILE C CG1 1 
ATOM   4563  C CG2 . ILE C 1 148 ? 9.944   34.529  -22.339  1.00 24.51 ? 148 ILE C CG2 1 
ATOM   4564  C CD1 . ILE C 1 148 ? 10.062  37.108  -24.236  1.00 24.18 ? 148 ILE C CD1 1 
ATOM   4565  N N   . ASP C 1 149 ? 7.618   32.491  -21.643  1.00 23.02 ? 149 ASP C N   1 
ATOM   4566  C CA  . ASP C 1 149 ? 7.417   31.662  -20.461  1.00 21.77 ? 149 ASP C CA  1 
ATOM   4567  C C   . ASP C 1 149 ? 7.727   32.499  -19.224  1.00 22.43 ? 149 ASP C C   1 
ATOM   4568  O O   . ASP C 1 149 ? 8.798   33.113  -19.153  1.00 21.90 ? 149 ASP C O   1 
ATOM   4569  C CB  . ASP C 1 149 ? 8.322   30.427  -20.521  1.00 20.50 ? 149 ASP C CB  1 
ATOM   4570  C CG  . ASP C 1 149 ? 7.994   29.395  -19.466  1.00 19.07 ? 149 ASP C CG  1 
ATOM   4571  O OD1 . ASP C 1 149 ? 7.945   29.746  -18.268  1.00 17.60 ? 149 ASP C OD1 1 
ATOM   4572  O OD2 . ASP C 1 149 ? 7.811   28.225  -19.860  1.00 18.55 ? 149 ASP C OD2 1 
ATOM   4573  N N   . PRO C 1 150 ? 6.792   32.552  -18.260  1.00 24.03 ? 150 PRO C N   1 
ATOM   4574  C CA  . PRO C 1 150 ? 6.967   33.358  -17.045  1.00 24.84 ? 150 PRO C CA  1 
ATOM   4575  C C   . PRO C 1 150 ? 8.276   33.165  -16.299  1.00 25.14 ? 150 PRO C C   1 
ATOM   4576  O O   . PRO C 1 150 ? 8.770   34.117  -15.679  1.00 26.53 ? 150 PRO C O   1 
ATOM   4577  C CB  . PRO C 1 150 ? 5.776   32.957  -16.186  1.00 25.31 ? 150 PRO C CB  1 
ATOM   4578  C CG  . PRO C 1 150 ? 4.712   32.726  -17.197  1.00 25.26 ? 150 PRO C CG  1 
ATOM   4579  C CD  . PRO C 1 150 ? 5.389   32.119  -18.406  1.00 25.35 ? 150 PRO C CD  1 
ATOM   4580  N N   . LEU C 1 151 ? 8.840   31.965  -16.342  1.00 24.38 ? 151 LEU C N   1 
ATOM   4581  C CA  . LEU C 1 151 ? 10.154  31.721  -15.724  1.00 24.10 ? 151 LEU C CA  1 
ATOM   4582  C C   . LEU C 1 151 ? 11.269  32.489  -16.434  1.00 22.55 ? 151 LEU C C   1 
ATOM   4583  O O   . LEU C 1 151 ? 12.195  32.946  -15.781  1.00 22.39 ? 151 LEU C O   1 
ATOM   4584  C CB  . LEU C 1 151 ? 10.464  30.229  -15.689  1.00 24.68 ? 151 LEU C CB  1 
ATOM   4585  C CG  . LEU C 1 151 ? 9.610   29.424  -14.669  1.00 24.93 ? 151 LEU C CG  1 
ATOM   4586  C CD1 . LEU C 1 151 ? 9.029   28.212  -15.405  1.00 25.29 ? 151 LEU C CD1 1 
ATOM   4587  C CD2 . LEU C 1 151 ? 10.282  29.008  -13.375  1.00 26.28 ? 151 LEU C CD2 1 
ATOM   4588  N N   . ALA C 1 152 ? 11.175  32.659  -17.750  1.00 20.36 ? 152 ALA C N   1 
ATOM   4589  C CA  . ALA C 1 152 ? 12.206  33.331  -18.544  1.00 19.68 ? 152 ALA C CA  1 
ATOM   4590  C C   . ALA C 1 152 ? 11.938  34.816  -18.820  1.00 19.51 ? 152 ALA C C   1 
ATOM   4591  O O   . ALA C 1 152 ? 12.863  35.582  -19.147  1.00 19.89 ? 152 ALA C O   1 
ATOM   4592  C CB  . ALA C 1 152 ? 12.383  32.615  -19.865  1.00 19.70 ? 152 ALA C CB  1 
ATOM   4593  N N   . ALA C 1 153 ? 10.685  35.247  -18.698  1.00 19.21 ? 153 ALA C N   1 
ATOM   4594  C CA  . ALA C 1 153 ? 10.324  36.634  -19.025  1.00 18.75 ? 153 ALA C CA  1 
ATOM   4595  C C   . ALA C 1 153 ? 11.159  37.723  -18.341  1.00 18.63 ? 153 ALA C C   1 
ATOM   4596  O O   . ALA C 1 153 ? 11.526  38.687  -18.994  1.00 18.54 ? 153 ALA C O   1 
ATOM   4597  C CB  . ALA C 1 153 ? 8.844   36.858  -18.769  1.00 18.78 ? 153 ALA C CB  1 
ATOM   4598  N N   . PRO C 1 154 ? 11.471  37.587  -17.037  1.00 18.96 ? 154 PRO C N   1 
ATOM   4599  C CA  . PRO C 1 154 ? 12.287  38.599  -16.345  1.00 19.54 ? 154 PRO C CA  1 
ATOM   4600  C C   . PRO C 1 154 ? 13.613  38.894  -17.022  1.00 20.03 ? 154 PRO C C   1 
ATOM   4601  O O   . PRO C 1 154 ? 14.095  40.026  -16.974  1.00 20.67 ? 154 PRO C O   1 
ATOM   4602  C CB  . PRO C 1 154 ? 12.544  37.974  -14.970  1.00 19.46 ? 154 PRO C CB  1 
ATOM   4603  C CG  . PRO C 1 154 ? 11.382  37.087  -14.758  1.00 19.63 ? 154 PRO C CG  1 
ATOM   4604  C CD  . PRO C 1 154 ? 11.094  36.508  -16.115  1.00 19.40 ? 154 PRO C CD  1 
ATOM   4605  N N   . ILE C 1 155 ? 14.179  37.862  -17.636  1.00 20.49 ? 155 ILE C N   1 
ATOM   4606  C CA  . ILE C 1 155 ? 15.466  37.915  -18.328  1.00 20.56 ? 155 ILE C CA  1 
ATOM   4607  C C   . ILE C 1 155 ? 15.348  38.489  -19.768  1.00 19.23 ? 155 ILE C C   1 
ATOM   4608  O O   . ILE C 1 155 ? 16.366  38.802  -20.380  1.00 19.14 ? 155 ILE C O   1 
ATOM   4609  C CB  . ILE C 1 155 ? 16.100  36.479  -18.242  1.00 21.55 ? 155 ILE C CB  1 
ATOM   4610  C CG1 . ILE C 1 155 ? 17.024  36.421  -17.046  1.00 23.95 ? 155 ILE C CG1 1 
ATOM   4611  C CG2 . ILE C 1 155 ? 16.828  36.026  -19.477  1.00 20.89 ? 155 ILE C CG2 1 
ATOM   4612  C CD1 . ILE C 1 155 ? 17.476  35.003  -16.652  1.00 26.19 ? 155 ILE C CD1 1 
ATOM   4613  N N   . PHE C 1 156 ? 14.127  38.643  -20.292  1.00 17.62 ? 156 PHE C N   1 
ATOM   4614  C CA  . PHE C 1 156 ? 13.910  39.213  -21.648  1.00 16.73 ? 156 PHE C CA  1 
ATOM   4615  C C   . PHE C 1 156 ? 13.090  40.510  -21.661  1.00 16.19 ? 156 PHE C C   1 
ATOM   4616  O O   . PHE C 1 156 ? 12.426  40.820  -22.639  1.00 15.56 ? 156 PHE C O   1 
ATOM   4617  C CB  . PHE C 1 156 ? 13.254  38.182  -22.580  1.00 16.05 ? 156 PHE C CB  1 
ATOM   4618  C CG  . PHE C 1 156 ? 14.184  37.095  -23.021  1.00 15.84 ? 156 PHE C CG  1 
ATOM   4619  C CD1 . PHE C 1 156 ? 15.120  37.336  -24.013  1.00 16.23 ? 156 PHE C CD1 1 
ATOM   4620  C CD2 . PHE C 1 156 ? 14.158  35.850  -22.429  1.00 15.45 ? 156 PHE C CD2 1 
ATOM   4621  C CE1 . PHE C 1 156 ? 16.023  36.360  -24.400  1.00 16.08 ? 156 PHE C CE1 1 
ATOM   4622  C CE2 . PHE C 1 156 ? 15.044  34.865  -22.811  1.00 15.64 ? 156 PHE C CE2 1 
ATOM   4623  C CZ  . PHE C 1 156 ? 15.978  35.118  -23.796  1.00 15.94 ? 156 PHE C CZ  1 
ATOM   4624  N N   . VAL C 1 157 ? 13.164  41.282  -20.581  1.00 15.87 ? 157 VAL C N   1 
ATOM   4625  C CA  . VAL C 1 157 ? 12.481  42.569  -20.511  1.00 15.31 ? 157 VAL C CA  1 
ATOM   4626  C C   . VAL C 1 157 ? 13.174  43.508  -21.508  1.00 15.40 ? 157 VAL C C   1 
ATOM   4627  O O   . VAL C 1 157 ? 14.392  43.480  -21.661  1.00 15.89 ? 157 VAL C O   1 
ATOM   4628  C CB  . VAL C 1 157 ? 12.485  43.145  -19.070  1.00 15.07 ? 157 VAL C CB  1 
ATOM   4629  C CG1 . VAL C 1 157 ? 12.038  44.607  -19.023  1.00 14.84 ? 157 VAL C CG1 1 
ATOM   4630  C CG2 . VAL C 1 157 ? 11.640  42.276  -18.146  1.00 14.59 ? 157 VAL C CG2 1 
ATOM   4631  N N   . ASP C 1 158 ? 12.376  44.296  -22.221  1.00 15.67 ? 158 ASP C N   1 
ATOM   4632  C CA  . ASP C 1 158 ? 12.829  45.125  -23.342  1.00 16.02 ? 158 ASP C CA  1 
ATOM   4633  C C   . ASP C 1 158 ? 13.497  44.354  -24.479  1.00 16.42 ? 158 ASP C C   1 
ATOM   4634  O O   . ASP C 1 158 ? 14.060  44.961  -25.378  1.00 16.45 ? 158 ASP C O   1 
ATOM   4635  C CB  . ASP C 1 158 ? 13.775  46.217  -22.860  1.00 16.52 ? 158 ASP C CB  1 
ATOM   4636  C CG  . ASP C 1 158 ? 13.218  46.994  -21.704  1.00 17.47 ? 158 ASP C CG  1 
ATOM   4637  O OD1 . ASP C 1 158 ? 12.039  47.399  -21.779  1.00 18.19 ? 158 ASP C OD1 1 
ATOM   4638  O OD2 . ASP C 1 158 ? 13.963  47.198  -20.716  1.00 18.15 ? 158 ASP C OD2 1 
ATOM   4639  N N   . GLY C 1 159 ? 13.432  43.024  -24.464  1.00 16.98 ? 159 GLY C N   1 
ATOM   4640  C CA  . GLY C 1 159 ? 14.133  42.213  -25.460  1.00 16.46 ? 159 GLY C CA  1 
ATOM   4641  C C   . GLY C 1 159 ? 13.435  42.209  -26.800  1.00 16.45 ? 159 GLY C C   1 
ATOM   4642  O O   . GLY C 1 159 ? 14.088  42.173  -27.839  1.00 15.62 ? 159 GLY C O   1 
ATOM   4643  N N   . LEU C 1 160 ? 12.102  42.238  -26.779  1.00 17.02 ? 160 LEU C N   1 
ATOM   4644  C CA  . LEU C 1 160 ? 11.307  42.207  -27.988  1.00 17.00 ? 160 LEU C CA  1 
ATOM   4645  C C   . LEU C 1 160 ? 11.676  43.367  -28.905  1.00 16.68 ? 160 LEU C C   1 
ATOM   4646  O O   . LEU C 1 160 ? 11.940  43.176  -30.091  1.00 16.40 ? 160 LEU C O   1 
ATOM   4647  C CB  . LEU C 1 160 ? 9.822   42.285  -27.632  1.00 17.57 ? 160 LEU C CB  1 
ATOM   4648  C CG  . LEU C 1 160 ? 8.844   42.426  -28.804  1.00 18.22 ? 160 LEU C CG  1 
ATOM   4649  C CD1 . LEU C 1 160 ? 9.016   41.254  -29.760  1.00 18.59 ? 160 LEU C CD1 1 
ATOM   4650  C CD2 . LEU C 1 160 ? 7.412   42.589  -28.349  1.00 18.80 ? 160 LEU C CD2 1 
ATOM   4651  N N   . ALA C 1 161 ? 11.692  44.570  -28.349  1.00 16.27 ? 161 ALA C N   1 
ATOM   4652  C CA  . ALA C 1 161 ? 11.961  45.771  -29.127  1.00 15.72 ? 161 ALA C CA  1 
ATOM   4653  C C   . ALA C 1 161 ? 13.359  45.709  -29.731  1.00 15.40 ? 161 ALA C C   1 
ATOM   4654  O O   . ALA C 1 161 ? 13.567  46.074  -30.873  1.00 14.55 ? 161 ALA C O   1 
ATOM   4655  C CB  . ALA C 1 161 ? 11.808  46.999  -28.231  1.00 15.94 ? 161 ALA C CB  1 
ATOM   4656  N N   . LYS C 1 162 ? 14.313  45.226  -28.947  1.00 15.95 ? 162 LYS C N   1 
ATOM   4657  C CA  . LYS C 1 162 ? 15.678  45.036  -29.420  1.00 16.17 ? 162 LYS C CA  1 
ATOM   4658  C C   . LYS C 1 162 ? 15.732  44.056  -30.569  1.00 16.36 ? 162 LYS C C   1 
ATOM   4659  O O   . LYS C 1 162 ? 16.398  44.306  -31.547  1.00 16.08 ? 162 LYS C O   1 
ATOM   4660  C CB  . LYS C 1 162 ? 16.576  44.551  -28.284  1.00 15.85 ? 162 LYS C CB  1 
ATOM   4661  C CG  . LYS C 1 162 ? 16.834  45.608  -27.230  1.00 15.50 ? 162 LYS C CG  1 
ATOM   4662  C CD  . LYS C 1 162 ? 17.605  45.037  -26.055  1.00 15.14 ? 162 LYS C CD  1 
ATOM   4663  C CE  . LYS C 1 162 ? 17.526  45.956  -24.860  1.00 14.76 ? 162 LYS C CE  1 
ATOM   4664  N NZ  . LYS C 1 162 ? 18.574  45.623  -23.882  1.00 14.93 ? 162 LYS C NZ  1 
ATOM   4665  N N   . SER C 1 163 ? 15.027  42.939  -30.450  1.00 17.08 ? 163 SER C N   1 
ATOM   4666  C CA  . SER C 1 163 ? 15.019  41.919  -31.504  1.00 17.97 ? 163 SER C CA  1 
ATOM   4667  C C   . SER C 1 163 ? 14.372  42.449  -32.788  1.00 19.24 ? 163 SER C C   1 
ATOM   4668  O O   . SER C 1 163 ? 14.759  42.064  -33.883  1.00 20.62 ? 163 SER C O   1 
ATOM   4669  C CB  . SER C 1 163 ? 14.334  40.639  -31.025  1.00 17.91 ? 163 SER C CB  1 
ATOM   4670  O OG  . SER C 1 163 ? 12.948  40.813  -30.836  1.00 18.74 ? 163 SER C OG  1 
ATOM   4671  N N   . GLU C 1 164 ? 13.398  43.340  -32.655  1.00 20.17 ? 164 GLU C N   1 
ATOM   4672  C CA  . GLU C 1 164 ? 12.757  43.951  -33.828  1.00 20.23 ? 164 GLU C CA  1 
ATOM   4673  C C   . GLU C 1 164 ? 13.716  44.871  -34.557  1.00 21.16 ? 164 GLU C C   1 
ATOM   4674  O O   . GLU C 1 164 ? 13.658  44.992  -35.769  1.00 22.12 ? 164 GLU C O   1 
ATOM   4675  C CB  . GLU C 1 164 ? 11.487  44.706  -33.437  1.00 19.86 ? 164 GLU C CB  1 
ATOM   4676  C CG  . GLU C 1 164 ? 10.259  43.814  -33.294  1.00 19.53 ? 164 GLU C CG  1 
ATOM   4677  C CD  . GLU C 1 164 ? 9.144   44.441  -32.471  1.00 19.60 ? 164 GLU C CD  1 
ATOM   4678  O OE1 . GLU C 1 164 ? 8.073   43.803  -32.352  1.00 20.44 ? 164 GLU C OE1 1 
ATOM   4679  O OE2 . GLU C 1 164 ? 9.328   45.561  -31.950  1.00 18.68 ? 164 GLU C OE2 1 
ATOM   4680  N N   . ALA C 1 165 ? 14.615  45.500  -33.820  1.00 22.15 ? 165 ALA C N   1 
ATOM   4681  C CA  . ALA C 1 165 ? 15.606  46.430  -34.397  1.00 22.22 ? 165 ALA C CA  1 
ATOM   4682  C C   . ALA C 1 165 ? 16.835  45.773  -35.033  1.00 22.12 ? 165 ALA C C   1 
ATOM   4683  O O   . ALA C 1 165 ? 17.622  46.468  -35.656  1.00 20.87 ? 165 ALA C O   1 
ATOM   4684  C CB  . ALA C 1 165 ? 16.067  47.413  -33.326  1.00 22.12 ? 165 ALA C CB  1 
ATOM   4685  N N   . LEU C 1 166 ? 17.002  44.454  -34.881  1.00 22.37 ? 166 LEU C N   1 
ATOM   4686  C CA  . LEU C 1 166 ? 18.224  43.785  -35.342  1.00 22.84 ? 166 LEU C CA  1 
ATOM   4687  C C   . LEU C 1 166 ? 18.354  43.719  -36.870  1.00 23.47 ? 166 LEU C C   1 
ATOM   4688  O O   . LEU C 1 166 ? 19.421  44.009  -37.391  1.00 24.37 ? 166 LEU C O   1 
ATOM   4689  C CB  . LEU C 1 166 ? 18.372  42.389  -34.732  1.00 22.73 ? 166 LEU C CB  1 
ATOM   4690  C CG  . LEU C 1 166 ? 18.628  42.326  -33.215  1.00 22.73 ? 166 LEU C CG  1 
ATOM   4691  C CD1 . LEU C 1 166 ? 18.790  40.875  -32.744  1.00 21.76 ? 166 LEU C CD1 1 
ATOM   4692  C CD2 . LEU C 1 166 ? 19.818  43.218  -32.781  1.00 22.46 ? 166 LEU C CD2 1 
ATOM   4693  N N   . PRO C 1 167 ? 17.280  43.361  -37.600  1.00 22.56 ? 167 PRO C N   1 
ATOM   4694  C CA  . PRO C 1 167 ? 17.435  43.305  -39.055  1.00 21.52 ? 167 PRO C CA  1 
ATOM   4695  C C   . PRO C 1 167 ? 18.058  44.574  -39.684  1.00 20.99 ? 167 PRO C C   1 
ATOM   4696  O O   . PRO C 1 167 ? 18.979  44.471  -40.501  1.00 21.00 ? 167 PRO C O   1 
ATOM   4697  C CB  . PRO C 1 167 ? 16.007  43.075  -39.548  1.00 21.32 ? 167 PRO C CB  1 
ATOM   4698  C CG  . PRO C 1 167 ? 15.310  42.413  -38.430  1.00 21.45 ? 167 PRO C CG  1 
ATOM   4699  C CD  . PRO C 1 167 ? 15.935  42.947  -37.175  1.00 21.89 ? 167 PRO C CD  1 
ATOM   4700  N N   . GLY C 1 168 ? 17.577  45.751  -39.298  1.00 20.11 ? 168 GLY C N   1 
ATOM   4701  C CA  . GLY C 1 168 ? 18.106  47.003  -39.840  1.00 19.31 ? 168 GLY C CA  1 
ATOM   4702  C C   . GLY C 1 168 ? 19.581  47.180  -39.556  1.00 19.54 ? 168 GLY C C   1 
ATOM   4703  O O   . GLY C 1 168 ? 20.360  47.490  -40.461  1.00 20.20 ? 168 GLY C O   1 
ATOM   4704  N N   . VAL C 1 169 ? 19.968  46.955  -38.298  1.00 19.66 ? 169 VAL C N   1 
ATOM   4705  C CA  . VAL C 1 169 ? 21.351  47.104  -37.854  1.00 19.86 ? 169 VAL C CA  1 
ATOM   4706  C C   . VAL C 1 169 ? 22.239  46.062  -38.515  1.00 19.96 ? 169 VAL C C   1 
ATOM   4707  O O   . VAL C 1 169 ? 23.282  46.393  -39.057  1.00 20.07 ? 169 VAL C O   1 
ATOM   4708  C CB  . VAL C 1 169 ? 21.490  46.972  -36.325  1.00 20.51 ? 169 VAL C CB  1 
ATOM   4709  C CG1 . VAL C 1 169 ? 22.949  47.051  -35.903  1.00 21.05 ? 169 VAL C CG1 1 
ATOM   4710  C CG2 . VAL C 1 169 ? 20.723  48.075  -35.609  1.00 20.84 ? 169 VAL C CG2 1 
ATOM   4711  N N   . TYR C 1 170 ? 21.822  44.801  -38.456  1.00 20.56 ? 170 TYR C N   1 
ATOM   4712  C CA  . TYR C 1 170 ? 22.568  43.685  -39.072  1.00 21.32 ? 170 TYR C CA  1 
ATOM   4713  C C   . TYR C 1 170 ? 22.817  43.925  -40.552  1.00 21.94 ? 170 TYR C C   1 
ATOM   4714  O O   . TYR C 1 170 ? 23.908  43.635  -41.047  1.00 23.04 ? 170 TYR C O   1 
ATOM   4715  C CB  . TYR C 1 170 ? 21.839  42.341  -38.882  1.00 21.65 ? 170 TYR C CB  1 
ATOM   4716  C CG  . TYR C 1 170 ? 22.115  41.632  -37.564  1.00 22.26 ? 170 TYR C CG  1 
ATOM   4717  C CD1 . TYR C 1 170 ? 22.451  42.356  -36.402  1.00 23.04 ? 170 TYR C CD1 1 
ATOM   4718  C CD2 . TYR C 1 170 ? 22.012  40.251  -37.461  1.00 21.99 ? 170 TYR C CD2 1 
ATOM   4719  C CE1 . TYR C 1 170 ? 22.699  41.712  -35.204  1.00 22.38 ? 170 TYR C CE1 1 
ATOM   4720  C CE2 . TYR C 1 170 ? 22.244  39.598  -36.263  1.00 22.16 ? 170 TYR C CE2 1 
ATOM   4721  C CZ  . TYR C 1 170 ? 22.591  40.337  -35.138  1.00 22.58 ? 170 TYR C CZ  1 
ATOM   4722  O OH  . TYR C 1 170 ? 22.830  39.709  -33.932  1.00 23.38 ? 170 TYR C OH  1 
ATOM   4723  N N   . LYS C 1 171 ? 21.821  44.452  -41.257  1.00 22.46 ? 171 LYS C N   1 
ATOM   4724  C CA  . LYS C 1 171 ? 21.988  44.736  -42.675  1.00 23.29 ? 171 LYS C CA  1 
ATOM   4725  C C   . LYS C 1 171 ? 23.087  45.777  -42.916  1.00 23.77 ? 171 LYS C C   1 
ATOM   4726  O O   . LYS C 1 171 ? 23.924  45.595  -43.808  1.00 25.51 ? 171 LYS C O   1 
ATOM   4727  C CB  . LYS C 1 171 ? 20.689  45.196  -43.346  1.00 23.47 ? 171 LYS C CB  1 
ATOM   4728  C CG  . LYS C 1 171 ? 20.848  45.179  -44.863  1.00 24.80 ? 171 LYS C CG  1 
ATOM   4729  C CD  . LYS C 1 171 ? 19.594  45.349  -45.643  1.00 25.94 ? 171 LYS C CD  1 
ATOM   4730  C CE  . LYS C 1 171 ? 19.772  46.700  -46.225  1.00 26.59 ? 171 LYS C CE  1 
ATOM   4731  N NZ  . LYS C 1 171 ? 18.509  46.979  -46.910  1.00 28.45 ? 171 LYS C NZ  1 
ATOM   4732  N N   . ALA C 1 172 ? 23.082  46.858  -42.135  1.00 22.42 ? 172 ALA C N   1 
ATOM   4733  C CA  . ALA C 1 172 ? 24.093  47.915  -42.289  1.00 20.91 ? 172 ALA C CA  1 
ATOM   4734  C C   . ALA C 1 172 ? 25.491  47.370  -42.022  1.00 19.77 ? 172 ALA C C   1 
ATOM   4735  O O   . ALA C 1 172 ? 26.413  47.596  -42.794  1.00 19.23 ? 172 ALA C O   1 
ATOM   4736  C CB  . ALA C 1 172 ? 23.796  49.085  -41.366  1.00 20.41 ? 172 ALA C CB  1 
ATOM   4737  N N   . ILE C 1 173 ? 25.620  46.637  -40.929  1.00 19.36 ? 173 ILE C N   1 
ATOM   4738  C CA  . ILE C 1 173 ? 26.889  46.060  -40.519  1.00 19.86 ? 173 ILE C CA  1 
ATOM   4739  C C   . ILE C 1 173 ? 27.427  45.083  -41.571  1.00 19.90 ? 173 ILE C C   1 
ATOM   4740  O O   . ILE C 1 173 ? 28.613  45.105  -41.886  1.00 19.24 ? 173 ILE C O   1 
ATOM   4741  C CB  . ILE C 1 173 ? 26.749  45.345  -39.150  1.00 19.81 ? 173 ILE C CB  1 
ATOM   4742  C CG1 . ILE C 1 173 ? 26.466  46.367  -38.041  1.00 19.11 ? 173 ILE C CG1 1 
ATOM   4743  C CG2 . ILE C 1 173 ? 27.984  44.498  -38.827  1.00 20.19 ? 173 ILE C CG2 1 
ATOM   4744  C CD1 . ILE C 1 173 ? 27.598  47.311  -37.753  1.00 19.18 ? 173 ILE C CD1 1 
ATOM   4745  N N   . ALA C 1 174 ? 26.550  44.228  -42.093  1.00 20.10 ? 174 ALA C N   1 
ATOM   4746  C CA  . ALA C 1 174 ? 26.931  43.244  -43.109  1.00 20.15 ? 174 ALA C CA  1 
ATOM   4747  C C   . ALA C 1 174 ? 27.406  43.953  -44.373  1.00 21.52 ? 174 ALA C C   1 
ATOM   4748  O O   . ALA C 1 174 ? 28.453  43.615  -44.933  1.00 20.45 ? 174 ALA C O   1 
ATOM   4749  C CB  . ALA C 1 174 ? 25.754  42.341  -43.442  1.00 19.13 ? 174 ALA C CB  1 
ATOM   4750  N N   . GLU C 1 175 ? 26.609  44.937  -44.797  1.00 22.61 ? 175 GLU C N   1 
ATOM   4751  C CA  . GLU C 1 175 ? 26.924  45.775  -45.942  1.00 23.28 ? 175 GLU C CA  1 
ATOM   4752  C C   . GLU C 1 175 ? 28.266  46.487  -45.735  1.00 22.03 ? 175 GLU C C   1 
ATOM   4753  O O   . GLU C 1 175 ? 29.088  46.515  -46.642  1.00 23.01 ? 175 GLU C O   1 
ATOM   4754  C CB  . GLU C 1 175 ? 25.821  46.802  -46.161  1.00 25.77 ? 175 GLU C CB  1 
ATOM   4755  C CG  . GLU C 1 175 ? 25.312  46.963  -47.585  1.00 28.56 ? 175 GLU C CG  1 
ATOM   4756  C CD  . GLU C 1 175 ? 23.817  47.297  -47.586  1.00 31.55 ? 175 GLU C CD  1 
ATOM   4757  O OE1 . GLU C 1 175 ? 23.460  48.504  -47.440  1.00 32.70 ? 175 GLU C OE1 1 
ATOM   4758  O OE2 . GLU C 1 175 ? 22.976  46.349  -47.702  1.00 33.46 ? 175 GLU C OE2 1 
ATOM   4759  N N   . ALA C 1 176 ? 28.497  47.037  -44.548  1.00 20.82 ? 176 ALA C N   1 
ATOM   4760  C CA  . ALA C 1 176 ? 29.749  47.755  -44.256  1.00 20.54 ? 176 ALA C CA  1 
ATOM   4761  C C   . ALA C 1 176 ? 30.955  46.853  -44.370  1.00 20.56 ? 176 ALA C C   1 
ATOM   4762  O O   . ALA C 1 176 ? 32.033  47.296  -44.706  1.00 19.91 ? 176 ALA C O   1 
ATOM   4763  C CB  . ALA C 1 176 ? 29.705  48.373  -42.859  1.00 20.84 ? 176 ALA C CB  1 
ATOM   4764  N N   . ALA C 1 177 ? 30.761  45.575  -44.067  1.00 22.18 ? 177 ALA C N   1 
ATOM   4765  C CA  . ALA C 1 177 ? 31.815  44.568  -44.157  1.00 21.63 ? 177 ALA C CA  1 
ATOM   4766  C C   . ALA C 1 177 ? 31.971  43.987  -45.560  1.00 21.29 ? 177 ALA C C   1 
ATOM   4767  O O   . ALA C 1 177 ? 32.804  43.124  -45.755  1.00 22.31 ? 177 ALA C O   1 
ATOM   4768  C CB  . ALA C 1 177 ? 31.507  43.450  -43.177  1.00 21.40 ? 177 ALA C CB  1 
ATOM   4769  N N   . GLY C 1 178 ? 31.159  44.431  -46.517  1.00 21.16 ? 178 GLY C N   1 
ATOM   4770  C CA  . GLY C 1 178 ? 31.110  43.821  -47.842  1.00 21.77 ? 178 GLY C CA  1 
ATOM   4771  C C   . GLY C 1 178 ? 30.674  42.354  -47.860  1.00 21.49 ? 178 GLY C C   1 
ATOM   4772  O O   . GLY C 1 178 ? 31.227  41.545  -48.601  1.00 22.80 ? 178 GLY C O   1 
ATOM   4773  N N   . GLU C 1 179 ? 29.679  42.026  -47.043  1.00 20.64 ? 179 GLU C N   1 
ATOM   4774  C CA  . GLU C 1 179 ? 29.190  40.650  -46.890  1.00 20.09 ? 179 GLU C CA  1 
ATOM   4775  C C   . GLU C 1 179 ? 27.670  40.622  -47.067  1.00 19.17 ? 179 GLU C C   1 
ATOM   4776  O O   . GLU C 1 179 ? 27.080  41.640  -47.371  1.00 19.12 ? 179 GLU C O   1 
ATOM   4777  C CB  . GLU C 1 179 ? 29.596  40.097  -45.519  1.00 20.98 ? 179 GLU C CB  1 
ATOM   4778  C CG  . GLU C 1 179 ? 31.112  40.087  -45.281  1.00 22.18 ? 179 GLU C CG  1 
ATOM   4779  C CD  . GLU C 1 179 ? 31.846  38.981  -46.041  1.00 22.77 ? 179 GLU C CD  1 
ATOM   4780  O OE1 . GLU C 1 179 ? 33.083  38.867  -45.862  1.00 22.68 ? 179 GLU C OE1 1 
ATOM   4781  O OE2 . GLU C 1 179 ? 31.197  38.205  -46.789  1.00 23.70 ? 179 GLU C OE2 1 
ATOM   4782  N N   . SER C 1 180 ? 27.033  39.472  -46.890  1.00 18.40 ? 180 SER C N   1 
ATOM   4783  C CA  . SER C 1 180 ? 25.619  39.338  -47.198  1.00 18.32 ? 180 SER C CA  1 
ATOM   4784  C C   . SER C 1 180 ? 24.730  39.305  -45.960  1.00 19.74 ? 180 SER C C   1 
ATOM   4785  O O   . SER C 1 180 ? 25.195  39.031  -44.851  1.00 21.13 ? 180 SER C O   1 
ATOM   4786  C CB  . SER C 1 180 ? 25.394  38.072  -48.006  1.00 17.60 ? 180 SER C CB  1 
ATOM   4787  O OG  . SER C 1 180 ? 26.342  37.978  -49.038  1.00 16.55 ? 180 SER C OG  1 
ATOM   4788  N N   . PHE C 1 181 ? 23.442  39.565  -46.175  1.00 20.63 ? 181 PHE C N   1 
ATOM   4789  C CA  . PHE C 1 181 ? 22.455  39.655  -45.109  1.00 21.41 ? 181 PHE C CA  1 
ATOM   4790  C C   . PHE C 1 181 ? 21.153  38.941  -45.453  1.00 22.34 ? 181 PHE C C   1 
ATOM   4791  O O   . PHE C 1 181 ? 20.760  38.878  -46.608  1.00 21.93 ? 181 PHE C O   1 
ATOM   4792  C CB  . PHE C 1 181 ? 22.117  41.115  -44.823  1.00 22.28 ? 181 PHE C CB  1 
ATOM   4793  C CG  . PHE C 1 181 ? 20.936  41.280  -43.919  1.00 23.08 ? 181 PHE C CG  1 
ATOM   4794  C CD1 . PHE C 1 181 ? 21.026  40.929  -42.580  1.00 23.53 ? 181 PHE C CD1 1 
ATOM   4795  C CD2 . PHE C 1 181 ? 19.734  41.744  -44.411  1.00 22.85 ? 181 PHE C CD2 1 
ATOM   4796  C CE1 . PHE C 1 181 ? 19.934  41.045  -41.745  1.00 23.71 ? 181 PHE C CE1 1 
ATOM   4797  C CE2 . PHE C 1 181 ? 18.637  41.877  -43.582  1.00 23.50 ? 181 PHE C CE2 1 
ATOM   4798  C CZ  . PHE C 1 181 ? 18.734  41.518  -42.249  1.00 23.73 ? 181 PHE C CZ  1 
ATOM   4799  N N   . PHE C 1 182 ? 20.483  38.410  -44.433  1.00 23.39 ? 182 PHE C N   1 
ATOM   4800  C CA  . PHE C 1 182 ? 19.137  37.855  -44.590  1.00 23.32 ? 182 PHE C CA  1 
ATOM   4801  C C   . PHE C 1 182 ? 18.379  37.950  -43.282  1.00 23.01 ? 182 PHE C C   1 
ATOM   4802  O O   . PHE C 1 182 ? 18.907  37.618  -42.220  1.00 22.41 ? 182 PHE C O   1 
ATOM   4803  C CB  . PHE C 1 182 ? 19.215  36.394  -45.042  1.00 23.28 ? 182 PHE C CB  1 
ATOM   4804  C CG  . PHE C 1 182 ? 17.879  35.738  -45.242  1.00 23.83 ? 182 PHE C CG  1 
ATOM   4805  C CD1 . PHE C 1 182 ? 17.208  35.190  -44.174  1.00 24.95 ? 182 PHE C CD1 1 
ATOM   4806  C CD2 . PHE C 1 182 ? 17.318  35.620  -46.511  1.00 23.78 ? 182 PHE C CD2 1 
ATOM   4807  C CE1 . PHE C 1 182 ? 15.974  34.549  -44.353  1.00 25.37 ? 182 PHE C CE1 1 
ATOM   4808  C CE2 . PHE C 1 182 ? 16.098  34.993  -46.702  1.00 23.88 ? 182 PHE C CE2 1 
ATOM   4809  C CZ  . PHE C 1 182 ? 15.407  34.474  -45.613  1.00 24.96 ? 182 PHE C CZ  1 
ATOM   4810  N N   . ASP C 1 183 ? 17.132  38.386  -43.366  1.00 23.47 ? 183 ASP C N   1 
ATOM   4811  C CA  . ASP C 1 183 ? 16.291  38.555  -42.179  1.00 24.32 ? 183 ASP C CA  1 
ATOM   4812  C C   . ASP C 1 183 ? 15.382  37.337  -42.008  1.00 23.53 ? 183 ASP C C   1 
ATOM   4813  O O   . ASP C 1 183 ? 14.422  37.157  -42.739  1.00 21.40 ? 183 ASP C O   1 
ATOM   4814  C CB  . ASP C 1 183 ? 15.462  39.829  -42.318  1.00 24.71 ? 183 ASP C CB  1 
ATOM   4815  C CG  . ASP C 1 183 ? 14.548  40.074  -41.144  1.00 23.74 ? 183 ASP C CG  1 
ATOM   4816  O OD1 . ASP C 1 183 ? 14.631  39.386  -40.119  1.00 21.91 ? 183 ASP C OD1 1 
ATOM   4817  O OD2 . ASP C 1 183 ? 13.724  40.991  -41.245  1.00 24.61 ? 183 ASP C OD2 1 
ATOM   4818  N N   . ALA C 1 184 ? 15.679  36.509  -41.025  1.00 25.01 ? 184 ALA C N   1 
ATOM   4819  C CA  . ALA C 1 184 ? 14.849  35.342  -40.761  1.00 25.63 ? 184 ALA C CA  1 
ATOM   4820  C C   . ALA C 1 184 ? 13.393  35.750  -40.493  1.00 26.12 ? 184 ALA C C   1 
ATOM   4821  O O   . ALA C 1 184 ? 12.468  34.991  -40.800  1.00 27.89 ? 184 ALA C O   1 
ATOM   4822  C CB  . ALA C 1 184 ? 15.406  34.546  -39.593  1.00 25.61 ? 184 ALA C CB  1 
ATOM   4823  N N   . GLY C 1 185 ? 13.189  36.945  -39.937  1.00 24.01 ? 185 GLY C N   1 
ATOM   4824  C CA  . GLY C 1 185 ? 11.852  37.474  -39.710  1.00 23.45 ? 185 GLY C CA  1 
ATOM   4825  C C   . GLY C 1 185 ? 11.022  37.717  -40.964  1.00 22.90 ? 185 GLY C C   1 
ATOM   4826  O O   . GLY C 1 185 ? 9.806   37.893  -40.870  1.00 21.49 ? 185 GLY C O   1 
ATOM   4827  N N   . SER C 1 186 ? 11.665  37.737  -42.131  1.00 23.39 ? 186 SER C N   1 
ATOM   4828  C CA  . SER C 1 186 ? 10.950  37.893  -43.402  1.00 23.46 ? 186 SER C CA  1 
ATOM   4829  C C   . SER C 1 186 ? 10.198  36.625  -43.830  1.00 23.82 ? 186 SER C C   1 
ATOM   4830  O O   . SER C 1 186 ? 9.299   36.708  -44.654  1.00 23.16 ? 186 SER C O   1 
ATOM   4831  C CB  . SER C 1 186 ? 11.917  38.313  -44.520  1.00 23.12 ? 186 SER C CB  1 
ATOM   4832  O OG  . SER C 1 186 ? 12.629  37.191  -45.043  1.00 24.02 ? 186 SER C OG  1 
ATOM   4833  N N   . VAL C 1 187 ? 10.566  35.467  -43.279  1.00 25.05 ? 187 VAL C N   1 
ATOM   4834  C CA  . VAL C 1 187 ? 9.940   34.191  -43.654  1.00 25.85 ? 187 VAL C CA  1 
ATOM   4835  C C   . VAL C 1 187 ? 9.356   33.379  -42.492  1.00 24.88 ? 187 VAL C C   1 
ATOM   4836  O O   . VAL C 1 187 ? 8.603   32.448  -42.737  1.00 24.11 ? 187 VAL C O   1 
ATOM   4837  C CB  . VAL C 1 187 ? 10.931  33.289  -44.429  1.00 26.50 ? 187 VAL C CB  1 
ATOM   4838  C CG1 . VAL C 1 187 ? 11.318  33.934  -45.746  1.00 26.62 ? 187 VAL C CG1 1 
ATOM   4839  C CG2 . VAL C 1 187 ? 12.182  33.011  -43.606  1.00 26.79 ? 187 VAL C CG2 1 
ATOM   4840  N N   . VAL C 1 188 ? 9.731   33.702  -41.251  1.00 24.12 ? 188 VAL C N   1 
ATOM   4841  C CA  . VAL C 1 188 ? 9.213   33.005  -40.054  1.00 24.65 ? 188 VAL C CA  1 
ATOM   4842  C C   . VAL C 1 188 ? 9.121   33.937  -38.842  1.00 24.70 ? 188 VAL C C   1 
ATOM   4843  O O   . VAL C 1 188 ? 9.664   35.041  -38.849  1.00 25.16 ? 188 VAL C O   1 
ATOM   4844  C CB  . VAL C 1 188 ? 10.092  31.807  -39.615  1.00 24.04 ? 188 VAL C CB  1 
ATOM   4845  C CG1 . VAL C 1 188 ? 10.290  30.811  -40.755  1.00 23.69 ? 188 VAL C CG1 1 
ATOM   4846  C CG2 . VAL C 1 188 ? 11.429  32.288  -39.067  1.00 24.03 ? 188 VAL C CG2 1 
ATOM   4847  N N   . SER C 1 189 ? 8.437   33.465  -37.802  1.00 24.69 ? 189 SER C N   1 
ATOM   4848  C CA  . SER C 1 189 ? 8.457   34.123  -36.495  1.00 25.41 ? 189 SER C CA  1 
ATOM   4849  C C   . SER C 1 189 ? 8.563   33.104  -35.367  1.00 27.31 ? 189 SER C C   1 
ATOM   4850  O O   . SER C 1 189 ? 8.437   31.891  -35.578  1.00 25.33 ? 189 SER C O   1 
ATOM   4851  C CB  . SER C 1 189 ? 7.247   35.027  -36.288  1.00 24.66 ? 189 SER C CB  1 
ATOM   4852  O OG  . SER C 1 189 ? 6.124   34.480  -36.895  1.00 23.94 ? 189 SER C OG  1 
ATOM   4853  N N   . THR C 1 190 ? 8.829   33.627  -34.172  1.00 29.27 ? 190 THR C N   1 
ATOM   4854  C CA  . THR C 1 190 ? 9.075   32.790  -33.009  1.00 28.08 ? 190 THR C CA  1 
ATOM   4855  C C   . THR C 1 190 ? 7.735   32.233  -32.523  1.00 27.02 ? 190 THR C C   1 
ATOM   4856  O O   . THR C 1 190 ? 6.997   32.874  -31.764  1.00 25.98 ? 190 THR C O   1 
ATOM   4857  C CB  . THR C 1 190 ? 9.821   33.586  -31.908  1.00 28.71 ? 190 THR C CB  1 
ATOM   4858  O OG1 . THR C 1 190 ? 10.965  34.245  -32.465  1.00 27.42 ? 190 THR C OG1 1 
ATOM   4859  C CG2 . THR C 1 190 ? 10.301  32.678  -30.834  1.00 28.96 ? 190 THR C CG2 1 
ATOM   4860  N N   . ASP C 1 191 ? 7.430   31.030  -32.996  1.00 27.06 ? 191 ASP C N   1 
ATOM   4861  C CA  . ASP C 1 191 ? 6.144   30.378  -32.731  1.00 27.29 ? 191 ASP C CA  1 
ATOM   4862  C C   . ASP C 1 191 ? 6.211   29.322  -31.633  1.00 24.55 ? 191 ASP C C   1 
ATOM   4863  O O   . ASP C 1 191 ? 5.213   28.696  -31.313  1.00 23.33 ? 191 ASP C O   1 
ATOM   4864  C CB  . ASP C 1 191 ? 5.608   29.733  -34.019  1.00 28.52 ? 191 ASP C CB  1 
ATOM   4865  C CG  . ASP C 1 191 ? 6.444   28.541  -34.458  1.00 29.03 ? 191 ASP C CG  1 
ATOM   4866  O OD1 . ASP C 1 191 ? 7.664   28.511  -34.147  1.00 26.79 ? 191 ASP C OD1 1 
ATOM   4867  O OD2 . ASP C 1 191 ? 5.880   27.642  -35.117  1.00 30.03 ? 191 ASP C OD2 1 
ATOM   4868  N N   . GLY C 1 192 ? 7.375   29.102  -31.051  1.00 23.24 ? 192 GLY C N   1 
ATOM   4869  C CA  . GLY C 1 192 ? 7.465   28.146  -29.950  1.00 22.79 ? 192 GLY C CA  1 
ATOM   4870  C C   . GLY C 1 192 ? 6.620   28.551  -28.768  1.00 21.51 ? 192 GLY C C   1 
ATOM   4871  O O   . GLY C 1 192 ? 6.422   29.735  -28.523  1.00 21.65 ? 192 GLY C O   1 
ATOM   4872  N N   . VAL C 1 193 ? 6.132   27.564  -28.033  1.00 21.08 ? 193 VAL C N   1 
ATOM   4873  C CA  . VAL C 1 193 ? 5.253   27.829  -26.885  1.00 20.50 ? 193 VAL C CA  1 
ATOM   4874  C C   . VAL C 1 193 ? 5.904   28.717  -25.807  1.00 19.91 ? 193 VAL C C   1 
ATOM   4875  O O   . VAL C 1 193 ? 5.211   29.449  -25.125  1.00 19.11 ? 193 VAL C O   1 
ATOM   4876  C CB  . VAL C 1 193 ? 4.719   26.517  -26.264  1.00 19.93 ? 193 VAL C CB  1 
ATOM   4877  C CG1 . VAL C 1 193 ? 5.822   25.774  -25.512  1.00 20.18 ? 193 VAL C CG1 1 
ATOM   4878  C CG2 . VAL C 1 193 ? 3.525   26.800  -25.372  1.00 19.67 ? 193 VAL C CG2 1 
ATOM   4879  N N   . ASP C 1 194 ? 7.230   28.659  -25.669  1.00 19.48 ? 194 ASP C N   1 
ATOM   4880  C CA  . ASP C 1 194 ? 7.939   29.440  -24.639  1.00 18.16 ? 194 ASP C CA  1 
ATOM   4881  C C   . ASP C 1 194 ? 8.253   30.872  -25.079  1.00 18.12 ? 194 ASP C C   1 
ATOM   4882  O O   . ASP C 1 194 ? 8.818   31.621  -24.316  1.00 17.51 ? 194 ASP C O   1 
ATOM   4883  C CB  . ASP C 1 194 ? 9.216   28.707  -24.154  1.00 17.60 ? 194 ASP C CB  1 
ATOM   4884  C CG  . ASP C 1 194 ? 10.215  28.388  -25.278  1.00 17.14 ? 194 ASP C CG  1 
ATOM   4885  O OD1 . ASP C 1 194 ? 10.094  28.957  -26.389  1.00 17.17 ? 194 ASP C OD1 1 
ATOM   4886  O OD2 . ASP C 1 194 ? 11.128  27.551  -25.042  1.00 16.92 ? 194 ASP C OD2 1 
ATOM   4887  N N   . GLY C 1 195 ? 7.881   31.238  -26.302  1.00 18.30 ? 195 GLY C N   1 
ATOM   4888  C CA  . GLY C 1 195 ? 8.089   32.593  -26.822  1.00 18.25 ? 195 GLY C CA  1 
ATOM   4889  C C   . GLY C 1 195 ? 9.510   32.912  -27.273  1.00 18.51 ? 195 GLY C C   1 
ATOM   4890  O O   . GLY C 1 195 ? 9.825   34.075  -27.536  1.00 18.47 ? 195 GLY C O   1 
ATOM   4891  N N   . ILE C 1 196 ? 10.370  31.893  -27.359  1.00 18.16 ? 196 ILE C N   1 
ATOM   4892  C CA  . ILE C 1 196 ? 11.775  32.092  -27.729  1.00 18.39 ? 196 ILE C CA  1 
ATOM   4893  C C   . ILE C 1 196 ? 12.279  31.184  -28.843  1.00 17.90 ? 196 ILE C C   1 
ATOM   4894  O O   . ILE C 1 196 ? 13.015  31.643  -29.713  1.00 17.57 ? 196 ILE C O   1 
ATOM   4895  C CB  . ILE C 1 196 ? 12.699  31.945  -26.499  1.00 19.23 ? 196 ILE C CB  1 
ATOM   4896  C CG1 . ILE C 1 196 ? 12.423  33.071  -25.503  1.00 19.81 ? 196 ILE C CG1 1 
ATOM   4897  C CG2 . ILE C 1 196 ? 14.184  31.959  -26.896  1.00 18.67 ? 196 ILE C CG2 1 
ATOM   4898  C CD1 . ILE C 1 196 ? 12.666  32.655  -24.079  1.00 20.03 ? 196 ILE C CD1 1 
ATOM   4899  N N   . HIS C 1 197 ? 11.879  29.917  -28.825  1.00 18.22 ? 197 HIS C N   1 
ATOM   4900  C CA  . HIS C 1 197 ? 12.413  28.908  -29.747  1.00 17.98 ? 197 HIS C CA  1 
ATOM   4901  C C   . HIS C 1 197 ? 11.429  28.501  -30.817  1.00 17.85 ? 197 HIS C C   1 
ATOM   4902  O O   . HIS C 1 197 ? 10.305  28.998  -30.845  1.00 17.27 ? 197 HIS C O   1 
ATOM   4903  C CB  . HIS C 1 197 ? 12.894  27.709  -28.952  1.00 18.14 ? 197 HIS C CB  1 
ATOM   4904  C CG  . HIS C 1 197 ? 13.832  28.093  -27.858  1.00 18.12 ? 197 HIS C CG  1 
ATOM   4905  N ND1 . HIS C 1 197 ? 13.439  28.182  -26.538  1.00 17.71 ? 197 HIS C ND1 1 
ATOM   4906  C CD2 . HIS C 1 197 ? 15.128  28.486  -27.903  1.00 17.71 ? 197 HIS C CD2 1 
ATOM   4907  C CE1 . HIS C 1 197 ? 14.469  28.576  -25.812  1.00 17.85 ? 197 HIS C CE1 1 
ATOM   4908  N NE2 . HIS C 1 197 ? 15.505  28.768  -26.616  1.00 17.87 ? 197 HIS C NE2 1 
ATOM   4909  N N   . PHE C 1 198 ? 11.880  27.632  -31.725  1.00 18.59 ? 198 PHE C N   1 
ATOM   4910  C CA  . PHE C 1 198 ? 11.119  27.320  -32.939  1.00 19.37 ? 198 PHE C CA  1 
ATOM   4911  C C   . PHE C 1 198 ? 10.505  25.915  -32.909  1.00 19.98 ? 198 PHE C C   1 
ATOM   4912  O O   . PHE C 1 198 ? 11.082  24.976  -32.370  1.00 19.40 ? 198 PHE C O   1 
ATOM   4913  C CB  . PHE C 1 198 ? 12.009  27.408  -34.190  1.00 19.12 ? 198 PHE C CB  1 
ATOM   4914  C CG  . PHE C 1 198 ? 12.625  28.761  -34.452  1.00 18.56 ? 198 PHE C CG  1 
ATOM   4915  C CD1 . PHE C 1 198 ? 12.146  29.929  -33.863  1.00 18.93 ? 198 PHE C CD1 1 
ATOM   4916  C CD2 . PHE C 1 198 ? 13.674  28.866  -35.354  1.00 18.62 ? 198 PHE C CD2 1 
ATOM   4917  C CE1 . PHE C 1 198 ? 12.724  31.161  -34.145  1.00 19.00 ? 198 PHE C CE1 1 
ATOM   4918  C CE2 . PHE C 1 198 ? 14.258  30.089  -35.637  1.00 18.94 ? 198 PHE C CE2 1 
ATOM   4919  C CZ  . PHE C 1 198 ? 13.781  31.241  -35.035  1.00 19.07 ? 198 PHE C CZ  1 
ATOM   4920  N N   . THR C 1 199 ? 9.355   25.788  -33.552  1.00 20.89 ? 199 THR C N   1 
ATOM   4921  C CA  . THR C 1 199 ? 8.759   24.486  -33.833  1.00 21.69 ? 199 THR C CA  1 
ATOM   4922  C C   . THR C 1 199 ? 9.457   23.876  -35.040  1.00 22.92 ? 199 THR C C   1 
ATOM   4923  O O   . THR C 1 199 ? 10.190  24.563  -35.747  1.00 21.83 ? 199 THR C O   1 
ATOM   4924  C CB  . THR C 1 199 ? 7.270   24.614  -34.200  1.00 21.10 ? 199 THR C CB  1 
ATOM   4925  O OG1 . THR C 1 199 ? 7.139   25.343  -35.429  1.00 19.94 ? 199 THR C OG1 1 
ATOM   4926  C CG2 . THR C 1 199 ? 6.496   25.307  -33.098  1.00 20.93 ? 199 THR C CG2 1 
ATOM   4927  N N   . ALA C 1 200 ? 9.195   22.594  -35.283  1.00 24.66 ? 200 ALA C N   1 
ATOM   4928  C CA  . ALA C 1 200 ? 9.742   21.913  -36.450  1.00 25.60 ? 200 ALA C CA  1 
ATOM   4929  C C   . ALA C 1 200 ? 9.202   22.506  -37.750  1.00 27.76 ? 200 ALA C C   1 
ATOM   4930  O O   . ALA C 1 200 ? 9.906   22.548  -38.768  1.00 28.49 ? 200 ALA C O   1 
ATOM   4931  C CB  . ALA C 1 200 ? 9.450   20.424  -36.387  1.00 25.06 ? 200 ALA C CB  1 
ATOM   4932  N N   . GLU C 1 201 ? 7.956   22.971  -37.722  1.00 30.27 ? 201 GLU C N   1 
ATOM   4933  C CA  . GLU C 1 201 ? 7.360   23.600  -38.897  1.00 32.16 ? 201 GLU C CA  1 
ATOM   4934  C C   . GLU C 1 201 ? 8.128   24.877  -39.259  1.00 30.17 ? 201 GLU C C   1 
ATOM   4935  O O   . GLU C 1 201 ? 8.397   25.122  -40.425  1.00 28.28 ? 201 GLU C O   1 
ATOM   4936  C CB  . GLU C 1 201 ? 5.860   23.870  -38.694  1.00 36.36 ? 201 GLU C CB  1 
ATOM   4937  C CG  . GLU C 1 201 ? 5.154   24.302  -39.978  1.00 41.59 ? 201 GLU C CG  1 
ATOM   4938  C CD  . GLU C 1 201 ? 3.761   24.913  -39.789  1.00 46.70 ? 201 GLU C CD  1 
ATOM   4939  O OE1 . GLU C 1 201 ? 3.317   25.564  -40.756  1.00 52.90 ? 201 GLU C OE1 1 
ATOM   4940  O OE2 . GLU C 1 201 ? 3.087   24.766  -38.731  1.00 49.96 ? 201 GLU C OE2 1 
ATOM   4941  N N   . THR C 1 202 ? 8.491   25.673  -38.254  1.00 28.35 ? 202 THR C N   1 
ATOM   4942  C CA  . THR C 1 202 ? 9.239   26.919  -38.482  1.00 26.62 ? 202 THR C CA  1 
ATOM   4943  C C   . THR C 1 202 ? 10.656  26.630  -38.956  1.00 27.29 ? 202 THR C C   1 
ATOM   4944  O O   . THR C 1 202 ? 11.185  27.330  -39.815  1.00 27.14 ? 202 THR C O   1 
ATOM   4945  C CB  . THR C 1 202 ? 9.287   27.791  -37.221  1.00 25.31 ? 202 THR C CB  1 
ATOM   4946  O OG1 . THR C 1 202 ? 7.997   28.371  -37.012  1.00 24.43 ? 202 THR C OG1 1 
ATOM   4947  C CG2 . THR C 1 202 ? 10.298  28.920  -37.343  1.00 25.20 ? 202 THR C CG2 1 
ATOM   4948  N N   . ASN C 1 203 ? 11.274  25.602  -38.390  1.00 28.32 ? 203 ASN C N   1 
ATOM   4949  C CA  . ASN C 1 203 ? 12.593  25.161  -38.845  1.00 27.47 ? 203 ASN C CA  1 
ATOM   4950  C C   . ASN C 1 203 ? 12.583  24.842  -40.329  1.00 27.34 ? 203 ASN C C   1 
ATOM   4951  O O   . ASN C 1 203 ? 13.460  25.283  -41.068  1.00 25.16 ? 203 ASN C O   1 
ATOM   4952  C CB  . ASN C 1 203 ? 13.058  23.929  -38.074  1.00 27.03 ? 203 ASN C CB  1 
ATOM   4953  C CG  . ASN C 1 203 ? 13.596  24.256  -36.692  1.00 28.35 ? 203 ASN C CG  1 
ATOM   4954  O OD1 . ASN C 1 203 ? 13.843  25.432  -36.334  1.00 25.21 ? 203 ASN C OD1 1 
ATOM   4955  N ND2 . ASN C 1 203 ? 13.787  23.195  -35.892  1.00 30.14 ? 203 ASN C ND2 1 
ATOM   4956  N N   . ARG C 1 204 ? 11.584  24.071  -40.752  1.00 29.48 ? 204 ARG C N   1 
ATOM   4957  C CA  . ARG C 1 204 ? 11.435  23.675  -42.162  1.00 29.28 ? 204 ARG C CA  1 
ATOM   4958  C C   . ARG C 1 204 ? 11.346  24.875  -43.085  1.00 26.53 ? 204 ARG C C   1 
ATOM   4959  O O   . ARG C 1 204 ? 12.033  24.915  -44.094  1.00 26.29 ? 204 ARG C O   1 
ATOM   4960  C CB  . ARG C 1 204 ? 10.216  22.766  -42.363  1.00 31.80 ? 204 ARG C CB  1 
ATOM   4961  C CG  . ARG C 1 204 ? 10.536  21.276  -42.272  1.00 34.22 ? 204 ARG C CG  1 
ATOM   4962  C CD  . ARG C 1 204 ? 9.327   20.401  -42.598  1.00 36.95 ? 204 ARG C CD  1 
ATOM   4963  N NE  . ARG C 1 204 ? 8.389   20.301  -41.461  1.00 38.97 ? 204 ARG C NE  1 
ATOM   4964  C CZ  . ARG C 1 204 ? 8.554   19.507  -40.400  1.00 38.52 ? 204 ARG C CZ  1 
ATOM   4965  N NH1 . ARG C 1 204 ? 9.632   18.722  -40.277  1.00 39.21 ? 204 ARG C NH1 1 
ATOM   4966  N NH2 . ARG C 1 204 ? 7.642   19.509  -39.444  1.00 38.17 ? 204 ARG C NH2 1 
ATOM   4967  N N   . THR C 1 205 ? 10.513  25.845  -42.735  1.00 24.24 ? 205 THR C N   1 
ATOM   4968  C CA  . THR C 1 205 ? 10.362  27.044  -43.550  1.00 23.86 ? 205 THR C CA  1 
ATOM   4969  C C   . THR C 1 205 ? 11.703  27.774  -43.672  1.00 24.40 ? 205 THR C C   1 
ATOM   4970  O O   . THR C 1 205 ? 12.122  28.132  -44.779  1.00 24.17 ? 205 THR C O   1 
ATOM   4971  C CB  . THR C 1 205 ? 9.304   28.004  -42.962  1.00 22.90 ? 205 THR C CB  1 
ATOM   4972  O OG1 . THR C 1 205 ? 8.108   27.292  -42.674  1.00 22.22 ? 205 THR C OG1 1 
ATOM   4973  C CG2 . THR C 1 205 ? 8.996   29.137  -43.914  1.00 22.41 ? 205 THR C CG2 1 
ATOM   4974  N N   . LEU C 1 206 ? 12.375  27.964  -42.534  1.00 24.21 ? 206 LEU C N   1 
ATOM   4975  C CA  . LEU C 1 206 ? 13.644  28.697  -42.485  1.00 24.08 ? 206 LEU C CA  1 
ATOM   4976  C C   . LEU C 1 206 ? 14.738  27.997  -43.279  1.00 23.87 ? 206 LEU C C   1 
ATOM   4977  O O   . LEU C 1 206 ? 15.458  28.635  -44.040  1.00 22.64 ? 206 LEU C O   1 
ATOM   4978  C CB  . LEU C 1 206 ? 14.099  28.887  -41.032  1.00 23.53 ? 206 LEU C CB  1 
ATOM   4979  C CG  . LEU C 1 206 ? 15.375  29.712  -40.810  1.00 23.16 ? 206 LEU C CG  1 
ATOM   4980  C CD1 . LEU C 1 206 ? 15.246  31.090  -41.444  1.00 23.05 ? 206 LEU C CD1 1 
ATOM   4981  C CD2 . LEU C 1 206 ? 15.698  29.825  -39.330  1.00 22.79 ? 206 LEU C CD2 1 
ATOM   4982  N N   . GLY C 1 207 ? 14.849  26.688  -43.095  1.00 23.98 ? 207 GLY C N   1 
ATOM   4983  C CA  . GLY C 1 207 ? 15.839  25.893  -43.807  1.00 25.49 ? 207 GLY C CA  1 
ATOM   4984  C C   . GLY C 1 207 ? 15.708  26.029  -45.308  1.00 27.08 ? 207 GLY C C   1 
ATOM   4985  O O   . GLY C 1 207 ? 16.704  26.205  -46.018  1.00 27.79 ? 207 GLY C O   1 
ATOM   4986  N N   . ALA C 1 208 ? 14.467  25.961  -45.788  1.00 27.71 ? 208 ALA C N   1 
ATOM   4987  C CA  . ALA C 1 208 ? 14.194  26.019  -47.223  1.00 27.82 ? 208 ALA C CA  1 
ATOM   4988  C C   . ALA C 1 208 ? 14.457  27.415  -47.766  1.00 27.34 ? 208 ALA C C   1 
ATOM   4989  O O   . ALA C 1 208 ? 14.994  27.552  -48.858  1.00 27.17 ? 208 ALA C O   1 
ATOM   4990  C CB  . ALA C 1 208 ? 12.761  25.594  -47.514  1.00 27.36 ? 208 ALA C CB  1 
ATOM   4991  N N   . ALA C 1 209 ? 14.084  28.443  -47.003  1.00 26.30 ? 209 ALA C N   1 
ATOM   4992  C CA  . ALA C 1 209 ? 14.302  29.830  -47.406  1.00 26.57 ? 209 ALA C CA  1 
ATOM   4993  C C   . ALA C 1 209 ? 15.769  30.159  -47.444  1.00 26.27 ? 209 ALA C C   1 
ATOM   4994  O O   . ALA C 1 209 ? 16.231  30.787  -48.394  1.00 28.69 ? 209 ALA C O   1 
ATOM   4995  C CB  . ALA C 1 209 ? 13.600  30.789  -46.462  1.00 27.39 ? 209 ALA C CB  1 
ATOM   4996  N N   . VAL C 1 210 ? 16.512  29.744  -46.419  1.00 24.47 ? 210 VAL C N   1 
ATOM   4997  C CA  . VAL C 1 210 ? 17.949  30.033  -46.353  1.00 23.10 ? 210 VAL C CA  1 
ATOM   4998  C C   . VAL C 1 210 ? 18.707  29.316  -47.473  1.00 21.88 ? 210 VAL C C   1 
ATOM   4999  O O   . VAL C 1 210 ? 19.658  29.855  -48.009  1.00 20.21 ? 210 VAL C O   1 
ATOM   5000  C CB  . VAL C 1 210 ? 18.529  29.708  -44.950  1.00 22.85 ? 210 VAL C CB  1 
ATOM   5001  C CG1 . VAL C 1 210 ? 20.035  29.842  -44.934  1.00 22.92 ? 210 VAL C CG1 1 
ATOM   5002  C CG2 . VAL C 1 210 ? 17.930  30.646  -43.907  1.00 23.25 ? 210 VAL C CG2 1 
ATOM   5003  N N   . ALA C 1 211 ? 18.269  28.115  -47.833  1.00 22.57 ? 211 ALA C N   1 
ATOM   5004  C CA  . ALA C 1 211 ? 18.867  27.371  -48.936  1.00 24.01 ? 211 ALA C CA  1 
ATOM   5005  C C   . ALA C 1 211 ? 18.789  28.132  -50.269  1.00 26.23 ? 211 ALA C C   1 
ATOM   5006  O O   . ALA C 1 211 ? 19.744  28.103  -51.045  1.00 28.19 ? 211 ALA C O   1 
ATOM   5007  C CB  . ALA C 1 211 ? 18.214  26.009  -49.072  1.00 23.87 ? 211 ALA C CB  1 
ATOM   5008  N N   . GLN C 1 212 ? 17.668  28.801  -50.531  1.00 27.51 ? 212 GLN C N   1 
ATOM   5009  C CA  . GLN C 1 212 ? 17.514  29.629  -51.734  1.00 29.30 ? 212 GLN C CA  1 
ATOM   5010  C C   . GLN C 1 212 ? 18.571  30.736  -51.715  1.00 29.40 ? 212 GLN C C   1 
ATOM   5011  O O   . GLN C 1 212 ? 19.268  30.969  -52.704  1.00 30.09 ? 212 GLN C O   1 
ATOM   5012  C CB  . GLN C 1 212 ? 16.107  30.271  -51.813  1.00 31.54 ? 212 GLN C CB  1 
ATOM   5013  C CG  . GLN C 1 212 ? 15.066  29.655  -52.790  1.00 33.73 ? 212 GLN C CG  1 
ATOM   5014  C CD  . GLN C 1 212 ? 15.716  29.057  -54.050  1.00 36.32 ? 212 GLN C CD  1 
ATOM   5015  O OE1 . GLN C 1 212 ? 16.541  29.695  -54.722  1.00 39.08 ? 212 GLN C OE1 1 
ATOM   5016  N NE2 . GLN C 1 212 ? 15.360  27.821  -54.359  1.00 35.17 ? 212 GLN C NE2 1 
ATOM   5017  N N   . LYS C 1 213 ? 18.675  31.406  -50.574  1.00 29.77 ? 213 LYS C N   1 
ATOM   5018  C CA  . LYS C 1 213 ? 19.617  32.494  -50.405  1.00 30.38 ? 213 LYS C CA  1 
ATOM   5019  C C   . LYS C 1 213 ? 21.057  32.021  -50.633  1.00 31.16 ? 213 LYS C C   1 
ATOM   5020  O O   . LYS C 1 213 ? 21.826  32.670  -51.335  1.00 30.82 ? 213 LYS C O   1 
ATOM   5021  C CB  . LYS C 1 213 ? 19.460  33.103  -49.000  1.00 29.67 ? 213 LYS C CB  1 
ATOM   5022  C CG  . LYS C 1 213 ? 20.384  34.267  -48.683  1.00 28.60 ? 213 LYS C CG  1 
ATOM   5023  C CD  . LYS C 1 213 ? 20.221  35.408  -49.684  1.00 28.03 ? 213 LYS C CD  1 
ATOM   5024  C CE  . LYS C 1 213 ? 20.634  36.756  -49.122  1.00 28.26 ? 213 LYS C CE  1 
ATOM   5025  N NZ  . LYS C 1 213 ? 21.460  37.565  -50.079  1.00 28.53 ? 213 LYS C NZ  1 
ATOM   5026  N N   . VAL C 1 214 ? 21.410  30.885  -50.047  1.00 31.55 ? 214 VAL C N   1 
ATOM   5027  C CA  . VAL C 1 214 ? 22.760  30.345  -50.172  1.00 33.28 ? 214 VAL C CA  1 
ATOM   5028  C C   . VAL C 1 214 ? 23.133  30.094  -51.636  1.00 34.69 ? 214 VAL C C   1 
ATOM   5029  O O   . VAL C 1 214 ? 24.208  30.516  -52.079  1.00 36.40 ? 214 VAL C O   1 
ATOM   5030  C CB  . VAL C 1 214 ? 22.933  29.065  -49.334  1.00 33.02 ? 214 VAL C CB  1 
ATOM   5031  C CG1 . VAL C 1 214 ? 24.231  28.370  -49.665  1.00 33.43 ? 214 VAL C CG1 1 
ATOM   5032  C CG2 . VAL C 1 214 ? 22.922  29.408  -47.850  1.00 33.22 ? 214 VAL C CG2 1 
ATOM   5033  N N   . LYS C 1 215 ? 22.252  29.428  -52.382  1.00 33.78 ? 215 LYS C N   1 
ATOM   5034  C CA  . LYS C 1 215 ? 22.493  29.140  -53.807  1.00 32.88 ? 215 LYS C CA  1 
ATOM   5035  C C   . LYS C 1 215 ? 22.725  30.411  -54.636  1.00 34.11 ? 215 LYS C C   1 
ATOM   5036  O O   . LYS C 1 215 ? 23.561  30.424  -55.542  1.00 39.54 ? 215 LYS C O   1 
ATOM   5037  C CB  . LYS C 1 215 ? 21.326  28.379  -54.409  1.00 32.03 ? 215 LYS C CB  1 
ATOM   5038  C CG  . LYS C 1 215 ? 21.209  26.949  -53.950  1.00 32.93 ? 215 LYS C CG  1 
ATOM   5039  C CD  . LYS C 1 215 ? 19.914  26.343  -54.498  1.00 33.80 ? 215 LYS C CD  1 
ATOM   5040  C CE  . LYS C 1 215 ? 19.392  25.163  -53.671  1.00 34.94 ? 215 LYS C CE  1 
ATOM   5041  N NZ  . LYS C 1 215 ? 17.893  25.199  -53.466  1.00 34.51 ? 215 LYS C NZ  1 
ATOM   5042  N N   . THR C 1 216 ? 21.967  31.460  -54.337  1.00 32.58 ? 216 THR C N   1 
ATOM   5043  C CA  . THR C 1 216 ? 22.205  32.774  -54.921  1.00 34.17 ? 216 THR C CA  1 
ATOM   5044  C C   . THR C 1 216 ? 23.652  33.249  -54.726  1.00 37.18 ? 216 THR C C   1 
ATOM   5045  O O   . THR C 1 216 ? 24.240  33.814  -55.649  1.00 36.59 ? 216 THR C O   1 
ATOM   5046  C CB  . THR C 1 216 ? 21.249  33.820  -54.312  1.00 34.46 ? 216 THR C CB  1 
ATOM   5047  O OG1 . THR C 1 216 ? 19.925  33.548  -54.769  1.00 34.54 ? 216 THR C OG1 1 
ATOM   5048  C CG2 . THR C 1 216 ? 21.640  35.261  -54.679  1.00 34.03 ? 216 THR C CG2 1 
ATOM   5049  N N   . LEU C 1 217 ? 24.213  33.017  -53.538  1.00 41.39 ? 217 LEU C N   1 
ATOM   5050  C CA  . LEU C 1 217 ? 25.570  33.465  -53.220  1.00 41.37 ? 217 LEU C CA  1 
ATOM   5051  C C   . LEU C 1 217 ? 26.669  32.587  -53.814  1.00 41.48 ? 217 LEU C C   1 
ATOM   5052  O O   . LEU C 1 217 ? 27.694  33.101  -54.233  1.00 43.36 ? 217 LEU C O   1 
ATOM   5053  C CB  . LEU C 1 217 ? 25.768  33.552  -51.706  1.00 39.46 ? 217 LEU C CB  1 
ATOM   5054  C CG  . LEU C 1 217 ? 24.880  34.536  -50.950  1.00 38.35 ? 217 LEU C CG  1 
ATOM   5055  C CD1 . LEU C 1 217 ? 25.198  34.466  -49.460  1.00 37.23 ? 217 LEU C CD1 1 
ATOM   5056  C CD2 . LEU C 1 217 ? 25.124  35.975  -51.368  1.00 38.18 ? 217 LEU C CD2 1 
ATOM   5057  N N   . LEU C 1 218 ? 26.463  31.276  -53.853  1.00 42.90 ? 218 LEU C N   1 
ATOM   5058  C CA  . LEU C 1 218 ? 27.535  30.360  -54.257  1.00 46.90 ? 218 LEU C CA  1 
ATOM   5059  C C   . LEU C 1 218 ? 27.470  29.795  -55.699  1.00 49.96 ? 218 LEU C C   1 
ATOM   5060  O O   . LEU C 1 218 ? 28.480  29.373  -56.222  1.00 51.40 ? 218 LEU C O   1 
ATOM   5061  C CB  . LEU C 1 218 ? 27.620  29.218  -53.247  1.00 47.24 ? 218 LEU C CB  1 
ATOM   5062  C CG  . LEU C 1 218 ? 27.884  29.639  -51.776  1.00 46.46 ? 218 LEU C CG  1 
ATOM   5063  C CD1 . LEU C 1 218 ? 27.947  28.444  -50.842  1.00 47.45 ? 218 LEU C CD1 1 
ATOM   5064  C CD2 . LEU C 1 218 ? 29.144  30.485  -51.616  1.00 45.92 ? 218 LEU C CD2 1 
ATOM   5065  N N   . GLN C 1 219 ? 26.298  29.848  -56.363  1.00 53.21 ? 219 GLN C N   1 
ATOM   5066  C CA  . GLN C 1 219 ? 26.006  29.002  -57.569  1.00 53.76 ? 219 GLN C CA  1 
ATOM   5067  C C   . GLN C 1 219 ? 26.541  27.568  -57.412  1.00 56.24 ? 219 GLN C C   1 
ATOM   5068  O O   . GLN C 1 219 ? 25.797  26.642  -57.075  1.00 56.17 ? 219 GLN C O   1 
ATOM   5069  C CB  . GLN C 1 219 ? 26.540  29.596  -58.911  1.00 53.06 ? 219 GLN C CB  1 
ATOM   5070  C CG  . GLN C 1 219 ? 25.568  30.547  -59.614  1.00 51.72 ? 219 GLN C CG  1 
ATOM   5071  C CD  . GLN C 1 219 ? 25.564  31.909  -58.963  1.00 48.72 ? 219 GLN C CD  1 
ATOM   5072  O OE1 . GLN C 1 219 ? 26.577  32.306  -58.401  1.00 46.75 ? 219 GLN C OE1 1 
ATOM   5073  N NE2 . GLN C 1 219 ? 24.425  32.597  -58.975  1.00 45.93 ? 219 GLN C NE2 1 
ATOM   5074  N N   . ASP D 1 2   ? 9.858   50.130  -44.803  1.00 65.28 ? 2   ASP D N   1 
ATOM   5075  C CA  . ASP D 1 2   ? 9.449   48.763  -45.353  1.00 64.60 ? 2   ASP D CA  1 
ATOM   5076  C C   . ASP D 1 2   ? 9.396   48.738  -46.884  1.00 62.47 ? 2   ASP D C   1 
ATOM   5077  O O   . ASP D 1 2   ? 8.501   49.376  -47.475  1.00 56.73 ? 2   ASP D O   1 
ATOM   5078  C CB  . ASP D 1 2   ? 8.087   48.320  -44.812  1.00 65.86 ? 2   ASP D CB  1 
ATOM   5079  C CG  . ASP D 1 2   ? 8.174   47.700  -43.444  1.00 69.86 ? 2   ASP D CG  1 
ATOM   5080  O OD1 . ASP D 1 2   ? 9.178   47.005  -43.187  1.00 70.86 ? 2   ASP D OD1 1 
ATOM   5081  O OD2 . ASP D 1 2   ? 7.241   47.898  -42.625  1.00 72.44 ? 2   ASP D OD2 1 
ATOM   5082  N N   . LYS D 1 3   ? 10.384  48.075  -47.483  1.00 58.44 ? 3   LYS D N   1 
ATOM   5083  C CA  . LYS D 1 3   ? 10.732  48.295  -48.895  1.00 53.20 ? 3   LYS D CA  1 
ATOM   5084  C C   . LYS D 1 3   ? 9.535   48.053  -49.819  1.00 48.24 ? 3   LYS D C   1 
ATOM   5085  O O   . LYS D 1 3   ? 8.847   47.062  -49.677  1.00 47.08 ? 3   LYS D O   1 
ATOM   5086  C CB  . LYS D 1 3   ? 11.908  47.374  -49.268  1.00 54.96 ? 3   LYS D CB  1 
ATOM   5087  C CG  . LYS D 1 3   ? 12.483  47.568  -50.661  1.00 57.77 ? 3   LYS D CG  1 
ATOM   5088  C CD  . LYS D 1 3   ? 13.006  46.263  -51.264  1.00 59.11 ? 3   LYS D CD  1 
ATOM   5089  C CE  . LYS D 1 3   ? 13.810  46.564  -52.494  1.00 61.02 ? 3   LYS D CE  1 
ATOM   5090  N NZ  . LYS D 1 3   ? 13.625  45.523  -53.532  1.00 61.23 ? 3   LYS D NZ  1 
ATOM   5091  N N   . ILE D 1 4   ? 9.269   48.995  -50.735  1.00 43.43 ? 4   ILE D N   1 
ATOM   5092  C CA  . ILE D 1 4   ? 8.167   48.848  -51.694  1.00 38.64 ? 4   ILE D CA  1 
ATOM   5093  C C   . ILE D 1 4   ? 8.629   47.909  -52.800  1.00 37.95 ? 4   ILE D C   1 
ATOM   5094  O O   . ILE D 1 4   ? 9.707   48.084  -53.351  1.00 42.96 ? 4   ILE D O   1 
ATOM   5095  C CB  . ILE D 1 4   ? 7.737   50.213  -52.264  1.00 36.48 ? 4   ILE D CB  1 
ATOM   5096  C CG1 . ILE D 1 4   ? 7.067   51.055  -51.160  1.00 37.40 ? 4   ILE D CG1 1 
ATOM   5097  C CG2 . ILE D 1 4   ? 6.707   50.044  -53.322  1.00 35.31 ? 4   ILE D CG2 1 
ATOM   5098  C CD1 . ILE D 1 4   ? 6.985   52.554  -51.430  1.00 37.10 ? 4   ILE D CD1 1 
ATOM   5099  N N   . LYS D 1 5   ? 7.807   46.923  -53.137  1.00 35.44 ? 5   LYS D N   1 
ATOM   5100  C CA  . LYS D 1 5   ? 8.155   45.926  -54.168  1.00 31.91 ? 5   LYS D CA  1 
ATOM   5101  C C   . LYS D 1 5   ? 7.796   46.370  -55.581  1.00 27.96 ? 5   LYS D C   1 
ATOM   5102  O O   . LYS D 1 5   ? 6.662   46.762  -55.860  1.00 25.77 ? 5   LYS D O   1 
ATOM   5103  C CB  . LYS D 1 5   ? 7.476   44.606  -53.837  1.00 32.74 ? 5   LYS D CB  1 
ATOM   5104  C CG  . LYS D 1 5   ? 8.176   43.925  -52.683  1.00 34.41 ? 5   LYS D CG  1 
ATOM   5105  C CD  . LYS D 1 5   ? 7.398   42.760  -52.120  1.00 36.24 ? 5   LYS D CD  1 
ATOM   5106  C CE  . LYS D 1 5   ? 7.872   42.451  -50.713  1.00 38.21 ? 5   LYS D CE  1 
ATOM   5107  N NZ  . LYS D 1 5   ? 6.737   41.827  -50.002  1.00 40.18 ? 5   LYS D NZ  1 
ATOM   5108  N N   . ARG D 1 6   ? 8.782   46.293  -56.472  1.00 25.23 ? 6   ARG D N   1 
ATOM   5109  C CA  . ARG D 1 6   ? 8.611   46.816  -57.826  1.00 24.14 ? 6   ARG D CA  1 
ATOM   5110  C C   . ARG D 1 6   ? 8.295   45.712  -58.845  1.00 22.99 ? 6   ARG D C   1 
ATOM   5111  O O   . ARG D 1 6   ? 9.059   44.753  -58.993  1.00 22.57 ? 6   ARG D O   1 
ATOM   5112  C CB  . ARG D 1 6   ? 9.849   47.623  -58.211  1.00 23.98 ? 6   ARG D CB  1 
ATOM   5113  C CG  . ARG D 1 6   ? 9.956   48.932  -57.427  1.00 23.59 ? 6   ARG D CG  1 
ATOM   5114  C CD  . ARG D 1 6   ? 11.273  49.664  -57.623  1.00 23.41 ? 6   ARG D CD  1 
ATOM   5115  N NE  . ARG D 1 6   ? 11.688  49.769  -59.024  1.00 23.49 ? 6   ARG D NE  1 
ATOM   5116  C CZ  . ARG D 1 6   ? 11.080  50.514  -59.950  1.00 23.78 ? 6   ARG D CZ  1 
ATOM   5117  N NH1 . ARG D 1 6   ? 9.988   51.229  -59.646  1.00 23.68 ? 6   ARG D NH1 1 
ATOM   5118  N NH2 . ARG D 1 6   ? 11.579  50.568  -61.187  1.00 23.70 ? 6   ARG D NH2 1 
ATOM   5119  N N   . VAL D 1 7   ? 7.156   45.845  -59.533  1.00 21.34 ? 7   VAL D N   1 
ATOM   5120  C CA  . VAL D 1 7   ? 6.726   44.848  -60.528  1.00 20.28 ? 7   VAL D CA  1 
ATOM   5121  C C   . VAL D 1 7   ? 6.643   45.447  -61.934  1.00 19.69 ? 7   VAL D C   1 
ATOM   5122  O O   . VAL D 1 7   ? 5.909   46.402  -62.163  1.00 18.92 ? 7   VAL D O   1 
ATOM   5123  C CB  . VAL D 1 7   ? 5.361   44.258  -60.156  1.00 19.73 ? 7   VAL D CB  1 
ATOM   5124  C CG1 . VAL D 1 7   ? 4.952   43.183  -61.147  1.00 19.63 ? 7   VAL D CG1 1 
ATOM   5125  C CG2 . VAL D 1 7   ? 5.379   43.717  -58.744  1.00 20.07 ? 7   VAL D CG2 1 
ATOM   5126  N N   . PHE D 1 8   ? 7.400   44.879  -62.870  1.00 19.92 ? 8   PHE D N   1 
ATOM   5127  C CA  . PHE D 1 8   ? 7.427   45.362  -64.248  1.00 19.80 ? 8   PHE D CA  1 
ATOM   5128  C C   . PHE D 1 8   ? 6.562   44.462  -65.109  1.00 18.57 ? 8   PHE D C   1 
ATOM   5129  O O   . PHE D 1 8   ? 6.742   43.251  -65.110  1.00 18.04 ? 8   PHE D O   1 
ATOM   5130  C CB  . PHE D 1 8   ? 8.858   45.364  -64.773  1.00 20.50 ? 8   PHE D CB  1 
ATOM   5131  C CG  . PHE D 1 8   ? 8.986   45.812  -66.204  1.00 20.51 ? 8   PHE D CG  1 
ATOM   5132  C CD1 . PHE D 1 8   ? 8.420   46.995  -66.619  1.00 19.63 ? 8   PHE D CD1 1 
ATOM   5133  C CD2 . PHE D 1 8   ? 9.709   45.056  -67.129  1.00 20.50 ? 8   PHE D CD2 1 
ATOM   5134  C CE1 . PHE D 1 8   ? 8.558   47.422  -67.925  1.00 19.65 ? 8   PHE D CE1 1 
ATOM   5135  C CE2 . PHE D 1 8   ? 9.855   45.487  -68.434  1.00 19.92 ? 8   PHE D CE2 1 
ATOM   5136  C CZ  . PHE D 1 8   ? 9.277   46.667  -68.835  1.00 19.58 ? 8   PHE D CZ  1 
ATOM   5137  N N   . VAL D 1 9   ? 5.619   45.062  -65.832  1.00 17.67 ? 9   VAL D N   1 
ATOM   5138  C CA  . VAL D 1 9   ? 4.713   44.316  -66.702  1.00 17.15 ? 9   VAL D CA  1 
ATOM   5139  C C   . VAL D 1 9   ? 5.030   44.608  -68.162  1.00 17.18 ? 9   VAL D C   1 
ATOM   5140  O O   . VAL D 1 9   ? 4.951   45.756  -68.608  1.00 17.44 ? 9   VAL D O   1 
ATOM   5141  C CB  . VAL D 1 9   ? 3.242   44.684  -66.455  1.00 16.69 ? 9   VAL D CB  1 
ATOM   5142  C CG1 . VAL D 1 9   ? 2.341   43.722  -67.200  1.00 16.54 ? 9   VAL D CG1 1 
ATOM   5143  C CG2 . VAL D 1 9   ? 2.926   44.640  -64.979  1.00 17.00 ? 9   VAL D CG2 1 
ATOM   5144  N N   . PHE D 1 10  ? 5.342   43.555  -68.907  1.00 16.69 ? 10  PHE D N   1 
ATOM   5145  C CA  . PHE D 1 10  ? 5.809   43.671  -70.275  1.00 16.19 ? 10  PHE D CA  1 
ATOM   5146  C C   . PHE D 1 10  ? 4.829   42.928  -71.154  1.00 16.84 ? 10  PHE D C   1 
ATOM   5147  O O   . PHE D 1 10  ? 4.728   41.697  -71.074  1.00 17.43 ? 10  PHE D O   1 
ATOM   5148  C CB  . PHE D 1 10  ? 7.195   43.026  -70.364  1.00 15.68 ? 10  PHE D CB  1 
ATOM   5149  C CG  . PHE D 1 10  ? 7.899   43.256  -71.663  1.00 14.97 ? 10  PHE D CG  1 
ATOM   5150  C CD1 . PHE D 1 10  ? 8.199   44.532  -72.074  1.00 14.81 ? 10  PHE D CD1 1 
ATOM   5151  C CD2 . PHE D 1 10  ? 8.289   42.184  -72.456  1.00 14.78 ? 10  PHE D CD2 1 
ATOM   5152  C CE1 . PHE D 1 10  ? 8.858   44.739  -73.265  1.00 15.13 ? 10  PHE D CE1 1 
ATOM   5153  C CE2 . PHE D 1 10  ? 8.955   42.379  -73.643  1.00 14.56 ? 10  PHE D CE2 1 
ATOM   5154  C CZ  . PHE D 1 10  ? 9.236   43.659  -74.049  1.00 15.06 ? 10  PHE D CZ  1 
ATOM   5155  N N   . GLY D 1 11  ? 4.103   43.652  -71.992  1.00 17.34 ? 11  GLY D N   1 
ATOM   5156  C CA  . GLY D 1 11  ? 3.097   43.013  -72.832  1.00 18.48 ? 11  GLY D CA  1 
ATOM   5157  C C   . GLY D 1 11  ? 2.813   43.713  -74.141  1.00 19.75 ? 11  GLY D C   1 
ATOM   5158  O O   . GLY D 1 11  ? 3.611   44.503  -74.629  1.00 18.85 ? 11  GLY D O   1 
ATOM   5159  N N   . ASP D 1 12  ? 1.647   43.404  -74.695  1.00 22.74 ? 12  ASP D N   1 
ATOM   5160  C CA  . ASP D 1 12  ? 1.238   43.889  -76.005  1.00 24.28 ? 12  ASP D CA  1 
ATOM   5161  C C   . ASP D 1 12  ? 0.053   44.834  -75.813  1.00 25.77 ? 12  ASP D C   1 
ATOM   5162  O O   . ASP D 1 12  ? -0.038  45.502  -74.799  1.00 27.77 ? 12  ASP D O   1 
ATOM   5163  C CB  . ASP D 1 12  ? 0.944   42.700  -76.955  1.00 24.71 ? 12  ASP D CB  1 
ATOM   5164  C CG  . ASP D 1 12  ? 0.072   41.615  -76.316  1.00 24.72 ? 12  ASP D CG  1 
ATOM   5165  O OD1 . ASP D 1 12  ? -0.692  41.952  -75.380  1.00 24.63 ? 12  ASP D OD1 1 
ATOM   5166  O OD2 . ASP D 1 12  ? 0.192   40.436  -76.753  1.00 25.79 ? 12  ASP D OD2 1 
HETATM 5167  N N   . SEP D 1 13  ? -0.844  44.908  -76.784  1.00 27.93 ? 13  SEP D N   1 
HETATM 5168  C CA  . SEP D 1 13  ? -1.974  45.849  -76.767  1.00 30.04 ? 13  SEP D CA  1 
HETATM 5169  C CB  . SEP D 1 13  ? -2.718  45.808  -78.134  1.00 35.81 ? 13  SEP D CB  1 
HETATM 5170  O OG  . SEP D 1 13  ? -2.043  44.998  -79.167  1.00 44.43 ? 13  SEP D OG  1 
HETATM 5171  C C   . SEP D 1 13  ? -2.916  45.537  -75.651  1.00 26.42 ? 13  SEP D C   1 
HETATM 5172  O O   . SEP D 1 13  ? -3.585  46.421  -75.155  1.00 25.16 ? 13  SEP D O   1 
HETATM 5173  P P   . SEP D 1 13  ? -2.412  43.515  -79.727  1.00 44.32 ? 13  SEP D P   1 
HETATM 5174  O O1P . SEP D 1 13  ? -3.254  43.980  -80.898  1.00 45.52 ? 13  SEP D O1P 1 
HETATM 5175  O O2P . SEP D 1 13  ? -1.073  42.863  -79.940  1.00 42.75 ? 13  SEP D O2P 1 
HETATM 5176  O O3P . SEP D 1 13  ? -3.392  42.806  -78.808  1.00 47.66 ? 13  SEP D O3P 1 
ATOM   5177  N N   . LEU D 1 14  ? -2.984  44.269  -75.254  1.00 24.36 ? 14  LEU D N   1 
ATOM   5178  C CA  . LEU D 1 14  ? -3.796  43.845  -74.106  1.00 22.96 ? 14  LEU D CA  1 
ATOM   5179  C C   . LEU D 1 14  ? -3.371  44.580  -72.830  1.00 22.10 ? 14  LEU D C   1 
ATOM   5180  O O   . LEU D 1 14  ? -4.184  44.854  -71.968  1.00 20.47 ? 14  LEU D O   1 
ATOM   5181  C CB  . LEU D 1 14  ? -3.674  42.337  -73.864  1.00 22.47 ? 14  LEU D CB  1 
ATOM   5182  C CG  . LEU D 1 14  ? -4.165  41.373  -74.955  1.00 23.25 ? 14  LEU D CG  1 
ATOM   5183  C CD1 . LEU D 1 14  ? -3.856  39.914  -74.615  1.00 23.04 ? 14  LEU D CD1 1 
ATOM   5184  C CD2 . LEU D 1 14  ? -5.652  41.551  -75.246  1.00 24.57 ? 14  LEU D CD2 1 
ATOM   5185  N N   . THR D 1 15  ? -2.078  44.863  -72.728  1.00 22.06 ? 15  THR D N   1 
ATOM   5186  C CA  . THR D 1 15  ? -1.466  45.525  -71.579  1.00 20.71 ? 15  THR D CA  1 
ATOM   5187  C C   . THR D 1 15  ? -1.402  47.061  -71.762  1.00 20.67 ? 15  THR D C   1 
ATOM   5188  O O   . THR D 1 15  ? -1.431  47.804  -70.795  1.00 20.22 ? 15  THR D O   1 
ATOM   5189  C CB  . THR D 1 15  ? -0.060  44.929  -71.346  1.00 19.25 ? 15  THR D CB  1 
ATOM   5190  O OG1 . THR D 1 15  ? -0.163  43.506  -71.197  1.00 17.82 ? 15  THR D OG1 1 
ATOM   5191  C CG2 . THR D 1 15  ? 0.602   45.535  -70.135  1.00 18.80 ? 15  THR D CG2 1 
ATOM   5192  N N   . TRP D 1 16  ? -1.301  47.524  -73.002  1.00 21.55 ? 16  TRP D N   1 
ATOM   5193  C CA  . TRP D 1 16  ? -1.445  48.952  -73.325  1.00 22.60 ? 16  TRP D CA  1 
ATOM   5194  C C   . TRP D 1 16  ? -2.836  49.438  -72.944  1.00 22.58 ? 16  TRP D C   1 
ATOM   5195  O O   . TRP D 1 16  ? -2.996  50.497  -72.346  1.00 21.78 ? 16  TRP D O   1 
ATOM   5196  C CB  . TRP D 1 16  ? -1.231  49.184  -74.830  1.00 23.56 ? 16  TRP D CB  1 
ATOM   5197  C CG  . TRP D 1 16  ? -1.372  50.639  -75.281  1.00 24.40 ? 16  TRP D CG  1 
ATOM   5198  C CD1 . TRP D 1 16  ? -0.521  51.678  -75.013  1.00 25.13 ? 16  TRP D CD1 1 
ATOM   5199  C CD2 . TRP D 1 16  ? -2.414  51.186  -76.101  1.00 25.12 ? 16  TRP D CD2 1 
ATOM   5200  N NE1 . TRP D 1 16  ? -0.980  52.832  -75.597  1.00 25.11 ? 16  TRP D NE1 1 
ATOM   5201  C CE2 . TRP D 1 16  ? -2.136  52.555  -76.276  1.00 25.14 ? 16  TRP D CE2 1 
ATOM   5202  C CE3 . TRP D 1 16  ? -3.560  50.652  -76.695  1.00 25.65 ? 16  TRP D CE3 1 
ATOM   5203  C CZ2 . TRP D 1 16  ? -2.964  53.399  -77.020  1.00 25.17 ? 16  TRP D CZ2 1 
ATOM   5204  C CZ3 . TRP D 1 16  ? -4.384  51.492  -77.433  1.00 25.85 ? 16  TRP D CZ3 1 
ATOM   5205  C CH2 . TRP D 1 16  ? -4.077  52.850  -77.591  1.00 25.15 ? 16  TRP D CH2 1 
ATOM   5206  N N   . GLY D 1 17  ? -3.838  48.645  -73.316  1.00 22.87 ? 17  GLY D N   1 
ATOM   5207  C CA  . GLY D 1 17  ? -5.234  48.971  -73.056  1.00 22.80 ? 17  GLY D CA  1 
ATOM   5208  C C   . GLY D 1 17  ? -6.047  49.212  -74.318  1.00 22.38 ? 17  GLY D C   1 
ATOM   5209  O O   . GLY D 1 17  ? -6.741  50.219  -74.412  1.00 23.15 ? 17  GLY D O   1 
ATOM   5210  N N   . TRP D 1 18  ? -5.978  48.287  -75.272  1.00 21.30 ? 18  TRP D N   1 
ATOM   5211  C CA  . TRP D 1 18  ? -6.748  48.389  -76.505  1.00 20.52 ? 18  TRP D CA  1 
ATOM   5212  C C   . TRP D 1 18  ? -8.228  48.239  -76.190  1.00 20.24 ? 18  TRP D C   1 
ATOM   5213  O O   . TRP D 1 18  ? -8.646  47.208  -75.648  1.00 19.41 ? 18  TRP D O   1 
ATOM   5214  C CB  . TRP D 1 18  ? -6.335  47.286  -77.491  1.00 20.40 ? 18  TRP D CB  1 
ATOM   5215  C CG  . TRP D 1 18  ? -6.981  47.357  -78.863  1.00 20.23 ? 18  TRP D CG  1 
ATOM   5216  C CD1 . TRP D 1 18  ? -8.305  47.268  -79.156  1.00 20.45 ? 18  TRP D CD1 1 
ATOM   5217  C CD2 . TRP D 1 18  ? -6.305  47.480  -80.122  1.00 20.37 ? 18  TRP D CD2 1 
ATOM   5218  N NE1 . TRP D 1 18  ? -8.507  47.356  -80.516  1.00 20.66 ? 18  TRP D NE1 1 
ATOM   5219  C CE2 . TRP D 1 18  ? -7.290  47.486  -81.130  1.00 20.33 ? 18  TRP D CE2 1 
ATOM   5220  C CE3 . TRP D 1 18  ? -4.963  47.600  -80.494  1.00 19.97 ? 18  TRP D CE3 1 
ATOM   5221  C CZ2 . TRP D 1 18  ? -6.973  47.598  -82.485  1.00 20.10 ? 18  TRP D CZ2 1 
ATOM   5222  C CZ3 . TRP D 1 18  ? -4.645  47.709  -81.837  1.00 19.79 ? 18  TRP D CZ3 1 
ATOM   5223  C CH2 . TRP D 1 18  ? -5.648  47.721  -82.818  1.00 20.08 ? 18  TRP D CH2 1 
ATOM   5224  N N   . THR D 1 19  ? -9.007  49.262  -76.549  1.00 20.14 ? 19  THR D N   1 
ATOM   5225  C CA  . THR D 1 19  ? -10.456 49.219  -76.410  1.00 20.67 ? 19  THR D CA  1 
ATOM   5226  C C   . THR D 1 19  ? -11.040 48.520  -77.643  1.00 21.74 ? 19  THR D C   1 
ATOM   5227  O O   . THR D 1 19  ? -10.883 49.030  -78.750  1.00 22.21 ? 19  THR D O   1 
ATOM   5228  C CB  . THR D 1 19  ? -11.069 50.636  -76.294  1.00 19.50 ? 19  THR D CB  1 
ATOM   5229  O OG1 . THR D 1 19  ? -10.534 51.311  -75.157  1.00 18.96 ? 19  THR D OG1 1 
ATOM   5230  C CG2 . THR D 1 19  ? -12.564 50.558  -76.128  1.00 19.09 ? 19  THR D CG2 1 
ATOM   5231  N N   . PRO D 1 20  ? -11.693 47.344  -77.465  1.00 22.27 ? 20  PRO D N   1 
ATOM   5232  C CA  . PRO D 1 20  ? -12.280 46.654  -78.621  1.00 23.06 ? 20  PRO D CA  1 
ATOM   5233  C C   . PRO D 1 20  ? -13.445 47.444  -79.217  1.00 24.39 ? 20  PRO D C   1 
ATOM   5234  O O   . PRO D 1 20  ? -14.299 47.932  -78.473  1.00 24.44 ? 20  PRO D O   1 
ATOM   5235  C CB  . PRO D 1 20  ? -12.766 45.308  -78.051  1.00 22.32 ? 20  PRO D CB  1 
ATOM   5236  C CG  . PRO D 1 20  ? -12.778 45.467  -76.586  1.00 21.93 ? 20  PRO D CG  1 
ATOM   5237  C CD  . PRO D 1 20  ? -11.830 46.566  -76.224  1.00 21.83 ? 20  PRO D CD  1 
ATOM   5238  N N   . VAL D 1 21  ? -13.453 47.572  -80.545  1.00 25.85 ? 21  VAL D N   1 
ATOM   5239  C CA  . VAL D 1 21  ? -14.422 48.410  -81.244  1.00 26.94 ? 21  VAL D CA  1 
ATOM   5240  C C   . VAL D 1 21  ? -14.744 47.884  -82.636  1.00 27.78 ? 21  VAL D C   1 
ATOM   5241  O O   . VAL D 1 21  ? -14.091 46.960  -83.135  1.00 30.02 ? 21  VAL D O   1 
ATOM   5242  C CB  . VAL D 1 21  ? -13.923 49.865  -81.372  1.00 27.75 ? 21  VAL D CB  1 
ATOM   5243  C CG1 . VAL D 1 21  ? -14.010 50.578  -80.024  1.00 27.61 ? 21  VAL D CG1 1 
ATOM   5244  C CG2 . VAL D 1 21  ? -12.505 49.899  -81.936  1.00 27.82 ? 21  VAL D CG2 1 
ATOM   5245  N N   . ALA D 1 22  ? -15.767 48.473  -83.247  1.00 27.64 ? 22  ALA D N   1 
ATOM   5246  C CA  . ALA D 1 22  ? -16.163 48.131  -84.601  1.00 27.05 ? 22  ALA D CA  1 
ATOM   5247  C C   . ALA D 1 22  ? -16.303 49.428  -85.407  1.00 26.22 ? 22  ALA D C   1 
ATOM   5248  O O   . ALA D 1 22  ? -17.029 50.316  -84.994  1.00 25.24 ? 22  ALA D O   1 
ATOM   5249  C CB  . ALA D 1 22  ? -17.464 47.353  -84.581  1.00 26.14 ? 22  ALA D CB  1 
ATOM   5250  N N   . PRO D 1 23  ? -15.586 49.562  -86.521  1.00 27.44 ? 23  PRO D N   1 
ATOM   5251  C CA  . PRO D 1 23  ? -14.626 48.550  -87.000  1.00 28.81 ? 23  PRO D CA  1 
ATOM   5252  C C   . PRO D 1 23  ? -13.390 48.453  -86.084  1.00 28.79 ? 23  PRO D C   1 
ATOM   5253  O O   . PRO D 1 23  ? -13.142 49.370  -85.266  1.00 29.16 ? 23  PRO D O   1 
ATOM   5254  C CB  . PRO D 1 23  ? -14.247 49.071  -88.399  1.00 28.86 ? 23  PRO D CB  1 
ATOM   5255  C CG  . PRO D 1 23  ? -14.559 50.557  -88.368  1.00 28.36 ? 23  PRO D CG  1 
ATOM   5256  C CD  . PRO D 1 23  ? -15.291 50.890  -87.089  1.00 27.56 ? 23  PRO D CD  1 
ATOM   5257  N N   . ILE D 1 24  ? -12.646 47.347  -86.221  1.00 27.65 ? 24  ILE D N   1 
ATOM   5258  C CA  . ILE D 1 24  ? -11.518 47.007  -85.324  1.00 26.85 ? 24  ILE D CA  1 
ATOM   5259  C C   . ILE D 1 24  ? -10.543 48.152  -85.048  1.00 25.30 ? 24  ILE D C   1 
ATOM   5260  O O   . ILE D 1 24  ? -10.078 48.294  -83.914  1.00 24.44 ? 24  ILE D O   1 
ATOM   5261  C CB  . ILE D 1 24  ? -10.734 45.757  -85.815  1.00 27.11 ? 24  ILE D CB  1 
ATOM   5262  C CG1 . ILE D 1 24  ? -9.629  45.376  -84.816  1.00 27.16 ? 24  ILE D CG1 1 
ATOM   5263  C CG2 . ILE D 1 24  ? -10.144 45.969  -87.208  1.00 27.73 ? 24  ILE D CG2 1 
ATOM   5264  C CD1 . ILE D 1 24  ? -9.001  44.044  -85.099  1.00 26.95 ? 24  ILE D CD1 1 
ATOM   5265  N N   . VAL D 1 25  ? -10.268 48.952  -86.078  1.00 24.80 ? 25  VAL D N   1 
ATOM   5266  C CA  . VAL D 1 25  ? -9.417  50.155  -85.989  1.00 25.78 ? 25  VAL D CA  1 
ATOM   5267  C C   . VAL D 1 25  ? -10.151 51.358  -86.616  1.00 25.17 ? 25  VAL D C   1 
ATOM   5268  O O   . VAL D 1 25  ? -10.974 51.175  -87.514  1.00 24.47 ? 25  VAL D O   1 
ATOM   5269  C CB  . VAL D 1 25  ? -8.072  49.963  -86.734  1.00 26.66 ? 25  VAL D CB  1 
ATOM   5270  C CG1 . VAL D 1 25  ? -7.289  48.807  -86.134  1.00 27.41 ? 25  VAL D CG1 1 
ATOM   5271  C CG2 . VAL D 1 25  ? -8.275  49.706  -88.226  1.00 26.71 ? 25  VAL D CG2 1 
ATOM   5272  N N   . PRO D 1 26  ? -9.879  52.577  -86.164  1.00 24.59 ? 26  PRO D N   1 
ATOM   5273  C CA  . PRO D 1 26  ? -8.955  52.876  -85.068  1.00 24.46 ? 26  PRO D CA  1 
ATOM   5274  C C   . PRO D 1 26  ? -9.580  52.683  -83.693  1.00 23.08 ? 26  PRO D C   1 
ATOM   5275  O O   . PRO D 1 26  ? -10.794 52.717  -83.558  1.00 22.56 ? 26  PRO D O   1 
ATOM   5276  C CB  . PRO D 1 26  ? -8.642  54.363  -85.282  1.00 24.51 ? 26  PRO D CB  1 
ATOM   5277  C CG  . PRO D 1 26  ? -9.860  54.916  -85.948  1.00 24.48 ? 26  PRO D CG  1 
ATOM   5278  C CD  . PRO D 1 26  ? -10.551 53.786  -86.670  1.00 24.58 ? 26  PRO D CD  1 
ATOM   5279  N N   . THR D 1 27  ? -8.732  52.482  -82.691  1.00 22.42 ? 27  THR D N   1 
ATOM   5280  C CA  . THR D 1 27  ? -9.152  52.339  -81.291  1.00 20.73 ? 27  THR D CA  1 
ATOM   5281  C C   . THR D 1 27  ? -8.669  53.536  -80.477  1.00 19.22 ? 27  THR D C   1 
ATOM   5282  O O   . THR D 1 27  ? -7.961  54.404  -80.971  1.00 17.46 ? 27  THR D O   1 
ATOM   5283  C CB  . THR D 1 27  ? -8.615  51.017  -80.660  1.00 20.28 ? 27  THR D CB  1 
ATOM   5284  O OG1 . THR D 1 27  ? -9.043  50.899  -79.296  1.00 20.43 ? 27  THR D OG1 1 
ATOM   5285  C CG2 . THR D 1 27  ? -7.102  50.955  -80.696  1.00 20.32 ? 27  THR D CG2 1 
ATOM   5286  N N   . THR D 1 28  ? -9.100  53.581  -79.229  1.00 19.32 ? 28  THR D N   1 
ATOM   5287  C CA  . THR D 1 28  ? -8.586  54.528  -78.256  1.00 19.43 ? 28  THR D CA  1 
ATOM   5288  C C   . THR D 1 28  ? -8.234  53.719  -77.009  1.00 19.62 ? 28  THR D C   1 
ATOM   5289  O O   . THR D 1 28  ? -8.745  52.611  -76.804  1.00 18.56 ? 28  THR D O   1 
ATOM   5290  C CB  . THR D 1 28  ? -9.606  55.637  -77.898  1.00 19.27 ? 28  THR D CB  1 
ATOM   5291  O OG1 . THR D 1 28  ? -10.628 55.090  -77.066  1.00 19.39 ? 28  THR D OG1 1 
ATOM   5292  C CG2 . THR D 1 28  ? -10.263 56.244  -79.142  1.00 19.05 ? 28  THR D CG2 1 
ATOM   5293  N N   . ARG D 1 29  ? -7.363  54.284  -76.182  1.00 20.69 ? 29  ARG D N   1 
ATOM   5294  C CA  . ARG D 1 29  ? -6.832  53.589  -75.021  1.00 20.82 ? 29  ARG D CA  1 
ATOM   5295  C C   . ARG D 1 29  ? -7.868  53.499  -73.919  1.00 20.39 ? 29  ARG D C   1 
ATOM   5296  O O   . ARG D 1 29  ? -8.492  54.487  -73.579  1.00 19.83 ? 29  ARG D O   1 
ATOM   5297  C CB  . ARG D 1 29  ? -5.584  54.309  -74.485  1.00 21.57 ? 29  ARG D CB  1 
ATOM   5298  C CG  . ARG D 1 29  ? -4.483  53.340  -74.066  1.00 22.10 ? 29  ARG D CG  1 
ATOM   5299  C CD  . ARG D 1 29  ? -3.875  53.667  -72.731  1.00 21.86 ? 29  ARG D CD  1 
ATOM   5300  N NE  . ARG D 1 29  ? -2.569  54.338  -72.789  1.00 21.40 ? 29  ARG D NE  1 
ATOM   5301  C CZ  . ARG D 1 29  ? -1.427  53.847  -72.305  1.00 20.43 ? 29  ARG D CZ  1 
ATOM   5302  N NH1 . ARG D 1 29  ? -1.366  52.637  -71.753  1.00 20.70 ? 29  ARG D NH1 1 
ATOM   5303  N NH2 . ARG D 1 29  ? -0.328  54.578  -72.379  1.00 19.95 ? 29  ARG D NH2 1 
ATOM   5304  N N   . HIS D 1 30  ? -8.055  52.315  -73.356  1.00 20.98 ? 30  HIS D N   1 
ATOM   5305  C CA  . HIS D 1 30  ? -8.905  52.180  -72.173  1.00 22.26 ? 30  HIS D CA  1 
ATOM   5306  C C   . HIS D 1 30  ? -8.521  53.282  -71.173  1.00 23.97 ? 30  HIS D C   1 
ATOM   5307  O O   . HIS D 1 30  ? -7.333  53.545  -70.962  1.00 25.03 ? 30  HIS D O   1 
ATOM   5308  C CB  . HIS D 1 30  ? -8.702  50.827  -71.487  1.00 22.35 ? 30  HIS D CB  1 
ATOM   5309  C CG  . HIS D 1 30  ? -9.520  49.710  -72.061  1.00 22.76 ? 30  HIS D CG  1 
ATOM   5310  N ND1 . HIS D 1 30  ? -10.890 49.653  -71.937  1.00 23.02 ? 30  HIS D ND1 1 
ATOM   5311  C CD2 . HIS D 1 30  ? -9.156  48.577  -72.709  1.00 22.35 ? 30  HIS D CD2 1 
ATOM   5312  C CE1 . HIS D 1 30  ? -11.334 48.550  -72.506  1.00 22.43 ? 30  HIS D CE1 1 
ATOM   5313  N NE2 . HIS D 1 30  ? -10.301 47.878  -72.980  1.00 21.84 ? 30  HIS D NE2 1 
ATOM   5314  N N   . PRO D 1 31  ? -9.511  53.930  -70.550  1.00 24.75 ? 31  PRO D N   1 
ATOM   5315  C CA  . PRO D 1 31  ? -9.188  54.806  -69.425  1.00 24.23 ? 31  PRO D CA  1 
ATOM   5316  C C   . PRO D 1 31  ? -8.346  54.063  -68.394  1.00 24.70 ? 31  PRO D C   1 
ATOM   5317  O O   . PRO D 1 31  ? -8.544  52.860  -68.187  1.00 24.75 ? 31  PRO D O   1 
ATOM   5318  C CB  . PRO D 1 31  ? -10.553 55.147  -68.824  1.00 24.34 ? 31  PRO D CB  1 
ATOM   5319  C CG  . PRO D 1 31  ? -11.541 54.914  -69.915  1.00 25.00 ? 31  PRO D CG  1 
ATOM   5320  C CD  . PRO D 1 31  ? -10.958 53.870  -70.830  1.00 25.09 ? 31  PRO D CD  1 
ATOM   5321  N N   . HIS D 1 32  ? -7.421  54.771  -67.754  1.00 24.83 ? 32  HIS D N   1 
ATOM   5322  C CA  . HIS D 1 32  ? -6.515  54.164  -66.770  1.00 24.61 ? 32  HIS D CA  1 
ATOM   5323  C C   . HIS D 1 32  ? -7.269  53.301  -65.751  1.00 24.80 ? 32  HIS D C   1 
ATOM   5324  O O   . HIS D 1 32  ? -6.828  52.189  -65.425  1.00 23.98 ? 32  HIS D O   1 
ATOM   5325  C CB  . HIS D 1 32  ? -5.722  55.268  -66.057  1.00 24.73 ? 32  HIS D CB  1 
ATOM   5326  C CG  . HIS D 1 32  ? -4.692  54.762  -65.094  1.00 24.21 ? 32  HIS D CG  1 
ATOM   5327  N ND1 . HIS D 1 32  ? -4.971  54.521  -63.763  1.00 23.22 ? 32  HIS D ND1 1 
ATOM   5328  C CD2 . HIS D 1 32  ? -3.380  54.466  -65.267  1.00 23.59 ? 32  HIS D CD2 1 
ATOM   5329  C CE1 . HIS D 1 32  ? -3.877  54.094  -63.158  1.00 22.74 ? 32  HIS D CE1 1 
ATOM   5330  N NE2 . HIS D 1 32  ? -2.898  54.050  -64.045  1.00 22.72 ? 32  HIS D NE2 1 
ATOM   5331  N N   . ALA D 1 33  ? -8.415  53.800  -65.270  1.00 24.45 ? 33  ALA D N   1 
ATOM   5332  C CA  . ALA D 1 33  ? -9.198  53.066  -64.269  1.00 24.15 ? 33  ALA D CA  1 
ATOM   5333  C C   . ALA D 1 33  ? -9.632  51.661  -64.734  1.00 24.17 ? 33  ALA D C   1 
ATOM   5334  O O   . ALA D 1 33  ? -9.826  50.769  -63.903  1.00 24.52 ? 33  ALA D O   1 
ATOM   5335  C CB  . ALA D 1 33  ? -10.391 53.877  -63.833  1.00 23.71 ? 33  ALA D CB  1 
ATOM   5336  N N   . ASP D 1 34  ? -9.750  51.465  -66.047  1.00 23.05 ? 34  ASP D N   1 
ATOM   5337  C CA  . ASP D 1 34  ? -10.215 50.198  -66.627  1.00 22.12 ? 34  ASP D CA  1 
ATOM   5338  C C   . ASP D 1 34  ? -9.113  49.254  -67.133  1.00 22.03 ? 34  ASP D C   1 
ATOM   5339  O O   . ASP D 1 34  ? -9.429  48.203  -67.695  1.00 20.55 ? 34  ASP D O   1 
ATOM   5340  C CB  . ASP D 1 34  ? -11.140 50.490  -67.818  1.00 21.85 ? 34  ASP D CB  1 
ATOM   5341  C CG  . ASP D 1 34  ? -12.373 51.264  -67.437  1.00 21.12 ? 34  ASP D CG  1 
ATOM   5342  O OD1 . ASP D 1 34  ? -12.820 51.138  -66.274  1.00 21.34 ? 34  ASP D OD1 1 
ATOM   5343  O OD2 . ASP D 1 34  ? -12.893 51.975  -68.319  1.00 19.40 ? 34  ASP D OD2 1 
ATOM   5344  N N   . ARG D 1 35  ? -7.838  49.621  -66.967  1.00 22.07 ? 35  ARG D N   1 
ATOM   5345  C CA  . ARG D 1 35  ? -6.731  48.781  -67.474  1.00 21.81 ? 35  ARG D CA  1 
ATOM   5346  C C   . ARG D 1 35  ? -6.389  47.654  -66.510  1.00 22.26 ? 35  ARG D C   1 
ATOM   5347  O O   . ARG D 1 35  ? -6.365  47.857  -65.292  1.00 21.30 ? 35  ARG D O   1 
ATOM   5348  C CB  . ARG D 1 35  ? -5.485  49.622  -67.751  1.00 21.12 ? 35  ARG D CB  1 
ATOM   5349  C CG  . ARG D 1 35  ? -5.675  50.640  -68.856  1.00 20.84 ? 35  ARG D CG  1 
ATOM   5350  C CD  . ARG D 1 35  ? -4.423  51.459  -69.071  1.00 20.72 ? 35  ARG D CD  1 
ATOM   5351  N NE  . ARG D 1 35  ? -4.763  52.788  -69.587  1.00 20.94 ? 35  ARG D NE  1 
ATOM   5352  C CZ  . ARG D 1 35  ? -4.002  53.871  -69.478  1.00 20.90 ? 35  ARG D CZ  1 
ATOM   5353  N NH1 . ARG D 1 35  ? -2.828  53.827  -68.863  1.00 21.71 ? 35  ARG D NH1 1 
ATOM   5354  N NH2 . ARG D 1 35  ? -4.430  55.018  -69.980  1.00 21.14 ? 35  ARG D NH2 1 
ATOM   5355  N N   . TRP D 1 36  ? -6.100  46.467  -67.053  1.00 23.29 ? 36  TRP D N   1 
ATOM   5356  C CA  . TRP D 1 36  ? -5.871  45.287  -66.190  1.00 22.74 ? 36  TRP D CA  1 
ATOM   5357  C C   . TRP D 1 36  ? -4.710  45.524  -65.218  1.00 20.93 ? 36  TRP D C   1 
ATOM   5358  O O   . TRP D 1 36  ? -4.801  45.166  -64.055  1.00 20.28 ? 36  TRP D O   1 
ATOM   5359  C CB  . TRP D 1 36  ? -5.698  43.993  -67.022  1.00 23.06 ? 36  TRP D CB  1 
ATOM   5360  C CG  . TRP D 1 36  ? -4.302  43.655  -67.479  1.00 23.47 ? 36  TRP D CG  1 
ATOM   5361  C CD1 . TRP D 1 36  ? -3.739  43.961  -68.673  1.00 24.70 ? 36  TRP D CD1 1 
ATOM   5362  C CD2 . TRP D 1 36  ? -3.326  42.898  -66.756  1.00 23.60 ? 36  TRP D CD2 1 
ATOM   5363  N NE1 . TRP D 1 36  ? -2.461  43.461  -68.737  1.00 24.73 ? 36  TRP D NE1 1 
ATOM   5364  C CE2 . TRP D 1 36  ? -2.182  42.804  -67.571  1.00 23.81 ? 36  TRP D CE2 1 
ATOM   5365  C CE3 . TRP D 1 36  ? -3.306  42.301  -65.492  1.00 23.68 ? 36  TRP D CE3 1 
ATOM   5366  C CZ2 . TRP D 1 36  ? -1.034  42.129  -67.173  1.00 23.37 ? 36  TRP D CZ2 1 
ATOM   5367  C CZ3 . TRP D 1 36  ? -2.170  41.613  -65.100  1.00 23.74 ? 36  TRP D CZ3 1 
ATOM   5368  C CH2 . TRP D 1 36  ? -1.039  41.547  -65.935  1.00 23.29 ? 36  TRP D CH2 1 
ATOM   5369  N N   . THR D 1 37  ? -3.650  46.153  -65.708  1.00 20.53 ? 37  THR D N   1 
ATOM   5370  C CA  . THR D 1 37  ? -2.499  46.523  -64.887  1.00 20.20 ? 37  THR D CA  1 
ATOM   5371  C C   . THR D 1 37  ? -2.870  47.459  -63.741  1.00 19.49 ? 37  THR D C   1 
ATOM   5372  O O   . THR D 1 37  ? -2.305  47.358  -62.652  1.00 17.71 ? 37  THR D O   1 
ATOM   5373  C CB  . THR D 1 37  ? -1.387  47.197  -65.720  1.00 19.54 ? 37  THR D CB  1 
ATOM   5374  O OG1 . THR D 1 37  ? -1.968  48.193  -66.567  1.00 19.06 ? 37  THR D OG1 1 
ATOM   5375  C CG2 . THR D 1 37  ? -0.682  46.159  -66.562  1.00 19.52 ? 37  THR D CG2 1 
ATOM   5376  N N   . THR D 1 38  ? -3.806  48.370  -63.986  1.00 19.29 ? 38  THR D N   1 
ATOM   5377  C CA  . THR D 1 38  ? -4.250  49.278  -62.925  1.00 19.48 ? 38  THR D CA  1 
ATOM   5378  C C   . THR D 1 38  ? -4.977  48.530  -61.819  1.00 19.21 ? 38  THR D C   1 
ATOM   5379  O O   . THR D 1 38  ? -4.724  48.751  -60.635  1.00 19.34 ? 38  THR D O   1 
ATOM   5380  C CB  . THR D 1 38  ? -5.144  50.394  -63.484  1.00 19.93 ? 38  THR D CB  1 
ATOM   5381  O OG1 . THR D 1 38  ? -4.366  51.201  -64.377  1.00 20.75 ? 38  THR D OG1 1 
ATOM   5382  C CG2 . THR D 1 38  ? -5.695  51.265  -62.371  1.00 19.87 ? 38  THR D CG2 1 
ATOM   5383  N N   . VAL D 1 39  ? -5.865  47.627  -62.206  1.00 18.76 ? 39  VAL D N   1 
ATOM   5384  C CA  . VAL D 1 39  ? -6.591  46.823  -61.234  1.00 18.23 ? 39  VAL D CA  1 
ATOM   5385  C C   . VAL D 1 39  ? -5.620  45.914  -60.514  1.00 18.01 ? 39  VAL D C   1 
ATOM   5386  O O   . VAL D 1 39  ? -5.713  45.762  -59.318  1.00 19.11 ? 39  VAL D O   1 
ATOM   5387  C CB  . VAL D 1 39  ? -7.744  46.031  -61.882  1.00 18.09 ? 39  VAL D CB  1 
ATOM   5388  C CG1 . VAL D 1 39  ? -8.386  45.114  -60.866  1.00 18.55 ? 39  VAL D CG1 1 
ATOM   5389  C CG2 . VAL D 1 39  ? -8.780  46.987  -62.459  1.00 17.79 ? 39  VAL D CG2 1 
ATOM   5390  N N   . LEU D 1 40  ? -4.680  45.323  -61.233  1.00 18.03 ? 40  LEU D N   1 
ATOM   5391  C CA  . LEU D 1 40  ? -3.564  44.593  -60.603  1.00 18.35 ? 40  LEU D CA  1 
ATOM   5392  C C   . LEU D 1 40  ? -2.894  45.422  -59.506  1.00 19.31 ? 40  LEU D C   1 
ATOM   5393  O O   . LEU D 1 40  ? -2.618  44.917  -58.422  1.00 19.25 ? 40  LEU D O   1 
ATOM   5394  C CB  . LEU D 1 40  ? -2.522  44.183  -61.650  1.00 18.09 ? 40  LEU D CB  1 
ATOM   5395  C CG  . LEU D 1 40  ? -1.183  43.668  -61.125  1.00 17.85 ? 40  LEU D CG  1 
ATOM   5396  C CD1 . LEU D 1 40  ? -1.337  42.323  -60.408  1.00 17.57 ? 40  LEU D CD1 1 
ATOM   5397  C CD2 . LEU D 1 40  ? -0.166  43.573  -62.249  1.00 17.79 ? 40  LEU D CD2 1 
ATOM   5398  N N   . GLY D 1 41  ? -2.631  46.692  -59.797  1.00 20.13 ? 41  GLY D N   1 
ATOM   5399  C CA  . GLY D 1 41  ? -1.992  47.600  -58.847  1.00 20.59 ? 41  GLY D CA  1 
ATOM   5400  C C   . GLY D 1 41  ? -2.832  47.861  -57.621  1.00 21.20 ? 41  GLY D C   1 
ATOM   5401  O O   . GLY D 1 41  ? -2.315  47.850  -56.500  1.00 20.72 ? 41  GLY D O   1 
ATOM   5402  N N   . GLU D 1 42  ? -4.129  48.089  -57.839  1.00 22.30 ? 42  GLU D N   1 
ATOM   5403  C CA  . GLU D 1 42  ? -5.076  48.364  -56.757  1.00 23.58 ? 42  GLU D CA  1 
ATOM   5404  C C   . GLU D 1 42  ? -5.246  47.182  -55.828  1.00 23.24 ? 42  GLU D C   1 
ATOM   5405  O O   . GLU D 1 42  ? -5.265  47.344  -54.624  1.00 23.16 ? 42  GLU D O   1 
ATOM   5406  C CB  . GLU D 1 42  ? -6.435  48.761  -57.308  1.00 25.64 ? 42  GLU D CB  1 
ATOM   5407  C CG  . GLU D 1 42  ? -6.592  50.243  -57.576  1.00 27.94 ? 42  GLU D CG  1 
ATOM   5408  C CD  . GLU D 1 42  ? -7.659  50.547  -58.638  1.00 28.95 ? 42  GLU D CD  1 
ATOM   5409  O OE1 . GLU D 1 42  ? -7.632  51.687  -59.171  1.00 30.73 ? 42  GLU D OE1 1 
ATOM   5410  O OE2 . GLU D 1 42  ? -8.534  49.684  -58.941  1.00 26.96 ? 42  GLU D OE2 1 
ATOM   5411  N N   . ASN D 1 43  ? -5.352  45.991  -56.391  1.00 24.25 ? 43  ASN D N   1 
ATOM   5412  C CA  . ASN D 1 43  ? -5.485  44.769  -55.600  1.00 25.67 ? 43  ASN D CA  1 
ATOM   5413  C C   . ASN D 1 43  ? -4.226  44.354  -54.876  1.00 25.35 ? 43  ASN D C   1 
ATOM   5414  O O   . ASN D 1 43  ? -4.284  43.548  -53.970  1.00 25.08 ? 43  ASN D O   1 
ATOM   5415  C CB  . ASN D 1 43  ? -5.970  43.616  -56.463  1.00 26.95 ? 43  ASN D CB  1 
ATOM   5416  C CG  . ASN D 1 43  ? -7.482  43.659  -56.660  1.00 28.67 ? 43  ASN D CG  1 
ATOM   5417  O OD1 . ASN D 1 43  ? -8.230  42.990  -55.954  1.00 31.21 ? 43  ASN D OD1 1 
ATOM   5418  N ND2 . ASN D 1 43  ? -7.939  44.447  -57.628  1.00 28.13 ? 43  ASN D ND2 1 
ATOM   5419  N N   . LEU D 1 44  ? -3.080  44.873  -55.295  1.00 27.21 ? 44  LEU D N   1 
ATOM   5420  C CA  . LEU D 1 44  ? -1.796  44.584  -54.623  1.00 28.48 ? 44  LEU D CA  1 
ATOM   5421  C C   . LEU D 1 44  ? -1.592  45.454  -53.393  1.00 28.77 ? 44  LEU D C   1 
ATOM   5422  O O   . LEU D 1 44  ? -1.027  45.000  -52.404  1.00 29.82 ? 44  LEU D O   1 
ATOM   5423  C CB  . LEU D 1 44  ? -0.608  44.741  -55.595  1.00 28.07 ? 44  LEU D CB  1 
ATOM   5424  C CG  . LEU D 1 44  ? -0.324  43.551  -56.523  1.00 27.93 ? 44  LEU D CG  1 
ATOM   5425  C CD1 . LEU D 1 44  ? 0.726   43.878  -57.558  1.00 27.98 ? 44  LEU D CD1 1 
ATOM   5426  C CD2 . LEU D 1 44  ? 0.097   42.324  -55.737  1.00 28.11 ? 44  LEU D CD2 1 
ATOM   5427  N N   . GLY D 1 45  ? -2.026  46.709  -53.477  1.00 29.17 ? 45  GLY D N   1 
ATOM   5428  C CA  . GLY D 1 45  ? -1.913  47.657  -52.377  1.00 30.86 ? 45  GLY D CA  1 
ATOM   5429  C C   . GLY D 1 45  ? -0.652  48.501  -52.411  1.00 32.64 ? 45  GLY D C   1 
ATOM   5430  O O   . GLY D 1 45  ? 0.135   48.446  -53.355  1.00 32.62 ? 45  GLY D O   1 
ATOM   5431  N N   . ASP D 1 46  ? -0.468  49.285  -51.351  1.00 34.84 ? 46  ASP D N   1 
ATOM   5432  C CA  . ASP D 1 46  ? 0.690   50.188  -51.207  1.00 33.80 ? 46  ASP D CA  1 
ATOM   5433  C C   . ASP D 1 46  ? 2.018   49.459  -51.062  1.00 31.29 ? 46  ASP D C   1 
ATOM   5434  O O   . ASP D 1 46  ? 3.074   50.072  -51.225  1.00 31.20 ? 46  ASP D O   1 
ATOM   5435  C CB  . ASP D 1 46  ? 0.501   51.113  -50.004  1.00 34.11 ? 46  ASP D CB  1 
ATOM   5436  C CG  . ASP D 1 46  ? -0.683  52.064  -50.173  1.00 34.91 ? 46  ASP D CG  1 
ATOM   5437  O OD1 . ASP D 1 46  ? -1.065  52.365  -51.336  1.00 35.84 ? 46  ASP D OD1 1 
ATOM   5438  O OD2 . ASP D 1 46  ? -1.234  52.507  -49.137  1.00 34.49 ? 46  ASP D OD2 1 
ATOM   5439  N N   . GLY D 1 47  ? 1.971   48.167  -50.747  1.00 28.62 ? 47  GLY D N   1 
ATOM   5440  C CA  . GLY D 1 47  ? 3.185   47.351  -50.680  1.00 27.14 ? 47  GLY D CA  1 
ATOM   5441  C C   . GLY D 1 47  ? 3.906   47.222  -52.018  1.00 24.71 ? 47  GLY D C   1 
ATOM   5442  O O   . GLY D 1 47  ? 5.086   46.872  -52.047  1.00 23.24 ? 47  GLY D O   1 
ATOM   5443  N N   . TYR D 1 48  ? 3.184   47.504  -53.111  1.00 22.56 ? 48  TYR D N   1 
ATOM   5444  C CA  . TYR D 1 48  ? 3.681   47.327  -54.466  1.00 20.91 ? 48  TYR D CA  1 
ATOM   5445  C C   . TYR D 1 48  ? 3.565   48.580  -55.321  1.00 20.86 ? 48  TYR D C   1 
ATOM   5446  O O   . TYR D 1 48  ? 2.733   49.452  -55.074  1.00 20.32 ? 48  TYR D O   1 
ATOM   5447  C CB  . TYR D 1 48  ? 2.927   46.188  -55.150  1.00 20.61 ? 48  TYR D CB  1 
ATOM   5448  C CG  . TYR D 1 48  ? 3.044   44.863  -54.419  1.00 20.72 ? 48  TYR D CG  1 
ATOM   5449  C CD1 . TYR D 1 48  ? 2.280   44.608  -53.268  1.00 20.26 ? 48  TYR D CD1 1 
ATOM   5450  C CD2 . TYR D 1 48  ? 3.896   43.856  -54.876  1.00 20.06 ? 48  TYR D CD2 1 
ATOM   5451  C CE1 . TYR D 1 48  ? 2.384   43.417  -52.599  1.00 20.05 ? 48  TYR D CE1 1 
ATOM   5452  C CE2 . TYR D 1 48  ? 3.985   42.659  -54.205  1.00 20.20 ? 48  TYR D CE2 1 
ATOM   5453  C CZ  . TYR D 1 48  ? 3.247   42.457  -53.068  1.00 20.72 ? 48  TYR D CZ  1 
ATOM   5454  O OH  . TYR D 1 48  ? 3.392   41.281  -52.373  1.00 23.00 ? 48  TYR D OH  1 
ATOM   5455  N N   . GLU D 1 49  ? 4.429   48.634  -56.334  1.00 21.39 ? 49  GLU D N   1 
ATOM   5456  C CA  . GLU D 1 49  ? 4.545   49.764  -57.253  1.00 21.81 ? 49  GLU D CA  1 
ATOM   5457  C C   . GLU D 1 49  ? 4.778   49.175  -58.652  1.00 21.39 ? 49  GLU D C   1 
ATOM   5458  O O   . GLU D 1 49  ? 5.725   48.402  -58.853  1.00 23.72 ? 49  GLU D O   1 
ATOM   5459  C CB  . GLU D 1 49  ? 5.727   50.634  -56.813  1.00 23.34 ? 49  GLU D CB  1 
ATOM   5460  C CG  . GLU D 1 49  ? 6.094   51.810  -57.680  1.00 25.37 ? 49  GLU D CG  1 
ATOM   5461  C CD  . GLU D 1 49  ? 7.530   52.323  -57.466  1.00 27.47 ? 49  GLU D CD  1 
ATOM   5462  O OE1 . GLU D 1 49  ? 7.977   53.103  -58.315  1.00 33.15 ? 49  GLU D OE1 1 
ATOM   5463  O OE2 . GLU D 1 49  ? 8.232   51.987  -56.496  1.00 27.34 ? 49  GLU D OE2 1 
ATOM   5464  N N   . LEU D 1 50  ? 3.922   49.514  -59.622  1.00 19.35 ? 50  LEU D N   1 
ATOM   5465  C CA  . LEU D 1 50  ? 4.034   48.933  -60.963  1.00 18.10 ? 50  LEU D CA  1 
ATOM   5466  C C   . LEU D 1 50  ? 4.758   49.816  -61.975  1.00 17.03 ? 50  LEU D C   1 
ATOM   5467  O O   . LEU D 1 50  ? 4.670   51.036  -61.918  1.00 17.22 ? 50  LEU D O   1 
ATOM   5468  C CB  . LEU D 1 50  ? 2.655   48.644  -61.527  1.00 18.04 ? 50  LEU D CB  1 
ATOM   5469  C CG  . LEU D 1 50  ? 1.787   47.608  -60.831  1.00 18.32 ? 50  LEU D CG  1 
ATOM   5470  C CD1 . LEU D 1 50  ? 0.535   47.399  -61.668  1.00 18.39 ? 50  LEU D CD1 1 
ATOM   5471  C CD2 . LEU D 1 50  ? 2.518   46.290  -60.602  1.00 18.36 ? 50  LEU D CD2 1 
ATOM   5472  N N   . VAL D 1 51  ? 5.452   49.174  -62.914  1.00 16.17 ? 51  VAL D N   1 
ATOM   5473  C CA  . VAL D 1 51  ? 5.942   49.824  -64.126  1.00 15.82 ? 51  VAL D CA  1 
ATOM   5474  C C   . VAL D 1 51  ? 5.385   49.024  -65.295  1.00 15.51 ? 51  VAL D C   1 
ATOM   5475  O O   . VAL D 1 51  ? 5.524   47.806  -65.318  1.00 16.22 ? 51  VAL D O   1 
ATOM   5476  C CB  . VAL D 1 51  ? 7.476   49.827  -64.197  1.00 15.69 ? 51  VAL D CB  1 
ATOM   5477  C CG1 . VAL D 1 51  ? 7.963   50.709  -65.337  1.00 15.52 ? 51  VAL D CG1 1 
ATOM   5478  C CG2 . VAL D 1 51  ? 8.058   50.303  -62.898  1.00 15.96 ? 51  VAL D CG2 1 
ATOM   5479  N N   . VAL D 1 52  ? 4.766   49.697  -66.258  1.00 14.70 ? 52  VAL D N   1 
ATOM   5480  C CA  . VAL D 1 52  ? 4.039   49.007  -67.307  1.00 15.02 ? 52  VAL D CA  1 
ATOM   5481  C C   . VAL D 1 52  ? 4.531   49.364  -68.700  1.00 15.50 ? 52  VAL D C   1 
ATOM   5482  O O   . VAL D 1 52  ? 4.643   50.528  -69.043  1.00 15.84 ? 52  VAL D O   1 
ATOM   5483  C CB  . VAL D 1 52  ? 2.526   49.304  -67.212  1.00 15.01 ? 52  VAL D CB  1 
ATOM   5484  C CG1 . VAL D 1 52  ? 1.743   48.515  -68.269  1.00 14.90 ? 52  VAL D CG1 1 
ATOM   5485  C CG2 . VAL D 1 52  ? 2.012   48.986  -65.817  1.00 15.12 ? 52  VAL D CG2 1 
ATOM   5486  N N   . ASP D 1 53  ? 4.805   48.348  -69.509  1.00 16.50 ? 53  ASP D N   1 
ATOM   5487  C CA  . ASP D 1 53  ? 5.215   48.568  -70.891  1.00 17.40 ? 53  ASP D CA  1 
ATOM   5488  C C   . ASP D 1 53  ? 4.433   47.685  -71.840  1.00 17.71 ? 53  ASP D C   1 
ATOM   5489  O O   . ASP D 1 53  ? 4.831   46.563  -72.113  1.00 18.19 ? 53  ASP D O   1 
ATOM   5490  C CB  . ASP D 1 53  ? 6.714   48.338  -71.055  1.00 17.51 ? 53  ASP D CB  1 
ATOM   5491  C CG  . ASP D 1 53  ? 7.279   49.093  -72.221  1.00 18.10 ? 53  ASP D CG  1 
ATOM   5492  O OD1 . ASP D 1 53  ? 6.928   48.772  -73.380  1.00 18.17 ? 53  ASP D OD1 1 
ATOM   5493  O OD2 . ASP D 1 53  ? 8.083   50.026  -71.960  1.00 18.54 ? 53  ASP D OD2 1 
ATOM   5494  N N   . GLY D 1 54  ? 3.317   48.212  -72.330  1.00 17.96 ? 54  GLY D N   1 
ATOM   5495  C CA  . GLY D 1 54  ? 2.468   47.504  -73.287  1.00 18.12 ? 54  GLY D CA  1 
ATOM   5496  C C   . GLY D 1 54  ? 2.490   48.165  -74.646  1.00 18.42 ? 54  GLY D C   1 
ATOM   5497  O O   . GLY D 1 54  ? 2.137   49.337  -74.769  1.00 17.93 ? 54  GLY D O   1 
ATOM   5498  N N   . LEU D 1 55  ? 2.911   47.406  -75.661  1.00 19.15 ? 55  LEU D N   1 
ATOM   5499  C CA  . LEU D 1 55  ? 3.003   47.896  -77.037  1.00 19.60 ? 55  LEU D CA  1 
ATOM   5500  C C   . LEU D 1 55  ? 2.068   47.130  -77.953  1.00 19.44 ? 55  LEU D C   1 
ATOM   5501  O O   . LEU D 1 55  ? 2.236   45.932  -78.139  1.00 19.48 ? 55  LEU D O   1 
ATOM   5502  C CB  . LEU D 1 55  ? 4.449   47.757  -77.569  1.00 19.65 ? 55  LEU D CB  1 
ATOM   5503  C CG  . LEU D 1 55  ? 4.671   48.156  -79.044  1.00 19.40 ? 55  LEU D CG  1 
ATOM   5504  C CD1 . LEU D 1 55  ? 4.288   49.591  -79.305  1.00 18.81 ? 55  LEU D CD1 1 
ATOM   5505  C CD2 . LEU D 1 55  ? 6.110   47.908  -79.458  1.00 19.89 ? 55  LEU D CD2 1 
ATOM   5506  N N   . SER D 1 56  ? 1.100   47.831  -78.540  1.00 19.68 ? 56  SER D N   1 
ATOM   5507  C CA  . SER D 1 56  ? 0.223   47.234  -79.538  1.00 19.73 ? 56  SER D CA  1 
ATOM   5508  C C   . SER D 1 56  ? 1.067   46.565  -80.607  1.00 20.05 ? 56  SER D C   1 
ATOM   5509  O O   . SER D 1 56  ? 2.014   47.166  -81.112  1.00 19.97 ? 56  SER D O   1 
ATOM   5510  C CB  . SER D 1 56  ? -0.702  48.282  -80.171  1.00 19.61 ? 56  SER D CB  1 
ATOM   5511  O OG  . SER D 1 56  ? -1.408  49.031  -79.194  1.00 19.79 ? 56  SER D OG  1 
ATOM   5512  N N   . GLY D 1 57  ? 0.749   45.311  -80.908  1.00 21.16 ? 57  GLY D N   1 
ATOM   5513  C CA  . GLY D 1 57  ? 1.412   44.591  -82.003  1.00 23.02 ? 57  GLY D CA  1 
ATOM   5514  C C   . GLY D 1 57  ? 2.635   43.758  -81.637  1.00 23.69 ? 57  GLY D C   1 
ATOM   5515  O O   . GLY D 1 57  ? 3.152   43.015  -82.479  1.00 24.25 ? 57  GLY D O   1 
ATOM   5516  N N   . ARG D 1 58  ? 3.064   43.845  -80.379  1.00 23.97 ? 58  ARG D N   1 
ATOM   5517  C CA  . ARG D 1 58  ? 4.342   43.279  -79.943  1.00 24.30 ? 58  ARG D CA  1 
ATOM   5518  C C   . ARG D 1 58  ? 4.356   41.743  -79.855  1.00 23.69 ? 58  ARG D C   1 
ATOM   5519  O O   . ARG D 1 58  ? 3.399   41.106  -79.356  1.00 24.59 ? 58  ARG D O   1 
ATOM   5520  C CB  . ARG D 1 58  ? 4.740   43.888  -78.586  1.00 25.35 ? 58  ARG D CB  1 
ATOM   5521  C CG  . ARG D 1 58  ? 6.030   43.335  -77.955  1.00 25.51 ? 58  ARG D CG  1 
ATOM   5522  C CD  . ARG D 1 58  ? 6.305   43.997  -76.605  1.00 25.44 ? 58  ARG D CD  1 
ATOM   5523  N NE  . ARG D 1 58  ? 7.015   45.279  -76.717  1.00 25.11 ? 58  ARG D NE  1 
ATOM   5524  C CZ  . ARG D 1 58  ? 7.031   46.230  -75.784  1.00 24.90 ? 58  ARG D CZ  1 
ATOM   5525  N NH1 . ARG D 1 58  ? 6.341   46.106  -74.652  1.00 24.76 ? 58  ARG D NH1 1 
ATOM   5526  N NH2 . ARG D 1 58  ? 7.738   47.336  -75.987  1.00 25.28 ? 58  ARG D NH2 1 
ATOM   5527  N N   . THR D 1 59  ? 5.464   41.170  -80.316  1.00 22.42 ? 59  THR D N   1 
ATOM   5528  C CA  . THR D 1 59  ? 5.683   39.730  -80.288  1.00 21.98 ? 59  THR D CA  1 
ATOM   5529  C C   . THR D 1 59  ? 6.677   39.375  -79.195  1.00 21.03 ? 59  THR D C   1 
ATOM   5530  O O   . THR D 1 59  ? 7.301   40.262  -78.614  1.00 21.55 ? 59  THR D O   1 
ATOM   5531  C CB  . THR D 1 59  ? 6.269   39.239  -81.627  1.00 21.92 ? 59  THR D CB  1 
ATOM   5532  O OG1 . THR D 1 59  ? 7.654   39.628  -81.726  1.00 22.20 ? 59  THR D OG1 1 
ATOM   5533  C CG2 . THR D 1 59  ? 5.495   39.807  -82.791  1.00 21.28 ? 59  THR D CG2 1 
ATOM   5534  N N   . THR D 1 60  ? 6.837   38.082  -78.937  1.00 19.90 ? 60  THR D N   1 
ATOM   5535  C CA  . THR D 1 60  ? 7.863   37.608  -78.017  1.00 19.63 ? 60  THR D CA  1 
ATOM   5536  C C   . THR D 1 60  ? 9.251   38.005  -78.513  1.00 20.08 ? 60  THR D C   1 
ATOM   5537  O O   . THR D 1 60  ? 9.928   38.828  -77.885  1.00 21.19 ? 60  THR D O   1 
ATOM   5538  C CB  . THR D 1 60  ? 7.844   36.071  -77.840  1.00 19.03 ? 60  THR D CB  1 
ATOM   5539  O OG1 . THR D 1 60  ? 7.863   35.435  -79.113  1.00 18.79 ? 60  THR D OG1 1 
ATOM   5540  C CG2 . THR D 1 60  ? 6.622   35.626  -77.105  1.00 18.86 ? 60  THR D CG2 1 
ATOM   5541  N N   . ASN D 1 61  ? 9.663   37.432  -79.646  1.00 19.42 ? 61  ASN D N   1 
ATOM   5542  C CA  . ASN D 1 61  ? 11.061  37.529  -80.085  1.00 18.70 ? 61  ASN D CA  1 
ATOM   5543  C C   . ASN D 1 61  ? 11.281  37.460  -81.594  1.00 17.96 ? 61  ASN D C   1 
ATOM   5544  O O   . ASN D 1 61  ? 12.345  37.052  -82.041  1.00 17.08 ? 61  ASN D O   1 
ATOM   5545  C CB  . ASN D 1 61  ? 11.855  36.404  -79.431  1.00 18.61 ? 61  ASN D CB  1 
ATOM   5546  C CG  . ASN D 1 61  ? 11.648  35.067  -80.125  1.00 19.00 ? 61  ASN D CG  1 
ATOM   5547  O OD1 . ASN D 1 61  ? 10.611  34.810  -80.720  1.00 20.35 ? 61  ASN D OD1 1 
ATOM   5548  N ND2 . ASN D 1 61  ? 12.638  34.211  -80.056  1.00 18.97 ? 61  ASN D ND2 1 
ATOM   5549  N N   . ILE D 1 62  ? 10.282  37.867  -82.374  1.00 17.86 ? 62  ILE D N   1 
ATOM   5550  C CA  . ILE D 1 62  ? 10.339  37.735  -83.829  1.00 17.97 ? 62  ILE D CA  1 
ATOM   5551  C C   . ILE D 1 62  ? 9.993   39.059  -84.510  1.00 18.29 ? 62  ILE D C   1 
ATOM   5552  O O   . ILE D 1 62  ? 9.074   39.762  -84.079  1.00 18.18 ? 62  ILE D O   1 
ATOM   5553  C CB  . ILE D 1 62  ? 9.396   36.633  -84.308  1.00 17.82 ? 62  ILE D CB  1 
ATOM   5554  C CG1 . ILE D 1 62  ? 9.569   36.386  -85.810  1.00 18.12 ? 62  ILE D CG1 1 
ATOM   5555  C CG2 . ILE D 1 62  ? 7.952   36.983  -83.997  1.00 18.56 ? 62  ILE D CG2 1 
ATOM   5556  C CD1 . ILE D 1 62  ? 8.888   35.117  -86.290  1.00 18.05 ? 62  ILE D CD1 1 
ATOM   5557  N N   . ASP D 1 63  ? 10.735  39.387  -85.567  1.00 18.12 ? 63  ASP D N   1 
ATOM   5558  C CA  . ASP D 1 63  ? 10.490  40.614  -86.351  1.00 17.73 ? 63  ASP D CA  1 
ATOM   5559  C C   . ASP D 1 63  ? 9.186   40.530  -87.111  1.00 17.57 ? 63  ASP D C   1 
ATOM   5560  O O   . ASP D 1 63  ? 8.863   39.489  -87.713  1.00 18.07 ? 63  ASP D O   1 
ATOM   5561  C CB  . ASP D 1 63  ? 11.592  40.873  -87.374  1.00 17.50 ? 63  ASP D CB  1 
ATOM   5562  C CG  . ASP D 1 63  ? 12.936  41.113  -86.740  1.00 17.97 ? 63  ASP D CG  1 
ATOM   5563  O OD1 . ASP D 1 63  ? 12.973  41.721  -85.613  1.00 17.93 ? 63  ASP D OD1 1 
ATOM   5564  O OD2 . ASP D 1 63  ? 13.942  40.668  -87.371  1.00 17.94 ? 63  ASP D OD2 1 
ATOM   5565  N N   . ASP D 1 64  ? 8.423   41.618  -87.072  1.00 17.63 ? 64  ASP D N   1 
ATOM   5566  C CA  . ASP D 1 64  ? 7.239   41.740  -87.903  1.00 18.29 ? 64  ASP D CA  1 
ATOM   5567  C C   . ASP D 1 64  ? 7.672   42.491  -89.168  1.00 18.17 ? 64  ASP D C   1 
ATOM   5568  O O   . ASP D 1 64  ? 8.113   43.651  -89.090  1.00 18.51 ? 64  ASP D O   1 
ATOM   5569  C CB  . ASP D 1 64  ? 6.119   42.478  -87.161  1.00 18.58 ? 64  ASP D CB  1 
ATOM   5570  C CG  . ASP D 1 64  ? 4.778   42.364  -87.870  1.00 18.70 ? 64  ASP D CG  1 
ATOM   5571  O OD1 . ASP D 1 64  ? 4.713   42.676  -89.079  1.00 18.69 ? 64  ASP D OD1 1 
ATOM   5572  O OD2 . ASP D 1 64  ? 3.796   41.953  -87.223  1.00 18.80 ? 64  ASP D OD2 1 
ATOM   5573  N N   . PRO D 1 65  ? 7.566   41.836  -90.343  1.00 17.67 ? 65  PRO D N   1 
ATOM   5574  C CA  . PRO D 1 65  ? 8.038   42.535  -91.548  1.00 17.65 ? 65  PRO D CA  1 
ATOM   5575  C C   . PRO D 1 65  ? 7.263   43.829  -91.849  1.00 17.75 ? 65  PRO D C   1 
ATOM   5576  O O   . PRO D 1 65  ? 7.749   44.666  -92.613  1.00 17.54 ? 65  PRO D O   1 
ATOM   5577  C CB  . PRO D 1 65  ? 7.880   41.496  -92.663  1.00 17.28 ? 65  PRO D CB  1 
ATOM   5578  C CG  . PRO D 1 65  ? 6.910   40.504  -92.138  1.00 17.26 ? 65  PRO D CG  1 
ATOM   5579  C CD  . PRO D 1 65  ? 7.033   40.495  -90.639  1.00 17.31 ? 65  PRO D CD  1 
ATOM   5580  N N   . ASN D 1 66  ? 6.100   44.005  -91.223  1.00 17.89 ? 66  ASN D N   1 
ATOM   5581  C CA  . ASN D 1 66  ? 5.296   45.215  -91.410  1.00 18.52 ? 66  ASN D CA  1 
ATOM   5582  C C   . ASN D 1 66  ? 5.668   46.395  -90.523  1.00 17.68 ? 66  ASN D C   1 
ATOM   5583  O O   . ASN D 1 66  ? 5.225   47.504  -90.773  1.00 17.24 ? 66  ASN D O   1 
ATOM   5584  C CB  . ASN D 1 66  ? 3.819   44.894  -91.193  1.00 18.88 ? 66  ASN D CB  1 
ATOM   5585  C CG  . ASN D 1 66  ? 3.317   43.834  -92.146  1.00 19.43 ? 66  ASN D CG  1 
ATOM   5586  O OD1 . ASN D 1 66  ? 3.182   44.063  -93.342  1.00 20.74 ? 66  ASN D OD1 1 
ATOM   5587  N ND2 . ASN D 1 66  ? 3.060   42.656  -91.625  1.00 20.17 ? 66  ASN D ND2 1 
ATOM   5588  N N   . ASP D 1 67  ? 6.448   46.155  -89.474  1.00 17.39 ? 67  ASP D N   1 
ATOM   5589  C CA  . ASP D 1 67  ? 6.779   47.204  -88.498  1.00 16.88 ? 67  ASP D CA  1 
ATOM   5590  C C   . ASP D 1 67  ? 8.003   46.788  -87.673  1.00 16.22 ? 67  ASP D C   1 
ATOM   5591  O O   . ASP D 1 67  ? 7.947   45.822  -86.901  1.00 16.58 ? 67  ASP D O   1 
ATOM   5592  C CB  . ASP D 1 67  ? 5.587   47.478  -87.582  1.00 16.59 ? 67  ASP D CB  1 
ATOM   5593  C CG  . ASP D 1 67  ? 5.763   48.728  -86.739  1.00 16.09 ? 67  ASP D CG  1 
ATOM   5594  O OD1 . ASP D 1 67  ? 6.909   49.273  -86.641  1.00 15.66 ? 67  ASP D OD1 1 
ATOM   5595  O OD2 . ASP D 1 67  ? 4.730   49.163  -86.170  1.00 14.93 ? 67  ASP D OD2 1 
ATOM   5596  N N   . PRO D 1 68  ? 9.118   47.518  -87.832  1.00 15.29 ? 68  PRO D N   1 
ATOM   5597  C CA  . PRO D 1 68  ? 10.331  47.103  -87.155  1.00 15.05 ? 68  PRO D CA  1 
ATOM   5598  C C   . PRO D 1 68  ? 10.367  47.312  -85.635  1.00 15.00 ? 68  PRO D C   1 
ATOM   5599  O O   . PRO D 1 68  ? 11.336  46.919  -85.024  1.00 14.42 ? 68  PRO D O   1 
ATOM   5600  C CB  . PRO D 1 68  ? 11.420  47.941  -87.830  1.00 15.28 ? 68  PRO D CB  1 
ATOM   5601  C CG  . PRO D 1 68  ? 10.738  49.053  -88.553  1.00 15.07 ? 68  PRO D CG  1 
ATOM   5602  C CD  . PRO D 1 68  ? 9.313   48.688  -88.710  1.00 15.19 ? 68  PRO D CD  1 
ATOM   5603  N N   . LYS D 1 69  ? 9.337   47.889  -85.010  1.00 15.55 ? 69  LYS D N   1 
ATOM   5604  C CA  . LYS D 1 69  ? 9.399   48.142  -83.564  1.00 15.89 ? 69  LYS D CA  1 
ATOM   5605  C C   . LYS D 1 69  ? 8.645   47.140  -82.682  1.00 15.80 ? 69  LYS D C   1 
ATOM   5606  O O   . LYS D 1 69  ? 8.489   47.375  -81.481  1.00 15.21 ? 69  LYS D O   1 
ATOM   5607  C CB  . LYS D 1 69  ? 8.908   49.560  -83.245  1.00 16.30 ? 69  LYS D CB  1 
ATOM   5608  C CG  . LYS D 1 69  ? 7.405   49.795  -83.391  1.00 16.69 ? 69  LYS D CG  1 
ATOM   5609  C CD  . LYS D 1 69  ? 7.069   51.266  -83.172  1.00 16.73 ? 69  LYS D CD  1 
ATOM   5610  C CE  . LYS D 1 69  ? 5.578   51.530  -83.302  1.00 16.99 ? 69  LYS D CE  1 
ATOM   5611  N NZ  . LYS D 1 69  ? 5.154   51.643  -84.730  1.00 17.38 ? 69  LYS D NZ  1 
ATOM   5612  N N   . LEU D 1 70  ? 8.200   46.022  -83.259  1.00 15.71 ? 70  LEU D N   1 
ATOM   5613  C CA  . LEU D 1 70  ? 7.287   45.108  -82.581  1.00 15.91 ? 70  LEU D CA  1 
ATOM   5614  C C   . LEU D 1 70  ? 7.938   43.873  -81.955  1.00 16.24 ? 70  LEU D C   1 
ATOM   5615  O O   . LEU D 1 70  ? 7.235   43.007  -81.434  1.00 16.32 ? 70  LEU D O   1 
ATOM   5616  C CB  . LEU D 1 70  ? 6.199   44.656  -83.563  1.00 15.47 ? 70  LEU D CB  1 
ATOM   5617  C CG  . LEU D 1 70  ? 5.370   45.779  -84.170  1.00 15.03 ? 70  LEU D CG  1 
ATOM   5618  C CD1 . LEU D 1 70  ? 4.299   45.193  -85.066  1.00 15.01 ? 70  LEU D CD1 1 
ATOM   5619  C CD2 . LEU D 1 70  ? 4.765   46.649  -83.075  1.00 14.91 ? 70  LEU D CD2 1 
ATOM   5620  N N   . ASN D 1 71  ? 9.257   43.785  -81.991  1.00 16.27 ? 71  ASN D N   1 
ATOM   5621  C CA  . ASN D 1 71  ? 9.934   42.628  -81.451  1.00 16.56 ? 71  ASN D CA  1 
ATOM   5622  C C   . ASN D 1 71  ? 10.277  42.848  -79.978  1.00 15.57 ? 71  ASN D C   1 
ATOM   5623  O O   . ASN D 1 71  ? 11.194  43.610  -79.663  1.00 14.67 ? 71  ASN D O   1 
ATOM   5624  C CB  . ASN D 1 71  ? 11.198  42.350  -82.251  1.00 17.66 ? 71  ASN D CB  1 
ATOM   5625  C CG  . ASN D 1 71  ? 11.811  41.001  -81.918  1.00 18.37 ? 71  ASN D CG  1 
ATOM   5626  O OD1 . ASN D 1 71  ? 11.816  40.564  -80.768  1.00 18.39 ? 71  ASN D OD1 1 
ATOM   5627  N ND2 . ASN D 1 71  ? 12.347  40.337  -82.933  1.00 18.47 ? 71  ASN D ND2 1 
ATOM   5628  N N   . GLY D 1 72  ? 9.556   42.162  -79.086  1.00 14.68 ? 72  GLY D N   1 
ATOM   5629  C CA  . GLY D 1 72  ? 9.781   42.284  -77.648  1.00 13.74 ? 72  GLY D CA  1 
ATOM   5630  C C   . GLY D 1 72  ? 11.235  42.158  -77.223  1.00 13.03 ? 72  GLY D C   1 
ATOM   5631  O O   . GLY D 1 72  ? 11.720  42.930  -76.397  1.00 12.73 ? 72  GLY D O   1 
ATOM   5632  N N   . ALA D 1 73  ? 11.931  41.196  -77.810  1.00 12.62 ? 73  ALA D N   1 
ATOM   5633  C CA  . ALA D 1 73  ? 13.307  40.886  -77.449  1.00 12.50 ? 73  ALA D CA  1 
ATOM   5634  C C   . ALA D 1 73  ? 14.313  41.945  -77.912  1.00 12.65 ? 73  ALA D C   1 
ATOM   5635  O O   . ALA D 1 73  ? 15.404  42.055  -77.356  1.00 12.66 ? 73  ALA D O   1 
ATOM   5636  C CB  . ALA D 1 73  ? 13.679  39.517  -77.992  1.00 12.39 ? 73  ALA D CB  1 
ATOM   5637  N N   . ASP D 1 74  ? 13.963  42.727  -78.931  1.00 13.29 ? 74  ASP D N   1 
ATOM   5638  C CA  . ASP D 1 74  ? 14.761  43.909  -79.287  1.00 13.70 ? 74  ASP D CA  1 
ATOM   5639  C C   . ASP D 1 74  ? 14.771  44.938  -78.171  1.00 13.96 ? 74  ASP D C   1 
ATOM   5640  O O   . ASP D 1 74  ? 15.735  45.641  -78.007  1.00 14.53 ? 74  ASP D O   1 
ATOM   5641  C CB  . ASP D 1 74  ? 14.227  44.593  -80.558  1.00 13.95 ? 74  ASP D CB  1 
ATOM   5642  C CG  . ASP D 1 74  ? 14.586  43.863  -81.841  1.00 13.78 ? 74  ASP D CG  1 
ATOM   5643  O OD1 . ASP D 1 74  ? 15.521  43.044  -81.821  1.00 13.50 ? 74  ASP D OD1 1 
ATOM   5644  O OD2 . ASP D 1 74  ? 13.946  44.152  -82.878  1.00 14.15 ? 74  ASP D OD2 1 
ATOM   5645  N N   . TYR D 1 75  ? 13.685  45.016  -77.409  1.00 14.58 ? 75  TYR D N   1 
ATOM   5646  C CA  . TYR D 1 75  ? 13.429  46.098  -76.437  1.00 14.65 ? 75  TYR D CA  1 
ATOM   5647  C C   . TYR D 1 75  ? 13.747  45.712  -74.993  1.00 14.98 ? 75  TYR D C   1 
ATOM   5648  O O   . TYR D 1 75  ? 14.173  46.557  -74.195  1.00 15.75 ? 75  TYR D O   1 
ATOM   5649  C CB  . TYR D 1 75  ? 11.945  46.426  -76.564  1.00 14.94 ? 75  TYR D CB  1 
ATOM   5650  C CG  . TYR D 1 75  ? 11.362  47.644  -75.879  1.00 15.21 ? 75  TYR D CG  1 
ATOM   5651  C CD1 . TYR D 1 75  ? 11.410  48.897  -76.475  1.00 15.72 ? 75  TYR D CD1 1 
ATOM   5652  C CD2 . TYR D 1 75  ? 10.654  47.521  -74.684  1.00 15.51 ? 75  TYR D CD2 1 
ATOM   5653  C CE1 . TYR D 1 75  ? 10.834  50.006  -75.871  1.00 16.12 ? 75  TYR D CE1 1 
ATOM   5654  C CE2 . TYR D 1 75  ? 10.064  48.620  -74.068  1.00 15.48 ? 75  TYR D CE2 1 
ATOM   5655  C CZ  . TYR D 1 75  ? 10.154  49.857  -74.665  1.00 15.89 ? 75  TYR D CZ  1 
ATOM   5656  O OH  . TYR D 1 75  ? 9.575   50.960  -74.081  1.00 15.89 ? 75  TYR D OH  1 
ATOM   5657  N N   . LEU D 1 76  ? 13.540  44.440  -74.652  1.00 14.71 ? 76  LEU D N   1 
ATOM   5658  C CA  . LEU D 1 76  ? 13.494  44.034  -73.253  1.00 14.51 ? 76  LEU D CA  1 
ATOM   5659  C C   . LEU D 1 76  ? 14.798  44.253  -72.478  1.00 14.48 ? 76  LEU D C   1 
ATOM   5660  O O   . LEU D 1 76  ? 14.748  44.715  -71.341  1.00 14.12 ? 76  LEU D O   1 
ATOM   5661  C CB  . LEU D 1 76  ? 13.002  42.598  -73.117  1.00 14.61 ? 76  LEU D CB  1 
ATOM   5662  C CG  . LEU D 1 76  ? 12.777  42.114  -71.681  1.00 15.08 ? 76  LEU D CG  1 
ATOM   5663  C CD1 . LEU D 1 76  ? 11.797  43.011  -70.939  1.00 15.03 ? 76  LEU D CD1 1 
ATOM   5664  C CD2 . LEU D 1 76  ? 12.289  40.666  -71.662  1.00 15.36 ? 76  LEU D CD2 1 
ATOM   5665  N N   . PRO D 1 77  ? 15.966  43.933  -73.079  1.00 14.67 ? 77  PRO D N   1 
ATOM   5666  C CA  . PRO D 1 77  ? 17.205  44.161  -72.333  1.00 14.64 ? 77  PRO D CA  1 
ATOM   5667  C C   . PRO D 1 77  ? 17.338  45.603  -71.838  1.00 14.76 ? 77  PRO D C   1 
ATOM   5668  O O   . PRO D 1 77  ? 17.674  45.832  -70.671  1.00 14.56 ? 77  PRO D O   1 
ATOM   5669  C CB  . PRO D 1 77  ? 18.288  43.804  -73.346  1.00 14.25 ? 77  PRO D CB  1 
ATOM   5670  C CG  . PRO D 1 77  ? 17.659  42.768  -74.191  1.00 14.16 ? 77  PRO D CG  1 
ATOM   5671  C CD  . PRO D 1 77  ? 16.236  43.216  -74.341  1.00 14.42 ? 77  PRO D CD  1 
ATOM   5672  N N   . ALA D 1 78  ? 17.059  46.557  -72.714  1.00 15.06 ? 78  ALA D N   1 
ATOM   5673  C CA  . ALA D 1 78  ? 17.122  47.973  -72.348  1.00 15.52 ? 78  ALA D CA  1 
ATOM   5674  C C   . ALA D 1 78  ? 16.095  48.313  -71.275  1.00 15.44 ? 78  ALA D C   1 
ATOM   5675  O O   . ALA D 1 78  ? 16.407  48.998  -70.308  1.00 15.00 ? 78  ALA D O   1 
ATOM   5676  C CB  . ALA D 1 78  ? 16.911  48.855  -73.576  1.00 15.78 ? 78  ALA D CB  1 
ATOM   5677  N N   . ALA D 1 79  ? 14.871  47.825  -71.459  1.00 15.47 ? 79  ALA D N   1 
ATOM   5678  C CA  . ALA D 1 79  ? 13.792  48.106  -70.528  1.00 15.29 ? 79  ALA D CA  1 
ATOM   5679  C C   . ALA D 1 79  ? 14.139  47.627  -69.114  1.00 15.01 ? 79  ALA D C   1 
ATOM   5680  O O   . ALA D 1 79  ? 13.947  48.353  -68.136  1.00 15.00 ? 79  ALA D O   1 
ATOM   5681  C CB  . ALA D 1 79  ? 12.504  47.451  -71.013  1.00 15.10 ? 79  ALA D CB  1 
ATOM   5682  N N   . LEU D 1 80  ? 14.673  46.415  -69.023  1.00 14.87 ? 80  LEU D N   1 
ATOM   5683  C CA  . LEU D 1 80  ? 15.027  45.826  -67.740  1.00 15.47 ? 80  LEU D CA  1 
ATOM   5684  C C   . LEU D 1 80  ? 16.042  46.664  -66.970  1.00 16.50 ? 80  LEU D C   1 
ATOM   5685  O O   . LEU D 1 80  ? 15.900  46.881  -65.757  1.00 17.53 ? 80  LEU D O   1 
ATOM   5686  C CB  . LEU D 1 80  ? 15.574  44.415  -67.940  1.00 14.91 ? 80  LEU D CB  1 
ATOM   5687  C CG  . LEU D 1 80  ? 14.563  43.357  -68.381  1.00 14.53 ? 80  LEU D CG  1 
ATOM   5688  C CD1 . LEU D 1 80  ? 15.282  42.139  -68.922  1.00 14.43 ? 80  LEU D CD1 1 
ATOM   5689  C CD2 . LEU D 1 80  ? 13.629  42.971  -67.240  1.00 14.72 ? 80  LEU D CD2 1 
ATOM   5690  N N   . ALA D 1 81  ? 17.059  47.131  -67.689  1.00 17.57 ? 81  ALA D N   1 
ATOM   5691  C CA  . ALA D 1 81  ? 18.152  47.926  -67.119  1.00 17.97 ? 81  ALA D CA  1 
ATOM   5692  C C   . ALA D 1 81  ? 17.695  49.317  -66.729  1.00 18.87 ? 81  ALA D C   1 
ATOM   5693  O O   . ALA D 1 81  ? 18.254  49.934  -65.813  1.00 19.83 ? 81  ALA D O   1 
ATOM   5694  C CB  . ALA D 1 81  ? 19.282  48.029  -68.120  1.00 17.69 ? 81  ALA D CB  1 
ATOM   5695  N N   . ALA D 1 82  ? 16.693  49.806  -67.457  1.00 19.73 ? 82  ALA D N   1 
ATOM   5696  C CA  . ALA D 1 82  ? 16.135  51.131  -67.251  1.00 19.93 ? 82  ALA D CA  1 
ATOM   5697  C C   . ALA D 1 82  ? 15.218  51.189  -66.034  1.00 20.65 ? 82  ALA D C   1 
ATOM   5698  O O   . ALA D 1 82  ? 14.970  52.280  -65.498  1.00 21.78 ? 82  ALA D O   1 
ATOM   5699  C CB  . ALA D 1 82  ? 15.372  51.571  -68.493  1.00 19.51 ? 82  ALA D CB  1 
ATOM   5700  N N   . HIS D 1 83  ? 14.708  50.030  -65.610  1.00 20.29 ? 83  HIS D N   1 
ATOM   5701  C CA  . HIS D 1 83  ? 13.808  49.960  -64.460  1.00 20.27 ? 83  HIS D CA  1 
ATOM   5702  C C   . HIS D 1 83  ? 14.360  49.167  -63.281  1.00 20.83 ? 83  HIS D C   1 
ATOM   5703  O O   . HIS D 1 83  ? 13.669  48.994  -62.272  1.00 20.79 ? 83  HIS D O   1 
ATOM   5704  C CB  . HIS D 1 83  ? 12.458  49.410  -64.905  1.00 19.54 ? 83  HIS D CB  1 
ATOM   5705  C CG  . HIS D 1 83  ? 11.838  50.212  -66.001  1.00 18.75 ? 83  HIS D CG  1 
ATOM   5706  N ND1 . HIS D 1 83  ? 11.687  51.579  -65.912  1.00 17.81 ? 83  HIS D ND1 1 
ATOM   5707  C CD2 . HIS D 1 83  ? 11.347  49.848  -67.209  1.00 18.89 ? 83  HIS D CD2 1 
ATOM   5708  C CE1 . HIS D 1 83  ? 11.124  52.028  -67.017  1.00 17.99 ? 83  HIS D CE1 1 
ATOM   5709  N NE2 . HIS D 1 83  ? 10.923  51.002  -67.824  1.00 18.87 ? 83  HIS D NE2 1 
ATOM   5710  N N   . GLU D 1 84  ? 15.614  48.722  -63.391  1.00 21.88 ? 84  GLU D N   1 
ATOM   5711  C CA  . GLU D 1 84  ? 16.307  48.101  -62.261  1.00 22.29 ? 84  GLU D CA  1 
ATOM   5712  C C   . GLU D 1 84  ? 16.319  49.082  -61.060  1.00 21.21 ? 84  GLU D C   1 
ATOM   5713  O O   . GLU D 1 84  ? 16.571  50.277  -61.244  1.00 21.01 ? 84  GLU D O   1 
ATOM   5714  C CB  . GLU D 1 84  ? 17.740  47.731  -62.670  1.00 23.66 ? 84  GLU D CB  1 
ATOM   5715  C CG  . GLU D 1 84  ? 18.476  46.885  -61.647  1.00 24.17 ? 84  GLU D CG  1 
ATOM   5716  C CD  . GLU D 1 84  ? 19.915  46.548  -62.054  1.00 23.98 ? 84  GLU D CD  1 
ATOM   5717  O OE1 . GLU D 1 84  ? 20.277  45.380  -61.822  1.00 24.26 ? 84  GLU D OE1 1 
ATOM   5718  O OE2 . GLU D 1 84  ? 20.672  47.425  -62.562  1.00 23.11 ? 84  GLU D OE2 1 
ATOM   5719  N N   . PRO D 1 85  ? 16.071  48.598  -59.838  1.00 19.63 ? 85  PRO D N   1 
ATOM   5720  C CA  . PRO D 1 85  ? 15.867  47.170  -59.516  1.00 18.54 ? 85  PRO D CA  1 
ATOM   5721  C C   . PRO D 1 85  ? 14.407  46.767  -59.468  1.00 17.41 ? 85  PRO D C   1 
ATOM   5722  O O   . PRO D 1 85  ? 13.567  47.551  -59.027  1.00 16.40 ? 85  PRO D O   1 
ATOM   5723  C CB  . PRO D 1 85  ? 16.455  47.060  -58.118  1.00 18.51 ? 85  PRO D CB  1 
ATOM   5724  C CG  . PRO D 1 85  ? 16.168  48.405  -57.509  1.00 19.01 ? 85  PRO D CG  1 
ATOM   5725  C CD  . PRO D 1 85  ? 16.205  49.427  -58.622  1.00 19.13 ? 85  PRO D CD  1 
ATOM   5726  N N   . LEU D 1 86  ? 14.121  45.545  -59.904  1.00 16.87 ? 86  LEU D N   1 
ATOM   5727  C CA  . LEU D 1 86  ? 12.767  45.008  -59.866  1.00 16.54 ? 86  LEU D CA  1 
ATOM   5728  C C   . LEU D 1 86  ? 12.681  43.788  -58.958  1.00 15.23 ? 86  LEU D C   1 
ATOM   5729  O O   . LEU D 1 86  ? 13.652  43.098  -58.739  1.00 13.94 ? 86  LEU D O   1 
ATOM   5730  C CB  . LEU D 1 86  ? 12.298  44.649  -61.277  1.00 17.07 ? 86  LEU D CB  1 
ATOM   5731  C CG  . LEU D 1 86  ? 12.275  45.803  -62.293  1.00 17.59 ? 86  LEU D CG  1 
ATOM   5732  C CD1 . LEU D 1 86  ? 12.242  45.253  -63.719  1.00 18.00 ? 86  LEU D CD1 1 
ATOM   5733  C CD2 . LEU D 1 86  ? 11.114  46.751  -62.043  1.00 17.40 ? 86  LEU D CD2 1 
ATOM   5734  N N   . ASP D 1 87  ? 11.489  43.554  -58.436  1.00 15.19 ? 87  ASP D N   1 
ATOM   5735  C CA  . ASP D 1 87  ? 11.190  42.382  -57.628  1.00 15.07 ? 87  ASP D CA  1 
ATOM   5736  C C   . ASP D 1 87  ? 10.475  41.294  -58.416  1.00 15.16 ? 87  ASP D C   1 
ATOM   5737  O O   . ASP D 1 87  ? 10.537  40.130  -58.023  1.00 14.48 ? 87  ASP D O   1 
ATOM   5738  C CB  . ASP D 1 87  ? 10.363  42.790  -56.425  1.00 14.76 ? 87  ASP D CB  1 
ATOM   5739  C CG  . ASP D 1 87  ? 11.138  43.668  -55.487  1.00 14.56 ? 87  ASP D CG  1 
ATOM   5740  O OD1 . ASP D 1 87  ? 11.915  43.083  -54.697  1.00 13.69 ? 87  ASP D OD1 1 
ATOM   5741  O OD2 . ASP D 1 87  ? 10.973  44.902  -55.495  1.00 14.67 ? 87  ASP D OD2 1 
ATOM   5742  N N   . LEU D 1 88  ? 9.825   41.684  -59.522  1.00 15.62 ? 88  LEU D N   1 
ATOM   5743  C CA  . LEU D 1 88  ? 9.204   40.726  -60.447  1.00 15.71 ? 88  LEU D CA  1 
ATOM   5744  C C   . LEU D 1 88  ? 9.037   41.275  -61.870  1.00 15.68 ? 88  LEU D C   1 
ATOM   5745  O O   . LEU D 1 88  ? 8.811   42.472  -62.068  1.00 15.61 ? 88  LEU D O   1 
ATOM   5746  C CB  . LEU D 1 88  ? 7.842   40.317  -59.915  1.00 16.00 ? 88  LEU D CB  1 
ATOM   5747  C CG  . LEU D 1 88  ? 7.036   39.267  -60.652  1.00 16.64 ? 88  LEU D CG  1 
ATOM   5748  C CD1 . LEU D 1 88  ? 7.713   37.921  -60.525  1.00 17.05 ? 88  LEU D CD1 1 
ATOM   5749  C CD2 . LEU D 1 88  ? 5.616   39.226  -60.122  1.00 16.93 ? 88  LEU D CD2 1 
ATOM   5750  N N   . VAL D 1 89  ? 9.156   40.391  -62.852  1.00 15.99 ? 89  VAL D N   1 
ATOM   5751  C CA  . VAL D 1 89  ? 8.848   40.729  -64.232  1.00 16.53 ? 89  VAL D CA  1 
ATOM   5752  C C   . VAL D 1 89  ? 7.695   39.839  -64.702  1.00 16.81 ? 89  VAL D C   1 
ATOM   5753  O O   . VAL D 1 89  ? 7.776   38.614  -64.632  1.00 16.90 ? 89  VAL D O   1 
ATOM   5754  C CB  . VAL D 1 89  ? 10.057  40.516  -65.156  1.00 16.68 ? 89  VAL D CB  1 
ATOM   5755  C CG1 . VAL D 1 89  ? 9.673   40.730  -66.619  1.00 16.40 ? 89  VAL D CG1 1 
ATOM   5756  C CG2 . VAL D 1 89  ? 11.182  41.463  -64.773  1.00 16.88 ? 89  VAL D CG2 1 
ATOM   5757  N N   . ILE D 1 90  ? 6.618   40.466  -65.158  1.00 16.63 ? 90  ILE D N   1 
ATOM   5758  C CA  . ILE D 1 90  ? 5.474   39.766  -65.685  1.00 16.28 ? 90  ILE D CA  1 
ATOM   5759  C C   . ILE D 1 90  ? 5.483   39.930  -67.188  1.00 16.32 ? 90  ILE D C   1 
ATOM   5760  O O   . ILE D 1 90  ? 5.613   41.038  -67.690  1.00 15.28 ? 90  ILE D O   1 
ATOM   5761  C CB  . ILE D 1 90  ? 4.162   40.347  -65.126  1.00 16.64 ? 90  ILE D CB  1 
ATOM   5762  C CG1 . ILE D 1 90  ? 4.042   40.045  -63.629  1.00 16.64 ? 90  ILE D CG1 1 
ATOM   5763  C CG2 . ILE D 1 90  ? 2.965   39.789  -65.892  1.00 16.84 ? 90  ILE D CG2 1 
ATOM   5764  C CD1 . ILE D 1 90  ? 2.824   40.669  -62.979  1.00 16.59 ? 90  ILE D CD1 1 
ATOM   5765  N N   . ILE D 1 91  ? 5.336   38.818  -67.900  1.00 17.30 ? 91  ILE D N   1 
ATOM   5766  C CA  . ILE D 1 91  ? 5.310   38.828  -69.355  1.00 17.53 ? 91  ILE D CA  1 
ATOM   5767  C C   . ILE D 1 91  ? 3.976   38.254  -69.780  1.00 17.78 ? 91  ILE D C   1 
ATOM   5768  O O   . ILE D 1 91  ? 3.662   37.121  -69.458  1.00 18.16 ? 91  ILE D O   1 
ATOM   5769  C CB  . ILE D 1 91  ? 6.450   37.974  -69.963  1.00 17.58 ? 91  ILE D CB  1 
ATOM   5770  C CG1 . ILE D 1 91  ? 7.810   38.515  -69.536  1.00 17.10 ? 91  ILE D CG1 1 
ATOM   5771  C CG2 . ILE D 1 91  ? 6.379   37.942  -71.493  1.00 17.80 ? 91  ILE D CG2 1 
ATOM   5772  C CD1 . ILE D 1 91  ? 8.944   37.548  -69.803  1.00 17.00 ? 91  ILE D CD1 1 
ATOM   5773  N N   . LEU D 1 92  ? 3.193   39.063  -70.478  1.00 18.51 ? 92  LEU D N   1 
ATOM   5774  C CA  . LEU D 1 92  ? 1.945   38.644  -71.090  1.00 19.14 ? 92  LEU D CA  1 
ATOM   5775  C C   . LEU D 1 92  ? 2.016   38.989  -72.571  1.00 19.49 ? 92  LEU D C   1 
ATOM   5776  O O   . LEU D 1 92  ? 1.603   40.085  -73.000  1.00 19.83 ? 92  LEU D O   1 
ATOM   5777  C CB  . LEU D 1 92  ? 0.754   39.347  -70.424  1.00 19.87 ? 92  LEU D CB  1 
ATOM   5778  C CG  . LEU D 1 92  ? -0.626  39.143  -71.080  1.00 20.08 ? 92  LEU D CG  1 
ATOM   5779  C CD1 . LEU D 1 92  ? -0.911  37.650  -71.276  1.00 19.70 ? 92  LEU D CD1 1 
ATOM   5780  C CD2 . LEU D 1 92  ? -1.695  39.803  -70.239  1.00 20.47 ? 92  LEU D CD2 1 
ATOM   5781  N N   . LEU D 1 93  ? 2.569   38.032  -73.320  1.00 19.62 ? 93  LEU D N   1 
ATOM   5782  C CA  . LEU D 1 93  ? 2.777   38.116  -74.757  1.00 19.70 ? 93  LEU D CA  1 
ATOM   5783  C C   . LEU D 1 93  ? 2.476   36.777  -75.388  1.00 20.15 ? 93  LEU D C   1 
ATOM   5784  O O   . LEU D 1 93  ? 2.449   35.751  -74.704  1.00 20.22 ? 93  LEU D O   1 
ATOM   5785  C CB  . LEU D 1 93  ? 4.233   38.451  -75.068  1.00 18.97 ? 93  LEU D CB  1 
ATOM   5786  C CG  . LEU D 1 93  ? 4.706   39.877  -74.805  1.00 18.51 ? 93  LEU D CG  1 
ATOM   5787  C CD1 . LEU D 1 93  ? 6.220   39.936  -74.973  1.00 18.73 ? 93  LEU D CD1 1 
ATOM   5788  C CD2 . LEU D 1 93  ? 4.009   40.884  -75.710  1.00 17.98 ? 93  LEU D CD2 1 
ATOM   5789  N N   . GLY D 1 94  ? 2.290   36.796  -76.706  1.00 21.07 ? 94  GLY D N   1 
ATOM   5790  C CA  . GLY D 1 94  ? 2.024   35.578  -77.481  1.00 21.70 ? 94  GLY D CA  1 
ATOM   5791  C C   . GLY D 1 94  ? 0.820   35.692  -78.408  1.00 22.26 ? 94  GLY D C   1 
ATOM   5792  O O   . GLY D 1 94  ? 0.667   34.905  -79.343  1.00 21.09 ? 94  GLY D O   1 
ATOM   5793  N N   . THR D 1 95  ? -0.045  36.666  -78.148  1.00 23.25 ? 95  THR D N   1 
ATOM   5794  C CA  . THR D 1 95  ? -1.252  36.824  -78.946  1.00 23.59 ? 95  THR D CA  1 
ATOM   5795  C C   . THR D 1 95  ? -0.895  37.216  -80.394  1.00 23.18 ? 95  THR D C   1 
ATOM   5796  O O   . THR D 1 95  ? -1.381  36.614  -81.348  1.00 22.86 ? 95  THR D O   1 
ATOM   5797  C CB  . THR D 1 95  ? -2.235  37.813  -78.277  1.00 23.34 ? 95  THR D CB  1 
ATOM   5798  O OG1 . THR D 1 95  ? -2.434  37.419  -76.912  1.00 24.37 ? 95  THR D OG1 1 
ATOM   5799  C CG2 . THR D 1 95  ? -3.560  37.791  -78.972  1.00 22.81 ? 95  THR D CG2 1 
ATOM   5800  N N   . ASN D 1 96  ? -0.008  38.186  -80.559  1.00 22.47 ? 96  ASN D N   1 
ATOM   5801  C CA  . ASN D 1 96  ? 0.435   38.582  -81.902  1.00 21.87 ? 96  ASN D CA  1 
ATOM   5802  C C   . ASN D 1 96  ? 1.282   37.525  -82.607  1.00 21.92 ? 96  ASN D C   1 
ATOM   5803  O O   . ASN D 1 96  ? 1.322   37.474  -83.833  1.00 20.82 ? 96  ASN D O   1 
ATOM   5804  C CB  . ASN D 1 96  ? 1.219   39.889  -81.847  1.00 21.92 ? 96  ASN D CB  1 
ATOM   5805  C CG  . ASN D 1 96  ? 0.373   41.054  -81.416  1.00 21.42 ? 96  ASN D CG  1 
ATOM   5806  O OD1 . ASN D 1 96  ? -0.571  41.448  -82.109  1.00 21.11 ? 96  ASN D OD1 1 
ATOM   5807  N ND2 . ASN D 1 96  ? 0.712   41.622  -80.268  1.00 21.57 ? 96  ASN D ND2 1 
ATOM   5808  N N   . ASP D 1 97  ? 1.953   36.677  -81.832  1.00 22.73 ? 97  ASP D N   1 
ATOM   5809  C CA  . ASP D 1 97  ? 2.779   35.608  -82.404  1.00 22.78 ? 97  ASP D CA  1 
ATOM   5810  C C   . ASP D 1 97  ? 1.968   34.576  -83.202  1.00 22.75 ? 97  ASP D C   1 
ATOM   5811  O O   . ASP D 1 97  ? 2.544   33.836  -84.016  1.00 23.61 ? 97  ASP D O   1 
ATOM   5812  C CB  . ASP D 1 97  ? 3.577   34.890  -81.310  1.00 22.23 ? 97  ASP D CB  1 
ATOM   5813  C CG  . ASP D 1 97  ? 4.587   35.803  -80.610  1.00 21.58 ? 97  ASP D CG  1 
ATOM   5814  O OD1 . ASP D 1 97  ? 4.150   36.743  -79.907  1.00 20.43 ? 97  ASP D OD1 1 
ATOM   5815  O OD2 . ASP D 1 97  ? 5.810   35.559  -80.741  1.00 22.06 ? 97  ASP D OD2 1 
ATOM   5816  N N   . THR D 1 98  ? 0.653   34.534  -82.978  1.00 22.53 ? 98  THR D N   1 
ATOM   5817  C CA  . THR D 1 98  ? -0.225  33.610  -83.697  1.00 22.54 ? 98  THR D CA  1 
ATOM   5818  C C   . THR D 1 98  ? -0.607  34.111  -85.090  1.00 21.38 ? 98  THR D C   1 
ATOM   5819  O O   . THR D 1 98  ? -1.199  33.359  -85.874  1.00 21.82 ? 98  THR D O   1 
ATOM   5820  C CB  . THR D 1 98  ? -1.525  33.354  -82.907  1.00 23.54 ? 98  THR D CB  1 
ATOM   5821  O OG1 . THR D 1 98  ? -2.314  34.561  -82.875  1.00 24.09 ? 98  THR D OG1 1 
ATOM   5822  C CG2 . THR D 1 98  ? -1.211  32.885  -81.484  1.00 23.94 ? 98  THR D CG2 1 
ATOM   5823  N N   . LYS D 1 99  ? -0.278  35.369  -85.390  1.00 20.71 ? 99  LYS D N   1 
ATOM   5824  C CA  . LYS D 1 99  ? -0.558  35.946  -86.706  1.00 20.26 ? 99  LYS D CA  1 
ATOM   5825  C C   . LYS D 1 99  ? 0.007   35.061  -87.798  1.00 19.81 ? 99  LYS D C   1 
ATOM   5826  O O   . LYS D 1 99  ? 1.163   34.646  -87.755  1.00 19.39 ? 99  LYS D O   1 
ATOM   5827  C CB  . LYS D 1 99  ? 0.015   37.370  -86.842  1.00 20.68 ? 99  LYS D CB  1 
ATOM   5828  C CG  . LYS D 1 99  ? -0.778  38.432  -86.097  1.00 20.68 ? 99  LYS D CG  1 
ATOM   5829  C CD  . LYS D 1 99  ? -0.117  39.808  -86.113  1.00 20.16 ? 99  LYS D CD  1 
ATOM   5830  C CE  . LYS D 1 99  ? -1.073  40.849  -85.551  1.00 20.16 ? 99  LYS D CE  1 
ATOM   5831  N NZ  . LYS D 1 99  ? -0.417  42.093  -85.070  1.00 20.16 ? 99  LYS D NZ  1 
ATOM   5832  N N   . THR D 1 100 ? -0.844  34.794  -88.774  1.00 20.39 ? 100 THR D N   1 
ATOM   5833  C CA  . THR D 1 100 ? -0.577  33.869  -89.872  1.00 20.43 ? 100 THR D CA  1 
ATOM   5834  C C   . THR D 1 100 ? 0.784   34.104  -90.534  1.00 19.70 ? 100 THR D C   1 
ATOM   5835  O O   . THR D 1 100 ? 1.560   33.173  -90.680  1.00 19.53 ? 100 THR D O   1 
ATOM   5836  C CB  . THR D 1 100 ? -1.698  33.983  -90.940  1.00 20.66 ? 100 THR D CB  1 
ATOM   5837  O OG1 . THR D 1 100 ? -2.889  33.314  -90.504  1.00 19.59 ? 100 THR D OG1 1 
ATOM   5838  C CG2 . THR D 1 100 ? -1.229  33.407  -92.292  1.00 20.86 ? 100 THR D CG2 1 
ATOM   5839  N N   . TYR D 1 101 ? 1.059   35.345  -90.926  1.00 19.60 ? 101 TYR D N   1 
ATOM   5840  C CA  . TYR D 1 101 ? 2.264   35.653  -91.690  1.00 19.71 ? 101 TYR D CA  1 
ATOM   5841  C C   . TYR D 1 101 ? 3.589   35.450  -90.931  1.00 20.47 ? 101 TYR D C   1 
ATOM   5842  O O   . TYR D 1 101 ? 4.629   35.380  -91.551  1.00 20.83 ? 101 TYR D O   1 
ATOM   5843  C CB  . TYR D 1 101 ? 2.204   37.068  -92.297  1.00 18.79 ? 101 TYR D CB  1 
ATOM   5844  C CG  . TYR D 1 101 ? 2.063   38.212  -91.325  1.00 18.31 ? 101 TYR D CG  1 
ATOM   5845  C CD1 . TYR D 1 101 ? 3.157   38.701  -90.619  1.00 18.48 ? 101 TYR D CD1 1 
ATOM   5846  C CD2 . TYR D 1 101 ? 0.842   38.835  -91.129  1.00 18.68 ? 101 TYR D CD2 1 
ATOM   5847  C CE1 . TYR D 1 101 ? 3.035   39.769  -89.736  1.00 18.27 ? 101 TYR D CE1 1 
ATOM   5848  C CE2 . TYR D 1 101 ? 0.702   39.905  -90.244  1.00 18.30 ? 101 TYR D CE2 1 
ATOM   5849  C CZ  . TYR D 1 101 ? 1.801   40.366  -89.555  1.00 17.73 ? 101 TYR D CZ  1 
ATOM   5850  O OH  . TYR D 1 101 ? 1.653   41.409  -88.691  1.00 16.89 ? 101 TYR D OH  1 
ATOM   5851  N N   . LEU D 1 102 ? 3.558   35.363  -89.605  1.00 21.07 ? 102 LEU D N   1 
ATOM   5852  C CA  . LEU D 1 102 ? 4.769   35.063  -88.836  1.00 21.69 ? 102 LEU D CA  1 
ATOM   5853  C C   . LEU D 1 102 ? 5.088   33.560  -88.832  1.00 20.72 ? 102 LEU D C   1 
ATOM   5854  O O   . LEU D 1 102 ? 6.187   33.151  -88.464  1.00 20.39 ? 102 LEU D O   1 
ATOM   5855  C CB  . LEU D 1 102 ? 4.636   35.559  -87.402  1.00 22.98 ? 102 LEU D CB  1 
ATOM   5856  C CG  . LEU D 1 102 ? 4.363   37.057  -87.267  1.00 24.40 ? 102 LEU D CG  1 
ATOM   5857  C CD1 . LEU D 1 102 ? 4.034   37.403  -85.812  1.00 24.91 ? 102 LEU D CD1 1 
ATOM   5858  C CD2 . LEU D 1 102 ? 5.552   37.878  -87.774  1.00 24.87 ? 102 LEU D CD2 1 
ATOM   5859  N N   . ASN D 1 103 ? 4.112   32.754  -89.207  1.00 20.38 ? 103 ASN D N   1 
ATOM   5860  C CA  . ASN D 1 103 ? 4.315   31.340  -89.456  1.00 20.70 ? 103 ASN D CA  1 
ATOM   5861  C C   . ASN D 1 103 ? 4.946   30.566  -88.272  1.00 20.09 ? 103 ASN D C   1 
ATOM   5862  O O   . ASN D 1 103 ? 5.848   29.739  -88.458  1.00 20.38 ? 103 ASN D O   1 
ATOM   5863  C CB  . ASN D 1 103 ? 5.139   31.174  -90.735  1.00 20.69 ? 103 ASN D CB  1 
ATOM   5864  C CG  . ASN D 1 103 ? 5.207   29.706  -91.184  1.00 21.02 ? 103 ASN D CG  1 
ATOM   5865  O OD1 . ASN D 1 103 ? 4.185   29.015  -91.348  1.00 21.56 ? 103 ASN D OD1 1 
ATOM   5866  N ND2 . ASN D 1 103 ? 6.415   29.215  -91.349  1.00 20.94 ? 103 ASN D ND2 1 
ATOM   5867  N N   . ARG D 1 104 ? 4.448   30.822  -87.065  1.00 19.16 ? 104 ARG D N   1 
ATOM   5868  C CA  . ARG D 1 104 ? 5.014   30.199  -85.865  1.00 18.40 ? 104 ARG D CA  1 
ATOM   5869  C C   . ARG D 1 104 ? 4.175   29.047  -85.346  1.00 18.40 ? 104 ARG D C   1 
ATOM   5870  O O   . ARG D 1 104 ? 2.939   29.081  -85.396  1.00 18.63 ? 104 ARG D O   1 
ATOM   5871  C CB  . ARG D 1 104 ? 5.146   31.222  -84.737  1.00 17.81 ? 104 ARG D CB  1 
ATOM   5872  C CG  . ARG D 1 104 ? 5.613   32.601  -85.160  1.00 17.43 ? 104 ARG D CG  1 
ATOM   5873  C CD  . ARG D 1 104 ? 6.247   33.312  -83.980  1.00 17.01 ? 104 ARG D CD  1 
ATOM   5874  N NE  . ARG D 1 104 ? 7.651   32.936  -83.801  1.00 17.14 ? 104 ARG D NE  1 
ATOM   5875  C CZ  . ARG D 1 104 ? 8.430   33.356  -82.804  1.00 16.83 ? 104 ARG D CZ  1 
ATOM   5876  N NH1 . ARG D 1 104 ? 7.959   34.167  -81.858  1.00 17.13 ? 104 ARG D NH1 1 
ATOM   5877  N NH2 . ARG D 1 104 ? 9.690   32.960  -82.756  1.00 16.26 ? 104 ARG D NH2 1 
ATOM   5878  N N   . THR D 1 105 ? 4.859   28.036  -84.824  1.00 18.45 ? 105 THR D N   1 
ATOM   5879  C CA  . THR D 1 105 ? 4.205   26.953  -84.117  1.00 18.78 ? 105 THR D CA  1 
ATOM   5880  C C   . THR D 1 105 ? 4.120   27.375  -82.663  1.00 19.00 ? 105 THR D C   1 
ATOM   5881  O O   . THR D 1 105 ? 4.844   28.278  -82.245  1.00 19.06 ? 105 THR D O   1 
ATOM   5882  C CB  . THR D 1 105 ? 5.030   25.664  -84.194  1.00 19.38 ? 105 THR D CB  1 
ATOM   5883  O OG1 . THR D 1 105 ? 6.220   25.798  -83.407  1.00 19.54 ? 105 THR D OG1 1 
ATOM   5884  C CG2 . THR D 1 105 ? 5.447   25.367  -85.645  1.00 19.19 ? 105 THR D CG2 1 
ATOM   5885  N N   . PRO D 1 106 ? 3.246   26.729  -81.877  1.00 19.16 ? 106 PRO D N   1 
ATOM   5886  C CA  . PRO D 1 106 ? 3.164   27.028  -80.441  1.00 18.62 ? 106 PRO D CA  1 
ATOM   5887  C C   . PRO D 1 106 ? 4.474   26.801  -79.704  1.00 18.54 ? 106 PRO D C   1 
ATOM   5888  O O   . PRO D 1 106 ? 4.821   27.606  -78.840  1.00 19.28 ? 106 PRO D O   1 
ATOM   5889  C CB  . PRO D 1 106 ? 2.109   26.044  -79.937  1.00 18.82 ? 106 PRO D CB  1 
ATOM   5890  C CG  . PRO D 1 106 ? 1.231   25.816  -81.118  1.00 19.05 ? 106 PRO D CG  1 
ATOM   5891  C CD  . PRO D 1 106 ? 2.163   25.830  -82.311  1.00 19.45 ? 106 PRO D CD  1 
ATOM   5892  N N   . PHE D 1 107 ? 5.195   25.726  -80.042  1.00 18.09 ? 107 PHE D N   1 
ATOM   5893  C CA  . PHE D 1 107 ? 6.493   25.451  -79.428  1.00 17.42 ? 107 PHE D CA  1 
ATOM   5894  C C   . PHE D 1 107 ? 7.471   26.574  -79.733  1.00 17.01 ? 107 PHE D C   1 
ATOM   5895  O O   . PHE D 1 107 ? 8.223   27.013  -78.858  1.00 17.44 ? 107 PHE D O   1 
ATOM   5896  C CB  . PHE D 1 107 ? 7.058   24.103  -79.899  1.00 17.61 ? 107 PHE D CB  1 
ATOM   5897  C CG  . PHE D 1 107 ? 8.406   23.783  -79.321  1.00 17.87 ? 107 PHE D CG  1 
ATOM   5898  C CD1 . PHE D 1 107 ? 8.574   23.587  -77.959  1.00 18.07 ? 107 PHE D CD1 1 
ATOM   5899  C CD2 . PHE D 1 107 ? 9.510   23.679  -80.140  1.00 18.35 ? 107 PHE D CD2 1 
ATOM   5900  C CE1 . PHE D 1 107 ? 9.830   23.297  -77.426  1.00 18.44 ? 107 PHE D CE1 1 
ATOM   5901  C CE2 . PHE D 1 107 ? 10.774  23.384  -79.614  1.00 18.49 ? 107 PHE D CE2 1 
ATOM   5902  C CZ  . PHE D 1 107 ? 10.935  23.196  -78.255  1.00 18.23 ? 107 PHE D CZ  1 
ATOM   5903  N N   . GLU D 1 108 ? 7.450   27.051  -80.971  1.00 16.58 ? 108 GLU D N   1 
ATOM   5904  C CA  . GLU D 1 108 ? 8.295   28.175  -81.352  1.00 16.67 ? 108 GLU D CA  1 
ATOM   5905  C C   . GLU D 1 108 ? 7.990   29.406  -80.501  1.00 16.33 ? 108 GLU D C   1 
ATOM   5906  O O   . GLU D 1 108 ? 8.894   30.133  -80.114  1.00 15.38 ? 108 GLU D O   1 
ATOM   5907  C CB  . GLU D 1 108 ? 8.092   28.520  -82.823  1.00 16.77 ? 108 GLU D CB  1 
ATOM   5908  C CG  . GLU D 1 108 ? 9.043   29.585  -83.310  1.00 16.99 ? 108 GLU D CG  1 
ATOM   5909  C CD  . GLU D 1 108 ? 8.928   29.807  -84.794  1.00 17.66 ? 108 GLU D CD  1 
ATOM   5910  O OE1 . GLU D 1 108 ? 8.728   30.962  -85.221  1.00 18.59 ? 108 GLU D OE1 1 
ATOM   5911  O OE2 . GLU D 1 108 ? 9.029   28.821  -85.542  1.00 18.40 ? 108 GLU D OE2 1 
ATOM   5912  N N   . ILE D 1 109 ? 6.709   29.636  -80.233  1.00 16.32 ? 109 ILE D N   1 
ATOM   5913  C CA  . ILE D 1 109 ? 6.285   30.808  -79.484  1.00 16.23 ? 109 ILE D CA  1 
ATOM   5914  C C   . ILE D 1 109 ? 6.718   30.654  -78.030  1.00 15.71 ? 109 ILE D C   1 
ATOM   5915  O O   . ILE D 1 109 ? 7.156   31.613  -77.405  1.00 15.29 ? 109 ILE D O   1 
ATOM   5916  C CB  . ILE D 1 109 ? 4.756   31.039  -79.599  1.00 16.79 ? 109 ILE D CB  1 
ATOM   5917  C CG1 . ILE D 1 109 ? 4.352   31.244  -81.065  1.00 16.69 ? 109 ILE D CG1 1 
ATOM   5918  C CG2 . ILE D 1 109 ? 4.340   32.254  -78.771  1.00 17.13 ? 109 ILE D CG2 1 
ATOM   5919  C CD1 . ILE D 1 109 ? 2.868   31.134  -81.350  1.00 16.69 ? 109 ILE D CD1 1 
ATOM   5920  N N   . GLY D 1 110 ? 6.618   29.443  -77.503  1.00 15.53 ? 110 GLY D N   1 
ATOM   5921  C CA  . GLY D 1 110 ? 7.190   29.140  -76.196  1.00 15.92 ? 110 GLY D CA  1 
ATOM   5922  C C   . GLY D 1 110 ? 8.676   29.479  -76.106  1.00 16.11 ? 110 GLY D C   1 
ATOM   5923  O O   . GLY D 1 110 ? 9.125   30.110  -75.155  1.00 16.26 ? 110 GLY D O   1 
ATOM   5924  N N   . LEU D 1 111 ? 9.442   29.048  -77.100  1.00 16.14 ? 111 LEU D N   1 
ATOM   5925  C CA  . LEU D 1 111 ? 10.871  29.364  -77.163  1.00 15.85 ? 111 LEU D CA  1 
ATOM   5926  C C   . LEU D 1 111 ? 11.109  30.881  -77.165  1.00 15.50 ? 111 LEU D C   1 
ATOM   5927  O O   . LEU D 1 111 ? 12.072  31.370  -76.575  1.00 14.82 ? 111 LEU D O   1 
ATOM   5928  C CB  . LEU D 1 111 ? 11.495  28.737  -78.403  1.00 16.09 ? 111 LEU D CB  1 
ATOM   5929  C CG  . LEU D 1 111 ? 11.606  27.208  -78.367  1.00 16.37 ? 111 LEU D CG  1 
ATOM   5930  C CD1 . LEU D 1 111 ? 12.159  26.720  -79.695  1.00 16.71 ? 111 LEU D CD1 1 
ATOM   5931  C CD2 . LEU D 1 111 ? 12.480  26.723  -77.214  1.00 16.66 ? 111 LEU D CD2 1 
ATOM   5932  N N   . GLY D 1 112 ? 10.220  31.613  -77.825  1.00 15.25 ? 112 GLY D N   1 
ATOM   5933  C CA  . GLY D 1 112 ? 10.276  33.068  -77.867  1.00 15.14 ? 112 GLY D CA  1 
ATOM   5934  C C   . GLY D 1 112 ? 10.094  33.658  -76.492  1.00 15.20 ? 112 GLY D C   1 
ATOM   5935  O O   . GLY D 1 112 ? 10.859  34.527  -76.075  1.00 15.31 ? 112 GLY D O   1 
ATOM   5936  N N   . ALA D 1 113 ? 9.083   33.177  -75.777  1.00 14.89 ? 113 ALA D N   1 
ATOM   5937  C CA  . ALA D 1 113 ? 8.865   33.583  -74.393  1.00 14.23 ? 113 ALA D CA  1 
ATOM   5938  C C   . ALA D 1 113 ? 10.062  33.191  -73.565  1.00 13.82 ? 113 ALA D C   1 
ATOM   5939  O O   . ALA D 1 113 ? 10.494  33.959  -72.718  1.00 14.37 ? 113 ALA D O   1 
ATOM   5940  C CB  . ALA D 1 113 ? 7.603   32.946  -73.830  1.00 14.39 ? 113 ALA D CB  1 
ATOM   5941  N N   . GLY D 1 114 ? 10.610  32.004  -73.819  1.00 13.38 ? 114 GLY D N   1 
ATOM   5942  C CA  . GLY D 1 114 ? 11.854  31.551  -73.178  1.00 12.91 ? 114 GLY D CA  1 
ATOM   5943  C C   . GLY D 1 114 ? 13.037  32.486  -73.402  1.00 12.67 ? 114 GLY D C   1 
ATOM   5944  O O   . GLY D 1 114 ? 13.806  32.764  -72.487  1.00 12.68 ? 114 GLY D O   1 
ATOM   5945  N N   . ALA D 1 115 ? 13.186  32.975  -74.622  1.00 12.55 ? 115 ALA D N   1 
ATOM   5946  C CA  . ALA D 1 115 ? 14.215  33.967  -74.941  1.00 12.46 ? 115 ALA D CA  1 
ATOM   5947  C C   . ALA D 1 115 ? 14.097  35.189  -74.054  1.00 12.12 ? 115 ALA D C   1 
ATOM   5948  O O   . ALA D 1 115 ? 15.104  35.753  -73.625  1.00 12.63 ? 115 ALA D O   1 
ATOM   5949  C CB  . ALA D 1 115 ? 14.132  34.385  -76.404  1.00 12.45 ? 115 ALA D CB  1 
ATOM   5950  N N   . LEU D 1 116 ? 12.865  35.604  -73.783  1.00 11.69 ? 116 LEU D N   1 
ATOM   5951  C CA  . LEU D 1 116 ? 12.630  36.762  -72.925  1.00 11.53 ? 116 LEU D CA  1 
ATOM   5952  C C   . LEU D 1 116 ? 12.970  36.449  -71.469  1.00 11.54 ? 116 LEU D C   1 
ATOM   5953  O O   . LEU D 1 116 ? 13.610  37.252  -70.798  1.00 11.37 ? 116 LEU D O   1 
ATOM   5954  C CB  . LEU D 1 116 ? 11.205  37.282  -73.080  1.00 11.17 ? 116 LEU D CB  1 
ATOM   5955  C CG  . LEU D 1 116 ? 10.821  37.789  -74.478  1.00 10.91 ? 116 LEU D CG  1 
ATOM   5956  C CD1 . LEU D 1 116 ? 9.374   38.262  -74.497  1.00 11.05 ? 116 LEU D CD1 1 
ATOM   5957  C CD2 . LEU D 1 116 ? 11.719  38.907  -74.939  1.00 10.71 ? 116 LEU D CD2 1 
ATOM   5958  N N   . ILE D 1 117 ? 12.577  35.275  -70.998  1.00 12.05 ? 117 ILE D N   1 
ATOM   5959  C CA  . ILE D 1 117 ? 12.922  34.838  -69.644  1.00 12.64 ? 117 ILE D CA  1 
ATOM   5960  C C   . ILE D 1 117 ? 14.438  34.859  -69.464  1.00 13.34 ? 117 ILE D C   1 
ATOM   5961  O O   . ILE D 1 117 ? 14.944  35.378  -68.454  1.00 13.63 ? 117 ILE D O   1 
ATOM   5962  C CB  . ILE D 1 117 ? 12.379  33.427  -69.318  1.00 12.42 ? 117 ILE D CB  1 
ATOM   5963  C CG1 . ILE D 1 117 ? 10.851  33.461  -69.222  1.00 12.68 ? 117 ILE D CG1 1 
ATOM   5964  C CG2 . ILE D 1 117 ? 12.941  32.939  -67.991  1.00 12.34 ? 117 ILE D CG2 1 
ATOM   5965  C CD1 . ILE D 1 117 ? 10.215  32.085  -69.295  1.00 12.89 ? 117 ILE D CD1 1 
ATOM   5966  N N   . ASN D 1 118 ? 15.149  34.308  -70.444  1.00 13.76 ? 118 ASN D N   1 
ATOM   5967  C CA  . ASN D 1 118 ? 16.597  34.307  -70.431  1.00 14.34 ? 118 ASN D CA  1 
ATOM   5968  C C   . ASN D 1 118 ? 17.184  35.720  -70.345  1.00 15.13 ? 118 ASN D C   1 
ATOM   5969  O O   . ASN D 1 118 ? 18.158  35.955  -69.611  1.00 16.29 ? 118 ASN D O   1 
ATOM   5970  C CB  . ASN D 1 118 ? 17.151  33.599  -71.677  1.00 14.46 ? 118 ASN D CB  1 
ATOM   5971  C CG  . ASN D 1 118 ? 18.648  33.367  -71.587  1.00 14.77 ? 118 ASN D CG  1 
ATOM   5972  O OD1 . ASN D 1 118 ? 19.472  34.123  -72.047  1.00 14.99 ? 118 ASN D OD1 1 
ATOM   5973  N ND2 . ASN D 1 118 ? 19.000  32.291  -70.975  1.00 15.62 ? 118 ASN D ND2 1 
ATOM   5974  N N   . MET D 1 119 ? 16.623  36.669  -71.099  1.00 15.20 ? 119 MET D N   1 
ATOM   5975  C CA  . MET D 1 119 ? 17.090  38.050  -71.018  1.00 15.46 ? 119 MET D CA  1 
ATOM   5976  C C   . MET D 1 119 ? 16.945  38.619  -69.605  1.00 14.91 ? 119 MET D C   1 
ATOM   5977  O O   . MET D 1 119 ? 17.825  39.347  -69.127  1.00 15.20 ? 119 MET D O   1 
ATOM   5978  C CB  . MET D 1 119 ? 16.353  38.933  -72.031  1.00 15.93 ? 119 MET D CB  1 
ATOM   5979  C CG  . MET D 1 119 ? 16.847  38.721  -73.448  1.00 16.18 ? 119 MET D CG  1 
ATOM   5980  S SD  . MET D 1 119 ? 15.780  39.437  -74.686  1.00 16.06 ? 119 MET D SD  1 
ATOM   5981  C CE  . MET D 1 119 ? 16.908  39.540  -76.060  1.00 15.71 ? 119 MET D CE  1 
ATOM   5982  N N   . VAL D 1 120 ? 15.843  38.278  -68.946  1.00 14.51 ? 120 VAL D N   1 
ATOM   5983  C CA  . VAL D 1 120 ? 15.612  38.712  -67.572  1.00 14.80 ? 120 VAL D CA  1 
ATOM   5984  C C   . VAL D 1 120 ? 16.618  38.057  -66.621  1.00 14.81 ? 120 VAL D C   1 
ATOM   5985  O O   . VAL D 1 120 ? 17.098  38.692  -65.701  1.00 13.68 ? 120 VAL D O   1 
ATOM   5986  C CB  . VAL D 1 120 ? 14.171  38.388  -67.091  1.00 14.68 ? 120 VAL D CB  1 
ATOM   5987  C CG1 . VAL D 1 120 ? 13.976  38.842  -65.656  1.00 14.38 ? 120 VAL D CG1 1 
ATOM   5988  C CG2 . VAL D 1 120 ? 13.129  39.053  -67.984  1.00 14.49 ? 120 VAL D CG2 1 
ATOM   5989  N N   . GLN D 1 121 ? 16.919  36.780  -66.839  1.00 15.57 ? 121 GLN D N   1 
ATOM   5990  C CA  . GLN D 1 121 ? 17.837  36.046  -65.962  1.00 15.98 ? 121 GLN D CA  1 
ATOM   5991  C C   . GLN D 1 121 ? 19.278  36.535  -66.080  1.00 17.38 ? 121 GLN D C   1 
ATOM   5992  O O   . GLN D 1 121 ? 20.016  36.523  -65.079  1.00 18.56 ? 121 GLN D O   1 
ATOM   5993  C CB  . GLN D 1 121 ? 17.768  34.544  -66.237  1.00 15.16 ? 121 GLN D CB  1 
ATOM   5994  C CG  . GLN D 1 121 ? 16.474  33.931  -65.750  1.00 14.51 ? 121 GLN D CG  1 
ATOM   5995  C CD  . GLN D 1 121 ? 16.432  32.436  -65.915  1.00 14.37 ? 121 GLN D CD  1 
ATOM   5996  O OE1 . GLN D 1 121 ? 17.294  31.840  -66.557  1.00 14.24 ? 121 GLN D OE1 1 
ATOM   5997  N NE2 . GLN D 1 121 ? 15.431  31.807  -65.314  1.00 14.31 ? 121 GLN D NE2 1 
ATOM   5998  N N   . LYS D 1 122 ? 19.657  36.997  -67.271  1.00 17.69 ? 122 LYS D N   1 
ATOM   5999  C CA  . LYS D 1 122 ? 20.956  37.598  -67.465  1.00 17.41 ? 122 LYS D CA  1 
ATOM   6000  C C   . LYS D 1 122 ? 20.911  39.121  -67.342  1.00 17.65 ? 122 LYS D C   1 
ATOM   6001  O O   . LYS D 1 122 ? 21.833  39.811  -67.768  1.00 18.03 ? 122 LYS D O   1 
ATOM   6002  C CB  . LYS D 1 122 ? 21.453  37.230  -68.857  1.00 17.11 ? 122 LYS D CB  1 
ATOM   6003  C CG  . LYS D 1 122 ? 21.481  35.789  -69.243  1.00 17.04 ? 122 LYS D CG  1 
ATOM   6004  C CD  . LYS D 1 122 ? 22.183  35.891  -70.611  1.00 17.58 ? 122 LYS D CD  1 
ATOM   6005  C CE  . LYS D 1 122 ? 23.042  34.749  -71.041  1.00 18.18 ? 122 LYS D CE  1 
ATOM   6006  N NZ  . LYS D 1 122 ? 23.357  35.055  -72.464  1.00 18.66 ? 122 LYS D NZ  1 
ATOM   6007  N N   . SER D 1 123 ? 19.844  39.633  -66.737  1.00 18.20 ? 123 SER D N   1 
ATOM   6008  C CA  . SER D 1 123 ? 19.552  41.069  -66.672  1.00 18.91 ? 123 SER D CA  1 
ATOM   6009  C C   . SER D 1 123 ? 20.610  41.838  -65.902  1.00 19.94 ? 123 SER D C   1 
ATOM   6010  O O   . SER D 1 123 ? 21.198  41.285  -64.961  1.00 20.23 ? 123 SER D O   1 
ATOM   6011  C CB  . SER D 1 123 ? 18.203  41.291  -66.016  1.00 18.55 ? 123 SER D CB  1 
ATOM   6012  O OG  . SER D 1 123 ? 17.593  42.399  -66.596  1.00 19.34 ? 123 SER D OG  1 
ATOM   6013  N N   . PRO D 1 124 ? 20.665  43.165  -66.128  1.00 21.08 ? 124 PRO D N   1 
ATOM   6014  C CA  . PRO D 1 124 ? 21.693  44.037  -66.714  1.00 20.84 ? 124 PRO D CA  1 
ATOM   6015  C C   . PRO D 1 124 ? 22.873  43.240  -67.156  1.00 22.11 ? 124 PRO D C   1 
ATOM   6016  O O   . PRO D 1 124 ? 23.253  42.294  -66.484  1.00 24.85 ? 124 PRO D O   1 
ATOM   6017  C CB  . PRO D 1 124 ? 22.086  44.964  -65.560  1.00 20.67 ? 124 PRO D CB  1 
ATOM   6018  C CG  . PRO D 1 124 ? 21.659  44.234  -64.341  1.00 20.99 ? 124 PRO D CG  1 
ATOM   6019  C CD  . PRO D 1 124 ? 20.322  43.700  -64.796  1.00 21.73 ? 124 PRO D CD  1 
ATOM   6020  N N   . GLY D 1 125 ? 23.498  43.580  -68.263  1.00 22.65 ? 125 GLY D N   1 
ATOM   6021  C CA  . GLY D 1 125 ? 24.681  42.803  -68.623  1.00 22.97 ? 125 GLY D CA  1 
ATOM   6022  C C   . GLY D 1 125 ? 25.968  43.379  -68.069  1.00 22.65 ? 125 GLY D C   1 
ATOM   6023  O O   . GLY D 1 125 ? 26.948  43.421  -68.792  1.00 24.23 ? 125 GLY D O   1 
ATOM   6024  N N   . TRP D 1 126 ? 25.999  43.829  -66.816  1.00 22.90 ? 126 TRP D N   1 
ATOM   6025  C CA  . TRP D 1 126 ? 27.104  44.698  -66.399  1.00 24.64 ? 126 TRP D CA  1 
ATOM   6026  C C   . TRP D 1 126 ? 27.493  44.805  -64.915  1.00 25.99 ? 126 TRP D C   1 
ATOM   6027  O O   . TRP D 1 126 ? 26.730  44.471  -64.003  1.00 26.39 ? 126 TRP D O   1 
ATOM   6028  C CB  . TRP D 1 126 ? 26.879  46.123  -66.960  1.00 25.42 ? 126 TRP D CB  1 
ATOM   6029  C CG  . TRP D 1 126 ? 25.636  46.859  -66.462  1.00 25.05 ? 126 TRP D CG  1 
ATOM   6030  C CD1 . TRP D 1 126 ? 25.108  46.848  -65.193  1.00 24.71 ? 126 TRP D CD1 1 
ATOM   6031  C CD2 . TRP D 1 126 ? 24.821  47.758  -67.221  1.00 24.54 ? 126 TRP D CD2 1 
ATOM   6032  N NE1 . TRP D 1 126 ? 24.012  47.660  -65.128  1.00 24.57 ? 126 TRP D NE1 1 
ATOM   6033  C CE2 . TRP D 1 126 ? 23.805  48.227  -66.358  1.00 24.34 ? 126 TRP D CE2 1 
ATOM   6034  C CE3 . TRP D 1 126 ? 24.845  48.206  -68.547  1.00 25.14 ? 126 TRP D CE3 1 
ATOM   6035  C CZ2 . TRP D 1 126 ? 22.815  49.117  -66.778  1.00 24.71 ? 126 TRP D CZ2 1 
ATOM   6036  C CZ3 . TRP D 1 126 ? 23.856  49.089  -68.969  1.00 25.55 ? 126 TRP D CZ3 1 
ATOM   6037  C CH2 . TRP D 1 126 ? 22.853  49.533  -68.082  1.00 25.20 ? 126 TRP D CH2 1 
ATOM   6038  N N   . ASP D 1 127 ? 28.713  45.288  -64.710  1.00 27.44 ? 127 ASP D N   1 
ATOM   6039  C CA  . ASP D 1 127 ? 29.259  45.617  -63.388  1.00 29.09 ? 127 ASP D CA  1 
ATOM   6040  C C   . ASP D 1 127 ? 28.839  46.999  -62.868  1.00 28.62 ? 127 ASP D C   1 
ATOM   6041  O O   . ASP D 1 127 ? 29.196  47.343  -61.744  1.00 29.87 ? 127 ASP D O   1 
ATOM   6042  C CB  . ASP D 1 127 ? 30.799  45.503  -63.396  1.00 32.12 ? 127 ASP D CB  1 
ATOM   6043  C CG  . ASP D 1 127 ? 31.483  46.379  -64.502  1.00 36.30 ? 127 ASP D CG  1 
ATOM   6044  O OD1 . ASP D 1 127 ? 30.779  46.979  -65.364  1.00 38.57 ? 127 ASP D OD1 1 
ATOM   6045  O OD2 . ASP D 1 127 ? 32.722  46.396  -64.553  1.00 36.98 ? 127 ASP D OD2 1 
ATOM   6046  N N   . TRP D 1 128 ? 28.099  47.788  -63.649  1.00 27.03 ? 128 TRP D N   1 
ATOM   6047  C CA  . TRP D 1 128 ? 27.747  49.164  -63.249  1.00 25.60 ? 128 TRP D CA  1 
ATOM   6048  C C   . TRP D 1 128 ? 26.847  49.215  -62.017  1.00 26.83 ? 128 TRP D C   1 
ATOM   6049  O O   . TRP D 1 128 ? 26.878  50.179  -61.259  1.00 27.45 ? 128 TRP D O   1 
ATOM   6050  C CB  . TRP D 1 128 ? 27.085  49.929  -64.403  1.00 23.63 ? 128 TRP D CB  1 
ATOM   6051  C CG  . TRP D 1 128 ? 27.971  50.133  -65.605  1.00 23.15 ? 128 TRP D CG  1 
ATOM   6052  C CD1 . TRP D 1 128 ? 29.292  49.863  -65.688  1.00 22.60 ? 128 TRP D CD1 1 
ATOM   6053  C CD2 . TRP D 1 128 ? 27.598  50.681  -66.886  1.00 23.12 ? 128 TRP D CD2 1 
ATOM   6054  N NE1 . TRP D 1 128 ? 29.767  50.177  -66.933  1.00 22.09 ? 128 TRP D NE1 1 
ATOM   6055  C CE2 . TRP D 1 128 ? 28.753  50.688  -67.688  1.00 22.51 ? 128 TRP D CE2 1 
ATOM   6056  C CE3 . TRP D 1 128 ? 26.394  51.136  -67.443  1.00 22.94 ? 128 TRP D CE3 1 
ATOM   6057  C CZ2 . TRP D 1 128 ? 28.750  51.142  -69.017  1.00 22.28 ? 128 TRP D CZ2 1 
ATOM   6058  C CZ3 . TRP D 1 128 ? 26.395  51.593  -68.757  1.00 22.43 ? 128 TRP D CZ3 1 
ATOM   6059  C CH2 . TRP D 1 128 ? 27.569  51.594  -69.526  1.00 22.12 ? 128 TRP D CH2 1 
ATOM   6060  N N   . THR D 1 129 ? 26.026  48.179  -61.857  1.00 27.93 ? 129 THR D N   1 
ATOM   6061  C CA  . THR D 1 129 ? 25.187  47.993  -60.677  1.00 26.86 ? 129 THR D CA  1 
ATOM   6062  C C   . THR D 1 129 ? 25.398  46.546  -60.266  1.00 25.84 ? 129 THR D C   1 
ATOM   6063  O O   . THR D 1 129 ? 25.827  45.730  -61.086  1.00 25.52 ? 129 THR D O   1 
ATOM   6064  C CB  . THR D 1 129 ? 23.681  48.198  -61.013  1.00 26.00 ? 129 THR D CB  1 
ATOM   6065  O OG1 . THR D 1 129 ? 23.232  47.254  -62.011  1.00 23.68 ? 129 THR D OG1 1 
ATOM   6066  C CG2 . THR D 1 129 ? 23.429  49.616  -61.495  1.00 25.45 ? 129 THR D CG2 1 
ATOM   6067  N N   . ASP D 1 130 ? 25.103  46.204  -59.020  1.00 24.48 ? 130 ASP D N   1 
ATOM   6068  C CA  . ASP D 1 130 ? 24.851  44.796  -58.733  1.00 25.61 ? 130 ASP D CA  1 
ATOM   6069  C C   . ASP D 1 130 ? 23.684  44.590  -57.785  1.00 24.31 ? 130 ASP D C   1 
ATOM   6070  O O   . ASP D 1 130 ? 23.816  44.446  -56.574  1.00 23.44 ? 130 ASP D O   1 
ATOM   6071  C CB  . ASP D 1 130 ? 26.142  43.988  -58.404  1.00 28.06 ? 130 ASP D CB  1 
ATOM   6072  C CG  . ASP D 1 130 ? 26.397  43.781  -56.903  1.00 27.89 ? 130 ASP D CG  1 
ATOM   6073  O OD1 . ASP D 1 130 ? 26.661  44.760  -56.208  1.00 29.27 ? 130 ASP D OD1 1 
ATOM   6074  O OD2 . ASP D 1 130 ? 26.374  42.633  -56.427  1.00 27.23 ? 130 ASP D OD2 1 
ATOM   6075  N N   . TYR D 1 131 ? 22.509  44.653  -58.396  1.00 22.92 ? 131 TYR D N   1 
ATOM   6076  C CA  . TYR D 1 131 ? 21.282  44.115  -57.833  1.00 21.04 ? 131 TYR D CA  1 
ATOM   6077  C C   . TYR D 1 131 ? 21.105  42.729  -58.423  1.00 20.22 ? 131 TYR D C   1 
ATOM   6078  O O   . TYR D 1 131 ? 21.614  42.455  -59.495  1.00 20.63 ? 131 TYR D O   1 
ATOM   6079  C CB  . TYR D 1 131 ? 20.094  44.987  -58.233  1.00 19.92 ? 131 TYR D CB  1 
ATOM   6080  C CG  . TYR D 1 131 ? 20.166  46.441  -57.813  1.00 18.56 ? 131 TYR D CG  1 
ATOM   6081  C CD1 . TYR D 1 131 ? 19.711  46.836  -56.567  1.00 18.24 ? 131 TYR D CD1 1 
ATOM   6082  C CD2 . TYR D 1 131 ? 20.648  47.420  -58.672  1.00 18.39 ? 131 TYR D CD2 1 
ATOM   6083  C CE1 . TYR D 1 131 ? 19.711  48.166  -56.178  1.00 18.67 ? 131 TYR D CE1 1 
ATOM   6084  C CE2 . TYR D 1 131 ? 20.678  48.756  -58.293  1.00 18.96 ? 131 TYR D CE2 1 
ATOM   6085  C CZ  . TYR D 1 131 ? 20.188  49.128  -57.046  1.00 18.83 ? 131 TYR D CZ  1 
ATOM   6086  O OH  . TYR D 1 131 ? 20.223  50.445  -56.658  1.00 17.57 ? 131 TYR D OH  1 
ATOM   6087  N N   . PRO D 1 132 ? 20.371  41.845  -57.735  1.00 19.81 ? 132 PRO D N   1 
ATOM   6088  C CA  . PRO D 1 132 ? 20.110  40.546  -58.366  1.00 19.68 ? 132 PRO D CA  1 
ATOM   6089  C C   . PRO D 1 132 ? 19.155  40.679  -59.552  1.00 19.79 ? 132 PRO D C   1 
ATOM   6090  O O   . PRO D 1 132 ? 18.493  41.705  -59.694  1.00 20.36 ? 132 PRO D O   1 
ATOM   6091  C CB  . PRO D 1 132 ? 19.459  39.726  -57.259  1.00 19.18 ? 132 PRO D CB  1 
ATOM   6092  C CG  . PRO D 1 132 ? 19.533  40.540  -56.015  1.00 19.25 ? 132 PRO D CG  1 
ATOM   6093  C CD  . PRO D 1 132 ? 19.722  41.970  -56.422  1.00 19.44 ? 132 PRO D CD  1 
ATOM   6094  N N   . PRO D 1 133 ? 19.080  39.658  -60.414  1.00 19.83 ? 133 PRO D N   1 
ATOM   6095  C CA  . PRO D 1 133 ? 18.045  39.698  -61.436  1.00 20.35 ? 133 PRO D CA  1 
ATOM   6096  C C   . PRO D 1 133 ? 16.694  39.273  -60.835  1.00 20.90 ? 133 PRO D C   1 
ATOM   6097  O O   . PRO D 1 133 ? 16.662  38.463  -59.905  1.00 21.86 ? 133 PRO D O   1 
ATOM   6098  C CB  . PRO D 1 133 ? 18.533  38.688  -62.484  1.00 20.11 ? 133 PRO D CB  1 
ATOM   6099  C CG  . PRO D 1 133 ? 19.543  37.846  -61.806  1.00 20.29 ? 133 PRO D CG  1 
ATOM   6100  C CD  . PRO D 1 133 ? 19.826  38.398  -60.434  1.00 20.24 ? 133 PRO D CD  1 
ATOM   6101  N N   . PRO D 1 134 ? 15.582  39.809  -61.354  1.00 20.12 ? 134 PRO D N   1 
ATOM   6102  C CA  . PRO D 1 134 ? 14.314  39.472  -60.725  1.00 20.27 ? 134 PRO D CA  1 
ATOM   6103  C C   . PRO D 1 134 ? 13.731  38.152  -61.232  1.00 20.45 ? 134 PRO D C   1 
ATOM   6104  O O   . PRO D 1 134 ? 14.032  37.734  -62.336  1.00 18.79 ? 134 PRO D O   1 
ATOM   6105  C CB  . PRO D 1 134 ? 13.401  40.636  -61.126  1.00 20.00 ? 134 PRO D CB  1 
ATOM   6106  C CG  . PRO D 1 134 ? 14.083  41.299  -62.288  1.00 20.13 ? 134 PRO D CG  1 
ATOM   6107  C CD  . PRO D 1 134 ? 15.402  40.638  -62.546  1.00 19.70 ? 134 PRO D CD  1 
ATOM   6108  N N   . PRO D 1 135 ? 12.874  37.507  -60.424  1.00 21.73 ? 135 PRO D N   1 
ATOM   6109  C CA  . PRO D 1 135 ? 12.125  36.351  -60.911  1.00 21.97 ? 135 PRO D CA  1 
ATOM   6110  C C   . PRO D 1 135 ? 11.118  36.744  -62.004  1.00 21.76 ? 135 PRO D C   1 
ATOM   6111  O O   . PRO D 1 135 ? 10.868  37.932  -62.211  1.00 20.64 ? 135 PRO D O   1 
ATOM   6112  C CB  . PRO D 1 135 ? 11.409  35.857  -59.655  1.00 21.98 ? 135 PRO D CB  1 
ATOM   6113  C CG  . PRO D 1 135 ? 11.234  37.076  -58.832  1.00 22.26 ? 135 PRO D CG  1 
ATOM   6114  C CD  . PRO D 1 135 ? 12.500  37.847  -59.040  1.00 22.21 ? 135 PRO D CD  1 
ATOM   6115  N N   . VAL D 1 136 ? 10.555  35.750  -62.693  1.00 22.10 ? 136 VAL D N   1 
ATOM   6116  C CA  . VAL D 1 136 ? 9.641   36.006  -63.804  1.00 23.24 ? 136 VAL D CA  1 
ATOM   6117  C C   . VAL D 1 136 ? 8.354   35.220  -63.638  1.00 22.19 ? 136 VAL D C   1 
ATOM   6118  O O   . VAL D 1 136 ? 8.388   34.050  -63.296  1.00 22.84 ? 136 VAL D O   1 
ATOM   6119  C CB  . VAL D 1 136 ? 10.282  35.639  -65.164  1.00 24.79 ? 136 VAL D CB  1 
ATOM   6120  C CG1 . VAL D 1 136 ? 9.283   35.822  -66.304  1.00 24.87 ? 136 VAL D CG1 1 
ATOM   6121  C CG2 . VAL D 1 136 ? 11.528  36.487  -65.415  1.00 25.26 ? 136 VAL D CG2 1 
ATOM   6122  N N   . LEU D 1 137 ? 7.229   35.887  -63.868  1.00 20.84 ? 137 LEU D N   1 
ATOM   6123  C CA  . LEU D 1 137 ? 5.931   35.237  -63.995  1.00 20.61 ? 137 LEU D CA  1 
ATOM   6124  C C   . LEU D 1 137 ? 5.498   35.336  -65.456  1.00 20.71 ? 137 LEU D C   1 
ATOM   6125  O O   . LEU D 1 137 ? 5.142   36.422  -65.947  1.00 20.22 ? 137 LEU D O   1 
ATOM   6126  C CB  . LEU D 1 137 ? 4.887   35.901  -63.084  1.00 20.76 ? 137 LEU D CB  1 
ATOM   6127  C CG  . LEU D 1 137 ? 3.402   35.566  -63.293  1.00 20.08 ? 137 LEU D CG  1 
ATOM   6128  C CD1 . LEU D 1 137 ? 3.117   34.092  -63.074  1.00 20.09 ? 137 LEU D CD1 1 
ATOM   6129  C CD2 . LEU D 1 137 ? 2.544   36.415  -62.370  1.00 19.78 ? 137 LEU D CD2 1 
ATOM   6130  N N   . LEU D 1 138 ? 5.548   34.207  -66.156  1.00 20.68 ? 138 LEU D N   1 
ATOM   6131  C CA  . LEU D 1 138 ? 5.125   34.151  -67.553  1.00 20.71 ? 138 LEU D CA  1 
ATOM   6132  C C   . LEU D 1 138 ? 3.631   33.900  -67.581  1.00 21.22 ? 138 LEU D C   1 
ATOM   6133  O O   . LEU D 1 138 ? 3.162   32.920  -66.994  1.00 21.56 ? 138 LEU D O   1 
ATOM   6134  C CB  . LEU D 1 138 ? 5.837   33.020  -68.296  1.00 20.21 ? 138 LEU D CB  1 
ATOM   6135  C CG  . LEU D 1 138 ? 5.424   32.862  -69.756  1.00 19.93 ? 138 LEU D CG  1 
ATOM   6136  C CD1 . LEU D 1 138 ? 5.697   34.129  -70.544  1.00 19.50 ? 138 LEU D CD1 1 
ATOM   6137  C CD2 . LEU D 1 138 ? 6.141   31.680  -70.374  1.00 19.62 ? 138 LEU D CD2 1 
ATOM   6138  N N   . ILE D 1 139 ? 2.891   34.783  -68.250  1.00 21.00 ? 139 ILE D N   1 
ATOM   6139  C CA  . ILE D 1 139 ? 1.442   34.649  -68.351  1.00 21.69 ? 139 ILE D CA  1 
ATOM   6140  C C   . ILE D 1 139 ? 1.051   34.331  -69.789  1.00 22.68 ? 139 ILE D C   1 
ATOM   6141  O O   . ILE D 1 139 ? 1.351   35.080  -70.717  1.00 24.49 ? 139 ILE D O   1 
ATOM   6142  C CB  . ILE D 1 139 ? 0.690   35.912  -67.877  1.00 21.58 ? 139 ILE D CB  1 
ATOM   6143  C CG1 . ILE D 1 139 ? 1.036   36.211  -66.421  1.00 21.63 ? 139 ILE D CG1 1 
ATOM   6144  C CG2 . ILE D 1 139 ? -0.819  35.720  -68.000  1.00 21.68 ? 139 ILE D CG2 1 
ATOM   6145  C CD1 . ILE D 1 139 ? 0.389   37.469  -65.893  1.00 21.82 ? 139 ILE D CD1 1 
ATOM   6146  N N   . SER D 1 140 ? 0.371   33.210  -69.965  1.00 22.60 ? 140 SER D N   1 
ATOM   6147  C CA  . SER D 1 140 ? -0.160  32.852  -71.250  1.00 22.35 ? 140 SER D CA  1 
ATOM   6148  C C   . SER D 1 140 ? -1.487  33.586  -71.433  1.00 21.41 ? 140 SER D C   1 
ATOM   6149  O O   . SER D 1 140 ? -2.281  33.627  -70.512  1.00 20.77 ? 140 SER D O   1 
ATOM   6150  C CB  . SER D 1 140 ? -0.365  31.344  -71.294  1.00 23.24 ? 140 SER D CB  1 
ATOM   6151  O OG  . SER D 1 140 ? -1.548  31.041  -71.962  1.00 24.49 ? 140 SER D OG  1 
ATOM   6152  N N   . PRO D 1 141 ? -1.729  34.160  -72.624  1.00 21.37 ? 141 PRO D N   1 
ATOM   6153  C CA  . PRO D 1 141 ? -3.001  34.818  -72.879  1.00 20.93 ? 141 PRO D CA  1 
ATOM   6154  C C   . PRO D 1 141 ? -4.114  33.813  -73.129  1.00 21.72 ? 141 PRO D C   1 
ATOM   6155  O O   . PRO D 1 141 ? -3.853  32.634  -73.356  1.00 21.63 ? 141 PRO D O   1 
ATOM   6156  C CB  . PRO D 1 141 ? -2.736  35.608  -74.150  1.00 20.93 ? 141 PRO D CB  1 
ATOM   6157  C CG  . PRO D 1 141 ? -1.750  34.779  -74.895  1.00 21.05 ? 141 PRO D CG  1 
ATOM   6158  C CD  . PRO D 1 141 ? -0.894  34.114  -73.841  1.00 21.64 ? 141 PRO D CD  1 
ATOM   6159  N N   . PRO D 1 142 ? -5.364  34.269  -73.086  1.00 23.33 ? 142 PRO D N   1 
ATOM   6160  C CA  . PRO D 1 142 ? -6.457  33.361  -73.354  1.00 23.69 ? 142 PRO D CA  1 
ATOM   6161  C C   . PRO D 1 142 ? -6.561  33.069  -74.843  1.00 24.06 ? 142 PRO D C   1 
ATOM   6162  O O   . PRO D 1 142 ? -5.893  33.711  -75.645  1.00 23.49 ? 142 PRO D O   1 
ATOM   6163  C CB  . PRO D 1 142 ? -7.673  34.144  -72.882  1.00 24.37 ? 142 PRO D CB  1 
ATOM   6164  C CG  . PRO D 1 142 ? -7.313  35.582  -73.090  1.00 24.68 ? 142 PRO D CG  1 
ATOM   6165  C CD  . PRO D 1 142 ? -5.834  35.645  -72.819  1.00 24.44 ? 142 PRO D CD  1 
ATOM   6166  N N   . PRO D 1 143 ? -7.386  32.087  -75.212  1.00 24.55 ? 143 PRO D N   1 
ATOM   6167  C CA  . PRO D 1 143 ? -7.602  31.854  -76.617  1.00 23.88 ? 143 PRO D CA  1 
ATOM   6168  C C   . PRO D 1 143 ? -8.221  33.056  -77.283  1.00 22.83 ? 143 PRO D C   1 
ATOM   6169  O O   . PRO D 1 143 ? -8.959  33.797  -76.659  1.00 20.65 ? 143 PRO D O   1 
ATOM   6170  C CB  . PRO D 1 143 ? -8.584  30.676  -76.641  1.00 24.10 ? 143 PRO D CB  1 
ATOM   6171  C CG  . PRO D 1 143 ? -8.373  29.977  -75.364  1.00 24.57 ? 143 PRO D CG  1 
ATOM   6172  C CD  . PRO D 1 143 ? -8.021  31.052  -74.379  1.00 25.11 ? 143 PRO D CD  1 
ATOM   6173  N N   . LEU D 1 144 ? -7.904  33.212  -78.558  1.00 23.80 ? 144 LEU D N   1 
ATOM   6174  C CA  . LEU D 1 144 ? -8.525  34.221  -79.386  1.00 24.58 ? 144 LEU D CA  1 
ATOM   6175  C C   . LEU D 1 144 ? -10.016 33.963  -79.472  1.00 25.86 ? 144 LEU D C   1 
ATOM   6176  O O   . LEU D 1 144 ? -10.488 32.864  -79.186  1.00 23.29 ? 144 LEU D O   1 
ATOM   6177  C CB  . LEU D 1 144 ? -7.951  34.182  -80.801  1.00 23.60 ? 144 LEU D CB  1 
ATOM   6178  C CG  . LEU D 1 144 ? -6.471  34.401  -81.024  1.00 22.48 ? 144 LEU D CG  1 
ATOM   6179  C CD1 . LEU D 1 144 ? -6.124  34.024  -82.453  1.00 22.68 ? 144 LEU D CD1 1 
ATOM   6180  C CD2 . LEU D 1 144 ? -6.152  35.858  -80.778  1.00 23.08 ? 144 LEU D CD2 1 
ATOM   6181  N N   . GLY D 1 145 ? -10.741 34.994  -79.896  1.00 29.62 ? 145 GLY D N   1 
ATOM   6182  C CA  . GLY D 1 145 ? -12.155 34.874  -80.190  1.00 31.71 ? 145 GLY D CA  1 
ATOM   6183  C C   . GLY D 1 145 ? -12.395 33.934  -81.356  1.00 32.51 ? 145 GLY D C   1 
ATOM   6184  O O   . GLY D 1 145 ? -11.551 33.785  -82.241  1.00 30.61 ? 145 GLY D O   1 
ATOM   6185  N N   . GLU D 1 146 ? -13.563 33.288  -81.346  1.00 34.65 ? 146 GLU D N   1 
ATOM   6186  C CA  . GLU D 1 146 ? -13.957 32.430  -82.451  1.00 36.77 ? 146 GLU D CA  1 
ATOM   6187  C C   . GLU D 1 146 ? -14.312 33.248  -83.659  1.00 34.29 ? 146 GLU D C   1 
ATOM   6188  O O   . GLU D 1 146 ? -14.202 32.750  -84.773  1.00 35.08 ? 146 GLU D O   1 
ATOM   6189  C CB  . GLU D 1 146 ? -15.106 31.505  -82.058  1.00 41.56 ? 146 GLU D CB  1 
ATOM   6190  C CG  . GLU D 1 146 ? -14.612 30.413  -81.083  1.00 45.63 ? 146 GLU D CG  1 
ATOM   6191  C CD  . GLU D 1 146 ? -15.265 29.071  -81.319  1.00 48.42 ? 146 GLU D CD  1 
ATOM   6192  O OE1 . GLU D 1 146 ? -14.579 28.005  -81.213  1.00 53.41 ? 146 GLU D OE1 1 
ATOM   6193  O OE2 . GLU D 1 146 ? -16.478 29.105  -81.615  1.00 48.53 ? 146 GLU D OE2 1 
ATOM   6194  N N   . THR D 1 147 ? -14.716 34.499  -83.438  1.00 32.35 ? 147 THR D N   1 
ATOM   6195  C CA  . THR D 1 147 ? -15.071 35.412  -84.526  1.00 31.74 ? 147 THR D CA  1 
ATOM   6196  C C   . THR D 1 147 ? -14.273 36.712  -84.485  1.00 31.49 ? 147 THR D C   1 
ATOM   6197  O O   . THR D 1 147 ? -14.455 37.570  -83.606  1.00 34.93 ? 147 THR D O   1 
ATOM   6198  C CB  . THR D 1 147 ? -16.571 35.721  -84.488  1.00 30.97 ? 147 THR D CB  1 
ATOM   6199  O OG1 . THR D 1 147 ? -17.276 34.485  -84.657  1.00 29.95 ? 147 THR D OG1 1 
ATOM   6200  C CG2 . THR D 1 147 ? -16.991 36.689  -85.588  1.00 29.91 ? 147 THR D CG2 1 
ATOM   6201  N N   . ILE D 1 148 ? -13.407 36.869  -85.473  1.00 30.62 ? 148 ILE D N   1 
ATOM   6202  C CA  . ILE D 1 148 ? -12.499 38.003  -85.529  1.00 30.25 ? 148 ILE D CA  1 
ATOM   6203  C C   . ILE D 1 148 ? -12.975 39.002  -86.576  1.00 28.20 ? 148 ILE D C   1 
ATOM   6204  O O   . ILE D 1 148 ? -13.475 38.614  -87.634  1.00 28.41 ? 148 ILE D O   1 
ATOM   6205  C CB  . ILE D 1 148 ? -11.061 37.498  -85.805  1.00 30.81 ? 148 ILE D CB  1 
ATOM   6206  C CG1 . ILE D 1 148 ? -10.597 36.624  -84.628  1.00 31.09 ? 148 ILE D CG1 1 
ATOM   6207  C CG2 . ILE D 1 148 ? -10.105 38.659  -86.035  1.00 31.05 ? 148 ILE D CG2 1 
ATOM   6208  C CD1 . ILE D 1 148 ? -9.459  35.695  -84.975  1.00 31.43 ? 148 ILE D CD1 1 
ATOM   6209  N N   . ASP D 1 149 ? -12.829 40.285  -86.275  1.00 26.24 ? 149 ASP D N   1 
ATOM   6210  C CA  . ASP D 1 149 ? -13.218 41.342  -87.203  1.00 26.47 ? 149 ASP D CA  1 
ATOM   6211  C C   . ASP D 1 149 ? -12.702 40.979  -88.598  1.00 27.52 ? 149 ASP D C   1 
ATOM   6212  O O   . ASP D 1 149 ? -11.521 40.659  -88.760  1.00 27.34 ? 149 ASP D O   1 
ATOM   6213  C CB  . ASP D 1 149 ? -12.637 42.680  -86.746  1.00 26.06 ? 149 ASP D CB  1 
ATOM   6214  C CG  . ASP D 1 149 ? -13.198 43.862  -87.499  1.00 25.26 ? 149 ASP D CG  1 
ATOM   6215  O OD1 . ASP D 1 149 ? -13.152 43.859  -88.746  1.00 25.85 ? 149 ASP D OD1 1 
ATOM   6216  O OD2 . ASP D 1 149 ? -13.657 44.819  -86.833  1.00 24.17 ? 149 ASP D OD2 1 
ATOM   6217  N N   . PRO D 1 150 ? -13.595 40.988  -89.606  1.00 29.05 ? 150 PRO D N   1 
ATOM   6218  C CA  . PRO D 1 150 ? -13.230 40.626  -90.982  1.00 27.81 ? 150 PRO D CA  1 
ATOM   6219  C C   . PRO D 1 150 ? -12.002 41.315  -91.550  1.00 27.27 ? 150 PRO D C   1 
ATOM   6220  O O   . PRO D 1 150 ? -11.317 40.718  -92.382  1.00 27.05 ? 150 PRO D O   1 
ATOM   6221  C CB  . PRO D 1 150 ? -14.485 40.988  -91.767  1.00 27.24 ? 150 PRO D CB  1 
ATOM   6222  C CG  . PRO D 1 150 ? -15.560 40.632  -90.829  1.00 27.73 ? 150 PRO D CG  1 
ATOM   6223  C CD  . PRO D 1 150 ? -15.064 41.032  -89.453  1.00 29.18 ? 150 PRO D CD  1 
ATOM   6224  N N   . LEU D 1 151 ? -11.722 42.547  -91.129  1.00 27.04 ? 151 LEU D N   1 
ATOM   6225  C CA  . LEU D 1 151 ? -10.492 43.241  -91.539  1.00 28.46 ? 151 LEU D CA  1 
ATOM   6226  C C   . LEU D 1 151 ? -9.230  42.521  -91.037  1.00 27.72 ? 151 LEU D C   1 
ATOM   6227  O O   . LEU D 1 151 ? -8.238  42.481  -91.734  1.00 28.10 ? 151 LEU D O   1 
ATOM   6228  C CB  . LEU D 1 151 ? -10.487 44.682  -91.037  1.00 30.22 ? 151 LEU D CB  1 
ATOM   6229  C CG  . LEU D 1 151 ? -11.347 45.673  -91.827  1.00 31.83 ? 151 LEU D CG  1 
ATOM   6230  C CD1 . LEU D 1 151 ? -12.520 46.302  -91.055  1.00 33.35 ? 151 LEU D CD1 1 
ATOM   6231  C CD2 . LEU D 1 151 ? -10.395 46.768  -92.296  1.00 32.42 ? 151 LEU D CD2 1 
ATOM   6232  N N   . ALA D 1 152 ? -9.285  41.955  -89.834  1.00 27.10 ? 152 ALA D N   1 
ATOM   6233  C CA  . ALA D 1 152 ? -8.137  41.311  -89.200  1.00 25.90 ? 152 ALA D CA  1 
ATOM   6234  C C   . ALA D 1 152 ? -8.095  39.783  -89.379  1.00 25.75 ? 152 ALA D C   1 
ATOM   6235  O O   . ALA D 1 152 ? -7.038  39.170  -89.236  1.00 26.25 ? 152 ALA D O   1 
ATOM   6236  C CB  . ALA D 1 152 ? -8.116  41.645  -87.719  1.00 26.00 ? 152 ALA D CB  1 
ATOM   6237  N N   . ALA D 1 153 ? -9.225  39.161  -89.691  1.00 24.91 ? 153 ALA D N   1 
ATOM   6238  C CA  . ALA D 1 153 ? -9.293  37.702  -89.797  1.00 23.50 ? 153 ALA D CA  1 
ATOM   6239  C C   . ALA D 1 153 ? -8.238  37.042  -90.702  1.00 23.04 ? 153 ALA D C   1 
ATOM   6240  O O   . ALA D 1 153 ? -7.659  36.028  -90.315  1.00 23.44 ? 153 ALA D O   1 
ATOM   6241  C CB  . ALA D 1 153 ? -10.691 37.274  -90.213  1.00 22.85 ? 153 ALA D CB  1 
ATOM   6242  N N   . PRO D 1 154 ? -7.971  37.602  -91.899  1.00 23.64 ? 154 PRO D N   1 
ATOM   6243  C CA  . PRO D 1 154 ? -6.960  36.994  -92.792  1.00 23.95 ? 154 PRO D CA  1 
ATOM   6244  C C   . PRO D 1 154 ? -5.589  36.827  -92.149  1.00 24.39 ? 154 PRO D C   1 
ATOM   6245  O O   . PRO D 1 154 ? -4.871  35.885  -92.470  1.00 23.99 ? 154 PRO D O   1 
ATOM   6246  C CB  . PRO D 1 154 ? -6.860  37.988  -93.952  1.00 23.89 ? 154 PRO D CB  1 
ATOM   6247  C CG  . PRO D 1 154 ? -8.169  38.687  -93.956  1.00 24.39 ? 154 PRO D CG  1 
ATOM   6248  C CD  . PRO D 1 154 ? -8.554  38.813  -92.501  1.00 24.32 ? 154 PRO D CD  1 
ATOM   6249  N N   . ILE D 1 155 ? -5.260  37.756  -91.249  1.00 25.03 ? 155 ILE D N   1 
ATOM   6250  C CA  . ILE D 1 155 ? -3.997  37.802  -90.532  1.00 25.26 ? 155 ILE D CA  1 
ATOM   6251  C C   . ILE D 1 155 ? -3.963  36.851  -89.302  1.00 24.66 ? 155 ILE D C   1 
ATOM   6252  O O   . ILE D 1 155 ? -2.894  36.617  -88.735  1.00 24.49 ? 155 ILE D O   1 
ATOM   6253  C CB  . ILE D 1 155 ? -3.696  39.303  -90.211  1.00 26.16 ? 155 ILE D CB  1 
ATOM   6254  C CG1 . ILE D 1 155 ? -2.796  39.858  -91.318  1.00 29.02 ? 155 ILE D CG1 1 
ATOM   6255  C CG2 . ILE D 1 155 ? -3.084  39.564  -88.838  1.00 25.79 ? 155 ILE D CG2 1 
ATOM   6256  C CD1 . ILE D 1 155 ? -2.647  41.382  -91.326  1.00 31.74 ? 155 ILE D CD1 1 
ATOM   6257  N N   . PHE D 1 156 ? -5.116  36.295  -88.902  1.00 23.08 ? 156 PHE D N   1 
ATOM   6258  C CA  . PHE D 1 156 ? -5.197  35.356  -87.762  1.00 21.86 ? 156 PHE D CA  1 
ATOM   6259  C C   . PHE D 1 156 ? -5.696  33.959  -88.133  1.00 21.23 ? 156 PHE D C   1 
ATOM   6260  O O   . PHE D 1 156 ? -6.285  33.268  -87.305  1.00 20.51 ? 156 PHE D O   1 
ATOM   6261  C CB  . PHE D 1 156 ? -6.063  35.940  -86.635  1.00 21.33 ? 156 PHE D CB  1 
ATOM   6262  C CG  . PHE D 1 156 ? -5.380  37.029  -85.858  1.00 21.07 ? 156 PHE D CG  1 
ATOM   6263  C CD1 . PHE D 1 156 ? -4.429  36.713  -84.907  1.00 21.51 ? 156 PHE D CD1 1 
ATOM   6264  C CD2 . PHE D 1 156 ? -5.674  38.356  -86.092  1.00 20.38 ? 156 PHE D CD2 1 
ATOM   6265  C CE1 . PHE D 1 156 ? -3.787  37.719  -84.189  1.00 21.64 ? 156 PHE D CE1 1 
ATOM   6266  C CE2 . PHE D 1 156 ? -5.044  39.366  -85.389  1.00 20.28 ? 156 PHE D CE2 1 
ATOM   6267  C CZ  . PHE D 1 156 ? -4.099  39.056  -84.442  1.00 20.78 ? 156 PHE D CZ  1 
ATOM   6268  N N   . VAL D 1 157 ? -5.441  33.537  -89.368  1.00 21.46 ? 157 VAL D N   1 
ATOM   6269  C CA  . VAL D 1 157 ? -5.834  32.197  -89.804  1.00 21.34 ? 157 VAL D CA  1 
ATOM   6270  C C   . VAL D 1 157 ? -4.975  31.185  -89.036  1.00 20.94 ? 157 VAL D C   1 
ATOM   6271  O O   . VAL D 1 157 ? -3.788  31.411  -88.827  1.00 21.58 ? 157 VAL D O   1 
ATOM   6272  C CB  . VAL D 1 157 ? -5.713  32.020  -91.343  1.00 21.33 ? 157 VAL D CB  1 
ATOM   6273  C CG1 . VAL D 1 157 ? -5.964  30.561  -91.738  1.00 20.85 ? 157 VAL D CG1 1 
ATOM   6274  C CG2 . VAL D 1 157 ? -6.697  32.916  -92.069  1.00 20.86 ? 157 VAL D CG2 1 
ATOM   6275  N N   . ASP D 1 158 ? -5.605  30.103  -88.579  1.00 20.78 ? 158 ASP D N   1 
ATOM   6276  C CA  . ASP D 1 158 ? -4.985  29.117  -87.689  1.00 20.35 ? 158 ASP D CA  1 
ATOM   6277  C C   . ASP D 1 158 ? -4.462  29.681  -86.372  1.00 20.54 ? 158 ASP D C   1 
ATOM   6278  O O   . ASP D 1 158 ? -3.745  28.994  -85.645  1.00 21.77 ? 158 ASP D O   1 
ATOM   6279  C CB  . ASP D 1 158 ? -3.864  28.387  -88.407  1.00 20.31 ? 158 ASP D CB  1 
ATOM   6280  C CG  . ASP D 1 158 ? -4.299  27.832  -89.726  1.00 20.83 ? 158 ASP D CG  1 
ATOM   6281  O OD1 . ASP D 1 158 ? -5.390  27.203  -89.770  1.00 20.62 ? 158 ASP D OD1 1 
ATOM   6282  O OD2 . ASP D 1 158 ? -3.552  28.026  -90.715  1.00 21.85 ? 158 ASP D OD2 1 
ATOM   6283  N N   . GLY D 1 159 ? -4.830  30.916  -86.043  1.00 20.68 ? 159 GLY D N   1 
ATOM   6284  C CA  . GLY D 1 159 ? -4.329  31.553  -84.834  1.00 20.91 ? 159 GLY D CA  1 
ATOM   6285  C C   . GLY D 1 159 ? -4.986  31.023  -83.565  1.00 20.90 ? 159 GLY D C   1 
ATOM   6286  O O   . GLY D 1 159 ? -4.346  30.919  -82.521  1.00 20.70 ? 159 GLY D O   1 
ATOM   6287  N N   . LEU D 1 160 ? -6.271  30.700  -83.657  1.00 21.67 ? 160 LEU D N   1 
ATOM   6288  C CA  . LEU D 1 160 ? -7.039  30.236  -82.526  1.00 22.12 ? 160 LEU D CA  1 
ATOM   6289  C C   . LEU D 1 160 ? -6.407  28.980  -81.944  1.00 23.17 ? 160 LEU D C   1 
ATOM   6290  O O   . LEU D 1 160 ? -6.185  28.887  -80.730  1.00 25.58 ? 160 LEU D O   1 
ATOM   6291  C CB  . LEU D 1 160 ? -8.477  29.937  -82.957  1.00 22.25 ? 160 LEU D CB  1 
ATOM   6292  C CG  . LEU D 1 160 ? -9.382  29.243  -81.925  1.00 23.00 ? 160 LEU D CG  1 
ATOM   6293  C CD1 . LEU D 1 160 ? -9.467  30.110  -80.679  1.00 23.91 ? 160 LEU D CD1 1 
ATOM   6294  C CD2 . LEU D 1 160 ? -10.760 28.986  -82.507  1.00 23.43 ? 160 LEU D CD2 1 
ATOM   6295  N N   . ALA D 1 161 ? -6.121  28.007  -82.808  1.00 23.12 ? 161 ALA D N   1 
ATOM   6296  C CA  . ALA D 1 161 ? -5.602  26.729  -82.347  1.00 22.72 ? 161 ALA D CA  1 
ATOM   6297  C C   . ALA D 1 161 ? -4.233  26.931  -81.687  1.00 22.80 ? 161 ALA D C   1 
ATOM   6298  O O   . ALA D 1 161 ? -3.928  26.324  -80.661  1.00 23.99 ? 161 ALA D O   1 
ATOM   6299  C CB  . ALA D 1 161 ? -5.516  25.760  -83.509  1.00 22.62 ? 161 ALA D CB  1 
ATOM   6300  N N   . LYS D 1 162 ? -3.423  27.804  -82.270  1.00 22.00 ? 162 LYS D N   1 
ATOM   6301  C CA  . LYS D 1 162 ? -2.131  28.146  -81.695  1.00 22.16 ? 162 LYS D CA  1 
ATOM   6302  C C   . LYS D 1 162 ? -2.283  28.763  -80.313  1.00 22.80 ? 162 LYS D C   1 
ATOM   6303  O O   . LYS D 1 162 ? -1.556  28.399  -79.401  1.00 22.53 ? 162 LYS D O   1 
ATOM   6304  C CB  . LYS D 1 162 ? -1.376  29.112  -82.601  1.00 21.22 ? 162 LYS D CB  1 
ATOM   6305  C CG  . LYS D 1 162 ? -0.887  28.456  -83.872  1.00 20.72 ? 162 LYS D CG  1 
ATOM   6306  C CD  . LYS D 1 162 ? -0.263  29.463  -84.820  1.00 20.48 ? 162 LYS D CD  1 
ATOM   6307  C CE  . LYS D 1 162 ? -0.128  28.875  -86.203  1.00 19.62 ? 162 LYS D CE  1 
ATOM   6308  N NZ  . LYS D 1 162 ? 0.818   29.682  -86.998  1.00 19.65 ? 162 LYS D NZ  1 
ATOM   6309  N N   . SER D 1 163 ? -3.224  29.692  -80.168  1.00 23.78 ? 163 SER D N   1 
ATOM   6310  C CA  . SER D 1 163 ? -3.444  30.358  -78.891  1.00 24.38 ? 163 SER D CA  1 
ATOM   6311  C C   . SER D 1 163 ? -3.937  29.376  -77.819  1.00 25.92 ? 163 SER D C   1 
ATOM   6312  O O   . SER D 1 163 ? -3.629  29.535  -76.632  1.00 27.16 ? 163 SER D O   1 
ATOM   6313  C CB  . SER D 1 163 ? -4.417  31.534  -79.036  1.00 23.73 ? 163 SER D CB  1 
ATOM   6314  O OG  . SER D 1 163 ? -5.733  31.109  -79.324  1.00 23.40 ? 163 SER D OG  1 
ATOM   6315  N N   . GLU D 1 164 ? -4.691  28.357  -78.234  1.00 25.67 ? 164 GLU D N   1 
ATOM   6316  C CA  . GLU D 1 164 ? -5.163  27.338  -77.294  1.00 24.91 ? 164 GLU D CA  1 
ATOM   6317  C C   . GLU D 1 164 ? -4.010  26.498  -76.773  1.00 22.68 ? 164 GLU D C   1 
ATOM   6318  O O   . GLU D 1 164 ? -4.030  26.060  -75.633  1.00 21.26 ? 164 GLU D O   1 
ATOM   6319  C CB  . GLU D 1 164 ? -6.225  26.450  -77.941  1.00 27.11 ? 164 GLU D CB  1 
ATOM   6320  C CG  . GLU D 1 164 ? -7.632  27.057  -77.889  1.00 29.44 ? 164 GLU D CG  1 
ATOM   6321  C CD  . GLU D 1 164 ? -8.599  26.440  -78.881  1.00 30.49 ? 164 GLU D CD  1 
ATOM   6322  O OE1 . GLU D 1 164 ? -9.783  26.849  -78.847  1.00 29.23 ? 164 GLU D OE1 1 
ATOM   6323  O OE2 . GLU D 1 164 ? -8.170  25.574  -79.692  1.00 32.78 ? 164 GLU D OE2 1 
ATOM   6324  N N   . ALA D 1 165 ? -2.993  26.300  -77.606  1.00 21.50 ? 165 ALA D N   1 
ATOM   6325  C CA  . ALA D 1 165 ? -1.829  25.488  -77.241  1.00 21.24 ? 165 ALA D CA  1 
ATOM   6326  C C   . ALA D 1 165 ? -0.761  26.200  -76.395  1.00 20.61 ? 165 ALA D C   1 
ATOM   6327  O O   . ALA D 1 165 ? 0.172   25.543  -75.928  1.00 20.07 ? 165 ALA D O   1 
ATOM   6328  C CB  . ALA D 1 165 ? -1.187  24.931  -78.496  1.00 21.69 ? 165 ALA D CB  1 
ATOM   6329  N N   . LEU D 1 166 ? -0.889  27.512  -76.187  1.00 19.76 ? 166 LEU D N   1 
ATOM   6330  C CA  . LEU D 1 166 ? 0.149   28.278  -75.505  1.00 19.91 ? 166 LEU D CA  1 
ATOM   6331  C C   . LEU D 1 166 ? 0.281   27.952  -74.000  1.00 20.43 ? 166 LEU D C   1 
ATOM   6332  O O   . LEU D 1 166 ? 1.396   27.777  -73.518  1.00 21.40 ? 166 LEU D O   1 
ATOM   6333  C CB  . LEU D 1 166 ? -0.032  29.788  -75.707  1.00 19.94 ? 166 LEU D CB  1 
ATOM   6334  C CG  . LEU D 1 166 ? 0.177   30.307  -77.145  1.00 20.44 ? 166 LEU D CG  1 
ATOM   6335  C CD1 . LEU D 1 166 ? -0.007  31.822  -77.228  1.00 20.62 ? 166 LEU D CD1 1 
ATOM   6336  C CD2 . LEU D 1 166 ? 1.531   29.884  -77.734  1.00 20.33 ? 166 LEU D CD2 1 
ATOM   6337  N N   . PRO D 1 167 ? -0.833  27.859  -73.255  1.00 19.44 ? 167 PRO D N   1 
ATOM   6338  C CA  . PRO D 1 167 ? -0.675  27.564  -71.829  1.00 19.05 ? 167 PRO D CA  1 
ATOM   6339  C C   . PRO D 1 167 ? 0.224   26.349  -71.516  1.00 18.93 ? 167 PRO D C   1 
ATOM   6340  O O   . PRO D 1 167 ? 1.108   26.439  -70.658  1.00 18.85 ? 167 PRO D O   1 
ATOM   6341  C CB  . PRO D 1 167 ? -2.112  27.333  -71.354  1.00 18.74 ? 167 PRO D CB  1 
ATOM   6342  C CG  . PRO D 1 167 ? -2.956  28.098  -72.285  1.00 19.00 ? 167 PRO D CG  1 
ATOM   6343  C CD  . PRO D 1 167 ? -2.241  28.067  -73.620  1.00 19.23 ? 167 PRO D CD  1 
ATOM   6344  N N   . GLY D 1 168 ? 0.016   25.239  -72.213  1.00 18.66 ? 168 GLY D N   1 
ATOM   6345  C CA  . GLY D 1 168 ? 0.815   24.037  -71.964  1.00 18.70 ? 168 GLY D CA  1 
ATOM   6346  C C   . GLY D 1 168 ? 2.291   24.264  -72.233  1.00 18.88 ? 168 GLY D C   1 
ATOM   6347  O O   . GLY D 1 168 ? 3.132   23.904  -71.406  1.00 17.73 ? 168 GLY D O   1 
ATOM   6348  N N   . VAL D 1 169 ? 2.597   24.883  -73.379  1.00 19.29 ? 169 VAL D N   1 
ATOM   6349  C CA  . VAL D 1 169 ? 3.973   25.163  -73.774  1.00 19.49 ? 169 VAL D CA  1 
ATOM   6350  C C   . VAL D 1 169 ? 4.615   26.160  -72.824  1.00 19.42 ? 169 VAL D C   1 
ATOM   6351  O O   . VAL D 1 169 ? 5.714   25.927  -72.335  1.00 18.90 ? 169 VAL D O   1 
ATOM   6352  C CB  . VAL D 1 169 ? 4.059   25.729  -75.217  1.00 19.82 ? 169 VAL D CB  1 
ATOM   6353  C CG1 . VAL D 1 169 ? 5.487   26.090  -75.569  1.00 20.92 ? 169 VAL D CG1 1 
ATOM   6354  C CG2 . VAL D 1 169 ? 3.557   24.732  -76.239  1.00 19.32 ? 169 VAL D CG2 1 
ATOM   6355  N N   . TYR D 1 170 ? 3.925   27.277  -72.581  1.00 20.35 ? 170 TYR D N   1 
ATOM   6356  C CA  . TYR D 1 170 ? 4.416   28.330  -71.658  1.00 20.34 ? 170 TYR D CA  1 
ATOM   6357  C C   . TYR D 1 170 ? 4.729   27.773  -70.277  1.00 20.32 ? 170 TYR D C   1 
ATOM   6358  O O   . TYR D 1 170 ? 5.728   28.146  -69.673  1.00 20.70 ? 170 TYR D O   1 
ATOM   6359  C CB  . TYR D 1 170 ? 3.402   29.482  -71.523  1.00 19.76 ? 170 TYR D CB  1 
ATOM   6360  C CG  . TYR D 1 170 ? 3.499   30.558  -72.590  1.00 19.28 ? 170 TYR D CG  1 
ATOM   6361  C CD1 . TYR D 1 170 ? 3.953   30.267  -73.876  1.00 19.53 ? 170 TYR D CD1 1 
ATOM   6362  C CD2 . TYR D 1 170 ? 3.096   31.860  -72.321  1.00 19.38 ? 170 TYR D CD2 1 
ATOM   6363  C CE1 . TYR D 1 170 ? 4.039   31.245  -74.851  1.00 19.84 ? 170 TYR D CE1 1 
ATOM   6364  C CE2 . TYR D 1 170 ? 3.167   32.847  -73.286  1.00 20.36 ? 170 TYR D CE2 1 
ATOM   6365  C CZ  . TYR D 1 170 ? 3.648   32.533  -74.553  1.00 20.61 ? 170 TYR D CZ  1 
ATOM   6366  O OH  . TYR D 1 170 ? 3.727   33.502  -75.536  1.00 21.53 ? 170 TYR D OH  1 
ATOM   6367  N N   . LYS D 1 171 ? 3.884   26.878  -69.781  1.00 20.56 ? 171 LYS D N   1 
ATOM   6368  C CA  . LYS D 1 171 ? 4.131   26.279  -68.484  1.00 21.21 ? 171 LYS D CA  1 
ATOM   6369  C C   . LYS D 1 171 ? 5.416   25.467  -68.455  1.00 20.36 ? 171 LYS D C   1 
ATOM   6370  O O   . LYS D 1 171 ? 6.189   25.578  -67.514  1.00 19.36 ? 171 LYS D O   1 
ATOM   6371  C CB  . LYS D 1 171 ? 2.952   25.392  -68.050  1.00 22.28 ? 171 LYS D CB  1 
ATOM   6372  C CG  . LYS D 1 171 ? 3.022   24.914  -66.628  1.00 22.99 ? 171 LYS D CG  1 
ATOM   6373  C CD  . LYS D 1 171 ? 2.245   23.556  -66.573  1.00 23.93 ? 171 LYS D CD  1 
ATOM   6374  C CE  . LYS D 1 171 ? 2.168   22.933  -65.194  1.00 25.14 ? 171 LYS D CE  1 
ATOM   6375  N NZ  . LYS D 1 171 ? 1.482   23.869  -64.252  1.00 26.18 ? 171 LYS D NZ  1 
ATOM   6376  N N   . ALA D 1 172 ? 5.653   24.660  -69.486  1.00 20.96 ? 172 ALA D N   1 
ATOM   6377  C CA  . ALA D 1 172 ? 6.871   23.835  -69.553  1.00 21.29 ? 172 ALA D CA  1 
ATOM   6378  C C   . ALA D 1 172 ? 8.099   24.714  -69.610  1.00 21.24 ? 172 ALA D C   1 
ATOM   6379  O O   . ALA D 1 172 ? 9.053   24.496  -68.880  1.00 22.03 ? 172 ALA D O   1 
ATOM   6380  C CB  . ALA D 1 172 ? 6.833   22.899  -70.755  1.00 21.03 ? 172 ALA D CB  1 
ATOM   6381  N N   . ILE D 1 173 ? 8.057   25.720  -70.472  1.00 21.39 ? 173 ILE D N   1 
ATOM   6382  C CA  . ILE D 1 173 ? 9.168   26.643  -70.661  1.00 21.71 ? 173 ILE D CA  1 
ATOM   6383  C C   . ILE D 1 173 ? 9.487   27.398  -69.373  1.00 22.18 ? 173 ILE D C   1 
ATOM   6384  O O   . ILE D 1 173 ? 10.652  27.549  -69.016  1.00 22.76 ? 173 ILE D O   1 
ATOM   6385  C CB  . ILE D 1 173 ? 8.856   27.638  -71.803  1.00 21.46 ? 173 ILE D CB  1 
ATOM   6386  C CG1 . ILE D 1 173 ? 8.807   26.903  -73.153  1.00 21.74 ? 173 ILE D CG1 1 
ATOM   6387  C CG2 . ILE D 1 173 ? 9.873   28.773  -71.846  1.00 21.51 ? 173 ILE D CG2 1 
ATOM   6388  C CD1 . ILE D 1 173 ? 10.136  26.295  -73.592  1.00 21.65 ? 173 ILE D CD1 1 
ATOM   6389  N N   . ALA D 1 174 ? 8.451   27.876  -68.689  1.00 22.39 ? 174 ALA D N   1 
ATOM   6390  C CA  . ALA D 1 174 ? 8.615   28.608  -67.435  1.00 22.61 ? 174 ALA D CA  1 
ATOM   6391  C C   . ALA D 1 174 ? 9.237   27.720  -66.376  1.00 22.81 ? 174 ALA D C   1 
ATOM   6392  O O   . ALA D 1 174 ? 10.196  28.110  -65.699  1.00 21.59 ? 174 ALA D O   1 
ATOM   6393  C CB  . ALA D 1 174 ? 7.276   29.130  -66.950  1.00 22.55 ? 174 ALA D CB  1 
ATOM   6394  N N   . GLU D 1 175 ? 8.677   26.525  -66.259  1.00 24.83 ? 175 GLU D N   1 
ATOM   6395  C CA  . GLU D 1 175 ? 9.171   25.494  -65.349  1.00 27.34 ? 175 GLU D CA  1 
ATOM   6396  C C   . GLU D 1 175 ? 10.634  25.160  -65.661  1.00 24.24 ? 175 GLU D C   1 
ATOM   6397  O O   . GLU D 1 175 ? 11.445  25.071  -64.748  1.00 21.94 ? 175 GLU D O   1 
ATOM   6398  C CB  . GLU D 1 175 ? 8.318   24.230  -65.452  1.00 31.99 ? 175 GLU D CB  1 
ATOM   6399  C CG  . GLU D 1 175 ? 7.843   23.661  -64.125  1.00 37.34 ? 175 GLU D CG  1 
ATOM   6400  C CD  . GLU D 1 175 ? 6.470   23.003  -64.270  1.00 42.30 ? 175 GLU D CD  1 
ATOM   6401  O OE1 . GLU D 1 175 ? 6.448   21.783  -64.642  1.00 44.49 ? 175 GLU D OE1 1 
ATOM   6402  O OE2 . GLU D 1 175 ? 5.417   23.693  -64.013  1.00 39.73 ? 175 GLU D OE2 1 
ATOM   6403  N N   . ALA D 1 176 ? 10.970  25.002  -66.943  1.00 22.30 ? 176 ALA D N   1 
ATOM   6404  C CA  . ALA D 1 176 ? 12.340  24.667  -67.349  1.00 21.42 ? 176 ALA D CA  1 
ATOM   6405  C C   . ALA D 1 176 ? 13.325  25.733  -66.943  1.00 20.61 ? 176 ALA D C   1 
ATOM   6406  O O   . ALA D 1 176 ? 14.478  25.441  -66.668  1.00 20.90 ? 176 ALA D O   1 
ATOM   6407  C CB  . ALA D 1 176 ? 12.418  24.447  -68.854  1.00 21.27 ? 176 ALA D CB  1 
ATOM   6408  N N   . ALA D 1 177 ? 12.860  26.978  -66.912  1.00 20.28 ? 177 ALA D N   1 
ATOM   6409  C CA  . ALA D 1 177 ? 13.678  28.120  -66.521  1.00 19.44 ? 177 ALA D CA  1 
ATOM   6410  C C   . ALA D 1 177 ? 13.719  28.331  -65.010  1.00 18.88 ? 177 ALA D C   1 
ATOM   6411  O O   . ALA D 1 177 ? 14.355  29.268  -64.556  1.00 19.75 ? 177 ALA D O   1 
ATOM   6412  C CB  . ALA D 1 177 ? 13.137  29.365  -67.189  1.00 19.05 ? 177 ALA D CB  1 
ATOM   6413  N N   . GLY D 1 178 ? 13.036  27.491  -64.239  1.00 18.18 ? 178 GLY D N   1 
ATOM   6414  C CA  . GLY D 1 178 ? 12.881  27.707  -62.803  1.00 18.01 ? 178 GLY D CA  1 
ATOM   6415  C C   . GLY D 1 178 ? 12.123  28.973  -62.424  1.00 17.88 ? 178 GLY D C   1 
ATOM   6416  O O   . GLY D 1 178 ? 12.487  29.651  -61.468  1.00 18.07 ? 178 GLY D O   1 
ATOM   6417  N N   . GLU D 1 179 ? 11.074  29.287  -63.180  1.00 17.99 ? 179 GLU D N   1 
ATOM   6418  C CA  . GLU D 1 179 ? 10.301  30.521  -63.003  1.00 17.86 ? 179 GLU D CA  1 
ATOM   6419  C C   . GLU D 1 179 ? 8.811   30.171  -62.899  1.00 17.83 ? 179 GLU D C   1 
ATOM   6420  O O   . GLU D 1 179 ? 8.459   29.005  -62.901  1.00 18.28 ? 179 GLU D O   1 
ATOM   6421  C CB  . GLU D 1 179 ? 10.571  31.490  -64.161  1.00 17.59 ? 179 GLU D CB  1 
ATOM   6422  C CG  . GLU D 1 179 ? 12.039  31.881  -64.309  1.00 18.04 ? 179 GLU D CG  1 
ATOM   6423  C CD  . GLU D 1 179 ? 12.533  32.868  -63.254  1.00 18.84 ? 179 GLU D CD  1 
ATOM   6424  O OE1 . GLU D 1 179 ? 13.726  33.263  -63.285  1.00 18.65 ? 179 GLU D OE1 1 
ATOM   6425  O OE2 . GLU D 1 179 ? 11.742  33.268  -62.386  1.00 19.92 ? 179 GLU D OE2 1 
ATOM   6426  N N   . SER D 1 180 ? 7.938   31.163  -62.810  1.00 17.55 ? 180 SER D N   1 
ATOM   6427  C CA  . SER D 1 180 ? 6.530   30.904  -62.547  1.00 17.68 ? 180 SER D CA  1 
ATOM   6428  C C   . SER D 1 180 ? 5.645   31.071  -63.770  1.00 17.89 ? 180 SER D C   1 
ATOM   6429  O O   . SER D 1 180 ? 6.022   31.725  -64.741  1.00 17.17 ? 180 SER D O   1 
ATOM   6430  C CB  . SER D 1 180 ? 6.036   31.829  -61.447  1.00 17.83 ? 180 SER D CB  1 
ATOM   6431  O OG  . SER D 1 180 ? 6.959   31.852  -60.392  1.00 18.44 ? 180 SER D OG  1 
ATOM   6432  N N   . PHE D 1 181 ? 4.449   30.482  -63.687  1.00 18.57 ? 181 PHE D N   1 
ATOM   6433  C CA  . PHE D 1 181 ? 3.487   30.470  -64.786  1.00 19.15 ? 181 PHE D CA  1 
ATOM   6434  C C   . PHE D 1 181 ? 2.069   30.773  -64.330  1.00 19.64 ? 181 PHE D C   1 
ATOM   6435  O O   . PHE D 1 181 ? 1.699   30.435  -63.214  1.00 20.41 ? 181 PHE D O   1 
ATOM   6436  C CB  . PHE D 1 181 ? 3.475   29.104  -65.465  1.00 18.90 ? 181 PHE D CB  1 
ATOM   6437  C CG  . PHE D 1 181 ? 2.345   28.934  -66.426  1.00 18.61 ? 181 PHE D CG  1 
ATOM   6438  C CD1 . PHE D 1 181 ? 2.335   29.648  -67.622  1.00 18.97 ? 181 PHE D CD1 1 
ATOM   6439  C CD2 . PHE D 1 181 ? 1.285   28.113  -66.135  1.00 18.55 ? 181 PHE D CD2 1 
ATOM   6440  C CE1 . PHE D 1 181 ? 1.285   29.526  -68.508  1.00 19.34 ? 181 PHE D CE1 1 
ATOM   6441  C CE2 . PHE D 1 181 ? 0.229   27.982  -67.024  1.00 18.95 ? 181 PHE D CE2 1 
ATOM   6442  C CZ  . PHE D 1 181 ? 0.229   28.690  -68.209  1.00 19.21 ? 181 PHE D CZ  1 
ATOM   6443  N N   . PHE D 1 182 ? 1.283   31.402  -65.200  1.00 19.96 ? 182 PHE D N   1 
ATOM   6444  C CA  . PHE D 1 182 ? -0.147  31.581  -64.959  1.00 20.60 ? 182 PHE D CA  1 
ATOM   6445  C C   . PHE D 1 182 ? -0.898  31.682  -66.277  1.00 20.57 ? 182 PHE D C   1 
ATOM   6446  O O   . PHE D 1 182 ? -0.474  32.397  -67.184  1.00 21.60 ? 182 PHE D O   1 
ATOM   6447  C CB  . PHE D 1 182 ? -0.412  32.825  -64.113  1.00 20.49 ? 182 PHE D CB  1 
ATOM   6448  C CG  . PHE D 1 182 ? -1.868  33.052  -63.803  1.00 20.25 ? 182 PHE D CG  1 
ATOM   6449  C CD1 . PHE D 1 182 ? -2.495  32.355  -62.778  1.00 19.83 ? 182 PHE D CD1 1 
ATOM   6450  C CD2 . PHE D 1 182 ? -2.610  33.970  -64.540  1.00 20.54 ? 182 PHE D CD2 1 
ATOM   6451  C CE1 . PHE D 1 182 ? -3.837  32.569  -62.491  1.00 20.21 ? 182 PHE D CE1 1 
ATOM   6452  C CE2 . PHE D 1 182 ? -3.952  34.193  -64.257  1.00 20.77 ? 182 PHE D CE2 1 
ATOM   6453  C CZ  . PHE D 1 182 ? -4.572  33.503  -63.222  1.00 20.54 ? 182 PHE D CZ  1 
ATOM   6454  N N   . ASP D 1 183 ? -2.018  30.970  -66.372  1.00 19.49 ? 183 ASP D N   1 
ATOM   6455  C CA  . ASP D 1 183 ? -2.812  30.945  -67.592  1.00 18.94 ? 183 ASP D CA  1 
ATOM   6456  C C   . ASP D 1 183 ? -3.967  31.929  -67.490  1.00 18.61 ? 183 ASP D C   1 
ATOM   6457  O O   . ASP D 1 183 ? -4.943  31.684  -66.783  1.00 19.25 ? 183 ASP D O   1 
ATOM   6458  C CB  . ASP D 1 183 ? -3.341  29.534  -67.818  1.00 18.57 ? 183 ASP D CB  1 
ATOM   6459  C CG  . ASP D 1 183 ? -4.170  29.405  -69.075  1.00 18.03 ? 183 ASP D CG  1 
ATOM   6460  O OD1 . ASP D 1 183 ? -4.248  30.340  -69.877  1.00 16.73 ? 183 ASP D OD1 1 
ATOM   6461  O OD2 . ASP D 1 183 ? -4.757  28.329  -69.251  1.00 19.19 ? 183 ASP D OD2 1 
ATOM   6462  N N   . ALA D 1 184 ? -3.878  33.037  -68.208  1.00 18.21 ? 184 ALA D N   1 
ATOM   6463  C CA  . ALA D 1 184 ? -4.953  34.012  -68.194  1.00 18.30 ? 184 ALA D CA  1 
ATOM   6464  C C   . ALA D 1 184 ? -6.284  33.379  -68.622  1.00 19.10 ? 184 ALA D C   1 
ATOM   6465  O O   . ALA D 1 184 ? -7.355  33.785  -68.163  1.00 20.49 ? 184 ALA D O   1 
ATOM   6466  C CB  . ALA D 1 184 ? -4.610  35.182  -69.095  1.00 18.34 ? 184 ALA D CB  1 
ATOM   6467  N N   . GLY D 1 185 ? -6.216  32.373  -69.492  1.00 19.55 ? 185 GLY D N   1 
ATOM   6468  C CA  . GLY D 1 185 ? -7.399  31.632  -69.923  1.00 19.19 ? 185 GLY D CA  1 
ATOM   6469  C C   . GLY D 1 185 ? -8.135  30.881  -68.841  1.00 19.20 ? 185 GLY D C   1 
ATOM   6470  O O   . GLY D 1 185 ? -9.259  30.451  -69.056  1.00 20.78 ? 185 GLY D O   1 
ATOM   6471  N N   . SER D 1 186 ? -7.506  30.693  -67.684  1.00 18.94 ? 186 SER D N   1 
ATOM   6472  C CA  . SER D 1 186 ? -8.150  30.021  -66.550  1.00 18.07 ? 186 SER D CA  1 
ATOM   6473  C C   . SER D 1 186 ? -9.187  30.914  -65.845  1.00 17.82 ? 186 SER D C   1 
ATOM   6474  O O   . SER D 1 186 ? -10.035 30.404  -65.131  1.00 17.19 ? 186 SER D O   1 
ATOM   6475  C CB  . SER D 1 186 ? -7.102  29.535  -65.547  1.00 17.35 ? 186 SER D CB  1 
ATOM   6476  O OG  . SER D 1 186 ? -6.674  30.591  -64.713  1.00 17.05 ? 186 SER D OG  1 
ATOM   6477  N N   . VAL D 1 187 ? -9.103  32.231  -66.036  1.00 17.64 ? 187 VAL D N   1 
ATOM   6478  C CA  . VAL D 1 187 ? -10.008 33.174  -65.357  1.00 17.23 ? 187 VAL D CA  1 
ATOM   6479  C C   . VAL D 1 187 ? -10.752 34.137  -66.285  1.00 17.32 ? 187 VAL D C   1 
ATOM   6480  O O   . VAL D 1 187 ? -11.693 34.781  -65.843  1.00 16.59 ? 187 VAL D O   1 
ATOM   6481  C CB  . VAL D 1 187 ? -9.244  34.019  -64.303  1.00 17.47 ? 187 VAL D CB  1 
ATOM   6482  C CG1 . VAL D 1 187 ? -8.697  33.139  -63.192  1.00 17.51 ? 187 VAL D CG1 1 
ATOM   6483  C CG2 . VAL D 1 187 ? -8.073  34.781  -64.931  1.00 17.50 ? 187 VAL D CG2 1 
ATOM   6484  N N   . VAL D 1 188 ? -10.319 34.264  -67.546  1.00 17.36 ? 188 VAL D N   1 
ATOM   6485  C CA  . VAL D 1 188 ? -10.978 35.134  -68.539  1.00 17.44 ? 188 VAL D CA  1 
ATOM   6486  C C   . VAL D 1 188 ? -10.859 34.585  -69.963  1.00 18.15 ? 188 VAL D C   1 
ATOM   6487  O O   . VAL D 1 188 ? -10.092 33.655  -70.222  1.00 17.94 ? 188 VAL D O   1 
ATOM   6488  C CB  . VAL D 1 188 ? -10.377 36.562  -68.580  1.00 17.14 ? 188 VAL D CB  1 
ATOM   6489  C CG1 . VAL D 1 188 ? -10.380 37.217  -67.213  1.00 16.90 ? 188 VAL D CG1 1 
ATOM   6490  C CG2 . VAL D 1 188 ? -8.963  36.549  -69.158  1.00 16.97 ? 188 VAL D CG2 1 
ATOM   6491  N N   . SER D 1 189 ? -11.625 35.181  -70.877  1.00 18.98 ? 189 SER D N   1 
ATOM   6492  C CA  . SER D 1 189 ? -11.494 34.902  -72.311  1.00 19.83 ? 189 SER D CA  1 
ATOM   6493  C C   . SER D 1 189 ? -11.606 36.167  -73.137  1.00 20.32 ? 189 SER D C   1 
ATOM   6494  O O   . SER D 1 189 ? -11.964 37.227  -72.637  1.00 20.75 ? 189 SER D O   1 
ATOM   6495  C CB  . SER D 1 189 ? -12.493 33.850  -72.795  1.00 19.67 ? 189 SER D CB  1 
ATOM   6496  O OG  . SER D 1 189 ? -13.701 33.992  -72.109  1.00 19.58 ? 189 SER D OG  1 
ATOM   6497  N N   . THR D 1 190 ? -11.262 36.046  -74.410  1.00 20.85 ? 190 THR D N   1 
ATOM   6498  C CA  . THR D 1 190 ? -11.231 37.193  -75.312  1.00 21.29 ? 190 THR D CA  1 
ATOM   6499  C C   . THR D 1 190 ? -12.690 37.523  -75.683  1.00 21.15 ? 190 THR D C   1 
ATOM   6500  O O   . THR D 1 190 ? -13.282 36.955  -76.611  1.00 20.67 ? 190 THR D O   1 
ATOM   6501  C CB  . THR D 1 190 ? -10.364 36.906  -76.557  1.00 21.75 ? 190 THR D CB  1 
ATOM   6502  O OG1 . THR D 1 190 ? -9.083  36.411  -76.138  1.00 21.85 ? 190 THR D OG1 1 
ATOM   6503  C CG2 . THR D 1 190 ? -10.143 38.156  -77.343  1.00 22.33 ? 190 THR D CG2 1 
ATOM   6504  N N   . ASP D 1 191 ? -13.253 38.457  -74.925  1.00 21.00 ? 191 ASP D N   1 
ATOM   6505  C CA  . ASP D 1 191 ? -14.643 38.853  -75.060  1.00 21.07 ? 191 ASP D CA  1 
ATOM   6506  C C   . ASP D 1 191 ? -14.834 40.151  -75.848  1.00 21.73 ? 191 ASP D C   1 
ATOM   6507  O O   . ASP D 1 191 ? -15.958 40.608  -76.028  1.00 22.28 ? 191 ASP D O   1 
ATOM   6508  C CB  . ASP D 1 191 ? -15.271 39.012  -73.670  1.00 21.01 ? 191 ASP D CB  1 
ATOM   6509  C CG  . ASP D 1 191 ? -14.718 40.201  -72.907  1.00 20.57 ? 191 ASP D CG  1 
ATOM   6510  O OD1 . ASP D 1 191 ? -13.547 40.582  -73.151  1.00 20.56 ? 191 ASP D OD1 1 
ATOM   6511  O OD2 . ASP D 1 191 ? -15.454 40.741  -72.061  1.00 19.30 ? 191 ASP D OD2 1 
ATOM   6512  N N   . GLY D 1 192 ? -13.757 40.769  -76.308  1.00 22.47 ? 192 GLY D N   1 
ATOM   6513  C CA  . GLY D 1 192 ? -13.904 41.989  -77.091  1.00 22.80 ? 192 GLY D CA  1 
ATOM   6514  C C   . GLY D 1 192 ? -14.669 41.747  -78.377  1.00 22.57 ? 192 GLY D C   1 
ATOM   6515  O O   . GLY D 1 192 ? -14.611 40.646  -78.957  1.00 22.29 ? 192 GLY D O   1 
ATOM   6516  N N   . VAL D 1 193 ? -15.376 42.775  -78.835  1.00 21.73 ? 193 VAL D N   1 
ATOM   6517  C CA  . VAL D 1 193 ? -16.169 42.665  -80.061  1.00 20.81 ? 193 VAL D CA  1 
ATOM   6518  C C   . VAL D 1 193 ? -15.343 42.283  -81.292  1.00 20.92 ? 193 VAL D C   1 
ATOM   6519  O O   . VAL D 1 193 ? -15.866 41.639  -82.187  1.00 20.20 ? 193 VAL D O   1 
ATOM   6520  C CB  . VAL D 1 193 ? -16.989 43.959  -80.324  1.00 19.83 ? 193 VAL D CB  1 
ATOM   6521  C CG1 . VAL D 1 193 ? -16.099 45.093  -80.777  1.00 19.81 ? 193 VAL D CG1 1 
ATOM   6522  C CG2 . VAL D 1 193 ? -18.073 43.730  -81.347  1.00 19.20 ? 193 VAL D CG2 1 
ATOM   6523  N N   . ASP D 1 194 ? -14.062 42.665  -81.332  1.00 23.03 ? 194 ASP D N   1 
ATOM   6524  C CA  . ASP D 1 194 ? -13.213 42.379  -82.509  1.00 24.49 ? 194 ASP D CA  1 
ATOM   6525  C C   . ASP D 1 194 ? -12.580 40.983  -82.478  1.00 24.83 ? 194 ASP D C   1 
ATOM   6526  O O   . ASP D 1 194 ? -11.858 40.618  -83.400  1.00 26.55 ? 194 ASP D O   1 
ATOM   6527  C CB  . ASP D 1 194 ? -12.142 43.468  -82.726  1.00 25.15 ? 194 ASP D CB  1 
ATOM   6528  C CG  . ASP D 1 194 ? -11.212 43.674  -81.516  1.00 25.94 ? 194 ASP D CG  1 
ATOM   6529  O OD1 . ASP D 1 194 ? -11.188 42.808  -80.617  1.00 24.83 ? 194 ASP D OD1 1 
ATOM   6530  O OD2 . ASP D 1 194 ? -10.516 44.735  -81.466  1.00 26.98 ? 194 ASP D OD2 1 
ATOM   6531  N N   . GLY D 1 195 ? -12.841 40.218  -81.419  1.00 24.40 ? 195 GLY D N   1 
ATOM   6532  C CA  . GLY D 1 195 ? -12.324 38.855  -81.289  1.00 23.73 ? 195 GLY D CA  1 
ATOM   6533  C C   . GLY D 1 195 ? -10.860 38.737  -80.882  1.00 23.30 ? 195 GLY D C   1 
ATOM   6534  O O   . GLY D 1 195 ? -10.287 37.638  -80.925  1.00 22.28 ? 195 GLY D O   1 
ATOM   6535  N N   . ILE D 1 196 ? -10.253 39.856  -80.478  1.00 23.57 ? 196 ILE D N   1 
ATOM   6536  C CA  . ILE D 1 196 ? -8.836  39.877  -80.096  1.00 24.54 ? 196 ILE D CA  1 
ATOM   6537  C C   . ILE D 1 196 ? -8.553  40.530  -78.743  1.00 23.06 ? 196 ILE D C   1 
ATOM   6538  O O   . ILE D 1 196 ? -7.721  40.018  -77.987  1.00 22.33 ? 196 ILE D O   1 
ATOM   6539  C CB  . ILE D 1 196 ? -7.983  40.556  -81.182  1.00 26.23 ? 196 ILE D CB  1 
ATOM   6540  C CG1 . ILE D 1 196 ? -8.000  39.708  -82.463  1.00 27.45 ? 196 ILE D CG1 1 
ATOM   6541  C CG2 . ILE D 1 196 ? -6.536  40.757  -80.722  1.00 26.04 ? 196 ILE D CG2 1 
ATOM   6542  C CD1 . ILE D 1 196 ? -7.877  40.541  -83.714  1.00 28.89 ? 196 ILE D CD1 1 
ATOM   6543  N N   . HIS D 1 197 ? -9.231  41.636  -78.441  1.00 22.04 ? 197 HIS D N   1 
ATOM   6544  C CA  . HIS D 1 197 ? -8.916  42.436  -77.251  1.00 22.37 ? 197 HIS D CA  1 
ATOM   6545  C C   . HIS D 1 197 ? -9.959  42.322  -76.155  1.00 21.41 ? 197 HIS D C   1 
ATOM   6546  O O   . HIS D 1 197 ? -10.937 41.602  -76.307  1.00 21.09 ? 197 HIS D O   1 
ATOM   6547  C CB  . HIS D 1 197 ? -8.721  43.885  -77.665  1.00 23.08 ? 197 HIS D CB  1 
ATOM   6548  C CG  . HIS D 1 197 ? -7.734  44.031  -78.766  1.00 23.89 ? 197 HIS D CG  1 
ATOM   6549  N ND1 . HIS D 1 197 ? -8.106  44.231  -80.074  1.00 25.17 ? 197 HIS D ND1 1 
ATOM   6550  C CD2 . HIS D 1 197 ? -6.387  43.931  -78.763  1.00 24.50 ? 197 HIS D CD2 1 
ATOM   6551  C CE1 . HIS D 1 197 ? -7.019  44.287  -80.828  1.00 25.94 ? 197 HIS D CE1 1 
ATOM   6552  N NE2 . HIS D 1 197 ? -5.960  44.108  -80.056  1.00 25.00 ? 197 HIS D NE2 1 
ATOM   6553  N N   . PHE D 1 198 ? -9.704  43.000  -75.033  1.00 20.59 ? 198 PHE D N   1 
ATOM   6554  C CA  . PHE D 1 198 ? -10.471 42.793  -73.803  1.00 19.78 ? 198 PHE D CA  1 
ATOM   6555  C C   . PHE D 1 198 ? -11.372 43.965  -73.467  1.00 20.31 ? 198 PHE D C   1 
ATOM   6556  O O   . PHE D 1 198 ? -11.038 45.115  -73.704  1.00 20.80 ? 198 PHE D O   1 
ATOM   6557  C CB  . PHE D 1 198 ? -9.548  42.580  -72.591  1.00 18.87 ? 198 PHE D CB  1 
ATOM   6558  C CG  . PHE D 1 198 ? -8.633  41.378  -72.675  1.00 18.39 ? 198 PHE D CG  1 
ATOM   6559  C CD1 . PHE D 1 198 ? -8.853  40.336  -73.572  1.00 18.74 ? 198 PHE D CD1 1 
ATOM   6560  C CD2 . PHE D 1 198 ? -7.576  41.267  -71.785  1.00 17.89 ? 198 PHE D CD2 1 
ATOM   6561  C CE1 . PHE D 1 198 ? -8.024  39.225  -73.590  1.00 18.61 ? 198 PHE D CE1 1 
ATOM   6562  C CE2 . PHE D 1 198 ? -6.746  40.169  -71.789  1.00 17.64 ? 198 PHE D CE2 1 
ATOM   6563  C CZ  . PHE D 1 198 ? -6.966  39.141  -72.695  1.00 18.18 ? 198 PHE D CZ  1 
ATOM   6564  N N   . THR D 1 199 ? -12.516 43.662  -72.875  1.00 21.12 ? 199 THR D N   1 
ATOM   6565  C CA  . THR D 1 199 ? -13.391 44.670  -72.286  1.00 21.26 ? 199 THR D CA  1 
ATOM   6566  C C   . THR D 1 199 ? -12.838 45.058  -70.927  1.00 21.40 ? 199 THR D C   1 
ATOM   6567  O O   . THR D 1 199 ? -11.945 44.395  -70.394  1.00 20.88 ? 199 THR D O   1 
ATOM   6568  C CB  . THR D 1 199 ? -14.800 44.125  -72.047  1.00 21.04 ? 199 THR D CB  1 
ATOM   6569  O OG1 . THR D 1 199 ? -14.745 43.075  -71.068  1.00 21.63 ? 199 THR D OG1 1 
ATOM   6570  C CG2 . THR D 1 199 ? -15.409 43.611  -73.363  1.00 20.77 ? 199 THR D CG2 1 
ATOM   6571  N N   . ALA D 1 200 ? -13.382 46.129  -70.355  1.00 21.89 ? 200 ALA D N   1 
ATOM   6572  C CA  . ALA D 1 200 ? -12.986 46.565  -69.027  1.00 23.13 ? 200 ALA D CA  1 
ATOM   6573  C C   . ALA D 1 200 ? -13.357 45.536  -67.966  1.00 24.39 ? 200 ALA D C   1 
ATOM   6574  O O   . ALA D 1 200 ? -12.648 45.384  -66.973  1.00 25.87 ? 200 ALA D O   1 
ATOM   6575  C CB  . ALA D 1 200 ? -13.613 47.910  -68.717  1.00 23.23 ? 200 ALA D CB  1 
ATOM   6576  N N   . GLU D 1 201 ? -14.461 44.830  -68.171  1.00 27.09 ? 201 GLU D N   1 
ATOM   6577  C CA  . GLU D 1 201 ? -14.876 43.781  -67.238  1.00 29.26 ? 201 GLU D CA  1 
ATOM   6578  C C   . GLU D 1 201 ? -13.820 42.666  -67.207  1.00 25.91 ? 201 GLU D C   1 
ATOM   6579  O O   . GLU D 1 201 ? -13.478 42.178  -66.141  1.00 24.61 ? 201 GLU D O   1 
ATOM   6580  C CB  . GLU D 1 201 ? -16.274 43.218  -67.571  1.00 34.58 ? 201 GLU D CB  1 
ATOM   6581  C CG  . GLU D 1 201 ? -16.807 42.285  -66.459  1.00 39.91 ? 201 GLU D CG  1 
ATOM   6582  C CD  . GLU D 1 201 ? -18.177 41.663  -66.730  1.00 45.85 ? 201 GLU D CD  1 
ATOM   6583  O OE1 . GLU D 1 201 ? -18.380 40.436  -66.482  1.00 44.56 ? 201 GLU D OE1 1 
ATOM   6584  O OE2 . GLU D 1 201 ? -19.088 42.397  -67.176  1.00 51.97 ? 201 GLU D OE2 1 
ATOM   6585  N N   . THR D 1 202 ? -13.300 42.283  -68.370  1.00 23.79 ? 202 THR D N   1 
ATOM   6586  C CA  . THR D 1 202 ? -12.284 41.230  -68.457  1.00 22.34 ? 202 THR D CA  1 
ATOM   6587  C C   . THR D 1 202 ? -10.962 41.686  -67.846  1.00 21.65 ? 202 THR D C   1 
ATOM   6588  O O   . THR D 1 202 ? -10.276 40.911  -67.172  1.00 21.30 ? 202 THR D O   1 
ATOM   6589  C CB  . THR D 1 202 ? -12.060 40.776  -69.910  1.00 21.66 ? 202 THR D CB  1 
ATOM   6590  O OG1 . THR D 1 202 ? -13.185 40.019  -70.338  1.00 21.11 ? 202 THR D OG1 1 
ATOM   6591  C CG2 . THR D 1 202 ? -10.805 39.913  -70.034  1.00 21.89 ? 202 THR D CG2 1 
ATOM   6592  N N   . ASN D 1 203 ? -10.605 42.944  -68.089  1.00 21.18 ? 203 ASN D N   1 
ATOM   6593  C CA  . ASN D 1 203 ? -9.419  43.523  -67.468  1.00 20.60 ? 203 ASN D CA  1 
ATOM   6594  C C   . ASN D 1 203 ? -9.478  43.414  -65.948  1.00 20.46 ? 203 ASN D C   1 
ATOM   6595  O O   . ASN D 1 203 ? -8.514  43.001  -65.310  1.00 20.97 ? 203 ASN D O   1 
ATOM   6596  C CB  . ASN D 1 203 ? -9.259  44.991  -67.858  1.00 19.87 ? 203 ASN D CB  1 
ATOM   6597  C CG  . ASN D 1 203 ? -8.669  45.180  -69.254  1.00 19.39 ? 203 ASN D CG  1 
ATOM   6598  O OD1 . ASN D 1 203 ? -8.176  44.246  -69.895  1.00 18.05 ? 203 ASN D OD1 1 
ATOM   6599  N ND2 . ASN D 1 203 ? -8.720  46.419  -69.728  1.00 19.32 ? 203 ASN D ND2 1 
ATOM   6600  N N   . ARG D 1 204 ? -10.620 43.796  -65.385  1.00 21.25 ? 204 ARG D N   1 
ATOM   6601  C CA  . ARG D 1 204 ? -10.839 43.765  -63.936  1.00 21.31 ? 204 ARG D CA  1 
ATOM   6602  C C   . ARG D 1 204 ? -10.632 42.375  -63.359  1.00 20.06 ? 204 ARG D C   1 
ATOM   6603  O O   . ARG D 1 204 ? -9.937  42.218  -62.351  1.00 20.51 ? 204 ARG D O   1 
ATOM   6604  C CB  . ARG D 1 204 ? -12.229 44.298  -63.563  1.00 23.07 ? 204 ARG D CB  1 
ATOM   6605  C CG  . ARG D 1 204 ? -12.265 45.796  -63.271  1.00 25.71 ? 204 ARG D CG  1 
ATOM   6606  C CD  . ARG D 1 204 ? -13.640 46.252  -62.793  1.00 29.10 ? 204 ARG D CD  1 
ATOM   6607  N NE  . ARG D 1 204 ? -14.604 46.424  -63.892  1.00 30.86 ? 204 ARG D NE  1 
ATOM   6608  C CZ  . ARG D 1 204 ? -14.662 47.494  -64.685  1.00 31.55 ? 204 ARG D CZ  1 
ATOM   6609  N NH1 . ARG D 1 204 ? -13.825 48.511  -64.544  1.00 33.05 ? 204 ARG D NH1 1 
ATOM   6610  N NH2 . ARG D 1 204 ? -15.557 47.554  -65.653  1.00 30.50 ? 204 ARG D NH2 1 
ATOM   6611  N N   . THR D 1 205 ? -11.222 41.368  -63.996  1.00 18.31 ? 205 THR D N   1 
ATOM   6612  C CA  . THR D 1 205 ? -11.084 39.997  -63.527  1.00 17.38 ? 205 THR D CA  1 
ATOM   6613  C C   . THR D 1 205 ? -9.614  39.578  -63.529  1.00 17.05 ? 205 THR D C   1 
ATOM   6614  O O   . THR D 1 205 ? -9.111  39.038  -62.530  1.00 16.97 ? 205 THR D O   1 
ATOM   6615  C CB  . THR D 1 205 ? -11.902 39.022  -64.389  1.00 17.20 ? 205 THR D CB  1 
ATOM   6616  O OG1 . THR D 1 205 ? -13.230 39.502  -64.543  1.00 16.50 ? 205 THR D OG1 1 
ATOM   6617  C CG2 . THR D 1 205 ? -11.940 37.632  -63.772  1.00 17.36 ? 205 THR D CG2 1 
ATOM   6618  N N   . LEU D 1 206 ? -8.933  39.849  -64.644  1.00 17.14 ? 206 LEU D N   1 
ATOM   6619  C CA  . LEU D 1 206 ? -7.535  39.460  -64.828  1.00 17.47 ? 206 LEU D CA  1 
ATOM   6620  C C   . LEU D 1 206 ? -6.623  40.139  -63.820  1.00 17.78 ? 206 LEU D C   1 
ATOM   6621  O O   . LEU D 1 206 ? -5.760  39.484  -63.222  1.00 18.60 ? 206 LEU D O   1 
ATOM   6622  C CB  . LEU D 1 206 ? -7.060  39.789  -66.253  1.00 17.55 ? 206 LEU D CB  1 
ATOM   6623  C CG  . LEU D 1 206 ? -5.630  39.398  -66.635  1.00 17.46 ? 206 LEU D CG  1 
ATOM   6624  C CD1 . LEU D 1 206 ? -5.419  37.921  -66.428  1.00 17.72 ? 206 LEU D CD1 1 
ATOM   6625  C CD2 . LEU D 1 206 ? -5.340  39.760  -68.080  1.00 17.52 ? 206 LEU D CD2 1 
ATOM   6626  N N   . GLY D 1 207 ? -6.813  41.447  -63.642  1.00 17.81 ? 207 GLY D N   1 
ATOM   6627  C CA  . GLY D 1 207 ? -6.019  42.217  -62.708  1.00 18.05 ? 207 GLY D CA  1 
ATOM   6628  C C   . GLY D 1 207 ? -6.080  41.652  -61.303  1.00 18.40 ? 207 GLY D C   1 
ATOM   6629  O O   . GLY D 1 207 ? -5.046  41.510  -60.628  1.00 17.82 ? 207 GLY D O   1 
ATOM   6630  N N   . ALA D 1 208 ? -7.299  41.317  -60.876  1.00 19.05 ? 208 ALA D N   1 
ATOM   6631  C CA  . ALA D 1 208 ? -7.524  40.808  -59.527  1.00 19.74 ? 208 ALA D CA  1 
ATOM   6632  C C   . ALA D 1 208 ? -6.929  39.413  -59.353  1.00 20.08 ? 208 ALA D C   1 
ATOM   6633  O O   . ALA D 1 208 ? -6.334  39.130  -58.308  1.00 21.34 ? 208 ALA D O   1 
ATOM   6634  C CB  . ALA D 1 208 ? -9.006  40.804  -59.190  1.00 19.34 ? 208 ALA D CB  1 
ATOM   6635  N N   . ALA D 1 209 ? -7.078  38.569  -60.376  1.00 19.90 ? 209 ALA D N   1 
ATOM   6636  C CA  . ALA D 1 209 ? -6.549  37.211  -60.340  1.00 19.94 ? 209 ALA D CA  1 
ATOM   6637  C C   . ALA D 1 209 ? -5.031  37.216  -60.321  1.00 20.12 ? 209 ALA D C   1 
ATOM   6638  O O   . ALA D 1 209 ? -4.411  36.477  -59.543  1.00 21.10 ? 209 ALA D O   1 
ATOM   6639  C CB  . ALA D 1 209 ? -7.038  36.398  -61.537  1.00 20.64 ? 209 ALA D CB  1 
ATOM   6640  N N   . VAL D 1 210 ? -4.430  38.039  -61.180  1.00 20.07 ? 210 VAL D N   1 
ATOM   6641  C CA  . VAL D 1 210 ? -2.969  38.092  -61.272  1.00 19.90 ? 210 VAL D CA  1 
ATOM   6642  C C   . VAL D 1 210 ? -2.350  38.644  -59.972  1.00 20.05 ? 210 VAL D C   1 
ATOM   6643  O O   . VAL D 1 210 ? -1.276  38.214  -59.566  1.00 20.39 ? 210 VAL D O   1 
ATOM   6644  C CB  . VAL D 1 210 ? -2.506  38.891  -62.511  1.00 19.42 ? 210 VAL D CB  1 
ATOM   6645  C CG1 . VAL D 1 210 ? -0.996  39.113  -62.497  1.00 19.61 ? 210 VAL D CG1 1 
ATOM   6646  C CG2 . VAL D 1 210 ? -2.907  38.159  -63.783  1.00 19.09 ? 210 VAL D CG2 1 
ATOM   6647  N N   . ALA D 1 211 ? -3.043  39.580  -59.322  1.00 20.43 ? 211 ALA D N   1 
ATOM   6648  C CA  . ALA D 1 211 ? -2.590  40.116  -58.051  1.00 20.86 ? 211 ALA D CA  1 
ATOM   6649  C C   . ALA D 1 211 ? -2.437  39.037  -56.972  1.00 21.70 ? 211 ALA D C   1 
ATOM   6650  O O   . ALA D 1 211 ? -1.488  39.071  -56.181  1.00 22.67 ? 211 ALA D O   1 
ATOM   6651  C CB  . ALA D 1 211 ? -3.532  41.205  -57.577  1.00 21.21 ? 211 ALA D CB  1 
ATOM   6652  N N   . GLN D 1 212 ? -3.359  38.084  -56.931  1.00 22.84 ? 212 GLN D N   1 
ATOM   6653  C CA  . GLN D 1 212 ? -3.246  36.948  -55.993  1.00 23.81 ? 212 GLN D CA  1 
ATOM   6654  C C   . GLN D 1 212 ? -2.000  36.162  -56.264  1.00 23.77 ? 212 GLN D C   1 
ATOM   6655  O O   . GLN D 1 212 ? -1.232  35.848  -55.354  1.00 23.56 ? 212 GLN D O   1 
ATOM   6656  C CB  . GLN D 1 212 ? -4.485  36.036  -56.077  1.00 24.14 ? 212 GLN D CB  1 
ATOM   6657  C CG  . GLN D 1 212 ? -5.801  36.721  -55.734  1.00 24.56 ? 212 GLN D CG  1 
ATOM   6658  C CD  . GLN D 1 212 ? -5.718  37.791  -54.642  1.00 24.50 ? 212 GLN D CD  1 
ATOM   6659  O OE1 . GLN D 1 212 ? -5.133  37.566  -53.582  1.00 25.79 ? 212 GLN D OE1 1 
ATOM   6660  N NE2 . GLN D 1 212 ? -6.286  38.958  -54.910  1.00 24.47 ? 212 GLN D NE2 1 
ATOM   6661  N N   . LYS D 1 213 ? -1.786  35.858  -57.534  1.00 24.79 ? 213 LYS D N   1 
ATOM   6662  C CA  . LYS D 1 213 ? -0.621  35.099  -57.955  1.00 24.97 ? 213 LYS D CA  1 
ATOM   6663  C C   . LYS D 1 213 ? 0.682   35.807  -57.568  1.00 25.76 ? 213 LYS D C   1 
ATOM   6664  O O   . LYS D 1 213 ? 1.606   35.184  -57.026  1.00 26.54 ? 213 LYS D O   1 
ATOM   6665  C CB  . LYS D 1 213 ? -0.699  34.861  -59.459  1.00 25.21 ? 213 LYS D CB  1 
ATOM   6666  C CG  . LYS D 1 213 ? 0.427   33.990  -59.997  1.00 26.69 ? 213 LYS D CG  1 
ATOM   6667  C CD  . LYS D 1 213 ? 0.514   32.636  -59.312  1.00 27.49 ? 213 LYS D CD  1 
ATOM   6668  C CE  . LYS D 1 213 ? 1.290   31.678  -60.193  1.00 28.73 ? 213 LYS D CE  1 
ATOM   6669  N NZ  . LYS D 1 213 ? 1.687   30.476  -59.440  1.00 29.51 ? 213 LYS D NZ  1 
ATOM   6670  N N   . VAL D 1 214 ? 0.747   37.108  -57.833  1.00 26.96 ? 214 VAL D N   1 
ATOM   6671  C CA  . VAL D 1 214 ? 1.939   37.893  -57.523  1.00 27.54 ? 214 VAL D CA  1 
ATOM   6672  C C   . VAL D 1 214 ? 2.295   37.825  -56.022  1.00 29.19 ? 214 VAL D C   1 
ATOM   6673  O O   . VAL D 1 214 ? 3.451   37.555  -55.669  1.00 28.93 ? 214 VAL D O   1 
ATOM   6674  C CB  . VAL D 1 214 ? 1.777   39.354  -57.964  1.00 26.92 ? 214 VAL D CB  1 
ATOM   6675  C CG1 . VAL D 1 214 ? 2.877   40.239  -57.382  1.00 28.28 ? 214 VAL D CG1 1 
ATOM   6676  C CG2 . VAL D 1 214 ? 1.782   39.452  -59.466  1.00 27.14 ? 214 VAL D CG2 1 
ATOM   6677  N N   . LYS D 1 215 ? 1.304   38.052  -55.158  1.00 30.70 ? 215 LYS D N   1 
ATOM   6678  C CA  . LYS D 1 215 ? 1.517   38.001  -53.711  1.00 32.74 ? 215 LYS D CA  1 
ATOM   6679  C C   . LYS D 1 215 ? 2.050   36.665  -53.223  1.00 32.11 ? 215 LYS D C   1 
ATOM   6680  O O   . LYS D 1 215 ? 2.883   36.616  -52.320  1.00 32.39 ? 215 LYS D O   1 
ATOM   6681  C CB  . LYS D 1 215 ? 0.230   38.314  -52.963  1.00 36.24 ? 215 LYS D CB  1 
ATOM   6682  C CG  . LYS D 1 215 ? -0.226  39.752  -53.030  1.00 38.43 ? 215 LYS D CG  1 
ATOM   6683  C CD  . LYS D 1 215 ? -1.599  39.856  -52.369  1.00 39.85 ? 215 LYS D CD  1 
ATOM   6684  C CE  . LYS D 1 215 ? -2.257  41.193  -52.620  1.00 40.70 ? 215 LYS D CE  1 
ATOM   6685  N NZ  . LYS D 1 215 ? -3.676  41.099  -52.181  1.00 42.22 ? 215 LYS D NZ  1 
ATOM   6686  N N   . THR D 1 216 ? 1.552   35.580  -53.809  1.00 32.52 ? 216 THR D N   1 
ATOM   6687  C CA  . THR D 1 216 ? 2.099   34.246  -53.570  1.00 32.54 ? 216 THR D CA  1 
ATOM   6688  C C   . THR D 1 216 ? 3.607   34.193  -53.815  1.00 31.89 ? 216 THR D C   1 
ATOM   6689  O O   . THR D 1 216 ? 4.329   33.551  -53.062  1.00 35.60 ? 216 THR D O   1 
ATOM   6690  C CB  . THR D 1 216 ? 1.396   33.212  -54.468  1.00 34.12 ? 216 THR D CB  1 
ATOM   6691  O OG1 . THR D 1 216 ? 0.055   33.041  -53.994  1.00 34.23 ? 216 THR D OG1 1 
ATOM   6692  C CG2 . THR D 1 216 ? 2.146   31.850  -54.510  1.00 33.88 ? 216 THR D CG2 1 
ATOM   6693  N N   . LEU D 1 217 ? 4.080   34.855  -54.869  1.00 29.43 ? 217 LEU D N   1 
ATOM   6694  C CA  . LEU D 1 217 ? 5.504   34.821  -55.224  1.00 27.16 ? 217 LEU D CA  1 
ATOM   6695  C C   . LEU D 1 217 ? 6.373   35.751  -54.384  1.00 25.93 ? 217 LEU D C   1 
ATOM   6696  O O   . LEU D 1 217 ? 7.490   35.405  -54.051  1.00 23.82 ? 217 LEU D O   1 
ATOM   6697  C CB  . LEU D 1 217 ? 5.681   35.152  -56.703  1.00 27.10 ? 217 LEU D CB  1 
ATOM   6698  C CG  . LEU D 1 217 ? 5.001   34.221  -57.712  1.00 26.67 ? 217 LEU D CG  1 
ATOM   6699  C CD1 . LEU D 1 217 ? 5.118   34.804  -59.110  1.00 26.59 ? 217 LEU D CD1 1 
ATOM   6700  C CD2 . LEU D 1 217 ? 5.558   32.812  -57.640  1.00 26.56 ? 217 LEU D CD2 1 
ATOM   6701  N N   . LEU D 1 218 ? 5.869   36.929  -54.037  1.00 26.33 ? 218 LEU D N   1 
ATOM   6702  C CA  . LEU D 1 218 ? 6.707   37.951  -53.401  1.00 25.73 ? 218 LEU D CA  1 
ATOM   6703  C C   . LEU D 1 218 ? 6.501   38.150  -51.886  1.00 27.12 ? 218 LEU D C   1 
ATOM   6704  O O   . LEU D 1 218 ? 7.241   38.889  -51.231  1.00 26.85 ? 218 LEU D O   1 
ATOM   6705  C CB  . LEU D 1 218 ? 6.508   39.284  -54.147  1.00 24.92 ? 218 LEU D CB  1 
ATOM   6706  C CG  . LEU D 1 218 ? 6.820   39.296  -55.641  1.00 24.67 ? 218 LEU D CG  1 
ATOM   6707  C CD1 . LEU D 1 218 ? 6.583   40.714  -56.153  1.00 24.37 ? 218 LEU D CD1 1 
ATOM   6708  C CD2 . LEU D 1 218 ? 8.226   38.813  -55.952  1.00 24.24 ? 218 LEU D CD2 1 
ATOM   6709  N N   . GLN D 1 219 ? 5.469   37.538  -51.332  1.00 29.22 ? 219 GLN D N   1 
ATOM   6710  C CA  . GLN D 1 219 ? 5.322   37.525  -49.889  1.00 30.72 ? 219 GLN D CA  1 
ATOM   6711  C C   . GLN D 1 219 ? 5.639   36.111  -49.366  1.00 32.11 ? 219 GLN D C   1 
ATOM   6712  O O   . GLN D 1 219 ? 4.892   35.157  -49.616  1.00 28.61 ? 219 GLN D O   1 
ATOM   6713  C CB  . GLN D 1 219 ? 3.996   38.123  -49.473  1.00 32.01 ? 219 GLN D CB  1 
ATOM   6714  C CG  . GLN D 1 219 ? 3.963   39.631  -49.711  1.00 32.27 ? 219 GLN D CG  1 
ATOM   6715  C CD  . GLN D 1 219 ? 2.545   40.241  -49.634  1.00 33.41 ? 219 GLN D CD  1 
ATOM   6716  O OE1 . GLN D 1 219 ? 2.314   41.294  -50.203  1.00 32.45 ? 219 GLN D OE1 1 
ATOM   6717  N NE2 . GLN D 1 219 ? 1.601   39.560  -48.993  1.00 34.39 ? 219 GLN D NE2 1 
ATOM   6718  N N   . PRO D 1 220 ? 6.846   35.966  -48.755  1.00 34.77 ? 220 PRO D N   1 
ATOM   6719  C CA  . PRO D 1 220 ? 7.371   34.625  -48.510  1.00 35.00 ? 220 PRO D CA  1 
ATOM   6720  C C   . PRO D 1 220 ? 6.623   33.831  -47.448  1.00 36.74 ? 220 PRO D C   1 
ATOM   6721  O O   . PRO D 1 220 ? 6.543   32.612  -47.572  1.00 36.85 ? 220 PRO D O   1 
ATOM   6722  C CB  . PRO D 1 220 ? 8.833   34.857  -48.131  1.00 34.81 ? 220 PRO D CB  1 
ATOM   6723  C CG  . PRO D 1 220 ? 9.058   36.326  -48.049  1.00 34.25 ? 220 PRO D CG  1 
ATOM   6724  C CD  . PRO D 1 220 ? 7.907   36.998  -48.697  1.00 34.35 ? 220 PRO D CD  1 
ATOM   6725  N N   . LYS D 1 221 ? 6.086   34.506  -46.428  1.00 39.41 ? 221 LYS D N   1 
ATOM   6726  C CA  . LYS D 1 221 ? 5.140   33.875  -45.487  1.00 41.44 ? 221 LYS D CA  1 
ATOM   6727  C C   . LYS D 1 221 ? 3.974   33.178  -46.205  1.00 48.07 ? 221 LYS D C   1 
ATOM   6728  O O   . LYS D 1 221 ? 3.564   32.083  -45.828  1.00 55.28 ? 221 LYS D O   1 
ATOM   6729  C CB  . LYS D 1 221 ? 4.603   34.895  -44.480  1.00 38.19 ? 221 LYS D CB  1 
ATOM   6730  C CG  . LYS D 1 221 ? 5.686   35.456  -43.567  1.00 36.58 ? 221 LYS D CG  1 
ATOM   6731  C CD  . LYS D 1 221 ? 5.277   35.475  -42.099  1.00 36.56 ? 221 LYS D CD  1 
ATOM   6732  C CE  . LYS D 1 221 ? 6.343   36.134  -41.248  1.00 35.96 ? 221 LYS D CE  1 
ATOM   6733  N NZ  . LYS D 1 221 ? 6.462   37.597  -41.524  1.00 34.91 ? 221 LYS D NZ  1 
ATOM   6734  N N   . LEU D 1 222 ? 3.454   33.809  -47.250  1.00 52.52 ? 222 LEU D N   1 
ATOM   6735  C CA  . LEU D 1 222 ? 2.396   33.208  -48.064  1.00 51.60 ? 222 LEU D CA  1 
ATOM   6736  C C   . LEU D 1 222 ? 2.966   32.116  -48.953  1.00 53.78 ? 222 LEU D C   1 
ATOM   6737  O O   . LEU D 1 222 ? 2.389   31.044  -49.065  1.00 52.17 ? 222 LEU D O   1 
ATOM   6738  C CB  . LEU D 1 222 ? 1.686   34.277  -48.902  1.00 49.90 ? 222 LEU D CB  1 
ATOM   6739  C CG  . LEU D 1 222 ? 0.715   35.216  -48.144  1.00 48.89 ? 222 LEU D CG  1 
ATOM   6740  C CD1 . LEU D 1 222 ? 1.185   35.653  -46.757  1.00 47.67 ? 222 LEU D CD1 1 
ATOM   6741  C CD2 . LEU D 1 222 ? 0.438   36.453  -48.977  1.00 49.50 ? 222 LEU D CD2 1 
ATOM   6742  N N   . ALA D 1 223 ? 4.098   32.384  -49.589  1.00 60.09 ? 223 ALA D N   1 
ATOM   6743  C CA  . ALA D 1 223 ? 4.769   31.355  -50.402  1.00 63.47 ? 223 ALA D CA  1 
ATOM   6744  C C   . ALA D 1 223 ? 4.970   30.092  -49.572  1.00 70.15 ? 223 ALA D C   1 
ATOM   6745  O O   . ALA D 1 223 ? 4.649   28.994  -50.021  1.00 79.47 ? 223 ALA D O   1 
ATOM   6746  C CB  . ALA D 1 223 ? 6.102   31.847  -50.943  1.00 58.50 ? 223 ALA D CB  1 
ATOM   6747  N N   . ALA D 1 224 ? 5.489   30.272  -48.356  1.00 71.15 ? 224 ALA D N   1 
ATOM   6748  C CA  . ALA D 1 224 ? 5.700   29.173  -47.405  1.00 69.89 ? 224 ALA D CA  1 
ATOM   6749  C C   . ALA D 1 224 ? 4.426   28.361  -47.183  1.00 72.48 ? 224 ALA D C   1 
ATOM   6750  O O   . ALA D 1 224 ? 4.423   27.163  -47.390  1.00 78.19 ? 224 ALA D O   1 
ATOM   6751  C CB  . ALA D 1 224 ? 6.214   29.715  -46.079  1.00 70.52 ? 224 ALA D CB  1 
ATOM   6752  N N   . ALA D 1 225 ? 3.364   29.036  -46.754  1.00 71.84 ? 225 ALA D N   1 
ATOM   6753  C CA  . ALA D 1 225 ? 2.046   28.432  -46.537  1.00 73.92 ? 225 ALA D CA  1 
ATOM   6754  C C   . ALA D 1 225 ? 1.540   27.573  -47.707  1.00 73.51 ? 225 ALA D C   1 
ATOM   6755  O O   . ALA D 1 225 ? 0.890   26.558  -47.470  1.00 72.01 ? 225 ALA D O   1 
ATOM   6756  C CB  . ALA D 1 225 ? 1.029   29.518  -46.208  1.00 70.83 ? 225 ALA D CB  1 
ATOM   6757  N N   . LEU D 1 226 ? 1.836   27.966  -48.944  1.00 73.11 ? 226 LEU D N   1 
ATOM   6758  C CA  . LEU D 1 226 ? 1.429   27.164  -50.114  1.00 77.75 ? 226 LEU D CA  1 
ATOM   6759  C C   . LEU D 1 226 ? 2.097   25.775  -50.196  1.00 81.37 ? 226 LEU D C   1 
ATOM   6760  O O   . LEU D 1 226 ? 1.457   24.821  -50.647  1.00 84.43 ? 226 LEU D O   1 
ATOM   6761  C CB  . LEU D 1 226 ? 1.622   27.920  -51.442  1.00 77.74 ? 226 LEU D CB  1 
ATOM   6762  C CG  . LEU D 1 226 ? 0.347   28.369  -52.198  1.00 74.78 ? 226 LEU D CG  1 
ATOM   6763  C CD1 . LEU D 1 226 ? -0.345  29.515  -51.466  1.00 71.53 ? 226 LEU D CD1 1 
ATOM   6764  C CD2 . LEU D 1 226 ? 0.659   28.726  -53.652  1.00 71.91 ? 226 LEU D CD2 1 
ATOM   6765  N N   . GLU D 1 227 ? 3.352   25.652  -49.767  1.00 81.56 ? 227 GLU D N   1 
ATOM   6766  C CA  . GLU D 1 227 ? 3.984   24.314  -49.664  1.00 79.71 ? 227 GLU D CA  1 
ATOM   6767  C C   . GLU D 1 227 ? 3.316   23.378  -48.626  1.00 83.56 ? 227 GLU D C   1 
ATOM   6768  O O   . GLU D 1 227 ? 3.259   22.165  -48.856  1.00 87.51 ? 227 GLU D O   1 
ATOM   6769  C CB  . GLU D 1 227 ? 5.487   24.436  -49.411  1.00 76.91 ? 227 GLU D CB  1 
ATOM   6770  C CG  . GLU D 1 227 ? 6.278   24.826  -50.654  1.00 76.70 ? 227 GLU D CG  1 
ATOM   6771  C CD  . GLU D 1 227 ? 7.438   25.786  -50.379  1.00 77.99 ? 227 GLU D CD  1 
ATOM   6772  O OE1 . GLU D 1 227 ? 8.010   26.319  -51.353  1.00 76.25 ? 227 GLU D OE1 1 
ATOM   6773  O OE2 . GLU D 1 227 ? 7.785   26.026  -49.201  1.00 79.23 ? 227 GLU D OE2 1 
ATOM   6774  N N   . HIS D 1 228 ? 2.769   23.926  -47.528  1.00 84.79 ? 228 HIS D N   1 
ATOM   6775  C CA  . HIS D 1 228 ? 2.077   23.107  -46.503  1.00 89.42 ? 228 HIS D CA  1 
ATOM   6776  C C   . HIS D 1 228 ? 1.663   21.744  -47.062  1.00 88.94 ? 228 HIS D C   1 
ATOM   6777  O O   . HIS D 1 228 ? 1.855   20.716  -46.412  1.00 89.45 ? 228 HIS D O   1 
ATOM   6778  C CB  . HIS D 1 228 ? 0.804   23.793  -45.961  1.00 91.97 ? 228 HIS D CB  1 
ATOM   6779  C CG  . HIS D 1 228 ? 1.021   24.662  -44.753  1.00 96.58 ? 228 HIS D CG  1 
ATOM   6780  N ND1 . HIS D 1 228 ? 0.422   25.900  -44.605  1.00 97.86 ? 228 HIS D ND1 1 
ATOM   6781  C CD2 . HIS D 1 228 ? 1.747   24.463  -43.627  1.00 96.15 ? 228 HIS D CD2 1 
ATOM   6782  C CE1 . HIS D 1 228 ? 0.780   26.430  -43.448  1.00 93.89 ? 228 HIS D CE1 1 
ATOM   6783  N NE2 . HIS D 1 228 ? 1.582   25.578  -42.834  1.00 97.99 ? 228 HIS D NE2 1 
ATOM   6784  N N   . ASP E 1 2   ? 10.840  -4.289  -97.076  1.00 74.66 ? 2   ASP E N   1 
ATOM   6785  C CA  . ASP E 1 2   ? 10.888  -3.550  -95.760  1.00 71.93 ? 2   ASP E CA  1 
ATOM   6786  C C   . ASP E 1 2   ? 11.744  -2.283  -95.796  1.00 63.40 ? 2   ASP E C   1 
ATOM   6787  O O   . ASP E 1 2   ? 12.965  -2.367  -95.901  1.00 61.47 ? 2   ASP E O   1 
ATOM   6788  C CB  . ASP E 1 2   ? 11.377  -4.473  -94.648  1.00 73.15 ? 2   ASP E CB  1 
ATOM   6789  C CG  . ASP E 1 2   ? 10.250  -5.277  -94.022  1.00 74.05 ? 2   ASP E CG  1 
ATOM   6790  O OD1 . ASP E 1 2   ? 9.214   -5.529  -94.690  1.00 72.16 ? 2   ASP E OD1 1 
ATOM   6791  O OD2 . ASP E 1 2   ? 10.400  -5.644  -92.841  1.00 73.37 ? 2   ASP E OD2 1 
ATOM   6792  N N   . LYS E 1 3   ? 11.060  -1.141  -95.746  1.00 56.24 ? 3   LYS E N   1 
ATOM   6793  C CA  . LYS E 1 3   ? 11.664  0.176   -95.919  1.00 51.49 ? 3   LYS E CA  1 
ATOM   6794  C C   . LYS E 1 3   ? 12.876  0.375   -94.990  1.00 45.89 ? 3   LYS E C   1 
ATOM   6795  O O   . LYS E 1 3   ? 12.807  0.063   -93.808  1.00 43.15 ? 3   LYS E O   1 
ATOM   6796  C CB  . LYS E 1 3   ? 10.589  1.240   -95.654  1.00 53.06 ? 3   LYS E CB  1 
ATOM   6797  C CG  . LYS E 1 3   ? 11.006  2.704   -95.821  1.00 53.81 ? 3   LYS E CG  1 
ATOM   6798  C CD  . LYS E 1 3   ? 10.285  3.633   -94.811  1.00 52.93 ? 3   LYS E CD  1 
ATOM   6799  C CE  . LYS E 1 3   ? 11.186  4.714   -94.196  1.00 52.34 ? 3   LYS E CE  1 
ATOM   6800  N NZ  . LYS E 1 3   ? 10.713  6.118   -94.455  1.00 51.82 ? 3   LYS E NZ  1 
ATOM   6801  N N   . ILE E 1 4   ? 13.998  0.849   -95.557  1.00 40.71 ? 4   ILE E N   1 
ATOM   6802  C CA  . ILE E 1 4   ? 15.202  1.110   -94.775  1.00 36.26 ? 4   ILE E CA  1 
ATOM   6803  C C   . ILE E 1 4   ? 15.009  2.444   -94.047  1.00 33.33 ? 4   ILE E C   1 
ATOM   6804  O O   . ILE E 1 4   ? 14.635  3.431   -94.652  1.00 32.99 ? 4   ILE E O   1 
ATOM   6805  C CB  . ILE E 1 4   ? 16.479  1.126   -95.631  1.00 36.47 ? 4   ILE E CB  1 
ATOM   6806  C CG1 . ILE E 1 4   ? 16.736  -0.293  -96.185  1.00 36.57 ? 4   ILE E CG1 1 
ATOM   6807  C CG2 . ILE E 1 4   ? 17.680  1.584   -94.812  1.00 36.39 ? 4   ILE E CG2 1 
ATOM   6808  C CD1 . ILE E 1 4   ? 17.898  -0.473  -97.143  1.00 36.55 ? 4   ILE E CD1 1 
ATOM   6809  N N   . LYS E 1 5   ? 15.271  2.461   -92.739  1.00 30.23 ? 5   LYS E N   1 
ATOM   6810  C CA  . LYS E 1 5   ? 15.037  3.644   -91.913  1.00 29.13 ? 5   LYS E CA  1 
ATOM   6811  C C   . LYS E 1 5   ? 16.234  4.589   -91.881  1.00 27.02 ? 5   LYS E C   1 
ATOM   6812  O O   . LYS E 1 5   ? 17.355  4.175   -91.570  1.00 26.79 ? 5   LYS E O   1 
ATOM   6813  C CB  . LYS E 1 5   ? 14.648  3.206   -90.507  1.00 30.80 ? 5   LYS E CB  1 
ATOM   6814  C CG  . LYS E 1 5   ? 13.222  2.710   -90.494  1.00 32.53 ? 5   LYS E CG  1 
ATOM   6815  C CD  . LYS E 1 5   ? 12.813  2.021   -89.220  1.00 35.36 ? 5   LYS E CD  1 
ATOM   6816  C CE  . LYS E 1 5   ? 11.284  1.864   -89.272  1.00 37.37 ? 5   LYS E CE  1 
ATOM   6817  N NZ  . LYS E 1 5   ? 10.797  0.558   -88.727  1.00 38.59 ? 5   LYS E NZ  1 
ATOM   6818  N N   . ARG E 1 6   ? 15.983  5.860   -92.182  1.00 24.03 ? 6   ARG E N   1 
ATOM   6819  C CA  . ARG E 1 6   ? 17.063  6.831   -92.337  1.00 22.18 ? 6   ARG E CA  1 
ATOM   6820  C C   . ARG E 1 6   ? 17.245  7.704   -91.084  1.00 20.62 ? 6   ARG E C   1 
ATOM   6821  O O   . ARG E 1 6   ? 16.309  8.370   -90.647  1.00 20.39 ? 6   ARG E O   1 
ATOM   6822  C CB  . ARG E 1 6   ? 16.812  7.674   -93.592  1.00 21.91 ? 6   ARG E CB  1 
ATOM   6823  C CG  . ARG E 1 6   ? 17.009  6.858   -94.873  1.00 22.23 ? 6   ARG E CG  1 
ATOM   6824  C CD  . ARG E 1 6   ? 16.560  7.592   -96.144  1.00 22.23 ? 6   ARG E CD  1 
ATOM   6825  N NE  . ARG E 1 6   ? 17.031  8.967   -96.237  1.00 22.39 ? 6   ARG E NE  1 
ATOM   6826  C CZ  . ARG E 1 6   ? 18.312  9.313   -96.413  1.00 23.64 ? 6   ARG E CZ  1 
ATOM   6827  N NH1 . ARG E 1 6   ? 19.286  8.384   -96.499  1.00 22.56 ? 6   ARG E NH1 1 
ATOM   6828  N NH2 . ARG E 1 6   ? 18.647  10.611  -96.487  1.00 24.72 ? 6   ARG E NH2 1 
ATOM   6829  N N   . VAL E 1 7   ? 18.446  7.686   -90.506  1.00 18.75 ? 7   VAL E N   1 
ATOM   6830  C CA  . VAL E 1 7   ? 18.753  8.472   -89.311  1.00 18.17 ? 7   VAL E CA  1 
ATOM   6831  C C   . VAL E 1 7   ? 19.841  9.517   -89.570  1.00 18.46 ? 7   VAL E C   1 
ATOM   6832  O O   . VAL E 1 7   ? 20.952  9.182   -89.962  1.00 19.22 ? 7   VAL E O   1 
ATOM   6833  C CB  . VAL E 1 7   ? 19.204  7.561   -88.154  1.00 17.52 ? 7   VAL E CB  1 
ATOM   6834  C CG1 . VAL E 1 7   ? 19.499  8.381   -86.887  1.00 17.26 ? 7   VAL E CG1 1 
ATOM   6835  C CG2 . VAL E 1 7   ? 18.170  6.470   -87.902  1.00 17.45 ? 7   VAL E CG2 1 
ATOM   6836  N N   . PHE E 1 8   ? 19.518  10.787  -89.342  1.00 18.50 ? 8   PHE E N   1 
ATOM   6837  C CA  . PHE E 1 8   ? 20.460  11.879  -89.524  1.00 18.13 ? 8   PHE E CA  1 
ATOM   6838  C C   . PHE E 1 8   ? 21.049  12.290  -88.187  1.00 18.30 ? 8   PHE E C   1 
ATOM   6839  O O   . PHE E 1 8   ? 20.312  12.570  -87.249  1.00 18.21 ? 8   PHE E O   1 
ATOM   6840  C CB  . PHE E 1 8   ? 19.747  13.057  -90.170  1.00 18.41 ? 8   PHE E CB  1 
ATOM   6841  C CG  . PHE E 1 8   ? 20.628  14.256  -90.391  1.00 18.77 ? 8   PHE E CG  1 
ATOM   6842  C CD1 . PHE E 1 8   ? 21.859  14.121  -91.026  1.00 18.99 ? 8   PHE E CD1 1 
ATOM   6843  C CD2 . PHE E 1 8   ? 20.232  15.526  -89.976  1.00 18.83 ? 8   PHE E CD2 1 
ATOM   6844  C CE1 . PHE E 1 8   ? 22.654  15.226  -91.236  1.00 19.13 ? 8   PHE E CE1 1 
ATOM   6845  C CE2 . PHE E 1 8   ? 21.028  16.627  -90.199  1.00 18.67 ? 8   PHE E CE2 1 
ATOM   6846  C CZ  . PHE E 1 8   ? 22.237  16.479  -90.825  1.00 18.88 ? 8   PHE E CZ  1 
ATOM   6847  N N   . VAL E 1 9   ? 22.374  12.308  -88.099  1.00 19.09 ? 9   VAL E N   1 
ATOM   6848  C CA  . VAL E 1 9   ? 23.074  12.680  -86.863  1.00 19.24 ? 9   VAL E CA  1 
ATOM   6849  C C   . VAL E 1 9   ? 23.764  14.027  -87.022  1.00 19.33 ? 9   VAL E C   1 
ATOM   6850  O O   . VAL E 1 9   ? 24.630  14.190  -87.882  1.00 20.63 ? 9   VAL E O   1 
ATOM   6851  C CB  . VAL E 1 9   ? 24.142  11.652  -86.474  1.00 19.52 ? 9   VAL E CB  1 
ATOM   6852  C CG1 . VAL E 1 9   ? 24.645  11.952  -85.065  1.00 20.21 ? 9   VAL E CG1 1 
ATOM   6853  C CG2 . VAL E 1 9   ? 23.580  10.239  -86.550  1.00 19.67 ? 9   VAL E CG2 1 
ATOM   6854  N N   . PHE E 1 10  ? 23.386  14.977  -86.178  1.00 18.72 ? 10  PHE E N   1 
ATOM   6855  C CA  . PHE E 1 10  ? 23.816  16.363  -86.297  1.00 18.36 ? 10  PHE E CA  1 
ATOM   6856  C C   . PHE E 1 10  ? 24.575  16.718  -85.035  1.00 18.57 ? 10  PHE E C   1 
ATOM   6857  O O   . PHE E 1 10  ? 23.988  16.768  -83.965  1.00 18.50 ? 10  PHE E O   1 
ATOM   6858  C CB  . PHE E 1 10  ? 22.586  17.252  -86.445  1.00 17.78 ? 10  PHE E CB  1 
ATOM   6859  C CG  . PHE E 1 10  ? 22.905  18.682  -86.802  1.00 17.57 ? 10  PHE E CG  1 
ATOM   6860  C CD1 . PHE E 1 10  ? 23.570  18.986  -87.979  1.00 17.27 ? 10  PHE E CD1 1 
ATOM   6861  C CD2 . PHE E 1 10  ? 22.508  19.727  -85.980  1.00 16.89 ? 10  PHE E CD2 1 
ATOM   6862  C CE1 . PHE E 1 10  ? 23.841  20.296  -88.316  1.00 16.66 ? 10  PHE E CE1 1 
ATOM   6863  C CE2 . PHE E 1 10  ? 22.773  21.037  -86.308  1.00 16.18 ? 10  PHE E CE2 1 
ATOM   6864  C CZ  . PHE E 1 10  ? 23.443  21.320  -87.477  1.00 16.64 ? 10  PHE E CZ  1 
ATOM   6865  N N   . GLY E 1 11  ? 25.877  16.942  -85.145  1.00 18.96 ? 11  GLY E N   1 
ATOM   6866  C CA  . GLY E 1 11  ? 26.691  17.204  -83.966  1.00 20.04 ? 11  GLY E CA  1 
ATOM   6867  C C   . GLY E 1 11  ? 27.917  18.058  -84.203  1.00 21.11 ? 11  GLY E C   1 
ATOM   6868  O O   . GLY E 1 11  ? 28.019  18.765  -85.208  1.00 20.48 ? 11  GLY E O   1 
ATOM   6869  N N   . ASP E 1 12  ? 28.851  17.968  -83.261  1.00 23.01 ? 12  ASP E N   1 
ATOM   6870  C CA  . ASP E 1 12  ? 30.055  18.793  -83.271  1.00 24.54 ? 12  ASP E CA  1 
ATOM   6871  C C   . ASP E 1 12  ? 31.258  17.872  -83.499  1.00 25.48 ? 12  ASP E C   1 
ATOM   6872  O O   . ASP E 1 12  ? 31.119  16.855  -84.169  1.00 24.67 ? 12  ASP E O   1 
ATOM   6873  C CB  . ASP E 1 12  ? 30.147  19.635  -81.980  1.00 24.98 ? 12  ASP E CB  1 
ATOM   6874  C CG  . ASP E 1 12  ? 29.876  18.822  -80.707  1.00 26.42 ? 12  ASP E CG  1 
ATOM   6875  O OD1 . ASP E 1 12  ? 30.092  17.574  -80.732  1.00 27.07 ? 12  ASP E OD1 1 
ATOM   6876  O OD2 . ASP E 1 12  ? 29.405  19.437  -79.706  1.00 26.08 ? 12  ASP E OD2 1 
HETATM 6877  N N   . SEP E 1 13  ? 32.422  18.214  -82.961  1.00 27.56 ? 13  SEP E N   1 
HETATM 6878  C CA  . SEP E 1 13  ? 33.657  17.460  -83.209  1.00 30.21 ? 13  SEP E CA  1 
HETATM 6879  C CB  . SEP E 1 13  ? 34.858  18.210  -82.620  1.00 36.30 ? 13  SEP E CB  1 
HETATM 6880  O OG  . SEP E 1 13  ? 34.517  18.648  -81.293  1.00 46.10 ? 13  SEP E OG  1 
HETATM 6881  C C   . SEP E 1 13  ? 33.566  16.080  -82.609  1.00 26.74 ? 13  SEP E C   1 
HETATM 6882  O O   . SEP E 1 13  ? 34.210  15.167  -83.089  1.00 26.36 ? 13  SEP E O   1 
HETATM 6883  P P   . SEP E 1 13  ? 34.319  20.131  -80.597  1.00 47.80 ? 13  SEP E P   1 
HETATM 6884  O O1P . SEP E 1 13  ? 33.392  20.902  -81.523  1.00 45.34 ? 13  SEP E O1P 1 
HETATM 6885  O O2P . SEP E 1 13  ? 33.569  19.716  -79.336  1.00 46.67 ? 13  SEP E O2P 1 
HETATM 6886  O O3P . SEP E 1 13  ? 35.678  20.808  -80.436  1.00 45.77 ? 13  SEP E O3P 1 
ATOM   6887  N N   . LEU E 1 14  ? 32.770  15.918  -81.557  1.00 24.37 ? 14  LEU E N   1 
ATOM   6888  C CA  . LEU E 1 14  ? 32.521  14.600  -80.969  1.00 23.42 ? 14  LEU E CA  1 
ATOM   6889  C C   . LEU E 1 14  ? 31.929  13.632  -81.984  1.00 22.35 ? 14  LEU E C   1 
ATOM   6890  O O   . LEU E 1 14  ? 32.176  12.437  -81.926  1.00 22.68 ? 14  LEU E O   1 
ATOM   6891  C CB  . LEU E 1 14  ? 31.558  14.699  -79.775  1.00 23.37 ? 14  LEU E CB  1 
ATOM   6892  C CG  . LEU E 1 14  ? 31.974  15.498  -78.540  1.00 23.13 ? 14  LEU E CG  1 
ATOM   6893  C CD1 . LEU E 1 14  ? 30.836  15.578  -77.516  1.00 22.93 ? 14  LEU E CD1 1 
ATOM   6894  C CD2 . LEU E 1 14  ? 33.198  14.863  -77.916  1.00 22.56 ? 14  LEU E CD2 1 
ATOM   6895  N N   . THR E 1 15  ? 31.127  14.167  -82.894  1.00 22.27 ? 15  THR E N   1 
ATOM   6896  C CA  . THR E 1 15  ? 30.439  13.396  -83.932  1.00 22.46 ? 15  THR E CA  1 
ATOM   6897  C C   . THR E 1 15  ? 31.262  13.335  -85.242  1.00 22.83 ? 15  THR E C   1 
ATOM   6898  O O   . THR E 1 15  ? 31.155  12.378  -86.002  1.00 22.70 ? 15  THR E O   1 
ATOM   6899  C CB  . THR E 1 15  ? 29.049  14.019  -84.180  1.00 21.96 ? 15  THR E CB  1 
ATOM   6900  O OG1 . THR E 1 15  ? 28.323  14.066  -82.942  1.00 21.45 ? 15  THR E OG1 1 
ATOM   6901  C CG2 . THR E 1 15  ? 28.271  13.250  -85.202  1.00 21.66 ? 15  THR E CG2 1 
ATOM   6902  N N   . TRP E 1 16  ? 32.069  14.361  -85.504  1.00 23.17 ? 16  TRP E N   1 
ATOM   6903  C CA  . TRP E 1 16  ? 33.052  14.332  -86.589  1.00 23.60 ? 16  TRP E CA  1 
ATOM   6904  C C   . TRP E 1 16  ? 34.060  13.210  -86.356  1.00 22.61 ? 16  TRP E C   1 
ATOM   6905  O O   . TRP E 1 16  ? 34.391  12.466  -87.269  1.00 20.79 ? 16  TRP E O   1 
ATOM   6906  C CB  . TRP E 1 16  ? 33.801  15.673  -86.672  1.00 23.91 ? 16  TRP E CB  1 
ATOM   6907  C CG  . TRP E 1 16  ? 34.872  15.769  -87.734  1.00 24.74 ? 16  TRP E CG  1 
ATOM   6908  C CD1 . TRP E 1 16  ? 34.680  15.838  -89.085  1.00 25.47 ? 16  TRP E CD1 1 
ATOM   6909  C CD2 . TRP E 1 16  ? 36.289  15.828  -87.537  1.00 25.02 ? 16  TRP E CD2 1 
ATOM   6910  N NE1 . TRP E 1 16  ? 35.888  15.920  -89.749  1.00 25.36 ? 16  TRP E NE1 1 
ATOM   6911  C CE2 . TRP E 1 16  ? 36.890  15.927  -88.816  1.00 26.08 ? 16  TRP E CE2 1 
ATOM   6912  C CE3 . TRP E 1 16  ? 37.112  15.814  -86.411  1.00 24.42 ? 16  TRP E CE3 1 
ATOM   6913  C CZ2 . TRP E 1 16  ? 38.273  16.000  -88.983  1.00 26.42 ? 16  TRP E CZ2 1 
ATOM   6914  C CZ3 . TRP E 1 16  ? 38.486  15.881  -86.586  1.00 24.40 ? 16  TRP E CZ3 1 
ATOM   6915  C CH2 . TRP E 1 16  ? 39.049  15.972  -87.853  1.00 25.52 ? 16  TRP E CH2 1 
ATOM   6916  N N   . GLY E 1 17  ? 34.543  13.122  -85.122  1.00 22.08 ? 17  GLY E N   1 
ATOM   6917  C CA  . GLY E 1 17  ? 35.537  12.130  -84.737  1.00 22.12 ? 17  GLY E CA  1 
ATOM   6918  C C   . GLY E 1 17  ? 36.869  12.728  -84.325  1.00 22.41 ? 17  GLY E C   1 
ATOM   6919  O O   . GLY E 1 17  ? 37.910  12.301  -84.814  1.00 23.25 ? 17  GLY E O   1 
ATOM   6920  N N   . TRP E 1 18  ? 36.846  13.705  -83.423  1.00 22.35 ? 18  TRP E N   1 
ATOM   6921  C CA  . TRP E 1 18  ? 38.071  14.326  -82.929  1.00 22.91 ? 18  TRP E CA  1 
ATOM   6922  C C   . TRP E 1 18  ? 38.865  13.335  -82.112  1.00 23.20 ? 18  TRP E C   1 
ATOM   6923  O O   . TRP E 1 18  ? 38.362  12.827  -81.120  1.00 22.43 ? 18  TRP E O   1 
ATOM   6924  C CB  . TRP E 1 18  ? 37.746  15.558  -82.087  1.00 23.08 ? 18  TRP E CB  1 
ATOM   6925  C CG  . TRP E 1 18  ? 38.928  16.374  -81.610  1.00 22.99 ? 18  TRP E CG  1 
ATOM   6926  C CD1 . TRP E 1 18  ? 39.949  15.954  -80.811  1.00 23.69 ? 18  TRP E CD1 1 
ATOM   6927  C CD2 . TRP E 1 18  ? 39.172  17.759  -81.868  1.00 23.20 ? 18  TRP E CD2 1 
ATOM   6928  N NE1 . TRP E 1 18  ? 40.829  16.980  -80.579  1.00 24.51 ? 18  TRP E NE1 1 
ATOM   6929  C CE2 . TRP E 1 18  ? 40.371  18.104  -81.217  1.00 23.81 ? 18  TRP E CE2 1 
ATOM   6930  C CE3 . TRP E 1 18  ? 38.498  18.744  -82.593  1.00 23.71 ? 18  TRP E CE3 1 
ATOM   6931  C CZ2 . TRP E 1 18  ? 40.908  19.397  -81.265  1.00 23.74 ? 18  TRP E CZ2 1 
ATOM   6932  C CZ3 . TRP E 1 18  ? 39.048  20.032  -82.651  1.00 23.76 ? 18  TRP E CZ3 1 
ATOM   6933  C CH2 . TRP E 1 18  ? 40.233  20.340  -81.988  1.00 23.52 ? 18  TRP E CH2 1 
ATOM   6934  N N   . THR E 1 19  ? 40.104  13.078  -82.532  1.00 24.71 ? 19  THR E N   1 
ATOM   6935  C CA  . THR E 1 19  ? 41.021  12.231  -81.783  1.00 26.21 ? 19  THR E CA  1 
ATOM   6936  C C   . THR E 1 19  ? 41.707  13.081  -80.709  1.00 27.62 ? 19  THR E C   1 
ATOM   6937  O O   . THR E 1 19  ? 42.429  14.023  -81.050  1.00 27.39 ? 19  THR E O   1 
ATOM   6938  C CB  . THR E 1 19  ? 42.097  11.601  -82.694  1.00 26.35 ? 19  THR E CB  1 
ATOM   6939  O OG1 . THR E 1 19  ? 41.474  10.816  -83.728  1.00 26.83 ? 19  THR E OG1 1 
ATOM   6940  C CG2 . THR E 1 19  ? 43.019  10.703  -81.880  1.00 25.69 ? 19  THR E CG2 1 
ATOM   6941  N N   . PRO E 1 20  ? 41.468  12.777  -79.408  1.00 29.68 ? 20  PRO E N   1 
ATOM   6942  C CA  . PRO E 1 20  ? 42.112  13.563  -78.346  1.00 31.21 ? 20  PRO E CA  1 
ATOM   6943  C C   . PRO E 1 20  ? 43.619  13.348  -78.320  1.00 32.84 ? 20  PRO E C   1 
ATOM   6944  O O   . PRO E 1 20  ? 44.078  12.201  -78.410  1.00 36.57 ? 20  PRO E O   1 
ATOM   6945  C CB  . PRO E 1 20  ? 41.462  13.038  -77.054  1.00 30.87 ? 20  PRO E CB  1 
ATOM   6946  C CG  . PRO E 1 20  ? 40.809  11.749  -77.407  1.00 30.01 ? 20  PRO E CG  1 
ATOM   6947  C CD  . PRO E 1 20  ? 40.526  11.775  -78.867  1.00 29.65 ? 20  PRO E CD  1 
ATOM   6948  N N   . VAL E 1 21  ? 44.376  14.438  -78.211  1.00 32.36 ? 21  VAL E N   1 
ATOM   6949  C CA  . VAL E 1 21  ? 45.837  14.391  -78.307  1.00 31.83 ? 21  VAL E CA  1 
ATOM   6950  C C   . VAL E 1 21  ? 46.495  15.494  -77.484  1.00 32.10 ? 21  VAL E C   1 
ATOM   6951  O O   . VAL E 1 21  ? 45.822  16.399  -76.974  1.00 30.94 ? 21  VAL E O   1 
ATOM   6952  C CB  . VAL E 1 21  ? 46.308  14.529  -79.774  1.00 31.47 ? 21  VAL E CB  1 
ATOM   6953  C CG1 . VAL E 1 21  ? 46.027  13.255  -80.552  1.00 31.58 ? 21  VAL E CG1 1 
ATOM   6954  C CG2 . VAL E 1 21  ? 45.650  15.720  -80.458  1.00 31.87 ? 21  VAL E CG2 1 
ATOM   6955  N N   . ALA E 1 22  ? 47.816  15.403  -77.356  1.00 31.45 ? 22  ALA E N   1 
ATOM   6956  C CA  . ALA E 1 22  ? 48.596  16.406  -76.648  1.00 30.81 ? 22  ALA E CA  1 
ATOM   6957  C C   . ALA E 1 22  ? 49.779  16.812  -77.534  1.00 31.30 ? 22  ALA E C   1 
ATOM   6958  O O   . ALA E 1 22  ? 50.527  15.941  -77.979  1.00 31.75 ? 22  ALA E O   1 
ATOM   6959  C CB  . ALA E 1 22  ? 49.074  15.860  -75.320  1.00 30.24 ? 22  ALA E CB  1 
ATOM   6960  N N   . PRO E 1 23  ? 49.934  18.105  -77.842  1.00 31.06 ? 23  PRO E N   1 
ATOM   6961  C CA  . PRO E 1 23  ? 48.995  19.150  -77.446  1.00 31.69 ? 23  PRO E CA  1 
ATOM   6962  C C   . PRO E 1 23  ? 47.625  19.009  -78.151  1.00 32.72 ? 23  PRO E C   1 
ATOM   6963  O O   . PRO E 1 23  ? 47.511  18.294  -79.168  1.00 32.88 ? 23  PRO E O   1 
ATOM   6964  C CB  . PRO E 1 23  ? 49.715  20.437  -77.886  1.00 30.73 ? 23  PRO E CB  1 
ATOM   6965  C CG  . PRO E 1 23  ? 50.674  20.015  -78.965  1.00 30.44 ? 23  PRO E CG  1 
ATOM   6966  C CD  . PRO E 1 23  ? 50.708  18.511  -79.028  1.00 30.07 ? 23  PRO E CD  1 
ATOM   6967  N N   . ILE E 1 24  ? 46.615  19.682  -77.591  1.00 32.99 ? 24  ILE E N   1 
ATOM   6968  C CA  . ILE E 1 24  ? 45.202  19.551  -78.021  1.00 31.68 ? 24  ILE E CA  1 
ATOM   6969  C C   . ILE E 1 24  ? 44.986  19.631  -79.525  1.00 30.46 ? 24  ILE E C   1 
ATOM   6970  O O   . ILE E 1 24  ? 44.148  18.887  -80.053  1.00 30.35 ? 24  ILE E O   1 
ATOM   6971  C CB  . ILE E 1 24  ? 44.275  20.568  -77.295  1.00 31.68 ? 24  ILE E CB  1 
ATOM   6972  C CG1 . ILE E 1 24  ? 42.810  20.352  -77.682  1.00 31.87 ? 24  ILE E CG1 1 
ATOM   6973  C CG2 . ILE E 1 24  ? 44.698  22.009  -77.560  1.00 31.99 ? 24  ILE E CG2 1 
ATOM   6974  C CD1 . ILE E 1 24  ? 41.841  21.131  -76.805  1.00 31.71 ? 24  ILE E CD1 1 
ATOM   6975  N N   . VAL E 1 25  ? 45.745  20.515  -80.190  1.00 29.00 ? 25  VAL E N   1 
ATOM   6976  C CA  . VAL E 1 25  ? 45.734  20.662  -81.661  1.00 28.90 ? 25  VAL E CA  1 
ATOM   6977  C C   . VAL E 1 25  ? 47.159  20.602  -82.215  1.00 27.99 ? 25  VAL E C   1 
ATOM   6978  O O   . VAL E 1 25  ? 48.098  20.951  -81.509  1.00 30.56 ? 25  VAL E O   1 
ATOM   6979  C CB  . VAL E 1 25  ? 45.095  22.018  -82.080  1.00 29.18 ? 25  VAL E CB  1 
ATOM   6980  C CG1 . VAL E 1 25  ? 43.642  22.095  -81.595  1.00 29.67 ? 25  VAL E CG1 1 
ATOM   6981  C CG2 . VAL E 1 25  ? 45.902  23.219  -81.588  1.00 28.31 ? 25  VAL E CG2 1 
ATOM   6982  N N   . PRO E 1 26  ? 47.357  20.169  -83.456  1.00 27.56 ? 26  PRO E N   1 
ATOM   6983  C CA  . PRO E 1 26  ? 46.294  19.711  -84.361  1.00 27.73 ? 26  PRO E CA  1 
ATOM   6984  C C   . PRO E 1 26  ? 45.896  18.267  -84.098  1.00 27.53 ? 26  PRO E C   1 
ATOM   6985  O O   . PRO E 1 26  ? 46.686  17.495  -83.533  1.00 28.08 ? 26  PRO E O   1 
ATOM   6986  C CB  . PRO E 1 26  ? 46.933  19.825  -85.745  1.00 27.33 ? 26  PRO E CB  1 
ATOM   6987  C CG  . PRO E 1 26  ? 48.385  19.665  -85.507  1.00 27.38 ? 26  PRO E CG  1 
ATOM   6988  C CD  . PRO E 1 26  ? 48.688  20.063  -84.075  1.00 27.85 ? 26  PRO E CD  1 
ATOM   6989  N N   . THR E 1 27  ? 44.678  17.919  -84.505  1.00 26.86 ? 27  THR E N   1 
ATOM   6990  C CA  . THR E 1 27  ? 44.169  16.551  -84.377  1.00 26.54 ? 27  THR E CA  1 
ATOM   6991  C C   . THR E 1 27  ? 44.020  15.925  -85.767  1.00 26.25 ? 27  THR E C   1 
ATOM   6992  O O   . THR E 1 27  ? 44.210  16.583  -86.797  1.00 24.73 ? 27  THR E O   1 
ATOM   6993  C CB  . THR E 1 27  ? 42.820  16.486  -83.617  1.00 26.49 ? 27  THR E CB  1 
ATOM   6994  O OG1 . THR E 1 27  ? 42.372  15.128  -83.497  1.00 26.95 ? 27  THR E OG1 1 
ATOM   6995  C CG2 . THR E 1 27  ? 41.760  17.291  -84.323  1.00 26.73 ? 27  THR E CG2 1 
ATOM   6996  N N   . THR E 1 28  ? 43.724  14.632  -85.764  1.00 25.68 ? 28  THR E N   1 
ATOM   6997  C CA  . THR E 1 28  ? 43.345  13.933  -86.968  1.00 25.95 ? 28  THR E CA  1 
ATOM   6998  C C   . THR E 1 28  ? 42.056  13.187  -86.653  1.00 25.84 ? 28  THR E C   1 
ATOM   6999  O O   . THR E 1 28  ? 41.749  12.917  -85.477  1.00 26.55 ? 28  THR E O   1 
ATOM   7000  C CB  . THR E 1 28  ? 44.429  12.947  -87.462  1.00 26.81 ? 28  THR E CB  1 
ATOM   7001  O OG1 . THR E 1 28  ? 44.452  11.803  -86.609  1.00 28.20 ? 28  THR E OG1 1 
ATOM   7002  C CG2 . THR E 1 28  ? 45.809  13.598  -87.512  1.00 26.80 ? 28  THR E CG2 1 
ATOM   7003  N N   . ARG E 1 29  ? 41.309  12.853  -87.704  1.00 25.04 ? 29  ARG E N   1 
ATOM   7004  C CA  . ARG E 1 29  ? 39.986  12.268  -87.548  1.00 24.31 ? 29  ARG E CA  1 
ATOM   7005  C C   . ARG E 1 29  ? 40.088  10.818  -87.120  1.00 24.55 ? 29  ARG E C   1 
ATOM   7006  O O   . ARG E 1 29  ? 40.850  10.053  -87.701  1.00 22.92 ? 29  ARG E O   1 
ATOM   7007  C CB  . ARG E 1 29  ? 39.210  12.359  -88.860  1.00 24.71 ? 29  ARG E CB  1 
ATOM   7008  C CG  . ARG E 1 29  ? 37.749  12.725  -88.656  1.00 26.19 ? 29  ARG E CG  1 
ATOM   7009  C CD  . ARG E 1 29  ? 36.801  11.871  -89.461  1.00 26.67 ? 29  ARG E CD  1 
ATOM   7010  N NE  . ARG E 1 29  ? 36.270  12.501  -90.672  1.00 26.89 ? 29  ARG E NE  1 
ATOM   7011  C CZ  . ARG E 1 29  ? 34.983  12.770  -90.902  1.00 26.74 ? 29  ARG E CZ  1 
ATOM   7012  N NH1 . ARG E 1 29  ? 34.044  12.518  -89.998  1.00 26.37 ? 29  ARG E NH1 1 
ATOM   7013  N NH2 . ARG E 1 29  ? 34.622  13.295  -92.057  1.00 27.79 ? 29  ARG E NH2 1 
ATOM   7014  N N   . HIS E 1 30  ? 39.333  10.429  -86.099  1.00 26.29 ? 30  HIS E N   1 
ATOM   7015  C CA  . HIS E 1 30  ? 39.237  9.011   -85.743  1.00 27.20 ? 30  HIS E CA  1 
ATOM   7016  C C   . HIS E 1 30  ? 38.988  8.215   -87.028  1.00 27.77 ? 30  HIS E C   1 
ATOM   7017  O O   . HIS E 1 30  ? 38.181  8.622   -87.875  1.00 28.65 ? 30  HIS E O   1 
ATOM   7018  C CB  . HIS E 1 30  ? 38.061  8.735   -84.793  1.00 27.17 ? 30  HIS E CB  1 
ATOM   7019  C CG  . HIS E 1 30  ? 38.369  8.964   -83.343  1.00 27.45 ? 30  HIS E CG  1 
ATOM   7020  N ND1 . HIS E 1 30  ? 39.242  8.170   -82.627  1.00 28.01 ? 30  HIS E ND1 1 
ATOM   7021  C CD2 . HIS E 1 30  ? 37.882  9.872   -82.464  1.00 26.62 ? 30  HIS E CD2 1 
ATOM   7022  C CE1 . HIS E 1 30  ? 39.292  8.596   -81.376  1.00 26.78 ? 30  HIS E CE1 1 
ATOM   7023  N NE2 . HIS E 1 30  ? 38.468  9.619   -81.250  1.00 25.92 ? 30  HIS E NE2 1 
ATOM   7024  N N   . PRO E 1 31  ? 39.683  7.075   -87.188  1.00 26.63 ? 31  PRO E N   1 
ATOM   7025  C CA  . PRO E 1 31  ? 39.323  6.190   -88.289  1.00 25.82 ? 31  PRO E CA  1 
ATOM   7026  C C   . PRO E 1 31  ? 37.831  5.859   -88.238  1.00 24.63 ? 31  PRO E C   1 
ATOM   7027  O O   . PRO E 1 31  ? 37.262  5.758   -87.150  1.00 23.55 ? 31  PRO E O   1 
ATOM   7028  C CB  . PRO E 1 31  ? 40.155  4.938   -88.028  1.00 25.98 ? 31  PRO E CB  1 
ATOM   7029  C CG  . PRO E 1 31  ? 41.275  5.374   -87.170  1.00 25.95 ? 31  PRO E CG  1 
ATOM   7030  C CD  . PRO E 1 31  ? 40.813  6.567   -86.399  1.00 26.39 ? 31  PRO E CD  1 
ATOM   7031  N N   . HIS E 1 32  ? 37.221  5.695   -89.403  1.00 24.10 ? 32  HIS E N   1 
ATOM   7032  C CA  . HIS E 1 32  ? 35.787  5.420   -89.500  1.00 25.92 ? 32  HIS E CA  1 
ATOM   7033  C C   . HIS E 1 32  ? 35.330  4.306   -88.544  1.00 25.91 ? 32  HIS E C   1 
ATOM   7034  O O   . HIS E 1 32  ? 34.306  4.425   -87.873  1.00 23.64 ? 32  HIS E O   1 
ATOM   7035  C CB  . HIS E 1 32  ? 35.422  5.072   -90.950  1.00 26.68 ? 32  HIS E CB  1 
ATOM   7036  C CG  . HIS E 1 32  ? 33.956  4.899   -91.186  1.00 26.67 ? 32  HIS E CG  1 
ATOM   7037  N ND1 . HIS E 1 32  ? 33.330  3.679   -91.064  1.00 27.47 ? 32  HIS E ND1 1 
ATOM   7038  C CD2 . HIS E 1 32  ? 33.002  5.782   -91.565  1.00 26.27 ? 32  HIS E CD2 1 
ATOM   7039  C CE1 . HIS E 1 32  ? 32.042  3.826   -91.339  1.00 28.18 ? 32  HIS E CE1 1 
ATOM   7040  N NE2 . HIS E 1 32  ? 31.818  5.095   -91.642  1.00 27.08 ? 32  HIS E NE2 1 
ATOM   7041  N N   . ALA E 1 33  ? 36.119  3.240   -88.470  1.00 27.08 ? 33  ALA E N   1 
ATOM   7042  C CA  . ALA E 1 33  ? 35.810  2.100   -87.600  1.00 28.25 ? 33  ALA E CA  1 
ATOM   7043  C C   . ALA E 1 33  ? 35.623  2.477   -86.118  1.00 27.90 ? 33  ALA E C   1 
ATOM   7044  O O   . ALA E 1 33  ? 34.900  1.807   -85.396  1.00 27.11 ? 33  ALA E O   1 
ATOM   7045  C CB  . ALA E 1 33  ? 36.891  1.037   -87.748  1.00 28.23 ? 33  ALA E CB  1 
ATOM   7046  N N   . ASP E 1 34  ? 36.274  3.554   -85.685  1.00 28.83 ? 34  ASP E N   1 
ATOM   7047  C CA  . ASP E 1 34  ? 36.270  3.990   -84.284  1.00 29.15 ? 34  ASP E CA  1 
ATOM   7048  C C   . ASP E 1 34  ? 35.292  5.127   -83.955  1.00 28.80 ? 34  ASP E C   1 
ATOM   7049  O O   . ASP E 1 34  ? 35.272  5.600   -82.814  1.00 27.82 ? 34  ASP E O   1 
ATOM   7050  C CB  . ASP E 1 34  ? 37.675  4.474   -83.893  1.00 30.03 ? 34  ASP E CB  1 
ATOM   7051  C CG  . ASP E 1 34  ? 38.722  3.391   -84.003  1.00 30.55 ? 34  ASP E CG  1 
ATOM   7052  O OD1 . ASP E 1 34  ? 38.370  2.206   -83.838  1.00 32.15 ? 34  ASP E OD1 1 
ATOM   7053  O OD2 . ASP E 1 34  ? 39.900  3.718   -84.257  1.00 29.93 ? 34  ASP E OD2 1 
ATOM   7054  N N   . ARG E 1 35  ? 34.507  5.593   -84.928  1.00 28.67 ? 35  ARG E N   1 
ATOM   7055  C CA  . ARG E 1 35  ? 33.583  6.719   -84.688  1.00 28.47 ? 35  ARG E CA  1 
ATOM   7056  C C   . ARG E 1 35  ? 32.277  6.250   -84.052  1.00 29.20 ? 35  ARG E C   1 
ATOM   7057  O O   . ARG E 1 35  ? 31.737  5.205   -84.431  1.00 30.20 ? 35  ARG E O   1 
ATOM   7058  C CB  . ARG E 1 35  ? 33.288  7.474   -85.983  1.00 28.49 ? 35  ARG E CB  1 
ATOM   7059  C CG  . ARG E 1 35  ? 34.497  8.142   -86.592  1.00 28.81 ? 35  ARG E CG  1 
ATOM   7060  C CD  . ARG E 1 35  ? 34.140  8.828   -87.896  1.00 29.59 ? 35  ARG E CD  1 
ATOM   7061  N NE  . ARG E 1 35  ? 35.318  8.897   -88.766  1.00 31.02 ? 35  ARG E NE  1 
ATOM   7062  C CZ  . ARG E 1 35  ? 35.283  9.046   -90.089  1.00 31.37 ? 35  ARG E CZ  1 
ATOM   7063  N NH1 . ARG E 1 35  ? 34.127  9.166   -90.737  1.00 30.22 ? 35  ARG E NH1 1 
ATOM   7064  N NH2 . ARG E 1 35  ? 36.425  9.073   -90.773  1.00 32.53 ? 35  ARG E NH2 1 
ATOM   7065  N N   . TRP E 1 36  ? 31.755  7.026   -83.101  1.00 29.26 ? 36  TRP E N   1 
ATOM   7066  C CA  . TRP E 1 36  ? 30.560  6.599   -82.353  1.00 28.68 ? 36  TRP E CA  1 
ATOM   7067  C C   . TRP E 1 36  ? 29.371  6.340   -83.284  1.00 29.29 ? 36  TRP E C   1 
ATOM   7068  O O   . TRP E 1 36  ? 28.652  5.354   -83.120  1.00 28.49 ? 36  TRP E O   1 
ATOM   7069  C CB  . TRP E 1 36  ? 30.212  7.585   -81.212  1.00 27.56 ? 36  TRP E CB  1 
ATOM   7070  C CG  . TRP E 1 36  ? 29.316  8.745   -81.549  1.00 26.43 ? 36  TRP E CG  1 
ATOM   7071  C CD1 . TRP E 1 36  ? 29.707  10.002  -81.916  1.00 26.15 ? 36  TRP E CD1 1 
ATOM   7072  C CD2 . TRP E 1 36  ? 27.890  8.761   -81.505  1.00 25.23 ? 36  TRP E CD2 1 
ATOM   7073  N NE1 . TRP E 1 36  ? 28.608  10.792  -82.121  1.00 26.88 ? 36  TRP E NE1 1 
ATOM   7074  C CE2 . TRP E 1 36  ? 27.477  10.054  -81.876  1.00 25.72 ? 36  TRP E CE2 1 
ATOM   7075  C CE3 . TRP E 1 36  ? 26.923  7.804   -81.202  1.00 25.20 ? 36  TRP E CE3 1 
ATOM   7076  C CZ2 . TRP E 1 36  ? 26.132  10.418  -81.960  1.00 25.54 ? 36  TRP E CZ2 1 
ATOM   7077  C CZ3 . TRP E 1 36  ? 25.577  8.173   -81.238  1.00 25.11 ? 36  TRP E CZ3 1 
ATOM   7078  C CH2 . TRP E 1 36  ? 25.202  9.468   -81.632  1.00 25.30 ? 36  TRP E CH2 1 
ATOM   7079  N N   . THR E 1 37  ? 29.207  7.212   -84.277  1.00 29.38 ? 37  THR E N   1 
ATOM   7080  C CA  . THR E 1 37  ? 28.173  7.067   -85.293  1.00 30.05 ? 37  THR E CA  1 
ATOM   7081  C C   . THR E 1 37  ? 28.317  5.774   -86.088  1.00 29.95 ? 37  THR E C   1 
ATOM   7082  O O   . THR E 1 37  ? 27.315  5.165   -86.460  1.00 29.40 ? 37  THR E O   1 
ATOM   7083  C CB  . THR E 1 37  ? 28.192  8.247   -86.288  1.00 30.41 ? 37  THR E CB  1 
ATOM   7084  O OG1 . THR E 1 37  ? 29.535  8.503   -86.714  1.00 30.26 ? 37  THR E OG1 1 
ATOM   7085  C CG2 . THR E 1 37  ? 27.650  9.482   -85.639  1.00 31.05 ? 37  THR E CG2 1 
ATOM   7086  N N   . THR E 1 38  ? 29.551  5.362   -86.361  1.00 29.95 ? 38  THR E N   1 
ATOM   7087  C CA  . THR E 1 38  ? 29.774  4.118   -87.085  1.00 31.48 ? 38  THR E CA  1 
ATOM   7088  C C   . THR E 1 38  ? 29.334  2.908   -86.269  1.00 30.04 ? 38  THR E C   1 
ATOM   7089  O O   . THR E 1 38  ? 28.656  2.011   -86.791  1.00 28.48 ? 38  THR E O   1 
ATOM   7090  C CB  . THR E 1 38  ? 31.240  3.965   -87.503  1.00 33.39 ? 38  THR E CB  1 
ATOM   7091  O OG1 . THR E 1 38  ? 31.563  5.008   -88.435  1.00 36.48 ? 38  THR E OG1 1 
ATOM   7092  C CG2 . THR E 1 38  ? 31.486  2.608   -88.157  1.00 32.70 ? 38  THR E CG2 1 
ATOM   7093  N N   . VAL E 1 39  ? 29.693  2.897   -84.990  1.00 29.11 ? 39  VAL E N   1 
ATOM   7094  C CA  . VAL E 1 39  ? 29.295  1.804   -84.119  1.00 28.18 ? 39  VAL E CA  1 
ATOM   7095  C C   . VAL E 1 39  ? 27.786  1.825   -83.949  1.00 27.47 ? 39  VAL E C   1 
ATOM   7096  O O   . VAL E 1 39  ? 27.169  0.775   -83.998  1.00 25.93 ? 39  VAL E O   1 
ATOM   7097  C CB  . VAL E 1 39  ? 30.013  1.861   -82.754  1.00 28.04 ? 39  VAL E CB  1 
ATOM   7098  C CG1 . VAL E 1 39  ? 29.456  0.812   -81.797  1.00 27.29 ? 39  VAL E CG1 1 
ATOM   7099  C CG2 . VAL E 1 39  ? 31.513  1.682   -82.946  1.00 27.32 ? 39  VAL E CG2 1 
ATOM   7100  N N   . LEU E 1 40  ? 27.204  3.012   -83.783  1.00 28.02 ? 40  LEU E N   1 
ATOM   7101  C CA  . LEU E 1 40  ? 25.745  3.154   -83.823  1.00 29.35 ? 40  LEU E CA  1 
ATOM   7102  C C   . LEU E 1 40  ? 25.133  2.459   -85.048  1.00 30.31 ? 40  LEU E C   1 
ATOM   7103  O O   . LEU E 1 40  ? 24.128  1.748   -84.939  1.00 29.96 ? 40  LEU E O   1 
ATOM   7104  C CB  . LEU E 1 40  ? 25.343  4.644   -83.830  1.00 28.02 ? 40  LEU E CB  1 
ATOM   7105  C CG  . LEU E 1 40  ? 23.880  4.965   -84.149  1.00 27.71 ? 40  LEU E CG  1 
ATOM   7106  C CD1 . LEU E 1 40  ? 22.945  4.474   -83.051  1.00 27.24 ? 40  LEU E CD1 1 
ATOM   7107  C CD2 . LEU E 1 40  ? 23.732  6.464   -84.362  1.00 28.02 ? 40  LEU E CD2 1 
ATOM   7108  N N   . GLY E 1 41  ? 25.738  2.684   -86.214  1.00 31.51 ? 41  GLY E N   1 
ATOM   7109  C CA  . GLY E 1 41  ? 25.251  2.106   -87.468  1.00 31.71 ? 41  GLY E CA  1 
ATOM   7110  C C   . GLY E 1 41  ? 25.339  0.597   -87.497  1.00 31.74 ? 41  GLY E C   1 
ATOM   7111  O O   . GLY E 1 41  ? 24.408  -0.075  -87.936  1.00 29.26 ? 41  GLY E O   1 
ATOM   7112  N N   . GLU E 1 42  ? 26.465  0.076   -87.017  1.00 32.82 ? 42  GLU E N   1 
ATOM   7113  C CA  . GLU E 1 42  ? 26.707  -1.370  -86.987  1.00 34.12 ? 42  GLU E CA  1 
ATOM   7114  C C   . GLU E 1 42  ? 25.785  -2.098  -86.048  1.00 33.16 ? 42  GLU E C   1 
ATOM   7115  O O   . GLU E 1 42  ? 25.284  -3.144  -86.395  1.00 31.39 ? 42  GLU E O   1 
ATOM   7116  C CB  . GLU E 1 42  ? 28.172  -1.667  -86.665  1.00 36.10 ? 42  GLU E CB  1 
ATOM   7117  C CG  . GLU E 1 42  ? 28.991  -1.728  -87.980  1.00 37.31 ? 42  GLU E CG  1 
ATOM   7118  C CD  . GLU E 1 42  ? 30.457  -1.363  -87.848  1.00 39.67 ? 42  GLU E CD  1 
ATOM   7119  O OE1 . GLU E 1 42  ? 31.041  -1.040  -88.891  1.00 39.60 ? 42  GLU E OE1 1 
ATOM   7120  O OE2 . GLU E 1 42  ? 31.000  -1.373  -86.721  1.00 41.12 ? 42  GLU E OE2 1 
ATOM   7121  N N   . ASN E 1 43  ? 25.555  -1.535  -84.874  1.00 34.71 ? 43  ASN E N   1 
ATOM   7122  C CA  . ASN E 1 43  ? 24.628  -2.127  -83.907  1.00 36.16 ? 43  ASN E CA  1 
ATOM   7123  C C   . ASN E 1 43  ? 23.170  -2.036  -84.316  1.00 36.45 ? 43  ASN E C   1 
ATOM   7124  O O   . ASN E 1 43  ? 22.344  -2.757  -83.769  1.00 39.71 ? 43  ASN E O   1 
ATOM   7125  C CB  . ASN E 1 43  ? 24.768  -1.463  -82.535  1.00 39.61 ? 43  ASN E CB  1 
ATOM   7126  C CG  . ASN E 1 43  ? 25.900  -2.017  -81.722  1.00 41.39 ? 43  ASN E CG  1 
ATOM   7127  O OD1 . ASN E 1 43  ? 25.665  -2.823  -80.862  1.00 45.37 ? 43  ASN E OD1 1 
ATOM   7128  N ND2 . ASN E 1 43  ? 27.119  -1.582  -81.987  1.00 43.98 ? 43  ASN E ND2 1 
ATOM   7129  N N   . LEU E 1 44  ? 22.838  -1.137  -85.242  1.00 35.85 ? 44  LEU E N   1 
ATOM   7130  C CA  . LEU E 1 44  ? 21.455  -1.002  -85.732  1.00 33.82 ? 44  LEU E CA  1 
ATOM   7131  C C   . LEU E 1 44  ? 21.132  -2.034  -86.800  1.00 32.96 ? 44  LEU E C   1 
ATOM   7132  O O   . LEU E 1 44  ? 20.013  -2.529  -86.861  1.00 32.36 ? 44  LEU E O   1 
ATOM   7133  C CB  . LEU E 1 44  ? 21.193  0.415   -86.258  1.00 33.12 ? 44  LEU E CB  1 
ATOM   7134  C CG  . LEU E 1 44  ? 20.869  1.502   -85.224  1.00 32.66 ? 44  LEU E CG  1 
ATOM   7135  C CD1 . LEU E 1 44  ? 20.832  2.886   -85.853  1.00 31.69 ? 44  LEU E CD1 1 
ATOM   7136  C CD2 . LEU E 1 44  ? 19.553  1.212   -84.528  1.00 33.03 ? 44  LEU E CD2 1 
ATOM   7137  N N   . GLY E 1 45  ? 22.109  -2.342  -87.645  1.00 35.35 ? 45  GLY E N   1 
ATOM   7138  C CA  . GLY E 1 45  ? 21.964  -3.360  -88.687  1.00 38.33 ? 45  GLY E CA  1 
ATOM   7139  C C   . GLY E 1 45  ? 21.543  -2.807  -90.030  1.00 41.63 ? 45  GLY E C   1 
ATOM   7140  O O   . GLY E 1 45  ? 21.443  -1.592  -90.211  1.00 44.15 ? 45  GLY E O   1 
ATOM   7141  N N   . ASP E 1 46  ? 21.280  -3.714  -90.975  1.00 43.64 ? 46  ASP E N   1 
ATOM   7142  C CA  . ASP E 1 46  ? 20.815  -3.359  -92.320  1.00 44.24 ? 46  ASP E CA  1 
ATOM   7143  C C   . ASP E 1 46  ? 19.454  -2.683  -92.369  1.00 42.15 ? 46  ASP E C   1 
ATOM   7144  O O   . ASP E 1 46  ? 19.113  -2.081  -93.379  1.00 42.23 ? 46  ASP E O   1 
ATOM   7145  C CB  . ASP E 1 46  ? 20.791  -4.606  -93.209  1.00 45.80 ? 46  ASP E CB  1 
ATOM   7146  C CG  . ASP E 1 46  ? 22.199  -5.144  -93.489  1.00 47.77 ? 46  ASP E CG  1 
ATOM   7147  O OD1 . ASP E 1 46  ? 23.188  -4.369  -93.390  1.00 49.87 ? 46  ASP E OD1 1 
ATOM   7148  O OD2 . ASP E 1 46  ? 22.322  -6.345  -93.804  1.00 45.38 ? 46  ASP E OD2 1 
ATOM   7149  N N   . GLY E 1 47  ? 18.682  -2.796  -91.293  1.00 39.81 ? 47  GLY E N   1 
ATOM   7150  C CA  . GLY E 1 47  ? 17.388  -2.115  -91.204  1.00 40.14 ? 47  GLY E CA  1 
ATOM   7151  C C   . GLY E 1 47  ? 17.507  -0.593  -91.234  1.00 40.46 ? 47  GLY E C   1 
ATOM   7152  O O   . GLY E 1 47  ? 16.524  0.108   -91.519  1.00 42.91 ? 47  GLY E O   1 
ATOM   7153  N N   . TYR E 1 48  ? 18.713  -0.090  -90.930  1.00 37.65 ? 48  TYR E N   1 
ATOM   7154  C CA  . TYR E 1 48  ? 18.968  1.342   -90.792  1.00 33.76 ? 48  TYR E CA  1 
ATOM   7155  C C   . TYR E 1 48  ? 20.126  1.837   -91.653  1.00 31.49 ? 48  TYR E C   1 
ATOM   7156  O O   . TYR E 1 48  ? 21.013  1.071   -92.020  1.00 29.64 ? 48  TYR E O   1 
ATOM   7157  C CB  . TYR E 1 48  ? 19.243  1.675   -89.325  1.00 31.78 ? 48  TYR E CB  1 
ATOM   7158  C CG  . TYR E 1 48  ? 18.117  1.285   -88.379  1.00 31.02 ? 48  TYR E CG  1 
ATOM   7159  C CD1 . TYR E 1 48  ? 17.947  -0.036  -87.990  1.00 30.91 ? 48  TYR E CD1 1 
ATOM   7160  C CD2 . TYR E 1 48  ? 17.216  2.226   -87.891  1.00 30.58 ? 48  TYR E CD2 1 
ATOM   7161  C CE1 . TYR E 1 48  ? 16.937  -0.416  -87.129  1.00 30.77 ? 48  TYR E CE1 1 
ATOM   7162  C CE2 . TYR E 1 48  ? 16.192  1.853   -87.040  1.00 31.32 ? 48  TYR E CE2 1 
ATOM   7163  C CZ  . TYR E 1 48  ? 16.078  0.527   -86.650  1.00 31.89 ? 48  TYR E CZ  1 
ATOM   7164  O OH  . TYR E 1 48  ? 15.073  0.125   -85.803  1.00 33.07 ? 48  TYR E OH  1 
ATOM   7165  N N   . GLU E 1 49  ? 20.083  3.129   -91.962  1.00 30.83 ? 49  GLU E N   1 
ATOM   7166  C CA  . GLU E 1 49  ? 21.051  3.803   -92.823  1.00 30.64 ? 49  GLU E CA  1 
ATOM   7167  C C   . GLU E 1 49  ? 21.321  5.189   -92.220  1.00 27.41 ? 49  GLU E C   1 
ATOM   7168  O O   . GLU E 1 49  ? 20.391  5.961   -92.025  1.00 26.11 ? 49  GLU E O   1 
ATOM   7169  C CB  . GLU E 1 49  ? 20.462  3.917   -94.238  1.00 33.37 ? 49  GLU E CB  1 
ATOM   7170  C CG  . GLU E 1 49  ? 21.302  4.636   -95.274  1.00 36.89 ? 49  GLU E CG  1 
ATOM   7171  C CD  . GLU E 1 49  ? 20.502  5.147   -96.483  1.00 42.34 ? 49  GLU E CD  1 
ATOM   7172  O OE1 . GLU E 1 49  ? 21.068  5.995   -97.198  1.00 45.56 ? 49  GLU E OE1 1 
ATOM   7173  O OE2 . GLU E 1 49  ? 19.325  4.739   -96.726  1.00 45.11 ? 49  GLU E OE2 1 
ATOM   7174  N N   . LEU E 1 50  ? 22.580  5.509   -91.916  1.00 24.97 ? 50  LEU E N   1 
ATOM   7175  C CA  . LEU E 1 50  ? 22.913  6.796   -91.289  1.00 22.88 ? 50  LEU E CA  1 
ATOM   7176  C C   . LEU E 1 50  ? 23.395  7.870   -92.263  1.00 21.18 ? 50  LEU E C   1 
ATOM   7177  O O   . LEU E 1 50  ? 24.040  7.573   -93.262  1.00 20.27 ? 50  LEU E O   1 
ATOM   7178  C CB  . LEU E 1 50  ? 24.005  6.623   -90.250  1.00 22.95 ? 50  LEU E CB  1 
ATOM   7179  C CG  . LEU E 1 50  ? 23.712  5.749   -89.038  1.00 23.59 ? 50  LEU E CG  1 
ATOM   7180  C CD1 . LEU E 1 50  ? 24.873  5.831   -88.072  1.00 23.74 ? 50  LEU E CD1 1 
ATOM   7181  C CD2 . LEU E 1 50  ? 22.430  6.143   -88.340  1.00 23.71 ? 50  LEU E CD2 1 
ATOM   7182  N N   . VAL E 1 51  ? 23.083  9.122   -91.939  1.00 19.64 ? 51  VAL E N   1 
ATOM   7183  C CA  . VAL E 1 51  ? 23.717  10.288  -92.552  1.00 18.80 ? 51  VAL E CA  1 
ATOM   7184  C C   . VAL E 1 51  ? 24.282  11.115  -91.408  1.00 18.28 ? 51  VAL E C   1 
ATOM   7185  O O   . VAL E 1 51  ? 23.568  11.409  -90.455  1.00 17.85 ? 51  VAL E O   1 
ATOM   7186  C CB  . VAL E 1 51  ? 22.716  11.142  -93.340  1.00 19.01 ? 51  VAL E CB  1 
ATOM   7187  C CG1 . VAL E 1 51  ? 23.438  12.202  -94.141  1.00 19.39 ? 51  VAL E CG1 1 
ATOM   7188  C CG2 . VAL E 1 51  ? 21.873  10.269  -94.251  1.00 19.14 ? 51  VAL E CG2 1 
ATOM   7189  N N   . VAL E 1 52  ? 25.557  11.489  -91.491  1.00 17.70 ? 52  VAL E N   1 
ATOM   7190  C CA  . VAL E 1 52  ? 26.235  12.106  -90.359  1.00 17.62 ? 52  VAL E CA  1 
ATOM   7191  C C   . VAL E 1 52  ? 26.814  13.474  -90.695  1.00 17.37 ? 52  VAL E C   1 
ATOM   7192  O O   . VAL E 1 52  ? 27.508  13.637  -91.677  1.00 17.45 ? 52  VAL E O   1 
ATOM   7193  C CB  . VAL E 1 52  ? 27.350  11.189  -89.825  1.00 17.63 ? 52  VAL E CB  1 
ATOM   7194  C CG1 . VAL E 1 52  ? 28.017  11.803  -88.597  1.00 17.86 ? 52  VAL E CG1 1 
ATOM   7195  C CG2 . VAL E 1 52  ? 26.784  9.811   -89.494  1.00 17.12 ? 52  VAL E CG2 1 
ATOM   7196  N N   . ASP E 1 53  ? 26.529  14.464  -89.856  1.00 17.34 ? 53  ASP E N   1 
ATOM   7197  C CA  . ASP E 1 53  ? 27.070  15.804  -90.050  1.00 17.23 ? 53  ASP E CA  1 
ATOM   7198  C C   . ASP E 1 53  ? 27.625  16.335  -88.745  1.00 17.81 ? 53  ASP E C   1 
ATOM   7199  O O   . ASP E 1 53  ? 26.920  16.956  -87.961  1.00 18.31 ? 53  ASP E O   1 
ATOM   7200  C CB  . ASP E 1 53  ? 26.004  16.752  -90.591  1.00 16.43 ? 53  ASP E CB  1 
ATOM   7201  C CG  . ASP E 1 53  ? 26.592  17.924  -91.325  1.00 15.92 ? 53  ASP E CG  1 
ATOM   7202  O OD1 . ASP E 1 53  ? 27.292  18.749  -90.704  1.00 14.81 ? 53  ASP E OD1 1 
ATOM   7203  O OD2 . ASP E 1 53  ? 26.323  18.023  -92.528  1.00 16.28 ? 53  ASP E OD2 1 
ATOM   7204  N N   . GLY E 1 54  ? 28.908  16.082  -88.529  1.00 18.18 ? 54  GLY E N   1 
ATOM   7205  C CA  . GLY E 1 54  ? 29.628  16.562  -87.358  1.00 18.18 ? 54  GLY E CA  1 
ATOM   7206  C C   . GLY E 1 54  ? 30.652  17.626  -87.739  1.00 17.48 ? 54  GLY E C   1 
ATOM   7207  O O   . GLY E 1 54  ? 31.550  17.358  -88.535  1.00 16.11 ? 54  GLY E O   1 
ATOM   7208  N N   . LEU E 1 55  ? 30.507  18.818  -87.154  1.00 17.31 ? 55  LEU E N   1 
ATOM   7209  C CA  . LEU E 1 55  ? 31.405  19.945  -87.402  1.00 17.98 ? 55  LEU E CA  1 
ATOM   7210  C C   . LEU E 1 55  ? 32.145  20.348  -86.143  1.00 18.20 ? 55  LEU E C   1 
ATOM   7211  O O   . LEU E 1 55  ? 31.524  20.779  -85.188  1.00 18.04 ? 55  LEU E O   1 
ATOM   7212  C CB  . LEU E 1 55  ? 30.639  21.163  -87.944  1.00 17.81 ? 55  LEU E CB  1 
ATOM   7213  C CG  . LEU E 1 55  ? 31.434  22.456  -88.166  1.00 17.86 ? 55  LEU E CG  1 
ATOM   7214  C CD1 . LEU E 1 55  ? 32.572  22.246  -89.147  1.00 17.71 ? 55  LEU E CD1 1 
ATOM   7215  C CD2 . LEU E 1 55  ? 30.540  23.594  -88.655  1.00 18.53 ? 55  LEU E CD2 1 
ATOM   7216  N N   . SER E 1 56  ? 33.471  20.232  -86.159  1.00 19.61 ? 56  SER E N   1 
ATOM   7217  C CA  . SER E 1 56  ? 34.289  20.729  -85.057  1.00 20.62 ? 56  SER E CA  1 
ATOM   7218  C C   . SER E 1 56  ? 33.921  22.174  -84.766  1.00 19.99 ? 56  SER E C   1 
ATOM   7219  O O   . SER E 1 56  ? 33.837  22.983  -85.667  1.00 20.35 ? 56  SER E O   1 
ATOM   7220  C CB  . SER E 1 56  ? 35.795  20.628  -85.375  1.00 21.98 ? 56  SER E CB  1 
ATOM   7221  O OG  . SER E 1 56  ? 36.159  19.325  -85.838  1.00 25.02 ? 56  SER E OG  1 
ATOM   7222  N N   . GLY E 1 57  ? 33.652  22.472  -83.505  1.00 19.82 ? 57  GLY E N   1 
ATOM   7223  C CA  . GLY E 1 57  ? 33.402  23.837  -83.050  1.00 20.23 ? 57  GLY E CA  1 
ATOM   7224  C C   . GLY E 1 57  ? 31.950  24.282  -83.023  1.00 20.26 ? 57  GLY E C   1 
ATOM   7225  O O   . GLY E 1 57  ? 31.653  25.374  -82.537  1.00 20.48 ? 57  GLY E O   1 
ATOM   7226  N N   . ARG E 1 58  ? 31.050  23.430  -83.506  1.00 19.95 ? 58  ARG E N   1 
ATOM   7227  C CA  . ARG E 1 58  ? 29.661  23.810  -83.751  1.00 20.51 ? 58  ARG E CA  1 
ATOM   7228  C C   . ARG E 1 58  ? 28.823  23.978  -82.473  1.00 20.95 ? 58  ARG E C   1 
ATOM   7229  O O   . ARG E 1 58  ? 28.900  23.164  -81.526  1.00 20.73 ? 58  ARG E O   1 
ATOM   7230  C CB  . ARG E 1 58  ? 28.992  22.778  -84.675  1.00 20.36 ? 58  ARG E CB  1 
ATOM   7231  C CG  . ARG E 1 58  ? 27.504  22.998  -84.963  1.00 19.91 ? 58  ARG E CG  1 
ATOM   7232  C CD  . ARG E 1 58  ? 26.957  21.897  -85.858  1.00 19.54 ? 58  ARG E CD  1 
ATOM   7233  N NE  . ARG E 1 58  ? 27.178  22.156  -87.288  1.00 19.41 ? 58  ARG E NE  1 
ATOM   7234  C CZ  . ARG E 1 58  ? 27.168  21.229  -88.244  1.00 19.76 ? 58  ARG E CZ  1 
ATOM   7235  N NH1 . ARG E 1 58  ? 26.988  19.942  -87.958  1.00 20.79 ? 58  ARG E NH1 1 
ATOM   7236  N NH2 . ARG E 1 58  ? 27.350  21.588  -89.499  1.00 19.42 ? 58  ARG E NH2 1 
ATOM   7237  N N   . THR E 1 59  ? 28.006  25.037  -82.481  1.00 20.67 ? 59  THR E N   1 
ATOM   7238  C CA  . THR E 1 59  ? 27.116  25.356  -81.373  1.00 20.40 ? 59  THR E CA  1 
ATOM   7239  C C   . THR E 1 59  ? 25.689  25.010  -81.754  1.00 20.78 ? 59  THR E C   1 
ATOM   7240  O O   . THR E 1 59  ? 25.408  24.700  -82.916  1.00 20.48 ? 59  THR E O   1 
ATOM   7241  C CB  . THR E 1 59  ? 27.156  26.851  -81.043  1.00 20.22 ? 59  THR E CB  1 
ATOM   7242  O OG1 . THR E 1 59  ? 26.466  27.595  -82.065  1.00 20.80 ? 59  THR E OG1 1 
ATOM   7243  C CG2 . THR E 1 59  ? 28.591  27.336  -80.962  1.00 19.95 ? 59  THR E CG2 1 
ATOM   7244  N N   . THR E 1 60  ? 24.783  25.088  -80.780  1.00 21.21 ? 60  THR E N   1 
ATOM   7245  C CA  . THR E 1 60  ? 23.360  24.922  -81.052  1.00 21.06 ? 60  THR E CA  1 
ATOM   7246  C C   . THR E 1 60  ? 22.872  25.991  -82.020  1.00 20.65 ? 60  THR E C   1 
ATOM   7247  O O   . THR E 1 60  ? 22.493  25.683  -83.157  1.00 22.33 ? 60  THR E O   1 
ATOM   7248  C CB  . THR E 1 60  ? 22.502  24.996  -79.778  1.00 21.19 ? 60  THR E CB  1 
ATOM   7249  O OG1 . THR E 1 60  ? 22.833  26.181  -79.044  1.00 22.77 ? 60  THR E OG1 1 
ATOM   7250  C CG2 . THR E 1 60  ? 22.729  23.790  -78.899  1.00 21.28 ? 60  THR E CG2 1 
ATOM   7251  N N   . ASN E 1 61  ? 22.891  27.249  -81.574  1.00 19.18 ? 61  ASN E N   1 
ATOM   7252  C CA  . ASN E 1 61  ? 22.215  28.329  -82.301  1.00 17.71 ? 61  ASN E CA  1 
ATOM   7253  C C   . ASN E 1 61  ? 22.823  29.723  -82.109  1.00 17.48 ? 61  ASN E C   1 
ATOM   7254  O O   . ASN E 1 61  ? 22.114  30.723  -82.232  1.00 16.56 ? 61  ASN E O   1 
ATOM   7255  C CB  . ASN E 1 61  ? 20.762  28.373  -81.854  1.00 17.08 ? 61  ASN E CB  1 
ATOM   7256  C CG  . ASN E 1 61  ? 20.582  29.051  -80.506  1.00 16.02 ? 61  ASN E CG  1 
ATOM   7257  O OD1 . ASN E 1 61  ? 21.473  29.060  -79.664  1.00 14.56 ? 61  ASN E OD1 1 
ATOM   7258  N ND2 . ASN E 1 61  ? 19.421  29.617  -80.309  1.00 15.47 ? 61  ASN E ND2 1 
ATOM   7259  N N   . ILE E 1 62  ? 24.123  29.792  -81.831  1.00 17.42 ? 62  ILE E N   1 
ATOM   7260  C CA  . ILE E 1 62  ? 24.781  31.067  -81.535  1.00 17.31 ? 62  ILE E CA  1 
ATOM   7261  C C   . ILE E 1 62  ? 26.039  31.242  -82.374  1.00 17.33 ? 62  ILE E C   1 
ATOM   7262  O O   . ILE E 1 62  ? 26.808  30.282  -82.566  1.00 16.49 ? 62  ILE E O   1 
ATOM   7263  C CB  . ILE E 1 62  ? 25.149  31.161  -80.049  1.00 17.20 ? 62  ILE E CB  1 
ATOM   7264  C CG1 . ILE E 1 62  ? 25.709  32.532  -79.691  1.00 16.80 ? 62  ILE E CG1 1 
ATOM   7265  C CG2 . ILE E 1 62  ? 26.150  30.101  -79.656  1.00 17.23 ? 62  ILE E CG2 1 
ATOM   7266  C CD1 . ILE E 1 62  ? 25.734  32.785  -78.201  1.00 17.03 ? 62  ILE E CD1 1 
ATOM   7267  N N   . ASP E 1 63  ? 26.239  32.474  -82.878  1.00 16.81 ? 63  ASP E N   1 
ATOM   7268  C CA  . ASP E 1 63  ? 27.447  32.799  -83.649  1.00 16.03 ? 63  ASP E CA  1 
ATOM   7269  C C   . ASP E 1 63  ? 28.708  32.767  -82.795  1.00 15.42 ? 63  ASP E C   1 
ATOM   7270  O O   . ASP E 1 63  ? 28.719  33.261  -81.676  1.00 15.51 ? 63  ASP E O   1 
ATOM   7271  C CB  . ASP E 1 63  ? 27.333  34.186  -84.260  1.00 15.60 ? 63  ASP E CB  1 
ATOM   7272  C CG  . ASP E 1 63  ? 26.275  34.270  -85.317  1.00 15.68 ? 63  ASP E CG  1 
ATOM   7273  O OD1 . ASP E 1 63  ? 25.931  33.275  -85.976  1.00 16.44 ? 63  ASP E OD1 1 
ATOM   7274  O OD2 . ASP E 1 63  ? 25.788  35.363  -85.532  1.00 15.59 ? 63  ASP E OD2 1 
ATOM   7275  N N   . ASP E 1 64  ? 29.758  32.173  -83.328  1.00 15.47 ? 64  ASP E N   1 
ATOM   7276  C CA  . ASP E 1 64  ? 31.073  32.231  -82.713  1.00 15.81 ? 64  ASP E CA  1 
ATOM   7277  C C   . ASP E 1 64  ? 31.822  33.395  -83.365  1.00 16.27 ? 64  ASP E C   1 
ATOM   7278  O O   . ASP E 1 64  ? 32.074  33.379  -84.576  1.00 15.80 ? 64  ASP E O   1 
ATOM   7279  C CB  . ASP E 1 64  ? 31.837  30.906  -82.887  1.00 15.50 ? 64  ASP E CB  1 
ATOM   7280  C CG  . ASP E 1 64  ? 33.054  30.814  -81.987  1.00 15.22 ? 64  ASP E CG  1 
ATOM   7281  O OD1 . ASP E 1 64  ? 33.877  31.745  -82.004  1.00 15.52 ? 64  ASP E OD1 1 
ATOM   7282  O OD2 . ASP E 1 64  ? 33.204  29.831  -81.261  1.00 14.68 ? 64  ASP E OD2 1 
ATOM   7283  N N   . PRO E 1 65  ? 32.169  34.428  -82.569  1.00 17.49 ? 65  PRO E N   1 
ATOM   7284  C CA  . PRO E 1 65  ? 32.842  35.573  -83.199  1.00 18.34 ? 65  PRO E CA  1 
ATOM   7285  C C   . PRO E 1 65  ? 34.199  35.209  -83.843  1.00 19.14 ? 65  PRO E C   1 
ATOM   7286  O O   . PRO E 1 65  ? 34.701  35.969  -84.665  1.00 18.23 ? 65  PRO E O   1 
ATOM   7287  C CB  . PRO E 1 65  ? 33.002  36.574  -82.051  1.00 17.84 ? 65  PRO E CB  1 
ATOM   7288  C CG  . PRO E 1 65  ? 32.889  35.765  -80.800  1.00 17.62 ? 65  PRO E CG  1 
ATOM   7289  C CD  . PRO E 1 65  ? 31.998  34.610  -81.113  1.00 17.20 ? 65  PRO E CD  1 
ATOM   7290  N N   . ASN E 1 66  ? 34.751  34.045  -83.502  1.00 20.49 ? 66  ASN E N   1 
ATOM   7291  C CA  . ASN E 1 66  ? 36.008  33.585  -84.076  1.00 22.17 ? 66  ASN E CA  1 
ATOM   7292  C C   . ASN E 1 66  ? 35.889  32.837  -85.402  1.00 22.98 ? 66  ASN E C   1 
ATOM   7293  O O   . ASN E 1 66  ? 36.908  32.585  -86.053  1.00 24.32 ? 66  ASN E O   1 
ATOM   7294  C CB  . ASN E 1 66  ? 36.731  32.674  -83.081  1.00 22.50 ? 66  ASN E CB  1 
ATOM   7295  C CG  . ASN E 1 66  ? 37.047  33.377  -81.790  1.00 22.29 ? 66  ASN E CG  1 
ATOM   7296  O OD1 . ASN E 1 66  ? 37.912  34.261  -81.741  1.00 21.56 ? 66  ASN E OD1 1 
ATOM   7297  N ND2 . ASN E 1 66  ? 36.338  32.997  -80.736  1.00 22.48 ? 66  ASN E ND2 1 
ATOM   7298  N N   . ASP E 1 67  ? 34.683  32.426  -85.778  1.00 23.11 ? 67  ASP E N   1 
ATOM   7299  C CA  . ASP E 1 67  ? 34.489  31.620  -86.990  1.00 23.15 ? 67  ASP E CA  1 
ATOM   7300  C C   . ASP E 1 67  ? 33.013  31.645  -87.410  1.00 23.79 ? 67  ASP E C   1 
ATOM   7301  O O   . ASP E 1 67  ? 32.135  31.122  -86.692  1.00 25.23 ? 67  ASP E O   1 
ATOM   7302  C CB  . ASP E 1 67  ? 34.949  30.173  -86.751  1.00 22.67 ? 67  ASP E CB  1 
ATOM   7303  C CG  . ASP E 1 67  ? 35.035  29.361  -88.019  1.00 22.22 ? 67  ASP E CG  1 
ATOM   7304  O OD1 . ASP E 1 67  ? 34.490  29.781  -89.067  1.00 21.18 ? 67  ASP E OD1 1 
ATOM   7305  O OD2 . ASP E 1 67  ? 35.659  28.275  -87.956  1.00 21.65 ? 67  ASP E OD2 1 
ATOM   7306  N N   . PRO E 1 68  ? 32.729  32.233  -88.577  1.00 23.27 ? 68  PRO E N   1 
ATOM   7307  C CA  . PRO E 1 68  ? 31.333  32.364  -88.977  1.00 22.41 ? 68  PRO E CA  1 
ATOM   7308  C C   . PRO E 1 68  ? 30.628  31.077  -89.421  1.00 20.81 ? 68  PRO E C   1 
ATOM   7309  O O   . PRO E 1 68  ? 29.460  31.136  -89.721  1.00 20.37 ? 68  PRO E O   1 
ATOM   7310  C CB  . PRO E 1 68  ? 31.373  33.385  -90.120  1.00 22.89 ? 68  PRO E CB  1 
ATOM   7311  C CG  . PRO E 1 68  ? 32.795  33.447  -90.591  1.00 23.51 ? 68  PRO E CG  1 
ATOM   7312  C CD  . PRO E 1 68  ? 33.667  32.869  -89.521  1.00 23.62 ? 68  PRO E CD  1 
ATOM   7313  N N   . LYS E 1 69  ? 31.286  29.927  -89.446  1.00 20.55 ? 69  LYS E N   1 
ATOM   7314  C CA  . LYS E 1 69  ? 30.609  28.694  -89.907  1.00 20.74 ? 69  LYS E CA  1 
ATOM   7315  C C   . LYS E 1 69  ? 30.109  27.748  -88.811  1.00 20.77 ? 69  LYS E C   1 
ATOM   7316  O O   . LYS E 1 69  ? 29.696  26.640  -89.123  1.00 21.08 ? 69  LYS E O   1 
ATOM   7317  C CB  . LYS E 1 69  ? 31.510  27.919  -90.884  1.00 20.04 ? 69  LYS E CB  1 
ATOM   7318  C CG  . LYS E 1 69  ? 32.711  27.228  -90.279  1.00 19.71 ? 69  LYS E CG  1 
ATOM   7319  C CD  . LYS E 1 69  ? 33.600  26.668  -91.389  1.00 19.74 ? 69  LYS E CD  1 
ATOM   7320  C CE  . LYS E 1 69  ? 34.859  25.980  -90.886  1.00 19.44 ? 69  LYS E CE  1 
ATOM   7321  N NZ  . LYS E 1 69  ? 35.920  26.933  -90.506  1.00 19.14 ? 69  LYS E NZ  1 
ATOM   7322  N N   . LEU E 1 70  ? 30.137  28.186  -87.552  1.00 20.85 ? 70  LEU E N   1 
ATOM   7323  C CA  . LEU E 1 70  ? 29.942  27.283  -86.410  1.00 20.51 ? 70  LEU E CA  1 
ATOM   7324  C C   . LEU E 1 70  ? 28.548  27.272  -85.788  1.00 19.70 ? 70  LEU E C   1 
ATOM   7325  O O   . LEU E 1 70  ? 28.323  26.611  -84.769  1.00 20.05 ? 70  LEU E O   1 
ATOM   7326  C CB  . LEU E 1 70  ? 30.967  27.606  -85.320  1.00 21.10 ? 70  LEU E CB  1 
ATOM   7327  C CG  . LEU E 1 70  ? 32.426  27.498  -85.754  1.00 21.59 ? 70  LEU E CG  1 
ATOM   7328  C CD1 . LEU E 1 70  ? 33.342  27.762  -84.575  1.00 21.71 ? 70  LEU E CD1 1 
ATOM   7329  C CD2 . LEU E 1 70  ? 32.702  26.127  -86.344  1.00 21.87 ? 70  LEU E CD2 1 
ATOM   7330  N N   . ASN E 1 71  ? 27.614  27.993  -86.381  1.00 19.26 ? 71  ASN E N   1 
ATOM   7331  C CA  . ASN E 1 71  ? 26.274  28.076  -85.819  1.00 19.10 ? 71  ASN E CA  1 
ATOM   7332  C C   . ASN E 1 71  ? 25.387  26.989  -86.400  1.00 19.37 ? 71  ASN E C   1 
ATOM   7333  O O   . ASN E 1 71  ? 24.982  27.074  -87.565  1.00 20.24 ? 71  ASN E O   1 
ATOM   7334  C CB  . ASN E 1 71  ? 25.681  29.446  -86.111  1.00 18.83 ? 71  ASN E CB  1 
ATOM   7335  C CG  . ASN E 1 71  ? 24.407  29.705  -85.335  1.00 18.62 ? 71  ASN E CG  1 
ATOM   7336  O OD1 . ASN E 1 71  ? 23.571  28.813  -85.151  1.00 18.50 ? 71  ASN E OD1 1 
ATOM   7337  N ND2 . ASN E 1 71  ? 24.241  30.939  -84.887  1.00 18.10 ? 71  ASN E ND2 1 
ATOM   7338  N N   . GLY E 1 72  ? 25.071  25.974  -85.591  1.00 18.88 ? 72  GLY E N   1 
ATOM   7339  C CA  . GLY E 1 72  ? 24.235  24.853  -86.038  1.00 17.60 ? 72  GLY E CA  1 
ATOM   7340  C C   . GLY E 1 72  ? 22.955  25.272  -86.743  1.00 16.88 ? 72  GLY E C   1 
ATOM   7341  O O   . GLY E 1 72  ? 22.595  24.703  -87.769  1.00 16.18 ? 72  GLY E O   1 
ATOM   7342  N N   . ALA E 1 73  ? 22.288  26.284  -86.196  1.00 16.78 ? 73  ALA E N   1 
ATOM   7343  C CA  . ALA E 1 73  ? 20.994  26.730  -86.695  1.00 16.29 ? 73  ALA E CA  1 
ATOM   7344  C C   . ALA E 1 73  ? 21.087  27.475  -88.034  1.00 16.26 ? 73  ALA E C   1 
ATOM   7345  O O   . ALA E 1 73  ? 20.103  27.547  -88.775  1.00 16.61 ? 73  ALA E O   1 
ATOM   7346  C CB  . ALA E 1 73  ? 20.315  27.589  -85.642  1.00 16.22 ? 73  ALA E CB  1 
ATOM   7347  N N   . ASP E 1 74  ? 22.254  28.031  -88.353  1.00 16.13 ? 74  ASP E N   1 
ATOM   7348  C CA  . ASP E 1 74  ? 22.493  28.564  -89.700  1.00 16.34 ? 74  ASP E CA  1 
ATOM   7349  C C   . ASP E 1 74  ? 22.443  27.456  -90.757  1.00 16.80 ? 74  ASP E C   1 
ATOM   7350  O O   . ASP E 1 74  ? 22.049  27.697  -91.876  1.00 17.52 ? 74  ASP E O   1 
ATOM   7351  C CB  . ASP E 1 74  ? 23.860  29.246  -89.809  1.00 16.41 ? 74  ASP E CB  1 
ATOM   7352  C CG  . ASP E 1 74  ? 23.905  30.627  -89.165  1.00 16.16 ? 74  ASP E CG  1 
ATOM   7353  O OD1 . ASP E 1 74  ? 22.851  31.218  -88.884  1.00 15.98 ? 74  ASP E OD1 1 
ATOM   7354  O OD2 . ASP E 1 74  ? 25.024  31.125  -88.939  1.00 16.00 ? 74  ASP E OD2 1 
ATOM   7355  N N   . TYR E 1 75  ? 22.837  26.246  -90.385  1.00 17.46 ? 75  TYR E N   1 
ATOM   7356  C CA  . TYR E 1 75  ? 23.072  25.125  -91.310  1.00 17.77 ? 75  TYR E CA  1 
ATOM   7357  C C   . TYR E 1 75  ? 21.915  24.120  -91.376  1.00 18.19 ? 75  TYR E C   1 
ATOM   7358  O O   . TYR E 1 75  ? 21.652  23.518  -92.424  1.00 17.69 ? 75  TYR E O   1 
ATOM   7359  C CB  . TYR E 1 75  ? 24.331  24.427  -90.806  1.00 17.70 ? 75  TYR E CB  1 
ATOM   7360  C CG  . TYR E 1 75  ? 25.015  23.370  -91.650  1.00 18.07 ? 75  TYR E CG  1 
ATOM   7361  C CD1 . TYR E 1 75  ? 24.627  22.033  -91.575  1.00 18.33 ? 75  TYR E CD1 1 
ATOM   7362  C CD2 . TYR E 1 75  ? 26.149  23.674  -92.418  1.00 17.76 ? 75  TYR E CD2 1 
ATOM   7363  C CE1 . TYR E 1 75  ? 25.300  21.047  -92.291  1.00 17.68 ? 75  TYR E CE1 1 
ATOM   7364  C CE2 . TYR E 1 75  ? 26.812  22.694  -93.137  1.00 17.74 ? 75  TYR E CE2 1 
ATOM   7365  C CZ  . TYR E 1 75  ? 26.383  21.379  -93.068  1.00 17.56 ? 75  TYR E CZ  1 
ATOM   7366  O OH  . TYR E 1 75  ? 27.045  20.397  -93.767  1.00 17.93 ? 75  TYR E OH  1 
ATOM   7367  N N   . LEU E 1 76  ? 21.225  23.936  -90.254  1.00 19.21 ? 76  LEU E N   1 
ATOM   7368  C CA  . LEU E 1 76  ? 20.326  22.795  -90.092  1.00 19.97 ? 76  LEU E CA  1 
ATOM   7369  C C   . LEU E 1 76  ? 19.148  22.774  -91.072  1.00 20.42 ? 76  LEU E C   1 
ATOM   7370  O O   . LEU E 1 76  ? 18.835  21.711  -91.610  1.00 19.71 ? 76  LEU E O   1 
ATOM   7371  C CB  . LEU E 1 76  ? 19.849  22.667  -88.643  1.00 19.85 ? 76  LEU E CB  1 
ATOM   7372  C CG  . LEU E 1 76  ? 19.007  21.419  -88.346  1.00 20.23 ? 76  LEU E CG  1 
ATOM   7373  C CD1 . LEU E 1 76  ? 19.743  20.139  -88.702  1.00 20.24 ? 76  LEU E CD1 1 
ATOM   7374  C CD2 . LEU E 1 76  ? 18.551  21.388  -86.894  1.00 20.35 ? 76  LEU E CD2 1 
ATOM   7375  N N   . PRO E 1 77  ? 18.491  23.934  -91.309  1.00 20.42 ? 77  PRO E N   1 
ATOM   7376  C CA  . PRO E 1 77  ? 17.372  23.900  -92.260  1.00 20.15 ? 77  PRO E CA  1 
ATOM   7377  C C   . PRO E 1 77  ? 17.773  23.327  -93.617  1.00 20.33 ? 77  PRO E C   1 
ATOM   7378  O O   . PRO E 1 77  ? 17.059  22.487  -94.159  1.00 20.49 ? 77  PRO E O   1 
ATOM   7379  C CB  . PRO E 1 77  ? 16.960  25.367  -92.363  1.00 19.30 ? 77  PRO E CB  1 
ATOM   7380  C CG  . PRO E 1 77  ? 17.289  25.917  -91.032  1.00 19.45 ? 77  PRO E CG  1 
ATOM   7381  C CD  . PRO E 1 77  ? 18.590  25.246  -90.654  1.00 19.93 ? 77  PRO E CD  1 
ATOM   7382  N N   . ALA E 1 78  ? 18.906  23.770  -94.144  1.00 20.86 ? 78  ALA E N   1 
ATOM   7383  C CA  . ALA E 1 78  ? 19.406  23.263  -95.425  1.00 22.24 ? 78  ALA E CA  1 
ATOM   7384  C C   . ALA E 1 78  ? 19.725  21.777  -95.348  1.00 23.22 ? 78  ALA E C   1 
ATOM   7385  O O   . ALA E 1 78  ? 19.355  21.014  -96.232  1.00 24.16 ? 78  ALA E O   1 
ATOM   7386  C CB  . ALA E 1 78  ? 20.633  24.038  -95.878  1.00 22.25 ? 78  ALA E CB  1 
ATOM   7387  N N   . ALA E 1 79  ? 20.402  21.374  -94.283  1.00 24.36 ? 79  ALA E N   1 
ATOM   7388  C CA  . ALA E 1 79  ? 20.798  19.987  -94.114  1.00 25.20 ? 79  ALA E CA  1 
ATOM   7389  C C   . ALA E 1 79  ? 19.579  19.058  -94.098  1.00 24.97 ? 79  ALA E C   1 
ATOM   7390  O O   . ALA E 1 79  ? 19.563  18.025  -94.758  1.00 24.65 ? 79  ALA E O   1 
ATOM   7391  C CB  . ALA E 1 79  ? 21.601  19.836  -92.831  1.00 26.59 ? 79  ALA E CB  1 
ATOM   7392  N N   . LEU E 1 80  ? 18.551  19.451  -93.358  1.00 25.19 ? 80  LEU E N   1 
ATOM   7393  C CA  . LEU E 1 80  ? 17.331  18.654  -93.239  1.00 24.79 ? 80  LEU E CA  1 
ATOM   7394  C C   . LEU E 1 80  ? 16.666  18.417  -94.590  1.00 25.86 ? 80  LEU E C   1 
ATOM   7395  O O   . LEU E 1 80  ? 16.230  17.298  -94.879  1.00 26.75 ? 80  LEU E O   1 
ATOM   7396  C CB  . LEU E 1 80  ? 16.344  19.341  -92.299  1.00 23.61 ? 80  LEU E CB  1 
ATOM   7397  C CG  . LEU E 1 80  ? 16.726  19.326  -90.815  1.00 23.51 ? 80  LEU E CG  1 
ATOM   7398  C CD1 . LEU E 1 80  ? 15.890  20.362  -90.069  1.00 23.58 ? 80  LEU E CD1 1 
ATOM   7399  C CD2 . LEU E 1 80  ? 16.583  17.926  -90.185  1.00 22.59 ? 80  LEU E CD2 1 
ATOM   7400  N N   . ALA E 1 81  ? 16.594  19.473  -95.400  1.00 25.79 ? 81  ALA E N   1 
ATOM   7401  C CA  . ALA E 1 81  ? 15.952  19.434  -96.719  1.00 25.08 ? 81  ALA E CA  1 
ATOM   7402  C C   . ALA E 1 81  ? 16.761  18.638  -97.712  1.00 24.63 ? 81  ALA E C   1 
ATOM   7403  O O   . ALA E 1 81  ? 16.212  18.058  -98.663  1.00 25.96 ? 81  ALA E O   1 
ATOM   7404  C CB  . ALA E 1 81  ? 15.753  20.850  -97.249  1.00 25.27 ? 81  ALA E CB  1 
ATOM   7405  N N   . ALA E 1 82  ? 18.075  18.645  -97.501  1.00 23.78 ? 82  ALA E N   1 
ATOM   7406  C CA  . ALA E 1 82  ? 19.020  17.962  -98.369  1.00 23.08 ? 82  ALA E CA  1 
ATOM   7407  C C   . ALA E 1 82  ? 19.033  16.448  -98.124  1.00 23.05 ? 82  ALA E C   1 
ATOM   7408  O O   . ALA E 1 82  ? 19.479  15.690  -98.994  1.00 22.88 ? 82  ALA E O   1 
ATOM   7409  C CB  . ALA E 1 82  ? 20.408  18.540  -98.167  1.00 22.44 ? 82  ALA E CB  1 
ATOM   7410  N N   . HIS E 1 83  ? 18.567  16.022  -96.947  1.00 22.41 ? 83  HIS E N   1 
ATOM   7411  C CA  . HIS E 1 83  ? 18.539  14.608  -96.593  1.00 21.83 ? 83  HIS E CA  1 
ATOM   7412  C C   . HIS E 1 83  ? 17.128  14.043  -96.389  1.00 22.08 ? 83  HIS E C   1 
ATOM   7413  O O   . HIS E 1 83  ? 16.979  12.858  -96.047  1.00 21.93 ? 83  HIS E O   1 
ATOM   7414  C CB  . HIS E 1 83  ? 19.408  14.367  -95.370  1.00 21.64 ? 83  HIS E CB  1 
ATOM   7415  C CG  . HIS E 1 83  ? 20.817  14.826  -95.556  1.00 21.95 ? 83  HIS E CG  1 
ATOM   7416  N ND1 . HIS E 1 83  ? 21.575  14.463  -96.649  1.00 22.12 ? 83  HIS E ND1 1 
ATOM   7417  C CD2 . HIS E 1 83  ? 21.598  15.649  -94.812  1.00 22.24 ? 83  HIS E CD2 1 
ATOM   7418  C CE1 . HIS E 1 83  ? 22.761  15.050  -96.568  1.00 22.72 ? 83  HIS E CE1 1 
ATOM   7419  N NE2 . HIS E 1 83  ? 22.801  15.768  -95.460  1.00 22.24 ? 83  HIS E NE2 1 
ATOM   7420  N N   . GLU E 1 84  ? 16.102  14.867  -96.637  1.00 21.56 ? 84  GLU E N   1 
ATOM   7421  C CA  . GLU E 1 84  ? 14.718  14.393  -96.623  1.00 20.76 ? 84  GLU E CA  1 
ATOM   7422  C C   . GLU E 1 84  ? 14.555  13.252  -97.645  1.00 20.58 ? 84  GLU E C   1 
ATOM   7423  O O   . GLU E 1 84  ? 15.085  13.351  -98.769  1.00 20.29 ? 84  GLU E O   1 
ATOM   7424  C CB  . GLU E 1 84  ? 13.762  15.552  -96.981  1.00 20.35 ? 84  GLU E CB  1 
ATOM   7425  C CG  . GLU E 1 84  ? 12.285  15.217  -96.798  1.00 19.90 ? 84  GLU E CG  1 
ATOM   7426  C CD  . GLU E 1 84  ? 11.346  16.326  -97.198  1.00 19.82 ? 84  GLU E CD  1 
ATOM   7427  O OE1 . GLU E 1 84  ? 10.383  16.521  -96.413  1.00 19.79 ? 84  GLU E OE1 1 
ATOM   7428  O OE2 . GLU E 1 84  ? 11.553  16.994  -98.269  1.00 20.00 ? 84  GLU E OE2 1 
ATOM   7429  N N   . PRO E 1 85  ? 13.831  12.178  -97.297  1.00 19.85 ? 85  PRO E N   1 
ATOM   7430  C CA  . PRO E 1 85  ? 13.097  12.024  -96.042  1.00 19.60 ? 85  PRO E CA  1 
ATOM   7431  C C   . PRO E 1 85  ? 13.875  11.258  -94.985  1.00 19.95 ? 85  PRO E C   1 
ATOM   7432  O O   . PRO E 1 85  ? 14.628  10.318  -95.310  1.00 20.77 ? 85  PRO E O   1 
ATOM   7433  C CB  . PRO E 1 85  ? 11.896  11.183  -96.466  1.00 19.51 ? 85  PRO E CB  1 
ATOM   7434  C CG  . PRO E 1 85  ? 12.434  10.314  -97.541  1.00 19.61 ? 85  PRO E CG  1 
ATOM   7435  C CD  . PRO E 1 85  ? 13.473  11.128  -98.268  1.00 19.59 ? 85  PRO E CD  1 
ATOM   7436  N N   . LEU E 1 86  ? 13.668  11.643  -93.727  1.00 19.55 ? 86  LEU E N   1 
ATOM   7437  C CA  . LEU E 1 86  ? 14.320  10.977  -92.604  1.00 18.37 ? 86  LEU E CA  1 
ATOM   7438  C C   . LEU E 1 86  ? 13.299  10.346  -91.677  1.00 18.14 ? 86  LEU E C   1 
ATOM   7439  O O   . LEU E 1 86  ? 12.159  10.770  -91.613  1.00 18.16 ? 86  LEU E O   1 
ATOM   7440  C CB  . LEU E 1 86  ? 15.182  11.985  -91.841  1.00 18.05 ? 86  LEU E CB  1 
ATOM   7441  C CG  . LEU E 1 86  ? 16.299  12.677  -92.641  1.00 17.81 ? 86  LEU E CG  1 
ATOM   7442  C CD1 . LEU E 1 86  ? 16.772  13.937  -91.921  1.00 17.36 ? 86  LEU E CD1 1 
ATOM   7443  C CD2 . LEU E 1 86  ? 17.454  11.709  -92.895  1.00 17.75 ? 86  LEU E CD2 1 
ATOM   7444  N N   . ASP E 1 87  ? 13.730  9.329   -90.950  1.00 18.85 ? 87  ASP E N   1 
ATOM   7445  C CA  . ASP E 1 87  ? 12.924  8.674   -89.926  1.00 18.48 ? 87  ASP E CA  1 
ATOM   7446  C C   . ASP E 1 87  ? 13.292  9.128   -88.518  1.00 17.83 ? 87  ASP E C   1 
ATOM   7447  O O   . ASP E 1 87  ? 12.484  8.956   -87.595  1.00 18.73 ? 87  ASP E O   1 
ATOM   7448  C CB  . ASP E 1 87  ? 13.089  7.170   -90.042  1.00 18.69 ? 87  ASP E CB  1 
ATOM   7449  C CG  . ASP E 1 87  ? 12.517  6.644   -91.312  1.00 19.03 ? 87  ASP E CG  1 
ATOM   7450  O OD1 . ASP E 1 87  ? 11.283  6.443   -91.319  1.00 19.24 ? 87  ASP E OD1 1 
ATOM   7451  O OD2 . ASP E 1 87  ? 13.262  6.383   -92.271  1.00 19.28 ? 87  ASP E OD2 1 
ATOM   7452  N N   . LEU E 1 88  ? 14.498  9.679   -88.354  1.00 16.99 ? 88  LEU E N   1 
ATOM   7453  C CA  . LEU E 1 88  ? 14.942  10.246  -87.079  1.00 17.14 ? 88  LEU E CA  1 
ATOM   7454  C C   . LEU E 1 88  ? 16.052  11.298  -87.241  1.00 16.99 ? 88  LEU E C   1 
ATOM   7455  O O   . LEU E 1 88  ? 16.906  11.192  -88.116  1.00 16.73 ? 88  LEU E O   1 
ATOM   7456  C CB  . LEU E 1 88  ? 15.445  9.119   -86.161  1.00 17.46 ? 88  LEU E CB  1 
ATOM   7457  C CG  . LEU E 1 88  ? 15.824  9.500   -84.724  1.00 17.44 ? 88  LEU E CG  1 
ATOM   7458  C CD1 . LEU E 1 88  ? 14.605  9.983   -83.921  1.00 17.15 ? 88  LEU E CD1 1 
ATOM   7459  C CD2 . LEU E 1 88  ? 16.483  8.272   -84.071  1.00 17.06 ? 88  LEU E CD2 1 
ATOM   7460  N N   . VAL E 1 89  ? 16.031  12.308  -86.383  1.00 17.13 ? 89  VAL E N   1 
ATOM   7461  C CA  . VAL E 1 89  ? 17.118  13.275  -86.294  1.00 17.45 ? 89  VAL E CA  1 
ATOM   7462  C C   . VAL E 1 89  ? 17.711  13.195  -84.895  1.00 17.74 ? 89  VAL E C   1 
ATOM   7463  O O   . VAL E 1 89  ? 16.993  13.367  -83.915  1.00 18.58 ? 89  VAL E O   1 
ATOM   7464  C CB  . VAL E 1 89  ? 16.638  14.714  -86.571  1.00 17.40 ? 89  VAL E CB  1 
ATOM   7465  C CG1 . VAL E 1 89  ? 17.755  15.701  -86.351  1.00 17.37 ? 89  VAL E CG1 1 
ATOM   7466  C CG2 . VAL E 1 89  ? 16.142  14.841  -87.995  1.00 17.79 ? 89  VAL E CG2 1 
ATOM   7467  N N   . ILE E 1 90  ? 19.011  12.929  -84.815  1.00 17.97 ? 90  ILE E N   1 
ATOM   7468  C CA  . ILE E 1 90  ? 19.718  12.883  -83.554  1.00 18.62 ? 90  ILE E CA  1 
ATOM   7469  C C   . ILE E 1 90  ? 20.568  14.126  -83.450  1.00 18.99 ? 90  ILE E C   1 
ATOM   7470  O O   . ILE E 1 90  ? 21.309  14.441  -84.375  1.00 20.16 ? 90  ILE E O   1 
ATOM   7471  C CB  . ILE E 1 90  ? 20.618  11.644  -83.458  1.00 19.30 ? 90  ILE E CB  1 
ATOM   7472  C CG1 . ILE E 1 90  ? 19.750  10.379  -83.318  1.00 20.14 ? 90  ILE E CG1 1 
ATOM   7473  C CG2 . ILE E 1 90  ? 21.527  11.745  -82.236  1.00 19.63 ? 90  ILE E CG2 1 
ATOM   7474  C CD1 . ILE E 1 90  ? 20.518  9.064   -83.301  1.00 19.94 ? 90  ILE E CD1 1 
ATOM   7475  N N   . ILE E 1 91  ? 20.466  14.829  -82.328  1.00 19.26 ? 91  ILE E N   1 
ATOM   7476  C CA  . ILE E 1 91  ? 21.239  16.048  -82.104  1.00 19.72 ? 91  ILE E CA  1 
ATOM   7477  C C   . ILE E 1 91  ? 22.092  15.818  -80.876  1.00 19.40 ? 91  ILE E C   1 
ATOM   7478  O O   . ILE E 1 91  ? 21.559  15.569  -79.806  1.00 18.51 ? 91  ILE E O   1 
ATOM   7479  C CB  . ILE E 1 91  ? 20.337  17.288  -81.881  1.00 19.72 ? 91  ILE E CB  1 
ATOM   7480  C CG1 . ILE E 1 91  ? 19.485  17.543  -83.122  1.00 19.67 ? 91  ILE E CG1 1 
ATOM   7481  C CG2 . ILE E 1 91  ? 21.159  18.545  -81.599  1.00 19.40 ? 91  ILE E CG2 1 
ATOM   7482  C CD1 . ILE E 1 91  ? 18.350  18.529  -82.913  1.00 19.95 ? 91  ILE E CD1 1 
ATOM   7483  N N   . LEU E 1 92  ? 23.408  15.875  -81.060  1.00 19.28 ? 92  LEU E N   1 
ATOM   7484  C CA  . LEU E 1 92  ? 24.361  15.826  -79.966  1.00 19.75 ? 92  LEU E CA  1 
ATOM   7485  C C   . LEU E 1 92  ? 25.251  17.063  -80.055  1.00 20.22 ? 92  LEU E C   1 
ATOM   7486  O O   . LEU E 1 92  ? 26.324  17.039  -80.693  1.00 20.75 ? 92  LEU E O   1 
ATOM   7487  C CB  . LEU E 1 92  ? 25.186  14.545  -80.044  1.00 20.42 ? 92  LEU E CB  1 
ATOM   7488  C CG  . LEU E 1 92  ? 26.354  14.401  -79.063  1.00 21.25 ? 92  LEU E CG  1 
ATOM   7489  C CD1 . LEU E 1 92  ? 25.886  14.658  -77.639  1.00 21.48 ? 92  LEU E CD1 1 
ATOM   7490  C CD2 . LEU E 1 92  ? 26.990  13.018  -79.175  1.00 20.71 ? 92  LEU E CD2 1 
ATOM   7491  N N   . LEU E 1 93  ? 24.766  18.129  -79.422  1.00 20.60 ? 93  LEU E N   1 
ATOM   7492  C CA  . LEU E 1 93  ? 25.408  19.439  -79.378  1.00 20.99 ? 93  LEU E CA  1 
ATOM   7493  C C   . LEU E 1 93  ? 25.241  20.045  -78.005  1.00 21.50 ? 93  LEU E C   1 
ATOM   7494  O O   . LEU E 1 93  ? 24.376  19.623  -77.235  1.00 20.49 ? 93  LEU E O   1 
ATOM   7495  C CB  . LEU E 1 93  ? 24.756  20.399  -80.361  1.00 21.90 ? 93  LEU E CB  1 
ATOM   7496  C CG  . LEU E 1 93  ? 24.996  20.188  -81.851  1.00 22.57 ? 93  LEU E CG  1 
ATOM   7497  C CD1 . LEU E 1 93  ? 24.072  21.123  -82.631  1.00 22.33 ? 93  LEU E CD1 1 
ATOM   7498  C CD2 . LEU E 1 93  ? 26.466  20.444  -82.196  1.00 22.87 ? 93  LEU E CD2 1 
ATOM   7499  N N   . GLY E 1 94  ? 26.066  21.047  -77.714  1.00 22.41 ? 94  GLY E N   1 
ATOM   7500  C CA  . GLY E 1 94  ? 26.046  21.732  -76.417  1.00 22.08 ? 94  GLY E CA  1 
ATOM   7501  C C   . GLY E 1 94  ? 27.405  21.875  -75.761  1.00 22.09 ? 94  GLY E C   1 
ATOM   7502  O O   . GLY E 1 94  ? 27.592  22.708  -74.871  1.00 22.60 ? 94  GLY E O   1 
ATOM   7503  N N   . THR E 1 95  ? 28.361  21.067  -76.190  1.00 22.48 ? 95  THR E N   1 
ATOM   7504  C CA  . THR E 1 95  ? 29.693  21.087  -75.581  1.00 22.49 ? 95  THR E CA  1 
ATOM   7505  C C   . THR E 1 95  ? 30.391  22.425  -75.875  1.00 22.62 ? 95  THR E C   1 
ATOM   7506  O O   . THR E 1 95  ? 30.907  23.067  -74.955  1.00 24.08 ? 95  THR E O   1 
ATOM   7507  C CB  . THR E 1 95  ? 30.522  19.859  -76.018  1.00 21.92 ? 95  THR E CB  1 
ATOM   7508  O OG1 . THR E 1 95  ? 29.751  18.665  -75.790  1.00 22.50 ? 95  THR E OG1 1 
ATOM   7509  C CG2 . THR E 1 95  ? 31.790  19.764  -75.256  1.00 21.46 ? 95  THR E CG2 1 
ATOM   7510  N N   . ASN E 1 96  ? 30.355  22.875  -77.129  1.00 21.99 ? 96  ASN E N   1 
ATOM   7511  C CA  . ASN E 1 96  ? 30.955  24.169  -77.472  1.00 22.36 ? 96  ASN E CA  1 
ATOM   7512  C C   . ASN E 1 96  ? 30.206  25.369  -76.885  1.00 22.35 ? 96  ASN E C   1 
ATOM   7513  O O   . ASN E 1 96  ? 30.787  26.426  -76.666  1.00 21.70 ? 96  ASN E O   1 
ATOM   7514  C CB  . ASN E 1 96  ? 31.059  24.343  -78.990  1.00 22.75 ? 96  ASN E CB  1 
ATOM   7515  C CG  . ASN E 1 96  ? 32.015  23.356  -79.615  1.00 22.99 ? 96  ASN E CG  1 
ATOM   7516  O OD1 . ASN E 1 96  ? 33.222  23.385  -79.364  1.00 21.64 ? 96  ASN E OD1 1 
ATOM   7517  N ND2 . ASN E 1 96  ? 31.479  22.477  -80.449  1.00 23.44 ? 96  ASN E ND2 1 
ATOM   7518  N N   . ASP E 1 97  ? 28.912  25.197  -76.624  1.00 23.08 ? 97  ASP E N   1 
ATOM   7519  C CA  . ASP E 1 97  ? 28.097  26.265  -76.051  1.00 23.12 ? 97  ASP E CA  1 
ATOM   7520  C C   . ASP E 1 97  ? 28.543  26.681  -74.643  1.00 22.49 ? 97  ASP E C   1 
ATOM   7521  O O   . ASP E 1 97  ? 28.196  27.768  -74.171  1.00 21.30 ? 97  ASP E O   1 
ATOM   7522  C CB  . ASP E 1 97  ? 26.619  25.859  -76.023  1.00 23.82 ? 97  ASP E CB  1 
ATOM   7523  C CG  . ASP E 1 97  ? 26.026  25.642  -77.430  1.00 23.80 ? 97  ASP E CG  1 
ATOM   7524  O OD1 . ASP E 1 97  ? 26.444  24.692  -78.117  1.00 22.63 ? 97  ASP E OD1 1 
ATOM   7525  O OD2 . ASP E 1 97  ? 25.128  26.425  -77.825  1.00 24.16 ? 97  ASP E OD2 1 
ATOM   7526  N N   . THR E 1 98  ? 29.305  25.817  -73.972  1.00 22.72 ? 98  THR E N   1 
ATOM   7527  C CA  . THR E 1 98  ? 29.816  26.108  -72.623  1.00 22.53 ? 98  THR E CA  1 
ATOM   7528  C C   . THR E 1 98  ? 31.069  27.000  -72.638  1.00 22.03 ? 98  THR E C   1 
ATOM   7529  O O   . THR E 1 98  ? 31.511  27.473  -71.582  1.00 21.39 ? 98  THR E O   1 
ATOM   7530  C CB  . THR E 1 98  ? 30.153  24.824  -71.866  1.00 22.27 ? 98  THR E CB  1 
ATOM   7531  O OG1 . THR E 1 98  ? 31.264  24.183  -72.482  1.00 22.33 ? 98  THR E OG1 1 
ATOM   7532  C CG2 . THR E 1 98  ? 28.948  23.868  -71.858  1.00 22.91 ? 98  THR E CG2 1 
ATOM   7533  N N   . LYS E 1 99  ? 31.633  27.222  -73.825  1.00 20.78 ? 99  LYS E N   1 
ATOM   7534  C CA  . LYS E 1 99  ? 32.793  28.097  -73.967  1.00 21.09 ? 99  LYS E CA  1 
ATOM   7535  C C   . LYS E 1 99  ? 32.511  29.460  -73.345  1.00 20.82 ? 99  LYS E C   1 
ATOM   7536  O O   . LYS E 1 99  ? 31.479  30.086  -73.605  1.00 20.20 ? 99  LYS E O   1 
ATOM   7537  C CB  . LYS E 1 99  ? 33.198  28.288  -75.445  1.00 21.87 ? 99  LYS E CB  1 
ATOM   7538  C CG  . LYS E 1 99  ? 33.904  27.077  -76.040  1.00 21.52 ? 99  LYS E CG  1 
ATOM   7539  C CD  . LYS E 1 99  ? 34.168  27.189  -77.532  1.00 21.32 ? 99  LYS E CD  1 
ATOM   7540  C CE  . LYS E 1 99  ? 35.062  26.052  -77.983  1.00 21.53 ? 99  LYS E CE  1 
ATOM   7541  N NZ  . LYS E 1 99  ? 35.010  25.812  -79.461  1.00 22.55 ? 99  LYS E NZ  1 
ATOM   7542  N N   . THR E 1 100 ? 33.462  29.889  -72.532  1.00 20.88 ? 100 THR E N   1 
ATOM   7543  C CA  . THR E 1 100 ? 33.381  31.107  -71.749  1.00 20.91 ? 100 THR E CA  1 
ATOM   7544  C C   . THR E 1 100 ? 32.914  32.320  -72.547  1.00 20.12 ? 100 THR E C   1 
ATOM   7545  O O   . THR E 1 100 ? 31.991  33.001  -72.141  1.00 19.34 ? 100 THR E O   1 
ATOM   7546  C CB  . THR E 1 100 ? 34.773  31.421  -71.106  1.00 21.18 ? 100 THR E CB  1 
ATOM   7547  O OG1 . THR E 1 100 ? 35.014  30.565  -69.982  1.00 20.78 ? 100 THR E OG1 1 
ATOM   7548  C CG2 . THR E 1 100 ? 34.877  32.885  -70.669  1.00 21.48 ? 100 THR E CG2 1 
ATOM   7549  N N   . TYR E 1 101 ? 33.555  32.585  -73.675  1.00 21.19 ? 101 TYR E N   1 
ATOM   7550  C CA  . TYR E 1 101 ? 33.294  33.814  -74.439  1.00 21.25 ? 101 TYR E CA  1 
ATOM   7551  C C   . TYR E 1 101 ? 31.893  33.886  -75.063  1.00 21.49 ? 101 TYR E C   1 
ATOM   7552  O O   . TYR E 1 101 ? 31.466  34.964  -75.438  1.00 21.14 ? 101 TYR E O   1 
ATOM   7553  C CB  . TYR E 1 101 ? 34.379  34.066  -75.504  1.00 20.89 ? 101 TYR E CB  1 
ATOM   7554  C CG  . TYR E 1 101 ? 34.553  32.978  -76.548  1.00 21.22 ? 101 TYR E CG  1 
ATOM   7555  C CD1 . TYR E 1 101 ? 33.687  32.868  -77.633  1.00 21.62 ? 101 TYR E CD1 1 
ATOM   7556  C CD2 . TYR E 1 101 ? 35.598  32.071  -76.468  1.00 21.50 ? 101 TYR E CD2 1 
ATOM   7557  C CE1 . TYR E 1 101 ? 33.860  31.882  -78.599  1.00 21.51 ? 101 TYR E CE1 1 
ATOM   7558  C CE2 . TYR E 1 101 ? 35.781  31.082  -77.419  1.00 21.21 ? 101 TYR E CE2 1 
ATOM   7559  C CZ  . TYR E 1 101 ? 34.908  30.989  -78.486  1.00 21.29 ? 101 TYR E CZ  1 
ATOM   7560  O OH  . TYR E 1 101 ? 35.085  30.010  -79.425  1.00 20.50 ? 101 TYR E OH  1 
ATOM   7561  N N   . LEU E 1 102 ? 31.181  32.765  -75.174  1.00 22.40 ? 102 LEU E N   1 
ATOM   7562  C CA  . LEU E 1 102 ? 29.799  32.797  -75.661  1.00 23.38 ? 102 LEU E CA  1 
ATOM   7563  C C   . LEU E 1 102 ? 28.813  33.201  -74.559  1.00 24.42 ? 102 LEU E C   1 
ATOM   7564  O O   . LEU E 1 102 ? 27.662  33.535  -74.833  1.00 25.06 ? 102 LEU E O   1 
ATOM   7565  C CB  . LEU E 1 102 ? 29.405  31.443  -76.231  1.00 23.19 ? 102 LEU E CB  1 
ATOM   7566  C CG  . LEU E 1 102 ? 30.280  30.936  -77.373  1.00 22.87 ? 102 LEU E CG  1 
ATOM   7567  C CD1 . LEU E 1 102 ? 29.910  29.490  -77.702  1.00 22.54 ? 102 LEU E CD1 1 
ATOM   7568  C CD2 . LEU E 1 102 ? 30.152  31.844  -78.601  1.00 22.66 ? 102 LEU E CD2 1 
ATOM   7569  N N   . ASN E 1 103 ? 29.264  33.128  -73.311  1.00 24.99 ? 103 ASN E N   1 
ATOM   7570  C CA  . ASN E 1 103 ? 28.534  33.696  -72.182  1.00 24.71 ? 103 ASN E CA  1 
ATOM   7571  C C   . ASN E 1 103 ? 27.089  33.160  -72.033  1.00 23.64 ? 103 ASN E C   1 
ATOM   7572  O O   . ASN E 1 103 ? 26.154  33.908  -71.774  1.00 22.36 ? 103 ASN E O   1 
ATOM   7573  C CB  . ASN E 1 103 ? 28.557  35.233  -72.320  1.00 26.05 ? 103 ASN E CB  1 
ATOM   7574  C CG  . ASN E 1 103 ? 27.979  35.936  -71.120  1.00 26.98 ? 103 ASN E CG  1 
ATOM   7575  O OD1 . ASN E 1 103 ? 28.423  35.741  -69.988  1.00 27.06 ? 103 ASN E OD1 1 
ATOM   7576  N ND2 . ASN E 1 103 ? 26.972  36.760  -71.361  1.00 27.82 ? 103 ASN E ND2 1 
ATOM   7577  N N   . ARG E 1 104 ? 26.926  31.849  -72.182  1.00 22.99 ? 104 ARG E N   1 
ATOM   7578  C CA  . ARG E 1 104 ? 25.607  31.221  -72.124  1.00 21.42 ? 104 ARG E CA  1 
ATOM   7579  C C   . ARG E 1 104 ? 25.354  30.529  -70.789  1.00 21.21 ? 104 ARG E C   1 
ATOM   7580  O O   . ARG E 1 104 ? 26.247  29.927  -70.193  1.00 20.96 ? 104 ARG E O   1 
ATOM   7581  C CB  . ARG E 1 104 ? 25.467  30.164  -73.211  1.00 21.99 ? 104 ARG E CB  1 
ATOM   7582  C CG  . ARG E 1 104 ? 26.091  30.521  -74.551  1.00 22.91 ? 104 ARG E CG  1 
ATOM   7583  C CD  . ARG E 1 104 ? 25.415  29.746  -75.680  1.00 23.28 ? 104 ARG E CD  1 
ATOM   7584  N NE  . ARG E 1 104 ? 24.174  30.396  -76.113  1.00 23.09 ? 104 ARG E NE  1 
ATOM   7585  C CZ  . ARG E 1 104 ? 23.351  29.899  -77.028  1.00 23.73 ? 104 ARG E CZ  1 
ATOM   7586  N NH1 . ARG E 1 104 ? 23.598  28.741  -77.640  1.00 23.58 ? 104 ARG E NH1 1 
ATOM   7587  N NH2 . ARG E 1 104 ? 22.270  30.579  -77.344  1.00 24.74 ? 104 ARG E NH2 1 
ATOM   7588  N N   . THR E 1 105 ? 24.115  30.611  -70.332  1.00 20.86 ? 105 THR E N   1 
ATOM   7589  C CA  . THR E 1 105 ? 23.637  29.846  -69.201  1.00 20.44 ? 105 THR E CA  1 
ATOM   7590  C C   . THR E 1 105 ? 23.145  28.510  -69.740  1.00 21.79 ? 105 THR E C   1 
ATOM   7591  O O   . THR E 1 105 ? 22.901  28.379  -70.938  1.00 21.56 ? 105 THR E O   1 
ATOM   7592  C CB  . THR E 1 105 ? 22.455  30.548  -68.534  1.00 19.64 ? 105 THR E CB  1 
ATOM   7593  O OG1 . THR E 1 105 ? 21.315  30.504  -69.403  1.00 19.33 ? 105 THR E OG1 1 
ATOM   7594  C CG2 . THR E 1 105 ? 22.788  31.995  -68.216  1.00 19.25 ? 105 THR E CG2 1 
ATOM   7595  N N   . PRO E 1 106 ? 22.984  27.510  -68.866  1.00 24.00 ? 106 PRO E N   1 
ATOM   7596  C CA  . PRO E 1 106 ? 22.432  26.218  -69.296  1.00 24.48 ? 106 PRO E CA  1 
ATOM   7597  C C   . PRO E 1 106 ? 21.036  26.330  -69.901  1.00 25.13 ? 106 PRO E C   1 
ATOM   7598  O O   . PRO E 1 106 ? 20.759  25.652  -70.892  1.00 26.75 ? 106 PRO E O   1 
ATOM   7599  C CB  . PRO E 1 106 ? 22.379  25.412  -68.000  1.00 24.57 ? 106 PRO E CB  1 
ATOM   7600  C CG  . PRO E 1 106 ? 23.480  25.977  -67.178  1.00 24.29 ? 106 PRO E CG  1 
ATOM   7601  C CD  . PRO E 1 106 ? 23.483  27.455  -67.480  1.00 24.30 ? 106 PRO E CD  1 
ATOM   7602  N N   . PHE E 1 107 ? 20.176  27.175  -69.322  1.00 23.69 ? 107 PHE E N   1 
ATOM   7603  C CA  . PHE E 1 107 ? 18.830  27.391  -69.875  1.00 21.94 ? 107 PHE E CA  1 
ATOM   7604  C C   . PHE E 1 107 ? 18.926  27.973  -71.284  1.00 20.90 ? 107 PHE E C   1 
ATOM   7605  O O   . PHE E 1 107 ? 18.187  27.577  -72.177  1.00 19.12 ? 107 PHE E O   1 
ATOM   7606  C CB  . PHE E 1 107 ? 18.015  28.325  -68.963  1.00 21.69 ? 107 PHE E CB  1 
ATOM   7607  C CG  . PHE E 1 107 ? 16.649  28.659  -69.506  1.00 21.61 ? 107 PHE E CG  1 
ATOM   7608  C CD1 . PHE E 1 107 ? 15.685  27.671  -69.652  1.00 21.53 ? 107 PHE E CD1 1 
ATOM   7609  C CD2 . PHE E 1 107 ? 16.326  29.955  -69.888  1.00 20.63 ? 107 PHE E CD2 1 
ATOM   7610  C CE1 . PHE E 1 107 ? 14.432  27.978  -70.171  1.00 21.38 ? 107 PHE E CE1 1 
ATOM   7611  C CE2 . PHE E 1 107 ? 15.081  30.258  -70.404  1.00 20.18 ? 107 PHE E CE2 1 
ATOM   7612  C CZ  . PHE E 1 107 ? 14.128  29.277  -70.539  1.00 20.52 ? 107 PHE E CZ  1 
ATOM   7613  N N   . GLU E 1 108 ? 19.850  28.892  -71.482  1.00 20.88 ? 108 GLU E N   1 
ATOM   7614  C CA  . GLU E 1 108 ? 20.065  29.478  -72.806  1.00 21.32 ? 108 GLU E CA  1 
ATOM   7615  C C   . GLU E 1 108 ? 20.447  28.384  -73.808  1.00 21.39 ? 108 GLU E C   1 
ATOM   7616  O O   . GLU E 1 108 ? 20.007  28.397  -74.955  1.00 22.42 ? 108 GLU E O   1 
ATOM   7617  C CB  . GLU E 1 108 ? 21.209  30.510  -72.786  1.00 21.80 ? 108 GLU E CB  1 
ATOM   7618  C CG  . GLU E 1 108 ? 21.024  31.957  -73.257  1.00 22.14 ? 108 GLU E CG  1 
ATOM   7619  C CD  . GLU E 1 108 ? 22.198  32.449  -74.033  1.00 22.41 ? 108 GLU E CD  1 
ATOM   7620  O OE1 . GLU E 1 108 ? 21.928  33.022  -75.090  1.00 23.67 ? 108 GLU E OE1 1 
ATOM   7621  O OE2 . GLU E 1 108 ? 23.342  32.238  -73.671  1.00 24.54 ? 108 GLU E OE2 1 
ATOM   7622  N N   . ILE E 1 109 ? 21.281  27.448  -73.369  1.00 21.28 ? 109 ILE E N   1 
ATOM   7623  C CA  . ILE E 1 109 ? 21.766  26.393  -74.238  1.00 21.31 ? 109 ILE E CA  1 
ATOM   7624  C C   . ILE E 1 109 ? 20.622  25.437  -74.562  1.00 19.99 ? 109 ILE E C   1 
ATOM   7625  O O   . ILE E 1 109 ? 20.486  24.978  -75.704  1.00 20.83 ? 109 ILE E O   1 
ATOM   7626  C CB  . ILE E 1 109 ? 22.976  25.656  -73.625  1.00 21.77 ? 109 ILE E CB  1 
ATOM   7627  C CG1 . ILE E 1 109 ? 24.133  26.651  -73.367  1.00 22.23 ? 109 ILE E CG1 1 
ATOM   7628  C CG2 . ILE E 1 109 ? 23.446  24.548  -74.567  1.00 21.76 ? 109 ILE E CG2 1 
ATOM   7629  C CD1 . ILE E 1 109 ? 25.229  26.135  -72.461  1.00 21.95 ? 109 ILE E CD1 1 
ATOM   7630  N N   . GLY E 1 110 ? 19.787  25.160  -73.572  1.00 18.40 ? 110 GLY E N   1 
ATOM   7631  C CA  . GLY E 1 110 ? 18.556  24.419  -73.809  1.00 17.76 ? 110 GLY E CA  1 
ATOM   7632  C C   . GLY E 1 110 ? 17.674  25.059  -74.874  1.00 17.19 ? 110 GLY E C   1 
ATOM   7633  O O   . GLY E 1 110 ? 17.195  24.370  -75.788  1.00 17.79 ? 110 GLY E O   1 
ATOM   7634  N N   . LEU E 1 111 ? 17.468  26.375  -74.767  1.00 16.26 ? 111 LEU E N   1 
ATOM   7635  C CA  . LEU E 1 111 ? 16.702  27.115  -75.768  1.00 15.59 ? 111 LEU E CA  1 
ATOM   7636  C C   . LEU E 1 111 ? 17.294  26.954  -77.160  1.00 15.77 ? 111 LEU E C   1 
ATOM   7637  O O   . LEU E 1 111 ? 16.556  26.868  -78.153  1.00 15.21 ? 111 LEU E O   1 
ATOM   7638  C CB  . LEU E 1 111 ? 16.642  28.602  -75.414  1.00 15.07 ? 111 LEU E CB  1 
ATOM   7639  C CG  . LEU E 1 111 ? 15.789  28.957  -74.218  1.00 15.12 ? 111 LEU E CG  1 
ATOM   7640  C CD1 . LEU E 1 111 ? 15.922  30.440  -73.914  1.00 15.16 ? 111 LEU E CD1 1 
ATOM   7641  C CD2 . LEU E 1 111 ? 14.338  28.584  -74.462  1.00 14.98 ? 111 LEU E CD2 1 
ATOM   7642  N N   . GLY E 1 112 ? 18.629  26.916  -77.220  1.00 16.45 ? 112 GLY E N   1 
ATOM   7643  C CA  . GLY E 1 112 ? 19.337  26.744  -78.477  1.00 16.50 ? 112 GLY E CA  1 
ATOM   7644  C C   . GLY E 1 112 ? 19.035  25.407  -79.086  1.00 16.59 ? 112 GLY E C   1 
ATOM   7645  O O   . GLY E 1 112 ? 18.723  25.325  -80.285  1.00 16.54 ? 112 GLY E O   1 
ATOM   7646  N N   . ALA E 1 113 ? 19.120  24.359  -78.262  1.00 16.57 ? 113 ALA E N   1 
ATOM   7647  C CA  . ALA E 1 113 ? 18.754  23.018  -78.710  1.00 17.05 ? 113 ALA E CA  1 
ATOM   7648  C C   . ALA E 1 113 ? 17.299  23.010  -79.125  1.00 17.34 ? 113 ALA E C   1 
ATOM   7649  O O   . ALA E 1 113 ? 16.953  22.398  -80.130  1.00 17.51 ? 113 ALA E O   1 
ATOM   7650  C CB  . ALA E 1 113 ? 18.993  21.987  -77.622  1.00 17.12 ? 113 ALA E CB  1 
ATOM   7651  N N   . GLY E 1 114 ? 16.455  23.699  -78.357  1.00 17.47 ? 114 GLY E N   1 
ATOM   7652  C CA  . GLY E 1 114 ? 15.039  23.873  -78.711  1.00 17.94 ? 114 GLY E CA  1 
ATOM   7653  C C   . GLY E 1 114 ? 14.805  24.512  -80.072  1.00 18.14 ? 114 GLY E C   1 
ATOM   7654  O O   . GLY E 1 114 ? 13.942  24.079  -80.838  1.00 17.40 ? 114 GLY E O   1 
ATOM   7655  N N   . ALA E 1 115 ? 15.583  25.545  -80.375  1.00 18.84 ? 115 ALA E N   1 
ATOM   7656  C CA  . ALA E 1 115 ? 15.526  26.189  -81.687  1.00 19.18 ? 115 ALA E CA  1 
ATOM   7657  C C   . ALA E 1 115 ? 15.776  25.182  -82.799  1.00 18.78 ? 115 ALA E C   1 
ATOM   7658  O O   . ALA E 1 115 ? 15.142  25.253  -83.855  1.00 18.99 ? 115 ALA E O   1 
ATOM   7659  C CB  . ALA E 1 115 ? 16.544  27.320  -81.768  1.00 19.99 ? 115 ALA E CB  1 
ATOM   7660  N N   . LEU E 1 116 ? 16.706  24.263  -82.565  1.00 18.28 ? 116 LEU E N   1 
ATOM   7661  C CA  . LEU E 1 116 ? 17.014  23.237  -83.557  1.00 18.96 ? 116 LEU E CA  1 
ATOM   7662  C C   . LEU E 1 116 ? 15.869  22.232  -83.691  1.00 18.81 ? 116 LEU E C   1 
ATOM   7663  O O   . LEU E 1 116 ? 15.494  21.857  -84.793  1.00 18.76 ? 116 LEU E O   1 
ATOM   7664  C CB  . LEU E 1 116 ? 18.340  22.524  -83.238  1.00 18.83 ? 116 LEU E CB  1 
ATOM   7665  C CG  . LEU E 1 116 ? 19.587  23.433  -83.252  1.00 19.00 ? 116 LEU E CG  1 
ATOM   7666  C CD1 . LEU E 1 116 ? 20.822  22.631  -82.880  1.00 19.21 ? 116 LEU E CD1 1 
ATOM   7667  C CD2 . LEU E 1 116 ? 19.783  24.113  -84.592  1.00 18.72 ? 116 LEU E CD2 1 
ATOM   7668  N N   . ILE E 1 117 ? 15.303  21.813  -82.568  1.00 18.80 ? 117 ILE E N   1 
ATOM   7669  C CA  . ILE E 1 117 ? 14.150  20.906  -82.586  1.00 18.83 ? 117 ILE E CA  1 
ATOM   7670  C C   . ILE E 1 117 ? 13.014  21.520  -83.404  1.00 18.06 ? 117 ILE E C   1 
ATOM   7671  O O   . ILE E 1 117 ? 12.407  20.853  -84.257  1.00 16.85 ? 117 ILE E O   1 
ATOM   7672  C CB  . ILE E 1 117 ? 13.652  20.552  -81.165  1.00 18.80 ? 117 ILE E CB  1 
ATOM   7673  C CG1 . ILE E 1 117 ? 14.693  19.676  -80.447  1.00 19.17 ? 117 ILE E CG1 1 
ATOM   7674  C CG2 . ILE E 1 117 ? 12.358  19.775  -81.253  1.00 18.50 ? 117 ILE E CG2 1 
ATOM   7675  C CD1 . ILE E 1 117 ? 14.496  19.606  -78.946  1.00 19.44 ? 117 ILE E CD1 1 
ATOM   7676  N N   . ASN E 1 118 ? 12.751  22.797  -83.143  1.00 17.73 ? 118 ASN E N   1 
ATOM   7677  C CA  . ASN E 1 118 ? 11.743  23.537  -83.891  1.00 17.76 ? 118 ASN E CA  1 
ATOM   7678  C C   . ASN E 1 118 ? 12.024  23.557  -85.402  1.00 17.74 ? 118 ASN E C   1 
ATOM   7679  O O   . ASN E 1 118 ? 11.110  23.404  -86.208  1.00 17.13 ? 118 ASN E O   1 
ATOM   7680  C CB  . ASN E 1 118 ? 11.624  24.957  -83.352  1.00 17.83 ? 118 ASN E CB  1 
ATOM   7681  C CG  . ASN E 1 118 ? 10.465  25.711  -83.961  1.00 18.10 ? 118 ASN E CG  1 
ATOM   7682  O OD1 . ASN E 1 118 ? 9.356   25.173  -84.143  1.00 19.12 ? 118 ASN E OD1 1 
ATOM   7683  N ND2 . ASN E 1 118 ? 10.714  26.955  -84.294  1.00 17.82 ? 118 ASN E ND2 1 
ATOM   7684  N N   . MET E 1 119 ? 13.281  23.749  -85.793  1.00 17.52 ? 119 MET E N   1 
ATOM   7685  C CA  . MET E 1 119 ? 13.633  23.693  -87.215  1.00 16.94 ? 119 MET E CA  1 
ATOM   7686  C C   . MET E 1 119 ? 13.305  22.343  -87.837  1.00 16.40 ? 119 MET E C   1 
ATOM   7687  O O   . MET E 1 119 ? 12.842  22.282  -88.967  1.00 16.71 ? 119 MET E O   1 
ATOM   7688  C CB  . MET E 1 119 ? 15.109  24.043  -87.417  1.00 16.79 ? 119 MET E CB  1 
ATOM   7689  C CG  . MET E 1 119 ? 15.377  25.525  -87.291  1.00 16.56 ? 119 MET E CG  1 
ATOM   7690  S SD  . MET E 1 119 ? 17.133  25.857  -87.188  1.00 16.74 ? 119 MET E SD  1 
ATOM   7691  C CE  . MET E 1 119 ? 17.120  27.616  -87.640  1.00 17.52 ? 119 MET E CE  1 
ATOM   7692  N N   . VAL E 1 120 ? 13.538  21.272  -87.090  1.00 16.28 ? 120 VAL E N   1 
ATOM   7693  C CA  . VAL E 1 120 ? 13.202  19.920  -87.547  1.00 16.30 ? 120 VAL E CA  1 
ATOM   7694  C C   . VAL E 1 120 ? 11.678  19.761  -87.666  1.00 16.79 ? 120 VAL E C   1 
ATOM   7695  O O   . VAL E 1 120 ? 11.197  19.141  -88.603  1.00 16.86 ? 120 VAL E O   1 
ATOM   7696  C CB  . VAL E 1 120 ? 13.752  18.827  -86.595  1.00 15.80 ? 120 VAL E CB  1 
ATOM   7697  C CG1 . VAL E 1 120 ? 13.332  17.441  -87.081  1.00 16.01 ? 120 VAL E CG1 1 
ATOM   7698  C CG2 . VAL E 1 120 ? 15.276  18.924  -86.498  1.00 15.74 ? 120 VAL E CG2 1 
ATOM   7699  N N   . GLN E 1 121 ? 10.927  20.313  -86.716  1.00 16.92 ? 121 GLN E N   1 
ATOM   7700  C CA  . GLN E 1 121 ? 9.468   20.176  -86.721  1.00 16.66 ? 121 GLN E CA  1 
ATOM   7701  C C   . GLN E 1 121 ? 8.808   20.951  -87.860  1.00 17.39 ? 121 GLN E C   1 
ATOM   7702  O O   . GLN E 1 121 ? 7.781   20.531  -88.388  1.00 17.35 ? 121 GLN E O   1 
ATOM   7703  C CB  . GLN E 1 121 ? 8.877   20.596  -85.375  1.00 16.07 ? 121 GLN E CB  1 
ATOM   7704  C CG  . GLN E 1 121 ? 9.198   19.611  -84.277  1.00 15.70 ? 121 GLN E CG  1 
ATOM   7705  C CD  . GLN E 1 121 ? 8.620   19.989  -82.943  1.00 15.30 ? 121 GLN E CD  1 
ATOM   7706  O OE1 . GLN E 1 121 ? 8.190   21.125  -82.747  1.00 15.79 ? 121 GLN E OE1 1 
ATOM   7707  N NE2 . GLN E 1 121 ? 8.671   19.060  -81.994  1.00 14.90 ? 121 GLN E NE2 1 
ATOM   7708  N N   . LYS E 1 122 ? 9.413   22.067  -88.241  1.00 17.99 ? 122 LYS E N   1 
ATOM   7709  C CA  . LYS E 1 122 ? 8.954   22.853  -89.380  1.00 18.48 ? 122 LYS E CA  1 
ATOM   7710  C C   . LYS E 1 122 ? 9.709   22.479  -90.653  1.00 18.77 ? 122 LYS E C   1 
ATOM   7711  O O   . LYS E 1 122 ? 9.693   23.220  -91.631  1.00 18.40 ? 122 LYS E O   1 
ATOM   7712  C CB  . LYS E 1 122 ? 9.174   24.333  -89.088  1.00 18.70 ? 122 LYS E CB  1 
ATOM   7713  C CG  . LYS E 1 122 ? 8.528   24.825  -87.812  1.00 18.99 ? 122 LYS E CG  1 
ATOM   7714  C CD  . LYS E 1 122 ? 8.902   26.271  -87.518  1.00 18.57 ? 122 LYS E CD  1 
ATOM   7715  C CE  . LYS E 1 122 ? 8.045   27.221  -88.352  1.00 17.85 ? 122 LYS E CE  1 
ATOM   7716  N NZ  . LYS E 1 122 ? 8.548   28.598  -88.337  1.00 17.13 ? 122 LYS E NZ  1 
ATOM   7717  N N   . SER E 1 123 ? 10.368  21.321  -90.641  1.00 20.25 ? 123 SER E N   1 
ATOM   7718  C CA  . SER E 1 123 ? 11.282  20.886  -91.704  1.00 20.50 ? 123 SER E CA  1 
ATOM   7719  C C   . SER E 1 123 ? 10.563  20.695  -93.023  1.00 21.09 ? 123 SER E C   1 
ATOM   7720  O O   . SER E 1 123 ? 9.381   20.318  -93.024  1.00 20.47 ? 123 SER E O   1 
ATOM   7721  C CB  . SER E 1 123 ? 11.950  19.588  -91.306  1.00 20.73 ? 123 SER E CB  1 
ATOM   7722  O OG  . SER E 1 123 ? 13.243  19.572  -91.825  1.00 22.14 ? 123 SER E OG  1 
ATOM   7723  N N   . PRO E 1 124 ? 11.339  20.702  -94.129  1.00 21.94 ? 124 PRO E N   1 
ATOM   7724  C CA  . PRO E 1 124 ? 11.419  21.591  -95.295  1.00 21.79 ? 124 PRO E CA  1 
ATOM   7725  C C   . PRO E 1 124 ? 10.449  22.728  -95.152  1.00 22.65 ? 124 PRO E C   1 
ATOM   7726  O O   . PRO E 1 124 ? 9.350   22.528  -94.662  1.00 25.98 ? 124 PRO E O   1 
ATOM   7727  C CB  . PRO E 1 124 ? 11.006  20.673  -96.461  1.00 21.35 ? 124 PRO E CB  1 
ATOM   7728  C CG  . PRO E 1 124 ? 10.264  19.578  -95.832  1.00 20.84 ? 124 PRO E CG  1 
ATOM   7729  C CD  . PRO E 1 124 ? 11.131  19.332  -94.628  1.00 21.57 ? 124 PRO E CD  1 
ATOM   7730  N N   . GLY E 1 125 ? 10.788  23.916  -95.584  1.00 22.08 ? 125 GLY E N   1 
ATOM   7731  C CA  . GLY E 1 125 ? 9.804   24.982  -95.472  1.00 22.08 ? 125 GLY E CA  1 
ATOM   7732  C C   . GLY E 1 125 ? 8.895   25.113  -96.682  1.00 21.87 ? 125 GLY E C   1 
ATOM   7733  O O   . GLY E 1 125 ? 8.640   26.223  -97.116  1.00 22.89 ? 125 GLY E O   1 
ATOM   7734  N N   . TRP E 1 126 ? 8.399   24.009  -97.247  1.00 21.29 ? 126 TRP E N   1 
ATOM   7735  C CA  . TRP E 1 126 ? 7.830   24.078  -98.597  1.00 21.21 ? 126 TRP E CA  1 
ATOM   7736  C C   . TRP E 1 126 ? 6.819   23.023  -99.064  1.00 22.56 ? 126 TRP E C   1 
ATOM   7737  O O   . TRP E 1 126 ? 6.709   21.910  -98.516  1.00 22.99 ? 126 TRP E O   1 
ATOM   7738  C CB  . TRP E 1 126 ? 8.968   24.166  -99.628  1.00 20.04 ? 126 TRP E CB  1 
ATOM   7739  C CG  . TRP E 1 126 ? 9.917   22.968  -99.699  1.00 19.30 ? 126 TRP E CG  1 
ATOM   7740  C CD1 . TRP E 1 126 ? 9.597   21.642  -99.606  1.00 18.80 ? 126 TRP E CD1 1 
ATOM   7741  C CD2 . TRP E 1 126 ? 11.333  23.017  -99.948  1.00 18.51 ? 126 TRP E CD2 1 
ATOM   7742  N NE1 . TRP E 1 126 ? 10.712  20.876  -99.777  1.00 18.90 ? 126 TRP E NE1 1 
ATOM   7743  C CE2 . TRP E 1 126 ? 11.794  21.691  -99.991  1.00 18.06 ? 126 TRP E CE2 1 
ATOM   7744  C CE3 . TRP E 1 126 ? 12.245  24.061  -100.153 1.00 18.48 ? 126 TRP E CE3 1 
ATOM   7745  C CZ2 . TRP E 1 126 ? 13.138  21.372  -100.180 1.00 17.58 ? 126 TRP E CZ2 1 
ATOM   7746  C CZ3 . TRP E 1 126 ? 13.571  23.747  -100.373 1.00 18.28 ? 126 TRP E CZ3 1 
ATOM   7747  C CH2 . TRP E 1 126 ? 14.006  22.406  -100.379 1.00 18.01 ? 126 TRP E CH2 1 
ATOM   7748  N N   . ASP E 1 127 ? 6.080   23.392  -100.098 1.00 24.51 ? 127 ASP E N   1 
ATOM   7749  C CA  . ASP E 1 127 ? 5.149   22.489  -100.805 1.00 25.45 ? 127 ASP E CA  1 
ATOM   7750  C C   . ASP E 1 127 ? 5.830   21.618  -101.878 1.00 23.09 ? 127 ASP E C   1 
ATOM   7751  O O   . ASP E 1 127 ? 5.156   20.803  -102.498 1.00 22.44 ? 127 ASP E O   1 
ATOM   7752  C CB  . ASP E 1 127 ? 3.984   23.280  -101.432 1.00 27.91 ? 127 ASP E CB  1 
ATOM   7753  C CG  . ASP E 1 127 ? 4.459   24.428  -102.374 1.00 32.05 ? 127 ASP E CG  1 
ATOM   7754  O OD1 . ASP E 1 127 ? 5.708   24.710  -102.488 1.00 36.02 ? 127 ASP E OD1 1 
ATOM   7755  O OD2 . ASP E 1 127 ? 3.563   25.084  -102.940 1.00 33.23 ? 127 ASP E OD2 1 
ATOM   7756  N N   . TRP E 1 128 ? 7.133   21.774  -102.098 1.00 20.85 ? 128 TRP E N   1 
ATOM   7757  C CA  . TRP E 1 128 ? 7.831   21.039  -103.162 1.00 20.16 ? 128 TRP E CA  1 
ATOM   7758  C C   . TRP E 1 128 ? 7.850   19.519  -102.941 1.00 20.33 ? 128 TRP E C   1 
ATOM   7759  O O   . TRP E 1 128 ? 7.896   18.746  -103.887 1.00 19.97 ? 128 TRP E O   1 
ATOM   7760  C CB  . TRP E 1 128 ? 9.273   21.537  -103.335 1.00 19.49 ? 128 TRP E CB  1 
ATOM   7761  C CG  . TRP E 1 128 ? 9.384   22.980  -103.764 1.00 19.70 ? 128 TRP E CG  1 
ATOM   7762  C CD1 . TRP E 1 128 ? 8.374   23.796  -104.141 1.00 19.33 ? 128 TRP E CD1 1 
ATOM   7763  C CD2 . TRP E 1 128 ? 10.590  23.773  -103.847 1.00 19.49 ? 128 TRP E CD2 1 
ATOM   7764  N NE1 . TRP E 1 128 ? 8.865   25.036  -104.461 1.00 19.02 ? 128 TRP E NE1 1 
ATOM   7765  C CE2 . TRP E 1 128 ? 10.217  25.052  -104.289 1.00 18.73 ? 128 TRP E CE2 1 
ATOM   7766  C CE3 . TRP E 1 128 ? 11.948  23.517  -103.582 1.00 20.05 ? 128 TRP E CE3 1 
ATOM   7767  C CZ2 . TRP E 1 128 ? 11.135  26.081  -104.481 1.00 19.26 ? 128 TRP E CZ2 1 
ATOM   7768  C CZ3 . TRP E 1 128 ? 12.866  24.529  -103.788 1.00 20.15 ? 128 TRP E CZ3 1 
ATOM   7769  C CH2 . TRP E 1 128 ? 12.455  25.805  -104.227 1.00 20.11 ? 128 TRP E CH2 1 
ATOM   7770  N N   . THR E 1 129 ? 7.847   19.120  -101.678 1.00 21.24 ? 129 THR E N   1 
ATOM   7771  C CA  . THR E 1 129 ? 7.716   17.734  -101.264 1.00 21.67 ? 129 THR E CA  1 
ATOM   7772  C C   . THR E 1 129 ? 6.665   17.744  -100.171 1.00 22.67 ? 129 THR E C   1 
ATOM   7773  O O   . THR E 1 129 ? 6.442   18.794  -99.544  1.00 23.49 ? 129 THR E O   1 
ATOM   7774  C CB  . THR E 1 129 ? 9.039   17.169  -100.665 1.00 21.80 ? 129 THR E CB  1 
ATOM   7775  O OG1 . THR E 1 129 ? 9.443   17.921  -99.506  1.00 20.69 ? 129 THR E OG1 1 
ATOM   7776  C CG2 . THR E 1 129 ? 10.151  17.214  -101.678 1.00 21.71 ? 129 THR E CG2 1 
ATOM   7777  N N   . ASP E 1 130 ? 6.003   16.618  -99.933  1.00 23.44 ? 130 ASP E N   1 
ATOM   7778  C CA  . ASP E 1 130 ? 5.340   16.496  -98.641  1.00 25.04 ? 130 ASP E CA  1 
ATOM   7779  C C   . ASP E 1 130 ? 5.486   15.113  -98.032  1.00 23.88 ? 130 ASP E C   1 
ATOM   7780  O O   . ASP E 1 130 ? 4.626   14.257  -98.123  1.00 21.28 ? 130 ASP E O   1 
ATOM   7781  C CB  . ASP E 1 130 ? 3.907   17.129  -98.564  1.00 26.15 ? 130 ASP E CB  1 
ATOM   7782  C CG  . ASP E 1 130 ? 2.792   16.141  -98.690  1.00 26.36 ? 130 ASP E CG  1 
ATOM   7783  O OD1 . ASP E 1 130 ? 2.636   15.570  -99.773  1.00 27.02 ? 130 ASP E OD1 1 
ATOM   7784  O OD2 . ASP E 1 130 ? 2.024   15.973  -97.714  1.00 27.28 ? 130 ASP E OD2 1 
ATOM   7785  N N   . TYR E 1 131 ? 6.654   14.953  -97.418  1.00 23.93 ? 131 TYR E N   1 
ATOM   7786  C CA  . TYR E 1 131 ? 6.912   13.943  -96.434  1.00 22.66 ? 131 TYR E CA  1 
ATOM   7787  C C   . TYR E 1 131 ? 6.657   14.590  -95.067  1.00 22.40 ? 131 TYR E C   1 
ATOM   7788  O O   . TYR E 1 131 ? 6.765   15.802  -94.920  1.00 23.72 ? 131 TYR E O   1 
ATOM   7789  C CB  . TYR E 1 131 ? 8.369   13.525  -96.507  1.00 21.86 ? 131 TYR E CB  1 
ATOM   7790  C CG  . TYR E 1 131 ? 8.835   12.950  -97.832  1.00 21.24 ? 131 TYR E CG  1 
ATOM   7791  C CD1 . TYR E 1 131 ? 8.698   11.598  -98.107  1.00 20.85 ? 131 TYR E CD1 1 
ATOM   7792  C CD2 . TYR E 1 131 ? 9.465   13.755  -98.794  1.00 21.38 ? 131 TYR E CD2 1 
ATOM   7793  C CE1 . TYR E 1 131 ? 9.147   11.052  -99.302  1.00 20.47 ? 131 TYR E CE1 1 
ATOM   7794  C CE2 . TYR E 1 131 ? 9.913   13.220  -99.990  1.00 21.08 ? 131 TYR E CE2 1 
ATOM   7795  C CZ  . TYR E 1 131 ? 9.751   11.852  -100.233 1.00 20.60 ? 131 TYR E CZ  1 
ATOM   7796  O OH  . TYR E 1 131 ? 10.199  11.271  -101.394 1.00 19.72 ? 131 TYR E OH  1 
ATOM   7797  N N   . PRO E 1 132 ? 6.318   13.789  -94.057  1.00 22.12 ? 132 PRO E N   1 
ATOM   7798  C CA  . PRO E 1 132 ? 6.177   14.366  -92.731  1.00 21.60 ? 132 PRO E CA  1 
ATOM   7799  C C   . PRO E 1 132 ? 7.527   14.807  -92.162  1.00 21.71 ? 132 PRO E C   1 
ATOM   7800  O O   . PRO E 1 132 ? 8.574   14.421  -92.683  1.00 21.80 ? 132 PRO E O   1 
ATOM   7801  C CB  . PRO E 1 132 ? 5.625   13.204  -91.910  1.00 22.13 ? 132 PRO E CB  1 
ATOM   7802  C CG  . PRO E 1 132 ? 6.139   11.985  -92.597  1.00 22.90 ? 132 PRO E CG  1 
ATOM   7803  C CD  . PRO E 1 132 ? 6.104   12.331  -94.054  1.00 22.92 ? 132 PRO E CD  1 
ATOM   7804  N N   . PRO E 1 133 ? 7.514   15.616  -91.091  1.00 21.64 ? 133 PRO E N   1 
ATOM   7805  C CA  . PRO E 1 133 ? 8.782   15.884  -90.426  1.00 21.23 ? 133 PRO E CA  1 
ATOM   7806  C C   . PRO E 1 133 ? 9.185   14.713  -89.525  1.00 20.45 ? 133 PRO E C   1 
ATOM   7807  O O   . PRO E 1 133 ? 8.319   14.027  -88.988  1.00 20.20 ? 133 PRO E O   1 
ATOM   7808  C CB  . PRO E 1 133 ? 8.492   17.147  -89.617  1.00 21.06 ? 133 PRO E CB  1 
ATOM   7809  C CG  . PRO E 1 133 ? 7.013   17.241  -89.515  1.00 21.47 ? 133 PRO E CG  1 
ATOM   7810  C CD  . PRO E 1 133 ? 6.377   16.182  -90.354  1.00 21.33 ? 133 PRO E CD  1 
ATOM   7811  N N   . PRO E 1 134 ? 10.491  14.477  -89.355  1.00 19.81 ? 134 PRO E N   1 
ATOM   7812  C CA  . PRO E 1 134 ? 10.872  13.318  -88.543  1.00 19.38 ? 134 PRO E CA  1 
ATOM   7813  C C   . PRO E 1 134 ? 10.884  13.628  -87.055  1.00 18.55 ? 134 PRO E C   1 
ATOM   7814  O O   . PRO E 1 134 ? 11.045  14.789  -86.679  1.00 18.11 ? 134 PRO E O   1 
ATOM   7815  C CB  . PRO E 1 134 ? 12.301  13.018  -89.022  1.00 19.58 ? 134 PRO E CB  1 
ATOM   7816  C CG  . PRO E 1 134 ? 12.778  14.260  -89.733  1.00 19.63 ? 134 PRO E CG  1 
ATOM   7817  C CD  . PRO E 1 134 ? 11.659  15.263  -89.787  1.00 19.64 ? 134 PRO E CD  1 
ATOM   7818  N N   . PRO E 1 135 ? 10.740  12.606  -86.204  1.00 18.74 ? 135 PRO E N   1 
ATOM   7819  C CA  . PRO E 1 135 ? 10.928  12.820  -84.757  1.00 19.22 ? 135 PRO E CA  1 
ATOM   7820  C C   . PRO E 1 135 ? 12.379  13.174  -84.420  1.00 19.39 ? 135 PRO E C   1 
ATOM   7821  O O   . PRO E 1 135 ? 13.262  13.025  -85.273  1.00 21.12 ? 135 PRO E O   1 
ATOM   7822  C CB  . PRO E 1 135 ? 10.546  11.467  -84.145  1.00 18.69 ? 135 PRO E CB  1 
ATOM   7823  C CG  . PRO E 1 135 ? 10.860  10.486  -85.230  1.00 18.72 ? 135 PRO E CG  1 
ATOM   7824  C CD  . PRO E 1 135 ? 10.472  11.193  -86.511  1.00 18.90 ? 135 PRO E CD  1 
ATOM   7825  N N   . VAL E 1 136 ? 12.618  13.647  -83.196  1.00 18.79 ? 136 VAL E N   1 
ATOM   7826  C CA  . VAL E 1 136 ? 13.955  14.089  -82.792  1.00 18.52 ? 136 VAL E CA  1 
ATOM   7827  C C   . VAL E 1 136 ? 14.349  13.427  -81.485  1.00 18.80 ? 136 VAL E C   1 
ATOM   7828  O O   . VAL E 1 136 ? 13.551  13.360  -80.561  1.00 19.67 ? 136 VAL E O   1 
ATOM   7829  C CB  . VAL E 1 136 ? 14.035  15.612  -82.621  1.00 18.33 ? 136 VAL E CB  1 
ATOM   7830  C CG1 . VAL E 1 136 ? 15.419  16.030  -82.106  1.00 18.58 ? 136 VAL E CG1 1 
ATOM   7831  C CG2 . VAL E 1 136 ? 13.720  16.318  -83.923  1.00 18.19 ? 136 VAL E CG2 1 
ATOM   7832  N N   . LEU E 1 137 ? 15.575  12.921  -81.442  1.00 19.45 ? 137 LEU E N   1 
ATOM   7833  C CA  . LEU E 1 137 ? 16.201  12.464  -80.208  1.00 20.34 ? 137 LEU E CA  1 
ATOM   7834  C C   . LEU E 1 137 ? 17.307  13.453  -79.854  1.00 20.93 ? 137 LEU E C   1 
ATOM   7835  O O   . LEU E 1 137 ? 18.361  13.492  -80.513  1.00 22.04 ? 137 LEU E O   1 
ATOM   7836  C CB  . LEU E 1 137 ? 16.791  11.055  -80.396  1.00 20.43 ? 137 LEU E CB  1 
ATOM   7837  C CG  . LEU E 1 137 ? 17.725  10.508  -79.301  1.00 20.51 ? 137 LEU E CG  1 
ATOM   7838  C CD1 . LEU E 1 137 ? 17.042  10.431  -77.934  1.00 20.49 ? 137 LEU E CD1 1 
ATOM   7839  C CD2 . LEU E 1 137 ? 18.222  9.119   -79.694  1.00 20.55 ? 137 LEU E CD2 1 
ATOM   7840  N N   . LEU E 1 138 ? 17.062  14.261  -78.821  1.00 20.81 ? 138 LEU E N   1 
ATOM   7841  C CA  . LEU E 1 138 ? 18.050  15.224  -78.350  1.00 20.55 ? 138 LEU E CA  1 
ATOM   7842  C C   . LEU E 1 138 ? 18.952  14.503  -77.363  1.00 21.80 ? 138 LEU E C   1 
ATOM   7843  O O   . LEU E 1 138 ? 18.469  13.929  -76.383  1.00 22.08 ? 138 LEU E O   1 
ATOM   7844  C CB  . LEU E 1 138 ? 17.389  16.403  -77.662  1.00 19.86 ? 138 LEU E CB  1 
ATOM   7845  C CG  . LEU E 1 138 ? 18.358  17.430  -77.062  1.00 19.56 ? 138 LEU E CG  1 
ATOM   7846  C CD1 . LEU E 1 138 ? 19.230  18.032  -78.141  1.00 19.32 ? 138 LEU E CD1 1 
ATOM   7847  C CD2 . LEU E 1 138 ? 17.573  18.514  -76.332  1.00 20.12 ? 138 LEU E CD2 1 
ATOM   7848  N N   . ILE E 1 139 ? 20.261  14.532  -77.625  1.00 22.31 ? 139 ILE E N   1 
ATOM   7849  C CA  . ILE E 1 139 ? 21.239  13.894  -76.750  1.00 22.00 ? 139 ILE E CA  1 
ATOM   7850  C C   . ILE E 1 139 ? 22.084  14.966  -76.065  1.00 21.65 ? 139 ILE E C   1 
ATOM   7851  O O   . ILE E 1 139 ? 22.737  15.777  -76.710  1.00 20.94 ? 139 ILE E O   1 
ATOM   7852  C CB  . ILE E 1 139 ? 22.148  12.904  -77.495  1.00 22.04 ? 139 ILE E CB  1 
ATOM   7853  C CG1 . ILE E 1 139 ? 21.306  11.800  -78.145  1.00 21.76 ? 139 ILE E CG1 1 
ATOM   7854  C CG2 . ILE E 1 139 ? 23.139  12.267  -76.537  1.00 21.83 ? 139 ILE E CG2 1 
ATOM   7855  C CD1 . ILE E 1 139 ? 22.107  10.760  -78.925  1.00 21.20 ? 139 ILE E CD1 1 
ATOM   7856  N N   . SER E 1 140 ? 22.065  14.953  -74.743  1.00 22.06 ? 140 SER E N   1 
ATOM   7857  C CA  . SER E 1 140 ? 22.914  15.812  -73.966  1.00 22.07 ? 140 SER E CA  1 
ATOM   7858  C C   . SER E 1 140 ? 24.290  15.172  -73.882  1.00 20.95 ? 140 SER E C   1 
ATOM   7859  O O   . SER E 1 140 ? 24.380  13.980  -73.644  1.00 21.58 ? 140 SER E O   1 
ATOM   7860  C CB  . SER E 1 140 ? 22.308  15.985  -72.579  1.00 22.73 ? 140 SER E CB  1 
ATOM   7861  O OG  . SER E 1 140 ? 23.307  15.977  -71.613  1.00 24.75 ? 140 SER E OG  1 
ATOM   7862  N N   . PRO E 1 141 ? 25.362  15.954  -74.064  1.00 20.61 ? 141 PRO E N   1 
ATOM   7863  C CA  . PRO E 1 141 ? 26.697  15.402  -73.941  1.00 21.36 ? 141 PRO E CA  1 
ATOM   7864  C C   . PRO E 1 141 ? 27.085  15.204  -72.485  1.00 22.78 ? 141 PRO E C   1 
ATOM   7865  O O   . PRO E 1 141 ? 26.426  15.726  -71.589  1.00 21.11 ? 141 PRO E O   1 
ATOM   7866  C CB  . PRO E 1 141 ? 27.584  16.479  -74.565  1.00 21.60 ? 141 PRO E CB  1 
ATOM   7867  C CG  . PRO E 1 141 ? 26.873  17.741  -74.267  1.00 21.75 ? 141 PRO E CG  1 
ATOM   7868  C CD  . PRO E 1 141 ? 25.396  17.413  -74.275  1.00 21.77 ? 141 PRO E CD  1 
ATOM   7869  N N   . PRO E 1 142 ? 28.161  14.445  -72.246  1.00 25.18 ? 142 PRO E N   1 
ATOM   7870  C CA  . PRO E 1 142 ? 28.582  14.246  -70.878  1.00 25.94 ? 142 PRO E CA  1 
ATOM   7871  C C   . PRO E 1 142 ? 29.273  15.490  -70.355  1.00 27.43 ? 142 PRO E C   1 
ATOM   7872  O O   . PRO E 1 142 ? 29.556  16.410  -71.120  1.00 25.43 ? 142 PRO E O   1 
ATOM   7873  C CB  . PRO E 1 142 ? 29.566  13.086  -70.982  1.00 25.85 ? 142 PRO E CB  1 
ATOM   7874  C CG  . PRO E 1 142 ? 30.136  13.202  -72.348  1.00 25.86 ? 142 PRO E CG  1 
ATOM   7875  C CD  . PRO E 1 142 ? 29.034  13.746  -73.206  1.00 25.59 ? 142 PRO E CD  1 
ATOM   7876  N N   . PRO E 1 143 ? 29.523  15.536  -69.040  1.00 30.44 ? 143 PRO E N   1 
ATOM   7877  C CA  . PRO E 1 143 ? 30.265  16.664  -68.519  1.00 30.53 ? 143 PRO E CA  1 
ATOM   7878  C C   . PRO E 1 143 ? 31.653  16.703  -69.117  1.00 30.89 ? 143 PRO E C   1 
ATOM   7879  O O   . PRO E 1 143 ? 32.222  15.649  -69.459  1.00 29.67 ? 143 PRO E O   1 
ATOM   7880  C CB  . PRO E 1 143 ? 30.357  16.366  -67.022  1.00 31.03 ? 143 PRO E CB  1 
ATOM   7881  C CG  . PRO E 1 143 ? 29.188  15.499  -66.736  1.00 31.26 ? 143 PRO E CG  1 
ATOM   7882  C CD  . PRO E 1 143 ? 28.993  14.675  -67.968  1.00 31.44 ? 143 PRO E CD  1 
ATOM   7883  N N   . LEU E 1 144 ? 32.182  17.912  -69.226  1.00 31.70 ? 144 LEU E N   1 
ATOM   7884  C CA  . LEU E 1 144 ? 33.548  18.110  -69.641  1.00 33.21 ? 144 LEU E CA  1 
ATOM   7885  C C   . LEU E 1 144 ? 34.489  17.432  -68.652  1.00 34.70 ? 144 LEU E C   1 
ATOM   7886  O O   . LEU E 1 144 ? 34.105  17.123  -67.515  1.00 33.24 ? 144 LEU E O   1 
ATOM   7887  C CB  . LEU E 1 144 ? 33.882  19.600  -69.657  1.00 33.86 ? 144 LEU E CB  1 
ATOM   7888  C CG  . LEU E 1 144 ? 33.096  20.547  -70.545  1.00 34.37 ? 144 LEU E CG  1 
ATOM   7889  C CD1 . LEU E 1 144 ? 33.407  21.978  -70.136  1.00 35.24 ? 144 LEU E CD1 1 
ATOM   7890  C CD2 . LEU E 1 144 ? 33.466  20.302  -71.994  1.00 34.71 ? 144 LEU E CD2 1 
ATOM   7891  N N   . GLY E 1 145 ? 35.730  17.235  -69.085  1.00 37.34 ? 145 GLY E N   1 
ATOM   7892  C CA  . GLY E 1 145 ? 36.786  16.736  -68.223  1.00 38.20 ? 145 GLY E CA  1 
ATOM   7893  C C   . GLY E 1 145 ? 37.093  17.741  -67.130  1.00 41.63 ? 145 GLY E C   1 
ATOM   7894  O O   . GLY E 1 145 ? 36.909  18.954  -67.308  1.00 42.40 ? 145 GLY E O   1 
ATOM   7895  N N   . GLU E 1 146 ? 37.545  17.244  -65.974  1.00 44.10 ? 146 GLU E N   1 
ATOM   7896  C CA  . GLU E 1 146 ? 37.936  18.126  -64.883  1.00 45.88 ? 146 GLU E CA  1 
ATOM   7897  C C   . GLU E 1 146 ? 39.243  18.831  -65.214  1.00 42.74 ? 146 GLU E C   1 
ATOM   7898  O O   . GLU E 1 146 ? 39.508  19.887  -64.678  1.00 45.45 ? 146 GLU E O   1 
ATOM   7899  C CB  . GLU E 1 146 ? 38.036  17.380  -63.574  1.00 50.83 ? 146 GLU E CB  1 
ATOM   7900  C CG  . GLU E 1 146 ? 36.646  17.053  -63.042  1.00 55.62 ? 146 GLU E CG  1 
ATOM   7901  C CD  . GLU E 1 146 ? 36.650  16.031  -61.952  1.00 62.08 ? 146 GLU E CD  1 
ATOM   7902  O OE1 . GLU E 1 146 ? 35.557  15.839  -61.368  1.00 64.05 ? 146 GLU E OE1 1 
ATOM   7903  O OE2 . GLU E 1 146 ? 37.708  15.409  -61.656  1.00 68.95 ? 146 GLU E OE2 1 
ATOM   7904  N N   . THR E 1 147 ? 40.031  18.241  -66.103  1.00 39.96 ? 147 THR E N   1 
ATOM   7905  C CA  . THR E 1 147 ? 41.300  18.820  -66.530  1.00 40.41 ? 147 THR E CA  1 
ATOM   7906  C C   . THR E 1 147 ? 41.388  19.017  -68.044  1.00 38.25 ? 147 THR E C   1 
ATOM   7907  O O   . THR E 1 147 ? 41.500  18.059  -68.810  1.00 39.57 ? 147 THR E O   1 
ATOM   7908  C CB  . THR E 1 147 ? 42.474  17.945  -66.062  1.00 40.46 ? 147 THR E CB  1 
ATOM   7909  O OG1 . THR E 1 147 ? 42.386  17.781  -64.646  1.00 42.07 ? 147 THR E OG1 1 
ATOM   7910  C CG2 . THR E 1 147 ? 43.814  18.588  -66.432  1.00 39.62 ? 147 THR E CG2 1 
ATOM   7911  N N   . ILE E 1 148 ? 41.376  20.278  -68.455  1.00 34.70 ? 148 ILE E N   1 
ATOM   7912  C CA  . ILE E 1 148 ? 41.357  20.623  -69.865  1.00 33.22 ? 148 ILE E CA  1 
ATOM   7913  C C   . ILE E 1 148 ? 42.741  21.102  -70.303  1.00 30.77 ? 148 ILE E C   1 
ATOM   7914  O O   . ILE E 1 148 ? 43.435  21.780  -69.553  1.00 29.27 ? 148 ILE E O   1 
ATOM   7915  C CB  . ILE E 1 148 ? 40.250  21.670  -70.134  1.00 32.81 ? 148 ILE E CB  1 
ATOM   7916  C CG1 . ILE E 1 148 ? 38.889  21.030  -69.839  1.00 31.89 ? 148 ILE E CG1 1 
ATOM   7917  C CG2 . ILE E 1 148 ? 40.324  22.196  -71.559  1.00 32.43 ? 148 ILE E CG2 1 
ATOM   7918  C CD1 . ILE E 1 148 ? 37.712  21.941  -69.737  1.00 31.68 ? 148 ILE E CD1 1 
ATOM   7919  N N   . ASP E 1 149 ? 43.136  20.731  -71.517  1.00 29.58 ? 149 ASP E N   1 
ATOM   7920  C CA  . ASP E 1 149 ? 44.426  21.131  -72.065  1.00 29.61 ? 149 ASP E CA  1 
ATOM   7921  C C   . ASP E 1 149 ? 44.629  22.619  -71.786  1.00 31.14 ? 149 ASP E C   1 
ATOM   7922  O O   . ASP E 1 149 ? 43.747  23.430  -72.081  1.00 34.04 ? 149 ASP E O   1 
ATOM   7923  C CB  . ASP E 1 149 ? 44.463  20.860  -73.571  1.00 28.95 ? 149 ASP E CB  1 
ATOM   7924  C CG  . ASP E 1 149 ? 45.844  20.999  -74.163  1.00 29.42 ? 149 ASP E CG  1 
ATOM   7925  O OD1 . ASP E 1 149 ? 46.465  22.061  -73.984  1.00 31.50 ? 149 ASP E OD1 1 
ATOM   7926  O OD2 . ASP E 1 149 ? 46.307  20.058  -74.837  1.00 28.47 ? 149 ASP E OD2 1 
ATOM   7927  N N   . PRO E 1 150 ? 45.772  22.986  -71.177  1.00 30.98 ? 150 PRO E N   1 
ATOM   7928  C CA  . PRO E 1 150 ? 46.064  24.383  -70.835  1.00 30.25 ? 150 PRO E CA  1 
ATOM   7929  C C   . PRO E 1 150 ? 45.884  25.401  -71.957  1.00 29.49 ? 150 PRO E C   1 
ATOM   7930  O O   . PRO E 1 150 ? 45.553  26.553  -71.664  1.00 29.08 ? 150 PRO E O   1 
ATOM   7931  C CB  . PRO E 1 150 ? 47.506  24.317  -70.366  1.00 30.77 ? 150 PRO E CB  1 
ATOM   7932  C CG  . PRO E 1 150 ? 47.537  23.018  -69.654  1.00 31.16 ? 150 PRO E CG  1 
ATOM   7933  C CD  . PRO E 1 150 ? 46.710  22.075  -70.499  1.00 31.11 ? 150 PRO E CD  1 
ATOM   7934  N N   . LEU E 1 151 ? 46.089  25.008  -73.211  1.00 30.18 ? 151 LEU E N   1 
ATOM   7935  C CA  . LEU E 1 151 ? 45.796  25.900  -74.347  1.00 31.75 ? 151 LEU E CA  1 
ATOM   7936  C C   . LEU E 1 151 ? 44.304  26.258  -74.442  1.00 32.39 ? 151 LEU E C   1 
ATOM   7937  O O   . LEU E 1 151 ? 43.963  27.374  -74.789  1.00 32.56 ? 151 LEU E O   1 
ATOM   7938  C CB  . LEU E 1 151 ? 46.231  25.252  -75.667  1.00 32.53 ? 151 LEU E CB  1 
ATOM   7939  C CG  . LEU E 1 151 ? 47.718  25.288  -75.991  1.00 32.69 ? 151 LEU E CG  1 
ATOM   7940  C CD1 . LEU E 1 151 ? 48.274  23.888  -76.211  1.00 33.84 ? 151 LEU E CD1 1 
ATOM   7941  C CD2 . LEU E 1 151 ? 47.946  26.161  -77.219  1.00 32.81 ? 151 LEU E CD2 1 
ATOM   7942  N N   . ALA E 1 152 ? 43.430  25.301  -74.126  1.00 32.38 ? 152 ALA E N   1 
ATOM   7943  C CA  . ALA E 1 152 ? 41.986  25.473  -74.254  1.00 31.54 ? 152 ALA E CA  1 
ATOM   7944  C C   . ALA E 1 152 ? 41.284  25.876  -72.945  1.00 31.91 ? 152 ALA E C   1 
ATOM   7945  O O   . ALA E 1 152 ? 40.173  26.387  -72.971  1.00 32.77 ? 152 ALA E O   1 
ATOM   7946  C CB  . ALA E 1 152 ? 41.376  24.190  -74.801  1.00 30.36 ? 152 ALA E CB  1 
ATOM   7947  N N   . ALA E 1 153 ? 41.914  25.641  -71.800  1.00 29.68 ? 153 ALA E N   1 
ATOM   7948  C CA  . ALA E 1 153 ? 41.282  25.916  -70.507  1.00 28.89 ? 153 ALA E CA  1 
ATOM   7949  C C   . ALA E 1 153 ? 40.691  27.342  -70.338  1.00 28.93 ? 153 ALA E C   1 
ATOM   7950  O O   . ALA E 1 153 ? 39.579  27.485  -69.828  1.00 31.26 ? 153 ALA E O   1 
ATOM   7951  C CB  . ALA E 1 153 ? 42.245  25.611  -69.377  1.00 27.28 ? 153 ALA E CB  1 
ATOM   7952  N N   . PRO E 1 154 ? 41.418  28.396  -70.765  1.00 27.57 ? 154 PRO E N   1 
ATOM   7953  C CA  . PRO E 1 154 ? 40.883  29.761  -70.624  1.00 27.74 ? 154 PRO E CA  1 
ATOM   7954  C C   . PRO E 1 154 ? 39.519  29.964  -71.288  1.00 28.68 ? 154 PRO E C   1 
ATOM   7955  O O   . PRO E 1 154 ? 38.718  30.762  -70.822  1.00 28.77 ? 154 PRO E O   1 
ATOM   7956  C CB  . PRO E 1 154 ? 41.926  30.628  -71.339  1.00 27.32 ? 154 PRO E CB  1 
ATOM   7957  C CG  . PRO E 1 154 ? 43.176  29.826  -71.310  1.00 27.15 ? 154 PRO E CG  1 
ATOM   7958  C CD  . PRO E 1 154 ? 42.745  28.399  -71.400  1.00 26.98 ? 154 PRO E CD  1 
ATOM   7959  N N   . ILE E 1 155 ? 39.292  29.234  -72.376  1.00 29.49 ? 155 ILE E N   1 
ATOM   7960  C CA  . ILE E 1 155 ? 38.074  29.281  -73.168  1.00 29.65 ? 155 ILE E CA  1 
ATOM   7961  C C   . ILE E 1 155 ? 36.931  28.405  -72.576  1.00 28.37 ? 155 ILE E C   1 
ATOM   7962  O O   . ILE E 1 155 ? 35.790  28.511  -73.017  1.00 27.34 ? 155 ILE E O   1 
ATOM   7963  C CB  . ILE E 1 155 ? 38.467  28.927  -74.649  1.00 31.06 ? 155 ILE E CB  1 
ATOM   7964  C CG1 . ILE E 1 155 ? 38.720  30.227  -75.404  1.00 32.73 ? 155 ILE E CG1 1 
ATOM   7965  C CG2 . ILE E 1 155 ? 37.478  28.014  -75.391  1.00 30.46 ? 155 ILE E CG2 1 
ATOM   7966  C CD1 . ILE E 1 155 ? 39.398  30.047  -76.763  1.00 35.53 ? 155 ILE E CD1 1 
ATOM   7967  N N   . PHE E 1 156 ? 37.229  27.571  -71.574  1.00 27.51 ? 156 PHE E N   1 
ATOM   7968  C CA  . PHE E 1 156 ? 36.214  26.734  -70.905  1.00 26.99 ? 156 PHE E CA  1 
ATOM   7969  C C   . PHE E 1 156 ? 36.052  27.023  -69.406  1.00 25.23 ? 156 PHE E C   1 
ATOM   7970  O O   . PHE E 1 156 ? 35.689  26.140  -68.624  1.00 24.59 ? 156 PHE E O   1 
ATOM   7971  C CB  . PHE E 1 156 ? 36.514  25.235  -71.117  1.00 27.09 ? 156 PHE E CB  1 
ATOM   7972  C CG  . PHE E 1 156 ? 36.190  24.747  -72.490  1.00 26.73 ? 156 PHE E CG  1 
ATOM   7973  C CD1 . PHE E 1 156 ? 34.882  24.496  -72.854  1.00 27.45 ? 156 PHE E CD1 1 
ATOM   7974  C CD2 . PHE E 1 156 ? 37.185  24.567  -73.430  1.00 28.22 ? 156 PHE E CD2 1 
ATOM   7975  C CE1 . PHE E 1 156 ? 34.569  24.053  -74.138  1.00 28.75 ? 156 PHE E CE1 1 
ATOM   7976  C CE2 . PHE E 1 156 ? 36.879  24.142  -74.718  1.00 29.15 ? 156 PHE E CE2 1 
ATOM   7977  C CZ  . PHE E 1 156 ? 35.566  23.865  -75.065  1.00 29.27 ? 156 PHE E CZ  1 
ATOM   7978  N N   . VAL E 1 157 ? 36.293  28.262  -69.008  1.00 24.76 ? 157 VAL E N   1 
ATOM   7979  C CA  . VAL E 1 157 ? 36.091  28.662  -67.613  1.00 25.59 ? 157 VAL E CA  1 
ATOM   7980  C C   . VAL E 1 157 ? 34.583  28.614  -67.330  1.00 26.34 ? 157 VAL E C   1 
ATOM   7981  O O   . VAL E 1 157 ? 33.772  28.993  -68.183  1.00 27.47 ? 157 VAL E O   1 
ATOM   7982  C CB  . VAL E 1 157 ? 36.705  30.063  -67.316  1.00 24.74 ? 157 VAL E CB  1 
ATOM   7983  C CG1 . VAL E 1 157 ? 36.290  30.583  -65.953  1.00 24.21 ? 157 VAL E CG1 1 
ATOM   7984  C CG2 . VAL E 1 157 ? 38.224  30.006  -67.428  1.00 24.53 ? 157 VAL E CG2 1 
ATOM   7985  N N   . ASP E 1 158 ? 34.223  28.101  -66.153  1.00 26.25 ? 158 ASP E N   1 
ATOM   7986  C CA  . ASP E 1 158 ? 32.833  27.821  -65.785  1.00 26.34 ? 158 ASP E CA  1 
ATOM   7987  C C   . ASP E 1 158 ? 32.092  26.863  -66.732  1.00 26.71 ? 158 ASP E C   1 
ATOM   7988  O O   . ASP E 1 158 ? 30.877  26.712  -66.617  1.00 28.22 ? 158 ASP E O   1 
ATOM   7989  C CB  . ASP E 1 158 ? 32.033  29.119  -65.676  1.00 25.83 ? 158 ASP E CB  1 
ATOM   7990  C CG  . ASP E 1 158 ? 32.712  30.140  -64.811  1.00 25.38 ? 158 ASP E CG  1 
ATOM   7991  O OD1 . ASP E 1 158 ? 33.164  29.797  -63.716  1.00 26.21 ? 158 ASP E OD1 1 
ATOM   7992  O OD2 . ASP E 1 158 ? 32.797  31.300  -65.213  1.00 25.75 ? 158 ASP E OD2 1 
ATOM   7993  N N   . GLY E 1 159 ? 32.811  26.200  -67.633  1.00 25.85 ? 159 GLY E N   1 
ATOM   7994  C CA  . GLY E 1 159 ? 32.178  25.325  -68.611  1.00 25.86 ? 159 GLY E CA  1 
ATOM   7995  C C   . GLY E 1 159 ? 31.683  24.006  -68.020  1.00 25.58 ? 159 GLY E C   1 
ATOM   7996  O O   . GLY E 1 159 ? 30.640  23.475  -68.419  1.00 26.33 ? 159 GLY E O   1 
ATOM   7997  N N   . LEU E 1 160 ? 32.450  23.473  -67.077  1.00 23.64 ? 160 LEU E N   1 
ATOM   7998  C CA  . LEU E 1 160 ? 32.141  22.185  -66.481  1.00 22.17 ? 160 LEU E CA  1 
ATOM   7999  C C   . LEU E 1 160 ? 30.774  22.207  -65.825  1.00 22.34 ? 160 LEU E C   1 
ATOM   8000  O O   . LEU E 1 160 ? 29.945  21.323  -66.051  1.00 21.21 ? 160 LEU E O   1 
ATOM   8001  C CB  . LEU E 1 160 ? 33.212  21.821  -65.463  1.00 21.60 ? 160 LEU E CB  1 
ATOM   8002  C CG  . LEU E 1 160 ? 32.988  20.595  -64.602  1.00 21.54 ? 160 LEU E CG  1 
ATOM   8003  C CD1 . LEU E 1 160 ? 32.818  19.382  -65.489  1.00 22.10 ? 160 LEU E CD1 1 
ATOM   8004  C CD2 . LEU E 1 160 ? 34.184  20.399  -63.667  1.00 21.35 ? 160 LEU E CD2 1 
ATOM   8005  N N   . ALA E 1 161 ? 30.538  23.231  -65.009  1.00 22.97 ? 161 ALA E N   1 
ATOM   8006  C CA  . ALA E 1 161 ? 29.289  23.320  -64.257  1.00 23.19 ? 161 ALA E CA  1 
ATOM   8007  C C   . ALA E 1 161 ? 28.104  23.446  -65.232  1.00 24.04 ? 161 ALA E C   1 
ATOM   8008  O O   . ALA E 1 161 ? 27.050  22.834  -65.028  1.00 24.88 ? 161 ALA E O   1 
ATOM   8009  C CB  . ALA E 1 161 ? 29.340  24.497  -63.308  1.00 22.12 ? 161 ALA E CB  1 
ATOM   8010  N N   . LYS E 1 162 ? 28.297  24.226  -66.296  1.00 23.19 ? 162 LYS E N   1 
ATOM   8011  C CA  . LYS E 1 162 ? 27.285  24.362  -67.327  1.00 21.64 ? 162 LYS E CA  1 
ATOM   8012  C C   . LYS E 1 162 ? 26.984  23.028  -67.989  1.00 21.80 ? 162 LYS E C   1 
ATOM   8013  O O   . LYS E 1 162 ? 25.817  22.693  -68.198  1.00 22.46 ? 162 LYS E O   1 
ATOM   8014  C CB  . LYS E 1 162 ? 27.728  25.357  -68.391  1.00 20.59 ? 162 LYS E CB  1 
ATOM   8015  C CG  . LYS E 1 162 ? 27.737  26.790  -67.901  1.00 19.95 ? 162 LYS E CG  1 
ATOM   8016  C CD  . LYS E 1 162 ? 28.314  27.717  -68.958  1.00 19.94 ? 162 LYS E CD  1 
ATOM   8017  C CE  . LYS E 1 162 ? 28.702  29.057  -68.376  1.00 19.22 ? 162 LYS E CE  1 
ATOM   8018  N NZ  . LYS E 1 162 ? 28.876  30.064  -69.436  1.00 18.67 ? 162 LYS E NZ  1 
ATOM   8019  N N   . SER E 1 163 ? 28.028  22.268  -68.318  1.00 21.29 ? 163 SER E N   1 
ATOM   8020  C CA  . SER E 1 163 ? 27.848  20.973  -68.974  1.00 20.23 ? 163 SER E CA  1 
ATOM   8021  C C   . SER E 1 163 ? 27.133  19.977  -68.062  1.00 19.91 ? 163 SER E C   1 
ATOM   8022  O O   . SER E 1 163 ? 26.387  19.119  -68.536  1.00 19.09 ? 163 SER E O   1 
ATOM   8023  C CB  . SER E 1 163 ? 29.191  20.409  -69.459  1.00 19.66 ? 163 SER E CB  1 
ATOM   8024  O OG  . SER E 1 163 ? 30.033  20.030  -68.397  1.00 19.84 ? 163 SER E OG  1 
ATOM   8025  N N   . GLU E 1 164 ? 27.354  20.090  -66.755  1.00 20.52 ? 164 GLU E N   1 
ATOM   8026  C CA  . GLU E 1 164 ? 26.675  19.208  -65.796  1.00 21.72 ? 164 GLU E CA  1 
ATOM   8027  C C   . GLU E 1 164 ? 25.180  19.500  -65.746  1.00 21.34 ? 164 GLU E C   1 
ATOM   8028  O O   . GLU E 1 164 ? 24.380  18.599  -65.540  1.00 20.90 ? 164 GLU E O   1 
ATOM   8029  C CB  . GLU E 1 164 ? 27.294  19.326  -64.410  1.00 23.11 ? 164 GLU E CB  1 
ATOM   8030  C CG  . GLU E 1 164 ? 28.534  18.454  -64.222  1.00 24.93 ? 164 GLU E CG  1 
ATOM   8031  C CD  . GLU E 1 164 ? 29.409  18.891  -63.054  1.00 27.43 ? 164 GLU E CD  1 
ATOM   8032  O OE1 . GLU E 1 164 ? 30.446  18.219  -62.813  1.00 27.95 ? 164 GLU E OE1 1 
ATOM   8033  O OE2 . GLU E 1 164 ? 29.074  19.919  -62.399  1.00 29.14 ? 164 GLU E OE2 1 
ATOM   8034  N N   . ALA E 1 165 ? 24.811  20.760  -65.960  1.00 20.94 ? 165 ALA E N   1 
ATOM   8035  C CA  . ALA E 1 165 ? 23.407  21.179  -65.934  1.00 19.89 ? 165 ALA E CA  1 
ATOM   8036  C C   . ALA E 1 165 ? 22.593  20.888  -67.210  1.00 19.76 ? 165 ALA E C   1 
ATOM   8037  O O   . ALA E 1 165 ? 21.382  21.073  -67.201  1.00 19.10 ? 165 ALA E O   1 
ATOM   8038  C CB  . ALA E 1 165 ? 23.328  22.660  -65.601  1.00 19.17 ? 165 ALA E CB  1 
ATOM   8039  N N   . LEU E 1 166 ? 23.243  20.446  -68.283  1.00 20.45 ? 166 LEU E N   1 
ATOM   8040  C CA  . LEU E 1 166 ? 22.561  20.290  -69.582  1.00 20.72 ? 166 LEU E CA  1 
ATOM   8041  C C   . LEU E 1 166 ? 21.546  19.150  -69.623  1.00 20.90 ? 166 LEU E C   1 
ATOM   8042  O O   . LEU E 1 166 ? 20.451  19.352  -70.126  1.00 22.65 ? 166 LEU E O   1 
ATOM   8043  C CB  . LEU E 1 166 ? 23.566  20.154  -70.738  1.00 20.61 ? 166 LEU E CB  1 
ATOM   8044  C CG  . LEU E 1 166 ? 24.430  21.387  -71.053  1.00 20.88 ? 166 LEU E CG  1 
ATOM   8045  C CD1 . LEU E 1 166 ? 25.361  21.131  -72.237  1.00 20.67 ? 166 LEU E CD1 1 
ATOM   8046  C CD2 . LEU E 1 166 ? 23.568  22.624  -71.280  1.00 20.94 ? 166 LEU E CD2 1 
ATOM   8047  N N   . PRO E 1 167 ? 21.879  17.960  -69.092  1.00 20.91 ? 167 PRO E N   1 
ATOM   8048  C CA  . PRO E 1 167 ? 20.878  16.891  -69.141  1.00 21.07 ? 167 PRO E CA  1 
ATOM   8049  C C   . PRO E 1 167 ? 19.480  17.292  -68.618  1.00 21.28 ? 167 PRO E C   1 
ATOM   8050  O O   . PRO E 1 167 ? 18.468  17.016  -69.274  1.00 22.10 ? 167 PRO E O   1 
ATOM   8051  C CB  . PRO E 1 167 ? 21.504  15.795  -68.281  1.00 20.76 ? 167 PRO E CB  1 
ATOM   8052  C CG  . PRO E 1 167 ? 22.965  16.016  -68.342  1.00 20.07 ? 167 PRO E CG  1 
ATOM   8053  C CD  . PRO E 1 167 ? 23.145  17.506  -68.482  1.00 20.61 ? 167 PRO E CD  1 
ATOM   8054  N N   . GLY E 1 168 ? 19.419  17.943  -67.469  1.00 21.07 ? 168 GLY E N   1 
ATOM   8055  C CA  . GLY E 1 168 ? 18.143  18.374  -66.903  1.00 21.30 ? 168 GLY E CA  1 
ATOM   8056  C C   . GLY E 1 168 ? 17.378  19.313  -67.812  1.00 21.93 ? 168 GLY E C   1 
ATOM   8057  O O   . GLY E 1 168 ? 16.190  19.112  -68.064  1.00 22.25 ? 168 GLY E O   1 
ATOM   8058  N N   . VAL E 1 169 ? 18.076  20.324  -68.321  1.00 22.82 ? 169 VAL E N   1 
ATOM   8059  C CA  . VAL E 1 169 ? 17.490  21.332  -69.208  1.00 23.04 ? 169 VAL E CA  1 
ATOM   8060  C C   . VAL E 1 169 ? 17.060  20.699  -70.528  1.00 22.97 ? 169 VAL E C   1 
ATOM   8061  O O   . VAL E 1 169 ? 15.943  20.893  -70.976  1.00 21.28 ? 169 VAL E O   1 
ATOM   8062  C CB  . VAL E 1 169 ? 18.469  22.488  -69.508  1.00 23.14 ? 169 VAL E CB  1 
ATOM   8063  C CG1 . VAL E 1 169 ? 17.837  23.481  -70.468  1.00 23.42 ? 169 VAL E CG1 1 
ATOM   8064  C CG2 . VAL E 1 169 ? 18.832  23.236  -68.238  1.00 23.76 ? 169 VAL E CG2 1 
ATOM   8065  N N   . TYR E 1 170 ? 17.966  19.951  -71.144  1.00 24.06 ? 170 TYR E N   1 
ATOM   8066  C CA  . TYR E 1 170 ? 17.687  19.251  -72.418  1.00 24.83 ? 170 TYR E CA  1 
ATOM   8067  C C   . TYR E 1 170 ? 16.465  18.351  -72.320  1.00 24.77 ? 170 TYR E C   1 
ATOM   8068  O O   . TYR E 1 170 ? 15.651  18.309  -73.248  1.00 23.02 ? 170 TYR E O   1 
ATOM   8069  C CB  . TYR E 1 170 ? 18.899  18.432  -72.891  1.00 24.72 ? 170 TYR E CB  1 
ATOM   8070  C CG  . TYR E 1 170 ? 19.936  19.210  -73.686  1.00 24.91 ? 170 TYR E CG  1 
ATOM   8071  C CD1 . TYR E 1 170 ? 20.112  20.587  -73.499  1.00 25.30 ? 170 TYR E CD1 1 
ATOM   8072  C CD2 . TYR E 1 170 ? 20.758  18.563  -74.612  1.00 24.91 ? 170 TYR E CD2 1 
ATOM   8073  C CE1 . TYR E 1 170 ? 21.071  21.287  -74.202  1.00 25.99 ? 170 TYR E CE1 1 
ATOM   8074  C CE2 . TYR E 1 170 ? 21.720  19.251  -75.324  1.00 24.72 ? 170 TYR E CE2 1 
ATOM   8075  C CZ  . TYR E 1 170 ? 21.867  20.618  -75.129  1.00 25.47 ? 170 TYR E CZ  1 
ATOM   8076  O OH  . TYR E 1 170 ? 22.809  21.330  -75.834  1.00 24.48 ? 170 TYR E OH  1 
ATOM   8077  N N   . LYS E 1 171 ? 16.332  17.644  -71.200  1.00 24.53 ? 171 LYS E N   1 
ATOM   8078  C CA  . LYS E 1 171 ? 15.178  16.776  -71.012  1.00 24.98 ? 171 LYS E CA  1 
ATOM   8079  C C   . LYS E 1 171 ? 13.867  17.569  -71.000  1.00 22.56 ? 171 LYS E C   1 
ATOM   8080  O O   . LYS E 1 171 ? 12.900  17.165  -71.638  1.00 21.44 ? 171 LYS E O   1 
ATOM   8081  C CB  . LYS E 1 171 ? 15.295  15.939  -69.737  1.00 26.97 ? 171 LYS E CB  1 
ATOM   8082  C CG  . LYS E 1 171 ? 14.218  14.838  -69.718  1.00 28.41 ? 171 LYS E CG  1 
ATOM   8083  C CD  . LYS E 1 171 ? 14.381  13.713  -68.731  1.00 29.08 ? 171 LYS E CD  1 
ATOM   8084  C CE  . LYS E 1 171 ? 14.141  14.144  -67.302  1.00 30.57 ? 171 LYS E CE  1 
ATOM   8085  N NZ  . LYS E 1 171 ? 13.219  13.186  -66.682  1.00 31.12 ? 171 LYS E NZ  1 
ATOM   8086  N N   . ALA E 1 172 ? 13.841  18.684  -70.276  1.00 21.33 ? 172 ALA E N   1 
ATOM   8087  C CA  . ALA E 1 172 ? 12.632  19.518  -70.196  1.00 20.76 ? 172 ALA E CA  1 
ATOM   8088  C C   . ALA E 1 172 ? 12.258  20.060  -71.565  1.00 20.34 ? 172 ALA E C   1 
ATOM   8089  O O   . ALA E 1 172 ? 11.112  19.982  -71.984  1.00 20.28 ? 172 ALA E O   1 
ATOM   8090  C CB  . ALA E 1 172 ? 12.818  20.663  -69.210  1.00 20.18 ? 172 ALA E CB  1 
ATOM   8091  N N   . ILE E 1 173 ? 13.246  20.595  -72.260  1.00 20.71 ? 173 ILE E N   1 
ATOM   8092  C CA  . ILE E 1 173 ? 13.051  21.181  -73.584  1.00 21.09 ? 173 ILE E CA  1 
ATOM   8093  C C   . ILE E 1 173 ? 12.556  20.138  -74.580  1.00 21.43 ? 173 ILE E C   1 
ATOM   8094  O O   . ILE E 1 173 ? 11.658  20.414  -75.365  1.00 21.03 ? 173 ILE E O   1 
ATOM   8095  C CB  . ILE E 1 173 ? 14.363  21.823  -74.087  1.00 21.51 ? 173 ILE E CB  1 
ATOM   8096  C CG1 . ILE E 1 173 ? 14.728  23.056  -73.228  1.00 21.41 ? 173 ILE E CG1 1 
ATOM   8097  C CG2 . ILE E 1 173 ? 14.271  22.199  -75.552  1.00 21.46 ? 173 ILE E CG2 1 
ATOM   8098  C CD1 . ILE E 1 173 ? 13.747  24.205  -73.328  1.00 20.87 ? 173 ILE E CD1 1 
ATOM   8099  N N   . ALA E 1 174 ? 13.147  18.949  -74.554  1.00 22.38 ? 174 ALA E N   1 
ATOM   8100  C CA  . ALA E 1 174 ? 12.750  17.859  -75.455  1.00 23.05 ? 174 ALA E CA  1 
ATOM   8101  C C   . ALA E 1 174 ? 11.320  17.445  -75.185  1.00 22.72 ? 174 ALA E C   1 
ATOM   8102  O O   . ALA E 1 174 ? 10.521  17.305  -76.106  1.00 20.85 ? 174 ALA E O   1 
ATOM   8103  C CB  . ALA E 1 174 ? 13.679  16.661  -75.284  1.00 23.38 ? 174 ALA E CB  1 
ATOM   8104  N N   . GLU E 1 175 ? 11.026  17.252  -73.905  1.00 23.84 ? 175 GLU E N   1 
ATOM   8105  C CA  . GLU E 1 175 ? 9.685   16.928  -73.429  1.00 24.45 ? 175 GLU E CA  1 
ATOM   8106  C C   . GLU E 1 175 ? 8.686   18.012  -73.853  1.00 22.61 ? 175 GLU E C   1 
ATOM   8107  O O   . GLU E 1 175 ? 7.615   17.695  -74.337  1.00 22.98 ? 175 GLU E O   1 
ATOM   8108  C CB  . GLU E 1 175 ? 9.676   16.772  -71.910  1.00 27.36 ? 175 GLU E CB  1 
ATOM   8109  C CG  . GLU E 1 175 ? 8.998   15.505  -71.401  1.00 31.55 ? 175 GLU E CG  1 
ATOM   8110  C CD  . GLU E 1 175 ? 9.691   14.962  -70.161  1.00 35.48 ? 175 GLU E CD  1 
ATOM   8111  O OE1 . GLU E 1 175 ? 9.298   15.394  -69.046  1.00 38.21 ? 175 GLU E OE1 1 
ATOM   8112  O OE2 . GLU E 1 175 ? 10.610  14.093  -70.276  1.00 38.63 ? 175 GLU E OE2 1 
ATOM   8113  N N   . ALA E 1 176 ? 9.046   19.282  -73.698  1.00 20.69 ? 176 ALA E N   1 
ATOM   8114  C CA  . ALA E 1 176 ? 8.160   20.395  -74.070  1.00 19.60 ? 176 ALA E CA  1 
ATOM   8115  C C   . ALA E 1 176 ? 7.830   20.381  -75.547  1.00 19.34 ? 176 ALA E C   1 
ATOM   8116  O O   . ALA E 1 176 ? 6.759   20.805  -75.951  1.00 19.98 ? 176 ALA E O   1 
ATOM   8117  C CB  . ALA E 1 176 ? 8.782   21.739  -73.699  1.00 18.90 ? 176 ALA E CB  1 
ATOM   8118  N N   . ALA E 1 177 ? 8.768   19.903  -76.351  1.00 19.04 ? 177 ALA E N   1 
ATOM   8119  C CA  . ALA E 1 177 ? 8.597   19.800  -77.798  1.00 18.59 ? 177 ALA E CA  1 
ATOM   8120  C C   . ALA E 1 177 ? 7.892   18.523  -78.223  1.00 18.05 ? 177 ALA E C   1 
ATOM   8121  O O   . ALA E 1 177 ? 7.706   18.315  -79.404  1.00 18.00 ? 177 ALA E O   1 
ATOM   8122  C CB  . ALA E 1 177 ? 9.961   19.864  -78.467  1.00 18.46 ? 177 ALA E CB  1 
ATOM   8123  N N   . GLY E 1 178 ? 7.526   17.662  -77.275  1.00 17.86 ? 178 GLY E N   1 
ATOM   8124  C CA  . GLY E 1 178 ? 6.986   16.342  -77.586  1.00 18.72 ? 178 GLY E CA  1 
ATOM   8125  C C   . GLY E 1 178 ? 7.948   15.424  -78.327  1.00 19.35 ? 178 GLY E C   1 
ATOM   8126  O O   . GLY E 1 178 ? 7.539   14.701  -79.237  1.00 19.69 ? 178 GLY E O   1 
ATOM   8127  N N   . GLU E 1 179 ? 9.221   15.458  -77.938  1.00 20.21 ? 179 GLU E N   1 
ATOM   8128  C CA  . GLU E 1 179 ? 10.281  14.696  -78.605  1.00 21.63 ? 179 GLU E CA  1 
ATOM   8129  C C   . GLU E 1 179 ? 11.066  13.893  -77.563  1.00 22.56 ? 179 GLU E C   1 
ATOM   8130  O O   . GLU E 1 179 ? 10.712  13.905  -76.392  1.00 23.30 ? 179 GLU E O   1 
ATOM   8131  C CB  . GLU E 1 179 ? 11.197  15.638  -79.387  1.00 21.73 ? 179 GLU E CB  1 
ATOM   8132  C CG  . GLU E 1 179 ? 10.469  16.443  -80.462  1.00 22.13 ? 179 GLU E CG  1 
ATOM   8133  C CD  . GLU E 1 179 ? 10.095  15.637  -81.704  1.00 22.43 ? 179 GLU E CD  1 
ATOM   8134  O OE1 . GLU E 1 179 ? 9.556   16.249  -82.663  1.00 21.92 ? 179 GLU E OE1 1 
ATOM   8135  O OE2 . GLU E 1 179 ? 10.376  14.408  -81.751  1.00 23.06 ? 179 GLU E OE2 1 
ATOM   8136  N N   . SER E 1 180 ? 12.121  13.196  -77.972  1.00 22.41 ? 180 SER E N   1 
ATOM   8137  C CA  . SER E 1 180 ? 12.813  12.283  -77.072  1.00 21.93 ? 180 SER E CA  1 
ATOM   8138  C C   . SER E 1 180 ? 14.143  12.825  -76.576  1.00 22.66 ? 180 SER E C   1 
ATOM   8139  O O   . SER E 1 180 ? 14.728  13.735  -77.176  1.00 23.71 ? 180 SER E O   1 
ATOM   8140  C CB  . SER E 1 180 ? 13.045  10.956  -77.775  1.00 21.92 ? 180 SER E CB  1 
ATOM   8141  O OG  . SER E 1 180 ? 11.865  10.544  -78.414  1.00 21.83 ? 180 SER E OG  1 
ATOM   8142  N N   . PHE E 1 181 ? 14.614  12.229  -75.478  1.00 23.30 ? 181 PHE E N   1 
ATOM   8143  C CA  . PHE E 1 181 ? 15.841  12.663  -74.810  1.00 23.62 ? 181 PHE E CA  1 
ATOM   8144  C C   . PHE E 1 181 ? 16.726  11.493  -74.402  1.00 24.00 ? 181 PHE E C   1 
ATOM   8145  O O   . PHE E 1 181 ? 16.227  10.415  -74.097  1.00 23.86 ? 181 PHE E O   1 
ATOM   8146  C CB  . PHE E 1 181 ? 15.509  13.456  -73.552  1.00 22.88 ? 181 PHE E CB  1 
ATOM   8147  C CG  . PHE E 1 181 ? 16.700  13.711  -72.690  1.00 22.39 ? 181 PHE E CG  1 
ATOM   8148  C CD1 . PHE E 1 181 ? 17.683  14.589  -73.100  1.00 21.90 ? 181 PHE E CD1 1 
ATOM   8149  C CD2 . PHE E 1 181 ? 16.859  13.047  -71.490  1.00 22.35 ? 181 PHE E CD2 1 
ATOM   8150  C CE1 . PHE E 1 181 ? 18.798  14.812  -72.320  1.00 22.23 ? 181 PHE E CE1 1 
ATOM   8151  C CE2 . PHE E 1 181 ? 17.967  13.272  -70.697  1.00 21.97 ? 181 PHE E CE2 1 
ATOM   8152  C CZ  . PHE E 1 181 ? 18.939  14.150  -71.112  1.00 22.04 ? 181 PHE E CZ  1 
ATOM   8153  N N   . PHE E 1 182 ? 18.039  11.716  -74.399  1.00 24.37 ? 182 PHE E N   1 
ATOM   8154  C CA  . PHE E 1 182 ? 18.990  10.749  -73.854  1.00 24.95 ? 182 PHE E CA  1 
ATOM   8155  C C   . PHE E 1 182 ? 20.240  11.461  -73.357  1.00 24.91 ? 182 PHE E C   1 
ATOM   8156  O O   . PHE E 1 182 ? 20.781  12.322  -74.031  1.00 24.80 ? 182 PHE E O   1 
ATOM   8157  C CB  . PHE E 1 182 ? 19.361  9.718   -74.903  1.00 25.66 ? 182 PHE E CB  1 
ATOM   8158  C CG  . PHE E 1 182 ? 20.316  8.668   -74.416  1.00 26.27 ? 182 PHE E CG  1 
ATOM   8159  C CD1 . PHE E 1 182 ? 21.680  8.913   -74.415  1.00 26.60 ? 182 PHE E CD1 1 
ATOM   8160  C CD2 . PHE E 1 182 ? 19.857  7.414   -74.012  1.00 27.24 ? 182 PHE E CD2 1 
ATOM   8161  C CE1 . PHE E 1 182 ? 22.573  7.944   -73.993  1.00 27.82 ? 182 PHE E CE1 1 
ATOM   8162  C CE2 . PHE E 1 182 ? 20.746  6.443   -73.576  1.00 27.72 ? 182 PHE E CE2 1 
ATOM   8163  C CZ  . PHE E 1 182 ? 22.100  6.718   -73.557  1.00 28.11 ? 182 PHE E CZ  1 
ATOM   8164  N N   . ASP E 1 183 ? 20.695  11.083  -72.170  1.00 25.24 ? 183 ASP E N   1 
ATOM   8165  C CA  . ASP E 1 183 ? 21.855  11.702  -71.547  1.00 25.72 ? 183 ASP E CA  1 
ATOM   8166  C C   . ASP E 1 183 ? 23.097  10.856  -71.801  1.00 26.35 ? 183 ASP E C   1 
ATOM   8167  O O   . ASP E 1 183 ? 23.272  9.796   -71.209  1.00 26.68 ? 183 ASP E O   1 
ATOM   8168  C CB  . ASP E 1 183 ? 21.610  11.831  -70.048  1.00 25.84 ? 183 ASP E CB  1 
ATOM   8169  C CG  . ASP E 1 183 ? 22.770  12.474  -69.314  1.00 26.41 ? 183 ASP E CG  1 
ATOM   8170  O OD1 . ASP E 1 183 ? 23.737  12.963  -69.942  1.00 28.01 ? 183 ASP E OD1 1 
ATOM   8171  O OD2 . ASP E 1 183 ? 22.695  12.492  -68.079  1.00 27.44 ? 183 ASP E OD2 1 
ATOM   8172  N N   . ALA E 1 184 ? 23.973  11.327  -72.672  1.00 26.63 ? 184 ALA E N   1 
ATOM   8173  C CA  . ALA E 1 184 ? 25.199  10.595  -72.957  1.00 26.65 ? 184 ALA E CA  1 
ATOM   8174  C C   . ALA E 1 184 ? 26.017  10.378  -71.679  1.00 26.77 ? 184 ALA E C   1 
ATOM   8175  O O   . ALA E 1 184 ? 26.722  9.373   -71.556  1.00 28.90 ? 184 ALA E O   1 
ATOM   8176  C CB  . ALA E 1 184 ? 26.029  11.324  -74.002  1.00 26.33 ? 184 ALA E CB  1 
ATOM   8177  N N   . GLY E 1 185 ? 25.907  11.298  -70.721  1.00 25.67 ? 185 GLY E N   1 
ATOM   8178  C CA  . GLY E 1 185 ? 26.568  11.155  -69.427  1.00 25.20 ? 185 GLY E CA  1 
ATOM   8179  C C   . GLY E 1 185 ? 26.120  9.970   -68.587  1.00 24.66 ? 185 GLY E C   1 
ATOM   8180  O O   . GLY E 1 185 ? 26.784  9.618   -67.626  1.00 25.72 ? 185 GLY E O   1 
ATOM   8181  N N   . SER E 1 186 ? 24.985  9.369   -68.928  1.00 24.34 ? 186 SER E N   1 
ATOM   8182  C CA  . SER E 1 186 ? 24.496  8.180   -68.226  1.00 23.79 ? 186 SER E CA  1 
ATOM   8183  C C   . SER E 1 186 ? 25.277  6.910   -68.592  1.00 23.89 ? 186 SER E C   1 
ATOM   8184  O O   . SER E 1 186 ? 25.226  5.937   -67.845  1.00 25.37 ? 186 SER E O   1 
ATOM   8185  C CB  . SER E 1 186 ? 23.001  7.967   -68.497  1.00 23.21 ? 186 SER E CB  1 
ATOM   8186  O OG  . SER E 1 186 ? 22.792  7.319   -69.741  1.00 23.73 ? 186 SER E OG  1 
ATOM   8187  N N   . VAL E 1 187 ? 25.986  6.915   -69.720  1.00 23.20 ? 187 VAL E N   1 
ATOM   8188  C CA  . VAL E 1 187 ? 26.726  5.736   -70.181  1.00 23.13 ? 187 VAL E CA  1 
ATOM   8189  C C   . VAL E 1 187 ? 28.210  5.941   -70.454  1.00 22.97 ? 187 VAL E C   1 
ATOM   8190  O O   . VAL E 1 187 ? 28.930  4.961   -70.598  1.00 22.30 ? 187 VAL E O   1 
ATOM   8191  C CB  . VAL E 1 187 ? 26.077  5.137   -71.458  1.00 23.72 ? 187 VAL E CB  1 
ATOM   8192  C CG1 . VAL E 1 187 ? 24.677  4.617   -71.156  1.00 25.19 ? 187 VAL E CG1 1 
ATOM   8193  C CG2 . VAL E 1 187 ? 26.018  6.136   -72.590  1.00 23.45 ? 187 VAL E CG2 1 
ATOM   8194  N N   . VAL E 1 188 ? 28.654  7.194   -70.572  1.00 25.00 ? 188 VAL E N   1 
ATOM   8195  C CA  . VAL E 1 188 ? 30.071  7.532   -70.812  1.00 26.38 ? 188 VAL E CA  1 
ATOM   8196  C C   . VAL E 1 188 ? 30.465  8.875   -70.187  1.00 26.12 ? 188 VAL E C   1 
ATOM   8197  O O   . VAL E 1 188 ? 29.598  9.650   -69.745  1.00 26.09 ? 188 VAL E O   1 
ATOM   8198  C CB  . VAL E 1 188 ? 30.403  7.652   -72.322  1.00 28.21 ? 188 VAL E CB  1 
ATOM   8199  C CG1 . VAL E 1 188 ? 30.056  6.361   -73.081  1.00 29.58 ? 188 VAL E CG1 1 
ATOM   8200  C CG2 . VAL E 1 188 ? 29.734  8.881   -72.943  1.00 28.33 ? 188 VAL E CG2 1 
ATOM   8201  N N   . SER E 1 189 ? 31.769  9.149   -70.166  1.00 26.14 ? 189 SER E N   1 
ATOM   8202  C CA  . SER E 1 189 ? 32.277  10.470  -69.790  1.00 26.40 ? 189 SER E CA  1 
ATOM   8203  C C   . SER E 1 189 ? 33.420  10.911  -70.691  1.00 26.61 ? 189 SER E C   1 
ATOM   8204  O O   . SER E 1 189 ? 33.964  10.124  -71.465  1.00 26.86 ? 189 SER E O   1 
ATOM   8205  C CB  . SER E 1 189 ? 32.706  10.520  -68.318  1.00 25.63 ? 189 SER E CB  1 
ATOM   8206  O OG  . SER E 1 189 ? 33.270  9.295   -67.942  1.00 23.74 ? 189 SER E OG  1 
ATOM   8207  N N   . THR E 1 190 ? 33.773  12.186  -70.567  1.00 26.17 ? 190 THR E N   1 
ATOM   8208  C CA  . THR E 1 190 ? 34.814  12.778  -71.381  1.00 25.36 ? 190 THR E CA  1 
ATOM   8209  C C   . THR E 1 190 ? 36.175  12.287  -70.890  1.00 25.88 ? 190 THR E C   1 
ATOM   8210  O O   . THR E 1 190 ? 36.769  12.848  -69.962  1.00 24.78 ? 190 THR E O   1 
ATOM   8211  C CB  . THR E 1 190 ? 34.707  14.322  -71.392  1.00 24.69 ? 190 THR E CB  1 
ATOM   8212  O OG1 . THR E 1 190 ? 33.356  14.716  -71.672  1.00 22.73 ? 190 THR E OG1 1 
ATOM   8213  C CG2 . THR E 1 190 ? 35.607  14.910  -72.454  1.00 25.63 ? 190 THR E CG2 1 
ATOM   8214  N N   . ASP E 1 191 ? 36.643  11.210  -71.516  1.00 27.40 ? 191 ASP E N   1 
ATOM   8215  C CA  . ASP E 1 191 ? 37.887  10.540  -71.114  1.00 27.14 ? 191 ASP E CA  1 
ATOM   8216  C C   . ASP E 1 191 ? 39.083  10.910  -72.001  1.00 27.29 ? 191 ASP E C   1 
ATOM   8217  O O   . ASP E 1 191 ? 40.173  10.428  -71.790  1.00 29.08 ? 191 ASP E O   1 
ATOM   8218  C CB  . ASP E 1 191 ? 37.694  9.025   -71.125  1.00 25.59 ? 191 ASP E CB  1 
ATOM   8219  C CG  . ASP E 1 191 ? 37.524  8.471   -72.527  1.00 25.35 ? 191 ASP E CG  1 
ATOM   8220  O OD1 . ASP E 1 191 ? 37.027  9.209   -73.409  1.00 25.41 ? 191 ASP E OD1 1 
ATOM   8221  O OD2 . ASP E 1 191 ? 37.876  7.290   -72.741  1.00 24.06 ? 191 ASP E OD2 1 
ATOM   8222  N N   . GLY E 1 192 ? 38.888  11.752  -72.998  1.00 26.95 ? 192 GLY E N   1 
ATOM   8223  C CA  . GLY E 1 192 ? 40.015  12.171  -73.825  1.00 26.47 ? 192 GLY E CA  1 
ATOM   8224  C C   . GLY E 1 192 ? 41.075  12.907  -73.029  1.00 25.55 ? 192 GLY E C   1 
ATOM   8225  O O   . GLY E 1 192 ? 40.765  13.595  -72.056  1.00 23.78 ? 192 GLY E O   1 
ATOM   8226  N N   . VAL E 1 193 ? 42.326  12.768  -73.454  1.00 26.01 ? 193 VAL E N   1 
ATOM   8227  C CA  . VAL E 1 193 ? 43.442  13.397  -72.759  1.00 26.88 ? 193 VAL E CA  1 
ATOM   8228  C C   . VAL E 1 193 ? 43.323  14.930  -72.674  1.00 27.34 ? 193 VAL E C   1 
ATOM   8229  O O   . VAL E 1 193 ? 43.815  15.525  -71.724  1.00 26.91 ? 193 VAL E O   1 
ATOM   8230  C CB  . VAL E 1 193 ? 44.805  12.992  -73.384  1.00 26.90 ? 193 VAL E CB  1 
ATOM   8231  C CG1 . VAL E 1 193 ? 45.021  13.654  -74.731  1.00 26.77 ? 193 VAL E CG1 1 
ATOM   8232  C CG2 . VAL E 1 193 ? 45.960  13.336  -72.453  1.00 27.29 ? 193 VAL E CG2 1 
ATOM   8233  N N   . ASP E 1 194 ? 42.667  15.563  -73.648  1.00 28.33 ? 194 ASP E N   1 
ATOM   8234  C CA  . ASP E 1 194 ? 42.548  17.035  -73.665  1.00 27.90 ? 194 ASP E CA  1 
ATOM   8235  C C   . ASP E 1 194 ? 41.373  17.555  -72.820  1.00 28.83 ? 194 ASP E C   1 
ATOM   8236  O O   . ASP E 1 194 ? 41.161  18.761  -72.742  1.00 28.23 ? 194 ASP E O   1 
ATOM   8237  C CB  . ASP E 1 194 ? 42.484  17.594  -75.104  1.00 26.67 ? 194 ASP E CB  1 
ATOM   8238  C CG  . ASP E 1 194 ? 41.330  17.013  -75.941  1.00 26.29 ? 194 ASP E CG  1 
ATOM   8239  O OD1 . ASP E 1 194 ? 40.396  16.403  -75.357  1.00 26.21 ? 194 ASP E OD1 1 
ATOM   8240  O OD2 . ASP E 1 194 ? 41.371  17.168  -77.197  1.00 25.00 ? 194 ASP E OD2 1 
ATOM   8241  N N   . GLY E 1 195 ? 40.619  16.648  -72.200  1.00 28.64 ? 195 GLY E N   1 
ATOM   8242  C CA  . GLY E 1 195 ? 39.505  17.019  -71.329  1.00 29.28 ? 195 GLY E CA  1 
ATOM   8243  C C   . GLY E 1 195 ? 38.223  17.432  -72.039  1.00 30.06 ? 195 GLY E C   1 
ATOM   8244  O O   . GLY E 1 195 ? 37.288  17.927  -71.396  1.00 29.78 ? 195 GLY E O   1 
ATOM   8245  N N   . ILE E 1 196 ? 38.165  17.228  -73.360  1.00 29.24 ? 196 ILE E N   1 
ATOM   8246  C CA  . ILE E 1 196 ? 36.999  17.637  -74.154  1.00 28.91 ? 196 ILE E CA  1 
ATOM   8247  C C   . ILE E 1 196 ? 36.442  16.538  -75.062  1.00 27.97 ? 196 ILE E C   1 
ATOM   8248  O O   . ILE E 1 196 ? 35.222  16.414  -75.172  1.00 26.80 ? 196 ILE E O   1 
ATOM   8249  C CB  . ILE E 1 196 ? 37.324  18.886  -74.997  1.00 29.40 ? 196 ILE E CB  1 
ATOM   8250  C CG1 . ILE E 1 196 ? 37.557  20.086  -74.078  1.00 29.31 ? 196 ILE E CG1 1 
ATOM   8251  C CG2 . ILE E 1 196 ? 36.201  19.212  -75.977  1.00 29.25 ? 196 ILE E CG2 1 
ATOM   8252  C CD1 . ILE E 1 196 ? 38.542  21.080  -74.642  1.00 29.22 ? 196 ILE E CD1 1 
ATOM   8253  N N   . HIS E 1 197 ? 37.320  15.756  -75.695  1.00 26.51 ? 197 HIS E N   1 
ATOM   8254  C CA  . HIS E 1 197 ? 36.906  14.794  -76.711  1.00 26.69 ? 197 HIS E CA  1 
ATOM   8255  C C   . HIS E 1 197 ? 36.976  13.354  -76.252  1.00 26.39 ? 197 HIS E C   1 
ATOM   8256  O O   . HIS E 1 197 ? 37.369  13.098  -75.120  1.00 24.98 ? 197 HIS E O   1 
ATOM   8257  C CB  . HIS E 1 197 ? 37.722  15.013  -77.976  1.00 26.86 ? 197 HIS E CB  1 
ATOM   8258  C CG  . HIS E 1 197 ? 37.692  16.429  -78.433  1.00 27.04 ? 197 HIS E CG  1 
ATOM   8259  N ND1 . HIS E 1 197 ? 38.728  17.309  -78.206  1.00 27.06 ? 197 HIS E ND1 1 
ATOM   8260  C CD2 . HIS E 1 197 ? 36.714  17.141  -79.038  1.00 27.01 ? 197 HIS E CD2 1 
ATOM   8261  C CE1 . HIS E 1 197 ? 38.406  18.494  -78.687  1.00 26.89 ? 197 HIS E CE1 1 
ATOM   8262  N NE2 . HIS E 1 197 ? 37.189  18.419  -79.197  1.00 27.17 ? 197 HIS E NE2 1 
ATOM   8263  N N   . PHE E 1 198 ? 36.569  12.428  -77.129  1.00 26.25 ? 198 PHE E N   1 
ATOM   8264  C CA  . PHE E 1 198 ? 36.389  11.032  -76.742  1.00 26.64 ? 198 PHE E CA  1 
ATOM   8265  C C   . PHE E 1 198 ? 37.448  10.107  -77.324  1.00 26.07 ? 198 PHE E C   1 
ATOM   8266  O O   . PHE E 1 198 ? 37.926  10.300  -78.424  1.00 26.58 ? 198 PHE E O   1 
ATOM   8267  C CB  . PHE E 1 198 ? 35.009  10.492  -77.188  1.00 26.82 ? 198 PHE E CB  1 
ATOM   8268  C CG  . PHE E 1 198 ? 33.813  11.206  -76.607  1.00 26.16 ? 198 PHE E CG  1 
ATOM   8269  C CD1 . PHE E 1 198 ? 33.899  12.013  -75.481  1.00 26.17 ? 198 PHE E CD1 1 
ATOM   8270  C CD2 . PHE E 1 198 ? 32.566  11.020  -77.192  1.00 26.14 ? 198 PHE E CD2 1 
ATOM   8271  C CE1 . PHE E 1 198 ? 32.766  12.643  -74.971  1.00 26.55 ? 198 PHE E CE1 1 
ATOM   8272  C CE2 . PHE E 1 198 ? 31.437  11.639  -76.684  1.00 26.49 ? 198 PHE E CE2 1 
ATOM   8273  C CZ  . PHE E 1 198 ? 31.537  12.455  -75.572  1.00 26.61 ? 198 PHE E CZ  1 
ATOM   8274  N N   . THR E 1 199 ? 37.768  9.061   -76.579  1.00 26.24 ? 199 THR E N   1 
ATOM   8275  C CA  . THR E 1 199 ? 38.576  7.954   -77.082  1.00 26.06 ? 199 THR E CA  1 
ATOM   8276  C C   . THR E 1 199 ? 37.691  7.041   -77.916  1.00 27.83 ? 199 THR E C   1 
ATOM   8277  O O   . THR E 1 199 ? 36.465  7.151   -77.880  1.00 28.23 ? 199 THR E O   1 
ATOM   8278  C CB  . THR E 1 199 ? 39.148  7.107   -75.945  1.00 23.90 ? 199 THR E CB  1 
ATOM   8279  O OG1 . THR E 1 199 ? 38.070  6.473   -75.243  1.00 23.19 ? 199 THR E OG1 1 
ATOM   8280  C CG2 . THR E 1 199 ? 39.979  7.967   -74.996  1.00 23.37 ? 199 THR E CG2 1 
ATOM   8281  N N   . ALA E 1 200 ? 38.323  6.119   -78.642  1.00 30.15 ? 200 ALA E N   1 
ATOM   8282  C CA  . ALA E 1 200 ? 37.589  5.144   -79.432  1.00 31.42 ? 200 ALA E CA  1 
ATOM   8283  C C   . ALA E 1 200 ? 36.767  4.204   -78.540  1.00 34.51 ? 200 ALA E C   1 
ATOM   8284  O O   . ALA E 1 200 ? 35.682  3.752   -78.925  1.00 33.30 ? 200 ALA E O   1 
ATOM   8285  C CB  . ALA E 1 200 ? 38.534  4.363   -80.320  1.00 30.52 ? 200 ALA E CB  1 
ATOM   8286  N N   . GLU E 1 201 ? 37.283  3.914   -77.346  1.00 39.63 ? 201 GLU E N   1 
ATOM   8287  C CA  . GLU E 1 201 ? 36.564  3.071   -76.403  1.00 42.99 ? 201 GLU E CA  1 
ATOM   8288  C C   . GLU E 1 201 ? 35.259  3.748   -75.979  1.00 38.12 ? 201 GLU E C   1 
ATOM   8289  O O   . GLU E 1 201 ? 34.225  3.079   -75.899  1.00 40.57 ? 201 GLU E O   1 
ATOM   8290  C CB  . GLU E 1 201 ? 37.449  2.734   -75.186  1.00 50.86 ? 201 GLU E CB  1 
ATOM   8291  C CG  . GLU E 1 201 ? 36.840  1.860   -74.095  1.00 56.78 ? 201 GLU E CG  1 
ATOM   8292  C CD  . GLU E 1 201 ? 37.702  1.915   -72.841  1.00 60.05 ? 201 GLU E CD  1 
ATOM   8293  O OE1 . GLU E 1 201 ? 37.790  2.996   -72.202  1.00 55.68 ? 201 GLU E OE1 1 
ATOM   8294  O OE2 . GLU E 1 201 ? 38.316  0.877   -72.523  1.00 65.87 ? 201 GLU E OE2 1 
ATOM   8295  N N   . THR E 1 202 ? 35.294  5.059   -75.731  1.00 35.00 ? 202 THR E N   1 
ATOM   8296  C CA  . THR E 1 202 ? 34.100  5.795   -75.322  1.00 33.79 ? 202 THR E CA  1 
ATOM   8297  C C   . THR E 1 202 ? 33.100  5.892   -76.471  1.00 34.35 ? 202 THR E C   1 
ATOM   8298  O O   . THR E 1 202 ? 31.878  5.783   -76.255  1.00 32.87 ? 202 THR E O   1 
ATOM   8299  C CB  . THR E 1 202 ? 34.446  7.208   -74.823  1.00 32.91 ? 202 THR E CB  1 
ATOM   8300  O OG1 . THR E 1 202 ? 35.056  7.109   -73.541  1.00 32.36 ? 202 THR E OG1 1 
ATOM   8301  C CG2 . THR E 1 202 ? 33.181  8.083   -74.697  1.00 33.06 ? 202 THR E CG2 1 
ATOM   8302  N N   . ASN E 1 203 ? 33.613  6.104   -77.685  1.00 34.29 ? 203 ASN E N   1 
ATOM   8303  C CA  . ASN E 1 203 ? 32.767  6.116   -78.865  1.00 34.59 ? 203 ASN E CA  1 
ATOM   8304  C C   . ASN E 1 203 ? 31.969  4.817   -78.985  1.00 36.37 ? 203 ASN E C   1 
ATOM   8305  O O   . ASN E 1 203 ? 30.757  4.846   -79.213  1.00 37.27 ? 203 ASN E O   1 
ATOM   8306  C CB  . ASN E 1 203 ? 33.598  6.308   -80.130  1.00 34.29 ? 203 ASN E CB  1 
ATOM   8307  C CG  . ASN E 1 203 ? 34.013  7.752   -80.369  1.00 34.26 ? 203 ASN E CG  1 
ATOM   8308  O OD1 . ASN E 1 203 ? 33.524  8.684   -79.723  1.00 34.10 ? 203 ASN E OD1 1 
ATOM   8309  N ND2 . ASN E 1 203 ? 34.928  7.942   -81.326  1.00 33.99 ? 203 ASN E ND2 1 
ATOM   8310  N N   . ARG E 1 204 ? 32.669  3.691   -78.833  1.00 39.70 ? 204 ARG E N   1 
ATOM   8311  C CA  . ARG E 1 204 ? 32.052  2.366   -78.932  1.00 41.43 ? 204 ARG E CA  1 
ATOM   8312  C C   . ARG E 1 204 ? 30.907  2.187   -77.946  1.00 38.04 ? 204 ARG E C   1 
ATOM   8313  O O   . ARG E 1 204 ? 29.837  1.726   -78.323  1.00 34.63 ? 204 ARG E O   1 
ATOM   8314  C CB  . ARG E 1 204 ? 33.087  1.251   -78.733  1.00 46.50 ? 204 ARG E CB  1 
ATOM   8315  C CG  . ARG E 1 204 ? 33.692  0.730   -80.024  1.00 52.34 ? 204 ARG E CG  1 
ATOM   8316  C CD  . ARG E 1 204 ? 34.633  -0.451  -79.790  1.00 58.48 ? 204 ARG E CD  1 
ATOM   8317  N NE  . ARG E 1 204 ? 35.960  -0.022  -79.326  1.00 62.76 ? 204 ARG E NE  1 
ATOM   8318  C CZ  . ARG E 1 204 ? 36.930  0.470   -80.107  1.00 61.39 ? 204 ARG E CZ  1 
ATOM   8319  N NH1 . ARG E 1 204 ? 36.755  0.634   -81.417  1.00 59.75 ? 204 ARG E NH1 1 
ATOM   8320  N NH2 . ARG E 1 204 ? 38.086  0.819   -79.558  1.00 61.62 ? 204 ARG E NH2 1 
ATOM   8321  N N   . THR E 1 205 ? 31.136  2.556   -76.689  1.00 36.59 ? 205 THR E N   1 
ATOM   8322  C CA  . THR E 1 205 ? 30.109  2.424   -75.664  1.00 35.53 ? 205 THR E CA  1 
ATOM   8323  C C   . THR E 1 205 ? 28.879  3.254   -76.041  1.00 34.31 ? 205 THR E C   1 
ATOM   8324  O O   . THR E 1 205 ? 27.750  2.754   -75.999  1.00 31.86 ? 205 THR E O   1 
ATOM   8325  C CB  . THR E 1 205 ? 30.646  2.858   -74.282  1.00 35.39 ? 205 THR E CB  1 
ATOM   8326  O OG1 . THR E 1 205 ? 31.847  2.100   -74.020  1.00 33.44 ? 205 THR E OG1 1 
ATOM   8327  C CG2 . THR E 1 205 ? 29.630  2.591   -73.167  1.00 35.45 ? 205 THR E CG2 1 
ATOM   8328  N N   . LEU E 1 206 ? 29.114  4.513   -76.431  1.00 33.28 ? 206 LEU E N   1 
ATOM   8329  C CA  . LEU E 1 206 ? 28.034  5.449   -76.756  1.00 31.11 ? 206 LEU E CA  1 
ATOM   8330  C C   . LEU E 1 206 ? 27.234  4.981   -77.962  1.00 31.29 ? 206 LEU E C   1 
ATOM   8331  O O   . LEU E 1 206 ? 26.003  5.011   -77.940  1.00 31.88 ? 206 LEU E O   1 
ATOM   8332  C CB  . LEU E 1 206 ? 28.596  6.845   -77.026  1.00 30.43 ? 206 LEU E CB  1 
ATOM   8333  C CG  . LEU E 1 206 ? 27.606  7.965   -77.353  1.00 30.36 ? 206 LEU E CG  1 
ATOM   8334  C CD1 . LEU E 1 206 ? 26.590  8.107   -76.222  1.00 31.46 ? 206 LEU E CD1 1 
ATOM   8335  C CD2 . LEU E 1 206 ? 28.379  9.265   -77.602  1.00 30.08 ? 206 LEU E CD2 1 
ATOM   8336  N N   . GLY E 1 207 ? 27.938  4.552   -79.011  1.00 31.36 ? 207 GLY E N   1 
ATOM   8337  C CA  . GLY E 1 207 ? 27.300  4.062   -80.223  1.00 31.25 ? 207 GLY E CA  1 
ATOM   8338  C C   . GLY E 1 207 ? 26.351  2.917   -79.940  1.00 32.27 ? 207 GLY E C   1 
ATOM   8339  O O   . GLY E 1 207 ? 25.228  2.896   -80.444  1.00 33.62 ? 207 GLY E O   1 
ATOM   8340  N N   . ALA E 1 208 ? 26.801  1.977   -79.115  1.00 32.25 ? 208 ALA E N   1 
ATOM   8341  C CA  . ALA E 1 208 ? 26.014  0.787   -78.796  1.00 31.83 ? 208 ALA E CA  1 
ATOM   8342  C C   . ALA E 1 208 ? 24.819  1.138   -77.929  1.00 30.79 ? 208 ALA E C   1 
ATOM   8343  O O   . ALA E 1 208 ? 23.734  0.591   -78.148  1.00 32.11 ? 208 ALA E O   1 
ATOM   8344  C CB  . ALA E 1 208 ? 26.875  -0.265  -78.109  1.00 32.41 ? 208 ALA E CB  1 
ATOM   8345  N N   . ALA E 1 209 ? 25.011  2.045   -76.972  1.00 29.24 ? 209 ALA E N   1 
ATOM   8346  C CA  . ALA E 1 209 ? 23.933  2.480   -76.083  1.00 28.82 ? 209 ALA E CA  1 
ATOM   8347  C C   . ALA E 1 209 ? 22.876  3.241   -76.855  1.00 28.92 ? 209 ALA E C   1 
ATOM   8348  O O   . ALA E 1 209 ? 21.682  2.992   -76.663  1.00 28.43 ? 209 ALA E O   1 
ATOM   8349  C CB  . ALA E 1 209 ? 24.472  3.365   -74.948  1.00 30.18 ? 209 ALA E CB  1 
ATOM   8350  N N   . VAL E 1 210 ? 23.306  4.163   -77.718  1.00 28.55 ? 210 VAL E N   1 
ATOM   8351  C CA  . VAL E 1 210 ? 22.362  4.979   -78.486  1.00 27.22 ? 210 VAL E CA  1 
ATOM   8352  C C   . VAL E 1 210 ? 21.573  4.117   -79.477  1.00 27.07 ? 210 VAL E C   1 
ATOM   8353  O O   . VAL E 1 210 ? 20.405  4.376   -79.715  1.00 26.95 ? 210 VAL E O   1 
ATOM   8354  C CB  . VAL E 1 210 ? 23.082  6.165   -79.201  1.00 27.00 ? 210 VAL E CB  1 
ATOM   8355  C CG1 . VAL E 1 210 ? 22.154  6.897   -80.158  1.00 25.95 ? 210 VAL E CG1 1 
ATOM   8356  C CG2 . VAL E 1 210 ? 23.636  7.144   -78.172  1.00 27.54 ? 210 VAL E CG2 1 
ATOM   8357  N N   . ALA E 1 211 ? 22.200  3.087   -80.029  1.00 27.05 ? 211 ALA E N   1 
ATOM   8358  C CA  . ALA E 1 211 ? 21.518  2.154   -80.927  1.00 27.71 ? 211 ALA E CA  1 
ATOM   8359  C C   . ALA E 1 211 ? 20.326  1.462   -80.261  1.00 28.07 ? 211 ALA E C   1 
ATOM   8360  O O   . ALA E 1 211 ? 19.294  1.260   -80.885  1.00 27.99 ? 211 ALA E O   1 
ATOM   8361  C CB  . ALA E 1 211 ? 22.495  1.110   -81.455  1.00 27.47 ? 211 ALA E CB  1 
ATOM   8362  N N   . GLN E 1 212 ? 20.470  1.078   -78.993  1.00 29.12 ? 212 GLN E N   1 
ATOM   8363  C CA  . GLN E 1 212 ? 19.350  0.504   -78.241  1.00 30.02 ? 212 GLN E CA  1 
ATOM   8364  C C   . GLN E 1 212 ? 18.213  1.482   -78.132  1.00 29.16 ? 212 GLN E C   1 
ATOM   8365  O O   . GLN E 1 212 ? 17.061  1.151   -78.381  1.00 25.12 ? 212 GLN E O   1 
ATOM   8366  C CB  . GLN E 1 212 ? 19.824  0.021   -76.876  1.00 31.33 ? 212 GLN E CB  1 
ATOM   8367  C CG  . GLN E 1 212 ? 20.811  -1.135  -76.940  1.00 32.16 ? 212 GLN E CG  1 
ATOM   8368  C CD  . GLN E 1 212 ? 20.550  -2.149  -78.068  1.00 32.08 ? 212 GLN E CD  1 
ATOM   8369  O OE1 . GLN E 1 212 ? 19.410  -2.589  -78.307  1.00 28.25 ? 212 GLN E OE1 1 
ATOM   8370  N NE2 . GLN E 1 212 ? 21.622  -2.516  -78.761  1.00 32.12 ? 212 GLN E NE2 1 
ATOM   8371  N N   . LYS E 1 213 ? 18.555  2.711   -77.774  1.00 29.38 ? 213 LYS E N   1 
ATOM   8372  C CA  . LYS E 1 213 ? 17.567  3.776   -77.634  1.00 31.16 ? 213 LYS E CA  1 
ATOM   8373  C C   . LYS E 1 213 ? 16.822  4.009   -78.959  1.00 32.46 ? 213 LYS E C   1 
ATOM   8374  O O   . LYS E 1 213 ? 15.593  4.114   -78.976  1.00 32.71 ? 213 LYS E O   1 
ATOM   8375  C CB  . LYS E 1 213 ? 18.262  5.043   -77.152  1.00 31.11 ? 213 LYS E CB  1 
ATOM   8376  C CG  . LYS E 1 213 ? 17.381  6.261   -76.986  1.00 30.69 ? 213 LYS E CG  1 
ATOM   8377  C CD  . LYS E 1 213 ? 16.267  6.017   -75.992  1.00 30.26 ? 213 LYS E CD  1 
ATOM   8378  C CE  . LYS E 1 213 ? 15.797  7.368   -75.374  1.00 30.27 ? 213 LYS E CE  1 
ATOM   8379  N NZ  . LYS E 1 213 ? 14.383  7.241   -74.946  1.00 30.12 ? 213 LYS E NZ  1 
ATOM   8380  N N   . VAL E 1 214 ? 17.567  4.077   -80.059  1.00 31.66 ? 214 VAL E N   1 
ATOM   8381  C CA  . VAL E 1 214 ? 16.973  4.304   -81.371  1.00 31.20 ? 214 VAL E CA  1 
ATOM   8382  C C   . VAL E 1 214 ? 15.951  3.224   -81.732  1.00 30.55 ? 214 VAL E C   1 
ATOM   8383  O O   . VAL E 1 214 ? 14.842  3.544   -82.143  1.00 30.74 ? 214 VAL E O   1 
ATOM   8384  C CB  . VAL E 1 214 ? 18.063  4.413   -82.461  1.00 31.16 ? 214 VAL E CB  1 
ATOM   8385  C CG1 . VAL E 1 214 ? 17.464  4.363   -83.847  1.00 31.84 ? 214 VAL E CG1 1 
ATOM   8386  C CG2 . VAL E 1 214 ? 18.836  5.712   -82.290  1.00 31.46 ? 214 VAL E CG2 1 
ATOM   8387  N N   . LYS E 1 215 ? 16.315  1.959   -81.565  1.00 31.64 ? 215 LYS E N   1 
ATOM   8388  C CA  . LYS E 1 215 ? 15.408  0.830   -81.850  1.00 33.30 ? 215 LYS E CA  1 
ATOM   8389  C C   . LYS E 1 215 ? 14.113  0.888   -81.054  1.00 34.76 ? 215 LYS E C   1 
ATOM   8390  O O   . LYS E 1 215 ? 13.050  0.552   -81.566  1.00 34.69 ? 215 LYS E O   1 
ATOM   8391  C CB  . LYS E 1 215 ? 16.091  -0.507  -81.566  1.00 33.31 ? 215 LYS E CB  1 
ATOM   8392  C CG  . LYS E 1 215 ? 17.153  -0.886  -82.558  1.00 34.56 ? 215 LYS E CG  1 
ATOM   8393  C CD  . LYS E 1 215 ? 17.845  -2.154  -82.094  1.00 35.08 ? 215 LYS E CD  1 
ATOM   8394  C CE  . LYS E 1 215 ? 19.065  -2.493  -82.939  1.00 36.44 ? 215 LYS E CE  1 
ATOM   8395  N NZ  . LYS E 1 215 ? 19.825  -3.552  -82.209  1.00 36.65 ? 215 LYS E NZ  1 
ATOM   8396  N N   . THR E 1 216 ? 14.208  1.292   -79.794  1.00 37.40 ? 216 THR E N   1 
ATOM   8397  C CA  . THR E 1 216 ? 13.024  1.572   -78.979  1.00 36.21 ? 216 THR E CA  1 
ATOM   8398  C C   . THR E 1 216 ? 12.071  2.557   -79.661  1.00 34.67 ? 216 THR E C   1 
ATOM   8399  O O   . THR E 1 216 ? 10.856  2.376   -79.611  1.00 34.76 ? 216 THR E O   1 
ATOM   8400  C CB  . THR E 1 216 ? 13.439  2.123   -77.601  1.00 37.00 ? 216 THR E CB  1 
ATOM   8401  O OG1 . THR E 1 216 ? 14.060  1.069   -76.853  1.00 34.71 ? 216 THR E OG1 1 
ATOM   8402  C CG2 . THR E 1 216 ? 12.228  2.696   -76.823  1.00 37.71 ? 216 THR E CG2 1 
ATOM   8403  N N   . LEU E 1 217 ? 12.622  3.595   -80.289  1.00 32.96 ? 217 LEU E N   1 
ATOM   8404  C CA  . LEU E 1 217 ? 11.812  4.637   -80.928  1.00 30.98 ? 217 LEU E CA  1 
ATOM   8405  C C   . LEU E 1 217 ? 11.254  4.224   -82.295  1.00 31.52 ? 217 LEU E C   1 
ATOM   8406  O O   . LEU E 1 217 ? 10.136  4.568   -82.627  1.00 31.45 ? 217 LEU E O   1 
ATOM   8407  C CB  . LEU E 1 217 ? 12.607  5.928   -81.064  1.00 29.19 ? 217 LEU E CB  1 
ATOM   8408  C CG  . LEU E 1 217 ? 13.093  6.578   -79.764  1.00 28.12 ? 217 LEU E CG  1 
ATOM   8409  C CD1 . LEU E 1 217 ? 13.855  7.866   -80.044  1.00 27.51 ? 217 LEU E CD1 1 
ATOM   8410  C CD2 . LEU E 1 217 ? 11.975  6.945   -78.795  1.00 28.32 ? 217 LEU E CD2 1 
ATOM   8411  N N   . LEU E 1 218 ? 12.027  3.504   -83.084  1.00 33.74 ? 218 LEU E N   1 
ATOM   8412  C CA  . LEU E 1 218 ? 11.642  3.224   -84.473  1.00 36.42 ? 218 LEU E CA  1 
ATOM   8413  C C   . LEU E 1 218 ? 11.111  1.799   -84.782  1.00 38.79 ? 218 LEU E C   1 
ATOM   8414  O O   . LEU E 1 218 ? 10.373  1.634   -85.734  1.00 37.02 ? 218 LEU E O   1 
ATOM   8415  C CB  . LEU E 1 218 ? 12.825  3.540   -85.402  1.00 35.73 ? 218 LEU E CB  1 
ATOM   8416  C CG  . LEU E 1 218 ? 13.371  4.984   -85.333  1.00 34.21 ? 218 LEU E CG  1 
ATOM   8417  C CD1 . LEU E 1 218 ? 14.534  5.189   -86.288  1.00 33.83 ? 218 LEU E CD1 1 
ATOM   8418  C CD2 . LEU E 1 218 ? 12.291  6.028   -85.617  1.00 34.12 ? 218 LEU E CD2 1 
ATOM   8419  N N   . GLN E 1 219 ? 11.516  0.796   -84.008  1.00 45.17 ? 219 GLN E N   1 
ATOM   8420  C CA  . GLN E 1 219 ? 11.486  -0.647  -84.392  1.00 46.62 ? 219 GLN E CA  1 
ATOM   8421  C C   . GLN E 1 219 ? 11.501  -0.967  -85.888  1.00 50.10 ? 219 GLN E C   1 
ATOM   8422  O O   . GLN E 1 219 ? 11.231  -2.100  -86.298  1.00 51.35 ? 219 GLN E O   1 
ATOM   8423  C CB  . GLN E 1 219 ? 10.317  -1.371  -83.785  1.00 46.51 ? 219 GLN E CB  1 
ATOM   8424  C CG  . GLN E 1 219 ? 10.013  -1.005  -82.359  1.00 45.44 ? 219 GLN E CG  1 
ATOM   8425  C CD  . GLN E 1 219 ? 8.926   0.032   -82.276  1.00 45.73 ? 219 GLN E CD  1 
ATOM   8426  O OE1 . GLN E 1 219 ? 8.508   0.621   -83.277  1.00 43.48 ? 219 GLN E OE1 1 
ATOM   8427  N NE2 . GLN E 1 219 ? 8.449   0.256   -81.071  1.00 46.98 ? 219 GLN E NE2 1 
ATOM   8428  N N   . ASP F 1 2   ? -10.700 68.911  -66.512  1.00 59.30 ? 2   ASP F N   1 
ATOM   8429  C CA  . ASP F 1 2   ? -9.307  69.071  -67.004  1.00 61.21 ? 2   ASP F CA  1 
ATOM   8430  C C   . ASP F 1 2   ? -8.580  67.746  -67.204  1.00 59.84 ? 2   ASP F C   1 
ATOM   8431  O O   . ASP F 1 2   ? -8.195  67.077  -66.246  1.00 57.92 ? 2   ASP F O   1 
ATOM   8432  C CB  . ASP F 1 2   ? -8.498  69.960  -66.040  1.00 61.17 ? 2   ASP F CB  1 
ATOM   8433  C CG  . ASP F 1 2   ? -8.624  71.426  -66.353  1.00 61.88 ? 2   ASP F CG  1 
ATOM   8434  O OD1 . ASP F 1 2   ? -8.763  71.774  -67.546  1.00 58.75 ? 2   ASP F OD1 1 
ATOM   8435  O OD2 . ASP F 1 2   ? -8.584  72.224  -65.398  1.00 69.09 ? 2   ASP F OD2 1 
ATOM   8436  N N   . LYS F 1 3   ? -8.321  67.434  -68.473  1.00 58.52 ? 3   LYS F N   1 
ATOM   8437  C CA  . LYS F 1 3   ? -7.421  66.350  -68.888  1.00 57.36 ? 3   LYS F CA  1 
ATOM   8438  C C   . LYS F 1 3   ? -6.090  66.397  -68.103  1.00 53.06 ? 3   LYS F C   1 
ATOM   8439  O O   . LYS F 1 3   ? -5.487  67.465  -67.981  1.00 52.25 ? 3   LYS F O   1 
ATOM   8440  C CB  . LYS F 1 3   ? -7.168  66.495  -70.398  1.00 60.71 ? 3   LYS F CB  1 
ATOM   8441  C CG  . LYS F 1 3   ? -6.361  65.375  -71.032  1.00 61.07 ? 3   LYS F CG  1 
ATOM   8442  C CD  . LYS F 1 3   ? -5.635  65.794  -72.301  1.00 59.44 ? 3   LYS F CD  1 
ATOM   8443  C CE  . LYS F 1 3   ? -4.380  64.940  -72.474  1.00 59.48 ? 3   LYS F CE  1 
ATOM   8444  N NZ  . LYS F 1 3   ? -4.130  64.426  -73.840  1.00 59.13 ? 3   LYS F NZ  1 
ATOM   8445  N N   . ILE F 1 4   ? -5.641  65.258  -67.577  1.00 46.87 ? 4   ILE F N   1 
ATOM   8446  C CA  . ILE F 1 4   ? -4.311  65.169  -66.971  1.00 44.60 ? 4   ILE F CA  1 
ATOM   8447  C C   . ILE F 1 4   ? -3.274  65.102  -68.099  1.00 44.49 ? 4   ILE F C   1 
ATOM   8448  O O   . ILE F 1 4   ? -3.407  64.306  -69.007  1.00 48.74 ? 4   ILE F O   1 
ATOM   8449  C CB  . ILE F 1 4   ? -4.153  63.928  -66.058  1.00 43.08 ? 4   ILE F CB  1 
ATOM   8450  C CG1 . ILE F 1 4   ? -5.156  63.928  -64.911  1.00 42.57 ? 4   ILE F CG1 1 
ATOM   8451  C CG2 . ILE F 1 4   ? -2.736  63.854  -65.512  1.00 42.91 ? 4   ILE F CG2 1 
ATOM   8452  C CD1 . ILE F 1 4   ? -5.356  62.539  -64.314  1.00 42.37 ? 4   ILE F CD1 1 
ATOM   8453  N N   . LYS F 1 5   ? -2.239  65.931  -68.033  1.00 41.72 ? 5   LYS F N   1 
ATOM   8454  C CA  . LYS F 1 5   ? -1.216  66.000  -69.075  1.00 39.12 ? 5   LYS F CA  1 
ATOM   8455  C C   . LYS F 1 5   ? -0.092  65.002  -68.876  1.00 34.64 ? 5   LYS F C   1 
ATOM   8456  O O   . LYS F 1 5   ? 0.533   64.964  -67.823  1.00 32.20 ? 5   LYS F O   1 
ATOM   8457  C CB  . LYS F 1 5   ? -0.665  67.433  -69.164  1.00 41.20 ? 5   LYS F CB  1 
ATOM   8458  C CG  . LYS F 1 5   ? -1.677  68.367  -69.788  1.00 43.54 ? 5   LYS F CG  1 
ATOM   8459  C CD  . LYS F 1 5   ? -1.613  69.809  -69.322  1.00 42.71 ? 5   LYS F CD  1 
ATOM   8460  C CE  . LYS F 1 5   ? -2.896  70.507  -69.685  1.00 44.08 ? 5   LYS F CE  1 
ATOM   8461  N NZ  . LYS F 1 5   ? -2.597  71.954  -69.757  1.00 47.04 ? 5   LYS F NZ  1 
ATOM   8462  N N   . ARG F 1 6   ? 0.182   64.210  -69.903  1.00 31.33 ? 6   ARG F N   1 
ATOM   8463  C CA  . ARG F 1 6   ? 1.154   63.129  -69.799  1.00 30.18 ? 6   ARG F CA  1 
ATOM   8464  C C   . ARG F 1 6   ? 2.516   63.519  -70.397  1.00 27.92 ? 6   ARG F C   1 
ATOM   8465  O O   . ARG F 1 6   ? 2.600   63.905  -71.562  1.00 27.88 ? 6   ARG F O   1 
ATOM   8466  C CB  . ARG F 1 6   ? 0.582   61.860  -70.438  1.00 30.24 ? 6   ARG F CB  1 
ATOM   8467  C CG  . ARG F 1 6   ? -0.531  61.252  -69.598  1.00 30.51 ? 6   ARG F CG  1 
ATOM   8468  C CD  . ARG F 1 6   ? -1.288  60.140  -70.324  1.00 31.77 ? 6   ARG F CD  1 
ATOM   8469  N NE  . ARG F 1 6   ? -0.414  59.146  -70.954  1.00 33.00 ? 6   ARG F NE  1 
ATOM   8470  C CZ  . ARG F 1 6   ? 0.353   58.278  -70.295  1.00 34.65 ? 6   ARG F CZ  1 
ATOM   8471  N NH1 . ARG F 1 6   ? 0.377   58.254  -68.982  1.00 35.66 ? 6   ARG F NH1 1 
ATOM   8472  N NH2 . ARG F 1 6   ? 1.103   57.404  -70.949  1.00 35.15 ? 6   ARG F NH2 1 
ATOM   8473  N N   . VAL F 1 7   ? 3.565   63.447  -69.575  1.00 24.47 ? 7   VAL F N   1 
ATOM   8474  C CA  . VAL F 1 7   ? 4.909   63.825  -69.994  1.00 21.98 ? 7   VAL F CA  1 
ATOM   8475  C C   . VAL F 1 7   ? 5.864   62.629  -69.916  1.00 21.17 ? 7   VAL F C   1 
ATOM   8476  O O   . VAL F 1 7   ? 6.071   62.047  -68.855  1.00 19.94 ? 7   VAL F O   1 
ATOM   8477  C CB  . VAL F 1 7   ? 5.472   64.970  -69.136  1.00 21.36 ? 7   VAL F CB  1 
ATOM   8478  C CG1 . VAL F 1 7   ? 6.872   65.368  -69.593  1.00 20.85 ? 7   VAL F CG1 1 
ATOM   8479  C CG2 . VAL F 1 7   ? 4.514   66.147  -69.125  1.00 21.30 ? 7   VAL F CG2 1 
ATOM   8480  N N   . PHE F 1 8   ? 6.458   62.278  -71.056  1.00 20.54 ? 8   PHE F N   1 
ATOM   8481  C CA  . PHE F 1 8   ? 7.385   61.169  -71.139  1.00 19.70 ? 8   PHE F CA  1 
ATOM   8482  C C   . PHE F 1 8   ? 8.810   61.695  -71.133  1.00 20.12 ? 8   PHE F C   1 
ATOM   8483  O O   . PHE F 1 8   ? 9.150   62.553  -71.933  1.00 19.27 ? 8   PHE F O   1 
ATOM   8484  C CB  . PHE F 1 8   ? 7.117   60.377  -72.412  1.00 19.10 ? 8   PHE F CB  1 
ATOM   8485  C CG  . PHE F 1 8   ? 8.049   59.214  -72.611  1.00 18.66 ? 8   PHE F CG  1 
ATOM   8486  C CD1 . PHE F 1 8   ? 8.260   58.298  -71.603  1.00 18.22 ? 8   PHE F CD1 1 
ATOM   8487  C CD2 . PHE F 1 8   ? 8.695   59.024  -73.828  1.00 18.84 ? 8   PHE F CD2 1 
ATOM   8488  C CE1 . PHE F 1 8   ? 9.099   57.227  -71.793  1.00 18.39 ? 8   PHE F CE1 1 
ATOM   8489  C CE2 . PHE F 1 8   ? 9.536   57.942  -74.032  1.00 18.11 ? 8   PHE F CE2 1 
ATOM   8490  C CZ  . PHE F 1 8   ? 9.739   57.047  -73.013  1.00 18.18 ? 8   PHE F CZ  1 
ATOM   8491  N N   . VAL F 1 9   ? 9.631   61.189  -70.218  1.00 21.43 ? 9   VAL F N   1 
ATOM   8492  C CA  . VAL F 1 9   ? 11.028  61.613  -70.099  1.00 21.95 ? 9   VAL F CA  1 
ATOM   8493  C C   . VAL F 1 9   ? 11.953  60.480  -70.533  1.00 22.53 ? 9   VAL F C   1 
ATOM   8494  O O   . VAL F 1 9   ? 11.949  59.393  -69.946  1.00 21.61 ? 9   VAL F O   1 
ATOM   8495  C CB  . VAL F 1 9   ? 11.403  61.996  -68.667  1.00 22.27 ? 9   VAL F CB  1 
ATOM   8496  C CG1 . VAL F 1 9   ? 12.784  62.642  -68.652  1.00 22.32 ? 9   VAL F CG1 1 
ATOM   8497  C CG2 . VAL F 1 9   ? 10.362  62.934  -68.075  1.00 22.81 ? 9   VAL F CG2 1 
ATOM   8498  N N   . PHE F 1 10  ? 12.768  60.761  -71.543  1.00 22.87 ? 10  PHE F N   1 
ATOM   8499  C CA  . PHE F 1 10  ? 13.610  59.766  -72.177  1.00 22.89 ? 10  PHE F CA  1 
ATOM   8500  C C   . PHE F 1 10  ? 15.050  60.196  -72.007  1.00 23.15 ? 10  PHE F C   1 
ATOM   8501  O O   . PHE F 1 10  ? 15.464  61.207  -72.563  1.00 23.09 ? 10  PHE F O   1 
ATOM   8502  C CB  . PHE F 1 10  ? 13.239  59.706  -73.660  1.00 22.91 ? 10  PHE F CB  1 
ATOM   8503  C CG  . PHE F 1 10  ? 13.873  58.570  -74.406  1.00 21.97 ? 10  PHE F CG  1 
ATOM   8504  C CD1 . PHE F 1 10  ? 13.603  57.273  -74.059  1.00 21.60 ? 10  PHE F CD1 1 
ATOM   8505  C CD2 . PHE F 1 10  ? 14.707  58.811  -75.488  1.00 22.16 ? 10  PHE F CD2 1 
ATOM   8506  C CE1 . PHE F 1 10  ? 14.170  56.226  -74.757  1.00 21.67 ? 10  PHE F CE1 1 
ATOM   8507  C CE2 . PHE F 1 10  ? 15.278  57.779  -76.192  1.00 21.37 ? 10  PHE F CE2 1 
ATOM   8508  C CZ  . PHE F 1 10  ? 15.008  56.486  -75.827  1.00 21.62 ? 10  PHE F CZ  1 
ATOM   8509  N N   . GLY F 1 11  ? 15.816  59.448  -71.229  1.00 24.47 ? 11  GLY F N   1 
ATOM   8510  C CA  . GLY F 1 11  ? 17.196  59.841  -70.941  1.00 26.35 ? 11  GLY F CA  1 
ATOM   8511  C C   . GLY F 1 11  ? 18.139  58.693  -70.645  1.00 28.48 ? 11  GLY F C   1 
ATOM   8512  O O   . GLY F 1 11  ? 17.870  57.544  -70.977  1.00 29.54 ? 11  GLY F O   1 
ATOM   8513  N N   . ASP F 1 12  ? 19.249  59.034  -70.002  1.00 30.18 ? 12  ASP F N   1 
ATOM   8514  C CA  . ASP F 1 12  ? 20.321  58.088  -69.720  1.00 30.15 ? 12  ASP F CA  1 
ATOM   8515  C C   . ASP F 1 12  ? 20.387  57.883  -68.202  1.00 31.72 ? 12  ASP F C   1 
ATOM   8516  O O   . ASP F 1 12  ? 19.372  57.962  -67.532  1.00 29.16 ? 12  ASP F O   1 
ATOM   8517  C CB  . ASP F 1 12  ? 21.650  58.576  -70.347  1.00 29.78 ? 12  ASP F CB  1 
ATOM   8518  C CG  . ASP F 1 12  ? 21.937  60.058  -70.079  1.00 29.36 ? 12  ASP F CG  1 
ATOM   8519  O OD1 . ASP F 1 12  ? 21.430  60.586  -69.051  1.00 29.58 ? 12  ASP F OD1 1 
ATOM   8520  O OD2 . ASP F 1 12  ? 22.654  60.680  -70.923  1.00 28.83 ? 12  ASP F OD2 1 
HETATM 8521  N N   . SEP F 1 13  ? 21.572  57.612  -67.664  1.00 35.62 ? 13  SEP F N   1 
HETATM 8522  C CA  . SEP F 1 13  ? 21.746  57.296  -66.245  1.00 38.46 ? 13  SEP F CA  1 
HETATM 8523  C CB  . SEP F 1 13  ? 23.192  56.837  -65.961  1.00 46.26 ? 13  SEP F CB  1 
HETATM 8524  O OG  . SEP F 1 13  ? 24.016  56.647  -67.177  1.00 59.96 ? 13  SEP F OG  1 
HETATM 8525  C C   . SEP F 1 13  ? 21.408  58.480  -65.386  1.00 34.98 ? 13  SEP F C   1 
HETATM 8526  O O   . SEP F 1 13  ? 21.005  58.316  -64.242  1.00 36.63 ? 13  SEP F O   1 
HETATM 8527  P P   . SEP F 1 13  ? 25.196  57.560  -67.836  1.00 66.88 ? 13  SEP F P   1 
HETATM 8528  O O1P . SEP F 1 13  ? 26.508  56.783  -67.748  1.00 62.27 ? 13  SEP F O1P 1 
HETATM 8529  O O2P . SEP F 1 13  ? 24.923  57.506  -69.316  1.00 69.03 ? 13  SEP F O2P 1 
HETATM 8530  O O3P . SEP F 1 13  ? 25.164  58.937  -67.182  1.00 65.84 ? 13  SEP F O3P 1 
ATOM   8531  N N   . LEU F 1 14  ? 21.577  59.685  -65.928  1.00 30.58 ? 14  LEU F N   1 
ATOM   8532  C CA  . LEU F 1 14  ? 21.184  60.915  -65.227  1.00 29.31 ? 14  LEU F CA  1 
ATOM   8533  C C   . LEU F 1 14  ? 19.703  60.908  -64.876  1.00 27.98 ? 14  LEU F C   1 
ATOM   8534  O O   . LEU F 1 14  ? 19.297  61.456  -63.859  1.00 29.15 ? 14  LEU F O   1 
ATOM   8535  C CB  . LEU F 1 14  ? 21.481  62.158  -66.077  1.00 28.65 ? 14  LEU F CB  1 
ATOM   8536  C CG  . LEU F 1 14  ? 22.948  62.466  -66.420  1.00 28.56 ? 14  LEU F CG  1 
ATOM   8537  C CD1 . LEU F 1 14  ? 23.092  63.646  -67.393  1.00 27.87 ? 14  LEU F CD1 1 
ATOM   8538  C CD2 . LEU F 1 14  ? 23.753  62.714  -65.145  1.00 28.11 ? 14  LEU F CD2 1 
ATOM   8539  N N   . THR F 1 15  ? 18.907  60.301  -65.745  1.00 26.88 ? 15  THR F N   1 
ATOM   8540  C CA  . THR F 1 15  ? 17.452  60.220  -65.608  1.00 25.59 ? 15  THR F CA  1 
ATOM   8541  C C   . THR F 1 15  ? 17.014  58.928  -64.872  1.00 24.86 ? 15  THR F C   1 
ATOM   8542  O O   . THR F 1 15  ? 15.984  58.917  -64.203  1.00 24.37 ? 15  THR F O   1 
ATOM   8543  C CB  . THR F 1 15  ? 16.813  60.299  -67.009  1.00 24.93 ? 15  THR F CB  1 
ATOM   8544  O OG1 . THR F 1 15  ? 17.262  61.502  -67.664  1.00 25.54 ? 15  THR F OG1 1 
ATOM   8545  C CG2 . THR F 1 15  ? 15.308  60.268  -66.937  1.00 23.98 ? 15  THR F CG2 1 
ATOM   8546  N N   . TRP F 1 16  ? 17.796  57.855  -64.993  1.00 24.12 ? 16  TRP F N   1 
ATOM   8547  C CA  . TRP F 1 16  ? 17.612  56.650  -64.181  1.00 23.56 ? 16  TRP F CA  1 
ATOM   8548  C C   . TRP F 1 16  ? 17.785  56.978  -62.711  1.00 23.67 ? 16  TRP F C   1 
ATOM   8549  O O   . TRP F 1 16  ? 16.996  56.555  -61.870  1.00 24.06 ? 16  TRP F O   1 
ATOM   8550  C CB  . TRP F 1 16  ? 18.636  55.575  -64.580  1.00 24.19 ? 16  TRP F CB  1 
ATOM   8551  C CG  . TRP F 1 16  ? 18.562  54.276  -63.786  1.00 24.91 ? 16  TRP F CG  1 
ATOM   8552  C CD1 . TRP F 1 16  ? 17.586  53.327  -63.856  1.00 25.86 ? 16  TRP F CD1 1 
ATOM   8553  C CD2 . TRP F 1 16  ? 19.521  53.785  -62.835  1.00 24.58 ? 16  TRP F CD2 1 
ATOM   8554  N NE1 . TRP F 1 16  ? 17.863  52.285  -62.992  1.00 25.55 ? 16  TRP F NE1 1 
ATOM   8555  C CE2 . TRP F 1 16  ? 19.050  52.543  -62.363  1.00 24.64 ? 16  TRP F CE2 1 
ATOM   8556  C CE3 . TRP F 1 16  ? 20.727  54.276  -62.335  1.00 24.76 ? 16  TRP F CE3 1 
ATOM   8557  C CZ2 . TRP F 1 16  ? 19.743  51.793  -61.416  1.00 24.56 ? 16  TRP F CZ2 1 
ATOM   8558  C CZ3 . TRP F 1 16  ? 21.407  53.527  -61.380  1.00 24.62 ? 16  TRP F CZ3 1 
ATOM   8559  C CH2 . TRP F 1 16  ? 20.915  52.305  -60.935  1.00 24.19 ? 16  TRP F CH2 1 
ATOM   8560  N N   . GLY F 1 17  ? 18.839  57.730  -62.409  1.00 24.58 ? 17  GLY F N   1 
ATOM   8561  C CA  . GLY F 1 17  ? 19.160  58.130  -61.040  1.00 25.24 ? 17  GLY F CA  1 
ATOM   8562  C C   . GLY F 1 17  ? 20.470  57.548  -60.538  1.00 26.05 ? 17  GLY F C   1 
ATOM   8563  O O   . GLY F 1 17  ? 20.511  56.971  -59.456  1.00 27.27 ? 17  GLY F O   1 
ATOM   8564  N N   . TRP F 1 18  ? 21.538  57.705  -61.314  1.00 27.25 ? 18  TRP F N   1 
ATOM   8565  C CA  . TRP F 1 18  ? 22.854  57.229  -60.907  1.00 29.06 ? 18  TRP F CA  1 
ATOM   8566  C C   . TRP F 1 18  ? 23.361  58.031  -59.714  1.00 29.48 ? 18  TRP F C   1 
ATOM   8567  O O   . TRP F 1 18  ? 23.495  59.254  -59.805  1.00 28.23 ? 18  TRP F O   1 
ATOM   8568  C CB  . TRP F 1 18  ? 23.840  57.372  -62.068  1.00 30.18 ? 18  TRP F CB  1 
ATOM   8569  C CG  . TRP F 1 18  ? 25.229  56.786  -61.816  1.00 29.91 ? 18  TRP F CG  1 
ATOM   8570  C CD1 . TRP F 1 18  ? 26.129  57.163  -60.866  1.00 29.88 ? 18  TRP F CD1 1 
ATOM   8571  C CD2 . TRP F 1 18  ? 25.867  55.761  -62.587  1.00 28.21 ? 18  TRP F CD2 1 
ATOM   8572  N NE1 . TRP F 1 18  ? 27.274  56.421  -60.981  1.00 30.37 ? 18  TRP F NE1 1 
ATOM   8573  C CE2 . TRP F 1 18  ? 27.131  55.551  -62.036  1.00 28.84 ? 18  TRP F CE2 1 
ATOM   8574  C CE3 . TRP F 1 18  ? 25.476  54.992  -63.683  1.00 26.86 ? 18  TRP F CE3 1 
ATOM   8575  C CZ2 . TRP F 1 18  ? 28.021  54.600  -62.556  1.00 28.44 ? 18  TRP F CZ2 1 
ATOM   8576  C CZ3 . TRP F 1 18  ? 26.361  54.050  -64.196  1.00 26.51 ? 18  TRP F CZ3 1 
ATOM   8577  C CH2 . TRP F 1 18  ? 27.607  53.858  -63.627  1.00 27.13 ? 18  TRP F CH2 1 
ATOM   8578  N N   . THR F 1 19  ? 23.646  57.334  -58.614  1.00 29.18 ? 19  THR F N   1 
ATOM   8579  C CA  . THR F 1 19  ? 24.236  57.953  -57.435  1.00 28.41 ? 19  THR F CA  1 
ATOM   8580  C C   . THR F 1 19  ? 25.757  58.015  -57.627  1.00 29.18 ? 19  THR F C   1 
ATOM   8581  O O   . THR F 1 19  ? 26.391  56.963  -57.741  1.00 31.30 ? 19  THR F O   1 
ATOM   8582  C CB  . THR F 1 19  ? 23.913  57.153  -56.153  1.00 28.28 ? 19  THR F CB  1 
ATOM   8583  O OG1 . THR F 1 19  ? 22.494  57.066  -55.961  1.00 26.55 ? 19  THR F OG1 1 
ATOM   8584  C CG2 . THR F 1 19  ? 24.550  57.812  -54.931  1.00 29.65 ? 19  THR F CG2 1 
ATOM   8585  N N   . PRO F 1 20  ? 26.346  59.231  -57.688  1.00 28.67 ? 20  PRO F N   1 
ATOM   8586  C CA  . PRO F 1 20  ? 27.810  59.326  -57.877  1.00 27.76 ? 20  PRO F CA  1 
ATOM   8587  C C   . PRO F 1 20  ? 28.565  58.813  -56.662  1.00 28.00 ? 20  PRO F C   1 
ATOM   8588  O O   . PRO F 1 20  ? 28.206  59.146  -55.533  1.00 27.47 ? 20  PRO F O   1 
ATOM   8589  C CB  . PRO F 1 20  ? 28.071  60.827  -58.102  1.00 26.82 ? 20  PRO F CB  1 
ATOM   8590  C CG  . PRO F 1 20  ? 26.840  61.529  -57.618  1.00 27.11 ? 20  PRO F CG  1 
ATOM   8591  C CD  . PRO F 1 20  ? 25.691  60.553  -57.699  1.00 28.48 ? 20  PRO F CD  1 
ATOM   8592  N N   . VAL F 1 21  ? 29.588  57.993  -56.903  1.00 29.14 ? 21  VAL F N   1 
ATOM   8593  C CA  . VAL F 1 21  ? 30.328  57.319  -55.834  1.00 29.87 ? 21  VAL F CA  1 
ATOM   8594  C C   . VAL F 1 21  ? 31.781  57.065  -56.214  1.00 30.22 ? 21  VAL F C   1 
ATOM   8595  O O   . VAL F 1 21  ? 32.186  57.256  -57.371  1.00 31.05 ? 21  VAL F O   1 
ATOM   8596  C CB  . VAL F 1 21  ? 29.671  55.966  -55.477  1.00 30.66 ? 21  VAL F CB  1 
ATOM   8597  C CG1 . VAL F 1 21  ? 28.371  56.181  -54.705  1.00 30.16 ? 21  VAL F CG1 1 
ATOM   8598  C CG2 . VAL F 1 21  ? 29.420  55.132  -56.729  1.00 31.09 ? 21  VAL F CG2 1 
ATOM   8599  N N   . ALA F 1 22  ? 32.563  56.645  -55.228  1.00 30.82 ? 22  ALA F N   1 
ATOM   8600  C CA  . ALA F 1 22  ? 33.970  56.316  -55.442  1.00 30.66 ? 22  ALA F CA  1 
ATOM   8601  C C   . ALA F 1 22  ? 34.249  54.950  -54.808  1.00 29.23 ? 22  ALA F C   1 
ATOM   8602  O O   . ALA F 1 22  ? 33.971  54.765  -53.632  1.00 27.97 ? 22  ALA F O   1 
ATOM   8603  C CB  . ALA F 1 22  ? 34.863  57.389  -54.843  1.00 31.38 ? 22  ALA F CB  1 
ATOM   8604  N N   . PRO F 1 23  ? 34.748  53.982  -55.575  1.00 30.59 ? 23  PRO F N   1 
ATOM   8605  C CA  . PRO F 1 23  ? 34.994  54.128  -57.011  1.00 32.62 ? 23  PRO F CA  1 
ATOM   8606  C C   . PRO F 1 23  ? 33.684  54.257  -57.819  1.00 33.97 ? 23  PRO F C   1 
ATOM   8607  O O   . PRO F 1 23  ? 32.592  53.924  -57.305  1.00 31.31 ? 23  PRO F O   1 
ATOM   8608  C CB  . PRO F 1 23  ? 35.750  52.835  -57.366  1.00 31.75 ? 23  PRO F CB  1 
ATOM   8609  C CG  . PRO F 1 23  ? 35.369  51.843  -56.292  1.00 31.07 ? 23  PRO F CG  1 
ATOM   8610  C CD  . PRO F 1 23  ? 34.600  52.562  -55.208  1.00 31.34 ? 23  PRO F CD  1 
ATOM   8611  N N   . ILE F 1 24  ? 33.817  54.751  -59.058  1.00 35.42 ? 24  ILE F N   1 
ATOM   8612  C CA  . ILE F 1 24  ? 32.671  55.102  -59.933  1.00 34.90 ? 24  ILE F CA  1 
ATOM   8613  C C   . ILE F 1 24  ? 31.576  54.039  -60.004  1.00 34.12 ? 24  ILE F C   1 
ATOM   8614  O O   . ILE F 1 24  ? 30.400  54.391  -60.024  1.00 32.86 ? 24  ILE F O   1 
ATOM   8615  C CB  . ILE F 1 24  ? 33.129  55.491  -61.365  1.00 34.35 ? 24  ILE F CB  1 
ATOM   8616  C CG1 . ILE F 1 24  ? 31.945  55.937  -62.225  1.00 34.65 ? 24  ILE F CG1 1 
ATOM   8617  C CG2 . ILE F 1 24  ? 33.867  54.360  -62.055  1.00 34.86 ? 24  ILE F CG2 1 
ATOM   8618  C CD1 . ILE F 1 24  ? 32.370  56.596  -63.539  1.00 34.31 ? 24  ILE F CD1 1 
ATOM   8619  N N   . VAL F 1 25  ? 31.983  52.767  -60.021  1.00 34.22 ? 25  VAL F N   1 
ATOM   8620  C CA  . VAL F 1 25  ? 31.075  51.602  -59.993  1.00 33.67 ? 25  VAL F CA  1 
ATOM   8621  C C   . VAL F 1 25  ? 31.514  50.624  -58.890  1.00 31.56 ? 25  VAL F C   1 
ATOM   8622  O O   . VAL F 1 25  ? 32.703  50.558  -58.572  1.00 29.99 ? 25  VAL F O   1 
ATOM   8623  C CB  . VAL F 1 25  ? 31.069  50.846  -61.349  1.00 35.15 ? 25  VAL F CB  1 
ATOM   8624  C CG1 . VAL F 1 25  ? 30.629  51.767  -62.478  1.00 36.24 ? 25  VAL F CG1 1 
ATOM   8625  C CG2 . VAL F 1 25  ? 32.434  50.263  -61.691  1.00 34.92 ? 25  VAL F CG2 1 
ATOM   8626  N N   . PRO F 1 26  ? 30.601  49.861  -58.302  1.00 29.61 ? 26  PRO F N   1 
ATOM   8627  C CA  . PRO F 1 26  ? 29.167  49.889  -58.607  1.00 29.30 ? 26  PRO F CA  1 
ATOM   8628  C C   . PRO F 1 26  ? 28.425  51.013  -57.915  1.00 27.64 ? 26  PRO F C   1 
ATOM   8629  O O   . PRO F 1 26  ? 28.882  51.507  -56.895  1.00 29.90 ? 26  PRO F O   1 
ATOM   8630  C CB  . PRO F 1 26  ? 28.675  48.543  -58.067  1.00 29.37 ? 26  PRO F CB  1 
ATOM   8631  C CG  . PRO F 1 26  ? 29.618  48.214  -56.952  1.00 29.29 ? 26  PRO F CG  1 
ATOM   8632  C CD  . PRO F 1 26  ? 30.919  48.920  -57.218  1.00 28.71 ? 26  PRO F CD  1 
ATOM   8633  N N   . THR F 1 27  ? 27.291  51.410  -58.480  1.00 26.60 ? 27  THR F N   1 
ATOM   8634  C CA  . THR F 1 27  ? 26.425  52.442  -57.906  1.00 26.89 ? 27  THR F CA  1 
ATOM   8635  C C   . THR F 1 27  ? 25.110  51.819  -57.469  1.00 25.76 ? 27  THR F C   1 
ATOM   8636  O O   . THR F 1 27  ? 24.851  50.633  -57.706  1.00 25.72 ? 27  THR F O   1 
ATOM   8637  C CB  . THR F 1 27  ? 26.148  53.607  -58.911  1.00 28.41 ? 27  THR F CB  1 
ATOM   8638  O OG1 . THR F 1 27  ? 25.299  54.600  -58.309  1.00 29.34 ? 27  THR F OG1 1 
ATOM   8639  C CG2 . THR F 1 27  ? 25.479  53.096  -60.179  1.00 29.16 ? 27  THR F CG2 1 
ATOM   8640  N N   . THR F 1 28  ? 24.295  52.624  -56.802  1.00 26.60 ? 28  THR F N   1 
ATOM   8641  C CA  . THR F 1 28  ? 22.918  52.252  -56.502  1.00 26.80 ? 28  THR F CA  1 
ATOM   8642  C C   . THR F 1 28  ? 22.040  53.417  -56.941  1.00 26.55 ? 28  THR F C   1 
ATOM   8643  O O   . THR F 1 28  ? 22.518  54.553  -57.069  1.00 27.48 ? 28  THR F O   1 
ATOM   8644  C CB  . THR F 1 28  ? 22.678  51.937  -55.009  1.00 25.55 ? 28  THR F CB  1 
ATOM   8645  O OG1 . THR F 1 28  ? 22.698  53.153  -54.272  1.00 24.80 ? 28  THR F OG1 1 
ATOM   8646  C CG2 . THR F 1 28  ? 23.734  50.982  -54.455  1.00 25.73 ? 28  THR F CG2 1 
ATOM   8647  N N   . ARG F 1 29  ? 20.762  53.127  -57.168  1.00 25.34 ? 29  ARG F N   1 
ATOM   8648  C CA  . ARG F 1 29  ? 19.838  54.105  -57.713  1.00 24.79 ? 29  ARG F CA  1 
ATOM   8649  C C   . ARG F 1 29  ? 19.457  55.138  -56.664  1.00 24.33 ? 29  ARG F C   1 
ATOM   8650  O O   . ARG F 1 29  ? 19.113  54.789  -55.539  1.00 23.86 ? 29  ARG F O   1 
ATOM   8651  C CB  . ARG F 1 29  ? 18.574  53.416  -58.222  1.00 25.55 ? 29  ARG F CB  1 
ATOM   8652  C CG  . ARG F 1 29  ? 18.069  53.982  -59.536  1.00 26.45 ? 29  ARG F CG  1 
ATOM   8653  C CD  . ARG F 1 29  ? 16.585  54.240  -59.545  1.00 26.83 ? 29  ARG F CD  1 
ATOM   8654  N NE  . ARG F 1 29  ? 15.788  53.233  -60.254  1.00 27.44 ? 29  ARG F NE  1 
ATOM   8655  C CZ  . ARG F 1 29  ? 15.039  53.459  -61.336  1.00 26.87 ? 29  ARG F CZ  1 
ATOM   8656  N NH1 . ARG F 1 29  ? 14.994  54.659  -61.905  1.00 27.58 ? 29  ARG F NH1 1 
ATOM   8657  N NH2 . ARG F 1 29  ? 14.330  52.465  -61.864  1.00 26.37 ? 29  ARG F NH2 1 
ATOM   8658  N N   . HIS F 1 30  ? 19.516  56.415  -57.021  1.00 24.21 ? 30  HIS F N   1 
ATOM   8659  C CA  . HIS F 1 30  ? 19.004  57.461  -56.134  1.00 24.08 ? 30  HIS F CA  1 
ATOM   8660  C C   . HIS F 1 30  ? 17.625  57.032  -55.626  1.00 24.22 ? 30  HIS F C   1 
ATOM   8661  O O   . HIS F 1 30  ? 16.808  56.521  -56.398  1.00 25.43 ? 30  HIS F O   1 
ATOM   8662  C CB  . HIS F 1 30  ? 18.850  58.799  -56.868  1.00 24.55 ? 30  HIS F CB  1 
ATOM   8663  C CG  . HIS F 1 30  ? 20.102  59.621  -56.935  1.00 25.34 ? 30  HIS F CG  1 
ATOM   8664  N ND1 . HIS F 1 30  ? 20.665  60.210  -55.826  1.00 26.13 ? 30  HIS F ND1 1 
ATOM   8665  C CD2 . HIS F 1 30  ? 20.867  60.001  -57.988  1.00 26.02 ? 30  HIS F CD2 1 
ATOM   8666  C CE1 . HIS F 1 30  ? 21.738  60.891  -56.183  1.00 26.90 ? 30  HIS F CE1 1 
ATOM   8667  N NE2 . HIS F 1 30  ? 21.882  60.784  -57.492  1.00 27.57 ? 30  HIS F NE2 1 
ATOM   8668  N N   . PRO F 1 31  ? 17.350  57.232  -54.337  1.00 24.85 ? 31  PRO F N   1 
ATOM   8669  C CA  . PRO F 1 31  ? 15.966  57.048  -53.873  1.00 24.21 ? 31  PRO F CA  1 
ATOM   8670  C C   . PRO F 1 31  ? 15.009  57.877  -54.711  1.00 23.85 ? 31  PRO F C   1 
ATOM   8671  O O   . PRO F 1 31  ? 15.365  58.972  -55.145  1.00 23.95 ? 31  PRO F O   1 
ATOM   8672  C CB  . PRO F 1 31  ? 15.991  57.570  -52.433  1.00 24.65 ? 31  PRO F CB  1 
ATOM   8673  C CG  . PRO F 1 31  ? 17.425  57.510  -52.008  1.00 25.41 ? 31  PRO F CG  1 
ATOM   8674  C CD  . PRO F 1 31  ? 18.270  57.637  -53.253  1.00 25.68 ? 31  PRO F CD  1 
ATOM   8675  N N   . HIS F 1 32  ? 13.810  57.357  -54.939  1.00 24.42 ? 32  HIS F N   1 
ATOM   8676  C CA  . HIS F 1 32  ? 12.808  58.031  -55.778  1.00 24.59 ? 32  HIS F CA  1 
ATOM   8677  C C   . HIS F 1 32  ? 12.647  59.512  -55.411  1.00 24.45 ? 32  HIS F C   1 
ATOM   8678  O O   . HIS F 1 32  ? 12.584  60.379  -56.290  1.00 24.55 ? 32  HIS F O   1 
ATOM   8679  C CB  . HIS F 1 32  ? 11.460  57.299  -55.674  1.00 24.93 ? 32  HIS F CB  1 
ATOM   8680  C CG  . HIS F 1 32  ? 10.398  57.843  -56.580  1.00 25.53 ? 32  HIS F CG  1 
ATOM   8681  N ND1 . HIS F 1 32  ? 9.537   58.850  -56.195  1.00 25.62 ? 32  HIS F ND1 1 
ATOM   8682  C CD2 . HIS F 1 32  ? 10.046  57.513  -57.845  1.00 25.89 ? 32  HIS F CD2 1 
ATOM   8683  C CE1 . HIS F 1 32  ? 8.707   59.122  -57.185  1.00 25.64 ? 32  HIS F CE1 1 
ATOM   8684  N NE2 . HIS F 1 32  ? 8.997   58.328  -58.200  1.00 25.77 ? 32  HIS F NE2 1 
ATOM   8685  N N   . ALA F 1 33  ? 12.603  59.800  -54.110  1.00 24.57 ? 33  ALA F N   1 
ATOM   8686  C CA  . ALA F 1 33  ? 12.417  61.176  -53.640  1.00 25.65 ? 33  ALA F CA  1 
ATOM   8687  C C   . ALA F 1 33  ? 13.505  62.152  -54.144  1.00 26.76 ? 33  ALA F C   1 
ATOM   8688  O O   . ALA F 1 33  ? 13.247  63.343  -54.273  1.00 25.95 ? 33  ALA F O   1 
ATOM   8689  C CB  . ALA F 1 33  ? 12.339  61.200  -52.130  1.00 25.90 ? 33  ALA F CB  1 
ATOM   8690  N N   . ASP F 1 34  ? 14.696  61.635  -54.444  1.00 28.37 ? 34  ASP F N   1 
ATOM   8691  C CA  . ASP F 1 34  ? 15.840  62.444  -54.867  1.00 28.92 ? 34  ASP F CA  1 
ATOM   8692  C C   . ASP F 1 34  ? 16.095  62.491  -56.382  1.00 29.87 ? 34  ASP F C   1 
ATOM   8693  O O   . ASP F 1 34  ? 17.089  63.098  -56.818  1.00 31.42 ? 34  ASP F O   1 
ATOM   8694  C CB  . ASP F 1 34  ? 17.116  61.897  -54.218  1.00 29.89 ? 34  ASP F CB  1 
ATOM   8695  C CG  . ASP F 1 34  ? 17.091  61.965  -52.711  1.00 30.28 ? 34  ASP F CG  1 
ATOM   8696  O OD1 . ASP F 1 34  ? 16.414  62.867  -52.176  1.00 29.87 ? 34  ASP F OD1 1 
ATOM   8697  O OD2 . ASP F 1 34  ? 17.765  61.109  -52.082  1.00 29.45 ? 34  ASP F OD2 1 
ATOM   8698  N N   . ARG F 1 35  ? 15.239  61.857  -57.190  1.00 28.95 ? 35  ARG F N   1 
ATOM   8699  C CA  . ARG F 1 35  ? 15.450  61.831  -58.654  1.00 27.21 ? 35  ARG F CA  1 
ATOM   8700  C C   . ARG F 1 35  ? 14.922  63.104  -59.315  1.00 26.71 ? 35  ARG F C   1 
ATOM   8701  O O   . ARG F 1 35  ? 13.845  63.608  -58.934  1.00 28.23 ? 35  ARG F O   1 
ATOM   8702  C CB  . ARG F 1 35  ? 14.779  60.609  -59.272  1.00 26.27 ? 35  ARG F CB  1 
ATOM   8703  C CG  . ARG F 1 35  ? 15.381  59.287  -58.820  1.00 25.63 ? 35  ARG F CG  1 
ATOM   8704  C CD  . ARG F 1 35  ? 14.670  58.101  -59.442  1.00 25.15 ? 35  ARG F CD  1 
ATOM   8705  N NE  . ARG F 1 35  ? 14.772  56.934  -58.578  1.00 24.93 ? 35  ARG F NE  1 
ATOM   8706  C CZ  . ARG F 1 35  ? 13.935  55.891  -58.589  1.00 25.67 ? 35  ARG F CZ  1 
ATOM   8707  N NH1 . ARG F 1 35  ? 12.903  55.827  -59.431  1.00 26.52 ? 35  ARG F NH1 1 
ATOM   8708  N NH2 . ARG F 1 35  ? 14.122  54.892  -57.737  1.00 25.35 ? 35  ARG F NH2 1 
ATOM   8709  N N   . TRP F 1 36  ? 15.658  63.619  -60.302  1.00 25.14 ? 36  TRP F N   1 
ATOM   8710  C CA  . TRP F 1 36  ? 15.284  64.914  -60.917  1.00 24.08 ? 36  TRP F CA  1 
ATOM   8711  C C   . TRP F 1 36  ? 13.862  64.881  -61.500  1.00 23.11 ? 36  TRP F C   1 
ATOM   8712  O O   . TRP F 1 36  ? 13.095  65.821  -61.349  1.00 22.68 ? 36  TRP F O   1 
ATOM   8713  C CB  . TRP F 1 36  ? 16.337  65.386  -61.949  1.00 23.37 ? 36  TRP F CB  1 
ATOM   8714  C CG  . TRP F 1 36  ? 16.170  64.903  -63.366  1.00 22.91 ? 36  TRP F CG  1 
ATOM   8715  C CD1 . TRP F 1 36  ? 16.746  63.802  -63.937  1.00 22.92 ? 36  TRP F CD1 1 
ATOM   8716  C CD2 . TRP F 1 36  ? 15.410  65.534  -64.397  1.00 23.03 ? 36  TRP F CD2 1 
ATOM   8717  N NE1 . TRP F 1 36  ? 16.375  63.699  -65.255  1.00 22.78 ? 36  TRP F NE1 1 
ATOM   8718  C CE2 . TRP F 1 36  ? 15.549  64.750  -65.561  1.00 22.94 ? 36  TRP F CE2 1 
ATOM   8719  C CE3 . TRP F 1 36  ? 14.607  66.678  -64.443  1.00 22.91 ? 36  TRP F CE3 1 
ATOM   8720  C CZ2 . TRP F 1 36  ? 14.921  65.079  -66.760  1.00 23.27 ? 36  TRP F CZ2 1 
ATOM   8721  C CZ3 . TRP F 1 36  ? 13.987  67.008  -65.634  1.00 22.88 ? 36  TRP F CZ3 1 
ATOM   8722  C CH2 . TRP F 1 36  ? 14.148  66.211  -66.776  1.00 23.32 ? 36  TRP F CH2 1 
ATOM   8723  N N   . THR F 1 37  ? 13.522  63.765  -62.138  1.00 22.70 ? 37  THR F N   1 
ATOM   8724  C CA  . THR F 1 37  ? 12.193  63.536  -62.695  1.00 21.90 ? 37  THR F CA  1 
ATOM   8725  C C   . THR F 1 37  ? 11.110  63.575  -61.629  1.00 22.04 ? 37  THR F C   1 
ATOM   8726  O O   . THR F 1 37  ? 10.006  64.050  -61.888  1.00 21.87 ? 37  THR F O   1 
ATOM   8727  C CB  . THR F 1 37  ? 12.115  62.175  -63.419  1.00 21.31 ? 37  THR F CB  1 
ATOM   8728  O OG1 . THR F 1 37  ? 12.718  61.164  -62.604  1.00 20.99 ? 37  THR F OG1 1 
ATOM   8729  C CG2 . THR F 1 37  ? 12.828  62.229  -64.730  1.00 21.06 ? 37  THR F CG2 1 
ATOM   8730  N N   . THR F 1 38  ? 11.406  63.065  -60.438  1.00 22.91 ? 38  THR F N   1 
ATOM   8731  C CA  . THR F 1 38  ? 10.427  63.086  -59.354  1.00 23.30 ? 38  THR F CA  1 
ATOM   8732  C C   . THR F 1 38  ? 10.150  64.511  -58.896  1.00 23.24 ? 38  THR F C   1 
ATOM   8733  O O   . THR F 1 38  ? 8.986   64.895  -58.715  1.00 24.11 ? 38  THR F O   1 
ATOM   8734  C CB  . THR F 1 38  ? 10.891  62.227  -58.173  1.00 24.34 ? 38  THR F CB  1 
ATOM   8735  O OG1 . THR F 1 38  ? 10.955  60.854  -58.589  1.00 24.32 ? 38  THR F OG1 1 
ATOM   8736  C CG2 . THR F 1 38  ? 9.932   62.354  -56.995  1.00 24.83 ? 38  THR F CG2 1 
ATOM   8737  N N   . VAL F 1 39  ? 11.204  65.301  -58.739  1.00 23.09 ? 39  VAL F N   1 
ATOM   8738  C CA  . VAL F 1 39  ? 11.039  66.688  -58.344  1.00 23.40 ? 39  VAL F CA  1 
ATOM   8739  C C   . VAL F 1 39  ? 10.330  67.445  -59.452  1.00 23.34 ? 39  VAL F C   1 
ATOM   8740  O O   . VAL F 1 39  ? 9.455   68.238  -59.169  1.00 23.99 ? 39  VAL F O   1 
ATOM   8741  C CB  . VAL F 1 39  ? 12.395  67.349  -57.999  1.00 23.80 ? 39  VAL F CB  1 
ATOM   8742  C CG1 . VAL F 1 39  ? 12.221  68.846  -57.750  1.00 24.06 ? 39  VAL F CG1 1 
ATOM   8743  C CG2 . VAL F 1 39  ? 13.026  66.661  -56.794  1.00 23.49 ? 39  VAL F CG2 1 
ATOM   8744  N N   . LEU F 1 40  ? 10.693  67.192  -60.707  1.00 24.93 ? 40  LEU F N   1 
ATOM   8745  C CA  . LEU F 1 40  ? 9.932   67.711  -61.844  1.00 26.97 ? 40  LEU F CA  1 
ATOM   8746  C C   . LEU F 1 40  ? 8.424   67.444  -61.690  1.00 28.81 ? 40  LEU F C   1 
ATOM   8747  O O   . LEU F 1 40  ? 7.593   68.336  -61.927  1.00 30.44 ? 40  LEU F O   1 
ATOM   8748  C CB  . LEU F 1 40  ? 10.432  67.096  -63.162  1.00 26.93 ? 40  LEU F CB  1 
ATOM   8749  C CG  . LEU F 1 40  ? 9.548   67.320  -64.402  1.00 27.51 ? 40  LEU F CG  1 
ATOM   8750  C CD1 . LEU F 1 40  ? 9.518   68.792  -64.813  1.00 28.05 ? 40  LEU F CD1 1 
ATOM   8751  C CD2 . LEU F 1 40  ? 10.019  66.447  -65.552  1.00 27.42 ? 40  LEU F CD2 1 
ATOM   8752  N N   . GLY F 1 41  ? 8.080   66.215  -61.308  1.00 30.20 ? 41  GLY F N   1 
ATOM   8753  C CA  . GLY F 1 41  ? 6.687   65.815  -61.140  1.00 30.75 ? 41  GLY F CA  1 
ATOM   8754  C C   . GLY F 1 41  ? 5.982   66.570  -60.029  1.00 31.09 ? 41  GLY F C   1 
ATOM   8755  O O   . GLY F 1 41  ? 4.838   67.016  -60.197  1.00 28.56 ? 41  GLY F O   1 
ATOM   8756  N N   . GLU F 1 42  ? 6.680   66.711  -58.899  1.00 31.97 ? 42  GLU F N   1 
ATOM   8757  C CA  . GLU F 1 42  ? 6.140   67.401  -57.730  1.00 31.99 ? 42  GLU F CA  1 
ATOM   8758  C C   . GLU F 1 42  ? 5.899   68.874  -57.983  1.00 31.46 ? 42  GLU F C   1 
ATOM   8759  O O   . GLU F 1 42  ? 4.861   69.392  -57.588  1.00 30.03 ? 42  GLU F O   1 
ATOM   8760  C CB  . GLU F 1 42  ? 7.059   67.241  -56.531  1.00 32.63 ? 42  GLU F CB  1 
ATOM   8761  C CG  . GLU F 1 42  ? 6.753   65.997  -55.704  1.00 33.54 ? 42  GLU F CG  1 
ATOM   8762  C CD  . GLU F 1 42  ? 7.968   65.488  -54.921  1.00 34.57 ? 42  GLU F CD  1 
ATOM   8763  O OE1 . GLU F 1 42  ? 7.906   64.302  -54.503  1.00 35.09 ? 42  GLU F OE1 1 
ATOM   8764  O OE2 . GLU F 1 42  ? 8.976   66.248  -54.738  1.00 31.99 ? 42  GLU F OE2 1 
ATOM   8765  N N   . ASN F 1 43  ? 6.845   69.532  -58.649  1.00 31.48 ? 43  ASN F N   1 
ATOM   8766  C CA  . ASN F 1 43  ? 6.702   70.939  -58.979  1.00 32.87 ? 43  ASN F CA  1 
ATOM   8767  C C   . ASN F 1 43  ? 5.653   71.228  -60.045  1.00 33.39 ? 43  ASN F C   1 
ATOM   8768  O O   . ASN F 1 43  ? 5.205   72.370  -60.160  1.00 33.40 ? 43  ASN F O   1 
ATOM   8769  C CB  . ASN F 1 43  ? 8.028   71.526  -59.448  1.00 34.04 ? 43  ASN F CB  1 
ATOM   8770  C CG  . ASN F 1 43  ? 8.928   71.921  -58.305  1.00 36.06 ? 43  ASN F CG  1 
ATOM   8771  O OD1 . ASN F 1 43  ? 8.986   73.078  -57.946  1.00 41.27 ? 43  ASN F OD1 1 
ATOM   8772  N ND2 . ASN F 1 43  ? 9.636   70.971  -57.736  1.00 36.56 ? 43  ASN F ND2 1 
ATOM   8773  N N   . LEU F 1 44  ? 5.283   70.217  -60.831  1.00 33.59 ? 44  LEU F N   1 
ATOM   8774  C CA  . LEU F 1 44  ? 4.256   70.382  -61.870  1.00 32.97 ? 44  LEU F CA  1 
ATOM   8775  C C   . LEU F 1 44  ? 2.848   70.290  -61.303  1.00 33.37 ? 44  LEU F C   1 
ATOM   8776  O O   . LEU F 1 44  ? 1.952   70.980  -61.766  1.00 34.02 ? 44  LEU F O   1 
ATOM   8777  C CB  . LEU F 1 44  ? 4.432   69.345  -62.999  1.00 32.91 ? 44  LEU F CB  1 
ATOM   8778  C CG  . LEU F 1 44  ? 5.482   69.665  -64.073  1.00 32.73 ? 44  LEU F CG  1 
ATOM   8779  C CD1 . LEU F 1 44  ? 5.693   68.463  -64.988  1.00 32.45 ? 44  LEU F CD1 1 
ATOM   8780  C CD2 . LEU F 1 44  ? 5.067   70.889  -64.873  1.00 32.60 ? 44  LEU F CD2 1 
ATOM   8781  N N   . GLY F 1 45  ? 2.662   69.420  -60.313  1.00 35.54 ? 45  GLY F N   1 
ATOM   8782  C CA  . GLY F 1 45  ? 1.377   69.263  -59.640  1.00 35.48 ? 45  GLY F CA  1 
ATOM   8783  C C   . GLY F 1 45  ? 0.519   68.160  -60.204  1.00 36.83 ? 45  GLY F C   1 
ATOM   8784  O O   . GLY F 1 45  ? 0.934   67.412  -61.077  1.00 35.03 ? 45  GLY F O   1 
ATOM   8785  N N   . ASP F 1 46  ? -0.703  68.067  -59.683  1.00 40.55 ? 46  ASP F N   1 
ATOM   8786  C CA  . ASP F 1 46  ? -1.686  67.036  -60.074  1.00 39.63 ? 46  ASP F CA  1 
ATOM   8787  C C   . ASP F 1 46  ? -2.157  67.181  -61.524  1.00 37.34 ? 46  ASP F C   1 
ATOM   8788  O O   . ASP F 1 46  ? -2.726  66.249  -62.082  1.00 33.71 ? 46  ASP F O   1 
ATOM   8789  C CB  . ASP F 1 46  ? -2.932  67.121  -59.181  1.00 41.83 ? 46  ASP F CB  1 
ATOM   8790  C CG  . ASP F 1 46  ? -2.647  66.855  -57.712  1.00 44.38 ? 46  ASP F CG  1 
ATOM   8791  O OD1 . ASP F 1 46  ? -1.480  66.939  -57.262  1.00 44.69 ? 46  ASP F OD1 1 
ATOM   8792  O OD2 . ASP F 1 46  ? -3.626  66.570  -56.997  1.00 45.41 ? 46  ASP F OD2 1 
ATOM   8793  N N   . GLY F 1 47  ? -1.941  68.356  -62.123  1.00 37.47 ? 47  GLY F N   1 
ATOM   8794  C CA  . GLY F 1 47  ? -2.268  68.579  -63.522  1.00 37.77 ? 47  GLY F CA  1 
ATOM   8795  C C   . GLY F 1 47  ? -1.470  67.714  -64.477  1.00 37.52 ? 47  GLY F C   1 
ATOM   8796  O O   . GLY F 1 47  ? -1.868  67.541  -65.624  1.00 34.48 ? 47  GLY F O   1 
ATOM   8797  N N   . TYR F 1 48  ? -0.352  67.167  -63.997  1.00 39.03 ? 48  TYR F N   1 
ATOM   8798  C CA  . TYR F 1 48  ? 0.589   66.402  -64.812  1.00 37.83 ? 48  TYR F CA  1 
ATOM   8799  C C   . TYR F 1 48  ? 0.889   65.013  -64.226  1.00 36.17 ? 48  TYR F C   1 
ATOM   8800  O O   . TYR F 1 48  ? 0.773   64.787  -63.023  1.00 33.53 ? 48  TYR F O   1 
ATOM   8801  C CB  . TYR F 1 48  ? 1.890   67.188  -64.977  1.00 38.00 ? 48  TYR F CB  1 
ATOM   8802  C CG  . TYR F 1 48  ? 1.710   68.572  -65.590  1.00 38.65 ? 48  TYR F CG  1 
ATOM   8803  C CD1 . TYR F 1 48  ? 1.225   69.632  -64.845  1.00 40.02 ? 48  TYR F CD1 1 
ATOM   8804  C CD2 . TYR F 1 48  ? 2.044   68.811  -66.916  1.00 39.36 ? 48  TYR F CD2 1 
ATOM   8805  C CE1 . TYR F 1 48  ? 1.067   70.891  -65.396  1.00 39.92 ? 48  TYR F CE1 1 
ATOM   8806  C CE2 . TYR F 1 48  ? 1.911   70.062  -67.484  1.00 39.53 ? 48  TYR F CE2 1 
ATOM   8807  C CZ  . TYR F 1 48  ? 1.409   71.105  -66.713  1.00 40.16 ? 48  TYR F CZ  1 
ATOM   8808  O OH  . TYR F 1 48  ? 1.280   72.377  -67.221  1.00 41.18 ? 48  TYR F OH  1 
ATOM   8809  N N   . GLU F 1 49  ? 1.290   64.106  -65.110  1.00 35.12 ? 49  GLU F N   1 
ATOM   8810  C CA  . GLU F 1 49  ? 1.575   62.712  -64.791  1.00 34.55 ? 49  GLU F CA  1 
ATOM   8811  C C   . GLU F 1 49  ? 2.802   62.290  -65.621  1.00 32.58 ? 49  GLU F C   1 
ATOM   8812  O O   . GLU F 1 49  ? 2.787   62.408  -66.847  1.00 33.48 ? 49  GLU F O   1 
ATOM   8813  C CB  . GLU F 1 49  ? 0.346   61.854  -65.162  1.00 37.41 ? 49  GLU F CB  1 
ATOM   8814  C CG  . GLU F 1 49  ? 0.490   60.352  -64.931  1.00 40.31 ? 49  GLU F CG  1 
ATOM   8815  C CD  . GLU F 1 49  ? -0.389  59.467  -65.824  1.00 42.17 ? 49  GLU F CD  1 
ATOM   8816  O OE1 . GLU F 1 49  ? 0.001   58.297  -65.977  1.00 42.37 ? 49  GLU F OE1 1 
ATOM   8817  O OE2 . GLU F 1 49  ? -1.449  59.927  -66.324  1.00 42.96 ? 49  GLU F OE2 1 
ATOM   8818  N N   . LEU F 1 50  ? 3.869   61.819  -64.971  1.00 29.38 ? 50  LEU F N   1 
ATOM   8819  C CA  . LEU F 1 50  ? 5.101   61.478  -65.682  1.00 27.50 ? 50  LEU F CA  1 
ATOM   8820  C C   . LEU F 1 50  ? 5.273   59.992  -66.000  1.00 25.90 ? 50  LEU F C   1 
ATOM   8821  O O   . LEU F 1 50  ? 4.842   59.138  -65.246  1.00 24.27 ? 50  LEU F O   1 
ATOM   8822  C CB  . LEU F 1 50  ? 6.313   61.901  -64.871  1.00 28.01 ? 50  LEU F CB  1 
ATOM   8823  C CG  . LEU F 1 50  ? 6.520   63.380  -64.584  1.00 28.60 ? 50  LEU F CG  1 
ATOM   8824  C CD1 . LEU F 1 50  ? 7.877   63.558  -63.947  1.00 29.36 ? 50  LEU F CD1 1 
ATOM   8825  C CD2 . LEU F 1 50  ? 6.454   64.226  -65.827  1.00 28.92 ? 50  LEU F CD2 1 
ATOM   8826  N N   . VAL F 1 51  ? 5.920   59.709  -67.131  1.00 24.70 ? 51  VAL F N   1 
ATOM   8827  C CA  . VAL F 1 51  ? 6.422   58.380  -67.461  1.00 23.72 ? 51  VAL F CA  1 
ATOM   8828  C C   . VAL F 1 51  ? 7.913   58.543  -67.741  1.00 23.68 ? 51  VAL F C   1 
ATOM   8829  O O   . VAL F 1 51  ? 8.301   59.411  -68.521  1.00 25.08 ? 51  VAL F O   1 
ATOM   8830  C CB  . VAL F 1 51  ? 5.740   57.809  -68.708  1.00 23.27 ? 51  VAL F CB  1 
ATOM   8831  C CG1 . VAL F 1 51  ? 6.115   56.339  -68.914  1.00 22.91 ? 51  VAL F CG1 1 
ATOM   8832  C CG2 . VAL F 1 51  ? 4.235   57.958  -68.597  1.00 23.31 ? 51  VAL F CG2 1 
ATOM   8833  N N   . VAL F 1 52  ? 8.748   57.728  -67.108  1.00 23.38 ? 52  VAL F N   1 
ATOM   8834  C CA  . VAL F 1 52  ? 10.188  57.962  -67.133  1.00 23.46 ? 52  VAL F CA  1 
ATOM   8835  C C   . VAL F 1 52  ? 10.956  56.750  -67.655  1.00 23.18 ? 52  VAL F C   1 
ATOM   8836  O O   . VAL F 1 52  ? 10.772  55.632  -67.178  1.00 22.79 ? 52  VAL F O   1 
ATOM   8837  C CB  . VAL F 1 52  ? 10.716  58.330  -65.729  1.00 23.19 ? 52  VAL F CB  1 
ATOM   8838  C CG1 . VAL F 1 52  ? 12.195  58.645  -65.776  1.00 22.96 ? 52  VAL F CG1 1 
ATOM   8839  C CG2 . VAL F 1 52  ? 9.960   59.521  -65.186  1.00 23.07 ? 52  VAL F CG2 1 
ATOM   8840  N N   . ASP F 1 53  ? 11.836  56.989  -68.625  1.00 22.51 ? 53  ASP F N   1 
ATOM   8841  C CA  . ASP F 1 53  ? 12.657  55.920  -69.168  1.00 22.82 ? 53  ASP F CA  1 
ATOM   8842  C C   . ASP F 1 53  ? 14.104  56.349  -69.252  1.00 22.41 ? 53  ASP F C   1 
ATOM   8843  O O   . ASP F 1 53  ? 14.532  56.915  -70.252  1.00 23.18 ? 53  ASP F O   1 
ATOM   8844  C CB  . ASP F 1 53  ? 12.150  55.487  -70.541  1.00 23.31 ? 53  ASP F CB  1 
ATOM   8845  C CG  . ASP F 1 53  ? 12.553  54.078  -70.888  1.00 24.08 ? 53  ASP F CG  1 
ATOM   8846  O OD1 . ASP F 1 53  ? 13.766  53.806  -71.039  1.00 23.16 ? 53  ASP F OD1 1 
ATOM   8847  O OD2 . ASP F 1 53  ? 11.637  53.237  -70.995  1.00 25.64 ? 53  ASP F OD2 1 
ATOM   8848  N N   . GLY F 1 54  ? 14.850  56.061  -68.189  1.00 21.55 ? 54  GLY F N   1 
ATOM   8849  C CA  . GLY F 1 54  ? 16.269  56.383  -68.116  1.00 21.00 ? 54  GLY F CA  1 
ATOM   8850  C C   . GLY F 1 54  ? 17.111  55.125  -68.107  1.00 20.78 ? 54  GLY F C   1 
ATOM   8851  O O   . GLY F 1 54  ? 16.962  54.284  -67.212  1.00 21.15 ? 54  GLY F O   1 
ATOM   8852  N N   . LEU F 1 55  ? 17.999  55.002  -69.103  1.00 20.48 ? 55  LEU F N   1 
ATOM   8853  C CA  . LEU F 1 55  ? 18.892  53.847  -69.235  1.00 19.62 ? 55  LEU F CA  1 
ATOM   8854  C C   . LEU F 1 55  ? 20.347  54.261  -69.101  1.00 19.29 ? 55  LEU F C   1 
ATOM   8855  O O   . LEU F 1 55  ? 20.848  55.020  -69.918  1.00 18.42 ? 55  LEU F O   1 
ATOM   8856  C CB  . LEU F 1 55  ? 18.694  53.168  -70.597  1.00 19.42 ? 55  LEU F CB  1 
ATOM   8857  C CG  . LEU F 1 55  ? 19.642  51.997  -70.949  1.00 19.11 ? 55  LEU F CG  1 
ATOM   8858  C CD1 . LEU F 1 55  ? 19.522  50.880  -69.934  1.00 19.07 ? 55  LEU F CD1 1 
ATOM   8859  C CD2 . LEU F 1 55  ? 19.377  51.447  -72.336  1.00 18.90 ? 55  LEU F CD2 1 
ATOM   8860  N N   . SER F 1 56  ? 21.022  53.740  -68.079  1.00 19.52 ? 56  SER F N   1 
ATOM   8861  C CA  . SER F 1 56  ? 22.456  53.959  -67.923  1.00 19.96 ? 56  SER F CA  1 
ATOM   8862  C C   . SER F 1 56  ? 23.160  53.580  -69.222  1.00 20.12 ? 56  SER F C   1 
ATOM   8863  O O   . SER F 1 56  ? 22.911  52.524  -69.783  1.00 19.32 ? 56  SER F O   1 
ATOM   8864  C CB  . SER F 1 56  ? 23.026  53.139  -66.757  1.00 20.02 ? 56  SER F CB  1 
ATOM   8865  O OG  . SER F 1 56  ? 22.292  53.339  -65.550  1.00 21.30 ? 56  SER F OG  1 
ATOM   8866  N N   . GLY F 1 57  ? 24.003  54.475  -69.715  1.00 21.13 ? 57  GLY F N   1 
ATOM   8867  C CA  . GLY F 1 57  ? 24.827  54.211  -70.901  1.00 21.52 ? 57  GLY F CA  1 
ATOM   8868  C C   . GLY F 1 57  ? 24.245  54.623  -72.245  1.00 21.36 ? 57  GLY F C   1 
ATOM   8869  O O   . GLY F 1 57  ? 24.929  54.548  -73.257  1.00 20.72 ? 57  GLY F O   1 
ATOM   8870  N N   . ARG F 1 58  ? 23.001  55.095  -72.243  1.00 21.95 ? 58  ARG F N   1 
ATOM   8871  C CA  . ARG F 1 58  ? 22.234  55.331  -73.475  1.00 21.30 ? 58  ARG F CA  1 
ATOM   8872  C C   . ARG F 1 58  ? 22.707  56.536  -74.294  1.00 19.74 ? 58  ARG F C   1 
ATOM   8873  O O   . ARG F 1 58  ? 22.990  57.618  -73.750  1.00 20.44 ? 58  ARG F O   1 
ATOM   8874  C CB  . ARG F 1 58  ? 20.740  55.469  -73.145  1.00 22.14 ? 58  ARG F CB  1 
ATOM   8875  C CG  . ARG F 1 58  ? 19.819  55.757  -74.327  1.00 23.09 ? 58  ARG F CG  1 
ATOM   8876  C CD  . ARG F 1 58  ? 18.357  55.905  -73.875  1.00 23.07 ? 58  ARG F CD  1 
ATOM   8877  N NE  . ARG F 1 58  ? 17.656  54.624  -73.784  1.00 23.63 ? 58  ARG F NE  1 
ATOM   8878  C CZ  . ARG F 1 58  ? 16.558  54.396  -73.060  1.00 24.00 ? 58  ARG F CZ  1 
ATOM   8879  N NH1 . ARG F 1 58  ? 16.018  55.351  -72.313  1.00 24.04 ? 58  ARG F NH1 1 
ATOM   8880  N NH2 . ARG F 1 58  ? 15.996  53.194  -73.072  1.00 23.80 ? 58  ARG F NH2 1 
ATOM   8881  N N   . THR F 1 59  ? 22.761  56.330  -75.609  1.00 17.94 ? 59  THR F N   1 
ATOM   8882  C CA  . THR F 1 59  ? 23.153  57.354  -76.562  1.00 17.07 ? 59  THR F CA  1 
ATOM   8883  C C   . THR F 1 59  ? 21.924  57.868  -77.296  1.00 16.82 ? 59  THR F C   1 
ATOM   8884  O O   . THR F 1 59  ? 20.842  57.297  -77.177  1.00 17.75 ? 59  THR F O   1 
ATOM   8885  C CB  . THR F 1 59  ? 24.119  56.794  -77.614  1.00 16.47 ? 59  THR F CB  1 
ATOM   8886  O OG1 . THR F 1 59  ? 23.408  55.970  -78.549  1.00 15.54 ? 59  THR F OG1 1 
ATOM   8887  C CG2 . THR F 1 59  ? 25.223  56.007  -76.951  1.00 16.32 ? 59  THR F CG2 1 
ATOM   8888  N N   . THR F 1 60  ? 22.101  58.933  -78.070  1.00 16.03 ? 60  THR F N   1 
ATOM   8889  C CA  . THR F 1 60  ? 21.040  59.427  -78.931  1.00 15.62 ? 60  THR F CA  1 
ATOM   8890  C C   . THR F 1 60  ? 20.627  58.373  -79.953  1.00 14.94 ? 60  THR F C   1 
ATOM   8891  O O   . THR F 1 60  ? 19.508  57.855  -79.900  1.00 14.47 ? 60  THR F O   1 
ATOM   8892  C CB  . THR F 1 60  ? 21.458  60.701  -79.698  1.00 15.72 ? 60  THR F CB  1 
ATOM   8893  O OG1 . THR F 1 60  ? 22.703  60.477  -80.374  1.00 15.48 ? 60  THR F OG1 1 
ATOM   8894  C CG2 . THR F 1 60  ? 21.589  61.877  -78.756  1.00 15.60 ? 60  THR F CG2 1 
ATOM   8895  N N   . ASN F 1 61  ? 21.541  58.044  -80.866  1.00 14.46 ? 61  ASN F N   1 
ATOM   8896  C CA  . ASN F 1 61  ? 21.200  57.236  -82.041  1.00 13.91 ? 61  ASN F CA  1 
ATOM   8897  C C   . ASN F 1 61  ? 22.337  56.390  -82.616  1.00 13.41 ? 61  ASN F C   1 
ATOM   8898  O O   . ASN F 1 61  ? 22.332  56.085  -83.800  1.00 12.64 ? 61  ASN F O   1 
ATOM   8899  C CB  . ASN F 1 61  ? 20.694  58.176  -83.137  1.00 13.90 ? 61  ASN F CB  1 
ATOM   8900  C CG  . ASN F 1 61  ? 21.824  58.890  -83.858  1.00 13.62 ? 61  ASN F CG  1 
ATOM   8901  O OD1 . ASN F 1 61  ? 22.892  59.122  -83.306  1.00 14.03 ? 61  ASN F OD1 1 
ATOM   8902  N ND2 . ASN F 1 61  ? 21.592  59.237  -85.089  1.00 13.22 ? 61  ASN F ND2 1 
ATOM   8903  N N   . ILE F 1 62  ? 23.299  56.011  -81.779  1.00 13.54 ? 62  ILE F N   1 
ATOM   8904  C CA  . ILE F 1 62  ? 24.491  55.299  -82.242  1.00 13.34 ? 62  ILE F CA  1 
ATOM   8905  C C   . ILE F 1 62  ? 24.742  54.054  -81.395  1.00 13.59 ? 62  ILE F C   1 
ATOM   8906  O O   . ILE F 1 62  ? 24.586  54.086  -80.171  1.00 13.04 ? 62  ILE F O   1 
ATOM   8907  C CB  . ILE F 1 62  ? 25.723  56.209  -82.195  1.00 13.18 ? 62  ILE F CB  1 
ATOM   8908  C CG1 . ILE F 1 62  ? 26.930  55.526  -82.827  1.00 13.09 ? 62  ILE F CG1 1 
ATOM   8909  C CG2 . ILE F 1 62  ? 26.037  56.625  -80.755  1.00 13.49 ? 62  ILE F CG2 1 
ATOM   8910  C CD1 . ILE F 1 62  ? 28.087  56.465  -83.058  1.00 13.07 ? 62  ILE F CD1 1 
ATOM   8911  N N   . ASP F 1 63  ? 25.130  52.960  -82.055  1.00 14.10 ? 63  ASP F N   1 
ATOM   8912  C CA  . ASP F 1 63  ? 25.472  51.713  -81.357  1.00 14.67 ? 63  ASP F CA  1 
ATOM   8913  C C   . ASP F 1 63  ? 26.743  51.852  -80.529  1.00 15.67 ? 63  ASP F C   1 
ATOM   8914  O O   . ASP F 1 63  ? 27.731  52.419  -80.980  1.00 15.52 ? 63  ASP F O   1 
ATOM   8915  C CB  . ASP F 1 63  ? 25.674  50.559  -82.334  1.00 13.97 ? 63  ASP F CB  1 
ATOM   8916  C CG  . ASP F 1 63  ? 24.428  50.188  -83.055  1.00 13.61 ? 63  ASP F CG  1 
ATOM   8917  O OD1 . ASP F 1 63  ? 23.315  50.328  -82.490  1.00 14.39 ? 63  ASP F OD1 1 
ATOM   8918  O OD2 . ASP F 1 63  ? 24.556  49.740  -84.198  1.00 13.24 ? 63  ASP F OD2 1 
ATOM   8919  N N   . ASP F 1 64  ? 26.695  51.322  -79.313  1.00 17.13 ? 64  ASP F N   1 
ATOM   8920  C CA  . ASP F 1 64  ? 27.878  51.176  -78.491  1.00 18.67 ? 64  ASP F CA  1 
ATOM   8921  C C   . ASP F 1 64  ? 28.431  49.765  -78.747  1.00 20.42 ? 64  ASP F C   1 
ATOM   8922  O O   . ASP F 1 64  ? 27.752  48.759  -78.481  1.00 20.70 ? 64  ASP F O   1 
ATOM   8923  C CB  . ASP F 1 64  ? 27.542  51.392  -77.021  1.00 18.96 ? 64  ASP F CB  1 
ATOM   8924  C CG  . ASP F 1 64  ? 28.780  51.564  -76.161  1.00 19.77 ? 64  ASP F CG  1 
ATOM   8925  O OD1 . ASP F 1 64  ? 29.681  50.690  -76.234  1.00 20.15 ? 64  ASP F OD1 1 
ATOM   8926  O OD2 . ASP F 1 64  ? 28.858  52.596  -75.424  1.00 19.96 ? 64  ASP F OD2 1 
ATOM   8927  N N   . PRO F 1 65  ? 29.662  49.672  -79.292  1.00 21.85 ? 65  PRO F N   1 
ATOM   8928  C CA  . PRO F 1 65  ? 30.174  48.330  -79.595  1.00 21.76 ? 65  PRO F CA  1 
ATOM   8929  C C   . PRO F 1 65  ? 30.327  47.440  -78.352  1.00 21.93 ? 65  PRO F C   1 
ATOM   8930  O O   . PRO F 1 65  ? 30.443  46.226  -78.489  1.00 21.90 ? 65  PRO F O   1 
ATOM   8931  C CB  . PRO F 1 65  ? 31.519  48.606  -80.281  1.00 21.69 ? 65  PRO F CB  1 
ATOM   8932  C CG  . PRO F 1 65  ? 31.906  49.979  -79.863  1.00 22.01 ? 65  PRO F CG  1 
ATOM   8933  C CD  . PRO F 1 65  ? 30.616  50.726  -79.665  1.00 21.87 ? 65  PRO F CD  1 
ATOM   8934  N N   . ASN F 1 66  ? 30.297  48.036  -77.161  1.00 22.44 ? 66  ASN F N   1 
ATOM   8935  C CA  . ASN F 1 66  ? 30.396  47.279  -75.913  1.00 23.44 ? 66  ASN F CA  1 
ATOM   8936  C C   . ASN F 1 66  ? 29.080  46.716  -75.391  1.00 24.57 ? 66  ASN F C   1 
ATOM   8937  O O   . ASN F 1 66  ? 29.090  45.866  -74.517  1.00 25.59 ? 66  ASN F O   1 
ATOM   8938  C CB  . ASN F 1 66  ? 31.008  48.156  -74.824  1.00 23.80 ? 66  ASN F CB  1 
ATOM   8939  C CG  . ASN F 1 66  ? 32.394  48.623  -75.186  1.00 23.82 ? 66  ASN F CG  1 
ATOM   8940  O OD1 . ASN F 1 66  ? 33.335  47.827  -75.176  1.00 24.14 ? 66  ASN F OD1 1 
ATOM   8941  N ND2 . ASN F 1 66  ? 32.528  49.909  -75.539  1.00 23.83 ? 66  ASN F ND2 1 
ATOM   8942  N N   . ASP F 1 67  ? 27.949  47.199  -75.901  1.00 25.16 ? 67  ASP F N   1 
ATOM   8943  C CA  . ASP F 1 67  ? 26.635  46.817  -75.372  1.00 23.98 ? 67  ASP F CA  1 
ATOM   8944  C C   . ASP F 1 67  ? 25.540  47.156  -76.388  1.00 24.24 ? 67  ASP F C   1 
ATOM   8945  O O   . ASP F 1 67  ? 25.272  48.346  -76.677  1.00 24.78 ? 67  ASP F O   1 
ATOM   8946  C CB  . ASP F 1 67  ? 26.368  47.532  -74.045  1.00 23.16 ? 67  ASP F CB  1 
ATOM   8947  C CG  . ASP F 1 67  ? 25.160  46.974  -73.309  1.00 22.27 ? 67  ASP F CG  1 
ATOM   8948  O OD1 . ASP F 1 67  ? 24.346  46.230  -73.909  1.00 20.55 ? 67  ASP F OD1 1 
ATOM   8949  O OD2 . ASP F 1 67  ? 25.043  47.304  -72.109  1.00 22.18 ? 67  ASP F OD2 1 
ATOM   8950  N N   . PRO F 1 68  ? 24.886  46.122  -76.928  1.00 24.18 ? 68  PRO F N   1 
ATOM   8951  C CA  . PRO F 1 68  ? 23.904  46.390  -77.974  1.00 23.50 ? 68  PRO F CA  1 
ATOM   8952  C C   . PRO F 1 68  ? 22.585  47.023  -77.519  1.00 23.15 ? 68  PRO F C   1 
ATOM   8953  O O   . PRO F 1 68  ? 21.764  47.301  -78.359  1.00 26.07 ? 68  PRO F O   1 
ATOM   8954  C CB  . PRO F 1 68  ? 23.659  45.017  -78.609  1.00 23.55 ? 68  PRO F CB  1 
ATOM   8955  C CG  . PRO F 1 68  ? 24.187  44.003  -77.656  1.00 24.03 ? 68  PRO F CG  1 
ATOM   8956  C CD  . PRO F 1 68  ? 25.076  44.683  -76.657  1.00 24.22 ? 68  PRO F CD  1 
ATOM   8957  N N   . LYS F 1 69  ? 22.369  47.280  -76.235  1.00 22.51 ? 69  LYS F N   1 
ATOM   8958  C CA  . LYS F 1 69  ? 21.074  47.846  -75.801  1.00 22.17 ? 69  LYS F CA  1 
ATOM   8959  C C   . LYS F 1 69  ? 21.056  49.347  -75.531  1.00 21.60 ? 69  LYS F C   1 
ATOM   8960  O O   . LYS F 1 69  ? 20.070  49.856  -75.009  1.00 21.48 ? 69  LYS F O   1 
ATOM   8961  C CB  . LYS F 1 69  ? 20.557  47.105  -74.550  1.00 22.35 ? 69  LYS F CB  1 
ATOM   8962  C CG  . LYS F 1 69  ? 21.306  47.388  -73.251  1.00 22.14 ? 69  LYS F CG  1 
ATOM   8963  C CD  . LYS F 1 69  ? 20.772  46.550  -72.116  1.00 22.37 ? 69  LYS F CD  1 
ATOM   8964  C CE  . LYS F 1 69  ? 21.511  46.771  -70.807  1.00 22.84 ? 69  LYS F CE  1 
ATOM   8965  N NZ  . LYS F 1 69  ? 22.819  46.061  -70.743  1.00 22.82 ? 69  LYS F NZ  1 
ATOM   8966  N N   . LEU F 1 70  ? 22.123  50.056  -75.902  1.00 21.47 ? 70  LEU F N   1 
ATOM   8967  C CA  . LEU F 1 70  ? 22.320  51.452  -75.473  1.00 20.00 ? 70  LEU F CA  1 
ATOM   8968  C C   . LEU F 1 70  ? 21.944  52.505  -76.511  1.00 18.86 ? 70  LEU F C   1 
ATOM   8969  O O   . LEU F 1 70  ? 22.169  53.689  -76.292  1.00 18.90 ? 70  LEU F O   1 
ATOM   8970  C CB  . LEU F 1 70  ? 23.784  51.638  -75.084  1.00 20.18 ? 70  LEU F CB  1 
ATOM   8971  C CG  . LEU F 1 70  ? 24.284  50.739  -73.956  1.00 20.01 ? 70  LEU F CG  1 
ATOM   8972  C CD1 . LEU F 1 70  ? 25.726  51.085  -73.603  1.00 19.41 ? 70  LEU F CD1 1 
ATOM   8973  C CD2 . LEU F 1 70  ? 23.374  50.878  -72.740  1.00 20.13 ? 70  LEU F CD2 1 
ATOM   8974  N N   . ASN F 1 71  ? 21.378  52.093  -77.640  1.00 17.83 ? 71  ASN F N   1 
ATOM   8975  C CA  . ASN F 1 71  ? 21.039  53.028  -78.686  1.00 17.56 ? 71  ASN F CA  1 
ATOM   8976  C C   . ASN F 1 71  ? 19.615  53.541  -78.499  1.00 17.56 ? 71  ASN F C   1 
ATOM   8977  O O   . ASN F 1 71  ? 18.654  52.807  -78.737  1.00 18.32 ? 71  ASN F O   1 
ATOM   8978  C CB  . ASN F 1 71  ? 21.182  52.353  -80.035  1.00 17.42 ? 71  ASN F CB  1 
ATOM   8979  C CG  . ASN F 1 71  ? 21.100  53.329  -81.191  1.00 17.26 ? 71  ASN F CG  1 
ATOM   8980  O OD1 . ASN F 1 71  ? 20.313  54.289  -81.170  1.00 16.88 ? 71  ASN F OD1 1 
ATOM   8981  N ND2 . ASN F 1 71  ? 21.911  53.085  -82.213  1.00 16.93 ? 71  ASN F ND2 1 
ATOM   8982  N N   . GLY F 1 72  ? 19.481  54.801  -78.083  1.00 16.77 ? 72  GLY F N   1 
ATOM   8983  C CA  . GLY F 1 72  ? 18.167  55.409  -77.851  1.00 16.36 ? 72  GLY F CA  1 
ATOM   8984  C C   . GLY F 1 72  ? 17.174  55.215  -78.989  1.00 15.90 ? 72  GLY F C   1 
ATOM   8985  O O   . GLY F 1 72  ? 16.006  54.909  -78.762  1.00 16.02 ? 72  GLY F O   1 
ATOM   8986  N N   . ALA F 1 73  ? 17.656  55.376  -80.216  1.00 15.36 ? 73  ALA F N   1 
ATOM   8987  C CA  . ALA F 1 73  ? 16.814  55.321  -81.397  1.00 14.74 ? 73  ALA F CA  1 
ATOM   8988  C C   . ALA F 1 73  ? 16.329  53.895  -81.738  1.00 14.33 ? 73  ALA F C   1 
ATOM   8989  O O   . ALA F 1 73  ? 15.308  53.731  -82.416  1.00 13.20 ? 73  ALA F O   1 
ATOM   8990  C CB  . ALA F 1 73  ? 17.562  55.935  -82.569  1.00 14.94 ? 73  ALA F CB  1 
ATOM   8991  N N   . ASP F 1 74  ? 17.055  52.873  -81.277  1.00 14.30 ? 74  ASP F N   1 
ATOM   8992  C CA  . ASP F 1 74  ? 16.542  51.495  -81.338  1.00 14.15 ? 74  ASP F CA  1 
ATOM   8993  C C   . ASP F 1 74  ? 15.273  51.322  -80.514  1.00 13.97 ? 74  ASP F C   1 
ATOM   8994  O O   . ASP F 1 74  ? 14.441  50.518  -80.858  1.00 14.12 ? 74  ASP F O   1 
ATOM   8995  C CB  . ASP F 1 74  ? 17.578  50.474  -80.816  1.00 14.35 ? 74  ASP F CB  1 
ATOM   8996  C CG  . ASP F 1 74  ? 18.701  50.191  -81.801  1.00 14.40 ? 74  ASP F CG  1 
ATOM   8997  O OD1 . ASP F 1 74  ? 18.504  50.463  -83.001  1.00 14.52 ? 74  ASP F OD1 1 
ATOM   8998  O OD2 . ASP F 1 74  ? 19.752  49.651  -81.378  1.00 14.00 ? 74  ASP F OD2 1 
ATOM   8999  N N   . TYR F 1 75  ? 15.151  52.073  -79.424  1.00 14.07 ? 75  TYR F N   1 
ATOM   9000  C CA  . TYR F 1 75  ? 14.102  51.882  -78.408  1.00 14.10 ? 75  TYR F CA  1 
ATOM   9001  C C   . TYR F 1 75  ? 12.916  52.848  -78.537  1.00 13.65 ? 75  TYR F C   1 
ATOM   9002  O O   . TYR F 1 75  ? 11.774  52.488  -78.233  1.00 13.19 ? 75  TYR F O   1 
ATOM   9003  C CB  . TYR F 1 75  ? 14.788  52.100  -77.063  1.00 14.46 ? 75  TYR F CB  1 
ATOM   9004  C CG  . TYR F 1 75  ? 14.072  51.718  -75.775  1.00 14.63 ? 75  TYR F CG  1 
ATOM   9005  C CD1 . TYR F 1 75  ? 14.118  50.411  -75.268  1.00 14.44 ? 75  TYR F CD1 1 
ATOM   9006  C CD2 . TYR F 1 75  ? 13.486  52.696  -74.991  1.00 14.83 ? 75  TYR F CD2 1 
ATOM   9007  C CE1 . TYR F 1 75  ? 13.534  50.096  -74.054  1.00 14.38 ? 75  TYR F CE1 1 
ATOM   9008  C CE2 . TYR F 1 75  ? 12.884  52.387  -73.782  1.00 14.88 ? 75  TYR F CE2 1 
ATOM   9009  C CZ  . TYR F 1 75  ? 12.916  51.090  -73.306  1.00 14.42 ? 75  TYR F CZ  1 
ATOM   9010  O OH  . TYR F 1 75  ? 12.330  50.801  -72.094  1.00 13.80 ? 75  TYR F OH  1 
ATOM   9011  N N   . LEU F 1 76  ? 13.190  54.069  -78.978  1.00 13.54 ? 76  LEU F N   1 
ATOM   9012  C CA  . LEU F 1 76  ? 12.235  55.156  -78.835  1.00 13.84 ? 76  LEU F CA  1 
ATOM   9013  C C   . LEU F 1 76  ? 10.910  54.948  -79.581  1.00 14.42 ? 76  LEU F C   1 
ATOM   9014  O O   . LEU F 1 76  ? 9.857   55.231  -79.013  1.00 14.38 ? 76  LEU F O   1 
ATOM   9015  C CB  . LEU F 1 76  ? 12.867  56.508  -79.218  1.00 13.77 ? 76  LEU F CB  1 
ATOM   9016  C CG  . LEU F 1 76  ? 11.988  57.741  -78.974  1.00 13.49 ? 76  LEU F CG  1 
ATOM   9017  C CD1 . LEU F 1 76  ? 11.544  57.821  -77.521  1.00 13.73 ? 76  LEU F CD1 1 
ATOM   9018  C CD2 . LEU F 1 76  ? 12.721  59.012  -79.323  1.00 13.23 ? 76  LEU F CD2 1 
ATOM   9019  N N   . PRO F 1 77  ? 10.947  54.462  -80.841  1.00 15.26 ? 77  PRO F N   1 
ATOM   9020  C CA  . PRO F 1 77  ? 9.676   54.267  -81.541  1.00 15.65 ? 77  PRO F CA  1 
ATOM   9021  C C   . PRO F 1 77  ? 8.708   53.383  -80.754  1.00 16.65 ? 77  PRO F C   1 
ATOM   9022  O O   . PRO F 1 77  ? 7.528   53.728  -80.630  1.00 16.96 ? 77  PRO F O   1 
ATOM   9023  C CB  . PRO F 1 77  ? 10.106  53.598  -82.848  1.00 15.32 ? 77  PRO F CB  1 
ATOM   9024  C CG  . PRO F 1 77  ? 11.438  54.169  -83.113  1.00 15.11 ? 77  PRO F CG  1 
ATOM   9025  C CD  . PRO F 1 77  ? 12.086  54.234  -81.749  1.00 15.42 ? 77  PRO F CD  1 
ATOM   9026  N N   . ALA F 1 78  ? 9.210   52.268  -80.221  1.00 17.13 ? 78  ALA F N   1 
ATOM   9027  C CA  . ALA F 1 78  ? 8.387   51.361  -79.420  1.00 16.54 ? 78  ALA F CA  1 
ATOM   9028  C C   . ALA F 1 78  ? 7.888   52.043  -78.159  1.00 16.68 ? 78  ALA F C   1 
ATOM   9029  O O   . ALA F 1 78  ? 6.722   51.937  -77.807  1.00 16.91 ? 78  ALA F O   1 
ATOM   9030  C CB  . ALA F 1 78  ? 9.162   50.103  -79.059  1.00 16.29 ? 78  ALA F CB  1 
ATOM   9031  N N   . ALA F 1 79  ? 8.780   52.746  -77.475  1.00 17.12 ? 79  ALA F N   1 
ATOM   9032  C CA  . ALA F 1 79  ? 8.438   53.408  -76.224  1.00 16.89 ? 79  ALA F CA  1 
ATOM   9033  C C   . ALA F 1 79  ? 7.314   54.420  -76.434  1.00 17.18 ? 79  ALA F C   1 
ATOM   9034  O O   . ALA F 1 79  ? 6.356   54.464  -75.665  1.00 18.12 ? 79  ALA F O   1 
ATOM   9035  C CB  . ALA F 1 79  ? 9.667   54.080  -75.642  1.00 16.74 ? 79  ALA F CB  1 
ATOM   9036  N N   . LEU F 1 80  ? 7.423   55.220  -77.488  1.00 16.53 ? 80  LEU F N   1 
ATOM   9037  C CA  . LEU F 1 80  ? 6.423   56.245  -77.787  1.00 15.97 ? 80  LEU F CA  1 
ATOM   9038  C C   . LEU F 1 80  ? 5.030   55.651  -77.992  1.00 16.06 ? 80  LEU F C   1 
ATOM   9039  O O   . LEU F 1 80  ? 4.045   56.191  -77.489  1.00 16.55 ? 80  LEU F O   1 
ATOM   9040  C CB  . LEU F 1 80  ? 6.829   57.023  -79.025  1.00 15.72 ? 80  LEU F CB  1 
ATOM   9041  C CG  . LEU F 1 80  ? 8.035   57.944  -78.896  1.00 15.84 ? 80  LEU F CG  1 
ATOM   9042  C CD1 . LEU F 1 80  ? 8.561   58.319  -80.276  1.00 15.60 ? 80  LEU F CD1 1 
ATOM   9043  C CD2 . LEU F 1 80  ? 7.690   59.186  -78.101  1.00 16.13 ? 80  LEU F CD2 1 
ATOM   9044  N N   . ALA F 1 81  ? 4.967   54.541  -78.727  1.00 15.89 ? 81  ALA F N   1 
ATOM   9045  C CA  . ALA F 1 81  ? 3.711   53.855  -79.047  1.00 16.05 ? 81  ALA F CA  1 
ATOM   9046  C C   . ALA F 1 81  ? 3.111   53.172  -77.848  1.00 16.70 ? 81  ALA F C   1 
ATOM   9047  O O   . ALA F 1 81  ? 1.888   53.000  -77.755  1.00 16.42 ? 81  ALA F O   1 
ATOM   9048  C CB  . ALA F 1 81  ? 3.948   52.829  -80.151  1.00 16.23 ? 81  ALA F CB  1 
ATOM   9049  N N   . ALA F 1 82  ? 3.993   52.759  -76.944  1.00 18.39 ? 82  ALA F N   1 
ATOM   9050  C CA  . ALA F 1 82  ? 3.613   52.058  -75.719  1.00 18.78 ? 82  ALA F CA  1 
ATOM   9051  C C   . ALA F 1 82  ? 3.047   53.007  -74.664  1.00 19.02 ? 82  ALA F C   1 
ATOM   9052  O O   . ALA F 1 82  ? 2.362   52.561  -73.747  1.00 18.30 ? 82  ALA F O   1 
ATOM   9053  C CB  . ALA F 1 82  ? 4.817   51.314  -75.161  1.00 18.87 ? 82  ALA F CB  1 
ATOM   9054  N N   . HIS F 1 83  ? 3.357   54.299  -74.788  1.00 20.02 ? 83  HIS F N   1 
ATOM   9055  C CA  . HIS F 1 83  ? 2.887   55.306  -73.842  1.00 20.89 ? 83  HIS F CA  1 
ATOM   9056  C C   . HIS F 1 83  ? 1.950   56.346  -74.446  1.00 20.59 ? 83  HIS F C   1 
ATOM   9057  O O   . HIS F 1 83  ? 1.525   57.271  -73.751  1.00 20.08 ? 83  HIS F O   1 
ATOM   9058  C CB  . HIS F 1 83  ? 4.081   55.967  -73.164  1.00 21.75 ? 83  HIS F CB  1 
ATOM   9059  C CG  . HIS F 1 83  ? 4.976   54.992  -72.473  1.00 22.88 ? 83  HIS F CG  1 
ATOM   9060  N ND1 . HIS F 1 83  ? 4.499   54.047  -71.589  1.00 23.44 ? 83  HIS F ND1 1 
ATOM   9061  C CD2 . HIS F 1 83  ? 6.314   54.796  -72.556  1.00 23.29 ? 83  HIS F CD2 1 
ATOM   9062  C CE1 . HIS F 1 83  ? 5.506   53.308  -71.156  1.00 24.02 ? 83  HIS F CE1 1 
ATOM   9063  N NE2 . HIS F 1 83  ? 6.616   53.736  -71.734  1.00 24.36 ? 83  HIS F NE2 1 
ATOM   9064  N N   . GLU F 1 84  ? 1.606   56.183  -75.723  1.00 21.36 ? 84  GLU F N   1 
ATOM   9065  C CA  . GLU F 1 84  ? 0.603   57.036  -76.360  1.00 22.75 ? 84  GLU F CA  1 
ATOM   9066  C C   . GLU F 1 84  ? -0.729  56.937  -75.573  1.00 23.37 ? 84  GLU F C   1 
ATOM   9067  O O   . GLU F 1 84  ? -1.132  55.829  -75.177  1.00 24.08 ? 84  GLU F O   1 
ATOM   9068  C CB  . GLU F 1 84  ? 0.395   56.599  -77.820  1.00 23.62 ? 84  GLU F CB  1 
ATOM   9069  C CG  . GLU F 1 84  ? -0.497  57.536  -78.633  1.00 24.10 ? 84  GLU F CG  1 
ATOM   9070  C CD  . GLU F 1 84  ? -0.743  57.076  -80.053  1.00 24.55 ? 84  GLU F CD  1 
ATOM   9071  O OE1 . GLU F 1 84  ? -0.678  57.956  -80.935  1.00 26.70 ? 84  GLU F OE1 1 
ATOM   9072  O OE2 . GLU F 1 84  ? -1.007  55.876  -80.296  1.00 24.01 ? 84  GLU F OE2 1 
ATOM   9073  N N   . PRO F 1 85  ? -1.428  58.056  -75.348  1.00 23.28 ? 85  PRO F N   1 
ATOM   9074  C CA  . PRO F 1 85  ? -1.084  59.384  -75.872  1.00 23.19 ? 85  PRO F CA  1 
ATOM   9075  C C   . PRO F 1 85  ? -0.299  60.228  -74.884  1.00 22.59 ? 85  PRO F C   1 
ATOM   9076  O O   . PRO F 1 85  ? -0.545  60.162  -73.675  1.00 22.20 ? 85  PRO F O   1 
ATOM   9077  C CB  . PRO F 1 85  ? -2.461  60.022  -76.099  1.00 22.96 ? 85  PRO F CB  1 
ATOM   9078  C CG  . PRO F 1 85  ? -3.295  59.439  -75.018  1.00 22.79 ? 85  PRO F CG  1 
ATOM   9079  C CD  . PRO F 1 85  ? -2.784  58.041  -74.771  1.00 23.18 ? 85  PRO F CD  1 
ATOM   9080  N N   . LEU F 1 86  ? 0.613   61.033  -75.412  1.00 21.54 ? 86  LEU F N   1 
ATOM   9081  C CA  . LEU F 1 86  ? 1.415   61.928  -74.596  1.00 21.00 ? 86  LEU F CA  1 
ATOM   9082  C C   . LEU F 1 86  ? 1.166   63.380  -74.976  1.00 19.92 ? 86  LEU F C   1 
ATOM   9083  O O   . LEU F 1 86  ? 0.775   63.680  -76.087  1.00 18.83 ? 86  LEU F O   1 
ATOM   9084  C CB  . LEU F 1 86  ? 2.903   61.590  -74.757  1.00 21.47 ? 86  LEU F CB  1 
ATOM   9085  C CG  . LEU F 1 86  ? 3.329   60.168  -74.381  1.00 21.27 ? 86  LEU F CG  1 
ATOM   9086  C CD1 . LEU F 1 86  ? 4.690   59.826  -74.968  1.00 20.93 ? 86  LEU F CD1 1 
ATOM   9087  C CD2 . LEU F 1 86  ? 3.352   60.004  -72.870  1.00 21.08 ? 86  LEU F CD2 1 
ATOM   9088  N N   . ASP F 1 87  ? 1.402   64.273  -74.031  1.00 20.29 ? 87  ASP F N   1 
ATOM   9089  C CA  . ASP F 1 87  ? 1.312   65.705  -74.241  1.00 20.78 ? 87  ASP F CA  1 
ATOM   9090  C C   . ASP F 1 87  ? 2.667   66.370  -74.416  1.00 20.30 ? 87  ASP F C   1 
ATOM   9091  O O   . ASP F 1 87  ? 2.737   67.499  -74.932  1.00 19.73 ? 87  ASP F O   1 
ATOM   9092  C CB  . ASP F 1 87  ? 0.579   66.338  -73.063  1.00 21.89 ? 87  ASP F CB  1 
ATOM   9093  C CG  . ASP F 1 87  ? -0.843  65.886  -72.978  1.00 22.81 ? 87  ASP F CG  1 
ATOM   9094  O OD1 . ASP F 1 87  ? -1.048  64.755  -72.463  1.00 23.34 ? 87  ASP F OD1 1 
ATOM   9095  O OD2 . ASP F 1 87  ? -1.716  66.652  -73.452  1.00 24.60 ? 87  ASP F OD2 1 
ATOM   9096  N N   . LEU F 1 88  ? 3.726   65.702  -73.959  1.00 20.67 ? 88  LEU F N   1 
ATOM   9097  C CA  . LEU F 1 88  ? 5.106   66.159  -74.154  1.00 20.54 ? 88  LEU F CA  1 
ATOM   9098  C C   . LEU F 1 88  ? 6.136   65.018  -74.071  1.00 20.12 ? 88  LEU F C   1 
ATOM   9099  O O   . LEU F 1 88  ? 5.982   64.073  -73.298  1.00 19.42 ? 88  LEU F O   1 
ATOM   9100  C CB  . LEU F 1 88  ? 5.454   67.218  -73.101  1.00 20.95 ? 88  LEU F CB  1 
ATOM   9101  C CG  . LEU F 1 88  ? 6.815   67.909  -73.218  1.00 21.55 ? 88  LEU F CG  1 
ATOM   9102  C CD1 . LEU F 1 88  ? 6.880   68.769  -74.483  1.00 21.67 ? 88  LEU F CD1 1 
ATOM   9103  C CD2 . LEU F 1 88  ? 7.046   68.747  -71.960  1.00 22.23 ? 88  LEU F CD2 1 
ATOM   9104  N N   . VAL F 1 89  ? 7.186   65.123  -74.873  1.00 20.11 ? 89  VAL F N   1 
ATOM   9105  C CA  . VAL F 1 89  ? 8.325   64.228  -74.773  1.00 21.21 ? 89  VAL F CA  1 
ATOM   9106  C C   . VAL F 1 89  ? 9.560   65.054  -74.431  1.00 22.15 ? 89  VAL F C   1 
ATOM   9107  O O   . VAL F 1 89  ? 9.900   65.994  -75.146  1.00 24.07 ? 89  VAL F O   1 
ATOM   9108  C CB  . VAL F 1 89  ? 8.566   63.455  -76.084  1.00 21.10 ? 89  VAL F CB  1 
ATOM   9109  C CG1 . VAL F 1 89  ? 9.842   62.636  -75.998  1.00 21.37 ? 89  VAL F CG1 1 
ATOM   9110  C CG2 . VAL F 1 89  ? 7.400   62.528  -76.365  1.00 21.07 ? 89  VAL F CG2 1 
ATOM   9111  N N   . ILE F 1 90  ? 10.216  64.703  -73.332  1.00 21.86 ? 90  ILE F N   1 
ATOM   9112  C CA  . ILE F 1 90  ? 11.440  65.361  -72.910  1.00 21.15 ? 90  ILE F CA  1 
ATOM   9113  C C   . ILE F 1 90  ? 12.589  64.421  -73.190  1.00 20.90 ? 90  ILE F C   1 
ATOM   9114  O O   . ILE F 1 90  ? 12.536  63.247  -72.830  1.00 20.88 ? 90  ILE F O   1 
ATOM   9115  C CB  . ILE F 1 90  ? 11.405  65.686  -71.411  1.00 21.10 ? 90  ILE F CB  1 
ATOM   9116  C CG1 . ILE F 1 90  ? 10.371  66.795  -71.143  1.00 20.71 ? 90  ILE F CG1 1 
ATOM   9117  C CG2 . ILE F 1 90  ? 12.770  66.139  -70.940  1.00 21.19 ? 90  ILE F CG2 1 
ATOM   9118  C CD1 . ILE F 1 90  ? 10.181  67.196  -69.698  1.00 20.04 ? 90  ILE F CD1 1 
ATOM   9119  N N   . ILE F 1 91  ? 13.627  64.937  -73.834  1.00 20.75 ? 91  ILE F N   1 
ATOM   9120  C CA  . ILE F 1 91  ? 14.809  64.139  -74.165  1.00 20.53 ? 91  ILE F CA  1 
ATOM   9121  C C   . ILE F 1 91  ? 15.987  64.801  -73.500  1.00 19.62 ? 91  ILE F C   1 
ATOM   9122  O O   . ILE F 1 91  ? 16.283  65.954  -73.788  1.00 19.35 ? 91  ILE F O   1 
ATOM   9123  C CB  . ILE F 1 91  ? 15.060  64.065  -75.694  1.00 21.12 ? 91  ILE F CB  1 
ATOM   9124  C CG1 . ILE F 1 91  ? 13.846  63.474  -76.417  1.00 21.60 ? 91  ILE F CG1 1 
ATOM   9125  C CG2 . ILE F 1 91  ? 16.319  63.257  -76.015  1.00 20.93 ? 91  ILE F CG2 1 
ATOM   9126  C CD1 . ILE F 1 91  ? 13.915  63.640  -77.922  1.00 21.87 ? 91  ILE F CD1 1 
ATOM   9127  N N   . LEU F 1 92  ? 16.635  64.074  -72.598  1.00 19.60 ? 92  LEU F N   1 
ATOM   9128  C CA  . LEU F 1 92  ? 17.888  64.505  -71.982  1.00 20.33 ? 92  LEU F CA  1 
ATOM   9129  C C   . LEU F 1 92  ? 18.925  63.421  -72.208  1.00 20.85 ? 92  LEU F C   1 
ATOM   9130  O O   . LEU F 1 92  ? 19.085  62.497  -71.371  1.00 23.37 ? 92  LEU F O   1 
ATOM   9131  C CB  . LEU F 1 92  ? 17.695  64.791  -70.490  1.00 20.45 ? 92  LEU F CB  1 
ATOM   9132  C CG  . LEU F 1 92  ? 18.931  65.056  -69.644  1.00 20.37 ? 92  LEU F CG  1 
ATOM   9133  C CD1 . LEU F 1 92  ? 19.757  66.163  -70.258  1.00 20.46 ? 92  LEU F CD1 1 
ATOM   9134  C CD2 . LEU F 1 92  ? 18.517  65.401  -68.223  1.00 20.82 ? 92  LEU F CD2 1 
ATOM   9135  N N   . LEU F 1 93  ? 19.596  63.541  -73.356  1.00 20.52 ? 93  LEU F N   1 
ATOM   9136  C CA  . LEU F 1 93  ? 20.633  62.619  -73.805  1.00 20.84 ? 93  LEU F CA  1 
ATOM   9137  C C   . LEU F 1 93  ? 21.765  63.387  -74.443  1.00 21.89 ? 93  LEU F C   1 
ATOM   9138  O O   . LEU F 1 93  ? 21.596  64.543  -74.818  1.00 20.10 ? 93  LEU F O   1 
ATOM   9139  C CB  . LEU F 1 93  ? 20.079  61.666  -74.862  1.00 20.40 ? 93  LEU F CB  1 
ATOM   9140  C CG  . LEU F 1 93  ? 19.129  60.564  -74.410  1.00 20.12 ? 93  LEU F CG  1 
ATOM   9141  C CD1 . LEU F 1 93  ? 18.513  59.895  -75.631  1.00 19.47 ? 93  LEU F CD1 1 
ATOM   9142  C CD2 . LEU F 1 93  ? 19.841  59.560  -73.511  1.00 19.88 ? 93  LEU F CD2 1 
ATOM   9143  N N   . GLY F 1 94  ? 22.903  62.713  -74.603  1.00 24.48 ? 94  GLY F N   1 
ATOM   9144  C CA  . GLY F 1 94  ? 24.088  63.307  -75.223  1.00 25.94 ? 94  GLY F CA  1 
ATOM   9145  C C   . GLY F 1 94  ? 25.370  63.152  -74.416  1.00 27.39 ? 94  GLY F C   1 
ATOM   9146  O O   . GLY F 1 94  ? 26.470  63.304  -74.946  1.00 26.42 ? 94  GLY F O   1 
ATOM   9147  N N   . THR F 1 95  ? 25.233  62.860  -73.128  1.00 29.96 ? 95  THR F N   1 
ATOM   9148  C CA  . THR F 1 95  ? 26.404  62.731  -72.260  1.00 28.88 ? 95  THR F CA  1 
ATOM   9149  C C   . THR F 1 95  ? 27.245  61.524  -72.674  1.00 26.55 ? 95  THR F C   1 
ATOM   9150  O O   . THR F 1 95  ? 28.455  61.649  -72.844  1.00 25.09 ? 95  THR F O   1 
ATOM   9151  C CB  . THR F 1 95  ? 25.976  62.692  -70.775  1.00 31.07 ? 95  THR F CB  1 
ATOM   9152  O OG1 . THR F 1 95  ? 25.115  63.816  -70.499  1.00 34.74 ? 95  THR F OG1 1 
ATOM   9153  C CG2 . THR F 1 95  ? 27.167  62.762  -69.868  1.00 31.39 ? 95  THR F CG2 1 
ATOM   9154  N N   . ASN F 1 96  ? 26.608  60.377  -72.901  1.00 26.42 ? 96  ASN F N   1 
ATOM   9155  C CA  . ASN F 1 96  ? 27.346  59.181  -73.357  1.00 25.45 ? 96  ASN F CA  1 
ATOM   9156  C C   . ASN F 1 96  ? 27.890  59.312  -74.785  1.00 24.36 ? 96  ASN F C   1 
ATOM   9157  O O   . ASN F 1 96  ? 28.873  58.689  -75.140  1.00 22.71 ? 96  ASN F O   1 
ATOM   9158  C CB  . ASN F 1 96  ? 26.481  57.937  -73.260  1.00 25.01 ? 96  ASN F CB  1 
ATOM   9159  C CG  . ASN F 1 96  ? 26.107  57.598  -71.826  1.00 24.86 ? 96  ASN F CG  1 
ATOM   9160  O OD1 . ASN F 1 96  ? 26.967  57.254  -71.011  1.00 23.54 ? 96  ASN F OD1 1 
ATOM   9161  N ND2 . ASN F 1 96  ? 24.815  57.671  -71.515  1.00 25.21 ? 96  ASN F ND2 1 
ATOM   9162  N N   . ASP F 1 97  ? 27.254  60.140  -75.599  1.00 25.10 ? 97  ASP F N   1 
ATOM   9163  C CA  . ASP F 1 97  ? 27.701  60.360  -76.979  1.00 25.22 ? 97  ASP F CA  1 
ATOM   9164  C C   . ASP F 1 97  ? 29.093  61.002  -77.073  1.00 25.66 ? 97  ASP F C   1 
ATOM   9165  O O   . ASP F 1 97  ? 29.733  60.937  -78.128  1.00 27.56 ? 97  ASP F O   1 
ATOM   9166  C CB  . ASP F 1 97  ? 26.688  61.219  -77.755  1.00 24.46 ? 97  ASP F CB  1 
ATOM   9167  C CG  . ASP F 1 97  ? 25.330  60.550  -77.904  1.00 23.44 ? 97  ASP F CG  1 
ATOM   9168  O OD1 . ASP F 1 97  ? 24.642  60.369  -76.881  1.00 24.13 ? 97  ASP F OD1 1 
ATOM   9169  O OD2 . ASP F 1 97  ? 24.934  60.234  -79.044  1.00 22.55 ? 97  ASP F OD2 1 
ATOM   9170  N N   . THR F 1 98  ? 29.542  61.634  -75.989  1.00 24.61 ? 98  THR F N   1 
ATOM   9171  C CA  . THR F 1 98  ? 30.860  62.270  -75.951  1.00 24.55 ? 98  THR F CA  1 
ATOM   9172  C C   . THR F 1 98  ? 31.995  61.267  -75.685  1.00 25.63 ? 98  THR F C   1 
ATOM   9173  O O   . THR F 1 98  ? 33.181  61.620  -75.795  1.00 24.36 ? 98  THR F O   1 
ATOM   9174  C CB  . THR F 1 98  ? 30.929  63.356  -74.876  1.00 24.77 ? 98  THR F CB  1 
ATOM   9175  O OG1 . THR F 1 98  ? 30.838  62.753  -73.585  1.00 25.54 ? 98  THR F OG1 1 
ATOM   9176  C CG2 . THR F 1 98  ? 29.794  64.371  -75.058  1.00 25.34 ? 98  THR F CG2 1 
ATOM   9177  N N   . LYS F 1 99  ? 31.636  60.024  -75.340  1.00 26.13 ? 99  LYS F N   1 
ATOM   9178  C CA  . LYS F 1 99  ? 32.621  58.967  -75.138  1.00 25.54 ? 99  LYS F CA  1 
ATOM   9179  C C   . LYS F 1 99  ? 33.544  58.861  -76.335  1.00 25.64 ? 99  LYS F C   1 
ATOM   9180  O O   . LYS F 1 99  ? 33.102  58.792  -77.480  1.00 26.10 ? 99  LYS F O   1 
ATOM   9181  C CB  . LYS F 1 99  ? 31.960  57.604  -74.864  1.00 26.31 ? 99  LYS F CB  1 
ATOM   9182  C CG  . LYS F 1 99  ? 31.362  57.476  -73.469  1.00 26.99 ? 99  LYS F CG  1 
ATOM   9183  C CD  . LYS F 1 99  ? 30.566  56.197  -73.249  1.00 27.11 ? 99  LYS F CD  1 
ATOM   9184  C CE  . LYS F 1 99  ? 30.193  56.076  -71.781  1.00 28.32 ? 99  LYS F CE  1 
ATOM   9185  N NZ  . LYS F 1 99  ? 29.064  55.130  -71.537  1.00 30.10 ? 99  LYS F NZ  1 
ATOM   9186  N N   . THR F 1 100 ? 34.833  58.845  -76.032  1.00 25.82 ? 100 THR F N   1 
ATOM   9187  C CA  . THR F 1 100 ? 35.910  58.838  -77.010  1.00 25.72 ? 100 THR F CA  1 
ATOM   9188  C C   . THR F 1 100 ? 35.706  57.813  -78.134  1.00 24.66 ? 100 THR F C   1 
ATOM   9189  O O   . THR F 1 100 ? 35.780  58.168  -79.301  1.00 24.04 ? 100 THR F O   1 
ATOM   9190  C CB  . THR F 1 100 ? 37.259  58.555  -76.299  1.00 26.74 ? 100 THR F CB  1 
ATOM   9191  O OG1 . THR F 1 100 ? 37.714  59.722  -75.603  1.00 28.09 ? 100 THR F OG1 1 
ATOM   9192  C CG2 . THR F 1 100 ? 38.330  58.076  -77.305  1.00 26.29 ? 100 THR F CG2 1 
ATOM   9193  N N   . TYR F 1 101 ? 35.444  56.562  -77.778  1.00 24.69 ? 101 TYR F N   1 
ATOM   9194  C CA  . TYR F 1 101 ? 35.378  55.483  -78.776  1.00 24.56 ? 101 TYR F CA  1 
ATOM   9195  C C   . TYR F 1 101 ? 34.208  55.587  -79.763  1.00 24.74 ? 101 TYR F C   1 
ATOM   9196  O O   . TYR F 1 101 ? 34.232  54.940  -80.792  1.00 23.81 ? 101 TYR F O   1 
ATOM   9197  C CB  . TYR F 1 101 ? 35.404  54.081  -78.126  1.00 23.30 ? 101 TYR F CB  1 
ATOM   9198  C CG  . TYR F 1 101 ? 34.290  53.793  -77.136  1.00 22.04 ? 101 TYR F CG  1 
ATOM   9199  C CD1 . TYR F 1 101 ? 33.017  53.431  -77.562  1.00 21.42 ? 101 TYR F CD1 1 
ATOM   9200  C CD2 . TYR F 1 101 ? 34.528  53.838  -75.767  1.00 21.35 ? 101 TYR F CD2 1 
ATOM   9201  C CE1 . TYR F 1 101 ? 32.007  53.157  -76.645  1.00 21.01 ? 101 TYR F CE1 1 
ATOM   9202  C CE2 . TYR F 1 101 ? 33.518  53.579  -74.851  1.00 20.93 ? 101 TYR F CE2 1 
ATOM   9203  C CZ  . TYR F 1 101 ? 32.262  53.226  -75.288  1.00 20.64 ? 101 TYR F CZ  1 
ATOM   9204  O OH  . TYR F 1 101 ? 31.274  52.955  -74.375  1.00 18.82 ? 101 TYR F OH  1 
ATOM   9205  N N   . LEU F 1 102 ? 33.193  56.387  -79.463  1.00 26.03 ? 102 LEU F N   1 
ATOM   9206  C CA  . LEU F 1 102 ? 32.094  56.608  -80.415  1.00 27.14 ? 102 LEU F CA  1 
ATOM   9207  C C   . LEU F 1 102 ? 32.468  57.642  -81.477  1.00 27.55 ? 102 LEU F C   1 
ATOM   9208  O O   . LEU F 1 102 ? 31.791  57.771  -82.493  1.00 28.95 ? 102 LEU F O   1 
ATOM   9209  C CB  . LEU F 1 102 ? 30.832  57.058  -79.681  1.00 28.41 ? 102 LEU F CB  1 
ATOM   9210  C CG  . LEU F 1 102 ? 30.332  56.097  -78.597  1.00 28.49 ? 102 LEU F CG  1 
ATOM   9211  C CD1 . LEU F 1 102 ? 29.193  56.702  -77.817  1.00 28.08 ? 102 LEU F CD1 1 
ATOM   9212  C CD2 . LEU F 1 102 ? 29.874  54.791  -79.207  1.00 29.24 ? 102 LEU F CD2 1 
ATOM   9213  N N   . ASN F 1 103 ? 33.528  58.403  -81.217  1.00 26.99 ? 103 ASN F N   1 
ATOM   9214  C CA  . ASN F 1 103 ? 34.136  59.267  -82.218  1.00 25.40 ? 103 ASN F CA  1 
ATOM   9215  C C   . ASN F 1 103 ? 33.159  60.281  -82.849  1.00 23.19 ? 103 ASN F C   1 
ATOM   9216  O O   . ASN F 1 103 ? 33.160  60.502  -84.059  1.00 22.87 ? 103 ASN F O   1 
ATOM   9217  C CB  . ASN F 1 103 ? 34.806  58.387  -83.281  1.00 26.30 ? 103 ASN F CB  1 
ATOM   9218  C CG  . ASN F 1 103 ? 35.632  59.199  -84.272  1.00 27.94 ? 103 ASN F CG  1 
ATOM   9219  O OD1 . ASN F 1 103 ? 36.534  59.955  -83.894  1.00 29.49 ? 103 ASN F OD1 1 
ATOM   9220  N ND2 . ASN F 1 103 ? 35.313  59.063  -85.553  1.00 28.07 ? 103 ASN F ND2 1 
ATOM   9221  N N   . ARG F 1 104 ? 32.339  60.914  -82.018  1.00 21.48 ? 104 ARG F N   1 
ATOM   9222  C CA  . ARG F 1 104 ? 31.328  61.858  -82.514  1.00 20.18 ? 104 ARG F CA  1 
ATOM   9223  C C   . ARG F 1 104 ? 31.733  63.313  -82.308  1.00 19.23 ? 104 ARG F C   1 
ATOM   9224  O O   . ARG F 1 104 ? 32.333  63.661  -81.305  1.00 18.53 ? 104 ARG F O   1 
ATOM   9225  C CB  . ARG F 1 104 ? 29.990  61.644  -81.802  1.00 19.49 ? 104 ARG F CB  1 
ATOM   9226  C CG  . ARG F 1 104 ? 29.625  60.194  -81.531  1.00 18.42 ? 104 ARG F CG  1 
ATOM   9227  C CD  . ARG F 1 104 ? 28.129  60.037  -81.378  1.00 17.79 ? 104 ARG F CD  1 
ATOM   9228  N NE  . ARG F 1 104 ? 27.453  59.917  -82.671  1.00 17.21 ? 104 ARG F NE  1 
ATOM   9229  C CZ  . ARG F 1 104 ? 26.130  59.863  -82.834  1.00 16.20 ? 104 ARG F CZ  1 
ATOM   9230  N NH1 . ARG F 1 104 ? 25.301  59.914  -81.794  1.00 15.59 ? 104 ARG F NH1 1 
ATOM   9231  N NH2 . ARG F 1 104 ? 25.634  59.759  -84.052  1.00 16.01 ? 104 ARG F NH2 1 
ATOM   9232  N N   . THR F 1 105 ? 31.383  64.154  -83.264  1.00 19.03 ? 105 THR F N   1 
ATOM   9233  C CA  . THR F 1 105 ? 31.501  65.590  -83.136  1.00 19.07 ? 105 THR F CA  1 
ATOM   9234  C C   . THR F 1 105 ? 30.205  66.088  -82.511  1.00 19.58 ? 105 THR F C   1 
ATOM   9235  O O   . THR F 1 105 ? 29.211  65.370  -82.516  1.00 19.39 ? 105 THR F O   1 
ATOM   9236  C CB  . THR F 1 105 ? 31.639  66.255  -84.513  1.00 19.22 ? 105 THR F CB  1 
ATOM   9237  O OG1 . THR F 1 105 ? 30.393  66.152  -85.233  1.00 19.80 ? 105 THR F OG1 1 
ATOM   9238  C CG2 . THR F 1 105 ? 32.753  65.605  -85.317  1.00 19.09 ? 105 THR F CG2 1 
ATOM   9239  N N   . PRO F 1 106 ? 30.205  67.320  -81.974  1.00 20.29 ? 106 PRO F N   1 
ATOM   9240  C CA  . PRO F 1 106 ? 28.982  67.905  -81.433  1.00 20.60 ? 106 PRO F CA  1 
ATOM   9241  C C   . PRO F 1 106 ? 27.845  67.997  -82.454  1.00 20.93 ? 106 PRO F C   1 
ATOM   9242  O O   . PRO F 1 106 ? 26.695  67.720  -82.096  1.00 21.61 ? 106 PRO F O   1 
ATOM   9243  C CB  . PRO F 1 106 ? 29.414  69.308  -81.009  1.00 20.41 ? 106 PRO F CB  1 
ATOM   9244  C CG  . PRO F 1 106 ? 30.857  69.170  -80.717  1.00 20.58 ? 106 PRO F CG  1 
ATOM   9245  C CD  . PRO F 1 106 ? 31.379  68.156  -81.684  1.00 20.42 ? 106 PRO F CD  1 
ATOM   9246  N N   . PHE F 1 107 ? 28.163  68.376  -83.696  1.00 20.05 ? 107 PHE F N   1 
ATOM   9247  C CA  . PHE F 1 107 ? 27.153  68.444  -84.745  1.00 19.40 ? 107 PHE F CA  1 
ATOM   9248  C C   . PHE F 1 107 ? 26.544  67.056  -84.997  1.00 19.41 ? 107 PHE F C   1 
ATOM   9249  O O   . PHE F 1 107 ? 25.326  66.909  -85.163  1.00 19.90 ? 107 PHE F O   1 
ATOM   9250  C CB  . PHE F 1 107 ? 27.722  69.011  -86.045  1.00 19.03 ? 107 PHE F CB  1 
ATOM   9251  C CG  . PHE F 1 107 ? 26.703  69.093  -87.150  1.00 19.25 ? 107 PHE F CG  1 
ATOM   9252  C CD1 . PHE F 1 107 ? 25.585  69.921  -87.037  1.00 19.32 ? 107 PHE F CD1 1 
ATOM   9253  C CD2 . PHE F 1 107 ? 26.847  68.343  -88.300  1.00 19.58 ? 107 PHE F CD2 1 
ATOM   9254  C CE1 . PHE F 1 107 ? 24.634  69.977  -88.043  1.00 19.18 ? 107 PHE F CE1 1 
ATOM   9255  C CE2 . PHE F 1 107 ? 25.903  68.412  -89.322  1.00 19.35 ? 107 PHE F CE2 1 
ATOM   9256  C CZ  . PHE F 1 107 ? 24.788  69.220  -89.184  1.00 19.32 ? 107 PHE F CZ  1 
ATOM   9257  N N   . GLU F 1 108 ? 27.394  66.042  -85.004  1.00 18.80 ? 108 GLU F N   1 
ATOM   9258  C CA  . GLU F 1 108 ? 26.916  64.680  -85.147  1.00 19.27 ? 108 GLU F CA  1 
ATOM   9259  C C   . GLU F 1 108 ? 25.931  64.300  -84.036  1.00 19.26 ? 108 GLU F C   1 
ATOM   9260  O O   . GLU F 1 108 ? 24.928  63.630  -84.280  1.00 19.13 ? 108 GLU F O   1 
ATOM   9261  C CB  . GLU F 1 108 ? 28.077  63.694  -85.127  1.00 19.54 ? 108 GLU F CB  1 
ATOM   9262  C CG  . GLU F 1 108 ? 27.629  62.272  -85.452  1.00 19.69 ? 108 GLU F CG  1 
ATOM   9263  C CD  . GLU F 1 108 ? 28.766  61.332  -85.622  1.00 19.90 ? 108 GLU F CD  1 
ATOM   9264  O OE1 . GLU F 1 108 ? 28.779  60.290  -84.946  1.00 21.12 ? 108 GLU F OE1 1 
ATOM   9265  O OE2 . GLU F 1 108 ? 29.697  61.682  -86.361  1.00 20.56 ? 108 GLU F OE2 1 
ATOM   9266  N N   . ILE F 1 109 ? 26.240  64.732  -82.816  1.00 18.87 ? 109 ILE F N   1 
ATOM   9267  C CA  . ILE F 1 109 ? 25.420  64.396  -81.665  1.00 18.56 ? 109 ILE F CA  1 
ATOM   9268  C C   . ILE F 1 109 ? 24.089  65.138  -81.759  1.00 18.54 ? 109 ILE F C   1 
ATOM   9269  O O   . ILE F 1 109 ? 23.033  64.577  -81.437  1.00 18.37 ? 109 ILE F O   1 
ATOM   9270  C CB  . ILE F 1 109 ? 26.148  64.706  -80.337  1.00 18.77 ? 109 ILE F CB  1 
ATOM   9271  C CG1 . ILE F 1 109 ? 27.446  63.892  -80.240  1.00 18.74 ? 109 ILE F CG1 1 
ATOM   9272  C CG2 . ILE F 1 109 ? 25.248  64.362  -79.147  1.00 19.08 ? 109 ILE F CG2 1 
ATOM   9273  C CD1 . ILE F 1 109 ? 28.412  64.349  -79.165  1.00 18.61 ? 109 ILE F CD1 1 
ATOM   9274  N N   . GLY F 1 110 ? 24.139  66.385  -82.221  1.00 18.25 ? 110 GLY F N   1 
ATOM   9275  C CA  . GLY F 1 110 ? 22.915  67.115  -82.545  1.00 18.58 ? 110 GLY F CA  1 
ATOM   9276  C C   . GLY F 1 110 ? 22.021  66.376  -83.526  1.00 18.09 ? 110 GLY F C   1 
ATOM   9277  O O   . GLY F 1 110 ? 20.812  66.262  -83.313  1.00 18.22 ? 110 GLY F O   1 
ATOM   9278  N N   . LEU F 1 111 ? 22.616  65.880  -84.604  1.00 17.65 ? 111 LEU F N   1 
ATOM   9279  C CA  . LEU F 1 111 ? 21.881  65.091  -85.592  1.00 17.67 ? 111 LEU F CA  1 
ATOM   9280  C C   . LEU F 1 111 ? 21.225  63.865  -84.959  1.00 17.70 ? 111 LEU F C   1 
ATOM   9281  O O   . LEU F 1 111 ? 20.106  63.478  -85.344  1.00 17.19 ? 111 LEU F O   1 
ATOM   9282  C CB  . LEU F 1 111 ? 22.805  64.659  -86.732  1.00 17.17 ? 111 LEU F CB  1 
ATOM   9283  C CG  . LEU F 1 111 ? 23.216  65.809  -87.656  1.00 16.92 ? 111 LEU F CG  1 
ATOM   9284  C CD1 . LEU F 1 111 ? 24.193  65.297  -88.698  1.00 17.34 ? 111 LEU F CD1 1 
ATOM   9285  C CD2 . LEU F 1 111 ? 22.024  66.459  -88.342  1.00 16.36 ? 111 LEU F CD2 1 
ATOM   9286  N N   . GLY F 1 112 ? 21.921  63.270  -83.996  1.00 17.50 ? 112 GLY F N   1 
ATOM   9287  C CA  . GLY F 1 112 ? 21.398  62.124  -83.275  1.00 18.27 ? 112 GLY F CA  1 
ATOM   9288  C C   . GLY F 1 112 ? 20.161  62.489  -82.485  1.00 19.18 ? 112 GLY F C   1 
ATOM   9289  O O   . GLY F 1 112 ? 19.146  61.788  -82.536  1.00 18.88 ? 112 GLY F O   1 
ATOM   9290  N N   . ALA F 1 113 ? 20.245  63.600  -81.757  1.00 20.32 ? 113 ALA F N   1 
ATOM   9291  C CA  . ALA F 1 113 ? 19.093  64.121  -81.037  1.00 20.34 ? 113 ALA F CA  1 
ATOM   9292  C C   . ALA F 1 113 ? 17.987  64.452  -82.027  1.00 20.64 ? 113 ALA F C   1 
ATOM   9293  O O   . ALA F 1 113 ? 16.821  64.176  -81.757  1.00 21.12 ? 113 ALA F O   1 
ATOM   9294  C CB  . ALA F 1 113 ? 19.462  65.343  -80.232  1.00 20.18 ? 113 ALA F CB  1 
ATOM   9295  N N   . GLY F 1 114 ? 18.361  65.024  -83.171  1.00 20.32 ? 114 GLY F N   1 
ATOM   9296  C CA  . GLY F 1 114 ? 17.419  65.279  -84.261  1.00 21.09 ? 114 GLY F CA  1 
ATOM   9297  C C   . GLY F 1 114 ? 16.690  64.031  -84.761  1.00 21.78 ? 114 GLY F C   1 
ATOM   9298  O O   . GLY F 1 114 ? 15.476  64.057  -85.002  1.00 22.15 ? 114 GLY F O   1 
ATOM   9299  N N   . ALA F 1 115 ? 17.433  62.935  -84.910  1.00 21.51 ? 115 ALA F N   1 
ATOM   9300  C CA  . ALA F 1 115 ? 16.842  61.657  -85.284  1.00 21.67 ? 115 ALA F CA  1 
ATOM   9301  C C   . ALA F 1 115 ? 15.744  61.251  -84.314  1.00 21.59 ? 115 ALA F C   1 
ATOM   9302  O O   . ALA F 1 115 ? 14.716  60.701  -84.728  1.00 23.57 ? 115 ALA F O   1 
ATOM   9303  C CB  . ALA F 1 115 ? 17.902  60.571  -85.339  1.00 21.87 ? 115 ALA F CB  1 
ATOM   9304  N N   . LEU F 1 116 ? 15.967  61.507  -83.028  1.00 20.08 ? 116 LEU F N   1 
ATOM   9305  C CA  . LEU F 1 116 ? 14.974  61.168  -82.013  1.00 19.17 ? 116 LEU F CA  1 
ATOM   9306  C C   . LEU F 1 116 ? 13.753  62.075  -82.099  1.00 18.84 ? 116 LEU F C   1 
ATOM   9307  O O   . LEU F 1 116 ? 12.625  61.604  -82.022  1.00 17.70 ? 116 LEU F O   1 
ATOM   9308  C CB  . LEU F 1 116 ? 15.594  61.202  -80.609  1.00 18.90 ? 116 LEU F CB  1 
ATOM   9309  C CG  . LEU F 1 116 ? 16.725  60.196  -80.360  1.00 18.42 ? 116 LEU F CG  1 
ATOM   9310  C CD1 . LEU F 1 116 ? 17.274  60.377  -78.965  1.00 18.49 ? 116 LEU F CD1 1 
ATOM   9311  C CD2 . LEU F 1 116 ? 16.262  58.759  -80.586  1.00 18.43 ? 116 LEU F CD2 1 
ATOM   9312  N N   . ILE F 1 117 ? 13.979  63.370  -82.294  1.00 19.64 ? 117 ILE F N   1 
ATOM   9313  C CA  . ILE F 1 117 ? 12.873  64.316  -82.473  1.00 19.56 ? 117 ILE F CA  1 
ATOM   9314  C C   . ILE F 1 117 ? 11.997  63.874  -83.648  1.00 19.72 ? 117 ILE F C   1 
ATOM   9315  O O   . ILE F 1 117 ? 10.763  63.842  -83.538  1.00 20.84 ? 117 ILE F O   1 
ATOM   9316  C CB  . ILE F 1 117 ? 13.363  65.763  -82.701  1.00 19.07 ? 117 ILE F CB  1 
ATOM   9317  C CG1 . ILE F 1 117 ? 14.021  66.308  -81.427  1.00 19.15 ? 117 ILE F CG1 1 
ATOM   9318  C CG2 . ILE F 1 117 ? 12.197  66.669  -83.090  1.00 18.84 ? 117 ILE F CG2 1 
ATOM   9319  C CD1 . ILE F 1 117 ? 14.845  67.550  -81.624  1.00 19.12 ? 117 ILE F CD1 1 
ATOM   9320  N N   . ASN F 1 118 ? 12.645  63.521  -84.754  1.00 18.80 ? 118 ASN F N   1 
ATOM   9321  C CA  . ASN F 1 118 ? 11.944  63.014  -85.924  1.00 18.84 ? 118 ASN F CA  1 
ATOM   9322  C C   . ASN F 1 118 ? 11.099  61.768  -85.619  1.00 18.70 ? 118 ASN F C   1 
ATOM   9323  O O   . ASN F 1 118 ? 9.969   61.649  -86.096  1.00 18.44 ? 118 ASN F O   1 
ATOM   9324  C CB  . ASN F 1 118 ? 12.934  62.722  -87.053  1.00 18.81 ? 118 ASN F CB  1 
ATOM   9325  C CG  . ASN F 1 118 ? 12.246  62.369  -88.352  1.00 18.72 ? 118 ASN F CG  1 
ATOM   9326  O OD1 . ASN F 1 118 ? 11.260  63.012  -88.751  1.00 19.13 ? 118 ASN F OD1 1 
ATOM   9327  N ND2 . ASN F 1 118 ? 12.747  61.337  -89.012  1.00 18.16 ? 118 ASN F ND2 1 
ATOM   9328  N N   . MET F 1 119 ? 11.638  60.839  -84.835  1.00 19.21 ? 119 MET F N   1 
ATOM   9329  C CA  . MET F 1 119 ? 10.865  59.658  -84.448  1.00 20.15 ? 119 MET F CA  1 
ATOM   9330  C C   . MET F 1 119 ? 9.600   60.036  -83.678  1.00 21.21 ? 119 MET F C   1 
ATOM   9331  O O   . MET F 1 119 ? 8.538   59.428  -83.882  1.00 22.38 ? 119 MET F O   1 
ATOM   9332  C CB  . MET F 1 119 ? 11.719  58.688  -83.635  1.00 20.27 ? 119 MET F CB  1 
ATOM   9333  C CG  . MET F 1 119 ? 12.698  57.912  -84.501  1.00 20.00 ? 119 MET F CG  1 
ATOM   9334  S SD  . MET F 1 119 ? 13.944  57.062  -83.523  1.00 18.70 ? 119 MET F SD  1 
ATOM   9335  C CE  . MET F 1 119 ? 14.473  55.818  -84.705  1.00 18.88 ? 119 MET F CE  1 
ATOM   9336  N N   . VAL F 1 120 ? 9.710   61.046  -82.813  1.00 20.68 ? 120 VAL F N   1 
ATOM   9337  C CA  . VAL F 1 120 ? 8.555   61.542  -82.069  1.00 20.07 ? 120 VAL F CA  1 
ATOM   9338  C C   . VAL F 1 120 ? 7.541   62.193  -83.012  1.00 19.51 ? 120 VAL F C   1 
ATOM   9339  O O   . VAL F 1 120 ? 6.347   62.029  -82.842  1.00 19.60 ? 120 VAL F O   1 
ATOM   9340  C CB  . VAL F 1 120 ? 8.960   62.564  -80.977  1.00 20.33 ? 120 VAL F CB  1 
ATOM   9341  C CG1 . VAL F 1 120 ? 7.725   63.088  -80.244  1.00 20.36 ? 120 VAL F CG1 1 
ATOM   9342  C CG2 . VAL F 1 120 ? 9.929   61.947  -79.986  1.00 20.44 ? 120 VAL F CG2 1 
ATOM   9343  N N   . GLN F 1 121 ? 8.022   62.944  -83.999  1.00 19.32 ? 121 GLN F N   1 
ATOM   9344  C CA  . GLN F 1 121 ? 7.134   63.652  -84.923  1.00 19.15 ? 121 GLN F CA  1 
ATOM   9345  C C   . GLN F 1 121 ? 6.377   62.706  -85.847  1.00 20.35 ? 121 GLN F C   1 
ATOM   9346  O O   . GLN F 1 121 ? 5.244   62.984  -86.240  1.00 20.42 ? 121 GLN F O   1 
ATOM   9347  C CB  . GLN F 1 121 ? 7.912   64.683  -85.730  1.00 18.54 ? 121 GLN F CB  1 
ATOM   9348  C CG  . GLN F 1 121 ? 8.357   65.867  -84.887  1.00 18.30 ? 121 GLN F CG  1 
ATOM   9349  C CD  . GLN F 1 121 ? 9.065   66.921  -85.707  1.00 18.18 ? 121 GLN F CD  1 
ATOM   9350  O OE1 . GLN F 1 121 ? 9.418   66.691  -86.857  1.00 17.66 ? 121 GLN F OE1 1 
ATOM   9351  N NE2 . GLN F 1 121 ? 9.274   68.090  -85.114  1.00 18.65 ? 121 GLN F NE2 1 
ATOM   9352  N N   . LYS F 1 122 ? 7.000   61.579  -86.183  1.00 21.49 ? 122 LYS F N   1 
ATOM   9353  C CA  . LYS F 1 122 ? 6.356   60.540  -86.977  1.00 21.92 ? 122 LYS F CA  1 
ATOM   9354  C C   . LYS F 1 122 ? 5.717   59.466  -86.091  1.00 23.57 ? 122 LYS F C   1 
ATOM   9355  O O   . LYS F 1 122 ? 5.352   58.404  -86.579  1.00 22.71 ? 122 LYS F O   1 
ATOM   9356  C CB  . LYS F 1 122 ? 7.387   59.902  -87.894  1.00 20.93 ? 122 LYS F CB  1 
ATOM   9357  C CG  . LYS F 1 122 ? 8.105   60.895  -88.799  1.00 20.58 ? 122 LYS F CG  1 
ATOM   9358  C CD  . LYS F 1 122 ? 9.201   60.234  -89.612  1.00 20.45 ? 122 LYS F CD  1 
ATOM   9359  C CE  . LYS F 1 122 ? 8.643   59.402  -90.764  1.00 20.01 ? 122 LYS F CE  1 
ATOM   9360  N NZ  . LYS F 1 122 ? 9.746   58.974  -91.633  1.00 19.76 ? 122 LYS F NZ  1 
ATOM   9361  N N   . SER F 1 123 ? 5.563   59.772  -84.802  1.00 26.34 ? 123 SER F N   1 
ATOM   9362  C CA  . SER F 1 123 ? 5.141   58.809  -83.783  1.00 27.55 ? 123 SER F CA  1 
ATOM   9363  C C   . SER F 1 123 ? 3.741   58.277  -84.031  1.00 28.29 ? 123 SER F C   1 
ATOM   9364  O O   . SER F 1 123 ? 2.900   59.005  -84.568  1.00 28.74 ? 123 SER F O   1 
ATOM   9365  C CB  . SER F 1 123 ? 5.180   59.463  -82.418  1.00 29.33 ? 123 SER F CB  1 
ATOM   9366  O OG  . SER F 1 123 ? 5.532   58.516  -81.464  1.00 31.28 ? 123 SER F OG  1 
ATOM   9367  N N   . PRO F 1 124 ? 3.427   57.120  -83.412  1.00 28.65 ? 124 PRO F N   1 
ATOM   9368  C CA  . PRO F 1 124 ? 3.106   55.772  -83.906  1.00 27.89 ? 124 PRO F CA  1 
ATOM   9369  C C   . PRO F 1 124 ? 3.176   55.737  -85.406  1.00 28.52 ? 124 PRO F C   1 
ATOM   9370  O O   . PRO F 1 124 ? 2.775   56.697  -86.060  1.00 30.36 ? 124 PRO F O   1 
ATOM   9371  C CB  . PRO F 1 124 ? 1.663   55.556  -83.434  1.00 27.61 ? 124 PRO F CB  1 
ATOM   9372  C CG  . PRO F 1 124 ? 1.140   56.919  -83.212  1.00 27.11 ? 124 PRO F CG  1 
ATOM   9373  C CD  . PRO F 1 124 ? 2.328   57.548  -82.525  1.00 28.17 ? 124 PRO F CD  1 
ATOM   9374  N N   . GLY F 1 125 ? 3.646   54.661  -85.993  1.00 28.11 ? 125 GLY F N   1 
ATOM   9375  C CA  . GLY F 1 125 ? 3.669   54.670  -87.456  1.00 28.59 ? 125 GLY F CA  1 
ATOM   9376  C C   . GLY F 1 125 ? 2.410   54.088  -88.071  1.00 27.98 ? 125 GLY F C   1 
ATOM   9377  O O   . GLY F 1 125 ? 2.508   53.368  -89.044  1.00 26.85 ? 125 GLY F O   1 
ATOM   9378  N N   . TRP F 1 126 ? 1.225   54.378  -87.530  1.00 28.63 ? 126 TRP F N   1 
ATOM   9379  C CA  . TRP F 1 126 ? 0.071   53.545  -87.845  1.00 28.44 ? 126 TRP F CA  1 
ATOM   9380  C C   . TRP F 1 126 ? -1.349  54.129  -87.740  1.00 30.07 ? 126 TRP F C   1 
ATOM   9381  O O   . TRP F 1 126 ? -1.611  55.140  -87.076  1.00 28.41 ? 126 TRP F O   1 
ATOM   9382  C CB  . TRP F 1 126 ? 0.154   52.254  -87.022  1.00 27.55 ? 126 TRP F CB  1 
ATOM   9383  C CG  . TRP F 1 126 ? 0.063   52.383  -85.513  1.00 26.57 ? 126 TRP F CG  1 
ATOM   9384  C CD1 . TRP F 1 126 ? -0.720  53.260  -84.789  1.00 26.47 ? 126 TRP F CD1 1 
ATOM   9385  C CD2 . TRP F 1 126 ? 0.719   51.561  -84.542  1.00 27.08 ? 126 TRP F CD2 1 
ATOM   9386  N NE1 . TRP F 1 126 ? -0.560  53.058  -83.443  1.00 26.24 ? 126 TRP F NE1 1 
ATOM   9387  C CE2 . TRP F 1 126 ? 0.317   52.022  -83.254  1.00 26.96 ? 126 TRP F CE2 1 
ATOM   9388  C CE3 . TRP F 1 126 ? 1.620   50.497  -84.621  1.00 26.69 ? 126 TRP F CE3 1 
ATOM   9389  C CZ2 . TRP F 1 126 ? 0.779   51.447  -82.071  1.00 25.89 ? 126 TRP F CZ2 1 
ATOM   9390  C CZ3 . TRP F 1 126 ? 2.085   49.925  -83.431  1.00 26.36 ? 126 TRP F CZ3 1 
ATOM   9391  C CH2 . TRP F 1 126 ? 1.655   50.406  -82.177  1.00 26.29 ? 126 TRP F CH2 1 
ATOM   9392  N N   . ASP F 1 127 ? -2.258  53.434  -88.439  1.00 32.64 ? 127 ASP F N   1 
ATOM   9393  C CA  . ASP F 1 127 ? -3.696  53.690  -88.383  1.00 33.32 ? 127 ASP F CA  1 
ATOM   9394  C C   . ASP F 1 127 ? -4.407  53.059  -87.196  1.00 31.50 ? 127 ASP F C   1 
ATOM   9395  O O   . ASP F 1 127 ? -5.608  53.276  -87.029  1.00 33.95 ? 127 ASP F O   1 
ATOM   9396  C CB  . ASP F 1 127 ? -4.351  53.231  -89.699  1.00 36.78 ? 127 ASP F CB  1 
ATOM   9397  C CG  . ASP F 1 127 ? -3.968  54.152  -90.890  1.00 41.42 ? 127 ASP F CG  1 
ATOM   9398  O OD1 . ASP F 1 127 ? -3.634  55.357  -90.688  1.00 42.87 ? 127 ASP F OD1 1 
ATOM   9399  O OD2 . ASP F 1 127 ? -4.052  53.709  -92.078  1.00 44.39 ? 127 ASP F OD2 1 
ATOM   9400  N N   . TRP F 1 128 ? -3.701  52.295  -86.358  1.00 28.51 ? 128 TRP F N   1 
ATOM   9401  C CA  . TRP F 1 128 ? -4.343  51.590  -85.235  1.00 26.46 ? 128 TRP F CA  1 
ATOM   9402  C C   . TRP F 1 128 ? -4.924  52.533  -84.181  1.00 24.80 ? 128 TRP F C   1 
ATOM   9403  O O   . TRP F 1 128 ? -5.884  52.191  -83.509  1.00 23.67 ? 128 TRP F O   1 
ATOM   9404  C CB  . TRP F 1 128 ? -3.364  50.611  -84.583  1.00 26.17 ? 128 TRP F CB  1 
ATOM   9405  C CG  . TRP F 1 128 ? -2.898  49.495  -85.487  1.00 26.08 ? 128 TRP F CG  1 
ATOM   9406  C CD1 . TRP F 1 128 ? -3.415  49.176  -86.697  1.00 26.47 ? 128 TRP F CD1 1 
ATOM   9407  C CD2 . TRP F 1 128 ? -1.874  48.513  -85.218  1.00 25.51 ? 128 TRP F CD2 1 
ATOM   9408  N NE1 . TRP F 1 128 ? -2.770  48.069  -87.214  1.00 26.23 ? 128 TRP F NE1 1 
ATOM   9409  C CE2 . TRP F 1 128 ? -1.824  47.644  -86.326  1.00 25.15 ? 128 TRP F CE2 1 
ATOM   9410  C CE3 . TRP F 1 128 ? -1.008  48.284  -84.150  1.00 25.89 ? 128 TRP F CE3 1 
ATOM   9411  C CZ2 . TRP F 1 128 ? -0.922  46.585  -86.419  1.00 25.10 ? 128 TRP F CZ2 1 
ATOM   9412  C CZ3 . TRP F 1 128 ? -0.098  47.225  -84.243  1.00 25.91 ? 128 TRP F CZ3 1 
ATOM   9413  C CH2 . TRP F 1 128 ? -0.072  46.386  -85.370  1.00 25.06 ? 128 TRP F CH2 1 
ATOM   9414  N N   . THR F 1 129 ? -4.316  53.703  -84.042  1.00 23.52 ? 129 THR F N   1 
ATOM   9415  C CA  . THR F 1 129 ? -4.813  54.788  -83.213  1.00 24.25 ? 129 THR F CA  1 
ATOM   9416  C C   . THR F 1 129 ? -4.740  56.040  -84.060  1.00 25.07 ? 129 THR F C   1 
ATOM   9417  O O   . THR F 1 129 ? -3.997  56.052  -85.029  1.00 27.55 ? 129 THR F O   1 
ATOM   9418  C CB  . THR F 1 129 ? -3.922  54.996  -81.953  1.00 24.52 ? 129 THR F CB  1 
ATOM   9419  O OG1 . THR F 1 129 ? -2.568  55.341  -82.323  1.00 23.98 ? 129 THR F OG1 1 
ATOM   9420  C CG2 . THR F 1 129 ? -3.913  53.748  -81.082  1.00 24.26 ? 129 THR F CG2 1 
ATOM   9421  N N   . ASP F 1 130 ? -5.478  57.094  -83.741  1.00 25.06 ? 130 ASP F N   1 
ATOM   9422  C CA  . ASP F 1 130 ? -5.084  58.407  -84.263  1.00 26.92 ? 130 ASP F CA  1 
ATOM   9423  C C   . ASP F 1 130 ? -5.229  59.517  -83.238  1.00 27.15 ? 130 ASP F C   1 
ATOM   9424  O O   . ASP F 1 130 ? -6.211  60.243  -83.171  1.00 27.50 ? 130 ASP F O   1 
ATOM   9425  C CB  . ASP F 1 130 ? -5.652  58.716  -85.680  1.00 28.72 ? 130 ASP F CB  1 
ATOM   9426  C CG  . ASP F 1 130 ? -6.900  59.605  -85.679  1.00 29.85 ? 130 ASP F CG  1 
ATOM   9427  O OD1 . ASP F 1 130 ? -7.948  59.143  -85.197  1.00 32.42 ? 130 ASP F OD1 1 
ATOM   9428  O OD2 . ASP F 1 130 ? -6.852  60.753  -86.188  1.00 28.43 ? 130 ASP F OD2 1 
ATOM   9429  N N   . TYR F 1 131 ? -4.220  59.568  -82.384  1.00 27.46 ? 131 TYR F N   1 
ATOM   9430  C CA  . TYR F 1 131 ? -3.911  60.724  -81.568  1.00 26.47 ? 131 TYR F CA  1 
ATOM   9431  C C   . TYR F 1 131 ? -2.850  61.523  -82.321  1.00 25.95 ? 131 TYR F C   1 
ATOM   9432  O O   . TYR F 1 131 ? -2.117  60.962  -83.126  1.00 28.15 ? 131 TYR F O   1 
ATOM   9433  C CB  . TYR F 1 131 ? -3.341  60.278  -80.228  1.00 26.28 ? 131 TYR F CB  1 
ATOM   9434  C CG  . TYR F 1 131 ? -4.239  59.388  -79.390  1.00 26.42 ? 131 TYR F CG  1 
ATOM   9435  C CD1 . TYR F 1 131 ? -5.171  59.934  -78.514  1.00 25.83 ? 131 TYR F CD1 1 
ATOM   9436  C CD2 . TYR F 1 131 ? -4.131  57.996  -79.440  1.00 26.16 ? 131 TYR F CD2 1 
ATOM   9437  C CE1 . TYR F 1 131 ? -5.964  59.130  -77.709  1.00 25.49 ? 131 TYR F CE1 1 
ATOM   9438  C CE2 . TYR F 1 131 ? -4.942  57.188  -78.652  1.00 25.37 ? 131 TYR F CE2 1 
ATOM   9439  C CZ  . TYR F 1 131 ? -5.841  57.760  -77.782  1.00 24.90 ? 131 TYR F CZ  1 
ATOM   9440  O OH  . TYR F 1 131 ? -6.636  56.943  -77.025  1.00 24.77 ? 131 TYR F OH  1 
ATOM   9441  N N   . PRO F 1 132 ? -2.746  62.826  -82.062  1.00 24.50 ? 132 PRO F N   1 
ATOM   9442  C CA  . PRO F 1 132 ? -1.645  63.560  -82.681  1.00 24.61 ? 132 PRO F CA  1 
ATOM   9443  C C   . PRO F 1 132 ? -0.288  63.162  -82.096  1.00 23.91 ? 132 PRO F C   1 
ATOM   9444  O O   . PRO F 1 132 ? -0.240  62.538  -81.046  1.00 25.88 ? 132 PRO F O   1 
ATOM   9445  C CB  . PRO F 1 132 ? -1.956  65.015  -82.318  1.00 25.16 ? 132 PRO F CB  1 
ATOM   9446  C CG  . PRO F 1 132 ? -2.738  64.914  -81.052  1.00 24.72 ? 132 PRO F CG  1 
ATOM   9447  C CD  . PRO F 1 132 ? -3.558  63.676  -81.180  1.00 24.09 ? 132 PRO F CD  1 
ATOM   9448  N N   . PRO F 1 133 ? 0.811   63.519  -82.768  1.00 22.56 ? 133 PRO F N   1 
ATOM   9449  C CA  . PRO F 1 133 ? 2.110   63.303  -82.124  1.00 21.84 ? 133 PRO F CA  1 
ATOM   9450  C C   . PRO F 1 133 ? 2.400   64.406  -81.108  1.00 21.20 ? 133 PRO F C   1 
ATOM   9451  O O   . PRO F 1 133 ? 1.946   65.532  -81.285  1.00 23.59 ? 133 PRO F O   1 
ATOM   9452  C CB  . PRO F 1 133 ? 3.096   63.348  -83.296  1.00 21.57 ? 133 PRO F CB  1 
ATOM   9453  C CG  . PRO F 1 133 ? 2.373   64.032  -84.422  1.00 21.43 ? 133 PRO F CG  1 
ATOM   9454  C CD  . PRO F 1 133 ? 0.939   64.238  -84.046  1.00 21.98 ? 133 PRO F CD  1 
ATOM   9455  N N   . PRO F 1 134 ? 3.138   64.106  -80.040  1.00 20.38 ? 134 PRO F N   1 
ATOM   9456  C CA  . PRO F 1 134 ? 3.356   65.147  -79.037  1.00 20.05 ? 134 PRO F CA  1 
ATOM   9457  C C   . PRO F 1 134 ? 4.503   66.083  -79.381  1.00 19.62 ? 134 PRO F C   1 
ATOM   9458  O O   . PRO F 1 134 ? 5.409   65.693  -80.105  1.00 19.66 ? 134 PRO F O   1 
ATOM   9459  C CB  . PRO F 1 134 ? 3.702   64.349  -77.768  1.00 20.05 ? 134 PRO F CB  1 
ATOM   9460  C CG  . PRO F 1 134 ? 4.078   62.977  -78.229  1.00 20.00 ? 134 PRO F CG  1 
ATOM   9461  C CD  . PRO F 1 134 ? 3.891   62.885  -79.720  1.00 20.26 ? 134 PRO F CD  1 
ATOM   9462  N N   . PRO F 1 135 ? 4.487   67.313  -78.844  1.00 19.07 ? 135 PRO F N   1 
ATOM   9463  C CA  . PRO F 1 135 ? 5.643   68.202  -78.986  1.00 19.27 ? 135 PRO F CA  1 
ATOM   9464  C C   . PRO F 1 135 ? 6.864   67.677  -78.231  1.00 19.65 ? 135 PRO F C   1 
ATOM   9465  O O   . PRO F 1 135 ? 6.730   66.740  -77.436  1.00 21.14 ? 135 PRO F O   1 
ATOM   9466  C CB  . PRO F 1 135 ? 5.142   69.507  -78.373  1.00 19.14 ? 135 PRO F CB  1 
ATOM   9467  C CG  . PRO F 1 135 ? 4.135   69.084  -77.380  1.00 19.28 ? 135 PRO F CG  1 
ATOM   9468  C CD  . PRO F 1 135 ? 3.429   67.935  -78.038  1.00 19.28 ? 135 PRO F CD  1 
ATOM   9469  N N   . VAL F 1 136 ? 8.037   68.267  -78.472  1.00 20.00 ? 136 VAL F N   1 
ATOM   9470  C CA  . VAL F 1 136 ? 9.281   67.786  -77.864  1.00 19.85 ? 136 VAL F CA  1 
ATOM   9471  C C   . VAL F 1 136 ? 10.037  68.923  -77.212  1.00 20.17 ? 136 VAL F C   1 
ATOM   9472  O O   . VAL F 1 136 ? 10.158  69.999  -77.783  1.00 19.83 ? 136 VAL F O   1 
ATOM   9473  C CB  . VAL F 1 136 ? 10.195  67.105  -78.905  1.00 19.74 ? 136 VAL F CB  1 
ATOM   9474  C CG1 . VAL F 1 136 ? 11.508  66.693  -78.276  1.00 19.63 ? 136 VAL F CG1 1 
ATOM   9475  C CG2 . VAL F 1 136 ? 9.511   65.879  -79.513  1.00 19.67 ? 136 VAL F CG2 1 
ATOM   9476  N N   . LEU F 1 137 ? 10.524  68.678  -76.000  1.00 21.32 ? 137 LEU F N   1 
ATOM   9477  C CA  . LEU F 1 137 ? 11.479  69.552  -75.324  1.00 22.46 ? 137 LEU F CA  1 
ATOM   9478  C C   . LEU F 1 137 ? 12.827  68.833  -75.284  1.00 21.93 ? 137 LEU F C   1 
ATOM   9479  O O   . LEU F 1 137 ? 13.003  67.875  -74.534  1.00 20.74 ? 137 LEU F O   1 
ATOM   9480  C CB  . LEU F 1 137 ? 10.996  69.880  -73.903  1.00 23.53 ? 137 LEU F CB  1 
ATOM   9481  C CG  . LEU F 1 137 ? 12.007  70.558  -72.946  1.00 25.06 ? 137 LEU F CG  1 
ATOM   9482  C CD1 . LEU F 1 137 ? 12.501  71.909  -73.467  1.00 25.35 ? 137 LEU F CD1 1 
ATOM   9483  C CD2 . LEU F 1 137 ? 11.432  70.726  -71.551  1.00 25.27 ? 137 LEU F CD2 1 
ATOM   9484  N N   . LEU F 1 138 ? 13.767  69.296  -76.101  1.00 22.53 ? 138 LEU F N   1 
ATOM   9485  C CA  . LEU F 1 138 ? 15.119  68.739  -76.123  1.00 22.98 ? 138 LEU F CA  1 
ATOM   9486  C C   . LEU F 1 138 ? 15.939  69.437  -75.062  1.00 22.96 ? 138 LEU F C   1 
ATOM   9487  O O   . LEU F 1 138 ? 16.043  70.655  -75.074  1.00 23.16 ? 138 LEU F O   1 
ATOM   9488  C CB  . LEU F 1 138 ? 15.777  68.938  -77.487  1.00 23.21 ? 138 LEU F CB  1 
ATOM   9489  C CG  . LEU F 1 138 ? 17.212  68.416  -77.586  1.00 23.97 ? 138 LEU F CG  1 
ATOM   9490  C CD1 . LEU F 1 138 ? 17.265  66.924  -77.309  1.00 24.97 ? 138 LEU F CD1 1 
ATOM   9491  C CD2 . LEU F 1 138 ? 17.799  68.706  -78.949  1.00 23.75 ? 138 LEU F CD2 1 
ATOM   9492  N N   . ILE F 1 139 ? 16.516  68.662  -74.147  1.00 22.81 ? 139 ILE F N   1 
ATOM   9493  C CA  . ILE F 1 139 ? 17.347  69.212  -73.075  1.00 22.16 ? 139 ILE F CA  1 
ATOM   9494  C C   . ILE F 1 139 ? 18.797  68.805  -73.276  1.00 22.53 ? 139 ILE F C   1 
ATOM   9495  O O   . ILE F 1 139 ? 19.126  67.630  -73.335  1.00 22.60 ? 139 ILE F O   1 
ATOM   9496  C CB  . ILE F 1 139 ? 16.872  68.775  -71.666  1.00 20.91 ? 139 ILE F CB  1 
ATOM   9497  C CG1 . ILE F 1 139 ? 15.427  69.228  -71.444  1.00 20.23 ? 139 ILE F CG1 1 
ATOM   9498  C CG2 . ILE F 1 139 ? 17.765  69.379  -70.589  1.00 20.77 ? 139 ILE F CG2 1 
ATOM   9499  C CD1 . ILE F 1 139 ? 14.845  68.820  -70.125  1.00 20.13 ? 139 ILE F CD1 1 
ATOM   9500  N N   . SER F 1 140 ? 19.660  69.796  -73.379  1.00 22.93 ? 140 SER F N   1 
ATOM   9501  C CA  . SER F 1 140 ? 21.081  69.556  -73.459  1.00 23.39 ? 140 SER F CA  1 
ATOM   9502  C C   . SER F 1 140 ? 21.606  69.372  -72.041  1.00 23.75 ? 140 SER F C   1 
ATOM   9503  O O   . SER F 1 140 ? 21.229  70.119  -71.146  1.00 24.71 ? 140 SER F O   1 
ATOM   9504  C CB  . SER F 1 140 ? 21.751  70.750  -74.115  1.00 23.96 ? 140 SER F CB  1 
ATOM   9505  O OG  . SER F 1 140 ? 22.314  71.634  -73.167  1.00 24.06 ? 140 SER F OG  1 
ATOM   9506  N N   . PRO F 1 141 ? 22.473  68.366  -71.820  1.00 23.21 ? 141 PRO F N   1 
ATOM   9507  C CA  . PRO F 1 141 ? 23.050  68.173  -70.495  1.00 23.16 ? 141 PRO F CA  1 
ATOM   9508  C C   . PRO F 1 141 ? 24.134  69.193  -70.195  1.00 24.44 ? 141 PRO F C   1 
ATOM   9509  O O   . PRO F 1 141 ? 24.609  69.879  -71.102  1.00 24.35 ? 141 PRO F O   1 
ATOM   9510  C CB  . PRO F 1 141 ? 23.666  66.787  -70.581  1.00 22.44 ? 141 PRO F CB  1 
ATOM   9511  C CG  . PRO F 1 141 ? 24.075  66.664  -71.998  1.00 22.76 ? 141 PRO F CG  1 
ATOM   9512  C CD  . PRO F 1 141 ? 23.058  67.441  -72.801  1.00 22.74 ? 141 PRO F CD  1 
ATOM   9513  N N   . PRO F 1 142 ? 24.531  69.302  -68.924  1.00 25.68 ? 142 PRO F N   1 
ATOM   9514  C CA  . PRO F 1 142 ? 25.585  70.240  -68.596  1.00 26.29 ? 142 PRO F CA  1 
ATOM   9515  C C   . PRO F 1 142 ? 26.933  69.696  -69.024  1.00 27.92 ? 142 PRO F C   1 
ATOM   9516  O O   . PRO F 1 142 ? 27.036  68.533  -69.399  1.00 26.82 ? 142 PRO F O   1 
ATOM   9517  C CB  . PRO F 1 142 ? 25.502  70.341  -67.076  1.00 25.74 ? 142 PRO F CB  1 
ATOM   9518  C CG  . PRO F 1 142 ? 24.972  69.025  -66.644  1.00 25.26 ? 142 PRO F CG  1 
ATOM   9519  C CD  . PRO F 1 142 ? 24.046  68.576  -67.738  1.00 25.37 ? 142 PRO F CD  1 
ATOM   9520  N N   . PRO F 1 143 ? 27.966  70.538  -68.988  1.00 31.08 ? 143 PRO F N   1 
ATOM   9521  C CA  . PRO F 1 143 ? 29.293  70.023  -69.282  1.00 30.83 ? 143 PRO F CA  1 
ATOM   9522  C C   . PRO F 1 143 ? 29.698  68.988  -68.282  1.00 30.47 ? 143 PRO F C   1 
ATOM   9523  O O   . PRO F 1 143 ? 29.280  69.048  -67.110  1.00 28.46 ? 143 PRO F O   1 
ATOM   9524  C CB  . PRO F 1 143 ? 30.194  71.254  -69.135  1.00 32.16 ? 143 PRO F CB  1 
ATOM   9525  C CG  . PRO F 1 143 ? 29.290  72.423  -69.389  1.00 32.57 ? 143 PRO F CG  1 
ATOM   9526  C CD  . PRO F 1 143 ? 27.946  72.010  -68.864  1.00 32.56 ? 143 PRO F CD  1 
ATOM   9527  N N   . LEU F 1 144 ? 30.510  68.046  -68.750  1.00 32.44 ? 144 LEU F N   1 
ATOM   9528  C CA  . LEU F 1 144 ? 31.097  67.040  -67.888  1.00 34.82 ? 144 LEU F CA  1 
ATOM   9529  C C   . LEU F 1 144 ? 31.955  67.716  -66.825  1.00 36.28 ? 144 LEU F C   1 
ATOM   9530  O O   . LEU F 1 144 ? 32.359  68.883  -66.975  1.00 35.27 ? 144 LEU F O   1 
ATOM   9531  C CB  . LEU F 1 144 ? 31.997  66.110  -68.690  1.00 35.33 ? 144 LEU F CB  1 
ATOM   9532  C CG  . LEU F 1 144 ? 31.415  65.301  -69.839  1.00 35.65 ? 144 LEU F CG  1 
ATOM   9533  C CD1 . LEU F 1 144 ? 32.518  64.712  -70.700  1.00 35.32 ? 144 LEU F CD1 1 
ATOM   9534  C CD2 . LEU F 1 144 ? 30.530  64.207  -69.288  1.00 37.82 ? 144 LEU F CD2 1 
ATOM   9535  N N   . GLY F 1 145 ? 32.251  66.958  -65.772  1.00 38.05 ? 145 GLY F N   1 
ATOM   9536  C CA  . GLY F 1 145 ? 33.182  67.395  -64.746  1.00 38.05 ? 145 GLY F CA  1 
ATOM   9537  C C   . GLY F 1 145 ? 34.577  67.549  -65.302  1.00 37.82 ? 145 GLY F C   1 
ATOM   9538  O O   . GLY F 1 145 ? 34.945  66.882  -66.264  1.00 39.51 ? 145 GLY F O   1 
ATOM   9539  N N   . GLU F 1 146 ? 35.354  68.430  -64.696  1.00 39.37 ? 146 GLU F N   1 
ATOM   9540  C CA  . GLU F 1 146 ? 36.747  68.632  -65.105  1.00 40.15 ? 146 GLU F CA  1 
ATOM   9541  C C   . GLU F 1 146 ? 37.589  67.457  -64.689  1.00 37.85 ? 146 GLU F C   1 
ATOM   9542  O O   . GLU F 1 146 ? 38.613  67.205  -65.292  1.00 35.01 ? 146 GLU F O   1 
ATOM   9543  C CB  . GLU F 1 146 ? 37.337  69.917  -64.485  1.00 43.40 ? 146 GLU F CB  1 
ATOM   9544  C CG  . GLU F 1 146 ? 36.628  71.208  -64.826  1.00 47.32 ? 146 GLU F CG  1 
ATOM   9545  C CD  . GLU F 1 146 ? 37.427  72.147  -65.724  1.00 50.54 ? 146 GLU F CD  1 
ATOM   9546  O OE1 . GLU F 1 146 ? 36.971  73.292  -65.894  1.00 50.66 ? 146 GLU F OE1 1 
ATOM   9547  O OE2 . GLU F 1 146 ? 38.482  71.719  -66.257  1.00 53.40 ? 146 GLU F OE2 1 
ATOM   9548  N N   . THR F 1 147 ? 37.151  66.734  -63.658  1.00 38.67 ? 147 THR F N   1 
ATOM   9549  C CA  . THR F 1 147 ? 37.896  65.591  -63.129  1.00 38.67 ? 147 THR F CA  1 
ATOM   9550  C C   . THR F 1 147 ? 37.038  64.331  -63.063  1.00 37.64 ? 147 THR F C   1 
ATOM   9551  O O   . THR F 1 147 ? 36.117  64.207  -62.240  1.00 41.39 ? 147 THR F O   1 
ATOM   9552  C CB  . THR F 1 147 ? 38.437  65.898  -61.721  1.00 38.98 ? 147 THR F CB  1 
ATOM   9553  O OG1 . THR F 1 147 ? 39.215  67.100  -61.776  1.00 41.73 ? 147 THR F OG1 1 
ATOM   9554  C CG2 . THR F 1 147 ? 39.268  64.740  -61.194  1.00 37.12 ? 147 THR F CG2 1 
ATOM   9555  N N   . ILE F 1 148 ? 37.359  63.380  -63.926  1.00 35.27 ? 148 ILE F N   1 
ATOM   9556  C CA  . ILE F 1 148 ? 36.561  62.181  -64.080  1.00 33.85 ? 148 ILE F CA  1 
ATOM   9557  C C   . ILE F 1 148 ? 37.269  60.996  -63.424  1.00 31.19 ? 148 ILE F C   1 
ATOM   9558  O O   . ILE F 1 148 ? 38.492  60.881  -63.470  1.00 28.47 ? 148 ILE F O   1 
ATOM   9559  C CB  . ILE F 1 148 ? 36.278  61.940  -65.582  1.00 34.69 ? 148 ILE F CB  1 
ATOM   9560  C CG1 . ILE F 1 148 ? 35.415  63.098  -66.120  1.00 34.04 ? 148 ILE F CG1 1 
ATOM   9561  C CG2 . ILE F 1 148 ? 35.600  60.587  -65.810  1.00 35.15 ? 148 ILE F CG2 1 
ATOM   9562  C CD1 . ILE F 1 148 ? 35.447  63.231  -67.626  1.00 34.89 ? 148 ILE F CD1 1 
ATOM   9563  N N   . ASP F 1 149 ? 36.488  60.125  -62.796  1.00 30.80 ? 149 ASP F N   1 
ATOM   9564  C CA  . ASP F 1 149 ? 37.029  58.946  -62.135  1.00 30.01 ? 149 ASP F CA  1 
ATOM   9565  C C   . ASP F 1 149 ? 38.035  58.282  -63.071  1.00 29.94 ? 149 ASP F C   1 
ATOM   9566  O O   . ASP F 1 149 ? 37.723  58.034  -64.235  1.00 28.36 ? 149 ASP F O   1 
ATOM   9567  C CB  . ASP F 1 149 ? 35.901  57.974  -61.782  1.00 30.01 ? 149 ASP F CB  1 
ATOM   9568  C CG  . ASP F 1 149 ? 36.340  56.875  -60.850  1.00 29.80 ? 149 ASP F CG  1 
ATOM   9569  O OD1 . ASP F 1 149 ? 37.305  56.169  -61.190  1.00 29.86 ? 149 ASP F OD1 1 
ATOM   9570  O OD2 . ASP F 1 149 ? 35.688  56.696  -59.790  1.00 30.45 ? 149 ASP F OD2 1 
ATOM   9571  N N   . PRO F 1 150 ? 39.265  58.027  -62.581  1.00 30.58 ? 150 PRO F N   1 
ATOM   9572  C CA  . PRO F 1 150 ? 40.320  57.398  -63.377  1.00 29.94 ? 150 PRO F CA  1 
ATOM   9573  C C   . PRO F 1 150 ? 39.926  56.138  -64.142  1.00 30.58 ? 150 PRO F C   1 
ATOM   9574  O O   . PRO F 1 150 ? 40.489  55.903  -65.213  1.00 31.64 ? 150 PRO F O   1 
ATOM   9575  C CB  . PRO F 1 150 ? 41.383  57.074  -62.326  1.00 28.86 ? 150 PRO F CB  1 
ATOM   9576  C CG  . PRO F 1 150 ? 41.266  58.208  -61.397  1.00 28.35 ? 150 PRO F CG  1 
ATOM   9577  C CD  . PRO F 1 150 ? 39.819  58.578  -61.329  1.00 29.11 ? 150 PRO F CD  1 
ATOM   9578  N N   . LEU F 1 151 ? 38.990  55.338  -63.614  1.00 31.43 ? 151 LEU F N   1 
ATOM   9579  C CA  . LEU F 1 151 ? 38.478  54.182  -64.358  1.00 32.14 ? 151 LEU F CA  1 
ATOM   9580  C C   . LEU F 1 151 ? 37.757  54.589  -65.657  1.00 32.29 ? 151 LEU F C   1 
ATOM   9581  O O   . LEU F 1 151 ? 37.861  53.904  -66.659  1.00 33.92 ? 151 LEU F O   1 
ATOM   9582  C CB  . LEU F 1 151 ? 37.515  53.376  -63.493  1.00 33.06 ? 151 LEU F CB  1 
ATOM   9583  C CG  . LEU F 1 151 ? 38.114  52.460  -62.438  1.00 34.58 ? 151 LEU F CG  1 
ATOM   9584  C CD1 . LEU F 1 151 ? 37.548  52.788  -61.059  1.00 34.70 ? 151 LEU F CD1 1 
ATOM   9585  C CD2 . LEU F 1 151 ? 37.872  50.993  -62.815  1.00 35.26 ? 151 LEU F CD2 1 
ATOM   9586  N N   . ALA F 1 152 ? 37.034  55.708  -65.622  1.00 30.75 ? 152 ALA F N   1 
ATOM   9587  C CA  . ALA F 1 152 ? 36.231  56.167  -66.751  1.00 28.54 ? 152 ALA F CA  1 
ATOM   9588  C C   . ALA F 1 152 ? 36.926  57.213  -67.636  1.00 27.23 ? 152 ALA F C   1 
ATOM   9589  O O   . ALA F 1 152 ? 36.548  57.398  -68.779  1.00 27.06 ? 152 ALA F O   1 
ATOM   9590  C CB  . ALA F 1 152 ? 34.908  56.719  -66.226  1.00 28.49 ? 152 ALA F CB  1 
ATOM   9591  N N   . ALA F 1 153 ? 37.939  57.895  -67.116  1.00 26.66 ? 153 ALA F N   1 
ATOM   9592  C CA  . ALA F 1 153 ? 38.588  58.982  -67.859  1.00 26.80 ? 153 ALA F CA  1 
ATOM   9593  C C   . ALA F 1 153 ? 39.068  58.631  -69.288  1.00 27.17 ? 153 ALA F C   1 
ATOM   9594  O O   . ALA F 1 153 ? 38.855  59.424  -70.213  1.00 26.09 ? 153 ALA F O   1 
ATOM   9595  C CB  . ALA F 1 153 ? 39.730  59.546  -67.049  1.00 27.50 ? 153 ALA F CB  1 
ATOM   9596  N N   . PRO F 1 154 ? 39.698  57.454  -69.484  1.00 28.89 ? 154 PRO F N   1 
ATOM   9597  C CA  . PRO F 1 154 ? 40.165  57.096  -70.842  1.00 30.21 ? 154 PRO F CA  1 
ATOM   9598  C C   . PRO F 1 154 ? 39.059  57.106  -71.895  1.00 32.33 ? 154 PRO F C   1 
ATOM   9599  O O   . PRO F 1 154 ? 39.311  57.385  -73.062  1.00 34.74 ? 154 PRO F O   1 
ATOM   9600  C CB  . PRO F 1 154 ? 40.697  55.663  -70.677  1.00 28.97 ? 154 PRO F CB  1 
ATOM   9601  C CG  . PRO F 1 154 ? 40.994  55.519  -69.223  1.00 29.03 ? 154 PRO F CG  1 
ATOM   9602  C CD  . PRO F 1 154 ? 40.000  56.390  -68.502  1.00 28.79 ? 154 PRO F CD  1 
ATOM   9603  N N   . ILE F 1 155 ? 37.848  56.785  -71.459  1.00 32.23 ? 155 ILE F N   1 
ATOM   9604  C CA  . ILE F 1 155 ? 36.657  56.705  -72.293  1.00 31.43 ? 155 ILE F CA  1 
ATOM   9605  C C   . ILE F 1 155 ? 35.990  58.082  -72.526  1.00 29.10 ? 155 ILE F C   1 
ATOM   9606  O O   . ILE F 1 155 ? 35.126  58.195  -73.373  1.00 27.29 ? 155 ILE F O   1 
ATOM   9607  C CB  . ILE F 1 155 ? 35.728  55.612  -71.650  1.00 33.51 ? 155 ILE F CB  1 
ATOM   9608  C CG1 . ILE F 1 155 ? 36.031  54.272  -72.315  1.00 36.03 ? 155 ILE F CG1 1 
ATOM   9609  C CG2 . ILE F 1 155 ? 34.239  55.953  -71.644  1.00 32.85 ? 155 ILE F CG2 1 
ATOM   9610  C CD1 . ILE F 1 155 ? 35.441  53.070  -71.596  1.00 39.58 ? 155 ILE F CD1 1 
ATOM   9611  N N   . PHE F 1 156 ? 36.418  59.121  -71.804  1.00 28.44 ? 156 PHE F N   1 
ATOM   9612  C CA  . PHE F 1 156 ? 35.888  60.494  -71.978  1.00 27.78 ? 156 PHE F CA  1 
ATOM   9613  C C   . PHE F 1 156 ? 36.938  61.519  -72.422  1.00 27.10 ? 156 PHE F C   1 
ATOM   9614  O O   . PHE F 1 156 ? 36.804  62.702  -72.134  1.00 26.48 ? 156 PHE F O   1 
ATOM   9615  C CB  . PHE F 1 156 ? 35.188  60.979  -70.691  1.00 27.38 ? 156 PHE F CB  1 
ATOM   9616  C CG  . PHE F 1 156 ? 33.845  60.344  -70.476  1.00 28.57 ? 156 PHE F CG  1 
ATOM   9617  C CD1 . PHE F 1 156 ? 32.737  60.753  -71.207  1.00 28.37 ? 156 PHE F CD1 1 
ATOM   9618  C CD2 . PHE F 1 156 ? 33.691  59.311  -69.565  1.00 29.17 ? 156 PHE F CD2 1 
ATOM   9619  C CE1 . PHE F 1 156 ? 31.505  60.153  -71.015  1.00 27.54 ? 156 PHE F CE1 1 
ATOM   9620  C CE2 . PHE F 1 156 ? 32.456  58.710  -69.371  1.00 27.90 ? 156 PHE F CE2 1 
ATOM   9621  C CZ  . PHE F 1 156 ? 31.362  59.137  -70.092  1.00 27.63 ? 156 PHE F CZ  1 
ATOM   9622  N N   . VAL F 1 157 ? 37.953  61.069  -73.148  1.00 27.39 ? 157 VAL F N   1 
ATOM   9623  C CA  . VAL F 1 157 ? 38.969  61.981  -73.681  1.00 27.52 ? 157 VAL F CA  1 
ATOM   9624  C C   . VAL F 1 157 ? 38.305  62.869  -74.735  1.00 27.17 ? 157 VAL F C   1 
ATOM   9625  O O   . VAL F 1 157 ? 37.483  62.400  -75.513  1.00 27.84 ? 157 VAL F O   1 
ATOM   9626  C CB  . VAL F 1 157 ? 40.203  61.207  -74.249  1.00 26.78 ? 157 VAL F CB  1 
ATOM   9627  C CG1 . VAL F 1 157 ? 41.150  62.139  -74.988  1.00 26.20 ? 157 VAL F CG1 1 
ATOM   9628  C CG2 . VAL F 1 157 ? 40.940  60.486  -73.124  1.00 25.92 ? 157 VAL F CG2 1 
ATOM   9629  N N   . ASP F 1 158 ? 38.638  64.156  -74.712  1.00 27.71 ? 158 ASP F N   1 
ATOM   9630  C CA  . ASP F 1 158 ? 37.971  65.183  -75.534  1.00 28.30 ? 158 ASP F CA  1 
ATOM   9631  C C   . ASP F 1 158 ? 36.462  65.299  -75.323  1.00 28.91 ? 158 ASP F C   1 
ATOM   9632  O O   . ASP F 1 158 ? 35.780  65.979  -76.086  1.00 30.90 ? 158 ASP F O   1 
ATOM   9633  C CB  . ASP F 1 158 ? 38.250  64.950  -77.013  1.00 27.85 ? 158 ASP F CB  1 
ATOM   9634  C CG  . ASP F 1 158 ? 39.722  64.767  -77.298  1.00 27.25 ? 158 ASP F CG  1 
ATOM   9635  O OD1 . ASP F 1 158 ? 40.527  65.570  -76.797  1.00 25.79 ? 158 ASP F OD1 1 
ATOM   9636  O OD2 . ASP F 1 158 ? 40.071  63.823  -78.030  1.00 26.40 ? 158 ASP F OD2 1 
ATOM   9637  N N   . GLY F 1 159 ? 35.931  64.662  -74.285  1.00 29.75 ? 159 GLY F N   1 
ATOM   9638  C CA  . GLY F 1 159 ? 34.480  64.653  -74.058  1.00 30.73 ? 159 GLY F CA  1 
ATOM   9639  C C   . GLY F 1 159 ? 33.960  65.968  -73.511  1.00 30.82 ? 159 GLY F C   1 
ATOM   9640  O O   . GLY F 1 159 ? 32.851  66.392  -73.839  1.00 30.37 ? 159 GLY F O   1 
ATOM   9641  N N   . LEU F 1 160 ? 34.761  66.602  -72.659  1.00 30.41 ? 160 LEU F N   1 
ATOM   9642  C CA  . LEU F 1 160 ? 34.380  67.847  -72.027  1.00 29.09 ? 160 LEU F CA  1 
ATOM   9643  C C   . LEU F 1 160 ? 34.053  68.915  -73.057  1.00 26.80 ? 160 LEU F C   1 
ATOM   9644  O O   . LEU F 1 160 ? 33.008  69.552  -72.991  1.00 24.81 ? 160 LEU F O   1 
ATOM   9645  C CB  . LEU F 1 160 ? 35.524  68.321  -71.124  1.00 29.89 ? 160 LEU F CB  1 
ATOM   9646  C CG  . LEU F 1 160 ? 35.391  69.690  -70.481  1.00 30.06 ? 160 LEU F CG  1 
ATOM   9647  C CD1 . LEU F 1 160 ? 34.100  69.736  -69.651  1.00 30.57 ? 160 LEU F CD1 1 
ATOM   9648  C CD2 . LEU F 1 160 ? 36.656  69.927  -69.633  1.00 28.99 ? 160 LEU F CD2 1 
ATOM   9649  N N   . ALA F 1 161 ? 34.948  69.095  -74.013  1.00 26.37 ? 161 ALA F N   1 
ATOM   9650  C CA  . ALA F 1 161 ? 34.782  70.136  -75.026  1.00 26.34 ? 161 ALA F CA  1 
ATOM   9651  C C   . ALA F 1 161 ? 33.535  69.867  -75.853  1.00 27.26 ? 161 ALA F C   1 
ATOM   9652  O O   . ALA F 1 161 ? 32.775  70.793  -76.168  1.00 30.74 ? 161 ALA F O   1 
ATOM   9653  C CB  . ALA F 1 161 ? 36.013  70.226  -75.918  1.00 25.49 ? 161 ALA F CB  1 
ATOM   9654  N N   . LYS F 1 162 ? 33.313  68.598  -76.187  1.00 26.71 ? 162 LYS F N   1 
ATOM   9655  C CA  . LYS F 1 162 ? 32.112  68.200  -76.909  1.00 25.70 ? 162 LYS F CA  1 
ATOM   9656  C C   . LYS F 1 162 ? 30.854  68.531  -76.118  1.00 25.53 ? 162 LYS F C   1 
ATOM   9657  O O   . LYS F 1 162 ? 29.900  69.061  -76.678  1.00 24.19 ? 162 LYS F O   1 
ATOM   9658  C CB  . LYS F 1 162 ? 32.138  66.709  -77.217  1.00 24.66 ? 162 LYS F CB  1 
ATOM   9659  C CG  . LYS F 1 162 ? 33.173  66.327  -78.246  1.00 24.30 ? 162 LYS F CG  1 
ATOM   9660  C CD  . LYS F 1 162 ? 33.261  64.824  -78.399  1.00 24.34 ? 162 LYS F CD  1 
ATOM   9661  C CE  . LYS F 1 162 ? 34.525  64.417  -79.131  1.00 24.71 ? 162 LYS F CE  1 
ATOM   9662  N NZ  . LYS F 1 162 ? 34.433  63.035  -79.655  1.00 24.91 ? 162 LYS F NZ  1 
ATOM   9663  N N   . SER F 1 163 ? 30.859  68.221  -74.822  1.00 26.33 ? 163 SER F N   1 
ATOM   9664  C CA  . SER F 1 163 ? 29.696  68.475  -73.980  1.00 26.66 ? 163 SER F CA  1 
ATOM   9665  C C   . SER F 1 163 ? 29.414  69.975  -73.845  1.00 27.13 ? 163 SER F C   1 
ATOM   9666  O O   . SER F 1 163 ? 28.250  70.381  -73.726  1.00 27.57 ? 163 SER F O   1 
ATOM   9667  C CB  . SER F 1 163 ? 29.864  67.829  -72.596  1.00 26.31 ? 163 SER F CB  1 
ATOM   9668  O OG  . SER F 1 163 ? 30.873  68.457  -71.824  1.00 26.58 ? 163 SER F OG  1 
ATOM   9669  N N   . GLU F 1 164 ? 30.467  70.796  -73.874  1.00 26.90 ? 164 GLU F N   1 
ATOM   9670  C CA  . GLU F 1 164 ? 30.293  72.244  -73.798  1.00 26.98 ? 164 GLU F CA  1 
ATOM   9671  C C   . GLU F 1 164 ? 29.615  72.782  -75.053  1.00 26.74 ? 164 GLU F C   1 
ATOM   9672  O O   . GLU F 1 164 ? 28.848  73.740  -74.979  1.00 26.49 ? 164 GLU F O   1 
ATOM   9673  C CB  . GLU F 1 164 ? 31.630  72.950  -73.577  1.00 27.94 ? 164 GLU F CB  1 
ATOM   9674  C CG  . GLU F 1 164 ? 32.064  73.007  -72.117  1.00 28.43 ? 164 GLU F CG  1 
ATOM   9675  C CD  . GLU F 1 164 ? 33.550  73.251  -71.924  1.00 29.26 ? 164 GLU F CD  1 
ATOM   9676  O OE1 . GLU F 1 164 ? 33.998  73.322  -70.767  1.00 32.14 ? 164 GLU F OE1 1 
ATOM   9677  O OE2 . GLU F 1 164 ? 34.284  73.343  -72.922  1.00 29.50 ? 164 GLU F OE2 1 
ATOM   9678  N N   . ALA F 1 165 ? 29.879  72.145  -76.192  1.00 25.95 ? 165 ALA F N   1 
ATOM   9679  C CA  . ALA F 1 165 ? 29.318  72.576  -77.473  1.00 25.54 ? 165 ALA F CA  1 
ATOM   9680  C C   . ALA F 1 165 ? 27.875  72.120  -77.754  1.00 26.46 ? 165 ALA F C   1 
ATOM   9681  O O   . ALA F 1 165 ? 27.289  72.539  -78.761  1.00 28.28 ? 165 ALA F O   1 
ATOM   9682  C CB  . ALA F 1 165 ? 30.219  72.104  -78.601  1.00 25.23 ? 165 ALA F CB  1 
ATOM   9683  N N   . LEU F 1 166 ? 27.307  71.254  -76.907  1.00 26.58 ? 166 LEU F N   1 
ATOM   9684  C CA  . LEU F 1 166 ? 25.997  70.664  -77.192  1.00 25.99 ? 166 LEU F CA  1 
ATOM   9685  C C   . LEU F 1 166 ? 24.831  71.649  -77.104  1.00 25.16 ? 166 LEU F C   1 
ATOM   9686  O O   . LEU F 1 166 ? 23.975  71.648  -77.981  1.00 25.81 ? 166 LEU F O   1 
ATOM   9687  C CB  . LEU F 1 166 ? 25.731  69.440  -76.300  1.00 27.14 ? 166 LEU F CB  1 
ATOM   9688  C CG  . LEU F 1 166 ? 26.591  68.190  -76.526  1.00 27.17 ? 166 LEU F CG  1 
ATOM   9689  C CD1 . LEU F 1 166 ? 26.096  67.020  -75.678  1.00 27.50 ? 166 LEU F CD1 1 
ATOM   9690  C CD2 . LEU F 1 166 ? 26.569  67.760  -77.975  1.00 26.95 ? 166 LEU F CD2 1 
ATOM   9691  N N   . PRO F 1 167 ? 24.781  72.505  -76.067  1.00 24.03 ? 167 PRO F N   1 
ATOM   9692  C CA  . PRO F 1 167 ? 23.661  73.452  -76.010  1.00 23.86 ? 167 PRO F CA  1 
ATOM   9693  C C   . PRO F 1 167 ? 23.421  74.229  -77.325  1.00 24.61 ? 167 PRO F C   1 
ATOM   9694  O O   . PRO F 1 167 ? 22.278  74.324  -77.787  1.00 27.44 ? 167 PRO F O   1 
ATOM   9695  C CB  . PRO F 1 167 ? 24.069  74.408  -74.886  1.00 23.57 ? 167 PRO F CB  1 
ATOM   9696  C CG  . PRO F 1 167 ? 24.909  73.561  -73.993  1.00 23.68 ? 167 PRO F CG  1 
ATOM   9697  C CD  . PRO F 1 167 ? 25.666  72.637  -74.898  1.00 23.98 ? 167 PRO F CD  1 
ATOM   9698  N N   . GLY F 1 168 ? 24.478  74.775  -77.921  1.00 23.98 ? 168 GLY F N   1 
ATOM   9699  C CA  . GLY F 1 168 ? 24.347  75.533  -79.163  1.00 23.92 ? 168 GLY F CA  1 
ATOM   9700  C C   . GLY F 1 168 ? 23.752  74.710  -80.293  1.00 24.12 ? 168 GLY F C   1 
ATOM   9701  O O   . GLY F 1 168 ? 22.812  75.139  -80.967  1.00 24.28 ? 168 GLY F O   1 
ATOM   9702  N N   . VAL F 1 169 ? 24.298  73.511  -80.479  1.00 23.61 ? 169 VAL F N   1 
ATOM   9703  C CA  . VAL F 1 169 ? 23.865  72.597  -81.538  1.00 22.39 ? 169 VAL F CA  1 
ATOM   9704  C C   . VAL F 1 169 ? 22.442  72.123  -81.280  1.00 21.80 ? 169 VAL F C   1 
ATOM   9705  O O   . VAL F 1 169 ? 21.608  72.180  -82.171  1.00 21.54 ? 169 VAL F O   1 
ATOM   9706  C CB  . VAL F 1 169 ? 24.794  71.369  -81.646  1.00 22.23 ? 169 VAL F CB  1 
ATOM   9707  C CG1 . VAL F 1 169 ? 24.270  70.390  -82.685  1.00 21.85 ? 169 VAL F CG1 1 
ATOM   9708  C CG2 . VAL F 1 169 ? 26.211  71.780  -82.015  1.00 22.46 ? 169 VAL F CG2 1 
ATOM   9709  N N   . TYR F 1 170 ? 22.179  71.652  -80.063  1.00 21.63 ? 170 TYR F N   1 
ATOM   9710  C CA  . TYR F 1 170 ? 20.835  71.184  -79.666  1.00 22.13 ? 170 TYR F CA  1 
ATOM   9711  C C   . TYR F 1 170 ? 19.765  72.242  -79.898  1.00 22.26 ? 170 TYR F C   1 
ATOM   9712  O O   . TYR F 1 170 ? 18.665  71.929  -80.363  1.00 20.28 ? 170 TYR F O   1 
ATOM   9713  C CB  . TYR F 1 170 ? 20.797  70.736  -78.194  1.00 22.17 ? 170 TYR F CB  1 
ATOM   9714  C CG  . TYR F 1 170 ? 21.234  69.296  -77.952  1.00 23.20 ? 170 TYR F CG  1 
ATOM   9715  C CD1 . TYR F 1 170 ? 22.169  68.662  -78.784  1.00 23.79 ? 170 TYR F CD1 1 
ATOM   9716  C CD2 . TYR F 1 170 ? 20.746  68.580  -76.863  1.00 23.02 ? 170 TYR F CD2 1 
ATOM   9717  C CE1 . TYR F 1 170 ? 22.574  67.359  -78.541  1.00 23.67 ? 170 TYR F CE1 1 
ATOM   9718  C CE2 . TYR F 1 170 ? 21.142  67.276  -76.618  1.00 22.62 ? 170 TYR F CE2 1 
ATOM   9719  C CZ  . TYR F 1 170 ? 22.062  66.676  -77.454  1.00 23.04 ? 170 TYR F CZ  1 
ATOM   9720  O OH  . TYR F 1 170 ? 22.474  65.380  -77.238  1.00 23.29 ? 170 TYR F OH  1 
ATOM   9721  N N   . LYS F 1 171 ? 20.091  73.498  -79.583  1.00 23.31 ? 171 LYS F N   1 
ATOM   9722  C CA  . LYS F 1 171 ? 19.147  74.583  -79.792  1.00 23.09 ? 171 LYS F CA  1 
ATOM   9723  C C   . LYS F 1 171 ? 18.796  74.744  -81.273  1.00 22.29 ? 171 LYS F C   1 
ATOM   9724  O O   . LYS F 1 171 ? 17.628  74.898  -81.615  1.00 22.09 ? 171 LYS F O   1 
ATOM   9725  C CB  . LYS F 1 171 ? 19.659  75.898  -79.224  1.00 23.73 ? 171 LYS F CB  1 
ATOM   9726  C CG  . LYS F 1 171 ? 18.549  76.964  -79.208  1.00 25.35 ? 171 LYS F CG  1 
ATOM   9727  C CD  . LYS F 1 171 ? 18.846  78.220  -78.416  1.00 25.68 ? 171 LYS F CD  1 
ATOM   9728  C CE  . LYS F 1 171 ? 19.882  79.088  -79.126  1.00 26.97 ? 171 LYS F CE  1 
ATOM   9729  N NZ  . LYS F 1 171 ? 19.395  80.442  -79.418  1.00 27.52 ? 171 LYS F NZ  1 
ATOM   9730  N N   . ALA F 1 172 ? 19.799  74.717  -82.143  1.00 21.94 ? 172 ALA F N   1 
ATOM   9731  C CA  . ALA F 1 172 ? 19.570  74.887  -83.583  1.00 22.36 ? 172 ALA F CA  1 
ATOM   9732  C C   . ALA F 1 172 ? 18.720  73.756  -84.119  1.00 23.29 ? 172 ALA F C   1 
ATOM   9733  O O   . ALA F 1 172 ? 17.751  73.992  -84.840  1.00 24.78 ? 172 ALA F O   1 
ATOM   9734  C CB  . ALA F 1 172 ? 20.891  74.956  -84.344  1.00 22.12 ? 172 ALA F CB  1 
ATOM   9735  N N   . ILE F 1 173 ? 19.081  72.529  -83.751  1.00 23.19 ? 173 ILE F N   1 
ATOM   9736  C CA  . ILE F 1 173 ? 18.370  71.333  -84.192  1.00 21.56 ? 173 ILE F CA  1 
ATOM   9737  C C   . ILE F 1 173 ? 16.911  71.357  -83.738  1.00 21.12 ? 173 ILE F C   1 
ATOM   9738  O O   . ILE F 1 173 ? 16.020  71.031  -84.507  1.00 19.28 ? 173 ILE F O   1 
ATOM   9739  C CB  . ILE F 1 173 ? 19.079  70.058  -83.662  1.00 20.85 ? 173 ILE F CB  1 
ATOM   9740  C CG1 . ILE F 1 173 ? 20.458  69.892  -84.313  1.00 20.60 ? 173 ILE F CG1 1 
ATOM   9741  C CG2 . ILE F 1 173 ? 18.229  68.816  -83.854  1.00 20.50 ? 173 ILE F CG2 1 
ATOM   9742  C CD1 . ILE F 1 173 ? 20.425  69.617  -85.791  1.00 20.53 ? 173 ILE F CD1 1 
ATOM   9743  N N   . ALA F 1 174 ? 16.683  71.729  -82.480  1.00 22.74 ? 174 ALA F N   1 
ATOM   9744  C CA  . ALA F 1 174 ? 15.331  71.787  -81.915  1.00 23.73 ? 174 ALA F CA  1 
ATOM   9745  C C   . ALA F 1 174 ? 14.506  72.830  -82.641  1.00 24.87 ? 174 ALA F C   1 
ATOM   9746  O O   . ALA F 1 174 ? 13.364  72.568  -83.032  1.00 24.90 ? 174 ALA F O   1 
ATOM   9747  C CB  . ALA F 1 174 ? 15.391  72.116  -80.433  1.00 24.05 ? 174 ALA F CB  1 
ATOM   9748  N N   . GLU F 1 175 ? 15.104  74.010  -82.814  1.00 25.84 ? 175 GLU F N   1 
ATOM   9749  C CA  . GLU F 1 175 ? 14.497  75.101  -83.553  1.00 27.57 ? 175 GLU F CA  1 
ATOM   9750  C C   . GLU F 1 175 ? 14.177  74.673  -84.987  1.00 26.50 ? 175 GLU F C   1 
ATOM   9751  O O   . GLU F 1 175 ? 13.094  74.950  -85.476  1.00 28.77 ? 175 GLU F O   1 
ATOM   9752  C CB  . GLU F 1 175 ? 15.445  76.317  -83.564  1.00 30.79 ? 175 GLU F CB  1 
ATOM   9753  C CG  . GLU F 1 175 ? 14.841  77.692  -83.313  1.00 32.77 ? 175 GLU F CG  1 
ATOM   9754  C CD  . GLU F 1 175 ? 15.346  78.355  -82.029  1.00 34.46 ? 175 GLU F CD  1 
ATOM   9755  O OE1 . GLU F 1 175 ? 16.461  78.902  -81.991  1.00 36.72 ? 175 GLU F OE1 1 
ATOM   9756  O OE2 . GLU F 1 175 ? 14.605  78.295  -81.048  1.00 35.31 ? 175 GLU F OE2 1 
ATOM   9757  N N   . ALA F 1 176 ? 15.100  73.984  -85.649  1.00 24.42 ? 176 ALA F N   1 
ATOM   9758  C CA  . ALA F 1 176 ? 14.885  73.531  -87.030  1.00 23.54 ? 176 ALA F CA  1 
ATOM   9759  C C   . ALA F 1 176 ? 13.706  72.588  -87.142  1.00 22.23 ? 176 ALA F C   1 
ATOM   9760  O O   . ALA F 1 176 ? 13.041  72.543  -88.162  1.00 22.71 ? 176 ALA F O   1 
ATOM   9761  C CB  . ALA F 1 176 ? 16.134  72.851  -87.579  1.00 23.69 ? 176 ALA F CB  1 
ATOM   9762  N N   . ALA F 1 177 ? 13.465  71.828  -86.085  1.00 21.37 ? 177 ALA F N   1 
ATOM   9763  C CA  . ALA F 1 177 ? 12.358  70.883  -86.021  1.00 20.99 ? 177 ALA F CA  1 
ATOM   9764  C C   . ALA F 1 177 ? 11.052  71.527  -85.578  1.00 21.11 ? 177 ALA F C   1 
ATOM   9765  O O   . ALA F 1 177 ? 10.043  70.834  -85.465  1.00 21.48 ? 177 ALA F O   1 
ATOM   9766  C CB  . ALA F 1 177 ? 12.714  69.757  -85.062  1.00 20.71 ? 177 ALA F CB  1 
ATOM   9767  N N   . GLY F 1 178 ? 11.067  72.831  -85.297  1.00 20.99 ? 178 GLY F N   1 
ATOM   9768  C CA  . GLY F 1 178 ? 9.908   73.521  -84.723  1.00 21.05 ? 178 GLY F CA  1 
ATOM   9769  C C   . GLY F 1 178 ? 9.515   73.042  -83.339  1.00 21.00 ? 178 GLY F C   1 
ATOM   9770  O O   . GLY F 1 178 ? 8.330   72.926  -83.042  1.00 21.26 ? 178 GLY F O   1 
ATOM   9771  N N   . GLU F 1 179 ? 10.505  72.756  -82.502  1.00 21.95 ? 179 GLU F N   1 
ATOM   9772  C CA  . GLU F 1 179 ? 10.283  72.188  -81.164  1.00 23.58 ? 179 GLU F CA  1 
ATOM   9773  C C   . GLU F 1 179 ? 11.038  73.022  -80.128  1.00 24.04 ? 179 GLU F C   1 
ATOM   9774  O O   . GLU F 1 179 ? 11.639  74.029  -80.478  1.00 25.46 ? 179 GLU F O   1 
ATOM   9775  C CB  . GLU F 1 179 ? 10.733  70.724  -81.128  1.00 24.22 ? 179 GLU F CB  1 
ATOM   9776  C CG  . GLU F 1 179 ? 10.019  69.824  -82.127  1.00 25.43 ? 179 GLU F CG  1 
ATOM   9777  C CD  . GLU F 1 179 ? 8.578   69.491  -81.746  1.00 26.93 ? 179 GLU F CD  1 
ATOM   9778  O OE1 . GLU F 1 179 ? 7.909   68.759  -82.514  1.00 28.49 ? 179 GLU F OE1 1 
ATOM   9779  O OE2 . GLU F 1 179 ? 8.105   69.941  -80.681  1.00 28.84 ? 179 GLU F OE2 1 
ATOM   9780  N N   . SER F 1 180 ? 11.016  72.620  -78.865  1.00 23.79 ? 180 SER F N   1 
ATOM   9781  C CA  . SER F 1 180 ? 11.587  73.445  -77.810  1.00 24.39 ? 180 SER F CA  1 
ATOM   9782  C C   . SER F 1 180 ? 12.930  72.952  -77.299  1.00 24.35 ? 180 SER F C   1 
ATOM   9783  O O   . SER F 1 180 ? 13.290  71.795  -77.486  1.00 25.01 ? 180 SER F O   1 
ATOM   9784  C CB  . SER F 1 180 ? 10.613  73.523  -76.650  1.00 24.86 ? 180 SER F CB  1 
ATOM   9785  O OG  . SER F 1 180 ? 9.309   73.774  -77.128  1.00 25.01 ? 180 SER F OG  1 
ATOM   9786  N N   . PHE F 1 181 ? 13.650  73.854  -76.637  1.00 24.35 ? 181 PHE F N   1 
ATOM   9787  C CA  . PHE F 1 181 ? 14.992  73.603  -76.132  1.00 24.87 ? 181 PHE F CA  1 
ATOM   9788  C C   . PHE F 1 181 ? 15.192  74.123  -74.711  1.00 25.82 ? 181 PHE F C   1 
ATOM   9789  O O   . PHE F 1 181 ? 14.597  75.111  -74.324  1.00 26.43 ? 181 PHE F O   1 
ATOM   9790  C CB  . PHE F 1 181 ? 16.025  74.278  -77.023  1.00 24.98 ? 181 PHE F CB  1 
ATOM   9791  C CG  . PHE F 1 181 ? 17.401  74.285  -76.424  1.00 24.97 ? 181 PHE F CG  1 
ATOM   9792  C CD1 . PHE F 1 181 ? 18.117  73.104  -76.319  1.00 25.20 ? 181 PHE F CD1 1 
ATOM   9793  C CD2 . PHE F 1 181 ? 17.960  75.451  -75.941  1.00 24.50 ? 181 PHE F CD2 1 
ATOM   9794  C CE1 . PHE F 1 181 ? 19.369  73.085  -75.754  1.00 24.80 ? 181 PHE F CE1 1 
ATOM   9795  C CE2 . PHE F 1 181 ? 19.220  75.441  -75.381  1.00 24.51 ? 181 PHE F CE2 1 
ATOM   9796  C CZ  . PHE F 1 181 ? 19.927  74.255  -75.284  1.00 24.56 ? 181 PHE F CZ  1 
ATOM   9797  N N   . PHE F 1 182 ? 16.044  73.449  -73.944  1.00 27.29 ? 182 PHE F N   1 
ATOM   9798  C CA  . PHE F 1 182 ? 16.467  73.932  -72.635  1.00 28.03 ? 182 PHE F CA  1 
ATOM   9799  C C   . PHE F 1 182 ? 17.853  73.411  -72.296  1.00 28.83 ? 182 PHE F C   1 
ATOM   9800  O O   . PHE F 1 182 ? 18.135  72.232  -72.477  1.00 27.85 ? 182 PHE F O   1 
ATOM   9801  C CB  . PHE F 1 182 ? 15.477  73.514  -71.553  1.00 27.82 ? 182 PHE F CB  1 
ATOM   9802  C CG  . PHE F 1 182 ? 15.835  74.018  -70.177  1.00 29.94 ? 182 PHE F CG  1 
ATOM   9803  C CD1 . PHE F 1 182 ? 15.531  75.321  -69.798  1.00 30.23 ? 182 PHE F CD1 1 
ATOM   9804  C CD2 . PHE F 1 182 ? 16.476  73.194  -69.257  1.00 30.98 ? 182 PHE F CD2 1 
ATOM   9805  C CE1 . PHE F 1 182 ? 15.855  75.789  -68.532  1.00 29.87 ? 182 PHE F CE1 1 
ATOM   9806  C CE2 . PHE F 1 182 ? 16.807  73.668  -67.996  1.00 30.91 ? 182 PHE F CE2 1 
ATOM   9807  C CZ  . PHE F 1 182 ? 16.480  74.964  -67.629  1.00 29.78 ? 182 PHE F CZ  1 
ATOM   9808  N N   . ASP F 1 183 ? 18.709  74.296  -71.800  1.00 30.52 ? 183 ASP F N   1 
ATOM   9809  C CA  . ASP F 1 183 ? 20.087  73.937  -71.473  1.00 31.20 ? 183 ASP F CA  1 
ATOM   9810  C C   . ASP F 1 183 ? 20.211  73.652  -69.985  1.00 31.24 ? 183 ASP F C   1 
ATOM   9811  O O   . ASP F 1 183 ? 20.190  74.563  -69.162  1.00 29.78 ? 183 ASP F O   1 
ATOM   9812  C CB  . ASP F 1 183 ? 21.015  75.086  -71.862  1.00 31.97 ? 183 ASP F CB  1 
ATOM   9813  C CG  . ASP F 1 183 ? 22.467  74.803  -71.565  1.00 31.80 ? 183 ASP F CG  1 
ATOM   9814  O OD1 . ASP F 1 183 ? 22.829  73.675  -71.181  1.00 32.06 ? 183 ASP F OD1 1 
ATOM   9815  O OD2 . ASP F 1 183 ? 23.265  75.733  -71.730  1.00 32.75 ? 183 ASP F OD2 1 
ATOM   9816  N N   . ALA F 1 184 ? 20.357  72.383  -69.631  1.00 32.78 ? 184 ALA F N   1 
ATOM   9817  C CA  . ALA F 1 184 ? 20.514  72.025  -68.233  1.00 35.43 ? 184 ALA F CA  1 
ATOM   9818  C C   . ALA F 1 184 ? 21.723  72.743  -67.602  1.00 36.24 ? 184 ALA F C   1 
ATOM   9819  O O   . ALA F 1 184 ? 21.717  73.057  -66.412  1.00 36.98 ? 184 ALA F O   1 
ATOM   9820  C CB  . ALA F 1 184 ? 20.647  70.523  -68.094  1.00 37.12 ? 184 ALA F CB  1 
ATOM   9821  N N   . GLY F 1 185 ? 22.741  73.022  -68.413  1.00 35.77 ? 185 GLY F N   1 
ATOM   9822  C CA  . GLY F 1 185 ? 23.911  73.770  -67.963  1.00 34.35 ? 185 GLY F CA  1 
ATOM   9823  C C   . GLY F 1 185 ? 23.649  75.199  -67.518  1.00 32.62 ? 185 GLY F C   1 
ATOM   9824  O O   . GLY F 1 185 ? 24.502  75.805  -66.883  1.00 31.73 ? 185 GLY F O   1 
ATOM   9825  N N   . SER F 1 186 ? 22.482  75.745  -67.857  1.00 31.71 ? 186 SER F N   1 
ATOM   9826  C CA  . SER F 1 186 ? 22.111  77.093  -67.442  1.00 30.88 ? 186 SER F CA  1 
ATOM   9827  C C   . SER F 1 186 ? 21.703  77.163  -65.965  1.00 31.30 ? 186 SER F C   1 
ATOM   9828  O O   . SER F 1 186 ? 21.716  78.243  -65.381  1.00 33.66 ? 186 SER F O   1 
ATOM   9829  C CB  . SER F 1 186 ? 20.973  77.636  -68.313  1.00 30.08 ? 186 SER F CB  1 
ATOM   9830  O OG  . SER F 1 186 ? 19.711  77.142  -67.888  1.00 29.19 ? 186 SER F OG  1 
ATOM   9831  N N   . VAL F 1 187 ? 21.343  76.026  -65.365  1.00 31.03 ? 187 VAL F N   1 
ATOM   9832  C CA  . VAL F 1 187 ? 20.882  75.991  -63.975  1.00 30.55 ? 187 VAL F CA  1 
ATOM   9833  C C   . VAL F 1 187 ? 21.642  75.034  -63.057  1.00 29.34 ? 187 VAL F C   1 
ATOM   9834  O O   . VAL F 1 187 ? 21.491  75.133  -61.845  1.00 29.96 ? 187 VAL F O   1 
ATOM   9835  C CB  . VAL F 1 187 ? 19.376  75.655  -63.893  1.00 32.05 ? 187 VAL F CB  1 
ATOM   9836  C CG1 . VAL F 1 187 ? 18.548  76.767  -64.524  1.00 31.97 ? 187 VAL F CG1 1 
ATOM   9837  C CG2 . VAL F 1 187 ? 19.079  74.307  -64.559  1.00 33.23 ? 187 VAL F CG2 1 
ATOM   9838  N N   . VAL F 1 188 ? 22.418  74.104  -63.620  1.00 29.36 ? 188 VAL F N   1 
ATOM   9839  C CA  . VAL F 1 188 ? 23.233  73.155  -62.837  1.00 31.26 ? 188 VAL F CA  1 
ATOM   9840  C C   . VAL F 1 188 ? 24.525  72.766  -63.554  1.00 31.86 ? 188 VAL F C   1 
ATOM   9841  O O   . VAL F 1 188 ? 24.696  73.042  -64.749  1.00 34.04 ? 188 VAL F O   1 
ATOM   9842  C CB  . VAL F 1 188 ? 22.488  71.829  -62.543  1.00 31.69 ? 188 VAL F CB  1 
ATOM   9843  C CG1 . VAL F 1 188 ? 21.144  72.081  -61.846  1.00 31.89 ? 188 VAL F CG1 1 
ATOM   9844  C CG2 . VAL F 1 188 ? 22.303  71.009  -63.824  1.00 32.24 ? 188 VAL F CG2 1 
ATOM   9845  N N   . SER F 1 189 ? 25.423  72.106  -62.823  1.00 32.05 ? 189 SER F N   1 
ATOM   9846  C CA  . SER F 1 189 ? 26.603  71.473  -63.434  1.00 32.73 ? 189 SER F CA  1 
ATOM   9847  C C   . SER F 1 189 ? 26.868  70.099  -62.831  1.00 32.29 ? 189 SER F C   1 
ATOM   9848  O O   . SER F 1 189 ? 26.263  69.716  -61.826  1.00 34.19 ? 189 SER F O   1 
ATOM   9849  C CB  . SER F 1 189 ? 27.847  72.354  -63.334  1.00 31.75 ? 189 SER F CB  1 
ATOM   9850  O OG  . SER F 1 189 ? 27.830  73.066  -62.130  1.00 32.23 ? 189 SER F OG  1 
ATOM   9851  N N   . THR F 1 190 ? 27.759  69.361  -63.481  1.00 31.79 ? 190 THR F N   1 
ATOM   9852  C CA  . THR F 1 190 ? 28.051  68.000  -63.100  1.00 32.12 ? 190 THR F CA  1 
ATOM   9853  C C   . THR F 1 190 ? 28.916  68.025  -61.828  1.00 32.07 ? 190 THR F C   1 
ATOM   9854  O O   . THR F 1 190 ? 30.148  68.148  -61.878  1.00 30.93 ? 190 THR F O   1 
ATOM   9855  C CB  . THR F 1 190 ? 28.733  67.223  -64.255  1.00 31.91 ? 190 THR F CB  1 
ATOM   9856  O OG1 . THR F 1 190 ? 27.990  67.401  -65.466  1.00 30.65 ? 190 THR F OG1 1 
ATOM   9857  C CG2 . THR F 1 190 ? 28.800  65.727  -63.929  1.00 31.52 ? 190 THR F CG2 1 
ATOM   9858  N N   . ASP F 1 191 ? 28.233  67.923  -60.688  1.00 30.92 ? 191 ASP F N   1 
ATOM   9859  C CA  . ASP F 1 191 ? 28.870  68.030  -59.375  1.00 29.15 ? 191 ASP F CA  1 
ATOM   9860  C C   . ASP F 1 191 ? 29.120  66.671  -58.714  1.00 29.57 ? 191 ASP F C   1 
ATOM   9861  O O   . ASP F 1 191 ? 29.632  66.600  -57.618  1.00 28.57 ? 191 ASP F O   1 
ATOM   9862  C CB  . ASP F 1 191 ? 28.012  68.893  -58.447  1.00 27.80 ? 191 ASP F CB  1 
ATOM   9863  C CG  . ASP F 1 191 ? 26.701  68.226  -58.072  1.00 27.90 ? 191 ASP F CG  1 
ATOM   9864  O OD1 . ASP F 1 191 ? 26.190  67.406  -58.871  1.00 27.75 ? 191 ASP F OD1 1 
ATOM   9865  O OD2 . ASP F 1 191 ? 26.186  68.537  -56.980  1.00 27.45 ? 191 ASP F OD2 1 
ATOM   9866  N N   . GLY F 1 192 ? 28.748  65.582  -59.358  1.00 30.85 ? 192 GLY F N   1 
ATOM   9867  C CA  . GLY F 1 192 ? 29.026  64.271  -58.779  1.00 31.40 ? 192 GLY F CA  1 
ATOM   9868  C C   . GLY F 1 192 ? 30.514  64.015  -58.638  1.00 30.39 ? 192 GLY F C   1 
ATOM   9869  O O   . GLY F 1 192 ? 31.315  64.499  -59.434  1.00 29.72 ? 192 GLY F O   1 
ATOM   9870  N N   . VAL F 1 193 ? 30.871  63.238  -57.623  1.00 30.20 ? 193 VAL F N   1 
ATOM   9871  C CA  . VAL F 1 193 ? 32.272  62.945  -57.339  1.00 29.35 ? 193 VAL F CA  1 
ATOM   9872  C C   . VAL F 1 193 ? 33.001  62.260  -58.500  1.00 27.79 ? 193 VAL F C   1 
ATOM   9873  O O   . VAL F 1 193 ? 34.198  62.445  -58.649  1.00 26.01 ? 193 VAL F O   1 
ATOM   9874  C CB  . VAL F 1 193 ? 32.420  62.107  -56.037  1.00 30.62 ? 193 VAL F CB  1 
ATOM   9875  C CG1 . VAL F 1 193 ? 31.935  60.675  -56.236  1.00 29.52 ? 193 VAL F CG1 1 
ATOM   9876  C CG2 . VAL F 1 193 ? 33.863  62.130  -55.536  1.00 31.24 ? 193 VAL F CG2 1 
ATOM   9877  N N   . ASP F 1 194 ? 32.291  61.491  -59.324  1.00 27.34 ? 194 ASP F N   1 
ATOM   9878  C CA  . ASP F 1 194 ? 32.924  60.756  -60.436  1.00 27.35 ? 194 ASP F CA  1 
ATOM   9879  C C   . ASP F 1 194 ? 33.079  61.602  -61.704  1.00 27.43 ? 194 ASP F C   1 
ATOM   9880  O O   . ASP F 1 194 ? 33.596  61.118  -62.712  1.00 26.04 ? 194 ASP F O   1 
ATOM   9881  C CB  . ASP F 1 194 ? 32.192  59.430  -60.751  1.00 27.14 ? 194 ASP F CB  1 
ATOM   9882  C CG  . ASP F 1 194 ? 30.697  59.613  -61.079  1.00 26.82 ? 194 ASP F CG  1 
ATOM   9883  O OD1 . ASP F 1 194 ? 30.272  60.768  -61.349  1.00 25.07 ? 194 ASP F OD1 1 
ATOM   9884  O OD2 . ASP F 1 194 ? 29.948  58.580  -61.030  1.00 26.28 ? 194 ASP F OD2 1 
ATOM   9885  N N   . GLY F 1 195 ? 32.633  62.859  -61.656  1.00 27.76 ? 195 GLY F N   1 
ATOM   9886  C CA  . GLY F 1 195 ? 32.783  63.782  -62.784  1.00 27.90 ? 195 GLY F CA  1 
ATOM   9887  C C   . GLY F 1 195 ? 31.772  63.596  -63.912  1.00 27.31 ? 195 GLY F C   1 
ATOM   9888  O O   . GLY F 1 195 ? 31.916  64.214  -64.971  1.00 27.08 ? 195 GLY F O   1 
ATOM   9889  N N   . ILE F 1 196 ? 30.755  62.755  -63.689  1.00 26.77 ? 196 ILE F N   1 
ATOM   9890  C CA  . ILE F 1 196 ? 29.758  62.450  -64.716  1.00 26.22 ? 196 ILE F CA  1 
ATOM   9891  C C   . ILE F 1 196 ? 28.309  62.590  -64.253  1.00 24.53 ? 196 ILE F C   1 
ATOM   9892  O O   . ILE F 1 196 ? 27.485  63.090  -65.015  1.00 26.42 ? 196 ILE F O   1 
ATOM   9893  C CB  . ILE F 1 196 ? 29.981  61.029  -65.290  1.00 26.80 ? 196 ILE F CB  1 
ATOM   9894  C CG1 . ILE F 1 196 ? 31.298  60.996  -66.075  1.00 27.26 ? 196 ILE F CG1 1 
ATOM   9895  C CG2 . ILE F 1 196 ? 28.851  60.612  -66.221  1.00 26.03 ? 196 ILE F CG2 1 
ATOM   9896  C CD1 . ILE F 1 196 ? 31.978  59.646  -66.042  1.00 27.82 ? 196 ILE F CD1 1 
ATOM   9897  N N   . HIS F 1 197 ? 28.001  62.154  -63.036  1.00 22.88 ? 197 HIS F N   1 
ATOM   9898  C CA  . HIS F 1 197 ? 26.614  62.085  -62.562  1.00 23.05 ? 197 HIS F CA  1 
ATOM   9899  C C   . HIS F 1 197 ? 26.262  63.152  -61.539  1.00 22.13 ? 197 HIS F C   1 
ATOM   9900  O O   . HIS F 1 197 ? 27.113  63.959  -61.179  1.00 21.68 ? 197 HIS F O   1 
ATOM   9901  C CB  . HIS F 1 197 ? 26.339  60.691  -62.024  1.00 23.72 ? 197 HIS F CB  1 
ATOM   9902  C CG  . HIS F 1 197 ? 26.695  59.626  -63.003  1.00 24.25 ? 197 HIS F CG  1 
ATOM   9903  N ND1 . HIS F 1 197 ? 27.851  58.889  -62.903  1.00 24.52 ? 197 HIS F ND1 1 
ATOM   9904  C CD2 . HIS F 1 197 ? 26.087  59.224  -64.146  1.00 24.40 ? 197 HIS F CD2 1 
ATOM   9905  C CE1 . HIS F 1 197 ? 27.921  58.048  -63.921  1.00 24.71 ? 197 HIS F CE1 1 
ATOM   9906  N NE2 . HIS F 1 197 ? 26.864  58.232  -64.690  1.00 24.20 ? 197 HIS F NE2 1 
ATOM   9907  N N   . PHE F 1 198 ? 25.000  63.177  -61.122  1.00 21.32 ? 198 PHE F N   1 
ATOM   9908  C CA  . PHE F 1 198 ? 24.469  64.281  -60.317  1.00 21.53 ? 198 PHE F CA  1 
ATOM   9909  C C   . PHE F 1 198 ? 24.205  63.879  -58.862  1.00 22.84 ? 198 PHE F C   1 
ATOM   9910  O O   . PHE F 1 198 ? 23.821  62.749  -58.562  1.00 23.67 ? 198 PHE F O   1 
ATOM   9911  C CB  . PHE F 1 198 ? 23.141  64.816  -60.882  1.00 19.78 ? 198 PHE F CB  1 
ATOM   9912  C CG  . PHE F 1 198 ? 23.215  65.370  -62.285  1.00 18.92 ? 198 PHE F CG  1 
ATOM   9913  C CD1 . PHE F 1 198 ? 24.414  65.724  -62.889  1.00 18.66 ? 198 PHE F CD1 1 
ATOM   9914  C CD2 . PHE F 1 198 ? 22.042  65.580  -62.998  1.00 18.42 ? 198 PHE F CD2 1 
ATOM   9915  C CE1 . PHE F 1 198 ? 24.444  66.230  -64.183  1.00 17.99 ? 198 PHE F CE1 1 
ATOM   9916  C CE2 . PHE F 1 198 ? 22.066  66.086  -64.285  1.00 17.67 ? 198 PHE F CE2 1 
ATOM   9917  C CZ  . PHE F 1 198 ? 23.263  66.412  -64.872  1.00 17.58 ? 198 PHE F CZ  1 
ATOM   9918  N N   . THR F 1 199 ? 24.377  64.843  -57.968  1.00 23.01 ? 199 THR F N   1 
ATOM   9919  C CA  . THR F 1 199 ? 23.945  64.710  -56.589  1.00 23.68 ? 199 THR F CA  1 
ATOM   9920  C C   . THR F 1 199 ? 22.454  64.944  -56.502  1.00 24.48 ? 199 THR F C   1 
ATOM   9921  O O   . THR F 1 199 ? 21.849  65.432  -57.458  1.00 23.94 ? 199 THR F O   1 
ATOM   9922  C CB  . THR F 1 199 ? 24.623  65.747  -55.682  1.00 23.40 ? 199 THR F CB  1 
ATOM   9923  O OG1 . THR F 1 199 ? 24.186  67.061  -56.054  1.00 23.27 ? 199 THR F OG1 1 
ATOM   9924  C CG2 . THR F 1 199 ? 26.155  65.631  -55.771  1.00 23.08 ? 199 THR F CG2 1 
ATOM   9925  N N   . ALA F 1 200 ? 21.866  64.623  -55.354  1.00 26.25 ? 200 ALA F N   1 
ATOM   9926  C CA  . ALA F 1 200 ? 20.436  64.862  -55.143  1.00 27.68 ? 200 ALA F CA  1 
ATOM   9927  C C   . ALA F 1 200 ? 20.129  66.360  -55.140  1.00 29.08 ? 200 ALA F C   1 
ATOM   9928  O O   . ALA F 1 200 ? 19.044  66.777  -55.568  1.00 27.79 ? 200 ALA F O   1 
ATOM   9929  C CB  . ALA F 1 200 ? 19.951  64.212  -53.847  1.00 27.49 ? 200 ALA F CB  1 
ATOM   9930  N N   . GLU F 1 201 ? 21.078  67.167  -54.661  1.00 32.58 ? 201 GLU F N   1 
ATOM   9931  C CA  . GLU F 1 201 ? 20.892  68.614  -54.673  1.00 36.35 ? 201 GLU F CA  1 
ATOM   9932  C C   . GLU F 1 201 ? 20.777  69.132  -56.109  1.00 34.87 ? 201 GLU F C   1 
ATOM   9933  O O   . GLU F 1 201 ? 19.924  69.970  -56.399  1.00 34.49 ? 201 GLU F O   1 
ATOM   9934  C CB  . GLU F 1 201 ? 21.996  69.345  -53.895  1.00 41.04 ? 201 GLU F CB  1 
ATOM   9935  C CG  . GLU F 1 201 ? 21.690  70.850  -53.682  1.00 45.75 ? 201 GLU F CG  1 
ATOM   9936  C CD  . GLU F 1 201 ? 20.226  71.188  -53.236  1.00 49.00 ? 201 GLU F CD  1 
ATOM   9937  O OE1 . GLU F 1 201 ? 19.609  70.452  -52.420  1.00 47.98 ? 201 GLU F OE1 1 
ATOM   9938  O OE2 . GLU F 1 201 ? 19.669  72.216  -53.701  1.00 49.64 ? 201 GLU F OE2 1 
ATOM   9939  N N   . THR F 1 202 ? 21.613  68.617  -57.006  1.00 33.72 ? 202 THR F N   1 
ATOM   9940  C CA  . THR F 1 202 ? 21.583  69.028  -58.415  1.00 32.99 ? 202 THR F CA  1 
ATOM   9941  C C   . THR F 1 202 ? 20.310  68.548  -59.105  1.00 31.42 ? 202 THR F C   1 
ATOM   9942  O O   . THR F 1 202 ? 19.725  69.272  -59.917  1.00 31.21 ? 202 THR F O   1 
ATOM   9943  C CB  . THR F 1 202 ? 22.819  68.517  -59.176  1.00 33.59 ? 202 THR F CB  1 
ATOM   9944  O OG1 . THR F 1 202 ? 23.970  69.258  -58.772  1.00 33.07 ? 202 THR F OG1 1 
ATOM   9945  C CG2 . THR F 1 202 ? 22.655  68.669  -60.681  1.00 35.39 ? 202 THR F CG2 1 
ATOM   9946  N N   . ASN F 1 203 ? 19.887  67.330  -58.784  1.00 29.63 ? 203 ASN F N   1 
ATOM   9947  C CA  . ASN F 1 203 ? 18.618  66.809  -59.296  1.00 28.18 ? 203 ASN F CA  1 
ATOM   9948  C C   . ASN F 1 203 ? 17.459  67.738  -58.956  1.00 27.70 ? 203 ASN F C   1 
ATOM   9949  O O   . ASN F 1 203 ? 16.647  68.064  -59.817  1.00 25.97 ? 203 ASN F O   1 
ATOM   9950  C CB  . ASN F 1 203 ? 18.319  65.417  -58.728  1.00 26.90 ? 203 ASN F CB  1 
ATOM   9951  C CG  . ASN F 1 203 ? 19.099  64.313  -59.411  1.00 26.49 ? 203 ASN F CG  1 
ATOM   9952  O OD1 . ASN F 1 203 ? 19.731  64.504  -60.471  1.00 24.56 ? 203 ASN F OD1 1 
ATOM   9953  N ND2 . ASN F 1 203 ? 19.055  63.129  -58.801  1.00 26.95 ? 203 ASN F ND2 1 
ATOM   9954  N N   . ARG F 1 204 ? 17.400  68.150  -57.689  1.00 29.76 ? 204 ARG F N   1 
ATOM   9955  C CA  . ARG F 1 204 ? 16.342  69.041  -57.201  1.00 31.82 ? 204 ARG F CA  1 
ATOM   9956  C C   . ARG F 1 204 ? 16.283  70.341  -57.978  1.00 30.37 ? 204 ARG F C   1 
ATOM   9957  O O   . ARG F 1 204 ? 15.211  70.766  -58.390  1.00 29.42 ? 204 ARG F O   1 
ATOM   9958  C CB  . ARG F 1 204 ? 16.499  69.334  -55.702  1.00 35.36 ? 204 ARG F CB  1 
ATOM   9959  C CG  . ARG F 1 204 ? 15.719  68.394  -54.798  1.00 40.26 ? 204 ARG F CG  1 
ATOM   9960  C CD  . ARG F 1 204 ? 15.834  68.803  -53.327  1.00 45.35 ? 204 ARG F CD  1 
ATOM   9961  N NE  . ARG F 1 204 ? 17.102  68.373  -52.710  1.00 47.02 ? 204 ARG F NE  1 
ATOM   9962  C CZ  . ARG F 1 204 ? 17.365  67.135  -52.286  1.00 45.09 ? 204 ARG F CZ  1 
ATOM   9963  N NH1 . ARG F 1 204 ? 16.474  66.156  -52.406  1.00 46.20 ? 204 ARG F NH1 1 
ATOM   9964  N NH2 . ARG F 1 204 ? 18.540  66.865  -51.748  1.00 43.30 ? 204 ARG F NH2 1 
ATOM   9965  N N   . THR F 1 205 ? 17.436  70.970  -58.181  1.00 29.63 ? 205 THR F N   1 
ATOM   9966  C CA  . THR F 1 205 ? 17.491  72.231  -58.911  1.00 29.85 ? 205 THR F CA  1 
ATOM   9967  C C   . THR F 1 205 ? 16.961  72.032  -60.332  1.00 32.39 ? 205 THR F C   1 
ATOM   9968  O O   . THR F 1 205 ? 16.121  72.811  -60.798  1.00 32.64 ? 205 THR F O   1 
ATOM   9969  C CB  . THR F 1 205 ? 18.923  72.792  -58.954  1.00 27.94 ? 205 THR F CB  1 
ATOM   9970  O OG1 . THR F 1 205 ? 19.435  72.847  -57.626  1.00 26.31 ? 205 THR F OG1 1 
ATOM   9971  C CG2 . THR F 1 205 ? 18.958  74.188  -59.548  1.00 27.53 ? 205 THR F CG2 1 
ATOM   9972  N N   . LEU F 1 206 ? 17.445  70.981  -61.001  1.00 34.23 ? 206 LEU F N   1 
ATOM   9973  C CA  . LEU F 1 206 ? 17.078  70.694  -62.392  1.00 33.29 ? 206 LEU F CA  1 
ATOM   9974  C C   . LEU F 1 206 ? 15.591  70.400  -62.535  1.00 32.39 ? 206 LEU F C   1 
ATOM   9975  O O   . LEU F 1 206 ? 14.939  70.914  -63.440  1.00 32.26 ? 206 LEU F O   1 
ATOM   9976  C CB  . LEU F 1 206 ? 17.893  69.510  -62.932  1.00 34.12 ? 206 LEU F CB  1 
ATOM   9977  C CG  . LEU F 1 206 ? 17.669  69.099  -64.388  1.00 35.07 ? 206 LEU F CG  1 
ATOM   9978  C CD1 . LEU F 1 206 ? 17.920  70.288  -65.310  1.00 36.47 ? 206 LEU F CD1 1 
ATOM   9979  C CD2 . LEU F 1 206 ? 18.561  67.914  -64.738  1.00 34.33 ? 206 LEU F CD2 1 
ATOM   9980  N N   . GLY F 1 207 ? 15.066  69.569  -61.641  1.00 32.26 ? 207 GLY F N   1 
ATOM   9981  C CA  . GLY F 1 207 ? 13.656  69.213  -61.651  1.00 32.19 ? 207 GLY F CA  1 
ATOM   9982  C C   . GLY F 1 207 ? 12.761  70.434  -61.575  1.00 31.79 ? 207 GLY F C   1 
ATOM   9983  O O   . GLY F 1 207 ? 11.786  70.556  -62.320  1.00 31.35 ? 207 GLY F O   1 
ATOM   9984  N N   . ALA F 1 208 ? 13.110  71.348  -60.672  1.00 32.08 ? 208 ALA F N   1 
ATOM   9985  C CA  . ALA F 1 208 ? 12.314  72.546  -60.440  1.00 32.24 ? 208 ALA F CA  1 
ATOM   9986  C C   . ALA F 1 208 ? 12.416  73.499  -61.622  1.00 34.31 ? 208 ALA F C   1 
ATOM   9987  O O   . ALA F 1 208 ? 11.418  74.099  -62.006  1.00 40.25 ? 208 ALA F O   1 
ATOM   9988  C CB  . ALA F 1 208 ? 12.745  73.238  -59.159  1.00 32.24 ? 208 ALA F CB  1 
ATOM   9989  N N   . ALA F 1 209 ? 13.615  73.636  -62.193  1.00 32.67 ? 209 ALA F N   1 
ATOM   9990  C CA  . ALA F 1 209 ? 13.834  74.502  -63.348  1.00 30.87 ? 209 ALA F CA  1 
ATOM   9991  C C   . ALA F 1 209 ? 13.108  73.977  -64.569  1.00 31.96 ? 209 ALA F C   1 
ATOM   9992  O O   . ALA F 1 209 ? 12.482  74.740  -65.287  1.00 33.82 ? 209 ALA F O   1 
ATOM   9993  C CB  . ALA F 1 209 ? 15.312  74.630  -63.648  1.00 30.00 ? 209 ALA F CB  1 
ATOM   9994  N N   . VAL F 1 210 ? 13.194  72.676  -64.815  1.00 32.41 ? 210 VAL F N   1 
ATOM   9995  C CA  . VAL F 1 210 ? 12.543  72.076  -65.987  1.00 32.98 ? 210 VAL F CA  1 
ATOM   9996  C C   . VAL F 1 210 ? 11.010  72.170  -65.872  1.00 32.53 ? 210 VAL F C   1 
ATOM   9997  O O   . VAL F 1 210 ? 10.328  72.357  -66.867  1.00 28.88 ? 210 VAL F O   1 
ATOM   9998  C CB  . VAL F 1 210 ? 13.016  70.613  -66.222  1.00 32.56 ? 210 VAL F CB  1 
ATOM   9999  C CG1 . VAL F 1 210 ? 12.197  69.929  -67.307  1.00 31.76 ? 210 VAL F CG1 1 
ATOM   10000 C CG2 . VAL F 1 210 ? 14.492  70.597  -66.586  1.00 32.94 ? 210 VAL F CG2 1 
ATOM   10001 N N   . ALA F 1 211 ? 10.485  72.059  -64.656  1.00 34.30 ? 211 ALA F N   1 
ATOM   10002 C CA  . ALA F 1 211 ? 9.053   72.207  -64.420  1.00 35.51 ? 211 ALA F CA  1 
ATOM   10003 C C   . ALA F 1 211 ? 8.528   73.589  -64.851  1.00 36.90 ? 211 ALA F C   1 
ATOM   10004 O O   . ALA F 1 211 ? 7.430   73.682  -65.400  1.00 36.68 ? 211 ALA F O   1 
ATOM   10005 C CB  . ALA F 1 211 ? 8.727   71.948  -62.959  1.00 35.45 ? 211 ALA F CB  1 
ATOM   10006 N N   . GLN F 1 212 ? 9.298   74.642  -64.598  1.00 36.63 ? 212 GLN F N   1 
ATOM   10007 C CA  . GLN F 1 212 ? 8.950   76.002  -65.047  1.00 36.50 ? 212 GLN F CA  1 
ATOM   10008 C C   . GLN F 1 212 ? 8.838   76.012  -66.569  1.00 32.15 ? 212 GLN F C   1 
ATOM   10009 O O   . GLN F 1 212 ? 7.870   76.511  -67.129  1.00 29.00 ? 212 GLN F O   1 
ATOM   10010 C CB  . GLN F 1 212 ? 10.039  77.031  -64.616  1.00 41.64 ? 212 GLN F CB  1 
ATOM   10011 C CG  . GLN F 1 212 ? 9.745   77.940  -63.397  1.00 44.39 ? 212 GLN F CG  1 
ATOM   10012 C CD  . GLN F 1 212 ? 8.281   78.359  -63.349  1.00 47.34 ? 212 GLN F CD  1 
ATOM   10013 O OE1 . GLN F 1 212 ? 7.728   78.846  -64.359  1.00 48.59 ? 212 GLN F OE1 1 
ATOM   10014 N NE2 . GLN F 1 212 ? 7.631   78.166  -62.182  1.00 45.63 ? 212 GLN F NE2 1 
ATOM   10015 N N   . LYS F 1 213 ? 9.852   75.452  -67.218  1.00 29.65 ? 213 LYS F N   1 
ATOM   10016 C CA  . LYS F 1 213 ? 9.903   75.409  -68.664  1.00 28.47 ? 213 LYS F CA  1 
ATOM   10017 C C   . LYS F 1 213 ? 8.701   74.656  -69.238  1.00 27.99 ? 213 LYS F C   1 
ATOM   10018 O O   . LYS F 1 213 ? 8.065   75.120  -70.185  1.00 27.29 ? 213 LYS F O   1 
ATOM   10019 C CB  . LYS F 1 213 ? 11.216  74.758  -69.112  1.00 27.88 ? 213 LYS F CB  1 
ATOM   10020 C CG  . LYS F 1 213 ? 11.412  74.614  -70.607  1.00 27.17 ? 213 LYS F CG  1 
ATOM   10021 C CD  . LYS F 1 213 ? 11.383  75.987  -71.265  1.00 27.45 ? 213 LYS F CD  1 
ATOM   10022 C CE  . LYS F 1 213 ? 11.858  75.956  -72.708  1.00 26.65 ? 213 LYS F CE  1 
ATOM   10023 N NZ  . LYS F 1 213 ? 12.762  77.105  -73.030  1.00 26.32 ? 213 LYS F NZ  1 
ATOM   10024 N N   . VAL F 1 214 ? 8.383   73.503  -68.656  1.00 28.04 ? 214 VAL F N   1 
ATOM   10025 C CA  . VAL F 1 214 ? 7.272   72.690  -69.130  1.00 28.90 ? 214 VAL F CA  1 
ATOM   10026 C C   . VAL F 1 214 ? 5.950   73.462  -69.085  1.00 30.88 ? 214 VAL F C   1 
ATOM   10027 O O   . VAL F 1 214 ? 5.216   73.484  -70.079  1.00 31.92 ? 214 VAL F O   1 
ATOM   10028 C CB  . VAL F 1 214 ? 7.168   71.373  -68.343  1.00 27.94 ? 214 VAL F CB  1 
ATOM   10029 C CG1 . VAL F 1 214 ? 5.855   70.664  -68.634  1.00 27.30 ? 214 VAL F CG1 1 
ATOM   10030 C CG2 . VAL F 1 214 ? 8.342   70.462  -68.703  1.00 28.15 ? 214 VAL F CG2 1 
ATOM   10031 N N   . LYS F 1 215 ? 5.660   74.103  -67.950  1.00 31.84 ? 215 LYS F N   1 
ATOM   10032 C CA  . LYS F 1 215 ? 4.423   74.888  -67.794  1.00 32.67 ? 215 LYS F CA  1 
ATOM   10033 C C   . LYS F 1 215 ? 4.293   76.004  -68.830  1.00 32.25 ? 215 LYS F C   1 
ATOM   10034 O O   . LYS F 1 215 ? 3.199   76.276  -69.318  1.00 32.79 ? 215 LYS F O   1 
ATOM   10035 C CB  . LYS F 1 215 ? 4.349   75.498  -66.402  1.00 33.69 ? 215 LYS F CB  1 
ATOM   10036 C CG  . LYS F 1 215 ? 4.068   74.493  -65.301  1.00 35.31 ? 215 LYS F CG  1 
ATOM   10037 C CD  . LYS F 1 215 ? 4.157   75.196  -63.951  1.00 35.03 ? 215 LYS F CD  1 
ATOM   10038 C CE  . LYS F 1 215 ? 4.110   74.229  -62.785  1.00 34.27 ? 215 LYS F CE  1 
ATOM   10039 N NZ  . LYS F 1 215 ? 4.408   74.994  -61.545  1.00 32.98 ? 215 LYS F NZ  1 
ATOM   10040 N N   . THR F 1 216 ? 5.403   76.659  -69.144  1.00 32.66 ? 216 THR F N   1 
ATOM   10041 C CA  . THR F 1 216 ? 5.455   77.616  -70.251  1.00 34.08 ? 216 THR F CA  1 
ATOM   10042 C C   . THR F 1 216 ? 4.941   77.021  -71.562  1.00 35.45 ? 216 THR F C   1 
ATOM   10043 O O   . THR F 1 216 ? 4.221   77.691  -72.302  1.00 34.39 ? 216 THR F O   1 
ATOM   10044 C CB  . THR F 1 216 ? 6.893   78.131  -70.458  1.00 35.17 ? 216 THR F CB  1 
ATOM   10045 O OG1 . THR F 1 216 ? 7.257   78.957  -69.347  1.00 35.49 ? 216 THR F OG1 1 
ATOM   10046 C CG2 . THR F 1 216 ? 7.033   78.930  -71.767  1.00 35.34 ? 216 THR F CG2 1 
ATOM   10047 N N   . LEU F 1 217 ? 5.306   75.771  -71.844  1.00 39.06 ? 217 LEU F N   1 
ATOM   10048 C CA  . LEU F 1 217 ? 4.922   75.115  -73.102  1.00 38.01 ? 217 LEU F CA  1 
ATOM   10049 C C   . LEU F 1 217 ? 3.485   74.591  -73.107  1.00 37.26 ? 217 LEU F C   1 
ATOM   10050 O O   . LEU F 1 217 ? 2.808   74.670  -74.117  1.00 37.45 ? 217 LEU F O   1 
ATOM   10051 C CB  . LEU F 1 217 ? 5.870   73.964  -73.416  1.00 38.10 ? 217 LEU F CB  1 
ATOM   10052 C CG  . LEU F 1 217 ? 7.351   74.313  -73.590  1.00 39.64 ? 217 LEU F CG  1 
ATOM   10053 C CD1 . LEU F 1 217 ? 8.166   73.023  -73.678  1.00 40.05 ? 217 LEU F CD1 1 
ATOM   10054 C CD2 . LEU F 1 217 ? 7.601   75.252  -74.768  1.00 39.43 ? 217 LEU F CD2 1 
ATOM   10055 N N   . LEU F 1 218 ? 3.012   74.062  -71.986  1.00 37.87 ? 218 LEU F N   1 
ATOM   10056 C CA  . LEU F 1 218 ? 1.726   73.371  -71.964  1.00 41.55 ? 218 LEU F CA  1 
ATOM   10057 C C   . LEU F 1 218 ? 0.542   74.149  -71.332  1.00 45.41 ? 218 LEU F C   1 
ATOM   10058 O O   . LEU F 1 218 ? -0.620  73.767  -71.558  1.00 45.80 ? 218 LEU F O   1 
ATOM   10059 C CB  . LEU F 1 218 ? 1.895   72.013  -71.265  1.00 41.66 ? 218 LEU F CB  1 
ATOM   10060 C CG  . LEU F 1 218 ? 2.931   71.051  -71.906  1.00 40.82 ? 218 LEU F CG  1 
ATOM   10061 C CD1 . LEU F 1 218 ? 2.991   69.735  -71.132  1.00 40.21 ? 218 LEU F CD1 1 
ATOM   10062 C CD2 . LEU F 1 218 ? 2.676   70.769  -73.391  1.00 39.29 ? 218 LEU F CD2 1 
ATOM   10063 N N   . GLN F 1 219 ? 0.803   75.210  -70.544  1.00 49.39 ? 219 GLN F N   1 
ATOM   10064 C CA  . GLN F 1 219 ? -0.200  75.827  -69.620  1.00 50.46 ? 219 GLN F CA  1 
ATOM   10065 C C   . GLN F 1 219 ? -1.084  74.780  -68.897  1.00 47.84 ? 219 GLN F C   1 
ATOM   10066 O O   . GLN F 1 219 ? -0.828  74.405  -67.744  1.00 41.92 ? 219 GLN F O   1 
ATOM   10067 C CB  . GLN F 1 219 ? -1.067  76.907  -70.335  1.00 51.98 ? 219 GLN F CB  1 
ATOM   10068 C CG  . GLN F 1 219 ? -0.582  78.339  -70.172  1.00 50.50 ? 219 GLN F CG  1 
ATOM   10069 C CD  . GLN F 1 219 ? 0.452   78.742  -71.192  1.00 48.13 ? 219 GLN F CD  1 
ATOM   10070 O OE1 . GLN F 1 219 ? 0.980   77.928  -71.942  1.00 45.62 ? 219 GLN F OE1 1 
ATOM   10071 N NE2 . GLN F 1 219 ? 0.708   80.032  -71.257  1.00 45.91 ? 219 GLN F NE2 1 
# 
